data_8W1V
# 
_entry.id   8W1V 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.395 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8W1V         pdb_00008w1v 10.2210/pdb8w1v/pdb 
WWPDB D_1000281248 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2024-07-17 
# 
_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_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8W1V 
_pdbx_database_status.recvd_initial_deposition_date   2024-02-19 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              liu_xy@mail.tsinghua.edu.cn 
_pdbx_contact_author.name_first         Xiangyu 
_pdbx_contact_author.name_last          Liu 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-3178-9238 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Gaiser, B.'          1  ? 
'Danielsen, M.'       2  ? 
'Xu, X.'              3  ? 
'Jorgensen, K.'       4  ? 
'Fronik, P.'          5  ? 
'Marcher-Rorsted, E.' 6  ? 
'Wrobe, T.'           7  ? 
'Hirata, K.'          8  ? 
'Liu, X.'             9  ? 
'Mathiesen, J.'       10 ? 
'Pedersen, D.'        11 ? 
# 
_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            J.Med.Chem. 
_citation.journal_id_ASTM           JMCMAR 
_citation.journal_id_CSD            0151 
_citation.journal_id_ISSN           0022-2623 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Bitopic Ligands Support the Presence of a Metastable Binding Site at the beta 2 Adrenergic Receptor.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acs.jmedchem.4c00578 
_citation.pdbx_database_id_PubMed   38952152 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Gaiser, B.I.'          1  ?                   
primary 'Danielsen, M.'         2  ?                   
primary 'Xu, X.'                3  ?                   
primary 'Ropke Jorgensen, K.'   4  ?                   
primary 'Fronik, P.'            5  ?                   
primary 'Marcher-Rorsted, E.'   6  0000-0002-2783-6655 
primary 'Wrobel, T.M.'          7  0000-0002-0313-2522 
primary 'Liu, X.'               8  ?                   
primary 'Mosolff Mathiesen, J.' 9  ?                   
primary 'Sejer Pedersen, D.'    10 0000-0003-3926-7047 
# 
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 'Beta-2 adrenergic receptor,Endolysin' 62208.852 2 3.2.1.17 N187E,C1054T,C1097A ? ? 
2 polymer     man Nanobody60 13531.025 2 ?        ?                   ? ? 
3 non-polymer syn 
;(2S)-1-[(3-{1-[4-(4-{(2S)-2-hydroxy-3-[(propan-2-yl)amino]propoxy}phenyl)butyl]-1H-1,2,3-triazol-4-yl}propyl)amino]-3-(2-propylphenoxy)propan-2-ol
;
581.789   2 ?        ?                   ? ? 
4 non-polymer syn 'Lauryl Maltose Neopentyl Glycol' 1005.188  1 ?        ?                   ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Beta-2 adrenoreceptor,Beta-2 adrenoceptor,Lysis protein,Lysozyme,Muramidase' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;MKTIIALSYIFCLVFADYKDDDDAMGQPGNGSAFLLAPNRSHAPDHDVTQQRDEVWVVGMGIVMSLIVLAIVFGNVLVIT
AIAKFERLQTVTNYFITSLACADLVMGLAVVPFGAAHILMKMWTFGNFWCEFWTSIDVLCVTASIETLCVIAVDRYFAIT
SPFKYQSLLTKNKARVIILMVWIVSGLTSFLPIQMHWYRATHQEAINCYAEETCCDFFTNQAYAIASSIVSFYVPLVIMV
FVYSRVFQEAKRQLYKIDKSEGRFHVQNLSQVEQDGRTGHGLRRSSKFCLKEHKALKTLGIIMGTFTLCWLPFFIVNIVH
VIQDNLIRKEVYILLNWIGYVNSGFNPLIYCRSPDFRIAFQELLCLRRSSLKAYGNGYSSNGNTGEQSGNIFEMLRIDEG
LRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNTNGVITKDEAEKLFNQDVDAAVRGILRNAKLKPVYDSLD
AVRRAALINMVFQMGETGVAGFTNSLRMLQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDAY
;
;MKTIIALSYIFCLVFADYKDDDDAMGQPGNGSAFLLAPNRSHAPDHDVTQQRDEVWVVGMGIVMSLIVLAIVFGNVLVIT
AIAKFERLQTVTNYFITSLACADLVMGLAVVPFGAAHILMKMWTFGNFWCEFWTSIDVLCVTASIETLCVIAVDRYFAIT
SPFKYQSLLTKNKARVIILMVWIVSGLTSFLPIQMHWYRATHQEAINCYAEETCCDFFTNQAYAIASSIVSFYVPLVIMV
FVYSRVFQEAKRQLYKIDKSEGRFHVQNLSQVEQDGRTGHGLRRSSKFCLKEHKALKTLGIIMGTFTLCWLPFFIVNIVH
VIQDNLIRKEVYILLNWIGYVNSGFNPLIYCRSPDFRIAFQELLCLRRSSLKAYGNGYSSNGNTGEQSGNIFEMLRIDEG
LRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNTNGVITKDEAEKLFNQDVDAAVRGILRNAKLKPVYDSLD
AVRRAALINMVFQMGETGVAGFTNSLRMLQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDAY
;
A,B ? 
2 'polypeptide(L)' no no 
;QVQLQESGGGLVQAGGSLRLSCAASGSIFSLNDMGWYRQAPGKLRELVAAITSGGSTKYADSVKGRFTISRDNAKNTVYL
QMNSLKAEDTAVYYCNAKVAGTFSIYDYWGQGTQVTVSSHHHHHH
;
;QVQLQESGGGLVQAGGSLRLSCAASGSIFSLNDMGWYRQAPGKLRELVAAITSGGSTKYADSVKGRFTISRDNAKNTVYL
QMNSLKAEDTAVYYCNAKVAGTFSIYDYWGQGTQVTVSSHHHHHH
;
D,F ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 
;(2S)-1-[(3-{1-[4-(4-{(2S)-2-hydroxy-3-[(propan-2-yl)amino]propoxy}phenyl)butyl]-1H-1,2,3-triazol-4-yl}propyl)amino]-3-(2-propylphenoxy)propan-2-ol
;
A1AE2 
4 'Lauryl Maltose Neopentyl Glycol' AV0   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   LYS n 
1 3   THR n 
1 4   ILE n 
1 5   ILE n 
1 6   ALA n 
1 7   LEU n 
1 8   SER n 
1 9   TYR n 
1 10  ILE n 
1 11  PHE n 
1 12  CYS n 
1 13  LEU n 
1 14  VAL n 
1 15  PHE n 
1 16  ALA n 
1 17  ASP n 
1 18  TYR n 
1 19  LYS n 
1 20  ASP n 
1 21  ASP n 
1 22  ASP n 
1 23  ASP n 
1 24  ALA n 
1 25  MET n 
1 26  GLY n 
1 27  GLN n 
1 28  PRO n 
1 29  GLY n 
1 30  ASN n 
1 31  GLY n 
1 32  SER n 
1 33  ALA n 
1 34  PHE n 
1 35  LEU n 
1 36  LEU n 
1 37  ALA n 
1 38  PRO n 
1 39  ASN n 
1 40  ARG n 
1 41  SER n 
1 42  HIS n 
1 43  ALA n 
1 44  PRO n 
1 45  ASP n 
1 46  HIS n 
1 47  ASP n 
1 48  VAL n 
1 49  THR n 
1 50  GLN n 
1 51  GLN n 
1 52  ARG n 
1 53  ASP n 
1 54  GLU n 
1 55  VAL n 
1 56  TRP n 
1 57  VAL n 
1 58  VAL n 
1 59  GLY n 
1 60  MET n 
1 61  GLY n 
1 62  ILE n 
1 63  VAL n 
1 64  MET n 
1 65  SER n 
1 66  LEU n 
1 67  ILE n 
1 68  VAL n 
1 69  LEU n 
1 70  ALA n 
1 71  ILE n 
1 72  VAL n 
1 73  PHE n 
1 74  GLY n 
1 75  ASN n 
1 76  VAL n 
1 77  LEU n 
1 78  VAL n 
1 79  ILE n 
1 80  THR n 
1 81  ALA n 
1 82  ILE n 
1 83  ALA n 
1 84  LYS n 
1 85  PHE n 
1 86  GLU n 
1 87  ARG n 
1 88  LEU n 
1 89  GLN n 
1 90  THR n 
1 91  VAL n 
1 92  THR n 
1 93  ASN n 
1 94  TYR n 
1 95  PHE n 
1 96  ILE n 
1 97  THR n 
1 98  SER n 
1 99  LEU n 
1 100 ALA n 
1 101 CYS n 
1 102 ALA n 
1 103 ASP n 
1 104 LEU n 
1 105 VAL n 
1 106 MET n 
1 107 GLY n 
1 108 LEU n 
1 109 ALA n 
1 110 VAL n 
1 111 VAL n 
1 112 PRO n 
1 113 PHE n 
1 114 GLY n 
1 115 ALA n 
1 116 ALA n 
1 117 HIS n 
1 118 ILE n 
1 119 LEU n 
1 120 MET n 
1 121 LYS n 
1 122 MET n 
1 123 TRP n 
1 124 THR n 
1 125 PHE n 
1 126 GLY n 
1 127 ASN n 
1 128 PHE n 
1 129 TRP n 
1 130 CYS n 
1 131 GLU n 
1 132 PHE n 
1 133 TRP n 
1 134 THR n 
1 135 SER n 
1 136 ILE n 
1 137 ASP n 
1 138 VAL n 
1 139 LEU n 
1 140 CYS n 
1 141 VAL n 
1 142 THR n 
1 143 ALA n 
1 144 SER n 
1 145 ILE n 
1 146 GLU n 
1 147 THR n 
1 148 LEU n 
1 149 CYS n 
1 150 VAL n 
1 151 ILE n 
1 152 ALA n 
1 153 VAL n 
1 154 ASP n 
1 155 ARG n 
1 156 TYR n 
1 157 PHE n 
1 158 ALA n 
1 159 ILE n 
1 160 THR n 
1 161 SER n 
1 162 PRO n 
1 163 PHE n 
1 164 LYS n 
1 165 TYR n 
1 166 GLN n 
1 167 SER n 
1 168 LEU n 
1 169 LEU n 
1 170 THR n 
1 171 LYS n 
1 172 ASN n 
1 173 LYS n 
1 174 ALA n 
1 175 ARG n 
1 176 VAL n 
1 177 ILE n 
1 178 ILE n 
1 179 LEU n 
1 180 MET n 
1 181 VAL n 
1 182 TRP n 
1 183 ILE n 
1 184 VAL n 
1 185 SER n 
1 186 GLY n 
1 187 LEU n 
1 188 THR n 
1 189 SER n 
1 190 PHE n 
1 191 LEU n 
1 192 PRO n 
1 193 ILE n 
1 194 GLN n 
1 195 MET n 
1 196 HIS n 
1 197 TRP n 
1 198 TYR n 
1 199 ARG n 
1 200 ALA n 
1 201 THR n 
1 202 HIS n 
1 203 GLN n 
1 204 GLU n 
1 205 ALA n 
1 206 ILE n 
1 207 ASN n 
1 208 CYS n 
1 209 TYR n 
1 210 ALA n 
1 211 GLU n 
1 212 GLU n 
1 213 THR n 
1 214 CYS n 
1 215 CYS n 
1 216 ASP n 
1 217 PHE n 
1 218 PHE n 
1 219 THR n 
1 220 ASN n 
1 221 GLN n 
1 222 ALA n 
1 223 TYR n 
1 224 ALA n 
1 225 ILE n 
1 226 ALA n 
1 227 SER n 
1 228 SER n 
1 229 ILE n 
1 230 VAL n 
1 231 SER n 
1 232 PHE n 
1 233 TYR n 
1 234 VAL n 
1 235 PRO n 
1 236 LEU n 
1 237 VAL n 
1 238 ILE n 
1 239 MET n 
1 240 VAL n 
1 241 PHE n 
1 242 VAL n 
1 243 TYR n 
1 244 SER n 
1 245 ARG n 
1 246 VAL n 
1 247 PHE n 
1 248 GLN n 
1 249 GLU n 
1 250 ALA n 
1 251 LYS n 
1 252 ARG n 
1 253 GLN n 
1 254 LEU n 
1 255 TYR n 
1 256 LYS n 
1 257 ILE n 
1 258 ASP n 
1 259 LYS n 
1 260 SER n 
1 261 GLU n 
1 262 GLY n 
1 263 ARG n 
1 264 PHE n 
1 265 HIS n 
1 266 VAL n 
1 267 GLN n 
1 268 ASN n 
1 269 LEU n 
1 270 SER n 
1 271 GLN n 
1 272 VAL n 
1 273 GLU n 
1 274 GLN n 
1 275 ASP n 
1 276 GLY n 
1 277 ARG n 
1 278 THR n 
1 279 GLY n 
1 280 HIS n 
1 281 GLY n 
1 282 LEU n 
1 283 ARG n 
1 284 ARG n 
1 285 SER n 
1 286 SER n 
1 287 LYS n 
1 288 PHE n 
1 289 CYS n 
1 290 LEU n 
1 291 LYS n 
1 292 GLU n 
1 293 HIS n 
1 294 LYS n 
1 295 ALA n 
1 296 LEU n 
1 297 LYS n 
1 298 THR n 
1 299 LEU n 
1 300 GLY n 
1 301 ILE n 
1 302 ILE n 
1 303 MET n 
1 304 GLY n 
1 305 THR n 
1 306 PHE n 
1 307 THR n 
1 308 LEU n 
1 309 CYS n 
1 310 TRP n 
1 311 LEU n 
1 312 PRO n 
1 313 PHE n 
1 314 PHE n 
1 315 ILE n 
1 316 VAL n 
1 317 ASN n 
1 318 ILE n 
1 319 VAL n 
1 320 HIS n 
1 321 VAL n 
1 322 ILE n 
1 323 GLN n 
1 324 ASP n 
1 325 ASN n 
1 326 LEU n 
1 327 ILE n 
1 328 ARG n 
1 329 LYS n 
1 330 GLU n 
1 331 VAL n 
1 332 TYR n 
1 333 ILE n 
1 334 LEU n 
1 335 LEU n 
1 336 ASN n 
1 337 TRP n 
1 338 ILE n 
1 339 GLY n 
1 340 TYR n 
1 341 VAL n 
1 342 ASN n 
1 343 SER n 
1 344 GLY n 
1 345 PHE n 
1 346 ASN n 
1 347 PRO n 
1 348 LEU n 
1 349 ILE n 
1 350 TYR n 
1 351 CYS n 
1 352 ARG n 
1 353 SER n 
1 354 PRO n 
1 355 ASP n 
1 356 PHE n 
1 357 ARG n 
1 358 ILE n 
1 359 ALA n 
1 360 PHE n 
1 361 GLN n 
1 362 GLU n 
1 363 LEU n 
1 364 LEU n 
1 365 CYS n 
1 366 LEU n 
1 367 ARG n 
1 368 ARG n 
1 369 SER n 
1 370 SER n 
1 371 LEU n 
1 372 LYS n 
1 373 ALA n 
1 374 TYR n 
1 375 GLY n 
1 376 ASN n 
1 377 GLY n 
1 378 TYR n 
1 379 SER n 
1 380 SER n 
1 381 ASN n 
1 382 GLY n 
1 383 ASN n 
1 384 THR n 
1 385 GLY n 
1 386 GLU n 
1 387 GLN n 
1 388 SER n 
1 389 GLY n 
1 390 ASN n 
1 391 ILE n 
1 392 PHE n 
1 393 GLU n 
1 394 MET n 
1 395 LEU n 
1 396 ARG n 
1 397 ILE n 
1 398 ASP n 
1 399 GLU n 
1 400 GLY n 
1 401 LEU n 
1 402 ARG n 
1 403 LEU n 
1 404 LYS n 
1 405 ILE n 
1 406 TYR n 
1 407 LYS n 
1 408 ASP n 
1 409 THR n 
1 410 GLU n 
1 411 GLY n 
1 412 TYR n 
1 413 TYR n 
1 414 THR n 
1 415 ILE n 
1 416 GLY n 
1 417 ILE n 
1 418 GLY n 
1 419 HIS n 
1 420 LEU n 
1 421 LEU n 
1 422 THR n 
1 423 LYS n 
1 424 SER n 
1 425 PRO n 
1 426 SER n 
1 427 LEU n 
1 428 ASN n 
1 429 ALA n 
1 430 ALA n 
1 431 LYS n 
1 432 SER n 
1 433 GLU n 
1 434 LEU n 
1 435 ASP n 
1 436 LYS n 
1 437 ALA n 
1 438 ILE n 
1 439 GLY n 
1 440 ARG n 
1 441 ASN n 
1 442 THR n 
1 443 ASN n 
1 444 GLY n 
1 445 VAL n 
1 446 ILE n 
1 447 THR n 
1 448 LYS n 
1 449 ASP n 
1 450 GLU n 
1 451 ALA n 
1 452 GLU n 
1 453 LYS n 
1 454 LEU n 
1 455 PHE n 
1 456 ASN n 
1 457 GLN n 
1 458 ASP n 
1 459 VAL n 
1 460 ASP n 
1 461 ALA n 
1 462 ALA n 
1 463 VAL n 
1 464 ARG n 
1 465 GLY n 
1 466 ILE n 
1 467 LEU n 
1 468 ARG n 
1 469 ASN n 
1 470 ALA n 
1 471 LYS n 
1 472 LEU n 
1 473 LYS n 
1 474 PRO n 
1 475 VAL n 
1 476 TYR n 
1 477 ASP n 
1 478 SER n 
1 479 LEU n 
1 480 ASP n 
1 481 ALA n 
1 482 VAL n 
1 483 ARG n 
1 484 ARG n 
1 485 ALA n 
1 486 ALA n 
1 487 LEU n 
1 488 ILE n 
1 489 ASN n 
1 490 MET n 
1 491 VAL n 
1 492 PHE n 
1 493 GLN n 
1 494 MET n 
1 495 GLY n 
1 496 GLU n 
1 497 THR n 
1 498 GLY n 
1 499 VAL n 
1 500 ALA n 
1 501 GLY n 
1 502 PHE n 
1 503 THR n 
1 504 ASN n 
1 505 SER n 
1 506 LEU n 
1 507 ARG n 
1 508 MET n 
1 509 LEU n 
1 510 GLN n 
1 511 GLN n 
1 512 LYS n 
1 513 ARG n 
1 514 TRP n 
1 515 ASP n 
1 516 GLU n 
1 517 ALA n 
1 518 ALA n 
1 519 VAL n 
1 520 ASN n 
1 521 LEU n 
1 522 ALA n 
1 523 LYS n 
1 524 SER n 
1 525 ARG n 
1 526 TRP n 
1 527 TYR n 
1 528 ASN n 
1 529 GLN n 
1 530 THR n 
1 531 PRO n 
1 532 ASN n 
1 533 ARG n 
1 534 ALA n 
1 535 LYS n 
1 536 ARG n 
1 537 VAL n 
1 538 ILE n 
1 539 THR n 
1 540 THR n 
1 541 PHE n 
1 542 ARG n 
1 543 THR n 
1 544 GLY n 
1 545 THR n 
1 546 TRP n 
1 547 ASP n 
1 548 ALA n 
1 549 TYR n 
2 1   GLN n 
2 2   VAL n 
2 3   GLN n 
2 4   LEU n 
2 5   GLN n 
2 6   GLU n 
2 7   SER n 
2 8   GLY n 
2 9   GLY n 
2 10  GLY n 
2 11  LEU n 
2 12  VAL n 
2 13  GLN n 
2 14  ALA n 
2 15  GLY n 
2 16  GLY n 
2 17  SER n 
2 18  LEU n 
2 19  ARG n 
2 20  LEU n 
2 21  SER n 
2 22  CYS n 
2 23  ALA n 
2 24  ALA n 
2 25  SER n 
2 26  GLY n 
2 27  SER n 
2 28  ILE n 
2 29  PHE n 
2 30  SER n 
2 31  LEU n 
2 32  ASN n 
2 33  ASP n 
2 34  MET n 
2 35  GLY n 
2 36  TRP n 
2 37  TYR n 
2 38  ARG n 
2 39  GLN n 
2 40  ALA n 
2 41  PRO n 
2 42  GLY n 
2 43  LYS n 
2 44  LEU n 
2 45  ARG n 
2 46  GLU n 
2 47  LEU n 
2 48  VAL n 
2 49  ALA n 
2 50  ALA n 
2 51  ILE n 
2 52  THR n 
2 53  SER n 
2 54  GLY n 
2 55  GLY n 
2 56  SER n 
2 57  THR n 
2 58  LYS n 
2 59  TYR n 
2 60  ALA n 
2 61  ASP n 
2 62  SER n 
2 63  VAL n 
2 64  LYS n 
2 65  GLY n 
2 66  ARG n 
2 67  PHE n 
2 68  THR n 
2 69  ILE n 
2 70  SER n 
2 71  ARG n 
2 72  ASP n 
2 73  ASN n 
2 74  ALA n 
2 75  LYS n 
2 76  ASN n 
2 77  THR n 
2 78  VAL n 
2 79  TYR n 
2 80  LEU n 
2 81  GLN n 
2 82  MET n 
2 83  ASN n 
2 84  SER n 
2 85  LEU n 
2 86  LYS n 
2 87  ALA n 
2 88  GLU n 
2 89  ASP n 
2 90  THR n 
2 91  ALA n 
2 92  VAL n 
2 93  TYR n 
2 94  TYR n 
2 95  CYS n 
2 96  ASN n 
2 97  ALA n 
2 98  LYS n 
2 99  VAL n 
2 100 ALA n 
2 101 GLY n 
2 102 THR n 
2 103 PHE n 
2 104 SER n 
2 105 ILE n 
2 106 TYR n 
2 107 ASP n 
2 108 TYR n 
2 109 TRP n 
2 110 GLY n 
2 111 GLN n 
2 112 GLY n 
2 113 THR n 
2 114 GLN n 
2 115 VAL n 
2 116 THR n 
2 117 VAL n 
2 118 SER n 
2 119 SER n 
2 120 HIS n 
2 121 HIS n 
2 122 HIS n 
2 123 HIS n 
2 124 HIS n 
2 125 HIS n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1   389 human ? 'ADRB2, ADRB2R, B2AR' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Spodoptera frugiperda' 7108 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
1 2 sample 'Biological sequence' 390 549 human ? ?                     ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Spodoptera frugiperda' 7108 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1   125 ?     ? ?                     ? ? ? ? ? ? 'Lama glama'   9844 ? ? ? ? ? ? ? ? 
'Spodoptera frugiperda' 7108 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
A1AE2 non-polymer         . 
;(2S)-1-[(3-{1-[4-(4-{(2S)-2-hydroxy-3-[(propan-2-yl)amino]propoxy}phenyl)butyl]-1H-1,2,3-triazol-4-yl}propyl)amino]-3-(2-propylphenoxy)propan-2-ol
;
? 'C33 H51 N5 O4'  581.789  
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  
AV0   non-polymer         . 'Lauryl Maltose Neopentyl Glycol' 
;2,2-didecylpropane-1,3-bis-b-D-maltopyranoside; 2-decyl-2-{[(4-O-alpha-D-glucopyranosyl-beta-D-glucopyranosyl)oxy]methyl}dodecyl4-O-alpha-D-glucopyranosyl-beta-D-glucopyranoside
;
'C47 H88 O22'    1005.188 
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  
ILE   'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'    131.173  
LEU   'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'    131.173  
LYS   'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195  
MET   'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'  149.211  
PHE   'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'    165.189  
PRO   'L-peptide linking' y PROLINE ? 'C5 H9 N O2'     115.130  
SER   'L-peptide linking' y SERINE ? 'C3 H7 N O3'     105.093  
THR   'L-peptide linking' y THREONINE ? 'C4 H9 N O3'     119.119  
TRP   'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2'  204.225  
TYR   'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'    181.189  
VAL   'L-peptide linking' y VALINE ? 'C5 H11 N O2'    117.146  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   -23  ?    ?   ?   A . n 
A 1 2   LYS 2   -22  ?    ?   ?   A . n 
A 1 3   THR 3   -21  ?    ?   ?   A . n 
A 1 4   ILE 4   -20  ?    ?   ?   A . n 
A 1 5   ILE 5   -19  ?    ?   ?   A . n 
A 1 6   ALA 6   -18  ?    ?   ?   A . n 
A 1 7   LEU 7   -17  ?    ?   ?   A . n 
A 1 8   SER 8   -16  ?    ?   ?   A . n 
A 1 9   TYR 9   -15  ?    ?   ?   A . n 
A 1 10  ILE 10  -14  ?    ?   ?   A . n 
A 1 11  PHE 11  -13  ?    ?   ?   A . n 
A 1 12  CYS 12  -12  ?    ?   ?   A . n 
A 1 13  LEU 13  -11  ?    ?   ?   A . n 
A 1 14  VAL 14  -10  ?    ?   ?   A . n 
A 1 15  PHE 15  -9   ?    ?   ?   A . n 
A 1 16  ALA 16  -8   ?    ?   ?   A . n 
A 1 17  ASP 17  -7   ?    ?   ?   A . n 
A 1 18  TYR 18  -6   ?    ?   ?   A . n 
A 1 19  LYS 19  -5   ?    ?   ?   A . n 
A 1 20  ASP 20  -4   ?    ?   ?   A . n 
A 1 21  ASP 21  -3   ?    ?   ?   A . n 
A 1 22  ASP 22  -2   ?    ?   ?   A . n 
A 1 23  ASP 23  -1   ?    ?   ?   A . n 
A 1 24  ALA 24  0    ?    ?   ?   A . n 
A 1 25  MET 25  1    ?    ?   ?   A . n 
A 1 26  GLY 26  2    ?    ?   ?   A . n 
A 1 27  GLN 27  3    ?    ?   ?   A . n 
A 1 28  PRO 28  4    ?    ?   ?   A . n 
A 1 29  GLY 29  5    ?    ?   ?   A . n 
A 1 30  ASN 30  6    ?    ?   ?   A . n 
A 1 31  GLY 31  7    ?    ?   ?   A . n 
A 1 32  SER 32  8    ?    ?   ?   A . n 
A 1 33  ALA 33  9    ?    ?   ?   A . n 
A 1 34  PHE 34  10   ?    ?   ?   A . n 
A 1 35  LEU 35  11   ?    ?   ?   A . n 
A 1 36  LEU 36  12   ?    ?   ?   A . n 
A 1 37  ALA 37  13   ?    ?   ?   A . n 
A 1 38  PRO 38  14   ?    ?   ?   A . n 
A 1 39  ASN 39  15   ?    ?   ?   A . n 
A 1 40  ARG 40  16   ?    ?   ?   A . n 
A 1 41  SER 41  17   ?    ?   ?   A . n 
A 1 42  HIS 42  18   ?    ?   ?   A . n 
A 1 43  ALA 43  19   ?    ?   ?   A . n 
A 1 44  PRO 44  20   ?    ?   ?   A . n 
A 1 45  ASP 45  21   ?    ?   ?   A . n 
A 1 46  HIS 46  22   ?    ?   ?   A . n 
A 1 47  ASP 47  23   ?    ?   ?   A . n 
A 1 48  VAL 48  24   ?    ?   ?   A . n 
A 1 49  THR 49  25   ?    ?   ?   A . n 
A 1 50  GLN 50  26   ?    ?   ?   A . n 
A 1 51  GLN 51  27   ?    ?   ?   A . n 
A 1 52  ARG 52  28   ?    ?   ?   A . n 
A 1 53  ASP 53  29   29   ASP ASP A . n 
A 1 54  GLU 54  30   30   GLU GLU A . n 
A 1 55  VAL 55  31   31   VAL VAL A . n 
A 1 56  TRP 56  32   32   TRP TRP A . n 
A 1 57  VAL 57  33   33   VAL VAL A . n 
A 1 58  VAL 58  34   34   VAL VAL A . n 
A 1 59  GLY 59  35   35   GLY GLY A . n 
A 1 60  MET 60  36   36   MET MET A . n 
A 1 61  GLY 61  37   37   GLY GLY A . n 
A 1 62  ILE 62  38   38   ILE ILE A . n 
A 1 63  VAL 63  39   39   VAL VAL A . n 
A 1 64  MET 64  40   40   MET MET A . n 
A 1 65  SER 65  41   41   SER SER A . n 
A 1 66  LEU 66  42   42   LEU LEU A . n 
A 1 67  ILE 67  43   43   ILE ILE A . n 
A 1 68  VAL 68  44   44   VAL VAL A . n 
A 1 69  LEU 69  45   45   LEU LEU A . n 
A 1 70  ALA 70  46   46   ALA ALA A . n 
A 1 71  ILE 71  47   47   ILE ILE A . n 
A 1 72  VAL 72  48   48   VAL VAL A . n 
A 1 73  PHE 73  49   49   PHE PHE A . n 
A 1 74  GLY 74  50   50   GLY GLY A . n 
A 1 75  ASN 75  51   51   ASN ASN A . n 
A 1 76  VAL 76  52   52   VAL VAL A . n 
A 1 77  LEU 77  53   53   LEU LEU A . n 
A 1 78  VAL 78  54   54   VAL VAL A . n 
A 1 79  ILE 79  55   55   ILE ILE A . n 
A 1 80  THR 80  56   56   THR THR A . n 
A 1 81  ALA 81  57   57   ALA ALA A . n 
A 1 82  ILE 82  58   58   ILE ILE A . n 
A 1 83  ALA 83  59   59   ALA ALA A . n 
A 1 84  LYS 84  60   60   LYS LYS A . n 
A 1 85  PHE 85  61   61   PHE PHE A . n 
A 1 86  GLU 86  62   62   GLU GLU A . n 
A 1 87  ARG 87  63   63   ARG ARG A . n 
A 1 88  LEU 88  64   64   LEU LEU A . n 
A 1 89  GLN 89  65   65   GLN GLN A . n 
A 1 90  THR 90  66   66   THR THR A . n 
A 1 91  VAL 91  67   67   VAL VAL A . n 
A 1 92  THR 92  68   68   THR THR A . n 
A 1 93  ASN 93  69   69   ASN ASN A . n 
A 1 94  TYR 94  70   70   TYR TYR A . n 
A 1 95  PHE 95  71   71   PHE PHE A . n 
A 1 96  ILE 96  72   72   ILE ILE A . n 
A 1 97  THR 97  73   73   THR THR A . n 
A 1 98  SER 98  74   74   SER SER A . n 
A 1 99  LEU 99  75   75   LEU LEU A . n 
A 1 100 ALA 100 76   76   ALA ALA A . n 
A 1 101 CYS 101 77   77   CYS CYS A . n 
A 1 102 ALA 102 78   78   ALA ALA A . n 
A 1 103 ASP 103 79   79   ASP ASP A . n 
A 1 104 LEU 104 80   80   LEU LEU A . n 
A 1 105 VAL 105 81   81   VAL VAL A . n 
A 1 106 MET 106 82   82   MET MET A . n 
A 1 107 GLY 107 83   83   GLY GLY A . n 
A 1 108 LEU 108 84   84   LEU LEU A . n 
A 1 109 ALA 109 85   85   ALA ALA A . n 
A 1 110 VAL 110 86   86   VAL VAL A . n 
A 1 111 VAL 111 87   87   VAL VAL A . n 
A 1 112 PRO 112 88   88   PRO PRO A . n 
A 1 113 PHE 113 89   89   PHE PHE A . n 
A 1 114 GLY 114 90   90   GLY GLY A . n 
A 1 115 ALA 115 91   91   ALA ALA A . n 
A 1 116 ALA 116 92   92   ALA ALA A . n 
A 1 117 HIS 117 93   93   HIS HIS A . n 
A 1 118 ILE 118 94   94   ILE ILE A . n 
A 1 119 LEU 119 95   95   LEU LEU A . n 
A 1 120 MET 120 96   96   MET MET A . n 
A 1 121 LYS 121 97   97   LYS LYS A . n 
A 1 122 MET 122 98   98   MET MET A . n 
A 1 123 TRP 123 99   99   TRP TRP A . n 
A 1 124 THR 124 100  100  THR THR A . n 
A 1 125 PHE 125 101  101  PHE PHE A . n 
A 1 126 GLY 126 102  102  GLY GLY A . n 
A 1 127 ASN 127 103  103  ASN ASN A . n 
A 1 128 PHE 128 104  104  PHE PHE A . n 
A 1 129 TRP 129 105  105  TRP TRP A . n 
A 1 130 CYS 130 106  106  CYS CYS A . n 
A 1 131 GLU 131 107  107  GLU GLU A . n 
A 1 132 PHE 132 108  108  PHE PHE A . n 
A 1 133 TRP 133 109  109  TRP TRP A . n 
A 1 134 THR 134 110  110  THR THR A . n 
A 1 135 SER 135 111  111  SER SER A . n 
A 1 136 ILE 136 112  112  ILE ILE A . n 
A 1 137 ASP 137 113  113  ASP ASP A . n 
A 1 138 VAL 138 114  114  VAL VAL A . n 
A 1 139 LEU 139 115  115  LEU LEU A . n 
A 1 140 CYS 140 116  116  CYS CYS A . n 
A 1 141 VAL 141 117  117  VAL VAL A . n 
A 1 142 THR 142 118  118  THR THR A . n 
A 1 143 ALA 143 119  119  ALA ALA A . n 
A 1 144 SER 144 120  120  SER SER A . n 
A 1 145 ILE 145 121  121  ILE ILE A . n 
A 1 146 GLU 146 122  122  GLU GLU A . n 
A 1 147 THR 147 123  123  THR THR A . n 
A 1 148 LEU 148 124  124  LEU LEU A . n 
A 1 149 CYS 149 125  125  CYS CYS A . n 
A 1 150 VAL 150 126  126  VAL VAL A . n 
A 1 151 ILE 151 127  127  ILE ILE A . n 
A 1 152 ALA 152 128  128  ALA ALA A . n 
A 1 153 VAL 153 129  129  VAL VAL A . n 
A 1 154 ASP 154 130  130  ASP ASP A . n 
A 1 155 ARG 155 131  131  ARG ARG A . n 
A 1 156 TYR 156 132  132  TYR TYR A . n 
A 1 157 PHE 157 133  133  PHE PHE A . n 
A 1 158 ALA 158 134  134  ALA ALA A . n 
A 1 159 ILE 159 135  135  ILE ILE A . n 
A 1 160 THR 160 136  136  THR THR A . n 
A 1 161 SER 161 137  137  SER SER A . n 
A 1 162 PRO 162 138  138  PRO PRO A . n 
A 1 163 PHE 163 139  139  PHE PHE A . n 
A 1 164 LYS 164 140  140  LYS LYS A . n 
A 1 165 TYR 165 141  141  TYR TYR A . n 
A 1 166 GLN 166 142  142  GLN GLN A . n 
A 1 167 SER 167 143  143  SER SER A . n 
A 1 168 LEU 168 144  144  LEU LEU A . n 
A 1 169 LEU 169 145  145  LEU LEU A . n 
A 1 170 THR 170 146  146  THR THR A . n 
A 1 171 LYS 171 147  147  LYS LYS A . n 
A 1 172 ASN 172 148  148  ASN ASN A . n 
A 1 173 LYS 173 149  149  LYS LYS A . n 
A 1 174 ALA 174 150  150  ALA ALA A . n 
A 1 175 ARG 175 151  151  ARG ARG A . n 
A 1 176 VAL 176 152  152  VAL VAL A . n 
A 1 177 ILE 177 153  153  ILE ILE A . n 
A 1 178 ILE 178 154  154  ILE ILE A . n 
A 1 179 LEU 179 155  155  LEU LEU A . n 
A 1 180 MET 180 156  156  MET MET A . n 
A 1 181 VAL 181 157  157  VAL VAL A . n 
A 1 182 TRP 182 158  158  TRP TRP A . n 
A 1 183 ILE 183 159  159  ILE ILE A . n 
A 1 184 VAL 184 160  160  VAL VAL A . n 
A 1 185 SER 185 161  161  SER SER A . n 
A 1 186 GLY 186 162  162  GLY GLY A . n 
A 1 187 LEU 187 163  163  LEU LEU A . n 
A 1 188 THR 188 164  164  THR THR A . n 
A 1 189 SER 189 165  165  SER SER A . n 
A 1 190 PHE 190 166  166  PHE PHE A . n 
A 1 191 LEU 191 167  167  LEU LEU A . n 
A 1 192 PRO 192 168  168  PRO PRO A . n 
A 1 193 ILE 193 169  169  ILE ILE A . n 
A 1 194 GLN 194 170  170  GLN GLN A . n 
A 1 195 MET 195 171  171  MET MET A . n 
A 1 196 HIS 196 172  172  HIS HIS A . n 
A 1 197 TRP 197 173  173  TRP TRP A . n 
A 1 198 TYR 198 174  174  TYR TYR A . n 
A 1 199 ARG 199 175  175  ARG ARG A . n 
A 1 200 ALA 200 176  176  ALA ALA A . n 
A 1 201 THR 201 177  177  THR THR A . n 
A 1 202 HIS 202 178  178  HIS HIS A . n 
A 1 203 GLN 203 179  179  GLN GLN A . n 
A 1 204 GLU 204 180  180  GLU GLU A . n 
A 1 205 ALA 205 181  181  ALA ALA A . n 
A 1 206 ILE 206 182  182  ILE ILE A . n 
A 1 207 ASN 207 183  183  ASN ASN A . n 
A 1 208 CYS 208 184  184  CYS CYS A . n 
A 1 209 TYR 209 185  185  TYR TYR A . n 
A 1 210 ALA 210 186  186  ALA ALA A . n 
A 1 211 GLU 211 187  187  GLU GLU A . n 
A 1 212 GLU 212 188  188  GLU GLU A . n 
A 1 213 THR 213 189  189  THR THR A . n 
A 1 214 CYS 214 190  190  CYS CYS A . n 
A 1 215 CYS 215 191  191  CYS CYS A . n 
A 1 216 ASP 216 192  192  ASP ASP A . n 
A 1 217 PHE 217 193  193  PHE PHE A . n 
A 1 218 PHE 218 194  194  PHE PHE A . n 
A 1 219 THR 219 195  195  THR THR A . n 
A 1 220 ASN 220 196  196  ASN ASN A . n 
A 1 221 GLN 221 197  197  GLN GLN A . n 
A 1 222 ALA 222 198  198  ALA ALA A . n 
A 1 223 TYR 223 199  199  TYR TYR A . n 
A 1 224 ALA 224 200  200  ALA ALA A . n 
A 1 225 ILE 225 201  201  ILE ILE A . n 
A 1 226 ALA 226 202  202  ALA ALA A . n 
A 1 227 SER 227 203  203  SER SER A . n 
A 1 228 SER 228 204  204  SER SER A . n 
A 1 229 ILE 229 205  205  ILE ILE A . n 
A 1 230 VAL 230 206  206  VAL VAL A . n 
A 1 231 SER 231 207  207  SER SER A . n 
A 1 232 PHE 232 208  208  PHE PHE A . n 
A 1 233 TYR 233 209  209  TYR TYR A . n 
A 1 234 VAL 234 210  210  VAL VAL A . n 
A 1 235 PRO 235 211  211  PRO PRO A . n 
A 1 236 LEU 236 212  212  LEU LEU A . n 
A 1 237 VAL 237 213  213  VAL VAL A . n 
A 1 238 ILE 238 214  214  ILE ILE A . n 
A 1 239 MET 239 215  215  MET MET A . n 
A 1 240 VAL 240 216  216  VAL VAL A . n 
A 1 241 PHE 241 217  217  PHE PHE A . n 
A 1 242 VAL 242 218  218  VAL VAL A . n 
A 1 243 TYR 243 219  219  TYR TYR A . n 
A 1 244 SER 244 220  220  SER SER A . n 
A 1 245 ARG 245 221  221  ARG ARG A . n 
A 1 246 VAL 246 222  222  VAL VAL A . n 
A 1 247 PHE 247 223  223  PHE PHE A . n 
A 1 248 GLN 248 224  224  GLN GLN A . n 
A 1 249 GLU 249 225  225  GLU GLU A . n 
A 1 250 ALA 250 226  226  ALA ALA A . n 
A 1 251 LYS 251 227  227  LYS LYS A . n 
A 1 252 ARG 252 228  228  ARG ARG A . n 
A 1 253 GLN 253 229  229  GLN GLN A . n 
A 1 254 LEU 254 230  230  LEU LEU A . n 
A 1 255 TYR 255 231  ?    ?   ?   A . n 
A 1 256 LYS 256 232  ?    ?   ?   A . n 
A 1 257 ILE 257 233  ?    ?   ?   A . n 
A 1 258 ASP 258 234  ?    ?   ?   A . n 
A 1 259 LYS 259 235  ?    ?   ?   A . n 
A 1 260 SER 260 236  ?    ?   ?   A . n 
A 1 261 GLU 261 237  ?    ?   ?   A . n 
A 1 262 GLY 262 238  ?    ?   ?   A . n 
A 1 263 ARG 263 239  ?    ?   ?   A . n 
A 1 264 PHE 264 240  ?    ?   ?   A . n 
A 1 265 HIS 265 241  ?    ?   ?   A . n 
A 1 266 VAL 266 242  ?    ?   ?   A . n 
A 1 267 GLN 267 243  ?    ?   ?   A . n 
A 1 268 ASN 268 244  ?    ?   ?   A . n 
A 1 269 LEU 269 245  ?    ?   ?   A . n 
A 1 270 SER 270 246  ?    ?   ?   A . n 
A 1 271 GLN 271 247  ?    ?   ?   A . n 
A 1 272 VAL 272 248  ?    ?   ?   A . n 
A 1 273 GLU 273 249  ?    ?   ?   A . n 
A 1 274 GLN 274 250  ?    ?   ?   A . n 
A 1 275 ASP 275 251  ?    ?   ?   A . n 
A 1 276 GLY 276 252  ?    ?   ?   A . n 
A 1 277 ARG 277 253  ?    ?   ?   A . n 
A 1 278 THR 278 254  ?    ?   ?   A . n 
A 1 279 GLY 279 255  ?    ?   ?   A . n 
A 1 280 HIS 280 256  ?    ?   ?   A . n 
A 1 281 GLY 281 257  ?    ?   ?   A . n 
A 1 282 LEU 282 258  ?    ?   ?   A . n 
A 1 283 ARG 283 259  ?    ?   ?   A . n 
A 1 284 ARG 284 260  ?    ?   ?   A . n 
A 1 285 SER 285 261  ?    ?   ?   A . n 
A 1 286 SER 286 262  ?    ?   ?   A . n 
A 1 287 LYS 287 263  263  LYS LYS A . n 
A 1 288 PHE 288 264  264  PHE PHE A . n 
A 1 289 CYS 289 265  265  CYS CYS A . n 
A 1 290 LEU 290 266  266  LEU LEU A . n 
A 1 291 LYS 291 267  267  LYS LYS A . n 
A 1 292 GLU 292 268  268  GLU GLU A . n 
A 1 293 HIS 293 269  269  HIS HIS A . n 
A 1 294 LYS 294 270  270  LYS LYS A . n 
A 1 295 ALA 295 271  271  ALA ALA A . n 
A 1 296 LEU 296 272  272  LEU LEU A . n 
A 1 297 LYS 297 273  273  LYS LYS A . n 
A 1 298 THR 298 274  274  THR THR A . n 
A 1 299 LEU 299 275  275  LEU LEU A . n 
A 1 300 GLY 300 276  276  GLY GLY A . n 
A 1 301 ILE 301 277  277  ILE ILE A . n 
A 1 302 ILE 302 278  278  ILE ILE A . n 
A 1 303 MET 303 279  279  MET MET A . n 
A 1 304 GLY 304 280  280  GLY GLY A . n 
A 1 305 THR 305 281  281  THR THR A . n 
A 1 306 PHE 306 282  282  PHE PHE A . n 
A 1 307 THR 307 283  283  THR THR A . n 
A 1 308 LEU 308 284  284  LEU LEU A . n 
A 1 309 CYS 309 285  285  CYS CYS A . n 
A 1 310 TRP 310 286  286  TRP TRP A . n 
A 1 311 LEU 311 287  287  LEU LEU A . n 
A 1 312 PRO 312 288  288  PRO PRO A . n 
A 1 313 PHE 313 289  289  PHE PHE A . n 
A 1 314 PHE 314 290  290  PHE PHE A . n 
A 1 315 ILE 315 291  291  ILE ILE A . n 
A 1 316 VAL 316 292  292  VAL VAL A . n 
A 1 317 ASN 317 293  293  ASN ASN A . n 
A 1 318 ILE 318 294  294  ILE ILE A . n 
A 1 319 VAL 319 295  295  VAL VAL A . n 
A 1 320 HIS 320 296  296  HIS HIS A . n 
A 1 321 VAL 321 297  297  VAL VAL A . n 
A 1 322 ILE 322 298  298  ILE ILE A . n 
A 1 323 GLN 323 299  299  GLN GLN A . n 
A 1 324 ASP 324 300  300  ASP ASP A . n 
A 1 325 ASN 325 301  301  ASN ASN A . n 
A 1 326 LEU 326 302  302  LEU LEU A . n 
A 1 327 ILE 327 303  303  ILE ILE A . n 
A 1 328 ARG 328 304  304  ARG ARG A . n 
A 1 329 LYS 329 305  305  LYS LYS A . n 
A 1 330 GLU 330 306  306  GLU GLU A . n 
A 1 331 VAL 331 307  307  VAL VAL A . n 
A 1 332 TYR 332 308  308  TYR TYR A . n 
A 1 333 ILE 333 309  309  ILE ILE A . n 
A 1 334 LEU 334 310  310  LEU LEU A . n 
A 1 335 LEU 335 311  311  LEU LEU A . n 
A 1 336 ASN 336 312  312  ASN ASN A . n 
A 1 337 TRP 337 313  313  TRP TRP A . n 
A 1 338 ILE 338 314  314  ILE ILE A . n 
A 1 339 GLY 339 315  315  GLY GLY A . n 
A 1 340 TYR 340 316  316  TYR TYR A . n 
A 1 341 VAL 341 317  317  VAL VAL A . n 
A 1 342 ASN 342 318  318  ASN ASN A . n 
A 1 343 SER 343 319  319  SER SER A . n 
A 1 344 GLY 344 320  320  GLY GLY A . n 
A 1 345 PHE 345 321  321  PHE PHE A . n 
A 1 346 ASN 346 322  322  ASN ASN A . n 
A 1 347 PRO 347 323  323  PRO PRO A . n 
A 1 348 LEU 348 324  324  LEU LEU A . n 
A 1 349 ILE 349 325  325  ILE ILE A . n 
A 1 350 TYR 350 326  326  TYR TYR A . n 
A 1 351 CYS 351 327  327  CYS CYS A . n 
A 1 352 ARG 352 328  328  ARG ARG A . n 
A 1 353 SER 353 329  329  SER SER A . n 
A 1 354 PRO 354 330  330  PRO PRO A . n 
A 1 355 ASP 355 331  331  ASP ASP A . n 
A 1 356 PHE 356 332  332  PHE PHE A . n 
A 1 357 ARG 357 333  333  ARG ARG A . n 
A 1 358 ILE 358 334  334  ILE ILE A . n 
A 1 359 ALA 359 335  335  ALA ALA A . n 
A 1 360 PHE 360 336  336  PHE PHE A . n 
A 1 361 GLN 361 337  337  GLN GLN A . n 
A 1 362 GLU 362 338  338  GLU GLU A . n 
A 1 363 LEU 363 339  339  LEU LEU A . n 
A 1 364 LEU 364 340  340  LEU LEU A . n 
A 1 365 CYS 365 341  341  CYS CYS A . n 
A 1 366 LEU 366 342  342  LEU LEU A . n 
A 1 367 ARG 367 979  ?    ?   ?   A . n 
A 1 368 ARG 368 980  ?    ?   ?   A . n 
A 1 369 SER 369 981  ?    ?   ?   A . n 
A 1 370 SER 370 982  ?    ?   ?   A . n 
A 1 371 LEU 371 983  ?    ?   ?   A . n 
A 1 372 LYS 372 984  ?    ?   ?   A . n 
A 1 373 ALA 373 985  ?    ?   ?   A . n 
A 1 374 TYR 374 986  ?    ?   ?   A . n 
A 1 375 GLY 375 987  ?    ?   ?   A . n 
A 1 376 ASN 376 988  ?    ?   ?   A . n 
A 1 377 GLY 377 989  ?    ?   ?   A . n 
A 1 378 TYR 378 990  ?    ?   ?   A . n 
A 1 379 SER 379 991  ?    ?   ?   A . n 
A 1 380 SER 380 992  ?    ?   ?   A . n 
A 1 381 ASN 381 993  ?    ?   ?   A . n 
A 1 382 GLY 382 994  ?    ?   ?   A . n 
A 1 383 ASN 383 995  ?    ?   ?   A . n 
A 1 384 THR 384 996  ?    ?   ?   A . n 
A 1 385 GLY 385 997  ?    ?   ?   A . n 
A 1 386 GLU 386 998  ?    ?   ?   A . n 
A 1 387 GLN 387 999  ?    ?   ?   A . n 
A 1 388 SER 388 1000 ?    ?   ?   A . n 
A 1 389 GLY 389 1001 ?    ?   ?   A . n 
A 1 390 ASN 390 1002 ?    ?   ?   A . n 
A 1 391 ILE 391 1003 1003 ILE ILE A . n 
A 1 392 PHE 392 1004 1004 PHE PHE A . n 
A 1 393 GLU 393 1005 1005 GLU GLU A . n 
A 1 394 MET 394 1006 1006 MET MET A . n 
A 1 395 LEU 395 1007 1007 LEU LEU A . n 
A 1 396 ARG 396 1008 1008 ARG ARG A . n 
A 1 397 ILE 397 1009 1009 ILE ILE A . n 
A 1 398 ASP 398 1010 1010 ASP ASP A . n 
A 1 399 GLU 399 1011 1011 GLU GLU A . n 
A 1 400 GLY 400 1012 1012 GLY GLY A . n 
A 1 401 LEU 401 1013 1013 LEU LEU A . n 
A 1 402 ARG 402 1014 1014 ARG ARG A . n 
A 1 403 LEU 403 1015 1015 LEU LEU A . n 
A 1 404 LYS 404 1016 1016 LYS LYS A . n 
A 1 405 ILE 405 1017 1017 ILE ILE A . n 
A 1 406 TYR 406 1018 1018 TYR TYR A . n 
A 1 407 LYS 407 1019 1019 LYS LYS A . n 
A 1 408 ASP 408 1020 1020 ASP ASP A . n 
A 1 409 THR 409 1021 1021 THR THR A . n 
A 1 410 GLU 410 1022 1022 GLU GLU A . n 
A 1 411 GLY 411 1023 1023 GLY GLY A . n 
A 1 412 TYR 412 1024 1024 TYR TYR A . n 
A 1 413 TYR 413 1025 1025 TYR TYR A . n 
A 1 414 THR 414 1026 1026 THR THR A . n 
A 1 415 ILE 415 1027 1027 ILE ILE A . n 
A 1 416 GLY 416 1028 1028 GLY GLY A . n 
A 1 417 ILE 417 1029 1029 ILE ILE A . n 
A 1 418 GLY 418 1030 1030 GLY GLY A . n 
A 1 419 HIS 419 1031 1031 HIS HIS A . n 
A 1 420 LEU 420 1032 1032 LEU LEU A . n 
A 1 421 LEU 421 1033 1033 LEU LEU A . n 
A 1 422 THR 422 1034 1034 THR THR A . n 
A 1 423 LYS 423 1035 1035 LYS LYS A . n 
A 1 424 SER 424 1036 1036 SER SER A . n 
A 1 425 PRO 425 1037 1037 PRO PRO A . n 
A 1 426 SER 426 1038 1038 SER SER A . n 
A 1 427 LEU 427 1039 1039 LEU LEU A . n 
A 1 428 ASN 428 1040 1040 ASN ASN A . n 
A 1 429 ALA 429 1041 1041 ALA ALA A . n 
A 1 430 ALA 430 1042 1042 ALA ALA A . n 
A 1 431 LYS 431 1043 1043 LYS LYS A . n 
A 1 432 SER 432 1044 1044 SER SER A . n 
A 1 433 GLU 433 1045 1045 GLU GLU A . n 
A 1 434 LEU 434 1046 1046 LEU LEU A . n 
A 1 435 ASP 435 1047 1047 ASP ASP A . n 
A 1 436 LYS 436 1048 1048 LYS LYS A . n 
A 1 437 ALA 437 1049 1049 ALA ALA A . n 
A 1 438 ILE 438 1050 1050 ILE ILE A . n 
A 1 439 GLY 439 1051 1051 GLY GLY A . n 
A 1 440 ARG 440 1052 1052 ARG ARG A . n 
A 1 441 ASN 441 1053 1053 ASN ASN A . n 
A 1 442 THR 442 1054 1054 THR THR A . n 
A 1 443 ASN 443 1055 1055 ASN ASN A . n 
A 1 444 GLY 444 1056 1056 GLY GLY A . n 
A 1 445 VAL 445 1057 1057 VAL VAL A . n 
A 1 446 ILE 446 1058 1058 ILE ILE A . n 
A 1 447 THR 447 1059 1059 THR THR A . n 
A 1 448 LYS 448 1060 1060 LYS LYS A . n 
A 1 449 ASP 449 1061 1061 ASP ASP A . n 
A 1 450 GLU 450 1062 1062 GLU GLU A . n 
A 1 451 ALA 451 1063 1063 ALA ALA A . n 
A 1 452 GLU 452 1064 1064 GLU GLU A . n 
A 1 453 LYS 453 1065 1065 LYS LYS A . n 
A 1 454 LEU 454 1066 1066 LEU LEU A . n 
A 1 455 PHE 455 1067 1067 PHE PHE A . n 
A 1 456 ASN 456 1068 1068 ASN ASN A . n 
A 1 457 GLN 457 1069 1069 GLN GLN A . n 
A 1 458 ASP 458 1070 1070 ASP ASP A . n 
A 1 459 VAL 459 1071 1071 VAL VAL A . n 
A 1 460 ASP 460 1072 1072 ASP ASP A . n 
A 1 461 ALA 461 1073 1073 ALA ALA A . n 
A 1 462 ALA 462 1074 1074 ALA ALA A . n 
A 1 463 VAL 463 1075 1075 VAL VAL A . n 
A 1 464 ARG 464 1076 1076 ARG ARG A . n 
A 1 465 GLY 465 1077 1077 GLY GLY A . n 
A 1 466 ILE 466 1078 1078 ILE ILE A . n 
A 1 467 LEU 467 1079 1079 LEU LEU A . n 
A 1 468 ARG 468 1080 1080 ARG ARG A . n 
A 1 469 ASN 469 1081 1081 ASN ASN A . n 
A 1 470 ALA 470 1082 1082 ALA ALA A . n 
A 1 471 LYS 471 1083 1083 LYS LYS A . n 
A 1 472 LEU 472 1084 1084 LEU LEU A . n 
A 1 473 LYS 473 1085 1085 LYS LYS A . n 
A 1 474 PRO 474 1086 1086 PRO PRO A . n 
A 1 475 VAL 475 1087 1087 VAL VAL A . n 
A 1 476 TYR 476 1088 1088 TYR TYR A . n 
A 1 477 ASP 477 1089 1089 ASP ASP A . n 
A 1 478 SER 478 1090 1090 SER SER A . n 
A 1 479 LEU 479 1091 1091 LEU LEU A . n 
A 1 480 ASP 480 1092 1092 ASP ASP A . n 
A 1 481 ALA 481 1093 1093 ALA ALA A . n 
A 1 482 VAL 482 1094 1094 VAL VAL A . n 
A 1 483 ARG 483 1095 1095 ARG ARG A . n 
A 1 484 ARG 484 1096 1096 ARG ARG A . n 
A 1 485 ALA 485 1097 1097 ALA ALA A . n 
A 1 486 ALA 486 1098 1098 ALA ALA A . n 
A 1 487 LEU 487 1099 1099 LEU LEU A . n 
A 1 488 ILE 488 1100 1100 ILE ILE A . n 
A 1 489 ASN 489 1101 1101 ASN ASN A . n 
A 1 490 MET 490 1102 1102 MET MET A . n 
A 1 491 VAL 491 1103 1103 VAL VAL A . n 
A 1 492 PHE 492 1104 1104 PHE PHE A . n 
A 1 493 GLN 493 1105 1105 GLN GLN A . n 
A 1 494 MET 494 1106 1106 MET MET A . n 
A 1 495 GLY 495 1107 1107 GLY GLY A . n 
A 1 496 GLU 496 1108 1108 GLU GLU A . n 
A 1 497 THR 497 1109 1109 THR THR A . n 
A 1 498 GLY 498 1110 1110 GLY GLY A . n 
A 1 499 VAL 499 1111 1111 VAL VAL A . n 
A 1 500 ALA 500 1112 1112 ALA ALA A . n 
A 1 501 GLY 501 1113 1113 GLY GLY A . n 
A 1 502 PHE 502 1114 1114 PHE PHE A . n 
A 1 503 THR 503 1115 1115 THR THR A . n 
A 1 504 ASN 504 1116 1116 ASN ASN A . n 
A 1 505 SER 505 1117 1117 SER SER A . n 
A 1 506 LEU 506 1118 1118 LEU LEU A . n 
A 1 507 ARG 507 1119 1119 ARG ARG A . n 
A 1 508 MET 508 1120 1120 MET MET A . n 
A 1 509 LEU 509 1121 1121 LEU LEU A . n 
A 1 510 GLN 510 1122 1122 GLN GLN A . n 
A 1 511 GLN 511 1123 1123 GLN GLN A . n 
A 1 512 LYS 512 1124 1124 LYS LYS A . n 
A 1 513 ARG 513 1125 1125 ARG ARG A . n 
A 1 514 TRP 514 1126 1126 TRP TRP A . n 
A 1 515 ASP 515 1127 1127 ASP ASP A . n 
A 1 516 GLU 516 1128 1128 GLU GLU A . n 
A 1 517 ALA 517 1129 1129 ALA ALA A . n 
A 1 518 ALA 518 1130 1130 ALA ALA A . n 
A 1 519 VAL 519 1131 1131 VAL VAL A . n 
A 1 520 ASN 520 1132 1132 ASN ASN A . n 
A 1 521 LEU 521 1133 1133 LEU LEU A . n 
A 1 522 ALA 522 1134 1134 ALA ALA A . n 
A 1 523 LYS 523 1135 1135 LYS LYS A . n 
A 1 524 SER 524 1136 1136 SER SER A . n 
A 1 525 ARG 525 1137 1137 ARG ARG A . n 
A 1 526 TRP 526 1138 1138 TRP TRP A . n 
A 1 527 TYR 527 1139 1139 TYR TYR A . n 
A 1 528 ASN 528 1140 1140 ASN ASN A . n 
A 1 529 GLN 529 1141 1141 GLN GLN A . n 
A 1 530 THR 530 1142 1142 THR THR A . n 
A 1 531 PRO 531 1143 1143 PRO PRO A . n 
A 1 532 ASN 532 1144 1144 ASN ASN A . n 
A 1 533 ARG 533 1145 1145 ARG ARG A . n 
A 1 534 ALA 534 1146 1146 ALA ALA A . n 
A 1 535 LYS 535 1147 1147 LYS LYS A . n 
A 1 536 ARG 536 1148 1148 ARG ARG A . n 
A 1 537 VAL 537 1149 1149 VAL VAL A . n 
A 1 538 ILE 538 1150 1150 ILE ILE A . n 
A 1 539 THR 539 1151 1151 THR THR A . n 
A 1 540 THR 540 1152 1152 THR THR A . n 
A 1 541 PHE 541 1153 1153 PHE PHE A . n 
A 1 542 ARG 542 1154 1154 ARG ARG A . n 
A 1 543 THR 543 1155 1155 THR THR A . n 
A 1 544 GLY 544 1156 1156 GLY GLY A . n 
A 1 545 THR 545 1157 1157 THR THR A . n 
A 1 546 TRP 546 1158 1158 TRP TRP A . n 
A 1 547 ASP 547 1159 1159 ASP ASP A . n 
A 1 548 ALA 548 1160 1160 ALA ALA A . n 
A 1 549 TYR 549 1161 1161 TYR TYR A . n 
B 1 1   MET 1   -23  ?    ?   ?   B . n 
B 1 2   LYS 2   -22  ?    ?   ?   B . n 
B 1 3   THR 3   -21  ?    ?   ?   B . n 
B 1 4   ILE 4   -20  ?    ?   ?   B . n 
B 1 5   ILE 5   -19  ?    ?   ?   B . n 
B 1 6   ALA 6   -18  ?    ?   ?   B . n 
B 1 7   LEU 7   -17  ?    ?   ?   B . n 
B 1 8   SER 8   -16  ?    ?   ?   B . n 
B 1 9   TYR 9   -15  ?    ?   ?   B . n 
B 1 10  ILE 10  -14  ?    ?   ?   B . n 
B 1 11  PHE 11  -13  ?    ?   ?   B . n 
B 1 12  CYS 12  -12  ?    ?   ?   B . n 
B 1 13  LEU 13  -11  ?    ?   ?   B . n 
B 1 14  VAL 14  -10  ?    ?   ?   B . n 
B 1 15  PHE 15  -9   ?    ?   ?   B . n 
B 1 16  ALA 16  -8   ?    ?   ?   B . n 
B 1 17  ASP 17  -7   ?    ?   ?   B . n 
B 1 18  TYR 18  -6   ?    ?   ?   B . n 
B 1 19  LYS 19  -5   ?    ?   ?   B . n 
B 1 20  ASP 20  -4   ?    ?   ?   B . n 
B 1 21  ASP 21  -3   ?    ?   ?   B . n 
B 1 22  ASP 22  -2   ?    ?   ?   B . n 
B 1 23  ASP 23  -1   ?    ?   ?   B . n 
B 1 24  ALA 24  0    ?    ?   ?   B . n 
B 1 25  MET 25  1    ?    ?   ?   B . n 
B 1 26  GLY 26  2    ?    ?   ?   B . n 
B 1 27  GLN 27  3    ?    ?   ?   B . n 
B 1 28  PRO 28  4    ?    ?   ?   B . n 
B 1 29  GLY 29  5    ?    ?   ?   B . n 
B 1 30  ASN 30  6    ?    ?   ?   B . n 
B 1 31  GLY 31  7    ?    ?   ?   B . n 
B 1 32  SER 32  8    ?    ?   ?   B . n 
B 1 33  ALA 33  9    ?    ?   ?   B . n 
B 1 34  PHE 34  10   ?    ?   ?   B . n 
B 1 35  LEU 35  11   ?    ?   ?   B . n 
B 1 36  LEU 36  12   ?    ?   ?   B . n 
B 1 37  ALA 37  13   ?    ?   ?   B . n 
B 1 38  PRO 38  14   ?    ?   ?   B . n 
B 1 39  ASN 39  15   ?    ?   ?   B . n 
B 1 40  ARG 40  16   ?    ?   ?   B . n 
B 1 41  SER 41  17   ?    ?   ?   B . n 
B 1 42  HIS 42  18   ?    ?   ?   B . n 
B 1 43  ALA 43  19   ?    ?   ?   B . n 
B 1 44  PRO 44  20   ?    ?   ?   B . n 
B 1 45  ASP 45  21   ?    ?   ?   B . n 
B 1 46  HIS 46  22   ?    ?   ?   B . n 
B 1 47  ASP 47  23   ?    ?   ?   B . n 
B 1 48  VAL 48  24   ?    ?   ?   B . n 
B 1 49  THR 49  25   ?    ?   ?   B . n 
B 1 50  GLN 50  26   ?    ?   ?   B . n 
B 1 51  GLN 51  27   ?    ?   ?   B . n 
B 1 52  ARG 52  28   ?    ?   ?   B . n 
B 1 53  ASP 53  29   29   ASP ASP B . n 
B 1 54  GLU 54  30   30   GLU GLU B . n 
B 1 55  VAL 55  31   31   VAL VAL B . n 
B 1 56  TRP 56  32   32   TRP TRP B . n 
B 1 57  VAL 57  33   33   VAL VAL B . n 
B 1 58  VAL 58  34   34   VAL VAL B . n 
B 1 59  GLY 59  35   35   GLY GLY B . n 
B 1 60  MET 60  36   36   MET MET B . n 
B 1 61  GLY 61  37   37   GLY GLY B . n 
B 1 62  ILE 62  38   38   ILE ILE B . n 
B 1 63  VAL 63  39   39   VAL VAL B . n 
B 1 64  MET 64  40   40   MET MET B . n 
B 1 65  SER 65  41   41   SER SER B . n 
B 1 66  LEU 66  42   42   LEU LEU B . n 
B 1 67  ILE 67  43   43   ILE ILE B . n 
B 1 68  VAL 68  44   44   VAL VAL B . n 
B 1 69  LEU 69  45   45   LEU LEU B . n 
B 1 70  ALA 70  46   46   ALA ALA B . n 
B 1 71  ILE 71  47   47   ILE ILE B . n 
B 1 72  VAL 72  48   48   VAL VAL B . n 
B 1 73  PHE 73  49   49   PHE PHE B . n 
B 1 74  GLY 74  50   50   GLY GLY B . n 
B 1 75  ASN 75  51   51   ASN ASN B . n 
B 1 76  VAL 76  52   52   VAL VAL B . n 
B 1 77  LEU 77  53   53   LEU LEU B . n 
B 1 78  VAL 78  54   54   VAL VAL B . n 
B 1 79  ILE 79  55   55   ILE ILE B . n 
B 1 80  THR 80  56   56   THR THR B . n 
B 1 81  ALA 81  57   57   ALA ALA B . n 
B 1 82  ILE 82  58   58   ILE ILE B . n 
B 1 83  ALA 83  59   59   ALA ALA B . n 
B 1 84  LYS 84  60   60   LYS LYS B . n 
B 1 85  PHE 85  61   61   PHE PHE B . n 
B 1 86  GLU 86  62   62   GLU GLU B . n 
B 1 87  ARG 87  63   63   ARG ARG B . n 
B 1 88  LEU 88  64   64   LEU LEU B . n 
B 1 89  GLN 89  65   65   GLN GLN B . n 
B 1 90  THR 90  66   66   THR THR B . n 
B 1 91  VAL 91  67   67   VAL VAL B . n 
B 1 92  THR 92  68   68   THR THR B . n 
B 1 93  ASN 93  69   69   ASN ASN B . n 
B 1 94  TYR 94  70   70   TYR TYR B . n 
B 1 95  PHE 95  71   71   PHE PHE B . n 
B 1 96  ILE 96  72   72   ILE ILE B . n 
B 1 97  THR 97  73   73   THR THR B . n 
B 1 98  SER 98  74   74   SER SER B . n 
B 1 99  LEU 99  75   75   LEU LEU B . n 
B 1 100 ALA 100 76   76   ALA ALA B . n 
B 1 101 CYS 101 77   77   CYS CYS B . n 
B 1 102 ALA 102 78   78   ALA ALA B . n 
B 1 103 ASP 103 79   79   ASP ASP B . n 
B 1 104 LEU 104 80   80   LEU LEU B . n 
B 1 105 VAL 105 81   81   VAL VAL B . n 
B 1 106 MET 106 82   82   MET MET B . n 
B 1 107 GLY 107 83   83   GLY GLY B . n 
B 1 108 LEU 108 84   84   LEU LEU B . n 
B 1 109 ALA 109 85   85   ALA ALA B . n 
B 1 110 VAL 110 86   86   VAL VAL B . n 
B 1 111 VAL 111 87   87   VAL VAL B . n 
B 1 112 PRO 112 88   88   PRO PRO B . n 
B 1 113 PHE 113 89   89   PHE PHE B . n 
B 1 114 GLY 114 90   90   GLY GLY B . n 
B 1 115 ALA 115 91   91   ALA ALA B . n 
B 1 116 ALA 116 92   92   ALA ALA B . n 
B 1 117 HIS 117 93   93   HIS HIS B . n 
B 1 118 ILE 118 94   94   ILE ILE B . n 
B 1 119 LEU 119 95   95   LEU LEU B . n 
B 1 120 MET 120 96   96   MET MET B . n 
B 1 121 LYS 121 97   97   LYS LYS B . n 
B 1 122 MET 122 98   98   MET MET B . n 
B 1 123 TRP 123 99   99   TRP TRP B . n 
B 1 124 THR 124 100  100  THR THR B . n 
B 1 125 PHE 125 101  101  PHE PHE B . n 
B 1 126 GLY 126 102  102  GLY GLY B . n 
B 1 127 ASN 127 103  103  ASN ASN B . n 
B 1 128 PHE 128 104  104  PHE PHE B . n 
B 1 129 TRP 129 105  105  TRP TRP B . n 
B 1 130 CYS 130 106  106  CYS CYS B . n 
B 1 131 GLU 131 107  107  GLU GLU B . n 
B 1 132 PHE 132 108  108  PHE PHE B . n 
B 1 133 TRP 133 109  109  TRP TRP B . n 
B 1 134 THR 134 110  110  THR THR B . n 
B 1 135 SER 135 111  111  SER SER B . n 
B 1 136 ILE 136 112  112  ILE ILE B . n 
B 1 137 ASP 137 113  113  ASP ASP B . n 
B 1 138 VAL 138 114  114  VAL VAL B . n 
B 1 139 LEU 139 115  115  LEU LEU B . n 
B 1 140 CYS 140 116  116  CYS CYS B . n 
B 1 141 VAL 141 117  117  VAL VAL B . n 
B 1 142 THR 142 118  118  THR THR B . n 
B 1 143 ALA 143 119  119  ALA ALA B . n 
B 1 144 SER 144 120  120  SER SER B . n 
B 1 145 ILE 145 121  121  ILE ILE B . n 
B 1 146 GLU 146 122  122  GLU GLU B . n 
B 1 147 THR 147 123  123  THR THR B . n 
B 1 148 LEU 148 124  124  LEU LEU B . n 
B 1 149 CYS 149 125  125  CYS CYS B . n 
B 1 150 VAL 150 126  126  VAL VAL B . n 
B 1 151 ILE 151 127  127  ILE ILE B . n 
B 1 152 ALA 152 128  128  ALA ALA B . n 
B 1 153 VAL 153 129  129  VAL VAL B . n 
B 1 154 ASP 154 130  130  ASP ASP B . n 
B 1 155 ARG 155 131  131  ARG ARG B . n 
B 1 156 TYR 156 132  132  TYR TYR B . n 
B 1 157 PHE 157 133  133  PHE PHE B . n 
B 1 158 ALA 158 134  134  ALA ALA B . n 
B 1 159 ILE 159 135  135  ILE ILE B . n 
B 1 160 THR 160 136  136  THR THR B . n 
B 1 161 SER 161 137  137  SER SER B . n 
B 1 162 PRO 162 138  138  PRO PRO B . n 
B 1 163 PHE 163 139  139  PHE PHE B . n 
B 1 164 LYS 164 140  140  LYS LYS B . n 
B 1 165 TYR 165 141  141  TYR TYR B . n 
B 1 166 GLN 166 142  142  GLN GLN B . n 
B 1 167 SER 167 143  143  SER SER B . n 
B 1 168 LEU 168 144  144  LEU LEU B . n 
B 1 169 LEU 169 145  145  LEU LEU B . n 
B 1 170 THR 170 146  146  THR THR B . n 
B 1 171 LYS 171 147  147  LYS LYS B . n 
B 1 172 ASN 172 148  148  ASN ASN B . n 
B 1 173 LYS 173 149  149  LYS LYS B . n 
B 1 174 ALA 174 150  150  ALA ALA B . n 
B 1 175 ARG 175 151  151  ARG ARG B . n 
B 1 176 VAL 176 152  152  VAL VAL B . n 
B 1 177 ILE 177 153  153  ILE ILE B . n 
B 1 178 ILE 178 154  154  ILE ILE B . n 
B 1 179 LEU 179 155  155  LEU LEU B . n 
B 1 180 MET 180 156  156  MET MET B . n 
B 1 181 VAL 181 157  157  VAL VAL B . n 
B 1 182 TRP 182 158  158  TRP TRP B . n 
B 1 183 ILE 183 159  159  ILE ILE B . n 
B 1 184 VAL 184 160  160  VAL VAL B . n 
B 1 185 SER 185 161  161  SER SER B . n 
B 1 186 GLY 186 162  162  GLY GLY B . n 
B 1 187 LEU 187 163  163  LEU LEU B . n 
B 1 188 THR 188 164  164  THR THR B . n 
B 1 189 SER 189 165  165  SER SER B . n 
B 1 190 PHE 190 166  166  PHE PHE B . n 
B 1 191 LEU 191 167  167  LEU LEU B . n 
B 1 192 PRO 192 168  168  PRO PRO B . n 
B 1 193 ILE 193 169  169  ILE ILE B . n 
B 1 194 GLN 194 170  170  GLN GLN B . n 
B 1 195 MET 195 171  171  MET MET B . n 
B 1 196 HIS 196 172  172  HIS HIS B . n 
B 1 197 TRP 197 173  173  TRP TRP B . n 
B 1 198 TYR 198 174  174  TYR TYR B . n 
B 1 199 ARG 199 175  175  ARG ARG B . n 
B 1 200 ALA 200 176  176  ALA ALA B . n 
B 1 201 THR 201 177  177  THR THR B . n 
B 1 202 HIS 202 178  178  HIS HIS B . n 
B 1 203 GLN 203 179  179  GLN GLN B . n 
B 1 204 GLU 204 180  180  GLU GLU B . n 
B 1 205 ALA 205 181  181  ALA ALA B . n 
B 1 206 ILE 206 182  182  ILE ILE B . n 
B 1 207 ASN 207 183  183  ASN ASN B . n 
B 1 208 CYS 208 184  184  CYS CYS B . n 
B 1 209 TYR 209 185  185  TYR TYR B . n 
B 1 210 ALA 210 186  186  ALA ALA B . n 
B 1 211 GLU 211 187  187  GLU GLU B . n 
B 1 212 GLU 212 188  188  GLU GLU B . n 
B 1 213 THR 213 189  189  THR THR B . n 
B 1 214 CYS 214 190  190  CYS CYS B . n 
B 1 215 CYS 215 191  191  CYS CYS B . n 
B 1 216 ASP 216 192  192  ASP ASP B . n 
B 1 217 PHE 217 193  193  PHE PHE B . n 
B 1 218 PHE 218 194  194  PHE PHE B . n 
B 1 219 THR 219 195  195  THR THR B . n 
B 1 220 ASN 220 196  196  ASN ASN B . n 
B 1 221 GLN 221 197  197  GLN GLN B . n 
B 1 222 ALA 222 198  198  ALA ALA B . n 
B 1 223 TYR 223 199  199  TYR TYR B . n 
B 1 224 ALA 224 200  200  ALA ALA B . n 
B 1 225 ILE 225 201  201  ILE ILE B . n 
B 1 226 ALA 226 202  202  ALA ALA B . n 
B 1 227 SER 227 203  203  SER SER B . n 
B 1 228 SER 228 204  204  SER SER B . n 
B 1 229 ILE 229 205  205  ILE ILE B . n 
B 1 230 VAL 230 206  206  VAL VAL B . n 
B 1 231 SER 231 207  207  SER SER B . n 
B 1 232 PHE 232 208  208  PHE PHE B . n 
B 1 233 TYR 233 209  209  TYR TYR B . n 
B 1 234 VAL 234 210  210  VAL VAL B . n 
B 1 235 PRO 235 211  211  PRO PRO B . n 
B 1 236 LEU 236 212  212  LEU LEU B . n 
B 1 237 VAL 237 213  213  VAL VAL B . n 
B 1 238 ILE 238 214  214  ILE ILE B . n 
B 1 239 MET 239 215  215  MET MET B . n 
B 1 240 VAL 240 216  216  VAL VAL B . n 
B 1 241 PHE 241 217  217  PHE PHE B . n 
B 1 242 VAL 242 218  218  VAL VAL B . n 
B 1 243 TYR 243 219  219  TYR TYR B . n 
B 1 244 SER 244 220  220  SER SER B . n 
B 1 245 ARG 245 221  221  ARG ARG B . n 
B 1 246 VAL 246 222  222  VAL VAL B . n 
B 1 247 PHE 247 223  223  PHE PHE B . n 
B 1 248 GLN 248 224  224  GLN GLN B . n 
B 1 249 GLU 249 225  225  GLU GLU B . n 
B 1 250 ALA 250 226  226  ALA ALA B . n 
B 1 251 LYS 251 227  227  LYS LYS B . n 
B 1 252 ARG 252 228  228  ARG ARG B . n 
B 1 253 GLN 253 229  229  GLN GLN B . n 
B 1 254 LEU 254 230  ?    ?   ?   B . n 
B 1 255 TYR 255 231  ?    ?   ?   B . n 
B 1 256 LYS 256 232  ?    ?   ?   B . n 
B 1 257 ILE 257 233  ?    ?   ?   B . n 
B 1 258 ASP 258 234  ?    ?   ?   B . n 
B 1 259 LYS 259 235  ?    ?   ?   B . n 
B 1 260 SER 260 236  ?    ?   ?   B . n 
B 1 261 GLU 261 237  ?    ?   ?   B . n 
B 1 262 GLY 262 238  ?    ?   ?   B . n 
B 1 263 ARG 263 239  ?    ?   ?   B . n 
B 1 264 PHE 264 240  ?    ?   ?   B . n 
B 1 265 HIS 265 241  ?    ?   ?   B . n 
B 1 266 VAL 266 242  ?    ?   ?   B . n 
B 1 267 GLN 267 243  ?    ?   ?   B . n 
B 1 268 ASN 268 244  ?    ?   ?   B . n 
B 1 269 LEU 269 245  ?    ?   ?   B . n 
B 1 270 SER 270 246  ?    ?   ?   B . n 
B 1 271 GLN 271 247  ?    ?   ?   B . n 
B 1 272 VAL 272 248  ?    ?   ?   B . n 
B 1 273 GLU 273 249  ?    ?   ?   B . n 
B 1 274 GLN 274 250  ?    ?   ?   B . n 
B 1 275 ASP 275 251  ?    ?   ?   B . n 
B 1 276 GLY 276 252  ?    ?   ?   B . n 
B 1 277 ARG 277 253  ?    ?   ?   B . n 
B 1 278 THR 278 254  ?    ?   ?   B . n 
B 1 279 GLY 279 255  ?    ?   ?   B . n 
B 1 280 HIS 280 256  ?    ?   ?   B . n 
B 1 281 GLY 281 257  ?    ?   ?   B . n 
B 1 282 LEU 282 258  ?    ?   ?   B . n 
B 1 283 ARG 283 259  ?    ?   ?   B . n 
B 1 284 ARG 284 260  ?    ?   ?   B . n 
B 1 285 SER 285 261  ?    ?   ?   B . n 
B 1 286 SER 286 262  ?    ?   ?   B . n 
B 1 287 LYS 287 263  263  LYS LYS B . n 
B 1 288 PHE 288 264  264  PHE PHE B . n 
B 1 289 CYS 289 265  265  CYS CYS B . n 
B 1 290 LEU 290 266  266  LEU LEU B . n 
B 1 291 LYS 291 267  267  LYS LYS B . n 
B 1 292 GLU 292 268  268  GLU GLU B . n 
B 1 293 HIS 293 269  269  HIS HIS B . n 
B 1 294 LYS 294 270  270  LYS LYS B . n 
B 1 295 ALA 295 271  271  ALA ALA B . n 
B 1 296 LEU 296 272  272  LEU LEU B . n 
B 1 297 LYS 297 273  273  LYS LYS B . n 
B 1 298 THR 298 274  274  THR THR B . n 
B 1 299 LEU 299 275  275  LEU LEU B . n 
B 1 300 GLY 300 276  276  GLY GLY B . n 
B 1 301 ILE 301 277  277  ILE ILE B . n 
B 1 302 ILE 302 278  278  ILE ILE B . n 
B 1 303 MET 303 279  279  MET MET B . n 
B 1 304 GLY 304 280  280  GLY GLY B . n 
B 1 305 THR 305 281  281  THR THR B . n 
B 1 306 PHE 306 282  282  PHE PHE B . n 
B 1 307 THR 307 283  283  THR THR B . n 
B 1 308 LEU 308 284  284  LEU LEU B . n 
B 1 309 CYS 309 285  285  CYS CYS B . n 
B 1 310 TRP 310 286  286  TRP TRP B . n 
B 1 311 LEU 311 287  287  LEU LEU B . n 
B 1 312 PRO 312 288  288  PRO PRO B . n 
B 1 313 PHE 313 289  289  PHE PHE B . n 
B 1 314 PHE 314 290  290  PHE PHE B . n 
B 1 315 ILE 315 291  291  ILE ILE B . n 
B 1 316 VAL 316 292  292  VAL VAL B . n 
B 1 317 ASN 317 293  293  ASN ASN B . n 
B 1 318 ILE 318 294  294  ILE ILE B . n 
B 1 319 VAL 319 295  295  VAL VAL B . n 
B 1 320 HIS 320 296  296  HIS HIS B . n 
B 1 321 VAL 321 297  297  VAL VAL B . n 
B 1 322 ILE 322 298  298  ILE ILE B . n 
B 1 323 GLN 323 299  299  GLN GLN B . n 
B 1 324 ASP 324 300  300  ASP ASP B . n 
B 1 325 ASN 325 301  301  ASN ASN B . n 
B 1 326 LEU 326 302  302  LEU LEU B . n 
B 1 327 ILE 327 303  303  ILE ILE B . n 
B 1 328 ARG 328 304  304  ARG ARG B . n 
B 1 329 LYS 329 305  305  LYS LYS B . n 
B 1 330 GLU 330 306  306  GLU GLU B . n 
B 1 331 VAL 331 307  307  VAL VAL B . n 
B 1 332 TYR 332 308  308  TYR TYR B . n 
B 1 333 ILE 333 309  309  ILE ILE B . n 
B 1 334 LEU 334 310  310  LEU LEU B . n 
B 1 335 LEU 335 311  311  LEU LEU B . n 
B 1 336 ASN 336 312  312  ASN ASN B . n 
B 1 337 TRP 337 313  313  TRP TRP B . n 
B 1 338 ILE 338 314  314  ILE ILE B . n 
B 1 339 GLY 339 315  315  GLY GLY B . n 
B 1 340 TYR 340 316  316  TYR TYR B . n 
B 1 341 VAL 341 317  317  VAL VAL B . n 
B 1 342 ASN 342 318  318  ASN ASN B . n 
B 1 343 SER 343 319  319  SER SER B . n 
B 1 344 GLY 344 320  320  GLY GLY B . n 
B 1 345 PHE 345 321  321  PHE PHE B . n 
B 1 346 ASN 346 322  322  ASN ASN B . n 
B 1 347 PRO 347 323  323  PRO PRO B . n 
B 1 348 LEU 348 324  324  LEU LEU B . n 
B 1 349 ILE 349 325  325  ILE ILE B . n 
B 1 350 TYR 350 326  326  TYR TYR B . n 
B 1 351 CYS 351 327  327  CYS CYS B . n 
B 1 352 ARG 352 328  328  ARG ARG B . n 
B 1 353 SER 353 329  329  SER SER B . n 
B 1 354 PRO 354 330  330  PRO PRO B . n 
B 1 355 ASP 355 331  331  ASP ASP B . n 
B 1 356 PHE 356 332  332  PHE PHE B . n 
B 1 357 ARG 357 333  333  ARG ARG B . n 
B 1 358 ILE 358 334  334  ILE ILE B . n 
B 1 359 ALA 359 335  335  ALA ALA B . n 
B 1 360 PHE 360 336  336  PHE PHE B . n 
B 1 361 GLN 361 337  337  GLN GLN B . n 
B 1 362 GLU 362 338  338  GLU GLU B . n 
B 1 363 LEU 363 339  339  LEU LEU B . n 
B 1 364 LEU 364 340  340  LEU LEU B . n 
B 1 365 CYS 365 341  341  CYS CYS B . n 
B 1 366 LEU 366 342  342  LEU LEU B . n 
B 1 367 ARG 367 979  ?    ?   ?   B . n 
B 1 368 ARG 368 980  ?    ?   ?   B . n 
B 1 369 SER 369 981  ?    ?   ?   B . n 
B 1 370 SER 370 982  ?    ?   ?   B . n 
B 1 371 LEU 371 983  ?    ?   ?   B . n 
B 1 372 LYS 372 984  ?    ?   ?   B . n 
B 1 373 ALA 373 985  ?    ?   ?   B . n 
B 1 374 TYR 374 986  ?    ?   ?   B . n 
B 1 375 GLY 375 987  ?    ?   ?   B . n 
B 1 376 ASN 376 988  ?    ?   ?   B . n 
B 1 377 GLY 377 989  ?    ?   ?   B . n 
B 1 378 TYR 378 990  ?    ?   ?   B . n 
B 1 379 SER 379 991  ?    ?   ?   B . n 
B 1 380 SER 380 992  ?    ?   ?   B . n 
B 1 381 ASN 381 993  ?    ?   ?   B . n 
B 1 382 GLY 382 994  ?    ?   ?   B . n 
B 1 383 ASN 383 995  ?    ?   ?   B . n 
B 1 384 THR 384 996  ?    ?   ?   B . n 
B 1 385 GLY 385 997  ?    ?   ?   B . n 
B 1 386 GLU 386 998  ?    ?   ?   B . n 
B 1 387 GLN 387 999  ?    ?   ?   B . n 
B 1 388 SER 388 1000 ?    ?   ?   B . n 
B 1 389 GLY 389 1001 ?    ?   ?   B . n 
B 1 390 ASN 390 1002 1002 ASN ASN B . n 
B 1 391 ILE 391 1003 1003 ILE ILE B . n 
B 1 392 PHE 392 1004 1004 PHE PHE B . n 
B 1 393 GLU 393 1005 1005 GLU GLU B . n 
B 1 394 MET 394 1006 1006 MET MET B . n 
B 1 395 LEU 395 1007 1007 LEU LEU B . n 
B 1 396 ARG 396 1008 1008 ARG ARG B . n 
B 1 397 ILE 397 1009 1009 ILE ILE B . n 
B 1 398 ASP 398 1010 1010 ASP ASP B . n 
B 1 399 GLU 399 1011 1011 GLU GLU B . n 
B 1 400 GLY 400 1012 1012 GLY GLY B . n 
B 1 401 LEU 401 1013 1013 LEU LEU B . n 
B 1 402 ARG 402 1014 1014 ARG ARG B . n 
B 1 403 LEU 403 1015 1015 LEU LEU B . n 
B 1 404 LYS 404 1016 1016 LYS LYS B . n 
B 1 405 ILE 405 1017 1017 ILE ILE B . n 
B 1 406 TYR 406 1018 1018 TYR TYR B . n 
B 1 407 LYS 407 1019 1019 LYS LYS B . n 
B 1 408 ASP 408 1020 1020 ASP ASP B . n 
B 1 409 THR 409 1021 1021 THR THR B . n 
B 1 410 GLU 410 1022 1022 GLU GLU B . n 
B 1 411 GLY 411 1023 1023 GLY GLY B . n 
B 1 412 TYR 412 1024 1024 TYR TYR B . n 
B 1 413 TYR 413 1025 1025 TYR TYR B . n 
B 1 414 THR 414 1026 1026 THR THR B . n 
B 1 415 ILE 415 1027 1027 ILE ALA B . n 
B 1 416 GLY 416 1028 1028 GLY GLY B . n 
B 1 417 ILE 417 1029 1029 ILE ILE B . n 
B 1 418 GLY 418 1030 1030 GLY GLY B . n 
B 1 419 HIS 419 1031 1031 HIS HIS B . n 
B 1 420 LEU 420 1032 1032 LEU LEU B . n 
B 1 421 LEU 421 1033 1033 LEU LEU B . n 
B 1 422 THR 422 1034 1034 THR THR B . n 
B 1 423 LYS 423 1035 1035 LYS LYS B . n 
B 1 424 SER 424 1036 1036 SER SER B . n 
B 1 425 PRO 425 1037 1037 PRO PRO B . n 
B 1 426 SER 426 1038 1038 SER SER B . n 
B 1 427 LEU 427 1039 1039 LEU LEU B . n 
B 1 428 ASN 428 1040 1040 ASN ASN B . n 
B 1 429 ALA 429 1041 1041 ALA ALA B . n 
B 1 430 ALA 430 1042 1042 ALA ALA B . n 
B 1 431 LYS 431 1043 1043 LYS LYS B . n 
B 1 432 SER 432 1044 1044 SER SER B . n 
B 1 433 GLU 433 1045 1045 GLU GLU B . n 
B 1 434 LEU 434 1046 1046 LEU LEU B . n 
B 1 435 ASP 435 1047 1047 ASP ASP B . n 
B 1 436 LYS 436 1048 1048 LYS LYS B . n 
B 1 437 ALA 437 1049 1049 ALA ALA B . n 
B 1 438 ILE 438 1050 1050 ILE ILE B . n 
B 1 439 GLY 439 1051 1051 GLY GLY B . n 
B 1 440 ARG 440 1052 1052 ARG ARG B . n 
B 1 441 ASN 441 1053 1053 ASN ASN B . n 
B 1 442 THR 442 1054 1054 THR THR B . n 
B 1 443 ASN 443 1055 1055 ASN ASN B . n 
B 1 444 GLY 444 1056 ?    ?   ?   B . n 
B 1 445 VAL 445 1057 ?    ?   ?   B . n 
B 1 446 ILE 446 1058 1058 ILE ILE B . n 
B 1 447 THR 447 1059 1059 THR THR B . n 
B 1 448 LYS 448 1060 1060 LYS LYS B . n 
B 1 449 ASP 449 1061 1061 ASP ASP B . n 
B 1 450 GLU 450 1062 1062 GLU GLU B . n 
B 1 451 ALA 451 1063 1063 ALA ALA B . n 
B 1 452 GLU 452 1064 1064 GLU GLU B . n 
B 1 453 LYS 453 1065 1065 LYS LYS B . n 
B 1 454 LEU 454 1066 1066 LEU LEU B . n 
B 1 455 PHE 455 1067 1067 PHE PHE B . n 
B 1 456 ASN 456 1068 1068 ASN ASN B . n 
B 1 457 GLN 457 1069 1069 GLN GLN B . n 
B 1 458 ASP 458 1070 1070 ASP ASP B . n 
B 1 459 VAL 459 1071 1071 VAL VAL B . n 
B 1 460 ASP 460 1072 1072 ASP ASP B . n 
B 1 461 ALA 461 1073 1073 ALA ALA B . n 
B 1 462 ALA 462 1074 1074 ALA ALA B . n 
B 1 463 VAL 463 1075 1075 VAL VAL B . n 
B 1 464 ARG 464 1076 1076 ARG ARG B . n 
B 1 465 GLY 465 1077 1077 GLY GLY B . n 
B 1 466 ILE 466 1078 1078 ILE ILE B . n 
B 1 467 LEU 467 1079 1079 LEU LEU B . n 
B 1 468 ARG 468 1080 1080 ARG ARG B . n 
B 1 469 ASN 469 1081 1081 ASN ASN B . n 
B 1 470 ALA 470 1082 1082 ALA ALA B . n 
B 1 471 LYS 471 1083 1083 LYS LYS B . n 
B 1 472 LEU 472 1084 1084 LEU LEU B . n 
B 1 473 LYS 473 1085 1085 LYS LYS B . n 
B 1 474 PRO 474 1086 1086 PRO PRO B . n 
B 1 475 VAL 475 1087 1087 VAL VAL B . n 
B 1 476 TYR 476 1088 1088 TYR TYR B . n 
B 1 477 ASP 477 1089 1089 ASP ASP B . n 
B 1 478 SER 478 1090 1090 SER SER B . n 
B 1 479 LEU 479 1091 1091 LEU LEU B . n 
B 1 480 ASP 480 1092 1092 ASP ASP B . n 
B 1 481 ALA 481 1093 1093 ALA ALA B . n 
B 1 482 VAL 482 1094 1094 VAL VAL B . n 
B 1 483 ARG 483 1095 1095 ARG ARG B . n 
B 1 484 ARG 484 1096 1096 ARG ARG B . n 
B 1 485 ALA 485 1097 1097 ALA ALA B . n 
B 1 486 ALA 486 1098 1098 ALA ALA B . n 
B 1 487 LEU 487 1099 1099 LEU LEU B . n 
B 1 488 ILE 488 1100 1100 ILE ILE B . n 
B 1 489 ASN 489 1101 1101 ASN ASN B . n 
B 1 490 MET 490 1102 1102 MET MET B . n 
B 1 491 VAL 491 1103 1103 VAL VAL B . n 
B 1 492 PHE 492 1104 1104 PHE PHE B . n 
B 1 493 GLN 493 1105 1105 GLN GLN B . n 
B 1 494 MET 494 1106 1106 MET MET B . n 
B 1 495 GLY 495 1107 1107 GLY GLY B . n 
B 1 496 GLU 496 1108 1108 GLU GLU B . n 
B 1 497 THR 497 1109 1109 THR THR B . n 
B 1 498 GLY 498 1110 1110 GLY GLY B . n 
B 1 499 VAL 499 1111 1111 VAL VAL B . n 
B 1 500 ALA 500 1112 1112 ALA ALA B . n 
B 1 501 GLY 501 1113 1113 GLY GLY B . n 
B 1 502 PHE 502 1114 1114 PHE PHE B . n 
B 1 503 THR 503 1115 1115 THR THR B . n 
B 1 504 ASN 504 1116 1116 ASN ASN B . n 
B 1 505 SER 505 1117 1117 SER SER B . n 
B 1 506 LEU 506 1118 1118 LEU LEU B . n 
B 1 507 ARG 507 1119 1119 ARG ARG B . n 
B 1 508 MET 508 1120 1120 MET MET B . n 
B 1 509 LEU 509 1121 1121 LEU LEU B . n 
B 1 510 GLN 510 1122 1122 GLN GLN B . n 
B 1 511 GLN 511 1123 1123 GLN GLN B . n 
B 1 512 LYS 512 1124 1124 LYS LYS B . n 
B 1 513 ARG 513 1125 1125 ARG ARG B . n 
B 1 514 TRP 514 1126 1126 TRP TRP B . n 
B 1 515 ASP 515 1127 1127 ASP ASP B . n 
B 1 516 GLU 516 1128 1128 GLU GLU B . n 
B 1 517 ALA 517 1129 1129 ALA ALA B . n 
B 1 518 ALA 518 1130 1130 ALA ALA B . n 
B 1 519 VAL 519 1131 1131 VAL VAL B . n 
B 1 520 ASN 520 1132 1132 ASN ASN B . n 
B 1 521 LEU 521 1133 1133 LEU LEU B . n 
B 1 522 ALA 522 1134 1134 ALA ALA B . n 
B 1 523 LYS 523 1135 1135 LYS LYS B . n 
B 1 524 SER 524 1136 1136 SER SER B . n 
B 1 525 ARG 525 1137 1137 ARG ARG B . n 
B 1 526 TRP 526 1138 1138 TRP TRP B . n 
B 1 527 TYR 527 1139 1139 TYR TYR B . n 
B 1 528 ASN 528 1140 1140 ASN ASN B . n 
B 1 529 GLN 529 1141 1141 GLN GLN B . n 
B 1 530 THR 530 1142 1142 THR THR B . n 
B 1 531 PRO 531 1143 1143 PRO PRO B . n 
B 1 532 ASN 532 1144 1144 ASN ASN B . n 
B 1 533 ARG 533 1145 1145 ARG ARG B . n 
B 1 534 ALA 534 1146 1146 ALA ALA B . n 
B 1 535 LYS 535 1147 1147 LYS LYS B . n 
B 1 536 ARG 536 1148 1148 ARG ARG B . n 
B 1 537 VAL 537 1149 1149 VAL VAL B . n 
B 1 538 ILE 538 1150 1150 ILE ILE B . n 
B 1 539 THR 539 1151 1151 THR THR B . n 
B 1 540 THR 540 1152 1152 THR THR B . n 
B 1 541 PHE 541 1153 1153 PHE PHE B . n 
B 1 542 ARG 542 1154 1154 ARG ARG B . n 
B 1 543 THR 543 1155 1155 THR THR B . n 
B 1 544 GLY 544 1156 1156 GLY GLY B . n 
B 1 545 THR 545 1157 1157 THR THR B . n 
B 1 546 TRP 546 1158 1158 TRP TRP B . n 
B 1 547 ASP 547 1159 1159 ASP ASP B . n 
B 1 548 ALA 548 1160 1160 ALA ALA B . n 
B 1 549 TYR 549 1161 1161 TYR TYR B . n 
C 2 1   GLN 1   1    ?    ?   ?   D . n 
C 2 2   VAL 2   2    2    VAL VAL D . n 
C 2 3   GLN 3   3    3    GLN GLN D . n 
C 2 4   LEU 4   4    4    LEU LEU D . n 
C 2 5   GLN 5   5    5    GLN GLN D . n 
C 2 6   GLU 6   6    6    GLU GLU D . n 
C 2 7   SER 7   7    7    SER SER D . n 
C 2 8   GLY 8   8    8    GLY GLY D . n 
C 2 9   GLY 9   9    9    GLY GLY D . n 
C 2 10  GLY 10  10   10   GLY GLY D . n 
C 2 11  LEU 11  11   11   LEU LEU D . n 
C 2 12  VAL 12  12   12   VAL VAL D . n 
C 2 13  GLN 13  13   13   GLN GLN D . n 
C 2 14  ALA 14  14   14   ALA ALA D . n 
C 2 15  GLY 15  15   15   GLY GLY D . n 
C 2 16  GLY 16  16   16   GLY GLY D . n 
C 2 17  SER 17  17   17   SER SER D . n 
C 2 18  LEU 18  18   18   LEU LEU D . n 
C 2 19  ARG 19  19   19   ARG ARG D . n 
C 2 20  LEU 20  20   20   LEU LEU D . n 
C 2 21  SER 21  21   21   SER SER D . n 
C 2 22  CYS 22  22   22   CYS CYS D . n 
C 2 23  ALA 23  23   23   ALA ALA D . n 
C 2 24  ALA 24  24   24   ALA ALA D . n 
C 2 25  SER 25  25   25   SER SER D . n 
C 2 26  GLY 26  26   26   GLY GLY D . n 
C 2 27  SER 27  27   27   SER SER D . n 
C 2 28  ILE 28  28   28   ILE ILE D . n 
C 2 29  PHE 29  29   29   PHE PHE D . n 
C 2 30  SER 30  30   30   SER SER D . n 
C 2 31  LEU 31  31   31   LEU LEU D . n 
C 2 32  ASN 32  32   32   ASN ASN D . n 
C 2 33  ASP 33  33   33   ASP ASP D . n 
C 2 34  MET 34  34   34   MET MET D . n 
C 2 35  GLY 35  35   35   GLY GLY D . n 
C 2 36  TRP 36  36   36   TRP TRP D . n 
C 2 37  TYR 37  37   37   TYR TYR D . n 
C 2 38  ARG 38  38   38   ARG ARG D . n 
C 2 39  GLN 39  39   39   GLN GLN D . n 
C 2 40  ALA 40  40   40   ALA ALA D . n 
C 2 41  PRO 41  41   41   PRO PRO D . n 
C 2 42  GLY 42  42   42   GLY GLY D . n 
C 2 43  LYS 43  43   43   LYS LYS D . n 
C 2 44  LEU 44  44   44   LEU LEU D . n 
C 2 45  ARG 45  45   45   ARG ARG D . n 
C 2 46  GLU 46  46   46   GLU GLU D . n 
C 2 47  LEU 47  47   47   LEU LEU D . n 
C 2 48  VAL 48  48   48   VAL VAL D . n 
C 2 49  ALA 49  49   49   ALA ALA D . n 
C 2 50  ALA 50  50   50   ALA ALA D . n 
C 2 51  ILE 51  51   51   ILE ILE D . n 
C 2 52  THR 52  52   52   THR THR D . n 
C 2 53  SER 53  53   53   SER SER D . n 
C 2 54  GLY 54  54   54   GLY GLY D . n 
C 2 55  GLY 55  55   55   GLY GLY D . n 
C 2 56  SER 56  56   56   SER SER D . n 
C 2 57  THR 57  57   57   THR THR D . n 
C 2 58  LYS 58  58   58   LYS LYS D . n 
C 2 59  TYR 59  59   59   TYR TYR D . n 
C 2 60  ALA 60  60   60   ALA ALA D . n 
C 2 61  ASP 61  61   61   ASP ASP D . n 
C 2 62  SER 62  62   62   SER SER D . n 
C 2 63  VAL 63  63   63   VAL VAL D . n 
C 2 64  LYS 64  64   64   LYS LYS D . n 
C 2 65  GLY 65  65   65   GLY GLY D . n 
C 2 66  ARG 66  66   66   ARG ARG D . n 
C 2 67  PHE 67  67   67   PHE PHE D . n 
C 2 68  THR 68  68   68   THR THR D . n 
C 2 69  ILE 69  69   69   ILE ILE D . n 
C 2 70  SER 70  70   70   SER SER D . n 
C 2 71  ARG 71  71   71   ARG ARG D . n 
C 2 72  ASP 72  72   72   ASP ASP D . n 
C 2 73  ASN 73  73   73   ASN ASN D . n 
C 2 74  ALA 74  74   74   ALA ALA D . n 
C 2 75  LYS 75  75   75   LYS LYS D . n 
C 2 76  ASN 76  76   76   ASN ASN D . n 
C 2 77  THR 77  77   77   THR THR D . n 
C 2 78  VAL 78  78   78   VAL VAL D . n 
C 2 79  TYR 79  79   79   TYR TYR D . n 
C 2 80  LEU 80  80   80   LEU LEU D . n 
C 2 81  GLN 81  81   81   GLN GLN D . n 
C 2 82  MET 82  82   82   MET MET D . n 
C 2 83  ASN 83  83   83   ASN ASN D . n 
C 2 84  SER 84  84   84   SER SER D . n 
C 2 85  LEU 85  85   85   LEU LEU D . n 
C 2 86  LYS 86  86   86   LYS LYS D . n 
C 2 87  ALA 87  87   87   ALA ALA D . n 
C 2 88  GLU 88  88   88   GLU GLU D . n 
C 2 89  ASP 89  89   89   ASP ASP D . n 
C 2 90  THR 90  90   90   THR THR D . n 
C 2 91  ALA 91  91   91   ALA ALA D . n 
C 2 92  VAL 92  92   92   VAL VAL D . n 
C 2 93  TYR 93  93   93   TYR TYR D . n 
C 2 94  TYR 94  94   94   TYR TYR D . n 
C 2 95  CYS 95  95   95   CYS CYS D . n 
C 2 96  ASN 96  96   96   ASN ASN D . n 
C 2 97  ALA 97  97   97   ALA ALA D . n 
C 2 98  LYS 98  98   98   LYS LYS D . n 
C 2 99  VAL 99  99   99   VAL VAL D . n 
C 2 100 ALA 100 100  100  ALA ALA D . n 
C 2 101 GLY 101 101  101  GLY GLY D . n 
C 2 102 THR 102 102  102  THR THR D . n 
C 2 103 PHE 103 103  103  PHE PHE D . n 
C 2 104 SER 104 104  104  SER SER D . n 
C 2 105 ILE 105 105  105  ILE ILE D . n 
C 2 106 TYR 106 106  106  TYR TYR D . n 
C 2 107 ASP 107 107  107  ASP ASP D . n 
C 2 108 TYR 108 108  108  TYR TYR D . n 
C 2 109 TRP 109 109  109  TRP TRP D . n 
C 2 110 GLY 110 110  110  GLY GLY D . n 
C 2 111 GLN 111 111  111  GLN GLN D . n 
C 2 112 GLY 112 112  112  GLY GLY D . n 
C 2 113 THR 113 113  113  THR THR D . n 
C 2 114 GLN 114 114  114  GLN GLN D . n 
C 2 115 VAL 115 115  115  VAL VAL D . n 
C 2 116 THR 116 116  116  THR THR D . n 
C 2 117 VAL 117 117  117  VAL VAL D . n 
C 2 118 SER 118 118  118  SER SER D . n 
C 2 119 SER 119 119  119  SER SER D . n 
C 2 120 HIS 120 120  120  HIS HIS D . n 
C 2 121 HIS 121 121  ?    ?   ?   D . n 
C 2 122 HIS 122 122  ?    ?   ?   D . n 
C 2 123 HIS 123 123  ?    ?   ?   D . n 
C 2 124 HIS 124 124  ?    ?   ?   D . n 
C 2 125 HIS 125 125  ?    ?   ?   D . n 
D 2 1   GLN 1   1    1    GLN GLN F . n 
D 2 2   VAL 2   2    2    VAL VAL F . n 
D 2 3   GLN 3   3    3    GLN GLN F . n 
D 2 4   LEU 4   4    4    LEU LEU F . n 
D 2 5   GLN 5   5    5    GLN GLN F . n 
D 2 6   GLU 6   6    6    GLU GLU F . n 
D 2 7   SER 7   7    7    SER SER F . n 
D 2 8   GLY 8   8    8    GLY GLY F . n 
D 2 9   GLY 9   9    9    GLY GLY F . n 
D 2 10  GLY 10  10   10   GLY GLY F . n 
D 2 11  LEU 11  11   11   LEU LEU F . n 
D 2 12  VAL 12  12   12   VAL VAL F . n 
D 2 13  GLN 13  13   13   GLN GLN F . n 
D 2 14  ALA 14  14   14   ALA ALA F . n 
D 2 15  GLY 15  15   15   GLY GLY F . n 
D 2 16  GLY 16  16   16   GLY GLY F . n 
D 2 17  SER 17  17   17   SER SER F . n 
D 2 18  LEU 18  18   18   LEU LEU F . n 
D 2 19  ARG 19  19   19   ARG ARG F . n 
D 2 20  LEU 20  20   20   LEU LEU F . n 
D 2 21  SER 21  21   21   SER SER F . n 
D 2 22  CYS 22  22   22   CYS CYS F . n 
D 2 23  ALA 23  23   23   ALA ALA F . n 
D 2 24  ALA 24  24   24   ALA ALA F . n 
D 2 25  SER 25  25   25   SER SER F . n 
D 2 26  GLY 26  26   26   GLY GLY F . n 
D 2 27  SER 27  27   27   SER SER F . n 
D 2 28  ILE 28  28   28   ILE ILE F . n 
D 2 29  PHE 29  29   29   PHE PHE F . n 
D 2 30  SER 30  30   30   SER SER F . n 
D 2 31  LEU 31  31   31   LEU LEU F . n 
D 2 32  ASN 32  32   32   ASN ASN F . n 
D 2 33  ASP 33  33   33   ASP ASP F . n 
D 2 34  MET 34  34   34   MET MET F . n 
D 2 35  GLY 35  35   35   GLY GLY F . n 
D 2 36  TRP 36  36   36   TRP TRP F . n 
D 2 37  TYR 37  37   37   TYR TYR F . n 
D 2 38  ARG 38  38   38   ARG ARG F . n 
D 2 39  GLN 39  39   39   GLN GLN F . n 
D 2 40  ALA 40  40   40   ALA ALA F . n 
D 2 41  PRO 41  41   41   PRO PRO F . n 
D 2 42  GLY 42  42   42   GLY GLY F . n 
D 2 43  LYS 43  43   43   LYS LYS F . n 
D 2 44  LEU 44  44   44   LEU LEU F . n 
D 2 45  ARG 45  45   45   ARG ARG F . n 
D 2 46  GLU 46  46   46   GLU GLU F . n 
D 2 47  LEU 47  47   47   LEU LEU F . n 
D 2 48  VAL 48  48   48   VAL VAL F . n 
D 2 49  ALA 49  49   49   ALA ALA F . n 
D 2 50  ALA 50  50   50   ALA ALA F . n 
D 2 51  ILE 51  51   51   ILE ILE F . n 
D 2 52  THR 52  52   52   THR THR F . n 
D 2 53  SER 53  53   53   SER SER F . n 
D 2 54  GLY 54  54   54   GLY GLY F . n 
D 2 55  GLY 55  55   55   GLY GLY F . n 
D 2 56  SER 56  56   56   SER SER F . n 
D 2 57  THR 57  57   57   THR THR F . n 
D 2 58  LYS 58  58   58   LYS LYS F . n 
D 2 59  TYR 59  59   59   TYR TYR F . n 
D 2 60  ALA 60  60   60   ALA ALA F . n 
D 2 61  ASP 61  61   61   ASP ASP F . n 
D 2 62  SER 62  62   62   SER SER F . n 
D 2 63  VAL 63  63   63   VAL VAL F . n 
D 2 64  LYS 64  64   64   LYS LYS F . n 
D 2 65  GLY 65  65   65   GLY GLY F . n 
D 2 66  ARG 66  66   66   ARG ARG F . n 
D 2 67  PHE 67  67   67   PHE PHE F . n 
D 2 68  THR 68  68   68   THR THR F . n 
D 2 69  ILE 69  69   69   ILE ILE F . n 
D 2 70  SER 70  70   70   SER SER F . n 
D 2 71  ARG 71  71   71   ARG ARG F . n 
D 2 72  ASP 72  72   72   ASP ASP F . n 
D 2 73  ASN 73  73   73   ASN ASN F . n 
D 2 74  ALA 74  74   74   ALA ALA F . n 
D 2 75  LYS 75  75   75   LYS LYS F . n 
D 2 76  ASN 76  76   76   ASN ASN F . n 
D 2 77  THR 77  77   77   THR THR F . n 
D 2 78  VAL 78  78   78   VAL VAL F . n 
D 2 79  TYR 79  79   79   TYR TYR F . n 
D 2 80  LEU 80  80   80   LEU LEU F . n 
D 2 81  GLN 81  81   81   GLN GLN F . n 
D 2 82  MET 82  82   82   MET MET F . n 
D 2 83  ASN 83  83   83   ASN ASN F . n 
D 2 84  SER 84  84   84   SER SER F . n 
D 2 85  LEU 85  85   85   LEU LEU F . n 
D 2 86  LYS 86  86   86   LYS LYS F . n 
D 2 87  ALA 87  87   87   ALA ALA F . n 
D 2 88  GLU 88  88   88   GLU GLU F . n 
D 2 89  ASP 89  89   89   ASP ASP F . n 
D 2 90  THR 90  90   90   THR THR F . n 
D 2 91  ALA 91  91   91   ALA ALA F . n 
D 2 92  VAL 92  92   92   VAL VAL F . n 
D 2 93  TYR 93  93   93   TYR TYR F . n 
D 2 94  TYR 94  94   94   TYR TYR F . n 
D 2 95  CYS 95  95   95   CYS CYS F . n 
D 2 96  ASN 96  96   96   ASN ASN F . n 
D 2 97  ALA 97  97   97   ALA ALA F . n 
D 2 98  LYS 98  98   98   LYS LYS F . n 
D 2 99  VAL 99  99   99   VAL VAL F . n 
D 2 100 ALA 100 100  100  ALA ALA F . n 
D 2 101 GLY 101 101  101  GLY GLY F . n 
D 2 102 THR 102 102  102  THR THR F . n 
D 2 103 PHE 103 103  103  PHE PHE F . n 
D 2 104 SER 104 104  104  SER SER F . n 
D 2 105 ILE 105 105  105  ILE ILE F . n 
D 2 106 TYR 106 106  106  TYR TYR F . n 
D 2 107 ASP 107 107  107  ASP ASP F . n 
D 2 108 TYR 108 108  108  TYR TYR F . n 
D 2 109 TRP 109 109  109  TRP TRP F . n 
D 2 110 GLY 110 110  110  GLY GLY F . n 
D 2 111 GLN 111 111  111  GLN GLN F . n 
D 2 112 GLY 112 112  112  GLY GLY F . n 
D 2 113 THR 113 113  113  THR THR F . n 
D 2 114 GLN 114 114  114  GLN GLN F . n 
D 2 115 VAL 115 115  115  VAL VAL F . n 
D 2 116 THR 116 116  116  THR THR F . n 
D 2 117 VAL 117 117  117  VAL VAL F . n 
D 2 118 SER 118 118  118  SER SER F . n 
D 2 119 SER 119 119  119  SER SER F . n 
D 2 120 HIS 120 120  ?    ?   ?   F . n 
D 2 121 HIS 121 121  ?    ?   ?   F . n 
D 2 122 HIS 122 122  ?    ?   ?   F . n 
D 2 123 HIS 123 123  ?    ?   ?   F . n 
D 2 124 HIS 124 124  ?    ?   ?   F . n 
D 2 125 HIS 125 125  ?    ?   ?   F . 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 
E 3 A1AE2 1 1201 1 A1AE2 DRG A . 
F 3 A1AE2 1 1201 2 A1AE2 DRG B . 
G 4 AV0   1 1202 1 AV0   LIG B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A ASP 29   ? CG  ? A ASP 53  CG  
2  1 Y 1 A ASP 29   ? OD1 ? A ASP 53  OD1 
3  1 Y 1 A ASP 29   ? OD2 ? A ASP 53  OD2 
4  1 Y 1 A GLN 299  ? CG  ? A GLN 323 CG  
5  1 Y 1 A GLN 299  ? CD  ? A GLN 323 CD  
6  1 Y 1 A GLN 299  ? OE1 ? A GLN 323 OE1 
7  1 Y 1 A GLN 299  ? NE2 ? A GLN 323 NE2 
8  1 Y 1 A ASP 300  ? CG  ? A ASP 324 CG  
9  1 Y 1 A ASP 300  ? OD1 ? A ASP 324 OD1 
10 1 Y 1 A ASP 300  ? OD2 ? A ASP 324 OD2 
11 1 Y 1 A GLN 1122 ? CG  ? A GLN 510 CG  
12 1 Y 1 A GLN 1122 ? CD  ? A GLN 510 CD  
13 1 Y 1 A GLN 1122 ? OE1 ? A GLN 510 OE1 
14 1 Y 1 A GLN 1122 ? NE2 ? A GLN 510 NE2 
15 1 Y 1 A GLN 1123 ? CG  ? A GLN 511 CG  
16 1 Y 1 A GLN 1123 ? CD  ? A GLN 511 CD  
17 1 Y 1 A GLN 1123 ? OE1 ? A GLN 511 OE1 
18 1 Y 1 A GLN 1123 ? NE2 ? A GLN 511 NE2 
19 1 Y 1 A ARG 1125 ? CG  ? A ARG 513 CG  
20 1 Y 1 A ARG 1125 ? CD  ? A ARG 513 CD  
21 1 Y 1 A ARG 1125 ? NE  ? A ARG 513 NE  
22 1 Y 1 A ARG 1125 ? CZ  ? A ARG 513 CZ  
23 1 Y 1 A ARG 1125 ? NH1 ? A ARG 513 NH1 
24 1 Y 1 A ARG 1125 ? NH2 ? A ARG 513 NH2 
25 1 Y 1 B ILE 1027 ? CG1 ? B ILE 415 CG1 
26 1 Y 1 B ILE 1027 ? CG2 ? B ILE 415 CG2 
27 1 Y 1 B ILE 1027 ? CD1 ? B ILE 415 CD1 
28 1 Y 1 B LEU 1032 ? CG  ? B LEU 420 CG  
29 1 Y 1 B LEU 1032 ? CD1 ? B LEU 420 CD1 
30 1 Y 1 B LEU 1032 ? CD2 ? B LEU 420 CD2 
31 1 Y 1 B ARG 1080 ? CG  ? B ARG 468 CG  
32 1 Y 1 B ARG 1080 ? CD  ? B ARG 468 CD  
33 1 Y 1 B ARG 1080 ? NE  ? B ARG 468 NE  
34 1 Y 1 B ARG 1080 ? CZ  ? B ARG 468 CZ  
35 1 Y 1 B ARG 1080 ? NH1 ? B ARG 468 NH1 
36 1 Y 1 B ARG 1080 ? NH2 ? B ARG 468 NH2 
37 1 Y 1 D GLN 13   ? CG  ? C GLN 13  CG  
38 1 Y 1 D GLN 13   ? CD  ? C GLN 13  CD  
39 1 Y 1 D GLN 13   ? OE1 ? C GLN 13  OE1 
40 1 Y 1 D GLN 13   ? NE2 ? C GLN 13  NE2 
41 1 Y 1 D LYS 43   ? CG  ? C LYS 43  CG  
42 1 Y 1 D LYS 43   ? CD  ? C LYS 43  CD  
43 1 Y 1 D LYS 43   ? CE  ? C LYS 43  CE  
44 1 Y 1 D LYS 43   ? NZ  ? C LYS 43  NZ  
45 1 Y 1 D LYS 58   ? CG  ? C LYS 58  CG  
46 1 Y 1 D LYS 58   ? CD  ? C LYS 58  CD  
47 1 Y 1 D LYS 58   ? CE  ? C LYS 58  CE  
48 1 Y 1 D LYS 58   ? NZ  ? C LYS 58  NZ  
49 1 Y 1 D LYS 64   ? CG  ? C LYS 64  CG  
50 1 Y 1 D LYS 64   ? CD  ? C LYS 64  CD  
51 1 Y 1 D LYS 64   ? CE  ? C LYS 64  CE  
52 1 Y 1 D LYS 64   ? NZ  ? C LYS 64  NZ  
53 1 Y 1 D LYS 75   ? CG  ? C LYS 75  CG  
54 1 Y 1 D LYS 75   ? CD  ? C LYS 75  CD  
55 1 Y 1 D LYS 75   ? CE  ? C LYS 75  CE  
56 1 Y 1 D LYS 75   ? NZ  ? C LYS 75  NZ  
57 1 Y 1 F GLN 1    ? CG  ? D GLN 1   CG  
58 1 Y 1 F GLN 1    ? CD  ? D GLN 1   CD  
59 1 Y 1 F GLN 1    ? OE1 ? D GLN 1   OE1 
60 1 Y 1 F GLN 1    ? NE2 ? D GLN 1   NE2 
61 1 Y 1 F GLN 3    ? CG  ? D GLN 3   CG  
62 1 Y 1 F GLN 3    ? CD  ? D GLN 3   CD  
63 1 Y 1 F GLN 3    ? OE1 ? D GLN 3   OE1 
64 1 Y 1 F GLN 3    ? NE2 ? D GLN 3   NE2 
65 1 Y 1 F GLN 5    ? CG  ? D GLN 5   CG  
66 1 Y 1 F GLN 5    ? CD  ? D GLN 5   CD  
67 1 Y 1 F GLN 5    ? OE1 ? D GLN 5   OE1 
68 1 Y 1 F GLN 5    ? NE2 ? D GLN 5   NE2 
69 1 Y 1 F GLN 13   ? CG  ? D GLN 13  CG  
70 1 Y 1 F GLN 13   ? CD  ? D GLN 13  CD  
71 1 Y 1 F GLN 13   ? OE1 ? D GLN 13  OE1 
72 1 Y 1 F GLN 13   ? NE2 ? D GLN 13  NE2 
73 1 Y 1 F LYS 58   ? CG  ? D LYS 58  CG  
74 1 Y 1 F LYS 58   ? CD  ? D LYS 58  CD  
75 1 Y 1 F LYS 58   ? CE  ? D LYS 58  CE  
76 1 Y 1 F LYS 58   ? NZ  ? D LYS 58  NZ  
77 1 Y 1 F LYS 64   ? CG  ? D LYS 64  CG  
78 1 Y 1 F LYS 64   ? CD  ? D LYS 64  CD  
79 1 Y 1 F LYS 64   ? CE  ? D LYS 64  CE  
80 1 Y 1 F LYS 64   ? NZ  ? D LYS 64  NZ  
81 1 Y 1 F LYS 75   ? CG  ? D LYS 75  CG  
82 1 Y 1 F LYS 75   ? CD  ? D LYS 75  CD  
83 1 Y 1 F LYS 75   ? CE  ? D LYS 75  CE  
84 1 Y 1 F LYS 75   ? NZ  ? D LYS 75  NZ  
85 1 Y 1 F GLN 111  ? CG  ? D GLN 111 CG  
86 1 Y 1 F GLN 111  ? CD  ? D GLN 111 CD  
87 1 Y 1 F GLN 111  ? OE1 ? D GLN 111 OE1 
88 1 Y 1 F GLN 111  ? NE2 ? D GLN 111 NE2 
# 
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       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.20.1_4487 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   107.060 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8W1V 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     73.680 
_cell.length_a_esd                 ? 
_cell.length_b                     146.770 
_cell.length_b_esd                 ? 
_cell.length_c                     91.830 
_cell.length_c_esd                 ? 
_cell.volume                       949354.705 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8W1V 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            'P 2yb' 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_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                   8W1V 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             3.29 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          62.57 
_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.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'LIPIDIC CUBIC PHASE' 
_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_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '100 mM Tris buffer (pH 8.0), 100 to 175 mM lithium sulfate, 38% to 42% PEG400, and 10 mM EDTA' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     80 
_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.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2020-07-15 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_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   1.000 
_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                        'SPRING-8 BEAMLINE BL32XU' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.000 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL32XU 
_diffrn_source.pdbx_synchrotron_site       SPring-8 
# 
_reflns.B_iso_Wilson_estimate                          54.78 
_reflns.entry_id                                       8W1V 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.92 
_reflns.d_resolution_low                               48.44 
_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                                     40547 
_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                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                55.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.25 
_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                                   0.984 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    3.0 
_reflns_shell.d_res_low                                     3.1 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             6655 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.564 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               60.43 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_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                                 8W1V 
_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                            3.00 
_refine.ls_d_res_low                             48.44 
_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                     37359 
_refine.ls_number_reflns_R_free                  2068 
_refine.ls_number_reflns_R_work                  35291 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.90 
_refine.ls_percent_reflns_R_free                 5.54 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2501 
_refine.ls_R_factor_R_free                       0.2919 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2477 
_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                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_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                          1.36 
_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               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_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                 31.5555 
_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                             ? 
_refine.overall_SU_ML                            0.4897 
_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                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       3.00 
_refine_hist.d_res_low                        48.44 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               8913 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        8760 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         153 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
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' ? 0.0071  ? 9106  ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.7050  ? 12348 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0434  ? 1429  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0043  ? 1509  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 14.8786 ? 3188  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_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_error 
_refine_ls_shell.R_factor_R_work 
_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_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 3.00 3.07  . . 133 2351 99.72  . . . . 0.3606 . . . . . . . . . . . 0.4421 
'X-RAY DIFFRACTION' 3.07 3.15  . . 134 2345 99.84  . . . . 0.3270 . . . . . . . . . . . 0.3752 
'X-RAY DIFFRACTION' 3.15 3.23  . . 137 2347 99.84  . . . . 0.3110 . . . . . . . . . . . 0.3531 
'X-RAY DIFFRACTION' 3.23 3.33  . . 135 2356 99.92  . . . . 0.2777 . . . . . . . . . . . 0.3299 
'X-RAY DIFFRACTION' 3.33 3.43  . . 140 2337 100.00 . . . . 0.2665 . . . . . . . . . . . 0.3057 
'X-RAY DIFFRACTION' 3.43 3.56  . . 139 2329 99.88  . . . . 0.2582 . . . . . . . . . . . 0.2889 
'X-RAY DIFFRACTION' 3.56 3.70  . . 137 2369 100.00 . . . . 0.2427 . . . . . . . . . . . 0.3100 
'X-RAY DIFFRACTION' 3.70 3.87  . . 145 2330 100.00 . . . . 0.2332 . . . . . . . . . . . 0.2870 
'X-RAY DIFFRACTION' 3.87 4.07  . . 128 2350 100.00 . . . . 0.2224 . . . . . . . . . . . 0.2359 
'X-RAY DIFFRACTION' 4.07 4.33  . . 142 2374 100.00 . . . . 0.2121 . . . . . . . . . . . 0.2586 
'X-RAY DIFFRACTION' 4.33 4.66  . . 138 2330 100.00 . . . . 0.2201 . . . . . . . . . . . 0.2833 
'X-RAY DIFFRACTION' 4.66 5.13  . . 142 2355 99.84  . . . . 0.2324 . . . . . . . . . . . 0.2731 
'X-RAY DIFFRACTION' 5.13 5.87  . . 140 2358 99.96  . . . . 0.2665 . . . . . . . . . . . 0.3246 
'X-RAY DIFFRACTION' 5.87 7.39  . . 136 2377 100.00 . . . . 0.2668 . . . . . . . . . . . 0.2785 
'X-RAY DIFFRACTION' 7.39 48.44 . . 142 2383 99.49  . . . . 0.2162 . . . . . . . . . . . 0.2513 
# 
_struct.entry_id                     8W1V 
_struct.title                        'The beta2 adrenergic receptor bound to a bitopic ligand' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        8W1V 
_struct_keywords.text            'signal transduction, bitopic ligand, , SIGNALING PROTEIN, GPCR, MEMBRANE PROTEIN' 
_struct_keywords.pdbx_keywords   'MEMBRANE PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
G N N 4 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP ADRB2_HUMAN P07550 ? 1 
;MGQPGNGSAFLLAPNGSHAPDHDVTQERDEVWVVGMGIVMSLIVLAIVFGNVLVITAIAKFERLQTVTNYFITSLACADL
VMGLAVVPFGAAHILMKMWTFGNFWCEFWTSIDVLCVTASIETLCVIAVDRYFAITSPFKYQSLLTKNKARVIILMVWIV
SGLTSFLPIQMHWYRATHQEAINCYANETCCDFFTNQAYAIASSIVSFYVPLVIMVFVYSRVFQEAKRQLQKIDKSEGRF
HVQNLSQVEQDGRTGHGLRRSSKFCLKEHKALKTLGIIMGTFTLCWLPFFIVNIVHVIQDNLIRKEVYILLNWIGYVNSG
FNPLIYCRSPDFRIAFQELLCLRRSSLKAYGNGYSSNGNTGEQSG
;
1 
2 UNP ENLYS_BPT4  P00720 ? 1 
;NIFEMLRIDERLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNCNGVITKDEAEKLFNQDVDAAVRGILRN
AKLKPVYDSLDAVRRCALINMVFQMGETGVAGFTNSLRMLQQKRWDEAAVNLAKSIWYNQTPNRAKRVITTFRTGTWDAY

;
2 
3 PDB 8W1V        8W1V   ? 2 ? 1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8W1V A 25  ? 389 ? P07550 1 ? 365 ? 1    1001 
2 2 8W1V A 390 ? 549 ? P00720 2 ? 161 ? 1002 1161 
3 1 8W1V B 25  ? 389 ? P07550 1 ? 365 ? 1    1001 
4 2 8W1V B 390 ? 549 ? P00720 2 ? 161 ? 1002 1161 
5 3 8W1V D 1   ? 125 ? 8W1V   1 ? 125 ? 1    125  
6 3 8W1V F 1   ? 125 ? 8W1V   1 ? 125 ? 1    125  
# 
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 8W1V MET A 1   ? UNP P07550 ?   ?   'initiating methionine' -23  1  
1 8W1V LYS A 2   ? UNP P07550 ?   ?   'expression tag'        -22  2  
1 8W1V THR A 3   ? UNP P07550 ?   ?   'expression tag'        -21  3  
1 8W1V ILE A 4   ? UNP P07550 ?   ?   'expression tag'        -20  4  
1 8W1V ILE A 5   ? UNP P07550 ?   ?   'expression tag'        -19  5  
1 8W1V ALA A 6   ? UNP P07550 ?   ?   'expression tag'        -18  6  
1 8W1V LEU A 7   ? UNP P07550 ?   ?   'expression tag'        -17  7  
1 8W1V SER A 8   ? UNP P07550 ?   ?   'expression tag'        -16  8  
1 8W1V TYR A 9   ? UNP P07550 ?   ?   'expression tag'        -15  9  
1 8W1V ILE A 10  ? UNP P07550 ?   ?   'expression tag'        -14  10 
1 8W1V PHE A 11  ? UNP P07550 ?   ?   'expression tag'        -13  11 
1 8W1V CYS A 12  ? UNP P07550 ?   ?   'expression tag'        -12  12 
1 8W1V LEU A 13  ? UNP P07550 ?   ?   'expression tag'        -11  13 
1 8W1V VAL A 14  ? UNP P07550 ?   ?   'expression tag'        -10  14 
1 8W1V PHE A 15  ? UNP P07550 ?   ?   'expression tag'        -9   15 
1 8W1V ALA A 16  ? UNP P07550 ?   ?   'expression tag'        -8   16 
1 8W1V ASP A 17  ? UNP P07550 ?   ?   'expression tag'        -7   17 
1 8W1V TYR A 18  ? UNP P07550 ?   ?   'expression tag'        -6   18 
1 8W1V LYS A 19  ? UNP P07550 ?   ?   'expression tag'        -5   19 
1 8W1V ASP A 20  ? UNP P07550 ?   ?   'expression tag'        -4   20 
1 8W1V ASP A 21  ? UNP P07550 ?   ?   'expression tag'        -3   21 
1 8W1V ASP A 22  ? UNP P07550 ?   ?   'expression tag'        -2   22 
1 8W1V ASP A 23  ? UNP P07550 ?   ?   'expression tag'        -1   23 
1 8W1V ALA A 24  ? UNP P07550 ?   ?   'expression tag'        0    24 
1 8W1V ARG A 40  ? UNP P07550 GLY 16  conflict                16   25 
1 8W1V GLN A 51  ? UNP P07550 GLU 27  conflict                27   26 
1 8W1V GLU A 211 ? UNP P07550 ASN 187 'engineered mutation'   187  27 
1 8W1V TYR A 255 ? UNP P07550 GLN 231 conflict                231  28 
2 8W1V GLY A 400 ? UNP P00720 ARG 12  conflict                1012 29 
2 8W1V THR A 442 ? UNP P00720 CYS 54  'engineered mutation'   1054 30 
2 8W1V ALA A 485 ? UNP P00720 CYS 97  'engineered mutation'   1097 31 
2 8W1V ARG A 525 ? UNP P00720 ILE 137 conflict                1137 32 
3 8W1V MET B 1   ? UNP P07550 ?   ?   'initiating methionine' -23  33 
3 8W1V LYS B 2   ? UNP P07550 ?   ?   'expression tag'        -22  34 
3 8W1V THR B 3   ? UNP P07550 ?   ?   'expression tag'        -21  35 
3 8W1V ILE B 4   ? UNP P07550 ?   ?   'expression tag'        -20  36 
3 8W1V ILE B 5   ? UNP P07550 ?   ?   'expression tag'        -19  37 
3 8W1V ALA B 6   ? UNP P07550 ?   ?   'expression tag'        -18  38 
3 8W1V LEU B 7   ? UNP P07550 ?   ?   'expression tag'        -17  39 
3 8W1V SER B 8   ? UNP P07550 ?   ?   'expression tag'        -16  40 
3 8W1V TYR B 9   ? UNP P07550 ?   ?   'expression tag'        -15  41 
3 8W1V ILE B 10  ? UNP P07550 ?   ?   'expression tag'        -14  42 
3 8W1V PHE B 11  ? UNP P07550 ?   ?   'expression tag'        -13  43 
3 8W1V CYS B 12  ? UNP P07550 ?   ?   'expression tag'        -12  44 
3 8W1V LEU B 13  ? UNP P07550 ?   ?   'expression tag'        -11  45 
3 8W1V VAL B 14  ? UNP P07550 ?   ?   'expression tag'        -10  46 
3 8W1V PHE B 15  ? UNP P07550 ?   ?   'expression tag'        -9   47 
3 8W1V ALA B 16  ? UNP P07550 ?   ?   'expression tag'        -8   48 
3 8W1V ASP B 17  ? UNP P07550 ?   ?   'expression tag'        -7   49 
3 8W1V TYR B 18  ? UNP P07550 ?   ?   'expression tag'        -6   50 
3 8W1V LYS B 19  ? UNP P07550 ?   ?   'expression tag'        -5   51 
3 8W1V ASP B 20  ? UNP P07550 ?   ?   'expression tag'        -4   52 
3 8W1V ASP B 21  ? UNP P07550 ?   ?   'expression tag'        -3   53 
3 8W1V ASP B 22  ? UNP P07550 ?   ?   'expression tag'        -2   54 
3 8W1V ASP B 23  ? UNP P07550 ?   ?   'expression tag'        -1   55 
3 8W1V ALA B 24  ? UNP P07550 ?   ?   'expression tag'        0    56 
3 8W1V ARG B 40  ? UNP P07550 GLY 16  conflict                16   57 
3 8W1V GLN B 51  ? UNP P07550 GLU 27  conflict                27   58 
3 8W1V GLU B 211 ? UNP P07550 ASN 187 'engineered mutation'   187  59 
3 8W1V TYR B 255 ? UNP P07550 GLN 231 conflict                231  60 
4 8W1V GLY B 400 ? UNP P00720 ARG 12  conflict                1012 61 
4 8W1V THR B 442 ? UNP P00720 CYS 54  'engineered mutation'   1054 62 
4 8W1V ALA B 485 ? UNP P00720 CYS 97  'engineered mutation'   1097 63 
4 8W1V ARG B 525 ? UNP P00720 ILE 137 conflict                1137 64 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
_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 
# 
_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_
_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 GLU A 54  ? PHE A 85  ? GLU A 30   PHE A 61   1 ? 32 
HELX_P HELX_P2  AA2 GLU A 86  ? GLN A 89  ? GLU A 62   GLN A 65   5 ? 4  
HELX_P HELX_P3  AA3 THR A 90  ? VAL A 110 ? THR A 66   VAL A 86   1 ? 21 
HELX_P HELX_P4  AA4 VAL A 110 ? LYS A 121 ? VAL A 86   LYS A 97   1 ? 12 
HELX_P HELX_P5  AA5 PHE A 125 ? ILE A 159 ? PHE A 101  ILE A 135  1 ? 35 
HELX_P HELX_P6  AA6 THR A 170 ? THR A 188 ? THR A 146  THR A 164  1 ? 19 
HELX_P HELX_P7  AA7 SER A 189 ? MET A 195 ? SER A 165  MET A 171  1 ? 7  
HELX_P HELX_P8  AA8 HIS A 202 ? GLU A 211 ? HIS A 178  GLU A 187  1 ? 10 
HELX_P HELX_P9  AA9 ASN A 220 ? PHE A 232 ? ASN A 196  PHE A 208  1 ? 13 
HELX_P HELX_P10 AB1 PHE A 232 ? GLN A 253 ? PHE A 208  GLN A 229  1 ? 22 
HELX_P HELX_P11 AB2 LEU A 290 ? GLN A 323 ? LEU A 266  GLN A 299  1 ? 34 
HELX_P HELX_P12 AB3 ARG A 328 ? ASN A 342 ? ARG A 304  ASN A 318  1 ? 15 
HELX_P HELX_P13 AB4 PHE A 345 ? TYR A 350 ? PHE A 321  TYR A 326  1 ? 6  
HELX_P HELX_P14 AB5 SER A 353 ? LEU A 364 ? SER A 329  LEU A 340  1 ? 12 
HELX_P HELX_P15 AB6 PHE A 392 ? GLY A 400 ? PHE A 1004 GLY A 1012 1 ? 9  
HELX_P HELX_P16 AB7 SER A 426 ? GLY A 439 ? SER A 1038 GLY A 1051 1 ? 14 
HELX_P HELX_P17 AB8 THR A 447 ? ARG A 468 ? THR A 1059 ARG A 1080 1 ? 22 
HELX_P HELX_P18 AB9 ASN A 469 ? LEU A 472 ? ASN A 1081 LEU A 1084 5 ? 4  
HELX_P HELX_P19 AC1 LYS A 473 ? LEU A 479 ? LYS A 1085 LEU A 1091 1 ? 7  
HELX_P HELX_P20 AC2 ASP A 480 ? VAL A 499 ? ASP A 1092 VAL A 1111 1 ? 20 
HELX_P HELX_P21 AC3 PHE A 502 ? GLN A 511 ? PHE A 1114 GLN A 1123 1 ? 10 
HELX_P HELX_P22 AC4 ARG A 513 ? LEU A 521 ? ARG A 1125 LEU A 1133 1 ? 9  
HELX_P HELX_P23 AC5 SER A 524 ? THR A 530 ? SER A 1136 THR A 1142 1 ? 7  
HELX_P HELX_P24 AC6 THR A 530 ? THR A 543 ? THR A 1142 THR A 1155 1 ? 14 
HELX_P HELX_P25 AC7 GLU B 54  ? PHE B 85  ? GLU B 30   PHE B 61   1 ? 32 
HELX_P HELX_P26 AC8 GLU B 86  ? GLN B 89  ? GLU B 62   GLN B 65   5 ? 4  
HELX_P HELX_P27 AC9 THR B 90  ? VAL B 110 ? THR B 66   VAL B 86   1 ? 21 
HELX_P HELX_P28 AD1 VAL B 110 ? MET B 120 ? VAL B 86   MET B 96   1 ? 11 
HELX_P HELX_P29 AD2 PHE B 125 ? THR B 160 ? PHE B 101  THR B 136  1 ? 36 
HELX_P HELX_P30 AD3 THR B 170 ? MET B 195 ? THR B 146  MET B 171  1 ? 26 
HELX_P HELX_P31 AD4 HIS B 202 ? GLU B 211 ? HIS B 178  GLU B 187  1 ? 10 
HELX_P HELX_P32 AD5 ASN B 220 ? SER B 231 ? ASN B 196  SER B 207  1 ? 12 
HELX_P HELX_P33 AD6 PHE B 232 ? GLN B 253 ? PHE B 208  GLN B 229  1 ? 22 
HELX_P HELX_P34 AD7 LEU B 290 ? GLN B 323 ? LEU B 266  GLN B 299  1 ? 34 
HELX_P HELX_P35 AD8 ARG B 328 ? ASN B 342 ? ARG B 304  ASN B 318  1 ? 15 
HELX_P HELX_P36 AD9 GLY B 344 ? TYR B 350 ? GLY B 320  TYR B 326  1 ? 7  
HELX_P HELX_P37 AE1 SER B 353 ? LEU B 364 ? SER B 329  LEU B 340  1 ? 12 
HELX_P HELX_P38 AE2 ILE B 391 ? GLY B 400 ? ILE B 1003 GLY B 1012 1 ? 10 
HELX_P HELX_P39 AE3 SER B 426 ? GLY B 439 ? SER B 1038 GLY B 1051 1 ? 14 
HELX_P HELX_P40 AE4 THR B 447 ? ARG B 468 ? THR B 1059 ARG B 1080 1 ? 22 
HELX_P HELX_P41 AE5 LEU B 472 ? LEU B 479 ? LEU B 1084 LEU B 1091 1 ? 8  
HELX_P HELX_P42 AE6 ASP B 480 ? GLY B 495 ? ASP B 1092 GLY B 1107 1 ? 16 
HELX_P HELX_P43 AE7 GLY B 495 ? ALA B 500 ? GLY B 1107 ALA B 1112 1 ? 6  
HELX_P HELX_P44 AE8 PHE B 502 ? GLN B 511 ? PHE B 1114 GLN B 1123 1 ? 10 
HELX_P HELX_P45 AE9 ARG B 513 ? ALA B 522 ? ARG B 1125 ALA B 1134 1 ? 10 
HELX_P HELX_P46 AF1 ARG B 525 ? THR B 530 ? ARG B 1137 THR B 1142 1 ? 6  
HELX_P HELX_P47 AF2 THR B 530 ? GLY B 544 ? THR B 1142 GLY B 1156 1 ? 15 
HELX_P HELX_P48 AF3 ILE C 28  ? ASN C 32  ? ILE D 28   ASN D 32   5 ? 5  
HELX_P HELX_P49 AF4 ASP C 61  ? LYS C 64  ? ASP D 61   LYS D 64   5 ? 4  
HELX_P HELX_P50 AF5 LYS C 86  ? THR C 90  ? LYS D 86   THR D 90   5 ? 5  
HELX_P HELX_P51 AF6 ILE D 28  ? ASN D 32  ? ILE F 28   ASN F 32   5 ? 5  
HELX_P HELX_P52 AF7 ASP D 61  ? LYS D 64  ? ASP F 61   LYS F 64   5 ? 4  
HELX_P HELX_P53 AF8 LYS D 86  ? THR D 90  ? LYS F 86   THR F 90   5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ? ? A CYS 130 SG ? ? ? 1_555 A CYS 215 SG ? ? A CYS 106 A CYS 191 1_555 ? ? ? ? ? ? ? 2.025 ? ? 
disulf2 disulf ? ? A CYS 208 SG ? ? ? 1_555 A CYS 214 SG ? ? A CYS 184 A CYS 190 1_555 ? ? ? ? ? ? ? 2.036 ? ? 
disulf3 disulf ? ? B CYS 130 SG ? ? ? 1_555 B CYS 215 SG ? ? B CYS 106 B CYS 191 1_555 ? ? ? ? ? ? ? 2.026 ? ? 
disulf4 disulf ? ? B CYS 208 SG ? ? ? 1_555 B CYS 214 SG ? ? B CYS 184 B CYS 190 1_555 ? ? ? ? ? ? ? 2.034 ? ? 
disulf5 disulf ? ? C CYS 22  SG ? ? ? 1_555 C CYS 95  SG ? ? D CYS 22  D CYS 95  1_555 ? ? ? ? ? ? ? 2.033 ? ? 
disulf6 disulf ? ? D CYS 22  SG ? ? ? 1_555 D CYS 95  SG ? ? F CYS 22  F CYS 95  1_555 ? ? ? ? ? ? ? 2.035 ? ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 6 ? 
AA5 ? 4 ? 
AA6 ? 4 ? 
AA7 ? 6 ? 
AA8 ? 4 ? 
# 
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 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA7 1 2 ? parallel      
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA7 4 5 ? anti-parallel 
AA7 5 6 ? anti-parallel 
AA8 1 2 ? parallel      
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ARG A 402 ? LYS A 407 ? ARG A 1014 LYS A 1019 
AA1 2 TYR A 413 ? GLY A 416 ? TYR A 1025 GLY A 1028 
AA1 3 HIS A 419 ? THR A 422 ? HIS A 1031 THR A 1034 
AA2 1 TYR B 406 ? LYS B 407 ? TYR B 1018 LYS B 1019 
AA2 2 TYR B 413 ? ILE B 415 ? TYR B 1025 ILE B 1027 
AA2 3 HIS B 419 ? LEU B 420 ? HIS B 1031 LEU B 1032 
AA3 1 GLN C 3   ? SER C 7   ? GLN D 3    SER D 7    
AA3 2 SER C 17  ? SER C 25  ? SER D 17   SER D 25   
AA3 3 THR C 77  ? ASN C 83  ? THR D 77   ASN D 83   
AA3 4 PHE C 67  ? ASP C 72  ? PHE D 67   ASP D 72   
AA4 1 LEU C 11  ? GLN C 13  ? LEU D 11   GLN D 13   
AA4 2 THR C 113 ? SER C 118 ? THR D 113  SER D 118  
AA4 3 ALA C 91  ? ALA C 100 ? ALA D 91   ALA D 100  
AA4 4 ASP C 33  ? GLN C 39  ? ASP D 33   GLN D 39   
AA4 5 GLU C 46  ? ILE C 51  ? GLU D 46   ILE D 51   
AA4 6 THR C 57  ? TYR C 59  ? THR D 57   TYR D 59   
AA5 1 LEU C 11  ? GLN C 13  ? LEU D 11   GLN D 13   
AA5 2 THR C 113 ? SER C 118 ? THR D 113  SER D 118  
AA5 3 ALA C 91  ? ALA C 100 ? ALA D 91   ALA D 100  
AA5 4 ILE C 105 ? TRP C 109 ? ILE D 105  TRP D 109  
AA6 1 GLN D 3   ? SER D 7   ? GLN F 3    SER F 7    
AA6 2 LEU D 18  ? SER D 25  ? LEU F 18   SER F 25   
AA6 3 THR D 77  ? MET D 82  ? THR F 77   MET F 82   
AA6 4 PHE D 67  ? ASP D 72  ? PHE F 67   ASP F 72   
AA7 1 GLY D 10  ? GLN D 13  ? GLY F 10   GLN F 13   
AA7 2 THR D 113 ? SER D 118 ? THR F 113  SER F 118  
AA7 3 ALA D 91  ? ALA D 100 ? ALA F 91   ALA F 100  
AA7 4 ASP D 33  ? GLN D 39  ? ASP F 33   GLN F 39   
AA7 5 GLU D 46  ? ILE D 51  ? GLU F 46   ILE F 51   
AA7 6 THR D 57  ? TYR D 59  ? THR F 57   TYR F 59   
AA8 1 GLY D 10  ? GLN D 13  ? GLY F 10   GLN F 13   
AA8 2 THR D 113 ? SER D 118 ? THR F 113  SER F 118  
AA8 3 ALA D 91  ? ALA D 100 ? ALA F 91   ALA F 100  
AA8 4 ILE D 105 ? TRP D 109 ? ILE F 105  TRP F 109  
# 
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 TYR A 406 ? N TYR A 1018 O THR A 414 ? O THR A 1026 
AA1 2 3 N TYR A 413 ? N TYR A 1025 O LEU A 421 ? O LEU A 1033 
AA2 1 2 N TYR B 406 ? N TYR B 1018 O THR B 414 ? O THR B 1026 
AA2 2 3 N ILE B 415 ? N ILE B 1027 O HIS B 419 ? O HIS B 1031 
AA3 1 2 N SER C 7   ? N SER D 7    O SER C 21  ? O SER D 21   
AA3 2 3 N LEU C 18  ? N LEU D 18   O MET C 82  ? O MET D 82   
AA3 3 4 O TYR C 79  ? O TYR D 79   N SER C 70  ? N SER D 70   
AA4 1 2 N VAL C 12  ? N VAL D 12   O SER C 118 ? O SER D 118  
AA4 2 3 O THR C 113 ? O THR D 113  N TYR C 93  ? N TYR D 93   
AA4 3 4 O TYR C 94  ? O TYR D 94   N TYR C 37  ? N TYR D 37   
AA4 4 5 N MET C 34  ? N MET D 34   O ILE C 51  ? O ILE D 51   
AA4 5 6 N ALA C 50  ? N ALA D 50   O LYS C 58  ? O LYS D 58   
AA5 1 2 N VAL C 12  ? N VAL D 12   O SER C 118 ? O SER D 118  
AA5 2 3 O THR C 113 ? O THR D 113  N TYR C 93  ? N TYR D 93   
AA5 3 4 N ALA C 97  ? N ALA D 97   O TYR C 108 ? O TYR D 108  
AA6 1 2 N GLN D 3   ? N GLN F 3    O SER D 25  ? O SER F 25   
AA6 2 3 N LEU D 20  ? N LEU F 20   O LEU D 80  ? O LEU F 80   
AA6 3 4 O TYR D 79  ? O TYR F 79   N SER D 70  ? N SER F 70   
AA7 1 2 N GLY D 10  ? N GLY F 10   O THR D 116 ? O THR F 116  
AA7 2 3 O THR D 113 ? O THR F 113  N TYR D 93  ? N TYR F 93   
AA7 3 4 O TYR D 94  ? O TYR F 94   N TYR D 37  ? N TYR F 37   
AA7 4 5 N MET D 34  ? N MET F 34   O ILE D 51  ? O ILE F 51   
AA7 5 6 N ALA D 50  ? N ALA F 50   O LYS D 58  ? O LYS F 58   
AA8 1 2 N GLY D 10  ? N GLY F 10   O THR D 116 ? O THR F 116  
AA8 2 3 O THR D 113 ? O THR F 113  N TYR D 93  ? N TYR F 93   
AA8 3 4 N VAL D 99  ? N VAL F 99   O TYR D 106 ? O TYR F 106  
# 
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 65   ? ? -82.56  49.10   
2  1 VAL A 86   ? ? -107.96 -67.44  
3  1 SER A 165  ? ? -133.51 -56.52  
4  1 PHE A 193  ? ? -102.68 62.26   
5  1 PHE A 208  ? ? -124.32 -65.16  
6  1 PHE A 264  ? ? 63.87   68.55   
7  1 GLN A 299  ? ? -84.75  -97.83  
8  1 ALA A 1082 ? ? 45.61   -136.11 
9  1 LYS A 1124 ? ? 58.39   15.27   
10 1 VAL B 86   ? ? -124.61 -67.66  
11 1 TYR B 141  ? ? 87.37   0.00    
12 1 PHE B 208  ? ? -129.37 -63.39  
13 1 CYS B 327  ? ? -69.15  2.61    
14 1 LYS B 1016 ? ? -116.95 -153.87 
15 1 ILE B 1029 ? ? -94.31  58.87   
16 1 MET B 1106 ? ? -133.69 -38.50  
17 1 SER D 7    ? ? -171.37 146.30  
18 1 THR D 102  ? ? -70.58  -72.98  
19 1 VAL F 12   ? ? -171.51 148.31  
20 1 THR F 102  ? ? -75.53  -74.08  
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z       
2 -x,y+1/2,-z 
# 
_pdbx_entry_details.entry_id                 8W1V 
_pdbx_entry_details.has_ligand_of_interest   Y 
_pdbx_entry_details.compound_details         ? 
_pdbx_entry_details.source_details           ? 
_pdbx_entry_details.nonpolymer_details       ? 
