data_5HDH
# 
_entry.id   5HDH 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.279 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   5HDH         
WWPDB D_1000216864 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        5HDH 
_pdbx_database_status.recvd_initial_deposition_date   2016-01-05 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    PDBJ 
_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 
'Tanji, H.'   1 
'Ohto, U.'    2 
'Shimizu, T.' 3 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Proc.Natl.Acad.Sci.USA 
_citation.journal_id_ASTM           PNASA6 
_citation.journal_id_CSD            0040 
_citation.journal_id_ISSN           1091-6490 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            113 
_citation.language                  ? 
_citation.page_first                3012 
_citation.page_last                 3017 
_citation.title                     'Autoinhibition and relief mechanism by the proteolytic processing of Toll-like receptor 8' 
_citation.year                      2016 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1073/pnas.1516000113 
_citation.pdbx_database_id_PubMed   26929371 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Tanji, H.'   1 
primary 'Ohto, U.'    2 
primary 'Motoi, Y.'   3 
primary 'Shibata, T.' 4 
primary 'Miyake, K.'  5 
primary 'Shimizu, T.' 6 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     5HDH 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     171.520 
_cell.length_a_esd                 ? 
_cell.length_b                     171.520 
_cell.length_b_esd                 ? 
_cell.length_c                     301.333 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        18 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
# 
_symmetry.entry_id                         5HDH 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                155 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'H 3 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
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 'Toll-like receptor 8'                 91407.523 1  ? ? 'UNP residues 27-827' ? 
2 non-polymer man N-ACETYL-D-GLUCOSAMINE                 221.208   12 ? ? ?                     ? 
3 non-polymer man BETA-D-MANNOSE                         180.156   2  ? ? ?                     ? 
4 non-polymer man ALPHA-D-MANNOSE                        180.156   3  ? ? ?                     ? 
5 non-polymer syn 'SULFATE ION'                          96.063    3  ? ? ?                     ? 
6 non-polymer syn '2-(N-MORPHOLINO)-ETHANESULFONIC ACID' 195.237   1  ? ? ?                     ? 
7 water       nat water                                  18.015    79 ? ? ?                     ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;EENFSRSYPCDEKKQNDSVIAECSNRRLQEVPQTVGKYVTELDLSDNFITHITNESFQGLQNLTKINLNHNPNVQHQNGN
PGIQSNGLNITDGAFLNLKNLRELLLEDNQLPQIPSGLPESLTELSLIQNNIYNITKEGISRLINLKNLYLAWNCYFNKV
CEKTNIEDGVFETLTNLELLSLSFNSLSHVPPKLPSSLRKLFLSNTQIKYISEEDFKGLINLTLLDLSGNCPRCFNAPFP
CVPCDGGASINIDRFAFQNLTQLRYLNLSSTSLRKINAAWFKNMPHLKVLDLEFNYLVGEIASGAFLTMLPRLEILDLSF
NYIKGSYPQHINISRNFSKLLSLRALHLRGYVFQELREDDFQPLMQLPNLSTINLGINFIKQIDFKLFQNFSNLEIIYLS
ENRISPLVKDTRQSYANSSSFQRHINQSNSTDFEFDPHSNFYHFTRPLIKPQCAAYGKALDLSLNSIFFIGPNQFENLPD
IACLNLSANSNAQVLSGTEFSAIPHVKYLDLTNNRLDFDNASALTELSDLEVLDLSYNSHYFRIAGVTHHLEFIQNFTNL
KVLNLSHNNIYTLTDKYNLESKSLVELVFSGNRLDILWNDDDNRYISIFKGLKNLTRLDLSLNRLKHIPNEAFLNLPASL
TELHINDNMLKFFNWTLLQQFPRLELLDLRGNKLLFLTDSLSDFTSSLRTLLLSHNRISHLPSGFLSEVSSLKHLDLSSN
LLKTINKSALETKTTTKLSMLELHGNPFECTCDIGDFRRWMDEHLNVKIPRLVDVICASPGDQRGKSIVSLELTTCVSDV
T
;
_entity_poly.pdbx_seq_one_letter_code_can   
;EENFSRSYPCDEKKQNDSVIAECSNRRLQEVPQTVGKYVTELDLSDNFITHITNESFQGLQNLTKINLNHNPNVQHQNGN
PGIQSNGLNITDGAFLNLKNLRELLLEDNQLPQIPSGLPESLTELSLIQNNIYNITKEGISRLINLKNLYLAWNCYFNKV
CEKTNIEDGVFETLTNLELLSLSFNSLSHVPPKLPSSLRKLFLSNTQIKYISEEDFKGLINLTLLDLSGNCPRCFNAPFP
CVPCDGGASINIDRFAFQNLTQLRYLNLSSTSLRKINAAWFKNMPHLKVLDLEFNYLVGEIASGAFLTMLPRLEILDLSF
NYIKGSYPQHINISRNFSKLLSLRALHLRGYVFQELREDDFQPLMQLPNLSTINLGINFIKQIDFKLFQNFSNLEIIYLS
ENRISPLVKDTRQSYANSSSFQRHINQSNSTDFEFDPHSNFYHFTRPLIKPQCAAYGKALDLSLNSIFFIGPNQFENLPD
IACLNLSANSNAQVLSGTEFSAIPHVKYLDLTNNRLDFDNASALTELSDLEVLDLSYNSHYFRIAGVTHHLEFIQNFTNL
KVLNLSHNNIYTLTDKYNLESKSLVELVFSGNRLDILWNDDDNRYISIFKGLKNLTRLDLSLNRLKHIPNEAFLNLPASL
TELHINDNMLKFFNWTLLQQFPRLELLDLRGNKLLFLTDSLSDFTSSLRTLLLSHNRISHLPSGFLSEVSSLKHLDLSSN
LLKTINKSALETKTTTKLSMLELHGNPFECTCDIGDFRRWMDEHLNVKIPRLVDVICASPGDQRGKSIVSLELTTCVSDV
T
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLU n 
1 2   GLU n 
1 3   ASN n 
1 4   PHE n 
1 5   SER n 
1 6   ARG n 
1 7   SER n 
1 8   TYR n 
1 9   PRO n 
1 10  CYS n 
1 11  ASP n 
1 12  GLU n 
1 13  LYS n 
1 14  LYS n 
1 15  GLN n 
1 16  ASN n 
1 17  ASP n 
1 18  SER n 
1 19  VAL n 
1 20  ILE n 
1 21  ALA n 
1 22  GLU n 
1 23  CYS n 
1 24  SER n 
1 25  ASN n 
1 26  ARG n 
1 27  ARG n 
1 28  LEU n 
1 29  GLN n 
1 30  GLU n 
1 31  VAL n 
1 32  PRO n 
1 33  GLN n 
1 34  THR n 
1 35  VAL n 
1 36  GLY n 
1 37  LYS n 
1 38  TYR n 
1 39  VAL n 
1 40  THR n 
1 41  GLU n 
1 42  LEU n 
1 43  ASP n 
1 44  LEU n 
1 45  SER n 
1 46  ASP n 
1 47  ASN n 
1 48  PHE n 
1 49  ILE n 
1 50  THR n 
1 51  HIS n 
1 52  ILE n 
1 53  THR n 
1 54  ASN n 
1 55  GLU n 
1 56  SER n 
1 57  PHE n 
1 58  GLN n 
1 59  GLY n 
1 60  LEU n 
1 61  GLN n 
1 62  ASN n 
1 63  LEU n 
1 64  THR n 
1 65  LYS n 
1 66  ILE n 
1 67  ASN n 
1 68  LEU n 
1 69  ASN n 
1 70  HIS n 
1 71  ASN n 
1 72  PRO n 
1 73  ASN n 
1 74  VAL n 
1 75  GLN n 
1 76  HIS n 
1 77  GLN n 
1 78  ASN n 
1 79  GLY n 
1 80  ASN n 
1 81  PRO n 
1 82  GLY n 
1 83  ILE n 
1 84  GLN n 
1 85  SER n 
1 86  ASN n 
1 87  GLY n 
1 88  LEU n 
1 89  ASN n 
1 90  ILE n 
1 91  THR n 
1 92  ASP n 
1 93  GLY n 
1 94  ALA n 
1 95  PHE n 
1 96  LEU n 
1 97  ASN n 
1 98  LEU n 
1 99  LYS n 
1 100 ASN n 
1 101 LEU n 
1 102 ARG n 
1 103 GLU n 
1 104 LEU n 
1 105 LEU n 
1 106 LEU n 
1 107 GLU n 
1 108 ASP n 
1 109 ASN n 
1 110 GLN n 
1 111 LEU n 
1 112 PRO n 
1 113 GLN n 
1 114 ILE n 
1 115 PRO n 
1 116 SER n 
1 117 GLY n 
1 118 LEU n 
1 119 PRO n 
1 120 GLU n 
1 121 SER n 
1 122 LEU n 
1 123 THR n 
1 124 GLU n 
1 125 LEU n 
1 126 SER n 
1 127 LEU n 
1 128 ILE n 
1 129 GLN n 
1 130 ASN n 
1 131 ASN n 
1 132 ILE n 
1 133 TYR n 
1 134 ASN n 
1 135 ILE n 
1 136 THR n 
1 137 LYS n 
1 138 GLU n 
1 139 GLY n 
1 140 ILE n 
1 141 SER n 
1 142 ARG n 
1 143 LEU n 
1 144 ILE n 
1 145 ASN n 
1 146 LEU n 
1 147 LYS n 
1 148 ASN n 
1 149 LEU n 
1 150 TYR n 
1 151 LEU n 
1 152 ALA n 
1 153 TRP n 
1 154 ASN n 
1 155 CYS n 
1 156 TYR n 
1 157 PHE n 
1 158 ASN n 
1 159 LYS n 
1 160 VAL n 
1 161 CYS n 
1 162 GLU n 
1 163 LYS n 
1 164 THR n 
1 165 ASN n 
1 166 ILE n 
1 167 GLU n 
1 168 ASP n 
1 169 GLY n 
1 170 VAL n 
1 171 PHE n 
1 172 GLU n 
1 173 THR n 
1 174 LEU n 
1 175 THR n 
1 176 ASN n 
1 177 LEU n 
1 178 GLU n 
1 179 LEU n 
1 180 LEU n 
1 181 SER n 
1 182 LEU n 
1 183 SER n 
1 184 PHE n 
1 185 ASN n 
1 186 SER n 
1 187 LEU n 
1 188 SER n 
1 189 HIS n 
1 190 VAL n 
1 191 PRO n 
1 192 PRO n 
1 193 LYS n 
1 194 LEU n 
1 195 PRO n 
1 196 SER n 
1 197 SER n 
1 198 LEU n 
1 199 ARG n 
1 200 LYS n 
1 201 LEU n 
1 202 PHE n 
1 203 LEU n 
1 204 SER n 
1 205 ASN n 
1 206 THR n 
1 207 GLN n 
1 208 ILE n 
1 209 LYS n 
1 210 TYR n 
1 211 ILE n 
1 212 SER n 
1 213 GLU n 
1 214 GLU n 
1 215 ASP n 
1 216 PHE n 
1 217 LYS n 
1 218 GLY n 
1 219 LEU n 
1 220 ILE n 
1 221 ASN n 
1 222 LEU n 
1 223 THR n 
1 224 LEU n 
1 225 LEU n 
1 226 ASP n 
1 227 LEU n 
1 228 SER n 
1 229 GLY n 
1 230 ASN n 
1 231 CYS n 
1 232 PRO n 
1 233 ARG n 
1 234 CYS n 
1 235 PHE n 
1 236 ASN n 
1 237 ALA n 
1 238 PRO n 
1 239 PHE n 
1 240 PRO n 
1 241 CYS n 
1 242 VAL n 
1 243 PRO n 
1 244 CYS n 
1 245 ASP n 
1 246 GLY n 
1 247 GLY n 
1 248 ALA n 
1 249 SER n 
1 250 ILE n 
1 251 ASN n 
1 252 ILE n 
1 253 ASP n 
1 254 ARG n 
1 255 PHE n 
1 256 ALA n 
1 257 PHE n 
1 258 GLN n 
1 259 ASN n 
1 260 LEU n 
1 261 THR n 
1 262 GLN n 
1 263 LEU n 
1 264 ARG n 
1 265 TYR n 
1 266 LEU n 
1 267 ASN n 
1 268 LEU n 
1 269 SER n 
1 270 SER n 
1 271 THR n 
1 272 SER n 
1 273 LEU n 
1 274 ARG n 
1 275 LYS n 
1 276 ILE n 
1 277 ASN n 
1 278 ALA n 
1 279 ALA n 
1 280 TRP n 
1 281 PHE n 
1 282 LYS n 
1 283 ASN n 
1 284 MET n 
1 285 PRO n 
1 286 HIS n 
1 287 LEU n 
1 288 LYS n 
1 289 VAL n 
1 290 LEU n 
1 291 ASP n 
1 292 LEU n 
1 293 GLU n 
1 294 PHE n 
1 295 ASN n 
1 296 TYR n 
1 297 LEU n 
1 298 VAL n 
1 299 GLY n 
1 300 GLU n 
1 301 ILE n 
1 302 ALA n 
1 303 SER n 
1 304 GLY n 
1 305 ALA n 
1 306 PHE n 
1 307 LEU n 
1 308 THR n 
1 309 MET n 
1 310 LEU n 
1 311 PRO n 
1 312 ARG n 
1 313 LEU n 
1 314 GLU n 
1 315 ILE n 
1 316 LEU n 
1 317 ASP n 
1 318 LEU n 
1 319 SER n 
1 320 PHE n 
1 321 ASN n 
1 322 TYR n 
1 323 ILE n 
1 324 LYS n 
1 325 GLY n 
1 326 SER n 
1 327 TYR n 
1 328 PRO n 
1 329 GLN n 
1 330 HIS n 
1 331 ILE n 
1 332 ASN n 
1 333 ILE n 
1 334 SER n 
1 335 ARG n 
1 336 ASN n 
1 337 PHE n 
1 338 SER n 
1 339 LYS n 
1 340 LEU n 
1 341 LEU n 
1 342 SER n 
1 343 LEU n 
1 344 ARG n 
1 345 ALA n 
1 346 LEU n 
1 347 HIS n 
1 348 LEU n 
1 349 ARG n 
1 350 GLY n 
1 351 TYR n 
1 352 VAL n 
1 353 PHE n 
1 354 GLN n 
1 355 GLU n 
1 356 LEU n 
1 357 ARG n 
1 358 GLU n 
1 359 ASP n 
1 360 ASP n 
1 361 PHE n 
1 362 GLN n 
1 363 PRO n 
1 364 LEU n 
1 365 MET n 
1 366 GLN n 
1 367 LEU n 
1 368 PRO n 
1 369 ASN n 
1 370 LEU n 
1 371 SER n 
1 372 THR n 
1 373 ILE n 
1 374 ASN n 
1 375 LEU n 
1 376 GLY n 
1 377 ILE n 
1 378 ASN n 
1 379 PHE n 
1 380 ILE n 
1 381 LYS n 
1 382 GLN n 
1 383 ILE n 
1 384 ASP n 
1 385 PHE n 
1 386 LYS n 
1 387 LEU n 
1 388 PHE n 
1 389 GLN n 
1 390 ASN n 
1 391 PHE n 
1 392 SER n 
1 393 ASN n 
1 394 LEU n 
1 395 GLU n 
1 396 ILE n 
1 397 ILE n 
1 398 TYR n 
1 399 LEU n 
1 400 SER n 
1 401 GLU n 
1 402 ASN n 
1 403 ARG n 
1 404 ILE n 
1 405 SER n 
1 406 PRO n 
1 407 LEU n 
1 408 VAL n 
1 409 LYS n 
1 410 ASP n 
1 411 THR n 
1 412 ARG n 
1 413 GLN n 
1 414 SER n 
1 415 TYR n 
1 416 ALA n 
1 417 ASN n 
1 418 SER n 
1 419 SER n 
1 420 SER n 
1 421 PHE n 
1 422 GLN n 
1 423 ARG n 
1 424 HIS n 
1 425 ILE n 
1 426 ASN n 
1 427 GLN n 
1 428 SER n 
1 429 ASN n 
1 430 SER n 
1 431 THR n 
1 432 ASP n 
1 433 PHE n 
1 434 GLU n 
1 435 PHE n 
1 436 ASP n 
1 437 PRO n 
1 438 HIS n 
1 439 SER n 
1 440 ASN n 
1 441 PHE n 
1 442 TYR n 
1 443 HIS n 
1 444 PHE n 
1 445 THR n 
1 446 ARG n 
1 447 PRO n 
1 448 LEU n 
1 449 ILE n 
1 450 LYS n 
1 451 PRO n 
1 452 GLN n 
1 453 CYS n 
1 454 ALA n 
1 455 ALA n 
1 456 TYR n 
1 457 GLY n 
1 458 LYS n 
1 459 ALA n 
1 460 LEU n 
1 461 ASP n 
1 462 LEU n 
1 463 SER n 
1 464 LEU n 
1 465 ASN n 
1 466 SER n 
1 467 ILE n 
1 468 PHE n 
1 469 PHE n 
1 470 ILE n 
1 471 GLY n 
1 472 PRO n 
1 473 ASN n 
1 474 GLN n 
1 475 PHE n 
1 476 GLU n 
1 477 ASN n 
1 478 LEU n 
1 479 PRO n 
1 480 ASP n 
1 481 ILE n 
1 482 ALA n 
1 483 CYS n 
1 484 LEU n 
1 485 ASN n 
1 486 LEU n 
1 487 SER n 
1 488 ALA n 
1 489 ASN n 
1 490 SER n 
1 491 ASN n 
1 492 ALA n 
1 493 GLN n 
1 494 VAL n 
1 495 LEU n 
1 496 SER n 
1 497 GLY n 
1 498 THR n 
1 499 GLU n 
1 500 PHE n 
1 501 SER n 
1 502 ALA n 
1 503 ILE n 
1 504 PRO n 
1 505 HIS n 
1 506 VAL n 
1 507 LYS n 
1 508 TYR n 
1 509 LEU n 
1 510 ASP n 
1 511 LEU n 
1 512 THR n 
1 513 ASN n 
1 514 ASN n 
1 515 ARG n 
1 516 LEU n 
1 517 ASP n 
1 518 PHE n 
1 519 ASP n 
1 520 ASN n 
1 521 ALA n 
1 522 SER n 
1 523 ALA n 
1 524 LEU n 
1 525 THR n 
1 526 GLU n 
1 527 LEU n 
1 528 SER n 
1 529 ASP n 
1 530 LEU n 
1 531 GLU n 
1 532 VAL n 
1 533 LEU n 
1 534 ASP n 
1 535 LEU n 
1 536 SER n 
1 537 TYR n 
1 538 ASN n 
1 539 SER n 
1 540 HIS n 
1 541 TYR n 
1 542 PHE n 
1 543 ARG n 
1 544 ILE n 
1 545 ALA n 
1 546 GLY n 
1 547 VAL n 
1 548 THR n 
1 549 HIS n 
1 550 HIS n 
1 551 LEU n 
1 552 GLU n 
1 553 PHE n 
1 554 ILE n 
1 555 GLN n 
1 556 ASN n 
1 557 PHE n 
1 558 THR n 
1 559 ASN n 
1 560 LEU n 
1 561 LYS n 
1 562 VAL n 
1 563 LEU n 
1 564 ASN n 
1 565 LEU n 
1 566 SER n 
1 567 HIS n 
1 568 ASN n 
1 569 ASN n 
1 570 ILE n 
1 571 TYR n 
1 572 THR n 
1 573 LEU n 
1 574 THR n 
1 575 ASP n 
1 576 LYS n 
1 577 TYR n 
1 578 ASN n 
1 579 LEU n 
1 580 GLU n 
1 581 SER n 
1 582 LYS n 
1 583 SER n 
1 584 LEU n 
1 585 VAL n 
1 586 GLU n 
1 587 LEU n 
1 588 VAL n 
1 589 PHE n 
1 590 SER n 
1 591 GLY n 
1 592 ASN n 
1 593 ARG n 
1 594 LEU n 
1 595 ASP n 
1 596 ILE n 
1 597 LEU n 
1 598 TRP n 
1 599 ASN n 
1 600 ASP n 
1 601 ASP n 
1 602 ASP n 
1 603 ASN n 
1 604 ARG n 
1 605 TYR n 
1 606 ILE n 
1 607 SER n 
1 608 ILE n 
1 609 PHE n 
1 610 LYS n 
1 611 GLY n 
1 612 LEU n 
1 613 LYS n 
1 614 ASN n 
1 615 LEU n 
1 616 THR n 
1 617 ARG n 
1 618 LEU n 
1 619 ASP n 
1 620 LEU n 
1 621 SER n 
1 622 LEU n 
1 623 ASN n 
1 624 ARG n 
1 625 LEU n 
1 626 LYS n 
1 627 HIS n 
1 628 ILE n 
1 629 PRO n 
1 630 ASN n 
1 631 GLU n 
1 632 ALA n 
1 633 PHE n 
1 634 LEU n 
1 635 ASN n 
1 636 LEU n 
1 637 PRO n 
1 638 ALA n 
1 639 SER n 
1 640 LEU n 
1 641 THR n 
1 642 GLU n 
1 643 LEU n 
1 644 HIS n 
1 645 ILE n 
1 646 ASN n 
1 647 ASP n 
1 648 ASN n 
1 649 MET n 
1 650 LEU n 
1 651 LYS n 
1 652 PHE n 
1 653 PHE n 
1 654 ASN n 
1 655 TRP n 
1 656 THR n 
1 657 LEU n 
1 658 LEU n 
1 659 GLN n 
1 660 GLN n 
1 661 PHE n 
1 662 PRO n 
1 663 ARG n 
1 664 LEU n 
1 665 GLU n 
1 666 LEU n 
1 667 LEU n 
1 668 ASP n 
1 669 LEU n 
1 670 ARG n 
1 671 GLY n 
1 672 ASN n 
1 673 LYS n 
1 674 LEU n 
1 675 LEU n 
1 676 PHE n 
1 677 LEU n 
1 678 THR n 
1 679 ASP n 
1 680 SER n 
1 681 LEU n 
1 682 SER n 
1 683 ASP n 
1 684 PHE n 
1 685 THR n 
1 686 SER n 
1 687 SER n 
1 688 LEU n 
1 689 ARG n 
1 690 THR n 
1 691 LEU n 
1 692 LEU n 
1 693 LEU n 
1 694 SER n 
1 695 HIS n 
1 696 ASN n 
1 697 ARG n 
1 698 ILE n 
1 699 SER n 
1 700 HIS n 
1 701 LEU n 
1 702 PRO n 
1 703 SER n 
1 704 GLY n 
1 705 PHE n 
1 706 LEU n 
1 707 SER n 
1 708 GLU n 
1 709 VAL n 
1 710 SER n 
1 711 SER n 
1 712 LEU n 
1 713 LYS n 
1 714 HIS n 
1 715 LEU n 
1 716 ASP n 
1 717 LEU n 
1 718 SER n 
1 719 SER n 
1 720 ASN n 
1 721 LEU n 
1 722 LEU n 
1 723 LYS n 
1 724 THR n 
1 725 ILE n 
1 726 ASN n 
1 727 LYS n 
1 728 SER n 
1 729 ALA n 
1 730 LEU n 
1 731 GLU n 
1 732 THR n 
1 733 LYS n 
1 734 THR n 
1 735 THR n 
1 736 THR n 
1 737 LYS n 
1 738 LEU n 
1 739 SER n 
1 740 MET n 
1 741 LEU n 
1 742 GLU n 
1 743 LEU n 
1 744 HIS n 
1 745 GLY n 
1 746 ASN n 
1 747 PRO n 
1 748 PHE n 
1 749 GLU n 
1 750 CYS n 
1 751 THR n 
1 752 CYS n 
1 753 ASP n 
1 754 ILE n 
1 755 GLY n 
1 756 ASP n 
1 757 PHE n 
1 758 ARG n 
1 759 ARG n 
1 760 TRP n 
1 761 MET n 
1 762 ASP n 
1 763 GLU n 
1 764 HIS n 
1 765 LEU n 
1 766 ASN n 
1 767 VAL n 
1 768 LYS n 
1 769 ILE n 
1 770 PRO n 
1 771 ARG n 
1 772 LEU n 
1 773 VAL n 
1 774 ASP n 
1 775 VAL n 
1 776 ILE n 
1 777 CYS n 
1 778 ALA n 
1 779 SER n 
1 780 PRO n 
1 781 GLY n 
1 782 ASP n 
1 783 GLN n 
1 784 ARG n 
1 785 GLY n 
1 786 LYS n 
1 787 SER n 
1 788 ILE n 
1 789 VAL n 
1 790 SER n 
1 791 LEU n 
1 792 GLU n 
1 793 LEU n 
1 794 THR n 
1 795 THR n 
1 796 CYS n 
1 797 VAL n 
1 798 SER n 
1 799 ASP n 
1 800 VAL n 
1 801 THR n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   801 
_entity_src_gen.gene_src_common_name               Human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'TLR8, UNQ249/PRO286' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      Drosophila 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     7215 
_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                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    TLR8_HUMAN 
_struct_ref.pdbx_db_accession          Q9NR97 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;EENFSRSYPCDEKKQNDSVIAECSNRRLQEVPQTVGKYVTELDLSDNFITHITNESFQGLQNLTKINLNHNPNVQHQNGN
PGIQSNGLNITDGAFLNLKNLRELLLEDNQLPQIPSGLPESLTELSLIQNNIYNITKEGISRLINLKNLYLAWNCYFNKV
CEKTNIEDGVFETLTNLELLSLSFNSLSHVPPKLPSSLRKLFLSNTQIKYISEEDFKGLINLTLLDLSGNCPRCFNAPFP
CVPCDGGASINIDRFAFQNLTQLRYLNLSSTSLRKINAAWFKNMPHLKVLDLEFNYLVGEIASGAFLTMLPRLEILDLSF
NYIKGSYPQHINISRNFSKLLSLRALHLRGYVFQELREDDFQPLMQLPNLSTINLGINFIKQIDFKLFQNFSNLEIIYLS
ENRISPLVKDTRQSYANSSSFQRHIRKRRSTDFEFDPHSNFYHFTRPLIKPQCAAYGKALDLSLNSIFFIGPNQFENLPD
IACLNLSANSNAQVLSGTEFSAIPHVKYLDLTNNRLDFDNASALTELSDLEVLDLSYNSHYFRIAGVTHHLEFIQNFTNL
KVLNLSHNNIYTLTDKYNLESKSLVELVFSGNRLDILWNDDDNRYISIFKGLKNLTRLDLSLNRLKHIPNEAFLNLPASL
TELHINDNMLKFFNWTLLQQFPRLELLDLRGNKLLFLTDSLSDFTSSLRTLLLSHNRISHLPSGFLSEVSSLKHLDLSSN
LLKTINKSALETKTTTKLSMLELHGNPFECTCDIGDFRRWMDEHLNVKIPRLVDVICASPGDQRGKSIVSLELTTCVSDV
T
;
_struct_ref.pdbx_align_begin           27 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              5HDH 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 801 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q9NR97 
_struct_ref_seq.db_align_beg                  27 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  827 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       27 
_struct_ref_seq.pdbx_auth_seq_align_end       827 
# 
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 5HDH ASN A 426 ? UNP Q9NR97 ARG 452 'engineered mutation' 452 1 
1 5HDH GLN A 427 ? UNP Q9NR97 LYS 453 'engineered mutation' 453 2 
1 5HDH SER A 428 ? UNP Q9NR97 ARG 454 'engineered mutation' 454 3 
1 5HDH ASN A 429 ? UNP Q9NR97 ARG 455 'engineered mutation' 455 4 
# 
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 
GLN 'L-peptide linking' y GLUTAMINE                              ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                        ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                                ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE                              ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                                  ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE                             ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                                ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                                 ? 'C6 H15 N2 O2 1' 147.195 
MAN D-saccharide        . ALPHA-D-MANNOSE                        ? 'C6 H12 O6'      180.156 
MES non-polymer         . '2-(N-MORPHOLINO)-ETHANESULFONIC ACID' ? 'C6 H13 N O4 S'  195.237 
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 
SO4 non-polymer         . 'SULFATE ION'                          ? 'O4 S -2'        96.063  
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.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   5HDH 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                      ? 
_exptl_crystal.density_diffrn              ? 
_exptl_crystal.density_Matthews            4.67 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         73.64 
_exptl_crystal.description                 ? 
_exptl_crystal.F_000                       ? 
_exptl_crystal.id                          1 
_exptl_crystal.preparation                 ? 
_exptl_crystal.size_max                    ? 
_exptl_crystal.size_mid                    ? 
_exptl_crystal.size_min                    ? 
_exptl_crystal.size_rad                    ? 
_exptl_crystal.colour_lustre               ? 
_exptl_crystal.colour_modifier             ? 
_exptl_crystal.colour_primary              ? 
_exptl_crystal.density_meas                ? 
_exptl_crystal.density_meas_esd            ? 
_exptl_crystal.density_meas_gt             ? 
_exptl_crystal.density_meas_lt             ? 
_exptl_crystal.density_meas_temp           ? 
_exptl_crystal.density_meas_temp_esd       ? 
_exptl_crystal.density_meas_temp_gt        ? 
_exptl_crystal.density_meas_temp_lt        ? 
_exptl_crystal.pdbx_crystal_image_url      ? 
_exptl_crystal.pdbx_crystal_image_format   ? 
_exptl_crystal.pdbx_mosaicity              ? 
_exptl_crystal.pdbx_mosaicity_esd          ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            293 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    'ammonium sulfate, sodium acetate, glycerol' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.ambient_environment    ? 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.ambient_temp_esd       ? 
_diffrn.crystal_id             1 
_diffrn.crystal_support        ? 
_diffrn.crystal_treatment      ? 
_diffrn.details                ? 
_diffrn.id                     1 
_diffrn.ambient_pressure       ? 
_diffrn.ambient_pressure_esd   ? 
_diffrn.ambient_pressure_gt    ? 
_diffrn.ambient_pressure_lt    ? 
_diffrn.ambient_temp_gt        ? 
_diffrn.ambient_temp_lt        ? 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'ADSC QUANTUM 270' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2013-06-01 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.0000 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'PHOTON FACTORY BEAMLINE AR-NE3A' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.0000 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   AR-NE3A 
_diffrn_source.pdbx_synchrotron_site       'Photon Factory' 
# 
_reflns.B_iso_Wilson_estimate            ? 
_reflns.entry_id                         5HDH 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                2.60 
_reflns.d_resolution_low                 45.02 
_reflns.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.number_all                       ? 
_reflns.number_obs                       49967 
_reflns.observed_criterion               ? 
_reflns.observed_criterion_F_max         ? 
_reflns.observed_criterion_F_min         ? 
_reflns.observed_criterion_I_max         ? 
_reflns.observed_criterion_I_min         ? 
_reflns.observed_criterion_sigma_F       ? 
_reflns.observed_criterion_sigma_I       ? 
_reflns.percent_possible_obs             100.0 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  19.5 
_reflns.pdbx_Rmerge_I_obs                ? 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  ? 
_reflns.pdbx_netI_over_av_sigmaI         ? 
_reflns.pdbx_netI_over_sigmaI            17.3 
_reflns.pdbx_res_netI_over_av_sigmaI_2   ? 
_reflns.pdbx_res_netI_over_sigmaI_2      ? 
_reflns.pdbx_chi_squared                 ? 
_reflns.pdbx_scaling_rejects             ? 
_reflns.pdbx_d_res_high_opt              ? 
_reflns.pdbx_d_res_low_opt               ? 
_reflns.pdbx_d_res_opt_method            ? 
_reflns.phase_calculation_details        ? 
_reflns.pdbx_Rrim_I_all                  ? 
_reflns.pdbx_Rpim_I_all                  ? 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         ? 
_reflns.pdbx_diffrn_id                   1 
_reflns.pdbx_ordinal                     1 
_reflns.pdbx_CC_half                     ? 
_reflns.pdbx_R_split                     ? 
# 
_refine.aniso_B[1][1]                            0.01 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][2]                            0.01 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -0.02 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               80.137 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.950 
_refine.correlation_coeff_Fo_to_Fc_free          0.936 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 5HDH 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.60 
_refine.ls_d_res_low                             45.02 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     49947 
_refine.ls_number_reflns_R_free                  2610 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.96 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.20756 
_refine.ls_R_factor_R_free                       0.23944 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.20589 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.278 
_refine.pdbx_overall_ESU_R_Free                  0.226 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             8.721 
_refine.overall_SU_ML                            0.183 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.pdbx_number_atoms_protein        6042 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         250 
_refine_hist.number_atoms_solvent             79 
_refine_hist.number_atoms_total               6371 
_refine_hist.d_res_high                       2.60 
_refine_hist.d_res_low                        45.02 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.012  0.019  6435  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.020  6119  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.770  2.012  8744  ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.832  3.000  14019 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 1.957  5.000  745   ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 27.044 24.883 299   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 10.858 15.000 1094  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 9.719  15.000 31    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.123  0.200  1045  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.013  0.020  7033  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.020  1462  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 7.607  7.701  2998  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 7.602  7.700  2997  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 10.530 11.517 3737  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 10.529 11.520 3738  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 8.460  8.386  3437  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 8.458  8.386  3437  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 12.428 12.312 5008  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 16.047 63.321 7338  ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 16.051 63.322 7332  ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.600 
_refine_ls_shell.d_res_low                        2.668 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             191 
_refine_ls_shell.number_reflns_R_work             3676 
_refine_ls_shell.percent_reflns_obs               100.00 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free                  0.346 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.323 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
# 
_struct.entry_id                     5HDH 
_struct.title                        'Crystal structure of human TLR8 with an uncleaved Z-loop' 
_struct.pdbx_descriptor              'Toll-like receptor 8' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               ? 
# 
_struct_keywords.entry_id        5HDH 
_struct_keywords.text            'IMMUNE SYSTEM, TLR8, innate immunity, proteolytic cleavage' 
_struct_keywords.pdbx_keywords   'IMMUNE SYSTEM' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 4 ? 
G N N 2 ? 
H N N 2 ? 
I N N 2 ? 
J N N 2 ? 
K N N 2 ? 
L N N 2 ? 
M N N 2 ? 
N N N 2 ? 
O N N 3 ? 
P N N 4 ? 
Q N N 4 ? 
R N N 2 ? 
S N N 5 ? 
T N N 5 ? 
U N N 5 ? 
V N N 6 ? 
W N N 7 ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 CYS A 244 ? ALA A 248 ? CYS A 270 ALA A 274 5 ? 5  
HELX_P HELX_P2  AA2 ASN A 277 ? LYS A 282 ? ASN A 303 LYS A 308 5 ? 6  
HELX_P HELX_P3  AA3 LEU A 297 ? GLY A 304 ? LEU A 323 GLY A 330 1 ? 8  
HELX_P HELX_P4  AA4 ALA A 305 ? LEU A 310 ? ALA A 331 LEU A 336 5 ? 6  
HELX_P HELX_P5  AA5 SER A 334 ? LEU A 340 ? SER A 360 LEU A 366 5 ? 7  
HELX_P HELX_P6  AA6 ARG A 357 ? MET A 365 ? ARG A 383 MET A 391 5 ? 9  
HELX_P HELX_P7  AA7 PHE A 385 ? PHE A 391 ? PHE A 411 PHE A 417 5 ? 7  
HELX_P HELX_P8  AA8 LYS A 450 ? ALA A 455 ? LYS A 476 ALA A 481 1 ? 6  
HELX_P HELX_P9  AA9 SER A 539 ? ILE A 544 ? SER A 565 ILE A 570 1 ? 6  
HELX_P HELX_P10 AB1 LEU A 551 ? PHE A 557 ? LEU A 577 PHE A 583 5 ? 7  
HELX_P HELX_P11 AB2 ARG A 593 ? ASP A 600 ? ARG A 619 ASP A 626 1 ? 8  
HELX_P HELX_P12 AB3 PRO A 629 ? ASN A 635 ? PRO A 655 ASN A 661 1 ? 7  
HELX_P HELX_P13 AB4 ASN A 654 ? PHE A 661 ? ASN A 680 PHE A 687 5 ? 8  
HELX_P HELX_P14 AB5 SER A 680 ? PHE A 684 ? SER A 706 PHE A 710 5 ? 5  
HELX_P HELX_P15 AB6 THR A 751 ? ASP A 753 ? THR A 777 ASP A 779 5 ? 3  
HELX_P HELX_P16 AB7 ILE A 754 ? HIS A 764 ? ILE A 780 HIS A 790 1 ? 11 
HELX_P HELX_P17 AB8 GLU A 792 ? VAL A 797 ? GLU A 818 VAL A 823 5 ? 6  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
disulf1  disulf ?    ? A CYS 10  SG  ? ? ? 1_555 A CYS 23  SG ? ? A CYS 36  A CYS 49  1_555 ? ? ? ? ? ? ? 2.033 ? 
disulf2  disulf ?    ? A CYS 155 SG  ? ? ? 1_555 A CYS 161 SG ? ? A CYS 181 A CYS 187 1_555 ? ? ? ? ? ? ? 2.030 ? 
disulf3  disulf ?    ? A CYS 231 SG  ? ? ? 1_555 A CYS 244 SG ? ? A CYS 257 A CYS 270 1_555 ? ? ? ? ? ? ? 2.078 ? 
disulf4  disulf ?    ? A CYS 234 SG  ? ? ? 1_555 A CYS 241 SG ? ? A CYS 260 A CYS 267 1_555 ? ? ? ? ? ? ? 2.052 ? 
disulf5  disulf ?    ? A CYS 453 SG  ? ? ? 1_555 A CYS 483 SG ? ? A CYS 479 A CYS 509 1_555 ? ? ? ? ? ? ? 2.031 ? 
disulf6  disulf ?    ? A CYS 750 SG  ? ? ? 1_555 A CYS 777 SG ? ? A CYS 776 A CYS 803 1_555 ? ? ? ? ? ? ? 2.035 ? 
disulf7  disulf ?    ? A CYS 752 SG  ? ? ? 1_555 A CYS 796 SG ? ? A CYS 778 A CYS 822 1_555 ? ? ? ? ? ? ? 2.040 ? 
covale1  covale one  ? A ASN 259 ND2 ? ? ? 1_555 B NAG .   C1 ? ? A ASN 285 A NAG 901 1_555 ? ? ? ? ? ? ? 1.300 ? 
covale2  covale one  ? A ASN 267 ND2 ? ? ? 1_555 C NAG .   C1 ? ? A ASN 293 A NAG 902 1_555 ? ? ? ? ? ? ? 1.446 ? 
covale3  covale one  ? A ASN 369 ND2 ? ? ? 1_555 G NAG .   C1 ? ? A ASN 395 A NAG 906 1_555 ? ? ? ? ? ? ? 1.446 ? 
covale4  covale one  ? A ASN 390 ND2 ? ? ? 1_555 H NAG .   C1 ? ? A ASN 416 A NAG 907 1_555 ? ? ? ? ? ? ? 1.438 ? 
covale5  covale one  ? A ASN 485 ND2 ? ? ? 1_555 I NAG .   C1 ? ? A ASN 511 A NAG 908 1_555 ? ? ? ? ? ? ? 1.429 ? 
covale6  covale one  ? A ASN 520 ND2 ? ? ? 1_555 K NAG .   C1 ? ? A ASN 546 A NAG 910 1_555 ? ? ? ? ? ? ? 1.428 ? 
covale7  covale one  ? A ASN 556 ND2 ? ? ? 1_555 L NAG .   C1 ? ? A ASN 582 A NAG 911 1_555 ? ? ? ? ? ? ? 1.434 ? 
covale8  covale one  ? A ASN 564 ND2 ? ? ? 1_555 M NAG .   C1 ? ? A ASN 590 A NAG 912 1_555 ? ? ? ? ? ? ? 1.448 ? 
covale9  covale one  ? A ASN 614 ND2 ? ? ? 1_555 R NAG .   C1 ? ? A ASN 640 A NAG 917 1_555 ? ? ? ? ? ? ? 1.430 ? 
covale10 covale both ? C NAG .   O4  ? ? ? 1_555 D NAG .   C1 ? ? A NAG 902 A NAG 903 1_555 ? ? ? ? ? ? ? 1.431 ? 
covale11 covale both ? D NAG .   O4  ? ? ? 1_555 E BMA .   C1 ? ? A NAG 903 A BMA 904 1_555 ? ? ? ? ? ? ? 1.431 ? 
covale12 covale one  ? E BMA .   O6  ? ? ? 1_555 F MAN .   C1 ? ? A BMA 904 A MAN 905 1_555 ? ? ? ? ? ? ? 1.444 ? 
covale13 covale both ? I NAG .   O4  ? ? ? 1_555 J NAG .   C1 ? ? A NAG 908 A NAG 909 1_555 ? ? ? ? ? ? ? 1.439 ? 
covale14 covale both ? M NAG .   O4  ? ? ? 1_555 N NAG .   C1 ? ? A NAG 912 A NAG 913 1_555 ? ? ? ? ? ? ? 1.442 ? 
covale15 covale both ? N NAG .   O4  ? ? ? 1_555 O BMA .   C1 ? ? A NAG 913 A BMA 914 1_555 ? ? ? ? ? ? ? 1.449 ? 
covale16 covale one  ? O BMA .   O3  ? ? ? 1_555 Q MAN .   C1 ? ? A BMA 914 A MAN 916 1_555 ? ? ? ? ? ? ? 1.443 ? 
covale17 covale one  ? O BMA .   O6  ? ? ? 1_555 P MAN .   C1 ? ? A BMA 914 A MAN 915 1_555 ? ? ? ? ? ? ? 1.464 ? 
# 
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  TYR 8   A . ? TYR 34  A PRO 9   A ? PRO 35  A 1 -1.27 
2  GLN 15  A . ? GLN 41  A ASN 16  A ? ASN 42  A 1 -2.96 
3  ASN 71  A . ? ASN 97  A PRO 72  A ? PRO 98  A 1 0.09  
4  PHE 157 A . ? PHE 183 A ASN 158 A ? ASN 184 A 1 0.25  
5  LYS 159 A . ? LYS 185 A VAL 160 A ? VAL 186 A 1 -0.33 
6  PHE 239 A . ? PHE 265 A PRO 240 A ? PRO 266 A 1 2.89  
7  PRO 437 A . ? PRO 463 A HIS 438 A ? HIS 464 A 1 -1.30 
8  GLY 704 A . ? GLY 730 A PHE 705 A ? PHE 731 A 1 0.99  
9  PHE 705 A . ? PHE 731 A LEU 706 A ? LEU 732 A 1 -0.29 
10 SER 779 A . ? SER 805 A PRO 780 A ? PRO 806 A 1 0.48  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 28 ? 
AA2 ? 2  ? 
AA3 ? 2  ? 
AA4 ? 2  ? 
AA5 ? 2  ? 
AA6 ? 2  ? 
AA7 ? 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 
AA1 1  2  ? anti-parallel 
AA1 2  3  ? parallel      
AA1 3  4  ? parallel      
AA1 4  5  ? parallel      
AA1 5  6  ? parallel      
AA1 6  7  ? parallel      
AA1 7  8  ? parallel      
AA1 8  9  ? parallel      
AA1 9  10 ? parallel      
AA1 10 11 ? parallel      
AA1 11 12 ? parallel      
AA1 12 13 ? parallel      
AA1 13 14 ? parallel      
AA1 14 15 ? parallel      
AA1 15 16 ? parallel      
AA1 16 17 ? parallel      
AA1 17 18 ? parallel      
AA1 18 19 ? parallel      
AA1 19 20 ? parallel      
AA1 20 21 ? parallel      
AA1 21 22 ? parallel      
AA1 22 23 ? parallel      
AA1 23 24 ? parallel      
AA1 24 25 ? parallel      
AA1 25 26 ? parallel      
AA1 26 27 ? parallel      
AA1 27 28 ? parallel      
AA2 1  2  ? parallel      
AA3 1  2  ? parallel      
AA4 1  2  ? parallel      
AA5 1  2  ? parallel      
AA6 1  2  ? parallel      
AA7 1  2  ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  ASP A 11  ? LYS A 14  ? ASP A 37  LYS A 40  
AA1 2  VAL A 19  ? GLU A 22  ? VAL A 45  GLU A 48  
AA1 3  GLU A 41  ? ASP A 43  ? GLU A 67  ASP A 69  
AA1 4  LYS A 65  ? ASN A 67  ? LYS A 91  ASN A 93  
AA1 5  GLU A 103 ? LEU A 105 ? GLU A 129 LEU A 131 
AA1 6  GLU A 124 ? SER A 126 ? GLU A 150 SER A 152 
AA1 7  ASN A 148 ? TYR A 150 ? ASN A 174 TYR A 176 
AA1 8  LEU A 179 ? SER A 181 ? LEU A 205 SER A 207 
AA1 9  LYS A 200 ? PHE A 202 ? LYS A 226 PHE A 228 
AA1 10 LEU A 224 ? ASP A 226 ? LEU A 250 ASP A 252 
AA1 11 TYR A 265 ? ASN A 267 ? TYR A 291 ASN A 293 
AA1 12 VAL A 289 ? ASP A 291 ? VAL A 315 ASP A 317 
AA1 13 ILE A 315 ? ASP A 317 ? ILE A 341 ASP A 343 
AA1 14 ALA A 345 ? HIS A 347 ? ALA A 371 HIS A 373 
AA1 15 THR A 372 ? ASN A 374 ? THR A 398 ASN A 400 
AA1 16 ILE A 396 ? TYR A 398 ? ILE A 422 TYR A 424 
AA1 17 ALA A 459 ? ASP A 461 ? ALA A 485 ASP A 487 
AA1 18 CYS A 483 ? ASN A 485 ? CYS A 509 ASN A 511 
AA1 19 TYR A 508 ? ASP A 510 ? TYR A 534 ASP A 536 
AA1 20 VAL A 532 ? ASP A 534 ? VAL A 558 ASP A 560 
AA1 21 VAL A 562 ? ASN A 564 ? VAL A 588 ASN A 590 
AA1 22 GLU A 586 ? VAL A 588 ? GLU A 612 VAL A 614 
AA1 23 ARG A 617 ? ASP A 619 ? ARG A 643 ASP A 645 
AA1 24 GLU A 642 ? HIS A 644 ? GLU A 668 HIS A 670 
AA1 25 LEU A 666 ? ASP A 668 ? LEU A 692 ASP A 694 
AA1 26 THR A 690 ? LEU A 692 ? THR A 716 LEU A 718 
AA1 27 HIS A 714 ? ASP A 716 ? HIS A 740 ASP A 742 
AA1 28 MET A 740 ? GLU A 742 ? MET A 766 GLU A 768 
AA2 1  HIS A 51  ? ILE A 52  ? HIS A 77  ILE A 78  
AA2 2  ASN A 89  ? ILE A 90  ? ASN A 115 ILE A 116 
AA3 1  ASN A 134 ? ILE A 135 ? ASN A 160 ILE A 161 
AA3 2  ASN A 165 ? ILE A 166 ? ASN A 191 ILE A 192 
AA4 1  TYR A 210 ? ILE A 211 ? TYR A 236 ILE A 237 
AA4 2  ASN A 251 ? ILE A 252 ? ASN A 277 ILE A 278 
AA5 1  GLU A 355 ? LEU A 356 ? GLU A 381 LEU A 382 
AA5 2  GLN A 382 ? ILE A 383 ? GLN A 408 ILE A 409 
AA6 1  GLU A 580 ? SER A 581 ? GLU A 606 SER A 607 
AA6 2  GLY A 611 ? LEU A 612 ? GLY A 637 LEU A 638 
AA7 1  PHE A 748 ? GLU A 749 ? PHE A 774 GLU A 775 
AA7 2  CYS A 777 ? SER A 779 ? CYS A 803 SER A 805 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1  2  N ASP A 11  ? N ASP A 37  O GLU A 22  ? O GLU A 48  
AA1 2  3  N ALA A 21  ? N ALA A 47  O ASP A 43  ? O ASP A 69  
AA1 3  4  N LEU A 42  ? N LEU A 68  O LYS A 65  ? O LYS A 91  
AA1 4  5  N ILE A 66  ? N ILE A 92  O LEU A 105 ? O LEU A 131 
AA1 5  6  N LEU A 104 ? N LEU A 130 O GLU A 124 ? O GLU A 150 
AA1 6  7  N LEU A 125 ? N LEU A 151 O ASN A 148 ? O ASN A 174 
AA1 7  8  N LEU A 149 ? N LEU A 175 O LEU A 179 ? O LEU A 205 
AA1 8  9  N LEU A 180 ? N LEU A 206 O LYS A 200 ? O LYS A 226 
AA1 9  10 N LEU A 201 ? N LEU A 227 O LEU A 224 ? O LEU A 250 
AA1 10 11 N LEU A 225 ? N LEU A 251 O TYR A 265 ? O TYR A 291 
AA1 11 12 N LEU A 266 ? N LEU A 292 O VAL A 289 ? O VAL A 315 
AA1 12 13 N LEU A 290 ? N LEU A 316 O ILE A 315 ? O ILE A 341 
AA1 13 14 N LEU A 316 ? N LEU A 342 O HIS A 347 ? O HIS A 373 
AA1 14 15 N LEU A 346 ? N LEU A 372 O ASN A 374 ? O ASN A 400 
AA1 15 16 N ILE A 373 ? N ILE A 399 O TYR A 398 ? O TYR A 424 
AA1 16 17 N ILE A 397 ? N ILE A 423 O ALA A 459 ? O ALA A 485 
AA1 17 18 N LEU A 460 ? N LEU A 486 O CYS A 483 ? O CYS A 509 
AA1 18 19 N LEU A 484 ? N LEU A 510 O ASP A 510 ? O ASP A 536 
AA1 19 20 N LEU A 509 ? N LEU A 535 O VAL A 532 ? O VAL A 558 
AA1 20 21 N LEU A 533 ? N LEU A 559 O VAL A 562 ? O VAL A 588 
AA1 21 22 N LEU A 563 ? N LEU A 589 O GLU A 586 ? O GLU A 612 
AA1 22 23 N LEU A 587 ? N LEU A 613 O ASP A 619 ? O ASP A 645 
AA1 23 24 N LEU A 618 ? N LEU A 644 O HIS A 644 ? O HIS A 670 
AA1 24 25 N LEU A 643 ? N LEU A 669 O ASP A 668 ? O ASP A 694 
AA1 25 26 N LEU A 667 ? N LEU A 693 O LEU A 692 ? O LEU A 718 
AA1 26 27 N LEU A 691 ? N LEU A 717 O ASP A 716 ? O ASP A 742 
AA1 27 28 N LEU A 715 ? N LEU A 741 O GLU A 742 ? O GLU A 768 
AA2 1  2  N ILE A 52  ? N ILE A 78  O ASN A 89  ? O ASN A 115 
AA3 1  2  N ILE A 135 ? N ILE A 161 O ASN A 165 ? O ASN A 191 
AA4 1  2  N ILE A 211 ? N ILE A 237 O ASN A 251 ? O ASN A 277 
AA5 1  2  N LEU A 356 ? N LEU A 382 O GLN A 382 ? O GLN A 408 
AA6 1  2  N SER A 581 ? N SER A 607 O GLY A 611 ? O GLY A 637 
AA7 1  2  N PHE A 748 ? N PHE A 774 O ALA A 778 ? O ALA A 804 
# 
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 A SO4 918 ? 3  'binding site for residue SO4 A 918'                                                       
AC2 Software A SO4 919 ? 4  'binding site for residue SO4 A 919'                                                       
AC3 Software A SO4 920 ? 2  'binding site for residue SO4 A 920'                                                       
AC4 Software A MES 921 ? 6  'binding site for residue MES A 921'                                                       
AC5 Software A NAG 901 ? 2  'binding site for Mono-Saccharide NAG A 901 bound to ASN A 285'                            
AC6 Software A ASN 293 ? 11 'binding site for Poly-Saccharide residues NAG A 902 through MAN A 905 bound to ASN A 293' 
AC7 Software A NAG 906 ? 6  'binding site for Mono-Saccharide NAG A 906 bound to ASN A 395'                            
AC8 Software A NAG 907 ? 5  'binding site for Mono-Saccharide NAG A 907 bound to ASN A 416'                            
AC9 Software A ASN 511 ? 7  'binding site for Poly-Saccharide residues NAG A 908 through NAG A 909 bound to ASN A 511' 
AD1 Software A NAG 910 ? 3  'binding site for Mono-Saccharide NAG A 910 bound to ASN A 546'                            
AD2 Software A NAG 911 ? 2  'binding site for Mono-Saccharide NAG A 911 bound to ASN A 582'                            
AD3 Software A ASN 590 ? 12 'binding site for Poly-Saccharide residues NAG A 912 through MAN A 916 bound to ASN A 590' 
AD4 Software A NAG 917 ? 4  'binding site for Mono-Saccharide NAG A 917 bound to ASN A 640'                            
# 
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 3  LYS A 651 ? LYS A 677  . ? 1_555 ? 
2  AC1 3  LYS A 673 ? LYS A 699  . ? 1_555 ? 
3  AC1 3  ARG A 697 ? ARG A 723  . ? 1_555 ? 
4  AC2 4  PHE A 255 ? PHE A 281  . ? 1_555 ? 
5  AC2 4  GLN A 258 ? GLN A 284  . ? 1_555 ? 
6  AC2 4  LYS A 282 ? LYS A 308  . ? 1_555 ? 
7  AC2 4  ASN A 283 ? ASN A 309  . ? 1_555 ? 
8  AC3 2  LYS A 282 ? LYS A 308  . ? 5_555 ? 
9  AC3 2  LYS A 339 ? LYS A 365  . ? 1_555 ? 
10 AC4 6  ARG A 264 ? ARG A 290  . ? 1_555 ? 
11 AC4 6  HIS A 286 ? HIS A 312  . ? 5_555 ? 
12 AC4 6  HIS A 286 ? HIS A 312  . ? 1_555 ? 
13 AC4 6  LYS A 288 ? LYS A 314  . ? 1_555 ? 
14 AC4 6  ARG A 312 ? ARG A 338  . ? 5_555 ? 
15 AC4 6  ARG A 312 ? ARG A 338  . ? 1_555 ? 
16 AC5 2  GLN A 258 ? GLN A 284  . ? 1_555 ? 
17 AC5 2  ASN A 259 ? ASN A 285  . ? 1_555 ? 
18 AC6 11 LYS A 200 ? LYS A 226  . ? 1_555 ? 
19 AC6 11 SER A 204 ? SER A 230  . ? 1_555 ? 
20 AC6 11 LEU A 224 ? LEU A 250  . ? 1_555 ? 
21 AC6 11 ASP A 226 ? ASP A 252  . ? 1_555 ? 
22 AC6 11 SER A 228 ? SER A 254  . ? 1_555 ? 
23 AC6 11 TYR A 265 ? TYR A 291  . ? 1_555 ? 
24 AC6 11 ASN A 267 ? ASN A 293  . ? 1_555 ? 
25 AC6 11 ASP A 291 ? ASP A 317  . ? 1_555 ? 
26 AC6 11 SER A 439 ? SER A 465  . ? 1_555 ? 
27 AC6 11 ASN A 440 ? ASN A 466  . ? 1_555 ? 
28 AC6 11 PHE A 441 ? PHE A 467  . ? 1_555 ? 
29 AC7 6  ILE A 220 ? ILE A 246  . ? 5_555 ? 
30 AC7 6  ASN A 221 ? ASN A 247  . ? 5_555 ? 
31 AC7 6  GLN A 262 ? GLN A 288  . ? 5_555 ? 
32 AC7 6  ARG A 344 ? ARG A 370  . ? 1_555 ? 
33 AC7 6  ASN A 369 ? ASN A 395  . ? 1_555 ? 
34 AC7 6  HOH W .   ? HOH A 1068 . ? 1_555 ? 
35 AC8 5  GLU A 358 ? GLU A 384  . ? 1_555 ? 
36 AC8 5  GLN A 362 ? GLN A 388  . ? 1_555 ? 
37 AC8 5  MET A 365 ? MET A 391  . ? 1_555 ? 
38 AC8 5  ASN A 390 ? ASN A 416  . ? 1_555 ? 
39 AC8 5  HOH W .   ? HOH A 1013 . ? 1_555 ? 
40 AC9 7  ILE A 449 ? ILE A 475  . ? 1_555 ? 
41 AC9 7  LYS A 450 ? LYS A 476  . ? 1_555 ? 
42 AC9 7  SER A 463 ? SER A 489  . ? 1_555 ? 
43 AC9 7  ASN A 485 ? ASN A 511  . ? 1_555 ? 
44 AC9 7  TYR A 508 ? TYR A 534  . ? 1_555 ? 
45 AC9 7  ASP A 510 ? ASP A 536  . ? 1_555 ? 
46 AC9 7  HOH W .   ? HOH A 1054 . ? 1_555 ? 
47 AD1 3  SER A 496 ? SER A 522  . ? 1_555 ? 
48 AD1 3  ASN A 520 ? ASN A 546  . ? 1_555 ? 
49 AD1 3  SER A 522 ? SER A 548  . ? 1_555 ? 
50 AD2 2  GLN A 555 ? GLN A 581  . ? 1_555 ? 
51 AD2 2  ASN A 556 ? ASN A 582  . ? 1_555 ? 
52 AD3 12 LYS A 450 ? LYS A 476  . ? 1_555 ? 
53 AD3 12 GLN A 452 ? GLN A 478  . ? 1_555 ? 
54 AD3 12 TYR A 508 ? TYR A 534  . ? 1_555 ? 
55 AD3 12 ASP A 534 ? ASP A 560  . ? 1_555 ? 
56 AD3 12 ASN A 564 ? ASN A 590  . ? 1_555 ? 
57 AD3 12 GLU A 586 ? GLU A 612  . ? 1_555 ? 
58 AD3 12 VAL A 588 ? VAL A 614  . ? 1_555 ? 
59 AD3 12 HOH W .   ? HOH A 1006 . ? 1_555 ? 
60 AD3 12 HOH W .   ? HOH A 1019 . ? 1_555 ? 
61 AD3 12 HOH W .   ? HOH A 1025 . ? 1_555 ? 
62 AD3 12 HOH W .   ? HOH A 1026 . ? 1_555 ? 
63 AD3 12 HOH W .   ? HOH A 1052 . ? 1_555 ? 
64 AD4 4  LYS A 582 ? LYS A 608  . ? 1_555 ? 
65 AD4 4  SER A 583 ? SER A 609  . ? 1_555 ? 
66 AD4 4  VAL A 585 ? VAL A 611  . ? 1_555 ? 
67 AD4 4  ASN A 614 ? ASN A 640  . ? 1_555 ? 
# 
_atom_sites.entry_id                    5HDH 
_atom_sites.fract_transf_matrix[1][1]   0.005830 
_atom_sites.fract_transf_matrix[1][2]   0.003366 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.006732 
_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]   0.003319 
_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 7   ? -101.381 -23.669 15.077  1.00 127.09 ? 33   SER A N   1 
ATOM   2    C CA  . SER A 1 7   ? -100.110 -24.173 14.473  1.00 129.36 ? 33   SER A CA  1 
ATOM   3    C C   . SER A 1 7   ? -99.341  -24.979 15.528  1.00 129.05 ? 33   SER A C   1 
ATOM   4    O O   . SER A 1 7   ? -98.863  -24.425 16.517  1.00 145.74 ? 33   SER A O   1 
ATOM   5    C CB  . SER A 1 7   ? -99.284  -23.007 13.890  1.00 136.03 ? 33   SER A CB  1 
ATOM   6    O OG  . SER A 1 7   ? -99.018  -21.992 14.846  1.00 120.91 ? 33   SER A OG  1 
ATOM   7    N N   . TYR A 1 8   ? -99.283  -26.299 15.326  1.00 126.45 ? 34   TYR A N   1 
ATOM   8    C CA  . TYR A 1 8   ? -98.619  -27.240 16.253  1.00 114.84 ? 34   TYR A CA  1 
ATOM   9    C C   . TYR A 1 8   ? -98.000  -28.443 15.483  1.00 113.91 ? 34   TYR A C   1 
ATOM   10   O O   . TYR A 1 8   ? -98.480  -28.791 14.403  1.00 120.76 ? 34   TYR A O   1 
ATOM   11   C CB  . TYR A 1 8   ? -99.685  -27.748 17.244  1.00 104.99 ? 34   TYR A CB  1 
ATOM   12   C CG  . TYR A 1 8   ? -99.234  -28.787 18.266  1.00 115.68 ? 34   TYR A CG  1 
ATOM   13   C CD1 . TYR A 1 8   ? -99.134  -28.473 19.624  1.00 118.46 ? 34   TYR A CD1 1 
ATOM   14   C CD2 . TYR A 1 8   ? -98.881  -30.078 17.869  1.00 117.64 ? 34   TYR A CD2 1 
ATOM   15   C CE1 . TYR A 1 8   ? -98.734  -29.423 20.555  1.00 112.63 ? 34   TYR A CE1 1 
ATOM   16   C CE2 . TYR A 1 8   ? -98.471  -31.030 18.792  1.00 108.64 ? 34   TYR A CE2 1 
ATOM   17   C CZ  . TYR A 1 8   ? -98.405  -30.700 20.132  1.00 113.66 ? 34   TYR A CZ  1 
ATOM   18   O OH  . TYR A 1 8   ? -98.005  -31.646 21.050  1.00 117.86 ? 34   TYR A OH  1 
ATOM   19   N N   . PRO A 1 9   ? -96.882  -29.002 15.965  1.00 124.78 ? 35   PRO A N   1 
ATOM   20   C CA  . PRO A 1 9   ? -96.196  -28.521 17.167  1.00 137.95 ? 35   PRO A CA  1 
ATOM   21   C C   . PRO A 1 9   ? -95.202  -27.410 16.801  1.00 146.05 ? 35   PRO A C   1 
ATOM   22   O O   . PRO A 1 9   ? -94.627  -26.760 17.676  1.00 136.39 ? 35   PRO A O   1 
ATOM   23   C CB  . PRO A 1 9   ? -95.447  -29.768 17.655  1.00 125.30 ? 35   PRO A CB  1 
ATOM   24   C CG  . PRO A 1 9   ? -95.127  -30.515 16.402  1.00 117.01 ? 35   PRO A CG  1 
ATOM   25   C CD  . PRO A 1 9   ? -96.274  -30.251 15.451  1.00 115.37 ? 35   PRO A CD  1 
ATOM   26   N N   . CYS A 1 10  ? -95.046  -27.189 15.499  1.00 144.31 ? 36   CYS A N   1 
ATOM   27   C CA  . CYS A 1 10  ? -94.137  -26.196 14.966  1.00 140.14 ? 36   CYS A CA  1 
ATOM   28   C C   . CYS A 1 10  ? -94.782  -24.815 14.938  1.00 135.85 ? 36   CYS A C   1 
ATOM   29   O O   . CYS A 1 10  ? -95.933  -24.671 14.523  1.00 143.71 ? 36   CYS A O   1 
ATOM   30   C CB  . CYS A 1 10  ? -93.786  -26.589 13.536  1.00 145.60 ? 36   CYS A CB  1 
ATOM   31   S SG  . CYS A 1 10  ? -93.336  -28.333 13.350  1.00 155.69 ? 36   CYS A SG  1 
ATOM   32   N N   . ASP A 1 11  ? -94.019  -23.796 15.334  1.00 143.34 ? 37   ASP A N   1 
ATOM   33   C CA  . ASP A 1 11  ? -94.511  -22.420 15.341  1.00 134.65 ? 37   ASP A CA  1 
ATOM   34   C C   . ASP A 1 11  ? -94.196  -21.792 13.997  1.00 135.42 ? 37   ASP A C   1 
ATOM   35   O O   . ASP A 1 11  ? -93.054  -21.433 13.731  1.00 149.79 ? 37   ASP A O   1 
ATOM   36   C CB  . ASP A 1 11  ? -93.861  -21.603 16.459  1.00 123.93 ? 37   ASP A CB  1 
ATOM   37   C CG  . ASP A 1 11  ? -94.152  -22.162 17.839  1.00 127.10 ? 37   ASP A CG  1 
ATOM   38   O OD1 . ASP A 1 11  ? -94.474  -23.364 17.951  1.00 134.48 ? 37   ASP A OD1 1 
ATOM   39   O OD2 . ASP A 1 11  ? -94.005  -21.414 18.822  1.00 123.21 ? 37   ASP A OD2 1 
ATOM   40   N N   . GLU A 1 12  ? -95.199  -21.707 13.133  1.00 134.73 ? 38   GLU A N   1 
ATOM   41   C CA  . GLU A 1 12  ? -95.005  -21.126 11.816  1.00 137.89 ? 38   GLU A CA  1 
ATOM   42   C C   . GLU A 1 12  ? -94.934  -19.616 11.943  1.00 141.60 ? 38   GLU A C   1 
ATOM   43   O O   . GLU A 1 12  ? -95.924  -18.973 12.286  1.00 139.50 ? 38   GLU A O   1 
ATOM   44   C CB  . GLU A 1 12  ? -96.145  -21.519 10.865  1.00 151.78 ? 38   GLU A CB  1 
ATOM   45   C CG  . GLU A 1 12  ? -96.292  -23.021 10.634  1.00 159.59 ? 38   GLU A CG  1 
ATOM   46   C CD  . GLU A 1 12  ? -97.381  -23.368 9.623   1.00 151.35 ? 38   GLU A CD  1 
ATOM   47   O OE1 . GLU A 1 12  ? -97.963  -22.436 9.024   1.00 124.70 ? 38   GLU A OE1 1 
ATOM   48   O OE2 . GLU A 1 12  ? -97.632  -24.575 9.401   1.00 145.41 ? 38   GLU A OE2 1 
ATOM   49   N N   . LYS A 1 13  ? -93.749  -19.053 11.717  1.00 154.91 ? 39   LYS A N   1 
ATOM   50   C CA  . LYS A 1 13  ? -93.573  -17.607 11.801  1.00 152.39 ? 39   LYS A CA  1 
ATOM   51   C C   . LYS A 1 13  ? -93.600  -17.091 10.366  1.00 147.80 ? 39   LYS A C   1 
ATOM   52   O O   . LYS A 1 13  ? -93.229  -17.809 9.436   1.00 139.22 ? 39   LYS A O   1 
ATOM   53   C CB  . LYS A 1 13  ? -92.254  -17.250 12.491  1.00 156.95 ? 39   LYS A CB  1 
ATOM   54   C CG  . LYS A 1 13  ? -92.131  -15.786 12.910  1.00 168.85 ? 39   LYS A CG  1 
ATOM   55   C CD  . LYS A 1 13  ? -93.163  -15.432 13.982  1.00 170.94 ? 39   LYS A CD  1 
ATOM   56   C CE  . LYS A 1 13  ? -93.032  -13.996 14.472  1.00 159.93 ? 39   LYS A CE  1 
ATOM   57   N NZ  . LYS A 1 13  ? -94.009  -13.692 15.557  1.00 143.37 ? 39   LYS A NZ  1 
ATOM   58   N N   . LYS A 1 14  ? -93.991  -15.836 10.193  1.00 152.58 ? 40   LYS A N   1 
ATOM   59   C CA  . LYS A 1 14  ? -94.097  -15.243 8.861   1.00 158.71 ? 40   LYS A CA  1 
ATOM   60   C C   . LYS A 1 14  ? -93.139  -14.090 8.588   1.00 155.28 ? 40   LYS A C   1 
ATOM   61   O O   . LYS A 1 14  ? -92.611  -13.473 9.512   1.00 163.07 ? 40   LYS A O   1 
ATOM   62   C CB  . LYS A 1 14  ? -95.550  -14.814 8.571   1.00 165.21 ? 40   LYS A CB  1 
ATOM   63   C CG  . LYS A 1 14  ? -96.235  -13.974 9.654   1.00 166.99 ? 40   LYS A CG  1 
ATOM   64   C CD  . LYS A 1 14  ? -96.559  -14.794 10.898  1.00 160.82 ? 40   LYS A CD  1 
ATOM   65   C CE  . LYS A 1 14  ? -97.264  -13.977 11.961  1.00 155.56 ? 40   LYS A CE  1 
ATOM   66   N NZ  . LYS A 1 14  ? -97.583  -14.831 13.138  1.00 158.65 ? 40   LYS A NZ  1 
ATOM   67   N N   . GLN A 1 15  ? -92.795  -13.920 7.322   1.00 153.40 ? 41   GLN A N   1 
ATOM   68   C CA  . GLN A 1 15  ? -91.878  -12.873 6.916   1.00 162.71 ? 41   GLN A CA  1 
ATOM   69   C C   . GLN A 1 15  ? -90.427  -13.348 6.983   1.00 160.46 ? 41   GLN A C   1 
ATOM   70   O O   . GLN A 1 15  ? -90.122  -14.285 7.715   1.00 123.60 ? 41   GLN A O   1 
ATOM   71   C CB  . GLN A 1 15  ? -92.065  -11.636 7.787   1.00 163.53 ? 41   GLN A CB  1 
ATOM   72   C CG  . GLN A 1 15  ? -92.745  -10.483 7.075   1.00 159.35 ? 41   GLN A CG  1 
ATOM   73   C CD  . GLN A 1 15  ? -91.788  -9.357  6.758   1.00 161.59 ? 41   GLN A CD  1 
ATOM   74   O OE1 . GLN A 1 15  ? -90.617  -9.409  7.121   1.00 165.86 ? 41   GLN A OE1 1 
ATOM   75   N NE2 . GLN A 1 15  ? -92.286  -8.326  6.082   1.00 153.28 ? 41   GLN A NE2 1 
ATOM   76   N N   . ASN A 1 16  ? -89.526  -12.687 6.253   1.00 167.63 ? 42   ASN A N   1 
ATOM   77   C CA  . ASN A 1 16  ? -89.869  -11.587 5.358   1.00 167.44 ? 42   ASN A CA  1 
ATOM   78   C C   . ASN A 1 16  ? -89.981  -12.067 3.925   1.00 169.66 ? 42   ASN A C   1 
ATOM   79   O O   . ASN A 1 16  ? -89.004  -12.477 3.312   1.00 175.89 ? 42   ASN A O   1 
ATOM   80   C CB  . ASN A 1 16  ? -88.804  -10.493 5.433   1.00 156.11 ? 42   ASN A CB  1 
ATOM   81   C CG  . ASN A 1 16  ? -87.395  -11.040 5.323   1.00 146.22 ? 42   ASN A CG  1 
ATOM   82   O OD1 . ASN A 1 16  ? -87.199  -12.233 5.098   1.00 151.06 ? 42   ASN A OD1 1 
ATOM   83   N ND2 . ASN A 1 16  ? -86.405  -10.172 5.494   1.00 123.36 ? 42   ASN A ND2 1 
ATOM   84   N N   . ASP A 1 17  ? -91.185  -12.023 3.386   1.00 157.55 ? 43   ASP A N   1 
ATOM   85   C CA  . ASP A 1 17  ? -91.368  -12.358 1.992   1.00 157.67 ? 43   ASP A CA  1 
ATOM   86   C C   . ASP A 1 17  ? -91.177  -13.853 1.794   1.00 149.54 ? 43   ASP A C   1 
ATOM   87   O O   . ASP A 1 17  ? -91.098  -14.337 0.673   1.00 139.39 ? 43   ASP A O   1 
ATOM   88   C CB  . ASP A 1 17  ? -90.392  -11.557 1.139   1.00 160.19 ? 43   ASP A CB  1 
ATOM   89   C CG  . ASP A 1 17  ? -90.397  -10.083 1.492   1.00 155.10 ? 43   ASP A CG  1 
ATOM   90   O OD1 . ASP A 1 17  ? -89.815  -9.273  0.741   1.00 140.56 ? 43   ASP A OD1 1 
ATOM   91   O OD2 . ASP A 1 17  ? -90.993  -9.734  2.529   1.00 144.95 ? 43   ASP A OD2 1 
ATOM   92   N N   . SER A 1 18  ? -91.109  -14.578 2.902   1.00 146.14 ? 44   SER A N   1 
ATOM   93   C CA  . SER A 1 18  ? -91.101  -16.025 2.892   1.00 134.63 ? 44   SER A CA  1 
ATOM   94   C C   . SER A 1 18  ? -91.634  -16.467 4.235   1.00 138.65 ? 44   SER A C   1 
ATOM   95   O O   . SER A 1 18  ? -91.566  -15.715 5.198   1.00 137.02 ? 44   SER A O   1 
ATOM   96   C CB  . SER A 1 18  ? -89.690  -16.539 2.700   1.00 113.15 ? 44   SER A CB  1 
ATOM   97   O OG  . SER A 1 18  ? -88.795  -15.765 3.459   1.00 102.82 ? 44   SER A OG  1 
ATOM   98   N N   . VAL A 1 19  ? -92.164  -17.680 4.307   1.00 144.78 ? 45   VAL A N   1 
ATOM   99   C CA  . VAL A 1 19  ? -92.613  -18.244 5.595   1.00 146.49 ? 45   VAL A CA  1 
ATOM   100  C C   . VAL A 1 19  ? -91.852  -19.501 6.009   1.00 127.55 ? 45   VAL A C   1 
ATOM   101  O O   . VAL A 1 19  ? -91.800  -20.499 5.285   1.00 99.17  ? 45   VAL A O   1 
ATOM   102  C CB  . VAL A 1 19  ? -94.128  -18.536 5.614   1.00 152.12 ? 45   VAL A CB  1 
ATOM   103  C CG1 . VAL A 1 19  ? -94.512  -19.278 6.890   1.00 149.23 ? 45   VAL A CG1 1 
ATOM   104  C CG2 . VAL A 1 19  ? -94.918  -17.239 5.481   1.00 145.11 ? 45   VAL A CG2 1 
ATOM   105  N N   . ILE A 1 20  ? -91.391  -19.468 7.252   1.00 122.43 ? 46   ILE A N   1 
ATOM   106  C CA  . ILE A 1 20  ? -90.612  -20.535 7.845   1.00 122.77 ? 46   ILE A CA  1 
ATOM   107  C C   . ILE A 1 20  ? -91.396  -21.196 8.967   1.00 116.20 ? 46   ILE A C   1 
ATOM   108  O O   . ILE A 1 20  ? -92.272  -20.577 9.583   1.00 111.72 ? 46   ILE A O   1 
ATOM   109  C CB  . ILE A 1 20  ? -89.275  -19.944 8.378   1.00 139.45 ? 46   ILE A CB  1 
ATOM   110  C CG1 . ILE A 1 20  ? -88.304  -21.018 8.890   1.00 148.44 ? 46   ILE A CG1 1 
ATOM   111  C CG2 . ILE A 1 20  ? -89.541  -18.911 9.475   1.00 128.65 ? 46   ILE A CG2 1 
ATOM   112  C CD1 . ILE A 1 20  ? -88.653  -21.633 10.228  1.00 152.59 ? 46   ILE A CD1 1 
ATOM   113  N N   . ALA A 1 21  ? -91.109  -22.476 9.183   1.00 104.70 ? 47   ALA A N   1 
ATOM   114  C CA  . ALA A 1 21  ? -91.750  -23.256 10.229  1.00 108.33 ? 47   ALA A CA  1 
ATOM   115  C C   . ALA A 1 21  ? -90.722  -23.580 11.324  1.00 106.25 ? 47   ALA A C   1 
ATOM   116  O O   . ALA A 1 21  ? -89.975  -24.560 11.217  1.00 104.92 ? 47   ALA A O   1 
ATOM   117  C CB  . ALA A 1 21  ? -92.330  -24.528 9.639   1.00 107.05 ? 47   ALA A CB  1 
ATOM   118  N N   . GLU A 1 22  ? -90.661  -22.720 12.345  1.00 105.85 ? 48   GLU A N   1 
ATOM   119  C CA  . GLU A 1 22  ? -89.721  -22.887 13.463  1.00 107.99 ? 48   GLU A CA  1 
ATOM   120  C C   . GLU A 1 22  ? -90.137  -24.141 14.181  1.00 96.77  ? 48   GLU A C   1 
ATOM   121  O O   . GLU A 1 22  ? -91.101  -24.104 14.932  1.00 93.35  ? 48   GLU A O   1 
ATOM   122  C CB  . GLU A 1 22  ? -89.818  -21.712 14.451  1.00 119.25 ? 48   GLU A CB  1 
ATOM   123  C CG  . GLU A 1 22  ? -89.572  -20.323 13.878  1.00 116.90 ? 48   GLU A CG  1 
ATOM   124  C CD  . GLU A 1 22  ? -89.733  -19.239 14.934  1.00 133.87 ? 48   GLU A CD  1 
ATOM   125  O OE1 . GLU A 1 22  ? -89.846  -18.047 14.570  1.00 137.79 ? 48   GLU A OE1 1 
ATOM   126  O OE2 . GLU A 1 22  ? -89.809  -19.588 16.133  1.00 142.15 ? 48   GLU A OE2 1 
ATOM   127  N N   . CYS A 1 23  ? -89.386  -25.228 14.038  1.00 105.08 ? 49   CYS A N   1 
ATOM   128  C CA  . CYS A 1 23  ? -89.803  -26.470 14.682  1.00 115.56 ? 49   CYS A CA  1 
ATOM   129  C C   . CYS A 1 23  ? -88.653  -27.296 15.234  1.00 111.91 ? 49   CYS A C   1 
ATOM   130  O O   . CYS A 1 23  ? -88.515  -28.488 14.927  1.00 111.75 ? 49   CYS A O   1 
ATOM   131  C CB  . CYS A 1 23  ? -90.558  -27.296 13.655  1.00 127.52 ? 49   CYS A CB  1 
ATOM   132  S SG  . CYS A 1 23  ? -91.594  -28.568 14.372  1.00 161.65 ? 49   CYS A SG  1 
ATOM   133  N N   . SER A 1 24  ? -87.860  -26.681 16.093  1.00 109.80 ? 50   SER A N   1 
ATOM   134  C CA  . SER A 1 24  ? -86.724  -27.362 16.674  1.00 107.22 ? 50   SER A CA  1 
ATOM   135  C C   . SER A 1 24  ? -86.840  -27.492 18.174  1.00 97.85  ? 50   SER A C   1 
ATOM   136  O O   . SER A 1 24  ? -87.589  -26.768 18.836  1.00 82.22  ? 50   SER A O   1 
ATOM   137  C CB  . SER A 1 24  ? -85.440  -26.617 16.329  1.00 103.96 ? 50   SER A CB  1 
ATOM   138  O OG  . SER A 1 24  ? -85.495  -25.294 16.812  1.00 109.33 ? 50   SER A OG  1 
ATOM   139  N N   . ASN A 1 25  ? -86.101  -28.448 18.703  1.00 95.62  ? 51   ASN A N   1 
ATOM   140  C CA  . ASN A 1 25  ? -86.083  -28.691 20.117  1.00 102.65 ? 51   ASN A CA  1 
ATOM   141  C C   . ASN A 1 25  ? -87.484  -29.008 20.650  1.00 111.90 ? 51   ASN A C   1 
ATOM   142  O O   . ASN A 1 25  ? -87.904  -28.455 21.664  1.00 100.80 ? 51   ASN A O   1 
ATOM   143  C CB  . ASN A 1 25  ? -85.507  -27.471 20.826  1.00 102.39 ? 51   ASN A CB  1 
ATOM   144  C CG  . ASN A 1 25  ? -85.113  -27.765 22.248  1.00 109.19 ? 51   ASN A CG  1 
ATOM   145  O OD1 . ASN A 1 25  ? -84.762  -28.901 22.588  1.00 113.08 ? 51   ASN A OD1 1 
ATOM   146  N ND2 . ASN A 1 25  ? -85.061  -26.728 23.065  1.00 105.49 ? 51   ASN A ND2 1 
ATOM   147  N N   . ARG A 1 26  ? -88.242  -29.805 19.893  1.00 125.34 ? 52   ARG A N   1 
ATOM   148  C CA  . ARG A 1 26  ? -89.585  -30.222 20.310  1.00 112.89 ? 52   ARG A CA  1 
ATOM   149  C C   . ARG A 1 26  ? -89.665  -31.710 20.653  1.00 118.23 ? 52   ARG A C   1 
ATOM   150  O O   . ARG A 1 26  ? -90.752  -32.272 20.693  1.00 123.74 ? 52   ARG A O   1 
ATOM   151  C CB  . ARG A 1 26  ? -90.691  -29.918 19.296  1.00 111.50 ? 52   ARG A CB  1 
ATOM   152  C CG  . ARG A 1 26  ? -91.224  -28.496 19.208  1.00 113.00 ? 52   ARG A CG  1 
ATOM   153  C CD  . ARG A 1 26  ? -90.507  -27.595 18.222  1.00 128.79 ? 52   ARG A CD  1 
ATOM   154  N NE  . ARG A 1 26  ? -91.353  -26.424 17.963  1.00 142.06 ? 52   ARG A NE  1 
ATOM   155  C CZ  . ARG A 1 26  ? -91.242  -25.236 18.557  1.00 138.41 ? 52   ARG A CZ  1 
ATOM   156  N NH1 . ARG A 1 26  ? -92.111  -24.276 18.264  1.00 134.58 ? 52   ARG A NH1 1 
ATOM   157  N NH2 . ARG A 1 26  ? -90.281  -25.000 19.442  1.00 138.95 ? 52   ARG A NH2 1 
ATOM   158  N N   . ARG A 1 27  ? -88.525  -32.356 20.860  1.00 120.63 ? 53   ARG A N   1 
ATOM   159  C CA  . ARG A 1 27  ? -88.510  -33.776 21.216  1.00 116.16 ? 53   ARG A CA  1 
ATOM   160  C C   . ARG A 1 27  ? -89.047  -34.711 20.145  1.00 115.61 ? 53   ARG A C   1 
ATOM   161  O O   . ARG A 1 27  ? -89.286  -35.883 20.418  1.00 127.37 ? 53   ARG A O   1 
ATOM   162  C CB  . ARG A 1 27  ? -89.296  -34.005 22.517  1.00 112.10 ? 53   ARG A CB  1 
ATOM   163  C CG  . ARG A 1 27  ? -88.651  -33.387 23.745  1.00 120.06 ? 53   ARG A CG  1 
ATOM   164  C CD  . ARG A 1 27  ? -89.348  -33.811 25.028  1.00 116.65 ? 53   ARG A CD  1 
ATOM   165  N NE  . ARG A 1 27  ? -90.616  -33.130 25.305  1.00 126.84 ? 53   ARG A NE  1 
ATOM   166  C CZ  . ARG A 1 27  ? -90.734  -32.076 26.119  1.00 138.38 ? 53   ARG A CZ  1 
ATOM   167  N NH1 . ARG A 1 27  ? -89.670  -31.598 26.757  1.00 146.19 ? 53   ARG A NH1 1 
ATOM   168  N NH2 . ARG A 1 27  ? -91.919  -31.521 26.336  1.00 137.69 ? 53   ARG A NH2 1 
ATOM   169  N N   . LEU A 1 28  ? -89.102  -34.248 18.906  1.00 107.13 ? 54   LEU A N   1 
ATOM   170  C CA  . LEU A 1 28  ? -89.644  -35.073 17.839  1.00 104.75 ? 54   LEU A CA  1 
ATOM   171  C C   . LEU A 1 28  ? -88.751  -36.269 17.519  1.00 121.16 ? 54   LEU A C   1 
ATOM   172  O O   . LEU A 1 28  ? -87.520  -36.204 17.636  1.00 111.57 ? 54   LEU A O   1 
ATOM   173  C CB  . LEU A 1 28  ? -89.859  -34.257 16.566  1.00 92.60  ? 54   LEU A CB  1 
ATOM   174  C CG  . LEU A 1 28  ? -90.443  -32.855 16.772  1.00 105.64 ? 54   LEU A CG  1 
ATOM   175  C CD1 . LEU A 1 28  ? -91.024  -32.313 15.478  1.00 96.28  ? 54   LEU A CD1 1 
ATOM   176  C CD2 . LEU A 1 28  ? -91.431  -32.763 17.926  1.00 104.48 ? 54   LEU A CD2 1 
ATOM   177  N N   . GLN A 1 29  ? -89.396  -37.377 17.165  1.00 131.40 ? 55   GLN A N   1 
ATOM   178  C CA  . GLN A 1 29  ? -88.700  -38.597 16.799  1.00 122.51 ? 55   GLN A CA  1 
ATOM   179  C C   . GLN A 1 29  ? -88.796  -38.635 15.265  1.00 119.34 ? 55   GLN A C   1 
ATOM   180  O O   . GLN A 1 29  ? -88.075  -39.386 14.612  1.00 116.18 ? 55   GLN A O   1 
ATOM   181  C CB  . GLN A 1 29  ? -89.445  -39.826 17.343  1.00 122.01 ? 55   GLN A CB  1 
ATOM   182  C CG  . GLN A 1 29  ? -89.935  -39.733 18.795  1.00 128.64 ? 55   GLN A CG  1 
ATOM   183  C CD  . GLN A 1 29  ? -88.898  -40.049 19.873  1.00 141.65 ? 55   GLN A CD  1 
ATOM   184  O OE1 . GLN A 1 29  ? -89.027  -39.594 21.014  1.00 133.22 ? 55   GLN A OE1 1 
ATOM   185  N NE2 . GLN A 1 29  ? -87.919  -40.889 19.547  1.00 144.97 ? 55   GLN A NE2 1 
ATOM   186  N N   . GLU A 1 30  ? -89.709  -37.832 14.702  1.00 118.46 ? 56   GLU A N   1 
ATOM   187  C CA  . GLU A 1 30  ? -89.926  -37.792 13.248  1.00 133.37 ? 56   GLU A CA  1 
ATOM   188  C C   . GLU A 1 30  ? -90.192  -36.386 12.695  1.00 126.76 ? 56   GLU A C   1 
ATOM   189  O O   . GLU A 1 30  ? -90.360  -35.431 13.446  1.00 133.38 ? 56   GLU A O   1 
ATOM   190  C CB  . GLU A 1 30  ? -91.159  -38.620 12.908  1.00 146.04 ? 56   GLU A CB  1 
ATOM   191  C CG  . GLU A 1 30  ? -92.427  -38.045 13.532  1.00 147.80 ? 56   GLU A CG  1 
ATOM   192  C CD  . GLU A 1 30  ? -93.686  -38.719 13.042  1.00 154.60 ? 56   GLU A CD  1 
ATOM   193  O OE1 . GLU A 1 30  ? -93.594  -39.565 12.128  1.00 160.50 ? 56   GLU A OE1 1 
ATOM   194  O OE2 . GLU A 1 30  ? -94.775  -38.356 13.531  1.00 150.47 ? 56   GLU A OE2 1 
ATOM   195  N N   . VAL A 1 31  ? -90.308  -36.292 11.381  1.00 108.38 ? 57   VAL A N   1 
ATOM   196  C CA  . VAL A 1 31  ? -90.615  -35.041 10.738  1.00 104.46 ? 57   VAL A CA  1 
ATOM   197  C C   . VAL A 1 31  ? -92.097  -34.959 10.549  1.00 115.01 ? 57   VAL A C   1 
ATOM   198  O O   . VAL A 1 31  ? -92.642  -35.730 9.772   1.00 120.80 ? 57   VAL A O   1 
ATOM   199  C CB  . VAL A 1 31  ? -90.055  -35.045 9.325   1.00 113.45 ? 57   VAL A CB  1 
ATOM   200  C CG1 . VAL A 1 31  ? -90.388  -33.760 8.603   1.00 102.34 ? 57   VAL A CG1 1 
ATOM   201  C CG2 . VAL A 1 31  ? -88.572  -35.314 9.343   1.00 113.14 ? 57   VAL A CG2 1 
ATOM   202  N N   . PRO A 1 32  ? -92.753  -33.932 11.244  1.00 119.74 ? 58   PRO A N   1 
ATOM   203  C CA  . PRO A 1 32  ? -94.211  -33.965 11.065  1.00 126.86 ? 58   PRO A CA  1 
ATOM   204  C C   . PRO A 1 32  ? -94.600  -33.765 9.626   1.00 135.65 ? 58   PRO A C   1 
ATOM   205  O O   . PRO A 1 32  ? -94.120  -32.852 8.985   1.00 141.55 ? 58   PRO A O   1 
ATOM   206  C CB  . PRO A 1 32  ? -94.698  -32.759 11.853  1.00 122.58 ? 58   PRO A CB  1 
ATOM   207  C CG  . PRO A 1 32  ? -93.731  -32.613 12.942  1.00 124.25 ? 58   PRO A CG  1 
ATOM   208  C CD  . PRO A 1 32  ? -92.459  -32.758 12.199  1.00 123.83 ? 58   PRO A CD  1 
ATOM   209  N N   . GLN A 1 33  ? -95.493  -34.607 9.138   1.00 141.10 ? 59   GLN A N   1 
ATOM   210  C CA  . GLN A 1 33  ? -96.096  -34.437 7.830   1.00 148.75 ? 59   GLN A CA  1 
ATOM   211  C C   . GLN A 1 33  ? -96.978  -33.216 7.781   1.00 152.59 ? 59   GLN A C   1 
ATOM   212  O O   . GLN A 1 33  ? -97.104  -32.563 6.755   1.00 158.98 ? 59   GLN A O   1 
ATOM   213  C CB  . GLN A 1 33  ? -96.861  -35.677 7.430   1.00 148.35 ? 59   GLN A CB  1 
ATOM   214  C CG  . GLN A 1 33  ? -95.943  -36.854 7.174   1.00 172.12 ? 59   GLN A CG  1 
ATOM   215  C CD  . GLN A 1 33  ? -95.132  -37.206 8.396   1.00 195.87 ? 59   GLN A CD  1 
ATOM   216  O OE1 . GLN A 1 33  ? -95.057  -36.423 9.339   1.00 220.01 ? 59   GLN A OE1 1 
ATOM   217  N NE2 . GLN A 1 33  ? -94.529  -38.389 8.394   1.00 197.90 ? 59   GLN A NE2 1 
ATOM   218  N N   . THR A 1 34  ? -97.608  -32.918 8.901   1.00 151.22 ? 60   THR A N   1 
ATOM   219  C CA  . THR A 1 34  ? -98.612  -31.886 8.934   1.00 135.37 ? 60   THR A CA  1 
ATOM   220  C C   . THR A 1 34  ? -97.906  -30.552 9.005   1.00 133.09 ? 60   THR A C   1 
ATOM   221  O O   . THR A 1 34  ? -97.978  -29.818 9.988   1.00 105.46 ? 60   THR A O   1 
ATOM   222  C CB  . THR A 1 34  ? -99.454  -32.067 10.184  1.00 137.42 ? 60   THR A CB  1 
ATOM   223  O OG1 . THR A 1 34  ? -98.650  -31.731 11.319  1.00 132.33 ? 60   THR A OG1 1 
ATOM   224  C CG2 . THR A 1 34  ? -99.872  -33.503 10.306  1.00 147.95 ? 60   THR A CG2 1 
ATOM   225  N N   . VAL A 1 35  ? -97.212  -30.242 7.924   1.00 142.93 ? 61   VAL A N   1 
ATOM   226  C CA  . VAL A 1 35  ? -96.448  -29.015 7.845   1.00 139.02 ? 61   VAL A CA  1 
ATOM   227  C C   . VAL A 1 35  ? -96.994  -28.131 6.737   1.00 136.35 ? 61   VAL A C   1 
ATOM   228  O O   . VAL A 1 35  ? -96.967  -28.485 5.567   1.00 132.92 ? 61   VAL A O   1 
ATOM   229  C CB  . VAL A 1 35  ? -94.961  -29.336 7.625   1.00 129.77 ? 61   VAL A CB  1 
ATOM   230  C CG1 . VAL A 1 35  ? -94.808  -30.491 6.659   1.00 133.07 ? 61   VAL A CG1 1 
ATOM   231  C CG2 . VAL A 1 35  ? -94.178  -28.122 7.165   1.00 130.24 ? 61   VAL A CG2 1 
ATOM   232  N N   . GLY A 1 36  ? -97.438  -26.951 7.129   1.00 130.94 ? 62   GLY A N   1 
ATOM   233  C CA  . GLY A 1 36  ? -98.075  -25.997 6.201   1.00 132.62 ? 62   GLY A CA  1 
ATOM   234  C C   . GLY A 1 36  ? -97.359  -26.008 4.864   1.00 141.56 ? 62   GLY A C   1 
ATOM   235  O O   . GLY A 1 36  ? -96.144  -25.855 4.823   1.00 164.66 ? 62   GLY A O   1 
ATOM   236  N N   . LYS A 1 37  ? -98.089  -26.178 3.762   1.00 140.55 ? 63   LYS A N   1 
ATOM   237  C CA  . LYS A 1 37  ? -97.422  -26.222 2.462   1.00 141.36 ? 63   LYS A CA  1 
ATOM   238  C C   . LYS A 1 37  ? -96.793  -24.863 2.185   1.00 140.84 ? 63   LYS A C   1 
ATOM   239  O O   . LYS A 1 37  ? -96.969  -23.908 2.950   1.00 118.35 ? 63   LYS A O   1 
ATOM   240  C CB  . LYS A 1 37  ? -98.340  -26.603 1.281   1.00 154.83 ? 63   LYS A CB  1 
ATOM   241  C CG  . LYS A 1 37  ? -99.262  -27.808 1.453   1.00 153.03 ? 63   LYS A CG  1 
ATOM   242  C CD  . LYS A 1 37  ? -100.562 -27.434 2.153   1.00 150.99 ? 63   LYS A CD  1 
ATOM   243  C CE  . LYS A 1 37  ? -101.333 -26.421 1.308   1.00 147.32 ? 63   LYS A CE  1 
ATOM   244  N NZ  . LYS A 1 37  ? -102.614 -25.985 1.918   1.00 154.27 ? 63   LYS A NZ  1 
ATOM   245  N N   . TYR A 1 38  ? -96.135  -24.774 1.038   1.00 149.33 ? 64   TYR A N   1 
ATOM   246  C CA  . TYR A 1 38  ? -95.437  -23.570 0.603   1.00 164.78 ? 64   TYR A CA  1 
ATOM   247  C C   . TYR A 1 38  ? -94.650  -22.909 1.742   1.00 167.82 ? 64   TYR A C   1 
ATOM   248  O O   . TYR A 1 38  ? -95.008  -21.844 2.254   1.00 164.74 ? 64   TYR A O   1 
ATOM   249  C CB  . TYR A 1 38  ? -96.331  -22.588 -0.197  1.00 172.56 ? 64   TYR A CB  1 
ATOM   250  C CG  . TYR A 1 38  ? -97.472  -21.907 0.537   1.00 187.30 ? 64   TYR A CG  1 
ATOM   251  C CD1 . TYR A 1 38  ? -97.297  -20.648 1.112   1.00 188.62 ? 64   TYR A CD1 1 
ATOM   252  C CD2 . TYR A 1 38  ? -98.754  -22.453 0.539   1.00 184.82 ? 64   TYR A CD2 1 
ATOM   253  C CE1 . TYR A 1 38  ? -98.342  -19.992 1.739   1.00 177.65 ? 64   TYR A CE1 1 
ATOM   254  C CE2 . TYR A 1 38  ? -99.809  -21.802 1.164   1.00 172.18 ? 64   TYR A CE2 1 
ATOM   255  C CZ  . TYR A 1 38  ? -99.596  -20.571 1.762   1.00 174.27 ? 64   TYR A CZ  1 
ATOM   256  O OH  . TYR A 1 38  ? -100.632 -19.912 2.387   1.00 144.75 ? 64   TYR A OH  1 
ATOM   257  N N   . VAL A 1 39  ? -93.606  -23.617 2.166   1.00 161.69 ? 65   VAL A N   1 
ATOM   258  C CA  . VAL A 1 39  ? -92.699  -23.162 3.210   1.00 145.90 ? 65   VAL A CA  1 
ATOM   259  C C   . VAL A 1 39  ? -91.360  -22.938 2.526   1.00 143.11 ? 65   VAL A C   1 
ATOM   260  O O   . VAL A 1 39  ? -90.973  -23.696 1.626   1.00 128.35 ? 65   VAL A O   1 
ATOM   261  C CB  . VAL A 1 39  ? -92.546  -24.199 4.339   1.00 143.81 ? 65   VAL A CB  1 
ATOM   262  C CG1 . VAL A 1 39  ? -91.487  -23.763 5.339   1.00 145.89 ? 65   VAL A CG1 1 
ATOM   263  C CG2 . VAL A 1 39  ? -93.868  -24.391 5.051   1.00 148.30 ? 65   VAL A CG2 1 
ATOM   264  N N   . THR A 1 40  ? -90.679  -21.867 2.905   1.00 131.60 ? 66   THR A N   1 
ATOM   265  C CA  . THR A 1 40  ? -89.396  -21.559 2.311   1.00 133.02 ? 66   THR A CA  1 
ATOM   266  C C   . THR A 1 40  ? -88.385  -22.538 2.884   1.00 131.14 ? 66   THR A C   1 
ATOM   267  O O   . THR A 1 40  ? -87.648  -23.204 2.146   1.00 111.88 ? 66   THR A O   1 
ATOM   268  C CB  . THR A 1 40  ? -88.951  -20.122 2.647   1.00 136.31 ? 66   THR A CB  1 
ATOM   269  O OG1 . THR A 1 40  ? -90.045  -19.224 2.445   1.00 137.06 ? 66   THR A OG1 1 
ATOM   270  C CG2 . THR A 1 40  ? -87.740  -19.695 1.789   1.00 125.07 ? 66   THR A CG2 1 
ATOM   271  N N   . GLU A 1 41  ? -88.394  -22.661 4.208   1.00 124.18 ? 67   GLU A N   1 
ATOM   272  C CA  . GLU A 1 41  ? -87.472  -23.550 4.895   1.00 125.31 ? 67   GLU A CA  1 
ATOM   273  C C   . GLU A 1 41  ? -87.999  -24.049 6.225   1.00 110.74 ? 67   GLU A C   1 
ATOM   274  O O   . GLU A 1 41  ? -88.857  -23.419 6.846   1.00 97.21  ? 67   GLU A O   1 
ATOM   275  C CB  . GLU A 1 41  ? -86.147  -22.842 5.113   1.00 140.09 ? 67   GLU A CB  1 
ATOM   276  C CG  . GLU A 1 41  ? -86.283  -21.491 5.800   1.00 153.29 ? 67   GLU A CG  1 
ATOM   277  C CD  . GLU A 1 41  ? -84.946  -20.836 6.105   1.00 153.74 ? 67   GLU A CD  1 
ATOM   278  O OE1 . GLU A 1 41  ? -83.962  -21.563 6.375   1.00 148.02 ? 67   GLU A OE1 1 
ATOM   279  O OE2 . GLU A 1 41  ? -84.905  -19.589 6.175   1.00 125.17 ? 67   GLU A OE2 1 
ATOM   280  N N   . LEU A 1 42  ? -87.395  -25.138 6.687   1.00 98.83  ? 68   LEU A N   1 
ATOM   281  C CA  . LEU A 1 42  ? -87.766  -25.791 7.933   1.00 96.84  ? 68   LEU A CA  1 
ATOM   282  C C   . LEU A 1 42  ? -86.606  -25.940 8.914   1.00 94.85  ? 68   LEU A C   1 
ATOM   283  O O   . LEU A 1 42  ? -85.504  -26.379 8.552   1.00 100.66 ? 68   LEU A O   1 
ATOM   284  C CB  . LEU A 1 42  ? -88.250  -27.203 7.618   1.00 118.23 ? 68   LEU A CB  1 
ATOM   285  C CG  . LEU A 1 42  ? -88.615  -28.057 8.835   1.00 123.77 ? 68   LEU A CG  1 
ATOM   286  C CD1 . LEU A 1 42  ? -89.929  -27.601 9.462   1.00 125.09 ? 68   LEU A CD1 1 
ATOM   287  C CD2 . LEU A 1 42  ? -88.714  -29.509 8.409   1.00 115.39 ? 68   LEU A CD2 1 
ATOM   288  N N   . ASP A 1 43  ? -86.920  -25.751 10.185  1.00 88.18  ? 69   ASP A N   1 
ATOM   289  C CA  . ASP A 1 43  ? -85.935  -25.868 11.239  1.00 96.70  ? 69   ASP A CA  1 
ATOM   290  C C   . ASP A 1 43  ? -86.238  -27.080 12.144  1.00 102.06 ? 69   ASP A C   1 
ATOM   291  O O   . ASP A 1 43  ? -87.165  -27.032 12.956  1.00 92.77  ? 69   ASP A O   1 
ATOM   292  C CB  . ASP A 1 43  ? -85.944  -24.587 12.073  1.00 88.12  ? 69   ASP A CB  1 
ATOM   293  C CG  . ASP A 1 43  ? -84.926  -24.616 13.175  1.00 90.84  ? 69   ASP A CG  1 
ATOM   294  O OD1 . ASP A 1 43  ? -83.915  -25.354 13.034  1.00 78.98  ? 69   ASP A OD1 1 
ATOM   295  O OD2 . ASP A 1 43  ? -85.117  -23.869 14.158  1.00 92.17  ? 69   ASP A OD2 1 
ATOM   296  N N   . LEU A 1 44  ? -85.429  -28.137 12.046  1.00 100.67 ? 70   LEU A N   1 
ATOM   297  C CA  . LEU A 1 44  ? -85.640  -29.349 12.864  1.00 102.89 ? 70   LEU A CA  1 
ATOM   298  C C   . LEU A 1 44  ? -84.444  -29.726 13.734  1.00 110.10 ? 70   LEU A C   1 
ATOM   299  O O   . LEU A 1 44  ? -84.228  -30.907 14.041  1.00 100.00 ? 70   LEU A O   1 
ATOM   300  C CB  . LEU A 1 44  ? -85.970  -30.539 11.967  1.00 103.69 ? 70   LEU A CB  1 
ATOM   301  C CG  . LEU A 1 44  ? -87.225  -30.442 11.103  1.00 101.25 ? 70   LEU A CG  1 
ATOM   302  C CD1 . LEU A 1 44  ? -87.269  -31.671 10.215  1.00 99.12  ? 70   LEU A CD1 1 
ATOM   303  C CD2 . LEU A 1 44  ? -88.496  -30.298 11.938  1.00 96.16  ? 70   LEU A CD2 1 
ATOM   304  N N   . SER A 1 45  ? -83.677  -28.729 14.148  1.00 104.01 ? 71   SER A N   1 
ATOM   305  C CA  . SER A 1 45  ? -82.513  -28.980 14.976  1.00 105.19 ? 71   SER A CA  1 
ATOM   306  C C   . SER A 1 45  ? -82.922  -29.351 16.393  1.00 98.89  ? 71   SER A C   1 
ATOM   307  O O   . SER A 1 45  ? -84.032  -29.050 16.824  1.00 86.38  ? 71   SER A O   1 
ATOM   308  C CB  . SER A 1 45  ? -81.632  -27.731 15.027  1.00 110.67 ? 71   SER A CB  1 
ATOM   309  O OG  . SER A 1 45  ? -82.338  -26.633 15.591  1.00 104.15 ? 71   SER A OG  1 
ATOM   310  N N   . ASP A 1 46  ? -82.012  -30.009 17.108  1.00 100.84 ? 72   ASP A N   1 
ATOM   311  C CA  . ASP A 1 46  ? -82.234  -30.407 18.504  1.00 113.23 ? 72   ASP A CA  1 
ATOM   312  C C   . ASP A 1 46  ? -83.459  -31.284 18.730  1.00 114.77 ? 72   ASP A C   1 
ATOM   313  O O   . ASP A 1 46  ? -84.383  -30.902 19.456  1.00 117.25 ? 72   ASP A O   1 
ATOM   314  C CB  . ASP A 1 46  ? -82.333  -29.164 19.407  1.00 125.60 ? 72   ASP A CB  1 
ATOM   315  C CG  . ASP A 1 46  ? -81.054  -28.333 19.419  1.00 118.76 ? 72   ASP A CG  1 
ATOM   316  O OD1 . ASP A 1 46  ? -80.003  -28.826 18.961  1.00 109.36 ? 72   ASP A OD1 1 
ATOM   317  O OD2 . ASP A 1 46  ? -81.095  -27.202 19.946  1.00 132.98 ? 72   ASP A OD2 1 
ATOM   318  N N   . ASN A 1 47  ? -83.442  -32.470 18.128  1.00 118.04 ? 73   ASN A N   1 
ATOM   319  C CA  . ASN A 1 47  ? -84.529  -33.447 18.255  1.00 110.50 ? 73   ASN A CA  1 
ATOM   320  C C   . ASN A 1 47  ? -83.980  -34.863 18.439  1.00 128.19 ? 73   ASN A C   1 
ATOM   321  O O   . ASN A 1 47  ? -82.781  -35.049 18.733  1.00 104.47 ? 73   ASN A O   1 
ATOM   322  C CB  . ASN A 1 47  ? -85.479  -33.365 17.051  1.00 99.83  ? 73   ASN A CB  1 
ATOM   323  C CG  . ASN A 1 47  ? -86.356  -32.124 17.084  1.00 101.70 ? 73   ASN A CG  1 
ATOM   324  O OD1 . ASN A 1 47  ? -86.798  -31.696 18.155  1.00 93.77  ? 73   ASN A OD1 1 
ATOM   325  N ND2 . ASN A 1 47  ? -86.711  -31.612 15.907  1.00 102.77 ? 73   ASN A ND2 1 
ATOM   326  N N   . PHE A 1 48  ? -84.877  -35.849 18.379  1.00 148.06 ? 74   PHE A N   1 
ATOM   327  C CA  . PHE A 1 48  ? -84.483  -37.247 18.530  1.00 140.88 ? 74   PHE A CA  1 
ATOM   328  C C   . PHE A 1 48  ? -84.590  -38.009 17.211  1.00 123.47 ? 74   PHE A C   1 
ATOM   329  O O   . PHE A 1 48  ? -84.346  -39.216 17.166  1.00 111.82 ? 74   PHE A O   1 
ATOM   330  C CB  . PHE A 1 48  ? -85.294  -37.943 19.629  1.00 136.82 ? 74   PHE A CB  1 
ATOM   331  C CG  . PHE A 1 48  ? -85.143  -37.310 20.987  1.00 135.83 ? 74   PHE A CG  1 
ATOM   332  C CD1 . PHE A 1 48  ? -83.966  -37.473 21.716  1.00 132.00 ? 74   PHE A CD1 1 
ATOM   333  C CD2 . PHE A 1 48  ? -86.212  -36.648 21.585  1.00 121.66 ? 74   PHE A CD2 1 
ATOM   334  C CE1 . PHE A 1 48  ? -83.826  -36.903 22.971  1.00 123.98 ? 74   PHE A CE1 1 
ATOM   335  C CE2 . PHE A 1 48  ? -86.085  -36.100 22.850  1.00 118.94 ? 74   PHE A CE2 1 
ATOM   336  C CZ  . PHE A 1 48  ? -84.890  -36.228 23.544  1.00 117.87 ? 74   PHE A CZ  1 
ATOM   337  N N   . ILE A 1 49  ? -84.917  -37.298 16.134  1.00 103.09 ? 75   ILE A N   1 
ATOM   338  C CA  . ILE A 1 49  ? -85.023  -37.926 14.826  1.00 95.17  ? 75   ILE A CA  1 
ATOM   339  C C   . ILE A 1 49  ? -83.808  -38.817 14.590  1.00 105.46 ? 75   ILE A C   1 
ATOM   340  O O   . ILE A 1 49  ? -82.692  -38.472 14.989  1.00 114.14 ? 75   ILE A O   1 
ATOM   341  C CB  . ILE A 1 49  ? -85.102  -36.886 13.699  1.00 86.35  ? 75   ILE A CB  1 
ATOM   342  C CG1 . ILE A 1 49  ? -86.376  -36.069 13.843  1.00 83.10  ? 75   ILE A CG1 1 
ATOM   343  C CG2 . ILE A 1 49  ? -85.088  -37.573 12.337  1.00 89.47  ? 75   ILE A CG2 1 
ATOM   344  C CD1 . ILE A 1 49  ? -86.545  -35.017 12.782  1.00 82.94  ? 75   ILE A CD1 1 
ATOM   345  N N   . THR A 1 50  ? -84.034  -39.980 13.984  1.00 103.71 ? 76   THR A N   1 
ATOM   346  C CA  . THR A 1 50  ? -82.946  -40.912 13.705  1.00 100.79 ? 76   THR A CA  1 
ATOM   347  C C   . THR A 1 50  ? -82.974  -41.460 12.289  1.00 101.42 ? 76   THR A C   1 
ATOM   348  O O   . THR A 1 50  ? -82.012  -42.098 11.835  1.00 86.84  ? 76   THR A O   1 
ATOM   349  C CB  . THR A 1 50  ? -82.927  -42.081 14.705  1.00 111.70 ? 76   THR A CB  1 
ATOM   350  O OG1 . THR A 1 50  ? -81.945  -43.039 14.294  1.00 111.78 ? 76   THR A OG1 1 
ATOM   351  C CG2 . THR A 1 50  ? -84.287  -42.769 14.772  1.00 117.73 ? 76   THR A CG2 1 
ATOM   352  N N   . HIS A 1 51  ? -84.054  -41.192 11.570  1.00 98.04  ? 77   HIS A N   1 
ATOM   353  C CA  . HIS A 1 51  ? -84.156  -41.676 10.215  1.00 107.65 ? 77   HIS A CA  1 
ATOM   354  C C   . HIS A 1 51  ? -84.553  -40.624 9.219   1.00 98.88  ? 77   HIS A C   1 
ATOM   355  O O   . HIS A 1 51  ? -85.525  -39.905 9.411   1.00 86.35  ? 77   HIS A O   1 
ATOM   356  C CB  . HIS A 1 51  ? -85.141  -42.856 10.099  1.00 128.14 ? 77   HIS A CB  1 
ATOM   357  C CG  . HIS A 1 51  ? -84.614  -44.149 10.642  1.00 135.22 ? 77   HIS A CG  1 
ATOM   358  N ND1 . HIS A 1 51  ? -85.116  -44.755 11.775  1.00 131.68 ? 77   HIS A ND1 1 
ATOM   359  C CD2 . HIS A 1 51  ? -83.575  -44.915 10.236  1.00 133.22 ? 77   HIS A CD2 1 
ATOM   360  C CE1 . HIS A 1 51  ? -84.448  -45.873 12.004  1.00 131.38 ? 77   HIS A CE1 1 
ATOM   361  N NE2 . HIS A 1 51  ? -83.493  -45.980 11.097  1.00 132.74 ? 77   HIS A NE2 1 
ATOM   362  N N   . ILE A 1 52  ? -83.771  -40.520 8.159   1.00 97.78  ? 78   ILE A N   1 
ATOM   363  C CA  . ILE A 1 52  ? -84.073  -39.592 7.100   1.00 115.80 ? 78   ILE A CA  1 
ATOM   364  C C   . ILE A 1 52  ? -84.277  -40.471 5.914   1.00 124.91 ? 78   ILE A C   1 
ATOM   365  O O   . ILE A 1 52  ? -83.401  -41.271 5.568   1.00 111.08 ? 78   ILE A O   1 
ATOM   366  C CB  . ILE A 1 52  ? -83.002  -38.523 6.887   1.00 125.01 ? 78   ILE A CB  1 
ATOM   367  C CG1 . ILE A 1 52  ? -83.008  -37.579 8.095   1.00 119.41 ? 78   ILE A CG1 1 
ATOM   368  C CG2 . ILE A 1 52  ? -83.296  -37.730 5.618   1.00 127.55 ? 78   ILE A CG2 1 
ATOM   369  C CD1 . ILE A 1 52  ? -84.377  -36.964 8.377   1.00 112.79 ? 78   ILE A CD1 1 
ATOM   370  N N   . THR A 1 53  ? -85.427  -40.287 5.271   1.00 133.26 ? 79   THR A N   1 
ATOM   371  C CA  . THR A 1 53  ? -85.805  -41.120 4.158   1.00 131.95 ? 79   THR A CA  1 
ATOM   372  C C   . THR A 1 53  ? -86.719  -40.482 3.109   1.00 127.93 ? 79   THR A C   1 
ATOM   373  O O   . THR A 1 53  ? -87.285  -39.413 3.335   1.00 125.72 ? 79   THR A O   1 
ATOM   374  C CB  . THR A 1 53  ? -86.522  -42.362 4.732   1.00 130.63 ? 79   THR A CB  1 
ATOM   375  O OG1 . THR A 1 53  ? -86.787  -43.299 3.689   1.00 132.99 ? 79   THR A OG1 1 
ATOM   376  C CG2 . THR A 1 53  ? -87.827  -41.961 5.442   1.00 123.09 ? 79   THR A CG2 1 
ATOM   377  N N   . ASN A 1 54  ? -86.826  -41.135 1.943   1.00 126.61 ? 80   ASN A N   1 
ATOM   378  C CA  . ASN A 1 54  ? -87.718  -40.663 0.865   1.00 118.63 ? 80   ASN A CA  1 
ATOM   379  C C   . ASN A 1 54  ? -89.062  -40.254 1.422   1.00 117.65 ? 80   ASN A C   1 
ATOM   380  O O   . ASN A 1 54  ? -89.670  -39.276 0.978   1.00 115.18 ? 80   ASN A O   1 
ATOM   381  C CB  . ASN A 1 54  ? -87.880  -41.724 -0.228  1.00 115.08 ? 80   ASN A CB  1 
ATOM   382  C CG  . ASN A 1 54  ? -86.997  -41.467 -1.430  1.00 120.39 ? 80   ASN A CG  1 
ATOM   383  O OD1 . ASN A 1 54  ? -86.208  -42.314 -1.848  1.00 119.45 ? 80   ASN A OD1 1 
ATOM   384  N ND2 . ASN A 1 54  ? -87.150  -40.279 -2.009  1.00 120.82 ? 80   ASN A ND2 1 
ATOM   385  N N   . GLU A 1 55  ? -89.554  -41.067 2.343   1.00 114.52 ? 81   GLU A N   1 
ATOM   386  C CA  . GLU A 1 55  ? -90.797  -40.789 3.024   1.00 138.24 ? 81   GLU A CA  1 
ATOM   387  C C   . GLU A 1 55  ? -90.685  -39.415 3.664   1.00 133.12 ? 81   GLU A C   1 
ATOM   388  O O   . GLU A 1 55  ? -91.539  -38.555 3.464   1.00 128.51 ? 81   GLU A O   1 
ATOM   389  C CB  . GLU A 1 55  ? -90.996  -41.812 4.159   1.00 160.44 ? 81   GLU A CB  1 
ATOM   390  C CG  . GLU A 1 55  ? -91.942  -41.341 5.267   1.00 159.27 ? 81   GLU A CG  1 
ATOM   391  C CD  . GLU A 1 55  ? -91.742  -42.096 6.586   1.00 145.60 ? 81   GLU A CD  1 
ATOM   392  O OE1 . GLU A 1 55  ? -91.413  -43.309 6.554   1.00 133.59 ? 81   GLU A OE1 1 
ATOM   393  O OE2 . GLU A 1 55  ? -91.927  -41.469 7.667   1.00 115.08 ? 81   GLU A OE2 1 
ATOM   394  N N   . SER A 1 56  ? -89.573  -39.219 4.381   1.00 134.18 ? 82   SER A N   1 
ATOM   395  C CA  . SER A 1 56  ? -89.275  -37.996 5.144   1.00 114.10 ? 82   SER A CA  1 
ATOM   396  C C   . SER A 1 56  ? -89.811  -36.680 4.581   1.00 106.31 ? 82   SER A C   1 
ATOM   397  O O   . SER A 1 56  ? -90.535  -35.957 5.277   1.00 87.38  ? 82   SER A O   1 
ATOM   398  C CB  . SER A 1 56  ? -87.771  -37.893 5.417   1.00 109.49 ? 82   SER A CB  1 
ATOM   399  O OG  . SER A 1 56  ? -87.289  -39.049 6.098   1.00 94.72  ? 82   SER A OG  1 
ATOM   400  N N   . PHE A 1 57  ? -89.445  -36.348 3.349   1.00 105.00 ? 83   PHE A N   1 
ATOM   401  C CA  . PHE A 1 57  ? -89.915  -35.102 2.742   1.00 118.94 ? 83   PHE A CA  1 
ATOM   402  C C   . PHE A 1 57  ? -90.672  -35.397 1.462   1.00 135.20 ? 83   PHE A C   1 
ATOM   403  O O   . PHE A 1 57  ? -90.070  -35.711 0.427   1.00 130.56 ? 83   PHE A O   1 
ATOM   404  C CB  . PHE A 1 57  ? -88.746  -34.137 2.478   1.00 121.26 ? 83   PHE A CB  1 
ATOM   405  C CG  . PHE A 1 57  ? -87.955  -33.803 3.717   1.00 115.02 ? 83   PHE A CG  1 
ATOM   406  C CD1 . PHE A 1 57  ? -88.393  -32.805 4.598   1.00 109.70 ? 83   PHE A CD1 1 
ATOM   407  C CD2 . PHE A 1 57  ? -86.787  -34.505 4.022   1.00 100.77 ? 83   PHE A CD2 1 
ATOM   408  C CE1 . PHE A 1 57  ? -87.696  -32.541 5.770   1.00 96.95  ? 83   PHE A CE1 1 
ATOM   409  C CE2 . PHE A 1 57  ? -86.087  -34.246 5.189   1.00 94.36  ? 83   PHE A CE2 1 
ATOM   410  C CZ  . PHE A 1 57  ? -86.544  -33.265 6.064   1.00 104.29 ? 83   PHE A CZ  1 
ATOM   411  N N   . GLN A 1 58  ? -92.001  -35.322 1.549   1.00 145.45 ? 84   GLN A N   1 
ATOM   412  C CA  . GLN A 1 58  ? -92.859  -35.583 0.401   1.00 139.55 ? 84   GLN A CA  1 
ATOM   413  C C   . GLN A 1 58  ? -93.403  -34.374 -0.317  1.00 140.67 ? 84   GLN A C   1 
ATOM   414  O O   . GLN A 1 58  ? -94.227  -33.625 0.226   1.00 111.67 ? 84   GLN A O   1 
ATOM   415  C CB  . GLN A 1 58  ? -94.041  -36.453 0.774   1.00 137.32 ? 84   GLN A CB  1 
ATOM   416  C CG  . GLN A 1 58  ? -93.659  -37.857 1.171   1.00 144.06 ? 84   GLN A CG  1 
ATOM   417  C CD  . GLN A 1 58  ? -94.840  -38.801 1.120   1.00 134.70 ? 84   GLN A CD  1 
ATOM   418  O OE1 . GLN A 1 58  ? -94.661  -40.020 1.082   1.00 113.67 ? 84   GLN A OE1 1 
ATOM   419  N NE2 . GLN A 1 58  ? -96.044  -38.247 0.978   1.00 131.73 ? 84   GLN A NE2 1 
ATOM   420  N N   . GLY A 1 59  ? -92.971  -34.223 -1.565  1.00 146.26 ? 85   GLY A N   1 
ATOM   421  C CA  . GLY A 1 59  ? -93.417  -33.137 -2.408  1.00 142.33 ? 85   GLY A CA  1 
ATOM   422  C C   . GLY A 1 59  ? -93.536  -31.811 -1.693  1.00 151.48 ? 85   GLY A C   1 
ATOM   423  O O   . GLY A 1 59  ? -94.589  -31.169 -1.750  1.00 138.38 ? 85   GLY A O   1 
ATOM   424  N N   . LEU A 1 60  ? -92.557  -31.499 -0.859  1.00 157.20 ? 86   LEU A N   1 
ATOM   425  C CA  . LEU A 1 60  ? -92.483  -30.178 -0.272  1.00 145.46 ? 86   LEU A CA  1 
ATOM   426  C C   . LEU A 1 60  ? -92.135  -29.165 -1.349  1.00 146.59 ? 86   LEU A C   1 
ATOM   427  O O   . LEU A 1 60  ? -92.678  -28.067 -1.397  1.00 124.31 ? 86   LEU A O   1 
ATOM   428  C CB  . LEU A 1 60  ? -91.489  -30.163 0.874   1.00 135.11 ? 86   LEU A CB  1 
ATOM   429  C CG  . LEU A 1 60  ? -91.877  -31.085 2.031   1.00 130.93 ? 86   LEU A CG  1 
ATOM   430  C CD1 . LEU A 1 60  ? -93.186  -30.637 2.653   1.00 115.76 ? 86   LEU A CD1 1 
ATOM   431  C CD2 . LEU A 1 60  ? -91.949  -32.539 1.589   1.00 129.41 ? 86   LEU A CD2 1 
ATOM   432  N N   . GLN A 1 61  ? -91.187  -29.539 -2.197  1.00 140.37 ? 87   GLN A N   1 
ATOM   433  C CA  . GLN A 1 61  ? -90.944  -28.833 -3.437  1.00 143.06 ? 87   GLN A CA  1 
ATOM   434  C C   . GLN A 1 61  ? -90.434  -27.450 -3.132  1.00 136.62 ? 87   GLN A C   1 
ATOM   435  O O   . GLN A 1 61  ? -89.352  -27.060 -3.535  1.00 130.30 ? 87   GLN A O   1 
ATOM   436  C CB  . GLN A 1 61  ? -92.210  -28.762 -4.279  1.00 154.30 ? 87   GLN A CB  1 
ATOM   437  C CG  . GLN A 1 61  ? -93.194  -29.890 -4.013  1.00 167.28 ? 87   GLN A CG  1 
ATOM   438  C CD  . GLN A 1 61  ? -94.500  -29.721 -4.768  1.00 164.29 ? 87   GLN A CD  1 
ATOM   439  O OE1 . GLN A 1 61  ? -95.151  -28.677 -4.687  1.00 150.23 ? 87   GLN A OE1 1 
ATOM   440  N NE2 . GLN A 1 61  ? -94.890  -30.753 -5.510  1.00 161.61 ? 87   GLN A NE2 1 
ATOM   441  N N   . ASN A 1 62  ? -91.253  -26.714 -2.404  1.00 130.01 ? 88   ASN A N   1 
ATOM   442  C CA  . ASN A 1 62  ? -90.997  -25.324 -2.096  1.00 127.56 ? 88   ASN A CA  1 
ATOM   443  C C   . ASN A 1 62  ? -89.754  -25.073 -1.267  1.00 125.02 ? 88   ASN A C   1 
ATOM   444  O O   . ASN A 1 62  ? -89.095  -24.066 -1.433  1.00 122.01 ? 88   ASN A O   1 
ATOM   445  C CB  . ASN A 1 62  ? -92.219  -24.702 -1.434  1.00 125.55 ? 88   ASN A CB  1 
ATOM   446  C CG  . ASN A 1 62  ? -93.266  -24.260 -2.436  1.00 126.00 ? 88   ASN A CG  1 
ATOM   447  O OD1 . ASN A 1 62  ? -94.376  -23.906 -2.059  1.00 130.82 ? 88   ASN A OD1 1 
ATOM   448  N ND2 . ASN A 1 62  ? -92.919  -24.273 -3.717  1.00 117.43 ? 88   ASN A ND2 1 
ATOM   449  N N   . LEU A 1 63  ? -89.475  -25.970 -0.338  1.00 122.26 ? 89   LEU A N   1 
ATOM   450  C CA  . LEU A 1 63  ? -88.364  -25.814 0.597   1.00 117.96 ? 89   LEU A CA  1 
ATOM   451  C C   . LEU A 1 63  ? -86.989  -25.551 0.007   1.00 117.55 ? 89   LEU A C   1 
