data_8YU4
# 
_entry.id   8YU4 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   8YU4         pdb_00008yu4 10.2210/pdb8yu4/pdb 
WWPDB D_1300046385 ?            ?                   
# 
_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       2025-03-26 
_pdbx_audit_revision_history.part_number         ? 
# 
_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                        8YU4 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-26 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_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           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              huileiyu@ecust.edu.cn 
_pdbx_contact_author.name_first         Yu 
_pdbx_contact_author.name_last          Huilei 
_pdbx_contact_author.name_mi            H 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-1925-3679 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Qiang, G.'   1 0000-0003-2842-8263 
'Zheng, Y.C.' 2 ?                   
'Feng, L.'    3 ?                   
'Yu, H.L.'    4 0000-0002-1925-3679 
# 
_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                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Loop Engineering Facilitates the Nicotinamide Cofactors Utilization of BVMOs' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Qiang, G.'   1 0000-0003-2842-8263 
primary 'Zheng, Y.C.' 2 ?                   
primary 'Feng, L.'    3 ?                   
primary 'Yu, H.L.'    4 0000-0002-1925-3679 
# 
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 'Putative flavin-binding monooxygenase'        62095.094 1   ? 
L143P,A145S,A146S,L149W,K151I,F246Y,K326C,N386S,I388K,M390I,L426F,F432L,T433A,L435S,S438I,E488K,S489C,W490R,F505L ? 
'N-end fusion of HIS tags' 
2 non-polymer syn '1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE' 665.441   1   ? ? ? ?                          
3 non-polymer syn 'FLAVIN-ADENINE DINUCLEOTIDE'                  785.550   1   ? ? ? ?                          
4 water       nat water                                          18.015    216 ? ? ? ?                          
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MHHHHHHTQKMDFDAIIIGAGFGGLYSLKKLRDDFNLKVRAFDRATEVGGTWFWNQYPGALSDSETHLYCYSWDKELLQE
MEIKRKYISQPDVLAYLKRVADKHDLRKDIQFETGIRSAYFDEENSFWNVTTENDEKFTARFLITALGPLSSPNWPIIKG
IETFKGELHHTSRWPKDVTFSGKRVGVIGTGSTGVQVITAIASQVKHLTVFQRSAQYSVPIGNVVMSETDVAKIKENYDQ
IWENVWNSALGYGLNESTLPTMSVSAEERDKIFEKAWQEGGGFRFMFETFGDIAVDETANIEAQNFIKKKISEIVKDPFV
AKKLTPTDLYACRPLCDSGYYEIFNRDNVSLEDVKANPIVEIKEDCVVTADGVEHKLDMLICATGFDAVDGSYKRIDIRG
KDGISIKDHWKDGPNSYLGMMVSNFPNMFMVFGPNGPLANSPPIIETQVRWIADLIGYAEDHQINQIEATKDAVDNWTNT
CSDIANKTLFAKAKCRIFGANVPGKKNTVYLYMGGLKEYRNQISEVSNNNYKGCLLKQSVKKTNLIES
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MHHHHHHTQKMDFDAIIIGAGFGGLYSLKKLRDDFNLKVRAFDRATEVGGTWFWNQYPGALSDSETHLYCYSWDKELLQE
MEIKRKYISQPDVLAYLKRVADKHDLRKDIQFETGIRSAYFDEENSFWNVTTENDEKFTARFLITALGPLSSPNWPIIKG
IETFKGELHHTSRWPKDVTFSGKRVGVIGTGSTGVQVITAIASQVKHLTVFQRSAQYSVPIGNVVMSETDVAKIKENYDQ
IWENVWNSALGYGLNESTLPTMSVSAEERDKIFEKAWQEGGGFRFMFETFGDIAVDETANIEAQNFIKKKISEIVKDPFV
AKKLTPTDLYACRPLCDSGYYEIFNRDNVSLEDVKANPIVEIKEDCVVTADGVEHKLDMLICATGFDAVDGSYKRIDIRG
KDGISIKDHWKDGPNSYLGMMVSNFPNMFMVFGPNGPLANSPPIIETQVRWIADLIGYAEDHQINQIEATKDAVDNWTNT
CSDIANKTLFAKAKCRIFGANVPGKKNTVYLYMGGLKEYRNQISEVSNNNYKGCLLKQSVKKTNLIES
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE' NAI 
3 'FLAVIN-ADENINE DINUCLEOTIDE'                  FAD 
4 water                                          HOH 
# 
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   HIS n 
1 3   HIS n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   THR n 
1 9   GLN n 
1 10  LYS n 
1 11  MET n 
1 12  ASP n 
1 13  PHE n 
1 14  ASP n 
1 15  ALA n 
1 16  ILE n 
1 17  ILE n 
1 18  ILE n 
1 19  GLY n 
1 20  ALA n 
1 21  GLY n 
1 22  PHE n 
1 23  GLY n 
1 24  GLY n 
1 25  LEU n 
1 26  TYR n 
1 27  SER n 
1 28  LEU n 
1 29  LYS n 
1 30  LYS n 
1 31  LEU n 
1 32  ARG n 
1 33  ASP n 
1 34  ASP n 
1 35  PHE n 
1 36  ASN n 
1 37  LEU n 
1 38  LYS n 
1 39  VAL n 
1 40  ARG n 
1 41  ALA n 
1 42  PHE n 
1 43  ASP n 
1 44  ARG n 
1 45  ALA n 
1 46  THR n 
1 47  GLU n 
1 48  VAL n 
1 49  GLY n 
1 50  GLY n 
1 51  THR n 
1 52  TRP n 
1 53  PHE n 
1 54  TRP n 
1 55  ASN n 
1 56  GLN n 
1 57  TYR n 
1 58  PRO n 
1 59  GLY n 
1 60  ALA n 
1 61  LEU n 
1 62  SER n 
1 63  ASP n 
1 64  SER n 
1 65  GLU n 
1 66  THR n 
1 67  HIS n 
1 68  LEU n 
1 69  TYR n 
1 70  CYS n 
1 71  TYR n 
1 72  SER n 
1 73  TRP n 
1 74  ASP n 
1 75  LYS n 
1 76  GLU n 
1 77  LEU n 
1 78  LEU n 
1 79  GLN n 
1 80  GLU n 
1 81  MET n 
1 82  GLU n 
1 83  ILE n 
1 84  LYS n 
1 85  ARG n 
1 86  LYS n 
1 87  TYR n 
1 88  ILE n 
1 89  SER n 
1 90  GLN n 
1 91  PRO n 
1 92  ASP n 
1 93  VAL n 
1 94  LEU n 
1 95  ALA n 
1 96  TYR n 
1 97  LEU n 
1 98  LYS n 
1 99  ARG n 
1 100 VAL n 
1 101 ALA n 
1 102 ASP n 
1 103 LYS n 
1 104 HIS n 
1 105 ASP n 
1 106 LEU n 
1 107 ARG n 
1 108 LYS n 
1 109 ASP n 
1 110 ILE n 
1 111 GLN n 
1 112 PHE n 
1 113 GLU n 
1 114 THR n 
1 115 GLY n 
1 116 ILE n 
1 117 ARG n 
1 118 SER n 
1 119 ALA n 
1 120 TYR n 
1 121 PHE n 
1 122 ASP n 
1 123 GLU n 
1 124 GLU n 
1 125 ASN n 
1 126 SER n 
1 127 PHE n 
1 128 TRP n 
1 129 ASN n 
1 130 VAL n 
1 131 THR n 
1 132 THR n 
1 133 GLU n 
1 134 ASN n 
1 135 ASP n 
1 136 GLU n 
1 137 LYS n 
1 138 PHE n 
1 139 THR n 
1 140 ALA n 
1 141 ARG n 
1 142 PHE n 
1 143 LEU n 
1 144 ILE n 
1 145 THR n 
1 146 ALA n 
1 147 LEU n 
1 148 GLY n 
1 149 PRO n 
1 150 LEU n 
1 151 SER n 
1 152 SER n 
1 153 PRO n 
1 154 ASN n 
1 155 TRP n 
1 156 PRO n 
1 157 ILE n 
1 158 ILE n 
1 159 LYS n 
1 160 GLY n 
1 161 ILE n 
1 162 GLU n 
1 163 THR n 
1 164 PHE n 
1 165 LYS n 
1 166 GLY n 
1 167 GLU n 
1 168 LEU n 
1 169 HIS n 
1 170 HIS n 
1 171 THR n 
1 172 SER n 
1 173 ARG n 
1 174 TRP n 
1 175 PRO n 
1 176 LYS n 
1 177 ASP n 
1 178 VAL n 
1 179 THR n 
1 180 PHE n 
1 181 SER n 
1 182 GLY n 
1 183 LYS n 
1 184 ARG n 
1 185 VAL n 
1 186 GLY n 
1 187 VAL n 
1 188 ILE n 
1 189 GLY n 
1 190 THR n 
1 191 GLY n 
1 192 SER n 
1 193 THR n 
1 194 GLY n 
1 195 VAL n 
1 196 GLN n 
1 197 VAL n 
1 198 ILE n 
1 199 THR n 
1 200 ALA n 
1 201 ILE n 
1 202 ALA n 
1 203 SER n 
1 204 GLN n 
1 205 VAL n 
1 206 LYS n 
1 207 HIS n 
1 208 LEU n 
1 209 THR n 
1 210 VAL n 
1 211 PHE n 
1 212 GLN n 
1 213 ARG n 
1 214 SER n 
1 215 ALA n 
1 216 GLN n 
1 217 TYR n 
1 218 SER n 
1 219 VAL n 
1 220 PRO n 
1 221 ILE n 
1 222 GLY n 
1 223 ASN n 
1 224 VAL n 
1 225 VAL n 
1 226 MET n 
1 227 SER n 
1 228 GLU n 
1 229 THR n 
1 230 ASP n 
1 231 VAL n 
1 232 ALA n 
1 233 LYS n 
1 234 ILE n 
1 235 LYS n 
1 236 GLU n 
1 237 ASN n 
1 238 TYR n 
1 239 ASP n 
1 240 GLN n 
1 241 ILE n 
1 242 TRP n 
1 243 GLU n 
1 244 ASN n 
1 245 VAL n 
1 246 TRP n 
1 247 ASN n 
1 248 SER n 
1 249 ALA n 
1 250 LEU n 
1 251 GLY n 
1 252 TYR n 
1 253 GLY n 
1 254 LEU n 
1 255 ASN n 
1 256 GLU n 
1 257 SER n 
1 258 THR n 
1 259 LEU n 
1 260 PRO n 
1 261 THR n 
1 262 MET n 
1 263 SER n 
1 264 VAL n 
1 265 SER n 
1 266 ALA n 
1 267 GLU n 
1 268 GLU n 
1 269 ARG n 
1 270 ASP n 
1 271 LYS n 
1 272 ILE n 
1 273 PHE n 
1 274 GLU n 
1 275 LYS n 
1 276 ALA n 
1 277 TRP n 
1 278 GLN n 
1 279 GLU n 
1 280 GLY n 
1 281 GLY n 
1 282 GLY n 
1 283 PHE n 
1 284 ARG n 
1 285 PHE n 
1 286 MET n 
1 287 PHE n 
1 288 GLU n 
1 289 THR n 
1 290 PHE n 
1 291 GLY n 
1 292 ASP n 
1 293 ILE n 
1 294 ALA n 
1 295 VAL n 
1 296 ASP n 
1 297 GLU n 
1 298 THR n 
1 299 ALA n 
1 300 ASN n 
1 301 ILE n 
1 302 GLU n 
1 303 ALA n 
1 304 GLN n 
1 305 ASN n 
1 306 PHE n 
1 307 ILE n 
1 308 LYS n 
1 309 LYS n 
1 310 LYS n 
1 311 ILE n 
1 312 SER n 
1 313 GLU n 
1 314 ILE n 
1 315 VAL n 
1 316 LYS n 
1 317 ASP n 
1 318 PRO n 
1 319 PHE n 
1 320 VAL n 
1 321 ALA n 
1 322 LYS n 
1 323 LYS n 
1 324 LEU n 
1 325 THR n 
1 326 PRO n 
1 327 THR n 
1 328 ASP n 
1 329 LEU n 
1 330 TYR n 
1 331 ALA n 
1 332 CYS n 
1 333 ARG n 
1 334 PRO n 
1 335 LEU n 
1 336 CYS n 
1 337 ASP n 
1 338 SER n 
1 339 GLY n 
1 340 TYR n 
1 341 TYR n 
1 342 GLU n 
1 343 ILE n 
1 344 PHE n 
1 345 ASN n 
1 346 ARG n 
1 347 ASP n 
1 348 ASN n 
1 349 VAL n 
1 350 SER n 
1 351 LEU n 
1 352 GLU n 
1 353 ASP n 
1 354 VAL n 
1 355 LYS n 
1 356 ALA n 
1 357 ASN n 
1 358 PRO n 
1 359 ILE n 
1 360 VAL n 
1 361 GLU n 
1 362 ILE n 
1 363 LYS n 
1 364 GLU n 
1 365 ASP n 
1 366 CYS n 
1 367 VAL n 
1 368 VAL n 
1 369 THR n 
1 370 ALA n 
1 371 ASP n 
1 372 GLY n 
1 373 VAL n 
1 374 GLU n 
1 375 HIS n 
1 376 LYS n 
1 377 LEU n 
1 378 ASP n 
1 379 MET n 
1 380 LEU n 
1 381 ILE n 
1 382 CYS n 
1 383 ALA n 
1 384 THR n 
1 385 GLY n 
1 386 PHE n 
1 387 ASP n 