_pdbx_entry_details.sequence_details         ? 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 A MET -23  ? A MET 1   
2   1 Y 1 A LYS -22  ? A LYS 2   
3   1 Y 1 A THR -21  ? A THR 3   
4   1 Y 1 A ILE -20  ? A ILE 4   
5   1 Y 1 A ILE -19  ? A ILE 5   
6   1 Y 1 A ALA -18  ? A ALA 6   
7   1 Y 1 A LEU -17  ? A LEU 7   
8   1 Y 1 A SER -16  ? A SER 8   
9   1 Y 1 A TYR -15  ? A TYR 9   
10  1 Y 1 A ILE -14  ? A ILE 10  
11  1 Y 1 A PHE -13  ? A PHE 11  
12  1 Y 1 A CYS -12  ? A CYS 12  
13  1 Y 1 A LEU -11  ? A LEU 13  
14  1 Y 1 A VAL -10  ? A VAL 14  
15  1 Y 1 A PHE -9   ? A PHE 15  
16  1 Y 1 A ALA -8   ? A ALA 16  
17  1 Y 1 A ASP -7   ? A ASP 17  
18  1 Y 1 A TYR -6   ? A TYR 18  
19  1 Y 1 A LYS -5   ? A LYS 19  
20  1 Y 1 A ASP -4   ? A ASP 20  
21  1 Y 1 A ASP -3   ? A ASP 21  
22  1 Y 1 A ASP -2   ? A ASP 22  
23  1 Y 1 A ASP -1   ? A ASP 23  
24  1 Y 1 A ALA 0    ? A ALA 24  
25  1 Y 1 A MET 1    ? A MET 25  
26  1 Y 1 A GLY 2    ? A GLY 26  
27  1 Y 1 A GLN 3    ? A GLN 27  
28  1 Y 1 A PRO 4    ? A PRO 28  
29  1 Y 1 A GLY 5    ? A GLY 29  
30  1 Y 1 A ASN 6    ? A ASN 30  
31  1 Y 1 A GLY 7    ? A GLY 31  
32  1 Y 1 A SER 8    ? A SER 32  
33  1 Y 1 A ALA 9    ? A ALA 33  
34  1 Y 1 A PHE 10   ? A PHE 34  
35  1 Y 1 A LEU 11   ? A LEU 35  
36  1 Y 1 A LEU 12   ? A LEU 36  
37  1 Y 1 A ALA 13   ? A ALA 37  
38  1 Y 1 A PRO 14   ? A PRO 38  
39  1 Y 1 A ASN 15   ? A ASN 39  
40  1 Y 1 A ARG 16   ? A ARG 40  
41  1 Y 1 A SER 17   ? A SER 41  
42  1 Y 1 A HIS 18   ? A HIS 42  
43  1 Y 1 A ALA 19   ? A ALA 43  
44  1 Y 1 A PRO 20   ? A PRO 44  
45  1 Y 1 A ASP 21   ? A ASP 45  
46  1 Y 1 A HIS 22   ? A HIS 46  
47  1 Y 1 A ASP 23   ? A ASP 47  
48  1 Y 1 A VAL 24   ? A VAL 48  
49  1 Y 1 A THR 25   ? A THR 49  
50  1 Y 1 A GLN 26   ? A GLN 50  
51  1 Y 1 A GLN 27   ? A GLN 51  
52  1 Y 1 A ARG 28   ? A ARG 52  
53  1 Y 1 A TYR 231  ? A TYR 255 
54  1 Y 1 A LYS 232  ? A LYS 256 
55  1 Y 1 A ILE 233  ? A ILE 257 
56  1 Y 1 A ASP 234  ? A ASP 258 
57  1 Y 1 A LYS 235  ? A LYS 259 
58  1 Y 1 A SER 236  ? A SER 260 
59  1 Y 1 A GLU 237  ? A GLU 261 
60  1 Y 1 A GLY 238  ? A GLY 262 
61  1 Y 1 A ARG 239  ? A ARG 263 
62  1 Y 1 A PHE 240  ? A PHE 264 
63  1 Y 1 A HIS 241  ? A HIS 265 
64  1 Y 1 A VAL 242  ? A VAL 266 
65  1 Y 1 A GLN 243  ? A GLN 267 
66  1 Y 1 A ASN 244  ? A ASN 268 
67  1 Y 1 A LEU 245  ? A LEU 269 
68  1 Y 1 A SER 246  ? A SER 270 
69  1 Y 1 A GLN 247  ? A GLN 271 
70  1 Y 1 A VAL 248  ? A VAL 272 
71  1 Y 1 A GLU 249  ? A GLU 273 
72  1 Y 1 A GLN 250  ? A GLN 274 
73  1 Y 1 A ASP 251  ? A ASP 275 
74  1 Y 1 A GLY 252  ? A GLY 276 
75  1 Y 1 A ARG 253  ? A ARG 277 
76  1 Y 1 A THR 254  ? A THR 278 
77  1 Y 1 A GLY 255  ? A GLY 279 
78  1 Y 1 A HIS 256  ? A HIS 280 
79  1 Y 1 A GLY 257  ? A GLY 281 
80  1 Y 1 A LEU 258  ? A LEU 282 
81  1 Y 1 A ARG 259  ? A ARG 283 
82  1 Y 1 A ARG 260  ? A ARG 284 
83  1 Y 1 A SER 261  ? A SER 285 
84  1 Y 1 A SER 262  ? A SER 286 
85  1 Y 1 A ARG 979  ? A ARG 367 
86  1 Y 1 A ARG 980  ? A ARG 368 
87  1 Y 1 A SER 981  ? A SER 369 
88  1 Y 1 A SER 982  ? A SER 370 
89  1 Y 1 A LEU 983  ? A LEU 371 
90  1 Y 1 A LYS 984  ? A LYS 372 
91  1 Y 1 A ALA 985  ? A ALA 373 
92  1 Y 1 A TYR 986  ? A TYR 374 
93  1 Y 1 A GLY 987  ? A GLY 375 
94  1 Y 1 A ASN 988  ? A ASN 376 
95  1 Y 1 A GLY 989  ? A GLY 377 
96  1 Y 1 A TYR 990  ? A TYR 378 
97  1 Y 1 A SER 991  ? A SER 379 
98  1 Y 1 A SER 992  ? A SER 380 
99  1 Y 1 A ASN 993  ? A ASN 381 
100 1 Y 1 A GLY 994  ? A GLY 382 
101 1 Y 1 A ASN 995  ? A ASN 383 
102 1 Y 1 A THR 996  ? A THR 384 
103 1 Y 1 A GLY 997  ? A GLY 385 
104 1 Y 1 A GLU 998  ? A GLU 386 
105 1 Y 1 A GLN 999  ? A GLN 387 
106 1 Y 1 A SER 1000 ? A SER 388 
107 1 Y 1 A GLY 1001 ? A GLY 389 
108 1 Y 1 A ASN 1002 ? A ASN 390 
109 1 Y 1 B MET -23  ? B MET 1   
110 1 Y 1 B LYS -22  ? B LYS 2   
111 1 Y 1 B THR -21  ? B THR 3   
112 1 Y 1 B ILE -20  ? B ILE 4   
113 1 Y 1 B ILE -19  ? B ILE 5   
114 1 Y 1 B ALA -18  ? B ALA 6   
115 1 Y 1 B LEU -17  ? B LEU 7   
116 1 Y 1 B SER -16  ? B SER 8   
117 1 Y 1 B TYR -15  ? B TYR 9   
118 1 Y 1 B ILE -14  ? B ILE 10  
119 1 Y 1 B PHE -13  ? B PHE 11  
120 1 Y 1 B CYS -12  ? B CYS 12  
121 1 Y 1 B LEU -11  ? B LEU 13  
122 1 Y 1 B VAL -10  ? B VAL 14  
123 1 Y 1 B PHE -9   ? B PHE 15  
124 1 Y 1 B ALA -8   ? B ALA 16  
125 1 Y 1 B ASP -7   ? B ASP 17  
126 1 Y 1 B TYR -6   ? B TYR 18  
127 1 Y 1 B LYS -5   ? B LYS 19  
128 1 Y 1 B ASP -4   ? B ASP 20  
129 1 Y 1 B ASP -3   ? B ASP 21  
130 1 Y 1 B ASP -2   ? B ASP 22  
131 1 Y 1 B ASP -1   ? B ASP 23  
132 1 Y 1 B ALA 0    ? B ALA 24  
133 1 Y 1 B MET 1    ? B MET 25  
134 1 Y 1 B GLY 2    ? B GLY 26  
135 1 Y 1 B GLN 3    ? B GLN 27  
136 1 Y 1 B PRO 4    ? B PRO 28  
137 1 Y 1 B GLY 5    ? B GLY 29  
138 1 Y 1 B ASN 6    ? B ASN 30  
139 1 Y 1 B GLY 7    ? B GLY 31  
140 1 Y 1 B SER 8    ? B SER 32  
141 1 Y 1 B ALA 9    ? B ALA 33  
142 1 Y 1 B PHE 10   ? B PHE 34  
143 1 Y 1 B LEU 11   ? B LEU 35  
144 1 Y 1 B LEU 12   ? B LEU 36  
145 1 Y 1 B ALA 13   ? B ALA 37  
146 1 Y 1 B PRO 14   ? B PRO 38  
147 1 Y 1 B ASN 15   ? B ASN 39  
148 1 Y 1 B ARG 16   ? B ARG 40  
149 1 Y 1 B SER 17   ? B SER 41  
150 1 Y 1 B HIS 18   ? B HIS 42  
151 1 Y 1 B ALA 19   ? B ALA 43  
152 1 Y 1 B PRO 20   ? B PRO 44  
153 1 Y 1 B ASP 21   ? B ASP 45  
154 1 Y 1 B HIS 22   ? B HIS 46  
155 1 Y 1 B ASP 23   ? B ASP 47  
156 1 Y 1 B VAL 24   ? B VAL 48  
157 1 Y 1 B THR 25   ? B THR 49  
158 1 Y 1 B GLN 26   ? B GLN 50  
159 1 Y 1 B GLN 27   ? B GLN 51  
160 1 Y 1 B ARG 28   ? B ARG 52  
161 1 Y 1 B LEU 230  ? B LEU 254 
162 1 Y 1 B TYR 231  ? B TYR 255 
163 1 Y 1 B LYS 232  ? B LYS 256 
164 1 Y 1 B ILE 233  ? B ILE 257 
165 1 Y 1 B ASP 234  ? B ASP 258 
166 1 Y 1 B LYS 235  ? B LYS 259 
167 1 Y 1 B SER 236  ? B SER 260 
168 1 Y 1 B GLU 237  ? B GLU 261 
169 1 Y 1 B GLY 238  ? B GLY 262 
170 1 Y 1 B ARG 239  ? B ARG 263 
171 1 Y 1 B PHE 240  ? B PHE 264 
172 1 Y 1 B HIS 241  ? B HIS 265 
173 1 Y 1 B VAL 242  ? B VAL 266 
174 1 Y 1 B GLN 243  ? B GLN 267 
175 1 Y 1 B ASN 244  ? B ASN 268 
176 1 Y 1 B LEU 245  ? B LEU 269 
177 1 Y 1 B SER 246  ? B SER 270 
178 1 Y 1 B GLN 247  ? B GLN 271 
179 1 Y 1 B VAL 248  ? B VAL 272 
180 1 Y 1 B GLU 249  ? B GLU 273 
181 1 Y 1 B GLN 250  ? B GLN 274 
182 1 Y 1 B ASP 251  ? B ASP 275 
183 1 Y 1 B GLY 252  ? B GLY 276 
184 1 Y 1 B ARG 253  ? B ARG 277 
185 1 Y 1 B THR 254  ? B THR 278 
186 1 Y 1 B GLY 255  ? B GLY 279 
187 1 Y 1 B HIS 256  ? B HIS 280 
188 1 Y 1 B GLY 257  ? B GLY 281 
189 1 Y 1 B LEU 258  ? B LEU 282 
190 1 Y 1 B ARG 259  ? B ARG 283 
191 1 Y 1 B ARG 260  ? B ARG 284 
192 1 Y 1 B SER 261  ? B SER 285 
193 1 Y 1 B SER 262  ? B SER 286 
194 1 Y 1 B ARG 979  ? B ARG 367 
195 1 Y 1 B ARG 980  ? B ARG 368 
196 1 Y 1 B SER 981  ? B SER 369 
197 1 Y 1 B SER 982  ? B SER 370 
198 1 Y 1 B LEU 983  ? B LEU 371 
199 1 Y 1 B LYS 984  ? B LYS 372 
200 1 Y 1 B ALA 985  ? B ALA 373 
201 1 Y 1 B TYR 986  ? B TYR 374 
202 1 Y 1 B GLY 987  ? B GLY 375 
203 1 Y 1 B ASN 988  ? B ASN 376 
204 1 Y 1 B GLY 989  ? B GLY 377 
205 1 Y 1 B TYR 990  ? B TYR 378 
206 1 Y 1 B SER 991  ? B SER 379 
207 1 Y 1 B SER 992  ? B SER 380 
208 1 Y 1 B ASN 993  ? B ASN 381 
209 1 Y 1 B GLY 994  ? B GLY 382 
210 1 Y 1 B ASN 995  ? B ASN 383 
211 1 Y 1 B THR 996  ? B THR 384 
212 1 Y 1 B GLY 997  ? B GLY 385 
213 1 Y 1 B GLU 998  ? B GLU 386 
214 1 Y 1 B GLN 999  ? B GLN 387 
215 1 Y 1 B SER 1000 ? B SER 388 
216 1 Y 1 B GLY 1001 ? B GLY 389 
217 1 Y 1 B GLY 1056 ? B GLY 444 
218 1 Y 1 B VAL 1057 ? B VAL 445 
219 1 Y 1 D GLN 1    ? C GLN 1   
220 1 Y 1 D HIS 121  ? C HIS 121 
221 1 Y 1 D HIS 122  ? C HIS 122 
222 1 Y 1 D HIS 123  ? C HIS 123 
223 1 Y 1 D HIS 124  ? C HIS 124 
224 1 Y 1 D HIS 125  ? C HIS 125 
225 1 Y 1 F HIS 120  ? D HIS 120 
226 1 Y 1 F HIS 121  ? D HIS 121 
227 1 Y 1 F HIS 122  ? D HIS 122 
228 1 Y 1 F HIS 123  ? D HIS 123 
229 1 Y 1 F HIS 124  ? D HIS 124 
230 1 Y 1 F HIS 125  ? D HIS 125 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1AE2 C4   C Y N 1   
A1AE2 C14  C N N 2   
A1AE2 C5   C Y N 3   
A1AE2 C6   C Y N 4   
A1AE2 C11  C N S 5   
A1AE2 C7   C N N 6   
A1AE2 C8   C N N 7   
A1AE2 C9   C N N 8   
A1AE2 C10  C N N 9   
A1AE2 C12  C N N 10  
A1AE2 C13  C N N 11  
A1AE2 N1   N N N 12  
A1AE2 N2   N Y N 13  
A1AE2 C3   C Y N 14  
A1AE2 N3   N Y N 15  
A1AE2 C1   C Y N 16  
A1AE2 C15  C N N 17  
A1AE2 C16  C Y N 18  
A1AE2 C17  C Y N 19  
A1AE2 C18  C N N 20  
A1AE2 C19  C N N 21  
A1AE2 C2   C Y N 22  
A1AE2 C20  C N N 23  
A1AE2 C21  C N N 24  
A1AE2 C22  C Y N 25  
A1AE2 C23  C Y N 26  
A1AE2 C24  C Y N 27  
A1AE2 C25  C Y N 28  
A1AE2 C26  C Y N 29  
A1AE2 C27  C Y N 30  
A1AE2 C28  C N N 31  
A1AE2 C29  C N S 32  
A1AE2 C30  C N N 33  
A1AE2 C31  C N N 34  
A1AE2 C32  C N N 35  
A1AE2 C33  C N N 36  
A1AE2 N4   N Y N 37  
A1AE2 N5   N N N 38  
A1AE2 O1   O N N 39  
A1AE2 O2   O N N 40  
A1AE2 O3   O N N 41  
A1AE2 O4   O N N 42  
A1AE2 H3   H N N 43  
A1AE2 H19  H N N 44  
A1AE2 H20  H N N 45  
A1AE2 H4   H N N 46  
A1AE2 H12  H N N 47  
A1AE2 H6   H N N 48  
A1AE2 H5   H N N 49  
A1AE2 H7   H N N 50  
A1AE2 H50  H N N 51  
A1AE2 H9   H N N 52  
A1AE2 H8   H N N 53  
A1AE2 H51  H N N 54  
A1AE2 H11  H N N 55  
A1AE2 H10  H N N 56  
A1AE2 H14  H N N 57  
A1AE2 H13  H N N 58  
A1AE2 H17  H N N 59  
A1AE2 H18  H N N 60  
A1AE2 H16  H N N 61  
A1AE2 H2   H N N 62  
A1AE2 H21  H N N 63  
A1AE2 H22  H N N 64  
A1AE2 H23  H N N 65  
A1AE2 H24  H N N 66  
A1AE2 H25  H N N 67  
A1AE2 H27  H N N 68  
A1AE2 H26  H N N 69  
A1AE2 H1   H N N 70  
A1AE2 H28  H N N 71  
A1AE2 H29  H N N 72  
A1AE2 H31  H N N 73  
A1AE2 H30  H N N 74  
A1AE2 H32  H N N 75  
A1AE2 H33  H N N 76  
A1AE2 H34  H N N 77  
A1AE2 H35  H N N 78  
A1AE2 H36  H N N 79  
A1AE2 H37  H N N 80  
A1AE2 H38  H N N 81  
A1AE2 H39  H N N 82  
A1AE2 H40  H N N 83  
A1AE2 H43  H N N 84  
A1AE2 H44  H N N 85  
A1AE2 H45  H N N 86  
A1AE2 H46  H N N 87  
A1AE2 H47  H N N 88  
A1AE2 H49  H N N 89  
A1AE2 H48  H N N 90  
A1AE2 H53  H N N 91  
A1AE2 H15  H N N 92  
A1AE2 H41  H N N 93  
ALA   N    N N N 94  
ALA   CA   C N S 95  
ALA   C    C N N 96  
ALA   O    O N N 97  
ALA   CB   C N N 98  
ALA   OXT  O N N 99  
ALA   H    H N N 100 
ALA   H2   H N N 101 
ALA   HA   H N N 102 
ALA   HB1  H N N 103 
ALA   HB2  H N N 104 
ALA   HB3  H N N 105 
ALA   HXT  H N N 106 
ARG   N    N N N 107 
ARG   CA   C N S 108 
ARG   C    C N N 109 
ARG   O    O N N 110 
ARG   CB   C N N 111 
ARG   CG   C N N 112 
ARG   CD   C N N 113 
ARG   NE   N N N 114 
ARG   CZ   C N N 115 
ARG   NH1  N N N 116 
ARG   NH2  N N N 117 
ARG   OXT  O N N 118 
ARG   H    H N N 119 
ARG   H2   H N N 120 
ARG   HA   H N N 121 
ARG   HB2  H N N 122 
ARG   HB3  H N N 123 
ARG   HG2  H N N 124 
ARG   HG3  H N N 125 
ARG   HD2  H N N 126 
ARG   HD3  H N N 127 
ARG   HE   H N N 128 
ARG   HH11 H N N 129 
ARG   HH12 H N N 130 
ARG   HH21 H N N 131 
ARG   HH22 H N N 132 
ARG   HXT  H N N 133 
ASN   N    N N N 134 
ASN   CA   C N S 135 
ASN   C    C N N 136 
ASN   O    O N N 137 
ASN   CB   C N N 138 
ASN   CG   C N N 139 
ASN   OD1  O N N 140 
ASN   ND2  N N N 141 
ASN   OXT  O N N 142 
ASN   H    H N N 143 
ASN   H2   H N N 144 
ASN   HA   H N N 145 
ASN   HB2  H N N 146 
ASN   HB3  H N N 147 
ASN   HD21 H N N 148 
ASN   HD22 H N N 149 
ASN   HXT  H N N 150 
ASP   N    N N N 151 
ASP   CA   C N S 152 
ASP   C    C N N 153 
ASP   O    O N N 154 
ASP   CB   C N N 155 
ASP   CG   C N N 156 
ASP   OD1  O N N 157 
ASP   OD2  O N N 158 
ASP   OXT  O N N 159 
ASP   H    H N N 160 
ASP   H2   H N N 161 
ASP   HA   H N N 162 
ASP   HB2  H N N 163 
ASP   HB3  H N N 164 
ASP   HD2  H N N 165 
ASP   HXT  H N N 166 
AV0   C1   C N R 167 
AV0   O1   O N N 168 
AV0   C2   C N R 169 
AV0   O2   O N N 170 
AV0   C3   C N R 171 
AV0   O3   O N N 172 
AV0   C4   C N S 173 
AV0   O4   O N N 174 
AV0   C5   C N R 175 
AV0   O5   O N N 176 
AV0   C6   C N N 177 
AV0   O6   O N N 178 
AV0   CAA  C N N 179 
AV0   CAB  C N N 180 
AV0   OAI  O N N 181 
AV0   OAJ  O N N 182 
AV0   OAL  O N N 183 
AV0   OAN  O N N 184 
AV0   OAP  O N N 185 
AV0   OAQ  O N N 186 
AV0   OAR  O N N 187 
AV0   OAS  O N N 188 
AV0   OAT  O N N 189 
AV0   OAU  O N N 190 
AV0   OAV  O N N 191 
AV0   CAW  C N N 192 
AV0   CAX  C N N 193 
AV0   CAY  C N N 194 
AV0   CAZ  C N N 195 
AV0   CBA  C N N 196 
AV0   CBB  C N N 197 
AV0   CBC  C N N 198 
AV0   CBD  C N N 199 
AV0   CBE  C N N 200 
AV0   CBF  C N N 201 
AV0   CBG  C N N 202 
AV0   CBH  C N N 203 
AV0   CBI  C N N 204 
AV0   CBJ  C N N 205 
AV0   CBK  C N N 206 
AV0   CBL  C N N 207 
AV0   CBM  C N N 208 
AV0   CBN  C N N 209 
AV0   CBP  C N N 210 
AV0   CBQ  C N N 211 
AV0   CBR  C N N 212 
AV0   CBS  C N N 213 
AV0   CBT  C N N 214 
AV0   OBV  O N N 215 
AV0   OBX  O N N 216 
AV0   OBY  O N N 217 
AV0   OBZ  O N N 218 
AV0   OCB  O N N 219 
AV0   CCC  C N R 220 
AV0   CCD  C N R 221 
AV0   CCF  C N R 222 
AV0   CCH  C N R 223 
AV0   CCJ  C N R 224 
AV0   CCL  C N R 225 
AV0   CCM  C N N 226 
AV0   CCN  C N S 227 
AV0   CCO  C N S 228 
AV0   CCQ  C N S 229 
AV0   CCR  C N R 230 
AV0   CCS  C N R 231 
AV0   CCT  C N S 232 
AV0   CCU  C N S 233 
AV0   CCV  C N R 234 
AV0   CCW  C N R 235 
AV0   H1   H N N 236 
AV0   H2   H N N 237 
AV0   H3   H N N 238 
AV0   H4   H N N 239 
AV0   H5   H N N 240 
AV0   H6   H N N 241 
AV0   H7   H N N 242 
AV0   H8   H N N 243 
AV0   H9   H N N 244 
AV0   H10  H N N 245 
AV0   H11  H N N 246 
AV0   H12  H N N 247 
AV0   H13  H N N 248 
AV0   H14  H N N 249 
AV0   H15  H N N 250 
AV0   H16  H N N 251 
AV0   H17  H N N 252 
AV0   H18  H N N 253 
AV0   H19  H N N 254 
AV0   H20  H N N 255 
AV0   H21  H N N 256 
AV0   H22  H N N 257 
AV0   H23  H N N 258 
AV0   H24  H N N 259 
AV0   H25  H N N 260 
AV0   H26  H N N 261 
AV0   H27  H N N 262 
AV0   H28  H N N 263 
AV0   H29  H N N 264 
AV0   H30  H N N 265 
AV0   H31  H N N 266 
AV0   H32  H N N 267 
AV0   H33  H N N 268 
AV0   H34  H N N 269 
AV0   H35  H N N 270 
AV0   H36  H N N 271 
AV0   H37  H N N 272 
AV0   H38  H N N 273 
AV0   H39  H N N 274 
AV0   H40  H N N 275 
AV0   H41  H N N 276 
AV0   H42  H N N 277 
AV0   H43  H N N 278 
AV0   H44  H N N 279 
AV0   H45  H N N 280 
AV0   H46  H N N 281 
AV0   H47  H N N 282 
AV0   H48  H N N 283 
AV0   H49  H N N 284 
AV0   H50  H N N 285 
AV0   H51  H N N 286 
AV0   H52  H N N 287 
AV0   H53  H N N 288 
AV0   H54  H N N 289 
AV0   H55  H N N 290 
AV0   H56  H N N 291 
AV0   H57  H N N 292 
AV0   H58  H N N 293 
AV0   H59  H N N 294 
AV0   H60  H N N 295 
AV0   H61  H N N 296 
AV0   H62  H N N 297 
AV0   H63  H N N 298 
AV0   H64  H N N 299 
AV0   H65  H N N 300 
AV0   H66  H N N 301 
AV0   H67  H N N 302 
AV0   H68  H N N 303 
AV0   H69  H N N 304 
AV0   H70  H N N 305 
AV0   H71  H N N 306 
AV0   H72  H N N 307 
AV0   H73  H N N 308 
AV0   H74  H N N 309 
AV0   H75  H N N 310 
AV0   H76  H N N 311 
AV0   H77  H N N 312 
AV0   H78  H N N 313 
AV0   H79  H N N 314 
AV0   H80  H N N 315 
AV0   H81  H N N 316 
AV0   H82  H N N 317 
AV0   H83  H N N 318 
AV0   H84  H N N 319 
AV0   H85  H N N 320 
AV0   H86  H N N 321 
AV0   H87  H N N 322 
AV0   H88  H N N 323 
CYS   N    N N N 324 
CYS   CA   C N R 325 
CYS   C    C N N 326 
CYS   O    O N N 327 
CYS   CB   C N N 328 
CYS   SG   S N N 329 
CYS   OXT  O N N 330 
CYS   H    H N N 331 
CYS   H2   H N N 332 
CYS   HA   H N N 333 
CYS   HB2  H N N 334 
CYS   HB3  H N N 335 
CYS   HG   H N N 336 
CYS   HXT  H N N 337 
GLN   N    N N N 338 
GLN   CA   C N S 339 
GLN   C    C N N 340 
GLN   O    O N N 341 
GLN   CB   C N N 342 
GLN   CG   C N N 343 
GLN   CD   C N N 344 
GLN   OE1  O N N 345 
GLN   NE2  N N N 346 
GLN   OXT  O N N 347 
GLN   H    H N N 348 
GLN   H2   H N N 349 
GLN   HA   H N N 350 
GLN   HB2  H N N 351 
GLN   HB3  H N N 352 
GLN   HG2  H N N 353 
GLN   HG3  H N N 354 
GLN   HE21 H N N 355 
GLN   HE22 H N N 356 
GLN   HXT  H N N 357 
GLU   N    N N N 358 
GLU   CA   C N S 359 
GLU   C    C N N 360 
GLU   O    O N N 361 
GLU   CB   C N N 362 
GLU   CG   C N N 363 
GLU   CD   C N N 364 
GLU   OE1  O N N 365 
GLU   OE2  O N N 366 
GLU   OXT  O N N 367 
GLU   H    H N N 368 
GLU   H2   H N N 369 
GLU   HA   H N N 370 
GLU   HB2  H N N 371 
GLU   HB3  H N N 372 
GLU   HG2  H N N 373 
GLU   HG3  H N N 374 
GLU   HE2  H N N 375 
GLU   HXT  H N N 376 
GLY   N    N N N 377 
GLY   CA   C N N 378 
GLY   C    C N N 379 
GLY   O    O N N 380 
GLY   OXT  O N N 381 
GLY   H    H N N 382 
GLY   H2   H N N 383 
GLY   HA2  H N N 384 
GLY   HA3  H N N 385 
GLY   HXT  H N N 386 
HIS   N    N N N 387 
HIS   CA   C N S 388 
HIS   C    C N N 389 
HIS   O    O N N 390 
HIS   CB   C N N 391 
HIS   CG   C Y N 392 
HIS   ND1  N Y N 393 
HIS   CD2  C Y N 394 
HIS   CE1  C Y N 395 
HIS   NE2  N Y N 396 
HIS   OXT  O N N 397 
HIS   H    H N N 398 
HIS   H2   H N N 399 
HIS   HA   H N N 400 
HIS   HB2  H N N 401 
HIS   HB3  H N N 402 
HIS   HD1  H N N 403 
HIS   HD2  H N N 404 
HIS   HE1  H N N 405 
HIS   HE2  H N N 406 
HIS   HXT  H N N 407 
ILE   N    N N N 408 
ILE   CA   C N S 409 
ILE   C    C N N 410 
ILE   O    O N N 411 
ILE   CB   C N S 412 
ILE   CG1  C N N 413 
ILE   CG2  C N N 414 
ILE   CD1  C N N 415 
ILE   OXT  O N N 416 
ILE   H    H N N 417 
ILE   H2   H N N 418 
ILE   HA   H N N 419 
ILE   HB   H N N 420 
ILE   HG12 H N N 421 
ILE   HG13 H N N 422 
ILE   HG21 H N N 423 
ILE   HG22 H N N 424 
ILE   HG23 H N N 425 
ILE   HD11 H N N 426 
ILE   HD12 H N N 427 
ILE   HD13 H N N 428 
ILE   HXT  H N N 429 
LEU   N    N N N 430 
LEU   CA   C N S 431 
LEU   C    C N N 432 
LEU   O    O N N 433 
LEU   CB   C N N 434 
LEU   CG   C N N 435 
LEU   CD1  C N N 436 
LEU   CD2  C N N 437 
LEU   OXT  O N N 438 
LEU   H    H N N 439 
LEU   H2   H N N 440 
LEU   HA   H N N 441 
LEU   HB2  H N N 442 
LEU   HB3  H N N 443 
LEU   HG   H N N 444 
LEU   HD11 H N N 445 
LEU   HD12 H N N 446 
LEU   HD13 H N N 447 
LEU   HD21 H N N 448 
LEU   HD22 H N N 449 
LEU   HD23 H N N 450 
LEU   HXT  H N N 451 
LYS   N    N N N 452 
LYS   CA   C N S 453 
LYS   C    C N N 454 
LYS   O    O N N 455 
LYS   CB   C N N 456 
LYS   CG   C N N 457 
LYS   CD   C N N 458 
LYS   CE   C N N 459 
LYS   NZ   N N N 460 
LYS   OXT  O N N 461 
LYS   H    H N N 462 
LYS   H2   H N N 463 
LYS   HA   H N N 464 
LYS   HB2  H N N 465 
LYS   HB3  H N N 466 
LYS   HG2  H N N 467 
LYS   HG3  H N N 468 
LYS   HD2  H N N 469 
LYS   HD3  H N N 470 
LYS   HE2  H N N 471 
LYS   HE3  H N N 472 
LYS   HZ1  H N N 473 
LYS   HZ2  H N N 474 
LYS   HZ3  H N N 475 
LYS   HXT  H N N 476 
MET   N    N N N 477 
MET   CA   C N S 478 
MET   C    C N N 479 
MET   O    O N N 480 
MET   CB   C N N 481 
MET   CG   C N N 482 
MET   SD   S N N 483 
MET   CE   C N N 484 
MET   OXT  O N N 485 
MET   H    H N N 486 
MET   H2   H N N 487 
MET   HA   H N N 488 
MET   HB2  H N N 489 
MET   HB3  H N N 490 
MET   HG2  H N N 491 
MET   HG3  H N N 492 
MET   HE1  H N N 493 
MET   HE2  H N N 494 
MET   HE3  H N N 495 
MET   HXT  H N N 496 
PHE   N    N N N 497 
PHE   CA   C N S 498 
PHE   C    C N N 499 
PHE   O    O N N 500 
PHE   CB   C N N 501 
PHE   CG   C Y N 502 
PHE   CD1  C Y N 503 
PHE   CD2  C Y N 504 
PHE   CE1  C Y N 505 
PHE   CE2  C Y N 506 
PHE   CZ   C Y N 507 
PHE   OXT  O N N 508 
PHE   H    H N N 509 
PHE   H2   H N N 510 
PHE   HA   H N N 511 
PHE   HB2  H N N 512 
PHE   HB3  H N N 513 
PHE   HD1  H N N 514 
PHE   HD2  H N N 515 
PHE   HE1  H N N 516 
PHE   HE2  H N N 517 
PHE   HZ   H N N 518 
PHE   HXT  H N N 519 
PRO   N    N N N 520 
PRO   CA   C N S 521 
PRO   C    C N N 522 
PRO   O    O N N 523 
PRO   CB   C N N 524 
PRO   CG   C N N 525 
PRO   CD   C N N 526 
PRO   OXT  O N N 527 
PRO   H    H N N 528 
PRO   HA   H N N 529 
PRO   HB2  H N N 530 
PRO   HB3  H N N 531 
PRO   HG2  H N N 532 
PRO   HG3  H N N 533 
PRO   HD2  H N N 534 
PRO   HD3  H N N 535 
PRO   HXT  H N N 536 
SER   N    N N N 537 
SER   CA   C N S 538 
SER   C    C N N 539 
SER   O    O N N 540 
SER   CB   C N N 541 
SER   OG   O N N 542 
SER   OXT  O N N 543 
SER   H    H N N 544 
SER   H2   H N N 545 
SER   HA   H N N 546 
SER   HB2  H N N 547 
SER   HB3  H N N 548 
SER   HG   H N N 549 
SER   HXT  H N N 550 
THR   N    N N N 551 
THR   CA   C N S 552 
THR   C    C N N 553 
THR   O    O N N 554 
THR   CB   C N R 555 
THR   OG1  O N N 556 
THR   CG2  C N N 557 
THR   OXT  O N N 558 
THR   H    H N N 559 
THR   H2   H N N 560 
THR   HA   H N N 561 
THR   HB   H N N 562 
THR   HG1  H N N 563 
THR   HG21 H N N 564 
THR   HG22 H N N 565 
THR   HG23 H N N 566 
THR   HXT  H N N 567 
TRP   N    N N N 568 
TRP   CA   C N S 569 
TRP   C    C N N 570 
TRP   O    O N N 571 
TRP   CB   C N N 572 
TRP   CG   C Y N 573 
TRP   CD1  C Y N 574 
TRP   CD2  C Y N 575 
TRP   NE1  N Y N 576 
TRP   CE2  C Y N 577 
TRP   CE3  C Y N 578 
TRP   CZ2  C Y N 579 
TRP   CZ3  C Y N 580 
TRP   CH2  C Y N 581 
TRP   OXT  O N N 582 
TRP   H    H N N 583 
TRP   H2   H N N 584 
TRP   HA   H N N 585 
TRP   HB2  H N N 586 
TRP   HB3  H N N 587 
TRP   HD1  H N N 588 
TRP   HE1  H N N 589 
TRP   HE3  H N N 590 
TRP   HZ2  H N N 591 
TRP   HZ3  H N N 592 
TRP   HH2  H N N 593 
TRP   HXT  H N N 594 
TYR   N    N N N 595 
TYR   CA   C N S 596 
TYR   C    C N N 597 
TYR   O    O N N 598 
TYR   CB   C N N 599 
TYR   CG   C Y N 600 
TYR   CD1  C Y N 601 
TYR   CD2  C Y N 602 
TYR   CE1  C Y N 603 
TYR   CE2  C Y N 604 
TYR   CZ   C Y N 605 
TYR   OH   O N N 606 
TYR   OXT  O N N 607 
TYR   H    H N N 608 
TYR   H2   H N N 609 
TYR   HA   H N N 610 
TYR   HB2  H N N 611 
TYR   HB3  H N N 612 
TYR   HD1  H N N 613 
TYR   HD2  H N N 614 
TYR   HE1  H N N 615 
TYR   HE2  H N N 616 
TYR   HH   H N N 617 
TYR   HXT  H N N 618 
VAL   N    N N N 619 
VAL   CA   C N S 620 
VAL   C    C N N 621 
VAL   O    O N N 622 
VAL   CB   C N N 623 
VAL   CG1  C N N 624 
VAL   CG2  C N N 625 
VAL   OXT  O N N 626 
VAL   H    H N N 627 
VAL   H2   H N N 628 
VAL   HA   H N N 629 
VAL   HB   H N N 630 
VAL   HG11 H N N 631 
VAL   HG12 H N N 632 
VAL   HG13 H N N 633 
VAL   HG21 H N N 634 
VAL   HG22 H N N 635 
VAL   HG23 H N N 636 
VAL   HXT  H N N 637 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1AE2 C1  C2   doub Y N 1   
A1AE2 C1  C6   sing Y N 2   
A1AE2 C1  O1   sing N N 3   
A1AE2 C2  C3   sing Y N 4   
A1AE2 C3  C4   doub Y N 5   
A1AE2 C4  C5   sing Y N 6   
A1AE2 C5  C6   doub Y N 7   
A1AE2 C6  C7   sing N N 8   
A1AE2 C7  C8   sing N N 9   
A1AE2 C8  C9   sing N N 10  
A1AE2 O1  C10  sing N N 11  
A1AE2 C10 C11  sing N N 12  
A1AE2 C11 C12  sing N N 13  
A1AE2 C11 O2   sing N N 14  
A1AE2 C12 N1   sing N N 15  
A1AE2 N1  C13  sing N N 16  
A1AE2 C13 C14  sing N N 17  
A1AE2 C14 C15  sing N N 18  
A1AE2 C15 C16  sing N N 19  
A1AE2 C16 N2   sing Y N 20  
A1AE2 C16 C17  doub Y N 21  
A1AE2 N2  N3   doub Y N 22  
A1AE2 N3  N4   sing Y N 23  
A1AE2 N4  C17  sing Y N 24  
A1AE2 N4  C18  sing N N 25  
A1AE2 C18 C19  sing N N 26  
A1AE2 C19 C20  sing N N 27  
A1AE2 C20 C21  sing N N 28  
A1AE2 C21 C22  sing N N 29  
A1AE2 C22 C23  doub Y N 30  
A1AE2 C22 C27  sing Y N 31  
A1AE2 C23 C24  sing Y N 32  
A1AE2 C24 C25  doub Y N 33  
A1AE2 C25 C26  sing Y N 34  
A1AE2 C25 O3   sing N N 35  
A1AE2 C26 C27  doub Y N 36  
A1AE2 O3  C28  sing N N 37  
A1AE2 C28 C29  sing N N 38  
A1AE2 C29 C30  sing N N 39  
A1AE2 C29 O4   sing N N 40  
A1AE2 C30 N5   sing N N 41  
A1AE2 N5  C31  sing N N 42  
A1AE2 C31 C32  sing N N 43  
A1AE2 C31 C33  sing N N 44  
A1AE2 C4  H3   sing N N 45  
A1AE2 C14 H19  sing N N 46  
A1AE2 C14 H20  sing N N 47  
A1AE2 C5  H4   sing N N 48  
A1AE2 C11 H12  sing N N 49  
A1AE2 C7  H6   sing N N 50  
A1AE2 C7  H5   sing N N 51  
A1AE2 C8  H7   sing N N 52  
A1AE2 C8  H50  sing N N 53  
A1AE2 C9  H9   sing N N 54  
A1AE2 C9  H8   sing N N 55  
A1AE2 C9  H51  sing N N 56  
A1AE2 C10 H11  sing N N 57  
A1AE2 C10 H10  sing N N 58  
A1AE2 C12 H14  sing N N 59  
A1AE2 C12 H13  sing N N 60  
A1AE2 C13 H17  sing N N 61  
A1AE2 C13 H18  sing N N 62  
A1AE2 N1  H16  sing N N 63  
A1AE2 C3  H2   sing N N 64  
A1AE2 C15 H21  sing N N 65  
A1AE2 C15 H22  sing N N 66  
A1AE2 C17 H23  sing N N 67  
A1AE2 C18 H24  sing N N 68  
A1AE2 C18 H25  sing N N 69  
A1AE2 C19 H27  sing N N 70  
A1AE2 C19 H26  sing N N 71  
A1AE2 C2  H1   sing N N 72  
A1AE2 C20 H28  sing N N 73  
A1AE2 C20 H29  sing N N 74  
A1AE2 C21 H31  sing N N 75  
A1AE2 C21 H30  sing N N 76  
A1AE2 C23 H32  sing N N 77  
A1AE2 C24 H33  sing N N 78  
A1AE2 C26 H34  sing N N 79  
A1AE2 C27 H35  sing N N 80  
A1AE2 C28 H36  sing N N 81  
A1AE2 C28 H37  sing N N 82  
A1AE2 C29 H38  sing N N 83  
A1AE2 C30 H39  sing N N 84  
A1AE2 C30 H40  sing N N 85  
A1AE2 C31 H43  sing N N 86  
A1AE2 C32 H44  sing N N 87  
A1AE2 C32 H45  sing N N 88  
A1AE2 C32 H46  sing N N 89  
A1AE2 C33 H47  sing N N 90  
A1AE2 C33 H49  sing N N 91  
A1AE2 C33 H48  sing N N 92  
A1AE2 N5  H53  sing N N 93  
A1AE2 O2  H15  sing N N 94  
A1AE2 O4  H41  sing N N 95  
ALA   N   CA   sing N N 96  
ALA   N   H    sing N N 97  
ALA   N   H2   sing N N 98  
ALA   CA  C    sing N N 99  
ALA   CA  CB   sing N N 100 
ALA   CA  HA   sing N N 101 
ALA   C   O    doub N N 102 
ALA   C   OXT  sing N N 103 
ALA   CB  HB1  sing N N 104 
ALA   CB  HB2  sing N N 105 
ALA   CB  HB3  sing N N 106 
ALA   OXT HXT  sing N N 107 
ARG   N   CA   sing N N 108 
ARG   N   H    sing N N 109 
ARG   N   H2   sing N N 110 
ARG   CA  C    sing N N 111 
ARG   CA  CB   sing N N 112 
ARG   CA  HA   sing N N 113 
ARG   C   O    doub N N 114 
ARG   C   OXT  sing N N 115 
ARG   CB  CG   sing N N 116 
ARG   CB  HB2  sing N N 117 
ARG   CB  HB3  sing N N 118 
ARG   CG  CD   sing N N 119 
ARG   CG  HG2  sing N N 120 
ARG   CG  HG3  sing N N 121 
ARG   CD  NE   sing N N 122 
ARG   CD  HD2  sing N N 123 
ARG   CD  HD3  sing N N 124 
ARG   NE  CZ   sing N N 125 
ARG   NE  HE   sing N N 126 
ARG   CZ  NH1  sing N N 127 
ARG   CZ  NH2  doub N N 128 
ARG   NH1 HH11 sing N N 129 
ARG   NH1 HH12 sing N N 130 
ARG   NH2 HH21 sing N N 131 
ARG   NH2 HH22 sing N N 132 
ARG   OXT HXT  sing N N 133 
ASN   N   CA   sing N N 134 
ASN   N   H    sing N N 135 
ASN   N   H2   sing N N 136 
ASN   CA  C    sing N N 137 
ASN   CA  CB   sing N N 138 
ASN   CA  HA   sing N N 139 
ASN   C   O    doub N N 140 
ASN   C   OXT  sing N N 141 
ASN   CB  CG   sing N N 142 
ASN   CB  HB2  sing N N 143 
ASN   CB  HB3  sing N N 144 
ASN   CG  OD1  doub N N 145 
ASN   CG  ND2  sing N N 146 
ASN   ND2 HD21 sing N N 147 
ASN   ND2 HD22 sing N N 148 
ASN   OXT HXT  sing N N 149 
ASP   N   CA   sing N N 150 
ASP   N   H    sing N N 151 
ASP   N   H2   sing N N 152 
ASP   CA  C    sing N N 153 
ASP   CA  CB   sing N N 154 
ASP   CA  HA   sing N N 155 
ASP   C   O    doub N N 156 
ASP   C   OXT  sing N N 157 
ASP   CB  CG   sing N N 158 
ASP   CB  HB2  sing N N 159 
ASP   CB  HB3  sing N N 160 
ASP   CG  OD1  doub N N 161 
ASP   CG  OD2  sing N N 162 
ASP   OD2 HD2  sing N N 163 
ASP   OXT HXT  sing N N 164 
AV0   CAB CAX  sing N N 165 
AV0   CAX CAZ  sing N N 166 
AV0   CAA CAW  sing N N 167 
AV0   CAZ CBB  sing N N 168 
AV0   CAW CAY  sing N N 169 
AV0   CBB CBD  sing N N 170 
AV0   CAY CBA  sing N N 171 
AV0   CBD CBF  sing N N 172 
AV0   CBA CBC  sing N N 173 
AV0   CBC CBE  sing N N 174 
AV0   CBF CBH  sing N N 175 
AV0   CBE CBG  sing N N 176 
AV0   CBH CBJ  sing N N 177 
AV0   OAJ CBN  sing N N 178 
AV0   OAR CCO  sing N N 179 
AV0   CBG CBI  sing N N 180 
AV0   CBJ CBL  sing N N 181 
AV0   CBL CBR  sing N N 182 
AV0   CBP OAL  sing N N 183 
AV0   CBP CCF  sing N N 184 
AV0   CBN CCD  sing N N 185 
AV0   CCO CCD  sing N N 186 
AV0   CCO CCU  sing N N 187 
AV0   CBI CBK  sing N N 188 
AV0   OAT CCU  sing N N 189 
AV0   CCD OBZ  sing N N 190 
AV0   CCU CCW  sing N N 191 
AV0   CBQ CBK  sing N N 192 
AV0   CBQ CCM  sing N N 193 
AV0   CCF OBX  sing N N 194 
AV0   CCF CCQ  sing N N 195 
AV0   CBR CCM  sing N N 196 
AV0   CBT CCM  sing N N 197 
AV0   CBT OBV  sing N N 198 
AV0   OBX CCJ  sing N N 199 
AV0   CCM CBS  sing N N 200 
AV0   OBZ CCS  sing N N 201 
AV0   OCB CCQ  sing N N 202 
AV0   OCB CCS  sing N N 203 
AV0   CCW CCS  sing N N 204 
AV0   CCW OAV  sing N N 205 
AV0   CCQ CCH  sing N N 206 
AV0   CCJ OBV  sing N N 207 
AV0   CCJ CCL  sing N N 208 
AV0   CBS O1   sing N N 209 
AV0   O1  C1   sing N N 210 
AV0   CCH CCL  sing N N 211 
AV0   CCH OAN  sing N N 212 
AV0   CCL OAP  sing N N 213 
AV0   O2  C2   sing N N 214 
AV0   C1  C2   sing N N 215 
AV0   C1  O5   sing N N 216 
AV0   C2  C3   sing N N 217 
AV0   O5  C5   sing N N 218 
AV0   C3  O3   sing N N 219 
AV0   C3  C4   sing N N 220 
AV0   C5  C4   sing N N 221 
AV0   C5  C6   sing N N 222 
AV0   C4  O4   sing N N 223 
AV0   C6  O6   sing N N 224 
AV0   O4  CCR  sing N N 225 
AV0   CCR OBY  sing N N 226 
AV0   CCR CCV  sing N N 227 
AV0   OBY CCC  sing N N 228 
AV0   OAU CCV  sing N N 229 
AV0   CCV CCT  sing N N 230 
AV0   CCC CBM  sing N N 231 
AV0   CCC CCN  sing N N 232 
AV0   CBM OAI  sing N N 233 
AV0   CCT CCN  sing N N 234 
AV0   CCT OAS  sing N N 235 
AV0   CCN OAQ  sing N N 236 
AV0   C1  H1   sing N N 237 
AV0   C2  H2   sing N N 238 
AV0   O2  H3   sing N N 239 
AV0   C3  H4   sing N N 240 
AV0   O3  H5   sing N N 241 
AV0   C4  H6   sing N N 242 
AV0   C5  H7   sing N N 243 
AV0   C6  H8   sing N N 244 
AV0   C6  H9   sing N N 245 
AV0   O6  H10  sing N N 246 
AV0   CAA H11  sing N N 247 
AV0   CAA H12  sing N N 248 
AV0   CAA H13  sing N N 249 
AV0   CAB H14  sing N N 250 
AV0   CAB H15  sing N N 251 
AV0   CAB H16  sing N N 252 
AV0   OAI H17  sing N N 253 
AV0   OAJ H18  sing N N 254 
AV0   OAL H19  sing N N 255 
AV0   OAN H20  sing N N 256 
AV0   OAP H21  sing N N 257 
AV0   OAQ H22  sing N N 258 
AV0   OAR H23  sing N N 259 
AV0   OAS H24  sing N N 260 
AV0   OAT H25  sing N N 261 
AV0   OAU H26  sing N N 262 
AV0   OAV H27  sing N N 263 
AV0   CAW H28  sing N N 264 
AV0   CAW H29  sing N N 265 
AV0   CAX H30  sing N N 266 
AV0   CAX H31  sing N N 267 
AV0   CAY H32  sing N N 268 
AV0   CAY H33  sing N N 269 
AV0   CAZ H34  sing N N 270 
AV0   CAZ H35  sing N N 271 
AV0   CBA H36  sing N N 272 
AV0   CBA H37  sing N N 273 
AV0   CBB H38  sing N N 274 
AV0   CBB H39  sing N N 275 
AV0   CBC H40  sing N N 276 
AV0   CBC H41  sing N N 277 
AV0   CBD H42  sing N N 278 
AV0   CBD H43  sing N N 279 
AV0   CBE H44  sing N N 280 
AV0   CBE H45  sing N N 281 
AV0   CBF H46  sing N N 282 
AV0   CBF H47  sing N N 283 
AV0   CBG H48  sing N N 284 
AV0   CBG H49  sing N N 285 
AV0   CBH H50  sing N N 286 
AV0   CBH H51  sing N N 287 
AV0   CBI H52  sing N N 288 
AV0   CBI H53  sing N N 289 
AV0   CBJ H54  sing N N 290 
AV0   CBJ H55  sing N N 291 
AV0   CBK H56  sing N N 292 
AV0   CBK H57  sing N N 293 
AV0   CBL H58  sing N N 294 
AV0   CBL H59  sing N N 295 
AV0   CBM H60  sing N N 296 
AV0   CBM H61  sing N N 297 
AV0   CBN H62  sing N N 298 
AV0   CBN H63  sing N N 299 
AV0   CBP H64  sing N N 300 
AV0   CBP H65  sing N N 301 
AV0   CBQ H66  sing N N 302 
AV0   CBQ H67  sing N N 303 
AV0   CBR H68  sing N N 304 
AV0   CBR H69  sing N N 305 
AV0   CBS H70  sing N N 306 
AV0   CBS H71  sing N N 307 
AV0   CBT H72  sing N N 308 
AV0   CBT H73  sing N N 309 
AV0   CCC H74  sing N N 310 
AV0   CCD H75  sing N N 311 
AV0   CCF H76  sing N N 312 
AV0   CCH H77  sing N N 313 
AV0   CCJ H78  sing N N 314 
AV0   CCL H79  sing N N 315 
AV0   CCN H80  sing N N 316 
AV0   CCO H81  sing N N 317 
AV0   CCQ H82  sing N N 318 
AV0   CCR H83  sing N N 319 
AV0   CCS H84  sing N N 320 
AV0   CCT H85  sing N N 321 
AV0   CCU H86  sing N N 322 
AV0   CCV H87  sing N N 323 
AV0   CCW H88  sing N N 324 
CYS   N   CA   sing N N 325 
CYS   N   H    sing N N 326 
CYS   N   H2   sing N N 327 
CYS   CA  C    sing N N 328 
CYS   CA  CB   sing N N 329 
CYS   CA  HA   sing N N 330 
CYS   C   O    doub N N 331 
CYS   C   OXT  sing N N 332 
CYS   CB  SG   sing N N 333 
CYS   CB  HB2  sing N N 334 
CYS   CB  HB3  sing N N 335 
CYS   SG  HG   sing N N 336 
CYS   OXT HXT  sing N N 337 
GLN   N   CA   sing N N 338 
GLN   N   H    sing N N 339 
GLN   N   H2   sing N N 340 
GLN   CA  C    sing N N 341 
GLN   CA  CB   sing N N 342 
GLN   CA  HA   sing N N 343 
GLN   C   O    doub N N 344 
GLN   C   OXT  sing N N 345 
GLN   CB  CG   sing N N 346 
GLN   CB  HB2  sing N N 347 
GLN   CB  HB3  sing N N 348 
GLN   CG  CD   sing N N 349 
GLN   CG  HG2  sing N N 350 
GLN   CG  HG3  sing N N 351 
GLN   CD  OE1  doub N N 352 
GLN   CD  NE2  sing N N 353 
GLN   NE2 HE21 sing N N 354 
GLN   NE2 HE22 sing N N 355 
GLN   OXT HXT  sing N N 356 
GLU   N   CA   sing N N 357 
GLU   N   H    sing N N 358 
GLU   N   H2   sing N N 359 
GLU   CA  C    sing N N 360 
GLU   CA  CB   sing N N 361 
GLU   CA  HA   sing N N 362 
GLU   C   O    doub N N 363 
GLU   C   OXT  sing N N 364 
GLU   CB  CG   sing N N 365 
GLU   CB  HB2  sing N N 366 
GLU   CB  HB3  sing N N 367 
GLU   CG  CD   sing N N 368 
GLU   CG  HG2  sing N N 369 
GLU   CG  HG3  sing N N 370 
GLU   CD  OE1  doub N N 371 
GLU   CD  OE2  sing N N 372 
GLU   OE2 HE2  sing N N 373 
GLU   OXT HXT  sing N N 374 
GLY   N   CA   sing N N 375 
GLY   N   H    sing N N 376 
GLY   N   H2   sing N N 377 
GLY   CA  C    sing N N 378 
GLY   CA  HA2  sing N N 379 
GLY   CA  HA3  sing N N 380 
GLY   C   O    doub N N 381 
GLY   C   OXT  sing N N 382 
GLY   OXT HXT  sing N N 383 
HIS   N   CA   sing N N 384 
HIS   N   H    sing N N 385 
HIS   N   H2   sing N N 386 
HIS   CA  C    sing N N 387 
HIS   CA  CB   sing N N 388 
HIS   CA  HA   sing N N 389 
HIS   C   O    doub N N 390 
HIS   C   OXT  sing N N 391 
HIS   CB  CG   sing N N 392 
HIS   CB  HB2  sing N N 393 
HIS   CB  HB3  sing N N 394 
HIS   CG  ND1  sing Y N 395 
HIS   CG  CD2  doub Y N 396 
HIS   ND1 CE1  doub Y N 397 
HIS   ND1 HD1  sing N N 398 
HIS   CD2 NE2  sing Y N 399 
HIS   CD2 HD2  sing N N 400 
HIS   CE1 NE2  sing Y N 401 
HIS   CE1 HE1  sing N N 402 
HIS   NE2 HE2  sing N N 403 
HIS   OXT HXT  sing N N 404 
ILE   N   CA   sing N N 405 
ILE   N   H    sing N N 406 
ILE   N   H2   sing N N 407 
ILE   CA  C    sing N N 408 
ILE   CA  CB   sing N N 409 
ILE   CA  HA   sing N N 410 
ILE   C   O    doub N N 411 
ILE   C   OXT  sing N N 412 
ILE   CB  CG1  sing N N 413 
ILE   CB  CG2  sing N N 414 
ILE   CB  HB   sing N N 415 
ILE   CG1 CD1  sing N N 416 
ILE   CG1 HG12 sing N N 417 
ILE   CG1 HG13 sing N N 418 
ILE   CG2 HG21 sing N N 419 
ILE   CG2 HG22 sing N N 420 
ILE   CG2 HG23 sing N N 421 
ILE   CD1 HD11 sing N N 422 
ILE   CD1 HD12 sing N N 423 
ILE   CD1 HD13 sing N N 424 
ILE   OXT HXT  sing N N 425 
LEU   N   CA   sing N N 426 
LEU   N   H    sing N N 427 
LEU   N   H2   sing N N 428 
LEU   CA  C    sing N N 429 
LEU   CA  CB   sing N N 430 
LEU   CA  HA   sing N N 431 
LEU   C   O    doub N N 432 
LEU   C   OXT  sing N N 433 
LEU   CB  CG   sing N N 434 
LEU   CB  HB2  sing N N 435 
LEU   CB  HB3  sing N N 436 
LEU   CG  CD1  sing N N 437 
LEU   CG  CD2  sing N N 438 
LEU   CG  HG   sing N N 439 
LEU   CD1 HD11 sing N N 440 
LEU   CD1 HD12 sing N N 441 
LEU   CD1 HD13 sing N N 442 
LEU   CD2 HD21 sing N N 443 
LEU   CD2 HD22 sing N N 444 
LEU   CD2 HD23 sing N N 445 
LEU   OXT HXT  sing N N 446 
LYS   N   CA   sing N N 447 
LYS   N   H    sing N N 448 
LYS   N   H2   sing N N 449 
LYS   CA  C    sing N N 450 
LYS   CA  CB   sing N N 451 
LYS   CA  HA   sing N N 452 
LYS   C   O    doub N N 453 
LYS   C   OXT  sing N N 454 
LYS   CB  CG   sing N N 455 
LYS   CB  HB2  sing N N 456 
LYS   CB  HB3  sing N N 457 
LYS   CG  CD   sing N N 458 
LYS   CG  HG2  sing N N 459 
LYS   CG  HG3  sing N N 460 
LYS   CD  CE   sing N N 461 
LYS   CD  HD2  sing N N 462 
LYS   CD  HD3  sing N N 463 
LYS   CE  NZ   sing N N 464 
LYS   CE  HE2  sing N N 465 
LYS   CE  HE3  sing N N 466 
LYS   NZ  HZ1  sing N N 467 
LYS   NZ  HZ2  sing N N 468 
LYS   NZ  HZ3  sing N N 469 
LYS   OXT HXT  sing N N 470 
MET   N   CA   sing N N 471 
MET   N   H    sing N N 472 
MET   N   H2   sing N N 473 
MET   CA  C    sing N N 474 
MET   CA  CB   sing N N 475 
MET   CA  HA   sing N N 476 
MET   C   O    doub N N 477 
MET   C   OXT  sing N N 478 
MET   CB  CG   sing N N 479 
MET   CB  HB2  sing N N 480 
MET   CB  HB3  sing N N 481 
MET   CG  SD   sing N N 482 
MET   CG  HG2  sing N N 483 
MET   CG  HG3  sing N N 484 
MET   SD  CE   sing N N 485 
MET   CE  HE1  sing N N 486 
MET   CE  HE2  sing N N 487 
MET   CE  HE3  sing N N 488 
MET   OXT HXT  sing N N 489 
PHE   N   CA   sing N N 490 
PHE   N   H    sing N N 491 
PHE   N   H2   sing N N 492 
PHE   CA  C    sing N N 493 
PHE   CA  CB   sing N N 494 
PHE   CA  HA   sing N N 495 
PHE   C   O    doub N N 496 
PHE   C   OXT  sing N N 497 
PHE   CB  CG   sing N N 498 
PHE   CB  HB2  sing N N 499 
PHE   CB  HB3  sing N N 500 
PHE   CG  CD1  doub Y N 501 
PHE   CG  CD2  sing Y N 502 
PHE   CD1 CE1  sing Y N 503 
PHE   CD1 HD1  sing N N 504 
PHE   CD2 CE2  doub Y N 505 
PHE   CD2 HD2  sing N N 506 
PHE   CE1 CZ   doub Y N 507 
PHE   CE1 HE1  sing N N 508 
PHE   CE2 CZ   sing Y N 509 
PHE   CE2 HE2  sing N N 510 
PHE   CZ  HZ   sing N N 511 
PHE   OXT HXT  sing N N 512 
PRO   N   CA   sing N N 513 
PRO   N   CD   sing N N 514 
PRO   N   H    sing N N 515 
PRO   CA  C    sing N N 516 
PRO   CA  CB   sing N N 517 
PRO   CA  HA   sing N N 518 
PRO   C   O    doub N N 519 
PRO   C   OXT  sing N N 520 
PRO   CB  CG   sing N N 521 
PRO   CB  HB2  sing N N 522 
PRO   CB  HB3  sing N N 523 
PRO   CG  CD   sing N N 524 
PRO   CG  HG2  sing N N 525 
PRO   CG  HG3  sing N N 526 
PRO   CD  HD2  sing N N 527 
PRO   CD  HD3  sing N N 528 
PRO   OXT HXT  sing N N 529 
SER   N   CA   sing N N 530 
SER   N   H    sing N N 531 
SER   N   H2   sing N N 532 
SER   CA  C    sing N N 533 
SER   CA  CB   sing N N 534 
SER   CA  HA   sing N N 535 
SER   C   O    doub N N 536 
SER   C   OXT  sing N N 537 
SER   CB  OG   sing N N 538 
SER   CB  HB2  sing N N 539 
SER   CB  HB3  sing N N 540 
SER   OG  HG   sing N N 541 
SER   OXT HXT  sing N N 542 
THR   N   CA   sing N N 543 
THR   N   H    sing N N 544 
THR   N   H2   sing N N 545 
THR   CA  C    sing N N 546 
THR   CA  CB   sing N N 547 
THR   CA  HA   sing N N 548 
THR   C   O    doub N N 549 
THR   C   OXT  sing N N 550 
THR   CB  OG1  sing N N 551 
THR   CB  CG2  sing N N 552 
THR   CB  HB   sing N N 553 
THR   OG1 HG1  sing N N 554 
THR   CG2 HG21 sing N N 555 
THR   CG2 HG22 sing N N 556 
THR   CG2 HG23 sing N N 557 
THR   OXT HXT  sing N N 558 
TRP   N   CA   sing N N 559 
TRP   N   H    sing N N 560 
TRP   N   H2   sing N N 561 
TRP   CA  C    sing N N 562 
TRP   CA  CB   sing N N 563 
TRP   CA  HA   sing N N 564 
TRP   C   O    doub N N 565 
TRP   C   OXT  sing N N 566 
TRP   CB  CG   sing N N 567 
TRP   CB  HB2  sing N N 568 
TRP   CB  HB3  sing N N 569 
TRP   CG  CD1  doub Y N 570 
TRP   CG  CD2  sing Y N 571 
TRP   CD1 NE1  sing Y N 572 
TRP   CD1 HD1  sing N N 573 
TRP   CD2 CE2  doub Y N 574 
TRP   CD2 CE3  sing Y N 575 
TRP   NE1 CE2  sing Y N 576 
TRP   NE1 HE1  sing N N 577 
TRP   CE2 CZ2  sing Y N 578 
TRP   CE3 CZ3  doub Y N 579 
TRP   CE3 HE3  sing N N 580 
TRP   CZ2 CH2  doub Y N 581 
TRP   CZ2 HZ2  sing N N 582 
TRP   CZ3 CH2  sing Y N 583 
TRP   CZ3 HZ3  sing N N 584 
TRP   CH2 HH2  sing N N 585 
TRP   OXT HXT  sing N N 586 
TYR   N   CA   sing N N 587 
TYR   N   H    sing N N 588 
TYR   N   H2   sing N N 589 
TYR   CA  C    sing N N 590 
TYR   CA  CB   sing N N 591 
TYR   CA  HA   sing N N 592 
TYR   C   O    doub N N 593 
TYR   C   OXT  sing N N 594 
TYR   CB  CG   sing N N 595 
TYR   CB  HB2  sing N N 596 
TYR   CB  HB3  sing N N 597 
TYR   CG  CD1  doub Y N 598 
TYR   CG  CD2  sing Y N 599 
TYR   CD1 CE1  sing Y N 600 
TYR   CD1 HD1  sing N N 601 
TYR   CD2 CE2  doub Y N 602 
TYR   CD2 HD2  sing N N 603 
TYR   CE1 CZ   doub Y N 604 
TYR   CE1 HE1  sing N N 605 
TYR   CE2 CZ   sing Y N 606 
TYR   CE2 HE2  sing N N 607 
TYR   CZ  OH   sing N N 608 
TYR   OH  HH   sing N N 609 
TYR   OXT HXT  sing N N 610 
VAL   N   CA   sing N N 611 
VAL   N   H    sing N N 612 
VAL   N   H2   sing N N 613 
VAL   CA  C    sing N N 614 
VAL   CA  CB   sing N N 615 
VAL   CA  HA   sing N N 616 
VAL   C   O    doub N N 617 
VAL   C   OXT  sing N N 618 
VAL   CB  CG1  sing N N 619 
VAL   CB  CG2  sing N N 620 
VAL   CB  HB   sing N N 621 
VAL   CG1 HG11 sing N N 622 
VAL   CG1 HG12 sing N N 623 
VAL   CG1 HG13 sing N N 624 
VAL   CG2 HG21 sing N N 625 
VAL   CG2 HG22 sing N N 626 
VAL   CG2 HG23 sing N N 627 
VAL   OXT HXT  sing N N 628 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           'Grant 32122041' 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        AV0 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   AV0 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 1 21 1' 
_space_group.name_Hall        'P 2yb' 
_space_group.IT_number        4 
_space_group.crystal_system   monoclinic 
_space_group.id               1 
# 
_atom_sites.entry_id                    8W1V 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.013572 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.004165 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.006813 
_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]   0.011391 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 6.96715 ?       ? ? 11.43723 ?        ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 7.96527 ?       ? ? 9.05267  ?        ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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   . ASP   A 1 53  ? -69.16900 8.61100   -22.97200 1.000 95.81156  ? 29   ASP   A N   1 
ATOM   2    C CA  . ASP   A 1 53  ? -70.23300 8.63900   -21.97600 1.000 104.79421 ? 29   ASP   A CA  1 
ATOM   3    C C   . ASP   A 1 53  ? -70.07900 9.83600   -21.04500 1.000 106.28790 ? 29   ASP   A C   1 
ATOM   4    O O   . ASP   A 1 53  ? -69.08400 9.96000   -20.32800 1.000 104.36519 ? 29   ASP   A O   1 
ATOM   5    C CB  . ASP   A 1 53  ? -70.25000 7.34000   -21.16600 1.000 95.44056  ? 29   ASP   A CB  1 
ATOM   6    N N   . GLU   A 1 54  ? -71.08200 10.71200  -21.05700 1.000 106.63761 ? 30   GLU   A N   1 
ATOM   7    C CA  . GLU   A 1 54  ? -71.08400 11.91800  -20.23900 1.000 99.42974  ? 30   GLU   A CA  1 
ATOM   8    C C   . GLU   A 1 54  ? -71.33300 11.61700  -18.75900 1.000 97.76847  ? 30   GLU   A C   1 
ATOM   9    O O   . GLU   A 1 54  ? -71.37100 12.54400  -17.94200 1.000 98.33712  ? 30   GLU   A O   1 
ATOM   10   C CB  . GLU   A 1 54  ? -72.13100 12.89100  -20.80800 1.000 101.76647 ? 30   GLU   A CB  1 
ATOM   11   C CG  . GLU   A 1 54  ? -72.21200 14.26200  -20.15100 1.000 103.26602 ? 30   GLU   A CG  1 
ATOM   12   C CD  . GLU   A 1 54  ? -73.62400 14.80000  -20.04300 1.000 111.60150 ? 30   GLU   A CD  1 
ATOM   13   O OE1 . GLU   A 1 54  ? -74.48800 14.10300  -19.47000 1.000 112.66848 ? 30   GLU   A OE1 1 
ATOM   14   O OE2 . GLU   A 1 54  ? -73.86900 15.92100  -20.53200 1.000 111.08521 ? 30   GLU   A OE2 1 
ATOM   15   N N   . VAL   A 1 55  ? -71.47400 10.34000  -18.38900 1.000 98.04409  ? 31   VAL   A N   1 
ATOM   16   C CA  . VAL   A 1 55  ? -71.69000 9.98300   -16.98900 1.000 98.17994  ? 31   VAL   A CA  1 
ATOM   17   C C   . VAL   A 1 55  ? -70.46800 10.32900  -16.14500 1.000 95.66769  ? 31   VAL   A C   1 
ATOM   18   O O   . VAL   A 1 55  ? -70.59700 10.80800  -15.01200 1.000 86.28218  ? 31   VAL   A O   1 
ATOM   19   C CB  . VAL   A 1 55  ? -72.06400 8.49200   -16.87000 1.000 96.53784  ? 31   VAL   A CB  1 
ATOM   20   C CG1 . VAL   A 1 55  ? -70.99200 7.60800   -17.50500 1.000 93.41824  ? 31   VAL   A CG1 1 
ATOM   21   C CG2 . VAL   A 1 55  ? -72.27400 8.11000   -15.40900 1.000 82.74417  ? 31   VAL   A CG2 1 
ATOM   22   N N   . TRP   A 1 56  ? -69.26800 10.10700  -16.68600 1.000 96.36210  ? 32   TRP   A N   1 
ATOM   23   C CA  . TRP   A 1 56  ? -68.04400 10.39300  -15.94300 1.000 90.36552  ? 32   TRP   A CA  1 
ATOM   24   C C   . TRP   A 1 56  ? -67.86800 11.88900  -15.70600 1.000 87.45191  ? 32   TRP   A C   1 
ATOM   25   O O   . TRP   A 1 56  ? -67.48300 12.30500  -14.60700 1.000 82.27224  ? 32   TRP   A O   1 
ATOM   26   C CB  . TRP   A 1 56  ? -66.84300 9.81500   -16.69300 1.000 92.63620  ? 32   TRP   A CB  1 
ATOM   27   C CG  . TRP   A 1 56  ? -65.50400 10.33000  -16.24000 1.000 92.15090  ? 32   TRP   A CG  1 
ATOM   28   C CD1 . TRP   A 1 56  ? -64.93900 10.18300  -15.00500 1.000 89.49311  ? 32   TRP   A CD1 1 
ATOM   29   C CD2 . TRP   A 1 56  ? -64.55700 11.06500  -17.03000 1.000 92.34826  ? 32   TRP   A CD2 1 
ATOM   30   N NE1 . TRP   A 1 56  ? -63.70300 10.78700  -14.97600 1.000 92.27954  ? 32   TRP   A NE1 1 
ATOM   31   C CE2 . TRP   A 1 56  ? -63.44600 11.33500  -16.20700 1.000 92.77030  ? 32   TRP   A CE2 1 
ATOM   32   C CE3 . TRP   A 1 56  ? -64.54400 11.52200  -18.35200 1.000 91.59349  ? 32   TRP   A CE3 1 
ATOM   33   C CZ2 . TRP   A 1 56  ? -62.33300 12.04300  -16.66300 1.000 87.28148  ? 32   TRP   A CZ2 1 
ATOM   34   C CZ3 . TRP   A 1 56  ? -63.44000 12.22400  -18.80200 1.000 90.75722  ? 32   TRP   A CZ3 1 
ATOM   35   C CH2 . TRP   A 1 56  ? -62.35100 12.47800  -17.96000 1.000 91.09403  ? 32   TRP   A CH2 1 
ATOM   36   N N   . VAL   A 1 57  ? -68.16400 12.71300  -16.71600 1.000 89.71761  ? 33   VAL   A N   1 
ATOM   37   C CA  . VAL   A 1 57  ? -67.83300 14.13400  -16.63400 1.000 84.92647  ? 33   VAL   A CA  1 
ATOM   38   C C   . VAL   A 1 57  ? -68.69300 14.83600  -15.58400 1.000 84.59829  ? 33   VAL   A C   1 
ATOM   39   O O   . VAL   A 1 57  ? -68.21100 15.72200  -14.86800 1.000 87.28415  ? 33   VAL   A O   1 
ATOM   40   C CB  . VAL   A 1 57  ? -67.94300 14.79500  -18.02500 1.000 83.28534  ? 33   VAL   A CB  1 
ATOM   41   C CG1 . VAL   A 1 57  ? -69.37700 15.14600  -18.37400 1.000 86.07487  ? 33   VAL   A CG1 1 
ATOM   42   C CG2 . VAL   A 1 57  ? -67.06100 16.03200  -18.09900 1.000 81.01397  ? 33   VAL   A CG2 1 
ATOM   43   N N   . VAL   A 1 58  ? -69.96300 14.44400  -15.45100 1.000 82.20049  ? 34   VAL   A N   1 
ATOM   44   C CA  . VAL   A 1 58  ? -70.79900 15.06500  -14.42900 1.000 84.04014  ? 34   VAL   A CA  1 
ATOM   45   C C   . VAL   A 1 58  ? -70.54800 14.44800  -13.06000 1.000 80.66439  ? 34   VAL   A C   1 
ATOM   46   O O   . VAL   A 1 58  ? -70.77300 15.10900  -12.03700 1.000 74.61636  ? 34   VAL   A O   1 
ATOM   47   C CB  . VAL   A 1 58  ? -72.28900 14.98300  -14.80800 1.000 86.88076  ? 34   VAL   A CB  1 
ATOM   48   C CG1 . VAL   A 1 58  ? -72.81700 13.56500  -14.64200 1.000 87.49839  ? 34   VAL   A CG1 1 
ATOM   49   C CG2 . VAL   A 1 58  ? -73.11000 15.97500  -13.98800 1.000 81.89648  ? 34   VAL   A CG2 1 
ATOM   50   N N   . GLY   A 1 59  ? -70.06700 13.20400  -13.01300 1.000 82.65327  ? 35   GLY   A N   1 
ATOM   51   C CA  . GLY   A 1 59  ? -69.70200 12.61200  -11.73900 1.000 69.86075  ? 35   GLY   A CA  1 
ATOM   52   C C   . GLY   A 1 59  ? -68.50700 13.29600  -11.10500 1.000 76.31805  ? 35   GLY   A C   1 
ATOM   53   O O   . GLY   A 1 59  ? -68.51200 13.58400  -9.90500  1.000 78.43744  ? 35   GLY   A O   1 
ATOM   54   N N   . MET   A 1 60  ? -67.46900 13.57500  -11.89800 1.000 77.21979  ? 36   MET   A N   1 
ATOM   55   C CA  . MET   A 1 60  ? -66.30800 14.27200  -11.35500 1.000 72.36409  ? 36   MET   A CA  1 
ATOM   56   C C   . MET   A 1 60  ? -66.62200 15.72900  -11.04500 1.000 74.10027  ? 36   MET   A C   1 
ATOM   57   O O   . MET   A 1 60  ? -66.09100 16.27900  -10.07400 1.000 75.43844  ? 36   MET   A O   1 
ATOM   58   C CB  . MET   A 1 60  ? -65.12800 14.16700  -12.32100 1.000 67.74280  ? 36   MET   A CB  1 
ATOM   59   C CG  . MET   A 1 60  ? -64.54600 12.76100  -12.44500 1.000 74.09151  ? 36   MET   A CG  1 
ATOM   60   S SD  . MET   A 1 60  ? -63.98900 12.04800  -10.87700 1.000 91.95719  ? 36   MET   A SD  1 
ATOM   61   C CE  . MET   A 1 60  ? -65.39200 11.04900  -10.37800 1.000 74.94933  ? 36   MET   A CE  1 
ATOM   62   N N   . GLY   A 1 61  ? -67.47900 16.36600  -11.84900 1.000 75.90229  ? 37   GLY   A N   1 
ATOM   63   C CA  . GLY   A 1 61  ? -67.88000 17.73400  -11.55400 1.000 75.64345  ? 37   GLY   A CA  1 
ATOM   64   C C   . GLY   A 1 61  ? -68.50400 17.87500  -10.17900 1.000 65.91763  ? 37   GLY   A C   1 
ATOM   65   O O   . GLY   A 1 61  ? -68.20900 18.82400  -9.44600  1.000 60.28784  ? 37   GLY   A O   1 
ATOM   66   N N   . ILE   A 1 62  ? -69.36800 16.92900  -9.80500  1.000 63.69579  ? 38   ILE   A N   1 
ATOM   67   C CA  . ILE   A 1 62  ? -69.91800 16.91900  -8.45200  1.000 70.31965  ? 38   ILE   A CA  1 
ATOM   68   C C   . ILE   A 1 62  ? -68.81200 16.67200  -7.43400  1.000 66.16701  ? 38   ILE   A C   1 
ATOM   69   O O   . ILE   A 1 62  ? -68.69800 17.38300  -6.42800  1.000 58.64546  ? 38   ILE   A O   1 
ATOM   70   C CB  . ILE   A 1 62  ? -71.03800 15.86900  -8.33300  1.000 61.13861  ? 38   ILE   A CB  1 
ATOM   71   C CG1 . ILE   A 1 62  ? -72.20400 16.21600  -9.26000  1.000 58.41742  ? 38   ILE   A CG1 1 
ATOM   72   C CG2 . ILE   A 1 62  ? -71.51400 15.76000  -6.89600  1.000 55.41959  ? 38   ILE   A CG2 1 
ATOM   73   C CD1 . ILE   A 1 62  ? -72.80300 17.58100  -9.00200  1.000 55.91706  ? 38   ILE   A CD1 1 
ATOM   74   N N   . VAL   A 1 63  ? -67.97500 15.66200  -7.68600  1.000 61.96069  ? 39   VAL   A N   1 
ATOM   75   C CA  . VAL   A 1 63  ? -66.89900 15.32900  -6.75600  1.000 60.72754  ? 39   VAL   A CA  1 
ATOM   76   C C   . VAL   A 1 63  ? -65.91500 16.48600  -6.63100  1.000 60.37034  ? 39   VAL   A C   1 
ATOM   77   O O   . VAL   A 1 63  ? -65.40600 16.77200  -5.54000  1.000 58.77902  ? 39   VAL   A O   1 
ATOM   78   C CB  . VAL   A 1 63  ? -66.19600 14.03200  -7.19700  1.000 63.15287  ? 39   VAL   A CB  1 
ATOM   79   C CG1 . VAL   A 1 63  ? -64.99800 13.74300  -6.30600  1.000 57.64204  ? 39   VAL   A CG1 1 
ATOM   80   C CG2 . VAL   A 1 63  ? -67.17200 12.86800  -7.16500  1.000 61.48969  ? 39   VAL   A CG2 1 
ATOM   81   N N   . MET   A 1 64  ? -65.63200 17.17200  -7.73900  1.000 57.94674  ? 40   MET   A N   1 
ATOM   82   C CA  . MET   A 1 64  ? -64.69600 18.29000  -7.68200  1.000 52.47060  ? 40   MET   A CA  1 
ATOM   83   C C   . MET   A 1 64  ? -65.31900 19.50100  -7.00600  1.000 52.77665  ? 40   MET   A C   1 
ATOM   84   O O   . MET   A 1 64  ? -64.63300 20.23400  -6.28400  1.000 48.99495  ? 40   MET   A O   1 
ATOM   85   C CB  . MET   A 1 64  ? -64.21500 18.64900  -9.08500  1.000 56.97418  ? 40   MET   A CB  1 
ATOM   86   C CG  . MET   A 1 64  ? -63.25100 17.64400  -9.67000  1.000 64.35494  ? 40   MET   A CG  1 
ATOM   87   S SD  . MET   A 1 64  ? -62.83500 18.01400  -11.37600 1.000 67.14908  ? 40   MET   A SD  1 
ATOM   88   C CE  . MET   A 1 64  ? -61.69200 16.68300  -11.72400 1.000 67.56895  ? 40   MET   A CE  1 
ATOM   89   N N   . SER   A 1 65  ? -66.61400 19.73200  -7.23200  1.000 56.21129  ? 41   SER   A N   1 
ATOM   90   C CA  . SER   A 1 65  ? -67.28000 20.86400  -6.59700  1.000 52.84201  ? 41   SER   A CA  1 
ATOM   91   C C   . SER   A 1 65  ? -67.22100 20.75400  -5.08000  1.000 51.72193  ? 41   SER   A C   1 
ATOM   92   O O   . SER   A 1 65  ? -66.95400 21.74300  -4.38800  1.000 47.30074  ? 41   SER   A O   1 
ATOM   93   C CB  . SER   A 1 65  ? -68.72800 20.95500  -7.07200  1.000 52.61433  ? 41   SER   A CB  1 
ATOM   94   O OG  . SER   A 1 65  ? -68.82200 21.73800  -8.24700  1.000 63.92688  ? 41   SER   A OG  1 
ATOM   95   N N   . LEU   A 1 66  ? -67.45900 19.55200  -4.54700  1.000 53.88864  ? 42   LEU   A N   1 
ATOM   96   C CA  . LEU   A 1 66  ? -67.39600 19.35300  -3.10300  1.000 45.91775  ? 42   LEU   A CA  1 
ATOM   97   C C   . LEU   A 1 66  ? -65.98300 19.56200  -2.57800  1.000 45.09487  ? 42   LEU   A C   1 
ATOM   98   O O   . LEU   A 1 66  ? -65.79600 20.14500  -1.50400  1.000 47.76704  ? 42   LEU   A O   1 
ATOM   99   C CB  . LEU   A 1 66  ? -67.89500 17.95500  -2.74600  1.000 41.93815  ? 42   LEU   A CB  1 
ATOM   100  C CG  . LEU   A 1 66  ? -69.32100 17.64100  -3.18900  1.000 47.16499  ? 42   LEU   A CG  1 
ATOM   101  C CD1 . LEU   A 1 66  ? -69.74700 16.26900  -2.68900  1.000 39.70559  ? 42   LEU   A CD1 1 
ATOM   102  C CD2 . LEU   A 1 66  ? -70.28300 18.72900  -2.72500  1.000 40.18292  ? 42   LEU   A CD2 1 
ATOM   103  N N   . ILE   A 1 67  ? -64.97900 19.08900  -3.31800  1.000 45.75553  ? 43   ILE   A N   1 
ATOM   104  C CA  . ILE   A 1 67  ? -63.59200 19.29700  -2.91100  1.000 45.94980  ? 43   ILE   A CA  1 
ATOM   105  C C   . ILE   A 1 67  ? -63.30400 20.78500  -2.76400  1.000 44.85146  ? 43   ILE   A C   1 
ATOM   106  O O   . ILE   A 1 67  ? -62.77200 21.23400  -1.74300  1.000 43.67967  ? 43   ILE   A O   1 
ATOM   107  C CB  . ILE   A 1 67  ? -62.63000 18.63100  -3.91100  1.000 43.58346  ? 43   ILE   A CB  1 
ATOM   108  C CG1 . ILE   A 1 67  ? -62.72100 17.10800  -3.80100  1.000 45.51000  ? 43   ILE   A CG1 1 
ATOM   109  C CG2 . ILE   A 1 67  ? -61.20600 19.10600  -3.67400  1.000 42.32730  ? 43   ILE   A CG2 1 
ATOM   110  C CD1 . ILE   A 1 67  ? -61.90200 16.36900  -4.84100  1.000 54.55753  ? 43   ILE   A CD1 1 
ATOM   111  N N   . VAL   A 1 68  ? -63.65800 21.57400  -3.78300  1.000 46.73036  ? 44   VAL   A N   1 
ATOM   112  C CA  . VAL   A 1 68  ? -63.55300 23.02500  -3.66100  1.000 47.36421  ? 44   VAL   A CA  1 
ATOM   113  C C   . VAL   A 1 68  ? -64.41300 23.51500  -2.50400  1.000 41.84273  ? 44   VAL   A C   1 
ATOM   114  O O   . VAL   A 1 68  ? -63.99800 24.37900  -1.72200  1.000 39.54750  ? 44   VAL   A O   1 
ATOM   115  C CB  . VAL   A 1 68  ? -63.93900 23.70900  -4.98800  1.000 43.51464  ? 44   VAL   A CB  1 
ATOM   116  C CG1 . VAL   A 1 68  ? -64.25400 25.18600  -4.76500  1.000 35.42673  ? 44   VAL   A CG1 1 
ATOM   117  C CG2 . VAL   A 1 68  ? -62.82700 23.54800  -6.01300  1.000 41.58947  ? 44   VAL   A CG2 1 
ATOM   118  N N   . LEU   A 1 69  ? -65.61400 22.94800  -2.36200  1.000 46.32260  ? 45   LEU   A N   1 
ATOM   119  C CA  . LEU   A 1 69  ? -66.52200 23.37400  -1.30100  1.000 47.62390  ? 45   LEU   A CA  1 
ATOM   120  C C   . LEU   A 1 69  ? -65.95000 23.06600  0.07900   1.000 42.15282  ? 45   LEU   A C   1 
ATOM   121  O O   . LEU   A 1 69  ? -66.01500 23.90500  0.98400   1.000 40.82277  ? 45   LEU   A O   1 
ATOM   122  C CB  . LEU   A 1 69  ? -67.88300 22.70200  -1.48400  1.000 49.85811  ? 45   LEU   A CB  1 
ATOM   123  C CG  . LEU   A 1 69  ? -69.09300 23.41000  -0.87800  1.000 57.03357  ? 45   LEU   A CG  1 
ATOM   124  C CD1 . LEU   A 1 69  ? -69.24100 24.79700  -1.47800  1.000 59.03828  ? 45   LEU   A CD1 1 
ATOM   125  C CD2 . LEU   A 1 69  ? -70.34800 22.58900  -1.11600  1.000 56.41076  ? 45   LEU   A CD2 1 
ATOM   126  N N   . ALA   A 1 70  ? -65.37700 21.87400  0.25500   1.000 36.76580  ? 46   ALA   A N   1 
ATOM   127  C CA  . ALA   A 1 70  ? -64.76300 21.53200  1.53200   1.000 28.97604  ? 46   ALA   A CA  1 
ATOM   128  C C   . ALA   A 1 70  ? -63.62600 22.48900  1.86900   1.000 34.31253  ? 46   ALA   A C   1 
ATOM   129  O O   . ALA   A 1 70  ? -63.53200 22.98200  2.99800   1.000 37.70314  ? 46   ALA   A O   1 
ATOM   130  C CB  . ALA   A 1 70  ? -64.26500 20.08700  1.50400   1.000 24.18724  ? 46   ALA   A CB  1 
ATOM   131  N N   . ILE   A 1 71  ? -62.75800 22.77500  0.89200   1.000 37.42557  ? 47   ILE   A N   1 
ATOM   132  C CA  . ILE   A 1 71  ? -61.57900 23.60500  1.14400   1.000 37.32232  ? 47   ILE   A CA  1 
ATOM   133  C C   . ILE   A 1 71  ? -61.98800 24.98300  1.64700   1.000 37.34868  ? 47   ILE   A C   1 
ATOM   134  O O   . ILE   A 1 71  ? -61.47800 25.47000  2.66300   1.000 42.99155  ? 47   ILE   A O   1 
ATOM   135  C CB  . ILE   A 1 71  ? -60.71200 23.71500  -0.12300  1.000 39.16788  ? 47   ILE   A CB  1 
ATOM   136  C CG1 . ILE   A 1 71  ? -60.10000 22.36300  -0.49400  1.000 44.25095  ? 47   ILE   A CG1 1 
ATOM   137  C CG2 . ILE   A 1 71  ? -59.62600 24.76000  0.06800   1.000 36.71562  ? 47   ILE   A CG2 1 
ATOM   138  C CD1 . ILE   A 1 71  ? -59.43400 22.35800  -1.86500  1.000 35.77015  ? 47   ILE   A CD1 1 
ATOM   139  N N   . VAL   A 1 72  ? -62.90600 25.63900  0.93600   1.000 35.79619  ? 48   VAL   A N   1 
ATOM   140  C CA  . VAL   A 1 72  ? -63.29500 26.99400  1.31000   1.000 38.49738  ? 48   VAL   A CA  1 
ATOM   141  C C   . VAL   A 1 72  ? -64.01600 27.00000  2.65500   1.000 40.12198  ? 48   VAL   A C   1 
ATOM   142  O O   . VAL   A 1 72  ? -63.80800 27.89800  3.47900   1.000 36.91126  ? 48   VAL   A O   1 
ATOM   143  C CB  . VAL   A 1 72  ? -64.14600 27.62900  0.19400   1.000 34.76135  ? 48   VAL   A CB  1 
ATOM   144  C CG1 . VAL   A 1 72  ? -64.61000 29.01500  0.59300   1.000 28.43982  ? 48   VAL   A CG1 1 
ATOM   145  C CG2 . VAL   A 1 72  ? -63.33100 27.71200  -1.08400  1.000 35.08626  ? 48   VAL   A CG2 1 
ATOM   146  N N   . PHE   A 1 73  ? -64.84900 25.98900  2.91500   1.000 39.93684  ? 49   PHE   A N   1 
ATOM   147  C CA  . PHE   A 1 73  ? -65.61900 25.96200  4.15600   1.000 33.15203  ? 49   PHE   A CA  1 
ATOM   148  C C   . PHE   A 1 73  ? -64.70200 25.84300  5.36700   1.000 38.42552  ? 49   PHE   A C   1 
ATOM   149  O O   . PHE   A 1 73  ? -64.65200 26.73800  6.22000   1.000 39.15378  ? 49   PHE   A O   1 
ATOM   150  C CB  . PHE   A 1 73  ? -66.62800 24.81300  4.11800   1.000 33.50633  ? 49   PHE   A CB  1 
ATOM   151  C CG  . PHE   A 1 73  ? -67.39900 24.63000  5.39700   1.000 36.32130  ? 49   PHE   A CG  1 
ATOM   152  C CD1 . PHE   A 1 73  ? -68.60100 25.29200  5.59400   1.000 34.31616  ? 49   PHE   A CD1 1 
ATOM   153  C CD2 . PHE   A 1 73  ? -66.94300 23.77000  6.38900   1.000 42.91951  ? 49   PHE   A CD2 1 
ATOM   154  C CE1 . PHE   A 1 73  ? -69.32300 25.12100  6.76700   1.000 35.08595  ? 49   PHE   A CE1 1 
ATOM   155  C CE2 . PHE   A 1 73  ? -67.66100 23.59500  7.56200   1.000 43.24652  ? 49   PHE   A CE2 1 
ATOM   156  C CZ  . PHE   A 1 73  ? -68.85400 24.27000  7.74800   1.000 37.91275  ? 49   PHE   A CZ  1 
ATOM   157  N N   . GLY   A 1 74  ? -63.95900 24.73800  5.45400   1.000 37.60640  ? 50   GLY   A N   1 
ATOM   158  C CA  . GLY   A 1 74  ? -63.13600 24.47300  6.62000   1.000 32.75127  ? 50   GLY   A CA  1 
ATOM   159  C C   . GLY   A 1 74  ? -62.06000 25.50700  6.88600   1.000 33.73427  ? 50   GLY   A C   1 
ATOM   160  O O   . GLY   A 1 74  ? -61.55300 25.58100  8.00800   1.000 35.15931  ? 50   GLY   A O   1 
ATOM   161  N N   . ASN   A 1 75  ? -61.69000 26.30500  5.88500   1.000 34.34781  ? 51   ASN   A N   1 
ATOM   162  C CA  . ASN   A 1 75  ? -60.64500 27.30000  6.08300   1.000 35.04835  ? 51   ASN   A CA  1 
ATOM   163  C C   . ASN   A 1 75  ? -61.18800 28.68400  6.40400   1.000 36.29392  ? 51   ASN   A C   1 
ATOM   164  O O   . ASN   A 1 75  ? -60.47500 29.48100  7.02300   1.000 31.32127  ? 51   ASN   A O   1 
ATOM   165  C CB  . ASN   A 1 75  ? -59.73400 27.37200  4.85300   1.000 35.84826  ? 51   ASN   A CB  1 
ATOM   166  C CG  . ASN   A 1 75  ? -58.65700 26.30100  4.86800   1.000 41.97752  ? 51   ASN   A CG  1 
ATOM   167  O OD1 . ASN   A 1 75  ? -57.76400 26.31100  5.71800   1.000 45.17648  ? 51   ASN   A OD1 1 
ATOM   168  N ND2 . ASN   A 1 75  ? -58.74100 25.36400  3.93000   1.000 39.83686  ? 51   ASN   A ND2 1 
ATOM   169  N N   . VAL   A 1 76  ? -62.42200 28.99200  5.99700   1.000 41.98172  ? 52   VAL   A N   1 
ATOM   170  C CA  . VAL   A 1 76  ? -63.10600 30.15200  6.56100   1.000 37.70523  ? 52   VAL   A CA  1 
ATOM   171  C C   . VAL   A 1 76  ? -63.44100 29.88900  8.02000   1.000 30.43625  ? 52   VAL   A C   1 
ATOM   172  O O   . VAL   A 1 76  ? -63.40500 30.80300  8.85400   1.000 26.88636  ? 52   VAL   A O   1 
ATOM   173  C CB  . VAL   A 1 76  ? -64.36700 30.49100  5.74100   1.000 31.13712  ? 52   VAL   A CB  1 
ATOM   174  C CG1 . VAL   A 1 76  ? -65.12500 31.63300  6.37800   1.000 26.36285  ? 52   VAL   A CG1 1 
ATOM   175  C CG2 . VAL   A 1 76  ? -63.98400 30.86800  4.32500   1.000 33.62516  ? 52   VAL   A CG2 1 
ATOM   176  N N   . LEU   A 1 77  ? -63.75100 28.63500  8.35300   1.000 34.75885  ? 53   LEU   A N   1 
ATOM   177  C CA  . LEU   A 1 77  ? -64.00500 28.25700  9.73800   1.000 36.56670  ? 53   LEU   A CA  1 
ATOM   178  C C   . LEU   A 1 77  ? -62.76800 28.46800  10.60500  1.000 30.80891  ? 53   LEU   A C   1 
ATOM   179  O O   . LEU   A 1 77  ? -62.86500 29.00000  11.71600  1.000 33.59178  ? 53   LEU   A O   1 
ATOM   180  C CB  . LEU   A 1 77  ? -64.46600 26.80000  9.78100   1.000 33.87829  ? 53   LEU   A CB  1 
ATOM   181  C CG  . LEU   A 1 77  ? -64.93100 26.16100  11.08300  1.000 38.73975  ? 53   LEU   A CG  1 
ATOM   182  C CD1 . LEU   A 1 77  ? -66.04200 26.97700  11.71300  1.000 41.61375  ? 53   LEU   A CD1 1 
ATOM   183  C CD2 . LEU   A 1 77  ? -65.40400 24.74300  10.79700  1.000 38.64571  ? 53   LEU   A CD2 1 
ATOM   184  N N   . VAL   A 1 78  ? -61.59400 28.07300  10.10600  1.000 30.72138  ? 54   VAL   A N   1 
ATOM   185  C CA  . VAL   A 1 78  ? -60.36100 28.22400  10.87600  1.000 26.36587  ? 54   VAL   A CA  1 
ATOM   186  C C   . VAL   A 1 78  ? -60.04100 29.69900  11.08400  1.000 26.66582  ? 54   VAL   A C   1 
ATOM   187  O O   . VAL   A 1 78  ? -59.80900 30.14800  12.21200  1.000 28.71983  ? 54   VAL   A O   1 
ATOM   188  C CB  . VAL   A 1 78  ? -59.20000 27.48800  10.18100  1.000 26.64053  ? 54   VAL   A CB  1 
ATOM   189  C CG1 . VAL   A 1 78  ? -57.86700 28.05600  10.62500  1.000 22.46401  ? 54   VAL   A CG1 1 
ATOM   190  C CG2 . VAL   A 1 78  ? -59.25800 26.00200  10.47600  1.000 26.43855  ? 54   VAL   A CG2 1 
ATOM   191  N N   . ILE   A 1 79  ? -60.02300 30.47300  9.99600   1.000 27.65886  ? 55   ILE   A N   1 
ATOM   192  C CA  . ILE   A 1 79  ? -59.70500 31.89700  10.08700  1.000 29.83190  ? 55   ILE   A CA  1 
ATOM   193  C C   . ILE   A 1 79  ? -60.66500 32.59900  11.04100  1.000 34.11187  ? 55   ILE   A C   1 
ATOM   194  O O   . ILE   A 1 79  ? -60.27400 33.49900  11.79500  1.000 33.46491  ? 55   ILE   A O   1 
ATOM   195  C CB  . ILE   A 1 79  ? -59.72200 32.53200  8.68300   1.000 26.56249  ? 55   ILE   A CB  1 
ATOM   196  C CG1 . ILE   A 1 79  ? -58.58600 31.96500  7.83200   1.000 26.59215  ? 55   ILE   A CG1 1 
ATOM   197  C CG2 . ILE   A 1 79  ? -59.62100 34.04700  8.76400   1.000 21.35411  ? 55   ILE   A CG2 1 
ATOM   198  C CD1 . ILE   A 1 79  ? -58.70500 32.28800  6.35600   1.000 30.27126  ? 55   ILE   A CD1 1 
ATOM   199  N N   . THR   A 1 80  ? -61.93000 32.17900  11.04100  1.000 37.66580  ? 56   THR   A N   1 
ATOM   200  C CA  . THR   A 1 80  ? -62.92200 32.80500  11.90700  1.000 37.51272  ? 56   THR   A CA  1 
ATOM   201  C C   . THR   A 1 80  ? -62.58100 32.59000  13.37500  1.000 37.36345  ? 56   THR   A C   1 
ATOM   202  O O   . THR   A 1 80  ? -62.58400 33.53700  14.16900  1.000 40.84096  ? 56   THR   A O   1 
ATOM   203  C CB  . THR   A 1 80  ? -64.30800 32.24900  11.58700  1.000 36.55561  ? 56   THR   A CB  1 
ATOM   204  O OG1 . THR   A 1 80  ? -64.60100 32.48900  10.20500  1.000 39.14903  ? 56   THR   A OG1 1 
ATOM   205  C CG2 . THR   A 1 80  ? -65.36700 32.91600  12.44600  1.000 31.92003  ? 56   THR   A CG2 1 
ATOM   206  N N   . ALA   A 1 81  ? -62.26900 31.34700  13.74900  1.000 34.94873  ? 57   ALA   A N   1 
ATOM   207  C CA  . ALA   A 1 81  ? -62.00900 31.02400  15.14800  1.000 34.80904  ? 57   ALA   A CA  1 
ATOM   208  C C   . ALA   A 1 81  ? -60.87800 31.87800  15.71300  1.000 38.60720  ? 57   ALA   A C   1 
ATOM   209  O O   . ALA   A 1 81  ? -61.05200 32.57400  16.72000  1.000 36.92721  ? 57   ALA   A O   1 
ATOM   210  C CB  . ALA   A 1 81  ? -61.69200 29.53400  15.28600  1.000 27.93785  ? 57   ALA   A CB  1 
ATOM   211  N N   . ILE   A 1 82  ? -59.71200 31.85100  15.06100  1.000 36.31264  ? 58   ILE   A N   1 
ATOM   212  C CA  . ILE   A 1 82  ? -58.54800 32.58200  15.55700  1.000 35.05808  ? 58   ILE   A CA  1 
ATOM   213  C C   . ILE   A 1 82  ? -58.83600 34.07600  15.65000  1.000 31.65057  ? 58   ILE   A C   1 
ATOM   214  O O   . ILE   A 1 82  ? -58.27800 34.77200  16.50600  1.000 29.46286  ? 58   ILE   A O   1 
ATOM   215  C CB  . ILE   A 1 82  ? -57.32600 32.27900  14.66300  1.000 34.53389  ? 58   ILE   A CB  1 
ATOM   216  C CG1 . ILE   A 1 82  ? -56.91900 30.81600  14.81300  1.000 30.70151  ? 58   ILE   A CG1 1 
ATOM   217  C CG2 . ILE   A 1 82  ? -56.14000 33.18200  14.98600  1.000 26.89007  ? 58   ILE   A CG2 1 
ATOM   218  C CD1 . ILE   A 1 82  ? -55.97400 30.37000  13.76300  1.000 27.73331  ? 58   ILE   A CD1 1 
ATOM   219  N N   . ALA   A 1 83  ? -59.72200 34.59000  14.79800  1.000 34.56542  ? 59   ALA   A N   1 
ATOM   220  C CA  . ALA   A 1 83  ? -60.03800 36.01300  14.84400  1.000 36.51119  ? 59   ALA   A CA  1 
ATOM   221  C C   . ALA   A 1 83  ? -61.09200 36.33100  15.90200  1.000 43.89655  ? 59   ALA   A C   1 
ATOM   222  O O   . ALA   A 1 83  ? -60.95400 37.32100  16.63000  1.000 48.81973  ? 59   ALA   A O   1 
ATOM   223  C CB  . ALA   A 1 83  ? -60.49800 36.49600  13.46800  1.000 35.77434  ? 59   ALA   A CB  1 
ATOM   224  N N   . LYS   A 1 84  ? -62.14900 35.51500  16.00500  1.000 40.59536  ? 60   LYS   A N   1 
ATOM   225  C CA  . LYS   A 1 84  ? -63.21000 35.80000  16.97000  1.000 47.49708  ? 60   LYS   A CA  1 
ATOM   226  C C   . LYS   A 1 84  ? -62.70500 35.65500  18.40300  1.000 43.79616  ? 60   LYS   A C   1 
ATOM   227  O O   . LYS   A 1 84  ? -62.84800 36.57100  19.22300  1.000 34.11372  ? 60   LYS   A O   1 
ATOM   228  C CB  . LYS   A 1 84  ? -64.41000 34.86800  16.76200  1.000 47.40074  ? 60   LYS   A CB  1 
ATOM   229  C CG  . LYS   A 1 84  ? -65.09200 34.85100  15.39300  1.000 52.45265  ? 60   LYS   A CG  1 
ATOM   230  C CD  . LYS   A 1 84  ? -65.74100 36.15400  14.97000  1.000 56.89251  ? 60   LYS   A CD  1 
ATOM   231  C CE  . LYS   A 1 84  ? -65.51500 36.39500  13.47100  1.000 69.70878  ? 60   LYS   A CE  1 
ATOM   232  N NZ  . LYS   A 1 84  ? -65.19300 37.82100  13.14400  1.000 57.68233  ? 60   LYS   A NZ  1 
ATOM   233  N N   . PHE   A 1 85  ? -62.11000 34.50700  18.71800  1.000 39.45144  ? 61   PHE   A N   1 
ATOM   234  C CA  . PHE   A 1 85  ? -61.83200 34.12200  20.09300  1.000 35.75489  ? 61   PHE   A CA  1 
ATOM   235  C C   . PHE   A 1 85  ? -60.48300 34.65700  20.56000  1.000 40.13786  ? 61   PHE   A C   1 
ATOM   236  O O   . PHE   A 1 85  ? -59.46300 34.47900  19.88900  1.000 38.15169  ? 61   PHE   A O   1 
ATOM   237  C CB  . PHE   A 1 85  ? -61.88400 32.60200  20.23100  1.000 33.47828  ? 61   PHE   A CB  1 
ATOM   238  C CG  . PHE   A 1 85  ? -63.19800 32.00900  19.82000  1.000 36.25745  ? 61   PHE   A CG  1 
ATOM   239  C CD1 . PHE   A 1 85  ? -64.35600 32.31500  20.51600  1.000 33.61342  ? 61   PHE   A CD1 1 
ATOM   240  C CD2 . PHE   A 1 85  ? -63.28100 31.15000  18.73900  1.000 42.04667  ? 61   PHE   A CD2 1 
ATOM   241  C CE1 . PHE   A 1 85  ? -65.56900 31.77300  20.14600  1.000 36.96843  ? 61   PHE   A CE1 1 
ATOM   242  C CE2 . PHE   A 1 85  ? -64.49900 30.60300  18.36200  1.000 42.63210  ? 61   PHE   A CE2 1 
ATOM   243  C CZ  . PHE   A 1 85  ? -65.64100 30.91500  19.06800  1.000 39.62026  ? 61   PHE   A CZ  1 
ATOM   244  N N   . GLU   A 1 86  ? -60.48900 35.29000  21.73200  1.000 56.51756  ? 62   GLU   A N   1 
ATOM   245  C CA  . GLU   A 1 86  ? -59.28900 35.89400  22.29000  1.000 47.13272  ? 62   GLU   A CA  1 
ATOM   246  C C   . GLU   A 1 86  ? -58.33200 34.86300  22.87500  1.000 41.36604  ? 62   GLU   A C   1 
ATOM   247  O O   . GLU   A 1 86  ? -57.13400 35.14400  22.97200  1.000 38.10089  ? 62   GLU   A O   1 
ATOM   248  C CB  . GLU   A 1 86  ? -59.68900 36.91500  23.35700  1.000 48.75656  ? 62   GLU   A CB  1 
ATOM   249  C CG  . GLU   A 1 86  ? -58.97500 38.24800  23.26100  1.000 56.56606  ? 62   GLU   A CG  1 
ATOM   250  C CD  . GLU   A 1 86  ? -59.34400 39.18200  24.40100  1.000 75.71903  ? 62   GLU   A CD  1 
ATOM   251  O OE1 . GLU   A 1 86  ? -59.52100 38.69600  25.53900  1.000 69.54462  ? 62   GLU   A OE1 1 
ATOM   252  O OE2 . GLU   A 1 86  ? -59.47400 40.40100  24.15600  1.000 85.25729  ? 62   GLU   A OE2 1 
ATOM   253  N N   . ARG   A 1 87  ? -58.83000 33.68100  23.25900  1.000 37.94836  ? 63   ARG   A N   1 
ATOM   254  C CA  . ARG   A 1 87  ? -57.94800 32.63500  23.76800  1.000 36.50661  ? 63   ARG   A CA  1 
ATOM   255  C C   . ARG   A 1 87  ? -56.96700 32.15300  22.70500  1.000 47.70687  ? 63   ARG   A C   1 
ATOM   256  O O   . ARG   A 1 87  ? -55.86300 31.70300  23.03900  1.000 43.95740  ? 63   ARG   A O   1 
ATOM   257  C CB  . ARG   A 1 87  ? -58.76200 31.44600  24.27800  1.000 32.64622  ? 63   ARG   A CB  1 
ATOM   258  C CG  . ARG   A 1 87  ? -59.17800 31.52700  25.73100  1.000 62.24283  ? 63   ARG   A CG  1 
ATOM   259  C CD  . ARG   A 1 87  ? -60.64000 31.93700  25.84300  1.000 74.96988  ? 63   ARG   A CD  1 
ATOM   260  N NE  . ARG   A 1 87  ? -61.09700 32.01600  27.22500  1.000 52.39157  ? 63   ARG   A NE  1 
ATOM   261  C CZ  . ARG   A 1 87  ? -62.36700 32.15000  27.57700  1.000 58.05074  ? 63   ARG   A CZ  1 
ATOM   262  N NH1 . ARG   A 1 87  ? -63.32900 32.23300  26.67300  1.000 56.68055  ? 63   ARG   A NH1 1 
ATOM   263  N NH2 . ARG   A 1 87  ? -62.68000 32.19700  28.86900  1.000 74.76182  ? 63   ARG   A NH2 1 
ATOM   264  N N   . LEU   A 1 88  ? -57.34800 32.23200  21.42900  1.000 46.52845  ? 64   LEU   A N   1 
ATOM   265  C CA  . LEU   A 1 88  ? -56.58800 31.62900  20.34100  1.000 38.65517  ? 64   LEU   A CA  1 
ATOM   266  C C   . LEU   A 1 88  ? -55.61500 32.59700  19.67400  1.000 38.92785  ? 64   LEU   A C   1 
ATOM   267  O O   . LEU   A 1 88  ? -55.10000 32.28800  18.59400  1.000 40.10170  ? 64   LEU   A O   1 
ATOM   268  C CB  . LEU   A 1 88  ? -57.54600 31.06000  19.29000  1.000 36.89199  ? 64   LEU   A CB  1 
ATOM   269  C CG  . LEU   A 1 88  ? -58.62800 30.09200  19.77400  1.000 39.54463  ? 64   LEU   A CG  1 
ATOM   270  C CD1 . LEU   A 1 88  ? -59.46400 29.59500  18.59900  1.000 40.72846  ? 64   LEU   A CD1 1 
ATOM   271  C CD2 . LEU   A 1 88  ? -58.01700 28.92700  20.53200  1.000 34.78385  ? 64   LEU   A CD2 1 
ATOM   272  N N   . GLN   A 1 89  ? -55.34400 33.75000  20.28800  1.000 38.70190  ? 65   GLN   A N   1 
ATOM   273  C CA  . GLN   A 1 89  ? -54.50100 34.77100  19.67400  1.000 36.14998  ? 65   GLN   A CA  1 
ATOM   274  C C   . GLN   A 1 89  ? -53.01600 34.49400  19.87000  1.000 35.52151  ? 65   GLN   A C   1 
ATOM   275  O O   . GLN   A 1 89  ? -52.26600 35.38600  20.27500  1.000 39.64893  ? 65   GLN   A O   1 
ATOM   276  C CB  . GLN   A 1 89  ? -54.83200 36.15100  20.24300  1.000 40.38359  ? 65   GLN   A CB  1 
ATOM   277  C CG  . GLN   A 1 89  ? -56.26900 36.58400  20.06000  1.000 45.78022  ? 65   GLN   A CG  1 
ATOM   278  C CD  . GLN   A 1 89  ? -56.51000 37.20500  18.70600  1.000 43.62191  ? 65   GLN   A CD  1 
ATOM   279  O OE1 . GLN   A 1 89  ? -57.43600 36.82600  17.99100  1.000 42.56340  ? 65   GLN   A OE1 1 
ATOM   280  N NE2 . GLN   A 1 89  ? -55.67100 38.16700  18.34300  1.000 46.45164  ? 65   GLN   A NE2 1 
ATOM   281  N N   . THR   A 1 90  ? -52.57800 33.27600  19.58300  1.000 33.81327  ? 66   THR   A N   1 
ATOM   282  C CA  . THR   A 1 90  ? -51.17000 32.93900  19.69500  1.000 30.87051  ? 66   THR   A CA  1 
ATOM   283  C C   . THR   A 1 90  ? -50.44200 33.25900  18.39700  1.000 31.05041  ? 66   THR   A C   1 
ATOM   284  O O   . THR   A 1 90  ? -51.03400 33.27200  17.31600  1.000 33.50375  ? 66   THR   A O   1 
ATOM   285  C CB  . THR   A 1 90  ? -50.98600 31.46100  20.03300  1.000 33.99205  ? 66   THR   A CB  1 
ATOM   286  O OG1 . THR   A 1 90  ? -51.26200 30.66900  18.87200  1.000 28.93130  ? 66   THR   A OG1 1 
ATOM   287  C CG2 . THR   A 1 90  ? -51.91300 31.04800  21.16900  1.000 33.13392  ? 66   THR   A CG2 1 
ATOM   288  N N   . VAL   A 1 91  ? -49.14100 33.53400  18.52300  1.000 37.11291  ? 67   VAL   A N   1 
ATOM   289  C CA  . VAL   A 1 91  ? -48.29100 33.69100  17.34600  1.000 27.18599  ? 67   VAL   A CA  1 
ATOM   290  C C   . VAL   A 1 91  ? -48.32800 32.42600  16.50100  1.000 29.84301  ? 67   VAL   A C   1 
ATOM   291  O O   . VAL   A 1 91  ? -48.38200 32.48900  15.26700  1.000 33.23157  ? 67   VAL   A O   1 
ATOM   292  C CB  . VAL   A 1 91  ? -46.85700 34.06000  17.77100  1.000 21.35411  ? 67   VAL   A CB  1 
ATOM   293  C CG1 . VAL   A 1 91  ? -45.87900 33.79900  16.65200  1.000 24.07775  ? 67   VAL   A CG1 1 
ATOM   294  C CG2 . VAL   A 1 91  ? -46.79800 35.52000  18.17400  1.000 25.23421  ? 67   VAL   A CG2 1 
ATOM   295  N N   . THR   A 1 92  ? -48.33500 31.25800  17.15000  1.000 29.30968  ? 68   THR   A N   1 
ATOM   296  C CA  . THR   A 1 92  ? -48.49400 30.00400  16.42000  1.000 30.22368  ? 68   THR   A CA  1 
ATOM   297  C C   . THR   A 1 92  ? -49.76600 29.99600  15.58400  1.000 29.14039  ? 68   THR   A C   1 
ATOM   298  O O   . THR   A 1 92  ? -49.81200 29.35200  14.53200  1.000 32.56277  ? 68   THR   A O   1 
ATOM   299  C CB  . THR   A 1 92  ? -48.49900 28.83000  17.40100  1.000 35.49826  ? 68   THR   A CB  1 
ATOM   300  O OG1 . THR   A 1 92  ? -47.31400 28.87400  18.20300  1.000 44.62931  ? 68   THR   A OG1 1 
ATOM   301  C CG2 . THR   A 1 92  ? -48.56800 27.49200  16.66700  1.000 28.72278  ? 68   THR   A CG2 1 
ATOM   302  N N   . ASN   A 1 93  ? -50.80200 30.70800  16.02300  1.000 33.40710  ? 69   ASN   A N   1 
ATOM   303  C CA  . ASN   A 1 93  ? -52.05900 30.72400  15.29200  1.000 30.71953  ? 69   ASN   A CA  1 
ATOM   304  C C   . ASN   A 1 93  ? -52.09000 31.77000  14.19100  1.000 29.78780  ? 69   ASN   A C   1 
ATOM   305  O O   . ASN   A 1 93  ? -52.82100 31.59600  13.21000  1.000 34.14577  ? 69   ASN   A O   1 
ATOM   306  C CB  . ASN   A 1 93  ? -53.23000 30.95500  16.25100  1.000 34.61134  ? 69   ASN   A CB  1 
ATOM   307  C CG  . ASN   A 1 93  ? -53.56300 29.72300  17.06700  1.000 31.62463  ? 69   ASN   A CG  1 
ATOM   308  O OD1 . ASN   A 1 93  ? -53.17800 28.60900  16.71500  1.000 31.21748  ? 69   ASN   A OD1 1 
ATOM   309  N ND2 . ASN   A 1 93  ? -54.30000 29.91500  18.14900  1.000 37.55281  ? 69   ASN   A ND2 1 
ATOM   310  N N   . TYR   A 1 94  ? -51.31100 32.84600  14.32400  1.000 30.39722  ? 70   TYR   A N   1 
ATOM   311  C CA  . TYR   A 1 94  ? -51.16200 33.78100  13.21300  1.000 35.16305  ? 70   TYR   A CA  1 
ATOM   312  C C   . TYR   A 1 94  ? -50.53100 33.10600  12.00300  1.000 30.07696  ? 70   TYR   A C   1 
ATOM   313  O O   . TYR   A 1 94  ? -50.78500 33.50600  10.86400  1.000 31.97131  ? 70   TYR   A O   1 
ATOM   314  C CB  . TYR   A 1 94  ? -50.31600 34.98800  13.62400  1.000 36.22218  ? 70   TYR   A CB  1 
ATOM   315  C CG  . TYR   A 1 94  ? -50.97400 35.95700  14.58400  1.000 35.98036  ? 70   TYR   A CG  1 
ATOM   316  C CD1 . TYR   A 1 94  ? -52.00500 35.56200  15.42400  1.000 33.21662  ? 70   TYR   A CD1 1 
ATOM   317  C CD2 . TYR   A 1 94  ? -50.56100 37.27900  14.63500  1.000 49.73166  ? 70   TYR   A CD2 1 
ATOM   318  C CE1 . TYR   A 1 94  ? -52.59600 36.45800  16.29600  1.000 41.60100  ? 70   TYR   A CE1 1 
ATOM   319  C CE2 . TYR   A 1 94  ? -51.14400 38.17700  15.49900  1.000 49.85843  ? 70   TYR   A CE2 1 
ATOM   320  C CZ  . TYR   A 1 94  ? -52.16000 37.76500  16.32500  1.000 46.23646  ? 70   TYR   A CZ  1 
ATOM   321  O OH  . TYR   A 1 94  ? -52.73400 38.67600  17.18000  1.000 60.59865  ? 70   TYR   A OH  1 
ATOM   322  N N   . PHE   A 1 95  ? -49.69100 32.09900  12.23500  1.000 30.27664  ? 71   PHE   A N   1 
ATOM   323  C CA  . PHE   A 1 95  ? -49.16300 31.29000  11.14500  1.000 31.35360  ? 71   PHE   A CA  1 
ATOM   324  C C   . PHE   A 1 95  ? -50.21600 30.31800  10.64100  1.000 31.70713  ? 71   PHE   A C   1 
ATOM   325  O O   . PHE   A 1 95  ? -50.31600 30.07100  9.43300   1.000 37.66809  ? 71   PHE   A O   1 
ATOM   326  C CB  . PHE   A 1 95  ? -47.92100 30.53300  11.61500  1.000 30.42836  ? 71   PHE   A CB  1 
ATOM   327  C CG  . PHE   A 1 95  ? -46.80200 31.42500  12.06500  1.000 28.37271  ? 71   PHE   A CG  1 
ATOM   328  C CD1 . PHE   A 1 95  ? -46.70000 32.72300  11.59600  1.000 34.36999  ? 71   PHE   A CD1 1 
ATOM   329  C CD2 . PHE   A 1 95  ? -45.86000 30.96900  12.96700  1.000 27.62676  ? 71   PHE   A CD2 1 
ATOM   330  C CE1 . PHE   A 1 95  ? -45.67400 33.54700  12.00800  1.000 34.59787  ? 71   PHE   A CE1 1 
ATOM   331  C CE2 . PHE   A 1 95  ? -44.83400 31.79000  13.38500  1.000 33.46264  ? 71   PHE   A CE2 1 
ATOM   332  C CZ  . PHE   A 1 95  ? -44.74100 33.08100  12.90400  1.000 37.59885  ? 71   PHE   A CZ  1 
ATOM   333  N N   . ILE   A 1 96  ? -51.00500 29.76400  11.56100  1.000 27.78678  ? 72   ILE   A N   1 
ATOM   334  C CA  . ILE   A 1 96  ? -52.12000 28.90100  11.18900  1.000 32.05194  ? 72   ILE   A CA  1 
ATOM   335  C C   . ILE   A 1 96  ? -53.05100 29.64200  10.23500  1.000 32.12043  ? 72   ILE   A C   1 
ATOM   336  O O   . ILE   A 1 96  ? -53.61000 29.05400  9.30100   1.000 31.08414  ? 72   ILE   A O   1 
ATOM   337  C CB  . ILE   A 1 96  ? -52.86000 28.43800  12.45900  1.000 33.95686  ? 72   ILE   A CB  1 
ATOM   338  C CG1 . ILE   A 1 96  ? -52.03800 27.39800  13.22500  1.000 34.60739  ? 72   ILE   A CG1 1 
ATOM   339  C CG2 . ILE   A 1 96  ? -54.21800 27.89200  12.11700  1.000 31.02995  ? 72   ILE   A CG2 1 
ATOM   340  C CD1 . ILE   A 1 96  ? -51.94600 26.04800  12.58600  1.000 34.27222  ? 72   ILE   A CD1 1 
ATOM   341  N N   . THR   A 1 97  ? -53.20600 30.95400  10.44400  1.000 28.37779  ? 73   THR   A N   1 
ATOM   342  C CA  . THR   A 1 97  ? -54.12200 31.75500  9.63800   1.000 31.36655  ? 73   THR   A CA  1 
ATOM   343  C C   . THR   A 1 97  ? -53.64400 31.86500  8.19900   1.000 35.78982  ? 73   THR   A C   1 
ATOM   344  O O   . THR   A 1 97  ? -54.32400 31.41200  7.27100   1.000 34.58621  ? 73   THR   A O   1 
ATOM   345  C CB  . THR   A 1 97  ? -54.29000 33.14200  10.25500  1.000 26.44645  ? 73   THR   A CB  1 
ATOM   346  O OG1 . THR   A 1 97  ? -54.97000 33.01200  11.50700  1.000 40.70159  ? 73   THR   A OG1 1 
ATOM   347  C CG2 . THR   A 1 97  ? -55.10300 34.03800  9.33200   1.000 21.35411  ? 73   THR   A CG2 1 
ATOM   348  N N   . SER   A 1 98  ? -52.47900 32.48700  7.98900   1.000 34.19481  ? 74   SER   A N   1 
ATOM   349  C CA  . SER   A 1 98  ? -51.95900 32.64300  6.63400   1.000 36.58720  ? 74   SER   A CA  1 
ATOM   350  C C   . SER   A 1 98  ? -51.82600 31.30000  5.93300   1.000 34.76621  ? 74   SER   A C   1 
ATOM   351  O O   . SER   A 1 98  ? -51.96100 31.21900  4.70700   1.000 37.16753  ? 74   SER   A O   1 
ATOM   352  C CB  . SER   A 1 98  ? -50.61300 33.36000  6.66700   1.000 39.04635  ? 74   SER   A CB  1 
ATOM   353  O OG  . SER   A 1 98  ? -49.65500 32.57400  7.34800   1.000 41.52687  ? 74   SER   A OG  1 
ATOM   354  N N   . LEU   A 1 99  ? -51.57300 30.23400  6.69600   1.000 31.44986  ? 75   LEU   A N   1 
ATOM   355  C CA  . LEU   A 1 99  ? -51.62200 28.89200  6.12800   1.000 34.12537  ? 75   LEU   A CA  1 
ATOM   356  C C   . LEU   A 1 99  ? -53.01100 28.59000  5.58100   1.000 37.16544  ? 75   LEU   A C   1 
ATOM   357  O O   . LEU   A 1 99  ? -53.15700 27.89700  4.56900   1.000 35.96005  ? 75   LEU   A O   1 
ATOM   358  C CB  . LEU   A 1 99  ? -51.22000 27.87200  7.19100   1.000 34.29762  ? 75   LEU   A CB  1 
ATOM   359  C CG  . LEU   A 1 99  ? -50.47100 26.61700  6.74700   1.000 36.71667  ? 75   LEU   A CG  1 
ATOM   360  C CD1 . LEU   A 1 99  ? -49.13200 27.00400  6.16100   1.000 35.11107  ? 75   LEU   A CD1 1 
ATOM   361  C CD2 . LEU   A 1 99  ? -50.28000 25.68800  7.93400   1.000 39.34019  ? 75   LEU   A CD2 1 
ATOM   362  N N   . ALA   A 1 100 ? -54.04900 29.11200  6.23600   1.000 39.99734  ? 76   ALA   A N   1 
ATOM   363  C CA  . ALA   A 1 100 ? -55.40700 28.88900  5.75800   1.000 37.56041  ? 76   ALA   A CA  1 
ATOM   364  C C   . ALA   A 1 100 ? -55.79700 29.89300  4.68100   1.000 35.44590  ? 76   ALA   A C   1 
ATOM   365  O O   . ALA   A 1 100 ? -56.67300 29.60300  3.86100   1.000 37.25555  ? 76   ALA   A O   1 
ATOM   366  C CB  . ALA   A 1 100 ? -56.39300 28.93900  6.92500   1.000 31.41904  ? 76   ALA   A CB  1 
ATOM   367  N N   . CYS   A 1 101 ? -55.17800 31.07700  4.67000   1.000 32.46484  ? 77   CYS   A N   1 
ATOM   368  C CA  . CYS   A 1 101 ? -55.38300 31.99100  3.55000   1.000 31.36084  ? 77   CYS   A CA  1 
ATOM   369  C C   . CYS   A 1 101 ? -54.75700 31.43500  2.27700   1.000 37.01698  ? 77   CYS   A C   1 
ATOM   370  O O   . CYS   A 1 101 ? -55.33500 31.55100  1.19100   1.000 35.98783  ? 77   CYS   A O   1 
ATOM   371  C CB  . CYS   A 1 101 ? -54.80400 33.37000  3.86200   1.000 33.20450  ? 77   CYS   A CB  1 
ATOM   372  S SG  . CYS   A 1 101 ? -55.57100 34.24700  5.23600   1.000 29.80803  ? 77   CYS   A SG  1 
ATOM   373  N N   . ALA   A 1 102 ? -53.57100 30.83300  2.39100   1.000 37.90614  ? 78   ALA   A N   1 
ATOM   374  C CA  . ALA   A 1 102 ? -52.97600 30.15800  1.24300   1.000 31.08217  ? 78   ALA   A CA  1 
ATOM   375  C C   . ALA   A 1 102 ? -53.85500 29.01400  0.75200   1.000 34.52520  ? 78   ALA   A C   1 
ATOM   376  O O   . ALA   A 1 102 ? -53.91800 28.75800  -0.45500  1.000 38.78009  ? 78   ALA   A O   1 
ATOM   377  C CB  . ALA   A 1 102 ? -51.58100 29.64600  1.59800   1.000 33.24976  ? 78   ALA   A CB  1 
ATOM   378  N N   . ASP   A 1 103 ? -54.54200 28.32000  1.66500   1.000 33.06455  ? 79   ASP   A N   1 
ATOM   379  C CA  . ASP   A 1 103 ? -55.47700 27.27400  1.26100   1.000 32.94316  ? 79   ASP   A CA  1 
ATOM   380  C C   . ASP   A 1 103 ? -56.77100 27.84900  0.70400   1.000 31.46032  ? 79   ASP   A C   1 
ATOM   381  O O   . ASP   A 1 103 ? -57.42500 27.20700  -0.12300  1.000 32.76071  ? 79   ASP   A O   1 
ATOM   382  C CB  . ASP   A 1 103 ? -55.79800 26.35400  2.43900   1.000 37.96744  ? 79   ASP   A CB  1 
ATOM   383  C CG  . ASP   A 1 103 ? -54.61500 25.51300  2.86500   1.000 48.22818  ? 79   ASP   A CG  1 
ATOM   384  O OD1 . ASP   A 1 103 ? -53.76900 25.18800  2.00400   1.000 48.03282  ? 79   ASP   A OD1 1 
ATOM   385  O OD2 . ASP   A 1 103 ? -54.54200 25.16700  4.06500   1.000 52.27754  ? 79   ASP   A OD2 1 
ATOM   386  N N   . LEU   A 1 104 ? -57.16200 29.04100  1.15200   1.000 31.51310  ? 80   LEU   A N   1 
ATOM   387  C CA  . LEU   A 1 104 ? -58.38400 29.65300  0.64500   1.000 30.17261  ? 80   LEU   A CA  1 
ATOM   388  C C   . LEU   A 1 104 ? -58.19300 30.15300  -0.78300  1.000 32.21180  ? 80   LEU   A C   1 
ATOM   389  O O   . LEU   A 1 104 ? -59.09800 30.02900  -1.61700  1.000 33.17255  ? 80   LEU   A O   1 
ATOM   390  C CB  . LEU   A 1 104 ? -58.81000 30.79500  1.56600   1.000 27.03863  ? 80   LEU   A CB  1 
ATOM   391  C CG  . LEU   A 1 104 ? -60.28300 31.18500  1.56900   1.000 25.76686  ? 80   LEU   A CG  1 
ATOM   392  C CD1 . LEU   A 1 104 ? -61.10200 30.03800  2.11400   1.000 31.53040  ? 80   LEU   A CD1 1 
ATOM   393  C CD2 . LEU   A 1 104 ? -60.49500 32.44100  2.38900   1.000 22.52901  ? 80   LEU   A CD2 1 
ATOM   394  N N   . VAL   A 1 105 ? -57.02100 30.71700  -1.08400  1.000 33.88855  ? 81   VAL   A N   1 
ATOM   395  C CA  . VAL   A 1 105 ? -56.73400 31.16100  -2.44400  1.000 34.49993  ? 81   VAL   A CA  1 
ATOM   396  C C   . VAL   A 1 105 ? -56.73700 29.97800  -3.40400  1.000 35.25314  ? 81   VAL   A C   1 
ATOM   397  O O   . VAL   A 1 105 ? -57.26800 30.06900  -4.51800  1.000 32.39667  ? 81   VAL   A O   1 
ATOM   398  C CB  . VAL   A 1 105 ? -55.39800 31.92700  -2.49000  1.000 38.03138  ? 81   VAL   A CB  1 
ATOM   399  C CG1 . VAL   A 1 105 ? -55.10900 32.41500  -3.90300  1.000 33.89072  ? 81   VAL   A CG1 1 
ATOM   400  C CG2 . VAL   A 1 105 ? -55.42800 33.09900  -1.52600  1.000 32.64149  ? 81   VAL   A CG2 1 
ATOM   401  N N   . MET   A 1 106 ? -56.15200 28.84800  -2.99100  1.000 31.83737  ? 82   MET   A N   1 
ATOM   402  C CA  . MET   A 1 106 ? -56.20300 27.64700  -3.82400  1.000 36.35340  ? 82   MET   A CA  1 
ATOM   403  C C   . MET   A 1 106 ? -57.64300 27.21900  -4.08100  1.000 41.10917  ? 82   MET   A C   1 
ATOM   404  O O   . MET   A 1 106 ? -58.01900 26.91100  -5.21900  1.000 42.92553  ? 82   MET   A O   1 
ATOM   405  C CB  . MET   A 1 106 ? -55.42100 26.50500  -3.17400  1.000 32.10721  ? 82   MET   A CB  1 
ATOM   406  C CG  . MET   A 1 106 ? -53.93000 26.73600  -3.06700  1.000 45.19097  ? 82   MET   A CG  1 
ATOM   407  S SD  . MET   A 1 106 ? -53.00000 26.18500  -4.51800  1.000 53.76602  ? 82   MET   A SD  1 
ATOM   408  C CE  . MET   A 1 106 ? -52.96500 24.41100  -4.26300  1.000 45.53933  ? 82   MET   A CE  1 
ATOM   409  N N   . GLY   A 1 107 ? -58.46600 27.19400  -3.03100  1.000 36.21679  ? 83   GLY   A N   1 
ATOM   410  C CA  . GLY   A 1 107 ? -59.84900 26.78000  -3.20000  1.000 35.74022  ? 83   GLY   A CA  1 
ATOM   411  C C   . GLY   A 1 107 ? -60.62500 27.68600  -4.13600  1.000 38.03530  ? 83   GLY   A C   1 
ATOM   412  O O   . GLY   A 1 107 ? -61.49100 27.22600  -4.88400  1.000 37.59547  ? 83   GLY   A O   1 
ATOM   413  N N   . LEU   A 1 108 ? -60.32700 28.98300  -4.11200  1.000 33.76709  ? 84   LEU   A N   1 
ATOM   414  C CA  . LEU   A 1 108 ? -61.03200 29.92600  -4.97400  1.000 33.32644  ? 84   LEU   A CA  1 
ATOM   415  C C   . LEU   A 1 108 ? -60.32400 30.11600  -6.31300  1.000 37.75734  ? 84   LEU   A C   1 
ATOM   416  O O   . LEU   A 1 108 ? -60.90300 29.83800  -7.36900  1.000 41.03720  ? 84   LEU   A O   1 
ATOM   417  C CB  . LEU   A 1 108 ? -61.20300 31.27400  -4.26200  1.000 34.16912  ? 84   LEU   A CB  1 
ATOM   418  C CG  . LEU   A 1 108 ? -61.96800 31.28500  -2.93900  1.000 29.08695  ? 84   LEU   A CG  1 
ATOM   419  C CD1 . LEU   A 1 108 ? -61.96900 32.68200  -2.33500  1.000 21.35411  ? 84   LEU   A CD1 1 
ATOM   420  C CD2 . LEU   A 1 108 ? -63.38100 30.79500  -3.16300  1.000 24.74525  ? 84   LEU   A CD2 1 
ATOM   421  N N   . ALA   A 1 109 ? -59.07000 30.57600  -6.28300  1.000 39.49959  ? 85   ALA   A N   1 
ATOM   422  C CA  . ALA   A 1 109 ? -58.39000 31.03400  -7.49100  1.000 32.95349  ? 85   ALA   A CA  1 
ATOM   423  C C   . ALA   A 1 109 ? -57.74800 29.92100  -8.30900  1.000 31.53121  ? 85   ALA   A C   1 
ATOM   424  O O   . ALA   A 1 109 ? -57.59400 30.08000  -9.52400  1.000 40.03307  ? 85   ALA   A O   1 
ATOM   425  C CB  . ALA   A 1 109 ? -57.31600 32.06600  -7.13700  1.000 22.41031  ? 85   ALA   A CB  1 
ATOM   426  N N   . VAL   A 1 110 ? -57.36800 28.80100  -7.69800  1.000 31.75895  ? 86   VAL   A N   1 
ATOM   427  C CA  . VAL   A 1 110 ? -56.59900 27.79500  -8.42700  1.000 32.13216  ? 86   VAL   A CA  1 
ATOM   428  C C   . VAL   A 1 110 ? -57.43900 26.56100  -8.73200  1.000 36.96326  ? 86   VAL   A C   1 
ATOM   429  O O   . VAL   A 1 110 ? -57.74100 26.28200  -9.89700  1.000 39.12500  ? 86   VAL   A O   1 
ATOM   430  C CB  . VAL   A 1 110 ? -55.32600 27.39700  -7.65600  1.000 33.16441  ? 86   VAL   A CB  1 
ATOM   431  C CG1 . VAL   A 1 110 ? -54.65500 26.19600  -8.31600  1.000 32.24965  ? 86   VAL   A CG1 1 
ATOM   432  C CG2 . VAL   A 1 110 ? -54.36400 28.55200  -7.59600  1.000 28.97183  ? 86   VAL   A CG2 1 
ATOM   433  N N   . VAL   A 1 111 ? -57.81300 25.81700  -7.68800  1.000 38.25210  ? 87   VAL   A N   1 
ATOM   434  C CA  . VAL   A 1 111 ? -58.39900 24.48500  -7.87800  1.000 37.14431  ? 87   VAL   A CA  1 
ATOM   435  C C   . VAL   A 1 111 ? -59.57300 24.47900  -8.86200  1.000 42.62761  ? 87   VAL   A C   1 
ATOM   436  O O   . VAL   A 1 111 ? -59.60800 23.60000  -9.73300  1.000 46.00869  ? 87   VAL   A O   1 
ATOM   437  C CB  . VAL   A 1 111 ? -58.75400 23.86600  -6.52400  1.000 36.00433  ? 87   VAL   A CB  1 
ATOM   438  C CG1 . VAL   A 1 111 ? -59.36800 22.48500  -6.71300  1.000 35.27535  ? 87   VAL   A CG1 1 
ATOM   439  C CG2 . VAL   A 1 111 ? -57.51800 23.78100  -5.63800  1.000 35.17103  ? 87   VAL   A CG2 1 
ATOM   440  N N   . PRO   A 1 112 ? -60.54700 25.40100  -8.78600  1.000 45.30311  ? 88   PRO   A N   1 
ATOM   441  C CA  . PRO   A 1 112 ? -61.68200 25.31700  -9.72800  1.000 41.88068  ? 88   PRO   A CA  1 
ATOM   442  C C   . PRO   A 1 112 ? -61.28000 25.38400  -11.19200 1.000 43.26830  ? 88   PRO   A C   1 
ATOM   443  O O   . PRO   A 1 112 ? -61.83700 24.64400  -12.01200 1.000 42.44112  ? 88   PRO   A O   1 
ATOM   444  C CB  . PRO   A 1 112 ? -62.55800 26.51500  -9.33400  1.000 40.89214  ? 88   PRO   A CB  1 
ATOM   445  C CG  . PRO   A 1 112 ? -62.17800 26.83100  -7.94800  1.000 39.32419  ? 88   PRO   A CG  1 
ATOM   446  C CD  . PRO   A 1 112 ? -60.72300 26.51500  -7.83700  1.000 44.18510  ? 88   PRO   A CD  1 
ATOM   447  N N   . PHE   A 1 113 ? -60.33300 26.25600  -11.54800 1.000 43.86656  ? 89   PHE   A N   1 
ATOM   448  C CA  . PHE   A 1 113 ? -59.92200 26.36400  -12.94600 1.000 40.42985  ? 89   PHE   A CA  1 
ATOM   449  C C   . PHE   A 1 113 ? -59.20400 25.10300  -13.40800 1.000 41.48533  ? 89   PHE   A C   1 
ATOM   450  O O   . PHE   A 1 113 ? -59.35500 24.68300  -14.56100 1.000 45.36561  ? 89   PHE   A O   1 
ATOM   451  C CB  . PHE   A 1 113 ? -59.03900 27.59200  -13.14700 1.000 30.87592  ? 89   PHE   A CB  1 
ATOM   452  C CG  . PHE   A 1 113 ? -59.73400 28.88600  -12.86000 1.000 36.28391  ? 89   PHE   A CG  1 
ATOM   453  C CD1 . PHE   A 1 113 ? -59.77000 29.39900  -11.57300 1.000 39.16187  ? 89   PHE   A CD1 1 
ATOM   454  C CD2 . PHE   A 1 113 ? -60.35800 29.58900  -13.87300 1.000 33.77045  ? 89   PHE   A CD2 1 
ATOM   455  C CE1 . PHE   A 1 113 ? -60.40900 30.59600  -11.30200 1.000 36.77469  ? 89   PHE   A CE1 1 
ATOM   456  C CE2 . PHE   A 1 113 ? -61.00100 30.78600  -13.60900 1.000 36.16191  ? 89   PHE   A CE2 1 
ATOM   457  C CZ  . PHE   A 1 113 ? -61.02600 31.28900  -12.32200 1.000 41.64454  ? 89   PHE   A CZ  1 
ATOM   458  N N   . GLY   A 1 114 ? -58.41000 24.49000  -12.52900 1.000 43.13145  ? 90   GLY   A N   1 
ATOM   459  C CA  . GLY   A 1 114 ? -57.84900 23.18600  -12.83400 1.000 38.92364  ? 90   GLY   A CA  1 
ATOM   460  C C   . GLY   A 1 114 ? -58.89500 22.10300  -12.97600 1.000 46.25712  ? 90   GLY   A C   1 
ATOM   461  O O   . GLY   A 1 114 ? -58.64800 21.10400  -13.65900 1.000 51.25541  ? 90   GLY   A O   1 
ATOM   462  N N   . ALA   A 1 115 ? -60.05800 22.27900  -12.34100 1.000 50.84840  ? 91   ALA   A N   1 
ATOM   463  C CA  . ALA   A 1 115 ? -61.17000 21.35800  -12.55000 1.000 57.12370  ? 91   ALA   A CA  1 
ATOM   464  C C   . ALA   A 1 115 ? -61.82400 21.58900  -13.90700 1.000 50.39898  ? 91   ALA   A C   1 
ATOM   465  O O   . ALA   A 1 115 ? -62.15700 20.63000  -14.61500 1.000 46.43103  ? 91   ALA   A O   1 
ATOM   466  C CB  . ALA   A 1 115 ? -62.19600 21.50800  -11.42500 1.000 47.11760  ? 91   ALA   A CB  1 
ATOM   467  N N   . ALA   A 1 116 ? -62.01400 22.85700  -14.28300 1.000 45.21363  ? 92   ALA   A N   1 
ATOM   468  C CA  . ALA   A 1 116 ? -62.58100 23.17400  -15.59000 1.000 49.07240  ? 92   ALA   A CA  1 
ATOM   469  C C   . ALA   A 1 116 ? -61.70600 22.64100  -16.71500 1.000 51.34198  ? 92   ALA   A C   1 
ATOM   470  O O   . ALA   A 1 116 ? -62.21500 22.13900  -17.72300 1.000 48.12093  ? 92   ALA   A O   1 
ATOM   471  C CB  . ALA   A 1 116 ? -62.76700 24.68600  -15.72600 1.000 40.83786  ? 92   ALA   A CB  1 
ATOM   472  N N   . HIS   A 1 117 ? -60.38400 22.73300  -16.55400 1.000 50.25073  ? 93   HIS   A N   1 
ATOM   473  C CA  . HIS   A 1 117 ? -59.47400 22.25700  -17.58900 1.000 51.40369  ? 93   HIS   A CA  1 
ATOM   474  C C   . HIS   A 1 117 ? -59.63700 20.76100  -17.82300 1.000 56.84238  ? 93   HIS   A C   1 
ATOM   475  O O   . HIS   A 1 117 ? -59.63900 20.30000  -18.97100 1.000 60.40976  ? 93   HIS   A O   1 
ATOM   476  C CB  . HIS   A 1 117 ? -58.03300 22.58500  -17.20100 1.000 51.05181  ? 93   HIS   A CB  1 
ATOM   477  C CG  . HIS   A 1 117 ? -57.05000 22.42200  -18.31900 1.000 53.77040  ? 93   HIS   A CG  1 
ATOM   478  N ND1 . HIS   A 1 117 ? -56.88300 21.23600  -19.00000 1.000 52.52485  ? 93   HIS   A ND1 1 
ATOM   479  C CD2 . HIS   A 1 117 ? -56.16500 23.29200  -18.86000 1.000 51.46718  ? 93   HIS   A CD2 1 
ATOM   480  C CE1 . HIS   A 1 117 ? -55.94800 21.38500  -19.92000 1.000 58.49081  ? 93   HIS   A CE1 1 
ATOM   481  N NE2 . HIS   A 1 117 ? -55.49500 22.62400  -19.85500 1.000 59.26115  ? 93   HIS   A NE2 1 
ATOM   482  N N   . ILE   A 1 118 ? -59.77000 19.98300  -16.74800 1.000 55.65698  ? 94   ILE   A N   1 
ATOM   483  C CA  . ILE   A 1 118 ? -59.87300 18.53400  -16.89500 1.000 60.79146  ? 94   ILE   A CA  1 
ATOM   484  C C   . ILE   A 1 118 ? -61.18700 18.15200  -17.56600 1.000 62.70773  ? 94   ILE   A C   1 
ATOM   485  O O   . ILE   A 1 118 ? -61.21400 17.31000  -18.47300 1.000 65.66296  ? 94   ILE   A O   1 
ATOM   486  C CB  . ILE   A 1 118 ? -59.71200 17.84500  -15.52600 1.000 59.88697  ? 94   ILE   A CB  1 
ATOM   487  C CG1 . ILE   A 1 118 ? -58.28500 18.01500  -15.00000 1.000 56.77210  ? 94   ILE   A CG1 1 
ATOM   488  C CG2 . ILE   A 1 118 ? -60.06600 16.37100  -15.61800 1.000 59.45787  ? 94   ILE   A CG2 1 
ATOM   489  C CD1 . ILE   A 1 118 ? -58.07300 17.43000  -13.62100 1.000 54.99148  ? 94   ILE   A CD1 1 
ATOM   490  N N   . LEU   A 1 119 ? -62.29300 18.76500  -17.14300 1.000 58.47040  ? 95   LEU   A N   1 
ATOM   491  C CA  . LEU   A 1 119 ? -63.60000 18.38700  -17.67100 1.000 61.42867  ? 95   LEU   A CA  1 
ATOM   492  C C   . LEU   A 1 119 ? -63.81800 18.92800  -19.08200 1.000 60.73866  ? 95   LEU   A C   1 
ATOM   493  O O   . LEU   A 1 119 ? -64.28000 18.19900  -19.96500 1.000 57.96236  ? 95   LEU   A O   1 
ATOM   494  C CB  . LEU   A 1 119 ? -64.70100 18.86700  -16.72100 1.000 62.79740  ? 95   LEU   A CB  1 
ATOM   495  C CG  . LEU   A 1 119 ? -64.56900 18.36600  -15.27800 1.000 67.06123  ? 95   LEU   A CG  1 
ATOM   496  C CD1 . LEU   A 1 119 ? -65.24600 19.30800  -14.29200 1.000 65.12582  ? 95   LEU   A CD1 1 
ATOM   497  C CD2 . LEU   A 1 119 ? -65.11000 16.95100  -15.12800 1.000 68.77152  ? 95   LEU   A CD2 1 
ATOM   498  N N   . MET   A 1 120 ? -63.49000 20.20300  -19.31300 1.000 58.93815  ? 96   MET   A N   1 
ATOM   499  C CA  . MET   A 1 120 ? -63.58400 20.78600  -20.64800 1.000 57.40176  ? 96   MET   A CA  1 
ATOM   500  C C   . MET   A 1 120 ? -62.54600 20.24400  -21.61800 1.000 62.68849  ? 96   MET   A C   1 
ATOM   501  O O   . MET   A 1 120 ? -62.63400 20.54700  -22.81300 1.000 65.94759  ? 96   MET   A O   1 
ATOM   502  C CB  . MET   A 1 120 ? -63.42600 22.30200  -20.58900 1.000 50.77881  ? 96   MET   A CB  1 
ATOM   503  C CG  . MET   A 1 120 ? -64.63400 23.07300  -20.13400 1.000 49.48006  ? 96   MET   A CG  1 
ATOM   504  S SD  . MET   A 1 120 ? -64.31000 24.80500  -20.49600 1.000 53.96892  ? 96   MET   A SD  1 
ATOM   505  C CE  . MET   A 1 120 ? -62.94800 25.05100  -19.36200 1.000 57.20434  ? 96   MET   A CE  1 
ATOM   506  N N   . LYS   A 1 121 ? -61.55600 19.49200  -21.13800 1.000 64.17329  ? 97   LYS   A N   1 
ATOM   507  C CA  . LYS   A 1 121 ? -60.48500 18.93100  -21.96400 1.000 60.10052  ? 97   LYS   A CA  1 
ATOM   508  C C   . LYS   A 1 121 ? -59.62100 20.00600  -22.62500 1.000 57.75511  ? 97   LYS   A C   1 
ATOM   509  O O   . LYS   A 1 121 ? -58.90500 19.71400  -23.58700 1.000 60.05861  ? 97   LYS   A O   1 
ATOM   510  C CB  . LYS   A 1 121 ? -61.04100 17.97900  -23.03100 1.000 53.22416  ? 97   LYS   A CB  1 
ATOM   511  C CG  . LYS   A 1 121 ? -61.54500 16.65700  -22.49000 1.000 52.00068  ? 97   LYS   A CG  1 
ATOM   512  C CD  . LYS   A 1 121 ? -60.38200 15.78000  -22.07400 1.000 52.73463  ? 97   LYS   A CD  1 
ATOM   513  C CE  . LYS   A 1 121 ? -60.85500 14.42500  -21.58700 1.000 62.83790  ? 97   LYS   A CE  1 
ATOM   514  N NZ  . LYS   A 1 121 ? -59.71800 13.61500  -21.06700 1.000 71.15866  ? 97   LYS   A NZ  1 
ATOM   515  N N   . MET   A 1 122 ? -59.66300 21.24200  -22.12800 1.000 56.96733  ? 98   MET   A N   1 
ATOM   516  C CA  . MET   A 1 122 ? -58.87300 22.33700  -22.68400 1.000 55.41791  ? 98   MET   A CA  1 
ATOM   517  C C   . MET   A 1 122 ? -58.99100 23.55400  -21.77500 1.000 51.93223  ? 98   MET   A C   1 
ATOM   518  O O   . MET   A 1 122 ? -59.83600 23.60800  -20.87700 1.000 50.24423  ? 98   MET   A O   1 
ATOM   519  C CB  . MET   A 1 122 ? -59.31000 22.68100  -24.11600 1.000 53.91046  ? 98   MET   A CB  1 
ATOM   520  C CG  . MET   A 1 122 ? -60.81200 22.70700  -24.32100 1.000 59.13871  ? 98   MET   A CG  1 
ATOM   521  S SD  . MET   A 1 122 ? -61.63800 24.12300  -23.57300 1.000 88.81612  ? 98   MET   A SD  1 
ATOM   522  C CE  . MET   A 1 122 ? -61.34800 25.39400  -24.79700 1.000 41.88661  ? 98   MET   A CE  1 
ATOM   523  N N   . TRP   A 1 123 ? -58.13200 24.53900  -22.03500 1.000 44.05352  ? 99   TRP   A N   1 
ATOM   524  C CA  . TRP   A 1 123 ? -58.08700 25.78500  -21.27900 1.000 44.18362  ? 99   TRP   A CA  1 
ATOM   525  C C   . TRP   A 1 123 ? -58.90300 26.84400  -22.01100 1.000 44.56042  ? 99   TRP   A C   1 
ATOM   526  O O   . TRP   A 1 123 ? -58.56700 27.21700  -23.13900 1.000 48.33310  ? 99   TRP   A O   1 
ATOM   527  C CB  . TRP   A 1 123 ? -56.64200 26.25000  -21.09400 1.000 38.63842  ? 99   TRP   A CB  1 
ATOM   528  C CG  . TRP   A 1 123 ? -56.53300 27.57400  -20.41900 1.000 39.32457  ? 99   TRP   A CG  1 
ATOM   529  C CD1 . TRP   A 1 123 ? -56.43300 28.79700  -21.01900 1.000 39.89128  ? 99   TRP   A CD1 1 
ATOM   530  C CD2 . TRP   A 1 123 ? -56.51700 27.81700  -19.01000 1.000 44.94555  ? 99   TRP   A CD2 1 
ATOM   531  N NE1 . TRP   A 1 123 ? -56.35800 29.78500  -20.07100 1.000 43.65605  ? 99   TRP   A NE1 1 
ATOM   532  C CE2 . TRP   A 1 123 ? -56.40800 29.21000  -18.82700 1.000 48.07317  ? 99   TRP   A CE2 1 
ATOM   533  C CE3 . TRP   A 1 123 ? -56.59100 26.99200  -17.88300 1.000 40.77306  ? 99   TRP   A CE3 1 
ATOM   534  C CZ2 . TRP   A 1 123 ? -56.37000 29.79500  -17.56400 1.000 42.51463  ? 99   TRP   A CZ2 1 
ATOM   535  C CZ3 . TRP   A 1 123 ? -56.55000 27.57400  -16.63100 1.000 35.62902  ? 99   TRP   A CZ3 1 
ATOM   536  C CH2 . TRP   A 1 123 ? -56.43800 28.96100  -16.48100 1.000 36.93013  ? 99   TRP   A CH2 1 
ATOM   537  N N   . THR   A 1 124 ? -59.95700 27.34300  -21.36100 1.000 41.28485  ? 100  THR   A N   1 
ATOM   538  C CA  . THR   A 1 124 ? -60.91200 28.24200  -22.00000 1.000 43.86550  ? 100  THR   A CA  1 
ATOM   539  C C   . THR   A 1 124 ? -60.75900 29.69900  -21.57900 1.000 40.95860  ? 100  THR   A C   1 
ATOM   540  O O   . THR   A 1 124 ? -61.54800 30.54200  -22.01900 1.000 43.39659  ? 100  THR   A O   1 
ATOM   541  C CB  . THR   A 1 124 ? -62.34700 27.78100  -21.71100 1.000 47.18599  ? 100  THR   A CB  1 
ATOM   542  O OG1 . THR   A 1 124 ? -63.21900 28.23400  -22.75400 1.000 53.13872  ? 100  THR   A OG1 1 
ATOM   543  C CG2 . THR   A 1 124 ? -62.83700 28.34400  -20.38000 1.000 39.47904  ? 100  THR   A CG2 1 
ATOM   544  N N   . PHE   A 1 125 ? -59.76200 30.02700  -20.76200 1.000 41.22763  ? 101  PHE   A N   1 
ATOM   545  C CA  . PHE   A 1 125 ? -59.69700 31.33900  -20.13200 1.000 44.98943  ? 101  PHE   A CA  1 
ATOM   546  C C   . PHE   A 1 125 ? -58.63600 32.24900  -20.74000 1.000 45.18177  ? 101  PHE   A C   1 
ATOM   547  O O   . PHE   A 1 125 ? -58.39100 33.33700  -20.20900 1.000 44.53048  ? 101  PHE   A O   1 
ATOM   548  C CB  . PHE   A 1 125 ? -59.46400 31.18700  -18.62700 1.000 42.21106  ? 101  PHE   A CB  1 
ATOM   549  C CG  . PHE   A 1 125 ? -60.28100 30.08900  -17.99700 1.000 41.65130  ? 101  PHE   A CG  1 
ATOM   550  C CD1 . PHE   A 1 125 ? -59.79500 28.79100  -17.93200 1.000 37.76292  ? 101  PHE   A CD1 1 
ATOM   551  C CD2 . PHE   A 1 125 ? -61.54600 30.34900  -17.49800 1.000 33.30563  ? 101  PHE   A CD2 1 
ATOM   552  C CE1 . PHE   A 1 125 ? -60.54700 27.78100  -17.36200 1.000 38.09981  ? 101  PHE   A CE1 1 
ATOM   553  C CE2 . PHE   A 1 125 ? -62.30100 29.34400  -16.93100 1.000 28.28609  ? 101  PHE   A CE2 1 
ATOM   554  C CZ  . PHE   A 1 125 ? -61.80000 28.05800  -16.86200 1.000 34.11255  ? 101  PHE   A CZ  1 
ATOM   555  N N   . GLY   A 1 126 ? -58.01400 31.84500  -21.84200 1.000 48.26244  ? 102  GLY   A N   1 
ATOM   556  C CA  . GLY   A 1 126 ? -56.99300 32.65300  -22.47200 1.000 52.16115  ? 102  GLY   A CA  1 
ATOM   557  C C   . GLY   A 1 126 ? -55.64200 32.49500  -21.79900 1.000 52.04956  ? 102  GLY   A C   1 
ATOM   558  O O   . GLY   A 1 126 ? -55.50300 31.90000  -20.73000 1.000 48.27824  ? 102  GLY   A O   1 
ATOM   559  N N   . ASN   A 1 127 ? -54.61800 33.05500  -22.44900 1.000 59.17150  ? 103  ASN   A N   1 
ATOM   560  C CA  . ASN   A 1 127 ? -53.24900 32.88700  -21.97500 1.000 55.82434  ? 103  ASN   A CA  1 
ATOM   561  C C   . ASN   A 1 127 ? -52.86700 33.86800  -20.87000 1.000 54.36379  ? 103  ASN   A C   1 
ATOM   562  O O   . ASN   A 1 127 ? -51.89600 33.60900  -20.15000 1.000 53.20199  ? 103  ASN   A O   1 
ATOM   563  C CB  . ASN   A 1 127 ? -52.26000 33.01200  -23.13900 1.000 54.32660  ? 103  ASN   A CB  1 
ATOM   564  C CG  . ASN   A 1 127 ? -52.01600 31.68400  -23.84800 1.000 60.22736  ? 103  ASN   A CG  1 
ATOM   565  O OD1 . ASN   A 1 127 ? -52.11600 30.61400  -23.24300 1.000 59.56063  ? 103  ASN   A OD1 1 
ATOM   566  N ND2 . ASN   A 1 127 ? -51.69700 31.75000  -25.13900 1.000 51.75381  ? 103  ASN   A ND2 1 
ATOM   567  N N   . PHE   A 1 128 ? -53.59000 34.98100  -20.71200 1.000 49.26871  ? 104  PHE   A N   1 
ATOM   568  C CA  . PHE   A 1 128 ? -53.29200 35.88500  -19.60300 1.000 47.10674  ? 104  PHE   A CA  1 
ATOM   569  C C   . PHE   A 1 128 ? -53.61400 35.22300  -18.27100 1.000 51.46008  ? 104  PHE   A C   1 
ATOM   570  O O   . PHE   A 1 128 ? -52.75900 35.13900  -17.38100 1.000 50.61584  ? 104  PHE   A O   1 
ATOM   571  C CB  . PHE   A 1 128 ? -54.06100 37.20200  -19.74500 1.000 46.34647  ? 104  PHE   A CB  1 
ATOM   572  C CG  . PHE   A 1 128 ? -53.84700 38.15700  -18.59100 1.000 52.52095  ? 104  PHE   A CG  1 
ATOM   573  C CD1 . PHE   A 1 128 ? -54.55000 38.00900  -17.39800 1.000 60.30212  ? 104  PHE   A CD1 1 
ATOM   574  C CD2 . PHE   A 1 128 ? -52.94000 39.19700  -18.69500 1.000 61.93112  ? 104  PHE   A CD2 1 
ATOM   575  C CE1 . PHE   A 1 128 ? -54.34700 38.87500  -16.33600 1.000 53.73777  ? 104  PHE   A CE1 1 
ATOM   576  C CE2 . PHE   A 1 128 ? -52.73700 40.07100  -17.63400 1.000 67.95378  ? 104  PHE   A CE2 1 
ATOM   577  C CZ  . PHE   A 1 128 ? -53.44200 39.90800  -16.45500 1.000 54.01050  ? 104  PHE   A CZ  1 
ATOM   578  N N   . TRP   A 1 129 ? -54.85900 34.77400  -18.10100 1.000 48.35151  ? 105  TRP   A N   1 
ATOM   579  C CA  . TRP   A 1 129 ? -55.19800 34.06000  -16.87900 1.000 47.55605  ? 105  TRP   A CA  1 
ATOM   580  C C   . TRP   A 1 129 ? -54.37500 32.78700  -16.75300 1.000 48.11477  ? 105  TRP   A C   1 
ATOM   581  O O   . TRP   A 1 129 ? -54.07000 32.35400  -15.63700 1.000 52.32343  ? 105  TRP   A O   1 
ATOM   582  C CB  . TRP   A 1 129 ? -56.69600 33.74500  -16.83500 1.000 41.70989  ? 105  TRP   A CB  1 
ATOM   583  C CG  . TRP   A 1 129 ? -57.13500 33.10100  -15.54000 1.000 47.56293  ? 105  TRP   A CG  1 
ATOM   584  C CD1 . TRP   A 1 129 ? -57.71900 31.87600  -15.39300 1.000 44.67659  ? 105  TRP   A CD1 1 
ATOM   585  C CD2 . TRP   A 1 129 ? -57.02000 33.64900  -14.21700 1.000 43.30017  ? 105  TRP   A CD2 1 
ATOM   586  N NE1 . TRP   A 1 129 ? -57.97300 31.62600  -14.06600 1.000 39.72356  ? 105  TRP   A NE1 1 
ATOM   587  C CE2 . TRP   A 1 129 ? -57.55500 32.69700  -13.32200 1.000 48.03438  ? 105  TRP   A CE2 1 
ATOM   588  C CE3 . TRP   A 1 129 ? -56.51600 34.84900  -13.70100 1.000 43.23639  ? 105  TRP   A CE3 1 
ATOM   589  C CZ2 . TRP   A 1 129 ? -57.60300 32.90900  -11.93900 1.000 45.63497  ? 105  TRP   A CZ2 1 
ATOM   590  C CZ3 . TRP   A 1 129 ? -56.56600 35.05700  -12.32700 1.000 52.26236  ? 105  TRP   A CZ3 1 
ATOM   591  C CH2 . TRP   A 1 129 ? -57.10600 34.09100  -11.46300 1.000 43.32010  ? 105  TRP   A CH2 1 
ATOM   592  N N   . CYS   A 1 130 ? -53.96800 32.20400  -17.88300 1.000 40.92106  ? 106  CYS   A N   1 
ATOM   593  C CA  . CYS   A 1 130 ? -53.21600 30.95500  -17.85100 1.000 42.96272  ? 106  CYS   A CA  1 
ATOM   594  C C   . CYS   A 1 130 ? -51.87400 31.13100  -17.14900 1.000 47.07503  ? 106  CYS   A C   1 
ATOM   595  O O   . CYS   A 1 130 ? -51.45700 30.27000  -16.36400 1.000 41.65820  ? 106  CYS   A O   1 
ATOM   596  C CB  . CYS   A 1 130 ? -53.02200 30.44400  -19.27600 1.000 48.22079  ? 106  CYS   A CB  1 
ATOM   597  S SG  . CYS   A 1 130 ? -51.68200 29.28800  -19.47600 1.000 35.39540  ? 106  CYS   A SG  1 
ATOM   598  N N   . GLU   A 1 131 ? -51.18600 32.24000  -17.41900 1.000 46.27216  ? 107  GLU   A N   1 
ATOM   599  C CA  . GLU   A 1 131 ? -49.92700 32.51900  -16.73800 1.000 47.15214  ? 107  GLU   A CA  1 
ATOM   600  C C   . GLU   A 1 131 ? -50.16000 33.10100  -15.34900 1.000 48.06587  ? 107  GLU   A C   1 
ATOM   601  O O   . GLU   A 1 131 ? -49.31400 32.93300  -14.46100 1.000 47.02293  ? 107  GLU   A O   1 
ATOM   602  C CB  . GLU   A 1 131 ? -49.07400 33.46500  -17.58700 1.000 50.74004  ? 107  GLU   A CB  1 
ATOM   603  C CG  . GLU   A 1 131 ? -48.18900 32.74800  -18.60700 1.000 46.44082  ? 107  GLU   A CG  1 
ATOM   604  C CD  . GLU   A 1 131 ? -47.09600 33.63800  -19.17400 1.000 56.10263  ? 107  GLU   A CD  1 
ATOM   605  O OE1 . GLU   A 1 131 ? -47.07700 34.84500  -18.84200 1.000 60.88261  ? 107  GLU   A OE1 1 
ATOM   606  O OE2 . GLU   A 1 131 ? -46.26400 33.13400  -19.96400 1.000 48.65740  ? 107  GLU   A OE2 1 
ATOM   607  N N   . PHE   A 1 132 ? -51.29500 33.77800  -15.14500 1.000 50.69068  ? 108  PHE   A N   1 
ATOM   608  C CA  . PHE   A 1 132 ? -51.66600 34.25000  -13.81200 1.000 49.86156  ? 108  PHE   A CA  1 
ATOM   609  C C   . PHE   A 1 132 ? -52.12700 33.10200  -12.92600 1.000 41.48449  ? 108  PHE   A C   1 
ATOM   610  O O   . PHE   A 1 132 ? -51.81200 33.06700  -11.73100 1.000 40.63270  ? 108  PHE   A O   1 
ATOM   611  C CB  . PHE   A 1 132 ? -52.77200 35.29900  -13.91600 1.000 48.04151  ? 108  PHE   A CB  1 
ATOM   612  C CG  . PHE   A 1 132 ? -52.71400 36.35900  -12.85500 1.000 42.21559  ? 108  PHE   A CG  1 
ATOM   613  C CD1 . PHE   A 1 132 ? -51.86100 37.44300  -12.98000 1.000 50.69923  ? 108  PHE   A CD1 1 
ATOM   614  C CD2 . PHE   A 1 132 ? -53.53000 36.28400  -11.74500 1.000 44.95466  ? 108  PHE   A CD2 1 
ATOM   615  C CE1 . PHE   A 1 132 ? -51.82100 38.42600  -12.00700 1.000 48.96372  ? 108  PHE   A CE1 1 
ATOM   616  C CE2 . PHE   A 1 132 ? -53.49600 37.26200  -10.77000 1.000 47.07919  ? 108  PHE   A CE2 1 
ATOM   617  C CZ  . PHE   A 1 132 ? -52.64000 38.33400  -10.90000 1.000 43.57930  ? 108  PHE   A CZ  1 
ATOM   618  N N   . TRP   A 1 133 ? -52.88500 32.16200  -13.49400 1.000 40.01645  ? 109  TRP   A N   1 
ATOM   619  C CA  . TRP   A 1 133 ? -53.40900 31.05200  -12.70800 1.000 39.12508  ? 109  TRP   A CA  1 
ATOM   620  C C   . TRP   A 1 133 ? -52.28300 30.23900  -12.08200 1.000 39.68080  ? 109  TRP   A C   1 
ATOM   621  O O   . TRP   A 1 133 ? -52.36700 29.84300  -10.91500 1.000 48.25505  ? 109  TRP   A O   1 
ATOM   622  C CB  . TRP   A 1 133 ? -54.27900 30.17000  -13.59700 1.000 35.15785  ? 109  TRP   A CB  1 
ATOM   623  C CG  . TRP   A 1 133 ? -54.70100 28.87800  -13.00700 1.000 29.22269  ? 109  TRP   A CG  1 
ATOM   624  C CD1 . TRP   A 1 133 ? -55.46400 28.70100  -11.90000 1.000 28.43242  ? 109  TRP   A CD1 1 
ATOM   625  C CD2 . TRP   A 1 133 ? -54.38600 27.57100  -13.49300 1.000 33.38232  ? 109  TRP   A CD2 1 
ATOM   626  N NE1 . TRP   A 1 133 ? -55.65400 27.36400  -11.66400 1.000 30.04893  ? 109  TRP   A NE1 1 
ATOM   627  C CE2 . TRP   A 1 133 ? -55.00000 26.64600  -12.62700 1.000 31.55669  ? 109  TRP   A CE2 1 
ATOM   628  C CE3 . TRP   A 1 133 ? -53.64500 27.09000  -14.57800 1.000 37.02685  ? 109  TRP   A CE3 1 
ATOM   629  C CZ2 . TRP   A 1 133 ? -54.89700 25.26900  -12.80600 1.000 34.21745  ? 109  TRP   A CZ2 1 
ATOM   630  C CZ3 . TRP   A 1 133 ? -53.54500 25.72100  -14.75700 1.000 38.35555  ? 109  TRP   A CZ3 1 
ATOM   631  C CH2 . TRP   A 1 133 ? -54.16700 24.82700  -13.87500 1.000 41.67236  ? 109  TRP   A CH2 1 
ATOM   632  N N   . THR   A 1 134 ? -51.21200 29.99300  -12.83800 1.000 38.99263  ? 110  THR   A N   1 
ATOM   633  C CA  . THR   A 1 134 ? -50.12100 29.17400  -12.32200 1.000 41.19245  ? 110  THR   A CA  1 
ATOM   634  C C   . THR   A 1 134 ? -49.21700 29.96000  -11.38200 1.000 45.10193  ? 110  THR   A C   1 
ATOM   635  O O   . THR   A 1 134 ? -48.74900 29.41700  -10.37500 1.000 46.85002  ? 110  THR   A O   1 
ATOM   636  C CB  . THR   A 1 134 ? -49.30300 28.58700  -13.47400 1.000 46.16468  ? 110  THR   A CB  1 
ATOM   637  O OG1 . THR   A 1 134 ? -49.04700 29.60400  -14.45300 1.000 55.76101  ? 110  THR   A OG1 1 
ATOM   638  C CG2 . THR   A 1 134 ? -50.04900 27.42700  -14.11800 1.000 49.43241  ? 110  THR   A CG2 1 
ATOM   639  N N   . SER   A 1 135 ? -48.94700 31.23000  -11.69200 1.000 40.75411  ? 111  SER   A N   1 
ATOM   640  C CA  . SER   A 1 135 ? -48.14500 32.03400  -10.77700 1.000 39.98758  ? 111  SER   A CA  1 
ATOM   641  C C   . SER   A 1 135 ? -48.83100 32.18400  -9.42500  1.000 38.41812  ? 111  SER   A C   1 
ATOM   642  O O   . SER   A 1 135 ? -48.15800 32.37300  -8.40600  1.000 44.24411  ? 111  SER   A O   1 
ATOM   643  C CB  . SER   A 1 135 ? -47.85100 33.40100  -11.38900 1.000 39.92868  ? 111  SER   A CB  1 
ATOM   644  O OG  . SER   A 1 135 ? -49.02900 33.99400  -11.89100 1.000 50.76938  ? 111  SER   A OG  1 
ATOM   645  N N   . ILE   A 1 136 ? -50.16100 32.09200  -9.39200  1.000 43.28659  ? 112  ILE   A N   1 
ATOM   646  C CA  . ILE   A 1 136 ? -50.87400 32.02700  -8.12100  1.000 38.73831  ? 112  ILE   A CA  1 
ATOM   647  C C   . ILE   A 1 136 ? -50.73700 30.63700  -7.51100  1.000 37.85916  ? 112  ILE   A C   1 
ATOM   648  O O   . ILE   A 1 136 ? -50.48400 30.49500  -6.30900  1.000 36.93700  ? 112  ILE   A O   1 
ATOM   649  C CB  . ILE   A 1 136 ? -52.35000 32.41500  -8.32200  1.000 34.12199  ? 112  ILE   A CB  1 
ATOM   650  C CG1 . ILE   A 1 136 ? -52.52000 33.92900  -8.25100  1.000 39.05729  ? 112  ILE   A CG1 1 
ATOM   651  C CG2 . ILE   A 1 136 ? -53.21100 31.79100  -7.25800  1.000 36.06467  ? 112  ILE   A CG2 1 
ATOM   652  C CD1 . ILE   A 1 136 ? -53.91900 34.39400  -8.58200  1.000 38.35434  ? 112  ILE   A CD1 1 
ATOM   653  N N   . ASP   A 1 137 ? -50.88300 29.59800  -8.34000  1.000 39.30109  ? 113  ASP   A N   1 
ATOM   654  C CA  . ASP   A 1 137 ? -50.77700 28.22000  -7.86900  1.000 36.50025  ? 113  ASP   A CA  1 
ATOM   655  C C   . ASP   A 1 137 ? -49.47300 28.00300  -7.11400  1.000 35.20042  ? 113  ASP   A C   1 
ATOM   656  O O   . ASP   A 1 137 ? -49.46900 27.47700  -5.99800  1.000 36.34438  ? 113  ASP   A O   1 
ATOM   657  C CB  . ASP   A 1 137 ? -50.89200 27.26800  -9.06500  1.000 36.39152  ? 113  ASP   A CB  1 
ATOM   658  C CG  . ASP   A 1 137 ? -50.71400 25.79900  -8.69300  1.000 38.56096  ? 113  ASP   A CG  1 
ATOM   659  O OD1 . ASP   A 1 137 ? -50.51600 25.47100  -7.50800  1.000 34.47934  ? 113  ASP   A OD1 1 
ATOM   660  O OD2 . ASP   A 1 137 ? -50.75900 24.95500  -9.61400  1.000 42.86022  ? 113  ASP   A OD2 1 
ATOM   661  N N   . VAL   A 1 138 ? -48.35400 28.42500  -7.70200  1.000 44.52158  ? 114  VAL   A N   1 
ATOM   662  C CA  . VAL   A 1 138 ? -47.06900 28.23200  -7.04200  1.000 44.35436  ? 114  VAL   A CA  1 
ATOM   663  C C   . VAL   A 1 138 ? -46.85100 29.22000  -5.90600  1.000 39.57205  ? 114  VAL   A C   1 
ATOM   664  O O   . VAL   A 1 138 ? -46.04800 28.94100  -5.01300  1.000 36.96087  ? 114  VAL   A O   1 
ATOM   665  C CB  . VAL   A 1 138 ? -45.90400 28.32300  -8.04400  1.000 41.07285  ? 114  VAL   A CB  1 
ATOM   666  C CG1 . VAL   A 1 138 ? -46.00000 27.20500  -9.06500  1.000 38.02800  ? 114  VAL   A CG1 1 
ATOM   667  C CG2 . VAL   A 1 138 ? -45.90200 29.67400  -8.73200  1.000 42.04945  ? 114  VAL   A CG2 1 
ATOM   668  N N   . LEU   A 1 139 ? -47.53800 30.36400  -5.91000  1.000 36.32559  ? 115  LEU   A N   1 
ATOM   669  C CA  . LEU   A 1 139 ? -47.43200 31.27900  -4.78100  1.000 32.91779  ? 115  LEU   A CA  1 
ATOM   670  C C   . LEU   A 1 139 ? -48.01100 30.65200  -3.51900  1.000 34.98909  ? 115  LEU   A C   1 
ATOM   671  O O   . LEU   A 1 139 ? -47.46300 30.82300  -2.42500  1.000 33.90789  ? 115  LEU   A O   1 
ATOM   672  C CB  . LEU   A 1 139 ? -48.13800 32.59300  -5.10300  1.000 34.84641  ? 115  LEU   A CB  1 
ATOM   673  C CG  . LEU   A 1 139 ? -48.43900 33.52300  -3.92600  1.000 37.73261  ? 115  LEU   A CG  1 
ATOM   674  C CD1 . LEU   A 1 139 ? -47.16500 33.94700  -3.19700  1.000 33.42422  ? 115  LEU   A CD1 1 
ATOM   675  C CD2 . LEU   A 1 139 ? -49.23100 34.73700  -4.38900  1.000 33.91028  ? 115  LEU   A CD2 1 
ATOM   676  N N   . CYS   A 1 140 ? -49.11100 29.91300  -3.65600  1.000 37.76906  ? 116  CYS   A N   1 
ATOM   677  C CA  . CYS   A 1 140 ? -49.75100 29.29200  -2.50400  1.000 34.91476  ? 116  CYS   A CA  1 
ATOM   678  C C   . CYS   A 1 140 ? -48.96600 28.10100  -1.98200  1.000 32.36091  ? 116  CYS   A C   1 
ATOM   679  O O   . CYS   A 1 140 ? -49.02700 27.80200  -0.78500  1.000 40.80328  ? 116  CYS   A O   1 
ATOM   680  C CB  . CYS   A 1 140 ? -51.16800 28.85100  -2.86300  1.000 32.23610  ? 116  CYS   A CB  1 
ATOM   681  S SG  . CYS   A 1 140 ? -52.33100 30.20300  -3.10000  1.000 45.43216  ? 116  CYS   A SG  1 
ATOM   682  N N   . VAL   A 1 141 ? -48.24000 27.40200  -2.85100  1.000 30.18801  ? 117  VAL   A N   1 
ATOM   683  C CA  . VAL   A 1 141 ? -47.50000 26.23400  -2.39700  1.000 33.18839  ? 117  VAL   A CA  1 
ATOM   684  C C   . VAL   A 1 141 ? -46.16500 26.65700  -1.79200  1.000 34.70896  ? 117  VAL   A C   1 
ATOM   685  O O   . VAL   A 1 141 ? -45.64400 25.99000  -0.89100  1.000 32.39910  ? 117  VAL   A O   1 
ATOM   686  C CB  . VAL   A 1 141 ? -47.32600 25.23700  -3.56000  1.000 34.86644  ? 117  VAL   A CB  1 
ATOM   687  C CG1 . VAL   A 1 141 ? -46.41700 24.07600  -3.16200  1.000 32.35498  ? 117  VAL   A CG1 1 
ATOM   688  C CG2 . VAL   A 1 141 ? -48.68500 24.73200  -4.03600  1.000 34.63220  ? 117  VAL   A CG2 1 
ATOM   689  N N   . THR   A 1 142 ? -45.59800 27.77000  -2.25100  1.000 38.29414  ? 118  THR   A N   1 
ATOM   690  C CA  . THR   A 1 142 ? -44.33400 28.22400  -1.68900  1.000 35.56334  ? 118  THR   A CA  1 
ATOM   691  C C   . THR   A 1 142 ? -44.53600 29.04600  -0.42500  1.000 34.99079  ? 118  THR   A C   1 
ATOM   692  O O   . THR   A 1 142 ? -43.76900 28.89800  0.53100   1.000 41.55096  ? 118  THR   A O   1 
ATOM   693  C CB  . THR   A 1 142 ? -43.54600 29.03500  -2.72100  1.000 34.10396  ? 118  THR   A CB  1 
ATOM   694  O OG1 . THR   A 1 142 ? -44.29000 30.20200  -3.08200  1.000 46.68541  ? 118  THR   A OG1 1 
ATOM   695  C CG2 . THR   A 1 142 ? -43.31800 28.20300  -3.95200  1.000 28.23646  ? 118  THR   A CG2 1 
ATOM   696  N N   . ALA   A 1 143 ? -45.55700 29.90900  -0.39400  1.000 31.88932  ? 119  ALA   A N   1 
ATOM   697  C CA  . ALA   A 1 143 ? -45.86200 30.63500  0.83300   1.000 34.14439  ? 119  ALA   A CA  1 
ATOM   698  C C   . ALA   A 1 143 ? -46.29200 29.70600  1.95900   1.000 33.27346  ? 119  ALA   A C   1 
ATOM   699  O O   . ALA   A 1 143 ? -46.20500 30.09100  3.12800   1.000 34.25238  ? 119  ALA   A O   1 
ATOM   700  C CB  . ALA   A 1 143 ? -46.95100 31.68100  0.59000   1.000 34.37489  ? 119  ALA   A CB  1 
ATOM   701  N N   . SER   A 1 144 ? -46.74100 28.49300  1.63600   1.000 33.63554  ? 120  SER   A N   1 
ATOM   702  C CA  . SER   A 1 144 ? -47.12400 27.53300  2.66500   1.000 31.91584  ? 120  SER   A CA  1 
ATOM   703  C C   . SER   A 1 144 ? -45.90100 26.90200  3.32000   1.000 35.87609  ? 120  SER   A C   1 
ATOM   704  O O   . SER   A 1 144 ? -45.66700 27.07900  4.51900   1.000 40.38036  ? 120  SER   A O   1 
ATOM   705  C CB  . SER   A 1 144 ? -48.02100 26.45200  2.06400   1.000 28.15185  ? 120  SER   A CB  1 
ATOM   706  O OG  . SER   A 1 144 ? -49.26400 27.00600  1.68300   1.000 38.17643  ? 120  SER   A OG  1 
ATOM   707  N N   . ILE   A 1 145 ? -45.10900 26.15800  2.54100   1.000 38.09854  ? 121  ILE   A N   1 
ATOM   708  C CA  . ILE   A 1 145 ? -43.93100 25.49100  3.08900   1.000 36.01687  ? 121  ILE   A CA  1 
ATOM   709  C C   . ILE   A 1 145 ? -43.00100 26.49600  3.74900   1.000 34.38191  ? 121  ILE   A C   1 
ATOM   710  O O   . ILE   A 1 145 ? -42.29400 26.16000  4.70500   1.000 35.50891  ? 121  ILE   A O   1 
ATOM   711  C CB  . ILE   A 1 145 ? -43.21300 24.68300  1.98700   1.000 42.72874  ? 121  ILE   A CB  1 
ATOM   712  C CG1 . ILE   A 1 145 ? -42.19300 23.71200  2.59500   1.000 41.85027  ? 121  ILE   A CG1 1 
ATOM   713  C CG2 . ILE   A 1 145 ? -42.55500 25.60700  0.97500   1.000 39.98212  ? 121  ILE   A CG2 1 
ATOM   714  C CD1 . ILE   A 1 145 ? -42.81000 22.63100  3.45400   1.000 36.17352  ? 121  ILE   A CD1 1 
ATOM   715  N N   . GLU   A 1 146 ? -42.99600 27.74500  3.27500   1.000 33.29239  ? 122  GLU   A N   1 
ATOM   716  C CA  . GLU   A 1 146 ? -42.21400 28.78100  3.94000   1.000 39.92491  ? 122  GLU   A CA  1 
ATOM   717  C C   . GLU   A 1 146 ? -42.82800 29.20200  5.26900   1.000 36.73821  ? 122  GLU   A C   1 
ATOM   718  O O   . GLU   A 1 146 ? -42.13100 29.78600  6.10400   1.000 34.99359  ? 122  GLU   A O   1 
ATOM   719  C CB  . GLU   A 1 146 ? -42.05400 29.99900  3.02800   1.000 38.11447  ? 122  GLU   A CB  1 
ATOM   720  C CG  . GLU   A 1 146 ? -40.97200 29.84100  1.97200   1.000 49.05520  ? 122  GLU   A CG  1 
ATOM   721  C CD  . GLU   A 1 146 ? -40.54600 31.16900  1.37000   1.000 55.10960  ? 122  GLU   A CD  1 
ATOM   722  O OE1 . GLU   A 1 146 ? -41.02200 32.21900  1.85200   1.000 54.27259  ? 122  GLU   A OE1 1 
ATOM   723  O OE2 . GLU   A 1 146 ? -39.74900 31.16500  0.40700   1.000 56.67949  ? 122  GLU   A OE2 1 
ATOM   724  N N   . THR   A 1 147 ? -44.11500 28.93300  5.48100   1.000 37.88826  ? 123  THR   A N   1 
ATOM   725  C CA  . THR   A 1 147 ? -44.73100 29.19400  6.77600   1.000 36.34259  ? 123  THR   A CA  1 
ATOM   726  C C   . THR   A 1 147 ? -44.67400 27.96900  7.68100   1.000 30.71026  ? 123  THR   A C   1 
ATOM   727  O O   . THR   A 1 147 ? -44.34500 28.09200  8.86400   1.000 35.29968  ? 123  THR   A O   1 
ATOM   728  C CB  . THR   A 1 147 ? -46.18100 29.65600  6.59400   1.000 34.84596  ? 123  THR   A CB  1 
ATOM   729  O OG1 . THR   A 1 147 ? -46.19800 30.92600  5.92700   1.000 28.72035  ? 123  THR   A OG1 1 
ATOM   730  C CG2 . THR   A 1 147 ? -46.87500 29.78700  7.94200   1.000 27.95860  ? 123  THR   A CG2 1 
ATOM   731  N N   . LEU   A 1 148 ? -44.96300 26.78500  7.13600   1.000 29.51613  ? 124  LEU   A N   1 
ATOM   732  C CA  . LEU   A 1 148 ? -44.79200 25.54600  7.88500   1.000 28.75996  ? 124  LEU   A CA  1 
ATOM   733  C C   . LEU   A 1 148 ? -43.35700 25.34600  8.34000   1.000 34.06195  ? 124  LEU   A C   1 
ATOM   734  O O   . LEU   A 1 148 ? -43.11000 24.56000  9.26000   1.000 39.33762  ? 124  LEU   A O   1 
ATOM   735  C CB  . LEU   A 1 148 ? -45.22200 24.35200  7.03900   1.000 28.31609  ? 124  LEU   A CB  1 
ATOM   736  C CG  . LEU   A 1 148 ? -46.72200 24.09200  7.02000   1.000 30.33315  ? 124  LEU   A CG  1 
ATOM   737  C CD1 . LEU   A 1 148 ? -47.05200 22.94000  6.08700   1.000 31.58534  ? 124  LEU   A CD1 1 
ATOM   738  C CD2 . LEU   A 1 148 ? -47.20300 23.81300  8.42900   1.000 40.97040  ? 124  LEU   A CD2 1 
ATOM   739  N N   . CYS   A 1 149 ? -42.40600 26.02400  7.70700   1.000 41.28571  ? 125  CYS   A N   1 
ATOM   740  C CA  . CYS   A 1 149 ? -41.01600 25.97600  8.12900   1.000 41.10277  ? 125  CYS   A CA  1 
ATOM   741  C C   . CYS   A 1 149 ? -40.69000 27.06000  9.15000   1.000 38.64162  ? 125  CYS   A C   1 
ATOM   742  O O   . CYS   A 1 149 ? -39.77300 26.87800  9.95800   1.000 39.95863  ? 125  CYS   A O   1 
ATOM   743  C CB  . CYS   A 1 149 ? -40.10800 26.09000  6.89500   1.000 33.16351  ? 125  CYS   A CB  1 
ATOM   744  S SG  . CYS   A 1 149 ? -38.34800 26.25400  7.18400   1.000 36.73245  ? 125  CYS   A SG  1 
ATOM   745  N N   . VAL   A 1 150 ? -41.43900 28.16600  9.14900   1.000 35.24593  ? 126  VAL   A N   1 
ATOM   746  C CA  . VAL   A 1 150 ? -41.28800 29.17800  10.19200  1.000 36.71492  ? 126  VAL   A CA  1 
ATOM   747  C C   . VAL   A 1 150 ? -41.89000 28.68900  11.50500  1.000 40.19860  ? 126  VAL   A C   1 
ATOM   748  O O   . VAL   A 1 150 ? -41.33300 28.92700  12.58500  1.000 39.70898  ? 126  VAL   A O   1 
ATOM   749  C CB  . VAL   A 1 150 ? -41.91800 30.50800  9.73700   1.000 35.69820  ? 126  VAL   A CB  1 
ATOM   750  C CG1 . VAL   A 1 150 ? -42.16800 31.42700  10.92400  1.000 26.49884  ? 126  VAL   A CG1 1 
ATOM   751  C CG2 . VAL   A 1 150 ? -41.01800 31.19000  8.71900   1.000 38.19103  ? 126  VAL   A CG2 1 
ATOM   752  N N   . ILE   A 1 151 ? -43.03300 27.99800  11.43400  1.000 34.22881  ? 127  ILE   A N   1 
ATOM   753  C CA  . ILE   A 1 151 ? -43.63200 27.39900  12.62500  1.000 32.79958  ? 127  ILE   A CA  1 
ATOM   754  C C   . ILE   A 1 151 ? -42.62100 26.50500  13.33000  1.000 38.94111  ? 127  ILE   A C   1 
ATOM   755  O O   . ILE   A 1 151 ? -42.38200 26.63200  14.53700  1.000 39.15358  ? 127  ILE   A O   1 
ATOM   756  C CB  . ILE   A 1 151 ? -44.89600 26.60600  12.25000  1.000 32.06725  ? 127  ILE   A CB  1 
ATOM   757  C CG1 . ILE   A 1 151 ? -46.02700 27.54100  11.83000  1.000 27.28137  ? 127  ILE   A CG1 1 
ATOM   758  C CG2 . ILE   A 1 151 ? -45.33100 25.72000  13.41300  1.000 34.98412  ? 127  ILE   A CG2 1 
ATOM   759  C CD1 . ILE   A 1 151 ? -47.15200 26.82100  11.12500  1.000 28.00787  ? 127  ILE   A CD1 1 
ATOM   760  N N   . ALA   A 1 152 ? -42.01100 25.58600  12.57600  1.000 43.15616  ? 128  ALA   A N   1 
ATOM   761  C CA  . ALA   A 1 152 ? -41.07700 24.63100  13.16200  1.000 40.78954  ? 128  ALA   A CA  1 
ATOM   762  C C   . ALA   A 1 152 ? -39.88000 25.32400  13.79600  1.000 37.33193  ? 128  ALA   A C   1 
ATOM   763  O O   . ALA   A 1 152 ? -39.34400 24.83800  14.79700  1.000 40.64922  ? 128  ALA   A O   1 
ATOM   764  C CB  . ALA   A 1 152 ? -40.61100 23.63600  12.10000  1.000 40.02224  ? 128  ALA   A CB  1 
ATOM   765  N N   . VAL   A 1 153 ? -39.44400 26.45100  13.23500  1.000 37.51148  ? 129  VAL   A N   1 
ATOM   766  C CA  . VAL   A 1 153 ? -38.34400 27.18500  13.84800  1.000 35.21748  ? 129  VAL   A CA  1 
ATOM   767  C C   . VAL   A 1 153 ? -38.84400 28.02400  15.01600  1.000 34.23004  ? 129  VAL   A C   1 
ATOM   768  O O   . VAL   A 1 153 ? -38.14600 28.16100  16.02700  1.000 44.64944  ? 129  VAL   A O   1 
ATOM   769  C CB  . VAL   A 1 153 ? -37.61500 28.03600  12.79300  1.000 33.98955  ? 129  VAL   A CB  1 
ATOM   770  C CG1 . VAL   A 1 153 ? -36.83000 29.15800  13.44400  1.000 28.16839  ? 129  VAL   A CG1 1 
ATOM   771  C CG2 . VAL   A 1 153 ? -36.67800 27.16200  11.97900  1.000 28.56495  ? 129  VAL   A CG2 1 
ATOM   772  N N   . ASP   A 1 154 ? -40.05800 28.57200  14.92200  1.000 36.41678  ? 130  ASP   A N   1 
ATOM   773  C CA  . ASP   A 1 154 ? -40.60400 29.33500  16.04200  1.000 42.08196  ? 130  ASP   A CA  1 
ATOM   774  C C   . ASP   A 1 154 ? -40.86800 28.43400  17.24500  1.000 41.24931  ? 130  ASP   A C   1 
ATOM   775  O O   . ASP   A 1 154 ? -40.56200 28.80600  18.38600  1.000 29.95433  ? 130  ASP   A O   1 
ATOM   776  C CB  . ASP   A 1 154 ? -41.88300 30.05300  15.62100  1.000 35.60027  ? 130  ASP   A CB  1 
ATOM   777  C CG  . ASP   A 1 154 ? -42.62500 30.64100  16.79600  1.000 38.47744  ? 130  ASP   A CG  1 
ATOM   778  O OD1 . ASP   A 1 154 ? -42.12300 31.63000  17.37000  1.000 38.83306  ? 130  ASP   A OD1 1 
ATOM   779  O OD2 . ASP   A 1 154 ? -43.69700 30.10700  17.15600  1.000 36.39037  ? 130  ASP   A OD2 1 
ATOM   780  N N   . ARG   A 1 155 ? -41.42900 27.24200  17.00900  1.000 38.55797  ? 131  ARG   A N   1 
ATOM   781  C CA  . ARG   A 1 155 ? -41.58900 26.26200  18.07700  1.000 33.02939  ? 131  ARG   A CA  1 
ATOM   782  C C   . ARG   A 1 155 ? -40.25700 25.74100  18.59600  1.000 37.91461  ? 131  ARG   A C   1 
ATOM   783  O O   . ARG   A 1 155 ? -40.22800 25.11800  19.66200  1.000 40.37584  ? 131  ARG   A O   1 
ATOM   784  C CB  . ARG   A 1 155 ? -42.45200 25.08300  17.61400  1.000 32.10792  ? 131  ARG   A CB  1 
ATOM   785  C CG  . ARG   A 1 155 ? -43.91800 25.41600  17.34300  1.000 37.27700  ? 131  ARG   A CG  1 
ATOM   786  C CD  . ARG   A 1 155 ? -44.62100 25.96900  18.57500  1.000 28.34447  ? 131  ARG   A CD  1 
ATOM   787  N NE  . ARG   A 1 155 ? -44.44800 27.41000  18.70200  1.000 29.74614  ? 131  ARG   A NE  1 
ATOM   788  C CZ  . ARG   A 1 155 ? -44.82900 28.12100  19.75300  1.000 33.07833  ? 131  ARG   A CZ  1 
ATOM   789  N NH1 . ARG   A 1 155 ? -45.43700 27.55800  20.78600  1.000 30.83835  ? 131  ARG   A NH1 1 
ATOM   790  N NH2 . ARG   A 1 155 ? -44.59100 29.42900  19.77100  1.000 30.52033  ? 131  ARG   A NH2 1 
ATOM   791  N N   . TYR   A 1 156 ? -39.15400 25.96500  17.87400  1.000 43.94052  ? 132  TYR   A N   1 
ATOM   792  C CA  . TYR   A 1 156 ? -37.86500 25.58100  18.43600  1.000 42.20615  ? 132  TYR   A CA  1 
ATOM   793  C C   . TYR   A 1 156 ? -37.35600 26.63700  19.40100  1.000 46.34340  ? 132  TYR   A C   1 
ATOM   794  O O   . TYR   A 1 156 ? -36.82500 26.30400  20.46600  1.000 49.41254  ? 132  TYR   A O   1 
ATOM   795  C CB  . TYR   A 1 156 ? -36.82800 25.33100  17.34400  1.000 40.75027  ? 132  TYR   A CB  1 
ATOM   796  C CG  . TYR   A 1 156 ? -35.54500 24.75700  17.91200  1.000 46.54481  ? 132  TYR   A CG  1 
ATOM   797  C CD1 . TYR   A 1 156 ? -35.38700 23.38500  18.06000  1.000 49.23835  ? 132  TYR   A CD1 1 
ATOM   798  C CD2 . TYR   A 1 156 ? -34.50500 25.58400  18.32500  1.000 41.09067  ? 132  TYR   A CD2 1 
ATOM   799  C CE1 . TYR   A 1 156 ? -34.22800 22.84900  18.58900  1.000 49.43207  ? 132  TYR   A CE1 1 
ATOM   800  C CE2 . TYR   A 1 156 ? -33.34300 25.05800  18.85700  1.000 37.99991  ? 132  TYR   A CE2 1 
ATOM   801  C CZ  . TYR   A 1 156 ? -33.20900 23.69100  18.98700  1.000 48.99422  ? 132  TYR   A CZ  1 
ATOM   802  O OH  . TYR   A 1 156 ? -32.05300 23.16100  19.51800  1.000 57.42768  ? 132  TYR   A OH  1 
ATOM   803  N N   . PHE   A 1 157 ? -37.51200 27.91200  19.05600  1.000 39.16260  ? 133  PHE   A N   1 
ATOM   804  C CA  . PHE   A 1 157 ? -37.15600 28.95200  20.00800  1.000 52.17752  ? 133  PHE   A CA  1 
ATOM   805  C C   . PHE   A 1 157 ? -38.15400 29.05500  21.16000  1.000 55.96865  ? 133  PHE   A C   1 
ATOM   806  O O   . PHE   A 1 157 ? -37.89900 29.79400  22.11900  1.000 41.07085  ? 133  PHE   A O   1 
ATOM   807  C CB  . PHE   A 1 157 ? -37.01300 30.28100  19.27000  1.000 36.68355  ? 133  PHE   A CB  1 
ATOM   808  C CG  . PHE   A 1 157 ? -35.63800 30.50000  18.71200  1.000 53.02926  ? 133  PHE   A CG  1 
ATOM   809  C CD1 . PHE   A 1 157 ? -35.25500 29.88900  17.52600  1.000 58.22656  ? 133  PHE   A CD1 1 
ATOM   810  C CD2 . PHE   A 1 157 ? -34.71700 31.29700  19.37800  1.000 61.67136  ? 133  PHE   A CD2 1 
ATOM   811  C CE1 . PHE   A 1 157 ? -33.98100 30.07800  17.00800  1.000 52.02102  ? 133  PHE   A CE1 1 
ATOM   812  C CE2 . PHE   A 1 157 ? -33.44100 31.49300  18.86600  1.000 54.46420  ? 133  PHE   A CE2 1 
ATOM   813  C CZ  . PHE   A 1 157 ? -33.07300 30.88300  17.67800  1.000 49.74796  ? 133  PHE   A CZ  1 
ATOM   814  N N   . ALA   A 1 158 ? -39.26500 28.31700  21.09900  1.000 49.53292  ? 134  ALA   A N   1 
ATOM   815  C CA  . ALA   A 1 158 ? -40.22500 28.26700  22.19200  1.000 42.04486  ? 134  ALA   A CA  1 
ATOM   816  C C   . ALA   A 1 158 ? -39.90000 27.16800  23.19400  1.000 49.84683  ? 134  ALA   A C   1 
ATOM   817  O O   . ALA   A 1 158 ? -40.12000 27.34800  24.39600  1.000 50.59662  ? 134  ALA   A O   1 
ATOM   818  C CB  . ALA   A 1 158 ? -41.64300 28.06700  21.64600  1.000 32.75186  ? 134  ALA   A CB  1 
ATOM   819  N N   . ILE   A 1 159 ? -39.37600 26.02900  22.72600  1.000 43.52146  ? 135  ILE   A N   1 
ATOM   820  C CA  . ILE   A 1 159 ? -39.09000 24.90800  23.61700  1.000 44.63795  ? 135  ILE   A CA  1 
ATOM   821  C C   . ILE   A 1 159 ? -37.68400 24.98900  24.20500  1.000 52.53604  ? 135  ILE   A C   1 
ATOM   822  O O   . ILE   A 1 159 ? -37.27300 24.09700  24.96100  1.000 49.95627  ? 135  ILE   A O   1 
ATOM   823  C CB  . ILE   A 1 159 ? -39.32900 23.57700  22.87300  1.000 40.61003  ? 135  ILE   A CB  1 
ATOM   824  C CG1 . ILE   A 1 159 ? -39.47500 22.41600  23.85600  1.000 44.54054  ? 135  ILE   A CG1 1 
ATOM   825  C CG2 . ILE   A 1 159 ? -38.20100 23.29600  21.89800  1.000 40.72557  ? 135  ILE   A CG2 1 
ATOM   826  C CD1 . ILE   A 1 159 ? -40.46400 21.38700  23.40800  1.000 44.85602  ? 135  ILE   A CD1 1 
ATOM   827  N N   . THR   A 1 160 ? -36.93400 26.04100  23.88800  1.000 50.79955  ? 136  THR   A N   1 
ATOM   828  C CA  . THR   A 1 160 ? -35.63000 26.28600  24.48800  1.000 42.59901  ? 136  THR   A CA  1 
ATOM   829  C C   . THR   A 1 160 ? -35.65300 27.48300  25.42400  1.000 45.17862  ? 136  THR   A C   1 
ATOM   830  O O   . THR   A 1 160 ? -34.59000 27.97000  25.82500  1.000 58.25502  ? 136  THR   A O   1 
ATOM   831  C CB  . THR   A 1 160 ? -34.57700 26.50200  23.40100  1.000 47.94539  ? 136  THR   A CB  1 
ATOM   832  O OG1 . THR   A 1 160 ? -34.85100 27.72600  22.70400  1.000 43.77813  ? 136  THR   A OG1 1 
ATOM   833  C CG2 . THR   A 1 160 ? -34.58500 25.34300  22.42000  1.000 43.82204  ? 136  THR   A CG2 1 
ATOM   834  N N   . SER   A 1 161 ? -36.83400 27.96800  25.76800  1.000 35.49427  ? 137  SER   A N   1 
ATOM   835  C CA  . SER   A 1 161 ? -37.00600 29.15100  26.59400  1.000 39.62544  ? 137  SER   A CA  1 
ATOM   836  C C   . SER   A 1 161 ? -37.78800 28.68000  27.82100  1.000 47.46820  ? 137  SER   A C   1 
ATOM   837  O O   . SER   A 1 161 ? -38.32700 27.56600  27.78700  1.000 42.71280  ? 137  SER   A O   1 
ATOM   838  C CB  . SER   A 1 161 ? -37.71300 30.23300  25.77200  1.000 44.35123  ? 137  SER   A CB  1 
ATOM   839  O OG  . SER   A 1 161 ? -37.51500 31.53800  26.27800  1.000 42.64199  ? 137  SER   A OG  1 
ATOM   840  N N   . PRO   A 1 162 ? -37.85700 29.46000  28.94100  1.000 49.72875  ? 138  PRO   A N   1 
ATOM   841  C CA  . PRO   A 1 162 ? -38.43500 28.91200  30.18400  1.000 46.91925  ? 138  PRO   A CA  1 
ATOM   842  C C   . PRO   A 1 162 ? -39.81300 28.28700  30.01900  1.000 49.51602  ? 138  PRO   A C   1 
ATOM   843  O O   . PRO   A 1 162 ? -40.00400 27.10700  30.33400  1.000 48.53868  ? 138  PRO   A O   1 
ATOM   844  C CB  . PRO   A 1 162 ? -38.48700 30.13100  31.12000  1.000 47.58504  ? 138  PRO   A CB  1 
ATOM   845  C CG  . PRO   A 1 162 ? -38.36300 31.31900  30.22900  1.000 58.17515  ? 138  PRO   A CG  1 
ATOM   846  C CD  . PRO   A 1 162 ? -37.46700 30.86900  29.12100  1.000 49.77804  ? 138  PRO   A CD  1 
ATOM   847  N N   . PHE   A 1 163 ? -40.78100 29.05900  29.53400  1.000 51.34647  ? 139  PHE   A N   1 
ATOM   848  C CA  . PHE   A 1 163 ? -42.07900 28.49900  29.18000  1.000 43.22930  ? 139  PHE   A CA  1 
ATOM   849  C C   . PHE   A 1 163 ? -41.90500 27.73100  27.87600  1.000 54.14912  ? 139  PHE   A C   1 
ATOM   850  O O   . PHE   A 1 163 ? -41.64000 28.32800  26.82500  1.000 58.22430  ? 139  PHE   A O   1 
ATOM   851  C CB  . PHE   A 1 163 ? -43.11100 29.62000  29.07000  1.000 38.05623  ? 139  PHE   A CB  1 
ATOM   852  C CG  . PHE   A 1 163 ? -44.53900 29.14900  29.05400  1.000 46.35411  ? 139  PHE   A CG  1 
ATOM   853  C CD1 . PHE   A 1 163 ? -45.10800 28.61500  27.90800  1.000 43.98998  ? 139  PHE   A CD1 1 
ATOM   854  C CD2 . PHE   A 1 163 ? -45.31300 29.23000  30.20600  1.000 53.96600  ? 139  PHE   A CD2 1 
ATOM   855  C CE1 . PHE   A 1 163 ? -46.43100 28.19100  27.90600  1.000 45.40740  ? 139  PHE   A CE1 1 
ATOM   856  C CE2 . PHE   A 1 163 ? -46.63500 28.80200  30.21400  1.000 42.22644  ? 139  PHE   A CE2 1 
ATOM   857  C CZ  . PHE   A 1 163 ? -47.19400 28.28400  29.06300  1.000 51.33254  ? 139  PHE   A CZ  1 
ATOM   858  N N   . LYS   A 1 164 ? -42.01000 26.40100  27.94700  1.000 45.03449  ? 140  LYS   A N   1 
ATOM   859  C CA  . LYS   A 1 164 ? -41.61400 25.54700  26.82900  1.000 47.36438  ? 140  LYS   A CA  1 
ATOM   860  C C   . LYS   A 1 164 ? -42.42500 25.78600  25.56000  1.000 50.59773  ? 140  LYS   A C   1 
ATOM   861  O O   . LYS   A 1 164 ? -42.05100 25.26300  24.50400  1.000 52.02282  ? 140  LYS   A O   1 
ATOM   862  C CB  . LYS   A 1 164 ? -41.73300 24.07500  27.22500  1.000 45.21668  ? 140  LYS   A CB  1 
ATOM   863  C CG  . LYS   A 1 164 ? -40.57400 23.54200  28.04400  1.000 52.16290  ? 140  LYS   A CG  1 
ATOM   864  C CD  . LYS   A 1 164 ? -40.57500 22.02100  28.02200  1.000 52.39884  ? 140  LYS   A CD  1 
ATOM   865  C CE  . LYS   A 1 164 ? -40.42200 21.43600  29.41500  1.000 50.20666  ? 140  LYS   A CE  1 
ATOM   866  N NZ  . LYS   A 1 164 ? -40.81100 20.00100  29.41800  1.000 57.61437  ? 140  LYS   A NZ  1 
ATOM   867  N N   . TYR   A 1 165 ? -43.52000 26.54900  25.63000  1.000 47.29702  ? 141  TYR   A N   1 
ATOM   868  C CA  . TYR   A 1 165 ? -44.42800 26.70200  24.50000  1.000 32.17891  ? 141  TYR   A CA  1 
ATOM   869  C C   . TYR   A 1 165 ? -44.74100 28.16600  24.21800  1.000 32.87598  ? 141  TYR   A C   1 
ATOM   870  O O   . TYR   A 1 165 ? -45.76500 28.46700  23.60000  1.000 34.96369  ? 141  TYR   A O   1 
ATOM   871  C CB  . TYR   A 1 165 ? -45.71100 25.91700  24.76000  1.000 31.32630  ? 141  TYR   A CB  1 
ATOM   872  C CG  . TYR   A 1 165 ? -45.43300 24.60900  25.45400  1.000 36.10446  ? 141  TYR   A CG  1 
ATOM   873  C CD1 . TYR   A 1 165 ? -44.72900 23.59800  24.81700  1.000 36.90670  ? 141  TYR   A CD1 1 
ATOM   874  C CD2 . TYR   A 1 165 ? -45.81400 24.41200  26.77200  1.000 39.31870  ? 141  TYR   A CD2 1 
ATOM   875  C CE1 . TYR   A 1 165 ? -44.44800 22.40800  25.46200  1.000 41.78248  ? 141  TYR   A CE1 1 
ATOM   876  C CE2 . TYR   A 1 165 ? -45.53800 23.22900  27.42300  1.000 47.04186  ? 141  TYR   A CE2 1 
ATOM   877  C CZ  . TYR   A 1 165 ? -44.85600 22.22900  26.76500  1.000 46.71521  ? 141  TYR   A CZ  1 
ATOM   878  O OH  . TYR   A 1 165 ? -44.58200 21.05300  27.42700  1.000 51.92566  ? 141  TYR   A OH  1 
ATOM   879  N N   . GLN   A 1 166 ? -43.87600 29.08000  24.64300  1.000 30.64915  ? 142  GLN   A N   1 
ATOM   880  C CA  . GLN   A 1 166 ? -44.07000 30.50600  24.42200  1.000 33.12118  ? 142  GLN   A CA  1 
ATOM   881  C C   . GLN   A 1 166 ? -43.19700 30.96300  23.25700  1.000 44.31205  ? 142  GLN   A C   1 
ATOM   882  O O   . GLN   A 1 166 ? -41.96900 30.82200  23.29900  1.000 44.01668  ? 142  GLN   A O   1 
ATOM   883  C CB  . GLN   A 1 166 ? -43.74000 31.29400  25.68800  1.000 34.89659  ? 142  GLN   A CB  1 
ATOM   884  C CG  . GLN   A 1 166 ? -44.14500 32.75700  25.64900  1.000 32.22812  ? 142  GLN   A CG  1 
ATOM   885  C CD  . GLN   A 1 166 ? -43.65900 33.52000  26.86900  1.000 38.78026  ? 142  GLN   A CD  1 
ATOM   886  O OE1 . GLN   A 1 166 ? -42.91700 32.98500  27.69500  1.000 40.56525  ? 142  GLN   A OE1 1 
ATOM   887  N NE2 . GLN   A 1 166 ? -44.08000 34.77500  26.99100  1.000 35.08065  ? 142  GLN   A NE2 1 
ATOM   888  N N   . SER   A 1 167 ? -43.83100 31.49200  22.21500  1.000 41.21196  ? 143  SER   A N   1 
ATOM   889  C CA  . SER   A 1 167 ? -43.08500 32.12500  21.13900  1.000 34.66868  ? 143  SER   A CA  1 
ATOM   890  C C   . SER   A 1 167 ? -42.26600 33.28400  21.68800  1.000 36.11072  ? 143  SER   A C   1 
ATOM   891  O O   . SER   A 1 167 ? -42.70200 33.99500  22.59400  1.000 37.36874  ? 143  SER   A O   1 
ATOM   892  C CB  . SER   A 1 167 ? -44.04000 32.62600  20.05500  1.000 27.62039  ? 143  SER   A CB  1 
ATOM   893  O OG  . SER   A 1 167 ? -43.33100 33.11700  18.93200  1.000 35.00864  ? 143  SER   A OG  1 
ATOM   894  N N   . LEU   A 1 168 ? -41.06600 33.46900  21.14300  1.000 35.59472  ? 144  LEU   A N   1 
ATOM   895  C CA  . LEU   A 1 168 ? -40.27700 34.63800  21.50700  1.000 32.26291  ? 144  LEU   A CA  1 
ATOM   896  C C   . LEU   A 1 168 ? -40.64700 35.86300  20.68200  1.000 32.92371  ? 144  LEU   A C   1 
ATOM   897  O O   . LEU   A 1 168 ? -40.02300 36.91500  20.84800  1.000 30.16077  ? 144  LEU   A O   1 
ATOM   898  C CB  . LEU   A 1 168 ? -38.78500 34.33700  21.35800  1.000 30.46252  ? 144  LEU   A CB  1 
ATOM   899  C CG  . LEU   A 1 168 ? -38.28900 33.01000  21.94200  1.000 36.31560  ? 144  LEU   A CG  1 
ATOM   900  C CD1 . LEU   A 1 168 ? -36.80700 32.85000  21.70000  1.000 34.01717  ? 144  LEU   A CD1 1 
ATOM   901  C CD2 . LEU   A 1 168 ? -38.58900 32.90300  23.42300  1.000 34.38005  ? 144  LEU   A CD2 1 
ATOM   902  N N   . LEU   A 1 169 ? -41.65700 35.75300  19.82300  1.000 38.69371  ? 145  LEU   A N   1 
ATOM   903  C CA  . LEU   A 1 169 ? -42.05400 36.80600  18.90000  1.000 39.79130  ? 145  LEU   A CA  1 
ATOM   904  C C   . LEU   A 1 169 ? -43.21900 37.62400  19.45100  1.000 42.52598  ? 145  LEU   A C   1 
ATOM   905  O O   . LEU   A 1 169 ? -44.10700 37.10100  20.12900  1.000 42.14728  ? 145  LEU   A O   1 
ATOM   906  C CB  . LEU   A 1 169 ? -42.45600 36.20800  17.54900  1.000 39.47259  ? 145  LEU   A CB  1 
ATOM   907  C CG  . LEU   A 1 169 ? -41.39900 35.51500  16.68700  1.000 37.36927  ? 145  LEU   A CG  1 
ATOM   908  C CD1 . LEU   A 1 169 ? -42.05400 34.51300  15.74200  1.000 30.98882  ? 145  LEU   A CD1 1 
ATOM   909  C CD2 . LEU   A 1 169 ? -40.60400 36.54500  15.90300  1.000 31.78722  ? 145  LEU   A CD2 1 
ATOM   910  N N   . THR   A 1 170 ? -43.20200 38.92000  19.14900  1.000 39.82490  ? 146  THR   A N   1 
ATOM   911  C CA  . THR   A 1 170 ? -44.36500 39.76900  19.34400  1.000 36.25352  ? 146  THR   A CA  1 
ATOM   912  C C   . THR   A 1 170 ? -45.44400 39.38400  18.33700  1.000 41.64040  ? 146  THR   A C   1 
ATOM   913  O O   . THR   A 1 170 ? -45.17200 38.73400  17.32600  1.000 48.76202  ? 146  THR   A O   1 
ATOM   914  C CB  . THR   A 1 170 ? -43.97800 41.24000  19.16700  1.000 42.21809  ? 146  THR   A CB  1 
ATOM   915  O OG1 . THR   A 1 170 ? -42.83100 41.52600  19.97200  1.000 55.51636  ? 146  THR   A OG1 1 
ATOM   916  C CG2 . THR   A 1 170 ? -45.10300 42.17600  19.58400  1.000 48.66506  ? 146  THR   A CG2 1 
ATOM   917  N N   . LYS   A 1 171 ? -46.68900 39.76900  18.63000  1.000 40.75148  ? 147  LYS   A N   1 
ATOM   918  C CA  . LYS   A 1 171 ? -47.73900 39.66600  17.62100  1.000 48.93420  ? 147  LYS   A CA  1 
ATOM   919  C C   . LYS   A 1 171 ? -47.37500 40.47300  16.38100  1.000 52.81292  ? 147  LYS   A C   1 
ATOM   920  O O   . LYS   A 1 171 ? -47.50100 39.99000  15.24900  1.000 48.42014  ? 147  LYS   A O   1 
ATOM   921  C CB  . LYS   A 1 171 ? -49.07500 40.14500  18.18800  1.000 55.88347  ? 147  LYS   A CB  1 
ATOM   922  C CG  . LYS   A 1 171 ? -49.72000 39.21900  19.20100  1.000 58.95219  ? 147  LYS   A CG  1 
ATOM   923  C CD  . LYS   A 1 171 ? -50.97700 39.86400  19.77000  1.000 65.39060  ? 147  LYS   A CD  1 
ATOM   924  C CE  . LYS   A 1 171 ? -51.42100 39.21100  21.06600  1.000 62.37575  ? 147  LYS   A CE  1 
ATOM   925  N NZ  . LYS   A 1 171 ? -52.54900 39.96700  21.67500  1.000 65.95170  ? 147  LYS   A NZ  1 
ATOM   926  N N   . ASN   A 1 172 ? -46.91500 41.71100  16.58000  1.000 56.35528  ? 148  ASN   A N   1 
ATOM   927  C CA  . ASN   A 1 172 ? -46.56600 42.57200  15.45400  1.000 51.79235  ? 148  ASN   A CA  1 
ATOM   928  C C   . ASN   A 1 172 ? -45.38600 42.00700  14.67500  1.000 47.34786  ? 148  ASN   A C   1 
ATOM   929  O O   . ASN   A 1 172 ? -45.41100 41.95600  13.44100  1.000 45.65190  ? 148  ASN   A O   1 
ATOM   930  C CB  . ASN   A 1 172 ? -46.25600 43.98000  15.95800  1.000 50.79828  ? 148  ASN   A CB  1 
ATOM   931  C CG  . ASN   A 1 172 ? -47.47800 44.67700  16.51400  1.000 61.14590  ? 148  ASN   A CG  1 
ATOM   932  O OD1 . ASN   A 1 172 ? -48.40000 45.02100  15.77500  1.000 64.20251  ? 148  ASN   A OD1 1 
ATOM   933  N ND2 . ASN   A 1 172 ? -47.50100 44.87400  17.82700  1.000 71.20431  ? 148  ASN   A ND2 1 