ATOM   452  O O   . LEU A 1 63  ? -86.428  -26.373 -0.734  1.00 96.01  ? 89   LEU A O   1 
ATOM   453  C CB  . LEU A 1 63  ? -88.245  -26.993 1.552   1.00 109.73 ? 89   LEU A CB  1 
ATOM   454  C CG  . LEU A 1 63  ? -89.462  -27.311 2.407   1.00 105.01 ? 89   LEU A CG  1 
ATOM   455  C CD1 . LEU A 1 63  ? -88.958  -28.162 3.560   1.00 97.25  ? 89   LEU A CD1 1 
ATOM   456  C CD2 . LEU A 1 63  ? -90.131  -26.059 2.956   1.00 99.58  ? 89   LEU A CD2 1 
ATOM   457  N N   . THR A 1 64  ? -86.405  -24.460 0.497   1.00 112.38 ? 90   THR A N   1 
ATOM   458  C CA  . THR A 1 64  ? -85.094  -24.001 0.097   1.00 106.27 ? 90   THR A CA  1 
ATOM   459  C C   . THR A 1 64  ? -84.028  -24.315 1.155   1.00 107.44 ? 90   THR A C   1 
ATOM   460  O O   . THR A 1 64  ? -82.876  -24.599 0.806   1.00 100.36 ? 90   THR A O   1 
ATOM   461  C CB  . THR A 1 64  ? -85.121  -22.490 -0.170  1.00 98.77  ? 90   THR A CB  1 
ATOM   462  O OG1 . THR A 1 64  ? -85.640  -21.820 0.979   1.00 97.46  ? 90   THR A OG1 1 
ATOM   463  C CG2 . THR A 1 64  ? -86.013  -22.164 -1.359  1.00 94.99  ? 90   THR A CG2 1 
ATOM   464  N N   . LYS A 1 65  ? -84.412  -24.268 2.434   1.00 101.21 ? 91   LYS A N   1 
ATOM   465  C CA  . LYS A 1 65  ? -83.482  -24.542 3.542   1.00 110.39 ? 91   LYS A CA  1 
ATOM   466  C C   . LYS A 1 65  ? -83.995  -25.589 4.531   1.00 105.26 ? 91   LYS A C   1 
ATOM   467  O O   . LYS A 1 65  ? -85.166  -25.576 4.915   1.00 86.83  ? 91   LYS A O   1 
ATOM   468  C CB  . LYS A 1 65  ? -83.180  -23.269 4.361   1.00 125.73 ? 91   LYS A CB  1 
ATOM   469  C CG  . LYS A 1 65  ? -82.369  -22.149 3.709   1.00 151.12 ? 91   LYS A CG  1 
ATOM   470  C CD  . LYS A 1 65  ? -82.996  -21.458 2.506   1.00 151.43 ? 91   LYS A CD  1 
ATOM   471  C CE  . LYS A 1 65  ? -82.062  -20.364 1.997   1.00 132.35 ? 91   LYS A CE  1 
ATOM   472  N NZ  . LYS A 1 65  ? -82.580  -19.674 0.791   1.00 139.26 ? 91   LYS A NZ  1 
ATOM   473  N N   . ILE A 1 66  ? -83.075  -26.422 5.023   1.00 111.15 ? 92   ILE A N   1 
ATOM   474  C CA  . ILE A 1 66  ? -83.402  -27.458 6.005   1.00 111.49 ? 92   ILE A CA  1 
ATOM   475  C C   . ILE A 1 66  ? -82.295  -27.600 7.040   1.00 101.41 ? 92   ILE A C   1 
ATOM   476  O O   . ILE A 1 66  ? -81.130  -27.842 6.689   1.00 90.23  ? 92   ILE A O   1 
ATOM   477  C CB  . ILE A 1 66  ? -83.573  -28.844 5.367   1.00 129.80 ? 92   ILE A CB  1 
ATOM   478  C CG1 . ILE A 1 66  ? -84.690  -28.829 4.322   1.00 140.31 ? 92   ILE A CG1 1 
ATOM   479  C CG2 . ILE A 1 66  ? -83.899  -29.863 6.451   1.00 129.99 ? 92   ILE A CG2 1 
ATOM   480  C CD1 . ILE A 1 66  ? -84.846  -30.142 3.581   1.00 136.79 ? 92   ILE A CD1 1 
ATOM   481  N N   . ASN A 1 67  ? -82.685  -27.536 8.314   1.00 84.47  ? 93   ASN A N   1 
ATOM   482  C CA  . ASN A 1 67  ? -81.752  -27.666 9.420   1.00 77.80  ? 93   ASN A CA  1 
ATOM   483  C C   . ASN A 1 67  ? -82.078  -28.928 10.250  1.00 90.27  ? 93   ASN A C   1 
ATOM   484  O O   . ASN A 1 67  ? -83.137  -29.018 10.889  1.00 84.22  ? 93   ASN A O   1 
ATOM   485  C CB  . ASN A 1 67  ? -81.846  -26.412 10.301  1.00 79.61  ? 93   ASN A CB  1 
ATOM   486  C CG  . ASN A 1 67  ? -80.756  -26.339 11.386  1.00 80.52  ? 93   ASN A CG  1 
ATOM   487  O OD1 . ASN A 1 67  ? -79.908  -27.237 11.541  1.00 75.75  ? 93   ASN A OD1 1 
ATOM   488  N ND2 . ASN A 1 67  ? -80.775  -25.242 12.139  1.00 73.57  ? 93   ASN A ND2 1 
ATOM   489  N N   . LEU A 1 68  ? -81.150  -29.879 10.255  1.00 85.87  ? 94   LEU A N   1 
ATOM   490  C CA  . LEU A 1 68  ? -81.302  -31.138 10.996  1.00 99.91  ? 94   LEU A CA  1 
ATOM   491  C C   . LEU A 1 68  ? -80.131  -31.348 11.959  1.00 107.16 ? 94   LEU A C   1 
ATOM   492  O O   . LEU A 1 68  ? -79.729  -32.483 12.241  1.00 105.44 ? 94   LEU A O   1 
ATOM   493  C CB  . LEU A 1 68  ? -81.321  -32.303 10.003  1.00 109.10 ? 94   LEU A CB  1 
ATOM   494  C CG  . LEU A 1 68  ? -82.478  -32.328 9.006   1.00 116.99 ? 94   LEU A CG  1 
ATOM   495  C CD1 . LEU A 1 68  ? -82.194  -33.296 7.870   1.00 113.15 ? 94   LEU A CD1 1 
ATOM   496  C CD2 . LEU A 1 68  ? -83.792  -32.650 9.708   1.00 120.27 ? 94   LEU A CD2 1 
ATOM   497  N N   . ASN A 1 69  ? -79.577  -30.263 12.468  1.00 102.74 ? 95   ASN A N   1 
ATOM   498  C CA  . ASN A 1 69  ? -78.444  -30.376 13.357  1.00 94.49  ? 95   ASN A CA  1 
ATOM   499  C C   . ASN A 1 69  ? -78.830  -30.886 14.721  1.00 93.74  ? 95   ASN A C   1 
ATOM   500  O O   . ASN A 1 69  ? -79.966  -30.717 15.168  1.00 86.49  ? 95   ASN A O   1 
ATOM   501  C CB  . ASN A 1 69  ? -77.741  -29.033 13.462  1.00 94.87  ? 95   ASN A CB  1 
ATOM   502  C CG  . ASN A 1 69  ? -77.195  -28.569 12.134  1.00 90.81  ? 95   ASN A CG  1 
ATOM   503  O OD1 . ASN A 1 69  ? -76.785  -29.378 11.296  1.00 89.88  ? 95   ASN A OD1 1 
ATOM   504  N ND2 . ASN A 1 69  ? -77.166  -27.268 11.941  1.00 82.24  ? 95   ASN A ND2 1 
ATOM   505  N N   . HIS A 1 70  ? -77.870  -31.539 15.363  1.00 87.89  ? 96   HIS A N   1 
ATOM   506  C CA  . HIS A 1 70  ? -78.057  -32.095 16.684  1.00 100.80 ? 96   HIS A CA  1 
ATOM   507  C C   . HIS A 1 70  ? -79.195  -33.118 16.687  1.00 100.26 ? 96   HIS A C   1 
ATOM   508  O O   . HIS A 1 70  ? -80.225  -32.895 17.315  1.00 91.14  ? 96   HIS A O   1 
ATOM   509  C CB  . HIS A 1 70  ? -78.344  -30.998 17.726  1.00 105.20 ? 96   HIS A CB  1 
ATOM   510  C CG  . HIS A 1 70  ? -77.328  -29.895 17.755  1.00 117.14 ? 96   HIS A CG  1 
ATOM   511  N ND1 . HIS A 1 70  ? -76.101  -30.027 18.371  1.00 122.70 ? 96   HIS A ND1 1 
ATOM   512  C CD2 . HIS A 1 70  ? -77.405  -28.605 17.347  1.00 110.76 ? 96   HIS A CD2 1 
ATOM   513  C CE1 . HIS A 1 70  ? -75.434  -28.892 18.265  1.00 113.68 ? 96   HIS A CE1 1 
ATOM   514  N NE2 . HIS A 1 70  ? -76.209  -28.009 17.659  1.00 110.86 ? 96   HIS A NE2 1 
ATOM   515  N N   . ASN A 1 71  ? -79.047  -34.170 15.883  1.00 101.10 ? 97   ASN A N   1 
ATOM   516  C CA  . ASN A 1 71  ? -80.025  -35.267 15.811  1.00 99.35  ? 97   ASN A CA  1 
ATOM   517  C C   . ASN A 1 71  ? -79.314  -36.604 15.813  1.00 106.23 ? 97   ASN A C   1 
ATOM   518  O O   . ASN A 1 71  ? -78.543  -36.895 14.902  1.00 119.21 ? 97   ASN A O   1 
ATOM   519  C CB  . ASN A 1 71  ? -80.957  -35.172 14.603  1.00 87.84  ? 97   ASN A CB  1 
ATOM   520  C CG  . ASN A 1 71  ? -82.035  -34.121 14.778  1.00 89.96  ? 97   ASN A CG  1 
ATOM   521  O OD1 . ASN A 1 71  ? -82.084  -33.430 15.783  1.00 99.52  ? 97   ASN A OD1 1 
ATOM   522  N ND2 . ASN A 1 71  ? -82.944  -34.046 13.825  1.00 101.32 ? 97   ASN A ND2 1 
ATOM   523  N N   . PRO A 1 72  ? -79.538  -37.408 16.851  1.00 118.22 ? 98   PRO A N   1 
ATOM   524  C CA  . PRO A 1 72  ? -80.421  -37.068 17.964  1.00 102.15 ? 98   PRO A CA  1 
ATOM   525  C C   . PRO A 1 72  ? -79.625  -36.682 19.203  1.00 108.84 ? 98   PRO A C   1 
ATOM   526  O O   . PRO A 1 72  ? -78.448  -37.038 19.304  1.00 122.49 ? 98   PRO A O   1 
ATOM   527  C CB  . PRO A 1 72  ? -81.131  -38.380 18.217  1.00 111.70 ? 98   PRO A CB  1 
ATOM   528  C CG  . PRO A 1 72  ? -80.077  -39.405 17.941  1.00 109.63 ? 98   PRO A CG  1 
ATOM   529  C CD  . PRO A 1 72  ? -79.256  -38.855 16.807  1.00 117.06 ? 98   PRO A CD  1 
ATOM   530  N N   . ASN A 1 73  ? -80.276  -36.042 20.173  1.00 114.27 ? 99   ASN A N   1 
ATOM   531  C CA  . ASN A 1 73  ? -79.596  -35.622 21.412  1.00 123.49 ? 99   ASN A CA  1 
ATOM   532  C C   . ASN A 1 73  ? -79.371  -36.769 22.408  1.00 131.86 ? 99   ASN A C   1 
ATOM   533  O O   . ASN A 1 73  ? -80.158  -36.962 23.338  1.00 133.75 ? 99   ASN A O   1 
ATOM   534  C CB  . ASN A 1 73  ? -80.383  -34.493 22.084  1.00 123.62 ? 99   ASN A CB  1 
ATOM   535  C CG  . ASN A 1 73  ? -80.528  -33.267 21.196  1.00 121.94 ? 99   ASN A CG  1 
ATOM   536  O OD1 . ASN A 1 73  ? -81.401  -32.430 21.420  1.00 106.47 ? 99   ASN A OD1 1 
ATOM   537  N ND2 . ASN A 1 73  ? -79.716  -33.184 20.150  1.00 126.96 ? 99   ASN A ND2 1 
ATOM   538  N N   . VAL A 1 74  ? -78.282  -37.515 22.215  1.00 138.11 ? 100  VAL A N   1 
ATOM   539  C CA  . VAL A 1 74  ? -77.945  -38.642 23.097  1.00 145.42 ? 100  VAL A CA  1 
ATOM   540  C C   . VAL A 1 74  ? -77.275  -38.136 24.373  1.00 138.49 ? 100  VAL A C   1 
ATOM   541  O O   . VAL A 1 74  ? -77.865  -37.366 25.128  1.00 117.50 ? 100  VAL A O   1 
ATOM   542  C CB  . VAL A 1 74  ? -77.025  -39.684 22.400  1.00 139.91 ? 100  VAL A CB  1 
ATOM   543  C CG1 . VAL A 1 74  ? -75.690  -39.067 21.992  1.00 133.86 ? 100  VAL A CG1 1 
ATOM   544  C CG2 . VAL A 1 74  ? -76.812  -40.899 23.300  1.00 132.83 ? 100  VAL A CG2 1 
ATOM   545  N N   . GLY A 1 87  ? -76.084  -41.729 16.197  1.00 107.22 ? 113  GLY A N   1 
ATOM   546  C CA  . GLY A 1 87  ? -75.983  -41.434 14.769  1.00 101.93 ? 113  GLY A CA  1 
ATOM   547  C C   . GLY A 1 87  ? -77.312  -41.074 14.129  1.00 108.73 ? 113  GLY A C   1 
ATOM   548  O O   . GLY A 1 87  ? -78.347  -41.069 14.793  1.00 115.26 ? 113  GLY A O   1 
ATOM   549  N N   . LEU A 1 88  ? -77.260  -40.699 12.850  1.00 105.82 ? 114  LEU A N   1 
ATOM   550  C CA  . LEU A 1 88  ? -78.454  -40.339 12.071  1.00 98.01  ? 114  LEU A CA  1 
ATOM   551  C C   . LEU A 1 88  ? -78.399  -41.133 10.791  1.00 98.89  ? 114  LEU A C   1 
ATOM   552  O O   . LEU A 1 88  ? -77.352  -41.189 10.143  1.00 79.68  ? 114  LEU A O   1 
ATOM   553  C CB  . LEU A 1 88  ? -78.485  -38.847 11.727  1.00 101.38 ? 114  LEU A CB  1 
ATOM   554  C CG  . LEU A 1 88  ? -79.665  -38.372 10.857  1.00 101.45 ? 114  LEU A CG  1 
ATOM   555  C CD1 . LEU A 1 88  ? -81.005  -38.591 11.539  1.00 96.16  ? 114  LEU A CD1 1 
ATOM   556  C CD2 . LEU A 1 88  ? -79.520  -36.904 10.502  1.00 101.82 ? 114  LEU A CD2 1 
ATOM   557  N N   . ASN A 1 89  ? -79.526  -41.744 10.431  1.00 112.21 ? 115  ASN A N   1 
ATOM   558  C CA  . ASN A 1 89  ? -79.623  -42.560 9.226   1.00 114.90 ? 115  ASN A CA  1 
ATOM   559  C C   . ASN A 1 89  ? -80.288  -41.787 8.106   1.00 106.76 ? 115  ASN A C   1 
ATOM   560  O O   . ASN A 1 89  ? -81.413  -41.309 8.261   1.00 96.80  ? 115  ASN A O   1 
ATOM   561  C CB  . ASN A 1 89  ? -80.413  -43.842 9.531   1.00 123.92 ? 115  ASN A CB  1 
ATOM   562  C CG  . ASN A 1 89  ? -80.587  -44.741 8.312   1.00 132.00 ? 115  ASN A CG  1 
ATOM   563  O OD1 . ASN A 1 89  ? -80.244  -44.366 7.196   1.00 130.47 ? 115  ASN A OD1 1 
ATOM   564  N ND2 . ASN A 1 89  ? -81.152  -45.927 8.523   1.00 141.50 ? 115  ASN A ND2 1 
ATOM   565  N N   . ILE A 1 90  ? -79.602  -41.705 6.965   1.00 104.95 ? 116  ILE A N   1 
ATOM   566  C CA  . ILE A 1 90  ? -80.115  -40.987 5.801   1.00 114.95 ? 116  ILE A CA  1 
ATOM   567  C C   . ILE A 1 90  ? -80.155  -41.836 4.522   1.00 123.14 ? 116  ILE A C   1 
ATOM   568  O O   . ILE A 1 90  ? -79.147  -42.424 4.099   1.00 101.53 ? 116  ILE A O   1 
ATOM   569  C CB  . ILE A 1 90  ? -79.284  -39.718 5.533   1.00 119.26 ? 116  ILE A CB  1 
ATOM   570  C CG1 . ILE A 1 90  ? -79.346  -38.797 6.756   1.00 123.84 ? 116  ILE A CG1 1 
ATOM   571  C CG2 . ILE A 1 90  ? -79.803  -38.993 4.294   1.00 118.98 ? 116  ILE A CG2 1 
ATOM   572  C CD1 . ILE A 1 90  ? -78.493  -37.554 6.650   1.00 120.99 ? 116  ILE A CD1 1 
ATOM   573  N N   . THR A 1 91  ? -81.317  -41.820 3.873   1.00 130.20 ? 117  THR A N   1 
ATOM   574  C CA  . THR A 1 91  ? -81.542  -42.568 2.630   1.00 131.22 ? 117  THR A CA  1 
ATOM   575  C C   . THR A 1 91  ? -81.070  -41.830 1.374   1.00 129.95 ? 117  THR A C   1 
ATOM   576  O O   . THR A 1 91  ? -81.475  -40.695 1.091   1.00 101.39 ? 117  THR A O   1 
ATOM   577  C CB  . THR A 1 91  ? -83.013  -43.004 2.491   1.00 128.65 ? 117  THR A CB  1 
ATOM   578  O OG1 . THR A 1 91  ? -83.291  -43.356 1.127   1.00 140.87 ? 117  THR A OG1 1 
ATOM   579  C CG2 . THR A 1 91  ? -83.898  -41.911 2.854   1.00 128.03 ? 117  THR A CG2 1 
ATOM   580  N N   . ASP A 1 92  ? -80.252  -42.534 0.597   1.00 119.70 ? 118  ASP A N   1 
ATOM   581  C CA  . ASP A 1 92  ? -79.671  -42.009 -0.639  1.00 112.08 ? 118  ASP A CA  1 
ATOM   582  C C   . ASP A 1 92  ? -80.736  -41.400 -1.517  1.00 108.81 ? 118  ASP A C   1 
ATOM   583  O O   . ASP A 1 92  ? -81.752  -42.023 -1.776  1.00 134.27 ? 118  ASP A O   1 
ATOM   584  C CB  . ASP A 1 92  ? -78.971  -43.129 -1.378  1.00 97.49  ? 118  ASP A CB  1 
ATOM   585  C CG  . ASP A 1 92  ? -78.075  -43.942 -0.457  1.00 113.76 ? 118  ASP A CG  1 
ATOM   586  O OD1 . ASP A 1 92  ? -78.332  -43.907 0.775   1.00 105.78 ? 118  ASP A OD1 1 
ATOM   587  O OD2 . ASP A 1 92  ? -77.188  -44.675 -0.954  1.00 98.64  ? 118  ASP A OD2 1 
ATOM   588  N N   . GLY A 1 93  ? -80.498  -40.178 -1.974  1.00 102.80 ? 119  GLY A N   1 
ATOM   589  C CA  . GLY A 1 93  ? -81.464  -39.475 -2.809  1.00 107.86 ? 119  GLY A CA  1 
ATOM   590  C C   . GLY A 1 93  ? -82.662  -38.969 -2.003  1.00 116.52 ? 119  GLY A C   1 
ATOM   591  O O   . GLY A 1 93  ? -83.646  -38.499 -2.573  1.00 129.30 ? 119  GLY A O   1 
ATOM   592  N N   . ALA A 1 94  ? -82.548  -38.991 -0.677  1.00 103.82 ? 120  ALA A N   1 
ATOM   593  C CA  . ALA A 1 94  ? -83.630  -38.553 0.206   1.00 102.98 ? 120  ALA A CA  1 
ATOM   594  C C   . ALA A 1 94  ? -84.168  -37.152 -0.034  1.00 110.49 ? 120  ALA A C   1 
ATOM   595  O O   . ALA A 1 94  ? -85.357  -36.907 0.153   1.00 129.58 ? 120  ALA A O   1 
ATOM   596  C CB  . ALA A 1 94  ? -83.180  -38.648 1.648   1.00 114.95 ? 120  ALA A CB  1 
ATOM   597  N N   . PHE A 1 95  ? -83.301  -36.226 -0.423  1.00 114.36 ? 121  PHE A N   1 
ATOM   598  C CA  . PHE A 1 95  ? -83.725  -34.836 -0.619  1.00 110.40 ? 121  PHE A CA  1 
ATOM   599  C C   . PHE A 1 95  ? -84.045  -34.434 -2.060  1.00 111.70 ? 121  PHE A C   1 
ATOM   600  O O   . PHE A 1 95  ? -84.679  -33.398 -2.288  1.00 114.40 ? 121  PHE A O   1 
ATOM   601  C CB  . PHE A 1 95  ? -82.635  -33.895 -0.081  1.00 106.62 ? 121  PHE A CB  1 
ATOM   602  C CG  . PHE A 1 95  ? -82.241  -34.161 1.355   1.00 79.45  ? 121  PHE A CG  1 
ATOM   603  C CD1 . PHE A 1 95  ? -82.970  -33.621 2.397   1.00 74.41  ? 121  PHE A CD1 1 
ATOM   604  C CD2 . PHE A 1 95  ? -81.087  -34.877 1.652   1.00 73.20  ? 121  PHE A CD2 1 
ATOM   605  C CE1 . PHE A 1 95  ? -82.602  -33.857 3.719   1.00 78.17  ? 121  PHE A CE1 1 
ATOM   606  C CE2 . PHE A 1 95  ? -80.702  -35.101 2.967   1.00 76.27  ? 121  PHE A CE2 1 
ATOM   607  C CZ  . PHE A 1 95  ? -81.461  -34.588 4.004   1.00 71.82  ? 121  PHE A CZ  1 
ATOM   608  N N   . LEU A 1 96  ? -83.675  -35.276 -3.018  1.00 104.87 ? 122  LEU A N   1 
ATOM   609  C CA  . LEU A 1 96  ? -83.892  -34.980 -4.451  1.00 104.90 ? 122  LEU A CA  1 
ATOM   610  C C   . LEU A 1 96  ? -85.308  -34.535 -4.807  1.00 105.56 ? 122  LEU A C   1 
ATOM   611  O O   . LEU A 1 96  ? -85.497  -33.762 -5.740  1.00 105.68 ? 122  LEU A O   1 
ATOM   612  C CB  . LEU A 1 96  ? -83.464  -36.169 -5.305  1.00 93.09  ? 122  LEU A CB  1 
ATOM   613  C CG  . LEU A 1 96  ? -81.952  -36.445 -5.318  1.00 105.95 ? 122  LEU A CG  1 
ATOM   614  C CD1 . LEU A 1 96  ? -81.264  -36.218 -3.972  1.00 109.45 ? 122  LEU A CD1 1 
ATOM   615  C CD2 . LEU A 1 96  ? -81.674  -37.843 -5.857  1.00 97.30  ? 122  LEU A CD2 1 
ATOM   616  N N   . ASN A 1 97  ? -86.299  -35.005 -4.060  1.00 124.64 ? 123  ASN A N   1 
ATOM   617  C CA  . ASN A 1 97  ? -87.682  -34.619 -4.323  1.00 143.45 ? 123  ASN A CA  1 
ATOM   618  C C   . ASN A 1 97  ? -87.813  -33.095 -4.223  1.00 142.15 ? 123  ASN A C   1 
ATOM   619  O O   . ASN A 1 97  ? -88.756  -32.498 -4.764  1.00 116.04 ? 123  ASN A O   1 
ATOM   620  C CB  . ASN A 1 97  ? -88.634  -35.306 -3.320  1.00 154.80 ? 123  ASN A CB  1 
ATOM   621  C CG  . ASN A 1 97  ? -90.113  -34.993 -3.575  1.00 159.87 ? 123  ASN A CG  1 
ATOM   622  O OD1 . ASN A 1 97  ? -90.982  -35.454 -2.834  1.00 150.01 ? 123  ASN A OD1 1 
ATOM   623  N ND2 . ASN A 1 97  ? -90.404  -34.222 -4.620  1.00 165.64 ? 123  ASN A ND2 1 
ATOM   624  N N   . LEU A 1 98  ? -86.867  -32.469 -3.525  1.00 146.18 ? 124  LEU A N   1 
ATOM   625  C CA  . LEU A 1 98  ? -86.887  -31.030 -3.352  1.00 142.01 ? 124  LEU A CA  1 
ATOM   626  C C   . LEU A 1 98  ? -85.751  -30.517 -4.226  1.00 136.07 ? 124  LEU A C   1 
ATOM   627  O O   . LEU A 1 98  ? -84.581  -30.824 -3.984  1.00 132.92 ? 124  LEU A O   1 
ATOM   628  C CB  . LEU A 1 98  ? -86.580  -30.661 -1.906  1.00 133.43 ? 124  LEU A CB  1 
ATOM   629  C CG  . LEU A 1 98  ? -86.968  -31.672 -0.818  1.00 137.50 ? 124  LEU A CG  1 
ATOM   630  C CD1 . LEU A 1 98  ? -86.795  -31.056 0.559   1.00 139.80 ? 124  LEU A CD1 1 
ATOM   631  C CD2 . LEU A 1 98  ? -88.338  -32.316 -0.974  1.00 151.11 ? 124  LEU A CD2 1 
ATOM   632  N N   . LYS A 1 99  ? -86.094  -29.816 -5.290  1.00 126.12 ? 125  LYS A N   1 
ATOM   633  C CA  . LYS A 1 99  ? -85.093  -29.271 -6.186  1.00 136.35 ? 125  LYS A CA  1 
ATOM   634  C C   . LYS A 1 99  ? -85.013  -27.737 -6.058  1.00 127.57 ? 125  LYS A C   1 
ATOM   635  O O   . LYS A 1 99  ? -84.509  -27.042 -6.935  1.00 112.60 ? 125  LYS A O   1 
ATOM   636  C CB  . LYS A 1 99  ? -85.316  -29.773 -7.621  1.00 142.71 ? 125  LYS A CB  1 
ATOM   637  C CG  . LYS A 1 99  ? -84.671  -28.905 -8.689  1.00 155.26 ? 125  LYS A CG  1 
ATOM   638  C CD  . LYS A 1 99  ? -83.158  -28.783 -8.629  1.00 139.57 ? 125  LYS A CD  1 
ATOM   639  C CE  . LYS A 1 99  ? -82.731  -27.496 -9.343  1.00 135.36 ? 125  LYS A CE  1 
ATOM   640  N NZ  . LYS A 1 99  ? -83.382  -27.281 -10.669 1.00 126.70 ? 125  LYS A NZ  1 
ATOM   641  N N   . ASN A 1 100 ? -85.570  -27.217 -4.973  1.00 127.74 ? 126  ASN A N   1 
ATOM   642  C CA  . ASN A 1 100 ? -85.504  -25.791 -4.685  1.00 125.49 ? 126  ASN A CA  1 
ATOM   643  C C   . ASN A 1 100 ? -84.788  -25.682 -3.365  1.00 124.70 ? 126  ASN A C   1 
ATOM   644  O O   . ASN A 1 100 ? -84.881  -24.673 -2.672  1.00 114.84 ? 126  ASN A O   1 
ATOM   645  C CB  . ASN A 1 100 ? -86.882  -25.162 -4.592  1.00 120.59 ? 126  ASN A CB  1 
ATOM   646  C CG  . ASN A 1 100 ? -87.630  -25.251 -5.885  1.00 114.16 ? 126  ASN A CG  1 
ATOM   647  O OD1 . ASN A 1 100 ? -87.290  -26.060 -6.737  1.00 110.96 ? 126  ASN A OD1 1 
ATOM   648  N ND2 . ASN A 1 100 ? -88.657  -24.424 -6.045  1.00 111.83 ? 126  ASN A ND2 1 
ATOM   649  N N   . LEU A 1 101 ? -84.066  -26.751 -3.035  1.00 122.49 ? 127  LEU A N   1 
ATOM   650  C CA  . LEU A 1 101 ? -83.323  -26.846 -1.799  1.00 114.13 ? 127  LEU A CA  1 
ATOM   651  C C   . LEU A 1 101 ? -81.950  -26.261 -2.054  1.00 114.17 ? 127  LEU A C   1 
ATOM   652  O O   . LEU A 1 101 ? -81.185  -26.771 -2.891  1.00 88.98  ? 127  LEU A O   1 
ATOM   653  C CB  . LEU A 1 101 ? -83.192  -28.313 -1.367  1.00 101.40 ? 127  LEU A CB  1 
ATOM   654  C CG  . LEU A 1 101 ? -82.602  -28.583 0.019   1.00 89.31  ? 127  LEU A CG  1 
ATOM   655  C CD1 . LEU A 1 101 ? -83.548  -28.089 1.097   1.00 80.77  ? 127  LEU A CD1 1 
ATOM   656  C CD2 . LEU A 1 101 ? -82.334  -30.062 0.225   1.00 87.89  ? 127  LEU A CD2 1 
ATOM   657  N N   . ARG A 1 102 ? -81.655  -25.172 -1.352  1.00 109.51 ? 128  ARG A N   1 
ATOM   658  C CA  . ARG A 1 102 ? -80.383  -24.503 -1.495  1.00 109.81 ? 128  ARG A CA  1 
ATOM   659  C C   . ARG A 1 102 ? -79.492  -24.627 -0.263  1.00 96.24  ? 128  ARG A C   1 
ATOM   660  O O   . ARG A 1 102 ? -78.288  -24.809 -0.394  1.00 91.43  ? 128  ARG A O   1 
ATOM   661  C CB  . ARG A 1 102 ? -80.611  -23.047 -1.893  1.00 110.54 ? 128  ARG A CB  1 
ATOM   662  C CG  . ARG A 1 102 ? -81.247  -22.920 -3.271  1.00 112.02 ? 128  ARG A CG  1 
ATOM   663  C CD  . ARG A 1 102 ? -81.453  -21.481 -3.705  1.00 115.63 ? 128  ARG A CD  1 
ATOM   664  N NE  . ARG A 1 102 ? -82.377  -20.760 -2.834  1.00 121.68 ? 128  ARG A NE  1 
ATOM   665  C CZ  . ARG A 1 102 ? -82.748  -19.494 -3.021  1.00 139.70 ? 128  ARG A CZ  1 
ATOM   666  N NH1 . ARG A 1 102 ? -82.271  -18.798 -4.051  1.00 140.64 ? 128  ARG A NH1 1 
ATOM   667  N NH2 . ARG A 1 102 ? -83.604  -18.921 -2.181  1.00 144.80 ? 128  ARG A NH2 1 
ATOM   668  N N   . GLU A 1 103 ? -80.088  -24.644 0.923   1.00 91.99  ? 129  GLU A N   1 
ATOM   669  C CA  . GLU A 1 103 ? -79.301  -24.742 2.150   1.00 94.46  ? 129  GLU A CA  1 
ATOM   670  C C   . GLU A 1 103 ? -79.637  -26.003 2.957   1.00 90.04  ? 129  GLU A C   1 
ATOM   671  O O   . GLU A 1 103 ? -80.779  -26.209 3.359   1.00 88.18  ? 129  GLU A O   1 
ATOM   672  C CB  . GLU A 1 103 ? -79.546  -23.482 3.001   1.00 100.16 ? 129  GLU A CB  1 
ATOM   673  C CG  . GLU A 1 103 ? -78.666  -23.302 4.238   1.00 99.90  ? 129  GLU A CG  1 
ATOM   674  C CD  . GLU A 1 103 ? -78.926  -21.982 4.970   1.00 99.85  ? 129  GLU A CD  1 
ATOM   675  O OE1 . GLU A 1 103 ? -79.790  -21.207 4.531   1.00 108.66 ? 129  GLU A OE1 1 
ATOM   676  O OE2 . GLU A 1 103 ? -78.259  -21.701 5.984   1.00 100.19 ? 129  GLU A OE2 1 
ATOM   677  N N   . LEU A 1 104 ? -78.636  -26.846 3.194   1.00 86.69  ? 130  LEU A N   1 
ATOM   678  C CA  . LEU A 1 104 ? -78.845  -28.051 3.976   1.00 80.06  ? 130  LEU A CA  1 
ATOM   679  C C   . LEU A 1 104 ? -77.850  -28.143 5.122   1.00 74.96  ? 130  LEU A C   1 
ATOM   680  O O   . LEU A 1 104 ? -76.641  -28.294 4.901   1.00 76.40  ? 130  LEU A O   1 
ATOM   681  C CB  . LEU A 1 104 ? -78.724  -29.306 3.117   1.00 92.83  ? 130  LEU A CB  1 
ATOM   682  C CG  . LEU A 1 104 ? -78.965  -30.595 3.930   1.00 92.80  ? 130  LEU A CG  1 
ATOM   683  C CD1 . LEU A 1 104 ? -80.368  -30.601 4.543   1.00 82.70  ? 130  LEU A CD1 1 
ATOM   684  C CD2 . LEU A 1 104 ? -78.737  -31.831 3.076   1.00 89.81  ? 130  LEU A CD2 1 
ATOM   685  N N   . LEU A 1 105 ? -78.372  -28.172 6.346   1.00 69.45  ? 131  LEU A N   1 
ATOM   686  C CA  . LEU A 1 105 ? -77.523  -28.255 7.533   1.00 74.91  ? 131  LEU A CA  1 
ATOM   687  C C   . LEU A 1 105 ? -77.601  -29.606 8.271   1.00 71.81  ? 131  LEU A C   1 
ATOM   688  O O   . LEU A 1 105 ? -78.595  -29.917 8.911   1.00 76.08  ? 131  LEU A O   1 
ATOM   689  C CB  . LEU A 1 105 ? -77.885  -27.126 8.495   1.00 77.27  ? 131  LEU A CB  1 
ATOM   690  C CG  . LEU A 1 105 ? -77.833  -25.715 7.899   1.00 80.75  ? 131  LEU A CG  1 
ATOM   691  C CD1 . LEU A 1 105 ? -78.226  -24.693 8.954   1.00 73.78  ? 131  LEU A CD1 1 
ATOM   692  C CD2 . LEU A 1 105 ? -76.456  -25.403 7.321   1.00 87.48  ? 131  LEU A CD2 1 
ATOM   693  N N   . LEU A 1 106 ? -76.486  -30.326 8.274   1.00 68.95  ? 132  LEU A N   1 
ATOM   694  C CA  . LEU A 1 106 ? -76.369  -31.627 8.910   1.00 63.74  ? 132  LEU A CA  1 
ATOM   695  C C   . LEU A 1 106 ? -75.188  -31.647 9.851   1.00 71.60  ? 132  LEU A C   1 
ATOM   696  O O   . LEU A 1 106 ? -74.205  -32.366 9.630   1.00 82.24  ? 132  LEU A O   1 
ATOM   697  C CB  . LEU A 1 106 ? -76.151  -32.685 7.837   1.00 78.33  ? 132  LEU A CB  1 
ATOM   698  C CG  . LEU A 1 106 ? -77.294  -32.796 6.821   1.00 89.74  ? 132  LEU A CG  1 
ATOM   699  C CD1 . LEU A 1 106 ? -76.903  -33.756 5.708   1.00 91.06  ? 132  LEU A CD1 1 
ATOM   700  C CD2 . LEU A 1 106 ? -78.591  -33.222 7.500   1.00 81.82  ? 132  LEU A CD2 1 
ATOM   701  N N   . GLU A 1 107 ? -75.305  -30.907 10.939  1.00 75.05  ? 133  GLU A N   1 
ATOM   702  C CA  . GLU A 1 107 ? -74.225  -30.816 11.896  1.00 77.40  ? 133  GLU A CA  1 
ATOM   703  C C   . GLU A 1 107 ? -74.553  -31.576 13.144  1.00 76.98  ? 133  GLU A C   1 
ATOM   704  O O   . GLU A 1 107 ? -75.713  -31.631 13.572  1.00 68.90  ? 133  GLU A O   1 
ATOM   705  C CB  . GLU A 1 107 ? -73.963  -29.341 12.276  1.00 85.42  ? 133  GLU A CB  1 
ATOM   706  C CG  . GLU A 1 107 ? -73.647  -28.430 11.098  1.00 95.37  ? 133  GLU A CG  1 
ATOM   707  C CD  . GLU A 1 107 ? -73.484  -26.965 11.479  1.00 90.86  ? 133  GLU A CD  1 
ATOM   708  O OE1 . GLU A 1 107 ? -73.233  -26.668 12.667  1.00 92.38  ? 133  GLU A OE1 1 
ATOM   709  O OE2 . GLU A 1 107 ? -73.601  -26.111 10.568  1.00 69.80  ? 133  GLU A OE2 1 
ATOM   710  N N   . ASP A 1 108 ? -73.536  -32.160 13.750  1.00 83.11  ? 134  ASP A N   1 
ATOM   711  C CA  . ASP A 1 108 ? -73.706  -32.909 14.973  1.00 90.40  ? 134  ASP A CA  1 
ATOM   712  C C   . ASP A 1 108 ? -74.714  -34.015 14.781  1.00 96.10  ? 134  ASP A C   1 
ATOM   713  O O   . ASP A 1 108 ? -75.562  -34.251 15.620  1.00 82.35  ? 134  ASP A O   1 
ATOM   714  C CB  . ASP A 1 108 ? -74.148  -31.997 16.098  1.00 95.32  ? 134  ASP A CB  1 
ATOM   715  C CG  . ASP A 1 108 ? -73.630  -32.442 17.423  1.00 92.30  ? 134  ASP A CG  1 
ATOM   716  O OD1 . ASP A 1 108 ? -72.644  -33.185 17.446  1.00 95.36  ? 134  ASP A OD1 1 
ATOM   717  O OD2 . ASP A 1 108 ? -74.206  -32.061 18.445  1.00 111.24 ? 134  ASP A OD2 1 
ATOM   718  N N   . ASN A 1 109 ? -74.642  -34.662 13.635  1.00 92.62  ? 135  ASN A N   1 
ATOM   719  C CA  . ASN A 1 109 ? -75.481  -35.797 13.352  1.00 85.97  ? 135  ASN A CA  1 
ATOM   720  C C   . ASN A 1 109 ? -74.666  -37.066 13.252  1.00 86.54  ? 135  ASN A C   1 
ATOM   721  O O   . ASN A 1 109 ? -75.137  -38.086 12.827  1.00 86.23  ? 135  ASN A O   1 
ATOM   722  C CB  . ASN A 1 109 ? -76.313  -35.527 12.115  1.00 83.03  ? 135  ASN A CB  1 
ATOM   723  C CG  . ASN A 1 109 ? -77.432  -34.562 12.393  1.00 86.49  ? 135  ASN A CG  1 
ATOM   724  O OD1 . ASN A 1 109 ? -77.861  -34.422 13.523  1.00 86.40  ? 135  ASN A OD1 1 
ATOM   725  N ND2 . ASN A 1 109 ? -77.906  -33.894 11.375  1.00 87.62  ? 135  ASN A ND2 1 
ATOM   726  N N   . GLN A 1 110 ? -73.410  -36.985 13.624  1.00 83.74  ? 136  GLN A N   1 
ATOM   727  C CA  . GLN A 1 110 ? -72.615  -38.173 13.796  1.00 94.34  ? 136  GLN A CA  1 
ATOM   728  C C   . GLN A 1 110 ? -72.411  -38.982 12.542  1.00 93.35  ? 136  GLN A C   1 
ATOM   729  O O   . GLN A 1 110 ? -72.153  -40.161 12.620  1.00 97.08  ? 136  GLN A O   1 
ATOM   730  C CB  . GLN A 1 110 ? -73.279  -39.061 14.818  1.00 102.98 ? 136  GLN A CB  1 
ATOM   731  C CG  . GLN A 1 110 ? -72.297  -39.742 15.738  1.00 111.33 ? 136  GLN A CG  1 
ATOM   732  C CD  . GLN A 1 110 ? -72.030  -38.927 16.970  1.00 108.60 ? 136  GLN A CD  1 
ATOM   733  O OE1 . GLN A 1 110 ? -72.873  -38.151 17.403  1.00 111.24 ? 136  GLN A OE1 1 
ATOM   734  N NE2 . GLN A 1 110 ? -70.850  -39.088 17.538  1.00 124.27 ? 136  GLN A NE2 1 
ATOM   735  N N   . LEU A 1 111 ? -72.479  -38.352 11.388  1.00 95.53  ? 137  LEU A N   1 
ATOM   736  C CA  . LEU A 1 111 ? -72.345  -39.078 10.149  1.00 82.97  ? 137  LEU A CA  1 
ATOM   737  C C   . LEU A 1 111 ? -70.984  -39.646 9.892   1.00 92.70  ? 137  LEU A C   1 
ATOM   738  O O   . LEU A 1 111 ? -69.966  -39.097 10.305  1.00 90.80  ? 137  LEU A O   1 
ATOM   739  C CB  . LEU A 1 111 ? -72.742  -38.205 8.984   1.00 83.19  ? 137  LEU A CB  1 
ATOM   740  C CG  . LEU A 1 111 ? -73.991  -37.370 9.151   1.00 89.60  ? 137  LEU A CG  1 
ATOM   741  C CD1 . LEU A 1 111 ? -74.646  -37.201 7.807   1.00 90.94  ? 137  LEU A CD1 1 
ATOM   742  C CD2 . LEU A 1 111 ? -74.971  -37.974 10.131  1.00 100.11 ? 137  LEU A CD2 1 
ATOM   743  N N   . PRO A 1 112 ? -71.010  -40.849 9.181   1.00 100.79 ? 138  PRO A N   1 
ATOM   744  C CA  . PRO A 1 112 ? -69.693  -41.343 8.832   1.00 87.31  ? 138  PRO A CA  1 
ATOM   745  C C   . PRO A 1 112 ? -69.460  -41.188 7.355   1.00 86.19  ? 138  PRO A C   1 
ATOM   746  O O   . PRO A 1 112 ? -68.371  -41.486 6.897   1.00 72.51  ? 138  PRO A O   1 
ATOM   747  C CB  . PRO A 1 112 ? -69.795  -42.812 9.183   1.00 90.14  ? 138  PRO A CB  1 
ATOM   748  C CG  . PRO A 1 112 ? -71.219  -43.164 8.912   1.00 95.51  ? 138  PRO A CG  1 
ATOM   749  C CD  . PRO A 1 112 ? -71.968  -41.911 8.626   1.00 98.02  ? 138  PRO A CD  1 
ATOM   750  N N   . GLN A 1 113 ? -70.446  -40.711 6.610   1.00 77.80  ? 139  GLN A N   1 
ATOM   751  C CA  . GLN A 1 113 ? -70.175  -40.422 5.191   1.00 97.68  ? 139  GLN A CA  1 
ATOM   752  C C   . GLN A 1 113 ? -71.001  -39.244 4.666   1.00 94.21  ? 139  GLN A C   1 
ATOM   753  O O   . GLN A 1 113 ? -71.973  -38.808 5.281   1.00 84.09  ? 139  GLN A O   1 
ATOM   754  C CB  . GLN A 1 113 ? -70.441  -41.655 4.290   1.00 118.98 ? 139  GLN A CB  1 
ATOM   755  C CG  . GLN A 1 113 ? -69.557  -42.881 4.528   1.00 124.22 ? 139  GLN A CG  1 
ATOM   756  C CD  . GLN A 1 113 ? -68.067  -42.615 4.316   1.00 132.31 ? 139  GLN A CD  1 
ATOM   757  O OE1 . GLN A 1 113 ? -67.636  -41.467 4.136   1.00 143.28 ? 139  GLN A OE1 1 
ATOM   758  N NE2 . GLN A 1 113 ? -67.268  -43.677 4.379   1.00 119.91 ? 139  GLN A NE2 1 
ATOM   759  N N   . ILE A 1 114 ? -70.604  -38.744 3.506   1.00 92.43  ? 140  ILE A N   1 
ATOM   760  C CA  . ILE A 1 114 ? -71.300  -37.642 2.881   1.00 92.48  ? 140  ILE A CA  1 
ATOM   761  C C   . ILE A 1 114 ? -72.536  -38.247 2.228   1.00 92.97  ? 140  ILE A C   1 
ATOM   762  O O   . ILE A 1 114 ? -72.429  -38.924 1.198   1.00 102.88 ? 140  ILE A O   1 
ATOM   763  C CB  . ILE A 1 114 ? -70.436  -37.001 1.775   1.00 93.64  ? 140  ILE A CB  1 
ATOM   764  C CG1 . ILE A 1 114 ? -69.053  -36.624 2.317   1.00 98.56  ? 140  ILE A CG1 1 
ATOM   765  C CG2 . ILE A 1 114 ? -71.166  -35.814 1.171   1.00 88.87  ? 140  ILE A CG2 1 
ATOM   766  C CD1 . ILE A 1 114 ? -68.095  -36.114 1.265   1.00 103.01 ? 140  ILE A CD1 1 
ATOM   767  N N   . PRO A 1 115 ? -73.712  -38.025 2.815   1.00 86.89  ? 141  PRO A N   1 
ATOM   768  C CA  . PRO A 1 115 ? -74.914  -38.600 2.213   1.00 87.26  ? 141  PRO A CA  1 
ATOM   769  C C   . PRO A 1 115 ? -74.856  -38.607 0.695   1.00 103.47 ? 141  PRO A C   1 
ATOM   770  O O   . PRO A 1 115 ? -74.754  -37.541 0.079   1.00 101.14 ? 141  PRO A O   1 
ATOM   771  C CB  . PRO A 1 115 ? -76.032  -37.678 2.693   1.00 77.19  ? 141  PRO A CB  1 
ATOM   772  C CG  . PRO A 1 115 ? -75.526  -37.091 3.972   1.00 88.91  ? 141  PRO A CG  1 
ATOM   773  C CD  . PRO A 1 115 ? -74.017  -37.194 3.989   1.00 92.24  ? 141  PRO A CD  1 
ATOM   774  N N   . SER A 1 116 ? -74.880  -39.790 0.100   1.00 116.64 ? 142  SER A N   1 
ATOM   775  C CA  . SER A 1 116 ? -74.813  -39.911 -1.343  1.00 98.06  ? 142  SER A CA  1 
ATOM   776  C C   . SER A 1 116 ? -76.130  -39.486 -1.922  1.00 84.60  ? 142  SER A C   1 
ATOM   777  O O   . SER A 1 116 ? -77.114  -39.405 -1.213  1.00 73.93  ? 142  SER A O   1 
ATOM   778  C CB  . SER A 1 116 ? -74.473  -41.327 -1.750  1.00 89.95  ? 142  SER A CB  1 
ATOM   779  O OG  . SER A 1 116 ? -73.282  -41.734 -1.127  1.00 92.15  ? 142  SER A OG  1 
ATOM   780  N N   . GLY A 1 117 ? -76.147  -39.200 -3.211  1.00 77.56  ? 143  GLY A N   1 
ATOM   781  C CA  . GLY A 1 117 ? -77.369  -38.751 -3.822  1.00 87.18  ? 143  GLY A CA  1 
ATOM   782  C C   . GLY A 1 117 ? -77.906  -37.494 -3.206  1.00 93.88  ? 143  GLY A C   1 
ATOM   783  O O   . GLY A 1 117 ? -78.926  -37.481 -2.540  1.00 82.75  ? 143  GLY A O   1 
ATOM   784  N N   . LEU A 1 118 ? -77.152  -36.427 -3.386  1.00 109.08 ? 144  LEU A N   1 
ATOM   785  C CA  . LEU A 1 118 ? -77.571  -35.131 -2.916  1.00 99.36  ? 144  LEU A CA  1 
ATOM   786  C C   . LEU A 1 118 ? -77.968  -34.254 -4.071  1.00 84.96  ? 144  LEU A C   1 
ATOM   787  O O   . LEU A 1 118 ? -77.449  -34.385 -5.159  1.00 89.15  ? 144  LEU A O   1 
ATOM   788  C CB  . LEU A 1 118 ? -76.463  -34.488 -2.111  1.00 109.88 ? 144  LEU A CB  1 
ATOM   789  C CG  . LEU A 1 118 ? -76.600  -34.694 -0.611  1.00 107.95 ? 144  LEU A CG  1 
ATOM   790  C CD1 . LEU A 1 118 ? -75.252  -34.557 0.057   1.00 110.76 ? 144  LEU A CD1 1 
ATOM   791  C CD2 . LEU A 1 118 ? -77.594  -33.715 -0.030  1.00 92.02  ? 144  LEU A CD2 1 
ATOM   792  N N   . PRO A 1 119 ? -78.953  -33.306 -3.772  1.00 74.36  ? 145  PRO A N   1 
ATOM   793  C CA  . PRO A 1 119 ? -79.430  -32.560 -4.944  1.00 76.86  ? 145  PRO A CA  1 
ATOM   794  C C   . PRO A 1 119 ? -78.385  -31.650 -5.538  1.00 91.15  ? 145  PRO A C   1 
ATOM   795  O O   . PRO A 1 119 ? -77.396  -31.403 -4.895  1.00 105.12 ? 145  PRO A O   1 
ATOM   796  C CB  . PRO A 1 119 ? -80.544  -31.687 -4.387  1.00 76.75  ? 145  PRO A CB  1 
ATOM   797  C CG  . PRO A 1 119 ? -81.028  -32.380 -3.199  1.00 81.64  ? 145  PRO A CG  1 
ATOM   798  C CD  . PRO A 1 119 ? -79.767  -32.783 -2.569  1.00 78.45  ? 145  PRO A CD  1 
ATOM   799  N N   . GLU A 1 120 ? -78.566  -31.210 -6.775  1.00 96.80  ? 146  GLU A N   1 
ATOM   800  C CA  . GLU A 1 120 ? -77.585  -30.350 -7.410  1.00 101.83 ? 146  GLU A CA  1 
ATOM   801  C C   . GLU A 1 120 ? -77.991  -28.874 -7.237  1.00 101.85 ? 146  GLU A C   1 
ATOM   802  O O   . GLU A 1 120 ? -77.213  -27.967 -7.516  1.00 104.28 ? 146  GLU A O   1 
ATOM   803  C CB  . GLU A 1 120 ? -77.381  -30.743 -8.879  1.00 110.58 ? 146  GLU A CB  1 
ATOM   804  C CG  . GLU A 1 120 ? -76.958  -32.207 -9.042  1.00 119.94 ? 146  GLU A CG  1 
ATOM   805  C CD  . GLU A 1 120 ? -76.448  -32.564 -10.437 1.00 119.58 ? 146  GLU A CD  1 
ATOM   806  O OE1 . GLU A 1 120 ? -76.539  -31.725 -11.361 1.00 111.42 ? 146  GLU A OE1 1 
ATOM   807  O OE2 . GLU A 1 120 ? -75.911  -33.685 -10.594 1.00 108.39 ? 146  GLU A OE2 1 
ATOM   808  N N   . SER A 1 121 ? -79.168  -28.650 -6.664  1.00 89.47  ? 147  SER A N   1 
ATOM   809  C CA  . SER A 1 121 ? -79.657  -27.307 -6.433  1.00 91.52  ? 147  SER A CA  1 
ATOM   810  C C   . SER A 1 121 ? -79.019  -26.658 -5.201  1.00 103.26 ? 147  SER A C   1 
ATOM   811  O O   . SER A 1 121 ? -79.304  -25.497 -4.881  1.00 96.75  ? 147  SER A O   1 
ATOM   812  C CB  . SER A 1 121 ? -81.162  -27.355 -6.231  1.00 103.16 ? 147  SER A CB  1 
ATOM   813  O OG  . SER A 1 121 ? -81.496  -28.219 -5.158  1.00 113.13 ? 147  SER A OG  1 
ATOM   814  N N   . LEU A 1 122 ? -78.179  -27.405 -4.493  1.00 109.04 ? 148  LEU A N   1 
ATOM   815  C CA  . LEU A 1 122 ? -77.531  -26.876 -3.289  1.00 109.35 ? 148  LEU A CA  1 
ATOM   816  C C   . LEU A 1 122 ? -76.454  -25.825 -3.505  1.00 94.77  ? 148  LEU A C   1 
ATOM   817  O O   . LEU A 1 122 ? -75.496  -26.027 -4.258  1.00 86.13  ? 148  LEU A O   1 
ATOM   818  C CB  . LEU A 1 122 ? -76.916  -27.999 -2.426  1.00 97.53  ? 148  LEU A CB  1 
ATOM   819  C CG  . LEU A 1 122 ? -77.830  -28.980 -1.681  1.00 89.01  ? 148  LEU A CG  1 
ATOM   820  C CD1 . LEU A 1 122 ? -76.969  -29.991 -0.944  1.00 93.15  ? 148  LEU A CD1 1 
ATOM   821  C CD2 . LEU A 1 122 ? -78.764  -28.276 -0.700  1.00 78.02  ? 148  LEU A CD2 1 
ATOM   822  N N   . THR A 1 123 ? -76.626  -24.713 -2.801  1.00 81.76  ? 149  THR A N   1 
ATOM   823  C CA  . THR A 1 123 ? -75.674  -23.621 -2.815  1.00 82.39  ? 149  THR A CA  1 
ATOM   824  C C   . THR A 1 123 ? -74.874  -23.671 -1.508  1.00 79.16  ? 149  THR A C   1 
ATOM   825  O O   . THR A 1 123 ? -73.686  -23.426 -1.510  1.00 87.44  ? 149  THR A O   1 
ATOM   826  C CB  . THR A 1 123 ? -76.353  -22.253 -2.981  1.00 80.71  ? 149  THR A CB  1 
ATOM   827  O OG1 . THR A 1 123 ? -77.310  -22.039 -1.933  1.00 75.95  ? 149  THR A OG1 1 
ATOM   828  C CG2 . THR A 1 123 ? -77.044  -22.180 -4.313  1.00 82.15  ? 149  THR A CG2 1 
ATOM   829  N N   . GLU A 1 124 ? -75.518  -24.078 -0.416  1.00 85.91  ? 150  GLU A N   1 
ATOM   830  C CA  . GLU A 1 124 ? -74.860  -24.173 0.884   1.00 82.63  ? 150  GLU A CA  1 
ATOM   831  C C   . GLU A 1 124 ? -75.068  -25.530 1.580   1.00 88.75  ? 150  GLU A C   1 
ATOM   832  O O   . GLU A 1 124 ? -76.202  -25.914 1.897   1.00 80.25  ? 150  GLU A O   1 
ATOM   833  C CB  . GLU A 1 124 ? -75.383  -23.092 1.811   1.00 82.34  ? 150  GLU A CB  1 
ATOM   834  C CG  . GLU A 1 124 ? -74.703  -23.129 3.168   1.00 91.67  ? 150  GLU A CG  1 
ATOM   835  C CD  . GLU A 1 124 ? -75.234  -22.100 4.135   1.00 101.29 ? 150  GLU A CD  1 
ATOM   836  O OE1 . GLU A 1 124 ? -76.158  -21.349 3.762   1.00 118.63 ? 150  GLU A OE1 1 
ATOM   837  O OE2 . GLU A 1 124 ? -74.732  -22.059 5.277   1.00 102.24 ? 150  GLU A OE2 1 
ATOM   838  N N   . LEU A 1 125 ? -73.963  -26.173 1.948   1.00 76.41  ? 151  LEU A N   1 
ATOM   839  C CA  . LEU A 1 125 ? -74.014  -27.462 2.616   1.00 75.50  ? 151  LEU A CA  1 
ATOM   840  C C   . LEU A 1 125 ? -73.087  -27.534 3.838   1.00 75.11  ? 151  LEU A C   1 
ATOM   841  O O   . LEU A 1 125 ? -71.859  -27.487 3.684   1.00 68.12  ? 151  LEU A O   1 
ATOM   842  C CB  . LEU A 1 125 ? -73.596  -28.574 1.636   1.00 79.13  ? 151  LEU A CB  1 
ATOM   843  C CG  . LEU A 1 125 ? -73.591  -30.001 2.220   1.00 79.36  ? 151  LEU A CG  1 
ATOM   844  C CD1 . LEU A 1 125 ? -74.994  -30.422 2.634   1.00 76.47  ? 151  LEU A CD1 1 
ATOM   845  C CD2 . LEU A 1 125 ? -73.002  -30.995 1.240   1.00 77.57  ? 151  LEU A CD2 1 
ATOM   846  N N   . SER A 1 126 ? -73.657  -27.789 5.022   1.00 69.50  ? 152  SER A N   1 
ATOM   847  C CA  . SER A 1 126 ? -72.845  -27.898 6.241   1.00 70.31  ? 152  SER A CA  1 
ATOM   848  C C   . SER A 1 126 ? -72.816  -29.310 6.866   1.00 66.80  ? 152  SER A C   1 
ATOM   849  O O   . SER A 1 126 ? -73.825  -29.825 7.312   1.00 60.19  ? 152  SER A O   1 
ATOM   850  C CB  . SER A 1 126 ? -73.323  -26.890 7.295   1.00 70.24  ? 152  SER A CB  1 
ATOM   851  O OG  . SER A 1 126 ? -72.455  -26.909 8.430   1.00 64.59  ? 152  SER A OG  1 
ATOM   852  N N   . LEU A 1 127 ? -71.631  -29.886 6.972   1.00 71.95  ? 153  LEU A N   1 
ATOM   853  C CA  . LEU A 1 127 ? -71.466  -31.209 7.556   1.00 64.41  ? 153  LEU A CA  1 
ATOM   854  C C   . LEU A 1 127 ? -70.489  -31.100 8.690   1.00 63.51  ? 153  LEU A C   1 
ATOM   855  O O   . LEU A 1 127 ? -69.594  -31.945 8.858   1.00 76.11  ? 153  LEU A O   1 
ATOM   856  C CB  . LEU A 1 127 ? -70.910  -32.191 6.512   1.00 79.98  ? 153  LEU A CB  1 
ATOM   857  C CG  . LEU A 1 127 ? -71.754  -32.410 5.247   1.00 85.63  ? 153  LEU A CG  1 
ATOM   858  C CD1 . LEU A 1 127 ? -71.053  -33.389 4.315   1.00 85.49  ? 153  LEU A CD1 1 
ATOM   859  C CD2 . LEU A 1 127 ? -73.148  -32.907 5.592   1.00 82.12  ? 153  LEU A CD2 1 
ATOM   860  N N   . ILE A 1 128 ? -70.644  -30.089 9.513   1.00 70.73  ? 154  ILE A N   1 
ATOM   861  C CA  . ILE A 1 128 ? -69.769  -29.929 10.662  1.00 80.96  ? 154  ILE A CA  1 
ATOM   862  C C   . ILE A 1 128 ? -70.037  -30.875 11.820  1.00 79.33  ? 154  ILE A C   1 
ATOM   863  O O   . ILE A 1 128 ? -71.160  -31.264 12.061  1.00 73.80  ? 154  ILE A O   1 
ATOM   864  C CB  . ILE A 1 128 ? -69.828  -28.502 11.190  1.00 82.46  ? 154  ILE A CB  1 
ATOM   865  C CG1 . ILE A 1 128 ? -69.825  -27.536 10.027  1.00 96.68  ? 154  ILE A CG1 1 
ATOM   866  C CG2 . ILE A 1 128 ? -68.647  -28.223 12.080  1.00 73.87  ? 154  ILE A CG2 1 
ATOM   867  C CD1 . ILE A 1 128 ? -69.601  -26.101 10.426  1.00 98.09  ? 154  ILE A CD1 1 
ATOM   868  N N   . GLN A 1 129 ? -69.008  -31.173 12.592  1.00 80.09  ? 155  GLN A N   1 
ATOM   869  C CA  . GLN A 1 129 ? -69.191  -31.992 13.763  1.00 81.78  ? 155  GLN A CA  1 
ATOM   870  C C   . GLN A 1 129 ? -69.765  -33.366 13.460  1.00 85.20  ? 155  GLN A C   1 
ATOM   871  O O   . GLN A 1 129 ? -70.772  -33.772 14.006  1.00 71.89  ? 155  GLN A O   1 
ATOM   872  C CB  . GLN A 1 129 ? -70.105  -31.256 14.714  1.00 87.18  ? 155  GLN A CB  1 
ATOM   873  C CG  . GLN A 1 129 ? -69.438  -30.807 15.984  1.00 109.91 ? 155  GLN A CG  1 
ATOM   874  C CD  . GLN A 1 129 ? -70.359  -29.964 16.823  1.00 120.13 ? 155  GLN A CD  1 
ATOM   875  O OE1 . GLN A 1 129 ? -71.082  -29.119 16.310  1.00 108.49 ? 155  GLN A OE1 1 
ATOM   876  N NE2 . GLN A 1 129 ? -70.348  -30.199 18.121  1.00 126.70 ? 155  GLN A NE2 1 
ATOM   877  N N   . ASN A 1 130 ? -69.120  -34.060 12.543  1.00 74.40  ? 156  ASN A N   1 
ATOM   878  C CA  . ASN A 1 130 ? -69.534  -35.366 12.110  1.00 69.00  ? 156  ASN A CA  1 
ATOM   879  C C   . ASN A 1 130 ? -68.351  -36.298 12.061  1.00 80.72  ? 156  ASN A C   1 
ATOM   880  O O   . ASN A 1 130 ? -67.300  -35.965 12.559  1.00 88.95  ? 156  ASN A O   1 
ATOM   881  C CB  . ASN A 1 130 ? -70.223  -35.270 10.779  1.00 69.30  ? 156  ASN A CB  1 
ATOM   882  C CG  . ASN A 1 130 ? -71.633  -34.804 10.918  1.00 74.88  ? 156  ASN A CG  1 
ATOM   883  O OD1 . ASN A 1 130 ? -72.308  -35.171 11.851  1.00 69.53  ? 156  ASN A OD1 1 
ATOM   884  N ND2 . ASN A 1 130 ? -72.083  -33.990 10.001  1.00 78.45  ? 156  ASN A ND2 1 
ATOM   885  N N   . ASN A 1 131 ? -68.546  -37.501 11.546  1.00 83.30  ? 157  ASN A N   1 
ATOM   886  C CA  . ASN A 1 131 ? -67.505  -38.518 11.539  1.00 85.20  ? 157  ASN A CA  1 
ATOM   887  C C   . ASN A 1 131 ? -66.831  -38.827 10.204  1.00 89.06  ? 157  ASN A C   1 
ATOM   888  O O   . ASN A 1 131 ? -66.189  -39.839 10.058  1.00 110.94 ? 157  ASN A O   1 
ATOM   889  C CB  . ASN A 1 131 ? -68.034  -39.780 12.176  1.00 87.06  ? 157  ASN A CB  1 
ATOM   890  C CG  . ASN A 1 131 ? -68.313  -39.598 13.640  1.00 83.51  ? 157  ASN A CG  1 
ATOM   891  O OD1 . ASN A 1 131 ? -67.443  -39.193 14.387  1.00 87.99  ? 157  ASN A OD1 1 
ATOM   892  N ND2 . ASN A 1 131 ? -69.530  -39.872 14.052  1.00 73.61  ? 157  ASN A ND2 1 
ATOM   893  N N   . ILE A 1 132 ? -66.984  -37.928 9.250   1.00 91.43  ? 158  ILE A N   1 
ATOM   894  C CA  . ILE A 1 132 ? -66.684  -38.094 7.836   1.00 72.80  ? 158  ILE A CA  1 
ATOM   895  C C   . ILE A 1 132 ? -65.195  -38.003 7.694   1.00 74.96  ? 158  ILE A C   1 
ATOM   896  O O   . ILE A 1 132 ? -64.603  -36.989 8.027   1.00 101.12 ? 158  ILE A O   1 
ATOM   897  C CB  . ILE A 1 132 ? -67.324  -36.987 7.043   1.00 65.92  ? 158  ILE A CB  1 
ATOM   898  C CG1 . ILE A 1 132 ? -68.827  -37.035 7.279   1.00 67.45  ? 158  ILE A CG1 1 
ATOM   899  C CG2 . ILE A 1 132 ? -66.969  -37.132 5.582   1.00 71.12  ? 158  ILE A CG2 1 
ATOM   900  C CD1 . ILE A 1 132 ? -69.596  -35.902 6.650   1.00 74.89  ? 158  ILE A CD1 1 
ATOM   901  N N   . TYR A 1 133 ? -64.578  -39.073 7.229   1.00 83.17  ? 159  TYR A N   1 
ATOM   902  C CA  . TYR A 1 133 ? -63.134  -39.101 7.103   1.00 85.98  ? 159  TYR A CA  1 
ATOM   903  C C   . TYR A 1 133 ? -62.686  -39.250 5.683   1.00 82.30  ? 159  TYR A C   1 
ATOM   904  O O   . TYR A 1 133 ? -61.480  -39.287 5.405   1.00 76.68  ? 159  TYR A O   1 
ATOM   905  C CB  . TYR A 1 133 ? -62.583  -40.240 7.941   1.00 108.96 ? 159  TYR A CB  1 
ATOM   906  C CG  . TYR A 1 133 ? -63.146  -40.219 9.342   1.00 144.76 ? 159  TYR A CG  1 
ATOM   907  C CD1 . TYR A 1 133 ? -62.800  -39.213 10.232  1.00 145.28 ? 159  TYR A CD1 1 
ATOM   908  C CD2 . TYR A 1 133 ? -64.002  -41.220 9.786   1.00 162.12 ? 159  TYR A CD2 1 
ATOM   909  C CE1 . TYR A 1 133 ? -63.316  -39.180 11.509  1.00 146.09 ? 159  TYR A CE1 1 
ATOM   910  C CE2 . TYR A 1 133 ? -64.507  -41.205 11.072  1.00 158.55 ? 159  TYR A CE2 1 
ATOM   911  C CZ  . TYR A 1 133 ? -64.157  -40.182 11.926  1.00 149.52 ? 159  TYR A CZ  1 
ATOM   912  O OH  . TYR A 1 133 ? -64.664  -40.147 13.197  1.00 158.48 ? 159  TYR A OH  1 
ATOM   913  N N   . ASN A 1 134 ? -63.653  -39.295 4.775   1.00 77.58  ? 160  ASN A N   1 
ATOM   914  C CA  . ASN A 1 134 ? -63.345  -39.437 3.386   1.00 87.51  ? 160  ASN A CA  1 
ATOM   915  C C   . ASN A 1 134 ? -64.196  -38.442 2.614   1.00 88.45  ? 160  ASN A C   1 
ATOM   916  O O   . ASN A 1 134 ? -65.438  -38.493 2.682   1.00 80.13  ? 160  ASN A O   1 
ATOM   917  C CB  . ASN A 1 134 ? -63.634  -40.871 2.932   1.00 95.78  ? 160  ASN A CB  1 
ATOM   918  C CG  . ASN A 1 134 ? -63.076  -41.174 1.549   1.00 117.30 ? 160  ASN A CG  1 
ATOM   919  O OD1 . ASN A 1 134 ? -62.281  -40.395 1.003   1.00 105.65 ? 160  ASN A OD1 1 
ATOM   920  N ND2 . ASN A 1 134 ? -63.416  -42.356 1.013   1.00 121.58 ? 160  ASN A ND2 1 
ATOM   921  N N   . ILE A 1 135 ? -63.527  -37.466 1.992   1.00 80.62  ? 161  ILE A N   1 
ATOM   922  C CA  . ILE A 1 135 ? -64.206  -36.441 1.184   1.00 86.15  ? 161  ILE A CA  1 
ATOM   923  C C   . ILE A 1 135 ? -64.075  -36.981 -0.227  1.00 79.15  ? 161  ILE A C   1 
ATOM   924  O O   . ILE A 1 135 ? -62.953  -37.089 -0.786  1.00 70.16  ? 161  ILE A O   1 
ATOM   925  C CB  . ILE A 1 135 ? -63.608  -35.026 1.390   1.00 90.84  ? 161  ILE A CB  1 
ATOM   926  C CG1 . ILE A 1 135 ? -63.740  -34.615 2.861   1.00 85.64  ? 161  ILE A CG1 1 
ATOM   927  C CG2 . ILE A 1 135 ? -64.337  -33.991 0.542   1.00 84.15  ? 161  ILE A CG2 1 
ATOM   928  C CD1 . ILE A 1 135 ? -65.174  -34.578 3.359   1.00 77.53  ? 161  ILE A CD1 1 
ATOM   929  N N   . THR A 1 136 ? -65.231  -37.276 -0.816  1.00 73.32  ? 162  THR A N   1 
ATOM   930  C CA  . THR A 1 136 ? -65.259  -37.929 -2.113  1.00 87.26  ? 162  THR A CA  1 
ATOM   931  C C   . THR A 1 136 ? -66.063  -37.333 -3.247  1.00 90.94  ? 162  THR A C   1 
ATOM   932  O O   . THR A 1 136 ? -67.188  -36.824 -3.069  1.00 77.04  ? 162  THR A O   1 
ATOM   933  C CB  . THR A 1 136 ? -65.824  -39.361 -1.921  1.00 94.53  ? 162  THR A CB  1 
ATOM   934  O OG1 . THR A 1 136 ? -67.202  -39.294 -1.500  1.00 85.01  ? 162  THR A OG1 1 
ATOM   935  C CG2 . THR A 1 136 ? -65.007  -40.127 -0.870  1.00 86.30  ? 162  THR A CG2 1 
ATOM   936  N N   . LYS A 1 137 ? -65.589  -37.692 -4.435  1.00 84.52  ? 163  LYS A N   1 
ATOM   937  C CA  . LYS A 1 137 ? -66.165  -37.253 -5.684  1.00 82.92  ? 163  LYS A CA  1 
ATOM   938  C C   . LYS A 1 137 ? -67.587  -37.797 -5.821  1.00 87.91  ? 163  LYS A C   1 
ATOM   939  O O   . LYS A 1 137 ? -68.463  -37.128 -6.369  1.00 92.48  ? 163  LYS A O   1 
ATOM   940  C CB  . LYS A 1 137 ? -65.274  -37.715 -6.839  1.00 83.35  ? 163  LYS A CB  1 
ATOM   941  C CG  . LYS A 1 137 ? -63.786  -37.448 -6.563  1.00 97.65  ? 163  LYS A CG  1 
ATOM   942  C CD  . LYS A 1 137 ? -62.842  -37.709 -7.732  1.00 99.07  ? 163  LYS A CD  1 
ATOM   943  C CE  . LYS A 1 137 ? -63.110  -36.740 -8.877  1.00 100.62 ? 163  LYS A CE  1 
ATOM   944  N NZ  . LYS A 1 137 ? -62.084  -36.863 -9.935  1.00 99.43  ? 163  LYS A NZ  1 
ATOM   945  N N   . GLU A 1 138 ? -67.844  -38.985 -5.278  1.00 97.55  ? 164  GLU A N   1 
ATOM   946  C CA  . GLU A 1 138 ? -69.187  -39.547 -5.374  1.00 110.49 ? 164  GLU A CA  1 
ATOM   947  C C   . GLU A 1 138 ? -70.179  -38.678 -4.637  1.00 99.62  ? 164  GLU A C   1 
ATOM   948  O O   . GLU A 1 138 ? -71.225  -38.326 -5.167  1.00 105.54 ? 164  GLU A O   1 
ATOM   949  C CB  . GLU A 1 138 ? -69.274  -40.969 -4.808  1.00 130.28 ? 164  GLU A CB  1 
ATOM   950  C CG  . GLU A 1 138 ? -70.709  -41.514 -4.859  1.00 147.75 ? 164  GLU A CG  1 
ATOM   951  C CD  . GLU A 1 138 ? -70.870  -42.903 -4.265  1.00 157.23 ? 164  GLU A CD  1 
ATOM   952  O OE1 . GLU A 1 138 ? -69.849  -43.532 -3.920  1.00 165.13 ? 164  GLU A OE1 1 
ATOM   953  O OE2 . GLU A 1 138 ? -72.027  -43.370 -4.150  1.00 153.20 ? 164  GLU A OE2 1 
ATOM   954  N N   . GLY A 1 139 ? -69.839  -38.326 -3.406  1.00 109.83 ? 165  GLY A N   1 
ATOM   955  C CA  . GLY A 1 139 ? -70.721  -37.517 -2.587  1.00 106.74 ? 165  GLY A CA  1 
ATOM   956  C C   . GLY A 1 139 ? -70.681  -36.016 -2.799  1.00 95.98  ? 165  GLY A C   1 
ATOM   957  O O   . GLY A 1 139 ? -71.699  -35.360 -2.604  1.00 88.20  ? 165  GLY A O   1 
ATOM   958  N N   . ILE A 1 140 ? -69.555  -35.478 -3.261  1.00 90.03  ? 166  ILE A N   1 
ATOM   959  C CA  . ILE A 1 140 ? -69.395  -34.026 -3.424  1.00 93.51  ? 166  ILE A CA  1 
ATOM   960  C C   . ILE A 1 140 ? -69.448  -33.420 -4.842  1.00 92.42  ? 166  ILE A C   1 
ATOM   961  O O   . ILE A 1 140 ? -70.139  -32.446 -5.083  1.00 76.27  ? 166  ILE A O   1 
ATOM   962  C CB  . ILE A 1 140 ? -68.129  -33.575 -2.659  1.00 89.79  ? 166  ILE A CB  1 
ATOM   963  C CG1 . ILE A 1 140 ? -68.422  -33.579 -1.180  1.00 90.91  ? 166  ILE A CG1 1 
ATOM   964  C CG2 . ILE A 1 140 ? -67.698  -32.168 -2.980  1.00 94.70  ? 166  ILE A CG2 1 
ATOM   965  C CD1 . ILE A 1 140 ? -69.678  -32.827 -0.849  1.00 94.03  ? 166  ILE A CD1 1 
ATOM   966  N N   . SER A 1 141 ? -68.732  -34.012 -5.775  1.00 87.21  ? 167  SER A N   1 
ATOM   967  C CA  . SER A 1 141 ? -68.431  -33.373 -7.040  1.00 84.08  ? 167  SER A CA  1 
ATOM   968  C C   . SER A 1 141 ? -69.621  -33.059 -7.903  1.00 82.14  ? 167  SER A C   1 
ATOM   969  O O   . SER A 1 141 ? -69.543  -32.228 -8.776  1.00 95.29  ? 167  SER A O   1 
ATOM   970  C CB  . SER A 1 141 ? -67.440  -34.194 -7.817  1.00 88.60  ? 167  SER A CB  1 
ATOM   971  O OG  . SER A 1 141 ? -66.376  -34.567 -6.981  1.00 100.98 ? 167  SER A OG  1 
ATOM   972  N N   . ARG A 1 142 ? -70.706  -33.766 -7.702  1.00 92.00  ? 168  ARG A N   1 
ATOM   973  C CA  . ARG A 1 142 ? -71.909  -33.489 -8.446  1.00 103.93 ? 168  ARG A CA  1 
ATOM   974  C C   . ARG A 1 142 ? -72.396  -32.104 -8.107  1.00 103.76 ? 168  ARG A C   1 
ATOM   975  O O   . ARG A 1 142 ? -73.058  -31.468 -8.897  1.00 93.13  ? 168  ARG A O   1 
ATOM   976  C CB  . ARG A 1 142 ? -72.993  -34.512 -8.125  1.00 123.05 ? 168  ARG A CB  1 
ATOM   977  C CG  . ARG A 1 142 ? -73.159  -35.600 -9.172  1.00 136.65 ? 168  ARG A CG  1 
ATOM   978  C CD  . ARG A 1 142 ? -71.927  -36.489 -9.242  1.00 143.79 ? 168  ARG A CD  1 
ATOM   979  N NE  . ARG A 1 142 ? -72.233  -37.917 -9.168  1.00 145.44 ? 168  ARG A NE  1 
ATOM   980  C CZ  . ARG A 1 142 ? -73.154  -38.453 -8.376  1.00 143.45 ? 168  ARG A CZ  1 
ATOM   981  N NH1 . ARG A 1 142 ? -73.885  -37.691 -7.576  1.00 145.95 ? 168  ARG A NH1 1 
ATOM   982  N NH2 . ARG A 1 142 ? -73.345  -39.761 -8.386  1.00 143.35 ? 168  ARG A NH2 1 
ATOM   983  N N   . LEU A 1 143 ? -72.088  -31.648 -6.905  1.00 101.64 ? 169  LEU A N   1 
ATOM   984  C CA  . LEU A 1 143 ? -72.831  -30.574 -6.271  1.00 95.09  ? 169  LEU A CA  1 
ATOM   985  C C   . LEU A 1 143 ? -72.861  -29.238 -7.003  1.00 95.77  ? 169  LEU A C   1 
ATOM   986  O O   . LEU A 1 143 ? -73.872  -28.560 -7.010  1.00 80.50  ? 169  LEU A O   1 
ATOM   987  C CB  . LEU A 1 143 ? -72.355  -30.409 -4.847  1.00 98.54  ? 169  LEU A CB  1 
ATOM   988  C CG  . LEU A 1 143 ? -73.092  -31.252 -3.815  1.00 99.12  ? 169  LEU A CG  1 
ATOM   989  C CD1 . LEU A 1 143 ? -74.536  -31.509 -4.182  1.00 90.00  ? 169  LEU A CD1 1 
ATOM   990  C CD2 . LEU A 1 143 ? -72.360  -32.540 -3.550  1.00 97.32  ? 169  LEU A CD2 1 
ATOM   991  N N   . ILE A 1 144 ? -71.754  -28.831 -7.586  1.00 97.60  ? 170  ILE A N   1 
ATOM   992  C CA  . ILE A 1 144 ? -71.794  -27.900 -8.697  1.00 99.57  ? 170  ILE A CA  1 
ATOM   993  C C   . ILE A 1 144 ? -72.204  -26.486 -8.351  1.00 86.96  ? 170  ILE A C   1 
ATOM   994  O O   . ILE A 1 144 ? -71.512  -25.555 -8.681  1.00 83.43  ? 170  ILE A O   1 
ATOM   995  C CB  . ILE A 1 144 ? -72.605  -28.462 -9.868  1.00 105.22 ? 170  ILE A CB  1 
ATOM   996  C CG1 . ILE A 1 144 ? -71.847  -29.627 -10.462 1.00 105.92 ? 170  ILE A CG1 1 
ATOM   997  C CG2 . ILE A 1 144 ? -72.761  -27.443 -10.977 1.00 100.64 ? 170  ILE A CG2 1 
ATOM   998  C CD1 . ILE A 1 144 ? -70.442  -29.255 -10.865 1.00 105.48 ? 170  ILE A CD1 1 
ATOM   999  N N   . ASN A 1 145 ? -73.352  -26.329 -7.726  1.00 88.94  ? 171  ASN A N   1 
ATOM   1000 C CA  . ASN A 1 145 ? -73.840  -25.003 -7.420  1.00 82.77  ? 171  ASN A CA  1 
ATOM   1001 C C   . ASN A 1 145 ? -73.434  -24.513 -6.067  1.00 92.84  ? 171  ASN A C   1 
ATOM   1002 O O   . ASN A 1 145 ? -73.916  -23.506 -5.604  1.00 93.21  ? 171  ASN A O   1 
ATOM   1003 C CB  . ASN A 1 145 ? -75.331  -24.946 -7.542  1.00 81.05  ? 171  ASN A CB  1 
ATOM   1004 C CG  . ASN A 1 145 ? -75.765  -25.065 -8.955  1.00 94.03  ? 171  ASN A CG  1 
ATOM   1005 O OD1 . ASN A 1 145 ? -75.068  -25.655 -9.756  1.00 99.63  ? 171  ASN A OD1 1 
ATOM   1006 N ND2 . ASN A 1 145 ? -76.903  -24.496 -9.280  1.00 101.27 ? 171  ASN A ND2 1 
ATOM   1007 N N   . LEU A 1 146 ? -72.573  -25.256 -5.411  1.00 87.13  ? 172  LEU A N   1 
ATOM   1008 C CA  . LEU A 1 146 ? -72.162  -24.890 -4.091  1.00 92.96  ? 172  LEU A CA  1 
ATOM   1009 C C   . LEU A 1 146 ? -71.334  -23.640 -3.979  1.00 88.15  ? 172  LEU A C   1 
ATOM   1010 O O   . LEU A 1 146 ? -70.257  -23.542 -4.573  1.00 78.59  ? 172  LEU A O   1 
ATOM   1011 C CB  . LEU A 1 146 ? -71.368  -26.023 -3.450  1.00 89.74  ? 172  LEU A CB  1 
ATOM   1012 C CG  . LEU A 1 146 ? -72.135  -27.249 -2.988  1.00 78.53  ? 172  LEU A CG  1 
ATOM   1013 C CD1 . LEU A 1 146 ? -71.140  -28.305 -2.544  1.00 76.85  ? 172  LEU A CD1 1 
ATOM   1014 C CD2 . LEU A 1 146 ? -73.089  -26.875 -1.860  1.00 81.03  ? 172  LEU A CD2 1 
ATOM   1015 N N   . LYS A 1 147 ? -71.878  -22.678 -3.235  1.00 78.10  ? 173  LYS A N   1 
ATOM   1016 C CA  . LYS A 1 147 ? -71.182  -21.450 -2.934  1.00 85.13  ? 173  LYS A CA  1 
ATOM   1017 C C   . LYS A 1 147 ? -70.405  -21.722 -1.634  1.00 75.76  ? 173  LYS A C   1 
ATOM   1018 O O   . LYS A 1 147 ? -69.199  -21.504 -1.566  1.00 65.32  ? 173  LYS A O   1 
ATOM   1019 C CB  . LYS A 1 147 ? -72.124  -20.259 -2.702  1.00 93.36  ? 173  LYS A CB  1 
ATOM   1020 C CG  . LYS A 1 147 ? -72.793  -19.647 -3.924  1.00 109.56 ? 173  LYS A CG  1 
ATOM   1021 C CD  . LYS A 1 147 ? -73.463  -18.324 -3.520  1.00 113.85 ? 173  LYS A CD  1 
ATOM   1022 C CE  . LYS A 1 147 ? -74.051  -17.546 -4.691  1.00 106.60 ? 173  LYS A CE  1 
ATOM   1023 N NZ  . LYS A 1 147 ? -75.161  -18.259 -5.383  1.00 115.79 ? 173  LYS A NZ  1 
ATOM   1024 N N   . ASN A 1 148 ? -71.110  -22.246 -0.627  1.00 73.25  ? 174  ASN A N   1 
ATOM   1025 C CA  . ASN A 1 148 ? -70.520  -22.543 0.693   1.00 82.94  ? 174  ASN A CA  1 
ATOM   1026 C C   . ASN A 1 148 ? -70.560  -24.008 1.178   1.00 75.02  ? 174  ASN A C   1 
ATOM   1027 O O   . ASN A 1 148 ? -71.621  -24.582 1.433   1.00 72.90  ? 174  ASN A O   1 
ATOM   1028 C CB  . ASN A 1 148 ? -71.218  -21.681 1.734   1.00 80.68  ? 174  ASN A CB  1 
ATOM   1029 C CG  . ASN A 1 148 ? -71.112  -20.214 1.426   1.00 71.43  ? 174  ASN A CG  1 
ATOM   1030 O OD1 . ASN A 1 148 ? -70.235  -19.788 0.685   1.00 72.99  ? 174  ASN A OD1 1 
ATOM   1031 N ND2 . ASN A 1 148 ? -71.979  -19.433 2.020   1.00 66.82  ? 174  ASN A ND2 1 
ATOM   1032 N N   . LEU A 1 149 ? -69.387  -24.542 1.446   1.00 63.40  ? 175  LEU A N   1 
ATOM   1033 C CA  . LEU A 1 149 ? -69.259  -25.887 1.911   1.00 60.59  ? 175  LEU A CA  1 
ATOM   1034 C C   . LEU A 1 149 ? -68.501  -25.917 3.237   1.00 61.76  ? 175  LEU A C   1 
ATOM   1035 O O   . LEU A 1 149 ? -67.307  -25.591 3.281   1.00 56.44  ? 175  LEU A O   1 
ATOM   1036 C CB  . LEU A 1 149 ? -68.493  -26.717 0.877   1.00 70.70  ? 175  LEU A CB  1 
ATOM   1037 C CG  . LEU A 1 149 ? -68.233  -28.187 1.239   1.00 71.47  ? 175  LEU A CG  1 
ATOM   1038 C CD1 . LEU A 1 149 ? -69.560  -28.882 1.501   1.00 66.26  ? 175  LEU A CD1 1 
ATOM   1039 C CD2 . LEU A 1 149 ? -67.432  -28.905 0.157   1.00 64.95  ? 175  LEU A CD2 1 
ATOM   1040 N N   . TYR A 1 150 ? -69.157  -26.432 4.282   1.00 62.76  ? 176  TYR A N   1 
ATOM   1041 C CA  . TYR A 1 150 ? -68.552  -26.532 5.611   1.00 60.19  ? 176  TYR A CA  1 
ATOM   1042 C C   . TYR A 1 150 ? -68.258  -27.983 6.058   1.00 67.39  ? 176  TYR A C   1 
ATOM   1043 O O   . TYR A 1 150 ? -69.173  -28.764 6.333   1.00 64.31  ? 176  TYR A O   1 
ATOM   1044 C CB  . TYR A 1 150 ? -69.470  -25.879 6.630   1.00 64.53  ? 176  TYR A CB  1 
ATOM   1045 C CG  . TYR A 1 150 ? -69.746  -24.402 6.414   1.00 68.23  ? 176  TYR A CG  1 
ATOM   1046 C CD1 . TYR A 1 150 ? -70.856  -23.978 5.698   1.00 72.85  ? 176  TYR A CD1 1 
ATOM   1047 C CD2 . TYR A 1 150 ? -68.927  -23.432 6.971   1.00 62.95  ? 176  TYR A CD2 1 
ATOM   1048 C CE1 . TYR A 1 150 ? -71.131  -22.625 5.534   1.00 64.98  ? 176  TYR A CE1 1 
ATOM   1049 C CE2 . TYR A 1 150 ? -69.213  -22.092 6.829   1.00 57.59  ? 176  TYR A CE2 1 
ATOM   1050 C CZ  . TYR A 1 150 ? -70.312  -21.699 6.105   1.00 56.79  ? 176  TYR A CZ  1 
ATOM   1051 O OH  . TYR A 1 150 ? -70.586  -20.362 5.947   1.00 69.44  ? 176  TYR A OH  1 
ATOM   1052 N N   . LEU A 1 151 ? -66.988  -28.300 6.257   1.00 65.71  ? 177  LEU A N   1 
ATOM   1053 C CA  . LEU A 1 151 ? -66.606  -29.648 6.668   1.00 60.71  ? 177  LEU A CA  1 
ATOM   1054 C C   . LEU A 1 151 ? -65.742  -29.675 7.923   1.00 66.27  ? 177  LEU A C   1 
ATOM   1055 O O   . LEU A 1 151 ? -64.956  -30.601 8.147   1.00 59.83  ? 177  LEU A O   1 
ATOM   1056 C CB  . LEU A 1 151 ? -65.844  -30.311 5.525   1.00 59.83  ? 177  LEU A CB  1 
ATOM   1057 C CG  . LEU A 1 151 ? -66.651  -30.429 4.230   1.00 71.91  ? 177  LEU A CG  1 
ATOM   1058 C CD1 . LEU A 1 151 ? -65.781  -31.095 3.179   1.00 71.92  ? 177  LEU A CD1 1 
ATOM   1059 C CD2 . LEU A 1 151 ? -67.949  -31.205 4.436   1.00 66.43  ? 177  LEU A CD2 1 
ATOM   1060 N N   . ALA A 1 152 ? -65.929  -28.704 8.787   1.00 67.16  ? 178  ALA A N   1 
ATOM   1061 C CA  . ALA A 1 152 ? -65.111  -28.647 9.982   1.00 71.84  ? 178  ALA A CA  1 
ATOM   1062 C C   . ALA A 1 152 ? -65.476  -29.684 11.057  1.00 69.08  ? 178  ALA A C   1 
ATOM   1063 O O   . ALA A 1 152 ? -66.630  -30.114 11.171  1.00 64.02  ? 178  ALA A O   1 
ATOM   1064 C CB  . ALA A 1 152 ? -65.196  -27.246 10.572  1.00 69.44  ? 178  ALA A CB  1 
ATOM   1065 N N   . TRP A 1 153 ? -64.516  -30.020 11.895  1.00 71.48  ? 179  TRP A N   1 
ATOM   1066 C CA  . TRP A 1 153 ? -64.759  -30.928 12.978  1.00 79.35  ? 179  TRP A CA  1 
ATOM   1067 C C   . TRP A 1 153 ? -65.222  -32.312 12.606  1.00 73.81  ? 179  TRP A C   1 
ATOM   1068 O O   . TRP A 1 153 ? -66.242  -32.806 13.113  1.00 60.68  ? 179  TRP A O   1 
ATOM   1069 C CB  . TRP A 1 153 ? -65.754  -30.289 13.929  1.00 76.84  ? 179  TRP A CB  1 
ATOM   1070 C CG  . TRP A 1 153 ? -65.301  -29.030 14.576  1.00 80.66  ? 179  TRP A CG  1 
ATOM   1071 C CD1 . TRP A 1 153 ? -65.661  -27.741 14.253  1.00 87.41  ? 179  TRP A CD1 1 
ATOM   1072 C CD2 . TRP A 1 153 ? -64.422  -28.898 15.714  1.00 83.15  ? 179  TRP A CD2 1 
ATOM   1073 N NE1 . TRP A 1 153 ? -65.070  -26.852 15.081  1.00 72.50  ? 179  TRP A NE1 1 
ATOM   1074 C CE2 . TRP A 1 153 ? -64.315  -27.479 15.979  1.00 88.37  ? 179  TRP A CE2 1 
ATOM   1075 C CE3 . TRP A 1 153 ? -63.732  -29.780 16.508  1.00 90.19  ? 179  TRP A CE3 1 
ATOM   1076 C CZ2 . TRP A 1 153 ? -63.542  -26.986 16.994  1.00 86.11  ? 179  TRP A CZ2 1 
ATOM   1077 C CZ3 . TRP A 1 153 ? -62.950  -29.270 17.530  1.00 89.34  ? 179  TRP A CZ3 1 
ATOM   1078 C CH2 . TRP A 1 153 ? -62.863  -27.906 17.767  1.00 90.07  ? 179  TRP A CH2 1 
ATOM   1079 N N   . ASN A 1 154 ? -64.523  -32.957 11.686  1.00 67.63  ? 180  ASN A N   1 
ATOM   1080 C CA  . ASN A 1 154 ? -64.799  -34.355 11.440  1.00 75.04  ? 180  ASN A CA  1 
ATOM   1081 C C   . ASN A 1 154 ? -63.757  -35.348 11.917  1.00 79.02  ? 180  ASN A C   1 
ATOM   1082 O O   . ASN A 1 154 ? -64.059  -36.209 12.701  1.00 93.15  ? 180  ASN A O   1 
ATOM   1083 C CB  . ASN A 1 154 ? -65.188  -34.569 9.999   1.00 65.57  ? 180  ASN A CB  1 
ATOM   1084 C CG  . ASN A 1 154 ? -66.557  -34.043 9.721   1.00 74.47  ? 180  ASN A CG  1 
ATOM   1085 O OD1 . ASN A 1 154 ? -67.408  -34.723 9.206   1.00 72.23  ? 180  ASN A OD1 1 
ATOM   1086 N ND2 . ASN A 1 154 ? -66.785  -32.831 10.111  1.00 97.44  ? 180  ASN A ND2 1 
ATOM   1087 N N   . CYS A 1 155 ? -62.525  -35.185 11.502  1.00 76.47  ? 181  CYS A N   1 
ATOM   1088 C CA  . CYS A 1 155 ? -61.440  -36.040 11.906  1.00 83.89  ? 181  CYS A CA  1 
ATOM   1089 C C   . CYS A 1 155 ? -60.576  -35.289 12.882  1.00 86.66  ? 181  CYS A C   1 
ATOM   1090 O O   . CYS A 1 155 ? -59.358  -35.218 12.713  1.00 90.98  ? 181  CYS A O   1 
ATOM   1091 C CB  . CYS A 1 155 ? -60.589  -36.440 10.707  1.00 106.60 ? 181  CYS A CB  1 
ATOM   1092 S SG  . CYS A 1 155 ? -59.213  -37.551 11.111  1.00 120.81 ? 181  CYS A SG  1 
ATOM   1093 N N   . TYR A 1 156 ? -61.179  -34.644 13.868  1.00 90.54  ? 182  TYR A N   1 
ATOM   1094 C CA  . TYR A 1 156 ? -60.337  -33.939 14.803  1.00 103.74 ? 182  TYR A CA  1 
ATOM   1095 C C   . TYR A 1 156 ? -59.894  -34.941 15.825  1.00 120.46 ? 182  TYR A C   1 
ATOM   1096 O O   . TYR A 1 156 ? -60.632  -35.272 16.764  1.00 118.01 ? 182  TYR A O   1 
ATOM   1097 C CB  . TYR A 1 156 ? -60.991  -32.719 15.440  1.00 99.57  ? 182  TYR A CB  1 
ATOM   1098 C CG  . TYR A 1 156 ? -59.970  -31.903 16.227  1.00 98.79  ? 182  TYR A CG  1 
ATOM   1099 C CD1 . TYR A 1 156 ? -58.812  -31.431 15.596  1.00 95.34  ? 182  TYR A CD1 1 
ATOM   1100 C CD2 . TYR A 1 156 ? -60.241  -31.447 17.515  1.00 108.62 ? 182  TYR A CD2 1 
ATOM   1101 C CE1 . TYR A 1 156 ? -57.887  -30.660 16.271  1.00 96.74  ? 182  TYR A CE1 1 
ATOM   1102 C CE2 . TYR A 1 156 ? -59.331  -30.650 18.199  1.00 104.67 ? 182  TYR A CE2 1 
ATOM   1103 C CZ  . TYR A 1 156 ? -58.157  -30.255 17.570  1.00 109.33 ? 182  TYR A CZ  1 
ATOM   1104 O OH  . TYR A 1 156 ? -57.253  -29.452 18.230  1.00 102.29 ? 182  TYR A OH  1 
ATOM   1105 N N   . PHE A 1 157 ? -58.687  -35.451 15.606  1.00 135.81 ? 183  PHE A N   1 
ATOM   1106 C CA  . PHE A 1 157 ? -58.112  -36.447 16.477  1.00 148.95 ? 183  PHE A CA  1 
ATOM   1107 C C   . PHE A 1 157 ? -58.535  -36.198 17.941  1.00 143.41 ? 183  PHE A C   1 
ATOM   1108 O O   . PHE A 1 157 ? -58.363  -35.091 18.487  1.00 109.14 ? 183  PHE A O   1 
ATOM   1109 C CB  . PHE A 1 157 ? -56.581  -36.487 16.331  1.00 152.26 ? 183  PHE A CB  1 
ATOM   1110 C CG  . PHE A 1 157 ? -55.887  -35.268 16.857  1.00 155.49 ? 183  PHE A CG  1 
ATOM   1111 C CD1 . PHE A 1 157 ? -55.555  -34.220 16.012  1.00 155.25 ? 183  PHE A CD1 1 
ATOM   1112 C CD2 . PHE A 1 157 ? -55.579  -35.163 18.208  1.00 143.86 ? 183  PHE A CD2 1 
ATOM   1113 C CE1 . PHE A 1 157 ? -54.909  -33.099 16.501  1.00 146.06 ? 183  PHE A CE1 1 
ATOM   1114 C CE2 . PHE A 1 157 ? -54.947  -34.041 18.704  1.00 138.48 ? 183  PHE A CE2 1 
ATOM   1115 C CZ  . PHE A 1 157 ? -54.603  -33.011 17.848  1.00 139.89 ? 183  PHE A CZ  1 
ATOM   1116 N N   . ASN A 1 158 ? -59.102  -37.229 18.562  1.00 132.43 ? 184  ASN A N   1 
ATOM   1117 C CA  . ASN A 1 158 ? -59.307  -38.519 17.902  1.00 147.51 ? 184  ASN A CA  1 
ATOM   1118 C C   . ASN A 1 158 ? -60.791  -38.787 17.801  1.00 127.14 ? 184  ASN A C   1 
ATOM   1119 O O   . ASN A 1 158 ? -61.597  -37.978 18.265  1.00 106.81 ? 184  ASN A O   1 
ATOM   1120 C CB  . ASN A 1 158 ? -58.716  -39.662 18.757  1.00 173.68 ? 184  ASN A CB  1 
ATOM   1121 C CG  . ASN A 1 158 ? -57.250  -39.458 19.132  1.00 186.95 ? 184  ASN A CG  1 
ATOM   1122 O OD1 . ASN A 1 158 ? -56.743  -40.121 20.040  1.00 188.03 ? 184  ASN A OD1 1 
ATOM   1123 N ND2 . ASN A 1 158 ? -56.581  -38.530 18.476  1.00 190.08 ? 184  ASN A ND2 1 
ATOM   1124 N N   . LYS A 1 159 ? -61.143  -39.848 17.078  1.00 113.07 ? 185  LYS A N   1 
ATOM   1125 C CA  . LYS A 1 159 ? -62.540  -40.289 16.980  1.00 142.30 ? 185  LYS A CA  1 
ATOM   1126 C C   . LYS A 1 159 ? -62.773  -41.822 17.166  1.00 136.41 ? 185  LYS A C   1 
ATOM   1127 O O   . LYS A 1 159 ? -63.878  -42.205 17.544  1.00 123.38 ? 185  LYS A O   1 
ATOM   1128 C CB  . LYS A 1 159 ? -63.285  -39.770 15.735  1.00 163.01 ? 185  LYS A CB  1 
ATOM   1129 C CG  . LYS A 1 159 ? -63.513  -38.254 15.648  1.00 154.54 ? 185  LYS A CG  1 
ATOM   1130 C CD  . LYS A 1 159 ? -64.143  -37.561 16.876  1.00 148.99 ? 185  LYS A CD  1 
ATOM   1131 C CE  . LYS A 1 159 ? -65.509  -38.065 17.365  1.00 151.92 ? 185  LYS A CE  1 
ATOM   1132 N NZ  . LYS A 1 159 ? -65.522  -39.348 18.136  1.00 149.93 ? 185  LYS A NZ  1 
ATOM   1133 N N   . VAL A 1 160 ? -61.791  -42.704 16.923  1.00 144.25 ? 186  VAL A N   1 
ATOM   1134 C CA  . VAL A 1 160 ? -60.434  -42.376 16.466  1.00 160.69 ? 186  VAL A CA  1 
ATOM   1135 C C   . VAL A 1 160 ? -60.436  -42.121 14.966  1.00 162.15 ? 186  VAL A C   1 
ATOM   1136 O O   . VAL A 1 160 ? -61.306  -42.612 14.235  1.00 132.44 ? 186  VAL A O   1 
ATOM   1137 C CB  . VAL A 1 160 ? -59.413  -43.520 16.786  1.00 157.54 ? 186  VAL A CB  1 
ATOM   1138 C CG1 . VAL A 1 160 ? -58.072  -43.303 16.080  1.00 143.19 ? 186  VAL A CG1 1 
ATOM   1139 C CG2 . VAL A 1 160 ? -59.206  -43.666 18.289  1.00 143.26 ? 186  VAL A CG2 1 
ATOM   1140 N N   . CYS A 1 161 ? -59.473  -41.317 14.528  1.00 162.93 ? 187  CYS A N   1 
ATOM   1141 C CA  . CYS A 1 161 ? -59.326  -40.982 13.131  1.00 136.71 ? 187  CYS A CA  1 
ATOM   1142 C C   . CYS A 1 161 ? -57.901  -40.554 12.844  1.00 130.98 ? 187  CYS A C   1 
ATOM   1143 O O   . CYS A 1 161 ? -57.410  -39.579 13.418  1.00 132.90 ? 187  CYS A O   1 
ATOM   1144 C CB  . CYS A 1 161 ? -60.270  -39.863 12.748  1.00 131.00 ? 187  CYS A CB  1 
ATOM   1145 S SG  . CYS A 1 161 ? -60.061  -39.393 11.021  1.00 167.67 ? 187  CYS A SG  1 
ATOM   1146 N N   . GLU A 1 162 ? -57.243  -41.291 11.954  1.00 126.86 ? 188  GLU A N   1 
ATOM   1147 C CA  . GLU A 1 162 ? -55.864  -40.995 11.577  1.00 130.34 ? 188  GLU A CA  1 
ATOM   1148 C C   . GLU A 1 162 ? -55.747  -39.615 10.894  1.00 126.96 ? 188  GLU A C   1 
ATOM   1149 O O   . GLU A 1 162 ? -55.171  -38.688 11.471  1.00 120.33 ? 188  GLU A O   1 
ATOM   1150 C CB  . GLU A 1 162 ? -55.262  -42.143 10.727  1.00 142.21 ? 188  GLU A CB  1 
ATOM   1151 C CG  . GLU A 1 162 ? -56.067  -42.564 9.494   1.00 143.28 ? 188  GLU A CG  1 
ATOM   1152 C CD  . GLU A 1 162 ? -55.388  -43.654 8.677   1.00 141.84 ? 188  GLU A CD  1 
ATOM   1153 O OE1 . GLU A 1 162 ? -55.947  -44.041 7.631   1.00 147.27 ? 188  GLU A OE1 1 
ATOM   1154 O OE2 . GLU A 1 162 ? -54.285  -44.103 9.057   1.00 142.13 ? 188  GLU A OE2 1 
ATOM   1155 N N   . LYS A 1 163 ? -56.292  -39.489 9.682   1.00 115.06 ? 189  LYS A N   1 
ATOM   1156 C CA  . LYS A 1 163 ? -56.279  -38.235 8.919   1.00 115.77 ? 189  LYS A CA  1 
ATOM   1157 C C   . LYS A 1 163 ? -57.544  -38.190 8.094   1.00 106.80 ? 189  LYS A C   1 
ATOM   1158 O O   . LYS A 1 163 ? -58.257  -39.180 8.008   1.00 87.72  ? 189  LYS A O   1 
ATOM   1159 C CB  . LYS A 1 163 ? -55.096  -38.124 7.925   1.00 123.43 ? 189  LYS A CB  1 
ATOM   1160 C CG  . LYS A 1 163 ? -53.677  -38.135 8.488   1.00 132.85 ? 189  LYS A CG  1 
ATOM   1161 C CD  . LYS A 1 163 ? -53.253  -39.498 9.016   1.00 137.12 ? 189  LYS A CD  1 
ATOM   1162 C CE  . LYS A 1 163 ? -51.814  -39.487 9.510   1.00 142.36 ? 189  LYS A CE  1 
ATOM   1163 N NZ  . LYS A 1 163 ? -51.387  -40.826 10.007  1.00 148.71 ? 189  LYS A NZ  1 
ATOM   1164 N N   . THR A 1 164 ? -57.886  -37.011 7.582   1.00 105.61 ? 190  THR A N   1 
ATOM   1165 C CA  . THR A 1 164 ? -59.044  -36.898 6.717   1.00 98.60  ? 190  THR A CA  1 
ATOM   1166 C C   . THR A 1 164 ? -58.494  -37.190 5.350   1.00 99.93  ? 190  THR A C   1 
ATOM   1167 O O   . THR A 1 164 ? -57.319  -36.928 5.086   1.00 94.30  ? 190  THR A O   1 
ATOM   1168 C CB  . THR A 1 164 ? -59.740  -35.515 6.736   1.00 87.15  ? 190  THR A CB  1 
ATOM   1169 O OG1 . THR A 1 164 ? -60.674  -35.459 7.825   1.00 77.33  ? 190  THR A OG1 1 
ATOM   1170 C CG2 . THR A 1 164 ? -60.568  -35.330 5.484   1.00 86.64  ? 190  THR A CG2 1 
ATOM   1171 N N   . ASN A 1 165 ? -59.278  -37.899 4.552   1.00 95.70  ? 191  ASN A N   1 
ATOM   1172 C CA  . ASN A 1 165 ? -58.868  -38.215 3.213   1.00 86.64  ? 191  ASN A CA  1 
ATOM   1173 C C   . ASN A 1 165 ? -59.763  -37.475 2.262   1.00 75.54  ? 191  ASN A C   1 
ATOM   1174 O O   . ASN A 1 165 ? -61.001  -37.556 2.352   1.00 69.85  ? 191  ASN A O   1 
ATOM   1175 C CB  . ASN A 1 165 ? -58.993  -39.689 2.888   1.00 86.46  ? 191  ASN A CB  1 
ATOM   1176 C CG  . ASN A 1 165 ? -58.570  -39.981 1.458   1.00 88.69  ? 191  ASN A CG  1 
ATOM   1177 O OD1 . ASN A 1 165 ? -57.376  -39.967 1.139   1.00 80.32  ? 191  ASN A OD1 1 
ATOM   1178 N ND2 . ASN A 1 165 ? -59.547  -40.283 0.594   1.00 71.98  ? 191  ASN A ND2 1 
ATOM   1179 N N   . ILE A 1 166 ? -59.122  -36.819 1.308   1.00 74.02  ? 192  ILE A N   1 
ATOM   1180 C CA  . ILE A 1 166 ? -59.790  -36.038 0.277   1.00 88.57  ? 192  ILE A CA  1 
ATOM   1181 C C   . ILE A 1 166 ? -59.269  -36.618 -1.014  1.00 87.88  ? 192  ILE A C   1 
ATOM   1182 O O   . ILE A 1 166 ? -58.076  -36.489 -1.299  1.00 85.69  ? 192  ILE A O   1 
ATOM   1183 C CB  . ILE A 1 166 ? -59.363  -34.560 0.416   1.00 97.48  ? 192  ILE A CB  1 
ATOM   1184 C CG1 . ILE A 1 166 ? -59.890  -34.016 1.752   1.00 97.85  ? 192  ILE A CG1 1 
ATOM   1185 C CG2 . ILE A 1 166 ? -59.924  -33.730 -0.731  1.00 103.20 ? 192  ILE A CG2 1 
ATOM   1186 C CD1 . ILE A 1 166 ? -59.210  -32.759 2.222   1.00 87.91  ? 192  ILE A CD1 1 
ATOM   1187 N N   . GLU A 1 167 ? -60.095  -37.295 -1.787  1.00 86.50  ? 193  GLU A N   1 
ATOM   1188 C CA  . GLU A 1 167 ? -59.559  -37.838 -3.021  1.00 110.95 ? 193  GLU A CA  1 
ATOM   1189 C C   . GLU A 1 167 ? -59.332  -36.735 -4.026  1.00 100.70 ? 193  GLU A C   1 
ATOM   1190 O O   . GLU A 1 167 ? -60.118  -35.814 -4.148  1.00 93.96  ? 193  GLU A O   1 
ATOM   1191 C CB  . GLU A 1 167 ? -60.394  -38.992 -3.584  1.00 124.30 ? 193  GLU A CB  1 
ATOM   1192 C CG  . GLU A 1 167 ? -59.635  -39.974 -4.489  1.00 126.82 ? 193  GLU A CG  1 
ATOM   1193 C CD  . GLU A 1 167 ? -58.328  -40.516 -3.914  1.00 118.24 ? 193  GLU A CD  1 
ATOM   1194 O OE1 . GLU A 1 167 ? -57.286  -40.400 -4.586  1.00 97.65  ? 193  GLU A OE1 1 
ATOM   1195 O OE2 . GLU A 1 167 ? -58.339  -41.093 -2.814  1.00 98.75  ? 193  GLU A OE2 1 
ATOM   1196 N N   . ASP A 1 168 ? -58.254  -36.870 -4.770  1.00 91.31  ? 194  ASP A N   1 
ATOM   1197 C CA  . ASP A 1 168 ? -57.699  -35.794 -5.534  1.00 87.93  ? 194  ASP A CA  1 
ATOM   1198 C C   . ASP A 1 168 ? -58.751  -35.292 -6.488  1.00 86.98  ? 194  ASP A C   1 
ATOM   1199 O O   . ASP A 1 168 ? -59.391  -36.067 -7.156  1.00 95.25  ? 194  ASP A O   1 
ATOM   1200 C CB  . ASP A 1 168 ? -56.483  -36.360 -6.255  1.00 84.33  ? 194  ASP A CB  1 
ATOM   1201 C CG  . ASP A 1 168 ? -55.987  -35.496 -7.361  1.00 97.62  ? 194  ASP A CG  1 
ATOM   1202 O OD1 . ASP A 1 168 ? -56.747  -35.237 -8.300  1.00 110.56 ? 194  ASP A OD1 1 
ATOM   1203 O OD2 . ASP A 1 168 ? -54.805  -35.122 -7.324  1.00 96.26  ? 194  ASP A OD2 1 
ATOM   1204 N N   . GLY A 1 169 ? -58.918  -33.978 -6.542  1.00 81.83  ? 195  GLY A N   1 
ATOM   1205 C CA  . GLY A 1 169 ? -59.876  -33.334 -7.415  1.00 68.54  ? 195  GLY A CA  1 
ATOM   1206 C C   . GLY A 1 169 ? -61.296  -33.229 -6.920  1.00 73.56  ? 195  GLY A C   1 
ATOM   1207 O O   . GLY A 1 169 ? -62.158  -32.738 -7.609  1.00 85.71  ? 195  GLY A O   1 
ATOM   1208 N N   . VAL A 1 170 ? -61.554  -33.674 -5.717  1.00 68.65  ? 196  VAL A N   1 
ATOM   1209 C CA  . VAL A 1 170 ? -62.916  -33.635 -5.212  1.00 81.46  ? 196  VAL A CA  1 
ATOM   1210 C C   . VAL A 1 170 ? -63.558  -32.258 -5.419  1.00 87.37  ? 196  VAL A C   1 
ATOM   1211 O O   . VAL A 1 170 ? -64.754  -32.155 -5.702  1.00 81.83  ? 196  VAL A O   1 
ATOM   1212 C CB  . VAL A 1 170 ? -62.994  -33.858 -3.683  1.00 87.11  ? 196  VAL A CB  1 
ATOM   1213 C CG1 . VAL A 1 170 ? -64.439  -34.159 -3.281  1.00 80.09  ? 196  VAL A CG1 1 
ATOM   1214 C CG2 . VAL A 1 170 ? -62.031  -34.923 -3.202  1.00 92.39  ? 196  VAL A CG2 1 
ATOM   1215 N N   . PHE A 1 171 ? -62.766  -31.200 -5.237  1.00 90.50  ? 197  PHE A N   1 
ATOM   1216 C CA  . PHE A 1 171 ? -63.290  -29.838 -5.338  1.00 90.80  ? 197  PHE A CA  1 
ATOM   1217 C C   . PHE A 1 171 ? -63.193  -29.109 -6.671  1.00 98.26  ? 197  PHE A C   1 
ATOM   1218 O O   . PHE A 1 171 ? -64.094  -28.327 -6.993  1.00 72.49  ? 197  PHE A O   1 
ATOM   1219 C CB  . PHE A 1 171 ? -62.647  -28.959 -4.276  1.00 85.51  ? 197  PHE A CB  1 
ATOM   1220 C CG  . PHE A 1 171 ? -62.817  -29.474 -2.884  1.00 73.34  ? 197  PHE A CG  1 
ATOM   1221 C CD1 . PHE A 1 171 ? -64.049  -29.413 -2.263  1.00 69.84  ? 197  PHE A CD1 1 
ATOM   1222 C CD2 . PHE A 1 171 ? -61.718  -29.892 -2.150  1.00 67.07  ? 197  PHE A CD2 1 
ATOM   1223 C CE1 . PHE A 1 171 ? -64.211  -29.870 -0.967  1.00 64.65  ? 197  PHE A CE1 1 
ATOM   1224 C CE2 . PHE A 1 171 ? -61.868  -30.340 -0.858  1.00 62.63  ? 197  PHE A CE2 1 
ATOM   1225 C CZ  . PHE A 1 171 ? -63.121  -30.329 -0.266  1.00 59.25  ? 197  PHE A CZ  1 
ATOM   1226 N N   . GLU A 1 172 ? -62.136  -29.359 -7.448  1.00 102.65 ? 198  GLU A N   1 
ATOM   1227 C CA  . GLU A 1 172 ? -61.954  -28.663 -8.738  1.00 101.34 ? 198  GLU A CA  1 
ATOM   1228 C C   . GLU A 1 172 ? -63.214  -28.553 -9.587  1.00 85.62  ? 198  GLU A C   1 
ATOM   1229 O O   . GLU A 1 172 ? -63.366  -27.591 -10.337 1.00 88.12  ? 198  GLU A O   1 
ATOM   1230 C CB  . GLU A 1 172 ? -60.842  -29.282 -9.580  1.00 100.26 ? 198  GLU A CB  1 
ATOM   1231 C CG  . GLU A 1 172 ? -61.123  -30.696 -10.044 1.00 114.74 ? 198  GLU A CG  1 
ATOM   1232 C CD  . GLU A 1 172 ? -60.027  -31.236 -10.944 1.00 120.28 ? 198  GLU A CD  1 
ATOM   1233 O OE1 . GLU A 1 172 ? -59.054  -30.487 -11.201 1.00 108.98 ? 198  GLU A OE1 1 
ATOM   1234 O OE2 . GLU A 1 172 ? -60.145  -32.403 -11.397 1.00 107.38 ? 198  GLU A OE2 1 
ATOM   1235 N N   . THR A 1 173 ? -64.139  -29.491 -9.440  1.00 76.99  ? 199  THR A N   1 
ATOM   1236 C CA  . THR A 1 173 ? -65.367  -29.445 -10.246 1.00 91.23  ? 199  THR A CA  1 
ATOM   1237 C C   . THR A 1 173 ? -66.383  -28.465 -9.680  1.00 79.83  ? 199  THR A C   1 
ATOM   1238 O O   . THR A 1 173 ? -67.459  -28.298 -10.244 1.00 93.13  ? 199  THR A O   1 
ATOM   1239 C CB  . THR A 1 173 ? -66.048  -30.845 -10.382 1.00 108.88 ? 199  THR A CB  1 
ATOM   1240 O OG1 . THR A 1 173 ? -66.697  -31.233 -9.156  1.00 98.57  ? 199  THR A OG1 1 
ATOM   1241 C CG2 . THR A 1 173 ? -65.024  -31.918 -10.824 1.00 100.39 ? 199  THR A CG2 1 
ATOM   1242 N N   . LEU A 1 174 ? -66.078  -27.907 -8.512  1.00 92.12  ? 200  LEU A N   1 
ATOM   1243 C CA  . LEU A 1 174 ? -66.951  -26.943 -7.825  1.00 95.09  ? 200  LEU A CA  1 
ATOM   1244 C C   . LEU A 1 174 ? -66.441  -25.558 -8.169  1.00 98.98  ? 200  LEU A C   1 
ATOM   1245 O O   . LEU A 1 174 ? -65.745  -24.897 -7.378  1.00 89.44  ? 200  LEU A O   1 
ATOM   1246 C CB  . LEU A 1 174 ? -66.883  -27.171 -6.322  1.00 100.24 ? 200  LEU A CB  1 
ATOM   1247 C CG  . LEU A 1 174 ? -67.335  -28.555 -5.877  1.00 99.93  ? 200  LEU A CG  1 
ATOM   1248 C CD1 . LEU A 1 174 ? -67.009  -28.754 -4.406  1.00 99.86  ? 200  LEU A CD1 1 
ATOM   1249 C CD2 . LEU A 1 174 ? -68.822  -28.751 -6.171  1.00 90.99  ? 200  LEU A CD2 1 
ATOM   1250 N N   . THR A 1 175 ? -66.859  -25.105 -9.339  1.00 96.23  ? 201  THR A N   1 
ATOM   1251 C CA  . THR A 1 175 ? -66.426  -23.838 -9.881  1.00 83.16  ? 201  THR A CA  1 
ATOM   1252 C C   . THR A 1 175 ? -67.140  -22.588 -9.394  1.00 80.54  ? 201  THR A C   1 
ATOM   1253 O O   . THR A 1 175 ? -66.809  -21.487 -9.842  1.00 77.11  ? 201  THR A O   1 
ATOM   1254 C CB  . THR A 1 175 ? -66.448  -23.905 -11.404 1.00 82.53  ? 201  THR A CB  1 
ATOM   1255 O OG1 . THR A 1 175 ? -67.793  -24.118 -11.860 1.00 74.65  ? 201  THR A OG1 1 
ATOM   1256 C CG2 . THR A 1 175 ? -65.531  -25.042 -11.875 1.00 70.16  ? 201  THR A CG2 1 
ATOM   1257 N N   . ASN A 1 176 ? -68.142  -22.752 -8.536  1.00 68.98  ? 202  ASN A N   1 
ATOM   1258 C CA  . ASN A 1 176 ? -68.856  -21.606 -7.953  1.00 81.23  ? 202  ASN A CA  1 
ATOM   1259 C C   . ASN A 1 176 ? -68.615  -21.617 -6.444  1.00 79.57  ? 202  ASN A C   1 
ATOM   1260 O O   . ASN A 1 176 ? -69.348  -20.985 -5.663  1.00 66.40  ? 202  ASN A O   1 
ATOM   1261 C CB  . ASN A 1 176 ? -70.350  -21.715 -8.204  1.00 83.26  ? 202  ASN A CB  1 
ATOM   1262 C CG  . ASN A 1 176 ? -70.688  -21.715 -9.663  1.00 96.43  ? 202  ASN A CG  1 
ATOM   1263 O OD1 . ASN A 1 176 ? -69.805  -21.698 -10.521 1.00 102.24 ? 202  ASN A OD1 1 
ATOM   1264 N ND2 . ASN A 1 176 ? -71.976  -21.746 -9.962  1.00 104.28 ? 202  ASN A ND2 1 
ATOM   1265 N N   . LEU A 1 177 ? -67.564  -22.319 -6.043  1.00 70.01  ? 203  LEU A N   1 
ATOM   1266 C CA  . LEU A 1 177 ? -67.267  -22.471 -4.641  1.00 78.14  ? 203  LEU A CA  1 
ATOM   1267 C C   . LEU A 1 177 ? -66.607  -21.230 -4.079  1.00 71.78  ? 203  LEU A C   1 
ATOM   1268 O O   . LEU A 1 177 ? -65.417  -20.957 -4.320  1.00 68.40  ? 203  LEU A O   1 
ATOM   1269 C CB  . LEU A 1 177 ? -66.384  -23.722 -4.405  1.00 75.39  ? 203  LEU A CB  1 
ATOM   1270 C CG  . LEU A 1 177 ? -66.225  -24.182 -2.941  1.00 63.56  ? 203  LEU A CG  1 
ATOM   1271 C CD1 . LEU A 1 177 ? -67.565  -24.578 -2.353  1.00 55.86  ? 203  LEU A CD1 1 
ATOM   1272 C CD2 . LEU A 1 177 ? -65.256  -25.346 -2.801  1.00 64.43  ? 203  LEU A CD2 1 
ATOM   1273 N N   . GLU A 1 178 ? -67.378  -20.483 -3.307  1.00 61.86  ? 204  GLU A N   1 
ATOM   1274 C CA  . GLU A 1 178 ? -66.853  -19.282 -2.688  1.00 69.38  ? 204  GLU A CA  1 
ATOM   1275 C C   . GLU A 1 178 ? -66.205  -19.492 -1.305  1.00 62.34  ? 204  GLU A C   1 
ATOM   1276 O O   . GLU A 1 178 ? -65.158  -18.928 -1.030  1.00 57.95  ? 204  GLU A O   1 
ATOM   1277 C CB  . GLU A 1 178 ? -67.914  -18.203 -2.670  1.00 68.54  ? 204  GLU A CB  1 
ATOM   1278 C CG  . GLU A 1 178 ? -68.197  -17.679 -4.063  1.00 74.28  ? 204  GLU A CG  1 
ATOM   1279 C CD  . GLU A 1 178 ? -69.300  -16.652 -4.094  1.00 81.77  ? 204  GLU A CD  1 
ATOM   1280 O OE1 . GLU A 1 178 ? -70.118  -16.593 -3.144  1.00 74.05  ? 204  GLU A OE1 1 
ATOM   1281 O OE2 . GLU A 1 178 ? -69.380  -15.940 -5.111  1.00 107.81 ? 204  GLU A OE2 1 
ATOM   1282 N N   . LEU A 1 179 ? -66.768  -20.369 -0.485  1.00 66.26  ? 205  LEU A N   1 
ATOM   1283 C CA  . LEU A 1 179 ? -66.224  -20.624 0.848   1.00 56.50  ? 205  LEU A CA  1 
ATOM   1284 C C   . LEU A 1 179 ? -66.049  -22.108 1.122   1.00 60.64  ? 205  LEU A C   1 
ATOM   1285 O O   . LEU A 1 179 ? -67.006  -22.897 1.036   1.00 59.12  ? 205  LEU A O   1 
ATOM   1286 C CB  . LEU A 1 179 ? -67.174  -20.053 1.904   1.00 54.72  ? 205  LEU A CB  1 
ATOM   1287 C CG  . LEU A 1 179 ? -66.759  -20.142 3.389   1.00 63.60  ? 205  LEU A CG  1 
ATOM   1288 C CD1 . LEU A 1 179 ? -67.760  -19.429 4.286   1.00 61.89  ? 205  LEU A CD1 1 
ATOM   1289 C CD2 . LEU A 1 179 ? -66.604  -21.570 3.856   1.00 68.72  ? 205  LEU A CD2 1 
ATOM   1290 N N   . LEU A 1 180 ? -64.845  -22.467 1.525   1.00 54.13  ? 206  LEU A N   1 
ATOM   1291 C CA  . LEU A 1 180 ? -64.516  -23.829 1.864   1.00 55.13  ? 206  LEU A CA  1 
ATOM   1292 C C   . LEU A 1 180 ? -63.916  -23.864 3.252   1.00 57.54  ? 206  LEU A C   1 
ATOM   1293 O O   . LEU A 1 180 ? -62.857  -23.270 3.481   1.00 49.90  ? 206  LEU A O   1 
ATOM   1294 C CB  . LEU A 1 180 ? -63.495  -24.441 0.879   1.00 56.21  ? 206  LEU A CB  1 
ATOM   1295 C CG  . LEU A 1 180 ? -63.059  -25.892 1.229   1.00 66.13  ? 206  LEU A CG  1 
ATOM   1296 C CD1 . LEU A 1 180 ? -64.260  -26.840 1.292   1.00 65.29  ? 206  LEU A CD1 1 
ATOM   1297 C CD2 . LEU A 1 180 ? -62.009  -26.443 0.270   1.00 59.63  ? 206  LEU A CD2 1 
ATOM   1298 N N   . SER A 1 181 ? -64.574  -24.578 4.169   1.00 59.23  ? 207  SER A N   1 
ATOM   1299 C CA  . SER A 1 181 ? -64.068  -24.723 5.533   1.00 56.78  ? 207  SER A CA  1 
ATOM   1300 C C   . SER A 1 181 ? -63.676  -26.156 5.892   1.00 59.67  ? 207  SER A C   1 
ATOM   1301 O O   . SER A 1 181 ? -64.535  -27.024 6.028   1.00 56.70  ? 207  SER A O   1 
ATOM   1302 C CB  . SER A 1 181 ? -65.083  -24.266 6.547   1.00 58.21  ? 207  SER A CB  1 
ATOM   1303 O OG  . SER A 1 181 ? -64.586  -24.574 7.851   1.00 62.06  ? 207  SER A OG  1 
ATOM   1304 N N   . LEU A 1 182 ? -62.393  -26.373 6.144   1.00 61.79  ? 208  LEU A N   1 
ATOM   1305 C CA  . LEU A 1 182 ? -61.886  -27.686 6.523   1.00 58.45  ? 208  LEU A CA  1 
ATOM   1306 C C   . LEU A 1 182 ? -61.174  -27.664 7.869   1.00 59.21  ? 208  LEU A C   1 
ATOM   1307 O O   . LEU A 1 182 ? -60.381  -28.542 8.161   1.00 59.85  ? 208  LEU A O   1 
ATOM   1308 C CB  . LEU A 1 182 ? -60.889  -28.183 5.467   1.00 60.93  ? 208  LEU A CB  1 
ATOM   1309 C CG  . LEU A 1 182 ? -61.479  -28.441 4.080   1.00 71.11  ? 208  LEU A CG  1 
ATOM   1310 C CD1 . LEU A 1 182 ? -60.389  -28.940 3.150   1.00 70.63  ? 208  LEU A CD1 1 
ATOM   1311 C CD2 . LEU A 1 182 ? -62.633  -29.443 4.148   1.00 73.17  ? 208  LEU A CD2 1 
ATOM   1312 N N   . SER A 1 183 ? -61.426  -26.656 8.689   1.00 68.26  ? 209  SER A N   1 
ATOM   1313 C CA  . SER A 1 183 ? -60.731  -26.571 9.977   1.00 66.64  ? 209  SER A CA  1 
ATOM   1314 C C   . SER A 1 183 ? -61.064  -27.720 10.923  1.00 67.28  ? 209  SER A C   1 
ATOM   1315 O O   . SER A 1 183 ? -62.148  -28.308 10.871  1.00 60.20  ? 209  SER A O   1 
ATOM   1316 C CB  . SER A 1 183 ? -60.999  -25.220 10.648  1.00 64.32  ? 209  SER A CB  1 
ATOM   1317 O OG  . SER A 1 183 ? -60.407  -24.156 9.910   1.00 66.09  ? 209  SER A OG  1 
ATOM   1318 N N   . PHE A 1 184 ? -60.105  -28.051 11.771  1.00 67.87  ? 210  PHE A N   1 
ATOM   1319 C CA  . PHE A 1 184 ? -60.280  -29.117 12.734  1.00 78.72  ? 210  PHE A CA  1 
ATOM   1320 C C   . PHE A 1 184 ? -60.539  -30.458 12.054  1.00 76.84  ? 210  PHE A C   1 
ATOM   1321 O O   . PHE A 1 184 ? -61.582  -31.105 12.257  1.00 57.38  ? 210  PHE A O   1 
ATOM   1322 C CB  . PHE A 1 184 ? -61.390  -28.771 13.727  1.00 77.40  ? 210  PHE A CB  1 
ATOM   1323 C CG  . PHE A 1 184 ? -61.117  -27.530 14.494  1.00 71.25  ? 210  PHE A CG  1 
ATOM   1324 C CD1 . PHE A 1 184 ? -61.708  -26.332 14.131  1.00 71.92  ? 210  PHE A CD1 1 
ATOM   1325 C CD2 . PHE A 1 184 ? -60.144  -27.525 15.482  1.00 70.16  ? 210  PHE A CD2 1 
ATOM   1326 C CE1 . PHE A 1 184 ? -61.422  -25.164 14.816  1.00 65.46  ? 210  PHE A CE1 1 
ATOM   1327 C CE2 . PHE A 1 184 ? -59.835  -26.362 16.163  1.00 67.47  ? 210  PHE A CE2 1 
ATOM   1328 C CZ  . PHE A 1 184 ? -60.476  -25.177 15.828  1.00 66.57  ? 210  PHE A CZ  1 
ATOM   1329 N N   . ASN A 1 185 ? -59.587  -30.801 11.199  1.00 66.21  ? 211  ASN A N   1 
ATOM   1330 C CA  . ASN A 1 185 ? -59.546  -32.032 10.438  1.00 60.73  ? 211  ASN A CA  1 
ATOM   1331 C C   . ASN A 1 185 ? -58.083  -32.233 10.152  1.00 72.21  ? 211  ASN A C   1 
ATOM   1332 O O   . ASN A 1 185 ? -57.367  -31.273 9.858   1.00 75.54  ? 211  ASN A O   1 
ATOM   1333 C CB  . ASN A 1 185 ? -60.310  -31.927 9.130   1.00 55.36  ? 211  ASN A CB  1 
ATOM   1334 C CG  . ASN A 1 185 ? -61.804  -31.941 9.315   1.00 58.59  ? 211  ASN A CG  1 
ATOM   1335 O OD1 . ASN A 1 185 ? -62.334  -32.705 10.109  1.00 87.18  ? 211  ASN A OD1 1 
ATOM   1336 N ND2 . ASN A 1 185 ? -62.497  -31.233 8.455   1.00 73.56  ? 211  ASN A ND2 1 
ATOM   1337 N N   . SER A 1 186 ? -57.595  -33.448 10.315  1.00 79.65  ? 212  SER A N   1 
ATOM   1338 C CA  . SER A 1 186 ? -56.187  -33.687 10.048  1.00 88.44  ? 212  SER A CA  1 
ATOM   1339 C C   . SER A 1 186 ? -55.934  -33.907 8.569   1.00 82.81  ? 212  SER A C   1 
ATOM   1340 O O   . SER A 1 186 ? -56.365  -34.910 7.992   1.00 91.71  ? 212  SER A O   1 
ATOM   1341 C CB  . SER A 1 186 ? -55.684  -34.829 10.895  1.00 86.08  ? 212  SER A CB  1 
ATOM   1342 O OG  . SER A 1 186 ? -56.597  -35.896 10.843  1.00 118.59 ? 212  SER A OG  1 
ATOM   1343 N N   . LEU A 1 187 ? -55.250  -32.941 7.959   1.00 69.54  ? 213  LEU A N   1 
ATOM   1344 C CA  . LEU A 1 187 ? -54.954  -32.997 6.555   1.00 65.73  ? 213  LEU A CA  1 
ATOM   1345 C C   . LEU A 1 187 ? -53.485  -33.191 6.274   1.00 59.89  ? 213  LEU A C   1 
ATOM   1346 O O   . LEU A 1 187 ? -53.125  -33.765 5.255   1.00 76.14  ? 213  LEU A O   1 
ATOM   1347 C CB  . LEU A 1 187 ? -55.393  -31.687 5.903   1.00 78.25  ? 213  LEU A CB  1 
ATOM   1348 C CG  . LEU A 1 187 ? -56.835  -31.249 6.143   1.00 73.79  ? 213  LEU A CG  1 
ATOM   1349 C CD1 . LEU A 1 187 ? -57.200  -30.066 5.248   1.00 74.20  ? 213  LEU A CD1 1 
ATOM   1350 C CD2 . LEU A 1 187 ? -57.761  -32.402 5.845   1.00 75.92  ? 213  LEU A CD2 1 
ATOM   1351 N N   . SER A 1 188 ? -52.642  -32.617 7.121   1.00 70.14  ? 214  SER A N   1 
ATOM   1352 C CA  . SER A 1 188 ? -51.177  -32.686 6.968   1.00 79.56  ? 214  SER A CA  1 
ATOM   1353 C C   . SER A 1 188 ? -50.687  -31.821 5.795   1.00 83.74  ? 214  SER A C   1 
ATOM   1354 O O   . SER A 1 188 ? -49.617  -31.189 5.868   1.00 83.16  ? 214  SER A O   1 
ATOM   1355 C CB  . SER A 1 188 ? -50.681  -34.137 6.816   1.00 93.66  ? 214  SER A CB  1 
ATOM   1356 O OG  . SER A 1 188 ? -50.906  -34.902 8.000   1.00 96.45  ? 214  SER A OG  1 
ATOM   1357 N N   . HIS A 1 189 ? -51.463  -31.798 4.716   1.00 80.20  ? 215  HIS A N   1 
ATOM   1358 C CA  . HIS A 1 189 ? -51.115  -31.022 3.542   1.00 78.64  ? 215  HIS A CA  1 
ATOM   1359 C C   . HIS A 1 189 ? -52.381  -30.412 3.016   1.00 76.86  ? 215  HIS A C   1 