1 388 ALA n 
1 389 VAL n 
1 390 ASP n 
1 391 GLY n 
1 392 SER n 
1 393 TYR n 
1 394 LYS n 
1 395 ARG n 
1 396 ILE n 
1 397 ASP n 
1 398 ILE n 
1 399 ARG n 
1 400 GLY n 
1 401 LYS n 
1 402 ASP n 
1 403 GLY n 
1 404 ILE n 
1 405 SER n 
1 406 ILE n 
1 407 LYS n 
1 408 ASP n 
1 409 HIS n 
1 410 TRP n 
1 411 LYS n 
1 412 ASP n 
1 413 GLY n 
1 414 PRO n 
1 415 ASN n 
1 416 SER n 
1 417 TYR n 
1 418 LEU n 
1 419 GLY n 
1 420 MET n 
1 421 MET n 
1 422 VAL n 
1 423 SER n 
1 424 ASN n 
1 425 PHE n 
1 426 PRO n 
1 427 ASN n 
1 428 MET n 
1 429 PHE n 
1 430 MET n 
1 431 VAL n 
1 432 PHE n 
1 433 GLY n 
1 434 PRO n 
1 435 ASN n 
1 436 GLY n 
1 437 PRO n 
1 438 LEU n 
1 439 ALA n 
1 440 ASN n 
1 441 SER n 
1 442 PRO n 
1 443 PRO n 
1 444 ILE n 
1 445 ILE n 
1 446 GLU n 
1 447 THR n 
1 448 GLN n 
1 449 VAL n 
1 450 ARG n 
1 451 TRP n 
1 452 ILE n 
1 453 ALA n 
1 454 ASP n 
1 455 LEU n 
1 456 ILE n 
1 457 GLY n 
1 458 TYR n 
1 459 ALA n 
1 460 GLU n 
1 461 ASP n 
1 462 HIS n 
1 463 GLN n 
1 464 ILE n 
1 465 ASN n 
1 466 GLN n 
1 467 ILE n 
1 468 GLU n 
1 469 ALA n 
1 470 THR n 
1 471 LYS n 
1 472 ASP n 
1 473 ALA n 
1 474 VAL n 
1 475 ASP n 
1 476 ASN n 
1 477 TRP n 
1 478 THR n 
1 479 ASN n 
1 480 THR n 
1 481 CYS n 
1 482 SER n 
1 483 ASP n 
1 484 ILE n 
1 485 ALA n 
1 486 ASN n 
1 487 LYS n 
1 488 THR n 
1 489 LEU n 
1 490 PHE n 
1 491 ALA n 
1 492 LYS n 
1 493 ALA n 
1 494 LYS n 
1 495 CYS n 
1 496 ARG n 
1 497 ILE n 
1 498 PHE n 
1 499 GLY n 
1 500 ALA n 
1 501 ASN n 
1 502 VAL n 
1 503 PRO n 
1 504 GLY n 
1 505 LYS n 
1 506 LYS n 
1 507 ASN n 
1 508 THR n 
1 509 VAL n 
1 510 TYR n 
1 511 LEU n 
1 512 TYR n 
1 513 MET n 
1 514 GLY n 
1 515 GLY n 
1 516 LEU n 
1 517 LYS n 
1 518 GLU n 
1 519 TYR n 
1 520 ARG n 
1 521 ASN n 
1 522 GLN n 
1 523 ILE n 
1 524 SER n 
1 525 GLU n 
1 526 VAL n 
1 527 SER n 
1 528 ASN n 
1 529 ASN n 
1 530 ASN n 
1 531 TYR n 
1 532 LYS n 
1 533 GLY n 
1 534 CYS n 
1 535 LEU n 
1 536 LEU n 
1 537 LYS n 
1 538 GLN n 
1 539 SER n 
1 540 VAL n 
1 541 LYS n 
1 542 LYS n 
1 543 THR n 
1 544 ASN n 
1 545 LEU n 
1 546 ILE n 
1 547 GLU n 
1 548 SER n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   548 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 P23_1101 
_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      'Acinetobacter calcoaceticus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     471 
_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      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_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                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                        ?    'C3 H7 N O2'        89.093  
ARG 'L-peptide linking' y ARGININE                                       ?    'C6 H15 N4 O2 1'    175.209 
ASN 'L-peptide linking' y ASPARAGINE                                     ?    'C4 H8 N2 O3'       132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                ?    'C4 H7 N O4'        133.103 
CYS 'L-peptide linking' y CYSTEINE                                       ?    'C3 H7 N O2 S'      121.158 
FAD non-polymer         . 'FLAVIN-ADENINE DINUCLEOTIDE'                  ?    'C27 H33 N9 O15 P2' 785.550 
GLN 'L-peptide linking' y GLUTAMINE                                      ?    'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                ?    'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                                        ?    'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE                                      ?    'C6 H10 N3 O2 1'    156.162 
HOH non-polymer         . WATER                                          ?    'H2 O'              18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                     ?    'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE                                        ?    'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE                                         ?    'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE                                     ?    'C5 H11 N O2 S'     149.211 
NAI non-polymer         . '1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE' NADH 'C21 H29 N7 O14 P2' 665.441 
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   -5  ?   ?   ?   A . n 
A 1 2   HIS 2   -4  ?   ?   ?   A . n 
A 1 3   HIS 3   -3  ?   ?   ?   A . n 
A 1 4   HIS 4   -2  ?   ?   ?   A . n 
A 1 5   HIS 5   -1  ?   ?   ?   A . n 
A 1 6   HIS 6   0   ?   ?   ?   A . n 
A 1 7   HIS 7   1   ?   ?   ?   A . n 
A 1 8   THR 8   2   2   THR THR A . n 
A 1 9   GLN 9   3   3   GLN GLN A . n 
A 1 10  LYS 10  4   4   LYS LYS A . n 
A 1 11  MET 11  5   5   MET MET A . n 
A 1 12  ASP 12  6   6   ASP ASP A . n 
A 1 13  PHE 13  7   7   PHE PHE A . n 
A 1 14  ASP 14  8   8   ASP ASP A . n 
A 1 15  ALA 15  9   9   ALA ALA A . n 
A 1 16  ILE 16  10  10  ILE ILE A . n 
A 1 17  ILE 17  11  11  ILE ILE A . n 
A 1 18  ILE 18  12  12  ILE ILE A . n 
A 1 19  GLY 19  13  13  GLY GLY A . n 
A 1 20  ALA 20  14  14  ALA ALA A . n 
A 1 21  GLY 21  15  15  GLY GLY A . n 
A 1 22  PHE 22  16  16  PHE PHE A . n 
A 1 23  GLY 23  17  17  GLY GLY A . n 
A 1 24  GLY 24  18  18  GLY GLY A . n 
A 1 25  LEU 25  19  19  LEU LEU A . n 
A 1 26  TYR 26  20  20  TYR TYR A . n 
A 1 27  SER 27  21  21  SER SER A . n 
A 1 28  LEU 28  22  22  LEU LEU A . n 
A 1 29  LYS 29  23  23  LYS LYS A . n 
A 1 30  LYS 30  24  24  LYS LYS A . n 
A 1 31  LEU 31  25  25  LEU LEU A . n 
A 1 32  ARG 32  26  26  ARG ARG A . n 
A 1 33  ASP 33  27  27  ASP ASP A . n 
A 1 34  ASP 34  28  28  ASP ASP A . n 
A 1 35  PHE 35  29  29  PHE PHE A . n 
A 1 36  ASN 36  30  30  ASN ASN A . n 
A 1 37  LEU 37  31  31  LEU LEU A . n 
A 1 38  LYS 38  32  32  LYS LYS A . n 
A 1 39  VAL 39  33  33  VAL VAL A . n 
A 1 40  ARG 40  34  34  ARG ARG A . n 
A 1 41  ALA 41  35  35  ALA ALA A . n 
A 1 42  PHE 42  36  36  PHE PHE A . n 
A 1 43  ASP 43  37  37  ASP ASP A . n 
A 1 44  ARG 44  38  38  ARG ARG A . n 
A 1 45  ALA 45  39  39  ALA ALA A . n 
A 1 46  THR 46  40  40  THR THR A . n 
A 1 47  GLU 47  41  41  GLU GLU A . n 
A 1 48  VAL 48  42  42  VAL VAL A . n 
A 1 49  GLY 49  43  43  GLY GLY A . n 
A 1 50  GLY 50  44  44  GLY GLY A . n 
A 1 51  THR 51  45  45  THR THR A . n 
A 1 52  TRP 52  46  46  TRP TRP A . n 
A 1 53  PHE 53  47  47  PHE PHE A . n 
A 1 54  TRP 54  48  48  TRP TRP A . n 
A 1 55  ASN 55  49  49  ASN ASN A . n 
A 1 56  GLN 56  50  50  GLN GLN A . n 
A 1 57  TYR 57  51  51  TYR TYR A . n 
A 1 58  PRO 58  52  52  PRO PRO A . n 
A 1 59  GLY 59  53  53  GLY GLY A . n 
A 1 60  ALA 60  54  54  ALA ALA A . n 
A 1 61  LEU 61  55  55  LEU LEU A . n 
A 1 62  SER 62  56  56  SER SER A . n 
A 1 63  ASP 63  57  57  ASP ASP A . n 
A 1 64  SER 64  58  58  SER SER A . n 
A 1 65  GLU 65  59  59  GLU GLU A . n 
A 1 66  THR 66  60  60  THR THR A . n 
A 1 67  HIS 67  61  61  HIS HIS A . n 
A 1 68  LEU 68  62  62  LEU LEU A . n 
A 1 69  TYR 69  63  63  TYR TYR A . n 
A 1 70  CYS 70  64  64  CYS CYS A . n 
A 1 71  TYR 71  65  65  TYR TYR A . n 
A 1 72  SER 72  66  66  SER SER A . n 
A 1 73  TRP 73  67  67  TRP TRP A . n 
A 1 74  ASP 74  68  68  ASP ASP A . n 
A 1 75  LYS 75  69  69  LYS LYS A . n 
A 1 76  GLU 76  70  70  GLU GLU A . n 
A 1 77  LEU 77  71  71  LEU LEU A . n 
A 1 78  LEU 78  72  72  LEU LEU A . n 
A 1 79  GLN 79  73  73  GLN GLN A . n 
A 1 80  GLU 80  74  74  GLU GLU A . n 
A 1 81  MET 81  75  75  MET MET A . n 
A 1 82  GLU 82  76  76  GLU GLU A . n 
A 1 83  ILE 83  77  77  ILE ILE A . n 
A 1 84  LYS 84  78  78  LYS LYS A . n 
A 1 85  ARG 85  79  79  ARG ARG A . n 
A 1 86  LYS 86  80  80  LYS LYS A . n 
A 1 87  TYR 87  81  81  TYR TYR A . n 
A 1 88  ILE 88  82  82  ILE ILE A . n 
A 1 89  SER 89  83  83  SER SER A . n 
A 1 90  GLN 90  84  84  GLN GLN A . n 
A 1 91  PRO 91  85  85  PRO PRO A . n 
A 1 92  ASP 92  86  86  ASP ASP A . n 
A 1 93  VAL 93  87  87  VAL VAL A . n 
A 1 94  LEU 94  88  88  LEU LEU A . n 
A 1 95  ALA 95  89  89  ALA ALA A . n 
A 1 96  TYR 96  90  90  TYR TYR A . n 
A 1 97  LEU 97  91  91  LEU LEU A . n 
A 1 98  LYS 98  92  92  LYS LYS A . n 
A 1 99  ARG 99  93  93  ARG ARG A . n 
A 1 100 VAL 100 94  94  VAL VAL A . n 
A 1 101 ALA 101 95  95  ALA ALA A . n 
A 1 102 ASP 102 96  96  ASP ASP A . n 
A 1 103 LYS 103 97  97  LYS LYS A . n 
A 1 104 HIS 104 98  98  HIS HIS A . n 
A 1 105 ASP 105 99  99  ASP ASP A . n 
A 1 106 LEU 106 100 100 LEU LEU A . n 
A 1 107 ARG 107 101 101 ARG ARG A . n 
A 1 108 LYS 108 102 102 LYS LYS A . n 
A 1 109 ASP 109 103 103 ASP ASP A . n 
A 1 110 ILE 110 104 104 ILE ILE A . n 
A 1 111 GLN 111 105 105 GLN GLN A . n 