ATOM   934  N N   . LYS   A 1 173 ? -44.33800 41.58100  15.38200  1.000 47.00094  ? 149  LYS   A N   1 
ATOM   935  C CA  . LYS   A 1 173 ? -43.22200 40.93300  14.70700  1.000 45.20507  ? 149  LYS   A CA  1 
ATOM   936  C C   . LYS   A 1 173 ? -43.66700 39.64700  14.02800  1.000 47.85671  ? 149  LYS   A C   1 
ATOM   937  O O   . LYS   A 1 173 ? -43.14900 39.29600  12.96000  1.000 47.27287  ? 149  LYS   A O   1 
ATOM   938  C CB  . LYS   A 1 173 ? -42.09000 40.66000  15.70000  1.000 47.50667  ? 149  LYS   A CB  1 
ATOM   939  C CG  . LYS   A 1 173 ? -41.48500 41.92700  16.28600  1.000 52.70802  ? 149  LYS   A CG  1 
ATOM   940  C CD  . LYS   A 1 173 ? -40.43400 41.62800  17.34100  1.000 57.66800  ? 149  LYS   A CD  1 
ATOM   941  C CE  . LYS   A 1 173 ? -39.89500 42.91800  17.94700  1.000 65.64924  ? 149  LYS   A CE  1 
ATOM   942  N NZ  . LYS   A 1 173 ? -38.81600 42.67800  18.94400  1.000 74.49186  ? 149  LYS   A NZ  1 
ATOM   943  N N   . ALA   A 1 174 ? -44.63800 38.94300  14.61700  1.000 41.88430  ? 150  ALA   A N   1 
ATOM   944  C CA  . ALA   A 1 174 ? -45.15900 37.74100  13.97800  1.000 43.65382  ? 150  ALA   A CA  1 
ATOM   945  C C   . ALA   A 1 174 ? -45.81100 38.05300  12.64000  1.000 43.40137  ? 150  ALA   A C   1 
ATOM   946  O O   . ALA   A 1 174 ? -45.75100 37.23300  11.71800  1.000 42.26530  ? 150  ALA   A O   1 
ATOM   947  C CB  . ALA   A 1 174 ? -46.16300 37.03900  14.89100  1.000 38.45918  ? 150  ALA   A CB  1 
ATOM   948  N N   . ARG   A 1 175 ? -46.42400 39.22800  12.50400  1.000 40.15278  ? 151  ARG   A N   1 
ATOM   949  C CA  . ARG   A 1 175 ? -47.18900 39.53000  11.30600  1.000 41.11950  ? 151  ARG   A CA  1 
ATOM   950  C C   . ARG   A 1 175 ? -46.45400 40.41500  10.30400  1.000 43.85711  ? 151  ARG   A C   1 
ATOM   951  O O   . ARG   A 1 175 ? -46.96300 40.60800  9.19600   1.000 48.68794  ? 151  ARG   A O   1 
ATOM   952  C CB  . ARG   A 1 175 ? -48.53700 40.16700  11.67600  1.000 45.42050  ? 151  ARG   A CB  1 
ATOM   953  C CG  . ARG   A 1 175 ? -48.46100 41.56100  12.24600  1.000 49.81695  ? 151  ARG   A CG  1 
ATOM   954  C CD  . ARG   A 1 175 ? -49.86300 42.11900  12.43900  1.000 53.66353  ? 151  ARG   A CD  1 
ATOM   955  N NE  . ARG   A 1 175 ? -50.61500 41.42600  13.48000  1.000 60.43061  ? 151  ARG   A NE  1 
ATOM   956  C CZ  . ARG   A 1 175 ? -50.88300 41.94200  14.67300  1.000 64.19151  ? 151  ARG   A CZ  1 
ATOM   957  N NH1 . ARG   A 1 175 ? -50.45500 43.14600  15.01500  1.000 63.57353  ? 151  ARG   A NH1 1 
ATOM   958  N NH2 . ARG   A 1 175 ? -51.60500 41.23700  15.54000  1.000 62.13720  ? 151  ARG   A NH2 1 
ATOM   959  N N   . VAL   A 1 176 ? -45.28100 40.95600  10.64300  1.000 46.29255  ? 152  VAL   A N   1 
ATOM   960  C CA  . VAL   A 1 176 ? -44.42400 41.45300  9.56900   1.000 40.12617  ? 152  VAL   A CA  1 
ATOM   961  C C   . VAL   A 1 176 ? -43.66200 40.29400  8.94700   1.000 36.24500  ? 152  VAL   A C   1 
ATOM   962  O O   . VAL   A 1 176 ? -43.35900 40.31800  7.75000   1.000 40.74680  ? 152  VAL   A O   1 
ATOM   963  C CB  . VAL   A 1 176 ? -43.46300 42.55900  10.04400  1.000 35.55009  ? 152  VAL   A CB  1 
ATOM   964  C CG1 . VAL   A 1 176 ? -44.23900 43.75300  10.57500  1.000 44.51863  ? 152  VAL   A CG1 1 
ATOM   965  C CG2 . VAL   A 1 176 ? -42.49700 42.02700  11.08800  1.000 36.89672  ? 152  VAL   A CG2 1 
ATOM   966  N N   . ILE   A 1 177 ? -43.35500 39.26000  9.73400   1.000 37.08224  ? 153  ILE   A N   1 
ATOM   967  C CA  . ILE   A 1 177 ? -42.75600 38.05300  9.17600   1.000 34.86492  ? 153  ILE   A CA  1 
ATOM   968  C C   . ILE   A 1 177 ? -43.71100 37.39800  8.19100   1.000 33.61582  ? 153  ILE   A C   1 
ATOM   969  O O   . ILE   A 1 177 ? -43.28100 36.85500  7.16600   1.000 37.70145  ? 153  ILE   A O   1 
ATOM   970  C CB  . ILE   A 1 177 ? -42.34300 37.09400  10.31300  1.000 35.36874  ? 153  ILE   A CB  1 
ATOM   971  C CG1 . ILE   A 1 177 ? -41.11900 37.64000  11.04700  1.000 30.62107  ? 153  ILE   A CG1 1 
ATOM   972  C CG2 . ILE   A 1 177 ? -42.04700 35.70300  9.78100   1.000 28.64999  ? 153  ILE   A CG2 1 
ATOM   973  C CD1 . ILE   A 1 177 ? -40.71200 36.81500  12.23600  1.000 28.79844  ? 153  ILE   A CD1 1 
ATOM   974  N N   . ILE   A 1 178 ? -45.01700 37.46300  8.46200   1.000 31.59186  ? 154  ILE   A N   1 
ATOM   975  C CA  . ILE   A 1 178 ? -45.99800 36.91000  7.53200   1.000 34.68318  ? 154  ILE   A CA  1 
ATOM   976  C C   . ILE   A 1 178 ? -46.02600 37.72300  6.24400   1.000 39.02358  ? 154  ILE   A C   1 
ATOM   977  O O   . ILE   A 1 178 ? -45.94900 37.17000  5.13900   1.000 36.23661  ? 154  ILE   A O   1 
ATOM   978  C CB  . ILE   A 1 178 ? -47.38800 36.84700  8.19000   1.000 35.21403  ? 154  ILE   A CB  1 
ATOM   979  C CG1 . ILE   A 1 178 ? -47.36100 35.89700  9.38700   1.000 34.95070  ? 154  ILE   A CG1 1 
ATOM   980  C CG2 . ILE   A 1 178 ? -48.43900 36.40700  7.17900   1.000 28.20260  ? 154  ILE   A CG2 1 
ATOM   981  C CD1 . ILE   A 1 178 ? -48.62200 35.91700  10.21700  1.000 36.74883  ? 154  ILE   A CD1 1 
ATOM   982  N N   . LEU   A 1 179 ? -46.14300 39.04900  6.36900   1.000 38.06948  ? 155  LEU   A N   1 
ATOM   983  C CA  . LEU   A 1 179 ? -46.07600 39.92700  5.20400   1.000 33.36532  ? 155  LEU   A CA  1 
ATOM   984  C C   . LEU   A 1 179 ? -44.82800 39.65000  4.38000   1.000 36.62052  ? 155  LEU   A C   1 
ATOM   985  O O   . LEU   A 1 179 ? -44.89200 39.53300  3.15100   1.000 35.01077  ? 155  LEU   A O   1 
ATOM   986  C CB  . LEU   A 1 179 ? -46.10500 41.38800  5.65400   1.000 31.25566  ? 155  LEU   A CB  1 
ATOM   987  C CG  . LEU   A 1 179 ? -46.20800 42.44200  4.55100   1.000 39.32924  ? 155  LEU   A CG  1 
ATOM   988  C CD1 . LEU   A 1 179 ? -47.56900 42.39200  3.87800   1.000 48.06383  ? 155  LEU   A CD1 1 
ATOM   989  C CD2 . LEU   A 1 179 ? -45.94300 43.82600  5.12500   1.000 47.27743  ? 155  LEU   A CD2 1 
ATOM   990  N N   . MET   A 1 180 ? -43.67900 39.53500  5.04900   1.000 35.77431  ? 156  MET   A N   1 
ATOM   991  C CA  . MET   A 1 180 ? -42.43600 39.23400  4.35100   1.000 35.59607  ? 156  MET   A CA  1 
ATOM   992  C C   . MET   A 1 180 ? -42.54200 37.93400  3.56900   1.000 40.16849  ? 156  MET   A C   1 
ATOM   993  O O   . MET   A 1 180 ? -42.19600 37.88300  2.38200   1.000 43.35088  ? 156  MET   A O   1 
ATOM   994  C CB  . MET   A 1 180 ? -41.28100 39.15700  5.34500   1.000 37.44508  ? 156  MET   A CB  1 
ATOM   995  C CG  . MET   A 1 180 ? -40.80100 40.49400  5.84700   1.000 42.93746  ? 156  MET   A CG  1 
ATOM   996  S SD  . MET   A 1 180 ? -39.33100 40.29600  6.86500   1.000 55.87267  ? 156  MET   A SD  1 
ATOM   997  C CE  . MET   A 1 180 ? -39.10500 41.97200  7.45700   1.000 47.65650  ? 156  MET   A CE  1 
ATOM   998  N N   . VAL   A 1 181 ? -43.00900 36.86800  4.22500   1.000 34.37734  ? 157  VAL   A N   1 
ATOM   999  C CA  . VAL   A 1 181 ? -43.07800 35.56500  3.57000   1.000 33.72077  ? 157  VAL   A CA  1 
ATOM   1000 C C   . VAL   A 1 181 ? -43.90600 35.64800  2.29700   1.000 37.71944  ? 157  VAL   A C   1 
ATOM   1001 O O   . VAL   A 1 181 ? -43.54900 35.06000  1.27000   1.000 38.52921  ? 157  VAL   A O   1 
ATOM   1002 C CB  . VAL   A 1 181 ? -43.63000 34.50500  4.53900   1.000 32.43922  ? 157  VAL   A CB  1 
ATOM   1003 C CG1 . VAL   A 1 181 ? -44.05400 33.26300  3.77700   1.000 35.64880  ? 157  VAL   A CG1 1 
ATOM   1004 C CG2 . VAL   A 1 181 ? -42.58200 34.15100  5.57700   1.000 28.31021  ? 157  VAL   A CG2 1 
ATOM   1005 N N   . TRP   A 1 182 ? -45.00000 36.41100  2.32500   1.000 35.98142  ? 158  TRP   A N   1 
ATOM   1006 C CA  . TRP   A 1 182 ? -45.83700 36.51200  1.13400   1.000 35.45435  ? 158  TRP   A CA  1 
ATOM   1007 C C   . TRP   A 1 182 ? -45.16900 37.35900  0.05800   1.000 31.79200  ? 158  TRP   A C   1 
ATOM   1008 O O   . TRP   A 1 182 ? -45.17600 36.98400  -1.11900  1.000 35.38503  ? 158  TRP   A O   1 
ATOM   1009 C CB  . TRP   A 1 182 ? -47.21400 37.06500  1.49900   1.000 32.40104  ? 158  TRP   A CB  1 
ATOM   1010 C CG  . TRP   A 1 182 ? -48.13400 35.99200  1.97300   1.000 25.77562  ? 158  TRP   A CG  1 
ATOM   1011 C CD1 . TRP   A 1 182 ? -48.33000 35.59800  3.25900   1.000 30.94667  ? 158  TRP   A CD1 1 
ATOM   1012 C CD2 . TRP   A 1 182 ? -48.94700 35.13700  1.16300   1.000 30.30005  ? 158  TRP   A CD2 1 
ATOM   1013 N NE1 . TRP   A 1 182 ? -49.23400 34.56800  3.30800   1.000 37.00798  ? 158  TRP   A NE1 1 
ATOM   1014 C CE2 . TRP   A 1 182 ? -49.62600 34.26400  2.03200   1.000 37.18943  ? 158  TRP   A CE2 1 
ATOM   1015 C CE3 . TRP   A 1 182 ? -49.17500 35.03200  -0.21300  1.000 36.66084  ? 158  TRP   A CE3 1 
ATOM   1016 C CZ2 . TRP   A 1 182 ? -50.52100 33.30000  1.57300   1.000 38.17322  ? 158  TRP   A CZ2 1 
ATOM   1017 C CZ3 . TRP   A 1 182 ? -50.06400 34.07100  -0.66700  1.000 33.55261  ? 158  TRP   A CZ3 1 
ATOM   1018 C CH2 . TRP   A 1 182 ? -50.72500 33.21900  0.22400   1.000 39.68073  ? 158  TRP   A CH2 1 
ATOM   1019 N N   . ILE   A 1 183 ? -44.58200 38.49900  0.43900   1.000 33.83808  ? 159  ILE   A N   1 
ATOM   1020 C CA  . ILE   A 1 183 ? -43.81100 39.30100  -0.51400  1.000 37.78321  ? 159  ILE   A CA  1 
ATOM   1021 C C   . ILE   A 1 183 ? -42.73100 38.44700  -1.16600  1.000 37.46790  ? 159  ILE   A C   1 
ATOM   1022 O O   . ILE   A 1 183 ? -42.68700 38.29100  -2.39100  1.000 37.93953  ? 159  ILE   A O   1 
ATOM   1023 C CB  . ILE   A 1 183 ? -43.19800 40.53400  0.17300   1.000 33.08930  ? 159  ILE   A CB  1 
ATOM   1024 C CG1 . ILE   A 1 183 ? -44.28900 41.48600  0.66100   1.000 33.06401  ? 159  ILE   A CG1 1 
ATOM   1025 C CG2 . ILE   A 1 183 ? -42.25500 41.25200  -0.77800  1.000 30.93003  ? 159  ILE   A CG2 1 
ATOM   1026 C CD1 . ILE   A 1 183 ? -43.75800 42.69300  1.40300   1.000 28.25679  ? 159  ILE   A CD1 1 
ATOM   1027 N N   . VAL   A 1 184 ? -41.85400 37.86600  -0.34400  1.000 35.46585  ? 160  VAL   A N   1 
ATOM   1028 C CA  . VAL   A 1 184 ? -40.74400 37.07500  -0.86800  1.000 38.40331  ? 160  VAL   A CA  1 
ATOM   1029 C C   . VAL   A 1 184 ? -41.25900 35.91900  -1.71900  1.000 39.55260  ? 160  VAL   A C   1 
ATOM   1030 O O   . VAL   A 1 184 ? -40.78300 35.69500  -2.83800  1.000 40.83518  ? 160  VAL   A O   1 
ATOM   1031 C CB  . VAL   A 1 184 ? -39.85000 36.57600  0.28100   1.000 37.35690  ? 160  VAL   A CB  1 
ATOM   1032 C CG1 . VAL   A 1 184 ? -39.04300 35.37100  -0.16300  1.000 35.05728  ? 160  VAL   A CG1 1 
ATOM   1033 C CG2 . VAL   A 1 184 ? -38.92200 37.68700  0.73800   1.000 30.45389  ? 160  VAL   A CG2 1 
ATOM   1034 N N   . SER   A 1 185 ? -42.24000 35.17100  -1.20700  1.000 38.47030  ? 161  SER   A N   1 
ATOM   1035 C CA  . SER   A 1 185 ? -42.74300 34.02200  -1.95600  1.000 40.08852  ? 161  SER   A CA  1 
ATOM   1036 C C   . SER   A 1 185 ? -43.33900 34.45400  -3.28700  1.000 37.15585  ? 161  SER   A C   1 
ATOM   1037 O O   . SER   A 1 185 ? -43.22100 33.74100  -4.29100  1.000 34.79348  ? 161  SER   A O   1 
ATOM   1038 C CB  . SER   A 1 185 ? -43.77800 33.25300  -1.13800  1.000 37.06417  ? 161  SER   A CB  1 
ATOM   1039 O OG  . SER   A 1 185 ? -43.15200 32.32700  -0.26900  1.000 35.14171  ? 161  SER   A OG  1 
ATOM   1040 N N   . GLY   A 1 186 ? -43.98600 35.62100  -3.31400  1.000 34.97763  ? 162  GLY   A N   1 
ATOM   1041 C CA  . GLY   A 1 186 ? -44.55100 36.11200  -4.55900  1.000 34.60117  ? 162  GLY   A CA  1 
ATOM   1042 C C   . GLY   A 1 186 ? -43.48800 36.47500  -5.57400  1.000 39.61524  ? 162  GLY   A C   1 
ATOM   1043 O O   . GLY   A 1 186 ? -43.61000 36.15000  -6.75800  1.000 43.43723  ? 162  GLY   A O   1 
ATOM   1044 N N   . LEU   A 1 187 ? -42.41900 37.13300  -5.12400  1.000 41.59897  ? 163  LEU   A N   1 
ATOM   1045 C CA  . LEU   A 1 187 ? -41.35800 37.54800  -6.03400  1.000 39.52750  ? 163  LEU   A CA  1 
ATOM   1046 C C   . LEU   A 1 187 ? -40.51400 36.37900  -6.52500  1.000 41.35388  ? 163  LEU   A C   1 
ATOM   1047 O O   . LEU   A 1 187 ? -39.84600 36.50800  -7.55500  1.000 50.87684  ? 163  LEU   A O   1 
ATOM   1048 C CB  . LEU   A 1 187 ? -40.47200 38.60100  -5.36500  1.000 39.91022  ? 163  LEU   A CB  1 
ATOM   1049 C CG  . LEU   A 1 187 ? -40.93000 40.06700  -5.41000  1.000 43.34264  ? 163  LEU   A CG  1 
ATOM   1050 C CD1 . LEU   A 1 187 ? -42.38900 40.25700  -5.01300  1.000 49.16700  ? 163  LEU   A CD1 1 
ATOM   1051 C CD2 . LEU   A 1 187 ? -40.03900 40.91300  -4.51700  1.000 45.36234  ? 163  LEU   A CD2 1 
ATOM   1052 N N   . THR   A 1 188 ? -40.52500 35.24800  -5.82500  1.000 35.79597  ? 164  THR   A N   1 
ATOM   1053 C CA  . THR   A 1 188 ? -39.86900 34.04100  -6.30600  1.000 38.43093  ? 164  THR   A CA  1 
ATOM   1054 C C   . THR   A 1 188 ? -40.83900 33.09400  -6.99800  1.000 41.37148  ? 164  THR   A C   1 
ATOM   1055 O O   . THR   A 1 188 ? -40.50600 31.92400  -7.21700  1.000 38.13249  ? 164  THR   A O   1 
ATOM   1056 C CB  . THR   A 1 188 ? -39.17000 33.32400  -5.15500  1.000 38.45103  ? 164  THR   A CB  1 
ATOM   1057 O OG1 . THR   A 1 188 ? -40.15500 32.79500  -4.26200  1.000 49.97601  ? 164  THR   A OG1 1 
ATOM   1058 C CG2 . THR   A 1 188 ? -38.27600 34.29100  -4.40300  1.000 34.55912  ? 164  THR   A CG2 1 
ATOM   1059 N N   . SER   A 1 189 ? -42.03400 33.57400  -7.34100  1.000 44.99093  ? 165  SER   A N   1 
ATOM   1060 C CA  . SER   A 1 189 ? -43.01700 32.76000  -8.04300  1.000 47.90271  ? 165  SER   A CA  1 
ATOM   1061 C C   . SER   A 1 189 ? -43.60600 33.54300  -9.20400  1.000 42.67722  ? 165  SER   A C   1 
ATOM   1062 O O   . SER   A 1 189 ? -43.54200 33.09800  -10.35100 1.000 49.84589  ? 165  SER   A O   1 
ATOM   1063 C CB  . SER   A 1 189 ? -44.12800 32.30000  -7.09700  1.000 45.16272  ? 165  SER   A CB  1 
ATOM   1064 O OG  . SER   A 1 189 ? -44.57000 33.36500  -6.27600  1.000 48.73025  ? 165  SER   A OG  1 
ATOM   1065 N N   . PHE   A 1 190 ? -44.17600 34.71500  -8.92300  1.000 37.35011  ? 166  PHE   A N   1 
ATOM   1066 C CA  . PHE   A 1 190 ? -44.74600 35.52100  -9.99700  1.000 38.15706  ? 166  PHE   A CA  1 
ATOM   1067 C C   . PHE   A 1 190 ? -43.66700 36.01800  -10.95100 1.000 44.87224  ? 166  PHE   A C   1 
ATOM   1068 O O   . PHE   A 1 190 ? -43.82600 35.94000  -12.17400 1.000 53.85990  ? 166  PHE   A O   1 
ATOM   1069 C CB  . PHE   A 1 190 ? -45.53700 36.69300  -9.41900  1.000 37.99236  ? 166  PHE   A CB  1 
ATOM   1070 C CG  . PHE   A 1 190 ? -46.98700 36.37800  -9.17400  1.000 48.08414  ? 166  PHE   A CG  1 
ATOM   1071 C CD1 . PHE   A 1 190 ? -47.40100 35.82200  -7.97500  1.000 47.90510  ? 166  PHE   A CD1 1 
ATOM   1072 C CD2 . PHE   A 1 190 ? -47.93500 36.63700  -10.14600 1.000 44.34831  ? 166  PHE   A CD2 1 
ATOM   1073 C CE1 . PHE   A 1 190 ? -48.73000 35.53200  -7.75800  1.000 38.64586  ? 166  PHE   A CE1 1 
ATOM   1074 C CE2 . PHE   A 1 190 ? -49.26100 36.34800  -9.93100  1.000 41.49979  ? 166  PHE   A CE2 1 
ATOM   1075 C CZ  . PHE   A 1 190 ? -49.65800 35.79500  -8.73800  1.000 38.94166  ? 166  PHE   A CZ  1 
ATOM   1076 N N   . LEU   A 1 191 ? -42.55600 36.51900  -10.41400 1.000 43.37082  ? 167  LEU   A N   1 
ATOM   1077 C CA  . LEU   A 1 191 ? -41.54400 37.13400  -11.27000 1.000 41.02561  ? 167  LEU   A CA  1 
ATOM   1078 C C   . LEU   A 1 191 ? -40.96900 36.17500  -12.30600 1.000 44.27063  ? 167  LEU   A C   1 
ATOM   1079 O O   . LEU   A 1 191 ? -40.91100 36.55400  -13.48800 1.000 44.80732  ? 167  LEU   A O   1 
ATOM   1080 C CB  . LEU   A 1 191 ? -40.44600 37.75800  -10.40400 1.000 40.58174  ? 167  LEU   A CB  1 
ATOM   1081 C CG  . LEU   A 1 191 ? -40.64400 39.23700  -10.07900 1.000 41.08592  ? 167  LEU   A CG  1 
ATOM   1082 C CD1 . LEU   A 1 191 ? -39.65300 39.69900  -9.02600  1.000 49.09171  ? 167  LEU   A CD1 1 
ATOM   1083 C CD2 . LEU   A 1 191 ? -40.51400 40.06900  -11.34000 1.000 36.94660  ? 167  LEU   A CD2 1 
ATOM   1084 N N   . PRO   A 1 192 ? -40.53500 34.95300  -11.96900 1.000 46.23472  ? 168  PRO   A N   1 
ATOM   1085 C CA  . PRO   A 1 192 ? -39.95900 34.08700  -13.01500 1.000 45.18547  ? 168  PRO   A CA  1 
ATOM   1086 C C   . PRO   A 1 192 ? -40.95900 33.61500  -14.05900 1.000 48.47877  ? 168  PRO   A C   1 
ATOM   1087 O O   . PRO   A 1 192 ? -40.53000 33.19100  -15.13900 1.000 48.01317  ? 168  PRO   A O   1 
ATOM   1088 C CB  . PRO   A 1 192 ? -39.38700 32.90400  -12.22400 1.000 43.75916  ? 168  PRO   A CB  1 
ATOM   1089 C CG  . PRO   A 1 192 ? -39.16100 33.43600  -10.85700 1.000 48.10688  ? 168  PRO   A CG  1 
ATOM   1090 C CD  . PRO   A 1 192 ? -40.30100 34.38900  -10.62700 1.000 47.63951  ? 168  PRO   A CD  1 
ATOM   1091 N N   . ILE   A 1 193 ? -42.26100 33.65800  -13.78400 1.000 46.73016  ? 169  ILE   A N   1 
ATOM   1092 C CA  . ILE   A 1 193 ? -43.26000 33.26800  -14.78200 1.000 41.27601  ? 169  ILE   A CA  1 
ATOM   1093 C C   . ILE   A 1 193 ? -43.75200 34.46800  -15.58000 1.000 38.31285  ? 169  ILE   A C   1 
ATOM   1094 O O   . ILE   A 1 193 ? -43.81400 34.42400  -16.81300 1.000 39.69834  ? 169  ILE   A O   1 
ATOM   1095 C CB  . ILE   A 1 193 ? -44.43500 32.51300  -14.12000 1.000 37.95327  ? 169  ILE   A CB  1 
ATOM   1096 C CG1 . ILE   A 1 193 ? -44.02900 31.07900  -13.76900 1.000 42.42261  ? 169  ILE   A CG1 1 
ATOM   1097 C CG2 . ILE   A 1 193 ? -45.65700 32.51900  -15.02800 1.000 43.91619  ? 169  ILE   A CG2 1 
ATOM   1098 C CD1 . ILE   A 1 193 ? -43.51200 30.90200  -12.38800 1.000 45.44551  ? 169  ILE   A CD1 1 
ATOM   1099 N N   . GLN   A 1 194 ? -44.10900 35.55700  -14.89900 1.000 36.44959  ? 170  GLN   A N   1 
ATOM   1100 C CA  . GLN   A 1 194 ? -44.54100 36.75100  -15.61300 1.000 44.82005  ? 170  GLN   A CA  1 
ATOM   1101 C C   . GLN   A 1 194 ? -43.42000 37.34000  -16.46400 1.000 45.75450  ? 170  GLN   A C   1 
ATOM   1102 O O   . GLN   A 1 194 ? -43.70500 38.02700  -17.44900 1.000 47.14578  ? 170  GLN   A O   1 
ATOM   1103 C CB  . GLN   A 1 194 ? -45.06200 37.79500  -14.62000 1.000 42.78965  ? 170  GLN   A CB  1 
ATOM   1104 C CG  . GLN   A 1 194 ? -46.28200 37.34600  -13.80400 1.000 46.72710  ? 170  GLN   A CG  1 
ATOM   1105 C CD  . GLN   A 1 194 ? -47.55800 37.20400  -14.62600 1.000 55.51701  ? 170  GLN   A CD  1 
ATOM   1106 O OE1 . GLN   A 1 194 ? -47.84100 38.01100  -15.51400 1.000 58.61164  ? 170  GLN   A OE1 1 
ATOM   1107 N NE2 . GLN   A 1 194 ? -48.33700 36.17100  -14.32600 1.000 49.49551  ? 170  GLN   A NE2 1 
ATOM   1108 N N   . MET   A 1 195 ? -42.16000 37.07700  -16.10700 1.000 47.23667  ? 171  MET   A N   1 
ATOM   1109 C CA  . MET   A 1 195 ? -40.99400 37.46800  -16.89300 1.000 40.56683  ? 171  MET   A CA  1 
ATOM   1110 C C   . MET   A 1 195 ? -40.53600 36.37800  -17.85400 1.000 41.93647  ? 171  MET   A C   1 
ATOM   1111 O O   . MET   A 1 195 ? -39.48400 36.53200  -18.48300 1.000 42.48185  ? 171  MET   A O   1 
ATOM   1112 C CB  . MET   A 1 195 ? -39.82300 37.83600  -15.97500 1.000 38.61666  ? 171  MET   A CB  1 
ATOM   1113 C CG  . MET   A 1 195 ? -39.95500 39.16500  -15.26500 1.000 37.18450  ? 171  MET   A CG  1 
ATOM   1114 S SD  . MET   A 1 195 ? -40.32300 40.51100  -16.39900 1.000 45.60879  ? 171  MET   A SD  1 
ATOM   1115 C CE  . MET   A 1 195 ? -38.88700 40.47100  -17.47100 1.000 52.42351  ? 171  MET   A CE  1 
ATOM   1116 N N   . HIS   A 1 196 ? -41.27700 35.27200  -17.94600 1.000 43.28350  ? 172  HIS   A N   1 
ATOM   1117 C CA  . HIS   A 1 196 ? -41.06100 34.20100  -18.91600 1.000 43.25551  ? 172  HIS   A CA  1 
ATOM   1118 C C   . HIS   A 1 196 ? -39.76500 33.42900  -18.69200 1.000 44.56632  ? 172  HIS   A C   1 
ATOM   1119 O O   . HIS   A 1 196 ? -39.31400 32.71400  -19.59600 1.000 43.66876  ? 172  HIS   A O   1 
ATOM   1120 C CB  . HIS   A 1 196 ? -41.09800 34.74400  -20.34900 1.000 49.97965  ? 172  HIS   A CB  1 
ATOM   1121 C CG  . HIS   A 1 196 ? -42.47900 35.01900  -20.85500 1.000 53.92736  ? 172  HIS   A CG  1 
ATOM   1122 N ND1 . HIS   A 1 196 ? -43.27300 36.01900  -20.33600 1.000 58.50991  ? 172  HIS   A ND1 1 
ATOM   1123 C CD2 . HIS   A 1 196 ? -43.19600 34.44500  -21.84800 1.000 54.17414  ? 172  HIS   A CD2 1 
ATOM   1124 C CE1 . HIS   A 1 196 ? -44.43000 36.03600  -20.97500 1.000 58.23858  ? 172  HIS   A CE1 1 
ATOM   1125 N NE2 . HIS   A 1 196 ? -44.40900 35.09100  -21.89800 1.000 59.28998  ? 172  HIS   A NE2 1 
ATOM   1126 N N   . TRP   A 1 197 ? -39.15200 33.53400  -17.50600 1.000 42.06200  ? 173  TRP   A N   1 
ATOM   1127 C CA  . TRP   A 1 197 ? -37.93400 32.77200  -17.24200 1.000 39.43287  ? 173  TRP   A CA  1 
ATOM   1128 C C   . TRP   A 1 197 ? -38.19000 31.27400  -17.17400 1.000 37.12882  ? 173  TRP   A C   1 
ATOM   1129 O O   . TRP   A 1 197 ? -37.23600 30.49300  -17.25200 1.000 41.37655  ? 173  TRP   A O   1 
ATOM   1130 C CB  . TRP   A 1 197 ? -37.27200 33.21000  -15.93700 1.000 39.90199  ? 173  TRP   A CB  1 
ATOM   1131 C CG  . TRP   A 1 197 ? -36.93700 34.66600  -15.83200 1.000 42.35799  ? 173  TRP   A CG  1 
ATOM   1132 C CD1 . TRP   A 1 197 ? -37.02300 35.61100  -16.81400 1.000 44.28195  ? 173  TRP   A CD1 1 
ATOM   1133 C CD2 . TRP   A 1 197 ? -36.46000 35.34200  -14.66500 1.000 43.86487  ? 173  TRP   A CD2 1 
ATOM   1134 N NE1 . TRP   A 1 197 ? -36.62800 36.83500  -16.32700 1.000 40.12209  ? 173  TRP   A NE1 1 
ATOM   1135 C CE2 . TRP   A 1 197 ? -36.27900 36.69600  -15.01000 1.000 42.64614  ? 173  TRP   A CE2 1 
ATOM   1136 C CE3 . TRP   A 1 197 ? -36.16900 34.93200  -13.35900 1.000 40.82222  ? 173  TRP   A CE3 1 
ATOM   1137 C CZ2 . TRP   A 1 197 ? -35.82000 37.64200  -14.09700 1.000 49.96059  ? 173  TRP   A CZ2 1 
ATOM   1138 C CZ3 . TRP   A 1 197 ? -35.71100 35.86900  -12.45800 1.000 37.74846  ? 173  TRP   A CZ3 1 
ATOM   1139 C CH2 . TRP   A 1 197 ? -35.54200 37.20900  -12.82800 1.000 45.58832  ? 173  TRP   A CH2 1 
ATOM   1140 N N   . TYR   A 1 198 ? -39.44400 30.85300  -17.01700 1.000 31.28445  ? 174  TYR   A N   1 
ATOM   1141 C CA  . TYR   A 1 198 ? -39.73800 29.42800  -16.99000 1.000 37.87634  ? 174  TYR   A CA  1 
ATOM   1142 C C   . TYR   A 1 198 ? -39.76000 28.81600  -18.37900 1.000 37.45367  ? 174  TYR   A C   1 
ATOM   1143 O O   . TYR   A 1 198 ? -39.67600 27.58900  -18.50000 1.000 37.56177  ? 174  TYR   A O   1 
ATOM   1144 C CB  . TYR   A 1 198 ? -41.09300 29.16000  -16.32000 1.000 44.71331  ? 174  TYR   A CB  1 
ATOM   1145 C CG  . TYR   A 1 198 ? -42.29600 29.51300  -17.17800 1.000 40.31567  ? 174  TYR   A CG  1 
ATOM   1146 C CD1 . TYR   A 1 198 ? -42.61400 30.83600  -17.46800 1.000 38.10924  ? 174  TYR   A CD1 1 
ATOM   1147 C CD2 . TYR   A 1 198 ? -43.09000 28.51600  -17.72900 1.000 36.15326  ? 174  TYR   A CD2 1 
ATOM   1148 C CE1 . TYR   A 1 198 ? -43.70400 31.15400  -18.25900 1.000 38.61881  ? 174  TYR   A CE1 1 
ATOM   1149 C CE2 . TYR   A 1 198 ? -44.17700 28.82200  -18.52300 1.000 39.13505  ? 174  TYR   A CE2 1 
ATOM   1150 C CZ  . TYR   A 1 198 ? -44.48400 30.14100  -18.78700 1.000 45.29247  ? 174  TYR   A CZ  1 
ATOM   1151 O OH  . TYR   A 1 198 ? -45.57500 30.44400  -19.58000 1.000 42.51551  ? 174  TYR   A OH  1 
ATOM   1152 N N   . ARG   A 1 199 ? -39.85000 29.64500  -19.41800 1.000 35.93943  ? 175  ARG   A N   1 
ATOM   1153 C CA  . ARG   A 1 199 ? -40.26100 29.17900  -20.73600 1.000 44.10359  ? 175  ARG   A CA  1 
ATOM   1154 C C   . ARG   A 1 199 ? -39.27200 28.17400  -21.31800 1.000 45.96431  ? 175  ARG   A C   1 
ATOM   1155 O O   . ARG   A 1 199 ? -38.05300 28.36100  -21.25300 1.000 42.37572  ? 175  ARG   A O   1 
ATOM   1156 C CB  . ARG   A 1 199 ? -40.41600 30.37300  -21.68100 1.000 51.43524  ? 175  ARG   A CB  1 
ATOM   1157 C CG  . ARG   A 1 199 ? -41.64400 31.24000  -21.40600 1.000 45.29722  ? 175  ARG   A CG  1 
ATOM   1158 C CD  . ARG   A 1 199 ? -42.90500 30.54400  -21.86700 1.000 45.18792  ? 175  ARG   A CD  1 
ATOM   1159 N NE  . ARG   A 1 199 ? -44.10700 31.36300  -21.76700 1.000 52.40131  ? 175  ARG   A NE  1 
ATOM   1160 C CZ  . ARG   A 1 199 ? -44.71700 31.92600  -22.80100 1.000 51.99703  ? 175  ARG   A CZ  1 
ATOM   1161 N NH1 . ARG   A 1 199 ? -44.23400 31.82400  -24.02800 1.000 50.07864  ? 175  ARG   A NH1 1 
ATOM   1162 N NH2 . ARG   A 1 199 ? -45.83300 32.62000  -22.59700 1.000 51.96944  ? 175  ARG   A NH2 1 
ATOM   1163 N N   . ALA   A 1 200 ? -39.81200 27.09700  -21.88700 1.000 40.05189  ? 176  ALA   A N   1 
ATOM   1164 C CA  . ALA   A 1 200 ? -39.00500 26.12800  -22.60900 1.000 42.37392  ? 176  ALA   A CA  1 
ATOM   1165 C C   . ALA   A 1 200 ? -38.77300 26.59600  -24.04400 1.000 49.63680  ? 176  ALA   A C   1 
ATOM   1166 O O   . ALA   A 1 200 ? -39.39100 27.54700  -24.52900 1.000 54.31245  ? 176  ALA   A O   1 
ATOM   1167 C CB  . ALA   A 1 200 ? -39.67100 24.75300  -22.60100 1.000 38.55912  ? 176  ALA   A CB  1 
ATOM   1168 N N   . THR   A 1 201 ? -37.86100 25.91600  -24.73200 1.000 46.22798  ? 177  THR   A N   1 
ATOM   1169 C CA  . THR   A 1 201 ? -37.52800 26.27900  -26.09800 1.000 41.02911  ? 177  THR   A CA  1 
ATOM   1170 C C   . THR   A 1 201 ? -37.77000 25.16400  -27.10300 1.000 41.08888  ? 177  THR   A C   1 
ATOM   1171 O O   . THR   A 1 201 ? -37.48100 25.35600  -28.28900 1.000 48.39431  ? 177  THR   A O   1 
ATOM   1172 C CB  . THR   A 1 201 ? -36.06600 26.72800  -26.19300 1.000 43.21202  ? 177  THR   A CB  1 
ATOM   1173 O OG1 . THR   A 1 201 ? -35.21200 25.58600  -26.06000 1.000 46.27637  ? 177  THR   A OG1 1 
ATOM   1174 C CG2 . THR   A 1 201 ? -35.74900 27.74400  -25.10600 1.000 39.47914  ? 177  THR   A CG2 1 
ATOM   1175 N N   . HIS   A 1 202 ? -38.27500 24.01000  -26.67500 1.000 38.68219  ? 178  HIS   A N   1 
ATOM   1176 C CA  . HIS   A 1 202 ? -38.67200 22.99600  -27.63600 1.000 42.59652  ? 178  HIS   A CA  1 
ATOM   1177 C C   . HIS   A 1 202 ? -39.96500 23.41200  -28.33500 1.000 43.91882  ? 178  HIS   A C   1 
ATOM   1178 O O   . HIS   A 1 202 ? -40.67200 24.32600  -27.90300 1.000 45.14451  ? 178  HIS   A O   1 
ATOM   1179 C CB  . HIS   A 1 202 ? -38.82700 21.63400  -26.95800 1.000 40.27052  ? 178  HIS   A CB  1 
ATOM   1180 C CG  . HIS   A 1 202 ? -39.93900 21.57700  -25.96100 1.000 44.97378  ? 178  HIS   A CG  1 
ATOM   1181 N ND1 . HIS   A 1 202 ? -39.80000 22.03600  -24.66900 1.000 44.43298  ? 178  HIS   A ND1 1 
ATOM   1182 C CD2 . HIS   A 1 202 ? -41.20700 21.11700  -26.06400 1.000 50.37402  ? 178  HIS   A CD2 1 
ATOM   1183 C CE1 . HIS   A 1 202 ? -40.93700 21.86100  -24.02000 1.000 50.55768  ? 178  HIS   A CE1 1 
ATOM   1184 N NE2 . HIS   A 1 202 ? -41.80700 21.30700  -24.84400 1.000 48.98872  ? 178  HIS   A NE2 1 
ATOM   1185 N N   . GLN   A 1 203 ? -40.26500 22.72600  -29.43900 1.000 39.41216  ? 179  GLN   A N   1 
ATOM   1186 C CA  . GLN   A 1 203 ? -41.30300 23.21200  -30.34100 1.000 41.58589  ? 179  GLN   A CA  1 
ATOM   1187 C C   . GLN   A 1 203 ? -42.69000 23.09700  -29.71600 1.000 41.29883  ? 179  GLN   A C   1 
ATOM   1188 O O   . GLN   A 1 203 ? -43.54800 23.96200  -29.93800 1.000 35.01887  ? 179  GLN   A O   1 
ATOM   1189 C CB  . GLN   A 1 203 ? -41.23300 22.45900  -31.67200 1.000 44.27538  ? 179  GLN   A CB  1 
ATOM   1190 C CG  . GLN   A 1 203 ? -42.05100 23.09800  -32.78500 1.000 35.01483  ? 179  GLN   A CG  1 
ATOM   1191 C CD  . GLN   A 1 203 ? -41.53800 24.47000  -33.17700 1.000 38.90857  ? 179  GLN   A CD  1 
ATOM   1192 O OE1 . GLN   A 1 203 ? -40.33100 24.69000  -33.27400 1.000 46.32048  ? 179  GLN   A OE1 1 
ATOM   1193 N NE2 . GLN   A 1 203 ? -42.45500 25.40200  -33.40000 1.000 36.17641  ? 179  GLN   A NE2 1 
ATOM   1194 N N   . GLU   A 1 204 ? -42.93200 22.04600  -28.92600 1.000 47.60103  ? 180  GLU   A N   1 
ATOM   1195 C CA  . GLU   A 1 204 ? -44.24800 21.86400  -28.31500 1.000 48.58674  ? 180  GLU   A CA  1 
ATOM   1196 C C   . GLU   A 1 204 ? -44.57600 23.00400  -27.36900 1.000 39.80927  ? 180  GLU   A C   1 
ATOM   1197 O O   . GLU   A 1 204 ? -45.67000 23.57800  -27.42400 1.000 41.06781  ? 180  GLU   A O   1 
ATOM   1198 C CB  . GLU   A 1 204 ? -44.30700 20.54100  -27.56800 1.000 43.09650  ? 180  GLU   A CB  1 
ATOM   1199 C CG  . GLU   A 1 204 ? -43.95300 19.38100  -28.43300 1.000 68.95338  ? 180  GLU   A CG  1 
ATOM   1200 C CD  . GLU   A 1 204 ? -44.83600 18.19900  -28.18300 1.000 85.15054  ? 180  GLU   A CD  1 
ATOM   1201 O OE1 . GLU   A 1 204 ? -45.74600 18.30500  -27.33300 1.000 82.31650  ? 180  GLU   A OE1 1 
ATOM   1202 O OE2 . GLU   A 1 204 ? -44.60900 17.16500  -28.83600 1.000 83.67358  ? 180  GLU   A OE2 1 
ATOM   1203 N N   . ALA   A 1 205 ? -43.64600 23.32300  -26.47200 1.000 35.08718  ? 181  ALA   A N   1 
ATOM   1204 C CA  . ALA   A 1 205 ? -43.80700 24.49800  -25.62900 1.000 40.39262  ? 181  ALA   A CA  1 
ATOM   1205 C C   . ALA   A 1 205 ? -44.14800 25.71700  -26.47100 1.000 38.84788  ? 181  ALA   A C   1 
ATOM   1206 O O   . ALA   A 1 205 ? -45.14100 26.40500  -26.21600 1.000 37.12192  ? 181  ALA   A O   1 
ATOM   1207 C CB  . ALA   A 1 205 ? -42.53200 24.73600  -24.82300 1.000 44.68069  ? 181  ALA   A CB  1 
ATOM   1208 N N   . ILE   A 1 206 ? -43.35700 25.96200  -27.51900 1.000 42.33340  ? 182  ILE   A N   1 
ATOM   1209 C CA  . ILE   A 1 206 ? -43.53800 27.14800  -28.34900 1.000 37.31947  ? 182  ILE   A CA  1 
ATOM   1210 C C   . ILE   A 1 206 ? -44.93300 27.17600  -28.95600 1.000 34.70229  ? 182  ILE   A C   1 
ATOM   1211 O O   . ILE   A 1 206 ? -45.57400 28.23200  -29.02700 1.000 30.50230  ? 182  ILE   A O   1 
ATOM   1212 C CB  . ILE   A 1 206 ? -42.44800 27.20000  -29.43300 1.000 38.99847  ? 182  ILE   A CB  1 
ATOM   1213 C CG1 . ILE   A 1 206 ? -41.07700 27.41400  -28.79300 1.000 43.33615  ? 182  ILE   A CG1 1 
ATOM   1214 C CG2 . ILE   A 1 206 ? -42.73900 28.30400  -30.42900 1.000 47.51770  ? 182  ILE   A CG2 1 
ATOM   1215 C CD1 . ILE   A 1 206 ? -39.93600 27.34500  -29.77000 1.000 40.90118  ? 182  ILE   A CD1 1 
ATOM   1216 N N   . ASN   A 1 207 ? -45.43000 26.01800  -29.39200 1.000 36.31655  ? 183  ASN   A N   1 
ATOM   1217 C CA  . ASN   A 1 207 ? -46.74800 25.97000  -30.01600 1.000 39.03627  ? 183  ASN   A CA  1 
ATOM   1218 C C   . ASN   A 1 207 ? -47.85800 26.10100  -28.98400 1.000 40.62400  ? 183  ASN   A C   1 
ATOM   1219 O O   . ASN   A 1 207 ? -48.90000 26.70400  -29.26400 1.000 41.70582  ? 183  ASN   A O   1 
ATOM   1220 C CB  . ASN   A 1 207 ? -46.90900 24.67500  -30.81300 1.000 41.81118  ? 183  ASN   A CB  1 
ATOM   1221 C CG  . ASN   A 1 207 ? -45.95400 24.59800  -31.99000 1.000 40.88358  ? 183  ASN   A CG  1 
ATOM   1222 O OD1 . ASN   A 1 207 ? -45.31200 23.57200  -32.21600 1.000 39.62940  ? 183  ASN   A OD1 1 
ATOM   1223 N ND2 . ASN   A 1 207 ? -45.83800 25.69600  -32.73100 1.000 32.59164  ? 183  ASN   A ND2 1 
ATOM   1224 N N   . CYS   A 1 208 ? -47.65100 25.54500  -27.78800 1.000 43.17276  ? 184  CYS   A N   1 
ATOM   1225 C CA  . CYS   A 1 208 ? -48.63200 25.70400  -26.72100 1.000 37.61146  ? 184  CYS   A CA  1 
ATOM   1226 C C   . CYS   A 1 208 ? -48.65000 27.13300  -26.19000 1.000 36.00291  ? 184  CYS   A C   1 
ATOM   1227 O O   . CYS   A 1 208 ? -49.71900 27.66900  -25.87500 1.000 42.40161  ? 184  CYS   A O   1 
ATOM   1228 C CB  . CYS   A 1 208 ? -48.34600 24.72200  -25.59100 1.000 38.28394  ? 184  CYS   A CB  1 
ATOM   1229 S SG  . CYS   A 1 208 ? -49.54200 24.85200  -24.26000 1.000 60.74805  ? 184  CYS   A SG  1 
ATOM   1230 N N   . TYR   A 1 209 ? -47.47800 27.76300  -26.07300 1.000 30.64621  ? 185  TYR   A N   1 
ATOM   1231 C CA  . TYR   A 1 209 ? -47.42200 29.16500  -25.67500 1.000 33.34149  ? 185  TYR   A CA  1 
ATOM   1232 C C   . TYR   A 1 209 ? -48.20800 30.05400  -26.62400 1.000 42.57147  ? 185  TYR   A C   1 
ATOM   1233 O O   . TYR   A 1 209 ? -48.65400 31.13400  -26.22200 1.000 44.47592  ? 185  TYR   A O   1 
ATOM   1234 C CB  . TYR   A 1 209 ? -45.97400 29.66000  -25.63100 1.000 34.98353  ? 185  TYR   A CB  1 
ATOM   1235 C CG  . TYR   A 1 209 ? -45.06000 28.90900  -24.69200 1.000 37.59968  ? 185  TYR   A CG  1 
ATOM   1236 C CD1 . TYR   A 1 209 ? -45.53300 28.36900  -23.50300 1.000 43.93854  ? 185  TYR   A CD1 1 
ATOM   1237 C CD2 . TYR   A 1 209 ? -43.71700 28.73900  -25.00100 1.000 36.09901  ? 185  TYR   A CD2 1 
ATOM   1238 C CE1 . TYR   A 1 209 ? -44.69600 27.67500  -22.64800 1.000 40.32432  ? 185  TYR   A CE1 1 
ATOM   1239 C CE2 . TYR   A 1 209 ? -42.87500 28.04700  -24.15800 1.000 43.80064  ? 185  TYR   A CE2 1 
ATOM   1240 C CZ  . TYR   A 1 209 ? -43.36800 27.51500  -22.98200 1.000 45.01703  ? 185  TYR   A CZ  1 
ATOM   1241 O OH  . TYR   A 1 209 ? -42.52400 26.83300  -22.13600 1.000 47.63862  ? 185  TYR   A OH  1 
ATOM   1242 N N   . ALA   A 1 210 ? -48.37600 29.62600  -27.87700 1.000 47.72845  ? 186  ALA   A N   1 
ATOM   1243 C CA  . ALA   A 1 210 ? -49.02900 30.43100  -28.89800 1.000 44.13871  ? 186  ALA   A CA  1 
ATOM   1244 C C   . ALA   A 1 210 ? -50.52600 30.17900  -28.99600 1.000 45.10984  ? 186  ALA   A C   1 
ATOM   1245 O O   . ALA   A 1 210 ? -51.25600 31.05500  -29.47700 1.000 43.38496  ? 186  ALA   A O   1 
ATOM   1246 C CB  . ALA   A 1 210 ? -48.38000 30.17400  -30.26000 1.000 47.78879  ? 186  ALA   A CB  1 
ATOM   1247 N N   . GLU   A 1 211 ? -50.99900 29.01600  -28.55900 1.000 42.46089  ? 187  GLU   A N   1 
ATOM   1248 C CA  . GLU   A 1 211 ? -52.42900 28.74000  -28.55200 1.000 45.37400  ? 187  GLU   A CA  1 
ATOM   1249 C C   . GLU   A 1 211 ? -53.07300 29.36600  -27.31900 1.000 54.53717  ? 187  GLU   A C   1 
ATOM   1250 O O   . GLU   A 1 211 ? -52.67800 29.07400  -26.18300 1.000 54.11878  ? 187  GLU   A O   1 
ATOM   1251 C CB  . GLU   A 1 211 ? -52.68900 27.23400  -28.59500 1.000 41.16390  ? 187  GLU   A CB  1 
ATOM   1252 C CG  . GLU   A 1 211 ? -54.14000 26.87300  -28.85600 1.000 43.30548  ? 187  GLU   A CG  1 
ATOM   1253 C CD  . GLU   A 1 211 ? -54.56900 27.16000  -30.28200 1.000 54.85494  ? 187  GLU   A CD  1 
ATOM   1254 O OE1 . GLU   A 1 211 ? -53.79700 26.84900  -31.21300 1.000 60.21058  ? 187  GLU   A OE1 1 
ATOM   1255 O OE2 . GLU   A 1 211 ? -55.67800 27.70100  -30.47400 1.000 61.43493  ? 187  GLU   A OE2 1 
ATOM   1256 N N   . GLU   A 1 212 ? -54.05900 30.23900  -27.55000 1.000 52.16718  ? 188  GLU   A N   1 
ATOM   1257 C CA  . GLU   A 1 212 ? -54.91100 30.74300  -26.48000 1.000 47.52755  ? 188  GLU   A CA  1 
ATOM   1258 C C   . GLU   A 1 212 ? -55.66100 29.62800  -25.77500 1.000 52.19914  ? 188  GLU   A C   1 
ATOM   1259 O O   . GLU   A 1 212 ? -56.23600 29.85600  -24.70400 1.000 57.61167  ? 188  GLU   A O   1 
ATOM   1260 C CB  . GLU   A 1 212 ? -55.91100 31.75200  -27.05100 1.000 45.33197  ? 188  GLU   A CB  1 
ATOM   1261 C CG  . GLU   A 1 212 ? -55.36500 33.15900  -27.24800 1.000 56.93762  ? 188  GLU   A CG  1 
ATOM   1262 C CD  . GLU   A 1 212 ? -54.33800 33.55400  -26.20400 1.000 61.01305  ? 188  GLU   A CD  1 
ATOM   1263 O OE1 . GLU   A 1 212 ? -54.62900 33.39500  -25.00300 1.000 65.39807  ? 188  GLU   A OE1 1 
ATOM   1264 O OE2 . GLU   A 1 212 ? -53.23400 34.00700  -26.58000 1.000 65.37760  ? 188  GLU   A OE2 1 
ATOM   1265 N N   . THR   A 1 213 ? -55.66200 28.43100  -26.34600 1.000 47.70778  ? 189  THR   A N   1 
ATOM   1266 C CA  . THR   A 1 213 ? -56.49500 27.33700  -25.88900 1.000 47.44091  ? 189  THR   A CA  1 
ATOM   1267 C C   . THR   A 1 213 ? -55.65700 26.21600  -25.28900 1.000 42.08015  ? 189  THR   A C   1 
ATOM   1268 O O   . THR   A 1 213 ? -56.18200 25.13500  -24.99800 1.000 41.68466  ? 189  THR   A O   1 
ATOM   1269 C CB  . THR   A 1 213 ? -57.33000 26.84300  -27.07200 1.000 51.84652  ? 189  THR   A CB  1 
ATOM   1270 O OG1 . THR   A 1 213 ? -57.71900 27.96800  -27.86400 1.000 54.07241  ? 189  THR   A OG1 1 
ATOM   1271 C CG2 . THR   A 1 213 ? -58.58800 26.18800  -26.59200 1.000 54.06669  ? 189  THR   A CG2 1 
ATOM   1272 N N   . CYS   A 1 214 ? -54.35900 26.45400  -25.10600 1.000 44.95591  ? 190  CYS   A N   1 
ATOM   1273 C CA  . CYS   A 1 214 ? -53.43700 25.50200  -24.50500 1.000 47.84294  ? 190  CYS   A CA  1 
ATOM   1274 C C   . CYS   A 1 214 ? -52.77300 26.18300  -23.32400 1.000 48.16389  ? 190  CYS   A C   1 
ATOM   1275 O O   . CYS   A 1 214 ? -52.23300 27.28500  -23.46700 1.000 51.52102  ? 190  CYS   A O   1 
ATOM   1276 C CB  . CYS   A 1 214 ? -52.37200 25.04000  -25.50700 1.000 46.73475  ? 190  CYS   A CB  1 
ATOM   1277 S SG  . CYS   A 1 214 ? -51.17500 23.80800  -24.88300 1.000 55.82910  ? 190  CYS   A SG  1 
ATOM   1278 N N   . CYS   A 1 215 ? -52.82300 25.54200  -22.16300 1.000 47.05498  ? 191  CYS   A N   1 
ATOM   1279 C CA  . CYS   A 1 215 ? -52.20000 26.08800  -20.96300 1.000 52.72716  ? 191  CYS   A CA  1 
ATOM   1280 C C   . CYS   A 1 215 ? -51.48600 24.98500  -20.19700 1.000 52.75071  ? 191  CYS   A C   1 
ATOM   1281 O O   . CYS   A 1 215 ? -51.68700 24.79200  -18.99800 1.000 51.96004  ? 191  CYS   A O   1 
ATOM   1282 C CB  . CYS   A 1 215 ? -53.22200 26.79000  -20.07500 1.000 55.64595  ? 191  CYS   A CB  1 
ATOM   1283 S SG  . CYS   A 1 215 ? -52.46900 27.60800  -18.66400 1.000 37.81379  ? 191  CYS   A SG  1 
ATOM   1284 N N   . ASP   A 1 216 ? -50.65600 24.22700  -20.89600 1.000 48.44039  ? 192  ASP   A N   1 
ATOM   1285 C CA  . ASP   A 1 216 ? -49.75200 23.33300  -20.20000 1.000 55.45437  ? 192  ASP   A CA  1 
ATOM   1286 C C   . ASP   A 1 216 ? -48.56800 24.13400  -19.67200 1.000 55.73961  ? 192  ASP   A C   1 
ATOM   1287 O O   . ASP   A 1 216 ? -48.24700 25.21500  -20.17200 1.000 58.22491  ? 192  ASP   A O   1 
ATOM   1288 C CB  . ASP   A 1 216 ? -49.29300 22.20600  -21.12100 1.000 62.00368  ? 192  ASP   A CB  1 
ATOM   1289 C CG  . ASP   A 1 216 ? -50.43600 21.30600  -21.54000 1.000 75.30075  ? 192  ASP   A CG  1 
ATOM   1290 O OD1 . ASP   A 1 216 ? -51.57900 21.55200  -21.09200 1.000 72.44060  ? 192  ASP   A OD1 1 
ATOM   1291 O OD2 . ASP   A 1 216 ? -50.19300 20.35900  -22.31800 1.000 77.60944  ? 192  ASP   A OD2 1 
ATOM   1292 N N   . PHE   A 1 217 ? -47.93300 23.61100  -18.63000 1.000 50.61080  ? 193  PHE   A N   1 
ATOM   1293 C CA  . PHE   A 1 217 ? -46.85800 24.34300  -17.96300 1.000 48.53966  ? 193  PHE   A CA  1 
ATOM   1294 C C   . PHE   A 1 217 ? -45.49800 23.78900  -18.37800 1.000 61.38757  ? 193  PHE   A C   1 
ATOM   1295 O O   . PHE   A 1 217 ? -44.72000 23.27300  -17.57100 1.000 69.15795  ? 193  PHE   A O   1 
ATOM   1296 C CB  . PHE   A 1 217 ? -47.04700 24.30200  -16.45100 1.000 59.11709  ? 193  PHE   A CB  1 
ATOM   1297 C CG  . PHE   A 1 217 ? -46.18500 25.28100  -15.70800 1.000 56.87272  ? 193  PHE   A CG  1 
ATOM   1298 C CD1 . PHE   A 1 217 ? -46.16700 26.61800  -16.07200 1.000 56.18583  ? 193  PHE   A CD1 1 
ATOM   1299 C CD2 . PHE   A 1 217 ? -45.42000 24.87600  -14.62900 1.000 54.94043  ? 193  PHE   A CD2 1 
ATOM   1300 C CE1 . PHE   A 1 217 ? -45.38700 27.52900  -15.38900 1.000 50.74323  ? 193  PHE   A CE1 1 
ATOM   1301 C CE2 . PHE   A 1 217 ? -44.63700 25.78500  -13.94000 1.000 60.02931  ? 193  PHE   A CE2 1 
ATOM   1302 C CZ  . PHE   A 1 217 ? -44.62100 27.11300  -14.32400 1.000 55.61315  ? 193  PHE   A CZ  1 
ATOM   1303 N N   . PHE   A 1 218 ? -45.22900 23.90600  -19.67700 1.000 56.57722  ? 194  PHE   A N   1 
ATOM   1304 C CA  . PHE   A 1 218 ? -43.92700 23.54800  -20.21300 1.000 47.55814  ? 194  PHE   A CA  1 
ATOM   1305 C C   . PHE   A 1 218 ? -42.86200 24.45800  -19.62000 1.000 44.39519  ? 194  PHE   A C   1 
ATOM   1306 O O   . PHE   A 1 218 ? -43.01000 25.68400  -19.61700 1.000 39.87729  ? 194  PHE   A O   1 
ATOM   1307 C CB  . PHE   A 1 218 ? -43.94500 23.66400  -21.73800 1.000 48.75163  ? 194  PHE   A CB  1 
ATOM   1308 C CG  . PHE   A 1 218 ? -44.57200 22.48800  -22.42400 1.000 45.57128  ? 194  PHE   A CG  1 
ATOM   1309 C CD1 . PHE   A 1 218 ? -43.98200 21.23700  -22.36300 1.000 45.87974  ? 194  PHE   A CD1 1 
ATOM   1310 C CD2 . PHE   A 1 218 ? -45.75800 22.63100  -23.11900 1.000 44.43701  ? 194  PHE   A CD2 1 
ATOM   1311 C CE1 . PHE   A 1 218 ? -44.55700 20.15500  -22.98500 1.000 37.96472  ? 194  PHE   A CE1 1 
ATOM   1312 C CE2 . PHE   A 1 218 ? -46.34100 21.55000  -23.74500 1.000 43.85087  ? 194  PHE   A CE2 1 
ATOM   1313 C CZ  . PHE   A 1 218 ? -45.73700 20.30800  -23.67700 1.000 41.88763  ? 194  PHE   A CZ  1 
ATOM   1314 N N   . THR   A 1 219 ? -41.79000 23.85700  -19.10600 1.000 48.98653  ? 195  THR   A N   1 
ATOM   1315 C CA  . THR   A 1 219 ? -40.75300 24.58500  -18.38800 1.000 48.51272  ? 195  THR   A CA  1 
ATOM   1316 C C   . THR   A 1 219 ? -39.38000 24.15700  -18.88000 1.000 46.67569  ? 195  THR   A C   1 
ATOM   1317 O O   . THR   A 1 219 ? -39.19300 23.02500  -19.33300 1.000 52.89871  ? 195  THR   A O   1 
ATOM   1318 C CB  . THR   A 1 219 ? -40.82600 24.34200  -16.87400 1.000 45.68209  ? 195  THR   A CB  1 
ATOM   1319 O OG1 . THR   A 1 219 ? -40.74100 22.93500  -16.61400 1.000 51.21603  ? 195  THR   A OG1 1 
ATOM   1320 C CG2 . THR   A 1 219 ? -42.12500 24.88000  -16.30200 1.000 46.27422  ? 195  THR   A CG2 1 
ATOM   1321 N N   . ASN   A 1 220 ? -38.41500 25.06600  -18.77800 1.000 42.00513  ? 196  ASN   A N   1 
ATOM   1322 C CA  . ASN   A 1 220 ? -37.04800 24.71700  -19.12200 1.000 37.78434  ? 196  ASN   A CA  1 
ATOM   1323 C C   . ASN   A 1 220 ? -36.41500 23.95100  -17.96500 1.000 36.94411  ? 196  ASN   A C   1 
ATOM   1324 O O   . ASN   A 1 220 ? -36.76200 24.15100  -16.79800 1.000 49.57854  ? 196  ASN   A O   1 
ATOM   1325 C CB  . ASN   A 1 220 ? -36.24900 25.97000  -19.51700 1.000 37.28940  ? 196  ASN   A CB  1 
ATOM   1326 C CG  . ASN   A 1 220 ? -36.01400 26.94300  -18.37100 1.000 32.91497  ? 196  ASN   A CG  1 
ATOM   1327 O OD1 . ASN   A 1 220 ? -35.68000 26.55800  -17.25700 1.000 39.84691  ? 196  ASN   A OD1 1 
ATOM   1328 N ND2 . ASN   A 1 220 ? -36.21100 28.22500  -18.65000 1.000 29.92102  ? 196  ASN   A ND2 1 
ATOM   1329 N N   . GLN   A 1 221 ? -35.51400 23.02500  -18.30600 1.000 39.17222  ? 197  GLN   A N   1 
ATOM   1330 C CA  . GLN   A 1 221 ? -35.00300 22.08400  -17.31300 1.000 41.32528  ? 197  GLN   A CA  1 
ATOM   1331 C C   . GLN   A 1 221 ? -34.32900 22.79400  -16.14400 1.000 46.20026  ? 197  GLN   A C   1 
ATOM   1332 O O   . GLN   A 1 221 ? -34.30600 22.26300  -15.02600 1.000 49.54400  ? 197  GLN   A O   1 
ATOM   1333 C CB  . GLN   A 1 221 ? -34.03600 21.10000  -17.97300 1.000 46.76424  ? 197  GLN   A CB  1 
ATOM   1334 C CG  . GLN   A 1 221 ? -34.42100 20.71900  -19.40000 1.000 63.58312  ? 197  GLN   A CG  1 
ATOM   1335 C CD  . GLN   A 1 221 ? -33.66800 21.52400  -20.45100 1.000 63.07830  ? 197  GLN   A CD  1 
ATOM   1336 O OE1 . GLN   A 1 221 ? -32.44900 21.68800  -20.37100 1.000 52.46013  ? 197  GLN   A OE1 1 
ATOM   1337 N NE2 . GLN   A 1 221 ? -34.39700 22.04000  -21.43700 1.000 52.15916  ? 197  GLN   A NE2 1 
ATOM   1338 N N   . ALA   A 1 222 ? -33.78800 23.99200  -16.37100 1.000 42.84842  ? 198  ALA   A N   1 
ATOM   1339 C CA  . ALA   A 1 222 ? -33.16300 24.72700  -15.27700 1.000 43.35760  ? 198  ALA   A CA  1 
ATOM   1340 C C   . ALA   A 1 222 ? -34.20400 25.26000  -14.30000 1.000 44.68611  ? 198  ALA   A C   1 
ATOM   1341 O O   . ALA   A 1 222 ? -34.01100 25.18100  -13.08000 1.000 42.09809  ? 198  ALA   A O   1 
ATOM   1342 C CB  . ALA   A 1 222 ? -32.30500 25.86900  -15.82300 1.000 39.95922  ? 198  ALA   A CB  1 
ATOM   1343 N N   . TYR   A 1 223 ? -35.31100 25.80700  -14.81200 1.000 42.86385  ? 199  TYR   A N   1 
ATOM   1344 C CA  . TYR   A 1 223 ? -36.33000 26.35200  -13.92300 1.000 42.68669  ? 199  TYR   A CA  1 
ATOM   1345 C C   . TYR   A 1 223 ? -36.98800 25.24800  -13.10400 1.000 44.63955  ? 199  TYR   A C   1 
ATOM   1346 O O   . TYR   A 1 223 ? -37.27000 25.43400  -11.91500 1.000 40.96262  ? 199  TYR   A O   1 
ATOM   1347 C CB  . TYR   A 1 223 ? -37.38300 27.12000  -14.72100 1.000 35.20975  ? 199  TYR   A CB  1 
ATOM   1348 C CG  . TYR   A 1 223 ? -38.60500 27.47100  -13.90900 1.000 39.59475  ? 199  TYR   A CG  1 
ATOM   1349 C CD1 . TYR   A 1 223 ? -38.62800 28.61200  -13.12300 1.000 39.78286  ? 199  TYR   A CD1 1 
ATOM   1350 C CD2 . TYR   A 1 223 ? -39.72800 26.65000  -13.90600 1.000 44.87333  ? 199  TYR   A CD2 1 
ATOM   1351 C CE1 . TYR   A 1 223 ? -39.73500 28.93500  -12.36600 1.000 49.97708  ? 199  TYR   A CE1 1 
ATOM   1352 C CE2 . TYR   A 1 223 ? -40.84000 26.96100  -13.14800 1.000 44.72809  ? 199  TYR   A CE2 1 
ATOM   1353 C CZ  . TYR   A 1 223 ? -40.83900 28.10500  -12.38000 1.000 52.71403  ? 199  TYR   A CZ  1 
ATOM   1354 O OH  . TYR   A 1 223 ? -41.94100 28.42200  -11.61900 1.000 52.26059  ? 199  TYR   A OH  1 
ATOM   1355 N N   . ALA   A 1 224 ? -37.23300 24.09000  -13.72200 1.000 37.32774  ? 200  ALA   A N   1 
ATOM   1356 C CA  . ALA   A 1 224 ? -37.92800 23.01400  -13.02500 1.000 43.26572  ? 200  ALA   A CA  1 
ATOM   1357 C C   . ALA   A 1 224 ? -37.14600 22.54500  -11.80300 1.000 43.25667  ? 200  ALA   A C   1 
ATOM   1358 O O   . ALA   A 1 224 ? -37.73600 22.16400  -10.78600 1.000 40.23136  ? 200  ALA   A O   1 
ATOM   1359 C CB  . ALA   A 1 224 ? -38.18200 21.85000  -13.98000 1.000 43.76400  ? 200  ALA   A CB  1 
ATOM   1360 N N   . ILE   A 1 225 ? -35.82100 22.55600  -11.88200 1.000 45.48634  ? 201  ILE   A N   1 
ATOM   1361 C CA  . ILE   A 1 225 ? -34.99800 22.11400  -10.76200 1.000 37.15128  ? 201  ILE   A CA  1 
ATOM   1362 C C   . ILE   A 1 225 ? -34.70300 23.25900  -9.80300  1.000 34.24452  ? 201  ILE   A C   1 
ATOM   1363 O O   . ILE   A 1 225 ? -34.77600 23.09000  -8.58500  1.000 42.17167  ? 201  ILE   A O   1 
ATOM   1364 C CB  . ILE   A 1 225 ? -33.69900 21.47100  -11.28900 1.000 42.78823  ? 201  ILE   A CB  1 
ATOM   1365 C CG1 . ILE   A 1 225 ? -34.01900 20.27800  -12.19000 1.000 42.66458  ? 201  ILE   A CG1 1 
ATOM   1366 C CG2 . ILE   A 1 225 ? -32.81000 21.04800  -10.13400 1.000 33.27349  ? 201  ILE   A CG2 1 
ATOM   1367 C CD1 . ILE   A 1 225 ? -32.82600 19.76700  -12.96000 1.000 37.37183  ? 201  ILE   A CD1 1 
ATOM   1368 N N   . ALA   A 1 226 ? -34.36900 24.43800  -10.32900 1.000 32.73440  ? 202  ALA   A N   1 
ATOM   1369 C CA  . ALA   A 1 226 ? -34.06300 25.57000  -9.46400  1.000 31.75374  ? 202  ALA   A CA  1 
ATOM   1370 C C   . ALA   A 1 226 ? -35.28600 26.07800  -8.71800  1.000 42.41554  ? 202  ALA   A C   1 
ATOM   1371 O O   . ALA   A 1 226 ? -35.13000 26.75300  -7.69600  1.000 48.05162  ? 202  ALA   A O   1 
ATOM   1372 C CB  . ALA   A 1 226 ? -33.44000 26.71000  -10.27200 1.000 40.44024  ? 202  ALA   A CB  1 
ATOM   1373 N N   . SER   A 1 227 ? -36.49600 25.77900  -9.20000  1.000 49.68561  ? 203  SER   A N   1 
ATOM   1374 C CA  . SER   A 1 227 ? -37.69700 26.15200  -8.45900  1.000 43.52679  ? 203  SER   A CA  1 
ATOM   1375 C C   . SER   A 1 227 ? -38.03000 25.11800  -7.39100  1.000 34.58124  ? 203  SER   A C   1 
ATOM   1376 O O   . SER   A 1 227 ? -38.18100 25.46700  -6.21800  1.000 40.63257  ? 203  SER   A O   1 
ATOM   1377 C CB  . SER   A 1 227 ? -38.87600 26.33900  -9.41400  1.000 42.14018  ? 203  SER   A CB  1 
ATOM   1378 O OG  . SER   A 1 227 ? -39.12800 25.15500  -10.14600 1.000 50.82133  ? 203  SER   A OG  1 
ATOM   1379 N N   . SER   A 1 228 ? -38.12700 23.84100  -7.78000  1.000 31.12547  ? 204  SER   A N   1 
ATOM   1380 C CA  . SER   A 1 228 ? -38.41100 22.77200  -6.82400  1.000 34.00347  ? 204  SER   A CA  1 
ATOM   1381 C C   . SER   A 1 228 ? -37.45300 22.80000  -5.64300  1.000 41.19014  ? 204  SER   A C   1 
ATOM   1382 O O   . SER   A 1 228 ? -37.84300 22.50300  -4.50700  1.000 40.75167  ? 204  SER   A O   1 
ATOM   1383 C CB  . SER   A 1 228 ? -38.33800 21.40600  -7.51500  1.000 36.43308  ? 204  SER   A CB  1 
ATOM   1384 O OG  . SER   A 1 228 ? -39.36500 21.24500  -8.47400  1.000 46.43272  ? 204  SER   A OG  1 
ATOM   1385 N N   . ILE   A 1 229 ? -36.19100 23.15400  -5.88700  1.000 42.89117  ? 205  ILE   A N   1 
ATOM   1386 C CA  . ILE   A 1 229 ? -35.20800 23.17400  -4.80800  1.000 40.16355  ? 205  ILE   A CA  1 
ATOM   1387 C C   . ILE   A 1 229 ? -35.45200 24.36900  -3.89500  1.000 35.83598  ? 205  ILE   A C   1 
ATOM   1388 O O   . ILE   A 1 229 ? -35.69300 24.21000  -2.69400  1.000 42.43557  ? 205  ILE   A O   1 
ATOM   1389 C CB  . ILE   A 1 229 ? -33.77600 23.16700  -5.37500  1.000 34.48304  ? 205  ILE   A CB  1 
ATOM   1390 C CG1 . ILE   A 1 229 ? -33.30900 21.73100  -5.60600  1.000 24.29956  ? 205  ILE   A CG1 1 
ATOM   1391 C CG2 . ILE   A 1 229 ? -32.81000 23.84800  -4.42300  1.000 31.55439  ? 205  ILE   A CG2 1 
ATOM   1392 C CD1 . ILE   A 1 229 ? -32.03200 21.63000  -6.37700  1.000 22.11220  ? 205  ILE   A CD1 1 
ATOM   1393 N N   . VAL   A 1 230 ? -35.42900 25.58100  -4.45800  1.000 29.93353  ? 206  VAL   A N   1 
ATOM   1394 C CA  . VAL   A 1 230 ? -35.49200 26.78200  -3.63000  1.000 34.30343  ? 206  VAL   A CA  1 
ATOM   1395 C C   . VAL   A 1 230 ? -36.87500 26.95700  -3.01300  1.000 42.42713  ? 206  VAL   A C   1 
ATOM   1396 O O   . VAL   A 1 230 ? -37.00400 27.44700  -1.88400  1.000 43.23544  ? 206  VAL   A O   1 
ATOM   1397 C CB  . VAL   A 1 230 ? -35.08400 28.01400  -4.45600  1.000 31.91098  ? 206  VAL   A CB  1 
ATOM   1398 C CG1 . VAL   A 1 230 ? -35.23800 29.29100  -3.63800  1.000 24.84577  ? 206  VAL   A CG1 1 
ATOM   1399 C CG2 . VAL   A 1 230 ? -33.66000 27.85700  -4.94300  1.000 33.95405  ? 206  VAL   A CG2 1 
ATOM   1400 N N   . SER   A 1 231 ? -37.92300 26.55100  -3.71800  1.000 41.56121  ? 207  SER   A N   1 
ATOM   1401 C CA  . SER   A 1 231 ? -39.27800 26.78200  -3.25100  1.000 35.21690  ? 207  SER   A CA  1 
ATOM   1402 C C   . SER   A 1 231 ? -39.83500 25.63800  -2.41700  1.000 40.64516  ? 207  SER   A C   1 
ATOM   1403 O O   . SER   A 1 231 ? -40.75500 25.86400  -1.62100  1.000 39.40239  ? 207  SER   A O   1 
ATOM   1404 C CB  . SER   A 1 231 ? -40.20000 27.03300  -4.44100  1.000 42.87376  ? 207  SER   A CB  1 
ATOM   1405 O OG  . SER   A 1 231 ? -39.99600 28.32800  -4.97900  1.000 51.94796  ? 207  SER   A OG  1 
ATOM   1406 N N   . PHE   A 1 232 ? -39.30800 24.42100  -2.57000  1.000 38.63222  ? 208  PHE   A N   1 
ATOM   1407 C CA  . PHE   A 1 232 ? -39.86900 23.25700  -1.88500  1.000 39.55985  ? 208  PHE   A CA  1 
ATOM   1408 C C   . PHE   A 1 232 ? -38.82800 22.52900  -1.04400  1.000 36.92283  ? 208  PHE   A C   1 
ATOM   1409 O O   . PHE   A 1 232 ? -38.96300 22.49200  0.17900   1.000 41.48625  ? 208  PHE   A O   1 
ATOM   1410 C CB  . PHE   A 1 232 ? -40.52000 22.31400  -2.89700  1.000 34.21306  ? 208  PHE   A CB  1 
ATOM   1411 C CG  . PHE   A 1 232 ? -41.11400 21.08400  -2.27800  1.000 36.25963  ? 208  PHE   A CG  1 
ATOM   1412 C CD1 . PHE   A 1 232 ? -42.21200 21.17100  -1.44000  1.000 31.98077  ? 208  PHE   A CD1 1 
ATOM   1413 C CD2 . PHE   A 1 232 ? -40.56100 19.83800  -2.52600  1.000 38.96364  ? 208  PHE   A CD2 1 
ATOM   1414 C CE1 . PHE   A 1 232 ? -42.75500 20.03300  -0.86700  1.000 29.23684  ? 208  PHE   A CE1 1 
ATOM   1415 C CE2 . PHE   A 1 232 ? -41.09700 18.69800  -1.95700  1.000 42.25554  ? 208  PHE   A CE2 1 
ATOM   1416 C CZ  . PHE   A 1 232 ? -42.19700 18.79500  -1.12500  1.000 35.94464  ? 208  PHE   A CZ  1 
ATOM   1417 N N   . TYR   A 1 233 ? -37.79800 21.93600  -1.65300  1.000 41.26227  ? 209  TYR   A N   1 
ATOM   1418 C CA  . TYR   A 1 233 ? -36.93200 21.02600  -0.90600  1.000 41.92730  ? 209  TYR   A CA  1 
ATOM   1419 C C   . TYR   A 1 233 ? -36.19000 21.74100  0.21800   1.000 41.92501  ? 209  TYR   A C   1 
ATOM   1420 O O   . TYR   A 1 233 ? -36.07700 21.20800  1.32800   1.000 41.13957  ? 209  TYR   A O   1 
ATOM   1421 C CB  . TYR   A 1 233 ? -35.93500 20.33800  -1.83900  1.000 40.35753  ? 209  TYR   A CB  1 
ATOM   1422 C CG  . TYR   A 1 233 ? -36.53000 19.27200  -2.73000  1.000 38.02989  ? 209  TYR   A CG  1 
ATOM   1423 C CD1 . TYR   A 1 233 ? -37.21100 19.60200  -3.89300  1.000 36.10854  ? 209  TYR   A CD1 1 
ATOM   1424 C CD2 . TYR   A 1 233 ? -36.44200 17.93100  -2.38000  1.000 38.62860  ? 209  TYR   A CD2 1 
ATOM   1425 C CE1 . TYR   A 1 233 ? -37.75700 18.62000  -4.70200  1.000 44.11534  ? 209  TYR   A CE1 1 
ATOM   1426 C CE2 . TYR   A 1 233 ? -36.99100 16.94400  -3.17700  1.000 40.36871  ? 209  TYR   A CE2 1 
ATOM   1427 C CZ  . TYR   A 1 233 ? -37.64600 17.29300  -4.33500  1.000 46.15950  ? 209  TYR   A CZ  1 
ATOM   1428 O OH  . TYR   A 1 233 ? -38.19100 16.30900  -5.12700  1.000 51.79412  ? 209  TYR   A OH  1 
ATOM   1429 N N   . VAL   A 1 234 ? -35.67900 22.93900  -0.04400  1.000 39.00173  ? 210  VAL   A N   1 
ATOM   1430 C CA  . VAL   A 1 234 ? -34.89700 23.66800  0.94900   1.000 38.31548  ? 210  VAL   A CA  1 
ATOM   1431 C C   . VAL   A 1 234 ? -35.75900 23.93200  2.18200   1.000 46.01002  ? 210  VAL   A C   1 
ATOM   1432 O O   . VAL   A 1 234 ? -35.34400 23.56200  3.29100   1.000 47.52095  ? 210  VAL   A O   1 
ATOM   1433 C CB  . VAL   A 1 234 ? -34.30300 24.96300  0.36700   1.000 39.12366  ? 210  VAL   A CB  1 
ATOM   1434 C CG1 . VAL   A 1 234 ? -34.07300 25.99600  1.46700   1.000 41.54515  ? 210  VAL   A CG1 1 
ATOM   1435 C CG2 . VAL   A 1 234 ? -33.00600 24.66600  -0.36900  1.000 36.99437  ? 210  VAL   A CG2 1 
ATOM   1436 N N   . PRO   A 1 235 ? -36.95500 24.53200  2.07100   1.000 44.31068  ? 211  PRO   A N   1 
ATOM   1437 C CA  . PRO   A 1 235 ? -37.77500 24.66700  3.28500   1.000 43.88568  ? 211  PRO   A CA  1 
ATOM   1438 C C   . PRO   A 1 235 ? -38.27100 23.33300  3.80800   1.000 43.75454  ? 211  PRO   A C   1 
ATOM   1439 O O   . PRO   A 1 235 ? -38.54200 23.22000  5.00800   1.000 48.31066  ? 211  PRO   A O   1 
ATOM   1440 C CB  . PRO   A 1 235 ? -38.93400 25.57400  2.84600   1.000 40.28689  ? 211  PRO   A CB  1 
ATOM   1441 C CG  . PRO   A 1 235 ? -38.97300 25.45800  1.38100   1.000 47.04767  ? 211  PRO   A CG  1 
ATOM   1442 C CD  . PRO   A 1 235 ? -37.57000 25.23600  0.93000   1.000 41.49129  ? 211  PRO   A CD  1 
ATOM   1443 N N   . LEU   A 1 236 ? -38.38200 22.31600  2.94700   1.000 41.69044  ? 212  LEU   A N   1 
ATOM   1444 C CA  . LEU   A 1 236 ? -38.84500 21.00800  3.40200   1.000 41.34379  ? 212  LEU   A CA  1 
ATOM   1445 C C   . LEU   A 1 236 ? -37.86400 20.39600  4.39300   1.000 43.61726  ? 212  LEU   A C   1 
ATOM   1446 O O   . LEU   A 1 236 ? -38.25200 19.98000  5.49000   1.000 44.83751  ? 212  LEU   A O   1 
ATOM   1447 C CB  . LEU   A 1 236 ? -39.06200 20.07700  2.20600   1.000 34.86381  ? 212  LEU   A CB  1 
ATOM   1448 C CG  . LEU   A 1 236 ? -39.83100 18.75900  2.39500   1.000 40.81505  ? 212  LEU   A CG  1 
ATOM   1449 C CD1 . LEU   A 1 236 ? -39.01300 17.66800  3.07300   1.000 43.34006  ? 212  LEU   A CD1 1 
ATOM   1450 C CD2 . LEU   A 1 236 ? -41.11200 19.00800  3.17300   1.000 42.15927  ? 212  LEU   A CD2 1 
ATOM   1451 N N   . VAL   A 1 237 ? -36.58400 20.33400  4.02900   1.000 44.97716  ? 213  VAL   A N   1 
ATOM   1452 C CA  . VAL   A 1 237 ? -35.64300 19.60300  4.87000   1.000 46.64220  ? 213  VAL   A CA  1 
ATOM   1453 C C   . VAL   A 1 237 ? -35.16300 20.44800  6.03900   1.000 40.42847  ? 213  VAL   A C   1 
ATOM   1454 O O   . VAL   A 1 237 ? -34.75700 19.90100  7.06600   1.000 46.03596  ? 213  VAL   A O   1 
ATOM   1455 C CB  . VAL   A 1 237 ? -34.46400 19.07600  4.03800   1.000 52.24775  ? 213  VAL   A CB  1 
ATOM   1456 C CG1 . VAL   A 1 237 ? -34.94800 18.00200  3.07200   1.000 43.27801  ? 213  VAL   A CG1 1 
ATOM   1457 C CG2 . VAL   A 1 237 ? -33.78300 20.21500  3.30300   1.000 47.97407  ? 213  VAL   A CG2 1 
ATOM   1458 N N   . ILE   A 1 238 ? -35.18300 21.77700  5.91800   1.000 37.51732  ? 214  ILE   A N   1 
ATOM   1459 C CA  . ILE   A 1 238 ? -35.00100 22.60700  7.10500   1.000 37.64232  ? 214  ILE   A CA  1 
ATOM   1460 C C   . ILE   A 1 238 ? -36.11000 22.31900  8.10400   1.000 43.16789  ? 214  ILE   A C   1 
ATOM   1461 O O   . ILE   A 1 238 ? -35.86900 22.18800  9.31000   1.000 45.49070  ? 214  ILE   A O   1 
ATOM   1462 C CB  . ILE   A 1 238 ? -34.95800 24.09800  6.72900   1.000 36.80342  ? 214  ILE   A CB  1 
ATOM   1463 C CG1 . ILE   A 1 238 ? -33.68800 24.42200  5.94500   1.000 39.04121  ? 214  ILE   A CG1 1 
ATOM   1464 C CG2 . ILE   A 1 238 ? -35.05500 24.96500  7.97400   1.000 26.67788  ? 214  ILE   A CG2 1 
ATOM   1465 C CD1 . ILE   A 1 238 ? -33.34900 25.89800  5.92600   1.000 40.09035  ? 214  ILE   A CD1 1 
ATOM   1466 N N   . MET   A 1 239 ? -37.34000 22.18400  7.60900   1.000 43.59904  ? 215  MET   A N   1 
ATOM   1467 C CA  . MET   A 1 239 ? -38.47700 21.87400  8.46600   1.000 41.70778  ? 215  MET   A CA  1 
ATOM   1468 C C   . MET   A 1 239 ? -38.33500 20.49000  9.09400   1.000 43.08938  ? 215  MET   A C   1 
ATOM   1469 O O   . MET   A 1 239 ? -38.40400 20.34000  10.31900  1.000 44.98508  ? 215  MET   A O   1 
ATOM   1470 C CB  . MET   A 1 239 ? -39.76700 21.97700  7.64900   1.000 44.42995  ? 215  MET   A CB  1 
ATOM   1471 C CG  . MET   A 1 239 ? -41.04900 21.87500  8.44600   1.000 43.45500  ? 215  MET   A CG  1 
ATOM   1472 S SD  . MET   A 1 239 ? -42.42700 21.50800  7.35100   1.000 34.78566  ? 215  MET   A SD  1 
ATOM   1473 C CE  . MET   A 1 239 ? -42.15300 19.75600  7.09400   1.000 36.14870  ? 215  MET   A CE  1 
ATOM   1474 N N   . VAL   A 1 240 ? -38.13700 19.46100  8.26200   1.000 38.51822  ? 216  VAL   A N   1 
ATOM   1475 C CA  . VAL   A 1 240 ? -38.04400 18.09300  8.77200   1.000 35.53689  ? 216  VAL   A CA  1 
ATOM   1476 C C   . VAL   A 1 240 ? -36.87100 17.94500  9.73200   1.000 43.62147  ? 216  VAL   A C   1 
ATOM   1477 O O   . VAL   A 1 240 ? -36.91100 17.12000  10.65400  1.000 48.47064  ? 216  VAL   A O   1 
ATOM   1478 C CB  . VAL   A 1 240 ? -37.95600 17.09700  7.59900   1.000 36.22807  ? 216  VAL   A CB  1 
ATOM   1479 C CG1 . VAL   A 1 240 ? -37.74600 15.68100  8.10300   1.000 25.22768  ? 216  VAL   A CG1 1 
ATOM   1480 C CG2 . VAL   A 1 240 ? -39.21800 17.16900  6.76400   1.000 47.83953  ? 216  VAL   A CG2 1 
ATOM   1481 N N   . PHE   A 1 241 ? -35.82500 18.75000  9.55900   1.000 45.66622  ? 217  PHE   A N   1 
ATOM   1482 C CA  . PHE   A 1 241 ? -34.69600 18.67700  10.47800  1.000 46.69938  ? 217  PHE   A CA  1 
ATOM   1483 C C   . PHE   A 1 241 ? -34.98200 19.44200  11.76600  1.000 47.63368  ? 217  PHE   A C   1 
ATOM   1484 O O   . PHE   A 1 241 ? -34.88200 18.88100  12.86300  1.000 47.67618  ? 217  PHE   A O   1 
ATOM   1485 C CB  . PHE   A 1 241 ? -33.43200 19.21400  9.80100   1.000 46.06430  ? 217  PHE   A CB  1 
ATOM   1486 C CG  . PHE   A 1 241 ? -32.31600 19.51100  10.75500  1.000 56.52748  ? 217  PHE   A CG  1 
ATOM   1487 C CD1 . PHE   A 1 241 ? -31.60500 18.47800  11.34400  1.000 57.29874  ? 217  PHE   A CD1 1 
ATOM   1488 C CD2 . PHE   A 1 241 ? -31.98000 20.81900  11.07000  1.000 54.72293  ? 217  PHE   A CD2 1 
ATOM   1489 C CE1 . PHE   A 1 241 ? -30.57700 18.74100  12.22600  1.000 58.51484  ? 217  PHE   A CE1 1 
ATOM   1490 C CE2 . PHE   A 1 241 ? -30.95200 21.08900  11.95300  1.000 54.99761  ? 217  PHE   A CE2 1 
ATOM   1491 C CZ  . PHE   A 1 241 ? -30.24900 20.04800  12.53100  1.000 62.64584  ? 217  PHE   A CZ  1 
ATOM   1492 N N   . VAL   A 1 242 ? -35.35100 20.72000  11.64800  1.000 45.24607  ? 218  VAL   A N   1 
ATOM   1493 C CA  . VAL   A 1 242 ? -35.48900 21.57600  12.82400  1.000 44.58892  ? 218  VAL   A CA  1 
ATOM   1494 C C   . VAL   A 1 242 ? -36.61400 21.08300  13.72700  1.000 45.06974  ? 218  VAL   A C   1 
ATOM   1495 O O   . VAL   A 1 242 ? -36.49700 21.10400  14.95900  1.000 39.60968  ? 218  VAL   A O   1 
ATOM   1496 C CB  . VAL   A 1 242 ? -35.70300 23.03900  12.39000  1.000 38.26676  ? 218  VAL   A CB  1 
ATOM   1497 C CG1 . VAL   A 1 242 ? -36.29100 23.86400  13.52500  1.000 36.76882  ? 218  VAL   A CG1 1 
ATOM   1498 C CG2 . VAL   A 1 242 ? -34.39400 23.64100  11.90900  1.000 36.16720  ? 218  VAL   A CG2 1 
ATOM   1499 N N   . TYR   A 1 243 ? -37.71500 20.61500  13.13900  1.000 47.10362  ? 219  TYR   A N   1 
ATOM   1500 C CA  . TYR   A 1 243 ? -38.84700 20.22400  13.97000  1.000 48.51364  ? 219  TYR   A CA  1 
ATOM   1501 C C   . TYR   A 1 243 ? -38.62800 18.88300  14.65700  1.000 48.63849  ? 219  TYR   A C   1 
ATOM   1502 O O   . TYR   A 1 243 ? -39.13000 18.67800  15.76700  1.000 55.12152  ? 219  TYR   A O   1 
ATOM   1503 C CB  . TYR   A 1 243 ? -40.13600 20.18000  13.15100  1.000 50.24546  ? 219  TYR   A CB  1 
ATOM   1504 C CG  . TYR   A 1 243 ? -41.36800 20.30100  14.02000  1.000 39.95639  ? 219  TYR   A CG  1 
ATOM   1505 C CD1 . TYR   A 1 243 ? -41.63000 21.47200  14.71600  1.000 39.99145  ? 219  TYR   A CD1 1 
ATOM   1506 C CD2 . TYR   A 1 243 ? -42.25400 19.24400  14.16100  1.000 38.70715  ? 219  TYR   A CD2 1 
ATOM   1507 C CE1 . TYR   A 1 243 ? -42.74300 21.59400  15.51900  1.000 42.20677  ? 219  TYR   A CE1 1 
ATOM   1508 C CE2 . TYR   A 1 243 ? -43.37500 19.35800  14.96300  1.000 44.99419  ? 219  TYR   A CE2 1 
ATOM   1509 C CZ  . TYR   A 1 243 ? -43.61100 20.53500  15.64200  1.000 41.77148  ? 219  TYR   A CZ  1 
ATOM   1510 O OH  . TYR   A 1 243 ? -44.71900 20.66300  16.44400  1.000 34.85608  ? 219  TYR   A OH  1 
ATOM   1511 N N   . SER   A 1 244 ? -37.89600 17.96100  14.02600  1.000 46.79690  ? 220  SER   A N   1 
ATOM   1512 C CA  . SER   A 1 244 ? -37.61700 16.68900  14.68700  1.000 51.46786  ? 220  SER   A CA  1 
ATOM   1513 C C   . SER   A 1 244 ? -36.81000 16.89200  15.96000  1.000 51.24079  ? 220  SER   A C   1 
ATOM   1514 O O   . SER   A 1 244 ? -36.88300 16.07000  16.88100  1.000 50.75910  ? 220  SER   A O   1 
ATOM   1515 C CB  . SER   A 1 244 ? -36.88900 15.74000  13.73600  1.000 48.04882  ? 220  SER   A CB  1 
ATOM   1516 O OG  . SER   A 1 244 ? -37.77000 15.26300  12.73500  1.000 56.27394  ? 220  SER   A OG  1 
ATOM   1517 N N   . ARG   A 1 245 ? -36.04500 17.97800  16.03700  1.000 45.13469  ? 221  ARG   A N   1 
ATOM   1518 C CA  . ARG   A 1 245 ? -35.34600 18.31500  17.26600  1.000 48.25983  ? 221  ARG   A CA  1 
ATOM   1519 C C   . ARG   A 1 245 ? -36.22000 19.10900  18.22800  1.000 57.02906  ? 221  ARG   A C   1 
ATOM   1520 O O   . ARG   A 1 245 ? -35.88600 19.20500  19.41300  1.000 63.67082  ? 221  ARG   A O   1 
ATOM   1521 C CB  . ARG   A 1 245 ? -34.05900 19.07500  16.93500  1.000 44.83216  ? 221  ARG   A CB  1 
ATOM   1522 C CG  . ARG   A 1 245 ? -32.90200 18.11600  16.67200  1.000 57.58983  ? 221  ARG   A CG  1 
ATOM   1523 C CD  . ARG   A 1 245 ? -31.64000 18.77600  16.13400  1.000 68.27358  ? 221  ARG   A CD  1 
ATOM   1524 N NE  . ARG   A 1 245 ? -31.24700 19.98800  16.84100  1.000 68.40623  ? 221  ARG   A NE  1 
ATOM   1525 C CZ  . ARG   A 1 245 ? -29.98900 20.38500  16.97900  1.000 74.24555  ? 221  ARG   A CZ  1 
ATOM   1526 N NH1 . ARG   A 1 245 ? -28.98300 19.66900  16.50300  1.000 75.50332  ? 221  ARG   A NH1 1 
ATOM   1527 N NH2 . ARG   A 1 245 ? -29.73300 21.52500  17.61600  1.000 70.22215  ? 221  ARG   A NH2 1 
ATOM   1528 N N   . VAL   A 1 246 ? -37.33300 19.67000  17.74600  1.000 54.16078  ? 222  VAL   A N   1 
ATOM   1529 C CA  . VAL   A 1 246 ? -38.34900 20.19800  18.65000  1.000 49.30422  ? 222  VAL   A CA  1 
ATOM   1530 C C   . VAL   A 1 246 ? -39.06200 19.05400  19.35000  1.000 53.28301  ? 222  VAL   A C   1 
ATOM   1531 O O   . VAL   A 1 246 ? -39.36300 19.12400  20.54900  1.000 55.22760  ? 222  VAL   A O   1 
ATOM   1532 C CB  . VAL   A 1 246 ? -39.34700 21.08400  17.88200  1.000 46.33911  ? 222  VAL   A CB  1 
ATOM   1533 C CG1 . VAL   A 1 246 ? -40.62000 21.29200  18.69500  1.000 39.03039  ? 222  VAL   A CG1 1 
ATOM   1534 C CG2 . VAL   A 1 246 ? -38.72200 22.39400  17.52200  1.000 42.56619  ? 222  VAL   A CG2 1 
ATOM   1535 N N   . PHE   A 1 247 ? -39.34400 17.98300  18.60900  1.000 46.92874  ? 223  PHE   A N   1 
ATOM   1536 C CA  . PHE   A 1 247 ? -40.04900 16.84200  19.17700  1.000 54.20973  ? 223  PHE   A CA  1 
ATOM   1537 C C   . PHE   A 1 247 ? -39.22600 16.15100  20.25300  1.000 57.76731  ? 223  PHE   A C   1 
ATOM   1538 O O   . PHE   A 1 247 ? -39.76700 15.74300  21.28700  1.000 58.13920  ? 223  PHE   A O   1 
ATOM   1539 C CB  . PHE   A 1 247 ? -40.41600 15.85500  18.07200  1.000 55.62323  ? 223  PHE   A CB  1 
ATOM   1540 C CG  . PHE   A 1 247 ? -41.81200 16.01600  17.56100  1.000 56.78371  ? 223  PHE   A CG  1 
ATOM   1541 C CD1 . PHE   A 1 247 ? -42.58700 17.09400  17.95800  1.000 54.91984  ? 223  PHE   A CD1 1 
ATOM   1542 C CD2 . PHE   A 1 247 ? -42.35300 15.09200  16.68600  1.000 53.15716  ? 223  PHE   A CD2 1 
ATOM   1543 C CE1 . PHE   A 1 247 ? -43.87600 17.24200  17.49400  1.000 51.60023  ? 223  PHE   A CE1 1 
ATOM   1544 C CE2 . PHE   A 1 247 ? -43.64100 15.23700  16.21500  1.000 55.81401  ? 223  PHE   A CE2 1 
ATOM   1545 C CZ  . PHE   A 1 247 ? -44.40300 16.31400  16.61700  1.000 53.16524  ? 223  PHE   A CZ  1 
ATOM   1546 N N   . GLN   A 1 248 ? -37.91900 16.00500  20.03200  1.000 62.23450  ? 224  GLN   A N   1 
ATOM   1547 C CA  . GLN   A 1 248 ? -37.12900 15.24000  20.98600  1.000 62.67738  ? 224  GLN   A CA  1 
ATOM   1548 C C   . GLN   A 1 248 ? -36.71400 16.08000  22.18700  1.000 58.46849  ? 224  GLN   A C   1 
ATOM   1549 O O   . GLN   A 1 248 ? -36.62100 15.54500  23.29500  1.000 59.51142  ? 224  GLN   A O   1 
ATOM   1550 C CB  . GLN   A 1 248 ? -35.91100 14.62000  20.30000  1.000 60.73138  ? 224  GLN   A CB  1 
ATOM   1551 C CG  . GLN   A 1 248 ? -35.48600 13.30900  20.95400  1.000 76.83098  ? 224  GLN   A CG  1 
ATOM   1552 C CD  . GLN   A 1 248 ? -34.49200 12.51400  20.12600  1.000 89.02987  ? 224  GLN   A CD  1 
ATOM   1553 O OE1 . GLN   A 1 248 ? -33.98700 12.98900  19.10800  1.000 91.68706  ? 224  GLN   A OE1 1 
ATOM   1554 N NE2 . GLN   A 1 248 ? -34.21300 11.28800  20.56000  1.000 83.73811  ? 224  GLN   A NE2 1 
ATOM   1555 N N   . GLU   A 1 249 ? -36.47900 17.38400  22.00500  1.000 51.81858  ? 225  GLU   A N   1 
ATOM   1556 C CA  . GLU   A 1 249 ? -36.25400 18.24500  23.16200  1.000 53.56095  ? 225  GLU   A CA  1 
ATOM   1557 C C   . GLU   A 1 249 ? -37.48200 18.32400  24.06000  1.000 57.29361  ? 225  GLU   A C   1 
ATOM   1558 O O   . GLU   A 1 249 ? -37.35000 18.63100  25.24900  1.000 54.24765  ? 225  GLU   A O   1 
ATOM   1559 C CB  . GLU   A 1 249 ? -35.84300 19.64900  22.72100  1.000 45.85496  ? 225  GLU   A CB  1 
ATOM   1560 C CG  . GLU   A 1 249 ? -34.33900 19.85800  22.67200  1.000 60.32171  ? 225  GLU   A CG  1 
ATOM   1561 C CD  . GLU   A 1 249 ? -33.94100 21.27400  23.03700  1.000 68.45072  ? 225  GLU   A CD  1 
ATOM   1562 O OE1 . GLU   A 1 249 ? -34.75600 22.19000  22.79800  1.000 67.27411  ? 225  GLU   A OE1 1 
ATOM   1563 O OE2 . GLU   A 1 249 ? -32.82500 21.47000  23.57000  1.000 60.53099  ? 225  GLU   A OE2 1 
ATOM   1564 N N   . ALA   A 1 250 ? -38.67000 18.06300  23.51300  1.000 58.86080  ? 226  ALA   A N   1 
ATOM   1565 C CA  . ALA   A 1 250 ? -39.86500 17.92800  24.33700  1.000 49.01818  ? 226  ALA   A CA  1 
ATOM   1566 C C   . ALA   A 1 250 ? -39.81200 16.64500  25.15000  1.000 54.27070  ? 226  ALA   A C   1 
ATOM   1567 O O   . ALA   A 1 250 ? -39.87800 16.67100  26.38400  1.000 67.13253  ? 226  ALA   A O   1 
ATOM   1568 C CB  . ALA   A 1 250 ? -41.11500 17.95200  23.45600  1.000 47.92143  ? 226  ALA   A CB  1 
ATOM   1569 N N   . LYS   A 1 251 ? -39.69500 15.50400  24.46400  1.000 55.83604  ? 227  LYS   A N   1 
ATOM   1570 C CA  . LYS   A 1 251 ? -39.54100 14.22200  25.13900  1.000 56.52854  ? 227  LYS   A CA  1 
ATOM   1571 C C   . LYS   A 1 251 ? -38.28000 14.18200  25.99500  1.000 58.97324  ? 227  LYS   A C   1 
ATOM   1572 O O   . LYS   A 1 251 ? -38.20800 13.38900  26.94000  1.000 63.28934  ? 227  LYS   A O   1 
ATOM   1573 C CB  . LYS   A 1 251 ? -39.54600 13.09900  24.09200  1.000 62.57532  ? 227  LYS   A CB  1 
ATOM   1574 C CG  . LYS   A 1 251 ? -39.30400 11.68800  24.61000  1.000 55.10158  ? 227  LYS   A CG  1 
ATOM   1575 C CD  . LYS   A 1 251 ? -37.89800 11.21000  24.27700  1.000 60.53454  ? 227  LYS   A CD  1 
ATOM   1576 C CE  . LYS   A 1 251 ? -37.74700 9.71000   24.51400  1.000 68.11417  ? 227  LYS   A CE  1 
ATOM   1577 N NZ  . LYS   A 1 251 ? -38.44300 8.89300   23.47400  1.000 60.79128  ? 227  LYS   A NZ  1 
ATOM   1578 N N   . ARG   A 1 252 ? -37.29800 15.04000  25.70400  1.000 60.37435  ? 228  ARG   A N   1 
ATOM   1579 C CA  . ARG   A 1 252 ? -36.11800 15.14500  26.55900  1.000 59.95917  ? 228  ARG   A CA  1 
ATOM   1580 C C   . ARG   A 1 252 ? -36.44800 15.84500  27.87200  1.000 57.47601  ? 228  ARG   A C   1 
ATOM   1581 O O   . ARG   A 1 252 ? -36.10400 15.35400  28.95300  1.000 66.90340  ? 228  ARG   A O   1 
ATOM   1582 C CB  . ARG   A 1 252 ? -34.99900 15.88900  25.82400  1.000 58.86996  ? 228  ARG   A CB  1 
ATOM   1583 C CG  . ARG   A 1 252 ? -33.68300 15.97300  26.58200  1.000 62.92565  ? 228  ARG   A CG  1 
ATOM   1584 C CD  . ARG   A 1 252 ? -32.92000 17.25000  26.24500  1.000 62.61024  ? 228  ARG   A CD  1 
ATOM   1585 N NE  . ARG   A 1 252 ? -31.94600 17.03300  25.18000  1.000 76.82267  ? 228  ARG   A NE  1 
ATOM   1586 C CZ  . ARG   A 1 252 ? -30.98500 17.88600  24.85000  1.000 83.59944  ? 228  ARG   A CZ  1 
ATOM   1587 N NH1 . ARG   A 1 252 ? -30.83600 19.03800  25.48300  1.000 91.66568  ? 228  ARG   A NH1 1 
ATOM   1588 N NH2 . ARG   A 1 252 ? -30.15400 17.57600  23.85900  1.000 75.55826  ? 228  ARG   A NH2 1 
ATOM   1589 N N   . GLN   A 1 253 ? -37.12300 16.99000  27.80000  1.000 53.75040  ? 229  GLN   A N   1 
ATOM   1590 C CA  . GLN   A 1 253 ? -37.31600 17.85800  28.95400  1.000 52.47291  ? 229  GLN   A CA  1 
ATOM   1591 C C   . GLN   A 1 253 ? -38.42300 17.38300  29.89700  1.000 60.20691  ? 229  GLN   A C   1 
ATOM   1592 O O   . GLN   A 1 253 ? -38.76300 18.10400  30.84500  1.000 53.69767  ? 229  GLN   A O   1 
ATOM   1593 C CB  . GLN   A 1 253 ? -37.60000 19.28300  28.47800  1.000 41.89778  ? 229  GLN   A CB  1 
ATOM   1594 C CG  . GLN   A 1 253 ? -36.38500 20.18300  28.51900  1.000 40.59318  ? 229  GLN   A CG  1 
ATOM   1595 C CD  . GLN   A 1 253 ? -36.61200 21.49600  27.80600  1.000 54.47880  ? 229  GLN   A CD  1 
ATOM   1596 O OE1 . GLN   A 1 253 ? -36.47300 22.56800  28.39500  1.000 57.36193  ? 229  GLN   A OE1 1 
ATOM   1597 N NE2 . GLN   A 1 253 ? -36.94700 21.42200  26.52200  1.000 55.35304  ? 229  GLN   A NE2 1 
ATOM   1598 N N   . LEU   A 1 254 ? -38.98200 16.19800  29.67000  1.000 55.95570  ? 230  LEU   A N   1 
ATOM   1599 C CA  . LEU   A 1 254 ? -39.97700 15.63100  30.57200  1.000 54.52713  ? 230  LEU   A CA  1 
ATOM   1600 C C   . LEU   A 1 254 ? -39.40400 15.39400  31.96600  1.000 61.67970  ? 230  LEU   A C   1 
ATOM   1601 O O   . LEU   A 1 254 ? -38.18900 15.29900  32.14300  1.000 59.93889  ? 230  LEU   A O   1 
ATOM   1602 C CB  . LEU   A 1 254 ? -40.52000 14.32100  30.00500  1.000 62.03234  ? 230  LEU   A CB  1 
ATOM   1603 C CG  . LEU   A 1 254 ? -41.82500 14.44200  29.22700  1.000 65.51480  ? 230  LEU   A CG  1 
ATOM   1604 C CD1 . LEU   A 1 254 ? -42.32600 13.06800  28.82300  1.000 59.78117  ? 230  LEU   A CD1 1 
ATOM   1605 C CD2 . LEU   A 1 254 ? -42.84300 15.15900  30.09200  1.000 59.35358  ? 230  LEU   A CD2 1 
ATOM   1606 N N   . LYS   A 1 287 ? -44.98900 8.65400   24.12300  1.000 77.11292  ? 263  LYS   A N   1 
ATOM   1607 C CA  . LYS   A 1 287 ? -44.94000 10.04200  24.65200  1.000 66.21228  ? 263  LYS   A CA  1 
ATOM   1608 C C   . LYS   A 1 287 ? -46.25400 10.75700  24.30700  1.000 65.38258  ? 263  LYS   A C   1 
ATOM   1609 O O   . LYS   A 1 287 ? -47.25900 10.04200  24.10700  1.000 69.93899  ? 263  LYS   A O   1 
ATOM   1610 C CB  . LYS   A 1 287 ? -43.71000 10.75900  24.08400  1.000 66.89380  ? 263  LYS   A CB  1 
ATOM   1611 C CG  . LYS   A 1 287 ? -43.15900 11.93300  24.88300  1.000 66.71385  ? 263  LYS   A CG  1 
ATOM   1612 C CD  . LYS   A 1 287 ? -43.18900 13.22700  24.07600  1.000 69.17114  ? 263  LYS   A CD  1 
ATOM   1613 C CE  . LYS   A 1 287 ? -43.54600 14.42400  24.89600  1.000 65.44025  ? 263  LYS   A CE  1 
ATOM   1614 N NZ  . LYS   A 1 287 ? -44.52600 14.11300  25.93900  1.000 78.61195  ? 263  LYS   A NZ  1 
ATOM   1615 N N   . PHE   A 1 288 ? -46.26000 12.09400  24.29200  1.000 59.51265  ? 264  PHE   A N   1 
ATOM   1616 C CA  . PHE   A 1 288 ? -47.43200 12.86100  23.86800  1.000 60.96636  ? 264  PHE   A CA  1 
ATOM   1617 C C   . PHE   A 1 288 ? -48.60600 12.62500  24.80700  1.000 55.97677  ? 264  PHE   A C   1 
ATOM   1618 O O   . PHE   A 1 288 ? -49.61000 12.01000  24.43900  1.000 48.89087  ? 264  PHE   A O   1 
ATOM   1619 C CB  . PHE   A 1 288 ? -47.78300 12.54300  22.40900  1.000 63.67959  ? 264  PHE   A CB  1 
ATOM   1620 C CG  . PHE   A 1 288 ? -46.59800 12.62900  21.47400  1.000 64.34107  ? 264  PHE   A CG  1 
ATOM   1621 C CD1 . PHE   A 1 288 ? -46.12400 13.86400  21.04900  1.000 61.75070  ? 264  PHE   A CD1 1 
ATOM   1622 C CD2 . PHE   A 1 288 ? -45.94900 11.48400  21.03500  1.000 59.23023  ? 264  PHE   A CD2 1 
ATOM   1623 C CE1 . PHE   A 1 288 ? -45.03300 13.95600  20.20200  1.000 52.51673  ? 264  PHE   A CE1 1 
ATOM   1624 C CE2 . PHE   A 1 288 ? -44.85600 11.57300  20.19000  1.000 56.32955  ? 264  PHE   A CE2 1 
ATOM   1625 C CZ  . PHE   A 1 288 ? -44.40100 12.81200  19.77400  1.000 53.87221  ? 264  PHE   A CZ  1 
ATOM   1626 N N   . CYS   A 1 289 ? -48.46900 13.12100  26.03000  1.000 63.10031  ? 265  CYS   A N   1 
ATOM   1627 C CA  . CYS   A 1 289 ? -49.52700 13.07600  27.02700  1.000 58.35379  ? 265  CYS   A CA  1 
ATOM   1628 C C   . CYS   A 1 289 ? -49.88800 14.44600  27.57700  1.000 52.12677  ? 265  CYS   A C   1 
ATOM   1629 O O   . CYS   A 1 289 ? -51.07100 14.71700  27.79000  1.000 58.78368  ? 265  CYS   A O   1 
ATOM   1630 C CB  . CYS   A 1 289 ? -49.13300 12.14000  28.17500  1.000 63.51031  ? 265  CYS   A CB  1 
ATOM   1631 S SG  . CYS   A 1 289 ? -48.78100 10.42900  27.69300  1.000 66.17868  ? 265  CYS   A SG  1 
ATOM   1632 N N   . LEU   A 1 290 ? -48.91200 15.32300  27.80500  1.000 44.68654  ? 266  LEU   A N   1 
ATOM   1633 C CA  . LEU   A 1 290 ? -49.23300 16.70500  28.14400  1.000 48.02689  ? 266  LEU   A CA  1 
ATOM   1634 C C   . LEU   A 1 290 ? -50.08300 17.31600  27.03400  1.000 47.99047  ? 266  LEU   A C   1 
ATOM   1635 O O   . LEU   A 1 290 ? -50.02400 16.89200  25.87700  1.000 58.74119  ? 266  LEU   A O   1 
ATOM   1636 C CB  . LEU   A 1 290 ? -47.96500 17.53600  28.33000  1.000 48.83884  ? 266  LEU   A CB  1 
ATOM   1637 C CG  . LEU   A 1 290 ? -47.02400 17.26700  29.50400  1.000 50.73139  ? 266  LEU   A CG  1 
ATOM   1638 C CD1 . LEU   A 1 290 ? -46.12500 16.09400  29.18800  1.000 55.14762  ? 266  LEU   A CD1 1 
ATOM   1639 C CD2 . LEU   A 1 290 ? -46.18900 18.50700  29.81500  1.000 45.51421  ? 266  LEU   A CD2 1 
ATOM   1640 N N   . LYS   A 1 291 ? -50.88500 18.32500  27.38800  1.000 37.57030  ? 267  LYS   A N   1 
ATOM   1641 C CA  . LYS   A 1 291 ? -51.74000 18.94900  26.38000  1.000 39.68710  ? 267  LYS   A CA  1 
ATOM   1642 C C   . LYS   A 1 291 ? -50.90500 19.63600  25.30600  1.000 44.90894  ? 267  LYS   A C   1 
ATOM   1643 O O   . LYS   A 1 291 ? -51.10200 19.40200  24.10600  1.000 38.56983  ? 267  LYS   A O   1 
ATOM   1644 C CB  . LYS   A 1 291 ? -52.70100 19.95300  27.01900  1.000 29.17385  ? 267  LYS   A CB  1 
ATOM   1645 C CG  . LYS   A 1 291 ? -53.56000 20.67800  25.99200  1.000 25.00470  ? 267  LYS   A CG  1 
ATOM   1646 C CD  . LYS   A 1 291 ? -54.74900 21.36300  26.62000  1.000 23.99131  ? 267  LYS   A CD  1 
ATOM   1647 C CE  . LYS   A 1 291 ? -54.38700 22.75400  27.09900  1.000 30.47416  ? 267  LYS   A CE  1 
ATOM   1648 N NZ  . LYS   A 1 291 ? -54.63600 23.76600  26.03700  1.000 29.39603  ? 267  LYS   A NZ  1 
ATOM   1649 N N   . GLU   A 1 292 ? -49.96100 20.48400  25.72000  1.000 41.55430  ? 268  GLU   A N   1 
ATOM   1650 C CA  . GLU   A 1 292 ? -49.17700 21.23500  24.74800  1.000 36.51467  ? 268  GLU   A CA  1 
ATOM   1651 C C   . GLU   A 1 292 ? -48.30600 20.31800  23.90400  1.000 41.88268  ? 268  GLU   A C   1 
ATOM   1652 O O   . GLU   A 1 292 ? -48.08600 20.59500  22.72100  1.000 45.48376  ? 268  GLU   A O   1 
ATOM   1653 C CB  . GLU   A 1 292 ? -48.32500 22.28000  25.46600  1.000 30.38605  ? 268  GLU   A CB  1 
ATOM   1654 C CG  . GLU   A 1 292 ? -49.13500 23.45100  25.97400  1.000 32.32123  ? 268  GLU   A CG  1 
ATOM   1655 C CD  . GLU   A 1 292 ? -49.61500 24.35300  24.85800  1.000 33.14059  ? 268  GLU   A CD  1 
ATOM   1656 O OE1 . GLU   A 1 292 ? -48.77700 24.81900  24.06800  1.000 32.52204  ? 268  GLU   A OE1 1 
ATOM   1657 O OE2 . GLU   A 1 292 ? -50.83800 24.58300  24.76000  1.000 41.87375  ? 268  GLU   A OE2 1 
ATOM   1658 N N   . HIS   A 1 293 ? -47.82300 19.21800  24.48400  1.000 39.76426  ? 269  HIS   A N   1 
ATOM   1659 C CA  . HIS   A 1 293 ? -46.99500 18.28200  23.73600  1.000 44.55004  ? 269  HIS   A CA  1 
ATOM   1660 C C   . HIS   A 1 293 ? -47.80300 17.53300  22.68500  1.000 46.53612  ? 269  HIS   A C   1 
ATOM   1661 O O   . HIS   A 1 293 ? -47.22600 17.03200  21.71300  1.000 45.09935  ? 269  HIS   A O   1 
ATOM   1662 C CB  . HIS   A 1 293 ? -46.30600 17.32900  24.71600  1.000 45.86952  ? 269  HIS   A CB  1 
ATOM   1663 C CG  . HIS   A 1 293 ? -45.14100 17.95500  25.41600  1.000 37.79054  ? 269  HIS   A CG  1 
ATOM   1664 N ND1 . HIS   A 1 293 ? -44.38700 17.30200  26.36700  1.000 40.85324  ? 269  HIS   A ND1 1 
ATOM   1665 C CD2 . HIS   A 1 293 ? -44.58600 19.18200  25.27700  1.000 42.80987  ? 269  HIS   A CD2 1 
ATOM   1666 C CE1 . HIS   A 1 293 ? -43.43000 18.10400  26.79800  1.000 48.28573  ? 269  HIS   A CE1 1 
ATOM   1667 N NE2 . HIS   A 1 293 ? -43.53100 19.25300  26.15400  1.000 47.53636  ? 269  HIS   A NE2 1 
ATOM   1668 N N   . LYS   A 1 294 ? -49.12500 17.46900  22.84800  1.000 45.49039  ? 270  LYS   A N   1 
ATOM   1669 C CA  . LYS   A 1 294 ? -49.98600 17.00300  21.76900  1.000 46.77168  ? 270  LYS   A CA  1 
ATOM   1670 C C   . LYS   A 1 294 ? -50.20700 18.08500  20.72200  1.000 41.38090  ? 270  LYS   A C   1 
ATOM   1671 O O   . LYS   A 1 294 ? -50.43100 17.76900  19.54900  1.000 43.88968  ? 270  LYS   A O   1 
ATOM   1672 C CB  . LYS   A 1 294 ? -51.32800 16.53100  22.33200  1.000 48.24161  ? 270  LYS   A CB  1 
ATOM   1673 C CG  . LYS   A 1 294 ? -51.23400 15.30000  23.21000  1.000 48.36364  ? 270  LYS   A CG  1 
ATOM   1674 C CD  . LYS   A 1 294 ? -52.60900 14.75600  23.54000  1.000 50.32622  ? 270  LYS   A CD  1 
ATOM   1675 C CE  . LYS   A 1 294 ? -52.50900 13.47400  24.34600  1.000 64.75411  ? 270  LYS   A CE  1 
ATOM   1676 N NZ  . LYS   A 1 294 ? -53.83700 12.83600  24.55600  1.000 79.54411  ? 270  LYS   A NZ  1 
ATOM   1677 N N   . ALA   A 1 295 ? -50.15700 19.35900  21.12600  1.000 34.51498  ? 271  ALA   A N   1 
ATOM   1678 C CA  . ALA   A 1 295 ? -50.22500 20.44600  20.15700  1.000 37.69527  ? 271  ALA   A CA  1 
ATOM   1679 C C   . ALA   A 1 295 ? -49.03200 20.40200  19.20900  1.000 47.44189  ? 271  ALA   A C   1 
ATOM   1680 O O   . ALA   A 1 295 ? -49.18300 20.58500  17.99300  1.000 39.09206  ? 271  ALA   A O   1 
ATOM   1681 C CB  . ALA   A 1 295 ? -50.29600 21.79100  20.88300  1.000 25.90419  ? 271  ALA   A CB  1 
ATOM   1682 N N   . LEU   A 1 296 ? -47.83500 20.15700  19.75300  1.000 41.23117  ? 272  LEU   A N   1 
ATOM   1683 C CA  . LEU   A 1 296 ? -46.65800 19.97800  18.91100  1.000 35.80016  ? 272  LEU   A CA  1 
ATOM   1684 C C   . LEU   A 1 296 ? -46.83300 18.79500  17.96800  1.000 45.92845  ? 272  LEU   A C   1 
ATOM   1685 O O   . LEU   A 1 296 ? -46.42900 18.85600  16.80000  1.000 47.56948  ? 272  LEU   A O   1 
ATOM   1686 C CB  . LEU   A 1 296 ? -45.41600 19.79600  19.78100  1.000 29.83241  ? 272  LEU   A CB  1 
ATOM   1687 C CG  . LEU   A 1 296 ? -45.05600 20.99000  20.65900  1.000 33.81692  ? 272  LEU   A CG  1 
ATOM   1688 C CD1 . LEU   A 1 296 ? -43.82300 20.69500  21.49900  1.000 29.22350  ? 272  LEU   A CD1 1 
ATOM   1689 C CD2 . LEU   A 1 296 ? -44.84600 22.22600  19.80100  1.000 32.54579  ? 272  LEU   A CD2 1 
ATOM   1690 N N   . LYS   A 1 297 ? -47.43400 17.70700  18.45600  1.000 41.47025  ? 273  LYS   A N   1 
ATOM   1691 C CA  . LYS   A 1 297 ? -47.73500 16.58100  17.58000  1.000 39.77752  ? 273  LYS   A CA  1 
ATOM   1692 C C   . LYS   A 1 297 ? -48.72500 16.98400  16.49600  1.000 42.87051  ? 273  LYS   A C   1 
ATOM   1693 O O   . LYS   A 1 297 ? -48.61800 16.53500  15.34900  1.000 42.75370  ? 273  LYS   A O   1 
ATOM   1694 C CB  . LYS   A 1 297 ? -48.27600 15.40300  18.39100  1.000 43.73462  ? 273  LYS   A CB  1 
ATOM   1695 C CG  . LYS   A 1 297 ? -48.68800 14.21400  17.53600  1.000 40.51093  ? 273  LYS   A CG  1 
ATOM   1696 C CD  . LYS   A 1 297 ? -48.84400 12.94000  18.34800  1.000 42.22671  ? 273  LYS   A CD  1 
ATOM   1697 C CE  . LYS   A 1 297 ? -49.27500 11.78600  17.45500  1.000 43.06490  ? 273  LYS   A CE  1 
ATOM   1698 N NZ  . LYS   A 1 297 ? -49.30700 10.47900  18.16500  1.000 44.90103  ? 273  LYS   A NZ  1 
ATOM   1699 N N   . THR   A 1 298 ? -49.69000 17.84000  16.83800  1.000 43.20579  ? 274  THR   A N   1 
ATOM   1700 C CA  . THR   A 1 298 ? -50.67900 18.26700  15.85300  1.000 45.78045  ? 274  THR   A CA  1 
ATOM   1701 C C   . THR   A 1 298 ? -50.01900 19.05000  14.72500  1.000 46.52467  ? 274  THR   A C   1 
ATOM   1702 O O   . THR   A 1 298 ? -50.31600 18.83000  13.54400  1.000 47.22992  ? 274  THR   A O   1 
ATOM   1703 C CB  . THR   A 1 298 ? -51.76800 19.10200  16.52400  1.000 38.26709  ? 274  THR   A CB  1 
ATOM   1704 O OG1 . THR   A 1 298 ? -52.43900 18.30400  17.50600  1.000 48.38968  ? 274  THR   A OG1 1 
ATOM   1705 C CG2 . THR   A 1 298 ? -52.77700 19.57100  15.49400  1.000 35.60631  ? 274  THR   A CG2 1 
ATOM   1706 N N   . LEU   A 1 299 ? -49.12000 19.97200  15.07000  1.000 40.26714  ? 275  LEU   A N   1 
ATOM   1707 C CA  . LEU   A 1 299 ? -48.34300 20.65800  14.04600  1.000 38.48755  ? 275  LEU   A CA  1 
ATOM   1708 C C   . LEU   A 1 299 ? -47.54100 19.66200  13.21900  1.000 44.82606  ? 275  LEU   A C   1 
ATOM   1709 O O   . LEU   A 1 299 ? -47.53400 19.72500  11.98300  1.000 41.05710  ? 275  LEU   A O   1 
ATOM   1710 C CB  . LEU   A 1 299 ? -47.42200 21.69200  14.69000  1.000 34.00462  ? 275  LEU   A CB  1 
ATOM   1711 C CG  . LEU   A 1 299 ? -48.14700 22.87300  15.32900  1.000 36.98811  ? 275  LEU   A CG  1 
ATOM   1712 C CD1 . LEU   A 1 299 ? -47.19800 23.70500  16.17200  1.000 37.32382  ? 275  LEU   A CD1 1 
ATOM   1713 C CD2 . LEU   A 1 299 ? -48.80300 23.72200  14.25200  1.000 32.08326  ? 275  LEU   A CD2 1 
ATOM   1714 N N   . GLY   A 1 300 ? -46.87400 18.71800  13.88700  1.000 43.53951  ? 276  GLY   A N   1 
ATOM   1715 C CA  . GLY   A 1 300 ? -46.11700 17.70900  13.16900  1.000 40.83772  ? 276  GLY   A CA  1 
ATOM   1716 C C   . GLY   A 1 300 ? -46.95600 16.92300  12.18200  1.000 38.40676  ? 276  GLY   A C   1 
ATOM   1717 O O   . GLY   A 1 300 ? -46.45400 16.48200  11.14800  1.000 46.16258  ? 276  GLY   A O   1 
ATOM   1718 N N   . ILE   A 1 301 ? -48.24100 16.74000  12.47900  1.000 39.20570  ? 277  ILE   A N   1 
ATOM   1719 C CA  . ILE   A 1 301 ? -49.11300 16.05000  11.53600  1.000 44.97158  ? 277  ILE   A CA  1 
ATOM   1720 C C   . ILE   A 1 301 ? -49.40700 16.93900  10.33400  1.000 47.96357  ? 277  ILE   A C   1 
ATOM   1721 O O   . ILE   A 1 301 ? -49.43500 16.46800  9.19000   1.000 42.59342  ? 277  ILE   A O   1 
ATOM   1722 C CB  . ILE   A 1 301 ? -50.40400 15.59300  12.23700  1.000 44.29287  ? 277  ILE   A CB  1 
ATOM   1723 C CG1 . ILE   A 1 301 ? -50.07300 14.59700  13.34800  1.000 42.97116  ? 277  ILE   A CG1 1 
ATOM   1724 C CG2 . ILE   A 1 301 ? -51.37600 14.99200  11.23600  1.000 38.62515  ? 277  ILE   A CG2 1 
ATOM   1725 C CD1 . ILE   A 1 301 ? -51.22600 14.32100  14.26600  1.000 46.69329  ? 277  ILE   A CD1 1 
ATOM   1726 N N   . ILE   A 1 302 ? -49.63400 18.23400  10.57300  1.000 47.04955  ? 278  ILE   A N   1 
ATOM   1727 C CA  . ILE   A 1 302 ? -49.83000 19.18400  9.47800   1.000 42.70647  ? 278  ILE   A CA  1 
ATOM   1728 C C   . ILE   A 1 302 ? -48.68000 19.08100  8.48900   1.000 44.73387  ? 278  ILE   A C   1 
ATOM   1729 O O   . ILE   A 1 302 ? -48.87300 18.81300  7.29700   1.000 46.18191  ? 278  ILE   A O   1 
ATOM   1730 C CB  . ILE   A 1 302 ? -49.96100 20.61500  10.02400  1.000 42.54730  ? 278  ILE   A CB  1 
ATOM   1731 C CG1 . ILE   A 1 302 ? -51.20800 20.72800  10.89300  1.000 45.70783  ? 278  ILE   A CG1 1 
ATOM   1732 C CG2 . ILE   A 1 302 ? -50.02900 21.61200  8.88500   1.000 38.79736  ? 278  ILE   A CG2 1 
ATOM   1733 C CD1 . ILE   A 1 302 ? -52.46300 20.48100  10.13100  1.000 40.42285  ? 278  ILE   A CD1 1 
ATOM   1734 N N   . MET   A 1 303 ? -47.46100 19.29400  8.98200   1.000 41.93908  ? 279  MET   A N   1 
ATOM   1735 C CA  . MET   A 1 303 ? -46.27400 19.08700  8.16500   1.000 39.13076  ? 279  MET   A CA  1 
ATOM   1736 C C   . MET   A 1 303 ? -46.23900 17.67000  7.60900   1.000 40.38609  ? 279  MET   A C   1 
ATOM   1737 O O   . MET   A 1 303 ? -45.94900 17.45700  6.42600   1.000 43.02648  ? 279  MET   A O   1 
ATOM   1738 C CB  . MET   A 1 303 ? -45.02800 19.36700  9.00200   1.000 36.48913  ? 279  MET   A CB  1 
ATOM   1739 C CG  . MET   A 1 303 ? -45.02900 20.73300  9.66600   1.000 40.42306  ? 279  MET   A CG  1 
ATOM   1740 S SD  . MET   A 1 303 ? -43.85000 20.85100  11.02600  1.000 41.96813  ? 279  MET   A SD  1 
ATOM   1741 C CE  . MET   A 1 303 ? -44.38000 22.36900  11.82100  1.000 40.46339  ? 279  MET   A CE  1 
ATOM   1742 N N   . GLY   A 1 304 ? -46.55600 16.68800  8.45500   1.000 39.66019  ? 280  GLY   A N   1 
ATOM   1743 C CA  . GLY   A 1 304 ? -46.44800 15.29700  8.04500   1.000 41.21947  ? 280  GLY   A CA  1 
ATOM   1744 C C   . GLY   A 1 304 ? -47.28800 14.97400  6.82600   1.000 42.13663  ? 280  GLY   A C   1 
ATOM   1745 O O   . GLY   A 1 304 ? -46.82000 14.32300  5.89200   1.000 39.59226  ? 280  GLY   A O   1 
ATOM   1746 N N   . THR   A 1 305 ? -48.54500 15.42200  6.81800   1.000 46.94245  ? 281  THR   A N   1 
ATOM   1747 C CA  . THR   A 1 305 ? -49.38900 15.18600  5.65000   1.000 46.50137  ? 281  THR   A CA  1 
ATOM   1748 C C   . THR   A 1 305 ? -48.94100 16.04300  4.47300   1.000 47.16405  ? 281  THR   A C   1 
ATOM   1749 O O   . THR   A 1 305 ? -48.83900 15.55200  3.34100   1.000 51.76882  ? 281  THR   A O   1 
ATOM   1750 C CB  . THR   A 1 305 ? -50.86100 15.45200  5.98100   1.000 42.98098  ? 281  THR   A CB  1 
ATOM   1751 O OG1 . THR   A 1 305 ? -51.10700 16.86400  6.01600   1.000 47.09943  ? 281  THR   A OG1 1 
ATOM   1752 C CG2 . THR   A 1 305 ? -51.23400 14.83100  7.31600   1.000 41.44829  ? 281  THR   A CG2 1 
ATOM   1753 N N   . PHE   A 1 306 ? -48.66600 17.32700  4.72500   1.000 43.90293  ? 282  PHE   A N   1 
ATOM   1754 C CA  . PHE   A 1 306 ? -48.23800 18.23400  3.66300   1.000 39.55139  ? 282  PHE   A CA  1 
ATOM   1755 C C   . PHE   A 1 306 ? -47.09600 17.63700  2.85900   1.000 41.80008  ? 282  PHE   A C   1 
ATOM   1756 O O   . PHE   A 1 306 ? -47.14500 17.59300  1.62500   1.000 43.90927  ? 282  PHE   A O   1 
ATOM   1757 C CB  . PHE   A 1 306 ? -47.82300 19.57800  4.26100   1.000 34.53557  ? 282  PHE   A CB  1 
ATOM   1758 C CG  . PHE   A 1 306 ? -47.55300 20.64600  3.23900   1.000 30.46107  ? 282  PHE   A CG  1 
ATOM   1759 C CD1 . PHE   A 1 306 ? -46.28700 20.80200  2.69800   1.000 42.24129  ? 282  PHE   A CD1 1 
ATOM   1760 C CD2 . PHE   A 1 306 ? -48.55200 21.51400  2.84400   1.000 30.23658  ? 282  PHE   A CD2 1 
ATOM   1761 C CE1 . PHE   A 1 306 ? -46.03000 21.79500  1.77000   1.000 39.93965  ? 282  PHE   A CE1 1 
ATOM   1762 C CE2 . PHE   A 1 306 ? -48.30100 22.50800  1.92000   1.000 31.17019  ? 282  PHE   A CE2 1 
ATOM   1763 C CZ  . PHE   A 1 306 ? -47.04100 22.64900  1.38200   1.000 36.62179  ? 282  PHE   A CZ  1 
ATOM   1764 N N   . THR   A 1 307 ? -46.05800 17.16600  3.55200   1.000 45.42781  ? 283  THR   A N   1 
ATOM   1765 C CA  . THR   A 1 307 ? -44.95700 16.48400  2.88600   1.000 45.47641  ? 283  THR   A CA  1 
ATOM   1766 C C   . THR   A 1 307 ? -45.47500 15.32900  2.03900   1.000 45.47908  ? 283  THR   A C   1 
ATOM   1767 O O   . THR   A 1 307 ? -45.24800 15.28000  0.82700   1.000 53.52555  ? 283  THR   A O   1 
ATOM   1768 C CB  . THR   A 1 307 ? -43.94100 15.98700  3.92100   1.000 44.19558  ? 283  THR   A CB  1 
ATOM   1769 O OG1 . THR   A 1 307 ? -43.34800 17.10700  4.59200   1.000 42.20161  ? 283  THR   A OG1 1 
ATOM   1770 C CG2 . THR   A 1 307 ? -42.84800 15.17300  3.24900   1.000 44.18077  ? 283  THR   A CG2 1 
ATOM   1771 N N   . LEU   A 1 308 ? -46.21900 14.41100  2.65800   1.000 38.77968  ? 284  LEU   A N   1 
ATOM   1772 C CA  . LEU   A 1 308 ? -46.64800 13.21400  1.94300   1.000 41.83493  ? 284  LEU   A CA  1 
ATOM   1773 C C   . LEU   A 1 308 ? -47.57600 13.53900  0.77800   1.000 49.72464  ? 284  LEU   A C   1 
ATOM   1774 O O   . LEU   A 1 308 ? -47.60400 12.80000  -0.21200  1.000 47.33698  ? 284  LEU   A O   1 
ATOM   1775 C CB  . LEU   A 1 308 ? -47.32500 12.24100  2.90500   1.000 38.47236  ? 284  LEU   A CB  1 
ATOM   1776 C CG  . LEU   A 1 308 ? -46.45400 11.83400  4.09400   1.000 47.13987  ? 284  LEU   A CG  1 
ATOM   1777 C CD1 . LEU   A 1 308 ? -47.20100 10.86900  5.00400   1.000 43.98203  ? 284  LEU   A CD1 1 
ATOM   1778 C CD2 . LEU   A 1 308 ? -45.11600 11.25100  3.63600   1.000 37.97924  ? 284  LEU   A CD2 1 
ATOM   1779 N N   . CYS   A 1 309 ? -48.33700 14.63000  0.86500   1.000 50.33981  ? 285  CYS   A N   1 
ATOM   1780 C CA  . CYS   A 1 309 ? -49.25100 14.94800  -0.22600  1.000 51.56917  ? 285  CYS   A CA  1 
ATOM   1781 C C   . CYS   A 1 309 ? -48.51800 15.56300  -1.41300  1.000 52.82531  ? 285  CYS   A C   1 
ATOM   1782 O O   . CYS   A 1 309 ? -48.82600 15.24700  -2.56700  1.000 58.03165  ? 285  CYS   A O   1 
ATOM   1783 C CB  . CYS   A 1 309 ? -50.36200 15.88000  0.26300   1.000 49.05465  ? 285  CYS   A CB  1 
ATOM   1784 S SG  . CYS   A 1 309 ? -51.46300 15.14200  1.49800   1.000 45.86157  ? 285  CYS   A SG  1 
ATOM   1785 N N   . TRP   A 1 310 ? -47.54600 16.43500  -1.15500  1.000 47.10054  ? 286  TRP   A N   1 
ATOM   1786 C CA  . TRP   A 1 310 ? -46.86000 17.15300  -2.22000  1.000 47.22919  ? 286  TRP   A CA  1 
ATOM   1787 C C   . TRP   A 1 310 ? -45.54400 16.51300  -2.63800  1.000 46.89621  ? 286  TRP   A C   1 
ATOM   1788 O O   . TRP   A 1 310 ? -44.96900 16.93300  -3.64500  1.000 47.49540  ? 286  TRP   A O   1 
ATOM   1789 C CB  . TRP   A 1 310 ? -46.60100 18.60200  -1.79600  1.000 43.91649  ? 286  TRP   A CB  1 
ATOM   1790 C CG  . TRP   A 1 310 ? -47.75600 19.52900  -2.02600  1.000 42.35298  ? 286  TRP   A CG  1 
ATOM   1791 C CD1 . TRP   A 1 310 ? -48.51900 20.13800  -1.07700  1.000 43.00478  ? 286  TRP   A CD1 1 
ATOM   1792 C CD2 . TRP   A 1 310 ? -48.26300 19.96600  -3.29200  1.000 43.59899  ? 286  TRP   A CD2 1 
ATOM   1793 N NE1 . TRP   A 1 310 ? -49.47800 20.92200  -1.67100  1.000 44.46949  ? 286  TRP   A NE1 1 
ATOM   1794 C CE2 . TRP   A 1 310 ? -49.33900 20.83800  -3.03100  1.000 47.40296  ? 286  TRP   A CE2 1 
ATOM   1795 C CE3 . TRP   A 1 310 ? -47.91100 19.70700  -4.61800  1.000 48.72847  ? 286  TRP   A CE3 1 
ATOM   1796 C CZ2 . TRP   A 1 310 ? -50.07100 21.44500  -4.04800  1.000 41.89681  ? 286  TRP   A CZ2 1 
ATOM   1797 C CZ3 . TRP   A 1 310 ? -48.63600 20.31400  -5.62700  1.000 52.37571  ? 286  TRP   A CZ3 1 
ATOM   1798 C CH2 . TRP   A 1 310 ? -49.70500 21.17200  -5.33600  1.000 50.91051  ? 286  TRP   A CH2 1 
ATOM   1799 N N   . LEU   A 1 311 ? -45.05300 15.51800  -1.90300  1.000 49.40959  ? 287  LEU   A N   1 
ATOM   1800 C CA  . LEU   A 1 311 ? -43.74400 14.94500  -2.20700  1.000 50.25811  ? 287  LEU   A CA  1 
ATOM   1801 C C   . LEU   A 1 311 ? -43.76200 14.02100  -3.42400  1.000 48.17711  ? 287  LEU   A C   1 
ATOM   1802 O O   . LEU   A 1 311 ? -42.83200 14.09100  -4.23500  1.000 56.79928  ? 287  LEU   A O   1 
ATOM   1803 C CB  . LEU   A 1 311 ? -43.17900 14.20100  -0.99500  1.000 48.00197  ? 287  LEU   A CB  1 
ATOM   1804 C CG  . LEU   A 1 311 ? -41.67100 13.97000  -1.02400  1.000 52.31367  ? 287  LEU   A CG  1 
ATOM   1805 C CD1 . LEU   A 1 311 ? -40.94200 15.27800  -1.27400  1.000 49.95085  ? 287  LEU   A CD1 1 
ATOM   1806 C CD2 . LEU   A 1 311 ? -41.21500 13.34900  0.28600   1.000 47.85963  ? 287  LEU   A CD2 1 
ATOM   1807 N N   . PRO   A 1 312 ? -44.76000 13.14000  -3.60200  1.000 45.06910  ? 288  PRO   A N   1 
ATOM   1808 C CA  . PRO   A 1 312 ? -44.77500 12.33300  -4.83700  1.000 51.84218  ? 288  PRO   A CA  1 
ATOM   1809 C C   . PRO   A 1 312 ? -44.80500 13.17200  -6.10200  1.000 51.81556  ? 288  PRO   A C   1 
ATOM   1810 O O   . PRO   A 1 312 ? -44.10900 12.84800  -7.07200  1.000 45.06497  ? 288  PRO   A O   1 
ATOM   1811 C CB  . PRO   A 1 312 ? -46.04100 11.47600  -4.68700  1.000 48.17579  ? 288  PRO   A CB  1 
ATOM   1812 C CG  . PRO   A 1 312 ? -46.31100 11.44900  -3.23500  1.000 48.13288  ? 288  PRO   A CG  1 
ATOM   1813 C CD  . PRO   A 1 312 ? -45.87900 12.77800  -2.71600  1.000 50.28980  ? 288  PRO   A CD  1 
ATOM   1814 N N   . PHE   A 1 313 ? -45.59600 14.24700  -6.12000  1.000 54.51629  ? 289  PHE   A N   1 
ATOM   1815 C CA  . PHE   A 1 313 ? -45.57600 15.15000  -7.26600  1.000 49.96753  ? 289  PHE   A CA  1 
ATOM   1816 C C   . PHE   A 1 313 ? -44.18000 15.70500  -7.50300  1.000 50.79997  ? 289  PHE   A C   1 
ATOM   1817 O O   . PHE   A 1 313 ? -43.71200 15.76600  -8.64500  1.000 61.65489  ? 289  PHE   A O   1 
ATOM   1818 C CB  . PHE   A 1 313 ? -46.58600 16.28100  -7.06100  1.000 45.34254  ? 289  PHE   A CB  1 
ATOM   1819 C CG  . PHE   A 1 313 ? -46.36600 17.47100  -7.96100  1.000 44.68723  ? 289  PHE   A CG  1 
ATOM   1820 C CD1 . PHE   A 1 313 ? -45.48900 18.48700  -7.60600  1.000 39.16169  ? 289  PHE   A CD1 1 
ATOM   1821 C CD2 . PHE   A 1 313 ? -47.02900 17.56700  -9.17200  1.000 52.54277  ? 289  PHE   A CD2 1 
ATOM   1822 C CE1 . PHE   A 1 313 ? -45.28600 19.57200  -8.43200  1.000 39.84993  ? 289  PHE   A CE1 1 
ATOM   1823 C CE2 . PHE   A 1 313 ? -46.83000 18.65300  -10.00200 1.000 43.19787  ? 289  PHE   A CE2 1 
ATOM   1824 C CZ  . PHE   A 1 313 ? -45.95500 19.65400  -9.63000  1.000 41.32084  ? 289  PHE   A CZ  1 
ATOM   1825 N N   . PHE   A 1 314 ? -43.49600 16.11600  -6.43700  1.000 46.51338  ? 290  PHE   A N   1 
ATOM   1826 C CA  . PHE   A 1 314 ? -42.22200 16.79800  -6.60900  1.000 51.47157  ? 290  PHE   A CA  1 
ATOM   1827 C C   . PHE   A 1 314 ? -41.07600 15.83400  -6.88800  1.000 54.28207  ? 290  PHE   A C   1 
ATOM   1828 O O   . PHE   A 1 314 ? -40.04700 16.25800  -7.42600  1.000 55.17984  ? 290  PHE   A O   1 
ATOM   1829 C CB  . PHE   A 1 314 ? -41.92100 17.65200  -5.37600  1.000 45.80945  ? 290  PHE   A CB  1 
ATOM   1830 C CG  . PHE   A 1 314 ? -42.39200 19.07700  -5.50300  1.000 43.46518  ? 290  PHE   A CG  1 
ATOM   1831 C CD1 . PHE   A 1 314 ? -41.69200 19.99200  -6.27300  1.000 45.27653  ? 290  PHE   A CD1 1 
ATOM   1832 C CD2 . PHE   A 1 314 ? -43.54500 19.49800  -4.86100  1.000 38.72650  ? 290  PHE   A CD2 1 
ATOM   1833 C CE1 . PHE   A 1 314 ? -42.13200 21.30200  -6.39400  1.000 43.33454  ? 290  PHE   A CE1 1 
ATOM   1834 C CE2 . PHE   A 1 314 ? -43.98700 20.80600  -4.97600  1.000 36.78923  ? 290  PHE   A CE2 1 
ATOM   1835 C CZ  . PHE   A 1 314 ? -43.28000 21.70700  -5.74400  1.000 37.05789  ? 290  PHE   A CZ  1 
ATOM   1836 N N   . ILE   A 1 315 ? -41.22700 14.55300  -6.54700  1.000 52.52371  ? 291  ILE   A N   1 
ATOM   1837 C CA  . ILE   A 1 315 ? -40.21000 13.56900  -6.90600  1.000 55.26380  ? 291  ILE   A CA  1 
ATOM   1838 C C   . ILE   A 1 315 ? -40.30200 13.22600  -8.38900  1.000 62.72817  ? 291  ILE   A C   1 
ATOM   1839 O O   . ILE   A 1 315 ? -39.29400 13.22700  -9.10500  1.000 61.38276  ? 291  ILE   A O   1 
ATOM   1840 C CB  . ILE   A 1 315 ? -40.33200 12.31300  -6.02300  1.000 52.77906  ? 291  ILE   A CB  1 
ATOM   1841 C CG1 . ILE   A 1 315 ? -40.02500 12.64500  -4.55900  1.000 51.18445  ? 291  ILE   A CG1 1 
ATOM   1842 C CG2 . ILE   A 1 315 ? -39.41100 11.21100  -6.52600  1.000 55.15893  ? 291  ILE   A CG2 1 
ATOM   1843 C CD1 . ILE   A 1 315 ? -38.59900 13.09900  -4.32000  1.000 49.75854  ? 291  ILE   A CD1 1 
ATOM   1844 N N   . VAL   A 1 316 ? -41.51100 12.93000  -8.87700  1.000 64.15879  ? 292  VAL   A N   1 
ATOM   1845 C CA  . VAL   A 1 316 ? -41.66400 12.59500  -10.28800 1.000 64.57700  ? 292  VAL   A CA  1 
ATOM   1846 C C   . VAL   A 1 316 ? -41.37100 13.79600  -11.17000 1.000 66.93392  ? 292  VAL   A C   1 
ATOM   1847 O O   . VAL   A 1 316 ? -41.04900 13.63400  -12.35400 1.000 76.00788  ? 292  VAL   A O   1 
ATOM   1848 C CB  . VAL   A 1 316 ? -43.06700 12.02700  -10.59100 1.000 60.73696  ? 292  VAL   A CB  1 
ATOM   1849 C CG1 . VAL   A 1 316 ? -43.41000 10.91200  -9.61000  1.000 57.56017  ? 292  VAL   A CG1 1 
ATOM   1850 C CG2 . VAL   A 1 316 ? -44.12600 13.13100  -10.58200 1.000 57.38127  ? 292  VAL   A CG2 1 
ATOM   1851 N N   . ASN   A 1 317 ? -41.47500 15.00500  -10.62200 1.000 62.35568  ? 293  ASN   A N   1 
ATOM   1852 C CA  . ASN   A 1 317 ? -41.05800 16.17800  -11.37300 1.000 67.52474  ? 293  ASN   A CA  1 
ATOM   1853 C C   . ASN   A 1 317 ? -39.56100 16.11100  -11.63600 1.000 68.66341  ? 293  ASN   A C   1 
ATOM   1854 O O   . ASN   A 1 317 ? -39.10900 16.34400  -12.76400 1.000 74.58199  ? 293  ASN   A O   1 
ATOM   1855 C CB  . ASN   A 1 317 ? -41.46400 17.43900  -10.59700 1.000 64.53366  ? 293  ASN   A CB  1 
ATOM   1856 C CG  . ASN   A 1 317 ? -40.81200 18.73100  -11.11100 1.000 76.06723  ? 293  ASN   A CG  1 
ATOM   1857 O OD1 . ASN   A 1 317 ? -40.02900 18.74100  -12.06000 1.000 83.78136  ? 293  ASN   A OD1 1 
ATOM   1858 N ND2 . ASN   A 1 317 ? -41.16300 19.84400  -10.47100 1.000 63.88597  ? 293  ASN   A ND2 1 
ATOM   1859 N N   . ILE   A 1 318 ? -38.78100 15.73500  -10.62300 1.000 64.41686  ? 294  ILE   A N   1 
ATOM   1860 C CA  . ILE   A 1 318 ? -37.33400 15.74700  -10.78200 1.000 71.14150  ? 294  ILE   A CA  1 
ATOM   1861 C C   . ILE   A 1 318 ? -36.87200 14.57100  -11.63700 1.000 79.84946  ? 294  ILE   A C   1 
ATOM   1862 O O   . ILE   A 1 318 ? -35.92300 14.70400  -12.41700 1.000 84.19264  ? 294  ILE   A O   1 
ATOM   1863 C CB  . ILE   A 1 318 ? -36.63300 15.77900  -9.41000  1.000 61.08372  ? 294  ILE   A CB  1 
ATOM   1864 C CG1 . ILE   A 1 318 ? -35.27500 16.46400  -9.53100  1.000 51.45396  ? 294  ILE   A CG1 1 
ATOM   1865 C CG2 . ILE   A 1 318 ? -36.45500 14.38700  -8.82700  1.000 64.38478  ? 294  ILE   A CG2 1 
ATOM   1866 C CD1 . ILE   A 1 318 ? -34.68800 16.86900  -8.20800  1.000 43.87864  ? 294  ILE   A CD1 1 
ATOM   1867 N N   . VAL   A 1 319 ? -37.54400 13.41700  -11.54200 1.000 77.45355  ? 295  VAL   A N   1 
ATOM   1868 C CA  . VAL   A 1 319 ? -37.07100 12.24800  -12.28200 1.000 81.32691  ? 295  VAL   A CA  1 
ATOM   1869 C C   . VAL   A 1 319 ? -37.31000 12.43400  -13.77500 1.000 78.66479  ? 295  VAL   A C   1 
ATOM   1870 O O   . VAL   A 1 319 ? -36.50600 11.99900  -14.60900 1.000 77.01557  ? 295  VAL   A O   1 
ATOM   1871 C CB  . VAL   A 1 319 ? -37.72900 10.95500  -11.75400 1.000 83.97113  ? 295  VAL   A CB  1 
ATOM   1872 C CG1 . VAL   A 1 319 ? -37.49800 10.81500  -10.25600 1.000 75.92061  ? 295  VAL   A CG1 1 
ATOM   1873 C CG2 . VAL   A 1 319 ? -39.21700 10.89500  -12.09500 1.000 78.93199  ? 295  VAL   A CG2 1 
ATOM   1874 N N   . HIS   A 1 320 ? -38.40700 13.09900  -14.13300 1.000 78.62450  ? 296  HIS   A N   1 
ATOM   1875 C CA  . HIS   A 1 320 ? -38.68500 13.37700  -15.53500 1.000 82.69513  ? 296  HIS   A CA  1 
ATOM   1876 C C   . HIS   A 1 320 ? -37.72000 14.41600  -16.09100 1.000 87.32783  ? 296  HIS   A C   1 
ATOM   1877 O O   . HIS   A 1 320 ? -37.15600 14.23700  -17.17700 1.000 92.82909  ? 296  HIS   A O   1 
ATOM   1878 C CB  . HIS   A 1 320 ? -40.13000 13.84600  -15.68300 1.000 81.54279  ? 296  HIS   A CB  1 
ATOM   1879 C CG  . HIS   A 1 320 ? -40.36600 14.71400  -16.87700 1.000 91.58120  ? 296  HIS   A CG  1 
ATOM   1880 N ND1 . HIS   A 1 320 ? -39.97600 14.35500  -18.14800 1.000 97.91880  ? 296  HIS   A ND1 1 
ATOM   1881 C CD2 . HIS   A 1 320 ? -40.96000 15.92400  -16.99300 1.000 94.66734  ? 296  HIS   A CD2 1 
ATOM   1882 C CE1 . HIS   A 1 320 ? -40.31200 15.31100  -18.99500 1.000 96.51694  ? 296  HIS   A CE1 1 
ATOM   1883 N NE2 . HIS   A 1 320 ? -40.91400 16.27300  -18.32100 1.000 97.81658  ? 296  HIS   A NE2 1 
ATOM   1884 N N   . VAL   A 1 321 ? -37.52200 15.51300  -15.35600 1.000 83.63517  ? 297  VAL   A N   1 
ATOM   1885 C CA  . VAL   A 1 321 ? -36.69900 16.61100  -15.85400 1.000 88.19530  ? 297  VAL   A CA  1 
ATOM   1886 C C   . VAL   A 1 321 ? -35.27500 16.13800  -16.11900 1.000 87.75046  ? 297  VAL   A C   1 
ATOM   1887 O O   . VAL   A 1 321 ? -34.68000 16.46400  -17.15400 1.000 86.89564  ? 297  VAL   A O   1 
ATOM   1888 C CB  . VAL   A 1 321 ? -36.73600 17.78900  -14.86200 1.000 76.05173  ? 297  VAL   A CB  1 
ATOM   1889 C CG1 . VAL   A 1 321 ? -35.63300 18.79500  -15.17000 1.000 62.50593  ? 297  VAL   A CG1 1 
ATOM   1890 C CG2 . VAL   A 1 321 ? -38.10200 18.45000  -14.88900 1.000 81.20622  ? 297  VAL   A CG2 1 
ATOM   1891 N N   . ILE   A 1 322 ? -34.71600 15.34000  -15.20600 1.000 85.67228  ? 298  ILE   A N   1 
ATOM   1892 C CA  . ILE   A 1 322 ? -33.31700 14.94400  -15.34000 1.000 88.07112  ? 298  ILE   A CA  1 
ATOM   1893 C C   . ILE   A 1 322 ? -33.15700 13.89500  -16.43700 1.000 95.03833  ? 298  ILE   A C   1 
ATOM   1894 O O   . ILE   A 1 322 ? -32.32400 14.04200  -17.33900 1.000 103.25179 ? 298  ILE   A O   1 
ATOM   1895 C CB  . ILE   A 1 322 ? -32.75300 14.46700  -13.98500 1.000 86.19833  ? 298  ILE   A CB  1 
ATOM   1896 C CG1 . ILE   A 1 322 ? -33.45200 13.19600  -13.48100 1.000 89.27525  ? 298  ILE   A CG1 1 
ATOM   1897 C CG2 . ILE   A 1 322 ? -32.84900 15.59000  -12.95500 1.000 83.65752  ? 298  ILE   A CG2 1 
ATOM   1898 C CD1 . ILE   A 1 322 ? -33.25600 12.90800  -12.00300 1.000 85.98317  ? 298  ILE   A CD1 1 
ATOM   1899 N N   . GLN   A 1 323 ? -33.96800 12.83900  -16.40000 1.000 94.67341  ? 299  GLN   A N   1 
ATOM   1900 C CA  . GLN   A 1 323 ? -33.81600 11.74500  -17.34900 1.000 95.40378  ? 299  GLN   A CA  1 
ATOM   1901 C C   . GLN   A 1 323 ? -34.54900 12.05900  -18.64400 1.000 87.18559  ? 299  GLN   A C   1 
ATOM   1902 O O   . GLN   A 1 323 ? -34.02300 12.77100  -19.50400 1.000 92.22017  ? 299  GLN   A O   1 
ATOM   1903 C CB  . GLN   A 1 323 ? -34.33000 10.43600  -16.74600 1.000 101.39671 ? 299  GLN   A CB  1 
ATOM   1904 N N   . ASP   A 1 324 ? -35.76200 11.53500  -18.78800 1.000 83.88445  ? 300  ASP   A N   1 
ATOM   1905 C CA  . ASP   A 1 324 ? -36.56000 11.76700  -19.98000 1.000 94.33068  ? 300  ASP   A CA  1 
ATOM   1906 C C   . ASP   A 1 324 ? -38.03200 11.63800  -19.61300 1.000 94.10417  ? 300  ASP   A C   1 
ATOM   1907 O O   . ASP   A 1 324 ? -38.38500 11.34900  -18.46600 1.000 95.26967  ? 300  ASP   A O   1 
ATOM   1908 C CB  . ASP   A 1 324 ? -36.17100 10.79900  -21.10200 1.000 99.17294  ? 300  ASP   A CB  1 
ATOM   1909 N N   . ASN   A 1 325 ? -38.89500 11.85700  -20.60500 1.000 96.94386  ? 301  ASN   A N   1 
ATOM   1910 C CA  . ASN   A 1 325 ? -40.33700 11.77900  -20.40400 1.000 92.71492  ? 301  ASN   A CA  1 
ATOM   1911 C C   . ASN   A 1 325 ? -40.79800 10.34200  -20.19200 1.000 96.48403  ? 301  ASN   A C   1 
ATOM   1912 O O   . ASN   A 1 325 ? -41.51100 9.78200   -21.03100 1.000 96.43037  ? 301  ASN   A O   1 
ATOM   1913 C CB  . ASN   A 1 325 ? -41.08000 12.39600  -21.59200 1.000 93.48107  ? 301  ASN   A CB  1 
ATOM   1914 C CG  . ASN   A 1 325 ? -40.70900 13.84800  -21.82500 1.000 101.45834 ? 301  ASN   A CG  1 
ATOM   1915 O OD1 . ASN   A 1 325 ? -39.54200 14.17800  -22.04000 1.000 98.81804  ? 301  ASN   A OD1 1 
ATOM   1916 N ND2 . ASN   A 1 325 ? -41.70600 14.72500  -21.78300 1.000 104.46601 ? 301  ASN   A ND2 1 
ATOM   1917 N N   . LEU   A 1 326 ? -40.39000 9.73600   -19.07800 1.000 100.47749 ? 302  LEU   A N   1 
ATOM   1918 C CA  . LEU   A 1 326 ? -40.91800 8.44200   -18.67000 1.000 98.70828  ? 302  LEU   A CA  1 
ATOM   1919 C C   . LEU   A 1 326 ? -42.16500 8.58300   -17.80200 1.000 101.11162 ? 302  LEU   A C   1 
ATOM   1920 O O   . LEU   A 1 326 ? -42.82700 7.58000   -17.51400 1.000 100.73820 ? 302  LEU   A O   1 
ATOM   1921 C CB  . LEU   A 1 326 ? -39.82400 7.64500   -17.93500 1.000 91.75885  ? 302  LEU   A CB  1 
ATOM   1922 C CG  . LEU   A 1 326 ? -40.11500 6.25400   -17.35900 1.000 90.33815  ? 302  LEU   A CG  1 
ATOM   1923 C CD1 . LEU   A 1 326 ? -40.04800 5.19500   -18.45400 1.000 86.80513  ? 302  LEU   A CD1 1 
ATOM   1924 C CD2 . LEU   A 1 326 ? -39.15200 5.92100   -16.22600 1.000 73.78592  ? 302  LEU   A CD2 1 
ATOM   1925 N N   . ILE   A 1 327 ? -42.51200 9.80600   -17.40600 1.000 96.86565  ? 303  ILE   A N   1 
ATOM   1926 C CA  . ILE   A 1 327 ? -43.71500 10.07800  -16.62800 1.000 85.68955  ? 303  ILE   A CA  1 
ATOM   1927 C C   . ILE   A 1 327 ? -44.83800 10.46300  -17.58200 1.000 83.23440  ? 303  ILE   A C   1 
ATOM   1928 O O   . ILE   A 1 327 ? -44.66200 11.31600  -18.46200 1.000 79.10882  ? 303  ILE   A O   1 
ATOM   1929 C CB  . ILE   A 1 327 ? -43.45200 11.15600  -15.55200 1.000 84.54384  ? 303  ILE   A CB  1 
ATOM   1930 C CG1 . ILE   A 1 327 ? -43.31300 12.57300  -16.13100 1.000 85.47269  ? 303  ILE   A CG1 1 
ATOM   1931 C CG2 . ILE   A 1 327 ? -42.19900 10.80800  -14.76300 1.000 86.08828  ? 303  ILE   A CG2 1 
ATOM   1932 C CD1 . ILE   A 1 327 ? -44.57300 13.42100  -16.13300 1.000 81.90298  ? 303  ILE   A CD1 1 
ATOM   1933 N N   . ARG   A 1 328 ? -45.97400 9.78700   -17.45200 1.000 85.73936  ? 304  ARG   A N   1 
ATOM   1934 C CA  . ARG   A 1 328 ? -47.15000 10.16400  -18.21400 1.000 87.46990  ? 304  ARG   A CA  1 
ATOM   1935 C C   . ARG   A 1 328 ? -47.70700 11.47700  -17.66900 1.000 84.20240  ? 304  ARG   A C   1 
ATOM   1936 O O   . ARG   A 1 328 ? -47.30100 11.96500  -16.61200 1.000 88.65486  ? 304  ARG   A O   1 
ATOM   1937 C CB  . ARG   A 1 328 ? -48.20200 9.05400   -18.16000 1.000 84.07366  ? 304  ARG   A CB  1 
ATOM   1938 C CG  . ARG   A 1 328 ? -47.63900 7.67200   -18.45100 1.000 89.62843  ? 304  ARG   A CG  1 
ATOM   1939 C CD  . ARG   A 1 328 ? -48.42100 6.57000   -17.74700 1.000 93.18561  ? 304  ARG   A CD  1 
ATOM   1940 N NE  . ARG   A 1 328 ? -49.83300 6.54600   -18.10800 1.000 102.38810 ? 304  ARG   A NE  1 
ATOM   1941 C CZ  . ARG   A 1 328 ? -50.71500 5.69000   -17.60900 1.000 102.47502 ? 304  ARG   A CZ  1 
ATOM   1942 N NH1 . ARG   A 1 328 ? -50.36200 4.76800   -16.72800 1.000 95.59493  ? 304  ARG   A NH1 1 
ATOM   1943 N NH2 . ARG   A 1 328 ? -51.98500 5.76400   -18.00000 1.000 101.12654 ? 304  ARG   A NH2 1 
ATOM   1944 N N   . LYS   A 1 329 ? -48.63900 12.06700  -18.40600 1.000 80.91670  ? 305  LYS   A N   1 
ATOM   1945 C CA  . LYS   A 1 329 ? -49.20600 13.32600  -17.94600 1.000 76.42380  ? 305  LYS   A CA  1 
ATOM   1946 C C   . LYS   A 1 329 ? -50.44700 13.12200  -17.09200 1.000 74.57154  ? 305  LYS   A C   1 
ATOM   1947 O O   . LYS   A 1 329 ? -50.75300 13.97000  -16.24700 1.000 79.48804  ? 305  LYS   A O   1 
ATOM   1948 C CB  . LYS   A 1 329 ? -49.50200 14.23200  -19.14100 1.000 84.69900  ? 305  LYS   A CB  1 
ATOM   1949 C CG  . LYS   A 1 329 ? -48.22400 14.71400  -19.81800 1.000 90.60162  ? 305  LYS   A CG  1 
ATOM   1950 C CD  . LYS   A 1 329 ? -48.49400 15.56900  -21.04000 1.000 97.11721  ? 305  LYS   A CD  1 
ATOM   1951 C CE  . LYS   A 1 329 ? -47.18600 16.02200  -21.67900 1.000 100.58797 ? 305  LYS   A CE  1 
ATOM   1952 N NZ  . LYS   A 1 329 ? -46.26600 14.87600  -21.95500 1.000 93.37744  ? 305  LYS   A NZ  1 
ATOM   1953 N N   . GLU   A 1 330 ? -51.15300 12.00400  -17.27100 1.000 80.22291  ? 306  GLU   A N   1 
ATOM   1954 C CA  . GLU   A 1 330 ? -52.26800 11.69500  -16.38400 1.000 76.50842  ? 306  GLU   A CA  1 
ATOM   1955 C C   . GLU   A 1 330 ? -51.78100 11.26900  -15.00500 1.000 74.34524  ? 306  GLU   A C   1 
ATOM   1956 O O   . GLU   A 1 330 ? -52.50700 11.43300  -14.01800 1.000 75.71729  ? 306  GLU   A O   1 
ATOM   1957 C CB  . GLU   A 1 330 ? -53.15200 10.61100  -17.00100 1.000 79.52918  ? 306  GLU   A CB  1 
ATOM   1958 C CG  . GLU   A 1 330 ? -54.52400 10.46000  -16.34300 1.000 93.18598  ? 306  GLU   A CG  1 
ATOM   1959 C CD  . GLU   A 1 330 ? -55.43000 11.66500  -16.55200 1.000 103.60385 ? 306  GLU   A CD  1 
ATOM   1960 O OE1 . GLU   A 1 330 ? -55.71400 12.00600  -17.72000 1.000 104.17719 ? 306  GLU   A OE1 1 
ATOM   1961 O OE2 . GLU   A 1 330 ? -55.87900 12.25400  -15.54400 1.000 105.49681 ? 306  GLU   A OE2 1 
ATOM   1962 N N   . VAL   A 1 331 ? -50.56800 10.72200  -14.91100 1.000 71.77864  ? 307  VAL   A N   1 
ATOM   1963 C CA  . VAL   A 1 331 ? -50.01600 10.43100  -13.59100 1.000 66.10566  ? 307  VAL   A CA  1 
ATOM   1964 C C   . VAL   A 1 331 ? -49.44300 11.69700  -12.96700 1.000 60.64963  ? 307  VAL   A C   1 
ATOM   1965 O O   . VAL   A 1 331 ? -49.53000 11.88600  -11.74900 1.000 60.93520  ? 307  VAL   A O   1 
ATOM   1966 C CB  . VAL   A 1 331 ? -48.96600 9.30600   -13.66600 1.000 66.21413  ? 307  VAL   A CB  1 
ATOM   1967 C CG1 . VAL   A 1 331 ? -47.92100 9.61300   -14.70600 1.000 76.36565  ? 307  VAL   A CG1 1 
ATOM   1968 C CG2 . VAL   A 1 331 ? -48.30500 9.09200   -12.31300 1.000 59.07712  ? 307  VAL   A CG2 1 
ATOM   1969 N N   . TYR   A 1 332 ? -48.87500 12.59000  -13.77700 1.000 68.98350  ? 308  TYR   A N   1 
ATOM   1970 C CA  . TYR   A 1 332 ? -48.40200 13.86100  -13.24100 1.000 65.69580  ? 308  TYR   A CA  1 
ATOM   1971 C C   . TYR   A 1 332 ? -49.57000 14.72300  -12.78300 1.000 60.38479  ? 308  TYR   A C   1 
ATOM   1972 O O   . TYR   A 1 332 ? -49.46600 15.43600  -11.77800 1.000 65.36798  ? 308  TYR   A O   1 
ATOM   1973 C CB  . TYR   A 1 332 ? -47.54800 14.58600  -14.28700 1.000 67.55349  ? 308  TYR   A CB  1 
ATOM   1974 C CG  . TYR   A 1 332 ? -47.31800 16.07400  -14.05400 1.000 68.83411  ? 308  TYR   A CG  1 
ATOM   1975 C CD1 . TYR   A 1 332 ? -48.29200 17.02300  -14.37200 1.000 60.78961  ? 308  TYR   A CD1 1 
ATOM   1976 C CD2 . TYR   A 1 332 ? -46.12300 16.52700  -13.50500 1.000 66.51411  ? 308  TYR   A CD2 1 
ATOM   1977 C CE1 . TYR   A 1 332 ? -48.07700 18.37500  -14.15700 1.000 54.37406  ? 308  TYR   A CE1 1 
ATOM   1978 C CE2 . TYR   A 1 332 ? -45.90500 17.87300  -13.28300 1.000 64.21515  ? 308  TYR   A CE2 1 
ATOM   1979 C CZ  . TYR   A 1 332 ? -46.87900 18.79200  -13.61200 1.000 62.90104  ? 308  TYR   A CZ  1 
ATOM   1980 O OH  . TYR   A 1 332 ? -46.64900 20.13000  -13.39100 1.000 61.66057  ? 308  TYR   A OH  1 
ATOM   1981 N N   . ILE   A 1 333 ? -50.69300 14.66300  -13.49900 1.000 61.27873  ? 309  ILE   A N   1 
ATOM   1982 C CA  . ILE   A 1 333 ? -51.82400 15.50200  -13.13000 1.000 64.55904  ? 309  ILE   A CA  1 
ATOM   1983 C C   . ILE   A 1 333 ? -52.55600 14.93500  -11.91500 1.000 61.13511  ? 309  ILE   A C   1 
ATOM   1984 O O   . ILE   A 1 333 ? -53.20300 15.68600  -11.17900 1.000 64.68820  ? 309  ILE   A O   1 
ATOM   1985 C CB  . ILE   A 1 333 ? -52.76500 15.68500  -14.33300 1.000 65.82772  ? 309  ILE   A CB  1 
ATOM   1986 C CG1 . ILE   A 1 333 ? -53.57500 16.97400  -14.18500 1.000 71.20402  ? 309  ILE   A CG1 1 
ATOM   1987 C CG2 . ILE   A 1 333 ? -53.69400 14.49500  -14.47300 1.000 72.83227  ? 309  ILE   A CG2 1 
ATOM   1988 C CD1 . ILE   A 1 333 ? -54.17400 17.45800  -15.48900 1.000 65.41636  ? 309  ILE   A CD1 1 
ATOM   1989 N N   . LEU   A 1 334 ? -52.46200 13.62400  -11.67000 1.000 55.69895  ? 310  LEU   A N   1 
ATOM   1990 C CA  . LEU   A 1 334 ? -53.08100 13.05200  -10.47800 1.000 52.10717  ? 310  LEU   A CA  1 
ATOM   1991 C C   . LEU   A 1 334 ? -52.23000 13.30200  -9.24100  1.000 55.38581  ? 310  LEU   A C   1 
ATOM   1992 O O   . LEU   A 1 334 ? -52.75000 13.69700  -8.19100  1.000 54.34318  ? 310  LEU   A O   1 
ATOM   1993 C CB  . LEU   A 1 334 ? -53.31900 11.55300  -10.65800 1.000 53.01935  ? 310  LEU   A CB  1 
ATOM   1994 C CG  . LEU   A 1 334 ? -54.26300 10.94600  -9.61400  1.000 56.25185  ? 310  LEU   A CG  1 
ATOM   1995 C CD1 . LEU   A 1 334 ? -55.72900 11.08900  -10.02500 1.000 48.87454  ? 310  LEU   A CD1 1 
ATOM   1996 C CD2 . LEU   A 1 334 ? -53.91100 9.48900   -9.34500  1.000 53.91081  ? 310  LEU   A CD2 1 
ATOM   1997 N N   . LEU   A 1 335 ? -50.92000 13.06100  -9.34700  1.000 59.00941  ? 311  LEU   A N   1 
ATOM   1998 C CA  . LEU   A 1 335 ? -50.01900 13.35600  -8.23900  1.000 57.63692  ? 311  LEU   A CA  1 
ATOM   1999 C C   . LEU   A 1 335 ? -50.07300 14.82700  -7.86000  1.000 55.29571  ? 311  LEU   A C   1 
ATOM   2000 O O   . LEU   A 1 335 ? -49.84900 15.17800  -6.69500  1.000 52.95613  ? 311  LEU   A O   1 
ATOM   2001 C CB  . LEU   A 1 335 ? -48.59200 12.95100  -8.60300  1.000 53.68936  ? 311  LEU   A CB  1 
ATOM   2002 C CG  . LEU   A 1 335 ? -48.35100 11.45800  -8.81600  1.000 51.56664  ? 311  LEU   A CG  1 
ATOM   2003 C CD1 . LEU   A 1 335 ? -46.87800 11.20700  -9.02200  1.000 53.51439  ? 311  LEU   A CD1 1 
ATOM   2004 C CD2 . LEU   A 1 335 ? -48.86600 10.65000  -7.63500  1.000 51.83631  ? 311  LEU   A CD2 1 
ATOM   2005 N N   . ASN   A 1 336 ? -50.37500 15.69900  -8.82600  1.000 50.69668  ? 312  ASN   A N   1 
ATOM   2006 C CA  . ASN   A 1 336 ? -50.54600 17.10900  -8.50600  1.000 47.61160  ? 312  ASN   A CA  1 
ATOM   2007 C C   . ASN   A 1 336 ? -51.82700 17.33800  -7.71300  1.000 51.41513  ? 312  ASN   A C   1 
ATOM   2008 O O   . ASN   A 1 336 ? -51.83600 18.11600  -6.75400  1.000 53.32038  ? 312  ASN   A O   1 
ATOM   2009 C CB  . ASN   A 1 336 ? -50.54700 17.93900  -9.78600  1.000 46.90251  ? 312  ASN   A CB  1 
ATOM   2010 C CG  . ASN   A 1 336 ? -50.49200 19.43000  -9.51200  1.000 47.99082  ? 312  ASN   A CG  1 
ATOM   2011 O OD1 . ASN   A 1 336 ? -50.29300 19.85900  -8.37600  1.000 40.26196  ? 312  ASN   A OD1 1 
ATOM   2012 N ND2 . ASN   A 1 336 ? -50.67500 20.22800  -10.55500 1.000 42.31212  ? 312  ASN   A ND2 1 
ATOM   2013 N N   . TRP   A 1 337 ? -52.91800 16.66300  -8.08600  1.000 50.54915  ? 313  TRP   A N   1 
ATOM   2014 C CA  . TRP   A 1 337 ? -54.17300 16.84900  -7.36800  1.000 47.11591  ? 313  TRP   A CA  1 
ATOM   2015 C C   . TRP   A 1 337 ? -54.13600 16.28000  -5.95300  1.000 55.55624  ? 313  TRP   A C   1 
ATOM   2016 O O   . TRP   A 1 337 ? -55.01200 16.61300  -5.14700  1.000 49.33576  ? 313  TRP   A O   1 
ATOM   2017 C CB  . TRP   A 1 337 ? -55.33800 16.23000  -8.14200  1.000 42.68175  ? 313  TRP   A CB  1 
ATOM   2018 C CG  . TRP   A 1 337 ? -56.01100 17.20100  -9.06800  1.000 52.95693  ? 313  TRP   A CG  1 
ATOM   2019 C CD1 . TRP   A 1 337 ? -55.60200 17.56200  -10.32000 1.000 61.22573  ? 313  TRP   A CD1 1 
ATOM   2020 C CD2 . TRP   A 1 337 ? -57.20000 17.95700  -8.80300  1.000 48.77506  ? 313  TRP   A CD2 1 
ATOM   2021 N NE1 . TRP   A 1 337 ? -56.47100 18.48300  -10.85600 1.000 59.55577  ? 313  TRP   A NE1 1 
ATOM   2022 C CE2 . TRP   A 1 337 ? -57.45800 18.74500  -9.94300  1.000 54.60353  ? 313  TRP   A CE2 1 
ATOM   2023 C CE3 . TRP   A 1 337 ? -58.07400 18.04000  -7.71500  1.000 53.78926  ? 313  TRP   A CE3 1 
ATOM   2024 C CZ2 . TRP   A 1 337 ? -58.55300 19.60400  -10.02400 1.000 52.58836  ? 313  TRP   A CZ2 1 
ATOM   2025 C CZ3 . TRP   A 1 337 ? -59.16000 18.89400  -7.79800  1.000 53.97720  ? 313  TRP   A CZ3 1 
ATOM   2026 C CH2 . TRP   A 1 337 ? -59.39000 19.66400  -8.94500  1.000 56.70311  ? 313  TRP   A CH2 1 
ATOM   2027 N N   . ILE   A 1 338 ? -53.15600 15.43200  -5.62900  1.000 54.14529  ? 314  ILE   A N   1 
ATOM   2028 C CA  . ILE   A 1 338 ? -53.00300 14.99300  -4.24500  1.000 49.24983  ? 314  ILE   A CA  1 
ATOM   2029 C C   . ILE   A 1 338 ? -52.58700 16.16600  -3.36800  1.000 51.71720  ? 314  ILE   A C   1 
ATOM   2030 O O   . ILE   A 1 338 ? -53.13400 16.37600  -2.27900  1.000 57.31364  ? 314  ILE   A O   1 
ATOM   2031 C CB  . ILE   A 1 338 ? -52.00200 13.82900  -4.14600  1.000 51.66101  ? 314  ILE   A CB  1 
ATOM   2032 C CG1 . ILE   A 1 338 ? -52.57900 12.57000  -4.79600  1.000 54.11692  ? 314  ILE   A CG1 1 
ATOM   2033 C CG2 . ILE   A 1 338 ? -51.64500 13.55500  -2.69500  1.000 46.51742  ? 314  ILE   A CG2 1 
ATOM   2034 C CD1 . ILE   A 1 338 ? -51.66300 11.37100  -4.71000  1.000 45.40691  ? 314  ILE   A CD1 1 
ATOM   2035 N N   . GLY   A 1 339 ? -51.61700 16.95600  -3.83200  1.000 48.08470  ? 315  GLY   A N   1 
ATOM   2036 C CA  . GLY   A 1 339 ? -51.29600 18.18600  -3.13300  1.000 50.07159  ? 315  GLY   A CA  1 
ATOM   2037 C C   . GLY   A 1 339 ? -52.40600 19.21400  -3.18300  1.000 49.22830  ? 315  GLY   A C   1 
ATOM   2038 O O   . GLY   A 1 339 ? -52.40600 20.15300  -2.38000  1.000 50.03050  ? 315  GLY   A O   1 
ATOM   2039 N N   . TYR   A 1 340 ? -53.35300 19.05200  -4.10700  1.000 46.79277  ? 316  TYR   A N   1 
ATOM   2040 C CA  . TYR   A 1 340 ? -54.46200 19.99200  -4.21500  1.000 48.88160  ? 316  TYR   A CA  1 
ATOM   2041 C C   . TYR   A 1 340 ? -55.46000 19.78500  -3.08000  1.000 48.07424  ? 316  TYR   A C   1 
ATOM   2042 O O   . TYR   A 1 340 ? -55.85900 20.74200  -2.40400  1.000 43.24481  ? 316  TYR   A O   1 
ATOM   2043 C CB  . TYR   A 1 340 ? -55.14000 19.83300  -5.57900  1.000 49.04478  ? 316  TYR   A CB  1 
ATOM   2044 C CG  . TYR   A 1 340 ? -54.63500 20.78500  -6.64600  1.000 54.64700  ? 316  TYR   A CG  1 
ATOM   2045 C CD1 . TYR   A 1 340 ? -53.28000 20.87800  -6.93900  1.000 54.60602  ? 316  TYR   A CD1 1 
ATOM   2046 C CD2 . TYR   A 1 340 ? -55.51300 21.56300  -7.38700  1.000 60.74938  ? 316  TYR   A CD2 1 
ATOM   2047 C CE1 . TYR   A 1 340 ? -52.81400 21.74000  -7.91900  1.000 47.75083  ? 316  TYR   A CE1 1 
ATOM   2048 C CE2 . TYR   A 1 340 ? -55.05500 22.42600  -8.37200  1.000 46.93710  ? 316  TYR   A CE2 1 
ATOM   2049 C CZ  . TYR   A 1 340 ? -53.70600 22.50900  -8.63000  1.000 40.55115  ? 316  TYR   A CZ  1 
ATOM   2050 O OH  . TYR   A 1 340 ? -53.24500 23.36300  -9.60200  1.000 44.96894  ? 316  TYR   A OH  1 
ATOM   2051 N N   . VAL   A 1 341 ? -55.87100 18.53600  -2.84600  1.000 41.85969  ? 317  VAL   A N   1 
ATOM   2052 C CA  . VAL   A 1 341 ? -56.83100 18.25900  -1.78400  1.000 37.51302  ? 317  VAL   A CA  1 
ATOM   2053 C C   . VAL   A 1 341 ? -56.23600 18.43500  -0.40000  1.000 43.68647  ? 317  VAL   A C   1 
ATOM   2054 O O   . VAL   A 1 341 ? -56.98500 18.48200  0.58100   1.000 44.90161  ? 317  VAL   A O   1 
ATOM   2055 C CB  . VAL   A 1 341 ? -57.39800 16.83300  -1.91100  1.000 35.00893  ? 317  VAL   A CB  1 
ATOM   2056 C CG1 . VAL   A 1 341 ? -58.24300 16.71300  -3.16600  1.000 32.14255  ? 317  VAL   A CG1 1 
ATOM   2057 C CG2 . VAL   A 1 341 ? -56.27800 15.80700  -1.89400  1.000 35.17219  ? 317  VAL   A CG2 1 
ATOM   2058 N N   . ASN   A 1 342 ? -54.90900 18.52600  -0.30000  1.000 46.51753  ? 318  ASN   A N   1 
ATOM   2059 C CA  . ASN   A 1 342 ? -54.27300 18.83000  0.97500   1.000 39.25067  ? 318  ASN   A CA  1 
ATOM   2060 C C   . ASN   A 1 342 ? -54.81200 20.11500  1.58700   1.000 43.51885  ? 318  ASN   A C   1 
ATOM   2061 O O   . ASN   A 1 342 ? -54.88300 20.23400  2.81700   1.000 48.62053  ? 318  ASN   A O   1 
ATOM   2062 C CB  . ASN   A 1 342 ? -52.76300 18.95200  0.78100   1.000 44.11811  ? 318  ASN   A CB  1 
ATOM   2063 C CG  . ASN   A 1 342 ? -51.99900 18.91900  2.08500   1.000 43.06465  ? 318  ASN   A CG  1 
ATOM   2064 O OD1 . ASN   A 1 342 ? -50.78900 19.11700  2.10300   1.000 48.49459  ? 318  ASN   A OD1 1 
ATOM   2065 N ND2 . ASN   A 1 342 ? -52.69200 18.63600  3.17700   1.000 50.39390  ? 318  ASN   A ND2 1 
ATOM   2066 N N   . SER   A 1 343 ? -55.19400 21.08400  0.75100   1.000 42.61859  ? 319  SER   A N   1 
ATOM   2067 C CA  . SER   A 1 343 ? -55.65900 22.36800  1.26500   1.000 46.83696  ? 319  SER   A CA  1 
ATOM   2068 C C   . SER   A 1 343 ? -56.90100 22.21700  2.13400   1.000 44.97501  ? 319  SER   A C   1 
ATOM   2069 O O   . SER   A 1 343 ? -57.13300 23.04000  3.02800   1.000 47.93150  ? 319  SER   A O   1 
ATOM   2070 C CB  . SER   A 1 343 ? -55.93300 23.33100  0.10900   1.000 42.51466  ? 319  SER   A CB  1 
ATOM   2071 O OG  . SER   A 1 343 ? -54.90700 23.25800  -0.86600  1.000 48.88278  ? 319  SER   A OG  1 
ATOM   2072 N N   . GLY   A 1 344 ? -57.70000 21.18400  1.90100   1.000 36.86576  ? 320  GLY   A N   1 
ATOM   2073 C CA  . GLY   A 1 344 ? -58.86600 20.92800  2.71400   1.000 39.08592  ? 320  GLY   A CA  1 
ATOM   2074 C C   . GLY   A 1 344 ? -58.63800 20.01700  3.89900   1.000 37.15936  ? 320  GLY   A C   1 
ATOM   2075 O O   . GLY   A 1 344 ? -59.60600 19.65100  4.57200   1.000 41.64023  ? 320  GLY   A O   1 
ATOM   2076 N N   . PHE   A 1 345 ? -57.39200 19.64500  4.18800   1.000 37.75417  ? 321  PHE   A N   1 
ATOM   2077 C CA  . PHE   A 1 345 ? -57.10100 18.67300  5.23700   1.000 45.05092  ? 321  PHE   A CA  1 
ATOM   2078 C C   . PHE   A 1 345 ? -56.72200 19.29600  6.57300   1.000 46.56891  ? 321  PHE   A C   1 
ATOM   2079 O O   . PHE   A 1 345 ? -57.12400 18.77400  7.61900   1.000 40.23930  ? 321  PHE   A O   1 
ATOM   2080 C CB  . PHE   A 1 345 ? -55.98200 17.72700  4.79500   1.000 36.52732  ? 321  PHE   A CB  1 
ATOM   2081 C CG  . PHE   A 1 345 ? -56.39000 16.77400  3.72200   1.000 40.29947  ? 321  PHE   A CG  1 
ATOM   2082 C CD1 . PHE   A 1 345 ? -57.71900 16.66500  3.34400   1.000 45.79448  ? 321  PHE   A CD1 1 
ATOM   2083 C CD2 . PHE   A 1 345 ? -55.45100 15.97300  3.10000   1.000 43.81009  ? 321  PHE   A CD2 1 
ATOM   2084 C CE1 . PHE   A 1 345 ? -58.10300 15.78200  2.35200   1.000 46.87656  ? 321  PHE   A CE1 1 
ATOM   2085 C CE2 . PHE   A 1 345 ? -55.82700 15.08700  2.11100   1.000 46.98741  ? 321  PHE   A CE2 1 
ATOM   2086 C CZ  . PHE   A 1 345 ? -57.15700 14.99100  1.73600   1.000 44.81976  ? 321  PHE   A CZ  1 
ATOM   2087 N N   . ASN   A 1 346 ? -55.93900 20.37800  6.57100   1.000 47.80578  ? 322  ASN   A N   1 
ATOM   2088 C CA  . ASN   A 1 346 ? -55.55300 21.01800  7.82900   1.000 47.56394  ? 322  ASN   A CA  1 
ATOM   2089 C C   . ASN   A 1 346 ? -56.73000 21.24100  8.77500   1.000 44.57176  ? 322  ASN   A C   1 
ATOM   2090 O O   . ASN   A 1 346 ? -56.65000 20.78700  9.92500   1.000 42.40648  ? 322  ASN   A O   1 
ATOM   2091 C CB  . ASN   A 1 346 ? -54.82000 22.34400  7.56400   1.000 45.18486  ? 322  ASN   A CB  1 
ATOM   2092 C CG  . ASN   A 1 346 ? -53.36900 22.15100  7.13600   1.000 41.43647  ? 322  ASN   A CG  1 
ATOM   2093 O OD1 . ASN   A 1 346 ? -52.84600 21.03600  7.12800   1.000 39.87494  ? 322  ASN   A OD1 1 
ATOM   2094 N ND2 . ASN   A 1 346 ? -52.70000 23.25700  6.82600   1.000 41.87123  ? 322  ASN   A ND2 1 
ATOM   2095 N N   . PRO   A 1 347 ? -57.84400 21.87000  8.36800   1.000 43.55224  ? 323  PRO   A N   1 
ATOM   2096 C CA  . PRO   A 1 347 ? -58.90500 22.17100  9.34700   1.000 39.51956  ? 323  PRO   A CA  1 
ATOM   2097 C C   . PRO   A 1 347 ? -59.38800 20.98100  10.16200  1.000 41.77132  ? 323  PRO   A C   1 
ATOM   2098 O O   . PRO   A 1 347 ? -59.82200 21.17500  11.30400  1.000 44.85079  ? 323  PRO   A O   1 
ATOM   2099 C CB  . PRO   A 1 347 ? -60.03000 22.74300  8.47400   1.000 34.28750  ? 323  PRO   A CB  1 
ATOM   2100 C CG  . PRO   A 1 347 ? -59.34000 23.29400  7.29200   1.000 42.43797  ? 323  PRO   A CG  1 
ATOM   2101 C CD  . PRO   A 1 347 ? -58.19600 22.37100  7.02600   1.000 42.47624  ? 323  PRO   A CD  1 
ATOM   2102 N N   . LEU   A 1 348 ? -59.32400 19.75800  9.63800   1.000 40.24593  ? 324  LEU   A N   1 
ATOM   2103 C CA  . LEU   A 1 348 ? -59.75200 18.62000  10.44200  1.000 42.17596  ? 324  LEU   A CA  1 
ATOM   2104 C C   . LEU   A 1 348 ? -58.62200 18.00100  11.25500  1.000 49.06182  ? 324  LEU   A C   1 
ATOM   2105 O O   . LEU   A 1 348 ? -58.89500 17.35300  12.27300  1.000 55.55550  ? 324  LEU   A O   1 
ATOM   2106 C CB  . LEU   A 1 348 ? -60.40600 17.54700  9.56700   1.000 42.40049  ? 324  LEU   A CB  1 
ATOM   2107 C CG  . LEU   A 1 348 ? -59.64300 17.02200  8.35700   1.000 53.94144  ? 324  LEU   A CG  1 
ATOM   2108 C CD1 . LEU   A 1 348 ? -58.87900 15.74800  8.69600   1.000 51.50824  ? 324  LEU   A CD1 1 
ATOM   2109 C CD2 . LEU   A 1 348 ? -60.61400 16.78700  7.21300   1.000 52.12081  ? 324  LEU   A CD2 1 
ATOM   2110 N N   . ILE   A 1 349 ? -57.36300 18.17700  10.84600  1.000 46.74223  ? 325  ILE   A N   1 
ATOM   2111 C CA  . ILE   A 1 349 ? -56.27300 17.84600  11.75700  1.000 46.31595  ? 325  ILE   A CA  1 
ATOM   2112 C C   . ILE   A 1 349 ? -56.37100 18.72600  12.99600  1.000 38.63991  ? 325  ILE   A C   1 
ATOM   2113 O O   . ILE   A 1 349 ? -55.97700 18.32100  14.09500  1.000 42.92667  ? 325  ILE   A O   1 
ATOM   2114 C CB  . ILE   A 1 349 ? -54.90900 17.99600  11.04800  1.000 49.87644  ? 325  ILE   A CB  1 
ATOM   2115 C CG1 . ILE   A 1 349 ? -54.75900 16.95500  9.93900   1.000 53.89844  ? 325  ILE   A CG1 1 
ATOM   2116 C CG2 . ILE   A 1 349 ? -53.75300 17.82700  12.03100  1.000 41.97812  ? 325  ILE   A CG2 1 
ATOM   2117 C CD1 . ILE   A 1 349 ? -53.49300 17.11700  9.11500   1.000 47.51341  ? 325  ILE   A CD1 1 
ATOM   2118 N N   . TYR   A 1 350 ? -56.93500 19.92600  12.84200  1.000 35.91185  ? 326  TYR   A N   1 
ATOM   2119 C CA  . TYR   A 1 350 ? -57.08500 20.87700  13.93500  1.000 40.17085  ? 326  TYR   A CA  1 
ATOM   2120 C C   . TYR   A 1 350 ? -58.09900 20.40900  14.96800  1.000 43.98234  ? 326  TYR   A C   1 
ATOM   2121 O O   . TYR   A 1 350 ? -58.03100 20.84100  16.12500  1.000 43.98687  ? 326  TYR   A O   1 
ATOM   2122 C CB  . TYR   A 1 350 ? -57.51800 22.22800  13.37200  1.000 37.81528  ? 326  TYR   A CB  1 
ATOM   2123 C CG  . TYR   A 1 350 ? -56.45000 22.97500  12.61100  1.000 39.10400  ? 326  TYR   A CG  1 
ATOM   2124 C CD1 . TYR   A 1 350 ? -55.36900 22.31000  12.05300  1.000 46.63486  ? 326  TYR   A CD1 1 
ATOM   2125 C CD2 . TYR   A 1 350 ? -56.59800 24.32100  12.32700  1.000 42.95552  ? 326  TYR   A CD2 1 
ATOM   2126 C CE1 . TYR   A 1 350 ? -54.42000 22.97800  11.31500  1.000 47.58344  ? 326  TYR   A CE1 1 
ATOM   2127 C CE2 . TYR   A 1 350 ? -55.65900 24.99300  11.57700  1.000 51.26424  ? 326  TYR   A CE2 1 
ATOM   2128 C CZ  . TYR   A 1 350 ? -54.56600 24.31700  11.07500  1.000 51.27188  ? 326  TYR   A CZ  1 
ATOM   2129 O OH  . TYR   A 1 350 ? -53.61900 24.97400  10.32300  1.000 50.31947  ? 326  TYR   A OH  1 
ATOM   2130 N N   . CYS   A 1 351 ? -59.04100 19.54600  14.58000  1.000 39.05730  ? 327  CYS   A N   1 
ATOM   2131 C CA  . CYS   A 1 351 ? -59.97900 18.99100  15.54800  1.000 40.07571  ? 327  CYS   A CA  1 
ATOM   2132 C C   . CYS   A 1 351 ? -59.28800 18.14400  16.60400  1.000 44.39465  ? 327  CYS   A C   1 
ATOM   2133 O O   . CYS   A 1 351 ? -59.91700 17.80200  17.61100  1.000 56.67994  ? 327  CYS   A O   1 
ATOM   2134 C CB  . CYS   A 1 351 ? -61.04700 18.15900  14.83900  1.000 43.26840  ? 327  CYS   A CB  1 
ATOM   2135 S SG  . CYS   A 1 351 ? -62.29900 19.14800  14.00700  1.000 50.09503  ? 327  CYS   A SG  1 
ATOM   2136 N N   . ARG   A 1 352 ? -58.01900 17.79200  16.39400  1.000 41.43772  ? 328  ARG   A N   1 
ATOM   2137 C CA  . ARG   A 1 352 ? -57.24400 17.14900  17.44700  1.000 40.90182  ? 328  ARG   A CA  1 
ATOM   2138 C C   . ARG   A 1 352 ? -57.11500 18.05600  18.66100  1.000 46.69734  ? 328  ARG   A C   1 
ATOM   2139 O O   . ARG   A 1 352 ? -57.19000 17.59400  19.80500  1.000 49.71433  ? 328  ARG   A O   1 
ATOM   2140 C CB  . ARG   A 1 352 ? -55.86400 16.77400  16.91500  1.000 40.36125  ? 328  ARG   A CB  1 
ATOM   2141 C CG  . ARG   A 1 352 ? -55.84000 15.50800  16.09900  1.000 37.30664  ? 328  ARG   A CG  1 
ATOM   2142 C CD  . ARG   A 1 352 ? -54.50300 15.37000  15.42100  1.000 38.51071  ? 328  ARG   A CD  1 
ATOM   2143 N NE  . ARG   A 1 352 ? -53.40200 15.65700  16.33400  1.000 41.14716  ? 328  ARG   A NE  1 
ATOM   2144 C CZ  . ARG   A 1 352 ? -52.97300 14.82500  17.27300  1.000 45.32361  ? 328  ARG   A CZ  1 
ATOM   2145 N NH1 . ARG   A 1 352 ? -53.53900 13.64300  17.46200  1.000 39.83069  ? 328  ARG   A NH1 1 
ATOM   2146 N NH2 . ARG   A 1 352 ? -51.94800 15.18600  18.04100  1.000 45.82828  ? 328  ARG   A NH2 1 
ATOM   2147 N N   . SER   A 1 353 ? -56.92100 19.34400  18.43400  1.000 41.74587  ? 329  SER   A N   1 
ATOM   2148 C CA  . SER   A 1 353 ? -56.78800 20.26800  19.54500  1.000 43.33389  ? 329  SER   A CA  1 
ATOM   2149 C C   . SER   A 1 353 ? -58.14900 20.49300  20.18900  1.000 46.19036  ? 329  SER   A C   1 
ATOM   2150 O O   . SER   A 1 353 ? -59.11800 20.80100  19.48600  1.000 45.45662  ? 329  SER   A O   1 
ATOM   2151 C CB  . SER   A 1 353 ? -56.20700 21.59800  19.07800  1.000 47.85680  ? 329  SER   A CB  1 
ATOM   2152 O OG  . SER   A 1 353 ? -56.48300 22.62000  20.02200  1.000 51.68870  ? 329  SER   A OG  1 
ATOM   2153 N N   . PRO   A 1 354 ? -58.27100 20.33500  21.50800  1.000 51.24902  ? 330  PRO   A N   1 
ATOM   2154 C CA  . PRO   A 1 354 ? -59.52500 20.72600  22.17000  1.000 45.77068  ? 330  PRO   A CA  1 
ATOM   2155 C C   . PRO   A 1 354 ? -59.85700 22.19300  21.98000  1.000 42.84989  ? 330  PRO   A C   1 
ATOM   2156 O O   . PRO   A 1 354 ? -61.03500 22.56700  22.01900  1.000 38.72736  ? 330  PRO   A O   1 
ATOM   2157 C CB  . PRO   A 1 354 ? -59.25700 20.39200  23.64300  1.000 39.84538  ? 330  PRO   A CB  1 
ATOM   2158 C CG  . PRO   A 1 354 ? -58.22300 19.31900  23.60000  1.000 37.71782  ? 330  PRO   A CG  1 
ATOM   2159 C CD  . PRO   A 1 354 ? -57.34500 19.65600  22.42900  1.000 44.26933  ? 330  PRO   A CD  1 
ATOM   2160 N N   . ASP   A 1 355 ? -58.84600 23.03400  21.75500  1.000 39.69759  ? 331  ASP   A N   1 
ATOM   2161 C CA  . ASP   A 1 355 ? -59.07200 24.46800  21.62600  1.000 40.55846  ? 331  ASP   A CA  1 
ATOM   2162 C C   . ASP   A 1 355 ? -59.83500 24.79700  20.34800  1.000 44.82315  ? 331  ASP   A C   1 
ATOM   2163 O O   . ASP   A 1 355 ? -60.84400 25.51100  20.38200  1.000 48.60069  ? 331  ASP   A O   1 
ATOM   2164 C CB  . ASP   A 1 355 ? -57.73200 25.20000  21.66700  1.000 40.27629  ? 331  ASP   A CB  1 
ATOM   2165 C CG  . ASP   A 1 355 ? -57.16000 25.27400  23.06500  1.000 43.73163  ? 331  ASP   A CG  1 
ATOM   2166 O OD1 . ASP   A 1 355 ? -57.94100 25.52700  24.00600  1.000 54.82483  ? 331  ASP   A OD1 1 
ATOM   2167 O OD2 . ASP   A 1 355 ? -55.94100 25.05300  23.22800  1.000 44.45156  ? 331  ASP   A OD2 1 
ATOM   2168 N N   . PHE   A 1 356 ? -59.36700 24.28800  19.20500  1.000 41.01103  ? 332  PHE   A N   1 
ATOM   2169 C CA  . PHE   A 1 356 ? -60.07600 24.54400  17.95800  1.000 40.69447  ? 332  PHE   A CA  1 
ATOM   2170 C C   . PHE   A 1 356 ? -61.41100 23.81700  17.92600  1.000 37.63792  ? 332  PHE   A C   1 
ATOM   2171 O O   . PHE   A 1 356 ? -62.38900 24.33200  17.37200  1.000 33.35114  ? 332  PHE   A O   1 
ATOM   2172 C CB  . PHE   A 1 356 ? -59.21800 24.12400  16.76200  1.000 38.73927  ? 332  PHE   A CB  1 
ATOM   2173 C CG  . PHE   A 1 356 ? -58.01100 24.99300  16.54600  1.000 39.02982  ? 332  PHE   A CG  1 
ATOM   2174 C CD1 . PHE   A 1 356 ? -58.13400 26.25200  15.98300  1.000 38.63628  ? 332  PHE   A CD1 1 
ATOM   2175 C CD2 . PHE   A 1 356 ? -56.74900 24.54400  16.89900  1.000 38.30866  ? 332  PHE   A CD2 1 
ATOM   2176 C CE1 . PHE   A 1 356 ? -57.01900 27.05000  15.78300  1.000 38.10893  ? 332  PHE   A CE1 1 
ATOM   2177 C CE2 . PHE   A 1 356 ? -55.63200 25.33600  16.70100  1.000 34.37340  ? 332  PHE   A CE2 1 
ATOM   2178 C CZ  . PHE   A 1 356 ? -55.76700 26.58900  16.14400  1.000 33.15642  ? 332  PHE   A CZ  1 
ATOM   2179 N N   . ARG   A 1 357 ? -61.47200 22.63300  18.53600  1.000 38.50003  ? 333  ARG   A N   1 
ATOM   2180 C CA  . ARG   A 1 357 ? -62.67200 21.81200  18.45200  1.000 41.95440  ? 333  ARG   A CA  1 
ATOM   2181 C C   . ARG   A 1 357 ? -63.83600 22.44500  19.20700  1.000 43.27043  ? 333  ARG   A C   1 
ATOM   2182 O O   . ARG   A 1 357 ? -64.97600 22.41500  18.72900  1.000 42.49434  ? 333  ARG   A O   1 
ATOM   2183 C CB  . ARG   A 1 357 ? -62.36100 20.40900  18.97200  1.000 44.39088  ? 333  ARG   A CB  1 
ATOM   2184 C CG  . ARG   A 1 357 ? -63.54300 19.47100  19.07500  1.000 50.22487  ? 333  ARG   A CG  1 
ATOM   2185 C CD  . ARG   A 1 357 ? -63.04200 18.09500  19.47000  1.000 57.13356  ? 333  ARG   A CD  1 
ATOM   2186 N NE  . ARG   A 1 357 ? -61.96400 18.20300  20.44600  1.000 60.26433  ? 333  ARG   A NE  1 
ATOM   2187 C CZ  . ARG   A 1 357 ? -61.36200 17.17100  21.02000  1.000 65.79502  ? 333  ARG   A CZ  1 
ATOM   2188 N NH1 . ARG   A 1 357 ? -61.70100 15.92500  20.73200  1.000 88.47411  ? 333  ARG   A NH1 1 
ATOM   2189 N NH2 . ARG   A 1 357 ? -60.39400 17.39500  21.90400  1.000 61.98847  ? 333  ARG   A NH2 1 
ATOM   2190 N N   . ILE   A 1 358 ? -63.57700 23.03500  20.37800  1.000 38.94410  ? 334  ILE   A N   1 
ATOM   2191 C CA  . ILE   A 1 358 ? -64.64800 23.75800  21.05700  1.000 37.84863  ? 334  ILE   A CA  1 
ATOM   2192 C C   . ILE   A 1 358 ? -64.91400 25.09100  20.37100  1.000 35.52156  ? 334  ILE   A C   1 
ATOM   2193 O O   . ILE   A 1 358 ? -66.03800 25.60400  20.42100  1.000 40.77780  ? 334  ILE   A O   1 
ATOM   2194 C CB  . ILE   A 1 358 ? -64.34000 23.96000  22.55200  1.000 48.71097  ? 334  ILE   A CB  1 
ATOM   2195 C CG1 . ILE   A 1 358 ? -63.13100 24.87600  22.74300  1.000 52.35690  ? 334  ILE   A CG1 1 
ATOM   2196 C CG2 . ILE   A 1 358 ? -64.13700 22.62100  23.25200  1.000 46.71232  ? 334  ILE   A CG2 1 
ATOM   2197 C CD1 . ILE   A 1 358 ? -62.82800 25.17600  24.19400  1.000 48.75540  ? 334  ILE   A CD1 1 
ATOM   2198 N N   . ALA   A 1 359 ? -63.90200 25.67800  19.73200  1.000 38.22877  ? 335  ALA   A N   1 
ATOM   2199 C CA  . ALA   A 1 359 ? -64.11700 26.91000  18.98100  1.000 38.74535  ? 335  ALA   A CA  1 
ATOM   2200 C C   . ALA   A 1 359 ? -64.99500 26.65500  17.76500  1.000 38.97955  ? 335  ALA   A C   1 
ATOM   2201 O O   . ALA   A 1 359 ? -65.95200 27.39600  17.51100  1.000 38.47854  ? 335  ALA   A O   1 
ATOM   2202 C CB  . ALA   A 1 359 ? -62.77600 27.51200  18.56400  1.000 37.80508  ? 335  ALA   A CB  1 
ATOM   2203 N N   . PHE   A 1 360 ? -64.68100 25.60200  17.00400  1.000 38.82046  ? 336  PHE   A N   1 
ATOM   2204 C CA  . PHE   A 1 360 ? -65.50500 25.23700  15.85600  1.000 46.68487  ? 336  PHE   A CA  1 
ATOM   2205 C C   . PHE   A 1 360 ? -66.92600 24.90000  16.28900  1.000 40.14440  ? 336  PHE   A C   1 
ATOM   2206 O O   . PHE   A 1 360 ? -67.89400 25.26500  15.61000  1.000 39.48687  ? 336  PHE   A O   1 
ATOM   2207 C CB  . PHE   A 1 360 ? -64.87800 24.04900  15.12400  1.000 42.18974  ? 336  PHE   A CB  1 
ATOM   2208 C CG  . PHE   A 1 360 ? -63.55300 24.35200  14.48300  1.000 36.90439  ? 336  PHE   A CG  1 
ATOM   2209 C CD1 . PHE   A 1 360 ? -63.12600 25.66100  14.30900  1.000 37.17810  ? 336  PHE   A CD1 1 
ATOM   2210 C CD2 . PHE   A 1 360 ? -62.71600 23.32000  14.08100  1.000 29.76093  ? 336  PHE   A CD2 1 
ATOM   2211 C CE1 . PHE   A 1 360 ? -61.89900 25.93300  13.72800  1.000 35.53013  ? 336  PHE   A CE1 1 
ATOM   2212 C CE2 . PHE   A 1 360 ? -61.49200 23.58700  13.50300  1.000 29.75156  ? 336  PHE   A CE2 1 
ATOM   2213 C CZ  . PHE   A 1 360 ? -61.08200 24.89400  13.32600  1.000 33.41982  ? 336  PHE   A CZ  1 
ATOM   2214 N N   . GLN   A 1 361 ? -67.06700 24.21200  17.42600  1.000 39.99113  ? 337  GLN   A N   1 
ATOM   2215 C CA  . GLN   A 1 361 ? -68.38100 23.80000  17.91100  1.000 44.83467  ? 337  GLN   A CA  1 
ATOM   2216 C C   . GLN   A 1 361 ? -69.26200 24.99300  18.25600  1.000 44.11103  ? 337  GLN   A C   1 
ATOM   2217 O O   . GLN   A 1 361 ? -70.49000 24.90600  18.15900  1.000 48.16471  ? 337  GLN   A O   1 
ATOM   2218 C CB  . GLN   A 1 361 ? -68.21400 22.88700  19.12300  1.000 33.85754  ? 337  GLN   A CB  1 
ATOM   2219 C CG  . GLN   A 1 361 ? -67.92100 21.44800  18.75100  1.000 43.50581  ? 337  GLN   A CG  1 
ATOM   2220 C CD  . GLN   A 1 361 ? -67.58400 20.59600  19.95300  1.000 51.60088  ? 337  GLN   A CD  1 
ATOM   2221 O OE1 . GLN   A 1 361 ? -67.60600 21.07000  21.08800  1.000 49.30052  ? 337  GLN   A OE1 1 
ATOM   2222 N NE2 . GLN   A 1 361 ? -67.26000 19.33000  19.71100  1.000 57.39634  ? 337  GLN   A NE2 1 
ATOM   2223 N N   . GLU   A 1 362 ? -68.66300 26.11200  18.66300  1.000 39.60736  ? 338  GLU   A N   1 
ATOM   2224 C CA  . GLU   A 1 362 ? -69.44900 27.31600  18.90000  1.000 42.97152  ? 338  GLU   A CA  1 
ATOM   2225 C C   . GLU   A 1 362 ? -69.71500 28.07000  17.60300  1.000 48.80880  ? 338  GLU   A C   1 
ATOM   2226 O O   . GLU   A 1 362 ? -70.78400 28.67200  17.44800  1.000 50.47286  ? 338  GLU   A O   1 
ATOM   2227 C CB  . GLU   A 1 362 ? -68.73800 28.20800  19.92200  1.000 43.64139  ? 338  GLU   A CB  1 
ATOM   2228 C CG  . GLU   A 1 362 ? -69.63600 29.21800  20.62400  1.000 51.71390  ? 338  GLU   A CG  1 
ATOM   2229 C CD  . GLU   A 1 362 ? -69.79700 30.52000  19.85300  1.000 62.82734  ? 338  GLU   A CD  1 
ATOM   2230 O OE1 . GLU   A 1 362 ? -69.19200 30.66400  18.76800  1.000 51.95411  ? 338  GLU   A OE1 1 
ATOM   2231 O OE2 . GLU   A 1 362 ? -70.54400 31.40000  20.33800  1.000 72.34911  ? 338  GLU   A OE2 1 
ATOM   2232 N N   . LEU   A 1 363 ? -68.76800 28.03700  16.66200  1.000 47.10674  ? 339  LEU   A N   1 
ATOM   2233 C CA  . LEU   A 1 363 ? -68.96400 28.69300  15.37700  1.000 47.71819  ? 339  LEU   A CA  1 
ATOM   2234 C C   . LEU   A 1 363 ? -70.03300 28.00900  14.53400  1.000 47.24456  ? 339  LEU   A C   1 
ATOM   2235 O O   . LEU   A 1 363 ? -70.65600 28.66800  13.69400  1.000 39.09391  ? 339  LEU   A O   1 
ATOM   2236 C CB  . LEU   A 1 363 ? -67.64400 28.73200  14.60100  1.000 35.54495  ? 339  LEU   A CB  1 
ATOM   2237 C CG  . LEU   A 1 363 ? -66.55700 29.67300  15.11800  1.000 33.88769  ? 339  LEU   A CG  1 
ATOM   2238 C CD1 . LEU   A 1 363 ? -65.33900 29.58900  14.22100  1.000 39.81214  ? 339  LEU   A CD1 1 
ATOM   2239 C CD2 . LEU   A 1 363 ? -67.06700 31.09900  15.21600  1.000 33.13367  ? 339  LEU   A CD2 1 
ATOM   2240 N N   . LEU   A 1 364 ? -70.26300 26.71200  14.74400  1.000 44.16482  ? 340  LEU   A N   1 
ATOM   2241 C CA  . LEU   A 1 364 ? -71.11500 25.91100  13.87400  1.000 47.96646  ? 340  LEU   A CA  1 
ATOM   2242 C C   . LEU   A 1 364 ? -72.46100 25.58200  14.51000  1.000 56.37003  ? 340  LEU   A C   1 
ATOM   2243 O O   . LEU   A 1 364 ? -73.07800 24.57500  14.15900  1.000 58.46867  ? 340  LEU   A O   1 
ATOM   2244 C CB  . LEU   A 1 364 ? -70.40600 24.62200  13.45700  1.000 47.29401  ? 340  LEU   A CB  1 
ATOM   2245 C CG  . LEU   A 1 364 ? -69.17200 24.71800  12.55100  1.000 40.90600  ? 340  LEU   A CG  1 
ATOM   2246 C CD1 . LEU   A 1 364 ? -68.68000 23.33200  12.17000  1.000 43.28896  ? 340  LEU   A CD1 1 
ATOM   2247 C CD2 . LEU   A 1 364 ? -69.47100 25.52900  11.30000  1.000 35.12246  ? 340  LEU   A CD2 1 
ATOM   2248 N N   . CYS   A 1 365 ? -72.92900 26.42100  15.44100  1.000 60.33424  ? 341  CYS   A N   1 
ATOM   2249 C CA  . CYS   A 1 365 ? -74.27800 26.31900  16.00700  1.000 52.11569  ? 341  CYS   A CA  1 
ATOM   2250 C C   . CYS   A 1 365 ? -74.41400 25.11400  16.93400  1.000 53.11976  ? 341  CYS   A C   1 
ATOM   2251 O O   . CYS   A 1 365 ? -75.49500 24.54500  17.06000  1.000 58.66994  ? 341  CYS   A O   1 
ATOM   2252 C CB  . CYS   A 1 365 ? -75.33900 26.23500  14.90400  1.000 53.44979  ? 341  CYS   A CB  1 
ATOM   2253 S SG  . CYS   A 1 365 ? -75.21400 27.44100  13.55500  1.000 66.00015  ? 341  CYS   A SG  1 
ATOM   2254 N N   . LEU   A 1 366 ? -73.33100 24.69400  17.58300  1.000 55.10910  ? 342  LEU   A N   1 
ATOM   2255 C CA  . LEU   A 1 366 ? -73.37600 23.47500  18.39500  1.000 57.12560  ? 342  LEU   A CA  1 
ATOM   2256 C C   . LEU   A 1 366 ? -73.00200 23.70700  19.86200  1.000 57.49256  ? 342  LEU   A C   1 
ATOM   2257 O O   . LEU   A 1 366 ? -73.15100 24.80900  20.39400  1.000 61.32300  ? 342  LEU   A O   1 
ATOM   2258 C CB  . LEU   A 1 366 ? -72.46000 22.40400  17.79000  1.000 56.74219  ? 342  LEU   A CB  1 
ATOM   2259 C CG  . LEU   A 1 366 ? -72.34700 22.37000  16.26700  1.000 55.47415  ? 342  LEU   A CG  1 
ATOM   2260 C CD1 . LEU   A 1 366 ? -71.25100 21.42400  15.83100  1.000 56.26597  ? 342  LEU   A CD1 1 
ATOM   2261 C CD2 . LEU   A 1 366 ? -73.67900 21.91500  15.69700  1.000 55.89724  ? 342  LEU   A CD2 1 
ATOM   2262 N N   . ILE   A 1 391 ? -40.59600 14.83100  36.74800  1.000 67.20793  ? 1003 ILE   A N   1 
ATOM   2263 C CA  . ILE   A 1 391 ? -41.57300 14.32200  37.70400  1.000 58.87073  ? 1003 ILE   A CA  1 