ATOM   1360 O O   . HIS A 1 189 ? -53.458  -31.010 3.125   1.00 70.13  ? 215  HIS A O   1 
ATOM   1361 C CB  . HIS A 1 189 ? -50.499  -31.911 2.447   1.00 90.03  ? 215  HIS A CB  1 
ATOM   1362 C CG  . HIS A 1 189 ? -49.234  -32.605 2.860   1.00 111.20 ? 215  HIS A CG  1 
ATOM   1363 N ND1 . HIS A 1 189 ? -47.982  -32.065 2.647   1.00 126.10 ? 215  HIS A ND1 1 
ATOM   1364 C CD2 . HIS A 1 189 ? -49.026  -33.807 3.452   1.00 119.31 ? 215  HIS A CD2 1 
ATOM   1365 C CE1 . HIS A 1 189 ? -47.059  -32.901 3.092   1.00 123.19 ? 215  HIS A CE1 1 
ATOM   1366 N NE2 . HIS A 1 189 ? -47.666  -33.962 3.594   1.00 119.10 ? 215  HIS A NE2 1 
ATOM   1367 N N   . VAL A 1 190 ? -52.241  -29.226 2.433   1.00 72.18  ? 216  VAL A N   1 
ATOM   1368 C CA  . VAL A 1 190 ? -53.362  -28.508 1.859   1.00 64.52  ? 216  VAL A CA  1 
ATOM   1369 C C   . VAL A 1 190 ? -53.791  -29.324 0.656   1.00 61.36  ? 216  VAL A C   1 
ATOM   1370 O O   . VAL A 1 190 ? -52.958  -29.792 -0.105  1.00 71.50  ? 216  VAL A O   1 
ATOM   1371 C CB  . VAL A 1 190 ? -52.926  -27.108 1.365   1.00 76.69  ? 216  VAL A CB  1 
ATOM   1372 C CG1 . VAL A 1 190 ? -54.083  -26.378 0.699   1.00 76.03  ? 216  VAL A CG1 1 
ATOM   1373 C CG2 . VAL A 1 190 ? -52.364  -26.276 2.507   1.00 78.44  ? 216  VAL A CG2 1 
ATOM   1374 N N   . PRO A 1 191 ? -55.085  -29.489 0.459   1.00 56.82  ? 217  PRO A N   1 
ATOM   1375 C CA  . PRO A 1 191 ? -55.515  -30.280 -0.697  1.00 57.80  ? 217  PRO A CA  1 
ATOM   1376 C C   . PRO A 1 191 ? -55.277  -29.573 -2.013  1.00 77.67  ? 217  PRO A C   1 
ATOM   1377 O O   . PRO A 1 191 ? -55.455  -28.358 -2.091  1.00 81.81  ? 217  PRO A O   1 
ATOM   1378 C CB  . PRO A 1 191 ? -57.019  -30.444 -0.485  1.00 57.99  ? 217  PRO A CB  1 
ATOM   1379 C CG  . PRO A 1 191 ? -57.407  -29.429 0.538   1.00 62.11  ? 217  PRO A CG  1 
ATOM   1380 C CD  . PRO A 1 191 ? -56.188  -29.122 1.348   1.00 57.78  ? 217  PRO A CD  1 
ATOM   1381 N N   . PRO A 1 192 ? -54.884  -30.328 -3.056  1.00 85.69  ? 218  PRO A N   1 
ATOM   1382 C CA  . PRO A 1 192 ? -54.672  -29.676 -4.335  1.00 68.64  ? 218  PRO A CA  1 
ATOM   1383 C C   . PRO A 1 192 ? -55.934  -29.618 -5.151  1.00 73.59  ? 218  PRO A C   1 
ATOM   1384 O O   . PRO A 1 192 ? -57.023  -29.996 -4.679  1.00 71.74  ? 218  PRO A O   1 
ATOM   1385 C CB  . PRO A 1 192 ? -53.643  -30.574 -5.038  1.00 73.10  ? 218  PRO A CB  1 
ATOM   1386 C CG  . PRO A 1 192 ? -53.087  -31.462 -3.978  1.00 76.71  ? 218  PRO A CG  1 
ATOM   1387 C CD  . PRO A 1 192 ? -54.217  -31.635 -3.007  1.00 77.88  ? 218  PRO A CD  1 
ATOM   1388 N N   . LYS A 1 193 ? -55.788  -29.106 -6.365  1.00 76.83  ? 219  LYS A N   1 
ATOM   1389 C CA  . LYS A 1 193 ? -56.894  -28.989 -7.300  1.00 82.71  ? 219  LYS A CA  1 
ATOM   1390 C C   . LYS A 1 193 ? -58.046  -28.213 -6.662  1.00 68.49  ? 219  LYS A C   1 
ATOM   1391 O O   . LYS A 1 193 ? -59.203  -28.628 -6.715  1.00 71.55  ? 219  LYS A O   1 
ATOM   1392 C CB  . LYS A 1 193 ? -57.382  -30.381 -7.751  1.00 97.09  ? 219  LYS A CB  1 
ATOM   1393 C CG  . LYS A 1 193 ? -56.316  -31.398 -8.207  1.00 104.68 ? 219  LYS A CG  1 
ATOM   1394 C CD  . LYS A 1 193 ? -55.483  -31.021 -9.428  1.00 121.19 ? 219  LYS A CD  1 
ATOM   1395 C CE  . LYS A 1 193 ? -54.515  -29.870 -9.178  1.00 138.79 ? 219  LYS A CE  1 
ATOM   1396 N NZ  . LYS A 1 193 ? -53.681  -29.567 -10.379 1.00 143.00 ? 219  LYS A NZ  1 
ATOM   1397 N N   . LEU A 1 194 ? -57.725  -27.086 -6.044  1.00 69.03  ? 220  LEU A N   1 
ATOM   1398 C CA  . LEU A 1 194 ? -58.746  -26.251 -5.425  1.00 68.75  ? 220  LEU A CA  1 
ATOM   1399 C C   . LEU A 1 194 ? -59.295  -25.352 -6.478  1.00 60.95  ? 220  LEU A C   1 
ATOM   1400 O O   . LEU A 1 194 ? -58.566  -24.935 -7.360  1.00 61.09  ? 220  LEU A O   1 
ATOM   1401 C CB  . LEU A 1 194 ? -58.153  -25.420 -4.294  1.00 79.03  ? 220  LEU A CB  1 
ATOM   1402 C CG  . LEU A 1 194 ? -57.794  -26.216 -3.044  1.00 77.34  ? 220  LEU A CG  1 
ATOM   1403 C CD1 . LEU A 1 194 ? -56.839  -25.462 -2.146  1.00 75.49  ? 220  LEU A CD1 1 
ATOM   1404 C CD2 . LEU A 1 194 ? -59.079  -26.617 -2.319  1.00 79.43  ? 220  LEU A CD2 1 
ATOM   1405 N N   . PRO A 1 195 ? -60.591  -25.069 -6.410  1.00 54.87  ? 221  PRO A N   1 
ATOM   1406 C CA  . PRO A 1 195 ? -61.251  -24.198 -7.380  1.00 55.34  ? 221  PRO A CA  1 
ATOM   1407 C C   . PRO A 1 195 ? -60.840  -22.707 -7.278  1.00 67.13  ? 221  PRO A C   1 
ATOM   1408 O O   . PRO A 1 195 ? -60.896  -22.106 -6.204  1.00 75.78  ? 221  PRO A O   1 
ATOM   1409 C CB  . PRO A 1 195 ? -62.743  -24.381 -7.066  1.00 62.16  ? 221  PRO A CB  1 
ATOM   1410 C CG  . PRO A 1 195 ? -62.817  -24.913 -5.661  1.00 63.59  ? 221  PRO A CG  1 
ATOM   1411 C CD  . PRO A 1 195 ? -61.446  -25.405 -5.262  1.00 60.41  ? 221  PRO A CD  1 
ATOM   1412 N N   . SER A 1 196 ? -60.478  -22.108 -8.404  1.00 69.76  ? 222  SER A N   1 
ATOM   1413 C CA  . SER A 1 196 ? -60.054  -20.697 -8.434  1.00 68.51  ? 222  SER A CA  1 
ATOM   1414 C C   . SER A 1 196 ? -61.148  -19.696 -8.027  1.00 62.99  ? 222  SER A C   1 
ATOM   1415 O O   . SER A 1 196 ? -60.855  -18.519 -7.818  1.00 70.32  ? 222  SER A O   1 
ATOM   1416 C CB  . SER A 1 196 ? -59.506  -20.321 -9.818  1.00 65.46  ? 222  SER A CB  1 
ATOM   1417 O OG  . SER A 1 196 ? -60.528  -20.426 -10.808 1.00 73.83  ? 222  SER A OG  1 
ATOM   1418 N N   . SER A 1 197 ? -62.394  -20.144 -7.910  1.00 61.21  ? 223  SER A N   1 
ATOM   1419 C CA  . SER A 1 197 ? -63.479  -19.240 -7.503  1.00 57.30  ? 223  SER A CA  1 
ATOM   1420 C C   . SER A 1 197 ? -63.456  -18.899 -6.007  1.00 63.02  ? 223  SER A C   1 
ATOM   1421 O O   . SER A 1 197 ? -64.249  -18.058 -5.552  1.00 58.40  ? 223  SER A O   1 
ATOM   1422 C CB  . SER A 1 197 ? -64.828  -19.886 -7.800  1.00 57.34  ? 223  SER A CB  1 
ATOM   1423 O OG  . SER A 1 197 ? -64.948  -21.145 -7.157  1.00 64.93  ? 223  SER A OG  1 
ATOM   1424 N N   . LEU A 1 198 ? -62.654  -19.646 -5.237  1.00 73.54  ? 224  LEU A N   1 
ATOM   1425 C CA  . LEU A 1 198 ? -62.545  -19.458 -3.774  1.00 73.62  ? 224  LEU A CA  1 
ATOM   1426 C C   . LEU A 1 198 ? -62.216  -18.073 -3.271  1.00 70.17  ? 224  LEU A C   1 
ATOM   1427 O O   . LEU A 1 198 ? -61.230  -17.452 -3.683  1.00 66.54  ? 224  LEU A O   1 
ATOM   1428 C CB  . LEU A 1 198 ? -61.536  -20.443 -3.129  1.00 66.82  ? 224  LEU A CB  1 
ATOM   1429 C CG  . LEU A 1 198 ? -61.952  -21.903 -2.856  1.00 65.36  ? 224  LEU A CG  1 
ATOM   1430 C CD1 . LEU A 1 198 ? -60.796  -22.705 -2.304  1.00 64.00  ? 224  LEU A CD1 1 
ATOM   1431 C CD2 . LEU A 1 198 ? -63.099  -21.973 -1.874  1.00 66.78  ? 224  LEU A CD2 1 
ATOM   1432 N N   . ARG A 1 199 ? -63.040  -17.628 -2.329  1.00 64.55  ? 225  ARG A N   1 
ATOM   1433 C CA  . ARG A 1 199 ? -62.855  -16.360 -1.681  1.00 66.27  ? 225  ARG A CA  1 
ATOM   1434 C C   . ARG A 1 199 ? -62.382  -16.560 -0.227  1.00 61.27  ? 225  ARG A C   1 
ATOM   1435 O O   . ARG A 1 199 ? -61.396  -15.953 0.184   1.00 58.82  ? 225  ARG A O   1 
ATOM   1436 C CB  . ARG A 1 199 ? -64.057  -15.425 -1.890  1.00 72.75  ? 225  ARG A CB  1 
ATOM   1437 C CG  . ARG A 1 199 ? -64.147  -15.090 -3.386  1.00 87.91  ? 225  ARG A CG  1 
ATOM   1438 C CD  . ARG A 1 199 ? -65.023  -13.918 -3.827  1.00 96.46  ? 225  ARG A CD  1 
ATOM   1439 N NE  . ARG A 1 199 ? -66.456  -14.068 -3.587  1.00 113.06 ? 225  ARG A NE  1 
ATOM   1440 C CZ  . ARG A 1 199 ? -67.385  -13.250 -4.093  1.00 116.18 ? 225  ARG A CZ  1 
ATOM   1441 N NH1 . ARG A 1 199 ? -68.668  -13.437 -3.815  1.00 120.71 ? 225  ARG A NH1 1 
ATOM   1442 N NH2 . ARG A 1 199 ? -67.036  -12.250 -4.892  1.00 119.41 ? 225  ARG A NH2 1 
ATOM   1443 N N   . LYS A 1 200 ? -62.937  -17.546 0.467   1.00 59.61  ? 226  LYS A N   1 
ATOM   1444 C CA  . LYS A 1 200 ? -62.531  -17.845 1.862   1.00 55.28  ? 226  LYS A CA  1 
ATOM   1445 C C   . LYS A 1 200 ? -62.103  -19.309 2.053   1.00 51.91  ? 226  LYS A C   1 
ATOM   1446 O O   . LYS A 1 200 ? -62.859  -20.226 1.779   1.00 50.22  ? 226  LYS A O   1 
ATOM   1447 C CB  . LYS A 1 200 ? -63.669  -17.523 2.808   1.00 49.06  ? 226  LYS A CB  1 
ATOM   1448 C CG  . LYS A 1 200 ? -64.003  -16.062 2.797   1.00 56.12  ? 226  LYS A CG  1 
ATOM   1449 C CD  . LYS A 1 200 ? -65.167  -15.700 3.697   1.00 62.90  ? 226  LYS A CD  1 
ATOM   1450 C CE  . LYS A 1 200 ? -65.354  -14.193 3.731   1.00 59.24  ? 226  LYS A CE  1 
ATOM   1451 N NZ  . LYS A 1 200 ? -66.570  -13.842 4.480   1.00 68.38  ? 226  LYS A NZ  1 
ATOM   1452 N N   . LEU A 1 201 ? -60.883  -19.513 2.513   1.00 46.79  ? 227  LEU A N   1 
ATOM   1453 C CA  . LEU A 1 201 ? -60.365  -20.843 2.739   1.00 47.00  ? 227  LEU A CA  1 
ATOM   1454 C C   . LEU A 1 201 ? -59.935  -21.010 4.208   1.00 47.89  ? 227  LEU A C   1 
ATOM   1455 O O   . LEU A 1 201 ? -58.913  -20.479 4.619   1.00 49.64  ? 227  LEU A O   1 
ATOM   1456 C CB  . LEU A 1 201 ? -59.179  -21.094 1.825   1.00 46.81  ? 227  LEU A CB  1 
ATOM   1457 C CG  . LEU A 1 201 ? -58.460  -22.436 1.954   1.00 57.99  ? 227  LEU A CG  1 
ATOM   1458 C CD1 . LEU A 1 201 ? -59.393  -23.579 1.648   1.00 59.08  ? 227  LEU A CD1 1 
ATOM   1459 C CD2 . LEU A 1 201 ? -57.258  -22.505 1.029   1.00 59.41  ? 227  LEU A CD2 1 
ATOM   1460 N N   . PHE A 1 202 ? -60.730  -21.734 4.992   1.00 48.52  ? 228  PHE A N   1 
ATOM   1461 C CA  . PHE A 1 202 ? -60.405  -21.982 6.404   1.00 49.86  ? 228  PHE A CA  1 
ATOM   1462 C C   . PHE A 1 202 ? -59.666  -23.306 6.616   1.00 51.30  ? 228  PHE A C   1 
ATOM   1463 O O   . PHE A 1 202 ? -60.184  -24.368 6.302   1.00 51.28  ? 228  PHE A O   1 
ATOM   1464 C CB  . PHE A 1 202 ? -61.667  -22.013 7.210   1.00 44.68  ? 228  PHE A CB  1 
ATOM   1465 C CG  . PHE A 1 202 ? -62.422  -20.730 7.197   1.00 45.49  ? 228  PHE A CG  1 
ATOM   1466 C CD1 . PHE A 1 202 ? -63.362  -20.479 6.224   1.00 50.43  ? 228  PHE A CD1 1 
ATOM   1467 C CD2 . PHE A 1 202 ? -62.226  -19.787 8.188   1.00 47.59  ? 228  PHE A CD2 1 
ATOM   1468 C CE1 . PHE A 1 202 ? -64.123  -19.324 6.241   1.00 48.73  ? 228  PHE A CE1 1 
ATOM   1469 C CE2 . PHE A 1 202 ? -62.977  -18.615 8.204   1.00 50.32  ? 228  PHE A CE2 1 
ATOM   1470 C CZ  . PHE A 1 202 ? -63.906  -18.379 7.210   1.00 49.13  ? 228  PHE A CZ  1 
ATOM   1471 N N   . LEU A 1 203 ? -58.480  -23.253 7.195   1.00 49.45  ? 229  LEU A N   1 
ATOM   1472 C CA  . LEU A 1 203 ? -57.703  -24.485 7.432   1.00 47.35  ? 229  LEU A CA  1 
ATOM   1473 C C   . LEU A 1 203 ? -57.059  -24.423 8.790   1.00 48.81  ? 229  LEU A C   1 
ATOM   1474 O O   . LEU A 1 203 ? -55.860  -24.716 8.931   1.00 48.81  ? 229  LEU A O   1 
ATOM   1475 C CB  . LEU A 1 203 ? -56.573  -24.604 6.397   1.00 49.55  ? 229  LEU A CB  1 
ATOM   1476 C CG  . LEU A 1 203 ? -56.958  -24.647 4.912   1.00 57.14  ? 229  LEU A CG  1 
ATOM   1477 C CD1 . LEU A 1 203 ? -55.730  -24.478 4.038   1.00 50.25  ? 229  LEU A CD1 1 
ATOM   1478 C CD2 . LEU A 1 203 ? -57.730  -25.906 4.542   1.00 54.77  ? 229  LEU A CD2 1 
ATOM   1479 N N   . SER A 1 204 ? -57.786  -23.925 9.776   1.00 47.41  ? 230  SER A N   1 
ATOM   1480 C CA  . SER A 1 204 ? -57.210  -23.834 11.131  1.00 58.72  ? 230  SER A CA  1 
ATOM   1481 C C   . SER A 1 204 ? -57.116  -25.251 11.781  1.00 50.54  ? 230  SER A C   1 
ATOM   1482 O O   . SER A 1 204 ? -57.971  -26.083 11.536  1.00 50.10  ? 230  SER A O   1 
ATOM   1483 C CB  . SER A 1 204 ? -58.091  -22.936 12.019  1.00 56.26  ? 230  SER A CB  1 
ATOM   1484 O OG  . SER A 1 204 ? -57.437  -22.677 13.249  1.00 55.01  ? 230  SER A OG  1 
ATOM   1485 N N   . ASN A 1 205 ? -56.087  -25.524 12.576  1.00 54.76  ? 231  ASN A N   1 
ATOM   1486 C CA  . ASN A 1 205 ? -55.988  -26.833 13.239  1.00 58.57  ? 231  ASN A CA  1 
ATOM   1487 C C   . ASN A 1 205 ? -56.177  -28.004 12.298  1.00 59.47  ? 231  ASN A C   1 
ATOM   1488 O O   . ASN A 1 205 ? -57.156  -28.775 12.406  1.00 58.44  ? 231  ASN A O   1 
ATOM   1489 C CB  . ASN A 1 205 ? -57.049  -26.904 14.323  1.00 61.66  ? 231  ASN A CB  1 
ATOM   1490 C CG  . ASN A 1 205 ? -56.764  -25.972 15.461  1.00 63.48  ? 231  ASN A CG  1 
ATOM   1491 O OD1 . ASN A 1 205 ? -57.490  -25.035 15.664  1.00 72.15  ? 231  ASN A OD1 1 
ATOM   1492 N ND2 . ASN A 1 205 ? -55.611  -26.126 16.087  1.00 66.13  ? 231  ASN A ND2 1 
ATOM   1493 N N   . THR A 1 206 ? -55.323  -28.054 11.294  1.00 59.12  ? 232  THR A N   1 
ATOM   1494 C CA  . THR A 1 206 ? -55.361  -29.113 10.319  1.00 58.24  ? 232  THR A CA  1 
ATOM   1495 C C   . THR A 1 206 ? -54.009  -29.836 10.323  1.00 60.86  ? 232  THR A C   1 
ATOM   1496 O O   . THR A 1 206 ? -53.677  -30.590 9.421   1.00 62.76  ? 232  THR A O   1 
ATOM   1497 C CB  . THR A 1 206 ? -55.667  -28.551 8.926   1.00 57.98  ? 232  THR A CB  1 
ATOM   1498 O OG1 . THR A 1 206 ? -54.704  -27.534 8.620   1.00 57.54  ? 232  THR A OG1 1 
ATOM   1499 C CG2 . THR A 1 206 ? -57.074  -27.965 8.859   1.00 48.35  ? 232  THR A CG2 1 
ATOM   1500 N N   . GLN A 1 207 ? -53.224  -29.600 11.353  1.00 65.79  ? 233  GLN A N   1 
ATOM   1501 C CA  . GLN A 1 207 ? -51.928  -30.245 11.459  1.00 80.39  ? 233  GLN A CA  1 
ATOM   1502 C C   . GLN A 1 207 ? -51.045  -30.048 10.240  1.00 78.05  ? 233  GLN A C   1 
ATOM   1503 O O   . GLN A 1 207 ? -50.255  -30.925 9.882   1.00 81.69  ? 233  GLN A O   1 
ATOM   1504 C CB  . GLN A 1 207 ? -52.102  -31.731 11.735  1.00 88.90  ? 233  GLN A CB  1 
ATOM   1505 C CG  . GLN A 1 207 ? -52.690  -32.036 13.096  1.00 94.93  ? 233  GLN A CG  1 
ATOM   1506 C CD  . GLN A 1 207 ? -52.811  -33.520 13.331  1.00 103.10 ? 233  GLN A CD  1 
ATOM   1507 O OE1 . GLN A 1 207 ? -52.119  -34.055 14.182  1.00 99.68  ? 233  GLN A OE1 1 
ATOM   1508 N NE2 . GLN A 1 207 ? -53.513  -34.212 12.440  1.00 97.01  ? 233  GLN A NE2 1 
ATOM   1509 N N   . ILE A 1 208 ? -51.144  -28.879 9.630   1.00 79.56  ? 234  ILE A N   1 
ATOM   1510 C CA  . ILE A 1 208 ? -50.335  -28.576 8.472   1.00 70.85  ? 234  ILE A CA  1 
ATOM   1511 C C   . ILE A 1 208 ? -49.148  -27.776 8.922   1.00 67.84  ? 234  ILE A C   1 
ATOM   1512 O O   . ILE A 1 208 ? -49.287  -26.679 9.405   1.00 89.77  ? 234  ILE A O   1 
ATOM   1513 C CB  . ILE A 1 208 ? -51.118  -27.803 7.439   1.00 69.07  ? 234  ILE A CB  1 
ATOM   1514 C CG1 . ILE A 1 208 ? -52.313  -28.636 7.008   1.00 63.27  ? 234  ILE A CG1 1 
ATOM   1515 C CG2 . ILE A 1 208 ? -50.224  -27.483 6.257   1.00 74.39  ? 234  ILE A CG2 1 
ATOM   1516 C CD1 . ILE A 1 208 ? -53.153  -27.965 5.957   1.00 68.16  ? 234  ILE A CD1 1 
ATOM   1517 N N   . LYS A 1 209 ? -47.976  -28.343 8.730   1.00 70.13  ? 235  LYS A N   1 
ATOM   1518 C CA  . LYS A 1 209 ? -46.705  -27.749 9.122   1.00 62.54  ? 235  LYS A CA  1 
ATOM   1519 C C   . LYS A 1 209 ? -45.975  -27.036 7.999   1.00 62.18  ? 235  LYS A C   1 
ATOM   1520 O O   . LYS A 1 209 ? -45.170  -26.158 8.250   1.00 67.34  ? 235  LYS A O   1 
ATOM   1521 C CB  . LYS A 1 209 ? -45.805  -28.884 9.662   1.00 73.08  ? 235  LYS A CB  1 
ATOM   1522 C CG  . LYS A 1 209 ? -44.292  -28.619 9.712   1.00 88.85  ? 235  LYS A CG  1 
ATOM   1523 C CD  . LYS A 1 209 ? -43.861  -27.447 10.591  1.00 97.04  ? 235  LYS A CD  1 
ATOM   1524 C CE  . LYS A 1 209 ? -42.351  -27.271 10.555  1.00 102.98 ? 235  LYS A CE  1 
ATOM   1525 N NZ  . LYS A 1 209 ? -41.649  -28.489 11.053  1.00 110.91 ? 235  LYS A NZ  1 
ATOM   1526 N N   . TYR A 1 210 ? -46.193  -27.437 6.758   1.00 68.17  ? 236  TYR A N   1 
ATOM   1527 C CA  . TYR A 1 210 ? -45.483  -26.792 5.675   1.00 70.57  ? 236  TYR A CA  1 
ATOM   1528 C C   . TYR A 1 210 ? -46.433  -26.299 4.623   1.00 67.24  ? 236  TYR A C   1 
ATOM   1529 O O   . TYR A 1 210 ? -47.377  -26.994 4.273   1.00 63.69  ? 236  TYR A O   1 
ATOM   1530 C CB  . TYR A 1 210 ? -44.425  -27.733 5.075   1.00 75.04  ? 236  TYR A CB  1 
ATOM   1531 C CG  . TYR A 1 210 ? -43.630  -27.123 3.926   1.00 98.81  ? 236  TYR A CG  1 
ATOM   1532 C CD1 . TYR A 1 210 ? -42.580  -26.243 4.175   1.00 113.81 ? 236  TYR A CD1 1 
ATOM   1533 C CD2 . TYR A 1 210 ? -43.889  -27.475 2.592   1.00 102.93 ? 236  TYR A CD2 1 
ATOM   1534 C CE1 . TYR A 1 210 ? -41.857  -25.673 3.135   1.00 118.75 ? 236  TYR A CE1 1 
ATOM   1535 C CE2 . TYR A 1 210 ? -43.154  -26.929 1.543   1.00 96.41  ? 236  TYR A CE2 1 
ATOM   1536 C CZ  . TYR A 1 210 ? -42.141  -26.027 1.821   1.00 116.39 ? 236  TYR A CZ  1 
ATOM   1537 O OH  . TYR A 1 210 ? -41.401  -25.465 0.801   1.00 112.39 ? 236  TYR A OH  1 
ATOM   1538 N N   . ILE A 1 211 ? -46.255  -25.032 4.237   1.00 72.44  ? 237  ILE A N   1 
ATOM   1539 C CA  . ILE A 1 211 ? -47.063  -24.384 3.195   1.00 70.22  ? 237  ILE A CA  1 
ATOM   1540 C C   . ILE A 1 211 ? -46.092  -24.124 2.057   1.00 71.57  ? 237  ILE A C   1 
ATOM   1541 O O   . ILE A 1 211 ? -45.102  -23.410 2.221   1.00 69.26  ? 237  ILE A O   1 
ATOM   1542 C CB  . ILE A 1 211 ? -47.656  -23.040 3.661   1.00 71.85  ? 237  ILE A CB  1 
ATOM   1543 C CG1 . ILE A 1 211 ? -48.604  -23.230 4.853   1.00 63.51  ? 237  ILE A CG1 1 
ATOM   1544 C CG2 . ILE A 1 211 ? -48.413  -22.375 2.527   1.00 72.02  ? 237  ILE A CG2 1 
ATOM   1545 C CD1 . ILE A 1 211 ? -49.815  -24.075 4.555   1.00 58.52  ? 237  ILE A CD1 1 
ATOM   1546 N N   . SER A 1 212 ? -46.346  -24.746 0.923   1.00 78.49  ? 238  SER A N   1 
ATOM   1547 C CA  . SER A 1 212 ? -45.470  -24.606 -0.241  1.00 86.71  ? 238  SER A CA  1 
ATOM   1548 C C   . SER A 1 212 ? -45.969  -23.587 -1.246  1.00 81.80  ? 238  SER A C   1 
ATOM   1549 O O   . SER A 1 212 ? -47.170  -23.282 -1.310  1.00 72.75  ? 238  SER A O   1 
ATOM   1550 C CB  . SER A 1 212 ? -45.371  -25.953 -0.958  1.00 90.33  ? 238  SER A CB  1 
ATOM   1551 O OG  . SER A 1 212 ? -46.651  -26.343 -1.452  1.00 90.37  ? 238  SER A OG  1 
ATOM   1552 N N   . GLU A 1 213 ? -45.043  -23.139 -2.091  1.00 85.80  ? 239  GLU A N   1 
ATOM   1553 C CA  . GLU A 1 213 ? -45.326  -22.173 -3.157  1.00 80.93  ? 239  GLU A CA  1 
ATOM   1554 C C   . GLU A 1 213 ? -46.536  -22.547 -4.012  1.00 76.34  ? 239  GLU A C   1 
ATOM   1555 O O   . GLU A 1 213 ? -47.306  -21.681 -4.423  1.00 78.55  ? 239  GLU A O   1 
ATOM   1556 C CB  . GLU A 1 213 ? -44.108  -22.078 -4.072  1.00 93.58  ? 239  GLU A CB  1 
ATOM   1557 C CG  . GLU A 1 213 ? -44.352  -21.287 -5.350  1.00 114.51 ? 239  GLU A CG  1 
ATOM   1558 C CD  . GLU A 1 213 ? -43.126  -21.203 -6.246  1.00 122.48 ? 239  GLU A CD  1 
ATOM   1559 O OE1 . GLU A 1 213 ? -42.038  -21.648 -5.813  1.00 124.60 ? 239  GLU A OE1 1 
ATOM   1560 O OE2 . GLU A 1 213 ? -43.248  -20.672 -7.377  1.00 115.09 ? 239  GLU A OE2 1 
ATOM   1561 N N   . GLU A 1 214 ? -46.715  -23.845 -4.234  1.00 73.14  ? 240  GLU A N   1 
ATOM   1562 C CA  . GLU A 1 214 ? -47.803  -24.371 -5.066  1.00 75.72  ? 240  GLU A CA  1 
ATOM   1563 C C   . GLU A 1 214 ? -49.117  -24.589 -4.328  1.00 68.47  ? 240  GLU A C   1 
ATOM   1564 O O   . GLU A 1 214 ? -50.145  -24.895 -4.942  1.00 66.01  ? 240  GLU A O   1 
ATOM   1565 C CB  . GLU A 1 214 ? -47.378  -25.736 -5.651  1.00 94.12  ? 240  GLU A CB  1 
ATOM   1566 C CG  . GLU A 1 214 ? -46.089  -25.770 -6.477  1.00 108.31 ? 240  GLU A CG  1 
ATOM   1567 C CD  . GLU A 1 214 ? -46.167  -24.976 -7.775  1.00 122.61 ? 240  GLU A CD  1 
ATOM   1568 O OE1 . GLU A 1 214 ? -46.850  -23.932 -7.816  1.00 120.30 ? 240  GLU A OE1 1 
ATOM   1569 O OE2 . GLU A 1 214 ? -45.479  -25.367 -8.744  1.00 137.80 ? 240  GLU A OE2 1 
ATOM   1570 N N   . ASP A 1 215 ? -49.097  -24.497 -3.011  1.00 70.30  ? 241  ASP A N   1 
ATOM   1571 C CA  . ASP A 1 215 ? -50.322  -24.734 -2.253  1.00 69.70  ? 241  ASP A CA  1 
ATOM   1572 C C   . ASP A 1 215 ? -51.524  -23.888 -2.609  1.00 63.45  ? 241  ASP A C   1 
ATOM   1573 O O   . ASP A 1 215 ? -52.649  -24.386 -2.582  1.00 61.26  ? 241  ASP A O   1 
ATOM   1574 C CB  . ASP A 1 215 ? -50.035  -24.643 -0.761  1.00 82.23  ? 241  ASP A CB  1 
ATOM   1575 C CG  . ASP A 1 215 ? -49.308  -25.844 -0.254  1.00 80.66  ? 241  ASP A CG  1 
ATOM   1576 O OD1 . ASP A 1 215 ? -49.800  -26.938 -0.578  1.00 80.88  ? 241  ASP A OD1 1 
ATOM   1577 O OD2 . ASP A 1 215 ? -48.345  -25.708 0.551   1.00 78.33  ? 241  ASP A OD2 1 
ATOM   1578 N N   . PHE A 1 216 ? -51.301  -22.611 -2.915  1.00 74.03  ? 242  PHE A N   1 
ATOM   1579 C CA  . PHE A 1 216 ? -52.405  -21.686 -3.248  1.00 82.23  ? 242  PHE A CA  1 
ATOM   1580 C C   . PHE A 1 216 ? -52.148  -21.032 -4.594  1.00 90.44  ? 242  PHE A C   1 
ATOM   1581 O O   . PHE A 1 216 ? -52.672  -19.954 -4.884  1.00 90.25  ? 242  PHE A O   1 
ATOM   1582 C CB  . PHE A 1 216 ? -52.433  -20.565 -2.214  1.00 77.10  ? 242  PHE A CB  1 
ATOM   1583 C CG  . PHE A 1 216 ? -52.346  -21.043 -0.805  1.00 69.10  ? 242  PHE A CG  1 
ATOM   1584 C CD1 . PHE A 1 216 ? -53.392  -21.727 -0.237  1.00 67.94  ? 242  PHE A CD1 1 
ATOM   1585 C CD2 . PHE A 1 216 ? -51.260  -20.710 -0.018  1.00 65.96  ? 242  PHE A CD2 1 
ATOM   1586 C CE1 . PHE A 1 216 ? -53.321  -22.163 1.070   1.00 62.94  ? 242  PHE A CE1 1 
ATOM   1587 C CE2 . PHE A 1 216 ? -51.202  -21.106 1.293   1.00 67.53  ? 242  PHE A CE2 1 
ATOM   1588 C CZ  . PHE A 1 216 ? -52.231  -21.840 1.836   1.00 66.52  ? 242  PHE A CZ  1 
ATOM   1589 N N   . LYS A 1 217 ? -51.497  -21.780 -5.466  1.00 100.68 ? 243  LYS A N   1 
ATOM   1590 C CA  . LYS A 1 217 ? -51.065  -21.283 -6.762  1.00 108.86 ? 243  LYS A CA  1 
ATOM   1591 C C   . LYS A 1 217 ? -52.058  -20.417 -7.558  1.00 104.72 ? 243  LYS A C   1 
ATOM   1592 O O   . LYS A 1 217 ? -51.719  -19.283 -7.971  1.00 79.74  ? 243  LYS A O   1 
ATOM   1593 C CB  . LYS A 1 217 ? -50.685  -22.461 -7.664  1.00 120.48 ? 243  LYS A CB  1 
ATOM   1594 C CG  . LYS A 1 217 ? -49.512  -22.163 -8.599  1.00 120.85 ? 243  LYS A CG  1 
ATOM   1595 C CD  . LYS A 1 217 ? -49.631  -22.925 -9.903  1.00 115.68 ? 243  LYS A CD  1 
ATOM   1596 C CE  . LYS A 1 217 ? -50.083  -24.365 -9.725  1.00 116.45 ? 243  LYS A CE  1 
ATOM   1597 N NZ  . LYS A 1 217 ? -50.397  -24.952 -11.057 1.00 112.72 ? 243  LYS A NZ  1 
ATOM   1598 N N   . GLY A 1 218 ? -53.239  -20.981 -7.840  1.00 83.46  ? 244  GLY A N   1 
ATOM   1599 C CA  . GLY A 1 218 ? -54.250  -20.287 -8.645  1.00 73.55  ? 244  GLY A CA  1 
ATOM   1600 C C   . GLY A 1 218 ? -55.435  -19.668 -7.947  1.00 70.92  ? 244  GLY A C   1 
ATOM   1601 O O   . GLY A 1 218 ? -56.448  -19.385 -8.586  1.00 69.06  ? 244  GLY A O   1 
ATOM   1602 N N   . LEU A 1 219 ? -55.319  -19.454 -6.642  1.00 84.90  ? 245  LEU A N   1 
ATOM   1603 C CA  . LEU A 1 219 ? -56.407  -18.879 -5.863  1.00 81.83  ? 245  LEU A CA  1 
ATOM   1604 C C   . LEU A 1 219 ? -56.234  -17.383 -5.897  1.00 81.75  ? 245  LEU A C   1 
ATOM   1605 O O   . LEU A 1 219 ? -55.854  -16.760 -4.912  1.00 91.71  ? 245  LEU A O   1 
ATOM   1606 C CB  . LEU A 1 219 ? -56.323  -19.390 -4.439  1.00 89.88  ? 245  LEU A CB  1 
ATOM   1607 C CG  . LEU A 1 219 ? -56.346  -20.912 -4.299  1.00 74.25  ? 245  LEU A CG  1 
ATOM   1608 C CD1 . LEU A 1 219 ? -56.120  -21.277 -2.849  1.00 71.37  ? 245  LEU A CD1 1 
ATOM   1609 C CD2 . LEU A 1 219 ? -57.661  -21.472 -4.808  1.00 69.50  ? 245  LEU A CD2 1 
ATOM   1610 N N   . ILE A 1 220 ? -56.513  -16.823 -7.062  1.00 77.20  ? 246  ILE A N   1 
ATOM   1611 C CA  . ILE A 1 220 ? -56.358  -15.403 -7.311  1.00 69.14  ? 246  ILE A CA  1 
ATOM   1612 C C   . ILE A 1 220 ? -57.486  -14.572 -6.739  1.00 57.92  ? 246  ILE A C   1 
ATOM   1613 O O   . ILE A 1 220 ? -57.391  -13.373 -6.715  1.00 60.40  ? 246  ILE A O   1 
ATOM   1614 C CB  . ILE A 1 220 ? -56.226  -15.121 -8.837  1.00 68.82  ? 246  ILE A CB  1 
ATOM   1615 C CG1 . ILE A 1 220 ? -57.476  -15.578 -9.588  1.00 69.39  ? 246  ILE A CG1 1 
ATOM   1616 C CG2 . ILE A 1 220 ? -55.012  -15.836 -9.392  1.00 67.13  ? 246  ILE A CG2 1 
ATOM   1617 C CD1 . ILE A 1 220 ? -57.479  -15.235 -11.059 1.00 74.01  ? 246  ILE A CD1 1 
ATOM   1618 N N   . ASN A 1 221 ? -58.574  -15.212 -6.344  1.00 57.01  ? 247  ASN A N   1 
ATOM   1619 C CA  . ASN A 1 221 ? -59.713  -14.511 -5.763  1.00 54.80  ? 247  ASN A CA  1 
ATOM   1620 C C   . ASN A 1 221 ? -59.806  -14.562 -4.233  1.00 54.14  ? 247  ASN A C   1 
ATOM   1621 O O   . ASN A 1 221 ? -60.748  -14.015 -3.659  1.00 57.47  ? 247  ASN A O   1 
ATOM   1622 C CB  . ASN A 1 221 ? -61.009  -15.050 -6.363  1.00 60.82  ? 247  ASN A CB  1 
ATOM   1623 C CG  . ASN A 1 221 ? -61.181  -14.665 -7.824  1.00 70.57  ? 247  ASN A CG  1 
ATOM   1624 O OD1 . ASN A 1 221 ? -61.175  -13.494 -8.148  1.00 75.07  ? 247  ASN A OD1 1 
ATOM   1625 N ND2 . ASN A 1 221 ? -61.526  -15.631 -8.663  1.00 77.21  ? 247  ASN A ND2 1 
ATOM   1626 N N   . LEU A 1 222 ? -58.874  -15.231 -3.564  1.00 57.41  ? 248  LEU A N   1 
ATOM   1627 C CA  . LEU A 1 222 ? -58.958  -15.300 -2.109  1.00 61.41  ? 248  LEU A CA  1 
ATOM   1628 C C   . LEU A 1 222 ? -58.928  -13.977 -1.431  1.00 56.12  ? 248  LEU A C   1 
ATOM   1629 O O   . LEU A 1 222 ? -58.021  -13.193 -1.635  1.00 57.75  ? 248  LEU A O   1 
ATOM   1630 C CB  . LEU A 1 222 ? -57.822  -16.095 -1.439  1.00 61.69  ? 248  LEU A CB  1 
ATOM   1631 C CG  . LEU A 1 222 ? -57.808  -17.596 -1.230  1.00 60.07  ? 248  LEU A CG  1 
ATOM   1632 C CD1 . LEU A 1 222 ? -56.635  -17.915 -0.314  1.00 57.98  ? 248  LEU A CD1 1 
ATOM   1633 C CD2 . LEU A 1 222 ? -59.081  -18.027 -0.538  1.00 63.27  ? 248  LEU A CD2 1 
ATOM   1634 N N   . THR A 1 223 ? -59.813  -13.843 -0.466  1.00 51.45  ? 249  THR A N   1 
ATOM   1635 C CA  . THR A 1 223 ? -59.893  -12.670 0.351   1.00 48.80  ? 249  THR A CA  1 
ATOM   1636 C C   . THR A 1 223 ? -59.569  -13.047 1.790   1.00 50.57  ? 249  THR A C   1 
ATOM   1637 O O   . THR A 1 223 ? -59.182  -12.200 2.569   1.00 63.05  ? 249  THR A O   1 
ATOM   1638 C CB  . THR A 1 223 ? -61.277  -12.111 0.305   1.00 51.31  ? 249  THR A CB  1 
ATOM   1639 O OG1 . THR A 1 223 ? -62.192  -13.144 0.646   1.00 58.78  ? 249  THR A OG1 1 
ATOM   1640 C CG2 . THR A 1 223 ? -61.582  -11.659 -1.088  1.00 64.68  ? 249  THR A CG2 1 
ATOM   1641 N N   . LEU A 1 224 ? -59.692  -14.335 2.125   1.00 57.94  ? 250  LEU A N   1 
ATOM   1642 C CA  . LEU A 1 224 ? -59.434  -14.820 3.482   1.00 53.67  ? 250  LEU A CA  1 
ATOM   1643 C C   . LEU A 1 224 ? -58.751  -16.150 3.538   1.00 52.74  ? 250  LEU A C   1 
ATOM   1644 O O   . LEU A 1 224 ? -59.185  -17.104 2.904   1.00 57.56  ? 250  LEU A O   1 
ATOM   1645 C CB  . LEU A 1 224 ? -60.742  -14.916 4.256   1.00 53.01  ? 250  LEU A CB  1 
ATOM   1646 C CG  . LEU A 1 224 ? -60.635  -15.379 5.710   1.00 55.30  ? 250  LEU A CG  1 
ATOM   1647 C CD1 . LEU A 1 224 ? -61.876  -14.997 6.504   1.00 56.65  ? 250  LEU A CD1 1 
ATOM   1648 C CD2 . LEU A 1 224 ? -60.322  -16.870 5.846   1.00 62.95  ? 250  LEU A CD2 1 
ATOM   1649 N N   . LEU A 1 225 ? -57.695  -16.219 4.339   1.00 47.40  ? 251  LEU A N   1 
ATOM   1650 C CA  . LEU A 1 225 ? -56.949  -17.444 4.509   1.00 47.36  ? 251  LEU A CA  1 
ATOM   1651 C C   . LEU A 1 225 ? -56.688  -17.670 5.995   1.00 53.28  ? 251  LEU A C   1 
ATOM   1652 O O   . LEU A 1 225 ? -55.964  -16.895 6.621   1.00 57.50  ? 251  LEU A O   1 
ATOM   1653 C CB  . LEU A 1 225 ? -55.621  -17.384 3.779   1.00 43.28  ? 251  LEU A CB  1 
ATOM   1654 C CG  . LEU A 1 225 ? -54.827  -18.675 3.953   1.00 50.06  ? 251  LEU A CG  1 
ATOM   1655 C CD1 . LEU A 1 225 ? -55.609  -19.847 3.388   1.00 57.48  ? 251  LEU A CD1 1 
ATOM   1656 C CD2 . LEU A 1 225 ? -53.462  -18.615 3.310   1.00 52.76  ? 251  LEU A CD2 1 
ATOM   1657 N N   . ASP A 1 226 ? -57.227  -18.760 6.532   1.00 51.04  ? 252  ASP A N   1 
ATOM   1658 C CA  . ASP A 1 226 ? -57.066  -19.114 7.973   1.00 48.79  ? 252  ASP A CA  1 
ATOM   1659 C C   . ASP A 1 226 ? -56.186  -20.345 8.147   1.00 52.64  ? 252  ASP A C   1 
ATOM   1660 O O   . ASP A 1 226 ? -56.591  -21.458 7.810   1.00 49.14  ? 252  ASP A O   1 
ATOM   1661 C CB  . ASP A 1 226 ? -58.439  -19.418 8.596   1.00 47.71  ? 252  ASP A CB  1 
ATOM   1662 C CG  . ASP A 1 226 ? -58.358  -19.667 10.081  1.00 50.65  ? 252  ASP A CG  1 
ATOM   1663 O OD1 . ASP A 1 226 ? -57.226  -19.606 10.598  1.00 51.15  ? 252  ASP A OD1 1 
ATOM   1664 O OD2 . ASP A 1 226 ? -59.422  -19.897 10.737  1.00 49.29  ? 252  ASP A OD2 1 
ATOM   1665 N N   . LEU A 1 227 ? -54.994  -20.130 8.670   1.00 47.32  ? 253  LEU A N   1 
ATOM   1666 C CA  . LEU A 1 227 ? -54.039  -21.175 8.914   1.00 43.32  ? 253  LEU A CA  1 
ATOM   1667 C C   . LEU A 1 227 ? -53.677  -21.207 10.390  1.00 48.66  ? 253  LEU A C   1 
ATOM   1668 O O   . LEU A 1 227 ? -52.554  -21.529 10.769  1.00 46.72  ? 253  LEU A O   1 
ATOM   1669 C CB  . LEU A 1 227 ? -52.769  -20.864 8.148   1.00 57.11  ? 253  LEU A CB  1 
ATOM   1670 C CG  . LEU A 1 227 ? -52.883  -20.920 6.633   1.00 67.73  ? 253  LEU A CG  1 
ATOM   1671 C CD1 . LEU A 1 227 ? -51.600  -20.404 5.997   1.00 61.13  ? 253  LEU A CD1 1 
ATOM   1672 C CD2 . LEU A 1 227 ? -53.176  -22.355 6.211   1.00 70.81  ? 253  LEU A CD2 1 
ATOM   1673 N N   . SER A 1 228 ? -54.609  -20.849 11.244  1.00 50.18  ? 254  SER A N   1 
ATOM   1674 C CA  . SER A 1 228 ? -54.304  -20.839 12.656  1.00 54.24  ? 254  SER A CA  1 
ATOM   1675 C C   . SER A 1 228 ? -54.338  -22.233 13.265  1.00 53.54  ? 254  SER A C   1 
ATOM   1676 O O   . SER A 1 228 ? -55.011  -23.122 12.768  1.00 59.83  ? 254  SER A O   1 
ATOM   1677 C CB  . SER A 1 228 ? -55.280  -19.922 13.368  1.00 49.22  ? 254  SER A CB  1 
ATOM   1678 O OG  . SER A 1 228 ? -56.594  -20.280 13.009  1.00 48.49  ? 254  SER A OG  1 
ATOM   1679 N N   . GLY A 1 229 ? -53.614  -22.404 14.359  1.00 56.16  ? 255  GLY A N   1 
ATOM   1680 C CA  . GLY A 1 229 ? -53.580  -23.672 15.043  1.00 63.91  ? 255  GLY A CA  1 
ATOM   1681 C C   . GLY A 1 229 ? -52.780  -24.758 14.353  1.00 60.66  ? 255  GLY A C   1 
ATOM   1682 O O   . GLY A 1 229 ? -53.118  -25.916 14.440  1.00 77.08  ? 255  GLY A O   1 
ATOM   1683 N N   . ASN A 1 230 ? -51.792  -24.361 13.579  1.00 53.43  ? 256  ASN A N   1 
ATOM   1684 C CA  . ASN A 1 230 ? -50.929  -25.277 12.905  1.00 50.10  ? 256  ASN A CA  1 
ATOM   1685 C C   . ASN A 1 230 ? -49.592  -24.953 13.508  1.00 56.67  ? 256  ASN A C   1 
ATOM   1686 O O   . ASN A 1 230 ? -49.042  -23.901 13.246  1.00 61.74  ? 256  ASN A O   1 
ATOM   1687 C CB  . ASN A 1 230 ? -50.993  -25.045 11.444  1.00 51.11  ? 256  ASN A CB  1 
ATOM   1688 C CG  . ASN A 1 230 ? -52.341  -25.414 10.869  1.00 58.14  ? 256  ASN A CG  1 
ATOM   1689 O OD1 . ASN A 1 230 ? -52.806  -26.514 11.064  1.00 59.24  ? 256  ASN A OD1 1 
ATOM   1690 N ND2 . ASN A 1 230 ? -52.908  -24.541 10.050  1.00 64.83  ? 256  ASN A ND2 1 
ATOM   1691 N N   . CYS A 1 231 ? -49.055  -25.911 14.260  1.00 55.97  ? 257  CYS A N   1 
ATOM   1692 C CA  . CYS A 1 231 ? -47.845  -25.737 15.037  1.00 53.40  ? 257  CYS A CA  1 
ATOM   1693 C C   . CYS A 1 231 ? -48.223  -24.774 16.137  1.00 53.30  ? 257  CYS A C   1 
ATOM   1694 O O   . CYS A 1 231 ? -47.519  -23.789 16.374  1.00 54.86  ? 257  CYS A O   1 
ATOM   1695 C CB  . CYS A 1 231 ? -46.662  -25.247 14.248  1.00 53.19  ? 257  CYS A CB  1 
ATOM   1696 S SG  . CYS A 1 231 ? -46.110  -26.443 13.034  1.00 71.95  ? 257  CYS A SG  1 
ATOM   1697 N N   . PRO A 1 232 ? -49.291  -25.106 16.884  1.00 52.09  ? 258  PRO A N   1 
ATOM   1698 C CA  . PRO A 1 232 ? -49.657  -24.145 17.910  1.00 60.64  ? 258  PRO A CA  1 
ATOM   1699 C C   . PRO A 1 232 ? -48.719  -23.983 19.041  1.00 57.54  ? 258  PRO A C   1 
ATOM   1700 O O   . PRO A 1 232 ? -47.789  -24.765 19.226  1.00 69.93  ? 258  PRO A O   1 
ATOM   1701 C CB  . PRO A 1 232 ? -50.954  -24.741 18.505  1.00 60.57  ? 258  PRO A CB  1 
ATOM   1702 C CG  . PRO A 1 232 ? -50.749  -26.200 18.371  1.00 57.63  ? 258  PRO A CG  1 
ATOM   1703 C CD  . PRO A 1 232 ? -50.080  -26.353 17.017  1.00 56.09  ? 258  PRO A CD  1 
ATOM   1704 N N   . ARG A 1 233 ? -48.966  -22.916 19.771  1.00 59.41  ? 259  ARG A N   1 
ATOM   1705 C CA  . ARG A 1 233 ? -48.238  -22.602 20.962  1.00 64.21  ? 259  ARG A CA  1 
ATOM   1706 C C   . ARG A 1 233 ? -49.263  -22.983 22.011  1.00 72.66  ? 259  ARG A C   1 
ATOM   1707 O O   . ARG A 1 233 ? -50.262  -22.288 22.224  1.00 60.69  ? 259  ARG A O   1 
ATOM   1708 C CB  . ARG A 1 233 ? -47.820  -21.147 21.017  1.00 55.79  ? 259  ARG A CB  1 
ATOM   1709 C CG  . ARG A 1 233 ? -47.412  -20.726 22.395  1.00 56.73  ? 259  ARG A CG  1 
ATOM   1710 C CD  . ARG A 1 233 ? -46.689  -19.401 22.444  1.00 58.37  ? 259  ARG A CD  1 
ATOM   1711 N NE  . ARG A 1 233 ? -46.505  -18.990 23.828  1.00 68.25  ? 259  ARG A NE  1 
ATOM   1712 C CZ  . ARG A 1 233 ? -45.713  -18.006 24.221  1.00 77.65  ? 259  ARG A CZ  1 
ATOM   1713 N NH1 . ARG A 1 233 ? -44.925  -17.408 23.356  1.00 88.26  ? 259  ARG A NH1 1 
ATOM   1714 N NH2 . ARG A 1 233 ? -45.623  -17.700 25.503  1.00 85.31  ? 259  ARG A NH2 1 
ATOM   1715 N N   . CYS A 1 234 ? -49.113  -24.214 22.481  1.00 89.27  ? 260  CYS A N   1 
ATOM   1716 C CA  . CYS A 1 234 ? -50.021  -24.796 23.450  1.00 78.23  ? 260  CYS A CA  1 
ATOM   1717 C C   . CYS A 1 234 ? -49.930  -24.208 24.783  1.00 62.52  ? 260  CYS A C   1 
ATOM   1718 O O   . CYS A 1 234 ? -50.908  -24.177 25.492  1.00 61.26  ? 260  CYS A O   1 
ATOM   1719 C CB  . CYS A 1 234 ? -49.792  -26.290 23.529  1.00 70.52  ? 260  CYS A CB  1 
ATOM   1720 S SG  . CYS A 1 234 ? -50.377  -27.095 22.041  1.00 86.18  ? 260  CYS A SG  1 
ATOM   1721 N N   . PHE A 1 235 ? -48.757  -23.695 25.100  1.00 73.78  ? 261  PHE A N   1 
ATOM   1722 C CA  . PHE A 1 235 ? -48.502  -23.086 26.398  1.00 88.56  ? 261  PHE A CA  1 
ATOM   1723 C C   . PHE A 1 235 ? -49.613  -23.113 27.416  1.00 95.91  ? 261  PHE A C   1 
ATOM   1724 O O   . PHE A 1 235 ? -50.604  -22.405 27.276  1.00 103.35 ? 261  PHE A O   1 
ATOM   1725 C CB  . PHE A 1 235 ? -47.913  -21.679 26.239  1.00 83.39  ? 261  PHE A CB  1 
ATOM   1726 C CG  . PHE A 1 235 ? -46.398  -21.676 26.107  1.00 61.87  ? 261  PHE A CG  1 
ATOM   1727 C CD1 . PHE A 1 235 ? -45.779  -22.314 25.088  1.00 51.36  ? 261  PHE A CD1 1 
ATOM   1728 C CD2 . PHE A 1 235 ? -45.636  -20.998 27.005  1.00 55.51  ? 261  PHE A CD2 1 
ATOM   1729 C CE1 . PHE A 1 235 ? -44.424  -22.317 24.990  1.00 61.69  ? 261  PHE A CE1 1 
ATOM   1730 C CE2 . PHE A 1 235 ? -44.305  -20.951 26.875  1.00 49.08  ? 261  PHE A CE2 1 
ATOM   1731 C CZ  . PHE A 1 235 ? -43.683  -21.622 25.882  1.00 51.77  ? 261  PHE A CZ  1 
ATOM   1732 N N   . ASN A 1 236 ? -49.393  -23.933 28.455  1.00 102.83 ? 262  ASN A N   1 
ATOM   1733 C CA  . ASN A 1 236 ? -50.319  -24.114 29.592  1.00 118.09 ? 262  ASN A CA  1 
ATOM   1734 C C   . ASN A 1 236 ? -51.644  -24.761 29.257  1.00 114.64 ? 262  ASN A C   1 
ATOM   1735 O O   . ASN A 1 236 ? -52.671  -24.480 29.884  1.00 119.74 ? 262  ASN A O   1 
ATOM   1736 C CB  . ASN A 1 236 ? -50.529  -22.789 30.352  1.00 131.78 ? 262  ASN A CB  1 
ATOM   1737 C CG  . ASN A 1 236 ? -49.300  -22.355 31.140  1.00 132.19 ? 262  ASN A CG  1 
ATOM   1738 O OD1 . ASN A 1 236 ? -48.937  -21.176 31.149  1.00 135.63 ? 262  ASN A OD1 1 
ATOM   1739 N ND2 . ASN A 1 236 ? -48.628  -23.315 31.769  1.00 121.71 ? 262  ASN A ND2 1 
ATOM   1740 N N   . ALA A 1 237 ? -51.596  -25.698 28.324  1.00 107.44 ? 263  ALA A N   1 
ATOM   1741 C CA  . ALA A 1 237 ? -52.782  -26.409 27.901  1.00 105.76 ? 263  ALA A CA  1 
ATOM   1742 C C   . ALA A 1 237 ? -52.391  -27.834 27.585  1.00 107.50 ? 263  ALA A C   1 
ATOM   1743 O O   . ALA A 1 237 ? -51.271  -28.084 27.144  1.00 98.29  ? 263  ALA A O   1 
ATOM   1744 C CB  . ALA A 1 237 ? -53.389  -25.748 26.681  1.00 112.39 ? 263  ALA A CB  1 
ATOM   1745 N N   . PRO A 1 238 ? -53.326  -28.775 27.767  1.00 111.34 ? 264  PRO A N   1 
ATOM   1746 C CA  . PRO A 1 238 ? -53.037  -30.159 27.504  1.00 105.15 ? 264  PRO A CA  1 
ATOM   1747 C C   . PRO A 1 238 ? -53.684  -30.642 26.220  1.00 101.75 ? 264  PRO A C   1 
ATOM   1748 O O   . PRO A 1 238 ? -54.413  -29.894 25.565  1.00 106.27 ? 264  PRO A O   1 
ATOM   1749 C CB  . PRO A 1 238 ? -53.745  -30.841 28.664  1.00 116.87 ? 264  PRO A CB  1 
ATOM   1750 C CG  . PRO A 1 238 ? -55.008  -30.031 28.808  1.00 105.44 ? 264  PRO A CG  1 
ATOM   1751 C CD  . PRO A 1 238 ? -54.674  -28.626 28.351  1.00 105.93 ? 264  PRO A CD  1 
ATOM   1752 N N   . PHE A 1 239 ? -53.442  -31.907 25.899  1.00 106.48 ? 265  PHE A N   1 
ATOM   1753 C CA  . PHE A 1 239 ? -54.033  -32.557 24.732  1.00 103.27 ? 265  PHE A CA  1 
ATOM   1754 C C   . PHE A 1 239 ? -55.547  -32.249 24.851  1.00 103.76 ? 265  PHE A C   1 
ATOM   1755 O O   . PHE A 1 239 ? -56.077  -32.367 25.959  1.00 118.24 ? 265  PHE A O   1 
ATOM   1756 C CB  . PHE A 1 239 ? -53.763  -34.053 24.867  1.00 91.44  ? 265  PHE A CB  1 
ATOM   1757 C CG  . PHE A 1 239 ? -54.190  -34.868 23.691  1.00 96.02  ? 265  PHE A CG  1 
ATOM   1758 C CD1 . PHE A 1 239 ? -53.260  -35.276 22.739  1.00 92.38  ? 265  PHE A CD1 1 
ATOM   1759 C CD2 . PHE A 1 239 ? -55.511  -35.261 23.550  1.00 92.33  ? 265  PHE A CD2 1 
ATOM   1760 C CE1 . PHE A 1 239 ? -53.646  -36.059 21.667  1.00 96.53  ? 265  PHE A CE1 1 
ATOM   1761 C CE2 . PHE A 1 239 ? -55.908  -36.024 22.469  1.00 93.41  ? 265  PHE A CE2 1 
ATOM   1762 C CZ  . PHE A 1 239 ? -54.975  -36.428 21.529  1.00 98.33  ? 265  PHE A CZ  1 
ATOM   1763 N N   . PRO A 1 240 ? -56.292  -32.016 23.757  1.00 100.27 ? 266  PRO A N   1 
ATOM   1764 C CA  . PRO A 1 240 ? -55.854  -32.069 22.358  1.00 100.08 ? 266  PRO A CA  1 
ATOM   1765 C C   . PRO A 1 240 ? -54.952  -30.978 21.739  1.00 89.77  ? 266  PRO A C   1 
ATOM   1766 O O   . PRO A 1 240 ? -54.842  -30.932 20.523  1.00 93.77  ? 266  PRO A O   1 
ATOM   1767 C CB  . PRO A 1 240 ? -57.192  -32.119 21.594  1.00 90.37  ? 266  PRO A CB  1 
ATOM   1768 C CG  . PRO A 1 240 ? -58.236  -31.603 22.554  1.00 88.98  ? 266  PRO A CG  1 
ATOM   1769 C CD  . PRO A 1 240 ? -57.566  -31.293 23.867  1.00 95.93  ? 266  PRO A CD  1 
ATOM   1770 N N   . CYS A 1 241 ? -54.329  -30.111 22.525  1.00 76.63  ? 267  CYS A N   1 
ATOM   1771 C CA  . CYS A 1 241 ? -53.441  -29.124 21.937  1.00 81.44  ? 267  CYS A CA  1 
ATOM   1772 C C   . CYS A 1 241 ? -52.120  -29.838 21.716  1.00 74.55  ? 267  CYS A C   1 
ATOM   1773 O O   . CYS A 1 241 ? -51.478  -30.215 22.673  1.00 83.89  ? 267  CYS A O   1 
ATOM   1774 C CB  . CYS A 1 241 ? -53.237  -27.926 22.851  1.00 86.26  ? 267  CYS A CB  1 
ATOM   1775 S SG  . CYS A 1 241 ? -52.365  -26.586 22.010  1.00 80.38  ? 267  CYS A SG  1 
ATOM   1776 N N   . VAL A 1 242 ? -51.641  -29.877 20.475  1.00 83.39  ? 268  VAL A N   1 
ATOM   1777 C CA  . VAL A 1 242 ? -50.406  -30.603 20.160  1.00 75.39  ? 268  VAL A CA  1 
ATOM   1778 C C   . VAL A 1 242 ? -49.398  -29.837 19.291  1.00 67.47  ? 268  VAL A C   1 
ATOM   1779 O O   . VAL A 1 242 ? -49.611  -29.676 18.093  1.00 71.31  ? 268  VAL A O   1 
ATOM   1780 C CB  . VAL A 1 242 ? -50.780  -31.881 19.357  1.00 79.76  ? 268  VAL A CB  1 
ATOM   1781 C CG1 . VAL A 1 242 ? -49.551  -32.743 19.075  1.00 71.93  ? 268  VAL A CG1 1 
ATOM   1782 C CG2 . VAL A 1 242 ? -51.847  -32.677 20.091  1.00 76.72  ? 268  VAL A CG2 1 
ATOM   1783 N N   . PRO A 1 243 ? -48.227  -29.529 19.848  1.00 62.60  ? 269  PRO A N   1 
ATOM   1784 C CA  . PRO A 1 243 ? -47.171  -28.814 19.133  1.00 66.24  ? 269  PRO A CA  1 
ATOM   1785 C C   . PRO A 1 243 ? -46.416  -29.592 18.092  1.00 68.69  ? 269  PRO A C   1 
ATOM   1786 O O   . PRO A 1 243 ? -46.488  -30.806 18.050  1.00 90.94  ? 269  PRO A O   1 
ATOM   1787 C CB  . PRO A 1 243 ? -46.170  -28.477 20.235  1.00 54.64  ? 269  PRO A CB  1 
ATOM   1788 C CG  . PRO A 1 243 ? -46.996  -28.395 21.461  1.00 67.82  ? 269  PRO A CG  1 
ATOM   1789 C CD  . PRO A 1 243 ? -48.007  -29.495 21.298  1.00 69.23  ? 269  PRO A CD  1 
ATOM   1790 N N   . CYS A 1 244 ? -45.740  -28.858 17.219  1.00 76.98  ? 270  CYS A N   1 
ATOM   1791 C CA  . CYS A 1 244 ? -44.911  -29.452 16.210  1.00 75.51  ? 270  CYS A CA  1 
ATOM   1792 C C   . CYS A 1 244 ? -43.653  -29.866 16.971  1.00 76.96  ? 270  CYS A C   1 
ATOM   1793 O O   . CYS A 1 244 ? -43.310  -29.265 17.994  1.00 64.13  ? 270  CYS A O   1 
ATOM   1794 C CB  . CYS A 1 244 ? -44.638  -28.473 15.031  1.00 65.02  ? 270  CYS A CB  1 
ATOM   1795 S SG  . CYS A 1 244 ? -46.130  -28.286 13.994  1.00 96.96  ? 270  CYS A SG  1 
ATOM   1796 N N   . ASP A 1 245 ? -43.010  -30.933 16.523  1.00 85.47  ? 271  ASP A N   1 
ATOM   1797 C CA  . ASP A 1 245 ? -41.808  -31.419 17.186  1.00 89.27  ? 271  ASP A CA  1 
ATOM   1798 C C   . ASP A 1 245 ? -40.777  -30.328 17.402  1.00 80.35  ? 271  ASP A C   1 
ATOM   1799 O O   . ASP A 1 245 ? -40.385  -29.634 16.473  1.00 84.54  ? 271  ASP A O   1 
ATOM   1800 C CB  . ASP A 1 245 ? -41.188  -32.592 16.406  1.00 106.58 ? 271  ASP A CB  1 
ATOM   1801 C CG  . ASP A 1 245 ? -42.085  -33.841 16.395  1.00 109.63 ? 271  ASP A CG  1 
ATOM   1802 O OD1 . ASP A 1 245 ? -43.114  -33.866 17.110  1.00 116.86 ? 271  ASP A OD1 1 
ATOM   1803 O OD2 . ASP A 1 245 ? -41.736  -34.812 15.697  1.00 97.12  ? 271  ASP A OD2 1 
ATOM   1804 N N   . GLY A 1 246 ? -40.360  -30.176 18.651  1.00 84.80  ? 272  GLY A N   1 
ATOM   1805 C CA  . GLY A 1 246 ? -39.357  -29.185 19.025  1.00 90.28  ? 272  GLY A CA  1 
ATOM   1806 C C   . GLY A 1 246 ? -39.930  -27.798 19.105  1.00 100.10 ? 272  GLY A C   1 
ATOM   1807 O O   . GLY A 1 246 ? -39.195  -26.822 19.030  1.00 104.83 ? 272  GLY A O   1 
ATOM   1808 N N   . GLY A 1 247 ? -41.247  -27.711 19.272  1.00 109.67 ? 273  GLY A N   1 
ATOM   1809 C CA  . GLY A 1 247 ? -41.941  -26.420 19.339  1.00 110.86 ? 273  GLY A CA  1 
ATOM   1810 C C   . GLY A 1 247 ? -41.633  -25.502 18.153  1.00 99.34  ? 273  GLY A C   1 
ATOM   1811 O O   . GLY A 1 247 ? -41.533  -24.283 18.320  1.00 86.89  ? 273  GLY A O   1 
ATOM   1812 N N   . ALA A 1 248 ? -41.483  -26.088 16.962  1.00 85.66  ? 274  ALA A N   1 
ATOM   1813 C CA  . ALA A 1 248 ? -41.169  -25.325 15.741  1.00 84.32  ? 274  ALA A CA  1 
ATOM   1814 C C   . ALA A 1 248 ? -42.388  -24.616 15.168  1.00 74.73  ? 274  ALA A C   1 
ATOM   1815 O O   . ALA A 1 248 ? -43.507  -25.110 15.264  1.00 76.10  ? 274  ALA A O   1 
ATOM   1816 C CB  . ALA A 1 248 ? -40.587  -26.244 14.689  1.00 79.92  ? 274  ALA A CB  1 
ATOM   1817 N N   . SER A 1 249 ? -42.163  -23.505 14.481  1.00 72.33  ? 275  SER A N   1 
ATOM   1818 C CA  . SER A 1 249 ? -43.286  -22.785 13.915  1.00 67.39  ? 275  SER A CA  1 
ATOM   1819 C C   . SER A 1 249 ? -43.665  -23.394 12.622  1.00 56.88  ? 275  SER A C   1 
ATOM   1820 O O   . SER A 1 249 ? -42.917  -24.173 12.029  1.00 62.42  ? 275  SER A O   1 
ATOM   1821 C CB  . SER A 1 249 ? -42.950  -21.333 13.619  1.00 67.12  ? 275  SER A CB  1 
ATOM   1822 O OG  . SER A 1 249 ? -42.118  -21.222 12.490  1.00 64.63  ? 275  SER A OG  1 
ATOM   1823 N N   . ILE A 1 250 ? -44.835  -23.009 12.164  1.00 56.01  ? 276  ILE A N   1 
ATOM   1824 C CA  . ILE A 1 250 ? -45.314  -23.454 10.875  1.00 58.06  ? 276  ILE A CA  1 
ATOM   1825 C C   . ILE A 1 250 ? -44.219  -22.947 9.923   1.00 59.32  ? 276  ILE A C   1 
ATOM   1826 O O   . ILE A 1 250 ? -43.490  -21.991 10.239  1.00 50.82  ? 276  ILE A O   1 
ATOM   1827 C CB  . ILE A 1 250 ? -46.640  -22.785 10.530  1.00 56.13  ? 276  ILE A CB  1 
ATOM   1828 C CG1 . ILE A 1 250 ? -47.252  -23.369 9.285   1.00 61.87  ? 276  ILE A CG1 1 
ATOM   1829 C CG2 . ILE A 1 250 ? -46.443  -21.291 10.340  1.00 62.59  ? 276  ILE A CG2 1 
ATOM   1830 C CD1 . ILE A 1 250 ? -48.619  -22.769 8.981   1.00 60.43  ? 276  ILE A CD1 1 
ATOM   1831 N N   . ASN A 1 251 ? -44.027  -23.654 8.829   1.00 58.76  ? 277  ASN A N   1 
ATOM   1832 C CA  . ASN A 1 251 ? -43.014  -23.290 7.863   1.00 65.01  ? 277  ASN A CA  1 
ATOM   1833 C C   . ASN A 1 251 ? -43.667  -22.856 6.584   1.00 65.68  ? 277  ASN A C   1 
ATOM   1834 O O   . ASN A 1 251 ? -44.271  -23.669 5.860   1.00 60.12  ? 277  ASN A O   1 
ATOM   1835 C CB  . ASN A 1 251 ? -42.076  -24.466 7.617   1.00 74.03  ? 277  ASN A CB  1 
ATOM   1836 C CG  . ASN A 1 251 ? -40.982  -24.138 6.633   1.00 71.14  ? 277  ASN A CG  1 
ATOM   1837 O OD1 . ASN A 1 251 ? -39.809  -24.232 6.967   1.00 74.64  ? 277  ASN A OD1 1 
ATOM   1838 N ND2 . ASN A 1 251 ? -41.353  -23.585 5.496   1.00 78.41  ? 277  ASN A ND2 1 
ATOM   1839 N N   . ILE A 1 252 ? -43.562  -21.565 6.304   1.00 67.94  ? 278  ILE A N   1 
ATOM   1840 C CA  . ILE A 1 252 ? -44.165  -21.016 5.104   1.00 69.75  ? 278  ILE A CA  1 
ATOM   1841 C C   . ILE A 1 252 ? -43.121  -20.552 4.106   1.00 61.17  ? 278  ILE A C   1 
ATOM   1842 O O   . ILE A 1 252 ? -42.259  -19.730 4.416   1.00 63.82  ? 278  ILE A O   1 
ATOM   1843 C CB  . ILE A 1 252 ? -45.115  -19.866 5.441   1.00 73.23  ? 278  ILE A CB  1 
ATOM   1844 C CG1 . ILE A 1 252 ? -46.089  -20.321 6.544   1.00 75.07  ? 278  ILE A CG1 1 
ATOM   1845 C CG2 . ILE A 1 252 ? -45.841  -19.432 4.176   1.00 68.75  ? 278  ILE A CG2 1 
ATOM   1846 C CD1 . ILE A 1 252 ? -47.056  -19.253 7.020   1.00 78.44  ? 278  ILE A CD1 1 
ATOM   1847 N N   . ASP A 1 253 ? -43.243  -21.069 2.892   1.00 68.27  ? 279  ASP A N   1 
ATOM   1848 C CA  . ASP A 1 253 ? -42.344  -20.752 1.799   1.00 76.82  ? 279  ASP A CA  1 
ATOM   1849 C C   . ASP A 1 253 ? -42.432  -19.256 1.445   1.00 77.67  ? 279  ASP A C   1 
ATOM   1850 O O   . ASP A 1 253 ? -43.519  -18.658 1.456   1.00 67.56  ? 279  ASP A O   1 
ATOM   1851 C CB  . ASP A 1 253 ? -42.718  -21.623 0.584   1.00 85.86  ? 279  ASP A CB  1 
ATOM   1852 C CG  . ASP A 1 253 ? -41.751  -21.479 -0.570  1.00 92.29  ? 279  ASP A CG  1 
ATOM   1853 O OD1 . ASP A 1 253 ? -40.625  -20.977 -0.364  1.00 89.48  ? 279  ASP A OD1 1 
ATOM   1854 O OD2 . ASP A 1 253 ? -42.101  -21.936 -1.676  1.00 106.23 ? 279  ASP A OD2 1 
ATOM   1855 N N   . ARG A 1 254 ? -41.277  -18.674 1.125   1.00 79.19  ? 280  ARG A N   1 
ATOM   1856 C CA  . ARG A 1 254 ? -41.161  -17.257 0.756   1.00 75.89  ? 280  ARG A CA  1 
ATOM   1857 C C   . ARG A 1 254 ? -42.198  -16.858 -0.307  1.00 68.90  ? 280  ARG A C   1 
ATOM   1858 O O   . ARG A 1 254 ? -42.834  -15.803 -0.211  1.00 66.33  ? 280  ARG A O   1 
ATOM   1859 C CB  . ARG A 1 254 ? -39.768  -16.978 0.185   1.00 79.50  ? 280  ARG A CB  1 
ATOM   1860 C CG  . ARG A 1 254 ? -39.481  -15.503 0.004   1.00 98.57  ? 280  ARG A CG  1 
ATOM   1861 C CD  . ARG A 1 254 ? -38.236  -15.262 -0.825  1.00 108.00 ? 280  ARG A CD  1 
ATOM   1862 N NE  . ARG A 1 254 ? -37.862  -13.842 -0.880  1.00 116.61 ? 280  ARG A NE  1 
ATOM   1863 C CZ  . ARG A 1 254 ? -38.463  -12.911 -1.629  1.00 113.56 ? 280  ARG A CZ  1 
ATOM   1864 N NH1 . ARG A 1 254 ? -39.620  -13.172 -2.249  1.00 89.77  ? 280  ARG A NH1 1 
ATOM   1865 N NH2 . ARG A 1 254 ? -37.996  -11.660 -1.618  1.00 109.00 ? 280  ARG A NH2 1 
ATOM   1866 N N   . PHE A 1 255 ? -42.403  -17.721 -1.293  1.00 63.87  ? 281  PHE A N   1 
ATOM   1867 C CA  . PHE A 1 255 ? -43.353  -17.419 -2.366  1.00 65.73  ? 281  PHE A CA  1 
ATOM   1868 C C   . PHE A 1 255 ? -44.725  -18.006 -2.179  1.00 60.46  ? 281  PHE A C   1 
ATOM   1869 O O   . PHE A 1 255 ? -45.543  -17.948 -3.081  1.00 60.01  ? 281  PHE A O   1 
ATOM   1870 C CB  . PHE A 1 255 ? -42.791  -17.846 -3.731  1.00 66.34  ? 281  PHE A CB  1 
ATOM   1871 C CG  . PHE A 1 255 ? -41.473  -17.203 -4.059  1.00 73.83  ? 281  PHE A CG  1 
ATOM   1872 C CD1 . PHE A 1 255 ? -41.416  -15.875 -4.456  1.00 71.42  ? 281  PHE A CD1 1 
ATOM   1873 C CD2 . PHE A 1 255 ? -40.295  -17.932 -3.997  1.00 81.39  ? 281  PHE A CD2 1 
ATOM   1874 C CE1 . PHE A 1 255 ? -40.204  -15.278 -4.742  1.00 78.19  ? 281  PHE A CE1 1 
ATOM   1875 C CE2 . PHE A 1 255 ? -39.076  -17.339 -4.286  1.00 83.16  ? 281  PHE A CE2 1 
ATOM   1876 C CZ  . PHE A 1 255 ? -39.031  -16.011 -4.658  1.00 78.31  ? 281  PHE A CZ  1 
ATOM   1877 N N   . ALA A 1 256 ? -45.034  -18.433 -0.971  1.00 64.13  ? 282  ALA A N   1 
ATOM   1878 C CA  . ALA A 1 256 ? -46.328  -19.055 -0.710  1.00 62.44  ? 282  ALA A CA  1 
ATOM   1879 C C   . ALA A 1 256 ? -47.544  -18.186 -0.987  1.00 60.41  ? 282  ALA A C   1 
ATOM   1880 O O   . ALA A 1 256 ? -48.624  -18.704 -1.277  1.00 62.78  ? 282  ALA A O   1 
ATOM   1881 C CB  . ALA A 1 256 ? -46.366  -19.555 0.722   1.00 63.79  ? 282  ALA A CB  1 
ATOM   1882 N N   . PHE A 1 257 ? -47.396  -16.875 -0.830  1.00 67.47  ? 283  PHE A N   1 
ATOM   1883 C CA  . PHE A 1 257 ? -48.528  -15.964 -1.045  1.00 70.73  ? 283  PHE A CA  1 
ATOM   1884 C C   . PHE A 1 257 ? -48.329  -14.945 -2.176  1.00 64.39  ? 283  PHE A C   1 
ATOM   1885 O O   . PHE A 1 257 ? -49.131  -14.027 -2.290  1.00 55.92  ? 283  PHE A O   1 
ATOM   1886 C CB  . PHE A 1 257 ? -48.803  -15.131 0.218   1.00 68.24  ? 283  PHE A CB  1 
ATOM   1887 C CG  . PHE A 1 257 ? -48.973  -15.926 1.481   1.00 68.19  ? 283  PHE A CG  1 
ATOM   1888 C CD1 . PHE A 1 257 ? -50.063  -16.748 1.659   1.00 82.72  ? 283  PHE A CD1 1 
ATOM   1889 C CD2 . PHE A 1 257 ? -48.198  -15.628 2.583   1.00 74.76  ? 283  PHE A CD2 1 
ATOM   1890 C CE1 . PHE A 1 257 ? -50.257  -17.417 2.852   1.00 77.92  ? 283  PHE A CE1 1 
ATOM   1891 C CE2 . PHE A 1 257 ? -48.414  -16.246 3.797   1.00 74.53  ? 283  PHE A CE2 1 
ATOM   1892 C CZ  . PHE A 1 257 ? -49.445  -17.144 3.931   1.00 77.58  ? 283  PHE A CZ  1 
ATOM   1893 N N   . GLN A 1 258 ? -47.329  -15.133 -3.044  1.00 74.50  ? 284  GLN A N   1 
ATOM   1894 C CA  . GLN A 1 258 ? -47.055  -14.158 -4.110  1.00 63.77  ? 284  GLN A CA  1 
ATOM   1895 C C   . GLN A 1 258 ? -48.214  -13.850 -5.029  1.00 57.31  ? 284  GLN A C   1 
ATOM   1896 O O   . GLN A 1 258 ? -48.281  -12.758 -5.567  1.00 64.00  ? 284  GLN A O   1 
ATOM   1897 C CB  . GLN A 1 258 ? -45.868  -14.545 -4.959  1.00 65.58  ? 284  GLN A CB  1 
ATOM   1898 C CG  . GLN A 1 258 ? -46.076  -15.755 -5.831  1.00 78.58  ? 284  GLN A CG  1 
ATOM   1899 C CD  . GLN A 1 258 ? -44.923  -15.995 -6.801  1.00 92.72  ? 284  GLN A CD  1 
ATOM   1900 O OE1 . GLN A 1 258 ? -44.869  -17.043 -7.452  1.00 104.63 ? 284  GLN A OE1 1 
ATOM   1901 N NE2 . GLN A 1 258 ? -43.998  -15.023 -6.912  1.00 79.25  ? 284  GLN A NE2 1 
ATOM   1902 N N   . ASN A 1 259 ? -49.131  -14.790 -5.208  1.00 60.24  ? 285  ASN A N   1 
ATOM   1903 C CA  . ASN A 1 259 ? -50.282  -14.562 -6.079  1.00 56.93  ? 285  ASN A CA  1 
ATOM   1904 C C   . ASN A 1 259 ? -51.564  -14.261 -5.391  1.00 48.26  ? 285  ASN A C   1 
ATOM   1905 O O   . ASN A 1 259 ? -52.595  -14.210 -6.040  1.00 52.74  ? 285  ASN A O   1 
ATOM   1906 C CB  . ASN A 1 259 ? -50.533  -15.777 -6.970  1.00 71.18  ? 285  ASN A CB  1 
ATOM   1907 C CG  . ASN A 1 259 ? -49.485  -15.943 -8.039  1.00 86.02  ? 285  ASN A CG  1 
ATOM   1908 O OD1 . ASN A 1 259 ? -48.714  -15.011 -8.325  1.00 81.09  ? 285  ASN A OD1 1 
ATOM   1909 N ND2 . ASN A 1 259 ? -49.479  -17.126 -8.691  1.00 99.00  ? 285  ASN A ND2 1 
ATOM   1910 N N   . LEU A 1 260 ? -51.554  -14.147 -4.076  1.00 59.38  ? 286  LEU A N   1 
ATOM   1911 C CA  . LEU A 1 260 ? -52.802  -13.862 -3.342  1.00 66.10  ? 286  LEU A CA  1 
ATOM   1912 C C   . LEU A 1 260 ? -53.015  -12.363 -3.132  1.00 72.05  ? 286  LEU A C   1 
ATOM   1913 O O   . LEU A 1 260 ? -53.257  -11.910 -2.009  1.00 68.60  ? 286  LEU A O   1 
ATOM   1914 C CB  . LEU A 1 260 ? -52.778  -14.618 -2.016  1.00 76.35  ? 286  LEU A CB  1 
ATOM   1915 C CG  . LEU A 1 260 ? -53.166  -16.097 -2.038  1.00 66.83  ? 286  LEU A CG  1 
ATOM   1916 C CD1 . LEU A 1 260 ? -52.660  -16.843 -3.250  1.00 86.18  ? 286  LEU A CD1 1 
ATOM   1917 C CD2 . LEU A 1 260 ? -52.715  -16.730 -0.737  1.00 72.01  ? 286  LEU A CD2 1 
ATOM   1918 N N   . THR A 1 261 ? -53.097  -11.626 -4.243  1.00 58.84  ? 287  THR A N   1 
ATOM   1919 C CA  . THR A 1 261 ? -53.215  -10.185 -4.190  1.00 49.62  ? 287  THR A CA  1 
ATOM   1920 C C   . THR A 1 261 ? -54.541  -9.678  -3.651  1.00 51.84  ? 287  THR A C   1 
ATOM   1921 O O   . THR A 1 261 ? -54.635  -8.517  -3.256  1.00 54.91  ? 287  THR A O   1 
ATOM   1922 C CB  . THR A 1 261 ? -52.907  -9.551  -5.564  1.00 58.69  ? 287  THR A CB  1 
ATOM   1923 O OG1 . THR A 1 261 ? -53.934  -9.872  -6.499  1.00 59.46  ? 287  THR A OG1 1 
ATOM   1924 C CG2 . THR A 1 261 ? -51.591  -10.064 -6.093  1.00 66.79  ? 287  THR A CG2 1 
ATOM   1925 N N   . GLN A 1 262 ? -55.568  -10.522 -3.622  1.00 43.62  ? 288  GLN A N   1 
ATOM   1926 C CA  . GLN A 1 262 ? -56.882  -10.086 -3.099  1.00 50.15  ? 288  GLN A CA  1 
ATOM   1927 C C   . GLN A 1 262 ? -57.077  -10.380 -1.587  1.00 54.03  ? 288  GLN A C   1 
ATOM   1928 O O   . GLN A 1 262 ? -58.137  -10.140 -1.013  1.00 46.98  ? 288  GLN A O   1 
ATOM   1929 C CB  . GLN A 1 262 ? -57.955  -10.821 -3.877  1.00 53.10  ? 288  GLN A CB  1 
ATOM   1930 C CG  . GLN A 1 262 ? -57.785  -10.562 -5.341  1.00 68.45  ? 288  GLN A CG  1 
ATOM   1931 C CD  . GLN A 1 262 ? -57.749  -9.078  -5.584  1.00 72.46  ? 288  GLN A CD  1 
ATOM   1932 O OE1 . GLN A 1 262 ? -58.630  -8.348  -5.111  1.00 72.13  ? 288  GLN A OE1 1 
ATOM   1933 N NE2 . GLN A 1 262 ? -56.725  -8.610  -6.311  1.00 62.07  ? 288  GLN A NE2 1 
ATOM   1934 N N   . LEU A 1 263 ? -56.028  -10.832 -0.934  1.00 47.28  ? 289  LEU A N   1 
ATOM   1935 C CA  . LEU A 1 263 ? -56.147  -11.209 0.439   1.00 54.76  ? 289  LEU A CA  1 
ATOM   1936 C C   . LEU A 1 263 ? -56.427  -10.038 1.387   1.00 52.71  ? 289  LEU A C   1 
ATOM   1937 O O   . LEU A 1 263 ? -55.682  -9.046  1.432   1.00 55.40  ? 289  LEU A O   1 
ATOM   1938 C CB  . LEU A 1 263 ? -54.851  -11.941 0.839   1.00 57.31  ? 289  LEU A CB  1 
ATOM   1939 C CG  . LEU A 1 263 ? -54.941  -12.931 1.982   1.00 57.84  ? 289  LEU A CG  1 
ATOM   1940 C CD1 . LEU A 1 263 ? -55.743  -14.121 1.510   1.00 58.99  ? 289  LEU A CD1 1 
ATOM   1941 C CD2 . LEU A 1 263 ? -53.573  -13.395 2.393   1.00 60.34  ? 289  LEU A CD2 1 
ATOM   1942 N N   . ARG A 1 264 ? -57.542  -10.134 2.097   1.00 52.30  ? 290  ARG A N   1 
ATOM   1943 C CA  . ARG A 1 264 ? -57.932  -9.140  3.106   1.00 50.93  ? 290  ARG A CA  1 
ATOM   1944 C C   . ARG A 1 264 ? -57.727  -9.581  4.548   1.00 47.16  ? 290  ARG A C   1 
ATOM   1945 O O   . ARG A 1 264 ? -57.635  -8.746  5.433   1.00 50.37  ? 290  ARG A O   1 
ATOM   1946 C CB  . ARG A 1 264 ? -59.410  -8.801  3.044   1.00 50.87  ? 290  ARG A CB  1 
ATOM   1947 C CG  . ARG A 1 264 ? -59.823  -7.707  2.112   1.00 61.99  ? 290  ARG A CG  1 
ATOM   1948 C CD  . ARG A 1 264 ? -59.565  -8.028  0.688   1.00 67.69  ? 290  ARG A CD  1 
ATOM   1949 N NE  . ARG A 1 264 ? -60.015  -6.918  -0.116  1.00 70.19  ? 290  ARG A NE  1 
ATOM   1950 C CZ  . ARG A 1 264 ? -59.848  -6.846  -1.423  1.00 65.12  ? 290  ARG A CZ  1 
ATOM   1951 N NH1 . ARG A 1 264 ? -59.237  -7.828  -2.059  1.00 60.08  ? 290  ARG A NH1 1 
ATOM   1952 N NH2 . ARG A 1 264 ? -60.266  -5.775  -2.081  1.00 73.96  ? 290  ARG A NH2 1 
ATOM   1953 N N   . TYR A 1 265 ? -57.945  -10.860 4.800   1.00 57.24  ? 291  TYR A N   1 
ATOM   1954 C CA  . TYR A 1 265 ? -57.848  -11.415 6.151   1.00 51.00  ? 291  TYR A CA  1 
ATOM   1955 C C   . TYR A 1 265 ? -56.919  -12.579 6.176   1.00 43.68  ? 291  TYR A C   1 
ATOM   1956 O O   . TYR A 1 265 ? -57.113  -13.536 5.429   1.00 48.13  ? 291  TYR A O   1 
ATOM   1957 C CB  . TYR A 1 265 ? -59.192  -11.928 6.568   1.00 49.27  ? 291  TYR A CB  1 
ATOM   1958 C CG  . TYR A 1 265 ? -60.303  -10.913 6.578   1.00 53.08  ? 291  TYR A CG  1 
ATOM   1959 C CD1 . TYR A 1 265 ? -61.077  -10.719 5.446   1.00 56.77  ? 291  TYR A CD1 1 
ATOM   1960 C CD2 . TYR A 1 265 ? -60.707  -10.296 7.765   1.00 53.84  ? 291  TYR A CD2 1 
ATOM   1961 C CE1 . TYR A 1 265 ? -62.166  -9.864  5.461   1.00 52.83  ? 291  TYR A CE1 1 
ATOM   1962 C CE2 . TYR A 1 265 ? -61.771  -9.416  7.784   1.00 59.01  ? 291  TYR A CE2 1 
ATOM   1963 C CZ  . TYR A 1 265 ? -62.488  -9.200  6.616   1.00 61.07  ? 291  TYR A CZ  1 
ATOM   1964 O OH  . TYR A 1 265 ? -63.569  -8.366  6.593   1.00 75.73  ? 291  TYR A OH  1 
ATOM   1965 N N   . LEU A 1 266 ? -55.920  -12.502 7.041   1.00 36.59  ? 292  LEU A N   1 
ATOM   1966 C CA  . LEU A 1 266 ? -54.921  -13.563 7.185   1.00 45.19  ? 292  LEU A CA  1 
ATOM   1967 C C   . LEU A 1 266 ? -54.818  -13.925 8.669   1.00 50.51  ? 292  LEU A C   1 
ATOM   1968 O O   . LEU A 1 266 ? -54.509  -13.065 9.513   1.00 42.23  ? 292  LEU A O   1 
ATOM   1969 C CB  . LEU A 1 266 ? -53.564  -13.096 6.677   1.00 41.18  ? 292  LEU A CB  1 
ATOM   1970 C CG  . LEU A 1 266 ? -52.462  -14.137 6.774   1.00 47.80  ? 292  LEU A CG  1 
ATOM   1971 C CD1 . LEU A 1 266 ? -52.862  -15.395 6.042   1.00 46.94  ? 292  LEU A CD1 1 
ATOM   1972 C CD2 . LEU A 1 266 ? -51.134  -13.597 6.252   1.00 46.42  ? 292  LEU A CD2 1 
ATOM   1973 N N   . ASN A 1 267 ? -55.122  -15.177 8.994   1.00 47.63  ? 293  ASN A N   1 
ATOM   1974 C CA  . ASN A 1 267 ? -55.061  -15.617 10.383  1.00 42.60  ? 293  ASN A CA  1 
ATOM   1975 C C   . ASN A 1 267 ? -53.927  -16.595 10.605  1.00 48.02  ? 293  ASN A C   1 
ATOM   1976 O O   . ASN A 1 267 ? -53.907  -17.675 10.031  1.00 51.05  ? 293  ASN A O   1 
ATOM   1977 C CB  . ASN A 1 267 ? -56.381  -16.217 10.790  1.00 41.50  ? 293  ASN A CB  1 
ATOM   1978 C CG  . ASN A 1 267 ? -56.504  -16.373 12.277  1.00 43.51  ? 293  ASN A CG  1 
ATOM   1979 O OD1 . ASN A 1 267 ? -55.504  -16.336 13.004  1.00 47.76  ? 293  ASN A OD1 1 
ATOM   1980 N ND2 . ASN A 1 267 ? -57.729  -16.558 12.753  1.00 44.37  ? 293  ASN A ND2 1 
ATOM   1981 N N   . LEU A 1 268 ? -52.911  -16.135 11.321  1.00 46.22  ? 294  LEU A N   1 
ATOM   1982 C CA  . LEU A 1 268 ? -51.752  -16.945 11.636  1.00 47.26  ? 294  LEU A CA  1 
ATOM   1983 C C   . LEU A 1 268 ? -51.597  -17.065 13.150  1.00 50.15  ? 294  LEU A C   1 
ATOM   1984 O O   . LEU A 1 268 ? -50.478  -17.180 13.670  1.00 47.87  ? 294  LEU A O   1 
ATOM   1985 C CB  . LEU A 1 268 ? -50.487  -16.361 11.024  1.00 51.34  ? 294  LEU A CB  1 
ATOM   1986 C CG  . LEU A 1 268 ? -50.425  -16.391 9.500   1.00 58.99  ? 294  LEU A CG  1 
ATOM   1987 C CD1 . LEU A 1 268 ? -49.208  -15.671 8.970   1.00 52.72  ? 294  LEU A CD1 1 
ATOM   1988 C CD2 . LEU A 1 268 ? -50.427  -17.808 8.989   1.00 67.96  ? 294  LEU A CD2 1 
ATOM   1989 N N   . SER A 1 269 ? -52.723  -17.005 13.853  1.00 41.77  ? 295  SER A N   1 
ATOM   1990 C CA  . SER A 1 269 ? -52.700  -17.140 15.285  1.00 56.10  ? 295  SER A CA  1 
ATOM   1991 C C   . SER A 1 269 ? -52.308  -18.553 15.685  1.00 54.49  ? 295  SER A C   1 
ATOM   1992 O O   . SER A 1 269 ? -52.790  -19.506 15.098  1.00 56.84  ? 295  SER A O   1 
ATOM   1993 C CB  . SER A 1 269 ? -54.073  -16.885 15.870  1.00 51.39  ? 295  SER A CB  1 
ATOM   1994 O OG  . SER A 1 269 ? -54.472  -15.551 15.663  1.00 65.17  ? 295  SER A OG  1 
ATOM   1995 N N   . SER A 1 270 ? -51.369  -18.666 16.621  1.00 58.39  ? 296  SER A N   1 
ATOM   1996 C CA  . SER A 1 270 ? -50.943  -19.959 17.163  1.00 57.51  ? 296  SER A CA  1 
ATOM   1997 C C   . SER A 1 270 ? -50.349  -20.887 16.111  1.00 59.21  ? 296  SER A C   1 
ATOM   1998 O O   . SER A 1 270 ? -50.930  -21.948 15.772  1.00 51.00  ? 296  SER A O   1 
ATOM   1999 C CB  . SER A 1 270 ? -52.144  -20.626 17.856  1.00 56.09  ? 296  SER A CB  1 
ATOM   2000 O OG  . SER A 1 270 ? -51.750  -21.756 18.581  1.00 61.42  ? 296  SER A OG  1 
ATOM   2001 N N   . THR A 1 271 ? -49.229  -20.430 15.558  1.00 50.98  ? 297  THR A N   1 
ATOM   2002 C CA  . THR A 1 271 ? -48.466  -21.151 14.548  1.00 51.80  ? 297  THR A CA  1 
ATOM   2003 C C   . THR A 1 271 ? -47.013  -21.116 15.021  1.00 53.02  ? 297  THR A C   1 
ATOM   2004 O O   . THR A 1 271 ? -46.076  -21.447 14.302  1.00 58.91  ? 297  THR A O   1 
ATOM   2005 C CB  . THR A 1 271 ? -48.636  -20.495 13.157  1.00 52.92  ? 297  THR A CB  1 
ATOM   2006 O OG1 . THR A 1 271 ? -48.341  -19.091 13.262  1.00 49.10  ? 297  THR A OG1 1 
ATOM   2007 C CG2 . THR A 1 271 ? -50.080  -20.646 12.666  1.00 48.55  ? 297  THR A CG2 1 
ATOM   2008 N N   . SER A 1 272 ? -46.834  -20.626 16.232  1.00 54.49  ? 298  SER A N   1 
ATOM   2009 C CA  . SER A 1 272 ? -45.524  -20.571 16.865  1.00 59.69  ? 298  SER A CA  1 
ATOM   2010 C C   . SER A 1 272 ? -44.482  -19.837 16.081  1.00 55.91  ? 298  SER A C   1 
ATOM   2011 O O   . SER A 1 272 ? -43.292  -20.159 16.176  1.00 63.88  ? 298  SER A O   1 
ATOM   2012 C CB  . SER A 1 272 ? -45.045  -22.001 17.173  1.00 56.39  ? 298  SER A CB  1 
ATOM   2013 O OG  . SER A 1 272 ? -45.995  -22.659 18.005  1.00 52.85  ? 298  SER A OG  1 
ATOM   2014 N N   . LEU A 1 273 ? -44.905  -18.786 15.383  1.00 60.92  ? 299  LEU A N   1 
ATOM   2015 C CA  . LEU A 1 273 ? -43.978  -17.977 14.586  1.00 53.19  ? 299  LEU A CA  1 
ATOM   2016 C C   . LEU A 1 273 ? -42.978  -17.172 15.393  1.00 46.85  ? 299  LEU A C   1 
ATOM   2017 O O   . LEU A 1 273 ? -43.315  -16.545 16.387  1.00 53.45  ? 299  LEU A O   1 
ATOM   2018 C CB  . LEU A 1 273 ? -44.766  -17.011 13.718  1.00 60.16  ? 299  LEU A CB  1 
ATOM   2019 C CG  . LEU A 1 273 ? -45.473  -17.586 12.513  1.00 57.45  ? 299  LEU A CG  1 
ATOM   2020 C CD1 . LEU A 1 273 ? -46.532  -16.634 12.018  1.00 57.25  ? 299  LEU A CD1 1 
ATOM   2021 C CD2 . LEU A 1 273 ? -44.446  -17.898 11.446  1.00 55.92  ? 299  LEU A CD2 1 
ATOM   2022 N N   . ARG A 1 274 ? -41.740  -17.172 14.934  1.00 56.24  ? 300  ARG A N   1 
ATOM   2023 C CA  . ARG A 1 274 ? -40.671  -16.396 15.562  1.00 62.81  ? 300  ARG A CA  1 
ATOM   2024 C C   . ARG A 1 274 ? -40.244  -15.324 14.580  1.00 68.37  ? 300  ARG A C   1 
ATOM   2025 O O   . ARG A 1 274 ? -39.845  -14.228 14.980  1.00 67.56  ? 300  ARG A O   1 
ATOM   2026 C CB  . ARG A 1 274 ? -39.512  -17.291 15.997  1.00 70.17  ? 300  ARG A CB  1 
ATOM   2027 C CG  . ARG A 1 274 ? -39.880  -18.130 17.207  1.00 77.62  ? 300  ARG A CG  1 
ATOM   2028 C CD  . ARG A 1 274 ? -38.849  -19.163 17.609  1.00 87.35  ? 300  ARG A CD  1 
ATOM   2029 N NE  . ARG A 1 274 ? -39.289  -19.802 18.841  1.00 93.05  ? 300  ARG A NE  1 
ATOM   2030 C CZ  . ARG A 1 274 ? -40.223  -20.747 18.897  1.00 99.28  ? 300  ARG A CZ  1 
ATOM   2031 N NH1 . ARG A 1 274 ? -40.556  -21.252 20.074  1.00 98.66  ? 300  ARG A NH1 1 
ATOM   2032 N NH2 . ARG A 1 274 ? -40.853  -21.166 17.787  1.00 84.37  ? 300  ARG A NH2 1 
ATOM   2033 N N   . LYS A 1 275 ? -40.299  -15.659 13.292  1.00 75.97  ? 301  LYS A N   1 
ATOM   2034 C CA  . LYS A 1 275 ? -39.970  -14.706 12.244  1.00 82.27  ? 301  LYS A CA  1 
ATOM   2035 C C   . LYS A 1 275 ? -41.127  -14.583 11.274  1.00 73.28  ? 301  LYS A C   1 
ATOM   2036 O O   . LYS A 1 275 ? -41.792  -15.572 10.946  1.00 70.76  ? 301  LYS A O   1 
ATOM   2037 C CB  . LYS A 1 275 ? -38.686  -15.046 11.453  1.00 83.15  ? 301  LYS A CB  1 
ATOM   2038 C CG  . LYS A 1 275 ? -37.382  -15.003 12.250  1.00 106.54 ? 301  LYS A CG  1 
ATOM   2039 C CD  . LYS A 1 275 ? -36.143  -14.784 11.352  1.00 116.94 ? 301  LYS A CD  1 
ATOM   2040 C CE  . LYS A 1 275 ? -35.889  -15.840 10.279  1.00 109.28 ? 301  LYS A CE  1 
ATOM   2041 N NZ  . LYS A 1 275 ? -35.520  -17.168 10.834  1.00 112.99 ? 301  LYS A NZ  1 
ATOM   2042 N N   . ILE A 1 276 ? -41.409  -13.341 10.899  1.00 67.88  ? 302  ILE A N   1 
ATOM   2043 C CA  . ILE A 1 276 ? -42.455  -13.010 9.927   1.00 66.06  ? 302  ILE A CA  1 
ATOM   2044 C C   . ILE A 1 276 ? -41.678  -12.500 8.716   1.00 64.78  ? 302  ILE A C   1 
ATOM   2045 O O   . ILE A 1 276 ? -40.981  -11.487 8.821   1.00 65.86  ? 302  ILE A O   1 
ATOM   2046 C CB  . ILE A 1 276 ? -43.335  -11.841 10.393  1.00 59.97  ? 302  ILE A CB  1 
ATOM   2047 C CG1 . ILE A 1 276 ? -44.046  -12.177 11.686  1.00 54.25  ? 302  ILE A CG1 1 
ATOM   2048 C CG2 . ILE A 1 276 ? -44.361  -11.506 9.320   1.00 56.02  ? 302  ILE A CG2 1 
ATOM   2049 C CD1 . ILE A 1 276 ? -45.061  -13.272 11.510  1.00 60.03  ? 302  ILE A CD1 1 
ATOM   2050 N N   . ASN A 1 277 ? -41.751  -13.212 7.594   1.00 58.69  ? 303  ASN A N   1 
ATOM   2051 C CA  . ASN A 1 277 ? -41.037  -12.793 6.395   1.00 56.22  ? 303  ASN A CA  1 
ATOM   2052 C C   . ASN A 1 277 ? -41.823  -11.662 5.718   1.00 52.49  ? 303  ASN A C   1 
ATOM   2053 O O   . ASN A 1 277 ? -42.938  -11.875 5.220   1.00 54.43  ? 303  ASN A O   1 
ATOM   2054 C CB  . ASN A 1 277 ? -40.878  -13.974 5.436   1.00 64.63  ? 303  ASN A CB  1 
ATOM   2055 C CG  . ASN A 1 277 ? -39.872  -13.693 4.329   1.00 64.26  ? 303  ASN A CG  1 
ATOM   2056 O OD1 . ASN A 1 277 ? -39.353  -12.592 4.213   1.00 69.98  ? 303  ASN A OD1 1 
ATOM   2057 N ND2 . ASN A 1 277 ? -39.569  -14.701 3.541   1.00 64.85  ? 303  ASN A ND2 1 
ATOM   2058 N N   . ALA A 1 278 ? -41.246  -10.467 5.706   1.00 50.82  ? 304  ALA A N   1 
ATOM   2059 C CA  . ALA A 1 278 ? -41.898  -9.299  5.101   1.00 53.31  ? 304  ALA A CA  1 
ATOM   2060 C C   . ALA A 1 278 ? -42.263  -9.552  3.682   1.00 52.75  ? 304  ALA A C   1 
ATOM   2061 O O   . ALA A 1 278 ? -43.326  -9.139  3.224   1.00 55.91  ? 304  ALA A O   1 
ATOM   2062 C CB  . ALA A 1 278 ? -41.016  -8.083  5.177   1.00 54.81  ? 304  ALA A CB  1 
ATOM   2063 N N   . ALA A 1 279 ? -41.457  -10.355 3.019   1.00 53.95  ? 305  ALA A N   1 
ATOM   2064 C CA  . ALA A 1 279 ? -41.719  -10.653 1.636   1.00 54.41  ? 305  ALA A CA  1 
ATOM   2065 C C   . ALA A 1 279 ? -43.035  -11.325 1.394   1.00 54.12  ? 305  ALA A C   1 
ATOM   2066 O O   . ALA A 1 279 ? -43.520  -11.311 0.260   1.00 56.51  ? 305  ALA A O   1 
ATOM   2067 C CB  . ALA A 1 279 ? -40.599  -11.484 1.058   1.00 57.93  ? 305  ALA A CB  1 
ATOM   2068 N N   . TRP A 1 280 ? -43.631  -11.935 2.419   1.00 64.33  ? 306  TRP A N   1 
ATOM   2069 C CA  . TRP A 1 280 ? -44.907  -12.626 2.183   1.00 60.07  ? 306  TRP A CA  1 
ATOM   2070 C C   . TRP A 1 280 ? -45.973  -11.643 1.815   1.00 53.68  ? 306  TRP A C   1 
ATOM   2071 O O   . TRP A 1 280 ? -47.033  -12.037 1.331   1.00 45.03  ? 306  TRP A O   1 
ATOM   2072 C CB  . TRP A 1 280 ? -45.449  -13.404 3.391   1.00 67.96  ? 306  TRP A CB  1 
ATOM   2073 C CG  . TRP A 1 280 ? -44.587  -14.450 3.999   1.00 81.43  ? 306  TRP A CG  1 
ATOM   2074 C CD1 . TRP A 1 280 ? -43.935  -15.433 3.343   1.00 79.64  ? 306  TRP A CD1 1 
ATOM   2075 C CD2 . TRP A 1 280 ? -44.647  -14.878 5.365   1.00 82.30  ? 306  TRP A CD2 1 
ATOM   2076 N NE1 . TRP A 1 280 ? -43.377  -16.302 4.229   1.00 83.19  ? 306  TRP A NE1 1 
ATOM   2077 C CE2 . TRP A 1 280 ? -43.832  -16.002 5.482   1.00 84.82  ? 306  TRP A CE2 1 
ATOM   2078 C CE3 . TRP A 1 280 ? -45.272  -14.377 6.511   1.00 76.31  ? 306  TRP A CE3 1 
ATOM   2079 C CZ2 . TRP A 1 280 ? -43.606  -16.633 6.695   1.00 77.44  ? 306  TRP A CZ2 1 
ATOM   2080 C CZ3 . TRP A 1 280 ? -45.033  -14.984 7.704   1.00 78.97  ? 306  TRP A CZ3 1 
ATOM   2081 C CH2 . TRP A 1 280 ? -44.194  -16.094 7.795   1.00 72.55  ? 306  TRP A CH2 1 
ATOM   2082 N N   . PHE A 1 281 ? -45.769  -10.394 2.213   1.00 50.28  ? 307  PHE A N   1 
ATOM   2083 C CA  . PHE A 1 281 ? -46.744  -9.345  1.943   1.00 60.19  ? 307  PHE A CA  1 
ATOM   2084 C C   . PHE A 1 281 ? -46.479  -8.445  0.721   1.00 56.07  ? 307  PHE A C   1 
ATOM   2085 O O   . PHE A 1 281 ? -47.253  -7.548  0.482   1.00 55.17  ? 307  PHE A O   1 
ATOM   2086 C CB  . PHE A 1 281 ? -46.898  -8.473  3.186   1.00 58.49  ? 307  PHE A CB  1 
ATOM   2087 C CG  . PHE A 1 281 ? -47.261  -9.251  4.398   1.00 51.52  ? 307  PHE A CG  1 
ATOM   2088 C CD1 . PHE A 1 281 ? -48.546  -9.743  4.556   1.00 58.98  ? 307  PHE A CD1 1 
ATOM   2089 C CD2 . PHE A 1 281 ? -46.330  -9.488  5.384   1.00 54.37  ? 307  PHE A CD2 1 
ATOM   2090 C CE1 . PHE A 1 281 ? -48.875  -10.527 5.643   1.00 58.33  ? 307  PHE A CE1 1 
ATOM   2091 C CE2 . PHE A 1 281 ? -46.645  -10.280 6.474   1.00 51.78  ? 307  PHE A CE2 1 
ATOM   2092 C CZ  . PHE A 1 281 ? -47.920  -10.804 6.597   1.00 54.19  ? 307  PHE A CZ  1 
ATOM   2093 N N   . LYS A 1 282 ? -45.414  -8.688  -0.045  1.00 64.54  ? 308  LYS A N   1 
ATOM   2094 C CA  . LYS A 1 282 ? -45.109  -7.842  -1.224  1.00 61.72  ? 308  LYS A CA  1 
ATOM   2095 C C   . LYS A 1 282 ? -46.270  -7.592  -2.142  1.00 58.60  ? 308  LYS A C   1 
ATOM   2096 O O   . LYS A 1 282 ? -46.423  -6.494  -2.665  1.00 54.11  ? 308  LYS A O   1 
ATOM   2097 C CB  . LYS A 1 282 ? -44.109  -8.475  -2.183  1.00 56.68  ? 308  LYS A CB  1 
ATOM   2098 C CG  . LYS A 1 282 ? -42.659  -8.491  -1.841  1.00 65.84  ? 308  LYS A CG  1 
ATOM   2099 C CD  . LYS A 1 282 ? -41.960  -8.835  -3.161  1.00 68.40  ? 308  LYS A CD  1 
ATOM   2100 C CE  . LYS A 1 282 ? -40.459  -8.622  -3.095  1.00 87.74  ? 308  LYS A CE  1 
ATOM   2101 N NZ  . LYS A 1 282 ? -39.873  -8.695  -4.456  1.00 89.90  ? 308  LYS A NZ  1 
ATOM   2102 N N   . ASN A 1 283 ? -47.032  -8.645  -2.397  1.00 44.54  ? 309  ASN A N   1 
ATOM   2103 C CA  . ASN A 1 283 ? -48.113  -8.580  -3.326  1.00 46.34  ? 309  ASN A CA  1 
ATOM   2104 C C   . ASN A 1 283 ? -49.426  -8.727  -2.721  1.00 44.02  ? 309  ASN A C   1 
ATOM   2105 O O   . ASN A 1 283 ? -50.320  -9.237  -3.369  1.00 46.38  ? 309  ASN A O   1 
ATOM   2106 C CB  . ASN A 1 283 ? -47.910  -9.701  -4.336  1.00 49.38  ? 309  ASN A CB  1 
ATOM   2107 C CG  . ASN A 1 283 ? -46.520  -9.649  -4.958  1.00 56.28  ? 309  ASN A CG  1 
ATOM   2108 O OD1 . ASN A 1 283 ? -45.836  -8.631  -4.886  1.00 57.83  ? 309  ASN A OD1 1 
ATOM   2109 N ND2 . ASN A 1 283 ? -46.086  -10.749 -5.516  1.00 57.65  ? 309  ASN A ND2 1 
ATOM   2110 N N   . MET A 1 284 ? -49.600  -8.155  -1.541  1.00 49.45  ? 310  MET A N   1 
ATOM   2111 C CA  . MET A 1 284 ? -50.856  -8.278  -0.831  1.00 55.59  ? 310  MET A CA  1 
ATOM   2112 C C   . MET A 1 284 ? -51.269  -6.890  -0.312  1.00 62.49  ? 310  MET A C   1 
ATOM   2113 O O   . MET A 1 284 ? -51.381  -6.669  0.880   1.00 60.62  ? 310  MET A O   1 
ATOM   2114 C CB  . MET A 1 284 ? -50.604  -9.265  0.294   1.00 64.35  ? 310  MET A CB  1 
ATOM   2115 C CG  . MET A 1 284 ? -51.825  -9.761  1.039   1.00 68.70  ? 310  MET A CG  1 
ATOM   2116 S SD  . MET A 1 284 ? -51.343  -10.888 2.366   1.00 61.18  ? 310  MET A SD  1 
ATOM   2117 C CE  . MET A 1 284 ? -50.557  -12.221 1.475   1.00 57.86  ? 310  MET A CE  1 
ATOM   2118 N N   . PRO A 1 285 ? -51.561  -5.958  -1.236  1.00 59.17  ? 311  PRO A N   1 
ATOM   2119 C CA  . PRO A 1 285 ? -51.922  -4.590  -0.896  1.00 45.13  ? 311  PRO A CA  1 
ATOM   2120 C C   . PRO A 1 285 ? -53.252  -4.363  -0.222  1.00 45.78  ? 311  PRO A C   1 
ATOM   2121 O O   . PRO A 1 285 ? -53.437  -3.303  0.378   1.00 44.60  ? 311  PRO A O   1 
ATOM   2122 C CB  . PRO A 1 285 ? -51.951  -3.906  -2.244  1.00 51.29  ? 311  PRO A CB  1 
ATOM   2123 C CG  . PRO A 1 285 ? -52.388  -4.988  -3.177  1.00 57.70  ? 311  PRO A CG  1 
ATOM   2124 C CD  . PRO A 1 285 ? -51.731  -6.229  -2.678  1.00 57.15  ? 311  PRO A CD  1 
ATOM   2125 N N   . HIS A 1 286 ? -54.157  -5.327  -0.260  1.00 45.18  ? 312  HIS A N   1 
ATOM   2126 C CA  . HIS A 1 286 ? -55.472  -5.138  0.361   1.00 45.71  ? 312  HIS A CA  1 
ATOM   2127 C C   . HIS A 1 286 ? -55.670  -5.715  1.772   1.00 44.08  ? 312  HIS A C   1 
ATOM   2128 O O   . HIS A 1 286 ? -56.758  -5.563  2.372   1.00 40.43  ? 312  HIS A O   1 
ATOM   2129 C CB  . HIS A 1 286 ? -56.533  -5.728  -0.548  1.00 51.48  ? 312  HIS A CB  1 
ATOM   2130 C CG  . HIS A 1 286 ? -56.496  -5.175  -1.949  1.00 66.16  ? 312  HIS A CG  1 
ATOM   2131 N ND1 . HIS A 1 286 ? -57.147  -4.019  -2.314  1.00 59.21  ? 312  HIS A ND1 1 
ATOM   2132 C CD2 . HIS A 1 286 ? -55.897  -5.640  -3.073  1.00 60.65  ? 312  HIS A CD2 1 
ATOM   2133 C CE1 . HIS A 1 286 ? -56.919  -3.777  -3.590  1.00 59.37  ? 312  HIS A CE1 1 
ATOM   2134 N NE2 . HIS A 1 286 ? -56.182  -4.757  -4.078  1.00 54.43  ? 312  HIS A NE2 1 
ATOM   2135 N N   . LEU A 1 287 ? -54.617  -6.245  2.363   1.00 42.21  ? 313  LEU A N   1 
ATOM   2136 C CA  . LEU A 1 287 ? -54.754  -6.861  3.685   1.00 46.63  ? 313  LEU A CA  1 
ATOM   2137 C C   . LEU A 1 287 ? -55.265  -5.905  4.738   1.00 39.81  ? 313  LEU A C   1 
ATOM   2138 O O   . LEU A 1 287 ? -54.567  -4.991  5.121   1.00 51.24  ? 313  LEU A O   1 
ATOM   2139 C CB  . LEU A 1 287 ? -53.431  -7.486  4.156   1.00 48.93  ? 313  LEU A CB  1 
ATOM   2140 C CG  . LEU A 1 287 ? -53.600  -8.455  5.350   1.00 47.80  ? 313  LEU A CG  1 
ATOM   2141 C CD1 . LEU A 1 287 ? -54.420  -9.649  4.919   1.00 49.23  ? 313  LEU A CD1 1 
ATOM   2142 C CD2 . LEU A 1 287 ? -52.278  -8.977  5.846   1.00 45.75  ? 313  LEU A CD2 1 
ATOM   2143 N N   . LYS A 1 288 ? -56.499  -6.128  5.184   1.00 47.04  ? 314  LYS A N   1 
ATOM   2144 C CA  . LYS A 1 288 ? -57.153  -5.325  6.224   1.00 47.78  ? 314  LYS A CA  1 
ATOM   2145 C C   . LYS A 1 288 ? -56.993  -5.848  7.659   1.00 47.60  ? 314  LYS A C   1 
ATOM   2146 O O   . LYS A 1 288 ? -57.102  -5.062  8.596   1.00 46.16  ? 314  LYS A O   1 
ATOM   2147 C CB  . LYS A 1 288 ? -58.695  -5.244  6.038   1.00 52.84  ? 314  LYS A CB  1 
ATOM   2148 C CG  . LYS A 1 288 ? -59.248  -4.404  4.907   1.00 68.89  ? 314  LYS A CG  1 
ATOM   2149 C CD  . LYS A 1 288 ? -60.711  -4.002  5.183   1.00 88.26  ? 314  LYS A CD  1 
ATOM   2150 C CE  . LYS A 1 288 ? -61.757  -5.099  5.065   1.00 97.29  ? 314  LYS A CE  1 
ATOM   2151 N NZ  . LYS A 1 288 ? -62.001  -5.437  3.633   1.00 108.87 ? 314  LYS A NZ  1 
ATOM   2152 N N   . VAL A 1 289 ? -56.951  -7.177  7.827   1.00 46.77  ? 315  VAL A N   1 
ATOM   2153 C CA  . VAL A 1 289 ? -56.881  -7.824  9.171   1.00 42.07  ? 315  VAL A CA  1 
ATOM   2154 C C   . VAL A 1 289 ? -55.810  -8.858  9.317   1.00 40.63  ? 315  VAL A C   1 
ATOM   2155 O O   . VAL A 1 289 ? -55.786  -9.827  8.574   1.00 43.02  ? 315  VAL A O   1 
ATOM   2156 C CB  . VAL A 1 289 ? -58.188  -8.554  9.463   1.00 43.10  ? 315  VAL A CB  1 
ATOM   2157 C CG1 . VAL A 1 289 ? -58.144  -9.212  10.817  1.00 47.28  ? 315  VAL A CG1 1 
ATOM   2158 C CG2 . VAL A 1 289 ? -59.366  -7.595  9.419   1.00 37.89  ? 315  VAL A CG2 1 
ATOM   2159 N N   . LEU A 1 290 ? -54.950  -8.702  10.312  1.00 38.39  ? 316  LEU A N   1 
ATOM   2160 C CA  . LEU A 1 290 ? -53.878  -9.671  10.493  1.00 45.01  ? 316  LEU A CA  1 
ATOM   2161 C C   . LEU A 1 290 ? -53.787  -10.161 11.956  1.00 48.63  ? 316  LEU A C   1 
ATOM   2162 O O   . LEU A 1 290 ? -53.471  -9.397  12.855  1.00 50.50  ? 316  LEU A O   1 
ATOM   2163 C CB  . LEU A 1 290 ? -52.572  -9.078  10.044  1.00 39.56  ? 316  LEU A CB  1 
ATOM   2164 C CG  . LEU A 1 290 ? -51.347  -9.929  10.287  1.00 45.33  ? 316  LEU A CG  1 
ATOM   2165 C CD1 . LEU A 1 290 ? -51.393  -11.222 9.512   1.00 52.65  ? 316  LEU A CD1 1 
ATOM   2166 C CD2 . LEU A 1 290 ? -50.111  -9.151  9.934   1.00 44.51  ? 316  LEU A CD2 1 
ATOM   2167 N N   . ASP A 1 291 ? -54.076  -11.448 12.151  1.00 52.64  ? 317  ASP A N   1 
ATOM   2168 C CA  . ASP A 1 291 ? -54.074  -12.120 13.467  1.00 45.56  ? 317  ASP A CA  1 
ATOM   2169 C C   . ASP A 1 291 ? -52.788  -12.898 13.689  1.00 47.14  ? 317  ASP A C   1 
ATOM   2170 O O   . ASP A 1 291 ? -52.507  -13.848 12.970  1.00 44.53  ? 317  ASP A O   1 
ATOM   2171 C CB  . ASP A 1 291 ? -55.267  -13.058 13.565  1.00 49.81  ? 317  ASP A CB  1 
ATOM   2172 C CG  . ASP A 1 291 ? -56.598  -12.327 13.820  1.00 62.33  ? 317  ASP A CG  1 
ATOM   2173 O OD1 . ASP A 1 291 ? -57.613  -12.565 13.100  1.00 85.95  ? 317  ASP A OD1 1 
ATOM   2174 O OD2 . ASP A 1 291 ? -56.630  -11.483 14.723  1.00 98.98  ? 317  ASP A OD2 1 
ATOM   2175 N N   . LEU A 1 292 ? -51.993  -12.450 14.656  1.00 40.34  ? 318  LEU A N   1 
ATOM   2176 C CA  . LEU A 1 292 ? -50.729  -13.084 15.001  1.00 48.22  ? 318  LEU A CA  1 
ATOM   2177 C C   . LEU A 1 292 ? -50.628  -13.359 16.538  1.00 46.26  ? 318  LEU A C   1 
ATOM   2178 O O   . LEU A 1 292 ? -49.552  -13.372 17.110  1.00 52.26  ? 318  LEU A O   1 
ATOM   2179 C CB  . LEU A 1 292 ? -49.578  -12.195 14.558  1.00 48.78  ? 318  LEU A CB  1 
ATOM   2180 C CG  . LEU A 1 292 ? -49.400  -12.038 13.065  1.00 49.23  ? 318  LEU A CG  1 
ATOM   2181 C CD1 . LEU A 1 292 ? -48.481  -10.866 12.783  1.00 51.92  ? 318  LEU A CD1 1 
ATOM   2182 C CD2 . LEU A 1 292 ? -48.853  -13.316 12.481  1.00 54.45  ? 318  LEU A CD2 1 
ATOM   2183 N N   . GLU A 1 293 ? -51.765  -13.614 17.154  1.00 44.13  ? 319  GLU A N   1 
ATOM   2184 C CA  . GLU A 1 293 ? -51.891  -13.917 18.584  1.00 51.52  ? 319  GLU A CA  1 
ATOM   2185 C C   . GLU A 1 293 ? -51.283  -15.315 18.860  1.00 56.39  ? 319  GLU A C   1 
ATOM   2186 O O   . GLU A 1 293 ? -51.309  -16.192 17.998  1.00 60.20  ? 319  GLU A O   1 
ATOM   2187 C CB  . GLU A 1 293 ? -53.380  -14.087 18.848  1.00 55.73  ? 319  GLU A CB  1 
ATOM   2188 C CG  . GLU A 1 293 ? -54.188  -13.065 18.061  1.00 83.40  ? 319  GLU A CG  1 
ATOM   2189 C CD  . GLU A 1 293 ? -55.571  -13.559 17.691  1.00 92.92  ? 319  GLU A CD  1 
ATOM   2190 O OE1 . GLU A 1 293 ? -55.974  -13.380 16.501  1.00 66.78  ? 319  GLU A OE1 1 
ATOM   2191 O OE2 . GLU A 1 293 ? -56.151  -14.296 18.510  1.00 109.78 ? 319  GLU A OE2 1 
ATOM   2192 N N   . PHE A 1 294 ? -50.781  -15.532 20.066  1.00 55.50  ? 320  PHE A N   1 
ATOM   2193 C CA  . PHE A 1 294 ? -50.258  -16.851 20.475  1.00 48.58  ? 320  PHE A CA  1 
ATOM   2194 C C   . PHE A 1 294 ? -49.112  -17.371 19.629  1.00 48.33  ? 320  PHE A C   1 
ATOM   2195 O O   . PHE A 1 294 ? -49.136  -18.492 19.141  1.00 48.39  ? 320  PHE A O   1 
ATOM   2196 C CB  . PHE A 1 294 ? -51.398  -17.882 20.510  1.00 39.66  ? 320  PHE A CB  1 
ATOM   2197 C CG  . PHE A 1 294 ? -52.629  -17.392 21.245  1.00 40.82  ? 320  PHE A CG  1 
ATOM   2198 C CD1 . PHE A 1 294 ? -52.633  -17.272 22.624  1.00 53.08  ? 320  PHE A CD1 1 
ATOM   2199 C CD2 . PHE A 1 294 ? -53.816  -17.225 20.586  1.00 41.14  ? 320  PHE A CD2 1 
ATOM   2200 C CE1 . PHE A 1 294 ? -53.755  -16.828 23.293  1.00 48.63  ? 320  PHE A CE1 1 
ATOM   2201 C CE2 . PHE A 1 294 ? -54.952  -16.773 21.248  1.00 43.01  ? 320  PHE A CE2 1 
ATOM   2202 C CZ  . PHE A 1 294 ? -54.916  -16.574 22.597  1.00 44.58  ? 320  PHE A CZ  1 
ATOM   2203 N N   . ASN A 1 295 ? -48.105  -16.533 19.499  1.00 45.82  ? 321  ASN A N   1 
ATOM   2204 C CA  . ASN A 1 295 ? -46.886  -16.828 18.764  1.00 52.12  ? 321  ASN A CA  1 
ATOM   2205 C C   . ASN A 1 295 ? -45.779  -16.321 19.668  1.00 50.47  ? 321  ASN A C   1 
ATOM   2206 O O   . ASN A 1 295 ? -46.058  -15.912 20.797  1.00 54.39  ? 321  ASN A O   1 
ATOM   2207 C CB  . ASN A 1 295 ? -46.872  -16.121 17.398  1.00 53.38  ? 321  ASN A CB  1 
ATOM   2208 C CG  . ASN A 1 295 ? -47.854  -16.741 16.417  1.00 56.34  ? 321  ASN A CG  1 
ATOM   2209 O OD1 . ASN A 1 295 ? -47.733  -17.912 16.058  1.00 56.99  ? 321  ASN A OD1 1 
ATOM   2210 N ND2 . ASN A 1 295 ? -48.738  -15.921 15.872  1.00 61.08  ? 321  ASN A ND2 1 
ATOM   2211 N N   . TYR A 1 296 ? -44.550  -16.320 19.170  1.00 52.15  ? 322  TYR A N   1 
ATOM   2212 C CA  . TYR A 1 296 ? -43.386  -15.867 19.928  1.00 60.51  ? 322  TYR A CA  1 
ATOM   2213 C C   . TYR A 1 296 ? -42.793  -14.675 19.187  1.00 62.51  ? 322  TYR A C   1 
ATOM   2214 O O   . TYR A 1 296 ? -41.606  -14.683 18.881  1.00 59.99  ? 322  TYR A O   1 
ATOM   2215 C CB  . TYR A 1 296 ? -42.356  -17.005 19.979  1.00 59.26  ? 322  TYR A CB  1 
ATOM   2216 C CG  . TYR A 1 296 ? -42.876  -18.285 20.587  1.00 59.53  ? 322  TYR A CG  1 
ATOM   2217 C CD1 . TYR A 1 296 ? -42.805  -18.508 21.951  1.00 63.85  ? 322  TYR A CD1 1 
ATOM   2218 C CD2 . TYR A 1 296 ? -43.379  -19.290 19.795  1.00 62.30  ? 322  TYR A CD2 1 
ATOM   2219 C CE1 . TYR A 1 296 ? -43.284  -19.682 22.518  1.00 61.97  ? 322  TYR A CE1 1 
ATOM   2220 C CE2 . TYR A 1 296 ? -43.856  -20.463 20.348  1.00 69.10  ? 322  TYR A CE2 1 
ATOM   2221 C CZ  . TYR A 1 296 ? -43.808  -20.655 21.718  1.00 67.53  ? 322  TYR A CZ  1 
ATOM   2222 O OH  . TYR A 1 296 ? -44.295  -21.826 22.274  1.00 52.87  ? 322  TYR A OH  1 
ATOM   2223 N N   . LEU A 1 297 ? -43.595  -13.617 18.997  1.00 59.43  ? 323  LEU A N   1 
ATOM   2224 C CA  . LEU A 1 297 ? -43.169  -12.429 18.223  1.00 54.73  ? 323  LEU A CA  1 
ATOM   2225 C C   . LEU A 1 297 ? -42.659  -11.162 18.903  1.00 56.82  ? 323  LEU A C   1 
ATOM   2226 O O   . LEU A 1 297 ? -42.635  -10.095 18.273  1.00 53.89  ? 323  LEU A O   1 
ATOM   2227 C CB  . LEU A 1 297 ? -44.319  -12.028 17.322  1.00 52.02  ? 323  LEU A CB  1 
ATOM   2228 C CG  . LEU A 1 297 ? -44.716  -13.137 16.364  1.00 49.92  ? 323  LEU A CG  1 
ATOM   2229 C CD1 . LEU A 1 297 ? -46.052  -12.837 15.711  1.00 51.69  ? 323  LEU A CD1 1 
ATOM   2230 C CD2 . LEU A 1 297 ? -43.623  -13.378 15.339  1.00 52.59  ? 323  LEU A CD2 1 
ATOM   2231 N N   . VAL A 1 298 ? -42.214  -11.247 20.144  1.00 52.60  ? 324  VAL A N   1 
ATOM   2232 C CA  . VAL A 1 298 ? -41.696  -10.054 20.816  1.00 56.11  ? 324  VAL A CA  1 
ATOM   2233 C C   . VAL A 1 298 ? -40.550  -9.411  19.994  1.00 56.28  ? 324  VAL A C   1 
ATOM   2234 O O   . VAL A 1 298 ? -40.390  -8.185  19.992  1.00 55.24  ? 324  VAL A O   1 
ATOM   2235 C CB  . VAL A 1 298 ? -41.192  -10.375 22.239  1.00 56.92  ? 324  VAL A CB  1 
ATOM   2236 C CG1 . VAL A 1 298 ? -40.484  -9.175  22.851  1.00 56.04  ? 324  VAL A CG1 1 
ATOM   2237 C CG2 . VAL A 1 298 ? -42.340  -10.815 23.119  1.00 55.78  ? 324  VAL A CG2 1 
ATOM   2238 N N   . GLY A 1 299 ? -39.746  -10.249 19.341  1.00 54.49  ? 325  GLY A N   1 
ATOM   2239 C CA  . GLY A 1 299 ? -38.618  -9.797  18.500  1.00 59.82  ? 325  GLY A CA  1 
ATOM   2240 C C   . GLY A 1 299 ? -39.118  -8.974  17.322  1.00 63.88  ? 325  GLY A C   1 
ATOM   2241 O O   . GLY A 1 299 ? -38.743  -7.796  17.148  1.00 66.10  ? 325  GLY A O   1 
ATOM   2242 N N   . GLU A 1 300 ? -39.990  -9.592  16.538  1.00 51.59  ? 326  GLU A N   1 
ATOM   2243 C CA  . GLU A 1 300 ? -40.609  -8.943  15.390  1.00 50.46  ? 326  GLU A CA  1 
ATOM   2244 C C   . GLU A 1 300 ? -41.308  -7.663  15.772  1.00 53.73  ? 326  GLU A C   1 
ATOM   2245 O O   . GLU A 1 300 ? -41.291  -6.706  15.016  1.00 64.47  ? 326  GLU A O   1 
ATOM   2246 C CB  . GLU A 1 300 ? -41.626  -9.872  14.765  1.00 51.59  ? 326  GLU A CB  1 
ATOM   2247 C CG  . GLU A 1 300 ? -41.002  -11.012 13.991  1.00 59.79  ? 326  GLU A CG  1 
ATOM   2248 C CD  . GLU A 1 300 ? -40.297  -10.502 12.761  1.00 60.73  ? 326  GLU A CD  1 
ATOM   2249 O OE1 . GLU A 1 300 ? -40.305  -9.262  12.572  1.00 66.74  ? 326  GLU A OE1 1 
ATOM   2250 O OE2 . GLU A 1 300 ? -39.783  -11.325 11.977  1.00 64.75  ? 326  GLU A OE2 1 
ATOM   2251 N N   . ILE A 1 301 ? -41.955  -7.656  16.930  1.00 49.14  ? 327  ILE A N   1 
ATOM   2252 C CA  . ILE A 1 301 ? -42.644  -6.470  17.395  1.00 47.36  ? 327  ILE A CA  1 
ATOM   2253 C C   . ILE A 1 301 ? -41.655  -5.348  17.612  1.00 52.62  ? 327  ILE A C   1 
ATOM   2254 O O   . ILE A 1 301 ? -41.974  -4.183  17.375  1.00 55.77  ? 327  ILE A O   1 
ATOM   2255 C CB  . ILE A 1 301 ? -43.394  -6.742  18.680  1.00 47.58  ? 327  ILE A CB  1 
ATOM   2256 C CG1 . ILE A 1 301 ? -44.470  -7.788  18.404  1.00 48.77  ? 327  ILE A CG1 1 
ATOM   2257 C CG2 . ILE A 1 301 ? -44.015  -5.460  19.235  1.00 46.49  ? 327  ILE A CG2 1 
ATOM   2258 C CD1 . ILE A 1 301 ? -45.242  -8.210  19.640  1.00 50.51  ? 327  ILE A CD1 1 
ATOM   2259 N N   . ALA A 1 302 ? -40.426  -5.699  17.982  1.00 53.11  ? 328  ALA A N   1 
ATOM   2260 C CA  . ALA A 1 302 ? -39.398  -4.682  18.194  1.00 53.32  ? 328  ALA A CA  1 
ATOM   2261 C C   . ALA A 1 302 ? -38.693  -4.232  16.901  1.00 58.21  ? 328  ALA A C   1 
ATOM   2262 O O   . ALA A 1 302 ? -38.333  -3.075  16.786  1.00 49.98  ? 328  ALA A O   1 
ATOM   2263 C CB  . ALA A 1 302 ? -38.376  -5.171  19.172  1.00 52.14  ? 328  ALA A CB  1 
ATOM   2264 N N   . SER A 1 303 ? -38.481  -5.143  15.953  1.00 60.76  ? 329  SER A N   1 
ATOM   2265 C CA  . SER A 1 303 ? -37.808  -4.797  14.705  1.00 69.35  ? 329  SER A CA  1 
ATOM   2266 C C   . SER A 1 303 ? -38.428  -5.516  13.521  1.00 70.91  ? 329  SER A C   1 
ATOM   2267 O O   . SER A 1 303 ? -37.737  -6.191  12.783  1.00 87.79  ? 329  SER A O   1 