A 1 112 PHE 112 106 106 PHE PHE A . n 
A 1 113 GLU 113 107 107 GLU GLU A . n 
A 1 114 THR 114 108 108 THR THR A . n 
A 1 115 GLY 115 109 109 GLY GLY A . n 
A 1 116 ILE 116 110 110 ILE ILE A . n 
A 1 117 ARG 117 111 111 ARG ARG A . n 
A 1 118 SER 118 112 112 SER SER A . n 
A 1 119 ALA 119 113 113 ALA ALA A . n 
A 1 120 TYR 120 114 114 TYR TYR A . n 
A 1 121 PHE 121 115 115 PHE PHE A . n 
A 1 122 ASP 122 116 116 ASP ASP A . n 
A 1 123 GLU 123 117 117 GLU GLU A . n 
A 1 124 GLU 124 118 118 GLU GLU A . n 
A 1 125 ASN 125 119 119 ASN ASN A . n 
A 1 126 SER 126 120 120 SER SER A . n 
A 1 127 PHE 127 121 121 PHE PHE A . n 
A 1 128 TRP 128 122 122 TRP TRP A . n 
A 1 129 ASN 129 123 123 ASN ASN A . n 
A 1 130 VAL 130 124 124 VAL VAL A . n 
A 1 131 THR 131 125 125 THR THR A . n 
A 1 132 THR 132 126 126 THR THR A . n 
A 1 133 GLU 133 127 127 GLU GLU A . n 
A 1 134 ASN 134 128 128 ASN ASN A . n 
A 1 135 ASP 135 129 129 ASP ASP A . n 
A 1 136 GLU 136 130 130 GLU GLU A . n 
A 1 137 LYS 137 131 131 LYS LYS A . n 
A 1 138 PHE 138 132 132 PHE PHE A . n 
A 1 139 THR 139 133 133 THR THR A . n 
A 1 140 ALA 140 134 134 ALA ALA A . n 
A 1 141 ARG 141 135 135 ARG ARG A . n 
A 1 142 PHE 142 136 136 PHE PHE A . n 
A 1 143 LEU 143 137 137 LEU LEU A . n 
A 1 144 ILE 144 138 138 ILE ILE A . n 
A 1 145 THR 145 139 139 THR THR A . n 
A 1 146 ALA 146 140 140 ALA ALA A . n 
A 1 147 LEU 147 141 141 LEU LEU A . n 
A 1 148 GLY 148 142 142 GLY GLY A . n 
A 1 149 PRO 149 143 143 PRO PRO A . n 
A 1 150 LEU 150 144 144 LEU LEU A . n 
A 1 151 SER 151 145 145 SER SER A . n 
A 1 152 SER 152 146 146 SER SER A . n 
A 1 153 PRO 153 147 147 PRO PRO A . n 
A 1 154 ASN 154 148 148 ASN ASN A . n 
A 1 155 TRP 155 149 149 TRP TRP A . n 
A 1 156 PRO 156 150 150 PRO PRO A . n 
A 1 157 ILE 157 151 151 ILE ILE A . n 
A 1 158 ILE 158 152 152 ILE ILE A . n 
A 1 159 LYS 159 153 153 LYS LYS A . n 
A 1 160 GLY 160 154 154 GLY GLY A . n 
A 1 161 ILE 161 155 155 ILE ILE A . n 
A 1 162 GLU 162 156 156 GLU GLU A . n 
A 1 163 THR 163 157 157 THR THR A . n 
A 1 164 PHE 164 158 158 PHE PHE A . n 
A 1 165 LYS 165 159 159 LYS LYS A . n 
A 1 166 GLY 166 160 160 GLY GLY A . n 
A 1 167 GLU 167 161 161 GLU GLU A . n 
A 1 168 LEU 168 162 162 LEU LEU A . n 
A 1 169 HIS 169 163 163 HIS HIS A . n 
A 1 170 HIS 170 164 164 HIS HIS A . n 
A 1 171 THR 171 165 165 THR THR A . n 
A 1 172 SER 172 166 166 SER SER A . n 
A 1 173 ARG 173 167 167 ARG ARG A . n 
A 1 174 TRP 174 168 168 TRP TRP A . n 
A 1 175 PRO 175 169 169 PRO PRO A . n 
A 1 176 LYS 176 170 170 LYS LYS A . n 
A 1 177 ASP 177 171 171 ASP ASP A . n 
A 1 178 VAL 178 172 172 VAL VAL A . n 
A 1 179 THR 179 173 173 THR THR A . n 
A 1 180 PHE 180 174 174 PHE PHE A . n 
A 1 181 SER 181 175 175 SER SER A . n 
A 1 182 GLY 182 176 176 GLY GLY A . n 
A 1 183 LYS 183 177 177 LYS LYS A . n 
A 1 184 ARG 184 178 178 ARG ARG A . n 
A 1 185 VAL 185 179 179 VAL VAL A . n 
A 1 186 GLY 186 180 180 GLY GLY A . n 
A 1 187 VAL 187 181 181 VAL VAL A . n 
A 1 188 ILE 188 182 182 ILE ILE A . n 
A 1 189 GLY 189 183 183 GLY GLY A . n 
A 1 190 THR 190 184 184 THR THR A . n 
A 1 191 GLY 191 185 185 GLY GLY A . n 
A 1 192 SER 192 186 186 SER SER A . n 
A 1 193 THR 193 187 187 THR THR A . n 
A 1 194 GLY 194 188 188 GLY GLY A . n 
A 1 195 VAL 195 189 189 VAL VAL A . n 
A 1 196 GLN 196 190 190 GLN GLN A . n 
A 1 197 VAL 197 191 191 VAL VAL A . n 
A 1 198 ILE 198 192 192 ILE ILE A . n 
A 1 199 THR 199 193 193 THR THR A . n 
A 1 200 ALA 200 194 194 ALA ALA A . n 
A 1 201 ILE 201 195 195 ILE ILE A . n 
A 1 202 ALA 202 196 196 ALA ALA A . n 
A 1 203 SER 203 197 197 SER SER A . n 
A 1 204 GLN 204 198 198 GLN GLN A . n 
A 1 205 VAL 205 199 199 VAL VAL A . n 
A 1 206 LYS 206 200 200 LYS LYS A . n 
A 1 207 HIS 207 201 201 HIS HIS A . n 
A 1 208 LEU 208 202 202 LEU LEU A . n 
A 1 209 THR 209 203 203 THR THR A . n 
A 1 210 VAL 210 204 204 VAL VAL A . n 
A 1 211 PHE 211 205 205 PHE PHE A . n 
A 1 212 GLN 212 206 206 GLN GLN A . n 
A 1 213 ARG 213 207 207 ARG ARG A . n 
A 1 214 SER 214 208 208 SER SER A . n 
A 1 215 ALA 215 209 209 ALA ALA A . n 
A 1 216 GLN 216 210 210 GLN GLN A . n 
A 1 217 TYR 217 211 211 TYR TYR A . n 
A 1 218 SER 218 212 212 SER SER A . n 
A 1 219 VAL 219 213 213 VAL VAL A . n 
A 1 220 PRO 220 214 214 PRO PRO A . n 
A 1 221 ILE 221 215 215 ILE ILE A . n 
A 1 222 GLY 222 216 216 GLY GLY A . n 
A 1 223 ASN 223 217 217 ASN ASN A . n 
A 1 224 VAL 224 218 218 VAL VAL A . n 
A 1 225 VAL 225 219 219 VAL VAL A . n 
A 1 226 MET 226 220 220 MET MET A . n 
A 1 227 SER 227 221 221 SER SER A . n 
A 1 228 GLU 228 222 222 GLU GLU A . n 
A 1 229 THR 229 223 223 THR THR A . n 
A 1 230 ASP 230 224 224 ASP ASP A . n 
A 1 231 VAL 231 225 225 VAL VAL A . n 
A 1 232 ALA 232 226 226 ALA ALA A . n 
A 1 233 LYS 233 227 227 LYS LYS A . n 
A 1 234 ILE 234 228 228 ILE ILE A . n 
A 1 235 LYS 235 229 229 LYS LYS A . n 
A 1 236 GLU 236 230 230 GLU GLU A . n 
A 1 237 ASN 237 231 231 ASN ASN A . n 
A 1 238 TYR 238 232 232 TYR TYR A . n 
A 1 239 ASP 239 233 233 ASP ASP A . n 
A 1 240 GLN 240 234 234 GLN GLN A . n 
A 1 241 ILE 241 235 235 ILE ILE A . n 
A 1 242 TRP 242 236 236 TRP TRP A . n 
A 1 243 GLU 243 237 237 GLU GLU A . n 
A 1 244 ASN 244 238 238 ASN ASN A . n 
A 1 245 VAL 245 239 239 VAL VAL A . n 
A 1 246 TRP 246 240 240 TRP TRP A . n 
A 1 247 ASN 247 241 241 ASN ASN A . n 
A 1 248 SER 248 242 242 SER SER A . n 
A 1 249 ALA 249 243 243 ALA ALA A . n 
A 1 250 LEU 250 244 244 LEU LEU A . n 
A 1 251 GLY 251 245 245 GLY GLY A . n 
A 1 252 TYR 252 246 246 TYR TYR A . n 
A 1 253 GLY 253 247 247 GLY GLY A . n 
A 1 254 LEU 254 248 248 LEU LEU A . n 
A 1 255 ASN 255 249 249 ASN ASN A . n 
A 1 256 GLU 256 250 250 GLU GLU A . n 
A 1 257 SER 257 251 251 SER SER A . n 
A 1 258 THR 258 252 252 THR THR A . n 
A 1 259 LEU 259 253 253 LEU LEU A . n 
A 1 260 PRO 260 254 254 PRO PRO A . n 
A 1 261 THR 261 255 255 THR THR A . n 
A 1 262 MET 262 256 256 MET MET A . n 
A 1 263 SER 263 257 257 SER SER A . n 
A 1 264 VAL 264 258 258 VAL VAL A . n 
A 1 265 SER 265 259 259 SER SER A . n 
A 1 266 ALA 266 260 260 ALA ALA A . n 
A 1 267 GLU 267 261 261 GLU GLU A . n 
A 1 268 GLU 268 262 262 GLU GLU A . n 
A 1 269 ARG 269 263 263 ARG ARG A . n 
A 1 270 ASP 270 264 264 ASP ASP A . n 
A 1 271 LYS 271 265 265 LYS LYS A . n 
A 1 272 ILE 272 266 266 ILE ILE A . n 
A 1 273 PHE 273 267 267 PHE PHE A . n 
A 1 274 GLU 274 268 268 GLU GLU A . n 
A 1 275 LYS 275 269 269 LYS LYS A . n 
A 1 276 ALA 276 270 270 ALA ALA A . n 
A 1 277 TRP 277 271 271 TRP TRP A . n 
A 1 278 GLN 278 272 272 GLN GLN A . n 
A 1 279 GLU 279 273 273 GLU GLU A . n 
A 1 280 GLY 280 274 274 GLY GLY A . n 
A 1 281 GLY 281 275 275 GLY GLY A . n 
A 1 282 GLY 282 276 276 GLY GLY A . n 
A 1 283 PHE 283 277 277 PHE PHE A . n 
A 1 284 ARG 284 278 278 ARG ARG A . n 
A 1 285 PHE 285 279 279 PHE PHE A . n 
A 1 286 MET 286 280 280 MET MET A . n 
A 1 287 PHE 287 281 281 PHE PHE A . n 
A 1 288 GLU 288 282 282 GLU GLU A . n 
A 1 289 THR 289 283 283 THR THR A . n 
A 1 290 PHE 290 284 284 PHE PHE A . n 
A 1 291 GLY 291 285 285 GLY GLY A . n 
A 1 292 ASP 292 286 286 ASP ASP A . n 
A 1 293 ILE 293 287 287 ILE ILE A . n 
A 1 294 ALA 294 288 288 ALA ALA A . n 
A 1 295 VAL 295 289 289 VAL VAL A . n 
A 1 296 ASP 296 290 290 ASP ASP A . n 
A 1 297 GLU 297 291 291 GLU GLU A . n 
A 1 298 THR 298 292 292 THR THR A . n 
A 1 299 ALA 299 293 293 ALA ALA A . n 
A 1 300 ASN 300 294 294 ASN ASN A . n 
A 1 301 ILE 301 295 295 ILE ILE A . n 
A 1 302 GLU 302 296 296 GLU GLU A . n 
A 1 303 ALA 303 297 297 ALA ALA A . n 
A 1 304 GLN 304 298 298 GLN GLN A . n 
A 1 305 ASN 305 299 299 ASN ASN A . n 
A 1 306 PHE 306 300 300 PHE PHE A . n 
A 1 307 ILE 307 301 301 ILE ILE A . n 
A 1 308 LYS 308 302 302 LYS LYS A . n 
A 1 309 LYS 309 303 303 LYS LYS A . n 
A 1 310 LYS 310 304 304 LYS LYS A . n 
A 1 311 ILE 311 305 305 ILE ILE A . n 
A 1 312 SER 312 306 306 SER SER A . n 
A 1 313 GLU 313 307 307 GLU GLU A . n 
A 1 314 ILE 314 308 308 ILE ILE A . n 
A 1 315 VAL 315 309 309 VAL VAL A . n 
A 1 316 LYS 316 310 310 LYS LYS A . n 
A 1 317 ASP 317 311 311 ASP ASP A . n 
A 1 318 PRO 318 312 312 PRO PRO A . n 
A 1 319 PHE 319 313 313 PHE PHE A . n 
A 1 320 VAL 320 314 314 VAL VAL A . n 
A 1 321 ALA 321 315 315 ALA ALA A . n 
A 1 322 LYS 322 316 316 LYS LYS A . n 
A 1 323 LYS 323 317 317 LYS LYS A . n 
A 1 324 LEU 324 318 318 LEU LEU A . n 
A 1 325 THR 325 319 319 THR THR A . n 
A 1 326 PRO 326 320 320 PRO PRO A . n 
A 1 327 THR 327 321 321 THR THR A . n 
A 1 328 ASP 328 322 322 ASP ASP A . n 
A 1 329 LEU 329 323 323 LEU LEU A . n 
A 1 330 TYR 330 324 324 TYR TYR A . n 
A 1 331 ALA 331 325 325 ALA ALA A . n 