ATOM   2264 C C   . ILE   A 1 391 ? -42.75200 15.28300  37.82900  1.000 52.01352  ? 1003 ILE   A C   1 
ATOM   2265 O O   . ILE   A 1 391 ? -43.90400 14.84500  37.87600  1.000 44.88223  ? 1003 ILE   A O   1 
ATOM   2266 C CB  . ILE   A 1 391 ? -40.91800 14.03900  39.08800  1.000 54.24402  ? 1003 ILE   A CB  1 
ATOM   2267 C CG1 . ILE   A 1 391 ? -41.89800 13.30900  40.01100  1.000 60.56676  ? 1003 ILE   A CG1 1 
ATOM   2268 C CG2 . ILE   A 1 391 ? -40.39100 15.31400  39.74600  1.000 43.29347  ? 1003 ILE   A CG2 1 
ATOM   2269 C CD1 . ILE   A 1 391 ? -42.26500 11.91400  39.54800  1.000 61.65533  ? 1003 ILE   A CD1 1 
ATOM   2270 N N   . PHE   A 1 392 ? -42.45700 16.58700  37.87100  1.000 48.16906  ? 1004 PHE   A N   1 
ATOM   2271 C CA  . PHE   A 1 392 ? -43.50400 17.59600  37.98100  1.000 40.27929  ? 1004 PHE   A CA  1 
ATOM   2272 C C   . PHE   A 1 392 ? -44.57500 17.38500  36.92300  1.000 52.28788  ? 1004 PHE   A C   1 
ATOM   2273 O O   . PHE   A 1 392 ? -45.76100 17.23000  37.23600  1.000 53.67105  ? 1004 PHE   A O   1 
ATOM   2274 C CB  . PHE   A 1 392 ? -42.90100 18.99400  37.86100  1.000 38.62614  ? 1004 PHE   A CB  1 
ATOM   2275 C CG  . PHE   A 1 392 ? -42.32500 19.51800  39.13700  1.000 50.31745  ? 1004 PHE   A CG  1 
ATOM   2276 C CD1 . PHE   A 1 392 ? -42.75600 19.03300  40.36100  1.000 55.42797  ? 1004 PHE   A CD1 1 
ATOM   2277 C CD2 . PHE   A 1 392 ? -41.35500 20.50600  39.11600  1.000 56.14574  ? 1004 PHE   A CD2 1 
ATOM   2278 C CE1 . PHE   A 1 392 ? -42.22500 19.52100  41.54400  1.000 53.41818  ? 1004 PHE   A CE1 1 
ATOM   2279 C CE2 . PHE   A 1 392 ? -40.82000 20.99800  40.29200  1.000 55.94804  ? 1004 PHE   A CE2 1 
ATOM   2280 C CZ  . PHE   A 1 392 ? -41.25500 20.50500  41.50800  1.000 55.98634  ? 1004 PHE   A CZ  1 
ATOM   2281 N N   . GLU   A 1 393 ? -44.17000 17.35700  35.65500  1.000 57.57147  ? 1005 GLU   A N   1 
ATOM   2282 C CA  . GLU   A 1 393 ? -45.13800 17.08900  34.60300  1.000 51.42691  ? 1005 GLU   A CA  1 
ATOM   2283 C C   . GLU   A 1 393 ? -45.40700 15.59900  34.42100  1.000 47.12580  ? 1005 GLU   A C   1 
ATOM   2284 O O   . GLU   A 1 393 ? -46.44200 15.24200  33.85000  1.000 40.48158  ? 1005 GLU   A O   1 
ATOM   2285 C CB  . GLU   A 1 393 ? -44.68700 17.73600  33.29000  1.000 50.65098  ? 1005 GLU   A CB  1 
ATOM   2286 C CG  . GLU   A 1 393 ? -43.23600 17.50700  32.89900  1.000 62.67354  ? 1005 GLU   A CG  1 
ATOM   2287 C CD  . GLU   A 1 393 ? -42.71800 18.57400  31.93800  1.000 60.51098  ? 1005 GLU   A CD  1 
ATOM   2288 O OE1 . GLU   A 1 393 ? -43.31800 19.66900  31.88000  1.000 55.92406  ? 1005 GLU   A OE1 1 
ATOM   2289 O OE2 . GLU   A 1 393 ? -41.72000 18.31400  31.23000  1.000 49.90893  ? 1005 GLU   A OE2 1 
ATOM   2290 N N   . MET   A 1 394 ? -44.53200 14.72200  34.92300  1.000 52.04209  ? 1006 MET   A N   1 
ATOM   2291 C CA  . MET   A 1 394 ? -44.81400 13.28800  34.86200  1.000 51.39068  ? 1006 MET   A CA  1 
ATOM   2292 C C   . MET   A 1 394 ? -46.01500 12.92400  35.72900  1.000 58.43504  ? 1006 MET   A C   1 
ATOM   2293 O O   . MET   A 1 394 ? -46.90900 12.19100  35.28800  1.000 55.93005  ? 1006 MET   A O   1 
ATOM   2294 C CB  . MET   A 1 394 ? -43.58700 12.47800  35.28700  1.000 61.41847  ? 1006 MET   A CB  1 
ATOM   2295 C CG  . MET   A 1 394 ? -43.84300 10.96500  35.35800  1.000 65.49151  ? 1006 MET   A CG  1 
ATOM   2296 S SD  . MET   A 1 394 ? -42.42800 10.01900  35.97500  1.000 80.51442  ? 1006 MET   A SD  1 
ATOM   2297 C CE  . MET   A 1 394 ? -43.17500 8.42900   36.32400  1.000 66.01344  ? 1006 MET   A CE  1 
ATOM   2298 N N   . LEU   A 1 395 ? -46.04800 13.41500  36.97300  1.000 54.60739  ? 1007 LEU   A N   1 
ATOM   2299 C CA  . LEU   A 1 395 ? -47.16700 13.09600  37.85700  1.000 48.73729  ? 1007 LEU   A CA  1 
ATOM   2300 C C   . LEU   A 1 395 ? -48.44200 13.80000  37.40800  1.000 48.25275  ? 1007 LEU   A C   1 
ATOM   2301 O O   . LEU   A 1 395 ? -49.53900 13.24600  37.54000  1.000 40.35461  ? 1007 LEU   A O   1 
ATOM   2302 C CB  . LEU   A 1 395 ? -46.82600 13.46800  39.29900  1.000 51.38399  ? 1007 LEU   A CB  1 
ATOM   2303 C CG  . LEU   A 1 395 ? -46.05400 12.42200  40.10800  1.000 49.05562  ? 1007 LEU   A CG  1 
ATOM   2304 C CD1 . LEU   A 1 395 ? -45.32400 13.10300  41.24600  1.000 42.96996  ? 1007 LEU   A CD1 1 
ATOM   2305 C CD2 . LEU   A 1 395 ? -46.96900 11.31500  40.62900  1.000 39.98069  ? 1007 LEU   A CD2 1 
ATOM   2306 N N   . ARG   A 1 396 ? -48.31600 15.01600  36.86500  1.000 51.08039  ? 1008 ARG   A N   1 
ATOM   2307 C CA  . ARG   A 1 396 ? -49.48300 15.72100  36.33900  1.000 43.81942  ? 1008 ARG   A CA  1 
ATOM   2308 C C   . ARG   A 1 396 ? -50.19400 14.90300  35.26600  1.000 44.46795  ? 1008 ARG   A C   1 
ATOM   2309 O O   . ARG   A 1 396 ? -51.42300 14.96800  35.15200  1.000 46.01808  ? 1008 ARG   A O   1 
ATOM   2310 C CB  . ARG   A 1 396 ? -49.06900 17.09200  35.79300  1.000 38.73411  ? 1008 ARG   A CB  1 
ATOM   2311 C CG  . ARG   A 1 396 ? -50.12600 17.79000  34.93400  1.000 37.42634  ? 1008 ARG   A CG  1 
ATOM   2312 C CD  . ARG   A 1 396 ? -51.35800 18.16700  35.74800  1.000 37.90267  ? 1008 ARG   A CD  1 
ATOM   2313 N NE  . ARG   A 1 396 ? -52.36200 18.88400  34.96900  1.000 30.67915  ? 1008 ARG   A NE  1 
ATOM   2314 C CZ  . ARG   A 1 396 ? -53.32100 18.30200  34.26000  1.000 37.07909  ? 1008 ARG   A CZ  1 
ATOM   2315 N NH1 . ARG   A 1 396 ? -53.40800 16.98400  34.16100  1.000 36.74142  ? 1008 ARG   A NH1 1 
ATOM   2316 N NH2 . ARG   A 1 396 ? -54.21900 19.05900  33.63500  1.000 35.05581  ? 1008 ARG   A NH2 1 
ATOM   2317 N N   . ILE   A 1 397 ? -49.45100 14.11500  34.48400  1.000 44.06217  ? 1009 ILE   A N   1 
ATOM   2318 C CA  . ILE   A 1 397 ? -50.08900 13.19600  33.54400  1.000 49.44818  ? 1009 ILE   A CA  1 
ATOM   2319 C C   . ILE   A 1 397 ? -50.73800 12.03300  34.28200  1.000 49.47404  ? 1009 ILE   A C   1 
ATOM   2320 O O   . ILE   A 1 397 ? -51.89600 11.68000  34.02800  1.000 38.94935  ? 1009 ILE   A O   1 
ATOM   2321 C CB  . ILE   A 1 397 ? -49.08100 12.68200  32.50000  1.000 54.94866  ? 1009 ILE   A CB  1 
ATOM   2322 C CG1 . ILE   A 1 397 ? -48.31600 13.82800  31.83700  1.000 53.70770  ? 1009 ILE   A CG1 1 
ATOM   2323 C CG2 . ILE   A 1 397 ? -49.78800 11.81200  31.48400  1.000 59.92596  ? 1009 ILE   A CG2 1 
ATOM   2324 C CD1 . ILE   A 1 397 ? -46.94700 13.41400  31.34800  1.000 49.13251  ? 1009 ILE   A CD1 1 
ATOM   2325 N N   . ASP   A 1 398 ? -49.99200 11.40600  35.19100  1.000 61.51940  ? 1010 ASP   A N   1 
ATOM   2326 C CA  . ASP   A 1 398 ? -50.46400 10.18900  35.84300  1.000 59.98352  ? 1010 ASP   A CA  1 
ATOM   2327 C C   . ASP   A 1 398 ? -51.47700 10.47800  36.94200  1.000 52.07432  ? 1010 ASP   A C   1 
ATOM   2328 O O   . ASP   A 1 398 ? -52.34600 9.64100   37.21000  1.000 50.40403  ? 1010 ASP   A O   1 
ATOM   2329 C CB  . ASP   A 1 398 ? -49.27300 9.41200   36.40300  1.000 65.24072  ? 1010 ASP   A CB  1 
ATOM   2330 C CG  . ASP   A 1 398 ? -48.49300 8.68700   35.31700  1.000 71.54468  ? 1010 ASP   A CG  1 
ATOM   2331 O OD1 . ASP   A 1 398 ? -48.98700 8.62300   34.17100  1.000 67.91002  ? 1010 ASP   A OD1 1 
ATOM   2332 O OD2 . ASP   A 1 398 ? -47.38000 8.19400   35.60800  1.000 72.48534  ? 1010 ASP   A OD2 1 
ATOM   2333 N N   . GLU   A 1 399 ? -51.39400 11.64700  37.58000  1.000 47.24240  ? 1011 GLU   A N   1 
ATOM   2334 C CA  . GLU   A 1 399 ? -52.36700 11.98300  38.61400  1.000 52.38045  ? 1011 GLU   A CA  1 
ATOM   2335 C C   . GLU   A 1 399 ? -53.64700 12.53900  38.00500  1.000 49.78131  ? 1011 GLU   A C   1 
ATOM   2336 O O   . GLU   A 1 399 ? -54.75000 12.11400  38.36200  1.000 57.32494  ? 1011 GLU   A O   1 
ATOM   2337 C CB  . GLU   A 1 399 ? -51.77400 12.99900  39.59800  1.000 51.60440  ? 1011 GLU   A CB  1 
ATOM   2338 C CG  . GLU   A 1 399 ? -50.70900 12.46200  40.55400  1.000 49.65972  ? 1011 GLU   A CG  1 
ATOM   2339 C CD  . GLU   A 1 399 ? -51.16300 11.27400  41.38500  1.000 52.89829  ? 1011 GLU   A CD  1 
ATOM   2340 O OE1 . GLU   A 1 399 ? -52.38600 11.03600  41.50600  1.000 55.34643  ? 1011 GLU   A OE1 1 
ATOM   2341 O OE2 . GLU   A 1 399 ? -50.28100 10.56900  41.92100  1.000 58.13917  ? 1011 GLU   A OE2 1 
ATOM   2342 N N   . GLY   A 1 400 ? -53.51400 13.47600  37.07800  1.000 46.76251  ? 1012 GLY   A N   1 
ATOM   2343 C CA  . GLY   A 1 400 ? -54.62500 14.29700  36.64800  1.000 39.77676  ? 1012 GLY   A CA  1 
ATOM   2344 C C   . GLY   A 1 400 ? -54.65600 15.60200  37.41600  1.000 41.35372  ? 1012 GLY   A C   1 
ATOM   2345 O O   . GLY   A 1 400 ? -53.74900 15.93700  38.18400  1.000 40.60392  ? 1012 GLY   A O   1 
ATOM   2346 N N   . LEU   A 1 401 ? -55.72700 16.35800  37.19400  1.000 38.62893  ? 1013 LEU   A N   1 
ATOM   2347 C CA  . LEU   A 1 401 ? -55.94700 17.59000  37.94400  1.000 41.73773  ? 1013 LEU   A CA  1 
ATOM   2348 C C   . LEU   A 1 401 ? -57.44200 17.82000  38.06300  1.000 42.72609  ? 1013 LEU   A C   1 
ATOM   2349 O O   . LEU   A 1 401 ? -58.14200 17.90200  37.05000  1.000 47.34555  ? 1013 LEU   A O   1 
ATOM   2350 C CB  . LEU   A 1 401 ? -55.27400 18.79300  37.27900  1.000 39.46130  ? 1013 LEU   A CB  1 
ATOM   2351 C CG  . LEU   A 1 401 ? -55.71600 20.15100  37.84000  1.000 40.37604  ? 1013 LEU   A CG  1 
ATOM   2352 C CD1 . LEU   A 1 401 ? -55.31700 20.29700  39.29500  1.000 42.06119  ? 1013 LEU   A CD1 1 
ATOM   2353 C CD2 . LEU   A 1 401 ? -55.15100 21.30000  37.02100  1.000 47.58270  ? 1013 LEU   A CD2 1 
ATOM   2354 N N   . ARG   A 1 402 ? -57.92600 17.91700  39.29700  1.000 45.37590  ? 1014 ARG   A N   1 
ATOM   2355 C CA  . ARG   A 1 402 ? -59.33200 18.15900  39.57500  1.000 43.39235  ? 1014 ARG   A CA  1 
ATOM   2356 C C   . ARG   A 1 402 ? -59.44300 19.25700  40.62200  1.000 39.82273  ? 1014 ARG   A C   1 
ATOM   2357 O O   . ARG   A 1 402 ? -58.70900 19.25400  41.61500  1.000 40.97572  ? 1014 ARG   A O   1 
ATOM   2358 C CB  . ARG   A 1 402 ? -60.02900 16.88500  40.06400  1.000 45.26554  ? 1014 ARG   A CB  1 
ATOM   2359 C CG  . ARG   A 1 402 ? -59.55900 15.62100  39.36400  1.000 43.51378  ? 1014 ARG   A CG  1 
ATOM   2360 C CD  . ARG   A 1 402 ? -60.71800 14.78100  38.87200  1.000 48.48136  ? 1014 ARG   A CD  1 
ATOM   2361 N NE  . ARG   A 1 402 ? -60.32200 13.39200  38.67400  1.000 54.75234  ? 1014 ARG   A NE  1 
ATOM   2362 C CZ  . ARG   A 1 402 ? -61.08100 12.34500  38.97300  1.000 60.34962  ? 1014 ARG   A CZ  1 
ATOM   2363 N NH1 . ARG   A 1 402 ? -62.28700 12.49400  39.50000  1.000 52.58474  ? 1014 ARG   A NH1 1 
ATOM   2364 N NH2 . ARG   A 1 402 ? -60.61800 11.12000  38.73800  1.000 55.53600  ? 1014 ARG   A NH2 1 
ATOM   2365 N N   . LEU   A 1 403 ? -60.35600 20.19500  40.39300  1.000 34.43417  ? 1015 LEU   A N   1 
ATOM   2366 C CA  . LEU   A 1 403 ? -60.50500 21.35100  41.26400  1.000 38.66360  ? 1015 LEU   A CA  1 
ATOM   2367 C C   . LEU   A 1 403 ? -61.56100 21.15200  42.34400  1.000 45.90956  ? 1015 LEU   A C   1 
ATOM   2368 O O   . LEU   A 1 403 ? -61.85500 22.09500  43.08700  1.000 45.01879  ? 1015 LEU   A O   1 
ATOM   2369 C CB  . LEU   A 1 403 ? -60.83800 22.59100  40.42900  1.000 38.62168  ? 1015 LEU   A CB  1 
ATOM   2370 C CG  . LEU   A 1 403 ? -59.68400 23.03600  39.53300  1.000 43.57529  ? 1015 LEU   A CG  1 
ATOM   2371 C CD1 . LEU   A 1 403 ? -60.09300 24.19300  38.63100  1.000 40.15617  ? 1015 LEU   A CD1 1 
ATOM   2372 C CD2 . LEU   A 1 403 ? -58.47400 23.39300  40.37700  1.000 49.91983  ? 1015 LEU   A CD2 1 
ATOM   2373 N N   . LYS   A 1 404 ? -62.13300 19.95800  42.45200  1.000 38.62376  ? 1016 LYS   A N   1 
ATOM   2374 C CA  . LYS   A 1 404 ? -63.11500 19.65200  43.47500  1.000 42.37685  ? 1016 LYS   A CA  1 
ATOM   2375 C C   . LYS   A 1 404 ? -62.71500 18.35100  44.15600  1.000 47.65931  ? 1016 LYS   A C   1 
ATOM   2376 O O   . LYS   A 1 404 ? -62.07100 17.49200  43.54800  1.000 42.86961  ? 1016 LYS   A O   1 
ATOM   2377 C CB  . LYS   A 1 404 ? -64.53200 19.54500  42.87800  1.000 48.14360  ? 1016 LYS   A CB  1 
ATOM   2378 C CG  . LYS   A 1 404 ? -65.63100 19.35600  43.91700  1.000 60.63119  ? 1016 LYS   A CG  1 
ATOM   2379 C CD  . LYS   A 1 404 ? -67.01900 19.46100  43.31400  1.000 69.37601  ? 1016 LYS   A CD  1 
ATOM   2380 C CE  . LYS   A 1 404 ? -68.07200 18.94800  44.29200  1.000 74.04825  ? 1016 LYS   A CE  1 
ATOM   2381 N NZ  . LYS   A 1 404 ? -68.07500 19.71700  45.57200  1.000 64.03704  ? 1016 LYS   A NZ  1 
ATOM   2382 N N   . ILE   A 1 405 ? -63.09000 18.22100  45.43300  1.000 55.55134  ? 1017 ILE   A N   1 
ATOM   2383 C CA  . ILE   A 1 405 ? -62.76000 17.02000  46.19500  1.000 50.70893  ? 1017 ILE   A CA  1 
ATOM   2384 C C   . ILE   A 1 405 ? -63.33500 15.79300  45.50500  1.000 53.25874  ? 1017 ILE   A C   1 
ATOM   2385 O O   . ILE   A 1 405 ? -64.52900 15.74200  45.18300  1.000 58.10303  ? 1017 ILE   A O   1 
ATOM   2386 C CB  . ILE   A 1 405 ? -63.28200 17.14200  47.63400  1.000 50.27711  ? 1017 ILE   A CB  1 
ATOM   2387 C CG1 . ILE   A 1 405 ? -62.47000 18.17500  48.41200  1.000 52.43152  ? 1017 ILE   A CG1 1 
ATOM   2388 C CG2 . ILE   A 1 405 ? -63.24000 15.79300  48.33900  1.000 54.67889  ? 1017 ILE   A CG2 1 
ATOM   2389 C CD1 . ILE   A 1 405 ? -62.96400 18.38100  49.81600  1.000 45.91447  ? 1017 ILE   A CD1 1 
ATOM   2390 N N   . TYR   A 1 406 ? -62.48200 14.79800  45.26500  1.000 50.34148  ? 1018 TYR   A N   1 
ATOM   2391 C CA  . TYR   A 1 406 ? -62.89600 13.54100  44.65600  1.000 53.12568  ? 1018 TYR   A CA  1 
ATOM   2392 C C   . TYR   A 1 406 ? -62.31900 12.38200  45.45900  1.000 52.07204  ? 1018 TYR   A C   1 
ATOM   2393 O O   . TYR   A 1 406 ? -61.53800 12.57100  46.39500  1.000 50.18620  ? 1018 TYR   A O   1 
ATOM   2394 C CB  . TYR   A 1 406 ? -62.46600 13.44600  43.18300  1.000 51.09743  ? 1018 TYR   A CB  1 
ATOM   2395 C CG  . TYR   A 1 406 ? -60.97200 13.49300  42.93600  1.000 49.92667  ? 1018 TYR   A CG  1 
ATOM   2396 C CD1 . TYR   A 1 406 ? -60.26800 14.68900  43.00700  1.000 49.19402  ? 1018 TYR   A CD1 1 
ATOM   2397 C CD2 . TYR   A 1 406 ? -60.26400 12.33400  42.64000  1.000 49.72600  ? 1018 TYR   A CD2 1 
ATOM   2398 C CE1 . TYR   A 1 406 ? -58.90200 14.72900  42.77900  1.000 49.00006  ? 1018 TYR   A CE1 1 
ATOM   2399 C CE2 . TYR   A 1 406 ? -58.90100 12.36400  42.41400  1.000 48.19384  ? 1018 TYR   A CE2 1 
ATOM   2400 C CZ  . TYR   A 1 406 ? -58.22500 13.56300  42.48400  1.000 48.65122  ? 1018 TYR   A CZ  1 
ATOM   2401 O OH  . TYR   A 1 406 ? -56.86800 13.59700  42.25700  1.000 56.10899  ? 1018 TYR   A OH  1 
ATOM   2402 N N   . LYS   A 1 407 ? -62.70800 11.17000  45.07900  1.000 54.56294  ? 1019 LYS   A N   1 
ATOM   2403 C CA  . LYS   A 1 407 ? -62.28200 9.95100   45.75200  1.000 58.92139  ? 1019 LYS   A CA  1 
ATOM   2404 C C   . LYS   A 1 407 ? -61.34100 9.18400   44.83600  1.000 62.39452  ? 1019 LYS   A C   1 
ATOM   2405 O O   . LYS   A 1 407 ? -61.66600 8.94900   43.66700  1.000 60.86148  ? 1019 LYS   A O   1 
ATOM   2406 C CB  . LYS   A 1 407 ? -63.48700 9.08400   46.11900  1.000 67.74109  ? 1019 LYS   A CB  1 
ATOM   2407 C CG  . LYS   A 1 407 ? -64.41000 9.71200   47.14900  1.000 69.46575  ? 1019 LYS   A CG  1 
ATOM   2408 C CD  . LYS   A 1 407 ? -64.64700 8.78600   48.32800  1.000 68.93081  ? 1019 LYS   A CD  1 
ATOM   2409 C CE  . LYS   A 1 407 ? -65.90200 9.18000   49.08900  1.000 69.42839  ? 1019 LYS   A CE  1 
ATOM   2410 N NZ  . LYS   A 1 407 ? -66.05600 8.38500   50.34100  1.000 76.25828  ? 1019 LYS   A NZ  1 
ATOM   2411 N N   . ASP   A 1 408 ? -60.18400 8.79100   45.36500  1.000 59.31408  ? 1020 ASP   A N   1 
ATOM   2412 C CA  . ASP   A 1 408 ? -59.19100 8.07700   44.57400  1.000 59.36156  ? 1020 ASP   A CA  1 
ATOM   2413 C C   . ASP   A 1 408 ? -59.64200 6.63000   44.35500  1.000 65.99713  ? 1020 ASP   A C   1 
ATOM   2414 O O   . ASP   A 1 408 ? -60.78200 6.25600   44.64600  1.000 70.61037  ? 1020 ASP   A O   1 
ATOM   2415 C CB  . ASP   A 1 408 ? -57.80900 8.19800   45.22400  1.000 62.08668  ? 1020 ASP   A CB  1 
ATOM   2416 C CG  . ASP   A 1 408 ? -57.67200 7.41000   46.52300  1.000 71.30030  ? 1020 ASP   A CG  1 
ATOM   2417 O OD1 . ASP   A 1 408 ? -58.62900 6.73500   46.95600  1.000 79.56420  ? 1020 ASP   A OD1 1 
ATOM   2418 O OD2 . ASP   A 1 408 ? -56.57800 7.47700   47.12300  1.000 68.81999  ? 1020 ASP   A OD2 1 
ATOM   2419 N N   . THR   A 1 409 ? -58.74200 5.80000   43.82100  1.000 76.57766  ? 1021 THR   A N   1 
ATOM   2420 C CA  . THR   A 1 409 ? -59.08600 4.40900   43.53600  1.000 81.67058  ? 1021 THR   A CA  1 
ATOM   2421 C C   . THR   A 1 409 ? -59.46100 3.66000   44.81000  1.000 88.78335  ? 1021 THR   A C   1 
ATOM   2422 O O   . THR   A 1 409 ? -60.39400 2.84700   44.81300  1.000 95.51846  ? 1021 THR   A O   1 
ATOM   2423 C CB  . THR   A 1 409 ? -57.91700 3.72000   42.82500  1.000 85.42462  ? 1021 THR   A CB  1 
ATOM   2424 O OG1 . THR   A 1 409 ? -57.83800 4.18400   41.47000  1.000 90.84874  ? 1021 THR   A OG1 1 
ATOM   2425 C CG2 . THR   A 1 409 ? -58.09200 2.20500   42.82700  1.000 87.60287  ? 1021 THR   A CG2 1 
ATOM   2426 N N   . GLU   A 1 410 ? -58.76600 3.94400   45.90900  1.000 85.52074  ? 1022 GLU   A N   1 
ATOM   2427 C CA  . GLU   A 1 410 ? -58.97200 3.25100   47.17200  1.000 80.80918  ? 1022 GLU   A CA  1 
ATOM   2428 C C   . GLU   A 1 410 ? -60.04800 3.89600   48.04000  1.000 85.79867  ? 1022 GLU   A C   1 
ATOM   2429 O O   . GLU   A 1 410 ? -60.28700 3.42200   49.15600  1.000 91.23407  ? 1022 GLU   A O   1 
ATOM   2430 C CB  . GLU   A 1 410 ? -57.64800 3.17600   47.94500  1.000 79.85030  ? 1022 GLU   A CB  1 
ATOM   2431 C CG  . GLU   A 1 410 ? -56.61400 2.24000   47.32300  1.000 82.69786  ? 1022 GLU   A CG  1 
ATOM   2432 C CD  . GLU   A 1 410 ? -55.97300 2.81300   46.06600  1.000 101.33571 ? 1022 GLU   A CD  1 
ATOM   2433 O OE1 . GLU   A 1 410 ? -56.24400 3.98800   45.73900  1.000 99.17735  ? 1022 GLU   A OE1 1 
ATOM   2434 O OE2 . GLU   A 1 410 ? -55.20700 2.08400   45.39800  1.000 110.68430 ? 1022 GLU   A OE2 1 
ATOM   2435 N N   . GLY   A 1 411 ? -60.69900 4.95300   47.56100  1.000 81.32342  ? 1023 GLY   A N   1 
ATOM   2436 C CA  . GLY   A 1 411 ? -61.79200 5.57200   48.28400  1.000 80.57300  ? 1023 GLY   A CA  1 
ATOM   2437 C C   . GLY   A 1 411 ? -61.42300 6.74400   49.16500  1.000 73.15164  ? 1023 GLY   A C   1 
ATOM   2438 O O   . GLY   A 1 411 ? -62.28600 7.23800   49.89900  1.000 77.94081  ? 1023 GLY   A O   1 
ATOM   2439 N N   . TYR   A 1 412 ? -60.18100 7.21300   49.11400  1.000 69.22570  ? 1024 TYR   A N   1 
ATOM   2440 C CA  . TYR   A 1 412 ? -59.73600 8.31800   49.95100  1.000 69.48227  ? 1024 TYR   A CA  1 
ATOM   2441 C C   . TYR   A 1 412 ? -60.01400 9.64900   49.26800  1.000 60.85975  ? 1024 TYR   A C   1 
ATOM   2442 O O   . TYR   A 1 412 ? -59.91100 9.76400   48.04500  1.000 70.44673  ? 1024 TYR   A O   1 
ATOM   2443 C CB  . TYR   A 1 412 ? -58.24300 8.19600   50.26200  1.000 73.11031  ? 1024 TYR   A CB  1 
ATOM   2444 C CG  . TYR   A 1 412 ? -57.88900 7.02400   51.15000  1.000 78.65548  ? 1024 TYR   A CG  1 
ATOM   2445 C CD1 . TYR   A 1 412 ? -58.09300 5.71400   50.73000  1.000 82.30782  ? 1024 TYR   A CD1 1 
ATOM   2446 C CD2 . TYR   A 1 412 ? -57.36900 7.22900   52.42000  1.000 72.95910  ? 1024 TYR   A CD2 1 
ATOM   2447 C CE1 . TYR   A 1 412 ? -57.77400 4.64500   51.54200  1.000 79.42165  ? 1024 TYR   A CE1 1 
ATOM   2448 C CE2 . TYR   A 1 412 ? -57.04900 6.16600   53.24000  1.000 75.43314  ? 1024 TYR   A CE2 1 
ATOM   2449 C CZ  . TYR   A 1 412 ? -57.25400 4.87700   52.79600  1.000 78.33298  ? 1024 TYR   A CZ  1 
ATOM   2450 O OH  . TYR   A 1 412 ? -56.93400 3.81900   53.61400  1.000 89.45569  ? 1024 TYR   A OH  1 
ATOM   2451 N N   . TYR   A 1 413 ? -60.36000 10.65600  50.06400  1.000 52.11349  ? 1025 TYR   A N   1 
ATOM   2452 C CA  . TYR   A 1 413 ? -60.65900 11.96400  49.49900  1.000 48.74779  ? 1025 TYR   A CA  1 
ATOM   2453 C C   . TYR   A 1 413 ? -59.37300 12.66300  49.07800  1.000 56.35817  ? 1025 TYR   A C   1 
ATOM   2454 O O   . TYR   A 1 413 ? -58.42400 12.77900  49.86000  1.000 54.27883  ? 1025 TYR   A O   1 
ATOM   2455 C CB  . TYR   A 1 413 ? -61.43800 12.82700  50.49000  1.000 50.44269  ? 1025 TYR   A CB  1 
ATOM   2456 C CG  . TYR   A 1 413 ? -62.78500 12.26100  50.88500  1.000 62.49957  ? 1025 TYR   A CG  1 
ATOM   2457 C CD1 . TYR   A 1 413 ? -62.88500 11.14900  51.71600  1.000 67.27114  ? 1025 TYR   A CD1 1 
ATOM   2458 C CD2 . TYR   A 1 413 ? -63.96000 12.83600  50.42100  1.000 57.23527  ? 1025 TYR   A CD2 1 
ATOM   2459 C CE1 . TYR   A 1 413 ? -64.11600 10.63300  52.07400  1.000 59.65859  ? 1025 TYR   A CE1 1 
ATOM   2460 C CE2 . TYR   A 1 413 ? -65.19400 12.32400  50.77400  1.000 55.03296  ? 1025 TYR   A CE2 1 
ATOM   2461 C CZ  . TYR   A 1 413 ? -65.26500 11.22800  51.60300  1.000 55.55480  ? 1025 TYR   A CZ  1 
ATOM   2462 O OH  . TYR   A 1 413 ? -66.49000 10.71800  51.95200  1.000 65.00539  ? 1025 TYR   A OH  1 
ATOM   2463 N N   . THR   A 1 414 ? -59.35500 13.12700  47.83000  1.000 60.26314  ? 1026 THR   A N   1 
ATOM   2464 C CA  . THR   A 1 414 ? -58.18500 13.70000  47.18300  1.000 50.08157  ? 1026 THR   A CA  1 
ATOM   2465 C C   . THR   A 1 414 ? -58.63200 14.93500  46.41100  1.000 50.18514  ? 1026 THR   A C   1 
ATOM   2466 O O   . THR   A 1 414 ? -59.80200 15.06400  46.04500  1.000 53.78580  ? 1026 THR   A O   1 
ATOM   2467 C CB  . THR   A 1 414 ? -57.52200 12.65800  46.25600  1.000 53.13584  ? 1026 THR   A CB  1 
ATOM   2468 O OG1 . THR   A 1 414 ? -57.29700 11.44000  46.97900  1.000 57.12332  ? 1026 THR   A OG1 1 
ATOM   2469 C CG2 . THR   A 1 414 ? -56.20600 13.15000  45.69800  1.000 54.90607  ? 1026 THR   A CG2 1 
ATOM   2470 N N   . ILE   A 1 415 ? -57.70100 15.86200  46.18000  1.000 48.11303  ? 1027 ILE   A N   1 
ATOM   2471 C CA  . ILE   A 1 415 ? -58.00100 17.07800  45.43200  1.000 46.74278  ? 1027 ILE   A CA  1 
ATOM   2472 C C   . ILE   A 1 415 ? -56.74800 17.50300  44.67700  1.000 47.59050  ? 1027 ILE   A C   1 
ATOM   2473 O O   . ILE   A 1 415 ? -55.63500 17.07000  44.98400  1.000 44.48460  ? 1027 ILE   A O   1 
ATOM   2474 C CB  . ILE   A 1 415 ? -58.50700 18.21700  46.35300  1.000 40.70012  ? 1027 ILE   A CB  1 
ATOM   2475 C CG1 . ILE   A 1 415 ? -59.18100 19.32100  45.53400  1.000 42.20598  ? 1027 ILE   A CG1 1 
ATOM   2476 C CG2 . ILE   A 1 415 ? -57.36600 18.78500  47.18100  1.000 43.21505  ? 1027 ILE   A CG2 1 
ATOM   2477 C CD1 . ILE   A 1 415 ? -59.96000 20.31200  46.36100  1.000 47.41252  ? 1027 ILE   A CD1 1 
ATOM   2478 N N   . GLY   A 1 416 ? -56.94000 18.34300  43.66100  1.000 44.08039  ? 1028 GLY   A N   1 
ATOM   2479 C CA  . GLY   A 1 416 ? -55.80500 18.89700  42.94000  1.000 44.04108  ? 1028 GLY   A CA  1 
ATOM   2480 C C   . GLY   A 1 416 ? -55.10500 17.86100  42.08000  1.000 45.72784  ? 1028 GLY   A C   1 
ATOM   2481 O O   . GLY   A 1 416 ? -55.73800 17.08200  41.36000  1.000 38.33983  ? 1028 GLY   A O   1 
ATOM   2482 N N   . ILE   A 1 417 ? -53.77800 17.84900  42.14700  1.000 40.28913  ? 1029 ILE   A N   1 
ATOM   2483 C CA  . ILE   A 1 417 ? -52.98100 16.87800  41.38700  1.000 46.75487  ? 1029 ILE   A CA  1 
ATOM   2484 C C   . ILE   A 1 417 ? -52.65400 15.76200  42.36900  1.000 43.85561  ? 1029 ILE   A C   1 
ATOM   2485 O O   . ILE   A 1 417 ? -51.55200 15.65000  42.91400  1.000 43.53374  ? 1029 ILE   A O   1 
ATOM   2486 C CB  . ILE   A 1 417 ? -51.74000 17.51100  40.75800  1.000 49.42473  ? 1029 ILE   A CB  1 
ATOM   2487 C CG1 . ILE   A 1 417 ? -52.14100 18.72500  39.90100  1.000 45.33476  ? 1029 ILE   A CG1 1 
ATOM   2488 C CG2 . ILE   A 1 417 ? -51.01300 16.52100  39.86500  1.000 44.81060  ? 1029 ILE   A CG2 1 
ATOM   2489 C CD1 . ILE   A 1 417 ? -51.00100 19.67300  39.58400  1.000 38.33475  ? 1029 ILE   A CD1 1 
ATOM   2490 N N   . GLY   A 1 418 ? -53.64300 14.90000  42.58900  1.000 43.91205  ? 1030 GLY   A N   1 
ATOM   2491 C CA  . GLY   A 1 418 ? -53.46700 13.70200  43.42200  1.000 47.87348  ? 1030 GLY   A CA  1 
ATOM   2492 C C   . GLY   A 1 418 ? -53.06400 13.97000  44.85300  1.000 50.04937  ? 1030 GLY   A C   1 
ATOM   2493 O O   . GLY   A 1 418 ? -52.35800 13.15400  45.45500  1.000 47.95767  ? 1030 GLY   A O   1 
ATOM   2494 N N   . HIS   A 1 419 ? -53.48900 15.10100  45.41300  1.000 52.41056  ? 1031 HIS   A N   1 
ATOM   2495 C CA  . HIS   A 1 419 ? -53.12300 15.48200  46.77200  1.000 52.57512  ? 1031 HIS   A CA  1 
ATOM   2496 C C   . HIS   A 1 419 ? -54.07800 14.83400  47.76500  1.000 52.04044  ? 1031 HIS   A C   1 
ATOM   2497 O O   . HIS   A 1 419 ? -55.25500 15.20100  47.83100  1.000 54.19692  ? 1031 HIS   A O   1 
ATOM   2498 C CB  . HIS   A 1 419 ? -53.14800 16.99500  46.94800  1.000 53.39831  ? 1031 HIS   A CB  1 
ATOM   2499 C CG  . HIS   A 1 419 ? -53.17300 17.42100  48.38300  1.000 54.92197  ? 1031 HIS   A CG  1 
ATOM   2500 N ND1 . HIS   A 1 419 ? -52.09500 17.25900  49.22600  1.000 61.33313  ? 1031 HIS   A ND1 1 
ATOM   2501 C CD2 . HIS   A 1 419 ? -54.15500 17.97500  49.13300  1.000 55.03225  ? 1031 HIS   A CD2 1 
ATOM   2502 C CE1 . HIS   A 1 419 ? -52.40500 17.71000  50.42800  1.000 56.72603  ? 1031 HIS   A CE1 1 
ATOM   2503 N NE2 . HIS   A 1 419 ? -53.65000 18.14800  50.40000  1.000 58.19820  ? 1031 HIS   A NE2 1 
ATOM   2504 N N   . LEU   A 1 420 ? -53.56800 13.89500  48.55700  1.000 52.62246  ? 1032 LEU   A N   1 
ATOM   2505 C CA  . LEU   A 1 420 ? -54.39000 13.27200  49.58600  1.000 58.32759  ? 1032 LEU   A CA  1 
ATOM   2506 C C   . LEU   A 1 420 ? -54.80700 14.30100  50.63100  1.000 56.10934  ? 1032 LEU   A C   1 
ATOM   2507 O O   . LEU   A 1 420 ? -54.00800 15.14000  51.05700  1.000 51.40640  ? 1032 LEU   A O   1 
ATOM   2508 C CB  . LEU   A 1 420 ? -53.63200 12.12400  50.25100  1.000 57.15001  ? 1032 LEU   A CB  1 
ATOM   2509 C CG  . LEU   A 1 420 ? -54.45200 11.30600  51.25000  1.000 52.38301  ? 1032 LEU   A CG  1 
ATOM   2510 C CD1 . LEU   A 1 420 ? -55.61900 10.63600  50.54700  1.000 58.70368  ? 1032 LEU   A CD1 1 
ATOM   2511 C CD2 . LEU   A 1 420 ? -53.58300 10.27300  51.94300  1.000 49.55636  ? 1032 LEU   A CD2 1 
ATOM   2512 N N   . LEU   A 1 421 ? -56.07600 14.23900  51.03600  1.000 50.04436  ? 1033 LEU   A N   1 
ATOM   2513 C CA  . LEU   A 1 421 ? -56.62100 15.16900  52.01700  1.000 51.07678  ? 1033 LEU   A CA  1 
ATOM   2514 C C   . LEU   A 1 421 ? -56.70700 14.56100  53.41000  1.000 57.31063  ? 1033 LEU   A C   1 
ATOM   2515 O O   . LEU   A 1 421 ? -56.21100 15.15100  54.37500  1.000 53.66147  ? 1033 LEU   A O   1 
ATOM   2516 C CB  . LEU   A 1 421 ? -58.00100 15.66000  51.57100  1.000 44.43447  ? 1033 LEU   A CB  1 
ATOM   2517 C CG  . LEU   A 1 421 ? -57.93900 16.79400  50.55100  1.000 47.34601  ? 1033 LEU   A CG  1 
ATOM   2518 C CD1 . LEU   A 1 421 ? -59.29000 17.00500  49.88300  1.000 49.02981  ? 1033 LEU   A CD1 1 
ATOM   2519 C CD2 . LEU   A 1 421 ? -57.44300 18.07100  51.20800  1.000 44.16508  ? 1033 LEU   A CD2 1 
ATOM   2520 N N   . THR   A 1 422 ? -57.32900 13.39200  53.53700  1.000 55.87857  ? 1034 THR   A N   1 
ATOM   2521 C CA  . THR   A 1 422 ? -57.32900 12.68500  54.80600  1.000 53.64768  ? 1034 THR   A CA  1 
ATOM   2522 C C   . THR   A 1 422 ? -57.70000 11.22900  54.57800  1.000 56.58229  ? 1034 THR   A C   1 
ATOM   2523 O O   . THR   A 1 422 ? -58.48300 10.90200  53.68200  1.000 54.91759  ? 1034 THR   A O   1 
ATOM   2524 C CB  . THR   A 1 422 ? -58.28700 13.32400  55.82500  1.000 56.82400  ? 1034 THR   A CB  1 
ATOM   2525 O OG1 . THR   A 1 422 ? -58.08400 12.72400  57.11200  1.000 56.26343  ? 1034 THR   A OG1 1 
ATOM   2526 C CG2 . THR   A 1 422 ? -59.74100 13.15200  55.40200  1.000 53.43287  ? 1034 THR   A CG2 1 
ATOM   2527 N N   . LYS   A 1 423 ? -57.09400 10.36300  55.38500  1.000 60.80787  ? 1035 LYS   A N   1 
ATOM   2528 C CA  . LYS   A 1 423 ? -57.49800 8.97000   55.49600  1.000 62.69020  ? 1035 LYS   A CA  1 
ATOM   2529 C C   . LYS   A 1 423 ? -58.88300 8.82200   56.10900  1.000 60.46092  ? 1035 LYS   A C   1 
ATOM   2530 O O   . LYS   A 1 423 ? -59.51100 7.76900   55.94600  1.000 59.44953  ? 1035 LYS   A O   1 
ATOM   2531 C CB  . LYS   A 1 423 ? -56.46600 8.19300   56.32600  1.000 62.27805  ? 1035 LYS   A CB  1 
ATOM   2532 C CG  . LYS   A 1 423 ? -56.17700 8.76900   57.72900  1.000 69.40595  ? 1035 LYS   A CG  1 
ATOM   2533 C CD  . LYS   A 1 423 ? -55.33000 10.04500  57.67400  1.000 65.15672  ? 1035 LYS   A CD  1 
ATOM   2534 C CE  . LYS   A 1 423 ? -54.82000 10.48100  59.02700  1.000 76.54588  ? 1035 LYS   A CE  1 
ATOM   2535 N NZ  . LYS   A 1 423 ? -54.15600 11.81000  58.92600  1.000 92.72033  ? 1035 LYS   A NZ  1 
ATOM   2536 N N   . SER   A 1 424 ? -59.36900 9.84500   56.80700  1.000 58.79759  ? 1036 SER   A N   1 
ATOM   2537 C CA  . SER   A 1 424 ? -60.68400 9.78000   57.42100  1.000 62.19831  ? 1036 SER   A CA  1 
ATOM   2538 C C   . SER   A 1 424 ? -61.77500 9.68800   56.35300  1.000 67.86059  ? 1036 SER   A C   1 
ATOM   2539 O O   . SER   A 1 424 ? -61.62100 10.21400  55.24600  1.000 69.80314  ? 1036 SER   A O   1 
ATOM   2540 C CB  . SER   A 1 424 ? -60.92000 11.00500  58.30000  1.000 57.68078  ? 1036 SER   A CB  1 
ATOM   2541 O OG  . SER   A 1 424 ? -62.29200 11.36400  58.31800  1.000 53.15691  ? 1036 SER   A OG  1 
ATOM   2542 N N   . PRO   A 1 425 ? -62.88300 9.01200   56.65600  1.000 64.59918  ? 1037 PRO   A N   1 
ATOM   2543 C CA  . PRO   A 1 425 ? -63.99800 8.91500   55.70600  1.000 60.35149  ? 1037 PRO   A CA  1 
ATOM   2544 C C   . PRO   A 1 425 ? -65.05200 10.00500  55.83200  1.000 59.27497  ? 1037 PRO   A C   1 
ATOM   2545 O O   . PRO   A 1 425 ? -66.03400 9.97000   55.08200  1.000 62.51723  ? 1037 PRO   A O   1 
ATOM   2546 C CB  . PRO   A 1 425 ? -64.60400 7.55000   56.05700  1.000 58.92521  ? 1037 PRO   A CB  1 
ATOM   2547 C CG  . PRO   A 1 425 ? -64.37000 7.42300   57.51500  1.000 66.16515  ? 1037 PRO   A CG  1 
ATOM   2548 C CD  . PRO   A 1 425 ? -63.05200 8.09900   57.80000  1.000 64.53780  ? 1037 PRO   A CD  1 
ATOM   2549 N N   . SER   A 1 426 ? -64.89600 10.95500  56.74900  1.000 56.96637  ? 1038 SER   A N   1 
ATOM   2550 C CA  . SER   A 1 426 ? -65.87700 12.02100  56.92200  1.000 63.06596  ? 1038 SER   A CA  1 
ATOM   2551 C C   . SER   A 1 426 ? -65.50400 13.18300  56.01200  1.000 58.77093  ? 1038 SER   A C   1 
ATOM   2552 O O   . SER   A 1 426 ? -64.48900 13.85100  56.23700  1.000 58.41738  ? 1038 SER   A O   1 
ATOM   2553 C CB  . SER   A 1 426 ? -65.95100 12.47100  58.37700  1.000 61.26984  ? 1038 SER   A CB  1 
ATOM   2554 O OG  . SER   A 1 426 ? -66.97400 13.43700  58.54700  1.000 67.31208  ? 1038 SER   A OG  1 
ATOM   2555 N N   . LEU   A 1 427 ? -66.33500 13.43000  54.99200  1.000 55.88007  ? 1039 LEU   A N   1 
ATOM   2556 C CA  . LEU   A 1 427 ? -66.07500 14.51400  54.04700  1.000 51.44269  ? 1039 LEU   A CA  1 
ATOM   2557 C C   . LEU   A 1 427 ? -65.83200 15.84400  54.75000  1.000 52.89766  ? 1039 LEU   A C   1 
ATOM   2558 O O   . LEU   A 1 427 ? -65.10400 16.69800  54.22900  1.000 48.45733  ? 1039 LEU   A O   1 
ATOM   2559 C CB  . LEU   A 1 427 ? -67.24000 14.64500  53.06100  1.000 45.35456  ? 1039 LEU   A CB  1 
ATOM   2560 C CG  . LEU   A 1 427 ? -67.18600 15.83300  52.09400  1.000 45.97838  ? 1039 LEU   A CG  1 
ATOM   2561 C CD1 . LEU   A 1 427 ? -66.16400 15.60600  50.98800  1.000 51.15446  ? 1039 LEU   A CD1 1 
ATOM   2562 C CD2 . LEU   A 1 427 ? -68.55900 16.13300  51.50900  1.000 51.99184  ? 1039 LEU   A CD2 1 
ATOM   2563 N N   . ASN   A 1 428 ? -66.41600 16.03800  55.93700  1.000 53.03778  ? 1040 ASN   A N   1 
ATOM   2564 C CA  . ASN   A 1 428 ? -66.18200 17.28200  56.65900  1.000 39.25423  ? 1040 ASN   A CA  1 
ATOM   2565 C C   . ASN   A 1 428 ? -64.73800 17.37400  57.12900  1.000 39.66165  ? 1040 ASN   A C   1 
ATOM   2566 O O   . ASN   A 1 428 ? -64.17700 18.47400  57.18300  1.000 41.03238  ? 1040 ASN   A O   1 
ATOM   2567 C CB  . ASN   A 1 428 ? -67.13800 17.40200  57.84500  1.000 50.13814  ? 1040 ASN   A CB  1 
ATOM   2568 C CG  . ASN   A 1 428 ? -67.08100 18.77400  58.50600  1.000 56.31681  ? 1040 ASN   A CG  1 
ATOM   2569 O OD1 . ASN   A 1 428 ? -66.45200 19.69900  57.99200  1.000 63.75838  ? 1040 ASN   A OD1 1 
ATOM   2570 N ND2 . ASN   A 1 428 ? -67.70100 18.89500  59.67200  1.000 43.30848  ? 1040 ASN   A ND2 1 
ATOM   2571 N N   . ALA   A 1 429 ? -64.12100 16.23700  57.46900  1.000 41.05369  ? 1041 ALA   A N   1 
ATOM   2572 C CA  . ALA   A 1 429 ? -62.70000 16.24800  57.80200  1.000 42.14308  ? 1041 ALA   A CA  1 
ATOM   2573 C C   . ALA   A 1 429 ? -61.86000 16.59700  56.58100  1.000 47.06224  ? 1041 ALA   A C   1 
ATOM   2574 O O   . ALA   A 1 429 ? -60.88100 17.34500  56.68700  1.000 43.68433  ? 1041 ALA   A O   1 
ATOM   2575 C CB  . ALA   A 1 429 ? -62.27100 14.89700  58.37900  1.000 31.92187  ? 1041 ALA   A CB  1 
ATOM   2576 N N   . ALA   A 1 430 ? -62.24000 16.07700  55.41100  1.000 48.41864  ? 1042 ALA   A N   1 
ATOM   2577 C CA  . ALA   A 1 430 ? -61.52300 16.39900  54.18300  1.000 46.45595  ? 1042 ALA   A CA  1 
ATOM   2578 C C   . ALA   A 1 430 ? -61.59800 17.89000  53.87500  1.000 45.87002  ? 1042 ALA   A C   1 
ATOM   2579 O O   . ALA   A 1 430 ? -60.58600 18.51000  53.52500  1.000 48.01299  ? 1042 ALA   A O   1 
ATOM   2580 C CB  . ALA   A 1 430 ? -62.08200 15.57600  53.02400  1.000 44.38994  ? 1042 ALA   A CB  1 
ATOM   2581 N N   . LYS   A 1 431 ? -62.78500 18.48900  54.01400  1.000 36.66305  ? 1043 LYS   A N   1 
ATOM   2582 C CA  . LYS   A 1 431 ? -62.90600 19.92600  53.79000  1.000 36.13512  ? 1043 LYS   A CA  1 
ATOM   2583 C C   . LYS   A 1 431 ? -62.14300 20.71800  54.84400  1.000 42.85504  ? 1043 LYS   A C   1 
ATOM   2584 O O   . LYS   A 1 431 ? -61.54400 21.75000  54.53000  1.000 45.90464  ? 1043 LYS   A O   1 
ATOM   2585 C CB  . LYS   A 1 431 ? -64.37500 20.34700  53.76500  1.000 38.72482  ? 1043 LYS   A CB  1 
ATOM   2586 C CG  . LYS   A 1 431 ? -65.17800 19.72700  52.63800  1.000 39.73986  ? 1043 LYS   A CG  1 
ATOM   2587 C CD  . LYS   A 1 431 ? -66.51700 20.42200  52.46000  1.000 34.20227  ? 1043 LYS   A CD  1 
ATOM   2588 C CE  . LYS   A 1 431 ? -67.26300 19.84300  51.27300  1.000 37.20000  ? 1043 LYS   A CE  1 
ATOM   2589 N NZ  . LYS   A 1 431 ? -68.55200 20.53900  51.03300  1.000 40.61894  ? 1043 LYS   A NZ  1 
ATOM   2590 N N   . SER   A 1 432 ? -62.13900 20.24800  56.09400  1.000 49.30924  ? 1044 SER   A N   1 
ATOM   2591 C CA  . SER   A 1 432 ? -61.44300 20.97700  57.15000  1.000 54.21770  ? 1044 SER   A CA  1 
ATOM   2592 C C   . SER   A 1 432 ? -59.93400 20.95700  56.93900  1.000 50.63502  ? 1044 SER   A C   1 
ATOM   2593 O O   . SER   A 1 432 ? -59.26700 21.98500  57.10700  1.000 54.92301  ? 1044 SER   A O   1 
ATOM   2594 C CB  . SER   A 1 432 ? -61.80400 20.39500  58.51600  1.000 50.12789  ? 1044 SER   A CB  1 
ATOM   2595 O OG  . SER   A 1 432 ? -61.26700 19.09300  58.66900  1.000 56.80523  ? 1044 SER   A OG  1 
ATOM   2596 N N   . GLU   A 1 433 ? -59.37800 19.80000  56.57300  1.000 46.70331  ? 1045 GLU   A N   1 
ATOM   2597 C CA  . GLU   A 1 433 ? -57.95900 19.74400  56.23500  1.000 47.58685  ? 1045 GLU   A CA  1 
ATOM   2598 C C   . GLU   A 1 433 ? -57.65200 20.60900  55.01700  1.000 49.10763  ? 1045 GLU   A C   1 
ATOM   2599 O O   . GLU   A 1 433 ? -56.63400 21.31000  54.98400  1.000 49.62053  ? 1045 GLU   A O   1 
ATOM   2600 C CB  . GLU   A 1 433 ? -57.53500 18.29700  55.98100  1.000 46.50024  ? 1045 GLU   A CB  1 
ATOM   2601 C CG  . GLU   A 1 433 ? -57.77100 17.35000  57.14300  1.000 51.77971  ? 1045 GLU   A CG  1 
ATOM   2602 C CD  . GLU   A 1 433 ? -56.67200 17.41600  58.18500  1.000 61.35561  ? 1045 GLU   A CD  1 
ATOM   2603 O OE1 . GLU   A 1 433 ? -55.74000 18.23200  58.02200  1.000 58.70106  ? 1045 GLU   A OE1 1 
ATOM   2604 O OE2 . GLU   A 1 433 ? -56.74300 16.64900  59.17000  1.000 64.49257  ? 1045 GLU   A OE2 1 
ATOM   2605 N N   . LEU   A 1 434 ? -58.52900 20.57600  54.01000  1.000 44.09733  ? 1046 LEU   A N   1 
ATOM   2606 C CA  . LEU   A 1 434 ? -58.31100 21.36800  52.80400  1.000 47.46324  ? 1046 LEU   A CA  1 
ATOM   2607 C C   . LEU   A 1 434 ? -58.30900 22.86200  53.10300  1.000 48.73761  ? 1046 LEU   A C   1 
ATOM   2608 O O   . LEU   A 1 434 ? -57.52200 23.61500  52.51700  1.000 52.67019  ? 1046 LEU   A O   1 
ATOM   2609 C CB  . LEU   A 1 434 ? -59.37600 21.03100  51.75900  1.000 47.24598  ? 1046 LEU   A CB  1 
ATOM   2610 C CG  . LEU   A 1 434 ? -59.43300 21.92600  50.52300  1.000 44.84930  ? 1046 LEU   A CG  1 
ATOM   2611 C CD1 . LEU   A 1 434 ? -58.13800 21.84900  49.72900  1.000 46.98696  ? 1046 LEU   A CD1 1 
ATOM   2612 C CD2 . LEU   A 1 434 ? -60.60800 21.51100  49.66500  1.000 46.72561  ? 1046 LEU   A CD2 1 
ATOM   2613 N N   . ASP   A 1 435 ? -59.18800 23.31700  54.00300  1.000 47.78392  ? 1047 ASP   A N   1 
ATOM   2614 C CA  . ASP   A 1 435 ? -59.19300 24.73400  54.35500  1.000 47.15325  ? 1047 ASP   A CA  1 
ATOM   2615 C C   . ASP   A 1 435 ? -57.92200 25.11600  55.10200  1.000 44.24967  ? 1047 ASP   A C   1 
ATOM   2616 O O   . ASP   A 1 435 ? -57.38300 26.21100  54.90200  1.000 44.31711  ? 1047 ASP   A O   1 
ATOM   2617 C CB  . ASP   A 1 435 ? -60.43100 25.08900  55.18400  1.000 48.91686  ? 1047 ASP   A CB  1 
ATOM   2618 C CG  . ASP   A 1 435 ? -61.73700 24.76200  54.47200  1.000 58.74638  ? 1047 ASP   A CG  1 
ATOM   2619 O OD1 . ASP   A 1 435 ? -61.90000 25.15800  53.29700  1.000 52.54025  ? 1047 ASP   A OD1 1 
ATOM   2620 O OD2 . ASP   A 1 435 ? -62.62300 24.14700  55.10600  1.000 69.23127  ? 1047 ASP   A OD2 1 
ATOM   2621 N N   . LYS   A 1 436 ? -57.42400 24.22800  55.96300  1.000 45.62900  ? 1048 LYS   A N   1 
ATOM   2622 C CA  . LYS   A 1 436 ? -56.17000 24.50500  56.65300  1.000 50.87878  ? 1048 LYS   A CA  1 
ATOM   2623 C C   . LYS   A 1 436 ? -55.00200 24.52600  55.67400  1.000 49.31941  ? 1048 LYS   A C   1 
ATOM   2624 O O   . LYS   A 1 436 ? -54.07500 25.33200  55.81900  1.000 47.95553  ? 1048 LYS   A O   1 
ATOM   2625 C CB  . LYS   A 1 436 ? -55.94500 23.47000  57.75800  1.000 51.71815  ? 1048 LYS   A CB  1 
ATOM   2626 C CG  . LYS   A 1 436 ? -54.60200 23.57800  58.46500  1.000 58.21081  ? 1048 LYS   A CG  1 
ATOM   2627 C CD  . LYS   A 1 436 ? -54.48400 22.55800  59.59100  1.000 69.15717  ? 1048 LYS   A CD  1 
ATOM   2628 C CE  . LYS   A 1 436 ? -54.77800 21.14800  59.10200  1.000 69.38056  ? 1048 LYS   A CE  1 
ATOM   2629 N NZ  . LYS   A 1 436 ? -54.72100 20.15500  60.21300  1.000 66.48737  ? 1048 LYS   A NZ  1 
ATOM   2630 N N   . ALA   A 1 437 ? -55.04300 23.66400  54.65500  1.000 47.10759  ? 1049 ALA   A N   1 
ATOM   2631 C CA  . ALA   A 1 437 ? -53.96100 23.61400  53.67800  1.000 46.37613  ? 1049 ALA   A CA  1 
ATOM   2632 C C   . ALA   A 1 437 ? -53.96000 24.84400  52.77900  1.000 47.50473  ? 1049 ALA   A C   1 
ATOM   2633 O O   . ALA   A 1 437 ? -52.89400 25.38500  52.46100  1.000 60.01325  ? 1049 ALA   A O   1 
ATOM   2634 C CB  . ALA   A 1 437 ? -54.07100 22.34100  52.83900  1.000 43.13478  ? 1049 ALA   A CB  1 
ATOM   2635 N N   . ILE   A 1 438 ? -55.13900 25.30000  52.36100  1.000 40.12609  ? 1050 ILE   A N   1 
ATOM   2636 C CA  . ILE   A 1 438 ? -55.22200 26.42100  51.43200  1.000 42.38944  ? 1050 ILE   A CA  1 
ATOM   2637 C C   . ILE   A 1 438 ? -55.24400 27.76400  52.16000  1.000 38.37283  ? 1050 ILE   A C   1 
ATOM   2638 O O   . ILE   A 1 438 ? -54.75500 28.76500  51.62800  1.000 40.67636  ? 1050 ILE   A O   1 
ATOM   2639 C CB  . ILE   A 1 438 ? -56.45000 26.25700  50.51400  1.000 48.97929  ? 1050 ILE   A CB  1 
ATOM   2640 C CG1 . ILE   A 1 438 ? -56.28500 25.03300  49.61100  1.000 47.14190  ? 1050 ILE   A CG1 1 
ATOM   2641 C CG2 . ILE   A 1 438 ? -56.66500 27.49000  49.64500  1.000 43.33442  ? 1050 ILE   A CG2 1 
ATOM   2642 C CD1 . ILE   A 1 438 ? -55.12100 25.14400  48.64100  1.000 51.12847  ? 1050 ILE   A CD1 1 
ATOM   2643 N N   . GLY   A 1 439 ? -55.77700 27.81200  53.37500  1.000 39.27101  ? 1051 GLY   A N   1 
ATOM   2644 C CA  . GLY   A 1 439 ? -55.84000 29.06200  54.10000  1.000 40.75535  ? 1051 GLY   A CA  1 
ATOM   2645 C C   . GLY   A 1 439 ? -57.06600 29.89500  53.81600  1.000 44.72936  ? 1051 GLY   A C   1 
ATOM   2646 O O   . GLY   A 1 439 ? -56.99000 31.12900  53.86200  1.000 48.63637  ? 1051 GLY   A O   1 
ATOM   2647 N N   . ARG   A 1 440 ? -58.19200 29.25900  53.50600  1.000 39.98173  ? 1052 ARG   A N   1 
ATOM   2648 C CA  . ARG   A 1 440 ? -59.47900 29.92300  53.33600  1.000 36.82300  ? 1052 ARG   A CA  1 
ATOM   2649 C C   . ARG   A 1 440 ? -60.54300 28.83500  53.35500  1.000 45.48756  ? 1052 ARG   A C   1 
ATOM   2650 O O   . ARG   A 1 440 ? -60.22900 27.64200  53.34800  1.000 46.84368  ? 1052 ARG   A O   1 
ATOM   2651 C CB  . ARG   A 1 440 ? -59.53700 30.73800  52.04000  1.000 43.65612  ? 1052 ARG   A CB  1 
ATOM   2652 C CG  . ARG   A 1 440 ? -59.41800 29.90400  50.77900  1.000 42.87490  ? 1052 ARG   A CG  1 
ATOM   2653 C CD  . ARG   A 1 440 ? -59.91300 30.66200  49.56100  1.000 39.17994  ? 1052 ARG   A CD  1 
ATOM   2654 N NE  . ARG   A 1 440 ? -59.66400 29.91500  48.33400  1.000 44.37740  ? 1052 ARG   A NE  1 
ATOM   2655 C CZ  . ARG   A 1 440 ? -60.46100 28.96700  47.86000  1.000 44.68792  ? 1052 ARG   A CZ  1 
ATOM   2656 N NH1 . ARG   A 1 440 ? -61.59000 28.64700  48.46700  1.000 46.50179  ? 1052 ARG   A NH1 1 
ATOM   2657 N NH2 . ARG   A 1 440 ? -60.11600 28.32400  46.74800  1.000 53.93432  ? 1052 ARG   A NH2 1 
ATOM   2658 N N   . ASN   A 1 441 ? -61.80700 29.25400  53.37700  1.000 48.42809  ? 1053 ASN   A N   1 
ATOM   2659 C CA  . ASN   A 1 441 ? -62.92800 28.31300  53.43300  1.000 51.74374  ? 1053 ASN   A CA  1 
ATOM   2660 C C   . ASN   A 1 441 ? -63.28000 27.88100  52.01300  1.000 52.53320  ? 1053 ASN   A C   1 
ATOM   2661 O O   . ASN   A 1 441 ? -64.02200 28.56800  51.30600  1.000 47.70111  ? 1053 ASN   A O   1 
ATOM   2662 C CB  . ASN   A 1 441 ? -64.13000 28.93400  54.13100  1.000 49.97119  ? 1053 ASN   A CB  1 
ATOM   2663 C CG  . ASN   A 1 441 ? -65.09800 27.88800  54.64700  1.000 60.73644  ? 1053 ASN   A CG  1 
ATOM   2664 O OD1 . ASN   A 1 441 ? -64.77700 26.69800  54.68600  1.000 60.94447  ? 1053 ASN   A OD1 1 
ATOM   2665 N ND2 . ASN   A 1 441 ? -66.29900 28.31900  55.01500  1.000 58.74965  ? 1053 ASN   A ND2 1 
ATOM   2666 N N   . THR   A 1 442 ? -62.76900 26.71700  51.60600  1.000 49.12579  ? 1054 THR   A N   1 
ATOM   2667 C CA  . THR   A 1 442 ? -62.92000 26.26800  50.22600  1.000 49.61833  ? 1054 THR   A CA  1 
ATOM   2668 C C   . THR   A 1 442 ? -64.30000 25.68300  49.95500  1.000 45.91622  ? 1054 THR   A C   1 
ATOM   2669 O O   . THR   A 1 442 ? -64.83500 25.84000  48.85300  1.000 49.11939  ? 1054 THR   A O   1 
ATOM   2670 C CB  . THR   A 1 442 ? -61.85200 25.22600  49.89500  1.000 48.44666  ? 1054 THR   A CB  1 
ATOM   2671 O OG1 . THR   A 1 442 ? -62.07100 24.05200  50.68700  1.000 41.94264  ? 1054 THR   A OG1 1 
ATOM   2672 C CG2 . THR   A 1 442 ? -60.46700 25.77700  50.18500  1.000 52.08934  ? 1054 THR   A CG2 1 
ATOM   2673 N N   . ASN   A 1 443 ? -64.88400 25.00700  50.94400  1.000 55.29785  ? 1055 ASN   A N   1 
ATOM   2674 C CA  . ASN   A 1 443 ? -66.08200 24.18500  50.75000  1.000 49.52504  ? 1055 ASN   A CA  1 
ATOM   2675 C C   . ASN   A 1 443 ? -65.86600 23.14200  49.65000  1.000 42.24439  ? 1055 ASN   A C   1 
ATOM   2676 O O   . ASN   A 1 443 ? -66.75700 22.86500  48.84500  1.000 48.35526  ? 1055 ASN   A O   1 
ATOM   2677 C CB  . ASN   A 1 443 ? -67.31700 25.04300  50.46300  1.000 42.15748  ? 1055 ASN   A CB  1 
ATOM   2678 C CG  . ASN   A 1 443 ? -68.61100 24.27800  50.66600  1.000 37.11352  ? 1055 ASN   A CG  1 
ATOM   2679 O OD1 . ASN   A 1 443 ? -68.59600 23.09600  51.00100  1.000 33.05173  ? 1055 ASN   A OD1 1 
ATOM   2680 N ND2 . ASN   A 1 443 ? -69.73500 24.94700  50.45600  1.000 42.21603  ? 1055 ASN   A ND2 1 
ATOM   2681 N N   . GLY   A 1 444 ? -64.66700 22.56100  49.61300  1.000 36.96611  ? 1056 GLY   A N   1 
ATOM   2682 C CA  . GLY   A 1 444 ? -64.38500 21.43500  48.75300  1.000 43.33173  ? 1056 GLY   A CA  1 
ATOM   2683 C C   . GLY   A 1 444 ? -63.85200 21.77200  47.37700  1.000 48.65805  ? 1056 GLY   A C   1 
ATOM   2684 O O   . GLY   A 1 444 ? -63.49600 20.85100  46.62900  1.000 40.17868  ? 1056 GLY   A O   1 
ATOM   2685 N N   . VAL   A 1 445 ? -63.78100 23.05200  47.01500  1.000 46.47612  ? 1057 VAL   A N   1 
ATOM   2686 C CA  . VAL   A 1 445 ? -63.34500 23.47100  45.68700  1.000 45.30013  ? 1057 VAL   A CA  1 
ATOM   2687 C C   . VAL   A 1 445 ? -62.21000 24.47900  45.81900  1.000 45.34544  ? 1057 VAL   A C   1 
ATOM   2688 O O   . VAL   A 1 445 ? -62.22600 25.34200  46.70400  1.000 43.91091  ? 1057 VAL   A O   1 
ATOM   2689 C CB  . VAL   A 1 445 ? -64.51500 24.05600  44.86600  1.000 43.20593  ? 1057 VAL   A CB  1 
ATOM   2690 C CG1 . VAL   A 1 445 ? -65.61200 23.01900  44.71300  1.000 45.65968  ? 1057 VAL   A CG1 1 
ATOM   2691 C CG2 . VAL   A 1 445 ? -65.06900 25.30400  45.53200  1.000 41.20794  ? 1057 VAL   A CG2 1 
ATOM   2692 N N   . ILE   A 1 446 ? -61.21900 24.36200  44.93500  1.000 45.26063  ? 1058 ILE   A N   1 
ATOM   2693 C CA  . ILE   A 1 446 ? -60.04300 25.22100  44.92500  1.000 50.18259  ? 1058 ILE   A CA  1 
ATOM   2694 C C   . ILE   A 1 446 ? -59.79300 25.69600  43.49600  1.000 48.80663  ? 1058 ILE   A C   1 
ATOM   2695 O O   . ILE   A 1 446 ? -60.50600 25.32800  42.56300  1.000 52.60578  ? 1058 ILE   A O   1 
ATOM   2696 C CB  . ILE   A 1 446 ? -58.79700 24.50900  45.49100  1.000 47.21039  ? 1058 ILE   A CB  1 
ATOM   2697 C CG1 . ILE   A 1 446 ? -58.45800 23.28600  44.63800  1.000 45.54900  ? 1058 ILE   A CG1 1 
ATOM   2698 C CG2 . ILE   A 1 446 ? -59.01700 24.10900  46.94400  1.000 49.72103  ? 1058 ILE   A CG2 1 
ATOM   2699 C CD1 . ILE   A 1 446 ? -57.21100 22.56800  45.07800  1.000 47.36688  ? 1058 ILE   A CD1 1 
ATOM   2700 N N   . THR   A 1 447 ? -58.76300 26.52100  43.33500  1.000 49.76191  ? 1059 THR   A N   1 
ATOM   2701 C CA  . THR   A 1 447 ? -58.35700 27.01700  42.02800  1.000 49.44870  ? 1059 THR   A CA  1 
ATOM   2702 C C   . THR   A 1 447 ? -57.12200 26.26900  41.53200  1.000 48.56788  ? 1059 THR   A C   1 
ATOM   2703 O O   . THR   A 1 447 ? -56.41300 25.61100  42.29700  1.000 46.90543  ? 1059 THR   A O   1 
ATOM   2704 C CB  . THR   A 1 447 ? -58.07300 28.52200  42.07300  1.000 44.37727  ? 1059 THR   A CB  1 
ATOM   2705 O OG1 . THR   A 1 447 ? -56.95900 28.77700  42.94000  1.000 44.87484  ? 1059 THR   A OG1 1 
ATOM   2706 C CG2 . THR   A 1 447 ? -59.29500 29.28700  42.56600  1.000 33.73702  ? 1059 THR   A CG2 1 
ATOM   2707 N N   . LYS   A 1 448 ? -56.87800 26.37100  40.22200  1.000 52.06177  ? 1060 LYS   A N   1 
ATOM   2708 C CA  . LYS   A 1 448 ? -55.73600 25.67400  39.63800  1.000 52.72374  ? 1060 LYS   A CA  1 
ATOM   2709 C C   . LYS   A 1 448 ? -54.42400 26.20800  40.19600  1.000 52.55258  ? 1060 LYS   A C   1 
ATOM   2710 O O   . LYS   A 1 448 ? -53.46800 25.44800  40.38300  1.000 47.26729  ? 1060 LYS   A O   1 
ATOM   2711 C CB  . LYS   A 1 448 ? -55.75400 25.79400  38.11400  1.000 55.21258  ? 1060 LYS   A CB  1 
ATOM   2712 C CG  . LYS   A 1 448 ? -54.66900 24.97100  37.42200  1.000 51.89566  ? 1060 LYS   A CG  1 
ATOM   2713 C CD  . LYS   A 1 448 ? -54.59100 25.26800  35.93200  1.000 43.77295  ? 1060 LYS   A CD  1 
ATOM   2714 C CE  . LYS   A 1 448 ? -54.64400 26.76500  35.66000  1.000 46.73232  ? 1060 LYS   A CE  1 
ATOM   2715 N NZ  . LYS   A 1 448 ? -53.34600 27.43500  35.96100  1.000 56.42812  ? 1060 LYS   A NZ  1 
ATOM   2716 N N   . ASP   A 1 449 ? -54.36200 27.51400  40.46800  1.000 57.21034  ? 1061 ASP   A N   1 
ATOM   2717 C CA  . ASP   A 1 449 ? -53.17000 28.08600  41.08300  1.000 56.29759  ? 1061 ASP   A CA  1 
ATOM   2718 C C   . ASP   A 1 449 ? -52.92700 27.49000  42.46200  1.000 52.11643  ? 1061 ASP   A C   1 
ATOM   2719 O O   . ASP   A 1 449 ? -51.78900 27.16100  42.81600  1.000 53.19836  ? 1061 ASP   A O   1 
ATOM   2720 C CB  . ASP   A 1 449 ? -53.31000 29.60400  41.17600  1.000 55.88112  ? 1061 ASP   A CB  1 
ATOM   2721 C CG  . ASP   A 1 449 ? -53.27400 30.27600  39.81700  1.000 57.28595  ? 1061 ASP   A CG  1 
ATOM   2722 O OD1 . ASP   A 1 449 ? -52.72800 29.67900  38.86400  1.000 60.77350  ? 1061 ASP   A OD1 1 
ATOM   2723 O OD2 . ASP   A 1 449 ? -53.80400 31.39900  39.70100  1.000 50.43284  ? 1061 ASP   A OD2 1 
ATOM   2724 N N   . GLU   A 1 450 ? -53.99200 27.33400  43.25100  1.000 51.65875  ? 1062 GLU   A N   1 
ATOM   2725 C CA  . GLU   A 1 450 ? -53.85200 26.72600  44.56800  1.000 52.64943  ? 1062 GLU   A CA  1 
ATOM   2726 C C   . GLU   A 1 450 ? -53.56800 25.23400  44.46200  1.000 51.87441  ? 1062 GLU   A C   1 
ATOM   2727 O O   . GLU   A 1 450 ? -52.80500 24.68400  45.26400  1.000 52.12392  ? 1062 GLU   A O   1 
ATOM   2728 C CB  . GLU   A 1 450 ? -55.11500 26.97500  45.39000  1.000 52.75267  ? 1062 GLU   A CB  1 
ATOM   2729 C CG  . GLU   A 1 450 ? -55.25700 28.40300  45.89100  1.000 59.44286  ? 1062 GLU   A CG  1 
ATOM   2730 C CD  . GLU   A 1 450 ? -56.64400 28.68900  46.42800  1.000 58.03465  ? 1062 GLU   A CD  1 
ATOM   2731 O OE1 . GLU   A 1 450 ? -57.56300 27.88900  46.14500  1.000 53.29539  ? 1062 GLU   A OE1 1 
ATOM   2732 O OE2 . GLU   A 1 450 ? -56.81100 29.70700  47.13500  1.000 55.81407  ? 1062 GLU   A OE2 1 
ATOM   2733 N N   . ALA   A 1 451 ? -54.16800 24.56500  43.47100  1.000 45.61792  ? 1063 ALA   A N   1 
ATOM   2734 C CA  . ALA   A 1 451 ? -54.04500 23.11400  43.36700  1.000 43.22171  ? 1063 ALA   A CA  1 
ATOM   2735 C C   . ALA   A 1 451 ? -52.60600 22.68700  43.11200  1.000 47.28538  ? 1063 ALA   A C   1 
ATOM   2736 O O   . ALA   A 1 451 ? -52.14600 21.67800  43.65900  1.000 47.92100  ? 1063 ALA   A O   1 
ATOM   2737 C CB  . ALA   A 1 451 ? -54.95800 22.58700  42.26200  1.000 40.40381  ? 1063 ALA   A CB  1 
ATOM   2738 N N   . GLU   A 1 452 ? -51.88200 23.43000  42.27500  1.000 51.71912  ? 1064 GLU   A N   1 
ATOM   2739 C CA  . GLU   A 1 452 ? -50.49500 23.08600  41.99300  1.000 55.76659  ? 1064 GLU   A CA  1 
ATOM   2740 C C   . GLU   A 1 452 ? -49.51200 23.82400  42.88900  1.000 54.06322  ? 1064 GLU   A C   1 
ATOM   2741 O O   . GLU   A 1 452 ? -48.33700 23.44600  42.93200  1.000 53.24955  ? 1064 GLU   A O   1 
ATOM   2742 C CB  . GLU   A 1 452 ? -50.15500 23.32700  40.51100  1.000 56.87790  ? 1064 GLU   A CB  1 
ATOM   2743 C CG  . GLU   A 1 452 ? -50.55200 24.67700  39.94200  1.000 61.75913  ? 1064 GLU   A CG  1 
ATOM   2744 C CD  . GLU   A 1 452 ? -50.72900 24.63600  38.43100  1.000 62.85507  ? 1064 GLU   A CD  1 
ATOM   2745 O OE1 . GLU   A 1 452 ? -50.94600 23.53000  37.89000  1.000 62.45131  ? 1064 GLU   A OE1 1 
ATOM   2746 O OE2 . GLU   A 1 452 ? -50.65600 25.70500  37.78600  1.000 58.35001  ? 1064 GLU   A OE2 1 
ATOM   2747 N N   . LYS   A 1 453 ? -49.95500 24.85800  43.60700  1.000 55.53811  ? 1065 LYS   A N   1 
ATOM   2748 C CA  . LYS   A 1 453 ? -49.18700 25.28800  44.77000  1.000 58.63344  ? 1065 LYS   A CA  1 
ATOM   2749 C C   . LYS   A 1 453 ? -49.09300 24.15300  45.78000  1.000 51.93584  ? 1065 LYS   A C   1 
ATOM   2750 O O   . LYS   A 1 453 ? -48.02700 23.90300  46.35400  1.000 53.12371  ? 1065 LYS   A O   1 
ATOM   2751 C CB  . LYS   A 1 453 ? -49.81900 26.52400  45.41100  1.000 56.51154  ? 1065 LYS   A CB  1 
ATOM   2752 C CG  . LYS   A 1 453 ? -49.03000 27.06100  46.60200  1.000 62.69491  ? 1065 LYS   A CG  1 
ATOM   2753 C CD  . LYS   A 1 453 ? -49.64600 28.33400  47.16700  1.000 78.11148  ? 1065 LYS   A CD  1 
ATOM   2754 C CE  . LYS   A 1 453 ? -50.87000 28.02700  48.03000  1.000 80.15331  ? 1065 LYS   A CE  1 
ATOM   2755 N NZ  . LYS   A 1 453 ? -50.52600 27.37100  49.32700  1.000 62.31374  ? 1065 LYS   A NZ  1 
ATOM   2756 N N   . LEU   A 1 454 ? -50.20100 23.44100  45.98800  1.000 47.37160  ? 1066 LEU   A N   1 
ATOM   2757 C CA  . LEU   A 1 454 ? -50.17500 22.24100  46.81300  1.000 49.06519  ? 1066 LEU   A CA  1 
ATOM   2758 C C   . LEU   A 1 454 ? -49.33700 21.15000  46.16000  1.000 47.94197  ? 1066 LEU   A C   1 
ATOM   2759 O O   . LEU   A 1 454 ? -48.53700 20.48800  46.83100  1.000 49.13777  ? 1066 LEU   A O   1 
ATOM   2760 C CB  . LEU   A 1 454 ? -51.60300 21.74600  47.05300  1.000 55.97338  ? 1066 LEU   A CB  1 
ATOM   2761 C CG  . LEU   A 1 454 ? -52.43900 22.42900  48.14200  1.000 56.61745  ? 1066 LEU   A CG  1 
ATOM   2762 C CD1 . LEU   A 1 454 ? -53.70700 21.63400  48.42300  1.000 51.15240  ? 1066 LEU   A CD1 1 
ATOM   2763 C CD2 . LEU   A 1 454 ? -51.62800 22.62600  49.41400  1.000 53.79217  ? 1066 LEU   A CD2 1 
ATOM   2764 N N   . PHE   A 1 455 ? -49.50700 20.95300  44.84800  1.000 50.10674  ? 1067 PHE   A N   1 
ATOM   2765 C CA  . PHE   A 1 455 ? -48.77500 19.90400  44.14000  1.000 53.26267  ? 1067 PHE   A CA  1 
ATOM   2766 C C   . PHE   A 1 455 ? -47.26800 20.09900  44.23900  1.000 50.61563  ? 1067 PHE   A C   1 
ATOM   2767 O O   . PHE   A 1 455 ? -46.52200 19.12900  44.41700  1.000 45.21655  ? 1067 PHE   A O   1 
ATOM   2768 C CB  . PHE   A 1 455 ? -49.20500 19.86300  42.67300  1.000 49.63776  ? 1067 PHE   A CB  1 
ATOM   2769 C CG  . PHE   A 1 455 ? -48.37700 18.93800  41.82500  1.000 47.49698  ? 1067 PHE   A CG  1 
ATOM   2770 C CD1 . PHE   A 1 455 ? -48.49800 17.56500  41.95100  1.000 50.33042  ? 1067 PHE   A CD1 1 
ATOM   2771 C CD2 . PHE   A 1 455 ? -47.47800 19.44400  40.89900  1.000 45.59830  ? 1067 PHE   A CD2 1 
ATOM   2772 C CE1 . PHE   A 1 455 ? -47.74000 16.71100  41.16600  1.000 49.98486  ? 1067 PHE   A CE1 1 
ATOM   2773 C CE2 . PHE   A 1 455 ? -46.71500 18.59700  40.11800  1.000 41.18296  ? 1067 PHE   A CE2 1 
ATOM   2774 C CZ  . PHE   A 1 455 ? -46.84700 17.22900  40.25100  1.000 46.30158  ? 1067 PHE   A CZ  1 
ATOM   2775 N N   . ASN   A 1 456 ? -46.79600 21.34000  44.10700  1.000 49.16599  ? 1068 ASN   A N   1 
ATOM   2776 C CA  . ASN   A 1 456 ? -45.37000 21.59300  44.26900  1.000 49.64585  ? 1068 ASN   A CA  1 
ATOM   2777 C C   . ASN   A 1 456 ? -44.91100 21.21600  45.67000  1.000 55.47808  ? 1068 ASN   A C   1 
ATOM   2778 O O   . ASN   A 1 456 ? -43.82800 20.64700  45.84900  1.000 55.50153  ? 1068 ASN   A O   1 
ATOM   2779 C CB  . ASN   A 1 456 ? -45.05900 23.05900  43.97400  1.000 56.51437  ? 1068 ASN   A CB  1 
ATOM   2780 C CG  . ASN   A 1 456 ? -43.60400 23.40500  44.22800  1.000 74.15881  ? 1068 ASN   A CG  1 
ATOM   2781 O OD1 . ASN   A 1 456 ? -43.28000 24.11700  45.18000  1.000 80.88411  ? 1068 ASN   A OD1 1 
ATOM   2782 N ND2 . ASN   A 1 456 ? -42.71600 22.89800  43.37700  1.000 60.96279  ? 1068 ASN   A ND2 1 
ATOM   2783 N N   . GLN   A 1 457 ? -45.73500 21.51500  46.67600  1.000 56.93064  ? 1069 GLN   A N   1 
ATOM   2784 C CA  . GLN   A 1 457 ? -45.41500 21.12200  48.04200  1.000 53.06990  ? 1069 GLN   A CA  1 
ATOM   2785 C C   . GLN   A 1 457 ? -45.47500 19.60800  48.20700  1.000 52.61147  ? 1069 GLN   A C   1 
ATOM   2786 O O   . GLN   A 1 457 ? -44.60000 19.01300  48.84600  1.000 62.50128  ? 1069 GLN   A O   1 
ATOM   2787 C CB  . GLN   A 1 457 ? -46.37000 21.81500  49.01400  1.000 49.80517  ? 1069 GLN   A CB  1 
ATOM   2788 C CG  . GLN   A 1 457 ? -46.23000 23.33400  49.04000  1.000 47.63485  ? 1069 GLN   A CG  1 
ATOM   2789 C CD  . GLN   A 1 457 ? -47.35700 24.02500  49.79400  1.000 59.39687  ? 1069 GLN   A CD  1 
ATOM   2790 O OE1 . GLN   A 1 457 ? -48.20200 23.37400  50.41500  1.000 64.88120  ? 1069 GLN   A OE1 1 
ATOM   2791 N NE2 . GLN   A 1 457 ? -47.37200 25.35400  49.74200  1.000 52.05997  ? 1069 GLN   A NE2 1 
ATOM   2792 N N   . ASP   A 1 458 ? -46.48700 18.96400  47.61800  1.000 45.26704  ? 1070 ASP   A N   1 
ATOM   2793 C CA  . ASP   A 1 458 ? -46.66500 17.52800  47.80700  1.000 48.52311  ? 1070 ASP   A CA  1 
ATOM   2794 C C   . ASP   A 1 458 ? -45.57000 16.71100  47.12700  1.000 59.21008  ? 1070 ASP   A C   1 
ATOM   2795 O O   . ASP   A 1 458 ? -45.26900 15.59900  47.57300  1.000 63.16546  ? 1070 ASP   A O   1 
ATOM   2796 C CB  . ASP   A 1 458 ? -48.04000 17.10100  47.29700  1.000 50.14902  ? 1070 ASP   A CB  1 
ATOM   2797 C CG  . ASP   A 1 458 ? -49.16700 17.66100  48.13800  1.000 54.87302  ? 1070 ASP   A CG  1 
ATOM   2798 O OD1 . ASP   A 1 458 ? -48.95600 17.88600  49.34600  1.000 59.44432  ? 1070 ASP   A OD1 1 
ATOM   2799 O OD2 . ASP   A 1 458 ? -50.26100 17.88700  47.58900  1.000 56.92410  ? 1070 ASP   A OD2 1 
ATOM   2800 N N   . VAL   A 1 459 ? -44.97400 17.22600  46.04800  1.000 63.43437  ? 1071 VAL   A N   1 
ATOM   2801 C CA  . VAL   A 1 459 ? -43.86500 16.51500  45.41400  1.000 64.86071  ? 1071 VAL   A CA  1 
ATOM   2802 C C   . VAL   A 1 459 ? -42.60800 16.62300  46.26800  1.000 62.12895  ? 1071 VAL   A C   1 
ATOM   2803 O O   . VAL   A 1 459 ? -41.84200 15.65800  46.40100  1.000 59.53397  ? 1071 VAL   A O   1 
ATOM   2804 C CB  . VAL   A 1 459 ? -43.62600 17.04100  43.98700  1.000 63.10749  ? 1071 VAL   A CB  1 
ATOM   2805 C CG1 . VAL   A 1 459 ? -42.42800 16.34600  43.35800  1.000 57.51684  ? 1071 VAL   A CG1 1 
ATOM   2806 C CG2 . VAL   A 1 459 ? -44.85600 16.81900  43.13500  1.000 55.06980  ? 1071 VAL   A CG2 1 
ATOM   2807 N N   . ASP   A 1 460 ? -42.37500 17.79900  46.85600  1.000 58.50372  ? 1072 ASP   A N   1 
ATOM   2808 C CA  . ASP   A 1 460 ? -41.26600 17.97200  47.78800  1.000 63.33288  ? 1072 ASP   A CA  1 
ATOM   2809 C C   . ASP   A 1 460 ? -41.31300 16.94800  48.91400  1.000 71.17194  ? 1072 ASP   A C   1 
ATOM   2810 O O   . ASP   A 1 460 ? -40.27100 16.49900  49.40400  1.000 70.65311  ? 1072 ASP   A O   1 
ATOM   2811 C CB  . ASP   A 1 460 ? -41.29800 19.38400  48.36600  1.000 64.93196  ? 1072 ASP   A CB  1 
ATOM   2812 C CG  . ASP   A 1 460 ? -40.48900 19.50300  49.63000  1.000 78.21761  ? 1072 ASP   A CG  1 
ATOM   2813 O OD1 . ASP   A 1 460 ? -39.24900 19.58800  49.52300  1.000 91.27785  ? 1072 ASP   A OD1 1 
ATOM   2814 O OD2 . ASP   A 1 460 ? -41.08800 19.49100  50.72900  1.000 70.75194  ? 1072 ASP   A OD2 1 
ATOM   2815 N N   . ALA   A 1 461 ? -42.51700 16.58300  49.35500  1.000 68.99992  ? 1073 ALA   A N   1 
ATOM   2816 C CA  . ALA   A 1 461 ? -42.65100 15.55100  50.37600  1.000 65.04390  ? 1073 ALA   A CA  1 
ATOM   2817 C C   . ALA   A 1 461 ? -42.12800 14.21200  49.86600  1.000 66.83021  ? 1073 ALA   A C   1 
ATOM   2818 O O   . ALA   A 1 461 ? -41.23600 13.60600  50.47000  1.000 70.76377  ? 1073 ALA   A O   1 
ATOM   2819 C CB  . ALA   A 1 461 ? -44.11200 15.43900  50.81300  1.000 62.36747  ? 1073 ALA   A CB  1 
ATOM   2820 N N   . ALA   A 1 462 ? -42.65700 13.75200  48.72800  1.000 73.46339  ? 1074 ALA   A N   1 
ATOM   2821 C CA  . ALA   A 1 462 ? -42.35200 12.41400  48.22700  1.000 77.30783  ? 1074 ALA   A CA  1 
ATOM   2822 C C   . ALA   A 1 462 ? -40.86200 12.18600  47.99500  1.000 77.75687  ? 1074 ALA   A C   1 
ATOM   2823 O O   . ALA   A 1 462 ? -40.43000 11.02800  47.92800  1.000 75.48398  ? 1074 ALA   A O   1 
ATOM   2824 C CB  . ALA   A 1 462 ? -43.12500 12.15600  46.93100  1.000 72.09900  ? 1074 ALA   A CB  1 
ATOM   2825 N N   . VAL   A 1 463 ? -40.06700 13.24700  47.86800  1.000 75.39205  ? 1075 VAL   A N   1 
ATOM   2826 C CA  . VAL   A 1 463 ? -38.62200 13.07600  47.74000  1.000 75.85521  ? 1075 VAL   A CA  1 
ATOM   2827 C C   . VAL   A 1 463 ? -37.94500 13.08100  49.10600  1.000 80.04958  ? 1075 VAL   A C   1 
ATOM   2828 O O   . VAL   A 1 463 ? -37.03900 12.28400  49.35400  1.000 81.41417  ? 1075 VAL   A O   1 
ATOM   2829 C CB  . VAL   A 1 463 ? -38.01900 14.14800  46.80200  1.000 79.85269  ? 1075 VAL   A CB  1 
ATOM   2830 C CG1 . VAL   A 1 463 ? -38.60000 14.02600  45.40000  1.000 82.33919  ? 1075 VAL   A CG1 1 
ATOM   2831 C CG2 . VAL   A 1 463 ? -38.21100 15.55500  47.34400  1.000 72.64694  ? 1075 VAL   A CG2 1 
ATOM   2832 N N   . ARG   A 1 464 ? -38.37400 13.95700  50.02100  1.000 80.11170  ? 1076 ARG   A N   1 
ATOM   2833 C CA  . ARG   A 1 464 ? -37.78100 13.97100  51.35500  1.000 80.13070  ? 1076 ARG   A CA  1 
ATOM   2834 C C   . ARG   A 1 464 ? -38.17800 12.73700  52.15400  1.000 76.29775  ? 1076 ARG   A C   1 
ATOM   2835 O O   . ARG   A 1 464 ? -37.37800 12.23000  52.94800  1.000 77.72474  ? 1076 ARG   A O   1 
ATOM   2836 C CB  . ARG   A 1 464 ? -38.19000 15.23900  52.10600  1.000 78.85278  ? 1076 ARG   A CB  1 
ATOM   2837 C CG  . ARG   A 1 464 ? -37.42000 16.48700  51.70200  1.000 79.00901  ? 1076 ARG   A CG  1 
ATOM   2838 C CD  . ARG   A 1 464 ? -38.14700 17.74200  52.16400  1.000 76.72993  ? 1076 ARG   A CD  1 
ATOM   2839 N NE  . ARG   A 1 464 ? -37.32200 18.93900  52.04600  1.000 76.13489  ? 1076 ARG   A NE  1 
ATOM   2840 C CZ  . ARG   A 1 464 ? -37.79200 20.17800  52.09500  1.000 78.84841  ? 1076 ARG   A CZ  1 
ATOM   2841 N NH1 . ARG   A 1 464 ? -39.08200 20.42200  52.26400  1.000 76.67391  ? 1076 ARG   A NH1 1 
ATOM   2842 N NH2 . ARG   A 1 464 ? -36.94800 21.19900  51.97000  1.000 71.64054  ? 1076 ARG   A NH2 1 
ATOM   2843 N N   . GLY   A 1 465 ? -39.40100 12.24400  51.95700  1.000 78.34639  ? 1077 GLY   A N   1 
ATOM   2844 C CA  . GLY   A 1 465 ? -39.86200 11.03200  52.61200  1.000 85.55253  ? 1077 GLY   A CA  1 
ATOM   2845 C C   . GLY   A 1 465 ? -39.19900 9.76600   52.12300  1.000 87.74666  ? 1077 GLY   A C   1 
ATOM   2846 O O   . GLY   A 1 465 ? -39.38300 8.71100   52.74000  1.000 90.60295  ? 1077 GLY   A O   1 
ATOM   2847 N N   . ILE   A 1 466 ? -38.44700 9.84100   51.02600  1.000 87.00410  ? 1078 ILE   A N   1 
ATOM   2848 C CA  . ILE   A 1 466 ? -37.63900 8.71300   50.58200  1.000 86.78921  ? 1078 ILE   A CA  1 
ATOM   2849 C C   . ILE   A 1 466 ? -36.15900 8.93600   50.88500  1.000 88.96175  ? 1078 ILE   A C   1 
ATOM   2850 O O   . ILE   A 1 466 ? -35.38300 7.96700   50.88400  1.000 82.55737  ? 1078 ILE   A O   1 
ATOM   2851 C CB  . ILE   A 1 466 ? -37.85900 8.42600   49.08000  1.000 86.73787  ? 1078 ILE   A CB  1 
ATOM   2852 C CG1 . ILE   A 1 466 ? -37.31100 7.05000   48.75000  1.000 90.25830  ? 1078 ILE   A CG1 1 
ATOM   2853 C CG2 . ILE   A 1 466 ? -37.17700 9.46800   48.21500  1.000 81.88134  ? 1078 ILE   A CG2 1 
ATOM   2854 C CD1 . ILE   A 1 466 ? -37.84700 6.03300   49.69200  1.000 80.66252  ? 1078 ILE   A CD1 1 
ATOM   2855 N N   . LEU   A 1 467 ? -35.75100 10.17900  51.16300  1.000 89.47292  ? 1079 LEU   A N   1 
ATOM   2856 C CA  . LEU   A 1 467 ? -34.41700 10.45100  51.68300  1.000 86.33086  ? 1079 LEU   A CA  1 
ATOM   2857 C C   . LEU   A 1 467 ? -34.18900 9.79500   53.03900  1.000 93.71833  ? 1079 LEU   A C   1 
ATOM   2858 O O   . LEU   A 1 467 ? -33.03700 9.56500   53.42200  1.000 97.88588  ? 1079 LEU   A O   1 
ATOM   2859 C CB  . LEU   A 1 467 ? -34.21300 11.96300  51.81900  1.000 76.74629  ? 1079 LEU   A CB  1 
ATOM   2860 C CG  . LEU   A 1 467 ? -34.24700 12.81600  50.55100  1.000 74.39980  ? 1079 LEU   A CG  1 
ATOM   2861 C CD1 . LEU   A 1 467 ? -33.63200 14.18500  50.79200  1.000 80.65911  ? 1079 LEU   A CD1 1 
ATOM   2862 C CD2 . LEU   A 1 467 ? -33.54300 12.10000  49.41500  1.000 66.43259  ? 1079 LEU   A CD2 1 
ATOM   2863 N N   . ARG   A 1 468 ? -35.26500 9.48500   53.76400  1.000 87.84042  ? 1080 ARG   A N   1 
ATOM   2864 C CA  . ARG   A 1 468 ? -35.19800 9.11500   55.17200  1.000 85.58206  ? 1080 ARG   A CA  1 
ATOM   2865 C C   . ARG   A 1 468 ? -35.71700 7.70900   55.45100  1.000 90.31662  ? 1080 ARG   A C   1 
ATOM   2866 O O   . ARG   A 1 468 ? -35.91600 7.35800   56.62100  1.000 102.87483 ? 1080 ARG   A O   1 
ATOM   2867 C CB  . ARG   A 1 468 ? -35.98800 10.14000  55.99900  1.000 85.18483  ? 1080 ARG   A CB  1 
ATOM   2868 C CG  . ARG   A 1 468 ? -37.49000 9.88100   56.01800  1.000 84.29558  ? 1080 ARG   A CG  1 
ATOM   2869 C CD  . ARG   A 1 468 ? -38.28500 11.05900  56.54700  1.000 85.96837  ? 1080 ARG   A CD  1 
ATOM   2870 N NE  . ARG   A 1 468 ? -39.69900 10.93100  56.21000  1.000 87.37412  ? 1080 ARG   A NE  1 
ATOM   2871 C CZ  . ARG   A 1 468 ? -40.59200 10.29200  56.95500  1.000 96.26044  ? 1080 ARG   A CZ  1 
ATOM   2872 N NH1 . ARG   A 1 468 ? -40.26000 9.73300   58.10800  1.000 97.07533  ? 1080 ARG   A NH1 1 
ATOM   2873 N NH2 . ARG   A 1 468 ? -41.84900 10.20400  56.52900  1.000 96.41887  ? 1080 ARG   A NH2 1 
ATOM   2874 N N   . ASN   A 1 469 ? -35.91700 6.88500   54.42700  1.000 82.30074  ? 1081 ASN   A N   1 
ATOM   2875 C CA  . ASN   A 1 469 ? -36.66200 5.63500   54.58000  1.000 86.91066  ? 1081 ASN   A CA  1 
ATOM   2876 C C   . ASN   A 1 469 ? -35.76700 4.42100   54.32500  1.000 92.80343  ? 1081 ASN   A C   1 
ATOM   2877 O O   . ASN   A 1 469 ? -35.66900 3.93700   53.19500  1.000 88.44004  ? 1081 ASN   A O   1 
ATOM   2878 C CB  . ASN   A 1 469 ? -37.87600 5.63500   53.64900  1.000 92.08715  ? 1081 ASN   A CB  1 
ATOM   2879 C CG  . ASN   A 1 469 ? -38.67400 4.34900   53.73100  1.000 95.38397  ? 1081 ASN   A CG  1 
ATOM   2880 O OD1 . ASN   A 1 469 ? -38.43500 3.40600   52.97700  1.000 91.48994  ? 1081 ASN   A OD1 1 
ATOM   2881 N ND2 . ASN   A 1 469 ? -39.63300 4.30600   54.65100  1.000 101.21793 ? 1081 ASN   A ND2 1 
ATOM   2882 N N   . ALA   A 1 470 ? -35.13200 3.92800   55.39400  1.000 101.67400 ? 1082 ALA   A N   1 
ATOM   2883 C CA  . ALA   A 1 470 ? -34.47600 2.62000   55.43500  1.000 99.37318  ? 1082 ALA   A CA  1 
ATOM   2884 C C   . ALA   A 1 470 ? -33.61100 2.31800   54.21800  1.000 91.24209  ? 1082 ALA   A C   1 
ATOM   2885 O O   . ALA   A 1 470 ? -32.84900 3.17300   53.75600  1.000 91.01253  ? 1082 ALA   A O   1 
ATOM   2886 C CB  . ALA   A 1 470 ? -35.52600 1.51800   55.59600  1.000 95.95923  ? 1082 ALA   A CB  1 
ATOM   2887 N N   . LYS   A 1 471 ? -33.72400 1.09300   53.69900  1.000 92.17085  ? 1083 LYS   A N   1 
ATOM   2888 C CA  . LYS   A 1 471 ? -32.96900 0.67900   52.52200  1.000 102.98329 ? 1083 LYS   A CA  1 
ATOM   2889 C C   . LYS   A 1 471 ? -33.51500 1.26800   51.22800  1.000 107.22559 ? 1083 LYS   A C   1 
ATOM   2890 O O   . LYS   A 1 471 ? -32.95800 0.97700   50.16200  1.000 105.27432 ? 1083 LYS   A O   1 
ATOM   2891 C CB  . LYS   A 1 471 ? -32.94800 -0.84900  52.40800  1.000 96.37582  ? 1083 LYS   A CB  1 
ATOM   2892 C CG  . LYS   A 1 471 ? -31.97300 -1.55400  53.33900  1.000 91.57799  ? 1083 LYS   A CG  1 
ATOM   2893 C CD  . LYS   A 1 471 ? -31.69600 -2.96600  52.84200  1.000 94.33624  ? 1083 LYS   A CD  1 
ATOM   2894 C CE  . LYS   A 1 471 ? -32.85100 -3.90800  53.14700  1.000 95.87451  ? 1083 LYS   A CE  1 
ATOM   2895 N NZ  . LYS   A 1 471 ? -32.51600 -5.32500  52.82600  1.000 92.52755  ? 1083 LYS   A NZ  1 
ATOM   2896 N N   . LEU   A 1 472 ? -34.57100 2.08000   51.28300  1.000 106.34821 ? 1084 LEU   A N   1 
ATOM   2897 C CA  . LEU   A 1 472 ? -35.19100 2.62400   50.08100  1.000 101.82898 ? 1084 LEU   A CA  1 
ATOM   2898 C C   . LEU   A 1 472 ? -34.56800 3.94000   49.62300  1.000 96.69881  ? 1084 LEU   A C   1 
ATOM   2899 O O   . LEU   A 1 472 ? -35.04900 4.52900   48.65000  1.000 90.65411  ? 1084 LEU   A O   1 
ATOM   2900 C CB  . LEU   A 1 472 ? -36.70100 2.79200   50.29700  1.000 105.70009 ? 1084 LEU   A CB  1 
ATOM   2901 C CG  . LEU   A 1 472 ? -37.54900 2.62400   49.03300  1.000 93.67285  ? 1084 LEU   A CG  1 
ATOM   2902 C CD1 . LEU   A 1 472 ? -37.31300 1.25900   48.47200  1.000 93.89696  ? 1084 LEU   A CD1 1 
ATOM   2903 C CD2 . LEU   A 1 472 ? -39.02500 2.81500   49.32300  1.000 81.09855  ? 1084 LEU   A CD2 1 
ATOM   2904 N N   . LYS   A 1 473 ? -33.51100 4.40700   50.28900  1.000 94.99376  ? 1085 LYS   A N   1 
ATOM   2905 C CA  . LYS   A 1 473 ? -32.71200 5.52000   49.78700  1.000 94.01430  ? 1085 LYS   A CA  1 
ATOM   2906 C C   . LYS   A 1 473 ? -31.59900 5.00100   48.87100  1.000 100.53213 ? 1085 LYS   A C   1 
ATOM   2907 O O   . LYS   A 1 473 ? -31.37700 5.58600   47.80400  1.000 98.13671  ? 1085 LYS   A O   1 
ATOM   2908 C CB  . LYS   A 1 473 ? -32.15200 6.35400   50.94900  1.000 86.30210  ? 1085 LYS   A CB  1 
ATOM   2909 C CG  . LYS   A 1 473 ? -31.43300 7.64900   50.55400  1.000 81.56991  ? 1085 LYS   A CG  1 
ATOM   2910 C CD  . LYS   A 1 473 ? -29.96600 7.41500   50.21800  1.000 89.36034  ? 1085 LYS   A CD  1 
ATOM   2911 C CE  . LYS   A 1 473 ? -29.25000 8.71000   49.89600  1.000 86.40606  ? 1085 LYS   A CE  1 
ATOM   2912 N NZ  . LYS   A 1 473 ? -27.95100 8.42800   49.22900  1.000 88.15789  ? 1085 LYS   A NZ  1 
ATOM   2913 N N   . PRO   A 1 474 ? -30.86900 3.93200   49.23200  1.000 105.33957 ? 1086 PRO   A N   1 
ATOM   2914 C CA  . PRO   A 1 474 ? -29.84500 3.42200   48.30100  1.000 102.25931 ? 1086 PRO   A CA  1 
ATOM   2915 C C   . PRO   A 1 474 ? -30.38500 3.00600   46.94100  1.000 98.99856  ? 1086 PRO   A C   1 
ATOM   2916 O O   . PRO   A 1 474 ? -29.66900 3.15000   45.94200  1.000 101.87942 ? 1086 PRO   A O   1 
ATOM   2917 C CB  . PRO   A 1 474 ? -29.25100 2.22700   49.05700  1.000 108.14945 ? 1086 PRO   A CB  1 
ATOM   2918 C CG  . PRO   A 1 474 ? -29.41600 2.58100   50.47800  1.000 107.57263 ? 1086 PRO   A CG  1 
ATOM   2919 C CD  . PRO   A 1 474 ? -30.73100 3.30700   50.56400  1.000 100.84350 ? 1086 PRO   A CD  1 
ATOM   2920 N N   . VAL   A 1 475 ? -31.61500 2.48600   46.86300  1.000 94.62683  ? 1087 VAL   A N   1 
ATOM   2921 C CA  . VAL   A 1 475 ? -32.17100 2.14700   45.55500  1.000 97.76385  ? 1087 VAL   A CA  1 
ATOM   2922 C C   . VAL   A 1 475 ? -32.44900 3.41100   44.75300  1.000 96.07228  ? 1087 VAL   A C   1 
ATOM   2923 O O   . VAL   A 1 475 ? -32.36700 3.40200   43.51700  1.000 92.03499  ? 1087 VAL   A O   1 
ATOM   2924 C CB  . VAL   A 1 475 ? -33.44500 1.29100   45.69300  1.000 84.11825  ? 1087 VAL   A CB  1 
ATOM   2925 C CG1 . VAL   A 1 475 ? -33.09700 -0.17000  45.91000  1.000 81.40980  ? 1087 VAL   A CG1 1 
ATOM   2926 C CG2 . VAL   A 1 475 ? -34.30400 1.81100   46.80600  1.000 89.41921  ? 1087 VAL   A CG2 1 
ATOM   2927 N N   . TYR   A 1 476 ? -32.77600 4.51400   45.43600  1.000 92.88347  ? 1088 TYR   A N   1 
ATOM   2928 C CA  . TYR   A 1 476 ? -33.04400 5.77500   44.74900  1.000 91.94844  ? 1088 TYR   A CA  1 
ATOM   2929 C C   . TYR   A 1 476 ? -31.81400 6.26000   43.98700  1.000 96.76473  ? 1088 TYR   A C   1 
ATOM   2930 O O   . TYR   A 1 476 ? -31.89900 6.60500   42.80200  1.000 95.68844  ? 1088 TYR   A O   1 
ATOM   2931 C CB  . TYR   A 1 476 ? -33.51600 6.82600   45.75800  1.000 89.30024  ? 1088 TYR   A CB  1 
ATOM   2932 C CG  . TYR   A 1 476 ? -33.77300 8.19100   45.15700  1.000 90.13276  ? 1088 TYR   A CG  1 
ATOM   2933 C CD1 . TYR   A 1 476 ? -34.91800 8.43800   44.40600  1.000 88.70020  ? 1088 TYR   A CD1 1 
ATOM   2934 C CD2 . TYR   A 1 476 ? -32.87200 9.23400   45.34200  1.000 89.38400  ? 1088 TYR   A CD2 1 
ATOM   2935 C CE1 . TYR   A 1 476 ? -35.15500 9.68400   43.85300  1.000 87.26811  ? 1088 TYR   A CE1 1 
ATOM   2936 C CE2 . TYR   A 1 476 ? -33.10000 10.48400  44.79400  1.000 90.29212  ? 1088 TYR   A CE2 1 
ATOM   2937 C CZ  . TYR   A 1 476 ? -34.24400 10.70300  44.04900  1.000 93.55035  ? 1088 TYR   A CZ  1 
ATOM   2938 O OH  . TYR   A 1 476 ? -34.47800 11.94400  43.50000  1.000 98.91566  ? 1088 TYR   A OH  1 
ATOM   2939 N N   . ASP   A 1 477 ? -30.65500 6.28400   44.64900  1.000 94.98188  ? 1089 ASP   A N   1 
ATOM   2940 C CA  . ASP   A 1 477 ? -29.42000 6.69700   43.99400  1.000 94.63407  ? 1089 ASP   A CA  1 
ATOM   2941 C C   . ASP   A 1 477 ? -28.78200 5.58700   43.16800  1.000 98.84896  ? 1089 ASP   A C   1 
ATOM   2942 O O   . ASP   A 1 477 ? -27.82800 5.85700   42.42900  1.000 98.30901  ? 1089 ASP   A O   1 
ATOM   2943 C CB  . ASP   A 1 477 ? -28.42800 7.21300   45.03600  1.000 94.34999  ? 1089 ASP   A CB  1 
ATOM   2944 C CG  . ASP   A 1 477 ? -29.06300 8.18800   45.99900  1.000 99.26064  ? 1089 ASP   A CG  1 
ATOM   2945 O OD1 . ASP   A 1 477 ? -29.69600 7.72900   46.97100  1.000 95.23919  ? 1089 ASP   A OD1 1 
ATOM   2946 O OD2 . ASP   A 1 477 ? -28.93700 9.41100   45.77600  1.000 103.54942 ? 1089 ASP   A OD2 1 
ATOM   2947 N N   . SER   A 1 478 ? -29.27800 4.35100   43.27300  1.000 95.90452  ? 1090 SER   A N   1 
ATOM   2948 C CA  . SER   A 1 478 ? -28.82000 3.29000   42.38500  1.000 93.83583  ? 1090 SER   A CA  1 
ATOM   2949 C C   . SER   A 1 478 ? -29.37800 3.44300   40.97700  1.000 97.25420  ? 1090 SER   A C   1 
ATOM   2950 O O   . SER   A 1 478 ? -28.83300 2.85200   40.03800  1.000 101.08149 ? 1090 SER   A O   1 
ATOM   2951 C CB  . SER   A 1 478 ? -29.21000 1.92000   42.94400  1.000 93.10622  ? 1090 SER   A CB  1 
ATOM   2952 O OG  . SER   A 1 478 ? -28.91200 0.89000   42.01600  1.000 96.86292  ? 1090 SER   A OG  1 
ATOM   2953 N N   . LEU   A 1 479 ? -30.44200 4.22200   40.81400  1.000 95.29228  ? 1091 LEU   A N   1 
ATOM   2954 C CA  . LEU   A 1 479 ? -31.12300 4.39400   39.54100  1.000 86.26423  ? 1091 LEU   A CA  1 
ATOM   2955 C C   . LEU   A 1 479 ? -30.84000 5.77600   38.96500  1.000 87.02314  ? 1091 LEU   A C   1 
ATOM   2956 O O   . LEU   A 1 479 ? -30.32500 6.67400   39.64000  1.000 81.61905  ? 1091 LEU   A O   1 
ATOM   2957 C CB  . LEU   A 1 479 ? -32.63200 4.17800   39.70500  1.000 82.67539  ? 1091 LEU   A CB  1 
ATOM   2958 C CG  . LEU   A 1 479 ? -33.05100 2.78400   40.18300  1.000 87.39032  ? 1091 LEU   A CG  1 
ATOM   2959 C CD1 . LEU   A 1 479 ? -34.50500 2.77700   40.63300  1.000 77.57767  ? 1091 LEU   A CD1 1 
ATOM   2960 C CD2 . LEU   A 1 479 ? -32.81900 1.74700   39.09100  1.000 86.16483  ? 1091 LEU   A CD2 1 
ATOM   2961 N N   . ASP   A 1 480 ? -31.19400 5.93000   37.69000  1.000 91.38203  ? 1092 ASP   A N   1 
ATOM   2962 C CA  . ASP   A 1 480 ? -30.97700 7.15100   36.93200  1.000 83.39144  ? 1092 ASP   A CA  1 
ATOM   2963 C C   . ASP   A 1 480 ? -32.16800 8.09600   37.08300  1.000 78.14816  ? 1092 ASP   A C   1 
ATOM   2964 O O   . ASP   A 1 480 ? -33.17400 7.77500   37.71900  1.000 81.37204  ? 1092 ASP   A O   1 
ATOM   2965 C CB  . ASP   A 1 480 ? -30.71600 6.81300   35.46500  1.000 71.51673  ? 1092 ASP   A CB  1 
ATOM   2966 C CG  . ASP   A 1 480 ? -31.59800 5.68600   34.96000  1.000 70.88912  ? 1092 ASP   A CG  1 
ATOM   2967 O OD1 . ASP   A 1 480 ? -32.45900 5.20900   35.72800  1.000 71.36731  ? 1092 ASP   A OD1 1 
ATOM   2968 O OD2 . ASP   A 1 480 ? -31.42100 5.26500   33.79900  1.000 82.84068  ? 1092 ASP   A OD2 1 
ATOM   2969 N N   . ALA   A 1 481 ? -32.05500 9.27700   36.46900  1.000 74.51279  ? 1093 ALA   A N   1 
ATOM   2970 C CA  . ALA   A 1 481 ? -33.06000 10.31800  36.66000  1.000 69.97468  ? 1093 ALA   A CA  1 
ATOM   2971 C C   . ALA   A 1 481 ? -34.43100 9.87800   36.15800  1.000 76.32847  ? 1093 ALA   A C   1 
ATOM   2972 O O   . ALA   A 1 481 ? -35.45600 10.22300  36.75900  1.000 87.24346  ? 1093 ALA   A O   1 
ATOM   2973 C CB  . ALA   A 1 481 ? -32.62000 11.60500  35.96200  1.000 59.19188  ? 1093 ALA   A CB  1 
ATOM   2974 N N   . VAL   A 1 482 ? -34.47300 9.11000   35.06600  1.000 73.25612  ? 1094 VAL   A N   1 
ATOM   2975 C CA  . VAL   A 1 482 ? -35.75100 8.70100   34.48600  1.000 78.31945  ? 1094 VAL   A CA  1 
ATOM   2976 C C   . VAL   A 1 482 ? -36.42000 7.59100   35.29600  1.000 78.61569  ? 1094 VAL   A C   1 
ATOM   2977 O O   . VAL   A 1 482 ? -37.64600 7.43000   35.22300  1.000 78.31185  ? 1094 VAL   A O   1 
ATOM   2978 C CB  . VAL   A 1 482 ? -35.54500 8.29100   33.01400  1.000 85.86256  ? 1094 VAL   A CB  1 
ATOM   2979 C CG1 . VAL   A 1 482 ? -34.46200 7.22200   32.89500  1.000 88.11785  ? 1094 VAL   A CG1 1 
ATOM   2980 C CG2 . VAL   A 1 482 ? -36.85800 7.85500   32.35000  1.000 73.42297  ? 1094 VAL   A CG2 1 
ATOM   2981 N N   . ARG   A 1 483 ? -35.65800 6.83300   36.08700  1.000 81.04499  ? 1095 ARG   A N   1 
ATOM   2982 C CA  . ARG   A 1 483 ? -36.24000 5.84900   36.99300  1.000 79.31146  ? 1095 ARG   A CA  1 
ATOM   2983 C C   . ARG   A 1 483 ? -36.40900 6.37200   38.41200  1.000 72.46717  ? 1095 ARG   A C   1 
ATOM   2984 O O   . ARG   A 1 483 ? -37.21600 5.81700   39.16600  1.000 70.33222  ? 1095 ARG   A O   1 
ATOM   2985 C CB  . ARG   A 1 483 ? -35.38900 4.57600   37.02200  1.000 77.83869  ? 1095 ARG   A CB  1 
ATOM   2986 C CG  . ARG   A 1 483 ? -35.65800 3.64900   35.85000  1.000 78.68541  ? 1095 ARG   A CG  1 
ATOM   2987 C CD  . ARG   A 1 483 ? -34.69500 2.48400   35.83700  1.000 79.71628  ? 1095 ARG   A CD  1 
ATOM   2988 N NE  . ARG   A 1 483 ? -34.72900 1.76700   34.56900  1.000 74.38107  ? 1095 ARG   A NE  1 
ATOM   2989 C CZ  . ARG   A 1 483 ? -33.67800 1.60800   33.77800  1.000 76.70085  ? 1095 ARG   A CZ  1 
ATOM   2990 N NH1 . ARG   A 1 483 ? -32.49300 2.10200   34.10000  1.000 74.36665  ? 1095 ARG   A NH1 1 
ATOM   2991 N NH2 . ARG   A 1 483 ? -33.81800 0.93800   32.63700  1.000 77.95788  ? 1095 ARG   A NH2 1 
ATOM   2992 N N   . ARG   A 1 484 ? -35.66100 7.41100   38.79200  1.000 72.08643  ? 1096 ARG   A N   1 
ATOM   2993 C CA  . ARG   A 1 484 ? -35.91000 8.08700   40.06000  1.000 70.56337  ? 1096 ARG   A CA  1 
ATOM   2994 C C   . ARG   A 1 484 ? -37.33000 8.63300   40.10700  1.000 71.56063  ? 1096 ARG   A C   1 
ATOM   2995 O O   . ARG   A 1 484 ? -38.04900 8.45500   41.09800  1.000 70.59060  ? 1096 ARG   A O   1 
ATOM   2996 C CB  . ARG   A 1 484 ? -34.88900 9.20800   40.26500  1.000 70.07520  ? 1096 ARG   A CB  1 
ATOM   2997 C CG  . ARG   A 1 484 ? -33.49600 8.71700   40.61300  1.000 82.85447  ? 1096 ARG   A CG  1 
ATOM   2998 C CD  . ARG   A 1 484 ? -32.49200 9.85500   40.67700  1.000 86.48825  ? 1096 ARG   A CD  1 
ATOM   2999 N NE  . ARG   A 1 484 ? -31.13400 9.37300   40.45700  1.000 90.86993  ? 1096 ARG   A NE  1 
ATOM   3000 C CZ  . ARG   A 1 484 ? -30.21400 9.26400   41.40700  1.000 92.46113  ? 1096 ARG   A CZ  1 
ATOM   3001 N NH1 . ARG   A 1 484 ? -30.47000 9.60700   42.65900  1.000 89.41562  ? 1096 ARG   A NH1 1 
ATOM   3002 N NH2 . ARG   A 1 484 ? -29.00900 8.79600   41.09300  1.000 92.34946  ? 1096 ARG   A NH2 1 
ATOM   3003 N N   . ALA   A 1 485 ? -37.75200 9.29800   39.02800  1.000 70.99275  ? 1097 ALA   A N   1 
ATOM   3004 C CA  . ALA   A 1 485 ? -39.12000 9.79300   38.93800  1.000 71.13109  ? 1097 ALA   A CA  1 
ATOM   3005 C C   . ALA   A 1 485 ? -40.13000 8.65400   38.87100  1.000 72.93932  ? 1097 ALA   A C   1 
ATOM   3006 O O   . ALA   A 1 485 ? -41.23600 8.78000   39.40900  1.000 71.54096  ? 1097 ALA   A O   1 
ATOM   3007 C CB  . ALA   A 1 485 ? -39.25900 10.70600  37.72000  1.000 70.57704  ? 1097 ALA   A CB  1 
ATOM   3008 N N   . ALA   A 1 486 ? -39.76800 7.53500   38.23300  1.000 72.32097  ? 1098 ALA   A N   1 
ATOM   3009 C CA  . ALA   A 1 486 ? -40.66700 6.38800   38.17000  1.000 74.25059  ? 1098 ALA   A CA  1 
ATOM   3010 C C   . ALA   A 1 486 ? -40.89000 5.74800   39.53400  1.000 73.16962  ? 1098 ALA   A C   1 
ATOM   3011 O O   . ALA   A 1 486 ? -41.84100 4.97800   39.69200  1.000 71.24764  ? 1098 ALA   A O   1 
ATOM   3012 C CB  . ALA   A 1 486 ? -40.13100 5.34500   37.18500  1.000 71.47646  ? 1098 ALA   A CB  1 
ATOM   3013 N N   . LEU   A 1 487 ? -40.04000 6.03700   40.51900  1.000 73.47471  ? 1099 LEU   A N   1 
ATOM   3014 C CA  . LEU   A 1 487 ? -40.25700 5.56500   41.88200  1.000 70.31841  ? 1099 LEU   A CA  1 
ATOM   3015 C C   . LEU   A 1 487 ? -40.82600 6.64200   42.79200  1.000 68.33252  ? 1099 LEU   A C   1 
ATOM   3016 O O   . LEU   A 1 487 ? -41.64300 6.33800   43.66900  1.000 61.28072  ? 1099 LEU   A O   1 
ATOM   3017 C CB  . LEU   A 1 487 ? -38.95300 5.02700   42.47600  1.000 68.47345  ? 1099 LEU   A CB  1 
ATOM   3018 C CG  . LEU   A 1 487 ? -39.15900 4.04100   43.62600  1.000 65.76162  ? 1099 LEU   A CG  1 
ATOM   3019 C CD1 . LEU   A 1 487 ? -40.31500 3.09800   43.31300  1.000 61.61371  ? 1099 LEU   A CD1 1 
ATOM   3020 C CD2 . LEU   A 1 487 ? -37.88400 3.26000   43.89900  1.000 58.24618  ? 1099 LEU   A CD2 1 
ATOM   3021 N N   . ILE   A 1 488 ? -40.40600 7.89700   42.60100  1.000 68.88157  ? 1100 ILE   A N   1 
ATOM   3022 C CA  . ILE   A 1 488 ? -41.05800 9.01900   43.26900  1.000 68.42750  ? 1100 ILE   A CA  1 
ATOM   3023 C C   . ILE   A 1 488 ? -42.54100 9.03700   42.92500  1.000 65.81161  ? 1100 ILE   A C   1 
ATOM   3024 O O   . ILE   A 1 488 ? -43.37400 9.45300   43.73900  1.000 62.13288  ? 1100 ILE   A O   1 
ATOM   3025 C CB  . ILE   A 1 488 ? -40.35500 10.33900  42.88400  1.000 61.96608  ? 1100 ILE   A CB  1 
ATOM   3026 C CG1 . ILE   A 1 488 ? -38.92200 10.34500  43.41500  1.000 62.03633  ? 1100 ILE   A CG1 1 
ATOM   3027 C CG2 . ILE   A 1 488 ? -41.10100 11.54500  43.43500  1.000 54.78016  ? 1100 ILE   A CG2 1 
ATOM   3028 C CD1 . ILE   A 1 488 ? -38.13400 11.55600  43.00400  1.000 54.75093  ? 1100 ILE   A CD1 1 
ATOM   3029 N N   . ASN   A 1 489 ? -42.89500 8.56900   41.72400  1.000 68.08715  ? 1101 ASN   A N   1 
ATOM   3030 C CA  . ASN   A 1 489 ? -44.29900 8.41000   41.35700  1.000 66.89296  ? 1101 ASN   A CA  1 
ATOM   3031 C C   . ASN   A 1 489 ? -44.97700 7.37700   42.25000  1.000 66.39075  ? 1101 ASN   A C   1 
ATOM   3032 O O   . ASN   A 1 489 ? -46.05400 7.62900   42.80300  1.000 68.16554  ? 1101 ASN   A O   1 
ATOM   3033 C CB  . ASN   A 1 489 ? -44.39900 8.02100   39.87600  1.000 63.97034  ? 1101 ASN   A CB  1 
ATOM   3034 C CG  . ASN   A 1 489 ? -45.83900 7.85700   39.38300  1.000 66.59670  ? 1101 ASN   A CG  1 
ATOM   3035 O OD1 . ASN   A 1 489 ? -46.71300 7.34000   40.08100  1.000 69.90100  ? 1101 ASN   A OD1 1 
ATOM   3036 N ND2 . ASN   A 1 489 ? -46.08100 8.30100   38.15700  1.000 63.15491  ? 1101 ASN   A ND2 1 
ATOM   3037 N N   . MET   A 1 490 ? -44.35700 6.20400   42.40200  1.000 68.22878  ? 1102 MET   A N   1 
ATOM   3038 C CA  . MET   A 1 490 ? -44.93200 5.17100   43.25800  1.000 69.98449  ? 1102 MET   A CA  1 
ATOM   3039 C C   . MET   A 1 490 ? -45.03600 5.64300   44.70600  1.000 74.75210  ? 1102 MET   A C   1 
ATOM   3040 O O   . MET   A 1 490 ? -46.02000 5.34200   45.39300  1.000 72.16157  ? 1102 MET   A O   1 
ATOM   3041 C CB  . MET   A 1 490 ? -44.10400 3.88800   43.16200  1.000 70.65755  ? 1102 MET   A CB  1 
ATOM   3042 C CG  . MET   A 1 490 ? -44.33100 3.08800   41.88800  1.000 77.57866  ? 1102 MET   A CG  1 
ATOM   3043 S SD  . MET   A 1 490 ? -43.49100 1.48500   41.91200  1.000 75.23220  ? 1102 MET   A SD  1 
ATOM   3044 C CE  . MET   A 1 490 ? -44.55300 0.54300   43.00000  1.000 82.72847  ? 1102 MET   A CE  1 
ATOM   3045 N N   . VAL   A 1 491 ? -44.03000 6.38000   45.19100  1.000 74.70084  ? 1103 VAL   A N   1 
ATOM   3046 C CA  . VAL   A 1 491 ? -44.11700 6.97200   46.52700  1.000 70.27761  ? 1103 VAL   A CA  1 
ATOM   3047 C C   . VAL   A 1 491 ? -45.27400 7.96300   46.58100  1.000 70.85573  ? 1103 VAL   A C   1 
ATOM   3048 O O   . VAL   A 1 491 ? -46.17100 7.85500   47.42300  1.000 77.35783  ? 1103 VAL   A O   1 
ATOM   3049 C CB  . VAL   A 1 491 ? -42.78900 7.64800   46.91400  1.000 70.32813  ? 1103 VAL   A CB  1 
ATOM   3050 C CG1 . VAL   A 1 491 ? -43.02200 8.69900   47.98700  1.000 65.53874  ? 1103 VAL   A CG1 1 
ATOM   3051 C CG2 . VAL   A 1 491 ? -41.77900 6.63000   47.39000  1.000 71.82762  ? 1103 VAL   A CG2 1 
ATOM   3052 N N   . PHE   A 1 492 ? -45.26900 8.93900   45.66700  1.000 68.76269  ? 1104 PHE   A N   1 
ATOM   3053 C CA  . PHE   A 1 492 ? -46.33900 9.93300   45.60000  1.000 65.06898  ? 1104 PHE   A CA  1 
ATOM   3054 C C   . PHE   A 1 492 ? -47.71500 9.28100   45.64300  1.000 68.63260  ? 1104 PHE   A C   1 
ATOM   3055 O O   . PHE   A 1 492 ? -48.62700 9.77500   46.31800  1.000 71.31270  ? 1104 PHE   A O   1 
ATOM   3056 C CB  . PHE   A 1 492 ? -46.18200 10.76900  44.32800  1.000 59.04610  ? 1104 PHE   A CB  1 
ATOM   3057 C CG  . PHE   A 1 492 ? -46.92500 12.07700  44.35200  1.000 51.79996  ? 1104 PHE   A CG  1 
ATOM   3058 C CD1 . PHE   A 1 492 ? -48.25700 12.14200  43.96900  1.000 44.95752  ? 1104 PHE   A CD1 1 
ATOM   3059 C CD2 . PHE   A 1 492 ? -46.28300 13.24600  44.73200  1.000 49.15253  ? 1104 PHE   A CD2 1 
ATOM   3060 C CE1 . PHE   A 1 492 ? -48.93900 13.34400  43.97700  1.000 41.42867  ? 1104 PHE   A CE1 1 
ATOM   3061 C CE2 . PHE   A 1 492 ? -46.95800 14.45100  44.74200  1.000 46.38145  ? 1104 PHE   A CE2 1 
ATOM   3062 C CZ  . PHE   A 1 492 ? -48.28800 14.50100  44.36400  1.000 44.78354  ? 1104 PHE   A CZ  1 
ATOM   3063 N N   . GLN   A 1 493 ? -47.87400 8.15200   44.94900  1.000 68.20799  ? 1105 GLN   A N   1 
ATOM   3064 C CA  . GLN   A 1 493 ? -49.15500 7.45600   44.92600  1.000 68.42143  ? 1105 GLN   A CA  1 
ATOM   3065 C C   . GLN   A 1 493 ? -49.40300 6.67600   46.21300  1.000 72.53844  ? 1105 GLN   A C   1 
ATOM   3066 O O   . GLN   A 1 493 ? -50.54700 6.58000   46.67100  1.000 71.69020  ? 1105 GLN   A O   1 
ATOM   3067 C CB  . GLN   A 1 493 ? -49.21000 6.52100   43.71700  1.000 64.27999  ? 1105 GLN   A CB  1 
ATOM   3068 C CG  . GLN   A 1 493 ? -50.55800 5.86900   43.47300  1.000 62.29882  ? 1105 GLN   A CG  1 
ATOM   3069 C CD  . GLN   A 1 493 ? -50.49200 4.79400   42.40500  1.000 67.83587  ? 1105 GLN   A CD  1 
ATOM   3070 O OE1 . GLN   A 1 493 ? -49.41100 4.33500   42.03600  1.000 76.21507  ? 1105 GLN   A OE1 1 
ATOM   3071 N NE2 . GLN   A 1 493 ? -51.65000 4.39300   41.89600  1.000 60.65565  ? 1105 GLN   A NE2 1 
ATOM   3072 N N   . MET   A 1 494 ? -48.35000 6.11200   46.81400  1.000 73.80443  ? 1106 MET   A N   1 
ATOM   3073 C CA  . MET   A 1 494 ? -48.51200 5.18800   47.92900  1.000 81.99003  ? 1106 MET   A CA  1 
ATOM   3074 C C   . MET   A 1 494 ? -47.61400 5.46700   49.13000  1.000 86.76661  ? 1106 MET   A C   1 
ATOM   3075 O O   . MET   A 1 494 ? -47.65000 4.69400   50.09500  1.000 87.42738  ? 1106 MET   A O   1 
ATOM   3076 C CB  . MET   A 1 494 ? -48.28000 3.74200   47.45100  1.000 82.28830  ? 1106 MET   A CB  1 
ATOM   3077 C CG  . MET   A 1 494 ? -49.17000 3.32300   46.28400  1.000 77.48482  ? 1106 MET   A CG  1 
ATOM   3078 S SD  . MET   A 1 494 ? -48.88300 1.64100   45.69800  1.000 99.45411  ? 1106 MET   A SD  1 
ATOM   3079 C CE  . MET   A 1 494 ? -47.29700 1.82500   44.89900  1.000 84.48661  ? 1106 MET   A CE  1 
ATOM   3080 N N   . GLY   A 1 495 ? -46.82900 6.54200   49.11500  1.000 83.75593  ? 1107 GLY   A N   1 
ATOM   3081 C CA  . GLY   A 1 495 ? -45.93100 6.84500   50.21900  1.000 85.75370  ? 1107 GLY   A CA  1 
ATOM   3082 C C   . GLY   A 1 495 ? -44.74300 5.89700   50.25700  1.000 94.26334  ? 1107 GLY   A C   1 
ATOM   3083 O O   . GLY   A 1 495 ? -44.59700 4.99000   49.43900  1.000 95.72496  ? 1107 GLY   A O   1 
ATOM   3084 N N   . GLU   A 1 496 ? -43.87000 6.13100   51.23600  1.000 97.56787  ? 1108 GLU   A N   1 
ATOM   3085 C CA  . GLU   A 1 496 ? -42.85000 5.15000   51.57600  1.000 98.89195  ? 1108 GLU   A CA  1 
ATOM   3086 C C   . GLU   A 1 496 ? -43.42500 3.98800   52.37300  1.000 101.52888 ? 1108 GLU   A C   1 
ATOM   3087 O O   . GLU   A 1 496 ? -42.66300 3.17100   52.89900  1.000 101.80852 ? 1108 GLU   A O   1 
ATOM   3088 C CB  . GLU   A 1 496 ? -41.70200 5.79800   52.35800  1.000 90.39293  ? 1108 GLU   A CB  1 
ATOM   3089 C CG  . GLU   A 1 496 ? -42.12000 6.53500   53.62500  1.000 98.89007  ? 1108 GLU   A CG  1 
ATOM   3090 C CD  . GLU   A 1 496 ? -42.59100 7.95500   53.36800  1.000 98.74012  ? 1108 GLU   A CD  1 
ATOM   3091 O OE1 . GLU   A 1 496 ? -42.97200 8.26800   52.21800  1.000 94.68919  ? 1108 GLU   A OE1 1 
ATOM   3092 O OE2 . GLU   A 1 496 ? -42.58700 8.75800   54.32600  1.000 98.26393  ? 1108 GLU   A OE2 1 
ATOM   3093 N N   . THR   A 1 497 ? -44.75300 3.91200   52.47500  1.000 100.11133 ? 1109 THR   A N   1 
ATOM   3094 C CA  . THR   A 1 497 ? -45.42000 2.82000   53.17400  1.000 101.04796 ? 1109 THR   A CA  1 
ATOM   3095 C C   . THR   A 1 497 ? -45.41400 1.54400   52.33900  1.000 101.14048 ? 1109 THR   A C   1 
ATOM   3096 O O   . THR   A 1 497 ? -44.92600 0.49900   52.78300  1.000 100.03129 ? 1109 THR   A O   1 
ATOM   3097 C CB  . THR   A 1 497 ? -46.85900 3.22400   53.51500  1.000 103.57503 ? 1109 THR   A CB  1 
ATOM   3098 O OG1 . THR   A 1 497 ? -47.68300 3.09300   52.34800  1.000 104.63554 ? 1109 THR   A OG1 1 
ATOM   3099 C CG2 . THR   A 1 497 ? -46.90700 4.67000   53.99300  1.000 100.33620 ? 1109 THR   A CG2 1 
ATOM   3100 N N   . GLY   A 1 498 ? -45.94800 1.61600   51.12000  1.000 97.39281  ? 1110 GLY   A N   1 
ATOM   3101 C CA  . GLY   A 1 498 ? -46.13100 0.43700   50.29800  1.000 93.80583  ? 1110 GLY   A CA  1 
ATOM   3102 C C   . GLY   A 1 498 ? -45.00400 0.14900   49.32800  1.000 98.12471  ? 1110 GLY   A C   1 
ATOM   3103 O O   . GLY   A 1 498 ? -44.67400 -1.01700  49.08800  1.000 98.70099  ? 1110 GLY   A O   1 
ATOM   3104 N N   . VAL   A 1 499 ? -44.41000 1.19600   48.75100  1.000 100.60403 ? 1111 VAL   A N   1 
ATOM   3105 C CA  . VAL   A 1 499 ? -43.32100 0.97600   47.80500  1.000 102.74027 ? 1111 VAL   A CA  1 
ATOM   3106 C C   . VAL   A 1 499 ? -42.09200 0.45100   48.53000  1.000 101.87865 ? 1111 VAL   A C   1 
ATOM   3107 O O   . VAL   A 1 499 ? -41.26700 -0.25600  47.93900  1.000 101.39856 ? 1111 VAL   A O   1 
ATOM   3108 C CB  . VAL   A 1 499 ? -43.01500 2.26500   47.02000  1.000 91.44564  ? 1111 VAL   A CB  1 
ATOM   3109 C CG1 . VAL   A 1 499 ? -44.29900 2.85300   46.48600  1.000 85.65118  ? 1111 VAL   A CG1 1 
ATOM   3110 C CG2 . VAL   A 1 499 ? -42.28200 3.26600   47.88600  1.000 91.99246  ? 1111 VAL   A CG2 1 
ATOM   3111 N N   . ALA   A 1 500 ? -41.94500 0.78200   49.81400  1.000 96.41038  ? 1112 ALA   A N   1 
ATOM   3112 C CA  . ALA   A 1 500 ? -40.97700 0.10400   50.66000  1.000 101.57132 ? 1112 ALA   A CA  1 
ATOM   3113 C C   . ALA   A 1 500 ? -41.46600 -1.26300  51.10800  1.000 99.94459  ? 1112 ALA   A C   1 
ATOM   3114 O O   . ALA   A 1 500 ? -40.68200 -2.03100  51.67600  1.000 94.01076  ? 1112 ALA   A O   1 
ATOM   3115 C CB  . ALA   A 1 500 ? -40.65200 0.95600   51.88900  1.000 100.71719 ? 1112 ALA   A CB  1 
ATOM   3116 N N   . GLY   A 1 501 ? -42.73300 -1.58200  50.86000  1.000 100.50180 ? 1113 GLY   A N   1 
ATOM   3117 C CA  . GLY   A 1 501 ? -43.30700 -2.83600  51.30200  1.000 102.84975 ? 1113 GLY   A CA  1 
ATOM   3118 C C   . GLY   A 1 501 ? -43.34900 -3.90500  50.23100  1.000 99.73410  ? 1113 GLY   A C   1 
ATOM   3119 O O   . GLY   A 1 501 ? -44.18700 -4.80900  50.28500  1.000 100.70397 ? 1113 GLY   A O   1 
ATOM   3120 N N   . PHE   A 1 502 ? -42.45700 -3.81100  49.23800  1.000 96.66961  ? 1114 PHE   A N   1 
ATOM   3121 C CA  . PHE   A 1 502 ? -42.27700 -4.89600  48.27100  1.000 98.81687  ? 1114 PHE   A CA  1 
ATOM   3122 C C   . PHE   A 1 502 ? -40.80100 -4.88700  47.86000  1.000 93.72143  ? 1114 PHE   A C   1 
ATOM   3123 O O   . PHE   A 1 502 ? -40.42800 -4.46900  46.76100  1.000 90.91031  ? 1114 PHE   A O   1 
ATOM   3124 C CB  . PHE   A 1 502 ? -43.20000 -4.77400  47.05900  1.000 101.03796 ? 1114 PHE   A CB  1 
ATOM   3125 C CG  . PHE   A 1 502 ? -43.33300 -6.05200  46.27700  1.000 98.66192  ? 1114 PHE   A CG  1 
ATOM   3126 C CD1 . PHE   A 1 502 ? -44.17900 -7.05900  46.71300  1.000 96.44677  ? 1114 PHE   A CD1 1 
ATOM   3127 C CD2 . PHE   A 1 502 ? -42.59600 -6.25500  45.12100  1.000 98.86992  ? 1114 PHE   A CD2 1 
ATOM   3128 C CE1 . PHE   A 1 502 ? -44.30000 -8.24000  46.00300  1.000 95.13705  ? 1114 PHE   A CE1 1 
ATOM   3129 C CE2 . PHE   A 1 502 ? -42.71200 -7.43600  44.40600  1.000 98.47197  ? 1114 PHE   A CE2 1 
ATOM   3130 C CZ  . PHE   A 1 502 ? -43.56600 -8.42900  44.84900  1.000 94.97897  ? 1114 PHE   A CZ  1 
ATOM   3131 N N   . THR   A 1 503 ? -39.95300 -5.36900  48.77100  1.000 92.94932  ? 1115 THR   A N   1 
ATOM   3132 C CA  . THR   A 1 503 ? -38.51000 -5.35800  48.57000  1.000 94.21598  ? 1115 THR   A CA  1 
ATOM   3133 C C   . THR   A 1 503 ? -38.06400 -6.36300  47.51100  1.000 94.67233  ? 1115 THR   A C   1 
ATOM   3134 O O   . THR   A 1 503 ? -36.92100 -6.28800  47.04700  1.000 94.09777  ? 1115 THR   A O   1 
ATOM   3135 C CB  . THR   A 1 503 ? -37.81900 -5.61100  49.91900  1.000 94.39044  ? 1115 THR   A CB  1 
ATOM   3136 O OG1 . THR   A 1 503 ? -38.25700 -4.62300  50.86000  1.000 94.30966  ? 1115 THR   A OG1 1 
ATOM   3137 C CG2 . THR   A 1 503 ? -36.30600 -5.48700  49.81000  1.000 88.94918  ? 1115 THR   A CG2 1 
ATOM   3138 N N   . ASN   A 1 504 ? -38.94900 -7.27100  47.09100  1.000 94.74453  ? 1116 ASN   A N   1 
ATOM   3139 C CA  . ASN   A 1 504 ? -38.60500 -8.21700  46.03300  1.000 91.63782  ? 1116 ASN   A CA  1 
ATOM   3140 C C   . ASN   A 1 504 ? -38.14100 -7.49100  44.77700  1.000 94.40285  ? 1116 ASN   A C   1 
ATOM   3141 O O   . ASN   A 1 504 ? -37.09500 -7.82000  44.20700  1.000 102.90537 ? 1116 ASN   A O   1 
ATOM   3142 C CB  . ASN   A 1 504 ? -39.80400 -9.11500  45.72100  1.000 96.92616  ? 1116 ASN   A CB  1 
ATOM   3143 C CG  . ASN   A 1 504 ? -40.30300 -9.86800  46.93900  1.000 95.16901  ? 1116 ASN   A CG  1 
ATOM   3144 O OD1 . ASN   A 1 504 ? -39.71500 -10.87000 47.35000  1.000 89.75308  ? 1116 ASN   A OD1 1 
ATOM   3145 N ND2 . ASN   A 1 504 ? -41.39600 -9.38800  47.52400  1.000 87.72024  ? 1116 ASN   A ND2 1 
ATOM   3146 N N   . SER   A 1 505 ? -38.90500 -6.48700  44.33500  1.000 93.95265  ? 1117 SER   A N   1 
ATOM   3147 C CA  . SER   A 1 505 ? -38.51900 -5.71800  43.15600  1.000 97.56984  ? 1117 SER   A CA  1 
ATOM   3148 C C   . SER   A 1 505 ? -37.48800 -4.64800  43.48200  1.000 96.21265  ? 1117 SER   A C   1 
ATOM   3149 O O   . SER   A 1 505 ? -36.69400 -4.27400  42.61200  1.000 94.02009  ? 1117 SER   A O   1 
ATOM   3150 C CB  . SER   A 1 505 ? -39.74500 -5.05700  42.52900  1.000 90.42724  ? 1117 SER   A CB  1 
ATOM   3151 O OG  . SER   A 1 505 ? -40.75600 -6.00500  42.27300  1.000 83.81690  ? 1117 SER   A OG  1 
ATOM   3152 N N   . LEU   A 1 506 ? -37.50200 -4.13900  44.71700  1.000 93.67643  ? 1118 LEU   A N   1 
ATOM   3153 C CA  . LEU   A 1 506 ? -36.55200 -3.10800  45.12000  1.000 95.48198  ? 1118 LEU   A CA  1 
ATOM   3154 C C   . LEU   A 1 506 ? -35.12200 -3.61500  44.99700  1.000 95.18483  ? 1118 LEU   A C   1 
ATOM   3155 O O   . LEU   A 1 506 ? -34.24800 -2.92900  44.45300  1.000 93.69045  ? 1118 LEU   A O   1 
ATOM   3156 C CB  . LEU   A 1 506 ? -36.85600 -2.66500  46.55100  1.000 94.86674  ? 1118 LEU   A CB  1 
ATOM   3157 C CG  . LEU   A 1 506 ? -38.28900 -2.16400  46.75200  1.000 87.98381  ? 1118 LEU   A CG  1 
ATOM   3158 C CD1 . LEU   A 1 506 ? -38.58100 -1.89400  48.21700  1.000 84.79087  ? 1118 LEU   A CD1 1 
ATOM   3159 C CD2 . LEU   A 1 506 ? -38.55700 -0.93100  45.90100  1.000 91.70228  ? 1118 LEU   A CD2 1 
ATOM   3160 N N   . ARG   A 1 507 ? -34.86600 -4.82600  45.49600  1.000 97.37793  ? 1119 ARG   A N   1 
ATOM   3161 C CA  . ARG   A 1 507 ? -33.56700 -5.45200  45.27300  1.000 100.26693 ? 1119 ARG   A CA  1 
ATOM   3162 C C   . ARG   A 1 507 ? -33.36400 -5.75000  43.79400  1.000 97.72448  ? 1119 ARG   A C   1 
ATOM   3163 O O   . ARG   A 1 507 ? -32.25800 -5.58800  43.26400  1.000 101.20171 ? 1119 ARG   A O   1 
ATOM   3164 C CB  . ARG   A 1 507 ? -33.44800 -6.73400  46.10100  1.000 104.77989 ? 1119 ARG   A CB  1 
ATOM   3165 C CG  . ARG   A 1 507 ? -33.71100 -6.57400  47.60200  1.000 106.72881 ? 1119 ARG   A CG  1 
ATOM   3166 C CD  . ARG   A 1 507 ? -32.45900 -6.18000  48.39300  1.000 101.29081 ? 1119 ARG   A CD  1 
ATOM   3167 N NE  . ARG   A 1 507 ? -31.90000 -4.88800  48.01000  1.000 105.25301 ? 1119 ARG   A NE  1 
ATOM   3168 C CZ  . ARG   A 1 507 ? -32.55600 -3.73300  48.01000  1.000 103.59566 ? 1119 ARG   A CZ  1 
ATOM   3169 N NH1 . ARG   A 1 507 ? -33.80000 -3.63700  48.45600  1.000 96.09491  ? 1119 ARG   A NH1 1 
ATOM   3170 N NH2 . ARG   A 1 507 ? -31.94400 -2.64200  47.56000  1.000 105.40352 ? 1119 ARG   A NH2 1 
ATOM   3171 N N   . MET   A 1 508 ? -34.43000 -6.18300  43.11100  1.000 97.02874  ? 1120 MET   A N   1 
ATOM   3172 C CA  . MET   A 1 508 ? -34.35100 -6.45000  41.67900  1.000 96.85218  ? 1120 MET   A CA  1 
ATOM   3173 C C   . MET   A 1 508 ? -33.95000 -5.19400  40.91400  1.000 99.67984  ? 1120 MET   A C   1 
ATOM   3174 O O   . MET   A 1 508 ? -33.20200 -5.26500  39.93000  1.000 96.92799  ? 1120 MET   A O   1 
ATOM   3175 C CB  . MET   A 1 508 ? -35.69700 -6.98000  41.17600  1.000 92.85544  ? 1120 MET   A CB  1 
ATOM   3176 C CG  . MET   A 1 508 ? -35.84400 -8.49800  41.21500  1.000 95.22980  ? 1120 MET   A CG  1 
ATOM   3177 S SD  . MET   A 1 508 ? -34.48200 -9.40300  40.44800  1.000 108.45393 ? 1120 MET   A SD  1 
ATOM   3178 C CE  . MET   A 1 508 ? -35.18200 -11.05100 40.35100  1.000 92.14852  ? 1120 MET   A CE  1 
ATOM   3179 N N   . LEU   A 1 509 ? -34.43200 -4.03200  41.36500  1.000 99.22234  ? 1121 LEU   A N   1 
ATOM   3180 C CA  . LEU   A 1 509 ? -34.08900 -2.76400  40.73100  1.000 97.72006  ? 1121 LEU   A CA  1 
ATOM   3181 C C   . LEU   A 1 509 ? -32.67500 -2.32100  41.09100  1.000 97.60564  ? 1121 LEU   A C   1 
ATOM   3182 O O   . LEU   A 1 509 ? -31.94900 -1.80300  40.23500  1.000 98.58826  ? 1121 LEU   A O   1 
ATOM   3183 C CB  . LEU   A 1 509 ? -35.10800 -1.69400  41.13100  1.000 93.60684  ? 1121 LEU   A CB  1 
ATOM   3184 C CG  . LEU   A 1 509 ? -36.43900 -1.71600  40.36900  1.000 94.82029  ? 1121 LEU   A CG  1 
ATOM   3185 C CD1 . LEU   A 1 509 ? -37.55100 -1.07500  41.18300  1.000 91.25474  ? 1121 LEU   A CD1 1 
ATOM   3186 C CD2 . LEU   A 1 509 ? -36.31000 -1.03900  39.01800  1.000 92.06741  ? 1121 LEU   A CD2 1 
ATOM   3187 N N   . GLN   A 1 510 ? -32.27100 -2.51300  42.35000  1.000 97.85650  ? 1122 GLN   A N   1 
ATOM   3188 C CA  . GLN   A 1 510 ? -30.90000 -2.20300  42.74500  1.000 99.39119  ? 1122 GLN   A CA  1 
ATOM   3189 C C   . GLN   A 1 510 ? -29.89900 -3.02800  41.94600  1.000 94.65078  ? 1122 GLN   A C   1 
ATOM   3190 O O   . GLN   A 1 510 ? -28.89800 -2.49700  41.45200  1.000 95.60031  ? 1122 GLN   A O   1 
ATOM   3191 C CB  . GLN   A 1 510 ? -30.71900 -2.44300  44.24400  1.000 89.95193  ? 1122 GLN   A CB  1 
ATOM   3192 N N   . GLN   A 1 511 ? -30.16400 -4.32600  41.79400  1.000 89.70706  ? 1123 GLN   A N   1 
ATOM   3193 C CA  . GLN   A 1 511 ? -29.31500 -5.21600  41.00600  1.000 91.75226  ? 1123 GLN   A CA  1 
ATOM   3194 C C   . GLN   A 1 511 ? -29.48700 -5.02200  39.50100  1.000 99.58625  ? 1123 GLN   A C   1 
ATOM   3195 O O   . GLN   A 1 511 ? -28.97800 -5.85500  38.73600  1.000 100.72262 ? 1123 GLN   A O   1 
ATOM   3196 C CB  . GLN   A 1 511 ? -29.59700 -6.67400  41.37500  1.000 87.10190  ? 1123 GLN   A CB  1 
ATOM   3197 N N   . LYS   A 1 512 ? -30.18200 -3.96500  39.08000  1.000 101.46872 ? 1124 LYS   A N   1 
ATOM   3198 C CA  . LYS   A 1 512 ? -30.44300 -3.61600  37.68500  1.000 95.67260  ? 1124 LYS   A CA  1 
ATOM   3199 C C   . LYS   A 1 512 ? -31.17500 -4.71500  36.92100  1.000 92.53978  ? 1124 LYS   A C   1 
ATOM   3200 O O   . LYS   A 1 512 ? -31.21300 -4.68400  35.68400  1.000 89.55378  ? 1124 LYS   A O   1 
ATOM   3201 C CB  . LYS   A 1 512 ? -29.15100 -3.23200  36.94600  1.000 86.02554  ? 1124 LYS   A CB  1 
ATOM   3202 C CG  . LYS   A 1 512 ? -28.12700 -2.51600  37.82000  1.000 90.17339  ? 1124 LYS   A CG  1 
ATOM   3203 C CD  . LYS   A 1 512 ? -28.52100 -1.07800  38.09300  1.000 94.76279  ? 1124 LYS   A CD  1 
ATOM   3204 C CE  . LYS   A 1 512 ? -27.40400 -0.33000  38.80500  1.000 90.20734  ? 1124 LYS   A CE  1 
ATOM   3205 N NZ  . LYS   A 1 512 ? -26.37400 0.19100   37.86400  1.000 84.02905  ? 1124 LYS   A NZ  1 
ATOM   3206 N N   . ARG   A 1 513 ? -31.76100 -5.68800  37.62200  1.000 91.63530  ? 1125 ARG   A N   1 
ATOM   3207 C CA  . ARG   A 1 513 ? -32.56100 -6.73800  36.98800  1.000 91.23448  ? 1125 ARG   A CA  1 
ATOM   3208 C C   . ARG   A 1 513 ? -33.96000 -6.18000  36.74100  1.000 91.70432  ? 1125 ARG   A C   1 
ATOM   3209 O O   . ARG   A 1 513 ? -34.90800 -6.41100  37.49700  1.000 94.51968  ? 1125 ARG   A O   1 
ATOM   3210 C CB  . ARG   A 1 513 ? -32.59600 -7.99200  37.85600  1.000 85.38026  ? 1125 ARG   A CB  1 
ATOM   3211 N N   . TRP   A 1 514 ? -34.08300 -5.43100  35.64500  1.000 91.01212  ? 1126 TRP   A N   1 
ATOM   3212 C CA  . TRP   A 1 514 ? -35.29400 -4.67000  35.36200  1.000 90.46339  ? 1126 TRP   A CA  1 
ATOM   3213 C C   . TRP   A 1 514 ? -36.35900 -5.49200  34.65200  1.000 88.87652  ? 1126 TRP   A C   1 
ATOM   3214 O O   . TRP   A 1 514 ? -37.55100 -5.33300  34.93700  1.000 88.82909  ? 1126 TRP   A O   1 
ATOM   3215 C CB  . TRP   A 1 514 ? -34.95200 -3.43900  34.52300  1.000 83.97042  ? 1126 TRP   A CB  1 
ATOM   3216 C CG  . TRP   A 1 514 ? -34.09100 -2.47200  35.25000  1.000 92.02888  ? 1126 TRP   A CG  1 
ATOM   3217 C CD1 . TRP   A 1 514 ? -34.37900 -1.84600  36.42600  1.000 91.60268  ? 1126 TRP   A CD1 1 
ATOM   3218 C CD2 . TRP   A 1 514 ? -32.79700 -2.00900  34.85300  1.000 84.41836  ? 1126 TRP   A CD2 1 
ATOM   3219 N NE1 . TRP   A 1 514 ? -33.34000 -1.02500  36.79200  1.000 93.62533  ? 1126 TRP   A NE1 1 
ATOM   3220 C CE2 . TRP   A 1 514 ? -32.35600 -1.10600  35.84100  1.000 89.79335  ? 1126 TRP   A CE2 1 
ATOM   3221 C CE3 . TRP   A 1 514 ? -31.96800 -2.27200  33.76200  1.000 76.72989  ? 1126 TRP   A CE3 1 
ATOM   3222 C CZ2 . TRP   A 1 514 ? -31.12500 -0.46300  35.76900  1.000 79.47096  ? 1126 TRP   A CZ2 1 
ATOM   3223 C CZ3 . TRP   A 1 514 ? -30.74700 -1.63400  33.69200  1.000 91.74273  ? 1126 TRP   A CZ3 1 
ATOM   3224 C CH2 . TRP   A 1 514 ? -30.33600 -0.74000  34.69000  1.000 85.45457  ? 1126 TRP   A CH2 1 
ATOM   3225 N N   . ASP   A 1 515 ? -35.95300 -6.36400  33.72700  1.000 97.43496  ? 1127 ASP   A N   1 
ATOM   3226 C CA  . ASP   A 1 515 ? -36.90700 -7.28100  33.11600  1.000 96.29320  ? 1127 ASP   A CA  1 
ATOM   3227 C C   . ASP   A 1 515 ? -37.60500 -8.12000  34.17400  1.000 92.47404  ? 1127 ASP   A C   1 
ATOM   3228 O O   . ASP   A 1 515 ? -38.75600 -8.53600  33.98500  1.000 88.84935  ? 1127 ASP   A O   1 
ATOM   3229 C CB  . ASP   A 1 515 ? -36.19300 -8.17900  32.10200  1.000 101.18694 ? 1127 ASP   A CB  1 
ATOM   3230 C CG  . ASP   A 1 515 ? -37.04000 -8.46900  30.88100  1.000 102.64890 ? 1127 ASP   A CG  1 
ATOM   3231 O OD1 . ASP   A 1 515 ? -37.74500 -7.54900  30.41300  1.000 95.98280  ? 1127 ASP   A OD1 1 
ATOM   3232 O OD2 . ASP   A 1 515 ? -37.00300 -9.61900  30.39000  1.000 127.51411 ? 1127 ASP   A OD2 1 
ATOM   3233 N N   . GLU   A 1 516 ? -36.92700 -8.36400  35.29800  1.000 97.22474  ? 1128 GLU   A N   1 
ATOM   3234 C CA  . GLU   A 1 516 ? -37.53700 -9.06900  36.41800  1.000 91.19194  ? 1128 GLU   A CA  1 
ATOM   3235 C C   . GLU   A 1 516 ? -38.34000 -8.12400  37.29900  1.000 88.36492  ? 1128 GLU   A C   1 
ATOM   3236 O O   . GLU   A 1 516 ? -39.47000 -8.43800  37.68800  1.000 91.81632  ? 1128 GLU   A O   1 
ATOM   3237 C CB  . GLU   A 1 516 ? -36.46700 -9.78500  37.24000  1.000 90.37534  ? 1128 GLU   A CB  1 
ATOM   3238 C CG  . GLU   A 1 516 ? -36.56000 -11.25200 37.02300  1.000 91.70913  ? 1128 GLU   A CG  1 
ATOM   3239 C CD  . GLU   A 1 516 ? -37.91100 -11.74900 37.44000  1.000 96.84048  ? 1128 GLU   A CD  1 
ATOM   3240 O OE1 . GLU   A 1 516 ? -38.32800 -11.49700 38.59000  1.000 107.02492 ? 1128 GLU   A OE1 1 
ATOM   3241 O OE2 . GLU   A 1 516 ? -38.61100 -12.26700 36.56100  1.000 92.73803  ? 1128 GLU   A OE2 1 
ATOM   3242 N N   . ALA   A 1 517 ? -37.76800 -6.96100  37.62400  1.000 85.25584  ? 1129 ALA   A N   1 
ATOM   3243 C CA  . ALA   A 1 517 ? -38.48700 -5.97400  38.42000  1.000 84.00328  ? 1129 ALA   A CA  1 
ATOM   3244 C C   . ALA   A 1 517 ? -39.81900 -5.60200  37.78400  1.000 87.04621  ? 1129 ALA   A C   1 
ATOM   3245 O O   . ALA   A 1 517 ? -40.77900 -5.28100  38.49200  1.000 89.23711  ? 1129 ALA   A O   1 
ATOM   3246 C CB  . ALA   A 1 517 ? -37.62400 -4.72700  38.60800  1.000 82.86405  ? 1129 ALA   A CB  1 
ATOM   3247 N N   . ALA   A 1 518 ? -39.90100 -5.66200  36.45200  1.000 84.81528  ? 1130 ALA   A N   1 
ATOM   3248 C CA  . ALA   A 1 518 ? -41.11300 -5.27800  35.74000  1.000 85.11088  ? 1130 ALA   A CA  1 
ATOM   3249 C C   . ALA   A 1 518 ? -42.17800 -6.36900  35.73600  1.000 85.00659  ? 1130 ALA   A C   1 
ATOM   3250 O O   . ALA   A 1 518 ? -43.35900 -6.05500  35.55700  1.000 85.92169  ? 1130 ALA   A O   1 
ATOM   3251 C CB  . ALA   A 1 518 ? -40.77100 -4.88700  34.30200  1.000 89.09648  ? 1130 ALA   A CB  1 
ATOM   3252 N N   . VAL   A 1 519 ? -41.79700 -7.63400  35.91800  1.000 84.24649  ? 1131 VAL   A N   1 
ATOM   3253 C CA  . VAL   A 1 519 ? -42.80400 -8.68700  36.01000  1.000 86.02223  ? 1131 VAL   A CA  1 
ATOM   3254 C C   . VAL   A 1 519 ? -43.38700 -8.75100  37.42100  1.000 91.52992  ? 1131 VAL   A C   1 
ATOM   3255 O O   . VAL   A 1 519 ? -44.58100 -9.03000  37.59400  1.000 94.09475  ? 1131 VAL   A O   1 
ATOM   3256 C CB  . VAL   A 1 519 ? -42.20600 -10.03900 35.57500  1.000 86.45785  ? 1131 VAL   A CB  1 
ATOM   3257 C CG1 . VAL   A 1 519 ? -43.03200 -11.20200 36.10900  1.000 89.47982  ? 1131 VAL   A CG1 1 
ATOM   3258 C CG2 . VAL   A 1 519 ? -42.10000 -10.11200 34.06000  1.000 84.27716  ? 1131 VAL   A CG2 1 
ATOM   3259 N N   . ASN   A 1 520 ? -42.57000 -8.47500  38.44100  1.000 90.93247  ? 1132 ASN   A N   1 
ATOM   3260 C CA  . ASN   A 1 520 ? -43.05800 -8.47200  39.81800  1.000 87.47999  ? 1132 ASN   A CA  1 
ATOM   3261 C C   . ASN   A 1 520 ? -44.10600 -7.38500  40.03200  1.000 85.14670  ? 1132 ASN   A C   1 
ATOM   3262 O O   . ASN   A 1 520 ? -45.18300 -7.64600  40.57800  1.000 83.94224  ? 1132 ASN   A O   1 
ATOM   3263 C CB  . ASN   A 1 520 ? -41.89000 -8.27500  40.78200  1.000 88.82176  ? 1132 ASN   A CB  1 
ATOM   3264 C CG  . ASN   A 1 520 ? -41.24300 -9.57400  41.19600  1.000 92.91395  ? 1132 ASN   A CG  1 
ATOM   3265 O OD1 . ASN   A 1 520 ? -40.20600 -9.96400  40.65500  1.000 85.96763  ? 1132 ASN   A OD1 1 
ATOM   3266 N ND2 . ASN   A 1 520 ? -41.84300 -10.24900 42.17000  1.000 91.18811  ? 1132 ASN   A ND2 1 
ATOM   3267 N N   . LEU   A 1 521 ? -43.79900 -6.15200  39.62000  1.000 83.29065  ? 1133 LEU   A N   1 
ATOM   3268 C CA  . LEU   A 1 521 ? -44.74300 -5.04800  39.75200  1.000 82.61286  ? 1133 LEU   A CA  1 
ATOM   3269 C C   . LEU   A 1 521 ? -45.97500 -5.20400  38.87000  1.000 85.89323  ? 1133 LEU   A C   1 
ATOM   3270 O O   . LEU   A 1 521 ? -46.96100 -4.49100  39.09000  1.000 88.40924  ? 1133 LEU   A O   1 
ATOM   3271 C CB  . LEU   A 1 521 ? -44.04400 -3.71900  39.45000  1.000 79.80243  ? 1133 LEU   A CB  1 
ATOM   3272 C CG  . LEU   A 1 521 ? -42.70300 -3.49800  40.14500  1.000 73.70827  ? 1133 LEU   A CG  1 
ATOM   3273 C CD1 . LEU   A 1 521 ? -42.23500 -2.07300  39.96600  1.000 76.48285  ? 1133 LEU   A CD1 1 
ATOM   3274 C CD2 . LEU   A 1 521 ? -42.89400 -3.78400  41.62000  1.000 79.54224  ? 1133 LEU   A CD2 1 
ATOM   3275 N N   . ALA   A 1 522 ? -45.94600 -6.10600  37.88700  1.000 84.56416  ? 1134 ALA   A N   1 
ATOM   3276 C CA  . ALA   A 1 522 ? -47.13500 -6.42100  37.10500  1.000 84.10736  ? 1134 ALA   A CA  1 
ATOM   3277 C C   . ALA   A 1 522 ? -48.07600 -7.37800  37.82500  1.000 86.24877  ? 1134 ALA   A C   1 
ATOM   3278 O O   . ALA   A 1 522 ? -49.22600 -7.52700  37.40100  1.000 86.37404  ? 1134 ALA   A O   1 
ATOM   3279 C CB  . ALA   A 1 522 ? -46.73700 -7.01600  35.75200  1.000 85.23215  ? 1134 ALA   A CB  1 
ATOM   3280 N N   . LYS   A 1 523 ? -47.61100 -8.03700  38.88800  1.000 85.65627  ? 1135 LYS   A N   1 
ATOM   3281 C CA  . LYS   A 1 523 ? -48.46600 -8.85400  39.73700  1.000 85.71784  ? 1135 LYS   A CA  1 
ATOM   3282 C C   . LYS   A 1 523 ? -48.82300 -8.15300  41.04300  1.000 86.17937  ? 1135 LYS   A C   1 
ATOM   3283 O O   . LYS   A 1 523 ? -49.81000 -8.53100  41.68400  1.000 85.58463  ? 1135 LYS   A O   1 
ATOM   3284 C CB  . LYS   A 1 523 ? -47.78100 -10.20100 40.02900  1.000 81.19973  ? 1135 LYS   A CB  1 
ATOM   3285 C CG  . LYS   A 1 523 ? -48.50200 -11.12100 41.01700  1.000 82.89328  ? 1135 LYS   A CG  1 
ATOM   3286 C CD  . LYS   A 1 523 ? -49.95900 -11.36100 40.61600  1.000 87.55531  ? 1135 LYS   A CD  1 
ATOM   3287 C CE  . LYS   A 1 523 ? -50.68400 -12.21000 41.64800  1.000 86.09572  ? 1135 LYS   A CE  1 
ATOM   3288 N NZ  . LYS   A 1 523 ? -50.69000 -11.53800 42.98000  1.000 81.41177  ? 1135 LYS   A NZ  1 
ATOM   3289 N N   . SER   A 1 524 ? -48.06600 -7.12100  41.42400  1.000 88.36351  ? 1136 SER   A N   1 
ATOM   3290 C CA  . SER   A 1 524 ? -48.30700 -6.40300  42.66900  1.000 89.05274  ? 1136 SER   A CA  1 
ATOM   3291 C C   . SER   A 1 524 ? -49.77200 -5.99000  42.78800  1.000 95.10628  ? 1136 SER   A C   1 
ATOM   3292 O O   . SER   A 1 524 ? -50.45200 -5.73400  41.78900  1.000 89.46319  ? 1136 SER   A O   1 
ATOM   3293 C CB  . SER   A 1 524 ? -47.40200 -5.16700  42.75100  1.000 85.86380  ? 1136 SER   A CB  1 
ATOM   3294 O OG  . SER   A 1 524 ? -46.19800 -5.44200  43.45300  1.000 79.10789  ? 1136 SER   A OG  1 
ATOM   3295 N N   . ARG   A 1 525 ? -50.26000 -5.95200  44.03500  1.000 100.35813 ? 1137 ARG   A N   1 
ATOM   3296 C CA  . ARG   A 1 525 ? -51.62700 -5.51400  44.30600  1.000 95.17752  ? 1137 ARG   A CA  1 
ATOM   3297 C C   . ARG   A 1 525 ? -51.91100 -4.14800  43.69500  1.000 96.32186  ? 1137 ARG   A C   1 
ATOM   3298 O O   . ARG   A 1 525 ? -53.05000 -3.85900  43.30800  1.000 97.46041  ? 1137 ARG   A O   1 
ATOM   3299 C CB  . ARG   A 1 525 ? -51.86300 -5.48600  45.81900  1.000 94.70456  ? 1137 ARG   A CB  1 
ATOM   3300 C CG  . ARG   A 1 525 ? -53.17900 -4.86500  46.25700  1.000 95.99441  ? 1137 ARG   A CG  1 
ATOM   3301 C CD  . ARG   A 1 525 ? -54.34300 -5.81700  46.05600  1.000 95.71878  ? 1137 ARG   A CD  1 
ATOM   3302 N NE  . ARG   A 1 525 ? -55.61700 -5.11100  46.04300  1.000 98.53092  ? 1137 ARG   A NE  1 
ATOM   3303 C CZ  . ARG   A 1 525 ? -56.27700 -4.73900  47.13200  1.000 98.27772  ? 1137 ARG   A CZ  1 
ATOM   3304 N NH1 . ARG   A 1 525 ? -55.81300 -4.99900  48.34400  1.000 95.86284  ? 1137 ARG   A NH1 1 
ATOM   3305 N NH2 . ARG   A 1 525 ? -57.43100 -4.09200  47.00200  1.000 98.08242  ? 1137 ARG   A NH2 1 
ATOM   3306 N N   . TRP   A 1 526 ? -50.88300 -3.30500  43.59000  1.000 97.26701  ? 1138 TRP   A N   1 
ATOM   3307 C CA  . TRP   A 1 526 ? -51.02600 -1.98900  42.98000  1.000 94.12095  ? 1138 TRP   A CA  1 
ATOM   3308 C C   . TRP   A 1 526 ? -51.32100 -2.07800  41.48600  1.000 87.68972  ? 1138 TRP   A C   1 
ATOM   3309 O O   . TRP   A 1 526 ? -51.98600 -1.19300  40.93500  1.000 80.24297  ? 1138 TRP   A O   1 
ATOM   3310 C CB  . TRP   A 1 526 ? -49.75300 -1.18600  43.23900  1.000 89.51826  ? 1138 TRP   A CB  1 
ATOM   3311 C CG  . TRP   A 1 526 ? -49.45400 -0.14200  42.22900  1.000 86.54166  ? 1138 TRP   A CG  1 
ATOM   3312 C CD1 . TRP   A 1 526 ? -50.20200 0.96000   41.93000  1.000 83.00486  ? 1138 TRP   A CD1 1 
ATOM   3313 C CD2 . TRP   A 1 526 ? -48.32600 -0.11300  41.35300  1.000 92.07950  ? 1138 TRP   A CD2 1 
ATOM   3314 N NE1 . TRP   A 1 526 ? -49.59600 1.68300   40.93000  1.000 85.79681  ? 1138 TRP   A NE1 1 
ATOM   3315 C CE2 . TRP   A 1 526 ? -48.44300 1.04200   40.55800  1.000 90.26294  ? 1138 TRP   A CE2 1 
ATOM   3316 C CE3 . TRP   A 1 526 ? -47.22100 -0.95300  41.16800  1.000 90.40112  ? 1138 TRP   A CE3 1 
ATOM   3317 C CZ2 . TRP   A 1 526 ? -47.49800 1.38000   39.59600  1.000 87.21176  ? 1138 TRP   A CZ2 1 
ATOM   3318 C CZ3 . TRP   A 1 526 ? -46.28700 -0.61600  40.21000  1.000 87.18626  ? 1138 TRP   A CZ3 1 
ATOM   3319 C CH2 . TRP   A 1 526 ? -46.42900 0.53900   39.43700  1.000 86.95288  ? 1138 TRP   A CH2 1 
ATOM   3320 N N   . TYR   A 1 527 ? -50.85000 -3.13500  40.81800  1.000 90.17797  ? 1139 TYR   A N   1 
ATOM   3321 C CA  . TYR   A 1 527 ? -51.06000 -3.24700  39.37700  1.000 93.50520  ? 1139 TYR   A CA  1 
ATOM   3322 C C   . TYR   A 1 527 ? -52.53800 -3.38600  39.03400  1.000 95.37918  ? 1139 TYR   A C   1 
ATOM   3323 O O   . TYR   A 1 527 ? -53.01400 -2.78000  38.06800  1.000 98.95696  ? 1139 TYR   A O   1 
ATOM   3324 C CB  . TYR   A 1 527 ? -50.28100 -4.43400  38.81200  1.000 89.62439  ? 1139 TYR   A CB  1 
ATOM   3325 C CG  . TYR   A 1 527 ? -50.49300 -4.64800  37.32600  1.000 86.46532  ? 1139 TYR   A CG  1 
ATOM   3326 C CD1 . TYR   A 1 527 ? -49.75300 -3.93700  36.39200  1.000 88.40197  ? 1139 TYR   A CD1 1 
ATOM   3327 C CD2 . TYR   A 1 527 ? -51.44600 -5.54900  36.85900  1.000 87.61212  ? 1139 TYR   A CD2 1 
ATOM   3328 C CE1 . TYR   A 1 527 ? -49.94300 -4.12500  35.03400  1.000 91.11377  ? 1139 TYR   A CE1 1 
ATOM   3329 C CE2 . TYR   A 1 527 ? -51.64500 -5.74300  35.50300  1.000 86.63612  ? 1139 TYR   A CE2 1 
ATOM   3330 C CZ  . TYR   A 1 527 ? -50.89000 -5.02700  34.59500  1.000 91.77491  ? 1139 TYR   A CZ  1 
ATOM   3331 O OH  . TYR   A 1 527 ? -51.07900 -5.21100  33.24200  1.000 92.82246  ? 1139 TYR   A OH  1 
ATOM   3332 N N   . ASN   A 1 528 ? -53.28000 -4.18400  39.80000  1.000 95.54371  ? 1140 ASN   A N   1 
ATOM   3333 C CA  . ASN   A 1 528 ? -54.65300 -4.49900  39.42800  1.000 94.37379  ? 1140 ASN   A CA  1 
ATOM   3334 C C   . ASN   A 1 528 ? -55.64300 -3.38900  39.76300  1.000 95.98011  ? 1140 ASN   A C   1 
ATOM   3335 O O   . ASN   A 1 528 ? -56.78900 -3.45500  39.30600  1.000 103.30761 ? 1140 ASN   A O   1 
ATOM   3336 C CB  . ASN   A 1 528 ? -55.08600 -5.80700  40.09600  1.000 97.88629  ? 1140 ASN   A CB  1 
ATOM   3337 C CG  . ASN   A 1 528 ? -54.56700 -7.03400  39.36200  1.000 99.78682  ? 1140 ASN   A CG  1 
ATOM   3338 O OD1 . ASN   A 1 528 ? -54.77100 -7.18400  38.15800  1.000 94.26825  ? 1140 ASN   A OD1 1 
ATOM   3339 N ND2 . ASN   A 1 528 ? -53.87200 -7.90600  40.08400  1.000 103.33054 ? 1140 ASN   A ND2 1 
ATOM   3340 N N   . GLN   A 1 529 ? -55.24000 -2.37500  40.53100  1.000 92.57704  ? 1141 GLN   A N   1 
ATOM   3341 C CA  . GLN   A 1 529 ? -56.13800 -1.26800  40.84600  1.000 88.96293  ? 1141 GLN   A CA  1 
ATOM   3342 C C   . GLN   A 1 529 ? -55.99800 -0.10200  39.87300  1.000 85.28847  ? 1141 GLN   A C   1 
ATOM   3343 O O   . GLN   A 1 529 ? -57.00000 0.52200   39.50700  1.000 85.17579  ? 1141 GLN   A O   1 
ATOM   3344 C CB  . GLN   A 1 529 ? -55.89700 -0.77000  42.27300  1.000 92.90408  ? 1141 GLN   A CB  1 
ATOM   3345 C CG  . GLN   A 1 529 ? -55.55900 -1.85300  43.27300  1.000 92.28802  ? 1141 GLN   A CG  1 
ATOM   3346 C CD  . GLN   A 1 529 ? -55.67800 -1.36400  44.70200  1.000 102.32776 ? 1141 GLN   A CD  1 
ATOM   3347 O OE1 . GLN   A 1 529 ? -56.70300 -0.80300  45.09200  1.000 106.08458 ? 1141 GLN   A OE1 1 
ATOM   3348 N NE2 . GLN   A 1 529 ? -54.62700 -1.56800  45.49000  1.000 103.75734 ? 1141 GLN   A NE2 1 
ATOM   3349 N N   . THR   A 1 530 ? -54.77500 0.21500   39.45600  1.000 79.83217  ? 1142 THR   A N   1 
ATOM   3350 C CA  . THR   A 1 530 ? -54.51900 1.28000   38.48500  1.000 82.39844  ? 1142 THR   A CA  1 
ATOM   3351 C C   . THR   A 1 530 ? -53.69900 0.72500   37.32600  1.000 89.82279  ? 1142 THR   A C   1 
ATOM   3352 O O   . THR   A 1 530 ? -52.55700 1.13900   37.10200  1.000 85.74136  ? 1142 THR   A O   1 
ATOM   3353 C CB  . THR   A 1 530 ? -53.80500 2.45700   39.14800  1.000 74.73034  ? 1142 THR   A CB  1 
ATOM   3354 O OG1 . THR   A 1 530 ? -52.79400 1.96800   40.04000  1.000 79.71962  ? 1142 THR   A OG1 1 
ATOM   3355 C CG2 . THR   A 1 530 ? -54.79500 3.31100   39.92200  1.000 68.03319  ? 1142 THR   A CG2 1 
ATOM   3356 N N   . PRO   A 1 531 ? -54.27200 -0.20200  36.54600  1.000 93.07113  ? 1143 PRO   A N   1 
ATOM   3357 C CA  . PRO   A 1 531 ? -53.44300 -0.97500  35.60100  1.000 85.38572  ? 1143 PRO   A CA  1 
ATOM   3358 C C   . PRO   A 1 531 ? -52.70400 -0.12300  34.58800  1.000 85.27140  ? 1143 PRO   A C   1 
ATOM   3359 O O   . PRO   A 1 531 ? -51.53300 -0.39400  34.29700  1.000 89.97160  ? 1143 PRO   A O   1 
ATOM   3360 C CB  . PRO   A 1 531 ? -54.46100 -1.90800  34.92400  1.000 81.60878  ? 1143 PRO   A CB  1 
ATOM   3361 C CG  . PRO   A 1 531 ? -55.63800 -1.94300  35.84900  1.000 85.92364  ? 1143 PRO   A CG  1 
ATOM   3362 C CD  . PRO   A 1 531 ? -55.69300 -0.58600  36.47300  1.000 89.25186  ? 1143 PRO   A CD  1 
ATOM   3363 N N   . ASN   A 1 532 ? -53.34900 0.91100   34.04800  1.000 86.36046  ? 1144 ASN   A N   1 
ATOM   3364 C CA  . ASN   A 1 532 ? -52.73100 1.67800   32.97200  1.000 84.88304  ? 1144 ASN   A CA  1 
ATOM   3365 C C   . ASN   A 1 532 ? -51.60500 2.56300   33.49500  1.000 84.77415  ? 1144 ASN   A C   1 
ATOM   3366 O O   . ASN   A 1 532 ? -50.50400 2.57600   32.92900  1.000 87.15754  ? 1144 ASN   A O   1 
ATOM   3367 C CB  . ASN   A 1 532 ? -53.79400 2.49800   32.24500  1.000 84.43826  ? 1144 ASN   A CB  1 
ATOM   3368 C CG  . ASN   A 1 532 ? -54.93600 1.63700   31.73800  1.000 90.07021  ? 1144 ASN   A CG  1 
ATOM   3369 O OD1 . ASN   A 1 532 ? -55.71400 1.09500   32.52400  1.000 93.16150  ? 1144 ASN   A OD1 1 
ATOM   3370 N ND2 . ASN   A 1 532 ? -55.03400 1.49400   30.42100  1.000 94.22559  ? 1144 ASN   A ND2 1 
ATOM   3371 N N   . ARG   A 1 533 ? -51.85000 3.30700   34.57800  1.000 80.13576  ? 1145 ARG   A N   1 
ATOM   3372 C CA  . ARG   A 1 533 ? -50.74800 4.04100   35.18700  1.000 76.04302  ? 1145 ARG   A CA  1 
ATOM   3373 C C   . ARG   A 1 533 ? -49.71000 3.09600   35.77700  1.000 78.61454  ? 1145 ARG   A C   1 
ATOM   3374 O O   . ARG   A 1 533 ? -48.54300 3.47800   35.90200  1.000 74.00517  ? 1145 ARG   A O   1 
ATOM   3375 C CB  . ARG   A 1 533 ? -51.25400 5.01300   36.26300  1.000 69.80533  ? 1145 ARG   A CB  1 
ATOM   3376 C CG  . ARG   A 1 533 ? -50.16800 5.97100   36.76600  1.000 63.54228  ? 1145 ARG   A CG  1 
ATOM   3377 C CD  . ARG   A 1 533 ? -49.65300 5.61300   38.16000  1.000 69.56467  ? 1145 ARG   A CD  1 
ATOM   3378 N NE  . ARG   A 1 533 ? -50.50900 6.13400   39.21700  1.000 75.34085  ? 1145 ARG   A NE  1 
ATOM   3379 C CZ  . ARG   A 1 533 ? -50.23400 7.21400   39.93800  1.000 66.27840  ? 1145 ARG   A CZ  1 
ATOM   3380 N NH1 . ARG   A 1 533 ? -49.10100 7.87800   39.78200  1.000 59.41548  ? 1145 ARG   A NH1 1 
ATOM   3381 N NH2 . ARG   A 1 533 ? -51.12000 7.64000   40.83500  1.000 59.48716  ? 1145 ARG   A NH2 1 
ATOM   3382 N N   . ALA   A 1 534 ? -50.10400 1.86500   36.11200  1.000 80.74404  ? 1146 ALA   A N   1 
ATOM   3383 C CA  . ALA   A 1 534 ? -49.13600 0.88700   36.59500  1.000 79.80352  ? 1146 ALA   A CA  1 
ATOM   3384 C C   . ALA   A 1 534 ? -48.12400 0.52900   35.51500  1.000 81.50364  ? 1146 ALA   A C   1 
ATOM   3385 O O   . ALA   A 1 534 ? -46.92600 0.42800   35.79400  1.000 81.06989  ? 1146 ALA   A O   1 
ATOM   3386 C CB  . ALA   A 1 534 ? -49.84700 -0.37000  37.09300  1.000 82.16735  ? 1146 ALA   A CB  1 
ATOM   3387 N N   . LYS   A 1 535 ? -48.57800 0.34400   34.27600  1.000 80.17115  ? 1147 LYS   A N   1 
ATOM   3388 C CA  . LYS   A 1 535 ? -47.66400 -0.09300  33.23000  1.000 79.76196  ? 1147 LYS   A CA  1 
ATOM   3389 C C   . LYS   A 1 535 ? -46.91000 1.05100   32.56700  1.000 78.55784  ? 1147 LYS   A C   1 
ATOM   3390 O O   . LYS   A 1 535 ? -45.82000 0.82400   32.02700  1.000 81.20003  ? 1147 LYS   A O   1 
ATOM   3391 C CB  . LYS   A 1 535 ? -48.40500 -0.90900  32.16700  1.000 80.16413  ? 1147 LYS   A CB  1 
ATOM   3392 C CG  . LYS   A 1 535 ? -47.56500 -2.07100  31.65100  1.000 83.49823  ? 1147 LYS   A CG  1 
ATOM   3393 C CD  . LYS   A 1 535 ? -48.40000 -3.21700  31.11200  1.000 83.33971  ? 1147 LYS   A CD  1 
ATOM   3394 C CE  . LYS   A 1 535 ? -48.12300 -4.48500  31.90600  1.000 78.49866  ? 1147 LYS   A CE  1 
ATOM   3395 N NZ  . LYS   A 1 535 ? -48.38200 -5.72100  31.12300  1.000 79.30052  ? 1147 LYS   A NZ  1 
ATOM   3396 N N   . ARG   A 1 536 ? -47.44700 2.27500   32.58300  1.000 71.94295  ? 1148 ARG   A N   1 
ATOM   3397 C CA  . ARG   A 1 536 ? -46.65700 3.40400   32.09600  1.000 74.92995  ? 1148 ARG   A CA  1 
ATOM   3398 C C   . ARG   A 1 536 ? -45.42100 3.61000   32.96000  1.000 72.04972  ? 1148 ARG   A C   1 
ATOM   3399 O O   . ARG   A 1 536 ? -44.33000 3.89100   32.44800  1.000 61.84073  ? 1148 ARG   A O   1 
ATOM   3400 C CB  . ARG   A 1 536 ? -47.50100 4.67800   32.05100  1.000 69.52668  ? 1148 ARG   A CB  1 
ATOM   3401 C CG  . ARG   A 1 536 ? -48.64100 4.64100   31.04900  1.000 68.71605  ? 1148 ARG   A CG  1 
ATOM   3402 C CD  . ARG   A 1 536 ? -49.12000 6.04200   30.70100  1.000 62.10555  ? 1148 ARG   A CD  1 
ATOM   3403 N NE  . ARG   A 1 536 ? -49.62300 6.76400   31.86200  1.000 63.64534  ? 1148 ARG   A NE  1 
ATOM   3404 C CZ  . ARG   A 1 536 ? -50.87700 6.71400   32.28900  1.000 63.92416  ? 1148 ARG   A CZ  1 
ATOM   3405 N NH1 . ARG   A 1 536 ? -51.78800 5.97400   31.67700  1.000 61.39780  ? 1148 ARG   A NH1 1 
ATOM   3406 N NH2 . ARG   A 1 536 ? -51.22600 7.42300   33.35900  1.000 63.58317  ? 1148 ARG   A NH2 1 
ATOM   3407 N N   . VAL   A 1 537 ? -45.56700 3.45100   34.27300  1.000 79.53317  ? 1149 VAL   A N   1 
ATOM   3408 C CA  . VAL   A 1 537 ? -44.42400 3.60800   35.16000  1.000 76.87211  ? 1149 VAL   A CA  1 
ATOM   3409 C C   . VAL   A 1 537 ? -43.58900 2.32900   35.21200  1.000 73.48019  ? 1149 VAL   A C   1 
ATOM   3410 O O   . VAL   A 1 537 ? -42.37100 2.39000   35.41800  1.000 72.39149  ? 1149 VAL   A O   1 
ATOM   3411 C CB  . VAL   A 1 537 ? -44.90400 4.04400   36.55200  1.000 68.43959  ? 1149 VAL   A CB  1 
ATOM   3412 C CG1 . VAL   A 1 537 ? -45.76700 2.98300   37.16000  1.000 69.60488  ? 1149 VAL   A CG1 1 
ATOM   3413 C CG2 . VAL   A 1 537 ? -43.73100 4.34000   37.44300  1.000 72.73865  ? 1149 VAL   A CG2 1 
ATOM   3414 N N   . ILE   A 1 538 ? -44.21000 1.16200   35.01400  1.000 68.83403  ? 1150 ILE   A N   1 
ATOM   3415 C CA  . ILE   A 1 538 ? -43.43600 -0.07100  34.88500  1.000 74.46730  ? 1150 ILE   A CA  1 
ATOM   3416 C C   . ILE   A 1 538 ? -42.54000 -0.01000  33.65400  1.000 79.37110  ? 1150 ILE   A C   1 
ATOM   3417 O O   . ILE   A 1 538 ? -41.37300 -0.41900  33.69700  1.000 82.50643  ? 1150 ILE   A O   1 
ATOM   3418 C CB  . ILE   A 1 538 ? -44.36800 -1.29800  34.85400  1.000 81.33412  ? 1150 ILE   A CB  1 
ATOM   3419 C CG1 . ILE   A 1 538 ? -44.82000 -1.66800  36.26900  1.000 81.52710  ? 1150 ILE   A CG1 1 
ATOM   3420 C CG2 . ILE   A 1 538 ? -43.69000 -2.49000  34.18800  1.000 78.93525  ? 1150 ILE   A CG2 1 
ATOM   3421 C CD1 . ILE   A 1 538 ? -45.89700 -2.73000  36.30100  1.000 77.53493  ? 1150 ILE   A CD1 1 
ATOM   3422 N N   . THR   A 1 539 ? -43.06200 0.51200   32.54000  1.000 74.72333  ? 1151 THR   A N   1 
ATOM   3423 C CA  . THR   A 1 539 ? -42.23200 0.66000   31.34800  1.000 75.22370  ? 1151 THR   A CA  1 
ATOM   3424 C C   . THR   A 1 539 ? -41.14000 1.70000   31.56600  1.000 70.98848  ? 1151 THR   A C   1 
ATOM   3425 O O   . THR   A 1 539 ? -39.99600 1.50200   31.14200  1.000 77.18545  ? 1151 THR   A O   1 
ATOM   3426 C CB  . THR   A 1 539 ? -43.09500 1.02800   30.14000  1.000 79.88288  ? 1151 THR   A CB  1 
ATOM   3427 O OG1 . THR   A 1 539 ? -44.00300 -0.04400  29.85300  1.000 83.71759  ? 1151 THR   A OG1 1 
ATOM   3428 C CG2 . THR   A 1 539 ? -42.22600 1.28000   28.91600  1.000 67.68343  ? 1151 THR   A CG2 1 
ATOM   3429 N N   . THR   A 1 540 ? -41.46900 2.80900   32.23300  1.000 66.77480  ? 1152 THR   A N   1 
ATOM   3430 C CA  . THR   A 1 540 ? -40.44300 3.78700   32.58000  1.000 67.35720  ? 1152 THR   A CA  1 
ATOM   3431 C C   . THR   A 1 540 ? -39.34400 3.15400   33.42200  1.000 74.22065  ? 1152 THR   A C   1 
ATOM   3432 O O   . THR   A 1 540 ? -38.19200 3.60300   33.38600  1.000 74.29449  ? 1152 THR   A O   1 
ATOM   3433 C CB  . THR   A 1 540 ? -41.07100 4.96300   33.32800  1.000 72.56988  ? 1152 THR   A CB  1 
ATOM   3434 O OG1 . THR   A 1 540 ? -42.27000 5.36600   32.65700  1.000 76.70350  ? 1152 THR   A OG1 1 
ATOM   3435 C CG2 . THR   A 1 540 ? -40.11000 6.14400   33.37500  1.000 68.43738  ? 1152 THR   A CG2 1 
ATOM   3436 N N   . PHE   A 1 541 ? -39.68400 2.10700   34.17900  1.000 76.49357  ? 1153 PHE   A N   1 
ATOM   3437 C CA  . PHE   A 1 541 ? -38.69600 1.35700   34.94300  1.000 73.99384  ? 1153 PHE   A CA  1 
ATOM   3438 C C   . PHE   A 1 541 ? -37.90400 0.40900   34.05200  1.000 74.48430  ? 1153 PHE   A C   1 
ATOM   3439 O O   . PHE   A 1 541 ? -36.67200 0.35200   34.13500  1.000 78.11174  ? 1153 PHE   A O   1 
ATOM   3440 C CB  . PHE   A 1 541 ? -39.38200 0.57200   36.06000  1.000 71.85430  ? 1153 PHE   A CB  1 
ATOM   3441 C CG  . PHE   A 1 541 ? -39.40400 1.28100   37.37500  1.000 73.99898  ? 1153 PHE   A CG  1 
ATOM   3442 C CD1 . PHE   A 1 541 ? -38.30200 2.00400   37.80600  1.000 76.69933  ? 1153 PHE   A CD1 1 
ATOM   3443 C CD2 . PHE   A 1 541 ? -40.51800 1.20900   38.19200  1.000 74.66131  ? 1153 PHE   A CD2 1 
ATOM   3444 C CE1 . PHE   A 1 541 ? -38.31700 2.65400   39.02500  1.000 73.67425  ? 1153 PHE   A CE1 1 
ATOM   3445 C CE2 . PHE   A 1 541 ? -40.54200 1.85600   39.41000  1.000 75.22713  ? 1153 PHE   A CE2 1 
ATOM   3446 C CZ  . PHE   A 1 541 ? -39.43900 2.58000   39.82800  1.000 75.52458  ? 1153 PHE   A CZ  1 
ATOM   3447 N N   . ARG   A 1 542 ? -38.59700 -0.35100  33.20200  1.000 75.18072  ? 1154 ARG   A N   1 
ATOM   3448 C CA  . ARG   A 1 542 ? -37.92800 -1.35400  32.37700  1.000 83.98869  ? 1154 ARG   A CA  1 
ATOM   3449 C C   . ARG   A 1 542 ? -37.03000 -0.70400  31.32800  1.000 82.02085  ? 1154 ARG   A C   1 
ATOM   3450 O O   . ARG   A 1 542 ? -35.81700 -0.94100  31.29600  1.000 77.61638  ? 1154 ARG   A O   1 
ATOM   3451 C CB  . ARG   A 1 542 ? -38.96300 -2.26300  31.70900  1.000 86.98439  ? 1154 ARG   A CB  1 
ATOM   3452 C CG  . ARG   A 1 542 ? -38.35100 -3.37600  30.86500  1.000 89.94361  ? 1154 ARG   A CG  1 
ATOM   3453 C CD  . ARG   A 1 542 ? -39.39200 -4.08400  30.00600  1.000 94.58500  ? 1154 ARG   A CD  1 
ATOM   3454 N NE  . ARG   A 1 542 ? -40.34900 -3.15400  29.42000  1.000 93.70175  ? 1154 ARG   A NE  1 
ATOM   3455 C CZ  . ARG   A 1 542 ? -41.36000 -3.51200  28.64000  1.000 100.43036 ? 1154 ARG   A CZ  1 
ATOM   3456 N NH1 . ARG   A 1 542 ? -41.57000 -4.77800  28.31700  1.000 105.98153 ? 1154 ARG   A NH1 1 
ATOM   3457 N NH2 . ARG   A 1 542 ? -42.18200 -2.57600  28.17300  1.000 98.32536  ? 1154 ARG   A NH2 1 
ATOM   3458 N N   . THR   A 1 543 ? -37.61200 0.12100   30.45600  1.000 84.48017  ? 1155 THR   A N   1 
ATOM   3459 C CA  . THR   A 1 543 ? -36.87800 0.68600   29.33200  1.000 79.13077  ? 1155 THR   A CA  1 
ATOM   3460 C C   . THR   A 1 543 ? -36.03300 1.90300   29.70800  1.000 79.64377  ? 1155 THR   A C   1 
ATOM   3461 O O   . THR   A 1 543 ? -35.25800 2.37300   28.86800  1.000 88.91940  ? 1155 THR   A O   1 
ATOM   3462 C CB  . THR   A 1 543 ? -37.85100 1.05500   28.20300  1.000 74.97717  ? 1155 THR   A CB  1 
ATOM   3463 O OG1 . THR   A 1 543 ? -39.05800 1.59500   28.75700  1.000 72.19293  ? 1155 THR   A OG1 1 
ATOM   3464 C CG2 . THR   A 1 543 ? -38.19700 -0.17400  27.37100  1.000 83.00955  ? 1155 THR   A CG2 1 
ATOM   3465 N N   . GLY   A 1 544 ? -36.15000 2.40800   30.93600  1.000 71.53662  ? 1156 GLY   A N   1 
ATOM   3466 C CA  . GLY   A 1 544 ? -35.40300 3.57800   31.36900  1.000 73.35459  ? 1156 GLY   A CA  1 
ATOM   3467 C C   . GLY   A 1 544 ? -35.54200 4.78600   30.47000  1.000 75.78346  ? 1156 GLY   A C   1 
ATOM   3468 O O   . GLY   A 1 544 ? -34.56200 5.51200   30.26800  1.000 72.00821  ? 1156 GLY   A O   1 
ATOM   3469 N N   . THR   A 1 545 ? -36.73400 5.02300   29.92000  1.000 80.13709  ? 1157 THR   A N   1 
ATOM   3470 C CA  . THR   A 1 545 ? -36.96600 6.09100   28.95700  1.000 75.55282  ? 1157 THR   A CA  1 
ATOM   3471 C C   . THR   A 1 545 ? -38.33600 6.71000   29.19000  1.000 72.57756  ? 1157 THR   A C   1 
ATOM   3472 O O   . THR   A 1 545 ? -39.15700 6.19700   29.95600  1.000 76.91413  ? 1157 THR   A O   1 
ATOM   3473 C CB  . THR   A 1 545 ? -36.87900 5.58000   27.51600  1.000 74.69699  ? 1157 THR   A CB  1 
ATOM   3474 O OG1 . THR   A 1 545 ? -37.15500 6.65400   26.60700  1.000 80.56958  ? 1157 THR   A OG1 1 
ATOM   3475 C CG2 . THR   A 1 545 ? -37.89100 4.47700   27.29900  1.000 71.36559  ? 1157 THR   A CG2 1 
ATOM   3476 N N   . TRP   A 1 546 ? -38.58300 7.81800   28.49500  1.000 68.83866  ? 1158 TRP   A N   1 
ATOM   3477 C CA  . TRP   A 1 546 ? -39.85400 8.51900   28.56000  1.000 64.74176  ? 1158 TRP   A CA  1 
ATOM   3478 C C   . TRP   A 1 546 ? -40.87200 7.98200   27.55700  1.000 68.72944  ? 1158 TRP   A C   1 
ATOM   3479 O O   . TRP   A 1 546 ? -41.85800 8.66800   27.27100  1.000 73.58333  ? 1158 TRP   A O   1 
ATOM   3480 C CB  . TRP   A 1 546 ? -39.64100 10.01700  28.32900  1.000 55.77521  ? 1158 TRP   A CB  1 
ATOM   3481 C CG  . TRP   A 1 546 ? -38.94600 10.73800  29.45400  1.000 66.36312  ? 1158 TRP   A CG  1 
ATOM   3482 C CD1 . TRP   A 1 546 ? -37.77200 11.43200  29.37900  1.000 69.18532  ? 1158 TRP   A CD1 1 
ATOM   3483 C CD2 . TRP   A 1 546 ? -39.38500 10.84400  30.81800  1.000 75.87960  ? 1158 TRP   A CD2 1 
ATOM   3484 N NE1 . TRP   A 1 546 ? -37.45000 11.96100  30.60800  1.000 70.84923  ? 1158 TRP   A NE1 1 
ATOM   3485 C CE2 . TRP   A 1 546 ? -38.42400 11.61400  31.50800  1.000 73.42294  ? 1158 TRP   A CE2 1 
ATOM   3486 C CE3 . TRP   A 1 546 ? -40.49400 10.36200  31.52200  1.000 68.08970  ? 1158 TRP   A CE3 1 
ATOM   3487 C CZ2 . TRP   A 1 546 ? -38.53900 11.91100  32.86400  1.000 71.43723  ? 1158 TRP   A CZ2 1 
ATOM   3488 C CZ3 . TRP   A 1 546 ? -40.60500 10.65700  32.86600  1.000 67.96155  ? 1158 TRP   A CZ3 1 
ATOM   3489 C CH2 . TRP   A 1 546 ? -39.63400 11.42500  33.52400  1.000 69.86255  ? 1158 TRP   A CH2 1 
ATOM   3490 N N   . ASP   A 1 547 ? -40.66100 6.76700   27.03500  1.000 71.31041  ? 1159 ASP   A N   1 
ATOM   3491 C CA  . ASP   A 1 547 ? -41.44400 6.27900   25.90100  1.000 70.71271  ? 1159 ASP   A CA  1 
ATOM   3492 C C   . ASP   A 1 547 ? -42.94400 6.28400   26.17200  1.000 69.99620  ? 1159 ASP   A C   1 
ATOM   3493 O O   . ASP   A 1 547 ? -43.74000 6.36400   25.22900  1.000 66.88407  ? 1159 ASP   A O   1 
ATOM   3494 C CB  . ASP   A 1 547 ? -41.00300 4.86500   25.51300  1.000 70.30461  ? 1159 ASP   A CB  1 
ATOM   3495 C CG  . ASP   A 1 547 ? -39.90300 4.85600   24.46300  1.000 79.92807  ? 1159 ASP   A CG  1 
ATOM   3496 O OD1 . ASP   A 1 547 ? -39.81800 5.81400   23.66500  1.000 85.16872  ? 1159 ASP   A OD1 1 
ATOM   3497 O OD2 . ASP   A 1 547 ? -39.13400 3.87300   24.42100  1.000 83.37211  ? 1159 ASP   A OD2 1 
ATOM   3498 N N   . ALA   A 1 548 ? -43.35800 6.19500   27.43300  1.000 74.95510  ? 1160 ALA   A N   1 
ATOM   3499 C CA  . ALA   A 1 548 ? -44.77100 6.03400   27.74500  1.000 71.88348  ? 1160 ALA   A CA  1 
ATOM   3500 C C   . ALA   A 1 548 ? -45.45900 7.33000   28.14900  1.000 62.81955  ? 1160 ALA   A C   1 
ATOM   3501 O O   . ALA   A 1 548 ? -46.63700 7.29400   28.51600  1.000 65.40218  ? 1160 ALA   A O   1 
ATOM   3502 C CB  . ALA   A 1 548 ? -44.94500 4.99300   28.85700  1.000 69.42703  ? 1160 ALA   A CB  1 
ATOM   3503 N N   . TYR   A 1 549 ? -44.77600 8.46700   28.07400  1.000 57.12118  ? 1161 TYR   A N   1 
ATOM   3504 C CA  . TYR   A 1 549 ? -45.33700 9.70100   28.61500  1.000 67.27217  ? 1161 TYR   A CA  1 
ATOM   3505 C C   . TYR   A 1 549 ? -45.46200 10.80700  27.57600  1.000 59.69944  ? 1161 TYR   A C   1 
ATOM   3506 O O   . TYR   A 1 549 ? -45.03700 11.94000  27.78900  1.000 56.54991  ? 1161 TYR   A O   1 
ATOM   3507 C CB  . TYR   A 1 549 ? -44.48900 10.16900  29.79500  1.000 81.48616  ? 1161 TYR   A CB  1 
ATOM   3508 C CG  . TYR   A 1 549 ? -44.68400 9.30500   31.01900  1.000 81.38648  ? 1161 TYR   A CG  1 
ATOM   3509 C CD1 . TYR   A 1 549 ? -45.90700 8.69500   31.27300  1.000 71.85556  ? 1161 TYR   A CD1 1 
ATOM   3510 C CD2 . TYR   A 1 549 ? -43.63700 9.06500   31.89600  1.000 81.96870  ? 1161 TYR   A CD2 1 
ATOM   3511 C CE1 . TYR   A 1 549 ? -46.09000 7.89100   32.37900  1.000 71.54678  ? 1161 TYR   A CE1 1 
ATOM   3512 C CE2 . TYR   A 1 549 ? -43.80700 8.26000   33.00300  1.000 84.74296  ? 1161 TYR   A CE2 1 
ATOM   3513 C CZ  . TYR   A 1 549 ? -45.03500 7.67600   33.24300  1.000 83.95062  ? 1161 TYR   A CZ  1 
ATOM   3514 O OH  . TYR   A 1 549 ? -45.20400 6.87300   34.35100  1.000 81.43470  ? 1161 TYR   A OH  1 
ATOM   3515 N N   . ASP   B 1 53  ? 3.31300   55.17900  -23.30200 1.000 104.41265 ? 29   ASP   B N   1 
ATOM   3516 C CA  . ASP   B 1 53  ? 2.42000   54.71100  -22.24900 1.000 107.53425 ? 29   ASP   B CA  1 
ATOM   3517 C C   . ASP   B 1 53  ? 3.03200   53.53200  -21.49800 1.000 107.33486 ? 29   ASP   B C   1 
ATOM   3518 O O   . ASP   B 1 53  ? 2.44800   53.03300  -20.53600 1.000 108.75936 ? 29   ASP   B O   1 
ATOM   3519 C CB  . ASP   B 1 53  ? 1.05900   54.31700  -22.82800 1.000 106.38057 ? 29   ASP   B CB  1 
ATOM   3520 C CG  . ASP   B 1 53  ? 1.08700   52.96200  -23.51000 1.000 109.05776 ? 29   ASP   B CG  1 
ATOM   3521 O OD1 . ASP   B 1 53  ? 1.88300   52.78700  -24.45600 1.000 116.36971 ? 29   ASP   B OD1 1 
ATOM   3522 O OD2 . ASP   B 1 53  ? 0.31300   52.07000  -23.09800 1.000 106.13980 ? 29   ASP   B OD2 1 
ATOM   3523 N N   . GLU   B 1 54  ? 4.20700   53.08300  -21.94900 1.000 101.99719 ? 30   GLU   B N   1 
ATOM   3524 C CA  . GLU   B 1 54  ? 4.92300   52.03700  -21.22800 1.000 103.57456 ? 30   GLU   B CA  1 
ATOM   3525 C C   . GLU   B 1 54  ? 5.29500   52.47100  -19.81800 1.000 105.94901 ? 30   GLU   B C   1 
ATOM   3526 O O   . GLU   B 1 54  ? 5.49300   51.61500  -18.94800 1.000 105.65740 ? 30   GLU   B O   1 
ATOM   3527 C CB  . GLU   B 1 54  ? 6.17700   51.62300  -22.00000 1.000 111.86030 ? 30   GLU   B CB  1 
ATOM   3528 C CG  . GLU   B 1 54  ? 5.88300   50.83600  -23.26800 1.000 119.93296 ? 30   GLU   B CG  1 
ATOM   3529 C CD  . GLU   B 1 54  ? 5.00600   49.62400  -23.00300 1.000 122.89696 ? 30   GLU   B CD  1 
ATOM   3530 O OE1 . GLU   B 1 54  ? 5.46300   48.69700  -22.30100 1.000 130.25411 ? 30   GLU   B OE1 1 
ATOM   3531 O OE2 . GLU   B 1 54  ? 3.85400   49.60700  -23.48800 1.000 115.93713 ? 30   GLU   B OE2 1 
ATOM   3532 N N   . VAL   B 1 55  ? 5.40000   53.77900  -19.57800 1.000 103.49795 ? 31   VAL   B N   1 
ATOM   3533 C CA  . VAL   B 1 55  ? 5.54200   54.28100  -18.21400 1.000 100.72800 ? 31   VAL   B CA  1 
ATOM   3534 C C   . VAL   B 1 55  ? 4.30500   53.94000  -17.39100 1.000 100.68678 ? 31   VAL   B C   1 
ATOM   3535 O O   . VAL   B 1 55  ? 4.40600   53.51600  -16.23300 1.000 100.70151 ? 31   VAL   B O   1 
ATOM   3536 C CB  . VAL   B 1 55  ? 5.81700   55.79600  -18.23200 1.000 98.87063  ? 31   VAL   B CB  1 
ATOM   3537 C CG1 . VAL   B 1 55  ? 7.25700   56.06900  -18.63600 1.000 101.50866 ? 31   VAL   B CG1 1 
ATOM   3538 C CG2 . VAL   B 1 55  ? 4.86700   56.49600  -19.20400 1.000 95.05196  ? 31   VAL   B CG2 1 
ATOM   3539 N N   . TRP   B 1 56  ? 3.11800   54.11800  -17.97900 1.000 99.95424  ? 32   TRP   B N   1 
ATOM   3540 C CA  . TRP   B 1 56  ? 1.87600   53.77600  -17.29200 1.000 92.27972  ? 32   TRP   B CA  1 
ATOM   3541 C C   . TRP   B 1 56  ? 1.80800   52.28600  -16.98300 1.000 86.34115  ? 32   TRP   B C   1 
ATOM   3542 O O   . TRP   B 1 56  ? 1.34000   51.88800  -15.91000 1.000 86.76924  ? 32   TRP   B O   1 
ATOM   3543 C CB  . TRP   B 1 56  ? 0.68500   54.20100  -18.15000 1.000 98.40434  ? 32   TRP   B CB  1 
ATOM   3544 C CG  . TRP   B 1 56  ? -0.65300  53.84500  -17.58300 1.000 96.07921  ? 32   TRP   B CG  1 
ATOM   3545 C CD1 . TRP   B 1 56  ? -1.27300  54.42200  -16.51300 1.000 95.87885  ? 32   TRP   B CD1 1 
ATOM   3546 C CD2 . TRP   B 1 56  ? -1.53900  52.82100  -18.05500 1.000 95.34173  ? 32   TRP   B CD2 1 
ATOM   3547 N NE1 . TRP   B 1 56  ? -2.49200  53.82500  -16.29500 1.000 101.13263 ? 32   TRP   B NE1 1 
ATOM   3548 C CE2 . TRP   B 1 56  ? -2.67800  52.83800  -17.22700 1.000 96.82884  ? 32   TRP   B CE2 1 
ATOM   3549 C CE3 . TRP   B 1 56  ? -1.47800  51.89200  -19.10000 1.000 97.83285  ? 32   TRP   B CE3 1 
ATOM   3550 C CZ2 . TRP   B 1 56  ? -3.74900  51.96100  -17.41100 1.000 97.07252  ? 32   TRP   B CZ2 1 
ATOM   3551 C CZ3 . TRP   B 1 56  ? -2.54200  51.02300  -19.28100 1.000 91.59003  ? 32   TRP   B CZ3 1 
ATOM   3552 C CH2 . TRP   B 1 56  ? -3.66200  51.06500  -18.44100 1.000 87.66625  ? 32   TRP   B CH2 1 
ATOM   3553 N N   . VAL   B 1 57  ? 2.27700   51.44900  -17.91300 1.000 84.92939  ? 33   VAL   B N   1 
ATOM   3554 C CA  . VAL   B 1 57  ? 2.19000   49.99900  -17.74500 1.000 86.79648  ? 33   VAL   B CA  1 
ATOM   3555 C C   . VAL   B 1 57  ? 2.97900   49.55200  -16.52100 1.000 86.14240  ? 33   VAL   B C   1 
ATOM   3556 O O   . VAL   B 1 57  ? 2.44900   48.88700  -15.62300 1.000 90.99827  ? 33   VAL   B O   1 
ATOM   3557 C CB  . VAL   B 1 57  ? 2.68100   49.28000  -19.01300 1.000 89.39387  ? 33   VAL   B CB  1 
ATOM   3558 C CG1 . VAL   B 1 57  ? 2.67500   47.77200  -18.80200 1.000 82.71756  ? 33   VAL   B CG1 1 
ATOM   3559 C CG2 . VAL   B 1 57  ? 1.82700   49.66700  -20.20600 1.000 97.69380  ? 33   VAL   B CG2 1 
ATOM   3560 N N   . VAL   B 1 58  ? 4.26500   49.90400  -16.47200 1.000 85.47365  ? 34   VAL   B N   1 
ATOM   3561 C CA  . VAL   B 1 58  ? 5.10300   49.46300  -15.36200 1.000 82.47644  ? 34   VAL   B CA  1 
ATOM   3562 C C   . VAL   B 1 58  ? 4.65000   50.10900  -14.05700 1.000 77.25467  ? 34   VAL   B C   1 
ATOM   3563 O O   . VAL   B 1 58  ? 4.58900   49.44600  -13.01600 1.000 76.16864  ? 34   VAL   B O   1 
ATOM   3564 C CB  . VAL   B 1 58  ? 6.59000   49.73900  -15.66800 1.000 79.52281  ? 34   VAL   B CB  1 
ATOM   3565 C CG1 . VAL   B 1 58  ? 6.85300   51.22900  -15.85400 1.000 86.62243  ? 34   VAL   B CG1 1 
ATOM   3566 C CG2 . VAL   B 1 58  ? 7.48000   49.16000  -14.57600 1.000 71.32488  ? 34   VAL   B CG2 1 
ATOM   3567 N N   . GLY   B 1 59  ? 4.28700   51.39400  -14.09500 1.000 76.63964  ? 35   GLY   B N   1 
ATOM   3568 C CA  . GLY   B 1 59  ? 3.87800   52.07500  -12.87700 1.000 77.87315  ? 35   GLY   B CA  1 
ATOM   3569 C C   . GLY   B 1 59  ? 2.61100   51.49700  -12.27700 1.000 76.88559  ? 35   GLY   B C   1 
ATOM   3570 O O   . GLY   B 1 59  ? 2.50500   51.33800  -11.05700 1.000 77.61810  ? 35   GLY   B O   1 
ATOM   3571 N N   . MET   B 1 60  ? 1.63100   51.17300  -13.12200 1.000 74.93702  ? 36   MET   B N   1 
ATOM   3572 C CA  . MET   B 1 60  ? 0.44000   50.49700  -12.62300 1.000 74.64017  ? 36   MET   B CA  1 
ATOM   3573 C C   . MET   B 1 60  ? 0.76200   49.08700  -12.15500 1.000 72.56807  ? 36   MET   B C   1 
ATOM   3574 O O   . MET   B 1 60  ? 0.15100   48.60100  -11.19600 1.000 73.07894  ? 36   MET   B O   1 
ATOM   3575 C CB  . MET   B 1 60  ? -0.63900  50.46700  -13.70400 1.000 77.32047  ? 36   MET   B CB  1 
ATOM   3576 C CG  . MET   B 1 60  ? -1.24500  51.82900  -14.01600 1.000 82.04200  ? 36   MET   B CG  1 
ATOM   3577 S SD  . MET   B 1 60  ? -1.78100  52.75200  -12.56200 1.000 100.05404 ? 36   MET   B SD  1 
ATOM   3578 C CE  . MET   B 1 60  ? -0.42100  53.90200  -12.33700 1.000 86.97080  ? 36   MET   B CE  1 
ATOM   3579 N N   . GLY   B 1 61  ? 1.71600   48.42300  -12.81000 1.000 66.30784  ? 37   GLY   B N   1 
ATOM   3580 C CA  . GLY   B 1 61  ? 2.12900   47.10700  -12.36000 1.000 67.49561  ? 37   GLY   B CA  1 
ATOM   3581 C C   . GLY   B 1 61  ? 2.59300   47.10400  -10.91500 1.000 66.54364  ? 37   GLY   B C   1 
ATOM   3582 O O   . GLY   B 1 61  ? 2.23100   46.21500  -10.14200 1.000 58.74710  ? 37   GLY   B O   1 
ATOM   3583 N N   . ILE   B 1 62  ? 3.39100   48.10300  -10.52600 1.000 68.63781  ? 38   ILE   B N   1 
ATOM   3584 C CA  . ILE   B 1 62  ? 3.88000   48.14900  -9.15100  1.000 69.06973  ? 38   ILE   B CA  1 
ATOM   3585 C C   . ILE   B 1 62  ? 2.73900   48.45100  -8.18400  1.000 68.86307  ? 38   ILE   B C   1 
ATOM   3586 O O   . ILE   B 1 62  ? 2.68000   47.88900  -7.08400  1.000 63.89883  ? 38   ILE   B O   1 
ATOM   3587 C CB  . ILE   B 1 62  ? 5.04600   49.15500  -9.01100  1.000 70.52740  ? 38   ILE   B CB  1 
ATOM   3588 C CG1 . ILE   B 1 62  ? 4.54800   50.57900  -8.72800  1.000 70.40443  ? 38   ILE   B CG1 1 
ATOM   3589 C CG2 . ILE   B 1 62  ? 5.94700   49.11600  -10.23900 1.000 69.05588  ? 38   ILE   B CG2 1 
ATOM   3590 C CD1 . ILE   B 1 62  ? 5.64700   51.57900  -8.43100  1.000 67.61678  ? 38   ILE   B CD1 1 
ATOM   3591 N N   . VAL   B 1 63  ? 1.80000   49.31300  -8.58100  1.000 68.23690  ? 39   VAL   B N   1 
ATOM   3592 C CA  . VAL   B 1 63  ? 0.69000   49.65300  -7.69600  1.000 63.81404  ? 39   VAL   B CA  1 
ATOM   3593 C C   . VAL   B 1 63  ? -0.21700  48.44600  -7.49900  1.000 59.92178  ? 39   VAL   B C   1 