ATOM   2268 C CB  . SER A 1 303 ? -36.362  -5.249  14.786  1.00 73.60  ? 329  SER A CB  1 
ATOM   2269 O OG  . SER A 1 303 ? -36.305  -6.672  14.818  1.00 74.04  ? 329  SER A OG  1 
ATOM   2270 N N   . GLY A 1 304 ? -39.712  -5.340  13.307  1.00 75.01  ? 330  GLY A N   1 
ATOM   2271 C CA  . GLY A 1 304 ? -40.386  -6.015  12.210  1.00 71.10  ? 330  GLY A CA  1 
ATOM   2272 C C   . GLY A 1 304 ? -40.530  -5.244  10.901  1.00 67.90  ? 330  GLY A C   1 
ATOM   2273 O O   . GLY A 1 304 ? -41.317  -4.281  10.758  1.00 60.29  ? 330  GLY A O   1 
ATOM   2274 N N   . ALA A 1 305 ? -39.857  -5.776  9.904   1.00 61.88  ? 331  ALA A N   1 
ATOM   2275 C CA  . ALA A 1 305 ? -39.870  -5.203  8.592   1.00 56.16  ? 331  ALA A CA  1 
ATOM   2276 C C   . ALA A 1 305 ? -41.252  -5.378  7.942   1.00 59.48  ? 331  ALA A C   1 
ATOM   2277 O O   . ALA A 1 305 ? -41.670  -4.546  7.143   1.00 59.28  ? 331  ALA A O   1 
ATOM   2278 C CB  . ALA A 1 305 ? -38.794  -5.872  7.757   1.00 47.25  ? 331  ALA A CB  1 
ATOM   2279 N N   . PHE A 1 306 ? -41.983  -6.416  8.360   1.00 58.94  ? 332  PHE A N   1 
ATOM   2280 C CA  . PHE A 1 306 ? -43.295  -6.715  7.800   1.00 52.38  ? 332  PHE A CA  1 
ATOM   2281 C C   . PHE A 1 306 ? -44.260  -5.554  8.074   1.00 51.74  ? 332  PHE A C   1 
ATOM   2282 O O   . PHE A 1 306 ? -45.288  -5.420  7.429   1.00 54.21  ? 332  PHE A O   1 
ATOM   2283 C CB  . PHE A 1 306 ? -43.861  -8.054  8.374   1.00 55.59  ? 332  PHE A CB  1 
ATOM   2284 C CG  . PHE A 1 306 ? -44.495  -7.935  9.747   1.00 46.44  ? 332  PHE A CG  1 
ATOM   2285 C CD1 . PHE A 1 306 ? -43.738  -7.967  10.887  1.00 53.50  ? 332  PHE A CD1 1 
ATOM   2286 C CD2 . PHE A 1 306 ? -45.861  -7.834  9.870   1.00 52.78  ? 332  PHE A CD2 1 
ATOM   2287 C CE1 . PHE A 1 306 ? -44.310  -7.816  12.125  1.00 50.49  ? 332  PHE A CE1 1 
ATOM   2288 C CE2 . PHE A 1 306 ? -46.450  -7.683  11.104  1.00 57.72  ? 332  PHE A CE2 1 
ATOM   2289 C CZ  . PHE A 1 306 ? -45.668  -7.668  12.236  1.00 55.24  ? 332  PHE A CZ  1 
ATOM   2290 N N   . LEU A 1 307 ? -43.933  -4.739  9.060   1.00 56.33  ? 333  LEU A N   1 
ATOM   2291 C CA  . LEU A 1 307 ? -44.771  -3.591  9.417   1.00 62.59  ? 333  LEU A CA  1 
ATOM   2292 C C   . LEU A 1 307 ? -44.775  -2.506  8.334   1.00 58.16  ? 333  LEU A C   1 
ATOM   2293 O O   . LEU A 1 307 ? -45.703  -1.717  8.222   1.00 64.05  ? 333  LEU A O   1 
ATOM   2294 C CB  . LEU A 1 307 ? -44.264  -3.005  10.742  1.00 61.40  ? 333  LEU A CB  1 
ATOM   2295 C CG  . LEU A 1 307 ? -44.477  -3.917  11.962  1.00 60.56  ? 333  LEU A CG  1 
ATOM   2296 C CD1 . LEU A 1 307 ? -43.655  -3.518  13.173  1.00 65.82  ? 333  LEU A CD1 1 
ATOM   2297 C CD2 . LEU A 1 307 ? -45.953  -4.013  12.313  1.00 59.49  ? 333  LEU A CD2 1 
ATOM   2298 N N   . THR A 1 308 ? -43.748  -2.495  7.510   1.00 57.88  ? 334  THR A N   1 
ATOM   2299 C CA  . THR A 1 308 ? -43.657  -1.488  6.465   1.00 65.54  ? 334  THR A CA  1 
ATOM   2300 C C   . THR A 1 308 ? -44.454  -1.883  5.243   1.00 55.82  ? 334  THR A C   1 
ATOM   2301 O O   . THR A 1 308 ? -44.705  -1.055  4.413   1.00 60.79  ? 334  THR A O   1 
ATOM   2302 C CB  . THR A 1 308 ? -42.188  -1.234  6.031   1.00 55.11  ? 334  THR A CB  1 
ATOM   2303 O OG1 . THR A 1 308 ? -41.625  -2.441  5.516   1.00 60.25  ? 334  THR A OG1 1 
ATOM   2304 C CG2 . THR A 1 308 ? -41.333  -0.757  7.205   1.00 55.08  ? 334  THR A CG2 1 
ATOM   2305 N N   . MET A 1 309 ? -44.966  -3.105  5.220   1.00 56.97  ? 335  MET A N   1 
ATOM   2306 C CA  . MET A 1 309 ? -45.708  -3.622  4.083   1.00 51.06  ? 335  MET A CA  1 
ATOM   2307 C C   . MET A 1 309 ? -47.190  -3.575  4.279   1.00 47.71  ? 335  MET A C   1 
ATOM   2308 O O   . MET A 1 309 ? -47.917  -4.121  3.456   1.00 56.09  ? 335  MET A O   1 
ATOM   2309 C CB  . MET A 1 309 ? -45.380  -5.116  3.926   1.00 50.02  ? 335  MET A CB  1 
ATOM   2310 C CG  . MET A 1 309 ? -43.904  -5.461  3.897   1.00 60.82  ? 335  MET A CG  1 
ATOM   2311 S SD  . MET A 1 309 ? -42.962  -4.902  2.464   1.00 62.26  ? 335  MET A SD  1 
ATOM   2312 C CE  . MET A 1 309 ? -43.676  -5.924  1.205   1.00 60.20  ? 335  MET A CE  1 
ATOM   2313 N N   . LEU A 1 310 ? -47.672  -2.891  5.308   1.00 52.81  ? 336  LEU A N   1 
ATOM   2314 C CA  . LEU A 1 310 ? -49.130  -2.902  5.592   1.00 46.21  ? 336  LEU A CA  1 
ATOM   2315 C C   . LEU A 1 310 ? -49.835  -1.567  5.868   1.00 47.61  ? 336  LEU A C   1 
ATOM   2316 O O   . LEU A 1 310 ? -50.646  -1.455  6.783   1.00 46.18  ? 336  LEU A O   1 
ATOM   2317 C CB  . LEU A 1 310 ? -49.303  -3.806  6.797   1.00 52.53  ? 336  LEU A CB  1 
ATOM   2318 C CG  . LEU A 1 310 ? -48.745  -5.229  6.596   1.00 53.13  ? 336  LEU A CG  1 
ATOM   2319 C CD1 . LEU A 1 310 ? -48.602  -6.006  7.902   1.00 52.80  ? 336  LEU A CD1 1 
ATOM   2320 C CD2 . LEU A 1 310 ? -49.614  -5.977  5.608   1.00 51.28  ? 336  LEU A CD2 1 
ATOM   2321 N N   . PRO A 1 311 ? -49.624  -0.577  5.002   1.00 55.23  ? 337  PRO A N   1 
ATOM   2322 C CA  . PRO A 1 311 ? -50.225  0.767   5.123   1.00 44.56  ? 337  PRO A CA  1 
ATOM   2323 C C   . PRO A 1 311 ? -51.745  0.764   5.066   1.00 40.85  ? 337  PRO A C   1 
ATOM   2324 O O   . PRO A 1 311 ? -52.413  1.724   5.501   1.00 43.15  ? 337  PRO A O   1 
ATOM   2325 C CB  . PRO A 1 311 ? -49.683  1.458   3.902   1.00 45.15  ? 337  PRO A CB  1 
ATOM   2326 C CG  . PRO A 1 311 ? -49.603  0.352   2.924   1.00 46.93  ? 337  PRO A CG  1 
ATOM   2327 C CD  . PRO A 1 311 ? -48.999  -0.758  3.687   1.00 45.78  ? 337  PRO A CD  1 
ATOM   2328 N N   . ARG A 1 312 ? -52.304  -0.330  4.608   1.00 41.94  ? 338  ARG A N   1 
ATOM   2329 C CA  . ARG A 1 312 ? -53.732  -0.419  4.509   1.00 46.06  ? 338  ARG A CA  1 
ATOM   2330 C C   . ARG A 1 312 ? -54.351  -1.334  5.640   1.00 47.31  ? 338  ARG A C   1 
ATOM   2331 O O   . ARG A 1 312 ? -55.565  -1.501  5.716   1.00 40.87  ? 338  ARG A O   1 
ATOM   2332 C CB  . ARG A 1 312 ? -54.031  -0.979  3.117   1.00 51.72  ? 338  ARG A CB  1 
ATOM   2333 C CG  . ARG A 1 312 ? -55.351  -0.536  2.519   1.00 63.65  ? 338  ARG A CG  1 
ATOM   2334 C CD  . ARG A 1 312 ? -56.493  -0.925  3.404   1.00 74.35  ? 338  ARG A CD  1 
ATOM   2335 N NE  . ARG A 1 312 ? -57.772  -0.364  3.019   1.00 72.05  ? 338  ARG A NE  1 
ATOM   2336 C CZ  . ARG A 1 312 ? -58.850  -0.543  3.759   1.00 81.97  ? 338  ARG A CZ  1 
ATOM   2337 N NH1 . ARG A 1 312 ? -58.726  -1.200  4.892   1.00 85.24  ? 338  ARG A NH1 1 
ATOM   2338 N NH2 . ARG A 1 312 ? -60.027  -0.031  3.423   1.00 103.75 ? 338  ARG A NH2 1 
ATOM   2339 N N   . LEU A 1 313 ? -53.538  -1.868  6.552   1.00 46.82  ? 339  LEU A N   1 
ATOM   2340 C CA  . LEU A 1 313 ? -54.069  -2.744  7.623   1.00 38.55  ? 339  LEU A CA  1 
ATOM   2341 C C   . LEU A 1 313 ? -54.942  -1.983  8.653   1.00 37.43  ? 339  LEU A C   1 
ATOM   2342 O O   . LEU A 1 313 ? -54.608  -0.903  9.087   1.00 44.64  ? 339  LEU A O   1 
ATOM   2343 C CB  . LEU A 1 313 ? -52.909  -3.369  8.363   1.00 43.58  ? 339  LEU A CB  1 
ATOM   2344 C CG  . LEU A 1 313 ? -53.189  -4.576  9.273   1.00 52.26  ? 339  LEU A CG  1 
ATOM   2345 C CD1 . LEU A 1 313 ? -53.522  -5.769  8.385   1.00 45.62  ? 339  LEU A CD1 1 
ATOM   2346 C CD2 . LEU A 1 313 ? -51.982  -4.921  10.136  1.00 42.78  ? 339  LEU A CD2 1 
ATOM   2347 N N   . GLU A 1 314 ? -56.090  -2.529  8.989   1.00 39.58  ? 340  GLU A N   1 
ATOM   2348 C CA  . GLU A 1 314 ? -56.961  -1.922  9.963   1.00 45.20  ? 340  GLU A CA  1 
ATOM   2349 C C   . GLU A 1 314 ? -56.910  -2.578  11.342  1.00 46.95  ? 340  GLU A C   1 
ATOM   2350 O O   . GLU A 1 314 ? -57.018  -1.895  12.340  1.00 49.06  ? 340  GLU A O   1 
ATOM   2351 C CB  . GLU A 1 314 ? -58.385  -1.959  9.499   1.00 49.84  ? 340  GLU A CB  1 
ATOM   2352 C CG  . GLU A 1 314 ? -58.633  -1.139  8.265   1.00 55.25  ? 340  GLU A CG  1 
ATOM   2353 C CD  . GLU A 1 314 ? -60.079  -1.181  7.822   1.00 53.07  ? 340  GLU A CD  1 
ATOM   2354 O OE1 . GLU A 1 314 ? -60.943  -1.646  8.581   1.00 67.40  ? 340  GLU A OE1 1 
ATOM   2355 O OE2 . GLU A 1 314 ? -60.358  -0.700  6.716   1.00 65.73  ? 340  GLU A OE2 1 
ATOM   2356 N N   . ILE A 1 315 ? -56.715  -3.890  11.393  1.00 47.63  ? 341  ILE A N   1 
ATOM   2357 C CA  . ILE A 1 315 ? -56.686  -4.603  12.660  1.00 40.34  ? 341  ILE A CA  1 
ATOM   2358 C C   . ILE A 1 315 ? -55.510  -5.497  12.767  1.00 39.40  ? 341  ILE A C   1 
ATOM   2359 O O   . ILE A 1 315 ? -55.299  -6.339  11.899  1.00 40.37  ? 341  ILE A O   1 
ATOM   2360 C CB  . ILE A 1 315 ? -57.928  -5.461  12.794  1.00 43.83  ? 341  ILE A CB  1 
ATOM   2361 C CG1 . ILE A 1 315 ? -59.148  -4.560  12.764  1.00 37.78  ? 341  ILE A CG1 1 
ATOM   2362 C CG2 . ILE A 1 315 ? -57.919  -6.193  14.118  1.00 42.72  ? 341  ILE A CG2 1 
ATOM   2363 C CD1 . ILE A 1 315 ? -60.425  -5.311  12.892  1.00 40.80  ? 341  ILE A CD1 1 
ATOM   2364 N N   . LEU A 1 316 ? -54.693  -5.260  13.788  1.00 35.34  ? 342  LEU A N   1 
ATOM   2365 C CA  . LEU A 1 316 ? -53.493  -6.074  14.019  1.00 38.74  ? 342  LEU A CA  1 
ATOM   2366 C C   . LEU A 1 316 ? -53.583  -6.633  15.431  1.00 47.96  ? 342  LEU A C   1 
ATOM   2367 O O   . LEU A 1 316 ? -53.749  -5.857  16.413  1.00 41.98  ? 342  LEU A O   1 
ATOM   2368 C CB  . LEU A 1 316 ? -52.231  -5.246  13.907  1.00 39.04  ? 342  LEU A CB  1 
ATOM   2369 C CG  . LEU A 1 316 ? -50.910  -5.973  14.160  1.00 40.94  ? 342  LEU A CG  1 
ATOM   2370 C CD1 . LEU A 1 316 ? -50.717  -7.120  13.217  1.00 40.10  ? 342  LEU A CD1 1 
ATOM   2371 C CD2 . LEU A 1 316 ? -49.751  -5.022  14.005  1.00 49.05  ? 342  LEU A CD2 1 
ATOM   2372 N N   . ASP A 1 317 ? -53.589  -7.969  15.528  1.00 46.13  ? 343  ASP A N   1 
ATOM   2373 C CA  . ASP A 1 317 ? -53.683  -8.632  16.836  1.00 47.71  ? 343  ASP A CA  1 
ATOM   2374 C C   . ASP A 1 317 ? -52.380  -9.306  17.134  1.00 43.08  ? 343  ASP A C   1 
ATOM   2375 O O   . ASP A 1 317 ? -51.958  -10.202 16.411  1.00 40.98  ? 343  ASP A O   1 
ATOM   2376 C CB  . ASP A 1 317 ? -54.820  -9.630  16.873  1.00 42.64  ? 343  ASP A CB  1 
ATOM   2377 C CG  . ASP A 1 317 ? -55.159  -10.090 18.289  1.00 53.81  ? 343  ASP A CG  1 
ATOM   2378 O OD1 . ASP A 1 317 ? -54.297  -10.034 19.224  1.00 51.46  ? 343  ASP A OD1 1 
ATOM   2379 O OD2 . ASP A 1 317 ? -56.300  -10.564 18.451  1.00 54.84  ? 343  ASP A OD2 1 
ATOM   2380 N N   . LEU A 1 318 ? -51.700  -8.802  18.149  1.00 40.02  ? 344  LEU A N   1 
ATOM   2381 C CA  . LEU A 1 318 ? -50.426  -9.362  18.552  1.00 47.81  ? 344  LEU A CA  1 
ATOM   2382 C C   . LEU A 1 318 ? -50.465  -9.886  20.011  1.00 45.74  ? 344  LEU A C   1 
ATOM   2383 O O   . LEU A 1 318 ? -49.436  -10.045 20.649  1.00 46.17  ? 344  LEU A O   1 
ATOM   2384 C CB  . LEU A 1 318 ? -49.366  -8.286  18.397  1.00 46.52  ? 344  LEU A CB  1 
ATOM   2385 C CG  . LEU A 1 318 ? -48.921  -7.971  16.978  1.00 48.31  ? 344  LEU A CG  1 
ATOM   2386 C CD1 . LEU A 1 318 ? -48.203  -6.635  16.922  1.00 51.28  ? 344  LEU A CD1 1 
ATOM   2387 C CD2 . LEU A 1 318 ? -48.042  -9.072  16.438  1.00 48.27  ? 344  LEU A CD2 1 
ATOM   2388 N N   . SER A 1 319 ? -51.659  -10.165 20.506  1.00 39.53  ? 345  SER A N   1 
ATOM   2389 C CA  . SER A 1 319 ? -51.824  -10.622 21.860  1.00 44.07  ? 345  SER A CA  1 
ATOM   2390 C C   . SER A 1 319 ? -51.163  -11.942 22.187  1.00 43.80  ? 345  SER A C   1 
ATOM   2391 O O   . SER A 1 319 ? -50.957  -12.798 21.341  1.00 49.48  ? 345  SER A O   1 
ATOM   2392 C CB  . SER A 1 319 ? -53.295  -10.734 22.171  1.00 45.06  ? 345  SER A CB  1 
ATOM   2393 O OG  . SER A 1 319 ? -53.914  -9.465  22.058  1.00 45.36  ? 345  SER A OG  1 
ATOM   2394 N N   . PHE A 1 320 ? -50.775  -12.062 23.434  1.00 48.93  ? 346  PHE A N   1 
ATOM   2395 C CA  . PHE A 1 320 ? -50.142  -13.265 23.953  1.00 42.81  ? 346  PHE A CA  1 
ATOM   2396 C C   . PHE A 1 320 ? -48.971  -13.768 23.177  1.00 45.49  ? 346  PHE A C   1 
ATOM   2397 O O   . PHE A 1 320 ? -49.027  -14.864 22.602  1.00 43.13  ? 346  PHE A O   1 
ATOM   2398 C CB  . PHE A 1 320 ? -51.170  -14.367 24.161  1.00 36.88  ? 346  PHE A CB  1 
ATOM   2399 C CG  . PHE A 1 320 ? -52.259  -13.964 25.110  1.00 41.91  ? 346  PHE A CG  1 
ATOM   2400 C CD1 . PHE A 1 320 ? -52.003  -13.865 26.460  1.00 44.98  ? 346  PHE A CD1 1 
ATOM   2401 C CD2 . PHE A 1 320 ? -53.516  -13.671 24.656  1.00 42.93  ? 346  PHE A CD2 1 
ATOM   2402 C CE1 . PHE A 1 320 ? -52.975  -13.467 27.325  1.00 46.92  ? 346  PHE A CE1 1 
ATOM   2403 C CE2 . PHE A 1 320 ? -54.497  -13.256 25.512  1.00 43.33  ? 346  PHE A CE2 1 
ATOM   2404 C CZ  . PHE A 1 320 ? -54.219  -13.130 26.849  1.00 51.15  ? 346  PHE A CZ  1 
ATOM   2405 N N   . ASN A 1 321 ? -47.963  -12.907 23.063  1.00 43.29  ? 347  ASN A N   1 
ATOM   2406 C CA  . ASN A 1 321 ? -46.704  -13.257 22.432  1.00 45.35  ? 347  ASN A CA  1 
ATOM   2407 C C   . ASN A 1 321 ? -45.613  -13.150 23.485  1.00 43.38  ? 347  ASN A C   1 
ATOM   2408 O O   . ASN A 1 321 ? -44.434  -13.070 23.165  1.00 48.89  ? 347  ASN A O   1 
ATOM   2409 C CB  . ASN A 1 321 ? -46.335  -12.374 21.218  1.00 43.20  ? 347  ASN A CB  1 
ATOM   2410 C CG  . ASN A 1 321 ? -47.028  -12.800 19.946  1.00 45.64  ? 347  ASN A CG  1 
ATOM   2411 O OD1 . ASN A 1 321 ? -46.412  -13.471 19.101  1.00 40.28  ? 347  ASN A OD1 1 
ATOM   2412 N ND2 . ASN A 1 321 ? -48.337  -12.638 19.907  1.00 48.52  ? 347  ASN A ND2 1 
ATOM   2413 N N   . TYR A 1 322 ? -45.980  -13.227 24.747  1.00 48.70  ? 348  TYR A N   1 
ATOM   2414 C CA  . TYR A 1 322 ? -44.965  -13.081 25.803  1.00 47.48  ? 348  TYR A CA  1 
ATOM   2415 C C   . TYR A 1 322 ? -43.956  -14.178 25.834  1.00 44.56  ? 348  TYR A C   1 
ATOM   2416 O O   . TYR A 1 322 ? -44.195  -15.262 25.337  1.00 53.88  ? 348  TYR A O   1 
ATOM   2417 C CB  . TYR A 1 322 ? -45.610  -13.032 27.180  1.00 44.49  ? 348  TYR A CB  1 
ATOM   2418 C CG  . TYR A 1 322 ? -46.293  -14.314 27.584  1.00 55.63  ? 348  TYR A CG  1 
ATOM   2419 C CD1 . TYR A 1 322 ? -47.646  -14.511 27.339  1.00 56.64  ? 348  TYR A CD1 1 
ATOM   2420 C CD2 . TYR A 1 322 ? -45.596  -15.313 28.289  1.00 67.54  ? 348  TYR A CD2 1 
ATOM   2421 C CE1 . TYR A 1 322 ? -48.287  -15.670 27.736  1.00 69.17  ? 348  TYR A CE1 1 
ATOM   2422 C CE2 . TYR A 1 322 ? -46.241  -16.469 28.723  1.00 64.68  ? 348  TYR A CE2 1 
ATOM   2423 C CZ  . TYR A 1 322 ? -47.578  -16.650 28.427  1.00 72.52  ? 348  TYR A CZ  1 
ATOM   2424 O OH  . TYR A 1 322 ? -48.219  -17.804 28.799  1.00 73.66  ? 348  TYR A OH  1 
ATOM   2425 N N   . ILE A 1 323 ? -42.778  -13.839 26.325  1.00 53.85  ? 349  ILE A N   1 
ATOM   2426 C CA  . ILE A 1 323 ? -41.707  -14.811 26.526  1.00 69.08  ? 349  ILE A CA  1 
ATOM   2427 C C   . ILE A 1 323 ? -41.861  -15.306 27.989  1.00 59.92  ? 349  ILE A C   1 
ATOM   2428 O O   . ILE A 1 323 ? -41.775  -14.517 28.906  1.00 54.42  ? 349  ILE A O   1 
ATOM   2429 C CB  . ILE A 1 323 ? -40.350  -14.151 26.409  1.00 69.62  ? 349  ILE A CB  1 
ATOM   2430 C CG1 . ILE A 1 323 ? -40.203  -13.558 25.007  1.00 65.77  ? 349  ILE A CG1 1 
ATOM   2431 C CG2 . ILE A 1 323 ? -39.274  -15.173 26.720  1.00 64.58  ? 349  ILE A CG2 1 
ATOM   2432 C CD1 . ILE A 1 323 ? -38.988  -12.671 24.836  1.00 60.15  ? 349  ILE A CD1 1 
ATOM   2433 N N   . LYS A 1 324 ? -42.085  -16.598 28.180  1.00 63.95  ? 350  LYS A N   1 
ATOM   2434 C CA  . LYS A 1 324 ? -42.284  -17.189 29.531  1.00 77.98  ? 350  LYS A CA  1 
ATOM   2435 C C   . LYS A 1 324 ? -41.231  -16.726 30.491  1.00 60.89  ? 350  LYS A C   1 
ATOM   2436 O O   . LYS A 1 324 ? -40.040  -16.754 30.199  1.00 59.49  ? 350  LYS A O   1 
ATOM   2437 C CB  . LYS A 1 324 ? -42.201  -18.722 29.516  1.00 83.75  ? 350  LYS A CB  1 
ATOM   2438 C CG  . LYS A 1 324 ? -42.638  -19.284 28.193  1.00 109.87 ? 350  LYS A CG  1 
ATOM   2439 C CD  . LYS A 1 324 ? -41.496  -19.048 27.200  1.00 120.15 ? 350  LYS A CD  1 
ATOM   2440 C CE  . LYS A 1 324 ? -41.906  -19.021 25.739  1.00 111.57 ? 350  LYS A CE  1 
ATOM   2441 N NZ  . LYS A 1 324 ? -40.703  -18.777 24.888  1.00 104.11 ? 350  LYS A NZ  1 
ATOM   2442 N N   . GLY A 1 325 ? -41.679  -16.244 31.623  1.00 58.20  ? 351  GLY A N   1 
ATOM   2443 C CA  . GLY A 1 325 ? -40.768  -15.811 32.653  1.00 61.86  ? 351  GLY A CA  1 
ATOM   2444 C C   . GLY A 1 325 ? -40.103  -14.489 32.440  1.00 64.91  ? 351  GLY A C   1 
ATOM   2445 O O   . GLY A 1 325 ? -39.408  -14.014 33.330  1.00 73.30  ? 351  GLY A O   1 
ATOM   2446 N N   . SER A 1 326 ? -40.357  -13.845 31.306  1.00 67.85  ? 352  SER A N   1 
ATOM   2447 C CA  . SER A 1 326 ? -39.747  -12.545 31.054  1.00 61.02  ? 352  SER A CA  1 
ATOM   2448 C C   . SER A 1 326 ? -40.699  -11.437 31.474  1.00 61.36  ? 352  SER A C   1 
ATOM   2449 O O   . SER A 1 326 ? -41.903  -11.552 31.269  1.00 69.28  ? 352  SER A O   1 
ATOM   2450 C CB  . SER A 1 326 ? -39.382  -12.393 29.599  1.00 64.34  ? 352  SER A CB  1 
ATOM   2451 O OG  . SER A 1 326 ? -38.646  -11.196 29.419  1.00 76.44  ? 352  SER A OG  1 
ATOM   2452 N N   . TYR A 1 327 ? -40.171  -10.399 32.121  1.00 59.15  ? 353  TYR A N   1 
ATOM   2453 C CA  . TYR A 1 327 ? -41.000  -9.281  32.567  1.00 54.30  ? 353  TYR A CA  1 
ATOM   2454 C C   . TYR A 1 327 ? -40.241  -7.971  32.394  1.00 49.18  ? 353  TYR A C   1 
ATOM   2455 O O   . TYR A 1 327 ? -39.945  -7.258  33.349  1.00 51.60  ? 353  TYR A O   1 
ATOM   2456 C CB  . TYR A 1 327 ? -41.455  -9.544  33.990  1.00 55.18  ? 353  TYR A CB  1 
ATOM   2457 C CG  . TYR A 1 327 ? -42.406  -8.558  34.613  1.00 55.90  ? 353  TYR A CG  1 
ATOM   2458 C CD1 . TYR A 1 327 ? -43.518  -8.116  33.913  1.00 61.21  ? 353  TYR A CD1 1 
ATOM   2459 C CD2 . TYR A 1 327 ? -42.455  -8.443  35.999  1.00 52.31  ? 353  TYR A CD2 1 
ATOM   2460 C CE1 . TYR A 1 327 ? -44.492  -7.327  34.526  1.00 56.34  ? 353  TYR A CE1 1 
ATOM   2461 C CE2 . TYR A 1 327 ? -43.438  -7.696  36.628  1.00 57.23  ? 353  TYR A CE2 1 
ATOM   2462 C CZ  . TYR A 1 327 ? -44.451  -7.133  35.881  1.00 57.00  ? 353  TYR A CZ  1 
ATOM   2463 O OH  . TYR A 1 327 ? -45.452  -6.442  36.504  1.00 56.32  ? 353  TYR A OH  1 
ATOM   2464 N N   . PRO A 1 328 ? -39.936  -7.647  31.138  1.00 51.70  ? 354  PRO A N   1 
ATOM   2465 C CA  . PRO A 1 328 ? -39.199  -6.436  30.767  1.00 47.05  ? 354  PRO A CA  1 
ATOM   2466 C C   . PRO A 1 328 ? -39.769  -5.179  31.349  1.00 47.44  ? 354  PRO A C   1 
ATOM   2467 O O   . PRO A 1 328 ? -40.971  -5.101  31.645  1.00 53.61  ? 354  PRO A O   1 
ATOM   2468 C CB  . PRO A 1 328 ? -39.323  -6.401  29.230  1.00 43.88  ? 354  PRO A CB  1 
ATOM   2469 C CG  . PRO A 1 328 ? -40.455  -7.316  28.904  1.00 52.32  ? 354  PRO A CG  1 
ATOM   2470 C CD  . PRO A 1 328 ? -40.405  -8.384  29.953  1.00 50.01  ? 354  PRO A CD  1 
ATOM   2471 N N   . GLN A 1 329 ? -38.901  -4.206  31.566  1.00 54.43  ? 355  GLN A N   1 
ATOM   2472 C CA  . GLN A 1 329 ? -39.339  -2.942  32.098  1.00 54.98  ? 355  GLN A CA  1 
ATOM   2473 C C   . GLN A 1 329 ? -40.250  -2.197  31.162  1.00 54.79  ? 355  GLN A C   1 
ATOM   2474 O O   . GLN A 1 329 ? -41.181  -1.531  31.614  1.00 57.13  ? 355  GLN A O   1 
ATOM   2475 C CB  . GLN A 1 329 ? -38.176  -2.026  32.431  1.00 63.81  ? 355  GLN A CB  1 
ATOM   2476 C CG  . GLN A 1 329 ? -37.453  -2.332  33.716  1.00 86.16  ? 355  GLN A CG  1 
ATOM   2477 C CD  . GLN A 1 329 ? -36.529  -1.187  34.096  1.00 109.67 ? 355  GLN A CD  1 
ATOM   2478 O OE1 . GLN A 1 329 ? -35.976  -0.499  33.232  1.00 100.77 ? 355  GLN A OE1 1 
ATOM   2479 N NE2 . GLN A 1 329 ? -36.380  -0.961  35.390  1.00 126.84 ? 355  GLN A NE2 1 
ATOM   2480 N N   . HIS A 1 330 ? -39.963  -2.272  29.865  1.00 55.04  ? 356  HIS A N   1 
ATOM   2481 C CA  . HIS A 1 330 ? -40.766  -1.556  28.880  1.00 67.67  ? 356  HIS A CA  1 
ATOM   2482 C C   . HIS A 1 330 ? -41.184  -2.422  27.718  1.00 60.63  ? 356  HIS A C   1 
ATOM   2483 O O   . HIS A 1 330 ? -40.593  -3.463  27.455  1.00 63.39  ? 356  HIS A O   1 
ATOM   2484 C CB  . HIS A 1 330 ? -39.954  -0.378  28.296  1.00 66.97  ? 356  HIS A CB  1 
ATOM   2485 C CG  . HIS A 1 330 ? -39.414  0.548   29.325  1.00 65.60  ? 356  HIS A CG  1 
ATOM   2486 N ND1 . HIS A 1 330 ? -38.105  0.494   29.749  1.00 68.98  ? 356  HIS A ND1 1 
ATOM   2487 C CD2 . HIS A 1 330 ? -40.029  1.464   30.109  1.00 76.29  ? 356  HIS A CD2 1 
ATOM   2488 C CE1 . HIS A 1 330 ? -37.925  1.370   30.723  1.00 74.01  ? 356  HIS A CE1 1 
ATOM   2489 N NE2 . HIS A 1 330 ? -39.078  1.969   30.965  1.00 77.17  ? 356  HIS A NE2 1 
ATOM   2490 N N   . ILE A 1 331 ? -42.199  -1.966  26.999  1.00 62.60  ? 357  ILE A N   1 
ATOM   2491 C CA  . ILE A 1 331 ? -42.650  -2.681  25.810  1.00 56.74  ? 357  ILE A CA  1 
ATOM   2492 C C   . ILE A 1 331 ? -41.785  -2.091  24.691  1.00 53.95  ? 357  ILE A C   1 
ATOM   2493 O O   . ILE A 1 331 ? -41.560  -0.885  24.673  1.00 51.29  ? 357  ILE A O   1 
ATOM   2494 C CB  . ILE A 1 331 ? -44.157  -2.488  25.547  1.00 52.18  ? 357  ILE A CB  1 
ATOM   2495 C CG1 . ILE A 1 331 ? -44.558  -3.240  24.294  1.00 50.60  ? 357  ILE A CG1 1 
ATOM   2496 C CG2 . ILE A 1 331 ? -44.519  -1.020  25.400  1.00 54.44  ? 357  ILE A CG2 1 
ATOM   2497 C CD1 . ILE A 1 331 ? -46.044  -3.234  24.069  1.00 51.21  ? 357  ILE A CD1 1 
ATOM   2498 N N   . ASN A 1 332 ? -41.220  -2.940  23.835  1.00 52.23  ? 358  ASN A N   1 
ATOM   2499 C CA  . ASN A 1 332 ? -40.364  -2.468  22.750  1.00 52.37  ? 358  ASN A CA  1 
ATOM   2500 C C   . ASN A 1 332 ? -41.110  -2.512  21.406  1.00 54.12  ? 358  ASN A C   1 
ATOM   2501 O O   . ASN A 1 332 ? -41.161  -3.540  20.706  1.00 55.12  ? 358  ASN A O   1 
ATOM   2502 C CB  . ASN A 1 332 ? -39.069  -3.281  22.700  1.00 54.12  ? 358  ASN A CB  1 
ATOM   2503 C CG  . ASN A 1 332 ? -38.006  -2.614  21.873  1.00 59.59  ? 358  ASN A CG  1 
ATOM   2504 O OD1 . ASN A 1 332 ? -38.220  -1.531  21.369  1.00 63.52  ? 358  ASN A OD1 1 
ATOM   2505 N ND2 . ASN A 1 332 ? -36.829  -3.211  21.806  1.00 69.46  ? 358  ASN A ND2 1 
ATOM   2506 N N   . ILE A 1 333 ? -41.692  -1.371  21.074  1.00 47.99  ? 359  ILE A N   1 
ATOM   2507 C CA  . ILE A 1 333 ? -42.496  -1.179  19.855  1.00 50.75  ? 359  ILE A CA  1 
ATOM   2508 C C   . ILE A 1 333 ? -41.685  -0.535  18.733  1.00 49.21  ? 359  ILE A C   1 
ATOM   2509 O O   . ILE A 1 333 ? -41.269  0.631   18.839  1.00 51.29  ? 359  ILE A O   1 
ATOM   2510 C CB  . ILE A 1 333 ? -43.689  -0.236  20.203  1.00 55.68  ? 359  ILE A CB  1 
ATOM   2511 C CG1 . ILE A 1 333 ? -44.602  -0.880  21.241  1.00 56.42  ? 359  ILE A CG1 1 
ATOM   2512 C CG2 . ILE A 1 333 ? -44.515  0.134   18.988  1.00 58.29  ? 359  ILE A CG2 1 
ATOM   2513 C CD1 . ILE A 1 333 ? -45.228  -2.158  20.762  1.00 61.02  ? 359  ILE A CD1 1 
ATOM   2514 N N   . SER A 1 334 ? -41.452  -1.270  17.663  1.00 51.04  ? 360  SER A N   1 
ATOM   2515 C CA  . SER A 1 334 ? -40.698  -0.734  16.504  1.00 54.84  ? 360  SER A CA  1 
ATOM   2516 C C   . SER A 1 334 ? -41.137  0.634   15.955  1.00 55.13  ? 360  SER A C   1 
ATOM   2517 O O   . SER A 1 334 ? -42.304  1.008   16.062  1.00 49.96  ? 360  SER A O   1 
ATOM   2518 C CB  . SER A 1 334 ? -40.858  -1.681  15.346  1.00 56.29  ? 360  SER A CB  1 
ATOM   2519 O OG  . SER A 1 334 ? -40.230  -1.151  14.213  1.00 50.61  ? 360  SER A OG  1 
ATOM   2520 N N   . ARG A 1 335 ? -40.199  1.352   15.321  1.00 64.05  ? 361  ARG A N   1 
ATOM   2521 C CA  . ARG A 1 335 ? -40.509  2.660   14.676  1.00 61.32  ? 361  ARG A CA  1 
ATOM   2522 C C   . ARG A 1 335 ? -41.479  2.431   13.515  1.00 52.11  ? 361  ARG A C   1 
ATOM   2523 O O   . ARG A 1 335 ? -42.366  3.229   13.270  1.00 53.16  ? 361  ARG A O   1 
ATOM   2524 C CB  . ARG A 1 335 ? -39.264  3.354   14.130  1.00 60.98  ? 361  ARG A CB  1 
ATOM   2525 C CG  . ARG A 1 335 ? -38.373  3.979   15.179  1.00 91.65  ? 361  ARG A CG  1 
ATOM   2526 C CD  . ARG A 1 335 ? -37.177  4.697   14.552  1.00 113.28 ? 361  ARG A CD  1 
ATOM   2527 N NE  . ARG A 1 335 ? -36.441  5.476   15.553  1.00 121.24 ? 361  ARG A NE  1 
ATOM   2528 C CZ  . ARG A 1 335 ? -36.712  6.745   15.866  1.00 126.11 ? 361  ARG A CZ  1 
ATOM   2529 N NH1 . ARG A 1 335 ? -37.689  7.408   15.246  1.00 119.41 ? 361  ARG A NH1 1 
ATOM   2530 N NH2 . ARG A 1 335 ? -36.000  7.362   16.798  1.00 129.48 ? 361  ARG A NH2 1 
ATOM   2531 N N   . ASN A 1 336 ? -41.351  1.285   12.872  1.00 48.03  ? 362  ASN A N   1 
ATOM   2532 C CA  . ASN A 1 336 ? -42.207  0.922   11.752  1.00 52.46  ? 362  ASN A CA  1 
ATOM   2533 C C   . ASN A 1 336 ? -43.694  0.865   12.059  1.00 55.73  ? 362  ASN A C   1 
ATOM   2534 O O   . ASN A 1 336 ? -44.510  0.828   11.132  1.00 59.35  ? 362  ASN A O   1 
ATOM   2535 C CB  . ASN A 1 336 ? -41.669  -0.333  11.093  1.00 57.36  ? 362  ASN A CB  1 
ATOM   2536 C CG  . ASN A 1 336 ? -40.260  -0.116  10.558  1.00 62.44  ? 362  ASN A CG  1 
ATOM   2537 O OD1 . ASN A 1 336 ? -39.866  1.017   10.313  1.00 63.67  ? 362  ASN A OD1 1 
ATOM   2538 N ND2 . ASN A 1 336 ? -39.499  -1.180  10.400  1.00 68.27  ? 362  ASN A ND2 1 
ATOM   2539 N N   . PHE A 1 337 ? -44.075  0.857   13.342  1.00 56.31  ? 363  PHE A N   1 
ATOM   2540 C CA  . PHE A 1 337 ? -45.513  0.891   13.658  1.00 52.03  ? 363  PHE A CA  1 
ATOM   2541 C C   . PHE A 1 337 ? -46.115  2.149   13.042  1.00 53.05  ? 363  PHE A C   1 
ATOM   2542 O O   . PHE A 1 337 ? -47.274  2.139   12.638  1.00 50.82  ? 363  PHE A O   1 
ATOM   2543 C CB  . PHE A 1 337 ? -45.826  0.800   15.192  1.00 49.52  ? 363  PHE A CB  1 
ATOM   2544 C CG  . PHE A 1 337 ? -46.059  -0.606  15.680  1.00 48.98  ? 363  PHE A CG  1 
ATOM   2545 C CD1 . PHE A 1 337 ? -45.005  -1.482  15.895  1.00 50.56  ? 363  PHE A CD1 1 
ATOM   2546 C CD2 . PHE A 1 337 ? -47.343  -1.080  15.802  1.00 51.62  ? 363  PHE A CD2 1 
ATOM   2547 C CE1 . PHE A 1 337 ? -45.226  -2.804  16.211  1.00 49.13  ? 363  PHE A CE1 1 
ATOM   2548 C CE2 . PHE A 1 337 ? -47.571  -2.405  16.115  1.00 59.36  ? 363  PHE A CE2 1 
ATOM   2549 C CZ  . PHE A 1 337 ? -46.503  -3.266  16.334  1.00 52.81  ? 363  PHE A CZ  1 
ATOM   2550 N N   . SER A 1 338 ? -45.313  3.225   12.984  1.00 59.71  ? 364  SER A N   1 
ATOM   2551 C CA  . SER A 1 338 ? -45.740  4.551   12.429  1.00 57.70  ? 364  SER A CA  1 
ATOM   2552 C C   . SER A 1 338 ? -46.212  4.415   10.988  1.00 46.14  ? 364  SER A C   1 
ATOM   2553 O O   . SER A 1 338 ? -46.991  5.220   10.517  1.00 53.51  ? 364  SER A O   1 
ATOM   2554 C CB  . SER A 1 338 ? -44.606  5.576   12.459  1.00 45.66  ? 364  SER A CB  1 
ATOM   2555 O OG  . SER A 1 338 ? -43.658  5.202   11.501  1.00 46.83  ? 364  SER A OG  1 
ATOM   2556 N N   . LYS A 1 339 ? -45.748  3.388   10.305  1.00 40.41  ? 365  LYS A N   1 
ATOM   2557 C CA  . LYS A 1 339 ? -46.187  3.123   8.943   1.00 39.45  ? 365  LYS A CA  1 
ATOM   2558 C C   . LYS A 1 339 ? -47.540  2.417   8.752   1.00 47.30  ? 365  LYS A C   1 
ATOM   2559 O O   . LYS A 1 339 ? -47.924  2.186   7.616   1.00 53.47  ? 365  LYS A O   1 
ATOM   2560 C CB  . LYS A 1 339 ? -45.119  2.348   8.189   1.00 41.29  ? 365  LYS A CB  1 
ATOM   2561 C CG  . LYS A 1 339 ? -43.843  3.158   8.105   1.00 47.84  ? 365  LYS A CG  1 
ATOM   2562 C CD  . LYS A 1 339 ? -42.832  2.554   7.179   1.00 65.21  ? 365  LYS A CD  1 
ATOM   2563 C CE  . LYS A 1 339 ? -41.561  3.385   7.222   1.00 83.17  ? 365  LYS A CE  1 
ATOM   2564 N NZ  . LYS A 1 339 ? -41.869  4.810   6.932   1.00 86.08  ? 365  LYS A NZ  1 
ATOM   2565 N N   . LEU A 1 340 ? -48.258  2.055   9.824   1.00 52.60  ? 366  LEU A N   1 
ATOM   2566 C CA  . LEU A 1 340 ? -49.581  1.372   9.683   1.00 50.65  ? 366  LEU A CA  1 
ATOM   2567 C C   . LEU A 1 340 ? -50.619  2.478   9.665   1.00 53.13  ? 366  LEU A C   1 
ATOM   2568 O O   . LEU A 1 340 ? -51.448  2.613   10.579  1.00 50.69  ? 366  LEU A O   1 
ATOM   2569 C CB  . LEU A 1 340 ? -49.833  0.428   10.869  1.00 51.91  ? 366  LEU A CB  1 
ATOM   2570 C CG  . LEU A 1 340 ? -48.814  -0.703  11.083  1.00 48.90  ? 366  LEU A CG  1 
ATOM   2571 C CD1 . LEU A 1 340 ? -48.986  -1.323  12.445  1.00 50.64  ? 366  LEU A CD1 1 
ATOM   2572 C CD2 . LEU A 1 340 ? -48.832  -1.756  10.008  1.00 44.44  ? 366  LEU A CD2 1 
ATOM   2573 N N   . LEU A 1 341 ? -50.653  3.188   8.552   1.00 54.31  ? 367  LEU A N   1 
ATOM   2574 C CA  . LEU A 1 341 ? -51.523  4.347   8.430   1.00 48.08  ? 367  LEU A CA  1 
ATOM   2575 C C   . LEU A 1 341 ? -52.992  4.120   8.433   1.00 48.11  ? 367  LEU A C   1 
ATOM   2576 O O   . LEU A 1 341 ? -53.733  5.054   8.693   1.00 48.57  ? 367  LEU A O   1 
ATOM   2577 C CB  . LEU A 1 341 ? -51.122  5.170   7.224   1.00 47.82  ? 367  LEU A CB  1 
ATOM   2578 C CG  . LEU A 1 341 ? -49.706  5.750   7.222   1.00 48.67  ? 367  LEU A CG  1 
ATOM   2579 C CD1 . LEU A 1 341 ? -49.473  6.533   5.937   1.00 53.64  ? 367  LEU A CD1 1 
ATOM   2580 C CD2 . LEU A 1 341 ? -49.493  6.668   8.411   1.00 50.36  ? 367  LEU A CD2 1 
ATOM   2581 N N   . SER A 1 342 ? -53.447  2.902   8.176   1.00 45.28  ? 368  SER A N   1 
ATOM   2582 C CA  . SER A 1 342 ? -54.887  2.663   8.183   1.00 46.09  ? 368  SER A CA  1 
ATOM   2583 C C   . SER A 1 342 ? -55.333  1.936   9.486   1.00 49.24  ? 368  SER A C   1 
ATOM   2584 O O   . SER A 1 342 ? -56.531  1.685   9.690   1.00 43.68  ? 368  SER A O   1 
ATOM   2585 C CB  . SER A 1 342 ? -55.262  1.821   6.974   1.00 52.36  ? 368  SER A CB  1 
ATOM   2586 O OG  . SER A 1 342 ? -54.751  2.366   5.779   1.00 44.94  ? 368  SER A OG  1 
ATOM   2587 N N   . LEU A 1 343 ? -54.396  1.731   10.409  1.00 42.77  ? 369  LEU A N   1 
ATOM   2588 C CA  . LEU A 1 343 ? -54.680  1.006   11.664  1.00 47.47  ? 369  LEU A CA  1 
ATOM   2589 C C   . LEU A 1 343 ? -55.758  1.616   12.515  1.00 41.70  ? 369  LEU A C   1 
ATOM   2590 O O   . LEU A 1 343 ? -55.678  2.766   12.898  1.00 46.42  ? 369  LEU A O   1 
ATOM   2591 C CB  . LEU A 1 343 ? -53.412  0.907   12.531  1.00 49.46  ? 369  LEU A CB  1 
ATOM   2592 C CG  . LEU A 1 343 ? -53.444  -0.207  13.591  1.00 48.74  ? 369  LEU A CG  1 
ATOM   2593 C CD1 . LEU A 1 343 ? -53.463  -1.570  12.894  1.00 43.34  ? 369  LEU A CD1 1 
ATOM   2594 C CD2 . LEU A 1 343 ? -52.220  -0.157  14.500  1.00 45.60  ? 369  LEU A CD2 1 
ATOM   2595 N N   . ARG A 1 344 ? -56.780  0.834   12.810  1.00 47.94  ? 370  ARG A N   1 
ATOM   2596 C CA  . ARG A 1 344 ? -57.864  1.294   13.646  1.00 49.65  ? 370  ARG A CA  1 
ATOM   2597 C C   . ARG A 1 344 ? -57.820  0.640   15.045  1.00 51.24  ? 370  ARG A C   1 
ATOM   2598 O O   . ARG A 1 344 ? -58.327  1.210   16.019  1.00 49.51  ? 370  ARG A O   1 
ATOM   2599 C CB  . ARG A 1 344 ? -59.199  0.942   13.041  1.00 56.91  ? 370  ARG A CB  1 
ATOM   2600 C CG  . ARG A 1 344 ? -59.459  1.416   11.630  1.00 59.50  ? 370  ARG A CG  1 
ATOM   2601 C CD  . ARG A 1 344 ? -60.925  1.141   11.336  1.00 63.56  ? 370  ARG A CD  1 
ATOM   2602 N NE  . ARG A 1 344 ? -61.280  1.273   9.929   1.00 90.23  ? 370  ARG A NE  1 
ATOM   2603 C CZ  . ARG A 1 344 ? -62.507  1.048   9.455   1.00 107.16 ? 370  ARG A CZ  1 
ATOM   2604 N NH1 . ARG A 1 344 ? -63.498  0.739   10.296  1.00 103.06 ? 370  ARG A NH1 1 
ATOM   2605 N NH2 . ARG A 1 344 ? -62.759  1.166   8.150   1.00 99.07  ? 370  ARG A NH2 1 
ATOM   2606 N N   . ALA A 1 345 ? -57.283  -0.580  15.127  1.00 46.70  ? 371  ALA A N   1 
ATOM   2607 C CA  . ALA A 1 345 ? -57.196  -1.303  16.407  1.00 42.10  ? 371  ALA A CA  1 
ATOM   2608 C C   . ALA A 1 345 ? -55.958  -2.116  16.506  1.00 40.80  ? 371  ALA A C   1 
ATOM   2609 O O   . ALA A 1 345 ? -55.636  -2.890  15.606  1.00 42.22  ? 371  ALA A O   1 
ATOM   2610 C CB  . ALA A 1 345 ? -58.376  -2.202  16.598  1.00 41.04  ? 371  ALA A CB  1 
ATOM   2611 N N   . LEU A 1 346 ? -55.291  -1.962  17.641  1.00 37.73  ? 372  LEU A N   1 
ATOM   2612 C CA  . LEU A 1 346 ? -54.081  -2.666  17.940  1.00 42.91  ? 372  LEU A CA  1 
ATOM   2613 C C   . LEU A 1 346 ? -54.328  -3.500  19.223  1.00 49.16  ? 372  LEU A C   1 
ATOM   2614 O O   . LEU A 1 346 ? -54.682  -2.961  20.303  1.00 37.32  ? 372  LEU A O   1 
ATOM   2615 C CB  . LEU A 1 346 ? -52.990  -1.661  18.210  1.00 43.22  ? 372  LEU A CB  1 
ATOM   2616 C CG  . LEU A 1 346 ? -51.633  -2.221  18.570  1.00 47.44  ? 372  LEU A CG  1 
ATOM   2617 C CD1 . LEU A 1 346 ? -51.083  -3.115  17.462  1.00 47.28  ? 372  LEU A CD1 1 
ATOM   2618 C CD2 . LEU A 1 346 ? -50.694  -1.055  18.800  1.00 46.25  ? 372  LEU A CD2 1 
ATOM   2619 N N   . HIS A 1 347 ? -54.208  -4.811  19.091  1.00 47.96  ? 373  HIS A N   1 
ATOM   2620 C CA  . HIS A 1 347 ? -54.415  -5.707  20.234  1.00 43.16  ? 373  HIS A CA  1 
ATOM   2621 C C   . HIS A 1 347 ? -53.094  -6.251  20.693  1.00 39.86  ? 373  HIS A C   1 
ATOM   2622 O O   . HIS A 1 347 ? -52.443  -7.037  19.975  1.00 41.10  ? 373  HIS A O   1 
ATOM   2623 C CB  . HIS A 1 347 ? -55.384  -6.815  19.887  1.00 41.62  ? 373  HIS A CB  1 
ATOM   2624 C CG  . HIS A 1 347 ? -56.751  -6.319  19.559  1.00 42.72  ? 373  HIS A CG  1 
ATOM   2625 N ND1 . HIS A 1 347 ? -57.644  -5.935  20.525  1.00 45.70  ? 373  HIS A ND1 1 
ATOM   2626 C CD2 . HIS A 1 347 ? -57.390  -6.166  18.375  1.00 46.69  ? 373  HIS A CD2 1 
ATOM   2627 C CE1 . HIS A 1 347 ? -58.771  -5.541  19.955  1.00 48.88  ? 373  HIS A CE1 1 
ATOM   2628 N NE2 . HIS A 1 347 ? -58.632  -5.645  18.647  1.00 45.80  ? 373  HIS A NE2 1 
ATOM   2629 N N   . LEU A 1 348 ? -52.680  -5.755  21.862  1.00 41.09  ? 374  LEU A N   1 
ATOM   2630 C CA  . LEU A 1 348 ? -51.418  -6.104  22.515  1.00 48.48  ? 374  LEU A CA  1 
ATOM   2631 C C   . LEU A 1 348 ? -51.594  -6.684  23.901  1.00 48.55  ? 374  LEU A C   1 
ATOM   2632 O O   . LEU A 1 348 ? -50.912  -6.280  24.850  1.00 44.31  ? 374  LEU A O   1 
ATOM   2633 C CB  . LEU A 1 348 ? -50.492  -4.887  22.611  1.00 49.12  ? 374  LEU A CB  1 
ATOM   2634 C CG  . LEU A 1 348 ? -49.707  -4.564  21.363  1.00 52.74  ? 374  LEU A CG  1 
ATOM   2635 C CD1 . LEU A 1 348 ? -49.045  -3.203  21.425  1.00 56.52  ? 374  LEU A CD1 1 
ATOM   2636 C CD2 . LEU A 1 348 ? -48.681  -5.657  21.199  1.00 57.11  ? 374  LEU A CD2 1 
ATOM   2637 N N   . ARG A 1 349 ? -52.535  -7.593  24.048  1.00 45.52  ? 375  ARG A N   1 
ATOM   2638 C CA  . ARG A 1 349 ? -52.678  -8.198  25.338  1.00 50.14  ? 375  ARG A CA  1 
ATOM   2639 C C   . ARG A 1 349 ? -51.578  -9.195  25.587  1.00 52.57  ? 375  ARG A C   1 
ATOM   2640 O O   . ARG A 1 349 ? -50.930  -9.702  24.653  1.00 45.49  ? 375  ARG A O   1 
ATOM   2641 C CB  . ARG A 1 349 ? -53.994  -8.915  25.507  1.00 44.63  ? 375  ARG A CB  1 
ATOM   2642 C CG  . ARG A 1 349 ? -55.126  -7.945  25.507  1.00 55.79  ? 375  ARG A CG  1 
ATOM   2643 C CD  . ARG A 1 349 ? -56.367  -8.556  26.075  1.00 58.39  ? 375  ARG A CD  1 
ATOM   2644 N NE  . ARG A 1 349 ? -56.655  -9.787  25.420  1.00 73.66  ? 375  ARG A NE  1 
ATOM   2645 C CZ  . ARG A 1 349 ? -57.691  -10.539 25.715  1.00 100.69 ? 375  ARG A CZ  1 
ATOM   2646 N NH1 . ARG A 1 349 ? -58.566  -10.128 26.630  1.00 88.77  ? 375  ARG A NH1 1 
ATOM   2647 N NH2 . ARG A 1 349 ? -57.861  -11.677 25.058  1.00 122.76 ? 375  ARG A NH2 1 
ATOM   2648 N N   . GLY A 1 350 ? -51.239  -9.338  26.852  1.00 44.99  ? 376  GLY A N   1 
ATOM   2649 C CA  . GLY A 1 350 ? -50.270  -10.344 27.215  1.00 46.56  ? 376  GLY A CA  1 
ATOM   2650 C C   . GLY A 1 350 ? -48.915  -10.350 26.598  1.00 43.98  ? 376  GLY A C   1 
ATOM   2651 O O   . GLY A 1 350 ? -48.445  -11.390 26.125  1.00 41.21  ? 376  GLY A O   1 
ATOM   2652 N N   . TYR A 1 351 ? -48.317  -9.177  26.546  1.00 46.28  ? 377  TYR A N   1 
ATOM   2653 C CA  . TYR A 1 351 ? -46.951  -9.035  26.070  1.00 50.36  ? 377  TYR A CA  1 
ATOM   2654 C C   . TYR A 1 351 ? -46.170  -9.169  27.390  1.00 43.77  ? 377  TYR A C   1 
ATOM   2655 O O   . TYR A 1 351 ? -45.128  -9.746  27.464  1.00 47.35  ? 377  TYR A O   1 
ATOM   2656 C CB  . TYR A 1 351 ? -46.749  -7.651  25.458  1.00 44.49  ? 377  TYR A CB  1 
ATOM   2657 C CG  . TYR A 1 351 ? -45.333  -7.338  25.067  1.00 46.18  ? 377  TYR A CG  1 
ATOM   2658 C CD1 . TYR A 1 351 ? -44.451  -6.829  25.996  1.00 54.98  ? 377  TYR A CD1 1 
ATOM   2659 C CD2 . TYR A 1 351 ? -44.922  -7.408  23.753  1.00 50.24  ? 377  TYR A CD2 1 
ATOM   2660 C CE1 . TYR A 1 351 ? -43.178  -6.458  25.651  1.00 50.34  ? 377  TYR A CE1 1 
ATOM   2661 C CE2 . TYR A 1 351 ? -43.638  -7.062  23.393  1.00 52.49  ? 377  TYR A CE2 1 
ATOM   2662 C CZ  . TYR A 1 351 ? -42.774  -6.558  24.345  1.00 55.89  ? 377  TYR A CZ  1 
ATOM   2663 O OH  . TYR A 1 351 ? -41.477  -6.178  24.002  1.00 53.93  ? 377  TYR A OH  1 
ATOM   2664 N N   . VAL A 1 352 ? -46.693  -8.521  28.408  1.00 43.22  ? 378  VAL A N   1 
ATOM   2665 C CA  . VAL A 1 352 ? -46.151  -8.565  29.754  1.00 47.24  ? 378  VAL A CA  1 
ATOM   2666 C C   . VAL A 1 352 ? -44.931  -7.692  29.930  1.00 44.63  ? 378  VAL A C   1 
ATOM   2667 O O   . VAL A 1 352 ? -43.826  -8.053  29.539  1.00 48.48  ? 378  VAL A O   1 
ATOM   2668 C CB  . VAL A 1 352 ? -45.877  -10.006 30.220  1.00 49.09  ? 378  VAL A CB  1 
ATOM   2669 C CG1 . VAL A 1 352 ? -45.649  -9.990  31.727  1.00 49.20  ? 378  VAL A CG1 1 
ATOM   2670 C CG2 . VAL A 1 352 ? -47.081  -10.908 29.920  1.00 43.41  ? 378  VAL A CG2 1 
ATOM   2671 N N   . PHE A 1 353 ? -45.136  -6.564  30.606  1.00 40.10  ? 379  PHE A N   1 
ATOM   2672 C CA  . PHE A 1 353 ? -44.068  -5.605  30.822  1.00 40.90  ? 379  PHE A CA  1 
ATOM   2673 C C   . PHE A 1 353 ? -44.479  -4.777  32.001  1.00 42.20  ? 379  PHE A C   1 
ATOM   2674 O O   . PHE A 1 353 ? -45.665  -4.716  32.293  1.00 49.36  ? 379  PHE A O   1 
ATOM   2675 C CB  . PHE A 1 353 ? -43.812  -4.772  29.566  1.00 44.20  ? 379  PHE A CB  1 
ATOM   2676 C CG  . PHE A 1 353 ? -44.981  -3.954  29.101  1.00 40.18  ? 379  PHE A CG  1 
ATOM   2677 C CD1 . PHE A 1 353 ? -45.961  -4.510  28.306  1.00 46.64  ? 379  PHE A CD1 1 
ATOM   2678 C CD2 . PHE A 1 353 ? -44.993  -2.589  29.297  1.00 44.79  ? 379  PHE A CD2 1 
ATOM   2679 C CE1 . PHE A 1 353 ? -47.010  -3.735  27.821  1.00 44.85  ? 379  PHE A CE1 1 
ATOM   2680 C CE2 . PHE A 1 353 ? -46.024  -1.806  28.805  1.00 41.49  ? 379  PHE A CE2 1 
ATOM   2681 C CZ  . PHE A 1 353 ? -47.032  -2.389  28.065  1.00 43.04  ? 379  PHE A CZ  1 
ATOM   2682 N N   . GLN A 1 354 ? -43.567  -3.987  32.554  1.00 47.36  ? 380  GLN A N   1 
ATOM   2683 C CA  . GLN A 1 354 ? -43.887  -3.260  33.806  1.00 52.68  ? 380  GLN A CA  1 
ATOM   2684 C C   . GLN A 1 354 ? -44.279  -1.830  33.745  1.00 58.74  ? 380  GLN A C   1 
ATOM   2685 O O   . GLN A 1 354 ? -45.057  -1.339  34.586  1.00 51.88  ? 380  GLN A O   1 
ATOM   2686 C CB  . GLN A 1 354 ? -42.660  -3.333  34.712  1.00 54.60  ? 380  GLN A CB  1 
ATOM   2687 C CG  . GLN A 1 354 ? -42.133  -4.760  34.886  1.00 62.28  ? 380  GLN A CG  1 
ATOM   2688 C CD  . GLN A 1 354 ? -40.850  -4.835  35.695  1.00 56.15  ? 380  GLN A CD  1 
ATOM   2689 O OE1 . GLN A 1 354 ? -40.688  -4.162  36.698  1.00 56.43  ? 380  GLN A OE1 1 
ATOM   2690 N NE2 . GLN A 1 354 ? -39.981  -5.724  35.303  1.00 61.09  ? 380  GLN A NE2 1 
ATOM   2691 N N   . GLU A 1 355 ? -43.721  -1.137  32.774  1.00 60.82  ? 381  GLU A N   1 
ATOM   2692 C CA  . GLU A 1 355 ? -43.976  0.254   32.669  1.00 62.39  ? 381  GLU A CA  1 
ATOM   2693 C C   . GLU A 1 355 ? -44.240  0.721   31.235  1.00 56.68  ? 381  GLU A C   1 
ATOM   2694 O O   . GLU A 1 355 ? -43.695  0.175   30.273  1.00 59.49  ? 381  GLU A O   1 
ATOM   2695 C CB  . GLU A 1 355 ? -42.759  0.949   33.268  1.00 70.01  ? 381  GLU A CB  1 
ATOM   2696 C CG  . GLU A 1 355 ? -42.853  2.457   33.365  1.00 102.57 ? 381  GLU A CG  1 
ATOM   2697 C CD  . GLU A 1 355 ? -41.624  3.065   34.007  1.00 105.98 ? 381  GLU A CD  1 
ATOM   2698 O OE1 . GLU A 1 355 ? -40.721  2.288   34.405  1.00 94.31  ? 381  GLU A OE1 1 
ATOM   2699 O OE2 . GLU A 1 355 ? -41.579  4.311   34.119  1.00 111.45 ? 381  GLU A OE2 1 
ATOM   2700 N N   . LEU A 1 356 ? -45.152  1.681   31.096  1.00 57.42  ? 382  LEU A N   1 
ATOM   2701 C CA  . LEU A 1 356 ? -45.466  2.244   29.779  1.00 59.32  ? 382  LEU A CA  1 
ATOM   2702 C C   . LEU A 1 356 ? -45.126  3.719   29.845  1.00 56.03  ? 382  LEU A C   1 
ATOM   2703 O O   . LEU A 1 356 ? -45.724  4.467   30.627  1.00 49.64  ? 382  LEU A O   1 
ATOM   2704 C CB  . LEU A 1 356 ? -46.933  2.083   29.417  1.00 55.84  ? 382  LEU A CB  1 
ATOM   2705 C CG  . LEU A 1 356 ? -47.362  2.558   28.017  1.00 50.61  ? 382  LEU A CG  1 
ATOM   2706 C CD1 . LEU A 1 356 ? -46.741  1.672   26.942  1.00 49.77  ? 382  LEU A CD1 1 
ATOM   2707 C CD2 . LEU A 1 356 ? -48.894  2.537   27.902  1.00 48.16  ? 382  LEU A CD2 1 
ATOM   2708 N N   . ARG A 1 357 ? -44.124  4.111   29.069  1.00 58.48  ? 383  ARG A N   1 
ATOM   2709 C CA  . ARG A 1 357 ? -43.677  5.494   29.006  1.00 69.91  ? 383  ARG A CA  1 
ATOM   2710 C C   . ARG A 1 357 ? -44.126  6.148   27.695  1.00 67.76  ? 383  ARG A C   1 
ATOM   2711 O O   . ARG A 1 357 ? -44.262  5.467   26.680  1.00 69.86  ? 383  ARG A O   1 
ATOM   2712 C CB  . ARG A 1 357 ? -42.168  5.529   29.056  1.00 76.14  ? 383  ARG A CB  1 
ATOM   2713 C CG  . ARG A 1 357 ? -41.568  4.892   30.281  1.00 84.11  ? 383  ARG A CG  1 
ATOM   2714 C CD  . ARG A 1 357 ? -40.062  4.904   30.156  1.00 92.60  ? 383  ARG A CD  1 
ATOM   2715 N NE  . ARG A 1 357 ? -39.619  4.169   28.971  1.00 86.89  ? 383  ARG A NE  1 
ATOM   2716 C CZ  . ARG A 1 357 ? -38.347  3.999   28.633  1.00 86.33  ? 383  ARG A CZ  1 
ATOM   2717 N NH1 . ARG A 1 357 ? -37.376  4.477   29.407  1.00 91.00  ? 383  ARG A NH1 1 
ATOM   2718 N NH2 . ARG A 1 357 ? -38.042  3.310   27.547  1.00 81.33  ? 383  ARG A NH2 1 
ATOM   2719 N N   . GLU A 1 358 ? -44.201  7.480   27.684  1.00 76.96  ? 384  GLU A N   1 
ATOM   2720 C CA  . GLU A 1 358 ? -44.634  8.223   26.486  1.00 74.33  ? 384  GLU A CA  1 
ATOM   2721 C C   . GLU A 1 358 ? -43.800  7.883   25.246  1.00 66.01  ? 384  GLU A C   1 
ATOM   2722 O O   . GLU A 1 358 ? -44.349  7.658   24.168  1.00 80.22  ? 384  GLU A O   1 
ATOM   2723 C CB  . GLU A 1 358 ? -44.692  9.737   26.764  1.00 85.91  ? 384  GLU A CB  1 
ATOM   2724 C CG  . GLU A 1 358 ? -45.342  10.554  25.642  1.00 108.29 ? 384  GLU A CG  1 
ATOM   2725 C CD  . GLU A 1 358 ? -45.771  11.974  26.052  1.00 111.63 ? 384  GLU A CD  1 
ATOM   2726 O OE1 . GLU A 1 358 ? -45.473  12.420  27.194  1.00 98.21  ? 384  GLU A OE1 1 
ATOM   2727 O OE2 . GLU A 1 358 ? -46.476  12.623  25.233  1.00 116.84 ? 384  GLU A OE2 1 
ATOM   2728 N N   . ASP A 1 359 ? -42.500  7.720   25.417  1.00 67.69  ? 385  ASP A N   1 
ATOM   2729 C CA  . ASP A 1 359 ? -41.629  7.389   24.288  1.00 72.42  ? 385  ASP A CA  1 
ATOM   2730 C C   . ASP A 1 359 ? -41.881  6.017   23.702  1.00 68.12  ? 385  ASP A C   1 
ATOM   2731 O O   . ASP A 1 359 ? -41.717  5.813   22.501  1.00 73.38  ? 385  ASP A O   1 
ATOM   2732 C CB  . ASP A 1 359 ? -40.149  7.529   24.674  1.00 80.28  ? 385  ASP A CB  1 
ATOM   2733 C CG  . ASP A 1 359 ? -39.707  8.990   24.831  1.00 94.00  ? 385  ASP A CG  1 
ATOM   2734 O OD1 . ASP A 1 359 ? -38.663  9.210   25.479  1.00 106.15 ? 385  ASP A OD1 1 
ATOM   2735 O OD2 . ASP A 1 359 ? -40.399  9.917   24.324  1.00 88.89  ? 385  ASP A OD2 1 
ATOM   2736 N N   . ASP A 1 360 ? -42.276  5.075   24.547  1.00 71.11  ? 386  ASP A N   1 
ATOM   2737 C CA  . ASP A 1 360 ? -42.544  3.702   24.106  1.00 64.24  ? 386  ASP A CA  1 
ATOM   2738 C C   . ASP A 1 360 ? -43.644  3.641   23.034  1.00 49.86  ? 386  ASP A C   1 
ATOM   2739 O O   . ASP A 1 360 ? -43.600  2.805   22.162  1.00 51.36  ? 386  ASP A O   1 
ATOM   2740 C CB  . ASP A 1 360 ? -42.944  2.850   25.312  1.00 81.99  ? 386  ASP A CB  1 
ATOM   2741 C CG  . ASP A 1 360 ? -41.849  2.776   26.377  1.00 79.67  ? 386  ASP A CG  1 
ATOM   2742 O OD1 . ASP A 1 360 ? -40.667  2.633   26.015  1.00 69.24  ? 386  ASP A OD1 1 
ATOM   2743 O OD2 . ASP A 1 360 ? -42.192  2.740   27.573  1.00 84.24  ? 386  ASP A OD2 1 
ATOM   2744 N N   . PHE A 1 361 ? -44.597  4.565   23.083  1.00 43.88  ? 387  PHE A N   1 
ATOM   2745 C CA  . PHE A 1 361 ? -45.713  4.622   22.127  1.00 46.80  ? 387  PHE A CA  1 
ATOM   2746 C C   . PHE A 1 361 ? -45.652  5.721   21.090  1.00 54.46  ? 387  PHE A C   1 
ATOM   2747 O O   . PHE A 1 361 ? -46.676  6.106   20.521  1.00 50.71  ? 387  PHE A O   1 
ATOM   2748 C CB  . PHE A 1 361 ? -47.022  4.669   22.914  1.00 45.80  ? 387  PHE A CB  1 
ATOM   2749 C CG  . PHE A 1 361 ? -47.623  3.323   23.140  1.00 54.44  ? 387  PHE A CG  1 
ATOM   2750 C CD1 . PHE A 1 361 ? -46.823  2.198   23.235  1.00 53.78  ? 387  PHE A CD1 1 
ATOM   2751 C CD2 . PHE A 1 361 ? -48.947  3.213   23.488  1.00 57.04  ? 387  PHE A CD2 1 
ATOM   2752 C CE1 . PHE A 1 361 ? -47.386  0.970   23.377  1.00 50.59  ? 387  PHE A CE1 1 
ATOM   2753 C CE2 . PHE A 1 361 ? -49.493  1.996   23.776  1.00 48.78  ? 387  PHE A CE2 1 
ATOM   2754 C CZ  . PHE A 1 361 ? -48.718  0.874   23.701  1.00 50.29  ? 387  PHE A CZ  1 
ATOM   2755 N N   . GLN A 1 362 ? -44.432  6.127   20.770  1.00 65.59  ? 388  GLN A N   1 
ATOM   2756 C CA  . GLN A 1 362 ? -44.170  7.198   19.819  1.00 68.83  ? 388  GLN A CA  1 
ATOM   2757 C C   . GLN A 1 362 ? -44.699  6.827   18.429  1.00 59.50  ? 388  GLN A C   1 
ATOM   2758 O O   . GLN A 1 362 ? -45.525  7.533   17.869  1.00 51.13  ? 388  GLN A O   1 
ATOM   2759 C CB  . GLN A 1 362 ? -42.658  7.458   19.763  1.00 89.03  ? 388  GLN A CB  1 
ATOM   2760 C CG  . GLN A 1 362 ? -42.236  8.699   19.003  1.00 107.31 ? 388  GLN A CG  1 
ATOM   2761 C CD  . GLN A 1 362 ? -42.586  9.982   19.728  1.00 106.87 ? 388  GLN A CD  1 
ATOM   2762 O OE1 . GLN A 1 362 ? -42.581  11.054  19.131  1.00 125.88 ? 388  GLN A OE1 1 
ATOM   2763 N NE2 . GLN A 1 362 ? -42.871  9.887   21.023  1.00 97.36  ? 388  GLN A NE2 1 
ATOM   2764 N N   . PRO A 1 363 ? -44.323  5.651   17.939  1.00 40.29  ? 389  PRO A N   1 
ATOM   2765 C CA  . PRO A 1 363 ? -44.730  5.223   16.634  1.00 47.38  ? 389  PRO A CA  1 
ATOM   2766 C C   . PRO A 1 363 ? -46.213  5.242   16.316  1.00 48.16  ? 389  PRO A C   1 
ATOM   2767 O O   . PRO A 1 363 ? -46.564  5.401   15.150  1.00 65.77  ? 389  PRO A O   1 
ATOM   2768 C CB  . PRO A 1 363 ? -44.184  3.789   16.555  1.00 53.00  ? 389  PRO A CB  1 
ATOM   2769 C CG  . PRO A 1 363 ? -43.006  3.777   17.476  1.00 43.12  ? 389  PRO A CG  1 
ATOM   2770 C CD  . PRO A 1 363 ? -43.506  4.629   18.615  1.00 42.78  ? 389  PRO A CD  1 
ATOM   2771 N N   . LEU A 1 364 ? -47.062  5.172   17.332  1.00 48.03  ? 390  LEU A N   1 
ATOM   2772 C CA  . LEU A 1 364 ? -48.522  5.130   17.160  1.00 47.24  ? 390  LEU A CA  1 
ATOM   2773 C C   . LEU A 1 364 ? -49.243  6.476   17.275  1.00 51.52  ? 390  LEU A C   1 
ATOM   2774 O O   . LEU A 1 364 ? -50.478  6.591   17.000  1.00 46.39  ? 390  LEU A O   1 
ATOM   2775 C CB  . LEU A 1 364 ? -49.098  4.219   18.272  1.00 49.44  ? 390  LEU A CB  1 
ATOM   2776 C CG  . LEU A 1 364 ? -48.564  2.783   18.442  1.00 51.81  ? 390  LEU A CG  1 
ATOM   2777 C CD1 . LEU A 1 364 ? -49.090  2.170   19.736  1.00 53.50  ? 390  LEU A CD1 1 
ATOM   2778 C CD2 . LEU A 1 364 ? -48.844  1.868   17.264  1.00 48.75  ? 390  LEU A CD2 1 
ATOM   2779 N N   . MET A 1 365 ? -48.536  7.478   17.777  1.00 52.81  ? 391  MET A N   1 
ATOM   2780 C CA  . MET A 1 365 ? -49.159  8.783   17.979  1.00 52.69  ? 391  MET A CA  1 
ATOM   2781 C C   . MET A 1 365 ? -49.526  9.530   16.713  1.00 52.52  ? 391  MET A C   1 
ATOM   2782 O O   . MET A 1 365 ? -50.278  10.488  16.767  1.00 54.98  ? 391  MET A O   1 
ATOM   2783 C CB  . MET A 1 365 ? -48.327  9.618   18.931  1.00 60.11  ? 391  MET A CB  1 
ATOM   2784 C CG  . MET A 1 365 ? -48.421  9.125   20.355  1.00 67.67  ? 391  MET A CG  1 
ATOM   2785 S SD  . MET A 1 365 ? -47.308  9.889   21.549  1.00 68.03  ? 391  MET A SD  1 
ATOM   2786 C CE  . MET A 1 365 ? -45.784  9.197   20.982  1.00 77.07  ? 391  MET A CE  1 
ATOM   2787 N N   . GLN A 1 366 ? -49.146  8.994   15.563  1.00 65.37  ? 392  GLN A N   1 
ATOM   2788 C CA  . GLN A 1 366 ? -49.474  9.648   14.312  1.00 81.30  ? 392  GLN A CA  1 
ATOM   2789 C C   . GLN A 1 366 ? -50.532  8.893   13.480  1.00 72.57  ? 392  GLN A C   1 
ATOM   2790 O O   . GLN A 1 366 ? -51.118  9.455   12.578  1.00 69.76  ? 392  GLN A O   1 
ATOM   2791 C CB  . GLN A 1 366 ? -48.195  9.874   13.515  1.00 106.07 ? 392  GLN A CB  1 
ATOM   2792 C CG  . GLN A 1 366 ? -47.460  8.624   13.045  1.00 115.99 ? 392  GLN A CG  1 
ATOM   2793 C CD  . GLN A 1 366 ? -46.103  8.966   12.445  1.00 123.70 ? 392  GLN A CD  1 
ATOM   2794 O OE1 . GLN A 1 366 ? -45.802  8.598   11.310  1.00 131.18 ? 392  GLN A OE1 1 
ATOM   2795 N NE2 . GLN A 1 366 ? -45.344  9.795   13.149  1.00 127.86 ? 392  GLN A NE2 1 
ATOM   2796 N N   . LEU A 1 367 ? -50.793  7.638   13.809  1.00 53.10  ? 393  LEU A N   1 
ATOM   2797 C CA  . LEU A 1 367 ? -51.771  6.856   13.080  1.00 53.52  ? 393  LEU A CA  1 
ATOM   2798 C C   . LEU A 1 367 ? -53.121  7.557   13.243  1.00 49.99  ? 393  LEU A C   1 
ATOM   2799 O O   . LEU A 1 367 ? -53.656  7.599   14.324  1.00 51.80  ? 393  LEU A O   1 
ATOM   2800 C CB  . LEU A 1 367 ? -51.805  5.439   13.627  1.00 48.36  ? 393  LEU A CB  1 
ATOM   2801 C CG  . LEU A 1 367 ? -50.431  4.752   13.643  1.00 49.10  ? 393  LEU A CG  1 
ATOM   2802 C CD1 . LEU A 1 367 ? -50.526  3.318   14.184  1.00 54.32  ? 393  LEU A CD1 1 
ATOM   2803 C CD2 . LEU A 1 367 ? -49.797  4.723   12.274  1.00 50.38  ? 393  LEU A CD2 1 
ATOM   2804 N N   . PRO A 1 368 ? -53.672  8.107   12.153  1.00 50.77  ? 394  PRO A N   1 
ATOM   2805 C CA  . PRO A 1 368 ? -54.926  8.872   12.214  1.00 47.56  ? 394  PRO A CA  1 
ATOM   2806 C C   . PRO A 1 368 ? -56.182  8.160   12.516  1.00 47.96  ? 394  PRO A C   1 
ATOM   2807 O O   . PRO A 1 368 ? -57.135  8.811   12.870  1.00 55.57  ? 394  PRO A O   1 
ATOM   2808 C CB  . PRO A 1 368 ? -55.045  9.479   10.815  1.00 45.50  ? 394  PRO A CB  1 
ATOM   2809 C CG  . PRO A 1 368 ? -54.227  8.605   9.948   1.00 48.10  ? 394  PRO A CG  1 
ATOM   2810 C CD  . PRO A 1 368 ? -53.108  8.098   10.795  1.00 50.46  ? 394  PRO A CD  1 
ATOM   2811 N N   . ASN A 1 369 ? -56.253  6.861   12.267  1.00 52.73  ? 395  ASN A N   1 
ATOM   2812 C CA  . ASN A 1 369 ? -57.484  6.133   12.557  1.00 57.17  ? 395  ASN A CA  1 
ATOM   2813 C C   . ASN A 1 369 ? -57.411  5.186   13.788  1.00 56.13  ? 395  ASN A C   1 
ATOM   2814 O O   . ASN A 1 369 ? -58.313  4.398   14.025  1.00 43.73  ? 395  ASN A O   1 
ATOM   2815 C CB  . ASN A 1 369 ? -57.891  5.349   11.328  1.00 67.86  ? 395  ASN A CB  1 
ATOM   2816 C CG  . ASN A 1 369 ? -58.252  6.232   10.169  1.00 63.59  ? 395  ASN A CG  1 
ATOM   2817 O OD1 . ASN A 1 369 ? -57.716  6.076   9.073   1.00 54.92  ? 395  ASN A OD1 1 
ATOM   2818 N ND2 . ASN A 1 369 ? -59.091  7.211   10.415  1.00 75.24  ? 395  ASN A ND2 1 
ATOM   2819 N N   . LEU A 1 370 ? -56.348  5.262   14.569  1.00 51.79  ? 396  LEU A N   1 
ATOM   2820 C CA  . LEU A 1 370 ? -56.235  4.393   15.730  1.00 48.72  ? 396  LEU A CA  1 
ATOM   2821 C C   . LEU A 1 370 ? -57.259  4.783   16.820  1.00 47.45  ? 396  LEU A C   1 
ATOM   2822 O O   . LEU A 1 370 ? -57.096  5.768   17.498  1.00 49.38  ? 396  LEU A O   1 
ATOM   2823 C CB  . LEU A 1 370 ? -54.827  4.459   16.263  1.00 45.11  ? 396  LEU A CB  1 
ATOM   2824 C CG  . LEU A 1 370 ? -54.527  3.544   17.419  1.00 50.19  ? 396  LEU A CG  1 
ATOM   2825 C CD1 . LEU A 1 370 ? -54.877  2.121   17.006  1.00 51.38  ? 396  LEU A CD1 1 
ATOM   2826 C CD2 . LEU A 1 370 ? -53.059  3.648   17.786  1.00 46.30  ? 396  LEU A CD2 1 
ATOM   2827 N N   . SER A 1 371 ? -58.347  4.034   16.934  1.00 44.37  ? 397  SER A N   1 
ATOM   2828 C CA  . SER A 1 371 ? -59.362  4.329   17.928  1.00 48.09  ? 397  SER A CA  1 
ATOM   2829 C C   . SER A 1 371 ? -59.383  3.374   19.137  1.00 49.30  ? 397  SER A C   1 
ATOM   2830 O O   . SER A 1 371 ? -59.908  3.729   20.190  1.00 45.69  ? 397  SER A O   1 
ATOM   2831 C CB  . SER A 1 371 ? -60.709  4.373   17.266  1.00 46.31  ? 397  SER A CB  1 
ATOM   2832 O OG  . SER A 1 371 ? -60.841  3.253   16.437  1.00 55.43  ? 397  SER A OG  1 
ATOM   2833 N N   . THR A 1 372 ? -58.733  2.224   19.000  1.00 41.87  ? 398  THR A N   1 
ATOM   2834 C CA  . THR A 1 372 ? -58.672  1.244   20.053  1.00 42.37  ? 398  THR A CA  1 
ATOM   2835 C C   . THR A 1 372 ? -57.282  0.702   20.352  1.00 45.52  ? 398  THR A C   1 
ATOM   2836 O O   . THR A 1 372 ? -56.631  0.118   19.465  1.00 42.88  ? 398  THR A O   1 
ATOM   2837 C CB  . THR A 1 372 ? -59.479  -0.006  19.665  1.00 51.11  ? 398  THR A CB  1 
ATOM   2838 O OG1 . THR A 1 372 ? -60.864  0.305   19.667  1.00 54.09  ? 398  THR A OG1 1 
ATOM   2839 C CG2 . THR A 1 372 ? -59.276  -1.105  20.667  1.00 53.11  ? 398  THR A CG2 1 
ATOM   2840 N N   . ILE A 1 373 ? -56.847  0.877   21.598  1.00 38.82  ? 399  ILE A N   1 
ATOM   2841 C CA  . ILE A 1 373 ? -55.576  0.327   22.066  1.00 51.18  ? 399  ILE A CA  1 
ATOM   2842 C C   . ILE A 1 373 ? -55.920  -0.667  23.200  1.00 48.25  ? 399  ILE A C   1 
ATOM   2843 O O   . ILE A 1 373 ? -56.538  -0.316  24.237  1.00 38.65  ? 399  ILE A O   1 
ATOM   2844 C CB  . ILE A 1 373 ? -54.582  1.376   22.573  1.00 57.24  ? 399  ILE A CB  1 
ATOM   2845 C CG1 . ILE A 1 373 ? -54.085  2.191   21.409  1.00 69.48  ? 399  ILE A CG1 1 
ATOM   2846 C CG2 . ILE A 1 373 ? -53.360  0.682   23.166  1.00 60.19  ? 399  ILE A CG2 1 
ATOM   2847 C CD1 . ILE A 1 373 ? -53.227  3.371   21.819  1.00 85.17  ? 399  ILE A CD1 1 
ATOM   2848 N N   . ASN A 1 374 ? -55.543  -1.910  22.981  1.00 46.49  ? 400  ASN A N   1 
ATOM   2849 C CA  . ASN A 1 374 ? -55.821  -2.970  23.940  1.00 43.98  ? 400  ASN A CA  1 
ATOM   2850 C C   . ASN A 1 374 ? -54.554  -3.444  24.592  1.00 43.28  ? 400  ASN A C   1 
ATOM   2851 O O   . ASN A 1 374 ? -53.731  -4.119  23.941  1.00 47.64  ? 400  ASN A O   1 
ATOM   2852 C CB  . ASN A 1 374 ? -56.472  -4.142  23.229  1.00 45.93  ? 400  ASN A CB  1 
ATOM   2853 C CG  . ASN A 1 374 ? -56.862  -5.257  24.174  1.00 51.04  ? 400  ASN A CG  1 
ATOM   2854 O OD1 . ASN A 1 374 ? -56.623  -5.198  25.403  1.00 42.60  ? 400  ASN A OD1 1 
ATOM   2855 N ND2 . ASN A 1 374 ? -57.524  -6.256  23.626  1.00 42.95  ? 400  ASN A ND2 1 
ATOM   2856 N N   . LEU A 1 375 ? -54.400  -3.084  25.871  1.00 39.12  ? 401  LEU A N   1 
ATOM   2857 C CA  . LEU A 1 375 ? -53.252  -3.452  26.666  1.00 44.80  ? 401  LEU A CA  1 
ATOM   2858 C C   . LEU A 1 375 ? -53.668  -4.280  27.867  1.00 45.00  ? 401  LEU A C   1 
ATOM   2859 O O   . LEU A 1 375 ? -53.018  -4.281  28.890  1.00 47.21  ? 401  LEU A O   1 
ATOM   2860 C CB  . LEU A 1 375 ? -52.493  -2.221  27.116  1.00 48.88  ? 401  LEU A CB  1 
ATOM   2861 C CG  . LEU A 1 375 ? -51.734  -1.490  26.024  1.00 49.20  ? 401  LEU A CG  1 
ATOM   2862 C CD1 . LEU A 1 375 ? -51.205  -0.178  26.575  1.00 49.99  ? 401  LEU A CD1 1 
ATOM   2863 C CD2 . LEU A 1 375 ? -50.620  -2.359  25.485  1.00 47.11  ? 401  LEU A CD2 1 
ATOM   2864 N N   . GLY A 1 376 ? -54.737  -5.025  27.719  1.00 44.06  ? 402  GLY A N   1 
ATOM   2865 C CA  . GLY A 1 376 ? -55.187  -5.848  28.781  1.00 40.05  ? 402  GLY A CA  1 
ATOM   2866 C C   . GLY A 1 376 ? -54.194  -6.952  29.088  1.00 43.46  ? 402  GLY A C   1 
ATOM   2867 O O   . GLY A 1 376 ? -53.429  -7.377  28.223  1.00 45.62  ? 402  GLY A O   1 
ATOM   2868 N N   . ILE A 1 377 ? -54.124  -7.311  30.367  1.00 43.20  ? 403  ILE A N   1 
ATOM   2869 C CA  . ILE A 1 377 ? -53.288  -8.405  30.861  1.00 44.01  ? 403  ILE A CA  1 
ATOM   2870 C C   . ILE A 1 377 ? -51.837  -8.268  30.564  1.00 37.65  ? 403  ILE A C   1 
ATOM   2871 O O   . ILE A 1 377 ? -51.243  -9.108  29.939  1.00 39.63  ? 403  ILE A O   1 
ATOM   2872 C CB  . ILE A 1 377 ? -53.729  -9.755  30.261  1.00 49.72  ? 403  ILE A CB  1 
ATOM   2873 C CG1 . ILE A 1 377 ? -55.233  -9.880  30.293  1.00 59.66  ? 403  ILE A CG1 1 
ATOM   2874 C CG2 . ILE A 1 377 ? -53.127  -10.908 31.058  1.00 54.31  ? 403  ILE A CG2 1 
ATOM   2875 C CD1 . ILE A 1 377 ? -55.714  -11.127 29.608  1.00 69.64  ? 403  ILE A CD1 1 
ATOM   2876 N N   . ASN A 1 378 ? -51.256  -7.203  31.027  1.00 43.78  ? 404  ASN A N   1 
ATOM   2877 C CA  . ASN A 1 378 ? -49.849  -6.958  30.814  1.00 47.47  ? 404  ASN A CA  1 
ATOM   2878 C C   . ASN A 1 378 ? -49.067  -6.777  32.112  1.00 44.55  ? 404  ASN A C   1 
ATOM   2879 O O   . ASN A 1 378 ? -47.842  -6.816  32.117  1.00 55.81  ? 404  ASN A O   1 
ATOM   2880 C CB  . ASN A 1 378 ? -49.696  -5.772  29.850  1.00 43.87  ? 404  ASN A CB  1 
ATOM   2881 C CG  . ASN A 1 378 ? -49.784  -6.201  28.412  1.00 45.37  ? 404  ASN A CG  1 
ATOM   2882 O OD1 . ASN A 1 378 ? -48.905  -6.962  27.907  1.00 39.96  ? 404  ASN A OD1 1 
ATOM   2883 N ND2 . ASN A 1 378 ? -50.743  -5.625  27.690  1.00 50.29  ? 404  ASN A ND2 1 
ATOM   2884 N N   . PHE A 1 379 ? -49.799  -6.702  33.204  1.00 43.33  ? 405  PHE A N   1 
ATOM   2885 C CA  . PHE A 1 379 ? -49.242  -6.547  34.529  1.00 52.49  ? 405  PHE A CA  1 
ATOM   2886 C C   . PHE A 1 379 ? -48.344  -5.369  34.601  1.00 46.48  ? 405  PHE A C   1 
ATOM   2887 O O   . PHE A 1 379 ? -47.310  -5.422  35.205  1.00 59.22  ? 405  PHE A O   1 
ATOM   2888 C CB  . PHE A 1 379 ? -48.539  -7.819  34.960  1.00 47.85  ? 405  PHE A CB  1 
ATOM   2889 C CG  . PHE A 1 379 ? -49.407  -9.017  34.824  1.00 50.72  ? 405  PHE A CG  1 
ATOM   2890 C CD1 . PHE A 1 379 ? -50.408  -9.266  35.751  1.00 58.16  ? 405  PHE A CD1 1 
ATOM   2891 C CD2 . PHE A 1 379 ? -49.297  -9.843  33.726  1.00 48.57  ? 405  PHE A CD2 1 
ATOM   2892 C CE1 . PHE A 1 379 ? -51.283  -10.320 35.574  1.00 55.93  ? 405  PHE A CE1 1 
ATOM   2893 C CE2 . PHE A 1 379 ? -50.134  -10.924 33.569  1.00 50.42  ? 405  PHE A CE2 1 
ATOM   2894 C CZ  . PHE A 1 379 ? -51.140  -11.155 34.483  1.00 53.94  ? 405  PHE A CZ  1 
ATOM   2895 N N   . ILE A 1 380 ? -48.864  -4.271  34.095  1.00 50.56  ? 406  ILE A N   1 
ATOM   2896 C CA  . ILE A 1 380 ? -48.200  -2.996  34.033  1.00 50.50  ? 406  ILE A CA  1 
ATOM   2897 C C   . ILE A 1 380 ? -48.367  -2.342  35.370  1.00 50.58  ? 406  ILE A C   1 
ATOM   2898 O O   . ILE A 1 380 ? -49.491  -2.228  35.834  1.00 43.23  ? 406  ILE A O   1 
ATOM   2899 C CB  . ILE A 1 380 ? -48.886  -2.117  32.951  1.00 52.51  ? 406  ILE A CB  1 
ATOM   2900 C CG1 . ILE A 1 380 ? -48.772  -2.814  31.582  1.00 51.01  ? 406  ILE A CG1 1 
ATOM   2901 C CG2 . ILE A 1 380 ? -48.242  -0.737  32.879  1.00 46.65  ? 406  ILE A CG2 1 
ATOM   2902 C CD1 . ILE A 1 380 ? -49.574  -2.168  30.490  1.00 45.28  ? 406  ILE A CD1 1 
ATOM   2903 N N   . LYS A 1 381 ? -47.256  -1.835  35.936  1.00 48.04  ? 407  LYS A N   1 
ATOM   2904 C CA  . LYS A 1 381 ? -47.254  -1.197  37.258  1.00 47.19  ? 407  LYS A CA  1 
ATOM   2905 C C   . LYS A 1 381 ? -47.338  0.302   37.202  1.00 49.99  ? 407  LYS A C   1 
ATOM   2906 O O   . LYS A 1 381 ? -47.817  0.966   38.149  1.00 45.15  ? 407  LYS A O   1 
ATOM   2907 C CB  . LYS A 1 381 ? -45.983  -1.590  38.012  1.00 52.83  ? 407  LYS A CB  1 
ATOM   2908 C CG  . LYS A 1 381 ? -45.848  -3.094  38.229  1.00 61.38  ? 407  LYS A CG  1 
ATOM   2909 C CD  . LYS A 1 381 ? -44.660  -3.446  39.091  1.00 63.30  ? 407  LYS A CD  1 
ATOM   2910 C CE  . LYS A 1 381 ? -44.614  -4.945  39.322  1.00 91.06  ? 407  LYS A CE  1 
ATOM   2911 N NZ  . LYS A 1 381 ? -43.471  -5.397  40.174  1.00 107.89 ? 407  LYS A NZ  1 
ATOM   2912 N N   . GLN A 1 382 ? -46.797  0.844   36.125  1.00 49.26  ? 408  GLN A N   1 
ATOM   2913 C CA  . GLN A 1 382 ? -46.795  2.266   35.909  1.00 52.64  ? 408  GLN A CA  1 
ATOM   2914 C C   . GLN A 1 382 ? -47.060  2.628   34.460  1.00 52.09  ? 408  GLN A C   1 
ATOM   2915 O O   . GLN A 1 382 ? -46.550  1.996   33.520  1.00 49.82  ? 408  GLN A O   1 
ATOM   2916 C CB  . GLN A 1 382 ? -45.445  2.865   36.256  1.00 67.07  ? 408  GLN A CB  1 
ATOM   2917 C CG  . GLN A 1 382 ? -45.105  2.985   37.710  1.00 88.01  ? 408  GLN A CG  1 
ATOM   2918 C CD  . GLN A 1 382 ? -43.759  3.663   37.884  1.00 110.30 ? 408  GLN A CD  1 
ATOM   2919 O OE1 . GLN A 1 382 ? -42.863  3.512   37.050  1.00 121.08 ? 408  GLN A OE1 1 
ATOM   2920 N NE2 . GLN A 1 382 ? -43.599  4.391   38.976  1.00 129.51 ? 408  GLN A NE2 1 
ATOM   2921 N N   . ILE A 1 383 ? -47.755  3.736   34.314  1.00 43.80  ? 409  ILE A N   1 
ATOM   2922 C CA  . ILE A 1 383 ? -48.087  4.290   33.049  1.00 55.31  ? 409  ILE A CA  1 
ATOM   2923 C C   . ILE A 1 383 ? -47.986  5.798   33.080  1.00 48.78  ? 409  ILE A C   1 
ATOM   2924 O O   . ILE A 1 383 ? -48.501  6.438   33.982  1.00 41.99  ? 409  ILE A O   1 
ATOM   2925 C CB  . ILE A 1 383 ? -49.554  3.963   32.653  1.00 58.39  ? 409  ILE A CB  1 
ATOM   2926 C CG1 . ILE A 1 383 ? -49.692  2.482   32.349  1.00 63.14  ? 409  ILE A CG1 1 
ATOM   2927 C CG2 . ILE A 1 383 ? -49.933  4.698   31.380  1.00 62.01  ? 409  ILE A CG2 1 
ATOM   2928 C CD1 . ILE A 1 383 ? -51.067  2.076   31.871  1.00 64.48  ? 409  ILE A CD1 1 
ATOM   2929 N N   . ASP A 1 384 ? -47.381  6.389   32.067  1.00 58.53  ? 410  ASP A N   1 
ATOM   2930 C CA  . ASP A 1 384 ? -47.353  7.846   32.015  1.00 59.17  ? 410  ASP A CA  1 
ATOM   2931 C C   . ASP A 1 384 ? -48.657  8.172   31.246  1.00 54.82  ? 410  ASP A C   1 
ATOM   2932 O O   . ASP A 1 384 ? -48.695  8.094   30.023  1.00 54.90  ? 410  ASP A O   1 
ATOM   2933 C CB  . ASP A 1 384 ? -46.097  8.343   31.296  1.00 70.16  ? 410  ASP A CB  1 
ATOM   2934 C CG  . ASP A 1 384 ? -45.959  9.883   31.317  1.00 96.62  ? 410  ASP A CG  1 
ATOM   2935 O OD1 . ASP A 1 384 ? -46.825  10.588  31.916  1.00 84.70  ? 410  ASP A OD1 1 
ATOM   2936 O OD2 . ASP A 1 384 ? -44.968  10.380  30.727  1.00 107.71 ? 410  ASP A OD2 1 
ATOM   2937 N N   . PHE A 1 385 ? -49.749  8.421   31.960  1.00 51.07  ? 411  PHE A N   1 
ATOM   2938 C CA  . PHE A 1 385 ? -51.050  8.705   31.291  1.00 53.98  ? 411  PHE A CA  1 
ATOM   2939 C C   . PHE A 1 385 ? -51.098  9.864   30.327  1.00 60.84  ? 411  PHE A C   1 
ATOM   2940 O O   . PHE A 1 385 ? -51.966  9.879   29.456  1.00 65.47  ? 411  PHE A O   1 
ATOM   2941 C CB  . PHE A 1 385 ? -52.229  8.854   32.274  1.00 53.95  ? 411  PHE A CB  1 
ATOM   2942 C CG  . PHE A 1 385 ? -52.672  7.569   32.890  1.00 66.62  ? 411  PHE A CG  1 
ATOM   2943 C CD1 . PHE A 1 385 ? -53.505  6.714   32.189  1.00 67.29  ? 411  PHE A CD1 1 
ATOM   2944 C CD2 . PHE A 1 385 ? -52.253  7.200   34.168  1.00 75.47  ? 411  PHE A CD2 1 
ATOM   2945 C CE1 . PHE A 1 385 ? -53.922  5.521   32.752  1.00 68.07  ? 411  PHE A CE1 1 
ATOM   2946 C CE2 . PHE A 1 385 ? -52.662  6.004   34.733  1.00 79.45  ? 411  PHE A CE2 1 
ATOM   2947 C CZ  . PHE A 1 385 ? -53.502  5.166   34.026  1.00 81.68  ? 411  PHE A CZ  1 
ATOM   2948 N N   . LYS A 1 386 ? -50.221  10.855  30.458  1.00 72.39  ? 412  LYS A N   1 
ATOM   2949 C CA  . LYS A 1 386 ? -50.300  11.976  29.501  1.00 80.27  ? 412  LYS A CA  1 
ATOM   2950 C C   . LYS A 1 386 ? -50.105  11.491  28.079  1.00 58.75  ? 412  LYS A C   1 
ATOM   2951 O O   . LYS A 1 386 ? -50.622  12.084  27.173  1.00 60.38  ? 412  LYS A O   1 
ATOM   2952 C CB  . LYS A 1 386 ? -49.288  13.099  29.772  1.00 89.43  ? 412  LYS A CB  1 
ATOM   2953 C CG  . LYS A 1 386 ? -47.822  12.723  29.601  1.00 112.68 ? 412  LYS A CG  1 
ATOM   2954 C CD  . LYS A 1 386 ? -46.925  13.956  29.681  1.00 139.99 ? 412  LYS A CD  1 
ATOM   2955 C CE  . LYS A 1 386 ? -47.098  14.726  30.987  1.00 161.39 ? 412  LYS A CE  1 
ATOM   2956 N NZ  . LYS A 1 386 ? -46.269  15.964  31.022  1.00 174.98 ? 412  LYS A NZ  1 
ATOM   2957 N N   . LEU A 1 387 ? -49.433  10.361  27.895  1.00 54.24  ? 413  LEU A N   1 
ATOM   2958 C CA  . LEU A 1 387 ? -49.180  9.863   26.559  1.00 52.44  ? 413  LEU A CA  1 
ATOM   2959 C C   . LEU A 1 387 ? -50.481  9.660   25.760  1.00 54.56  ? 413  LEU A C   1 
ATOM   2960 O O   . LEU A 1 387 ? -50.487  9.843   24.555  1.00 54.43  ? 413  LEU A O   1 
ATOM   2961 C CB  . LEU A 1 387 ? -48.321  8.592   26.587  1.00 51.55  ? 413  LEU A CB  1 
ATOM   2962 C CG  . LEU A 1 387 ? -48.922  7.239   26.975  1.00 59.65  ? 413  LEU A CG  1 
ATOM   2963 C CD1 . LEU A 1 387 ? -49.697  6.717   25.782  1.00 56.44  ? 413  LEU A CD1 1 
ATOM   2964 C CD2 . LEU A 1 387 ? -47.837  6.225   27.334  1.00 57.29  ? 413  LEU A CD2 1 
ATOM   2965 N N   . PHE A 1 388 ? -51.588  9.352   26.427  1.00 53.61  ? 414  PHE A N   1 
ATOM   2966 C CA  . PHE A 1 388 ? -52.847  9.147   25.702  1.00 54.27  ? 414  PHE A CA  1 
ATOM   2967 C C   . PHE A 1 388 ? -53.442  10.434  25.108  1.00 62.86  ? 414  PHE A C   1 
ATOM   2968 O O   . PHE A 1 388 ? -54.227  10.385  24.155  1.00 68.78  ? 414  PHE A O   1 
ATOM   2969 C CB  . PHE A 1 388 ? -53.878  8.339   26.520  1.00 48.07  ? 414  PHE A CB  1 
ATOM   2970 C CG  . PHE A 1 388 ? -53.448  6.918   26.768  1.00 52.56  ? 414  PHE A CG  1 
ATOM   2971 C CD1 . PHE A 1 388 ? -53.326  6.035   25.711  1.00 51.93  ? 414  PHE A CD1 1 
ATOM   2972 C CD2 . PHE A 1 388 ? -53.169  6.456   28.051  1.00 50.74  ? 414  PHE A CD2 1 
ATOM   2973 C CE1 . PHE A 1 388 ? -52.851  4.742   25.907  1.00 53.58  ? 414  PHE A CE1 1 
ATOM   2974 C CE2 . PHE A 1 388 ? -52.751  5.157   28.259  1.00 53.43  ? 414  PHE A CE2 1 
ATOM   2975 C CZ  . PHE A 1 388 ? -52.617  4.283   27.188  1.00 51.97  ? 414  PHE A CZ  1 
ATOM   2976 N N   . GLN A 1 389 ? -53.033  11.582  25.631  1.00 61.95  ? 415  GLN A N   1 
ATOM   2977 C CA  . GLN A 1 389 ? -53.513  12.854  25.111  1.00 61.46  ? 415  GLN A CA  1 
ATOM   2978 C C   . GLN A 1 389 ? -52.914  13.131  23.756  1.00 58.02  ? 415  GLN A C   1 
ATOM   2979 O O   . GLN A 1 389 ? -53.485  13.855  22.983  1.00 57.96  ? 415  GLN A O   1 
ATOM   2980 C CB  . GLN A 1 389 ? -53.135  14.013  26.015  1.00 59.11  ? 415  GLN A CB  1 
ATOM   2981 C CG  . GLN A 1 389 ? -53.909  14.108  27.303  1.00 72.13  ? 415  GLN A CG  1 
ATOM   2982 C CD  . GLN A 1 389 ? -53.361  15.204  28.200  1.00 74.25  ? 415  GLN A CD  1 
ATOM   2983 O OE1 . GLN A 1 389 ? -52.210  15.601  28.062  1.00 75.46  ? 415  GLN A OE1 1 
ATOM   2984 N NE2 . GLN A 1 389 ? -54.137  15.606  29.193  1.00 81.79  ? 415  GLN A NE2 1 
ATOM   2985 N N   . ASN A 1 390 ? -51.811  12.486  23.429  1.00 59.02  ? 416  ASN A N   1 
ATOM   2986 C CA  . ASN A 1 390 ? -51.176  12.749  22.162  1.00 59.65  ? 416  ASN A CA  1 
ATOM   2987 C C   . ASN A 1 390 ? -51.642  11.813  21.033  1.00 56.50  ? 416  ASN A C   1 
ATOM   2988 O O   . ASN A 1 390 ? -50.833  11.336  20.236  1.00 67.38  ? 416  ASN A O   1 
ATOM   2989 C CB  . ASN A 1 390 ? -49.647  12.720  22.350  1.00 67.88  ? 416  ASN A CB  1 
ATOM   2990 C CG  . ASN A 1 390 ? -48.903  13.397  21.210  1.00 80.95  ? 416  ASN A CG  1 
ATOM   2991 O OD1 . ASN A 1 390 ? -49.501  14.017  20.330  1.00 78.95  ? 416  ASN A OD1 1 
ATOM   2992 N ND2 . ASN A 1 390 ? -47.602  13.328  21.249  1.00 98.43  ? 416  ASN A ND2 1 
ATOM   2993 N N   . PHE A 1 391 ? -52.953  11.581  20.950  1.00 54.72  ? 417  PHE A N   1 
ATOM   2994 C CA  . PHE A 1 391 ? -53.527  10.700  19.913  1.00 48.74  ? 417  PHE A CA  1 
ATOM   2995 C C   . PHE A 1 391 ? -54.700  11.379  19.220  1.00 56.37  ? 417  PHE A C   1 
ATOM   2996 O O   . PHE A 1 391 ? -55.608  11.893  19.857  1.00 64.00  ? 417  PHE A O   1 
ATOM   2997 C CB  . PHE A 1 391 ? -54.010  9.347   20.512  1.00 54.44  ? 417  PHE A CB  1 
ATOM   2998 C CG  . PHE A 1 391 ? -52.902  8.378   20.842  1.00 47.73  ? 417  PHE A CG  1 
ATOM   2999 C CD1 . PHE A 1 391 ? -52.226  8.454   22.019  1.00 56.51  ? 417  PHE A CD1 1 
ATOM   3000 C CD2 . PHE A 1 391 ? -52.606  7.354   20.003  1.00 51.29  ? 417  PHE A CD2 1 
ATOM   3001 C CE1 . PHE A 1 391 ? -51.188  7.583   22.296  1.00 53.00  ? 417  PHE A CE1 1 
ATOM   3002 C CE2 . PHE A 1 391 ? -51.592  6.465   20.289  1.00 55.89  ? 417  PHE A CE2 1 
ATOM   3003 C CZ  . PHE A 1 391 ? -50.909  6.569   21.466  1.00 49.89  ? 417  PHE A CZ  1 
ATOM   3004 N N   . SER A 1 392 ? -54.753  11.234  17.915  1.00 57.21  ? 418  SER A N   1 
ATOM   3005 C CA  . SER A 1 392 ? -55.796  11.852  17.132  1.00 71.58  ? 418  SER A CA  1 
ATOM   3006 C C   . SER A 1 392 ? -57.194  11.300  17.449  1.00 68.30  ? 418  SER A C   1 
ATOM   3007 O O   . SER A 1 392 ? -58.087  12.041  17.809  1.00 68.31  ? 418  SER A O   1 
ATOM   3008 C CB  . SER A 1 392 ? -55.539  11.576  15.624  1.00 81.14  ? 418  SER A CB  1 
ATOM   3009 O OG  . SER A 1 392 ? -54.172  11.719  15.261  1.00 78.00  ? 418  SER A OG  1 
ATOM   3010 N N   . ASN A 1 393 ? -57.357  9.981   17.348  1.00 66.17  ? 419  ASN A N   1 
ATOM   3011 C CA  . ASN A 1 393 ? -58.671  9.366   17.527  1.00 66.55  ? 419  ASN A CA  1 
ATOM   3012 C C   . ASN A 1 393 ? -58.994  8.305   18.572  1.00 57.52  ? 419  ASN A C   1 
ATOM   3013 O O   . ASN A 1 393 ? -59.951  7.593   18.385  1.00 49.66  ? 419  ASN A O   1 
ATOM   3014 C CB  . ASN A 1 393 ? -59.106  8.813   16.168  1.00 72.30  ? 419  ASN A CB  1 
ATOM   3015 C CG  . ASN A 1 393 ? -59.514  9.896   15.216  1.00 82.08  ? 419  ASN A CG  1 
ATOM   3016 O OD1 . ASN A 1 393 ? -60.151  10.865  15.613  1.00 84.82  ? 419  ASN A OD1 1 
ATOM   3017 N ND2 . ASN A 1 393 ? -59.275  9.675   13.934  1.00 101.91 ? 419  ASN A ND2 1 
ATOM   3018 N N   . LEU A 1 394 ? -58.239  8.179   19.653  1.00 58.53  ? 420  LEU A N   1 
ATOM   3019 C CA  . LEU A 1 394 ? -58.588  7.184   20.657  1.00 47.65  ? 420  LEU A CA  1 
ATOM   3020 C C   . LEU A 1 394 ? -59.978  7.299   21.233  1.00 50.55  ? 420  LEU A C   1 
ATOM   3021 O O   . LEU A 1 394 ? -60.368  8.341   21.747  1.00 53.84  ? 420  LEU A O   1 
ATOM   3022 C CB  . LEU A 1 394 ? -57.643  7.197   21.827  1.00 47.37  ? 420  LEU A CB  1 
ATOM   3023 C CG  . LEU A 1 394 ? -56.324  6.540   21.558  1.00 55.80  ? 420  LEU A CG  1 
ATOM   3024 C CD1 . LEU A 1 394 ? -55.489  6.595   22.819  1.00 55.64  ? 420  LEU A CD1 1 
ATOM   3025 C CD2 . LEU A 1 394 ? -56.591  5.103   21.155  1.00 56.42  ? 420  LEU A CD2 1 
ATOM   3026 N N   . GLU A 1 395 ? -60.717  6.199   21.153  1.00 52.81  ? 421  GLU A N   1 
ATOM   3027 C CA  . GLU A 1 395 ? -62.038  6.127   21.733  1.00 59.66  ? 421  GLU A CA  1 
ATOM   3028 C C   . GLU A 1 395 ? -62.091  5.053   22.825  1.00 53.07  ? 421  GLU A C   1 
ATOM   3029 O O   . GLU A 1 395 ? -62.938  5.123   23.726  1.00 51.32  ? 421  GLU A O   1 
ATOM   3030 C CB  . GLU A 1 395 ? -63.100  5.893   20.668  1.00 59.61  ? 421  GLU A CB  1 
ATOM   3031 C CG  . GLU A 1 395 ? -63.301  7.125   19.833  1.00 67.77  ? 421  GLU A CG  1 
ATOM   3032 C CD  . GLU A 1 395 ? -63.769  8.297   20.681  1.00 85.25  ? 421  GLU A CD  1 
ATOM   3033 O OE1 . GLU A 1 395 ? -64.819  8.169   21.386  1.00 84.08  ? 421  GLU A OE1 1 
ATOM   3034 O OE2 . GLU A 1 395 ? -63.143  9.378   20.569  1.00 90.72  ? 421  GLU A OE2 1 
ATOM   3035 N N   . ILE A 1 396 ? -61.156  4.100   22.759  1.00 47.04  ? 422  ILE A N   1 
ATOM   3036 C CA  . ILE A 1 396 ? -61.085  3.002   23.694  1.00 43.02  ? 422  ILE A CA  1 
ATOM   3037 C C   . ILE A 1 396 ? -59.697  2.672   24.129  1.00 44.26  ? 422  ILE A C   1 
ATOM   3038 O O   . ILE A 1 396 ? -58.864  2.250   23.306  1.00 40.61  ? 422  ILE A O   1 
ATOM   3039 C CB  . ILE A 1 396 ? -61.677  1.745   23.086  1.00 52.25  ? 422  ILE A CB  1 
ATOM   3040 C CG1 . ILE A 1 396 ? -63.186  1.936   22.934  1.00 54.58  ? 422  ILE A CG1 1 
ATOM   3041 C CG2 . ILE A 1 396 ? -61.412  0.555   24.006  1.00 54.06  ? 422  ILE A CG2 1 
ATOM   3042 C CD1 . ILE A 1 396 ? -63.878  0.767   22.311  1.00 54.56  ? 422  ILE A CD1 1 
ATOM   3043 N N   . ILE A 1 397 ? -59.468  2.839   25.440  1.00 42.31  ? 423  ILE A N   1 
ATOM   3044 C CA  . ILE A 1 397 ? -58.174  2.553   26.093  1.00 43.57  ? 423  ILE A CA  1 
ATOM   3045 C C   . ILE A 1 397 ? -58.458  1.389   27.077  1.00 45.75  ? 423  ILE A C   1 
ATOM   3046 O O   . ILE A 1 397 ? -59.047  1.571   28.153  1.00 36.71  ? 423  ILE A O   1 
ATOM   3047 C CB  . ILE A 1 397 ? -57.677  3.767   26.869  1.00 46.31  ? 423  ILE A CB  1 
ATOM   3048 C CG1 . ILE A 1 397 ? -57.670  5.001   25.958  1.00 53.68  ? 423  ILE A CG1 1 
ATOM   3049 C CG2 . ILE A 1 397 ? -56.298  3.485   27.441  1.00 52.70  ? 423  ILE A CG2 1 
ATOM   3050 C CD1 . ILE A 1 397 ? -57.240  6.296   26.622  1.00 52.46  ? 423  ILE A CD1 1 
ATOM   3051 N N   . TYR A 1 398 ? -58.096  0.189   26.673  1.00 45.67  ? 424  TYR A N   1 
ATOM   3052 C CA  . TYR A 1 398 ? -58.376  -0.967  27.480  1.00 44.20  ? 424  TYR A CA  1 
ATOM   3053 C C   . TYR A 1 398 ? -57.166  -1.381  28.272  1.00 46.10  ? 424  TYR A C   1 
ATOM   3054 O O   . TYR A 1 398 ? -56.177  -1.889  27.727  1.00 44.58  ? 424  TYR A O   1 
ATOM   3055 C CB  . TYR A 1 398 ? -58.887  -2.108  26.579  1.00 48.37  ? 424  TYR A CB  1 
ATOM   3056 C CG  . TYR A 1 398 ? -59.476  -3.256  27.357  1.00 51.63  ? 424  TYR A CG  1 
ATOM   3057 C CD1 . TYR A 1 398 ? -60.732  -3.142  27.914  1.00 52.12  ? 424  TYR A CD1 1 
ATOM   3058 C CD2 . TYR A 1 398 ? -58.800  -4.459  27.504  1.00 50.64  ? 424  TYR A CD2 1 
ATOM   3059 C CE1 . TYR A 1 398 ? -61.247  -4.132  28.716  1.00 49.32  ? 424  TYR A CE1 1 
ATOM   3060 C CE2 . TYR A 1 398 ? -59.332  -5.481  28.248  1.00 48.66  ? 424  TYR A CE2 1 
ATOM   3061 C CZ  . TYR A 1 398 ? -60.561  -5.313  28.854  1.00 52.46  ? 424  TYR A CZ  1 
ATOM   3062 O OH  . TYR A 1 398 ? -61.139  -6.332  29.593  1.00 49.97  ? 424  TYR A OH  1 
ATOM   3063 N N   . LEU A 1 399 ? -57.267  -1.200  29.581  1.00 45.28  ? 425  LEU A N   1 
ATOM   3064 C CA  . LEU A 1 399 ? -56.184  -1.541  30.491  1.00 46.26  ? 425  LEU A CA  1 
ATOM   3065 C C   . LEU A 1 399 ? -56.604  -2.537  31.637  1.00 42.82  ? 425  LEU A C   1 
ATOM   3066 O O   . LEU A 1 399 ? -56.003  -2.566  32.687  1.00 37.64  ? 425  LEU A O   1 
ATOM   3067 C CB  . LEU A 1 399 ? -55.656  -0.249  31.095  1.00 41.56  ? 425  LEU A CB  1 
ATOM   3068 C CG  . LEU A 1 399 ? -54.951  0.733   30.189  1.00 45.12  ? 425  LEU A CG  1 
ATOM   3069 C CD1 . LEU A 1 399 ? -54.754  2.055   30.905  1.00 45.96  ? 425  LEU A CD1 1 
ATOM   3070 C CD2 . LEU A 1 399 ? -53.620  0.198   29.727  1.00 47.55  ? 425  LEU A CD2 1 
ATOM   3071 N N   . SER A 1 400 ? -57.555  -3.408  31.391  1.00 42.74  ? 426  SER A N   1 
ATOM   3072 C CA  . SER A 1 400 ? -57.975  -4.315  32.432  1.00 42.40  ? 426  SER A CA  1 
ATOM   3073 C C   . SER A 1 400 ? -56.902  -5.326  32.739  1.00 41.23  ? 426  SER A C   1 
ATOM   3074 O O   . SER A 1 400 ? -56.133  -5.715  31.869  1.00 41.51  ? 426  SER A O   1 
ATOM   3075 C CB  . SER A 1 400 ? -59.242  -5.044  32.032  1.00 44.65  ? 426  SER A CB  1 
ATOM   3076 O OG  . SER A 1 400 ? -59.770  -5.758  33.130  1.00 49.31  ? 426  SER A OG  1 
ATOM   3077 N N   . GLU A 1 401 ? -56.835  -5.737  33.993  1.00 40.91  ? 427  GLU A N   1 
ATOM   3078 C CA  . GLU A 1 401 ? -55.851  -6.727  34.428  1.00 43.83  ? 427  GLU A CA  1 
ATOM   3079 C C   . GLU A 1 401 ? -54.410  -6.246  34.302  1.00 39.10  ? 427  GLU A C   1 
ATOM   3080 O O   . GLU A 1 401 ? -53.539  -6.849  33.649  1.00 42.76  ? 427  GLU A O   1 
ATOM   3081 C CB  . GLU A 1 401 ? -56.036  -8.096  33.767  1.00 38.51  ? 427  GLU A CB  1 
ATOM   3082 C CG  . GLU A 1 401 ? -57.432  -8.642  33.970  1.00 51.27  ? 427  GLU A CG  1 
ATOM   3083 C CD  . GLU A 1 401 ? -57.599  -10.078 33.437  1.00 65.74  ? 427  GLU A CD  1 
ATOM   3084 O OE1 . GLU A 1 401 ? -56.900  -11.000 33.918  1.00 72.16  ? 427  GLU A OE1 1 
ATOM   3085 O OE2 . GLU A 1 401 ? -58.536  -10.318 32.655  1.00 65.71  ? 427  GLU A OE2 1 
ATOM   3086 N N   . ASN A 1 402 ? -54.179  -5.117  34.898  1.00 41.33  ? 428  ASN A N   1 
ATOM   3087 C CA  . ASN A 1 402 ? -52.837  -4.580  34.965  1.00 48.96  ? 428  ASN A CA  1 
ATOM   3088 C C   . ASN A 1 402 ? -52.601  -4.295  36.428  1.00 45.14  ? 428  ASN A C   1 
ATOM   3089 O O   . ASN A 1 402 ? -53.482  -4.576  37.246  1.00 40.88  ? 428  ASN A O   1 
ATOM   3090 C CB  . ASN A 1 402 ? -52.678  -3.394  34.031  1.00 40.17  ? 428  ASN A CB  1 
ATOM   3091 C CG  . ASN A 1 402 ? -52.516  -3.854  32.624  1.00 42.23  ? 428  ASN A CG  1 
ATOM   3092 O OD1 . ASN A 1 402 ? -51.458  -4.402  32.272  1.00 38.87  ? 428  ASN A OD1 1 
ATOM   3093 N ND2 . ASN A 1 402 ? -53.537  -3.617  31.783  1.00 43.53  ? 428  ASN A ND2 1 
ATOM   3094 N N   . ARG A 1 403 ? -51.474  -3.694  36.768  1.00 46.42  ? 429  ARG A N   1 
ATOM   3095 C CA  . ARG A 1 403 ? -51.201  -3.439  38.161  1.00 46.14  ? 429  ARG A CA  1 
ATOM   3096 C C   . ARG A 1 403 ? -51.103  -1.980  38.569  1.00 49.04  ? 429  ARG A C   1 
ATOM   3097 O O   . ARG A 1 403 ? -50.253  -1.613  39.390  1.00 41.78  ? 429  ARG A O   1 
ATOM   3098 C CB  . ARG A 1 403 ? -49.959  -4.199  38.586  1.00 46.63  ? 429  ARG A CB  1 
ATOM   3099 C CG  . ARG A 1 403 ? -50.026  -5.688  38.238  1.00 53.07  ? 429  ARG A CG  1 
ATOM   3100 C CD  . ARG A 1 403 ? -49.253  -6.437  39.301  1.00 70.02  ? 429  ARG A CD  1 
ATOM   3101 N NE  . ARG A 1 403 ? -50.010  -6.255  40.545  1.00 69.36  ? 429  ARG A NE  1 
ATOM   3102 C CZ  . ARG A 1 403 ? -49.560  -6.477  41.767  1.00 66.32  ? 429  ARG A CZ  1 
ATOM   3103 N NH1 . ARG A 1 403 ? -48.272  -6.764  41.985  1.00 80.02  ? 429  ARG A NH1 1 
ATOM   3104 N NH2 . ARG A 1 403 ? -50.380  -6.248  42.777  1.00 67.25  ? 429  ARG A NH2 1 
ATOM   3105 N N   . ILE A 1 404 ? -51.988  -1.152  38.029  1.00 46.45  ? 430  ILE A N   1 
ATOM   3106 C CA  . ILE A 1 404 ? -51.980  0.256   38.392  1.00 51.22  ? 430  ILE A CA  1 
ATOM   3107 C C   . ILE A 1 404 ? -52.360  0.336   39.862  1.00 42.87  ? 430  ILE A C   1 
ATOM   3108 O O   . ILE A 1 404 ? -53.384  -0.195  40.268  1.00 44.98  ? 430  ILE A O   1 
ATOM   3109 C CB  . ILE A 1 404 ? -52.907  1.134   37.486  1.00 49.78  ? 430  ILE A CB  1 
ATOM   3110 C CG1 . ILE A 1 404 ? -52.237  1.428   36.178  1.00 50.40  ? 430  ILE A CG1 1 
ATOM   3111 C CG2 . ILE A 1 404 ? -53.068  2.534   38.051  1.00 49.23  ? 430  ILE A CG2 1 
ATOM   3112 C CD1 . ILE A 1 404 ? -51.850  0.215   35.447  1.00 61.14  ? 430  ILE A CD1 1 
ATOM   3113 N N   . SER A 1 405 ? -51.584  1.130   40.593  1.00 50.28  ? 431  SER A N   1 
ATOM   3114 C CA  . SER A 1 405 ? -51.718  1.359   42.032  1.00 50.57  ? 431  SER A CA  1 
ATOM   3115 C C   . SER A 1 405 ? -52.169  2.765   42.285  1.00 52.92  ? 431  SER A C   1 
ATOM   3116 O O   . SER A 1 405 ? -52.071  3.606   41.403  1.00 54.99  ? 431  SER A O   1 
ATOM   3117 C CB  . SER A 1 405 ? -50.337  1.344   42.637  1.00 46.05  ? 431  SER A CB  1 
ATOM   3118 O OG  . SER A 1 405 ? -49.571  0.336   42.023  1.00 54.06  ? 431  SER A OG  1 
ATOM   3119 N N   . PRO A 1 406 ? -52.484  3.067   43.543  1.00 45.08  ? 432  PRO A N   1 
ATOM   3120 C CA  . PRO A 1 406 ? -52.885  4.407   43.873  1.00 52.39  ? 432  PRO A CA  1 
ATOM   3121 C C   . PRO A 1 406 ? -51.689  5.310   43.654  1.00 57.15  ? 432  PRO A C   1 
ATOM   3122 O O   . PRO A 1 406 ? -50.571  4.899   43.929  1.00 51.16  ? 432  PRO A O   1 
ATOM   3123 C CB  . PRO A 1 406 ? -53.238  4.327   45.369  1.00 45.08  ? 432  PRO A CB  1 
ATOM   3124 C CG  . PRO A 1 406 ? -53.523  2.903   45.615  1.00 44.57  ? 432  PRO A CG  1 
ATOM   3125 C CD  . PRO A 1 406 ? -52.639  2.148   44.670  1.00 43.59  ? 432  PRO A CD  1 
ATOM   3126 N N   . LEU A 1 407 ? -51.939  6.511   43.127  1.00 73.47  ? 433  LEU A N   1 
ATOM   3127 C CA  . LEU A 1 407 ? -50.893  7.491   42.825  1.00 80.41  ? 433  LEU A CA  1 
ATOM   3128 C C   . LEU A 1 407 ? -50.913  8.662   43.819  1.00 94.03  ? 433  LEU A C   1 
ATOM   3129 O O   . LEU A 1 407 ? -51.854  9.462   43.854  1.00 82.62  ? 433  LEU A O   1 
ATOM   3130 C CB  . LEU A 1 407 ? -51.028  7.985   41.363  1.00 76.14  ? 433  LEU A CB  1 
ATOM   3131 C CG  . LEU A 1 407 ? -50.878  6.932   40.227  1.00 81.48  ? 433  LEU A CG  1 
ATOM   3132 C CD1 . LEU A 1 407 ? -51.236  7.461   38.833  1.00 74.68  ? 433  LEU A CD1 1 
ATOM   3133 C CD2 . LEU A 1 407 ? -49.486  6.306   40.188  1.00 80.41  ? 433  LEU A CD2 1 
ATOM   3134 N N   . VAL A 1 408 ? -49.850  8.731   44.621  1.00 118.01 ? 434  VAL A N   1 
ATOM   3135 C CA  . VAL A 1 408 ? -49.663  9.762   45.643  1.00 121.47 ? 434  VAL A CA  1 
ATOM   3136 C C   . VAL A 1 408 ? -48.529  10.715  45.249  1.00 113.63 ? 434  VAL A C   1 
ATOM   3137 O O   . VAL A 1 408 ? -48.738  11.700  44.544  1.00 93.21  ? 434  VAL A O   1 
ATOM   3138 C CB  . VAL A 1 408 ? -49.299  9.113   46.997  1.00 119.23 ? 434  VAL A CB  1 
ATOM   3139 C CG1 . VAL A 1 408 ? -48.978  10.175  48.039  1.00 123.25 ? 434  VAL A CG1 1 
ATOM   3140 C CG2 . VAL A 1 408 ? -50.423  8.203   47.467  1.00 107.50 ? 434  VAL A CG2 1 
ATOM   3141 N N   . ASN A 1 417 ? -38.742  -5.549  39.435  1.00 107.90 ? 443  ASN A N   1 
ATOM   3142 C CA  . ASN A 1 417 ? -38.457  -6.987  39.391  1.00 110.64 ? 443  ASN A CA  1 
ATOM   3143 C C   . ASN A 1 417 ? -37.626  -7.324  38.150  1.00 105.95 ? 443  ASN A C   1 
ATOM   3144 O O   . ASN A 1 417 ? -37.115  -6.429  37.469  1.00 114.03 ? 443  ASN A O   1 
ATOM   3145 C CB  . ASN A 1 417 ? -39.767  -7.785  39.356  1.00 95.54  ? 443  ASN A CB  1 
ATOM   3146 C CG  . ASN A 1 417 ? -40.728  -7.379  40.454  1.00 91.99  ? 443  ASN A CG  1 
ATOM   3147 O OD1 . ASN A 1 417 ? -40.462  -6.476  41.240  1.00 104.84 ? 443  ASN A OD1 1 
ATOM   3148 N ND2 . ASN A 1 417 ? -41.851  -8.044  40.506  1.00 92.74  ? 443  ASN A ND2 1 
ATOM   3149 N N   . SER A 1 418 ? -37.516  -8.613  37.847  1.00 103.19 ? 444  SER A N   1 
ATOM   3150 C CA  . SER A 1 418 ? -36.749  -9.075  36.688  1.00 101.01 ? 444  SER A CA  1 
ATOM   3151 C C   . SER A 1 418 ? -37.490  -10.188 35.927  1.00 94.76  ? 444  SER A C   1 
ATOM   3152 O O   . SER A 1 418 ? -37.319  -10.348 34.715  1.00 96.16  ? 444  SER A O   1 
ATOM   3153 C CB  . SER A 1 418 ? -35.402  -9.618  37.175  1.00 101.16 ? 444  SER A CB  1 
ATOM   3154 O OG  . SER A 1 418 ? -34.749  -8.683  38.032  1.00 94.76  ? 444  SER A OG  1 
ATOM   3155 N N   . SER A 1 419 ? -38.363  -10.897 36.646  1.00 91.06  ? 445  SER A N   1 
ATOM   3156 C CA  . SER A 1 419 ? -39.124  -12.002 36.110  1.00 79.87  ? 445  SER A CA  1 
ATOM   3157 C C   . SER A 1 419 ? -40.560  -11.996 36.580  1.00 77.85  ? 445  SER A C   1 
ATOM   3158 O O   . SER A 1 419 ? -40.932  -11.169 37.414  1.00 76.49  ? 445  SER A O   1 
ATOM   3159 C CB  . SER A 1 419 ? -38.493  -13.297 36.587  1.00 92.25  ? 445  SER A CB  1 
ATOM   3160 O OG  . SER A 1 419 ? -39.262  -14.408 36.149  1.00 111.37 ? 445  SER A OG  1 
ATOM   3161 N N   . SER A 1 420 ? -41.349  -12.954 36.072  1.00 84.20  ? 446  SER A N   1 
ATOM   3162 C CA  . SER A 1 420 ? -42.782  -13.099 36.431  1.00 100.76 ? 446  SER A CA  1 
ATOM   3163 C C   . SER A 1 420 ? -43.253  -14.531 36.150  1.00 102.52 ? 446  SER A C   1 
ATOM   3164 O O   . SER A 1 420 ? -42.508  -15.351 35.608  1.00 81.94  ? 446  SER A O   1 
ATOM   3165 C CB  . SER A 1 420 ? -43.665  -12.108 35.621  1.00 106.07 ? 446  SER A CB  1 
ATOM   3166 O OG  . SER A 1 420 ? -45.046  -12.145 36.009  1.00 91.67  ? 446  SER A OG  1 
ATOM   3167 N N   . PHE A 1 421 ? -44.473  -14.838 36.579  1.00 108.41 ? 447  PHE A N   1 
ATOM   3168 C CA  . PHE A 1 421 ? -45.055  -16.143 36.331  1.00 122.82 ? 447  PHE A CA  1 
ATOM   3169 C C   . PHE A 1 421 ? -46.467  -16.009 35.754  1.00 129.15 ? 447  PHE A C   1 
ATOM   3170 O O   . PHE A 1 421 ? -47.458  -16.123 36.478  1.00 150.04 ? 447  PHE A O   1 
ATOM   3171 C CB  . PHE A 1 421 ? -45.071  -17.035 37.575  1.00 140.59 ? 447  PHE A CB  1 
ATOM   3172 C CG  . PHE A 1 421 ? -45.728  -18.376 37.338  1.00 167.79 ? 447  PHE A CG  1 
ATOM   3173 C CD1 . PHE A 1 421 ? -44.999  -19.446 36.825  1.00 173.93 ? 447  PHE A CD1 1 
ATOM   3174 C CD2 . PHE A 1 421 ? -47.091  -18.549 37.569  1.00 171.78 ? 447  PHE A CD2 1 
ATOM   3175 C CE1 . PHE A 1 421 ? -45.611  -20.665 36.575  1.00 176.09 ? 447  PHE A CE1 1 