A 1 332 CYS 332 326 326 CYS CYS A . n 
A 1 333 ARG 333 327 327 ARG ARG A . n 
A 1 334 PRO 334 328 328 PRO PRO A . n 
A 1 335 LEU 335 329 329 LEU LEU A . n 
A 1 336 CYS 336 330 330 CYS CYS A . n 
A 1 337 ASP 337 331 331 ASP ASP A . n 
A 1 338 SER 338 332 332 SER SER A . n 
A 1 339 GLY 339 333 333 GLY GLY A . n 
A 1 340 TYR 340 334 334 TYR TYR A . n 
A 1 341 TYR 341 335 335 TYR TYR A . n 
A 1 342 GLU 342 336 336 GLU GLU A . n 
A 1 343 ILE 343 337 337 ILE ILE A . n 
A 1 344 PHE 344 338 338 PHE PHE A . n 
A 1 345 ASN 345 339 339 ASN ASN A . n 
A 1 346 ARG 346 340 340 ARG ARG A . n 
A 1 347 ASP 347 341 341 ASP ASP A . n 
A 1 348 ASN 348 342 342 ASN ASN A . n 
A 1 349 VAL 349 343 343 VAL VAL A . n 
A 1 350 SER 350 344 344 SER SER A . n 
A 1 351 LEU 351 345 345 LEU LEU A . n 
A 1 352 GLU 352 346 346 GLU GLU A . n 
A 1 353 ASP 353 347 347 ASP ASP A . n 
A 1 354 VAL 354 348 348 VAL VAL A . n 
A 1 355 LYS 355 349 349 LYS LYS A . n 
A 1 356 ALA 356 350 350 ALA ALA A . n 
A 1 357 ASN 357 351 351 ASN ASN A . n 
A 1 358 PRO 358 352 352 PRO PRO A . n 
A 1 359 ILE 359 353 353 ILE ILE A . n 
A 1 360 VAL 360 354 354 VAL VAL A . n 
A 1 361 GLU 361 355 355 GLU GLU A . n 
A 1 362 ILE 362 356 356 ILE ILE A . n 
A 1 363 LYS 363 357 357 LYS LYS A . n 
A 1 364 GLU 364 358 358 GLU GLU A . n 
A 1 365 ASP 365 359 359 ASP ASP A . n 
A 1 366 CYS 366 360 360 CYS CYS A . n 
A 1 367 VAL 367 361 361 VAL VAL A . n 
A 1 368 VAL 368 362 362 VAL VAL A . n 
A 1 369 THR 369 363 363 THR THR A . n 
A 1 370 ALA 370 364 364 ALA ALA A . n 
A 1 371 ASP 371 365 365 ASP ASP A . n 
A 1 372 GLY 372 366 366 GLY GLY A . n 
A 1 373 VAL 373 367 367 VAL VAL A . n 
A 1 374 GLU 374 368 368 GLU GLU A . n 
A 1 375 HIS 375 369 369 HIS HIS A . n 
A 1 376 LYS 376 370 370 LYS LYS A . n 
A 1 377 LEU 377 371 371 LEU LEU A . n 
A 1 378 ASP 378 372 372 ASP ASP A . n 
A 1 379 MET 379 373 373 MET MET A . n 
A 1 380 LEU 380 374 374 LEU LEU A . n 
A 1 381 ILE 381 375 375 ILE ILE A . n 
A 1 382 CYS 382 376 376 CYS CYS A . n 
A 1 383 ALA 383 377 377 ALA ALA A . n 
A 1 384 THR 384 378 378 THR THR A . n 
A 1 385 GLY 385 379 379 GLY GLY A . n 
A 1 386 PHE 386 380 380 PHE PHE A . n 
A 1 387 ASP 387 381 381 ASP ASP A . n 
A 1 388 ALA 388 382 382 ALA ALA A . n 
A 1 389 VAL 389 383 383 VAL VAL A . n 
A 1 390 ASP 390 384 384 ASP ASP A . n 
A 1 391 GLY 391 385 385 GLY GLY A . n 
A 1 392 SER 392 386 386 SER SER A . n 
A 1 393 TYR 393 387 387 TYR TYR A . n 
A 1 394 LYS 394 388 388 LYS LYS A . n 
A 1 395 ARG 395 389 389 ARG ARG A . n 
A 1 396 ILE 396 390 390 ILE ILE A . n 
A 1 397 ASP 397 391 391 ASP ASP A . n 
A 1 398 ILE 398 392 392 ILE ILE A . n 
A 1 399 ARG 399 393 393 ARG ARG A . n 
A 1 400 GLY 400 394 394 GLY GLY A . n 
A 1 401 LYS 401 395 395 LYS LYS A . n 
A 1 402 ASP 402 396 396 ASP ASP A . n 
A 1 403 GLY 403 397 397 GLY GLY A . n 
A 1 404 ILE 404 398 398 ILE ILE A . n 
A 1 405 SER 405 399 399 SER SER A . n 
A 1 406 ILE 406 400 400 ILE ILE A . n 
A 1 407 LYS 407 401 401 LYS LYS A . n 
A 1 408 ASP 408 402 402 ASP ASP A . n 
A 1 409 HIS 409 403 403 HIS HIS A . n 
A 1 410 TRP 410 404 404 TRP TRP A . n 
A 1 411 LYS 411 405 405 LYS LYS A . n 
A 1 412 ASP 412 406 406 ASP ASP A . n 
A 1 413 GLY 413 407 407 GLY GLY A . n 
A 1 414 PRO 414 408 408 PRO PRO A . n 
A 1 415 ASN 415 409 409 ASN ASN A . n 
A 1 416 SER 416 410 410 SER SER A . n 
A 1 417 TYR 417 411 411 TYR TYR A . n 
A 1 418 LEU 418 412 412 LEU LEU A . n 
A 1 419 GLY 419 413 413 GLY GLY A . n 
A 1 420 MET 420 414 414 MET MET A . n 
A 1 421 MET 421 415 415 MET MET A . n 
A 1 422 VAL 422 416 416 VAL VAL A . n 
A 1 423 SER 423 417 417 SER SER A . n 
A 1 424 ASN 424 418 418 ASN ASN A . n 
A 1 425 PHE 425 419 419 PHE PHE A . n 
A 1 426 PRO 426 420 420 PRO PRO A . n 
A 1 427 ASN 427 421 421 ASN ASN A . n 
A 1 428 MET 428 422 422 MET MET A . n 
A 1 429 PHE 429 423 423 PHE PHE A . n 
A 1 430 MET 430 424 424 MET MET A . n 
A 1 431 VAL 431 425 425 VAL VAL A . n 
A 1 432 PHE 432 426 426 PHE PHE A . n 
A 1 433 GLY 433 427 427 GLY GLY A . n 
A 1 434 PRO 434 428 428 PRO PRO A . n 
A 1 435 ASN 435 429 429 ASN ASN A . n 
A 1 436 GLY 436 430 430 GLY GLY A . n 
A 1 437 PRO 437 431 431 PRO PRO A . n 
A 1 438 LEU 438 432 432 LEU LEU A . n 
A 1 439 ALA 439 433 433 ALA ALA A . n 
A 1 440 ASN 440 434 434 ASN ASN A . n 
A 1 441 SER 441 435 435 SER SER A . n 
A 1 442 PRO 442 436 436 PRO PRO A . n 
A 1 443 PRO 443 437 437 PRO PRO A . n 
A 1 444 ILE 444 438 438 ILE ILE A . n 
A 1 445 ILE 445 439 439 ILE ILE A . n 
A 1 446 GLU 446 440 440 GLU GLU A . n 
A 1 447 THR 447 441 441 THR THR A . n 
A 1 448 GLN 448 442 442 GLN GLN A . n 
A 1 449 VAL 449 443 443 VAL VAL A . n 
A 1 450 ARG 450 444 444 ARG ARG A . n 
A 1 451 TRP 451 445 445 TRP TRP A . n 
A 1 452 ILE 452 446 446 ILE ILE A . n 
A 1 453 ALA 453 447 447 ALA ALA A . n 
A 1 454 ASP 454 448 448 ASP ASP A . n 
A 1 455 LEU 455 449 449 LEU LEU A . n 
A 1 456 ILE 456 450 450 ILE ILE A . n 
A 1 457 GLY 457 451 451 GLY GLY A . n 
A 1 458 TYR 458 452 452 TYR TYR A . n 
A 1 459 ALA 459 453 453 ALA ALA A . n 
A 1 460 GLU 460 454 454 GLU GLU A . n 
A 1 461 ASP 461 455 455 ASP ASP A . n 
A 1 462 HIS 462 456 456 HIS HIS A . n 
A 1 463 GLN 463 457 457 GLN GLN A . n 
A 1 464 ILE 464 458 458 ILE ILE A . n 
A 1 465 ASN 465 459 459 ASN ASN A . n 
A 1 466 GLN 466 460 460 GLN GLN A . n 
A 1 467 ILE 467 461 461 ILE ILE A . n 
A 1 468 GLU 468 462 462 GLU GLU A . n 
A 1 469 ALA 469 463 463 ALA ALA A . n 
A 1 470 THR 470 464 464 THR THR A . n 
A 1 471 LYS 471 465 465 LYS LYS A . n 
A 1 472 ASP 472 466 466 ASP ASP A . n 
A 1 473 ALA 473 467 467 ALA ALA A . n 
A 1 474 VAL 474 468 468 VAL VAL A . n 
A 1 475 ASP 475 469 469 ASP ASP A . n 
A 1 476 ASN 476 470 470 ASN ASN A . n 
A 1 477 TRP 477 471 471 TRP TRP A . n 
A 1 478 THR 478 472 472 THR THR A . n 
A 1 479 ASN 479 473 473 ASN ASN A . n 
A 1 480 THR 480 474 474 THR THR A . n 
A 1 481 CYS 481 475 475 CYS CYS A . n 
A 1 482 SER 482 476 476 SER SER A . n 
A 1 483 ASP 483 477 477 ASP ASP A . n 
A 1 484 ILE 484 478 478 ILE ILE A . n 
A 1 485 ALA 485 479 479 ALA ALA A . n 
A 1 486 ASN 486 480 480 ASN ASN A . n 
A 1 487 LYS 487 481 481 LYS LYS A . n 
A 1 488 THR 488 482 482 THR THR A . n 
A 1 489 LEU 489 483 483 LEU LEU A . n 
A 1 490 PHE 490 484 484 PHE PHE A . n 
A 1 491 ALA 491 485 485 ALA ALA A . n 
A 1 492 LYS 492 486 486 LYS LYS A . n 
A 1 493 ALA 493 487 487 ALA ALA A . n 
A 1 494 LYS 494 488 488 LYS LYS A . n 
A 1 495 CYS 495 489 ?   ?   ?   A . n 
A 1 496 ARG 496 490 ?   ?   ?   A . n 
A 1 497 ILE 497 491 ?   ?   ?   A . n 
A 1 498 PHE 498 492 ?   ?   ?   A . n 
A 1 499 GLY 499 493 ?   ?   ?   A . n 
A 1 500 ALA 500 494 ?   ?   ?   A . n 
A 1 501 ASN 501 495 ?   ?   ?   A . n 
A 1 502 VAL 502 496 ?   ?   ?   A . n 
A 1 503 PRO 503 497 ?   ?   ?   A . n 
A 1 504 GLY 504 498 ?   ?   ?   A . n 
A 1 505 LYS 505 499 ?   ?   ?   A . n 
A 1 506 LYS 506 500 ?   ?   ?   A . n 
A 1 507 ASN 507 501 501 ASN ASN A . n 
A 1 508 THR 508 502 502 THR THR A . n 
A 1 509 VAL 509 503 503 VAL VAL A . n 
A 1 510 TYR 510 504 504 TYR TYR A . n 
A 1 511 LEU 511 505 505 LEU LEU A . n 
A 1 512 TYR 512 506 506 TYR TYR A . n 
A 1 513 MET 513 507 507 MET MET A . n 
A 1 514 GLY 514 508 508 GLY GLY A . n 
A 1 515 GLY 515 509 509 GLY GLY A . n 
A 1 516 LEU 516 510 510 LEU LEU A . n 
A 1 517 LYS 517 511 511 LYS LYS A . n 
A 1 518 GLU 518 512 512 GLU GLU A . n 
A 1 519 TYR 519 513 513 TYR TYR A . n 
A 1 520 ARG 520 514 514 ARG ARG A . n 
A 1 521 ASN 521 515 515 ASN ASN A . n 
A 1 522 GLN 522 516 516 GLN GLN A . n 
A 1 523 ILE 523 517 517 ILE ILE A . n 
A 1 524 SER 524 518 518 SER SER A . n 
A 1 525 GLU 525 519 519 GLU GLU A . n 
A 1 526 VAL 526 520 520 VAL VAL A . n 
A 1 527 SER 527 521 521 SER SER A . n 
A 1 528 ASN 528 522 522 ASN ASN A . n 
A 1 529 ASN 529 523 523 ASN ASN A . n 
A 1 530 ASN 530 524 524 ASN ASN A . n 
A 1 531 TYR 531 525 525 TYR TYR A . n 
A 1 532 LYS 532 526 526 LYS LYS A . n 
A 1 533 GLY 533 527 527 GLY GLY A . n 
A 1 534 CYS 534 528 528 CYS CYS A . n 
A 1 535 LEU 535 529 529 LEU LEU A . n 
A 1 536 LEU 536 530 530 LEU LEU A . n 
A 1 537 LYS 537 531 531 LYS LYS A . n 
A 1 538 GLN 538 532 532 GLN GLN A . n 
A 1 539 SER 539 533 533 SER SER A . n 
A 1 540 VAL 540 534 ?   ?   ?   A . n 
A 1 541 LYS 541 535 ?   ?   ?   A . n 
A 1 542 LYS 542 536 ?   ?   ?   A . n 
A 1 543 THR 543 537 ?   ?   ?   A . n 
A 1 544 ASN 544 538 ?   ?   ?   A . n 
A 1 545 LEU 545 539 ?   ?   ?   A . n 
A 1 546 ILE 546 540 ?   ?   ?   A . n 
A 1 547 GLU 547 541 ?   ?   ?   A . n 
A 1 548 SER 548 542 ?   ?   ?   A . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 FAD ? ? FAD ? ? 'SUBJECT OF INVESTIGATION' ? 