ATOM   3594 O O   . VAL   B 1 63  ? -0.50600  48.04200  -6.36600  1.000 57.85822  ? 39   VAL   B O   1 
ATOM   3595 C CB  . VAL   B 1 63  ? -0.08700  50.86100  -8.24900  1.000 63.05052  ? 39   VAL   B CB  1 
ATOM   3596 C CG1 . VAL   B 1 63  ? -1.34200  51.09900  -7.43000  1.000 53.68431  ? 39   VAL   B CG1 1 
ATOM   3597 C CG2 . VAL   B 1 63  ? 0.79800   52.10000  -8.24900  1.000 60.12495  ? 39   VAL   B CG2 1 
ATOM   3598 N N   . MET   B 1 64  ? -0.66900  47.84700  -8.60300  1.000 61.31168  ? 40   MET   B N   1 
ATOM   3599 C CA  . MET   B 1 64  ? -1.47700  46.63400  -8.53200  1.000 58.86817  ? 40   MET   B CA  1 
ATOM   3600 C C   . MET   B 1 64  ? -0.75600  45.53600  -7.75700  1.000 59.83542  ? 40   MET   B C   1 
ATOM   3601 O O   . MET   B 1 64  ? -1.34400  44.88600  -6.88400  1.000 60.89845  ? 40   MET   B O   1 
ATOM   3602 C CB  . MET   B 1 64  ? -1.81800  46.16300  -9.94500  1.000 60.21708  ? 40   MET   B CB  1 
ATOM   3603 C CG  . MET   B 1 64  ? -2.76400  47.08600  -10.69400 1.000 62.83069  ? 40   MET   B CG  1 
ATOM   3604 S SD  . MET   B 1 64  ? -3.02700  46.56000  -12.39900 1.000 58.30370  ? 40   MET   B SD  1 
ATOM   3605 C CE  . MET   B 1 64  ? -4.12700  47.84600  -12.98800 1.000 61.36321  ? 40   MET   B CE  1 
ATOM   3606 N N   . SER   B 1 65  ? 0.52700   45.31800  -8.06200  1.000 59.63265  ? 41   SER   B N   1 
ATOM   3607 C CA  . SER   B 1 65  ? 1.28900   44.30800  -7.33400  1.000 55.52442  ? 41   SER   B CA  1 
ATOM   3608 C C   . SER   B 1 65  ? 1.39300   44.66000  -5.85700  1.000 57.64026  ? 41   SER   B C   1 
ATOM   3609 O O   . SER   B 1 65  ? 1.33300   43.77500  -4.99600  1.000 61.95059  ? 41   SER   B O   1 
ATOM   3610 C CB  . SER   B 1 65  ? 2.67900   44.14400  -7.94500  1.000 54.13290  ? 41   SER   B CB  1 
ATOM   3611 O OG  . SER   B 1 65  ? 2.59500   43.68900  -9.28500  1.000 62.97252  ? 41   SER   B OG  1 
ATOM   3612 N N   . LEU   B 1 66  ? 1.55200   45.94900  -5.54200  1.000 55.84447  ? 42   LEU   B N   1 
ATOM   3613 C CA  . LEU   B 1 66  ? 1.48600   46.36500  -4.14400  1.000 52.60371  ? 42   LEU   B CA  1 
ATOM   3614 C C   . LEU   B 1 66  ? 0.11100   46.08000  -3.56100  1.000 55.56314  ? 42   LEU   B C   1 
ATOM   3615 O O   . LEU   B 1 66  ? -0.00400  45.59500  -2.42900  1.000 58.54077  ? 42   LEU   B O   1 
ATOM   3616 C CB  . LEU   B 1 66  ? 1.82400   47.85100  -4.00300  1.000 59.94121  ? 42   LEU   B CB  1 
ATOM   3617 C CG  . LEU   B 1 66  ? 3.28900   48.30200  -4.07300  1.000 60.65309  ? 42   LEU   B CG  1 
ATOM   3618 C CD1 . LEU   B 1 66  ? 3.39700   49.80600  -3.84900  1.000 50.57535  ? 42   LEU   B CD1 1 
ATOM   3619 C CD2 . LEU   B 1 66  ? 4.15200   47.54200  -3.07500  1.000 45.14674  ? 42   LEU   B CD2 1 
ATOM   3620 N N   . ILE   B 1 67  ? -0.94400  46.36600  -4.32600  1.000 54.05738  ? 43   ILE   B N   1 
ATOM   3621 C CA  . ILE   B 1 67  ? -2.30200  46.11200  -3.85200  1.000 50.34404  ? 43   ILE   B CA  1 
ATOM   3622 C C   . ILE   B 1 67  ? -2.49600  44.62700  -3.57300  1.000 49.08591  ? 43   ILE   B C   1 
ATOM   3623 O O   . ILE   B 1 67  ? -3.00400  44.23900  -2.51300  1.000 49.83862  ? 43   ILE   B O   1 
ATOM   3624 C CB  . ILE   B 1 67  ? -3.33200  46.64000  -4.86700  1.000 48.10100  ? 43   ILE   B CB  1 
ATOM   3625 C CG1 . ILE   B 1 67  ? -3.56800  48.13400  -4.64900  1.000 44.55209  ? 43   ILE   B CG1 1 
ATOM   3626 C CG2 . ILE   B 1 67  ? -4.64300  45.86900  -4.76600  1.000 50.28172  ? 43   ILE   B CG2 1 
ATOM   3627 C CD1 . ILE   B 1 67  ? -4.59100  48.72100  -5.58000  1.000 43.40744  ? 43   ILE   B CD1 1 
ATOM   3628 N N   . VAL   B 1 68  ? -2.08200  43.77500  -4.51500  1.000 43.61193  ? 44   VAL   B N   1 
ATOM   3629 C CA  . VAL   B 1 68  ? -2.22200  42.33200  -4.33500  1.000 47.57625  ? 44   VAL   B CA  1 
ATOM   3630 C C   . VAL   B 1 68  ? -1.48500  41.87300  -3.08400  1.000 52.71157  ? 44   VAL   B C   1 
ATOM   3631 O O   . VAL   B 1 68  ? -1.97300  41.01900  -2.33400  1.000 49.37013  ? 44   VAL   B O   1 
ATOM   3632 C CB  . VAL   B 1 68  ? -1.72600  41.58600  -5.58600  1.000 46.83274  ? 44   VAL   B CB  1 
ATOM   3633 C CG1 . VAL   B 1 68  ? -1.64500  40.09000  -5.32000  1.000 41.69713  ? 44   VAL   B CG1 1 
ATOM   3634 C CG2 . VAL   B 1 68  ? -2.64700  41.86400  -6.75900  1.000 54.86054  ? 44   VAL   B CG2 1 
ATOM   3635 N N   . LEU   B 1 69  ? -0.30800  42.44600  -2.82800  1.000 55.84163  ? 45   LEU   B N   1 
ATOM   3636 C CA  . LEU   B 1 69  ? 0.45800   42.04700  -1.65400  1.000 50.84422  ? 45   LEU   B CA  1 
ATOM   3637 C C   . LEU   B 1 69  ? -0.22000  42.49800  -0.36600  1.000 50.22866  ? 45   LEU   B C   1 
ATOM   3638 O O   . LEU   B 1 69  ? -0.32100  41.72000  0.58800   1.000 52.11304  ? 45   LEU   B O   1 
ATOM   3639 C CB  . LEU   B 1 69  ? 1.87700   42.60100  -1.74400  1.000 53.81575  ? 45   LEU   B CB  1 
ATOM   3640 C CG  . LEU   B 1 69  ? 2.95600   41.59400  -1.34800  1.000 57.76411  ? 45   LEU   B CG  1 
ATOM   3641 C CD1 . LEU   B 1 69  ? 2.89100   40.36400  -2.23800  1.000 53.32155  ? 45   LEU   B CD1 1 
ATOM   3642 C CD2 . LEU   B 1 69  ? 4.33000   42.23200  -1.41300  1.000 60.49235  ? 45   LEU   B CD2 1 
ATOM   3643 N N   . ALA   B 1 70  ? -0.70400  43.74500  -0.32600  1.000 51.56653  ? 46   ALA   B N   1 
ATOM   3644 C CA  . ALA   B 1 70  ? -1.34800  44.25700  0.88300   1.000 50.72021  ? 46   ALA   B CA  1 
ATOM   3645 C C   . ALA   B 1 70  ? -2.56400  43.42200  1.26200   1.000 49.38598  ? 46   ALA   B C   1 
ATOM   3646 O O   . ALA   B 1 70  ? -2.81400  43.17900  2.45000   1.000 49.81121  ? 46   ALA   B O   1 
ATOM   3647 C CB  . ALA   B 1 70  ? -1.75000  45.71900  0.69000   1.000 47.49638  ? 46   ALA   B CB  1 
ATOM   3648 N N   . ILE   B 1 71  ? -3.33900  42.98400  0.26800   1.000 43.89903  ? 47   ILE   B N   1 
ATOM   3649 C CA  . ILE   B 1 71  ? -4.46000  42.08800  0.53800   1.000 44.42483  ? 47   ILE   B CA  1 
ATOM   3650 C C   . ILE   B 1 71  ? -3.95700  40.81100  1.20000   1.000 40.54232  ? 47   ILE   B C   1 
ATOM   3651 O O   . ILE   B 1 71  ? -4.35700  40.46500  2.31800   1.000 39.98642  ? 47   ILE   B O   1 
ATOM   3652 C CB  . ILE   B 1 71  ? -5.23200  41.78200  -0.75800  1.000 44.69303  ? 47   ILE   B CB  1 
ATOM   3653 C CG1 . ILE   B 1 71  ? -5.99400  43.01700  -1.24100  1.000 45.21719  ? 47   ILE   B CG1 1 
ATOM   3654 C CG2 . ILE   B 1 71  ? -6.19100  40.62700  -0.55100  1.000 39.44158  ? 47   ILE   B CG2 1 
ATOM   3655 C CD1 . ILE   B 1 71  ? -6.66600  42.82500  -2.59000  1.000 46.59957  ? 47   ILE   B CD1 1 
ATOM   3656 N N   . VAL   B 1 72  ? -3.05100  40.10600  0.52200   1.000 40.14773  ? 48   VAL   B N   1 
ATOM   3657 C CA  . VAL   B 1 72  ? -2.57600  38.82300  1.02900   1.000 41.73357  ? 48   VAL   B CA  1 
ATOM   3658 C C   . VAL   B 1 72  ? -1.85600  38.99600  2.36100   1.000 40.25562  ? 48   VAL   B C   1 
ATOM   3659 O O   . VAL   B 1 72  ? -2.04000  38.19600  3.28500   1.000 39.00818  ? 48   VAL   B O   1 
ATOM   3660 C CB  . VAL   B 1 72  ? -1.68200  38.13500  -0.01900  1.000 42.15626  ? 48   VAL   B CB  1 
ATOM   3661 C CG1 . VAL   B 1 72  ? -1.28600  36.75000  0.45300   1.000 33.68243  ? 48   VAL   B CG1 1 
ATOM   3662 C CG2 . VAL   B 1 72  ? -2.41900  38.04400  -1.34800  1.000 37.97601  ? 48   VAL   B CG2 1 
ATOM   3663 N N   . PHE   B 1 73  ? -1.04100  40.04500  2.49200   1.000 40.49793  ? 49   PHE   B N   1 
ATOM   3664 C CA  . PHE   B 1 73  ? -0.23800  40.20800  3.70200   1.000 38.42462  ? 49   PHE   B CA  1 
ATOM   3665 C C   . PHE   B 1 73  ? -1.12300  40.43200  4.92300   1.000 39.40427  ? 49   PHE   B C   1 
ATOM   3666 O O   . PHE   B 1 73  ? -1.03500  39.69800  5.91400   1.000 36.60558  ? 49   PHE   B O   1 
ATOM   3667 C CB  . PHE   B 1 73  ? 0.75400   41.36100  3.53200   1.000 35.07845  ? 49   PHE   B CB  1 
ATOM   3668 C CG  . PHE   B 1 73  ? 1.58600   41.62800  4.75400   1.000 32.12242  ? 49   PHE   B CG  1 
ATOM   3669 C CD1 . PHE   B 1 73  ? 2.66500   40.81700  5.06500   1.000 34.49040  ? 49   PHE   B CD1 1 
ATOM   3670 C CD2 . PHE   B 1 73  ? 1.29100   42.69000  5.59200   1.000 35.28475  ? 49   PHE   B CD2 1 
ATOM   3671 C CE1 . PHE   B 1 73  ? 3.43100   41.06000  6.19400   1.000 32.79918  ? 49   PHE   B CE1 1 
ATOM   3672 C CE2 . PHE   B 1 73  ? 2.05400   42.93900  6.72200   1.000 35.94013  ? 49   PHE   B CE2 1 
ATOM   3673 C CZ  . PHE   B 1 73  ? 3.12400   42.12300  7.02100   1.000 32.84268  ? 49   PHE   B CZ  1 
ATOM   3674 N N   . GLY   B 1 74  ? -1.99200  41.44300  4.86500   1.000 40.97968  ? 50   GLY   B N   1 
ATOM   3675 C CA  . GLY   B 1 74  ? -2.79600  41.78100  6.02800   1.000 36.90851  ? 50   GLY   B CA  1 
ATOM   3676 C C   . GLY   B 1 74  ? -3.79900  40.70300  6.39600   1.000 34.54932  ? 50   GLY   B C   1 
ATOM   3677 O O   . GLY   B 1 74  ? -4.01600  40.42300  7.57500   1.000 37.69293  ? 50   GLY   B O   1 
ATOM   3678 N N   . ASN   B 1 75  ? -4.43500  40.09300  5.39600   1.000 35.43154  ? 51   ASN   B N   1 
ATOM   3679 C CA  . ASN   B 1 75  ? -5.45300  39.09200  5.69200   1.000 34.39215  ? 51   ASN   B CA  1 
ATOM   3680 C C   . ASN   B 1 75  ? -4.84100  37.84100  6.30800   1.000 35.41973  ? 51   ASN   B C   1 
ATOM   3681 O O   . ASN   B 1 75  ? -5.39100  37.28900  7.26500   1.000 40.14792  ? 51   ASN   B O   1 
ATOM   3682 C CB  . ASN   B 1 75  ? -6.24000  38.75100  4.43100   1.000 39.07601  ? 51   ASN   B CB  1 
ATOM   3683 C CG  . ASN   B 1 75  ? -7.30600  39.77300  4.13100   1.000 44.33907  ? 51   ASN   B CG  1 
ATOM   3684 O OD1 . ASN   B 1 75  ? -7.26500  40.44600  3.10300   1.000 42.00192  ? 51   ASN   B OD1 1 
ATOM   3685 N ND2 . ASN   B 1 75  ? -8.27200  39.90200  5.03600   1.000 49.53010  ? 51   ASN   B ND2 1 
ATOM   3686 N N   . VAL   B 1 76  ? -3.70600  37.37600  5.77900   1.000 37.16913  ? 52   VAL   B N   1 
ATOM   3687 C CA  . VAL   B 1 76  ? -3.00700  36.25900  6.41200   1.000 35.43232  ? 52   VAL   B CA  1 
ATOM   3688 C C   . VAL   B 1 76  ? -2.58800  36.62900  7.82600   1.000 36.01570  ? 52   VAL   B C   1 
ATOM   3689 O O   . VAL   B 1 76  ? -2.56600  35.77700  8.72200   1.000 40.40441  ? 52   VAL   B O   1 
ATOM   3690 C CB  . VAL   B 1 76  ? -1.79300  35.82100  5.56900   1.000 42.48137  ? 52   VAL   B CB  1 
ATOM   3691 C CG1 . VAL   B 1 76  ? -0.97900  34.78200  6.31600   1.000 35.39965  ? 52   VAL   B CG1 1 
ATOM   3692 C CG2 . VAL   B 1 76  ? -2.24800  35.24400  4.24600   1.000 39.89597  ? 52   VAL   B CG2 1 
ATOM   3693 N N   . LEU   B 1 77  ? -2.26400  37.90200  8.05500   1.000 38.48850  ? 53   LEU   B N   1 
ATOM   3694 C CA  . LEU   B 1 77  ? -1.93000  38.34500  9.40400   1.000 38.38094  ? 53   LEU   B CA  1 
ATOM   3695 C C   . LEU   B 1 77  ? -3.12600  38.19000  10.33800  1.000 36.27850  ? 53   LEU   B C   1 
ATOM   3696 O O   . LEU   B 1 77  ? -2.96300  37.86700  11.52100  1.000 39.16377  ? 53   LEU   B O   1 
ATOM   3697 C CB  . LEU   B 1 77  ? -1.44800  39.79600  9.35900   1.000 35.71693  ? 53   LEU   B CB  1 
ATOM   3698 C CG  . LEU   B 1 77  ? -0.82900  40.43600  10.59700  1.000 40.01501  ? 53   LEU   B CG  1 
ATOM   3699 C CD1 . LEU   B 1 77  ? 0.25500   39.54000  11.15000  1.000 42.98295  ? 53   LEU   B CD1 1 
ATOM   3700 C CD2 . LEU   B 1 77  ? -0.26600  41.80700  10.25100  1.000 36.78932  ? 53   LEU   B CD2 1 
ATOM   3701 N N   . VAL   B 1 78  ? -4.33900  38.40000  9.81700   1.000 31.90379  ? 54   VAL   B N   1 
ATOM   3702 C CA  . VAL   B 1 78  ? -5.54600  38.20800  10.61500  1.000 27.23038  ? 54   VAL   B CA  1 
ATOM   3703 C C   . VAL   B 1 78  ? -5.79400  36.72600  10.85900  1.000 28.05131  ? 54   VAL   B C   1 
ATOM   3704 O O   . VAL   B 1 78  ? -6.04100  36.29900  11.99300  1.000 29.22430  ? 54   VAL   B O   1 
ATOM   3705 C CB  . VAL   B 1 78  ? -6.75600  38.86800  9.92800   1.000 29.17587  ? 54   VAL   B CB  1 
ATOM   3706 C CG1 . VAL   B 1 78  ? -8.03700  38.54200  10.67900  1.000 27.73910  ? 54   VAL   B CG1 1 
ATOM   3707 C CG2 . VAL   B 1 78  ? -6.55900  40.36700  9.83400   1.000 35.79860  ? 54   VAL   B CG2 1 
ATOM   3708 N N   . ILE   B 1 79  ? -5.73600  35.92000  9.79600   1.000 26.38999  ? 55   ILE   B N   1 
ATOM   3709 C CA  . ILE   B 1 79  ? -6.01200  34.49200  9.92700   1.000 25.97910  ? 55   ILE   B CA  1 
ATOM   3710 C C   . ILE   B 1 79  ? -5.02700  33.84400  10.89400  1.000 31.87772  ? 55   ILE   B C   1 
ATOM   3711 O O   . ILE   B 1 79  ? -5.39700  32.96500  11.68400  1.000 33.37224  ? 55   ILE   B O   1 
ATOM   3712 C CB  . ILE   B 1 79  ? -5.99000  33.81200  8.54300   1.000 24.54635  ? 55   ILE   B CB  1 
ATOM   3713 C CG1 . ILE   B 1 79  ? -7.08400  34.38200  7.64200   1.000 25.29101  ? 55   ILE   B CG1 1 
ATOM   3714 C CG2 . ILE   B 1 79  ? -6.16400  32.31300  8.66700   1.000 21.35411  ? 55   ILE   B CG2 1 
ATOM   3715 C CD1 . ILE   B 1 79  ? -6.61800  34.69900  6.24200   1.000 34.81949  ? 55   ILE   B CD1 1 
ATOM   3716 N N   . THR   B 1 80  ? -3.76500  34.28200  10.86600  1.000 32.30281  ? 56   THR   B N   1 
ATOM   3717 C CA  . THR   B 1 80  ? -2.77000  33.72900  11.78100  1.000 34.41206  ? 56   THR   B CA  1 
ATOM   3718 C C   . THR   B 1 80  ? -3.04300  34.14500  13.22200  1.000 37.51092  ? 56   THR   B C   1 
ATOM   3719 O O   . THR   B 1 80  ? -2.93300  33.32700  14.14200  1.000 33.87490  ? 56   THR   B O   1 
ATOM   3720 C CB  . THR   B 1 80  ? -1.36700  34.16500  11.36000  1.000 27.63062  ? 56   THR   B CB  1 
ATOM   3721 O OG1 . THR   B 1 80  ? -1.17200  33.85700  9.97700   1.000 36.24525  ? 56   THR   B OG1 1 
ATOM   3722 C CG2 . THR   B 1 80  ? -0.31000  33.45200  12.18700  1.000 30.01597  ? 56   THR   B CG2 1 
ATOM   3723 N N   . ALA   B 1 81  ? -3.39900  35.41400  13.43600  1.000 33.29366  ? 57   ALA   B N   1 
ATOM   3724 C CA  . ALA   B 1 81  ? -3.60200  35.90200  14.79500  1.000 32.20426  ? 57   ALA   B CA  1 
ATOM   3725 C C   . ALA   B 1 81  ? -4.77600  35.19800  15.46800  1.000 42.28515  ? 57   ALA   B C   1 
ATOM   3726 O O   . ALA   B 1 81  ? -4.68900  34.81400  16.64000  1.000 43.41514  ? 57   ALA   B O   1 
ATOM   3727 C CB  . ALA   B 1 81  ? -3.80900  37.41600  14.77800  1.000 31.99372  ? 57   ALA   B CB  1 
ATOM   3728 N N   . ILE   B 1 82  ? -5.88200  35.01300  14.74300  1.000 35.23300  ? 58   ILE   B N   1 
ATOM   3729 C CA  . ILE   B 1 82  ? -7.02900  34.33200  15.33500  1.000 32.35970  ? 58   ILE   B CA  1 
ATOM   3730 C C   . ILE   B 1 82  ? -6.72300  32.85200  15.53600  1.000 32.48612  ? 58   ILE   B C   1 
ATOM   3731 O O   . ILE   B 1 82  ? -7.21700  32.22900  16.48400  1.000 38.19971  ? 58   ILE   B O   1 
ATOM   3732 C CB  . ILE   B 1 82  ? -8.28300  34.56500  14.46700  1.000 27.76949  ? 58   ILE   B CB  1 
ATOM   3733 C CG1 . ILE   B 1 82  ? -8.80300  35.98700  14.67500  1.000 23.71084  ? 58   ILE   B CG1 1 
ATOM   3734 C CG2 . ILE   B 1 82  ? -9.37700  33.56000  14.78900  1.000 21.35411  ? 58   ILE   B CG2 1 
ATOM   3735 C CD1 . ILE   B 1 82  ? -9.87800  36.39300  13.70600  1.000 26.94169  ? 58   ILE   B CD1 1 
ATOM   3736 N N   . ALA   B 1 83  ? -5.87900  32.27400  14.68300  1.000 33.59491  ? 59   ALA   B N   1 
ATOM   3737 C CA  . ALA   B 1 83  ? -5.51700  30.87200  14.84100  1.000 37.05860  ? 59   ALA   B CA  1 
ATOM   3738 C C   . ALA   B 1 83  ? -4.53500  30.65300  15.98600  1.000 41.23485  ? 59   ALA   B C   1 
ATOM   3739 O O   . ALA   B 1 83  ? -4.57300  29.59700  16.62600  1.000 50.55075  ? 59   ALA   B O   1 
ATOM   3740 C CB  . ALA   B 1 83  ? -4.93200  30.32100  13.53700  1.000 35.89294  ? 59   ALA   B CB  1 
ATOM   3741 N N   . LYS   B 1 84  ? -3.65500  31.62000  16.26100  1.000 42.08199  ? 60   LYS   B N   1 
ATOM   3742 C CA  . LYS   B 1 84  ? -2.69000  31.48900  17.34900  1.000 43.80745  ? 60   LYS   B CA  1 
ATOM   3743 C C   . LYS   B 1 84  ? -3.33000  31.56400  18.72100  1.000 45.65300  ? 60   LYS   B C   1 
ATOM   3744 O O   . LYS   B 1 84  ? -3.35800  30.57800  19.46300  1.000 46.69671  ? 60   LYS   B O   1 
ATOM   3745 C CB  . LYS   B 1 84  ? -1.62300  32.58700  17.27600  1.000 46.58461  ? 60   LYS   B CB  1 
ATOM   3746 C CG  . LYS   B 1 84  ? -0.59200  32.47800  16.17900  1.000 46.50117  ? 60   LYS   B CG  1 
ATOM   3747 C CD  . LYS   B 1 84  ? 0.01300   31.10100  16.09100  1.000 47.75877  ? 60   LYS   B CD  1 
ATOM   3748 C CE  . LYS   B 1 84  ? -0.61300  30.30200  14.95600  1.000 53.41222  ? 60   LYS   B CE  1 
ATOM   3749 N NZ  . LYS   B 1 84  ? 0.30700   29.25900  14.38200  1.000 72.00931  ? 60   LYS   B NZ  1 
ATOM   3750 N N   . PHE   B 1 85  ? -3.84700  32.74400  19.05000  1.000 39.64273  ? 61   PHE   B N   1 
ATOM   3751 C CA  . PHE   B 1 85  ? -4.07000  33.13900  20.43000  1.000 40.40999  ? 61   PHE   B CA  1 
ATOM   3752 C C   . PHE   B 1 85  ? -5.42200  32.64800  20.91900  1.000 42.69360  ? 61   PHE   B C   1 
ATOM   3753 O O   . PHE   B 1 85  ? -6.43400  32.80400  20.22900  1.000 48.27429  ? 61   PHE   B O   1 
ATOM   3754 C CB  . PHE   B 1 85  ? -3.97000  34.65700  20.55600  1.000 43.64944  ? 61   PHE   B CB  1 
ATOM   3755 C CG  . PHE   B 1 85  ? -2.68300  35.21800  20.02900  1.000 43.75161  ? 61   PHE   B CG  1 
ATOM   3756 C CD1 . PHE   B 1 85  ? -1.57300  35.32100  20.85100  1.000 46.60249  ? 61   PHE   B CD1 1 
ATOM   3757 C CD2 . PHE   B 1 85  ? -2.56900  35.60600  18.70700  1.000 44.08815  ? 61   PHE   B CD2 1 
ATOM   3758 C CE1 . PHE   B 1 85  ? -0.38200  35.81800  20.37100  1.000 44.14246  ? 61   PHE   B CE1 1 
ATOM   3759 C CE2 . PHE   B 1 85  ? -1.37700  36.10600  18.22000  1.000 51.07619  ? 61   PHE   B CE2 1 
ATOM   3760 C CZ  . PHE   B 1 85  ? -0.28300  36.21100  19.05500  1.000 50.93356  ? 61   PHE   B CZ  1 
ATOM   3761 N N   . GLU   B 1 86  ? -5.43100  32.05600  22.11400  1.000 45.23924  ? 62   GLU   B N   1 
ATOM   3762 C CA  . GLU   B 1 86  ? -6.68600  31.58000  22.68100  1.000 45.93478  ? 62   GLU   B CA  1 
ATOM   3763 C C   . GLU   B 1 86  ? -7.56900  32.74200  23.11100  1.000 41.46976  ? 62   GLU   B C   1 
ATOM   3764 O O   . GLU   B 1 86  ? -8.79700  32.66200  22.99200  1.000 37.74472  ? 62   GLU   B O   1 
ATOM   3765 C CB  . GLU   B 1 86  ? -6.41500  30.64800  23.86000  1.000 38.71889  ? 62   GLU   B CB  1 
ATOM   3766 C CG  . GLU   B 1 86  ? -5.40200  29.56000  23.56300  1.000 45.93456  ? 62   GLU   B CG  1 
ATOM   3767 C CD  . GLU   B 1 86  ? -5.82700  28.20600  24.09000  1.000 58.90052  ? 62   GLU   B CD  1 
ATOM   3768 O OE1 . GLU   B 1 86  ? -5.93200  28.04300  25.32600  1.000 65.36865  ? 62   GLU   B OE1 1 
ATOM   3769 O OE2 . GLU   B 1 86  ? -6.04700  27.30000  23.26100  1.000 65.88861  ? 62   GLU   B OE2 1 
ATOM   3770 N N   . ARG   B 1 87  ? -6.96000  33.83000  23.59000  1.000 43.11344  ? 63   ARG   B N   1 
ATOM   3771 C CA  . ARG   B 1 87  ? -7.68100  35.05900  23.89700  1.000 42.26125  ? 63   ARG   B CA  1 
ATOM   3772 C C   . ARG   B 1 87  ? -8.57200  35.51900  22.74900  1.000 47.44674  ? 63   ARG   B C   1 
ATOM   3773 O O   . ARG   B 1 87  ? -9.55400  36.23200  22.99000  1.000 47.24259  ? 63   ARG   B O   1 
ATOM   3774 C CB  . ARG   B 1 87  ? -6.66800  36.15700  24.24300  1.000 40.43762  ? 63   ARG   B CB  1 
ATOM   3775 C CG  . ARG   B 1 87  ? -7.24000  37.37600  24.94300  1.000 49.69482  ? 63   ARG   B CG  1 
ATOM   3776 C CD  . ARG   B 1 87  ? -6.12900  38.30700  25.42600  1.000 58.14474  ? 63   ARG   B CD  1 
ATOM   3777 N NE  . ARG   B 1 87  ? -4.99900  37.58200  26.00000  1.000 73.49678  ? 63   ARG   B NE  1 
ATOM   3778 C CZ  . ARG   B 1 87  ? -5.02000  36.92700  27.15400  1.000 67.79467  ? 63   ARG   B CZ  1 
ATOM   3779 N NH1 . ARG   B 1 87  ? -6.09700  36.91500  27.92400  1.000 55.86603  ? 63   ARG   B NH1 1 
ATOM   3780 N NH2 . ARG   B 1 87  ? -3.93200  36.26800  27.54500  1.000 57.97302  ? 63   ARG   B NH2 1 
ATOM   3781 N N   . LEU   B 1 88  ? -8.26200  35.12100  21.51300  1.000 37.82186  ? 64   LEU   B N   1 
ATOM   3782 C CA  . LEU   B 1 88  ? -8.98100  35.57600  20.33100  1.000 41.80833  ? 64   LEU   B CA  1 
ATOM   3783 C C   . LEU   B 1 88  ? -10.03400 34.58900  19.83900  1.000 41.93183  ? 64   LEU   B C   1 
ATOM   3784 O O   . LEU   B 1 88  ? -10.69900 34.86900  18.83600  1.000 37.95159  ? 64   LEU   B O   1 
ATOM   3785 C CB  . LEU   B 1 88  ? -7.99400  35.86500  19.19300  1.000 38.29965  ? 64   LEU   B CB  1 
ATOM   3786 C CG  . LEU   B 1 88  ? -6.97500  36.98600  19.40500  1.000 38.91600  ? 64   LEU   B CG  1 
ATOM   3787 C CD1 . LEU   B 1 88  ? -6.19900  37.24100  18.11600  1.000 36.40187  ? 64   LEU   B CD1 1 
ATOM   3788 C CD2 . LEU   B 1 88  ? -7.63000  38.26500  19.91200  1.000 34.26744  ? 64   LEU   B CD2 1 
ATOM   3789 N N   . GLN   B 1 89  ? -10.20200 33.44700  20.50400  1.000 42.10186  ? 65   GLN   B N   1 
ATOM   3790 C CA  . GLN   B 1 89  ? -11.18100 32.44400  20.08000  1.000 41.84737  ? 65   GLN   B CA  1 
ATOM   3791 C C   . GLN   B 1 89  ? -12.58100 32.88800  20.49700  1.000 42.52773  ? 65   GLN   B C   1 
ATOM   3792 O O   . GLN   B 1 89  ? -13.11700 32.47600  21.52700  1.000 47.93077  ? 65   GLN   B O   1 
ATOM   3793 C CB  . GLN   B 1 89  ? -10.84100 31.08100  20.66900  1.000 50.29827  ? 65   GLN   B CB  1 
ATOM   3794 C CG  . GLN   B 1 89  ? -9.40100  30.65000  20.45600  1.000 44.59660  ? 65   GLN   B CG  1 
ATOM   3795 C CD  . GLN   B 1 89  ? -9.14900  30.22300  19.03400  1.000 41.59995  ? 65   GLN   B CD  1 
ATOM   3796 O OE1 . GLN   B 1 89  ? -9.98500  29.55700  18.42300  1.000 49.30086  ? 65   GLN   B OE1 1 
ATOM   3797 N NE2 . GLN   B 1 89  ? -7.99600  30.60000  18.49400  1.000 45.28534  ? 65   GLN   B NE2 1 
ATOM   3798 N N   . THR   B 1 90  ? -13.18400 33.74400  19.67100  1.000 43.04477  ? 66   THR   B N   1 
ATOM   3799 C CA  . THR   B 1 90  ? -14.56000 34.18400  19.85700  1.000 39.28618  ? 66   THR   B CA  1 
ATOM   3800 C C   . THR   B 1 90  ? -15.33900 33.94800  18.57100  1.000 39.12648  ? 66   THR   B C   1 
ATOM   3801 O O   . THR   B 1 90  ? -14.76800 33.95200  17.47700  1.000 44.12130  ? 66   THR   B O   1 
ATOM   3802 C CB  . THR   B 1 90  ? -14.64900 35.66900  20.24200  1.000 40.69354  ? 66   THR   B CB  1 
ATOM   3803 O OG1 . THR   B 1 90  ? -14.56000 36.47700  19.06000  1.000 38.93242  ? 66   THR   B OG1 1 
ATOM   3804 C CG2 . THR   B 1 90  ? -13.52800 36.04600  21.19300  1.000 36.97965  ? 66   THR   B CG2 1 
ATOM   3805 N N   . VAL   B 1 91  ? -16.65300 33.73600  18.71400  1.000 43.23708  ? 67   VAL   B N   1 
ATOM   3806 C CA  . VAL   B 1 91  ? -17.49600 33.46000  17.54900  1.000 42.86942  ? 67   VAL   B CA  1 
ATOM   3807 C C   . VAL   B 1 91  ? -17.37500 34.58500  16.52900  1.000 43.55586  ? 67   VAL   B C   1 
ATOM   3808 O O   . VAL   B 1 91  ? -17.21600 34.34100  15.32600  1.000 35.76267  ? 67   VAL   B O   1 
ATOM   3809 C CB  . VAL   B 1 91  ? -18.95800 33.23600  17.97700  1.000 33.44370  ? 67   VAL   B CB  1 
ATOM   3810 C CG1 . VAL   B 1 91  ? -19.90000 33.53600  16.82700  1.000 36.04697  ? 67   VAL   B CG1 1 
ATOM   3811 C CG2 . VAL   B 1 91  ? -19.15600 31.80500  18.44700  1.000 36.76345  ? 67   VAL   B CG2 1 
ATOM   3812 N N   . THR   B 1 92  ? -17.42500 35.83600  16.99900  1.000 44.09840  ? 68   THR   B N   1 
ATOM   3813 C CA  . THR   B 1 92  ? -17.24700 36.97200  16.09900  1.000 41.55890  ? 68   THR   B CA  1 
ATOM   3814 C C   . THR   B 1 92  ? -15.92000 36.88300  15.35700  1.000 41.34360  ? 68   THR   B C   1 
ATOM   3815 O O   . THR   B 1 92  ? -15.85100 37.18000  14.15800  1.000 43.25887  ? 68   THR   B O   1 
ATOM   3816 C CB  . THR   B 1 92  ? -17.34100 38.28500  16.87700  1.000 41.39762  ? 68   THR   B CB  1 
ATOM   3817 O OG1 . THR   B 1 92  ? -18.67900 38.46100  17.35500  1.000 42.10192  ? 68   THR   B OG1 1 
ATOM   3818 C CG2 . THR   B 1 92  ? -16.96500 39.46700  15.99000  1.000 38.32905  ? 68   THR   B CG2 1 
ATOM   3819 N N   . ASN   B 1 93  ? -14.85500 36.45900  16.04800  1.000 42.88652  ? 69   ASN   B N   1 
ATOM   3820 C CA  . ASN   B 1 93  ? -13.56800 36.28500  15.37800  1.000 39.62256  ? 69   ASN   B CA  1 
ATOM   3821 C C   . ASN   B 1 93  ? -13.61900 35.18000  14.33100  1.000 36.36448  ? 69   ASN   B C   1 
ATOM   3822 O O   . ASN   B 1 93  ? -12.93500 35.27400  13.30600  1.000 32.67594  ? 69   ASN   B O   1 
ATOM   3823 C CB  . ASN   B 1 93  ? -12.46500 35.98700  16.39600  1.000 35.32645  ? 69   ASN   B CB  1 
ATOM   3824 C CG  . ASN   B 1 93  ? -11.87900 37.24500  17.01200  1.000 34.32327  ? 69   ASN   B CG  1 
ATOM   3825 O OD1 . ASN   B 1 93  ? -12.19000 38.35900  16.59400  1.000 37.92496  ? 69   ASN   B OD1 1 
ATOM   3826 N ND2 . ASN   B 1 93  ? -11.00900 37.07000  17.99700  1.000 32.73749  ? 69   ASN   B ND2 1 
ATOM   3827 N N   . TYR   B 1 94  ? -14.41300 34.13100  14.56400  1.000 40.25455  ? 70   TYR   B N   1 
ATOM   3828 C CA  . TYR   B 1 94  ? -14.52500 33.06300  13.57300  1.000 40.90947  ? 70   TYR   B CA  1 
ATOM   3829 C C   . TYR   B 1 94  ? -15.17900 33.56300  12.29200  1.000 37.30398  ? 70   TYR   B C   1 
ATOM   3830 O O   . TYR   B 1 94  ? -14.78100 33.16600  11.19100  1.000 39.64392  ? 70   TYR   B O   1 
ATOM   3831 C CB  . TYR   B 1 94  ? -15.30800 31.87700  14.13800  1.000 37.67283  ? 70   TYR   B CB  1 
ATOM   3832 C CG  . TYR   B 1 94  ? -14.54500 31.01800  15.12300  1.000 32.13222  ? 70   TYR   B CG  1 
ATOM   3833 C CD1 . TYR   B 1 94  ? -13.44000 31.50900  15.79900  1.000 33.55680  ? 70   TYR   B CD1 1 
ATOM   3834 C CD2 . TYR   B 1 94  ? -14.92600 29.70500  15.36000  1.000 39.72045  ? 70   TYR   B CD2 1 
ATOM   3835 C CE1 . TYR   B 1 94  ? -12.74400 30.72400  16.69900  1.000 41.77579  ? 70   TYR   B CE1 1 
ATOM   3836 C CE2 . TYR   B 1 94  ? -14.23700 28.90800  16.25400  1.000 47.22008  ? 70   TYR   B CE2 1 
ATOM   3837 C CZ  . TYR   B 1 94  ? -13.14500 29.42200  16.92200  1.000 49.24010  ? 70   TYR   B CZ  1 
ATOM   3838 O OH  . TYR   B 1 94  ? -12.45400 28.63200  17.81700  1.000 49.29323  ? 70   TYR   B OH  1 
ATOM   3839 N N   . PHE   B 1 95  ? -16.18800 34.42700  12.41100  1.000 34.58905  ? 71   PHE   B N   1 
ATOM   3840 C CA  . PHE   B 1 95  ? -16.76000 35.04100  11.21900  1.000 38.00766  ? 71   PHE   B CA  1 
ATOM   3841 C C   . PHE   B 1 95  ? -15.74900 35.95500  10.54000  1.000 35.63428  ? 71   PHE   B C   1 
ATOM   3842 O O   . PHE   B 1 95  ? -15.66900 35.99600  9.30700   1.000 36.71314  ? 71   PHE   B O   1 
ATOM   3843 C CB  . PHE   B 1 95  ? -18.02900 35.81500  11.57500  1.000 38.33185  ? 71   PHE   B CB  1 
ATOM   3844 C CG  . PHE   B 1 95  ? -19.11200 34.96800  12.17500  1.000 39.64231  ? 71   PHE   B CG  1 
ATOM   3845 C CD1 . PHE   B 1 95  ? -19.29400 33.65700  11.76600  1.000 37.81110  ? 71   PHE   B CD1 1 
ATOM   3846 C CD2 . PHE   B 1 95  ? -19.95400 35.48400  13.14600  1.000 39.51853  ? 71   PHE   B CD2 1 
ATOM   3847 C CE1 . PHE   B 1 95  ? -20.29300 32.87300  12.31800  1.000 34.90612  ? 71   PHE   B CE1 1 
ATOM   3848 C CE2 . PHE   B 1 95  ? -20.95300 34.70800  13.69700  1.000 39.39768  ? 71   PHE   B CE2 1 
ATOM   3849 C CZ  . PHE   B 1 95  ? -21.12200 33.40000  13.28200  1.000 40.85226  ? 71   PHE   B CZ  1 
ATOM   3850 N N   . ILE   B 1 96  ? -14.96800 36.69300  11.33100  1.000 31.59452  ? 72   ILE   B N   1 
ATOM   3851 C CA  . ILE   B 1 96  ? -13.93000 37.55400  10.77300  1.000 36.38351  ? 72   ILE   B CA  1 
ATOM   3852 C C   . ILE   B 1 96  ? -12.86800 36.72200  10.06500  1.000 33.61458  ? 72   ILE   B C   1 
ATOM   3853 O O   . ILE   B 1 96  ? -12.30200 37.14800  9.05000   1.000 32.08499  ? 72   ILE   B O   1 
ATOM   3854 C CB  . ILE   B 1 96  ? -13.33100 38.43200  11.89100  1.000 36.67647  ? 72   ILE   B CB  1 
ATOM   3855 C CG1 . ILE   B 1 96  ? -14.19900 39.66700  12.11300  1.000 35.83656  ? 72   ILE   B CG1 1 
ATOM   3856 C CG2 . ILE   B 1 96  ? -11.90500 38.85000  11.56300  1.000 38.18405  ? 72   ILE   B CG2 1 
ATOM   3857 C CD1 . ILE   B 1 96  ? -13.67000 40.57800  13.18600  1.000 41.63980  ? 72   ILE   B CD1 1 
ATOM   3858 N N   . THR   B 1 97  ? -12.59600 35.51900  10.57200  1.000 33.74497  ? 73   THR   B N   1 
ATOM   3859 C CA  . THR   B 1 97  ? -11.62000 34.64700  9.92900   1.000 32.18985  ? 73   THR   B CA  1 
ATOM   3860 C C   . THR   B 1 97  ? -12.06500 34.27000  8.52400   1.000 32.84093  ? 73   THR   B C   1 
ATOM   3861 O O   . THR   B 1 97  ? -11.28000 34.34800  7.57200   1.000 37.07560  ? 73   THR   B O   1 
ATOM   3862 C CB  . THR   B 1 97  ? -11.39300 33.39700  10.77800  1.000 36.08835  ? 73   THR   B CB  1 
ATOM   3863 O OG1 . THR   B 1 97  ? -10.65600 33.75100  11.95300  1.000 31.76307  ? 73   THR   B OG1 1 
ATOM   3864 C CG2 . THR   B 1 97  ? -10.62200 32.34200  9.99300   1.000 31.76182  ? 73   THR   B CG2 1 
ATOM   3865 N N   . SER   B 1 98  ? -13.32700 33.86200  8.37100   1.000 34.73502  ? 74   SER   B N   1 
ATOM   3866 C CA  . SER   B 1 98  ? -13.82500 33.53500  7.03900   1.000 39.38803  ? 74   SER   B CA  1 
ATOM   3867 C C   . SER   B 1 98  ? -13.91700 34.78100  6.16900   1.000 33.00476  ? 74   SER   B C   1 
ATOM   3868 O O   . SER   B 1 98  ? -13.58100 34.74000  4.97900   1.000 31.65994  ? 74   SER   B O   1 
ATOM   3869 C CB  . SER   B 1 98  ? -15.18500 32.85000  7.13500   1.000 33.53700  ? 74   SER   B CB  1 
ATOM   3870 O OG  . SER   B 1 98  ? -16.22700 33.80300  7.10600   1.000 34.49452  ? 74   SER   B OG  1 
ATOM   3871 N N   . LEU   B 1 99  ? -14.37300 35.89500  6.74600   1.000 33.08934  ? 75   LEU   B N   1 
ATOM   3872 C CA  . LEU   B 1 99  ? -14.35500 37.17000  6.03800   1.000 33.92750  ? 75   LEU   B CA  1 
ATOM   3873 C C   . LEU   B 1 99  ? -12.97200 37.46000  5.47400   1.000 38.29501  ? 75   LEU   B C   1 
ATOM   3874 O O   . LEU   B 1 99  ? -12.83900 37.95900  4.35000   1.000 37.74023  ? 75   LEU   B O   1 
ATOM   3875 C CB  . LEU   B 1 99  ? -14.79900 38.28900  6.98100   1.000 32.47796  ? 75   LEU   B CB  1 
ATOM   3876 C CG  . LEU   B 1 99  ? -15.23000 39.61100  6.35300   1.000 37.41994  ? 75   LEU   B CG  1 
ATOM   3877 C CD1 . LEU   B 1 99  ? -16.51600 39.39900  5.58300   1.000 41.66242  ? 75   LEU   B CD1 1 
ATOM   3878 C CD2 . LEU   B 1 99  ? -15.41600 40.68100  7.41600   1.000 32.27367  ? 75   LEU   B CD2 1 
ATOM   3879 N N   . ALA   B 1 100 ? -11.92600 37.13300  6.23700   1.000 39.83416  ? 76   ALA   B N   1 
ATOM   3880 C CA  . ALA   B 1 100 ? -10.56400 37.29000  5.74100   1.000 38.92157  ? 76   ALA   B CA  1 
ATOM   3881 C C   . ALA   B 1 100 ? -10.26600 36.30900  4.61000   1.000 39.41962  ? 76   ALA   B C   1 
ATOM   3882 O O   . ALA   B 1 100 ? -9.55900  36.65300  3.65600   1.000 44.72774  ? 76   ALA   B O   1 
ATOM   3883 C CB  . ALA   B 1 100 ? -9.56600  37.11400  6.88500   1.000 33.29515  ? 76   ALA   B CB  1 
ATOM   3884 N N   . CYS   B 1 101 ? -10.78900 35.08300  4.69900   1.000 35.25674  ? 77   CYS   B N   1 
ATOM   3885 C CA  . CYS   B 1 101 ? -10.57700 34.11600  3.62600   1.000 37.55869  ? 77   CYS   B CA  1 
ATOM   3886 C C   . CYS   B 1 101 ? -11.18400 34.60100  2.31600   1.000 44.07862  ? 77   CYS   B C   1 
ATOM   3887 O O   . CYS   B 1 101 ? -10.63100 34.35000  1.23900   1.000 41.27015  ? 77   CYS   B O   1 
ATOM   3888 C CB  . CYS   B 1 101 ? -11.16300 32.75800  4.00400   1.000 35.60887  ? 77   CYS   B CB  1 
ATOM   3889 S SG  . CYS   B 1 101 ? -10.38400 31.97600  5.41400   1.000 34.05922  ? 77   CYS   B SG  1 
ATOM   3890 N N   . ALA   B 1 102 ? -12.33000 35.28200  2.38500   1.000 39.43969  ? 78   ALA   B N   1 
ATOM   3891 C CA  . ALA   B 1 102 ? -12.89700 35.87900  1.18100   1.000 38.93478  ? 78   ALA   B CA  1 
ATOM   3892 C C   . ALA   B 1 102 ? -11.93900 36.90400  0.58800   1.000 44.02441  ? 78   ALA   B C   1 
ATOM   3893 O O   . ALA   B 1 102 ? -11.66900 36.89600  -0.61900  1.000 49.25696  ? 78   ALA   B O   1 
ATOM   3894 C CB  . ALA   B 1 102 ? -14.25200 36.51500  1.49100   1.000 34.56136  ? 78   ALA   B CB  1 
ATOM   3895 N N   . ASP   B 1 103 ? -11.39700 37.78800  1.42900   1.000 41.22183  ? 79   ASP   B N   1 
ATOM   3896 C CA  . ASP   B 1 103 ? -10.43600 38.76600  0.93300   1.000 47.20899  ? 79   ASP   B CA  1 
ATOM   3897 C C   . ASP   B 1 103 ? -9.13900  38.09800  0.48300   1.000 47.46044  ? 79   ASP   B C   1 
ATOM   3898 O O   . ASP   B 1 103 ? -8.48700  38.57800  -0.45200  1.000 43.68685  ? 79   ASP   B O   1 
ATOM   3899 C CB  . ASP   B 1 103 ? -10.15900 39.82100  2.00600   1.000 45.57678  ? 79   ASP   B CB  1 
ATOM   3900 C CG  . ASP   B 1 103 ? -11.39900 40.62100  2.38200   1.000 48.72012  ? 79   ASP   B CG  1 
ATOM   3901 O OD1 . ASP   B 1 103 ? -12.30700 40.75300  1.53700   1.000 62.21854  ? 79   ASP   B OD1 1 
ATOM   3902 O OD2 . ASP   B 1 103 ? -11.46500 41.13200  3.51800   1.000 49.58432  ? 79   ASP   B OD2 1 
ATOM   3903 N N   . LEU   B 1 104 ? -8.76000  36.98700  1.11700   1.000 44.81865  ? 80   LEU   B N   1 
ATOM   3904 C CA  . LEU   B 1 104 ? -7.52800  36.30000  0.74100   1.000 42.94511  ? 80   LEU   B CA  1 
ATOM   3905 C C   . LEU   B 1 104 ? -7.64400  35.66700  -0.64200  1.000 40.71561  ? 80   LEU   B C   1 
ATOM   3906 O O   . LEU   B 1 104 ? -6.74300  35.80800  -1.47600  1.000 40.02996  ? 80   LEU   B O   1 
ATOM   3907 C CB  . LEU   B 1 104 ? -7.17300  35.24800  1.79200   1.000 39.18639  ? 80   LEU   B CB  1 
ATOM   3908 C CG  . LEU   B 1 104 ? -5.78400  34.63300  1.64100   1.000 37.39110  ? 80   LEU   B CG  1 
ATOM   3909 C CD1 . LEU   B 1 104 ? -4.74100  35.70400  1.85500   1.000 37.79588  ? 80   LEU   B CD1 1 
ATOM   3910 C CD2 . LEU   B 1 104 ? -5.59100  33.50100  2.63200   1.000 30.64755  ? 80   LEU   B CD2 1 
ATOM   3911 N N   . VAL   B 1 105 ? -8.74700  34.95900  -0.90000  1.000 43.21259  ? 81   VAL   B N   1 
ATOM   3912 C CA  . VAL   B 1 105 ? -8.94800  34.35600  -2.21300  1.000 37.23451  ? 81   VAL   B CA  1 
ATOM   3913 C C   . VAL   B 1 105 ? -9.10900  35.43900  -3.27200  1.000 43.48330  ? 81   VAL   B C   1 
ATOM   3914 O O   . VAL   B 1 105 ? -8.72900  35.24500  -4.43500  1.000 46.88914  ? 81   VAL   B O   1 
ATOM   3915 C CB  . VAL   B 1 105 ? -10.14600 33.38800  -2.16600  1.000 28.22807  ? 81   VAL   B CB  1 
ATOM   3916 C CG1 . VAL   B 1 105 ? -10.62200 33.04800  -3.55400  1.000 34.92467  ? 81   VAL   B CG1 1 
ATOM   3917 C CG2 . VAL   B 1 105 ? -9.76200  32.11900  -1.43700  1.000 23.98255  ? 81   VAL   B CG2 1 
ATOM   3918 N N   . MET   B 1 106 ? -9.64700  36.59900  -2.89000  1.000 39.88690  ? 82   MET   B N   1 
ATOM   3919 C CA  . MET   B 1 106 ? -9.63800  37.75900  -3.77600  1.000 41.82614  ? 82   MET   B CA  1 
ATOM   3920 C C   . MET   B 1 106 ? -8.22000  38.09100  -4.22400  1.000 45.10403  ? 82   MET   B C   1 
ATOM   3921 O O   . MET   B 1 106 ? -7.92800  38.15100  -5.42400  1.000 44.73549  ? 82   MET   B O   1 
ATOM   3922 C CB  . MET   B 1 106 ? -10.26900 38.95800  -3.07000  1.000 42.93383  ? 82   MET   B CB  1 
ATOM   3923 C CG  . MET   B 1 106 ? -11.77900 38.96000  -3.08100  1.000 51.15176  ? 82   MET   B CG  1 
ATOM   3924 S SD  . MET   B 1 106 ? -12.46000 39.41500  -4.68300  1.000 61.46634  ? 82   MET   B SD  1 
ATOM   3925 C CE  . MET   B 1 106 ? -12.25400 41.19400  -4.62700  1.000 53.72685  ? 82   MET   B CE  1 
ATOM   3926 N N   . GLY   B 1 107 ? -7.31800  38.30100  -3.26400  1.000 46.03771  ? 83   GLY   B N   1 
ATOM   3927 C CA  . GLY   B 1 107 ? -5.96400  38.70600  -3.59600  1.000 48.03447  ? 83   GLY   B CA  1 
ATOM   3928 C C   . GLY   B 1 107 ? -5.16300  37.65100  -4.32700  1.000 45.80608  ? 83   GLY   B C   1 
ATOM   3929 O O   . GLY   B 1 107 ? -4.15600  37.97800  -4.96100  1.000 48.23980  ? 83   GLY   B O   1 
ATOM   3930 N N   . LEU   B 1 108 ? -5.57800  36.38900  -4.25300  1.000 40.60071  ? 84   LEU   B N   1 
ATOM   3931 C CA  . LEU   B 1 108 ? -4.83200  35.33200  -4.92600  1.000 43.04955  ? 84   LEU   B CA  1 
ATOM   3932 C C   . LEU   B 1 108 ? -5.42200  35.00500  -6.29600  1.000 52.38096  ? 84   LEU   B C   1 
ATOM   3933 O O   . LEU   B 1 108 ? -4.71600  35.04400  -7.31000  1.000 42.29082  ? 84   LEU   B O   1 
ATOM   3934 C CB  . LEU   B 1 108 ? -4.77700  34.07900  -4.04500  1.000 33.98255  ? 84   LEU   B CB  1 
ATOM   3935 C CG  . LEU   B 1 108 ? -4.03400  34.22200  -2.71600  1.000 46.77695  ? 84   LEU   B CG  1 
ATOM   3936 C CD1 . LEU   B 1 108 ? -4.06600  32.90600  -1.95300  1.000 41.43578  ? 84   LEU   B CD1 1 
ATOM   3937 C CD2 . LEU   B 1 108 ? -2.60000  34.66300  -2.96400  1.000 32.81934  ? 84   LEU   B CD2 1 
ATOM   3938 N N   . ALA   B 1 109 ? -6.71800  34.69900  -6.34000  1.000 49.65623  ? 85   ALA   B N   1 
ATOM   3939 C CA  . ALA   B 1 109 ? -7.34200  34.12700  -7.52200  1.000 33.28418  ? 85   ALA   B CA  1 
ATOM   3940 C C   . ALA   B 1 109 ? -8.12300  35.13500  -8.34800  1.000 41.27211  ? 85   ALA   B C   1 
ATOM   3941 O O   . ALA   B 1 109 ? -8.63800  34.76900  -9.40700  1.000 51.01119  ? 85   ALA   B O   1 
ATOM   3942 C CB  . ALA   B 1 109 ? -8.27000  32.97400  -7.12100  1.000 26.04449  ? 85   ALA   B CB  1 
ATOM   3943 N N   . VAL   B 1 110 ? -8.23200  36.38600  -7.90600  1.000 39.31382  ? 86   VAL   B N   1 
ATOM   3944 C CA  . VAL   B 1 110 ? -9.09000  37.33200  -8.61100  1.000 42.86679  ? 86   VAL   B CA  1 
ATOM   3945 C C   . VAL   B 1 110 ? -8.31300  38.57900  -9.01700  1.000 45.56117  ? 86   VAL   B C   1 
ATOM   3946 O O   . VAL   B 1 110 ? -8.09800  38.81500  -10.21100 1.000 43.96448  ? 86   VAL   B O   1 
ATOM   3947 C CB  . VAL   B 1 110 ? -10.32400 37.69400  -7.76400  1.000 39.44578  ? 86   VAL   B CB  1 
ATOM   3948 C CG1 . VAL   B 1 110 ? -11.07900 38.87200  -8.37300  1.000 40.76583  ? 86   VAL   B CG1 1 
ATOM   3949 C CG2 . VAL   B 1 110 ? -11.24200 36.49100  -7.63700  1.000 37.81142  ? 86   VAL   B CG2 1 
ATOM   3950 N N   . VAL   B 1 111 ? -7.89200  39.38000  -8.02800  1.000 43.98990  ? 87   VAL   B N   1 
ATOM   3951 C CA  . VAL   B 1 111 ? -7.24400  40.65700  -8.33600  1.000 45.39986  ? 87   VAL   B CA  1 
ATOM   3952 C C   . VAL   B 1 111 ? -6.03500  40.49600  -9.24300  1.000 46.17238  ? 87   VAL   B C   1 
ATOM   3953 O O   . VAL   B 1 111 ? -5.87800  41.31100  -10.16100 1.000 50.20168  ? 87   VAL   B O   1 
ATOM   3954 C CB  . VAL   B 1 111 ? -6.93100  41.41600  -7.03900  1.000 45.83318  ? 87   VAL   B CB  1 
ATOM   3955 C CG1 . VAL   B 1 111 ? -6.25800  42.74500  -7.35200  1.000 44.34638  ? 87   VAL   B CG1 1 
ATOM   3956 C CG2 . VAL   B 1 111 ? -8.22400  41.64900  -6.25700  1.000 43.55194  ? 87   VAL   B CG2 1 
ATOM   3957 N N   . PRO   B 1 112 ? -5.15600  39.47800  -9.08600  1.000 46.79408  ? 88   PRO   B N   1 
ATOM   3958 C CA  . PRO   B 1 112 ? -4.03600  39.33600  -10.03000 1.000 48.63407  ? 88   PRO   B CA  1 
ATOM   3959 C C   . PRO   B 1 112 ? -4.46000  39.19400  -11.48600 1.000 51.57569  ? 88   PRO   B C   1 
ATOM   3960 O O   . PRO   B 1 112 ? -4.01000  39.96900  -12.33700 1.000 46.86860  ? 88   PRO   B O   1 
ATOM   3961 C CB  . PRO   B 1 112 ? -3.32100  38.06500  -9.54100  1.000 46.78119  ? 88   PRO   B CB  1 
ATOM   3962 C CG  . PRO   B 1 112 ? -3.66500  37.95700  -8.12000  1.000 49.68665  ? 88   PRO   B CG  1 
ATOM   3963 C CD  . PRO   B 1 112 ? -5.06100  38.48300  -8.00500  1.000 49.76600  ? 88   PRO   B CD  1 
ATOM   3964 N N   . PHE   B 1 113 ? -5.31400  38.21000  -11.78500 1.000 49.96718  ? 89   PHE   B N   1 
ATOM   3965 C CA  . PHE   B 1 113 ? -5.72400  37.97900  -13.16700 1.000 40.82113  ? 89   PHE   B CA  1 
ATOM   3966 C C   . PHE   B 1 113 ? -6.44700  39.18600  -13.75100 1.000 44.94122  ? 89   PHE   B C   1 
ATOM   3967 O O   . PHE   B 1 113 ? -6.33800  39.45100  -14.95400 1.000 53.66243  ? 89   PHE   B O   1 
ATOM   3968 C CB  . PHE   B 1 113 ? -6.60300  36.73400  -13.24200 1.000 40.49842  ? 89   PHE   B CB  1 
ATOM   3969 C CG  . PHE   B 1 113 ? -5.91000  35.48700  -12.79000 1.000 45.90967  ? 89   PHE   B CG  1 
ATOM   3970 C CD1 . PHE   B 1 113 ? -4.96800  34.87300  -13.59400 1.000 50.69901  ? 89   PHE   B CD1 1 
ATOM   3971 C CD2 . PHE   B 1 113 ? -6.18800  34.93400  -11.55200 1.000 49.95782  ? 89   PHE   B CD2 1 
ATOM   3972 C CE1 . PHE   B 1 113 ? -4.31800  33.72600  -13.17600 1.000 51.00607  ? 89   PHE   B CE1 1 
ATOM   3973 C CE2 . PHE   B 1 113 ? -5.54400  33.78600  -11.12800 1.000 50.35937  ? 89   PHE   B CE2 1 
ATOM   3974 C CZ  . PHE   B 1 113 ? -4.60700  33.18100  -11.94200 1.000 50.24589  ? 89   PHE   B CZ  1 
ATOM   3975 N N   . GLY   B 1 114 ? -7.18200  39.93200  -12.92500 1.000 45.10277  ? 90   GLY   B N   1 
ATOM   3976 C CA  . GLY   B 1 114 ? -7.78600  41.16400  -13.40100 1.000 48.18298  ? 90   GLY   B CA  1 
ATOM   3977 C C   . GLY   B 1 114 ? -6.77600  42.26900  -13.61300 1.000 54.91068  ? 90   GLY   B C   1 
ATOM   3978 O O   . GLY   B 1 114 ? -6.97300  43.14000  -14.46500 1.000 58.04713  ? 90   GLY   B O   1 
ATOM   3979 N N   . ALA   B 1 115 ? -5.69000  42.26000  -12.83700 1.000 51.98870  ? 91   ALA   B N   1 
ATOM   3980 C CA  . ALA   B 1 115 ? -4.58800  43.17900  -13.09500 1.000 54.43995  ? 91   ALA   B CA  1 
ATOM   3981 C C   . ALA   B 1 115 ? -3.85600  42.80700  -14.38000 1.000 56.89477  ? 91   ALA   B C   1 
ATOM   3982 O O   . ALA   B 1 115 ? -3.46300  43.68400  -15.16000 1.000 54.08920  ? 91   ALA   B O   1 
ATOM   3983 C CB  . ALA   B 1 115 ? -3.62700  43.18300  -11.90800 1.000 46.49852  ? 91   ALA   B CB  1 
ATOM   3984 N N   . ALA   B 1 116 ? -3.66200  41.50700  -14.61500 1.000 50.25317  ? 92   ALA   B N   1 
ATOM   3985 C CA  . ALA   B 1 116 ? -3.05500  41.06300  -15.86200 1.000 42.18337  ? 92   ALA   B CA  1 
ATOM   3986 C C   . ALA   B 1 116 ? -3.94800  41.39000  -17.04900 1.000 65.13593  ? 92   ALA   B C   1 
ATOM   3987 O O   . ALA   B 1 116 ? -3.45600  41.75600  -18.12400 1.000 73.76307  ? 92   ALA   B O   1 
ATOM   3988 C CB  . ALA   B 1 116 ? -2.77400  39.56300  -15.80600 1.000 38.63691  ? 92   ALA   B CB  1 
ATOM   3989 N N   . HIS   B 1 117 ? -5.26700  41.26900  -16.87100 1.000 63.38460  ? 93   HIS   B N   1 
ATOM   3990 C CA  . HIS   B 1 117 ? -6.18700  41.52700  -17.97300 1.000 62.28561  ? 93   HIS   B CA  1 
ATOM   3991 C C   . HIS   B 1 117 ? -6.10000  42.97200  -18.44800 1.000 64.52854  ? 93   HIS   B C   1 
ATOM   3992 O O   . HIS   B 1 117 ? -6.15900  43.24000  -19.65400 1.000 64.70814  ? 93   HIS   B O   1 
ATOM   3993 C CB  . HIS   B 1 117 ? -7.61800  41.19300  -17.55300 1.000 57.56988  ? 93   HIS   B CB  1 
ATOM   3994 C CG  . HIS   B 1 117 ? -8.64100  41.50900  -18.59800 1.000 59.20030  ? 93   HIS   B CG  1 
ATOM   3995 N ND1 . HIS   B 1 117 ? -9.37400  42.67700  -18.59100 1.000 65.21239  ? 93   HIS   B ND1 1 
ATOM   3996 C CD2 . HIS   B 1 117 ? -9.05200  40.81300  -19.68400 1.000 54.14679  ? 93   HIS   B CD2 1 
ATOM   3997 C CE1 . HIS   B 1 117 ? -10.19300 42.68500  -19.62700 1.000 72.83862  ? 93   HIS   B CE1 1 
ATOM   3998 N NE2 . HIS   B 1 117 ? -10.01700 41.56600  -20.30700 1.000 67.50280  ? 93   HIS   B NE2 1 
ATOM   3999 N N   . ILE   B 1 118 ? -5.93700  43.91400  -17.52000 1.000 63.67958  ? 94   ILE   B N   1 
ATOM   4000 C CA  . ILE   B 1 118 ? -5.99500  45.33100  -17.87500 1.000 69.45186  ? 94   ILE   B CA  1 
ATOM   4001 C C   . ILE   B 1 118 ? -4.71500  45.77900  -18.57400 1.000 72.54825  ? 94   ILE   B C   1 
ATOM   4002 O O   . ILE   B 1 118 ? -4.75700  46.32000  -19.68600 1.000 72.00610  ? 94   ILE   B O   1 
ATOM   4003 C CB  . ILE   B 1 118 ? -6.29800  46.18700  -16.63200 1.000 65.63284  ? 94   ILE   B CB  1 
ATOM   4004 C CG1 . ILE   B 1 118 ? -7.64500  45.77800  -16.03800 1.000 65.36345  ? 94   ILE   B CG1 1 
ATOM   4005 C CG2 . ILE   B 1 118 ? -6.28600  47.66600  -16.98400 1.000 66.08134  ? 94   ILE   B CG2 1 
ATOM   4006 C CD1 . ILE   B 1 118 ? -8.74900  45.66400  -17.07500 1.000 67.35174  ? 94   ILE   B CD1 1 
ATOM   4007 N N   . LEU   B 1 119 ? -3.55700  45.57800  -17.93800 1.000 67.20190  ? 95   LEU   B N   1 
ATOM   4008 C CA  . LEU   B 1 119 ? -2.33000  46.09200  -18.54200 1.000 72.10312  ? 95   LEU   B CA  1 
ATOM   4009 C C   . LEU   B 1 119 ? -1.96400  45.33400  -19.81400 1.000 70.93850  ? 95   LEU   B C   1 
ATOM   4010 O O   . LEU   B 1 119 ? -1.29500  45.89300  -20.69100 1.000 77.67348  ? 95   LEU   B O   1 
ATOM   4011 C CB  . LEU   B 1 119 ? -1.17300  46.08100  -17.53200 1.000 69.53654  ? 95   LEU   B CB  1 
ATOM   4012 C CG  . LEU   B 1 119 ? -0.73200  44.85500  -16.72900 1.000 68.01565  ? 95   LEU   B CG  1 
ATOM   4013 C CD1 . LEU   B 1 119 ? 0.14700   43.92800  -17.55600 1.000 73.79466  ? 95   LEU   B CD1 1 
ATOM   4014 C CD2 . LEU   B 1 119 ? 0.00800   45.30400  -15.47800 1.000 58.01184  ? 95   LEU   B CD2 1 
ATOM   4015 N N   . MET   B 1 120 ? -2.39800  44.07900  -19.95000 1.000 65.98009  ? 96   MET   B N   1 
ATOM   4016 C CA  . MET   B 1 120 ? -2.26600  43.41300  -21.24000 1.000 62.36253  ? 96   MET   B CA  1 
ATOM   4017 C C   . MET   B 1 120 ? -3.41100  43.74000  -22.19000 1.000 65.00108  ? 96   MET   B C   1 
ATOM   4018 O O   . MET   B 1 120 ? -3.34700  43.34000  -23.35600 1.000 62.32074  ? 96   MET   B O   1 
ATOM   4019 C CB  . MET   B 1 120 ? -2.18800  41.89300  -21.08400 1.000 56.98922  ? 96   MET   B CB  1 
ATOM   4020 C CG  . MET   B 1 120 ? -0.89800  41.38900  -20.48900 1.000 58.26199  ? 96   MET   B CG  1 
ATOM   4021 S SD  . MET   B 1 120 ? -1.00400  39.64400  -20.06400 1.000 64.86308  ? 96   MET   B SD  1 
ATOM   4022 C CE  . MET   B 1 120 ? -0.70500  38.92200  -21.67100 1.000 57.81589  ? 96   MET   B CE  1 
ATOM   4023 N N   . LYS   B 1 121 ? -4.45700  44.42300  -21.71300 1.000 72.82369  ? 97   LYS   B N   1 
ATOM   4024 C CA  . LYS   B 1 121 ? -5.57800  44.86100  -22.55400 1.000 72.13440  ? 97   LYS   B CA  1 
ATOM   4025 C C   . LYS   B 1 121 ? -6.20400  43.69400  -23.31500 1.000 65.06523  ? 97   LYS   B C   1 
ATOM   4026 O O   . LYS   B 1 121 ? -6.73800  43.86300  -24.41300 1.000 56.19913  ? 97   LYS   B O   1 
ATOM   4027 C CB  . LYS   B 1 121 ? -5.13600  45.97100  -23.51500 1.000 66.68673  ? 97   LYS   B CB  1 
ATOM   4028 C CG  . LYS   B 1 121 ? -4.87200  47.30900  -22.82900 1.000 73.86970  ? 97   LYS   B CG  1 
ATOM   4029 C CD  . LYS   B 1 121 ? -3.97400  48.23100  -23.64500 1.000 66.26772  ? 97   LYS   B CD  1 
ATOM   4030 C CE  . LYS   B 1 121 ? -2.50900  47.85800  -23.47600 1.000 77.55655  ? 97   LYS   B CE  1 
ATOM   4031 N NZ  . LYS   B 1 121 ? -1.58700  48.80600  -24.16500 1.000 85.81870  ? 97   LYS   B NZ  1 
ATOM   4032 N N   . MET   B 1 122 ? -6.16600  42.50800  -22.71300 1.000 61.98832  ? 98   MET   B N   1 
ATOM   4033 C CA  . MET   B 1 122 ? -6.49300  41.26700  -23.39900 1.000 60.02647  ? 98   MET   B CA  1 
ATOM   4034 C C   . MET   B 1 122 ? -6.46500  40.13700  -22.37900 1.000 57.06317  ? 98   MET   B C   1 
ATOM   4035 O O   . MET   B 1 122 ? -5.72200  40.19400  -21.39600 1.000 61.08572  ? 98   MET   B O   1 
ATOM   4036 C CB  . MET   B 1 122 ? -5.50000  41.00200  -24.54200 1.000 58.95989  ? 98   MET   B CB  1 
ATOM   4037 C CG  . MET   B 1 122 ? -5.55900  39.62400  -25.15400 1.000 55.31024  ? 98   MET   B CG  1 
ATOM   4038 S SD  . MET   B 1 122 ? -4.21600  38.52900  -24.64600 1.000 75.50840  ? 98   MET   B SD  1 
ATOM   4039 C CE  . MET   B 1 122 ? -4.28900  37.28800  -25.93800 1.000 73.17611  ? 98   MET   B CE  1 
ATOM   4040 N N   . TRP   B 1 123 ? -7.28000  39.11300  -22.62700 1.000 52.83966  ? 99   TRP   B N   1 
ATOM   4041 C CA  . TRP   B 1 123 ? -7.35300  37.95200  -21.74800 1.000 56.19521  ? 99   TRP   B CA  1 
ATOM   4042 C C   . TRP   B 1 123 ? -6.43000  36.85200  -22.25400 1.000 56.15721  ? 99   TRP   B C   1 
ATOM   4043 O O   . TRP   B 1 123 ? -6.44200  36.52300  -23.44400 1.000 58.81195  ? 99   TRP   B O   1 
ATOM   4044 C CB  . TRP   B 1 123 ? -8.78500  37.42100  -21.64100 1.000 56.38527  ? 99   TRP   B CB  1 
ATOM   4045 C CG  . TRP   B 1 123 ? -8.91000  36.30800  -20.65800 1.000 49.52339  ? 99   TRP   B CG  1 
ATOM   4046 C CD1 . TRP   B 1 123 ? -8.93500  34.97200  -20.93000 1.000 50.43968  ? 99   TRP   B CD1 1 
ATOM   4047 C CD2 . TRP   B 1 123 ? -9.00700  36.43300  -19.23600 1.000 48.61326  ? 99   TRP   B CD2 1 
ATOM   4048 N NE1 . TRP   B 1 123 ? -9.04700  34.25500  -19.76400 1.000 47.79538  ? 99   TRP   B NE1 1 
ATOM   4049 C CE2 . TRP   B 1 123 ? -9.09500  35.12900  -18.70900 1.000 53.15621  ? 99   TRP   B CE2 1 
ATOM   4050 C CE3 . TRP   B 1 123 ? -9.03400  37.52100  -18.35900 1.000 47.62553  ? 99   TRP   B CE3 1 
ATOM   4051 C CZ2 . TRP   B 1 123 ? -9.21100  34.88200  -17.34000 1.000 49.26894  ? 99   TRP   B CZ2 1 
ATOM   4052 C CZ3 . TRP   B 1 123 ? -9.14800  37.27600  -17.00100 1.000 48.88276  ? 99   TRP   B CZ3 1 
ATOM   4053 C CH2 . TRP   B 1 123 ? -9.23500  35.96600  -16.50500 1.000 45.92726  ? 99   TRP   B CH2 1 
ATOM   4054 N N   . THR   B 1 124 ? -5.66600  36.25700  -21.33300 1.000 59.10828  ? 100  THR   B N   1 
ATOM   4055 C CA  . THR   B 1 124 ? -4.54100  35.39400  -21.66800 1.000 58.91191  ? 100  THR   B CA  1 
ATOM   4056 C C   . THR   B 1 124 ? -4.75000  33.92800  -21.30900 1.000 56.93102  ? 100  THR   B C   1 
ATOM   4057 O O   . THR   B 1 124 ? -4.06400  33.06800  -21.86900 1.000 60.49081  ? 100  THR   B O   1 
ATOM   4058 C CB  . THR   B 1 124 ? -3.28000  35.89200  -20.94400 1.000 63.56060  ? 100  THR   B CB  1 
ATOM   4059 O OG1 . THR   B 1 124 ? -3.23100  37.31900  -21.01800 1.000 68.53540  ? 100  THR   B OG1 1 
ATOM   4060 C CG2 . THR   B 1 124 ? -2.02500  35.33100  -21.58300 1.000 68.86261  ? 100  THR   B CG2 1 
ATOM   4061 N N   . PHE   B 1 125 ? -5.68300  33.62000  -20.41000 1.000 60.17638  ? 101  PHE   B N   1 
ATOM   4062 C CA  . PHE   B 1 125 ? -5.73300  32.32300  -19.74600 1.000 62.28546  ? 101  PHE   B CA  1 
ATOM   4063 C C   . PHE   B 1 125 ? -6.80000  31.39900  -20.32700 1.000 64.27952  ? 101  PHE   B C   1 
ATOM   4064 O O   . PHE   B 1 125 ? -7.27200  30.49300  -19.63000 1.000 71.49932  ? 101  PHE   B O   1 
ATOM   4065 C CB  . PHE   B 1 125 ? -5.95400  32.51200  -18.24000 1.000 51.90620  ? 101  PHE   B CB  1 
ATOM   4066 C CG  . PHE   B 1 125 ? -5.14200  33.63200  -17.64400 1.000 45.75002  ? 101  PHE   B CG  1 
ATOM   4067 C CD1 . PHE   B 1 125 ? -5.57000  34.94900  -17.74200 1.000 45.24171  ? 101  PHE   B CD1 1 
ATOM   4068 C CD2 . PHE   B 1 125 ? -3.94200  33.37100  -17.00600 1.000 40.64053  ? 101  PHE   B CD2 1 
ATOM   4069 C CE1 . PHE   B 1 125 ? -4.82400  35.97800  -17.20800 1.000 47.60073  ? 101  PHE   B CE1 1 
ATOM   4070 C CE2 . PHE   B 1 125 ? -3.18800  34.39900  -16.47000 1.000 39.94571  ? 101  PHE   B CE2 1 
ATOM   4071 C CZ  . PHE   B 1 125 ? -3.63000  35.70400  -16.57200 1.000 45.50454  ? 101  PHE   B CZ  1 
ATOM   4072 N N   . GLY   B 1 126 ? -7.18300  31.60000  -21.58100 1.000 58.25728  ? 102  GLY   B N   1 
ATOM   4073 C CA  . GLY   B 1 126 ? -8.20900  30.77500  -22.18800 1.000 67.11873  ? 102  GLY   B CA  1 
ATOM   4074 C C   . GLY   B 1 126 ? -9.58500  31.05300  -21.60100 1.000 67.99627  ? 102  GLY   B C   1 
ATOM   4075 O O   . GLY   B 1 126 ? -9.76700  31.86700  -20.69700 1.000 55.30789  ? 102  GLY   B O   1 
ATOM   4076 N N   . ASN   B 1 127 ? -10.57600 30.33900  -22.13800 1.000 72.27663  ? 103  ASN   B N   1 
ATOM   4077 C CA  . ASN   B 1 127 ? -11.96100 30.58800  -21.75600 1.000 69.20543  ? 103  ASN   B CA  1 
ATOM   4078 C C   . ASN   B 1 127 ? -12.34800 29.92400  -20.43700 1.000 67.28770  ? 103  ASN   B C   1 
ATOM   4079 O O   . ASN   B 1 127 ? -13.18200 30.46900  -19.70500 1.000 59.32072  ? 103  ASN   B O   1 
ATOM   4080 C CB  . ASN   B 1 127 ? -12.90000 30.11600  -22.87000 1.000 68.16930  ? 103  ASN   B CB  1 
ATOM   4081 C CG  . ASN   B 1 127 ? -13.26100 31.22600  -23.84600 1.000 70.76257  ? 103  ASN   B CG  1 
ATOM   4082 O OD1 . ASN   B 1 127 ? -13.02300 32.40700  -23.58300 1.000 62.02758  ? 103  ASN   B OD1 1 
ATOM   4083 N ND2 . ASN   B 1 127 ? -13.85000 30.84900  -24.97600 1.000 68.14463  ? 103  ASN   B ND2 1 
ATOM   4084 N N   . PHE   B 1 128 ? -11.76400 28.76600  -20.11400 1.000 64.95134  ? 104  PHE   B N   1 
ATOM   4085 C CA  . PHE   B 1 128 ? -12.20000 28.01800  -18.93500 1.000 59.44171  ? 104  PHE   B CA  1 
ATOM   4086 C C   . PHE   B 1 128 ? -11.92500 28.79500  -17.65400 1.000 60.88803  ? 104  PHE   B C   1 
ATOM   4087 O O   . PHE   B 1 128 ? -12.79600 28.90200  -16.78200 1.000 63.10480  ? 104  PHE   B O   1 
ATOM   4088 C CB  . PHE   B 1 128 ? -11.52100 26.64600  -18.89000 1.000 59.27832  ? 104  PHE   B CB  1 
ATOM   4089 C CG  . PHE   B 1 128 ? -11.90900 25.80400  -17.69500 1.000 50.50430  ? 104  PHE   B CG  1 
ATOM   4090 C CD1 . PHE   B 1 128 ? -11.31300 25.99700  -16.45800 1.000 55.11240  ? 104  PHE   B CD1 1 
ATOM   4091 C CD2 . PHE   B 1 128 ? -12.87400 24.81800  -17.81500 1.000 60.21662  ? 104  PHE   B CD2 1 
ATOM   4092 C CE1 . PHE   B 1 128 ? -11.67400 25.22500  -15.36600 1.000 56.68573  ? 104  PHE   B CE1 1 
ATOM   4093 C CE2 . PHE   B 1 128 ? -13.23700 24.04200  -16.72500 1.000 59.56354  ? 104  PHE   B CE2 1 
ATOM   4094 C CZ  . PHE   B 1 128 ? -12.63600 24.24700  -15.50200 1.000 54.54216  ? 104  PHE   B CZ  1 
ATOM   4095 N N   . TRP   B 1 129 ? -10.70500 29.31900  -17.50400 1.000 60.21505  ? 105  TRP   B N   1 
ATOM   4096 C CA  . TRP   B 1 129 ? -10.41500 30.13600  -16.33300 1.000 56.64878  ? 105  TRP   B CA  1 
ATOM   4097 C C   . TRP   B 1 129 ? -11.29100 31.37600  -16.30200 1.000 55.94230  ? 105  TRP   B C   1 
ATOM   4098 O O   . TRP   B 1 129 ? -11.64000 31.85700  -15.22100 1.000 63.96765  ? 105  TRP   B O   1 
ATOM   4099 C CB  . TRP   B 1 129 ? -8.93800  30.53000  -16.29200 1.000 58.91864  ? 105  TRP   B CB  1 
ATOM   4100 C CG  . TRP   B 1 129 ? -8.55100  31.23500  -15.01700 1.000 56.33255  ? 105  TRP   B CG  1 
ATOM   4101 C CD1 . TRP   B 1 129 ? -8.06400  32.50700  -14.89300 1.000 55.06370  ? 105  TRP   B CD1 1 
ATOM   4102 C CD2 . TRP   B 1 129 ? -8.64000  30.71100  -13.68400 1.000 51.53675  ? 105  TRP   B CD2 1 
ATOM   4103 N NE1 . TRP   B 1 129 ? -7.83200  32.80000  -13.56900 1.000 50.51381  ? 105  TRP   B NE1 1 
ATOM   4104 C CE2 . TRP   B 1 129 ? -8.18100  31.71700  -12.80700 1.000 54.94019  ? 105  TRP   B CE2 1 
ATOM   4105 C CE3 . TRP   B 1 129 ? -9.05700  29.48700  -13.14800 1.000 45.60640  ? 105  TRP   B CE3 1 
ATOM   4106 C CZ2 . TRP   B 1 129 ? -8.12900  31.53600  -11.42400 1.000 47.20701  ? 105  TRP   B CZ2 1 
ATOM   4107 C CZ3 . TRP   B 1 129 ? -9.00400  29.31000  -11.77500 1.000 48.35369  ? 105  TRP   B CZ3 1 
ATOM   4108 C CH2 . TRP   B 1 129 ? -8.54300  30.32900  -10.93000 1.000 45.48777  ? 105  TRP   B CH2 1 
ATOM   4109 N N   . CYS   B 1 130 ? -11.67500 31.88900  -17.47200 1.000 54.95273  ? 106  CYS   B N   1 
ATOM   4110 C CA  . CYS   B 1 130 ? -12.51700 33.07800  -17.52600 1.000 48.14968  ? 106  CYS   B CA  1 
ATOM   4111 C C   . CYS   B 1 130 ? -13.83700 32.85400  -16.79900 1.000 49.21659  ? 106  CYS   B C   1 
ATOM   4112 O O   . CYS   B 1 130 ? -14.25500 33.68300  -15.98300 1.000 46.69779  ? 106  CYS   B O   1 
ATOM   4113 C CB  . CYS   B 1 130 ? -12.75900 33.47400  -18.97900 1.000 40.16082  ? 106  CYS   B CB  1 
ATOM   4114 S SG  . CYS   B 1 130 ? -13.95500 34.78700  -19.17500 1.000 43.75547  ? 106  CYS   B SG  1 
ATOM   4115 N N   . GLU   B 1 131 ? -14.50700 31.73200  -17.08400 1.000 53.20419  ? 107  GLU   B N   1 
ATOM   4116 C CA  . GLU   B 1 131 ? -15.76600 31.41800  -16.41100 1.000 56.31645  ? 107  GLU   B CA  1 
ATOM   4117 C C   . GLU   B 1 131 ? -15.54100 31.16300  -14.92600 1.000 58.14480  ? 107  GLU   B C   1 
ATOM   4118 O O   . GLU   B 1 131 ? -16.38900 31.50800  -14.09200 1.000 51.71027  ? 107  GLU   B O   1 
ATOM   4119 C CB  . GLU   B 1 131 ? -16.42000 30.20000  -17.06800 1.000 47.49645  ? 107  GLU   B CB  1 
ATOM   4120 C CG  . GLU   B 1 131 ? -16.79400 30.39400  -18.53200 1.000 53.04208  ? 107  GLU   B CG  1 
ATOM   4121 C CD  . GLU   B 1 131 ? -18.27600 30.62900  -18.76000 1.000 49.50406  ? 107  GLU   B CD  1 
ATOM   4122 O OE1 . GLU   B 1 131 ? -19.05400 29.65700  -18.64400 1.000 52.11343  ? 107  GLU   B OE1 1 
ATOM   4123 O OE2 . GLU   B 1 131 ? -18.66000 31.77800  -19.06600 1.000 46.34284  ? 107  GLU   B OE2 1 
ATOM   4124 N N   . PHE   B 1 132 ? -14.39900 30.56100  -14.58200 1.000 55.61828  ? 108  PHE   B N   1 
ATOM   4125 C CA  . PHE   B 1 132 ? -14.05200 30.30200  -13.19000 1.000 50.82949  ? 108  PHE   B CA  1 
ATOM   4126 C C   . PHE   B 1 132 ? -13.59400 31.56900  -12.47800 1.000 48.00403  ? 108  PHE   B C   1 
ATOM   4127 O O   . PHE   B 1 132 ? -13.95100 31.79300  -11.31700 1.000 51.16313  ? 108  PHE   B O   1 
ATOM   4128 C CB  . PHE   B 1 132 ? -12.95400 29.24000  -13.12100 1.000 48.23468  ? 108  PHE   B CB  1 
ATOM   4129 C CG  . PHE   B 1 132 ? -13.14800 28.23500  -12.02500 1.000 48.07427  ? 108  PHE   B CG  1 
ATOM   4130 C CD1 . PHE   B 1 132 ? -12.72900 28.51100  -10.73500 1.000 48.40963  ? 108  PHE   B CD1 1 
ATOM   4131 C CD2 . PHE   B 1 132 ? -13.73800 27.00900  -12.28500 1.000 46.32852  ? 108  PHE   B CD2 1 
ATOM   4132 C CE1 . PHE   B 1 132 ? -12.90300 27.58900  -9.72200  1.000 47.83099  ? 108  PHE   B CE1 1 
ATOM   4133 C CE2 . PHE   B 1 132 ? -13.91300 26.08200  -11.27700 1.000 45.99681  ? 108  PHE   B CE2 1 
ATOM   4134 C CZ  . PHE   B 1 132 ? -13.49500 26.37300  -9.99200  1.000 46.04318  ? 108  PHE   B CZ  1 
ATOM   4135 N N   . TRP   B 1 133 ? -12.79700 32.39600  -13.15900 1.000 46.15241  ? 109  TRP   B N   1 
ATOM   4136 C CA  . TRP   B 1 133 ? -12.26000 33.60800  -12.54600 1.000 46.40816  ? 109  TRP   B CA  1 
ATOM   4137 C C   . TRP   B 1 133 ? -13.37000 34.53800  -12.08100 1.000 48.60749  ? 109  TRP   B C   1 
ATOM   4138 O O   . TRP   B 1 133 ? -13.25000 35.18800  -11.03600 1.000 54.95642  ? 109  TRP   B O   1 
ATOM   4139 C CB  . TRP   B 1 133 ? -11.34800 34.32500  -13.54100 1.000 46.87303  ? 109  TRP   B CB  1 
ATOM   4140 C CG  . TRP   B 1 133 ? -10.84100 35.65400  -13.10400 1.000 42.92932  ? 109  TRP   B CG  1 
ATOM   4141 C CD1 . TRP   B 1 133 ? -9.99900  35.91000  -12.06500 1.000 43.04632  ? 109  TRP   B CD1 1 
ATOM   4142 C CD2 . TRP   B 1 133 ? -11.13700 36.92200  -13.70400 1.000 49.03277  ? 109  TRP   B CD2 1 
ATOM   4143 N NE1 . TRP   B 1 133 ? -9.75100  37.26000  -11.97900 1.000 42.73538  ? 109  TRP   B NE1 1 
ATOM   4144 C CE2 . TRP   B 1 133 ? -10.43800 37.90200  -12.97500 1.000 45.60562  ? 109  TRP   B CE2 1 
ATOM   4145 C CE3 . TRP   B 1 133 ? -11.92900 37.32400  -14.78700 1.000 51.71911  ? 109  TRP   B CE3 1 
ATOM   4146 C CZ2 . TRP   B 1 133 ? -10.50800 39.25600  -13.28900 1.000 49.02488  ? 109  TRP   B CZ2 1 
ATOM   4147 C CZ3 . TRP   B 1 133 ? -11.99300 38.67200  -15.09900 1.000 48.98652  ? 109  TRP   B CZ3 1 
ATOM   4148 C CH2 . TRP   B 1 133 ? -11.28600 39.62100  -14.35400 1.000 48.67297  ? 109  TRP   B CH2 1 
ATOM   4149 N N   . THR   B 1 134 ? -14.45600 34.62200  -12.84100 1.000 48.49744  ? 110  THR   B N   1 
ATOM   4150 C CA  . THR   B 1 134 ? -15.57200 35.47200  -12.45900 1.000 54.39574  ? 110  THR   B CA  1 
ATOM   4151 C C   . THR   B 1 134 ? -16.57000 34.77400  -11.54100 1.000 48.73787  ? 110  THR   B C   1 
ATOM   4152 O O   . THR   B 1 134 ? -17.38900 35.45300  -10.91600 1.000 46.11179  ? 110  THR   B O   1 
ATOM   4153 C CB  . THR   B 1 134 ? -16.28900 35.99300  -13.70600 1.000 52.66653  ? 110  THR   B CB  1 
ATOM   4154 O OG1 . THR   B 1 134 ? -17.16700 37.06500  -13.33800 1.000 51.28037  ? 110  THR   B OG1 1 
ATOM   4155 C CG2 . THR   B 1 134 ? -17.07900 34.87100  -14.37300 1.000 48.84467  ? 110  THR   B CG2 1 
ATOM   4156 N N   . SER   B 1 135 ? -16.52400 33.44500  -11.44100 1.000 45.43226  ? 111  SER   B N   1 
ATOM   4157 C CA  . SER   B 1 135 ? -17.34200 32.75400  -10.45200 1.000 41.63732  ? 111  SER   B CA  1 
ATOM   4158 C C   . SER   B 1 135 ? -16.73300 32.86300  -9.06100  1.000 45.89045  ? 111  SER   B C   1 
ATOM   4159 O O   . SER   B 1 135 ? -17.45000 33.10200  -8.08300  1.000 43.16999  ? 111  SER   B O   1 
ATOM   4160 C CB  . SER   B 1 135 ? -17.50900 31.29000  -10.84000 1.000 39.65687  ? 111  SER   B CB  1 
ATOM   4161 O OG  . SER   B 1 135 ? -17.63700 31.15700  -12.24100 1.000 51.47802  ? 111  SER   B OG  1 
ATOM   4162 N N   . ILE   B 1 136 ? -15.41400 32.68400  -8.95500  1.000 45.42261  ? 112  ILE   B N   1 
ATOM   4163 C CA  . ILE   B 1 136 ? -14.73300 32.94200  -7.69000  1.000 41.18240  ? 112  ILE   B CA  1 
ATOM   4164 C C   . ILE   B 1 136 ? -14.90800 34.39900  -7.28900  1.000 39.90639  ? 112  ILE   B C   1 
ATOM   4165 O O   . ILE   B 1 136 ? -15.07300 34.71900  -6.10600  1.000 44.94415  ? 112  ILE   B O   1 
ATOM   4166 C CB  . ILE   B 1 136 ? -13.24600 32.55500  -7.79000  1.000 42.90886  ? 112  ILE   B CB  1 
ATOM   4167 C CG1 . ILE   B 1 136 ? -13.08800 31.03600  -7.87800  1.000 47.21131  ? 112  ILE   B CG1 1 
ATOM   4168 C CG2 . ILE   B 1 136 ? -12.46100 33.09600  -6.61000  1.000 39.87106  ? 112  ILE   B CG2 1 
ATOM   4169 C CD1 . ILE   B 1 136 ? -11.66000 30.59600  -8.12200  1.000 49.10646  ? 112  ILE   B CD1 1 
ATOM   4170 N N   . ASP   B 1 137 ? -14.88500 35.30400  -8.26900  1.000 40.37908  ? 113  ASP   B N   1 
ATOM   4171 C CA  . ASP   B 1 137 ? -15.09500 36.72000  -7.98400  1.000 40.53491  ? 113  ASP   B CA  1 
ATOM   4172 C C   . ASP   B 1 137 ? -16.44000 36.94700  -7.30500  1.000 48.37742  ? 113  ASP   B C   1 
ATOM   4173 O O   . ASP   B 1 137 ? -16.51700 37.58600  -6.24900  1.000 47.46787  ? 113  ASP   B O   1 
ATOM   4174 C CB  . ASP   B 1 137 ? -14.99400 37.52300  -9.28000  1.000 42.66036  ? 113  ASP   B CB  1 
ATOM   4175 C CG  . ASP   B 1 137 ? -14.96500 39.02000  -9.04700  1.000 43.63256  ? 113  ASP   B CG  1 
ATOM   4176 O OD1 . ASP   B 1 137 ? -15.29900 39.47300  -7.93100  1.000 41.19935  ? 113  ASP   B OD1 1 
ATOM   4177 O OD2 . ASP   B 1 137 ? -14.60600 39.75300  -9.99100  1.000 49.05540  ? 113  ASP   B OD2 1 
ATOM   4178 N N   . VAL   B 1 138 ? -17.51500 36.42900  -7.89900  1.000 51.45519  ? 114  VAL   B N   1 
ATOM   4179 C CA  . VAL   B 1 138 ? -18.83100 36.59500  -7.29500  1.000 51.29549  ? 114  VAL   B CA  1 
ATOM   4180 C C   . VAL   B 1 138 ? -18.91100 35.82700  -5.98100  1.000 45.15756  ? 114  VAL   B C   1 
ATOM   4181 O O   . VAL   B 1 138 ? -19.52300 36.29200  -5.01300  1.000 41.33595  ? 114  VAL   B O   1 
ATOM   4182 C CB  . VAL   B 1 138 ? -19.93300 36.16900  -8.28500  1.000 47.70766  ? 114  VAL   B CB  1 
ATOM   4183 C CG1 . VAL   B 1 138 ? -21.30800 36.36800  -7.67500  1.000 50.52185  ? 114  VAL   B CG1 1 
ATOM   4184 C CG2 . VAL   B 1 138 ? -19.82300 36.97100  -9.56400  1.000 43.39433  ? 114  VAL   B CG2 1 
ATOM   4185 N N   . LEU   B 1 139 ? -18.26600 34.65900  -5.91300  1.000 42.81172  ? 115  LEU   B N   1 
ATOM   4186 C CA  . LEU   B 1 139 ? -18.31600 33.85600  -4.69500  1.000 41.77294  ? 115  LEU   B CA  1 
ATOM   4187 C C   . LEU   B 1 139 ? -17.73700 34.61600  -3.51000  1.000 43.30649  ? 115  LEU   B C   1 
ATOM   4188 O O   . LEU   B 1 139 ? -18.29000 34.57000  -2.40500  1.000 41.41084  ? 115  LEU   B O   1 
ATOM   4189 C CB  . LEU   B 1 139 ? -17.57000 32.53700  -4.90100  1.000 37.97393  ? 115  LEU   B CB  1 
ATOM   4190 C CG  . LEU   B 1 139 ? -17.34600 31.65100  -3.67600  1.000 31.77878  ? 115  LEU   B CG  1 
ATOM   4191 C CD1 . LEU   B 1 139 ? -18.65300 31.41300  -2.95100  1.000 37.27045  ? 115  LEU   B CD1 1 
ATOM   4192 C CD2 . LEU   B 1 139 ? -16.72600 30.32900  -4.08900  1.000 32.52362  ? 115  LEU   B CD2 1 
ATOM   4193 N N   . CYS   B 1 140 ? -16.63200 35.33000  -3.72400  1.000 40.58550  ? 116  CYS   B N   1 
ATOM   4194 C CA  . CYS   B 1 140 ? -16.01600 36.08900  -2.64200  1.000 37.96261  ? 116  CYS   B CA  1 
ATOM   4195 C C   . CYS   B 1 140 ? -16.90000 37.25500  -2.21000  1.000 41.32609  ? 116  CYS   B C   1 
ATOM   4196 O O   . CYS   B 1 140 ? -17.10600 37.47700  -1.01200  1.000 48.47333  ? 116  CYS   B O   1 
ATOM   4197 C CB  . CYS   B 1 140 ? -14.63600 36.58700  -3.07000  1.000 37.44539  ? 116  CYS   B CB  1 
ATOM   4198 S SG  . CYS   B 1 140 ? -13.34000 35.33000  -3.02600  1.000 39.98180  ? 116  CYS   B SG  1 
ATOM   4199 N N   . VAL   B 1 141 ? -17.43900 38.00700  -3.16900  1.000 44.98576  ? 117  VAL   B N   1 
ATOM   4200 C CA  . VAL   B 1 141 ? -18.21600 39.19500  -2.82400  1.000 45.04341  ? 117  VAL   B CA  1 
ATOM   4201 C C   . VAL   B 1 141 ? -19.51600 38.81300  -2.12200  1.000 43.61058  ? 117  VAL   B C   1 
ATOM   4202 O O   . VAL   B 1 141 ? -19.88600 39.41900  -1.11000  1.000 44.77573  ? 117  VAL   B O   1 
ATOM   4203 C CB  . VAL   B 1 141 ? -18.47000 40.05000  -4.07700  1.000 45.77746  ? 117  VAL   B CB  1 
ATOM   4204 C CG1 . VAL   B 1 141 ? -19.16600 41.34500  -3.70300  1.000 43.37567  ? 117  VAL   B CG1 1 
ATOM   4205 C CG2 . VAL   B 1 141 ? -17.15700 40.34200  -4.78400  1.000 51.40757  ? 117  VAL   B CG2 1 
ATOM   4206 N N   . THR   B 1 142 ? -20.22600 37.80500  -2.63600  1.000 44.50360  ? 118  THR   B N   1 
ATOM   4207 C CA  . THR   B 1 142 ? -21.48100 37.40100  -2.00600  1.000 44.10699  ? 118  THR   B CA  1 
ATOM   4208 C C   . THR   B 1 142 ? -21.25400 36.81700  -0.61700  1.000 43.51896  ? 118  THR   B C   1 
ATOM   4209 O O   . THR   B 1 142 ? -22.06600 37.03600  0.29000   1.000 42.75485  ? 118  THR   B O   1 
ATOM   4210 C CB  . THR   B 1 142 ? -22.22500 36.39400  -2.88300  1.000 48.58916  ? 118  THR   B CB  1 
ATOM   4211 O OG1 . THR   B 1 142 ? -21.52600 35.14200  -2.88400  1.000 52.88663  ? 118  THR   B OG1 1 
ATOM   4212 C CG2 . THR   B 1 142 ? -22.37300 36.91200  -4.29900  1.000 48.75252  ? 118  THR   B CG2 1 
ATOM   4213 N N   . ALA   B 1 143 ? -20.16900 36.06000  -0.42900  1.000 43.68660  ? 119  ALA   B N   1 
ATOM   4214 C CA  . ALA   B 1 143 ? -19.91300 35.47000  0.88300   1.000 36.92740  ? 119  ALA   B CA  1 
ATOM   4215 C C   . ALA   B 1 143 ? -19.57700 36.53100  1.92000   1.000 30.31118  ? 119  ALA   B C   1 
ATOM   4216 O O   . ALA   B 1 143 ? -19.90900 36.36800  3.09700   1.000 34.52177  ? 119  ALA   B O   1 
ATOM   4217 C CB  . ALA   B 1 143 ? -18.78800 34.43900  0.79800   1.000 33.93130  ? 119  ALA   B CB  1 
ATOM   4218 N N   . SER   B 1 144 ? -18.93600 37.62300  1.50600   1.000 28.95469  ? 120  SER   B N   1 
ATOM   4219 C CA  . SER   B 1 144 ? -18.59000 38.67400  2.45600   1.000 35.18644  ? 120  SER   B CA  1 
ATOM   4220 C C   . SER   B 1 144 ? -19.83200 39.40500  2.94600   1.000 37.81458  ? 120  SER   B C   1 
ATOM   4221 O O   . SER   B 1 144 ? -19.99700 39.62700  4.15100   1.000 39.86791  ? 120  SER   B O   1 
ATOM   4222 C CB  . SER   B 1 144 ? -17.60000 39.65100  1.82500   1.000 35.89030  ? 120  SER   B CB  1 
ATOM   4223 O OG  . SER   B 1 144 ? -16.51900 38.96000  1.22200   1.000 39.28747  ? 120  SER   B OG  1 
ATOM   4224 N N   . ILE   B 1 145 ? -20.72300 39.78200  2.02700   1.000 36.52754  ? 121  ILE   B N   1 
ATOM   4225 C CA  . ILE   B 1 145 ? -21.90200 40.54400  2.42300   1.000 37.92263  ? 121  ILE   B CA  1 
ATOM   4226 C C   . ILE   B 1 145 ? -22.85400 39.68400  3.25000   1.000 38.24985  ? 121  ILE   B C   1 
ATOM   4227 O O   . ILE   B 1 145 ? -23.52600 40.19000  4.15800   1.000 35.06149  ? 121  ILE   B O   1 
ATOM   4228 C CB  . ILE   B 1 145 ? -22.59400 41.14000  1.18200   1.000 35.06877  ? 121  ILE   B CB  1 
ATOM   4229 C CG1 . ILE   B 1 145 ? -23.71400 42.09200  1.59900   1.000 35.92457  ? 121  ILE   B CG1 1 
ATOM   4230 C CG2 . ILE   B 1 145 ? -23.12900 40.04100  0.28800   1.000 32.18785  ? 121  ILE   B CG2 1 
ATOM   4231 C CD1 . ILE   B 1 145 ? -23.27500 43.14000  2.59200   1.000 35.72651  ? 121  ILE   B CD1 1 
ATOM   4232 N N   . GLU   B 1 146 ? -22.92800 38.38200  2.96500   1.000 35.11855  ? 122  GLU   B N   1 
ATOM   4233 C CA  . GLU   B 1 146 ? -23.71100 37.49700  3.81800   1.000 34.10538  ? 122  GLU   B CA  1 
ATOM   4234 C C   . GLU   B 1 146 ? -23.05800 37.34000  5.18200   1.000 43.57519  ? 122  GLU   B C   1 
ATOM   4235 O O   . GLU   B 1 146 ? -23.73600 37.40500  6.21500   1.000 45.51816  ? 122  GLU   B O   1 
ATOM   4236 C CB  . GLU   B 1 146 ? -23.89200 36.13200  3.15500   1.000 32.75323  ? 122  GLU   B CB  1 
ATOM   4237 C CG  . GLU   B 1 146 ? -25.24800 35.94200  2.50400   1.000 48.85902  ? 122  GLU   B CG  1 
ATOM   4238 C CD  . GLU   B 1 146 ? -25.33900 34.66000  1.69300   1.000 56.83210  ? 122  GLU   B CD  1 
ATOM   4239 O OE1 . GLU   B 1 146 ? -24.93000 33.59400  2.20500   1.000 49.37068  ? 122  GLU   B OE1 1 
ATOM   4240 O OE2 . GLU   B 1 146 ? -25.83100 34.71800  0.54500   1.000 56.80980  ? 122  GLU   B OE2 1 
ATOM   4241 N N   . THR   B 1 147 ? -21.73800 37.14100  5.20700   1.000 40.82383  ? 123  THR   B N   1 
ATOM   4242 C CA  . THR   B 1 147 ? -21.04500 36.94800  6.47700   1.000 36.91014  ? 123  THR   B CA  1 
ATOM   4243 C C   . THR   B 1 147 ? -21.07700 38.21800  7.31800   1.000 37.35217  ? 123  THR   B C   1 
ATOM   4244 O O   . THR   B 1 147 ? -21.19100 38.15000  8.54700   1.000 38.06625  ? 123  THR   B O   1 
ATOM   4245 C CB  . THR   B 1 147 ? -19.60900 36.49200  6.22000   1.000 35.38742  ? 123  THR   B CB  1 
ATOM   4246 O OG1 . THR   B 1 147 ? -19.61400 35.12500  5.78600   1.000 33.11933  ? 123  THR   B OG1 1 
ATOM   4247 C CG2 . THR   B 1 147 ? -18.76400 36.60700  7.48000   1.000 39.54016  ? 123  THR   B CG2 1 
ATOM   4248 N N   . LEU   B 1 148 ? -21.00800 39.38500  6.67400   1.000 37.73509  ? 124  LEU   B N   1 
ATOM   4249 C CA  . LEU   B 1 148 ? -21.04700 40.63900  7.41900   1.000 33.02156  ? 124  LEU   B CA  1 
ATOM   4250 C C   . LEU   B 1 148 ? -22.36200 40.82300  8.15900   1.000 40.15009  ? 124  LEU   B C   1 
ATOM   4251 O O   . LEU   B 1 148 ? -22.39100 41.47400  9.20900   1.000 50.61610  ? 124  LEU   B O   1 
ATOM   4252 C CB  . LEU   B 1 148 ? -20.81300 41.82400  6.48900   1.000 38.75994  ? 124  LEU   B CB  1 
ATOM   4253 C CG  . LEU   B 1 148 ? -19.36700 42.29200  6.36400   1.000 46.19325  ? 124  LEU   B CG  1 
ATOM   4254 C CD1 . LEU   B 1 148 ? -19.23500 43.32000  5.24400   1.000 43.47404  ? 124  LEU   B CD1 1 
ATOM   4255 C CD2 . LEU   B 1 148 ? -18.89500 42.85700  7.68900   1.000 33.99834  ? 124  LEU   B CD2 1 
ATOM   4256 N N   . CYS   B 1 149 ? -23.46100 40.27400  7.63800   1.000 38.24760  ? 125  CYS   B N   1 
ATOM   4257 C CA  . CYS   B 1 149 ? -24.73400 40.41600  8.33300   1.000 44.26333  ? 125  CYS   B CA  1 
ATOM   4258 C C   . CYS   B 1 149 ? -25.04200 39.24100  9.25200   1.000 42.34079  ? 125  CYS   B C   1 
ATOM   4259 O O   . CYS   B 1 149 ? -25.82000 39.40500  10.20000  1.000 46.70313  ? 125  CYS   B O   1 
ATOM   4260 C CB  . CYS   B 1 149 ? -25.88200 40.63300  7.33400   1.000 40.90293  ? 125  CYS   B CB  1 
ATOM   4261 S SG  . CYS   B 1 149 ? -26.41400 39.21500  6.37500   1.000 52.67121  ? 125  CYS   B SG  1 
ATOM   4262 N N   . VAL   B 1 150 ? -24.44500 38.06900  9.01700   1.000 38.76781  ? 126  VAL   B N   1 
ATOM   4263 C CA  . VAL   B 1 150 ? -24.48100 37.02100  10.03100  1.000 38.76141  ? 126  VAL   B CA  1 
ATOM   4264 C C   . VAL   B 1 150 ? -23.72500 37.46900  11.27800  1.000 39.39939  ? 126  VAL   B C   1 
ATOM   4265 O O   . VAL   B 1 150 ? -23.93300 36.92400  12.36600  1.000 40.34542  ? 126  VAL   B O   1 
ATOM   4266 C CB  . VAL   B 1 150 ? -23.92600 35.69800  9.45200   1.000 37.41401  ? 126  VAL   B CB  1 
ATOM   4267 C CG1 . VAL   B 1 150 ? -23.91300 34.59700  10.49800  1.000 27.30783  ? 126  VAL   B CG1 1 
ATOM   4268 C CG2 . VAL   B 1 150 ? -24.74700 35.26100  8.25400   1.000 37.46676  ? 126  VAL   B CG2 1 
ATOM   4269 N N   . ILE   B 1 151 ? -22.86200 38.47500  11.14800  1.000 35.24237  ? 127  ILE   B N   1 
ATOM   4270 C CA  . ILE   B 1 151 ? -22.27400 39.10900  12.32100  1.000 35.47493  ? 127  ILE   B CA  1 
ATOM   4271 C C   . ILE   B 1 151 ? -23.26500 40.07500  12.95200  1.000 40.71534  ? 127  ILE   B C   1 
ATOM   4272 O O   . ILE   B 1 151 ? -23.49400 40.05000  14.16700  1.000 41.31767  ? 127  ILE   B O   1 
ATOM   4273 C CB  . ILE   B 1 151 ? -20.96300 39.82200  11.94300  1.000 34.30440  ? 127  ILE   B CB  1 
ATOM   4274 C CG1 . ILE   B 1 151 ? -19.86900 38.79800  11.65200  1.000 34.68689  ? 127  ILE   B CG1 1 
ATOM   4275 C CG2 . ILE   B 1 151 ? -20.52600 40.76800  13.05400  1.000 37.29717  ? 127  ILE   B CG2 1 
ATOM   4276 C CD1 . ILE   B 1 151 ? -18.66600 39.38400  10.96900  1.000 29.89519  ? 127  ILE   B CD1 1 
ATOM   4277 N N   . ALA   B 1 152 ? -23.87600 40.93300  12.13100  1.000 40.51806  ? 128  ALA   B N   1 
ATOM   4278 C CA  . ALA   B 1 152 ? -24.79400 41.93800  12.65400  1.000 39.72544  ? 128  ALA   B CA  1 
ATOM   4279 C C   . ALA   B 1 152 ? -25.97300 41.30400  13.38000  1.000 41.16751  ? 128  ALA   B C   1 
ATOM   4280 O O   . ALA   B 1 152 ? -26.47600 41.87300  14.35500  1.000 46.62536  ? 128  ALA   B O   1 
ATOM   4281 C CB  . ALA   B 1 152 ? -25.28600 42.83800  11.52200  1.000 40.32942  ? 128  ALA   B CB  1 
ATOM   4282 N N   . VAL   B 1 153 ? -26.42700 40.13400  12.92900  1.000 37.40954  ? 129  VAL   B N   1 
ATOM   4283 C CA  . VAL   B 1 153 ? -27.50900 39.45000  13.62800  1.000 37.42710  ? 129  VAL   B CA  1 
ATOM   4284 C C   . VAL   B 1 153 ? -26.98400 38.77100  14.88500  1.000 40.15922  ? 129  VAL   B C   1 
ATOM   4285 O O   . VAL   B 1 153 ? -27.63300 38.80100  15.93700  1.000 39.61833  ? 129  VAL   B O   1 
ATOM   4286 C CB  . VAL   B 1 153 ? -28.20500 38.44800  12.68800  1.000 36.76115  ? 129  VAL   B CB  1 
ATOM   4287 C CG1 . VAL   B 1 153 ? -28.93000 37.37300  13.48400  1.000 34.84889  ? 129  VAL   B CG1 1 
ATOM   4288 C CG2 . VAL   B 1 153 ? -29.16700 39.16800  11.77100  1.000 28.94164  ? 129  VAL   B CG2 1 
ATOM   4289 N N   . ASP   B 1 154 ? -25.79800 38.15800  14.80100  1.000 41.43840  ? 130  ASP   B N   1 
ATOM   4290 C CA  . ASP   B 1 154 ? -25.19500 37.54400  15.98000  1.000 37.97888  ? 130  ASP   B CA  1 
ATOM   4291 C C   . ASP   B 1 154 ? -24.89900 38.58400  17.05000  1.000 36.86646  ? 130  ASP   B C   1 
ATOM   4292 O O   . ASP   B 1 154 ? -25.05200 38.31700  18.24700  1.000 40.81916  ? 130  ASP   B O   1 
ATOM   4293 C CB  . ASP   B 1 154 ? -23.91800 36.80300  15.59600  1.000 34.57701  ? 130  ASP   B CB  1 
ATOM   4294 C CG  . ASP   B 1 154 ? -23.27500 36.11900  16.77600  1.000 40.77437  ? 130  ASP   B CG  1 
ATOM   4295 O OD1 . ASP   B 1 154 ? -23.69100 34.99000  17.10400  1.000 44.86006  ? 130  ASP   B OD1 1 
ATOM   4296 O OD2 . ASP   B 1 154 ? -22.36400 36.71600  17.39000  1.000 43.55530  ? 130  ASP   B OD2 1 
ATOM   4297 N N   . ARG   B 1 155 ? -24.47100 39.77800  16.63600  1.000 35.29224  ? 131  ARG   B N   1 
ATOM   4298 C CA  . ARG   B 1 155 ? -24.26700 40.85800  17.59100  1.000 36.74336  ? 131  ARG   B CA  1 
ATOM   4299 C C   . ARG   B 1 155 ? -25.57600 41.31000  18.22100  1.000 42.40042  ? 131  ARG   B C   1 
ATOM   4300 O O   . ARG   B 1 155 ? -25.57600 41.79100  19.36000  1.000 47.24299  ? 131  ARG   B O   1 
ATOM   4301 C CB  . ARG   B 1 155 ? -23.56800 42.03600  16.91200  1.000 39.82497  ? 131  ARG   B CB  1 
ATOM   4302 C CG  . ARG   B 1 155 ? -22.11500 41.78400  16.52900  1.000 42.36782  ? 131  ARG   B CG  1 
ATOM   4303 C CD  . ARG   B 1 155 ? -21.24600 41.45800  17.74500  1.000 43.30019  ? 131  ARG   B CD  1 
ATOM   4304 N NE  . ARG   B 1 155 ? -21.36300 40.06600  18.16000  1.000 38.47677  ? 131  ARG   B NE  1 
ATOM   4305 C CZ  . ARG   B 1 155 ? -21.04500 39.61500  19.36300  1.000 32.77700  ? 131  ARG   B CZ  1 
ATOM   4306 N NH1 . ARG   B 1 155 ? -20.53700 40.41400  20.28600  1.000 31.76947  ? 131  ARG   B NH1 1 
ATOM   4307 N NH2 . ARG   B 1 155 ? -21.24300 38.33100  19.64600  1.000 30.38821  ? 131  ARG   B NH2 1 
ATOM   4308 N N   . TYR   B 1 156 ? -26.69600 41.16000  17.51000  1.000 47.10508  ? 132  TYR   B N   1 
ATOM   4309 C CA  . TYR   B 1 156 ? -27.96800 41.64000  18.04200  1.000 48.01820  ? 132  TYR   B CA  1 
ATOM   4310 C C   . TYR   B 1 156 ? -28.46500 40.74800  19.17300  1.000 42.00926  ? 132  TYR   B C   1 
ATOM   4311 O O   . TYR   B 1 156 ? -28.78300 41.23300  20.26400  1.000 46.06275  ? 132  TYR   B O   1 
ATOM   4312 C CB  . TYR   B 1 156 ? -29.01200 41.72400  16.93200  1.000 42.47122  ? 132  TYR   B CB  1 
ATOM   4313 C CG  . TYR   B 1 156 ? -30.35400 42.18400  17.44400  1.000 44.72448  ? 132  TYR   B CG  1 
ATOM   4314 C CD1 . TYR   B 1 156 ? -30.61900 43.53700  17.61300  1.000 50.66421  ? 132  TYR   B CD1 1 
ATOM   4315 C CD2 . TYR   B 1 156 ? -31.34500 41.27200  17.78200  1.000 41.68946  ? 132  TYR   B CD2 1 
ATOM   4316 C CE1 . TYR   B 1 156 ? -31.83900 43.96900  18.09000  1.000 56.00576  ? 132  TYR   B CE1 1 
ATOM   4317 C CE2 . TYR   B 1 156 ? -32.56700 41.69500  18.26300  1.000 46.36960  ? 132  TYR   B CE2 1 
ATOM   4318 C CZ  . TYR   B 1 156 ? -32.80800 43.04500  18.41400  1.000 58.14681  ? 132  TYR   B CZ  1 
ATOM   4319 O OH  . TYR   B 1 156 ? -34.02400 43.47600  18.89200  1.000 72.16983  ? 132  TYR   B OH  1 
ATOM   4320 N N   . PHE   B 1 157 ? -28.54500 39.43800  18.92700  1.000 33.58666  ? 133  PHE   B N   1 
ATOM   4321 C CA  . PHE   B 1 157 ? -29.00700 38.51500  19.95800  1.000 38.92971  ? 133  PHE   B CA  1 
ATOM   4322 C C   . PHE   B 1 157 ? -28.11700 38.54700  21.19400  1.000 50.95159  ? 133  PHE   B C   1 
ATOM   4323 O O   . PHE   B 1 157 ? -28.54300 38.10200  22.26500  1.000 49.26854  ? 133  PHE   B O   1 
ATOM   4324 C CB  . PHE   B 1 157 ? -29.07100 37.09400  19.39600  1.000 33.90978  ? 133  PHE   B CB  1 
ATOM   4325 C CG  . PHE   B 1 157 ? -30.26600 36.84200  18.52100  1.000 46.64187  ? 133  PHE   B CG  1 
ATOM   4326 C CD1 . PHE   B 1 157 ? -30.47700 37.59700  17.37900  1.000 51.11910  ? 133  PHE   B CD1 1 
ATOM   4327 C CD2 . PHE   B 1 157 ? -31.17100 35.84000  18.83500  1.000 47.14066  ? 133  PHE   B CD2 1 
ATOM   4328 C CE1 . PHE   B 1 157 ? -31.57200 37.36500  16.57000  1.000 53.54299  ? 133  PHE   B CE1 1 
ATOM   4329 C CE2 . PHE   B 1 157 ? -32.26900 35.60200  18.02800  1.000 42.34228  ? 133  PHE   B CE2 1 
ATOM   4330 C CZ  . PHE   B 1 157 ? -32.46800 36.36700  16.89300  1.000 57.90702  ? 133  PHE   B CZ  1 
ATOM   4331 N N   . ALA   B 1 158 ? -26.89900 39.07400  21.06900  1.000 46.93787  ? 134  ALA   B N   1 
ATOM   4332 C CA  . ALA   B 1 158 ? -25.93700 39.13800  22.15900  1.000 43.37563  ? 134  ALA   B CA  1 
ATOM   4333 C C   . ALA   B 1 158 ? -26.16700 40.33800  23.06400  1.000 43.58369  ? 134  ALA   B C   1 
ATOM   4334 O O   . ALA   B 1 158 ? -26.01600 40.23200  24.28500  1.000 50.46793  ? 134  ALA   B O   1 
ATOM   4335 C CB  . ALA   B 1 158 ? -24.51600 39.17500  21.59400  1.000 40.76513  ? 134  ALA   B CB  1 
ATOM   4336 N N   . ILE   B 1 159 ? -26.51800 41.48600  22.48200  1.000 41.70697  ? 135  ILE   B N   1 
ATOM   4337 C CA  . ILE   B 1 159 ? -26.75800 42.69200  23.26700  1.000 44.82061  ? 135  ILE   B CA  1 
ATOM   4338 C C   . ILE   B 1 159 ? -28.11600 42.66500  23.94600  1.000 49.87418  ? 135  ILE   B C   1 
ATOM   4339 O O   . ILE   B 1 159 ? -28.40500 43.53200  24.78000  1.000 49.51160  ? 135  ILE   B O   1 
ATOM   4340 C CB  . ILE   B 1 159 ? -26.60000 43.92000  22.35300  1.000 46.96703  ? 135  ILE   B CB  1 
ATOM   4341 C CG1 . ILE   B 1 159 ? -26.09300 45.11700  23.15200  1.000 51.99640  ? 135  ILE   B CG1 1 
ATOM   4342 C CG2 . ILE   B 1 159 ? -27.91100 44.23900  21.64600  1.000 50.21169  ? 135  ILE   B CG2 1 
ATOM   4343 C CD1 . ILE   B 1 159 ? -25.24600 46.04200  22.33100  1.000 50.87622  ? 135  ILE   B CD1 1 
ATOM   4344 N N   . THR   B 1 160 ? -28.95400 41.69000  23.60300  1.000 48.85143  ? 136  THR   B N   1 
ATOM   4345 C CA  . THR   B 1 160 ? -30.20100 41.41600  24.30000  1.000 51.28569  ? 136  THR   B CA  1 
ATOM   4346 C C   . THR   B 1 160 ? -30.08400 40.20400  25.21900  1.000 48.31133  ? 136  THR   B C   1 
ATOM   4347 O O   . THR   B 1 160 ? -31.09400 39.55800  25.52000  1.000 50.54612  ? 136  THR   B O   1 
ATOM   4348 C CB  . THR   B 1 160 ? -31.32800 41.21000  23.28600  1.000 51.65724  ? 136  THR   B CB  1 
ATOM   4349 O OG1 . THR   B 1 160 ? -31.09700 39.99500  22.56100  1.000 45.56753  ? 136  THR   B OG1 1 
ATOM   4350 C CG2 . THR   B 1 160 ? -31.38200 42.37900  22.31400  1.000 49.66333  ? 136  THR   B CG2 1 
ATOM   4351 N N   . SER   B 1 161 ? -28.87100 39.88200  25.65300  1.000 42.76052  ? 137  SER   B N   1 
ATOM   4352 C CA  . SER   B 1 161 ? -28.56300 38.72500  26.47300  1.000 46.03438  ? 137  SER   B CA  1 
ATOM   4353 C C   . SER   B 1 161 ? -27.84900 39.16500  27.74300  1.000 51.24457  ? 137  SER   B C   1 
ATOM   4354 O O   . SER   B 1 161 ? -27.31600 40.28000  27.80200  1.000 49.99171  ? 137  SER   B O   1 
ATOM   4355 C CB  . SER   B 1 161 ? -27.70100 37.72900  25.69000  1.000 54.28758  ? 137  SER   B CB  1 
ATOM   4356 O OG  . SER   B 1 161 ? -28.52100 36.84200  24.95500  1.000 58.95311  ? 137  SER   B OG  1 
ATOM   4357 N N   . PRO   B 1 162 ? -27.82400 38.31500  28.78500  1.000 47.86574  ? 138  PRO   B N   1 
ATOM   4358 C CA  . PRO   B 1 162 ? -27.28200 38.76100  30.08200  1.000 43.04919  ? 138  PRO   B CA  1 
ATOM   4359 C C   . PRO   B 1 162 ? -25.92400 39.42500  29.97800  1.000 49.23782  ? 138  PRO   B C   1 
ATOM   4360 O O   . PRO   B 1 162 ? -25.74800 40.56700  30.42100  1.000 46.83776  ? 138  PRO   B O   1 
ATOM   4361 C CB  . PRO   B 1 162 ? -27.22300 37.45700  30.89300  1.000 44.17538  ? 138  PRO   B CB  1 
ATOM   4362 C CG  . PRO   B 1 162 ? -27.33100 36.35200  29.88500  1.000 46.82339  ? 138  PRO   B CG  1 
ATOM   4363 C CD  . PRO   B 1 162 ? -28.22700 36.89900  28.83300  1.000 48.90581  ? 138  PRO   B CD  1 
ATOM   4364 N N   . PHE   B 1 163 ? -24.95700 38.74000  29.38100  1.000 55.12274  ? 139  PHE   B N   1 
ATOM   4365 C CA  . PHE   B 1 163 ? -23.64300 39.32200  29.13900  1.000 47.97013  ? 139  PHE   B CA  1 
ATOM   4366 C C   . PHE   B 1 163 ? -23.73200 39.96300  27.76600  1.000 56.27849  ? 139  PHE   B C   1 
ATOM   4367 O O   . PHE   B 1 163 ? -23.58500 39.30000  26.73800  1.000 65.63683  ? 139  PHE   B O   1 
ATOM   4368 C CB  . PHE   B 1 163 ? -22.55800 38.25500  29.22700  1.000 43.96894  ? 139  PHE   B CB  1 
ATOM   4369 C CG  . PHE   B 1 163 ? -21.15500 38.79800  29.30200  1.000 46.55916  ? 139  PHE   B CG  1 
ATOM   4370 C CD1 . PHE   B 1 163 ? -20.60200 39.50800  28.25700  1.000 54.50356  ? 139  PHE   B CD1 1 
ATOM   4371 C CD2 . PHE   B 1 163 ? -20.38600 38.58000  30.43000  1.000 51.89559  ? 139  PHE   B CD2 1 
ATOM   4372 C CE1 . PHE   B 1 163 ? -19.30900 39.99300  28.33300  1.000 53.12283  ? 139  PHE   B CE1 1 
ATOM   4373 C CE2 . PHE   B 1 163 ? -19.09500 39.06500  30.51200  1.000 56.96518  ? 139  PHE   B CE2 1 
ATOM   4374 C CZ  . PHE   B 1 163 ? -18.55700 39.77100  29.46000  1.000 46.83436  ? 139  PHE   B CZ  1 
ATOM   4375 N N   . LYS   B 1 164 ? -24.05700 41.25500  27.74900  1.000 58.71996  ? 140  LYS   B N   1 
ATOM   4376 C CA  . LYS   B 1 164 ? -23.93000 42.02500  26.52300  1.000 56.94297  ? 140  LYS   B CA  1 
ATOM   4377 C C   . LYS   B 1 164 ? -22.54000 41.78800  25.95600  1.000 63.24594  ? 140  LYS   B C   1 
ATOM   4378 O O   . LYS   B 1 164 ? -21.55900 41.76200  26.70400  1.000 64.65474  ? 140  LYS   B O   1 
ATOM   4379 C CB  . LYS   B 1 164 ? -24.16100 43.51400  26.80300  1.000 51.57039  ? 140  LYS   B CB  1 
ATOM   4380 C CG  . LYS   B 1 164 ? -25.40200 43.78700  27.64600  1.000 55.92666  ? 140  LYS   B CG  1 
ATOM   4381 C CD  . LYS   B 1 164 ? -25.68100 45.27400  27.81600  1.000 58.52500  ? 140  LYS   B CD  1 
ATOM   4382 C CE  . LYS   B 1 164 ? -24.54700 46.00800  28.50400  1.000 60.00455  ? 140  LYS   B CE  1 
ATOM   4383 N NZ  . LYS   B 1 164 ? -24.91400 47.43700  28.73700  1.000 62.23094  ? 140  LYS   B NZ  1 
ATOM   4384 N N   . TYR   B 1 165 ? -22.47100 41.54600  24.64300  1.000 46.99077  ? 141  TYR   B N   1 
ATOM   4385 C CA  . TYR   B 1 165 ? -21.26700 41.27700  23.84100  1.000 39.74158  ? 141  TYR   B CA  1 
ATOM   4386 C C   . TYR   B 1 165 ? -20.91400 39.78900  23.83600  1.000 38.16152  ? 141  TYR   B C   1 
ATOM   4387 O O   . TYR   B 1 165 ? -19.93200 39.40900  23.19500  1.000 35.50661  ? 141  TYR   B O   1 
ATOM   4388 C CB  . TYR   B 1 165 ? -20.03600 42.08000  24.30200  1.000 40.52412  ? 141  TYR   B CB  1 
ATOM   4389 C CG  . TYR   B 1 165 ? -20.35700 43.50300  24.71000  1.000 48.02889  ? 141  TYR   B CG  1 
ATOM   4390 C CD1 . TYR   B 1 165 ? -21.17300 44.30800  23.92500  1.000 47.22466  ? 141  TYR   B CD1 1 
ATOM   4391 C CD2 . TYR   B 1 165 ? -19.92300 44.00800  25.93300  1.000 41.89689  ? 141  TYR   B CD2 1 
ATOM   4392 C CE1 . TYR   B 1 165 ? -21.49100 45.59900  24.31500  1.000 59.19179  ? 141  TYR   B CE1 1 
ATOM   4393 C CE2 . TYR   B 1 165 ? -20.24100 45.28800  26.33300  1.000 44.14220  ? 141  TYR   B CE2 1 
ATOM   4394 C CZ  . TYR   B 1 165 ? -21.02300 46.08100  25.52200  1.000 58.96649  ? 141  TYR   B CZ  1 
ATOM   4395 O OH  . TYR   B 1 165 ? -21.33500 47.35900  25.92700  1.000 57.74918  ? 141  TYR   B OH  1 
ATOM   4396 N N   . GLN   B 1 166 ? -21.68300 38.94000  24.51500  1.000 37.56608  ? 142  GLN   B N   1 
ATOM   4397 C CA  . GLN   B 1 166 ? -21.44000 37.50200  24.54600  1.000 38.15381  ? 142  GLN   B CA  1 
ATOM   4398 C C   . GLN   B 1 166 ? -22.34100 36.82000  23.52700  1.000 44.10852  ? 142  GLN   B C   1 
ATOM   4399 O O   . GLN   B 1 166 ? -23.56700 36.83900  23.66800  1.000 50.27879  ? 142  GLN   B O   1 
ATOM   4400 C CB  . GLN   B 1 166 ? -21.69700 36.92600  25.93800  1.000 40.60043  ? 142  GLN   B CB  1 
ATOM   4401 C CG  . GLN   B 1 166 ? -21.37600 35.44200  26.09400  1.000 40.77238  ? 142  GLN   B CG  1 
ATOM   4402 C CD  . GLN   B 1 166 ? -22.10900 34.79400  27.27300  1.000 42.69254  ? 142  GLN   B CD  1 
ATOM   4403 O OE1 . GLN   B 1 166 ? -22.91200 35.43800  27.95500  1.000 38.07981  ? 142  GLN   B OE1 1 
ATOM   4404 N NE2 . GLN   B 1 166 ? -21.83100 33.51500  27.51300  1.000 33.11908  ? 142  GLN   B NE2 1 
ATOM   4405 N N   . SER   B 1 167 ? -21.73500 36.21400  22.51200  1.000 42.76022  ? 143  SER   B N   1 
ATOM   4406 C CA  . SER   B 1 167 ? -22.51000 35.50000  21.50900  1.000 46.23356  ? 143  SER   B CA  1 
ATOM   4407 C C   . SER   B 1 167 ? -23.22600 34.30700  22.13000  1.000 46.36304  ? 143  SER   B C   1 
ATOM   4408 O O   . SER   B 1 167 ? -22.74800 33.69200  23.08500  1.000 47.98355  ? 143  SER   B O   1 
ATOM   4409 C CB  . SER   B 1 167 ? -21.62100 35.02900  20.36200  1.000 44.12856  ? 143  SER   B CB  1 
ATOM   4410 O OG  . SER   B 1 167 ? -22.38900 34.36000  19.37500  1.000 38.00014  ? 143  SER   B OG  1 
ATOM   4411 N N   . LEU   B 1 168 ? -24.38700 33.98500  21.56900  1.000 44.06020  ? 144  LEU   B N   1 
ATOM   4412 C CA  . LEU   B 1 168 ? -25.21000 32.87500  22.02400  1.000 38.15903  ? 144  LEU   B CA  1 
ATOM   4413 C C   . LEU   B 1 168 ? -24.89000 31.57800  21.29600  1.000 42.34330  ? 144  LEU   B C   1 
ATOM   4414 O O   . LEU   B 1 168 ? -25.57100 30.57100  21.51100  1.000 46.66507  ? 144  LEU   B O   1 
ATOM   4415 C CB  . LEU   B 1 168 ? -26.69600 33.22100  21.86100  1.000 32.69587  ? 144  LEU   B CB  1 
ATOM   4416 C CG  . LEU   B 1 168 ? -27.31200 34.28900  22.77700  1.000 40.38812  ? 144  LEU   B CG  1 
ATOM   4417 C CD1 . LEU   B 1 168 ? -26.67500 35.66200  22.62900  1.000 41.39247  ? 144  LEU   B CD1 1 
ATOM   4418 C CD2 . LEU   B 1 168 ? -28.81000 34.38500  22.53600  1.000 43.22393  ? 144  LEU   B CD2 1 
ATOM   4419 N N   . LEU   B 1 169 ? -23.85900 31.57800  20.46000  1.000 46.62574  ? 145  LEU   B N   1 
ATOM   4420 C CA  . LEU   B 1 169 ? -23.54900 30.46400  19.58100  1.000 44.51200  ? 145  LEU   B CA  1 
ATOM   4421 C C   . LEU   B 1 169 ? -22.41000 29.62200  20.13900  1.000 42.82813  ? 145  LEU   B C   1 
ATOM   4422 O O   . LEU   B 1 169 ? -21.51500 30.12300  20.82400  1.000 49.79534  ? 145  LEU   B O   1 
ATOM   4423 C CB  . LEU   B 1 169 ? -23.17400 30.97600  18.19100  1.000 48.44955  ? 145  LEU   B CB  1 
ATOM   4424 C CG  . LEU   B 1 169 ? -24.31600 31.23600  17.20900  1.000 45.96949  ? 145  LEU   B CG  1 
ATOM   4425 C CD1 . LEU   B 1 169 ? -23.79500 32.00900  16.01200  1.000 40.86555  ? 145  LEU   B CD1 1 
ATOM   4426 C CD2 . LEU   B 1 169 ? -24.95200 29.92600  16.76800  1.000 39.64104  ? 145  LEU   B CD2 1 
ATOM   4427 N N   . THR   B 1 170 ? -22.46500 28.32900  19.84300  1.000 42.00774  ? 146  THR   B N   1 
ATOM   4428 C CA  . THR   B 1 170 ? -21.34800 27.43200  20.07800  1.000 39.45761  ? 146  THR   B CA  1 
ATOM   4429 C C   . THR   B 1 170 ? -20.27300 27.67600  19.02600  1.000 47.28003  ? 146  THR   B C   1 
ATOM   4430 O O   . THR   B 1 170 ? -20.56300 28.09100  17.90100  1.000 49.58997  ? 146  THR   B O   1 
ATOM   4431 C CB  . THR   B 1 170 ? -21.83300 25.97900  20.04300  1.000 39.24923  ? 146  THR   B CB  1 
ATOM   4432 O OG1 . THR   B 1 170 ? -22.62100 25.71700  21.20900  1.000 50.40337  ? 146  THR   B OG1 1 
ATOM   4433 C CG2 . THR   B 1 170 ? -20.68600 24.98400  19.98300  1.000 40.20726  ? 146  THR   B CG2 1 
ATOM   4434 N N   . LYS   B 1 171 ? -19.01500 27.45700  19.41800  1.000 50.64571  ? 147  LYS   B N   1 
ATOM   4435 C CA  . LYS   B 1 171 ? -17.91600 27.57500  18.46600  1.000 49.88817  ? 147  LYS   B CA  1 
ATOM   4436 C C   . LYS   B 1 171 ? -18.12300 26.64900  17.27200  1.000 48.08764  ? 147  LYS   B C   1 
ATOM   4437 O O   . LYS   B 1 171 ? -17.86700 27.03800  16.12700  1.000 52.42205  ? 147  LYS   B O   1 
ATOM   4438 C CB  . LYS   B 1 171 ? -16.59100 27.28000  19.17000  1.000 52.47687  ? 147  LYS   B CB  1 
ATOM   4439 C CG  . LYS   B 1 171 ? -15.93000 28.51600  19.76700  1.000 46.76046  ? 147  LYS   B CG  1 
ATOM   4440 C CD  . LYS   B 1 171 ? -14.88000 28.14100  20.80000  1.000 59.12056  ? 147  LYS   B CD  1 
ATOM   4441 C CE  . LYS   B 1 171 ? -14.48000 29.34100  21.64900  1.000 62.40868  ? 147  LYS   B CE  1 
ATOM   4442 N NZ  . LYS   B 1 171 ? -13.43500 28.99900  22.65500  1.000 49.59991  ? 147  LYS   B NZ  1 
ATOM   4443 N N   . ASN   B 1 172 ? -18.61300 25.42900  17.51500  1.000 44.40271  ? 148  ASN   B N   1 
ATOM   4444 C CA  . ASN   B 1 172 ? -18.89500 24.51000  16.41600  1.000 41.62984  ? 148  ASN   B CA  1 
ATOM   4445 C C   . ASN   B 1 172 ? -20.17900 24.86700  15.67800  1.000 45.93834  ? 148  ASN   B C   1 
ATOM   4446 O O   . ASN   B 1 172 ? -20.30800 24.56200  14.48800  1.000 53.08264  ? 148  ASN   B O   1 
ATOM   4447 C CB  . ASN   B 1 172 ? -18.97500 23.07300  16.92800  1.000 43.88411  ? 148  ASN   B CB  1 
ATOM   4448 C CG  . ASN   B 1 172 ? -17.94200 22.77800  17.98900  1.000 58.16587  ? 148  ASN   B CG  1 
ATOM   4449 O OD1 . ASN   B 1 172 ? -18.21800 22.87700  19.18700  1.000 57.84946  ? 148  ASN   B OD1 1 
ATOM   4450 N ND2 . ASN   B 1 172 ? -16.74000 22.40900  17.55600  1.000 68.71734  ? 148  ASN   B ND2 1 
ATOM   4451 N N   . LYS   B 1 173 ? -21.14500 25.48700  16.35700  1.000 52.04289  ? 149  LYS   B N   1 
ATOM   4452 C CA  . LYS   B 1 173 ? -22.31100 25.99900  15.64700  1.000 44.48467  ? 149  LYS   B CA  1 
ATOM   4453 C C   . LYS   B 1 173 ? -21.91200 27.12800  14.70700  1.000 41.94460  ? 149  LYS   B C   1 
ATOM   4454 O O   . LYS   B 1 173 ? -22.39700 27.20200  13.57300  1.000 43.67384  ? 149  LYS   B O   1 
ATOM   4455 C CB  . LYS   B 1 173 ? -23.37400 26.47300  16.64100  1.000 48.01891  ? 149  LYS   B CB  1 
ATOM   4456 C CG  . LYS   B 1 173 ? -24.03700 25.34900  17.42700  1.000 49.07492  ? 149  LYS   B CG  1 
ATOM   4457 C CD  . LYS   B 1 173 ? -25.31200 24.85800  16.76800  1.000 52.23947  ? 149  LYS   B CD  1 
ATOM   4458 C CE  . LYS   B 1 173 ? -25.74600 23.52400  17.35500  1.000 59.59748  ? 149  LYS   B CE  1 
ATOM   4459 N NZ  . LYS   B 1 173 ? -26.34300 23.67800  18.71300  1.000 76.15802  ? 149  LYS   B NZ  1 
ATOM   4460 N N   . ALA   B 1 174 ? -21.01600 28.00900  15.16300  1.000 45.07761  ? 150  ALA   B N   1 
ATOM   4461 C CA  . ALA   B 1 174 ? -20.52000 29.08100  14.30600  1.000 46.03913  ? 150  ALA   B CA  1 
ATOM   4462 C C   . ALA   B 1 174 ? -19.77500 28.53100  13.10100  1.000 40.12239  ? 150  ALA   B C   1 
ATOM   4463 O O   . ALA   B 1 174 ? -19.83000 29.12200  12.01900  1.000 39.93409  ? 150  ALA   B O   1 
ATOM   4464 C CB  . ALA   B 1 174 ? -19.61500 30.01900  15.10400  1.000 45.99730  ? 150  ALA   B CB  1 
ATOM   4465 N N   . ARG   B 1 175 ? -19.07700 27.40500  13.26800  1.000 41.90916  ? 151  ARG   B N   1 
ATOM   4466 C CA  . ARG   B 1 175 ? -18.40300 26.77300  12.13800  1.000 40.44211  ? 151  ARG   B CA  1 
ATOM   4467 C C   . ARG   B 1 175 ? -19.40400 26.32700  11.08100  1.000 45.45996  ? 151  ARG   B C   1 
ATOM   4468 O O   . ARG   B 1 175 ? -19.20800 26.56900  9.88400   1.000 50.40358  ? 151  ARG   B O   1 
ATOM   4469 C CB  . ARG   B 1 175 ? -17.56900 25.58400  12.61300  1.000 32.87176  ? 151  ARG   B CB  1 
ATOM   4470 C CG  . ARG   B 1 175 ? -16.39800 25.94100  13.50700  1.000 33.00029  ? 151  ARG   B CG  1 
ATOM   4471 C CD  . ARG   B 1 175 ? -15.55300 24.71000  13.76400  1.000 45.62467  ? 151  ARG   B CD  1 
ATOM   4472 N NE  . ARG   B 1 175 ? -14.90700 24.73500  15.07100  1.000 55.38884  ? 151  ARG   B NE  1 
ATOM   4473 C CZ  . ARG   B 1 175 ? -13.70200 25.23800  15.30200  1.000 63.78237  ? 151  ARG   B CZ  1 
ATOM   4474 N NH1 . ARG   B 1 175 ? -12.98300 25.78500  14.33300  1.000 60.10240  ? 151  ARG   B NH1 1 
ATOM   4475 N NH2 . ARG   B 1 175 ? -13.20400 25.18900  16.53600  1.000 55.87584  ? 151  ARG   B NH2 1 
ATOM   4476 N N   . VAL   B 1 176 ? -20.48600 25.66800  11.50800  1.000 41.40412  ? 152  VAL   B N   1 
ATOM   4477 C CA  . VAL   B 1 176 ? -21.49300 25.18900  10.56100  1.000 44.99136  ? 152  VAL   B CA  1 
ATOM   4478 C C   . VAL   B 1 176 ? -22.09100 26.35400  9.78000   1.000 44.04186  ? 152  VAL   B C   1 
ATOM   4479 O O   . VAL   B 1 176 ? -22.23200 26.29100  8.55300   1.000 42.38706  ? 152  VAL   B O   1 
ATOM   4480 C CB  . VAL   B 1 176 ? -22.58100 24.38100  11.28900  1.000 40.09669  ? 152  VAL   B CB  1 
ATOM   4481 C CG1 . VAL   B 1 176 ? -23.67700 23.98600  10.32000  1.000 39.78775  ? 152  VAL   B CG1 1 
ATOM   4482 C CG2 . VAL   B 1 176 ? -21.97500 23.14300  11.91600  1.000 41.04098  ? 152  VAL   B CG2 1 
ATOM   4483 N N   . ILE   B 1 177 ? -22.44400 27.43600  10.48000  1.000 40.83314  ? 153  ILE   B N   1 
ATOM   4484 C CA  . ILE   B 1 177 ? -22.99200 28.61500  9.81000   1.000 40.87567  ? 153  ILE   B CA  1 
ATOM   4485 C C   . ILE   B 1 177 ? -22.06700 29.06900  8.68800   1.000 41.36203  ? 153  ILE   B C   1 
ATOM   4486 O O   . ILE   B 1 177 ? -22.49900 29.27200  7.54600   1.000 45.00338  ? 153  ILE   B O   1 
ATOM   4487 C CB  . ILE   B 1 177 ? -23.23500 29.74200  10.82800  1.000 39.29150  ? 153  ILE   B CB  1 
ATOM   4488 C CG1 . ILE   B 1 177 ? -24.26300 29.29900  11.86400  1.000 35.42032  ? 153  ILE   B CG1 1 
ATOM   4489 C CG2 . ILE   B 1 177 ? -23.68700 31.00800  10.12300  1.000 37.19342  ? 153  ILE   B CG2 1 
ATOM   4490 C CD1 . ILE   B 1 177 ? -24.42600 30.27600  12.98600  1.000 38.51610  ? 153  ILE   B CD1 1 
ATOM   4491 N N   . ILE   B 1 178 ? -20.77600 29.22100  8.99600   1.000 37.82588  ? 154  ILE   B N   1 
ATOM   4492 C CA  . ILE   B 1 178 ? -19.80600 29.61900  7.97900   1.000 38.52992  ? 154  ILE   B CA  1 
ATOM   4493 C C   . ILE   B 1 178 ? -19.74700 28.59400  6.85600   1.000 44.32765  ? 154  ILE   B C   1 
ATOM   4494 O O   . ILE   B 1 178 ? -19.59700 28.94800  5.67900   1.000 41.18162  ? 154  ILE   B O   1 
ATOM   4495 C CB  . ILE   B 1 178 ? -18.42000 29.83400  8.61200   1.000 37.76965  ? 154  ILE   B CB  1 
ATOM   4496 C CG1 . ILE   B 1 178 ? -18.50600 30.81900  9.77600   1.000 37.65435  ? 154  ILE   B CG1 1 
ATOM   4497 C CG2 . ILE   B 1 178 ? -17.42700 30.29100  7.56100   1.000 38.45052  ? 154  ILE   B CG2 1 
ATOM   4498 C CD1 . ILE   B 1 178 ? -17.30400 30.78500  10.68600  1.000 36.95792  ? 154  ILE   B CD1 1 
ATOM   4499 N N   . LEU   B 1 179 ? -19.85700 27.30900  7.19600   1.000 44.58429  ? 155  LEU   B N   1 
ATOM   4500 C CA  . LEU   B 1 179 ? -19.82100 26.27900  6.16400   1.000 39.06696  ? 155  LEU   B CA  1 
ATOM   4501 C C   . LEU   B 1 179 ? -20.99500 26.42500  5.20400   1.000 45.50115  ? 155  LEU   B C   1 
ATOM   4502 O O   . LEU   B 1 179 ? -20.83000 26.28000  3.98800   1.000 50.01156  ? 155  LEU   B O   1 
ATOM   4503 C CB  . LEU   B 1 179 ? -19.81100 24.89400  6.80800   1.000 44.51382  ? 155  LEU   B CB  1 
ATOM   4504 C CG  . LEU   B 1 179 ? -19.58500 23.71500  5.86100   1.000 48.40347  ? 155  LEU   B CG  1 
ATOM   4505 C CD1 . LEU   B 1 179 ? -18.19200 23.78100  5.26400   1.000 46.30063  ? 155  LEU   B CD1 1 
ATOM   4506 C CD2 . LEU   B 1 179 ? -19.80000 22.39500  6.58800   1.000 54.39286  ? 155  LEU   B CD2 1 
ATOM   4507 N N   . MET   B 1 180 ? -22.18300 26.74100  5.72800   1.000 45.85980  ? 156  MET   B N   1 
ATOM   4508 C CA  . MET   B 1 180 ? -23.34900 26.90600  4.86400   1.000 43.73325  ? 156  MET   B CA  1 
ATOM   4509 C C   . MET   B 1 180 ? -23.30300 28.21500  4.08700   1.000 38.98331  ? 156  MET   B C   1 
ATOM   4510 O O   . MET   B 1 180 ? -23.75600 28.26600  2.94000   1.000 44.00477  ? 156  MET   B O   1 
ATOM   4511 C CB  . MET   B 1 180 ? -24.63600 26.83800  5.67900   1.000 43.22795  ? 156  MET   B CB  1 
ATOM   4512 C CG  . MET   B 1 180 ? -24.63700 25.79200  6.76100   1.000 52.85596  ? 156  MET   B CG  1 
ATOM   4513 S SD  . MET   B 1 180 ? -26.30000 25.50900  7.38200   1.000 68.13129  ? 156  MET   B SD  1 
ATOM   4514 C CE  . MET   B 1 180 ? -26.76100 27.17100  7.86500   1.000 61.15157  ? 156  MET   B CE  1 
ATOM   4515 N N   . VAL   B 1 181 ? -22.78800 29.28500  4.69800   1.000 31.56078  ? 157  VAL   B N   1 
ATOM   4516 C CA  . VAL   B 1 181 ? -22.66100 30.55100  3.98300   1.000 32.26116  ? 157  VAL   B CA  1 
ATOM   4517 C C   . VAL   B 1 181 ? -21.83900 30.36100  2.71700   1.000 41.88530  ? 157  VAL   B C   1 
ATOM   4518 O O   . VAL   B 1 181 ? -22.20400 30.84900  1.64000   1.000 44.07372  ? 157  VAL   B O   1 
ATOM   4519 C CB  . VAL   B 1 181 ? -22.05000 31.62800  4.89800   1.000 33.38453  ? 157  VAL   B CB  1 
ATOM   4520 C CG1 . VAL   B 1 181 ? -21.59900 32.83100  4.08300   1.000 29.23001  ? 157  VAL   B CG1 1 
ATOM   4521 C CG2 . VAL   B 1 181 ? -23.05600 32.04500  5.96300   1.000 33.26646  ? 157  VAL   B CG2 1 
ATOM   4522 N N   . TRP   B 1 182 ? -20.73100 29.62200  2.81800   1.000 43.09546  ? 158  TRP   B N   1 
ATOM   4523 C CA  . TRP   B 1 182 ? -19.92900 29.33500  1.63400   1.000 38.01471  ? 158  TRP   B CA  1 
ATOM   4524 C C   . TRP   B 1 182 ? -20.63300 28.34100  0.71800   1.000 38.84850  ? 158  TRP   B C   1 
ATOM   4525 O O   . TRP   B 1 182 ? -20.56800 28.46500  -0.50900  1.000 37.06298  ? 158  TRP   B O   1 
ATOM   4526 C CB  . TRP   B 1 182 ? -18.55300 28.81400  2.04700   1.000 29.05604  ? 158  TRP   B CB  1 
ATOM   4527 C CG  . TRP   B 1 182 ? -17.64700 29.89400  2.54400   1.000 30.60966  ? 158  TRP   B CG  1 
ATOM   4528 C CD1 . TRP   B 1 182 ? -17.47100 30.28500  3.84000   1.000 39.95756  ? 158  TRP   B CD1 1 
ATOM   4529 C CD2 . TRP   B 1 182 ? -16.80500 30.74200  1.75300   1.000 35.08676  ? 158  TRP   B CD2 1 
ATOM   4530 N NE1 . TRP   B 1 182 ? -16.56500 31.31700  3.90700   1.000 39.11745  ? 158  TRP   B NE1 1 
ATOM   4531 C CE2 . TRP   B 1 182 ? -16.14200 31.61700  2.63900   1.000 34.42785  ? 158  TRP   B CE2 1 
ATOM   4532 C CE3 . TRP   B 1 182 ? -16.54200 30.84100  0.38300   1.000 29.16052  ? 158  TRP   B CE3 1 
ATOM   4533 C CZ2 . TRP   B 1 182 ? -15.23600 32.57800  2.19900   1.000 32.66822  ? 158  TRP   B CZ2 1 
ATOM   4534 C CZ3 . TRP   B 1 182 ? -15.64600 31.79400  -0.04900  1.000 30.91802  ? 158  TRP   B CZ3 1 
ATOM   4535 C CH2 . TRP   B 1 182 ? -15.00200 32.65200  0.85600   1.000 39.84971  ? 158  TRP   B CH2 1 
ATOM   4536 N N   . ILE   B 1 183 ? -21.32600 27.35800  1.29700   1.000 42.30392  ? 159  ILE   B N   1 
ATOM   4537 C CA  . ILE   B 1 183 ? -22.03000 26.36700  0.49000   1.000 44.71366  ? 159  ILE   B CA  1 
ATOM   4538 C C   . ILE   B 1 183 ? -23.19800 26.99300  -0.26800  1.000 41.46222  ? 159  ILE   B C   1 
ATOM   4539 O O   . ILE   B 1 183 ? -23.51000 26.57000  -1.38600  1.000 43.29632  ? 159  ILE   B O   1 
ATOM   4540 C CB  . ILE   B 1 183 ? -22.47400 25.18800  1.38100   1.000 41.98547  ? 159  ILE   B CB  1 
ATOM   4541 C CG1 . ILE   B 1 183 ? -21.28800 24.25800  1.65200   1.000 47.36988  ? 159  ILE   B CG1 1 
ATOM   4542 C CG2 . ILE   B 1 183 ? -23.61200 24.40300  0.75300   1.000 35.68446  ? 159  ILE   B CG2 1 
ATOM   4543 C CD1 . ILE   B 1 183 ? -21.57600 23.18900  2.68400   1.000 53.49565  ? 159  ILE   B CD1 1 
ATOM   4544 N N   . VAL   B 1 184 ? -23.84300 28.01600  0.29100   1.000 39.19313  ? 160  VAL   B N   1 
ATOM   4545 C CA  . VAL   B 1 184 ? -25.00400 28.61500  -0.36400  1.000 41.10562  ? 160  VAL   B CA  1 
ATOM   4546 C C   . VAL   B 1 184 ? -24.55500 29.65400  -1.38200  1.000 45.33649  ? 160  VAL   B C   1 
ATOM   4547 O O   . VAL   B 1 184 ? -24.89400 29.56300  -2.56900  1.000 44.74657  ? 160  VAL   B O   1 
ATOM   4548 C CB  . VAL   B 1 184 ? -25.96800 29.23800  0.65800   1.000 41.80664  ? 160  VAL   B CB  1 
ATOM   4549 C CG1 . VAL   B 1 184 ? -26.92700 30.19600  -0.03800  1.000 34.39107  ? 160  VAL   B CG1 1 
ATOM   4550 C CG2 . VAL   B 1 184 ? -26.72700 28.14600  1.39200   1.000 40.13770  ? 160  VAL   B CG2 1 
ATOM   4551 N N   . SER   B 1 185 ? -23.79400 30.65300  -0.92800  1.000 45.23163  ? 161  SER   B N   1 
ATOM   4552 C CA  . SER   B 1 185 ? -23.30200 31.67200  -1.84600  1.000 46.51899  ? 161  SER   B CA  1 
ATOM   4553 C C   . SER   B 1 185 ? -22.45700 31.07000  -2.96100  1.000 42.25771  ? 161  SER   B C   1 
ATOM   4554 O O   . SER   B 1 185 ? -22.32900 31.68100  -4.02400  1.000 49.05687  ? 161  SER   B O   1 
ATOM   4555 C CB  . SER   B 1 185 ? -22.50400 32.73500  -1.08500  1.000 45.50783  ? 161  SER   B CB  1 
ATOM   4556 O OG  . SER   B 1 185 ? -21.59700 32.14400  -0.17300  1.000 47.77087  ? 161  SER   B OG  1 
ATOM   4557 N N   . GLY   B 1 186 ? -21.88800 29.88300  -2.74700  1.000 41.86538  ? 162  GLY   B N   1 
ATOM   4558 C CA  . GLY   B 1 186 ? -21.23400 29.18400  -3.83900  1.000 44.77302  ? 162  GLY   B CA  1 
ATOM   4559 C C   . GLY   B 1 186 ? -22.22000 28.67300  -4.87100  1.000 45.64261  ? 162  GLY   B C   1 
ATOM   4560 O O   . GLY   B 1 186 ? -21.97200 28.76200  -6.07800  1.000 43.69459  ? 162  GLY   B O   1 
ATOM   4561 N N   . LEU   B 1 187 ? -23.35400 28.13300  -4.41400  1.000 46.95888  ? 163  LEU   B N   1 
ATOM   4562 C CA  . LEU   B 1 187 ? -24.39200 27.69000  -5.33900  1.000 42.13752  ? 163  LEU   B CA  1 
ATOM   4563 C C   . LEU   B 1 187 ? -24.97000 28.86500  -6.11800  1.000 42.10238  ? 163  LEU   B C   1 
ATOM   4564 O O   . LEU   B 1 187 ? -25.06900 28.82000  -7.34900  1.000 44.63349  ? 163  LEU   B O   1 
ATOM   4565 C CB  . LEU   B 1 187 ? -25.49800 26.95700  -4.58000  1.000 40.84921  ? 163  LEU   B CB  1 
ATOM   4566 C CG  . LEU   B 1 187 ? -25.11300 25.65200  -3.88700  1.000 40.65745  ? 163  LEU   B CG  1 
ATOM   4567 C CD1 . LEU   B 1 187 ? -26.33300 24.97900  -3.27800  1.000 33.74161  ? 163  LEU   B CD1 1 
ATOM   4568 C CD2 . LEU   B 1 187 ? -24.41300 24.71900  -4.85600  1.000 37.41611  ? 163  LEU   B CD2 1 
ATOM   4569 N N   . THR   B 1 188 ? -25.35000 29.93600  -5.41900  1.000 38.97761  ? 164  THR   B N   1 
ATOM   4570 C CA  . THR   B 1 188 ? -25.96200 31.07400  -6.09200  1.000 41.69381  ? 164  THR   B CA  1 
ATOM   4571 C C   . THR   B 1 188 ? -24.96300 31.91400  -6.88200  1.000 45.95568  ? 164  THR   B C   1 
ATOM   4572 O O   . THR   B 1 188 ? -25.38200 32.84600  -7.57700  1.000 46.48001  ? 164  THR   B O   1 
ATOM   4573 C CB  . THR   B 1 188 ? -26.68800 31.95800  -5.07600  1.000 41.16082  ? 164  THR   B CB  1 
ATOM   4574 O OG1 . THR   B 1 188 ? -25.73600 32.72000  -4.32600  1.000 47.73012  ? 164  THR   B OG1 1 
ATOM   4575 C CG2 . THR   B 1 188 ? -27.49300 31.10000  -4.12300  1.000 36.06928  ? 164  THR   B CG2 1 
ATOM   4576 N N   . SER   B 1 189 ? -23.66500 31.61600  -6.80600  1.000 44.57388  ? 165  SER   B N   1 
ATOM   4577 C CA  . SER   B 1 189 ? -22.67700 32.36500  -7.57100  1.000 50.23616  ? 165  SER   B CA  1 
ATOM   4578 C C   . SER   B 1 189 ? -22.02800 31.56700  -8.68700  1.000 45.00240  ? 165  SER   B C   1 
ATOM   4579 O O   . SER   B 1 189 ? -21.66700 32.15100  -9.70900  1.000 48.74817  ? 165  SER   B O   1 
ATOM   4580 C CB  . SER   B 1 189 ? -21.57500 32.90400  -6.65200  1.000 46.41814  ? 165  SER   B CB  1 
ATOM   4581 O OG  . SER   B 1 189 ? -22.08600 33.90200  -5.78500  1.000 48.00968  ? 165  SER   B OG  1 
ATOM   4582 N N   . PHE   B 1 190 ? -21.86400 30.25600  -8.52200  1.000 44.54904  ? 166  PHE   B N   1 
ATOM   4583 C CA  . PHE   B 1 190 ? -21.26500 29.43500  -9.56800  1.000 43.21113  ? 166  PHE   B CA  1 
ATOM   4584 C C   . PHE   B 1 190 ? -22.30700 28.89700  -10.54000 1.000 47.19773  ? 166  PHE   B C   1 
ATOM   4585 O O   . PHE   B 1 190 ? -22.14700 29.03500  -11.75700 1.000 56.10196  ? 166  PHE   B O   1 
ATOM   4586 C CB  . PHE   B 1 190 ? -20.47600 28.28000  -8.94500  1.000 43.18731  ? 166  PHE   B CB  1 
ATOM   4587 C CG  . PHE   B 1 190 ? -19.01700 28.57900  -8.75200  1.000 47.72574  ? 166  PHE   B CG  1 
ATOM   4588 C CD1 . PHE   B 1 190 ? -18.59800 29.44600  -7.75800  1.000 47.85216  ? 166  PHE   B CD1 1 
ATOM   4589 C CD2 . PHE   B 1 190 ? -18.06300 27.96800  -9.54400  1.000 44.29699  ? 166  PHE   B CD2 1 
ATOM   4590 C CE1 . PHE   B 1 190 ? -17.26000 29.71800  -7.57700  1.000 39.46857  ? 166  PHE   B CE1 1 
ATOM   4591 C CE2 . PHE   B 1 190 ? -16.72300 28.23200  -9.36200  1.000 44.41753  ? 166  PHE   B CE2 1 
ATOM   4592 C CZ  . PHE   B 1 190 ? -16.32100 29.10800  -8.37900  1.000 43.46365  ? 166  PHE   B CZ  1 
ATOM   4593 N N   . LEU   B 1 191 ? -23.37400 28.28600  -10.01700 1.000 43.34250  ? 167  LEU   B N   1 
ATOM   4594 C CA  . LEU   B 1 191 ? -24.42500 27.72500  -10.86500 1.000 40.00508  ? 167  LEU   B CA  1 
ATOM   4595 C C   . LEU   B 1 191 ? -24.94400 28.70600  -11.90900 1.000 49.37946  ? 167  LEU   B C   1 
ATOM   4596 O O   . LEU   B 1 191 ? -24.98500 28.33700  -13.09100 1.000 49.43738  ? 167  LEU   B O   1 
ATOM   4597 C CB  . LEU   B 1 191 ? -25.56900 27.19500  -9.99000  1.000 37.82139  ? 167  LEU   B CB  1 
ATOM   4598 C CG  . LEU   B 1 191 ? -25.30800 25.85100  -9.31100  1.000 44.10429  ? 167  LEU   B CG  1 
ATOM   4599 C CD1 . LEU   B 1 191 ? -26.45100 25.48000  -8.38500  1.000 43.67211  ? 167  LEU   B CD1 1 
ATOM   4600 C CD2 . LEU   B 1 191 ? -25.08100 24.76800  -10.34800 1.000 39.29543  ? 167  LEU   B CD2 1 
ATOM   4601 N N   . PRO   B 1 192 ? -25.32600 29.94400  -11.57800 1.000 49.51438  ? 168  PRO   B N   1 
ATOM   4602 C CA  . PRO   B 1 192 ? -25.74600 30.86000  -12.65300 1.000 44.65288  ? 168  PRO   B CA  1 
ATOM   4603 C C   . PRO   B 1 192 ? -24.66800 31.10000  -13.70000 1.000 49.92307  ? 168  PRO   B C   1 
ATOM   4604 O O   . PRO   B 1 192 ? -24.99700 31.34900  -14.86700 1.000 55.73764  ? 168  PRO   B O   1 
ATOM   4605 C CB  . PRO   B 1 192 ? -26.10300 32.14800  -11.90100 1.000 44.27465  ? 168  PRO   B CB  1 
ATOM   4606 C CG  . PRO   B 1 192 ? -26.40600 31.70700  -10.51800 1.000 52.23129  ? 168  PRO   B CG  1 
ATOM   4607 C CD  . PRO   B 1 192 ? -25.47900 30.56600  -10.25000 1.000 45.62596  ? 168  PRO   B CD  1 
ATOM   4608 N N   . ILE   B 1 193 ? -23.39400 31.01200  -13.33300 1.000 52.29720  ? 169  ILE   B N   1 
ATOM   4609 C CA  . ILE   B 1 193 ? -22.31800 31.28000  -14.28400 1.000 53.72375  ? 169  ILE   B CA  1 
ATOM   4610 C C   . ILE   B 1 193 ? -21.88500 30.01300  -15.01100 1.000 54.98736  ? 169  ILE   B C   1 
ATOM   4611 O O   . ILE   B 1 193 ? -21.75600 30.00300  -16.23900 1.000 55.88273  ? 169  ILE   B O   1 
ATOM   4612 C CB  . ILE   B 1 193 ? -21.13500 31.95800  -13.56500 1.000 46.40574  ? 169  ILE   B CB  1 
ATOM   4613 C CG1 . ILE   B 1 193 ? -21.52000 33.38600  -13.17900 1.000 47.23178  ? 169  ILE   B CG1 1 
ATOM   4614 C CG2 . ILE   B 1 193 ? -19.89700 31.95100  -14.44900 1.000 54.19457  ? 169  ILE   B CG2 1 
ATOM   4615 C CD1 . ILE   B 1 193 ? -20.41900 34.15000  -12.49600 1.000 44.62142  ? 169  ILE   B CD1 1 
ATOM   4616 N N   . GLN   B 1 194 ? -21.66700 28.91900  -14.27900 1.000 46.61282  ? 170  GLN   B N   1 
ATOM   4617 C CA  . GLN   B 1 194 ? -21.29500 27.66800  -14.93000 1.000 49.04247  ? 170  GLN   B CA  1 
ATOM   4618 C C   . GLN   B 1 194 ? -22.41900 27.09700  -15.79200 1.000 56.33046  ? 170  GLN   B C   1 
ATOM   4619 O O   . GLN   B 1 194 ? -22.15200 26.23700  -16.63800 1.000 56.53172  ? 170  GLN   B O   1 
ATOM   4620 C CB  . GLN   B 1 194 ? -20.86200 26.64200  -13.88100 1.000 39.74152  ? 170  GLN   B CB  1 
ATOM   4621 C CG  . GLN   B 1 194 ? -19.78200 27.15100  -12.94200 1.000 46.13844  ? 170  GLN   B CG  1 
ATOM   4622 C CD  . GLN   B 1 194 ? -18.42700 27.27400  -13.61500 1.000 49.56718  ? 170  GLN   B CD  1 
ATOM   4623 O OE1 . GLN   B 1 194 ? -17.91300 26.31100  -14.18900 1.000 55.55010  ? 170  GLN   B OE1 1 
ATOM   4624 N NE2 . GLN   B 1 194 ? -17.84300 28.46800  -13.55600 1.000 48.65008  ? 170  GLN   B NE2 1 
ATOM   4625 N N   . MET   B 1 195 ? -23.66000 27.55100  -15.60400 1.000 54.14447  ? 171  MET   B N   1 
ATOM   4626 C CA  . MET   B 1 195 ? -24.79800 27.07600  -16.38000 1.000 46.28238  ? 171  MET   B CA  1 
ATOM   4627 C C   . MET   B 1 195 ? -25.24000 28.06400  -17.45600 1.000 52.58541  ? 171  MET   B C   1 
ATOM   4628 O O   . MET   B 1 195 ? -26.24700 27.81100  -18.12700 1.000 57.14324  ? 171  MET   B O   1 
ATOM   4629 C CB  . MET   B 1 195 ? -25.98500 26.77600  -15.45500 1.000 48.92980  ? 171  MET   B CB  1 
ATOM   4630 C CG  . MET   B 1 195 ? -25.74600 25.68900  -14.41800 1.000 45.03084  ? 171  MET   B CG  1 
ATOM   4631 S SD  . MET   B 1 195 ? -25.56700 24.04500  -15.11000 1.000 48.83889  ? 171  MET   B SD  1 
ATOM   4632 C CE  . MET   B 1 195 ? -27.29200 23.59100  -15.29000 1.000 58.56511  ? 171  MET   B CE  1 
ATOM   4633 N N   . HIS   B 1 196 ? -24.53600 29.18800  -17.61100 1.000 52.28153  ? 172  HIS   B N   1 
ATOM   4634 C CA  . HIS   B 1 196 ? -24.70400 30.19000  -18.67600 1.000 58.19456  ? 172  HIS   B CA  1 
ATOM   4635 C C   . HIS   B 1 196 ? -25.93100 31.07500  -18.49400 1.000 51.08701  ? 172  HIS   B C   1 
ATOM   4636 O O   . HIS   B 1 196 ? -26.34000 31.73500  -19.46100 1.000 53.58330  ? 172  HIS   B O   1 
ATOM   4637 C CB  . HIS   B 1 196 ? -24.79200 29.55300  -20.06800 1.000 58.97476  ? 172  HIS   B CB  1 
ATOM   4638 C CG  . HIS   B 1 196 ? -23.54500 28.83700  -20.48800 1.000 60.65032  ? 172  HIS   B CG  1 
ATOM   4639 N ND1 . HIS   B 1 196 ? -22.29700 29.15400  -19.99600 1.000 60.69470  ? 172  HIS   B ND1 1 
ATOM   4640 C CD2 . HIS   B 1 196 ? -23.36400 27.78500  -21.32200 1.000 61.50538  ? 172  HIS   B CD2 1 
ATOM   4641 C CE1 . HIS   B 1 196 ? -21.39900 28.34300  -20.52700 1.000 61.45320  ? 172  HIS   B CE1 1 
ATOM   4642 N NE2 . HIS   B 1 196 ? -22.02100 27.50200  -21.33400 1.000 57.40473  ? 172  HIS   B NE2 1 
ATOM   4643 N N   . TRP   B 1 197 ? -26.53100 31.12200  -17.30300 1.000 48.70046  ? 173  TRP   B N   1 
ATOM   4644 C CA  . TRP   B 1 197 ? -27.74700 31.91300  -17.12600 1.000 46.53487  ? 173  TRP   B CA  1 
ATOM   4645 C C   . TRP   B 1 197 ? -27.48900 33.40000  -17.31600 1.000 45.23579  ? 173  TRP   B C   1 
ATOM   4646 O O   . TRP   B 1 197 ? -28.38200 34.13200  -17.75300 1.000 50.78713  ? 173  TRP   B O   1 
ATOM   4647 C CB  . TRP   B 1 197 ? -28.35200 31.65700  -15.74200 1.000 38.91337  ? 173  TRP   B CB  1 
ATOM   4648 C CG  . TRP   B 1 197 ? -28.67100 30.21600  -15.46600 1.000 41.81009  ? 173  TRP   B CG  1 
ATOM   4649 C CD1 . TRP   B 1 197 ? -28.59600 29.17800  -16.34600 1.000 46.80790  ? 173  TRP   B CD1 1 
ATOM   4650 C CD2 . TRP   B 1 197 ? -29.12800 29.65700  -14.22500 1.000 46.25104  ? 173  TRP   B CD2 1 
ATOM   4651 N NE1 . TRP   B 1 197 ? -28.97200 28.00800  -15.73300 1.000 49.45845  ? 173  TRP   B NE1 1 
ATOM   4652 C CE2 . TRP   B 1 197 ? -29.30300 28.27400  -14.43100 1.000 45.98218  ? 173  TRP   B CE2 1 
ATOM   4653 C CE3 . TRP   B 1 197 ? -29.40600 30.19100  -12.96200 1.000 47.64101  ? 173  TRP   B CE3 1 
ATOM   4654 C CZ2 . TRP   B 1 197 ? -29.74300 27.41800  -13.42300 1.000 43.96196  ? 173  TRP   B CZ2 1 
ATOM   4655 C CZ3 . TRP   B 1 197 ? -29.84100 29.33700  -11.96200 1.000 40.55615  ? 173  TRP   B CZ3 1 
ATOM   4656 C CH2 . TRP   B 1 197 ? -30.00500 27.96700  -12.19900 1.000 38.09991  ? 173  TRP   B CH2 1 
ATOM   4657 N N   . TYR   B 1 198 ? -26.28200 33.86700  -16.99400 1.000 46.54314  ? 174  TYR   B N   1 
ATOM   4658 C CA  . TYR   B 1 198 ? -25.99700 35.29200  -17.10800 1.000 51.65276  ? 174  TYR   B CA  1 
ATOM   4659 C C   . TYR   B 1 198 ? -25.99600 35.75200  -18.55700 1.000 52.98251  ? 174  TYR   B C   1 
ATOM   4660 O O   . TYR   B 1 198 ? -26.27500 36.92300  -18.83300 1.000 52.30473  ? 174  TYR   B O   1 
ATOM   4661 C CB  . TYR   B 1 198 ? -24.64400 35.62500  -16.47000 1.000 54.47931  ? 174  TYR   B CB  1 
ATOM   4662 C CG  . TYR   B 1 198 ? -23.44100 35.04900  -17.19700 1.000 57.29925  ? 174  TYR   B CG  1 
ATOM   4663 C CD1 . TYR   B 1 198 ? -23.19300 33.68000  -17.21000 1.000 57.13915  ? 174  TYR   B CD1 1 
ATOM   4664 C CD2 . TYR   B 1 198 ? -22.55800 35.87900  -17.87600 1.000 50.92134  ? 174  TYR   B CD2 1 
ATOM   4665 C CE1 . TYR   B 1 198 ? -22.09600 33.15700  -17.87600 1.000 52.10400  ? 174  TYR   B CE1 1 
ATOM   4666 C CE2 . TYR   B 1 198 ? -21.46200 35.36500  -18.54300 1.000 48.34161  ? 174  TYR   B CE2 1 
ATOM   4667 C CZ  . TYR   B 1 198 ? -21.23500 34.00500  -18.53900 1.000 49.36567  ? 174  TYR   B CZ  1 
ATOM   4668 O OH  . TYR   B 1 198 ? -20.14100 33.49800  -19.20600 1.000 51.69520  ? 174  TYR   B OH  1 
ATOM   4669 N N   . ARG   B 1 199 ? -25.73200 34.84000  -19.48600 1.000 54.98723  ? 175  ARG   B N   1 
ATOM   4670 C CA  . ARG   B 1 199 ? -25.20800 35.21900  -20.79000 1.000 58.02751  ? 175  ARG   B CA  1 
ATOM   4671 C C   . ARG   B 1 199 ? -26.21100 36.02600  -21.60600 1.000 58.16429  ? 175  ARG   B C   1 
ATOM   4672 O O   . ARG   B 1 199 ? -27.42200 35.79500  -21.54700 1.000 58.88305  ? 175  ARG   B O   1 
ATOM   4673 C CB  . ARG   B 1 199 ? -24.78500 33.97000  -21.55500 1.000 57.63048  ? 175  ARG   B CB  1 
ATOM   4674 C CG  . ARG   B 1 199 ? -23.36700 33.57400  -21.22500 1.000 59.12769  ? 175  ARG   B CG  1 
ATOM   4675 C CD  . ARG   B 1 199 ? -23.02500 32.18200  -21.67200 1.000 56.72478  ? 175  ARG   B CD  1 
ATOM   4676 N NE  . ARG   B 1 199 ? -21.58000 32.04800  -21.78700 1.000 62.52973  ? 175  ARG   B NE  1 
ATOM   4677 C CZ  . ARG   B 1 199 ? -20.96400 31.06100  -22.42000 1.000 69.25759  ? 175  ARG   B CZ  1 
ATOM   4678 N NH1 . ARG   B 1 199 ? -21.64200 30.09400  -23.01800 1.000 73.85533  ? 175  ARG   B NH1 1 
ATOM   4679 N NH2 . ARG   B 1 199 ? -19.63400 31.04100  -22.45200 1.000 69.87074  ? 175  ARG   B NH2 1 
ATOM   4680 N N   . ALA   B 1 200 ? -25.68800 36.98500  -22.37000 1.000 60.25978  ? 176  ALA   B N   1 
ATOM   4681 C CA  . ALA   B 1 200 ? -26.48100 37.82800  -23.24700 1.000 61.51674  ? 176  ALA   B CA  1 
ATOM   4682 C C   . ALA   B 1 200 ? -26.61400 37.18300  -24.62600 1.000 59.72159  ? 176  ALA   B C   1 
ATOM   4683 O O   . ALA   B 1 200 ? -26.03400 36.13000  -24.90800 1.000 49.33359  ? 176  ALA   B O   1 
ATOM   4684 C CB  . ALA   B 1 200 ? -25.85800 39.21800  -23.35500 1.000 58.77989  ? 176  ALA   B CB  1 
ATOM   4685 N N   . THR   B 1 201 ? -27.38700 37.82800  -25.50300 1.000 63.92685  ? 177  THR   B N   1 
ATOM   4686 C CA  . THR   B 1 201 ? -27.61500 37.31900  -26.84900 1.000 66.68448  ? 177  THR   B CA  1 
ATOM   4687 C C   . THR   B 1 201 ? -27.24500 38.29800  -27.95700 1.000 69.10898  ? 177  THR   B C   1 
ATOM   4688 O O   . THR   B 1 201 ? -27.49900 37.99500  -29.12900 1.000 70.99895  ? 177  THR   B O   1 
ATOM   4689 C CB  . THR   B 1 201 ? -29.08100 36.90300  -27.03500 1.000 54.82688  ? 177  THR   B CB  1 
ATOM   4690 O OG1 . THR   B 1 201 ? -29.93100 38.04000  -26.84100 1.000 57.37569  ? 177  THR   B OG1 1 
ATOM   4691 C CG2 . THR   B 1 201 ? -29.45600 35.80400  -26.04800 1.000 59.75786  ? 177  THR   B CG2 1 
ATOM   4692 N N   . HIS   B 1 202 ? -26.67400 39.45700  -27.64100 1.000 67.66547  ? 178  HIS   B N   1 
ATOM   4693 C CA  . HIS   B 1 202 ? -26.18800 40.33700  -28.69200 1.000 63.17818  ? 178  HIS   B CA  1 
ATOM   4694 C C   . HIS   B 1 202 ? -24.88200 39.78600  -29.25000 1.000 68.98415  ? 178  HIS   B C   1 
ATOM   4695 O O   . HIS   B 1 202 ? -24.03300 39.29100  -28.50300 1.000 69.11386  ? 178  HIS   B O   1 
ATOM   4696 C CB  . HIS   B 1 202 ? -26.00800 41.77300  -28.18300 1.000 62.16168  ? 178  HIS   B CB  1 
ATOM   4697 C CG  . HIS   B 1 202 ? -25.22300 41.88700  -26.91200 1.000 71.71240  ? 178  HIS   B CG  1 
ATOM   4698 N ND1 . HIS   B 1 202 ? -25.82100 41.99600  -25.67400 1.000 75.88127  ? 178  HIS   B ND1 1 
ATOM   4699 C CD2 . HIS   B 1 202 ? -23.88800 41.93900  -26.68900 1.000 71.32641  ? 178  HIS   B CD2 1 
ATOM   4700 C CE1 . HIS   B 1 202 ? -24.88900 42.09800  -24.74300 1.000 70.28344  ? 178  HIS   B CE1 1 
ATOM   4701 N NE2 . HIS   B 1 202 ? -23.70700 42.06200  -25.33200 1.000 74.02318  ? 178  HIS   B NE2 1 
ATOM   4702 N N   . GLN   B 1 203 ? -24.74200 39.85300  -30.57900 1.000 72.71805  ? 179  GLN   B N   1 
ATOM   4703 C CA  . GLN   B 1 203 ? -23.60600 39.22900  -31.25600 1.000 72.99788  ? 179  GLN   B CA  1 
ATOM   4704 C C   . GLN   B 1 203 ? -22.27900 39.66700  -30.64800 1.000 68.72300  ? 179  GLN   B C   1 
ATOM   4705 O O   . GLN   B 1 203 ? -21.34200 38.86600  -30.54400 1.000 68.83848  ? 179  GLN   B O   1 
ATOM   4706 C CB  . GLN   B 1 203 ? -23.65000 39.54300  -32.75600 1.000 76.29633  ? 179  GLN   B CB  1 
ATOM   4707 C CG  . GLN   B 1 203 ? -22.66700 38.74200  -33.62000 1.000 69.65586  ? 179  GLN   B CG  1 
ATOM   4708 C CD  . GLN   B 1 203 ? -23.22800 37.41800  -34.12000 1.000 75.37768  ? 179  GLN   B CD  1 
ATOM   4709 O OE1 . GLN   B 1 203 ? -22.47400 36.52500  -34.51600 1.000 70.44805  ? 179  GLN   B OE1 1 
ATOM   4710 N NE2 . GLN   B 1 203 ? -24.54900 37.27800  -34.08700 1.000 78.72669  ? 179  GLN   B NE2 1 
ATOM   4711 N N   . GLU   B 1 204 ? -22.18800 40.93000  -30.21700 1.000 64.48632  ? 180  GLU   B N   1 
ATOM   4712 C CA  . GLU   B 1 204 ? -20.97000 41.40400  -29.56200 1.000 69.41974  ? 180  GLU   B CA  1 
ATOM   4713 C C   . GLU   B 1 204 ? -20.61900 40.55300  -28.34400 1.000 68.12310  ? 180  GLU   B C   1 
ATOM   4714 O O   . GLU   B 1 204 ? -19.43600 40.39400  -28.01500 1.000 62.85384  ? 180  GLU   B O   1 
ATOM   4715 C CB  . GLU   B 1 204 ? -21.13100 42.87200  -29.17100 1.000 63.51092  ? 180  GLU   B CB  1 
ATOM   4716 C CG  . GLU   B 1 204 ? -19.87500 43.51100  -28.62000 1.000 58.10113  ? 180  GLU   B CG  1 
ATOM   4717 C CD  . GLU   B 1 204 ? -19.98400 45.02100  -28.56000 1.000 73.50865  ? 180  GLU   B CD  1 
ATOM   4718 O OE1 . GLU   B 1 204 ? -21.04800 45.55500  -28.94600 1.000 70.50147  ? 180  GLU   B OE1 1 
ATOM   4719 O OE2 . GLU   B 1 204 ? -19.00800 45.67100  -28.13000 1.000 73.99689  ? 180  GLU   B OE2 1 
ATOM   4720 N N   . ALA   B 1 205 ? -21.62700 39.98900  -27.67300 1.000 62.94597  ? 181  ALA   B N   1 
ATOM   4721 C CA  . ALA   B 1 205 ? -21.36500 39.02900  -26.60800 1.000 61.02241  ? 181  ALA   B CA  1 
ATOM   4722 C C   . ALA   B 1 205 ? -21.12500 37.63100  -27.16100 1.000 62.03398  ? 181  ALA   B C   1 
ATOM   4723 O O   . ALA   B 1 205 ? -20.19800 36.94200  -26.72100 1.000 60.55311  ? 181  ALA   B O   1 
ATOM   4724 C CB  . ALA   B 1 205 ? -22.52500 39.00900  -25.61500 1.000 66.60659  ? 181  ALA   B CB  1 
ATOM   4725 N N   . ILE   B 1 206 ? -21.94400 37.19900  -28.12700 1.000 65.17526  ? 182  ILE   B N   1 
ATOM   4726 C CA  . ILE   B 1 206 ? -21.81700 35.84600  -28.66600 1.000 66.55203  ? 182  ILE   B CA  1 
ATOM   4727 C C   . ILE   B 1 206 ? -20.45100 35.63500  -29.30200 1.000 62.50730  ? 182  ILE   B C   1 
ATOM   4728 O O   . ILE   B 1 206 ? -19.93300 34.51100  -29.31800 1.000 58.93023  ? 182  ILE   B O   1 
ATOM   4729 C CB  . ILE   B 1 206 ? -22.94800 35.54700  -29.67000 1.000 64.54928  ? 182  ILE   B CB  1 
ATOM   4730 C CG1 . ILE   B 1 206 ? -24.27700 36.12000  -29.18600 1.000 62.58779  ? 182  ILE   B CG1 1 
ATOM   4731 C CG2 . ILE   B 1 206 ? -23.08200 34.04700  -29.89800 1.000 66.53280  ? 182  ILE   B CG2 1 
ATOM   4732 C CD1 . ILE   B 1 206 ? -25.28800 36.24900  -30.29100 1.000 70.50544  ? 182  ILE   B CD1 1 
ATOM   4733 N N   . ASN   B 1 207 ? -19.84500 36.69800  -29.83500 1.000 62.14292  ? 183  ASN   B N   1 
ATOM   4734 C CA  . ASN   B 1 207 ? -18.49100 36.57900  -30.36600 1.000 64.23701  ? 183  ASN   B CA  1 
ATOM   4735 C C   . ASN   B 1 207 ? -17.46300 36.53100  -29.24200 1.000 63.40867  ? 183  ASN   B C   1 
ATOM   4736 O O   . ASN   B 1 207 ? -16.57200 35.67400  -29.24300 1.000 57.28031  ? 183  ASN   B O   1 
ATOM   4737 C CB  . ASN   B 1 207 ? -18.18300 37.73700  -31.31700 1.000 64.23085  ? 183  ASN   B CB  1 
ATOM   4738 C CG  . ASN   B 1 207 ? -19.20500 37.86900  -32.42500 1.000 65.62787  ? 183  ASN   B CG  1 
ATOM   4739 O OD1 . ASN   B 1 207 ? -19.69600 38.96300  -32.69700 1.000 66.47618  ? 183  ASN   B OD1 1 
ATOM   4740 N ND2 . ASN   B 1 207 ? -19.55000 36.75000  -33.05600 1.000 58.99197  ? 183  ASN   B ND2 1 
ATOM   4741 N N   . CYS   B 1 208 ? -17.57100 37.44900  -28.27600 1.000 66.49707  ? 184  CYS   B N   1 
ATOM   4742 C CA  . CYS   B 1 208 ? -16.67000 37.42600  -27.12900 1.000 64.99963  ? 184  CYS   B CA  1 
ATOM   4743 C C   . CYS   B 1 208 ? -16.75500 36.09800  -26.39200 1.000 59.70044  ? 184  CYS   B C   1 
ATOM   4744 O O   . CYS   B 1 208 ? -15.74800 35.59700  -25.87600 1.000 62.38571  ? 184  CYS   B O   1 
ATOM   4745 C CB  . CYS   B 1 208 ? -16.98900 38.58300  -26.18100 1.000 68.28700  ? 184  CYS   B CB  1 
ATOM   4746 S SG  . CYS   B 1 208 ? -16.03700 38.56300  -24.63900 1.000 74.43253  ? 184  CYS   B SG  1 
ATOM   4747 N N   . TYR   B 1 209 ? -17.95200 35.51200  -26.33400 1.000 52.29213  ? 185  TYR   B N   1 
ATOM   4748 C CA  . TYR   B 1 209 ? -18.11300 34.19600  -25.73200 1.000 59.53776  ? 185  TYR   B CA  1 
ATOM   4749 C C   . TYR   B 1 209 ? -17.40500 33.11200  -26.53000 1.000 64.08062  ? 185  TYR   B C   1 
ATOM   4750 O O   . TYR   B 1 209 ? -17.04200 32.07600  -25.96100 1.000 66.15679  ? 185  TYR   B O   1 
ATOM   4751 C CB  . TYR   B 1 209 ? -19.59800 33.85900  -25.60600 1.000 61.22009  ? 185  TYR   B CB  1 
ATOM   4752 C CG  . TYR   B 1 209 ? -20.36600 34.75000  -24.65700 1.000 62.38962  ? 185  TYR   B CG  1 
ATOM   4753 C CD1 . TYR   B 1 209 ? -19.72300 35.71200  -23.88500 1.000 60.23045  ? 185  TYR   B CD1 1 
ATOM   4754 C CD2 . TYR   B 1 209 ? -21.74300 34.65000  -24.56200 1.000 63.03874  ? 185  TYR   B CD2 1 
ATOM   4755 C CE1 . TYR   B 1 209 ? -20.43400 36.52900  -23.03200 1.000 59.66168  ? 185  TYR   B CE1 1 
ATOM   4756 C CE2 . TYR   B 1 209 ? -22.45800 35.46700  -23.72300 1.000 58.84617  ? 185  TYR   B CE2 1 
ATOM   4757 C CZ  . TYR   B 1 209 ? -21.80400 36.39700  -22.95400 1.000 57.31225  ? 185  TYR   B CZ  1 
ATOM   4758 O OH  . TYR   B 1 209 ? -22.53600 37.19700  -22.11300 1.000 53.70793  ? 185  TYR   B OH  1 
ATOM   4759 N N   . ALA   B 1 210 ? -17.20000 33.33100  -27.83000 1.000 67.22582  ? 186  ALA   B N   1 
ATOM   4760 C CA  . ALA   B 1 210 ? -16.55900 32.35600  -28.70400 1.000 63.48068  ? 186  ALA   B CA  1 
ATOM   4761 C C   . ALA   B 1 210 ? -15.04000 32.47500  -28.69700 1.000 61.09068  ? 186  ALA   B C   1 
ATOM   4762 O O   . ALA   B 1 210 ? -14.34000 31.45700  -28.70600 1.000 59.99606  ? 186  ALA   B O   1 
ATOM   4763 C CB  . ALA   B 1 210 ? -17.08400 32.51100  -30.13200 1.000 59.52514  ? 186  ALA   B CB  1 
ATOM   4764 N N   . GLU   B 1 211 ? -14.51800 33.69900  -28.68300 1.000 54.99895  ? 187  GLU   B N   1 
ATOM   4765 C CA  . GLU   B 1 211 ? -13.07900 33.91200  -28.69400 1.000 60.25596  ? 187  GLU   B CA  1 
ATOM   4766 C C   . GLU   B 1 211 ? -12.51100 33.75900  -27.28400 1.000 70.52601  ? 187  GLU   B C   1 
ATOM   4767 O O   . GLU   B 1 211 ? -13.01200 34.36600  -26.33100 1.000 69.11205  ? 187  GLU   B O   1 
ATOM   4768 C CB  . GLU   B 1 211 ? -12.75600 35.29600  -29.25900 1.000 59.25756  ? 187  GLU   B CB  1 
ATOM   4769 C CG  . GLU   B 1 211 ? -11.27900 35.66000  -29.21100 1.000 64.86967  ? 187  GLU   B CG  1 
ATOM   4770 C CD  . GLU   B 1 211 ? -10.80000 36.40400  -30.45200 1.000 76.45399  ? 187  GLU   B CD  1 
ATOM   4771 O OE1 . GLU   B 1 211 ? -11.51600 36.39900  -31.47700 1.000 83.13452  ? 187  GLU   B OE1 1 
ATOM   4772 O OE2 . GLU   B 1 211 ? -9.70300  37.00100  -30.39900 1.000 74.44253  ? 187  GLU   B OE2 1 
ATOM   4773 N N   . GLU   B 1 212 ? -11.46600 32.94000  -27.15200 1.000 65.91684  ? 188  GLU   B N   1 
ATOM   4774 C CA  . GLU   B 1 212 ? -10.79800 32.74100  -25.87300 1.000 63.29020  ? 188  GLU   B CA  1 
ATOM   4775 C C   . GLU   B 1 212 ? -9.82900  33.86500  -25.53700 1.000 57.40909  ? 188  GLU   B C   1 
ATOM   4776 O O   . GLU   B 1 212 ? -9.01100  33.71700  -24.62100 1.000 55.60168  ? 188  GLU   B O   1 
ATOM   4777 C CB  . GLU   B 1 212 ? -10.07500 31.39400  -25.86200 1.000 63.38001  ? 188  GLU   B CB  1 
ATOM   4778 C CG  . GLU   B 1 212 ? -10.94800 30.24500  -26.34000 1.000 74.59470  ? 188  GLU   B CG  1 
ATOM   4779 C CD  . GLU   B 1 212 ? -10.32300 28.89000  -26.09200 1.000 90.45404  ? 188  GLU   B CD  1 
ATOM   4780 O OE1 . GLU   B 1 212 ? -9.58800  28.75100  -25.09100 1.000 89.17398  ? 188  GLU   B OE1 1 
ATOM   4781 O OE2 . GLU   B 1 212 ? -10.57000 27.96400  -26.89500 1.000 114.54411 ? 188  GLU   B OE2 1 
ATOM   4782 N N   . THR   B 1 213 ? -9.91200  34.97600  -26.26300 1.000 59.12828  ? 189  THR   B N   1 
ATOM   4783 C CA  . THR   B 1 213 ? -9.12900  36.17300  -26.00100 1.000 62.25963  ? 189  THR   B CA  1 
ATOM   4784 C C   . THR   B 1 213 ? -9.94900  37.26300  -25.32500 1.000 54.90634  ? 189  THR   B C   1 
ATOM   4785 O O   . THR   B 1 213 ? -9.37900  38.11400  -24.63400 1.000 55.79925  ? 189  THR   B O   1 
ATOM   4786 C CB  . THR   B 1 213 ? -8.53100  36.68800  -27.32400 1.000 59.04346  ? 189  THR   B CB  1 
ATOM   4787 O OG1 . THR   B 1 213 ? -7.64500  35.69800  -27.86000 1.000 50.46165  ? 189  THR   B OG1 1 
ATOM   4788 C CG2 . THR   B 1 213 ? -7.78300  37.99400  -27.16000 1.000 53.86700  ? 189  THR   B CG2 1 
ATOM   4789 N N   . CYS   B 1 214 ? -11.26800 37.23900  -25.48300 1.000 56.86497  ? 190  CYS   B N   1 
ATOM   4790 C CA  . CYS   B 1 214 ? -12.15400 38.19500  -24.83800 1.000 62.78886  ? 190  CYS   B CA  1 
ATOM   4791 C C   . CYS   B 1 214 ? -12.82000 37.53700  -23.63900 1.000 68.44172  ? 190  CYS   B C   1 
ATOM   4792 O O   . CYS   B 1 214 ? -13.44400 36.48000  -23.77400 1.000 64.24724  ? 190  CYS   B O   1 
ATOM   4793 C CB  . CYS   B 1 214 ? -13.21900 38.70200  -25.80700 1.000 63.45483  ? 190  CYS   B CB  1 
ATOM   4794 S SG  . CYS   B 1 214 ? -14.44400 39.76900  -25.02000 1.000 85.62942  ? 190  CYS   B SG  1 
ATOM   4795 N N   . CYS   B 1 215 ? -12.68500 38.16400  -22.47300 1.000 63.57942  ? 191  CYS   B N   1 
ATOM   4796 C CA  . CYS   B 1 215 ? -13.31600 37.69600  -21.24400 1.000 59.99412  ? 191  CYS   B CA  1 
ATOM   4797 C C   . CYS   B 1 215 ? -14.00600 38.85900  -20.54600 1.000 62.85967  ? 191  CYS   B C   1 
ATOM   4798 O O   . CYS   B 1 215 ? -13.78400 39.14700  -19.36900 1.000 58.31371  ? 191  CYS   B O   1 
ATOM   4799 C CB  . CYS   B 1 215 ? -12.29400 37.01500  -20.34000 1.000 59.06886  ? 191  CYS   B CB  1 
ATOM   4800 S SG  . CYS   B 1 215 ? -12.91700 36.47000  -18.73400 1.000 35.22270  ? 191  CYS   B SG  1 
ATOM   4801 N N   . ASP   B 1 216 ? -14.84800 39.56400  -21.29300 1.000 63.26949  ? 192  ASP   B N   1 
ATOM   4802 C CA  . ASP   B 1 216 ? -15.68000 40.61200  -20.72800 1.000 67.26286  ? 192  ASP   B CA  1 
ATOM   4803 C C   . ASP   B 1 216 ? -17.02200 40.02000  -20.32100 1.000 68.77967  ? 192  ASP   B C   1 
ATOM   4804 O O   . ASP   B 1 216 ? -17.54500 39.11900  -20.98300 1.000 78.17118  ? 192  ASP   B O   1 
ATOM   4805 C CB  . ASP   B 1 216 ? -15.87000 41.75800  -21.72100 1.000 71.52824  ? 192  ASP   B CB  1 
ATOM   4806 C CG  . ASP   B 1 216 ? -14.55800 42.43000  -22.08700 1.000 84.45629  ? 192  ASP   B CG  1 
ATOM   4807 O OD1 . ASP   B 1 216 ? -13.80700 42.80800  -21.16100 1.000 85.63063  ? 192  ASP   B OD1 1 
ATOM   4808 O OD2 . ASP   B 1 216 ? -14.28000 42.58700  -23.29600 1.000 84.93691  ? 192  ASP   B OD2 1 
ATOM   4809 N N   . PHE   B 1 217 ? -17.57000 40.52600  -19.21900 1.000 66.48544  ? 193  PHE   B N   1 
ATOM   4810 C CA  . PHE   B 1 217 ? -18.69500 39.88000  -18.54700 1.000 65.91337  ? 193  PHE   B CA  1 
ATOM   4811 C C   . PHE   B 1 217 ? -20.00000 40.46900  -19.07600 1.000 65.68022  ? 193  PHE   B C   1 
ATOM   4812 O O   . PHE   B 1 217 ? -20.66900 41.28000  -18.43000 1.000 73.07989  ? 193  PHE   B O   1 
ATOM   4813 C CB  . PHE   B 1 217 ? -18.55600 40.03700  -17.03700 1.000 63.88699  ? 193  PHE   B CB  1 
ATOM   4814 C CG  . PHE   B 1 217 ? -19.29500 39.00200  -16.24200 1.000 46.32340  ? 193  PHE   B CG  1 
ATOM   4815 C CD1 . PHE   B 1 217 ? -19.01500 37.65800  -16.40800 1.000 46.81149  ? 193  PHE   B CD1 1 
ATOM   4816 C CD2 . PHE   B 1 217 ? -20.23900 39.37400  -15.30400 1.000 47.42103  ? 193  PHE   B CD2 1 
ATOM   4817 C CE1 . PHE   B 1 217 ? -19.68700 36.70200  -15.67700 1.000 46.58661  ? 193  PHE   B CE1 1 
ATOM   4818 C CE2 . PHE   B 1 217 ? -20.91000 38.42200  -14.56400 1.000 50.87887  ? 193  PHE   B CE2 1 
ATOM   4819 C CZ  . PHE   B 1 217 ? -20.63300 37.08300  -14.75000 1.000 49.49175  ? 193  PHE   B CZ  1 
ATOM   4820 N N   . PHE   B 1 218 ? -20.35900 40.05300  -20.28900 1.000 58.65523  ? 194  PHE   B N   1 
ATOM   4821 C CA  . PHE   B 1 218 ? -21.65700 40.40900  -20.84700 1.000 58.96282  ? 194  PHE   B CA  1 
ATOM   4822 C C   . PHE   B 1 218 ? -22.73800 39.59400  -20.15400 1.000 56.40248  ? 194  PHE   B C   1 
ATOM   4823 O O   . PHE   B 1 218 ? -22.62200 38.37000  -20.04500 1.000 62.20903  ? 194  PHE   B O   1 
ATOM   4824 C CB  . PHE   B 1 218 ? -21.69300 40.13800  -22.35100 1.000 65.74181  ? 194  PHE   B CB  1 
ATOM   4825 C CG  . PHE   B 1 218 ? -20.74500 40.98000  -23.15400 1.000 64.20067  ? 194  PHE   B CG  1 
ATOM   4826 C CD1 . PHE   B 1 218 ? -21.00400 42.32300  -23.37600 1.000 57.76981  ? 194  PHE   B CD1 1 
ATOM   4827 C CD2 . PHE   B 1 218 ? -19.60400 40.41900  -23.70600 1.000 59.06738  ? 194  PHE   B CD2 1 
ATOM   4828 C CE1 . PHE   B 1 218 ? -20.13500 43.09400  -24.11800 1.000 55.33216  ? 194  PHE   B CE1 1 
ATOM   4829 C CE2 . PHE   B 1 218 ? -18.73100 41.18300  -24.44900 1.000 59.85110  ? 194  PHE   B CE2 1 
ATOM   4830 C CZ  . PHE   B 1 218 ? -18.99600 42.52200  -24.65700 1.000 61.38869  ? 194  PHE   B CZ  1 
ATOM   4831 N N   . THR   B 1 219 ? -23.78900 40.26500  -19.67900 1.000 59.68868  ? 195  THR   B N   1 
ATOM   4832 C CA  . THR   B 1 219 ? -24.87400 39.58400  -18.98000 1.000 60.96713  ? 195  THR   B CA  1 
ATOM   4833 C C   . THR   B 1 219 ? -26.22000 40.11100  -19.45100 1.000 57.60690  ? 195  THR   B C   1 
ATOM   4834 O O   . THR   B 1 219 ? -26.38800 41.31900  -19.64000 1.000 62.53239  ? 195  THR   B O   1 
ATOM   4835 C CB  . THR   B 1 219 ? -24.79300 39.75800  -17.45000 1.000 55.40615  ? 195  THR   B CB  1 
ATOM   4836 O OG1 . THR   B 1 219 ? -25.06000 41.12200  -17.10300 1.000 56.50062  ? 195  THR   B OG1 1 
ATOM   4837 C CG2 . THR   B 1 219 ? -23.42000 39.35500  -16.91800 1.000 51.39150  ? 195  THR   B CG2 1 
ATOM   4838 N N   . ASN   B 1 220 ? -27.18000 39.20400  -19.63300 1.000 51.72497  ? 196  ASN   B N   1 
ATOM   4839 C CA  . ASN   B 1 220 ? -28.55800 39.63500  -19.82100 1.000 50.62917  ? 196  ASN   B CA  1 
ATOM   4840 C C   . ASN   B 1 220 ? -29.01800 40.37400  -18.57100 1.000 54.30922  ? 196  ASN   B C   1 
ATOM   4841 O O   . ASN   B 1 220 ? -28.63700 40.02200  -17.45200 1.000 65.66427  ? 196  ASN   B O   1 
ATOM   4842 C CB  . ASN   B 1 220 ? -29.46000 38.43300  -20.16200 1.000 54.96579  ? 196  ASN   B CB  1 
ATOM   4843 C CG  . ASN   B 1 220 ? -29.62100 37.42200  -19.01600 1.000 48.61677  ? 196  ASN   B CG  1 
ATOM   4844 O OD1 . ASN   B 1 220 ? -29.88000 37.77300  -17.86700 1.000 44.61170  ? 196  ASN   B OD1 1 
ATOM   4845 N ND2 . ASN   B 1 220 ? -29.46100 36.14500  -19.34900 1.000 50.58431  ? 196  ASN   B ND2 1 
ATOM   4846 N N   . GLN   B 1 221 ? -29.79300 41.44500  -18.75900 1.000 56.73292  ? 197  GLN   B N   1 
ATOM   4847 C CA  . GLN   B 1 221 ? -30.09700 42.31100  -17.62500 1.000 57.18956  ? 197  GLN   B CA  1 
ATOM   4848 C C   . GLN   B 1 221 ? -30.95400 41.62600  -16.57000 1.000 54.43682  ? 197  GLN   B C   1 
ATOM   4849 O O   . GLN   B 1 221 ? -31.06900 42.15100  -15.45600 1.000 56.07806  ? 197  GLN   B O   1 
ATOM   4850 C CB  . GLN   B 1 221 ? -30.77100 43.60100  -18.09500 1.000 62.46728  ? 197  GLN   B CB  1 
ATOM   4851 C CG  . GLN   B 1 221 ? -31.56100 43.47900  -19.38000 1.000 75.01898  ? 197  GLN   B CG  1 
ATOM   4852 C CD  . GLN   B 1 221 ? -32.35500 44.73500  -19.68600 1.000 88.13051  ? 197  GLN   B CD  1 
ATOM   4853 O OE1 . GLN   B 1 221 ? -32.82000 45.42500  -18.77700 1.000 89.32137  ? 197  GLN   B OE1 1 
ATOM   4854 N NE2 . GLN   B 1 221 ? -32.50100 45.04700  -20.96900 1.000 91.60660  ? 197  GLN   B NE2 1 
ATOM   4855 N N   . ALA   B 1 222 ? -31.54600 40.47000  -16.88000 1.000 50.18667  ? 198  ALA   B N   1 
ATOM   4856 C CA  . ALA   B 1 222 ? -32.22100 39.69400  -15.84500 1.000 48.25981  ? 198  ALA   B CA  1 
ATOM   4857 C C   . ALA   B 1 222 ? -31.22800 39.23400  -14.78600 1.000 51.03334  ? 198  ALA   B C   1 
ATOM   4858 O O   . ALA   B 1 222 ? -31.43300 39.45600  -13.58800 1.000 48.52402  ? 198  ALA   B O   1 
ATOM   4859 C CB  . ALA   B 1 222 ? -32.94500 38.50200  -16.46800 1.000 47.28244  ? 198  ALA   B CB  1 
ATOM   4860 N N   . TYR   B 1 223 ? -30.13300 38.59900  -15.21600 1.000 51.35098  ? 199  TYR   B N   1 
ATOM   4861 C CA  . TYR   B 1 223 ? -29.04900 38.25800  -14.29900 1.000 41.86240  ? 199  TYR   B CA  1 
ATOM   4862 C C   . TYR   B 1 223 ? -28.49800 39.49700  -13.60900 1.000 45.86978  ? 199  TYR   B C   1 
ATOM   4863 O O   . TYR   B 1 223 ? -28.30400 39.50900  -12.38700 1.000 52.34032  ? 199  TYR   B O   1 
ATOM   4864 C CB  . TYR   B 1 223 ? -27.93600 37.53600  -15.05500 1.000 43.44324  ? 199  TYR   B CB  1 
ATOM   4865 C CG  . TYR   B 1 223 ? -26.76900 37.10000  -14.19300 1.000 44.73568  ? 199  TYR   B CG  1 
ATOM   4866 C CD1 . TYR   B 1 223 ? -25.70600 37.96100  -13.94000 1.000 44.62439  ? 199  TYR   B CD1 1 
ATOM   4867 C CD2 . TYR   B 1 223 ? -26.72100 35.82500  -13.64700 1.000 45.74994  ? 199  TYR   B CD2 1 
ATOM   4868 C CE1 . TYR   B 1 223 ? -24.63500 37.56900  -13.15800 1.000 45.33315  ? 199  TYR   B CE1 1 
ATOM   4869 C CE2 . TYR   B 1 223 ? -25.65400 35.42200  -12.86900 1.000 48.69086  ? 199  TYR   B CE2 1 
ATOM   4870 C CZ  . TYR   B 1 223 ? -24.61300 36.29700  -12.62400 1.000 54.17007  ? 199  TYR   B CZ  1 
ATOM   4871 O OH  . TYR   B 1 223 ? -23.54600 35.89800  -11.84400 1.000 53.20134  ? 199  TYR   B OH  1 
ATOM   4872 N N   . ALA   B 1 224 ? -28.23200 40.55100  -14.38400 1.000 42.88908  ? 200  ALA   B N   1 
ATOM   4873 C CA  . ALA   B 1 224 ? -27.55500 41.72500  -13.84500 1.000 46.08028  ? 200  ALA   B CA  1 
ATOM   4874 C C   . ALA   B 1 224 ? -28.30200 42.31500  -12.65500 1.000 47.16904  ? 200  ALA   B C   1 
ATOM   4875 O O   . ALA   B 1 224 ? -27.67900 42.78800  -11.70100 1.000 51.06578  ? 200  ALA   B O   1 
ATOM   4876 C CB  . ALA   B 1 224 ? -27.37900 42.77300  -14.94200 1.000 56.34881  ? 200  ALA   B CB  1 
ATOM   4877 N N   . ILE   B 1 225 ? -29.63200 42.29400  -12.68700 1.000 51.12716  ? 201  ILE   B N   1 
ATOM   4878 C CA  . ILE   B 1 225 ? -30.42800 42.84300  -11.58800 1.000 49.31331  ? 201  ILE   B CA  1 
ATOM   4879 C C   . ILE   B 1 225 ? -30.73400 41.78700  -10.53600 1.000 46.47937  ? 201  ILE   B C   1 
ATOM   4880 O O   . ILE   B 1 225 ? -30.52300 42.01500  -9.34100  1.000 47.04555  ? 201  ILE   B O   1 
ATOM   4881 C CB  . ILE   B 1 225 ? -31.72500 43.48000  -12.12400 1.000 51.37357  ? 201  ILE   B CB  1 
ATOM   4882 C CG1 . ILE   B 1 225 ? -31.42100 44.82400  -12.78200 1.000 53.94039  ? 201  ILE   B CG1 1 
ATOM   4883 C CG2 . ILE   B 1 225 ? -32.75100 43.62600  -11.00500 1.000 44.49993  ? 201  ILE   B CG2 1 
ATOM   4884 C CD1 . ILE   B 1 225 ? -32.62000 45.73200  -12.89100 1.000 54.23070  ? 201  ILE   B CD1 1 
ATOM   4885 N N   . ALA   B 1 226 ? -31.25000 40.63100  -10.96400 1.000 42.88101  ? 202  ALA   B N   1 
ATOM   4886 C CA  . ALA   B 1 226 ? -31.61400 39.57400  -10.02800 1.000 40.68285  ? 202  ALA   B CA  1 
ATOM   4887 C C   . ALA   B 1 226 ? -30.45700 39.24400  -9.09500  1.000 43.25656  ? 202  ALA   B C   1 
ATOM   4888 O O   . ALA   B 1 226 ? -30.58500 39.33400  -7.87000  1.000 49.90982  ? 202  ALA   B O   1 
ATOM   4889 C CB  . ALA   B 1 226 ? -32.06500 38.32700  -10.78900 1.000 38.70894  ? 202  ALA   B CB  1 
ATOM   4890 N N   . SER   B 1 227 ? -29.30600 38.88100  -9.66500  1.000 44.99784  ? 203  SER   B N   1 
ATOM   4891 C CA  . SER   B 1 227 ? -28.14800 38.54200  -8.84500  1.000 47.90131  ? 203  SER   B CA  1 
ATOM   4892 C C   . SER   B 1 227 ? -27.67500 39.73900  -8.02500  1.000 46.07457  ? 203  SER   B C   1 
ATOM   4893 O O   . SER   B 1 227 ? -27.21800 39.57900  -6.88700  1.000 45.28574  ? 203  SER   B O   1 
ATOM   4894 C CB  . SER   B 1 227 ? -27.01900 38.01400  -9.73000  1.000 43.82475  ? 203  SER   B CB  1 
ATOM   4895 O OG  . SER   B 1 227 ? -26.43200 39.06200  -10.47900 1.000 40.57155  ? 203  SER   B OG  1 
ATOM   4896 N N   . SER   B 1 228 ? -27.77300 40.94800  -8.58600  1.000 42.09882  ? 204  SER   B N   1 
ATOM   4897 C CA  . SER   B 1 228 ? -27.35600 42.13600  -7.84900  1.000 37.71672  ? 204  SER   B CA  1 
ATOM   4898 C C   . SER   B 1 228 ? -28.20000 42.34600  -6.60100  1.000 45.59109  ? 204  SER   B C   1 
ATOM   4899 O O   . SER   B 1 228 ? -27.71500 42.90400  -5.61100  1.000 43.13035  ? 204  SER   B O   1 
ATOM   4900 C CB  . SER   B 1 228 ? -27.43600 43.36900  -8.74900  1.000 40.60833  ? 204  SER   B CB  1 
ATOM   4901 O OG  . SER   B 1 228 ? -26.88200 44.51400  -8.13000  1.000 44.22984  ? 204  SER   B OG  1 
ATOM   4902 N N   . ILE   B 1 229 ? -29.45400 41.90100  -6.62200  1.000 48.23683  ? 205  ILE   B N   1 
ATOM   4903 C CA  . ILE   B 1 229 ? -30.36600 42.13000  -5.50700  1.000 46.46221  ? 205  ILE   B CA  1 
ATOM   4904 C C   . ILE   B 1 229 ? -30.21500 41.02800  -4.46600  1.000 43.38239  ? 205  ILE   B C   1 
ATOM   4905 O O   . ILE   B 1 229 ? -29.96900 41.30900  -3.28700  1.000 47.90217  ? 205  ILE   B O   1 
ATOM   4906 C CB  . ILE   B 1 229 ? -31.82300 42.23600  -5.99500  1.000 42.17228  ? 205  ILE   B CB  1 
ATOM   4907 C CG1 . ILE   B 1 229 ? -32.09100 43.63000  -6.56300  1.000 41.14942  ? 205  ILE   B CG1 1 
ATOM   4908 C CG2 . ILE   B 1 229 ? -32.79400 41.93300  -4.86700  1.000 40.11222  ? 205  ILE   B CG2 1 
ATOM   4909 C CD1 . ILE   B 1 229 ? -33.45800 43.77700  -7.17700  1.000 32.54198  ? 205  ILE   B CD1 1 
ATOM   4910 N N   . VAL   B 1 230 ? -30.35200 39.76800  -4.89000  1.000 36.75492  ? 206  VAL   B N   1 
ATOM   4911 C CA  . VAL   B 1 230 ? -30.36000 38.66200  -3.93500  1.000 38.28535  ? 206  VAL   B CA  1 
ATOM   4912 C C   . VAL   B 1 230 ? -29.02600 38.57000  -3.20200  1.000 41.60646  ? 206  VAL   B C   1 
ATOM   4913 O O   . VAL   B 1 230 ? -28.98100 38.27000  -2.00400  1.000 51.38341  ? 206  VAL   B O   1 
ATOM   4914 C CB  . VAL   B 1 230 ? -30.70700 37.33700  -4.64000  1.000 29.20322  ? 206  VAL   B CB  1 
ATOM   4915 C CG1 . VAL   B 1 230 ? -29.83800 37.13800  -5.86100  1.000 45.49013  ? 206  VAL   B CG1 1 
ATOM   4916 C CG2 . VAL   B 1 230 ? -30.54200 36.16700  -3.69100  1.000 26.57601  ? 206  VAL   B CG2 1 
ATOM   4917 N N   . SER   B 1 231 ? -27.92500 38.84900  -3.89700  1.000 40.07317  ? 207  SER   B N   1 
ATOM   4918 C CA  . SER   B 1 231 ? -26.59500 38.63500  -3.34400  1.000 34.65815  ? 207  SER   B CA  1 
ATOM   4919 C C   . SER   B 1 231 ? -25.91700 39.90700  -2.85400  1.000 37.35668  ? 207  SER   B C   1 
ATOM   4920 O O   . SER   B 1 231 ? -24.82200 39.81900  -2.29500  1.000 41.20257  ? 207  SER   B O   1 
ATOM   4921 C CB  . SER   B 1 231 ? -25.69300 37.95400  -4.38000  1.000 43.98384  ? 207  SER   B CB  1 
ATOM   4922 O OG  . SER   B 1 231 ? -26.28500 36.76900  -4.88500  1.000 57.33599  ? 207  SER   B OG  1 
ATOM   4923 N N   . PHE   B 1 232 ? -26.51700 41.07900  -3.05100  1.000 41.18069  ? 208  PHE   B N   1 