ATOM   3176 C CE2 . PHE A 1 421 ? -47.705  -19.763 37.317  1.00 177.32 ? 447  PHE A CE2 1 
ATOM   3177 C CZ  . PHE A 1 421 ? -46.963  -20.825 36.826  1.00 175.84 ? 447  PHE A CZ  1 
ATOM   3178 N N   . GLN A 1 422 ? -46.541  -15.667 34.469  1.00 115.53 ? 448  GLN A N   1 
ATOM   3179 C CA  . GLN A 1 422 ? -47.815  -15.557 33.760  1.00 100.81 ? 448  GLN A CA  1 
ATOM   3180 C C   . GLN A 1 422 ? -48.093  -16.914 33.113  1.00 103.15 ? 448  GLN A C   1 
ATOM   3181 O O   . GLN A 1 422 ? -47.200  -17.520 32.522  1.00 83.94  ? 448  GLN A O   1 
ATOM   3182 C CB  . GLN A 1 422 ? -47.783  -14.426 32.698  1.00 104.37 ? 448  GLN A CB  1 
ATOM   3183 C CG  . GLN A 1 422 ? -48.916  -14.419 31.631  1.00 89.90  ? 448  GLN A CG  1 
ATOM   3184 C CD  . GLN A 1 422 ? -50.339  -14.318 32.186  1.00 91.23  ? 448  GLN A CD  1 
ATOM   3185 O OE1 . GLN A 1 422 ? -51.316  -14.364 31.433  1.00 72.33  ? 448  GLN A OE1 1 
ATOM   3186 N NE2 . GLN A 1 422 ? -50.462  -14.191 33.497  1.00 84.73  ? 448  GLN A NE2 1 
ATOM   3187 N N   . ARG A 1 423 ? -49.301  -17.426 33.333  1.00 110.80 ? 449  ARG A N   1 
ATOM   3188 C CA  . ARG A 1 423 ? -49.737  -18.696 32.766  1.00 116.98 ? 449  ARG A CA  1 
ATOM   3189 C C   . ARG A 1 423 ? -51.089  -18.444 32.128  1.00 118.43 ? 449  ARG A C   1 
ATOM   3190 O O   . ARG A 1 423 ? -52.028  -18.016 32.806  1.00 119.32 ? 449  ARG A O   1 
ATOM   3191 C CB  . ARG A 1 423 ? -49.857  -19.791 33.843  1.00 140.13 ? 449  ARG A CB  1 
ATOM   3192 C CG  . ARG A 1 423 ? -50.736  -19.419 35.038  1.00 151.06 ? 449  ARG A CG  1 
ATOM   3193 C CD  . ARG A 1 423 ? -50.980  -20.595 35.976  1.00 149.64 ? 449  ARG A CD  1 
ATOM   3194 N NE  . ARG A 1 423 ? -51.687  -20.189 37.197  1.00 142.67 ? 449  ARG A NE  1 
ATOM   3195 C CZ  . ARG A 1 423 ? -52.118  -21.027 38.144  1.00 142.38 ? 449  ARG A CZ  1 
ATOM   3196 N NH1 . ARG A 1 423 ? -52.004  -22.342 37.987  1.00 135.52 ? 449  ARG A NH1 1 
ATOM   3197 N NH2 . ARG A 1 423 ? -52.729  -20.553 39.225  1.00 142.78 ? 449  ARG A NH2 1 
ATOM   3198 N N   . HIS A 1 424 ? -51.178  -18.641 30.818  1.00 102.85 ? 450  HIS A N   1 
ATOM   3199 C CA  . HIS A 1 424 ? -52.442  -18.424 30.119  1.00 113.65 ? 450  HIS A CA  1 
ATOM   3200 C C   . HIS A 1 424 ? -53.294  -19.716 30.082  1.00 112.11 ? 450  HIS A C   1 
ATOM   3201 O O   . HIS A 1 424 ? -52.750  -20.815 30.061  1.00 112.75 ? 450  HIS A O   1 
ATOM   3202 C CB  . HIS A 1 424 ? -52.189  -17.840 28.707  1.00 101.83 ? 450  HIS A CB  1 
ATOM   3203 C CG  . HIS A 1 424 ? -53.434  -17.691 27.886  1.00 100.84 ? 450  HIS A CG  1 
ATOM   3204 N ND1 . HIS A 1 424 ? -54.359  -16.691 28.107  1.00 94.37  ? 450  HIS A ND1 1 
ATOM   3205 C CD2 . HIS A 1 424 ? -53.910  -18.420 26.845  1.00 95.42  ? 450  HIS A CD2 1 
ATOM   3206 C CE1 . HIS A 1 424 ? -55.369  -16.833 27.264  1.00 95.33  ? 450  HIS A CE1 1 
ATOM   3207 N NE2 . HIS A 1 424 ? -55.122  -17.875 26.488  1.00 92.44  ? 450  HIS A NE2 1 
ATOM   3208 N N   . ILE A 1 425 ? -54.622  -19.570 30.175  1.00 113.62 ? 451  ILE A N   1 
ATOM   3209 C CA  . ILE A 1 425 ? -55.550  -20.721 30.139  1.00 119.90 ? 451  ILE A CA  1 
ATOM   3210 C C   . ILE A 1 425 ? -56.864  -20.340 29.464  1.00 98.40  ? 451  ILE A C   1 
ATOM   3211 O O   . ILE A 1 425 ? -56.976  -20.401 28.250  1.00 90.48  ? 451  ILE A O   1 
ATOM   3212 C CB  . ILE A 1 425 ? -55.835  -21.317 31.556  1.00 132.80 ? 451  ILE A CB  1 
ATOM   3213 C CG1 . ILE A 1 425 ? -56.671  -20.373 32.456  1.00 123.55 ? 451  ILE A CG1 1 
ATOM   3214 C CG2 . ILE A 1 425 ? -54.536  -21.732 32.241  1.00 137.67 ? 451  ILE A CG2 1 
ATOM   3215 C CD1 . ILE A 1 425 ? -58.129  -20.201 32.054  1.00 119.19 ? 451  ILE A CD1 1 
ATOM   3216 N N   . PRO A 1 437 ? -68.489  -24.341 17.749  1.00 115.21 ? 463  PRO A N   1 
ATOM   3217 C CA  . PRO A 1 437 ? -68.011  -23.100 17.156  1.00 128.28 ? 463  PRO A CA  1 
ATOM   3218 C C   . PRO A 1 437 ? -67.054  -23.325 15.968  1.00 134.26 ? 463  PRO A C   1 
ATOM   3219 O O   . PRO A 1 437 ? -66.108  -24.101 16.104  1.00 129.00 ? 463  PRO A O   1 
ATOM   3220 C CB  . PRO A 1 437 ? -67.266  -22.440 18.319  1.00 115.88 ? 463  PRO A CB  1 
ATOM   3221 C CG  . PRO A 1 437 ? -68.000  -22.886 19.532  1.00 110.89 ? 463  PRO A CG  1 
ATOM   3222 C CD  . PRO A 1 437 ? -68.490  -24.279 19.225  1.00 117.05 ? 463  PRO A CD  1 
ATOM   3223 N N   . HIS A 1 438 ? -67.317  -22.748 14.790  1.00 126.65 ? 464  HIS A N   1 
ATOM   3224 C CA  . HIS A 1 438 ? -68.483  -21.899 14.461  1.00 134.42 ? 464  HIS A CA  1 
ATOM   3225 C C   . HIS A 1 438 ? -68.324  -20.460 15.008  1.00 129.24 ? 464  HIS A C   1 
ATOM   3226 O O   . HIS A 1 438 ? -69.171  -19.582 14.769  1.00 105.55 ? 464  HIS A O   1 
ATOM   3227 C CB  . HIS A 1 438 ? -69.785  -22.516 14.968  1.00 140.45 ? 464  HIS A CB  1 
ATOM   3228 C CG  . HIS A 1 438 ? -70.914  -22.388 14.002  1.00 143.05 ? 464  HIS A CG  1 
ATOM   3229 N ND1 . HIS A 1 438 ? -71.572  -21.203 13.744  1.00 148.65 ? 464  HIS A ND1 1 
ATOM   3230 C CD2 . HIS A 1 438 ? -71.490  -23.320 13.208  1.00 137.86 ? 464  HIS A CD2 1 
ATOM   3231 C CE1 . HIS A 1 438 ? -72.496  -21.412 12.821  1.00 148.17 ? 464  HIS A CE1 1 
ATOM   3232 N NE2 . HIS A 1 438 ? -72.469  -22.689 12.485  1.00 148.21 ? 464  HIS A NE2 1 
ATOM   3233 N N   . SER A 1 439 ? -67.280  -20.268 15.793  1.00 132.13 ? 465  SER A N   1 
ATOM   3234 C CA  . SER A 1 439 ? -66.974  -18.973 16.350  1.00 120.46 ? 465  SER A CA  1 
ATOM   3235 C C   . SER A 1 439 ? -65.491  -18.907 16.630  1.00 121.11 ? 465  SER A C   1 
ATOM   3236 O O   . SER A 1 439 ? -64.821  -19.929 16.662  1.00 113.01 ? 465  SER A O   1 
ATOM   3237 C CB  . SER A 1 439 ? -67.803  -18.705 17.603  1.00 118.03 ? 465  SER A CB  1 
ATOM   3238 O OG  . SER A 1 439 ? -67.106  -19.017 18.791  1.00 126.04 ? 465  SER A OG  1 
ATOM   3239 N N   . ASN A 1 440 ? -65.019  -17.681 16.794  1.00 120.09 ? 466  ASN A N   1 
ATOM   3240 C CA  . ASN A 1 440 ? -63.637  -17.307 17.065  1.00 120.96 ? 466  ASN A CA  1 
ATOM   3241 C C   . ASN A 1 440 ? -63.284  -16.092 16.231  1.00 135.52 ? 466  ASN A C   1 
ATOM   3242 O O   . ASN A 1 440 ? -64.102  -15.201 16.072  1.00 161.45 ? 466  ASN A O   1 
ATOM   3243 C CB  . ASN A 1 440 ? -62.604  -18.435 16.977  1.00 107.38 ? 466  ASN A CB  1 
ATOM   3244 C CG  . ASN A 1 440 ? -61.983  -18.767 18.322  1.00 99.77  ? 466  ASN A CG  1 
ATOM   3245 O OD1 . ASN A 1 440 ? -61.221  -19.714 18.437  1.00 98.75  ? 466  ASN A OD1 1 
ATOM   3246 N ND2 . ASN A 1 440 ? -62.306  -17.993 19.340  1.00 97.05  ? 466  ASN A ND2 1 
ATOM   3247 N N   . PHE A 1 441 ? -62.092  -16.103 15.663  1.00 132.97 ? 467  PHE A N   1 
ATOM   3248 C CA  . PHE A 1 441 ? -61.241  -14.978 15.353  1.00 137.61 ? 467  PHE A CA  1 
ATOM   3249 C C   . PHE A 1 441 ? -60.108  -15.014 16.368  1.00 142.88 ? 467  PHE A C   1 
ATOM   3250 O O   . PHE A 1 441 ? -59.018  -14.549 16.073  1.00 143.72 ? 467  PHE A O   1 
ATOM   3251 C CB  . PHE A 1 441 ? -61.956  -13.649 15.562  1.00 139.46 ? 467  PHE A CB  1 
ATOM   3252 C CG  . PHE A 1 441 ? -62.735  -13.136 14.380  1.00 127.66 ? 467  PHE A CG  1 
ATOM   3253 C CD1 . PHE A 1 441 ? -62.089  -12.650 13.256  1.00 151.93 ? 467  PHE A CD1 1 
ATOM   3254 C CD2 . PHE A 1 441 ? -64.105  -13.044 14.441  1.00 96.58  ? 467  PHE A CD2 1 
ATOM   3255 C CE1 . PHE A 1 441 ? -62.805  -12.138 12.187  1.00 131.45 ? 467  PHE A CE1 1 
ATOM   3256 C CE2 . PHE A 1 441 ? -64.823  -12.536 13.390  1.00 99.67  ? 467  PHE A CE2 1 
ATOM   3257 C CZ  . PHE A 1 441 ? -64.175  -12.080 12.262  1.00 120.85 ? 467  PHE A CZ  1 
ATOM   3258 N N   . TYR A 1 442 ? -60.340  -15.658 17.517  1.00 154.22 ? 468  TYR A N   1 
ATOM   3259 C CA  . TYR A 1 442 ? -59.390  -15.757 18.621  1.00 143.22 ? 468  TYR A CA  1 
ATOM   3260 C C   . TYR A 1 442 ? -59.338  -14.574 19.580  1.00 148.03 ? 468  TYR A C   1 
ATOM   3261 O O   . TYR A 1 442 ? -58.363  -14.457 20.307  1.00 154.15 ? 468  TYR A O   1 
ATOM   3262 C CB  . TYR A 1 442 ? -57.975  -15.993 18.107  1.00 140.27 ? 468  TYR A CB  1 
ATOM   3263 C CG  . TYR A 1 442 ? -57.532  -17.427 17.969  1.00 123.86 ? 468  TYR A CG  1 
ATOM   3264 C CD1 . TYR A 1 442 ? -57.658  -18.324 18.994  1.00 127.87 ? 468  TYR A CD1 1 
ATOM   3265 C CD2 . TYR A 1 442 ? -56.948  -17.866 16.804  1.00 129.24 ? 468  TYR A CD2 1 
ATOM   3266 C CE1 . TYR A 1 442 ? -57.215  -19.627 18.850  1.00 130.32 ? 468  TYR A CE1 1 
ATOM   3267 C CE2 . TYR A 1 442 ? -56.511  -19.161 16.653  1.00 117.04 ? 468  TYR A CE2 1 
ATOM   3268 C CZ  . TYR A 1 442 ? -56.643  -20.039 17.675  1.00 108.08 ? 468  TYR A CZ  1 
ATOM   3269 O OH  . TYR A 1 442 ? -56.200  -21.320 17.505  1.00 89.58  ? 468  TYR A OH  1 
ATOM   3270 N N   . HIS A 1 443 ? -60.297  -13.662 19.551  1.00 137.10 ? 469  HIS A N   1 
ATOM   3271 C CA  . HIS A 1 443 ? -60.225  -12.626 20.553  1.00 150.66 ? 469  HIS A CA  1 
ATOM   3272 C C   . HIS A 1 443 ? -61.511  -12.202 21.177  1.00 157.94 ? 469  HIS A C   1 
ATOM   3273 O O   . HIS A 1 443 ? -61.926  -11.035 21.015  1.00 173.90 ? 469  HIS A O   1 
ATOM   3274 C CB  . HIS A 1 443 ? -59.430  -11.415 20.058  1.00 155.13 ? 469  HIS A CB  1 
ATOM   3275 C CG  . HIS A 1 443 ? -58.683  -10.674 21.157  1.00 136.12 ? 469  HIS A CG  1 
ATOM   3276 N ND1 . HIS A 1 443 ? -59.176  -9.588  21.757  1.00 116.40 ? 469  HIS A ND1 1 
ATOM   3277 C CD2 . HIS A 1 443 ? -57.442  -10.910 21.738  1.00 114.33 ? 469  HIS A CD2 1 
ATOM   3278 C CE1 . HIS A 1 443 ? -58.304  -9.158  22.677  1.00 108.50 ? 469  HIS A CE1 1 
ATOM   3279 N NE2 . HIS A 1 443 ? -57.245  -9.966  22.659  1.00 93.41  ? 469  HIS A NE2 1 
ATOM   3280 N N   . PHE A 1 444 ? -62.141  -13.108 21.918  1.00 156.85 ? 470  PHE A N   1 
ATOM   3281 C CA  . PHE A 1 444 ? -63.108  -12.725 22.925  1.00 148.03 ? 470  PHE A CA  1 
ATOM   3282 C C   . PHE A 1 444 ? -64.127  -11.735 22.402  1.00 164.29 ? 470  PHE A C   1 
ATOM   3283 O O   . PHE A 1 444 ? -64.292  -10.657 22.976  1.00 185.06 ? 470  PHE A O   1 
ATOM   3284 C CB  . PHE A 1 444 ? -62.382  -12.173 24.145  1.00 138.70 ? 470  PHE A CB  1 
ATOM   3285 C CG  . PHE A 1 444 ? -61.301  -13.076 24.655  1.00 130.95 ? 470  PHE A CG  1 
ATOM   3286 C CD1 . PHE A 1 444 ? -61.299  -14.416 24.343  1.00 133.11 ? 470  PHE A CD1 1 
ATOM   3287 C CD2 . PHE A 1 444 ? -60.289  -12.585 25.438  1.00 137.29 ? 470  PHE A CD2 1 
ATOM   3288 C CE1 . PHE A 1 444 ? -60.311  -15.252 24.806  1.00 122.88 ? 470  PHE A CE1 1 
ATOM   3289 C CE2 . PHE A 1 444 ? -59.292  -13.411 25.907  1.00 139.70 ? 470  PHE A CE2 1 
ATOM   3290 C CZ  . PHE A 1 444 ? -59.303  -14.750 25.590  1.00 127.37 ? 470  PHE A CZ  1 
ATOM   3291 N N   . THR A 1 445 ? -64.830  -12.114 21.340  1.00 161.90 ? 471  THR A N   1 
ATOM   3292 C CA  . THR A 1 445 ? -65.386  -11.229 20.322  1.00 153.50 ? 471  THR A CA  1 
ATOM   3293 C C   . THR A 1 445 ? -66.329  -10.222 20.964  1.00 143.49 ? 471  THR A C   1 
ATOM   3294 O O   . THR A 1 445 ? -66.654  -9.181  20.396  1.00 95.18  ? 471  THR A O   1 
ATOM   3295 C CB  . THR A 1 445 ? -66.117  -12.035 19.226  1.00 135.75 ? 471  THR A CB  1 
ATOM   3296 O OG1 . THR A 1 445 ? -66.296  -11.223 18.065  1.00 125.30 ? 471  THR A OG1 1 
ATOM   3297 C CG2 . THR A 1 445 ? -67.473  -12.513 19.707  1.00 127.56 ? 471  THR A CG2 1 
ATOM   3298 N N   . ARG A 1 446 ? -66.725  -10.543 22.183  1.00 130.88 ? 472  ARG A N   1 
ATOM   3299 C CA  . ARG A 1 446 ? -67.526  -9.674  23.000  1.00 116.89 ? 472  ARG A CA  1 
ATOM   3300 C C   . ARG A 1 446 ? -66.757  -8.391  23.107  1.00 99.81  ? 472  ARG A C   1 
ATOM   3301 O O   . ARG A 1 446 ? -65.537  -8.406  23.066  1.00 100.28 ? 472  ARG A O   1 
ATOM   3302 C CB  . ARG A 1 446 ? -67.633  -10.281 24.387  1.00 116.20 ? 472  ARG A CB  1 
ATOM   3303 C CG  . ARG A 1 446 ? -66.293  -10.730 24.940  1.00 125.17 ? 472  ARG A CG  1 
ATOM   3304 C CD  . ARG A 1 446 ? -66.475  -11.788 26.015  1.00 134.94 ? 472  ARG A CD  1 
ATOM   3305 N NE  . ARG A 1 446 ? -65.225  -12.171 26.665  1.00 134.80 ? 472  ARG A NE  1 
ATOM   3306 C CZ  . ARG A 1 446 ? -65.160  -12.779 27.844  1.00 135.10 ? 472  ARG A CZ  1 
ATOM   3307 N NH1 . ARG A 1 446 ? -63.987  -13.101 28.367  1.00 132.01 ? 472  ARG A NH1 1 
ATOM   3308 N NH2 . ARG A 1 446 ? -66.273  -13.067 28.503  1.00 133.71 ? 472  ARG A NH2 1 
ATOM   3309 N N   . PRO A 1 447 ? -67.538  -7.230  23.173  1.00 82.14  ? 473  PRO A N   1 
ATOM   3310 C CA  . PRO A 1 447 ? -66.756  -5.999  23.119  1.00 61.44  ? 473  PRO A CA  1 
ATOM   3311 C C   . PRO A 1 447 ? -65.941  -5.818  24.352  1.00 55.86  ? 473  PRO A C   1 
ATOM   3312 O O   . PRO A 1 447 ? -66.293  -6.325  25.382  1.00 62.27  ? 473  PRO A O   1 
ATOM   3313 C CB  . PRO A 1 447 ? -67.809  -4.910  23.083  1.00 61.20  ? 473  PRO A CB  1 
ATOM   3314 C CG  . PRO A 1 447 ? -68.999  -5.534  22.522  1.00 72.17  ? 473  PRO A CG  1 
ATOM   3315 C CD  . PRO A 1 447 ? -69.004  -6.779  23.301  1.00 75.28  ? 473  PRO A CD  1 
ATOM   3316 N N   . LEU A 1 448 ? -64.861  -5.075  24.229  1.00 45.23  ? 474  LEU A N   1 
ATOM   3317 C CA  . LEU A 1 448 ? -63.987  -4.799  25.328  1.00 48.60  ? 474  LEU A CA  1 
ATOM   3318 C C   . LEU A 1 448 ? -64.702  -4.046  26.413  1.00 51.78  ? 474  LEU A C   1 
ATOM   3319 O O   . LEU A 1 448 ? -64.500  -4.305  27.566  1.00 63.71  ? 474  LEU A O   1 
ATOM   3320 C CB  . LEU A 1 448 ? -62.797  -3.998  24.853  1.00 52.69  ? 474  LEU A CB  1 
ATOM   3321 C CG  . LEU A 1 448 ? -61.883  -4.650  23.838  1.00 51.90  ? 474  LEU A CG  1 
ATOM   3322 C CD1 . LEU A 1 448 ? -60.724  -3.759  23.489  1.00 51.56  ? 474  LEU A CD1 1 
ATOM   3323 C CD2 . LEU A 1 448 ? -61.393  -5.985  24.322  1.00 55.43  ? 474  LEU A CD2 1 
ATOM   3324 N N   . ILE A 1 449 ? -65.546  -3.110  26.042  1.00 47.66  ? 475  ILE A N   1 
ATOM   3325 C CA  . ILE A 1 449 ? -66.290  -2.287  27.010  1.00 46.78  ? 475  ILE A CA  1 
ATOM   3326 C C   . ILE A 1 449 ? -67.794  -2.382  26.738  1.00 44.02  ? 475  ILE A C   1 
ATOM   3327 O O   . ILE A 1 449 ? -68.203  -2.379  25.612  1.00 50.69  ? 475  ILE A O   1 
ATOM   3328 C CB  . ILE A 1 449 ? -65.961  -0.798  26.807  1.00 53.62  ? 475  ILE A CB  1 
ATOM   3329 C CG1 . ILE A 1 449 ? -64.460  -0.563  26.690  1.00 60.01  ? 475  ILE A CG1 1 
ATOM   3330 C CG2 . ILE A 1 449 ? -66.594  0.053   27.875  1.00 60.52  ? 475  ILE A CG2 1 
ATOM   3331 C CD1 . ILE A 1 449 ? -63.664  -1.031  27.851  1.00 62.30  ? 475  ILE A CD1 1 
ATOM   3332 N N   . LYS A 1 450 ? -68.651  -2.405  27.746  1.00 51.79  ? 476  LYS A N   1 
ATOM   3333 C CA  . LYS A 1 450 ? -70.047  -2.445  27.401  1.00 48.45  ? 476  LYS A CA  1 
ATOM   3334 C C   . LYS A 1 450 ? -70.316  -1.276  26.442  1.00 51.18  ? 476  LYS A C   1 
ATOM   3335 O O   . LYS A 1 450 ? -69.761  -0.185  26.605  1.00 52.04  ? 476  LYS A O   1 
ATOM   3336 C CB  . LYS A 1 450 ? -70.939  -2.322  28.609  1.00 53.25  ? 476  LYS A CB  1 
ATOM   3337 C CG  . LYS A 1 450 ? -70.934  -3.540  29.506  1.00 73.15  ? 476  LYS A CG  1 
ATOM   3338 C CD  . LYS A 1 450 ? -71.956  -3.420  30.643  1.00 94.18  ? 476  LYS A CD  1 
ATOM   3339 C CE  . LYS A 1 450 ? -73.392  -3.239  30.125  1.00 100.30 ? 476  LYS A CE  1 
ATOM   3340 N NZ  . LYS A 1 450 ? -74.442  -3.153  31.189  1.00 92.25  ? 476  LYS A NZ  1 
ATOM   3341 N N   . PRO A 1 451 ? -71.126  -1.509  25.405  1.00 53.83  ? 477  PRO A N   1 
ATOM   3342 C CA  . PRO A 1 451 ? -71.480  -0.455  24.434  1.00 54.27  ? 477  PRO A CA  1 
ATOM   3343 C C   . PRO A 1 451 ? -72.292  0.700   25.044  1.00 48.71  ? 477  PRO A C   1 
ATOM   3344 O O   . PRO A 1 451 ? -72.178  1.840   24.621  1.00 45.46  ? 477  PRO A O   1 
ATOM   3345 C CB  . PRO A 1 451 ? -72.314  -1.214  23.415  1.00 56.22  ? 477  PRO A CB  1 
ATOM   3346 C CG  . PRO A 1 451 ? -71.680  -2.556  23.413  1.00 57.93  ? 477  PRO A CG  1 
ATOM   3347 C CD  . PRO A 1 451 ? -71.354  -2.844  24.851  1.00 54.96  ? 477  PRO A CD  1 
ATOM   3348 N N   . GLN A 1 452 ? -73.068  0.419   26.070  1.00 41.21  ? 478  GLN A N   1 
ATOM   3349 C CA  . GLN A 1 452 ? -73.811  1.461   26.673  1.00 44.22  ? 478  GLN A CA  1 
ATOM   3350 C C   . GLN A 1 452 ? -72.863  2.449   27.320  1.00 53.21  ? 478  GLN A C   1 
ATOM   3351 O O   . GLN A 1 452 ? -73.247  3.586   27.634  1.00 58.99  ? 478  GLN A O   1 
ATOM   3352 C CB  . GLN A 1 452 ? -74.775  0.932   27.729  1.00 51.01  ? 478  GLN A CB  1 
ATOM   3353 C CG  . GLN A 1 452 ? -75.860  -0.047  27.256  1.00 45.98  ? 478  GLN A CG  1 
ATOM   3354 C CD  . GLN A 1 452 ? -75.399  -1.482  27.088  1.00 51.07  ? 478  GLN A CD  1 
ATOM   3355 O OE1 . GLN A 1 452 ? -74.215  -1.794  26.827  1.00 52.67  ? 478  GLN A OE1 1 
ATOM   3356 N NE2 . GLN A 1 452 ? -76.343  -2.377  27.256  1.00 53.54  ? 478  GLN A NE2 1 
ATOM   3357 N N   . CYS A 1 453 ? -71.612  2.039   27.491  1.00 53.47  ? 479  CYS A N   1 
ATOM   3358 C CA  . CYS A 1 453 ? -70.641  2.897   28.124  1.00 51.51  ? 479  CYS A CA  1 
ATOM   3359 C C   . CYS A 1 453 ? -69.813  3.609   27.087  1.00 41.99  ? 479  CYS A C   1 
ATOM   3360 O O   . CYS A 1 453 ? -69.571  4.802   27.195  1.00 48.85  ? 479  CYS A O   1 
ATOM   3361 C CB  . CYS A 1 453 ? -69.722  2.084   29.082  1.00 53.62  ? 479  CYS A CB  1 
ATOM   3362 S SG  . CYS A 1 453 ? -68.732  3.087   30.254  1.00 56.20  ? 479  CYS A SG  1 
ATOM   3363 N N   . ALA A 1 454 ? -69.349  2.901   26.086  1.00 47.35  ? 480  ALA A N   1 
ATOM   3364 C CA  . ALA A 1 454 ? -68.507  3.558   25.077  1.00 53.31  ? 480  ALA A CA  1 
ATOM   3365 C C   . ALA A 1 454 ? -69.303  4.596   24.301  1.00 53.85  ? 480  ALA A C   1 
ATOM   3366 O O   . ALA A 1 454 ? -68.809  5.675   23.999  1.00 64.31  ? 480  ALA A O   1 
ATOM   3367 C CB  . ALA A 1 454 ? -67.893  2.547   24.138  1.00 51.52  ? 480  ALA A CB  1 
ATOM   3368 N N   . ALA A 1 455 ? -70.559  4.288   24.048  1.00 46.70  ? 481  ALA A N   1 
ATOM   3369 C CA  . ALA A 1 455 ? -71.435  5.192   23.322  1.00 49.05  ? 481  ALA A CA  1 
ATOM   3370 C C   . ALA A 1 455 ? -71.259  6.660   23.769  1.00 52.12  ? 481  ALA A C   1 
ATOM   3371 O O   . ALA A 1 455 ? -71.442  7.557   22.996  1.00 61.71  ? 481  ALA A O   1 
ATOM   3372 C CB  . ALA A 1 455 ? -72.890  4.756   23.510  1.00 44.43  ? 481  ALA A CB  1 
ATOM   3373 N N   . TYR A 1 456 ? -70.920  6.906   25.017  1.00 49.23  ? 482  TYR A N   1 
ATOM   3374 C CA  . TYR A 1 456 ? -70.761  8.280   25.458  1.00 47.99  ? 482  TYR A CA  1 
ATOM   3375 C C   . TYR A 1 456 ? -69.440  8.954   25.079  1.00 43.03  ? 482  TYR A C   1 
ATOM   3376 O O   . TYR A 1 456 ? -69.266  10.121  25.323  1.00 48.55  ? 482  TYR A O   1 
ATOM   3377 C CB  . TYR A 1 456 ? -70.905  8.367   26.981  1.00 48.61  ? 482  TYR A CB  1 
ATOM   3378 C CG  . TYR A 1 456 ? -72.277  8.133   27.493  1.00 44.86  ? 482  TYR A CG  1 
ATOM   3379 C CD1 . TYR A 1 456 ? -73.174  9.164   27.551  1.00 47.35  ? 482  TYR A CD1 1 
ATOM   3380 C CD2 . TYR A 1 456 ? -72.642  6.928   28.037  1.00 46.89  ? 482  TYR A CD2 1 
ATOM   3381 C CE1 . TYR A 1 456 ? -74.436  8.990   28.083  1.00 46.55  ? 482  TYR A CE1 1 
ATOM   3382 C CE2 . TYR A 1 456 ? -73.905  6.731   28.552  1.00 40.19  ? 482  TYR A CE2 1 
ATOM   3383 C CZ  . TYR A 1 456 ? -74.795  7.773   28.578  1.00 44.00  ? 482  TYR A CZ  1 
ATOM   3384 O OH  . TYR A 1 456 ? -76.059  7.617   29.093  1.00 45.24  ? 482  TYR A OH  1 
ATOM   3385 N N   . GLY A 1 457 ? -68.452  8.222   24.639  1.00 43.32  ? 483  GLY A N   1 
ATOM   3386 C CA  . GLY A 1 457 ? -67.212  8.883   24.321  1.00 44.93  ? 483  GLY A CA  1 
ATOM   3387 C C   . GLY A 1 457 ? -65.976  8.067   24.604  1.00 49.34  ? 483  GLY A C   1 
ATOM   3388 O O   . GLY A 1 457 ? -66.016  6.842   24.577  1.00 50.73  ? 483  GLY A O   1 
ATOM   3389 N N   . LYS A 1 458 ? -64.866  8.758   24.864  1.00 47.21  ? 484  LYS A N   1 
ATOM   3390 C CA  . LYS A 1 458 ? -63.630  8.085   25.135  1.00 51.50  ? 484  LYS A CA  1 
ATOM   3391 C C   . LYS A 1 458 ? -63.843  7.243   26.383  1.00 49.52  ? 484  LYS A C   1 
ATOM   3392 O O   . LYS A 1 458 ? -64.350  7.728   27.396  1.00 52.68  ? 484  LYS A O   1 
ATOM   3393 C CB  . LYS A 1 458 ? -62.453  9.050   25.321  1.00 55.26  ? 484  LYS A CB  1 
ATOM   3394 C CG  . LYS A 1 458 ? -62.212  10.015  24.185  1.00 64.69  ? 484  LYS A CG  1 
ATOM   3395 C CD  . LYS A 1 458 ? -60.931  10.804  24.420  1.00 72.35  ? 484  LYS A CD  1 
ATOM   3396 C CE  . LYS A 1 458 ? -60.859  12.032  23.525  1.00 76.38  ? 484  LYS A CE  1 
ATOM   3397 N NZ  . LYS A 1 458 ? -61.017  11.732  22.081  1.00 88.50  ? 484  LYS A NZ  1 
ATOM   3398 N N   . ALA A 1 459 ? -63.379  6.004   26.304  1.00 45.23  ? 485  ALA A N   1 
ATOM   3399 C CA  . ALA A 1 459 ? -63.519  5.058   27.357  1.00 43.01  ? 485  ALA A CA  1 
ATOM   3400 C C   . ALA A 1 459 ? -62.215  4.603   27.873  1.00 43.17  ? 485  ALA A C   1 
ATOM   3401 O O   . ALA A 1 459 ? -61.311  4.227   27.098  1.00 42.61  ? 485  ALA A O   1 
ATOM   3402 C CB  . ALA A 1 459 ? -64.269  3.858   26.830  1.00 42.69  ? 485  ALA A CB  1 
ATOM   3403 N N   . LEU A 1 460 ? -62.140  4.518   29.193  1.00 39.29  ? 486  LEU A N   1 
ATOM   3404 C CA  . LEU A 1 460 ? -60.928  4.029   29.838  1.00 44.39  ? 486  LEU A CA  1 
ATOM   3405 C C   . LEU A 1 460 ? -61.317  2.864   30.748  1.00 43.19  ? 486  LEU A C   1 
ATOM   3406 O O   . LEU A 1 460 ? -62.084  3.042   31.694  1.00 41.61  ? 486  LEU A O   1 
ATOM   3407 C CB  . LEU A 1 460 ? -60.278  5.126   30.692  1.00 44.61  ? 486  LEU A CB  1 
ATOM   3408 C CG  . LEU A 1 460 ? -59.081  4.694   31.542  1.00 44.70  ? 486  LEU A CG  1 
ATOM   3409 C CD1 . LEU A 1 460 ? -57.973  4.117   30.685  1.00 49.20  ? 486  LEU A CD1 1 
ATOM   3410 C CD2 . LEU A 1 460 ? -58.558  5.876   32.327  1.00 48.62  ? 486  LEU A CD2 1 
ATOM   3411 N N   . ASP A 1 461 ? -60.720  1.706   30.527  1.00 42.03  ? 487  ASP A N   1 
ATOM   3412 C CA  . ASP A 1 461 ? -61.017  0.562   31.365  1.00 39.74  ? 487  ASP A CA  1 
ATOM   3413 C C   . ASP A 1 461 ? -59.840  0.239   32.261  1.00 39.79  ? 487  ASP A C   1 
ATOM   3414 O O   . ASP A 1 461 ? -58.764  -0.187  31.785  1.00 41.18  ? 487  ASP A O   1 
ATOM   3415 C CB  . ASP A 1 461 ? -61.365  -0.650  30.533  1.00 43.58  ? 487  ASP A CB  1 
ATOM   3416 C CG  . ASP A 1 461 ? -61.991  -1.755  31.357  1.00 53.34  ? 487  ASP A CG  1 
ATOM   3417 O OD1 . ASP A 1 461 ? -61.583  -1.970  32.524  1.00 60.83  ? 487  ASP A OD1 1 
ATOM   3418 O OD2 . ASP A 1 461 ? -62.896  -2.412  30.820  1.00 55.01  ? 487  ASP A OD2 1 
ATOM   3419 N N   . LEU A 1 462 ? -60.064  0.421   33.563  1.00 34.72  ? 488  LEU A N   1 
ATOM   3420 C CA  . LEU A 1 462 ? -59.045  0.152   34.580  1.00 46.90  ? 488  LEU A CA  1 
ATOM   3421 C C   . LEU A 1 462 ? -59.520  -0.904  35.600  1.00 46.56  ? 488  LEU A C   1 
ATOM   3422 O O   . LEU A 1 462 ? -59.074  -0.958  36.743  1.00 52.08  ? 488  LEU A O   1 
ATOM   3423 C CB  . LEU A 1 462 ? -58.625  1.449   35.266  1.00 44.59  ? 488  LEU A CB  1 
ATOM   3424 C CG  . LEU A 1 462 ? -57.675  2.341   34.487  1.00 43.67  ? 488  LEU A CG  1 
ATOM   3425 C CD1 . LEU A 1 462 ? -57.503  3.682   35.148  1.00 47.27  ? 488  LEU A CD1 1 
ATOM   3426 C CD2 . LEU A 1 462 ? -56.336  1.648   34.388  1.00 47.61  ? 488  LEU A CD2 1 
ATOM   3427 N N   . SER A 1 463 ? -60.392  -1.781  35.148  1.00 41.57  ? 489  SER A N   1 
ATOM   3428 C CA  . SER A 1 463 ? -60.899  -2.821  36.003  1.00 39.25  ? 489  SER A CA  1 
ATOM   3429 C C   . SER A 1 463 ? -59.773  -3.813  36.279  1.00 40.26  ? 489  SER A C   1 
ATOM   3430 O O   . SER A 1 463 ? -58.820  -3.901  35.518  1.00 37.82  ? 489  SER A O   1 
ATOM   3431 C CB  . SER A 1 463 ? -62.037  -3.561  35.312  1.00 35.36  ? 489  SER A CB  1 
ATOM   3432 O OG  . SER A 1 463 ? -61.551  -4.279  34.159  1.00 39.91  ? 489  SER A OG  1 
ATOM   3433 N N   . LEU A 1 464 ? -59.839  -4.502  37.406  1.00 39.17  ? 490  LEU A N   1 
ATOM   3434 C CA  . LEU A 1 464 ? -58.832  -5.537  37.703  1.00 41.28  ? 490  LEU A CA  1 
ATOM   3435 C C   . LEU A 1 464 ? -57.424  -5.042  37.806  1.00 36.86  ? 490  LEU A C   1 
ATOM   3436 O O   . LEU A 1 464 ? -56.522  -5.613  37.261  1.00 38.35  ? 490  LEU A O   1 
ATOM   3437 C CB  . LEU A 1 464 ? -58.932  -6.715  36.710  1.00 41.49  ? 490  LEU A CB  1 
ATOM   3438 C CG  . LEU A 1 464 ? -60.320  -7.430  36.803  1.00 50.36  ? 490  LEU A CG  1 
ATOM   3439 C CD1 . LEU A 1 464 ? -60.626  -8.364  35.652  1.00 54.05  ? 490  LEU A CD1 1 
ATOM   3440 C CD2 . LEU A 1 464 ? -60.458  -8.198  38.103  1.00 50.89  ? 490  LEU A CD2 1 
ATOM   3441 N N   . ASN A 1 465 ? -57.281  -3.879  38.398  1.00 40.23  ? 491  ASN A N   1 
ATOM   3442 C CA  . ASN A 1 465 ? -55.989  -3.332  38.668  1.00 43.17  ? 491  ASN A CA  1 
ATOM   3443 C C   . ASN A 1 465 ? -55.907  -3.269  40.201  1.00 45.63  ? 491  ASN A C   1 
ATOM   3444 O O   . ASN A 1 465 ? -56.715  -3.913  40.886  1.00 45.56  ? 491  ASN A O   1 
ATOM   3445 C CB  . ASN A 1 465 ? -55.752  -1.962  37.982  1.00 47.88  ? 491  ASN A CB  1 
ATOM   3446 C CG  . ASN A 1 465 ? -55.374  -2.094  36.521  1.00 42.56  ? 491  ASN A CG  1 
ATOM   3447 O OD1 . ASN A 1 465 ? -54.183  -2.054  36.206  1.00 47.23  ? 491  ASN A OD1 1 
ATOM   3448 N ND2 . ASN A 1 465 ? -56.327  -2.483  35.678  1.00 43.34  ? 491  ASN A ND2 1 
ATOM   3449 N N   . SER A 1 466 ? -54.991  -2.472  40.743  1.00 43.20  ? 492  SER A N   1 
ATOM   3450 C CA  . SER A 1 466 ? -54.839  -2.382  42.188  1.00 44.55  ? 492  SER A CA  1 
ATOM   3451 C C   . SER A 1 466 ? -55.142  -1.008  42.686  1.00 42.15  ? 492  SER A C   1 
ATOM   3452 O O   . SER A 1 466 ? -54.485  -0.512  43.572  1.00 39.87  ? 492  SER A O   1 
ATOM   3453 C CB  . SER A 1 466 ? -53.421  -2.727  42.536  1.00 40.61  ? 492  SER A CB  1 
ATOM   3454 O OG  . SER A 1 466 ? -53.146  -4.035  42.117  1.00 54.95  ? 492  SER A OG  1 
ATOM   3455 N N   . ILE A 1 467 ? -56.145  -0.377  42.118  1.00 44.65  ? 493  ILE A N   1 
ATOM   3456 C CA  . ILE A 1 467 ? -56.459  0.973   42.534  1.00 45.35  ? 493  ILE A CA  1 
ATOM   3457 C C   . ILE A 1 467 ? -57.350  0.841   43.745  1.00 42.53  ? 493  ILE A C   1 
ATOM   3458 O O   . ILE A 1 467 ? -58.552  1.131   43.709  1.00 48.72  ? 493  ILE A O   1 
ATOM   3459 C CB  . ILE A 1 467 ? -57.042  1.771   41.348  1.00 40.60  ? 493  ILE A CB  1 
ATOM   3460 C CG1 . ILE A 1 467 ? -56.040  1.704   40.180  1.00 49.40  ? 493  ILE A CG1 1 
ATOM   3461 C CG2 . ILE A 1 467 ? -57.231  3.213   41.726  1.00 39.54  ? 493  ILE A CG2 1 
ATOM   3462 C CD1 . ILE A 1 467 ? -56.561  2.263   38.860  1.00 54.79  ? 493  ILE A CD1 1 
ATOM   3463 N N   . PHE A 1 468 ? -56.764  0.398   44.831  1.00 46.61  ? 494  PHE A N   1 
ATOM   3464 C CA  . PHE A 1 468 ? -57.524  0.158   46.035  1.00 48.37  ? 494  PHE A CA  1 
ATOM   3465 C C   . PHE A 1 468 ? -57.935  1.423   46.708  1.00 46.69  ? 494  PHE A C   1 
ATOM   3466 O O   . PHE A 1 468 ? -58.732  1.441   47.606  1.00 46.38  ? 494  PHE A O   1 
ATOM   3467 C CB  . PHE A 1 468 ? -56.820  -0.800  46.979  1.00 43.65  ? 494  PHE A CB  1 
ATOM   3468 C CG  . PHE A 1 468 ? -55.546  -0.301  47.527  1.00 40.51  ? 494  PHE A CG  1 
ATOM   3469 C CD1 . PHE A 1 468 ? -55.527  0.389   48.682  1.00 46.62  ? 494  PHE A CD1 1 
ATOM   3470 C CD2 . PHE A 1 468 ? -54.376  -0.582  46.921  1.00 43.38  ? 494  PHE A CD2 1 
ATOM   3471 C CE1 . PHE A 1 468 ? -54.361  0.841   49.209  1.00 45.41  ? 494  PHE A CE1 1 
ATOM   3472 C CE2 . PHE A 1 468 ? -53.200  -0.136  47.440  1.00 41.33  ? 494  PHE A CE2 1 
ATOM   3473 C CZ  . PHE A 1 468 ? -53.192  0.577   48.586  1.00 45.96  ? 494  PHE A CZ  1 
ATOM   3474 N N   . PHE A 1 469 ? -57.319  2.489   46.273  1.00 45.88  ? 495  PHE A N   1 
ATOM   3475 C CA  . PHE A 1 469 ? -57.623  3.784   46.758  1.00 53.56  ? 495  PHE A CA  1 
ATOM   3476 C C   . PHE A 1 469 ? -57.305  4.705   45.610  1.00 50.52  ? 495  PHE A C   1 
ATOM   3477 O O   . PHE A 1 469 ? -56.306  4.542   44.971  1.00 43.60  ? 495  PHE A O   1 
ATOM   3478 C CB  . PHE A 1 469 ? -56.713  3.979   47.949  1.00 57.11  ? 495  PHE A CB  1 
ATOM   3479 C CG  . PHE A 1 469 ? -56.425  5.375   48.290  1.00 52.37  ? 495  PHE A CG  1 
ATOM   3480 C CD1 . PHE A 1 469 ? -57.407  6.191   48.755  1.00 72.62  ? 495  PHE A CD1 1 
ATOM   3481 C CD2 . PHE A 1 469 ? -55.158  5.843   48.200  1.00 54.70  ? 495  PHE A CD2 1 
ATOM   3482 C CE1 . PHE A 1 469 ? -57.139  7.481   49.111  1.00 74.69  ? 495  PHE A CE1 1 
ATOM   3483 C CE2 . PHE A 1 469 ? -54.869  7.126   48.532  1.00 64.96  ? 495  PHE A CE2 1 
ATOM   3484 C CZ  . PHE A 1 469 ? -55.862  7.953   48.990  1.00 79.48  ? 495  PHE A CZ  1 
ATOM   3485 N N   . ILE A 1 470 ? -58.138  5.697   45.371  1.00 49.84  ? 496  ILE A N   1 
ATOM   3486 C CA  . ILE A 1 470 ? -57.895  6.621   44.297  1.00 51.00  ? 496  ILE A CA  1 
ATOM   3487 C C   . ILE A 1 470 ? -57.213  7.794   44.920  1.00 54.35  ? 496  ILE A C   1 
ATOM   3488 O O   . ILE A 1 470 ? -57.766  8.462   45.754  1.00 46.01  ? 496  ILE A O   1 
ATOM   3489 C CB  . ILE A 1 470 ? -59.198  7.089   43.648  1.00 52.68  ? 496  ILE A CB  1 
ATOM   3490 C CG1 . ILE A 1 470 ? -59.811  5.990   42.818  1.00 54.70  ? 496  ILE A CG1 1 
ATOM   3491 C CG2 . ILE A 1 470 ? -58.973  8.256   42.723  1.00 51.49  ? 496  ILE A CG2 1 
ATOM   3492 C CD1 . ILE A 1 470 ? -61.274  6.198   42.567  1.00 49.19  ? 496  ILE A CD1 1 
ATOM   3493 N N   . GLY A 1 471 ? -55.996  8.035   44.476  1.00 55.60  ? 497  GLY A N   1 
ATOM   3494 C CA  . GLY A 1 471 ? -55.165  9.132   44.993  1.00 61.28  ? 497  GLY A CA  1 
ATOM   3495 C C   . GLY A 1 471 ? -55.518  10.493  44.407  1.00 66.18  ? 497  GLY A C   1 
ATOM   3496 O O   . GLY A 1 471 ? -56.280  10.589  43.460  1.00 63.54  ? 497  GLY A O   1 
ATOM   3497 N N   . PRO A 1 472 ? -54.901  11.561  44.923  1.00 85.26  ? 498  PRO A N   1 
ATOM   3498 C CA  . PRO A 1 472 ? -55.212  12.908  44.409  1.00 74.92  ? 498  PRO A CA  1 
ATOM   3499 C C   . PRO A 1 472 ? -54.754  13.172  42.954  1.00 60.55  ? 498  PRO A C   1 
ATOM   3500 O O   . PRO A 1 472 ? -55.355  13.963  42.272  1.00 61.53  ? 498  PRO A O   1 
ATOM   3501 C CB  . PRO A 1 472 ? -54.498  13.836  45.401  1.00 82.39  ? 498  PRO A CB  1 
ATOM   3502 C CG  . PRO A 1 472 ? -54.024  12.962  46.530  1.00 80.67  ? 498  PRO A CG  1 
ATOM   3503 C CD  . PRO A 1 472 ? -53.858  11.594  45.961  1.00 78.57  ? 498  PRO A CD  1 
ATOM   3504 N N   . ASN A 1 473 ? -53.724  12.486  42.489  1.00 62.56  ? 499  ASN A N   1 
ATOM   3505 C CA  . ASN A 1 473 ? -53.235  12.649  41.120  1.00 61.28  ? 499  ASN A CA  1 
ATOM   3506 C C   . ASN A 1 473 ? -53.484  11.372  40.313  1.00 63.06  ? 499  ASN A C   1 
ATOM   3507 O O   . ASN A 1 473 ? -52.824  11.094  39.323  1.00 53.35  ? 499  ASN A O   1 
ATOM   3508 C CB  . ASN A 1 473 ? -51.727  12.900  41.170  1.00 77.58  ? 499  ASN A CB  1 
ATOM   3509 C CG  . ASN A 1 473 ? -51.373  14.140  41.961  1.00 90.42  ? 499  ASN A CG  1 
ATOM   3510 O OD1 . ASN A 1 473 ? -52.048  15.178  41.859  1.00 85.29  ? 499  ASN A OD1 1 
ATOM   3511 N ND2 . ASN A 1 473 ? -50.275  14.064  42.711  1.00 94.45  ? 499  ASN A ND2 1 
ATOM   3512 N N   . GLN A 1 474 ? -54.452  10.587  40.729  1.00 66.06  ? 500  GLN A N   1 
ATOM   3513 C CA  . GLN A 1 474 ? -54.678  9.348   40.052  1.00 60.24  ? 500  GLN A CA  1 
ATOM   3514 C C   . GLN A 1 474 ? -54.972  9.544   38.573  1.00 58.63  ? 500  GLN A C   1 
ATOM   3515 O O   . GLN A 1 474 ? -54.395  8.877   37.725  1.00 59.70  ? 500  GLN A O   1 
ATOM   3516 C CB  . GLN A 1 474 ? -55.863  8.604   40.686  1.00 64.64  ? 500  GLN A CB  1 
ATOM   3517 C CG  . GLN A 1 474 ? -55.911  7.144   40.279  1.00 56.61  ? 500  GLN A CG  1 
ATOM   3518 C CD  . GLN A 1 474 ? -54.759  6.401   40.911  1.00 55.22  ? 500  GLN A CD  1 
ATOM   3519 O OE1 . GLN A 1 474 ? -54.521  6.545   42.110  1.00 55.72  ? 500  GLN A OE1 1 
ATOM   3520 N NE2 . GLN A 1 474 ? -54.099  5.541   40.145  1.00 53.77  ? 500  GLN A NE2 1 
ATOM   3521 N N   . PHE A 1 475 ? -55.866  10.477  38.275  1.00 55.24  ? 501  PHE A N   1 
ATOM   3522 C CA  . PHE A 1 475 ? -56.283  10.704  36.912  1.00 59.78  ? 501  PHE A CA  1 
ATOM   3523 C C   . PHE A 1 475 ? -55.707  11.928  36.172  1.00 63.97  ? 501  PHE A C   1 
ATOM   3524 O O   . PHE A 1 475 ? -56.155  12.253  35.083  1.00 68.91  ? 501  PHE A O   1 
ATOM   3525 C CB  . PHE A 1 475 ? -57.799  10.728  36.902  1.00 55.48  ? 501  PHE A CB  1 
ATOM   3526 C CG  . PHE A 1 475 ? -58.400  9.552   37.580  1.00 52.10  ? 501  PHE A CG  1 
ATOM   3527 C CD1 . PHE A 1 475 ? -58.160  8.285   37.114  1.00 57.76  ? 501  PHE A CD1 1 
ATOM   3528 C CD2 . PHE A 1 475 ? -59.320  9.711   38.584  1.00 54.91  ? 501  PHE A CD2 1 
ATOM   3529 C CE1 . PHE A 1 475 ? -58.724  7.181   37.730  1.00 55.61  ? 501  PHE A CE1 1 
ATOM   3530 C CE2 . PHE A 1 475 ? -59.935  8.614   39.174  1.00 51.57  ? 501  PHE A CE2 1 
ATOM   3531 C CZ  . PHE A 1 475 ? -59.630  7.351   38.754  1.00 46.48  ? 501  PHE A CZ  1 
ATOM   3532 N N   . GLU A 1 476 ? -54.644  12.522  36.700  1.00 68.90  ? 502  GLU A N   1 
ATOM   3533 C CA  . GLU A 1 476 ? -54.026  13.687  36.071  1.00 76.50  ? 502  GLU A CA  1 
ATOM   3534 C C   . GLU A 1 476 ? -53.492  13.397  34.664  1.00 71.10  ? 502  GLU A C   1 
ATOM   3535 O O   . GLU A 1 476 ? -52.992  12.323  34.388  1.00 74.65  ? 502  GLU A O   1 
ATOM   3536 C CB  . GLU A 1 476 ? -52.893  14.234  36.954  1.00 80.12  ? 502  GLU A CB  1 
ATOM   3537 C CG  . GLU A 1 476 ? -53.347  14.646  38.359  1.00 100.88 ? 502  GLU A CG  1 
ATOM   3538 C CD  . GLU A 1 476 ? -54.453  15.722  38.398  1.00 111.86 ? 502  GLU A CD  1 
ATOM   3539 O OE1 . GLU A 1 476 ? -54.687  16.412  37.373  1.00 125.77 ? 502  GLU A OE1 1 
ATOM   3540 O OE2 . GLU A 1 476 ? -55.070  15.903  39.483  1.00 93.49  ? 502  GLU A OE2 1 
ATOM   3541 N N   . ASN A 1 477 ? -53.635  14.364  33.770  1.00 70.47  ? 503  ASN A N   1 
ATOM   3542 C CA  . ASN A 1 477 ? -53.146  14.231  32.385  1.00 69.55  ? 503  ASN A CA  1 
ATOM   3543 C C   . ASN A 1 477 ? -53.935  13.299  31.489  1.00 66.11  ? 503  ASN A C   1 
ATOM   3544 O O   . ASN A 1 477 ? -53.436  12.902  30.436  1.00 70.31  ? 503  ASN A O   1 
ATOM   3545 C CB  . ASN A 1 477 ? -51.672  13.810  32.371  1.00 72.24  ? 503  ASN A CB  1 
ATOM   3546 C CG  . ASN A 1 477 ? -50.789  14.775  33.126  1.00 67.74  ? 503  ASN A CG  1 
ATOM   3547 O OD1 . ASN A 1 477 ? -51.106  15.949  33.237  1.00 67.74  ? 503  ASN A OD1 1 
ATOM   3548 N ND2 . ASN A 1 477 ? -49.664  14.288  33.626  1.00 69.25  ? 503  ASN A ND2 1 
ATOM   3549 N N   . LEU A 1 478 ? -55.100  12.848  31.942  1.00 67.60  ? 504  LEU A N   1 
ATOM   3550 C CA  . LEU A 1 478 ? -55.934  11.977  31.103  1.00 63.57  ? 504  LEU A CA  1 
ATOM   3551 C C   . LEU A 1 478 ? -56.777  12.766  30.140  1.00 61.34  ? 504  LEU A C   1 
ATOM   3552 O O   . LEU A 1 478 ? -57.207  13.863  30.449  1.00 76.49  ? 504  LEU A O   1 
ATOM   3553 C CB  . LEU A 1 478 ? -56.902  11.164  31.938  1.00 61.71  ? 504  LEU A CB  1 
ATOM   3554 C CG  . LEU A 1 478 ? -56.370  9.963   32.690  1.00 65.80  ? 504  LEU A CG  1 
ATOM   3555 C CD1 . LEU A 1 478 ? -57.487  9.403   33.555  1.00 53.11  ? 504  LEU A CD1 1 
ATOM   3556 C CD2 . LEU A 1 478 ? -55.859  8.929   31.678  1.00 58.80  ? 504  LEU A CD2 1 
ATOM   3557 N N   . PRO A 1 479 ? -57.054  12.199  28.971  1.00 64.57  ? 505  PRO A N   1 
ATOM   3558 C CA  . PRO A 1 479 ? -57.934  12.964  28.083  1.00 57.72  ? 505  PRO A CA  1 
ATOM   3559 C C   . PRO A 1 479 ? -59.334  13.033  28.704  1.00 54.90  ? 505  PRO A C   1 
ATOM   3560 O O   . PRO A 1 479 ? -59.554  12.506  29.772  1.00 62.50  ? 505  PRO A O   1 
ATOM   3561 C CB  . PRO A 1 479 ? -57.921  12.180  26.786  1.00 55.09  ? 505  PRO A CB  1 
ATOM   3562 C CG  . PRO A 1 479 ? -57.262  10.857  27.111  1.00 64.17  ? 505  PRO A CG  1 
ATOM   3563 C CD  . PRO A 1 479 ? -56.371  11.101  28.280  1.00 64.13  ? 505  PRO A CD  1 
ATOM   3564 N N   . ASP A 1 480 ? -60.241  13.746  28.080  1.00 59.88  ? 506  ASP A N   1 
ATOM   3565 C CA  . ASP A 1 480 ? -61.568  13.900  28.610  1.00 60.09  ? 506  ASP A CA  1 
ATOM   3566 C C   . ASP A 1 480 ? -62.308  12.593  28.483  1.00 63.57  ? 506  ASP A C   1 
ATOM   3567 O O   . ASP A 1 480 ? -62.927  12.337  27.466  1.00 76.83  ? 506  ASP A O   1 
ATOM   3568 C CB  . ASP A 1 480 ? -62.293  14.986  27.827  1.00 61.38  ? 506  ASP A CB  1 
ATOM   3569 C CG  . ASP A 1 480 ? -63.668  15.287  28.374  1.00 71.25  ? 506  ASP A CG  1 
ATOM   3570 O OD1 . ASP A 1 480 ? -63.956  14.924  29.534  1.00 88.39  ? 506  ASP A OD1 1 
ATOM   3571 O OD2 . ASP A 1 480 ? -64.430  15.980  27.674  1.00 81.65  ? 506  ASP A OD2 1 
ATOM   3572 N N   . ILE A 1 481 ? -62.333  11.827  29.564  1.00 58.05  ? 507  ILE A N   1 
ATOM   3573 C CA  . ILE A 1 481 ? -62.986  10.520  29.593  1.00 50.68  ? 507  ILE A CA  1 
ATOM   3574 C C   . ILE A 1 481 ? -64.467  10.594  29.805  1.00 48.02  ? 507  ILE A C   1 
ATOM   3575 O O   . ILE A 1 481 ? -64.928  11.269  30.710  1.00 45.61  ? 507  ILE A O   1 
ATOM   3576 C CB  . ILE A 1 481 ? -62.385  9.666   30.723  1.00 53.38  ? 507  ILE A CB  1 
ATOM   3577 C CG1 . ILE A 1 481 ? -60.938  9.360   30.413  1.00 49.45  ? 507  ILE A CG1 1 
ATOM   3578 C CG2 . ILE A 1 481 ? -63.157  8.390   30.932  1.00 59.53  ? 507  ILE A CG2 1 
ATOM   3579 C CD1 . ILE A 1 481 ? -60.747  8.739   29.059  1.00 48.73  ? 507  ILE A CD1 1 
ATOM   3580 N N   . ALA A 1 482 ? -65.217  9.852   28.999  1.00 44.44  ? 508  ALA A N   1 
ATOM   3581 C CA  . ALA A 1 482 ? -66.686  9.837   29.142  1.00 45.74  ? 508  ALA A CA  1 
ATOM   3582 C C   . ALA A 1 482 ? -67.176  8.596   29.865  1.00 49.58  ? 508  ALA A C   1 
ATOM   3583 O O   . ALA A 1 482 ? -68.223  8.626   30.564  1.00 49.20  ? 508  ALA A O   1 
ATOM   3584 C CB  . ALA A 1 482 ? -67.351  9.893   27.777  1.00 42.03  ? 508  ALA A CB  1 
ATOM   3585 N N   . CYS A 1 483 ? -66.410  7.519   29.681  1.00 40.79  ? 509  CYS A N   1 
ATOM   3586 C CA  . CYS A 1 483 ? -66.702  6.197   30.209  1.00 48.86  ? 509  CYS A CA  1 
ATOM   3587 C C   . CYS A 1 483 ? -65.504  5.667   30.970  1.00 43.47  ? 509  CYS A C   1 
ATOM   3588 O O   . CYS A 1 483 ? -64.417  5.479   30.392  1.00 45.42  ? 509  CYS A O   1 
ATOM   3589 C CB  . CYS A 1 483 ? -67.010  5.284   29.008  1.00 53.60  ? 509  CYS A CB  1 
ATOM   3590 S SG  . CYS A 1 483 ? -66.989  3.499   29.297  1.00 59.65  ? 509  CYS A SG  1 
ATOM   3591 N N   . LEU A 1 484 ? -65.746  5.259   32.209  1.00 43.53  ? 510  LEU A N   1 
ATOM   3592 C CA  . LEU A 1 484 ? -64.669  4.766   33.087  1.00 47.00  ? 510  LEU A CA  1 
ATOM   3593 C C   . LEU A 1 484 ? -65.075  3.522   33.901  1.00 44.83  ? 510  LEU A C   1 
ATOM   3594 O O   . LEU A 1 484 ? -66.072  3.535   34.644  1.00 38.69  ? 510  LEU A O   1 
ATOM   3595 C CB  . LEU A 1 484 ? -64.289  5.895   34.094  1.00 42.70  ? 510  LEU A CB  1 
ATOM   3596 C CG  . LEU A 1 484 ? -63.132  5.626   35.055  1.00 44.95  ? 510  LEU A CG  1 
ATOM   3597 C CD1 . LEU A 1 484 ? -61.803  5.565   34.327  1.00 41.98  ? 510  LEU A CD1 1 
ATOM   3598 C CD2 . LEU A 1 484 ? -63.072  6.704   36.106  1.00 51.79  ? 510  LEU A CD2 1 
ATOM   3599 N N   . ASN A 1 485 ? -64.241  2.502   33.856  1.00 41.52  ? 511  ASN A N   1 
ATOM   3600 C CA  . ASN A 1 485 ? -64.506  1.297   34.613  1.00 44.84  ? 511  ASN A CA  1 
ATOM   3601 C C   . ASN A 1 485 ? -63.409  1.124   35.703  1.00 43.97  ? 511  ASN A C   1 
ATOM   3602 O O   . ASN A 1 485 ? -62.199  1.025   35.387  1.00 38.83  ? 511  ASN A O   1 
ATOM   3603 C CB  . ASN A 1 485 ? -64.504  0.092   33.670  1.00 42.82  ? 511  ASN A CB  1 
ATOM   3604 C CG  . ASN A 1 485 ? -65.138  -1.152  34.288  1.00 47.75  ? 511  ASN A CG  1 
ATOM   3605 O OD1 . ASN A 1 485 ? -65.470  -1.183  35.469  1.00 50.59  ? 511  ASN A OD1 1 
ATOM   3606 N ND2 . ASN A 1 485 ? -65.337  -2.166  33.462  1.00 49.25  ? 511  ASN A ND2 1 
ATOM   3607 N N   . LEU A 1 486 ? -63.835  1.098   36.964  1.00 38.40  ? 512  LEU A N   1 
ATOM   3608 C CA  . LEU A 1 486 ? -62.920  0.910   38.115  1.00 39.35  ? 512  LEU A CA  1 
ATOM   3609 C C   . LEU A 1 486 ? -63.342  -0.312  38.947  1.00 40.11  ? 512  LEU A C   1 
ATOM   3610 O O   . LEU A 1 486 ? -63.072  -0.414  40.139  1.00 35.97  ? 512  LEU A O   1 
ATOM   3611 C CB  . LEU A 1 486 ? -62.935  2.128   38.985  1.00 38.05  ? 512  LEU A CB  1 
ATOM   3612 C CG  . LEU A 1 486 ? -62.306  3.363   38.374  1.00 43.25  ? 512  LEU A CG  1 
ATOM   3613 C CD1 . LEU A 1 486 ? -62.606  4.535   39.278  1.00 43.61  ? 512  LEU A CD1 1 
ATOM   3614 C CD2 . LEU A 1 486 ? -60.817  3.147   38.210  1.00 42.26  ? 512  LEU A CD2 1 
ATOM   3615 N N   . SER A 1 487 ? -64.013  -1.233  38.288  1.00 41.00  ? 513  SER A N   1 
ATOM   3616 C CA  . SER A 1 487 ? -64.489  -2.426  38.916  1.00 43.44  ? 513  SER A CA  1 
ATOM   3617 C C   . SER A 1 487 ? -63.345  -3.329  39.366  1.00 44.65  ? 513  SER A C   1 
ATOM   3618 O O   . SER A 1 487 ? -62.271  -3.328  38.787  1.00 42.12  ? 513  SER A O   1 
ATOM   3619 C CB  . SER A 1 487 ? -65.377  -3.179  37.906  1.00 43.71  ? 513  SER A CB  1 
ATOM   3620 O OG  . SER A 1 487 ? -65.984  -4.336  38.441  1.00 42.51  ? 513  SER A OG  1 
ATOM   3621 N N   . ALA A 1 488 ? -63.564  -4.038  40.468  1.00 41.65  ? 514  ALA A N   1 
ATOM   3622 C CA  . ALA A 1 488 ? -62.591  -4.997  40.969  1.00 33.98  ? 514  ALA A CA  1 
ATOM   3623 C C   . ALA A 1 488 ? -61.206  -4.504  41.215  1.00 35.38  ? 514  ALA A C   1 
ATOM   3624 O O   . ALA A 1 488 ? -60.256  -5.091  40.709  1.00 39.51  ? 514  ALA A O   1 
ATOM   3625 C CB  . ALA A 1 488 ? -62.523  -6.201  40.053  1.00 35.09  ? 514  ALA A CB  1 
ATOM   3626 N N   . ASN A 1 489 ? -61.087  -3.496  42.069  1.00 39.34  ? 515  ASN A N   1 
ATOM   3627 C CA  . ASN A 1 489 ? -59.813  -2.935  42.462  1.00 44.59  ? 515  ASN A CA  1 
ATOM   3628 C C   . ASN A 1 489 ? -59.622  -2.931  43.989  1.00 43.00  ? 515  ASN A C   1 
ATOM   3629 O O   . ASN A 1 489 ? -58.740  -2.281  44.477  1.00 53.89  ? 515  ASN A O   1 
ATOM   3630 C CB  . ASN A 1 489 ? -59.737  -1.494  41.930  1.00 49.70  ? 515  ASN A CB  1 
ATOM   3631 C CG  . ASN A 1 489 ? -59.318  -1.430  40.492  1.00 47.38  ? 515  ASN A CG  1 
ATOM   3632 O OD1 . ASN A 1 489 ? -58.120  -1.577  40.182  1.00 46.19  ? 515  ASN A OD1 1 
ATOM   3633 N ND2 . ASN A 1 489 ? -60.251  -1.043  39.622  1.00 44.01  ? 515  ASN A ND2 1 
ATOM   3634 N N   . SER A 1 490 ? -60.407  -3.697  44.727  1.00 46.44  ? 516  SER A N   1 
ATOM   3635 C CA  . SER A 1 490 ? -60.318  -3.725  46.214  1.00 45.04  ? 516  SER A CA  1 
ATOM   3636 C C   . SER A 1 490 ? -60.322  -2.314  46.723  1.00 50.28  ? 516  SER A C   1 
ATOM   3637 O O   . SER A 1 490 ? -59.504  -1.956  47.536  1.00 58.42  ? 516  SER A O   1 
ATOM   3638 C CB  . SER A 1 490 ? -59.041  -4.390  46.697  1.00 42.11  ? 516  SER A CB  1 
ATOM   3639 O OG  . SER A 1 490 ? -58.893  -5.654  46.085  1.00 57.08  ? 516  SER A OG  1 
ATOM   3640 N N   . ASN A 1 491 ? -61.173  -1.466  46.187  1.00 52.45  ? 517  ASN A N   1 
ATOM   3641 C CA  . ASN A 1 491 ? -61.166  -0.114  46.663  1.00 49.33  ? 517  ASN A CA  1 
ATOM   3642 C C   . ASN A 1 491 ? -62.058  0.023   47.864  1.00 45.35  ? 517  ASN A C   1 
ATOM   3643 O O   . ASN A 1 491 ? -63.279  -0.126  47.769  1.00 47.75  ? 517  ASN A O   1 
ATOM   3644 C CB  . ASN A 1 491 ? -61.571  0.855   45.558  1.00 50.04  ? 517  ASN A CB  1 
ATOM   3645 C CG  . ASN A 1 491 ? -61.557  2.278   46.021  1.00 47.00  ? 517  ASN A CG  1 
ATOM   3646 O OD1 . ASN A 1 491 ? -61.761  2.557   47.184  1.00 56.44  ? 517  ASN A OD1 1 
ATOM   3647 N ND2 . ASN A 1 491 ? -61.359  3.177   45.118  1.00 47.92  ? 517  ASN A ND2 1 
ATOM   3648 N N   . ALA A 1 492 ? -61.467  0.378   48.995  1.00 46.97  ? 518  ALA A N   1 
ATOM   3649 C CA  . ALA A 1 492 ? -62.248  0.533   50.238  1.00 48.96  ? 518  ALA A CA  1 
ATOM   3650 C C   . ALA A 1 492 ? -62.309  1.947   50.737  1.00 45.48  ? 518  ALA A C   1 
ATOM   3651 O O   . ALA A 1 492 ? -62.640  2.155   51.895  1.00 47.48  ? 518  ALA A O   1 
ATOM   3652 C CB  . ALA A 1 492 ? -61.655  -0.348  51.321  1.00 49.36  ? 518  ALA A CB  1 
ATOM   3653 N N   . GLN A 1 493 ? -62.118  2.923   49.850  1.00 48.52  ? 519  GLN A N   1 
ATOM   3654 C CA  . GLN A 1 493 ? -62.082  4.310   50.268  1.00 45.09  ? 519  GLN A CA  1 
ATOM   3655 C C   . GLN A 1 493 ? -63.412  4.959   50.439  1.00 51.74  ? 519  GLN A C   1 
ATOM   3656 O O   . GLN A 1 493 ? -64.433  4.422   50.004  1.00 49.04  ? 519  GLN A O   1 
ATOM   3657 C CB  . GLN A 1 493 ? -61.291  5.150   49.274  1.00 45.88  ? 519  GLN A CB  1 
ATOM   3658 C CG  . GLN A 1 493 ? -61.983  5.491   47.969  1.00 49.65  ? 519  GLN A CG  1 
ATOM   3659 C CD  . GLN A 1 493 ? -61.073  6.267   47.005  1.00 50.71  ? 519  GLN A CD  1 
ATOM   3660 O OE1 . GLN A 1 493 ? -60.825  5.818   45.885  1.00 51.98  ? 519  GLN A OE1 1 
ATOM   3661 N NE2 . GLN A 1 493 ? -60.422  7.293   47.506  1.00 56.26  ? 519  GLN A NE2 1 
ATOM   3662 N N   . VAL A 1 494 ? -63.374  6.131   51.092  1.00 51.22  ? 520  VAL A N   1 
ATOM   3663 C CA  . VAL A 1 494 ? -64.544  6.965   51.317  1.00 46.80  ? 520  VAL A CA  1 
ATOM   3664 C C   . VAL A 1 494 ? -64.482  8.076   50.286  1.00 55.63  ? 520  VAL A C   1 
ATOM   3665 O O   . VAL A 1 494 ? -63.655  8.965   50.408  1.00 54.84  ? 520  VAL A O   1 
ATOM   3666 C CB  . VAL A 1 494 ? -64.534  7.628   52.704  1.00 50.32  ? 520  VAL A CB  1 
ATOM   3667 C CG1 . VAL A 1 494 ? -65.598  8.696   52.774  1.00 51.34  ? 520  VAL A CG1 1 
ATOM   3668 C CG2 . VAL A 1 494 ? -64.763  6.601   53.814  1.00 51.44  ? 520  VAL A CG2 1 
ATOM   3669 N N   . LEU A 1 495 ? -65.280  7.970   49.218  1.00 63.19  ? 521  LEU A N   1 
ATOM   3670 C CA  . LEU A 1 495 ? -65.305  8.991   48.172  1.00 55.22  ? 521  LEU A CA  1 
ATOM   3671 C C   . LEU A 1 495 ? -65.805  10.274  48.785  1.00 60.81  ? 521  LEU A C   1 
ATOM   3672 O O   . LEU A 1 495 ? -66.795  10.269  49.502  1.00 63.37  ? 521  LEU A O   1 
ATOM   3673 C CB  . LEU A 1 495 ? -66.162  8.558   47.008  1.00 54.00  ? 521  LEU A CB  1 
ATOM   3674 C CG  . LEU A 1 495 ? -65.581  7.398   46.204  1.00 56.17  ? 521  LEU A CG  1 
ATOM   3675 C CD1 . LEU A 1 495 ? -66.571  6.926   45.166  1.00 57.82  ? 521  LEU A CD1 1 
ATOM   3676 C CD2 . LEU A 1 495 ? -64.268  7.766   45.538  1.00 53.92  ? 521  LEU A CD2 1 
ATOM   3677 N N   . SER A 1 496 ? -65.146  11.383  48.470  1.00 63.22  ? 522  SER A N   1 
ATOM   3678 C CA  . SER A 1 496 ? -65.511  12.659  49.081  1.00 70.85  ? 522  SER A CA  1 
ATOM   3679 C C   . SER A 1 496 ? -65.908  13.825  48.190  1.00 72.94  ? 522  SER A C   1 
ATOM   3680 O O   . SER A 1 496 ? -66.305  14.860  48.695  1.00 72.43  ? 522  SER A O   1 
ATOM   3681 C CB  . SER A 1 496 ? -64.362  13.077  49.961  1.00 68.77  ? 522  SER A CB  1 
ATOM   3682 O OG  . SER A 1 496 ? -63.175  13.020  49.211  1.00 58.74  ? 522  SER A OG  1 
ATOM   3683 N N   . GLY A 1 497 ? -65.828  13.662  46.879  1.00 76.83  ? 523  GLY A N   1 
ATOM   3684 C CA  . GLY A 1 497 ? -66.218  14.733  45.970  1.00 63.17  ? 523  GLY A CA  1 
ATOM   3685 C C   . GLY A 1 497 ? -65.077  15.402  45.233  1.00 59.21  ? 523  GLY A C   1 
ATOM   3686 O O   . GLY A 1 497 ? -65.306  16.359  44.502  1.00 60.20  ? 523  GLY A O   1 
ATOM   3687 N N   . THR A 1 498 ? -63.864  14.876  45.378  1.00 51.38  ? 524  THR A N   1 
ATOM   3688 C CA  . THR A 1 498 ? -62.683  15.437  44.715  1.00 52.18  ? 524  THR A CA  1 
ATOM   3689 C C   . THR A 1 498 ? -61.883  14.418  43.911  1.00 54.94  ? 524  THR A C   1 
ATOM   3690 O O   . THR A 1 498 ? -60.997  14.770  43.125  1.00 61.95  ? 524  THR A O   1 
ATOM   3691 C CB  . THR A 1 498 ? -61.675  15.976  45.782  1.00 59.82  ? 524  THR A CB  1 
ATOM   3692 O OG1 . THR A 1 498 ? -61.142  14.888  46.571  1.00 50.61  ? 524  THR A OG1 1 
ATOM   3693 C CG2 . THR A 1 498 ? -62.353  16.987  46.704  1.00 56.88  ? 524  THR A CG2 1 
ATOM   3694 N N   . GLU A 1 499 ? -62.138  13.148  44.153  1.00 61.29  ? 525  GLU A N   1 
ATOM   3695 C CA  . GLU A 1 499 ? -61.380  12.117  43.492  1.00 53.75  ? 525  GLU A CA  1 
ATOM   3696 C C   . GLU A 1 499 ? -61.408  12.179  42.000  1.00 49.49  ? 525  GLU A C   1 
ATOM   3697 O O   . GLU A 1 499 ? -60.430  11.792  41.413  1.00 49.71  ? 525  GLU A O   1 
ATOM   3698 C CB  . GLU A 1 499 ? -61.775  10.711  43.979  1.00 56.95  ? 525  GLU A CB  1 
ATOM   3699 C CG  . GLU A 1 499 ? -61.572  10.466  45.477  1.00 48.64  ? 525  GLU A CG  1 
ATOM   3700 C CD  . GLU A 1 499 ? -62.562  11.220  46.349  1.00 51.76  ? 525  GLU A CD  1 
ATOM   3701 O OE1 . GLU A 1 499 ? -63.648  11.584  45.862  1.00 66.41  ? 525  GLU A OE1 1 
ATOM   3702 O OE2 . GLU A 1 499 ? -62.317  11.362  47.554  1.00 58.28  ? 525  GLU A OE2 1 
ATOM   3703 N N   . PHE A 1 500 ? -62.506  12.661  41.391  1.00 45.13  ? 526  PHE A N   1 
ATOM   3704 C CA  . PHE A 1 500 ? -62.626  12.739  39.911  1.00 46.70  ? 526  PHE A CA  1 
ATOM   3705 C C   . PHE A 1 500 ? -62.590  14.173  39.314  1.00 56.33  ? 526  PHE A C   1 
ATOM   3706 O O   . PHE A 1 500 ? -63.001  14.417  38.161  1.00 49.60  ? 526  PHE A O   1 
ATOM   3707 C CB  . PHE A 1 500 ? -63.920  12.063  39.448  1.00 51.23  ? 526  PHE A CB  1 
ATOM   3708 C CG  . PHE A 1 500 ? -64.018  10.604  39.800  1.00 48.91  ? 526  PHE A CG  1 
ATOM   3709 C CD1 . PHE A 1 500 ? -64.665  10.201  40.942  1.00 57.16  ? 526  PHE A CD1 1 
ATOM   3710 C CD2 . PHE A 1 500 ? -63.493  9.646   38.975  1.00 55.42  ? 526  PHE A CD2 1 
ATOM   3711 C CE1 . PHE A 1 500 ? -64.725  8.870   41.287  1.00 49.10  ? 526  PHE A CE1 1 
ATOM   3712 C CE2 . PHE A 1 500 ? -63.587  8.301   39.291  1.00 51.28  ? 526  PHE A CE2 1 
ATOM   3713 C CZ  . PHE A 1 500 ? -64.185  7.924   40.455  1.00 49.38  ? 526  PHE A CZ  1 
ATOM   3714 N N   . SER A 1 501 ? -61.976  15.095  40.028  1.00 59.58  ? 527  SER A N   1 
ATOM   3715 C CA  . SER A 1 501 ? -61.915  16.461  39.561  1.00 55.72  ? 527  SER A CA  1 
ATOM   3716 C C   . SER A 1 501 ? -61.206  16.609  38.202  1.00 51.72  ? 527  SER A C   1 
ATOM   3717 O O   . SER A 1 501 ? -61.577  17.471  37.433  1.00 65.77  ? 527  SER A O   1 
ATOM   3718 C CB  . SER A 1 501 ? -61.224  17.327  40.599  1.00 56.44  ? 527  SER A CB  1 
ATOM   3719 O OG  . SER A 1 501 ? -59.862  16.960  40.728  1.00 66.28  ? 527  SER A OG  1 
ATOM   3720 N N   . ALA A 1 502 ? -60.180  15.798  37.931  1.00 45.05  ? 528  ALA A N   1 
ATOM   3721 C CA  . ALA A 1 502 ? -59.436  15.858  36.653  1.00 43.69  ? 528  ALA A CA  1 
ATOM   3722 C C   . ALA A 1 502 ? -60.168  15.261  35.459  1.00 52.61  ? 528  ALA A C   1 
ATOM   3723 O O   . ALA A 1 502 ? -59.694  15.389  34.343  1.00 57.18  ? 528  ALA A O   1 
ATOM   3724 C CB  . ALA A 1 502 ? -58.049  15.218  36.766  1.00 40.76  ? 528  ALA A CB  1 
ATOM   3725 N N   . ILE A 1 503 ? -61.248  14.519  35.696  1.00 53.66  ? 529  ILE A N   1 
ATOM   3726 C CA  . ILE A 1 503 ? -62.035  13.938  34.597  1.00 48.00  ? 529  ILE A CA  1 
ATOM   3727 C C   . ILE A 1 503 ? -63.469  14.113  35.026  1.00 56.52  ? 529  ILE A C   1 
ATOM   3728 O O   . ILE A 1 503 ? -64.206  13.164  35.227  1.00 57.81  ? 529  ILE A O   1 
ATOM   3729 C CB  . ILE A 1 503 ? -61.697  12.483  34.350  1.00 45.52  ? 529  ILE A CB  1 
ATOM   3730 C CG1 . ILE A 1 503 ? -61.781  11.691  35.660  1.00 52.28  ? 529  ILE A CG1 1 
ATOM   3731 C CG2 . ILE A 1 503 ? -60.265  12.358  33.833  1.00 46.92  ? 529  ILE A CG2 1 
ATOM   3732 C CD1 . ILE A 1 503 ? -61.477  10.212  35.501  1.00 54.68  ? 529  ILE A CD1 1 
ATOM   3733 N N   . PRO A 1 504 ? -63.889  15.362  35.117  1.00 58.57  ? 530  PRO A N   1 
ATOM   3734 C CA  . PRO A 1 504 ? -65.222  15.636  35.586  1.00 57.82  ? 530  PRO A CA  1 
ATOM   3735 C C   . PRO A 1 504 ? -66.306  15.429  34.585  1.00 56.93  ? 530  PRO A C   1 
ATOM   3736 O O   . PRO A 1 504 ? -67.465  15.596  34.935  1.00 55.86  ? 530  PRO A O   1 
ATOM   3737 C CB  . PRO A 1 504 ? -65.143  17.105  35.984  1.00 56.84  ? 530  PRO A CB  1 
ATOM   3738 C CG  . PRO A 1 504 ? -64.081  17.682  35.096  1.00 50.56  ? 530  PRO A CG  1 
ATOM   3739 C CD  . PRO A 1 504 ? -63.225  16.563  34.588  1.00 49.45  ? 530  PRO A CD  1 
ATOM   3740 N N   . HIS A 1 505 ? -65.986  14.999  33.372  1.00 55.94  ? 531  HIS A N   1 
ATOM   3741 C CA  . HIS A 1 505 ? -67.079  14.813  32.412  1.00 60.49  ? 531  HIS A CA  1 
ATOM   3742 C C   . HIS A 1 505 ? -67.492  13.358  32.191  1.00 56.85  ? 531  HIS A C   1 
ATOM   3743 O O   . HIS A 1 505 ? -68.208  13.038  31.254  1.00 63.78  ? 531  HIS A O   1 
ATOM   3744 C CB  . HIS A 1 505 ? -66.796  15.555  31.108  1.00 63.53  ? 531  HIS A CB  1 
ATOM   3745 C CG  . HIS A 1 505 ? -66.385  16.982  31.325  1.00 71.99  ? 531  HIS A CG  1 
ATOM   3746 N ND1 . HIS A 1 505 ? -67.217  17.915  31.910  1.00 72.44  ? 531  HIS A ND1 1 
ATOM   3747 C CD2 . HIS A 1 505 ? -65.239  17.637  31.022  1.00 61.72  ? 531  HIS A CD2 1 
ATOM   3748 C CE1 . HIS A 1 505 ? -66.588  19.072  31.995  1.00 61.98  ? 531  HIS A CE1 1 
ATOM   3749 N NE2 . HIS A 1 505 ? -65.385  18.928  31.468  1.00 67.52  ? 531  HIS A NE2 1 
ATOM   3750 N N   . VAL A 1 506 ? -67.165  12.501  33.138  1.00 54.85  ? 532  VAL A N   1 
ATOM   3751 C CA  . VAL A 1 506 ? -67.538  11.123  33.014  1.00 49.01  ? 532  VAL A CA  1 
ATOM   3752 C C   . VAL A 1 506 ? -69.042  11.022  33.019  1.00 46.97  ? 532  VAL A C   1 
ATOM   3753 O O   . VAL A 1 506 ? -69.706  11.665  33.837  1.00 47.39  ? 532  VAL A O   1 
ATOM   3754 C CB  . VAL A 1 506 ? -66.976  10.302  34.164  1.00 48.87  ? 532  VAL A CB  1 
ATOM   3755 C CG1 . VAL A 1 506 ? -67.535  8.894   34.113  1.00 42.51  ? 532  VAL A CG1 1 
ATOM   3756 C CG2 . VAL A 1 506 ? -65.451  10.296  34.108  1.00 46.55  ? 532  VAL A CG2 1 
ATOM   3757 N N   . LYS A 1 507 ? -69.586  10.231  32.096  1.00 48.31  ? 533  LYS A N   1 
ATOM   3758 C CA  . LYS A 1 507 ? -71.048  10.051  31.991  1.00 52.26  ? 533  LYS A CA  1 
ATOM   3759 C C   . LYS A 1 507 ? -71.506  8.705   32.543  1.00 50.19  ? 533  LYS A C   1 
ATOM   3760 O O   . LYS A 1 507 ? -72.637  8.552   33.033  1.00 43.86  ? 533  LYS A O   1 
ATOM   3761 C CB  . LYS A 1 507 ? -71.437  10.049  30.530  1.00 64.78  ? 533  LYS A CB  1 
ATOM   3762 C CG  . LYS A 1 507 ? -71.092  11.281  29.739  1.00 68.11  ? 533  LYS A CG  1 
ATOM   3763 C CD  . LYS A 1 507 ? -71.875  12.488  30.189  1.00 76.13  ? 533  LYS A CD  1 
ATOM   3764 C CE  . LYS A 1 507 ? -71.599  13.637  29.240  1.00 84.46  ? 533  LYS A CE  1 
ATOM   3765 N NZ  . LYS A 1 507 ? -72.084  13.319  27.869  1.00 88.52  ? 533  LYS A NZ  1 
ATOM   3766 N N   . TYR A 1 508 ? -70.675  7.702   32.306  1.00 49.67  ? 534  TYR A N   1 
ATOM   3767 C CA  . TYR A 1 508 ? -70.956  6.357   32.737  1.00 53.00  ? 534  TYR A CA  1 
ATOM   3768 C C   . TYR A 1 508 ? -69.792  5.934   33.634  1.00 46.65  ? 534  TYR A C   1 
ATOM   3769 O O   . TYR A 1 508 ? -68.633  5.888   33.188  1.00 41.15  ? 534  TYR A O   1 
ATOM   3770 C CB  . TYR A 1 508 ? -71.019  5.442   31.509  1.00 53.86  ? 534  TYR A CB  1 
ATOM   3771 C CG  . TYR A 1 508 ? -71.577  4.056   31.761  1.00 56.12  ? 534  TYR A CG  1 
ATOM   3772 C CD1 . TYR A 1 508 ? -70.893  3.130   32.528  1.00 62.59  ? 534  TYR A CD1 1 
ATOM   3773 C CD2 . TYR A 1 508 ? -72.684  3.616   31.067  1.00 59.92  ? 534  TYR A CD2 1 
ATOM   3774 C CE1 . TYR A 1 508 ? -71.388  1.850   32.707  1.00 61.79  ? 534  TYR A CE1 1 
ATOM   3775 C CE2 . TYR A 1 508 ? -73.182  2.349   31.243  1.00 61.03  ? 534  TYR A CE2 1 
ATOM   3776 C CZ  . TYR A 1 508 ? -72.526  1.473   32.056  1.00 59.40  ? 534  TYR A CZ  1 
ATOM   3777 O OH  . TYR A 1 508 ? -73.010  0.212   32.180  1.00 54.98  ? 534  TYR A OH  1 
ATOM   3778 N N   . LEU A 1 509 ? -70.087  5.642   34.893  1.00 41.34  ? 535  LEU A N   1 
ATOM   3779 C CA  . LEU A 1 509 ? -69.035  5.230   35.823  1.00 43.05  ? 535  LEU A CA  1 
ATOM   3780 C C   . LEU A 1 509 ? -69.347  3.872   36.420  1.00 41.44  ? 535  LEU A C   1 
ATOM   3781 O O   . LEU A 1 509 ? -70.400  3.686   37.037  1.00 41.02  ? 535  LEU A O   1 
ATOM   3782 C CB  . LEU A 1 509 ? -68.928  6.242   36.957  1.00 43.91  ? 535  LEU A CB  1 
ATOM   3783 C CG  . LEU A 1 509 ? -67.905  5.942   38.036  1.00 46.52  ? 535  LEU A CG  1 
ATOM   3784 C CD1 . LEU A 1 509 ? -66.521  5.864   37.402  1.00 49.01  ? 535  LEU A CD1 1 
ATOM   3785 C CD2 . LEU A 1 509 ? -67.957  7.027   39.111  1.00 43.13  ? 535  LEU A CD2 1 
ATOM   3786 N N   . ASP A 1 510 ? -68.415  2.944   36.260  1.00 44.06  ? 536  ASP A N   1 
ATOM   3787 C CA  . ASP A 1 510 ? -68.562  1.603   36.790  1.00 48.90  ? 536  ASP A CA  1 
ATOM   3788 C C   . ASP A 1 510 ? -67.640  1.417   38.005  1.00 47.22  ? 536  ASP A C   1 
ATOM   3789 O O   . ASP A 1 510 ? -66.422  1.378   37.874  1.00 41.69  ? 536  ASP A O   1 
ATOM   3790 C CB  . ASP A 1 510 ? -68.256  0.572   35.716  1.00 47.82  ? 536  ASP A CB  1 
ATOM   3791 C CG  . ASP A 1 510 ? -68.604  -0.839  36.149  1.00 58.34  ? 536  ASP A CG  1 
ATOM   3792 O OD1 . ASP A 1 510 ? -68.638  -1.104  37.376  1.00 49.80  ? 536  ASP A OD1 1 
ATOM   3793 O OD2 . ASP A 1 510 ? -68.834  -1.686  35.250  1.00 63.33  ? 536  ASP A OD2 1 
ATOM   3794 N N   . LEU A 1 511 ? -68.255  1.270   39.153  1.00 40.48  ? 537  LEU A N   1 
ATOM   3795 C CA  . LEU A 1 511 ? -67.550  1.105   40.380  1.00 45.52  ? 537  LEU A CA  1 
ATOM   3796 C C   . LEU A 1 511 ? -67.887  -0.219  41.011  1.00 45.53  ? 537  LEU A C   1 
ATOM   3797 O O   . LEU A 1 511 ? -67.784  -0.359  42.184  1.00 43.33  ? 537  LEU A O   1 
ATOM   3798 C CB  . LEU A 1 511 ? -67.919  2.230   41.321  1.00 43.49  ? 537  LEU A CB  1 
ATOM   3799 C CG  . LEU A 1 511 ? -67.330  3.589   41.013  1.00 44.19  ? 537  LEU A CG  1 
ATOM   3800 C CD1 . LEU A 1 511 ? -67.733  4.583   42.054  1.00 49.35  ? 537  LEU A CD1 1 
ATOM   3801 C CD2 . LEU A 1 511 ? -65.835  3.508   40.976  1.00 50.19  ? 537  LEU A CD2 1 
ATOM   3802 N N   . THR A 1 512 ? -68.335  -1.180  40.232  1.00 38.96  ? 538  THR A N   1 
ATOM   3803 C CA  . THR A 1 512 ? -68.797  -2.429  40.774  1.00 34.94  ? 538  THR A CA  1 
ATOM   3804 C C   . THR A 1 512 ? -67.692  -3.262  41.341  1.00 43.64  ? 538  THR A C   1 
ATOM   3805 O O   . THR A 1 512 ? -66.550  -3.095  41.007  1.00 38.16  ? 538  THR A O   1 
ATOM   3806 C CB  . THR A 1 512 ? -69.502  -3.269  39.727  1.00 37.40  ? 538  THR A CB  1 
ATOM   3807 O OG1 . THR A 1 512 ? -68.583  -3.625  38.714  1.00 38.76  ? 538  THR A OG1 1 
ATOM   3808 C CG2 . THR A 1 512 ? -70.569  -2.526  39.133  1.00 36.23  ? 538  THR A CG2 1 
ATOM   3809 N N   . ASN A 1 513 ? -68.071  -4.174  42.212  1.00 41.64  ? 539  ASN A N   1 
ATOM   3810 C CA  . ASN A 1 513 ? -67.175  -5.134  42.811  1.00 44.13  ? 539  ASN A CA  1 
ATOM   3811 C C   . ASN A 1 513 ? -65.978  -4.615  43.564  1.00 37.11  ? 539  ASN A C   1 
ATOM   3812 O O   . ASN A 1 513 ? -64.883  -5.060  43.377  1.00 43.88  ? 539  ASN A O   1 
ATOM   3813 C CB  . ASN A 1 513 ? -66.772  -6.198  41.812  1.00 43.86  ? 539  ASN A CB  1 
ATOM   3814 C CG  . ASN A 1 513 ? -66.434  -7.491  42.476  1.00 55.81  ? 539  ASN A CG  1 
ATOM   3815 O OD1 . ASN A 1 513 ? -66.635  -7.645  43.659  1.00 65.37  ? 539  ASN A OD1 1 
ATOM   3816 N ND2 . ASN A 1 513 ? -65.906  -8.418  41.731  1.00 69.55  ? 539  ASN A ND2 1 
ATOM   3817 N N   . ASN A 1 514 ? -66.225  -3.666  44.436  1.00 40.24  ? 540  ASN A N   1 
ATOM   3818 C CA  . ASN A 1 514 ? -65.213  -3.051  45.260  1.00 40.24  ? 540  ASN A CA  1 
ATOM   3819 C C   . ASN A 1 514 ? -65.738  -3.085  46.663  1.00 41.21  ? 540  ASN A C   1 
ATOM   3820 O O   . ASN A 1 514 ? -66.682  -3.760  46.899  1.00 42.00  ? 540  ASN A O   1 
ATOM   3821 C CB  . ASN A 1 514 ? -64.973  -1.634  44.810  1.00 39.78  ? 540  ASN A CB  1 
ATOM   3822 C CG  . ASN A 1 514 ? -64.061  -1.555  43.645  1.00 37.52  ? 540  ASN A CG  1 
ATOM   3823 O OD1 . ASN A 1 514 ? -62.920  -1.876  43.738  1.00 43.82  ? 540  ASN A OD1 1 
ATOM   3824 N ND2 . ASN A 1 514 ? -64.565  -1.123  42.551  1.00 39.15  ? 540  ASN A ND2 1 
ATOM   3825 N N   . ARG A 1 515 ? -65.103  -2.417  47.607  1.00 46.66  ? 541  ARG A N   1 
ATOM   3826 C CA  . ARG A 1 515 ? -65.678  -2.298  48.933  1.00 47.41  ? 541  ARG A CA  1 
ATOM   3827 C C   . ARG A 1 515 ? -65.711  -0.875  49.382  1.00 48.83  ? 541  ARG A C   1 
ATOM   3828 O O   . ARG A 1 515 ? -65.273  -0.533  50.435  1.00 54.57  ? 541  ARG A O   1 
ATOM   3829 C CB  . ARG A 1 515 ? -64.966  -3.168  49.946  1.00 47.19  ? 541  ARG A CB  1 
ATOM   3830 C CG  . ARG A 1 515 ? -63.654  -3.714  49.520  1.00 49.42  ? 541  ARG A CG  1 
ATOM   3831 C CD  . ARG A 1 515 ? -63.081  -4.470  50.677  1.00 60.45  ? 541  ARG A CD  1 
ATOM   3832 N NE  . ARG A 1 515 ? -63.362  -5.884  50.606  1.00 62.20  ? 541  ARG A NE  1 
ATOM   3833 C CZ  . ARG A 1 515 ? -62.829  -6.772  51.414  1.00 62.52  ? 541  ARG A CZ  1 
ATOM   3834 N NH1 . ARG A 1 515 ? -62.002  -6.391  52.340  1.00 67.55  ? 541  ARG A NH1 1 
ATOM   3835 N NH2 . ARG A 1 515 ? -63.121  -8.034  51.293  1.00 54.83  ? 541  ARG A NH2 1 
ATOM   3836 N N   . LEU A 1 516 ? -66.329  -0.054  48.577  1.00 51.45  ? 542  LEU A N   1 
ATOM   3837 C CA  . LEU A 1 516 ? -66.410  1.372   48.852  1.00 50.35  ? 542  LEU A CA  1 
ATOM   3838 C C   . LEU A 1 516 ? -67.195  1.649   50.103  1.00 50.88  ? 542  LEU A C   1 
ATOM   3839 O O   . LEU A 1 516 ? -68.172  0.965   50.429  1.00 54.35  ? 542  LEU A O   1 
ATOM   3840 C CB  . LEU A 1 516 ? -66.996  2.124   47.667  1.00 46.21  ? 542  LEU A CB  1 
ATOM   3841 C CG  . LEU A 1 516 ? -66.176  2.035   46.376  1.00 44.63  ? 542  LEU A CG  1 
ATOM   3842 C CD1 . LEU A 1 516 ? -67.024  2.408   45.159  1.00 48.15  ? 542  LEU A CD1 1 
ATOM   3843 C CD2 . LEU A 1 516 ? -64.905  2.872   46.460  1.00 49.46  ? 542  LEU A CD2 1 
ATOM   3844 N N   . ASP A 1 517 ? -66.760  2.697   50.783  1.00 55.51  ? 543  ASP A N   1 
ATOM   3845 C CA  . ASP A 1 517 ? -67.331  3.119   52.018  1.00 52.17  ? 543  ASP A CA  1 
ATOM   3846 C C   . ASP A 1 517 ? -68.017  4.442   51.810  1.00 51.41  ? 543  ASP A C   1 
ATOM   3847 O O   . ASP A 1 517 ? -67.384  5.482   51.776  1.00 57.03  ? 543  ASP A O   1 
ATOM   3848 C CB  . ASP A 1 517 ? -66.212  3.240   53.047  1.00 59.14  ? 543  ASP A CB  1 
ATOM   3849 C CG  . ASP A 1 517 ? -66.712  3.648   54.445  1.00 70.83  ? 543  ASP A CG  1 
ATOM   3850 O OD1 . ASP A 1 517 ? -67.955  3.835   54.667  1.00 65.51  ? 543  ASP A OD1 1 
ATOM   3851 O OD2 . ASP A 1 517 ? -65.831  3.766   55.328  1.00 60.35  ? 543  ASP A OD2 1 
ATOM   3852 N N   . PHE A 1 518 ? -69.329  4.378   51.687  1.00 48.64  ? 544  PHE A N   1 
ATOM   3853 C CA  . PHE A 1 518 ? -70.144  5.538   51.479  1.00 56.32  ? 544  PHE A CA  1 
ATOM   3854 C C   . PHE A 1 518 ? -70.431  6.253   52.756  1.00 58.68  ? 544  PHE A C   1 
ATOM   3855 O O   . PHE A 1 518 ? -71.543  6.199   53.285  1.00 57.33  ? 544  PHE A O   1 
ATOM   3856 C CB  . PHE A 1 518 ? -71.421  5.166   50.717  1.00 60.27  ? 544  PHE A CB  1 
ATOM   3857 C CG  . PHE A 1 518 ? -71.135  4.742   49.331  1.00 54.34  ? 544  PHE A CG  1 
ATOM   3858 C CD1 . PHE A 1 518 ? -70.815  5.696   48.379  1.00 56.19  ? 544  PHE A CD1 1 
ATOM   3859 C CD2 . PHE A 1 518 ? -71.033  3.410   49.008  1.00 58.08  ? 544  PHE A CD2 1 
ATOM   3860 C CE1 . PHE A 1 518 ? -70.446  5.330   47.106  1.00 61.15  ? 544  PHE A CE1 1 
ATOM   3861 C CE2 . PHE A 1 518 ? -70.654  3.030   47.740  1.00 60.65  ? 544  PHE A CE2 1 
ATOM   3862 C CZ  . PHE A 1 518 ? -70.351  3.990   46.787  1.00 60.66  ? 544  PHE A CZ  1 
ATOM   3863 N N   . ASP A 1 519 ? -69.439  7.011   53.202  1.00 65.49  ? 545  ASP A N   1 
ATOM   3864 C CA  . ASP A 1 519 ? -69.577  7.732   54.438  1.00 69.13  ? 545  ASP A CA  1 
ATOM   3865 C C   . ASP A 1 519 ? -69.332  9.223   54.274  1.00 70.11  ? 545  ASP A C   1 
ATOM   3866 O O   . ASP A 1 519 ? -68.708  9.836   55.122  1.00 79.27  ? 545  ASP A O   1 
ATOM   3867 C CB  . ASP A 1 519 ? -68.579  7.181   55.425  1.00 64.40  ? 545  ASP A CB  1 
ATOM   3868 C CG  . ASP A 1 519 ? -68.888  7.587   56.811  1.00 73.17  ? 545  ASP A CG  1 
ATOM   3869 O OD1 . ASP A 1 519 ? -70.102  7.709   57.124  1.00 66.66  ? 545  ASP A OD1 1 
ATOM   3870 O OD2 . ASP A 1 519 ? -67.938  7.663   57.608  1.00 87.75  ? 545  ASP A OD2 1 
ATOM   3871 N N   . ASN A 1 520 ? -69.813  9.795   53.174  1.00 78.51  ? 546  ASN A N   1 
ATOM   3872 C CA  . ASN A 1 520 ? -69.648  11.226  52.888  1.00 63.39  ? 546  ASN A CA  1 
ATOM   3873 C C   . ASN A 1 520 ? -70.616  11.686  51.781  1.00 60.20  ? 546  ASN A C   1 
ATOM   3874 O O   . ASN A 1 520 ? -70.468  11.348  50.609  1.00 66.08  ? 546  ASN A O   1 
ATOM   3875 C CB  . ASN A 1 520 ? -68.195  11.549  52.534  1.00 60.68  ? 546  ASN A CB  1 
ATOM   3876 C CG  . ASN A 1 520 ? -67.965  13.038  52.284  1.00 65.77  ? 546  ASN A CG  1 
ATOM   3877 O OD1 . ASN A 1 520 ? -68.602  13.652  51.428  1.00 67.82  ? 546  ASN A OD1 1 
ATOM   3878 N ND2 . ASN A 1 520 ? -67.007  13.600  52.986  1.00 69.80  ? 546  ASN A ND2 1 
ATOM   3879 N N   . ALA A 1 521 ? -71.604  12.461  52.199  1.00 59.38  ? 547  ALA A N   1 
ATOM   3880 C CA  . ALA A 1 521 ? -72.641  12.997  51.338  1.00 68.92  ? 547  ALA A CA  1 
ATOM   3881 C C   . ALA A 1 521 ? -72.165  13.711  50.053  1.00 68.29  ? 547  ALA A C   1 
ATOM   3882 O O   . ALA A 1 521 ? -72.952  13.913  49.136  1.00 68.41  ? 547  ALA A O   1 
ATOM   3883 C CB  . ALA A 1 521 ? -73.541  13.923  52.156  1.00 63.12  ? 547  ALA A CB  1 
ATOM   3884 N N   . SER A 1 522 ? -70.911  14.127  49.999  1.00 55.10  ? 548  SER A N   1 
ATOM   3885 C CA  . SER A 1 522 ? -70.412  14.810  48.809  1.00 59.95  ? 548  SER A CA  1 
ATOM   3886 C C   . SER A 1 522 ? -69.827  13.841  47.782  1.00 66.22  ? 548  SER A C   1 
ATOM   3887 O O   . SER A 1 522 ? -69.253  14.263  46.770  1.00 52.29  ? 548  SER A O   1 
ATOM   3888 C CB  . SER A 1 522 ? -69.306  15.795  49.216  1.00 60.71  ? 548  SER A CB  1 
ATOM   3889 O OG  . SER A 1 522 ? -69.787  16.750  50.141  1.00 67.34  ? 548  SER A OG  1 
ATOM   3890 N N   . ALA A 1 523 ? -69.918  12.546  48.062  1.00 65.78  ? 549  ALA A N   1 
ATOM   3891 C CA  . ALA A 1 523 ? -69.351  11.542  47.167  1.00 60.25  ? 549  ALA A CA  1 
ATOM   3892 C C   . ALA A 1 523 ? -69.744  11.710  45.706  1.00 54.98  ? 549  ALA A C   1 
ATOM   3893 O O   . ALA A 1 523 ? -70.917  11.850  45.409  1.00 47.26  ? 549  ALA A O   1 
ATOM   3894 C CB  . ALA A 1 523 ? -69.757  10.161  47.634  1.00 55.04  ? 549  ALA A CB  1 
ATOM   3895 N N   . LEU A 1 524 ? -68.749  11.762  44.816  1.00 55.22  ? 550  LEU A N   1 
ATOM   3896 C CA  . LEU A 1 524 ? -68.980  11.840  43.359  1.00 57.87  ? 550  LEU A CA  1 
ATOM   3897 C C   . LEU A 1 524 ? -69.716  13.086  42.808  1.00 63.56  ? 550  LEU A C   1 
ATOM   3898 O O   . LEU A 1 524 ? -69.948  13.196  41.583  1.00 56.71  ? 550  LEU A O   1 
ATOM   3899 C CB  . LEU A 1 524 ? -69.754  10.573  42.930  1.00 56.08  ? 550  LEU A CB  1 
ATOM   3900 C CG  . LEU A 1 524 ? -69.093  9.232   43.282  1.00 53.82  ? 550  LEU A CG  1 
ATOM   3901 C CD1 . LEU A 1 524 ? -70.080  8.100   43.174  1.00 59.46  ? 550  LEU A CD1 1 
ATOM   3902 C CD2 . LEU A 1 524 ? -67.849  8.956   42.452  1.00 49.34  ? 550  LEU A CD2 1 
ATOM   3903 N N   . THR A 1 525 ? -70.040  14.042  43.676  1.00 60.83  ? 551  THR A N   1 
ATOM   3904 C CA  . THR A 1 525 ? -70.741  15.244  43.224  1.00 56.57  ? 551  THR A CA  1 
ATOM   3905 C C   . THR A 1 525 ? -69.923  16.043  42.233  1.00 56.29  ? 551  THR A C   1 
ATOM   3906 O O   . THR A 1 525 ? -70.475  16.801  41.453  1.00 66.93  ? 551  THR A O   1 
ATOM   3907 C CB  . THR A 1 525 ? -71.179  16.144  44.368  1.00 56.12  ? 551  THR A CB  1 
ATOM   3908 O OG1 . THR A 1 525 ? -70.042  16.498  45.150  1.00 58.17  ? 551  THR A OG1 1 
ATOM   3909 C CG2 . THR A 1 525 ? -72.200  15.440  45.231  1.00 57.04  ? 551  THR A CG2 1 
ATOM   3910 N N   . GLU A 1 526 ? -68.626  15.802  42.168  1.00 58.16  ? 552  GLU A N   1 
ATOM   3911 C CA  . GLU A 1 526 ? -67.836  16.527  41.201  1.00 51.94  ? 552  GLU A CA  1 
ATOM   3912 C C   . GLU A 1 526 ? -68.125  16.095  39.780  1.00 54.64  ? 552  GLU A C   1 
ATOM   3913 O O   . GLU A 1 526 ? -67.568  16.680  38.867  1.00 61.46  ? 552  GLU A O   1 
ATOM   3914 C CB  . GLU A 1 526 ? -66.346  16.408  41.440  1.00 47.64  ? 552  GLU A CB  1 
ATOM   3915 C CG  . GLU A 1 526 ? -65.717  15.027  41.257  1.00 61.55  ? 552  GLU A CG  1 
ATOM   3916 C CD  . GLU A 1 526 ? -65.930  14.023  42.401  1.00 60.39  ? 552  GLU A CD  1 
ATOM   3917 O OE1 . GLU A 1 526 ? -67.046  13.908  42.986  1.00 47.57  ? 552  GLU A OE1 1 
ATOM   3918 O OE2 . GLU A 1 526 ? -64.955  13.261  42.620  1.00 54.67  ? 552  GLU A OE2 1 
ATOM   3919 N N   . LEU A 1 527 ? -68.869  14.998  39.589  1.00 60.55  ? 553  LEU A N   1 
ATOM   3920 C CA  . LEU A 1 527 ? -69.223  14.507  38.220  1.00 52.62  ? 553  LEU A CA  1 
ATOM   3921 C C   . LEU A 1 527 ? -70.625  15.008  37.838  1.00 57.86  ? 553  LEU A C   1 
ATOM   3922 O O   . LEU A 1 527 ? -71.617  14.260  37.797  1.00 52.16  ? 553  LEU A O   1 
ATOM   3923 C CB  . LEU A 1 527 ? -69.189  12.993  38.160  1.00 47.66  ? 553  LEU A CB  1 
ATOM   3924 C CG  . LEU A 1 527 ? -67.854  12.338  38.412  1.00 49.63  ? 553  LEU A CG  1 
ATOM   3925 C CD1 . LEU A 1 527 ? -68.012  10.826  38.470  1.00 48.57  ? 553  LEU A CD1 1 
ATOM   3926 C CD2 . LEU A 1 527 ? -66.842  12.736  37.355  1.00 52.99  ? 553  LEU A CD2 1 
ATOM   3927 N N   . SER A 1 528 ? -70.695  16.304  37.608  1.00 61.89  ? 554  SER A N   1 
ATOM   3928 C CA  . SER A 1 528 ? -71.926  16.984  37.251  1.00 56.11  ? 554  SER A CA  1 
ATOM   3929 C C   . SER A 1 528 ? -72.663  16.392  36.070  1.00 51.63  ? 554  SER A C   1 
ATOM   3930 O O   . SER A 1 528 ? -73.879  16.410  36.058  1.00 56.17  ? 554  SER A O   1 
ATOM   3931 C CB  . SER A 1 528 ? -71.586  18.432  36.983  1.00 57.06  ? 554  SER A CB  1 
ATOM   3932 O OG  . SER A 1 528 ? -70.461  18.464  36.125  1.00 79.00  ? 554  SER A OG  1 
ATOM   3933 N N   . ASP A 1 529 ? -71.949  15.782  35.127  1.00 48.61  ? 555  ASP A N   1 
ATOM   3934 C CA  . ASP A 1 529 ? -72.590  15.191  33.931  1.00 52.32  ? 555  ASP A CA  1 
ATOM   3935 C C   . ASP A 1 529 ? -73.010  13.725  34.049  1.00 59.12  ? 555  ASP A C   1 
ATOM   3936 O O   . ASP A 1 529 ? -73.641  13.182  33.140  1.00 68.86  ? 555  ASP A O   1 
ATOM   3937 C CB  . ASP A 1 529 ? -71.617  15.274  32.748  1.00 58.54  ? 555  ASP A CB  1 
ATOM   3938 C CG  . ASP A 1 529 ? -71.198  16.703  32.427  1.00 64.46  ? 555  ASP A CG  1 
ATOM   3939 O OD1 . ASP A 1 529 ? -71.971  17.618  32.711  1.00 63.37  ? 555  ASP A OD1 1 
ATOM   3940 O OD2 . ASP A 1 529 ? -70.129  16.904  31.818  1.00 71.76  ? 555  ASP A OD2 1 
ATOM   3941 N N   . LEU A 1 530 ? -72.685  13.084  35.161  1.00 59.59  ? 556  LEU A N   1 
ATOM   3942 C CA  . LEU A 1 530 ? -72.985  11.675  35.323  1.00 55.51  ? 556  LEU A CA  1 
ATOM   3943 C C   . LEU A 1 530 ? -74.418  11.230  34.939  1.00 50.51  ? 556  LEU A C   1 
ATOM   3944 O O   . LEU A 1 530 ? -75.390  11.753  35.445  1.00 51.94  ? 556  LEU A O   1 
ATOM   3945 C CB  . LEU A 1 530 ? -72.712  11.291  36.747  1.00 55.76  ? 556  LEU A CB  1 
ATOM   3946 C CG  . LEU A 1 530 ? -72.611  9.799   37.003  1.00 50.31  ? 556  LEU A CG  1 
ATOM   3947 C CD1 . LEU A 1 530 ? -71.326  9.274   36.361  1.00 47.61  ? 556  LEU A CD1 1 
ATOM   3948 C CD2 . LEU A 1 530 ? -72.570  9.583   38.503  1.00 53.55  ? 556  LEU A CD2 1 
ATOM   3949 N N   . GLU A 1 531 ? -74.536  10.211  34.094  1.00 53.96  ? 557  GLU A N   1 
ATOM   3950 C CA  . GLU A 1 531 ? -75.869  9.725   33.680  1.00 58.86  ? 557  GLU A CA  1 
ATOM   3951 C C   . GLU A 1 531 ? -76.088  8.296   34.112  1.00 54.01  ? 557  GLU A C   1 
ATOM   3952 O O   . GLU A 1 531 ? -77.221  7.885   34.369  1.00 52.25  ? 557  GLU A O   1 
ATOM   3953 C CB  . GLU A 1 531 ? -76.102  9.867   32.171  1.00 60.65  ? 557  GLU A CB  1 
ATOM   3954 C CG  . GLU A 1 531 ? -76.088  11.310  31.647  1.00 66.70  ? 557  GLU A CG  1 
ATOM   3955 C CD  . GLU A 1 531 ? -76.280  11.397  30.132  1.00 66.57  ? 557  GLU A CD  1 
ATOM   3956 O OE1 . GLU A 1 531 ? -76.942  10.507  29.569  1.00 65.06  ? 557  GLU A OE1 1 
ATOM   3957 O OE2 . GLU A 1 531 ? -75.770  12.352  29.504  1.00 65.20  ? 557  GLU A OE2 1 
ATOM   3958 N N   . VAL A 1 532 ? -75.015  7.522   34.167  1.00 50.88  ? 558  VAL A N   1 
ATOM   3959 C CA  . VAL A 1 532 ? -75.131  6.147   34.610  1.00 50.52  ? 558  VAL A CA  1 
ATOM   3960 C C   . VAL A 1 532 ? -74.063  5.846   35.670  1.00 52.13  ? 558  VAL A C   1 
ATOM   3961 O O   . VAL A 1 532 ? -72.838  5.995   35.435  1.00 47.87  ? 558  VAL A O   1 
ATOM   3962 C CB  . VAL A 1 532 ? -74.966  5.144   33.463  1.00 51.46  ? 558  VAL A CB  1 
ATOM   3963 C CG1 . VAL A 1 532 ? -75.170  3.744   33.979  1.00 47.79  ? 558  VAL A CG1 1 
ATOM   3964 C CG2 . VAL A 1 532 ? -75.945  5.417   32.348  1.00 47.18  ? 558  VAL A CG2 1 
ATOM   3965 N N   . LEU A 1 533 ? -74.540  5.386   36.818  1.00 47.67  ? 559  LEU A N   1 
ATOM   3966 C CA  . LEU A 1 533 ? -73.687  5.034   37.939  1.00 43.50  ? 559  LEU A CA  1 
ATOM   3967 C C   . LEU A 1 533 ? -74.002  3.628   38.380  1.00 47.98  ? 559  LEU A C   1 
ATOM   3968 O O   . LEU A 1 533 ? -75.134  3.331   38.798  1.00 50.60  ? 559  LEU A O   1 
ATOM   3969 C CB  . LEU A 1 533 ? -73.943  5.975   39.131  1.00 42.94  ? 559  LEU A CB  1 
ATOM   3970 C CG  . LEU A 1 533 ? -73.118  5.739   40.400  1.00 42.97  ? 559  LEU A CG  1 
ATOM   3971 C CD1 . LEU A 1 533 ? -71.623  5.746   40.131  1.00 46.98  ? 559  LEU A CD1 1 
ATOM   3972 C CD2 . LEU A 1 533 ? -73.441  6.772   41.432  1.00 45.69  ? 559  LEU A CD2 1 
ATOM   3973 N N   . ASP A 1 534 ? -73.009  2.757   38.309  1.00 46.47  ? 560  ASP A N   1 
ATOM   3974 C CA  . ASP A 1 534 ? -73.203  1.397   38.752  1.00 42.67  ? 560  ASP A CA  1 
ATOM   3975 C C   . ASP A 1 534 ? -72.350  1.141   40.031  1.00 44.24  ? 560  ASP A C   1 
ATOM   3976 O O   . ASP A 1 534 ? -71.110  1.153   39.961  1.00 46.63  ? 560  ASP A O   1 
ATOM   3977 C CB  . ASP A 1 534 ? -72.804  0.431   37.661  1.00 41.70  ? 560  ASP A CB  1 
ATOM   3978 C CG  . ASP A 1 534 ? -73.242  -1.006  37.969  1.00 47.80  ? 560  ASP A CG  1 
ATOM   3979 O OD1 . ASP A 1 534 ? -73.898  -1.200  39.022  1.00 48.23  ? 560  ASP A OD1 1 
ATOM   3980 O OD2 . ASP A 1 534 ? -73.030  -1.906  37.110  1.00 49.66  ? 560  ASP A OD2 1 
ATOM   3981 N N   . LEU A 1 535 ? -73.025  0.978   41.178  1.00 41.35  ? 561  LEU A N   1 
ATOM   3982 C CA  . LEU A 1 535 ? -72.371  0.703   42.476  1.00 47.85  ? 561  LEU A CA  1 
ATOM   3983 C C   . LEU A 1 535 ? -72.630  -0.730  42.966  1.00 53.24  ? 561  LEU A C   1 
ATOM   3984 O O   . LEU A 1 535 ? -72.568  -0.995  44.157  1.00 53.12  ? 561  LEU A O   1 
ATOM   3985 C CB  . LEU A 1 535 ? -72.897  1.629   43.564  1.00 44.29  ? 561  LEU A CB  1 
ATOM   3986 C CG  . LEU A 1 535 ? -72.805  3.128   43.320  1.00 52.18  ? 561  LEU A CG  1 
ATOM   3987 C CD1 . LEU A 1 535 ? -73.463  3.923   44.456  1.00 47.03  ? 561  LEU A CD1 1 
ATOM   3988 C CD2 . LEU A 1 535 ? -71.343  3.517   43.151  1.00 52.75  ? 561  LEU A CD2 1 
ATOM   3989 N N   . SER A 1 536 ? -73.021  -1.618  42.069  1.00 48.75  ? 562  SER A N   1 
ATOM   3990 C CA  . SER A 1 536 ? -73.274  -2.986  42.436  1.00 46.38  ? 562  SER A CA  1 
ATOM   3991 C C   . SER A 1 536 ? -72.111  -3.668  43.116  1.00 43.17  ? 562  SER A C   1 
ATOM   3992 O O   . SER A 1 536 ? -70.975  -3.430  42.779  1.00 46.10  ? 562  SER A O   1 
ATOM   3993 C CB  . SER A 1 536 ? -73.616  -3.815  41.199  1.00 46.08  ? 562  SER A CB  1 
ATOM   3994 O OG  . SER A 1 536 ? -74.832  -3.372  40.659  1.00 59.14  ? 562  SER A OG  1 
ATOM   3995 N N   . TYR A 1 537 ? -72.438  -4.611  44.000  1.00 45.18  ? 563  TYR A N   1 
ATOM   3996 C CA  . TYR A 1 537 ? -71.466  -5.414  44.717  1.00 42.95  ? 563  TYR A CA  1 
ATOM   3997 C C   . TYR A 1 537 ? -70.420  -4.674  45.519  1.00 45.08  ? 563  TYR A C   1 
ATOM   3998 O O   . TYR A 1 537 ? -69.209  -4.824  45.295  1.00 39.54  ? 563  TYR A O   1 
ATOM   3999 C CB  . TYR A 1 537 ? -70.794  -6.405  43.774  1.00 48.04  ? 563  TYR A CB  1 
ATOM   4000 C CG  . TYR A 1 537 ? -71.757  -7.393  43.181  1.00 50.99  ? 563  TYR A CG  1 
ATOM   4001 C CD1 . TYR A 1 537 ? -72.112  -8.543  43.879  1.00 50.23  ? 563  TYR A CD1 1 
ATOM   4002 C CD2 . TYR A 1 537 ? -72.307  -7.196  41.911  1.00 58.73  ? 563  TYR A CD2 1 
ATOM   4003 C CE1 . TYR A 1 537 ? -73.033  -9.444  43.364  1.00 51.88  ? 563  TYR A CE1 1 
ATOM   4004 C CE2 . TYR A 1 537 ? -73.192  -8.117  41.369  1.00 58.08  ? 563  TYR A CE2 1 
ATOM   4005 C CZ  . TYR A 1 537 ? -73.551  -9.234  42.104  1.00 56.72  ? 563  TYR A CZ  1 
ATOM   4006 O OH  . TYR A 1 537 ? -74.447  -10.121 41.579  1.00 70.24  ? 563  TYR A OH  1 
ATOM   4007 N N   . ASN A 1 538 ? -70.914  -3.838  46.413  1.00 44.61  ? 564  ASN A N   1 
ATOM   4008 C CA  . ASN A 1 538 ? -70.108  -3.074  47.367  1.00 48.56  ? 564  ASN A CA  1 
ATOM   4009 C C   . ASN A 1 538 ? -70.771  -3.263  48.721  1.00 50.66  ? 564  ASN A C   1 
ATOM   4010 O O   . ASN A 1 538 ? -70.944  -2.316  49.484  1.00 49.86  ? 564  ASN A O   1 
ATOM   4011 C CB  . ASN A 1 538 ? -70.011  -1.598  46.988  1.00 46.40  ? 564  ASN A CB  1 
ATOM   4012 C CG  . ASN A 1 538 ? -68.974  -1.352  45.927  1.00 47.55  ? 564  ASN A CG  1 
ATOM   4013 O OD1 . ASN A 1 538 ? -67.775  -1.463  46.190  1.00 47.22  ? 564  ASN A OD1 1 
ATOM   4014 N ND2 . ASN A 1 538 ? -69.408  -0.890  44.776  1.00 46.11  ? 564  ASN A ND2 1 
ATOM   4015 N N   . SER A 1 539 ? -71.145  -4.508  49.009  1.00 48.43  ? 565  SER A N   1 
ATOM   4016 C CA  . SER A 1 539 ? -71.836  -4.827  50.275  1.00 52.59  ? 565  SER A CA  1 
ATOM   4017 C C   . SER A 1 539 ? -70.994  -4.708  51.540  1.00 48.98  ? 565  SER A C   1 
ATOM   4018 O O   . SER A 1 539 ? -71.511  -4.287  52.568  1.00 47.90  ? 565  SER A O   1 
ATOM   4019 C CB  . SER A 1 539 ? -72.383  -6.237  50.205  1.00 43.58  ? 565  SER A CB  1 
ATOM   4020 O OG  . SER A 1 539 ? -71.345  -7.068  49.733  1.00 55.38  ? 565  SER A OG  1 
ATOM   4021 N N   . HIS A 1 540 ? -69.687  -4.800  51.462  1.00 44.11  ? 566  HIS A N   1 
ATOM   4022 C CA  . HIS A 1 540 ? -68.897  -5.010  52.637  1.00 48.72  ? 566  HIS A CA  1 
ATOM   4023 C C   . HIS A 1 540 ? -69.100  -4.015  53.742  1.00 48.15  ? 566  HIS A C   1 
ATOM   4024 O O   . HIS A 1 540 ? -69.307  -4.442  54.858  1.00 53.48  ? 566  HIS A O   1 
ATOM   4025 C CB  . HIS A 1 540 ? -67.437  -5.024  52.221  1.00 49.79  ? 566  HIS A CB  1 
ATOM   4026 C CG  . HIS A 1 540 ? -66.463  -5.024  53.360  1.00 63.78  ? 566  HIS A CG  1 
ATOM   4027 N ND1 . HIS A 1 540 ? -65.938  -6.126  53.851  1.00 63.55  ? 566  HIS A ND1 1 
ATOM   4028 C CD2 . HIS A 1 540 ? -65.927  -3.989  54.080  1.00 68.92  ? 566  HIS A CD2 1 
ATOM   4029 C CE1 . HIS A 1 540 ? -65.117  -5.820  54.844  1.00 58.46  ? 566  HIS A CE1 1 
ATOM   4030 N NE2 . HIS A 1 540 ? -65.111  -4.513  54.980  1.00 63.91  ? 566  HIS A NE2 1 
ATOM   4031 N N   . TYR A 1 541 ? -69.128  -2.720  53.501  1.00 42.46  ? 567  TYR A N   1 
ATOM   4032 C CA  . TYR A 1 541 ? -69.447  -1.795  54.581  1.00 44.59  ? 567  TYR A CA  1 
ATOM   4033 C C   . TYR A 1 541 ? -70.901  -1.645  54.889  1.00 52.94  ? 567  TYR A C   1 
ATOM   4034 O O   . TYR A 1 541 ? -71.239  -1.111  55.954  1.00 55.25  ? 567  TYR A O   1 
ATOM   4035 C CB  . TYR A 1 541 ? -68.815  -0.407  54.403  1.00 42.54  ? 567  TYR A CB  1 
ATOM   4036 C CG  . TYR A 1 541 ? -67.326  -0.427  54.594  1.00 52.93  ? 567  TYR A CG  1 
ATOM   4037 C CD1 . TYR A 1 541 ? -66.779  -0.461  55.877  1.00 56.82  ? 567  TYR A CD1 1 
ATOM   4038 C CD2 . TYR A 1 541 ? -66.452  -0.393  53.508  1.00 48.70  ? 567  TYR A CD2 1 
ATOM   4039 C CE1 . TYR A 1 541 ? -65.412  -0.488  56.076  1.00 48.16  ? 567  TYR A CE1 1 
ATOM   4040 C CE2 . TYR A 1 541 ? -65.092  -0.437  53.701  1.00 55.91  ? 567  TYR A CE2 1 
ATOM   4041 C CZ  . TYR A 1 541 ? -64.581  -0.469  54.987  1.00 56.63  ? 567  TYR A CZ  1 
ATOM   4042 O OH  . TYR A 1 541 ? -63.228  -0.465  55.167  1.00 60.66  ? 567  TYR A OH  1 
ATOM   4043 N N   . PHE A 1 542 ? -71.774  -2.031  53.964  1.00 52.70  ? 568  PHE A N   1 
ATOM   4044 C CA  . PHE A 1 542 ? -73.215  -1.914  54.222  1.00 49.13  ? 568  PHE A CA  1 
ATOM   4045 C C   . PHE A 1 542 ? -73.678  -2.919  55.236  1.00 50.00  ? 568  PHE A C   1 
ATOM   4046 O O   . PHE A 1 542 ? -74.583  -2.636  55.999  1.00 62.03  ? 568  PHE A O   1 
ATOM   4047 C CB  . PHE A 1 542 ? -74.047  -2.024  52.947  1.00 51.42  ? 568  PHE A CB  1 
ATOM   4048 C CG  . PHE A 1 542 ? -73.997  -0.788  52.084  1.00 48.52  ? 568  PHE A CG  1 
ATOM   4049 C CD1 . PHE A 1 542 ? -74.791  0.294   52.388  1.00 44.22  ? 568  PHE A CD1 1 
ATOM   4050 C CD2 . PHE A 1 542 ? -73.222  -0.743  50.942  1.00 50.12  ? 568  PHE A CD2 1 
ATOM   4051 C CE1 . PHE A 1 542 ? -74.763  1.425   51.618  1.00 49.26  ? 568  PHE A CE1 1 
ATOM   4052 C CE2 . PHE A 1 542 ? -73.202  0.384   50.153  1.00 57.75  ? 568  PHE A CE2 1 
ATOM   4053 C CZ  . PHE A 1 542 ? -73.980  1.473   50.489  1.00 51.71  ? 568  PHE A CZ  1 
ATOM   4054 N N   . ARG A 1 543 ? -73.024  -4.073  55.260  1.00 46.85  ? 569  ARG A N   1 
ATOM   4055 C CA  . ARG A 1 543 ? -73.352  -5.125  56.187  1.00 56.52  ? 569  ARG A CA  1 
ATOM   4056 C C   . ARG A 1 543 ? -73.035  -4.861  57.679  1.00 68.06  ? 569  ARG A C   1 
ATOM   4057 O O   . ARG A 1 543 ? -73.762  -5.310  58.557  1.00 82.71  ? 569  ARG A O   1 
ATOM   4058 C CB  . ARG A 1 543 ? -72.526  -6.333  55.844  1.00 57.23  ? 569  ARG A CB  1 
ATOM   4059 C CG  . ARG A 1 543 ? -72.760  -6.919  54.501  1.00 62.41  ? 569  ARG A CG  1 
ATOM   4060 C CD  . ARG A 1 543 ? -71.872  -8.138  54.341  1.00 70.73  ? 569  ARG A CD  1 
ATOM   4061 N NE  . ARG A 1 543 ? -72.110  -8.731  53.042  1.00 88.10  ? 569  ARG A NE  1 
ATOM   4062 C CZ  . ARG A 1 543 ? -73.132  -9.537  52.788  1.00 94.47  ? 569  ARG A CZ  1 
ATOM   4063 N NH1 . ARG A 1 543 ? -74.012  -9.809  53.745  1.00 78.79  ? 569  ARG A NH1 1 
ATOM   4064 N NH2 . ARG A 1 543 ? -73.296  -10.040 51.573  1.00 117.45 ? 569  ARG A NH2 1 
ATOM   4065 N N   . ILE A 1 544 ? -71.932  -4.167  57.937  1.00 72.78  ? 570  ILE A N   1 
ATOM   4066 C CA  . ILE A 1 544 ? -71.423  -3.891  59.298  1.00 58.42  ? 570  ILE A CA  1 
ATOM   4067 C C   . ILE A 1 544 ? -72.179  -2.923  60.206  1.00 55.10  ? 570  ILE A C   1 
ATOM   4068 O O   . ILE A 1 544 ? -72.333  -1.761  59.907  1.00 64.74  ? 570  ILE A O   1 
ATOM   4069 C CB  . ILE A 1 544 ? -69.984  -3.424  59.193  1.00 56.10  ? 570  ILE A CB  1 
ATOM   4070 C CG1 . ILE A 1 544 ? -69.181  -4.464  58.401  1.00 49.83  ? 570  ILE A CG1 1 
ATOM   4071 C CG2 . ILE A 1 544 ? -69.420  -3.192  60.586  1.00 57.86  ? 570  ILE A CG2 1 
ATOM   4072 C CD1 . ILE A 1 544 ? -67.792  -4.019  58.022  1.00 48.89  ? 570  ILE A CD1 1 
ATOM   4073 N N   . ALA A 1 545 ? -72.645  -3.415  61.345  1.00 51.52  ? 571  ALA A N   1 
ATOM   4074 C CA  . ALA A 1 545 ? -73.377  -2.556  62.268  1.00 56.63  ? 571  ALA A CA  1 
ATOM   4075 C C   . ALA A 1 545 ? -72.482  -1.453  62.824  1.00 61.66  ? 571  ALA A C   1 
ATOM   4076 O O   . ALA A 1 545 ? -71.292  -1.680  63.088  1.00 67.70  ? 571  ALA A O   1 
ATOM   4077 C CB  . ALA A 1 545 ? -73.946  -3.384  63.402  1.00 64.82  ? 571  ALA A CB  1 
ATOM   4078 N N   . GLY A 1 546 ? -73.025  -0.241  62.933  1.00 61.38  ? 572  GLY A N   1 
ATOM   4079 C CA  . GLY A 1 546 ? -72.262  0.881   63.487  1.00 70.82  ? 572  GLY A CA  1 
ATOM   4080 C C   . GLY A 1 546 ? -71.626  1.777   62.468  1.00 69.02  ? 572  GLY A C   1 
ATOM   4081 O O   . GLY A 1 546 ? -71.327  2.941   62.760  1.00 75.70  ? 572  GLY A O   1 
ATOM   4082 N N   . VAL A 1 547 ? -71.277  1.207   61.319  1.00 65.74  ? 573  VAL A N   1 
ATOM   4083 C CA  . VAL A 1 547 ? -70.722  2.016   60.272  1.00 62.02  ? 573  VAL A CA  1 