2 NAI ? ? NAI ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 NAI 1   601 601 NAI NAI A . 
C 3 FAD 1   602 602 FAD FAD A . 
D 4 HOH 1   701 201 HOH HOH A . 
D 4 HOH 2   702 77  HOH HOH A . 
D 4 HOH 3   703 166 HOH HOH A . 
D 4 HOH 4   704 217 HOH HOH A . 
D 4 HOH 5   705 59  HOH HOH A . 
D 4 HOH 6   706 212 HOH HOH A . 
D 4 HOH 7   707 8   HOH HOH A . 
D 4 HOH 8   708 190 HOH HOH A . 
D 4 HOH 9   709 117 HOH HOH A . 
D 4 HOH 10  710 161 HOH HOH A . 
D 4 HOH 11  711 165 HOH HOH A . 
D 4 HOH 12  712 15  HOH HOH A . 
D 4 HOH 13  713 134 HOH HOH A . 
D 4 HOH 14  714 31  HOH HOH A . 
D 4 HOH 15  715 182 HOH HOH A . 
D 4 HOH 16  716 172 HOH HOH A . 
D 4 HOH 17  717 167 HOH HOH A . 
D 4 HOH 18  718 183 HOH HOH A . 
D 4 HOH 19  719 7   HOH HOH A . 
D 4 HOH 20  720 1   HOH HOH A . 
D 4 HOH 21  721 115 HOH HOH A . 
D 4 HOH 22  722 85  HOH HOH A . 
D 4 HOH 23  723 141 HOH HOH A . 
D 4 HOH 24  724 132 HOH HOH A . 
D 4 HOH 25  725 76  HOH HOH A . 
D 4 HOH 26  726 109 HOH HOH A . 
D 4 HOH 27  727 196 HOH HOH A . 
D 4 HOH 28  728 120 HOH HOH A . 
D 4 HOH 29  729 131 HOH HOH A . 
D 4 HOH 30  730 105 HOH HOH A . 
D 4 HOH 31  731 29  HOH HOH A . 
D 4 HOH 32  732 56  HOH HOH A . 
D 4 HOH 33  733 147 HOH HOH A . 
D 4 HOH 34  734 126 HOH HOH A . 
D 4 HOH 35  735 39  HOH HOH A . 
D 4 HOH 36  736 74  HOH HOH A . 
D 4 HOH 37  737 157 HOH HOH A . 
D 4 HOH 38  738 142 HOH HOH A . 
D 4 HOH 39  739 2   HOH HOH A . 
D 4 HOH 40  740 163 HOH HOH A . 
D 4 HOH 41  741 43  HOH HOH A . 
D 4 HOH 42  742 149 HOH HOH A . 
D 4 HOH 43  743 49  HOH HOH A . 
D 4 HOH 44  744 136 HOH HOH A . 
D 4 HOH 45  745 58  HOH HOH A . 
D 4 HOH 46  746 146 HOH HOH A . 
D 4 HOH 47  747 112 HOH HOH A . 
D 4 HOH 48  748 41  HOH HOH A . 
D 4 HOH 49  749 154 HOH HOH A . 
D 4 HOH 50  750 153 HOH HOH A . 
D 4 HOH 51  751 86  HOH HOH A . 
D 4 HOH 52  752 113 HOH HOH A . 
D 4 HOH 53  753 61  HOH HOH A . 
D 4 HOH 54  754 94  HOH HOH A . 
D 4 HOH 55  755 20  HOH HOH A . 
D 4 HOH 56  756 53  HOH HOH A . 
D 4 HOH 57  757 44  HOH HOH A . 
D 4 HOH 58  758 151 HOH HOH A . 
D 4 HOH 59  759 38  HOH HOH A . 
D 4 HOH 60  760 144 HOH HOH A . 
D 4 HOH 61  761 81  HOH HOH A . 
D 4 HOH 62  762 171 HOH HOH A . 
D 4 HOH 63  763 138 HOH HOH A . 
D 4 HOH 64  764 89  HOH HOH A . 
D 4 HOH 65  765 45  HOH HOH A . 
D 4 HOH 66  766 42  HOH HOH A . 
D 4 HOH 67  767 33  HOH HOH A . 
D 4 HOH 68  768 186 HOH HOH A . 
D 4 HOH 69  769 3   HOH HOH A . 
D 4 HOH 70  770 70  HOH HOH A . 
D 4 HOH 71  771 128 HOH HOH A . 
D 4 HOH 72  772 17  HOH HOH A . 
D 4 HOH 73  773 4   HOH HOH A . 
D 4 HOH 74  774 111 HOH HOH A . 
D 4 HOH 75  775 210 HOH HOH A . 
D 4 HOH 76  776 160 HOH HOH A . 
D 4 HOH 77  777 13  HOH HOH A . 
D 4 HOH 78  778 176 HOH HOH A . 
D 4 HOH 79  779 137 HOH HOH A . 
D 4 HOH 80  780 23  HOH HOH A . 
D 4 HOH 81  781 48  HOH HOH A . 
D 4 HOH 82  782 96  HOH HOH A . 
D 4 HOH 83  783 66  HOH HOH A . 
D 4 HOH 84  784 14  HOH HOH A . 
D 4 HOH 85  785 11  HOH HOH A . 
D 4 HOH 86  786 188 HOH HOH A . 
D 4 HOH 87  787 50  HOH HOH A . 
D 4 HOH 88  788 214 HOH HOH A . 
D 4 HOH 89  789 133 HOH HOH A . 
D 4 HOH 90  790 84  HOH HOH A . 
D 4 HOH 91  791 101 HOH HOH A . 
D 4 HOH 92  792 82  HOH HOH A . 
D 4 HOH 93  793 80  HOH HOH A . 
D 4 HOH 94  794 123 HOH HOH A . 
D 4 HOH 95  795 40  HOH HOH A . 
D 4 HOH 96  796 181 HOH HOH A . 
D 4 HOH 97  797 114 HOH HOH A . 
D 4 HOH 98  798 148 HOH HOH A . 
D 4 HOH 99  799 118 HOH HOH A . 
D 4 HOH 100 800 150 HOH HOH A . 
D 4 HOH 101 801 24  HOH HOH A . 
D 4 HOH 102 802 99  HOH HOH A . 
D 4 HOH 103 803 22  HOH HOH A . 
D 4 HOH 104 804 79  HOH HOH A . 
D 4 HOH 105 805 91  HOH HOH A . 
D 4 HOH 106 806 5   HOH HOH A . 
D 4 HOH 107 807 72  HOH HOH A . 
D 4 HOH 108 808 90  HOH HOH A . 
D 4 HOH 109 809 143 HOH HOH A . 
D 4 HOH 110 810 93  HOH HOH A . 
D 4 HOH 111 811 68  HOH HOH A . 
D 4 HOH 112 812 108 HOH HOH A . 
D 4 HOH 113 813 97  HOH HOH A . 
D 4 HOH 114 814 69  HOH HOH A . 
D 4 HOH 115 815 110 HOH HOH A . 
D 4 HOH 116 816 64  HOH HOH A . 
D 4 HOH 117 817 36  HOH HOH A . 
D 4 HOH 118 818 124 HOH HOH A . 
D 4 HOH 119 819 130 HOH HOH A . 
D 4 HOH 120 820 216 HOH HOH A . 
D 4 HOH 121 821 12  HOH HOH A . 
D 4 HOH 122 822 215 HOH HOH A . 
D 4 HOH 123 823 16  HOH HOH A . 
D 4 HOH 124 824 103 HOH HOH A . 
D 4 HOH 125 825 47  HOH HOH A . 
D 4 HOH 126 826 129 HOH HOH A . 
D 4 HOH 127 827 65  HOH HOH A . 
D 4 HOH 128 828 78  HOH HOH A . 
D 4 HOH 129 829 62  HOH HOH A . 
D 4 HOH 130 830 37  HOH HOH A . 
D 4 HOH 131 831 51  HOH HOH A . 
D 4 HOH 132 832 152 HOH HOH A . 
D 4 HOH 133 833 52  HOH HOH A . 
D 4 HOH 134 834 27  HOH HOH A . 
D 4 HOH 135 835 19  HOH HOH A . 
D 4 HOH 136 836 139 HOH HOH A . 
D 4 HOH 137 837 71  HOH HOH A . 
D 4 HOH 138 838 18  HOH HOH A . 
D 4 HOH 139 839 10  HOH HOH A . 
D 4 HOH 140 840 106 HOH HOH A . 
D 4 HOH 141 841 63  HOH HOH A . 
D 4 HOH 142 842 87  HOH HOH A . 
D 4 HOH 143 843 98  HOH HOH A . 
D 4 HOH 144 844 46  HOH HOH A . 
D 4 HOH 145 845 207 HOH HOH A . 
D 4 HOH 146 846 6   HOH HOH A . 
D 4 HOH 147 847 30  HOH HOH A . 
D 4 HOH 148 848 57  HOH HOH A . 
D 4 HOH 149 849 104 HOH HOH A . 
D 4 HOH 150 850 102 HOH HOH A . 
D 4 HOH 151 851 155 HOH HOH A . 
D 4 HOH 152 852 175 HOH HOH A . 
D 4 HOH 153 853 67  HOH HOH A . 
D 4 HOH 154 854 83  HOH HOH A . 
D 4 HOH 155 855 60  HOH HOH A . 
D 4 HOH 156 856 95  HOH HOH A . 
D 4 HOH 157 857 9   HOH HOH A . 
D 4 HOH 158 858 25  HOH HOH A . 
D 4 HOH 159 859 156 HOH HOH A . 
D 4 HOH 160 860 127 HOH HOH A . 
D 4 HOH 161 861 170 HOH HOH A . 
D 4 HOH 162 862 100 HOH HOH A . 
D 4 HOH 163 863 174 HOH HOH A . 
D 4 HOH 164 864 122 HOH HOH A . 
D 4 HOH 165 865 213 HOH HOH A . 
D 4 HOH 166 866 32  HOH HOH A . 
D 4 HOH 167 867 28  HOH HOH A . 
D 4 HOH 168 868 206 HOH HOH A . 
D 4 HOH 169 869 121 HOH HOH A . 
D 4 HOH 170 870 35  HOH HOH A . 
D 4 HOH 171 871 179 HOH HOH A . 
D 4 HOH 172 872 75  HOH HOH A . 
D 4 HOH 173 873 21  HOH HOH A . 
D 4 HOH 174 874 55  HOH HOH A . 
D 4 HOH 175 875 209 HOH HOH A . 
D 4 HOH 176 876 26  HOH HOH A . 
D 4 HOH 177 877 168 HOH HOH A . 
D 4 HOH 178 878 169 HOH HOH A . 
D 4 HOH 179 879 107 HOH HOH A . 
D 4 HOH 180 880 145 HOH HOH A . 
D 4 HOH 181 881 192 HOH HOH A . 
D 4 HOH 182 882 189 HOH HOH A . 
D 4 HOH 183 883 34  HOH HOH A . 
D 4 HOH 184 884 180 HOH HOH A . 
D 4 HOH 185 885 140 HOH HOH A . 
D 4 HOH 186 886 185 HOH HOH A . 