ATOM   4924 C CA  . PHE   B 1 232 ? -25.94400 42.29700  -2.49200  1.000 35.57675  ? 208  PHE   B CA  1 
ATOM   4925 C C   . PHE   B 1 232 ? -26.98600 43.09100  -1.71900  1.000 41.36246  ? 208  PHE   B C   1 
ATOM   4926 O O   . PHE   B 1 232 ? -26.85300 43.25700  -0.50400  1.000 49.47580  ? 208  PHE   B O   1 
ATOM   4927 C CB  . PHE   B 1 232 ? -25.31800 43.17100  -3.58100  1.000 38.32827  ? 208  PHE   B CB  1 
ATOM   4928 C CG  . PHE   B 1 232 ? -24.71900 44.45400  -3.06200  1.000 43.18203  ? 208  PHE   B CG  1 
ATOM   4929 C CD1 . PHE   B 1 232 ? -23.45300 44.46700  -2.49100  1.000 42.84065  ? 208  PHE   B CD1 1 
ATOM   4930 C CD2 . PHE   B 1 232 ? -25.41200 45.65200  -3.16500  1.000 43.44800  ? 208  PHE   B CD2 1 
ATOM   4931 C CE1 . PHE   B 1 232 ? -22.89300 45.64900  -2.01800  1.000 35.12834  ? 208  PHE   B CE1 1 
ATOM   4932 C CE2 . PHE   B 1 232 ? -24.85700 46.83400  -2.70000  1.000 46.03722  ? 208  PHE   B CE2 1 
ATOM   4933 C CZ  . PHE   B 1 232 ? -23.59600 46.83200  -2.12100  1.000 38.68412  ? 208  PHE   B CZ  1 
ATOM   4934 N N   . TYR   B 1 233 ? -28.03100 43.57300  -2.39800  1.000 41.98323  ? 209  TYR   B N   1 
ATOM   4935 C CA  . TYR   B 1 233 ? -28.95400 44.50300  -1.75200  1.000 40.53148  ? 209  TYR   B CA  1 
ATOM   4936 C C   . TYR   B 1 233 ? -29.72300 43.84000  -0.61400  1.000 43.46776  ? 209  TYR   B C   1 
ATOM   4937 O O   . TYR   B 1 233 ? -29.81500 44.39800  0.48500   1.000 44.40242  ? 209  TYR   B O   1 
ATOM   4938 C CB  . TYR   B 1 233 ? -29.91400 45.09800  -2.77600  1.000 36.89138  ? 209  TYR   B CB  1 
ATOM   4939 C CG  . TYR   B 1 233 ? -29.24100 46.02900  -3.74600  1.000 41.04016  ? 209  TYR   B CG  1 
ATOM   4940 C CD1 . TYR   B 1 233 ? -28.98800 47.35100  -3.40000  1.000 40.29790  ? 209  TYR   B CD1 1 
ATOM   4941 C CD2 . TYR   B 1 233 ? -28.89400 45.60600  -5.01900  1.000 41.34386  ? 209  TYR   B CD2 1 
ATOM   4942 C CE1 . TYR   B 1 233 ? -28.37600 48.21500  -4.28500  1.000 40.81629  ? 209  TYR   B CE1 1 
ATOM   4943 C CE2 . TYR   B 1 233 ? -28.28700 46.46500  -5.91500  1.000 44.63993  ? 209  TYR   B CE2 1 
ATOM   4944 C CZ  . TYR   B 1 233 ? -28.03100 47.77000  -5.54200  1.000 44.01894  ? 209  TYR   B CZ  1 
ATOM   4945 O OH  . TYR   B 1 233 ? -27.43000 48.63700  -6.42400  1.000 50.78575  ? 209  TYR   B OH  1 
ATOM   4946 N N   . VAL   B 1 234 ? -30.28800 42.65200  -0.85200  1.000 43.14055  ? 210  VAL   B N   1 
ATOM   4947 C CA  . VAL   B 1 234 ? -31.05500 41.97900  0.19900   1.000 40.04038  ? 210  VAL   B CA  1 
ATOM   4948 C C   . VAL   B 1 234 ? -30.22000 41.76100  1.45800   1.000 43.39779  ? 210  VAL   B C   1 
ATOM   4949 O O   . VAL   B 1 234 ? -30.66900 42.15700  2.54200   1.000 42.05286  ? 210  VAL   B O   1 
ATOM   4950 C CB  . VAL   B 1 234 ? -31.67900 40.68000  -0.34100  1.000 39.35309  ? 210  VAL   B CB  1 
ATOM   4951 C CG1 . VAL   B 1 234 ? -32.24500 39.85800  0.80400   1.000 27.05269  ? 210  VAL   B CG1 1 
ATOM   4952 C CG2 . VAL   B 1 234 ? -32.76100 40.99700  -1.35700  1.000 43.02526  ? 210  VAL   B CG2 1 
ATOM   4953 N N   . PRO   B 1 235 ? -29.01700 41.17400  1.39700   1.000 49.27363  ? 211  PRO   B N   1 
ATOM   4954 C CA  . PRO   B 1 235 ? -28.21500 41.09200  2.63100   1.000 45.33054  ? 211  PRO   B CA  1 
ATOM   4955 C C   . PRO   B 1 235 ? -27.78300 42.45200  3.14700   1.000 43.60985  ? 211  PRO   B C   1 
ATOM   4956 O O   . PRO   B 1 235 ? -27.75400 42.66300  4.36600   1.000 49.47692  ? 211  PRO   B O   1 
ATOM   4957 C CB  . PRO   B 1 235 ? -27.01000 40.22800  2.22400   1.000 40.13342  ? 211  PRO   B CB  1 
ATOM   4958 C CG  . PRO   B 1 235 ? -26.98700 40.24200  0.74700   1.000 43.84603  ? 211  PRO   B CG  1 
ATOM   4959 C CD  . PRO   B 1 235 ? -28.39500 40.41800  0.29400   1.000 41.02881  ? 211  PRO   B CD  1 
ATOM   4960 N N   . LEU   B 1 236 ? -27.45000 43.38500  2.25000   1.000 38.13849  ? 212  LEU   B N   1 
ATOM   4961 C CA  . LEU   B 1 236 ? -27.01300 44.70700  2.68600   1.000 38.61179  ? 212  LEU   B CA  1 
ATOM   4962 C C   . LEU   B 1 236 ? -28.10700 45.41500  3.47200   1.000 41.62889  ? 212  LEU   B C   1 
ATOM   4963 O O   . LEU   B 1 236 ? -27.83000 46.06200  4.48800   1.000 42.75775  ? 212  LEU   B O   1 
ATOM   4964 C CB  . LEU   B 1 236 ? -26.59400 45.55000  1.48200   1.000 38.01581  ? 212  LEU   B CB  1 
ATOM   4965 C CG  . LEU   B 1 236 ? -26.53900 47.07600  1.62200   1.000 46.58666  ? 212  LEU   B CG  1 
ATOM   4966 C CD1 . LEU   B 1 236 ? -25.65500 47.52300  2.77500   1.000 44.89369  ? 212  LEU   B CD1 1 
ATOM   4967 C CD2 . LEU   B 1 236 ? -26.09000 47.72800  0.32300   1.000 45.94838  ? 212  LEU   B CD2 1 
ATOM   4968 N N   . VAL   B 1 237 ? -29.35800 45.30400  3.02100   1.000 43.65425  ? 213  VAL   B N   1 
ATOM   4969 C CA  . VAL   B 1 237 ? -30.44900 45.99800  3.70000   1.000 38.46679  ? 213  VAL   B CA  1 
ATOM   4970 C C   . VAL   B 1 237 ? -30.71000 45.37200  5.06300   1.000 42.77568  ? 213  VAL   B C   1 
ATOM   4971 O O   . VAL   B 1 237 ? -30.84900 46.07700  6.07100   1.000 43.32429  ? 213  VAL   B O   1 
ATOM   4972 C CB  . VAL   B 1 237 ? -31.71500 46.00400  2.82900   1.000 35.05149  ? 213  VAL   B CB  1 
ATOM   4973 C CG1 . VAL   B 1 237 ? -32.89200 46.52700  3.62500   1.000 33.39619  ? 213  VAL   B CG1 1 
ATOM   4974 C CG2 . VAL   B 1 237 ? -31.49900 46.86600  1.59800   1.000 40.20694  ? 213  VAL   B CG2 1 
ATOM   4975 N N   . ILE   B 1 238 ? -30.77900 44.03900  5.11300   1.000 40.09034  ? 214  ILE   B N   1 
ATOM   4976 C CA  . ILE   B 1 238 ? -30.92300 43.34400  6.39100   1.000 42.00498  ? 214  ILE   B CA  1 
ATOM   4977 C C   . ILE   B 1 238 ? -29.82400 43.77700  7.35400   1.000 40.71770  ? 214  ILE   B C   1 
ATOM   4978 O O   . ILE   B 1 238 ? -30.08900 44.14100  8.50400   1.000 40.68149  ? 214  ILE   B O   1 
ATOM   4979 C CB  . ILE   B 1 238 ? -30.91300 41.82000  6.17500   1.000 40.52509  ? 214  ILE   B CB  1 
ATOM   4980 C CG1 . ILE   B 1 238 ? -32.23700 41.36000  5.56600   1.000 33.16551  ? 214  ILE   B CG1 1 
ATOM   4981 C CG2 . ILE   B 1 238 ? -30.63900 41.09400  7.48000   1.000 37.46808  ? 214  ILE   B CG2 1 
ATOM   4982 C CD1 . ILE   B 1 238 ? -32.20100 39.94500  5.04200   1.000 30.00747  ? 214  ILE   B CD1 1 
ATOM   4983 N N   . MET   B 1 239 ? -28.57500 43.76800  6.88200   1.000 42.34157  ? 215  MET   B N   1 
ATOM   4984 C CA  . MET   B 1 239 ? -27.44100 44.14800  7.71700   1.000 40.83346  ? 215  MET   B CA  1 
ATOM   4985 C C   . MET   B 1 239 ? -27.61600 45.54600  8.29900   1.000 41.83537  ? 215  MET   B C   1 
ATOM   4986 O O   . MET   B 1 239 ? -27.56800 45.73600  9.51900   1.000 42.10794  ? 215  MET   B O   1 
ATOM   4987 C CB  . MET   B 1 239 ? -26.14600 44.07900  6.90700   1.000 42.80337  ? 215  MET   B CB  1 
ATOM   4988 C CG  . MET   B 1 239 ? -24.91800 44.53400  7.68700   1.000 42.21589  ? 215  MET   B CG  1 
ATOM   4989 S SD  . MET   B 1 239 ? -23.47600 44.86100  6.66300   1.000 49.03411  ? 215  MET   B SD  1 
ATOM   4990 C CE  . MET   B 1 239 ? -23.92600 46.44900  5.96700   1.000 39.59500  ? 215  MET   B CE  1 
ATOM   4991 N N   . VAL   B 1 240 ? -27.81100 46.54100  7.42800   1.000 39.59615  ? 216  VAL   B N   1 
ATOM   4992 C CA  . VAL   B 1 240 ? -27.90100 47.92700  7.88300   1.000 42.26113  ? 216  VAL   B CA  1 
ATOM   4993 C C   . VAL   B 1 240 ? -29.05500 48.10500  8.86100   1.000 50.14180  ? 216  VAL   B C   1 
ATOM   4994 O O   . VAL   B 1 240 ? -28.96700 48.90400  9.80100   1.000 50.98550  ? 216  VAL   B O   1 
ATOM   4995 C CB  . VAL   B 1 240 ? -28.02000 48.88000  6.67500   1.000 34.92061  ? 216  VAL   B CB  1 
ATOM   4996 C CG1 . VAL   B 1 240 ? -28.43000 50.27800  7.11300   1.000 29.91001  ? 216  VAL   B CG1 1 
ATOM   4997 C CG2 . VAL   B 1 240 ? -26.70100 48.94400  5.93900   1.000 40.78441  ? 216  VAL   B CG2 1 
ATOM   4998 N N   . PHE   B 1 241 ? -30.13700 47.34900  8.68600   1.000 48.63362  ? 217  PHE   B N   1 
ATOM   4999 C CA  . PHE   B 1 241 ? -31.23600 47.44300  9.63900   1.000 48.96021  ? 217  PHE   B CA  1 
ATOM   5000 C C   . PHE   B 1 241 ? -30.89300 46.74400  10.95200  1.000 49.02619  ? 217  PHE   B C   1 
ATOM   5001 O O   . PHE   B 1 241 ? -30.97500 47.34800  12.02700  1.000 50.85299  ? 217  PHE   B O   1 
ATOM   5002 C CB  . PHE   B 1 241 ? -32.51500 46.85800  9.04100   1.000 50.77710  ? 217  PHE   B CB  1 
ATOM   5003 C CG  . PHE   B 1 241 ? -33.65700 46.82600  10.00600  1.000 49.89544  ? 217  PHE   B CG  1 
ATOM   5004 C CD1 . PHE   B 1 241 ? -34.36400 47.98100  10.29300  1.000 50.34211  ? 217  PHE   B CD1 1 
ATOM   5005 C CD2 . PHE   B 1 241 ? -34.01000 45.64900  10.64800  1.000 53.64894  ? 217  PHE   B CD2 1 
ATOM   5006 C CE1 . PHE   B 1 241 ? -35.41200 47.96600  11.19100  1.000 56.86799  ? 217  PHE   B CE1 1 
ATOM   5007 C CE2 . PHE   B 1 241 ? -35.05900 45.62400  11.54900  1.000 63.66801  ? 217  PHE   B CE2 1 
ATOM   5008 C CZ  . PHE   B 1 241 ? -35.76100 46.78500  11.82100  1.000 63.15885  ? 217  PHE   B CZ  1 
ATOM   5009 N N   . VAL   B 1 242 ? -30.50900 45.46400  10.88000  1.000 48.37283  ? 218  VAL   B N   1 
ATOM   5010 C CA  . VAL   B 1 242 ? -30.25500 44.68200  12.09000  1.000 44.93033  ? 218  VAL   B CA  1 
ATOM   5011 C C   . VAL   B 1 242 ? -29.19100 45.35100  12.95100  1.000 48.44798  ? 218  VAL   B C   1 
ATOM   5012 O O   . VAL   B 1 242 ? -29.38900 45.57400  14.15200  1.000 46.35137  ? 218  VAL   B O   1 
ATOM   5013 C CB  . VAL   B 1 242 ? -29.85000 43.24100  11.73100  1.000 36.29991  ? 218  VAL   B CB  1 
ATOM   5014 C CG1 . VAL   B 1 242 ? -29.33000 42.53200  12.96000  1.000 36.51643  ? 218  VAL   B CG1 1 
ATOM   5015 C CG2 . VAL   B 1 242 ? -31.02500 42.49000  11.14800  1.000 31.19193  ? 218  VAL   B CG2 1 
ATOM   5016 N N   . TYR   B 1 243 ? -28.04900 45.68800  12.35200  1.000 50.01221  ? 219  TYR   B N   1 
ATOM   5017 C CA  . TYR   B 1 243 ? -26.97200 46.27700  13.13800  1.000 52.58124  ? 219  TYR   B CA  1 
ATOM   5018 C C   . TYR   B 1 243 ? -27.32100 47.66300  13.66600  1.000 48.06533  ? 219  TYR   B C   1 
ATOM   5019 O O   . TYR   B 1 243 ? -26.73100 48.09600  14.66000  1.000 50.20298  ? 219  TYR   B O   1 
ATOM   5020 C CB  . TYR   B 1 243 ? -25.68100 46.35200  12.31900  1.000 44.52988  ? 219  TYR   B CB  1 
ATOM   5021 C CG  . TYR   B 1 243 ? -24.45700 46.41600  13.19900  1.000 39.17538  ? 219  TYR   B CG  1 
ATOM   5022 C CD1 . TYR   B 1 243 ? -24.10100 45.33900  13.99700  1.000 42.35390  ? 219  TYR   B CD1 1 
ATOM   5023 C CD2 . TYR   B 1 243 ? -23.68100 47.56500  13.26500  1.000 42.04670  ? 219  TYR   B CD2 1 
ATOM   5024 C CE1 . TYR   B 1 243 ? -22.99400 45.39200  14.82100  1.000 38.44355  ? 219  TYR   B CE1 1 
ATOM   5025 C CE2 . TYR   B 1 243 ? -22.57000 47.62800  14.08900  1.000 41.27686  ? 219  TYR   B CE2 1 
ATOM   5026 C CZ  . TYR   B 1 243 ? -22.23300 46.53900  14.86300  1.000 37.56912  ? 219  TYR   B CZ  1 
ATOM   5027 O OH  . TYR   B 1 243 ? -21.13200 46.58800  15.68100  1.000 38.61253  ? 219  TYR   B OH  1 
ATOM   5028 N N   . SER   B 1 244 ? -28.25700 48.36700  13.03200  1.000 46.08625  ? 220  SER   B N   1 
ATOM   5029 C CA  . SER   B 1 244 ? -28.63700 49.68100  13.53400  1.000 48.55257  ? 220  SER   B CA  1 
ATOM   5030 C C   . SER   B 1 244 ? -29.28800 49.57700  14.90600  1.000 51.43523  ? 220  SER   B C   1 
ATOM   5031 O O   . SER   B 1 244 ? -28.98300 50.37000  15.80400  1.000 47.94502  ? 220  SER   B O   1 
ATOM   5032 C CB  . SER   B 1 244 ? -29.56900 50.37600  12.54400  1.000 47.38603  ? 220  SER   B CB  1 
ATOM   5033 O OG  . SER   B 1 244 ? -30.74300 49.61300  12.33600  1.000 57.29344  ? 220  SER   B OG  1 
ATOM   5034 N N   . ARG   B 1 245 ? -30.19000 48.60700  15.08900  1.000 49.76057  ? 221  ARG   B N   1 
ATOM   5035 C CA  . ARG   B 1 245 ? -30.74400 48.37600  16.42000  1.000 55.32710  ? 221  ARG   B CA  1 
ATOM   5036 C C   . ARG   B 1 245 ? -29.66400 47.95100  17.40500  1.000 54.79184  ? 221  ARG   B C   1 
ATOM   5037 O O   . ARG   B 1 245 ? -29.73700 48.29400  18.59100  1.000 57.47581  ? 221  ARG   B O   1 
ATOM   5038 C CB  . ARG   B 1 245 ? -31.85900 47.32400  16.36500  1.000 59.07831  ? 221  ARG   B CB  1 
ATOM   5039 C CG  . ARG   B 1 245 ? -33.05900 47.64400  17.26600  1.000 68.02419  ? 221  ARG   B CG  1 
ATOM   5040 C CD  . ARG   B 1 245 ? -34.37000 47.11900  16.68900  1.000 74.88878  ? 221  ARG   B CD  1 
ATOM   5041 N NE  . ARG   B 1 245 ? -35.30700 46.67200  17.71500  1.000 76.80710  ? 221  ARG   B NE  1 
ATOM   5042 C CZ  . ARG   B 1 245 ? -36.22200 45.72800  17.53400  1.000 74.25859  ? 221  ARG   B CZ  1 
ATOM   5043 N NH1 . ARG   B 1 245 ? -36.32400 45.07500  16.38700  1.000 66.68180  ? 221  ARG   B NH1 1 
ATOM   5044 N NH2 . ARG   B 1 245 ? -37.05700 45.43400  18.52700  1.000 59.93340  ? 221  ARG   B NH2 1 
ATOM   5045 N N   . VAL   B 1 246 ? -28.65600 47.21500  16.93100  1.000 53.52050  ? 222  VAL   B N   1 
ATOM   5046 C CA  . VAL   B 1 246 ? -27.53900 46.82600  17.79100  1.000 52.43307  ? 222  VAL   B CA  1 
ATOM   5047 C C   . VAL   B 1 246 ? -26.90600 48.06100  18.41600  1.000 52.60030  ? 222  VAL   B C   1 
ATOM   5048 O O   . VAL   B 1 246 ? -26.70700 48.13500  19.63500  1.000 51.13868  ? 222  VAL   B O   1 
ATOM   5049 C CB  . VAL   B 1 246 ? -26.50300 46.01000  16.99400  1.000 49.53442  ? 222  VAL   B CB  1 
ATOM   5050 C CG1 . VAL   B 1 246 ? -25.28900 45.68900  17.85800  1.000 48.34136  ? 222  VAL   B CG1 1 
ATOM   5051 C CG2 . VAL   B 1 246 ? -27.12800 44.74500  16.43900  1.000 48.33802  ? 222  VAL   B CG2 1 
ATOM   5052 N N   . PHE   B 1 247 ? -26.58100 49.05200  17.58100  1.000 50.36694  ? 223  PHE   B N   1 
ATOM   5053 C CA  . PHE   B 1 247 ? -26.00200 50.29100  18.08900  1.000 51.30334  ? 223  PHE   B CA  1 
ATOM   5054 C C   . PHE   B 1 247 ? -26.95200 50.98500  19.05200  1.000 56.39828  ? 223  PHE   B C   1 
ATOM   5055 O O   . PHE   B 1 247 ? -26.52300 51.52200  20.08000  1.000 59.32951  ? 223  PHE   B O   1 
ATOM   5056 C CB  . PHE   B 1 247 ? -25.65200 51.22200  16.93000  1.000 49.50189  ? 223  PHE   B CB  1 
ATOM   5057 C CG  . PHE   B 1 247 ? -24.25900 51.04400  16.40700  1.000 52.25046  ? 223  PHE   B CG  1 
ATOM   5058 C CD1 . PHE   B 1 247 ? -23.25100 50.55800  17.22500  1.000 57.13924  ? 223  PHE   B CD1 1 
ATOM   5059 C CD2 . PHE   B 1 247 ? -23.95500 51.36700  15.09500  1.000 46.36685  ? 223  PHE   B CD2 1 
ATOM   5060 C CE1 . PHE   B 1 247 ? -21.96500 50.39500  16.74300  1.000 57.75588  ? 223  PHE   B CE1 1 
ATOM   5061 C CE2 . PHE   B 1 247 ? -22.67300 51.20700  14.60700  1.000 51.58927  ? 223  PHE   B CE2 1 
ATOM   5062 C CZ  . PHE   B 1 247 ? -21.67500 50.71900  15.43000  1.000 53.67076  ? 223  PHE   B CZ  1 
ATOM   5063 N N   . GLN   B 1 248 ? -28.24800 50.98500  18.73400  1.000 58.08140  ? 224  GLN   B N   1 
ATOM   5064 C CA  . GLN   B 1 248 ? -29.22900 51.61400  19.61000  1.000 57.85722  ? 224  GLN   B CA  1 
ATOM   5065 C C   . GLN   B 1 248 ? -29.28700 50.90900  20.96000  1.000 59.09356  ? 224  GLN   B C   1 
ATOM   5066 O O   . GLN   B 1 248 ? -29.16200 51.54700  22.01300  1.000 61.87192  ? 224  GLN   B O   1 
ATOM   5067 C CB  . GLN   B 1 248 ? -30.60200 51.61400  18.93800  1.000 61.89302  ? 224  GLN   B CB  1 
ATOM   5068 C CG  . GLN   B 1 248 ? -31.62700 52.50300  19.62000  1.000 71.86613  ? 224  GLN   B CG  1 
ATOM   5069 C CD  . GLN   B 1 248 ? -32.94500 51.79000  19.86100  1.000 81.28808  ? 224  GLN   B CD  1 
ATOM   5070 O OE1 . GLN   B 1 248 ? -33.36000 50.94200  19.06800  1.000 79.61128  ? 224  GLN   B OE1 1 
ATOM   5071 N NE2 . GLN   B 1 248 ? -33.60400 52.12200  20.96900  1.000 72.09430  ? 224  GLN   B NE2 1 
ATOM   5072 N N   . GLU   B 1 249 ? -29.46500 49.58400  20.94600  1.000 57.34693  ? 225  GLU   B N   1 
ATOM   5073 C CA  . GLU   B 1 249 ? -29.52400 48.82200  22.19100  1.000 57.53077  ? 225  GLU   B CA  1 
ATOM   5074 C C   . GLU   B 1 249 ? -28.26200 48.99800  23.02300  1.000 56.50853  ? 225  GLU   B C   1 
ATOM   5075 O O   . GLU   B 1 249 ? -28.29900 48.83900  24.24800  1.000 55.60692  ? 225  GLU   B O   1 
ATOM   5076 C CB  . GLU   B 1 249 ? -29.74000 47.34000  21.88800  1.000 50.98152  ? 225  GLU   B CB  1 
ATOM   5077 C CG  . GLU   B 1 249 ? -31.04300 47.03600  21.18000  1.000 63.29800  ? 225  GLU   B CG  1 
ATOM   5078 C CD  . GLU   B 1 249 ? -32.24700 47.25300  22.06600  1.000 73.14764  ? 225  GLU   B CD  1 
ATOM   5079 O OE1 . GLU   B 1 249 ? -32.18800 46.85900  23.25000  1.000 72.89742  ? 225  GLU   B OE1 1 
ATOM   5080 O OE2 . GLU   B 1 249 ? -33.25100 47.81700  21.57800  1.000 81.77261  ? 225  GLU   B OE2 1 
ATOM   5081 N N   . ALA   B 1 250 ? -27.14000 49.32600  22.37700  1.000 59.46836  ? 226  ALA   B N   1 
ATOM   5082 C CA  . ALA   B 1 250 ? -25.87900 49.47600  23.09400  1.000 57.48804  ? 226  ALA   B CA  1 
ATOM   5083 C C   . ALA   B 1 250 ? -25.90600 50.67700  24.02900  1.000 57.88751  ? 226  ALA   B C   1 
ATOM   5084 O O   . ALA   B 1 250 ? -25.38500 50.60700  25.14800  1.000 67.83324  ? 226  ALA   B O   1 
ATOM   5085 C CB  . ALA   B 1 250 ? -24.72300 49.59500  22.10100  1.000 56.32176  ? 226  ALA   B CB  1 
ATOM   5086 N N   . LYS   B 1 251 ? -26.50000 51.78800  23.59300  1.000 53.94555  ? 227  LYS   B N   1 
ATOM   5087 C CA  . LYS   B 1 251 ? -26.56400 52.96700  24.44700  1.000 59.83821  ? 227  LYS   B CA  1 
ATOM   5088 C C   . LYS   B 1 251 ? -27.80100 52.97800  25.33500  1.000 65.19246  ? 227  LYS   B C   1 
ATOM   5089 O O   . LYS   B 1 251 ? -27.78300 53.60900  26.39900  1.000 66.80898  ? 227  LYS   B O   1 
ATOM   5090 C CB  . LYS   B 1 251 ? -26.50700 54.24300  23.60000  1.000 53.09139  ? 227  LYS   B CB  1 
ATOM   5091 C CG  . LYS   B 1 251 ? -27.71200 54.48900  22.71100  1.000 62.73330  ? 227  LYS   B CG  1 
ATOM   5092 C CD  . LYS   B 1 251 ? -27.50200 55.73800  21.86500  1.000 65.75083  ? 227  LYS   B CD  1 
ATOM   5093 C CE  . LYS   B 1 251 ? -28.67700 55.99200  20.93800  1.000 75.62911  ? 227  LYS   B CE  1 
ATOM   5094 N NZ  . LYS   B 1 251 ? -28.43900 57.17500  20.06600  1.000 81.21480  ? 227  LYS   B NZ  1 
ATOM   5095 N N   . ARG   B 1 252 ? -28.86900 52.28200  24.93800  1.000 62.32052  ? 228  ARG   B N   1 
ATOM   5096 C CA  . ARG   B 1 252 ? -30.02600 52.16500  25.81800  1.000 65.98366  ? 228  ARG   B CA  1 
ATOM   5097 C C   . ARG   B 1 252 ? -29.67100 51.42200  27.10000  1.000 73.53982  ? 228  ARG   B C   1 
ATOM   5098 O O   . ARG   B 1 252 ? -30.28000 51.66600  28.14900  1.000 83.25019  ? 228  ARG   B O   1 
ATOM   5099 C CB  . ARG   B 1 252 ? -31.17500 51.46100  25.09300  1.000 68.27700  ? 228  ARG   B CB  1 
ATOM   5100 C CG  . ARG   B 1 252 ? -32.49800 51.49000  25.85100  1.000 74.29701  ? 228  ARG   B CG  1 
ATOM   5101 C CD  . ARG   B 1 252 ? -33.63500 50.88300  25.04200  1.000 84.11771  ? 228  ARG   B CD  1 
ATOM   5102 N NE  . ARG   B 1 252 ? -33.71400 49.43400  25.18300  1.000 86.08900  ? 228  ARG   B NE  1 
ATOM   5103 C CZ  . ARG   B 1 252 ? -34.57000 48.66300  24.52500  1.000 95.16717  ? 228  ARG   B CZ  1 
ATOM   5104 N NH1 . ARG   B 1 252 ? -35.42000 49.16700  23.64300  1.000 82.76958  ? 228  ARG   B NH1 1 
ATOM   5105 N NH2 . ARG   B 1 252 ? -34.57500 47.35300  24.75900  1.000 95.57502  ? 228  ARG   B NH2 1 
ATOM   5106 N N   . GLN   B 1 253 ? -28.68400 50.53300  27.04200  1.000 63.37760  ? 229  GLN   B N   1 
ATOM   5107 C CA  . GLN   B 1 253 ? -28.30400 49.72800  28.19800  1.000 62.03428  ? 229  GLN   B CA  1 
ATOM   5108 C C   . GLN   B 1 253 ? -26.98600 50.22000  28.78600  1.000 63.79237  ? 229  GLN   B C   1 
ATOM   5109 O O   . GLN   B 1 253 ? -26.94200 50.70900  29.91400  1.000 63.61320  ? 229  GLN   B O   1 
ATOM   5110 C CB  . GLN   B 1 253 ? -28.19500 48.25300  27.80400  1.000 53.95193  ? 229  GLN   B CB  1 
ATOM   5111 C CG  . GLN   B 1 253 ? -29.41500 47.72400  27.06300  1.000 54.91968  ? 229  GLN   B CG  1 
ATOM   5112 C CD  . GLN   B 1 253 ? -29.44500 46.20900  26.95500  1.000 51.74480  ? 229  GLN   B CD  1 
ATOM   5113 O OE1 . GLN   B 1 253 ? -28.75600 45.50300  27.68800  1.000 44.23471  ? 229  GLN   B OE1 1 
ATOM   5114 N NE2 . GLN   B 1 253 ? -30.23500 45.70500  26.01700  1.000 64.34837  ? 229  GLN   B NE2 1 
ATOM   5115 N N   . LYS   B 1 287 ? -21.72200 58.08900  24.16000  1.000 75.39123  ? 263  LYS   B N   1 
ATOM   5116 C CA  . LYS   B 1 287 ? -21.65600 56.79000  23.50100  1.000 70.45397  ? 263  LYS   B CA  1 
ATOM   5117 C C   . LYS   B 1 287 ? -20.21600 56.43600  23.13600  1.000 65.85185  ? 263  LYS   B C   1 
ATOM   5118 O O   . LYS   B 1 287 ? -19.34600 57.30800  23.08600  1.000 60.34496  ? 263  LYS   B O   1 
ATOM   5119 C CB  . LYS   B 1 287 ? -22.53800 56.79100  22.25100  1.000 67.07992  ? 263  LYS   B CB  1 
ATOM   5120 C CG  . LYS   B 1 287 ? -22.47800 58.09100  21.46200  1.000 64.86473  ? 263  LYS   B CG  1 
ATOM   5121 C CD  . LYS   B 1 287 ? -23.23800 57.98600  20.15700  1.000 58.84158  ? 263  LYS   B CD  1 
ATOM   5122 C CE  . LYS   B 1 287 ? -24.71700 57.77600  20.42000  1.000 67.36963  ? 263  LYS   B CE  1 
ATOM   5123 N NZ  . LYS   B 1 287 ? -25.50000 57.74000  19.15900  1.000 78.56848  ? 263  LYS   B NZ  1 
ATOM   5124 N N   . PHE   B 1 288 ? -19.96800 55.14200  22.92100  1.000 60.96740  ? 264  PHE   B N   1 
ATOM   5125 C CA  . PHE   B 1 288 ? -18.75100 54.66000  22.27400  1.000 63.33351  ? 264  PHE   B CA  1 
ATOM   5126 C C   . PHE   B 1 288 ? -17.50600 54.87900  23.13400  1.000 62.46147  ? 264  PHE   B C   1 
ATOM   5127 O O   . PHE   B 1 288 ? -16.41500 55.12000  22.60600  1.000 64.17154  ? 264  PHE   B O   1 
ATOM   5128 C CB  . PHE   B 1 288 ? -18.57700 55.31900  20.89900  1.000 61.66715  ? 264  PHE   B CB  1 
ATOM   5129 C CG  . PHE   B 1 288 ? -19.62800 54.91800  19.89100  1.000 59.47836  ? 264  PHE   B CG  1 
ATOM   5130 C CD1 . PHE   B 1 288 ? -20.63800 54.02900  20.22600  1.000 63.63695  ? 264  PHE   B CD1 1 
ATOM   5131 C CD2 . PHE   B 1 288 ? -19.65300 55.49700  18.63400  1.000 65.41148  ? 264  PHE   B CD2 1 
ATOM   5132 C CE1 . PHE   B 1 288 ? -21.61100 53.67900  19.31000  1.000 59.24443  ? 264  PHE   B CE1 1 
ATOM   5133 C CE2 . PHE   B 1 288 ? -20.63000 55.15500  17.71300  1.000 60.74562  ? 264  PHE   B CE2 1 
ATOM   5134 C CZ  . PHE   B 1 288 ? -21.61000 54.24500  18.05500  1.000 53.07856  ? 264  PHE   B CZ  1 
ATOM   5135 N N   . CYS   B 1 289 ? -17.64900 54.79700  24.46000  1.000 56.51258  ? 265  CYS   B N   1 
ATOM   5136 C CA  . CYS   B 1 289 ? -16.51000 54.90300  25.37000  1.000 57.89824  ? 265  CYS   B CA  1 
ATOM   5137 C C   . CYS   B 1 289 ? -16.09500 53.56700  25.97700  1.000 52.48283  ? 265  CYS   B C   1 
ATOM   5138 O O   . CYS   B 1 289 ? -14.89700 53.33500  26.17000  1.000 53.99746  ? 265  CYS   B O   1 
ATOM   5139 C CB  . CYS   B 1 289 ? -16.79800 55.89900  26.49700  1.000 57.19358  ? 265  CYS   B CB  1 
ATOM   5140 S SG  . CYS   B 1 289 ? -17.30000 57.54900  25.96700  1.000 57.50806  ? 265  CYS   B SG  1 
ATOM   5141 N N   . LEU   B 1 290 ? -17.04400 52.69000  26.30300  1.000 51.40155  ? 266  LEU   B N   1 
ATOM   5142 C CA  . LEU   B 1 290 ? -16.68700 51.36800  26.80700  1.000 50.94413  ? 266  LEU   B CA  1 
ATOM   5143 C C   . LEU   B 1 290 ? -15.87800 50.60600  25.76500  1.000 52.13701  ? 266  LEU   B C   1 
ATOM   5144 O O   . LEU   B 1 290 ? -15.97600 50.86200  24.56200  1.000 58.09426  ? 266  LEU   B O   1 
ATOM   5145 C CB  . LEU   B 1 290 ? -17.93700 50.57200  27.18200  1.000 50.30444  ? 266  LEU   B CB  1 
ATOM   5146 C CG  . LEU   B 1 290 ? -18.71900 50.98500  28.43100  1.000 50.99621  ? 266  LEU   B CG  1 
ATOM   5147 C CD1 . LEU   B 1 290 ? -19.89400 50.04600  28.66000  1.000 49.38962  ? 266  LEU   B CD1 1 
ATOM   5148 C CD2 . LEU   B 1 290 ? -17.80800 50.99400  29.64600  1.000 47.54253  ? 266  LEU   B CD2 1 
ATOM   5149 N N   . LYS   B 1 291 ? -15.06800 49.65600  26.24000  1.000 54.75919  ? 267  LYS   B N   1 
ATOM   5150 C CA  . LYS   B 1 291 ? -14.16300 48.93800  25.34600  1.000 48.90501  ? 267  LYS   B CA  1 
ATOM   5151 C C   . LYS   B 1 291 ? -14.93900 48.15000  24.29400  1.000 53.22611  ? 267  LYS   B C   1 
ATOM   5152 O O   . LYS   B 1 291 ? -14.75100 48.34300  23.08700  1.000 54.23133  ? 267  LYS   B O   1 
ATOM   5153 C CB  . LYS   B 1 291 ? -13.24500 48.01700  26.15300  1.000 35.67055  ? 267  LYS   B CB  1 
ATOM   5154 C CG  . LYS   B 1 291 ? -12.39500 47.08100  25.29900  1.000 35.92013  ? 267  LYS   B CG  1 
ATOM   5155 C CD  . LYS   B 1 291 ? -11.33400 46.38000  26.13200  1.000 46.25987  ? 267  LYS   B CD  1 
ATOM   5156 C CE  . LYS   B 1 291 ? -10.40100 45.52700  25.28100  1.000 37.87160  ? 267  LYS   B CE  1 
ATOM   5157 N NZ  . LYS   B 1 291 ? -11.00800 44.21400  24.92700  1.000 50.53778  ? 267  LYS   B NZ  1 
ATOM   5158 N N   . GLU   B 1 292 ? -15.83200 47.26200  24.73400  1.000 44.78068  ? 268  GLU   B N   1 
ATOM   5159 C CA  . GLU   B 1 292 ? -16.58200 46.46100  23.77700  1.000 45.22605  ? 268  GLU   B CA  1 
ATOM   5160 C C   . GLU   B 1 292 ? -17.58300 47.29500  22.98600  1.000 54.34203  ? 268  GLU   B C   1 
ATOM   5161 O O   . GLU   B 1 292 ? -18.01200 46.86400  21.90900  1.000 55.93871  ? 268  GLU   B O   1 
ATOM   5162 C CB  . GLU   B 1 292 ? -17.29100 45.31700  24.49300  1.000 41.40696  ? 268  GLU   B CB  1 
ATOM   5163 C CG  . GLU   B 1 292 ? -16.35800 44.28900  25.12200  1.000 41.53016  ? 268  GLU   B CG  1 
ATOM   5164 C CD  . GLU   B 1 292 ? -15.94500 43.18100  24.16300  1.000 49.36239  ? 268  GLU   B CD  1 
ATOM   5165 O OE1 . GLU   B 1 292 ? -16.84000 42.49400  23.62800  1.000 46.34554  ? 268  GLU   B OE1 1 
ATOM   5166 O OE2 . GLU   B 1 292 ? -14.72500 42.99000  23.95200  1.000 52.43816  ? 268  GLU   B OE2 1 
ATOM   5167 N N   . HIS   B 1 293 ? -17.97100 48.47000  23.49300  1.000 53.10518  ? 269  HIS   B N   1 
ATOM   5168 C CA  . HIS   B 1 293 ? -18.71000 49.41900  22.66300  1.000 53.64777  ? 269  HIS   B CA  1 
ATOM   5169 C C   . HIS   B 1 293 ? -17.84500 49.91800  21.51400  1.000 53.47167  ? 269  HIS   B C   1 
ATOM   5170 O O   . HIS   B 1 293 ? -18.27000 49.91400  20.35300  1.000 56.54582  ? 269  HIS   B O   1 
ATOM   5171 C CB  . HIS   B 1 293 ? -19.20700 50.60100  23.49700  1.000 53.30227  ? 269  HIS   B CB  1 
ATOM   5172 C CG  . HIS   B 1 293 ? -20.51600 50.35700  24.17800  1.000 54.58024  ? 269  HIS   B CG  1 
ATOM   5173 N ND1 . HIS   B 1 293 ? -20.71300 50.59200  25.52100  1.000 62.28995  ? 269  HIS   B ND1 1 
ATOM   5174 C CD2 . HIS   B 1 293 ? -21.69600 49.89800  23.70100  1.000 58.55923  ? 269  HIS   B CD2 1 
ATOM   5175 C CE1 . HIS   B 1 293 ? -21.96000 50.29500  25.84100  1.000 58.55964  ? 269  HIS   B CE1 1 
ATOM   5176 N NE2 . HIS   B 1 293 ? -22.57700 49.86800  24.75500  1.000 59.25230  ? 269  HIS   B NE2 1 
ATOM   5177 N N   . LYS   B 1 294 ? -16.62400 50.36200  21.82500  1.000 52.45708  ? 270  LYS   B N   1 
ATOM   5178 C CA  . LYS   B 1 294 ? -15.68400 50.75600  20.78200  1.000 52.98494  ? 270  LYS   B CA  1 
ATOM   5179 C C   . LYS   B 1 294 ? -15.43500 49.61500  19.80300  1.000 48.84667  ? 270  LYS   B C   1 
ATOM   5180 O O   . LYS   B 1 294 ? -15.14800 49.85700  18.62600  1.000 46.66349  ? 270  LYS   B O   1 
ATOM   5181 C CB  . LYS   B 1 294 ? -14.37200 51.22100  21.42000  1.000 47.71722  ? 270  LYS   B CB  1 
ATOM   5182 C CG  . LYS   B 1 294 ? -14.39600 52.65700  21.93900  1.000 46.79742  ? 270  LYS   B CG  1 
ATOM   5183 C CD  . LYS   B 1 294 ? -13.06100 53.04400  22.56800  1.000 53.99537  ? 270  LYS   B CD  1 
ATOM   5184 C CE  . LYS   B 1 294 ? -12.98100 54.53700  22.87200  1.000 53.17655  ? 270  LYS   B CE  1 
ATOM   5185 N NZ  . LYS   B 1 294 ? -12.60900 55.33900  21.67000  1.000 62.20146  ? 270  LYS   B NZ  1 
ATOM   5186 N N   . ALA   B 1 295 ? -15.54900 48.36800  20.27100  1.000 48.37842  ? 271  ALA   B N   1 
ATOM   5187 C CA  . ALA   B 1 295 ? -15.40600 47.22100  19.38000  1.000 48.55842  ? 271  ALA   B CA  1 
ATOM   5188 C C   . ALA   B 1 295 ? -16.56600 47.13500  18.39500  1.000 53.99517  ? 271  ALA   B C   1 
ATOM   5189 O O   . ALA   B 1 295 ? -16.36800 46.79300  17.22100  1.000 47.00387  ? 271  ALA   B O   1 
ATOM   5190 C CB  . ALA   B 1 295 ? -15.30100 45.93400  20.19800  1.000 40.59175  ? 271  ALA   B CB  1 
ATOM   5191 N N   . LEU   B 1 296 ? -17.78600 47.43900  18.85100  1.000 49.17045  ? 272  LEU   B N   1 
ATOM   5192 C CA  . LEU   B 1 296 ? -18.93700 47.38800  17.95600  1.000 41.95234  ? 272  LEU   B CA  1 
ATOM   5193 C C   . LEU   B 1 296 ? -18.87500 48.48400  16.90000  1.000 46.36090  ? 272  LEU   B C   1 
ATOM   5194 O O   . LEU   B 1 296 ? -19.31500 48.27300  15.76200  1.000 47.95018  ? 272  LEU   B O   1 
ATOM   5195 C CB  . LEU   B 1 296 ? -20.23600 47.48600  18.75500  1.000 45.85865  ? 272  LEU   B CB  1 
ATOM   5196 C CG  . LEU   B 1 296 ? -20.55700 46.33900  19.71800  1.000 42.75775  ? 272  LEU   B CG  1 
ATOM   5197 C CD1 . LEU   B 1 296 ? -21.87800 46.59500  20.41700  1.000 43.84869  ? 272  LEU   B CD1 1 
ATOM   5198 C CD2 . LEU   B 1 296 ? -20.59500 45.00600  18.99200  1.000 40.45770  ? 272  LEU   B CD2 1 
ATOM   5199 N N   . LYS   B 1 297 ? -18.33500 49.65500  17.24700  1.000 45.97291  ? 273  LYS   B N   1 
ATOM   5200 C CA  . LYS   B 1 297 ? -18.09500 50.67500  16.23200  1.000 48.41732  ? 273  LYS   B CA  1 
ATOM   5201 C C   . LYS   B 1 297 ? -17.02000 50.23900  15.24300  1.000 48.14436  ? 273  LYS   B C   1 
ATOM   5202 O O   . LYS   B 1 297 ? -17.01400 50.71200  14.10200  1.000 47.33543  ? 273  LYS   B O   1 
ATOM   5203 C CB  . LYS   B 1 297 ? -17.71400 52.00300  16.89400  1.000 46.23013  ? 273  LYS   B CB  1 
ATOM   5204 C CG  . LYS   B 1 297 ? -17.57600 53.17100  15.92200  1.000 46.40319  ? 273  LYS   B CG  1 
ATOM   5205 C CD  . LYS   B 1 297 ? -17.09400 54.43300  16.61700  1.000 49.07375  ? 273  LYS   B CD  1 
ATOM   5206 C CE  . LYS   B 1 297 ? -15.86900 55.02200  15.93800  1.000 54.27473  ? 273  LYS   B CE  1 
ATOM   5207 N NZ  . LYS   B 1 297 ? -14.90400 55.56400  16.94200  1.000 69.70977  ? 273  LYS   B NZ  1 
ATOM   5208 N N   . THR   B 1 298 ? -16.11800 49.34400  15.65000  1.000 42.03081  ? 274  THR   B N   1 
ATOM   5209 C CA  . THR   B 1 298 ? -15.18200 48.76000  14.69700  1.000 43.29919  ? 274  THR   B CA  1 
ATOM   5210 C C   . THR   B 1 298 ? -15.89900 47.79700  13.76000  1.000 46.82066  ? 274  THR   B C   1 
ATOM   5211 O O   . THR   B 1 298 ? -15.71300 47.85100  12.53800  1.000 43.54919  ? 274  THR   B O   1 
ATOM   5212 C CB  . THR   B 1 298 ? -14.04400 48.05700  15.43600  1.000 45.04514  ? 274  THR   B CB  1 
ATOM   5213 O OG1 . THR   B 1 298 ? -13.21000 49.03600  16.06900  1.000 50.76105  ? 274  THR   B OG1 1 
ATOM   5214 C CG2 . THR   B 1 298 ? -13.20500 47.23100  14.46800  1.000 44.37648  ? 274  THR   B CG2 1 
ATOM   5215 N N   . LEU   B 1 299 ? -16.72700 46.90500  14.31600  1.000 46.26788  ? 275  LEU   B N   1 
ATOM   5216 C CA  . LEU   B 1 299 ? -17.57300 46.06400  13.47500  1.000 40.81663  ? 275  LEU   B CA  1 
ATOM   5217 C C   . LEU   B 1 299 ? -18.41700 46.91100  12.53600  1.000 40.13956  ? 275  LEU   B C   1 
ATOM   5218 O O   . LEU   B 1 299 ? -18.66400 46.52400  11.38800  1.000 42.19639  ? 275  LEU   B O   1 
ATOM   5219 C CB  . LEU   B 1 299 ? -18.46800 45.17400  14.33700  1.000 36.35982  ? 275  LEU   B CB  1 
ATOM   5220 C CG  . LEU   B 1 299 ? -17.82400 43.97400  15.02400  1.000 36.43791  ? 275  LEU   B CG  1 
ATOM   5221 C CD1 . LEU   B 1 299 ? -18.86600 43.19200  15.78700  1.000 38.82103  ? 275  LEU   B CD1 1 
ATOM   5222 C CD2 . LEU   B 1 299 ? -17.15600 43.08300  14.00500  1.000 39.18877  ? 275  LEU   B CD2 1 
ATOM   5223 N N   . GLY   B 1 300 ? -18.86300 48.07700  13.00600  1.000 39.31004  ? 276  GLY   B N   1 
ATOM   5224 C CA  . GLY   B 1 300 ? -19.59100 48.98100  12.13200  1.000 42.22981  ? 276  GLY   B CA  1 
ATOM   5225 C C   . GLY   B 1 300 ? -18.73300 49.51400  11.00100  1.000 41.58135  ? 276  GLY   B C   1 
ATOM   5226 O O   . GLY   B 1 300 ? -19.17700 49.58000  9.85200   1.000 42.16864  ? 276  GLY   B O   1 
ATOM   5227 N N   . ILE   B 1 301 ? -17.49000 49.89300  11.30700  1.000 43.97215  ? 277  ILE   B N   1 
ATOM   5228 C CA  . ILE   B 1 301 ? -16.60900 50.44500  10.28100  1.000 43.30439  ? 277  ILE   B CA  1 
ATOM   5229 C C   . ILE   B 1 301 ? -16.25300 49.38200  9.24800   1.000 45.21479  ? 277  ILE   B C   1 
ATOM   5230 O O   . ILE   B 1 301 ? -16.11800 49.68000  8.05500   1.000 46.59908  ? 277  ILE   B O   1 
ATOM   5231 C CB  . ILE   B 1 301 ? -15.35800 51.06200  10.93200  1.000 40.56303  ? 277  ILE   B CB  1 
ATOM   5232 C CG1 . ILE   B 1 301 ? -15.74100 52.31000  11.72700  1.000 44.65877  ? 277  ILE   B CG1 1 
ATOM   5233 C CG2 . ILE   B 1 301 ? -14.31500 51.40800  9.88800   1.000 41.74767  ? 277  ILE   B CG2 1 
ATOM   5234 C CD1 . ILE   B 1 301 ? -14.62100 52.85300  12.57500  1.000 52.70927  ? 277  ILE   B CD1 1 
ATOM   5235 N N   . ILE   B 1 302 ? -16.10500 48.12800  9.68100   1.000 41.82147  ? 278  ILE   B N   1 
ATOM   5236 C CA  . ILE   B 1 302 ? -15.91700 47.03300  8.73100   1.000 40.00948  ? 278  ILE   B CA  1 
ATOM   5237 C C   . ILE   B 1 302 ? -17.07000 46.99400  7.73500   1.000 43.05101  ? 278  ILE   B C   1 
ATOM   5238 O O   . ILE   B 1 302 ? -16.86100 46.96400  6.51600   1.000 44.82804  ? 278  ILE   B O   1 
ATOM   5239 C CB  . ILE   B 1 302 ? -15.77100 45.69400  9.47400   1.000 38.51241  ? 278  ILE   B CB  1 
ATOM   5240 C CG1 . ILE   B 1 302 ? -14.41800 45.62000  10.17100  1.000 42.75266  ? 278  ILE   B CG1 1 
ATOM   5241 C CG2 . ILE   B 1 302 ? -15.88500 44.54100  8.50400   1.000 38.52756  ? 278  ILE   B CG2 1 
ATOM   5242 C CD1 . ILE   B 1 302 ? -13.26500 45.70900  9.22600   1.000 40.04456  ? 278  ILE   B CD1 1 
ATOM   5243 N N   . MET   B 1 303 ? -18.30700 47.00200  8.24000   1.000 39.62671  ? 279  MET   B N   1 
ATOM   5244 C CA  . MET   B 1 303 ? -19.47100 47.01600  7.35900   1.000 39.10677  ? 279  MET   B CA  1 
ATOM   5245 C C   . MET   B 1 303 ? -19.50700 48.29000  6.52500   1.000 41.46286  ? 279  MET   B C   1 
ATOM   5246 O O   . MET   B 1 303 ? -19.72600 48.24600  5.30800   1.000 38.44653  ? 279  MET   B O   1 
ATOM   5247 C CB  . MET   B 1 303 ? -20.75500 46.88400  8.18000   1.000 38.32871  ? 279  MET   B CB  1 
ATOM   5248 C CG  . MET   B 1 303 ? -20.88600 45.58700  8.96100   1.000 45.47321  ? 279  MET   B CG  1 
ATOM   5249 S SD  . MET   B 1 303 ? -21.99300 45.71500  10.38300  1.000 43.77206  ? 279  MET   B SD  1 
ATOM   5250 C CE  . MET   B 1 303 ? -21.88300 44.05900  11.05200  1.000 33.98893  ? 279  MET   B CE  1 
ATOM   5251 N N   . GLY   B 1 304 ? -19.29300 49.43600  7.16900   1.000 41.86936  ? 280  GLY   B N   1 
ATOM   5252 C CA  . GLY   B 1 304 ? -19.36200 50.73100  6.52100   1.000 41.44286  ? 280  GLY   B CA  1 
ATOM   5253 C C   . GLY   B 1 304 ? -18.48900 50.87400  5.29300   1.000 45.47561  ? 280  GLY   B C   1 
ATOM   5254 O O   . GLY   B 1 304 ? -19.00000 51.12000  4.19800   1.000 45.53792  ? 280  GLY   B O   1 
ATOM   5255 N N   . THR   B 1 305 ? -17.17100 50.71900  5.45600   1.000 47.19845  ? 281  THR   B N   1 
ATOM   5256 C CA  . THR   B 1 305 ? -16.27000 50.83700  4.31300   1.000 48.82478  ? 281  THR   B CA  1 
ATOM   5257 C C   . THR   B 1 305 ? -16.59600 49.81500  3.23100   1.000 46.50526  ? 281  THR   B C   1 
ATOM   5258 O O   . THR   B 1 305 ? -16.38100 50.08300  2.04500   1.000 49.49810  ? 281  THR   B O   1 
ATOM   5259 C CB  . THR   B 1 305 ? -14.81300 50.68300  4.76000   1.000 50.79290  ? 281  THR   B CB  1 
ATOM   5260 O OG1 . THR   B 1 305 ? -14.59100 49.35000  5.24100   1.000 52.49758  ? 281  THR   B OG1 1 
ATOM   5261 C CG2 . THR   B 1 305 ? -14.48400 51.67700  5.86200   1.000 40.17978  ? 281  THR   B CG2 1 
ATOM   5262 N N   . PHE   B 1 306 ? -17.11800 48.64700  3.61300   1.000 44.85654  ? 282  PHE   B N   1 
ATOM   5263 C CA  . PHE   B 1 306 ? -17.48300 47.63900  2.62100   1.000 41.69086  ? 282  PHE   B CA  1 
ATOM   5264 C C   . PHE   B 1 306 ? -18.60500 48.13800  1.72100   1.000 46.12624  ? 282  PHE   B C   1 
ATOM   5265 O O   . PHE   B 1 306 ? -18.51400 48.05500  0.49000   1.000 49.92834  ? 282  PHE   B O   1 
ATOM   5266 C CB  . PHE   B 1 306 ? -17.89300 46.34300  3.31600   1.000 38.14427  ? 282  PHE   B CB  1 
ATOM   5267 C CG  . PHE   B 1 306 ? -18.36400 45.26900  2.37400   1.000 36.45658  ? 282  PHE   B CG  1 
ATOM   5268 C CD1 . PHE   B 1 306 ? -19.69700 45.18500  2.00300   1.000 42.08534  ? 282  PHE   B CD1 1 
ATOM   5269 C CD2 . PHE   B 1 306 ? -17.48000 44.32900  1.87900   1.000 34.86041  ? 282  PHE   B CD2 1 
ATOM   5270 C CE1 . PHE   B 1 306 ? -20.13000 44.19700  1.14500   1.000 39.01518  ? 282  PHE   B CE1 1 
ATOM   5271 C CE2 . PHE   B 1 306 ? -17.91100 43.33500  1.02400   1.000 36.78494  ? 282  PHE   B CE2 1 
ATOM   5272 C CZ  . PHE   B 1 306 ? -19.23700 43.26900  0.65700   1.000 35.49101  ? 282  PHE   B CZ  1 
ATOM   5273 N N   . THR   B 1 307 ? -19.68300 48.64400  2.31900   1.000 44.08165  ? 283  THR   B N   1 
ATOM   5274 C CA  . THR   B 1 307 ? -20.79300 49.14200  1.51700   1.000 43.88396  ? 283  THR   B CA  1 
ATOM   5275 C C   . THR   B 1 307 ? -20.35800 50.32200  0.66100   1.000 43.49499  ? 283  THR   B C   1 
ATOM   5276 O O   . THR   B 1 307 ? -20.74700 50.42700  -0.50600  1.000 49.65128  ? 283  THR   B O   1 
ATOM   5277 C CB  . THR   B 1 307 ? -21.96400 49.53400  2.41700   1.000 45.39325  ? 283  THR   B CB  1 
ATOM   5278 O OG1 . THR   B 1 307 ? -21.59800 50.66800  3.21100   1.000 52.65175  ? 283  THR   B OG1 1 
ATOM   5279 C CG2 . THR   B 1 307 ? -22.32000 48.38600  3.34200   1.000 39.48097  ? 283  THR   B CG2 1 
ATOM   5280 N N   . LEU   B 1 308 ? -19.52600 51.20700  1.21300   1.000 42.55178  ? 284  LEU   B N   1 
ATOM   5281 C CA  . LEU   B 1 308 ? -19.10700 52.38700  0.46600   1.000 48.11453  ? 284  LEU   B CA  1 
ATOM   5282 C C   . LEU   B 1 308 ? -18.24500 52.02600  -0.73900  1.000 47.56823  ? 284  LEU   B C   1 
ATOM   5283 O O   . LEU   B 1 308 ? -18.25400 52.75200  -1.73800  1.000 47.26161  ? 284  LEU   B O   1 
ATOM   5284 C CB  . LEU   B 1 308 ? -18.35200 53.35000  1.38200   1.000 54.11028  ? 284  LEU   B CB  1 
ATOM   5285 C CG  . LEU   B 1 308 ? -19.11400 53.89300  2.59700   1.000 58.94238  ? 284  LEU   B CG  1 
ATOM   5286 C CD1 . LEU   B 1 308 ? -18.31400 54.98500  3.29500   1.000 57.88178  ? 284  LEU   B CD1 1 
ATOM   5287 C CD2 . LEU   B 1 308 ? -20.50200 54.39300  2.21600   1.000 49.65691  ? 284  LEU   B CD2 1 
ATOM   5288 N N   . CYS   B 1 309 ? -17.49800 50.92200  -0.67200  1.000 48.57586  ? 285  CYS   B N   1 
ATOM   5289 C CA  . CYS   B 1 309 ? -16.61600 50.55900  -1.77800  1.000 52.98365  ? 285  CYS   B CA  1 
ATOM   5290 C C   . CYS   B 1 309 ? -17.33800 49.78000  -2.87000  1.000 51.41915  ? 285  CYS   B C   1 
ATOM   5291 O O   . CYS   B 1 309 ? -16.91200 49.81400  -4.03100  1.000 57.10784  ? 285  CYS   B O   1 
ATOM   5292 C CB  . CYS   B 1 309 ? -15.42300 49.74000  -1.27300  1.000 54.43623  ? 285  CYS   B CB  1 
ATOM   5293 S SG  . CYS   B 1 309 ? -14.33500 50.58200  -0.10300  1.000 58.11465  ? 285  CYS   B SG  1 
ATOM   5294 N N   . TRP   B 1 310 ? -18.41200 49.07000  -2.52700  1.000 43.44434  ? 286  TRP   B N   1 
ATOM   5295 C CA  . TRP   B 1 310 ? -19.12400 48.25700  -3.50200  1.000 43.60081  ? 286  TRP   B CA  1 
ATOM   5296 C C   . TRP   B 1 310 ? -20.42800 48.88100  -3.97600  1.000 44.46839  ? 286  TRP   B C   1 
ATOM   5297 O O   . TRP   B 1 310 ? -20.92600 48.50000  -5.04100  1.000 44.28576  ? 286  TRP   B O   1 
ATOM   5298 C CB  . TRP   B 1 310 ? -19.42400 46.87400  -2.91900  1.000 42.55651  ? 286  TRP   B CB  1 
ATOM   5299 C CG  . TRP   B 1 310 ? -18.26200 45.94300  -2.92800  1.000 40.56040  ? 286  TRP   B CG  1 
ATOM   5300 C CD1 . TRP   B 1 310 ? -17.61700 45.43400  -1.84200  1.000 44.90927  ? 286  TRP   B CD1 1 
ATOM   5301 C CD2 . TRP   B 1 310 ? -17.61000 45.39200  -4.07800  1.000 46.91258  ? 286  TRP   B CD2 1 
ATOM   5302 N NE1 . TRP   B 1 310 ? -16.60000 44.60100  -2.24300  1.000 50.76409  ? 286  TRP   B NE1 1 
ATOM   5303 C CE2 . TRP   B 1 310 ? -16.57600 44.55800  -3.61200  1.000 46.67993  ? 286  TRP   B CE2 1 
ATOM   5304 C CE3 . TRP   B 1 310 ? -17.79900 45.52300  -5.45600  1.000 48.22663  ? 286  TRP   B CE3 1 
ATOM   5305 C CZ2 . TRP   B 1 310 ? -15.73500 43.85900  -4.47300  1.000 44.48233  ? 286  TRP   B CZ2 1 
ATOM   5306 C CZ3 . TRP   B 1 310 ? -16.96500 44.83000  -6.30800  1.000 46.64593  ? 286  TRP   B CZ3 1 
ATOM   5307 C CH2 . TRP   B 1 310 ? -15.94400 44.01000  -5.81400  1.000 49.88094  ? 286  TRP   B CH2 1 
ATOM   5308 N N   . LEU   B 1 311 ? -20.99700 49.81300  -3.21800  1.000 49.43191  ? 287  LEU   B N   1 
ATOM   5309 C CA  . LEU   B 1 311 ? -22.26300 50.40800  -3.63100  1.000 53.58154  ? 287  LEU   B CA  1 
ATOM   5310 C C   . LEU   B 1 311 ? -22.15000 51.19800  -4.92900  1.000 55.04528  ? 287  LEU   B C   1 
ATOM   5311 O O   . LEU   B 1 311 ? -23.04600 51.05200  -5.77900  1.000 56.32489  ? 287  LEU   B O   1 
ATOM   5312 C CB  . LEU   B 1 311 ? -22.82600 51.28100  -2.50400  1.000 48.50076  ? 287  LEU   B CB  1 
ATOM   5313 C CG  . LEU   B 1 311 ? -24.30200 51.63400  -2.63500  1.000 48.88688  ? 287  LEU   B CG  1 
ATOM   5314 C CD1 . LEU   B 1 311 ? -25.13400 50.37200  -2.82100  1.000 49.54788  ? 287  LEU   B CD1 1 
ATOM   5315 C CD2 . LEU   B 1 311 ? -24.75900 52.41300  -1.41700  1.000 46.21136  ? 287  LEU   B CD2 1 
ATOM   5316 N N   . PRO   B 1 312 ? -21.12000 52.03100  -5.15700  1.000 53.11783  ? 288  PRO   B N   1 
ATOM   5317 C CA  . PRO   B 1 312 ? -21.00800 52.67900  -6.47700  1.000 54.27210  ? 288  PRO   B CA  1 
ATOM   5318 C C   . PRO   B 1 312 ? -20.98700 51.68900  -7.62600  1.000 52.08600  ? 288  PRO   B C   1 
ATOM   5319 O O   . PRO   B 1 312 ? -21.65200 51.91700  -8.64100  1.000 53.24610  ? 288  PRO   B O   1 
ATOM   5320 C CB  . PRO   B 1 312 ? -19.69200 53.46300  -6.37300  1.000 49.66675  ? 288  PRO   B CB  1 
ATOM   5321 C CG  . PRO   B 1 312 ? -19.51600 53.71000  -4.92500  1.000 50.56821  ? 288  PRO   B CG  1 
ATOM   5322 C CD  . PRO   B 1 312 ? -20.06200 52.49400  -4.24100  1.000 50.65945  ? 288  PRO   B CD  1 
ATOM   5323 N N   . PHE   B 1 313 ? -20.25600 50.58200  -7.48700  1.000 49.84538  ? 289  PHE   B N   1 
ATOM   5324 C CA  . PHE   B 1 313 ? -20.25700 49.55500  -8.52500  1.000 47.90914  ? 289  PHE   B CA  1 
ATOM   5325 C C   . PHE   B 1 313 ? -21.65300 48.97300  -8.72500  1.000 53.94345  ? 289  PHE   B C   1 
ATOM   5326 O O   . PHE   B 1 313 ? -22.11500 48.81400  -9.86000  1.000 57.03038  ? 289  PHE   B O   1 
ATOM   5327 C CB  . PHE   B 1 313 ? -19.25800 48.45700  -8.16200  1.000 47.90505  ? 289  PHE   B CB  1 
ATOM   5328 C CG  . PHE   B 1 313 ? -19.38100 47.21300  -8.99700  1.000 48.38810  ? 289  PHE   B CG  1 
ATOM   5329 C CD1 . PHE   B 1 313 ? -18.75500 47.12100  -10.22900 1.000 48.64122  ? 289  PHE   B CD1 1 
ATOM   5330 C CD2 . PHE   B 1 313 ? -20.11200 46.12700  -8.54100  1.000 43.76991  ? 289  PHE   B CD2 1 
ATOM   5331 C CE1 . PHE   B 1 313 ? -18.85800 45.96900  -10.99100 1.000 47.04742  ? 289  PHE   B CE1 1 
ATOM   5332 C CE2 . PHE   B 1 313 ? -20.22300 44.97600  -9.29900  1.000 46.53404  ? 289  PHE   B CE2 1 
ATOM   5333 C CZ  . PHE   B 1 313 ? -19.59400 44.89600  -10.52400 1.000 47.93335  ? 289  PHE   B CZ  1 
ATOM   5334 N N   . PHE   B 1 314 ? -22.34400 48.64900  -7.62800  1.000 55.81766  ? 290  PHE   B N   1 
ATOM   5335 C CA  . PHE   B 1 314 ? -23.65300 48.01500  -7.73100  1.000 52.67123  ? 290  PHE   B CA  1 
ATOM   5336 C C   . PHE   B 1 314 ? -24.77500 49.00200  -8.03400  1.000 52.64638  ? 290  PHE   B C   1 
ATOM   5337 O O   . PHE   B 1 314 ? -25.82300 48.58100  -8.53600  1.000 51.98811  ? 290  PHE   B O   1 
ATOM   5338 C CB  . PHE   B 1 314 ? -23.98100 47.24500  -6.44700  1.000 45.87596  ? 290  PHE   B CB  1 
ATOM   5339 C CG  . PHE   B 1 314 ? -23.30600 45.90100  -6.34800  1.000 42.86526  ? 290  PHE   B CG  1 
ATOM   5340 C CD1 . PHE   B 1 314 ? -23.75200 44.82900  -7.10300  1.000 43.34020  ? 290  PHE   B CD1 1 
ATOM   5341 C CD2 . PHE   B 1 314 ? -22.23800 45.70400  -5.48600  1.000 46.35164  ? 290  PHE   B CD2 1 
ATOM   5342 C CE1 . PHE   B 1 314 ? -23.13600 43.58900  -7.01400  1.000 41.96427  ? 290  PHE   B CE1 1 
ATOM   5343 C CE2 . PHE   B 1 314 ? -21.62000 44.46400  -5.38900  1.000 45.69525  ? 290  PHE   B CE2 1 
ATOM   5344 C CZ  . PHE   B 1 314 ? -22.07200 43.40600  -6.15500  1.000 45.04141  ? 290  PHE   B CZ  1 
ATOM   5345 N N   . ILE   B 1 315 ? -24.59500 50.29200  -7.73500  1.000 54.03674  ? 291  ILE   B N   1 
ATOM   5346 C CA  . ILE   B 1 315 ? -25.61100 51.28000  -8.09600  1.000 56.35772  ? 291  ILE   B CA  1 
ATOM   5347 C C   . ILE   B 1 315 ? -25.58200 51.54900  -9.59600  1.000 70.51759  ? 291  ILE   B C   1 
ATOM   5348 O O   . ILE   B 1 315 ? -26.61700 51.50600  -10.27300 1.000 72.24109  ? 291  ILE   B O   1 
ATOM   5349 C CB  . ILE   B 1 315 ? -25.42500 52.58700  -7.30100  1.000 50.05312  ? 291  ILE   B CB  1 
ATOM   5350 C CG1 . ILE   B 1 315 ? -25.91400 52.44800  -5.86300  1.000 55.19121  ? 291  ILE   B CG1 1 
ATOM   5351 C CG2 . ILE   B 1 315 ? -26.15600 53.74100  -7.96900  1.000 46.41760  ? 291  ILE   B CG2 1 
ATOM   5352 C CD1 . ILE   B 1 315 ? -25.71700 53.72000  -5.06100  1.000 49.06488  ? 291  ILE   B CD1 1 
ATOM   5353 N N   . VAL   B 1 316 ? -24.39800 51.82500  -10.14200 1.000 66.63703  ? 292  VAL   B N   1 
ATOM   5354 C CA  . VAL   B 1 316 ? -24.30600 52.29000  -11.52100 1.000 65.96695  ? 292  VAL   B CA  1 
ATOM   5355 C C   . VAL   B 1 316 ? -24.35100 51.10200  -12.47000 1.000 73.60925  ? 292  VAL   B C   1 
ATOM   5356 O O   . VAL   B 1 316 ? -24.04700 51.23800  -13.65900 1.000 80.86129  ? 292  VAL   B O   1 
ATOM   5357 C CB  . VAL   B 1 316 ? -23.03400 53.12400  -11.76400 1.000 63.80119  ? 292  VAL   B CB  1 
ATOM   5358 C CG1 . VAL   B 1 316 ? -23.00600 54.35100  -10.85200 1.000 59.34972  ? 292  VAL   B CG1 1 
ATOM   5359 C CG2 . VAL   B 1 316 ? -21.78500 52.26500  -11.63500 1.000 62.69294  ? 292  VAL   B CG2 1 
ATOM   5360 N N   . ASN   B 1 317 ? -24.71400 49.92500  -11.95600 1.000 69.79640  ? 293  ASN   B N   1 
ATOM   5361 C CA  . ASN   B 1 317 ? -24.93500 48.77500  -12.81800 1.000 72.77338  ? 293  ASN   B CA  1 
ATOM   5362 C C   . ASN   B 1 317 ? -26.39900 48.37600  -12.93300 1.000 73.55067  ? 293  ASN   B C   1 
ATOM   5363 O O   . ASN   B 1 317 ? -26.76900 47.75100  -13.92900 1.000 84.65630  ? 293  ASN   B O   1 
ATOM   5364 C CB  . ASN   B 1 317 ? -24.06300 47.58100  -12.36700 1.000 69.85455  ? 293  ASN   B CB  1 
ATOM   5365 C CG  . ASN   B 1 317 ? -24.65000 46.76000  -11.20300 1.000 73.85504  ? 293  ASN   B CG  1 
ATOM   5366 O OD1 . ASN   B 1 317 ? -25.83300 46.82400  -10.86900 1.000 77.42698  ? 293  ASN   B OD1 1 
ATOM   5367 N ND2 . ASN   B 1 317 ? -23.78900 45.95000  -10.59600 1.000 66.68023  ? 293  ASN   B ND2 1 
ATOM   5368 N N   . ILE   B 1 318 ? -27.23700 48.71900  -11.95300 1.000 74.79021  ? 294  ILE   B N   1 
ATOM   5369 C CA  . ILE   B 1 318 ? -28.67200 48.52700  -12.13400 1.000 80.36825  ? 294  ILE   B CA  1 
ATOM   5370 C C   . ILE   B 1 318 ? -29.27700 49.71200  -12.88000 1.000 85.13206  ? 294  ILE   B C   1 
ATOM   5371 O O   . ILE   B 1 318 ? -30.30900 49.56600  -13.54600 1.000 87.60730  ? 294  ILE   B O   1 
ATOM   5372 C CB  . ILE   B 1 318 ? -29.38000 48.27400  -10.78700 1.000 63.12057  ? 294  ILE   B CB  1 
ATOM   5373 C CG1 . ILE   B 1 318 ? -29.11800 49.40600  -9.78800  1.000 63.23185  ? 294  ILE   B CG1 1 
ATOM   5374 C CG2 . ILE   B 1 318 ? -28.97600 46.92300  -10.21200 1.000 60.16943  ? 294  ILE   B CG2 1 
ATOM   5375 C CD1 . ILE   B 1 318 ? -30.13800 50.52800  -9.82800  1.000 62.82018  ? 294  ILE   B CD1 1 
ATOM   5376 N N   . VAL   B 1 319 ? -28.66100 50.89400  -12.78800 1.000 81.02220  ? 295  VAL   B N   1 
ATOM   5377 C CA  . VAL   B 1 319 ? -29.10000 51.99900  -13.63200 1.000 84.39455  ? 295  VAL   B CA  1 
ATOM   5378 C C   . VAL   B 1 319 ? -28.61900 51.78100  -15.06000 1.000 92.05104  ? 295  VAL   B C   1 
ATOM   5379 O O   . VAL   B 1 319 ? -29.33000 52.08600  -16.02600 1.000 90.11818  ? 295  VAL   B O   1 
ATOM   5380 C CB  . VAL   B 1 319 ? -28.62500 53.35300  -13.06500 1.000 78.48096  ? 295  VAL   B CB  1 
ATOM   5381 C CG1 . VAL   B 1 319 ? -29.09800 53.52900  -11.63000 1.000 81.99450  ? 295  VAL   B CG1 1 
ATOM   5382 C CG2 . VAL   B 1 319 ? -27.11900 53.50500  -13.16800 1.000 77.02665  ? 295  VAL   B CG2 1 
ATOM   5383 N N   . HIS   B 1 320 ? -27.42400 51.20400  -15.20900 1.000 93.18138  ? 296  HIS   B N   1 
ATOM   5384 C CA  . HIS   B 1 320 ? -26.84300 50.93300  -16.51700 1.000 90.87622  ? 296  HIS   B CA  1 
ATOM   5385 C C   . HIS   B 1 320 ? -27.67800 49.93900  -17.31400 1.000 93.87934  ? 296  HIS   B C   1 
ATOM   5386 O O   . HIS   B 1 320 ? -27.55000 49.88000  -18.54200 1.000 96.93910  ? 296  HIS   B O   1 
ATOM   5387 C CB  . HIS   B 1 320 ? -25.40600 50.43400  -16.31300 1.000 89.61572  ? 296  HIS   B CB  1 
ATOM   5388 C CG  . HIS   B 1 320 ? -24.79500 49.77200  -17.51000 1.000 99.16942  ? 296  HIS   B CG  1 
ATOM   5389 N ND1 . HIS   B 1 320 ? -24.78600 48.40400  -17.68100 1.000 96.52996  ? 296  HIS   B ND1 1 
ATOM   5390 C CD2 . HIS   B 1 320 ? -24.12900 50.28800  -18.57000 1.000 98.55692  ? 296  HIS   B CD2 1 
ATOM   5391 C CE1 . HIS   B 1 320 ? -24.16300 48.10700  -18.80700 1.000 99.62428  ? 296  HIS   B CE1 1 
ATOM   5392 N NE2 . HIS   B 1 320 ? -23.75200 49.23200  -19.36400 1.000 100.58599 ? 296  HIS   B NE2 1 
ATOM   5393 N N   . VAL   B 1 321 ? -28.54900 49.17700  -16.64900 1.000 87.27212  ? 297  VAL   B N   1 
ATOM   5394 C CA  . VAL   B 1 321 ? -29.43700 48.25000  -17.33700 1.000 87.48449  ? 297  VAL   B CA  1 
ATOM   5395 C C   . VAL   B 1 321 ? -30.85700 48.80700  -17.39300 1.000 89.69914  ? 297  VAL   B C   1 
ATOM   5396 O O   . VAL   B 1 321 ? -31.59400 48.53500  -18.34700 1.000 95.37442  ? 297  VAL   B O   1 
ATOM   5397 C CB  . VAL   B 1 321 ? -29.40800 46.85200  -16.68400 1.000 76.93354  ? 297  VAL   B CB  1 
ATOM   5398 C CG1 . VAL   B 1 321 ? -27.97400 46.38900  -16.48500 1.000 76.99147  ? 297  VAL   B CG1 1 
ATOM   5399 C CG2 . VAL   B 1 321 ? -30.15100 46.85200  -15.36800 1.000 73.61811  ? 297  VAL   B CG2 1 
ATOM   5400 N N   . ILE   B 1 322 ? -31.25800 49.59900  -16.39600 1.000 85.06057  ? 298  ILE   B N   1 
ATOM   5401 C CA  . ILE   B 1 322 ? -32.61700 50.13600  -16.42800 1.000 95.33240  ? 298  ILE   B CA  1 
ATOM   5402 C C   . ILE   B 1 322 ? -32.71100 51.28700  -17.42500 1.000 96.22307  ? 298  ILE   B C   1 
ATOM   5403 O O   . ILE   B 1 322 ? -33.70100 51.41000  -18.15400 1.000 101.57428 ? 298  ILE   B O   1 
ATOM   5404 C CB  . ILE   B 1 322 ? -33.08500 50.54100  -15.01400 1.000 96.75200  ? 298  ILE   B CB  1 
ATOM   5405 C CG1 . ILE   B 1 322 ? -34.60400 50.69900  -14.97400 1.000 91.45510  ? 298  ILE   B CG1 1 
ATOM   5406 C CG2 . ILE   B 1 322 ? -32.44100 51.83300  -14.54400 1.000 96.53210  ? 298  ILE   B CG2 1 
ATOM   5407 C CD1 . ILE   B 1 322 ? -35.15600 50.76400  -13.56900 1.000 92.52819  ? 298  ILE   B CD1 1 
ATOM   5408 N N   . GLN   B 1 323 ? -31.68200 52.12700  -17.48800 1.000 91.58909  ? 299  GLN   B N   1 
ATOM   5409 C CA  . GLN   B 1 323 ? -31.50700 53.09600  -18.55700 1.000 95.69336  ? 299  GLN   B CA  1 
ATOM   5410 C C   . GLN   B 1 323 ? -30.34100 52.63400  -19.41400 1.000 98.47270  ? 299  GLN   B C   1 
ATOM   5411 O O   . GLN   B 1 323 ? -29.29800 52.23800  -18.88200 1.000 102.37345 ? 299  GLN   B O   1 
ATOM   5412 C CB  . GLN   B 1 323 ? -31.24600 54.50000  -18.00500 1.000 88.90351  ? 299  GLN   B CB  1 
ATOM   5413 C CG  . GLN   B 1 323 ? -32.50500 55.29000  -17.69400 1.000 96.33316  ? 299  GLN   B CG  1 
ATOM   5414 C CD  . GLN   B 1 323 ? -33.21500 54.78900  -16.45300 1.000 100.48142 ? 299  GLN   B CD  1 
ATOM   5415 O OE1 . GLN   B 1 323 ? -34.12100 53.95800  -16.53600 1.000 105.14908 ? 299  GLN   B OE1 1 
ATOM   5416 N NE2 . GLN   B 1 323 ? -32.81100 55.29500  -15.29400 1.000 98.07399  ? 299  GLN   B NE2 1 
ATOM   5417 N N   . ASP   B 1 324 ? -30.52100 52.67100  -20.73300 1.000 98.82960  ? 300  ASP   B N   1 
ATOM   5418 C CA  . ASP   B 1 324 ? -29.50100 52.17700  -21.65100 1.000 104.48570 ? 300  ASP   B CA  1 
ATOM   5419 C C   . ASP   B 1 324 ? -28.15800 52.86400  -21.41600 1.000 106.36863 ? 300  ASP   B C   1 
ATOM   5420 O O   . ASP   B 1 324 ? -28.09900 53.97600  -20.87900 1.000 105.07042 ? 300  ASP   B O   1 
ATOM   5421 C CB  . ASP   B 1 324 ? -29.97400 52.33900  -23.09500 1.000 103.06966 ? 300  ASP   B CB  1 
ATOM   5422 C CG  . ASP   B 1 324 ? -31.38600 51.81500  -23.30000 1.000 109.69115 ? 300  ASP   B CG  1 
ATOM   5423 O OD1 . ASP   B 1 324 ? -31.53900 50.59600  -23.52900 1.000 113.36313 ? 300  ASP   B OD1 1 
ATOM   5424 O OD2 . ASP   B 1 324 ? -32.34100 52.61500  -23.21200 1.000 113.11508 ? 300  ASP   B OD2 1 
ATOM   5425 N N   . ASN   B 1 325 ? -27.08100 52.20200  -21.83200 1.000 99.48334  ? 301  ASN   B N   1 
ATOM   5426 C CA  . ASN   B 1 325 ? -25.75900 52.43900  -21.26300 1.000 96.96545  ? 301  ASN   B CA  1 
ATOM   5427 C C   . ASN   B 1 325 ? -25.21500 53.81900  -21.61900 1.000 100.15433 ? 301  ASN   B C   1 
ATOM   5428 O O   . ASN   B 1 325 ? -25.05800 54.15400  -22.79800 1.000 105.02367 ? 301  ASN   B O   1 
ATOM   5429 C CB  . ASN   B 1 325 ? -24.79700 51.35200  -21.73800 1.000 102.89727 ? 301  ASN   B CB  1 
ATOM   5430 C CG  . ASN   B 1 325 ? -25.43900 49.97600  -21.76500 1.000 103.63068 ? 301  ASN   B CG  1 
ATOM   5431 O OD1 . ASN   B 1 325 ? -26.18200 49.60900  -20.85600 1.000 98.40458  ? 301  ASN   B OD1 1 
ATOM   5432 N ND2 . ASN   B 1 325 ? -25.14400 49.20400  -22.80400 1.000 100.47930 ? 301  ASN   B ND2 1 
ATOM   5433 N N   . LEU   B 1 326 ? -24.92900 54.61500  -20.58900 1.000 96.86012  ? 302  LEU   B N   1 
ATOM   5434 C CA  . LEU   B 1 326 ? -23.99700 55.73100  -20.67200 1.000 96.61100  ? 302  LEU   B CA  1 
ATOM   5435 C C   . LEU   B 1 326 ? -22.74900 55.44100  -19.84100 1.000 99.43349  ? 302  LEU   B C   1 
ATOM   5436 O O   . LEU   B 1 326 ? -21.86000 56.29100  -19.73100 1.000 102.31542 ? 302  LEU   B O   1 
ATOM   5437 C CB  . LEU   B 1 326 ? -24.69900 57.03200  -20.24800 1.000 89.00948  ? 302  LEU   B CB  1 
ATOM   5438 C CG  . LEU   B 1 326 ? -24.12200 58.45900  -20.34100 1.000 95.05783  ? 302  LEU   B CG  1 
ATOM   5439 C CD1 . LEU   B 1 326 ? -23.19000 58.86100  -19.19600 1.000 90.28818  ? 302  LEU   B CD1 1 
ATOM   5440 C CD2 . LEU   B 1 326 ? -23.40600 58.62600  -21.67400 1.000 96.27308  ? 302  LEU   B CD2 1 
ATOM   5441 N N   . ILE   B 1 327 ? -22.64600 54.22800  -19.30200 1.000 93.46215  ? 303  ILE   B N   1 
ATOM   5442 C CA  . ILE   B 1 327 ? -21.53600 53.82800  -18.44400 1.000 85.52330  ? 303  ILE   B CA  1 
ATOM   5443 C C   . ILE   B 1 327 ? -20.42500 53.31300  -19.35600 1.000 84.62454  ? 303  ILE   B C   1 
ATOM   5444 O O   . ILE   B 1 327 ? -20.50300 52.20400  -19.89200 1.000 82.90259  ? 303  ILE   B O   1 
ATOM   5445 C CB  . ILE   B 1 327 ? -21.96100 52.77700  -17.41300 1.000 80.74096  ? 303  ILE   B CB  1 
ATOM   5446 C CG1 . ILE   B 1 327 ? -22.85600 53.37700  -16.31600 1.000 83.13656  ? 303  ILE   B CG1 1 
ATOM   5447 C CG2 . ILE   B 1 327 ? -20.74300 52.12900  -16.77200 1.000 75.54663  ? 303  ILE   B CG2 1 
ATOM   5448 C CD1 . ILE   B 1 327 ? -24.23200 53.86700  -16.75300 1.000 86.25998  ? 303  ILE   B CD1 1 
ATOM   5449 N N   . ARG   B 1 328 ? -19.39000 54.13000  -19.54600 1.000 75.61125  ? 304  ARG   B N   1 
ATOM   5450 C CA  . ARG   B 1 328 ? -18.24500 53.70200  -20.33700 1.000 81.60804  ? 304  ARG   B CA  1 
ATOM   5451 C C   . ARG   B 1 328 ? -17.38500 52.72300  -19.54200 1.000 81.40882  ? 304  ARG   B C   1 
ATOM   5452 O O   . ARG   B 1 328 ? -17.29000 52.79600  -18.31400 1.000 86.09077  ? 304  ARG   B O   1 
ATOM   5453 C CB  . ARG   B 1 328 ? -17.41900 54.91100  -20.78800 1.000 87.56667  ? 304  ARG   B CB  1 
ATOM   5454 C CG  . ARG   B 1 328 ? -17.01200 55.87100  -19.67900 1.000 89.55892  ? 304  ARG   B CG  1 
ATOM   5455 C CD  . ARG   B 1 328 ? -15.67500 56.53200  -19.99500 1.000 92.84157  ? 304  ARG   B CD  1 
ATOM   5456 N NE  . ARG   B 1 328 ? -15.36700 57.63100  -19.08700 1.000 94.48303  ? 304  ARG   B NE  1 
ATOM   5457 C CZ  . ARG   B 1 328 ? -14.16200 58.16500  -18.93700 1.000 95.32125  ? 304  ARG   B CZ  1 
ATOM   5458 N NH1 . ARG   B 1 328 ? -13.11800 57.71800  -19.61500 1.000 88.45145  ? 304  ARG   B NH1 1 
ATOM   5459 N NH2 . ARG   B 1 328 ? -14.00100 59.17200  -18.08200 1.000 96.37721  ? 304  ARG   B NH2 1 
ATOM   5460 N N   . LYS   B 1 329 ? -16.75100 51.79600  -20.26500 1.000 81.03940  ? 305  LYS   B N   1 
ATOM   5461 C CA  . LYS   B 1 329 ? -16.10400 50.65800  -19.61900 1.000 81.11631  ? 305  LYS   B CA  1 
ATOM   5462 C C   . LYS   B 1 329 ? -14.88700 51.06500  -18.79600 1.000 80.60743  ? 305  LYS   B C   1 
ATOM   5463 O O   . LYS   B 1 329 ? -14.52400 50.35600  -17.85100 1.000 73.61608  ? 305  LYS   B O   1 
ATOM   5464 C CB  . LYS   B 1 329 ? -15.72400 49.61100  -20.66700 1.000 82.96384  ? 305  LYS   B CB  1 
ATOM   5465 C CG  . LYS   B 1 329 ? -16.93000 49.04800  -21.40500 1.000 89.18873  ? 305  LYS   B CG  1 
ATOM   5466 C CD  . LYS   B 1 329 ? -16.55800 47.91800  -22.34900 1.000 83.37190  ? 305  LYS   B CD  1 
ATOM   5467 C CE  . LYS   B 1 329 ? -17.65900 47.68500  -23.37000 1.000 79.00768  ? 305  LYS   B CE  1 
ATOM   5468 N NZ  . LYS   B 1 329 ? -17.29800 48.20000  -24.72100 1.000 77.21566  ? 305  LYS   B NZ  1 
ATOM   5469 N N   . GLU   B 1 330 ? -14.24400 52.18900  -19.12700 1.000 87.15107  ? 306  GLU   B N   1 
ATOM   5470 C CA  . GLU   B 1 330 ? -13.15400 52.67200  -18.28300 1.000 86.30708  ? 306  GLU   B CA  1 
ATOM   5471 C C   . GLU   B 1 330 ? -13.63700 52.97300  -16.86900 1.000 76.84257  ? 306  GLU   B C   1 
ATOM   5472 O O   . GLU   B 1 330 ? -12.87200 52.83900  -15.90700 1.000 76.00363  ? 306  GLU   B O   1 
ATOM   5473 C CB  . GLU   B 1 330 ? -12.50700 53.92200  -18.88800 1.000 89.14956  ? 306  GLU   B CB  1 
ATOM   5474 C CG  . GLU   B 1 330 ? -11.97600 53.76600  -20.30600 1.000 86.75320  ? 306  GLU   B CG  1 
ATOM   5475 C CD  . GLU   B 1 330 ? -12.99800 54.15000  -21.36400 1.000 101.76060 ? 306  GLU   B CD  1 
ATOM   5476 O OE1 . GLU   B 1 330 ? -14.20800 53.92900  -21.13900 1.000 95.17914  ? 306  GLU   B OE1 1 
ATOM   5477 O OE2 . GLU   B 1 330 ? -12.58800 54.68200  -22.41800 1.000 112.41204 ? 306  GLU   B OE2 1 
ATOM   5478 N N   . VAL   B 1 331 ? -14.89900 53.37000  -16.72300 1.000 73.94633  ? 307  VAL   B N   1 
ATOM   5479 C CA  . VAL   B 1 331 ? -15.44300 53.71900  -15.41500 1.000 74.22465  ? 307  VAL   B CA  1 
ATOM   5480 C C   . VAL   B 1 331 ? -15.96800 52.49100  -14.68000 1.000 68.98208  ? 307  VAL   B C   1 
ATOM   5481 O O   . VAL   B 1 331 ? -15.80900 52.37800  -13.46200 1.000 67.39671  ? 307  VAL   B O   1 
ATOM   5482 C CB  . VAL   B 1 331 ? -16.53600 54.79500  -15.57700 1.000 72.36122  ? 307  VAL   B CB  1 
ATOM   5483 C CG1 . VAL   B 1 331 ? -17.25100 55.03700  -14.26000 1.000 60.71365  ? 307  VAL   B CG1 1 
ATOM   5484 C CG2 . VAL   B 1 331 ? -15.92900 56.09000  -16.09800 1.000 78.93029  ? 307  VAL   B CG2 1 
ATOM   5485 N N   . TYR   B 1 332 ? -16.58700 51.55000  -15.39900 1.000 67.37841  ? 308  TYR   B N   1 
ATOM   5486 C CA  . TYR   B 1 332 ? -17.14900 50.37500  -14.73800 1.000 61.98072  ? 308  TYR   B CA  1 
ATOM   5487 C C   . TYR   B 1 332 ? -16.05700 49.54400  -14.07300 1.000 63.21893  ? 308  TYR   B C   1 
ATOM   5488 O O   . TYR   B 1 332 ? -16.22700 49.07800  -12.94100 1.000 69.44143  ? 308  TYR   B O   1 
ATOM   5489 C CB  . TYR   B 1 332 ? -17.95000 49.54200  -15.74300 1.000 61.23373  ? 308  TYR   B CB  1 
ATOM   5490 C CG  . TYR   B 1 332 ? -18.20100 48.09400  -15.35100 1.000 53.47281  ? 308  TYR   B CG  1 
ATOM   5491 C CD1 . TYR   B 1 332 ? -17.23800 47.10700  -15.55200 1.000 61.85678  ? 308  TYR   B CD1 1 
ATOM   5492 C CD2 . TYR   B 1 332 ? -19.40900 47.71700  -14.78200 1.000 50.28482  ? 308  TYR   B CD2 1 
ATOM   5493 C CE1 . TYR   B 1 332 ? -17.47500 45.79000  -15.19400 1.000 62.61594  ? 308  TYR   B CE1 1 
ATOM   5494 C CE2 . TYR   B 1 332 ? -19.65300 46.40500  -14.41900 1.000 56.81065  ? 308  TYR   B CE2 1 
ATOM   5495 C CZ  . TYR   B 1 332 ? -18.68600 45.44600  -14.62800 1.000 57.67487  ? 308  TYR   B CZ  1 
ATOM   5496 O OH  . TYR   B 1 332 ? -18.93400 44.14000  -14.26700 1.000 52.50189  ? 308  TYR   B OH  1 
ATOM   5497 N N   . ILE   B 1 333 ? -14.92400 49.35100  -14.75700 1.000 66.22154  ? 309  ILE   B N   1 
ATOM   5498 C CA  . ILE   B 1 333 ? -13.83000 48.59600  -14.15600 1.000 68.22259  ? 309  ILE   B CA  1 
ATOM   5499 C C   . ILE   B 1 333 ? -13.10300 49.42400  -13.10700 1.000 61.93836  ? 309  ILE   B C   1 
ATOM   5500 O O   . ILE   B 1 333 ? -12.41300 48.86400  -12.25000 1.000 59.85771  ? 309  ILE   B O   1 
ATOM   5501 C CB  . ILE   B 1 333 ? -12.83200 48.09200  -15.22000 1.000 70.52818  ? 309  ILE   B CB  1 
ATOM   5502 C CG1 . ILE   B 1 333 ? -11.87600 49.20700  -15.65000 1.000 63.63958  ? 309  ILE   B CG1 1 
ATOM   5503 C CG2 . ILE   B 1 333 ? -13.57600 47.56500  -16.42700 1.000 72.37431  ? 309  ILE   B CG2 1 
ATOM   5504 C CD1 . ILE   B 1 333 ? -10.74100 48.73200  -16.54800 1.000 69.24634  ? 309  ILE   B CD1 1 
ATOM   5505 N N   . LEU   B 1 334 ? -13.23000 50.75100  -13.15300 1.000 61.01845  ? 310  LEU   B N   1 
ATOM   5506 C CA  . LEU   B 1 334 ? -12.59200 51.57300  -12.13400 1.000 61.89557  ? 310  LEU   B CA  1 
ATOM   5507 C C   . LEU   B 1 334 ? -13.38200 51.54200  -10.83200 1.000 65.51206  ? 310  LEU   B C   1 
ATOM   5508 O O   . LEU   B 1 334 ? -12.79600 51.42100  -9.75000  1.000 69.57705  ? 310  LEU   B O   1 
ATOM   5509 C CB  . LEU   B 1 334 ? -12.43300 53.00800  -12.63200 1.000 63.65392  ? 310  LEU   B CB  1 
ATOM   5510 C CG  . LEU   B 1 334 ? -11.89500 53.98200  -11.58200 1.000 67.22286  ? 310  LEU   B CG  1 
ATOM   5511 C CD1 . LEU   B 1 334 ? -10.41100 53.72900  -11.31900 1.000 65.28233  ? 310  LEU   B CD1 1 
ATOM   5512 C CD2 . LEU   B 1 334 ? -12.13700 55.42500  -11.99200 1.000 75.45589  ? 310  LEU   B CD2 1 
ATOM   5513 N N   . LEU   B 1 335 ? -14.71200 51.64300  -10.91700 1.000 59.84958  ? 311  LEU   B N   1 
ATOM   5514 C CA  . LEU   B 1 335 ? -15.53700 51.53500  -9.71900  1.000 54.97225  ? 311  LEU   B CA  1 
ATOM   5515 C C   . LEU   B 1 335 ? -15.49600 50.12500  -9.14900  1.000 54.21289  ? 311  LEU   B C   1 
ATOM   5516 O O   . LEU   B 1 335 ? -15.66700 49.93600  -7.93800  1.000 51.38336  ? 311  LEU   B O   1 
ATOM   5517 C CB  . LEU   B 1 335 ? -16.97400 51.95600  -10.02800 1.000 49.30012  ? 311  LEU   B CB  1 
ATOM   5518 C CG  . LEU   B 1 335 ? -17.31000 53.45400  -9.98500  1.000 51.07506  ? 311  LEU   B CG  1 
ATOM   5519 C CD1 . LEU   B 1 335 ? -16.24300 54.33600  -10.63000 1.000 57.02529  ? 311  LEU   B CD1 1 
ATOM   5520 C CD2 . LEU   B 1 335 ? -18.66200 53.70900  -10.63200 1.000 53.74092  ? 311  LEU   B CD2 1 
ATOM   5521 N N   . ASN   B 1 336 ? -15.25500 49.13200  -10.00300 1.000 50.67405  ? 312  ASN   B N   1 
ATOM   5522 C CA  . ASN   B 1 336 ? -15.07900 47.76600  -9.53000  1.000 49.54903  ? 312  ASN   B CA  1 
ATOM   5523 C C   . ASN   B 1 336 ? -13.76500 47.60200  -8.77100  1.000 53.88033  ? 312  ASN   B C   1 
ATOM   5524 O O   . ASN   B 1 336 ? -13.69900 46.83300  -7.80500  1.000 56.11787  ? 312  ASN   B O   1 
ATOM   5525 C CB  . ASN   B 1 336 ? -15.15400 46.81200  -10.72100 1.000 51.70215  ? 312  ASN   B CB  1 
ATOM   5526 C CG  . ASN   B 1 336 ? -15.22000 45.35700  -10.30900 1.000 49.18642  ? 312  ASN   B CG  1 
ATOM   5527 O OD1 . ASN   B 1 336 ? -15.14100 45.02400  -9.13400  1.000 51.98355  ? 312  ASN   B OD1 1 
ATOM   5528 N ND2 . ASN   B 1 336 ? -15.37800 44.48000  -11.28500 1.000 48.45521  ? 312  ASN   B ND2 1 
ATOM   5529 N N   . TRP   B 1 337 ? -12.71200 48.31200  -9.18400  1.000 53.11955  ? 313  TRP   B N   1 
ATOM   5530 C CA  . TRP   B 1 337 ? -11.45400 48.25500  -8.44800  1.000 52.83214  ? 313  TRP   B CA  1 
ATOM   5531 C C   . TRP   B 1 337 ? -11.54100 48.97700  -7.10900  1.000 56.18795  ? 313  TRP   B C   1 
ATOM   5532 O O   . TRP   B 1 337 ? -10.72100 48.71200  -6.22300  1.000 55.93772  ? 313  TRP   B O   1 
ATOM   5533 C CB  . TRP   B 1 337 ? -10.30900 48.82000  -9.29700  1.000 53.79723  ? 313  TRP   B CB  1 
ATOM   5534 C CG  . TRP   B 1 337 ? -9.66200  47.76700  -10.14700 1.000 48.95181  ? 313  TRP   B CG  1 
ATOM   5535 C CD1 . TRP   B 1 337 ? -10.10200 47.30500  -11.35100 1.000 46.89182  ? 313  TRP   B CD1 1 
ATOM   5536 C CD2 . TRP   B 1 337 ? -8.48100  47.01700  -9.83800  1.000 44.37520  ? 313  TRP   B CD2 1 
ATOM   5537 N NE1 . TRP   B 1 337 ? -9.26600  46.32300  -11.81700 1.000 46.27665  ? 313  TRP   B NE1 1 
ATOM   5538 C CE2 . TRP   B 1 337 ? -8.26100  46.12700  -10.90700 1.000 44.71869  ? 313  TRP   B CE2 1 
ATOM   5539 C CE3 . TRP   B 1 337 ? -7.58600  47.01400  -8.76500  1.000 49.30630  ? 313  TRP   B CE3 1 
ATOM   5540 C CZ2 . TRP   B 1 337 ? -7.18300  45.24500  -10.93500 1.000 47.58612  ? 313  TRP   B CZ2 1 
ATOM   5541 C CZ3 . TRP   B 1 337 ? -6.51600  46.13700  -8.79600  1.000 46.18653  ? 313  TRP   B CZ3 1 
ATOM   5542 C CH2 . TRP   B 1 337 ? -6.32400  45.26600  -9.87300  1.000 44.22832  ? 313  TRP   B CH2 1 
ATOM   5543 N N   . ILE   B 1 338 ? -12.51100 49.87800  -6.93800  1.000 53.55187  ? 314  ILE   B N   1 
ATOM   5544 C CA  . ILE   B 1 338 ? -12.82200 50.36500  -5.59700  1.000 56.31430  ? 314  ILE   B CA  1 
ATOM   5545 C C   . ILE   B 1 338 ? -13.31200 49.21400  -4.72800  1.000 53.21651  ? 314  ILE   B C   1 
ATOM   5546 O O   . ILE   B 1 338 ? -12.99000 49.13000  -3.53600  1.000 53.80826  ? 314  ILE   B O   1 
ATOM   5547 C CB  . ILE   B 1 338 ? -13.85200 51.50900  -5.66000  1.000 58.87075  ? 314  ILE   B CB  1 
ATOM   5548 C CG1 . ILE   B 1 338 ? -13.27800 52.70900  -6.41400  1.000 51.95268  ? 314  ILE   B CG1 1 
ATOM   5549 C CG2 . ILE   B 1 338 ? -14.28100 51.92500  -4.26000  1.000 49.91559  ? 314  ILE   B CG2 1 
ATOM   5550 C CD1 . ILE   B 1 338 ? -14.28700 53.81200  -6.64300  1.000 41.68369  ? 314  ILE   B CD1 1 
ATOM   5551 N N   . GLY   B 1 339 ? -14.09000 48.30200  -5.31100  1.000 50.61134  ? 315  GLY   B N   1 
ATOM   5552 C CA  . GLY   B 1 339 ? -14.49000 47.11600  -4.58000  1.000 49.98263  ? 315  GLY   B CA  1 
ATOM   5553 C C   . GLY   B 1 339 ? -13.34300 46.15700  -4.33400  1.000 54.68660  ? 315  GLY   B C   1 
ATOM   5554 O O   . GLY   B 1 339 ? -13.32500 45.45500  -3.31900  1.000 57.52718  ? 315  GLY   B O   1 
ATOM   5555 N N   . TYR   B 1 340 ? -12.37100 46.11400  -5.24600  1.000 49.49302  ? 316  TYR   B N   1 
ATOM   5556 C CA  . TYR   B 1 340 ? -11.26500 45.17300  -5.09400  1.000 50.13771  ? 316  TYR   B CA  1 
ATOM   5557 C C   . TYR   B 1 340 ? -10.35600 45.56100  -3.93400  1.000 49.35609  ? 316  TYR   B C   1 
ATOM   5558 O O   . TYR   B 1 340 ? -9.87500  44.69000  -3.19900  1.000 46.37085  ? 316  TYR   B O   1 
ATOM   5559 C CB  . TYR   B 1 340 ? -10.46400 45.08600  -6.39400  1.000 53.47394  ? 316  TYR   B CB  1 
ATOM   5560 C CG  . TYR   B 1 340 ? -11.08200 44.21100  -7.46600  1.000 56.28582  ? 316  TYR   B CG  1 
ATOM   5561 C CD1 . TYR   B 1 340 ? -12.36700 43.70100  -7.32800  1.000 55.05273  ? 316  TYR   B CD1 1 
ATOM   5562 C CD2 . TYR   B 1 340 ? -10.37700 43.90000  -8.62200  1.000 53.11100  ? 316  TYR   B CD2 1 
ATOM   5563 C CE1 . TYR   B 1 340 ? -12.93000 42.90100  -8.31300  1.000 55.81207  ? 316  TYR   B CE1 1 
ATOM   5564 C CE2 . TYR   B 1 340 ? -10.93100 43.10300  -9.61000  1.000 51.82556  ? 316  TYR   B CE2 1 
ATOM   5565 C CZ  . TYR   B 1 340 ? -12.20600 42.60700  -9.45200  1.000 55.55101  ? 316  TYR   B CZ  1 
ATOM   5566 O OH  . TYR   B 1 340 ? -12.75600 41.81400  -10.43500 1.000 53.23346  ? 316  TYR   B OH  1 
ATOM   5567 N N   . VAL   B 1 341 ? -10.10600 46.86000  -3.75300  1.000 52.07825  ? 317  VAL   B N   1 
ATOM   5568 C CA  . VAL   B 1 341 ? -9.15900  47.29300  -2.72900  1.000 56.52201  ? 317  VAL   B CA  1 
ATOM   5569 C C   . VAL   B 1 341 ? -9.74000  47.19200  -1.32600  1.000 58.64010  ? 317  VAL   B C   1 
ATOM   5570 O O   . VAL   B 1 341 ? -8.97900  47.16100  -0.35000  1.000 54.85874  ? 317  VAL   B O   1 
ATOM   5571 C CB  . VAL   B 1 341 ? -8.67900  48.72900  -2.99700  1.000 53.83167  ? 317  VAL   B CB  1 
ATOM   5572 C CG1 . VAL   B 1 341 ? -8.07200  48.82900  -4.38600  1.000 50.75309  ? 317  VAL   B CG1 1 
ATOM   5573 C CG2 . VAL   B 1 341 ? -9.81900  49.72400  -2.82800  1.000 55.16650  ? 317  VAL   B CG2 1 
ATOM   5574 N N   . ASN   B 1 342 ? -11.07000 47.13500  -1.19900  1.000 60.08904  ? 318  ASN   B N   1 
ATOM   5575 C CA  . ASN   B 1 342 ? -11.69700 46.95600  0.10600   1.000 52.74925  ? 318  ASN   B CA  1 
ATOM   5576 C C   . ASN   B 1 342 ? -11.18600 45.70500  0.81000   1.000 59.05791  ? 318  ASN   B C   1 
ATOM   5577 O O   . ASN   B 1 342 ? -11.21400 45.63100  2.04600   1.000 61.19220  ? 318  ASN   B O   1 
ATOM   5578 C CB  . ASN   B 1 342 ? -13.21400 46.88500  -0.06300  1.000 57.10527  ? 318  ASN   B CB  1 
ATOM   5579 C CG  . ASN   B 1 342 ? -13.93400 46.56700  1.23100   1.000 56.89001  ? 318  ASN   B CG  1 
ATOM   5580 O OD1 . ASN   B 1 342 ? -14.97900 45.92000  1.22300   1.000 59.54851  ? 318  ASN   B OD1 1 
ATOM   5581 N ND2 . ASN   B 1 342 ? -13.39800 47.04700  2.34700   1.000 54.17747  ? 318  ASN   B ND2 1 
ATOM   5582 N N   . SER   B 1 343 ? -10.71100 44.71500  0.04500   1.000 53.31864  ? 319  SER   B N   1 
ATOM   5583 C CA  . SER   B 1 343 ? -10.17900 43.49500  0.64300   1.000 55.30193  ? 319  SER   B CA  1 
ATOM   5584 C C   . SER   B 1 343 ? -8.92300  43.75300  1.46500   1.000 55.74603  ? 319  SER   B C   1 
ATOM   5585 O O   . SER   B 1 343 ? -8.59500  42.94700  2.34200   1.000 54.90288  ? 319  SER   B O   1 
ATOM   5586 C CB  . SER   B 1 343 ? -9.88600  42.45700  -0.44000  1.000 46.01020  ? 319  SER   B CB  1 
ATOM   5587 O OG  . SER   B 1 343 ? -10.97200 42.34500  -1.34100  1.000 51.70960  ? 319  SER   B OG  1 
ATOM   5588 N N   . GLY   B 1 344 ? -8.21200  44.84600  1.20500   1.000 51.42177  ? 320  GLY   B N   1 
ATOM   5589 C CA  . GLY   B 1 344 ? -7.07700  45.21700  2.02000   1.000 49.61465  ? 320  GLY   B CA  1 
ATOM   5590 C C   . GLY   B 1 344 ? -7.39900  46.12100  3.18800   1.000 50.77762  ? 320  GLY   B C   1 
ATOM   5591 O O   . GLY   B 1 344 ? -6.51600  46.42200  3.99900   1.000 45.51575  ? 320  GLY   B O   1 
ATOM   5592 N N   . PHE   B 1 345 ? -8.65700  46.55000  3.30700   1.000 53.38849  ? 321  PHE   B N   1 
ATOM   5593 C CA  . PHE   B 1 345 ? -9.03200  47.54100  4.31100   1.000 55.91146  ? 321  PHE   B CA  1 
ATOM   5594 C C   . PHE   B 1 345 ? -9.20600  46.92500  5.69500   1.000 52.18123  ? 321  PHE   B C   1 
ATOM   5595 O O   . PHE   B 1 345 ? -8.81800  47.53600  6.69800   1.000 46.14346  ? 321  PHE   B O   1 
ATOM   5596 C CB  . PHE   B 1 345 ? -10.31900 48.25200  3.88800   1.000 52.40817  ? 321  PHE   B CB  1 
ATOM   5597 C CG  . PHE   B 1 345 ? -10.08900 49.47400  3.05000   1.000 59.88384  ? 321  PHE   B CG  1 
ATOM   5598 C CD1 . PHE   B 1 345 ? -9.51400  49.37200  1.79400   1.000 67.00674  ? 321  PHE   B CD1 1 
ATOM   5599 C CD2 . PHE   B 1 345 ? -10.44100 50.72800  3.52200   1.000 63.35744  ? 321  PHE   B CD2 1 
ATOM   5600 C CE1 . PHE   B 1 345 ? -9.29800  50.49700  1.02000   1.000 67.08080  ? 321  PHE   B CE1 1 
ATOM   5601 C CE2 . PHE   B 1 345 ? -10.22700 51.85800  2.75300   1.000 73.38120  ? 321  PHE   B CE2 1 
ATOM   5602 C CZ  . PHE   B 1 345 ? -9.65500  51.74100  1.50000   1.000 72.84554  ? 321  PHE   B CZ  1 
ATOM   5603 N N   . ASN   B 1 346 ? -9.78600  45.72600  5.77200   1.000 51.82275  ? 322  ASN   B N   1 
ATOM   5604 C CA  . ASN   B 1 346 ? -10.17500 45.18300  7.07200   1.000 47.39870  ? 322  ASN   B CA  1 
ATOM   5605 C C   . ASN   B 1 346 ? -8.99600  44.97400  8.01600   1.000 44.25350  ? 322  ASN   B C   1 
ATOM   5606 O O   . ASN   B 1 346 ? -9.09700  45.39200  9.18200   1.000 41.72647  ? 322  ASN   B O   1 
ATOM   5607 C CB  . ASN   B 1 346 ? -10.98700 43.89600  6.87700   1.000 45.66931  ? 322  ASN   B CB  1 
ATOM   5608 C CG  . ASN   B 1 346 ? -12.38200 44.16400  6.34000   1.000 43.01618  ? 322  ASN   B CG  1 
ATOM   5609 O OD1 . ASN   B 1 346 ? -12.76400 45.31400  6.11600   1.000 42.95015  ? 322  ASN   B OD1 1 
ATOM   5610 N ND2 . ASN   B 1 346 ? -13.16300 43.10300  6.16900   1.000 44.12004  ? 322  ASN   B ND2 1 
ATOM   5611 N N   . PRO   B 1 347 ? -7.87200  44.35700  7.61200   1.000 47.01087  ? 323  PRO   B N   1 
ATOM   5612 C CA  . PRO   B 1 347 ? -6.73500  44.26400  8.54600   1.000 45.45576  ? 323  PRO   B CA  1 
ATOM   5613 C C   . PRO   B 1 347 ? -6.33200  45.60100  9.14300   1.000 45.00198  ? 323  PRO   B C   1 
ATOM   5614 O O   . PRO   B 1 347 ? -6.03700  45.67200  10.34100  1.000 49.56903  ? 323  PRO   B O   1 
ATOM   5615 C CB  . PRO   B 1 347 ? -5.62100  43.66600  7.67800   1.000 34.86162  ? 323  PRO   B CB  1 
ATOM   5616 C CG  . PRO   B 1 347 ? -6.34400  42.85500  6.67900   1.000 40.77569  ? 323  PRO   B CG  1 
ATOM   5617 C CD  . PRO   B 1 347 ? -7.60300  43.61600  6.36400   1.000 44.07082  ? 323  PRO   B CD  1 
ATOM   5618 N N   . LEU   B 1 348 ? -6.33200  46.67100  8.34500   1.000 41.57926  ? 324  LEU   B N   1 
ATOM   5619 C CA  . LEU   B 1 348 ? -6.07100  47.99800  8.89300   1.000 43.74029  ? 324  LEU   B CA  1 
ATOM   5620 C C   . LEU   B 1 348 ? -7.13200  48.39300  9.91400   1.000 50.15818  ? 324  LEU   B C   1 
ATOM   5621 O O   . LEU   B 1 348 ? -6.80700  48.84800  11.01700  1.000 50.08903  ? 324  LEU   B O   1 
ATOM   5622 C CB  . LEU   B 1 348 ? -6.00400  49.02900  7.76800   1.000 43.26689  ? 324  LEU   B CB  1 
ATOM   5623 C CG  . LEU   B 1 348 ? -4.84800  48.90200  6.78200   1.000 51.65591  ? 324  LEU   B CG  1 
ATOM   5624 C CD1 . LEU   B 1 348 ? -4.95800  49.96600  5.70900   1.000 61.16701  ? 324  LEU   B CD1 1 
ATOM   5625 C CD2 . LEU   B 1 348 ? -3.53200  49.03000  7.52100   1.000 55.05926  ? 324  LEU   B CD2 1 
ATOM   5626 N N   . ILE   B 1 349 ? -8.41100  48.22800  9.56200   1.000 45.66051  ? 325  ILE   B N   1 
ATOM   5627 C CA  . ILE   B 1 349 ? -9.49200  48.64400  10.45400  1.000 45.80623  ? 325  ILE   B CA  1 
ATOM   5628 C C   . ILE   B 1 349 ? -9.39000  47.92800  11.79400  1.000 48.15631  ? 325  ILE   B C   1 
ATOM   5629 O O   . ILE   B 1 349 ? -9.69100  48.50700  12.84600  1.000 45.96606  ? 325  ILE   B O   1 
ATOM   5630 C CB  . ILE   B 1 349 ? -10.86000 48.39300  9.78800   1.000 48.39276  ? 325  ILE   B CB  1 
ATOM   5631 C CG1 . ILE   B 1 349 ? -11.05400 49.31100  8.58300   1.000 48.51835  ? 325  ILE   B CG1 1 
ATOM   5632 C CG2 . ILE   B 1 349 ? -11.98700 48.61600  10.78000  1.000 50.13814  ? 325  ILE   B CG2 1 
ATOM   5633 C CD1 . ILE   B 1 349 ? -12.24800 48.93800  7.72100   1.000 39.11081  ? 325  ILE   B CD1 1 
ATOM   5634 N N   . TYR   B 1 350 ? -8.94000  46.67100  11.78500  1.000 47.64573  ? 326  TYR   B N   1 
ATOM   5635 C CA  . TYR   B 1 350 ? -8.87600  45.88300  13.00600  1.000 43.91286  ? 326  TYR   B CA  1 
ATOM   5636 C C   . TYR   B 1 350 ? -7.82400  46.38900  13.98200  1.000 46.26443  ? 326  TYR   B C   1 
ATOM   5637 O O   . TYR   B 1 350 ? -7.84200  45.97900  15.14800  1.000 46.96008  ? 326  TYR   B O   1 
ATOM   5638 C CB  . TYR   B 1 350 ? -8.60300  44.41800  12.67700  1.000 43.95549  ? 326  TYR   B CB  1 
ATOM   5639 C CG  . TYR   B 1 350 ? -9.74400  43.74300  11.96400  1.000 45.62284  ? 326  TYR   B CG  1 
ATOM   5640 C CD1 . TYR   B 1 350 ? -11.04900 43.88500  12.41700  1.000 44.83425  ? 326  TYR   B CD1 1 
ATOM   5641 C CD2 . TYR   B 1 350 ? -9.51600  42.93700  10.85500  1.000 46.44516  ? 326  TYR   B CD2 1 
ATOM   5642 C CE1 . TYR   B 1 350 ? -12.09700 43.26900  11.76600  1.000 44.98942  ? 326  TYR   B CE1 1 
ATOM   5643 C CE2 . TYR   B 1 350 ? -10.55800 42.31300  10.20000  1.000 42.90200  ? 326  TYR   B CE2 1 
ATOM   5644 C CZ  . TYR   B 1 350 ? -11.84500 42.48000  10.66100  1.000 44.79171  ? 326  TYR   B CZ  1 
ATOM   5645 O OH  . TYR   B 1 350 ? -12.88200 41.85600  10.01400  1.000 47.66519  ? 326  TYR   B OH  1 
ATOM   5646 N N   . CYS   B 1 351 ? -6.91400  47.26000  13.54400  1.000 43.46396  ? 327  CYS   B N   1 
ATOM   5647 C CA  . CYS   B 1 351 ? -5.99500  47.90200  14.47800  1.000 47.44485  ? 327  CYS   B CA  1 
ATOM   5648 C C   . CYS   B 1 351 ? -6.68700  48.89000  15.40200  1.000 47.22990  ? 327  CYS   B C   1 
ATOM   5649 O O   . CYS   B 1 351 ? -6.00400  49.54600  16.19200  1.000 52.61333  ? 327  CYS   B O   1 
ATOM   5650 C CB  . CYS   B 1 351 ? -4.87100  48.61000  13.72200  1.000 49.76828  ? 327  CYS   B CB  1 
ATOM   5651 S SG  . CYS   B 1 351 ? -3.69900  47.49300  12.94600  1.000 52.03779  ? 327  CYS   B SG  1 
ATOM   5652 N N   . ARG   B 1 352 ? -8.00800  49.02800  15.31300  1.000 44.83588  ? 328  ARG   B N   1 
ATOM   5653 C CA  . ARG   B 1 352 ? -8.74100  49.83600  16.27600  1.000 45.52944  ? 328  ARG   B CA  1 
ATOM   5654 C C   . ARG   B 1 352 ? -8.96300  49.08300  17.58000  1.000 51.48633  ? 328  ARG   B C   1 
ATOM   5655 O O   . ARG   B 1 352 ? -9.03800  49.70100  18.64800  1.000 53.43063  ? 328  ARG   B O   1 
ATOM   5656 C CB  . ARG   B 1 352 ? -10.07200 50.27100  15.66800  1.000 49.95658  ? 328  ARG   B CB  1 
ATOM   5657 C CG  . ARG   B 1 352 ? -9.93400  51.39200  14.65600  1.000 49.46654  ? 328  ARG   B CG  1 
ATOM   5658 C CD  . ARG   B 1 352 ? -11.23600 51.61300  13.91900  1.000 50.86147  ? 328  ARG   B CD  1 
ATOM   5659 N NE  . ARG   B 1 352 ? -12.37900 51.50600  14.81800  1.000 46.23353  ? 328  ARG   B NE  1 
ATOM   5660 C CZ  . ARG   B 1 352 ? -12.83400 52.49600  15.57300  1.000 41.02941  ? 328  ARG   B CZ  1 
ATOM   5661 N NH1 . ARG   B 1 352 ? -12.24800 53.68200  15.58500  1.000 37.25101  ? 328  ARG   B NH1 1 
ATOM   5662 N NH2 . ARG   B 1 352 ? -13.90300 52.28900  16.33700  1.000 47.03712  ? 328  ARG   B NH2 1 
ATOM   5663 N N   . SER   B 1 353 ? -9.06800  47.76500  17.51300  1.000 42.94812  ? 329  SER   B N   1 
ATOM   5664 C CA  . SER   B 1 353 ? -9.12900  46.96400  18.72200  1.000 44.19666  ? 329  SER   B CA  1 
ATOM   5665 C C   . SER   B 1 353 ? -7.74200  46.87800  19.34600  1.000 50.97281  ? 329  SER   B C   1 
ATOM   5666 O O   . SER   B 1 353 ? -6.77600  46.54900  18.64800  1.000 53.67072  ? 329  SER   B O   1 
ATOM   5667 C CB  . SER   B 1 353 ? -9.64800  45.56400  18.40800  1.000 48.03416  ? 329  SER   B CB  1 
ATOM   5668 O OG  . SER   B 1 353 ? -9.42500  44.68400  19.49600  1.000 49.89118  ? 329  SER   B OG  1 
ATOM   5669 N N   . PRO   B 1 354 ? -7.59400  47.18200  20.63700  1.000 56.63322  ? 330  PRO   B N   1 
ATOM   5670 C CA  . PRO   B 1 354 ? -6.30800  46.91300  21.30000  1.000 52.35918  ? 330  PRO   B CA  1 
ATOM   5671 C C   . PRO   B 1 354 ? -5.95400  45.43800  21.31500  1.000 51.74313  ? 330  PRO   B C   1 
ATOM   5672 O O   . PRO   B 1 354 ? -4.76600  45.08800  21.28100  1.000 42.21196  ? 330  PRO   B O   1 
ATOM   5673 C CB  . PRO   B 1 354 ? -6.52700  47.45900  22.71900  1.000 40.38023  ? 330  PRO   B CB  1 
ATOM   5674 C CG  . PRO   B 1 354 ? -7.63800  48.44200  22.58300  1.000 46.55050  ? 330  PRO   B CG  1 
ATOM   5675 C CD  . PRO   B 1 354 ? -8.53500  47.88900  21.52000  1.000 53.13419  ? 330  PRO   B CD  1 
ATOM   5676 N N   . ASP   B 1 355 ? -6.96400  44.56500  21.35000  1.000 54.15744  ? 331  ASP   B N   1 
ATOM   5677 C CA  . ASP   B 1 355 ? -6.72300  43.12600  21.39800  1.000 53.95263  ? 331  ASP   B CA  1 
ATOM   5678 C C   . ASP   B 1 355 ? -6.02700  42.63500  20.13500  1.000 50.40198  ? 331  ASP   B C   1 
ATOM   5679 O O   . ASP   B 1 355 ? -5.17200  41.74500  20.19600  1.000 57.12731  ? 331  ASP   B O   1 
ATOM   5680 C CB  . ASP   B 1 355 ? -8.05000  42.39300  21.60000  1.000 55.88545  ? 331  ASP   B CB  1 
ATOM   5681 C CG  . ASP   B 1 355 ? -8.46600  42.32600  23.05900  1.000 59.02057  ? 331  ASP   B CG  1 
ATOM   5682 O OD1 . ASP   B 1 355 ? -7.63900  41.91300  23.89900  1.000 67.29922  ? 331  ASP   B OD1 1 
ATOM   5683 O OD2 . ASP   B 1 355 ? -9.61300  42.71200  23.37100  1.000 48.55867  ? 331  ASP   B OD2 1 
ATOM   5684 N N   . PHE   B 1 356 ? -6.37800  43.20300  18.98100  1.000 48.06247  ? 332  PHE   B N   1 
ATOM   5685 C CA  . PHE   B 1 356 ? -5.78800  42.74500  17.72800  1.000 47.37908  ? 332  PHE   B CA  1 
ATOM   5686 C C   . PHE   B 1 356 ? -4.38400  43.30500  17.53000  1.000 42.73381  ? 332  PHE   B C   1 
ATOM   5687 O O   . PHE   B 1 356 ? -3.50700  42.60600  17.00900  1.000 42.36270  ? 332  PHE   B O   1 
ATOM   5688 C CB  . PHE   B 1 356 ? -6.69000  43.12200  16.54800  1.000 47.84286  ? 332  PHE   B CB  1 
ATOM   5689 C CG  . PHE   B 1 356 ? -7.85800  42.19000  16.34300  1.000 41.87759  ? 332  PHE   B CG  1 
ATOM   5690 C CD1 . PHE   B 1 356 ? -8.43600  41.52600  17.40900  1.000 54.88398  ? 332  PHE   B CD1 1 
ATOM   5691 C CD2 . PHE   B 1 356 ? -8.37800  41.98400  15.08300  1.000 48.92598  ? 332  PHE   B CD2 1 
ATOM   5692 C CE1 . PHE   B 1 356 ? -9.51100  40.67400  17.21400  1.000 52.99614  ? 332  PHE   B CE1 1 
ATOM   5693 C CE2 . PHE   B 1 356 ? -9.45200  41.13500  14.88500  1.000 52.78767  ? 332  PHE   B CE2 1 
ATOM   5694 C CZ  . PHE   B 1 356 ? -10.01800 40.48000  15.95000  1.000 39.84332  ? 332  PHE   B CZ  1 
ATOM   5695 N N   . ARG   B 1 357 ? -4.14900  44.55700  17.93700  1.000 42.04371  ? 333  ARG   B N   1 
ATOM   5696 C CA  . ARG   B 1 357 ? -2.82000  45.14800  17.79500  1.000 44.65120  ? 333  ARG   B CA  1 
ATOM   5697 C C   . ARG   B 1 357 ? -1.77300  44.34400  18.55200  1.000 46.94355  ? 333  ARG   B C   1 
ATOM   5698 O O   . ARG   B 1 357 ? -0.70000  44.04300  18.01800  1.000 46.22241  ? 333  ARG   B O   1 
ATOM   5699 C CB  . ARG   B 1 357 ? -2.82700  46.59500  18.27800  1.000 43.87439  ? 333  ARG   B CB  1 
ATOM   5700 C CG  . ARG   B 1 357 ? -3.38200  47.57500  17.27600  1.000 50.03602  ? 333  ARG   B CG  1 
ATOM   5701 C CD  . ARG   B 1 357 ? -3.40600  48.97600  17.85000  1.000 51.38866  ? 333  ARG   B CD  1 
ATOM   5702 N NE  . ARG   B 1 357 ? -4.19000  49.03500  19.07600  1.000 54.32350  ? 333  ARG   B NE  1 
ATOM   5703 C CZ  . ARG   B 1 357 ? -4.56500  50.15900  19.67000  1.000 62.58570  ? 333  ARG   B CZ  1 
ATOM   5704 N NH1 . ARG   B 1 357 ? -4.25300  51.34300  19.17000  1.000 72.54411  ? 333  ARG   B NH1 1 
ATOM   5705 N NH2 . ARG   B 1 357 ? -5.27700  50.09300  20.79200  1.000 63.13265  ? 333  ARG   B NH2 1 
ATOM   5706 N N   . ILE   B 1 358 ? -2.06700  43.99100  19.80500  1.000 47.67036  ? 334  ILE   B N   1 
ATOM   5707 C CA  . ILE   B 1 358 ? -1.13200  43.18600  20.58600  1.000 50.64892  ? 334  ILE   B CA  1 
ATOM   5708 C C   . ILE   B 1 358 ? -0.85400  41.86000  19.89200  1.000 47.56243  ? 334  ILE   B C   1 
ATOM   5709 O O   . ILE   B 1 358 ? 0.26000   41.32600  19.97500  1.000 50.18313  ? 334  ILE   B O   1 
ATOM   5710 C CB  . ILE   B 1 358 ? -1.67300  42.98700  22.01600  1.000 47.07551  ? 334  ILE   B CB  1 
ATOM   5711 C CG1 . ILE   B 1 358 ? -1.88100  44.34400  22.69200  1.000 51.43690  ? 334  ILE   B CG1 1 
ATOM   5712 C CG2 . ILE   B 1 358 ? -0.72600  42.13600  22.83500  1.000 46.61262  ? 334  ILE   B CG2 1 
ATOM   5713 C CD1 . ILE   B 1 358 ? -0.68900  45.27900  22.57800  1.000 45.42996  ? 334  ILE   B CD1 1 
ATOM   5714 N N   . ALA   B 1 359 ? -1.84300  41.31500  19.18300  1.000 45.25429  ? 335  ALA   B N   1 
ATOM   5715 C CA  . ALA   B 1 359 ? -1.60700  40.10600  18.40100  1.000 50.21161  ? 335  ALA   B CA  1 
ATOM   5716 C C   . ALA   B 1 359 ? -0.70200  40.40000  17.20800  1.000 49.13918  ? 335  ALA   B C   1 
ATOM   5717 O O   . ALA   B 1 359 ? 0.26100   39.66600  16.94900  1.000 44.51501  ? 335  ALA   B O   1 
ATOM   5718 C CB  . ALA   B 1 359 ? -2.93800  39.50900  17.94400  1.000 38.53232  ? 335  ALA   B CB  1 
ATOM   5719 N N   . PHE   B 1 360 ? -0.99500  41.47800  16.47600  1.000 44.92228  ? 336  PHE   B N   1 
ATOM   5720 C CA  . PHE   B 1 360 ? -0.17000  41.85500  15.33300  1.000 43.09366  ? 336  PHE   B CA  1 
ATOM   5721 C C   . PHE   B 1 360 ? 1.26100   42.14800  15.76400  1.000 45.58607  ? 336  PHE   B C   1 
ATOM   5722 O O   . PHE   B 1 360 ? 2.22100   41.67000  15.14700  1.000 43.70835  ? 336  PHE   B O   1 
ATOM   5723 C CB  . PHE   B 1 360 ? -0.77300  43.07300  14.63100  1.000 40.03497  ? 336  PHE   B CB  1 
ATOM   5724 C CG  . PHE   B 1 360 ? -2.11800  42.82000  14.00900  1.000 40.59323  ? 336  PHE   B CG  1 
ATOM   5725 C CD1 . PHE   B 1 360 ? -2.46900  41.55600  13.56700  1.000 40.62078  ? 336  PHE   B CD1 1 
ATOM   5726 C CD2 . PHE   B 1 360 ? -3.02500  43.85700  13.85000  1.000 38.16228  ? 336  PHE   B CD2 1 
ATOM   5727 C CE1 . PHE   B 1 360 ? -3.70300  41.32800  12.99200  1.000 38.97759  ? 336  PHE   B CE1 1 
ATOM   5728 C CE2 . PHE   B 1 360 ? -4.26000  43.63500  13.27500  1.000 33.71823  ? 336  PHE   B CE2 1 
ATOM   5729 C CZ  . PHE   B 1 360 ? -4.59900  42.36900  12.84600  1.000 38.20962  ? 336  PHE   B CZ  1 
ATOM   5730 N N   . GLN   B 1 361 ? 1.41800   42.93700  16.83000  1.000 52.00511  ? 337  GLN   B N   1 
ATOM   5731 C CA  . GLN   B 1 361 ? 2.74700   43.32600  17.29200  1.000 51.81049  ? 337  GLN   B CA  1 
ATOM   5732 C C   . GLN   B 1 361 ? 3.58300   42.11000  17.66900  1.000 48.99236  ? 337  GLN   B C   1 
ATOM   5733 O O   . GLN   B 1 361 ? 4.77900   42.05200  17.36000  1.000 51.00292  ? 337  GLN   B O   1 
ATOM   5734 C CB  . GLN   B 1 361 ? 2.61700   44.28900  18.47300  1.000 50.94413  ? 337  GLN   B CB  1 
ATOM   5735 C CG  . GLN   B 1 361 ? 1.98200   45.61900  18.08500  1.000 56.05391  ? 337  GLN   B CG  1 
ATOM   5736 C CD  . GLN   B 1 361 ? 1.62300   46.48700  19.27500  1.000 53.85891  ? 337  GLN   B CD  1 
ATOM   5737 O OE1 . GLN   B 1 361 ? 1.72600   46.06300  20.42500  1.000 56.18567  ? 337  GLN   B OE1 1 
ATOM   5738 N NE2 . GLN   B 1 361 ? 1.19800   47.71400  19.00000  1.000 54.24712  ? 337  GLN   B NE2 1 
ATOM   5739 N N   . GLU   B 1 362 ? 2.97200   41.12400  18.32900  1.000 44.68916  ? 338  GLU   B N   1 
ATOM   5740 C CA  . GLU   B 1 362 ? 3.69100   39.89200  18.63600  1.000 46.53651  ? 338  GLU   B CA  1 
ATOM   5741 C C   . GLU   B 1 362 ? 4.04500   39.13200  17.36200  1.000 53.60434  ? 338  GLU   B C   1 
ATOM   5742 O O   . GLU   B 1 362 ? 5.15400   38.59800  17.23700  1.000 51.98952  ? 338  GLU   B O   1 
ATOM   5743 C CB  . GLU   B 1 362 ? 2.85700   39.01900  19.57600  1.000 49.86506  ? 338  GLU   B CB  1 
ATOM   5744 C CG  . GLU   B 1 362 ? 3.62700   37.88500  20.25100  1.000 53.67921  ? 338  GLU   B CG  1 
ATOM   5745 C CD  . GLU   B 1 362 ? 3.48700   36.54800  19.53600  1.000 59.53177  ? 338  GLU   B CD  1 
ATOM   5746 O OE1 . GLU   B 1 362 ? 3.26500   36.53500  18.30700  1.000 63.52398  ? 338  GLU   B OE1 1 
ATOM   5747 O OE2 . GLU   B 1 362 ? 3.60900   35.50300  20.21000  1.000 61.02527  ? 338  GLU   B OE2 1 
ATOM   5748 N N   . LEU   B 1 363 ? 3.11700   39.08000  16.40300  1.000 52.46684  ? 339  LEU   B N   1 
ATOM   5749 C CA  . LEU   B 1 363 ? 3.32700   38.33600  15.16700  1.000 50.66854  ? 339  LEU   B CA  1 
ATOM   5750 C C   . LEU   B 1 363 ? 4.42800   38.92000  14.29100  1.000 50.53046  ? 339  LEU   B C   1 
ATOM   5751 O O   . LEU   B 1 363 ? 4.85300   38.25500  13.33900  1.000 43.38480  ? 339  LEU   B O   1 
ATOM   5752 C CB  . LEU   B 1 363 ? 2.02200   38.27200  14.36700  1.000 43.89212  ? 339  LEU   B CB  1 
ATOM   5753 C CG  . LEU   B 1 363 ? 0.97600   37.25000  14.81600  1.000 41.12570  ? 339  LEU   B CG  1 
ATOM   5754 C CD1 . LEU   B 1 363 ? -0.17300  37.20700  13.82900  1.000 39.35304  ? 339  LEU   B CD1 1 
ATOM   5755 C CD2 . LEU   B 1 363 ? 1.59600   35.87300  14.97000  1.000 35.54814  ? 339  LEU   B CD2 1 
ATOM   5756 N N   . LEU   B 1 364 ? 4.90300   40.13300  14.58400  1.000 48.07627  ? 340  LEU   B N   1 
ATOM   5757 C CA  . LEU   B 1 364 ? 5.85900   40.81900  13.72200  1.000 46.60858  ? 340  LEU   B CA  1 
ATOM   5758 C C   . LEU   B 1 364 ? 7.14200   41.20000  14.45600  1.000 52.93294  ? 340  LEU   B C   1 
ATOM   5759 O O   . LEU   B 1 364 ? 7.83400   42.13000  14.03300  1.000 56.25018  ? 340  LEU   B O   1 
ATOM   5760 C CB  . LEU   B 1 364 ? 5.21500   42.06200  13.10600  1.000 42.96267  ? 340  LEU   B CB  1 
ATOM   5761 C CG  . LEU   B 1 364 ? 3.95000   41.81800  12.27700  1.000 44.17785  ? 340  LEU   B CG  1 
ATOM   5762 C CD1 . LEU   B 1 364 ? 3.28100   43.13100  11.89100  1.000 35.59624  ? 340  LEU   B CD1 1 
ATOM   5763 C CD2 . LEU   B 1 364 ? 4.27000   40.99700  11.04100  1.000 38.61118  ? 340  LEU   B CD2 1 
ATOM   5764 N N   . CYS   B 1 365 ? 7.47000   40.50200  15.54600  1.000 49.55384  ? 341  CYS   B N   1 
ATOM   5765 C CA  . CYS   B 1 365 ? 8.68400   40.74800  16.32800  1.000 43.54952  ? 341  CYS   B CA  1 
ATOM   5766 C C   . CYS   B 1 365 ? 8.74400   42.18600  16.84100  1.000 49.94730  ? 341  CYS   B C   1 
ATOM   5767 O O   . CYS   B 1 365 ? 9.70600   42.91800  16.60400  1.000 55.60710  ? 341  CYS   B O   1 
ATOM   5768 C CB  . CYS   B 1 365 ? 9.93800   40.42300  15.52000  1.000 51.78863  ? 341  CYS   B CB  1 
ATOM   5769 S SG  . CYS   B 1 365 ? 10.04100  38.73500  14.97800  1.000 65.03881  ? 341  CYS   B SG  1 
ATOM   5770 N N   . LEU   B 1 366 ? 7.70200   42.58000  17.56100  1.000 51.19465  ? 342  LEU   B N   1 
ATOM   5771 C CA  . LEU   B 1 366 ? 7.63400   43.93300  18.09400  1.000 42.95139  ? 342  LEU   B CA  1 
ATOM   5772 C C   . LEU   B 1 366 ? 7.29000   43.91800  19.58200  1.000 54.85366  ? 342  LEU   B C   1 
ATOM   5773 O O   . LEU   B 1 366 ? 7.45500   42.90000  20.26200  1.000 53.20937  ? 342  LEU   B O   1 
ATOM   5774 C CB  . LEU   B 1 366 ? 6.60900   44.76000  17.30900  1.000 48.83504  ? 342  LEU   B CB  1 
ATOM   5775 C CG  . LEU   B 1 366 ? 6.65300   44.65500  15.77800  1.000 47.10862  ? 342  LEU   B CG  1 
ATOM   5776 C CD1 . LEU   B 1 366 ? 5.50300   45.40900  15.13500  1.000 45.92691  ? 342  LEU   B CD1 1 
ATOM   5777 C CD2 . LEU   B 1 366 ? 7.97200   45.17300  15.24100  1.000 49.02404  ? 342  LEU   B CD2 1 
ATOM   5778 N N   . ASN   B 1 390 ? -26.84900 52.63300  32.23000  1.000 67.38105  ? 1002 ASN   B N   1 
ATOM   5779 C CA  . ASN   B 1 390 ? -26.41900 51.85800  33.38700  1.000 63.28477  ? 1002 ASN   B CA  1 
ATOM   5780 C C   . ASN   B 1 390 ? -25.44900 52.67500  34.23500  1.000 67.32240  ? 1002 ASN   B C   1 
ATOM   5781 O O   . ASN   B 1 390 ? -24.43800 53.17100  33.73900  1.000 64.36417  ? 1002 ASN   B O   1 
ATOM   5782 C CB  . ASN   B 1 390 ? -25.77400 50.54700  32.93900  1.000 66.46102  ? 1002 ASN   B CB  1 
ATOM   5783 C CG  . ASN   B 1 390 ? -25.38000 49.65500  34.09800  1.000 64.73337  ? 1002 ASN   B CG  1 
ATOM   5784 O OD1 . ASN   B 1 390 ? -25.51900 50.02200  35.26200  1.000 72.48526  ? 1002 ASN   B OD1 1 
ATOM   5785 N ND2 . ASN   B 1 390 ? -24.87600 48.46900  33.77900  1.000 73.38554  ? 1002 ASN   B ND2 1 
ATOM   5786 N N   . ILE   B 1 391 ? -25.77100 52.79300  35.52500  1.000 76.13584  ? 1003 ILE   B N   1 
ATOM   5787 C CA  . ILE   B 1 391 ? -24.99900 53.64300  36.42800  1.000 73.91466  ? 1003 ILE   B CA  1 
ATOM   5788 C C   . ILE   B 1 391 ? -23.58500 53.09800  36.61200  1.000 69.88262  ? 1003 ILE   B C   1 
ATOM   5789 O O   . ILE   B 1 391 ? -22.60400 53.84800  36.56300  1.000 65.00447  ? 1003 ILE   B O   1 
ATOM   5790 C CB  . ILE   B 1 391 ? -25.73600 53.78800  37.77200  1.000 68.59643  ? 1003 ILE   B CB  1 
ATOM   5791 C CG1 . ILE   B 1 391 ? -24.88800 54.57500  38.77100  1.000 74.39223  ? 1003 ILE   B CG1 1 
ATOM   5792 C CG2 . ILE   B 1 391 ? -26.14700 52.42600  38.32500  1.000 70.12708  ? 1003 ILE   B CG2 1 
ATOM   5793 C CD1 . ILE   B 1 391 ? -24.73000 56.01700  38.41500  1.000 71.79416  ? 1003 ILE   B CD1 1 
ATOM   5794 N N   . PHE   B 1 392 ? -23.46200 51.78300  36.82100  1.000 71.35299  ? 1004 PHE   B N   1 
ATOM   5795 C CA  . PHE   B 1 392 ? -22.15100 51.17300  37.02400  1.000 71.82949  ? 1004 PHE   B CA  1 
ATOM   5796 C C   . PHE   B 1 392 ? -21.24800 51.39600  35.81700  1.000 71.29124  ? 1004 PHE   B C   1 
ATOM   5797 O O   . PHE   B 1 392 ? -20.08800 51.80400  35.95800  1.000 71.45638  ? 1004 PHE   B O   1 
ATOM   5798 C CB  . PHE   B 1 392 ? -22.31000 49.67700  37.30100  1.000 72.03636  ? 1004 PHE   B CB  1 
ATOM   5799 C CG  . PHE   B 1 392 ? -23.32000 49.35900  38.36400  1.000 73.02845  ? 1004 PHE   B CG  1 
ATOM   5800 C CD1 . PHE   B 1 392 ? -22.96400 49.37300  39.70200  1.000 82.88552  ? 1004 PHE   B CD1 1 
ATOM   5801 C CD2 . PHE   B 1 392 ? -24.62600 49.03700  38.02600  1.000 70.68307  ? 1004 PHE   B CD2 1 
ATOM   5802 C CE1 . PHE   B 1 392 ? -23.89500 49.07700  40.68600  1.000 84.85908  ? 1004 PHE   B CE1 1 
ATOM   5803 C CE2 . PHE   B 1 392 ? -25.56100 48.74100  39.00300  1.000 77.56680  ? 1004 PHE   B CE2 1 
ATOM   5804 C CZ  . PHE   B 1 392 ? -25.19500 48.76000  40.33500  1.000 80.27250  ? 1004 PHE   B CZ  1 
ATOM   5805 N N   . GLU   B 1 393 ? -21.76600 51.12400  34.61600  1.000 70.83176  ? 1005 GLU   B N   1 
ATOM   5806 C CA  . GLU   B 1 393 ? -20.99200 51.35800  33.40100  1.000 68.55811  ? 1005 GLU   B CA  1 
ATOM   5807 C C   . GLU   B 1 393 ? -20.61400 52.82500  33.26400  1.000 67.46391  ? 1005 GLU   B C   1 
ATOM   5808 O O   . GLU   B 1 393 ? -19.49200 53.14800  32.85600  1.000 64.68698  ? 1005 GLU   B O   1 
ATOM   5809 C CB  . GLU   B 1 393 ? -21.78600 50.90500  32.17600  1.000 61.58896  ? 1005 GLU   B CB  1 
ATOM   5810 C CG  . GLU   B 1 393 ? -22.01600 49.40900  32.09100  1.000 60.77294  ? 1005 GLU   B CG  1 
ATOM   5811 C CD  . GLU   B 1 393 ? -22.99200 49.03500  30.99100  1.000 70.42113  ? 1005 GLU   B CD  1 
ATOM   5812 O OE1 . GLU   B 1 393 ? -23.69100 49.93500  30.47600  1.000 68.86446  ? 1005 GLU   B OE1 1 
ATOM   5813 O OE2 . GLU   B 1 393 ? -23.05900 47.83900  30.64000  1.000 76.59745  ? 1005 GLU   B OE2 1 
ATOM   5814 N N   . MET   B 1 394 ? -21.54000 53.72600  33.60100  1.000 70.70100  ? 1006 MET   B N   1 
ATOM   5815 C CA  . MET   B 1 394 ? -21.28000 55.15400  33.45400  1.000 72.58490  ? 1006 MET   B CA  1 
ATOM   5816 C C   . MET   B 1 394 ? -20.06000 55.58800  34.25600  1.000 74.76207  ? 1006 MET   B C   1 
ATOM   5817 O O   . MET   B 1 394 ? -19.26000 56.40500  33.78600  1.000 73.89777  ? 1006 MET   B O   1 
ATOM   5818 C CB  . MET   B 1 394 ? -22.51100 55.95700  33.87500  1.000 74.01360  ? 1006 MET   B CB  1 
ATOM   5819 C CG  . MET   B 1 394 ? -22.29800 57.46400  33.88800  1.000 75.40832  ? 1006 MET   B CG  1 
ATOM   5820 S SD  . MET   B 1 394 ? -23.66300 58.32500  34.69000  1.000 80.01411  ? 1006 MET   B SD  1 
ATOM   5821 C CE  . MET   B 1 394 ? -23.10500 60.02400  34.59800  1.000 73.15035  ? 1006 MET   B CE  1 
ATOM   5822 N N   . LEU   B 1 395 ? -19.89000 55.04200  35.46200  1.000 70.51712  ? 1007 LEU   B N   1 
ATOM   5823 C CA  . LEU   B 1 395 ? -18.79800 55.48800  36.32000  1.000 73.16016  ? 1007 LEU   B CA  1 
ATOM   5824 C C   . LEU   B 1 395 ? -17.47400 54.80900  36.00500  1.000 71.52719  ? 1007 LEU   B C   1 
ATOM   5825 O O   . LEU   B 1 395 ? -16.41800 55.43000  36.17400  1.000 66.91395  ? 1007 LEU   B O   1 
ATOM   5826 C CB  . LEU   B 1 395 ? -19.16700 55.28900  37.78400  1.000 78.10351  ? 1007 LEU   B CB  1 
ATOM   5827 C CG  . LEU   B 1 395 ? -19.90300 56.52300  38.29500  1.000 80.36780  ? 1007 LEU   B CG  1 
ATOM   5828 C CD1 . LEU   B 1 395 ? -21.37100 56.42600  38.01400  1.000 82.31962  ? 1007 LEU   B CD1 1 
ATOM   5829 C CD2 . LEU   B 1 395 ? -19.67500 56.64300  39.75700  1.000 76.24802  ? 1007 LEU   B CD2 1 
ATOM   5830 N N   . ARG   B 1 396 ? -17.49100 53.55500  35.55100  1.000 69.93576  ? 1008 ARG   B N   1 
ATOM   5831 C CA  . ARG   B 1 396 ? -16.24700 52.95900  35.07400  1.000 72.24268  ? 1008 ARG   B CA  1 
ATOM   5832 C C   . ARG   B 1 396 ? -15.67100 53.76500  33.91300  1.000 69.47408  ? 1008 ARG   B C   1 
ATOM   5833 O O   . ARG   B 1 396 ? -14.44800 53.86300  33.76800  1.000 69.30853  ? 1008 ARG   B O   1 
ATOM   5834 C CB  . ARG   B 1 396 ? -16.48000 51.50100  34.66600  1.000 68.12487  ? 1008 ARG   B CB  1 
ATOM   5835 C CG  . ARG   B 1 396 ? -15.30300 50.85500  33.93800  1.000 62.46643  ? 1008 ARG   B CG  1 
ATOM   5836 C CD  . ARG   B 1 396 ? -14.01600 50.96100  34.74800  1.000 63.12620  ? 1008 ARG   B CD  1 
ATOM   5837 N NE  . ARG   B 1 396 ? -12.87900 51.32800  33.91100  1.000 69.31540  ? 1008 ARG   B NE  1 
ATOM   5838 C CZ  . ARG   B 1 396 ? -12.18900 50.48500  33.15600  1.000 73.83105  ? 1008 ARG   B CZ  1 
ATOM   5839 N NH1 . ARG   B 1 396 ? -12.47100 49.19300  33.12900  1.000 71.51178  ? 1008 ARG   B NH1 1 
ATOM   5840 N NH2 . ARG   B 1 396 ? -11.19000 50.95100  32.40900  1.000 66.87660  ? 1008 ARG   B NH2 1 
ATOM   5841 N N   . ILE   B 1 397 ? -16.53800 54.38100  33.10500  1.000 70.09754  ? 1009 ILE   B N   1 
ATOM   5842 C CA  . ILE   B 1 397 ? -16.07500 55.17400  31.96800  1.000 71.77971  ? 1009 ILE   B CA  1 
ATOM   5843 C C   . ILE   B 1 397 ? -15.23200 56.35700  32.43300  1.000 75.10984  ? 1009 ILE   B C   1 
ATOM   5844 O O   . ILE   B 1 397 ? -14.17200 56.64200  31.86200  1.000 77.29388  ? 1009 ILE   B O   1 
ATOM   5845 C CB  . ILE   B 1 397 ? -17.27300 55.63500  31.11500  1.000 67.17165  ? 1009 ILE   B CB  1 
ATOM   5846 C CG1 . ILE   B 1 397 ? -17.86100 54.45100  30.34600  1.000 61.88201  ? 1009 ILE   B CG1 1 
ATOM   5847 C CG2 . ILE   B 1 397 ? -16.86700 56.75600  30.16500  1.000 61.10308  ? 1009 ILE   B CG2 1 
ATOM   5848 C CD1 . ILE   B 1 397 ? -19.17100 54.75500  29.65800  1.000 64.98653  ? 1009 ILE   B CD1 1 
ATOM   5849 N N   . ASP   B 1 398 ? -15.67900 57.06300  33.47200  1.000 74.09144  ? 1010 ASP   B N   1 
ATOM   5850 C CA  . ASP   B 1 398 ? -15.04300 58.31300  33.86800  1.000 73.96423  ? 1010 ASP   B CA  1 
ATOM   5851 C C   . ASP   B 1 398 ? -14.29100 58.22700  35.18800  1.000 71.17715  ? 1010 ASP   B C   1 
ATOM   5852 O O   . ASP   B 1 398 ? -13.66600 59.21400  35.58700  1.000 74.02767  ? 1010 ASP   B O   1 
ATOM   5853 C CB  . ASP   B 1 398 ? -16.08200 59.43700  33.94000  1.000 77.75182  ? 1010 ASP   B CB  1 
ATOM   5854 C CG  . ASP   B 1 398 ? -17.34900 59.00600  34.63100  1.000 80.42883  ? 1010 ASP   B CG  1 
ATOM   5855 O OD1 . ASP   B 1 398 ? -17.37100 57.87100  35.13900  1.000 75.23455  ? 1010 ASP   B OD1 1 
ATOM   5856 O OD2 . ASP   B 1 398 ? -18.32400 59.78900  34.65000  1.000 82.81543  ? 1010 ASP   B OD2 1 
ATOM   5857 N N   . GLU   B 1 399 ? -14.33400 57.08700  35.87900  1.000 74.35913  ? 1011 GLU   B N   1 
ATOM   5858 C CA  . GLU   B 1 399 ? -13.46000 56.86800  37.02400  1.000 76.77034  ? 1011 GLU   B CA  1 
ATOM   5859 C C   . GLU   B 1 399 ? -12.22500 56.04600  36.67800  1.000 72.44354  ? 1011 GLU   B C   1 
ATOM   5860 O O   . GLU   B 1 399 ? -11.24100 56.09500  37.42600  1.000 71.38233  ? 1011 GLU   B O   1 
ATOM   5861 C CB  . GLU   B 1 399 ? -14.21300 56.16400  38.16300  1.000 72.98872  ? 1011 GLU   B CB  1 
ATOM   5862 C CG  . GLU   B 1 399 ? -15.24300 57.01000  38.90200  1.000 77.98527  ? 1011 GLU   B CG  1 
ATOM   5863 C CD  . GLU   B 1 399 ? -14.61800 58.11800  39.73100  1.000 83.84802  ? 1011 GLU   B CD  1 
ATOM   5864 O OE1 . GLU   B 1 399 ? -13.42600 57.99900  40.08800  1.000 83.45027  ? 1011 GLU   B OE1 1 
ATOM   5865 O OE2 . GLU   B 1 399 ? -15.32600 59.09900  40.04100  1.000 88.41717  ? 1011 GLU   B OE2 1 
ATOM   5866 N N   . GLY   B 1 400 ? -12.25700 55.29400  35.57700  1.000 63.89502  ? 1012 GLY   B N   1 
ATOM   5867 C CA  . GLY   B 1 400 ? -11.17200 54.40200  35.21400  1.000 62.93780  ? 1012 GLY   B CA  1 
ATOM   5868 C C   . GLY   B 1 400 ? -10.98900 53.26600  36.20000  1.000 68.98646  ? 1012 GLY   B C   1 
ATOM   5869 O O   . GLY   B 1 400 ? -11.61600 53.25500  37.26300  1.000 72.60422  ? 1012 GLY   B O   1 
ATOM   5870 N N   . LEU   B 1 401 ? -10.13900 52.29700  35.86800  1.000 68.17613  ? 1013 LEU   B N   1 
ATOM   5871 C CA  . LEU   B 1 401 ? -9.81100  51.21800  36.79000  1.000 71.10222  ? 1013 LEU   B CA  1 
ATOM   5872 C C   . LEU   B 1 401 ? -8.30000  51.06900  36.87900  1.000 77.30592  ? 1013 LEU   B C   1 
ATOM   5873 O O   . LEU   B 1 401 ? -7.60800  51.04900  35.85600  1.000 76.15762  ? 1013 LEU   B O   1 
ATOM   5874 C CB  . LEU   B 1 401 ? -10.45600 49.89100  36.36900  1.000 64.94752  ? 1013 LEU   B CB  1 
ATOM   5875 C CG  . LEU   B 1 401 ? -10.07500 48.68200  37.23200  1.000 65.15730  ? 1013 LEU   B CG  1 
ATOM   5876 C CD1 . LEU   B 1 401 ? -11.30500 47.90100  37.64900  1.000 65.48006  ? 1013 LEU   B CD1 1 
ATOM   5877 C CD2 . LEU   B 1 401 ? -9.10300  47.77400  36.49700  1.000 67.39695  ? 1013 LEU   B CD2 1 
ATOM   5878 N N   . ARG   B 1 402 ? -7.80000  50.97100  38.10900  1.000 75.15074  ? 1014 ARG   B N   1 
ATOM   5879 C CA  . ARG   B 1 402 ? -6.38700  50.76000  38.38700  1.000 75.72525  ? 1014 ARG   B CA  1 
ATOM   5880 C C   . ARG   B 1 402 ? -6.28100  49.80600  39.56600  1.000 80.24486  ? 1014 ARG   B C   1 
ATOM   5881 O O   . ARG   B 1 402 ? -6.96800  49.98500  40.57600  1.000 80.84199  ? 1014 ARG   B O   1 
ATOM   5882 C CB  . ARG   B 1 402 ? -5.67600  52.08600  38.69000  1.000 80.51559  ? 1014 ARG   B CB  1 
ATOM   5883 C CG  . ARG   B 1 402 ? -4.26200  51.95600  39.25500  1.000 87.53583  ? 1014 ARG   B CG  1 
ATOM   5884 C CD  . ARG   B 1 402 ? -3.19800  51.72800  38.18100  1.000 87.53110  ? 1014 ARG   B CD  1 
ATOM   5885 N NE  . ARG   B 1 402 ? -3.31500  50.43700  37.51400  1.000 84.95937  ? 1014 ARG   B NE  1 
ATOM   5886 C CZ  . ARG   B 1 402 ? -2.51400  50.02500  36.54000  1.000 83.49195  ? 1014 ARG   B CZ  1 
ATOM   5887 N NH1 . ARG   B 1 402 ? -1.51600  50.77600  36.10400  1.000 80.57534  ? 1014 ARG   B NH1 1 
ATOM   5888 N NH2 . ARG   B 1 402 ? -2.71700  48.82900  35.99500  1.000 87.17221  ? 1014 ARG   B NH2 1 
ATOM   5889 N N   . LEU   B 1 403 ? -5.42700  48.79300  39.43700  1.000 83.91496  ? 1015 LEU   B N   1 
ATOM   5890 C CA  . LEU   B 1 403 ? -5.35600  47.71600  40.41800  1.000 87.54818  ? 1015 LEU   B CA  1 
ATOM   5891 C C   . LEU   B 1 403 ? -4.35800  47.97700  41.53900  1.000 88.20058  ? 1015 LEU   B C   1 
ATOM   5892 O O   . LEU   B 1 403 ? -4.16100  47.10000  42.38700  1.000 82.00689  ? 1015 LEU   B O   1 
ATOM   5893 C CB  . LEU   B 1 403 ? -5.01000  46.39600  39.72200  1.000 84.85364  ? 1015 LEU   B CB  1 
ATOM   5894 C CG  . LEU   B 1 403 ? -6.08600  45.89300  38.76100  1.000 79.33231  ? 1015 LEU   B CG  1 
ATOM   5895 C CD1 . LEU   B 1 403 ? -5.85100  44.44000  38.36800  1.000 76.74364  ? 1015 LEU   B CD1 1 
ATOM   5896 C CD2 . LEU   B 1 403 ? -7.45500  46.08000  39.39300  1.000 85.87948  ? 1015 LEU   B CD2 1 
ATOM   5897 N N   . LYS   B 1 404 ? -3.73100  49.15100  41.56900  1.000 89.27955  ? 1016 LYS   B N   1 
ATOM   5898 C CA  . LYS   B 1 404 ? -2.74300  49.46600  42.59300  1.000 87.58154  ? 1016 LYS   B CA  1 
ATOM   5899 C C   . LYS   B 1 404 ? -3.23100  50.63800  43.43400  1.000 93.17370  ? 1016 LYS   B C   1 
ATOM   5900 O O   . LYS   B 1 404 ? -4.44200  50.85600  43.55200  1.000 92.56486  ? 1016 LYS   B O   1 
ATOM   5901 C CB  . LYS   B 1 404 ? -1.39300  49.76900  41.93800  1.000 83.65356  ? 1016 LYS   B CB  1 
ATOM   5902 C CG  . LYS   B 1 404 ? -1.09700  48.85200  40.75400  1.000 87.14091  ? 1016 LYS   B CG  1 
ATOM   5903 C CD  . LYS   B 1 404 ? 0.25900   49.11600  40.11900  1.000 85.47981  ? 1016 LYS   B CD  1 
ATOM   5904 C CE  . LYS   B 1 404 ? 0.52900   48.11100  39.00100  1.000 76.12803  ? 1016 LYS   B CE  1 
ATOM   5905 N NZ  . LYS   B 1 404 ? 1.90900   48.21500  38.44500  1.000 75.24128  ? 1016 LYS   B NZ  1 
ATOM   5906 N N   . ILE   B 1 405 ? -2.31100  51.39400  44.02900  1.000 95.54136  ? 1017 ILE   B N   1 
ATOM   5907 C CA  . ILE   B 1 405 ? -2.63600  52.62100  44.74800  1.000 98.81211  ? 1017 ILE   B CA  1 
ATOM   5908 C C   . ILE   B 1 405 ? -2.04400  53.78800  43.97100  1.000 98.30279  ? 1017 ILE   B C   1 
ATOM   5909 O O   . ILE   B 1 405 ? -0.86500  53.75800  43.59600  1.000 98.88294  ? 1017 ILE   B O   1 
ATOM   5910 C CB  . ILE   B 1 405 ? -2.11300  52.59100  46.19600  1.000 100.22938 ? 1017 ILE   B CB  1 
ATOM   5911 C CG1 . ILE   B 1 405 ? -3.02800  51.73800  47.07800  1.000 98.70037  ? 1017 ILE   B CG1 1 
ATOM   5912 C CG2 . ILE   B 1 405 ? -2.00800  54.00300  46.76200  1.000 100.33496 ? 1017 ILE   B CG2 1 
ATOM   5913 C CD1 . ILE   B 1 405 ? -2.65100  51.76900  48.54800  1.000 100.50614 ? 1017 ILE   B CD1 1 
ATOM   5914 N N   . TYR   B 1 406 ? -2.86100  54.81000  43.72100  1.000 98.97213  ? 1018 TYR   B N   1 
ATOM   5915 C CA  . TYR   B 1 406 ? -2.45300  55.92600  42.88300  1.000 99.94998  ? 1018 TYR   B CA  1 
ATOM   5916 C C   . TYR   B 1 406 ? -2.97100  57.23300  43.46600  1.000 101.73286 ? 1018 TYR   B C   1 
ATOM   5917 O O   . TYR   B 1 406 ? -3.94300  57.26400  44.22500  1.000 98.77147  ? 1018 TYR   B O   1 
ATOM   5918 C CB  . TYR   B 1 406 ? -2.95200  55.75900  41.43700  1.000 95.46604  ? 1018 TYR   B CB  1 
ATOM   5919 C CG  . TYR   B 1 406 ? -4.44300  55.97000  41.27200  1.000 93.65090  ? 1018 TYR   B CG  1 
ATOM   5920 C CD1 . TYR   B 1 406 ? -5.35500  55.02600  41.73000  1.000 93.18516  ? 1018 TYR   B CD1 1 
ATOM   5921 C CD2 . TYR   B 1 406 ? -4.93800  57.11700  40.66600  1.000 94.26838  ? 1018 TYR   B CD2 1 
ATOM   5922 C CE1 . TYR   B 1 406 ? -6.71900  55.21700  41.58500  1.000 90.26682  ? 1018 TYR   B CE1 1 
ATOM   5923 C CE2 . TYR   B 1 406 ? -6.29900  57.31800  40.51600  1.000 93.34062  ? 1018 TYR   B CE2 1 
ATOM   5924 C CZ  . TYR   B 1 406 ? -7.18500  56.36500  40.97600  1.000 92.02049  ? 1018 TYR   B CZ  1 
ATOM   5925 O OH  . TYR   B 1 406 ? -8.54000  56.56300  40.82900  1.000 93.54123  ? 1018 TYR   B OH  1 
ATOM   5926 N N   . LYS   B 1 407 ? -2.29600  58.31700  43.09500  1.000 106.10606 ? 1019 LYS   B N   1 
ATOM   5927 C CA  . LYS   B 1 407 ? -2.69900  59.66400  43.47700  1.000 104.42570 ? 1019 LYS   B CA  1 
ATOM   5928 C C   . LYS   B 1 407 ? -3.74000  60.19200  42.49500  1.000 104.83476 ? 1019 LYS   B C   1 
ATOM   5929 O O   . LYS   B 1 407 ? -3.54600  60.12200  41.27700  1.000 110.50445 ? 1019 LYS   B O   1 
ATOM   5930 C CB  . LYS   B 1 407 ? -1.47000  60.57300  43.51100  1.000 107.62766 ? 1019 LYS   B CB  1 
ATOM   5931 C CG  . LYS   B 1 407 ? -1.73400  62.05500  43.32300  1.000 106.17486 ? 1019 LYS   B CG  1 
ATOM   5932 C CD  . LYS   B 1 407 ? -0.41600  62.79700  43.13800  1.000 105.89083 ? 1019 LYS   B CD  1 
ATOM   5933 C CE  . LYS   B 1 407 ? -0.53200  63.91100  42.11100  1.000 98.79065  ? 1019 LYS   B CE  1 
ATOM   5934 N NZ  . LYS   B 1 407 ? -0.95700  65.19600  42.73200  1.000 100.17150 ? 1019 LYS   B NZ  1 
ATOM   5935 N N   . ASP   B 1 408 ? -4.84700  60.71700  43.02200  1.000 102.79526 ? 1020 ASP   B N   1 
ATOM   5936 C CA  . ASP   B 1 408 ? -5.92600  61.20700  42.17500  1.000 106.58705 ? 1020 ASP   B CA  1 
ATOM   5937 C C   . ASP   B 1 408 ? -5.76100  62.70900  41.92800  1.000 107.88903 ? 1020 ASP   B C   1 
ATOM   5938 O O   . ASP   B 1 408 ? -4.72200  63.30300  42.23200  1.000 106.69227 ? 1020 ASP   B O   1 
ATOM   5939 C CB  . ASP   B 1 408 ? -7.28900  60.85000  42.77600  1.000 107.17367 ? 1020 ASP   B CB  1 
ATOM   5940 C CG  . ASP   B 1 408 ? -7.60000  61.60800  44.06000  1.000 109.76601 ? 1020 ASP   B CG  1 
ATOM   5941 O OD1 . ASP   B 1 408 ? -6.70000  62.27500  44.61200  1.000 109.67158 ? 1020 ASP   B OD1 1 
ATOM   5942 O OD2 . ASP   B 1 408 ? -8.76300  61.53700  44.51500  1.000 106.44418 ? 1020 ASP   B OD2 1 
ATOM   5943 N N   . THR   B 1 409 ? -6.80300  63.33900  41.37100  1.000 107.68406 ? 1021 THR   B N   1 
ATOM   5944 C CA  . THR   B 1 409 ? -6.69100  64.72400  40.92200  1.000 107.46256 ? 1021 THR   B CA  1 
ATOM   5945 C C   . THR   B 1 409 ? -6.44100  65.68400  42.07700  1.000 112.45448 ? 1021 THR   B C   1 
ATOM   5946 O O   . THR   B 1 409 ? -5.84400  66.74800  41.87800  1.000 115.43041 ? 1021 THR   B O   1 
ATOM   5947 C CB  . THR   B 1 409 ? -7.95400  65.13300  40.16500  1.000 109.18346 ? 1021 THR   B CB  1 
ATOM   5948 O OG1 . THR   B 1 409 ? -7.94900  66.55000  39.94600  1.000 107.10387 ? 1021 THR   B OG1 1 
ATOM   5949 C CG2 . THR   B 1 409 ? -9.19700  64.74700  40.95700  1.000 105.55659 ? 1021 THR   B CG2 1 
ATOM   5950 N N   . GLU   B 1 410 ? -6.88000  65.33400  43.28300  1.000 113.17157 ? 1022 GLU   B N   1 
ATOM   5951 C CA  . GLU   B 1 410 ? -6.66300  66.17300  44.45200  1.000 108.33712 ? 1022 GLU   B CA  1 
ATOM   5952 C C   . GLU   B 1 410 ? -5.53900  65.66100  45.34700  1.000 111.37957 ? 1022 GLU   B C   1 
ATOM   5953 O O   . GLU   B 1 410 ? -5.27900  66.25900  46.39500  1.000 118.16884 ? 1022 GLU   B O   1 
ATOM   5954 C CB  . GLU   B 1 410 ? -7.96500  66.30400  45.25100  1.000 106.76331 ? 1022 GLU   B CB  1 
ATOM   5955 C CG  . GLU   B 1 410 ? -9.05900  67.07200  44.50900  1.000 107.32209 ? 1022 GLU   B CG  1 
ATOM   5956 C CD  . GLU   B 1 410 ? -9.61800  68.23100  45.31300  1.000 107.47938 ? 1022 GLU   B CD  1 
ATOM   5957 O OE1 . GLU   B 1 410 ? -9.08700  68.50000  46.41000  1.000 111.63362 ? 1022 GLU   B OE1 1 
ATOM   5958 O OE2 . GLU   B 1 410 ? -10.58500 68.87300  44.84700  1.000 101.84266 ? 1022 GLU   B OE2 1 
ATOM   5959 N N   . GLY   B 1 411 ? -4.87200  64.57400  44.96100  1.000 111.12091 ? 1023 GLY   B N   1 
ATOM   5960 C CA  . GLY   B 1 411 ? -3.68700  64.10200  45.64800  1.000 107.30498 ? 1023 GLY   B CA  1 
ATOM   5961 C C   . GLY   B 1 411 ? -3.88300  62.97900  46.64400  1.000 107.60270 ? 1023 GLY   B C   1 
ATOM   5962 O O   . GLY   B 1 411 ? -2.93200  62.64200  47.35800  1.000 107.89075 ? 1023 GLY   B O   1 
ATOM   5963 N N   . TYR   B 1 412 ? -5.06800  62.38000  46.70700  1.000 110.37475 ? 1024 TYR   B N   1 
ATOM   5964 C CA  . TYR   B 1 412 ? -5.36500  61.37800  47.72200  1.000 109.36687 ? 1024 TYR   B CA  1 
ATOM   5965 C C   . TYR   B 1 412 ? -5.05900  59.97600  47.20900  1.000 107.90863 ? 1024 TYR   B C   1 
ATOM   5966 O O   . TYR   B 1 412 ? -5.08700  59.70900  46.00400  1.000 110.56935 ? 1024 TYR   B O   1 
ATOM   5967 C CB  . TYR   B 1 412 ? -6.82800  61.46700  48.16100  1.000 107.88189 ? 1024 TYR   B CB  1 
ATOM   5968 C CG  . TYR   B 1 412 ? -7.27000  62.86400  48.54500  1.000 110.48886 ? 1024 TYR   B CG  1 
ATOM   5969 C CD1 . TYR   B 1 412 ? -6.34700  63.82200  48.95800  1.000 108.87710 ? 1024 TYR   B CD1 1 
ATOM   5970 C CD2 . TYR   B 1 412 ? -8.60800  63.23000  48.48000  1.000 111.89684 ? 1024 TYR   B CD2 1 
ATOM   5971 C CE1 . TYR   B 1 412 ? -6.74400  65.09800  49.29600  1.000 109.37091 ? 1024 TYR   B CE1 1 
ATOM   5972 C CE2 . TYR   B 1 412 ? -9.01600  64.50600  48.82000  1.000 115.23456 ? 1024 TYR   B CE2 1 
ATOM   5973 C CZ  . TYR   B 1 412 ? -8.07900  65.43500  49.22700  1.000 113.85719 ? 1024 TYR   B CZ  1 
ATOM   5974 O OH  . TYR   B 1 412 ? -8.47800  66.70600  49.56800  1.000 112.11678 ? 1024 TYR   B OH  1 
ATOM   5975 N N   . TYR   B 1 413 ? -4.77100  59.07700  48.14600  1.000 102.57620 ? 1025 TYR   B N   1 
ATOM   5976 C CA  . TYR   B 1 413 ? -4.36500  57.71400  47.81600  1.000 100.97980 ? 1025 TYR   B CA  1 
ATOM   5977 C C   . TYR   B 1 413 ? -5.61700  56.91900  47.47800  1.000 101.54308 ? 1025 TYR   B C   1 
ATOM   5978 O O   . TYR   B 1 413 ? -6.29900  56.38300  48.35200  1.000 102.55735 ? 1025 TYR   B O   1 
ATOM   5979 C CB  . TYR   B 1 413 ? -3.58400  57.08600  48.96300  1.000 101.28843 ? 1025 TYR   B CB  1 
ATOM   5980 C CG  . TYR   B 1 413 ? -2.20200  57.67500  49.14600  1.000 100.32203 ? 1025 TYR   B CG  1 
ATOM   5981 C CD1 . TYR   B 1 413 ? -2.03100  59.01800  49.45800  1.000 102.67204 ? 1025 TYR   B CD1 1 
ATOM   5982 C CD2 . TYR   B 1 413 ? -1.06900  56.89700  48.97600  1.000 96.50279  ? 1025 TYR   B CD2 1 
ATOM   5983 C CE1 . TYR   B 1 413 ? -0.77300  59.56200  49.61300  1.000 99.01192  ? 1025 TYR   B CE1 1 
ATOM   5984 C CE2 . TYR   B 1 413 ? 0.19200   57.43600  49.12500  1.000 99.19658  ? 1025 TYR   B CE2 1 
ATOM   5985 C CZ  . TYR   B 1 413 ? 0.33700   58.76400  49.44600  1.000 100.72097 ? 1025 TYR   B CZ  1 
ATOM   5986 O OH  . TYR   B 1 413 ? 1.59900   59.29300  49.59600  1.000 102.61286 ? 1025 TYR   B OH  1 
ATOM   5987 N N   . THR   B 1 414 ? -5.92600  56.85700  46.18800  1.000 101.22648 ? 1026 THR   B N   1 
ATOM   5988 C CA  . THR   B 1 414 ? -7.09200  56.14500  45.69000  1.000 96.77463  ? 1026 THR   B CA  1 
ATOM   5989 C C   . THR   B 1 414 ? -6.67800  54.82900  45.03700  1.000 94.22337  ? 1026 THR   B C   1 
ATOM   5990 O O   . THR   B 1 414 ? -5.49300  54.53800  44.85000  1.000 93.37719  ? 1026 THR   B O   1 
ATOM   5991 C CB  . THR   B 1 414 ? -7.87300  57.01700  44.70100  1.000 93.87727  ? 1026 THR   B CB  1 
ATOM   5992 O OG1 . THR   B 1 414 ? -6.96700  57.58800  43.74900  1.000 102.53360 ? 1026 THR   B OG1 1 
ATOM   5993 C CG2 . THR   B 1 414 ? -8.60200  58.13700  45.43500  1.000 96.21700  ? 1026 THR   B CG2 1 
ATOM   5994 N N   . ILE   B 1 415 ? -7.68200  54.02600  44.69100  1.000 93.50326  ? 1027 ILE   B N   1 
ATOM   5995 C CA  . ILE   B 1 415 ? -7.45700  52.71200  44.10700  1.000 93.38877  ? 1027 ILE   B CA  1 
ATOM   5996 C C   . ILE   B 1 415 ? -8.73200  52.25700  43.41200  1.000 89.90514  ? 1027 ILE   B C   1 
ATOM   5997 O O   . ILE   B 1 415 ? -9.83700  52.64700  43.79700  1.000 87.39203  ? 1027 ILE   B O   1 
ATOM   5998 C CB  . ILE   B 1 415 ? -7.03500  51.68800  45.16900  1.000 88.09082  ? 1027 ILE   B CB  1 
ATOM   5999 N N   . GLY   B 1 416 ? -8.56400  51.42900  42.38200  1.000 83.10040  ? 1028 GLY   B N   1 
ATOM   6000 C CA  . GLY   B 1 416 ? -9.72100  50.86700  41.70600  1.000 75.78998  ? 1028 GLY   B CA  1 
ATOM   6001 C C   . GLY   B 1 416 ? -10.47500 51.91100  40.90400  1.000 80.55723  ? 1028 GLY   B C   1 
ATOM   6002 O O   . GLY   B 1 416 ? -9.88700  52.75900  40.22200  1.000 79.40007  ? 1028 GLY   B O   1 
ATOM   6003 N N   . ILE   B 1 417 ? -11.80200 51.85000  40.99100  1.000 80.03831  ? 1029 ILE   B N   1 
ATOM   6004 C CA  . ILE   B 1 417 ? -12.67400 52.72300  40.21500  1.000 77.43605  ? 1029 ILE   B CA  1 
ATOM   6005 C C   . ILE   B 1 417 ? -13.03700 53.94500  41.05100  1.000 77.09877  ? 1029 ILE   B C   1 
ATOM   6006 O O   . ILE   B 1 417 ? -14.21600 54.20700  41.31900  1.000 76.04797  ? 1029 ILE   B O   1 
ATOM   6007 C CB  . ILE   B 1 417 ? -13.92400 51.95700  39.74000  1.000 77.64855  ? 1029 ILE   B CB  1 
ATOM   6008 C CG1 . ILE   B 1 417 ? -13.52500 50.56900  39.24000  1.000 68.74844  ? 1029 ILE   B CG1 1 
ATOM   6009 C CG2 . ILE   B 1 417 ? -14.62100 52.69500  38.61100  1.000 74.84930  ? 1029 ILE   B CG2 1 
ATOM   6010 C CD1 . ILE   B 1 417 ? -14.67600 49.76400  38.69300  1.000 63.61563  ? 1029 ILE   B CD1 1 
ATOM   6011 N N   . GLY   B 1 418 ? -12.02000 54.69300  41.47700  1.000 78.23069  ? 1030 GLY   B N   1 
ATOM   6012 C CA  . GLY   B 1 418 ? -12.22100 55.93400  42.20000  1.000 80.68807  ? 1030 GLY   B CA  1 
ATOM   6013 C C   . GLY   B 1 418 ? -12.66600 55.77700  43.64100  1.000 85.71901  ? 1030 GLY   B C   1 
ATOM   6014 O O   . GLY   B 1 418 ? -13.61000 56.44300  44.07800  1.000 83.88411  ? 1030 GLY   B O   1 
ATOM   6015 N N   . HIS   B 1 419 ? -11.99600 54.90600  44.39100  1.000 86.40286  ? 1031 HIS   B N   1 
ATOM   6016 C CA  . HIS   B 1 419 ? -12.27900 54.70400  45.80600  1.000 86.56512  ? 1031 HIS   B CA  1 
ATOM   6017 C C   . HIS   B 1 419 ? -11.20200 55.41900  46.61200  1.000 91.04336  ? 1031 HIS   B C   1 
ATOM   6018 O O   . HIS   B 1 419 ? -10.01400 55.10500  46.48300  1.000 91.05338  ? 1031 HIS   B O   1 
ATOM   6019 C CB  . HIS   B 1 419 ? -12.32400 53.21100  46.14600  1.000 81.71045  ? 1031 HIS   B CB  1 
ATOM   6020 C CG  . HIS   B 1 419 ? -12.55400 52.91300  47.59800  1.000 87.52418  ? 1031 HIS   B CG  1 
ATOM   6021 N ND1 . HIS   B 1 419 ? -13.55800 52.07300  48.03100  1.000 87.18986  ? 1031 HIS   B ND1 1 
ATOM   6022 C CD2 . HIS   B 1 419 ? -11.90400 53.32500  48.71400  1.000 91.84705  ? 1031 HIS   B CD2 1 
ATOM   6023 C CE1 . HIS   B 1 419 ? -13.52400 51.99100  49.34900  1.000 93.48367  ? 1031 HIS   B CE1 1 
ATOM   6024 N NE2 . HIS   B 1 419 ? -12.53000 52.74200  49.78800  1.000 92.71870  ? 1031 HIS   B NE2 1 
ATOM   6025 N N   . LEU   B 1 420 ? -11.61700 56.37700  47.43900  1.000 93.75919  ? 1032 LEU   B N   1 
ATOM   6026 C CA  . LEU   B 1 420 ? -10.69000 57.11800  48.29200  1.000 94.67673  ? 1032 LEU   B CA  1 
ATOM   6027 C C   . LEU   B 1 420 ? -10.32100 56.23800  49.47900  1.000 94.81316  ? 1032 LEU   B C   1 
ATOM   6028 O O   . LEU   B 1 420 ? -11.11900 56.04800  50.40000  1.000 95.52166  ? 1032 LEU   B O   1 
ATOM   6029 C CB  . LEU   B 1 420 ? -11.31100 58.43300  48.74900  1.000 90.81794  ? 1032 LEU   B CB  1 
ATOM   6030 N N   . LEU   B 1 421 ? -9.10400  55.68800  49.45600  1.000 90.15364  ? 1033 LEU   B N   1 
ATOM   6031 C CA  . LEU   B 1 421 ? -8.66500  54.82700  50.55000  1.000 91.88467  ? 1033 LEU   B CA  1 
ATOM   6032 C C   . LEU   B 1 421 ? -8.40900  55.62300  51.82100  1.000 99.65483  ? 1033 LEU   B C   1 
ATOM   6033 O O   . LEU   B 1 421 ? -8.51100  55.07600  52.92700  1.000 100.24103 ? 1033 LEU   B O   1 
ATOM   6034 C CB  . LEU   B 1 421 ? -7.40900  54.06000  50.15000  1.000 86.08218  ? 1033 LEU   B CB  1 
ATOM   6035 C CG  . LEU   B 1 421 ? -7.59500  52.90800  49.16500  1.000 87.67406  ? 1033 LEU   B CG  1 
ATOM   6036 C CD1 . LEU   B 1 421 ? -6.25600  52.29100  48.81500  1.000 92.18608  ? 1033 LEU   B CD1 1 
ATOM   6037 C CD2 . LEU   B 1 421 ? -8.51200  51.86300  49.77100  1.000 85.35261  ? 1033 LEU   B CD2 1 
ATOM   6038 N N   . THR   B 1 422 ? -8.08400  56.90600  51.68500  1.000 102.32921 ? 1034 THR   B N   1 
ATOM   6039 C CA  . THR   B 1 422 ? -7.73900  57.76100  52.81400  1.000 100.38089 ? 1034 THR   B CA  1 
ATOM   6040 C C   . THR   B 1 422 ? -7.56000  59.18000  52.29100  1.000 105.61680 ? 1034 THR   B C   1 
ATOM   6041 O O   . THR   B 1 422 ? -7.52700  59.42200  51.08000  1.000 104.75247 ? 1034 THR   B O   1 
ATOM   6042 C CB  . THR   B 1 422 ? -6.46300  57.29100  53.51900  1.000 96.80249  ? 1034 THR   B CB  1 
ATOM   6043 O OG1 . THR   B 1 422 ? -6.21500  58.11100  54.66800  1.000 100.06306 ? 1034 THR   B OG1 1 
ATOM   6044 C CG2 . THR   B 1 422 ? -5.27300  57.38000  52.57300  1.000 94.42826  ? 1034 THR   B CG2 1 
ATOM   6045 N N   . LYS   B 1 423 ? -7.45600  60.11900  53.23200  1.000 109.78014 ? 1035 LYS   B N   1 
ATOM   6046 C CA  . LYS   B 1 423 ? -7.02500  61.47700  52.94500  1.000 109.79098 ? 1035 LYS   B CA  1 
ATOM   6047 C C   . LYS   B 1 423 ? -5.62100  61.76500  53.45800  1.000 109.48751 ? 1035 LYS   B C   1 
ATOM   6048 O O   . LYS   B 1 423 ? -5.02200  62.76600  53.04700  1.000 108.41684 ? 1035 LYS   B O   1 
ATOM   6049 C CB  . LYS   B 1 423 ? -8.00300  62.49600  53.55200  1.000 106.22511 ? 1035 LYS   B CB  1 
ATOM   6050 C CG  . LYS   B 1 423 ? -9.41500  61.97800  53.77600  1.000 105.48313 ? 1035 LYS   B CG  1 
ATOM   6051 C CD  . LYS   B 1 423 ? -10.13100 61.69700  52.46100  1.000 113.71184 ? 1035 LYS   B CD  1 
ATOM   6052 C CE  . LYS   B 1 423 ? -11.61300 61.45200  52.69200  1.000 115.03153 ? 1035 LYS   B CE  1 
ATOM   6053 N NZ  . LYS   B 1 423 ? -11.84300 60.50300  53.81700  1.000 115.98935 ? 1035 LYS   B NZ  1 
ATOM   6054 N N   . SER   B 1 424 ? -5.08600  60.91700  54.33600  1.000 107.58750 ? 1036 SER   B N   1 
ATOM   6055 C CA  . SER   B 1 424 ? -3.76400  61.13500  54.90100  1.000 105.40641 ? 1036 SER   B CA  1 
ATOM   6056 C C   . SER   B 1 424 ? -2.68500  60.96200  53.83300  1.000 110.53614 ? 1036 SER   B C   1 
ATOM   6057 O O   . SER   B 1 424 ? -2.84600  60.17600  52.89500  1.000 111.90606 ? 1036 SER   B O   1 
ATOM   6058 C CB  . SER   B 1 424 ? -3.51100  60.16500  56.05400  1.000 103.70270 ? 1036 SER   B CB  1 
ATOM   6059 O OG  . SER   B 1 424 ? -2.12900  59.88800  56.20400  1.000 98.50624  ? 1036 SER   B OG  1 
ATOM   6060 N N   . PRO   B 1 425 ? -1.57200  61.69200  53.95200  1.000 110.93639 ? 1037 PRO   B N   1 
ATOM   6061 C CA  . PRO   B 1 425 ? -0.49700  61.55400  52.95800  1.000 106.90596 ? 1037 PRO   B CA  1 
ATOM   6062 C C   . PRO   B 1 425 ? 0.31100   60.27800  53.10900  1.000 107.29157 ? 1037 PRO   B C   1 
ATOM   6063 O O   . PRO   B 1 425 ? 0.96500   59.86300  52.14400  1.000 111.92556 ? 1037 PRO   B O   1 
ATOM   6064 C CB  . PRO   B 1 425 ? 0.37100   62.79300  53.20800  1.000 105.23942 ? 1037 PRO   B CB  1 
ATOM   6065 C CG  . PRO   B 1 425 ? 0.15000   63.10500  54.65200  1.000 112.21125 ? 1037 PRO   B CG  1 
ATOM   6066 C CD  . PRO   B 1 425 ? -1.29000  62.75900  54.92900  1.000 111.19392 ? 1037 PRO   B CD  1 
ATOM   6067 N N   . SER   B 1 426 ? 0.29700   59.64900  54.28200  1.000 108.06856 ? 1038 SER   B N   1 
ATOM   6068 C CA  . SER   B 1 426 ? 1.07300   58.43400  54.49700  1.000 109.42561 ? 1038 SER   B CA  1 
ATOM   6069 C C   . SER   B 1 426 ? 0.45400   57.28000  53.71900  1.000 106.51416 ? 1038 SER   B C   1 
ATOM   6070 O O   . SER   B 1 426 ? -0.73200  56.97400  53.88700  1.000 103.05834 ? 1038 SER   B O   1 
ATOM   6071 C CB  . SER   B 1 426 ? 1.13600   58.10700  55.98900  1.000 106.76555 ? 1038 SER   B CB  1 
ATOM   6072 O OG  . SER   B 1 426 ? 1.99400   57.00700  56.24100  1.000 106.09253 ? 1038 SER   B OG  1 
ATOM   6073 N N   . LEU   B 1 427 ? 1.25400   56.64300  52.86200  1.000 103.31003 ? 1039 LEU   B N   1 
ATOM   6074 C CA  . LEU   B 1 427 ? 0.76900   55.46200  52.15800  1.000 102.87318 ? 1039 LEU   B CA  1 
ATOM   6075 C C   . LEU   B 1 427 ? 0.54700   54.32000  53.14300  1.000 106.18821 ? 1039 LEU   B C   1 
ATOM   6076 O O   . LEU   B 1 427 ? -0.28800  53.44100  52.90200  1.000 104.13803 ? 1039 LEU   B O   1 
ATOM   6077 C CB  . LEU   B 1 427 ? 1.76000   55.07300  51.05400  1.000 97.54455  ? 1039 LEU   B CB  1 
ATOM   6078 C CG  . LEU   B 1 427 ? 1.31900   54.32600  49.77900  1.000 98.37104  ? 1039 LEU   B CG  1 
ATOM   6079 C CD1 . LEU   B 1 427 ? 2.51200   54.05700  48.85700  1.000 95.09827  ? 1039 LEU   B CD1 1 
ATOM   6080 C CD2 . LEU   B 1 427 ? 0.51800   53.05700  50.00500  1.000 94.22198  ? 1039 LEU   B CD2 1 
ATOM   6081 N N   . ASN   B 1 428 ? 1.27700   54.33400  54.26600  1.000 107.75187 ? 1040 ASN   B N   1 
ATOM   6082 C CA  . ASN   B 1 428 ? 0.99000   53.42100  55.36600  1.000 101.91698 ? 1040 ASN   B CA  1 
ATOM   6083 C C   . ASN   B 1 428 ? -0.47500  53.49900  55.77000  1.000 102.25237 ? 1040 ASN   B C   1 
ATOM   6084 O O   . ASN   B 1 428 ? -1.09600  52.47900  56.09000  1.000 101.89174 ? 1040 ASN   B O   1 
ATOM   6085 C CB  . ASN   B 1 428 ? 1.88200   53.74400  56.57000  1.000 101.44678 ? 1040 ASN   B CB  1 
ATOM   6086 C CG  . ASN   B 1 428 ? 3.35600   53.50900  56.29300  1.000 107.81764 ? 1040 ASN   B CG  1 
ATOM   6087 O OD1 . ASN   B 1 428 ? 3.72800   52.58300  55.57200  1.000 112.22544 ? 1040 ASN   B OD1 1 
ATOM   6088 N ND2 . ASN   B 1 428 ? 4.20700   54.35200  56.87200  1.000 106.28363 ? 1040 ASN   B ND2 1 
ATOM   6089 N N   . ALA   B 1 429 ? -1.04400  54.70800  55.75700  1.000 103.09416 ? 1041 ALA   B N   1 
ATOM   6090 C CA  . ALA   B 1 429 ? -2.45800  54.89400  56.06000  1.000 103.17463 ? 1041 ALA   B CA  1 
ATOM   6091 C C   . ALA   B 1 429 ? -3.36500  54.50800  54.89700  1.000 104.52548 ? 1041 ALA   B C   1 
ATOM   6092 O O   . ALA   B 1 429 ? -4.54200  54.20000  55.12400  1.000 100.20107 ? 1041 ALA   B O   1 
ATOM   6093 C CB  . ALA   B 1 429 ? -2.72200  56.34600  56.46400  1.000 101.71602 ? 1041 ALA   B CB  1 
ATOM   6094 N N   . ALA   B 1 430 ? -2.85200  54.52100  53.66500  1.000 100.72312 ? 1042 ALA   B N   1 
ATOM   6095 C CA  . ALA   B 1 430 ? -3.63400  54.04200  52.53000  1.000 99.13469  ? 1042 ALA   B CA  1 
ATOM   6096 C C   . ALA   B 1 430 ? -3.82200  52.53200  52.60200  1.000 98.22838  ? 1042 ALA   B C   1 
ATOM   6097 O O   . ALA   B 1 430 ? -4.95400  52.03400  52.65200  1.000 96.67771  ? 1042 ALA   B O   1 
ATOM   6098 C CB  . ALA   B 1 430 ? -2.96000  54.44300  51.21800  1.000 98.11183  ? 1042 ALA   B CB  1 
ATOM   6099 N N   . LYS   B 1 431 ? -2.71200  51.78500  52.61000  1.000 97.74253  ? 1043 LYS   B N   1 
ATOM   6100 C CA  . LYS   B 1 431 ? -2.79000  50.34100  52.80000  1.000 97.49293  ? 1043 LYS   B CA  1 
ATOM   6101 C C   . LYS   B 1 431 ? -3.52500  49.97700  54.08300  1.000 97.07861  ? 1043 LYS   B C   1 
ATOM   6102 O O   . LYS   B 1 431 ? -4.26500  48.99000  54.10000  1.000 95.57135  ? 1043 LYS   B O   1 
ATOM   6103 C CB  . LYS   B 1 431 ? -1.38700  49.72500  52.79400  1.000 96.08733  ? 1043 LYS   B CB  1 
ATOM   6104 C CG  . LYS   B 1 431 ? -0.51900  50.17400  51.62400  1.000 97.51143  ? 1043 LYS   B CG  1 
ATOM   6105 C CD  . LYS   B 1 431 ? 0.70300   49.28600  51.43200  1.000 88.43088  ? 1043 LYS   B CD  1 
ATOM   6106 C CE  . LYS   B 1 431 ? 1.49400   49.71900  50.20200  1.000 95.33729  ? 1043 LYS   B CE  1 
ATOM   6107 N NZ  . LYS   B 1 431 ? 2.76800   48.97300  50.01300  1.000 102.96431 ? 1043 LYS   B NZ  1 
ATOM   6108 N N   . SER   B 1 432 ? -3.37700  50.78600  55.13900  1.000 101.69536 ? 1044 SER   B N   1 
ATOM   6109 C CA  . SER   B 1 432 ? -3.97000  50.46800  56.43800  1.000 98.59919  ? 1044 SER   B CA  1 
ATOM   6110 C C   . SER   B 1 432 ? -5.42500  50.03400  56.31500  1.000 96.08515  ? 1044 SER   B C   1 
ATOM   6111 O O   . SER   B 1 432 ? -5.87200  49.12500  57.02400  1.000 93.50800  ? 1044 SER   B O   1 
ATOM   6112 C CB  . SER   B 1 432 ? -3.86900  51.67300  57.37300  1.000 96.00287  ? 1044 SER   B CB  1 
ATOM   6113 O OG  . SER   B 1 432 ? -4.67300  52.74400  56.90600  1.000 100.74092 ? 1044 SER   B OG  1 
ATOM   6114 N N   . GLU   B 1 433 ? -6.18000  50.67400  55.42300  1.000 95.80171  ? 1045 GLU   B N   1 
ATOM   6115 C CA  . GLU   B 1 433 ? -7.56400  50.29800  55.19400  1.000 97.01331  ? 1045 GLU   B CA  1 
ATOM   6116 C C   . GLU   B 1 433 ? -7.81800  49.71900  53.81100  1.000 98.29519  ? 1045 GLU   B C   1 
ATOM   6117 O O   . GLU   B 1 433 ? -8.92900  49.23600  53.56100  1.000 98.86973  ? 1045 GLU   B O   1 
ATOM   6118 C CB  . GLU   B 1 433 ? -8.49400  51.49600  55.42300  1.000 95.47246  ? 1045 GLU   B CB  1 
ATOM   6119 C CG  . GLU   B 1 433 ? -8.17200  52.27700  56.67800  1.000 100.39988 ? 1045 GLU   B CG  1 
ATOM   6120 C CD  . GLU   B 1 433 ? -9.17900  53.37000  56.94700  1.000 110.34806 ? 1045 GLU   B CD  1 
ATOM   6121 O OE1 . GLU   B 1 433 ? -10.28400 53.31200  56.36500  1.000 109.75780 ? 1045 GLU   B OE1 1 
ATOM   6122 O OE2 . GLU   B 1 433 ? -8.87100  54.28000  57.74600  1.000 110.84954 ? 1045 GLU   B OE2 1 
ATOM   6123 N N   . LEU   B 1 434 ? -6.83600  49.75400  52.90900  1.000 93.14723  ? 1046 LEU   B N   1 
ATOM   6124 C CA  . LEU   B 1 434 ? -6.97900  49.02900  51.65200  1.000 94.31742  ? 1046 LEU   B CA  1 
ATOM   6125 C C   . LEU   B 1 434 ? -7.16000  47.54000  51.91300  1.000 94.28993  ? 1046 LEU   B C   1 
ATOM   6126 O O   . LEU   B 1 434 ? -8.04000  46.89500  51.33000  1.000 98.49784  ? 1046 LEU   B O   1 
ATOM   6127 C CB  . LEU   B 1 434 ? -5.76900  49.27900  50.75000  1.000 97.89263  ? 1046 LEU   B CB  1 
ATOM   6128 C CG  . LEU   B 1 434 ? -5.65800  48.37800  49.51400  1.000 90.49112  ? 1046 LEU   B CG  1 
ATOM   6129 C CD1 . LEU   B 1 434 ? -6.80800  48.61300  48.54300  1.000 85.03038  ? 1046 LEU   B CD1 1 
ATOM   6130 C CD2 . LEU   B 1 434 ? -4.32000  48.57400  48.82400  1.000 88.59440  ? 1046 LEU   B CD2 1 
ATOM   6131 N N   . ASP   B 1 435 ? -6.34000  46.97600  52.80400  1.000 92.02710  ? 1047 ASP   B N   1 
ATOM   6132 C CA  . ASP   B 1 435 ? -6.51200  45.58500  53.19300  1.000 90.24880  ? 1047 ASP   B CA  1 
ATOM   6133 C C   . ASP   B 1 435 ? -7.61100  45.39200  54.22800  1.000 90.15658  ? 1047 ASP   B C   1 
ATOM   6134 O O   . ASP   B 1 435 ? -8.05500  44.25700  54.43500  1.000 92.90239  ? 1047 ASP   B O   1 
ATOM   6135 C CB  . ASP   B 1 435 ? -5.20500  45.00000  53.73300  1.000 91.72229  ? 1047 ASP   B CB  1 
ATOM   6136 C CG  . ASP   B 1 435 ? -4.55000  45.87500  54.77400  1.000 101.53622 ? 1047 ASP   B CG  1 
ATOM   6137 O OD1 . ASP   B 1 435 ? -4.95700  45.81400  55.95400  1.000 109.27460 ? 1047 ASP   B OD1 1 
ATOM   6138 O OD2 . ASP   B 1 435 ? -3.55800  46.55000  54.43000  1.000 100.20468 ? 1047 ASP   B OD2 1 
ATOM   6139 N N   . LYS   B 1 436 ? -8.05600  46.46300  54.88700  1.000 88.05725  ? 1048 LYS   B N   1 
ATOM   6140 C CA  . LYS   B 1 436 ? -9.17400  46.34400  55.81500  1.000 87.03937  ? 1048 LYS   B CA  1 
ATOM   6141 C C   . LYS   B 1 436 ? -10.48600 46.06200  55.09600  1.000 89.49506  ? 1048 LYS   B C   1 
ATOM   6142 O O   . LYS   B 1 436 ? -11.42000 45.54300  55.71700  1.000 86.77495  ? 1048 LYS   B O   1 
ATOM   6143 C CB  . LYS   B 1 436 ? -9.29700  47.61900  56.65100  1.000 89.42669  ? 1048 LYS   B CB  1 
ATOM   6144 C CG  . LYS   B 1 436 ? -9.65300  47.38600  58.11200  1.000 95.86450  ? 1048 LYS   B CG  1 
ATOM   6145 C CD  . LYS   B 1 436 ? -10.03000 48.69100  58.80600  1.000 90.22696  ? 1048 LYS   B CD  1 
ATOM   6146 C CE  . LYS   B 1 436 ? -11.29400 49.29600  58.20700  1.000 88.61716  ? 1048 LYS   B CE  1 
ATOM   6147 N NZ  . LYS   B 1 436 ? -11.64500 50.59800  58.83900  1.000 81.14412  ? 1048 LYS   B NZ  1 
ATOM   6148 N N   . ALA   B 1 437 ? -10.57400 46.38100  53.80400  1.000 94.62250  ? 1049 ALA   B N   1 
ATOM   6149 C CA  . ALA   B 1 437 ? -11.78800 46.20100  53.01600  1.000 90.95416  ? 1049 ALA   B CA  1 
ATOM   6150 C C   . ALA   B 1 437 ? -11.76600 44.94700  52.15100  1.000 91.05347  ? 1049 ALA   B C   1 
ATOM   6151 O O   . ALA   B 1 437 ? -12.79900 44.28600  52.00500  1.000 91.11654  ? 1049 ALA   B O   1 
ATOM   6152 C CB  . ALA   B 1 437 ? -12.02200 47.42500  52.12500  1.000 80.29073  ? 1049 ALA   B CB  1 
ATOM   6153 N N   . ILE   B 1 438 ? -10.61300 44.60900  51.56900  1.000 87.82771  ? 1050 ILE   B N   1 
ATOM   6154 C CA  . ILE   B 1 438 ? -10.51400 43.41200  50.73600  1.000 90.42388  ? 1050 ILE   B CA  1 
ATOM   6155 C C   . ILE   B 1 438 ? -10.76600 42.16100  51.56900  1.000 93.02637  ? 1050 ILE   B C   1 
ATOM   6156 O O   . ILE   B 1 438 ? -11.60400 41.31900  51.22300  1.000 98.21146  ? 1050 ILE   B O   1 
ATOM   6157 C CB  . ILE   B 1 438 ? -9.13800  43.34800  50.05000  1.000 87.34621  ? 1050 ILE   B CB  1 
ATOM   6158 C CG1 . ILE   B 1 438 ? -8.89600  44.60600  49.22300  1.000 88.41685  ? 1050 ILE   B CG1 1 
ATOM   6159 C CG2 . ILE   B 1 438 ? -9.03900  42.10600  49.17300  1.000 82.27877  ? 1050 ILE   B CG2 1 
ATOM   6160 C CD1 . ILE   B 1 438 ? -9.84500  44.76100  48.07900  1.000 90.93906  ? 1050 ILE   B CD1 1 
ATOM   6161 N N   . GLY   B 1 439 ? -10.03500 42.01900  52.67500  1.000 84.23376  ? 1051 GLY   B N   1 
ATOM   6162 C CA  . GLY   B 1 439 ? -10.09600 40.82900  53.50200  1.000 86.04879  ? 1051 GLY   B CA  1 
ATOM   6163 C C   . GLY   B 1 439 ? -8.72400  40.27800  53.84100  1.000 94.80272  ? 1051 GLY   B C   1 
ATOM   6164 O O   . GLY   B 1 439 ? -8.48200  39.84200  54.97100  1.000 107.13074 ? 1051 GLY   B O   1 
ATOM   6165 N N   . ARG   B 1 440 ? -7.82100  40.28600  52.86500  1.000 89.60106  ? 1052 ARG   B N   1 
ATOM   6166 C CA  . ARG   B 1 440 ? -6.43900  39.87400  53.04600  1.000 86.15829  ? 1052 ARG   B CA  1 
ATOM   6167 C C   . ARG   B 1 440 ? -5.59300  41.11100  53.34700  1.000 86.44573  ? 1052 ARG   B C   1 
ATOM   6168 O O   . ARG   B 1 440 ? -6.12500  42.17100  53.68700  1.000 80.71242  ? 1052 ARG   B O   1 
ATOM   6169 C CB  . ARG   B 1 440 ? -5.95700  39.14700  51.78300  1.000 84.59733  ? 1052 ARG   B CB  1 
ATOM   6170 C CG  . ARG   B 1 440 ? -6.03100  40.01600  50.54400  1.000 85.24533  ? 1052 ARG   B CG  1 
ATOM   6171 C CD  . ARG   B 1 440 ? -5.66400  39.25600  49.28900  1.000 83.43138  ? 1052 ARG   B CD  1 
ATOM   6172 N NE  . ARG   B 1 440 ? -6.40800  39.74900  48.13800  1.000 88.41104  ? 1052 ARG   B NE  1 
ATOM   6173 C CZ  . ARG   B 1 440 ? -5.90600  40.55800  47.21500  1.000 94.33125  ? 1052 ARG   B CZ  1 
ATOM   6174 N NH1 . ARG   B 1 440 ? -4.64100  40.94600  47.25200  1.000 88.85208  ? 1052 ARG   B NH1 1 
ATOM   6175 N NH2 . ARG   B 1 440 ? -6.69100  40.98300  46.22700  1.000 94.89723  ? 1052 ARG   B NH2 1 
ATOM   6176 N N   . ASN   B 1 441 ? -4.27300  40.98200  53.22700  1.000 91.81055  ? 1053 ASN   B N   1 
ATOM   6177 C CA  . ASN   B 1 441 ? -3.35800  42.11900  53.22800  1.000 91.77659  ? 1053 ASN   B CA  1 
ATOM   6178 C C   . ASN   B 1 441 ? -2.84700  42.26800  51.80000  1.000 90.94924  ? 1053 ASN   B C   1 
ATOM   6179 O O   . ASN   B 1 441 ? -1.95000  41.53800  51.37000  1.000 91.37738  ? 1053 ASN   B O   1 
ATOM   6180 C CB  . ASN   B 1 441 ? -2.21900  41.92800  54.22600  1.000 92.16140  ? 1053 ASN   B CB  1 
ATOM   6181 C CG  . ASN   B 1 441 ? -1.67600  43.24900  54.75000  1.000 97.75359  ? 1053 ASN   B CG  1 
ATOM   6182 O OD1 . ASN   B 1 441 ? -1.63400  44.24600  54.02700  1.000 98.44199  ? 1053 ASN   B OD1 1 
ATOM   6183 N ND2 . ASN   B 1 441 ? -1.27400  43.26500  56.01700  1.000 97.44926  ? 1053 ASN   B ND2 1 
ATOM   6184 N N   . THR   B 1 442 ? -3.42700  43.21800  51.06500  1.000 92.30644  ? 1054 THR   B N   1 
ATOM   6185 C CA  . THR   B 1 442 ? -3.14200  43.34300  49.64200  1.000 91.18667  ? 1054 THR   B CA  1 
ATOM   6186 C C   . THR   B 1 442 ? -1.84100  44.08500  49.37800  1.000 88.75799  ? 1054 THR   B C   1 
ATOM   6187 O O   . THR   B 1 442 ? -1.20900  43.86400  48.33800  1.000 95.11228  ? 1054 THR   B O   1 
ATOM   6188 C CB  . THR   B 1 442 ? -4.29900  44.05400  48.94400  1.000 91.29277  ? 1054 THR   B CB  1 
ATOM   6189 O OG1 . THR   B 1 442 ? -4.41400  45.38600  49.45600  1.000 91.55047  ? 1054 THR   B OG1 1 
ATOM   6190 C CG2 . THR   B 1 442 ? -5.58900  43.32100  49.22400  1.000 89.66189  ? 1054 THR   B CG2 1 
ATOM   6191 N N   . ASN   B 1 443 ? -1.44200  44.97000  50.28700  1.000 86.45324  ? 1055 ASN   B N   1 
ATOM   6192 C CA  . ASN   B 1 443 ? -0.15800  45.65900  50.21200  1.000 89.12277  ? 1055 ASN   B CA  1 
ATOM   6193 C C   . ASN   B 1 443 ? -0.03400  46.49600  48.94000  1.000 85.58807  ? 1055 ASN   B C   1 
ATOM   6194 O O   . ASN   B 1 443 ? 1.04600   46.60600  48.35700  1.000 76.56997  ? 1055 ASN   B O   1 
ATOM   6195 C CB  . ASN   B 1 443 ? 0.99000   44.64800  50.29600  1.000 92.52543  ? 1055 ASN   B CB  1 
ATOM   6196 C CG  . ASN   B 1 443 ? 0.95600   43.83400  51.57800  1.000 94.30565  ? 1055 ASN   B CG  1 
ATOM   6197 O OD1 . ASN   B 1 443 ? 0.64400   42.64200  51.56200  1.000 89.38731  ? 1055 ASN   B OD1 1 
ATOM   6198 N ND2 . ASN   B 1 443 ? 1.27700   44.47500  52.69600  1.000 95.05301  ? 1055 ASN   B ND2 1 
ATOM   6199 N N   . ILE   B 1 446 ? -4.58800  44.95300  44.49200  1.000 82.44028  ? 1058 ILE   B N   1 
ATOM   6200 C CA  . ILE   B 1 446 ? -5.82700  44.18500  44.54900  1.000 77.42418  ? 1058 ILE   B CA  1 
ATOM   6201 C C   . ILE   B 1 446 ? -6.17600  43.67000  43.15500  1.000 86.56407  ? 1058 ILE   B C   1 
ATOM   6202 O O   . ILE   B 1 446 ? -5.77400  44.25900  42.14800  1.000 84.65491  ? 1058 ILE   B O   1 
ATOM   6203 C CB  . ILE   B 1 446 ? -6.97200  45.02500  45.12700  1.000 74.93550  ? 1058 ILE   B CB  1 
ATOM   6204 C CG1 . ILE   B 1 446 ? -7.15500  46.31200  44.32200  1.000 75.99539  ? 1058 ILE   B CG1 1 
ATOM   6205 C CG2 . ILE   B 1 446 ? -6.67000  45.39900  46.55700  1.000 82.59695  ? 1058 ILE   B CG2 1 
ATOM   6206 C CD1 . ILE   B 1 446 ? -8.37300  47.11300  44.73400  1.000 72.23805  ? 1058 ILE   B CD1 1 
ATOM   6207 N N   . THR   B 1 447 ? -6.92500  42.57200  43.09400  1.000 81.26082  ? 1059 THR   B N   1 
ATOM   6208 C CA  . THR   B 1 447 ? -7.26800  41.98700  41.80700  1.000 78.36911  ? 1059 THR   B CA  1 
ATOM   6209 C C   . THR   B 1 447 ? -8.33600  42.82100  41.10300  1.000 77.86398  ? 1059 THR   B C   1 
ATOM   6210 O O   . THR   B 1 447 ? -9.03100  43.63900  41.71400  1.000 76.30058  ? 1059 THR   B O   1 
ATOM   6211 C CB  . THR   B 1 447 ? -7.76300  40.55100  41.98100  1.000 81.58806  ? 1059 THR   B CB  1 
ATOM   6212 O OG1 . THR   B 1 447 ? -9.04800  40.55800  42.61600  1.000 85.49501  ? 1059 THR   B OG1 1 
ATOM   6213 C CG2 . THR   B 1 447 ? -6.79100  39.75700  42.83800  1.000 92.34116  ? 1059 THR   B CG2 1 
ATOM   6214 N N   . LYS   B 1 448 ? -8.45900  42.60200  39.79000  1.000 80.79414  ? 1060 LYS   B N   1 
ATOM   6215 C CA  . LYS   B 1 448 ? -9.50800  43.26700  39.02200  1.000 78.52109  ? 1060 LYS   B CA  1 
ATOM   6216 C C   . LYS   B 1 448 ? -10.89000 42.86600  39.51600  1.000 76.17414  ? 1060 LYS   B C   1 
ATOM   6217 O O   . LYS   B 1 448 ? -11.82900 43.66800  39.45700  1.000 75.75153  ? 1060 LYS   B O   1 
ATOM   6218 C CB  . LYS   B 1 448 ? -9.33700  42.95400  37.53100  1.000 73.75069  ? 1060 LYS   B CB  1 
ATOM   6219 C CG  . LYS   B 1 448 ? -10.28700 43.68200  36.57500  1.000 68.78151  ? 1060 LYS   B CG  1 
ATOM   6220 C CD  . LYS   B 1 448 ? -11.57000 42.90500  36.36400  1.000 65.50519  ? 1060 LYS   B CD  1 
ATOM   6221 C CE  . LYS   B 1 448 ? -11.25700 41.54000  35.79800  1.000 61.02459  ? 1060 LYS   B CE  1 
ATOM   6222 N NZ  . LYS   B 1 448 ? -12.46400 40.69500  35.73400  1.000 59.79666  ? 1060 LYS   B NZ  1 
ATOM   6223 N N   . ASP   B 1 449 ? -11.03200 41.63800  40.01300  1.000 67.69776  ? 1061 ASP   B N   1 
ATOM   6224 C CA  . ASP   B 1 449 ? -12.29500 41.22600  40.60700  1.000 70.66842  ? 1061 ASP   B CA  1 
ATOM   6225 C C   . ASP   B 1 449 ? -12.49500 41.85500  41.98200  1.000 74.37652  ? 1061 ASP   B C   1 
ATOM   6226 O O   . ASP   B 1 449 ? -13.63600 42.10700  42.38400  1.000 71.40969  ? 1061 ASP   B O   1 
ATOM   6227 C CB  . ASP   B 1 449 ? -12.34400 39.70400  40.68600  1.000 71.64602  ? 1061 ASP   B CB  1 
ATOM   6228 C CG  . ASP   B 1 449 ? -12.43400 39.06000  39.31600  1.000 70.59425  ? 1061 ASP   B CG  1 
ATOM   6229 O OD1 . ASP   B 1 449 ? -13.03900 39.66500  38.40500  1.000 74.70930  ? 1061 ASP   B OD1 1 
ATOM   6230 O OD2 . ASP   B 1 449 ? -11.86700 37.96700  39.13700  1.000 57.79615  ? 1061 ASP   B OD2 1 
ATOM   6231 N N   . GLU   B 1 450 ? -11.40400 42.11700  42.71100  1.000 76.87568  ? 1062 GLU   B N   1 
ATOM   6232 C CA  . GLU   B 1 450 ? -11.51600 42.84700  43.97200  1.000 80.80762  ? 1062 GLU   B CA  1 
ATOM   6233 C C   . GLU   B 1 450 ? -11.89200 44.30400  43.73500  1.000 78.36088  ? 1062 GLU   B C   1 
ATOM   6234 O O   . GLU   B 1 450 ? -12.72800 44.86000  44.45900  1.000 80.10174  ? 1062 GLU   B O   1 
ATOM   6235 C CB  . GLU   B 1 450 ? -10.21400 42.74800  44.77000  1.000 80.06661  ? 1062 GLU   B CB  1 
ATOM   6236 C CG  . GLU   B 1 450 ? -10.01500 41.42000  45.49300  1.000 83.45053  ? 1062 GLU   B CG  1 
ATOM   6237 C CD  . GLU   B 1 450 ? -11.16800 41.08200  46.43200  1.000 88.25375  ? 1062 GLU   B CD  1 
ATOM   6238 O OE1 . GLU   B 1 450 ? -11.82600 42.01400  46.94500  1.000 79.19540  ? 1062 GLU   B OE1 1 
ATOM   6239 O OE2 . GLU   B 1 450 ? -11.41900 39.87700  46.65700  1.000 89.06550  ? 1062 GLU   B OE2 1 
ATOM   6240 N N   . ALA   B 1 451 ? -11.29100 44.93800  42.72500  1.000 69.06335  ? 1063 ALA   B N   1 
ATOM   6241 C CA  . ALA   B 1 451 ? -11.68700 46.29400  42.36400  1.000 74.27691  ? 1063 ALA   B CA  1 
ATOM   6242 C C   . ALA   B 1 451 ? -13.14800 46.37600  41.93500  1.000 80.16147  ? 1063 ALA   B C   1 
ATOM   6243 O O   . ALA   B 1 451 ? -13.74800 47.45400  42.02000  1.000 77.95183  ? 1063 ALA   B O   1 
ATOM   6244 C CB  . ALA   B 1 451 ? -10.78400 46.82300  41.24600  1.000 66.01490  ? 1063 ALA   B CB  1 
ATOM   6245 N N   . GLU   B 1 452 ? -13.73300 45.26100  41.49100  1.000 81.47430  ? 1064 GLU   B N   1 
ATOM   6246 C CA  . GLU   B 1 452 ? -15.11600 45.26300  41.02600  1.000 81.03804  ? 1064 GLU   B CA  1 
ATOM   6247 C C   . GLU   B 1 452 ? -16.10400 45.29600  42.18600  1.000 79.75913  ? 1064 GLU   B C   1 
ATOM   6248 O O   . GLU   B 1 452 ? -17.02700 46.11800  42.19800  1.000 74.96891  ? 1064 GLU   B O   1 
ATOM   6249 C CB  . GLU   B 1 452 ? -15.37200 44.04300  40.13900  1.000 78.83161  ? 1064 GLU   B CB  1 
ATOM   6250 C CG  . GLU   B 1 452 ? -14.82000 44.18100  38.73100  1.000 77.12210  ? 1064 GLU   B CG  1 
ATOM   6251 C CD  . GLU   B 1 452 ? -15.23700 43.04300  37.82300  1.000 74.39113  ? 1064 GLU   B CD  1 
ATOM   6252 O OE1 . GLU   B 1 452 ? -15.74000 42.01800  38.33300  1.000 74.97765  ? 1064 GLU   B OE1 1 
ATOM   6253 O OE2 . GLU   B 1 452 ? -15.05400 43.17100  36.59600  1.000 77.25937  ? 1064 GLU   B OE2 1 