ATOM   4084 C C   . VAL A 1 547 ? -71.873  2.796   59.655  1.00 57.65  ? 573  VAL A C   1 
ATOM   4085 O O   . VAL A 1 547 ? -72.988  2.325   59.585  1.00 66.08  ? 573  VAL A O   1 
ATOM   4086 C CB  . VAL A 1 547 ? -69.863  1.239   59.257  1.00 68.24  ? 573  VAL A CB  1 
ATOM   4087 C CG1 . VAL A 1 547 ? -70.335  -0.162  59.069  1.00 80.11  ? 573  VAL A CG1 1 
ATOM   4088 C CG2 . VAL A 1 547 ? -69.768  2.001   57.937  1.00 74.36  ? 573  VAL A CG2 1 
ATOM   4089 N N   . THR A 1 548 ? -71.630  4.067   59.423  1.00 55.54  ? 574  THR A N   1 
ATOM   4090 C CA  . THR A 1 548 ? -72.612  4.952   58.855  1.00 54.59  ? 574  THR A CA  1 
ATOM   4091 C C   . THR A 1 548 ? -72.648  4.933   57.313  1.00 54.76  ? 574  THR A C   1 
ATOM   4092 O O   . THR A 1 548 ? -71.624  4.776   56.634  1.00 59.98  ? 574  THR A O   1 
ATOM   4093 C CB  . THR A 1 548 ? -72.359  6.353   59.388  1.00 59.42  ? 574  THR A CB  1 
ATOM   4094 O OG1 . THR A 1 548 ? -70.960  6.662   59.231  1.00 53.28  ? 574  THR A OG1 1 
ATOM   4095 C CG2 . THR A 1 548 ? -72.732  6.400   60.874  1.00 53.65  ? 574  THR A CG2 1 
ATOM   4096 N N   . HIS A 1 549 ? -73.831  5.154   56.767  1.00 54.74  ? 575  HIS A N   1 
ATOM   4097 C CA  . HIS A 1 549 ? -74.013  5.104   55.313  1.00 52.88  ? 575  HIS A CA  1 
ATOM   4098 C C   . HIS A 1 549 ? -74.761  6.304   54.796  1.00 54.75  ? 575  HIS A C   1 
ATOM   4099 O O   . HIS A 1 549 ? -75.895  6.559   55.202  1.00 63.23  ? 575  HIS A O   1 
ATOM   4100 C CB  . HIS A 1 549 ? -74.812  3.871   55.005  1.00 55.21  ? 575  HIS A CB  1 
ATOM   4101 C CG  . HIS A 1 549 ? -74.382  2.681   55.803  1.00 52.40  ? 575  HIS A CG  1 
ATOM   4102 N ND1 . HIS A 1 549 ? -73.263  1.940   55.495  1.00 48.64  ? 575  HIS A ND1 1 
ATOM   4103 C CD2 . HIS A 1 549 ? -74.928  2.105   56.899  1.00 53.59  ? 575  HIS A CD2 1 
ATOM   4104 C CE1 . HIS A 1 549 ? -73.154  0.940   56.351  1.00 56.70  ? 575  HIS A CE1 1 
ATOM   4105 N NE2 . HIS A 1 549 ? -74.153  1.014   57.213  1.00 54.63  ? 575  HIS A NE2 1 
ATOM   4106 N N   . HIS A 1 550 ? -74.124  7.029   53.889  1.00 54.41  ? 576  HIS A N   1 
ATOM   4107 C CA  . HIS A 1 550 ? -74.692  8.216   53.311  1.00 56.99  ? 576  HIS A CA  1 
ATOM   4108 C C   . HIS A 1 550 ? -74.863  8.142   51.791  1.00 57.90  ? 576  HIS A C   1 
ATOM   4109 O O   . HIS A 1 550 ? -73.886  8.166   51.035  1.00 60.12  ? 576  HIS A O   1 
ATOM   4110 C CB  . HIS A 1 550 ? -73.808  9.406   53.673  1.00 62.02  ? 576  HIS A CB  1 
ATOM   4111 C CG  . HIS A 1 550 ? -73.762  9.706   55.147  1.00 66.43  ? 576  HIS A CG  1 
ATOM   4112 N ND1 . HIS A 1 550 ? -74.681  10.518  55.769  1.00 69.36  ? 576  HIS A ND1 1 
ATOM   4113 C CD2 . HIS A 1 550 ? -72.858  9.373   56.097  1.00 65.35  ? 576  HIS A CD2 1 
ATOM   4114 C CE1 . HIS A 1 550 ? -74.378  10.630  57.047  1.00 65.55  ? 576  HIS A CE1 1 
ATOM   4115 N NE2 . HIS A 1 550 ? -73.274  9.948   57.270  1.00 65.57  ? 576  HIS A NE2 1 
ATOM   4116 N N   . LEU A 1 551 ? -76.117  8.106   51.350  1.00 67.73  ? 577  LEU A N   1 
ATOM   4117 C CA  . LEU A 1 551 ? -76.444  8.066   49.907  1.00 67.11  ? 577  LEU A CA  1 
ATOM   4118 C C   . LEU A 1 551 ? -77.084  9.373   49.414  1.00 67.24  ? 577  LEU A C   1 
ATOM   4119 O O   . LEU A 1 551 ? -77.652  9.420   48.325  1.00 65.62  ? 577  LEU A O   1 
ATOM   4120 C CB  . LEU A 1 551 ? -77.363  6.872   49.575  1.00 55.93  ? 577  LEU A CB  1 
ATOM   4121 C CG  . LEU A 1 551 ? -76.716  5.508   49.825  1.00 58.20  ? 577  LEU A CG  1 
ATOM   4122 C CD1 . LEU A 1 551 ? -77.649  4.409   49.385  1.00 61.31  ? 577  LEU A CD1 1 
ATOM   4123 C CD2 . LEU A 1 551 ? -75.399  5.360   49.083  1.00 63.98  ? 577  LEU A CD2 1 
ATOM   4124 N N   . GLU A 1 552 ? -76.912  10.440  50.189  1.00 72.33  ? 578  GLU A N   1 
ATOM   4125 C CA  . GLU A 1 552 ? -77.483  11.732  49.862  1.00 66.29  ? 578  GLU A CA  1 
ATOM   4126 C C   . GLU A 1 552 ? -76.979  12.298  48.549  1.00 67.77  ? 578  GLU A C   1 
ATOM   4127 O O   . GLU A 1 552 ? -77.649  13.157  47.971  1.00 72.40  ? 578  GLU A O   1 
ATOM   4128 C CB  . GLU A 1 552 ? -77.178  12.800  50.924  1.00 68.67  ? 578  GLU A CB  1 
ATOM   4129 C CG  . GLU A 1 552 ? -77.649  12.579  52.352  1.00 80.26  ? 578  GLU A CG  1 
ATOM   4130 C CD  . GLU A 1 552 ? -76.762  11.664  53.183  1.00 82.07  ? 578  GLU A CD  1 
ATOM   4131 O OE1 . GLU A 1 552 ? -75.910  10.964  52.621  1.00 77.08  ? 578  GLU A OE1 1 
ATOM   4132 O OE2 . GLU A 1 552 ? -76.915  11.673  54.423  1.00 81.12  ? 578  GLU A OE2 1 
ATOM   4133 N N   . PHE A 1 553 ? -75.772  11.902  48.126  1.00 54.68  ? 579  PHE A N   1 
ATOM   4134 C CA  . PHE A 1 553 ? -75.191  12.432  46.879  1.00 54.94  ? 579  PHE A CA  1 
ATOM   4135 C C   . PHE A 1 553 ? -76.049  12.209  45.637  1.00 59.31  ? 579  PHE A C   1 
ATOM   4136 O O   . PHE A 1 553 ? -75.920  12.921  44.642  1.00 67.68  ? 579  PHE A O   1 
ATOM   4137 C CB  . PHE A 1 553 ? -73.772  11.893  46.649  1.00 58.90  ? 579  PHE A CB  1 
ATOM   4138 C CG  . PHE A 1 553 ? -73.698  10.401  46.531  1.00 60.24  ? 579  PHE A CG  1 
ATOM   4139 C CD1 . PHE A 1 553 ? -73.864  9.786   45.315  1.00 66.65  ? 579  PHE A CD1 1 
ATOM   4140 C CD2 . PHE A 1 553 ? -73.402  9.630   47.620  1.00 61.46  ? 579  PHE A CD2 1 
ATOM   4141 C CE1 . PHE A 1 553 ? -73.800  8.417   45.205  1.00 64.44  ? 579  PHE A CE1 1 
ATOM   4142 C CE2 . PHE A 1 553 ? -73.353  8.260   47.523  1.00 58.78  ? 579  PHE A CE2 1 
ATOM   4143 C CZ  . PHE A 1 553 ? -73.544  7.656   46.316  1.00 63.56  ? 579  PHE A CZ  1 
ATOM   4144 N N   . ILE A 1 554 ? -76.939  11.237  45.710  1.00 57.21  ? 580  ILE A N   1 
ATOM   4145 C CA  . ILE A 1 554 ? -77.810  10.912  44.610  1.00 60.20  ? 580  ILE A CA  1 
ATOM   4146 C C   . ILE A 1 554 ? -78.556  12.130  44.082  1.00 65.84  ? 580  ILE A C   1 
ATOM   4147 O O   . ILE A 1 554 ? -78.538  12.394  42.881  1.00 62.89  ? 580  ILE A O   1 
ATOM   4148 C CB  . ILE A 1 554 ? -78.777  9.803   45.021  1.00 62.86  ? 580  ILE A CB  1 
ATOM   4149 C CG1 . ILE A 1 554 ? -77.987  8.504   45.194  1.00 69.54  ? 580  ILE A CG1 1 
ATOM   4150 C CG2 . ILE A 1 554 ? -79.834  9.599   43.969  1.00 62.17  ? 580  ILE A CG2 1 
ATOM   4151 C CD1 . ILE A 1 554 ? -78.813  7.340   45.679  1.00 75.67  ? 580  ILE A CD1 1 
ATOM   4152 N N   . GLN A 1 555 ? -79.138  12.912  44.984  1.00 62.51  ? 581  GLN A N   1 
ATOM   4153 C CA  . GLN A 1 555 ? -79.889  14.094  44.585  1.00 61.63  ? 581  GLN A CA  1 
ATOM   4154 C C   . GLN A 1 555 ? -79.100  15.207  43.933  1.00 65.73  ? 581  GLN A C   1 
ATOM   4155 O O   . GLN A 1 555 ? -79.656  15.952  43.148  1.00 79.35  ? 581  GLN A O   1 
ATOM   4156 C CB  . GLN A 1 555 ? -80.707  14.652  45.726  1.00 65.58  ? 581  GLN A CB  1 
ATOM   4157 C CG  . GLN A 1 555 ? -79.957  14.752  47.035  1.00 91.10  ? 581  GLN A CG  1 
ATOM   4158 C CD  . GLN A 1 555 ? -80.694  15.591  48.050  1.00 100.94 ? 581  GLN A CD  1 
ATOM   4159 O OE1 . GLN A 1 555 ? -81.293  15.061  48.984  1.00 102.39 ? 581  GLN A OE1 1 
ATOM   4160 N NE2 . GLN A 1 555 ? -80.815  16.878  47.762  1.00 105.80 ? 581  GLN A NE2 1 
ATOM   4161 N N   . ASN A 1 556 ? -77.804  15.280  44.169  1.00 66.74  ? 582  ASN A N   1 
ATOM   4162 C CA  . ASN A 1 556 ? -77.003  16.352  43.571  1.00 70.84  ? 582  ASN A CA  1 
ATOM   4163 C C   . ASN A 1 556 ? -76.786  16.300  42.089  1.00 65.82  ? 582  ASN A C   1 
ATOM   4164 O O   . ASN A 1 556 ? -76.195  17.211  41.552  1.00 90.44  ? 582  ASN A O   1 
ATOM   4165 C CB  . ASN A 1 556 ? -75.623  16.449  44.238  1.00 76.35  ? 582  ASN A CB  1 
ATOM   4166 C CG  . ASN A 1 556 ? -75.685  16.996  45.653  1.00 98.96  ? 582  ASN A CG  1 
ATOM   4167 O OD1 . ASN A 1 556 ? -75.177  16.378  46.595  1.00 126.84 ? 582  ASN A OD1 1 
ATOM   4168 N ND2 . ASN A 1 556 ? -76.346  18.135  45.823  1.00 101.68 ? 582  ASN A ND2 1 
ATOM   4169 N N   . PHE A 1 557 ? -77.178  15.226  41.424  1.00 71.09  ? 583  PHE A N   1 
ATOM   4170 C CA  . PHE A 1 557 ? -76.947  15.141  39.978  1.00 68.36  ? 583  PHE A CA  1 
ATOM   4171 C C   . PHE A 1 557 ? -78.182  15.618  39.253  1.00 71.39  ? 583  PHE A C   1 
ATOM   4172 O O   . PHE A 1 557 ? -79.293  15.249  39.608  1.00 71.61  ? 583  PHE A O   1 
ATOM   4173 C CB  . PHE A 1 557 ? -76.634  13.711  39.539  1.00 65.37  ? 583  PHE A CB  1 
ATOM   4174 C CG  . PHE A 1 557 ? -75.475  13.107  40.246  1.00 57.97  ? 583  PHE A CG  1 
ATOM   4175 C CD1 . PHE A 1 557 ? -74.194  13.385  39.853  1.00 56.43  ? 583  PHE A CD1 1 
ATOM   4176 C CD2 . PHE A 1 557 ? -75.672  12.192  41.246  1.00 65.05  ? 583  PHE A CD2 1 
ATOM   4177 C CE1 . PHE A 1 557 ? -73.117  12.830  40.507  1.00 56.54  ? 583  PHE A CE1 1 
ATOM   4178 C CE2 . PHE A 1 557 ? -74.596  11.618  41.899  1.00 66.02  ? 583  PHE A CE2 1 
ATOM   4179 C CZ  . PHE A 1 557 ? -73.321  11.942  41.531  1.00 60.10  ? 583  PHE A CZ  1 
ATOM   4180 N N   . THR A 1 558 ? -77.990  16.418  38.218  1.00 60.79  ? 584  THR A N   1 
ATOM   4181 C CA  . THR A 1 558 ? -79.116  16.929  37.473  1.00 65.19  ? 584  THR A CA  1 
ATOM   4182 C C   . THR A 1 558 ? -79.422  16.063  36.283  1.00 60.30  ? 584  THR A C   1 
ATOM   4183 O O   . THR A 1 558 ? -80.559  15.984  35.862  1.00 63.76  ? 584  THR A O   1 
ATOM   4184 C CB  . THR A 1 558 ? -78.844  18.348  36.919  1.00 71.17  ? 584  THR A CB  1 
ATOM   4185 O OG1 . THR A 1 558 ? -77.775  18.307  35.960  1.00 71.68  ? 584  THR A OG1 1 
ATOM   4186 C CG2 . THR A 1 558 ? -78.489  19.308  38.028  1.00 72.55  ? 584  THR A CG2 1 
ATOM   4187 N N   . ASN A 1 559 ? -78.431  15.332  35.795  1.00 65.95  ? 585  ASN A N   1 
ATOM   4188 C CA  . ASN A 1 559 ? -78.642  14.528  34.604  1.00 67.65  ? 585  ASN A CA  1 
ATOM   4189 C C   . ASN A 1 559 ? -78.435  13.007  34.834  1.00 60.18  ? 585  ASN A C   1 
ATOM   4190 O O   . ASN A 1 559 ? -78.148  12.266  33.907  1.00 58.97  ? 585  ASN A O   1 
ATOM   4191 C CB  . ASN A 1 559 ? -77.689  15.085  33.531  1.00 68.34  ? 585  ASN A CB  1 
ATOM   4192 C CG  . ASN A 1 559 ? -78.055  14.659  32.124  1.00 91.66  ? 585  ASN A CG  1 
ATOM   4193 O OD1 . ASN A 1 559 ? -79.243  14.600  31.759  1.00 71.55  ? 585  ASN A OD1 1 
ATOM   4194 N ND2 . ASN A 1 559 ? -77.030  14.480  31.281  1.00 100.94 ? 585  ASN A ND2 1 
ATOM   4195 N N   . LEU A 1 560 ? -78.616  12.541  36.068  1.00 62.66  ? 586  LEU A N   1 
ATOM   4196 C CA  . LEU A 1 560 ? -78.427  11.118  36.392  1.00 56.03  ? 586  LEU A CA  1 
ATOM   4197 C C   . LEU A 1 560 ? -79.667  10.345  35.966  1.00 55.29  ? 586  LEU A C   1 
ATOM   4198 O O   . LEU A 1 560 ? -80.763  10.615  36.476  1.00 56.67  ? 586  LEU A O   1 
ATOM   4199 C CB  . LEU A 1 560 ? -78.185  10.932  37.893  1.00 54.34  ? 586  LEU A CB  1 
ATOM   4200 C CG  . LEU A 1 560 ? -78.006  9.486   38.382  1.00 53.87  ? 586  LEU A CG  1 
ATOM   4201 C CD1 . LEU A 1 560 ? -76.755  8.864   37.777  1.00 54.80  ? 586  LEU A CD1 1 
ATOM   4202 C CD2 . LEU A 1 560 ? -77.921  9.416   39.899  1.00 54.16  ? 586  LEU A CD2 1 
ATOM   4203 N N   . LYS A 1 561 ? -79.484  9.307   35.144  1.00 46.98  ? 587  LYS A N   1 
ATOM   4204 C CA  . LYS A 1 561 ? -80.629  8.528   34.639  1.00 53.75  ? 587  LYS A CA  1 
ATOM   4205 C C   . LYS A 1 561 ? -80.798  7.120   35.193  1.00 58.00  ? 587  LYS A C   1 
ATOM   4206 O O   . LYS A 1 561 ? -81.928  6.687   35.457  1.00 61.11  ? 587  LYS A O   1 
ATOM   4207 C CB  . LYS A 1 561 ? -80.535  8.427   33.113  1.00 50.27  ? 587  LYS A CB  1 
ATOM   4208 C CG  . LYS A 1 561 ? -80.510  9.774   32.423  1.00 60.79  ? 587  LYS A CG  1 
ATOM   4209 C CD  . LYS A 1 561 ? -80.204  9.671   30.935  1.00 69.27  ? 587  LYS A CD  1 
ATOM   4210 C CE  . LYS A 1 561 ? -80.073  11.058  30.311  1.00 78.42  ? 587  LYS A CE  1 
ATOM   4211 N NZ  . LYS A 1 561 ? -79.669  10.988  28.885  1.00 84.62  ? 587  LYS A NZ  1 
ATOM   4212 N N   . VAL A 1 562 ? -79.680  6.415   35.349  1.00 52.70  ? 588  VAL A N   1 
ATOM   4213 C CA  . VAL A 1 562 ? -79.668  5.027   35.822  1.00 51.98  ? 588  VAL A CA  1 
ATOM   4214 C C   . VAL A 1 562 ? -78.726  4.800   37.005  1.00 55.77  ? 588  VAL A C   1 
ATOM   4215 O O   . VAL A 1 562 ? -77.519  5.063   36.935  1.00 58.44  ? 588  VAL A O   1 
ATOM   4216 C CB  . VAL A 1 562 ? -79.170  4.133   34.685  1.00 52.03  ? 588  VAL A CB  1 
ATOM   4217 C CG1 . VAL A 1 562 ? -79.126  2.685   35.102  1.00 51.78  ? 588  VAL A CG1 1 
ATOM   4218 C CG2 . VAL A 1 562 ? -80.051  4.300   33.474  1.00 52.98  ? 588  VAL A CG2 1 
ATOM   4219 N N   . LEU A 1 563 ? -79.261  4.215   38.051  1.00 51.75  ? 589  LEU A N   1 
ATOM   4220 C CA  . LEU A 1 563 ? -78.481  3.946   39.236  1.00 53.61  ? 589  LEU A CA  1 
ATOM   4221 C C   . LEU A 1 563 ? -78.686  2.504   39.646  1.00 49.75  ? 589  LEU A C   1 
ATOM   4222 O O   . LEU A 1 563 ? -79.824  2.044   39.821  1.00 50.44  ? 589  LEU A O   1 
ATOM   4223 C CB  . LEU A 1 563 ? -78.937  4.875   40.366  1.00 52.44  ? 589  LEU A CB  1 
ATOM   4224 C CG  . LEU A 1 563 ? -78.302  4.697   41.748  1.00 55.10  ? 589  LEU A CG  1 
ATOM   4225 C CD1 . LEU A 1 563 ? -76.796  4.904   41.709  1.00 51.76  ? 589  LEU A CD1 1 
ATOM   4226 C CD2 . LEU A 1 563 ? -78.931  5.654   42.757  1.00 52.67  ? 589  LEU A CD2 1 
ATOM   4227 N N   . ASN A 1 564 ? -77.593  1.783   39.798  1.00 44.32  ? 590  ASN A N   1 
ATOM   4228 C CA  . ASN A 1 564 ? -77.676  0.392   40.207  1.00 41.28  ? 590  ASN A CA  1 
ATOM   4229 C C   . ASN A 1 564 ? -76.954  0.217   41.550  1.00 48.68  ? 590  ASN A C   1 
ATOM   4230 O O   . ASN A 1 564 ? -75.725  0.399   41.633  1.00 47.54  ? 590  ASN A O   1 
ATOM   4231 C CB  . ASN A 1 564 ? -77.054  -0.486  39.134  1.00 40.67  ? 590  ASN A CB  1 
ATOM   4232 C CG  . ASN A 1 564 ? -77.244  -1.967  39.391  1.00 41.26  ? 590  ASN A CG  1 
ATOM   4233 O OD1 . ASN A 1 564 ? -77.517  -2.377  40.500  1.00 49.08  ? 590  ASN A OD1 1 
ATOM   4234 N ND2 . ASN A 1 564 ? -77.065  -2.781  38.367  1.00 46.74  ? 590  ASN A ND2 1 
ATOM   4235 N N   . LEU A 1 565 ? -77.745  -0.070  42.593  1.00 43.14  ? 591  LEU A N   1 
ATOM   4236 C CA  . LEU A 1 565 ? -77.267  -0.317  43.964  1.00 39.65  ? 591  LEU A CA  1 
ATOM   4237 C C   . LEU A 1 565 ? -77.496  -1.803  44.298  1.00 43.59  ? 591  LEU A C   1 
ATOM   4238 O O   . LEU A 1 565 ? -77.697  -2.165  45.456  1.00 46.05  ? 591  LEU A O   1 
ATOM   4239 C CB  . LEU A 1 565 ? -78.096  0.474   44.962  1.00 38.28  ? 591  LEU A CB  1 
ATOM   4240 C CG  . LEU A 1 565 ? -78.111  1.985   44.806  1.00 46.46  ? 591  LEU A CG  1 
ATOM   4241 C CD1 . LEU A 1 565 ? -79.052  2.624   45.811  1.00 46.91  ? 591  LEU A CD1 1 
ATOM   4242 C CD2 . LEU A 1 565 ? -76.709  2.530   44.969  1.00 53.48  ? 591  LEU A CD2 1 
ATOM   4243 N N   . SER A 1 566 ? -77.523  -2.665  43.299  1.00 43.09  ? 592  SER A N   1 
ATOM   4244 C CA  . SER A 1 566 ? -77.782  -4.075  43.579  1.00 49.49  ? 592  SER A CA  1 
ATOM   4245 C C   . SER A 1 566 ? -76.659  -4.788  44.345  1.00 51.04  ? 592  SER A C   1 
ATOM   4246 O O   . SER A 1 566 ? -75.485  -4.461  44.210  1.00 51.89  ? 592  SER A O   1 
ATOM   4247 C CB  . SER A 1 566 ? -78.036  -4.864  42.286  1.00 48.29  ? 592  SER A CB  1 
ATOM   4248 O OG  . SER A 1 566 ? -76.856  -4.958  41.507  1.00 49.13  ? 592  SER A OG  1 
ATOM   4249 N N   . HIS A 1 567 ? -77.059  -5.793  45.117  1.00 44.85  ? 593  HIS A N   1 
ATOM   4250 C CA  . HIS A 1 567 ? -76.151  -6.643  45.893  1.00 44.44  ? 593  HIS A CA  1 
ATOM   4251 C C   . HIS A 1 567 ? -75.201  -5.927  46.863  1.00 43.92  ? 593  HIS A C   1 
ATOM   4252 O O   . HIS A 1 567 ? -74.053  -6.310  46.998  1.00 41.65  ? 593  HIS A O   1 
ATOM   4253 C CB  . HIS A 1 567 ? -75.385  -7.567  44.968  1.00 43.71  ? 593  HIS A CB  1 
ATOM   4254 C CG  . HIS A 1 567 ? -76.268  -8.345  44.050  1.00 58.77  ? 593  HIS A CG  1 
ATOM   4255 N ND1 . HIS A 1 567 ? -76.944  -9.478  44.446  1.00 59.05  ? 593  HIS A ND1 1 
ATOM   4256 C CD2 . HIS A 1 567 ? -76.600  -8.146  42.751  1.00 65.70  ? 593  HIS A CD2 1 
ATOM   4257 C CE1 . HIS A 1 567 ? -77.637  -9.954  43.428  1.00 58.82  ? 593  HIS A CE1 1 
ATOM   4258 N NE2 . HIS A 1 567 ? -77.428  -9.175  42.383  1.00 63.54  ? 593  HIS A NE2 1 
ATOM   4259 N N   . ASN A 1 568 ? -75.779  -4.990  47.614  1.00 42.07  ? 594  ASN A N   1 
ATOM   4260 C CA  . ASN A 1 568 ? -75.127  -4.192  48.623  1.00 45.89  ? 594  ASN A CA  1 
ATOM   4261 C C   . ASN A 1 568 ? -75.690  -4.448  50.025  1.00 47.95  ? 594  ASN A C   1 
ATOM   4262 O O   . ASN A 1 568 ? -75.211  -3.889  51.017  1.00 56.83  ? 594  ASN A O   1 
ATOM   4263 C CB  . ASN A 1 568 ? -75.254  -2.706  48.258  1.00 42.32  ? 594  ASN A CB  1 
ATOM   4264 C CG  . ASN A 1 568 ? -74.337  -2.331  47.122  1.00 51.26  ? 594  ASN A CG  1 
ATOM   4265 O OD1 . ASN A 1 568 ? -73.199  -2.781  47.081  1.00 49.46  ? 594  ASN A OD1 1 
ATOM   4266 N ND2 . ASN A 1 568 ? -74.783  -1.436  46.252  1.00 54.84  ? 594  ASN A ND2 1 
ATOM   4267 N N   . ASN A 1 569 ? -76.688  -5.309  50.109  1.00 46.91  ? 595  ASN A N   1 
ATOM   4268 C CA  . ASN A 1 569 ? -77.320  -5.638  51.387  1.00 48.30  ? 595  ASN A CA  1 
ATOM   4269 C C   . ASN A 1 569 ? -77.662  -4.418  52.203  1.00 48.26  ? 595  ASN A C   1 
ATOM   4270 O O   . ASN A 1 569 ? -77.445  -4.408  53.417  1.00 50.35  ? 595  ASN A O   1 
ATOM   4271 C CB  . ASN A 1 569 ? -76.440  -6.536  52.245  1.00 55.54  ? 595  ASN A CB  1 
ATOM   4272 C CG  . ASN A 1 569 ? -76.164  -7.870  51.609  1.00 65.12  ? 595  ASN A CG  1 
ATOM   4273 O OD1 . ASN A 1 569 ? -76.377  -8.898  52.232  1.00 99.56  ? 595  ASN A OD1 1 
ATOM   4274 N ND2 . ASN A 1 569 ? -75.798  -7.871  50.344  1.00 77.39  ? 595  ASN A ND2 1 
ATOM   4275 N N   . ILE A 1 570 ? -78.133  -3.369  51.548  1.00 40.78  ? 596  ILE A N   1 
ATOM   4276 C CA  . ILE A 1 570 ? -78.495  -2.172  52.274  1.00 48.59  ? 596  ILE A CA  1 
ATOM   4277 C C   . ILE A 1 570 ? -79.691  -2.475  53.144  1.00 48.76  ? 596  ILE A C   1 
ATOM   4278 O O   . ILE A 1 570 ? -80.664  -3.030  52.664  1.00 55.89  ? 596  ILE A O   1 
ATOM   4279 C CB  . ILE A 1 570 ? -78.820  -1.026  51.344  1.00 50.02  ? 596  ILE A CB  1 
ATOM   4280 C CG1 . ILE A 1 570 ? -77.588  -0.690  50.517  1.00 54.70  ? 596  ILE A CG1 1 
ATOM   4281 C CG2 . ILE A 1 570 ? -79.233  0.191   52.147  1.00 51.38  ? 596  ILE A CG2 1 
ATOM   4282 C CD1 . ILE A 1 570 ? -77.860  0.334   49.434  1.00 67.79  ? 596  ILE A CD1 1 
ATOM   4283 N N   . TYR A 1 571 ? -79.563  -2.196  54.445  1.00 55.02  ? 597  TYR A N   1 
ATOM   4284 C CA  . TYR A 1 571 ? -80.637  -2.450  55.426  1.00 54.23  ? 597  TYR A CA  1 
ATOM   4285 C C   . TYR A 1 571 ? -80.834  -1.291  56.364  1.00 50.21  ? 597  TYR A C   1 
ATOM   4286 O O   . TYR A 1 571 ? -81.605  -1.394  57.281  1.00 67.57  ? 597  TYR A O   1 
ATOM   4287 C CB  . TYR A 1 571 ? -80.312  -3.660  56.284  1.00 55.41  ? 597  TYR A CB  1 
ATOM   4288 C CG  . TYR A 1 571 ? -79.221  -3.424  57.314  1.00 63.61  ? 597  TYR A CG  1 
ATOM   4289 C CD1 . TYR A 1 571 ? -77.879  -3.593  57.006  1.00 67.30  ? 597  TYR A CD1 1 
ATOM   4290 C CD2 . TYR A 1 571 ? -79.547  -3.099  58.625  1.00 71.46  ? 597  TYR A CD2 1 
ATOM   4291 C CE1 . TYR A 1 571 ? -76.895  -3.390  57.961  1.00 72.95  ? 597  TYR A CE1 1 
ATOM   4292 C CE2 . TYR A 1 571 ? -78.576  -2.911  59.584  1.00 70.09  ? 597  TYR A CE2 1 
ATOM   4293 C CZ  . TYR A 1 571 ? -77.255  -3.061  59.254  1.00 74.06  ? 597  TYR A CZ  1 
ATOM   4294 O OH  . TYR A 1 571 ? -76.306  -2.883  60.226  1.00 71.34  ? 597  TYR A OH  1 
ATOM   4295 N N   . THR A 1 572 ? -80.075  -0.221  56.175  1.00 55.22  ? 598  THR A N   1 
ATOM   4296 C CA  . THR A 1 572 ? -80.180  0.974   57.003  1.00 53.83  ? 598  THR A CA  1 
ATOM   4297 C C   . THR A 1 572 ? -79.402  2.120   56.377  1.00 54.10  ? 598  THR A C   1 
ATOM   4298 O O   . THR A 1 572 ? -78.395  1.894   55.710  1.00 58.19  ? 598  THR A O   1 
ATOM   4299 C CB  . THR A 1 572 ? -79.608  0.773   58.417  1.00 56.94  ? 598  THR A CB  1 
ATOM   4300 O OG1 . THR A 1 572 ? -79.771  1.984   59.153  1.00 54.70  ? 598  THR A OG1 1 
ATOM   4301 C CG2 . THR A 1 572 ? -78.132  0.440   58.368  1.00 57.77  ? 598  THR A CG2 1 
ATOM   4302 N N   . LEU A 1 573 ? -79.855  3.342   56.627  1.00 55.03  ? 599  LEU A N   1 
ATOM   4303 C CA  . LEU A 1 573 ? -79.192  4.540   56.111  1.00 63.91  ? 599  LEU A CA  1 
ATOM   4304 C C   . LEU A 1 573 ? -79.006  5.504   57.266  1.00 60.81  ? 599  LEU A C   1 
ATOM   4305 O O   . LEU A 1 573 ? -79.763  5.486   58.219  1.00 66.18  ? 599  LEU A O   1 
ATOM   4306 C CB  . LEU A 1 573 ? -80.015  5.221   55.019  1.00 69.83  ? 599  LEU A CB  1 
ATOM   4307 C CG  . LEU A 1 573 ? -80.313  4.408   53.754  1.00 77.68  ? 599  LEU A CG  1 
ATOM   4308 C CD1 . LEU A 1 573 ? -81.111  5.259   52.774  1.00 76.41  ? 599  LEU A CD1 1 
ATOM   4309 C CD2 . LEU A 1 573 ? -79.036  3.932   53.099  1.00 72.88  ? 599  LEU A CD2 1 
ATOM   4310 N N   . THR A 1 574 ? -78.038  6.392   57.146  1.00 56.85  ? 600  THR A N   1 
ATOM   4311 C CA  . THR A 1 574 ? -77.774  7.335   58.197  1.00 58.82  ? 600  THR A CA  1 
ATOM   4312 C C   . THR A 1 574 ? -78.243  8.751   57.904  1.00 63.96  ? 600  THR A C   1 
ATOM   4313 O O   . THR A 1 574 ? -77.892  9.347   56.862  1.00 58.91  ? 600  THR A O   1 
ATOM   4314 C CB  . THR A 1 574 ? -76.267  7.409   58.473  1.00 64.09  ? 600  THR A CB  1 
ATOM   4315 O OG1 . THR A 1 574 ? -75.780  6.102   58.761  1.00 61.73  ? 600  THR A OG1 1 
ATOM   4316 C CG2 . THR A 1 574 ? -75.982  8.344   59.646  1.00 63.45  ? 600  THR A CG2 1 
ATOM   4317 N N   . ASP A 1 575 ? -78.993  9.300   58.856  1.00 63.43  ? 601  ASP A N   1 
ATOM   4318 C CA  . ASP A 1 575 ? -79.496  10.678  58.776  1.00 79.66  ? 601  ASP A CA  1 
ATOM   4319 C C   . ASP A 1 575 ? -80.564  10.939  57.720  1.00 75.86  ? 601  ASP A C   1 
ATOM   4320 O O   . ASP A 1 575 ? -81.668  11.368  58.047  1.00 92.17  ? 601  ASP A O   1 
ATOM   4321 C CB  . ASP A 1 575 ? -78.325  11.657  58.554  1.00 72.83  ? 601  ASP A CB  1 
ATOM   4322 C CG  . ASP A 1 575 ? -77.310  11.630  59.685  1.00 83.71  ? 601  ASP A CG  1 
ATOM   4323 O OD1 . ASP A 1 575 ? -77.689  11.290  60.843  1.00 86.79  ? 601  ASP A OD1 1 
ATOM   4324 O OD2 . ASP A 1 575 ? -76.142  12.005  59.418  1.00 70.95  ? 601  ASP A OD2 1 
ATOM   4325 N N   . LYS A 1 576 ? -80.232  10.675  56.463  1.00 79.86  ? 602  LYS A N   1 
ATOM   4326 C CA  . LYS A 1 576 ? -81.147  10.920  55.366  1.00 73.83  ? 602  LYS A CA  1 
ATOM   4327 C C   . LYS A 1 576 ? -81.646  9.546   54.885  1.00 63.38  ? 602  LYS A C   1 
ATOM   4328 O O   . LYS A 1 576 ? -80.894  8.734   54.369  1.00 63.25  ? 602  LYS A O   1 
ATOM   4329 C CB  . LYS A 1 576 ? -80.379  11.744  54.353  1.00 77.01  ? 602  LYS A CB  1 
ATOM   4330 C CG  . LYS A 1 576 ? -81.223  12.705  53.559  1.00 94.79  ? 602  LYS A CG  1 
ATOM   4331 C CD  . LYS A 1 576 ? -81.785  12.227  52.244  1.00 99.29  ? 602  LYS A CD  1 
ATOM   4332 C CE  . LYS A 1 576 ? -82.674  13.358  51.738  1.00 101.57 ? 602  LYS A CE  1 
ATOM   4333 N NZ  . LYS A 1 576 ? -82.714  13.455  50.253  1.00 103.89 ? 602  LYS A NZ  1 
ATOM   4334 N N   . TYR A 1 577 ? -82.925  9.282   55.128  1.00 75.26  ? 603  TYR A N   1 
ATOM   4335 C CA  . TYR A 1 577 ? -83.539  7.976   54.820  1.00 78.85  ? 603  TYR A CA  1 
ATOM   4336 C C   . TYR A 1 577 ? -84.242  7.783   53.492  1.00 74.59  ? 603  TYR A C   1 
ATOM   4337 O O   . TYR A 1 577 ? -84.641  6.679   53.188  1.00 78.04  ? 603  TYR A O   1 
ATOM   4338 C CB  . TYR A 1 577 ? -84.528  7.635   55.944  1.00 70.65  ? 603  TYR A CB  1 
ATOM   4339 C CG  . TYR A 1 577 ? -83.913  7.930   57.264  1.00 84.44  ? 603  TYR A CG  1 
ATOM   4340 C CD1 . TYR A 1 577 ? -82.797  7.222   57.699  1.00 97.61  ? 603  TYR A CD1 1 
ATOM   4341 C CD2 . TYR A 1 577 ? -84.407  8.944   58.072  1.00 97.80  ? 603  TYR A CD2 1 
ATOM   4342 C CE1 . TYR A 1 577 ? -82.166  7.539   58.886  1.00 108.53 ? 603  TYR A CE1 1 
ATOM   4343 C CE2 . TYR A 1 577 ? -83.799  9.251   59.280  1.00 106.50 ? 603  TYR A CE2 1 
ATOM   4344 C CZ  . TYR A 1 577 ? -82.676  8.550   59.679  1.00 111.96 ? 603  TYR A CZ  1 
ATOM   4345 O OH  . TYR A 1 577 ? -82.054  8.858   60.869  1.00 103.46 ? 603  TYR A OH  1 
ATOM   4346 N N   . ASN A 1 578 ? -84.359  8.826   52.687  1.00 76.57  ? 604  ASN A N   1 
ATOM   4347 C CA  . ASN A 1 578 ? -85.047  8.718   51.409  1.00 70.24  ? 604  ASN A CA  1 
ATOM   4348 C C   . ASN A 1 578 ? -84.166  9.012   50.219  1.00 70.34  ? 604  ASN A C   1 
ATOM   4349 O O   . ASN A 1 578 ? -83.401  9.976   50.242  1.00 74.74  ? 604  ASN A O   1 
ATOM   4350 C CB  . ASN A 1 578 ? -86.118  9.781   51.379  1.00 69.74  ? 604  ASN A CB  1 
ATOM   4351 C CG  . ASN A 1 578 ? -87.056  9.683   52.535  1.00 70.96  ? 604  ASN A CG  1 
ATOM   4352 O OD1 . ASN A 1 578 ? -87.750  8.676   52.715  1.00 66.26  ? 604  ASN A OD1 1 
ATOM   4353 N ND2 . ASN A 1 578 ? -87.199  10.787  53.244  1.00 73.62  ? 604  ASN A ND2 1 
ATOM   4354 N N   . LEU A 1 579 ? -84.323  8.231   49.155  1.00 64.14  ? 605  LEU A N   1 
ATOM   4355 C CA  . LEU A 1 579 ? -83.570  8.473   47.934  1.00 61.19  ? 605  LEU A CA  1 
ATOM   4356 C C   . LEU A 1 579 ? -84.406  9.506   47.174  1.00 65.91  ? 605  LEU A C   1 
ATOM   4357 O O   . LEU A 1 579 ? -85.645  9.456   47.181  1.00 58.86  ? 605  LEU A O   1 
ATOM   4358 C CB  . LEU A 1 579 ? -83.401  7.209   47.114  1.00 61.92  ? 605  LEU A CB  1 
ATOM   4359 C CG  . LEU A 1 579 ? -82.788  6.036   47.858  1.00 64.27  ? 605  LEU A CG  1 
ATOM   4360 C CD1 . LEU A 1 579 ? -82.570  4.874   46.914  1.00 67.06  ? 605  LEU A CD1 1 
ATOM   4361 C CD2 . LEU A 1 579 ? -81.488  6.446   48.495  1.00 61.69  ? 605  LEU A CD2 1 
ATOM   4362 N N   . GLU A 1 580 ? -83.723  10.459  46.554  1.00 63.55  ? 606  GLU A N   1 
ATOM   4363 C CA  . GLU A 1 580 ? -84.373  11.526  45.845  1.00 64.80  ? 606  GLU A CA  1 
ATOM   4364 C C   . GLU A 1 580 ? -83.624  11.981  44.623  1.00 67.69  ? 606  GLU A C   1 
ATOM   4365 O O   . GLU A 1 580 ? -82.420  12.215  44.676  1.00 68.27  ? 606  GLU A O   1 
ATOM   4366 C CB  . GLU A 1 580 ? -84.492  12.710  46.771  1.00 71.14  ? 606  GLU A CB  1 
ATOM   4367 C CG  . GLU A 1 580 ? -85.350  12.426  47.984  1.00 91.25  ? 606  GLU A CG  1 
ATOM   4368 C CD  . GLU A 1 580 ? -85.419  13.601  48.925  1.00 91.44  ? 606  GLU A CD  1 
ATOM   4369 O OE1 . GLU A 1 580 ? -84.673  14.580  48.701  1.00 91.79  ? 606  GLU A OE1 1 
ATOM   4370 O OE2 . GLU A 1 580 ? -86.166  13.513  49.921  1.00 102.16 ? 606  GLU A OE2 1 
ATOM   4371 N N   . SER A 1 581 ? -84.362  12.141  43.529  1.00 64.48  ? 607  SER A N   1 
ATOM   4372 C CA  . SER A 1 581 ? -83.793  12.593  42.274  1.00 60.02  ? 607  SER A CA  1 
ATOM   4373 C C   . SER A 1 581 ? -84.896  13.067  41.346  1.00 60.00  ? 607  SER A C   1 
ATOM   4374 O O   . SER A 1 581 ? -85.905  12.382  41.137  1.00 68.53  ? 607  SER A O   1 
ATOM   4375 C CB  . SER A 1 581 ? -82.999  11.477  41.590  1.00 60.92  ? 607  SER A CB  1 
ATOM   4376 O OG  . SER A 1 581 ? -82.431  11.933  40.359  1.00 55.03  ? 607  SER A OG  1 
ATOM   4377 N N   . LYS A 1 582 ? -84.701  14.254  40.801  1.00 61.85  ? 608  LYS A N   1 
ATOM   4378 C CA  . LYS A 1 582 ? -85.646  14.822  39.871  1.00 71.91  ? 608  LYS A CA  1 
ATOM   4379 C C   . LYS A 1 582 ? -85.396  14.256  38.474  1.00 70.11  ? 608  LYS A C   1 
ATOM   4380 O O   . LYS A 1 582 ? -86.251  14.384  37.606  1.00 77.10  ? 608  LYS A O   1 
ATOM   4381 C CB  . LYS A 1 582 ? -85.531  16.357  39.850  1.00 68.57  ? 608  LYS A CB  1 
ATOM   4382 C CG  . LYS A 1 582 ? -85.968  17.001  41.152  1.00 80.57  ? 608  LYS A CG  1 
ATOM   4383 C CD  . LYS A 1 582 ? -85.885  18.519  41.114  1.00 95.74  ? 608  LYS A CD  1 
ATOM   4384 C CE  . LYS A 1 582 ? -86.406  19.125  42.416  1.00 102.99 ? 608  LYS A CE  1 
ATOM   4385 N NZ  . LYS A 1 582 ? -86.354  20.614  42.422  1.00 106.37 ? 608  LYS A NZ  1 
ATOM   4386 N N   . SER A 1 583 ? -84.263  13.567  38.283  1.00 65.32  ? 609  SER A N   1 
ATOM   4387 C CA  . SER A 1 583 ? -83.907  13.016  36.959  1.00 59.79  ? 609  SER A CA  1 
ATOM   4388 C C   . SER A 1 583 ? -83.881  11.522  36.856  1.00 59.25  ? 609  SER A C   1 
ATOM   4389 O O   . SER A 1 583 ? -84.199  10.964  35.809  1.00 63.42  ? 609  SER A O   1 
ATOM   4390 C CB  . SER A 1 583 ? -82.523  13.525  36.525  1.00 53.48  ? 609  SER A CB  1 
ATOM   4391 O OG  . SER A 1 583 ? -81.534  13.138  37.454  1.00 62.50  ? 609  SER A OG  1 
ATOM   4392 N N   . LEU A 1 584 ? -83.477  10.862  37.924  1.00 59.45  ? 610  LEU A N   1 
ATOM   4393 C CA  . LEU A 1 584 ? -83.379  9.426   37.874  1.00 61.60  ? 610  LEU A CA  1 
ATOM   4394 C C   . LEU A 1 584 ? -84.618  8.776   37.245  1.00 56.01  ? 610  LEU A C   1 
ATOM   4395 O O   . LEU A 1 584 ? -85.738  8.964   37.705  1.00 61.68  ? 610  LEU A O   1 
ATOM   4396 C CB  . LEU A 1 584 ? -83.110  8.828   39.262  1.00 60.78  ? 610  LEU A CB  1 
ATOM   4397 C CG  . LEU A 1 584 ? -82.715  7.347   39.220  1.00 53.38  ? 610  LEU A CG  1 
ATOM   4398 C CD1 . LEU A 1 584 ? -81.391  7.183   38.510  1.00 54.85  ? 610  LEU A CD1 1 
ATOM   4399 C CD2 . LEU A 1 584 ? -82.596  6.779   40.607  1.00 58.54  ? 610  LEU A CD2 1 
ATOM   4400 N N   . VAL A 1 585 ? -84.338  7.900   36.290  1.00 50.18  ? 611  VAL A N   1 
ATOM   4401 C CA  . VAL A 1 585 ? -85.325  7.136   35.529  1.00 55.27  ? 611  VAL A CA  1 
ATOM   4402 C C   . VAL A 1 585 ? -85.401  5.663   35.920  1.00 51.10  ? 611  VAL A C   1 
ATOM   4403 O O   . VAL A 1 585 ? -86.466  5.073   35.908  1.00 54.65  ? 611  VAL A O   1 
ATOM   4404 C CB  . VAL A 1 585 ? -84.958  7.177   34.012  1.00 58.11  ? 611  VAL A CB  1 
ATOM   4405 C CG1 . VAL A 1 585 ? -85.574  6.019   33.266  1.00 67.46  ? 611  VAL A CG1 1 
ATOM   4406 C CG2 . VAL A 1 585 ? -85.330  8.513   33.401  1.00 52.42  ? 611  VAL A CG2 1 
ATOM   4407 N N   . GLU A 1 586 ? -84.260  5.058   36.206  1.00 56.84  ? 612  GLU A N   1 
ATOM   4408 C CA  . GLU A 1 586 ? -84.200  3.642   36.571  1.00 57.89  ? 612  GLU A CA  1 
ATOM   4409 C C   . GLU A 1 586 ? -83.366  3.402   37.837  1.00 56.15  ? 612  GLU A C   1 
ATOM   4410 O O   . GLU A 1 586 ? -82.235  3.902   37.957  1.00 52.93  ? 612  GLU A O   1 
ATOM   4411 C CB  . GLU A 1 586 ? -83.569  2.864   35.409  1.00 52.67  ? 612  GLU A CB  1 
ATOM   4412 C CG  . GLU A 1 586 ? -83.393  1.369   35.632  1.00 52.33  ? 612  GLU A CG  1 
ATOM   4413 C CD  . GLU A 1 586 ? -82.688  0.670   34.454  1.00 64.14  ? 612  GLU A CD  1 
ATOM   4414 O OE1 . GLU A 1 586 ? -82.310  1.353   33.457  1.00 65.66  ? 612  GLU A OE1 1 
ATOM   4415 O OE2 . GLU A 1 586 ? -82.488  -0.567  34.532  1.00 59.75  ? 612  GLU A OE2 1 
ATOM   4416 N N   . LEU A 1 587 ? -83.933  2.628   38.762  1.00 52.74  ? 613  LEU A N   1 
ATOM   4417 C CA  . LEU A 1 587 ? -83.263  2.262   40.005  1.00 49.89  ? 613  LEU A CA  1 
ATOM   4418 C C   . LEU A 1 587 ? -83.277  0.748   40.169  1.00 54.78  ? 613  LEU A C   1 
ATOM   4419 O O   . LEU A 1 587 ? -84.337  0.140   40.212  1.00 47.94  ? 613  LEU A O   1 
ATOM   4420 C CB  . LEU A 1 587 ? -83.953  2.857   41.222  1.00 49.77  ? 613  LEU A CB  1 
ATOM   4421 C CG  . LEU A 1 587 ? -83.303  2.481   42.589  1.00 53.50  ? 613  LEU A CG  1 
ATOM   4422 C CD1 . LEU A 1 587 ? -81.889  3.037   42.717  1.00 45.89  ? 613  LEU A CD1 1 
ATOM   4423 C CD2 . LEU A 1 587 ? -84.141  2.980   43.788  1.00 51.53  ? 613  LEU A CD2 1 
ATOM   4424 N N   . VAL A 1 588 ? -82.105  0.131   40.157  1.00 51.75  ? 614  VAL A N   1 
ATOM   4425 C CA  . VAL A 1 588 ? -82.011  -1.297  40.372  1.00 48.93  ? 614  VAL A CA  1 
ATOM   4426 C C   . VAL A 1 588 ? -81.637  -1.447  41.875  1.00 52.54  ? 614  VAL A C   1 
ATOM   4427 O O   . VAL A 1 588 ? -80.529  -1.089  42.276  1.00 50.11  ? 614  VAL A O   1 
ATOM   4428 C CB  . VAL A 1 588 ? -80.921  -1.917  39.510  1.00 50.81  ? 614  VAL A CB  1 
ATOM   4429 C CG1 . VAL A 1 588 ? -80.812  -3.406  39.792  1.00 52.75  ? 614  VAL A CG1 1 
ATOM   4430 C CG2 . VAL A 1 588 ? -81.175  -1.648  38.033  1.00 52.93  ? 614  VAL A CG2 1 
ATOM   4431 N N   . PHE A 1 589 ? -82.531  -2.021  42.684  1.00 49.69  ? 615  PHE A N   1 
ATOM   4432 C CA  . PHE A 1 589 ? -82.286  -2.167  44.113  1.00 40.49  ? 615  PHE A CA  1 
ATOM   4433 C C   . PHE A 1 589 ? -82.385  -3.593  44.560  1.00 43.01  ? 615  PHE A C   1 
ATOM   4434 O O   . PHE A 1 589 ? -82.773  -3.882  45.682  1.00 44.76  ? 615  PHE A O   1 
ATOM   4435 C CB  . PHE A 1 589 ? -83.317  -1.355  44.851  1.00 44.76  ? 615  PHE A CB  1 
ATOM   4436 C CG  . PHE A 1 589 ? -82.952  -1.039  46.274  1.00 48.47  ? 615  PHE A CG  1 
ATOM   4437 C CD1 . PHE A 1 589 ? -82.133  0.029   46.546  1.00 47.29  ? 615  PHE A CD1 1 
ATOM   4438 C CD2 . PHE A 1 589 ? -83.562  -1.681  47.323  1.00 53.28  ? 615  PHE A CD2 1 
ATOM   4439 C CE1 . PHE A 1 589 ? -81.858  0.399   47.832  1.00 50.44  ? 615  PHE A CE1 1 
ATOM   4440 C CE2 . PHE A 1 589 ? -83.273  -1.325  48.611  1.00 52.59  ? 615  PHE A CE2 1 
ATOM   4441 C CZ  . PHE A 1 589 ? -82.431  -0.275  48.865  1.00 48.74  ? 615  PHE A CZ  1 
ATOM   4442 N N   . SER A 1 590 ? -82.037  -4.510  43.681  1.00 46.68  ? 616  SER A N   1 
ATOM   4443 C CA  . SER A 1 590 ? -82.127  -5.891  44.044  1.00 46.98  ? 616  SER A CA  1 
ATOM   4444 C C   . SER A 1 590 ? -80.978  -6.356  44.928  1.00 45.02  ? 616  SER A C   1 
ATOM   4445 O O   . SER A 1 590 ? -79.919  -5.788  44.912  1.00 51.36  ? 616  SER A O   1 
ATOM   4446 C CB  . SER A 1 590 ? -82.184  -6.749  42.785  1.00 45.52  ? 616  SER A CB  1 
ATOM   4447 O OG  . SER A 1 590 ? -81.005  -6.660  42.068  1.00 45.30  ? 616  SER A OG  1 
ATOM   4448 N N   . GLY A 1 591 ? -81.202  -7.386  45.710  1.00 50.46  ? 617  GLY A N   1 
ATOM   4449 C CA  . GLY A 1 591 ? -80.149  -7.942  46.506  1.00 45.76  ? 617  GLY A CA  1 
ATOM   4450 C C   . GLY A 1 591 ? -79.790  -7.122  47.697  1.00 48.30  ? 617  GLY A C   1 
ATOM   4451 O O   . GLY A 1 591 ? -78.740  -7.276  48.239  1.00 53.56  ? 617  GLY A O   1 
ATOM   4452 N N   . ASN A 1 592 ? -80.667  -6.224  48.074  1.00 49.70  ? 618  ASN A N   1 
ATOM   4453 C CA  . ASN A 1 592 ? -80.535  -5.439  49.273  1.00 47.76  ? 618  ASN A CA  1 
ATOM   4454 C C   . ASN A 1 592 ? -81.454  -5.992  50.338  1.00 52.91  ? 618  ASN A C   1 
ATOM   4455 O O   . ASN A 1 592 ? -81.827  -7.125  50.248  1.00 51.39  ? 618  ASN A O   1 
ATOM   4456 C CB  . ASN A 1 592 ? -80.809  -3.987  48.966  1.00 48.71  ? 618  ASN A CB  1 
ATOM   4457 C CG  . ASN A 1 592 ? -79.694  -3.345  48.197  1.00 56.50  ? 618  ASN A CG  1 
ATOM   4458 O OD1 . ASN A 1 592 ? -78.610  -3.215  48.681  1.00 67.24  ? 618  ASN A OD1 1 
ATOM   4459 N ND2 . ASN A 1 592 ? -79.963  -2.944  47.002  1.00 64.29  ? 618  ASN A ND2 1 
ATOM   4460 N N   . ARG A 1 593 ? -81.798  -5.221  51.358  1.00 49.13  ? 619  ARG A N   1 
ATOM   4461 C CA  . ARG A 1 593 ? -82.667  -5.732  52.404  1.00 54.72  ? 619  ARG A CA  1 
ATOM   4462 C C   . ARG A 1 593 ? -83.861  -4.855  52.745  1.00 57.28  ? 619  ARG A C   1 
ATOM   4463 O O   . ARG A 1 593 ? -83.976  -4.344  53.822  1.00 62.25  ? 619  ARG A O   1 
ATOM   4464 C CB  . ARG A 1 593 ? -81.864  -6.015  53.667  1.00 55.03  ? 619  ARG A CB  1 
ATOM   4465 C CG  . ARG A 1 593 ? -80.644  -6.862  53.470  1.00 48.25  ? 619  ARG A CG  1 
ATOM   4466 C CD  . ARG A 1 593 ? -80.958  -8.328  53.479  1.00 49.31  ? 619  ARG A CD  1 
ATOM   4467 N NE  . ARG A 1 593 ? -82.030  -8.659  54.386  1.00 61.13  ? 619  ARG A NE  1 
ATOM   4468 C CZ  . ARG A 1 593 ? -81.893  -9.442  55.441  1.00 69.36  ? 619  ARG A CZ  1 
ATOM   4469 N NH1 . ARG A 1 593 ? -80.726  -9.962  55.728  1.00 63.36  ? 619  ARG A NH1 1 
ATOM   4470 N NH2 . ARG A 1 593 ? -82.921  -9.697  56.211  1.00 62.93  ? 619  ARG A NH2 1 
ATOM   4471 N N   . LEU A 1 594 ? -84.796  -4.753  51.829  1.00 63.98  ? 620  LEU A N   1 
ATOM   4472 C CA  . LEU A 1 594 ? -86.008  -4.003  52.049  1.00 60.81  ? 620  LEU A CA  1 
ATOM   4473 C C   . LEU A 1 594 ? -86.829  -4.613  53.134  1.00 53.60  ? 620  LEU A C   1 
ATOM   4474 O O   . LEU A 1 594 ? -87.638  -3.950  53.734  1.00 59.82  ? 620  LEU A O   1 
ATOM   4475 C CB  . LEU A 1 594 ? -86.840  -3.958  50.793  1.00 68.16  ? 620  LEU A CB  1 
ATOM   4476 C CG  . LEU A 1 594 ? -86.589  -2.798  49.874  1.00 68.80  ? 620  LEU A CG  1 
ATOM   4477 C CD1 . LEU A 1 594 ? -87.503  -2.941  48.692  1.00 81.22  ? 620  LEU A CD1 1 
ATOM   4478 C CD2 . LEU A 1 594 ? -86.837  -1.497  50.588  1.00 67.80  ? 620  LEU A CD2 1 
ATOM   4479 N N   . ASP A 1 595 ? -86.670  -5.904  53.340  1.00 49.27  ? 621  ASP A N   1 
ATOM   4480 C CA  . ASP A 1 595 ? -87.476  -6.580  54.315  1.00 58.60  ? 621  ASP A CA  1 
ATOM   4481 C C   . ASP A 1 595 ? -87.187  -5.948  55.633  1.00 60.55  ? 621  ASP A C   1 
ATOM   4482 O O   . ASP A 1 595 ? -88.073  -5.739  56.415  1.00 72.06  ? 621  ASP A O   1 
ATOM   4483 C CB  . ASP A 1 595 ? -87.160  -8.052  54.363  1.00 61.45  ? 621  ASP A CB  1 
ATOM   4484 C CG  . ASP A 1 595 ? -85.750  -8.317  54.694  1.00 66.80  ? 621  ASP A CG  1 
ATOM   4485 O OD1 . ASP A 1 595 ? -84.925  -7.461  54.406  1.00 69.86  ? 621  ASP A OD1 1 
ATOM   4486 O OD2 . ASP A 1 595 ? -85.456  -9.380  55.239  1.00 64.32  ? 621  ASP A OD2 1 
ATOM   4487 N N   . ILE A 1 596 ? -85.933  -5.624  55.875  1.00 65.27  ? 622  ILE A N   1 
ATOM   4488 C CA  . ILE A 1 596 ? -85.552  -4.935  57.097  1.00 51.30  ? 622  ILE A CA  1 
ATOM   4489 C C   . ILE A 1 596 ? -85.886  -3.455  57.077  1.00 48.87  ? 622  ILE A C   1 
ATOM   4490 O O   . ILE A 1 596 ? -86.349  -2.924  58.056  1.00 56.46  ? 622  ILE A O   1 
ATOM   4491 C CB  . ILE A 1 596 ? -84.082  -5.178  57.406  1.00 56.74  ? 622  ILE A CB  1 
ATOM   4492 C CG1 . ILE A 1 596 ? -83.887  -6.662  57.761  1.00 52.05  ? 622  ILE A CG1 1 
ATOM   4493 C CG2 . ILE A 1 596 ? -83.619  -4.296  58.547  1.00 53.18  ? 622  ILE A CG2 1 
ATOM   4494 C CD1 . ILE A 1 596 ? -82.442  -7.106  57.830  1.00 55.12  ? 622  ILE A CD1 1 
ATOM   4495 N N   . LEU A 1 597 ? -85.644  -2.773  55.978  1.00 53.07  ? 623  LEU A N   1 
ATOM   4496 C CA  . LEU A 1 597 ? -85.949  -1.334  55.914  1.00 54.21  ? 623  LEU A CA  1 
ATOM   4497 C C   . LEU A 1 597 ? -87.422  -1.053  56.136  1.00 60.08  ? 623  LEU A C   1 
ATOM   4498 O O   . LEU A 1 597 ? -87.771  -0.123  56.833  1.00 73.48  ? 623  LEU A O   1 
ATOM   4499 C CB  . LEU A 1 597 ? -85.520  -0.779  54.564  1.00 53.41  ? 623  LEU A CB  1 
ATOM   4500 C CG  . LEU A 1 597 ? -84.011  -0.733  54.335  1.00 59.14  ? 623  LEU A CG  1 
ATOM   4501 C CD1 . LEU A 1 597 ? -83.665  -0.675  52.855  1.00 58.41  ? 623  LEU A CD1 1 
ATOM   4502 C CD2 . LEU A 1 597 ? -83.373  0.427   55.123  1.00 59.32  ? 623  LEU A CD2 1 
ATOM   4503 N N   . TRP A 1 598 ? -88.284  -1.822  55.476  1.00 72.05  ? 624  TRP A N   1 
ATOM   4504 C CA  . TRP A 1 598 ? -89.719  -1.640  55.611  1.00 71.78  ? 624  TRP A CA  1 
ATOM   4505 C C   . TRP A 1 598 ? -90.369  -2.523  56.653  1.00 80.58  ? 624  TRP A C   1 
ATOM   4506 O O   . TRP A 1 598 ? -91.086  -2.041  57.492  1.00 70.27  ? 624  TRP A O   1 
ATOM   4507 C CB  . TRP A 1 598 ? -90.483  -1.978  54.319  1.00 68.35  ? 624  TRP A CB  1 
ATOM   4508 C CG  . TRP A 1 598 ? -90.293  -1.122  53.171  1.00 68.23  ? 624  TRP A CG  1 
ATOM   4509 C CD1 . TRP A 1 598 ? -90.243  0.248   53.194  1.00 61.33  ? 624  TRP A CD1 1 
ATOM   4510 C CD2 . TRP A 1 598 ? -90.621  -1.470  51.798  1.00 59.14  ? 624  TRP A CD2 1 
ATOM   4511 N NE1 . TRP A 1 598 ? -90.241  0.737   51.908  1.00 66.04  ? 624  TRP A NE1 1 
ATOM   4512 C CE2 . TRP A 1 598 ? -90.528  -0.292  51.039  1.00 64.45  ? 624  TRP A CE2 1 
ATOM   4513 C CE3 . TRP A 1 598 ? -90.911  -2.668  51.143  1.00 64.05  ? 624  TRP A CE3 1 
ATOM   4514 C CZ2 . TRP A 1 598 ? -90.715  -0.279  49.657  1.00 67.70  ? 624  TRP A CZ2 1 
ATOM   4515 C CZ3 . TRP A 1 598 ? -91.081  -2.656  49.769  1.00 67.85  ? 624  TRP A CZ3 1 
ATOM   4516 C CH2 . TRP A 1 598 ? -90.981  -1.474  49.043  1.00 70.29  ? 624  TRP A CH2 1 
ATOM   4517 N N   . ASN A 1 599 ? -90.188  -3.840  56.510  1.00 106.34 ? 625  ASN A N   1 
ATOM   4518 C CA  . ASN A 1 599 ? -90.838  -4.840  57.395  1.00 112.30 ? 625  ASN A CA  1 
ATOM   4519 C C   . ASN A 1 599 ? -90.687  -4.607  58.886  1.00 111.46 ? 625  ASN A C   1 
ATOM   4520 O O   . ASN A 1 599 ? -91.342  -5.274  59.693  1.00 132.11 ? 625  ASN A O   1 
ATOM   4521 C CB  . ASN A 1 599 ? -90.506  -6.309  56.998  1.00 118.54 ? 625  ASN A CB  1 
ATOM   4522 C CG  . ASN A 1 599 ? -91.042  -6.698  55.591  1.00 115.18 ? 625  ASN A CG  1 
ATOM   4523 O OD1 . ASN A 1 599 ? -91.026  -7.893  55.188  1.00 86.66  ? 625  ASN A OD1 1 
ATOM   4524 N ND2 . ASN A 1 599 ? -91.524  -5.702  54.844  1.00 101.30 ? 625  ASN A ND2 1 
ATOM   4525 N N   . ASP A 1 600 ? -89.799  -3.695  59.256  1.00 90.42  ? 626  ASP A N   1 
ATOM   4526 C CA  . ASP A 1 600 ? -89.627  -3.343  60.656  1.00 105.37 ? 626  ASP A CA  1 
ATOM   4527 C C   . ASP A 1 600 ? -89.393  -1.850  60.622  1.00 96.79  ? 626  ASP A C   1 
ATOM   4528 O O   . ASP A 1 600 ? -89.282  -1.264  59.542  1.00 80.74  ? 626  ASP A O   1 
ATOM   4529 C CB  . ASP A 1 600 ? -88.344  -3.945  61.277  1.00 116.50 ? 626  ASP A CB  1 
ATOM   4530 C CG  . ASP A 1 600 ? -88.198  -5.439  61.045  1.00 132.00 ? 626  ASP A CG  1 
ATOM   4531 O OD1 . ASP A 1 600 ? -87.034  -5.918  61.076  1.00 113.99 ? 626  ASP A OD1 1 
ATOM   4532 O OD2 . ASP A 1 600 ? -89.213  -6.117  60.764  1.00 132.62 ? 626  ASP A OD2 1 
ATOM   4533 N N   . ASP A 1 601 ? -89.502  -1.240  61.787  1.00 105.84 ? 627  ASP A N   1 
ATOM   4534 C CA  . ASP A 1 601 ? -89.130  0.140   61.927  1.00 108.90 ? 627  ASP A CA  1 
ATOM   4535 C C   . ASP A 1 601 ? -90.099  1.108   62.609  1.00 110.19 ? 627  ASP A C   1 
ATOM   4536 O O   . ASP A 1 601 ? -91.007  0.726   63.329  1.00 92.84  ? 627  ASP A O   1 
ATOM   4537 C CB  . ASP A 1 601 ? -88.689  0.680   60.582  1.00 96.79  ? 627  ASP A CB  1 
ATOM   4538 C CG  . ASP A 1 601 ? -87.729  1.795   60.732  1.00 100.59 ? 627  ASP A CG  1 
ATOM   4539 O OD1 . ASP A 1 601 ? -88.166  2.946   60.616  1.00 104.76 ? 627  ASP A OD1 1 
ATOM   4540 O OD2 . ASP A 1 601 ? -86.556  1.525   61.021  1.00 96.11  ? 627  ASP A OD2 1 
ATOM   4541 N N   . ASP A 1 602 ? -89.808  2.382   62.396  1.00 122.88 ? 628  ASP A N   1 
ATOM   4542 C CA  . ASP A 1 602 ? -90.626  3.512   62.767  1.00 106.14 ? 628  ASP A CA  1 
ATOM   4543 C C   . ASP A 1 602 ? -91.165  4.123   61.498  1.00 108.61 ? 628  ASP A C   1 
ATOM   4544 O O   . ASP A 1 602 ? -91.467  5.304   61.457  1.00 92.01  ? 628  ASP A O   1 
ATOM   4545 C CB  . ASP A 1 602 ? -89.788  4.553   63.469  1.00 105.97 ? 628  ASP A CB  1 
ATOM   4546 C CG  . ASP A 1 602 ? -90.166  4.717   64.894  1.00 108.89 ? 628  ASP A CG  1 
ATOM   4547 O OD1 . ASP A 1 602 ? -89.910  5.795   65.451  1.00 107.06 ? 628  ASP A OD1 1 
ATOM   4548 O OD2 . ASP A 1 602 ? -90.721  3.766   65.457  1.00 112.17 ? 628  ASP A OD2 1 
ATOM   4549 N N   . ASN A 1 603 ? -91.240  3.330   60.444  1.00 91.22  ? 629  ASN A N   1 
ATOM   4550 C CA  . ASN A 1 603 ? -91.620  3.859   59.168  1.00 92.09  ? 629  ASN A CA  1 
ATOM   4551 C C   . ASN A 1 603 ? -90.583  4.830   58.692  1.00 88.29  ? 629  ASN A C   1 
ATOM   4552 O O   . ASN A 1 603 ? -90.889  5.819   58.060  1.00 83.57  ? 629  ASN A O   1 
ATOM   4553 C CB  . ASN A 1 603 ? -92.941  4.581   59.308  1.00 97.09  ? 629  ASN A CB  1 
ATOM   4554 C CG  . ASN A 1 603 ? -94.040  3.681   59.792  1.00 93.18  ? 629  ASN A CG  1 
ATOM   4555 O OD1 . ASN A 1 603 ? -94.929  4.112   60.506  1.00 109.58 ? 629  ASN A OD1 1 
ATOM   4556 N ND2 . ASN A 1 603 ? -93.987  2.425   59.405  1.00 88.72  ? 629  ASN A ND2 1 
ATOM   4557 N N   . ARG A 1 604 ? -89.338  4.549   59.020  1.00 89.91  ? 630  ARG A N   1 
ATOM   4558 C CA  . ARG A 1 604 ? -88.260  5.410   58.603  1.00 84.36  ? 630  ARG A CA  1 
ATOM   4559 C C   . ARG A 1 604 ? -88.170  5.437   57.099  1.00 80.64  ? 630  ARG A C   1 
ATOM   4560 O O   . ARG A 1 604 ? -88.013  6.484   56.506  1.00 66.01  ? 630  ARG A O   1 
ATOM   4561 C CB  . ARG A 1 604 ? -86.957  4.885   59.173  1.00 95.83  ? 630  ARG A CB  1 
ATOM   4562 C CG  . ARG A 1 604 ? -86.088  5.913   59.855  1.00 103.68 ? 630  ARG A CG  1 
ATOM   4563 C CD  . ARG A 1 604 ? -85.232  5.259   60.919  1.00 109.12 ? 630  ARG A CD  1 
ATOM   4564 N NE  . ARG A 1 604 ? -85.213  6.070   62.122  1.00 115.30 ? 630  ARG A NE  1 
ATOM   4565 C CZ  . ARG A 1 604 ? -84.158  6.741   62.541  1.00 105.22 ? 630  ARG A CZ  1 
ATOM   4566 N NH1 . ARG A 1 604 ? -83.029  6.679   61.857  1.00 97.90  ? 630  ARG A NH1 1 
ATOM   4567 N NH2 . ARG A 1 604 ? -84.236  7.470   63.640  1.00 107.82 ? 630  ARG A NH2 1 
ATOM   4568 N N   . TYR A 1 605 ? -88.297  4.273   56.486  1.00 75.83  ? 631  TYR A N   1 
ATOM   4569 C CA  . TYR A 1 605 ? -88.127  4.132   55.042  1.00 80.09  ? 631  TYR A CA  1 
ATOM   4570 C C   . TYR A 1 605 ? -89.463  3.818   54.356  1.00 77.83  ? 631  TYR A C   1 
ATOM   4571 O O   . TYR A 1 605 ? -89.517  3.112   53.343  1.00 73.38  ? 631  TYR A O   1 
ATOM   4572 C CB  . TYR A 1 605 ? -87.103  3.002   54.777  1.00 79.71  ? 631  TYR A CB  1 
ATOM   4573 C CG  . TYR A 1 605 ? -85.839  3.128   55.615  1.00 68.43  ? 631  TYR A CG  1 
ATOM   4574 C CD1 . TYR A 1 605 ? -84.836  4.000   55.261  1.00 61.89  ? 631  TYR A CD1 1 
ATOM   4575 C CD2 . TYR A 1 605 ? -85.669  2.369   56.774  1.00 70.60  ? 631  TYR A CD2 1 
ATOM   4576 C CE1 . TYR A 1 605 ? -83.712  4.146   56.042  1.00 67.89  ? 631  TYR A CE1 1 
ATOM   4577 C CE2 . TYR A 1 605 ? -84.544  2.498   57.562  1.00 58.80  ? 631  TYR A CE2 1 
ATOM   4578 C CZ  . TYR A 1 605 ? -83.566  3.392   57.195  1.00 67.77  ? 631  TYR A CZ  1 
ATOM   4579 O OH  . TYR A 1 605 ? -82.422  3.531   57.962  1.00 63.47  ? 631  TYR A OH  1 
ATOM   4580 N N   . ILE A 1 606 ? -90.533  4.419   54.850  1.00 71.64  ? 632  ILE A N   1 
ATOM   4581 C CA  . ILE A 1 606 ? -91.842  4.149   54.295  1.00 67.46  ? 632  ILE A CA  1 
ATOM   4582 C C   . ILE A 1 606 ? -92.007  4.868   52.960  1.00 66.13  ? 632  ILE A C   1 
ATOM   4583 O O   . ILE A 1 606 ? -92.707  4.399   52.081  1.00 80.10  ? 632  ILE A O   1 
ATOM   4584 C CB  . ILE A 1 606 ? -92.951  4.583   55.270  1.00 78.08  ? 632  ILE A CB  1 
ATOM   4585 C CG1 . ILE A 1 606 ? -94.172  3.685   55.111  1.00 82.11  ? 632  ILE A CG1 1 
ATOM   4586 C CG2 . ILE A 1 606 ? -93.209  6.097   55.215  1.00 73.46  ? 632  ILE A CG2 1 
ATOM   4587 C CD1 . ILE A 1 606 ? -93.874  2.252   55.499  1.00 83.23  ? 632  ILE A CD1 1 
ATOM   4588 N N   . SER A 1 607 ? -91.278  5.964   52.797  1.00 64.73  ? 633  SER A N   1 
ATOM   4589 C CA  . SER A 1 607 ? -91.310  6.768   51.584  1.00 69.48  ? 633  SER A CA  1 
ATOM   4590 C C   . SER A 1 607 ? -89.913  6.808   50.965  1.00 70.09  ? 633  SER A C   1 
ATOM   4591 O O   . SER A 1 607 ? -89.498  7.819   50.364  1.00 66.43  ? 633  SER A O   1 
ATOM   4592 C CB  . SER A 1 607 ? -91.714  8.188   51.963  1.00 70.55  ? 633  SER A CB  1 
ATOM   4593 O OG  . SER A 1 607 ? -92.934  8.160   52.670  1.00 84.72  ? 633  SER A OG  1 
ATOM   4594 N N   . ILE A 1 608 ? -89.209  5.689   51.052  1.00 62.06  ? 634  ILE A N   1 
ATOM   4595 C CA  . ILE A 1 608 ? -87.843  5.642   50.556  1.00 65.58  ? 634  ILE A CA  1 
ATOM   4596 C C   . ILE A 1 608 ? -87.633  5.987   49.079  1.00 63.75  ? 634  ILE A C   1 
ATOM   4597 O O   . ILE A 1 608 ? -86.664  6.679   48.739  1.00 63.08  ? 634  ILE A O   1 
ATOM   4598 C CB  . ILE A 1 608 ? -87.172  4.304   50.884  1.00 67.24  ? 634  ILE A CB  1 
ATOM   4599 C CG1 . ILE A 1 608 ? -85.657  4.408   50.624  1.00 69.81  ? 634  ILE A CG1 1 
ATOM   4600 C CG2 . ILE A 1 608 ? -87.836  3.171   50.109  1.00 66.89  ? 634  ILE A CG2 1 
ATOM   4601 C CD1 . ILE A 1 608 ? -84.863  3.197   51.061  1.00 61.72  ? 634  ILE A CD1 1 
ATOM   4602 N N   . PHE A 1 609 ? -88.521  5.524   48.199  1.00 70.44  ? 635  PHE A N   1 
ATOM   4603 C CA  . PHE A 1 609 ? -88.357  5.815   46.770  1.00 70.83  ? 635  PHE A CA  1 
ATOM   4604 C C   . PHE A 1 609 ? -89.256  6.938   46.248  1.00 70.03  ? 635  PHE A C   1 
ATOM   4605 O O   . PHE A 1 609 ? -89.043  7.439   45.151  1.00 57.58  ? 635  PHE A O   1 
ATOM   4606 C CB  . PHE A 1 609 ? -88.588  4.560   45.931  1.00 66.39  ? 635  PHE A CB  1 
ATOM   4607 C CG  . PHE A 1 609 ? -87.803  3.380   46.393  1.00 63.94  ? 635  PHE A CG  1 
ATOM   4608 C CD1 . PHE A 1 609 ? -86.426  3.358   46.267  1.00 66.53  ? 635  PHE A CD1 1 
ATOM   4609 C CD2 . PHE A 1 609 ? -88.446  2.269   46.904  1.00 64.63  ? 635  PHE A CD2 1 
ATOM   4610 C CE1 . PHE A 1 609 ? -85.694  2.284   46.715  1.00 62.59  ? 635  PHE A CE1 1 
ATOM   4611 C CE2 . PHE A 1 609 ? -87.723  1.178   47.337  1.00 68.10  ? 635  PHE A CE2 1 
ATOM   4612 C CZ  . PHE A 1 609 ? -86.340  1.183   47.224  1.00 67.08  ? 635  PHE A CZ  1 
ATOM   4613 N N   . LYS A 1 610 ? -90.191  7.392   47.068  1.00 72.49  ? 636  LYS A N   1 
ATOM   4614 C CA  . LYS A 1 610 ? -91.127  8.425   46.647  1.00 82.69  ? 636  LYS A CA  1 
ATOM   4615 C C   . LYS A 1 610 ? -90.489  9.642   45.968  1.00 73.93  ? 636  LYS A C   1 
ATOM   4616 O O   . LYS A 1 610 ? -90.998  10.123  44.953  1.00 73.67  ? 636  LYS A O   1 
ATOM   4617 C CB  . LYS A 1 610 ? -91.986  8.867   47.834  1.00 90.09  ? 636  LYS A CB  1 
ATOM   4618 C CG  . LYS A 1 610 ? -93.092  9.846   47.478  1.00 94.13  ? 636  LYS A CG  1 
ATOM   4619 C CD  . LYS A 1 610 ? -93.888  10.222  48.719  1.00 115.47 ? 636  LYS A CD  1 
ATOM   4620 C CE  . LYS A 1 610 ? -94.998  11.216  48.414  1.00 115.58 ? 636  LYS A CE  1 
ATOM   4621 N NZ  . LYS A 1 610 ? -96.009  10.652  47.484  1.00 114.51 ? 636  LYS A NZ  1 
ATOM   4622 N N   . GLY A 1 611 ? -89.355  10.100  46.491  1.00 69.59  ? 637  GLY A N   1 
ATOM   4623 C CA  . GLY A 1 611 ? -88.652  11.286  45.947  1.00 62.09  ? 637  GLY A CA  1 
ATOM   4624 C C   . GLY A 1 611 ? -87.949  11.105  44.614  1.00 64.18  ? 637  GLY A C   1 
ATOM   4625 O O   . GLY A 1 611 ? -87.139  11.944  44.208  1.00 65.92  ? 637  GLY A O   1 
ATOM   4626 N N   . LEU A 1 612 ? -88.176  9.954   43.995  1.00 62.45  ? 638  LEU A N   1 
ATOM   4627 C CA  . LEU A 1 612 ? -87.624  9.627   42.701  1.00 68.97  ? 638  LEU A CA  1 
ATOM   4628 C C   . LEU A 1 612 ? -88.771  9.957   41.739  1.00 72.01  ? 638  LEU A C   1 
ATOM   4629 O O   . LEU A 1 612 ? -89.419  9.082   41.145  1.00 70.87  ? 638  LEU A O   1 
ATOM   4630 C CB  . LEU A 1 612 ? -87.221  8.151   42.674  1.00 64.95  ? 638  LEU A CB  1 
ATOM   4631 C CG  . LEU A 1 612 ? -86.117  7.827   43.681  1.00 64.63  ? 638  LEU A CG  1 
ATOM   4632 C CD1 . LEU A 1 612 ? -85.837  6.343   43.712  1.00 67.03  ? 638  LEU A CD1 1 
ATOM   4633 C CD2 . LEU A 1 612 ? -84.847  8.602   43.372  1.00 65.63  ? 638  LEU A CD2 1 
ATOM   4634 N N   . LYS A 1 613 ? -89.023  11.259  41.657  1.00 73.81  ? 639  LYS A N   1 
ATOM   4635 C CA  . LYS A 1 613 ? -90.107  11.853  40.872  1.00 78.94  ? 639  LYS A CA  1 
ATOM   4636 C C   . LYS A 1 613 ? -90.216  11.515  39.400  1.00 71.38  ? 639  LYS A C   1 
ATOM   4637 O O   . LYS A 1 613 ? -91.308  11.535  38.855  1.00 89.97  ? 639  LYS A O   1 
ATOM   4638 C CB  . LYS A 1 613 ? -90.068  13.386  41.037  1.00 85.27  ? 639  LYS A CB  1 
ATOM   4639 C CG  . LYS A 1 613 ? -90.355  13.865  42.457  1.00 95.61  ? 639  LYS A CG  1 
ATOM   4640 C CD  . LYS A 1 613 ? -91.773  13.480  42.902  1.00 114.29 ? 639  LYS A CD  1 
ATOM   4641 C CE  . LYS A 1 613 ? -92.067  13.856  44.354  1.00 127.63 ? 639  LYS A CE  1 
ATOM   4642 N NZ  . LYS A 1 613 ? -91.979  15.318  44.640  1.00 136.27 ? 639  LYS A NZ  1 
ATOM   4643 N N   . ASN A 1 614 ? -89.125  11.114  38.777  1.00 72.54  ? 640  ASN A N   1 
ATOM   4644 C CA  . ASN A 1 614 ? -89.148  10.829  37.346  1.00 64.40  ? 640  ASN A CA  1 
ATOM   4645 C C   . ASN A 1 614 ? -88.852  9.376   37.069  1.00 65.04  ? 640  ASN A C   1 
ATOM   4646 O O   . ASN A 1 614 ? -88.626  8.996   35.934  1.00 60.97  ? 640  ASN A O   1 
ATOM   4647 C CB  . ASN A 1 614 ? -88.078  11.710  36.696  1.00 59.75  ? 640  ASN A CB  1 
ATOM   4648 C CG  . ASN A 1 614 ? -88.183  11.789  35.190  1.00 64.87  ? 640  ASN A CG  1 
ATOM   4649 O OD1 . ASN A 1 614 ? -89.096  11.258  34.571  1.00 87.10  ? 640  ASN A OD1 1 
ATOM   4650 N ND2 . ASN A 1 614 ? -87.235  12.489  34.600  1.00 65.66  ? 640  ASN A ND2 1 
ATOM   4651 N N   . LEU A 1 615 ? -89.008  8.534   38.077  1.00 64.51  ? 641  LEU A N   1 
ATOM   4652 C CA  . LEU A 1 615 ? -88.670  7.138   37.911  1.00 62.23  ? 641  LEU A CA  1 
ATOM   4653 C C   . LEU A 1 615 ? -89.693  6.362   37.120  1.00 58.08  ? 641  LEU A C   1 
ATOM   4654 O O   . LEU A 1 615 ? -90.870  6.399   37.445  1.00 67.41  ? 641  LEU A O   1 
ATOM   4655 C CB  . LEU A 1 615 ? -88.539  6.492   39.305  1.00 66.41  ? 641  LEU A CB  1 
ATOM   4656 C CG  . LEU A 1 615 ? -87.863  5.122   39.397  1.00 62.11  ? 641  LEU A CG  1 
ATOM   4657 C CD1 . LEU A 1 615 ? -86.383  5.308   39.094  1.00 63.97  ? 641  LEU A CD1 1 
ATOM   4658 C CD2 . LEU A 1 615 ? -88.012  4.528   40.780  1.00 64.37  ? 641  LEU A CD2 1 
ATOM   4659 N N   . THR A 1 616 ? -89.229  5.552   36.176  1.00 61.02  ? 642  THR A N   1 
ATOM   4660 C CA  . THR A 1 616 ? -90.130  4.703   35.379  1.00 61.07  ? 642  THR A CA  1 
ATOM   4661 C C   . THR A 1 616 ? -89.866  3.205   35.546  1.00 60.37  ? 642  THR A C   1 
ATOM   4662 O O   . THR A 1 616 ? -90.733  2.396   35.219  1.00 65.44  ? 642  THR A O   1 
ATOM   4663 C CB  . THR A 1 616 ? -90.111  5.050   33.891  1.00 59.49  ? 642  THR A CB  1 
ATOM   4664 O OG1 . THR A 1 616 ? -88.800  4.874   33.356  1.00 60.93  ? 642  THR A OG1 1 
ATOM   4665 C CG2 . THR A 1 616 ? -90.528  6.462   33.698  1.00 66.31  ? 642  THR A CG2 1 
ATOM   4666 N N   . ARG A 1 617 ? -88.645  2.826   35.921  1.00 60.28  ? 643  ARG A N   1 
ATOM   4667 C CA  . ARG A 1 617 ? -88.307  1.395   36.158  1.00 63.50  ? 643  ARG A CA  1 
ATOM   4668 C C   . ARG A 1 617 ? -87.761  1.210   37.576  1.00 64.11  ? 643  ARG A C   1 
ATOM   4669 O O   . ARG A 1 617 ? -86.924  1.989   38.027  1.00 62.00  ? 643  ARG A O   1 
ATOM   4670 C CB  . ARG A 1 617 ? -87.289  0.815   35.160  1.00 61.36  ? 643  ARG A CB  1 
ATOM   4671 C CG  . ARG A 1 617 ? -87.775  0.542   33.736  1.00 89.76  ? 643  ARG A CG  1 
ATOM   4672 C CD  . ARG A 1 617 ? -88.051  1.757   32.849  1.00 97.47  ? 643  ARG A CD  1 
ATOM   4673 N NE  . ARG A 1 617 ? -86.826  2.496   32.574  1.00 111.98 ? 643  ARG A NE  1 
ATOM   4674 C CZ  . ARG A 1 617 ? -85.950  2.169   31.630  1.00 111.60 ? 643  ARG A CZ  1 
ATOM   4675 N NH1 . ARG A 1 617 ? -84.842  2.889   31.469  1.00 105.89 ? 643  ARG A NH1 1 
ATOM   4676 N NH2 . ARG A 1 617 ? -86.160  1.098   30.873  1.00 110.89 ? 643  ARG A NH2 1 
ATOM   4677 N N   . LEU A 1 618 ? -88.215  0.156   38.254  1.00 58.32  ? 644  LEU A N   1 
ATOM   4678 C CA  . LEU A 1 618 ? -87.771  -0.144  39.616  1.00 56.19  ? 644  LEU A CA  1 
ATOM   4679 C C   . LEU A 1 618 ? -87.646  -1.650  39.851  1.00 54.38  ? 644  LEU A C   1 
ATOM   4680 O O   . LEU A 1 618 ? -88.600  -2.396  39.688  1.00 58.06  ? 644  LEU A O   1 
ATOM   4681 C CB  . LEU A 1 618 ? -88.730  0.464   40.643  1.00 53.42  ? 644  LEU A CB  1 
ATOM   4682 C CG  . LEU A 1 618 ? -88.372  0.276   42.130  1.00 62.55  ? 644  LEU A CG  1 
ATOM   4683 C CD1 . LEU A 1 618 ? -87.001  0.857   42.461  1.00 65.58  ? 644  LEU A CD1 1 
ATOM   4684 C CD2 . LEU A 1 618 ? -89.420  0.886   43.057  1.00 58.25  ? 644  LEU A CD2 1 
ATOM   4685 N N   . ASP A 1 619 ? -86.456  -2.099  40.213  1.00 56.50  ? 645  ASP A N   1 
ATOM   4686 C CA  . ASP A 1 619 ? -86.239  -3.522  40.476  1.00 56.39  ? 645  ASP A CA  1 
ATOM   4687 C C   . ASP A 1 619 ? -86.066  -3.759  41.977  1.00 58.76  ? 645  ASP A C   1 
ATOM   4688 O O   . ASP A 1 619 ? -85.099  -3.281  42.580  1.00 59.81  ? 645  ASP A O   1 
ATOM   4689 C CB  . ASP A 1 619 ? -85.016  -4.036  39.710  1.00 50.98  ? 645  ASP A CB  1 
ATOM   4690 C CG  . ASP A 1 619 ? -84.743  -5.497  39.971  1.00 57.99  ? 645  ASP A CG  1 
ATOM   4691 O OD1 . ASP A 1 619 ? -85.344  -6.066  40.926  1.00 59.33  ? 645  ASP A OD1 1 
ATOM   4692 O OD2 . ASP A 1 619 ? -83.883  -6.063  39.260  1.00 57.40  ? 645  ASP A OD2 1 
ATOM   4693 N N   . LEU A 1 620 ? -87.021  -4.471  42.572  1.00 52.79  ? 646  LEU A N   1 
ATOM   4694 C CA  . LEU A 1 620 ? -86.981  -4.789  43.993  1.00 46.31  ? 646  LEU A CA  1 
ATOM   4695 C C   . LEU A 1 620 ? -86.833  -6.280  44.213  1.00 45.82  ? 646  LEU A C   1 
ATOM   4696 O O   . LEU A 1 620 ? -87.224  -6.800  45.255  1.00 53.77  ? 646  LEU A O   1 
ATOM   4697 C CB  . LEU A 1 620 ? -88.237  -4.319  44.712  1.00 48.39  ? 646  LEU A CB  1 
ATOM   4698 C CG  . LEU A 1 620 ? -88.573  -2.845  44.521  1.00 54.03  ? 646  LEU A CG  1 
ATOM   4699 C CD1 . LEU A 1 620 ? -89.799  -2.501  45.349  1.00 55.68  ? 646  LEU A CD1 1 
ATOM   4700 C CD2 . LEU A 1 620 ? -87.418  -1.947  44.910  1.00 58.96  ? 646  LEU A CD2 1 
ATOM   4701 N N   . SER A 1 621 ? -86.246  -6.977  43.258  1.00 42.23  ? 647  SER A N   1 
ATOM   4702 C CA  . SER A 1 621 ? -86.087  -8.409  43.418  1.00 45.70  ? 647  SER A CA  1 
ATOM   4703 C C   . SER A 1 621 ? -85.054  -8.749  44.478  1.00 48.99  ? 647  SER A C   1 
ATOM   4704 O O   . SER A 1 621 ? -84.361  -7.880  44.959  1.00 51.30  ? 647  SER A O   1 
ATOM   4705 C CB  . SER A 1 621 ? -85.725  -9.034  42.082  1.00 46.34  ? 647  SER A CB  1 
ATOM   4706 O OG  . SER A 1 621 ? -84.674  -8.306  41.465  1.00 46.08  ? 647  SER A OG  1 
ATOM   4707 N N   . LEU A 1 622 ? -85.016  -10.010 44.890  1.00 52.38  ? 648  LEU A N   1 
ATOM   4708 C CA  . LEU A 1 622 ? -84.059  -10.466 45.887  1.00 50.52  ? 648  LEU A CA  1 
ATOM   4709 C C   . LEU A 1 622 ? -83.889  -9.552  47.119  1.00 47.26  ? 648  LEU A C   1 
ATOM   4710 O O   . LEU A 1 622 ? -82.802  -9.111  47.404  1.00 50.85  ? 648  LEU A O   1 
ATOM   4711 C CB  . LEU A 1 622 ? -82.718  -10.698 45.212  1.00 47.47  ? 648  LEU A CB  1 
ATOM   4712 C CG  . LEU A 1 622 ? -82.679  -11.888 44.275  1.00 50.01  ? 648  LEU A CG  1 
ATOM   4713 C CD1 . LEU A 1 622 ? -81.429  -11.940 43.426  1.00 50.16  ? 648  LEU A CD1 1 
ATOM   4714 C CD2 . LEU A 1 622 ? -82.761  -13.146 45.101  1.00 55.64  ? 648  LEU A CD2 1 
ATOM   4715 N N   . ASN A 1 623 ? -84.985  -9.147  47.734  1.00 46.18  ? 649  ASN A N   1 
ATOM   4716 C CA  . ASN A 1 623 ? -84.933  -8.346  48.952  1.00 49.22  ? 649  ASN A CA  1 
ATOM   4717 C C   . ASN A 1 623 ? -85.579  -9.071  50.139  1.00 49.78  ? 649  ASN A C   1 
ATOM   4718 O O   . ASN A 1 623 ? -85.875  -8.457  51.174  1.00 53.31  ? 649  ASN A O   1 
ATOM   4719 C CB  . ASN A 1 623 ? -85.582  -6.975  48.795  1.00 54.98  ? 649  ASN A CB  1 
ATOM   4720 C CG  . ASN A 1 623 ? -84.661  -5.947  48.187  1.00 59.57  ? 649  ASN A CG  1 
ATOM   4721 O OD1 . ASN A 1 623 ? -84.274  -5.014  48.881  1.00 58.03  ? 649  ASN A OD1 1 
ATOM   4722 N ND2 . ASN A 1 623 ? -84.181  -6.185  46.983  1.00 66.48  ? 649  ASN A ND2 1 
ATOM   4723 N N   . ARG A 1 624 ? -85.842  -10.358 49.965  1.00 47.56  ? 650  ARG A N   1 
ATOM   4724 C CA  . ARG A 1 624 ? -86.445  -11.187 51.004  1.00 53.77  ? 650  ARG A CA  1 
ATOM   4725 C C   . ARG A 1 624 ? -87.767  -10.635 51.510  1.00 56.77  ? 650  ARG A C   1 
ATOM   4726 O O   . ARG A 1 624 ? -88.065  -10.705 52.692  1.00 61.13  ? 650  ARG A O   1 
ATOM   4727 C CB  . ARG A 1 624 ? -85.481  -11.336 52.167  1.00 56.02  ? 650  ARG A CB  1 
ATOM   4728 C CG  . ARG A 1 624 ? -84.128  -11.817 51.728  1.00 64.33  ? 650  ARG A CG  1 
ATOM   4729 C CD  . ARG A 1 624 ? -83.172  -11.924 52.875  1.00 72.44  ? 650  ARG A CD  1 
ATOM   4730 N NE  . ARG A 1 624 ? -81.807  -12.116 52.394  1.00 95.32  ? 650  ARG A NE  1 
ATOM   4731 C CZ  . ARG A 1 624 ? -80.756  -12.308 53.182  1.00 99.21  ? 650  ARG A CZ  1 
ATOM   4732 N NH1 . ARG A 1 624 ? -80.925  -12.434 54.490  1.00 105.69 ? 650  ARG A NH1 1 
ATOM   4733 N NH2 . ARG A 1 624 ? -79.548  -12.452 52.655  1.00 100.55 ? 650  ARG A NH2 1 
ATOM   4734 N N   . LEU A 1 625 ? -88.553  -10.045 50.640  1.00 55.66  ? 651  LEU A N   1 
ATOM   4735 C CA  . LEU A 1 625 ? -89.825  -9.522  51.090  1.00 60.57  ? 651  LEU A CA  1 
ATOM   4736 C C   . LEU A 1 625 ? -90.863  -10.646 51.279  1.00 65.16  ? 651  LEU A C   1 
ATOM   4737 O O   . LEU A 1 625 ? -91.038  -11.493 50.395  1.00 62.89  ? 651  LEU A O   1 
ATOM   4738 C CB  . LEU A 1 625 ? -90.345  -8.484  50.116  1.00 57.25  ? 651  LEU A CB  1 
ATOM   4739 C CG  . LEU A 1 625 ? -89.566  -7.191  50.097  1.00 62.54  ? 651  LEU A CG  1 
ATOM   4740 C CD1 . LEU A 1 625 ? -89.971  -6.354  48.904  1.00 72.71  ? 651  LEU A CD1 1 
ATOM   4741 C CD2 . LEU A 1 625 ? -89.784  -6.418  51.386  1.00 66.11  ? 651  LEU A CD2 1 
ATOM   4742 N N   . LYS A 1 626 ? -91.438  -10.707 52.487  1.00 66.65  ? 652  LYS A N   1 
ATOM   4743 C CA  . LYS A 1 626 ? -92.478  -11.675 52.837  1.00 62.05  ? 652  LYS A CA  1 
ATOM   4744 C C   . LYS A 1 626 ? -93.799  -10.915 52.879  1.00 63.25  ? 652  LYS A C   1 
ATOM   4745 O O   . LYS A 1 626 ? -94.866  -11.489 52.674  1.00 77.95  ? 652  LYS A O   1 
ATOM   4746 C CB  . LYS A 1 626 ? -92.256  -12.277 54.223  1.00 62.79  ? 652  LYS A CB  1 
ATOM   4747 C CG  . LYS A 1 626 ? -91.079  -13.222 54.431  1.00 67.36  ? 652  LYS A CG  1 
ATOM   4748 C CD  . LYS A 1 626 ? -91.057  -13.590 55.917  1.00 70.01  ? 652  LYS A CD  1 
ATOM   4749 C CE  . LYS A 1 626 ? -89.905  -14.490 56.355  1.00 88.83  ? 652  LYS A CE  1 
ATOM   4750 N NZ  . LYS A 1 626 ? -89.937  -15.875 55.815  1.00 86.87  ? 652  LYS A NZ  1 
ATOM   4751 N N   . HIS A 1 627 ? -93.714  -9.608  53.088  1.00 63.38  ? 653  HIS A N   1 
ATOM   4752 C CA  . HIS A 1 627 ? -94.893  -8.760  53.182  1.00 77.67  ? 653  HIS A CA  1 
ATOM   4753 C C   . HIS A 1 627 ? -94.537  -7.283  52.937  1.00 80.81  ? 653  HIS A C   1 
ATOM   4754 O O   . HIS A 1 627 ? -93.572  -6.772  53.487  1.00 84.53  ? 653  HIS A O   1 
ATOM   4755 C CB  . HIS A 1 627 ? -95.521  -8.950  54.580  1.00 85.98  ? 653  HIS A CB  1 
ATOM   4756 C CG  . HIS A 1 627 ? -96.659  -8.020  54.879  1.00 115.91 ? 653  HIS A CG  1 
ATOM   4757 N ND1 . HIS A 1 627 ? -96.502  -6.867  55.621  1.00 128.81 ? 653  HIS A ND1 1 
ATOM   4758 C CD2 . HIS A 1 627 ? -97.969  -8.072  54.540  1.00 123.10 ? 653  HIS A CD2 1 
ATOM   4759 C CE1 . HIS A 1 627 ? -97.668  -6.257  55.739  1.00 126.17 ? 653  HIS A CE1 1 
ATOM   4760 N NE2 . HIS A 1 627 ? -98.573  -6.962  55.082  1.00 133.67 ? 653  HIS A NE2 1 
ATOM   4761 N N   . ILE A 1 628 ? -95.327  -6.602  52.119  1.00 75.72  ? 654  ILE A N   1 
ATOM   4762 C CA  . ILE A 1 628 ? -95.083  -5.202  51.825  1.00 66.45  ? 654  ILE A CA  1 
ATOM   4763 C C   . ILE A 1 628 ? -96.083  -4.309  52.520  1.00 68.36  ? 654  ILE A C   1 
ATOM   4764 O O   . ILE A 1 628 ? -97.279  -4.427  52.306  1.00 74.10  ? 654  ILE A O   1 
ATOM   4765 C CB  . ILE A 1 628 ? -95.189  -4.933  50.322  1.00 67.25  ? 654  ILE A CB  1 
ATOM   4766 C CG1 . ILE A 1 628 ? -94.208  -5.832  49.573  1.00 69.74  ? 654  ILE A CG1 1 
ATOM   4767 C CG2 . ILE A 1 628 ? -94.942  -3.452  50.029  1.00 73.60  ? 654  ILE A CG2 1 
ATOM   4768 C CD1 . ILE A 1 628 ? -94.209  -5.632  48.078  1.00 81.46  ? 654  ILE A CD1 1 
ATOM   4769 N N   . PRO A 1 629 ? -95.604  -3.386  53.346  1.00 79.96  ? 655  PRO A N   1 
ATOM   4770 C CA  . PRO A 1 629 ? -96.621  -2.560  53.965  1.00 76.51  ? 655  PRO A CA  1 
ATOM   4771 C C   . PRO A 1 629 ? -97.392  -1.815  52.899  1.00 74.24  ? 655  PRO A C   1 
ATOM   4772 O O   . PRO A 1 629 ? -96.803  -1.319  51.927  1.00 70.63  ? 655  PRO A O   1 
ATOM   4773 C CB  . PRO A 1 629 ? -95.813  -1.613  54.851  1.00 75.16  ? 655  PRO A CB  1 
ATOM   4774 C CG  . PRO A 1 629 ? -94.604  -2.413  55.220  1.00 77.36  ? 655  PRO A CG  1 
ATOM   4775 C CD  . PRO A 1 629 ? -94.296  -3.259  54.014  1.00 82.59  ? 655  PRO A CD  1 
ATOM   4776 N N   . ASN A 1 630 ? -98.706  -1.779  53.055  1.00 78.60  ? 656  ASN A N   1 
ATOM   4777 C CA  . ASN A 1 630 ? -99.564  -1.109  52.087  1.00 83.53  ? 656  ASN A CA  1 
ATOM   4778 C C   . ASN A 1 630 ? -99.153  0.325   51.829  1.00 73.65  ? 656  ASN A C   1 
ATOM   4779 O O   . ASN A 1 630 ? -99.117  0.745   50.677  1.00 86.03  ? 656  ASN A O   1 
ATOM   4780 C CB  . ASN A 1 630 ? -101.057 -1.229  52.475  1.00 78.43  ? 656  ASN A CB  1 
ATOM   4781 C CG  . ASN A 1 630 ? -101.591 -2.660  52.329  1.00 79.64  ? 656  ASN A CG  1 
ATOM   4782 O OD1 . ASN A 1 630 ? -101.163 -3.424  51.456  1.00 77.73  ? 656  ASN A OD1 1 
ATOM   4783 N ND2 . ASN A 1 630 ? -102.561 -3.002  53.145  1.00 86.87  ? 656  ASN A ND2 1 
ATOM   4784 N N   . GLU A 1 631 ? -98.783  1.068   52.868  1.00 72.39  ? 657  GLU A N   1 
ATOM   4785 C CA  . GLU A 1 631 ? -98.377  2.455   52.641  1.00 79.08  ? 657  GLU A CA  1 
ATOM   4786 C C   . GLU A 1 631 ? -96.968  2.490   51.986  1.00 78.74  ? 657  GLU A C   1 
ATOM   4787 O O   . GLU A 1 631 ? -96.560  3.501   51.377  1.00 74.19  ? 657  GLU A O   1 
ATOM   4788 C CB  . GLU A 1 631 ? -98.391  3.284   53.931  1.00 82.00  ? 657  GLU A CB  1 
ATOM   4789 C CG  . GLU A 1 631 ? -98.187  4.778   53.648  1.00 101.99 ? 657  GLU A CG  1 
ATOM   4790 C CD  . GLU A 1 631 ? -97.935  5.625   54.887  1.00 110.99 ? 657  GLU A CD  1 
ATOM   4791 O OE1 . GLU A 1 631 ? -97.773  5.059   55.988  1.00 114.45 ? 657  GLU A OE1 1 
ATOM   4792 O OE2 . GLU A 1 631 ? -97.811  6.863   54.736  1.00 112.20 ? 657  GLU A OE2 1 
ATOM   4793 N N   . ALA A 1 632 ? -96.216  1.404   52.139  1.00 69.82  ? 658  ALA A N   1 
ATOM   4794 C CA  . ALA A 1 632 ? -94.892  1.332   51.556  1.00 79.96  ? 658  ALA A CA  1 
ATOM   4795 C C   . ALA A 1 632 ? -95.060  1.282   50.049  1.00 83.91  ? 658  ALA A C   1 
ATOM   4796 O O   . ALA A 1 632 ? -94.422  2.039   49.305  1.00 86.21  ? 658  ALA A O   1 
ATOM   4797 C CB  . ALA A 1 632 ? -94.156  0.100   52.048  1.00 82.87  ? 658  ALA A CB  1 
ATOM   4798 N N   . PHE A 1 633 ? -95.972  0.421   49.617  1.00 74.97  ? 659  PHE A N   1 
ATOM   4799 C CA  . PHE A 1 633 ? -96.258  0.249   48.204  1.00 76.96  ? 659  PHE A CA  1 
ATOM   4800 C C   . PHE A 1 633 ? -96.862  1.528   47.602  1.00 70.57  ? 659  PHE A C   1 
ATOM   4801 O O   . PHE A 1 633 ? -96.457  1.947   46.537  1.00 77.15  ? 659  PHE A O   1 
ATOM   4802 C CB  . PHE A 1 633 ? -97.206  -0.928  48.012  1.00 66.56  ? 659  PHE A CB  1 
ATOM   4803 C CG  . PHE A 1 633 ? -97.355  -1.357  46.593  1.00 73.29  ? 659  PHE A CG  1 
ATOM   4804 C CD1 . PHE A 1 633 ? -98.224  -0.703  45.741  1.00 83.08  ? 659  PHE A CD1 1 
ATOM   4805 C CD2 . PHE A 1 633 ? -96.705  -2.490  46.137  1.00 79.59  ? 659  PHE A CD2 1 
ATOM   4806 C CE1 . PHE A 1 633 ? -98.399  -1.140  44.440  1.00 82.51  ? 659  PHE A CE1 1 
ATOM   4807 C CE2 . PHE A 1 633 ? -96.861  -2.924  44.832  1.00 77.86  ? 659  PHE A CE2 1 
ATOM   4808 C CZ  . PHE A 1 633 ? -97.709  -2.250  43.985  1.00 84.43  ? 659  PHE A CZ  1 
ATOM   4809 N N   . LEU A 1 634 ? -97.802  2.162   48.298  1.00 68.33  ? 660  LEU A N   1 
ATOM   4810 C CA  . LEU A 1 634 ? -98.428  3.389   47.786  1.00 70.24  ? 660  LEU A CA  1 
ATOM   4811 C C   . LEU A 1 634 ? -97.465  4.513   47.612  1.00 73.55  ? 660  LEU A C   1 
ATOM   4812 O O   . LEU A 1 634 ? -97.751  5.444   46.856  1.00 81.35  ? 660  LEU A O   1 
ATOM   4813 C CB  . LEU A 1 634 ? -99.569  3.887   48.681  1.00 81.83  ? 660  LEU A CB  1 
ATOM   4814 C CG  . LEU A 1 634 ? -100.866 3.087   48.751  1.00 79.44  ? 660  LEU A CG  1 
ATOM   4815 C CD1 . LEU A 1 634 ? -101.812 3.725   49.750  1.00 79.16  ? 660  LEU A CD1 1 
ATOM   4816 C CD2 . LEU A 1 634 ? -101.505 3.044   47.385  1.00 76.28  ? 660  LEU A CD2 1 
ATOM   4817 N N   . ASN A 1 635 ? -96.369  4.492   48.370  1.00 75.08  ? 661  ASN A N   1 
ATOM   4818 C CA  . ASN A 1 635 ? -95.367  5.551   48.260  1.00 68.48  ? 661  ASN A CA  1 
ATOM   4819 C C   . ASN A 1 635 ? -94.325  5.359   47.152  1.00 66.67  ? 661  ASN A C   1 
ATOM   4820 O O   . ASN A 1 635 ? -93.463  6.221   46.963  1.00 63.91  ? 661  ASN A O   1 
ATOM   4821 C CB  . ASN A 1 635 ? -94.743  5.879   49.617  1.00 82.88  ? 661  ASN A CB  1 
ATOM   4822 C CG  . ASN A 1 635 ? -95.671  6.703   50.501  1.00 81.35  ? 661  ASN A CG  1 
ATOM   4823 O OD1 . ASN A 1 635 ? -96.490  7.473   50.001  1.00 88.43  ? 661  ASN A OD1 1 
ATOM   4824 N ND2 . ASN A 1 635 ? -95.430  6.673   51.798  1.00 79.35  ? 661  ASN A ND2 1 
ATOM   4825 N N   . LEU A 1 636 ? -94.418  4.247   46.409  1.00 65.83  ? 662  LEU A N   1 
ATOM   4826 C CA  . LEU A 1 636 ? -93.509  4.007   45.288  1.00 63.88  ? 662  LEU A CA  1 
ATOM   4827 C C   . LEU A 1 636 ? -93.947  5.056   44.282  1.00 65.33  ? 662  LEU A C   1 
ATOM   4828 O O   . LEU A 1 636 ? -95.123  5.380   44.225  1.00 76.40  ? 662  LEU A O   1 
ATOM   4829 C CB  . LEU A 1 636 ? -93.690  2.608   44.690  1.00 59.92  ? 662  LEU A CB  1 
ATOM   4830 C CG  . LEU A 1 636 ? -93.459  1.415   45.622  1.00 61.23  ? 662  LEU A CG  1 
ATOM   4831 C CD1 . LEU A 1 636 ? -93.741  0.093   44.923  1.00 55.22  ? 662  LEU A CD1 1 
ATOM   4832 C CD2 . LEU A 1 636 ? -92.039  1.428   46.170  1.00 70.99  ? 662  LEU A CD2 1 
ATOM   4833 N N   . PRO A 1 637 ? -93.021  5.579   43.477  1.00 72.97  ? 663  PRO A N   1 
ATOM   4834 C CA  . PRO A 1 637 ? -93.392  6.621   42.514  1.00 70.18  ? 663  PRO A CA  1 
ATOM   4835 C C   . PRO A 1 637 ? -94.547  6.261   41.583  1.00 74.09  ? 663  PRO A C   1 
ATOM   4836 O O   . PRO A 1 637 ? -94.536  5.209   40.931  1.00 74.96  ? 663  PRO A O   1 
ATOM   4837 C CB  . PRO A 1 637 ? -92.106  6.841   41.711  1.00 69.52  ? 663  PRO A CB  1 
ATOM   4838 C CG  . PRO A 1 637 ? -91.027  6.174   42.490  1.00 72.16  ? 663  PRO A CG  1 
ATOM   4839 C CD  . PRO A 1 637 ? -91.690  5.031   43.188  1.00 69.35  ? 663  PRO A CD  1 
ATOM   4840 N N   . ALA A 1 638 ? -95.523  7.161   41.505  1.00 83.57  ? 664  ALA A N   1 
ATOM   4841 C CA  . ALA A 1 638 ? -96.702  6.969   40.659  1.00 84.83  ? 664  ALA A CA  1 
ATOM   4842 C C   . ALA A 1 638 ? -96.302  6.950   39.181  1.00 90.33  ? 664  ALA A C   1 
ATOM   4843 O O   . ALA A 1 638 ? -97.025  6.395   38.323  1.00 93.43  ? 664  ALA A O   1 
ATOM   4844 C CB  . ALA A 1 638 ? -97.709  8.066   40.927  1.00 73.77  ? 664  ALA A CB  1 
ATOM   4845 N N   . SER A 1 639 ? -95.126  7.522   38.904  1.00 74.19  ? 665  SER A N   1 
ATOM   4846 C CA  . SER A 1 639 ? -94.583  7.582   37.553  1.00 64.22  ? 665  SER A CA  1 
ATOM   4847 C C   . SER A 1 639 ? -94.106  6.244   37.015  1.00 64.83  ? 665  SER A C   1 
ATOM   4848 O O   . SER A 1 639 ? -93.777  6.143   35.830  1.00 68.90  ? 665  SER A O   1 
ATOM   4849 C CB  . SER A 1 639 ? -93.441  8.603   37.479  1.00 66.35  ? 665  SER A CB  1 
ATOM   4850 O OG  . SER A 1 639 ? -92.426  8.354   38.443  1.00 77.15  ? 665  SER A OG  1 
ATOM   4851 N N   . LEU A 1 640 ? -94.094  5.207   37.848  1.00 63.06  ? 666  LEU A N   1 
ATOM   4852 C CA  . LEU A 1 640 ? -93.625  3.901   37.378  1.00 71.85  ? 666  LEU A CA  1 
ATOM   4853 C C   . LEU A 1 640 ? -94.389  3.321   36.203  1.00 71.91  ? 666  LEU A C   1 
ATOM   4854 O O   . LEU A 1 640 ? -95.614  3.379   36.145  1.00 81.66  ? 666  LEU A O   1 
ATOM   4855 C CB  . LEU A 1 640 ? -93.624  2.850   38.498  1.00 72.73  ? 666  LEU A CB  1 
ATOM   4856 C CG  . LEU A 1 640 ? -92.644  3.038   39.658  1.00 78.60  ? 666  LEU A CG  1 
ATOM   4857 C CD1 . LEU A 1 640 ? -92.760  1.846   40.590  1.00 81.34  ? 666  LEU A CD1 1 
ATOM   4858 C CD2 . LEU A 1 640 ? -91.212  3.171   39.159  1.00 79.73  ? 666  LEU A CD2 1 
ATOM   4859 N N   . THR A 1 641 ? -93.630  2.721   35.296  1.00 71.66  ? 667  THR A N   1 
ATOM   4860 C CA  . THR A 1 641 ? -94.166  2.061   34.125  1.00 68.16  ? 667  THR A CA  1 
ATOM   4861 C C   . THR A 1 641 ? -93.736  0.601   34.196  1.00 62.91  ? 667  THR A C   1 
ATOM   4862 O O   . THR A 1 641 ? -94.316  -0.251  33.554  1.00 74.78  ? 667  THR A O   1 
ATOM   4863 C CB  . THR A 1 641 ? -93.593  2.633   32.814  1.00 67.87  ? 667  THR A CB  1 
ATOM   4864 O OG1 . THR A 1 641 ? -92.252  2.174   32.627  1.00 84.78  ? 667  THR A OG1 1 
ATOM   4865 C CG2 . THR A 1 641 ? -93.636  4.164   32.823  1.00 71.83  ? 667  THR A CG2 1 
ATOM   4866 N N   . GLU A 1 642 ? -92.703  0.317   34.975  1.00 65.56  ? 668  GLU A N   1 
ATOM   4867 C CA  . GLU A 1 642 ? -92.201  -1.037  35.099  1.00 64.29  ? 668  GLU A CA  1 
ATOM   4868 C C   . GLU A 1 642 ? -91.758  -1.316  36.543  1.00 62.50  ? 668  GLU A C   1 
ATOM   4869 O O   . GLU A 1 642 ? -91.060  -0.520  37.151  1.00 67.70  ? 668  GLU A O   1 
ATOM   4870 C CB  . GLU A 1 642 ? -91.073  -1.198  34.119  1.00 62.39  ? 668  GLU A CB  1 
ATOM   4871 C CG  . GLU A 1 642 ? -90.447  -2.565  34.123  1.00 79.99  ? 668  GLU A CG  1 
ATOM   4872 C CD  . GLU A 1 642 ? -89.393  -2.686  33.048  1.00 81.45  ? 668  GLU A CD  1 
ATOM   4873 O OE1 . GLU A 1 642 ? -89.284  -1.739  32.224  1.00 67.76  ? 668  GLU A OE1 1 
ATOM   4874 O OE2 . GLU A 1 642 ? -88.706  -3.732  33.008  1.00 89.10  ? 668  GLU A OE2 1 
ATOM   4875 N N   . LEU A 1 643 ? -92.266  -2.387  37.124  1.00 66.50  ? 669  LEU A N   1 
ATOM   4876 C CA  . LEU A 1 643 ? -91.931  -2.744  38.484  1.00 59.00  ? 669  LEU A CA  1 
ATOM   4877 C C   . LEU A 1 643 ? -91.637  -4.205  38.616  1.00 64.40  ? 669  LEU A C   1 
ATOM   4878 O O   . LEU A 1 643 ? -92.463  -5.014  38.303  1.00 61.25  ? 669  LEU A O   1 
ATOM   4879 C CB  . LEU A 1 643 ? -93.082  -2.402  39.396  1.00 57.24  ? 669  LEU A CB  1 
ATOM   4880 C CG  . LEU A 1 643 ? -92.958  -2.812  40.844  1.00 65.12  ? 669  LEU A CG  1 
ATOM   4881 C CD1 . LEU A 1 643 ? -91.680  -2.280  41.425  1.00 71.16  ? 669  LEU A CD1 1 
ATOM   4882 C CD2 . LEU A 1 643 ? -94.111  -2.239  41.614  1.00 68.17  ? 669  LEU A CD2 1 
ATOM   4883 N N   . HIS A 1 644 ? -90.479  -4.535  39.158  1.00 63.22  ? 670  HIS A N   1 
ATOM   4884 C CA  . HIS A 1 644 ? -90.108  -5.904  39.358  1.00 61.44  ? 670  HIS A CA  1 
ATOM   4885 C C   . HIS A 1 644 ? -90.019  -6.171  40.806  1.00 59.34  ? 670  HIS A C   1 
ATOM   4886 O O   . HIS A 1 644 ? -89.433  -5.408  41.546  1.00 58.24  ? 670  HIS A O   1 
ATOM   4887 C CB  . HIS A 1 644 ? -88.764  -6.179  38.744  1.00 63.46  ? 670  HIS A CB  1 
ATOM   4888 C CG  . HIS A 1 644 ? -88.731  -6.046  37.256  1.00 67.65  ? 670  HIS A CG  1 
ATOM   4889 N ND1 . HIS A 1 644 ? -88.686  -7.093  36.453  1.00 71.57  ? 670  HIS A ND1 1 
ATOM   4890 C CD2 . HIS A 1 644 ? -88.710  -4.941  36.448  1.00 64.51  ? 670  HIS A CD2 1 
ATOM   4891 C CE1 . HIS A 1 644 ? -88.655  -6.688  35.192  1.00 68.46  ? 670  HIS A CE1 1 
ATOM   4892 N NE2 . HIS A 1 644 ? -88.671  -5.368  35.190  1.00 60.04  ? 670  HIS A NE2 1 
ATOM   4893 N N   . ILE A 1 645 ? -90.654  -7.233  41.242  1.00 59.56  ? 671  ILE A N   1 
ATOM   4894 C CA  . ILE A 1 645 ? -90.581  -7.657  42.608  1.00 52.78  ? 671  ILE A CA  1 
ATOM   4895 C C   . ILE A 1 645 ? -90.332  -9.132  42.662  1.00 50.64  ? 671  ILE A C   1 
ATOM   4896 O O   . ILE A 1 645 ? -90.706  -9.772  43.603  1.00 59.78  ? 671  ILE A O   1 
ATOM   4897 C CB  . ILE A 1 645 ? -91.868  -7.348  43.352  1.00 55.83  ? 671  ILE A CB  1 
ATOM   4898 C CG1 . ILE A 1 645 ? -92.264  -5.911  43.141  1.00 69.59  ? 671  ILE A CG1 1 
ATOM   4899 C CG2 . ILE A 1 645 ? -91.681  -7.566  44.822  1.00 65.74  ? 671  ILE A CG2 1 
ATOM   4900 C CD1 . ILE A 1 645 ? -93.572  -5.574  43.792  1.00 69.03  ? 671  ILE A CD1 1 
ATOM   4901 N N   . ASN A 1 646 ? -89.720  -9.679  41.638  1.00 43.89  ? 672  ASN A N   1 
ATOM   4902 C CA  . ASN A 1 646 ? -89.580  -11.107 41.548  1.00 48.33  ? 672  ASN A CA  1 
ATOM   4903 C C   . ASN A 1 646 ? -88.627  -11.648 42.555  1.00 56.75  ? 672  ASN A C   1 
ATOM   4904 O O   . ASN A 1 646 ? -87.875  -10.932 43.145  1.00 56.38  ? 672  ASN A O   1 
ATOM   4905 C CB  . ASN A 1 646 ? -89.124  -11.523 40.178  1.00 52.34  ? 672  ASN A CB  1 
ATOM   4906 C CG  . ASN A 1 646 ? -87.986  -10.712 39.683  1.00 44.81  ? 672  ASN A CG  1 
ATOM   4907 O OD1 . ASN A 1 646 ? -88.062  -9.521  39.640  1.00 58.43  ? 672  ASN A OD1 1 
ATOM   4908 N ND2 . ASN A 1 646 ? -86.936  -11.359 39.291  1.00 53.20  ? 672  ASN A ND2 1 
ATOM   4909 N N   . ASP A 1 647 ? -88.716  -12.935 42.787  1.00 60.92  ? 673  ASP A N   1 
ATOM   4910 C CA  . ASP A 1 647 ? -87.751  -13.617 43.591  1.00 60.99  ? 673  ASP A CA  1 
ATOM   4911 C C   . ASP A 1 647 ? -87.645  -13.072 44.973  1.00 67.28  ? 673  ASP A C   1 
ATOM   4912 O O   . ASP A 1 647 ? -86.583  -12.882 45.495  1.00 69.08  ? 673  ASP A O   1 
ATOM   4913 C CB  . ASP A 1 647 ? -86.432  -13.620 42.890  1.00 67.03  ? 673  ASP A CB  1 
ATOM   4914 C CG  . ASP A 1 647 ? -86.412  -14.591 41.777  1.00 73.00  ? 673  ASP A CG  1 
ATOM   4915 O OD1 . ASP A 1 647 ? -87.098  -15.601 41.874  1.00 74.16  ? 673  ASP A OD1 1 
ATOM   4916 O OD2 . ASP A 1 647 ? -85.726  -14.361 40.791  1.00 95.64  ? 673  ASP A OD2 1 
ATOM   4917 N N   . ASN A 1 648 ? -88.792  -12.813 45.551  1.00 65.22  ? 674  ASN A N   1 
ATOM   4918 C CA  . ASN A 1 648 ? -88.914  -12.526 46.933  1.00 56.89  ? 674  ASN A CA  1 
ATOM   4919 C C   . ASN A 1 648 ? -89.640  -13.694 47.518  1.00 59.19  ? 674  ASN A C   1 
ATOM   4920 O O   . ASN A 1 648 ? -89.504  -14.782 47.023  1.00 65.45  ? 674  ASN A O   1 
ATOM   4921 C CB  . ASN A 1 648 ? -89.695  -11.267 47.107  1.00 59.38  ? 674  ASN A CB  1 
ATOM   4922 C CG  . ASN A 1 648 ? -88.830  -10.057 47.032  1.00 67.60  ? 674  ASN A CG  1 
ATOM   4923 O OD1 . ASN A 1 648 ? -88.107  -9.757  47.943  1.00 70.85  ? 674  ASN A OD1 1 
ATOM   4924 N ND2 . ASN A 1 648 ? -88.899  -9.368  45.944  1.00 71.50  ? 674  ASN A ND2 1 
ATOM   4925 N N   . MET A 1 649 ? -90.356  -13.493 48.606  1.00 63.85  ? 675  MET A N   1 
ATOM   4926 C CA  . MET A 1 649 ? -91.171  -14.553 49.173  1.00 70.67  ? 675  MET A CA  1 
ATOM   4927 C C   . MET A 1 649 ? -92.576  -14.125 49.544  1.00 58.25  ? 675  MET A C   1 
ATOM   4928 O O   . MET A 1 649 ? -93.080  -14.501 50.560  1.00 65.83  ? 675  MET A O   1 
ATOM   4929 C CB  . MET A 1 649 ? -90.471  -15.175 50.363  1.00 74.28  ? 675  MET A CB  1 
ATOM   4930 C CG  . MET A 1 649 ? -88.977  -15.231 50.201  1.00 85.63  ? 675  MET A CG  1 
ATOM   4931 S SD  . MET A 1 649 ? -88.156  -15.182 51.783  1.00 99.00  ? 675  MET A SD  1 
ATOM   4932 C CE  . MET A 1 649 ? -88.015  -16.930 52.079  1.00 110.53 ? 675  MET A CE  1 
ATOM   4933 N N   . LEU A 1 650 ? -93.195  -13.311 48.726  1.00 54.91  ? 676  LEU A N   1 
ATOM   4934 C CA  . LEU A 1 650 ? -94.521  -12.758 49.015  1.00 65.13  ? 676  LEU A CA  1 
ATOM   4935 C C   . LEU A 1 650 ? -95.615  -13.797 48.855  1.00 67.70  ? 676  LEU A C   1 
ATOM   4936 O O   . LEU A 1 650 ? -95.549  -14.620 47.941  1.00 59.16  ? 676  LEU A O   1 
ATOM   4937 C CB  . LEU A 1 650 ? -94.833  -11.620 48.052  1.00 67.06  ? 676  LEU A CB  1 
ATOM   4938 C CG  . LEU A 1 650 ? -93.885  -10.435 48.056  1.00 67.01  ? 676  LEU A CG  1 
ATOM   4939 C CD1 . LEU A 1 650 ? -94.284  -9.467  46.963  1.00 65.42  ? 676  LEU A CD1 1 
ATOM   4940 C CD2 . LEU A 1 650 ? -93.916  -9.760  49.413  1.00 70.22  ? 676  LEU A CD2 1 
ATOM   4941 N N   . LYS A 1 651 ? -96.592  -13.769 49.766  1.00 66.38  ? 677  LYS A N   1 
ATOM   4942 C CA  . LYS A 1 651 ? -97.748  -14.682 49.730  1.00 70.39  ? 677  LYS A CA  1 
ATOM   4943 C C   . LYS A 1 651 ? -99.046  -13.974 49.359  1.00 66.25  ? 677  LYS A C   1 
ATOM   4944 O O   . LYS A 1 651 ? -99.982  -14.600 48.870  1.00 74.22  ? 677  LYS A O   1 
ATOM   4945 C CB  . LYS A 1 651 ? -97.920  -15.439 51.039  1.00 68.19  ? 677  LYS A CB  1 
ATOM   4946 C CG  . LYS A 1 651 ? -96.964  -16.605 51.199  1.00 69.37  ? 677  LYS A CG  1 
ATOM   4947 C CD  . LYS A 1 651 ? -97.189  -17.278 52.537  1.00 70.24  ? 677  LYS A CD  1 
ATOM   4948 C CE  . LYS A 1 651 ? -96.277  -18.475 52.739  1.00 73.26  ? 677  LYS A CE  1 
ATOM   4949 N NZ  . LYS A 1 651 ? -96.395  -18.955 54.147  1.00 80.25  ? 677  LYS A NZ  1 
ATOM   4950 N N   . PHE A 1 652 ? -99.101  -12.675 49.597  1.00 65.06  ? 678  PHE A N   1 
ATOM   4951 C CA  . PHE A 1 652 ? -100.273 -11.904 49.270  1.00 75.38  ? 678  PHE A CA  1 
ATOM   4952 C C   . PHE A 1 652 ? -99.795  -10.628 48.592  1.00 73.03  ? 678  PHE A C   1 
ATOM   4953 O O   . PHE A 1 652 ? -98.637  -10.258 48.714  1.00 77.04  ? 678  PHE A O   1 
ATOM   4954 C CB  . PHE A 1 652 ? -101.121 -11.604 50.529  1.00 75.37  ? 678  PHE A CB  1 
ATOM   4955 C CG  . PHE A 1 652 ? -101.480 -12.845 51.329  1.00 99.50  ? 678  PHE A CG  1 
ATOM   4956 C CD1 . PHE A 1 652 ? -102.504 -13.698 50.919  1.00 108.52 ? 678  PHE A CD1 1 
ATOM   4957 C CD2 . PHE A 1 652 ? -100.808 -13.149 52.515  1.00 127.96 ? 678  PHE A CD2 1 
ATOM   4958 C CE1 . PHE A 1 652 ? -102.817 -14.850 51.642  1.00 117.48 ? 678  PHE A CE1 1 
ATOM   4959 C CE2 . PHE A 1 652 ? -101.132 -14.288 53.253  1.00 132.10 ? 678  PHE A CE2 1 
ATOM   4960 C CZ  . PHE A 1 652 ? -102.135 -15.140 52.813  1.00 125.63 ? 678  PHE A CZ  1 
ATOM   4961 N N   . PHE A 1 653 ? -100.652 -10.046 47.766  1.00 76.23  ? 679  PHE A N   1 
ATOM   4962 C CA  . PHE A 1 653 ? -100.340 -8.815  47.062  1.00 70.40  ? 679  PHE A CA  1 
ATOM   4963 C C   . PHE A 1 653 ? -101.657 -8.046  46.966  1.00 68.54  ? 679  PHE A C   1 
ATOM   4964 O O   . PHE A 1 653 ? -102.629 -8.556  46.429  1.00 82.76  ? 679  PHE A O   1 
ATOM   4965 C CB  . PHE A 1 653 ? -99.724  -9.116  45.684  1.00 72.94  ? 679  PHE A CB  1 
ATOM   4966 C CG  . PHE A 1 653 ? -99.366  -7.881  44.901  1.00 78.30  ? 679  PHE A CG  1 
ATOM   4967 C CD1 . PHE A 1 653 ? -98.179  -7.224  45.131  1.00 77.37  ? 679  PHE A CD1 1 
ATOM   4968 C CD2 . PHE A 1 653 ? -100.216 -7.382  43.931  1.00 85.79  ? 679  PHE A CD2 1 
ATOM   4969 C CE1 . PHE A 1 653 ? -97.859  -6.058  44.447  1.00 78.68  ? 679  PHE A CE1 1 
ATOM   4970 C CE2 . PHE A 1 653 ? -99.892  -6.230  43.224  1.00 86.50  ? 679  PHE A CE2 1 
ATOM   4971 C CZ  . PHE A 1 653 ? -98.710  -5.567  43.481  1.00 79.41  ? 679  PHE A CZ  1 
ATOM   4972 N N   . ASN A 1 654 ? -101.710 -6.867  47.579  1.00 73.48  ? 680  ASN A N   1 
ATOM   4973 C CA  . ASN A 1 654 ? -102.923 -6.054  47.593  1.00 68.21  ? 680  ASN A CA  1 
ATOM   4974 C C   . ASN A 1 654 ? -103.071 -5.350  46.245  1.00 66.17  ? 680  ASN A C   1 
ATOM   4975 O O   . ASN A 1 654 ? -102.688 -4.197  46.076  1.00 71.58  ? 680  ASN A O   1 
ATOM   4976 C CB  . ASN A 1 654 ? -102.922 -5.088  48.813  1.00 71.04  ? 680  ASN A CB  1 
ATOM   4977 C CG  . ASN A 1 654 ? -104.260 -4.342  49.015  1.00 85.81  ? 680  ASN A CG  1 
ATOM   4978 O OD1 . ASN A 1 654 ? -104.954 -4.040  48.054  1.00 91.77  ? 680  ASN A OD1 1 
ATOM   4979 N ND2 . ASN A 1 654 ? -104.572 -3.963  50.279  1.00 78.80  ? 680  ASN A ND2 1 
ATOM   4980 N N   . TRP A 1 655 ? -103.669 -6.074  45.299  1.00 65.33  ? 681  TRP A N   1 
ATOM   4981 C CA  . TRP A 1 655 ? -103.914 -5.586  43.927  1.00 73.10  ? 681  TRP A CA  1 
ATOM   4982 C C   . TRP A 1 655 ? -104.581 -4.222  43.832  1.00 69.12  ? 681  TRP A C   1 
ATOM   4983 O O   . TRP A 1 655 ? -104.378 -3.479  42.888  1.00 72.57  ? 681  TRP A O   1 
ATOM   4984 C CB  . TRP A 1 655 ? -104.787 -6.575  43.218  1.00 63.76  ? 681  TRP A CB  1 
ATOM   4985 C CG  . TRP A 1 655 ? -104.179 -7.862  43.120  1.00 59.69  ? 681  TRP A CG  1 
ATOM   4986 C CD1 . TRP A 1 655 ? -104.323 -8.908  43.978  1.00 60.90  ? 681  TRP A CD1 1 
ATOM   4987 C CD2 . TRP A 1 655 ? -103.245 -8.271  42.123  1.00 55.50  ? 681  TRP A CD2 1 
ATOM   4988 N NE1 . TRP A 1 655 ? -103.562 -9.989  43.539  1.00 67.36  ? 681  TRP A NE1 1 
ATOM   4989 C CE2 . TRP A 1 655 ? -102.891 -9.615  42.403  1.00 58.62  ? 681  TRP A CE2 1 
ATOM   4990 C CE3 . TRP A 1 655 ? -102.666 -7.632  41.024  1.00 57.19  ? 681  TRP A CE3 1 
ATOM   4991 C CZ2 . TRP A 1 655 ? -101.997 -10.325 41.624  1.00 62.15  ? 681  TRP A CZ2 1 