D 4 HOH 187 887 208 HOH HOH A . 
D 4 HOH 188 888 193 HOH HOH A . 
D 4 HOH 189 889 194 HOH HOH A . 
D 4 HOH 190 890 116 HOH HOH A . 
D 4 HOH 191 891 187 HOH HOH A . 
D 4 HOH 192 892 177 HOH HOH A . 
D 4 HOH 193 893 203 HOH HOH A . 
D 4 HOH 194 894 178 HOH HOH A . 
D 4 HOH 195 895 199 HOH HOH A . 
D 4 HOH 196 896 211 HOH HOH A . 
D 4 HOH 197 897 191 HOH HOH A . 
D 4 HOH 198 898 205 HOH HOH A . 
D 4 HOH 199 899 195 HOH HOH A . 
D 4 HOH 200 900 92  HOH HOH A . 
D 4 HOH 201 901 73  HOH HOH A . 
D 4 HOH 202 902 119 HOH HOH A . 
D 4 HOH 203 903 88  HOH HOH A . 
D 4 HOH 204 904 164 HOH HOH A . 
D 4 HOH 205 905 173 HOH HOH A . 
D 4 HOH 206 906 198 HOH HOH A . 
D 4 HOH 207 907 135 HOH HOH A . 
D 4 HOH 208 908 125 HOH HOH A . 
D 4 HOH 209 909 204 HOH HOH A . 
D 4 HOH 210 910 200 HOH HOH A . 
D 4 HOH 211 911 162 HOH HOH A . 
D 4 HOH 212 912 54  HOH HOH A . 
D 4 HOH 213 913 202 HOH HOH A . 
D 4 HOH 214 914 159 HOH HOH A . 
D 4 HOH 215 915 197 HOH HOH A . 
D 4 HOH 216 916 184 HOH HOH A . 
# 
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 ? ? ? 1.19.2_4158 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   96.855 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8YU4 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     52.920 
_cell.length_a_esd                 ? 
_cell.length_b                     53.230 
_cell.length_b_esd                 ? 
_cell.length_c                     101.490 
_cell.length_c_esd                 ? 
_cell.volume                       283846.669 
_cell.volume_esd                   ? 
_cell.Z_PDB                        2 
_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                         8YU4 
_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                   8YU4 
_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             2.40 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          48.80 
_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          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              8.75 
_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    
;0.1 M Tris (base)-Bicine pH 8.75; 20% (v/v) PEG 500*MME; 10% (w/v) PEG 20000; 0.09 M Halogens (Sodium fluoride; Sodium bromide; Sodium iodide).
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 S 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         2023-09-15 
_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   0.97918 
_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                        'SSRF BEAMLINE BL02U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97918 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL02U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          37.04 
_reflns.entry_id                                       8YU4 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.02 
_reflns.d_resolution_low                               44.46 
_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                                     36825 
_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                           99.27 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          12.03 
_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                                   0.995 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.1405 
_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                                    2.02 
_reflns_shell.d_res_low                                     2.092 
_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                             3633 
_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                                  0.627 
_reflns_shell.pdbx_CC_star                                  0.878 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.392 
_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                               44.36 
_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                                 8YU4 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.02 
_refine.ls_d_res_low                             44.46 
_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                     36818 
_refine.ls_number_reflns_R_free                  1754 
_refine.ls_number_reflns_R_work                  35064 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.28 
_refine.ls_percent_reflns_R_free                 4.76 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2199 
_refine.ls_R_factor_R_free                       0.2595 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2180 
_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                          1.34 
_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                      AlphaFold 
_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             1.1100 
_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                 27.5524 
_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                            0.2588 
_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                       2.02 
_refine_hist.d_res_low                        44.46 
_refine_hist.number_atoms_solvent             216 
_refine_hist.number_atoms_total               4456 
_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        4143 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         97 
_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' ? 0.0019  ? 4343 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.5416  ? 5897 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0421  ? 635  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0026  ? 745  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 15.0985 ? 596  ? 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' 2.02 2.07  . . 111 2678 98.52 . . . . 0.3182 . . . . . . . . . . . 0.3358 
'X-RAY DIFFRACTION' 2.07 2.14  . . 141 2644 98.62 . . . . 0.2834 . . . . . . . . . . . 0.2954 
'X-RAY DIFFRACTION' 2.14 2.20  . . 125 2725 99.23 . . . . 0.2826 . . . . . . . . . . . 0.3374 
'X-RAY DIFFRACTION' 2.20 2.28  . . 158 2618 99.28 . . . . 0.2711 . . . . . . . . . . . 0.3441 
'X-RAY DIFFRACTION' 2.28 2.37  . . 138 2664 99.19 . . . . 0.2641 . . . . . . . . . . . 0.3172 
'X-RAY DIFFRACTION' 2.37 2.48  . . 161 2651 99.19 . . . . 0.2542 . . . . . . . . . . . 0.2959 
'X-RAY DIFFRACTION' 2.48 2.61  . . 122 2700 99.54 . . . . 0.2468 . . . . . . . . . . . 0.2819 
'X-RAY DIFFRACTION' 2.61 2.78  . . 160 2703 99.58 . . . . 0.2426 . . . . . . . . . . . 0.2773 
'X-RAY DIFFRACTION' 2.78 2.99  . . 132 2686 99.40 . . . . 0.2366 . . . . . . . . . . . 0.2576 
'X-RAY DIFFRACTION' 2.99 3.29  . . 134 2722 99.79 . . . . 0.2339 . . . . . . . . . . . 0.3003 
'X-RAY DIFFRACTION' 3.29 3.77  . . 132 2719 99.69 . . . . 0.2079 . . . . . . . . . . . 0.2767 
'X-RAY DIFFRACTION' 3.77 4.75  . . 98  2777 99.83 . . . . 0.1763 . . . . . . . . . . . 0.1780 
'X-RAY DIFFRACTION' 4.75 44.46 . . 142 2777 98.85 . . . . 0.1834 . . . . . . . . . . . 0.2205 
# 
_struct.entry_id                     8YU4 
_struct.title                        'Structure of cyclohexanone monooxygenase mutant from Acinetobacter calcoaceticus' 
_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        8YU4 
_struct_keywords.text            'Complex, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A0A8XFY0_ACICA 
_struct_ref.pdbx_db_accession          A0A0A8XFY0 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;TQKMDFDAIIIGAGFGGLYSLKKLRDDFNLKVRAFDRATEVGGTWFWNQYPGALSDSETHLYCYSWDKELLQEMEIKRKY
ISQPDVLAYLKRVADKHDLRKDIQFETGIRSAYFDEENSFWNVTTENDEKFTARFLITALGLLAAPNLPKIKGIETFKGE
LHHTSRWPKDVTFSGKRVGVIGTGSTGVQVITAIASQVKHLTVFQRSAQYSVPIGNVVMSETDVAKIKENYDQIWENVWN
SALGFGLNESTLPTMSVSAEERDKIFEKAWQEGGGFRFMFETFGDIAVDETANIEAQNFIKKKISEIVKDPFVAKKLTPT
DLYAKRPLCDSGYYEIFNRDNVSLEDVKANPIVEIKEDCVVTADGVEHKLDMLICATGFDAVDGNYIRMDIRGKDGISIK
DHWKDGPNSYLGMMVSNFPNMFMVLGPNGPFTNLPPSIETQVRWIADLIGYAEDHQINQIEATKDAVDNWTNTCSDIANK
TLFAKAESWIFGANVPGKKNTVYFYMGGLKEYRNQISEVSNNNYKGCLLKQSVKKTNLIES
;
_struct_ref.pdbx_align_begin           2 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8YU4 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 8 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 548 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             A0A0A8XFY0 
_struct_ref_seq.db_align_beg                  2 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  542 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       2 
_struct_ref_seq.pdbx_auth_seq_align_end       542 
# 
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 8YU4 MET A 1   ? UNP A0A0A8XFY0 ?   ?   'initiating methionine' -5  1  
1 8YU4 HIS A 2   ? UNP A0A0A8XFY0 ?   ?   'expression tag'        -4  2  
1 8YU4 HIS A 3   ? UNP A0A0A8XFY0 ?   ?   'expression tag'        -3  3  
1 8YU4 HIS A 4   ? UNP A0A0A8XFY0 ?   ?   'expression tag'        -2  4  
1 8YU4 HIS A 5   ? UNP A0A0A8XFY0 ?   ?   'expression tag'        -1  5  
1 8YU4 HIS A 6   ? UNP A0A0A8XFY0 ?   ?   'expression tag'        0   6  
1 8YU4 HIS A 7   ? UNP A0A0A8XFY0 ?   ?   'expression tag'        1   7  
1 8YU4 PRO A 149 ? UNP A0A0A8XFY0 LEU 143 'engineered mutation'   143 8  
1 8YU4 SER A 151 ? UNP A0A0A8XFY0 ALA 145 'engineered mutation'   145 9  
1 8YU4 SER A 152 ? UNP A0A0A8XFY0 ALA 146 'engineered mutation'   146 10 
1 8YU4 TRP A 155 ? UNP A0A0A8XFY0 LEU 149 'engineered mutation'   149 11 
1 8YU4 ILE A 157 ? UNP A0A0A8XFY0 LYS 151 'engineered mutation'   151 12 
1 8YU4 TYR A 252 ? UNP A0A0A8XFY0 PHE 246 'engineered mutation'   246 13 
1 8YU4 CYS A 332 ? UNP A0A0A8XFY0 LYS 326 'engineered mutation'   326 14 
1 8YU4 SER A 392 ? UNP A0A0A8XFY0 ASN 386 'engineered mutation'   386 15 
1 8YU4 LYS A 394 ? UNP A0A0A8XFY0 ILE 388 'engineered mutation'   388 16 
1 8YU4 ILE A 396 ? UNP A0A0A8XFY0 MET 390 'engineered mutation'   390 17 
1 8YU4 PHE A 432 ? UNP A0A0A8XFY0 LEU 426 'engineered mutation'   426 18 
1 8YU4 LEU A 438 ? UNP A0A0A8XFY0 PHE 432 'engineered mutation'   432 19 
1 8YU4 ALA A 439 ? UNP A0A0A8XFY0 THR 433 'engineered mutation'   433 20 
1 8YU4 SER A 441 ? UNP A0A0A8XFY0 LEU 435 'engineered mutation'   435 21 
1 8YU4 ILE A 444 ? UNP A0A0A8XFY0 SER 438 'engineered mutation'   438 22 
1 8YU4 LYS A 494 ? UNP A0A0A8XFY0 GLU 488 'engineered mutation'   488 23 
1 8YU4 CYS A 495 ? UNP A0A0A8XFY0 SER 489 'engineered mutation'   489 24 
1 8YU4 ARG A 496 ? UNP A0A0A8XFY0 TRP 490 'engineered mutation'   490 25 
1 8YU4 LEU A 511 ? UNP A0A0A8XFY0 PHE 505 'engineered mutation'   505 26 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 2680  ? 
1 MORE         -10   ? 
1 'SSA (A^2)'  21590 ? 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
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 GLY A 21  ? ASP A 34  ? GLY A 15  ASP A 28  1 ? 14 
HELX_P HELX_P2  AA2 GLY A 50  ? ASN A 55  ? GLY A 44  ASN A 49  1 ? 6  
HELX_P HELX_P3  AA3 ASP A 74  ? MET A 81  ? ASP A 68  MET A 75  1 ? 8  
HELX_P HELX_P4  AA4 SER A 89  ? HIS A 104 ? SER A 83  HIS A 98  1 ? 16 
HELX_P HELX_P5  AA5 LEU A 106 ? LYS A 108 ? LEU A 100 LYS A 102 5 ? 3  
HELX_P HELX_P6  AA6 GLY A 160 ? PHE A 164 ? GLY A 154 PHE A 158 5 ? 5  
HELX_P HELX_P7  AA7 SER A 172 ? TRP A 174 ? SER A 166 TRP A 168 5 ? 3  
HELX_P HELX_P8  AA8 GLY A 191 ? ALA A 202 ? GLY A 185 ALA A 196 1 ? 12 
HELX_P HELX_P9  AA9 SER A 227 ? ASN A 237 ? SER A 221 ASN A 231 1 ? 11 
HELX_P HELX_P10 AB1 ASN A 237 ? ASN A 247 ? ASN A 231 ASN A 241 1 ? 11 
HELX_P HELX_P11 AB2 PRO A 260 ? VAL A 264 ? PRO A 254 VAL A 258 5 ? 5  
HELX_P HELX_P12 AB3 SER A 265 ? GLY A 280 ? SER A 259 GLY A 274 1 ? 16 
HELX_P HELX_P13 AB4 GLY A 281 ? GLU A 288 ? GLY A 275 GLU A 282 1 ? 8  
HELX_P HELX_P14 AB5 ASP A 296 ? VAL A 315 ? ASP A 290 VAL A 309 1 ? 20 
HELX_P HELX_P15 AB6 ASP A 317 ? THR A 325 ? ASP A 311 THR A 319 1 ? 9  
HELX_P HELX_P16 AB7 GLY A 339 ? PHE A 344 ? GLY A 333 PHE A 338 1 ? 6  
HELX_P HELX_P17 AB8 VAL A 389 ? ARG A 395 ? VAL A 383 ARG A 389 1 ? 7  
HELX_P HELX_P18 AB9 GLY A 400 ? ILE A 404 ? GLY A 394 ILE A 398 5 ? 5  
HELX_P HELX_P19 AC1 SER A 405 ? TRP A 410 ? SER A 399 TRP A 404 1 ? 6  
HELX_P HELX_P20 AC2 ASN A 440 ? HIS A 462 ? ASN A 434 HIS A 456 1 ? 23 
HELX_P HELX_P21 AC3 THR A 470 ? ASN A 486 ? THR A 464 ASN A 480 1 ? 17 
HELX_P HELX_P22 AC4 LYS A 487 ? LYS A 492 ? LYS A 481 LYS A 486 5 ? 6  
HELX_P HELX_P23 AC5 GLY A 515 ? ASN A 529 ? GLY A 509 ASN A 523 1 ? 15 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 5 ? 