ATOM   6254 N N   . LYS   B 1 453 ? -15.94100 44.40300  43.16400  1.000 81.71431  ? 1065 LYS   B N   1 
ATOM   6255 C CA  . LYS   B 1 453 ? -16.90600 44.34900  44.25400  1.000 81.24464  ? 1065 LYS   B CA  1 
ATOM   6256 C C   . LYS   B 1 453 ? -16.73200 45.47900  45.26400  1.000 82.65193  ? 1065 LYS   B C   1 
ATOM   6257 O O   . LYS   B 1 453 ? -17.67300 45.76400  46.00900  1.000 78.66909  ? 1065 LYS   B O   1 
ATOM   6258 C CB  . LYS   B 1 453 ? -16.85700 42.98600  44.95300  1.000 75.95294  ? 1065 LYS   B CB  1 
ATOM   6259 C CG  . LYS   B 1 453 ? -15.53300 42.58800  45.57600  1.000 76.53036  ? 1065 LYS   B CG  1 
ATOM   6260 C CD  . LYS   B 1 453 ? -15.73700 41.35500  46.44800  1.000 73.87941  ? 1065 LYS   B CD  1 
ATOM   6261 C CE  . LYS   B 1 453 ? -15.34200 40.07700  45.72300  1.000 76.98011  ? 1065 LYS   B CE  1 
ATOM   6262 N NZ  . LYS   B 1 453 ? -13.87100 39.87700  45.65000  1.000 76.14713  ? 1065 LYS   B NZ  1 
ATOM   6263 N N   . LEU   B 1 454 ? -15.57100 46.14000  45.30400  1.000 81.58981  ? 1066 LEU   B N   1 
ATOM   6264 C CA  . LEU   B 1 454 ? -15.48400 47.39100  46.05600  1.000 82.22531  ? 1066 LEU   B CA  1 
ATOM   6265 C C   . LEU   B 1 454 ? -16.24800 48.51300  45.36300  1.000 88.49858  ? 1066 LEU   B C   1 
ATOM   6266 O O   . LEU   B 1 454 ? -16.74800 49.42600  46.03200  1.000 88.75993  ? 1066 LEU   B O   1 
ATOM   6267 C CB  . LEU   B 1 454 ? -14.02500 47.79600  46.27000  1.000 80.66796  ? 1066 LEU   B CB  1 
ATOM   6268 C CG  . LEU   B 1 454 ? -13.38000 47.27000  47.55300  1.000 82.13034  ? 1066 LEU   B CG  1 
ATOM   6269 C CD1 . LEU   B 1 454 ? -13.07500 45.79400  47.43500  1.000 84.74801  ? 1066 LEU   B CD1 1 
ATOM   6270 C CD2 . LEU   B 1 454 ? -12.12000 48.05500  47.88600  1.000 73.88256  ? 1066 LEU   B CD2 1 
ATOM   6271 N N   . PHE   B 1 455 ? -16.34800 48.46500  44.03300  1.000 88.46548  ? 1067 PHE   B N   1 
ATOM   6272 C CA  . PHE   B 1 455 ? -17.14300 49.45500  43.31300  1.000 84.62706  ? 1067 PHE   B CA  1 
ATOM   6273 C C   . PHE   B 1 455 ? -18.63100 49.24800  43.56800  1.000 85.17217  ? 1067 PHE   B C   1 
ATOM   6274 O O   . PHE   B 1 455 ? -19.35400 50.19800  43.88900  1.000 83.57402  ? 1067 PHE   B O   1 
ATOM   6275 C CB  . PHE   B 1 455 ? -16.82800 49.39000  41.81700  1.000 85.39139  ? 1067 PHE   B CB  1 
ATOM   6276 C CG  . PHE   B 1 455 ? -17.62800 50.35400  40.98200  1.000 84.62765  ? 1067 PHE   B CG  1 
ATOM   6277 C CD1 . PHE   B 1 455 ? -17.20100 51.65900  40.80900  1.000 76.76552  ? 1067 PHE   B CD1 1 
ATOM   6278 C CD2 . PHE   B 1 455 ? -18.79400 49.94700  40.34900  1.000 84.81913  ? 1067 PHE   B CD2 1 
ATOM   6279 C CE1 . PHE   B 1 455 ? -17.92700 52.54600  40.03800  1.000 77.40322  ? 1067 PHE   B CE1 1 
ATOM   6280 C CE2 . PHE   B 1 455 ? -19.52600 50.82800  39.57500  1.000 76.37304  ? 1067 PHE   B CE2 1 
ATOM   6281 C CZ  . PHE   B 1 455 ? -19.09100 52.13000  39.42000  1.000 76.92696  ? 1067 PHE   B CZ  1 
ATOM   6282 N N   . ASN   B 1 456 ? -19.10600 48.00500  43.43900  1.000 89.63544  ? 1068 ASN   B N   1 
ATOM   6283 C CA  . ASN   B 1 456 ? -20.51700 47.71500  43.67400  1.000 90.46503  ? 1068 ASN   B CA  1 
ATOM   6284 C C   . ASN   B 1 456 ? -20.92700 47.99700  45.11400  1.000 88.74615  ? 1068 ASN   B C   1 
ATOM   6285 O O   . ASN   B 1 456 ? -22.11900 48.18600  45.38100  1.000 89.59462  ? 1068 ASN   B O   1 
ATOM   6286 C CB  . ASN   B 1 456 ? -20.81900 46.25700  43.31800  1.000 91.51281  ? 1068 ASN   B CB  1 
ATOM   6287 C CG  . ASN   B 1 456 ? -22.28600 46.02200  42.98200  1.000 99.60271  ? 1068 ASN   B CG  1 
ATOM   6288 O OD1 . ASN   B 1 456 ? -22.63900 45.00200  42.39100  1.000 110.12411 ? 1068 ASN   B OD1 1 
ATOM   6289 N ND2 . ASN   B 1 456 ? -23.14400 46.96900  43.35100  1.000 102.22428 ? 1068 ASN   B ND2 1 
ATOM   6290 N N   . GLN   B 1 457 ? -19.97200 48.03100  46.04200  1.000 87.33542  ? 1069 GLN   B N   1 
ATOM   6291 C CA  . GLN   B 1 457 ? -20.26600 48.38000  47.42500  1.000 93.52436  ? 1069 GLN   B CA  1 
ATOM   6292 C C   . GLN   B 1 457 ? -20.09400 49.86800  47.70500  1.000 91.68016  ? 1069 GLN   B C   1 
ATOM   6293 O O   . GLN   B 1 457 ? -20.71900 50.39000  48.63400  1.000 95.68662  ? 1069 GLN   B O   1 
ATOM   6294 C CB  . GLN   B 1 457 ? -19.38300 47.55500  48.36800  1.000 86.28228  ? 1069 GLN   B CB  1 
ATOM   6295 C CG  . GLN   B 1 457 ? -19.65200 46.05700  48.27100  1.000 87.81889  ? 1069 GLN   B CG  1 
ATOM   6296 C CD  . GLN   B 1 457 ? -18.60700 45.21900  48.97700  1.000 77.55066  ? 1069 GLN   B CD  1 
ATOM   6297 O OE1 . GLN   B 1 457 ? -17.43100 45.58000  49.01800  1.000 79.61080  ? 1069 GLN   B OE1 1 
ATOM   6298 N NE2 . GLN   B 1 457 ? -19.02800 44.08300  49.52500  1.000 72.67694  ? 1069 GLN   B NE2 1 
ATOM   6299 N N   . ASP   B 1 458 ? -19.26700 50.56600  46.92300  1.000 87.75904  ? 1070 ASP   B N   1 
ATOM   6300 C CA  . ASP   B 1 458 ? -19.17800 52.01600  47.05700  1.000 87.07111  ? 1070 ASP   B CA  1 
ATOM   6301 C C   . ASP   B 1 458 ? -20.36400 52.72600  46.41800  1.000 92.43319  ? 1070 ASP   B C   1 
ATOM   6302 O O   . ASP   B 1 458 ? -20.79100 53.77500  46.91500  1.000 94.34387  ? 1070 ASP   B O   1 
ATOM   6303 C CB  . ASP   B 1 458 ? -17.87500 52.53200  46.44500  1.000 82.64487  ? 1070 ASP   B CB  1 
ATOM   6304 C CG  . ASP   B 1 458 ? -16.75600 52.63500  47.46000  1.000 96.85373  ? 1070 ASP   B CG  1 
ATOM   6305 O OD1 . ASP   B 1 458 ? -16.99600 52.31300  48.64400  1.000 102.58981 ? 1070 ASP   B OD1 1 
ATOM   6306 O OD2 . ASP   B 1 458 ? -15.64100 53.05100  47.07900  1.000 96.98228  ? 1070 ASP   B OD2 1 
ATOM   6307 N N   . VAL   B 1 459 ? -20.91100 52.17400  45.33200  1.000 92.02711  ? 1071 VAL   B N   1 
ATOM   6308 C CA  . VAL   B 1 459 ? -22.03100 52.82000  44.64900  1.000 88.64246  ? 1071 VAL   B CA  1 
ATOM   6309 C C   . VAL   B 1 459 ? -23.28400 52.78400  45.51800  1.000 90.04893  ? 1071 VAL   B C   1 
ATOM   6310 O O   . VAL   B 1 459 ? -23.96400 53.80300  45.68900  1.000 87.96369  ? 1071 VAL   B O   1 
ATOM   6311 C CB  . VAL   B 1 459 ? -22.27700 52.17200  43.27400  1.000 86.91757  ? 1071 VAL   B CB  1 
ATOM   6312 C CG1 . VAL   B 1 459 ? -23.48000 52.80700  42.59700  1.000 81.77357  ? 1071 VAL   B CG1 1 
ATOM   6313 C CG2 . VAL   B 1 459 ? -21.05200 52.32500  42.39100  1.000 84.87746  ? 1071 VAL   B CG2 1 
ATOM   6314 N N   . ASP   B 1 460 ? -23.60900 51.61200  46.08000  1.000 91.48682  ? 1072 ASP   B N   1 
ATOM   6315 C CA  . ASP   B 1 460 ? -24.77700 51.51200  46.95400  1.000 95.14847  ? 1072 ASP   B CA  1 
ATOM   6316 C C   . ASP   B 1 460 ? -24.66800 52.45000  48.15100  1.000 89.85547  ? 1072 ASP   B C   1 
ATOM   6317 O O   . ASP   B 1 460 ? -25.67900 53.00300  48.59900  1.000 85.65826  ? 1072 ASP   B O   1 
ATOM   6318 C CB  . ASP   B 1 460 ? -24.99100 50.04900  47.38700  1.000 95.63662  ? 1072 ASP   B CB  1 
ATOM   6319 C CG  . ASP   B 1 460 ? -23.98400 49.55000  48.44200  1.000 94.79822  ? 1072 ASP   B CG  1 
ATOM   6320 O OD1 . ASP   B 1 460 ? -23.36700 50.33900  49.18600  1.000 93.84923  ? 1072 ASP   B OD1 1 
ATOM   6321 O OD2 . ASP   B 1 460 ? -23.81500 48.31500  48.52900  1.000 93.86678  ? 1072 ASP   B OD2 1 
ATOM   6322 N N   . ALA   B 1 461 ? -23.45100 52.64500  48.67000  1.000 86.60318  ? 1073 ALA   B N   1 
ATOM   6323 C CA  . ALA   B 1 461 ? -23.23900 53.61100  49.74100  1.000 86.63617  ? 1073 ALA   B CA  1 
ATOM   6324 C C   . ALA   B 1 461 ? -23.59900 55.02300  49.30000  1.000 88.38446  ? 1073 ALA   B C   1 
ATOM   6325 O O   . ALA   B 1 461 ? -24.09500 55.81800  50.10600  1.000 84.39077  ? 1073 ALA   B O   1 
ATOM   6326 C CB  . ALA   B 1 461 ? -21.78500 53.55500  50.20800  1.000 81.71088  ? 1073 ALA   B CB  1 
ATOM   6327 N N   . ALA   B 1 462 ? -23.36600 55.34600  48.02600  1.000 90.88867  ? 1074 ALA   B N   1 
ATOM   6328 C CA  . ALA   B 1 462 ? -23.72000 56.65600  47.50000  1.000 85.54195  ? 1074 ALA   B CA  1 
ATOM   6329 C C   . ALA   B 1 462 ? -25.19700 56.77100  47.15000  1.000 82.36207  ? 1074 ALA   B C   1 
ATOM   6330 O O   . ALA   B 1 462 ? -25.69700 57.89200  47.04100  1.000 80.96832  ? 1074 ALA   B O   1 
ATOM   6331 C CB  . ALA   B 1 462 ? -22.87200 56.98100  46.26700  1.000 79.35920  ? 1074 ALA   B CB  1 
ATOM   6332 N N   . VAL   B 1 463 ? -25.90400 55.65500  46.97300  1.000 80.53265  ? 1075 VAL   B N   1 
ATOM   6333 C CA  . VAL   B 1 463 ? -27.33800 55.71400  46.68800  1.000 83.71070  ? 1075 VAL   B CA  1 
ATOM   6334 C C   . VAL   B 1 463 ? -28.15800 55.75700  47.97300  1.000 86.53466  ? 1075 VAL   B C   1 
ATOM   6335 O O   . VAL   B 1 463 ? -29.14800 56.48900  48.05600  1.000 83.36528  ? 1075 VAL   B O   1 
ATOM   6336 C CB  . VAL   B 1 463 ? -27.76500 54.53700  45.78700  1.000 88.99082  ? 1075 VAL   B CB  1 
ATOM   6337 C CG1 . VAL   B 1 463 ? -29.17600 54.76100  45.25600  1.000 81.84312  ? 1075 VAL   B CG1 1 
ATOM   6338 C CG2 . VAL   B 1 463 ? -26.79700 54.37400  44.62900  1.000 88.29982  ? 1075 VAL   B CG2 1 
ATOM   6339 N N   . ARG   B 1 464 ? -27.77700 54.97500  48.98900  1.000 91.61223  ? 1076 ARG   B N   1 
ATOM   6340 C CA  . ARG   B 1 464 ? -28.36800 55.16400  50.31200  1.000 89.11930  ? 1076 ARG   B CA  1 
ATOM   6341 C C   . ARG   B 1 464 ? -28.02600 56.54400  50.85800  1.000 86.49749  ? 1076 ARG   B C   1 
ATOM   6342 O O   . ARG   B 1 464 ? -28.88000 57.21900  51.44700  1.000 85.30839  ? 1076 ARG   B O   1 
ATOM   6343 C CB  . ARG   B 1 464 ? -27.89800 54.07100  51.27300  1.000 85.09755  ? 1076 ARG   B CB  1 
ATOM   6344 C CG  . ARG   B 1 464 ? -27.99400 52.65800  50.72400  1.000 86.91439  ? 1076 ARG   B CG  1 
ATOM   6345 C CD  . ARG   B 1 464 ? -26.95800 51.74500  51.36200  1.000 87.70515  ? 1076 ARG   B CD  1 
ATOM   6346 N NE  . ARG   B 1 464 ? -25.82800 52.49100  51.90300  1.000 88.00980  ? 1076 ARG   B NE  1 
ATOM   6347 C CZ  . ARG   B 1 464 ? -24.87900 51.96400  52.66500  1.000 90.38126  ? 1076 ARG   B CZ  1 
ATOM   6348 N NH1 . ARG   B 1 464 ? -24.88200 50.68000  52.98300  1.000 95.98898  ? 1076 ARG   B NH1 1 
ATOM   6349 N NH2 . ARG   B 1 464 ? -23.90100 52.74500  53.11700  1.000 90.28894  ? 1076 ARG   B NH2 1 
ATOM   6350 N N   . GLY   B 1 465 ? -26.78000 56.98600  50.65500  1.000 83.86932  ? 1077 GLY   B N   1 
ATOM   6351 C CA  . GLY   B 1 465 ? -26.37900 58.33700  51.01000  1.000 84.17709  ? 1077 GLY   B CA  1 
ATOM   6352 C C   . GLY   B 1 465 ? -27.15200 59.42000  50.28400  1.000 85.12458  ? 1077 GLY   B C   1 
ATOM   6353 O O   . GLY   B 1 465 ? -27.14100 60.57500  50.72200  1.000 83.64889  ? 1077 GLY   B O   1 
ATOM   6354 N N   . ILE   B 1 466 ? -27.81000 59.07700  49.17400  1.000 90.76530  ? 1078 ILE   B N   1 
ATOM   6355 C CA  . ILE   B 1 466 ? -28.74900 59.99700  48.54100  1.000 88.85727  ? 1078 ILE   B CA  1 
ATOM   6356 C C   . ILE   B 1 466 ? -30.11100 59.93900  49.22600  1.000 84.37733  ? 1078 ILE   B C   1 
ATOM   6357 O O   . ILE   B 1 466 ? -30.77800 60.97000  49.37200  1.000 87.78402  ? 1078 ILE   B O   1 
ATOM   6358 C CB  . ILE   B 1 466 ? -28.86700 59.69500  47.03500  1.000 87.99416  ? 1078 ILE   B CB  1 
ATOM   6359 C CG1 . ILE   B 1 466 ? -27.58600 60.07900  46.30000  1.000 85.63318  ? 1078 ILE   B CG1 1 
ATOM   6360 C CG2 . ILE   B 1 466 ? -30.02300 60.45000  46.41600  1.000 86.27509  ? 1078 ILE   B CG2 1 
ATOM   6361 C CD1 . ILE   B 1 466 ? -27.55400 59.61000  44.85900  1.000 85.35504  ? 1078 ILE   B CD1 1 
ATOM   6362 N N   . LEU   B 1 467 ? -30.53700 58.75500  49.67200  1.000 79.03654  ? 1079 LEU   B N   1 
ATOM   6363 C CA  . LEU   B 1 467 ? -31.86300 58.60100  50.25900  1.000 85.02417  ? 1079 LEU   B CA  1 
ATOM   6364 C C   . LEU   B 1 467 ? -31.92100 59.01700  51.72500  1.000 92.00140  ? 1079 LEU   B C   1 
ATOM   6365 O O   . LEU   B 1 467 ? -33.01600 59.29200  52.23000  1.000 92.00270  ? 1079 LEU   B O   1 
ATOM   6366 C CB  . LEU   B 1 467 ? -32.33800 57.15400  50.10700  1.000 88.26503  ? 1079 LEU   B CB  1 
ATOM   6367 C CG  . LEU   B 1 467 ? -32.42700 56.63800  48.66500  1.000 87.13757  ? 1079 LEU   B CG  1 
ATOM   6368 C CD1 . LEU   B 1 467 ? -33.15800 55.30500  48.60200  1.000 79.20076  ? 1079 LEU   B CD1 1 
ATOM   6369 C CD2 . LEU   B 1 467 ? -33.08800 57.66300  47.74800  1.000 80.87949  ? 1079 LEU   B CD2 1 
ATOM   6370 N N   . ARG   B 1 468 ? -30.78400 59.06800  52.41900  1.000 91.20850  ? 1080 ARG   B N   1 
ATOM   6371 C CA  . ARG   B 1 468 ? -30.72700 59.56200  53.78900  1.000 83.60184  ? 1080 ARG   B CA  1 
ATOM   6372 C C   . ARG   B 1 468 ? -30.45900 61.06100  53.85700  1.000 85.49693  ? 1080 ARG   B C   1 
ATOM   6373 O O   . ARG   B 1 468 ? -30.15500 61.57600  54.93800  1.000 90.90982  ? 1080 ARG   B O   1 
ATOM   6374 C CB  . ARG   B 1 468 ? -29.65900 58.80600  54.58500  1.000 77.92655  ? 1080 ARG   B CB  1 
ATOM   6375 N N   . ASN   B 1 469 ? -30.55500 61.76100  52.72900  1.000 85.13560  ? 1081 ASN   B N   1 
ATOM   6376 C CA  . ASN   B 1 469 ? -30.42000 63.21200  52.66400  1.000 88.64873  ? 1081 ASN   B CA  1 
ATOM   6377 C C   . ASN   B 1 469 ? -31.75900 63.79200  52.23000  1.000 92.10141  ? 1081 ASN   B C   1 
ATOM   6378 O O   . ASN   B 1 469 ? -32.23100 63.50500  51.12400  1.000 91.19041  ? 1081 ASN   B O   1 
ATOM   6379 C CB  . ASN   B 1 469 ? -29.30800 63.62000  51.69200  1.000 88.41641  ? 1081 ASN   B CB  1 
ATOM   6380 C CG  . ASN   B 1 469 ? -28.83300 65.04800  51.90600  1.000 88.20610  ? 1081 ASN   B CG  1 
ATOM   6381 O OD1 . ASN   B 1 469 ? -29.58400 66.00300  51.70400  1.000 87.71143  ? 1081 ASN   B OD1 1 
ATOM   6382 N ND2 . ASN   B 1 469 ? -27.57700 65.19900  52.31000  1.000 84.91165  ? 1081 ASN   B ND2 1 
ATOM   6383 N N   . ALA   B 1 470 ? -32.37100 64.59800  53.10000  1.000 91.32900  ? 1082 ALA   B N   1 
ATOM   6384 C CA  . ALA   B 1 470 ? -33.67900 65.16900  52.80100  1.000 90.75618  ? 1082 ALA   B CA  1 
ATOM   6385 C C   . ALA   B 1 470 ? -33.62700 66.25900  51.73900  1.000 96.63281  ? 1082 ALA   B C   1 
ATOM   6386 O O   . ALA   B 1 470 ? -34.68400 66.65000  51.23100  1.000 97.10497  ? 1082 ALA   B O   1 
ATOM   6387 C CB  . ALA   B 1 470 ? -34.31300 65.72500  54.07700  1.000 92.91838  ? 1082 ALA   B CB  1 
ATOM   6388 N N   . LYS   B 1 471 ? -32.43900 66.76500  51.40200  1.000 92.95921  ? 1083 LYS   B N   1 
ATOM   6389 C CA  . LYS   B 1 471 ? -32.30900 67.73800  50.32400  1.000 94.79711  ? 1083 LYS   B CA  1 
ATOM   6390 C C   . LYS   B 1 471 ? -32.10300 67.07700  48.97000  1.000 99.57176  ? 1083 LYS   B C   1 
ATOM   6391 O O   . LYS   B 1 471 ? -32.45400 67.66700  47.94200  1.000 103.65113 ? 1083 LYS   B O   1 
ATOM   6392 C CB  . LYS   B 1 471 ? -31.15000 68.69800  50.61000  1.000 92.05624  ? 1083 LYS   B CB  1 
ATOM   6393 C CG  . LYS   B 1 471 ? -31.56700 69.97500  51.31600  1.000 95.34567  ? 1083 LYS   B CG  1 
ATOM   6394 C CD  . LYS   B 1 471 ? -30.36000 70.71600  51.85400  1.000 96.23548  ? 1083 LYS   B CD  1 
ATOM   6395 C CE  . LYS   B 1 471 ? -29.41400 71.08500  50.73700  1.000 93.44910  ? 1083 LYS   B CE  1 
ATOM   6396 N NZ  . LYS   B 1 471 ? -28.32000 71.98300  51.20200  1.000 95.95471  ? 1083 LYS   B NZ  1 
ATOM   6397 N N   . LEU   B 1 472 ? -31.54700 65.86700  48.94400  1.000 96.72766  ? 1084 LEU   B N   1 
ATOM   6398 C CA  . LEU   B 1 472 ? -31.34900 65.13400  47.70100  1.000 93.50808  ? 1084 LEU   B CA  1 
ATOM   6399 C C   . LEU   B 1 472 ? -32.46200 64.14000  47.39900  1.000 92.59166  ? 1084 LEU   B C   1 
ATOM   6400 O O   . LEU   B 1 472 ? -32.85700 64.01200  46.23700  1.000 93.08010  ? 1084 LEU   B O   1 
ATOM   6401 C CB  . LEU   B 1 472 ? -30.01000 64.39300  47.72400  1.000 83.74590  ? 1084 LEU   B CB  1 
ATOM   6402 C CG  . LEU   B 1 472 ? -28.79800 65.15700  48.24100  1.000 85.98268  ? 1084 LEU   B CG  1 
ATOM   6403 C CD1 . LEU   B 1 472 ? -27.59900 64.23500  48.28500  1.000 83.98950  ? 1084 LEU   B CD1 1 
ATOM   6404 C CD2 . LEU   B 1 472 ? -28.52100 66.36900  47.36900  1.000 87.11887  ? 1084 LEU   B CD2 1 
ATOM   6405 N N   . LYS   B 1 473 ? -32.97900 63.43400  48.40700  1.000 87.86199  ? 1085 LYS   B N   1 
ATOM   6406 C CA  . LYS   B 1 473 ? -33.97200 62.39100  48.14500  1.000 85.69252  ? 1085 LYS   B CA  1 
ATOM   6407 C C   . LYS   B 1 473 ? -35.17200 62.88500  47.34500  1.000 88.44090  ? 1085 LYS   B C   1 
ATOM   6408 O O   . LYS   B 1 473 ? -35.53300 62.22300  46.35900  1.000 86.02153  ? 1085 LYS   B O   1 
ATOM   6409 C CB  . LYS   B 1 473 ? -34.41800 61.73300  49.45900  1.000 82.43201  ? 1085 LYS   B CB  1 
ATOM   6410 C CG  . LYS   B 1 473 ? -35.39700 60.58500  49.23200  1.000 82.91575  ? 1085 LYS   B CG  1 
ATOM   6411 C CD  . LYS   B 1 473 ? -35.67100 59.76600  50.48000  1.000 81.15325  ? 1085 LYS   B CD  1 
ATOM   6412 C CE  . LYS   B 1 473 ? -36.53800 58.55900  50.14000  1.000 84.07121  ? 1085 LYS   B CE  1 
ATOM   6413 N NZ  . LYS   B 1 473 ? -37.02200 57.83500  51.35000  1.000 92.62814  ? 1085 LYS   B NZ  1 
ATOM   6414 N N   . PRO   B 1 474 ? -35.81400 64.01600  47.67400  1.000 93.00450  ? 1086 PRO   B N   1 
ATOM   6415 C CA  . PRO   B 1 474 ? -36.90400 64.49500  46.80400  1.000 94.02787  ? 1086 PRO   B CA  1 
ATOM   6416 C C   . PRO   B 1 474 ? -36.46500 64.75900  45.37200  1.000 93.22225  ? 1086 PRO   B C   1 
ATOM   6417 O O   . PRO   B 1 474 ? -37.27900 64.61600  44.45100  1.000 92.52197  ? 1086 PRO   B O   1 
ATOM   6418 C CB  . PRO   B 1 474 ? -37.37200 65.78400  47.49700  1.000 92.36754  ? 1086 PRO   B CB  1 
ATOM   6419 C CG  . PRO   B 1 474 ? -36.93100 65.64400  48.90700  1.000 98.59678  ? 1086 PRO   B CG  1 
ATOM   6420 C CD  . PRO   B 1 474 ? -35.64900 64.87700  48.85900  1.000 93.13279  ? 1086 PRO   B CD  1 
ATOM   6421 N N   . VAL   B 1 475 ? -35.20200 65.13500  45.15700  1.000 91.70882  ? 1087 VAL   B N   1 
ATOM   6422 C CA  . VAL   B 1 475 ? -34.69600 65.32700  43.80000  1.000 89.84237  ? 1087 VAL   B CA  1 
ATOM   6423 C C   . VAL   B 1 475 ? -34.51600 63.98200  43.10500  1.000 87.72364  ? 1087 VAL   B C   1 
ATOM   6424 O O   . VAL   B 1 475 ? -35.00500 63.76700  41.98900  1.000 81.36659  ? 1087 VAL   B O   1 
ATOM   6425 C CB  . VAL   B 1 475 ? -33.37900 66.12400  43.82700  1.000 93.48881  ? 1087 VAL   B CB  1 
ATOM   6426 C CG1 . VAL   B 1 475 ? -33.03600 66.63900  42.43600  1.000 85.60632  ? 1087 VAL   B CG1 1 
ATOM   6427 C CG2 . VAL   B 1 475 ? -33.46800 67.26800  44.82800  1.000 93.30475  ? 1087 VAL   B CG2 1 
ATOM   6428 N N   . TYR   B 1 476 ? -33.80800 63.05700  43.76000  1.000 89.49279  ? 1088 TYR   B N   1 
ATOM   6429 C CA  . TYR   B 1 476 ? -33.58200 61.72300  43.21300  1.000 87.14333  ? 1088 TYR   B CA  1 
ATOM   6430 C C   . TYR   B 1 476 ? -34.88700 60.96700  42.99200  1.000 87.14239  ? 1088 TYR   B C   1 
ATOM   6431 O O   . TYR   B 1 476 ? -34.94000 60.08800  42.12500  1.000 88.82784  ? 1088 TYR   B O   1 
ATOM   6432 C CB  . TYR   B 1 476 ? -32.63600 60.95700  44.15400  1.000 85.44511  ? 1088 TYR   B CB  1 
ATOM   6433 C CG  . TYR   B 1 476 ? -32.33100 59.50500  43.80900  1.000 93.38694  ? 1088 TYR   B CG  1 
ATOM   6434 C CD1 . TYR   B 1 476 ? -33.25600 58.49100  44.04800  1.000 91.01789  ? 1088 TYR   B CD1 1 
ATOM   6435 C CD2 . TYR   B 1 476 ? -31.10400 59.15000  43.25300  1.000 94.30657  ? 1088 TYR   B CD2 1 
ATOM   6436 C CE1 . TYR   B 1 476 ? -32.97100 57.17000  43.73700  1.000 96.38393  ? 1088 TYR   B CE1 1 
ATOM   6437 C CE2 . TYR   B 1 476 ? -30.81000 57.83100  42.93900  1.000 92.05418  ? 1088 TYR   B CE2 1 
ATOM   6438 C CZ  . TYR   B 1 476 ? -31.74700 56.84600  43.18300  1.000 96.76921  ? 1088 TYR   B CZ  1 
ATOM   6439 O OH  . TYR   B 1 476 ? -31.46300 55.53400  42.87400  1.000 97.42770  ? 1088 TYR   B OH  1 
ATOM   6440 N N   . ASP   B 1 477 ? -35.94300 61.30300  43.74100  1.000 88.92870  ? 1089 ASP   B N   1 
ATOM   6441 C CA  . ASP   B 1 477 ? -37.21200 60.59500  43.60000  1.000 84.82258  ? 1089 ASP   B CA  1 
ATOM   6442 C C   . ASP   B 1 477 ? -37.91300 60.92700  42.28700  1.000 75.38969  ? 1089 ASP   B C   1 
ATOM   6443 O O   . ASP   B 1 477 ? -38.57800 60.06100  41.70800  1.000 64.89992  ? 1089 ASP   B O   1 
ATOM   6444 C CB  . ASP   B 1 477 ? -38.14200 60.91600  44.77700  1.000 88.81510  ? 1089 ASP   B CB  1 
ATOM   6445 C CG  . ASP   B 1 477 ? -37.73300 60.21400  46.06800  1.000 92.75642  ? 1089 ASP   B CG  1 
ATOM   6446 O OD1 . ASP   B 1 477 ? -37.44400 59.00100  46.02700  1.000 92.42411  ? 1089 ASP   B OD1 1 
ATOM   6447 O OD2 . ASP   B 1 477 ? -37.74800 60.86700  47.13500  1.000 95.63201  ? 1089 ASP   B OD2 1 
ATOM   6448 N N   . SER   B 1 478 ? -37.78000 62.16300  41.80400  1.000 74.57045  ? 1090 SER   B N   1 
ATOM   6449 C CA  . SER   B 1 478 ? -38.50700 62.61900  40.62500  1.000 81.96021  ? 1090 SER   B CA  1 
ATOM   6450 C C   . SER   B 1 478 ? -37.74200 62.42600  39.32000  1.000 84.33220  ? 1090 SER   B C   1 
ATOM   6451 O O   . SER   B 1 478 ? -38.30700 62.67300  38.24700  1.000 68.46056  ? 1090 SER   B O   1 
ATOM   6452 C CB  . SER   B 1 478 ? -38.87600 64.10000  40.78000  1.000 80.06509  ? 1090 SER   B CB  1 
ATOM   6453 O OG  . SER   B 1 478 ? -37.77300 64.85200  41.25600  1.000 83.91767  ? 1090 SER   B OG  1 
ATOM   6454 N N   . LEU   B 1 479 ? -36.48700 61.98800  39.37700  1.000 83.59896  ? 1091 LEU   B N   1 
ATOM   6455 C CA  . LEU   B 1 479 ? -35.67900 61.85700  38.17600  1.000 78.66699  ? 1091 LEU   B CA  1 
ATOM   6456 C C   . LEU   B 1 479 ? -35.95200 60.53100  37.47000  1.000 82.86514  ? 1091 LEU   B C   1 
ATOM   6457 O O   . LEU   B 1 479 ? -36.44900 59.56700  38.06000  1.000 76.65058  ? 1091 LEU   B O   1 
ATOM   6458 C CB  . LEU   B 1 479 ? -34.19300 61.97000  38.51300  1.000 76.73919  ? 1091 LEU   B CB  1 
ATOM   6459 C CG  . LEU   B 1 479 ? -33.69300 63.36700  38.88200  1.000 79.27453  ? 1091 LEU   B CG  1 
ATOM   6460 C CD1 . LEU   B 1 479 ? -32.25000 63.31600  39.36200  1.000 82.29153  ? 1091 LEU   B CD1 1 
ATOM   6461 C CD2 . LEU   B 1 479 ? -33.83500 64.30900  37.69900  1.000 71.35332  ? 1091 LEU   B CD2 1 
ATOM   6462 N N   . ASP   B 1 480 ? -35.61000 60.49500  36.18600  1.000 87.15111  ? 1092 ASP   B N   1 
ATOM   6463 C CA  . ASP   B 1 480 ? -35.73000 59.28200  35.38700  1.000 84.97368  ? 1092 ASP   B CA  1 
ATOM   6464 C C   . ASP   B 1 480 ? -34.61200 58.31400  35.77600  1.000 84.50033  ? 1092 ASP   B C   1 
ATOM   6465 O O   . ASP   B 1 480 ? -33.86200 58.53600  36.72800  1.000 83.41817  ? 1092 ASP   B O   1 
ATOM   6466 C CB  . ASP   B 1 480 ? -35.71800 59.63100  33.90000  1.000 77.58531  ? 1092 ASP   B CB  1 
ATOM   6467 C CG  . ASP   B 1 480 ? -34.36400 60.15000  33.41800  1.000 78.85962  ? 1092 ASP   B CG  1 
ATOM   6468 O OD1 . ASP   B 1 480 ? -33.38700 60.14700  34.19400  1.000 79.95608  ? 1092 ASP   B OD1 1 
ATOM   6469 O OD2 . ASP   B 1 480 ? -34.28000 60.57300  32.24500  1.000 85.47926  ? 1092 ASP   B OD2 1 
ATOM   6470 N N   . ALA   B 1 481 ? -34.46500 57.23100  35.01200  1.000 77.85961  ? 1093 ALA   B N   1 
ATOM   6471 C CA  . ALA   B 1 481 ? -33.36900 56.30400  35.27400  1.000 69.55038  ? 1093 ALA   B CA  1 
ATOM   6472 C C   . ALA   B 1 481 ? -32.02500 56.92500  34.91700  1.000 75.09366  ? 1093 ALA   B C   1 
ATOM   6473 O O   . ALA   B 1 481 ? -31.02900 56.71100  35.61900  1.000 82.39390  ? 1093 ALA   B O   1 
ATOM   6474 C CB  . ALA   B 1 481 ? -33.58100 55.00400  34.50100  1.000 63.75544  ? 1093 ALA   B CB  1 
ATOM   6475 N N   . VAL   B 1 482 ? -31.98000 57.70900  33.84000  1.000 73.06062  ? 1094 VAL   B N   1 
ATOM   6476 C CA  . VAL   B 1 482 ? -30.70800 58.22800  33.34800  1.000 73.65500  ? 1094 VAL   B CA  1 
ATOM   6477 C C   . VAL   B 1 482 ? -30.19900 59.34600  34.25400  1.000 73.97635  ? 1094 VAL   B C   1 
ATOM   6478 O O   . VAL   B 1 482 ? -29.08200 59.28200  34.78000  1.000 71.15461  ? 1094 VAL   B O   1 
ATOM   6479 C CB  . VAL   B 1 482 ? -30.84700 58.69700  31.88800  1.000 76.69201  ? 1094 VAL   B CB  1 
ATOM   6480 C CG1 . VAL   B 1 482 ? -29.55400 59.32200  31.40000  1.000 69.32599  ? 1094 VAL   B CG1 1 
ATOM   6481 C CG2 . VAL   B 1 482 ? -31.24900 57.53400  30.99200  1.000 71.76620  ? 1094 VAL   B CG2 1 
ATOM   6482 N N   . ARG   B 1 483 ? -31.01400 60.38400  34.45900  1.000 72.75712  ? 1095 ARG   B N   1 
ATOM   6483 C CA  . ARG   B 1 483 ? -30.55800 61.51600  35.26100  1.000 70.90586  ? 1095 ARG   B CA  1 
ATOM   6484 C C   . ARG   B 1 483 ? -30.39800 61.16400  36.73500  1.000 78.42928  ? 1095 ARG   B C   1 
ATOM   6485 O O   . ARG   B 1 483 ? -29.62900 61.83500  37.43300  1.000 77.82696  ? 1095 ARG   B O   1 
ATOM   6486 C CB  . ARG   B 1 483 ? -31.50100 62.70700  35.09200  1.000 72.16147  ? 1095 ARG   B CB  1 
ATOM   6487 C CG  . ARG   B 1 483 ? -32.11600 62.82000  33.70600  1.000 73.77083  ? 1095 ARG   B CG  1 
ATOM   6488 C CD  . ARG   B 1 483 ? -33.37100 63.66500  33.73600  1.000 70.02821  ? 1095 ARG   B CD  1 
ATOM   6489 N NE  . ARG   B 1 483 ? -34.16600 63.52900  32.52100  1.000 69.95956  ? 1095 ARG   B NE  1 
ATOM   6490 C CZ  . ARG   B 1 483 ? -34.18500 64.41300  31.53400  1.000 68.04805  ? 1095 ARG   B CZ  1 
ATOM   6491 N NH1 . ARG   B 1 483 ? -33.41800 65.49100  31.55700  1.000 66.80309  ? 1095 ARG   B NH1 1 
ATOM   6492 N NH2 . ARG   B 1 483 ? -34.99100 64.21000  30.49600  1.000 66.67827  ? 1095 ARG   B NH2 1 
ATOM   6493 N N   . ARG   B 1 484 ? -31.10300 60.14200  37.23100  1.000 78.73722  ? 1096 ARG   B N   1 
ATOM   6494 C CA  . ARG   B 1 484 ? -30.74400 59.58000  38.53100  1.000 75.58333  ? 1096 ARG   B CA  1 
ATOM   6495 C C   . ARG   B 1 484 ? -29.29400 59.12500  38.52400  1.000 74.02938  ? 1096 ARG   B C   1 
ATOM   6496 O O   . ARG   B 1 484 ? -28.51000 59.49100  39.40600  1.000 74.72819  ? 1096 ARG   B O   1 
ATOM   6497 C CB  . ARG   B 1 484 ? -31.65900 58.41000  38.89400  1.000 78.25076  ? 1096 ARG   B CB  1 
ATOM   6498 C CG  . ARG   B 1 484 ? -32.95100 58.78400  39.60400  1.000 83.42675  ? 1096 ARG   B CG  1 
ATOM   6499 C CD  . ARG   B 1 484 ? -33.77500 57.53500  39.88600  1.000 82.94231  ? 1096 ARG   B CD  1 
ATOM   6500 N NE  . ARG   B 1 484 ? -34.98500 57.82000  40.64700  1.000 89.02527  ? 1096 ARG   B NE  1 
ATOM   6501 C CZ  . ARG   B 1 484 ? -35.88800 56.90900  40.98500  1.000 84.59472  ? 1096 ARG   B CZ  1 
ATOM   6502 N NH1 . ARG   B 1 484 ? -35.73200 55.63300  40.67000  1.000 85.45207  ? 1096 ARG   B NH1 1 
ATOM   6503 N NH2 . ARG   B 1 484 ? -36.97100 57.28500  41.65900  1.000 77.04510  ? 1096 ARG   B NH2 1 
ATOM   6504 N N   . ALA   B 1 485 ? -28.92000 58.33000  37.51700  1.000 76.63881  ? 1097 ALA   B N   1 
ATOM   6505 C CA  . ALA   B 1 485 ? -27.53500 57.89400  37.38100  1.000 79.07250  ? 1097 ALA   B CA  1 
ATOM   6506 C C   . ALA   B 1 485 ? -26.58500 59.08200  37.29400  1.000 77.22681  ? 1097 ALA   B C   1 
ATOM   6507 O O   . ALA   B 1 485 ? -25.46200 59.02800  37.80700  1.000 76.01688  ? 1097 ALA   B O   1 
ATOM   6508 C CB  . ALA   B 1 485 ? -27.38800 56.99400  36.15400  1.000 78.51224  ? 1097 ALA   B CB  1 
ATOM   6509 N N   . ALA   B 1 486 ? -27.02000 60.17000  36.65300  1.000 73.06592  ? 1098 ALA   B N   1 
ATOM   6510 C CA  . ALA   B 1 486 ? -26.20100 61.37700  36.62400  1.000 75.71472  ? 1098 ALA   B CA  1 
ATOM   6511 C C   . ALA   B 1 486 ? -26.02900 61.96000  38.02200  1.000 79.44995  ? 1098 ALA   B C   1 
ATOM   6512 O O   . ALA   B 1 486 ? -24.96200 62.49100  38.35300  1.000 76.93217  ? 1098 ALA   B O   1 
ATOM   6513 C CB  . ALA   B 1 486 ? -26.81600 62.40500  35.67500  1.000 75.18825  ? 1098 ALA   B CB  1 
ATOM   6514 N N   . LEU   B 1 487 ? -27.06600 61.86100  38.86200  1.000 79.15598  ? 1099 LEU   B N   1 
ATOM   6515 C CA  . LEU   B 1 487 ? -26.95800 62.34000  40.23900  1.000 80.95193  ? 1099 LEU   B CA  1 
ATOM   6516 C C   . LEU   B 1 487 ? -26.01500 61.46300  41.05500  1.000 76.26329  ? 1099 LEU   B C   1 
ATOM   6517 O O   . LEU   B 1 487 ? -25.18400 61.97500  41.81600  1.000 69.85402  ? 1099 LEU   B O   1 
ATOM   6518 C CB  . LEU   B 1 487 ? -28.34600 62.39100  40.88700  1.000 83.82841  ? 1099 LEU   B CB  1 
ATOM   6519 C CG  . LEU   B 1 487 ? -28.65500 63.39100  42.01300  1.000 77.95643  ? 1099 LEU   B CG  1 
ATOM   6520 C CD1 . LEU   B 1 487 ? -30.12800 63.33400  42.38300  1.000 76.14807  ? 1099 LEU   B CD1 1 
ATOM   6521 C CD2 . LEU   B 1 487 ? -27.81200 63.16200  43.25400  1.000 75.82689  ? 1099 LEU   B CD2 1 
ATOM   6522 N N   . ILE   B 1 488 ? -26.13400 60.14000  40.91500  1.000 76.37130  ? 1100 ILE   B N   1 
ATOM   6523 C CA  . ILE   B 1 488 ? -25.27400 59.22400  41.66000  1.000 78.00982  ? 1100 ILE   B CA  1 
ATOM   6524 C C   . ILE   B 1 488 ? -23.81600 59.39100  41.25600  1.000 76.36892  ? 1100 ILE   B C   1 
ATOM   6525 O O   . ILE   B 1 488 ? -22.91000 59.12400  42.05500  1.000 74.70975  ? 1100 ILE   B O   1 
ATOM   6526 C CB  . ILE   B 1 488 ? -25.75200 57.76900  41.46900  1.000 77.80036  ? 1100 ILE   B CB  1 
ATOM   6527 C CG1 . ILE   B 1 488 ? -27.27500 57.68300  41.59200  1.000 77.81715  ? 1100 ILE   B CG1 1 
ATOM   6528 C CG2 . ILE   B 1 488 ? -25.08700 56.84300  42.47700  1.000 74.92150  ? 1100 ILE   B CG2 1 
ATOM   6529 C CD1 . ILE   B 1 488 ? -27.81300 56.27000  41.54200  1.000 77.77351  ? 1100 ILE   B CD1 1 
ATOM   6530 N N   . ASN   B 1 489 ? -23.56000 59.83300  40.02100  1.000 81.00088  ? 1101 ASN   B N   1 
ATOM   6531 C CA  . ASN   B 1 489 ? -22.18400 60.07900  39.59900  1.000 81.66001  ? 1101 ASN   B CA  1 
ATOM   6532 C C   . ASN   B 1 489 ? -21.59100 61.27700  40.33100  1.000 80.52333  ? 1101 ASN   B C   1 
ATOM   6533 O O   . ASN   B 1 489 ? -20.38800 61.29500  40.61400  1.000 81.77374  ? 1101 ASN   B O   1 
ATOM   6534 C CB  . ASN   B 1 489 ? -22.13400 60.27300  38.08000  1.000 78.01675  ? 1101 ASN   B CB  1 
ATOM   6535 C CG  . ASN   B 1 489 ? -20.71300 60.36000  37.53500  1.000 80.41809  ? 1101 ASN   B CG  1 
ATOM   6536 O OD1 . ASN   B 1 489 ? -19.91000 61.18800  37.96400  1.000 79.76607  ? 1101 ASN   B OD1 1 
ATOM   6537 N ND2 . ASN   B 1 489 ? -20.39600 59.48500  36.58700  1.000 81.00078  ? 1101 ASN   B ND2 1 
ATOM   6538 N N   . MET   B 1 490 ? -22.41800 62.26900  40.66700  1.000 82.17313  ? 1102 MET   B N   1 
ATOM   6539 C CA  . MET   B 1 490 ? -21.93300 63.40400  41.44200  1.000 86.11697  ? 1102 MET   B CA  1 
ATOM   6540 C C   . MET   B 1 490 ? -21.74700 63.03900  42.91200  1.000 85.34924  ? 1102 MET   B C   1 
ATOM   6541 O O   . MET   B 1 490 ? -20.75200 63.43400  43.53100  1.000 79.84591  ? 1102 MET   B O   1 
ATOM   6542 C CB  . MET   B 1 490 ? -22.89400 64.58500  41.29900  1.000 82.85751  ? 1102 MET   B CB  1 
ATOM   6543 C CG  . MET   B 1 490 ? -23.03200 65.11100  39.88000  1.000 74.30441  ? 1102 MET   B CG  1 
ATOM   6544 S SD  . MET   B 1 490 ? -24.04800 66.59900  39.82600  1.000 84.49768  ? 1102 MET   B SD  1 
ATOM   6545 C CE  . MET   B 1 490 ? -25.62000 65.94300  40.38200  1.000 76.24880  ? 1102 MET   B CE  1 
ATOM   6546 N N   . VAL   B 1 491 ? -22.68900 62.28200  43.48200  1.000 83.59057  ? 1103 VAL   B N   1 
ATOM   6547 C CA  . VAL   B 1 491 ? -22.56200 61.84100  44.86800  1.000 85.78861  ? 1103 VAL   B CA  1 
ATOM   6548 C C   . VAL   B 1 491 ? -21.38100 60.89000  45.02800  1.000 85.98701  ? 1103 VAL   B C   1 
ATOM   6549 O O   . VAL   B 1 491 ? -20.74700 60.84600  46.08900  1.000 92.20750  ? 1103 VAL   B O   1 
ATOM   6550 C CB  . VAL   B 1 491 ? -23.88400 61.20100  45.33700  1.000 85.48237  ? 1103 VAL   B CB  1 
ATOM   6551 C CG1 . VAL   B 1 491 ? -23.77300 60.70400  46.77100  1.000 87.13289  ? 1103 VAL   B CG1 1 
ATOM   6552 C CG2 . VAL   B 1 491 ? -25.01500 62.20100  45.21200  1.000 80.68221  ? 1103 VAL   B CG2 1 
ATOM   6553 N N   . PHE   B 1 492 ? -21.05600 60.12600  43.98400  1.000 81.74884  ? 1104 PHE   B N   1 
ATOM   6554 C CA  . PHE   B 1 492 ? -19.88900 59.25000  44.03500  1.000 82.32573  ? 1104 PHE   B CA  1 
ATOM   6555 C C   . PHE   B 1 492 ? -18.59700 60.05900  44.05000  1.000 81.58700  ? 1104 PHE   B C   1 
ATOM   6556 O O   . PHE   B 1 492 ? -17.71500 59.83000  44.88600  1.000 75.09491  ? 1104 PHE   B O   1 
ATOM   6557 C CB  . PHE   B 1 492 ? -19.91100 58.29800  42.84000  1.000 77.93041  ? 1104 PHE   B CB  1 
ATOM   6558 C CG  . PHE   B 1 492 ? -18.87000 57.21400  42.89600  1.000 77.40661  ? 1104 PHE   B CG  1 
ATOM   6559 C CD1 . PHE   B 1 492 ? -17.60900 57.41800  42.35100  1.000 73.90164  ? 1104 PHE   B CD1 1 
ATOM   6560 C CD2 . PHE   B 1 492 ? -19.16800 55.97500  43.44000  1.000 73.79054  ? 1104 PHE   B CD2 1 
ATOM   6561 C CE1 . PHE   B 1 492 ? -16.65400 56.42100  42.38400  1.000 71.29664  ? 1104 PHE   B CE1 1 
ATOM   6562 C CE2 . PHE   B 1 492 ? -18.21700 54.97300  43.47400  1.000 75.17852  ? 1104 PHE   B CE2 1 
ATOM   6563 C CZ  . PHE   B 1 492 ? -16.95900 55.19600  42.94600  1.000 72.45253  ? 1104 PHE   B CZ  1 
ATOM   6564 N N   . GLN   B 1 493 ? -18.47200 61.00900  43.12000  1.000 86.64802  ? 1105 GLN   B N   1 
ATOM   6565 C CA  . GLN   B 1 493 ? -17.25800 61.80400  42.98400  1.000 87.99417  ? 1105 GLN   B CA  1 
ATOM   6566 C C   . GLN   B 1 493 ? -17.07900 62.78500  44.13700  1.000 91.88544  ? 1105 GLN   B C   1 
ATOM   6567 O O   . GLN   B 1 493 ? -15.96100 63.26200  44.36300  1.000 92.56094  ? 1105 GLN   B O   1 
ATOM   6568 C CB  . GLN   B 1 493 ? -17.29200 62.54100  41.63800  1.000 82.85672  ? 1105 GLN   B CB  1 
ATOM   6569 C CG  . GLN   B 1 493 ? -16.20500 63.57800  41.41400  1.000 81.49675  ? 1105 GLN   B CG  1 
ATOM   6570 C CD  . GLN   B 1 493 ? -16.46500 64.43500  40.19000  1.000 82.57552  ? 1105 GLN   B CD  1 
ATOM   6571 O OE1 . GLN   B 1 493 ? -17.49300 64.29700  39.52500  1.000 75.07555  ? 1105 GLN   B OE1 1 
ATOM   6572 N NE2 . GLN   B 1 493 ? -15.52700 65.32500  39.88300  1.000 84.53248  ? 1105 GLN   B NE2 1 
ATOM   6573 N N   . MET   B 1 494 ? -18.13300 63.06200  44.89300  1.000 92.13647  ? 1106 MET   B N   1 
ATOM   6574 C CA  . MET   B 1 494 ? -18.09300 64.16100  45.85400  1.000 94.70747  ? 1106 MET   B CA  1 
ATOM   6575 C C   . MET   B 1 494 ? -18.63700 63.80500  47.22800  1.000 93.81441  ? 1106 MET   B C   1 
ATOM   6576 O O   . MET   B 1 494 ? -18.08300 64.25600  48.23400  1.000 96.35956  ? 1106 MET   B O   1 
ATOM   6577 C CB  . MET   B 1 494 ? -18.86900 65.34300  45.27200  1.000 97.78177  ? 1106 MET   B CB  1 
ATOM   6578 C CG  . MET   B 1 494 ? -18.09600 66.09100  44.21600  1.000 96.94878  ? 1106 MET   B CG  1 
ATOM   6579 S SD  . MET   B 1 494 ? -19.07900 67.33200  43.37900  1.000 93.86010  ? 1106 MET   B SD  1 
ATOM   6580 C CE  . MET   B 1 494 ? -17.74700 68.33700  42.75700  1.000 87.96054  ? 1106 MET   B CE  1 
ATOM   6581 N N   . GLY   B 1 495 ? -19.69600 63.01900  47.30000  1.000 92.33424  ? 1107 GLY   B N   1 
ATOM   6582 C CA  . GLY   B 1 495 ? -20.40400 62.82700  48.54600  1.000 91.08808  ? 1107 GLY   B CA  1 
ATOM   6583 C C   . GLY   B 1 495 ? -21.68200 63.64300  48.58500  1.000 94.81894  ? 1107 GLY   B C   1 
ATOM   6584 O O   . GLY   B 1 495 ? -21.81000 64.68700  47.93600  1.000 92.05801  ? 1107 GLY   B O   1 
ATOM   6585 N N   . GLU   B 1 496 ? -22.65100 63.16100  49.36900  1.000 96.82123  ? 1108 GLU   B N   1 
ATOM   6586 C CA  . GLU   B 1 496 ? -23.95100 63.81900  49.45000  1.000 90.00127  ? 1108 GLU   B CA  1 
ATOM   6587 C C   . GLU   B 1 496 ? -23.87100 65.18900  50.11300  1.000 89.59859  ? 1108 GLU   B C   1 
ATOM   6588 O O   . GLU   B 1 496 ? -24.75400 66.02500  49.88800  1.000 89.30173  ? 1108 GLU   B O   1 
ATOM   6589 C CB  . GLU   B 1 496 ? -24.94300 62.90600  50.17800  1.000 83.06075  ? 1108 GLU   B CB  1 
ATOM   6590 C CG  . GLU   B 1 496 ? -24.38200 62.18100  51.40200  1.000 92.66386  ? 1108 GLU   B CG  1 
ATOM   6591 C CD  . GLU   B 1 496 ? -24.29300 63.04600  52.65400  1.000 102.42520 ? 1108 GLU   B CD  1 
ATOM   6592 O OE1 . GLU   B 1 496 ? -24.69400 64.22800  52.62100  1.000 105.73292 ? 1108 GLU   B OE1 1 
ATOM   6593 O OE2 . GLU   B 1 496 ? -23.80400 62.53600  53.68400  1.000 96.84444  ? 1108 GLU   B OE2 1 
ATOM   6594 N N   . THR   B 1 497 ? -22.83700 65.43800  50.92100  1.000 90.73183  ? 1109 THR   B N   1 
ATOM   6595 C CA  . THR   B 1 497 ? -22.69600 66.74400  51.55700  1.000 93.59809  ? 1109 THR   B CA  1 
ATOM   6596 C C   . THR   B 1 497 ? -22.41100 67.82800  50.52700  1.000 91.47016  ? 1109 THR   B C   1 
ATOM   6597 O O   . THR   B 1 497 ? -23.00300 68.91300  50.58000  1.000 94.74114  ? 1109 THR   B O   1 
ATOM   6598 C CB  . THR   B 1 497 ? -21.59000 66.69700  52.61100  1.000 101.09480 ? 1109 THR   B CB  1 
ATOM   6599 O OG1 . THR   B 1 497 ? -21.96400 65.79800  53.66300  1.000 97.58464  ? 1109 THR   B OG1 1 
ATOM   6600 C CG2 . THR   B 1 497 ? -21.34900 68.08400  53.19600  1.000 98.00910  ? 1109 THR   B CG2 1 
ATOM   6601 N N   . GLY   B 1 498 ? -21.51200 67.55100  49.57800  1.000 91.08022  ? 1110 GLY   B N   1 
ATOM   6602 C CA  . GLY   B 1 498 ? -21.23900 68.50800  48.52100  1.000 90.66641  ? 1110 GLY   B CA  1 
ATOM   6603 C C   . GLY   B 1 498 ? -22.32200 68.57700  47.46600  1.000 91.64214  ? 1110 GLY   B C   1 
ATOM   6604 O O   . GLY   B 1 498 ? -22.50600 69.62300  46.83600  1.000 96.05822  ? 1110 GLY   B O   1 
ATOM   6605 N N   . VAL   B 1 499 ? -23.05200 67.47900  47.25400  1.000 89.22567  ? 1111 VAL   B N   1 
ATOM   6606 C CA  . VAL   B 1 499 ? -24.14300 67.49200  46.28400  1.000 91.37470  ? 1111 VAL   B CA  1 
ATOM   6607 C C   . VAL   B 1 499 ? -25.32800 68.28300  46.82400  1.000 91.60701  ? 1111 VAL   B C   1 
ATOM   6608 O O   . VAL   B 1 499 ? -26.09300 68.87500  46.05300  1.000 91.14111  ? 1111 VAL   B O   1 
ATOM   6609 C CB  . VAL   B 1 499 ? -24.52800 66.04900  45.90200  1.000 94.17342  ? 1111 VAL   B CB  1 
ATOM   6610 C CG1 . VAL   B 1 499 ? -25.75800 66.02400  45.00100  1.000 89.85650  ? 1111 VAL   B CG1 1 
ATOM   6611 C CG2 . VAL   B 1 499 ? -23.35900 65.36800  45.20900  1.000 94.09313  ? 1111 VAL   B CG2 1 
ATOM   6612 N N   . ALA   B 1 500 ? -25.48900 68.33500  48.14600  1.000 94.41359  ? 1112 ALA   B N   1 
ATOM   6613 C CA  . ALA   B 1 500 ? -26.45700 69.24400  48.74800  1.000 91.64689  ? 1112 ALA   B CA  1 
ATOM   6614 C C   . ALA   B 1 500 ? -26.06300 70.71000  48.59600  1.000 94.30329  ? 1112 ALA   B C   1 
ATOM   6615 O O   . ALA   B 1 500 ? -26.83600 71.58400  49.00300  1.000 93.85087  ? 1112 ALA   B O   1 
ATOM   6616 C CB  . ALA   B 1 500 ? -26.63700 68.90700  50.23000  1.000 84.39355  ? 1112 ALA   B CB  1 
ATOM   6617 N N   . GLY   B 1 501 ? -24.89700 70.99500  48.01600  1.000 92.43229  ? 1113 GLY   B N   1 
ATOM   6618 C CA  . GLY   B 1 501 ? -24.38800 72.34800  47.89000  1.000 88.40217  ? 1113 GLY   B CA  1 
ATOM   6619 C C   . GLY   B 1 501 ? -25.23200 73.28200  47.04600  1.000 96.39496  ? 1113 GLY   B C   1 
ATOM   6620 O O   . GLY   B 1 501 ? -25.82200 74.23000  47.57300  1.000 104.81827 ? 1113 GLY   B O   1 
ATOM   6621 N N   . PHE   B 1 502 ? -25.29500 73.04100  45.73600  1.000 91.99754  ? 1114 PHE   B N   1 
ATOM   6622 C CA  . PHE   B 1 502 ? -26.05800 73.91000  44.83900  1.000 95.67347  ? 1114 PHE   B CA  1 
ATOM   6623 C C   . PHE   B 1 502 ? -27.52300 73.48000  44.84300  1.000 95.84309  ? 1114 PHE   B C   1 
ATOM   6624 O O   . PHE   B 1 502 ? -28.01300 72.80300  43.93700  1.000 95.24224  ? 1114 PHE   B O   1 
ATOM   6625 C CB  . PHE   B 1 502 ? -25.47200 73.89200  43.43300  1.000 96.81581  ? 1114 PHE   B CB  1 
ATOM   6626 C CG  . PHE   B 1 502 ? -24.69900 75.13100  43.08600  1.000 96.32387  ? 1114 PHE   B CG  1 
ATOM   6627 C CD1 . PHE   B 1 502 ? -25.28900 76.38100  43.19600  1.000 94.71206  ? 1114 PHE   B CD1 1 
ATOM   6628 C CD2 . PHE   B 1 502 ? -23.39000 75.04700  42.63600  1.000 99.29461  ? 1114 PHE   B CD2 1 
ATOM   6629 C CE1 . PHE   B 1 502 ? -24.58300 77.52700  42.87700  1.000 98.77419  ? 1114 PHE   B CE1 1 
ATOM   6630 C CE2 . PHE   B 1 502 ? -22.67900 76.18900  42.31300  1.000 97.18204  ? 1114 PHE   B CE2 1 
ATOM   6631 C CZ  . PHE   B 1 502 ? -23.27700 77.43200  42.43400  1.000 96.50194  ? 1114 PHE   B CZ  1 
ATOM   6632 N N   . THR   B 1 503 ? -28.23400 73.89600  45.89600  1.000 95.52427  ? 1115 THR   B N   1 
ATOM   6633 C CA  . THR   B 1 503 ? -29.68700 73.75600  45.91000  1.000 95.35954  ? 1115 THR   B CA  1 
ATOM   6634 C C   . THR   B 1 503 ? -30.31600 74.41200  44.69100  1.000 90.71914  ? 1115 THR   B C   1 
ATOM   6635 O O   . THR   B 1 503 ? -31.34100 73.93800  44.18700  1.000 88.44518  ? 1115 THR   B O   1 
ATOM   6636 C CB  . THR   B 1 503 ? -30.26700 74.37400  47.18500  1.000 88.12425  ? 1115 THR   B CB  1 
ATOM   6637 O OG1 . THR   B 1 503 ? -29.60700 75.61500  47.46200  1.000 90.72048  ? 1115 THR   B OG1 1 
ATOM   6638 C CG2 . THR   B 1 503 ? -30.09300 73.44100  48.36100  1.000 78.70492  ? 1115 THR   B CG2 1 
ATOM   6639 N N   . ASN   B 1 504 ? -29.71700 75.50600  44.21500  1.000 88.66722  ? 1116 ASN   B N   1 
ATOM   6640 C CA  . ASN   B 1 504 ? -30.19500 76.17300  43.01100  1.000 92.73422  ? 1116 ASN   B CA  1 
ATOM   6641 C C   . ASN   B 1 504 ? -30.30000 75.19200  41.85000  1.000 93.74014  ? 1116 ASN   B C   1 
ATOM   6642 O O   . ASN   B 1 504 ? -31.35800 75.05900  41.22300  1.000 93.25588  ? 1116 ASN   B O   1 
ATOM   6643 C CB  . ASN   B 1 504 ? -29.25700 77.33000  42.66000  1.000 97.75761  ? 1116 ASN   B CB  1 
ATOM   6644 C CG  . ASN   B 1 504 ? -29.55700 78.59200  43.45400  1.000 98.34085  ? 1116 ASN   B CG  1 
ATOM   6645 O OD1 . ASN   B 1 504 ? -30.71400 78.90500  43.73400  1.000 92.91213  ? 1116 ASN   B OD1 1 
ATOM   6646 N ND2 . ASN   B 1 504 ? -28.50800 79.31900  43.82600  1.000 101.45976 ? 1116 ASN   B ND2 1 
ATOM   6647 N N   . SER   B 1 505 ? -29.20600 74.48700  41.55600  1.000 93.03997  ? 1117 SER   B N   1 
ATOM   6648 C CA  . SER   B 1 505 ? -29.24500 73.45800  40.52300  1.000 88.23715  ? 1117 SER   B CA  1 
ATOM   6649 C C   . SER   B 1 505 ? -30.04400 72.24300  40.98100  1.000 86.69637  ? 1117 SER   B C   1 
ATOM   6650 O O   . SER   B 1 505 ? -30.73600 71.61100  40.17400  1.000 83.36514  ? 1117 SER   B O   1 
ATOM   6651 C CB  . SER   B 1 505 ? -27.82300 73.05200  40.13600  1.000 87.07182  ? 1117 SER   B CB  1 
ATOM   6652 O OG  . SER   B 1 505 ? -26.96400 74.17900  40.09800  1.000 88.67923  ? 1117 SER   B OG  1 
ATOM   6653 N N   . LEU   B 1 506 ? -29.96300 71.90300  42.27300  1.000 89.74708  ? 1118 LEU   B N   1 
ATOM   6654 C CA  . LEU   B 1 506 ? -30.66900 70.72900  42.78300  1.000 88.34813  ? 1118 LEU   B CA  1 
ATOM   6655 C C   . LEU   B 1 506 ? -32.17800 70.86500  42.61700  1.000 89.60008  ? 1118 LEU   B C   1 
ATOM   6656 O O   . LEU   B 1 506 ? -32.86600 69.88400  42.31300  1.000 84.54790  ? 1118 LEU   B O   1 
ATOM   6657 C CB  . LEU   B 1 506 ? -30.30900 70.49600  44.25100  1.000 84.05251  ? 1118 LEU   B CB  1 
ATOM   6658 C CG  . LEU   B 1 506 ? -29.31400 69.36300  44.49800  1.000 90.72902  ? 1118 LEU   B CG  1 
ATOM   6659 C CD1 . LEU   B 1 506 ? -29.89000 68.04500  44.02000  1.000 90.22126  ? 1118 LEU   B CD1 1 
ATOM   6660 C CD2 . LEU   B 1 506 ? -28.02000 69.65200  43.76800  1.000 92.45518  ? 1118 LEU   B CD2 1 
ATOM   6661 N N   . ARG   B 1 507 ? -32.71400 72.06800  42.81600  1.000 90.18722  ? 1119 ARG   B N   1 
ATOM   6662 C CA  . ARG   B 1 507 ? -34.14000 72.28100  42.62200  1.000 84.66116  ? 1119 ARG   B CA  1 
ATOM   6663 C C   . ARG   B 1 507 ? -34.49200 72.60200  41.17800  1.000 89.03190  ? 1119 ARG   B C   1 
ATOM   6664 O O   . ARG   B 1 507 ? -35.64400 72.39700  40.77700  1.000 86.48089  ? 1119 ARG   B O   1 
ATOM   6665 C CB  . ARG   B 1 507 ? -34.64500 73.39200  43.54800  1.000 88.71603  ? 1119 ARG   B CB  1 
ATOM   6666 C CG  . ARG   B 1 507 ? -34.66000 74.79000  42.95200  1.000 96.32080  ? 1119 ARG   B CG  1 
ATOM   6667 C CD  . ARG   B 1 507 ? -35.37900 75.74800  43.89400  1.000 102.42720 ? 1119 ARG   B CD  1 
ATOM   6668 N NE  . ARG   B 1 507 ? -35.80100 76.97900  43.23700  1.000 108.82739 ? 1119 ARG   B NE  1 
ATOM   6669 C CZ  . ARG   B 1 507 ? -35.13000 78.12200  43.28700  1.000 105.22048 ? 1119 ARG   B CZ  1 
ATOM   6670 N NH1 . ARG   B 1 507 ? -33.98800 78.22600  43.94900  1.000 99.53139  ? 1119 ARG   B NH1 1 
ATOM   6671 N NH2 . ARG   B 1 507 ? -35.61800 79.18900  42.65900  1.000 95.14415  ? 1119 ARG   B NH2 1 
ATOM   6672 N N   . MET   B 1 508 ? -33.53100 73.08800  40.38600  1.000 91.13654  ? 1120 MET   B N   1 
ATOM   6673 C CA  . MET   B 1 508 ? -33.77200 73.24100  38.95500  1.000 88.24193  ? 1120 MET   B CA  1 
ATOM   6674 C C   . MET   B 1 508 ? -33.96900 71.88600  38.28600  1.000 84.78361  ? 1120 MET   B C   1 
ATOM   6675 O O   . MET   B 1 508 ? -34.81100 71.74700  37.39100  1.000 82.68557  ? 1120 MET   B O   1 
ATOM   6676 C CB  . MET   B 1 508 ? -32.62100 74.00300  38.29700  1.000 81.39616  ? 1120 MET   B CB  1 
ATOM   6677 C CG  . MET   B 1 508 ? -32.78200 75.51400  38.31800  1.000 86.13359  ? 1120 MET   B CG  1 
ATOM   6678 S SD  . MET   B 1 508 ? -31.49100 76.37700  37.39800  1.000 94.66411  ? 1120 MET   B SD  1 
ATOM   6679 C CE  . MET   B 1 508 ? -30.17000 76.42000  38.60200  1.000 81.33437  ? 1120 MET   B CE  1 
ATOM   6680 N N   . LEU   B 1 509 ? -33.20700 70.87600  38.71300  1.000 80.79234  ? 1121 LEU   B N   1 
ATOM   6681 C CA  . LEU   B 1 509 ? -33.39600 69.52900  38.18200  1.000 79.10272  ? 1121 LEU   B CA  1 
ATOM   6682 C C   . LEU   B 1 509 ? -34.76100 68.97500  38.57000  1.000 82.97981  ? 1121 LEU   B C   1 
ATOM   6683 O O   . LEU   B 1 509 ? -35.45100 68.36400  37.74300  1.000 80.64582  ? 1121 LEU   B O   1 
ATOM   6684 C CB  . LEU   B 1 509 ? -32.27900 68.60900  38.67900  1.000 77.67698  ? 1121 LEU   B CB  1 
ATOM   6685 C CG  . LEU   B 1 509 ? -30.88200 68.86500  38.10600  1.000 79.40992  ? 1121 LEU   B CG  1 
ATOM   6686 C CD1 . LEU   B 1 509 ? -29.79300 68.31000  39.01500  1.000 64.18166  ? 1121 LEU   B CD1 1 
ATOM   6687 C CD2 . LEU   B 1 509 ? -30.77100 68.27500  36.70900  1.000 85.00959  ? 1121 LEU   B CD2 1 
ATOM   6688 N N   . GLN   B 1 510 ? -35.16700 69.17800  39.82700  1.000 86.82927  ? 1122 GLN   B N   1 
ATOM   6689 C CA  . GLN   B 1 510 ? -36.47900 68.71900  40.27400  1.000 82.53564  ? 1122 GLN   B CA  1 
ATOM   6690 C C   . GLN   B 1 510 ? -37.59800 69.40300  39.50100  1.000 85.21616  ? 1122 GLN   B C   1 
ATOM   6691 O O   . GLN   B 1 510 ? -38.59300 68.76600  39.13600  1.000 85.20772  ? 1122 GLN   B O   1 
ATOM   6692 C CB  . GLN   B 1 510 ? -36.64000 68.97400  41.77100  1.000 87.83905  ? 1122 GLN   B CB  1 
ATOM   6693 C CG  . GLN   B 1 510 ? -37.64600 68.06500  42.45000  1.000 87.86232  ? 1122 GLN   B CG  1 
ATOM   6694 C CD  . GLN   B 1 510 ? -37.78800 68.36100  43.92900  1.000 88.56349  ? 1122 GLN   B CD  1 
ATOM   6695 O OE1 . GLN   B 1 510 ? -36.95000 69.04400  44.52000  1.000 94.43746  ? 1122 GLN   B OE1 1 
ATOM   6696 N NE2 . GLN   B 1 510 ? -38.85300 67.84900  44.53600  1.000 88.37882  ? 1122 GLN   B NE2 1 
ATOM   6697 N N   . GLN   B 1 511 ? -37.45000 70.70200  39.23700  1.000 84.80067  ? 1123 GLN   B N   1 
ATOM   6698 C CA  . GLN   B 1 511 ? -38.45600 71.45600  38.49900  1.000 83.22163  ? 1123 GLN   B CA  1 
ATOM   6699 C C   . GLN   B 1 511 ? -38.51600 71.07900  37.02300  1.000 79.98949  ? 1123 GLN   B C   1 
ATOM   6700 O O   . GLN   B 1 511 ? -39.31600 71.67000  36.28900  1.000 77.71146  ? 1123 GLN   B O   1 
ATOM   6701 C CB  . GLN   B 1 511 ? -38.18300 72.95400  38.64300  1.000 85.15920  ? 1123 GLN   B CB  1 
ATOM   6702 C CG  . GLN   B 1 511 ? -38.55200 73.54000  40.00300  1.000 91.24668  ? 1123 GLN   B CG  1 
ATOM   6703 C CD  . GLN   B 1 511 ? -37.74700 74.78600  40.34000  1.000 92.57158  ? 1123 GLN   B CD  1 
ATOM   6704 O OE1 . GLN   B 1 511 ? -36.70100 75.04100  39.74400  1.000 99.52540  ? 1123 GLN   B OE1 1 
ATOM   6705 N NE2 . GLN   B 1 511 ? -38.23100 75.56400  41.30400  1.000 80.99484  ? 1123 GLN   B NE2 1 
ATOM   6706 N N   . LYS   B 1 512 ? -37.69100 70.12500  36.58200  1.000 79.84272  ? 1124 LYS   B N   1 
ATOM   6707 C CA  . LYS   B 1 512 ? -37.64200 69.67000  35.19000  1.000 76.28318  ? 1124 LYS   B CA  1 
ATOM   6708 C C   . LYS   B 1 512 ? -37.22800 70.79400  34.24100  1.000 75.23398  ? 1124 LYS   B C   1 
ATOM   6709 O O   . LYS   B 1 512 ? -37.59600 70.80100  33.06400  1.000 71.14262  ? 1124 LYS   B O   1 
ATOM   6710 C CB  . LYS   B 1 512 ? -38.97600 69.04200  34.76500  1.000 70.23928  ? 1124 LYS   B CB  1 
ATOM   6711 C CG  . LYS   B 1 512 ? -39.22700 67.68700  35.42500  1.000 71.16708  ? 1124 LYS   B CG  1 
ATOM   6712 C CD  . LYS   B 1 512 ? -40.69400 67.28300  35.41500  1.000 69.94731  ? 1124 LYS   B CD  1 
ATOM   6713 C CE  . LYS   B 1 512 ? -41.19000 66.97700  34.01500  1.000 65.68554  ? 1124 LYS   B CE  1 
ATOM   6714 N NZ  . LYS   B 1 512 ? -42.54400 66.35900  34.05200  1.000 57.07809  ? 1124 LYS   B NZ  1 
ATOM   6715 N N   . ARG   B 1 513 ? -36.45000 71.74700  34.75400  1.000 77.96948  ? 1125 ARG   B N   1 
ATOM   6716 C CA  . ARG   B 1 513 ? -35.88300 72.82700  33.94800  1.000 74.37452  ? 1125 ARG   B CA  1 
ATOM   6717 C C   . ARG   B 1 513 ? -34.43700 72.47500  33.60200  1.000 80.70094  ? 1125 ARG   B C   1 
ATOM   6718 O O   . ARG   B 1 513 ? -33.47400 73.01400  34.15200  1.000 78.50231  ? 1125 ARG   B O   1 
ATOM   6719 C CB  . ARG   B 1 513 ? -35.97700 74.15400  34.69800  1.000 82.73122  ? 1125 ARG   B CB  1 
ATOM   6720 C CG  . ARG   B 1 513 ? -37.35100 74.44100  35.29100  1.000 88.75722  ? 1125 ARG   B CG  1 
ATOM   6721 C CD  . ARG   B 1 513 ? -37.27400 75.45200  36.43300  1.000 89.35720  ? 1125 ARG   B CD  1 
ATOM   6722 N NE  . ARG   B 1 513 ? -37.05200 76.81200  35.96000  1.000 93.04278  ? 1125 ARG   B NE  1 
ATOM   6723 C CZ  . ARG   B 1 513 ? -38.02000 77.67800  35.69400  1.000 90.76871  ? 1125 ARG   B CZ  1 
ATOM   6724 N NH1 . ARG   B 1 513 ? -39.29400 77.36800  35.87400  1.000 84.36633  ? 1125 ARG   B NH1 1 
ATOM   6725 N NH2 . ARG   B 1 513 ? -37.70100 78.88600  35.23600  1.000 87.91197  ? 1125 ARG   B NH2 1 
ATOM   6726 N N   . TRP   B 1 514 ? -34.30900 71.53800  32.66000  1.000 86.25030  ? 1126 TRP   B N   1 
ATOM   6727 C CA  . TRP   B 1 514 ? -33.01300 70.92800  32.37400  1.000 79.30391  ? 1126 TRP   B CA  1 
ATOM   6728 C C   . TRP   B 1 514 ? -32.02500 71.94600  31.82400  1.000 82.37772  ? 1126 TRP   B C   1 
ATOM   6729 O O   . TRP   B 1 514 ? -30.91100 72.08700  32.34400  1.000 82.86984  ? 1126 TRP   B O   1 
ATOM   6730 C CB  . TRP   B 1 514 ? -33.18900 69.77000  31.39400  1.000 73.13410  ? 1126 TRP   B CB  1 
ATOM   6731 C CG  . TRP   B 1 514 ? -34.29300 68.84700  31.77800  1.000 74.60882  ? 1126 TRP   B CG  1 
ATOM   6732 C CD1 . TRP   B 1 514 ? -35.43800 68.60200  31.07700  1.000 75.61547  ? 1126 TRP   B CD1 1 
ATOM   6733 C CD2 . TRP   B 1 514 ? -34.37300 68.05900  32.96900  1.000 72.92156  ? 1126 TRP   B CD2 1 
ATOM   6734 N NE1 . TRP   B 1 514 ? -36.22100 67.69800  31.75400  1.000 75.67146  ? 1126 TRP   B NE1 1 
ATOM   6735 C CE2 . TRP   B 1 514 ? -35.58900 67.35000  32.91900  1.000 70.47560  ? 1126 TRP   B CE2 1 
ATOM   6736 C CE3 . TRP   B 1 514 ? -33.52900 67.87700  34.07000  1.000 74.92234  ? 1126 TRP   B CE3 1 
ATOM   6737 C CZ2 . TRP   B 1 514 ? -35.98400 66.47400  33.92800  1.000 72.27495  ? 1126 TRP   B CZ2 1 
ATOM   6738 C CZ3 . TRP   B 1 514 ? -33.92300 67.00800  35.07100  1.000 73.08224  ? 1126 TRP   B CZ3 1 
ATOM   6739 C CH2 . TRP   B 1 514 ? -35.14000 66.31900  34.99500  1.000 72.58891  ? 1126 TRP   B CH2 1 
ATOM   6740 N N   . ASP   B 1 515 ? -32.41100 72.66000  30.76100  1.000 79.09639  ? 1127 ASP   B N   1 
ATOM   6741 C CA  . ASP   B 1 515 ? -31.50900 73.64100  30.16700  1.000 83.35972  ? 1127 ASP   B CA  1 
ATOM   6742 C C   . ASP   B 1 515 ? -31.05800 74.68200  31.18000  1.000 86.99523  ? 1127 ASP   B C   1 
ATOM   6743 O O   . ASP   B 1 515 ? -29.91000 75.13400  31.12800  1.000 86.85341  ? 1127 ASP   B O   1 
ATOM   6744 C CB  . ASP   B 1 515 ? -32.17600 74.31900  28.97100  1.000 87.89225  ? 1127 ASP   B CB  1 
ATOM   6745 C CG  . ASP   B 1 515 ? -32.11200 73.47700  27.71300  1.000 89.06463  ? 1127 ASP   B CG  1 
ATOM   6746 O OD1 . ASP   B 1 515 ? -31.20300 72.62700  27.61700  1.000 83.68186  ? 1127 ASP   B OD1 1 
ATOM   6747 O OD2 . ASP   B 1 515 ? -32.96400 73.66500  26.81900  1.000 94.03803  ? 1127 ASP   B OD2 1 
ATOM   6748 N N   . GLU   B 1 516 ? -31.93200 75.05700  32.11500  1.000 85.72073  ? 1128 GLU   B N   1 
ATOM   6749 C CA  . GLU   B 1 516 ? -31.53600 75.99700  33.15800  1.000 80.80935  ? 1128 GLU   B CA  1 
ATOM   6750 C C   . GLU   B 1 516 ? -30.53100 75.36400  34.11200  1.000 81.28600  ? 1128 GLU   B C   1 
ATOM   6751 O O   . GLU   B 1 516 ? -29.51500 75.97800  34.45900  1.000 84.83768  ? 1128 GLU   B O   1 
ATOM   6752 C CB  . GLU   B 1 516 ? -32.76700 76.47800  33.92400  1.000 82.43233  ? 1128 GLU   B CB  1 
ATOM   6753 C CG  . GLU   B 1 516 ? -33.81900 77.14200  33.05700  1.000 88.15008  ? 1128 GLU   B CG  1 
ATOM   6754 C CD  . GLU   B 1 516 ? -34.97700 77.68300  33.87100  1.000 92.38216  ? 1128 GLU   B CD  1 
ATOM   6755 O OE1 . GLU   B 1 516 ? -34.91300 77.60900  35.11800  1.000 93.12926  ? 1128 GLU   B OE1 1 
ATOM   6756 O OE2 . GLU   B 1 516 ? -35.96300 78.15900  33.26500  1.000 87.91519  ? 1128 GLU   B OE2 1 
ATOM   6757 N N   . ALA   B 1 517 ? -30.80100 74.13000  34.55000  1.000 81.20243  ? 1129 ALA   B N   1 
ATOM   6758 C CA  . ALA   B 1 517 ? -29.90900 73.46500  35.49500  1.000 85.24778  ? 1129 ALA   B CA  1 
ATOM   6759 C C   . ALA   B 1 517 ? -28.54000 73.19700  34.88400  1.000 91.80734  ? 1129 ALA   B C   1 
ATOM   6760 O O   . ALA   B 1 517 ? -27.54500 73.09500  35.61100  1.000 88.56223  ? 1129 ALA   B O   1 
ATOM   6761 C CB  . ALA   B 1 517 ? -30.53700 72.15800  35.97900  1.000 81.23381  ? 1129 ALA   B CB  1 
ATOM   6762 N N   . ALA   B 1 518 ? -28.46900 73.08800  33.55700  1.000 92.77433  ? 1130 ALA   B N   1 
ATOM   6763 C CA  . ALA   B 1 518 ? -27.21100 72.79700  32.88500  1.000 88.88807  ? 1130 ALA   B CA  1 
ATOM   6764 C C   . ALA   B 1 518 ? -26.29600 74.01200  32.77700  1.000 87.60534  ? 1130 ALA   B C   1 
ATOM   6765 O O   . ALA   B 1 518 ? -25.07900 73.84000  32.64300  1.000 86.17292  ? 1130 ALA   B O   1 
ATOM   6766 C CB  . ALA   B 1 518 ? -27.48600 72.22900  31.49200  1.000 87.35497  ? 1130 ALA   B CB  1 
ATOM   6767 N N   . VAL   B 1 519 ? -26.84400 75.22900  32.83100  1.000 88.02075  ? 1131 VAL   B N   1 
ATOM   6768 C CA  . VAL   B 1 519 ? -25.99800 76.41900  32.77900  1.000 87.62709  ? 1131 VAL   B CA  1 
ATOM   6769 C C   . VAL   B 1 519 ? -25.43700 76.75900  34.15800  1.000 87.64867  ? 1131 VAL   B C   1 
ATOM   6770 O O   . VAL   B 1 519 ? -24.33200 77.30500  34.26200  1.000 86.44135  ? 1131 VAL   B O   1 
ATOM   6771 C CB  . VAL   B 1 519 ? -26.76800 77.61000  32.17900  1.000 79.72524  ? 1131 VAL   B CB  1 
ATOM   6772 C CG1 . VAL   B 1 519 ? -25.80300 78.69500  31.72500  1.000 77.28942  ? 1131 VAL   B CG1 1 
ATOM   6773 C CG2 . VAL   B 1 519 ? -27.61200 77.16000  31.00700  1.000 78.56522  ? 1131 VAL   B CG2 1 
ATOM   6774 N N   . ASN   B 1 520 ? -26.16700 76.44400  35.23300  1.000 87.12728  ? 1132 ASN   B N   1 
ATOM   6775 C CA  . ASN   B 1 520 ? -25.65400 76.71700  36.57300  1.000 94.05812  ? 1132 ASN   B CA  1 
ATOM   6776 C C   . ASN   B 1 520 ? -24.56000 75.73100  36.96400  1.000 95.30436  ? 1132 ASN   B C   1 
ATOM   6777 O O   . ASN   B 1 520 ? -23.59200 76.10500  37.63600  1.000 97.23533  ? 1132 ASN   B O   1 
ATOM   6778 C CB  . ASN   B 1 520 ? -26.78500 76.67300  37.59800  1.000 93.24354  ? 1132 ASN   B CB  1 
ATOM   6779 C CG  . ASN   B 1 520 ? -26.37700 77.25600  38.93900  1.000 97.67332  ? 1132 ASN   B CG  1 
ATOM   6780 O OD1 . ASN   B 1 520 ? -25.77100 78.32600  39.00600  1.000 99.55173  ? 1132 ASN   B OD1 1 
ATOM   6781 N ND2 . ASN   B 1 520 ? -26.69600 76.54600  40.01600  1.000 96.88734  ? 1132 ASN   B ND2 1 
ATOM   6782 N N   . LEU   B 1 521 ? -24.70500 74.46500  36.56600  1.000 92.56971  ? 1133 LEU   B N   1 
ATOM   6783 C CA  . LEU   B 1 521 ? -23.72600 73.45700  36.95600  1.000 88.82523  ? 1133 LEU   B CA  1 
ATOM   6784 C C   . LEU   B 1 521 ? -22.36400 73.72200  36.32600  1.000 91.20610  ? 1133 LEU   B C   1 
ATOM   6785 O O   . LEU   B 1 521 ? -21.33200 73.41600  36.93400  1.000 95.94111  ? 1133 LEU   B O   1 
ATOM   6786 C CB  . LEU   B 1 521 ? -24.23700 72.06700  36.57700  1.000 84.94171  ? 1133 LEU   B CB  1 
ATOM   6787 C CG  . LEU   B 1 521 ? -25.29400 71.49600  37.52400  1.000 79.91935  ? 1133 LEU   B CG  1 
ATOM   6788 C CD1 . LEU   B 1 521 ? -25.88400 70.19800  36.98500  1.000 77.05505  ? 1133 LEU   B CD1 1 
ATOM   6789 C CD2 . LEU   B 1 521 ? -24.70300 71.29100  38.90800  1.000 77.06669  ? 1133 LEU   B CD2 1 
ATOM   6790 N N   . ALA   B 1 522 ? -22.34100 74.30400  35.12600  1.000 92.87199  ? 1134 ALA   B N   1 
ATOM   6791 C CA  . ALA   B 1 522 ? -21.09500 74.58800  34.42500  1.000 92.59969  ? 1134 ALA   B CA  1 
ATOM   6792 C C   . ALA   B 1 522 ? -20.36600 75.81100  34.96800  1.000 90.75680  ? 1134 ALA   B C   1 
ATOM   6793 O O   . ALA   B 1 522 ? -19.30900 76.16700  34.43800  1.000 88.81759  ? 1134 ALA   B O   1 
ATOM   6794 C CB  . ALA   B 1 522 ? -21.36100 74.76900  32.92700  1.000 95.59460  ? 1134 ALA   B CB  1 
ATOM   6795 N N   . LYS   B 1 523 ? -20.90000 76.47100  35.99400  1.000 94.37896  ? 1135 LYS   B N   1 
ATOM   6796 C CA  . LYS   B 1 523 ? -20.17700 77.53400  36.67700  1.000 96.26145  ? 1135 LYS   B CA  1 
ATOM   6797 C C   . LYS   B 1 523 ? -19.55600 77.07400  37.99000  1.000 92.83232  ? 1135 LYS   B C   1 
ATOM   6798 O O   . LYS   B 1 523 ? -18.74600 77.80800  38.56600  1.000 82.80056  ? 1135 LYS   B O   1 
ATOM   6799 C CB  . LYS   B 1 523 ? -21.09800 78.73300  36.93900  1.000 85.90871  ? 1135 LYS   B CB  1 
ATOM   6800 C CG  . LYS   B 1 523 ? -21.72400 79.32400  35.68500  1.000 87.13206  ? 1135 LYS   B CG  1 
ATOM   6801 C CD  . LYS   B 1 523 ? -22.77800 80.36000  36.03600  1.000 84.81380  ? 1135 LYS   B CD  1 
ATOM   6802 C CE  . LYS   B 1 523 ? -23.73000 79.83500  37.09800  1.000 90.13540  ? 1135 LYS   B CE  1 
ATOM   6803 N NZ  . LYS   B 1 523 ? -24.96400 80.66200  37.21300  1.000 83.91714  ? 1135 LYS   B NZ  1 
ATOM   6804 N N   . SER   B 1 524 ? -19.90900 75.88200  38.46500  1.000 92.75707  ? 1136 SER   B N   1 
ATOM   6805 C CA  . SER   B 1 524 ? -19.33900 75.35400  39.69300  1.000 93.05034  ? 1136 SER   B CA  1 
ATOM   6806 C C   . SER   B 1 524 ? -17.84100 75.11200  39.53100  1.000 98.10559  ? 1136 SER   B C   1 
ATOM   6807 O O   . SER   B 1 524 ? -17.32600 74.93500  38.42300  1.000 101.32673 ? 1136 SER   B O   1 
ATOM   6808 C CB  . SER   B 1 524 ? -20.03700 74.05200  40.08600  1.000 97.44085  ? 1136 SER   B CB  1 
ATOM   6809 O OG  . SER   B 1 524 ? -19.19500 73.24500  40.89000  1.000 99.47865  ? 1136 SER   B OG  1 
ATOM   6810 N N   . ARG   B 1 525 ? -17.13500 75.11500  40.66800  1.000 104.09663 ? 1137 ARG   B N   1 
ATOM   6811 C CA  . ARG   B 1 525 ? -15.72800 74.72300  40.67400  1.000 100.19907 ? 1137 ARG   B CA  1 
ATOM   6812 C C   . ARG   B 1 525 ? -15.56100 73.29300  40.17900  1.000 102.42856 ? 1137 ARG   B C   1 
ATOM   6813 O O   . ARG   B 1 525 ? -14.49900 72.93100  39.65500  1.000 102.20124 ? 1137 ARG   B O   1 
ATOM   6814 C CB  . ARG   B 1 525 ? -15.14900 74.88000  42.08200  1.000 97.08537  ? 1137 ARG   B CB  1 
ATOM   6815 C CG  . ARG   B 1 525 ? -13.64000 75.08600  42.14100  1.000 102.66418 ? 1137 ARG   B CG  1 
ATOM   6816 C CD  . ARG   B 1 525 ? -12.88700 73.76400  42.22300  1.000 102.71519 ? 1137 ARG   B CD  1 
ATOM   6817 N NE  . ARG   B 1 525 ? -13.02800 73.13500  43.53100  1.000 105.92918 ? 1137 ARG   B NE  1 
ATOM   6818 C CZ  . ARG   B 1 525 ? -12.25000 73.39200  44.57400  1.000 110.70431 ? 1137 ARG   B CZ  1 
ATOM   6819 N NH1 . ARG   B 1 525 ? -11.25600 74.26300  44.49600  1.000 110.72691 ? 1137 ARG   B NH1 1 
ATOM   6820 N NH2 . ARG   B 1 525 ? -12.47600 72.76200  45.72500  1.000 99.76401  ? 1137 ARG   B NH2 1 
ATOM   6821 N N   . TRP   B 1 526 ? -16.60500 72.47500  40.33500  1.000 102.26471 ? 1138 TRP   B N   1 
ATOM   6822 C CA  . TRP   B 1 526 ? -16.59300 71.11300  39.81500  1.000 100.46203 ? 1138 TRP   B CA  1 
ATOM   6823 C C   . TRP   B 1 526 ? -16.36600 71.09100  38.31100  1.000 98.42931  ? 1138 TRP   B C   1 
ATOM   6824 O O   . TRP   B 1 526 ? -15.60100 70.26300  37.80200  1.000 98.66291  ? 1138 TRP   B O   1 
ATOM   6825 C CB  . TRP   B 1 526 ? -17.91300 70.42900  40.16700  1.000 97.76134  ? 1138 TRP   B CB  1 
ATOM   6826 C CG  . TRP   B 1 526 ? -18.20200 69.16800  39.41000  1.000 95.49773  ? 1138 TRP   B CG  1 
ATOM   6827 C CD1 . TRP   B 1 526 ? -17.40700 68.06100  39.32100  1.000 90.90106  ? 1138 TRP   B CD1 1 
ATOM   6828 C CD2 . TRP   B 1 526 ? -19.39600 68.86500  38.67500  1.000 89.75639  ? 1138 TRP   B CD2 1 
ATOM   6829 N NE1 . TRP   B 1 526 ? -18.02100 67.09800  38.55500  1.000 92.46798  ? 1138 TRP   B NE1 1 
ATOM   6830 C CE2 . TRP   B 1 526 ? -19.24400 67.56700  38.14900  1.000 89.72039  ? 1138 TRP   B CE2 1 
ATOM   6831 C CE3 . TRP   B 1 526 ? -20.57200 69.57000  38.40200  1.000 83.93779  ? 1138 TRP   B CE3 1 
ATOM   6832 C CZ2 . TRP   B 1 526 ? -20.22600 66.95900  37.36800  1.000 85.89645  ? 1138 TRP   B CZ2 1 
ATOM   6833 C CZ3 . TRP   B 1 526 ? -21.54400 68.96500  37.62500  1.000 80.58370  ? 1138 TRP   B CZ3 1 
ATOM   6834 C CH2 . TRP   B 1 526 ? -21.36500 67.67400  37.11700  1.000 81.84009  ? 1138 TRP   B CH2 1 
ATOM   6835 N N   . TYR   B 1 527 ? -17.01500 72.00200  37.58200  1.000 98.39619  ? 1139 TYR   B N   1 
ATOM   6836 C CA  . TYR   B 1 527 ? -16.97200 71.97100  36.12700  1.000 99.47026  ? 1139 TYR   B CA  1 
ATOM   6837 C C   . TYR   B 1 527 ? -15.61700 72.38400  35.56100  1.000 102.72180 ? 1139 TYR   B C   1 
ATOM   6838 O O   . TYR   B 1 527 ? -15.39500 72.21600  34.35900  1.000 101.05489 ? 1139 TYR   B O   1 
ATOM   6839 C CB  . TYR   B 1 527 ? -18.07900 72.86300  35.55200  1.000 93.24920  ? 1139 TYR   B CB  1 
ATOM   6840 C CG  . TYR   B 1 527 ? -18.09400 72.95200  34.03600  1.000 97.85066  ? 1139 TYR   B CG  1 
ATOM   6841 C CD1 . TYR   B 1 527 ? -18.67300 71.95100  33.26600  1.000 95.86685  ? 1139 TYR   B CD1 1 
ATOM   6842 C CD2 . TYR   B 1 527 ? -17.51800 74.03400  33.37600  1.000 101.12531 ? 1139 TYR   B CD2 1 
ATOM   6843 C CE1 . TYR   B 1 527 ? -18.68400 72.02900  31.88500  1.000 95.84733  ? 1139 TYR   B CE1 1 
ATOM   6844 C CE2 . TYR   B 1 527 ? -17.52300 74.11900  31.99800  1.000 94.16126  ? 1139 TYR   B CE2 1 
ATOM   6845 C CZ  . TYR   B 1 527 ? -18.10700 73.11600  31.25800  1.000 97.14333  ? 1139 TYR   B CZ  1 
ATOM   6846 O OH  . TYR   B 1 527 ? -18.11200 73.20500  29.88600  1.000 98.51193  ? 1139 TYR   B OH  1 
ATOM   6847 N N   . ASN   B 1 528 ? -14.70000 72.90200  36.37900  1.000 97.92587  ? 1140 ASN   B N   1 
ATOM   6848 C CA  . ASN   B 1 528 ? -13.39500 73.29600  35.87100  1.000 103.61388 ? 1140 ASN   B CA  1 
ATOM   6849 C C   . ASN   B 1 528 ? -12.22300 72.59600  36.54900  1.000 104.39587 ? 1140 ASN   B C   1 
ATOM   6850 O O   . ASN   B 1 528 ? -11.08300 72.77400  36.10300  1.000 102.62333 ? 1140 ASN   B O   1 
ATOM   6851 C CB  . ASN   B 1 528 ? -13.21500 74.81900  35.97700  1.000 106.52905 ? 1140 ASN   B CB  1 
ATOM   6852 C CG  . ASN   B 1 528 ? -13.06400 75.48100  34.61500  1.000 106.68135 ? 1140 ASN   B CG  1 
ATOM   6853 O OD1 . ASN   B 1 528 ? -13.02000 74.80600  33.58400  1.000 101.02504 ? 1140 ASN   B OD1 1 
ATOM   6854 N ND2 . ASN   B 1 528 ? -12.99300 76.80800  34.60500  1.000 99.48221  ? 1140 ASN   B ND2 1 
ATOM   6855 N N   . GLN   B 1 529 ? -12.45800 71.81200  37.60100  1.000 102.02410 ? 1141 GLN   B N   1 
ATOM   6856 C CA  . GLN   B 1 529 ? -11.41400 70.93600  38.11900  1.000 100.24233 ? 1141 GLN   B CA  1 
ATOM   6857 C C   . GLN   B 1 529 ? -11.41200 69.58200  37.42100  1.000 103.91433 ? 1141 GLN   B C   1 
ATOM   6858 O O   . GLN   B 1 529 ? -10.35000 68.96100  37.29100  1.000 111.31903 ? 1141 GLN   B O   1 
ATOM   6859 C CB  . GLN   B 1 529 ? -11.56800 70.74900  39.63300  1.000 97.11434  ? 1141 GLN   B CB  1 
ATOM   6860 C CG  . GLN   B 1 529 ? -12.69900 69.82700  40.05400  1.000 100.01008 ? 1141 GLN   B CG  1 
ATOM   6861 C CD  . GLN   B 1 529 ? -12.84700 69.74300  41.55900  1.000 98.29758  ? 1141 GLN   B CD  1 
ATOM   6862 O OE1 . GLN   B 1 529 ? -11.93000 70.08900  42.30200  1.000 102.06597 ? 1141 GLN   B OE1 1 
ATOM   6863 N NE2 . GLN   B 1 529 ? -14.00200 69.27000  42.01600  1.000 91.73557  ? 1141 GLN   B NE2 1 
ATOM   6864 N N   . THR   B 1 530 ? -12.57800 69.11600  36.97100  1.000 99.31782  ? 1142 THR   B N   1 
ATOM   6865 C CA  . THR   B 1 530 ? -12.69900 67.93900  36.10800  1.000 100.19234 ? 1142 THR   B CA  1 
ATOM   6866 C C   . THR   B 1 530 ? -13.70600 68.26500  35.01200  1.000 92.65539  ? 1142 THR   B C   1 
ATOM   6867 O O   . THR   B 1 530 ? -14.82200 67.73200  34.98400  1.000 88.43211  ? 1142 THR   B O   1 
ATOM   6868 C CB  . THR   B 1 530 ? -13.12200 66.70100  36.90700  1.000 97.93161  ? 1142 THR   B CB  1 
ATOM   6869 O OG1 . THR   B 1 530 ? -14.33500 66.97500  37.62200  1.000 91.53501  ? 1142 THR   B OG1 1 
ATOM   6870 C CG2 . THR   B 1 530 ? -12.02700 66.27200  37.88800  1.000 89.06606  ? 1142 THR   B CG2 1 
ATOM   6871 N N   . PRO   B 1 531 ? -13.33400 69.14500  34.07700  1.000 92.91829  ? 1143 PRO   B N   1 
ATOM   6872 C CA  . PRO   B 1 531 ? -14.32700 69.63700  33.10700  1.000 94.75339  ? 1143 PRO   B CA  1 
ATOM   6873 C C   . PRO   B 1 531 ? -14.81300 68.58200  32.13100  1.000 96.67374  ? 1143 PRO   B C   1 
ATOM   6874 O O   . PRO   B 1 531 ? -16.01400 68.53100  31.83500  1.000 93.28969  ? 1143 PRO   B O   1 
ATOM   6875 C CB  . PRO   B 1 531 ? -13.57600 70.76900  32.39100  1.000 97.18833  ? 1143 PRO   B CB  1 
ATOM   6876 C CG  . PRO   B 1 531 ? -12.13800 70.39600  32.50600  1.000 98.05058  ? 1143 PRO   B CG  1 
ATOM   6877 C CD  . PRO   B 1 531 ? -11.99500 69.71600  33.84200  1.000 98.99447  ? 1143 PRO   B CD  1 
ATOM   6878 N N   . ASN   B 1 532 ? -13.91000 67.74900  31.61000  1.000 99.64520  ? 1144 ASN   B N   1 
ATOM   6879 C CA  . ASN   B 1 532 ? -14.30100 66.74900  30.62300  1.000 92.34740  ? 1144 ASN   B CA  1 
ATOM   6880 C C   . ASN   B 1 532 ? -15.33300 65.78700  31.19500  1.000 91.47587  ? 1144 ASN   B C   1 
ATOM   6881 O O   . ASN   B 1 532 ? -16.27500 65.38600  30.50100  1.000 87.36723  ? 1144 ASN   B O   1 
ATOM   6882 C CB  . ASN   B 1 532 ? -13.06500 65.98800  30.14800  1.000 86.19867  ? 1144 ASN   B CB  1 
ATOM   6883 C CG  . ASN   B 1 532 ? -11.91500 66.91200  29.80900  1.000 86.23592  ? 1144 ASN   B CG  1 
ATOM   6884 O OD1 . ASN   B 1 532 ? -12.08400 67.89900  29.09400  1.000 91.11912  ? 1144 ASN   B OD1 1 
ATOM   6885 N ND2 . ASN   B 1 532 ? -10.73800 66.60500  30.34000  1.000 91.15530  ? 1144 ASN   B ND2 1 
ATOM   6886 N N   . ARG   B 1 533 ? -15.17300 65.41200  32.46500  1.000 92.06024  ? 1145 ARG   B N   1 
ATOM   6887 C CA  . ARG   B 1 533 ? -16.13600 64.52800  33.10800  1.000 90.84286  ? 1145 ARG   B CA  1 
ATOM   6888 C C   . ARG   B 1 533 ? -17.39500 65.28000  33.51500  1.000 89.48337  ? 1145 ARG   B C   1 
ATOM   6889 O O   . ARG   B 1 533 ? -18.50500 64.75700  33.36800  1.000 89.26500  ? 1145 ARG   B O   1 
ATOM   6890 C CB  . ARG   B 1 533 ? -15.50100 63.85100  34.32300  1.000 92.84853  ? 1145 ARG   B CB  1 
ATOM   6891 C CG  . ARG   B 1 533 ? -16.38500 62.78900  34.95400  1.000 85.92560  ? 1145 ARG   B CG  1 
ATOM   6892 C CD  . ARG   B 1 533 ? -16.88600 63.19300  36.32300  1.000 77.98244  ? 1145 ARG   B CD  1 
ATOM   6893 N NE  . ARG   B 1 533 ? -17.38900 62.03900  37.05900  1.000 81.70957  ? 1145 ARG   B NE  1 
ATOM   6894 C CZ  . ARG   B 1 533 ? -16.67700 61.34100  37.93400  1.000 80.71516  ? 1145 ARG   B CZ  1 
ATOM   6895 N NH1 . ARG   B 1 533 ? -15.41400 61.63900  38.19200  1.000 82.11558  ? 1145 ARG   B NH1 1 
ATOM   6896 N NH2 . ARG   B 1 533 ? -17.24600 60.31800  38.56600  1.000 77.68463  ? 1145 ARG   B NH2 1 
ATOM   6897 N N   . ALA   B 1 534 ? -17.23900 66.50500  34.02500  1.000 90.90562  ? 1146 ALA   B N   1 
ATOM   6898 C CA  . ALA   B 1 534 ? -18.39400 67.29500  34.43700  1.000 87.17876  ? 1146 ALA   B CA  1 
ATOM   6899 C C   . ALA   B 1 534 ? -19.35500 67.51400  33.27600  1.000 84.40105  ? 1146 ALA   B C   1 
ATOM   6900 O O   . ALA   B 1 534 ? -20.56900 67.32300  33.41500  1.000 82.46627  ? 1146 ALA   B O   1 
ATOM   6901 C CB  . ALA   B 1 534 ? -17.93100 68.63300  35.01300  1.000 89.26964  ? 1146 ALA   B CB  1 
ATOM   6902 N N   . LYS   B 1 535 ? -18.82300 67.90300  32.11300  1.000 83.27397  ? 1147 LYS   B N   1 
ATOM   6903 C CA  . LYS   B 1 535 ? -19.66800 68.16000  30.95200  1.000 80.92481  ? 1147 LYS   B CA  1 
ATOM   6904 C C   . LYS   B 1 535 ? -20.45000 66.91900  30.53800  1.000 79.71424  ? 1147 LYS   B C   1 
ATOM   6905 O O   . LYS   B 1 535 ? -21.55400 67.03500  29.99500  1.000 78.86343  ? 1147 LYS   B O   1 
ATOM   6906 C CB  . LYS   B 1 535 ? -18.81400 68.66700  29.78900  1.000 85.75629  ? 1147 LYS   B CB  1 
ATOM   6907 C CG  . LYS   B 1 535 ? -19.59800 69.05900  28.54600  1.000 81.52786  ? 1147 LYS   B CG  1 
ATOM   6908 C CD  . LYS   B 1 535 ? -18.66400 69.53700  27.44700  1.000 87.70149  ? 1147 LYS   B CD  1 
ATOM   6909 C CE  . LYS   B 1 535 ? -18.19500 70.96000  27.70200  1.000 94.80543  ? 1147 LYS   B CE  1 
ATOM   6910 N NZ  . LYS   B 1 535 ? -17.45200 71.53800  26.54600  1.000 88.83744  ? 1147 LYS   B NZ  1 
ATOM   6911 N N   . ARG   B 1 536 ? -19.90600 65.72700  30.79600  1.000 79.90155  ? 1148 ARG   B N   1 
ATOM   6912 C CA  . ARG   B 1 536 ? -20.62500 64.50600  30.44900  1.000 79.39636  ? 1148 ARG   B CA  1 
ATOM   6913 C C   . ARG   B 1 536 ? -21.79100 64.25900  31.40100  1.000 80.43047  ? 1148 ARG   B C   1 
ATOM   6914 O O   . ARG   B 1 536 ? -22.85000 63.77700  30.97900  1.000 79.99088  ? 1148 ARG   B O   1 
ATOM   6915 C CB  . ARG   B 1 536 ? -19.67200 63.31100  30.44700  1.000 82.19263  ? 1148 ARG   B CB  1 
ATOM   6916 C CG  . ARG   B 1 536 ? -18.69600 63.27600  29.28700  1.000 79.90714  ? 1148 ARG   B CG  1 
ATOM   6917 C CD  . ARG   B 1 536 ? -17.94500 61.95200  29.24300  1.000 76.81098  ? 1148 ARG   B CD  1 
ATOM   6918 N NE  . ARG   B 1 536 ? -17.03900 61.77700  30.37300  1.000 84.32727  ? 1148 ARG   B NE  1 
ATOM   6919 C CZ  . ARG   B 1 536 ? -15.79300 62.23000  30.41500  1.000 83.03487  ? 1148 ARG   B CZ  1 
ATOM   6920 N NH1 . ARG   B 1 536 ? -15.28300 62.94400  29.42600  1.000 87.39830  ? 1148 ARG   B NH1 1 
ATOM   6921 N NH2 . ARG   B 1 536 ? -15.03800 61.95500  31.47500  1.000 82.38121  ? 1148 ARG   B NH2 1 
ATOM   6922 N N   . VAL   B 1 537 ? -21.61900 64.57900  32.68700  1.000 82.92643  ? 1149 VAL   B N   1 
ATOM   6923 C CA  . VAL   B 1 537 ? -22.71700 64.42000  33.63700  1.000 79.40059  ? 1149 VAL   B CA  1 
ATOM   6924 C C   . VAL   B 1 537 ? -23.77000 65.50000  33.43000  1.000 77.75096  ? 1149 VAL   B C   1 
ATOM   6925 O O   . VAL   B 1 537 ? -24.96500 65.26100  33.64200  1.000 80.88843  ? 1149 VAL   B O   1 
ATOM   6926 C CB  . VAL   B 1 537 ? -22.19400 64.42900  35.08600  1.000 78.01293  ? 1149 VAL   B CB  1 
ATOM   6927 C CG1 . VAL   B 1 537 ? -23.24300 63.86100  36.03200  1.000 72.47466  ? 1149 VAL   B CG1 1 
ATOM   6928 C CG2 . VAL   B 1 537 ? -20.89800 63.64600  35.19000  1.000 80.55035  ? 1149 VAL   B CG2 1 
ATOM   6929 N N   . ILE   B 1 538 ? -23.35800 66.70300  33.02500  1.000 77.44156  ? 1150 ILE   B N   1 
ATOM   6930 C CA  . ILE   B 1 538 ? -24.32900 67.77200  32.82200  1.000 73.33393  ? 1150 ILE   B CA  1 
ATOM   6931 C C   . ILE   B 1 538 ? -25.09700 67.55600  31.52300  1.000 78.05822  ? 1150 ILE   B C   1 
ATOM   6932 O O   . ILE   B 1 538 ? -26.30200 67.82400  31.44700  1.000 79.30142  ? 1150 ILE   B O   1 
ATOM   6933 C CB  . ILE   B 1 538 ? -23.63300 69.14600  32.85800  1.000 72.26582  ? 1150 ILE   B CB  1 
ATOM   6934 C CG1 . ILE   B 1 538 ? -23.04400 69.41300  34.24600  1.000 74.70005  ? 1150 ILE   B CG1 1 
ATOM   6935 C CG2 . ILE   B 1 538 ? -24.59800 70.25200  32.48500  1.000 72.48995  ? 1150 ILE   B CG2 1 
ATOM   6936 C CD1 . ILE   B 1 538 ? -21.71400 70.13800  34.22200  1.000 77.84184  ? 1150 ILE   B CD1 1 
ATOM   6937 N N   . THR   B 1 539 ? -24.42100 67.05100  30.48800  1.000 81.36901  ? 1151 THR   B N   1 
ATOM   6938 C CA  . THR   B 1 539 ? -25.08600 66.86900  29.20000  1.000 82.61171  ? 1151 THR   B CA  1 
ATOM   6939 C C   . THR   B 1 539 ? -26.12900 65.75800  29.25300  1.000 84.22637  ? 1151 THR   B C   1 
ATOM   6940 O O   . THR   B 1 539 ? -27.12000 65.80800  28.51500  1.000 83.47986  ? 1151 THR   B O   1 
ATOM   6941 C CB  . THR   B 1 539 ? -24.05600 66.58200  28.10800  1.000 76.88732  ? 1151 THR   B CB  1 
ATOM   6942 O OG1 . THR   B 1 539 ? -22.96500 67.50300  28.23100  1.000 80.19821  ? 1151 THR   B OG1 1 
ATOM   6943 C CG2 . THR   B 1 539 ? -24.68300 66.74700  26.73600  1.000 74.47647  ? 1151 THR   B CG2 1 
ATOM   6944 N N   . THR   B 1 540 ? -25.93400 64.75500  30.11400  1.000 77.62565  ? 1152 THR   B N   1 
ATOM   6945 C CA  . THR   B 1 540 ? -26.95300 63.72200  30.26600  1.000 78.65570  ? 1152 THR   B CA  1 
ATOM   6946 C C   . THR   B 1 540 ? -28.10600 64.19700  31.14700  1.000 82.50458  ? 1152 THR   B C   1 
ATOM   6947 O O   . THR   B 1 540 ? -29.23100 63.70500  31.00500  1.000 78.48803  ? 1152 THR   B O   1 
ATOM   6948 C CB  . THR   B 1 540 ? -26.33400 62.43400  30.81900  1.000 76.01935  ? 1152 THR   B CB  1 
ATOM   6949 O OG1 . THR   B 1 540 ? -27.35100 61.43900  30.97100  1.000 82.02066  ? 1152 THR   B OG1 1 
ATOM   6950 C CG2 . THR   B 1 540 ? -25.67800 62.67300  32.16000  1.000 74.45740  ? 1152 THR   B CG2 1 
ATOM   6951 N N   . PHE   B 1 541 ? -27.84500 65.14700  32.05200  1.000 81.62471  ? 1153 PHE   B N   1 
ATOM   6952 C CA  . PHE   B 1 541 ? -28.92700 65.86500  32.72200  1.000 76.51840  ? 1153 PHE   B CA  1 
ATOM   6953 C C   . PHE   B 1 541 ? -29.81500 66.58000  31.71300  1.000 75.17534  ? 1153 PHE   B C   1 
ATOM   6954 O O   . PHE   B 1 541 ? -31.04800 66.55600  31.82500  1.000 69.00968  ? 1153 PHE   B O   1 
ATOM   6955 C CB  . PHE   B 1 541 ? -28.34800 66.87600  33.71100  1.000 74.41963  ? 1153 PHE   B CB  1 
ATOM   6956 C CG  . PHE   B 1 541 ? -28.20100 66.35700  35.10800  1.000 71.31531  ? 1153 PHE   B CG  1 
ATOM   6957 C CD1 . PHE   B 1 541 ? -29.03200 65.35700  35.58600  1.000 71.42240  ? 1153 PHE   B CD1 1 
ATOM   6958 C CD2 . PHE   B 1 541 ? -27.22700 66.87300  35.94600  1.000 71.69941  ? 1153 PHE   B CD2 1 
ATOM   6959 C CE1 . PHE   B 1 541 ? -28.89800 64.88500  36.87700  1.000 72.72262  ? 1153 PHE   B CE1 1 
ATOM   6960 C CE2 . PHE   B 1 541 ? -27.08200 66.40400  37.23400  1.000 76.42774  ? 1153 PHE   B CE2 1 
ATOM   6961 C CZ  . PHE   B 1 541 ? -27.91900 65.40700  37.70200  1.000 81.55675  ? 1153 PHE   B CZ  1 
ATOM   6962 N N   . ARG   B 1 542 ? -29.19900 67.22600  30.72100  1.000 78.87112  ? 1154 ARG   B N   1 
ATOM   6963 C CA  . ARG   B 1 542 ? -29.94300 68.03100  29.75800  1.000 80.84510  ? 1154 ARG   B CA  1 
ATOM   6964 C C   . ARG   B 1 542 ? -30.83200 67.16600  28.87100  1.000 77.94777  ? 1154 ARG   B C   1 
ATOM   6965 O O   . ARG   B 1 542 ? -32.01000 67.47900  28.66100  1.000 71.48059  ? 1154 ARG   B O   1 
ATOM   6966 C CB  . ARG   B 1 542 ? -28.96500 68.84100  28.90500  1.000 81.95760  ? 1154 ARG   B CB  1 
ATOM   6967 C CG  . ARG   B 1 542 ? -29.59100 70.01100  28.17600  1.000 85.42157  ? 1154 ARG   B CG  1 
ATOM   6968 C CD  . ARG   B 1 542 ? -28.59600 70.69000  27.23900  1.000 91.93591  ? 1154 ARG   B CD  1 
ATOM   6969 N NE  . ARG   B 1 542 ? -27.45100 71.26300  27.93900  1.000 96.85712  ? 1154 ARG   B NE  1 
ATOM   6970 C CZ  . ARG   B 1 542 ? -27.22300 72.56400  28.06300  1.000 95.10326  ? 1154 ARG   B CZ  1 
ATOM   6971 N NH1 . ARG   B 1 542 ? -28.06100 73.46300  27.57200  1.000 92.10223  ? 1154 ARG   B NH1 1 
ATOM   6972 N NH2 . ARG   B 1 542 ? -26.12500 72.97400  28.69300  1.000 90.67116  ? 1154 ARG   B NH2 1 
ATOM   6973 N N   . THR   B 1 543 ? -30.28500 66.07100  28.34500  1.000 79.53309  ? 1155 THR   B N   1 
ATOM   6974 C CA  . THR   B 1 543 ? -30.95900 65.30500  27.30600  1.000 79.53264  ? 1155 THR   B CA  1 
ATOM   6975 C C   . THR   B 1 543 ? -31.77400 64.13800  27.84200  1.000 71.87354  ? 1155 THR   B C   1 
ATOM   6976 O O   . THR   B 1 543 ? -32.69600 63.68000  27.15700  1.000 70.10359  ? 1155 THR   B O   1 
ATOM   6977 C CB  . THR   B 1 543 ? -29.93400 64.77600  26.29200  1.000 82.36530  ? 1155 THR   B CB  1 
ATOM   6978 O OG1 . THR   B 1 543 ? -29.18900 63.69700  26.87300  1.000 84.80714  ? 1155 THR   B OG1 1 
ATOM   6979 C CG2 . THR   B 1 543 ? -28.97000 65.88300  25.87800  1.000 74.94636  ? 1155 THR   B CG2 1 
ATOM   6980 N N   . GLY   B 1 544 ? -31.46600 63.64900  29.04100  1.000 70.59483  ? 1156 GLY   B N   1 
ATOM   6981 C CA  . GLY   B 1 544 ? -32.09000 62.44200  29.53700  1.000 70.90292  ? 1156 GLY   B CA  1 
ATOM   6982 C C   . GLY   B 1 544 ? -31.63700 61.16800  28.86300  1.000 72.90306  ? 1156 GLY   B C   1 
ATOM   6983 O O   . GLY   B 1 544 ? -32.16200 60.09600  29.18500  1.000 68.15270  ? 1156 GLY   B O   1 
ATOM   6984 N N   . THR   B 1 545 ? -30.68200 61.24900  27.94000  1.000 75.08702  ? 1157 THR   B N   1 
ATOM   6985 C CA  . THR   B 1 545 ? -30.14600 60.10900  27.21200  1.000 74.56552  ? 1157 THR   B CA  1 
ATOM   6986 C C   . THR   B 1 545 ? -28.67200 59.91400  27.56800  1.000 73.96392  ? 1157 THR   B C   1 
ATOM   6987 O O   . THR   B 1 545 ? -28.10700 60.61400  28.41500  1.000 68.90218  ? 1157 THR   B O   1 
ATOM   6988 C CB  . THR   B 1 545 ? -30.32900 60.29800  25.70300  1.000 73.03512  ? 1157 THR   B CB  1 
ATOM   6989 O OG1 . THR   B 1 545 ? -29.67700 61.50400  25.28400  1.000 71.67134  ? 1157 THR   B OG1 1 
ATOM   6990 C CG2 . THR   B 1 545 ? -31.80800 60.39100  25.36000  1.000 70.42214  ? 1157 THR   B CG2 1 
ATOM   6991 N N   . TRP   B 1 546 ? -28.04600 58.94700  26.89800  1.000 71.29928  ? 1158 TRP   B N   1 
ATOM   6992 C CA  . TRP   B 1 546 ? -26.66900 58.55800  27.17100  1.000 73.50894  ? 1158 TRP   B CA  1 
ATOM   6993 C C   . TRP   B 1 546 ? -25.71100 59.02800  26.07900  1.000 71.84433  ? 1158 TRP   B C   1 
ATOM   6994 O O   . TRP   B 1 546 ? -24.64500 58.43600  25.88800  1.000 66.83460  ? 1158 TRP   B O   1 
ATOM   6995 C CB  . TRP   B 1 546 ? -26.57500 57.04300  27.33200  1.000 70.59140  ? 1158 TRP   B CB  1 
ATOM   6996 C CG  . TRP   B 1 546 ? -27.28400 56.50000  28.54200  1.000 67.84762  ? 1158 TRP   B CG  1 
ATOM   6997 C CD1 . TRP   B 1 546 ? -28.51900 55.91900  28.57700  1.000 63.46999  ? 1158 TRP   B CD1 1 
ATOM   6998 C CD2 . TRP   B 1 546 ? -26.79200 56.47500  29.88700  1.000 72.43329  ? 1158 TRP   B CD2 1 
ATOM   6999 N NE1 . TRP   B 1 546 ? -28.82800 55.53700  29.85900  1.000 62.86612  ? 1158 TRP   B NE1 1 
ATOM   7000 C CE2 . TRP   B 1 546 ? -27.78400 55.86800  30.68300  1.000 70.31002  ? 1158 TRP   B CE2 1 
ATOM   7001 C CE3 . TRP   B 1 546 ? -25.61000 56.90900  30.49500  1.000 72.03801  ? 1158 TRP   B CE3 1 
ATOM   7002 C CZ2 . TRP   B 1 546 ? -27.63000 55.68700  32.05700  1.000 75.76815  ? 1158 TRP   B CZ2 1 
ATOM   7003 C CZ3 . TRP   B 1 546 ? -25.45900 56.72700  31.85800  1.000 72.87180  ? 1158 TRP   B CZ3 1 
ATOM   7004 C CH2 . TRP   B 1 546 ? -26.46200 56.12000  32.62400  1.000 74.40691  ? 1158 TRP   B CH2 1 
ATOM   7005 N N   . ASP   B 1 547 ? -26.07700 60.10000  25.36500  1.000 73.24525  ? 1159 ASP   B N   1 
ATOM   7006 C CA  . ASP   B 1 547 ? -25.34300 60.50000  24.16500  1.000 76.68996  ? 1159 ASP   B CA  1 
ATOM   7007 C C   . ASP   B 1 547 ? -23.86400 60.75500  24.44000  1.000 74.41430  ? 1159 ASP   B C   1 
ATOM   7008 O O   . ASP   B 1 547 ? -23.03100 60.57300  23.54500  1.000 74.61974  ? 1159 ASP   B O   1 
ATOM   7009 C CB  . ASP   B 1 547 ? -25.97800 61.74800  23.54800  1.000 78.09368  ? 1159 ASP   B CB  1 
ATOM   7010 C CG  . ASP   B 1 547 ? -27.32200 61.46500  22.90300  1.000 80.46665  ? 1159 ASP   B CG  1 
ATOM   7011 O OD1 . ASP   B 1 547 ? -27.48700 60.37300  22.31900  1.000 76.73264  ? 1159 ASP   B OD1 1 
ATOM   7012 O OD2 . ASP   B 1 547 ? -28.20600 62.34600  22.96700  1.000 82.68617  ? 1159 ASP   B OD2 1 
ATOM   7013 N N   . ALA   B 1 548 ? -23.51400 61.16800  25.65600  1.000 73.11372  ? 1160 ALA   B N   1 
ATOM   7014 C CA  . ALA   B 1 548 ? -22.13800 61.54300  25.95300  1.000 73.18319  ? 1160 ALA   B CA  1 
ATOM   7015 C C   . ALA   B 1 548 ? -21.31500 60.41200  26.55700  1.000 75.70399  ? 1160 ALA   B C   1 
ATOM   7016 O O   . ALA   B 1 548 ? -20.10200 60.57500  26.72200  1.000 78.33770  ? 1160 ALA   B O   1 
ATOM   7017 C CB  . ALA   B 1 548 ? -22.11300 62.74700  26.90000  1.000 78.23495  ? 1160 ALA   B CB  1 
ATOM   7018 N N   . TYR   B 1 549 ? -21.93000 59.27800  26.87900  1.000 79.58679  ? 1161 TYR   B N   1 
ATOM   7019 C CA  . TYR   B 1 549 ? -21.22800 58.19700  27.57000  1.000 81.30303  ? 1161 TYR   B CA  1 
ATOM   7020 C C   . TYR   B 1 549 ? -21.21300 56.88500  26.79600  1.000 75.15260  ? 1161 TYR   B C   1 
ATOM   7021 O O   . TYR   B 1 549 ? -20.15900 56.42700  26.35600  1.000 68.55382  ? 1161 TYR   B O   1 
ATOM   7022 C CB  . TYR   B 1 549 ? -21.85400 57.96000  28.94200  1.000 78.82442  ? 1161 TYR   B CB  1 
ATOM   7023 C CG  . TYR   B 1 549 ? -21.29400 58.84200  30.02400  1.000 83.87705  ? 1161 TYR   B CG  1 
ATOM   7024 C CD1 . TYR   B 1 549 ? -19.98100 58.69100  30.45300  1.000 85.25139  ? 1161 TYR   B CD1 1 
ATOM   7025 C CD2 . TYR   B 1 549 ? -22.07500 59.81800  30.62600  1.000 82.62627  ? 1161 TYR   B CD2 1 
ATOM   7026 C CE1 . TYR   B 1 549 ? -19.45800 59.49000  31.45000  1.000 84.76155  ? 1161 TYR   B CE1 1 
ATOM   7027 C CE2 . TYR   B 1 549 ? -21.56300 60.62300  31.62100  1.000 83.45043  ? 1161 TYR   B CE2 1 
ATOM   7028 C CZ  . TYR   B 1 549 ? -20.25500 60.45100  32.03300  1.000 85.42240  ? 1161 TYR   B CZ  1 
ATOM   7029 O OH  . TYR   B 1 549 ? -19.73800 61.25200  33.02400  1.000 85.70798  ? 1161 TYR   B OH  1 
ATOM   7030 N N   . VAL   C 2 2   ? -45.72000 28.65300  36.00700  1.000 39.63819  ? 2    VAL   D N   1 
ATOM   7031 C CA  . VAL   C 2 2   ? -45.36600 30.03400  36.32000  1.000 48.65841  ? 2    VAL   D CA  1 
ATOM   7032 C C   . VAL   C 2 2   ? -46.05100 30.44000  37.62600  1.000 56.85883  ? 2    VAL   D C   1 
ATOM   7033 O O   . VAL   C 2 2   ? -47.03300 29.81400  38.02700  1.000 54.39937  ? 2    VAL   D O   1 
ATOM   7034 C CB  . VAL   C 2 2   ? -45.76200 30.98400  35.18600  1.000 44.25013  ? 2    VAL   D CB  1 
ATOM   7035 C CG1 . VAL   C 2 2   ? -45.26800 30.45400  33.85200  1.000 51.56668  ? 2    VAL   D CG1 1 
ATOM   7036 C CG2 . VAL   C 2 2   ? -47.24300 31.20800  35.17800  1.000 45.98082  ? 2    VAL   D CG2 1 
ATOM   7037 N N   . GLN   C 2 3   ? -45.53300 31.47700  38.29400  1.000 58.83026  ? 3    GLN   D N   1 
ATOM   7038 C CA  . GLN   C 2 3   ? -45.99600 31.85900  39.62500  1.000 54.22308  ? 3    GLN   D CA  1 
ATOM   7039 C C   . GLN   C 2 3   ? -46.05600 33.37600  39.75500  1.000 51.13272  ? 3    GLN   D C   1 
ATOM   7040 O O   . GLN   C 2 3   ? -45.24400 34.09700  39.17200  1.000 49.49270  ? 3    GLN   D O   1 
ATOM   7041 C CB  . GLN   C 2 3   ? -45.08400 31.27800  40.71800  1.000 52.11122  ? 3    GLN   D CB  1 
ATOM   7042 C CG  . GLN   C 2 3   ? -44.43600 29.95300  40.33800  1.000 60.69610  ? 3    GLN   D CG  1 
ATOM   7043 C CD  . GLN   C 2 3   ? -43.32300 29.54200  41.27100  1.000 70.34574  ? 3    GLN   D CD  1 
ATOM   7044 O OE1 . GLN   C 2 3   ? -43.25400 29.99300  42.41500  1.000 75.16811  ? 3    GLN   D OE1 1 
ATOM   7045 N NE2 . GLN   C 2 3   ? -42.44200 28.67300  40.78700  1.000 63.51290  ? 3    GLN   D NE2 1 
ATOM   7046 N N   . LEU   C 2 4   ? -47.02300 33.85500  40.54300  1.000 55.14096  ? 4    LEU   D N   1 
ATOM   7047 C CA  . LEU   C 2 4   ? -47.24500 35.28100  40.74700  1.000 57.70581  ? 4    LEU   D CA  1 
ATOM   7048 C C   . LEU   C 2 4   ? -47.25500 35.59700  42.24000  1.000 70.06801  ? 4    LEU   D C   1 
ATOM   7049 O O   . LEU   C 2 4   ? -47.63000 34.75900  43.06500  1.000 70.08449  ? 4    LEU   D O   1 
ATOM   7050 C CB  . LEU   C 2 4   ? -48.55800 35.74600  40.09400  1.000 57.53336  ? 4    LEU   D CB  1 
ATOM   7051 C CG  . LEU   C 2 4   ? -48.57500 35.79500  38.56100  1.000 50.10858  ? 4    LEU   D CG  1 
ATOM   7052 C CD1 . LEU   C 2 4   ? -48.76300 34.41400  37.95000  1.000 46.49215  ? 4    LEU   D CD1 1 
ATOM   7053 C CD2 . LEU   C 2 4   ? -49.65200 36.73500  38.06300  1.000 44.93273  ? 4    LEU   D CD2 1 
ATOM   7054 N N   . GLN   C 2 5   ? -46.85300 36.82600  42.57800  1.000 75.40329  ? 5    GLN   D N   1 
ATOM   7055 C CA  . GLN   C 2 5   ? -46.51000 37.19600  43.95600  1.000 64.55249  ? 5    GLN   D CA  1 
ATOM   7056 C C   . GLN   C 2 5   ? -46.93600 38.64300  44.20700  1.000 66.60944  ? 5    GLN   D C   1 
ATOM   7057 O O   . GLN   C 2 5   ? -46.22200 39.57500  43.82600  1.000 62.65318  ? 5    GLN   D O   1 
ATOM   7058 C CB  . GLN   C 2 5   ? -45.01100 37.00800  44.18100  1.000 54.96826  ? 5    GLN   D CB  1 
ATOM   7059 C CG  . GLN   C 2 5   ? -44.47200 37.43200  45.54400  1.000 75.36093  ? 5    GLN   D CG  1 
ATOM   7060 C CD  . GLN   C 2 5   ? -45.01500 36.60300  46.69500  1.000 78.62727  ? 5    GLN   D CD  1 
ATOM   7061 O OE1 . GLN   C 2 5   ? -44.45900 35.55600  47.03800  1.000 72.94715  ? 5    GLN   D OE1 1 
ATOM   7062 N NE2 . GLN   C 2 5   ? -46.09600 37.07600  47.30800  1.000 67.49312  ? 5    GLN   D NE2 1 
ATOM   7063 N N   . GLU   C 2 6   ? -48.08700 38.83100  44.85800  1.000 71.64364  ? 6    GLU   D N   1 
ATOM   7064 C CA  . GLU   C 2 6   ? -48.60300 40.17400  45.10500  1.000 73.51695  ? 6    GLU   D CA  1 
ATOM   7065 C C   . GLU   C 2 6   ? -47.94000 40.81000  46.33000  1.000 77.37006  ? 6    GLU   D C   1 
ATOM   7066 O O   . GLU   C 2 6   ? -47.23600 40.15800  47.10800  1.000 73.59947  ? 6    GLU   D O   1 
ATOM   7067 C CB  . GLU   C 2 6   ? -50.11700 40.16200  45.32400  1.000 69.03331  ? 6    GLU   D CB  1 
ATOM   7068 C CG  . GLU   C 2 6   ? -50.98600 39.98500  44.09600  1.000 70.34948  ? 6    GLU   D CG  1 
ATOM   7069 C CD  . GLU   C 2 6   ? -51.46700 38.56100  43.92600  1.000 70.89540  ? 6    GLU   D CD  1 
ATOM   7070 O OE1 . GLU   C 2 6   ? -50.94000 37.66600  44.62400  1.000 64.39024  ? 6    GLU   D OE1 1 
ATOM   7071 O OE2 . GLU   C 2 6   ? -52.39900 38.34900  43.11900  1.000 65.51321  ? 6    GLU   D OE2 1 
ATOM   7072 N N   . SER   C 2 7   ? -48.19600 42.11000  46.49700  1.000 75.09249  ? 7    SER   D N   1 
ATOM   7073 C CA  . SER   C 2 7   ? -47.78400 42.89800  47.65500  1.000 78.18247  ? 7    SER   D CA  1 
ATOM   7074 C C   . SER   C 2 7   ? -48.44100 44.27000  47.58000  1.000 81.38965  ? 7    SER   D C   1 
ATOM   7075 O O   . SER   C 2 7   ? -48.65700 44.80600  46.48900  1.000 76.36531  ? 7    SER   D O   1 
ATOM   7076 C CB  . SER   C 2 7   ? -46.25600 43.05700  47.73200  1.000 73.55124  ? 7    SER   D CB  1 
ATOM   7077 O OG  . SER   C 2 7   ? -45.59700 41.80900  47.87300  1.000 67.04028  ? 7    SER   D OG  1 
ATOM   7078 N N   . GLY   C 2 8   ? -48.76800 44.82400  48.75100  1.000 86.49774  ? 8    GLY   D N   1 
ATOM   7079 C CA  . GLY   C 2 8   ? -49.09500 46.23700  48.84400  1.000 89.29942  ? 8    GLY   D CA  1 
ATOM   7080 C C   . GLY   C 2 8   ? -50.49400 46.63300  49.28000  1.000 90.79421  ? 8    GLY   D C   1 
ATOM   7081 O O   . GLY   C 2 8   ? -50.99700 47.67400  48.84800  1.000 89.10677  ? 8    GLY   D O   1 
ATOM   7082 N N   . GLY   C 2 9   ? -51.11500 45.83900  50.15800  1.000 91.86070  ? 9    GLY   D N   1 
ATOM   7083 C CA  . GLY   C 2 9   ? -52.49600 46.12200  50.60300  1.000 94.26999  ? 9    GLY   D CA  1 
ATOM   7084 C C   . GLY   C 2 9   ? -52.53200 46.76000  51.98000  1.000 100.92809 ? 9    GLY   D C   1 
ATOM   7085 O O   . GLY   C 2 9   ? -51.98600 46.15100  52.92100  1.000 97.75313  ? 9    GLY   D O   1 
ATOM   7086 N N   . GLY   C 2 10  ? -53.21400 47.89500  52.11400  1.000 104.30282 ? 10   GLY   D N   1 
ATOM   7087 C CA  . GLY   C 2 10  ? -53.23500 48.59300  53.41000  1.000 104.39586 ? 10   GLY   D CA  1 
ATOM   7088 C C   . GLY   C 2 10  ? -54.55900 49.27600  53.67500  1.000 102.10851 ? 10   GLY   D C   1 
ATOM   7089 O O   . GLY   C 2 10  ? -55.33500 49.46600  52.71400  1.000 99.55201  ? 10   GLY   D O   1 
ATOM   7090 N N   . LEU   C 2 11  ? -54.81900 49.61900  54.93700  1.000 95.98605  ? 11   LEU   D N   1 
ATOM   7091 C CA  . LEU   C 2 11  ? -56.05000 50.38300  55.27300  1.000 84.34829  ? 11   LEU   D CA  1 
ATOM   7092 C C   . LEU   C 2 11  ? -55.79900 51.86300  54.95900  1.000 84.48935  ? 11   LEU   D C   1 
ATOM   7093 O O   . LEU   C 2 11  ? -54.77200 52.39400  55.42900  1.000 91.55702  ? 11   LEU   D O   1 
ATOM   7094 C CB  . LEU   C 2 11  ? -56.44200 50.18900  56.73600  1.000 80.00108  ? 11   LEU   D CB  1 
ATOM   7095 C CG  . LEU   C 2 11  ? -57.58700 51.07400  57.23700  1.000 79.91373  ? 11   LEU   D CG  1 
ATOM   7096 C CD1 . LEU   C 2 11  ? -58.92200 50.58500  56.70700  1.000 84.03066  ? 11   LEU   D CD1 1 
ATOM   7097 C CD2 . LEU   C 2 11  ? -57.60500 51.14600  58.75200  1.000 67.66066  ? 11   LEU   D CD2 1 
ATOM   7098 N N   . VAL   C 2 12  ? -56.69700 52.50200  54.20600  1.000 83.06888  ? 12   VAL   D N   1 
ATOM   7099 C CA  . VAL   C 2 12  ? -56.51400 53.88700  53.79100  1.000 89.92609  ? 12   VAL   D CA  1 
ATOM   7100 C C   . VAL   C 2 12  ? -57.80500 54.64700  54.06100  1.000 89.46328  ? 12   VAL   D C   1 
ATOM   7101 O O   . VAL   C 2 12  ? -58.90200 54.11600  53.85200  1.000 86.25974  ? 12   VAL   D O   1 
ATOM   7102 C CB  . VAL   C 2 12  ? -56.12700 53.98900  52.29600  1.000 88.68814  ? 12   VAL   D CB  1 
ATOM   7103 C CG1 . VAL   C 2 12  ? -55.87700 55.43200  51.89300  1.000 80.89099  ? 12   VAL   D CG1 1 
ATOM   7104 C CG2 . VAL   C 2 12  ? -54.91000 53.13000  51.98800  1.000 89.91830  ? 12   VAL   D CG2 1 
ATOM   7105 N N   . GLN   C 2 13  ? -57.67700 55.88100  54.53900  1.000 89.19906  ? 13   GLN   D N   1 
ATOM   7106 C CA  . GLN   C 2 13  ? -58.83300 56.75700  54.61100  1.000 87.75206  ? 13   GLN   D CA  1 
ATOM   7107 C C   . GLN   C 2 13  ? -59.29500 57.10500  53.20100  1.000 91.50207  ? 13   GLN   D C   1 
ATOM   7108 O O   . GLN   C 2 13  ? -58.52200 57.05100  52.24000  1.000 94.91597  ? 13   GLN   D O   1 
ATOM   7109 C CB  . GLN   C 2 13  ? -58.50400 58.03200  55.38900  1.000 82.51135  ? 13   GLN   D CB  1 
ATOM   7110 N N   . ALA   C 2 14  ? -60.57500 57.45400  53.08000  1.000 90.90649  ? 14   ALA   D N   1 
ATOM   7111 C CA  . ALA   C 2 14  ? -61.11600 57.83700  51.78300  1.000 89.97118  ? 14   ALA   D CA  1 
ATOM   7112 C C   . ALA   C 2 14  ? -60.29700 58.97900  51.19000  1.000 96.08042  ? 14   ALA   D C   1 
ATOM   7113 O O   . ALA   C 2 14  ? -59.67800 59.76800  51.90900  1.000 97.61476  ? 14   ALA   D O   1 
ATOM   7114 C CB  . ALA   C 2 14  ? -62.58800 58.23300  51.91200  1.000 74.68278  ? 14   ALA   D CB  1 
ATOM   7115 N N   . GLY   C 2 15  ? -60.29100 59.05900  49.85800  1.000 96.62951  ? 15   GLY   D N   1 
ATOM   7116 C CA  . GLY   C 2 15  ? -59.48700 60.03600  49.15300  1.000 91.28590  ? 15   GLY   D CA  1 
ATOM   7117 C C   . GLY   C 2 15  ? -57.99600 59.79000  49.18900  1.000 91.72531  ? 15   GLY   D C   1 
ATOM   7118 O O   . GLY   C 2 15  ? -57.25600 60.47500  48.47000  1.000 93.76125  ? 15   GLY   D O   1 
ATOM   7119 N N   . GLY   C 2 16  ? -57.52400 58.84200  49.99500  1.000 92.97921  ? 16   GLY   D N   1 
ATOM   7120 C CA  . GLY   C 2 16  ? -56.11300 58.52200  50.05100  1.000 92.33178  ? 16   GLY   D CA  1 
ATOM   7121 C C   . GLY   C 2 16  ? -55.63100 57.80800  48.80800  1.000 86.71623  ? 16   GLY   D C   1 
ATOM   7122 O O   . GLY   C 2 16  ? -56.26900 57.88000  47.75200  1.000 85.47937  ? 16   GLY   D O   1 
ATOM   7123 N N   . SER   C 2 17  ? -54.50300 57.11500  48.91200  1.000 82.34086  ? 17   SER   D N   1 
ATOM   7124 C CA  . SER   C 2 17  ? -53.91800 56.47700  47.74300  1.000 81.68792  ? 17   SER   D CA  1 
ATOM   7125 C C   . SER   C 2 17  ? -52.94700 55.40000  48.19700  1.000 83.67494  ? 17   SER   D C   1 
ATOM   7126 O O   . SER   C 2 17  ? -52.53800 55.35500  49.36100  1.000 83.69149  ? 17   SER   D O   1 
ATOM   7127 C CB  . SER   C 2 17  ? -53.20700 57.50000  46.84800  1.000 82.86435  ? 17   SER   D CB  1 
ATOM   7128 O OG  . SER   C 2 17  ? -54.05100 58.59600  46.53900  1.000 78.19360  ? 17   SER   D OG  1 
ATOM   7129 N N   . LEU   C 2 18  ? -52.57600 54.54200  47.25100  1.000 81.34136  ? 18   LEU   D N   1 
ATOM   7130 C CA  . LEU   C 2 18  ? -51.67200 53.42600  47.49700  1.000 84.05455  ? 18   LEU   D CA  1 
ATOM   7131 C C   . LEU   C 2 18  ? -51.32300 52.82400  46.14100  1.000 83.26205  ? 18   LEU   D C   1 
ATOM   7132 O O   . LEU   C 2 18  ? -51.94200 53.15100  45.12600  1.000 85.36432  ? 18   LEU   D O   1 
ATOM   7133 C CB  . LEU   C 2 18  ? -52.31300 52.39900  48.43900  1.000 89.89917  ? 18   LEU   D CB  1 
ATOM   7134 C CG  . LEU   C 2 18  ? -51.56800 51.13500  48.86200  1.000 89.51172  ? 18   LEU   D CG  1 
ATOM   7135 C CD1 . LEU   C 2 18  ? -50.28900 51.49400  49.59400  1.000 83.12338  ? 18   LEU   D CD1 1 
ATOM   7136 C CD2 . LEU   C 2 18  ? -52.47600 50.29600  49.74200  1.000 85.86763  ? 18   LEU   D CD2 1 
ATOM   7137 N N   . ARG   C 2 19  ? -50.30600 51.96400  46.12300  1.000 81.60837  ? 19   ARG   D N   1 
ATOM   7138 C CA  . ARG   C 2 19  ? -49.94200 51.25800  44.90500  1.000 79.50078  ? 19   ARG   D CA  1 
ATOM   7139 C C   . ARG   C 2 19  ? -49.77200 49.77400  45.19000  1.000 80.60529  ? 19   ARG   D C   1 
ATOM   7140 O O   . ARG   C 2 19  ? -49.43100 49.37000  46.30600  1.000 85.26345  ? 19   ARG   D O   1 
ATOM   7141 C CB  . ARG   C 2 19  ? -48.66100 51.81500  44.27100  1.000 82.84371  ? 19   ARG   D CB  1 
ATOM   7142 C CG  . ARG   C 2 19  ? -47.38200 51.06700  44.60300  1.000 92.30255  ? 19   ARG   D CG  1 
ATOM   7143 C CD  . ARG   C 2 19  ? -46.32000 51.31800  43.53700  1.000 84.87175  ? 19   ARG   D CD  1 
ATOM   7144 N NE  . ARG   C 2 19  ? -44.97000 51.07500  44.03200  1.000 86.33951  ? 19   ARG   D NE  1 
ATOM   7145 C CZ  . ARG   C 2 19  ? -43.86300 51.40200  43.38100  1.000 93.24084  ? 19   ARG   D CZ  1 
ATOM   7146 N NH1 . ARG   C 2 19  ? -43.90600 51.98700  42.19400  1.000 98.11097  ? 19   ARG   D NH1 1 
ATOM   7147 N NH2 . ARG   C 2 19  ? -42.68200 51.13100  43.93100  1.000 89.02045  ? 19   ARG   D NH2 1 
ATOM   7148 N N   . LEU   C 2 20  ? -50.01900 48.96600  44.16100  1.000 78.80299  ? 20   LEU   D N   1 
ATOM   7149 C CA  . LEU   C 2 20  ? -49.93700 47.51700  44.24600  1.000 78.90996  ? 20   LEU   D CA  1 
ATOM   7150 C C   . LEU   C 2 20  ? -48.82200 47.00200  43.34300  1.000 76.62559  ? 20   LEU   D C   1 
ATOM   7151 O O   . LEU   C 2 20  ? -48.51700 47.59400  42.30300  1.000 74.20054  ? 20   LEU   D O   1 
ATOM   7152 C CB  . LEU   C 2 20  ? -51.27600 46.86300  43.86500  1.000 77.13957  ? 20   LEU   D CB  1 
ATOM   7153 C CG  . LEU   C 2 20  ? -52.38100 46.82300  44.93000  1.000 80.96285  ? 20   LEU   D CG  1 
ATOM   7154 C CD1 . LEU   C 2 20  ? -51.86200 46.15500  46.18300  1.000 85.30802  ? 20   LEU   D CD1 1 
ATOM   7155 C CD2 . LEU   C 2 20  ? -52.93600 48.20800  45.25200  1.000 75.92076  ? 20   LEU   D CD2 1 
ATOM   7156 N N   . SER   C 2 21  ? -48.21800 45.88800  43.75300  1.000 73.61551  ? 21   SER   D N   1 
ATOM   7157 C CA  . SER   C 2 21  ? -47.08800 45.29400  43.05300  1.000 71.68373  ? 21   SER   D CA  1 
ATOM   7158 C C   . SER   C 2 21  ? -47.34400 43.81000  42.81700  1.000 77.82001  ? 21   SER   D C   1 
ATOM   7159 O O   . SER   C 2 21  ? -48.15200 43.18000  43.50600  1.000 76.63922  ? 21   SER   D O   1 
ATOM   7160 C CB  . SER   C 2 21  ? -45.78500 45.48300  43.84300  1.000 66.02239  ? 21   SER   D CB  1 
ATOM   7161 O OG  . SER   C 2 21  ? -44.76000 44.63800  43.34900  1.000 72.79044  ? 21   SER   D OG  1 
ATOM   7162 N N   . CYS   C 2 22  ? -46.63900 43.25200  41.83300  1.000 77.58808  ? 22   CYS   D N   1 
ATOM   7163 C CA  . CYS   C 2 22  ? -46.78300 41.83500  41.50200  1.000 69.26415  ? 22   CYS   D CA  1 
ATOM   7164 C C   . CYS   C 2 22  ? -45.53400 41.35700  40.78100  1.000 64.07370  ? 22   CYS   D C   1 
ATOM   7165 O O   . CYS   C 2 22  ? -45.22000 41.86000  39.70000  1.000 67.36764  ? 22   CYS   D O   1 
ATOM   7166 C CB  . CYS   C 2 22  ? -48.01600 41.60500  40.63500  1.000 64.65489  ? 22   CYS   D CB  1 
ATOM   7167 S SG  . CYS   C 2 22  ? -48.35800 39.86700  40.27800  1.000 65.32466  ? 22   CYS   D SG  1 
ATOM   7168 N N   . ALA   C 2 23  ? -44.83400 40.39000  41.36500  1.000 60.44584  ? 23   ALA   D N   1 
ATOM   7169 C CA  . ALA   C 2 23  ? -43.68700 39.75100  40.73700  1.000 52.29473  ? 23   ALA   D CA  1 
ATOM   7170 C C   . ALA   C 2 23  ? -44.12100 38.46000  40.05600  1.000 61.84985  ? 23   ALA   D C   1 
ATOM   7171 O O   . ALA   C 2 23  ? -45.12000 37.84000  40.43000  1.000 59.86940  ? 23   ALA   D O   1 
ATOM   7172 C CB  . ALA   C 2 23  ? -42.59300 39.45700  41.76400  1.000 59.38669  ? 23   ALA   D CB  1 
ATOM   7173 N N   . ALA   C 2 24  ? -43.35100 38.05300  39.04700  1.000 64.51455  ? 24   ALA   D N   1 
ATOM   7174 C CA  . ALA   C 2 24  ? -43.72400 36.90600  38.23200  1.000 52.60494  ? 24   ALA   D CA  1 
ATOM   7175 C C   . ALA   C 2 24  ? -42.49200 36.11200  37.82000  1.000 40.45956  ? 24   ALA   D C   1 
ATOM   7176 O O   . ALA   C 2 24  ? -41.39200 36.65400  37.67900  1.000 32.58581  ? 24   ALA   D O   1 
ATOM   7177 C CB  . ALA   C 2 24  ? -44.51300 37.33900  36.99100  1.000 39.98128  ? 24   ALA   D CB  1 
ATOM   7178 N N   . SER   C 2 25  ? -42.70200 34.81400  37.62100  1.000 38.03926  ? 25   SER   D N   1 
ATOM   7179 C CA  . SER   C 2 25  ? -41.65300 33.89400  37.21000  1.000 47.90542  ? 25   SER   D CA  1 
ATOM   7180 C C   . SER   C 2 25  ? -42.26600 32.82100  36.32200  1.000 58.14802  ? 25   SER   D C   1 
ATOM   7181 O O   . SER   C 2 25  ? -43.46300 32.54000  36.40200  1.000 54.08833  ? 25   SER   D O   1 
ATOM   7182 C CB  . SER   C 2 25  ? -40.96700 33.25600  38.42200  1.000 43.02894  ? 25   SER   D CB  1 
ATOM   7183 O OG  . SER   C 2 25  ? -40.32600 32.04400  38.06500  1.000 48.15934  ? 25   SER   D OG  1 
ATOM   7184 N N   . GLY   C 2 26  ? -41.43400 32.22600  35.46500  1.000 49.45571  ? 26   GLY   D N   1 
ATOM   7185 C CA  . GLY   C 2 26  ? -41.83200 31.08300  34.67100  1.000 48.15038  ? 26   GLY   D CA  1 
ATOM   7186 C C   . GLY   C 2 26  ? -42.12500 31.36800  33.21200  1.000 53.13324  ? 26   GLY   D C   1 
ATOM   7187 O O   . GLY   C 2 26  ? -42.34700 30.41900  32.44600  1.000 43.41972  ? 26   GLY   D O   1 
ATOM   7188 N N   . SER   C 2 27  ? -42.15100 32.63200  32.80500  1.000 49.42892  ? 27   SER   D N   1 
ATOM   7189 C CA  . SER   C 2 27  ? -42.36600 32.97800  31.40900  1.000 44.28331  ? 27   SER   D CA  1 
ATOM   7190 C C   . SER   C 2 27  ? -41.43400 34.13200  31.06500  1.000 42.96342  ? 27   SER   D C   1 
ATOM   7191 O O   . SER   C 2 27  ? -40.46600 34.41400  31.77700  1.000 40.14171  ? 27   SER   D O   1 
ATOM   7192 C CB  . SER   C 2 27  ? -43.83900 33.32400  31.15000  1.000 39.54743  ? 27   SER   D CB  1 
ATOM   7193 O OG  . SER   C 2 27  ? -44.26800 34.39300  31.97500  1.000 39.83859  ? 27   SER   D OG  1 
ATOM   7194 N N   . ILE   C 2 28  ? -41.72100 34.80000  29.95700  1.000 45.19364  ? 28   ILE   D N   1 
ATOM   7195 C CA  . ILE   C 2 28  ? -41.05300 36.04000  29.59100  1.000 46.05586  ? 28   ILE   D CA  1 
ATOM   7196 C C   . ILE   C 2 28  ? -42.04800 37.15200  29.89100  1.000 40.81236  ? 28   ILE   D C   1 
ATOM   7197 O O   . ILE   C 2 28  ? -42.95000 37.42900  29.09800  1.000 48.69631  ? 28   ILE   D O   1 
ATOM   7198 C CB  . ILE   C 2 28  ? -40.60100 36.03600  28.12800  1.000 42.40877  ? 28   ILE   D CB  1 
ATOM   7199 C CG1 . ILE   C 2 28  ? -39.80900 34.76400  27.83300  1.000 30.08025  ? 28   ILE   D CG1 1 
ATOM   7200 C CG2 . ILE   C 2 28  ? -39.78700 37.28900  27.79300  1.000 35.81339  ? 28   ILE   D CG2 1 
ATOM   7201 C CD1 . ILE   C 2 28  ? -39.60600 34.52900  26.38000  1.000 43.19339  ? 28   ILE   D CD1 1 
ATOM   7202 N N   . PHE   C 2 29  ? -41.88800 37.78300  31.05700  1.000 39.84033  ? 29   PHE   D N   1 
ATOM   7203 C CA  . PHE   C 2 29  ? -42.83800 38.80400  31.48800  1.000 51.25696  ? 29   PHE   D CA  1 
ATOM   7204 C C   . PHE   C 2 29  ? -43.00600 39.87300  30.41900  1.000 40.56602  ? 29   PHE   D C   1 
ATOM   7205 O O   . PHE   C 2 29  ? -44.07100 40.49100  30.31600  1.000 38.97392  ? 29   PHE   D O   1 
ATOM   7206 C CB  . PHE   C 2 29  ? -42.37200 39.40500  32.82600  1.000 52.94635  ? 29   PHE   D CB  1 
ATOM   7207 C CG  . PHE   C 2 29  ? -43.27900 40.47500  33.37400  1.000 44.75921  ? 29   PHE   D CG  1 
ATOM   7208 C CD1 . PHE   C 2 29  ? -43.21000 41.78200  32.90900  1.000 50.42244  ? 29   PHE   D CD1 1 
ATOM   7209 C CD2 . PHE   C 2 29  ? -44.20300 40.17000  34.35400  1.000 39.62576  ? 29   PHE   D CD2 1 
ATOM   7210 C CE1 . PHE   C 2 29  ? -44.05100 42.75700  33.40900  1.000 53.28426  ? 29   PHE   D CE1 1 
ATOM   7211 C CE2 . PHE   C 2 29  ? -45.04200 41.14300  34.86300  1.000 52.17959  ? 29   PHE   D CE2 1 
ATOM   7212 C CZ  . PHE   C 2 29  ? -44.96800 42.43700  34.38700  1.000 54.78699  ? 29   PHE   D CZ  1 
ATOM   7213 N N   . SER   C 2 30  ? -41.97100 40.08000  29.60100  1.000 44.92123  ? 30   SER   D N   1 
ATOM   7214 C CA  . SER   C 2 30  ? -42.04700 41.01800  28.48800  1.000 51.74141  ? 30   SER   D CA  1 
ATOM   7215 C C   . SER   C 2 30  ? -43.26800 40.75000  27.61900  1.000 50.08401  ? 30   SER   D C   1 
ATOM   7216 O O   . SER   C 2 30  ? -44.00700 41.67300  27.25700  1.000 47.27992  ? 30   SER   D O   1 
ATOM   7217 C CB  . SER   C 2 30  ? -40.77300 40.91800  27.64500  1.000 51.28149  ? 30   SER   D CB  1 
ATOM   7218 O OG  . SER   C 2 30  ? -39.61800 40.81200  28.46100  1.000 64.30124  ? 30   SER   D OG  1 
ATOM   7219 N N   . LEU   C 2 31  ? -43.50400 39.48000  27.29600  1.000 46.03662  ? 31   LEU   D N   1 
ATOM   7220 C CA  . LEU   C 2 31  ? -44.47000 39.09600  26.27900  1.000 43.89488  ? 31   LEU   D CA  1 
ATOM   7221 C C   . LEU   C 2 31  ? -45.88400 38.90100  26.81500  1.000 50.60932  ? 31   LEU   D C   1 
ATOM   7222 O O   . LEU   C 2 31  ? -46.82000 38.78500  26.01700  1.000 55.04135  ? 31   LEU   D O   1 
ATOM   7223 C CB  . LEU   C 2 31  ? -43.99500 37.81400  25.58700  1.000 40.27389  ? 31   LEU   D CB  1 
ATOM   7224 C CG  . LEU   C 2 31  ? -42.63200 37.91600  24.89500  1.000 41.96265  ? 31   LEU   D CG  1 
ATOM   7225 C CD1 . LEU   C 2 31  ? -42.21300 36.58400  24.30000  1.000 34.40772  ? 31   LEU   D CD1 1 
ATOM   7226 C CD2 . LEU   C 2 31  ? -42.66100 38.99100  23.82000  1.000 33.84191  ? 31   LEU   D CD2 1 
ATOM   7227 N N   . ASN   C 2 32  ? -46.07200 38.88700  28.12900  1.000 47.95165  ? 32   ASN   D N   1 
ATOM   7228 C CA  . ASN   C 2 32  ? -47.36700 38.57000  28.71400  1.000 41.33308  ? 32   ASN   D CA  1 
ATOM   7229 C C   . ASN   C 2 32  ? -48.19400 39.82700  28.95000  1.000 45.95822  ? 32   ASN   D C   1 
ATOM   7230 O O   . ASN   C 2 32  ? -47.67800 40.85100  29.40700  1.000 48.27694  ? 32   ASN   D O   1 
ATOM   7231 C CB  . ASN   C 2 32  ? -47.18400 37.82100  30.03400  1.000 40.99826  ? 32   ASN   D CB  1 
ATOM   7232 C CG  . ASN   C 2 32  ? -46.26700 36.62300  29.90000  1.000 49.49834  ? 32   ASN   D CG  1 
ATOM   7233 O OD1 . ASN   C 2 32  ? -45.34500 36.43600  30.70300  1.000 44.73088  ? 32   ASN   D OD1 1 
ATOM   7234 N ND2 . ASN   C 2 32  ? -46.50500 35.80700  28.87300  1.000 40.35509  ? 32   ASN   D ND2 1 
ATOM   7235 N N   . ASP   C 2 33  ? -49.48500 39.74500  28.63500  1.000 47.77100  ? 33   ASP   D N   1 
ATOM   7236 C CA  . ASP   C 2 33  ? -50.41100 40.78500  29.05400  1.000 49.11975  ? 33   ASP   D CA  1 
ATOM   7237 C C   . ASP   C 2 33  ? -50.62600 40.71200  30.55800  1.000 53.09003  ? 33   ASP   D C   1 
ATOM   7238 O O   . ASP   C 2 33  ? -50.51500 39.64700  31.17300  1.000 48.67055  ? 33   ASP   D O   1 
ATOM   7239 C CB  . ASP   C 2 33  ? -51.75600 40.65100  28.34300  1.000 52.06709  ? 33   ASP   D CB  1 
ATOM   7240 C CG  . ASP   C 2 33  ? -51.64100 40.77700  26.84700  1.000 54.29231  ? 33   ASP   D CG  1 
ATOM   7241 O OD1 . ASP   C 2 33  ? -50.50300 40.88600  26.34900  1.000 67.13864  ? 33   ASP   D OD1 1 
ATOM   7242 O OD2 . ASP   C 2 33  ? -52.69400 40.78700  26.17400  1.000 44.36424  ? 33   ASP   D OD2 1 
ATOM   7243 N N   . MET   C 2 34  ? -50.94200 41.86000  31.15300  1.000 56.45408  ? 34   MET   D N   1 
ATOM   7244 C CA  . MET   C 2 34  ? -51.09600 41.94300  32.59900  1.000 55.03462  ? 34   MET   D CA  1 
ATOM   7245 C C   . MET   C 2 34  ? -52.29300 42.81900  32.94300  1.000 58.67576  ? 34   MET   D C   1 
ATOM   7246 O O   . MET   C 2 34  ? -52.76400 43.61600  32.12500  1.000 53.87702  ? 34   MET   D O   1 
ATOM   7247 C CB  . MET   C 2 34  ? -49.83200 42.48800  33.26900  1.000 49.93057  ? 34   MET   D CB  1 
ATOM   7248 C CG  . MET   C 2 34  ? -48.60000 41.64300  33.02500  1.000 48.39545  ? 34   MET   D CG  1 
ATOM   7249 S SD  . MET   C 2 34  ? -48.54700 40.21300  34.10700  1.000 53.58624  ? 34   MET   D SD  1 
ATOM   7250 C CE  . MET   C 2 34  ? -47.31900 39.23100  33.26500  1.000 50.17443  ? 34   MET   D CE  1 
ATOM   7251 N N   . GLY   C 2 35  ? -52.78000 42.65600  34.17400  1.000 59.53170  ? 35   GLY   D N   1 
ATOM   7252 C CA  . GLY   C 2 35  ? -53.90200 43.42500  34.67100  1.000 65.15818  ? 35   GLY   D CA  1 
ATOM   7253 C C   . GLY   C 2 35  ? -54.32600 43.02400  36.07100  1.000 62.14234  ? 35   GLY   D C   1 
ATOM   7254 O O   . GLY   C 2 35  ? -53.99200 41.92900  36.52100  1.000 64.32644  ? 35   GLY   D O   1 
ATOM   7255 N N   . TRP   C 2 36  ? -55.05200 43.89200  36.77800  1.000 67.69229  ? 36   TRP   D N   1 
ATOM   7256 C CA  . TRP   C 2 36  ? -55.53600 43.57900  38.11500  1.000 70.14061  ? 36   TRP   D CA  1 
ATOM   7257 C C   . TRP   C 2 36  ? -57.04300 43.36900  38.10000  1.000 69.57753  ? 36   TRP   D C   1 
ATOM   7258 O O   . TRP   C 2 36  ? -57.76300 43.96500  37.29500  1.000 70.23108  ? 36   TRP   D O   1 
ATOM   7259 C CB  . TRP   C 2 36  ? -55.18600 44.68300  39.11500  1.000 68.05500  ? 36   TRP   D CB  1 
ATOM   7260 C CG  . TRP   C 2 36  ? -53.72600 44.84800  39.37200  1.000 71.74683  ? 36   TRP   D CG  1 
ATOM   7261 C CD1 . TRP   C 2 36  ? -52.88300 45.68700  38.72400  1.000 70.11015  ? 36   TRP   D CD1 1 
ATOM   7262 C CD2 . TRP   C 2 36  ? -52.94300 44.18100  40.37100  1.000 65.33563  ? 36   TRP   D CD2 1 
ATOM   7263 N NE1 . TRP   C 2 36  ? -51.61500 45.57600  39.23500  1.000 67.18559  ? 36   TRP   D NE1 1 
ATOM   7264 C CE2 . TRP   C 2 36  ? -51.62500 44.65900  40.25100  1.000 64.97343  ? 36   TRP   D CE2 1 
ATOM   7265 C CE3 . TRP   C 2 36  ? -53.22800 43.22400  41.34700  1.000 64.55356  ? 36   TRP   D CE3 1 
ATOM   7266 C CZ2 . TRP   C 2 36  ? -50.59100 44.21300  41.06700  1.000 66.74855  ? 36   TRP   D CZ2 1 
ATOM   7267 C CZ3 . TRP   C 2 36  ? -52.20200 42.78200  42.15900  1.000 67.06644  ? 36   TRP   D CZ3 1 
ATOM   7268 C CH2 . TRP   C 2 36  ? -50.89800 43.27600  42.01200  1.000 69.10226  ? 36   TRP   D CH2 1 
ATOM   7269 N N   . TYR   C 2 37  ? -57.51300 42.51500  39.00400  1.000 71.51893  ? 37   TYR   D N   1 
ATOM   7270 C CA  . TYR   C 2 37  ? -58.93600 42.28500  39.19800  1.000 68.53964  ? 37   TYR   D CA  1 
ATOM   7271 C C   . TYR   C 2 37  ? -59.26700 42.40600  40.67500  1.000 70.47760  ? 37   TYR   D C   1 
ATOM   7272 O O   . TYR   C 2 37  ? -58.47400 42.00000  41.53000  1.000 71.38290  ? 37   TYR   D O   1 
ATOM   7273 C CB  . TYR   C 2 37  ? -59.37100 40.90500  38.69000  1.000 64.99300  ? 37   TYR   D CB  1 
ATOM   7274 C CG  . TYR   C 2 37  ? -59.40000 40.76600  37.18700  1.000 64.22468  ? 37   TYR   D CG  1 
ATOM   7275 C CD1 . TYR   C 2 37  ? -58.23100 40.80900  36.44000  1.000 62.06899  ? 37   TYR   D CD1 1 
ATOM   7276 C CD2 . TYR   C 2 37  ? -60.59900 40.57000  36.51800  1.000 65.69105  ? 37   TYR   D CD2 1 
ATOM   7277 C CE1 . TYR   C 2 37  ? -58.25900 40.67600  35.06700  1.000 60.42765  ? 37   TYR   D CE1 1 
ATOM   7278 C CE2 . TYR   C 2 37  ? -60.63600 40.43500  35.14900  1.000 65.40614  ? 37   TYR   D CE2 1 
ATOM   7279 C CZ  . TYR   C 2 37  ? -59.46600 40.48900  34.42800  1.000 60.42470  ? 37   TYR   D CZ  1 
ATOM   7280 O OH  . TYR   C 2 37  ? -59.51200 40.35200  33.06100  1.000 70.36714  ? 37   TYR   D OH  1 
ATOM   7281 N N   . ARG   C 2 38  ? -60.43400 42.96700  40.97700  1.000 68.43782  ? 38   ARG   D N   1 
ATOM   7282 C CA  . ARG   C 2 38  ? -60.89000 43.06800  42.35200  1.000 71.31568  ? 38   ARG   D CA  1 
ATOM   7283 C C   . ARG   C 2 38  ? -62.16700 42.26000  42.53600  1.000 69.97082  ? 38   ARG   D C   1 
ATOM   7284 O O   . ARG   C 2 38  ? -62.91500 42.01000  41.58600  1.000 65.83412  ? 38   ARG   D O   1 
ATOM   7285 C CB  . ARG   C 2 38  ? -61.14300 44.52300  42.77000  1.000 73.74023  ? 38   ARG   D CB  1 
ATOM   7286 C CG  . ARG   C 2 38  ? -62.40700 45.14000  42.18500  1.000 68.40931  ? 38   ARG   D CG  1 
ATOM   7287 C CD  . ARG   C 2 38  ? -62.50200 46.61500  42.54100  1.000 64.19655  ? 38   ARG   D CD  1 
ATOM   7288 N NE  . ARG   C 2 38  ? -63.67200 47.25000  41.94800  1.000 69.35915  ? 38   ARG   D NE  1 
ATOM   7289 C CZ  . ARG   C 2 38  ? -63.89900 48.55600  41.96300  1.000 75.65422  ? 38   ARG   D CZ  1 
ATOM   7290 N NH1 . ARG   C 2 38  ? -63.05500 49.39800  42.53500  1.000 66.52047  ? 38   ARG   D NH1 1 
ATOM   7291 N NH2 . ARG   C 2 38  ? -65.00400 49.02900  41.39300  1.000 86.82914  ? 38   ARG   D NH2 1 
ATOM   7292 N N   . GLN   C 2 39  ? -62.40400 41.85400  43.78000  1.000 75.57947  ? 39   GLN   D N   1 
ATOM   7293 C CA  . GLN   C 2 39  ? -63.65800 41.20400  44.15100  1.000 77.31064  ? 39   GLN   D CA  1 
ATOM   7294 C C   . GLN   C 2 39  ? -63.96400 41.55700  45.59800  1.000 75.52530  ? 39   GLN   D C   1 
ATOM   7295 O O   . GLN   C 2 39  ? -63.22900 41.15200  46.50300  1.000 73.42557  ? 39   GLN   D O   1 
ATOM   7296 C CB  . GLN   C 2 39  ? -63.58500 39.69200  43.97100  1.000 75.32496  ? 39   GLN   D CB  1 
ATOM   7297 C CG  . GLN   C 2 39  ? -64.95400 39.04000  43.95400  1.000 64.73292  ? 39   GLN   D CG  1 
ATOM   7298 C CD  . GLN   C 2 39  ? -64.93100 37.61300  44.44100  1.000 69.17438  ? 39   GLN   D CD  1 
ATOM   7299 O OE1 . GLN   C 2 39  ? -64.05300 37.22100  45.21000  1.000 72.74552  ? 39   GLN   D OE1 1 
ATOM   7300 N NE2 . GLN   C 2 39  ? -65.89700 36.82100  43.99100  1.000 71.05731  ? 39   GLN   D NE2 1 
ATOM   7301 N N   . ALA   C 2 40  ? -65.04400 42.30500  45.81000  1.000 77.34259  ? 40   ALA   D N   1 
ATOM   7302 C CA  . ALA   C 2 40  ? -65.58800 42.68800  47.10600  1.000 79.96738  ? 40   ALA   D CA  1 
ATOM   7303 C C   . ALA   C 2 40  ? -66.64100 41.67600  47.55300  1.000 82.87219  ? 40   ALA   D C   1 
ATOM   7304 O O   . ALA   C 2 40  ? -67.37000 41.13500  46.71500  1.000 83.05519  ? 40   ALA   D O   1 
ATOM   7305 C CB  . ALA   C 2 40  ? -66.21300 44.07900  47.03700  1.000 84.59580  ? 40   ALA   D CB  1 
ATOM   7306 N N   . PRO   C 2 41  ? -66.75100 41.40000  48.85400  1.000 91.01227  ? 41   PRO   D N   1 
ATOM   7307 C CA  . PRO   C 2 41  ? -67.73000 40.40400  49.31300  1.000 84.22210  ? 41   PRO   D CA  1 
ATOM   7308 C C   . PRO   C 2 41  ? -69.14000 40.80700  48.91400  1.000 78.06129  ? 41   PRO   D C   1 
ATOM   7309 O O   . PRO   C 2 41  ? -69.56600 41.94400  49.13200  1.000 79.34571  ? 41   PRO   D O   1 
ATOM   7310 C CB  . PRO   C 2 41  ? -67.54400 40.39400  50.83400  1.000 71.95393  ? 41   PRO   D CB  1 
ATOM   7311 C CG  . PRO   C 2 41  ? -66.96500 41.72900  51.15000  1.000 82.13714  ? 41   PRO   D CG  1 
ATOM   7312 C CD  . PRO   C 2 41  ? -66.08300 42.07400  49.98200  1.000 89.26854  ? 41   PRO   D CD  1 
ATOM   7313 N N   . GLY   C 2 42  ? -69.85700 39.86400  48.30800  1.000 75.54189  ? 42   GLY   D N   1 
ATOM   7314 C CA  . GLY   C 2 42  ? -71.14100 40.14800  47.71000  1.000 80.30655  ? 42   GLY   D CA  1 
ATOM   7315 C C   . GLY   C 2 42  ? -71.07500 40.68100  46.29700  1.000 81.17051  ? 42   GLY   D C   1 
ATOM   7316 O O   . GLY   C 2 42  ? -72.12800 40.91300  45.68900  1.000 84.11772  ? 42   GLY   D O   1 
ATOM   7317 N N   . LYS   C 2 43  ? -69.87600 40.89000  45.75700  1.000 78.99965  ? 43   LYS   D N   1 
ATOM   7318 C CA  . LYS   C 2 43  ? -69.68900 41.34700  44.38900  1.000 79.32259  ? 43   LYS   D CA  1 
ATOM   7319 C C   . LYS   C 2 43  ? -68.82900 40.34400  43.63100  1.000 80.55881  ? 43   LYS   D C   1 
ATOM   7320 O O   . LYS   C 2 43  ? -67.95300 39.69400  44.20700  1.000 83.22893  ? 43   LYS   D O   1 
ATOM   7321 C CB  . LYS   C 2 43  ? -69.03200 42.73500  44.34800  1.000 72.56091  ? 43   LYS   D CB  1 
ATOM   7322 N N   . LEU   C 2 44  ? -69.08600 40.21900  42.33300  1.000 75.22517  ? 44   LEU   D N   1 
ATOM   7323 C CA  . LEU   C 2 44  ? -68.30900 39.30500  41.51300  1.000 75.02951  ? 44   LEU   D CA  1 
ATOM   7324 C C   . LEU   C 2 44  ? -66.95500 39.92000  41.16200  1.000 79.19737  ? 44   LEU   D C   1 
ATOM   7325 O O   . LEU   C 2 44  ? -66.75100 41.13400  41.25400  1.000 83.15570  ? 44   LEU   D O   1 
ATOM   7326 C CB  . LEU   C 2 44  ? -69.06700 38.93900  40.23600  1.000 73.92808  ? 44   LEU   D CB  1 
ATOM   7327 C CG  . LEU   C 2 44  ? -70.22200 37.93300  40.29900  1.000 77.28577  ? 44   LEU   D CG  1 
ATOM   7328 C CD1 . LEU   C 2 44  ? -71.36500 38.39600  41.20100  1.000 89.78697  ? 44   LEU   D CD1 1 
ATOM   7329 C CD2 . LEU   C 2 44  ? -70.73500 37.65900  38.89300  1.000 70.28674  ? 44   LEU   D CD2 1 
ATOM   7330 N N   . ARG   C 2 45  ? -66.02100 39.05500  40.76800  1.000 73.70761  ? 45   ARG   D N   1 
ATOM   7331 C CA  . ARG   C 2 45  ? -64.70800 39.51300  40.33600  1.000 66.64529  ? 45   ARG   D CA  1 
ATOM   7332 C C   . ARG   C 2 45  ? -64.85300 40.50100  39.18500  1.000 68.13565  ? 45   ARG   D C   1 
ATOM   7333 O O   . ARG   C 2 45  ? -65.68100 40.31700  38.28900  1.000 69.09268  ? 45   ARG   D O   1 
ATOM   7334 C CB  . ARG   C 2 45  ? -63.85000 38.31900  39.91800  1.000 67.34054  ? 45   ARG   D CB  1 
ATOM   7335 C CG  . ARG   C 2 45  ? -62.39400 38.64600  39.64500  1.000 72.73448  ? 45   ARG   D CG  1 
ATOM   7336 C CD  . ARG   C 2 45  ? -61.62300 37.39100  39.27500  1.000 70.41124  ? 45   ARG   D CD  1 
ATOM   7337 N NE  . ARG   C 2 45  ? -61.51700 36.47100  40.40100  1.000 75.16742  ? 45   ARG   D NE  1 
ATOM   7338 C CZ  . ARG   C 2 45  ? -61.07400 35.22400  40.31200  1.000 79.56932  ? 45   ARG   D CZ  1 
ATOM   7339 N NH1 . ARG   C 2 45  ? -60.71200 34.69900  39.15200  1.000 67.88281  ? 45   ARG   D NH1 1 
ATOM   7340 N NH2 . ARG   C 2 45  ? -60.99300 34.48500  41.41500  1.000 84.57300  ? 45   ARG   D NH2 1 
ATOM   7341 N N   . GLU   C 2 46  ? -64.05600 41.56700  39.22500  1.000 67.10678  ? 46   GLU   D N   1 
ATOM   7342 C CA  . GLU   C 2 46  ? -64.17400 42.65500  38.26500  1.000 71.63899  ? 46   GLU   D CA  1 
ATOM   7343 C C   . GLU   C 2 46  ? -62.79800 43.08500  37.78400  1.000 75.21670  ? 46   GLU   D C   1 
ATOM   7344 O O   . GLU   C 2 46  ? -61.85900 43.18900  38.57900  1.000 75.77497  ? 46   GLU   D O   1 
ATOM   7345 C CB  . GLU   C 2 46  ? -64.90200 43.86100  38.87700  1.000 73.20451  ? 46   GLU   D CB  1 
ATOM   7346 C CG  . GLU   C 2 46  ? -66.39200 43.92400  38.57500  1.000 87.19366  ? 46   GLU   D CG  1 
ATOM   7347 C CD  . GLU   C 2 46  ? -67.03300 45.20900  39.07100  1.000 99.25439  ? 46   GLU   D CD  1 
ATOM   7348 O OE1 . GLU   C 2 46  ? -66.46700 45.84200  39.99000  1.000 93.35448  ? 46   GLU   D OE1 1 
ATOM   7349 O OE2 . GLU   C 2 46  ? -68.10100 45.58700  38.54000  1.000 95.58346  ? 46   GLU   D OE2 1 
ATOM   7350 N N   . LEU   C 2 47  ? -62.68600 43.34500  36.48200  1.000 66.23735  ? 47   LEU   D N   1 
ATOM   7351 C CA  . LEU   C 2 47  ? -61.46700 43.93200  35.94400  1.000 67.14270  ? 47   LEU   D CA  1 
ATOM   7352 C C   . LEU   C 2 47  ? -61.37000 45.39000  36.36800  1.000 74.44947  ? 47   LEU   D C   1 
ATOM   7353 O O   . LEU   C 2 47  ? -62.34700 46.14000  36.27300  1.000 73.45531  ? 47   LEU   D O   1 
ATOM   7354 C CB  . LEU   C 2 47  ? -61.44400 43.83400  34.42200  1.000 69.88075  ? 47   LEU   D CB  1 
ATOM   7355 C CG  . LEU   C 2 47  ? -60.36000 44.68400  33.75100  1.000 69.14820  ? 47   LEU   D CG  1 
ATOM   7356 C CD1 . LEU   C 2 47  ? -58.96600 44.21300  34.16000  1.000 72.90506  ? 47   LEU   D CD1 1 
ATOM   7357 C CD2 . LEU   C 2 47  ? -60.51300 44.69400  32.23700  1.000 66.55275  ? 47   LEU   D CD2 1 
ATOM   7358 N N   . VAL   C 2 48  ? -60.19200 45.79500  36.83500  1.000 74.71413  ? 48   VAL   D N   1 
ATOM   7359 C CA  . VAL   C 2 48  ? -59.95000 47.16700  37.24700  1.000 76.85189  ? 48   VAL   D CA  1 
ATOM   7360 C C   . VAL   C 2 48  ? -59.03600 47.89600  36.26700  1.000 73.71426  ? 48   VAL   D C   1 
ATOM   7361 O O   . VAL   C 2 48  ? -59.26600 49.06800  35.95600  1.000 69.02426  ? 48   VAL   D O   1 
ATOM   7362 C CB  . VAL   C 2 48  ? -59.38900 47.22100  38.68900  1.000 68.24300  ? 48   VAL   D CB  1 
ATOM   7363 C CG1 . VAL   C 2 48  ? -60.17300 46.28000  39.58700  1.000 67.55952  ? 48   VAL   D CG1 1 
ATOM   7364 C CG2 . VAL   C 2 48  ? -57.90400 46.88600  38.74000  1.000 71.98768  ? 48   VAL   D CG2 1 
ATOM   7365 N N   . ALA   C 2 49  ? -58.02700 47.20900  35.73500  1.000 69.17875  ? 49   ALA   D N   1 
ATOM   7366 C CA  . ALA   C 2 49  ? -57.03900 47.81800  34.85700  1.000 69.55022  ? 49   ALA   D CA  1 
ATOM   7367 C C   . ALA   C 2 49  ? -56.20000 46.71500  34.24100  1.000 68.47961  ? 49   ALA   D C   1 
ATOM   7368 O O   . ALA   C 2 49  ? -55.80600 45.77400  34.93200  1.000 66.36187  ? 49   ALA   D O   1 
ATOM   7369 C CB  . ALA   C 2 49  ? -56.14200 48.80000  35.61500  1.000 72.14123  ? 49   ALA   D CB  1 
ATOM   7370 N N   . ALA   C 2 50  ? -55.93000 46.84000  32.94400  1.000 72.61255  ? 50   ALA   D N   1 
ATOM   7371 C CA  . ALA   C 2 50  ? -55.16500 45.84600  32.20600  1.000 71.81109  ? 50   ALA   D CA  1 
ATOM   7372 C C   . ALA   C 2 50  ? -54.12500 46.54500  31.34700  1.000 72.17599  ? 50   ALA   D C   1 
ATOM   7373 O O   . ALA   C 2 50  ? -54.46100 47.45300  30.57700  1.000 68.14643  ? 50   ALA   D O   1 
ATOM   7374 C CB  . ALA   C 2 50  ? -56.07800 44.97600  31.33400  1.000 72.02272  ? 50   ALA   D CB  1 
ATOM   7375 N N   . ILE   C 2 51  ? -52.86900 46.12500  31.48900  1.000 72.20317  ? 51   ILE   D N   1 
ATOM   7376 C CA  . ILE   C 2 51  ? -51.76200 46.59500  30.66100  1.000 65.11611  ? 51   ILE   D CA  1 
ATOM   7377 C C   . ILE   C 2 51  ? -51.36900 45.47000  29.70900  1.000 57.78441  ? 51   ILE   D C   1 
ATOM   7378 O O   . ILE   C 2 51  ? -50.95700 44.38600  30.14300  1.000 57.99570  ? 51   ILE   D O   1 
ATOM   7379 C CB  . ILE   C 2 51  ? -50.56900 47.06200  31.51300  1.000 64.00605  ? 51   ILE   D CB  1 
ATOM   7380 C CG1 . ILE   C 2 51  ? -49.41700 47.52400  30.62300  1.000 67.10787  ? 51   ILE   D CG1 1 
ATOM   7381 C CG2 . ILE   C 2 51  ? -50.10400 45.98100  32.49300  1.000 58.47776  ? 51   ILE   D CG2 1 
ATOM   7382 C CD1 . ILE   C 2 51  ? -49.61800 48.84400  29.97800  1.000 69.84446  ? 51   ILE   D CD1 1 
ATOM   7383 N N   . THR   C 2 52  ? -51.51100 45.71500  28.41200  1.000 59.14033  ? 52   THR   D N   1 
ATOM   7384 C CA  . THR   C 2 52  ? -51.18700 44.65800  27.47200  1.000 59.42994  ? 52   THR   D CA  1 
ATOM   7385 C C   . THR   C 2 52  ? -49.67600 44.58700  27.27800  1.000 59.77580  ? 52   THR   D C   1 
ATOM   7386 O O   . THR   C 2 52  ? -48.92000 45.44600  27.74300  1.000 61.09805  ? 52   THR   D O   1 
ATOM   7387 C CB  . THR   C 2 52  ? -51.89300 44.87500  26.13800  1.000 50.45738  ? 52   THR   D CB  1 
ATOM   7388 O OG1 . THR   C 2 52  ? -51.86600 43.65400  25.39100  1.000 52.77147  ? 52   THR   D OG1 1 
ATOM   7389 C CG2 . THR   C 2 52  ? -51.17800 45.93400  25.33500  1.000 53.06352  ? 52   THR   D CG2 1 
ATOM   7390 N N   . SER   C 2 53  ? -49.23400 43.53600  26.58400  1.000 57.25424  ? 53   SER   D N   1 
ATOM   7391 C CA  . SER   C 2 53  ? -47.80100 43.30800  26.42600  1.000 56.15216  ? 53   SER   D CA  1 
ATOM   7392 C C   . SER   C 2 53  ? -47.14000 44.44900  25.66800  1.000 53.60941  ? 53   SER   D C   1 
ATOM   7393 O O   . SER   C 2 53  ? -46.01900 44.85600  25.99600  1.000 45.64127  ? 53   SER   D O   1 
ATOM   7394 C CB  . SER   C 2 53  ? -47.55500 41.98100  25.71400  1.000 47.83569  ? 53   SER   D CB  1 
ATOM   7395 O OG  . SER   C 2 53  ? -46.17000 41.70300  25.66500  1.000 47.56762  ? 53   SER   D OG  1 
ATOM   7396 N N   . GLY   C 2 54  ? -47.82100 44.97700  24.65100  1.000 57.74882  ? 54   GLY   D N   1 
ATOM   7397 C CA  . GLY   C 2 54  ? -47.29700 46.10600  23.90700  1.000 55.73390  ? 54   GLY   D CA  1 
ATOM   7398 C C   . GLY   C 2 54  ? -47.30100 47.41000  24.67400  1.000 61.60210  ? 54   GLY   D C   1 
ATOM   7399 O O   . GLY   C 2 54  ? -46.58300 48.33900  24.29400  1.000 65.10228  ? 54   GLY   D O   1 
ATOM   7400 N N   . GLY   C 2 55  ? -48.09300 47.50400  25.73800  1.000 66.45242  ? 55   GLY   D N   1 
ATOM   7401 C CA  . GLY   C 2 55  ? -48.15100 48.71000  26.55100  1.000 67.04189  ? 55   GLY   D CA  1 
ATOM   7402 C C   . GLY   C 2 55  ? -49.48900 49.42700  26.55900  1.000 71.25052  ? 55   GLY   D C   1 
ATOM   7403 O O   . GLY   C 2 55  ? -49.61500 50.44400  27.25500  1.000 78.62880  ? 55   GLY   D O   1 
ATOM   7404 N N   . SER   C 2 56  ? -50.49900 48.96800  25.82500  1.000 64.21584  ? 56   SER   D N   1 
ATOM   7405 C CA  . SER   C 2 56  ? -51.80500 49.60900  25.86900  1.000 66.39077  ? 56   SER   D CA  1 
ATOM   7406 C C   . SER   C 2 56  ? -52.47100 49.37700  27.22300  1.000 71.12253  ? 56   SER   D C   1 
ATOM   7407 O O   . SER   C 2 56  ? -52.21200 48.38200  27.90600  1.000 70.14480  ? 56   SER   D O   1 
ATOM   7408 C CB  . SER   C 2 56  ? -52.69300 49.08000  24.74400  1.000 71.02807  ? 56   SER   D CB  1 
ATOM   7409 O OG  . SER   C 2 56  ? -51.92900 48.83000  23.57600  1.000 77.61751  ? 56   SER   D OG  1 
ATOM   7410 N N   . THR   C 2 57  ? -53.33700 50.31500  27.61200  1.000 72.21512  ? 57   THR   D N   1 
ATOM   7411 C CA  . THR   C 2 57  ? -53.98000 50.29300  28.92000  1.000 80.14087  ? 57   THR   D CA  1 
ATOM   7412 C C   . THR   C 2 57  ? -55.49400 50.38300  28.77600  1.000 79.93835  ? 57   THR   D C   1 
ATOM   7413 O O   . THR   C 2 57  ? -56.00500 51.13000  27.93600  1.000 77.44393  ? 57   THR   D O   1 
ATOM   7414 C CB  . THR   C 2 57  ? -53.49600 51.45000  29.81100  1.000 79.03252  ? 57   THR   D CB  1 
ATOM   7415 O OG1 . THR   C 2 57  ? -53.43400 52.65600  29.04000  1.000 89.09173  ? 57   THR   D OG1 1 
ATOM   7416 C CG2 . THR   C 2 57  ? -52.13100 51.15400  30.39200  1.000 65.29103  ? 57   THR   D CG2 1 
ATOM   7417 N N   . LYS   C 2 58  ? -56.20400 49.62300  29.60700  1.000 76.95351  ? 58   LYS   D N   1 
ATOM   7418 C CA  . LYS   C 2 58  ? -57.65600 49.69700  29.70100  1.000 82.05752  ? 58   LYS   D CA  1 
ATOM   7419 C C   . LYS   C 2 58  ? -58.04200 49.78700  31.16900  1.000 81.94516  ? 58   LYS   D C   1 
ATOM   7420 O O   . LYS   C 2 58  ? -57.46500 49.09300  32.01100  1.000 79.43016  ? 58   LYS   D O   1 
ATOM   7421 C CB  . LYS   C 2 58  ? -58.33400 48.48400  29.05000  1.000 72.39133  ? 58   LYS   D CB  1 
ATOM   7422 N N   . TYR   C 2 59  ? -59.01500 50.64700  31.47200  1.000 76.89558  ? 59   TYR   D N   1 
ATOM   7423 C CA  . TYR   C 2 59  ? -59.43000 50.90800  32.84100  1.000 76.00807  ? 59   TYR   D CA  1 
ATOM   7424 C C   . TYR   C 2 59  ? -60.93800 50.75200  32.96100  1.000 82.09027  ? 59   TYR   D C   1 
ATOM   7425 O O   . TYR   C 2 59  ? -61.68600 51.07200  32.03300  1.000 88.82975  ? 59   TYR   D O   1 
ATOM   7426 C CB  . TYR   C 2 59  ? -59.01900 52.31800  33.29000  1.000 75.23651  ? 59   TYR   D CB  1 
ATOM   7427 C CG  . TYR   C 2 59  ? -57.52600 52.49900  33.41700  1.000 78.15852  ? 59   TYR   D CG  1 
ATOM   7428 C CD1 . TYR   C 2 59  ? -56.83100 51.98000  34.50100  1.000 74.45547  ? 59   TYR   D CD1 1 
ATOM   7429 C CD2 . TYR   C 2 59  ? -56.80900 53.18500  32.44900  1.000 78.91141  ? 59   TYR   D CD2 1 
ATOM   7430 C CE1 . TYR   C 2 59  ? -55.46400 52.13900  34.61600  1.000 71.06849  ? 59   TYR   D CE1 1 
ATOM   7431 C CE2 . TYR   C 2 59  ? -55.44500 53.35100  32.55700  1.000 77.43080  ? 59   TYR   D CE2 1 
ATOM   7432 C CZ  . TYR   C 2 59  ? -54.77800 52.82700  33.64200  1.000 78.53707  ? 59   TYR   D CZ  1 
ATOM   7433 O OH  . TYR   C 2 59  ? -53.41700 52.99100  33.74200  1.000 91.31958  ? 59   TYR   D OH  1 
ATOM   7434 N N   . ALA   C 2 60  ? -61.37900 50.25500  34.11500  1.000 85.32589  ? 60   ALA   D N   1 
ATOM   7435 C CA  . ALA   C 2 60  ? -62.80800 50.12600  34.37300  1.000 89.88091  ? 60   ALA   D CA  1 
ATOM   7436 C C   . ALA   C 2 60  ? -63.45200 51.50400  34.46900  1.000 91.31202  ? 60   ALA   D C   1 
ATOM   7437 O O   . ALA   C 2 60  ? -62.85000 52.45300  34.97800  1.000 95.64180  ? 60   ALA   D O   1 
ATOM   7438 C CB  . ALA   C 2 60  ? -63.05300 49.33500  35.65800  1.000 80.79203  ? 60   ALA   D CB  1 
ATOM   7439 N N   . ASP   C 2 61  ? -64.68600 51.61200  33.96700  1.000 91.49135  ? 61   ASP   D N   1 
ATOM   7440 C CA  . ASP   C 2 61  ? -65.36400 52.90600  33.93800  1.000 91.90307  ? 61   ASP   D CA  1 
ATOM   7441 C C   . ASP   C 2 61  ? -65.56700 53.46100  35.34200  1.000 87.94475  ? 61   ASP   D C   1 
ATOM   7442 O O   . ASP   C 2 61  ? -65.36100 54.65700  35.58100  1.000 82.97197  ? 61   ASP   D O   1 
ATOM   7443 C CB  . ASP   C 2 61  ? -66.70700 52.78300  33.21700  1.000 101.32479 ? 61   ASP   D CB  1 
ATOM   7444 C CG  . ASP   C 2 61  ? -66.58500 52.96500  31.71700  1.000 102.92173 ? 61   ASP   D CG  1 
ATOM   7445 O OD1 . ASP   C 2 61  ? -65.78900 53.82400  31.28300  1.000 102.54411 ? 61   ASP   D OD1 1 
ATOM   7446 O OD2 . ASP   C 2 61  ? -67.29300 52.25400  30.97200  1.000 111.25411 ? 61   ASP   D OD2 1 
ATOM   7447 N N   . SER   C 2 62  ? -65.96300 52.60600  36.28800  1.000 91.41672  ? 62   SER   D N   1 
ATOM   7448 C CA  . SER   C 2 62  ? -66.20900 53.05200  37.65500  1.000 89.62151  ? 62   SER   D CA  1 
ATOM   7449 C C   . SER   C 2 62  ? -64.95500 53.57500  38.34300  1.000 89.15165  ? 62   SER   D C   1 
ATOM   7450 O O   . SER   C 2 62  ? -65.05900 54.13200  39.44200  1.000 92.00585  ? 62   SER   D O   1 
ATOM   7451 C CB  . SER   C 2 62  ? -66.80700 51.90900  38.48200  1.000 88.95394  ? 62   SER   D CB  1 
ATOM   7452 O OG  . SER   C 2 62  ? -65.84600 50.89800  38.73500  1.000 84.11856  ? 62   SER   D OG  1 
ATOM   7453 N N   . VAL   C 2 63  ? -63.78100 53.40900  37.73300  1.000 83.44901  ? 63   VAL   D N   1 
ATOM   7454 C CA  . VAL   C 2 63  ? -62.52100 53.80000  38.35400  1.000 80.68219  ? 63   VAL   D CA  1 
ATOM   7455 C C   . VAL   C 2 63  ? -61.63800 54.53600  37.35100  1.000 85.46609  ? 63   VAL   D C   1 
ATOM   7456 O O   . VAL   C 2 63  ? -60.42900 54.68300  37.56700  1.000 84.01874  ? 63   VAL   D O   1 
ATOM   7457 C CB  . VAL   C 2 63  ? -61.79100 52.57100  38.92800  1.000 77.13368  ? 63   VAL   D CB  1 
ATOM   7458 C CG1 . VAL   C 2 63  ? -62.67100 51.82400  39.92200  1.000 80.47808  ? 63   VAL   D CG1 1 
ATOM   7459 C CG2 . VAL   C 2 63  ? -61.33800 51.64700  37.81100  1.000 80.99281  ? 63   VAL   D CG2 1 
ATOM   7460 N N   . LYS   C 2 64  ? -62.23200 55.01100  36.25600  1.000 88.82614  ? 64   LYS   D N   1 
ATOM   7461 C CA  . LYS   C 2 64  ? -61.45900 55.67800  35.21500  1.000 90.86474  ? 64   LYS   D CA  1 
ATOM   7462 C C   . LYS   C 2 64  ? -60.95900 57.03500  35.69700  1.000 92.08670  ? 64   LYS   D C   1 
ATOM   7463 O O   . LYS   C 2 64  ? -61.67600 57.77600  36.37600  1.000 90.15493  ? 64   LYS   D O   1 
ATOM   7464 C CB  . LYS   C 2 64  ? -62.30000 55.85000  33.95000  1.000 81.28809  ? 64   LYS   D CB  1 
ATOM   7465 N N   . GLY   C 2 65  ? -59.71800 57.36000  35.33800  1.000 90.45195  ? 65   GLY   D N   1 
ATOM   7466 C CA  . GLY   C 2 65  ? -59.11600 58.59700  35.78900  1.000 90.22492  ? 65   GLY   D CA  1 
ATOM   7467 C C   . GLY   C 2 65  ? -58.68600 58.60600  37.23700  1.000 94.83057  ? 65   GLY   D C   1 
ATOM   7468 O O   . GLY   C 2 65  ? -58.25700 59.65200  37.73400  1.000 98.54940  ? 65   GLY   D O   1 
ATOM   7469 N N   . ARG   C 2 66  ? -58.79000 57.47100  37.93300  1.000 90.27615  ? 66   ARG   D N   1 
ATOM   7470 C CA  . ARG   C 2 66  ? -58.36900 57.36400  39.32000  1.000 80.69805  ? 66   ARG   D CA  1 
ATOM   7471 C C   . ARG   C 2 66  ? -57.38300 56.22800  39.55500  1.000 80.50078  ? 66   ARG   D C   1 
ATOM   7472 O O   . ARG   C 2 66  ? -57.01700 55.97700  40.70900  1.000 85.65777  ? 66   ARG   D O   1 
ATOM   7473 C CB  . ARG   C 2 66  ? -59.58800 57.16200  40.23600  1.000 85.20554  ? 66   ARG   D CB  1 
ATOM   7474 C CG  . ARG   C 2 66  ? -60.65900 58.23300  40.11200  1.000 84.91550  ? 66   ARG   D CG  1 
ATOM   7475 C CD  . ARG   C 2 66  ? -61.74500 58.06600  41.17000  1.000 78.44189  ? 66   ARG   D CD  1 
ATOM   7476 N NE  . ARG   C 2 66  ? -62.42000 56.77400  41.09200  1.000 80.22950  ? 66   ARG   D NE  1 
ATOM   7477 C CZ  . ARG   C 2 66  ? -62.21900 55.76700  41.93300  1.000 80.32270  ? 66   ARG   D CZ  1 
ATOM   7478 N NH1 . ARG   C 2 66  ? -61.36600 55.86600  42.93900  1.000 79.03627  ? 66   ARG   D NH1 1 
ATOM   7479 N NH2 . ARG   C 2 66  ? -62.89400 54.63400  41.76200  1.000 79.32412  ? 66   ARG   D NH2 1 
ATOM   7480 N N   . PHE   C 2 67  ? -56.97300 55.51400  38.51000  1.000 80.97797  ? 67   PHE   D N   1 
ATOM   7481 C CA  . PHE   C 2 67  ? -56.11200 54.34700  38.63200  1.000 82.84034  ? 67   PHE   D CA  1 
ATOM   7482 C C   . PHE   C 2 67  ? -55.15200 54.32700  37.45200  1.000 81.71712  ? 67   PHE   D C   1 
ATOM   7483 O O   . PHE   C 2 67  ? -55.52900 54.67700  36.33000  1.000 83.40001  ? 67   PHE   D O   1 
ATOM   7484 C CB  . PHE   C 2 67  ? -56.93000 53.04300  38.67400  1.000 83.80935  ? 67   PHE   D CB  1 
ATOM   7485 C CG  . PHE   C 2 67  ? -57.72900 52.85200  39.94300  1.000 86.72724  ? 67   PHE   D CG  1 
ATOM   7486 C CD1 . PHE   C 2 67  ? -58.86600 53.60400  40.18900  1.000 83.98117  ? 67   PHE   D CD1 1 
ATOM   7487 C CD2 . PHE   C 2 67  ? -57.36900 51.88500  40.86700  1.000 87.02896  ? 67   PHE   D CD2 1 
ATOM   7488 C CE1 . PHE   C 2 67  ? -59.60100 53.43100  41.34700  1.000 80.52694  ? 67   PHE   D CE1 1 
ATOM   7489 C CE2 . PHE   C 2 67  ? -58.11400 51.69700  42.01900  1.000 81.98878  ? 67   PHE   D CE2 1 
ATOM   7490 C CZ  . PHE   C 2 67  ? -59.22600 52.47300  42.25900  1.000 80.05999  ? 67   PHE   D CZ  1 
ATOM   7491 N N   . THR   C 2 68  ? -53.90300 53.93800  37.71100  1.000 76.00294  ? 68   THR   D N   1 
ATOM   7492 C CA  . THR   C 2 68  ? -52.88100 53.85000  36.67100  1.000 74.01842  ? 68   THR   D CA  1 
ATOM   7493 C C   . THR   C 2 68  ? -52.15700 52.51600  36.79300  1.000 78.21788  ? 68   THR   D C   1 
ATOM   7494 O O   . THR   C 2 68  ? -51.36700 52.31400  37.72300  1.000 75.71287  ? 68   THR   D O   1 
ATOM   7495 C CB  . THR   C 2 68  ? -51.88700 55.01400  36.74700  1.000 83.96189  ? 68   THR   D CB  1 
ATOM   7496 O OG1 . THR   C 2 68  ? -51.00000 54.83100  37.86000  1.000 85.68071  ? 68   THR   D OG1 1 
ATOM   7497 C CG2 . THR   C 2 68  ? -52.60700 56.35600  36.85900  1.000 80.15324  ? 68   THR   D CG2 1 
ATOM   7498 N N   . ILE   C 2 69  ? -52.42600 51.61500  35.85500  1.000 74.61805  ? 69   ILE   D N   1 
ATOM   7499 C CA  . ILE   C 2 69  ? -51.66000 50.38300  35.73000  1.000 73.31202  ? 69   ILE   D CA  1 
ATOM   7500 C C   . ILE   C 2 69  ? -50.35300 50.68400  35.00100  1.000 70.45965  ? 69   ILE   D C   1 
ATOM   7501 O O   . ILE   C 2 69  ? -50.29500 51.55800  34.12800  1.000 68.29135  ? 69   ILE   D O   1 
ATOM   7502 C CB  . ILE   C 2 69  ? -52.50000 49.31000  35.00400  1.000 68.28069  ? 69   ILE   D CB  1 
ATOM   7503 C CG1 . ILE   C 2 69  ? -51.74200 47.99000  34.89600  1.000 62.09570  ? 69   ILE   D CG1 1 
ATOM   7504 C CG2 . ILE   C 2 69  ? -52.93500 49.79500  33.63600  1.000 72.59651  ? 69   ILE   D CG2 1 
ATOM   7505 C CD1 . ILE   C 2 69  ? -51.64600 47.25500  36.17900  1.000 61.73036  ? 69   ILE   D CD1 1 
ATOM   7506 N N   . SER   C 2 70  ? -49.28400 49.98500  35.38400  1.000 68.52649  ? 70   SER   D N   1 
ATOM   7507 C CA  . SER   C 2 70  ? -47.97800 50.18400  34.76300  1.000 65.54344  ? 70   SER   D CA  1 
ATOM   7508 C C   . SER   C 2 70  ? -47.09600 48.98000  35.06000  1.000 66.75695  ? 70   SER   D C   1 
ATOM   7509 O O   . SER   C 2 70  ? -47.32100 48.24500  36.02400  1.000 70.15142  ? 70   SER   D O   1 
ATOM   7510 C CB  . SER   C 2 70  ? -47.30700 51.47400  35.25000  1.000 72.90953  ? 70   SER   D CB  1 
ATOM   7511 O OG  . SER   C 2 70  ? -46.54200 51.24600  36.42200  1.000 76.61078  ? 70   SER   D OG  1 
ATOM   7512 N N   . ARG   C 2 71  ? -46.07800 48.79300  34.22500  1.000 68.57116  ? 71   ARG   D N   1 
ATOM   7513 C CA  . ARG   C 2 71  ? -45.23000 47.61700  34.32500  1.000 67.37622  ? 71   ARG   D CA  1 
ATOM   7514 C C   . ARG   C 2 71  ? -43.77200 48.02700  34.19700  1.000 64.34273  ? 71   ARG   D C   1 
ATOM   7515 O O   . ARG   C 2 71  ? -43.44500 49.06800  33.62400  1.000 67.12747  ? 71   ARG   D O   1 
ATOM   7516 C CB  . ARG   C 2 71  ? -45.57600 46.58200  33.24600  1.000 66.02075  ? 71   ARG   D CB  1 
ATOM   7517 C CG  . ARG   C 2 71  ? -45.68800 47.17200  31.85000  1.000 58.56352  ? 71   ARG   D CG  1 
ATOM   7518 C CD  . ARG   C 2 71  ? -46.36100 46.21100  30.88000  1.000 53.53426  ? 71   ARG   D CD  1 
ATOM   7519 N NE  . ARG   C 2 71  ? -45.71900 44.90500  30.79500  1.000 48.79374  ? 71   ARG   D NE  1 
ATOM   7520 C CZ  . ARG   C 2 71  ? -46.29800 43.82800  30.27900  1.000 47.75310  ? 71   ARG   D CZ  1 
ATOM   7521 N NH1 . ARG   C 2 71  ? -47.52300 43.87500  29.77800  1.000 42.46033  ? 71   ARG   D NH1 1 
ATOM   7522 N NH2 . ARG   C 2 71  ? -45.63600 42.67400  30.27300  1.000 46.49217  ? 71   ARG   D NH2 1 
ATOM   7523 N N   . ASP   C 2 72  ? -42.89600 47.18900  34.74700  1.000 59.32947  ? 72   ASP   D N   1 
ATOM   7524 C CA  . ASP   C 2 72  ? -41.45200 47.30700  34.55700  1.000 61.32543  ? 72   ASP   D CA  1 
ATOM   7525 C C   . ASP   C 2 72  ? -40.93600 45.92300  34.18200  1.000 65.18150  ? 72   ASP   D C   1 
ATOM   7526 O O   . ASP   C 2 72  ? -40.73700 45.07000  35.05300  1.000 58.27536  ? 72   ASP   D O   1 
ATOM   7527 C CB  . ASP   C 2 72  ? -40.75400 47.83400  35.80200  1.000 67.28143  ? 72   ASP   D CB  1 
ATOM   7528 C CG  . ASP   C 2 72  ? -39.25800 47.96000  35.61000  1.000 74.61082  ? 72   ASP   D CG  1 
ATOM   7529 O OD1 . ASP   C 2 72  ? -38.81500 48.98300  35.04700  1.000 82.75907  ? 72   ASP   D OD1 1 
ATOM   7530 O OD2 . ASP   C 2 72  ? -38.52800 47.02500  36.00500  1.000 68.02474  ? 72   ASP   D OD2 1 
ATOM   7531 N N   . ASN   C 2 73  ? -40.72700 45.70200  32.88200  1.000 64.54881  ? 73   ASN   D N   1 
ATOM   7532 C CA  . ASN   C 2 73  ? -40.30700 44.39200  32.40400  1.000 60.64394  ? 73   ASN   D CA  1 
ATOM   7533 C C   . ASN   C 2 73  ? -38.89000 44.03900  32.82000  1.000 57.86743  ? 73   ASN   D C   1 
ATOM   7534 O O   . ASN   C 2 73  ? -38.50700 42.86900  32.71400  1.000 53.23502  ? 73   ASN   D O   1 
ATOM   7535 C CB  . ASN   C 2 73  ? -40.43700 44.32700  30.88400  1.000 51.64696  ? 73   ASN   D CB  1 
ATOM   7536 C CG  . ASN   C 2 73  ? -41.80300 44.76200  30.40400  1.000 60.75489  ? 73   ASN   D CG  1 
ATOM   7537 O OD1 . ASN   C 2 73  ? -42.82500 44.33600  30.94400  1.000 65.49706  ? 73   ASN   D OD1 1 
ATOM   7538 N ND2 . ASN   C 2 73  ? -41.83200 45.62300  29.39400  1.000 62.55213  ? 73   ASN   D ND2 1 
ATOM   7539 N N   . ALA   C 2 74  ? -38.10900 45.01200  33.29100  1.000 65.12650  ? 74   ALA   D N   1 
ATOM   7540 C CA  . ALA   C 2 74  ? -36.78000 44.70900  33.80900  1.000 67.76130  ? 74   ALA   D CA  1 
ATOM   7541 C C   . ALA   C 2 74  ? -36.87200 43.95400  35.12700  1.000 70.65945  ? 74   ALA   D C   1 
ATOM   7542 O O   . ALA   C 2 74  ? -36.20900 42.92600  35.31400  1.000 68.70236  ? 74   ALA   D O   1 
ATOM   7543 C CB  . ALA   C 2 74  ? -35.97700 45.99800  33.98200  1.000 67.14139  ? 74   ALA   D CB  1 
ATOM   7544 N N   . LYS   C 2 75  ? -37.69400 44.44700  36.05000  1.000 69.10787  ? 75   LYS   D N   1 
ATOM   7545 C CA  . LYS   C 2 75  ? -37.86300 43.82600  37.35700  1.000 71.91489  ? 75   LYS   D CA  1 
ATOM   7546 C C   . LYS   C 2 75  ? -38.92800 42.73400  37.36900  1.000 74.04884  ? 75   LYS   D C   1 
ATOM   7547 O O   . LYS   C 2 75  ? -39.19000 42.16600  38.43700  1.000 77.35403  ? 75   LYS   D O   1 
ATOM   7548 C CB  . LYS   C 2 75  ? -38.20500 44.89200  38.40600  1.000 67.48045  ? 75   LYS   D CB  1 
ATOM   7549 N N   . ASN   C 2 76  ? -39.54200 42.43100  36.21800  1.000 60.85979  ? 76   ASN   D N   1 
ATOM   7550 C CA  . ASN   C 2 76  ? -40.54900 41.37000  36.10600  1.000 59.29949  ? 76   ASN   D CA  1 
ATOM   7551 C C   . ASN   C 2 76  ? -41.79300 41.67800  36.93800  1.000 62.69618  ? 76   ASN   D C   1 
ATOM   7552 O O   . ASN   C 2 76  ? -42.40900 40.78100  37.51700  1.000 58.67763  ? 76   ASN   D O   1 
ATOM   7553 C CB  . ASN   C 2 76  ? -39.97000 40.00700  36.50200  1.000 54.69272  ? 76   ASN   D CB  1 
ATOM   7554 C CG  . ASN   C 2 76  ? -39.13600 39.38200  35.40700  1.000 61.31503  ? 76   ASN   D CG  1 
ATOM   7555 O OD1 . ASN   C 2 76  ? -39.66900 38.79100  34.46900  1.000 64.14857  ? 76   ASN   D OD1 1 
ATOM   7556 N ND2 . ASN   C 2 76  ? -37.81800 39.51300  35.51500  1.000 68.31101  ? 76   ASN   D ND2 1 
ATOM   7557 N N   . THR   C 2 77  ? -42.17500 42.95400  37.00600  1.000 58.43094  ? 77   THR   D N   1 
ATOM   7558 C CA  . THR   C 2 77  ? -43.28700 43.35800  37.85400  1.000 61.43221  ? 77   THR   D CA  1 
ATOM   7559 C C   . THR   C 2 77  ? -44.25100 44.26900  37.10600  1.000 59.95234  ? 77   THR   D C   1 
ATOM   7560 O O   . THR   C 2 77  ? -43.91900 44.86400  36.07800  1.000 59.45375  ? 77   THR   D O   1 
ATOM   7561 C CB  . THR   C 2 77  ? -42.81900 44.07000  39.14000  1.000 71.32234  ? 77   THR   D CB  1 
ATOM   7562 O OG1 . THR   C 2 77  ? -42.31300 45.37300  38.82000  1.000 72.83199  ? 77   THR   D OG1 1 
ATOM   7563 C CG2 . THR   C 2 77  ? -41.75700 43.25600  39.87300  1.000 62.72485  ? 77   THR   D CG2 1 
ATOM   7564 N N   . VAL   C 2 78  ? -45.45900 44.36500  37.66000  1.000 66.49397  ? 78   VAL   D N   1 
ATOM   7565 C CA  . VAL   C 2 78  ? -46.51900 45.23500  37.17000  1.000 66.60438  ? 78   VAL   D CA  1 
ATOM   7566 C C   . VAL   C 2 78  ? -47.09500 45.99800  38.35900  1.000 71.15055  ? 78   VAL   D C   1 
ATOM   7567 O O   . VAL   C 2 78  ? -47.25300 45.43700  39.45100  1.000 59.82864  ? 78   VAL   D O   1 
ATOM   7568 C CB  . VAL   C 2 78  ? -47.60600 44.42500  36.42700  1.000 59.68519  ? 78   VAL   D CB  1 
ATOM   7569 C CG1 . VAL   C 2 78  ? -48.08500 43.25500  37.27800  1.000 55.84573  ? 78   VAL   D CG1 1 
ATOM   7570 C CG2 . VAL   C 2 78  ? -48.76500 45.31300  36.01900  1.000 52.80427  ? 78   VAL   D CG2 1 
ATOM   7571 N N   . TYR   C 2 79  ? -47.38700 47.28400  38.15500  1.000 70.47968  ? 79   TYR   D N   1 
ATOM   7572 C CA  . TYR   C 2 79  ? -47.79400 48.18300  39.22500  1.000 67.59653  ? 79   TYR   D CA  1 
ATOM   7573 C C   . TYR   C 2 79  ? -49.15400 48.79900  38.92600  1.000 73.10032  ? 79   TYR   D C   1 
ATOM   7574 O O   . TYR   C 2 79  ? -49.52200 49.00500  37.76600  1.000 69.86933  ? 79   TYR   D O   1 
ATOM   7575 C CB  . TYR   C 2 79  ? -46.78100 49.31800  39.42800  1.000 75.19530  ? 79   TYR   D CB  1 
ATOM   7576 C CG  . TYR   C 2 79  ? -45.36200 48.86500  39.67100  1.000 79.26838  ? 79   TYR   D CG  1 
ATOM   7577 C CD1 . TYR   C 2 79  ? -45.04800 48.05000  40.74900  1.000 79.74804  ? 79   TYR   D CD1 1 
ATOM   7578 C CD2 . TYR   C 2 79  ? -44.33000 49.27400  38.83300  1.000 70.22941  ? 79   TYR   D CD2 1 
ATOM   7579 C CE1 . TYR   C 2 79  ? -43.75000 47.63900  40.97700  1.000 82.57276  ? 79   TYR   D CE1 1 
ATOM   7580 C CE2 . TYR   C 2 79  ? -43.03000 48.87100  39.05500  1.000 67.28878  ? 79   TYR   D CE2 1 
ATOM   7581 C CZ  . TYR   C 2 79  ? -42.74600 48.05400  40.12900  1.000 79.09166  ? 79   TYR   D CZ  1 
ATOM   7582 O OH  . TYR   C 2 79  ? -41.45300 47.64500  40.35900  1.000 90.55203  ? 79   TYR   D OH  1 
ATOM   7583 N N   . LEU   C 2 80  ? -49.88900 49.11400  39.99400  1.000 80.64551  ? 80   LEU   D N   1 