ATOM   4992 C CZ3 . TRP A 1 655 ? -101.787 -8.344  40.233  1.00 61.45  ? 681  TRP A CZ3 1 
ATOM   4993 C CH2 . TRP A 1 655 ? -101.462 -9.683  40.535  1.00 66.69  ? 681  TRP A CH2 1 
ATOM   4994 N N   . THR A 1 656 ? -105.449 -3.955  44.780  1.00 68.37  ? 682  THR A N   1 
ATOM   4995 C CA  . THR A 1 656 ? -106.157 -2.707  44.856  1.00 75.27  ? 682  THR A CA  1 
ATOM   4996 C C   . THR A 1 656 ? -105.189 -1.540  44.789  1.00 87.39  ? 682  THR A C   1 
ATOM   4997 O O   . THR A 1 656 ? -105.517 -0.452  44.296  1.00 84.72  ? 682  THR A O   1 
ATOM   4998 C CB  . THR A 1 656 ? -106.886 -2.629  46.208  1.00 78.00  ? 682  THR A CB  1 
ATOM   4999 O OG1 . THR A 1 656 ? -107.651 -3.830  46.404  1.00 76.24  ? 682  THR A OG1 1 
ATOM   5000 C CG2 . THR A 1 656 ? -107.771 -1.381  46.300  1.00 78.09  ? 682  THR A CG2 1 
ATOM   5001 N N   . LEU A 1 657 ? -103.988 -1.767  45.301  1.00 93.38  ? 683  LEU A N   1 
ATOM   5002 C CA  . LEU A 1 657 ? -102.976 -0.734  45.325  1.00 86.79  ? 683  LEU A CA  1 
ATOM   5003 C C   . LEU A 1 657 ? -102.587 -0.306  43.927  1.00 80.17  ? 683  LEU A C   1 
ATOM   5004 O O   . LEU A 1 657 ? -102.178 0.836   43.733  1.00 78.86  ? 683  LEU A O   1 
ATOM   5005 C CB  . LEU A 1 657 ? -101.777 -1.205  46.135  1.00 97.78  ? 683  LEU A CB  1 
ATOM   5006 C CG  . LEU A 1 657 ? -102.178 -1.526  47.583  1.00 91.57  ? 683  LEU A CG  1 
ATOM   5007 C CD1 . LEU A 1 657 ? -101.044 -2.153  48.373  1.00 92.00  ? 683  LEU A CD1 1 
ATOM   5008 C CD2 . LEU A 1 657 ? -102.685 -0.269  48.267  1.00 94.26  ? 683  LEU A CD2 1 
ATOM   5009 N N   . LEU A 1 658 ? -102.804 -1.174  42.935  1.00 70.22  ? 684  LEU A N   1 
ATOM   5010 C CA  . LEU A 1 658 ? -102.472 -0.818  41.555  1.00 74.80  ? 684  LEU A CA  1 
ATOM   5011 C C   . LEU A 1 658 ? -103.214 0.424   41.091  1.00 74.30  ? 684  LEU A C   1 
ATOM   5012 O O   . LEU A 1 658 ? -102.797 1.072   40.148  1.00 75.74  ? 684  LEU A O   1 
ATOM   5013 C CB  . LEU A 1 658 ? -102.713 -1.974  40.592  1.00 70.79  ? 684  LEU A CB  1 
ATOM   5014 C CG  . LEU A 1 658 ? -101.828 -3.200  40.867  1.00 81.16  ? 684  LEU A CG  1 
ATOM   5015 C CD1 . LEU A 1 658 ? -102.026 -4.273  39.806  1.00 76.76  ? 684  LEU A CD1 1 
ATOM   5016 C CD2 . LEU A 1 658 ? -100.355 -2.815  40.924  1.00 84.89  ? 684  LEU A CD2 1 
ATOM   5017 N N   . GLN A 1 659 ? -104.284 0.784   41.787  1.00 91.09  ? 685  GLN A N   1 
ATOM   5018 C CA  . GLN A 1 659 ? -105.055 1.967   41.425  1.00 97.90  ? 685  GLN A CA  1 
ATOM   5019 C C   . GLN A 1 659 ? -104.269 3.247   41.395  1.00 95.30  ? 685  GLN A C   1 
ATOM   5020 O O   . GLN A 1 659 ? -104.647 4.164   40.687  1.00 101.32 ? 685  GLN A O   1 
ATOM   5021 C CB  . GLN A 1 659 ? -106.209 2.181   42.385  1.00 104.99 ? 685  GLN A CB  1 
ATOM   5022 C CG  . GLN A 1 659 ? -107.294 1.140   42.292  1.00 119.60 ? 685  GLN A CG  1 
ATOM   5023 C CD  . GLN A 1 659 ? -108.414 1.405   43.270  1.00 122.29 ? 685  GLN A CD  1 
ATOM   5024 O OE1 . GLN A 1 659 ? -108.311 2.278   44.132  1.00 118.04 ? 685  GLN A OE1 1 
ATOM   5025 N NE2 . GLN A 1 659 ? -109.489 0.646   43.150  1.00 138.25 ? 685  GLN A NE2 1 
ATOM   5026 N N   . GLN A 1 660 ? -103.199 3.339   42.180  1.00 99.49  ? 686  GLN A N   1 
ATOM   5027 C CA  . GLN A 1 660 ? -102.413 4.574   42.218  1.00 96.51  ? 686  GLN A CA  1 
ATOM   5028 C C   . GLN A 1 660 ? -101.311 4.633   41.166  1.00 84.29  ? 686  GLN A C   1 
ATOM   5029 O O   . GLN A 1 660 ? -100.625 5.637   41.065  1.00 85.46  ? 686  GLN A O   1 
ATOM   5030 C CB  . GLN A 1 660 ? -101.817 4.793   43.611  1.00 102.50 ? 686  GLN A CB  1 
ATOM   5031 C CG  . GLN A 1 660 ? -102.849 4.752   44.740  1.00 122.33 ? 686  GLN A CG  1 
ATOM   5032 C CD  . GLN A 1 660 ? -103.984 5.771   44.610  1.00 123.36 ? 686  GLN A CD  1 
ATOM   5033 O OE1 . GLN A 1 660 ? -103.933 6.688   43.796  1.00 120.34 ? 686  GLN A OE1 1 
ATOM   5034 N NE2 . GLN A 1 660 ? -105.000 5.627   45.458  1.00 123.61 ? 686  GLN A NE2 1 
ATOM   5035 N N   . PHE A 1 661 ? -101.213 3.602   40.327  1.00 79.68  ? 687  PHE A N   1 
ATOM   5036 C CA  . PHE A 1 661 ? -100.184 3.535   39.286  1.00 84.58  ? 687  PHE A CA  1 
ATOM   5037 C C   . PHE A 1 661 ? -100.761 3.541   37.865  1.00 83.02  ? 687  PHE A C   1 
ATOM   5038 O O   . PHE A 1 661 ? -100.682 2.551   37.144  1.00 67.61  ? 687  PHE A O   1 
ATOM   5039 C CB  . PHE A 1 661 ? -99.284  2.330   39.552  1.00 79.55  ? 687  PHE A CB  1 
ATOM   5040 C CG  . PHE A 1 661 ? -98.559  2.440   40.848  1.00 78.44  ? 687  PHE A CG  1 
ATOM   5041 C CD1 . PHE A 1 661 ? -99.090  1.891   41.997  1.00 84.93  ? 687  PHE A CD1 1 
ATOM   5042 C CD2 . PHE A 1 661 ? -97.457  3.268   40.955  1.00 81.72  ? 687  PHE A CD2 1 
ATOM   5043 C CE1 . PHE A 1 661 ? -98.478  2.087   43.218  1.00 86.33  ? 687  PHE A CE1 1 
ATOM   5044 C CE2 . PHE A 1 661 ? -96.832  3.458   42.168  1.00 88.15  ? 687  PHE A CE2 1 
ATOM   5045 C CZ  . PHE A 1 661 ? -97.347  2.874   43.303  1.00 84.93  ? 687  PHE A CZ  1 
ATOM   5046 N N   . PRO A 1 662 ? -101.244 4.714   37.433  1.00 82.23  ? 688  PRO A N   1 
ATOM   5047 C CA  . PRO A 1 662 ? -101.870 4.943   36.132  1.00 78.23  ? 688  PRO A CA  1 
ATOM   5048 C C   . PRO A 1 662 ? -101.012 4.624   34.920  1.00 86.93  ? 688  PRO A C   1 
ATOM   5049 O O   . PRO A 1 662 ? -101.559 4.248   33.888  1.00 87.62  ? 688  PRO A O   1 
ATOM   5050 C CB  . PRO A 1 662 ? -102.202 6.431   36.156  1.00 82.91  ? 688  PRO A CB  1 
ATOM   5051 C CG  . PRO A 1 662 ? -101.291 7.031   37.169  1.00 84.66  ? 688  PRO A CG  1 
ATOM   5052 C CD  . PRO A 1 662 ? -101.009 5.969   38.174  1.00 79.91  ? 688  PRO A CD  1 
ATOM   5053 N N   . ARG A 1 663 ? -99.692  4.792   35.024  1.00 86.25  ? 689  ARG A N   1 
ATOM   5054 C CA  . ARG A 1 663 ? -98.791  4.505   33.885  1.00 74.61  ? 689  ARG A CA  1 
ATOM   5055 C C   . ARG A 1 663 ? -98.093  3.142   33.945  1.00 67.39  ? 689  ARG A C   1 
ATOM   5056 O O   . ARG A 1 663 ? -97.416  2.760   33.003  1.00 58.03  ? 689  ARG A O   1 
ATOM   5057 C CB  . ARG A 1 663 ? -97.809  5.674   33.643  1.00 69.52  ? 689  ARG A CB  1 
ATOM   5058 C CG  . ARG A 1 663 ? -98.565  6.906   33.149  1.00 84.49  ? 689  ARG A CG  1 
ATOM   5059 C CD  . ARG A 1 663 ? -97.755  8.163   32.897  1.00 84.96  ? 689  ARG A CD  1 
ATOM   5060 N NE  . ARG A 1 663 ? -97.231  8.781   34.116  1.00 103.38 ? 689  ARG A NE  1 
ATOM   5061 C CZ  . ARG A 1 663 ? -96.616  9.971   34.151  1.00 106.72 ? 689  ARG A CZ  1 
ATOM   5062 N NH1 . ARG A 1 663 ? -96.512  10.707  33.048  1.00 100.27 ? 689  ARG A NH1 1 
ATOM   5063 N NH2 . ARG A 1 663 ? -96.162  10.463  35.300  1.00 99.83  ? 689  ARG A NH2 1 
ATOM   5064 N N   . LEU A 1 664 ? -98.443  2.327   34.935  1.00 65.89  ? 690  LEU A N   1 
ATOM   5065 C CA  . LEU A 1 664 ? -97.817  1.020   35.092  1.00 65.08  ? 690  LEU A CA  1 
ATOM   5066 C C   . LEU A 1 664 ? -98.143  0.003   34.003  1.00 63.65  ? 690  LEU A C   1 
ATOM   5067 O O   . LEU A 1 664 ? -99.203  -0.608  34.013  1.00 78.52  ? 690  LEU A O   1 
ATOM   5068 C CB  . LEU A 1 664 ? -98.177  0.430   36.458  1.00 68.19  ? 690  LEU A CB  1 
ATOM   5069 C CG  . LEU A 1 664 ? -97.575  -0.949  36.758  1.00 75.82  ? 690  LEU A CG  1 
ATOM   5070 C CD1 . LEU A 1 664 ? -96.051  -0.890  36.706  1.00 84.03  ? 690  LEU A CD1 1 
ATOM   5071 C CD2 . LEU A 1 664 ? -98.044  -1.471  38.113  1.00 74.87  ? 690  LEU A CD2 1 
ATOM   5072 N N   . GLU A 1 665 ? -97.176  -0.270  33.142  1.00 70.43  ? 691  GLU A N   1 
ATOM   5073 C CA  . GLU A 1 665 ? -97.352  -1.249  32.065  1.00 77.88  ? 691  GLU A CA  1 
ATOM   5074 C C   . GLU A 1 665 ? -96.863  -2.659  32.403  1.00 76.57  ? 691  GLU A C   1 
ATOM   5075 O O   . GLU A 1 665 ? -97.446  -3.637  31.946  1.00 77.22  ? 691  GLU A O   1 
ATOM   5076 C CB  . GLU A 1 665 ? -96.609  -0.806  30.811  1.00 75.02  ? 691  GLU A CB  1 
ATOM   5077 C CG  . GLU A 1 665 ? -97.024  0.559   30.302  1.00 84.57  ? 691  GLU A CG  1 
ATOM   5078 C CD  . GLU A 1 665 ? -96.363  0.908   28.983  1.00 95.91  ? 691  GLU A CD  1 
ATOM   5079 O OE1 . GLU A 1 665 ? -96.110  -0.015  28.171  1.00 109.08 ? 691  GLU A OE1 1 
ATOM   5080 O OE2 . GLU A 1 665 ? -96.173  2.111   28.727  1.00 96.11  ? 691  GLU A OE2 1 
ATOM   5081 N N   . LEU A 1 666 ? -95.747  -2.773  33.122  1.00 71.99  ? 692  LEU A N   1 
ATOM   5082 C CA  . LEU A 1 666 ? -95.223  -4.091  33.442  1.00 66.85  ? 692  LEU A CA  1 
ATOM   5083 C C   . LEU A 1 666 ? -95.136  -4.327  34.941  1.00 65.40  ? 692  LEU A C   1 
ATOM   5084 O O   . LEU A 1 666 ? -94.726  -3.457  35.693  1.00 66.19  ? 692  LEU A O   1 
ATOM   5085 C CB  . LEU A 1 666 ? -93.861  -4.275  32.792  1.00 67.79  ? 692  LEU A CB  1 
ATOM   5086 C CG  . LEU A 1 666 ? -93.315  -5.709  32.799  1.00 73.88  ? 692  LEU A CG  1 
ATOM   5087 C CD1 . LEU A 1 666 ? -91.989  -5.742  32.077  1.00 75.46  ? 692  LEU A CD1 1 
ATOM   5088 C CD2 . LEU A 1 666 ? -93.150  -6.267  34.191  1.00 81.20  ? 692  LEU A CD2 1 
ATOM   5089 N N   . LEU A 1 667 ? -95.619  -5.483  35.367  1.00 59.02  ? 693  LEU A N   1 
ATOM   5090 C CA  . LEU A 1 667 ? -95.600  -5.863  36.761  1.00 59.90  ? 693  LEU A CA  1 
ATOM   5091 C C   . LEU A 1 667 ? -95.063  -7.258  36.821  1.00 60.80  ? 693  LEU A C   1 
ATOM   5092 O O   . LEU A 1 667 ? -95.624  -8.170  36.225  1.00 59.23  ? 693  LEU A O   1 
ATOM   5093 C CB  . LEU A 1 667 ? -96.973  -5.765  37.399  1.00 61.40  ? 693  LEU A CB  1 
ATOM   5094 C CG  . LEU A 1 667 ? -97.072  -6.320  38.825  1.00 68.38  ? 693  LEU A CG  1 
ATOM   5095 C CD1 . LEU A 1 667 ? -95.975  -5.791  39.740  1.00 72.65  ? 693  LEU A CD1 1 
ATOM   5096 C CD2 . LEU A 1 667 ? -98.442  -6.009  39.402  1.00 72.44  ? 693  LEU A CD2 1 
ATOM   5097 N N   . ASP A 1 668 ? -93.950  -7.417  37.533  1.00 61.65  ? 694  ASP A N   1 
ATOM   5098 C CA  . ASP A 1 668 ? -93.291  -8.693  37.621  1.00 57.48  ? 694  ASP A CA  1 
ATOM   5099 C C   . ASP A 1 668 ? -93.262  -9.241  39.023  1.00 60.31  ? 694  ASP A C   1 
ATOM   5100 O O   . ASP A 1 668 ? -92.730  -8.618  39.933  1.00 63.50  ? 694  ASP A O   1 
ATOM   5101 C CB  . ASP A 1 668 ? -91.883  -8.525  37.085  1.00 56.91  ? 694  ASP A CB  1 
ATOM   5102 C CG  . ASP A 1 668 ? -91.096  -9.775  37.143  1.00 61.22  ? 694  ASP A CG  1 
ATOM   5103 O OD1 . ASP A 1 668 ? -91.619  -10.793 37.647  1.00 67.94  ? 694  ASP A OD1 1 
ATOM   5104 O OD2 . ASP A 1 668 ? -89.925  -9.727  36.732  1.00 62.83  ? 694  ASP A OD2 1 
ATOM   5105 N N   . LEU A 1 669 ? -93.823  -10.433 39.177  1.00 63.21  ? 695  LEU A N   1 
ATOM   5106 C CA  . LEU A 1 669 ? -93.887  -11.094 40.463  1.00 53.02  ? 695  LEU A CA  1 
ATOM   5107 C C   . LEU A 1 669 ? -93.436  -12.509 40.362  1.00 53.08  ? 695  LEU A C   1 
ATOM   5108 O O   . LEU A 1 669 ? -93.829  -13.328 41.189  1.00 61.88  ? 695  LEU A O   1 
ATOM   5109 C CB  . LEU A 1 669 ? -95.300  -11.086 41.003  1.00 54.57  ? 695  LEU A CB  1 
ATOM   5110 C CG  . LEU A 1 669 ? -95.937  -9.732  41.248  1.00 64.86  ? 695  LEU A CG  1 
ATOM   5111 C CD1 . LEU A 1 669 ? -97.378  -9.916  41.655  1.00 72.46  ? 695  LEU A CD1 1 
ATOM   5112 C CD2 . LEU A 1 669 ? -95.184  -8.971  42.324  1.00 76.16  ? 695  LEU A CD2 1 
ATOM   5113 N N   . ARG A 1 670 ? -92.609  -12.847 39.376  1.00 51.82  ? 696  ARG A N   1 
ATOM   5114 C CA  . ARG A 1 670 ? -92.183  -14.235 39.331  1.00 58.91  ? 696  ARG A CA  1 
ATOM   5115 C C   . ARG A 1 670 ? -91.423  -14.598 40.617  1.00 62.29  ? 696  ARG A C   1 
ATOM   5116 O O   . ARG A 1 670 ? -91.010  -13.740 41.379  1.00 64.24  ? 696  ARG A O   1 
ATOM   5117 C CB  . ARG A 1 670 ? -91.279  -14.595 38.139  1.00 63.05  ? 696  ARG A CB  1 
ATOM   5118 C CG  . ARG A 1 670 ? -91.825  -14.310 36.756  1.00 67.32  ? 696  ARG A CG  1 
ATOM   5119 C CD  . ARG A 1 670 ? -91.232  -13.063 36.184  1.00 68.99  ? 696  ARG A CD  1 
ATOM   5120 N NE  . ARG A 1 670 ? -89.900  -13.404 35.725  1.00 79.16  ? 696  ARG A NE  1 
ATOM   5121 C CZ  . ARG A 1 670 ? -88.979  -12.528 35.385  1.00 81.71  ? 696  ARG A CZ  1 
ATOM   5122 N NH1 . ARG A 1 670 ? -89.153  -11.247 35.640  1.00 81.34  ? 696  ARG A NH1 1 
ATOM   5123 N NH2 . ARG A 1 670 ? -87.813  -12.961 34.967  1.00 89.70  ? 696  ARG A NH2 1 
ATOM   5124 N N   . GLY A 1 671 ? -91.257  -15.890 40.834  1.00 67.76  ? 697  GLY A N   1 
ATOM   5125 C CA  . GLY A 1 671 ? -90.523  -16.408 41.965  1.00 66.83  ? 697  GLY A CA  1 
ATOM   5126 C C   . GLY A 1 671 ? -90.921  -16.003 43.371  1.00 73.17  ? 697  GLY A C   1 
ATOM   5127 O O   . GLY A 1 671 ? -90.089  -15.569 44.157  1.00 66.71  ? 697  GLY A O   1 
ATOM   5128 N N   . ASN A 1 672 ? -92.205  -16.011 43.645  1.00 70.41  ? 698  ASN A N   1 
ATOM   5129 C CA  . ASN A 1 672 ? -92.680  -15.736 44.975  1.00 65.42  ? 698  ASN A CA  1 
ATOM   5130 C C   . ASN A 1 672 ? -93.442  -16.974 45.465  1.00 61.14  ? 698  ASN A C   1 
ATOM   5131 O O   . ASN A 1 672 ? -93.209  -18.077 45.000  1.00 67.69  ? 698  ASN A O   1 
ATOM   5132 C CB  . ASN A 1 672 ? -93.521  -14.453 45.089  1.00 69.19  ? 698  ASN A CB  1 
ATOM   5133 C CG  . ASN A 1 672 ? -92.676  -13.177 45.073  1.00 75.81  ? 698  ASN A CG  1 
ATOM   5134 O OD1 . ASN A 1 672 ? -92.415  -12.587 46.127  1.00 70.73  ? 698  ASN A OD1 1 
ATOM   5135 N ND2 . ASN A 1 672 ? -92.153  -12.819 43.920  1.00 76.72  ? 698  ASN A ND2 1 
ATOM   5136 N N   . LYS A 1 673 ? -94.292  -16.787 46.451  1.00 68.77  ? 699  LYS A N   1 
ATOM   5137 C CA  . LYS A 1 673 ? -95.087  -17.852 47.030  1.00 76.39  ? 699  LYS A CA  1 
ATOM   5138 C C   . LYS A 1 673 ? -96.577  -17.477 46.962  1.00 74.24  ? 699  LYS A C   1 
ATOM   5139 O O   . LYS A 1 673 ? -97.375  -17.906 47.796  1.00 76.96  ? 699  LYS A O   1 
ATOM   5140 C CB  . LYS A 1 673 ? -94.652  -18.000 48.493  1.00 71.99  ? 699  LYS A CB  1 
ATOM   5141 C CG  . LYS A 1 673 ? -93.376  -18.790 48.714  1.00 72.87  ? 699  LYS A CG  1 
ATOM   5142 C CD  . LYS A 1 673 ? -92.839  -18.488 50.111  1.00 80.06  ? 699  LYS A CD  1 
ATOM   5143 C CE  . LYS A 1 673 ? -91.781  -19.476 50.568  1.00 73.49  ? 699  LYS A CE  1 
ATOM   5144 N NZ  . LYS A 1 673 ? -91.241  -19.031 51.890  1.00 81.22  ? 699  LYS A NZ  1 
ATOM   5145 N N   . LEU A 1 674 ? -96.947  -16.673 45.971  1.00 73.24  ? 700  LEU A N   1 
ATOM   5146 C CA  . LEU A 1 674 ? -98.346  -16.204 45.841  1.00 82.20  ? 700  LEU A CA  1 
ATOM   5147 C C   . LEU A 1 674 ? -99.403  -17.293 45.788  1.00 83.31  ? 700  LEU A C   1 
ATOM   5148 O O   . LEU A 1 674 ? -99.293  -18.267 45.021  1.00 59.29  ? 700  LEU A O   1 
ATOM   5149 C CB  . LEU A 1 674 ? -98.507  -15.292 44.650  1.00 78.61  ? 700  LEU A CB  1 
ATOM   5150 C CG  . LEU A 1 674 ? -97.731  -13.996 44.743  1.00 79.61  ? 700  LEU A CG  1 
ATOM   5151 C CD1 . LEU A 1 674 ? -97.813  -13.294 43.411  1.00 90.06  ? 700  LEU A CD1 1 
ATOM   5152 C CD2 . LEU A 1 674 ? -98.259  -13.112 45.855  1.00 81.85  ? 700  LEU A CD2 1 
ATOM   5153 N N   . LEU A 1 675 ? -100.494 -17.023 46.496  1.00 74.83  ? 701  LEU A N   1 
ATOM   5154 C CA  . LEU A 1 675 ? -101.591 -17.961 46.630  1.00 88.45  ? 701  LEU A CA  1 
ATOM   5155 C C   . LEU A 1 675 ? -102.862 -17.654 45.843  1.00 88.96  ? 701  LEU A C   1 
ATOM   5156 O O   . LEU A 1 675 ? -103.376 -18.526 45.145  1.00 89.12  ? 701  LEU A O   1 
ATOM   5157 C CB  . LEU A 1 675 ? -101.939 -18.058 48.116  1.00 88.68  ? 701  LEU A CB  1 
ATOM   5158 C CG  . LEU A 1 675 ? -100.812 -18.599 49.003  1.00 93.18  ? 701  LEU A CG  1 
ATOM   5159 C CD1 . LEU A 1 675 ? -101.131 -18.425 50.483  1.00 89.56  ? 701  LEU A CD1 1 
ATOM   5160 C CD2 . LEU A 1 675 ? -100.513 -20.056 48.659  1.00 86.02  ? 701  LEU A CD2 1 
ATOM   5161 N N   . PHE A 1 676 ? -103.346 -16.421 45.937  1.00 81.19  ? 702  PHE A N   1 
ATOM   5162 C CA  . PHE A 1 676 ? -104.571 -16.056 45.267  1.00 87.26  ? 702  PHE A CA  1 
ATOM   5163 C C   . PHE A 1 676 ? -104.420 -14.871 44.313  1.00 84.99  ? 702  PHE A C   1 
ATOM   5164 O O   . PHE A 1 676 ? -103.434 -14.163 44.341  1.00 80.11  ? 702  PHE A O   1 
ATOM   5165 C CB  . PHE A 1 676 ? -105.626 -15.713 46.328  1.00 93.82  ? 702  PHE A CB  1 
ATOM   5166 C CG  . PHE A 1 676 ? -105.499 -14.326 46.905  1.00 111.96 ? 702  PHE A CG  1 
ATOM   5167 C CD1 . PHE A 1 676 ? -106.373 -13.319 46.499  1.00 133.81 ? 702  PHE A CD1 1 
ATOM   5168 C CD2 . PHE A 1 676 ? -104.489 -13.999 47.796  1.00 143.75 ? 702  PHE A CD2 1 
ATOM   5169 C CE1 . PHE A 1 676 ? -106.278 -12.035 47.014  1.00 146.70 ? 702  PHE A CE1 1 
ATOM   5170 C CE2 . PHE A 1 676 ? -104.375 -12.701 48.295  1.00 155.03 ? 702  PHE A CE2 1 
ATOM   5171 C CZ  . PHE A 1 676 ? -105.273 -11.723 47.909  1.00 150.11 ? 702  PHE A CZ  1 
ATOM   5172 N N   . LEU A 1 677 ? -105.413 -14.698 43.446  1.00 90.74  ? 703  LEU A N   1 
ATOM   5173 C CA  . LEU A 1 677 ? -105.461 -13.591 42.490  1.00 77.29  ? 703  LEU A CA  1 
ATOM   5174 C C   . LEU A 1 677 ? -106.705 -12.747 42.733  1.00 86.78  ? 703  LEU A C   1 
ATOM   5175 O O   . LEU A 1 677 ? -107.691 -13.230 43.283  1.00 107.95 ? 703  LEU A O   1 
ATOM   5176 C CB  . LEU A 1 677 ? -105.452 -14.102 41.062  1.00 71.50  ? 703  LEU A CB  1 
ATOM   5177 C CG  . LEU A 1 677 ? -104.119 -14.650 40.567  1.00 81.00  ? 703  LEU A CG  1 
ATOM   5178 C CD1 . LEU A 1 677 ? -104.238 -15.261 39.180  1.00 80.65  ? 703  LEU A CD1 1 
ATOM   5179 C CD2 . LEU A 1 677 ? -103.093 -13.529 40.548  1.00 87.58  ? 703  LEU A CD2 1 
ATOM   5180 N N   . THR A 1 678 ? -106.648 -11.473 42.356  1.00 92.32  ? 704  THR A N   1 
ATOM   5181 C CA  . THR A 1 678 ? -107.787 -10.576 42.554  1.00 89.32  ? 704  THR A CA  1 
ATOM   5182 C C   . THR A 1 678 ? -108.892 -10.976 41.607  1.00 89.88  ? 704  THR A C   1 
ATOM   5183 O O   . THR A 1 678 ? -108.634 -11.409 40.488  1.00 80.83  ? 704  THR A O   1 
ATOM   5184 C CB  . THR A 1 678 ? -107.428 -9.091  42.312  1.00 93.66  ? 704  THR A CB  1 
ATOM   5185 O OG1 . THR A 1 678 ? -108.539 -8.252  42.657  1.00 82.97  ? 704  THR A OG1 1 
ATOM   5186 C CG2 . THR A 1 678 ? -107.029 -8.839  40.863  1.00 95.36  ? 704  THR A CG2 1 
ATOM   5187 N N   . ASP A 1 679 ? -110.124 -10.864 42.081  1.00 109.12 ? 705  ASP A N   1 
ATOM   5188 C CA  . ASP A 1 679 ? -111.291 -11.215 41.281  1.00 119.37 ? 705  ASP A CA  1 
ATOM   5189 C C   . ASP A 1 679 ? -111.681 -10.091 40.323  1.00 105.98 ? 705  ASP A C   1 
ATOM   5190 O O   . ASP A 1 679 ? -112.185 -10.351 39.232  1.00 112.13 ? 705  ASP A O   1 
ATOM   5191 C CB  . ASP A 1 679 ? -112.472 -11.612 42.189  1.00 126.09 ? 705  ASP A CB  1 
ATOM   5192 C CG  . ASP A 1 679 ? -112.791 -10.556 43.257  1.00 139.75 ? 705  ASP A CG  1 
ATOM   5193 O OD1 . ASP A 1 679 ? -113.858 -10.672 43.896  1.00 147.96 ? 705  ASP A OD1 1 
ATOM   5194 O OD2 . ASP A 1 679 ? -111.983 -9.620  43.464  1.00 134.27 ? 705  ASP A OD2 1 
ATOM   5195 N N   . SER A 1 680 ? -111.365 -8.856  40.701  1.00 90.66  ? 706  SER A N   1 
ATOM   5196 C CA  . SER A 1 680 ? -111.691 -7.684  39.893  1.00 97.50  ? 706  SER A CA  1 
ATOM   5197 C C   . SER A 1 680 ? -110.459 -6.847  39.525  1.00 96.67  ? 706  SER A C   1 
ATOM   5198 O O   . SER A 1 680 ? -110.361 -5.670  39.883  1.00 85.69  ? 706  SER A O   1 
ATOM   5199 C CB  . SER A 1 680 ? -112.689 -6.825  40.660  1.00 97.09  ? 706  SER A CB  1 
ATOM   5200 O OG  . SER A 1 680 ? -112.165 -6.481  41.924  1.00 84.95  ? 706  SER A OG  1 
ATOM   5201 N N   . LEU A 1 681 ? -109.608 -7.403  38.674  1.00 93.04  ? 707  LEU A N   1 
ATOM   5202 C CA  . LEU A 1 681 ? -108.381 -6.721  38.281  1.00 97.61  ? 707  LEU A CA  1 
ATOM   5203 C C   . LEU A 1 681 ? -108.641 -5.347  37.630  1.00 90.44  ? 707  LEU A C   1 
ATOM   5204 O O   . LEU A 1 681 ? -108.042 -4.352  38.031  1.00 101.40 ? 707  LEU A O   1 
ATOM   5205 C CB  . LEU A 1 681 ? -107.547 -7.635  37.359  1.00 98.89  ? 707  LEU A CB  1 
ATOM   5206 C CG  . LEU A 1 681 ? -106.031 -7.375  37.177  1.00 97.73  ? 707  LEU A CG  1 
ATOM   5207 C CD1 . LEU A 1 681 ? -105.409 -8.378  36.211  1.00 105.01 ? 707  LEU A CD1 1 
ATOM   5208 C CD2 . LEU A 1 681 ? -105.703 -5.979  36.726  1.00 92.86  ? 707  LEU A CD2 1 
ATOM   5209 N N   . SER A 1 682 ? -109.634 -5.251  36.754  1.00 98.41  ? 708  SER A N   1 
ATOM   5210 C CA  . SER A 1 682 ? -109.894 -3.970  36.066  1.00 98.18  ? 708  SER A CA  1 
ATOM   5211 C C   . SER A 1 682 ? -110.428 -2.843  36.915  1.00 94.43  ? 708  SER A C   1 
ATOM   5212 O O   . SER A 1 682 ? -110.584 -1.732  36.422  1.00 87.00  ? 708  SER A O   1 
ATOM   5213 C CB  . SER A 1 682 ? -110.808 -4.119  34.868  1.00 101.68 ? 708  SER A CB  1 
ATOM   5214 O OG  . SER A 1 682 ? -111.006 -2.854  34.271  1.00 111.53 ? 708  SER A OG  1 
ATOM   5215 N N   . ASP A 1 683 ? -110.792 -3.111  38.155  1.00 96.93  ? 709  ASP A N   1 
ATOM   5216 C CA  . ASP A 1 683 ? -111.271 -2.020  38.985  1.00 114.16 ? 709  ASP A CA  1 
ATOM   5217 C C   . ASP A 1 683 ? -110.031 -1.319  39.535  1.00 117.85 ? 709  ASP A C   1 
ATOM   5218 O O   . ASP A 1 683 ? -110.139 -0.268  40.179  1.00 106.23 ? 709  ASP A O   1 
ATOM   5219 C CB  . ASP A 1 683 ? -112.176 -2.521  40.127  1.00 116.13 ? 709  ASP A CB  1 
ATOM   5220 C CG  . ASP A 1 683 ? -113.459 -3.189  39.622  1.00 114.16 ? 709  ASP A CG  1 
ATOM   5221 O OD1 . ASP A 1 683 ? -113.809 -3.036  38.431  1.00 108.99 ? 709  ASP A OD1 1 
ATOM   5222 O OD2 . ASP A 1 683 ? -114.132 -3.849  40.434  1.00 109.07 ? 709  ASP A OD2 1 
ATOM   5223 N N   . PHE A 1 684 ? -108.847 -1.844  39.192  1.00 116.65 ? 710  PHE A N   1 
ATOM   5224 C CA  . PHE A 1 684 ? -107.600 -1.273  39.695  1.00 113.15 ? 710  PHE A CA  1 
ATOM   5225 C C   . PHE A 1 684 ? -106.615 -0.755  38.644  1.00 109.59 ? 710  PHE A C   1 
ATOM   5226 O O   . PHE A 1 684 ? -105.965 0.262   38.871  1.00 114.86 ? 710  PHE A O   1 
ATOM   5227 C CB  . PHE A 1 684 ? -106.877 -2.301  40.567  1.00 103.91 ? 710  PHE A CB  1 
ATOM   5228 C CG  . PHE A 1 684 ? -107.783 -3.034  41.517  1.00 84.72  ? 710  PHE A CG  1 
ATOM   5229 C CD1 . PHE A 1 684 ? -108.485 -2.348  42.492  1.00 81.21  ? 710  PHE A CD1 1 
ATOM   5230 C CD2 . PHE A 1 684 ? -107.806 -4.422  41.532  1.00 86.11  ? 710  PHE A CD2 1 
ATOM   5231 C CE1 . PHE A 1 684 ? -109.301 -3.020  43.387  1.00 83.64  ? 710  PHE A CE1 1 
ATOM   5232 C CE2 . PHE A 1 684 ? -108.592 -5.106  42.442  1.00 84.50  ? 710  PHE A CE2 1 
ATOM   5233 C CZ  . PHE A 1 684 ? -109.340 -4.404  43.375  1.00 84.34  ? 710  PHE A CZ  1 
ATOM   5234 N N   . THR A 1 685 ? -106.479 -1.450  37.515  1.00 102.62 ? 711  THR A N   1 
ATOM   5235 C CA  . THR A 1 685 ? -105.525 -1.021  36.475  1.00 99.67  ? 711  THR A CA  1 
ATOM   5236 C C   . THR A 1 685 ? -106.142 -0.863  35.097  1.00 100.61 ? 711  THR A C   1 
ATOM   5237 O O   . THR A 1 685 ? -106.923 -1.692  34.651  1.00 112.32 ? 711  THR A O   1 
ATOM   5238 C CB  . THR A 1 685 ? -104.344 -2.013  36.348  1.00 88.31  ? 711  THR A CB  1 
ATOM   5239 O OG1 . THR A 1 685 ? -103.454 -1.596  35.307  1.00 83.38  ? 711  THR A OG1 1 
ATOM   5240 C CG2 . THR A 1 685 ? -104.834 -3.371  36.012  1.00 83.62  ? 711  THR A CG2 1 
ATOM   5241 N N   . SER A 1 686 ? -105.725 0.181   34.400  1.00 99.96  ? 712  SER A N   1 
ATOM   5242 C CA  . SER A 1 686 ? -106.216 0.450   33.067  1.00 90.66  ? 712  SER A CA  1 
ATOM   5243 C C   . SER A 1 686 ? -105.025 0.473   32.103  1.00 99.82  ? 712  SER A C   1 
ATOM   5244 O O   . SER A 1 686 ? -105.208 0.595   30.893  1.00 96.71  ? 712  SER A O   1 
ATOM   5245 C CB  . SER A 1 686 ? -106.886 1.816   33.063  1.00 87.68  ? 712  SER A CB  1 
ATOM   5246 O OG  . SER A 1 686 ? -107.792 1.927   34.150  1.00 89.91  ? 712  SER A OG  1 
ATOM   5247 N N   . SER A 1 687 ? -103.807 0.322   32.646  1.00 100.35 ? 713  SER A N   1 
ATOM   5248 C CA  . SER A 1 687 ? -102.560 0.357   31.840  1.00 85.76  ? 713  SER A CA  1 
ATOM   5249 C C   . SER A 1 687 ? -101.719 -0.924  31.821  1.00 73.22  ? 713  SER A C   1 
ATOM   5250 O O   . SER A 1 687 ? -100.935 -1.142  30.897  1.00 67.65  ? 713  SER A O   1 
ATOM   5251 C CB  . SER A 1 687 ? -101.675 1.506   32.322  1.00 85.64  ? 713  SER A CB  1 
ATOM   5252 O OG  . SER A 1 687 ? -101.371 1.360   33.702  1.00 84.99  ? 713  SER A OG  1 
ATOM   5253 N N   . LEU A 1 688 ? -101.874 -1.776  32.823  1.00 73.27  ? 714  LEU A N   1 
ATOM   5254 C CA  . LEU A 1 688 ? -101.091 -2.988  32.869  1.00 70.86  ? 714  LEU A CA  1 
ATOM   5255 C C   . LEU A 1 688 ? -101.191 -3.747  31.545  1.00 63.21  ? 714  LEU A C   1 
ATOM   5256 O O   . LEU A 1 688 ? -102.269 -3.989  31.054  1.00 72.18  ? 714  LEU A O   1 
ATOM   5257 C CB  . LEU A 1 688 ? -101.532 -3.859  34.049  1.00 80.62  ? 714  LEU A CB  1 
ATOM   5258 C CG  . LEU A 1 688 ? -100.664 -5.100  34.324  1.00 96.67  ? 714  LEU A CG  1 
ATOM   5259 C CD1 . LEU A 1 688 ? -99.220  -4.689  34.581  1.00 107.97 ? 714  LEU A CD1 1 
ATOM   5260 C CD2 . LEU A 1 688 ? -101.182 -5.901  35.511  1.00 90.03  ? 714  LEU A CD2 1 
ATOM   5261 N N   . ARG A 1 689 ? -100.044 -4.029  30.939  1.00 71.15  ? 715  ARG A N   1 
ATOM   5262 C CA  . ARG A 1 689 ? -99.953  -4.765  29.672  1.00 69.71  ? 715  ARG A CA  1 
ATOM   5263 C C   . ARG A 1 689 ? -99.299  -6.118  29.869  1.00 73.51  ? 715  ARG A C   1 
ATOM   5264 O O   . ARG A 1 689 ? -99.636  -7.074  29.175  1.00 76.29  ? 715  ARG A O   1 
ATOM   5265 C CB  . ARG A 1 689 ? -99.087  -4.010  28.640  1.00 80.35  ? 715  ARG A CB  1 
ATOM   5266 C CG  . ARG A 1 689 ? -99.587  -2.638  28.207  1.00 100.50 ? 715  ARG A CG  1 
ATOM   5267 C CD  . ARG A 1 689 ? -98.637  -1.960  27.209  1.00 114.57 ? 715  ARG A CD  1 
ATOM   5268 N NE  . ARG A 1 689 ? -98.416  -2.731  25.974  1.00 128.97 ? 715  ARG A NE  1 
ATOM   5269 C CZ  . ARG A 1 689 ? -97.402  -3.580  25.765  1.00 122.79 ? 715  ARG A CZ  1 
ATOM   5270 N NH1 . ARG A 1 689 ? -97.300  -4.225  24.606  1.00 103.73 ? 715  ARG A NH1 1 
ATOM   5271 N NH2 . ARG A 1 689 ? -96.482  -3.785  26.701  1.00 130.32 ? 715  ARG A NH2 1 
ATOM   5272 N N   . THR A 1 690 ? -98.267  -6.173  30.717  1.00 78.19  ? 716  THR A N   1 
ATOM   5273 C CA  . THR A 1 690 ? -97.556  -7.431  30.953  1.00 72.54  ? 716  THR A CA  1 
ATOM   5274 C C   . THR A 1 690 ? -97.607  -7.807  32.415  1.00 69.12  ? 716  THR A C   1 
ATOM   5275 O O   . THR A 1 690 ? -97.310  -6.984  33.273  1.00 77.20  ? 716  THR A O   1 
ATOM   5276 C CB  . THR A 1 690 ? -96.082  -7.320  30.557  1.00 69.19  ? 716  THR A CB  1 
ATOM   5277 O OG1 . THR A 1 690 ? -95.959  -6.731  29.262  1.00 67.51  ? 716  THR A OG1 1 
ATOM   5278 C CG2 . THR A 1 690 ? -95.419  -8.697  30.580  1.00 73.34  ? 716  THR A CG2 1 
ATOM   5279 N N   . LEU A 1 691 ? -97.937  -9.063  32.692  1.00 62.92  ? 717  LEU A N   1 
ATOM   5280 C CA  . LEU A 1 691 ? -98.029  -9.549  34.069  1.00 67.37  ? 717  LEU A CA  1 
ATOM   5281 C C   . LEU A 1 691 ? -97.333  -10.908 34.171  1.00 71.65  ? 717  LEU A C   1 
ATOM   5282 O O   . LEU A 1 691 ? -97.782  -11.910 33.571  1.00 59.98  ? 717  LEU A O   1 
ATOM   5283 C CB  . LEU A 1 691 ? -99.485  -9.622  34.506  1.00 73.84  ? 717  LEU A CB  1 
ATOM   5284 C CG  . LEU A 1 691 ? -99.790  -10.067 35.939  1.00 86.63  ? 717  LEU A CG  1 
ATOM   5285 C CD1 . LEU A 1 691 ? -99.053  -9.216  36.967  1.00 86.39  ? 717  LEU A CD1 1 
ATOM   5286 C CD2 . LEU A 1 691 ? -101.299 -10.017 36.181  1.00 79.30  ? 717  LEU A CD2 1 
ATOM   5287 N N   . LEU A 1 692 ? -96.219  -10.932 34.915  1.00 66.01  ? 718  LEU A N   1 
ATOM   5288 C CA  . LEU A 1 692 ? -95.431  -12.147 35.065  1.00 63.17  ? 718  LEU A CA  1 
ATOM   5289 C C   . LEU A 1 692 ? -95.618  -12.772 36.448  1.00 65.93  ? 718  LEU A C   1 
ATOM   5290 O O   . LEU A 1 692 ? -95.196  -12.217 37.453  1.00 58.63  ? 718  LEU A O   1 
ATOM   5291 C CB  . LEU A 1 692 ? -93.979  -11.810 34.825  1.00 72.96  ? 718  LEU A CB  1 
ATOM   5292 C CG  . LEU A 1 692 ? -93.672  -11.024 33.539  1.00 77.36  ? 718  LEU A CG  1 
ATOM   5293 C CD1 . LEU A 1 692 ? -92.175  -10.763 33.462  1.00 64.51  ? 718  LEU A CD1 1 
ATOM   5294 C CD2 . LEU A 1 692 ? -94.146  -11.759 32.283  1.00 76.09  ? 718  LEU A CD2 1 
ATOM   5295 N N   . LEU A 1 693 ? -96.236  -13.949 36.483  1.00 69.34  ? 719  LEU A N   1 
ATOM   5296 C CA  . LEU A 1 693 ? -96.521  -14.635 37.737  1.00 59.65  ? 719  LEU A CA  1 
ATOM   5297 C C   . LEU A 1 693 ? -95.972  -16.040 37.746  1.00 55.86  ? 719  LEU A C   1 
ATOM   5298 O O   . LEU A 1 693 ? -96.449  -16.879 38.514  1.00 57.93  ? 719  LEU A O   1 
ATOM   5299 C CB  . LEU A 1 693 ? -98.045  -14.715 37.948  1.00 63.77  ? 719  LEU A CB  1 
ATOM   5300 C CG  . LEU A 1 693 ? -98.835  -13.407 37.951  1.00 72.95  ? 719  LEU A CG  1 
ATOM   5301 C CD1 . LEU A 1 693 ? -100.329 -13.652 37.966  1.00 73.80  ? 719  LEU A CD1 1 
ATOM   5302 C CD2 . LEU A 1 693 ? -98.440  -12.551 39.138  1.00 85.59  ? 719  LEU A CD2 1 
ATOM   5303 N N   . SER A 1 694 ? -95.059  -16.366 36.843  1.00 49.12  ? 720  SER A N   1 
ATOM   5304 C CA  . SER A 1 694 ? -94.512  -17.718 36.884  1.00 56.79  ? 720  SER A CA  1 
ATOM   5305 C C   . SER A 1 694 ? -93.834  -17.982 38.242  1.00 55.29  ? 720  SER A C   1 
ATOM   5306 O O   . SER A 1 694 ? -93.431  -17.058 38.936  1.00 67.87  ? 720  SER A O   1 
ATOM   5307 C CB  . SER A 1 694 ? -93.580  -17.985 35.707  1.00 60.27  ? 720  SER A CB  1 
ATOM   5308 O OG  . SER A 1 694 ? -92.624  -16.963 35.569  1.00 69.37  ? 720  SER A OG  1 
ATOM   5309 N N   . HIS A 1 695 ? -93.750  -19.246 38.617  1.00 62.54  ? 721  HIS A N   1 
ATOM   5310 C CA  . HIS A 1 695 ? -93.161  -19.670 39.894  1.00 63.48  ? 721  HIS A CA  1 
ATOM   5311 C C   . HIS A 1 695 ? -93.843  -19.093 41.119  1.00 72.03  ? 721  HIS A C   1 
ATOM   5312 O O   . HIS A 1 695 ? -93.246  -18.417 41.964  1.00 68.84  ? 721  HIS A O   1 
ATOM   5313 C CB  . HIS A 1 695 ? -91.676  -19.486 39.923  1.00 57.99  ? 721  HIS A CB  1 
ATOM   5314 C CG  . HIS A 1 695 ? -90.970  -20.366 38.958  1.00 57.49  ? 721  HIS A CG  1 
ATOM   5315 N ND1 . HIS A 1 695 ? -90.603  -21.655 39.270  1.00 57.66  ? 721  HIS A ND1 1 
ATOM   5316 C CD2 . HIS A 1 695 ? -90.565  -20.152 37.687  1.00 56.30  ? 721  HIS A CD2 1 
ATOM   5317 C CE1 . HIS A 1 695 ? -89.977  -22.195 38.237  1.00 55.70  ? 721  HIS A CE1 1 
ATOM   5318 N NE2 . HIS A 1 695 ? -89.958  -21.310 37.257  1.00 56.41  ? 721  HIS A NE2 1 
ATOM   5319 N N   . ASN A 1 696 ? -95.129  -19.371 41.181  1.00 71.48  ? 722  ASN A N   1 
ATOM   5320 C CA  . ASN A 1 696 ? -95.944  -18.966 42.274  1.00 68.82  ? 722  ASN A CA  1 
ATOM   5321 C C   . ASN A 1 696 ? -96.774  -20.155 42.726  1.00 64.70  ? 722  ASN A C   1 
ATOM   5322 O O   . ASN A 1 696 ? -96.403  -21.291 42.410  1.00 61.97  ? 722  ASN A O   1 
ATOM   5323 C CB  . ASN A 1 696 ? -96.706  -17.710 41.925  1.00 75.55  ? 722  ASN A CB  1 
ATOM   5324 C CG  . ASN A 1 696 ? -95.854  -16.466 42.110  1.00 74.85  ? 722  ASN A CG  1 
ATOM   5325 O OD1 . ASN A 1 696 ? -95.613  -16.062 43.240  1.00 68.64  ? 722  ASN A OD1 1 
ATOM   5326 N ND2 . ASN A 1 696 ? -95.573  -15.760 41.028  1.00 80.51  ? 722  ASN A ND2 1 
ATOM   5327 N N   . ARG A 1 697 ? -97.744  -19.927 43.610  1.00 67.15  ? 723  ARG A N   1 
ATOM   5328 C CA  . ARG A 1 697 ? -98.589  -21.000 44.133  1.00 72.24  ? 723  ARG A CA  1 
ATOM   5329 C C   . ARG A 1 697 ? -100.067 -20.736 43.840  1.00 79.64  ? 723  ARG A C   1 
ATOM   5330 O O   . ARG A 1 697 ? -100.943 -20.905 44.698  1.00 83.81  ? 723  ARG A O   1 
ATOM   5331 C CB  . ARG A 1 697 ? -98.345  -21.142 45.632  1.00 75.56  ? 723  ARG A CB  1 
ATOM   5332 C CG  . ARG A 1 697 ? -96.942  -21.606 45.966  1.00 80.07  ? 723  ARG A CG  1 
ATOM   5333 C CD  . ARG A 1 697 ? -96.676  -21.580 47.462  1.00 78.05  ? 723  ARG A CD  1 
ATOM   5334 N NE  . ARG A 1 697 ? -95.307  -21.978 47.759  1.00 73.83  ? 723  ARG A NE  1 
ATOM   5335 C CZ  . ARG A 1 697 ? -94.766  -21.967 48.974  1.00 78.57  ? 723  ARG A CZ  1 
ATOM   5336 N NH1 . ARG A 1 697 ? -95.464  -21.552 50.025  1.00 68.54  ? 723  ARG A NH1 1 
ATOM   5337 N NH2 . ARG A 1 697 ? -93.504  -22.344 49.129  1.00 85.60  ? 723  ARG A NH2 1 
ATOM   5338 N N   . ILE A 1 698 ? -100.328 -20.230 42.645  1.00 79.76  ? 724  ILE A N   1 
ATOM   5339 C CA  . ILE A 1 698 ? -101.681 -19.957 42.234  1.00 76.51  ? 724  ILE A CA  1 
ATOM   5340 C C   . ILE A 1 698 ? -102.280 -21.306 41.842  1.00 85.25  ? 724  ILE A C   1 
ATOM   5341 O O   . ILE A 1 698 ? -101.647 -22.102 41.107  1.00 66.48  ? 724  ILE A O   1 
ATOM   5342 C CB  . ILE A 1 698 ? -101.702 -18.951 41.093  1.00 76.72  ? 724  ILE A CB  1 
ATOM   5343 C CG1 . ILE A 1 698 ? -101.239 -17.598 41.634  1.00 75.21  ? 724  ILE A CG1 1 
ATOM   5344 C CG2 . ILE A 1 698 ? -103.100 -18.829 40.530  1.00 74.04  ? 724  ILE A CG2 1 
ATOM   5345 C CD1 . ILE A 1 698 ? -101.123 -16.491 40.601  1.00 77.86  ? 724  ILE A CD1 1 
ATOM   5346 N N   . SER A 1 699 ? -103.433 -21.621 42.435  1.00 74.61  ? 725  SER A N   1 
ATOM   5347 C CA  . SER A 1 699 ? -104.075 -22.901 42.164  1.00 82.01  ? 725  SER A CA  1 
ATOM   5348 C C   . SER A 1 699 ? -105.409 -22.739 41.491  1.00 80.91  ? 725  SER A C   1 
ATOM   5349 O O   . SER A 1 699 ? -105.927 -23.680 40.896  1.00 88.50  ? 725  SER A O   1 
ATOM   5350 C CB  . SER A 1 699 ? -104.235 -23.694 43.458  1.00 74.14  ? 725  SER A CB  1 
ATOM   5351 O OG  . SER A 1 699 ? -105.008 -22.969 44.405  1.00 77.73  ? 725  SER A OG  1 
ATOM   5352 N N   . HIS A 1 700 ? -105.920 -21.521 41.511  1.00 79.92  ? 726  HIS A N   1 
ATOM   5353 C CA  . HIS A 1 700 ? -107.197 -21.233 40.922  1.00 85.45  ? 726  HIS A CA  1 
ATOM   5354 C C   . HIS A 1 700 ? -107.190 -19.899 40.214  1.00 83.62  ? 726  HIS A C   1 
ATOM   5355 O O   . HIS A 1 700 ? -106.844 -18.869 40.802  1.00 71.97  ? 726  HIS A O   1 
ATOM   5356 C CB  . HIS A 1 700 ? -108.266 -21.238 42.022  1.00 92.34  ? 726  HIS A CB  1 
ATOM   5357 C CG  . HIS A 1 700 ? -109.619 -20.802 41.558  1.00 110.26 ? 726  HIS A CG  1 
ATOM   5358 N ND1 . HIS A 1 700 ? -110.499 -21.651 40.918  1.00 120.22 ? 726  HIS A ND1 1 
ATOM   5359 C CD2 . HIS A 1 700 ? -110.272 -19.623 41.701  1.00 121.60 ? 726  HIS A CD2 1 
ATOM   5360 C CE1 . HIS A 1 700 ? -111.618 -21.000 40.650  1.00 132.10 ? 726  HIS A CE1 1 
ATOM   5361 N NE2 . HIS A 1 700 ? -111.507 -19.768 41.117  1.00 124.83 ? 726  HIS A NE2 1 
ATOM   5362 N N   . LEU A 1 701 ? -107.595 -19.911 38.952  1.00 91.15  ? 727  LEU A N   1 
ATOM   5363 C CA  . LEU A 1 701 ? -107.659 -18.680 38.179  1.00 95.10  ? 727  LEU A CA  1 
ATOM   5364 C C   . LEU A 1 701 ? -109.131 -18.299 38.272  1.00 84.68  ? 727  LEU A C   1 
ATOM   5365 O O   . LEU A 1 701 ? -109.981 -19.103 37.933  1.00 95.72  ? 727  LEU A O   1 
ATOM   5366 C CB  . LEU A 1 701 ? -107.241 -18.939 36.738  1.00 84.90  ? 727  LEU A CB  1 
ATOM   5367 C CG  . LEU A 1 701 ? -106.784 -17.708 35.958  1.00 99.22  ? 727  LEU A CG  1 
ATOM   5368 C CD1 . LEU A 1 701 ? -106.309 -18.160 34.588  1.00 87.39  ? 727  LEU A CD1 1 
ATOM   5369 C CD2 . LEU A 1 701 ? -107.832 -16.601 35.849  1.00 110.07 ? 727  LEU A CD2 1 
ATOM   5370 N N   . PRO A 1 702 ? -109.444 -17.107 38.804  1.00 99.48  ? 728  PRO A N   1 
ATOM   5371 C CA  . PRO A 1 702 ? -110.856 -16.733 38.933  1.00 114.29 ? 728  PRO A CA  1 
ATOM   5372 C C   . PRO A 1 702 ? -111.522 -16.195 37.670  1.00 126.41 ? 728  PRO A C   1 
ATOM   5373 O O   . PRO A 1 702 ? -110.875 -16.024 36.633  1.00 128.11 ? 728  PRO A O   1 
ATOM   5374 C CB  . PRO A 1 702 ? -110.839 -15.649 40.020  1.00 111.33 ? 728  PRO A CB  1 
ATOM   5375 C CG  . PRO A 1 702 ? -109.483 -15.048 39.944  1.00 106.82 ? 728  PRO A CG  1 
ATOM   5376 C CD  . PRO A 1 702 ? -108.546 -16.084 39.371  1.00 108.40 ? 728  PRO A CD  1 
ATOM   5377 N N   . SER A 1 703 ? -112.826 -15.948 37.783  1.00 141.55 ? 729  SER A N   1 
ATOM   5378 C CA  . SER A 1 703 ? -113.627 -15.423 36.688  1.00 132.79 ? 729  SER A CA  1 
ATOM   5379 C C   . SER A 1 703 ? -112.900 -14.198 36.134  1.00 128.60 ? 729  SER A C   1 
ATOM   5380 O O   . SER A 1 703 ? -112.375 -13.377 36.889  1.00 142.02 ? 729  SER A O   1 
ATOM   5381 C CB  . SER A 1 703 ? -115.016 -15.055 37.208  1.00 128.07 ? 729  SER A CB  1 
ATOM   5382 O OG  . SER A 1 703 ? -115.615 -16.173 37.854  1.00 111.05 ? 729  SER A OG  1 
ATOM   5383 N N   . GLY A 1 704 ? -112.850 -14.087 34.819  1.00 114.00 ? 730  GLY A N   1 
ATOM   5384 C CA  . GLY A 1 704 ? -112.145 -12.985 34.188  1.00 120.97 ? 730  GLY A CA  1 
ATOM   5385 C C   . GLY A 1 704 ? -110.839 -13.536 33.621  1.00 137.55 ? 730  GLY A C   1 
ATOM   5386 O O   . GLY A 1 704 ? -110.641 -14.749 33.597  1.00 134.41 ? 730  GLY A O   1 
ATOM   5387 N N   . PHE A 1 705 ? -109.904 -12.665 33.249  1.00 148.00 ? 731  PHE A N   1 
ATOM   5388 C CA  . PHE A 1 705 ? -110.064 -11.228 33.378  1.00 151.71 ? 731  PHE A CA  1 
ATOM   5389 C C   . PHE A 1 705 ? -110.155 -10.651 31.956  1.00 138.07 ? 731  PHE A C   1 
ATOM   5390 O O   . PHE A 1 705 ? -109.339 -11.006 31.119  1.00 128.53 ? 731  PHE A O   1 
ATOM   5391 C CB  . PHE A 1 705 ? -108.827 -10.658 34.093  1.00 161.48 ? 731  PHE A CB  1 
ATOM   5392 C CG  . PHE A 1 705 ? -108.310 -11.533 35.215  1.00 180.36 ? 731  PHE A CG  1 
ATOM   5393 C CD1 . PHE A 1 705 ? -107.032 -12.097 35.135  1.00 173.84 ? 731  PHE A CD1 1 
ATOM   5394 C CD2 . PHE A 1 705 ? -109.150 -11.956 36.233  1.00 167.07 ? 731  PHE A CD2 1 
ATOM   5395 C CE1 . PHE A 1 705 ? -106.553 -12.930 36.132  1.00 137.48 ? 731  PHE A CE1 1 
ATOM   5396 C CE2 . PHE A 1 705 ? -108.683 -12.809 37.218  1.00 152.40 ? 731  PHE A CE2 1 
ATOM   5397 C CZ  . PHE A 1 705 ? -107.384 -13.296 37.167  1.00 138.33 ? 731  PHE A CZ  1 
ATOM   5398 N N   . LEU A 1 706 ? -111.157 -9.828  31.635  1.00 131.61 ? 732  LEU A N   1 
ATOM   5399 C CA  . LEU A 1 706 ? -112.231 -9.403  32.537  1.00 137.00 ? 732  LEU A CA  1 
ATOM   5400 C C   . LEU A 1 706 ? -113.532 -9.259  31.762  1.00 133.91 ? 732  LEU A C   1 
ATOM   5401 O O   . LEU A 1 706 ? -114.284 -10.214 31.613  1.00 126.62 ? 732  LEU A O   1 
ATOM   5402 C CB  . LEU A 1 706 ? -111.884 -8.060  33.154  1.00 138.58 ? 732  LEU A CB  1 
ATOM   5403 C CG  . LEU A 1 706 ? -110.704 -8.078  34.113  1.00 142.93 ? 732  LEU A CG  1 
ATOM   5404 C CD1 . LEU A 1 706 ? -110.227 -6.682  34.337  1.00 141.78 ? 732  LEU A CD1 1 
ATOM   5405 C CD2 . LEU A 1 706 ? -111.050 -8.761  35.432  1.00 132.83 ? 732  LEU A CD2 1 
ATOM   5406 N N   . SER A 1 710 ? -109.487 -4.465  29.371  1.00 113.90 ? 736  SER A N   1 
ATOM   5407 C CA  . SER A 1 710 ? -108.136 -4.969  29.582  1.00 109.14 ? 736  SER A CA  1 
ATOM   5408 C C   . SER A 1 710 ? -107.125 -4.594  28.488  1.00 113.40 ? 736  SER A C   1 
ATOM   5409 O O   . SER A 1 710 ? -107.335 -4.800  27.273  1.00 83.39  ? 736  SER A O   1 
ATOM   5410 C CB  . SER A 1 710 ? -108.131 -6.492  29.805  1.00 105.00 ? 736  SER A CB  1 
ATOM   5411 O OG  . SER A 1 710 ? -108.746 -6.840  31.041  1.00 111.44 ? 736  SER A OG  1 
ATOM   5412 N N   . SER A 1 711 ? -106.030 -4.015  28.969  1.00 110.87 ? 737  SER A N   1 
ATOM   5413 C CA  . SER A 1 711 ? -104.893 -3.592  28.164  1.00 98.64  ? 737  SER A CA  1 
ATOM   5414 C C   . SER A 1 711 ? -103.832 -4.683  28.260  1.00 89.56  ? 737  SER A C   1 
ATOM   5415 O O   . SER A 1 711 ? -102.803 -4.652  27.590  1.00 84.07  ? 737  SER A O   1 
ATOM   5416 C CB  . SER A 1 711 ? -104.350 -2.282  28.752  1.00 101.71 ? 737  SER A CB  1 
ATOM   5417 O OG  . SER A 1 711 ? -104.241 -2.372  30.170  1.00 89.21  ? 737  SER A OG  1 
ATOM   5418 N N   . LEU A 1 712 ? -104.207 -5.739  28.957  1.00 81.07  ? 738  LEU A N   1 
ATOM   5419 C CA  . LEU A 1 712 ? -103.337 -6.841  29.242  1.00 82.79  ? 738  LEU A CA  1 
ATOM   5420 C C   . LEU A 1 712 ? -103.022 -7.708  28.026  1.00 71.79  ? 738  LEU A C   1 
ATOM   5421 O O   . LEU A 1 712 ? -103.802 -8.555  27.633  1.00 88.02  ? 738  LEU A O   1 
ATOM   5422 C CB  . LEU A 1 712 ? -103.997 -7.618  30.376  1.00 88.13  ? 738  LEU A CB  1 
ATOM   5423 C CG  . LEU A 1 712 ? -103.138 -8.354  31.393  1.00 101.30 ? 738  LEU A CG  1 
ATOM   5424 C CD1 . LEU A 1 712 ? -103.960 -8.487  32.671  1.00 99.54  ? 738  LEU A CD1 1 
ATOM   5425 C CD2 . LEU A 1 712 ? -102.516 -9.668  30.930  1.00 110.48 ? 738  LEU A CD2 1 
ATOM   5426 N N   . LYS A 1 713 ? -101.821 -7.532  27.491  1.00 76.91  ? 739  LYS A N   1 
ATOM   5427 C CA  . LYS A 1 713 ? -101.374 -8.279  26.335  1.00 77.10  ? 739  LYS A CA  1 
ATOM   5428 C C   . LYS A 1 713 ? -100.543 -9.505  26.657  1.00 78.91  ? 739  LYS A C   1 
ATOM   5429 O O   . LYS A 1 713 ? -100.455 -10.411 25.840  1.00 73.58  ? 739  LYS A O   1 
ATOM   5430 C CB  . LYS A 1 713 ? -100.565 -7.378  25.403  1.00 87.60  ? 739  LYS A CB  1 
ATOM   5431 C CG  . LYS A 1 713 ? -101.360 -6.209  24.824  1.00 114.66 ? 739  LYS A CG  1 
ATOM   5432 C CD  . LYS A 1 713 ? -100.549 -5.463  23.765  1.00 130.37 ? 739  LYS A CD  1 
ATOM   5433 C CE  . LYS A 1 713 ? -101.372 -4.410  23.025  1.00 130.18 ? 739  LYS A CE  1 
ATOM   5434 N NZ  . LYS A 1 713 ? -100.626 -3.824  21.870  1.00 126.61 ? 739  LYS A NZ  1 
ATOM   5435 N N   . HIS A 1 714 ? -99.897  -9.537  27.819  1.00 80.71  ? 740  HIS A N   1 
ATOM   5436 C CA  . HIS A 1 714 ? -99.056  -10.689 28.166  1.00 79.23  ? 740  HIS A CA  1 
ATOM   5437 C C   . HIS A 1 714 ? -99.353  -11.171 29.585  1.00 75.75  ? 740  HIS A C   1 
ATOM   5438 O O   . HIS A 1 714 ? -99.344  -10.382 30.523  1.00 86.12  ? 740  HIS A O   1 
ATOM   5439 C CB  . HIS A 1 714 ? -97.599  -10.279 28.094  1.00 78.58  ? 740  HIS A CB  1 
ATOM   5440 C CG  . HIS A 1 714 ? -96.640  -11.411 28.268  1.00 73.43  ? 740  HIS A CG  1 
ATOM   5441 N ND1 . HIS A 1 714 ? -95.579  -11.612 27.418  1.00 84.06  ? 740  HIS A ND1 1 
ATOM   5442 C CD2 . HIS A 1 714 ? -96.697  -12.512 29.053  1.00 82.73  ? 740  HIS A CD2 1 
ATOM   5443 C CE1 . HIS A 1 714 ? -94.918  -12.693 27.790  1.00 78.55  ? 740  HIS A CE1 1 
ATOM   5444 N NE2 . HIS A 1 714 ? -95.590  -13.274 28.763  1.00 79.53  ? 740  HIS A NE2 1 
ATOM   5445 N N   . LEU A 1 715 ? -99.553  -12.475 29.741  1.00 70.03  ? 741  LEU A N   1 
ATOM   5446 C CA  . LEU A 1 715 ? -99.858  -13.068 31.050  1.00 74.02  ? 741  LEU A CA  1 
ATOM   5447 C C   . LEU A 1 715 ? -99.084  -14.353 31.216  1.00 83.70  ? 741  LEU A C   1 
ATOM   5448 O O   . LEU A 1 715 ? -99.274  -15.302 30.441  1.00 76.83  ? 741  LEU A O   1 
ATOM   5449 C CB  . LEU A 1 715 ? -101.340 -13.387 31.179  1.00 73.64  ? 741  LEU A CB  1 
ATOM   5450 C CG  . LEU A 1 715 ? -101.727 -14.117 32.469  1.00 76.70  ? 741  LEU A CG  1 
ATOM   5451 C CD1 . LEU A 1 715 ? -101.478 -13.232 33.679  1.00 81.06  ? 741  LEU A CD1 1 
ATOM   5452 C CD2 . LEU A 1 715 ? -103.184 -14.542 32.443  1.00 72.80  ? 741  LEU A CD2 1 
ATOM   5453 N N   . ASP A 1 716 ? -98.246  -14.408 32.253  1.00 80.11  ? 742  ASP A N   1 
ATOM   5454 C CA  . ASP A 1 716 ? -97.438  -15.593 32.492  1.00 74.06  ? 742  ASP A CA  1 
ATOM   5455 C C   . ASP A 1 716 ? -97.850  -16.301 33.761  1.00 71.01  ? 742  ASP A C   1 
ATOM   5456 O O   . ASP A 1 716 ? -97.646  -15.783 34.853  1.00 69.84  ? 742  ASP A O   1 
ATOM   5457 C CB  . ASP A 1 716 ? -95.973  -15.220 32.569  1.00 79.87  ? 742  ASP A CB  1 
ATOM   5458 C CG  . ASP A 1 716 ? -95.112  -16.395 32.875  1.00 81.95  ? 742  ASP A CG  1 
ATOM   5459 O OD1 . ASP A 1 716 ? -95.676  -17.504 32.951  1.00 85.21  ? 742  ASP A OD1 1 
ATOM   5460 O OD2 . ASP A 1 716 ? -93.882  -16.219 33.038  1.00 80.14  ? 742  ASP A OD2 1 
ATOM   5461 N N   . LEU A 1 717 ? -98.431  -17.491 33.598  1.00 73.85  ? 743  LEU A N   1 
ATOM   5462 C CA  . LEU A 1 717 ? -98.904  -18.313 34.715  1.00 72.87  ? 743  LEU A CA  1 
ATOM   5463 C C   . LEU A 1 717 ? -98.228  -19.655 34.701  1.00 70.45  ? 743  LEU A C   1 
ATOM   5464 O O   . LEU A 1 717 ? -98.734  -20.635 35.256  1.00 74.86  ? 743  LEU A O   1 
ATOM   5465 C CB  . LEU A 1 717 ? -100.420 -18.495 34.655  1.00 72.73  ? 743  LEU A CB  1 
ATOM   5466 C CG  . LEU A 1 717 ? -101.269 -17.241 34.887  1.00 81.47  ? 743  LEU A CG  1 
ATOM   5467 C CD1 . LEU A 1 717 ? -102.715 -17.459 34.473  1.00 89.71  ? 743  LEU A CD1 1 
ATOM   5468 C CD2 . LEU A 1 717 ? -101.184 -16.779 36.333  1.00 78.56  ? 743  LEU A CD2 1 
ATOM   5469 N N   . SER A 1 718 ? -97.079  -19.705 34.057  1.00 63.39  ? 744  SER A N   1 
ATOM   5470 C CA  . SER A 1 718 ? -96.319  -20.934 33.995  1.00 64.76  ? 744  SER A CA  1 
ATOM   5471 C C   . SER A 1 718 ? -95.770  -21.286 35.384  1.00 64.43  ? 744  SER A C   1 
ATOM   5472 O O   . SER A 1 718 ? -95.681  -20.451 36.264  1.00 59.76  ? 744  SER A O   1 
ATOM   5473 C CB  . SER A 1 718 ? -95.196  -20.797 32.966  1.00 68.67  ? 744  SER A CB  1 
ATOM   5474 O OG  . SER A 1 718 ? -94.421  -19.637 33.218  1.00 73.68  ? 744  SER A OG  1 
ATOM   5475 N N   . SER A 1 719 ? -95.444  -22.548 35.576  1.00 66.71  ? 745  SER A N   1 
ATOM   5476 C CA  . SER A 1 719 ? -94.919  -23.029 36.832  1.00 63.47  ? 745  SER A CA  1 
ATOM   5477 C C   . SER A 1 719 ? -95.674  -22.617 38.104  1.00 73.04  ? 745  SER A C   1 
ATOM   5478 O O   . SER A 1 719 ? -95.090  -22.088 39.028  1.00 73.74  ? 745  SER A O   1 
ATOM   5479 C CB  . SER A 1 719 ? -93.435  -22.737 36.927  1.00 72.11  ? 745  SER A CB  1 
ATOM   5480 O OG  . SER A 1 719 ? -92.733  -23.426 35.885  1.00 69.11  ? 745  SER A OG  1 
ATOM   5481 N N   . ASN A 1 720 ? -96.998  -22.732 38.085  1.00 66.70  ? 746  ASN A N   1 
ATOM   5482 C CA  . ASN A 1 720 ? -97.789  -22.480 39.274  1.00 61.77  ? 746  ASN A CA  1 
ATOM   5483 C C   . ASN A 1 720 ? -98.427  -23.810 39.664  1.00 66.89  ? 746  ASN A C   1 
ATOM   5484 O O   . ASN A 1 720 ? -97.880  -24.876 39.353  1.00 69.73  ? 746  ASN A O   1 
ATOM   5485 C CB  . ASN A 1 720 ? -98.860  -21.430 39.113  1.00 65.47  ? 746  ASN A CB  1 
ATOM   5486 C CG  . ASN A 1 720 ? -98.320  -20.049 39.082  1.00 69.77  ? 746  ASN A CG  1 
ATOM   5487 O OD1 . ASN A 1 720 ? -98.619  -19.253 39.977  1.00 70.31  ? 746  ASN A OD1 1 
ATOM   5488 N ND2 . ASN A 1 720 ? -97.438  -19.776 38.141  1.00 74.94  ? 746  ASN A ND2 1 
ATOM   5489 N N   . LEU A 1 721 ? -99.564  -23.749 40.358  1.00 68.59  ? 747  LEU A N   1 
ATOM   5490 C CA  . LEU A 1 721 ? -100.268 -24.942 40.780  1.00 78.49  ? 747  LEU A CA  1 
ATOM   5491 C C   . LEU A 1 721 ? -101.701 -25.012 40.219  1.00 89.84  ? 747  LEU A C   1 
ATOM   5492 O O   . LEU A 1 721 ? -102.671 -25.163 40.965  1.00 92.30  ? 747  LEU A O   1 
ATOM   5493 C CB  . LEU A 1 721 ? -100.295 -24.984 42.295  1.00 82.48  ? 747  LEU A CB  1 
ATOM   5494 C CG  . LEU A 1 721 ? -98.934  -25.075 42.995  1.00 78.36  ? 747  LEU A CG  1 
ATOM   5495 C CD1 . LEU A 1 721 ? -99.130  -24.918 44.497  1.00 71.32  ? 747  LEU A CD1 1 
ATOM   5496 C CD2 . LEU A 1 721 ? -98.198  -26.369 42.657  1.00 66.75  ? 747  LEU A CD2 1 
ATOM   5497 N N   . LEU A 1 722 ? -101.834 -24.877 38.906  1.00 94.09  ? 748  LEU A N   1 
ATOM   5498 C CA  . LEU A 1 722 ? -103.150 -24.944 38.270  1.00 86.03  ? 748  LEU A CA  1 
ATOM   5499 C C   . LEU A 1 722 ? -103.475 -26.358 37.814  1.00 82.31  ? 748  LEU A C   1 
ATOM   5500 O O   . LEU A 1 722 ? -102.768 -26.939 36.972  1.00 71.07  ? 748  LEU A O   1 
ATOM   5501 C CB  . LEU A 1 722 ? -103.245 -23.972 37.105  1.00 78.29  ? 748  LEU A CB  1 
ATOM   5502 C CG  . LEU A 1 722 ? -103.191 -22.500 37.532  1.00 78.77  ? 748  LEU A CG  1 
ATOM   5503 C CD1 . LEU A 1 722 ? -103.117 -21.602 36.313  1.00 69.85  ? 748  LEU A CD1 1 
ATOM   5504 C CD2 . LEU A 1 722 ? -104.370 -22.098 38.422  1.00 74.41  ? 748  LEU A CD2 1 
ATOM   5505 N N   . LYS A 1 723 ? -104.498 -26.932 38.454  1.00 88.88  ? 749  LYS A N   1 
ATOM   5506 C CA  . LYS A 1 723 ? -104.978 -28.288 38.156  1.00 94.45  ? 749  LYS A CA  1 
ATOM   5507 C C   . LYS A 1 723 ? -105.754 -28.259 36.827  1.00 95.92  ? 749  LYS A C   1 
ATOM   5508 O O   . LYS A 1 723 ? -105.657 -29.170 36.007  1.00 80.49  ? 749  LYS A O   1 
ATOM   5509 C CB  . LYS A 1 723 ? -105.841 -28.821 39.321  1.00 86.20  ? 749  LYS A CB  1 
ATOM   5510 C CG  . LYS A 1 723 ? -105.052 -29.088 40.604  1.00 91.68  ? 749  LYS A CG  1 
ATOM   5511 C CD  . LYS A 1 723 ? -105.940 -29.416 41.801  1.00 109.54 ? 749  LYS A CD  1 
ATOM   5512 C CE  . LYS A 1 723 ? -106.645 -30.766 41.708  1.00 126.72 ? 749  LYS A CE  1 
ATOM   5513 N NZ  . LYS A 1 723 ? -107.623 -30.945 42.830  1.00 132.92 ? 749  LYS A NZ  1 
ATOM   5514 N N   . THR A 1 724 ? -106.459 -27.166 36.593  1.00 83.97  ? 750  THR A N   1 
ATOM   5515 C CA  . THR A 1 724 ? -107.206 -27.001 35.378  1.00 104.88 ? 750  THR A CA  1 
ATOM   5516 C C   . THR A 1 724 ? -107.670 -25.559 35.302  1.00 103.98 ? 750  THR A C   1 
ATOM   5517 O O   . THR A 1 724 ? -107.664 -24.847 36.307  1.00 83.46  ? 750  THR A O   1 
ATOM   5518 C CB  . THR A 1 724 ? -108.420 -27.958 35.342  1.00 128.60 ? 750  THR A CB  1 
ATOM   5519 O OG1 . THR A 1 724 ? -109.132 -27.793 34.108  1.00 142.64 ? 750  THR A OG1 1 
ATOM   5520 C CG2 . THR A 1 724 ? -109.360 -27.708 36.540  1.00 116.46 ? 750  THR A CG2 1 
ATOM   5521 N N   . ILE A 1 725 ? -108.051 -25.116 34.111  1.00 110.38 ? 751  ILE A N   1 
ATOM   5522 C CA  . ILE A 1 725 ? -108.522 -23.754 33.963  1.00 106.74 ? 751  ILE A CA  1 
ATOM   5523 C C   . ILE A 1 725 ? -110.003 -23.706 33.656  1.00 116.84 ? 751  ILE A C   1 
ATOM   5524 O O   . ILE A 1 725 ? -110.442 -24.143 32.590  1.00 127.33 ? 751  ILE A O   1 
ATOM   5525 C CB  . ILE A 1 725 ? -107.784 -22.995 32.872  1.00 104.03 ? 751  ILE A CB  1 
ATOM   5526 C CG1 . ILE A 1 725 ? -106.280 -23.155 33.069  1.00 111.88 ? 751  ILE A CG1 1 
ATOM   5527 C CG2 . ILE A 1 725 ? -108.224 -21.535 32.882  1.00 98.72  ? 751  ILE A CG2 1 
ATOM   5528 C CD1 . ILE A 1 725 ? -105.453 -22.261 32.177  1.00 117.40 ? 751  ILE A CD1 1 
ATOM   5529 N N   . ASN A 1 726 ? -110.755 -23.110 34.566  1.00 122.23 ? 752  ASN A N   1 
ATOM   5530 C CA  . ASN A 1 726 ? -112.177 -22.911 34.415  1.00 128.49 ? 752  ASN A CA  1 
ATOM   5531 C C   . ASN A 1 726 ? -112.384 -21.887 33.322  1.00 134.20 ? 752  ASN A C   1 
ATOM   5532 O O   . ASN A 1 726 ? -111.456 -21.221 32.916  1.00 126.92 ? 752  ASN A O   1 
ATOM   5533 C CB  . ASN A 1 726 ? -112.787 -22.455 35.735  1.00 138.48 ? 752  ASN A CB  1 
ATOM   5534 C CG  . ASN A 1 726 ? -112.846 -23.567 36.772  1.00 136.94 ? 752  ASN A CG  1 
ATOM   5535 O OD1 . ASN A 1 726 ? -113.477 -23.418 37.819  1.00 127.62 ? 752  ASN A OD1 1 
ATOM   5536 N ND2 . ASN A 1 726 ? -112.190 -24.687 36.486  1.00 122.77 ? 752  ASN A ND2 1 
ATOM   5537 N N   . LYS A 1 727 ? -113.587 -21.804 32.790  1.00 146.84 ? 753  LYS A N   1 
ATOM   5538 C CA  . LYS A 1 727 ? -113.785 -21.306 31.444  1.00 144.96 ? 753  LYS A CA  1 
ATOM   5539 C C   . LYS A 1 727 ? -113.291 -19.891 31.157  1.00 148.46 ? 753  LYS A C   1 
ATOM   5540 O O   . LYS A 1 727 ? -112.540 -19.693 30.206  1.00 130.35 ? 753  LYS A O   1 
ATOM   5541 C CB  . LYS A 1 727 ? -115.283 -21.339 31.161  1.00 136.80 ? 753  LYS A CB  1 
ATOM   5542 C CG  . LYS A 1 727 ? -116.146 -20.975 32.363  1.00 136.81 ? 753  LYS A CG  1 
ATOM   5543 C CD  . LYS A 1 727 ? -116.239 -22.136 33.340  1.00 139.79 ? 753  LYS A CD  1 
ATOM   5544 C CE  . LYS A 1 727 ? -116.112 -21.676 34.786  1.00 132.43 ? 753  LYS A CE  1 
ATOM   5545 N NZ  . LYS A 1 727 ? -116.752 -22.617 35.754  1.00 119.42 ? 753  LYS A NZ  1 
ATOM   5546 N N   . SER A 1 728 ? -113.653 -18.921 31.987  1.00 141.33 ? 754  SER A N   1 
ATOM   5547 C CA  . SER A 1 728 ? -112.975 -17.633 31.988  1.00 133.47 ? 754  SER A CA  1 
ATOM   5548 C C   . SER A 1 728 ? -112.739 -17.029 30.607  1.00 141.88 ? 754  SER A C   1 
ATOM   5549 O O   . SER A 1 728 ? -111.607 -16.711 30.269  1.00 123.14 ? 754  SER A O   1 
ATOM   5550 C CB  . SER A 1 728 ? -111.687 -17.689 32.789  1.00 124.01 ? 754  SER A CB  1 
ATOM   5551 O OG  . SER A 1 728 ? -111.926 -17.253 34.111  1.00 125.07 ? 754  SER A OG  1 
ATOM   5552 N N   . ALA A 1 729 ? -113.782 -16.921 29.797  1.00 152.74 ? 755  ALA A N   1 
ATOM   5553 C CA  . ALA A 1 729 ? -113.664 -16.354 28.452  1.00 155.43 ? 755  ALA A CA  1 
ATOM   5554 C C   . ALA A 1 729 ? -113.309 -14.868 28.443  1.00 154.61 ? 755  ALA A C   1 
ATOM   5555 O O   . ALA A 1 729 ? -113.761 -14.116 29.296  1.00 162.76 ? 755  ALA A O   1 
ATOM   5556 C CB  . ALA A 1 729 ? -114.952 -16.579 27.681  1.00 138.39 ? 755  ALA A CB  1 
ATOM   5557 N N   . LEU A 1 730 ? -112.509 -14.443 27.470  1.00 143.36 ? 756  LEU A N   1 
ATOM   5558 C CA  . LEU A 1 730 ? -112.193 -13.028 27.326  1.00 137.85 ? 756  LEU A CA  1 
ATOM   5559 C C   . LEU A 1 730 ? -111.924 -12.365 28.682  1.00 133.99 ? 756  LEU A C   1 
ATOM   5560 O O   . LEU A 1 730 ? -112.816 -11.795 29.304  1.00 126.41 ? 756  LEU A O   1 
ATOM   5561 C CB  . LEU A 1 730 ? -113.287 -12.307 26.515  1.00 132.30 ? 756  LEU A CB  1 
ATOM   5562 C CG  . LEU A 1 730 ? -113.346 -10.774 26.563  1.00 132.92 ? 756  LEU A CG  1 
ATOM   5563 C CD1 . LEU A 1 730 ? -114.297 -10.219 27.635  1.00 119.38 ? 756  LEU A CD1 1 
ATOM   5564 C CD2 . LEU A 1 730 ? -111.939 -10.177 26.623  1.00 120.48 ? 756  LEU A CD2 1 
ATOM   5565 N N   . LYS A 1 737 ? -108.085 -9.776  23.491  1.00 91.73  ? 763  LYS A N   1 
ATOM   5566 C CA  . LYS A 1 737 ? -107.034 -8.757  23.397  1.00 109.77 ? 763  LYS A CA  1 
ATOM   5567 C C   . LYS A 1 737 ? -105.612 -9.111  23.901  1.00 110.58 ? 763  LYS A C   1 
ATOM   5568 O O   . LYS A 1 737 ? -104.755 -8.211  23.999  1.00 85.02  ? 763  LYS A O   1 
ATOM   5569 C CB  . LYS A 1 737 ? -107.499 -7.431  24.023  1.00 118.17 ? 763  LYS A CB  1 
ATOM   5570 C CG  . LYS A 1 737 ? -108.481 -6.657  23.149  1.00 140.97 ? 763  LYS A CG  1 
ATOM   5571 C CD  . LYS A 1 737 ? -108.860 -5.303  23.750  1.00 144.77 ? 763  LYS A CD  1 
ATOM   5572 C CE  . LYS A 1 737 ? -109.592 -4.400  22.749  1.00 134.11 ? 763  LYS A CE  1 
ATOM   5573 N NZ  . LYS A 1 737 ? -110.845 -4.981  22.188  1.00 140.66 ? 763  LYS A NZ  1 
ATOM   5574 N N   . LEU A 1 738 ? -105.325 -10.393 24.156  1.00 97.37  ? 764  LEU A N   1 
ATOM   5575 C CA  . LEU A 1 738 ? -103.984 -10.755 24.616  1.00 94.30  ? 764  LEU A CA  1 
ATOM   5576 C C   . LEU A 1 738 ? -103.198 -11.656 23.645  1.00 87.41  ? 764  LEU A C   1 
ATOM   5577 O O   . LEU A 1 738 ? -103.667 -12.698 23.222  1.00 97.56  ? 764  LEU A O   1 
ATOM   5578 C CB  . LEU A 1 738 ? -103.989 -11.295 26.061  1.00 98.73  ? 764  LEU A CB  1 
ATOM   5579 C CG  . LEU A 1 738 ? -104.648 -12.594 26.533  1.00 83.93  ? 764  LEU A CG  1 
ATOM   5580 C CD1 . LEU A 1 738 ? -103.984 -13.835 25.968  1.00 86.00  ? 764  LEU A CD1 1 
ATOM   5581 C CD2 . LEU A 1 738 ? -104.588 -12.622 28.051  1.00 79.24  ? 764  LEU A CD2 1 
ATOM   5582 N N   . SER A 1 739 ? -101.984 -11.217 23.322  1.00 76.81  ? 765  SER A N   1 
ATOM   5583 C CA  . SER A 1 739 ? -101.075 -11.901 22.404  1.00 78.55  ? 765  SER A CA  1 
ATOM   5584 C C   . SER A 1 739 ? -100.331 -13.116 22.951  1.00 84.83  ? 765  SER A C   1 
ATOM   5585 O O   . SER A 1 739 ? -99.718  -13.859 22.165  1.00 80.12  ? 765  SER A O   1 
ATOM   5586 C CB  . SER A 1 739 ? -99.968  -10.924 21.968  1.00 81.63  ? 765  SER A CB  1 
ATOM   5587 O OG  . SER A 1 739 ? -100.491 -9.718  21.447  1.00 103.92 ? 765  SER A OG  1 
ATOM   5588 N N   . MET A 1 740 ? -100.239 -13.249 24.277  1.00 89.23  ? 766  MET A N   1 
ATOM   5589 C CA  . MET A 1 740 ? -99.491  -14.378 24.849  1.00 90.64  ? 766  MET A CA  1 
ATOM   5590 C C   . MET A 1 740 ? -99.983  -14.819 26.215  1.00 76.70  ? 766  MET A C   1 
ATOM   5591 O O   . MET A 1 740 ? -100.487 -14.014 26.995  1.00 72.85  ? 766  MET A O   1 
ATOM   5592 C CB  . MET A 1 740 ? -97.996  -14.036 24.902  1.00 87.77  ? 766  MET A CB  1 
ATOM   5593 C CG  . MET A 1 740 ? -97.108  -15.164 25.387  1.00 97.39  ? 766  MET A CG  1 
ATOM   5594 S SD  . MET A 1 740 ? -95.345  -14.789 25.250  1.00 99.80  ? 766  MET A SD  1 
ATOM   5595 C CE  . MET A 1 740 ? -95.148  -14.662 23.475  1.00 95.80  ? 766  MET A CE  1 
ATOM   5596 N N   . LEU A 1 741 ? -99.853  -16.121 26.469  1.00 68.22  ? 767  LEU A N   1 
ATOM   5597 C CA  . LEU A 1 741 ? -100.276 -16.731 27.724  1.00 70.31  ? 767  LEU A CA  1 
ATOM   5598 C C   . LEU A 1 741 ? -99.336  -17.883 27.989  1.00 85.68  ? 767  LEU A C   1 
ATOM   5599 O O   . LEU A 1 741 ? -99.282  -18.834 27.195  1.00 71.29  ? 767  LEU A O   1 
ATOM   5600 C CB  . LEU A 1 741 ? -101.675 -17.270 27.596  1.00 74.55  ? 767  LEU A CB  1 
ATOM   5601 C CG  . LEU A 1 741 ? -102.253 -17.951 28.825  1.00 87.40  ? 767  LEU A CG  1 
ATOM   5602 C CD1 . LEU A 1 741 ? -102.456 -16.930 29.932  1.00 89.71  ? 767  LEU A CD1 1 
ATOM   5603 C CD2 . LEU A 1 741 ? -103.580 -18.600 28.459  1.00 89.09  ? 767  LEU A CD2 1 
ATOM   5604 N N   . GLU A 1 742 ? -98.596  -17.815 29.096  1.00 76.64  ? 768  GLU A N   1 
ATOM   5605 C CA  . GLU A 1 742 ? -97.646  -18.866 29.397  1.00 77.44  ? 768  GLU A CA  1 
ATOM   5606 C C   . GLU A 1 742 ? -98.253  -19.803 30.426  1.00 78.43  ? 768  GLU A C   1 
ATOM   5607 O O   . GLU A 1 742 ? -98.779  -19.353 31.456  1.00 75.72  ? 768  GLU A O   1 
ATOM   5608 C CB  . GLU A 1 742 ? -96.346  -18.245 29.876  1.00 93.65  ? 768  GLU A CB  1 
ATOM   5609 C CG  . GLU A 1 742 ? -95.849  -17.159 28.927  1.00 102.70 ? 768  GLU A CG  1 
ATOM   5610 C CD  . GLU A 1 742 ? -94.493  -16.593 29.304  1.00 93.58  ? 768  GLU A CD  1 
ATOM   5611 O OE1 . GLU A 1 742 ? -93.702  -17.320 29.927  1.00 101.41 ? 768  GLU A OE1 1 
ATOM   5612 O OE2 . GLU A 1 742 ? -94.191  -15.451 28.897  1.00 81.13  ? 768  GLU A OE2 1 
ATOM   5613 N N   . LEU A 1 743 ? -98.178  -21.106 30.150  1.00 71.18  ? 769  LEU A N   1 
ATOM   5614 C CA  . LEU A 1 743 ? -98.771  -22.114 31.042  1.00 70.14  ? 769  LEU A CA  1 
ATOM   5615 C C   . LEU A 1 743 ? -97.943  -23.361 31.372  1.00 70.08  ? 769  LEU A C   1 
ATOM   5616 O O   . LEU A 1 743 ? -98.323  -24.112 32.281  1.00 73.34  ? 769  LEU A O   1 
ATOM   5617 C CB  . LEU A 1 743 ? -100.121 -22.555 30.468  1.00 70.62  ? 769  LEU A CB  1 
ATOM   5618 C CG  . LEU A 1 743 ? -101.210 -21.478 30.419  1.00 87.14  ? 769  LEU A CG  1 
ATOM   5619 C CD1 . LEU A 1 743 ? -102.403 -21.923 29.603  1.00 97.72  ? 769  LEU A CD1 1 
ATOM   5620 C CD2 . LEU A 1 743 ? -101.650 -21.086 31.822  1.00 99.79  ? 769  LEU A CD2 1 
ATOM   5621 N N   . HIS A 1 744 ? -96.808  -23.581 30.706  1.00 60.39  ? 770  HIS A N   1 
ATOM   5622 C CA  . HIS A 1 744 ? -96.023  -24.784 31.017  1.00 67.80  ? 770  HIS A CA  1 
ATOM   5623 C C   . HIS A 1 744 ? -95.717  -24.828 32.500  1.00 67.14  ? 770  HIS A C   1 
ATOM   5624 O O   . HIS A 1 744 ? -95.667  -23.802 33.168  1.00 78.72  ? 770  HIS A O   1 
ATOM   5625 C CB  . HIS A 1 744 ? -94.705  -24.811 30.247  1.00 82.07  ? 770  HIS A CB  1 
ATOM   5626 C CG  . HIS A 1 744 ? -93.711  -23.801 30.722  1.00 96.04  ? 770  HIS A CG  1 
ATOM   5627 N ND1 . HIS A 1 744 ? -92.647  -24.138 31.532  1.00 95.38  ? 770  HIS A ND1 1 
ATOM   5628 C CD2 . HIS A 1 744 ? -93.678  -22.452 30.596  1.00 93.96  ? 770  HIS A CD2 1 
ATOM   5629 C CE1 . HIS A 1 744 ? -91.966  -23.047 31.832  1.00 105.47 ? 770  HIS A CE1 1 
ATOM   5630 N NE2 . HIS A 1 744 ? -92.576  -22.010 31.285  1.00 101.11 ? 770  HIS A NE2 1 
ATOM   5631 N N   . GLY A 1 745 ? -95.551  -26.018 33.031  1.00 73.01  ? 771  GLY A N   1 
ATOM   5632 C CA  . GLY A 1 745 ? -95.221  -26.151 34.430  1.00 70.74  ? 771  GLY A CA  1 
ATOM   5633 C C   . GLY A 1 745 ? -96.344  -26.260 35.418  1.00 71.27  ? 771  GLY A C   1 
ATOM   5634 O O   . GLY A 1 745 ? -96.091  -26.352 36.611  1.00 96.42  ? 771  GLY A O   1 
ATOM   5635 N N   . ASN A 1 746 ? -97.587  -26.162 34.987  1.00 79.67  ? 772  ASN A N   1 
ATOM   5636 C CA  . ASN A 1 746 ? -98.645  -26.324 35.965  1.00 79.49  ? 772  ASN A CA  1 
ATOM   5637 C C   . ASN A 1 746 ? -99.025  -27.782 35.970  1.00 80.70  ? 772  ASN A C   1 
ATOM   5638 O O   . ASN A 1 746 ? -98.831  -28.471 34.963  1.00 77.54  ? 772  ASN A O   1 
ATOM   5639 C CB  . ASN A 1 746 ? -99.866  -25.478 35.698  1.00 77.46  ? 772  ASN A CB  1 
ATOM   5640 C CG  . ASN A 1 746 ? -99.567  -24.011 35.720  1.00 79.59  ? 772  ASN A CG  1 
ATOM   5641 O OD1 . ASN A 1 746 ? -100.004 -23.303 36.624  1.00 81.19  ? 772  ASN A OD1 1 
ATOM   5642 N ND2 . ASN A 1 746 ? -98.710  -23.567 34.813  1.00 81.96  ? 772  ASN A ND2 1 
ATOM   5643 N N   . PRO A 1 747 ? -99.513  -28.271 37.118  1.00 79.09  ? 773  PRO A N   1 
ATOM   5644 C CA  . PRO A 1 747 ? -99.919  -29.644 37.258  1.00 84.93  ? 773  PRO A CA  1 
ATOM   5645 C C   . PRO A 1 747 ? -101.405 -29.808 36.822  1.00 89.06  ? 773  PRO A C   1 
ATOM   5646 O O   . PRO A 1 747 ? -102.318 -29.911 37.658  1.00 87.04  ? 773  PRO A O   1 
ATOM   5647 C CB  . PRO A 1 747 ? -99.725  -29.885 38.758  1.00 70.12  ? 773  PRO A CB  1 
ATOM   5648 C CG  . PRO A 1 747 ? -100.084 -28.569 39.381  1.00 76.41  ? 773  PRO A CG  1 
ATOM   5649 C CD  . PRO A 1 747 ? -99.840  -27.500 38.334  1.00 81.81  ? 773  PRO A CD  1 
ATOM   5650 N N   . PHE A 1 748 ? -101.635 -29.786 35.515  1.00 92.37  ? 774  PHE A N   1 
ATOM   5651 C CA  . PHE A 1 748 ? -102.988 -29.921 34.970  1.00 92.03  ? 774  PHE A CA  1 
ATOM   5652 C C   . PHE A 1 748 ? -103.649 -31.281 35.179  1.00 86.71  ? 774  PHE A C   1 
ATOM   5653 O O   . PHE A 1 748 ? -103.038 -32.324 34.909  1.00 75.04  ? 774  PHE A O   1 
ATOM   5654 C CB  . PHE A 1 748 ? -102.988 -29.646 33.479  1.00 87.13  ? 774  PHE A CB  1 
ATOM   5655 C CG  . PHE A 1 748 ? -102.718 -28.232 33.128  1.00 79.42  ? 774  PHE A CG  1 
ATOM   5656 C CD1 . PHE A 1 748 ? -103.737 -27.302 33.172  1.00 83.51  ? 774  PHE A CD1 1 
ATOM   5657 C CD2 . PHE A 1 748 ? -101.495 -27.855 32.639  1.00 86.16  ? 774  PHE A CD2 1 
ATOM   5658 C CE1 . PHE A 1 748 ? -103.516 -25.993 32.805  1.00 88.93  ? 774  PHE A CE1 1 
ATOM   5659 C CE2 . PHE A 1 748 ? -101.259 -26.549 32.275  1.00 85.96  ? 774  PHE A CE2 1 
ATOM   5660 C CZ  . PHE A 1 748 ? -102.272 -25.617 32.355  1.00 92.00  ? 774  PHE A CZ  1 
ATOM   5661 N N   . GLU A 1 749 ? -104.918 -31.249 35.596  1.00 78.93  ? 775  GLU A N   1 
ATOM   5662 C CA  . GLU A 1 749 ? -105.722 -32.463 35.826  1.00 102.38 ? 775  GLU A CA  1 
ATOM   5663 C C   . GLU A 1 749 ? -106.476 -32.793 34.510  1.00 109.80 ? 775  GLU A C   1 
ATOM   5664 O O   . GLU A 1 749 ? -107.472 -32.132 34.135  1.00 85.13  ? 775  GLU A O   1 
ATOM   5665 C CB  . GLU A 1 749 ? -106.685 -32.252 37.002  1.00 107.30 ? 775  GLU A CB  1 
ATOM   5666 C CG  . GLU A 1 749 ? -107.487 -33.485 37.391  1.00 118.81 ? 775  GLU A CG  1 
ATOM   5667 C CD  . GLU A 1 749 ? -108.282 -33.299 38.677  1.00 127.36 ? 775  GLU A CD  1 
ATOM   5668 O OE1 . GLU A 1 749 ? -108.644 -34.319 39.290  1.00 146.57 ? 775  GLU A OE1 1 
ATOM   5669 O OE2 . GLU A 1 749 ? -108.464 -32.149 39.131  1.00 121.77 ? 775  GLU A OE2 1 
ATOM   5670 N N   . CYS A 1 750 ? -105.957 -33.790 33.794  1.00 104.52 ? 776  CYS A N   1 
ATOM   5671 C CA  . CYS A 1 750 ? -106.521 -34.203 32.511  1.00 113.95 ? 776  CYS A CA  1 
ATOM   5672 C C   . CYS A 1 750 ? -107.762 -35.109 32.513  1.00 111.00 ? 776  CYS A C   1 
ATOM   5673 O O   . CYS A 1 750 ? -107.765 -36.194 31.935  1.00 94.98  ? 776  CYS A O   1 
ATOM   5674 C CB  . CYS A 1 750 ? -105.415 -34.736 31.595  1.00 108.31 ? 776  CYS A CB  1 
ATOM   5675 S SG  . CYS A 1 750 ? -104.323 -33.390 31.080  1.00 99.87  ? 776  CYS A SG  1 
ATOM   5676 N N   . THR A 1 751 ? -108.805 -34.647 33.194  1.00 104.20 ? 777  THR A N   1 
ATOM   5677 C CA  . THR A 1 751 ? -110.064 -35.342 33.232  1.00 103.60 ? 777  THR A CA  1 
ATOM   5678 C C   . THR A 1 751 ? -110.819 -34.595 32.140  1.00 116.28 ? 777  THR A C   1 
ATOM   5679 O O   . THR A 1 751 ? -110.255 -33.698 31.508  1.00 116.55 ? 777  THR A O   1 
ATOM   5680 C CB  . THR A 1 751 ? -110.797 -35.212 34.592  1.00 109.67 ? 777  THR A CB  1 
ATOM   5681 O OG1 . THR A 1 751 ? -111.096 -33.839 34.872  1.00 113.79 ? 777  THR A OG1 1 
ATOM   5682 C CG2 . THR A 1 751 ? -109.959 -35.781 35.716  1.00 113.23 ? 777  THR A CG2 1 
ATOM   5683 N N   . CYS A 1 752 ? -112.080 -34.927 31.914  1.00 132.43 ? 778  CYS A N   1 
ATOM   5684 C CA  . CYS A 1 752 ? -112.839 -34.239 30.874  1.00 137.65 ? 778  CYS A CA  1 
ATOM   5685 C C   . CYS A 1 752 ? -113.012 -32.733 31.119  1.00 130.42 ? 778  CYS A C   1 
ATOM   5686 O O   . CYS A 1 752 ? -113.415 -32.000 30.207  1.00 132.11 ? 778  CYS A O   1 
ATOM   5687 C CB  . CYS A 1 752 ? -114.166 -34.956 30.584  1.00 146.05 ? 778  CYS A CB  1 
ATOM   5688 S SG  . CYS A 1 752 ? -113.960 -36.512 29.658  1.00 121.43 ? 778  CYS A SG  1 
ATOM   5689 N N   . ASP A 1 753 ? -112.644 -32.275 32.323  1.00 133.14 ? 779  ASP A N   1 
ATOM   5690 C CA  . ASP A 1 753 ? -112.719 -30.846 32.698  1.00 121.86 ? 779  ASP A CA  1 
ATOM   5691 C C   . ASP A 1 753 ? -111.717 -30.022 31.906  1.00 113.47 ? 779  ASP A C   1 
ATOM   5692 O O   . ASP A 1 753 ? -111.807 -28.800 31.867  1.00 102.13 ? 779  ASP A O   1 
ATOM   5693 C CB  . ASP A 1 753 ? -112.422 -30.651 34.189  1.00 124.41 ? 779  ASP A CB  1 
ATOM   5694 C CG  . ASP A 1 753 ? -113.488 -31.240 35.085  1.00 128.76 ? 779  ASP A CG  1 
ATOM   5695 O OD1 . ASP A 1 753 ? -114.672 -31.210 34.699  1.00 144.41 ? 779  ASP A OD1 1 
ATOM   5696 O OD2 . ASP A 1 753 ? -113.160 -31.623 36.226  1.00 120.28 ? 779  ASP A OD2 1 
ATOM   5697 N N   . ILE A 1 754 ? -110.756 -30.699 31.282  1.00 111.11 ? 780  ILE A N   1 
ATOM   5698 C CA  . ILE A 1 754 ? -109.743 -30.028 30.494  1.00 99.53  ? 780  ILE A CA  1 
ATOM   5699 C C   . ILE A 1 754 ? -110.344 -29.701 29.133  1.00 100.54 ? 780  ILE A C   1 
ATOM   5700 O O   . ILE A 1 754 ? -109.619 -29.454 28.173  1.00 101.57 ? 780  ILE A O   1 
ATOM   5701 C CB  . ILE A 1 754 ? -108.522 -30.947 30.277  1.00 106.71 ? 780  ILE A CB  1 
ATOM   5702 C CG1 . ILE A 1 754 ? -107.248 -30.129 30.073  1.00 110.91 ? 780  ILE A CG1 1 
ATOM   5703 C CG2 . ILE A 1 754 ? -108.791 -31.980 29.189  1.00 106.93 ? 780  ILE A CG2 1 
ATOM   5704 C CD1 . ILE A 1 754 ? -106.881 -29.309 31.294  1.00 109.92 ? 780  ILE A CD1 1 
ATOM   5705 N N   . GLY A 1 755 ? -111.676 -29.702 29.059  1.00 92.22  ? 781  GLY A N   1 
ATOM   5706 C CA  . GLY A 1 755 ? -112.378 -29.431 27.823  1.00 77.96  ? 781  GLY A CA  1 
ATOM   5707 C C   . GLY A 1 755 ? -112.630 -27.966 27.557  1.00 87.41  ? 781  GLY A C   1 
ATOM   5708 O O   . GLY A 1 755 ? -112.385 -27.489 26.439  1.00 92.34  ? 781  GLY A O   1 
ATOM   5709 N N   . ASP A 1 756 ? -113.161 -27.255 28.557  1.00 94.32  ? 782  ASP A N   1 
ATOM   5710 C CA  . ASP A 1 756 ? -113.449 -25.814 28.410  1.00 110.68 ? 782  ASP A CA  1 
ATOM   5711 C C   . ASP A 1 756 ? -112.200 -25.117 27.911  1.00 115.58 ? 782  ASP A C   1 
ATOM   5712 O O   . ASP A 1 756 ? -112.240 -24.330 26.963  1.00 114.78 ? 782  ASP A O   1 
ATOM   5713 C CB  . ASP A 1 756 ? -113.834 -25.152 29.745  1.00 120.52 ? 782  ASP A CB  1 
ATOM   5714 C CG  . ASP A 1 756 ? -115.065 -25.752 30.380  1.00 119.41 ? 782  ASP A CG  1 
ATOM   5715 O OD1 . ASP A 1 756 ? -115.381 -26.928 30.117  1.00 130.07 ? 782  ASP A OD1 1 
ATOM   5716 O OD2 . ASP A 1 756 ? -115.658 -25.061 31.231  1.00 129.35 ? 782  ASP A OD2 1 
ATOM   5717 N N   . PHE A 1 757 ? -111.099 -25.363 28.613  1.00 106.22 ? 783  PHE A N   1 
ATOM   5718 C CA  . PHE A 1 757 ? -109.837 -24.777 28.250  1.00 115.11 ? 783  PHE A CA  1 
ATOM   5719 C C   . PHE A 1 757 ? -109.388 -25.316 26.897  1.00 109.82 ? 783  PHE A C   1 
ATOM   5720 O O   . PHE A 1 757 ? -109.134 -24.548 25.971  1.00 123.58 ? 783  PHE A O   1 
ATOM   5721 C CB  . PHE A 1 757 ? -108.776 -25.013 29.338  1.00 119.74 ? 783  PHE A CB  1 
ATOM   5722 C CG  . PHE A 1 757 ? -107.404 -24.551 28.940  1.00 113.08 ? 783  PHE A CG  1 
ATOM   5723 C CD1 . PHE A 1 757 ? -107.115 -23.190 28.852  1.00 100.93 ? 783  PHE A CD1 1 
ATOM   5724 C CD2 . PHE A 1 757 ? -106.399 -25.469 28.666  1.00 98.77  ? 783  PHE A CD2 1 
ATOM   5725 C CE1 . PHE A 1 757 ? -105.873 -22.760 28.444  1.00 86.84  ? 783  PHE A CE1 1 
ATOM   5726 C CE2 . PHE A 1 757 ? -105.148 -25.037 28.275  1.00 101.53 ? 783  PHE A CE2 1 
ATOM   5727 C CZ  . PHE A 1 757 ? -104.885 -23.684 28.165  1.00 95.91  ? 783  PHE A CZ  1 
ATOM   5728 N N   . ARG A 1 758 ? -109.312 -26.634 26.774  1.00 105.84 ? 784  ARG A N   1 
ATOM   5729 C CA  . ARG A 1 758 ? -108.903 -27.242 25.515  1.00 105.84 ? 784  ARG A CA  1 
ATOM   5730 C C   . ARG A 1 758 ? -109.650 -26.565 24.372  1.00 109.32 ? 784  ARG A C   1 
ATOM   5731 O O   . ARG A 1 758 ? -109.107 -26.356 23.271  1.00 94.26  ? 784  ARG A O   1 
ATOM   5732 C CB  . ARG A 1 758 ? -109.186 -28.727 25.543  1.00 113.33 ? 784  ARG A CB  1 
ATOM   5733 C CG  . ARG A 1 758 ? -108.884 -29.416 24.242  1.00 123.35 ? 784  ARG A CG  1 
ATOM   5734 C CD  . ARG A 1 758 ? -107.494 -29.070 23.771  1.00 113.46 ? 784  ARG A CD  1 
ATOM   5735 N NE  . ARG A 1 758 ? -107.106 -29.989 22.729  1.00 133.16 ? 784  ARG A NE  1 
ATOM   5736 C CZ  . ARG A 1 758 ? -106.603 -31.187 22.985  1.00 140.14 ? 784  ARG A CZ  1 
ATOM   5737 N NH1 . ARG A 1 758 ? -106.266 -32.001 21.995  1.00 143.83 ? 784  ARG A NH1 1 
ATOM   5738 N NH2 . ARG A 1 758 ? -106.456 -31.578 24.248  1.00 132.47 ? 784  ARG A NH2 1 
ATOM   5739 N N   . ARG A 1 759 ? -110.925 -26.293 24.627  1.00 101.62 ? 785  ARG A N   1 
ATOM   5740 C CA  . ARG A 1 759 ? -111.760 -25.598 23.679  1.00 114.28 ? 785  ARG A CA  1 
ATOM   5741 C C   . ARG A 1 759 ? -111.107 -24.259 23.366  1.00 118.37 ? 785  ARG A C   1 
ATOM   5742 O O   . ARG A 1 759 ? -110.683 -23.993 22.235  1.00 115.68 ? 785  ARG A O   1 
ATOM   5743 C CB  . ARG A 1 759 ? -113.137 -25.324 24.291  1.00 120.59 ? 785  ARG A CB  1 
ATOM   5744 C CG  . ARG A 1 759 ? -113.863 -24.218 23.554  1.00 131.01 ? 785  ARG A CG  1 
ATOM   5745 C CD  . ARG A 1 759 ? -115.151 -23.739 24.202  1.00 135.78 ? 785  ARG A CD  1 
ATOM   5746 N NE  . ARG A 1 759 ? -116.276 -24.644 24.012  1.00 141.33 ? 785  ARG A NE  1 
ATOM   5747 C CZ  . ARG A 1 759 ? -116.968 -24.730 22.875  1.00 132.37 ? 785  ARG A CZ  1 
ATOM   5748 N NH1 . ARG A 1 759 ? -118.021 -25.529 22.802  1.00 117.26 ? 785  ARG A NH1 1 
ATOM   5749 N NH2 . ARG A 1 759 ? -116.607 -24.016 21.803  1.00 118.76 ? 785  ARG A NH2 1 
ATOM   5750 N N   . TRP A 1 760 ? -111.015 -23.441 24.414  1.00 122.26 ? 786  TRP A N   1 
ATOM   5751 C CA  . TRP A 1 760 ? -110.446 -22.102 24.358  1.00 107.00 ? 786  TRP A CA  1 
ATOM   5752 C C   . TRP A 1 760 ? -109.307 -21.923 23.387  1.00 105.33 ? 786  TRP A C   1 
ATOM   5753 O O   . TRP A 1 760 ? -109.296 -20.963 22.616  1.00 93.80  ? 786  TRP A O   1 
ATOM   5754 C CB  . TRP A 1 760 ? -109.889 -21.724 25.731  1.00 117.38 ? 786  TRP A CB  1 
ATOM   5755 C CG  . TRP A 1 760 ? -109.307 -20.355 25.753  1.00 120.11 ? 786  TRP A CG  1 
ATOM   5756 C CD1 . TRP A 1 760 ? -108.042 -19.973 25.374  1.00 106.22 ? 786  TRP A CD1 1 
ATOM   5757 C CD2 . TRP A 1 760 ? -109.967 -19.180 26.186  1.00 125.60 ? 786  TRP A CD2 1 
ATOM   5758 N NE1 . TRP A 1 760 ? -107.904 -18.615 25.503  1.00 105.03 ? 786  TRP A NE1 1 
ATOM   5759 C CE2 . TRP A 1 760 ? -109.069 -18.105 26.014  1.00 121.67 ? 786  TRP A CE2 1 
ATOM   5760 C CE3 . TRP A 1 760 ? -111.234 -18.927 26.707  1.00 122.91 ? 786  TRP A CE3 1 
ATOM   5761 C CZ2 . TRP A 1 760 ? -109.401 -16.805 26.351  1.00 135.20 ? 786  TRP A CZ2 1 
ATOM   5762 C CZ3 . TRP A 1 760 ? -111.562 -17.654 27.019  1.00 138.89 ? 786  TRP A CZ3 1 
ATOM   5763 C CH2 . TRP A 1 760 ? -110.647 -16.597 26.855  1.00 149.26 ? 786  TRP A CH2 1 
ATOM   5764 N N   . MET A 1 761 ? -108.336 -22.835 23.451  1.00 104.84 ? 787  MET A N   1 
ATOM   5765 C CA  . MET A 1 761 ? -107.133 -22.742 22.622  1.00 115.86 ? 787  MET A CA  1 
ATOM   5766 C C   . MET A 1 761 ? -107.485 -22.943 21.168  1.00 122.02 ? 787  MET A C   1 
ATOM   5767 O O   . MET A 1 761 ? -107.033 -22.198 20.301  1.00 131.09 ? 787  MET A O   1 
ATOM   5768 C CB  . MET A 1 761 ? -106.120 -23.832 22.973  1.00 116.82 ? 787  MET A CB  1 
ATOM   5769 C CG  . MET A 1 761 ? -106.207 -24.401 24.378  1.00 120.05 ? 787  MET A CG  1 
ATOM   5770 S SD  . MET A 1 761 ? -104.691 -25.241 24.866  1.00 119.55 ? 787  MET A SD  1 
ATOM   5771 C CE  . MET A 1 761 ? -104.122 -25.909 23.301  1.00 117.28 ? 787  MET A CE  1 
ATOM   5772 N N   . ASP A 1 762 ? -108.257 -23.997 20.915  1.00 131.65 ? 788  ASP A N   1 
ATOM   5773 C CA  . ASP A 1 762 ? -108.681 -24.355 19.570  1.00 131.54 ? 788  ASP A CA  1 
ATOM   5774 C C   . ASP A 1 762 ? -109.257 -23.109 18.890  1.00 122.60 ? 788  ASP A C   1 
ATOM   5775 O O   . ASP A 1 762 ? -108.873 -22.765 17.773  1.00 106.30 ? 788  ASP A O   1 
ATOM   5776 C CB  . ASP A 1 762 ? -109.715 -25.484 19.641  1.00 141.57 ? 788  ASP A CB  1 
ATOM   5777 C CG  . ASP A 1 762 ? -109.948 -26.162 18.298  1.00 158.86 ? 788  ASP A CG  1 
ATOM   5778 O OD1 . ASP A 1 762 ? -109.361 -25.726 17.284  1.00 172.03 ? 788  ASP A OD1 1 
ATOM   5779 O OD2 . ASP A 1 762 ? -110.690 -27.168 18.269  1.00 159.77 ? 788  ASP A OD2 1 
ATOM   5780 N N   . GLU A 1 763 ? -110.146 -22.414 19.593  1.00 109.35 ? 789  GLU A N   1 
ATOM   5781 C CA  . GLU A 1 763 ? -110.750 -21.191 19.071  1.00 119.94 ? 789  GLU A CA  1 
ATOM   5782 C C   . GLU A 1 763 ? -109.748 -20.040 18.856  1.00 138.66 ? 789  GLU A C   1 
ATOM   5783 O O   . GLU A 1 763 ? -109.763 -19.384 17.814  1.00 131.75 ? 789  GLU A O   1 
ATOM   5784 C CB  . GLU A 1 763 ? -111.844 -20.704 20.014  1.00 111.10 ? 789  GLU A CB  1 
ATOM   5785 C CG  . GLU A 1 763 ? -113.047 -21.615 20.091  1.00 118.78 ? 789  GLU A CG  1 
ATOM   5786 C CD  . GLU A 1 763 ? -114.118 -21.067 21.014  1.00 125.80 ? 789  GLU A CD  1 
ATOM   5787 O OE1 . GLU A 1 763 ? -113.769 -20.266 21.908  1.00 125.50 ? 789  GLU A OE1 1 
ATOM   5788 O OE2 . GLU A 1 763 ? -115.299 -21.466 20.875  1.00 109.55 ? 789  GLU A OE2 1 
ATOM   5789 N N   . HIS A 1 764 ? -108.863 -19.818 19.825  1.00 146.92 ? 790  HIS A N   1 
ATOM   5790 C CA  . HIS A 1 764 ? -107.900 -18.725 19.733  1.00 131.36 ? 790  HIS A CA  1 
ATOM   5791 C C   . HIS A 1 764 ? -106.469 -19.115 19.355  1.00 133.14 ? 790  HIS A C   1 
ATOM   5792 O O   . HIS A 1 764 ? -105.628 -19.268 20.239  1.00 135.47 ? 790  HIS A O   1 
ATOM   5793 C CB  . HIS A 1 764 ? -107.831 -17.993 21.076  1.00 125.99 ? 790  HIS A CB  1 
ATOM   5794 C CG  . HIS A 1 764 ? -109.149 -17.486 21.568  1.00 119.68 ? 790  HIS A CG  1 
ATOM   5795 N ND1 . HIS A 1 764 ? -109.960 -18.226 22.401  1.00 114.57 ? 790  HIS A ND1 1 
ATOM   5796 C CD2 . HIS A 1 764 ? -109.763 -16.292 21.406  1.00 116.95 ? 790  HIS A CD2 1 
ATOM   5797 C CE1 . HIS A 1 764 ? -111.024 -17.513 22.721  1.00 117.48 ? 790  HIS A CE1 1 
ATOM   5798 N NE2 . HIS A 1 764 ? -110.931 -16.338 22.126  1.00 120.16 ? 790  HIS A NE2 1 
ATOM   5799 N N   . LEU A 1 765 ? -106.184 -19.287 18.062  1.00 143.30 ? 791  LEU A N   1 
ATOM   5800 C CA  . LEU A 1 765 ? -104.800 -19.598 17.635  1.00 140.94 ? 791  LEU A CA  1 
ATOM   5801 C C   . LEU A 1 765 ? -104.061 -18.250 17.525  1.00 130.79 ? 791  LEU A C   1 
ATOM   5802 O O   . LEU A 1 765 ? -102.874 -18.182 17.160  1.00 106.84 ? 791  LEU A O   1 
ATOM   5803 C CB  . LEU A 1 765 ? -104.719 -20.394 16.311  1.00 141.21 ? 791  LEU A CB  1 
ATOM   5804 C CG  . LEU A 1 765 ? -105.219 -21.852 16.272  1.00 131.89 ? 791  LEU A CG  1 
ATOM   5805 C CD1 . LEU A 1 765 ? -106.711 -21.932 16.535  1.00 119.41 ? 791  LEU A CD1 1 
ATOM   5806 C CD2 . LEU A 1 765 ? -104.892 -22.510 14.936  1.00 124.45 ? 791  LEU A CD2 1 
ATOM   5807 N N   . ASN A 1 766 ? -104.804 -17.187 17.847  1.00 105.97 ? 792  ASN A N   1 
ATOM   5808 C CA  . ASN A 1 766 ? -104.313 -15.814 17.839  1.00 118.32 ? 792  ASN A CA  1 
ATOM   5809 C C   . ASN A 1 766 ? -103.513 -15.446 19.116  1.00 121.35 ? 792  ASN A C   1 
ATOM   5810 O O   . ASN A 1 766 ? -102.873 -14.391 19.177  1.00 117.53 ? 792  ASN A O   1 
ATOM   5811 C CB  . ASN A 1 766 ? -105.500 -14.846 17.637  1.00 111.34 ? 792  ASN A CB  1 
ATOM   5812 C CG  . ASN A 1 766 ? -106.678 -15.161 18.555  1.00 120.82 ? 792  ASN A CG  1 
ATOM   5813 O OD1 . ASN A 1 766 ? -106.941 -16.330 18.859  1.00 103.90 ? 792  ASN A OD1 1 
ATOM   5814 N ND2 . ASN A 1 766 ? -107.461 -14.138 18.899  1.00 116.74 ? 792  ASN A ND2 1 
ATOM   5815 N N   . VAL A 1 767 ? -103.552 -16.324 20.119  1.00 112.28 ? 793  VAL A N   1 
ATOM   5816 C CA  . VAL A 1 767 ? -102.846 -16.110 21.381  1.00 93.87  ? 793  VAL A CA  1 
ATOM   5817 C C   . VAL A 1 767 ? -101.718 -17.140 21.485  1.00 96.10  ? 793  VAL A C   1 
ATOM   5818 O O   . VAL A 1 767 ? -101.967 -18.325 21.671  1.00 97.28  ? 793  VAL A O   1 
ATOM   5819 C CB  . VAL A 1 767 ? -103.790 -16.264 22.596  1.00 92.23  ? 793  VAL A CB  1 
ATOM   5820 C CG1 . VAL A 1 767 ? -105.014 -15.369 22.443  1.00 83.54  ? 793  VAL A CG1 1 
ATOM   5821 C CG2 . VAL A 1 767 ? -104.249 -17.702 22.762  1.00 104.55 ? 793  VAL A CG2 1 
ATOM   5822 N N   . LYS A 1 768 ? -100.481 -16.698 21.313  1.00 93.38  ? 794  LYS A N   1 
ATOM   5823 C CA  . LYS A 1 768 ? -99.343  -17.600 21.386  1.00 95.91  ? 794  LYS A CA  1 
ATOM   5824 C C   . LYS A 1 768 ? -99.265  -18.278 22.758  1.00 97.06  ? 794  LYS A C   1 
ATOM   5825 O O   . LYS A 1 768 ? -99.542  -17.664 23.788  1.00 106.97 ? 794  LYS A O   1 
ATOM   5826 C CB  . LYS A 1 768 ? -98.042  -16.825 21.135  1.00 115.22 ? 794  LYS A CB  1 
ATOM   5827 C CG  . LYS A 1 768 ? -96.762  -17.662 21.209  1.00 122.97 ? 794  LYS A CG  1 
ATOM   5828 C CD  . LYS A 1 768 ? -96.642  -18.679 20.083  1.00 133.44 ? 794  LYS A CD  1 
ATOM   5829 C CE  . LYS A 1 768 ? -96.542  -17.992 18.721  1.00 140.54 ? 794  LYS A CE  1 
ATOM   5830 N NZ  . LYS A 1 768 ? -96.371  -18.952 17.593  1.00 131.82 ? 794  LYS A NZ  1 
ATOM   5831 N N   . ILE A 1 769 ? -98.927  -19.559 22.752  1.00 90.88  ? 795  ILE A N   1 
ATOM   5832 C CA  . ILE A 1 769 ? -98.774  -20.330 23.975  1.00 87.63  ? 795  ILE A CA  1 
ATOM   5833 C C   . ILE A 1 769 ? -97.430  -21.010 23.808  1.00 87.71  ? 795  ILE A C   1 
ATOM   5834 O O   . ILE A 1 769 ? -97.353  -22.184 23.460  1.00 97.79  ? 795  ILE A O   1 
ATOM   5835 C CB  . ILE A 1 769 ? -99.853  -21.416 24.162  1.00 95.05  ? 795  ILE A CB  1 
ATOM   5836 C CG1 . ILE A 1 769 ? -101.270 -20.828 24.137  1.00 96.11  ? 795  ILE A CG1 1 
ATOM   5837 C CG2 . ILE A 1 769 ? -99.619  -22.164 25.472  1.00 96.96  ? 795  ILE A CG2 1 
ATOM   5838 C CD1 . ILE A 1 769 ? -101.583 -19.874 25.263  1.00 109.67 ? 795  ILE A CD1 1 
ATOM   5839 N N   . PRO A 1 770 ? -96.357  -20.269 24.052  1.00 88.17  ? 796  PRO A N   1 
ATOM   5840 C CA  . PRO A 1 770 ? -95.077  -20.907 23.875  1.00 79.10  ? 796  PRO A CA  1 
ATOM   5841 C C   . PRO A 1 770 ? -94.942  -22.171 24.690  1.00 90.17  ? 796  PRO A C   1 
ATOM   5842 O O   . PRO A 1 770 ? -95.473  -22.275 25.800  1.00 105.05 ? 796  PRO A O   1 
ATOM   5843 C CB  . PRO A 1 770 ? -94.087  -19.852 24.357  1.00 89.25  ? 796  PRO A CB  1 
ATOM   5844 C CG  . PRO A 1 770 ? -94.868  -18.907 25.223  1.00 87.42  ? 796  PRO A CG  1 
ATOM   5845 C CD  . PRO A 1 770 ? -96.323  -19.215 25.077  1.00 92.84  ? 796  PRO A CD  1 
ATOM   5846 N N   . ARG A 1 771 ? -94.300  -23.157 24.101  1.00 99.17  ? 797  ARG A N   1 
ATOM   5847 C CA  . ARG A 1 771 ? -94.072  -24.423 24.764  1.00 110.71 ? 797  ARG A CA  1 
ATOM   5848 C C   . ARG A 1 771 ? -95.340  -25.219 25.090  1.00 116.48 ? 797  ARG A C   1 
ATOM   5849 O O   . ARG A 1 771 ? -95.545  -25.599 26.237  1.00 129.35 ? 797  ARG A O   1 
ATOM   5850 C CB  . ARG A 1 771 ? -93.217  -24.207 26.026  1.00 108.04 ? 797  ARG A CB  1 
ATOM   5851 C CG  . ARG A 1 771 ? -91.866  -23.556 25.725  1.00 114.77 ? 797  ARG A CG  1 
ATOM   5852 C CD  . ARG A 1 771 ? -91.041  -23.223 26.968  1.00 111.16 ? 797  ARG A CD  1 
ATOM   5853 N NE  . ARG A 1 771 ? -90.578  -24.388 27.721  1.00 109.64 ? 797  ARG A NE  1 
ATOM   5854 C CZ  . ARG A 1 771 ? -89.874  -24.317 28.854  1.00 115.13 ? 797  ARG A CZ  1 
ATOM   5855 N NH1 . ARG A 1 771 ? -89.565  -23.138 29.385  1.00 126.93 ? 797  ARG A NH1 1 
ATOM   5856 N NH2 . ARG A 1 771 ? -89.494  -25.426 29.472  1.00 109.56 ? 797  ARG A NH2 1 
ATOM   5857 N N   . LEU A 1 772 ? -96.203  -25.440 24.093  1.00 114.82 ? 798  LEU A N   1 
ATOM   5858 C CA  . LEU A 1 772 ? -97.413  -26.257 24.299  1.00 94.60  ? 798  LEU A CA  1 
ATOM   5859 C C   . LEU A 1 772 ? -96.932  -27.641 24.613  1.00 88.30  ? 798  LEU A C   1 
ATOM   5860 O O   . LEU A 1 772 ? -97.571  -28.392 25.339  1.00 88.02  ? 798  LEU A O   1 
ATOM   5861 C CB  . LEU A 1 772 ? -98.265  -26.330 23.045  1.00 101.46 ? 798  LEU A CB  1 
ATOM   5862 C CG  . LEU A 1 772 ? -99.055  -25.082 22.699  1.00 119.53 ? 798  LEU A CG  1 
ATOM   5863 C CD1 . LEU A 1 772 ? -99.610  -25.159 21.288  1.00 132.04 ? 798  LEU A CD1 1 
ATOM   5864 C CD2 . LEU A 1 772 ? -100.165 -24.892 23.721  1.00 113.00 ? 798  LEU A CD2 1 
ATOM   5865 N N   . VAL A 1 773 ? -95.779  -27.966 24.049  1.00 90.85  ? 799  VAL A N   1 
ATOM   5866 C CA  . VAL A 1 773 ? -95.155  -29.252 24.248  1.00 99.17  ? 799  VAL A CA  1 
ATOM   5867 C C   . VAL A 1 773 ? -94.925  -29.493 25.743  1.00 99.86  ? 799  VAL A C   1 
ATOM   5868 O O   . VAL A 1 773 ? -95.114  -30.605 26.234  1.00 105.96 ? 799  VAL A O   1 
ATOM   5869 C CB  . VAL A 1 773 ? -93.808  -29.314 23.512  1.00 103.77 ? 799  VAL A CB  1 
ATOM   5870 C CG1 . VAL A 1 773 ? -93.203  -30.697 23.633  1.00 107.16 ? 799  VAL A CG1 1 
ATOM   5871 C CG2 . VAL A 1 773 ? -93.989  -28.972 22.041  1.00 114.27 ? 799  VAL A CG2 1 
ATOM   5872 N N   . ASP A 1 774 ? -94.534  -28.442 26.464  1.00 112.34 ? 800  ASP A N   1 
ATOM   5873 C CA  . ASP A 1 774 ? -94.278  -28.544 27.912  1.00 112.70 ? 800  ASP A CA  1 
ATOM   5874 C C   . ASP A 1 774 ? -95.518  -28.409 28.799  1.00 100.50 ? 800  ASP A C   1 
ATOM   5875 O O   . ASP A 1 774 ? -95.437  -28.670 29.995  1.00 106.39 ? 800  ASP A O   1 
ATOM   5876 C CB  . ASP A 1 774 ? -93.156  -27.593 28.352  1.00 108.18 ? 800  ASP A CB  1 
ATOM   5877 C CG  . ASP A 1 774 ? -91.778  -28.025 27.829  1.00 117.38 ? 800  ASP A CG  1 
ATOM   5878 O OD1 . ASP A 1 774 ? -91.543  -29.246 27.674  1.00 110.62 ? 800  ASP A OD1 1 
ATOM   5879 O OD2 . ASP A 1 774 ? -90.895  -27.156 27.666  1.00 132.01 ? 800  ASP A OD2 1 
ATOM   5880 N N   . VAL A 1 775 ? -96.641  -27.962 28.238  1.00 97.02  ? 801  VAL A N   1 
ATOM   5881 C CA  . VAL A 1 775 ? -97.893  -27.870 29.015  1.00 100.52 ? 801  VAL A CA  1 
ATOM   5882 C C   . VAL A 1 775 ? -98.309  -29.347 29.140  1.00 102.19 ? 801  VAL A C   1 
ATOM   5883 O O   . VAL A 1 775 ? -98.674  -29.987 28.151  1.00 102.46 ? 801  VAL A O   1 
ATOM   5884 C CB  . VAL A 1 775 ? -98.966  -27.006 28.319  1.00 94.79  ? 801  VAL A CB  1 
ATOM   5885 C CG1 . VAL A 1 775 ? -100.240 -26.984 29.132  1.00 92.26  ? 801  VAL A CG1 1 
ATOM   5886 C CG2 . VAL A 1 775 ? -98.468  -25.579 28.146  1.00 89.05  ? 801  VAL A CG2 1 
ATOM   5887 N N   . ILE A 1 776 ? -98.247  -29.873 30.361  1.00 100.28 ? 802  ILE A N   1 
ATOM   5888 C CA  . ILE A 1 776 ? -98.501  -31.287 30.614  1.00 89.68  ? 802  ILE A CA  1 
ATOM   5889 C C   . ILE A 1 776 ? -99.528  -31.689 31.663  1.00 92.40  ? 802  ILE A C   1 
ATOM   5890 O O   . ILE A 1 776 ? -99.910  -30.909 32.535  1.00 107.23 ? 802  ILE A O   1 
ATOM   5891 C CB  . ILE A 1 776 ? -97.142  -31.937 30.970  1.00 92.00  ? 802  ILE A CB  1 
ATOM   5892 C CG1 . ILE A 1 776 ? -96.243  -31.930 29.720  1.00 97.42  ? 802  ILE A CG1 1 
ATOM   5893 C CG2 . ILE A 1 776 ? -97.303  -33.351 31.498  1.00 95.01  ? 802  ILE A CG2 1 
ATOM   5894 C CD1 . ILE A 1 776 ? -94.852  -32.498 29.929  1.00 104.08 ? 802  ILE A CD1 1 
ATOM   5895 N N   . CYS A 1 777 ? -99.991  -32.930 31.521  1.00 96.52  ? 803  CYS A N   1 
ATOM   5896 C CA  . CYS A 1 777 ? -100.963 -33.529 32.418  1.00 92.98  ? 803  CYS A CA  1 
ATOM   5897 C C   . CYS A 1 777 ? -100.290 -34.070 33.659  1.00 93.66  ? 803  CYS A C   1 
ATOM   5898 O O   . CYS A 1 777 ? -99.386  -34.919 33.577  1.00 81.26  ? 803  CYS A O   1 
ATOM   5899 C CB  . CYS A 1 777 ? -101.683 -34.701 31.732  1.00 108.40 ? 803  CYS A CB  1 