AA3 ? 5 ? 
AA4 ? 2 ? 
AA5 ? 3 ? 
AA6 ? 2 ? 
AA7 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA3 1 2 ? parallel      
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA3 4 5 ? parallel      
AA4 1 2 ? parallel      
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA6 1 2 ? parallel      
AA7 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ILE A 110 ? GLN A 111 ? ILE A 104 GLN A 105 
AA1 2 VAL A 39  ? PHE A 42  ? VAL A 33  PHE A 36  
AA1 3 PHE A 13  ? ILE A 18  ? PHE A 7   ILE A 12  
AA1 4 LYS A 137 ? THR A 145 ? LYS A 131 THR A 139 
AA1 5 PHE A 127 ? THR A 132 ? PHE A 121 THR A 126 
AA1 6 ILE A 116 ? ASP A 122 ? ILE A 110 ASP A 116 
AA1 7 ASP A 397 ? ARG A 399 ? ASP A 391 ARG A 393 
AA2 1 ILE A 110 ? GLN A 111 ? ILE A 104 GLN A 105 
AA2 2 VAL A 39  ? PHE A 42  ? VAL A 33  PHE A 36  
AA2 3 PHE A 13  ? ILE A 18  ? PHE A 7   ILE A 12  
AA2 4 LYS A 137 ? THR A 145 ? LYS A 131 THR A 139 
AA2 5 MET A 428 ? MET A 430 ? MET A 422 MET A 424 
AA3 1 GLU A 167 ? HIS A 170 ? GLU A 161 HIS A 164 
AA3 2 MET A 379 ? CYS A 382 ? MET A 373 CYS A 376 
AA3 3 ARG A 184 ? ILE A 188 ? ARG A 178 ILE A 182 
AA3 4 HIS A 207 ? GLN A 212 ? HIS A 201 GLN A 206 
AA3 5 VAL A 349 ? ASP A 353 ? VAL A 343 ASP A 347 
AA4 1 SER A 218 ? PRO A 220 ? SER A 212 PRO A 214 
AA4 2 LEU A 335 ? ASP A 337 ? LEU A 329 ASP A 331 
AA5 1 ILE A 359 ? ILE A 362 ? ILE A 353 ILE A 356 
AA5 2 CYS A 366 ? THR A 369 ? CYS A 360 THR A 363 
AA5 3 GLU A 374 ? LYS A 376 ? GLU A 368 LYS A 370 
AA6 1 GLY A 436 ? PRO A 437 ? GLY A 430 PRO A 431 
AA6 2 LEU A 511 ? TYR A 512 ? LEU A 505 TYR A 506 
AA7 1 ILE A 464 ? ALA A 469 ? ILE A 458 ALA A 463 
AA7 2 CYS A 534 ? GLN A 538 ? CYS A 528 GLN A 532 
# 
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 O GLN A 111 ? O GLN A 105 N ALA A 41  ? N ALA A 35  
AA1 2 3 O ARG A 40  ? O ARG A 34  N ILE A 17  ? N ILE A 11  
AA1 3 4 N ILE A 16  ? N ILE A 10  O ILE A 144 ? O ILE A 138 
AA1 4 5 O ALA A 140 ? O ALA A 134 N TRP A 128 ? N TRP A 122 
AA1 5 6 O ASN A 129 ? O ASN A 123 N TYR A 120 ? N TYR A 114 
AA1 6 7 N ALA A 119 ? N ALA A 113 O ASP A 397 ? O ASP A 391 
AA2 1 2 O GLN A 111 ? O GLN A 105 N ALA A 41  ? N ALA A 35  
AA2 2 3 O ARG A 40  ? O ARG A 34  N ILE A 17  ? N ILE A 11  
AA2 3 4 N ILE A 16  ? N ILE A 10  O ILE A 144 ? O ILE A 138 
AA2 4 5 N LEU A 143 ? N LEU A 137 O PHE A 429 ? O PHE A 423 
AA3 1 2 N GLU A 167 ? N GLU A 161 O LEU A 380 ? O LEU A 374 
AA3 2 3 O ILE A 381 ? O ILE A 375 N GLY A 186 ? N GLY A 180 
AA3 3 4 N VAL A 187 ? N VAL A 181 O PHE A 211 ? O PHE A 205 
AA3 4 5 N VAL A 210 ? N VAL A 204 O GLU A 352 ? O GLU A 346 
AA4 1 2 N VAL A 219 ? N VAL A 213 O LEU A 335 ? O LEU A 329 
AA5 1 2 N GLU A 361 ? N GLU A 355 O VAL A 368 ? O VAL A 362 
AA5 2 3 N VAL A 367 ? N VAL A 361 O HIS A 375 ? O HIS A 369 
AA6 1 2 N GLY A 436 ? N GLY A 430 O TYR A 512 ? O TYR A 506 
AA7 1 2 N GLU A 468 ? N GLU A 462 O LEU A 535 ? O LEU A 529 
# 
_pdbx_entry_details.entry_id                   8YU4 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
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 MET A 5   ? ? 67.57   131.85  
2  1 ILE A 77  ? ? -116.87 79.99   
3  1 ALA A 140 ? ? -115.24 71.04   
4  1 SER A 145 ? ? -105.52 -142.10 
5  1 CYS A 326 ? ? -78.01  -103.37 
6  1 GLU A 355 ? ? -173.95 149.89  
7  1 LYS A 357 ? ? -113.82 -163.03 
8  1 ASP A 359 ? ? -140.66 12.71   
9  1 ALA A 377 ? ? -99.45  54.10   
10 1 ASP A 396 ? ? 49.56   -6.82   
11 1 ALA A 487 ? ? -75.99  -156.50 
12 1 ASN A 523 ? ? -88.44  40.63   
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z       
2 -x,y+1/2,-z 
# 
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 -5  ? A MET 1   
2  1 Y 1 A HIS -4  ? A HIS 2   
3  1 Y 1 A HIS -3  ? A HIS 3   
4  1 Y 1 A HIS -2  ? A HIS 4   
5  1 Y 1 A HIS -1  ? A HIS 5   
6  1 Y 1 A HIS 0   ? A HIS 6   
7  1 Y 1 A HIS 1   ? A HIS 7   
8  1 Y 1 A CYS 489 ? A CYS 495 
9  1 Y 1 A ARG 490 ? A ARG 496 
10 1 Y 1 A ILE 491 ? A ILE 497 
11 1 Y 1 A PHE 492 ? A PHE 498 
12 1 Y 1 A GLY 493 ? A GLY 499 
13 1 Y 1 A ALA 494 ? A ALA 500 
14 1 Y 1 A ASN 495 ? A ASN 501 
15 1 Y 1 A VAL 496 ? A VAL 502 
16 1 Y 1 A PRO 497 ? A PRO 503 
17 1 Y 1 A GLY 498 ? A GLY 504 
18 1 Y 1 A LYS 499 ? A LYS 505 
19 1 Y 1 A LYS 500 ? A LYS 506 
20 1 Y 1 A VAL 534 ? A VAL 540 
21 1 Y 1 A LYS 535 ? A LYS 541 
22 1 Y 1 A LYS 536 ? A LYS 542 
23 1 Y 1 A THR 537 ? A THR 543 
24 1 Y 1 A ASN 538 ? A ASN 544 
25 1 Y 1 A LEU 539 ? A LEU 545 
26 1 Y 1 A ILE 540 ? A ILE 546 
27 1 Y 1 A GLU 541 ? A GLU 547 
28 1 Y 1 A SER 542 ? A SER 548 
# 
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 
ALA N      N N N 1   
ALA CA     C N S 2   
ALA C      C N N 3   
ALA O      O N N 4   
ALA CB     C N N 5   
ALA OXT    O N N 6   
ALA H      H N N 7   
ALA H2     H N N 8   
ALA HA     H N N 9   
ALA HB1    H N N 10  
ALA HB2    H N N 11  
ALA HB3    H N N 12  
ALA HXT    H N N 13  
ARG N      N N N 14  
ARG CA     C N S 15  
ARG C      C N N 16  
ARG O      O N N 17  
ARG CB     C N N 18  
ARG CG     C N N 19  
ARG CD     C N N 20  
ARG NE     N N N 21  
ARG CZ     C N N 22  
ARG NH1    N N N 23  
ARG NH2    N N N 24  
ARG OXT    O N N 25  
ARG H      H N N 26  
ARG H2     H N N 27  
ARG HA     H N N 28  
ARG HB2    H N N 29  
ARG HB3    H N N 30  
ARG HG2    H N N 31  
ARG HG3    H N N 32  
ARG HD2    H N N 33  
ARG HD3    H N N 34  
ARG HE     H N N 35  
ARG HH11   H N N 36  
ARG HH12   H N N 37  
ARG HH21   H N N 38  
ARG HH22   H N N 39  
ARG HXT    H N N 40  
ASN N      N N N 41  
ASN CA     C N S 42  
ASN C      C N N 43  
ASN O      O N N 44  
ASN CB     C N N 45  
ASN CG     C N N 46  
ASN OD1    O N N 47  
ASN ND2    N N N 48  
ASN OXT    O N N 49  
ASN H      H N N 50  
ASN H2     H N N 51  
ASN HA     H N N 52  
ASN HB2    H N N 53  
ASN HB3    H N N 54  
ASN HD21   H N N 55  
ASN HD22   H N N 56  
ASN HXT    H N N 57  
ASP N      N N N 58  
ASP CA     C N S 59  
ASP C      C N N 60  
ASP O      O N N 61  
ASP CB     C N N 62  
ASP CG     C N N 63  
ASP OD1    O N N 64  
ASP OD2    O N N 65  
ASP OXT    O N N 66  
ASP H      H N N 67  
ASP H2     H N N 68  
ASP HA     H N N 69  
ASP HB2    H N N 70  
ASP HB3    H N N 71  
ASP HD2    H N N 72  
ASP HXT    H N N 73  
CYS N      N N N 74  
CYS CA     C N R 75  
CYS C      C N N 76  
CYS O      O N N 77  
CYS CB     C N N 78  
CYS SG     S N N 79  
CYS OXT    O N N 80  
CYS H      H N N 81  
CYS H2     H N N 82  
CYS HA     H N N 83  
CYS HB2    H N N 84  
CYS HB3    H N N 85  
CYS HG     H N N 86  
CYS HXT    H N N 87  
FAD PA     P N R 88  
FAD O1A    O N N 89  
FAD O2A    O N N 90  
FAD O5B    O N N 91  
FAD C5B    C N N 92  
FAD C4B    C N R 93  
FAD O4B    O N N 94  
FAD C3B    C N S 95  
FAD O3B    O N N 96  
FAD C2B    C N R 97  
FAD O2B    O N N 98  
FAD C1B    C N R 99  
FAD N9A    N Y N 100 
FAD C8A    C Y N 101 
FAD N7A    N Y N 102 
FAD C5A    C Y N 103 
FAD C6A    C Y N 104 
FAD N6A    N N N 105 
FAD N1A    N Y N 106 
FAD C2A    C Y N 107 
FAD N3A    N Y N 108 
FAD C4A    C Y N 109 
FAD N1     N N N 110 
FAD C2     C N N 111 
FAD O2     O N N 112 
FAD N3     N N N 113 
FAD C4     C N N 114 
FAD O4     O N N 115 
FAD C4X    C N N 116 
FAD N5     N N N 117 
FAD C5X    C Y N 118 
FAD C6     C Y N 119 
FAD C7     C Y N 120 
FAD C7M    C N N 121 
FAD C8     C Y N 122 
FAD C8M    C N N 123 
FAD C9     C Y N 124 
FAD C9A    C Y N 125 
FAD N10    N N N 126 
FAD C10    C N N 127 
FAD "C1'"  C N N 128 
FAD "C2'"  C N S 129 
FAD "O2'"  O N N 130 
FAD "C3'"  C N S 131 
FAD "O3'"  O N N 132 
FAD "C4'"  C N R 133 
FAD "O4'"  O N N 134 
FAD "C5'"  C N N 135 
FAD "O5'"  O N N 136 
FAD P      P N R 137 
FAD O1P    O N N 138 
FAD O2P    O N N 139 
FAD O3P    O N N 140 
FAD HOA2   H N N 141 
FAD H51A   H N N 142 
FAD H52A   H N N 143 
FAD H4B    H N N 144 
FAD H3B    H N N 145 
FAD HO3A   H N N 146 
FAD H2B    H N N 147 
FAD HO2A   H N N 148 
FAD H1B    H N N 149 
FAD H8A    H N N 150 
FAD H61A   H N N 151 
FAD H62A   H N N 152 
FAD H2A    H N N 153 
FAD HN3    H N N 154 
FAD H6     H N N 155 
FAD HM71   H N N 156 
FAD HM72   H N N 157 
FAD HM73   H N N 158 
FAD HM81   H N N 159 
FAD HM82   H N N 160 
FAD HM83   H N N 161 
FAD H9     H N N 162 
FAD "H1'1" H N N 163 
FAD "H1'2" H N N 164 
FAD "H2'"  H N N 165 