ATOM   7584 C CA  . LEU   C 2 80  ? -51.16400 49.82000  39.89200  1.000 76.29055  ? 80   LEU   D CA  1 
ATOM   7585 C C   . LEU   C 2 80  ? -51.19500 50.89600  40.96800  1.000 79.41130  ? 80   LEU   D C   1 
ATOM   7586 O O   . LEU   C 2 80  ? -51.22200 50.57800  42.16100  1.000 76.46390  ? 80   LEU   D O   1 
ATOM   7587 C CB  . LEU   C 2 80  ? -52.35000 48.86500  40.04900  1.000 70.87909  ? 80   LEU   D CB  1 
ATOM   7588 C CG  . LEU   C 2 80  ? -53.73900 49.49100  39.87800  1.000 76.34285  ? 80   LEU   D CG  1 
ATOM   7589 C CD1 . LEU   C 2 80  ? -54.49300 48.84600  38.73000  1.000 76.64964  ? 80   LEU   D CD1 1 
ATOM   7590 C CD2 . LEU   C 2 80  ? -54.53500 49.38700  41.15700  1.000 69.97941  ? 80   LEU   D CD2 1 
ATOM   7591 N N   . GLN   C 2 81  ? -51.19000 52.16300  40.55100  1.000 82.57740  ? 81   GLN   D N   1 
ATOM   7592 C CA  . GLN   C 2 81  ? -51.25100 53.30400  41.46600  1.000 81.51176  ? 81   GLN   D CA  1 
ATOM   7593 C C   . GLN   C 2 81  ? -52.70100 53.76400  41.58300  1.000 80.93898  ? 81   GLN   D C   1 
ATOM   7594 O O   . GLN   C 2 81  ? -53.16200 54.62600  40.83300  1.000 77.59134  ? 81   GLN   D O   1 
ATOM   7595 C CB  . GLN   C 2 81  ? -50.35500 54.44200  40.98800  1.000 85.22494  ? 81   GLN   D CB  1 
ATOM   7596 C CG  . GLN   C 2 81  ? -48.86200 54.26500  41.23900  1.000 90.85715  ? 81   GLN   D CG  1 
ATOM   7597 C CD  . GLN   C 2 81  ? -48.46100 54.68300  42.64100  1.000 94.51690  ? 81   GLN   D CD  1 
ATOM   7598 O OE1 . GLN   C 2 81  ? -47.36900 54.35800  43.11300  1.000 103.94008 ? 81   GLN   D OE1 1 
ATOM   7599 N NE2 . GLN   C 2 81  ? -49.35500 55.38700  43.32600  1.000 85.86317  ? 81   GLN   D NE2 1 
ATOM   7600 N N   . MET   C 2 82  ? -53.42600 53.19100  42.53900  1.000 81.23261  ? 82   MET   D N   1 
ATOM   7601 C CA  . MET   C 2 82  ? -54.73600 53.72800  42.88200  1.000 82.28526  ? 82   MET   D CA  1 
ATOM   7602 C C   . MET   C 2 82  ? -54.58600 55.05200  43.62400  1.000 84.21649  ? 82   MET   D C   1 
ATOM   7603 O O   . MET   C 2 82  ? -53.88800 55.13100  44.64000  1.000 79.79180  ? 82   MET   D O   1 
ATOM   7604 C CB  . MET   C 2 82  ? -55.52100 52.73700  43.74500  1.000 81.09045  ? 82   MET   D CB  1 
ATOM   7605 C CG  . MET   C 2 82  ? -54.68900 51.92000  44.71400  1.000 88.22946  ? 82   MET   D CG  1 
ATOM   7606 S SD  . MET   C 2 82  ? -55.62500 50.63400  45.57200  1.000 100.15818 ? 82   MET   D SD  1 
ATOM   7607 C CE  . MET   C 2 82  ? -56.15300 49.58200  44.22000  1.000 76.79417  ? 82   MET   D CE  1 
ATOM   7608 N N   . ASN   C 2 83  ? -55.23500 56.09600  43.11500  1.000 86.94043  ? 83   ASN   D N   1 
ATOM   7609 C CA  . ASN   C 2 83  ? -55.38600 57.33900  43.85500  1.000 85.90714  ? 83   ASN   D CA  1 
ATOM   7610 C C   . ASN   C 2 83  ? -56.86400 57.69300  43.96700  1.000 88.02657  ? 83   ASN   D C   1 
ATOM   7611 O O   . ASN   C 2 83  ? -57.70900 57.16400  43.24000  1.000 85.38874  ? 83   ASN   D O   1 
ATOM   7612 C CB  . ASN   C 2 83  ? -54.62000 58.50900  43.21300  1.000 81.08535  ? 83   ASN   D CB  1 
ATOM   7613 C CG  . ASN   C 2 83  ? -55.11200 58.84300  41.81800  1.000 95.36277  ? 83   ASN   D CG  1 
ATOM   7614 O OD1 . ASN   C 2 83  ? -55.36600 57.95900  41.00600  1.000 99.13830  ? 83   ASN   D OD1 1 
ATOM   7615 N ND2 . ASN   C 2 83  ? -55.28100 60.13300  41.54500  1.000 97.68742  ? 83   ASN   D ND2 1 
ATOM   7616 N N   . SER   C 2 84  ? -57.15900 58.59500  44.90700  1.000 94.13322  ? 84   SER   D N   1 
ATOM   7617 C CA  . SER   C 2 84  ? -58.51900 59.08500  45.15000  1.000 90.81568  ? 84   SER   D CA  1 
ATOM   7618 C C   . SER   C 2 84  ? -59.46700 57.93700  45.50500  1.000 89.44383  ? 84   SER   D C   1 
ATOM   7619 O O   . SER   C 2 84  ? -60.57800 57.83000  44.98300  1.000 86.78757  ? 84   SER   D O   1 
ATOM   7620 C CB  . SER   C 2 84  ? -59.03500 59.88400  43.94600  1.000 86.33689  ? 84   SER   D CB  1 
ATOM   7621 O OG  . SER   C 2 84  ? -60.45100 59.95100  43.92300  1.000 87.89736  ? 84   SER   D OG  1 
ATOM   7622 N N   . LEU   C 2 85  ? -59.01200 57.07700  46.41700  1.000 86.92958  ? 85   LEU   D N   1 
ATOM   7623 C CA  . LEU   C 2 85  ? -59.78600 55.90800  46.81700  1.000 90.03419  ? 85   LEU   D CA  1 
ATOM   7624 C C   . LEU   C 2 85  ? -61.12900 56.30700  47.42500  1.000 91.77596  ? 85   LEU   D C   1 
ATOM   7625 O O   . LEU   C 2 85  ? -61.22100 57.25200  48.21300  1.000 94.14477  ? 85   LEU   D O   1 
ATOM   7626 C CB  . LEU   C 2 85  ? -58.98200 55.07200  47.81400  1.000 87.06595  ? 85   LEU   D CB  1 
ATOM   7627 C CG  . LEU   C 2 85  ? -57.68400 54.43200  47.32400  1.000 78.88761  ? 85   LEU   D CG  1 
ATOM   7628 C CD1 . LEU   C 2 85  ? -56.93500 53.79000  48.48100  1.000 85.85766  ? 85   LEU   D CD1 1 
ATOM   7629 C CD2 . LEU   C 2 85  ? -57.99900 53.39800  46.26400  1.000 77.48709  ? 85   LEU   D CD2 1 
ATOM   7630 N N   . LYS   C 2 86  ? -62.17400 55.57600  47.04800  1.000 88.80887  ? 86   LYS   D N   1 
ATOM   7631 C CA  . LYS   C 2 86  ? -63.52700 55.76600  47.54900  1.000 91.09483  ? 86   LYS   D CA  1 
ATOM   7632 C C   . LYS   C 2 86  ? -63.93900 54.54500  48.36700  1.000 94.81475  ? 86   LYS   D C   1 
ATOM   7633 O O   . LYS   C 2 86  ? -63.31600 53.48400  48.29000  1.000 95.51204  ? 86   LYS   D O   1 
ATOM   7634 C CB  . LYS   C 2 86  ? -64.50300 55.99700  46.38200  1.000 95.01474  ? 86   LYS   D CB  1 
ATOM   7635 C CG  . LYS   C 2 86  ? -65.95000 56.35300  46.75100  1.000 95.76788  ? 86   LYS   D CG  1 
ATOM   7636 C CD  . LYS   C 2 86  ? -66.02900 57.39700  47.86300  1.000 97.86502  ? 86   LYS   D CD  1 
ATOM   7637 C CE  . LYS   C 2 86  ? -67.40900 57.40400  48.51000  1.000 96.40173  ? 86   LYS   D CE  1 
ATOM   7638 N NZ  . LYS   C 2 86  ? -67.33800 57.57700  49.98900  1.000 73.72008  ? 86   LYS   D NZ  1 
ATOM   7639 N N   . ALA   C 2 87  ? -64.99700 54.71000  49.16700  1.000 99.39784  ? 87   ALA   D N   1 
ATOM   7640 C CA  . ALA   C 2 87  ? -65.53500 53.59300  49.93900  1.000 96.06153  ? 87   ALA   D CA  1 
ATOM   7641 C C   . ALA   C 2 87  ? -65.97600 52.43800  49.04500  1.000 95.49854  ? 87   ALA   D C   1 
ATOM   7642 O O   . ALA   C 2 87  ? -66.00700 51.28700  49.49500  1.000 90.63848  ? 87   ALA   D O   1 
ATOM   7643 C CB  . ALA   C 2 87  ? -66.70700 54.07100  50.79900  1.000 93.86781  ? 87   ALA   D CB  1 
ATOM   7644 N N   . GLU   C 2 88  ? -66.31800 52.71800  47.78200  1.000 97.44115  ? 88   GLU   D N   1 
ATOM   7645 C CA  . GLU   C 2 88  ? -66.77400 51.65900  46.88500  1.000 97.42098  ? 88   GLU   D CA  1 
ATOM   7646 C C   . GLU   C 2 88  ? -65.62800 50.77000  46.41400  1.000 89.37309  ? 88   GLU   D C   1 
ATOM   7647 O O   . GLU   C 2 88  ? -65.85500 49.60700  46.06200  1.000 92.41899  ? 88   GLU   D O   1 
ATOM   7648 C CB  . GLU   C 2 88  ? -67.48500 52.25800  45.67100  1.000 99.05172  ? 88   GLU   D CB  1 
ATOM   7649 C CG  . GLU   C 2 88  ? -68.36000 53.46100  45.96600  1.000 103.60388 ? 88   GLU   D CG  1 
ATOM   7650 C CD  . GLU   C 2 88  ? -68.77200 54.19700  44.70300  1.000 115.21276 ? 88   GLU   D CD  1 
ATOM   7651 O OE1 . GLU   C 2 88  ? -67.99700 54.17700  43.72000  1.000 114.90272 ? 88   GLU   D OE1 1 
ATOM   7652 O OE2 . GLU   C 2 88  ? -69.87000 54.79300  44.69200  1.000 119.44655 ? 88   GLU   D OE2 1 
ATOM   7653 N N   . ASP   C 2 89  ? -64.40000 51.29200  46.38900  1.000 84.60006  ? 89   ASP   D N   1 
ATOM   7654 C CA  . ASP   C 2 89  ? -63.26800 50.54800  45.84700  1.000 83.92014  ? 89   ASP   D CA  1 
ATOM   7655 C C   . ASP   C 2 89  ? -62.84200 49.37400  46.72100  1.000 83.95447  ? 89   ASP   D C   1 
ATOM   7656 O O   . ASP   C 2 89  ? -62.04500 48.54900  46.26100  1.000 84.90919  ? 89   ASP   D O   1 
ATOM   7657 C CB  . ASP   C 2 89  ? -62.07400 51.48500  45.63800  1.000 80.82923  ? 89   ASP   D CB  1 
ATOM   7658 C CG  . ASP   C 2 89  ? -62.22000 52.35000  44.39800  1.000 85.43221  ? 89   ASP   D CG  1 
ATOM   7659 O OD1 . ASP   C 2 89  ? -62.90600 51.92100  43.44500  1.000 86.30525  ? 89   ASP   D OD1 1 
ATOM   7660 O OD2 . ASP   C 2 89  ? -61.64900 53.46200  44.37600  1.000 81.48355  ? 89   ASP   D OD2 1 
ATOM   7661 N N   . THR   C 2 90  ? -63.35100 49.27900  47.95100  1.000 83.00120  ? 90   THR   D N   1 
ATOM   7662 C CA  . THR   C 2 90  ? -62.92800 48.23700  48.88300  1.000 83.40367  ? 90   THR   D CA  1 
ATOM   7663 C C   . THR   C 2 90  ? -63.22200 46.84700  48.33000  1.000 83.25350  ? 90   THR   D C   1 
ATOM   7664 O O   . THR   C 2 90  ? -64.38400 46.49400  48.10500  1.000 79.03152  ? 90   THR   D O   1 
ATOM   7665 C CB  . THR   C 2 90  ? -63.63200 48.42600  50.22400  1.000 82.32291  ? 90   THR   D CB  1 
ATOM   7666 O OG1 . THR   C 2 90  ? -63.12300 49.59700  50.87400  1.000 81.48621  ? 90   THR   D OG1 1 
ATOM   7667 C CG2 . THR   C 2 90  ? -63.41300 47.21100  51.10900  1.000 81.84420  ? 90   THR   D CG2 1 
ATOM   7668 N N   . ALA   C 2 91  ? -62.16700 46.05700  48.13200  1.000 85.43260  ? 91   ALA   D N   1 
ATOM   7669 C CA  . ALA   C 2 91  ? -62.27600 44.71600  47.56000  1.000 81.39331  ? 91   ALA   D CA  1 
ATOM   7670 C C   . ALA   C 2 91  ? -60.94100 43.99800  47.74300  1.000 77.38047  ? 91   ALA   D C   1 
ATOM   7671 O O   . ALA   C 2 91  ? -59.96400 44.57100  48.23600  1.000 76.12450  ? 91   ALA   D O   1 
ATOM   7672 C CB  . ALA   C 2 91  ? -62.67300 44.76800  46.08400  1.000 77.69448  ? 91   ALA   D CB  1 
ATOM   7673 N N   . VAL   C 2 92  ? -60.91300 42.72900  47.33800  1.000 76.02414  ? 92   VAL   D N   1 
ATOM   7674 C CA  . VAL   C 2 92  ? -59.69500 41.92500  47.30200  1.000 79.32992  ? 92   VAL   D CA  1 
ATOM   7675 C C   . VAL   C 2 92  ? -59.14300 41.98000  45.88200  1.000 78.63767  ? 92   VAL   D C   1 
ATOM   7676 O O   . VAL   C 2 92  ? -59.83500 41.61700  44.92200  1.000 68.59079  ? 92   VAL   D O   1 
ATOM   7677 C CB  . VAL   C 2 92  ? -59.96200 40.47400  47.73800  1.000 70.85825  ? 92   VAL   D CB  1 
ATOM   7678 C CG1 . VAL   C 2 92  ? -58.66600 39.78600  48.14600  1.000 64.64904  ? 92   VAL   D CG1 1 
ATOM   7679 C CG2 . VAL   C 2 92  ? -60.96700 40.43800  48.88200  1.000 68.46677  ? 92   VAL   D CG2 1 
ATOM   7680 N N   . TYR   C 2 93  ? -57.90200 42.43600  45.74400  1.000 77.80752  ? 93   TYR   D N   1 
ATOM   7681 C CA  . TYR   C 2 93  ? -57.28700 42.64500  44.44200  1.000 71.88289  ? 93   TYR   D CA  1 
ATOM   7682 C C   . TYR   C 2 93  ? -56.35400 41.48900  44.10700  1.000 70.94306  ? 93   TYR   D C   1 
ATOM   7683 O O   . TYR   C 2 93  ? -55.57100 41.04000  44.95100  1.000 63.29060  ? 93   TYR   D O   1 
ATOM   7684 C CB  . TYR   C 2 93  ? -56.52700 43.97300  44.41100  1.000 72.69411  ? 93   TYR   D CB  1 
ATOM   7685 C CG  . TYR   C 2 93  ? -57.44100 45.17700  44.44500  1.000 73.40741  ? 93   TYR   D CG  1 
ATOM   7686 C CD1 . TYR   C 2 93  ? -57.98300 45.62600  45.64100  1.000 76.82567  ? 93   TYR   D CD1 1 
ATOM   7687 C CD2 . TYR   C 2 93  ? -57.77100 45.85700  43.27900  1.000 74.10602  ? 93   TYR   D CD2 1 
ATOM   7688 C CE1 . TYR   C 2 93  ? -58.82500 46.72100  45.67900  1.000 77.62325  ? 93   TYR   D CE1 1 
ATOM   7689 C CE2 . TYR   C 2 93  ? -58.61100 46.95600  43.30800  1.000 77.48512  ? 93   TYR   D CE2 1 
ATOM   7690 C CZ  . TYR   C 2 93  ? -59.13600 47.38300  44.51100  1.000 80.27138  ? 93   TYR   D CZ  1 
ATOM   7691 O OH  . TYR   C 2 93  ? -59.97400 48.47400  44.54900  1.000 81.81050  ? 93   TYR   D OH  1 
ATOM   7692 N N   . TYR   C 2 94  ? -56.44700 41.01000  42.86700  1.000 73.97900  ? 94   TYR   D N   1 
ATOM   7693 C CA  . TYR   C 2 94  ? -55.68800 39.85600  42.40800  1.000 72.57131  ? 94   TYR   D CA  1 
ATOM   7694 C C   . TYR   C 2 94  ? -54.89300 40.22100  41.16400  1.000 66.78209  ? 94   TYR   D C   1 
ATOM   7695 O O   . TYR   C 2 94  ? -55.32600 41.03900  40.34600  1.000 59.44690  ? 94   TYR   D O   1 
ATOM   7696 C CB  . TYR   C 2 94  ? -56.60600 38.66600  42.10500  1.000 72.90505  ? 94   TYR   D CB  1 
ATOM   7697 C CG  . TYR   C 2 94  ? -57.57700 38.33600  43.21900  1.000 69.47713  ? 94   TYR   D CG  1 
ATOM   7698 C CD1 . TYR   C 2 94  ? -57.20900 37.50000  44.26700  1.000 57.97035  ? 94   TYR   D CD1 1 
ATOM   7699 C CD2 . TYR   C 2 94  ? -58.86000 38.86700  43.22200  1.000 69.83432  ? 94   TYR   D CD2 1 
ATOM   7700 C CE1 . TYR   C 2 94  ? -58.09500 37.19800  45.28000  1.000 66.81582  ? 94   TYR   D CE1 1 
ATOM   7701 C CE2 . TYR   C 2 94  ? -59.75100 38.57400  44.23100  1.000 70.74053  ? 94   TYR   D CE2 1 
ATOM   7702 C CZ  . TYR   C 2 94  ? -59.36600 37.74000  45.25800  1.000 70.33970  ? 94   TYR   D CZ  1 
ATOM   7703 O OH  . TYR   C 2 94  ? -60.26200 37.45100  46.26300  1.000 69.65941  ? 94   TYR   D OH  1 
ATOM   7704 N N   . CYS   C 2 95  ? -53.72900 39.59000  41.02900  1.000 69.82306  ? 95   CYS   D N   1 
ATOM   7705 C CA  . CYS   C 2 95  ? -52.79600 39.84500  39.93700  1.000 64.41568  ? 95   CYS   D CA  1 
ATOM   7706 C C   . CYS   C 2 95  ? -52.95000 38.77800  38.85900  1.000 56.55828  ? 95   CYS   D C   1 
ATOM   7707 O O   . CYS   C 2 95  ? -52.85400 37.58200  39.15100  1.000 55.53272  ? 95   CYS   D O   1 
ATOM   7708 C CB  . CYS   C 2 95  ? -51.36200 39.85500  40.46500  1.000 65.39318  ? 95   CYS   D CB  1 
ATOM   7709 S SG  . CYS   C 2 95  ? -50.08500 39.95200  39.20900  1.000 74.24737  ? 95   CYS   D SG  1 
ATOM   7710 N N   . ASN   C 2 96  ? -53.17100 39.21100  37.61800  1.000 56.73625  ? 96   ASN   D N   1 
ATOM   7711 C CA  . ASN   C 2 96  ? -53.38400 38.31000  36.49000  1.000 55.66989  ? 96   ASN   D CA  1 
ATOM   7712 C C   . ASN   C 2 96  ? -52.24800 38.43200  35.48300  1.000 50.53081  ? 96   ASN   D C   1 
ATOM   7713 O O   . ASN   C 2 96  ? -51.86700 39.54300  35.09600  1.000 45.10035  ? 96   ASN   D O   1 
ATOM   7714 C CB  . ASN   C 2 96  ? -54.71400 38.60000  35.78800  1.000 54.09248  ? 96   ASN   D CB  1 
ATOM   7715 C CG  . ASN   C 2 96  ? -55.14500 37.47000  34.86600  1.000 50.37151  ? 96   ASN   D CG  1 
ATOM   7716 O OD1 . ASN   C 2 96  ? -54.67700 36.33900  34.99100  1.000 52.37831  ? 96   ASN   D OD1 1 
ATOM   7717 N ND2 . ASN   C 2 96  ? -56.02000 37.77900  33.91900  1.000 51.14886  ? 96   ASN   D ND2 1 
ATOM   7718 N N   . ALA   C 2 97  ? -51.73000 37.28400  35.05000  1.000 47.89349  ? 97   ALA   D N   1 
ATOM   7719 C CA  . ALA   C 2 97  ? -50.74900 37.19800  33.97700  1.000 44.03858  ? 97   ALA   D CA  1 
ATOM   7720 C C   . ALA   C 2 97  ? -51.26300 36.22500  32.92900  1.000 44.33355  ? 97   ALA   D C   1 
ATOM   7721 O O   . ALA   C 2 97  ? -51.66000 35.10500  33.26400  1.000 40.68192  ? 97   ALA   D O   1 
ATOM   7722 C CB  . ALA   C 2 97  ? -49.38800 36.73200  34.49600  1.000 45.07914  ? 97   ALA   D CB  1 
ATOM   7723 N N   . LYS   C 2 98  ? -51.25700 36.64800  31.66900  1.000 45.95555  ? 98   LYS   D N   1 
ATOM   7724 C CA  . LYS   C 2 98  ? -51.67100 35.80000  30.56000  1.000 35.82528  ? 98   LYS   D CA  1 
ATOM   7725 C C   . LYS   C 2 98  ? -50.43200 35.34500  29.80500  1.000 35.03748  ? 98   LYS   D C   1 
ATOM   7726 O O   . LYS   C 2 98  ? -49.65600 36.17600  29.32800  1.000 43.24754  ? 98   LYS   D O   1 
ATOM   7727 C CB  . LYS   C 2 98  ? -52.62800 36.54500  29.63500  1.000 35.36229  ? 98   LYS   D CB  1 
ATOM   7728 C CG  . LYS   C 2 98  ? -53.90800 36.95900  30.32300  1.000 44.11088  ? 98   LYS   D CG  1 
ATOM   7729 C CD  . LYS   C 2 98  ? -54.86900 37.64000  29.37500  1.000 41.82042  ? 98   LYS   D CD  1 
ATOM   7730 C CE  . LYS   C 2 98  ? -56.18500 37.89800  30.07200  1.000 44.83123  ? 98   LYS   D CE  1 
ATOM   7731 N NZ  . LYS   C 2 98  ? -56.75700 36.61500  30.56100  1.000 39.15076  ? 98   LYS   D NZ  1 
ATOM   7732 N N   . VAL   C 2 99  ? -50.24400 34.03300  29.70300  1.000 35.64764  ? 99   VAL   D N   1 
ATOM   7733 C CA  . VAL   C 2 99  ? -49.04800 33.45800  29.09700  1.000 35.24680  ? 99   VAL   D CA  1 
ATOM   7734 C C   . VAL   C 2 99  ? -49.48200 32.56400  27.94300  1.000 36.55329  ? 99   VAL   D C   1 
ATOM   7735 O O   . VAL   C 2 99  ? -50.13000 31.53200  28.15600  1.000 35.39319  ? 99   VAL   D O   1 
ATOM   7736 C CB  . VAL   C 2 99  ? -48.20800 32.67700  30.11300  1.000 33.72988  ? 99   VAL   D CB  1 
ATOM   7737 C CG1 . VAL   C 2 99  ? -46.95300 32.16500  29.45100  1.000 42.84323  ? 99   VAL   D CG1 1 
ATOM   7738 C CG2 . VAL   C 2 99  ? -47.85600 33.56000  31.29000  1.000 31.34366  ? 99   VAL   D CG2 1 
ATOM   7739 N N   . ALA   C 2 100 ? -49.10000 32.94400  26.72400  1.000 37.24979  ? 100  ALA   D N   1 
ATOM   7740 C CA  . ALA   C 2 100 ? -49.55000 32.25300  25.52400  1.000 33.47529  ? 100  ALA   D CA  1 
ATOM   7741 C C   . ALA   C 2 100 ? -48.79900 30.94500  25.31700  1.000 27.73358  ? 100  ALA   D C   1 
ATOM   7742 O O   . ALA   C 2 100 ? -47.59600 30.85600  25.56300  1.000 34.13331  ? 100  ALA   D O   1 
ATOM   7743 C CB  . ALA   C 2 100 ? -49.36700 33.14600  24.29700  1.000 36.04865  ? 100  ALA   D CB  1 
ATOM   7744 N N   . GLY   C 2 101 ? -49.52200 29.92900  24.85700  1.000 30.20534  ? 101  GLY   D N   1 
ATOM   7745 C CA  . GLY   C 2 101 ? -48.92600 28.64800  24.53700  1.000 28.03163  ? 101  GLY   D CA  1 
ATOM   7746 C C   . GLY   C 2 101 ? -48.95200 28.38900  23.04700  1.000 35.77487  ? 101  GLY   D C   1 
ATOM   7747 O O   . GLY   C 2 101 ? -48.86500 29.33300  22.25500  1.000 43.12742  ? 101  GLY   D O   1 
ATOM   7748 N N   . THR   C 2 102 ? -49.07900 27.12600  22.64200  1.000 36.32143  ? 102  THR   D N   1 
ATOM   7749 C CA  . THR   C 2 102 ? -49.10000 26.82400  21.21600  1.000 32.40174  ? 102  THR   D CA  1 
ATOM   7750 C C   . THR   C 2 102 ? -50.40200 27.31600  20.59300  1.000 30.75780  ? 102  THR   D C   1 
ATOM   7751 O O   . THR   C 2 102 ? -50.40000 28.32500  19.88500  1.000 34.10238  ? 102  THR   D O   1 
ATOM   7752 C CB  . THR   C 2 102 ? -48.90200 25.32800  20.95800  1.000 33.80061  ? 102  THR   D CB  1 
ATOM   7753 O OG1 . THR   C 2 102 ? -47.58500 24.94100  21.37700  1.000 33.66390  ? 102  THR   D OG1 1 
ATOM   7754 C CG2 . THR   C 2 102 ? -49.04200 25.02700  19.48000  1.000 40.74381  ? 102  THR   D CG2 1 
ATOM   7755 N N   . PHE   C 2 103 ? -51.52000 26.64200  20.86100  1.000 35.74618  ? 103  PHE   D N   1 
ATOM   7756 C CA  . PHE   C 2 103 ? -52.78700 27.03500  20.25100  1.000 38.29776  ? 103  PHE   D CA  1 
ATOM   7757 C C   . PHE   C 2 103 ? -53.63500 27.96800  21.11200  1.000 39.91368  ? 103  PHE   D C   1 
ATOM   7758 O O   . PHE   C 2 103 ? -54.57500 28.57300  20.58400  1.000 40.32850  ? 103  PHE   D O   1 
ATOM   7759 C CB  . PHE   C 2 103 ? -53.63300 25.80400  19.89400  1.000 36.98946  ? 103  PHE   D CB  1 
ATOM   7760 C CG  . PHE   C 2 103 ? -52.96400 24.84600  18.94800  1.000 31.96478  ? 103  PHE   D CG  1 
ATOM   7761 C CD1 . PHE   C 2 103 ? -52.28900 25.31000  17.83500  1.000 35.52610  ? 103  PHE   D CD1 1 
ATOM   7762 C CD2 . PHE   C 2 103 ? -53.05000 23.47900  19.15100  1.000 28.57486  ? 103  PHE   D CD2 1 
ATOM   7763 C CE1 . PHE   C 2 103 ? -51.68600 24.42900  16.95800  1.000 37.84199  ? 103  PHE   D CE1 1 
ATOM   7764 C CE2 . PHE   C 2 103 ? -52.45600 22.59400  18.27900  1.000 29.26599  ? 103  PHE   D CE2 1 
ATOM   7765 C CZ  . PHE   C 2 103 ? -51.77000 23.06700  17.18200  1.000 38.71692  ? 103  PHE   D CZ  1 
ATOM   7766 N N   . SER   C 2 104 ? -53.35100 28.10800  22.40800  1.000 36.64607  ? 104  SER   D N   1 
ATOM   7767 C CA  . SER   C 2 104 ? -54.23400 28.87500  23.27800  1.000 37.52858  ? 104  SER   D CA  1 
ATOM   7768 C C   . SER   C 2 104 ? -53.43100 29.68900  24.28100  1.000 36.74516  ? 104  SER   D C   1 
ATOM   7769 O O   . SER   C 2 104 ? -52.23600 29.46600  24.48800  1.000 36.60601  ? 104  SER   D O   1 
ATOM   7770 C CB  . SER   C 2 104 ? -55.21700 27.97000  24.02900  1.000 34.23366  ? 104  SER   D CB  1 
ATOM   7771 O OG  . SER   C 2 104 ? -54.54200 26.88300  24.63900  1.000 44.30511  ? 104  SER   D OG  1 
ATOM   7772 N N   . ILE   C 2 105 ? -54.12200 30.63300  24.91500  1.000 32.44178  ? 105  ILE   D N   1 
ATOM   7773 C CA  . ILE   C 2 105 ? -53.55000 31.51300  25.92700  1.000 35.20409  ? 105  ILE   D CA  1 
ATOM   7774 C C   . ILE   C 2 105 ? -54.05800 31.06700  27.29200  1.000 36.34520  ? 105  ILE   D C   1 
ATOM   7775 O O   . ILE   C 2 105 ? -55.20800 30.63500  27.42600  1.000 35.04261  ? 105  ILE   D O   1 
ATOM   7776 C CB  . ILE   C 2 105 ? -53.91100 32.98300  25.63800  1.000 32.55926  ? 105  ILE   D CB  1 
ATOM   7777 C CG1 . ILE   C 2 105 ? -53.29400 33.42100  24.30900  1.000 31.50804  ? 105  ILE   D CG1 1 
ATOM   7778 C CG2 . ILE   C 2 105 ? -53.45400 33.89500  26.76300  1.000 33.11002  ? 105  ILE   D CG2 1 
ATOM   7779 C CD1 . ILE   C 2 105 ? -53.83400 34.73100  23.78400  1.000 36.75483  ? 105  ILE   D CD1 1 
ATOM   7780 N N   . TYR   C 2 106 ? -53.19400 31.15600  28.30100  1.000 36.19580  ? 106  TYR   D N   1 
ATOM   7781 C CA  . TYR   C 2 106 ? -53.47600 30.65600  29.63700  1.000 32.73699  ? 106  TYR   D CA  1 
ATOM   7782 C C   . TYR   C 2 106 ? -53.53200 31.80000  30.64100  1.000 37.08519  ? 106  TYR   D C   1 
ATOM   7783 O O   . TYR   C 2 106 ? -52.89300 32.84200  30.46100  1.000 31.29317  ? 106  TYR   D O   1 
ATOM   7784 C CB  . TYR   C 2 106 ? -52.41800 29.64100  30.07300  1.000 29.09606  ? 106  TYR   D CB  1 
ATOM   7785 C CG  . TYR   C 2 106 ? -52.34600 28.42300  29.18100  1.000 30.59410  ? 106  TYR   D CG  1 
ATOM   7786 C CD1 . TYR   C 2 106 ? -53.38600 27.50600  29.13900  1.000 32.63599  ? 106  TYR   D CD1 1 
ATOM   7787 C CD2 . TYR   C 2 106 ? -51.24900 28.20600  28.35800  1.000 37.70033  ? 106  TYR   D CD2 1 
ATOM   7788 C CE1 . TYR   C 2 106 ? -53.32600 26.39400  28.32000  1.000 39.25328  ? 106  TYR   D CE1 1 
ATOM   7789 C CE2 . TYR   C 2 106 ? -51.17900 27.10000  27.53400  1.000 34.28278  ? 106  TYR   D CE2 1 
ATOM   7790 C CZ  . TYR   C 2 106 ? -52.22000 26.19700  27.51800  1.000 38.83903  ? 106  TYR   D CZ  1 
ATOM   7791 O OH  . TYR   C 2 106 ? -52.15700 25.09500  26.69800  1.000 30.79089  ? 106  TYR   D OH  1 
ATOM   7792 N N   . ASP   C 2 107 ? -54.30300 31.58700  31.70800  1.000 42.28896  ? 107  ASP   D N   1 
ATOM   7793 C CA  . ASP   C 2 107 ? -54.46100 32.54800  32.79200  1.000 36.51953  ? 107  ASP   D CA  1 
ATOM   7794 C C   . ASP   C 2 107 ? -53.72500 32.07900  34.03900  1.000 39.36685  ? 107  ASP   D C   1 
ATOM   7795 O O   . ASP   C 2 107 ? -53.67600 30.88100  34.33900  1.000 42.54270  ? 107  ASP   D O   1 
ATOM   7796 C CB  . ASP   C 2 107 ? -55.93500 32.77300  33.12000  1.000 33.12461  ? 107  ASP   D CB  1 
ATOM   7797 C CG  . ASP   C 2 107 ? -56.49100 34.02400  32.47500  1.000 48.30432  ? 107  ASP   D CG  1 
ATOM   7798 O OD1 . ASP   C 2 107 ? -55.69200 34.84600  31.98000  1.000 52.58445  ? 107  ASP   D OD1 1 
ATOM   7799 O OD2 . ASP   C 2 107 ? -57.72600 34.18300  32.44300  1.000 63.77661  ? 107  ASP   D OD2 1 
ATOM   7800 N N   . TYR   C 2 108 ? -53.16000 33.03600  34.76300  1.000 40.59746  ? 108  TYR   D N   1 
ATOM   7801 C CA  . TYR   C 2 108 ? -52.46800 32.76200  36.01000  1.000 40.99518  ? 108  TYR   D CA  1 
ATOM   7802 C C   . TYR   C 2 108 ? -52.73600 33.90500  36.97400  1.000 45.66432  ? 108  TYR   D C   1 
ATOM   7803 O O   . TYR   C 2 108 ? -52.73900 35.07500  36.57800  1.000 41.19127  ? 108  TYR   D O   1 
ATOM   7804 C CB  . TYR   C 2 108 ? -50.96300 32.59400  35.79900  1.000 43.61814  ? 108  TYR   D CB  1 
ATOM   7805 C CG  . TYR   C 2 108 ? -50.56000 31.32600  35.07900  1.000 44.19745  ? 108  TYR   D CG  1 
ATOM   7806 C CD1 . TYR   C 2 108 ? -50.42900 30.12600  35.76900  1.000 44.72486  ? 108  TYR   D CD1 1 
ATOM   7807 C CD2 . TYR   C 2 108 ? -50.27500 31.33400  33.71700  1.000 40.65396  ? 108  TYR   D CD2 1 
ATOM   7808 C CE1 . TYR   C 2 108 ? -50.04200 28.96800  35.12100  1.000 39.05438  ? 108  TYR   D CE1 1 
ATOM   7809 C CE2 . TYR   C 2 108 ? -49.88400 30.17800  33.06200  1.000 35.61312  ? 108  TYR   D CE2 1 
ATOM   7810 C CZ  . TYR   C 2 108 ? -49.77000 28.99900  33.77200  1.000 33.66797  ? 108  TYR   D CZ  1 
ATOM   7811 O OH  . TYR   C 2 108 ? -49.39200 27.84300  33.13600  1.000 34.96372  ? 108  TYR   D OH  1 
ATOM   7812 N N   . TRP   C 2 109 ? -52.95700 33.56000  38.23800  1.000 48.49808  ? 109  TRP   D N   1 
ATOM   7813 C CA  . TRP   C 2 109 ? -53.32500 34.53200  39.25300  1.000 48.88797  ? 109  TRP   D CA  1 
ATOM   7814 C C   . TRP   C 2 109 ? -52.42500 34.37300  40.47000  1.000 48.33062  ? 109  TRP   D C   1 
ATOM   7815 O O   . TRP   C 2 109 ? -51.89400 33.29100  40.73400  1.000 46.04251  ? 109  TRP   D O   1 
ATOM   7816 C CB  . TRP   C 2 109 ? -54.79000 34.36900  39.66600  1.000 44.39545  ? 109  TRP   D CB  1 
ATOM   7817 C CG  . TRP   C 2 109 ? -55.75800 34.50700  38.53600  1.000 40.57838  ? 109  TRP   D CG  1 
ATOM   7818 C CD1 . TRP   C 2 109 ? -56.12800 33.53600  37.65400  1.000 41.52008  ? 109  TRP   D CD1 1 
ATOM   7819 C CD2 . TRP   C 2 109 ? -56.50900 35.67400  38.18500  1.000 41.71483  ? 109  TRP   D CD2 1 
ATOM   7820 N NE1 . TRP   C 2 109 ? -57.05100 34.02800  36.76600  1.000 41.19572  ? 109  TRP   D NE1 1 
ATOM   7821 C CE2 . TRP   C 2 109 ? -57.30400 35.33900  37.07100  1.000 40.29060  ? 109  TRP   D CE2 1 
ATOM   7822 C CE3 . TRP   C 2 109 ? -56.58300 36.97000  38.70000  1.000 50.81389  ? 109  TRP   D CE3 1 
ATOM   7823 C CZ2 . TRP   C 2 109 ? -58.15800 36.25200  36.46300  1.000 48.72018  ? 109  TRP   D CZ2 1 
ATOM   7824 C CZ3 . TRP   C 2 109 ? -57.43300 37.87500  38.09400  1.000 55.53575  ? 109  TRP   D CZ3 1 
ATOM   7825 C CH2 . TRP   C 2 109 ? -58.21000 37.51100  36.98800  1.000 53.28175  ? 109  TRP   D CH2 1 
ATOM   7826 N N   . GLY   C 2 110 ? -52.25600 35.46600  41.21000  1.000 52.49499  ? 110  GLY   D N   1 
ATOM   7827 C CA  . GLY   C 2 110 ? -51.56700 35.41400  42.47900  1.000 65.54383  ? 110  GLY   D CA  1 
ATOM   7828 C C   . GLY   C 2 110 ? -52.49500 35.01500  43.61400  1.000 66.26286  ? 110  GLY   D C   1 
ATOM   7829 O O   . GLY   C 2 110 ? -53.69600 34.80500  43.44200  1.000 59.01795  ? 110  GLY   D O   1 
ATOM   7830 N N   . GLN   C 2 111 ? -51.91100 34.91400  44.81200  1.000 73.35759  ? 111  GLN   D N   1 
ATOM   7831 C CA  . GLN   C 2 111 ? -52.68500 34.45400  45.96200  1.000 80.98786  ? 111  GLN   D CA  1 
ATOM   7832 C C   . GLN   C 2 111 ? -53.66300 35.51800  46.44900  1.000 74.76775  ? 111  GLN   D C   1 
ATOM   7833 O O   . GLN   C 2 111 ? -54.72900 35.17900  46.97800  1.000 72.03907  ? 111  GLN   D O   1 
ATOM   7834 C CB  . GLN   C 2 111 ? -51.74500 34.02300  47.08900  1.000 78.93152  ? 111  GLN   D CB  1 
ATOM   7835 C CG  . GLN   C 2 111 ? -50.75900 32.93600  46.67500  1.000 89.67381  ? 111  GLN   D CG  1 
ATOM   7836 C CD  . GLN   C 2 111 ? -50.00700 32.33900  47.85000  1.000 100.46324 ? 111  GLN   D CD  1 
ATOM   7837 O OE1 . GLN   C 2 111 ? -50.34200 32.58600  49.01000  1.000 100.24552 ? 111  GLN   D OE1 1 
ATOM   7838 N NE2 . GLN   C 2 111 ? -48.97400 31.55600  47.55400  1.000 91.55348  ? 111  GLN   D NE2 1 
ATOM   7839 N N   . GLY   C 2 112 ? -53.33000 36.79600  46.28100  1.000 74.55765  ? 112  GLY   D N   1 
ATOM   7840 C CA  . GLY   C 2 112 ? -54.28100 37.85600  46.55800  1.000 78.21199  ? 112  GLY   D CA  1 
ATOM   7841 C C   . GLY   C 2 112 ? -53.85700 38.86800  47.60500  1.000 80.27652  ? 112  GLY   D C   1 
ATOM   7842 O O   . GLY   C 2 112 ? -53.01100 38.58300  48.45900  1.000 75.48803  ? 112  GLY   D O   1 
ATOM   7843 N N   . THR   C 2 113 ? -54.44000 40.06800  47.52700  1.000 80.05743  ? 113  THR   D N   1 
ATOM   7844 C CA  . THR   C 2 113 ? -54.28900 41.12100  48.52300  1.000 82.53887  ? 113  THR   D CA  1 
ATOM   7845 C C   . THR   C 2 113 ? -55.61300 41.85500  48.67200  1.000 85.10683  ? 113  THR   D C   1 
ATOM   7846 O O   . THR   C 2 113 ? -56.40900 41.91900  47.73100  1.000 80.74448  ? 113  THR   D O   1 
ATOM   7847 C CB  . THR   C 2 113 ? -53.20700 42.15000  48.15600  1.000 80.27092  ? 113  THR   D CB  1 
ATOM   7848 O OG1 . THR   C 2 113 ? -53.53600 42.77000  46.90500  1.000 76.93504  ? 113  THR   D OG1 1 
ATOM   7849 C CG2 . THR   C 2 113 ? -51.82500 41.51100  48.09600  1.000 79.86098  ? 113  THR   D CG2 1 
ATOM   7850 N N   . GLN   C 2 114 ? -55.83300 42.43300  49.85400  1.000 88.68201  ? 114  GLN   D N   1 
ATOM   7851 C CA  . GLN   C 2 114 ? -57.06900 43.14400  50.14800  1.000 83.21827  ? 114  GLN   D CA  1 
ATOM   7852 C C   . GLN   C 2 114 ? -56.80800 44.62300  50.40000  1.000 83.67055  ? 114  GLN   D C   1 
ATOM   7853 O O   . GLN   C 2 114 ? -55.85000 44.99400  51.08900  1.000 78.87978  ? 114  GLN   D O   1 
ATOM   7854 C CB  . GLN   C 2 114 ? -57.79300 42.53900  51.35300  1.000 80.04315  ? 114  GLN   D CB  1 
ATOM   7855 C CG  . GLN   C 2 114 ? -59.21700 43.05100  51.49200  1.000 78.55750  ? 114  GLN   D CG  1 
ATOM   7856 C CD  . GLN   C 2 114 ? -60.16200 42.01000  52.04500  1.000 79.89639  ? 114  GLN   D CD  1 
ATOM   7857 O OE1 . GLN   C 2 114 ? -59.74500 40.91900  52.43600  1.000 82.11900  ? 114  GLN   D OE1 1 
ATOM   7858 N NE2 . GLN   C 2 114 ? -61.44900 42.33600  52.06800  1.000 78.09120  ? 114  GLN   D NE2 1 
ATOM   7859 N N   . VAL   C 2 115 ? -57.67700 45.45600  49.83200  1.000 85.62726  ? 115  VAL   D N   1 
ATOM   7860 C CA  . VAL   C 2 115 ? -57.68500 46.89700  50.04000  1.000 83.43072  ? 115  VAL   D CA  1 
ATOM   7861 C C   . VAL   C 2 115 ? -59.04900 47.27900  50.59700  1.000 83.50283  ? 115  VAL   D C   1 
ATOM   7862 O O   . VAL   C 2 115 ? -60.08100 46.79400  50.11800  1.000 79.84015  ? 115  VAL   D O   1 
ATOM   7863 C CB  . VAL   C 2 115 ? -57.39600 47.66100  48.73000  1.000 84.00004  ? 115  VAL   D CB  1 
ATOM   7864 C CG1 . VAL   C 2 115 ? -57.56300 49.16100  48.92700  1.000 87.21196  ? 115  VAL   D CG1 1 
ATOM   7865 C CG2 . VAL   C 2 115 ? -56.00600 47.32800  48.20900  1.000 87.14208  ? 115  VAL   D CG2 1 
ATOM   7866 N N   . THR   C 2 116 ? -59.05500 48.13700  51.61700  1.000 92.10345  ? 116  THR   D N   1 
ATOM   7867 C CA  . THR   C 2 116 ? -60.29800 48.57200  52.24500  1.000 90.86391  ? 116  THR   D CA  1 
ATOM   7868 C C   . THR   C 2 116 ? -60.20100 50.04800  52.59200  1.000 85.22226  ? 116  THR   D C   1 
ATOM   7869 O O   . THR   C 2 116 ? -59.36400 50.44800  53.40700  1.000 83.12857  ? 116  THR   D O   1 
ATOM   7870 C CB  . THR   C 2 116 ? -60.61800 47.74900  53.49600  1.000 87.25850  ? 116  THR   D CB  1 
ATOM   7871 O OG1 . THR   C 2 116 ? -60.90500 46.39700  53.11700  1.000 87.77896  ? 116  THR   D OG1 1 
ATOM   7872 C CG2 . THR   C 2 116 ? -61.82200 48.33600  54.21900  1.000 84.12924  ? 116  THR   D CG2 1 
ATOM   7873 N N   . VAL   C 2 117 ? -61.06400 50.84400  51.97500  1.000 85.27190  ? 117  VAL   D N   1 
ATOM   7874 C CA  . VAL   C 2 117 ? -61.12300 52.27600  52.23500  1.000 86.88348  ? 117  VAL   D CA  1 
ATOM   7875 C C   . VAL   C 2 117 ? -62.01000 52.52300  53.44800  1.000 97.17289  ? 117  VAL   D C   1 
ATOM   7876 O O   . VAL   C 2 117 ? -63.11500 51.97600  53.54700  1.000 98.98671  ? 117  VAL   D O   1 
ATOM   7877 C CB  . VAL   C 2 117 ? -61.64000 53.01800  50.99500  1.000 84.93584  ? 117  VAL   D CB  1 
ATOM   7878 C CG1 . VAL   C 2 117 ? -61.84400 54.47900  51.29300  1.000 90.52967  ? 117  VAL   D CG1 1 
ATOM   7879 C CG2 . VAL   C 2 117 ? -60.66500 52.83300  49.85200  1.000 86.13712  ? 117  VAL   D CG2 1 
ATOM   7880 N N   . SER   C 2 118 ? -61.52500 53.34500  54.37700  1.000 102.98168 ? 118  SER   D N   1 
ATOM   7881 C CA  . SER   C 2 118 ? -62.20100 53.59700  55.64400  1.000 99.20807  ? 118  SER   D CA  1 
ATOM   7882 C C   . SER   C 2 118 ? -62.91600 54.94100  55.59100  1.000 95.50186  ? 118  SER   D C   1 
ATOM   7883 O O   . SER   C 2 118 ? -62.28200 55.97700  55.36200  1.000 96.14943  ? 118  SER   D O   1 
ATOM   7884 C CB  . SER   C 2 118 ? -61.20600 53.57200  56.80500  1.000 93.67437  ? 118  SER   D CB  1 
ATOM   7885 O OG  . SER   C 2 118 ? -60.77000 54.87900  57.14000  1.000 93.92442  ? 118  SER   D OG  1 
ATOM   7886 N N   . SER   C 2 119 ? -64.22900 54.92100  55.80800  1.000 95.74112  ? 119  SER   D N   1 
ATOM   7887 C CA  . SER   C 2 119 ? -64.95900 56.16000  56.01000  1.000 101.07223 ? 119  SER   D CA  1 
ATOM   7888 C C   . SER   C 2 119 ? -64.53500 56.80400  57.33100  1.000 106.99011 ? 119  SER   D C   1 
ATOM   7889 O O   . SER   C 2 119 ? -63.80200 56.22000  58.13600  1.000 103.98018 ? 119  SER   D O   1 
ATOM   7890 C CB  . SER   C 2 119 ? -66.46900 55.91100  55.98900  1.000 99.38255  ? 119  SER   D CB  1 
ATOM   7891 O OG  . SER   C 2 119 ? -66.82700 54.96200  54.99800  1.000 89.08464  ? 119  SER   D OG  1 
ATOM   7892 N N   . HIS   C 2 120 ? -65.00200 58.03100  57.54300  1.000 110.15023 ? 120  HIS   D N   1 
ATOM   7893 C CA  . HIS   C 2 120 ? -64.67300 58.79900  58.74300  1.000 117.67439 ? 120  HIS   D CA  1 
ATOM   7894 C C   . HIS   C 2 120 ? -65.06200 58.07900  60.03700  1.000 120.68494 ? 120  HIS   D C   1 
ATOM   7895 O O   . HIS   C 2 120 ? -66.22600 57.73700  60.25400  1.000 119.92105 ? 120  HIS   D O   1 
ATOM   7896 C CB  . HIS   C 2 120 ? -65.35400 60.16900  58.68400  1.000 115.01352 ? 120  HIS   D CB  1 
ATOM   7897 C CG  . HIS   C 2 120 ? -66.83400 60.09300  58.47900  1.000 112.39009 ? 120  HIS   D CG  1 
ATOM   7898 N ND1 . HIS   C 2 120 ? -67.40100 59.86100  57.24500  1.000 112.50084 ? 120  HIS   D ND1 1 
ATOM   7899 C CD2 . HIS   C 2 120 ? -67.86400 60.20500  59.35200  1.000 114.90013 ? 120  HIS   D CD2 1 
ATOM   7900 C CE1 . HIS   C 2 120 ? -68.71700 59.83800  57.36500  1.000 115.84714 ? 120  HIS   D CE1 1 
ATOM   7901 N NE2 . HIS   C 2 120 ? -69.02300 60.04500  58.63300  1.000 117.02296 ? 120  HIS   D NE2 1 
ATOM   7902 N N   . GLN   D 2 1   ? -18.65300 42.50900  35.32400  1.000 50.65600  ? 1    GLN   F N   1 
ATOM   7903 C CA  . GLN   D 2 1   ? -20.10700 42.50100  35.39100  1.000 51.27301  ? 1    GLN   F CA  1 
ATOM   7904 C C   . GLN   D 2 1   ? -20.62800 41.11200  35.76300  1.000 51.10496  ? 1    GLN   F C   1 
ATOM   7905 O O   . GLN   D 2 1   ? -21.80800 40.94300  36.07300  1.000 48.54818  ? 1    GLN   F O   1 
ATOM   7906 C CB  . GLN   D 2 1   ? -20.70900 42.95900  34.06000  1.000 54.35788  ? 1    GLN   F CB  1 
ATOM   7907 N N   . VAL   D 2 2   ? -19.75500 40.11200  35.72300  1.000 48.65093  ? 2    VAL   F N   1 
ATOM   7908 C CA  . VAL   D 2 2   ? -20.10300 38.79400  36.21700  1.000 47.65617  ? 2    VAL   F CA  1 
ATOM   7909 C C   . VAL   D 2 2   ? -19.51600 38.66800  37.61400  1.000 55.17909  ? 2    VAL   F C   1 
ATOM   7910 O O   . VAL   D 2 2   ? -18.62500 39.42300  38.01200  1.000 57.46037  ? 2    VAL   F O   1 
ATOM   7911 C CB  . VAL   D 2 2   ? -19.60500 37.64100  35.31200  1.000 46.66536  ? 2    VAL   F CB  1 
ATOM   7912 C CG1 . VAL   D 2 2   ? -20.07900 37.82500  33.87800  1.000 54.57794  ? 2    VAL   F CG1 1 
ATOM   7913 C CG2 . VAL   D 2 2   ? -18.10700 37.49300  35.40000  1.000 42.95068  ? 2    VAL   F CG2 1 
ATOM   7914 N N   . GLN   D 2 3   ? -20.01800 37.69600  38.37100  1.000 51.42895  ? 3    GLN   F N   1 
ATOM   7915 C CA  . GLN   D 2 3   ? -19.58300 37.49600  39.74400  1.000 45.30677  ? 3    GLN   F CA  1 
ATOM   7916 C C   . GLN   D 2 3   ? -19.38700 36.00900  40.00100  1.000 43.98079  ? 3    GLN   F C   1 
ATOM   7917 O O   . GLN   D 2 3   ? -20.05200 35.16500  39.39400  1.000 40.44903  ? 3    GLN   F O   1 
ATOM   7918 C CB  . GLN   D 2 3   ? -20.58900 38.08800  40.73900  1.000 37.60817  ? 3    GLN   F CB  1 
ATOM   7919 N N   . LEU   D 2 4   ? -18.45600 35.70000  40.90500  1.000 41.25176  ? 4    LEU   F N   1 
ATOM   7920 C CA  . LEU   D 2 4   ? -18.12400 34.33100  41.27500  1.000 44.32506  ? 4    LEU   F CA  1 
ATOM   7921 C C   . LEU   D 2 4   ? -18.01500 34.22800  42.78900  1.000 49.78873  ? 4    LEU   F C   1 
ATOM   7922 O O   . LEU   D 2 4   ? -17.49900 35.13800  43.44500  1.000 49.50978  ? 4    LEU   F O   1 
ATOM   7923 C CB  . LEU   D 2 4   ? -16.81000 33.88100  40.62700  1.000 44.77449  ? 4    LEU   F CB  1 
ATOM   7924 C CG  . LEU   D 2 4   ? -16.77900 33.75300  39.10500  1.000 41.08573  ? 4    LEU   F CG  1 
ATOM   7925 C CD1 . LEU   D 2 4   ? -15.35500 33.75800  38.64200  1.000 45.38565  ? 4    LEU   F CD1 1 
ATOM   7926 C CD2 . LEU   D 2 4   ? -17.45100 32.47700  38.65800  1.000 39.51092  ? 4    LEU   F CD2 1 
ATOM   7927 N N   . GLN   D 2 5   ? -18.49700 33.11700  43.34200  1.000 52.47857  ? 5    GLN   F N   1 
ATOM   7928 C CA  . GLN   D 2 5   ? -18.49600 32.91100  44.78900  1.000 49.03651  ? 5    GLN   F CA  1 
ATOM   7929 C C   . GLN   D 2 5   ? -18.14700 31.45800  45.08300  1.000 47.93355  ? 5    GLN   F C   1 
ATOM   7930 O O   . GLN   D 2 5   ? -18.94900 30.55800  44.81100  1.000 46.96068  ? 5    GLN   F O   1 
ATOM   7931 C CB  . GLN   D 2 5   ? -19.85000 33.27800  45.39800  1.000 49.88541  ? 5    GLN   F CB  1 
ATOM   7932 N N   . GLU   D 2 6   ? -16.95700 31.23000  45.63700  1.000 42.54998  ? 6    GLU   F N   1 
ATOM   7933 C CA  . GLU   D 2 6   ? -16.57100 29.89600  46.06700  1.000 44.09001  ? 6    GLU   F CA  1 
ATOM   7934 C C   . GLU   D 2 6   ? -17.24500 29.54300  47.39200  1.000 51.12405  ? 6    GLU   F C   1 
ATOM   7935 O O   . GLU   D 2 6   ? -17.76900 30.40200  48.10800  1.000 50.23073  ? 6    GLU   F O   1 
ATOM   7936 C CB  . GLU   D 2 6   ? -15.05400 29.78200  46.22700  1.000 48.51984  ? 6    GLU   F CB  1 
ATOM   7937 C CG  . GLU   D 2 6   ? -14.24700 29.85000  44.94700  1.000 47.03994  ? 6    GLU   F CG  1 
ATOM   7938 C CD  . GLU   D 2 6   ? -13.77100 31.25000  44.62700  1.000 48.64059  ? 6    GLU   F CD  1 
ATOM   7939 O OE1 . GLU   D 2 6   ? -14.26700 32.21400  45.24600  1.000 48.43220  ? 6    GLU   F OE1 1 
ATOM   7940 O OE2 . GLU   D 2 6   ? -12.88000 31.38100  43.76600  1.000 52.12194  ? 6    GLU   F OE2 1 
ATOM   7941 N N   . SER   D 2 7   ? -17.22200 28.25200  47.71600  1.000 48.74291  ? 7    SER   F N   1 
ATOM   7942 C CA  . SER   D 2 7   ? -17.75600 27.75000  48.97400  1.000 40.74835  ? 7    SER   F CA  1 
ATOM   7943 C C   . SER   D 2 7   ? -17.23300 26.34000  49.20400  1.000 49.01794  ? 7    SER   F C   1 
ATOM   7944 O O   . SER   D 2 7   ? -17.00000 25.58600  48.25500  1.000 53.67799  ? 7    SER   F O   1 
ATOM   7945 C CB  . SER   D 2 7   ? -19.29000 27.73200  48.99500  1.000 43.55716  ? 7    SER   F CB  1 
ATOM   7946 O OG  . SER   D 2 7   ? -19.86000 28.87700  48.38200  1.000 54.00790  ? 7    SER   F OG  1 
ATOM   7947 N N   . GLY   D 2 8   ? -17.05000 25.99800  50.47700  1.000 54.74700  ? 8    GLY   F N   1 
ATOM   7948 C CA  . GLY   D 2 8   ? -16.80500 24.62400  50.86600  1.000 54.87601  ? 8    GLY   F CA  1 
ATOM   7949 C C   . GLY   D 2 8   ? -15.35900 24.24800  51.11400  1.000 55.99526  ? 8    GLY   F C   1 
ATOM   7950 O O   . GLY   D 2 8   ? -14.94600 23.14200  50.75600  1.000 55.42992  ? 8    GLY   F O   1 
ATOM   7951 N N   . GLY   D 2 9   ? -14.58000 25.14200  51.72700  1.000 57.65874  ? 9    GLY   F N   1 
ATOM   7952 C CA  . GLY   D 2 9   ? -13.20900 24.86700  52.08700  1.000 59.55244  ? 9    GLY   F CA  1 
ATOM   7953 C C   . GLY   D 2 9   ? -13.01200 24.76500  53.59300  1.000 59.99080  ? 9    GLY   F C   1 
ATOM   7954 O O   . GLY   D 2 9   ? -13.94500 24.85500  54.38600  1.000 71.27161  ? 9    GLY   F O   1 
ATOM   7955 N N   . GLY   D 2 10  ? -11.75300 24.57200  53.97600  1.000 55.67607  ? 10   GLY   F N   1 
ATOM   7956 C CA  . GLY   D 2 10  ? -11.41600 24.46100  55.38300  1.000 49.36148  ? 10   GLY   F CA  1 
ATOM   7957 C C   . GLY   D 2 10  ? -10.41100 23.36400  55.65500  1.000 54.87708  ? 10   GLY   F C   1 
ATOM   7958 O O   . GLY   D 2 10  ? -9.54800  23.09000  54.81400  1.000 58.50628  ? 10   GLY   F O   1 
ATOM   7959 N N   . LEU   D 2 11  ? -10.50400 22.72100  56.81300  1.000 54.67106  ? 11   LEU   F N   1 
ATOM   7960 C CA  . LEU   D 2 11  ? -9.54600  21.68500  57.16500  1.000 54.41647  ? 11   LEU   F CA  1 
ATOM   7961 C C   . LEU   D 2 11  ? -10.16900 20.30900  57.00900  1.000 58.59050  ? 11   LEU   F C   1 
ATOM   7962 O O   . LEU   D 2 11  ? -11.39200 20.15100  56.97100  1.000 65.78320  ? 11   LEU   F O   1 
ATOM   7963 C CB  . LEU   D 2 11  ? -9.06300  21.82400  58.60500  1.000 59.57743  ? 11   LEU   F CB  1 
ATOM   7964 C CG  . LEU   D 2 11  ? -8.76700  23.20400  59.14800  1.000 63.69999  ? 11   LEU   F CG  1 
ATOM   7965 C CD1 . LEU   D 2 11  ? -10.02100 23.59400  59.85900  1.000 55.12080  ? 11   LEU   F CD1 1 
ATOM   7966 C CD2 . LEU   D 2 11  ? -7.58500  23.16400  60.09400  1.000 58.54335  ? 11   LEU   F CD2 1 
ATOM   7967 N N   . VAL   D 2 12  ? -9.29500  19.30800  56.95300  1.000 58.14437  ? 12   VAL   F N   1 
ATOM   7968 C CA  . VAL   D 2 12  ? -9.67500  17.90200  57.00000  1.000 64.24596  ? 12   VAL   F CA  1 
ATOM   7969 C C   . VAL   D 2 12  ? -8.38700  17.10100  57.12500  1.000 64.12949  ? 12   VAL   F C   1 
ATOM   7970 O O   . VAL   D 2 12  ? -7.32900  17.53000  56.64900  1.000 54.63753  ? 12   VAL   F O   1 
ATOM   7971 C CB  . VAL   D 2 12  ? -10.50000 17.48400  55.76500  1.000 71.30424  ? 12   VAL   F CB  1 
ATOM   7972 C CG1 . VAL   D 2 12  ? -9.63100  17.44700  54.51500  1.000 59.52894  ? 12   VAL   F CG1 1 
ATOM   7973 C CG2 . VAL   D 2 12  ? -11.18600 16.14200  56.00300  1.000 78.50390  ? 12   VAL   F CG2 1 
ATOM   7974 N N   . GLN   D 2 13  ? -8.45400  15.96100  57.80400  1.000 70.85760  ? 13   GLN   F N   1 
ATOM   7975 C CA  . GLN   D 2 13  ? -7.28800  15.10500  57.92800  1.000 75.05525  ? 13   GLN   F CA  1 
ATOM   7976 C C   . GLN   D 2 13  ? -6.90200  14.55200  56.56300  1.000 67.52136  ? 13   GLN   F C   1 
ATOM   7977 O O   . GLN   D 2 13  ? -7.72400  14.47200  55.64700  1.000 70.66541  ? 13   GLN   F O   1 
ATOM   7978 C CB  . GLN   D 2 13  ? -7.56200  13.95600  58.90000  1.000 86.76680  ? 13   GLN   F CB  1 
ATOM   7979 N N   . ALA   D 2 14  ? -5.63100  14.17200  56.43200  1.000 65.54040  ? 14   ALA   F N   1 
ATOM   7980 C CA  . ALA   D 2 14  ? -5.16200  13.57100  55.19000  1.000 67.83884  ? 14   ALA   F CA  1 
ATOM   7981 C C   . ALA   D 2 14  ? -5.99400  12.34100  54.85200  1.000 69.10487  ? 14   ALA   F C   1 
ATOM   7982 O O   . ALA   D 2 14  ? -6.52800  11.66100  55.73400  1.000 75.48238  ? 14   ALA   F O   1 
ATOM   7983 C CB  . ALA   D 2 14  ? -3.68600  13.19200  55.29100  1.000 67.36073  ? 14   ALA   F CB  1 
ATOM   7984 N N   . GLY   D 2 15  ? -6.10600  12.06000  53.55500  1.000 66.80732  ? 15   GLY   F N   1 
ATOM   7985 C CA  . GLY   D 2 15  ? -7.03300  11.06500  53.07300  1.000 62.72961  ? 15   GLY   F CA  1 
ATOM   7986 C C   . GLY   D 2 15  ? -8.48100  11.49600  53.09600  1.000 61.05829  ? 15   GLY   F C   1 
ATOM   7987 O O   . GLY   D 2 15  ? -9.34300  10.73900  52.62800  1.000 61.96766  ? 15   GLY   F O   1 
ATOM   7988 N N   . GLY   D 2 16  ? -8.77700  12.68100  53.61800  1.000 62.08570  ? 16   GLY   F N   1 
ATOM   7989 C CA  . GLY   D 2 16  ? -10.12800 13.18500  53.67400  1.000 64.26446  ? 16   GLY   F CA  1 
ATOM   7990 C C   . GLY   D 2 16  ? -10.62900 13.58300  52.29900  1.000 57.08459  ? 16   GLY   F C   1 
ATOM   7991 O O   . GLY   D 2 16  ? -10.01300 13.32200  51.26500  1.000 62.72557  ? 16   GLY   F O   1 
ATOM   7992 N N   . SER   D 2 17  ? -11.78700 14.23700  52.29900  1.000 56.23240  ? 17   SER   F N   1 
ATOM   7993 C CA  . SER   D 2 17  ? -12.41400 14.64500  51.05200  1.000 57.98294  ? 17   SER   F CA  1 
ATOM   7994 C C   . SER   D 2 17  ? -13.11000 15.98200  51.24600  1.000 53.93944  ? 17   SER   F C   1 
ATOM   7995 O O   . SER   D 2 17  ? -13.62000 16.28300  52.32700  1.000 65.98705  ? 17   SER   F O   1 
ATOM   7996 C CB  . SER   D 2 17  ? -13.40900 13.59400  50.55100  1.000 62.87581  ? 17   SER   F CB  1 
ATOM   7997 O OG  . SER   D 2 17  ? -12.84800 12.29400  50.61300  1.000 71.26197  ? 17   SER   F OG  1 
ATOM   7998 N N   . LEU   D 2 18  ? -13.12200 16.78000  50.18300  1.000 58.57566  ? 18   LEU   F N   1 
ATOM   7999 C CA  . LEU   D 2 18  ? -13.80400 18.06300  50.18100  1.000 55.63889  ? 18   LEU   F CA  1 
ATOM   8000 C C   . LEU   D 2 18  ? -14.47200 18.26600  48.82900  1.000 58.04410  ? 18   LEU   F C   1 
ATOM   8001 O O   . LEU   D 2 18  ? -14.07900 17.67200  47.82100  1.000 52.45305  ? 18   LEU   F O   1 
ATOM   8002 C CB  . LEU   D 2 18  ? -12.84200 19.22100  50.47200  1.000 51.28621  ? 18   LEU   F CB  1 
ATOM   8003 C CG  . LEU   D 2 18  ? -12.72200 19.65400  51.93100  1.000 62.04890  ? 18   LEU   F CG  1 
ATOM   8004 C CD1 . LEU   D 2 18  ? -11.33400 20.22300  52.19300  1.000 68.22041  ? 18   LEU   F CD1 1 
ATOM   8005 C CD2 . LEU   D 2 18  ? -13.80900 20.65700  52.30500  1.000 52.30950  ? 18   LEU   F CD2 1 
ATOM   8006 N N   . ARG   D 2 19  ? -15.49200 19.12100  48.81600  1.000 54.67815  ? 19   ARG   F N   1 
ATOM   8007 C CA  . ARG   D 2 19  ? -16.24100 19.44200  47.60300  1.000 51.21241  ? 19   ARG   F CA  1 
ATOM   8008 C C   . ARG   D 2 19  ? -16.31600 20.96100  47.50300  1.000 54.47240  ? 19   ARG   F C   1 
ATOM   8009 O O   . ARG   D 2 19  ? -17.21600 21.58100  48.07800  1.000 56.52320  ? 19   ARG   F O   1 
ATOM   8010 C CB  . ARG   D 2 19  ? -17.62800 18.80600  47.63300  1.000 54.90690  ? 19   ARG   F CB  1 
ATOM   8011 C CG  . ARG   D 2 19  ? -18.40200 18.90900  46.32900  1.000 52.72470  ? 19   ARG   F CG  1 
ATOM   8012 C CD  . ARG   D 2 19  ? -19.80600 18.34500  46.48800  1.000 60.30131  ? 19   ARG   F CD  1 
ATOM   8013 N NE  . ARG   D 2 19  ? -20.50600 18.22100  45.21600  1.000 76.86272  ? 19   ARG   F NE  1 
ATOM   8014 C CZ  . ARG   D 2 19  ? -21.77400 17.84800  45.09600  1.000 87.07238  ? 19   ARG   F CZ  1 
ATOM   8015 N NH1 . ARG   D 2 19  ? -22.51400 17.56900  46.15700  1.000 92.44490  ? 19   ARG   F NH1 1 
ATOM   8016 N NH2 . ARG   D 2 19  ? -22.31300 17.75500  43.88300  1.000 78.07903  ? 19   ARG   F NH2 1 
ATOM   8017 N N   . LEU   D 2 20  ? -15.36900 21.56300  46.78700  1.000 50.04120  ? 20   LEU   F N   1 
ATOM   8018 C CA  . LEU   D 2 20  ? -15.43200 22.99800  46.55900  1.000 48.09593  ? 20   LEU   F CA  1 
ATOM   8019 C C   . LEU   D 2 20  ? -16.40700 23.26900  45.42600  1.000 49.15768  ? 20   LEU   F C   1 
ATOM   8020 O O   . LEU   D 2 20  ? -16.43600 22.53900  44.43200  1.000 52.58627  ? 20   LEU   F O   1 
ATOM   8021 C CB  . LEU   D 2 20  ? -14.06600 23.57100  46.19400  1.000 49.45897  ? 20   LEU   F CB  1 
ATOM   8022 C CG  . LEU   D 2 20  ? -12.92000 23.42800  47.18900  1.000 46.65842  ? 20   LEU   F CG  1 
ATOM   8023 C CD1 . LEU   D 2 20  ? -11.63600 23.35700  46.39900  1.000 41.44908  ? 20   LEU   F CD1 1 
ATOM   8024 C CD2 . LEU   D 2 20  ? -12.88300 24.52800  48.23800  1.000 46.45028  ? 20   LEU   F CD2 1 
ATOM   8025 N N   . SER   D 2 21  ? -17.19900 24.32700  45.57100  1.000 40.33871  ? 21   SER   F N   1 
ATOM   8026 C CA  . SER   D 2 21  ? -18.23200 24.64000  44.59800  1.000 38.12882  ? 21   SER   F CA  1 
ATOM   8027 C C   . SER   D 2 21  ? -18.28500 26.14100  44.35900  1.000 46.01271  ? 21   SER   F C   1 
ATOM   8028 O O   . SER   D 2 21  ? -18.21600 26.93200  45.30400  1.000 40.50545  ? 21   SER   F O   1 
ATOM   8029 C CB  . SER   D 2 21  ? -19.59500 24.14200  45.06400  1.000 36.89423  ? 21   SER   F CB  1 
ATOM   8030 O OG  . SER   D 2 21  ? -20.25500 25.14400  45.81100  1.000 48.97492  ? 21   SER   F OG  1 
ATOM   8031 N N   . CYS   D 2 22  ? -18.42800 26.52400  43.09000  1.000 54.22285  ? 22   CYS   F N   1 
ATOM   8032 C CA  . CYS   D 2 22  ? -18.39800 27.92000  42.67300  1.000 52.79746  ? 22   CYS   F CA  1 
ATOM   8033 C C   . CYS   D 2 22  ? -19.63100 28.23800  41.84400  1.000 46.83006  ? 22   CYS   F C   1 
ATOM   8034 O O   . CYS   D 2 22  ? -19.88700 27.57600  40.83500  1.000 45.70560  ? 22   CYS   F O   1 
ATOM   8035 C CB  . CYS   D 2 22  ? -17.13500 28.22300  41.86000  1.000 48.45243  ? 22   CYS   F CB  1 
ATOM   8036 S SG  . CYS   D 2 22  ? -17.14100 29.82300  41.01200  1.000 61.36167  ? 22   CYS   F SG  1 
ATOM   8037 N N   . ALA   D 2 23  ? -20.37700 29.25800  42.26100  1.000 41.04408  ? 23   ALA   F N   1 
ATOM   8038 C CA  . ALA   D 2 23  ? -21.55600 29.71900  41.54100  1.000 42.20884  ? 23   ALA   F CA  1 
ATOM   8039 C C   . ALA   D 2 23  ? -21.23900 31.00700  40.79600  1.000 45.02098  ? 23   ALA   F C   1 
ATOM   8040 O O   . ALA   D 2 23  ? -20.61100 31.91500  41.34900  1.000 49.74130  ? 23   ALA   F O   1 
ATOM   8041 C CB  . ALA   D 2 23  ? -22.72700 29.95000  42.49500  1.000 45.62354  ? 23   ALA   F CB  1 
ATOM   8042 N N   . ALA   D 2 24  ? -21.68600 31.08100  39.54200  1.000 41.05799  ? 24   ALA   F N   1 
ATOM   8043 C CA  . ALA   D 2 24  ? -21.41400 32.21000  38.66500  1.000 38.25815  ? 24   ALA   F CA  1 
ATOM   8044 C C   . ALA   D 2 24  ? -22.71000 32.89100  38.25300  1.000 40.17644  ? 24   ALA   F C   1 
ATOM   8045 O O   . ALA   D 2 24  ? -23.76400 32.25300  38.15000  1.000 40.72498  ? 24   ALA   F O   1 
ATOM   8046 C CB  . ALA   D 2 24  ? -20.65400 31.76700  37.41100  1.000 41.88616  ? 24   ALA   F CB  1 
ATOM   8047 N N   . SER   D 2 25  ? -22.61800 34.19600  38.00400  1.000 34.39860  ? 25   SER   F N   1 
ATOM   8048 C CA  . SER   D 2 25  ? -23.75600 34.98100  37.55000  1.000 40.19733  ? 25   SER   F CA  1 
ATOM   8049 C C   . SER   D 2 25  ? -23.25200 36.14800  36.71900  1.000 49.10484  ? 25   SER   F C   1 
ATOM   8050 O O   . SER   D 2 25  ? -22.28400 36.81000  37.09900  1.000 56.54012  ? 25   SER   F O   1 
ATOM   8051 C CB  . SER   D 2 25  ? -24.57200 35.52400  38.71900  1.000 41.31745  ? 25   SER   F CB  1 
ATOM   8052 O OG  . SER   D 2 25  ? -24.04600 36.77600  39.12200  1.000 38.99675  ? 25   SER   F OG  1 
ATOM   8053 N N   . GLY   D 2 26  ? -23.92200 36.40900  35.60100  1.000 40.99512  ? 26   GLY   F N   1 
ATOM   8054 C CA  . GLY   D 2 26  ? -23.57300 37.53900  34.76400  1.000 41.06071  ? 26   GLY   F CA  1 
ATOM   8055 C C   . GLY   D 2 26  ? -23.47200 37.18000  33.29600  1.000 45.84169  ? 26   GLY   F C   1 
ATOM   8056 O O   . GLY   D 2 26  ? -23.38800 38.06000  32.43300  1.000 35.37919  ? 26   GLY   F O   1 
ATOM   8057 N N   . SER   D 2 27  ? -23.48700 35.88200  33.00300  1.000 45.02453  ? 27   SER   F N   1 
ATOM   8058 C CA  . SER   D 2 27  ? -23.32200 35.39900  31.64200  1.000 39.05884  ? 27   SER   F CA  1 
ATOM   8059 C C   . SER   D 2 27  ? -24.04400 34.06800  31.50200  1.000 35.77508  ? 27   SER   F C   1 
ATOM   8060 O O   . SER   D 2 27  ? -24.47400 33.46400  32.48600  1.000 48.20294  ? 27   SER   F O   1 
ATOM   8061 C CB  . SER   D 2 27  ? -21.84100 35.24600  31.28300  1.000 41.76612  ? 27   SER   F CB  1 
ATOM   8062 O OG  . SER   D 2 27  ? -21.20100 34.33200  32.15800  1.000 41.05326  ? 27   SER   F OG  1 
ATOM   8063 N N   . ILE   D 2 28  ? -24.17600 33.61500  30.25900  1.000 36.47985  ? 28   ILE   F N   1 
ATOM   8064 C CA  . ILE   D 2 28  ? -24.71000 32.28500  29.99600  1.000 40.59760  ? 28   ILE   F CA  1 
ATOM   8065 C C   . ILE   D 2 28  ? -23.65600 31.27000  30.41000  1.000 42.09931  ? 28   ILE   F C   1 
ATOM   8066 O O   . ILE   D 2 28  ? -22.72500 30.97900  29.65100  1.000 51.44930  ? 28   ILE   F O   1 
ATOM   8067 C CB  . ILE   D 2 28  ? -25.10700 32.11000  28.51800  1.000 43.23980  ? 28   ILE   F CB  1 
ATOM   8068 C CG1 . ILE   D 2 28  ? -25.86600 33.34000  28.02100  1.000 36.92140  ? 28   ILE   F CG1 1 
ATOM   8069 C CG2 . ILE   D 2 28  ? -25.93200 30.84100  28.32700  1.000 43.76628  ? 28   ILE   F CG2 1 
ATOM   8070 C CD1 . ILE   D 2 28  ? -25.93100 33.43600  26.51500  1.000 42.71880  ? 28   ILE   F CD1 1 
ATOM   8071 N N   . PHE   D 2 29  ? -23.79900 30.72600  31.62000  1.000 39.53052  ? 29   PHE   F N   1 
ATOM   8072 C CA  . PHE   D 2 29  ? -22.81300 29.79500  32.16000  1.000 42.13166  ? 29   PHE   F CA  1 
ATOM   8073 C C   . PHE   D 2 29  ? -22.61400 28.59000  31.24800  1.000 42.66581  ? 29   PHE   F C   1 
ATOM   8074 O O   . PHE   D 2 29  ? -21.57100 27.93200  31.32200  1.000 46.13423  ? 29   PHE   F O   1 
ATOM   8075 C CB  . PHE   D 2 29  ? -23.25400 29.37500  33.57000  1.000 41.04275  ? 29   PHE   F CB  1 
ATOM   8076 C CG  . PHE   D 2 29  ? -22.32500 28.41000  34.25300  1.000 38.93490  ? 29   PHE   F CG  1 
ATOM   8077 C CD1 . PHE   D 2 29  ? -22.43500 27.04300  34.04800  1.000 40.30142  ? 29   PHE   F CD1 1 
ATOM   8078 C CD2 . PHE   D 2 29  ? -21.34800 28.87600  35.11700  1.000 39.47496  ? 29   PHE   F CD2 1 
ATOM   8079 C CE1 . PHE   D 2 29  ? -21.58000 26.16600  34.68200  1.000 45.65852  ? 29   PHE   F CE1 1 
ATOM   8080 C CE2 . PHE   D 2 29  ? -20.48900 28.00100  35.75700  1.000 43.68890  ? 29   PHE   F CE2 1 
ATOM   8081 C CZ  . PHE   D 2 29  ? -20.60400 26.64400  35.53800  1.000 48.87313  ? 29   PHE   F CZ  1 
ATOM   8082 N N   . SER   D 2 30  ? -23.57800 28.31400  30.36700  1.000 44.18698  ? 30   SER   F N   1 
ATOM   8083 C CA  . SER   D 2 30  ? -23.46200 27.18300  29.45400  1.000 49.13501  ? 30   SER   F CA  1 
ATOM   8084 C C   . SER   D 2 30  ? -22.33500 27.39000  28.44700  1.000 45.42502  ? 30   SER   F C   1 
ATOM   8085 O O   . SER   D 2 30  ? -21.63700 26.43500  28.08200  1.000 39.55724  ? 30   SER   F O   1 
ATOM   8086 C CB  . SER   D 2 30  ? -24.79500 26.96300  28.73600  1.000 50.86002  ? 30   SER   F CB  1 
ATOM   8087 O OG  . SER   D 2 30  ? -24.72300 25.88000  27.82600  1.000 57.49384  ? 30   SER   F OG  1 
ATOM   8088 N N   . LEU   D 2 31  ? -22.13900 28.62800  27.98700  1.000 45.40691  ? 31   LEU   F N   1 
ATOM   8089 C CA  . LEU   D 2 31  ? -21.17100 28.94200  26.94100  1.000 45.70471  ? 31   LEU   F CA  1 
ATOM   8090 C C   . LEU   D 2 31  ? -19.81600 29.38100  27.48100  1.000 46.01246  ? 31   LEU   F C   1 
ATOM   8091 O O   . LEU   D 2 31  ? -19.00700 29.92600  26.72400  1.000 49.04677  ? 31   LEU   F O   1 
ATOM   8092 C CB  . LEU   D 2 31  ? -21.72600 30.02500  26.01400  1.000 40.94694  ? 31   LEU   F CB  1 
ATOM   8093 C CG  . LEU   D 2 31  ? -23.03100 29.72200  25.29100  1.000 43.43221  ? 31   LEU   F CG  1 
ATOM   8094 C CD1 . LEU   D 2 31  ? -23.63800 31.01000  24.76900  1.000 46.87460  ? 31   LEU   F CD1 1 
ATOM   8095 C CD2 . LEU   D 2 31  ? -22.75900 28.75600  24.15400  1.000 34.65325  ? 31   LEU   F CD2 1 
ATOM   8096 N N   . ASN   D 2 32  ? -19.54500 29.16100  28.75800  1.000 46.39894  ? 32   ASN   F N   1 
ATOM   8097 C CA  . ASN   D 2 32  ? -18.28700 29.57900  29.35000  1.000 41.48546  ? 32   ASN   F CA  1 
ATOM   8098 C C   . ASN   D 2 32  ? -17.44500 28.36500  29.71300  1.000 42.37245  ? 32   ASN   F C   1 
ATOM   8099 O O   . ASN   D 2 32  ? -17.96500 27.31300  30.09700  1.000 39.50796  ? 32   ASN   F O   1 
ATOM   8100 C CB  . ASN   D 2 32  ? -18.52500 30.43500  30.59100  1.000 36.97137  ? 32   ASN   F CB  1 
ATOM   8101 C CG  . ASN   D 2 32  ? -19.15400 31.76400  30.26600  1.000 45.33261  ? 32   ASN   F CG  1 
ATOM   8102 O OD1 . ASN   D 2 32  ? -19.55000 32.50800  31.16500  1.000 40.92903  ? 32   ASN   F OD1 1 
ATOM   8103 N ND2 . ASN   D 2 32  ? -19.23600 32.08500  28.97500  1.000 45.50555  ? 32   ASN   F ND2 1 
ATOM   8104 N N   . ASP   D 2 33  ? -16.13600 28.51600  29.56800  1.000 48.19492  ? 33   ASP   F N   1 
ATOM   8105 C CA  . ASP   D 2 33  ? -15.20800 27.51600  30.06500  1.000 47.93933  ? 33   ASP   F CA  1 
ATOM   8106 C C   . ASP   D 2 33  ? -14.94300 27.77600  31.54100  1.000 46.77496  ? 33   ASP   F C   1 
ATOM   8107 O O   . ASP   D 2 33  ? -14.95700 28.92200  32.00100  1.000 41.28952  ? 33   ASP   F O   1 
ATOM   8108 C CB  . ASP   D 2 33  ? -13.90400 27.53800  29.27100  1.000 49.95156  ? 33   ASP   F CB  1 
ATOM   8109 C CG  . ASP   D 2 33  ? -14.03100 26.82700  27.93700  1.000 54.91090  ? 33   ASP   F CG  1 
ATOM   8110 O OD1 . ASP   D 2 33  ? -15.12100 26.29100  27.65400  1.000 54.77501  ? 33   ASP   F OD1 1 
ATOM   8111 O OD2 . ASP   D 2 33  ? -13.04400 26.80100  27.17300  1.000 56.75561  ? 33   ASP   F OD2 1 
ATOM   8112 N N   . MET   D 2 34  ? -14.73100 26.69900  32.29000  1.000 49.38125  ? 34   MET   F N   1 
ATOM   8113 C CA  . MET   D 2 34  ? -14.61400 26.78400  33.73600  1.000 43.49175  ? 34   MET   F CA  1 
ATOM   8114 C C   . MET   D 2 34  ? -13.41400 25.97300  34.20500  1.000 44.45722  ? 34   MET   F C   1 
ATOM   8115 O O   . MET   D 2 34  ? -13.04200 24.96900  33.59200  1.000 45.82809  ? 34   MET   F O   1 
ATOM   8116 C CB  . MET   D 2 34  ? -15.89900 26.29400  34.41900  1.000 37.19988  ? 34   MET   F CB  1 
ATOM   8117 C CG  . MET   D 2 34  ? -17.10400 27.18100  34.15200  1.000 32.11668  ? 34   MET   F CG  1 
ATOM   8118 S SD  . MET   D 2 34  ? -16.98500 28.76200  35.01500  1.000 38.19908  ? 34   MET   F SD  1 
ATOM   8119 C CE  . MET   D 2 34  ? -18.02600 29.80000  34.00700  1.000 35.73040  ? 34   MET   F CE  1 
ATOM   8120 N N   . GLY   D 2 35  ? -12.80500 26.42100  35.29700  1.000 40.05670  ? 35   GLY   F N   1 
ATOM   8121 C CA  . GLY   D 2 35  ? -11.63400 25.73900  35.81200  1.000 39.86239  ? 35   GLY   F CA  1 
ATOM   8122 C C   . GLY   D 2 35  ? -11.31600 26.14700  37.23000  1.000 39.86317  ? 35   GLY   F C   1 
ATOM   8123 O O   . GLY   D 2 35  ? -11.76500 27.18900  37.72000  1.000 40.26707  ? 35   GLY   F O   1 
ATOM   8124 N N   . TRP   D 2 36  ? -10.52000 25.30500  37.88700  1.000 40.90920  ? 36   TRP   F N   1 
ATOM   8125 C CA  . TRP   D 2 36  ? -10.07000 25.53300  39.25300  1.000 40.47525  ? 36   TRP   F CA  1 
ATOM   8126 C C   . TRP   D 2 36  ? -8.55600  25.69500  39.27300  1.000 42.17534  ? 36   TRP   F C   1 
ATOM   8127 O O   . TRP   D 2 36  ? -7.83200  24.92800  38.62700  1.000 42.82579  ? 36   TRP   F O   1 
ATOM   8128 C CB  . TRP   D 2 36  ? -10.49600 24.37900  40.16700  1.000 47.93311  ? 36   TRP   F CB  1 
ATOM   8129 C CG  . TRP   D 2 36  ? -11.94700 24.40300  40.55500  1.000 47.77307  ? 36   TRP   F CG  1 
ATOM   8130 C CD1 . TRP   D 2 36  ? -12.97200 23.75800  39.92700  1.000 42.50387  ? 36   TRP   F CD1 1 
ATOM   8131 C CD2 . TRP   D 2 36  ? -12.52800 25.09100  41.67000  1.000 43.53749  ? 36   TRP   F CD2 1 
ATOM   8132 N NE1 . TRP   D 2 36  ? -14.15700 24.01100  40.57400  1.000 43.34090  ? 36   TRP   F NE1 1 
ATOM   8133 C CE2 . TRP   D 2 36  ? -13.91200 24.82600  41.64700  1.000 47.47981  ? 36   TRP   F CE2 1 
ATOM   8134 C CE3 . TRP   D 2 36  ? -12.01400 25.91000  42.67900  1.000 43.64636  ? 36   TRP   F CE3 1 
ATOM   8135 C CZ2 . TRP   D 2 36  ? -14.79100 25.34900  42.59800  1.000 46.09423  ? 36   TRP   F CZ2 1 
ATOM   8136 C CZ3 . TRP   D 2 36  ? -12.88700 26.43000  43.62500  1.000 50.13246  ? 36   TRP   F CZ3 1 
ATOM   8137 C CH2 . TRP   D 2 36  ? -14.26000 26.14700  43.57500  1.000 48.52127  ? 36   TRP   F CH2 1 
ATOM   8138 N N   . TYR   D 2 37  ? -8.08700  26.69800  40.00700  1.000 42.26987  ? 37   TYR   F N   1 
ATOM   8139 C CA  . TYR   D 2 37  ? -6.67100  26.94600  40.22500  1.000 40.73933  ? 37   TYR   F CA  1 
ATOM   8140 C C   . TYR   D 2 37  ? -6.39900  26.98700  41.72100  1.000 42.02235  ? 37   TYR   F C   1 
ATOM   8141 O O   . TYR   D 2 37  ? -7.28000  27.33100  42.51700  1.000 44.92015  ? 37   TYR   F O   1 
ATOM   8142 C CB  . TYR   D 2 37  ? -6.23300  28.26800  39.59200  1.000 40.59221  ? 37   TYR   F CB  1 
ATOM   8143 C CG  . TYR   D 2 37  ? -6.32000  28.33000  38.08300  1.000 40.07936  ? 37   TYR   F CG  1 
ATOM   8144 C CD1 . TYR   D 2 37  ? -7.54200  28.46900  37.44200  1.000 40.93920  ? 37   TYR   F CD1 1 
ATOM   8145 C CD2 . TYR   D 2 37  ? -5.17300  28.31500  37.30300  1.000 40.95175  ? 37   TYR   F CD2 1 
ATOM   8146 C CE1 . TYR   D 2 37  ? -7.62300  28.55600  36.06700  1.000 42.10696  ? 37   TYR   F CE1 1 
ATOM   8147 C CE2 . TYR   D 2 37  ? -5.24400  28.40000  35.92500  1.000 46.19177  ? 37   TYR   F CE2 1 
ATOM   8148 C CZ  . TYR   D 2 37  ? -6.47400  28.52300  35.31200  1.000 42.07591  ? 37   TYR   F CZ  1 
ATOM   8149 O OH  . TYR   D 2 37  ? -6.55300  28.60900  33.94300  1.000 30.88046  ? 37   TYR   F OH  1 
ATOM   8150 N N   . ARG   D 2 38  ? -5.17200  26.64300  42.10500  1.000 40.95192  ? 38   ARG   F N   1 
ATOM   8151 C CA  . ARG   D 2 38  ? -4.75100  26.73000  43.49600  1.000 38.75903  ? 38   ARG   F CA  1 
ATOM   8152 C C   . ARG   D 2 38  ? -3.39300  27.40800  43.57800  1.000 39.53259  ? 38   ARG   F C   1 
ATOM   8153 O O   . ARG   D 2 38  ? -2.57300  27.31100  42.66000  1.000 38.95283  ? 38   ARG   F O   1 
ATOM   8154 C CB  . ARG   D 2 38  ? -4.68400  25.34900  44.17100  1.000 39.37703  ? 38   ARG   F CB  1 
ATOM   8155 C CG  . ARG   D 2 38  ? -3.51700  24.47300  43.74800  1.000 36.00365  ? 38   ARG   F CG  1 
ATOM   8156 C CD  . ARG   D 2 38  ? -3.62100  23.10500  44.40400  1.000 41.75014  ? 38   ARG   F CD  1 
ATOM   8157 N NE  . ARG   D 2 38  ? -2.51100  22.22700  44.05300  1.000 49.38548  ? 38   ARG   F NE  1 
ATOM   8158 C CZ  . ARG   D 2 38  ? -2.43400  20.94900  44.39800  1.000 53.06126  ? 38   ARG   F CZ  1 
ATOM   8159 N NH1 . ARG   D 2 38  ? -3.39500  20.36300  45.09400  1.000 51.30045  ? 38   ARG   F NH1 1 
ATOM   8160 N NH2 . ARG   D 2 38  ? -1.37300  20.23900  44.02800  1.000 60.55393  ? 38   ARG   F NH2 1 
ATOM   8161 N N   . GLN   D 2 39  ? -3.16700  28.10300  44.68900  1.000 45.33882  ? 39   GLN   F N   1 
ATOM   8162 C CA  . GLN   D 2 39  ? -1.90300  28.78100  44.96600  1.000 42.75631  ? 39   GLN   F CA  1 
ATOM   8163 C C   . GLN   D 2 39  ? -1.39300  28.28000  46.30800  1.000 34.75027  ? 39   GLN   F C   1 
ATOM   8164 O O   . GLN   D 2 39  ? -1.75700  28.81500  47.35400  1.000 38.11385  ? 39   GLN   F O   1 
ATOM   8165 C CB  . GLN   D 2 39  ? -2.06400  30.29000  44.97100  1.000 43.64394  ? 39   GLN   F CB  1 
ATOM   8166 C CG  . GLN   D 2 39  ? -0.74700  31.03400  44.85200  1.000 46.90004  ? 39   GLN   F CG  1 
ATOM   8167 C CD  . GLN   D 2 39  ? -0.84200  32.45900  45.34500  1.000 57.18450  ? 39   GLN   F CD  1 
ATOM   8168 O OE1 . GLN   D 2 39  ? -1.77600  32.81700  46.06500  1.000 67.58764  ? 39   GLN   F OE1 1 
ATOM   8169 N NE2 . GLN   D 2 39  ? 0.13100   33.28300  44.96800  1.000 46.65290  ? 39   GLN   F NE2 1 
ATOM   8170 N N   . ALA   D 2 40  ? -0.55500  27.24800  46.27300  1.000 42.45567  ? 40   ALA   F N   1 
ATOM   8171 C CA  . ALA   D 2 40  ? 0.06900   26.75200  47.48700  1.000 40.48222  ? 40   ALA   F CA  1 
ATOM   8172 C C   . ALA   D 2 40  ? 1.09800   27.75900  48.00000  1.000 41.02825  ? 40   ALA   F C   1 
ATOM   8173 O O   . ALA   D 2 40  ? 1.64000   28.55300  47.22700  1.000 39.37588  ? 40   ALA   F O   1 
ATOM   8174 C CB  . ALA   D 2 40  ? 0.73700   25.40200  47.23400  1.000 41.28579  ? 40   ALA   F CB  1 
ATOM   8175 N N   . PRO   D 2 41  ? 1.37200   27.75800  49.30500  1.000 47.15804  ? 41   PRO   F N   1 
ATOM   8176 C CA  . PRO   D 2 41  ? 2.36600   28.69500  49.84000  1.000 45.71209  ? 41   PRO   F CA  1 
ATOM   8177 C C   . PRO   D 2 41  ? 3.73600   28.46300  49.22000  1.000 42.71560  ? 41   PRO   F C   1 
ATOM   8178 O O   . PRO   D 2 41  ? 4.11800   27.33100  48.91100  1.000 39.52544  ? 41   PRO   F O   1 
ATOM   8179 C CB  . PRO   D 2 41  ? 2.36400   28.39300  51.34400  1.000 31.07066  ? 41   PRO   F CB  1 
ATOM   8180 C CG  . PRO   D 2 41  ? 1.77800   27.02200  51.45600  1.000 27.69389  ? 41   PRO   F CG  1 
ATOM   8181 C CD  . PRO   D 2 41  ? 0.75800   26.94800  50.37100  1.000 37.12763  ? 41   PRO   F CD  1 
ATOM   8182 N N   . GLY   D 2 42  ? 4.46500   29.55800  49.01500  1.000 37.86536  ? 42   GLY   F N   1 
ATOM   8183 C CA  . GLY   D 2 42  ? 5.79700   29.48800  48.44600  1.000 47.81578  ? 42   GLY   F CA  1 
ATOM   8184 C C   . GLY   D 2 42  ? 5.82700   28.93600  47.03500  1.000 49.75969  ? 42   GLY   F C   1 
ATOM   8185 O O   . GLY   D 2 42  ? 6.89100   28.58300  46.51600  1.000 50.36705  ? 42   GLY   F O   1 
ATOM   8186 N N   . LYS   D 2 43  ? 4.65900   28.85600  46.40700  1.000 48.07247  ? 43   LYS   F N   1 
ATOM   8187 C CA  . LYS   D 2 43  ? 4.52200   28.33700  45.05900  1.000 42.12461  ? 43   LYS   F CA  1 
ATOM   8188 C C   . LYS   D 2 43  ? 3.76500   29.35000  44.21500  1.000 44.91472  ? 43   LYS   F C   1 
ATOM   8189 O O   . LYS   D 2 43  ? 3.30000   30.38300  44.70600  1.000 42.32131  ? 43   LYS   F O   1 
ATOM   8190 C CB  . LYS   D 2 43  ? 3.80300   26.98100  45.05100  1.000 38.97769  ? 43   LYS   F CB  1 
ATOM   8191 C CG  . LYS   D 2 43  ? 4.70900   25.80000  45.35200  1.000 42.67508  ? 43   LYS   F CG  1 
ATOM   8192 C CD  . LYS   D 2 43  ? 3.90500   24.56200  45.71100  1.000 49.92371  ? 43   LYS   F CD  1 
ATOM   8193 C CE  . LYS   D 2 43  ? 4.80500   23.45200  46.23400  1.000 58.22233  ? 43   LYS   F CE  1 
ATOM   8194 N NZ  . LYS   D 2 43  ? 4.08300   22.15900  46.41400  1.000 63.65190  ? 43   LYS   F NZ  1 
ATOM   8195 N N   . LEU   D 2 44  ? 3.65100   29.05000  42.92900  1.000 44.87386  ? 44   LEU   F N   1 
ATOM   8196 C CA  . LEU   D 2 44  ? 2.93800   29.91000  41.99900  1.000 44.97034  ? 44   LEU   F CA  1 
ATOM   8197 C C   . LEU   D 2 44  ? 1.55800   29.33500  41.70100  1.000 47.67284  ? 44   LEU   F C   1 
ATOM   8198 O O   . LEU   D 2 44  ? 1.28300   28.15400  41.92800  1.000 57.30384  ? 44   LEU   F O   1 
ATOM   8199 C CB  . LEU   D 2 44  ? 3.73100   30.10200  40.69900  1.000 52.99845  ? 44   LEU   F CB  1 
ATOM   8200 C CG  . LEU   D 2 44  ? 5.14000   30.71800  40.72400  1.000 53.49749  ? 44   LEU   F CG  1 
ATOM   8201 C CD1 . LEU   D 2 44  ? 6.20700   29.81600  41.36200  1.000 54.21262  ? 44   LEU   F CD1 1 
ATOM   8202 C CD2 . LEU   D 2 44  ? 5.55200   31.11400  39.31400  1.000 40.39640  ? 44   LEU   F CD2 1 
ATOM   8203 N N   . ARG   D 2 45  ? 0.68300   30.20000  41.19500  1.000 42.79501  ? 45   ARG   F N   1 
ATOM   8204 C CA  . ARG   D 2 45  ? -0.70400  29.83000  40.94600  1.000 41.01646  ? 45   ARG   F CA  1 
ATOM   8205 C C   . ARG   D 2 45  ? -0.78400  28.84600  39.78500  1.000 39.22581  ? 45   ARG   F C   1 
ATOM   8206 O O   . ARG   D 2 45  ? -0.43600  29.18400  38.64900  1.000 49.35558  ? 45   ARG   F O   1 
ATOM   8207 C CB  . ARG   D 2 45  ? -1.51500  31.08700  40.65400  1.000 43.50316  ? 45   ARG   F CB  1 
ATOM   8208 C CG  . ARG   D 2 45  ? -2.90400  30.86500  40.10500  1.000 44.79925  ? 45   ARG   F CG  1 
ATOM   8209 C CD  . ARG   D 2 45  ? -3.71000  32.15400  40.22100  1.000 57.05328  ? 45   ARG   F CD  1 
ATOM   8210 N NE  . ARG   D 2 45  ? -3.44000  32.85100  41.47700  1.000 78.38217  ? 45   ARG   F NE  1 
ATOM   8211 C CZ  . ARG   D 2 45  ? -2.75900  33.98500  41.58100  1.000 81.86907  ? 45   ARG   F CZ  1 
ATOM   8212 N NH1 . ARG   D 2 45  ? -2.26100  34.59400  40.51700  1.000 105.59411 ? 45   ARG   F NH1 1 
ATOM   8213 N NH2 . ARG   D 2 45  ? -2.56600  34.51900  42.78500  1.000 68.70719  ? 45   ARG   F NH2 1 
ATOM   8214 N N   . GLU   D 2 46  ? -1.24500  27.63100  40.06500  1.000 34.95692  ? 46   GLU   F N   1 
ATOM   8215 C CA  . GLU   D 2 46  ? -1.28200  26.56600  39.07700  1.000 35.51998  ? 46   GLU   F CA  1 
ATOM   8216 C C   . GLU   D 2 46  ? -2.70800  26.06700  38.88100  1.000 38.68212  ? 46   GLU   F C   1 
ATOM   8217 O O   . GLU   D 2 46  ? -3.54200  26.13700  39.78800  1.000 48.31261  ? 46   GLU   F O   1 
ATOM   8218 C CB  . GLU   D 2 46  ? -0.36900  25.40300  39.48700  1.000 37.62784  ? 46   GLU   F CB  1 
ATOM   8219 C CG  . GLU   D 2 46  ? -0.85300  24.61000  40.69300  1.000 52.18766  ? 46   GLU   F CG  1 
ATOM   8220 C CD  . GLU   D 2 46  ? 0.04600   23.42600  41.01700  1.000 66.70276  ? 46   GLU   F CD  1 
ATOM   8221 O OE1 . GLU   D 2 46  ? 0.96900   23.14400  40.22200  1.000 75.95411  ? 46   GLU   F OE1 1 
ATOM   8222 O OE2 . GLU   D 2 46  ? -0.16600  22.78400  42.07000  1.000 66.20771  ? 46   GLU   F OE2 1 
ATOM   8223 N N   . LEU   D 2 47  ? -2.98000  25.57600  37.67600  1.000 38.47221  ? 47   LEU   F N   1 
ATOM   8224 C CA  . LEU   D 2 47  ? -4.26400  24.95900  37.37700  1.000 40.30521  ? 47   LEU   F CA  1 
ATOM   8225 C C   . LEU   D 2 47  ? -4.33400  23.57200  38.00300  1.000 40.99027  ? 47   LEU   F C   1 
ATOM   8226 O O   . LEU   D 2 47  ? -3.34300  22.83900  38.03200  1.000 41.69986  ? 47   LEU   F O   1 
ATOM   8227 C CB  . LEU   D 2 47  ? -4.45400  24.87300  35.85800  1.000 36.21441  ? 47   LEU   F CB  1 
ATOM   8228 C CG  . LEU   D 2 47  ? -5.75400  24.33100  35.25800  1.000 34.34831  ? 47   LEU   F CG  1 
ATOM   8229 C CD1 . LEU   D 2 47  ? -6.30100  25.29400  34.22500  1.000 29.56665  ? 47   LEU   F CD1 1 
ATOM   8230 C CD2 . LEU   D 2 47  ? -5.51600  22.96700  34.63100  1.000 26.48769  ? 47   LEU   F CD2 1 
ATOM   8231 N N   . VAL   D 2 48  ? -5.50300  23.21100  38.52600  1.000 37.70145  ? 48   VAL   F N   1 
ATOM   8232 C CA  . VAL   D 2 48  ? -5.74300  21.86500  39.02000  1.000 39.72376  ? 48   VAL   F CA  1 
ATOM   8233 C C   . VAL   D 2 48  ? -6.67400  21.09100  38.09600  1.000 38.52503  ? 48   VAL   F C   1 
ATOM   8234 O O   . VAL   D 2 48  ? -6.44700  19.90900  37.83100  1.000 40.57198  ? 48   VAL   F O   1 
ATOM   8235 C CB  . VAL   D 2 48  ? -6.28100  21.87600  40.47200  1.000 40.82731  ? 48   VAL   F CB  1 
ATOM   8236 C CG1 . VAL   D 2 48  ? -5.34800  22.65300  41.36300  1.000 44.23705  ? 48   VAL   F CG1 1 
ATOM   8237 C CG2 . VAL   D 2 48  ? -7.68000  22.44700  40.56000  1.000 43.52658  ? 48   VAL   F CG2 1 
ATOM   8238 N N   . ALA   D 2 49  ? -7.69900  21.75300  37.56700  1.000 40.90754  ? 49   ALA   F N   1 
ATOM   8239 C CA  . ALA   D 2 49  ? -8.67500  21.11600  36.69700  1.000 41.87900  ? 49   ALA   F CA  1 
ATOM   8240 C C   . ALA   D 2 49  ? -9.40300  22.20000  35.92400  1.000 39.75113  ? 49   ALA   F C   1 
ATOM   8241 O O   . ALA   D 2 49  ? -9.62800  23.29800  36.43600  1.000 40.04665  ? 49   ALA   F O   1 
ATOM   8242 C CB  . ALA   D 2 49  ? -9.67400  20.26900  37.48900  1.000 38.03689  ? 49   ALA   F CB  1 
ATOM   8243 N N   . ALA   D 2 50  ? -9.76200  21.88200  34.68500  1.000 44.44639  ? 50   ALA   F N   1 
ATOM   8244 C CA  . ALA   D 2 50  ? -10.55900 22.77800  33.86300  1.000 41.73989  ? 50   ALA   F CA  1 
ATOM   8245 C C   . ALA   D 2 50  ? -11.59900 21.96100  33.11700  1.000 41.20041  ? 50   ALA   F C   1 
ATOM   8246 O O   . ALA   D 2 50  ? -11.30300 20.86400  32.63700  1.000 40.91654  ? 50   ALA   F O   1 
ATOM   8247 C CB  . ALA   D 2 50  ? -9.69100  23.56200  32.87500  1.000 37.02160  ? 50   ALA   F CB  1 
ATOM   8248 N N   . ILE   D 2 51  ? -12.82100 22.48700  33.04500  1.000 41.20550  ? 51   ILE   F N   1 
ATOM   8249 C CA  . ILE   D 2 51  ? -13.88100 21.91900  32.21900  1.000 41.89788  ? 51   ILE   F CA  1 
ATOM   8250 C C   . ILE   D 2 51  ? -14.27300 22.94400  31.16300  1.000 42.88239  ? 51   ILE   F C   1 
ATOM   8251 O O   . ILE   D 2 51  ? -14.52500 24.11300  31.47700  1.000 39.73604  ? 51   ILE   F O   1 
ATOM   8252 C CB  . ILE   D 2 51  ? -15.09900 21.46900  33.05400  1.000 42.37152  ? 51   ILE   F CB  1 
ATOM   8253 C CG1 . ILE   D 2 51  ? -16.01400 20.56500  32.22000  1.000 42.63707  ? 51   ILE   F CG1 1 
ATOM   8254 C CG2 . ILE   D 2 51  ? -15.87000 22.65200  33.64800  1.000 42.41785  ? 51   ILE   F CG2 1 
ATOM   8255 C CD1 . ILE   D 2 51  ? -17.03700 19.80800  33.03500  1.000 46.51122  ? 51   ILE   F CD1 1 
ATOM   8256 N N   . THR   D 2 52  ? -14.28100 22.51200  29.90800  1.000 49.80769  ? 52   THR   F N   1 
ATOM   8257 C CA  . THR   D 2 52  ? -14.71200 23.35900  28.81000  1.000 45.90508  ? 52   THR   F CA  1 
ATOM   8258 C C   . THR   D 2 52  ? -16.22100 23.25100  28.63200  1.000 53.24441  ? 52   THR   F C   1 
ATOM   8259 O O   . THR   D 2 52  ? -16.85400 22.28100  29.05700  1.000 56.36650  ? 52   THR   F O   1 
ATOM   8260 C CB  . THR   D 2 52  ? -13.99900 22.97200  27.51700  1.000 41.23014  ? 52   THR   F CB  1 
ATOM   8261 O OG1 . THR   D 2 52  ? -14.36600 21.63600  27.15100  1.000 44.70028  ? 52   THR   F OG1 1 
ATOM   8262 C CG2 . THR   D 2 52  ? -12.49300 23.03900  27.71000  1.000 51.10273  ? 52   THR   F CG2 1 
ATOM   8263 N N   . SER   D 2 53  ? -16.79900 24.27400  27.99900  1.000 52.63998  ? 53   SER   F N   1 
ATOM   8264 C CA  . SER   D 2 53  ? -18.24400 24.29800  27.80300  1.000 50.00200  ? 53   SER   F CA  1 
ATOM   8265 C C   . SER   D 2 53  ? -18.73400 23.10100  26.99700  1.000 46.94231  ? 53   SER   F C   1 
ATOM   8266 O O   . SER   D 2 53  ? -19.92300 22.77300  27.05400  1.000 52.04990  ? 53   SER   F O   1 
ATOM   8267 C CB  . SER   D 2 53  ? -18.65600 25.60300  27.12600  1.000 46.21367  ? 53   SER   F CB  1 
ATOM   8268 O OG  . SER   D 2 53  ? -18.33600 25.57600  25.74900  1.000 60.34716  ? 53   SER   F OG  1 
ATOM   8269 N N   . GLY   D 2 54  ? -17.84400 22.44000  26.26100  1.000 42.43970  ? 54   GLY   F N   1 
ATOM   8270 C CA  . GLY   D 2 54  ? -18.15700 21.20500  25.57600  1.000 45.69714  ? 54   GLY   F CA  1 
ATOM   8271 C C   . GLY   D 2 54  ? -18.01700 19.95300  26.40600  1.000 54.22187  ? 54   GLY   F C   1 
ATOM   8272 O O   . GLY   D 2 54  ? -18.40700 18.87400  25.95100  1.000 61.37411  ? 54   GLY   F O   1 
ATOM   8273 N N   . GLY   D 2 55  ? -17.45500 20.05700  27.61100  1.000 52.20869  ? 55   GLY   F N   1 
ATOM   8274 C CA  . GLY   D 2 55  ? -17.38200 18.95000  28.54400  1.000 50.39972  ? 55   GLY   F CA  1 
ATOM   8275 C C   . GLY   D 2 55  ? -15.99600 18.37500  28.75100  1.000 57.81761  ? 55   GLY   F C   1 
ATOM   8276 O O   . GLY   D 2 55  ? -15.78000 17.66600  29.74300  1.000 66.83092  ? 55   GLY   F O   1 
ATOM   8277 N N   . SER   D 2 56  ? -15.05200 18.65100  27.85400  1.000 53.65824  ? 56   SER   F N   1 
ATOM   8278 C CA  . SER   D 2 56  ? -13.72700 18.05200  27.96600  1.000 53.78185  ? 56   SER   F CA  1 
ATOM   8279 C C   . SER   D 2 56  ? -12.99200 18.58900  29.19200  1.000 55.99212  ? 56   SER   F C   1 
ATOM   8280 O O   . SER   D 2 56  ? -13.11800 19.76400  29.54800  1.000 50.05648  ? 56   SER   F O   1 
ATOM   8281 C CB  . SER   D 2 56  ? -12.91900 18.31800  26.69600  1.000 51.30031  ? 56   SER   F CB  1 
ATOM   8282 O OG  . SER   D 2 56  ? -11.99400 17.27100  26.45800  1.000 63.59757  ? 56   SER   F OG  1 
ATOM   8283 N N   . THR   D 2 57  ? -12.22300 17.71600  29.84400  1.000 55.86759  ? 57   THR   F N   1 
ATOM   8284 C CA  . THR   D 2 57  ? -11.60800 18.04300  31.12500  1.000 49.16853  ? 57   THR   F CA  1 
ATOM   8285 C C   . THR   D 2 57  ? -10.15800 17.58800  31.16000  1.000 49.54819  ? 57   THR   F C   1 
ATOM   8286 O O   . THR   D 2 57  ? -9.86900  16.41200  30.92100  1.000 49.45052  ? 57   THR   F O   1 
ATOM   8287 C CB  . THR   D 2 57  ? -12.35800 17.38100  32.28800  1.000 50.19714  ? 57   THR   F CB  1 
ATOM   8288 O OG1 . THR   D 2 57  ? -12.42300 15.96700  32.06700  1.000 52.56840  ? 57   THR   F OG1 1 
ATOM   8289 C CG2 . THR   D 2 57  ? -13.76800 17.92400  32.39900  1.000 46.89097  ? 57   THR   F CG2 1 
ATOM   8290 N N   . LYS   D 2 58  ? -9.25900  18.51400  31.48500  1.000 58.64715  ? 58   LYS   F N   1 
ATOM   8291 C CA  . LYS   D 2 58  ? -7.87300  18.20800  31.80800  1.000 55.28804  ? 58   LYS   F CA  1 
ATOM   8292 C C   . LYS   D 2 58  ? -7.63200  18.46400  33.29100  1.000 50.84334  ? 58   LYS   F C   1 
ATOM   8293 O O   . LYS   D 2 58  ? -8.32900  19.25800  33.92900  1.000 46.03967  ? 58   LYS   F O   1 
ATOM   8294 C CB  . LYS   D 2 58  ? -6.90100  19.04300  30.96400  1.000 35.71279  ? 58   LYS   F CB  1 
ATOM   8295 N N   . TYR   D 2 59  ? -6.63300  17.77600  33.83800  1.000 49.62916  ? 59   TYR   F N   1 
ATOM   8296 C CA  . TYR   D 2 59  ? -6.32300  17.85200  35.25700  1.000 46.61895  ? 59   TYR   F CA  1 
ATOM   8297 C C   . TYR   D 2 59  ? -4.83700  18.10300  35.45700  1.000 50.46876  ? 59   TYR   F C   1 
ATOM   8298 O O   . TYR   D 2 59  ? -4.01200  17.75100  34.61200  1.000 53.30139  ? 59   TYR   F O   1 
ATOM   8299 C CB  . TYR   D 2 59  ? -6.71300  16.56300  35.98700  1.000 50.88301  ? 59   TYR   F CB  1 
ATOM   8300 C CG  . TYR   D 2 59  ? -8.19900  16.36000  36.13300  1.000 49.96999  ? 59   TYR   F CG  1 
ATOM   8301 C CD1 . TYR   D 2 59  ? -8.89500  16.93400  37.18400  1.000 48.44001  ? 59   TYR   F CD1 1 
ATOM   8302 C CD2 . TYR   D 2 59  ? -8.90300  15.59000  35.22100  1.000 47.25807  ? 59   TYR   F CD2 1 
ATOM   8303 C CE1 . TYR   D 2 59  ? -10.25200 16.75000  37.32100  1.000 51.64270  ? 59   TYR   F CE1 1 
ATOM   8304 C CE2 . TYR   D 2 59  ? -10.26100 15.39900  35.35100  1.000 46.45947  ? 59   TYR   F CE2 1 
ATOM   8305 C CZ  . TYR   D 2 59  ? -10.93100 15.98100  36.40100  1.000 50.71034  ? 59   TYR   F CZ  1 
ATOM   8306 O OH  . TYR   D 2 59  ? -12.28700 15.79400  36.53000  1.000 56.95782  ? 59   TYR   F OH  1 
ATOM   8307 N N   . ALA   D 2 60  ? -4.50200  18.71000  36.59200  1.000 54.75096  ? 60   ALA   F N   1 
ATOM   8308 C CA  . ALA   D 2 60  ? -3.10600  18.77300  36.99700  1.000 52.58385  ? 60   ALA   F CA  1 
ATOM   8309 C C   . ALA   D 2 60  ? -2.59600  17.36900  37.28800  1.000 56.76274  ? 60   ALA   F C   1 
ATOM   8310 O O   . ALA   D 2 60  ? -3.30400  16.54300  37.87300  1.000 56.49344  ? 60   ALA   F O   1 
ATOM   8311 C CB  . ALA   D 2 60  ? -2.94600  19.66400  38.22900  1.000 45.54597  ? 60   ALA   F CB  1 
ATOM   8312 N N   . ASP   D 2 61  ? -1.35700  17.09900  36.87000  1.000 59.73602  ? 61   ASP   F N   1 
ATOM   8313 C CA  . ASP   D 2 61  ? -0.80200  15.75700  37.02200  1.000 65.35302  ? 61   ASP   F CA  1 
ATOM   8314 C C   . ASP   D 2 61  ? -0.77000  15.32800  38.48400  1.000 66.33467  ? 61   ASP   F C   1 
ATOM   8315 O O   . ASP   D 2 61  ? -0.98800  14.15200  38.79900  1.000 67.08009  ? 61   ASP   F O   1 
ATOM   8316 C CB  . ASP   D 2 61  ? 0.59800   15.69800  36.41100  1.000 73.04451  ? 61   ASP   F CB  1 
ATOM   8317 C CG  . ASP   D 2 61  ? 0.57200   15.67900  34.89300  1.000 90.42699  ? 61   ASP   F CG  1 
ATOM   8318 O OD1 . ASP   D 2 61  ? -0.37200  15.09200  34.32100  1.000 89.05411  ? 61   ASP   F OD1 1 
ATOM   8319 O OD2 . ASP   D 2 61  ? 1.49600   16.24700  34.27200  1.000 119.55411 ? 61   ASP   F OD2 1 
ATOM   8320 N N   . SER   D 2 62  ? -0.51600  16.27300  39.39400  1.000 65.90505  ? 62   SER   F N   1 
ATOM   8321 C CA  . SER   D 2 62  ? -0.46700  15.94200  40.81400  1.000 56.31809  ? 62   SER   F CA  1 
ATOM   8322 C C   . SER   D 2 62  ? -1.83300  15.53400  41.34700  1.000 57.55359  ? 62   SER   F C   1 
ATOM   8323 O O   . SER   D 2 62  ? -1.91500  14.77500  42.32000  1.000 63.93463  ? 62   SER   F O   1 
ATOM   8324 C CB  . SER   D 2 62  ? 0.06800   17.13000  41.61100  1.000 59.00736  ? 62   SER   F CB  1 
ATOM   8325 O OG  . SER   D 2 62  ? -0.38500  18.35500  41.06000  1.000 60.38375  ? 62   SER   F OG  1 
ATOM   8326 N N   . VAL   D 2 63  ? -2.91000  16.02100  40.73300  1.000 55.97356  ? 63   VAL   F N   1 
ATOM   8327 C CA  . VAL   D 2 63  ? -4.26300  15.75800  41.20500  1.000 58.61125  ? 63   VAL   F CA  1 
ATOM   8328 C C   . VAL   D 2 63  ? -5.01600  14.79700  40.30600  1.000 58.84688  ? 63   VAL   F C   1 
ATOM   8329 O O   . VAL   D 2 63  ? -6.20500  14.53800  40.55100  1.000 56.55197  ? 63   VAL   F O   1 
ATOM   8330 C CB  . VAL   D 2 63  ? -5.05600  17.06700  41.37500  1.000 54.77028  ? 63   VAL   F CB  1 
ATOM   8331 C CG1 . VAL   D 2 63  ? -4.22200  18.08400  42.13300  1.000 52.59025  ? 63   VAL   F CG1 1 
ATOM   8332 C CG2 . VAL   D 2 63  ? -5.47800  17.61400  40.02200  1.000 55.48116  ? 63   VAL   F CG2 1 
ATOM   8333 N N   . LYS   D 2 64  ? -4.36900  14.25200  39.27800  1.000 60.66919  ? 64   LYS   F N   1 
ATOM   8334 C CA  . LYS   D 2 64  ? -5.04600  13.34000  38.36800  1.000 62.78771  ? 64   LYS   F CA  1 
ATOM   8335 C C   . LYS   D 2 64  ? -5.45500  12.06800  39.09800  1.000 59.86562  ? 64   LYS   F C   1 
ATOM   8336 O O   . LYS   D 2 64  ? -4.62900  11.40700  39.73300  1.000 64.82659  ? 64   LYS   F O   1 
ATOM   8337 C CB  . LYS   D 2 64  ? -4.13900  13.00400  37.18300  1.000 66.69420  ? 64   LYS   F CB  1 
ATOM   8338 N N   . GLY   D 2 65  ? -6.73800  11.72800  39.00000  1.000 61.40751  ? 65   GLY   F N   1 
ATOM   8339 C CA  . GLY   D 2 65  ? -7.29500  10.58800  39.68900  1.000 64.82045  ? 65   GLY   F CA  1 
ATOM   8340 C C   . GLY   D 2 65  ? -7.82900  10.88800  41.07200  1.000 63.38406  ? 65   GLY   F C   1 
ATOM   8341 O O   . GLY   D 2 65  ? -8.68600  10.14600  41.56900  1.000 59.72680  ? 65   GLY   F O   1 
ATOM   8342 N N   . ARG   D 2 66  ? -7.35300  11.96000  41.70300  1.000 61.57388  ? 66   ARG   F N   1 
ATOM   8343 C CA  . ARG   D 2 66  ? -7.82200  12.33600  43.02900  1.000 63.19752  ? 66   ARG   F CA  1 
ATOM   8344 C C   . ARG   D 2 66  ? -8.94600  13.36300  42.97200  1.000 65.33318  ? 66   ARG   F C   1 
ATOM   8345 O O   . ARG   D 2 66  ? -9.91700  13.25500  43.72800  1.000 68.23936  ? 66   ARG   F O   1 
ATOM   8346 C CB  . ARG   D 2 66  ? -6.65300  12.86800  43.86600  1.000 61.79545  ? 66   ARG   F CB  1 
ATOM   8347 C CG  . ARG   D 2 66  ? -5.50300  11.87900  44.02300  1.000 53.42823  ? 66   ARG   F CG  1 
ATOM   8348 C CD  . ARG   D 2 66  ? -4.47400  12.35700  45.03700  1.000 52.27523  ? 66   ARG   F CD  1 
ATOM   8349 N NE  . ARG   D 2 66  ? -3.72900  13.51900  44.56900  1.000 54.18115  ? 66   ARG   F NE  1 
ATOM   8350 C CZ  . ARG   D 2 66  ? -3.68000  14.68500  45.20000  1.000 56.63071  ? 66   ARG   F CZ  1 
ATOM   8351 N NH1 . ARG   D 2 66  ? -4.31600  14.87900  46.34300  1.000 54.31339  ? 66   ARG   F NH1 1 
ATOM   8352 N NH2 . ARG   D 2 66  ? -2.97000  15.68000  44.67300  1.000 57.36569  ? 66   ARG   F NH2 1 
ATOM   8353 N N   . PHE   D 2 67  ? -8.84600  14.35900  42.09600  1.000 60.45469  ? 67   PHE   F N   1 
ATOM   8354 C CA  . PHE   D 2 67  ? -9.88100  15.37600  41.97200  1.000 60.24051  ? 67   PHE   F CA  1 
ATOM   8355 C C   . PHE   D 2 67  ? -10.70500 15.12800  40.71500  1.000 63.35283  ? 67   PHE   F C   1 
ATOM   8356 O O   . PHE   D 2 67  ? -10.18800 14.66700  39.69200  1.000 62.54899  ? 67   PHE   F O   1 
ATOM   8357 C CB  . PHE   D 2 67  ? -9.29800  16.79500  41.91400  1.000 58.38149  ? 67   PHE   F CB  1 
ATOM   8358 C CG  . PHE   D 2 67  ? -8.48800  17.19900  43.12500  1.000 57.55788  ? 67   PHE   F CG  1 
ATOM   8359 C CD1 . PHE   D 2 67  ? -8.21700  16.30700  44.15300  1.000 60.56180  ? 67   PHE   F CD1 1 
ATOM   8360 C CD2 . PHE   D 2 67  ? -8.00400  18.49200  43.23200  1.000 52.91693  ? 67   PHE   F CD2 1 
ATOM   8361 C CE1 . PHE   D 2 67  ? -7.47000  16.68700  45.24500  1.000 57.21615  ? 67   PHE   F CE1 1 
ATOM   8362 C CE2 . PHE   D 2 67  ? -7.26000  18.88000  44.32600  1.000 53.46842  ? 67   PHE   F CE2 1 
ATOM   8363 C CZ  . PHE   D 2 67  ? -6.99000  17.97300  45.33100  1.000 56.02950  ? 67   PHE   F CZ  1 
ATOM   8364 N N   . THR   D 2 68  ? -11.99500 15.44600  40.80000  1.000 57.64719  ? 68   THR   F N   1 
ATOM   8365 C CA  . THR   D 2 68  ? -12.89500 15.39900  39.65300  1.000 56.42293  ? 68   THR   F CA  1 
ATOM   8366 C C   . THR   D 2 68  ? -13.58400 16.74600  39.50800  1.000 56.69882  ? 68   THR   F C   1 
ATOM   8367 O O   . THR   D 2 68  ? -14.29800 17.18400  40.41800  1.000 53.32818  ? 68   THR   F O   1 
ATOM   8368 C CB  . THR   D 2 68  ? -13.93300 14.28400  39.78800  1.000 54.34309  ? 68   THR   F CB  1 
ATOM   8369 O OG1 . THR   D 2 68  ? -13.31300 13.01600  39.53700  1.000 59.00398  ? 68   THR   F OG1 1 
ATOM   8370 C CG2 . THR   D 2 68  ? -15.06100 14.49300  38.79300  1.000 56.93934  ? 68   THR   F CG2 1 
ATOM   8371 N N   . ILE   D 2 69  ? -13.36200 17.40400  38.37500  1.000 48.04699  ? 69   ILE   F N   1 
ATOM   8372 C CA  . ILE   D 2 69  ? -14.11400 18.59800  38.01800  1.000 44.27205  ? 69   ILE   F CA  1 
ATOM   8373 C C   . ILE   D 2 69  ? -15.40000 18.16500  37.33400  1.000 46.80602  ? 69   ILE   F C   1 
ATOM   8374 O O   . ILE   D 2 69  ? -15.43500 17.15200  36.62300  1.000 51.22468  ? 69   ILE   F O   1 
ATOM   8375 C CB  . ILE   D 2 69  ? -13.28000 19.53800  37.12600  1.000 43.01105  ? 69   ILE   F CB  1 
ATOM   8376 C CG1 . ILE   D 2 69  ? -13.93500 20.91700  37.04400  1.000 41.80763  ? 69   ILE   F CG1 1 
ATOM   8377 C CG2 . ILE   D 2 69  ? -13.08200 18.94300  35.74300  1.000 44.96483  ? 69   ILE   F CG2 1 
ATOM   8378 C CD1 . ILE   D 2 69  ? -13.01300 22.00900  36.57700  1.000 39.07682  ? 69   ILE   F CD1 1 
ATOM   8379 N N   . SER   D 2 70  ? -16.47100 18.91300  37.57800  1.000 46.10203  ? 70   SER   F N   1 
ATOM   8380 C CA  . SER   D 2 70  ? -17.77600 18.59400  37.02200  1.000 43.18812  ? 70   SER   F CA  1 
ATOM   8381 C C   . SER   D 2 70  ? -18.59200 19.87400  36.95900  1.000 45.96603  ? 70   SER   F C   1 
ATOM   8382 O O   . SER   D 2 70  ? -18.26600 20.87100  37.60500  1.000 45.49226  ? 70   SER   F O   1 
ATOM   8383 C CB  . SER   D 2 70  ? -18.50300 17.53200  37.85100  1.000 44.22880  ? 70   SER   F CB  1 
ATOM   8384 O OG  . SER   D 2 70  ? -18.73300 17.98400  39.17400  1.000 48.28938  ? 70   SER   F OG  1 
ATOM   8385 N N   . ARG   D 2 71  ? -19.66400 19.83000  36.18100  1.000 50.72002  ? 71   ARG   F N   1 
ATOM   8386 C CA  . ARG   D 2 71  ? -20.45700 21.01600  35.91300  1.000 49.66237  ? 71   ARG   F CA  1 
ATOM   8387 C C   . ARG   D 2 71  ? -21.93000 20.72300  36.14700  1.000 46.60855  ? 71   ARG   F C   1 
ATOM   8388 O O   . ARG   D 2 71  ? -22.39700 19.60000  35.93800  1.000 47.84807  ? 71   ARG   F O   1 
ATOM   8389 C CB  . ARG   D 2 71  ? -20.24800 21.51400  34.46900  1.000 52.87269  ? 71   ARG   F CB  1 
ATOM   8390 C CG  . ARG   D 2 71  ? -20.85900 22.87300  34.22700  1.000 50.18181  ? 71   ARG   F CG  1 
ATOM   8391 C CD  . ARG   D 2 71  ? -20.73600 23.35600  32.80000  1.000 41.51221  ? 71   ARG   F CD  1 
ATOM   8392 N NE  . ARG   D 2 71  ? -19.37500 23.47000  32.29800  1.000 44.55436  ? 71   ARG   F NE  1 
ATOM   8393 C CZ  . ARG   D 2 71  ? -18.95900 24.48300  31.55200  1.000 47.79692  ? 71   ARG   F CZ  1 
ATOM   8394 N NH1 . ARG   D 2 71  ? -19.74300 25.51900  31.29800  1.000 37.10943  ? 71   ARG   F NH1 1 
ATOM   8395 N NH2 . ARG   D 2 71  ? -17.72500 24.46200  31.05600  1.000 45.59706  ? 71   ARG   F NH2 1 
ATOM   8396 N N   . ASP   D 2 72  ? -22.65400 21.74400  36.60400  1.000 47.47840  ? 72   ASP   F N   1 
ATOM   8397 C CA  . ASP   D 2 72  ? -24.11400 21.72800  36.62600  1.000 53.36896  ? 72   ASP   F CA  1 
ATOM   8398 C C   . ASP   D 2 72  ? -24.60300 23.05700  36.07000  1.000 56.59141  ? 72   ASP   F C   1 
ATOM   8399 O O   . ASP   D 2 72  ? -24.49600 24.09200  36.73700  1.000 51.34834  ? 72   ASP   F O   1 
ATOM   8400 C CB  . ASP   D 2 72  ? -24.66800 21.48900  38.03000  1.000 59.87831  ? 72   ASP   F CB  1 
ATOM   8401 C CG  . ASP   D 2 72  ? -26.18600 21.53400  38.06300  1.000 63.11359  ? 72   ASP   F CG  1 
ATOM   8402 O OD1 . ASP   D 2 72  ? -26.81800 20.66000  37.43200  1.000 68.22089  ? 72   ASP   F OD1 1 
ATOM   8403 O OD2 . ASP   D 2 72  ? -26.75100 22.44000  38.70900  1.000 62.31073  ? 72   ASP   F OD2 1 
ATOM   8404 N N   . ASN   D 2 73  ? -25.13400 23.02000  34.84400  1.000 62.21926  ? 73   ASN   F N   1 
ATOM   8405 C CA  . ASN   D 2 73  ? -25.63000 24.20800  34.16200  1.000 56.53745  ? 73   ASN   F CA  1 
ATOM   8406 C C   . ASN   D 2 73  ? -26.99000 24.66300  34.67000  1.000 63.09689  ? 73   ASN   F C   1 
ATOM   8407 O O   . ASN   D 2 73  ? -27.32900 25.84200  34.51600  1.000 59.65862  ? 73   ASN   F O   1 
ATOM   8408 C CB  . ASN   D 2 73  ? -25.70400 23.93100  32.66200  1.000 54.65186  ? 73   ASN   F CB  1 
ATOM   8409 C CG  . ASN   D 2 73  ? -24.34400 23.71200  32.05500  1.000 51.39442  ? 73   ASN   F CG  1 
ATOM   8410 O OD1 . ASN   D 2 73  ? -23.44500 24.52600  32.23900  1.000 52.83177  ? 73   ASN   F OD1 1 
ATOM   8411 N ND2 . ASN   D 2 73  ? -24.16600 22.58600  31.37400  1.000 53.69657  ? 73   ASN   F ND2 1 
ATOM   8412 N N   . ALA   D 2 74  ? -27.77000 23.76400  35.27100  1.000 62.57640  ? 74   ALA   F N   1 
ATOM   8413 C CA  . ALA   D 2 74  ? -29.06500 24.16200  35.81100  1.000 55.70034  ? 74   ALA   F CA  1 
ATOM   8414 C C   . ALA   D 2 74  ? -28.90900 25.18900  36.92500  1.000 61.72154  ? 74   ALA   F C   1 
ATOM   8415 O O   . ALA   D 2 74  ? -29.74700 26.08400  37.07300  1.000 73.52516  ? 74   ALA   F O   1 
ATOM   8416 C CB  . ALA   D 2 74  ? -29.81800 22.93300  36.31600  1.000 61.68983  ? 74   ALA   F CB  1 
ATOM   8417 N N   . LYS   D 2 75  ? -27.83900 25.08300  37.71400  1.000 58.08761  ? 75   LYS   F N   1 
ATOM   8418 C CA  . LYS   D 2 75  ? -27.65700 25.94300  38.87800  1.000 65.52786  ? 75   LYS   F CA  1 
ATOM   8419 C C   . LYS   D 2 75  ? -26.50600 26.93200  38.72400  1.000 60.80772  ? 75   LYS   F C   1 
ATOM   8420 O O   . LYS   D 2 75  ? -26.17700 27.62800  39.69000  1.000 62.65700  ? 75   LYS   F O   1 
ATOM   8421 C CB  . LYS   D 2 75  ? -27.45500 25.09900  40.13900  1.000 60.03366  ? 75   LYS   F CB  1 
ATOM   8422 N N   . ASN   D 2 76  ? -25.89200 27.01500  37.54000  1.000 54.78310  ? 76   ASN   F N   1 
ATOM   8423 C CA  . ASN   D 2 76  ? -24.80500 27.96500  37.27600  1.000 54.33667  ? 76   ASN   F CA  1 
ATOM   8424 C C   . ASN   D 2 76  ? -23.60200 27.71200  38.18300  1.000 49.41629  ? 76   ASN   F C   1 
ATOM   8425 O O   . ASN   D 2 76  ? -22.97700 28.64800  38.68800  1.000 43.59727  ? 76   ASN   F O   1 
ATOM   8426 C CB  . ASN   D 2 76  ? -25.28100 29.41200  37.42400  1.000 50.06493  ? 76   ASN   F CB  1 
ATOM   8427 C CG  . ASN   D 2 76  ? -26.21400 29.83000  36.32100  1.000 58.68266  ? 76   ASN   F CG  1 
ATOM   8428 O OD1 . ASN   D 2 76  ? -26.54700 29.03600  35.44200  1.000 61.04977  ? 76   ASN   F OD1 1 
ATOM   8429 N ND2 . ASN   D 2 76  ? -26.64800 31.08500  36.35800  1.000 61.35529  ? 76   ASN   F ND2 1 
ATOM   8430 N N   . THR   D 2 77  ? -23.27700 26.43900  38.40000  1.000 45.18944  ? 77   THR   F N   1 
ATOM   8431 C CA  . THR   D 2 77  ? -22.24000 26.07100  39.35300  1.000 49.93961  ? 77   THR   F CA  1 
ATOM   8432 C C   . THR   D 2 77  ? -21.33400 24.99300  38.77700  1.000 47.44423  ? 77   THR   F C   1 
ATOM   8433 O O   . THR   D 2 77  ? -21.77100 24.13000  38.01200  1.000 49.61645  ? 77   THR   F O   1 
ATOM   8434 C CB  . THR   D 2 77  ? -22.83300 25.58100  40.68600  1.000 48.75008  ? 77   THR   F CB  1 
ATOM   8435 O OG1 . THR   D 2 77  ? -23.59500 24.38600  40.46900  1.000 47.66549  ? 77   THR   F OG1 1 
ATOM   8436 C CG2 . THR   D 2 77  ? -23.70300 26.64800  41.32400  1.000 41.03869  ? 77   THR   F CG2 1 
ATOM   8437 N N   . VAL   D 2 78  ? -20.06100 25.05500  39.16900  1.000 43.39958  ? 78   VAL   F N   1 
ATOM   8438 C CA  . VAL   D 2 78  ? -19.04500 24.07700  38.80000  1.000 44.36870  ? 78   VAL   F CA  1 
ATOM   8439 C C   . VAL   D 2 78  ? -18.41600 23.54100  40.08200  1.000 43.59877  ? 78   VAL   F C   1 
ATOM   8440 O O   . VAL   D 2 78  ? -18.20200 24.29200  41.04000  1.000 39.61172  ? 78   VAL   F O   1 
ATOM   8441 C CB  . VAL   D 2 78  ? -17.98600 24.69300  37.85600  1.000 40.35080  ? 78   VAL   F CB  1 
ATOM   8442 C CG1 . VAL   D 2 78  ? -17.34700 25.91900  38.48700  1.000 44.29933  ? 78   VAL   F CG1 1 
ATOM   8443 C CG2 . VAL   D 2 78  ? -16.92100 23.67200  37.48000  1.000 39.88484  ? 78   VAL   F CG2 1 
ATOM   8444 N N   . TYR   D 2 79  ? -18.13600 22.23800  40.10200  1.000 42.58457  ? 79   TYR   F N   1 
ATOM   8445 C CA  . TYR   D 2 79  ? -17.75700 21.52700  41.31500  1.000 40.00450  ? 79   TYR   F CA  1 
ATOM   8446 C C   . TYR   D 2 79  ? -16.37800 20.90400  41.15800  1.000 47.13735  ? 79   TYR   F C   1 
ATOM   8447 O O   . TYR   D 2 79  ? -16.08700 20.27200  40.13700  1.000 45.97686  ? 79   TYR   F O   1 
ATOM   8448 C CB  . TYR   D 2 79  ? -18.77800 20.43000  41.64700  1.000 49.07272  ? 79   TYR   F CB  1 
ATOM   8449 C CG  . TYR   D 2 79  ? -20.17000 20.94100  41.96300  1.000 57.01631  ? 79   TYR   F CG  1 
ATOM   8450 C CD1 . TYR   D 2 79  ? -20.50900 21.33500  43.24800  1.000 51.67754  ? 79   TYR   F CD1 1 
ATOM   8451 C CD2 . TYR   D 2 79  ? -21.14500 21.02400  40.97300  1.000 54.73799  ? 79   TYR   F CD2 1 
ATOM   8452 C CE1 . TYR   D 2 79  ? -21.77600 21.80100  43.54300  1.000 60.52532  ? 79   TYR   F CE1 1 
ATOM   8453 C CE2 . TYR   D 2 79  ? -22.41600 21.48900  41.25700  1.000 54.01600  ? 79   TYR   F CE2 1 
ATOM   8454 C CZ  . TYR   D 2 79  ? -22.72600 21.87700  42.54600  1.000 66.03307  ? 79   TYR   F CZ  1 
ATOM   8455 O OH  . TYR   D 2 79  ? -23.98900 22.34200  42.84700  1.000 68.31083  ? 79   TYR   F OH  1 
ATOM   8456 N N   . LEU   D 2 80  ? -15.53600 21.07600  42.17600  1.000 54.80991  ? 80   LEU   F N   1 
ATOM   8457 C CA  . LEU   D 2 80  ? -14.29400 20.32300  42.31500  1.000 51.96458  ? 80   LEU   F CA  1 
ATOM   8458 C C   . LEU   D 2 80  ? -14.44900 19.39900  43.51600  1.000 47.14691  ? 80   LEU   F C   1 
ATOM   8459 O O   . LEU   D 2 80  ? -14.59500 19.86500  44.65100  1.000 42.77283  ? 80   LEU   F O   1 
ATOM   8460 C CB  . LEU   D 2 80  ? -13.08600 21.24500  42.48200  1.000 47.54218  ? 80   LEU   F CB  1 
ATOM   8461 C CG  . LEU   D 2 80  ? -11.74400 20.50900  42.56600  1.000 43.83869  ? 80   LEU   F CG  1 
ATOM   8462 C CD1 . LEU   D 2 80  ? -11.52100 19.67000  41.32100  1.000 51.39870  ? 80   LEU   F CD1 1 
ATOM   8463 C CD2 . LEU   D 2 80  ? -10.58800 21.47800  42.77000  1.000 39.69726  ? 80   LEU   F CD2 1 
ATOM   8464 N N   . GLN   D 2 81  ? -14.43300 18.09500  43.26000  1.000 45.36760  ? 81   GLN   F N   1 
ATOM   8465 C CA  . GLN   D 2 81  ? -14.52500 17.08600  44.31000  1.000 46.95143  ? 81   GLN   F CA  1 
ATOM   8466 C C   . GLN   D 2 81  ? -13.10300 16.63800  44.62400  1.000 57.31182  ? 81   GLN   F C   1 
ATOM   8467 O O   . GLN   D 2 81  ? -12.51900 15.83100  43.89500  1.000 60.89449  ? 81   GLN   F O   1 
ATOM   8468 C CB  . GLN   D 2 81  ? -15.40600 15.92000  43.87600  1.000 46.50846  ? 81   GLN   F CB  1 
ATOM   8469 C CG  . GLN   D 2 81  ? -15.56800 14.83500  44.92900  1.000 50.42324  ? 81   GLN   F CG  1 
ATOM   8470 C CD  . GLN   D 2 81  ? -16.14600 15.36600  46.23100  1.000 62.30531  ? 81   GLN   F CD  1 
ATOM   8471 O OE1 . GLN   D 2 81  ? -17.30200 15.79500  46.28300  1.000 54.30582  ? 81   GLN   F OE1 1 
ATOM   8472 N NE2 . GLN   D 2 81  ? -15.34500 15.33400  47.29200  1.000 62.73502  ? 81   GLN   F NE2 1 
ATOM   8473 N N   . MET   D 2 82  ? -12.54200 17.18100  45.70200  1.000 58.30704  ? 82   MET   F N   1 
ATOM   8474 C CA  . MET   D 2 82  ? -11.18500 16.85000  46.12700  1.000 56.09554  ? 82   MET   F CA  1 
ATOM   8475 C C   . MET   D 2 82  ? -11.22500 15.56500  46.94500  1.000 59.91051  ? 82   MET   F C   1 
ATOM   8476 O O   . MET   D 2 82  ? -11.76700 15.54400  48.05400  1.000 58.90200  ? 82   MET   F O   1 
ATOM   8477 C CB  . MET   D 2 82  ? -10.58900 17.99700  46.93800  1.000 48.93493  ? 82   MET   F CB  1 
ATOM   8478 C CG  . MET   D 2 82  ? -10.81400 19.36700  46.34800  1.000 46.64398  ? 82   MET   F CG  1 
ATOM   8479 S SD  . MET   D 2 82  ? -9.97300  20.64300  47.29300  1.000 51.73286  ? 82   MET   F SD  1 
ATOM   8480 C CE  . MET   D 2 82  ? -8.43500  19.83400  47.71700  1.000 50.91685  ? 82   MET   F CE  1 
ATOM   8481 N N   . ASN   D 2 83  ? -10.64600 14.49500  46.40900  1.000 58.31706  ? 83   ASN   F N   1 
ATOM   8482 C CA  . ASN   D 2 83  ? -10.67700 13.19000  47.05000  1.000 59.64967  ? 83   ASN   F CA  1 
ATOM   8483 C C   . ASN   D 2 83  ? -9.25500  12.69200  47.25600  1.000 62.54179  ? 83   ASN   F C   1 
ATOM   8484 O O   . ASN   D 2 83  ? -8.34300  13.05200  46.50600  1.000 62.98217  ? 83   ASN   F O   1 
ATOM   8485 C CB  . ASN   D 2 83  ? -11.47400 12.18000  46.21300  1.000 61.28812  ? 83   ASN   F CB  1 
ATOM   8486 C CG  . ASN   D 2 83  ? -12.97400 12.36000  46.35500  1.000 66.18292  ? 83   ASN   F CG  1 
ATOM   8487 O OD1 . ASN   D 2 83  ? -13.44000 13.21100  47.11300  1.000 67.81845  ? 83   ASN   F OD1 1 
ATOM   8488 N ND2 . ASN   D 2 83  ? -13.73900 11.56300  45.61400  1.000 62.41148  ? 83   ASN   F ND2 1 
ATOM   8489 N N   . SER   D 2 84  ? -9.08000  11.85600  48.28400  1.000 64.18910  ? 84   SER   F N   1 
ATOM   8490 C CA  . SER   D 2 84  ? -7.77000  11.32600  48.66800  1.000 55.47513  ? 84   SER   F CA  1 
ATOM   8491 C C   . SER   D 2 84  ? -6.79400  12.46200  48.96700  1.000 57.53035  ? 84   SER   F C   1 
ATOM   8492 O O   . SER   D 2 84  ? -5.69700  12.53200  48.40700  1.000 61.09717  ? 84   SER   F O   1 
ATOM   8493 C CB  . SER   D 2 84  ? -7.21000  10.39500  47.58900  1.000 50.27617  ? 84   SER   F CB  1 
ATOM   8494 O OG  . SER   D 2 84  ? -8.14500  9.38800   47.24700  1.000 55.97204  ? 84   SER   F OG  1 
ATOM   8495 N N   . LEU   D 2 85  ? -7.20300  13.35800  49.86400  1.000 53.97645  ? 85   LEU   F N   1 
ATOM   8496 C CA  . LEU   D 2 85  ? -6.44300  14.58100  50.08700  1.000 59.00426  ? 85   LEU   F CA  1 
ATOM   8497 C C   . LEU   D 2 85  ? -5.06000  14.28600  50.65600  1.000 59.66904  ? 85   LEU   F C   1 
ATOM   8498 O O   . LEU   D 2 85  ? -4.85600  13.33600  51.41600  1.000 58.86336  ? 85   LEU   F O   1 
ATOM   8499 C CB  . LEU   D 2 85  ? -7.19900  15.53300  51.01700  1.000 58.07585  ? 85   LEU   F CB  1 
ATOM   8500 C CG  . LEU   D 2 85  ? -8.49300  16.13700  50.47000  1.000 55.31796  ? 85   LEU   F CG  1 
ATOM   8501 C CD1 . LEU   D 2 85  ? -8.71700  17.53000  51.03100  1.000 51.97754  ? 85   LEU   F CD1 1 
ATOM   8502 C CD2 . LEU   D 2 85  ? -8.44200  16.18300  48.96100  1.000 56.96378  ? 85   LEU   F CD2 1 
ATOM   8503 N N   . LYS   D 2 86  ? -4.10300  15.11700  50.25700  1.000 58.86202  ? 86   LYS   F N   1 
ATOM   8504 C CA  . LYS   D 2 86  ? -2.73000  15.05400  50.72200  1.000 56.37875  ? 86   LYS   F CA  1 
ATOM   8505 C C   . LYS   D 2 86  ? -2.34900  16.42100  51.26800  1.000 56.95851  ? 86   LYS   F C   1 
ATOM   8506 O O   . LYS   D 2 86  ? -2.94400  17.43800  50.89900  1.000 54.34981  ? 86   LYS   F O   1 
ATOM   8507 C CB  . LYS   D 2 86  ? -1.77700  14.63800  49.58600  1.000 60.86438  ? 86   LYS   F CB  1 
ATOM   8508 C CG  . LYS   D 2 86  ? -2.28600  13.45000  48.77400  1.000 62.02145  ? 86   LYS   F CG  1 
ATOM   8509 C CD  . LYS   D 2 86  ? -1.22800  12.87400  47.84300  1.000 55.13888  ? 86   LYS   F CD  1 
ATOM   8510 C CE  . LYS   D 2 86  ? -0.64500  13.92900  46.92400  1.000 62.45614  ? 86   LYS   F CE  1 
ATOM   8511 N NZ  . LYS   D 2 86  ? -0.52900  13.42300  45.52200  1.000 70.56767  ? 86   LYS   F NZ  1 
ATOM   8512 N N   . ALA   D 2 87  ? -1.36000  16.43900  52.16400  1.000 57.24153  ? 87   ALA   F N   1 
ATOM   8513 C CA  . ALA   D 2 87  ? -0.94700  17.70200  52.76900  1.000 59.78263  ? 87   ALA   F CA  1 
ATOM   8514 C C   . ALA   D 2 87  ? -0.43600  18.68700  51.72500  1.000 58.17077  ? 87   ALA   F C   1 
ATOM   8515 O O   . ALA   D 2 87  ? -0.51400  19.90500  51.93000  1.000 52.25090  ? 87   ALA   F O   1 
ATOM   8516 C CB  . ALA   D 2 87  ? 0.11800   17.45100  53.83600  1.000 65.05852  ? 87   ALA   F CB  1 
ATOM   8517 N N   . GLU   D 2 88  ? 0.07700   18.18400  50.60000  1.000 55.74311  ? 88   GLU   F N   1 
ATOM   8518 C CA  . GLU   D 2 88  ? 0.55200   19.05900  49.53600  1.000 46.97499  ? 88   GLU   F CA  1 
ATOM   8519 C C   . GLU   D 2 88  ? -0.57400  19.85000  48.88100  1.000 51.81876  ? 88   GLU   F C   1 
ATOM   8520 O O   . GLU   D 2 88  ? -0.30300  20.88300  48.26100  1.000 55.54327  ? 88   GLU   F O   1 
ATOM   8521 C CB  . GLU   D 2 88  ? 1.29300   18.24100  48.48000  1.000 48.31455  ? 88   GLU   F CB  1 
ATOM   8522 C CG  . GLU   D 2 88  ? 2.70300   17.84100  48.88000  1.000 62.30574  ? 88   GLU   F CG  1 
ATOM   8523 C CD  . GLU   D 2 88  ? 3.76300   18.55300  48.06000  1.000 70.75715  ? 88   GLU   F CD  1 
ATOM   8524 O OE1 . GLU   D 2 88  ? 3.90900   19.78500  48.21500  1.000 63.20802  ? 88   GLU   F OE1 1 
ATOM   8525 O OE2 . GLU   D 2 88  ? 4.44300   17.88200  47.25300  1.000 77.36075  ? 88   GLU   F OE2 1 
ATOM   8526 N N   . ASP   D 2 89  ? -1.82500  19.40100  49.00900  1.000 54.37838  ? 89   ASP   F N   1 
ATOM   8527 C CA  . ASP   D 2 89  ? -2.96900  20.08100  48.41000  1.000 51.56124  ? 89   ASP   F CA  1 
ATOM   8528 C C   . ASP   D 2 89  ? -3.38600  21.33900  49.16600  1.000 46.39083  ? 89   ASP   F C   1 
ATOM   8529 O O   . ASP   D 2 89  ? -4.43800  21.90800  48.85400  1.000 42.45853  ? 89   ASP   F O   1 
ATOM   8530 C CB  . ASP   D 2 89  ? -4.16400  19.12600  48.30600  1.000 47.17940  ? 89   ASP   F CB  1 
ATOM   8531 C CG  . ASP   D 2 89  ? -3.87800  17.92100  47.42400  1.000 60.13460  ? 89   ASP   F CG  1 
ATOM   8532 O OD1 . ASP   D 2 89  ? -3.37300  18.11000  46.29500  1.000 60.43858  ? 89   ASP   F OD1 1 
ATOM   8533 O OD2 . ASP   D 2 89  ? -4.16900  16.78500  47.85500  1.000 62.37909  ? 89   ASP   F OD2 1 
ATOM   8534 N N   . THR   D 2 90  ? -2.59400  21.79100  50.13500  1.000 48.46582  ? 90   THR   F N   1 
ATOM   8535 C CA  . THR   D 2 90  ? -2.94800  22.95300  50.94300  1.000 49.69841  ? 90   THR   F CA  1 
ATOM   8536 C C   . THR   D 2 90  ? -2.69800  24.22200  50.13500  1.000 44.33557  ? 90   THR   F C   1 
ATOM   8537 O O   . THR   D 2 90  ? -1.54600  24.55100  49.82500  1.000 40.58269  ? 90   THR   F O   1 
ATOM   8538 C CB  . THR   D 2 90  ? -2.14500  22.95600  52.24200  1.000 46.17206  ? 90   THR   F CB  1 
ATOM   8539 O OG1 . THR   D 2 90  ? -2.35700  21.71900  52.93300  1.000 45.38070  ? 90   THR   F OG1 1 
ATOM   8540 C CG2 . THR   D 2 90  ? -2.56300  24.11400  53.13700  1.000 36.49746  ? 90   THR   F CG2 1 
ATOM   8541 N N   . ALA   D 2 91  ? -3.77000  24.94600  49.81600  1.000 37.26891  ? 91   ALA   F N   1 
ATOM   8542 C CA  . ALA   D 2 91  ? -3.67200  26.14200  48.99000  1.000 36.83787  ? 91   ALA   F CA  1 
ATOM   8543 C C   . ALA   D 2 91  ? -4.99600  26.89000  49.03200  1.000 33.26665  ? 91   ALA   F C   1 
ATOM   8544 O O   . ALA   D 2 91  ? -6.03300  26.33200  49.39800  1.000 39.76969  ? 91   ALA   F O   1 
ATOM   8545 C CB  . ALA   D 2 91  ? -3.31300  25.79300  47.54200  1.000 41.61919  ? 91   ALA   F CB  1 
ATOM   8546 N N   . VAL   D 2 92  ? -4.94700  28.16100  48.64900  1.000 29.26448  ? 92   VAL   F N   1 
ATOM   8547 C CA  . VAL   D 2 92  ? -6.16400  28.91000  48.35600  1.000 37.57356  ? 92   VAL   F CA  1 
ATOM   8548 C C   . VAL   D 2 92  ? -6.63700  28.50700  46.96500  1.000 40.63623  ? 92   VAL   F C   1 
ATOM   8549 O O   . VAL   D 2 92  ? -5.92700  28.70800  45.97400  1.000 39.20235  ? 92   VAL   F O   1 
ATOM   8550 C CB  . VAL   D 2 92  ? -5.92600  30.42400  48.43600  1.000 33.98098  ? 92   VAL   F CB  1 
ATOM   8551 C CG1 . VAL   D 2 92  ? -7.13400  31.17000  47.89000  1.000 38.21651  ? 92   VAL   F CG1 1 
ATOM   8552 C CG2 . VAL   D 2 92  ? -5.64000  30.84300  49.85300  1.000 30.05192  ? 92   VAL   F CG2 1 
ATOM   8553 N N   . TYR   D 2 93  ? -7.83000  27.93000  46.88500  1.000 37.82075  ? 93   TYR   F N   1 
ATOM   8554 C CA  . TYR   D 2 93  ? -8.35700  27.46900  45.61100  1.000 34.61784  ? 93   TYR   F CA  1 
ATOM   8555 C C   . TYR   D 2 93  ? -9.23200  28.54400  44.98900  1.000 44.01204  ? 93   TYR   F C   1 
ATOM   8556 O O   . TYR   D 2 93  ? -10.01400 29.20600  45.67900  1.000 43.05507  ? 93   TYR   F O   1 
ATOM   8557 C CB  . TYR   D 2 93  ? -9.14200  26.16800  45.77300  1.000 30.53903  ? 93   TYR   F CB  1 
ATOM   8558 C CG  . TYR   D 2 93  ? -8.24900  24.96800  45.96200  1.000 33.25078  ? 93   TYR   F CG  1 
ATOM   8559 C CD1 . TYR   D 2 93  ? -7.24200  24.97200  46.91300  1.000 36.57542  ? 93   TYR   F CD1 1 
ATOM   8560 C CD2 . TYR   D 2 93  ? -8.38600  23.84500  45.16200  1.000 37.39440  ? 93   TYR   F CD2 1 
ATOM   8561 C CE1 . TYR   D 2 93  ? -6.41300  23.88600  47.08100  1.000 40.88030  ? 93   TYR   F CE1 1 
ATOM   8562 C CE2 . TYR   D 2 93  ? -7.56100  22.75000  45.32200  1.000 40.19977  ? 93   TYR   F CE2 1 
ATOM   8563 C CZ  . TYR   D 2 93  ? -6.57400  22.77800  46.28300  1.000 43.41589  ? 93   TYR   F CZ  1 
ATOM   8564 O OH  . TYR   D 2 93  ? -5.74300  21.69300  46.45000  1.000 44.97310  ? 93   TYR   F OH  1 
ATOM   8565 N N   . TYR   D 2 94  ? -9.08200  28.72000  43.67800  1.000 45.42819  ? 94   TYR   F N   1 
ATOM   8566 C CA  . TYR   D 2 94  ? -9.74900  29.78300  42.94600  1.000 40.90205  ? 94   TYR   F CA  1 
ATOM   8567 C C   . TYR   D 2 94  ? -10.64500 29.20800  41.86200  1.000 43.71282  ? 94   TYR   F C   1 
ATOM   8568 O O   . TYR   D 2 94  ? -10.30900 28.20700  41.22000  1.000 40.13118  ? 94   TYR   F O   1 
ATOM   8569 C CB  . TYR   D 2 94  ? -8.74000  30.73800  42.31600  1.000 43.53994  ? 94   TYR   F CB  1 
ATOM   8570 C CG  . TYR   D 2 94  ? -8.06600  31.64200  43.31300  1.000 42.19123  ? 94   TYR   F CG  1 
ATOM   8571 C CD1 . TYR   D 2 94  ? -8.72100  32.75600  43.82100  1.000 39.25740  ? 94   TYR   F CD1 1 
ATOM   8572 C CD2 . TYR   D 2 94  ? -6.77000  31.38700  43.74400  1.000 41.24859  ? 94   TYR   F CD2 1 
ATOM   8573 C CE1 . TYR   D 2 94  ? -8.10500  33.58800  44.74000  1.000 42.60366  ? 94   TYR   F CE1 1 
ATOM   8574 C CE2 . TYR   D 2 94  ? -6.14500  32.21300  44.65800  1.000 42.57204  ? 94   TYR   F CE2 1 
ATOM   8575 C CZ  . TYR   D 2 94  ? -6.81700  33.31200  45.15300  1.000 41.27846  ? 94   TYR   F CZ  1 
ATOM   8576 O OH  . TYR   D 2 94  ? -6.19800  34.13900  46.06300  1.000 45.11256  ? 94   TYR   F OH  1 
ATOM   8577 N N   . CYS   D 2 95  ? -11.78600 29.85900  41.67400  1.000 45.84150  ? 95   CYS   F N   1 
ATOM   8578 C CA  . CYS   D 2 95  ? -12.72200 29.56800  40.60000  1.000 40.51201  ? 95   CYS   F CA  1 
ATOM   8579 C C   . CYS   D 2 95  ? -12.47900 30.55200  39.46600  1.000 45.68088  ? 95   CYS   F C   1 
ATOM   8580 O O   . CYS   D 2 95  ? -12.41300 31.76400  39.70000  1.000 43.35227  ? 95   CYS   F O   1 
ATOM   8581 C CB  . CYS   D 2 95  ? -14.15500 29.67800  41.11400  1.000 47.19659  ? 95   CYS   F CB  1 
ATOM   8582 S SG  . CYS   D 2 95  ? -15.45500 29.74500  39.87500  1.000 72.55622  ? 95   CYS   F SG  1 
ATOM   8583 N N   . ASN   D 2 96  ? -12.33000 30.03300  38.24800  1.000 41.52350  ? 96   ASN   F N   1 
ATOM   8584 C CA  . ASN   D 2 96  ? -12.05200 30.84600  37.07100  1.000 41.64502  ? 96   ASN   F CA  1 
ATOM   8585 C C   . ASN   D 2 96  ? -13.18700 30.70400  36.06700  1.000 39.77246  ? 96   ASN   F C   1 
ATOM   8586 O O   . ASN   D 2 96  ? -13.69500 29.60200  35.83900  1.000 39.88894  ? 96   ASN   F O   1 
ATOM   8587 C CB  . ASN   D 2 96  ? -10.71900 30.44600  36.41000  1.000 40.85785  ? 96   ASN   F CB  1 
ATOM   8588 C CG  . ASN   D 2 96  ? -10.42800 31.23900  35.13100  1.000 40.34444  ? 96   ASN   F CG  1 
ATOM   8589 O OD1 . ASN   D 2 96  ? -10.92100 32.35100  34.94300  1.000 40.85783  ? 96   ASN   F OD1 1 
ATOM   8590 N ND2 . ASN   D 2 96  ? -9.63200  30.65400  34.24300  1.000 41.53581  ? 96   ASN   F ND2 1 
ATOM   8591 N N   . ALA   D 2 97  ? -13.57500 31.82300  35.46600  1.000 39.15552  ? 97   ALA   F N   1 
ATOM   8592 C CA  . ALA   D 2 97  ? -14.53300 31.83700  34.37400  1.000 43.43190  ? 97   ALA   F CA  1 
ATOM   8593 C C   . ALA   D 2 97  ? -13.90200 32.51300  33.16500  1.000 40.05163  ? 97   ALA   F C   1 
ATOM   8594 O O   . ALA   D 2 97  ? -13.23400 33.54200  33.29600  1.000 39.70493  ? 97   ALA   F O   1 
ATOM   8595 C CB  . ALA   D 2 97  ? -15.82600 32.56200  34.77300  1.000 41.25943  ? 97   ALA   F CB  1 
ATOM   8596 N N   . LYS   D 2 98  ? -14.10300 31.92500  31.99100  1.000 45.03711  ? 98   LYS   F N   1 
ATOM   8597 C CA  . LYS   D 2 98  ? -13.62300 32.49800  30.73600  1.000 43.66521  ? 98   LYS   F CA  1 
ATOM   8598 C C   . LYS   D 2 98  ? -14.84600 32.81300  29.87800  1.000 42.68687  ? 98   LYS   F C   1 
ATOM   8599 O O   . LYS   D 2 98  ? -15.48000 31.90800  29.32700  1.000 42.67194  ? 98   LYS   F O   1 
ATOM   8600 C CB  . LYS   D 2 98  ? -12.64100 31.55500  30.04100  1.000 29.64036  ? 98   LYS   F CB  1 
ATOM   8601 C CG  . LYS   D 2 98  ? -11.33100 31.44800  30.79600  1.000 37.73004  ? 98   LYS   F CG  1 
ATOM   8602 C CD  . LYS   D 2 98  ? -10.26000 30.66500  30.06700  1.000 37.87249  ? 98   LYS   F CD  1 
ATOM   8603 C CE  . LYS   D 2 98  ? -8.92200  30.82000  30.78400  1.000 32.77116  ? 98   LYS   F CE  1 
ATOM   8604 N NZ  . LYS   D 2 98  ? -7.76700  30.33600  29.97700  1.000 54.03113  ? 98   LYS   F NZ  1 
ATOM   8605 N N   . VAL   D 2 99  ? -15.17400 34.09900  29.77900  1.000 38.88569  ? 99   VAL   F N   1 
ATOM   8606 C CA  . VAL   D 2 99  ? -16.36800 34.57100  29.09000  1.000 37.61059  ? 99   VAL   F CA  1 
ATOM   8607 C C   . VAL   D 2 99  ? -15.93600 35.29600  27.82500  1.000 42.31724  ? 99   VAL   F C   1 
ATOM   8608 O O   . VAL   D 2 99  ? -15.14900 36.25000  27.88200  1.000 35.93195  ? 99   VAL   F O   1 
ATOM   8609 C CB  . VAL   D 2 99  ? -17.21300 35.49000  29.98200  1.000 39.78243  ? 99   VAL   F CB  1 
ATOM   8610 C CG1 . VAL   D 2 99  ? -18.53700 35.78700  29.30800  1.000 42.37841  ? 99   VAL   F CG1 1 
ATOM   8611 C CG2 . VAL   D 2 99  ? -17.43200 34.85100  31.34100  1.000 37.66623  ? 99   VAL   F CG2 1 
ATOM   8612 N N   . ALA   D 2 100 ? -16.46600 34.86200  26.68800  1.000 44.62022  ? 100  ALA   F N   1 
ATOM   8613 C CA  . ALA   D 2 100 ? -16.06900 35.43300  25.41100  1.000 38.46656  ? 100  ALA   F CA  1 
ATOM   8614 C C   . ALA   D 2 100 ? -16.91800 36.65500  25.08800  1.000 32.41425  ? 100  ALA   F C   1 
ATOM   8615 O O   . ALA   D 2 100 ? -18.14700 36.62100  25.19800  1.000 33.78725  ? 100  ALA   F O   1 
ATOM   8616 C CB  . ALA   D 2 100 ? -16.19000 34.39100  24.29900  1.000 46.44719  ? 100  ALA   F CB  1 
ATOM   8617 N N   . GLY   D 2 101 ? -16.25600 37.73700  24.69500  1.000 37.42783  ? 101  GLY   F N   1 
ATOM   8618 C CA  . GLY   D 2 101 ? -16.94800 38.92100  24.23800  1.000 32.94049  ? 101  GLY   F CA  1 
ATOM   8619 C C   . GLY   D 2 101 ? -16.87800 39.07100  22.73300  1.000 43.57032  ? 101  GLY   F C   1 
ATOM   8620 O O   . GLY   D 2 101 ? -17.02600 38.09000  21.99500  1.000 48.39325  ? 101  GLY   F O   1 
ATOM   8621 N N   . THR   D 2 102 ? -16.64300 40.29400  22.25900  1.000 42.94029  ? 102  THR   F N   1 
ATOM   8622 C CA  . THR   D 2 102 ? -16.62400 40.52900  20.81700  1.000 41.02709  ? 102  THR   F CA  1 
ATOM   8623 C C   . THR   D 2 102 ? -15.33500 40.00300  20.19400  1.000 40.60104  ? 102  THR   F C   1 
ATOM   8624 O O   . THR   D 2 102 ? -15.33500 38.96500  19.52700  1.000 47.12628  ? 102  THR   F O   1 
ATOM   8625 C CB  . THR   D 2 102 ? -16.81300 42.01800  20.51900  1.000 42.26660  ? 102  THR   F CB  1 
ATOM   8626 O OG1 . THR   D 2 102 ? -18.01800 42.47700  21.14500  1.000 39.22473  ? 102  THR   F OG1 1 
ATOM   8627 C CG2 . THR   D 2 102 ? -16.91300 42.23800  19.01800  1.000 40.51028  ? 102  THR   F CG2 1 
ATOM   8628 N N   . PHE   D 2 103 ? -14.22300 40.70400  20.40800  1.000 40.81523  ? 103  PHE   F N   1 
ATOM   8629 C CA  . PHE   D 2 103 ? -12.95500 40.32200  19.80300  1.000 40.61293  ? 103  PHE   F CA  1 
ATOM   8630 C C   . PHE   D 2 103 ? -12.04700 39.54200  20.74500  1.000 41.59062  ? 103  PHE   F C   1 
ATOM   8631 O O   . PHE   D 2 103 ? -10.97400 39.10500  20.31800  1.000 40.91204  ? 103  PHE   F O   1 
ATOM   8632 C CB  . PHE   D 2 103 ? -12.20600 41.55900  19.29200  1.000 40.01741  ? 103  PHE   F CB  1 
ATOM   8633 C CG  . PHE   D 2 103 ? -12.97800 42.36500  18.28700  1.000 36.13221  ? 103  PHE   F CG  1 
ATOM   8634 C CD1 . PHE   D 2 103 ? -13.66900 41.74000  17.26500  1.000 39.71359  ? 103  PHE   F CD1 1 
ATOM   8635 C CD2 . PHE   D 2 103 ? -12.98700 43.74900  18.34800  1.000 30.89558  ? 103  PHE   F CD2 1 
ATOM   8636 C CE1 . PHE   D 2 103 ? -14.37700 42.47600  16.33400  1.000 39.03349  ? 103  PHE   F CE1 1 
ATOM   8637 C CE2 . PHE   D 2 103 ? -13.68800 44.49100  17.42000  1.000 42.33876  ? 103  PHE   F CE2 1 
ATOM   8638 C CZ  . PHE   D 2 103 ? -14.38600 43.85400  16.41100  1.000 44.55167  ? 103  PHE   F CZ  1 
ATOM   8639 N N   . SER   D 2 104 ? -12.43800 39.35000  22.00400  1.000 45.07226  ? 104  SER   F N   1 
ATOM   8640 C CA  . SER   D 2 104 ? -11.55300 38.70700  22.96400  1.000 44.70285  ? 104  SER   F CA  1 
ATOM   8641 C C   . SER   D 2 104 ? -12.36300 37.94000  23.99700  1.000 43.54715  ? 104  SER   F C   1 
ATOM   8642 O O   . SER   D 2 104 ? -13.57300 38.12800  24.13700  1.000 40.90141  ? 104  SER   F O   1 
ATOM   8643 C CB  . SER   D 2 104 ? -10.65400 39.72500  23.67400  1.000 48.57649  ? 104  SER   F CB  1 
ATOM   8644 O OG  . SER   D 2 104 ? -11.42800 40.73300  24.30500  1.000 53.73242  ? 104  SER   F OG  1 
ATOM   8645 N N   . ILE   D 2 105 ? -11.66600 37.07400  24.72900  1.000 41.62913  ? 105  ILE   F N   1 
ATOM   8646 C CA  . ILE   D 2 105 ? -12.22800 36.34600  25.86100  1.000 44.58159  ? 105  ILE   F CA  1 
ATOM   8647 C C   . ILE   D 2 105 ? -11.76700 37.02100  27.14600  1.000 46.01159  ? 105  ILE   F C   1 
ATOM   8648 O O   . ILE   D 2 105 ? -10.62300 37.48300  27.24200  1.000 44.38185  ? 105  ILE   F O   1 
ATOM   8649 C CB  . ILE   D 2 105 ? -11.80300 34.86600  25.83000  1.000 41.93104  ? 105  ILE   F CB  1 
ATOM   8650 C CG1 . ILE   D 2 105 ? -12.18800 34.23000  24.49700  1.000 36.62721  ? 105  ILE   F CG1 1 
ATOM   8651 C CG2 . ILE   D 2 105 ? -12.42200 34.10200  26.99400  1.000 37.92941  ? 105  ILE   F CG2 1 
ATOM   8652 C CD1 . ILE   D 2 105 ? -11.67600 32.82500  24.34400  1.000 39.97384  ? 105  ILE   F CD1 1 
ATOM   8653 N N   . TYR   D 2 106 ? -12.65400 37.08000  28.13600  1.000 45.36178  ? 106  TYR   F N   1 
ATOM   8654 C CA  . TYR   D 2 106 ? -12.36500 37.72200  29.41000  1.000 39.42579  ? 106  TYR   F CA  1 
ATOM   8655 C C   . TYR   D 2 106 ? -12.21900 36.68600  30.51500  1.000 39.36779  ? 106  TYR   F C   1 
ATOM   8656 O O   . TYR   D 2 106 ? -12.89700 35.65500  30.51800  1.000 39.73145  ? 106  TYR   F O   1 
ATOM   8657 C CB  . TYR   D 2 106 ? -13.46000 38.72500  29.77300  1.000 34.33162  ? 106  TYR   F CB  1 
ATOM   8658 C CG  . TYR   D 2 106 ? -13.51800 39.88000  28.81200  1.000 38.03294  ? 106  TYR   F CG  1 
ATOM   8659 C CD1 . TYR   D 2 106 ? -12.71000 40.99200  28.99300  1.000 42.83077  ? 106  TYR   F CD1 1 
ATOM   8660 C CD2 . TYR   D 2 106 ? -14.35600 39.84900  27.70500  1.000 40.97111  ? 106  TYR   F CD2 1 
ATOM   8661 C CE1 . TYR   D 2 106 ? -12.74300 42.05200  28.10800  1.000 47.57242  ? 106  TYR   F CE1 1 
ATOM   8662 C CE2 . TYR   D 2 106 ? -14.39900 40.90700  26.81300  1.000 40.44304  ? 106  TYR   F CE2 1 
ATOM   8663 C CZ  . TYR   D 2 106 ? -13.58900 42.00500  27.02000  1.000 44.93308  ? 106  TYR   F CZ  1 
ATOM   8664 O OH  . TYR   D 2 106 ? -13.61600 43.06400  26.14200  1.000 41.80767  ? 106  TYR   F OH  1 
ATOM   8665 N N   . ASP   D 2 107 ? -11.32000 36.97000  31.45300  1.000 40.41943  ? 107  ASP   F N   1 
ATOM   8666 C CA  . ASP   D 2 107 ? -11.05800 36.08900  32.58100  1.000 37.85233  ? 107  ASP   F CA  1 
ATOM   8667 C C   . ASP   D 2 107 ? -11.66200 36.66900  33.85000  1.000 42.38027  ? 107  ASP   F C   1 
ATOM   8668 O O   . ASP   D 2 107 ? -11.64100 37.88500  34.06400  1.000 47.63014  ? 107  ASP   F O   1 
ATOM   8669 C CB  . ASP   D 2 107 ? -9.56000  35.85000  32.76300  1.000 37.75600  ? 107  ASP   F CB  1 
ATOM   8670 C CG  . ASP   D 2 107 ? -9.07600  34.62800  32.00200  1.000 50.66409  ? 107  ASP   F CG  1 
ATOM   8671 O OD1 . ASP   D 2 107 ? -9.53200  33.51400  32.34000  1.000 44.81437  ? 107  ASP   F OD1 1 
ATOM   8672 O OD2 . ASP   D 2 107 ? -8.25700  34.77200  31.06800  1.000 57.57639  ? 107  ASP   F OD2 1 
ATOM   8673 N N   . TYR   D 2 108 ? -12.19700 35.78500  34.68700  1.000 40.79605  ? 108  TYR   F N   1 
ATOM   8674 C CA  . TYR   D 2 108 ? -12.95700 36.16900  35.86700  1.000 38.47688  ? 108  TYR   F CA  1 
ATOM   8675 C C   . TYR   D 2 108 ? -12.67400 35.18500  36.98900  1.000 37.61076  ? 108  TYR   F C   1 
ATOM   8676 O O   . TYR   D 2 108 ? -12.83000 33.97300  36.81000  1.000 32.38454  ? 108  TYR   F O   1 
ATOM   8677 C CB  . TYR   D 2 108 ? -14.45000 36.20000  35.55400  1.000 43.28559  ? 108  TYR   F CB  1 
ATOM   8678 C CG  . TYR   D 2 108 ? -14.90400 37.46200  34.86400  1.000 47.13070  ? 108  TYR   F CG  1 
ATOM   8679 C CD1 . TYR   D 2 108 ? -14.89400 38.67600  35.53500  1.000 56.43350  ? 108  TYR   F CD1 1 
ATOM   8680 C CD2 . TYR   D 2 108 ? -15.36000 37.44100  33.55200  1.000 45.34047  ? 108  TYR   F CD2 1 
ATOM   8681 C CE1 . TYR   D 2 108 ? -15.32200 39.83000  34.92300  1.000 52.38717  ? 108  TYR   F CE1 1 
ATOM   8682 C CE2 . TYR   D 2 108 ? -15.79500 38.59800  32.93300  1.000 45.12312  ? 108  TYR   F CE2 1 
ATOM   8683 C CZ  . TYR   D 2 108 ? -15.76700 39.78900  33.62500  1.000 45.22463  ? 108  TYR   F CZ  1 
ATOM   8684 O OH  . TYR   D 2 108 ? -16.18900 40.95000  33.02900  1.000 53.37960  ? 108  TYR   F OH  1 
ATOM   8685 N N   . TRP   D 2 109 ? -12.28000 35.70800  38.14300  1.000 36.73984  ? 109  TRP   F N   1 
ATOM   8686 C CA  . TRP   D 2 109 ? -11.78900 34.89700  39.24200  1.000 36.58031  ? 109  TRP   F CA  1 
ATOM   8687 C C   . TRP   D 2 109 ? -12.66900 35.07800  40.47100  1.000 41.91540  ? 109  TRP   F C   1 
ATOM   8688 O O   . TRP   D 2 109 ? -13.27300 36.13600  40.67600  1.000 41.21482  ? 109  TRP   F O   1 
ATOM   8689 C CB  . TRP   D 2 109 ? -10.35300 35.27800  39.58400  1.000 39.43217  ? 109  TRP   F CB  1 
ATOM   8690 C CG  . TRP   D 2 109 ? -9.38200  35.01000  38.48400  1.000 40.11998  ? 109  TRP   F CG  1 
ATOM   8691 C CD1 . TRP   D 2 109 ? -8.96000  35.88800  37.52600  1.000 35.14124  ? 109  TRP   F CD1 1 
ATOM   8692 C CD2 . TRP   D 2 109 ? -8.68600  33.78700  38.24100  1.000 37.97965  ? 109  TRP   F CD2 1 
ATOM   8693 N NE1 . TRP   D 2 109 ? -8.05200  35.28000  36.69600  1.000 33.51291  ? 109  TRP   F NE1 1 
ATOM   8694 C CE2 . TRP   D 2 109 ? -7.86600  33.98900  37.11400  1.000 33.46072  ? 109  TRP   F CE2 1 
ATOM   8695 C CE3 . TRP   D 2 109 ? -8.67900  32.53700  38.86600  1.000 39.82398  ? 109  TRP   F CE3 1 
ATOM   8696 C CZ2 . TRP   D 2 109 ? -7.05000  32.99000  36.60000  1.000 38.15284  ? 109  TRP   F CZ2 1 
ATOM   8697 C CZ3 . TRP   D 2 109 ? -7.86900  31.55200  38.35700  1.000 41.19628  ? 109  TRP   F CZ3 1 
ATOM   8698 C CH2 . TRP   D 2 109 ? -7.06600  31.78000  37.23300  1.000 38.48854  ? 109  TRP   F CH2 1 
ATOM   8699 N N   . GLY   D 2 110 ? -12.73400 34.03800  41.29100  1.000 39.10733  ? 110  GLY   F N   1 
ATOM   8700 C CA  . GLY   D 2 110 ? -13.40800 34.16000  42.56100  1.000 46.64508  ? 110  GLY   F CA  1 
ATOM   8701 C C   . GLY   D 2 110 ? -12.50300 34.73300  43.63200  1.000 47.68034  ? 110  GLY   F C   1 
ATOM   8702 O O   . GLY   D 2 110 ? -11.30300 34.94200  43.43500  1.000 44.21594  ? 110  GLY   F O   1 
ATOM   8703 N N   . GLN   D 2 111 ? -13.10300 34.99800  44.79600  1.000 46.64550  ? 111  GLN   F N   1 
ATOM   8704 C CA  . GLN   D 2 111 ? -12.32700 35.50700  45.92200  1.000 48.79595  ? 111  GLN   F CA  1 
ATOM   8705 C C   . GLN   D 2 111 ? -11.31100 34.48200  46.40400  1.000 41.75520  ? 111  GLN   F C   1 
ATOM   8706 O O   . GLN   D 2 111 ? -10.21600 34.85300  46.84100  1.000 40.44119  ? 111  GLN   F O   1 
ATOM   8707 C CB  . GLN   D 2 111 ? -13.25600 35.91100  47.06600  1.000 54.81854  ? 111  GLN   F CB  1 
ATOM   8708 N N   . GLY   D 2 112 ? -11.64300 33.19900  46.31700  1.000 41.37057  ? 112  GLY   F N   1 
ATOM   8709 C CA  . GLY   D 2 112 ? -10.78700 32.14000  46.80600  1.000 42.97248  ? 112  GLY   F CA  1 
ATOM   8710 C C   . GLY   D 2 112 ? -11.28700 31.57200  48.12200  1.000 52.51575  ? 112  GLY   F C   1 
ATOM   8711 O O   . GLY   D 2 112 ? -12.13100 32.14800  48.81400  1.000 61.21592  ? 112  GLY   F O   1 
ATOM   8712 N N   . THR   D 2 113 ? -10.74100 30.40900  48.47100  1.000 48.88633  ? 113  THR   F N   1 
ATOM   8713 C CA  . THR   D 2 113 ? -11.17200 29.69400  49.66400  1.000 45.83461  ? 113  THR   F CA  1 
ATOM   8714 C C   . THR   D 2 113 ? -10.09600 28.69200  50.06500  1.000 44.56213  ? 113  THR   F C   1 
ATOM   8715 O O   . THR   D 2 113 ? -9.48700  28.04600  49.20900  1.000 48.14534  ? 113  THR   F O   1 
ATOM   8716 C CB  . THR   D 2 113 ? -12.53000 29.01200  49.42500  1.000 51.12393  ? 113  THR   F CB  1 
ATOM   8717 O OG1 . THR   D 2 113 ? -13.03400 28.46400  50.65200  1.000 71.97678  ? 113  THR   F OG1 1 
ATOM   8718 C CG2 . THR   D 2 113 ? -12.44000 27.94600  48.34700  1.000 41.47740  ? 113  THR   F CG2 1 
ATOM   8719 N N   . GLN   D 2 114 ? -9.85700  28.58000  51.36800  1.000 48.94650  ? 114  GLN   F N   1 
ATOM   8720 C CA  . GLN   D 2 114 ? -8.69900  27.84700  51.85800  1.000 48.94473  ? 114  GLN   F CA  1 
ATOM   8721 C C   . GLN   D 2 114 ? -9.01800  26.38500  52.14300  1.000 45.41625  ? 114  GLN   F C   1 
ATOM   8722 O O   . GLN   D 2 114 ? -10.13300 26.02400  52.52500  1.000 49.00507  ? 114  GLN   F O   1 
ATOM   8723 C CB  . GLN   D 2 114 ? -8.13200  28.50400  53.11600  1.000 45.70463  ? 114  GLN   F CB  1 
ATOM   8724 C CG  . GLN   D 2 114 ? -6.84200  29.25000  52.83900  1.000 52.99282  ? 114  GLN   F CG  1 
ATOM   8725 C CD  . GLN   D 2 114 ? -6.31900  29.99300  54.03900  1.000 65.05427  ? 114  GLN   F CD  1 
ATOM   8726 O OE1 . GLN   D 2 114 ? -7.02100  30.15700  55.03700  1.000 67.81116  ? 114  GLN   F OE1 1 
ATOM   8727 N NE2 . GLN   D 2 114 ? -5.07600  30.46000  53.94700  1.000 69.98601  ? 114  GLN   F NE2 1 
ATOM   8728 N N   . VAL   D 2 115 ? -8.00400  25.54600  51.94500  1.000 43.42730  ? 115  VAL   F N   1 
ATOM   8729 C CA  . VAL   D 2 115 ? -8.07100  24.10900  52.18300  1.000 49.78239  ? 115  VAL   F CA  1 
ATOM   8730 C C   . VAL   D 2 115 ? -6.76400  23.72100  52.86600  1.000 56.03747  ? 115  VAL   F C   1 
ATOM   8731 O O   . VAL   D 2 115 ? -5.70100  23.75200  52.23500  1.000 49.54509  ? 115  VAL   F O   1 
ATOM   8732 C CB  . VAL   D 2 115 ? -8.26200  23.30400  50.88700  1.000 50.29602  ? 115  VAL   F CB  1 
ATOM   8733 C CG1 . VAL   D 2 115 ? -8.16300  21.81100  51.16000  1.000 43.08940  ? 115  VAL   F CG1 1 
ATOM   8734 C CG2 . VAL   D 2 115 ? -9.59300  23.64100  50.23100  1.000 54.83755  ? 115  VAL   F CG2 1 
ATOM   8735 N N   . THR   D 2 116 ? -6.83300  23.36900  54.14800  1.000 53.65358  ? 116  THR   F N   1 
ATOM   8736 C CA  . THR   D 2 116 ? -5.67000  22.92700  54.90600  1.000 44.62517  ? 116  THR   F CA  1 
ATOM   8737 C C   . THR   D 2 116 ? -5.77400  21.43100  55.16900  1.000 49.35134  ? 116  THR   F C   1 
ATOM   8738 O O   . THR   D 2 116 ? -6.80300  20.95200  55.65700  1.000 55.24094  ? 116  THR   F O   1 
ATOM   8739 C CB  . THR   D 2 116 ? -5.54400  23.68900  56.22900  1.000 49.23619  ? 116  THR   F CB  1 
ATOM   8740 O OG1 . THR   D 2 116 ? -5.50700  25.09800  55.97200  1.000 47.93558  ? 116  THR   F OG1 1 
ATOM   8741 C CG2 . THR   D 2 116 ? -4.27700  23.27600  56.96600  1.000 47.52095  ? 116  THR   F CG2 1 
ATOM   8742 N N   . VAL   D 2 117 ? -4.71200  20.70200  54.84500  1.000 52.63739  ? 117  VAL   F N   1 
ATOM   8743 C CA  . VAL   D 2 117 ? -4.65600  19.26200  55.05300  1.000 62.91146  ? 117  VAL   F CA  1 
ATOM   8744 C C   . VAL   D 2 117 ? -3.60500  18.97400  56.12000  1.000 66.25687  ? 117  VAL   F C   1 
ATOM   8745 O O   . VAL   D 2 117 ? -2.65400  19.74200  56.30600  1.000 62.73858  ? 117  VAL   F O   1 
ATOM   8746 C CB  . VAL   D 2 117 ? -4.35800  18.52400  53.72800  1.000 56.32807  ? 117  VAL   F CB  1 
ATOM   8747 C CG1 . VAL   D 2 117 ? -4.37000  17.01100  53.91800  1.000 60.03155  ? 117  VAL   F CG1 1 
ATOM   8748 C CG2 . VAL   D 2 117 ? -5.35300  18.94100  52.65600  1.000 46.91882  ? 117  VAL   F CG2 1 
ATOM   8749 N N   . SER   D 2 118 ? -3.79000  17.86500  56.83900  1.000 68.69330  ? 118  SER   F N   1 
ATOM   8750 C CA  . SER   D 2 118 ? -2.96200  17.51400  57.98700  1.000 65.48780  ? 118  SER   F CA  1 
ATOM   8751 C C   . SER   D 2 118 ? -2.40300  16.11400  57.78500  1.000 75.07393  ? 118  SER   F C   1 
ATOM   8752 O O   . SER   D 2 118 ? -3.17000  15.16400  57.60500  1.000 83.65236  ? 118  SER   F O   1 
ATOM   8753 C CB  . SER   D 2 118 ? -3.78200  17.57600  59.27500  1.000 63.42231  ? 118  SER   F CB  1 
ATOM   8754 O OG  . SER   D 2 118 ? -4.60100  18.73100  59.28000  1.000 62.91406  ? 118  SER   F OG  1 
ATOM   8755 N N   . SER   D 2 119 ? -1.07900  15.98000  57.84100  1.000 74.54770  ? 119  SER   F N   1 
ATOM   8756 C CA  . SER   D 2 119 ? -0.43400  14.69500  57.55500  1.000 74.29874  ? 119  SER   F CA  1 
ATOM   8757 C C   . SER   D 2 119 ? -0.77900  13.63100  58.59600  1.000 76.26976  ? 119  SER   F C   1 
ATOM   8758 O O   . SER   D 2 119 ? -1.38000  13.92200  59.63100  1.000 79.53059  ? 119  SER   F O   1 
ATOM   8759 C CB  . SER   D 2 119 ? 1.08600   14.85600  57.47800  1.000 78.36967  ? 119  SER   F CB  1 
ATOM   8760 O OG  . SER   D 2 119 ? 1.45400   15.87100  56.55900  1.000 76.27118  ? 119  SER   F OG  1 
HETATM 8761 C C4  . A1AE2 E 3 .   ? -43.03000 25.81100  -6.59700  1.000 42.12060  ? 1201 A1AE2 A C4  1 
HETATM 8762 C C14 . A1AE2 E 3 .   ? -49.57400 22.03900  -12.93400 1.000 56.86386  ? 1201 A1AE2 A C14 1 
HETATM 8763 C C5  . A1AE2 E 3 .   ? -42.81500 25.29200  -7.78500  1.000 44.31014  ? 1201 A1AE2 A C5  1 
HETATM 8764 C C6  . A1AE2 E 3 .   ? -43.86400 24.38300  -8.42800  1.000 56.21722  ? 1201 A1AE2 A C6  1 
HETATM 8765 C C11 . A1AE2 E 3 .   ? -48.24600 22.65800  -8.64500  1.000 47.95370  ? 1201 A1AE2 A C11 1 
HETATM 8766 C C7  . A1AE2 E 3 .   ? -43.58100 23.79400  -9.80900  1.000 45.84091  ? 1201 A1AE2 A C7  1 
HETATM 8767 C C8  . A1AE2 E 3 .   ? -42.16100 23.23500  -9.83600  1.000 40.88238  ? 1201 A1AE2 A C8  1 
HETATM 8768 C C9  . A1AE2 E 3 .   ? -41.56400 23.21500  -11.24100 1.000 52.05991  ? 1201 A1AE2 A C9  1 
HETATM 8769 C C10 . A1AE2 E 3 .   ? -47.26700 23.79700  -8.36300  1.000 39.59913  ? 1201 A1AE2 A C10 1 
HETATM 8770 C C12 . A1AE2 E 3 .   ? -48.09200 22.23900  -10.09900 1.000 49.21456  ? 1201 A1AE2 A C12 1 
HETATM 8771 C C13 . A1AE2 E 3 .   ? -48.50000 22.92000  -12.31900 1.000 62.84762  ? 1201 A1AE2 A C13 1 
HETATM 8772 N N1  . A1AE2 E 3 .   ? -48.85700 23.14400  -10.93000 1.000 52.95021  ? 1201 A1AE2 A N1  1 
HETATM 8773 N N2  . A1AE2 E 3 .   ? -50.73700 23.75700  -15.51400 1.000 62.89988  ? 1201 A1AE2 A N2  1 
HETATM 8774 C C3  . A1AE2 E 3 .   ? -44.33100 25.50300  -5.86200  1.000 44.47651  ? 1201 A1AE2 A C3  1 
HETATM 8775 N N3  . A1AE2 E 3 .   ? -51.24600 23.33300  -16.74100 1.000 65.11065  ? 1201 A1AE2 A N3  1 
HETATM 8776 C C1  . A1AE2 E 3 .   ? -44.99400 24.11500  -7.79300  1.000 47.89595  ? 1201 A1AE2 A C1  1 
HETATM 8777 C C15 . A1AE2 E 3 .   ? -50.82100 22.89700  -13.09200 1.000 62.07998  ? 1201 A1AE2 A C15 1 
HETATM 8778 C C16 . A1AE2 E 3 .   ? -51.15200 22.84500  -14.57000 1.000 62.43370  ? 1201 A1AE2 A C16 1 
HETATM 8779 C C17 . A1AE2 E 3 .   ? -51.90800 21.86600  -15.19300 1.000 60.29501  ? 1201 A1AE2 A C17 1 
HETATM 8780 C C18 . A1AE2 E 3 .   ? -52.63900 21.44000  -17.61300 1.000 76.97856  ? 1201 A1AE2 A C18 1 
HETATM 8781 C C19 . A1AE2 E 3 .   ? -52.45900 19.91700  -17.55600 1.000 83.25947  ? 1201 A1AE2 A C19 1 
HETATM 8782 C C2  . A1AE2 E 3 .   ? -45.23600 24.72100  -6.41400  1.000 47.37929  ? 1201 A1AE2 A C2  1 
HETATM 8783 C C20 . A1AE2 E 3 .   ? -51.07100 19.50800  -17.06200 1.000 87.07411  ? 1201 A1AE2 A C20 1 
HETATM 8784 C C21 . A1AE2 E 3 .   ? -50.56700 18.24200  -17.74400 1.000 77.66411  ? 1201 A1AE2 A C21 1 
HETATM 8785 C C22 . A1AE2 E 3 .   ? -49.12200 18.51800  -18.14600 1.000 85.52411  ? 1201 A1AE2 A C22 1 
HETATM 8786 C C23 . A1AE2 E 3 .   ? -48.13700 17.56200  -17.96300 1.000 80.87411  ? 1201 A1AE2 A C23 1 
HETATM 8787 C C24 . A1AE2 E 3 .   ? -46.82700 17.83900  -18.33800 1.000 84.23140  ? 1201 A1AE2 A C24 1 
HETATM 8788 C C25 . A1AE2 E 3 .   ? -46.51400 19.08100  -18.89000 1.000 89.41544  ? 1201 A1AE2 A C25 1 
HETATM 8789 C C26 . A1AE2 E 3 .   ? -47.50700 20.03300  -19.06100 1.000 83.84073  ? 1201 A1AE2 A C26 1 
HETATM 8790 C C27 . A1AE2 E 3 .   ? -48.80100 19.74500  -18.68600 1.000 82.17411  ? 1201 A1AE2 A C27 1 
HETATM 8791 C C28 . A1AE2 E 3 .   ? -44.50500 20.12800  -18.32300 1.000 77.61820  ? 1201 A1AE2 A C28 1 
HETATM 8792 C C29 . A1AE2 E 3 .   ? -43.09400 19.57100  -18.17700 1.000 86.19831  ? 1201 A1AE2 A C29 1 
HETATM 8793 C C30 . A1AE2 E 3 .   ? -43.00300 18.77700  -16.87600 1.000 81.78200  ? 1201 A1AE2 A C30 1 
HETATM 8794 C C31 . A1AE2 E 3 .   ? -42.52900 19.75000  -14.77000 1.000 83.22415  ? 1201 A1AE2 A C31 1 
HETATM 8795 C C32 . A1AE2 E 3 .   ? -41.61400 20.76200  -14.08300 1.000 69.79591  ? 1201 A1AE2 A C32 1 
HETATM 8796 C C33 . A1AE2 E 3 .   ? -42.64200 18.50200  -13.90100 1.000 77.76155  ? 1201 A1AE2 A C33 1 
HETATM 8797 N N4  . A1AE2 E 3 .   ? -51.95400 22.17300  -16.55300 1.000 70.76813  ? 1201 A1AE2 A N4  1 
HETATM 8798 N N5  . A1AE2 E 3 .   ? -41.96500 19.36400  -16.04900 1.000 88.52100  ? 1201 A1AE2 A N5  1 
HETATM 8799 O O1  . A1AE2 E 3 .   ? -45.96600 23.28100  -8.36700  1.000 39.63668  ? 1201 A1AE2 A O1  1 
HETATM 8800 O O2  . A1AE2 E 3 .   ? -49.57000 23.06700  -8.44000  1.000 39.78443  ? 1201 A1AE2 A O2  1 
HETATM 8801 O O3  . A1AE2 E 3 .   ? -45.20000 19.37500  -19.27100 1.000 84.46861  ? 1201 A1AE2 A O3  1 
HETATM 8802 O O4  . A1AE2 E 3 .   ? -42.18200 20.63400  -18.14900 1.000 80.39477  ? 1201 A1AE2 A O4  1 
HETATM 8803 C C4  . A1AE2 F 3 .   ? -23.00100 39.53800  -6.99900  1.000 45.71437  ? 1201 A1AE2 B C4  1 
HETATM 8804 C C14 . A1AE2 F 3 .   ? -16.45400 40.75000  -13.53500 1.000 58.43244  ? 1201 A1AE2 B C14 1 
HETATM 8805 C C5  . A1AE2 F 3 .   ? -23.10000 40.05300  -8.20300  1.000 48.90101  ? 1201 A1AE2 B C5  1 
HETATM 8806 C C6  . A1AE2 F 3 .   ? -21.88100 40.70100  -8.85400  1.000 52.17644  ? 1201 A1AE2 B C6  1 
HETATM 8807 C C11 . A1AE2 F 3 .   ? -17.34700 41.80800  -9.12900  1.000 61.51290  ? 1201 A1AE2 B C11 1 
HETATM 8808 C C7  . A1AE2 F 3 .   ? -21.99100 41.30000  -10.25000 1.000 42.44128  ? 1201 A1AE2 B C7  1 
HETATM 8809 C C8  . A1AE2 F 3 .   ? -23.46300 41.53400  -10.55700 1.000 47.22415  ? 1201 A1AE2 B C8  1 
HETATM 8810 C C9  . A1AE2 F 3 .   ? -23.65200 42.32800  -11.84000 1.000 52.93981  ? 1201 A1AE2 B C9  1 
HETATM 8811 C C10 . A1AE2 F 3 .   ? -18.37800 41.00700  -8.33900  1.000 53.52338  ? 1201 A1AE2 B C10 1 
HETATM 8812 C C12 . A1AE2 F 3 .   ? -17.33400 41.24700  -10.55000 1.000 56.06775  ? 1201 A1AE2 B C12 1 
HETATM 8813 C C13 . A1AE2 F 3 .   ? -16.56100 41.98900  -12.65100 1.000 61.08172  ? 1201 A1AE2 B C13 1 
HETATM 8814 N N1  . A1AE2 F 3 .   ? -16.16500 41.68400  -11.28500 1.000 51.98630  ? 1201 A1AE2 B N1  1 
HETATM 8815 N N2  . A1AE2 F 3 .   ? -14.37800 40.66500  -16.34300 1.000 75.95093  ? 1201 A1AE2 B N2  1 
HETATM 8816 C C3  . A1AE2 F 3 .   ? -21.66700 39.59600  -6.26000  1.000 55.54281  ? 1201 A1AE2 B C3  1 
HETATM 8817 N N3  . A1AE2 F 3 .   ? -13.93200 41.66700  -17.21100 1.000 80.61251  ? 1201 A1AE2 B N3  1 
HETATM 8818 C C1  . A1AE2 F 3 .   ? -20.73100 40.74900  -8.21800  1.000 54.85154  ? 1201 A1AE2 B C1  1 
HETATM 8819 C C15 . A1AE2 F 3 .   ? -14.98600 40.46100  -13.83600 1.000 57.03100  ? 1201 A1AE2 B C15 1 
HETATM 8820 C C16 . A1AE2 F 3 .   ? -14.52400 41.21600  -15.08300 1.000 67.12123  ? 1201 A1AE2 B C16 1 
HETATM 8821 C C17 . A1AE2 F 3 .   ? -14.16800 42.55800  -15.16200 1.000 66.10891  ? 1201 A1AE2 B C17 1 
HETATM 8822 C C18 . A1AE2 F 3 .   ? -13.36400 44.10000  -17.01100 1.000 72.51422  ? 1201 A1AE2 B C18 1 
HETATM 8823 C C19 . A1AE2 F 3 .   ? -13.94500 44.31300  -18.40800 1.000 72.62442  ? 1201 A1AE2 B C19 1 
HETATM 8824 C C2  . A1AE2 F 3 .   ? -20.61500 40.15500  -6.81900  1.000 59.18158  ? 1201 A1AE2 B C2  1 
HETATM 8825 C C20 . A1AE2 F 3 .   ? -15.25900 45.08000  -18.28100 1.000 78.89134  ? 1201 A1AE2 B C20 1 
HETATM 8826 C C21 . A1AE2 F 3 .   ? -15.76600 45.52200  -19.65100 1.000 77.88473  ? 1201 A1AE2 B C21 1 
HETATM 8827 C C22 . A1AE2 F 3 .   ? -17.25000 45.17500  -19.76100 1.000 86.27237  ? 1201 A1AE2 B C22 1 
HETATM 8828 C C23 . A1AE2 F 3 .   ? -18.19600 46.17500  -19.92400 1.000 84.68678  ? 1201 A1AE2 B C23 1 
HETATM 8829 C C24 . A1AE2 F 3 .   ? -19.54700 45.85100  -20.02500 1.000 89.09887  ? 1201 A1AE2 B C24 1 
HETATM 8830 C C25 . A1AE2 F 3 .   ? -19.94700 44.51900  -19.95600 1.000 82.29291  ? 1201 A1AE2 B C25 1 
HETATM 8831 C C26 . A1AE2 F 3 .   ? -18.99600 43.52500  -19.78600 1.000 80.51259  ? 1201 A1AE2 B C26 1 
HETATM 8832 C C27 . A1AE2 F 3 .   ? -17.66000 43.85900  -19.68900 1.000 88.12536  ? 1201 A1AE2 B C27 1 
HETATM 8833 C C28 . A1AE2 F 3 .   ? -22.10200 44.88000  -19.13900 1.000 73.36223  ? 1201 A1AE2 B C28 1 
HETATM 8834 C C29 . A1AE2 F 3 .   ? -23.22400 43.95700  -18.68600 1.000 74.32329  ? 1201 A1AE2 B C29 1 
HETATM 8835 C C30 . A1AE2 F 3 .   ? -22.95500 43.54500  -17.24000 1.000 77.12724  ? 1201 A1AE2 B C30 1 
HETATM 8836 C C31 . A1AE2 F 3 .   ? -23.31400 44.70800  -15.19800 1.000 78.91117  ? 1201 A1AE2 B C31 1 
HETATM 8837 C C32 . A1AE2 F 3 .   ? -24.36100 44.63500  -14.09600 1.000 69.30128  ? 1201 A1AE2 B C32 1 
HETATM 8838 C C33 . A1AE2 F 3 .   ? -22.94200 46.17100  -15.42900 1.000 85.64403  ? 1201 A1AE2 B C33 1 
HETATM 8839 N N4  . A1AE2 F 3 .   ? -13.80400 42.82200  -16.48300 1.000 77.10024  ? 1201 A1AE2 B N4  1 
HETATM 8840 N N5  . A1AE2 F 3 .   ? -23.94000 44.19600  -16.39900 1.000 79.50982  ? 1201 A1AE2 B N5  1 
HETATM 8841 O O1  . A1AE2 F 3 .   ? -19.63500 41.35500  -8.83900  1.000 53.06557  ? 1201 A1AE2 B O1  1 
HETATM 8842 O O2  . A1AE2 F 3 .   ? -16.08700 41.70800  -8.52600  1.000 53.76626  ? 1201 A1AE2 B O2  1 
HETATM 8843 O O3  . A1AE2 F 3 .   ? -21.30300 44.18800  -20.05200 1.000 71.70400  ? 1201 A1AE2 B O3  1 
HETATM 8844 O O4  . A1AE2 F 3 .   ? -23.25900 42.82900  -19.51800 1.000 60.65504  ? 1201 A1AE2 B O4  1 
HETATM 8845 C C1  . AV0   G 4 .   ? -35.38500 33.20600  -20.09600 1.000 45.66741  ? 1202 AV0   B C1  1 
HETATM 8846 O O1  . AV0   G 4 .   ? -34.19200 33.11600  -19.31100 1.000 44.12109  ? 1202 AV0   B O1  1 
HETATM 8847 C C2  . AV0   G 4 .   ? -35.43500 34.56800  -20.73500 1.000 46.05774  ? 1202 AV0   B C2  1 
HETATM 8848 O O2  . AV0   G 4 .   ? -35.40900 35.56700  -19.74700 1.000 37.30983  ? 1202 AV0   B O2  1 
HETATM 8849 C C3  . AV0   G 4 .   ? -36.73800 34.64300  -21.54800 1.000 50.89966  ? 1202 AV0   B C3  1 
HETATM 8850 O O3  . AV0   G 4 .   ? -36.81200 35.87200  -22.18200 1.000 57.57170  ? 1202 AV0   B O3  1 
HETATM 8851 C C4  . AV0   G 4 .   ? -36.75100 33.52200  -22.60000 1.000 49.40893  ? 1202 AV0   B C4  1 
HETATM 8852 O O4  . AV0   G 4 .   ? -38.04000 33.47300  -23.17900 1.000 58.52189  ? 1202 AV0   B O4  1 
HETATM 8853 C C5  . AV0   G 4 .   ? -36.39800 32.16300  -21.98000 1.000 46.91634  ? 1202 AV0   B C5  1 
HETATM 8854 O O5  . AV0   G 4 .   ? -35.32000 32.24600  -21.08600 1.000 48.74893  ? 1202 AV0   B O5  1 
HETATM 8855 C C6  . AV0   G 4 .   ? -35.93200 31.20100  -23.07500 1.000 49.11495  ? 1202 AV0   B C6  1 
HETATM 8856 O O6  . AV0   G 4 .   ? -37.01800 30.78900  -23.86500 1.000 62.42187  ? 1202 AV0   B O6  1 
HETATM 8857 C CAA . AV0   G 4 .   ? -38.18800 29.72000  -8.09200  1.000 53.76263  ? 1202 AV0   B CAA 1 
HETATM 8858 C CAB . AV0   G 4 .   ? -27.86600 34.75300  -8.36500  1.000 52.84779  ? 1202 AV0   B CAB 1 
HETATM 8859 O OAI . AV0   G 4 .   ? -39.39500 30.33300  -25.93600 1.000 51.07733  ? 1202 AV0   B OAI 1 
HETATM 8860 O OAJ . AV0   G 4 .   ? -27.07300 27.17000  -23.69200 1.000 83.01655  ? 1202 AV0   B OAJ 1 
HETATM 8861 O OAL . AV0   G 4 .   ? -28.79200 33.20100  -23.56800 1.000 53.80339  ? 1202 AV0   B OAL 1 
HETATM 8862 O OAN . AV0   G 4 .   ? -28.76200 27.99200  -21.85100 1.000 65.19100  ? 1202 AV0   B OAN 1 
HETATM 8863 O OAP . AV0   G 4 .   ? -30.47000 28.30300  -19.58300 1.000 59.07202  ? 1202 AV0   B OAP 1 
HETATM 8864 O OAQ . AV0   G 4 .   ? -42.09900 33.51600  -25.07000 1.000 61.90213  ? 1202 AV0   B OAQ 1 
HETATM 8865 O OAR . AV0   G 4 .   ? -25.73300 30.04100  -27.22500 1.000 88.18354  ? 1202 AV0   B OAR 1 
HETATM 8866 O OAS . AV0   G 4 .   ? -40.89700 36.05100  -25.00200 1.000 64.20545  ? 1202 AV0   B OAS 1 
HETATM 8867 O OAT . AV0   G 4 .   ? -23.92100 30.31800  -24.27500 1.000 69.19449  ? 1202 AV0   B OAT 1 
HETATM 8868 O OAU . AV0   G 4 .   ? -38.19800 36.11000  -24.14200 1.000 70.98339  ? 1202 AV0   B OAU 1 
HETATM 8869 O OAV . AV0   G 4 .   ? -26.94900 32.09800  -25.00700 1.000 77.34836  ? 1202 AV0   B OAV 1 
HETATM 8870 C CAW . AV0   G 4 .   ? -36.69900 29.91100  -8.44400  1.000 53.41596  ? 1202 AV0   B CAW 1 
HETATM 8871 C CAX . AV0   G 4 .   ? -29.31400 34.24300  -8.36100  1.000 55.08990  ? 1202 AV0   B CAX 1 
HETATM 8872 C CAY . AV0   G 4 .   ? -36.53800 30.14100  -9.97800  1.000 48.09959  ? 1202 AV0   B CAY 1 
HETATM 8873 C CAZ . AV0   G 4 .   ? -29.65200 33.59800  -9.72500  1.000 56.43772  ? 1202 AV0   B CAZ 1 
HETATM 8874 C CBA . AV0   G 4 .   ? -35.06800 30.56900  -10.27500 1.000 49.46146  ? 1202 AV0   B CBA 1 
HETATM 8875 C CBB . AV0   G 4 .   ? -30.05700 34.71700  -10.75200 1.000 53.29856  ? 1202 AV0   B CBB 1 
HETATM 8876 C CBC . AV0   G 4 .   ? -34.86900 30.82500  -11.80900 1.000 51.29288  ? 1202 AV0   B CBC 1 
HETATM 8877 C CBD . AV0   G 4 .   ? -30.54100 34.04500  -12.08300 1.000 57.95710  ? 1202 AV0   B CBD 1 
HETATM 8878 C CBE . AV0   G 4 .   ? -34.68300 29.45200  -12.53800 1.000 51.69273  ? 1202 AV0   B CBE 1 
HETATM 8879 C CBF . AV0   G 4 .   ? -31.81800 34.82000  -12.62700 1.000 57.15554  ? 1202 AV0   B CBF 1 
HETATM 8880 C CBG . AV0   G 4 .   ? -33.33500 29.46300  -13.34100 1.000 43.31671  ? 1202 AV0   B CBG 1 
HETATM 8881 C CBH . AV0   G 4 .   ? -31.39000 35.67400  -13.91100 1.000 54.42573  ? 1202 AV0   B CBH 1 
HETATM 8882 C CBI . AV0   G 4 .   ? -33.67500 29.40800  -14.88600 1.000 47.42035  ? 1202 AV0   B CBI 1 
HETATM 8883 C CBJ . AV0   G 4 .   ? -32.38300 35.35300  -15.09900 1.000 44.90627  ? 1202 AV0   B CBJ 1 
HETATM 8884 C CBK . AV0   G 4 .   ? -33.77800 30.89300  -15.46000 1.000 50.19306  ? 1202 AV0   B CBK 1 
HETATM 8885 C CBL . AV0   G 4 .   ? -32.04100 33.90500  -15.68400 1.000 45.90023  ? 1202 AV0   B CBL 1 
HETATM 8886 C CBM . AV0   G 4 .   ? -40.41900 31.27900  -25.83200 1.000 58.43825  ? 1202 AV0   B CBM 1 
HETATM 8887 C CBN . AV0   G 4 .   ? -26.43200 27.50500  -24.90200 1.000 81.53368  ? 1202 AV0   B CBN 1 
HETATM 8888 C CBP . AV0   G 4 .   ? -29.85800 32.36100  -23.21200 1.000 63.37574  ? 1202 AV0   B CBP 1 
HETATM 8889 C CBQ . AV0   G 4 .   ? -32.55100 31.11700  -16.45200 1.000 46.24160  ? 1202 AV0   B CBQ 1 
HETATM 8890 C CBR . AV0   G 4 .   ? -32.91500 33.72300  -16.98000 1.000 44.89323  ? 1202 AV0   B CBR 1 
HETATM 8891 C CBS . AV0   G 4 .   ? -34.14000 31.98900  -18.39500 1.000 49.25163  ? 1202 AV0   B CBS 1 
HETATM 8892 C CBT . AV0   G 4 .   ? -31.63900 32.16900  -18.61500 1.000 47.76883  ? 1202 AV0   B CBT 1 
HETATM 8893 O OBV . AV0   G 4 .   ? -31.56300 30.80000  -19.10900 1.000 54.68835  ? 1202 AV0   B OBV 1 
HETATM 8894 O OBX . AV0   G 4 .   ? -30.70200 31.53900  -21.11900 1.000 54.10526  ? 1202 AV0   B OBX 1 
HETATM 8895 O OBY . AV0   G 4 .   ? -38.54100 32.67700  -25.31000 1.000 56.34075  ? 1202 AV0   B OBY 1 
HETATM 8896 O OBZ . AV0   G 4 .   ? -27.58700 29.61600  -24.41300 1.000 75.94129  ? 1202 AV0   B OBZ 1 
HETATM 8897 O OCB . AV0   G 4 .   ? -27.41000 30.69300  -22.32500 1.000 70.17845  ? 1202 AV0   B OCB 1 
HETATM 8898 C CCC . AV0   G 4 .   ? -39.93900 32.45400  -25.02900 1.000 54.22790  ? 1202 AV0   B CCC 1 
HETATM 8899 C CCD . AV0   G 4 .   ? -26.80300 28.92200  -25.38500 1.000 78.85930  ? 1202 AV0   B CCD 1 
HETATM 8900 C CCF . AV0   G 4 .   ? -29.50500 31.64900  -21.92400 1.000 59.14532  ? 1202 AV0   B CCF 1 
HETATM 8901 C CCH . AV0   G 4 .   ? -28.97900 29.25100  -21.25100 1.000 62.52010  ? 1202 AV0   B CCH 1 
HETATM 8902 C CCJ . AV0   G 4 .   ? -30.49100 30.66200  -20.00200 1.000 52.08789  ? 1202 AV0   B CCJ 1 
HETATM 8903 C CCL . AV0   G 4 .   ? -30.37600 29.27400  -20.58400 1.000 58.05617  ? 1202 AV0   B CCL 1 
HETATM 8904 C CCM . AV0   G 4 .   ? -32.82100 32.23600  -17.56700 1.000 45.04396  ? 1202 AV0   B CCM 1 
HETATM 8905 C CCN . AV0   G 4 .   ? -40.73100 33.70500  -25.39200 1.000 60.88249  ? 1202 AV0   B CCN 1 
HETATM 8906 C CCO . AV0   G 4 .   ? -25.52700 29.60700  -25.88000 1.000 76.38936  ? 1202 AV0   B CCO 1 
HETATM 8907 C CCQ . AV0   G 4 .   ? -28.82000 30.34200  -22.26800 1.000 61.64254  ? 1202 AV0   B CCQ 1 
HETATM 8908 C CCR . AV0   G 4 .   ? -37.97100 33.76100  -24.56400 1.000 63.25264  ? 1202 AV0   B CCR 1 
HETATM 8909 C CCS . AV0   G 4 .   ? -26.73700 30.24800  -23.47800 1.000 72.98531  ? 1202 AV0   B CCS 1 
HETATM 8910 C CCT . AV0   G 4 .   ? -40.19900 34.87300  -24.62000 1.000 60.29214  ? 1202 AV0   B CCT 1 
HETATM 8911 C CCU . AV0   G 4 .   ? -24.98400 30.77600  -25.08900 1.000 68.72376  ? 1202 AV0   B CCU 1 
HETATM 8912 C CCV . AV0   G 4 .   ? -38.71300 35.04800  -24.90300 1.000 59.53179  ? 1202 AV0   B CCV 1 
HETATM 8913 C CCW . AV0   G 4 .   ? -26.04900 31.42000  -24.20900 1.000 74.48248  ? 1202 AV0   B CCW 1 
# 