ATOM   5900 S SG  . CYS A 1 777 ? -102.684 -34.298 30.287  1.00 100.09 ? 803  CYS A SG  1 
ATOM   5901 N N   . ALA A 1 778 ? -100.736 -33.578 34.807  1.00 101.87 ? 804  ALA A N   1 
ATOM   5902 C CA  . ALA A 1 778 ? -100.215 -34.013 36.095  1.00 109.90 ? 804  ALA A CA  1 
ATOM   5903 C C   . ALA A 1 778 ? -100.948 -35.281 36.485  1.00 114.82 ? 804  ALA A C   1 
ATOM   5904 O O   . ALA A 1 778 ? -100.362 -36.209 37.039  1.00 126.25 ? 804  ALA A O   1 
ATOM   5905 C CB  . ALA A 1 778 ? -100.453 -32.941 37.144  1.00 106.05 ? 804  ALA A CB  1 
ATOM   5906 N N   . SER A 1 779 ? -102.246 -35.296 36.194  1.00 114.43 ? 805  SER A N   1 
ATOM   5907 C CA  . SER A 1 779 ? -103.100 -36.430 36.500  1.00 109.05 ? 805  SER A CA  1 
ATOM   5908 C C   . SER A 1 779 ? -104.237 -36.524 35.469  1.00 116.56 ? 805  SER A C   1 
ATOM   5909 O O   . SER A 1 779 ? -104.530 -35.540 34.782  1.00 105.30 ? 805  SER A O   1 
ATOM   5910 C CB  . SER A 1 779 ? -103.674 -36.267 37.903  1.00 95.03  ? 805  SER A CB  1 
ATOM   5911 O OG  . SER A 1 779 ? -104.499 -35.121 37.974  1.00 89.18  ? 805  SER A OG  1 
ATOM   5912 N N   . PRO A 1 780 ? -104.895 -37.688 35.383  1.00 125.37 ? 806  PRO A N   1 
ATOM   5913 C CA  . PRO A 1 780 ? -104.575 -38.845 36.233  1.00 112.69 ? 806  PRO A CA  1 
ATOM   5914 C C   . PRO A 1 780 ? -103.533 -39.813 35.647  1.00 110.35 ? 806  PRO A C   1 
ATOM   5915 O O   . PRO A 1 780 ? -103.158 -39.707 34.480  1.00 103.88 ? 806  PRO A O   1 
ATOM   5916 C CB  . PRO A 1 780 ? -105.934 -39.543 36.413  1.00 118.66 ? 806  PRO A CB  1 
ATOM   5917 C CG  . PRO A 1 780 ? -106.950 -38.689 35.698  1.00 116.46 ? 806  PRO A CG  1 
ATOM   5918 C CD  . PRO A 1 780 ? -106.190 -37.868 34.709  1.00 118.11 ? 806  PRO A CD  1 
ATOM   5919 N N   . GLY A 1 781 ? -103.222 -40.891 36.338  1.00 111.32 ? 807  GLY A N   1 
ATOM   5920 C CA  . GLY A 1 781 ? -102.007 -41.614 36.042  1.00 101.39 ? 807  GLY A CA  1 
ATOM   5921 C C   . GLY A 1 781 ? -101.840 -42.103 34.620  1.00 107.01 ? 807  GLY A C   1 
ATOM   5922 O O   . GLY A 1 781 ? -100.763 -41.980 34.076  1.00 105.64 ? 807  GLY A O   1 
ATOM   5923 N N   . ASP A 1 782 ? -102.888 -42.604 34.001  1.00 128.29 ? 808  ASP A N   1 
ATOM   5924 C CA  . ASP A 1 782 ? -102.743 -42.996 32.616  1.00 134.66 ? 808  ASP A CA  1 
ATOM   5925 C C   . ASP A 1 782 ? -102.411 -41.740 31.856  1.00 122.63 ? 808  ASP A C   1 
ATOM   5926 O O   . ASP A 1 782 ? -101.613 -41.746 30.931  1.00 120.28 ? 808  ASP A O   1 
ATOM   5927 C CB  . ASP A 1 782 ? -104.013 -43.650 32.062  1.00 136.25 ? 808  ASP A CB  1 
ATOM   5928 C CG  . ASP A 1 782 ? -105.258 -43.241 32.809  1.00 144.00 ? 808  ASP A CG  1 
ATOM   5929 O OD1 . ASP A 1 782 ? -105.287 -43.391 34.047  1.00 145.54 ? 808  ASP A OD1 1 
ATOM   5930 O OD2 . ASP A 1 782 ? -106.212 -42.773 32.154  1.00 132.37 ? 808  ASP A OD2 1 
ATOM   5931 N N   . GLN A 1 783 ? -103.067 -40.665 32.252  1.00 125.28 ? 809  GLN A N   1 
ATOM   5932 C CA  . GLN A 1 783 ? -102.868 -39.360 31.654  1.00 134.98 ? 809  GLN A CA  1 
ATOM   5933 C C   . GLN A 1 783 ? -101.491 -38.746 31.857  1.00 134.15 ? 809  GLN A C   1 
ATOM   5934 O O   . GLN A 1 783 ? -100.968 -38.083 30.974  1.00 124.89 ? 809  GLN A O   1 
ATOM   5935 C CB  . GLN A 1 783 ? -103.954 -38.399 32.101  1.00 143.37 ? 809  GLN A CB  1 
ATOM   5936 C CG  . GLN A 1 783 ? -104.797 -37.889 30.951  1.00 145.07 ? 809  GLN A CG  1 
ATOM   5937 C CD  . GLN A 1 783 ? -105.158 -38.981 29.971  1.00 142.51 ? 809  GLN A CD  1 
ATOM   5938 O OE1 . GLN A 1 783 ? -104.291 -39.609 29.370  1.00 133.30 ? 809  GLN A OE1 1 
ATOM   5939 N NE2 . GLN A 1 783 ? -106.448 -39.213 29.805  1.00 140.42 ? 809  GLN A NE2 1 
ATOM   5940 N N   . ARG A 1 784 ? -100.901 -38.956 33.022  1.00 135.82 ? 810  ARG A N   1 
ATOM   5941 C CA  . ARG A 1 784 ? -99.752  -38.165 33.414  1.00 130.30 ? 810  ARG A CA  1 
ATOM   5942 C C   . ARG A 1 784 ? -98.635  -38.267 32.399  1.00 125.63 ? 810  ARG A C   1 
ATOM   5943 O O   . ARG A 1 784 ? -98.348  -39.326 31.862  1.00 100.77 ? 810  ARG A O   1 
ATOM   5944 C CB  . ARG A 1 784 ? -99.253  -38.568 34.807  1.00 120.76 ? 810  ARG A CB  1 
ATOM   5945 C CG  . ARG A 1 784 ? -97.831  -38.141 35.132  1.00 123.62 ? 810  ARG A CG  1 
ATOM   5946 C CD  . ARG A 1 784 ? -97.458  -38.414 36.578  1.00 126.10 ? 810  ARG A CD  1 
ATOM   5947 N NE  . ARG A 1 784 ? -97.112  -37.192 37.297  1.00 126.86 ? 810  ARG A NE  1 
ATOM   5948 C CZ  . ARG A 1 784 ? -95.911  -36.929 37.798  1.00 126.85 ? 810  ARG A CZ  1 
ATOM   5949 N NH1 . ARG A 1 784 ? -95.691  -35.791 38.433  1.00 120.10 ? 810  ARG A NH1 1 
ATOM   5950 N NH2 . ARG A 1 784 ? -94.928  -37.804 37.667  1.00 136.13 ? 810  ARG A NH2 1 
ATOM   5951 N N   . GLY A 1 785 ? -98.014  -37.120 32.161  1.00 112.71 ? 811  GLY A N   1 
ATOM   5952 C CA  . GLY A 1 785 ? -96.908  -36.990 31.244  1.00 119.18 ? 811  GLY A CA  1 
ATOM   5953 C C   . GLY A 1 785 ? -97.297  -36.647 29.829  1.00 125.59 ? 811  GLY A C   1 
ATOM   5954 O O   . GLY A 1 785 ? -96.442  -36.433 28.984  1.00 118.27 ? 811  GLY A O   1 
ATOM   5955 N N   . LYS A 1 786 ? -98.585  -36.540 29.572  1.00 130.02 ? 812  LYS A N   1 
ATOM   5956 C CA  . LYS A 1 786 ? -99.031  -36.326 28.216  1.00 137.91 ? 812  LYS A CA  1 
ATOM   5957 C C   . LYS A 1 786 ? -99.412  -34.882 28.010  1.00 119.74 ? 812  LYS A C   1 
ATOM   5958 O O   . LYS A 1 786 ? -100.120 -34.309 28.813  1.00 109.45 ? 812  LYS A O   1 
ATOM   5959 C CB  . LYS A 1 786 ? -100.210 -37.246 27.896  1.00 153.97 ? 812  LYS A CB  1 
ATOM   5960 C CG  . LYS A 1 786 ? -99.839  -38.471 27.074  1.00 156.67 ? 812  LYS A CG  1 
ATOM   5961 C CD  . LYS A 1 786 ? -101.071 -39.265 26.664  1.00 164.69 ? 812  LYS A CD  1 
ATOM   5962 C CE  . LYS A 1 786 ? -100.815 -40.113 25.425  1.00 159.11 ? 812  LYS A CE  1 
ATOM   5963 N NZ  . LYS A 1 786 ? -101.989 -40.947 25.030  1.00 151.12 ? 812  LYS A NZ  1 
ATOM   5964 N N   . SER A 1 787 ? -98.934  -34.293 26.929  1.00 106.00 ? 813  SER A N   1 
ATOM   5965 C CA  . SER A 1 787 ? -99.225  -32.908 26.661  1.00 102.45 ? 813  SER A CA  1 
ATOM   5966 C C   . SER A 1 787 ? -100.709 -32.728 26.490  1.00 99.02  ? 813  SER A C   1 
ATOM   5967 O O   . SER A 1 787 ? -101.357 -33.514 25.835  1.00 105.71 ? 813  SER A O   1 
ATOM   5968 C CB  . SER A 1 787 ? -98.521  -32.483 25.394  1.00 104.12 ? 813  SER A CB  1 
ATOM   5969 O OG  . SER A 1 787 ? -99.050  -31.265 24.938  1.00 119.32 ? 813  SER A OG  1 
ATOM   5970 N N   . ILE A 1 788 ? -101.248 -31.666 27.057  1.00 93.35  ? 814  ILE A N   1 
ATOM   5971 C CA  . ILE A 1 788 ? -102.719 -31.496 27.084  1.00 96.71  ? 814  ILE A CA  1 
ATOM   5972 C C   . ILE A 1 788 ? -103.380 -31.362 25.726  1.00 97.12  ? 814  ILE A C   1 
ATOM   5973 O O   . ILE A 1 788 ? -104.565 -31.048 25.643  1.00 102.31 ? 814  ILE A O   1 
ATOM   5974 C CB  . ILE A 1 788 ? -103.190 -30.309 27.941  1.00 105.47 ? 814  ILE A CB  1 
ATOM   5975 C CG1 . ILE A 1 788 ? -102.783 -28.987 27.296  1.00 112.35 ? 814  ILE A CG1 1 
ATOM   5976 C CG2 . ILE A 1 788 ? -102.692 -30.454 29.373  1.00 102.84 ? 814  ILE A CG2 1 
ATOM   5977 C CD1 . ILE A 1 788 ? -103.308 -27.781 28.038  1.00 114.65 ? 814  ILE A CD1 1 
ATOM   5978 N N   . VAL A 1 789 ? -102.598 -31.503 24.667  1.00 108.80 ? 815  VAL A N   1 
ATOM   5979 C CA  . VAL A 1 789 ? -103.129 -31.434 23.310  1.00 113.52 ? 815  VAL A CA  1 
ATOM   5980 C C   . VAL A 1 789 ? -102.995 -32.805 22.645  1.00 122.66 ? 815  VAL A C   1 
ATOM   5981 O O   . VAL A 1 789 ? -103.822 -33.193 21.818  1.00 123.11 ? 815  VAL A O   1 
ATOM   5982 C CB  . VAL A 1 789 ? -102.477 -30.314 22.478  1.00 97.60  ? 815  VAL A CB  1 
ATOM   5983 C CG1 . VAL A 1 789 ? -102.912 -28.960 23.008  1.00 91.59  ? 815  VAL A CG1 1 
ATOM   5984 C CG2 . VAL A 1 789 ? -100.960 -30.439 22.504  1.00 86.48  ? 815  VAL A CG2 1 
ATOM   5985 N N   . SER A 1 790 ? -102.035 -33.573 23.111  1.00 118.67 ? 816  SER A N   1 
ATOM   5986 C CA  . SER A 1 790 ? -101.841 -34.905 22.609  1.00 125.99 ? 816  SER A CA  1 
ATOM   5987 C C   . SER A 1 790 ? -103.055 -35.748 22.973  1.00 140.41 ? 816  SER A C   1 
ATOM   5988 O O   . SER A 1 790 ? -103.239 -36.855 22.466  1.00 149.52 ? 816  SER A O   1 
ATOM   5989 C CB  . SER A 1 790 ? -100.582 -35.508 23.210  1.00 132.09 ? 816  SER A CB  1 
ATOM   5990 O OG  . SER A 1 790 ? -100.547 -36.909 23.014  1.00 143.66 ? 816  SER A OG  1 
ATOM   5991 N N   . LEU A 1 791 ? -103.877 -35.241 23.876  1.00 134.07 ? 817  LEU A N   1 
ATOM   5992 C CA  . LEU A 1 791 ? -104.910 -36.046 24.486  1.00 137.77 ? 817  LEU A CA  1 
ATOM   5993 C C   . LEU A 1 791 ? -105.855 -36.665 23.488  1.00 147.52 ? 817  LEU A C   1 
ATOM   5994 O O   . LEU A 1 791 ? -106.338 -36.008 22.577  1.00 144.19 ? 817  LEU A O   1 
ATOM   5995 C CB  . LEU A 1 791 ? -105.737 -35.179 25.414  1.00 129.35 ? 817  LEU A CB  1 
ATOM   5996 C CG  . LEU A 1 791 ? -105.071 -34.900 26.742  1.00 124.28 ? 817  LEU A CG  1 
ATOM   5997 C CD1 . LEU A 1 791 ? -106.017 -34.157 27.660  1.00 109.59 ? 817  LEU A CD1 1 
ATOM   5998 C CD2 . LEU A 1 791 ? -104.638 -36.212 27.350  1.00 121.50 ? 817  LEU A CD2 1 
ATOM   5999 N N   . GLU A 1 792 ? -106.132 -37.944 23.705  1.00 156.40 ? 818  GLU A N   1 
ATOM   6000 C CA  . GLU A 1 792 ? -107.105 -38.679 22.929  1.00 144.50 ? 818  GLU A CA  1 
ATOM   6001 C C   . GLU A 1 792 ? -108.421 -38.385 23.577  1.00 133.22 ? 818  GLU A C   1 
ATOM   6002 O O   . GLU A 1 792 ? -108.974 -39.200 24.295  1.00 138.79 ? 818  GLU A O   1 
ATOM   6003 C CB  . GLU A 1 792 ? -106.826 -40.180 22.978  1.00 143.84 ? 818  GLU A CB  1 
ATOM   6004 C CG  . GLU A 1 792 ? -105.879 -40.632 24.079  1.00 145.75 ? 818  GLU A CG  1 
ATOM   6005 C CD  . GLU A 1 792 ? -106.356 -40.242 25.455  1.00 136.25 ? 818  GLU A CD  1 
ATOM   6006 O OE1 . GLU A 1 792 ? -106.796 -39.094 25.620  1.00 121.26 ? 818  GLU A OE1 1 
ATOM   6007 O OE2 . GLU A 1 792 ? -106.296 -41.086 26.366  1.00 118.69 ? 818  GLU A OE2 1 
ATOM   6008 N N   . LEU A 1 793 ? -108.920 -37.194 23.331  1.00 124.26 ? 819  LEU A N   1 
ATOM   6009 C CA  . LEU A 1 793 ? -110.088 -36.724 24.035  1.00 143.09 ? 819  LEU A CA  1 
ATOM   6010 C C   . LEU A 1 793 ? -111.288 -37.600 23.755  1.00 157.25 ? 819  LEU A C   1 
ATOM   6011 O O   . LEU A 1 793 ? -112.162 -37.781 24.601  1.00 144.13 ? 819  LEU A O   1 
ATOM   6012 C CB  . LEU A 1 793 ? -110.390 -35.288 23.654  1.00 152.24 ? 819  LEU A CB  1 
ATOM   6013 C CG  . LEU A 1 793 ? -111.218 -34.537 24.694  1.00 171.34 ? 819  LEU A CG  1 
ATOM   6014 C CD1 . LEU A 1 793 ? -110.419 -34.309 25.963  1.00 174.52 ? 819  LEU A CD1 1 
ATOM   6015 C CD2 . LEU A 1 793 ? -111.702 -33.209 24.140  1.00 175.78 ? 819  LEU A CD2 1 
ATOM   6016 N N   . THR A 1 794 ? -111.361 -38.089 22.528  1.00 166.49 ? 820  THR A N   1 
ATOM   6017 C CA  . THR A 1 794 ? -112.607 -38.705 22.031  1.00 147.49 ? 820  THR A CA  1 
ATOM   6018 C C   . THR A 1 794 ? -113.274 -39.651 23.041  1.00 151.24 ? 820  THR A C   1 
ATOM   6019 O O   . THR A 1 794 ? -114.497 -39.614 23.219  1.00 152.83 ? 820  THR A O   1 
ATOM   6020 C CB  . THR A 1 794 ? -112.375 -39.464 20.711  1.00 139.01 ? 820  THR A CB  1 
ATOM   6021 O OG1 . THR A 1 794 ? -111.457 -40.543 20.925  1.00 132.98 ? 820  THR A OG1 1 
ATOM   6022 C CG2 . THR A 1 794 ? -111.830 -38.522 19.633  1.00 138.97 ? 820  THR A CG2 1 
ATOM   6023 N N   . THR A 1 795 ? -112.461 -40.463 23.721  1.00 155.79 ? 821  THR A N   1 
ATOM   6024 C CA  . THR A 1 795 ? -112.942 -41.429 24.726  1.00 141.75 ? 821  THR A CA  1 
ATOM   6025 C C   . THR A 1 795 ? -113.761 -40.721 25.817  1.00 135.14 ? 821  THR A C   1 
ATOM   6026 O O   . THR A 1 795 ? -114.280 -41.351 26.739  1.00 113.68 ? 821  THR A O   1 
ATOM   6027 C CB  . THR A 1 795 ? -111.747 -42.129 25.415  1.00 140.30 ? 821  THR A CB  1 
ATOM   6028 O OG1 . THR A 1 795 ? -110.834 -42.623 24.428  1.00 144.90 ? 821  THR A OG1 1 
ATOM   6029 C CG2 . THR A 1 795 ? -112.212 -43.276 26.319  1.00 137.55 ? 821  THR A CG2 1 
ATOM   6030 N N   . CYS A 1 796 ? -113.874 -39.406 25.697  1.00 136.82 ? 822  CYS A N   1 
ATOM   6031 C CA  . CYS A 1 796 ? -114.592 -38.604 26.661  1.00 135.18 ? 822  CYS A CA  1 
ATOM   6032 C C   . CYS A 1 796 ? -116.107 -38.574 26.408  1.00 123.83 ? 822  CYS A C   1 
ATOM   6033 O O   . CYS A 1 796 ? -116.878 -38.478 27.361  1.00 105.46 ? 822  CYS A O   1 
ATOM   6034 C CB  . CYS A 1 796 ? -113.989 -37.191 26.672  1.00 137.73 ? 822  CYS A CB  1 
ATOM   6035 S SG  . CYS A 1 796 ? -114.722 -36.021 27.831  1.00 168.19 ? 822  CYS A SG  1 
ATOM   6036 N N   . VAL A 1 797 ? -116.523 -38.698 25.141  1.00 130.91 ? 823  VAL A N   1 
ATOM   6037 C CA  . VAL A 1 797 ? -117.966 -38.679 24.761  1.00 142.03 ? 823  VAL A CA  1 
ATOM   6038 C C   . VAL A 1 797 ? -118.788 -37.689 25.593  1.00 127.47 ? 823  VAL A C   1 
ATOM   6039 O O   . VAL A 1 797 ? -118.823 -36.497 25.298  1.00 115.90 ? 823  VAL A O   1 
ATOM   6040 C CB  . VAL A 1 797 ? -118.629 -40.083 24.859  1.00 126.09 ? 823  VAL A CB  1 
ATOM   6041 C CG1 . VAL A 1 797 ? -120.139 -39.982 24.658  1.00 97.02  ? 823  VAL A CG1 1 
ATOM   6042 C CG2 . VAL A 1 797 ? -118.001 -41.050 23.860  1.00 117.40 ? 823  VAL A CG2 1 
HETATM 6043 C C1  . NAG B 2 .   ? -48.633  -17.177 -9.677  1.00 106.28 ? 901  NAG A C1  1 
HETATM 6044 C C2  . NAG B 2 .   ? -49.274  -16.695 -10.973 1.00 102.78 ? 901  NAG A C2  1 
HETATM 6045 C C3  . NAG B 2 .   ? -48.300  -16.811 -12.140 1.00 104.06 ? 901  NAG A C3  1 
HETATM 6046 C C4  . NAG B 2 .   ? -46.952  -16.192 -11.789 1.00 111.93 ? 901  NAG A C4  1 
HETATM 6047 C C5  . NAG B 2 .   ? -46.450  -16.704 -10.444 1.00 114.19 ? 901  NAG A C5  1 
HETATM 6048 C C6  . NAG B 2 .   ? -45.140  -16.028 -10.058 1.00 116.48 ? 901  NAG A C6  1 
HETATM 6049 C C7  . NAG B 2 .   ? -51.636  -16.870 -11.500 1.00 102.70 ? 901  NAG A C7  1 
HETATM 6050 C C8  . NAG B 2 .   ? -52.751  -17.779 -11.924 1.00 83.51  ? 901  NAG A C8  1 
HETATM 6051 N N2  . NAG B 2 .   ? -50.472  -17.463 -11.249 1.00 122.09 ? 901  NAG A N2  1 
HETATM 6052 O O3  . NAG B 2 .   ? -48.847  -16.147 -13.285 1.00 104.69 ? 901  NAG A O3  1 
HETATM 6053 O O4  . NAG B 2 .   ? -46.000  -16.515 -12.809 1.00 110.61 ? 901  NAG A O4  1 
HETATM 6054 O O5  . NAG B 2 .   ? -47.431  -16.447 -9.442  1.00 118.78 ? 901  NAG A O5  1 
HETATM 6055 O O6  . NAG B 2 .   ? -44.328  -15.856 -11.225 1.00 122.09 ? 901  NAG A O6  1 
HETATM 6056 O O7  . NAG B 2 .   ? -51.787  -15.664 -11.391 1.00 95.36  ? 901  NAG A O7  1 
HETATM 6057 C C1  . NAG C 2 .   ? -58.931  -16.555 11.949  1.00 44.28  ? 902  NAG A C1  1 
HETATM 6058 C C2  . NAG C 2 .   ? -60.094  -17.177 12.728  1.00 47.83  ? 902  NAG A C2  1 
HETATM 6059 C C3  . NAG C 2 .   ? -61.416  -17.067 12.003  1.00 54.48  ? 902  NAG A C3  1 
HETATM 6060 C C4  . NAG C 2 .   ? -61.628  -15.634 11.481  1.00 48.43  ? 902  NAG A C4  1 
HETATM 6061 C C5  . NAG C 2 .   ? -60.333  -15.213 10.810  1.00 53.25  ? 902  NAG A C5  1 
HETATM 6062 C C6  . NAG C 2 .   ? -60.350  -13.869 10.123  1.00 52.91  ? 902  NAG A C6  1 
HETATM 6063 C C7  . NAG C 2 .   ? -60.014  -19.109 14.148  1.00 60.13  ? 902  NAG A C7  1 
HETATM 6064 C C8  . NAG C 2 .   ? -59.663  -20.561 14.297  1.00 59.09  ? 902  NAG A C8  1 
HETATM 6065 N N2  . NAG C 2 .   ? -59.826  -18.566 12.963  1.00 62.03  ? 902  NAG A N2  1 
HETATM 6066 O O3  . NAG C 2 .   ? -62.463  -17.565 12.833  1.00 50.04  ? 902  NAG A O3  1 
HETATM 6067 O O4  . NAG C 2 .   ? -62.620  -15.662 10.484  1.00 52.90  ? 902  NAG A O4  1 
HETATM 6068 O O5  . NAG C 2 .   ? -59.337  -15.228 11.776  1.00 48.31  ? 902  NAG A O5  1 
HETATM 6069 O O6  . NAG C 2 .   ? -61.165  -13.060 10.921  1.00 73.88  ? 902  NAG A O6  1 
HETATM 6070 O O7  . NAG C 2 .   ? -60.425  -18.457 15.087  1.00 55.67  ? 902  NAG A O7  1 
HETATM 6071 C C1  . NAG D 2 .   ? -63.929  -15.475 11.031  1.00 57.13  ? 903  NAG A C1  1 
HETATM 6072 C C2  . NAG D 2 .   ? -64.877  -15.032 9.937   1.00 57.17  ? 903  NAG A C2  1 
HETATM 6073 C C3  . NAG D 2 .   ? -66.206  -14.722 10.541  1.00 54.83  ? 903  NAG A C3  1 
HETATM 6074 C C4  . NAG D 2 .   ? -66.731  -15.882 11.333  1.00 63.96  ? 903  NAG A C4  1 
HETATM 6075 C C5  . NAG D 2 .   ? -65.652  -16.372 12.276  1.00 68.84  ? 903  NAG A C5  1 
HETATM 6076 C C6  . NAG D 2 .   ? -66.125  -17.616 13.020  1.00 67.09  ? 903  NAG A C6  1 
HETATM 6077 C C7  . NAG D 2 .   ? -64.559  -13.575 8.020   1.00 61.80  ? 903  NAG A C7  1 
HETATM 6078 C C8  . NAG D 2 .   ? -64.094  -12.224 7.548   1.00 52.95  ? 903  NAG A C8  1 
HETATM 6079 N N2  . NAG D 2 .   ? -64.447  -13.801 9.330   1.00 59.59  ? 903  NAG A N2  1 
HETATM 6080 O O3  . NAG D 2 .   ? -67.101  -14.401 9.521   1.00 60.29  ? 903  NAG A O3  1 
HETATM 6081 O O4  . NAG D 2 .   ? -67.766  -15.348 12.114  1.00 74.23  ? 903  NAG A O4  1 
HETATM 6082 O O5  . NAG D 2 .   ? -64.452  -16.647 11.564  1.00 60.67  ? 903  NAG A O5  1 
HETATM 6083 O O6  . NAG D 2 .   ? -65.980  -18.754 12.188  1.00 72.00  ? 903  NAG A O6  1 
HETATM 6084 O O7  . NAG D 2 .   ? -65.010  -14.401 7.221   1.00 62.59  ? 903  NAG A O7  1 
HETATM 6085 C C1  . BMA E 3 .   ? -69.008  -15.981 11.789  1.00 81.29  ? 904  BMA A C1  1 
HETATM 6086 C C2  . BMA E 3 .   ? -69.950  -15.830 12.984  1.00 89.92  ? 904  BMA A C2  1 
HETATM 6087 C C3  . BMA E 3 .   ? -71.326  -16.406 12.679  1.00 98.41  ? 904  BMA A C3  1 
HETATM 6088 C C4  . BMA E 3 .   ? -71.845  -15.762 11.415  1.00 101.40 ? 904  BMA A C4  1 
HETATM 6089 C C5  . BMA E 3 .   ? -70.856  -15.958 10.268  1.00 109.69 ? 904  BMA A C5  1 
HETATM 6090 C C6  . BMA E 3 .   ? -71.399  -15.309 8.993   1.00 115.42 ? 904  BMA A C6  1 
HETATM 6091 O O2  . BMA E 3 .   ? -70.101  -14.443 13.321  1.00 68.47  ? 904  BMA A O2  1 
HETATM 6092 O O3  . BMA E 3 .   ? -72.249  -16.148 13.744  1.00 105.35 ? 904  BMA A O3  1 
HETATM 6093 O O4  . BMA E 3 .   ? -73.100  -16.343 11.077  1.00 103.14 ? 904  BMA A O4  1 
HETATM 6094 O O5  . BMA E 3 .   ? -69.573  -15.405 10.613  1.00 95.67  ? 904  BMA A O5  1 
HETATM 6095 O O6  . BMA E 3 .   ? -72.335  -14.268 9.324   1.00 130.41 ? 904  BMA A O6  1 
HETATM 6096 C C1  . MAN F 4 .   ? -72.595  -13.427 8.179   1.00 138.30 ? 905  MAN A C1  1 
HETATM 6097 C C2  . MAN F 4 .   ? -71.513  -12.342 8.082   1.00 135.92 ? 905  MAN A C2  1 
HETATM 6098 C C3  . MAN F 4 .   ? -71.662  -11.251 9.153   1.00 138.20 ? 905  MAN A C3  1 
HETATM 6099 C C4  . MAN F 4 .   ? -73.107  -10.768 9.268   1.00 122.89 ? 905  MAN A C4  1 
HETATM 6100 C C5  . MAN F 4 .   ? -74.040  -11.981 9.364   1.00 118.44 ? 905  MAN A C5  1 
HETATM 6101 C C6  . MAN F 4 .   ? -75.493  -11.565 9.462   1.00 114.21 ? 905  MAN A C6  1 
HETATM 6102 O O2  . MAN F 4 .   ? -71.539  -11.775 6.793   1.00 135.82 ? 905  MAN A O2  1 
HETATM 6103 O O3  . MAN F 4 .   ? -70.827  -10.150 8.861   1.00 129.30 ? 905  MAN A O3  1 
HETATM 6104 O O4  . MAN F 4 .   ? -73.244  -9.899  10.384  1.00 100.36 ? 905  MAN A O4  1 
HETATM 6105 O O5  . MAN F 4 .   ? -73.881  -12.829 8.242   1.00 124.11 ? 905  MAN A O5  1 
HETATM 6106 O O6  . MAN F 4 .   ? -75.932  -11.909 10.753  1.00 102.47 ? 905  MAN A O6  1 
HETATM 6107 C C1  . NAG G 2 .   ? -59.437  8.124   9.349   1.00 72.13  ? 906  NAG A C1  1 
HETATM 6108 C C2  . NAG G 2 .   ? -60.874  7.978   8.854   1.00 72.76  ? 906  NAG A C2  1 
HETATM 6109 C C3  . NAG G 2 .   ? -61.124  8.989   7.744   1.00 74.30  ? 906  NAG A C3  1 
HETATM 6110 C C4  . NAG G 2 .   ? -60.795  10.388  8.248   1.00 73.03  ? 906  NAG A C4  1 
HETATM 6111 C C5  . NAG G 2 .   ? -59.333  10.399  8.694   1.00 75.03  ? 906  NAG A C5  1 
HETATM 6112 C C6  . NAG G 2 .   ? -58.854  11.743  9.215   1.00 77.74  ? 906  NAG A C6  1 
HETATM 6113 C C7  . NAG G 2 .   ? -62.151  5.932   8.461   1.00 72.37  ? 906  NAG A C7  1 
HETATM 6114 C C8  . NAG G 2 .   ? -62.178  4.616   7.735   1.00 64.21  ? 906  NAG A C8  1 
HETATM 6115 N N2  . NAG G 2 .   ? -61.066  6.670   8.270   1.00 73.34  ? 906  NAG A N2  1 
HETATM 6116 O O3  . NAG G 2 .   ? -62.452  8.875   7.273   1.00 81.87  ? 906  NAG A O3  1 
HETATM 6117 O O4  . NAG G 2 .   ? -61.034  11.317  7.222   1.00 74.15  ? 906  NAG A O4  1 
HETATM 6118 O O5  . NAG G 2 .   ? -59.167  9.462   9.724   1.00 71.98  ? 906  NAG A O5  1 
HETATM 6119 O O6  . NAG G 2 .   ? -59.443  11.978  10.468  1.00 80.15  ? 906  NAG A O6  1 
HETATM 6120 O O7  . NAG G 2 .   ? -63.074  6.270   9.203   1.00 82.63  ? 906  NAG A O7  1 
HETATM 6121 C C1  . NAG H 2 .   ? -46.907  13.946  20.152  1.00 90.35  ? 907  NAG A C1  1 
HETATM 6122 C C2  . NAG H 2 .   ? -45.529  13.498  20.606  1.00 92.52  ? 907  NAG A C2  1 
HETATM 6123 C C3  . NAG H 2 .   ? -44.525  13.865  19.531  1.00 97.82  ? 907  NAG A C3  1 
HETATM 6124 C C4  . NAG H 2 .   ? -44.911  13.229  18.216  1.00 99.01  ? 907  NAG A C4  1 
HETATM 6125 C C5  . NAG H 2 .   ? -46.366  13.510  17.856  1.00 97.74  ? 907  NAG A C5  1 
HETATM 6126 C C6  . NAG H 2 .   ? -46.786  12.586  16.721  1.00 95.87  ? 907  NAG A C6  1 
HETATM 6127 C C7  . NAG H 2 .   ? -44.445  13.516  22.743  1.00 91.83  ? 907  NAG A C7  1 
HETATM 6128 C C8  . NAG H 2 .   ? -44.067  14.323  23.950  1.00 105.72 ? 907  NAG A C8  1 
HETATM 6129 N N2  . NAG H 2 .   ? -45.156  14.153  21.846  1.00 81.86  ? 907  NAG A N2  1 
HETATM 6130 O O3  . NAG H 2 .   ? -43.245  13.413  19.889  1.00 116.23 ? 907  NAG A O3  1 
HETATM 6131 O O4  . NAG H 2 .   ? -44.056  13.757  17.223  1.00 108.71 ? 907  NAG A O4  1 
HETATM 6132 O O5  . NAG H 2 .   ? -47.250  13.305  18.942  1.00 85.70  ? 907  NAG A O5  1 
HETATM 6133 O O6  . NAG H 2 .   ? -48.049  12.985  16.241  1.00 89.35  ? 907  NAG A O6  1 
HETATM 6134 O O7  . NAG H 2 .   ? -44.117  12.325  22.602  1.00 96.59  ? 907  NAG A O7  1 
HETATM 6135 C C1  . NAG I 2 .   ? -65.940  -3.419  33.790  1.00 45.62  ? 908  NAG A C1  1 
HETATM 6136 C C2  . NAG I 2 .   ? -67.098  -3.852  32.883  1.00 42.55  ? 908  NAG A C2  1 
HETATM 6137 C C3  . NAG I 2 .   ? -67.740  -5.090  33.457  1.00 54.56  ? 908  NAG A C3  1 
HETATM 6138 C C4  . NAG I 2 .   ? -66.709  -6.181  33.768  1.00 54.44  ? 908  NAG A C4  1 
HETATM 6139 C C5  . NAG I 2 .   ? -65.514  -5.571  34.507  1.00 52.22  ? 908  NAG A C5  1 
HETATM 6140 C C6  . NAG I 2 .   ? -64.444  -6.612  34.697  1.00 46.62  ? 908  NAG A C6  1 
HETATM 6141 C C7  . NAG I 2 .   ? -68.287  -2.060  31.655  1.00 43.74  ? 908  NAG A C7  1 
HETATM 6142 C C8  . NAG I 2 .   ? -69.286  -0.956  31.782  1.00 43.48  ? 908  NAG A C8  1 
HETATM 6143 N N2  . NAG I 2 .   ? -68.062  -2.787  32.773  1.00 45.97  ? 908  NAG A N2  1 
HETATM 6144 O O3  . NAG I 2 .   ? -68.729  -5.540  32.565  1.00 52.26  ? 908  NAG A O3  1 
HETATM 6145 O O4  . NAG I 2 .   ? -67.373  -7.087  34.622  1.00 64.71  ? 908  NAG A O4  1 
HETATM 6146 O O5  . NAG I 2 .   ? -64.972  -4.461  33.799  1.00 57.66  ? 908  NAG A O5  1 
HETATM 6147 O O6  . NAG I 2 .   ? -63.938  -7.002  33.460  1.00 47.87  ? 908  NAG A O6  1 
HETATM 6148 O O7  . NAG I 2 .   ? -67.717  -2.195  30.572  1.00 51.15  ? 908  NAG A O7  1 
HETATM 6149 C C1  . NAG J 2 .   ? -67.498  -8.352  33.947  1.00 80.08  ? 909  NAG A C1  1 
HETATM 6150 C C2  . NAG J 2 .   ? -67.799  -9.443  34.967  1.00 87.56  ? 909  NAG A C2  1 
HETATM 6151 C C3  . NAG J 2 .   ? -67.953  -10.799 34.287  1.00 108.21 ? 909  NAG A C3  1 
HETATM 6152 C C4  . NAG J 2 .   ? -68.906  -10.709 33.102  1.00 118.41 ? 909  NAG A C4  1 
HETATM 6153 C C5  . NAG J 2 .   ? -68.540  -9.542  32.193  1.00 116.41 ? 909  NAG A C5  1 
HETATM 6154 C C6  . NAG J 2 .   ? -69.538  -9.406  31.049  1.00 104.21 ? 909  NAG A C6  1 
HETATM 6155 C C7  . NAG J 2 .   ? -66.738  -8.704  37.020  1.00 74.37  ? 909  NAG A C7  1 
HETATM 6156 C C8  . NAG J 2 .   ? -65.470  -8.691  37.820  1.00 72.18  ? 909  NAG A C8  1 
HETATM 6157 N N2  . NAG J 2 .   ? -66.741  -9.503  35.957  1.00 58.87  ? 909  NAG A N2  1 
HETATM 6158 O O3  . NAG J 2 .   ? -68.453  -11.752 35.231  1.00 121.31 ? 909  NAG A O3  1 
HETATM 6159 O O4  . NAG J 2 .   ? -68.855  -11.930 32.354  1.00 129.06 ? 909  NAG A O4  1 
HETATM 6160 O O5  . NAG J 2 .   ? -68.521  -8.335  32.953  1.00 94.84  ? 909  NAG A O5  1 
HETATM 6161 O O6  . NAG J 2 .   ? -70.570  -8.486  31.423  1.00 97.46  ? 909  NAG A O6  1 
HETATM 6162 O O7  . NAG J 2 .   ? -67.705  -8.025  37.325  1.00 86.79  ? 909  NAG A O7  1 
HETATM 6163 C C1  . NAG K 2 .   ? -66.678  14.982  52.843  1.00 77.11  ? 910  NAG A C1  1 
HETATM 6164 C C2  . NAG K 2 .   ? -66.734  15.531  54.266  1.00 88.16  ? 910  NAG A C2  1 
HETATM 6165 C C3  . NAG K 2 .   ? -66.128  16.933  54.311  1.00 92.81  ? 910  NAG A C3  1 
HETATM 6166 C C4  . NAG K 2 .   ? -64.767  16.900  53.639  1.00 96.22  ? 910  NAG A C4  1 
HETATM 6167 C C5  . NAG K 2 .   ? -64.826  16.302  52.249  1.00 91.36  ? 910  NAG A C5  1 
HETATM 6168 C C6  . NAG K 2 .   ? -63.395  16.083  51.810  1.00 92.89  ? 910  NAG A C6  1 
HETATM 6169 C C7  . NAG K 2 .   ? -69.213  15.850  54.304  1.00 104.69 ? 910  NAG A C7  1 
HETATM 6170 C C8  . NAG K 2 .   ? -70.485  15.548  55.049  1.00 103.16 ? 910  NAG A C8  1 
HETATM 6171 N N2  . NAG K 2 .   ? -68.071  15.390  54.859  1.00 89.85  ? 910  NAG A N2  1 
HETATM 6172 O O3  . NAG K 2 .   ? -65.887  17.339  55.636  1.00 91.06  ? 910  NAG A O3  1 
HETATM 6173 O O4  . NAG K 2 .   ? -64.224  18.190  53.551  1.00 95.52  ? 910  NAG A O4  1 
HETATM 6174 O O5  . NAG K 2 .   ? -65.360  15.019  52.385  1.00 87.32  ? 910  NAG A O5  1 
HETATM 6175 O O6  . NAG K 2 .   ? -62.855  15.130  52.719  1.00 85.24  ? 910  NAG A O6  1 
HETATM 6176 O O7  . NAG K 2 .   ? -69.284  16.501  53.251  1.00 91.69  ? 910  NAG A O7  1 
HETATM 6177 C C1  . NAG L 2 .   ? -76.401  18.705  47.138  1.00 111.16 ? 911  NAG A C1  1 
HETATM 6178 C C2  . NAG L 2 .   ? -75.487  19.923  47.306  1.00 113.83 ? 911  NAG A C2  1 
HETATM 6179 C C3  . NAG L 2 .   ? -75.534  20.436  48.738  1.00 122.69 ? 911  NAG A C3  1 
HETATM 6180 C C4  . NAG L 2 .   ? -76.960  20.480  49.300  1.00 129.10 ? 911  NAG A C4  1 
HETATM 6181 C C5  . NAG L 2 .   ? -77.770  19.233  48.960  1.00 140.32 ? 911  NAG A C5  1 
HETATM 6182 C C6  . NAG L 2 .   ? -79.216  19.390  49.436  1.00 142.32 ? 911  NAG A C6  1 
HETATM 6183 C C7  . NAG L 2 .   ? -73.536  20.107  45.800  1.00 111.00 ? 911  NAG A C7  1 
HETATM 6184 C C8  . NAG L 2 .   ? -72.077  19.803  45.591  1.00 101.82 ? 911  NAG A C8  1 
HETATM 6185 N N2  . NAG L 2 .   ? -74.090  19.670  46.940  1.00 111.50 ? 911  NAG A N2  1 
HETATM 6186 O O3  . NAG L 2 .   ? -74.970  21.729  48.744  1.00 115.94 ? 911  NAG A O3  1 
HETATM 6187 O O4  . NAG L 2 .   ? -76.907  20.563  50.706  1.00 127.85 ? 911  NAG A O4  1 
HETATM 6188 O O5  . NAG L 2 .   ? -77.718  18.978  47.569  1.00 121.44 ? 911  NAG A O5  1 
HETATM 6189 O O6  . NAG L 2 .   ? -79.933  20.236  48.563  1.00 145.25 ? 911  NAG A O6  1 
HETATM 6190 O O7  . NAG L 2 .   ? -74.155  20.732  44.939  1.00 108.50 ? 911  NAG A O7  1 
HETATM 6191 C C1  . NAG M 2 .   ? -76.843  -2.345  37.004  1.00 45.78  ? 912  NAG A C1  1 
HETATM 6192 C C2  . NAG M 2 .   ? -76.344  -3.549  36.215  1.00 43.69  ? 912  NAG A C2  1 
HETATM 6193 C C3  . NAG M 2 .   ? -76.182  -3.241  34.749  1.00 47.27  ? 912  NAG A C3  1 
HETATM 6194 C C4  . NAG M 2 .   ? -77.500  -2.738  34.225  1.00 45.76  ? 912  NAG A C4  1 
HETATM 6195 C C5  . NAG M 2 .   ? -77.977  -1.593  35.090  1.00 48.71  ? 912  NAG A C5  1 
HETATM 6196 C C6  . NAG M 2 .   ? -79.260  -0.987  34.543  1.00 46.80  ? 912  NAG A C6  1 
HETATM 6197 C C7  . NAG M 2 .   ? -74.778  -5.176  37.059  1.00 46.52  ? 912  NAG A C7  1 
HETATM 6198 C C8  . NAG M 2 .   ? -73.400  -5.454  37.538  1.00 46.03  ? 912  NAG A C8  1 
HETATM 6199 N N2  . NAG M 2 .   ? -75.043  -3.939  36.690  1.00 50.29  ? 912  NAG A N2  1 
HETATM 6200 O O3  . NAG M 2 .   ? -75.620  -4.349  34.033  1.00 45.88  ? 912  NAG A O3  1 
HETATM 6201 O O4  . NAG M 2 .   ? -77.258  -2.215  32.952  1.00 54.65  ? 912  NAG A O4  1 
HETATM 6202 O O5  . NAG M 2 .   ? -78.101  -1.976  36.451  1.00 50.60  ? 912  NAG A O5  1 
HETATM 6203 O O6  . NAG M 2 .   ? -80.221  -2.002  34.487  1.00 45.37  ? 912  NAG A O6  1 
HETATM 6204 O O7  . NAG M 2 .   ? -75.615  -6.051  37.067  1.00 51.98  ? 912  NAG A O7  1 
HETATM 6205 C C1  . NAG N 2 .   ? -78.299  -2.637  32.048  1.00 50.66  ? 913  NAG A C1  1 
HETATM 6206 C C2  . NAG N 2 .   ? -78.203  -1.812  30.785  1.00 52.93  ? 913  NAG A C2  1 
HETATM 6207 C C3  . NAG N 2 .   ? -79.115  -2.238  29.627  1.00 57.98  ? 913  NAG A C3  1 
HETATM 6208 C C4  . NAG N 2 .   ? -79.091  -3.764  29.480  1.00 58.33  ? 913  NAG A C4  1 
HETATM 6209 C C5  . NAG N 2 .   ? -79.214  -4.402  30.874  1.00 62.68  ? 913  NAG A C5  1 
HETATM 6210 C C6  . NAG N 2 .   ? -79.126  -5.926  30.884  1.00 56.89  ? 913  NAG A C6  1 
HETATM 6211 C C7  . NAG N 2 .   ? -77.053  0.284   30.878  1.00 49.69  ? 913  NAG A C7  1 
HETATM 6212 C C8  . NAG N 2 .   ? -77.124  1.771   31.027  1.00 42.88  ? 913  NAG A C8  1 
HETATM 6213 N N2  . NAG N 2 .   ? -78.214  -0.386  31.013  1.00 43.70  ? 913  NAG A N2  1 
HETATM 6214 O O3  . NAG N 2 .   ? -78.572  -1.668  28.453  1.00 45.89  ? 913  NAG A O3  1 
HETATM 6215 O O4  . NAG N 2 .   ? -80.101  -4.207  28.586  1.00 68.06  ? 913  NAG A O4  1 
HETATM 6216 O O5  . NAG N 2 .   ? -78.102  -3.956  31.631  1.00 56.91  ? 913  NAG A O5  1 
HETATM 6217 O O6  . NAG N 2 .   ? -77.847  -6.233  30.356  1.00 75.99  ? 913  NAG A O6  1 
HETATM 6218 O O7  . NAG N 2 .   ? -75.958  -0.284  30.628  1.00 53.38  ? 913  NAG A O7  1 
HETATM 6219 C C1  . BMA O 3 .   ? -79.573  -4.782  27.365  1.00 68.33  ? 914  BMA A C1  1 
HETATM 6220 C C2  . BMA O 3 .   ? -80.598  -5.743  26.769  1.00 82.25  ? 914  BMA A C2  1 
HETATM 6221 C C3  . BMA O 3 .   ? -80.013  -6.431  25.529  1.00 99.38  ? 914  BMA A C3  1 
HETATM 6222 C C4  . BMA O 3 .   ? -79.615  -5.353  24.540  1.00 97.38  ? 914  BMA A C4  1 
HETATM 6223 C C5  . BMA O 3 .   ? -78.685  -4.331  25.195  1.00 98.11  ? 914  BMA A C5  1 
HETATM 6224 C C6  . BMA O 3 .   ? -78.293  -3.214  24.205  1.00 106.67 ? 914  BMA A C6  1 
HETATM 6225 O O2  . BMA O 3 .   ? -81.739  -4.964  26.425  1.00 83.76  ? 914  BMA A O2  1 
HETATM 6226 O O3  . BMA O 3 .   ? -80.797  -7.445  24.836  1.00 107.38 ? 914  BMA A O3  1 
HETATM 6227 O O4  . BMA O 3 .   ? -78.934  -5.984  23.459  1.00 103.82 ? 914  BMA A O4  1 
HETATM 6228 O O5  . BMA O 3 .   ? -79.306  -3.793  26.377  1.00 83.78  ? 914  BMA A O5  1 
HETATM 6229 O O6  . BMA O 3 .   ? -79.425  -2.382  23.882  1.00 125.48 ? 914  BMA A O6  1 
HETATM 6230 C C1  . MAN P 4 .   ? -79.153  -1.414  22.818  1.00 128.10 ? 915  MAN A C1  1 
HETATM 6231 C C2  . MAN P 4 .   ? -80.198  -0.285  22.862  1.00 119.52 ? 915  MAN A C2  1 
HETATM 6232 C C3  . MAN P 4 .   ? -81.609  -0.824  22.537  1.00 114.32 ? 915  MAN A C3  1 
HETATM 6233 C C4  . MAN P 4 .   ? -81.607  -1.630  21.238  1.00 104.70 ? 915  MAN A C4  1 
HETATM 6234 C C5  . MAN P 4 .   ? -80.450  -2.626  21.292  1.00 103.58 ? 915  MAN A C5  1 
HETATM 6235 C C6  . MAN P 4 .   ? -80.323  -3.499  20.068  1.00 93.27  ? 915  MAN A C6  1 
HETATM 6236 O O2  . MAN P 4 .   ? -79.811  0.706   21.938  1.00 97.01  ? 915  MAN A O2  1 
HETATM 6237 O O3  . MAN P 4 .   ? -82.618  0.169   22.530  1.00 110.89 ? 915  MAN A O3  1 
HETATM 6238 O O4  . MAN P 4 .   ? -82.811  -2.353  21.172  1.00 88.82  ? 915  MAN A O4  1 
HETATM 6239 O O5  . MAN P 4 .   ? -79.212  -1.966  21.512  1.00 109.63 ? 915  MAN A O5  1 
HETATM 6240 O O6  . MAN P 4 .   ? -79.053  -4.102  20.179  1.00 92.88  ? 915  MAN A O6  1 
HETATM 6241 C C1  . MAN Q 4 .   ? -82.184  -7.592  25.206  1.00 116.42 ? 916  MAN A C1  1 
HETATM 6242 C C2  . MAN Q 4 .   ? -82.334  -8.619  26.323  1.00 124.11 ? 916  MAN A C2  1 
HETATM 6243 C C3  . MAN Q 4 .   ? -81.887  -9.993  25.827  1.00 127.31 ? 916  MAN A C3  1 
HETATM 6244 C C4  . MAN Q 4 .   ? -82.698  -10.391 24.597  1.00 127.02 ? 916  MAN A C4  1 
HETATM 6245 C C5  . MAN Q 4 .   ? -82.699  -9.271  23.554  1.00 129.71 ? 916  MAN A C5  1 
HETATM 6246 C C6  . MAN Q 4 .   ? -83.666  -9.614  22.420  1.00 126.32 ? 916  MAN A C6  1 
HETATM 6247 O O2  . MAN Q 4 .   ? -83.697  -8.671  26.691  1.00 109.41 ? 916  MAN A O2  1 
HETATM 6248 O O3  . MAN Q 4 .   ? -82.059  -10.953 26.844  1.00 115.74 ? 916  MAN A O3  1 
HETATM 6249 O O4  . MAN Q 4 .   ? -82.154  -11.569 24.029  1.00 112.61 ? 916  MAN A O4  1 
HETATM 6250 O O5  . MAN Q 4 .   ? -83.017  -7.998  24.120  1.00 131.61 ? 916  MAN A O5  1 
HETATM 6251 O O6  . MAN Q 4 .   ? -83.126  -10.668 21.647  1.00 119.51 ? 916  MAN A O6  1 
HETATM 6252 C C1  . NAG R 2 .   ? -87.106  12.673  33.188  1.00 65.45  ? 917  NAG A C1  1 
HETATM 6253 C C2  . NAG R 2 .   ? -86.091  13.800  33.108  1.00 64.15  ? 917  NAG A C2  1 
HETATM 6254 C C3  . NAG R 2 .   ? -86.026  14.247  31.664  1.00 71.02  ? 917  NAG A C3  1 
HETATM 6255 C C4  . NAG R 2 .   ? -85.574  13.045  30.858  1.00 80.81  ? 917  NAG A C4  1 
HETATM 6256 C C5  . NAG R 2 .   ? -86.515  11.856  31.093  1.00 81.18  ? 917  NAG A C5  1 
HETATM 6257 C C6  . NAG R 2 .   ? -86.058  10.624  30.310  1.00 87.35  ? 917  NAG A C6  1 
HETATM 6258 C C7  . NAG R 2 .   ? -85.728  15.640  34.684  1.00 70.41  ? 917  NAG A C7  1 
HETATM 6259 C C8  . NAG R 2 .   ? -86.407  16.605  35.613  1.00 67.50  ? 917  NAG A C8  1 
HETATM 6260 N N2  . NAG R 2 .   ? -86.540  14.836  33.998  1.00 70.61  ? 917  NAG A N2  1 
HETATM 6261 O O3  . NAG R 2 .   ? -85.088  15.280  31.488  1.00 85.03  ? 917  NAG A O3  1 
HETATM 6262 O O4  . NAG R 2 .   ? -85.516  13.414  29.504  1.00 85.57  ? 917  NAG A O4  1 
HETATM 6263 O O5  . NAG R 2 .   ? -86.605  11.561  32.483  1.00 72.59  ? 917  NAG A O5  1 
HETATM 6264 O O6  . NAG R 2 .   ? -84.661  10.416  30.472  1.00 77.90  ? 917  NAG A O6  1 
HETATM 6265 O O7  . NAG R 2 .   ? -84.506  15.648  34.568  1.00 72.05  ? 917  NAG A O7  1 
HETATM 6266 S S   . SO4 S 5 .   ? -93.636  -22.059 53.359  1.00 90.28  ? 918  SO4 A S   1 
HETATM 6267 O O1  . SO4 S 5 .   ? -92.542  -21.717 52.423  1.00 85.84  ? 918  SO4 A O1  1 
HETATM 6268 O O2  . SO4 S 5 .   ? -94.132  -23.379 52.929  1.00 87.97  ? 918  SO4 A O2  1 
HETATM 6269 O O3  . SO4 S 5 .   ? -94.708  -21.027 53.308  1.00 71.23  ? 918  SO4 A O3  1 
HETATM 6270 O O4  . SO4 S 5 .   ? -93.132  -22.147 54.754  1.00 96.14  ? 918  SO4 A O4  1 
HETATM 6271 S S   . SO4 T 5 .   ? -42.063  -11.749 -6.512  1.00 120.97 ? 919  SO4 A S   1 
HETATM 6272 O O1  . SO4 T 5 .   ? -41.089  -12.700 -7.090  1.00 132.40 ? 919  SO4 A O1  1 
HETATM 6273 O O2  . SO4 T 5 .   ? -42.977  -11.251 -7.564  1.00 108.98 ? 919  SO4 A O2  1 
HETATM 6274 O O3  . SO4 T 5 .   ? -42.858  -12.476 -5.495  1.00 136.52 ? 919  SO4 A O3  1 
HETATM 6275 O O4  . SO4 T 5 .   ? -41.328  -10.608 -5.906  1.00 94.36  ? 919  SO4 A O4  1 
HETATM 6276 S S   . SO4 U 5 .   ? -38.371  5.963   6.471   1.00 112.87 ? 920  SO4 A S   1 
HETATM 6277 O O1  . SO4 U 5 .   ? -38.144  7.422   6.328   1.00 98.98  ? 920  SO4 A O1  1 
HETATM 6278 O O2  . SO4 U 5 .   ? -39.214  5.508   5.335   1.00 97.61  ? 920  SO4 A O2  1 
HETATM 6279 O O3  . SO4 U 5 .   ? -39.050  5.739   7.765   1.00 109.36 ? 920  SO4 A O3  1 
HETATM 6280 O O4  . SO4 U 5 .   ? -37.091  5.205   6.457   1.00 104.59 ? 920  SO4 A O4  1 
HETATM 6281 O O1  . MES V 6 .   ? -58.122  1.145   0.956   0.50 58.46  ? 921  MES A O1  1 
HETATM 6282 C C2  . MES V 6 .   ? -59.484  1.274   0.563   0.50 80.37  ? 921  MES A C2  1 
HETATM 6283 C C3  . MES V 6 .   ? -60.137  -0.097  0.249   0.50 81.47  ? 921  MES A C3  1 
HETATM 6284 N N4  . MES V 6 .   ? -59.342  -0.939  -0.689  0.50 82.00  ? 921  MES A N4  1 
HETATM 6285 C C5  . MES V 6 .   ? -57.905  -0.920  -0.354  0.50 68.13  ? 921  MES A C5  1 
HETATM 6286 C C6  . MES V 6 .   ? -57.418  0.518   -0.104  0.50 70.59  ? 921  MES A C6  1 
HETATM 6287 C C7  . MES V 6 .   ? -59.800  -2.352  -0.681  0.50 79.38  ? 921  MES A C7  1 
HETATM 6288 C C8  . MES V 6 .   ? -61.324  -2.478  -0.731  0.50 74.79  ? 921  MES A C8  1 
HETATM 6289 S S   . MES V 6 .   ? -61.839  -3.441  0.523   0.50 78.70  ? 921  MES A S   1 
HETATM 6290 O O1S . MES V 6 .   ? -62.672  -4.549  0.021   0.50 79.13  ? 921  MES A O1S 1 
HETATM 6291 O O2S . MES V 6 .   ? -60.672  -4.005  1.246   0.50 86.40  ? 921  MES A O2S 1 
HETATM 6292 O O3S . MES V 6 .   ? -62.620  -2.638  1.479   0.50 74.19  ? 921  MES A O3S 1 
HETATM 6293 O O   . HOH W 7 .   ? -53.771  -22.914 -6.899  1.00 80.55  ? 1001 HOH A O   1 
HETATM 6294 O O   . HOH W 7 .   ? -47.799  -0.137  40.618  1.00 57.96  ? 1002 HOH A O   1 
HETATM 6295 O O   . HOH W 7 .   ? -59.191  13.715  45.867  1.00 45.50  ? 1003 HOH A O   1 
HETATM 6296 O O   . HOH W 7 .   ? -85.650  -12.128 48.302  1.00 57.95  ? 1004 HOH A O   1 
HETATM 6297 O O   . HOH W 7 .   ? -89.197  7.476   54.270  1.00 69.96  ? 1005 HOH A O   1 
HETATM 6298 O O   . HOH W 7 .   ? -85.429  -7.558  24.451  1.00 92.62  ? 1006 HOH A O   1 
HETATM 6299 O O   . HOH W 7 .   ? -67.938  17.799  44.846  1.00 65.34  ? 1007 HOH A O   1 
HETATM 6300 O O   . HOH W 7 .   ? -109.626 -9.840  38.143  1.00 92.98  ? 1008 HOH A O   1 
HETATM 6301 O O   . HOH W 7 .   ? -57.726  12.159  42.168  1.00 52.18  ? 1009 HOH A O   1 
HETATM 6302 O O   . HOH W 7 .   ? -40.897  -6.149  21.366  1.00 48.34  ? 1010 HOH A O   1 
HETATM 6303 O O   . HOH W 7 .   ? -61.302  -21.558 10.906  1.00 55.18  ? 1011 HOH A O   1 
HETATM 6304 O O   . HOH W 7 .   ? -55.798  -13.002 20.651  1.00 77.57  ? 1012 HOH A O   1 
HETATM 6305 O O   . HOH W 7 .   ? -47.217  12.148  14.001  1.00 72.04  ? 1013 HOH A O   1 
HETATM 6306 O O   . HOH W 7 .   ? -80.695  -36.219 -1.212  1.00 91.95  ? 1014 HOH A O   1 
HETATM 6307 O O   . HOH W 7 .   ? -80.060  13.014  40.602  1.00 54.26  ? 1015 HOH A O   1 
HETATM 6308 O O   . HOH W 7 .   ? -71.080  2.655   54.350  1.00 67.82  ? 1016 HOH A O   1 
HETATM 6309 O O   . HOH W 7 .   ? -65.559  4.753   23.140  1.00 50.07  ? 1017 HOH A O   1 
HETATM 6310 O O   . HOH W 7 .   ? -60.868  4.101   13.783  1.00 50.59  ? 1018 HOH A O   1 
HETATM 6311 O O   . HOH W 7 .   ? -77.459  -6.178  33.932  1.00 63.53  ? 1019 HOH A O   1 
HETATM 6312 O O   . HOH W 7 .   ? -65.890  11.538  44.551  1.00 49.73  ? 1020 HOH A O   1 
HETATM 6313 O O   . HOH W 7 .   ? -80.009  -7.235  39.733  1.00 66.64  ? 1021 HOH A O   1 
HETATM 6314 O O   . HOH W 7 .   ? -58.515  3.033   8.660   1.00 53.11  ? 1022 HOH A O   1 
HETATM 6315 O O   . HOH W 7 .   ? -54.617  4.978   11.475  1.00 49.46  ? 1023 HOH A O   1 
HETATM 6316 O O   . HOH W 7 .   ? -70.279  -7.295  47.353  1.00 42.23  ? 1024 HOH A O   1 
HETATM 6317 O O   . HOH W 7 .   ? -80.557  -4.329  35.644  1.00 53.45  ? 1025 HOH A O   1 
HETATM 6318 O O   . HOH W 7 .   ? -80.868  0.293   31.528  1.00 59.74  ? 1026 HOH A O   1 
HETATM 6319 O O   . HOH W 7 .   ? -63.792  13.669  31.874  1.00 49.47  ? 1027 HOH A O   1 
HETATM 6320 O O   . HOH W 7 .   ? -81.050  -9.639  49.818  1.00 57.34  ? 1028 HOH A O   1 
HETATM 6321 O O   . HOH W 7 .   ? -87.951  9.201   48.574  1.00 65.57  ? 1029 HOH A O   1 
HETATM 6322 O O   . HOH W 7 .   ? -40.804  -18.817 13.051  1.00 54.43  ? 1030 HOH A O   1 
HETATM 6323 O O   . HOH W 7 .   ? -67.276  -6.564  46.033  1.00 50.90  ? 1031 HOH A O   1 
HETATM 6324 O O   . HOH W 7 .   ? -68.861  -15.258 4.645   1.00 71.36  ? 1032 HOH A O   1 
HETATM 6325 O O   . HOH W 7 .   ? -64.690  -12.283 0.085   1.00 57.91  ? 1033 HOH A O   1 
HETATM 6326 O O   . HOH W 7 .   ? -48.490  -9.956  23.513  1.00 48.46  ? 1034 HOH A O   1 
HETATM 6327 O O   . HOH W 7 .   ? -63.780  -39.706 -4.447  1.00 78.98  ? 1035 HOH A O   1 
HETATM 6328 O O   . HOH W 7 .   ? -56.037  -13.406 -3.466  1.00 61.22  ? 1036 HOH A O   1 
HETATM 6329 O O   . HOH W 7 .   ? -41.439  1.006   22.352  1.00 50.98  ? 1037 HOH A O   1 
HETATM 6330 O O   . HOH W 7 .   ? -60.092  -30.797 -5.032  1.00 69.66  ? 1038 HOH A O   1 
HETATM 6331 O O   . HOH W 7 .   ? -69.733  14.078  35.075  1.00 50.96  ? 1039 HOH A O   1 
HETATM 6332 O O   . HOH W 7 .   ? -75.717  14.415  36.154  1.00 60.44  ? 1040 HOH A O   1 
HETATM 6333 O O   . HOH W 7 .   ? -56.432  12.724  39.711  1.00 67.11  ? 1041 HOH A O   1 
HETATM 6334 O O   . HOH W 7 .   ? -53.099  -28.638 14.265  1.00 62.73  ? 1042 HOH A O   1 
HETATM 6335 O O   . HOH W 7 .   ? -59.193  -17.958 -5.727  1.00 58.45  ? 1043 HOH A O   1 
HETATM 6336 O O   . HOH W 7 .   ? -46.510  -24.559 23.233  1.00 70.79  ? 1044 HOH A O   1 
HETATM 6337 O O   . HOH W 7 .   ? -53.984  -8.064  -0.632  1.00 47.05  ? 1045 HOH A O   1 
HETATM 6338 O O   . HOH W 7 .   ? -52.218  0.224   8.314   1.00 47.03  ? 1046 HOH A O   1 
HETATM 6339 O O   . HOH W 7 .   ? -68.290  8.045   50.134  1.00 55.37  ? 1047 HOH A O   1 
HETATM 6340 O O   . HOH W 7 .   ? -36.726  4.831   32.065  1.00 82.34  ? 1048 HOH A O   1 
HETATM 6341 O O   . HOH W 7 .   ? -48.939  11.550  33.410  1.00 75.28  ? 1049 HOH A O   1 
HETATM 6342 O O   . HOH W 7 .   ? -66.762  5.661   48.901  1.00 58.44  ? 1050 HOH A O   1 
HETATM 6343 O O   . HOH W 7 .   ? -108.263 2.396   36.849  1.00 89.29  ? 1051 HOH A O   1 
HETATM 6344 O O   . HOH W 7 .   ? -78.116  -5.359  38.304  1.00 67.81  ? 1052 HOH A O   1 
HETATM 6345 O O   . HOH W 7 .   ? -91.135  4.695   48.702  1.00 67.38  ? 1053 HOH A O   1 
HETATM 6346 O O   . HOH W 7 .   ? -63.181  -5.294  31.187  1.00 56.43  ? 1054 HOH A O   1 
HETATM 6347 O O   . HOH W 7 .   ? -52.224  12.458  13.400  1.00 67.79  ? 1055 HOH A O   1 
HETATM 6348 O O   . HOH W 7 .   ? -68.404  -1.773  50.938  1.00 48.09  ? 1056 HOH A O   1 
HETATM 6349 O O   . HOH W 7 .   ? -49.506  2.887   39.329  1.00 55.45  ? 1057 HOH A O   1 
HETATM 6350 O O   . HOH W 7 .   ? -47.954  -11.633 -1.375  1.00 54.26  ? 1058 HOH A O   1 
HETATM 6351 O O   . HOH W 7 .   ? -55.689  5.862   6.797   1.00 51.45  ? 1059 HOH A O   1 
HETATM 6352 O O   . HOH W 7 .   ? -59.620  -21.990 19.020  1.00 76.85  ? 1060 HOH A O   1 
HETATM 6353 O O   . HOH W 7 .   ? -61.235  6.899   12.258  1.00 68.16  ? 1061 HOH A O   1 
HETATM 6354 O O   . HOH W 7 .   ? -43.214  7.064   9.396   1.00 61.04  ? 1062 HOH A O   1 
HETATM 6355 O O   . HOH W 7 .   ? -42.687  -19.866 8.414   1.00 60.20  ? 1063 HOH A O   1 
HETATM 6356 O O   . HOH W 7 .   ? -69.013  -25.110 -7.169  1.00 70.82  ? 1064 HOH A O   1 
HETATM 6357 O O   . HOH W 7 .   ? -60.784  8.725   50.365  1.00 67.72  ? 1065 HOH A O   1 
HETATM 6358 O O   . HOH W 7 .   ? -68.012  -5.397  48.917  1.00 43.47  ? 1066 HOH A O   1 
HETATM 6359 O O   . HOH W 7 .   ? -60.858  -5.122  16.799  1.00 56.12  ? 1067 HOH A O   1 
HETATM 6360 O O   . HOH W 7 .   ? -62.508  11.789  4.718   1.00 54.30  ? 1068 HOH A O   1 
HETATM 6361 O O   . HOH W 7 .   ? -83.042  -4.575  36.853  1.00 58.12  ? 1069 HOH A O   1 
HETATM 6362 O O   . HOH W 7 .   ? -87.206  -15.163 38.306  1.00 79.96  ? 1070 HOH A O   1 
HETATM 6363 O O   . HOH W 7 .   ? -82.760  -18.697 -7.017  1.00 81.84  ? 1071 HOH A O   1 
HETATM 6364 O O   . HOH W 7 .   ? -47.471  16.146  34.549  1.00 81.23  ? 1072 HOH A O   1 
HETATM 6365 O O   . HOH W 7 .   ? -92.659  -22.606 46.241  1.00 72.18  ? 1073 HOH A O   1 
HETATM 6366 O O   . HOH W 7 .   ? -54.817  -29.206 16.431  1.00 70.09  ? 1074 HOH A O   1 
HETATM 6367 O O   . HOH W 7 .   ? -72.583  -4.479  33.248  1.00 73.40  ? 1075 HOH A O   1 
HETATM 6368 O O   . HOH W 7 .   ? -79.635  14.152  28.739  1.00 82.77  ? 1076 HOH A O   1 
HETATM 6369 O O   . HOH W 7 .   ? -60.771  6.867   52.591  1.00 57.63  ? 1077 HOH A O   1 
HETATM 6370 O O   . HOH W 7 .   ? -75.048  12.607  26.486  1.00 63.82  ? 1078 HOH A O   1 
HETATM 6371 O O   . HOH W 7 .   ? -66.318  3.336   20.683  1.00 66.25  ? 1079 HOH A O   1 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLU 1   27  ?   ?   ?   A . n 
A 1 2   GLU 2   28  ?   ?   ?   A . n 
A 1 3   ASN 3   29  ?   ?   ?   A . n 
A 1 4   PHE 4   30  ?   ?   ?   A . n 
A 1 5   SER 5   31  ?   ?   ?   A . n 
A 1 6   ARG 6   32  ?   ?   ?   A . n 
A 1 7   SER 7   33  33  SER SER A . n 
A 1 8   TYR 8   34  34  TYR TYR A . n 
A 1 9   PRO 9   35  35  PRO PRO A . n 
A 1 10  CYS 10  36  36  CYS CYS A . n 
A 1 11  ASP 11  37  37  ASP ASP A . n 
A 1 12  GLU 12  38  38  GLU GLU A . n 
A 1 13  LYS 13  39  39  LYS LYS A . n 
A 1 14  LYS 14  40  40  LYS LYS A . n 
A 1 15  GLN 15  41  41  GLN GLN A . n 
A 1 16  ASN 16  42  42  ASN ASN A . n 
A 1 17  ASP 17  43  43  ASP ASP A . n 
A 1 18  SER 18  44  44  SER SER A . n 
A 1 19  VAL 19  45  45  VAL VAL A . n 
A 1 20  ILE 20  46  46  ILE ILE A . n 
A 1 21  ALA 21  47  47  ALA ALA A . n 
A 1 22  GLU 22  48  48  GLU GLU A . n 
A 1 23  CYS 23  49  49  CYS CYS A . n 
A 1 24  SER 24  50  50  SER SER A . n 
A 1 25  ASN 25  51  51  ASN ASN A . n 
A 1 26  ARG 26  52  52  ARG ARG A . n 
A 1 27  ARG 27  53  53  ARG ARG A . n 
A 1 28  LEU 28  54  54  LEU LEU A . n 
A 1 29  GLN 29  55  55  GLN GLN A . n 
A 1 30  GLU 30  56  56  GLU GLU A . n 
A 1 31  VAL 31  57  57  VAL VAL A . n 
A 1 32  PRO 32  58  58  PRO PRO A . n 
A 1 33  GLN 33  59  59  GLN GLN A . n 
A 1 34  THR 34  60  60  THR THR A . n 
A 1 35  VAL 35  61  61  VAL VAL A . n 
A 1 36  GLY 36  62  62  GLY GLY A . n 
A 1 37  LYS 37  63  63  LYS LYS A . n 
A 1 38  TYR 38  64  64  TYR TYR A . n 
A 1 39  VAL 39  65  65  VAL VAL A . n 
A 1 40  THR 40  66  66  THR THR A . n 
A 1 41  GLU 41  67  67  GLU GLU A . n 
A 1 42  LEU 42  68  68  LEU LEU A . n 
A 1 43  ASP 43  69  69  ASP ASP A . n 
A 1 44  LEU 44  70  70  LEU LEU A . n 
A 1 45  SER 45  71  71  SER SER A . n 
A 1 46  ASP 46  72  72  ASP ASP A . n 
A 1 47  ASN 47  73  73  ASN ASN A . n 
A 1 48  PHE 48  74  74  PHE PHE A . n 
A 1 49  ILE 49  75  75  ILE ILE A . n 
A 1 50  THR 50  76  76  THR THR A . n 
A 1 51  HIS 51  77  77  HIS HIS A . n 
A 1 52  ILE 52  78  78  ILE ILE A . n 
A 1 53  THR 53  79  79  THR THR A . n 
A 1 54  ASN 54  80  80  ASN ASN A . n 
A 1 55  GLU 55  81  81  GLU GLU A . n 
A 1 56  SER 56  82  82  SER SER A . n 
A 1 57  PHE 57  83  83  PHE PHE A . n 
A 1 58  GLN 58  84  84  GLN GLN A . n 
A 1 59  GLY 59  85  85  GLY GLY A . n 
A 1 60  LEU 60  86  86  LEU LEU A . n 
A 1 61  GLN 61  87  87  GLN GLN A . n 
A 1 62  ASN 62  88  88  ASN ASN A . n 
A 1 63  LEU 63  89  89  LEU LEU A . n 
A 1 64  THR 64  90  90  THR THR A . n 
A 1 65  LYS 65  91  91  LYS LYS A . n 
A 1 66  ILE 66  92  92  ILE ILE A . n 
A 1 67  ASN 67  93  93  ASN ASN A . n 
A 1 68  LEU 68  94  94  LEU LEU A . n 
A 1 69  ASN 69  95  95  ASN ASN A . n 
A 1 70  HIS 70  96  96  HIS HIS A . n 
A 1 71  ASN 71  97  97  ASN ASN A . n 
A 1 72  PRO 72  98  98  PRO PRO A . n 
A 1 73  ASN 73  99  99  ASN ASN A . n 
A 1 74  VAL 74  100 100 VAL VAL A . n 
A 1 75  GLN 75  101 ?   ?   ?   A . n 
A 1 76  HIS 76  102 ?   ?   ?   A . n 
A 1 77  GLN 77  103 ?   ?   ?   A . n 
A 1 78  ASN 78  104 ?   ?   ?   A . n 
A 1 79  GLY 79  105 ?   ?   ?   A . n 
A 1 80  ASN 80  106 ?   ?   ?   A . n 
A 1 81  PRO 81  107 ?   ?   ?   A . n 
A 1 82  GLY 82  108 ?   ?   ?   A . n 
A 1 83  ILE 83  109 ?   ?   ?   A . n 
A 1 84  GLN 84  110 ?   ?   ?   A . n 
A 1 85  SER 85  111 ?   ?   ?   A . n 
A 1 86  ASN 86  112 ?   ?   ?   A . n 
A 1 87  GLY 87  113 113 GLY GLY A . n 
A 1 88  LEU 88  114 114 LEU LEU A . n 
A 1 89  ASN 89  115 115 ASN ASN A . n 
A 1 90  ILE 90  116 116 ILE ILE A . n 
A 1 91  THR 91  117 117 THR THR A . n 
A 1 92  ASP 92  118 118 ASP ASP A . n 
A 1 93  GLY 93  119 119 GLY GLY A . n 
A 1 94  ALA 94  120 120 ALA ALA A . n 
A 1 95  PHE 95  121 121 PHE PHE A . n 
A 1 96  LEU 96  122 122 LEU LEU A . n 
A 1 97  ASN 97  123 123 ASN ASN A . n 
A 1 98  LEU 98  124 124 LEU LEU A . n 
A 1 99  LYS 99  125 125 LYS LYS A . n 
A 1 100 ASN 100 126 126 ASN ASN A . n 
A 1 101 LEU 101 127 127 LEU LEU A . n 
A 1 102 ARG 102 128 128 ARG ARG A . n 
A 1 103 GLU 103 129 129 GLU GLU A . n 
A 1 104 LEU 104 130 130 LEU LEU A . n 
A 1 105 LEU 105 131 131 LEU LEU A . n 
A 1 106 LEU 106 132 132 LEU LEU A . n 
A 1 107 GLU 107 133 133 GLU GLU A . n 
A 1 108 ASP 108 134 134 ASP ASP A . n 
A 1 109 ASN 109 135 135 ASN ASN A . n 
A 1 110 GLN 110 136 136 GLN GLN A . n 
A 1 111 LEU 111 137 137 LEU LEU A . n 
A 1 112 PRO 112 138 138 PRO PRO A . n 
A 1 113 GLN 113 139 139 GLN GLN A . n 
A 1 114 ILE 114 140 140 ILE ILE A . n 
A 1 115 PRO 115 141 141 PRO PRO A . n 
A 1 116 SER 116 142 142 SER SER A . n 
A 1 117 GLY 117 143 143 GLY GLY A . n 
A 1 118 LEU 118 144 144 LEU LEU A . n 
A 1 119 PRO 119 145 145 PRO PRO A . n 
A 1 120 GLU 120 146 146 GLU GLU A . n 
A 1 121 SER 121 147 147 SER SER A . n 
A 1 122 LEU 122 148 148 LEU LEU A . n 
A 1 123 THR 123 149 149 THR THR A . n 
A 1 124 GLU 124 150 150 GLU GLU A . n 
A 1 125 LEU 125 151 151 LEU LEU A . n 
A 1 126 SER 126 152 152 SER SER A . n 
A 1 127 LEU 127 153 153 LEU LEU A . n 
A 1 128 ILE 128 154 154 ILE ILE A . n 
A 1 129 GLN 129 155 155 GLN GLN A . n 
A 1 130 ASN 130 156 156 ASN ASN A . n 
A 1 131 ASN 131 157 157 ASN ASN A . n 
A 1 132 ILE 132 158 158 ILE ILE A . n 
A 1 133 TYR 133 159 159 TYR TYR A . n 
A 1 134 ASN 134 160 160 ASN ASN A . n 
A 1 135 ILE 135 161 161 ILE ILE A . n 
A 1 136 THR 136 162 162 THR THR A . n 
A 1 137 LYS 137 163 163 LYS LYS A . n 
A 1 138 GLU 138 164 164 GLU GLU A . n 
A 1 139 GLY 139 165 165 GLY GLY A . n 
A 1 140 ILE 140 166 166 ILE ILE A . n 
A 1 141 SER 141 167 167 SER SER A . n 
A 1 142 ARG 142 168 168 ARG ARG A . n 
A 1 143 LEU 143 169 169 LEU LEU A . n 
A 1 144 ILE 144 170 170 ILE ILE A . n 
A 1 145 ASN 145 171 171 ASN ASN A . n 
A 1 146 LEU 146 172 172 LEU LEU A . n 
A 1 147 LYS 147 173 173 LYS LYS A . n 
A 1 148 ASN 148 174 174 ASN ASN A . n 
A 1 149 LEU 149 175 175 LEU LEU A . n 
A 1 150 TYR 150 176 176 TYR TYR A . n 
A 1 151 LEU 151 177 177 LEU LEU A . n 
A 1 152 ALA 152 178 178 ALA ALA A . n 
A 1 153 TRP 153 179 179 TRP TRP A . n 
A 1 154 ASN 154 180 180 ASN ASN A . n 
A 1 155 CYS 155 181 181 CYS CYS A . n 
A 1 156 TYR 156 182 182 TYR TYR A . n 
A 1 157 PHE 157 183 183 PHE PHE A . n 
A 1 158 ASN 158 184 184 ASN ASN A . n 
A 1 159 LYS 159 185 185 LYS LYS A . n 
A 1 160 VAL 160 186 186 VAL VAL A . n 
A 1 161 CYS 161 187 187 CYS CYS A . n 
A 1 162 GLU 162 188 188 GLU GLU A . n 
A 1 163 LYS 163 189 189 LYS LYS A . n 
A 1 164 THR 164 190 190 THR THR A . n 
A 1 165 ASN 165 191 191 ASN ASN A . n 
A 1 166 ILE 166 192 192 ILE ILE A . n 
A 1 167 GLU 167 193 193 GLU GLU A . n 
A 1 168 ASP 168 194 194 ASP ASP A . n 
A 1 169 GLY 169 195 195 GLY GLY A . n 
A 1 170 VAL 170 196 196 VAL VAL A . n 
A 1 171 PHE 171 197 197 PHE PHE A . n 
A 1 172 GLU 172 198 198 GLU GLU A . n 
A 1 173 THR 173 199 199 THR THR A . n 
A 1 174 LEU 174 200 200 LEU LEU A . n 
A 1 175 THR 175 201 201 THR THR A . n 
A 1 176 ASN 176 202 202 ASN ASN A . n 
A 1 177 LEU 177 203 203 LEU LEU A . n 
A 1 178 GLU 178 204 204 GLU GLU A . n 
A 1 179 LEU 179 205 205 LEU LEU A . n 
A 1 180 LEU 180 206 206 LEU LEU A . n 
A 1 181 SER 181 207 207 SER SER A . n 
A 1 182 LEU 182 208 208 LEU LEU A . n 
A 1 183 SER 183 209 209 SER SER A . n 
A 1 184 PHE 184 210 210 PHE PHE A . n 
A 1 185 ASN 185 211 211 ASN ASN A . n 
A 1 186 SER 186 212 212 SER SER A . n 
A 1 187 LEU 187 213 213 LEU LEU A . n 
A 1 188 SER 188 214 214 SER SER A . n 
A 1 189 HIS 189 215 215 HIS HIS A . n 
A 1 190 VAL 190 216 216 VAL VAL A . n 
A 1 191 PRO 191 217 217 PRO PRO A . n 
A 1 192 PRO 192 218 218 PRO PRO A . n 
A 1 193 LYS 193 219 219 LYS LYS A . n 
A 1 194 LEU 194 220 220 LEU LEU A . n 
A 1 195 PRO 195 221 221 PRO PRO A . n 
A 1 196 SER 196 222 222 SER SER A . n 
A 1 197 SER 197 223 223 SER SER A . n 
A 1 198 LEU 198 224 224 LEU LEU A . n 
A 1 199 ARG 199 225 225 ARG ARG A . n 
A 1 200 LYS 200 226 226 LYS LYS A . n 
A 1 201 LEU 201 227 227 LEU LEU A . n 
A 1 202 PHE 202 228 228 PHE PHE A . n 
A 1 203 LEU 203 229 229 LEU LEU A . n 
A 1 204 SER 204 230 230 SER SER A . n 
A 1 205 ASN 205 231 231 ASN ASN A . n 
A 1 206 THR 206 232 232 THR THR A . n 
A 1 207 GLN 207 233 233 GLN GLN A . n 
A 1 208 ILE 208 234 234 ILE ILE A . n 
A 1 209 LYS 209 235 235 LYS LYS A . n 
A 1 210 TYR 210 236 236 TYR TYR A . n 
A 1 211 ILE 211 237 237 ILE ILE A . n 
A 1 212 SER 212 238 238 SER SER A . n 
A 1 213 GLU 213 239 239 GLU GLU A . n 
A 1 214 GLU 214 240 240 GLU GLU A . n 
A 1 215 ASP 215 241 241 ASP ASP A . n 
A 1 216 PHE 216 242 242 PHE PHE A . n 
A 1 217 LYS 217 243 243 LYS LYS A . n 
A 1 218 GLY 218 244 244 GLY GLY A . n 
A 1 219 LEU 219 245 245 LEU LEU A . n 
A 1 220 ILE 220 246 246 ILE ILE A . n 
A 1 221 ASN 221 247 247 ASN ASN A . n 
A 1 222 LEU 222 248 248 LEU LEU A . n 
A 1 223 THR 223 249 249 THR THR A . n 
A 1 224 LEU 224 250 250 LEU LEU A . n 
A 1 225 LEU 225 251 251 LEU LEU A . n 
A 1 226 ASP 226 252 252 ASP ASP A . n 
A 1 227 LEU 227 253 253 LEU LEU A . n 
A 1 228 SER 228 254 254 SER SER A . n 
A 1 229 GLY 229 255 255 GLY GLY A . n 
A 1 230 ASN 230 256 256 ASN ASN A . n 
A 1 231 CYS 231 257 257 CYS CYS A . n 
A 1 232 PRO 232 258 258 PRO PRO A . n 
A 1 233 ARG 233 259 259 ARG ARG A . n 
A 1 234 CYS 234 260 260 CYS CYS A . n 
A 1 235 PHE 235 261 261 PHE PHE A . n 
A 1 236 ASN 236 262 262 ASN ASN A . n 
A 1 237 ALA 237 263 263 ALA ALA A . n 
A 1 238 PRO 238 264 264 PRO PRO A . n 
A 1 239 PHE 239 265 265 PHE PHE A . n 
A 1 240 PRO 240 266 266 PRO PRO A . n 
A 1 241 CYS 241 267 267 CYS CYS A . n 
A 1 242 VAL 242 268 268 VAL VAL A . n 
A 1 243 PRO 243 269 269 PRO PRO A . n 
A 1 244 CYS 244 270 270 CYS CYS A . n 
A 1 245 ASP 245 271 271 ASP ASP A . n 
A 1 246 GLY 246 272 272 GLY GLY A . n 
A 1 247 GLY 247 273 273 GLY GLY A . n 
A 1 248 ALA 248 274 274 ALA ALA A . n 
A 1 249 SER 249 275 275 SER SER A . n 
A 1 250 ILE 250 276 276 ILE ILE A . n 
A 1 251 ASN 251 277 277 ASN ASN A . n 
A 1 252 ILE 252 278 278 ILE ILE A . n 
A 1 253 ASP 253 279 279 ASP ASP A . n 
A 1 254 ARG 254 280 280 ARG ARG A . n 
A 1 255 PHE 255 281 281 PHE PHE A . n 
A 1 256 ALA 256 282 282 ALA ALA A . n 
A 1 257 PHE 257 283 283 PHE PHE A . n 
A 1 258 GLN 258 284 284 GLN GLN A . n 
A 1 259 ASN 259 285 285 ASN ASN A . n 
A 1 260 LEU 260 286 286 LEU LEU A . n 
A 1 261 THR 261 287 287 THR THR A . n 
A 1 262 GLN 262 288 288 GLN GLN A . n 
A 1 263 LEU 263 289 289 LEU LEU A . n 
A 1 264 ARG 264 290 290 ARG ARG A . n 
A 1 265 TYR 265 291 291 TYR TYR A . n 
A 1 266 LEU 266 292 292 LEU LEU A . n 
A 1 267 ASN 267 293 293 ASN ASN A . n 
A 1 268 LEU 268 294 294 LEU LEU A . n 
A 1 269 SER 269 295 295 SER SER A . n 
A 1 270 SER 270 296 296 SER SER A . n 
A 1 271 THR 271 297 297 THR THR A . n 
A 1 272 SER 272 298 298 SER SER A . n 
A 1 273 LEU 273 299 299 LEU LEU A . n 
A 1 274 ARG 274 300 300 ARG ARG A . n 
A 1 275 LYS 275 301 301 LYS LYS A . n 
A 1 276 ILE 276 302 302 ILE ILE A . n 
A 1 277 ASN 277 303 303 ASN ASN A . n 
A 1 278 ALA 278 304 304 ALA ALA A . n 
A 1 279 ALA 279 305 305 ALA ALA A . n 
A 1 280 TRP 280 306 306 TRP TRP A . n 
A 1 281 PHE 281 307 307 PHE PHE A . n 
A 1 282 LYS 282 308 308 LYS LYS A . n 
A 1 283 ASN 283 309 309 ASN ASN A . n 
A 1 284 MET 284 310 310 MET MET A . n 
A 1 285 PRO 285 311 311 PRO PRO A . n 
A 1 286 HIS 286 312 312 HIS HIS A . n 
A 1 287 LEU 287 313 313 LEU LEU A . n 
A 1 288 LYS 288 314 314 LYS LYS A . n 
A 1 289 VAL 289 315 315 VAL VAL A . n 
A 1 290 LEU 290 316 316 LEU LEU A . n 
A 1 291 ASP 291 317 317 ASP ASP A . n 
A 1 292 LEU 292 318 318 LEU LEU A . n 
A 1 293 GLU 293 319 319 GLU GLU A . n 
A 1 294 PHE 294 320 320 PHE PHE A . n 
A 1 295 ASN 295 321 321 ASN ASN A . n 
A 1 296 TYR 296 322 322 TYR TYR A . n 
A 1 297 LEU 297 323 323 LEU LEU A . n 
A 1 298 VAL 298 324 324 VAL VAL A . n 
A 1 299 GLY 299 325 325 GLY GLY A . n 
A 1 300 GLU 300 326 326 GLU GLU A . n 
A 1 301 ILE 301 327 327 ILE ILE A . n 
A 1 302 ALA 302 328 328 ALA ALA A . n 
A 1 303 SER 303 329 329 SER SER A . n 
A 1 304 GLY 304 330 330 GLY GLY A . n 
A 1 305 ALA 305 331 331 ALA ALA A . n 
A 1 306 PHE 306 332 332 PHE PHE A . n 
A 1 307 LEU 307 333 333 LEU LEU A . n 
A 1 308 THR 308 334 334 THR THR A . n 
A 1 309 MET 309 335 335 MET MET A . n 
A 1 310 LEU 310 336 336 LEU LEU A . n 
A 1 311 PRO 311 337 337 PRO PRO A . n 
A 1 312 ARG 312 338 338 ARG ARG A . n 
A 1 313 LEU 313 339 339 LEU LEU A . n 
A 1 314 GLU 314 340 340 GLU GLU A . n 
A 1 315 ILE 315 341 341 ILE ILE A . n 
A 1 316 LEU 316 342 342 LEU LEU A . n 
A 1 317 ASP 317 343 343 ASP ASP A . n 
A 1 318 LEU 318 344 344 LEU LEU A . n 
A 1 319 SER 319 345 345 SER SER A . n 
A 1 320 PHE 320 346 346 PHE PHE A . n 
A 1 321 ASN 321 347 347 ASN ASN A . n 
A 1 322 TYR 322 348 348 TYR TYR A . n 
A 1 323 ILE 323 349 349 ILE ILE A . n 
A 1 324 LYS 324 350 350 LYS LYS A . n 
A 1 325 GLY 325 351 351 GLY GLY A . n 
A 1 326 SER 326 352 352 SER SER A . n 
A 1 327 TYR 327 353 353 TYR TYR A . n 
A 1 328 PRO 328 354 354 PRO PRO A . n 
A 1 329 GLN 329 355 355 GLN GLN A . n 
A 1 330 HIS 330 356 356 HIS HIS A . n 
A 1 331 ILE 331 357 357 ILE ILE A . n 
A 1 332 ASN 332 358 358 ASN ASN A . n 
A 1 333 ILE 333 359 359 ILE ILE A . n 
A 1 334 SER 334 360 360 SER SER A . n 
A 1 335 ARG 335 361 361 ARG ARG A . n 
A 1 336 ASN 336 362 362 ASN ASN A . n 
A 1 337 PHE 337 363 363 PHE PHE A . n 
A 1 338 SER 338 364 364 SER SER A . n 
A 1 339 LYS 339 365 365 LYS LYS A . n 
A 1 340 LEU 340 366 366 LEU LEU A . n 
A 1 341 LEU 341 367 367 LEU LEU A . n 
A 1 342 SER 342 368 368 SER SER A . n 
A 1 343 LEU 343 369 369 LEU LEU A . n 
A 1 344 ARG 344 370 370 ARG ARG A . n 
A 1 345 ALA 345 371 371 ALA ALA A . n 
A 1 346 LEU 346 372 372 LEU LEU A . n 
A 1 347 HIS 347 373 373 HIS HIS A . n 
A 1 348 LEU 348 374 374 LEU LEU A . n 
A 1 349 ARG 349 375 375 ARG ARG A . n 
A 1 350 GLY 350 376 376 GLY GLY A . n 
A 1 351 TYR 351 377 377 TYR TYR A . n 
A 1 352 VAL 352 378 378 VAL VAL A . n 
A 1 353 PHE 353 379 379 PHE PHE A . n 
A 1 354 GLN 354 380 380 GLN GLN A . n 
A 1 355 GLU 355 381 381 GLU GLU A . n 
A 1 356 LEU 356 382 382 LEU LEU A . n 
A 1 357 ARG 357 383 383 ARG ARG A . n 
A 1 358 GLU 358 384 384 GLU GLU A . n 
A 1 359 ASP 359 385 385 ASP ASP A . n 
A 1 360 ASP 360 386 386 ASP ASP A . n 
A 1 361 PHE 361 387 387 PHE PHE A . n 
A 1 362 GLN 362 388 388 GLN GLN A . n 
A 1 363 PRO 363 389 389 PRO PRO A . n 
A 1 364 LEU 364 390 390 LEU LEU A . n 
A 1 365 MET 365 391 391 MET MET A . n 
A 1 366 GLN 366 392 392 GLN GLN A . n 
A 1 367 LEU 367 393 393 LEU LEU A . n 
A 1 368 PRO 368 394 394 PRO PRO A . n 
A 1 369 ASN 369 395 395 ASN ASN A . n 
A 1 370 LEU 370 396 396 LEU LEU A . n 
A 1 371 SER 371 397 397 SER SER A . n 
A 1 372 THR 372 398 398 THR THR A . n 
A 1 373 ILE 373 399 399 ILE ILE A . n 
A 1 374 ASN 374 400 400 ASN ASN A . n 
A 1 375 LEU 375 401 401 LEU LEU A . n 
A 1 376 GLY 376 402 402 GLY GLY A . n 
A 1 377 ILE 377 403 403 ILE ILE A . n 
A 1 378 ASN 378 404 404 ASN ASN A . n 
A 1 379 PHE 379 405 405 PHE PHE A . n 
A 1 380 ILE 380 406 406 ILE ILE A . n 
A 1 381 LYS 381 407 407 LYS LYS A . n 
A 1 382 GLN 382 408 408 GLN GLN A . n 
A 1 383 ILE 383 409 409 ILE ILE A . n 
A 1 384 ASP 384 410 410 ASP ASP A . n 
A 1 385 PHE 385 411 411 PHE PHE A . n 
A 1 386 LYS 386 412 412 LYS LYS A . n 
A 1 387 LEU 387 413 413 LEU LEU A . n 
A 1 388 PHE 388 414 414 PHE PHE A . n 
A 1 389 GLN 389 415 415 GLN GLN A . n 
A 1 390 ASN 390 416 416 ASN ASN A . n 
A 1 391 PHE 391 417 417 PHE PHE A . n 
A 1 392 SER 392 418 418 SER SER A . n 
A 1 393 ASN 393 419 419 ASN ASN A . n 
A 1 394 LEU 394 420 420 LEU LEU A . n 
A 1 395 GLU 395 421 421 GLU GLU A . n 
A 1 396 ILE 396 422 422 ILE ILE A . n 
A 1 397 ILE 397 423 423 ILE ILE A . n 
A 1 398 TYR 398 424 424 TYR TYR A . n 
A 1 399 LEU 399 425 425 LEU LEU A . n 
A 1 400 SER 400 426 426 SER SER A . n 
A 1 401 GLU 401 427 427 GLU GLU A . n 
A 1 402 ASN 402 428 428 ASN ASN A . n 
A 1 403 ARG 403 429 429 ARG ARG A . n 
A 1 404 ILE 404 430 430 ILE ILE A . n 
A 1 405 SER 405 431 431 SER SER A . n 
A 1 406 PRO 406 432 432 PRO PRO A . n 
A 1 407 LEU 407 433 433 LEU LEU A . n 
A 1 408 VAL 408 434 434 VAL VAL A . n 
A 1 409 LYS 409 435 ?   ?   ?   A . n 
A 1 410 ASP 410 436 ?   ?   ?   A . n 
A 1 411 THR 411 437 ?   ?   ?   A . n 
A 1 412 ARG 412 438 ?   ?   ?   A . n 
A 1 413 GLN 413 439 ?   ?   ?   A . n 
A 1 414 SER 414 440 ?   ?   ?   A . n 
A 1 415 TYR 415 441 ?   ?   ?   A . n 
A 1 416 ALA 416 442 ?   ?   ?   A . n 
A 1 417 ASN 417 443 443 ASN ASN A . n 
A 1 418 SER 418 444 444 SER SER A . n 
A 1 419 SER 419 445 445 SER SER A . n 
A 1 420 SER 420 446 446 SER SER A . n 
A 1 421 PHE 421 447 447 PHE PHE A . n 
A 1 422 GLN 422 448 448 GLN GLN A . n 
A 1 423 ARG 423 449 449 ARG ARG A . n 
A 1 424 HIS 424 450 450 HIS HIS A . n 
A 1 425 ILE 425 451 451 ILE ILE A . n 
A 1 426 ASN 426 452 ?   ?   ?   A . n 
A 1 427 GLN 427 453 ?   ?   ?   A . n 
A 1 428 SER 428 454 ?   ?   ?   A . n 
A 1 429 ASN 429 455 ?   ?   ?   A . n 
A 1 430 SER 430 456 ?   ?   ?   A . n 
A 1 431 THR 431 457 ?   ?   ?   A . n 
A 1 432 ASP 432 458 ?   ?   ?   A . n 
A 1 433 PHE 433 459 ?   ?   ?   A . n 
A 1 434 GLU 434 460 ?   ?   ?   A . n 
A 1 435 PHE 435 461 ?   ?   ?   A . n 
A 1 436 ASP 436 462 ?   ?   ?   A . n 
A 1 437 PRO 437 463 463 PRO PRO A . n 
A 1 438 HIS 438 464 464 HIS HIS A . n 
A 1 439 SER 439 465 465 SER SER A . n 
A 1 440 ASN 440 466 466 ASN ASN A . n 
A 1 441 PHE 441 467 467 PHE PHE A . n 
A 1 442 TYR 442 468 468 TYR TYR A . n 
A 1 443 HIS 443 469 469 HIS HIS A . n 
A 1 444 PHE 444 470 470 PHE PHE A . n 
A 1 445 THR 445 471 471 THR THR A . n 
A 1 446 ARG 446 472 472 ARG ARG A . n 
A 1 447 PRO 447 473 473 PRO PRO A . n 
A 1 448 LEU 448 474 474 LEU LEU A . n 
A 1 449 ILE 449 475 475 ILE ILE A . n 
A 1 450 LYS 450 476 476 LYS LYS A . n 
A 1 451 PRO 451 477 477 PRO PRO A . n 
A 1 452 GLN 452 478 478 GLN GLN A . n 
A 1 453 CYS 453 479 479 CYS CYS A . n 
A 1 454 ALA 454 480 480 ALA ALA A . n 
A 1 455 ALA 455 481 481 ALA ALA A . n 
A 1 456 TYR 456 482 482 TYR TYR A . n 
A 1 457 GLY 457 483 483 GLY GLY A . n 
A 1 458 LYS 458 484 484 LYS LYS A . n 
A 1 459 ALA 459 485 485 ALA ALA A . n 
A 1 460 LEU 460 486 486 LEU LEU A . n 
A 1 461 ASP 461 487 487 ASP ASP A . n 
A 1 462 LEU 462 488 488 LEU LEU A . n 
A 1 463 SER 463 489 489 SER SER A . n 
A 1 464 LEU 464 490 490 LEU LEU A . n 
A 1 465 ASN 465 491 491 ASN ASN A . n 
A 1 466 SER 466 492 492 SER SER A . n 
A 1 467 ILE 467 493 493 ILE ILE A . n 
A 1 468 PHE 468 494 494 PHE PHE A . n 
A 1 469 PHE 469 495 495 PHE PHE A . n 
A 1 470 ILE 470 496 496 ILE ILE A . n 
A 1 471 GLY 471 497 497 GLY GLY A . n 
A 1 472 PRO 472 498 498 PRO PRO A . n 
A 1 473 ASN 473 499 499 ASN ASN A . n 
A 1 474 GLN 474 500 500 GLN GLN A . n 
A 1 475 PHE 475 501 501 PHE PHE A . n 
A 1 476 GLU 476 502 502 GLU GLU A . n 
A 1 477 ASN 477 503 503 ASN ASN A . n 
A 1 478 LEU 478 504 504 LEU LEU A . n 
A 1 479 PRO 479 505 505 PRO PRO A . n 
A 1 480 ASP 480 506 506 ASP ASP A . n 
A 1 481 ILE 481 507 507 ILE ILE A . n 
A 1 482 ALA 482 508 508 ALA ALA A . n 
A 1 483 CYS 483 509 509 CYS CYS A . n 
A 1 484 LEU 484 510 510 LEU LEU A . n 
A 1 485 ASN 485 511 511 ASN ASN A . n 
A 1 486 LEU 486 512 512 LEU LEU A . n 
A 1 487 SER 487 513 513 SER SER A . n 
A 1 488 ALA 488 514 514 ALA ALA A . n 
A 1 489 ASN 489 515 515 ASN ASN A . n 
A 1 490 SER 490 516 516 SER SER A . n 
A 1 491 ASN 491 517 517 ASN ASN A . n 
A 1 492 ALA 492 518 518 ALA ALA A . n 
A 1 493 GLN 493 519 519 GLN GLN A . n 
A 1 494 VAL 494 520 520 VAL VAL A . n 
A 1 495 LEU 495 521 521 LEU LEU A . n 
A 1 496 SER 496 522 522 SER SER A . n 
A 1 497 GLY 497 523 523 GLY GLY A . n 
A 1 498 THR 498 524 524 THR THR A . n 
A 1 499 GLU 499 525 525 GLU GLU A . n 
A 1 500 PHE 500 526 526 PHE PHE A . n 
A 1 501 SER 501 527 527 SER SER A . n 
A 1 502 ALA 502 528 528 ALA ALA A . n 
A 1 503 ILE 503 529 529 ILE ILE A . n 
A 1 504 PRO 504 530 530 PRO PRO A . n 
A 1 505 HIS 505 531 531 HIS HIS A . n 
A 1 506 VAL 506 532 532 VAL VAL A . n 
A 1 507 LYS 507 533 533 LYS LYS A . n 
A 1 508 TYR 508 534 534 TYR TYR A . n 
A 1 509 LEU 509 535 535 LEU LEU A . n 
A 1 510 ASP 510 536 536 ASP ASP A . n 
A 1 511 LEU 511 537 537 LEU LEU A . n 
A 1 512 THR 512 538 538 THR THR A . n 
A 1 513 ASN 513 539 539 ASN ASN A . n 
A 1 514 ASN 514 540 540 ASN ASN A . n 
A 1 515 ARG 515 541 541 ARG ARG A . n 
A 1 516 LEU 516 542 542 LEU LEU A . n 
A 1 517 ASP 517 543 543 ASP ASP A . n 
A 1 518 PHE 518 544 544 PHE PHE A . n 
A 1 519 ASP 519 545 545 ASP ASP A . n 
A 1 520 ASN 520 546 546 ASN ASN A . n 
A 1 521 ALA 521 547 547 ALA ALA A . n 
A 1 522 SER 522 548 548 SER SER A . n 
A 1 523 ALA 523 549 549 ALA ALA A . n 
A 1 524 LEU 524 550 550 LEU LEU A . n 
A 1 525 THR 525 551 551 THR THR A . n 
A 1 526 GLU 526 552 552 GLU GLU A . n 
A 1 527 LEU 527 553 553 LEU LEU A . n 
A 1 528 SER 528 554 554 SER SER A . n 
A 1 529 ASP 529 555 555 ASP ASP A . n 
A 1 530 LEU 530 556 556 LEU LEU A . n 
A 1 531 GLU 531 557 557 GLU GLU A . n 
A 1 532 VAL 532 558 558 VAL VAL A . n 
A 1 533 LEU 533 559 559 LEU LEU A . n 
A 1 534 ASP 534 560 560 ASP ASP A . n 
A 1 535 LEU 535 561 561 LEU LEU A . n 
A 1 536 SER 536 562 562 SER SER A . n 
A 1 537 TYR 537 563 563 TYR TYR A . n 
A 1 538 ASN 538 564 564 ASN ASN A . n 
A 1 539 SER 539 565 565 SER SER A . n 
A 1 540 HIS 540 566 566 HIS HIS A . n 
A 1 541 TYR 541 567 567 TYR TYR A . n 
A 1 542 PHE 542 568 568 PHE PHE A . n 
A 1 543 ARG 543 569 569 ARG ARG A . n 
A 1 544 ILE 544 570 570 ILE ILE A . n 
A 1 545 ALA 545 571 571 ALA ALA A . n 
A 1 546 GLY 546 572 572 GLY GLY A . n 
A 1 547 VAL 547 573 573 VAL VAL A . n 
A 1 548 THR 548 574 574 THR THR A . n 
A 1 549 HIS 549 575 575 HIS HIS A . n 
A 1 550 HIS 550 576 576 HIS HIS A . n 
A 1 551 LEU 551 577 577 LEU LEU A . n 
A 1 552 GLU 552 578 578 GLU GLU A . n 
A 1 553 PHE 553 579 579 PHE PHE A . n 
A 1 554 ILE 554 580 580 ILE ILE A . n 
A 1 555 GLN 555 581 581 GLN GLN A . n 
A 1 556 ASN 556 582 582 ASN ASN A . n 
A 1 557 PHE 557 583 583 PHE PHE A . n 
A 1 558 THR 558 584 584 THR THR A . n 
A 1 559 ASN 559 585 585 ASN ASN A . n 
A 1 560 LEU 560 586 586 LEU LEU A . n 
A 1 561 LYS 561 587 587 LYS LYS A . n 
A 1 562 VAL 562 588 588 VAL VAL A . n 
A 1 563 LEU 563 589 589 LEU LEU A . n 
A 1 564 ASN 564 590 590 ASN ASN A . n 
A 1 565 LEU 565 591 591 LEU LEU A . n 
A 1 566 SER 566 592 592 SER SER A . n 
A 1 567 HIS 567 593 593 HIS HIS A . n 
A 1 568 ASN 568 594 594 ASN ASN A . n 
A 1 569 ASN 569 595 595 ASN ASN A . n 
A 1 570 ILE 570 596 596 ILE ILE A . n 
A 1 571 TYR 571 597 597 TYR TYR A . n 
A 1 572 THR 572 598 598 THR THR A . n 
A 1 573 LEU 573 599 599 LEU LEU A . n 
A 1 574 THR 574 600 600 THR THR A . n 
A 1 575 ASP 575 601 601 ASP ASP A . n 
A 1 576 LYS 576 602 602 LYS LYS A . n 
A 1 577 TYR 577 603 603 TYR TYR A . n 
A 1 578 ASN 578 604 604 ASN ASN A . n 
A 1 579 LEU 579 605 605 LEU LEU A . n 
A 1 580 GLU 580 606 606 GLU GLU A . n 
A 1 581 SER 581 607 607 SER SER A . n 
A 1 582 LYS 582 608 608 LYS LYS A . n 
A 1 583 SER 583 609 609 SER SER A . n 
A 1 584 LEU 584 610 610 LEU LEU A . n 
A 1 585 VAL 585 611 611 VAL VAL A . n 
A 1 586 GLU 586 612 612 GLU GLU A . n 
A 1 587 LEU 587 613 613 LEU LEU A . n 
A 1 588 VAL 588 614 614 VAL VAL A . n 
A 1 589 PHE 589 615 615 PHE PHE A . n 
A 1 590 SER 590 616 616 SER SER A . n 
A 1 591 GLY 591 617 617 GLY GLY A . n 
A 1 592 ASN 592 618 618 ASN ASN A . n 
A 1 593 ARG 593 619 619 ARG ARG A . n 
A 1 594 LEU 594 620 620 LEU LEU A . n 
A 1 595 ASP 595 621 621 ASP ASP A . n 
A 1 596 ILE 596 622 622 ILE ILE A . n 
A 1 597 LEU 597 623 623 LEU LEU A . n 
A 1 598 TRP 598 624 624 TRP TRP A . n 
A 1 599 ASN 599 625 625 ASN ASN A . n 
A 1 600 ASP 600 626 626 ASP ASP A . n 
A 1 601 ASP 601 627 627 ASP ASP A . n 
A 1 602 ASP 602 628 628 ASP ASP A . n 
A 1 603 ASN 603 629 629 ASN ASN A . n 
A 1 604 ARG 604 630 630 ARG ARG A . n 
A 1 605 TYR 605 631 631 TYR TYR A . n 
A 1 606 ILE 606 632 632 ILE ILE A . n 
A 1 607 SER 607 633 633 SER SER A . n 
A 1 608 ILE 608 634 634 ILE ILE A . n 
A 1 609 PHE 609 635 635 PHE PHE A . n 
A 1 610 LYS 610 636 636 LYS LYS A . n 
A 1 611 GLY 611 637 637 GLY GLY A . n 
A 1 612 LEU 612 638 638 LEU LEU A . n 
A 1 613 LYS 613 639 639 LYS LYS A . n 
A 1 614 ASN 614 640 640 ASN ASN A . n 
A 1 615 LEU 615 641 641 LEU LEU A . n 
A 1 616 THR 616 642 642 THR THR A . n 
A 1 617 ARG 617 643 643 ARG ARG A . n 
A 1 618 LEU 618 644 644 LEU LEU A . n 
A 1 619 ASP 619 645 645 ASP ASP A . n 
A 1 620 LEU 620 646 646 LEU LEU A . n 
A 1 621 SER 621 647 647 SER SER A . n 
A 1 622 LEU 622 648 648 LEU LEU A . n 
A 1 623 ASN 623 649 649 ASN ASN A . n 
A 1 624 ARG 624 650 650 ARG ARG A . n 
A 1 625 LEU 625 651 651 LEU LEU A . n 
A 1 626 LYS 626 652 652 LYS LYS A . n 
A 1 627 HIS 627 653 653 HIS HIS A . n 
A 1 628 ILE 628 654 654 ILE ILE A . n 
A 1 629 PRO 629 655 655 PRO PRO A . n 
A 1 630 ASN 630 656 656 ASN ASN A . n 
A 1 631 GLU 631 657 657 GLU GLU A . n 
A 1 632 ALA 632 658 658 ALA ALA A . n 
A 1 633 PHE 633 659 659 PHE PHE A . n 
A 1 634 LEU 634 660 660 LEU LEU A . n 
A 1 635 ASN 635 661 661 ASN ASN A . n 
A 1 636 LEU 636 662 662 LEU LEU A . n 
A 1 637 PRO 637 663 663 PRO PRO A . n 
A 1 638 ALA 638 664 664 ALA ALA A . n 
A 1 639 SER 639 665 665 SER SER A . n 
A 1 640 LEU 640 666 666 LEU LEU A . n 
A 1 641 THR 641 667 667 THR THR A . n 
A 1 642 GLU 642 668 668 GLU GLU A . n 
A 1 643 LEU 643 669 669 LEU LEU A . n 
A 1 644 HIS 644 670 670 HIS HIS A . n 
A 1 645 ILE 645 671 671 ILE ILE A . n 
A 1 646 ASN 646 672 672 ASN ASN A . n 
A 1 647 ASP 647 673 673 ASP ASP A . n 
A 1 648 ASN 648 674 674 ASN ASN A . n 
A 1 649 MET 649 675 675 MET MET A . n 
A 1 650 LEU 650 676 676 LEU LEU A . n 
A 1 651 LYS 651 677 677 LYS LYS A . n 
A 1 652 PHE 652 678 678 PHE PHE A . n 
A 1 653 PHE 653 679 679 PHE PHE A . n 
A 1 654 ASN 654 680 680 ASN ASN A . n 
A 1 655 TRP 655 681 681 TRP TRP A . n 
A 1 656 THR 656 682 682 THR THR A . n 
A 1 657 LEU 657 683 683 LEU LEU A . n 
A 1 658 LEU 658 684 684 LEU LEU A . n 
A 1 659 GLN 659 685 685 GLN GLN A . n 
A 1 660 GLN 660 686 686 GLN GLN A . n 
A 1 661 PHE 661 687 687 PHE PHE A . n 
A 1 662 PRO 662 688 688 PRO PRO A . n 
A 1 663 ARG 663 689 689 ARG ARG A . n 
A 1 664 LEU 664 690 690 LEU LEU A . n 
A 1 665 GLU 665 691 691 GLU GLU A . n 
A 1 666 LEU 666 692 692 LEU LEU A . n 
A 1 667 LEU 667 693 693 LEU LEU A . n 
A 1 668 ASP 668 694 694 ASP ASP A . n 
A 1 669 LEU 669 695 695 LEU LEU A . n 
A 1 670 ARG 670 696 696 ARG ARG A . n 
A 1 671 GLY 671 697 697 GLY GLY A . n 
A 1 672 ASN 672 698 698 ASN ASN A . n 
A 1 673 LYS 673 699 699 LYS LYS A . n 
A 1 674 LEU 674 700 700 LEU LEU A . n 
A 1 675 LEU 675 701 701 LEU LEU A . n 
A 1 676 PHE 676 702 702 PHE PHE A . n 
A 1 677 LEU 677 703 703 LEU LEU A . n 
A 1 678 THR 678 704 704 THR THR A . n 
A 1 679 ASP 679 705 705 ASP ASP A . n 
A 1 680 SER 680 706 706 SER SER A . n 
A 1 681 LEU 681 707 707 LEU LEU A . n 
A 1 682 SER 682 708 708 SER SER A . n 
A 1 683 ASP 683 709 709 ASP ASP A . n 
A 1 684 PHE 684 710 710 PHE PHE A . n 
A 1 685 THR 685 711 711 THR THR A . n 
A 1 686 SER 686 712 712 SER SER A . n 
A 1 687 SER 687 713 713 SER SER A . n 
A 1 688 LEU 688 714 714 LEU LEU A . n 
A 1 689 ARG 689 715 715 ARG ARG A . n 
A 1 690 THR 690 716 716 THR THR A . n 
A 1 691 LEU 691 717 717 LEU LEU A . n 
A 1 692 LEU 692 718 718 LEU LEU A . n 
A 1 693 LEU 693 719 719 LEU LEU A . n 
A 1 694 SER 694 720 720 SER SER A . n 
A 1 695 HIS 695 721 721 HIS HIS A . n 
A 1 696 ASN 696 722 722 ASN ASN A . n 
A 1 697 ARG 697 723 723 ARG ARG A . n 
A 1 698 ILE 698 724 724 ILE ILE A . n 
A 1 699 SER 699 725 725 SER SER A . n 
A 1 700 HIS 700 726 726 HIS HIS A . n 
A 1 701 LEU 701 727 727 LEU LEU A . n 
A 1 702 PRO 702 728 728 PRO PRO A . n 
A 1 703 SER 703 729 729 SER SER A . n 
A 1 704 GLY 704 730 730 GLY GLY A . n 
A 1 705 PHE 705 731 731 PHE PHE A . n 
A 1 706 LEU 706 732 732 LEU LEU A . n 
A 1 707 SER 707 733 ?   ?   ?   A . n 
A 1 708 GLU 708 734 ?   ?   ?   A . n 
A 1 709 VAL 709 735 ?   ?   ?   A . n 
A 1 710 SER 710 736 736 SER SER A . n 
A 1 711 SER 711 737 737 SER SER A . n 
A 1 712 LEU 712 738 738 LEU LEU A . n 
A 1 713 LYS 713 739 739 LYS LYS A . n 
A 1 714 HIS 714 740 740 HIS HIS A . n 
A 1 715 LEU 715 741 741 LEU LEU A . n 
A 1 716 ASP 716 742 742 ASP ASP A . n 
A 1 717 LEU 717 743 743 LEU LEU A . n 
A 1 718 SER 718 744 744 SER SER A . n 
A 1 719 SER 719 745 745 SER SER A . n 
A 1 720 ASN 720 746 746 ASN ASN A . n 
A 1 721 LEU 721 747 747 LEU LEU A . n 
A 1 722 LEU 722 748 748 LEU LEU A . n 
A 1 723 LYS 723 749 749 LYS LYS A . n 
A 1 724 THR 724 750 750 THR THR A . n 
A 1 725 ILE 725 751 751 ILE ILE A . n 
A 1 726 ASN 726 752 752 ASN ASN A . n 
A 1 727 LYS 727 753 753 LYS LYS A . n 
A 1 728 SER 728 754 754 SER SER A . n 
A 1 729 ALA 729 755 755 ALA ALA A . n 
A 1 730 LEU 730 756 756 LEU LEU A . n 
A 1 731 GLU 731 757 ?   ?   ?   A . n 
A 1 732 THR 732 758 ?   ?   ?   A . n 
A 1 733 LYS 733 759 ?   ?   ?   A . n 
A 1 734 THR 734 760 ?   ?   ?   A . n 
A 1 735 THR 735 761 ?   ?   ?   A . n 
A 1 736 THR 736 762 ?   ?   ?   A . n 
A 1 737 LYS 737 763 763 LYS LYS A . n 
A 1 738 LEU 738 764 764 LEU LEU A . n 
A 1 739 SER 739 765 765 SER SER A . n 
A 1 740 MET 740 766 766 MET MET A . n 
A 1 741 LEU 741 767 767 LEU LEU A . n 
A 1 742 GLU 742 768 768 GLU GLU A . n 
A 1 743 LEU 743 769 769 LEU LEU A . n 
A 1 744 HIS 744 770 770 HIS HIS A . n 
A 1 745 GLY 745 771 771 GLY GLY A . n 
A 1 746 ASN 746 772 772 ASN ASN A . n 
A 1 747 PRO 747 773 773 PRO PRO A . n 
A 1 748 PHE 748 774 774 PHE PHE A . n 
A 1 749 GLU 749 775 775 GLU GLU A . n 
A 1 750 CYS 750 776 776 CYS CYS A . n 
A 1 751 THR 751 777 777 THR THR A . n 
A 1 752 CYS 752 778 778 CYS CYS A . n 
A 1 753 ASP 753 779 779 ASP ASP A . n 
A 1 754 ILE 754 780 780 ILE ILE A . n 
A 1 755 GLY 755 781 781 GLY GLY A . n 
A 1 756 ASP 756 782 782 ASP ASP A . n 
A 1 757 PHE 757 783 783 PHE PHE A . n 
A 1 758 ARG 758 784 784 ARG ARG A . n 
A 1 759 ARG 759 785 785 ARG ARG A . n 
A 1 760 TRP 760 786 786 TRP TRP A . n 
A 1 761 MET 761 787 787 MET MET A . n 
A 1 762 ASP 762 788 788 ASP ASP A . n 
A 1 763 GLU 763 789 789 GLU GLU A . n 
A 1 764 HIS 764 790 790 HIS HIS A . n 
A 1 765 LEU 765 791 791 LEU LEU A . n 
A 1 766 ASN 766 792 792 ASN ASN A . n 
A 1 767 VAL 767 793 793 VAL VAL A . n 
A 1 768 LYS 768 794 794 LYS LYS A . n 
A 1 769 ILE 769 795 795 ILE ILE A . n 
A 1 770 PRO 770 796 796 PRO PRO A . n 
A 1 771 ARG 771 797 797 ARG ARG A . n 
A 1 772 LEU 772 798 798 LEU LEU A . n 
A 1 773 VAL 773 799 799 VAL VAL A . n 
A 1 774 ASP 774 800 800 ASP ASP A . n 
A 1 775 VAL 775 801 801 VAL VAL A . n 
A 1 776 ILE 776 802 802 ILE ILE A . n 
A 1 777 CYS 777 803 803 CYS CYS A . n 
A 1 778 ALA 778 804 804 ALA ALA A . n 
A 1 779 SER 779 805 805 SER SER A . n 
A 1 780 PRO 780 806 806 PRO PRO A . n 
A 1 781 GLY 781 807 807 GLY GLY A . n 
A 1 782 ASP 782 808 808 ASP ASP A . n 
A 1 783 GLN 783 809 809 GLN GLN A . n 
A 1 784 ARG 784 810 810 ARG ARG A . n 
A 1 785 GLY 785 811 811 GLY GLY A . n 
A 1 786 LYS 786 812 812 LYS LYS A . n 
A 1 787 SER 787 813 813 SER SER A . n 
A 1 788 ILE 788 814 814 ILE ILE A . n 
A 1 789 VAL 789 815 815 VAL VAL A . n 
A 1 790 SER 790 816 816 SER SER A . n 
A 1 791 LEU 791 817 817 LEU LEU A . n 
A 1 792 GLU 792 818 818 GLU GLU A . n 
A 1 793 LEU 793 819 819 LEU LEU A . n 
A 1 794 THR 794 820 820 THR THR A . n 
A 1 795 THR 795 821 821 THR THR A . n 
A 1 796 CYS 796 822 822 CYS CYS A . n 
A 1 797 VAL 797 823 823 VAL VAL A . n 
A 1 798 SER 798 824 ?   ?   ?   A . n 
A 1 799 ASP 799 825 ?   ?   ?   A . n 
A 1 800 VAL 800 826 ?   ?   ?   A . n 
A 1 801 THR 801 827 ?   ?   ?   A . 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 
B 2 NAG 1  901  1070 NAG NAG A . 
C 2 NAG 1  902  1080 NAG NAG A . 
D 2 NAG 2  903  1081 NAG NAG A . 
E 3 BMA 3  904  1082 BMA BMA A . 
F 4 MAN 4  905  1083 MAN MAN A . 
G 2 NAG 1  906  1110 NAG NAG A . 
H 2 NAG 1  907  1120 NAG NAG A . 
I 2 NAG 1  908  1140 NAG NAG A . 
J 2 NAG 2  909  1141 NAG NAG A . 
K 2 NAG 1  910  1150 NAG NAG A . 
L 2 NAG 1  911  1160 NAG NAG A . 
M 2 NAG 1  912  1170 NAG NAG A . 
N 2 NAG 2  913  1171 NAG NAG A . 
O 3 BMA 3  914  1172 BMA BMA A . 
P 4 MAN 4  915  1173 MAN MAN A . 
Q 4 MAN 5  916  1174 MAN MAN A . 
R 2 NAG 1  917  1180 NAG NAG A . 
S 5 SO4 1  918  1    SO4 SO4 A . 
T 5 SO4 1  919  2    SO4 SO4 A . 
U 5 SO4 1  920  3    SO4 SO4 A . 
V 6 MES 1  921  1    MES MES A . 
W 7 HOH 1  1001 95   HOH HOH A . 
W 7 HOH 2  1002 77   HOH HOH A . 
W 7 HOH 3  1003 50   HOH HOH A . 
W 7 HOH 4  1004 10   HOH HOH A . 
W 7 HOH 5  1005 72   HOH HOH A . 
W 7 HOH 6  1006 63   HOH HOH A . 
W 7 HOH 7  1007 65   HOH HOH A . 
W 7 HOH 8  1008 15   HOH HOH A . 
W 7 HOH 9  1009 47   HOH HOH A . 
W 7 HOH 10 1010 20   HOH HOH A . 
W 7 HOH 11 1011 14   HOH HOH A . 
W 7 HOH 12 1012 107  HOH HOH A . 
W 7 HOH 13 1013 73   HOH HOH A . 
W 7 HOH 14 1014 43   HOH HOH A . 
W 7 HOH 15 1015 48   HOH HOH A . 
W 7 HOH 16 1016 6    HOH HOH A . 
W 7 HOH 17 1017 16   HOH HOH A . 
W 7 HOH 18 1018 31   HOH HOH A . 
W 7 HOH 19 1019 74   HOH HOH A . 
W 7 HOH 20 1020 2    HOH HOH A . 
W 7 HOH 21 1021 62   HOH HOH A . 
W 7 HOH 22 1022 42   HOH HOH A . 
W 7 HOH 23 1023 1    HOH HOH A . 
W 7 HOH 24 1024 108  HOH HOH A . 
W 7 HOH 25 1025 45   HOH HOH A . 
W 7 HOH 26 1026 30   HOH HOH A . 
W 7 HOH 27 1027 38   HOH HOH A . 
W 7 HOH 28 1028 32   HOH HOH A . 
W 7 HOH 29 1029 4    HOH HOH A . 
W 7 HOH 30 1030 23   HOH HOH A . 
W 7 HOH 31 1031 41   HOH HOH A . 
W 7 HOH 32 1032 89   HOH HOH A . 
W 7 HOH 33 1033 19   HOH HOH A . 
W 7 HOH 34 1034 81   HOH HOH A . 
W 7 HOH 35 1035 13   HOH HOH A . 
W 7 HOH 36 1036 84   HOH HOH A . 
W 7 HOH 37 1037 12   HOH HOH A . 
W 7 HOH 38 1038 110  HOH HOH A . 
W 7 HOH 39 1039 79   HOH HOH A . 
W 7 HOH 40 1040 11   HOH HOH A . 
W 7 HOH 41 1041 70   HOH HOH A . 
W 7 HOH 42 1042 46   HOH HOH A . 
W 7 HOH 43 1043 36   HOH HOH A . 
W 7 HOH 44 1044 44   HOH HOH A . 
W 7 HOH 45 1045 3    HOH HOH A . 
W 7 HOH 46 1046 80   HOH HOH A . 
W 7 HOH 47 1047 39   HOH HOH A . 
W 7 HOH 48 1048 58   HOH HOH A . 
W 7 HOH 49 1049 67   HOH HOH A . 
W 7 HOH 50 1050 17   HOH HOH A . 
W 7 HOH 51 1051 90   HOH HOH A . 
W 7 HOH 52 1052 55   HOH HOH A . 
W 7 HOH 53 1053 18   HOH HOH A . 
W 7 HOH 54 1054 53   HOH HOH A . 
W 7 HOH 55 1055 52   HOH HOH A . 
W 7 HOH 56 1056 5    HOH HOH A . 
W 7 HOH 57 1057 26   HOH HOH A . 
W 7 HOH 58 1058 22   HOH HOH A . 
W 7 HOH 59 1059 27   HOH HOH A . 
W 7 HOH 60 1060 85   HOH HOH A . 
W 7 HOH 61 1061 51   HOH HOH A . 
W 7 HOH 62 1062 92   HOH HOH A . 
W 7 HOH 63 1063 24   HOH HOH A . 
W 7 HOH 64 1064 35   HOH HOH A . 
W 7 HOH 65 1065 59   HOH HOH A . 
W 7 HOH 66 1066 37   HOH HOH A . 
W 7 HOH 67 1067 68   HOH HOH A . 
W 7 HOH 68 1068 8    HOH HOH A . 
W 7 HOH 69 1069 69   HOH HOH A . 
W 7 HOH 70 1070 88   HOH HOH A . 
W 7 HOH 71 1071 93   HOH HOH A . 
W 7 HOH 72 1072 91   HOH HOH A . 
W 7 HOH 73 1073 87   HOH HOH A . 
W 7 HOH 74 1074 33   HOH HOH A . 
W 7 HOH 75 1075 56   HOH HOH A . 
W 7 HOH 76 1076 64   HOH HOH A . 
W 7 HOH 77 1077 71   HOH HOH A . 
W 7 HOH 78 1078 54   HOH HOH A . 
W 7 HOH 79 1079 61   HOH HOH A . 
# 
_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   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_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 
# 
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)' 4970  ? 
1 MORE         50    ? 
1 'SSA (A^2)'  34180 ? 
# 
_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 2016-03-09 
2 'Structure model' 1 1 2016-06-22 
# 
_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         ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               Other 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? 5.8.0073 1 
? 'data processing' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .        2 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .        3 
? phasing           ? ? ? ? ? ? ? ? ? ? ? MOLREP  ? ? ? .        4 
# 
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 OD2 A ASP 694 ? ? NH1 A ARG 696 ? ? 2.02 
2 1 OD1 A ASN 95  ? ? N   A GLU 133 ? ? 2.16 
3 1 ND2 A ASN 416 ? ? C2  A NAG 907 ? ? 2.18 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 C A LEU 137 ? ? N A PRO 138 ? ? CD A PRO 138 ? ? 142.32 128.40 13.92 2.10 Y 
2 1 C A ARG 472 ? ? N A PRO 473 ? ? CD A PRO 473 ? ? 141.06 128.40 12.66 2.10 Y 
# 
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 GLN A 41  ? ? 88.11   158.71  
2  1 CYS A 49  ? ? -142.75 56.08   
3  1 GLN A 87  ? ? 66.24   -59.04  
4  1 PRO A 141 ? ? -35.93  117.33  
5  1 ILE A 170 ? ? 70.11   -54.96  
6  1 CYS A 181 ? ? -106.29 47.04   
7  1 PHE A 183 ? ? -34.82  125.88  
8  1 SER A 214 ? ? 71.86   -37.58  
9  1 PHE A 261 ? ? 2.85    109.65  
10 1 LEU A 286 ? ? -92.19  59.87   
11 1 SER A 296 ? ? 61.18   63.63   
12 1 TYR A 322 ? ? -118.39 58.72   
13 1 SER A 329 ? ? -141.72 56.99   
14 1 SER A 360 ? ? -49.36  153.94  
15 1 VAL A 378 ? ? 77.67   105.41  
16 1 ASN A 416 ? ? -91.95  43.91   
17 1 HIS A 464 ? ? 78.03   -7.51   
18 1 ASN A 466 ? ? 138.01  -138.01 
19 1 PHE A 467 ? ? 106.47  -22.93  
20 1 TYR A 468 ? ? 82.76   13.45   
21 1 ASN A 491 ? ? -115.88 -161.58 
22 1 ASN A 546 ? ? -164.15 108.93  
23 1 ASP A 601 ? ? 69.30   -58.80  
24 1 ASN A 618 ? ? -102.91 -159.98 
25 1 ASP A 627 ? ? 130.71  -164.49 
26 1 ASN A 674 ? ? -111.69 -152.94 
27 1 PHE A 687 ? ? -116.12 73.37   
28 1 ASN A 698 ? ? -119.36 -159.33 
29 1 ASN A 746 ? ? -114.52 -154.29 
30 1 ILE A 814 ? ? -63.20  4.55    
31 1 THR A 821 ? ? -55.99  -1.29   
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   ASN 
_pdbx_validate_peptide_omega.auth_asym_id_1   A 
_pdbx_validate_peptide_omega.auth_seq_id_1    466 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   PHE 
_pdbx_validate_peptide_omega.auth_asym_id_2   A 
_pdbx_validate_peptide_omega.auth_seq_id_2    467 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            -149.43 
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    TYR 
_pdbx_validate_planes.auth_asym_id    A 
_pdbx_validate_planes.auth_seq_id     353 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.057 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLU 27  ? A GLU 1   
2  1 Y 1 A GLU 28  ? A GLU 2   
3  1 Y 1 A ASN 29  ? A ASN 3   
4  1 Y 1 A PHE 30  ? A PHE 4   
5  1 Y 1 A SER 31  ? A SER 5   
6  1 Y 1 A ARG 32  ? A ARG 6   
7  1 Y 1 A GLN 101 ? A GLN 75  
8  1 Y 1 A HIS 102 ? A HIS 76  
9  1 Y 1 A GLN 103 ? A GLN 77  
10 1 Y 1 A ASN 104 ? A ASN 78  
11 1 Y 1 A GLY 105 ? A GLY 79  
12 1 Y 1 A ASN 106 ? A ASN 80  
13 1 Y 1 A PRO 107 ? A PRO 81  
14 1 Y 1 A GLY 108 ? A GLY 82  
15 1 Y 1 A ILE 109 ? A ILE 83  
16 1 Y 1 A GLN 110 ? A GLN 84  
17 1 Y 1 A SER 111 ? A SER 85  
18 1 Y 1 A ASN 112 ? A ASN 86  
19 1 Y 1 A LYS 435 ? A LYS 409 
20 1 Y 1 A ASP 436 ? A ASP 410 
21 1 Y 1 A THR 437 ? A THR 411 
22 1 Y 1 A ARG 438 ? A ARG 412 
23 1 Y 1 A GLN 439 ? A GLN 413 
24 1 Y 1 A SER 440 ? A SER 414 
25 1 Y 1 A TYR 441 ? A TYR 415 
26 1 Y 1 A ALA 442 ? A ALA 416 
27 1 Y 1 A ASN 452 ? A ASN 426 
28 1 Y 1 A GLN 453 ? A GLN 427 
29 1 Y 1 A SER 454 ? A SER 428 
30 1 Y 1 A ASN 455 ? A ASN 429 
31 1 Y 1 A SER 456 ? A SER 430 
32 1 Y 1 A THR 457 ? A THR 431 
33 1 Y 1 A ASP 458 ? A ASP 432 
34 1 Y 1 A PHE 459 ? A PHE 433 
35 1 Y 1 A GLU 460 ? A GLU 434 
36 1 Y 1 A PHE 461 ? A PHE 435 
37 1 Y 1 A ASP 462 ? A ASP 436 
38 1 Y 1 A SER 733 ? A SER 707 
39 1 Y 1 A GLU 734 ? A GLU 708 
40 1 Y 1 A VAL 735 ? A VAL 709 
41 1 Y 1 A GLU 757 ? A GLU 731 
42 1 Y 1 A THR 758 ? A THR 732 
43 1 Y 1 A LYS 759 ? A LYS 733 
44 1 Y 1 A THR 760 ? A THR 734 
45 1 Y 1 A THR 761 ? A THR 735 
46 1 Y 1 A THR 762 ? A THR 736 
47 1 Y 1 A SER 824 ? A SER 798 
48 1 Y 1 A ASP 825 ? A ASP 799 
49 1 Y 1 A VAL 826 ? A VAL 800 
50 1 Y 1 A THR 827 ? A THR 801 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 N-ACETYL-D-GLUCOSAMINE                 NAG 
3 BETA-D-MANNOSE                         BMA 
4 ALPHA-D-MANNOSE                        MAN 
5 'SULFATE ION'                          SO4 
6 '2-(N-MORPHOLINO)-ETHANESULFONIC ACID' MES 
7 water                                  HOH 
# 