FAD "HO2'" H N N 166 
FAD "H3'"  H N N 167 
FAD "HO3'" H N N 168 
FAD "H4'"  H N N 169 
FAD "HO4'" H N N 170 
FAD "H5'1" H N N 171 
FAD "H5'2" H N N 172 
FAD HOP2   H N N 173 
GLN N      N N N 174 
GLN CA     C N S 175 
GLN C      C N N 176 
GLN O      O N N 177 
GLN CB     C N N 178 
GLN CG     C N N 179 
GLN CD     C N N 180 
GLN OE1    O N N 181 
GLN NE2    N N N 182 
GLN OXT    O N N 183 
GLN H      H N N 184 
GLN H2     H N N 185 
GLN HA     H N N 186 
GLN HB2    H N N 187 
GLN HB3    H N N 188 
GLN HG2    H N N 189 
GLN HG3    H N N 190 
GLN HE21   H N N 191 
GLN HE22   H N N 192 
GLN HXT    H N N 193 
GLU N      N N N 194 
GLU CA     C N S 195 
GLU C      C N N 196 
GLU O      O N N 197 
GLU CB     C N N 198 
GLU CG     C N N 199 
GLU CD     C N N 200 
GLU OE1    O N N 201 
GLU OE2    O N N 202 
GLU OXT    O N N 203 
GLU H      H N N 204 
GLU H2     H N N 205 
GLU HA     H N N 206 
GLU HB2    H N N 207 
GLU HB3    H N N 208 
GLU HG2    H N N 209 
GLU HG3    H N N 210 
GLU HE2    H N N 211 
GLU HXT    H N N 212 
GLY N      N N N 213 
GLY CA     C N N 214 
GLY C      C N N 215 
GLY O      O N N 216 
GLY OXT    O N N 217 
GLY H      H N N 218 
GLY H2     H N N 219 
GLY HA2    H N N 220 
GLY HA3    H N N 221 
GLY HXT    H N N 222 
HIS N      N N N 223 
HIS CA     C N S 224 
HIS C      C N N 225 
HIS O      O N N 226 
HIS CB     C N N 227 
HIS CG     C Y N 228 
HIS ND1    N Y N 229 
HIS CD2    C Y N 230 
HIS CE1    C Y N 231 
HIS NE2    N Y N 232 
HIS OXT    O N N 233 
HIS H      H N N 234 
HIS H2     H N N 235 
HIS HA     H N N 236 
HIS HB2    H N N 237 
HIS HB3    H N N 238 
HIS HD1    H N N 239 
HIS HD2    H N N 240 
HIS HE1    H N N 241 
HIS HE2    H N N 242 
HIS HXT    H N N 243 
HOH O      O N N 244 
HOH H1     H N N 245 
HOH H2     H N N 246 
ILE N      N N N 247 
ILE CA     C N S 248 
ILE C      C N N 249 
ILE O      O N N 250 
ILE CB     C N S 251 
ILE CG1    C N N 252 
ILE CG2    C N N 253 
ILE CD1    C N N 254 
ILE OXT    O N N 255 
ILE H      H N N 256 
ILE H2     H N N 257 
ILE HA     H N N 258 
ILE HB     H N N 259 
ILE HG12   H N N 260 
ILE HG13   H N N 261 
ILE HG21   H N N 262 
ILE HG22   H N N 263 
ILE HG23   H N N 264 
ILE HD11   H N N 265 
ILE HD12   H N N 266 
ILE HD13   H N N 267 
ILE HXT    H N N 268 
LEU N      N N N 269 
LEU CA     C N S 270 
LEU C      C N N 271 
LEU O      O N N 272 
LEU CB     C N N 273 
LEU CG     C N N 274 
LEU CD1    C N N 275 
LEU CD2    C N N 276 
LEU OXT    O N N 277 
LEU H      H N N 278 
LEU H2     H N N 279 
LEU HA     H N N 280 
LEU HB2    H N N 281 
LEU HB3    H N N 282 
LEU HG     H N N 283 
LEU HD11   H N N 284 
LEU HD12   H N N 285 
LEU HD13   H N N 286 
LEU HD21   H N N 287 
LEU HD22   H N N 288 
LEU HD23   H N N 289 
LEU HXT    H N N 290 
LYS N      N N N 291 
LYS CA     C N S 292 
LYS C      C N N 293 
LYS O      O N N 294 
LYS CB     C N N 295 
LYS CG     C N N 296 
LYS CD     C N N 297 
LYS CE     C N N 298 
LYS NZ     N N N 299 
LYS OXT    O N N 300 
LYS H      H N N 301 
LYS H2     H N N 302 
LYS HA     H N N 303 
LYS HB2    H N N 304 
LYS HB3    H N N 305 
LYS HG2    H N N 306 
LYS HG3    H N N 307 
LYS HD2    H N N 308 
LYS HD3    H N N 309 
LYS HE2    H N N 310 
LYS HE3    H N N 311 
LYS HZ1    H N N 312 
LYS HZ2    H N N 313 
LYS HZ3    H N N 314 
LYS HXT    H N N 315 
MET N      N N N 316 
MET CA     C N S 317 
MET C      C N N 318 
MET O      O N N 319 
MET CB     C N N 320 
MET CG     C N N 321 
MET SD     S N N 322 
MET CE     C N N 323 
MET OXT    O N N 324 
MET H      H N N 325 
MET H2     H N N 326 
MET HA     H N N 327 
MET HB2    H N N 328 
MET HB3    H N N 329 
MET HG2    H N N 330 
MET HG3    H N N 331 
MET HE1    H N N 332 
MET HE2    H N N 333 
MET HE3    H N N 334 
MET HXT    H N N 335 
NAI PA     P N S 336 
NAI O1A    O N N 337 
NAI O2A    O N N 338 
NAI O5B    O N N 339 
NAI C5B    C N N 340 
NAI C4B    C N R 341 
NAI O4B    O N N 342 
NAI C3B    C N S 343 
NAI O3B    O N N 344 
NAI C2B    C N R 345 
NAI O2B    O N N 346 
NAI C1B    C N R 347 
NAI N9A    N Y N 348 
NAI C8A    C Y N 349 
NAI N7A    N Y N 350 
NAI C5A    C Y N 351 
NAI C6A    C Y N 352 
NAI N6A    N N N 353 
NAI N1A    N Y N 354 
NAI C2A    C Y N 355 
NAI N3A    N Y N 356 
NAI C4A    C Y N 357 
NAI O3     O N N 358 
NAI PN     P N S 359 
NAI O1N    O N N 360 
NAI O2N    O N N 361 
NAI O5D    O N N 362 
NAI C5D    C N N 363 
NAI C4D    C N R 364 
NAI O4D    O N N 365 
NAI C3D    C N S 366 
NAI O3D    O N N 367 
NAI C2D    C N R 368 
NAI O2D    O N N 369 
NAI C1D    C N R 370 
NAI N1N    N N N 371 
NAI C2N    C N N 372 
NAI C3N    C N N 373 
NAI C7N    C N N 374 
NAI O7N    O N N 375 
NAI N7N    N N N 376 
NAI C4N    C N N 377 
NAI C5N    C N N 378 
NAI C6N    C N N 379 
NAI HOA2   H N N 380 
NAI H51A   H N N 381 
NAI H52A   H N N 382 
NAI H4B    H N N 383 
NAI H3B    H N N 384 
NAI HO3A   H N N 385 
NAI H2B    H N N 386 
NAI HO2A   H N N 387 
NAI H1B    H N N 388 
NAI H8A    H N N 389 
NAI H61A   H N N 390 
NAI H62A   H N N 391 
NAI H2A    H N N 392 
NAI HO1N   H N N 393 
NAI H51N   H N N 394 
NAI H52N   H N N 395 
NAI H4D    H N N 396 
NAI H3D    H N N 397 
NAI HO3N   H N N 398 
NAI H2D    H N N 399 
NAI HO2N   H N N 400 
NAI H1D    H N N 401 
NAI H2N    H N N 402 
NAI H71N   H N N 403 
NAI H72N   H N N 404 
NAI H4N    H N N 405 
NAI H42N   H N N 406 
NAI H5N    H N N 407 
NAI H6N    H N N 408 
PHE N      N N N 409 
PHE CA     C N S 410 
PHE C      C N N 411 
PHE O      O N N 412 
PHE CB     C N N 413 
PHE CG     C Y N 414 
PHE CD1    C Y N 415 
PHE CD2    C Y N 416 
PHE CE1    C Y N 417 
PHE CE2    C Y N 418 
PHE CZ     C Y N 419 
PHE OXT    O N N 420 
PHE H      H N N 421 
PHE H2     H N N 422 
PHE HA     H N N 423 
PHE HB2    H N N 424 
PHE HB3    H N N 425 
PHE HD1    H N N 426 
PHE HD2    H N N 427 
PHE HE1    H N N 428 
PHE HE2    H N N 429 
PHE HZ     H N N 430 
PHE HXT    H N N 431 
PRO N      N N N 432 
PRO CA     C N S 433 
PRO C      C N N 434 
PRO O      O N N 435 
PRO CB     C N N 436 
PRO CG     C N N 437 
PRO CD     C N N 438 
PRO OXT    O N N 439 
PRO H      H N N 440 
PRO HA     H N N 441 
PRO HB2    H N N 442 
PRO HB3    H N N 443 
PRO HG2    H N N 444 
PRO HG3    H N N 445 
PRO HD2    H N N 446 
PRO HD3    H N N 447 
PRO HXT    H N N 448 
SER N      N N N 449 
SER CA     C N S 450 
SER C      C N N 451 
SER O      O N N 452 
SER CB     C N N 453 
SER OG     O N N 454 
SER OXT    O N N 455 
SER H      H N N 456 
SER H2     H N N 457 
SER HA     H N N 458 
SER HB2    H N N 459 
SER HB3    H N N 460 
SER HG     H N N 461 
SER HXT    H N N 462 
THR N      N N N 463 
THR CA     C N S 464 
THR C      C N N 465 
THR O      O N N 466 
THR CB     C N R 467 
THR OG1    O N N 468 
THR CG2    C N N 469 
THR OXT    O N N 470 
THR H      H N N 471 
THR H2     H N N 472 
THR HA     H N N 473 
THR HB     H N N 474 
THR HG1    H N N 475 
THR HG21   H N N 476 
THR HG22   H N N 477 
THR HG23   H N N 478 
THR HXT    H N N 479 
TRP N      N N N 480 
TRP CA     C N S 481 
TRP C      C N N 482 
TRP O      O N N 483 
TRP CB     C N N 484 
TRP CG     C Y N 485 
TRP CD1    C Y N 486 
TRP CD2    C Y N 487 
TRP NE1    N Y N 488 
TRP CE2    C Y N 489 
TRP CE3    C Y N 490 
TRP CZ2    C Y N 491 
TRP CZ3    C Y N 492 
TRP CH2    C Y N 493 
TRP OXT    O N N 494 
TRP H      H N N 495 
TRP H2     H N N 496 
TRP HA     H N N 497 
TRP HB2    H N N 498 
TRP HB3    H N N 499 
TRP HD1    H N N 500 
TRP HE1    H N N 501 
TRP HE3    H N N 502 
TRP HZ2    H N N 503 
TRP HZ3    H N N 504 
TRP HH2    H N N 505 
TRP HXT    H N N 506 
TYR N      N N N 507 
TYR CA     C N S 508 
TYR C      C N N 509 
TYR O      O N N 510 
TYR CB     C N N 511 
TYR CG     C Y N 512 
TYR CD1    C Y N 513 
TYR CD2    C Y N 514 
TYR CE1    C Y N 515 
TYR CE2    C Y N 516 
TYR CZ     C Y N 517 
TYR OH     O N N 518 
TYR OXT    O N N 519 
TYR H      H N N 520 
TYR H2     H N N 521 
TYR HA     H N N 522 
TYR HB2    H N N 523 
TYR HB3    H N N 524 
TYR HD1    H N N 525 
TYR HD2    H N N 526 
TYR HE1    H N N 527 
TYR HE2    H N N 528 
TYR HH     H N N 529 
TYR HXT    H N N 530 
VAL N      N N N 531 
VAL CA     C N S 532 
VAL C      C N N 533 
VAL O      O N N 534 
VAL CB     C N N 535 
VAL CG1    C N N 536 
VAL CG2    C N N 537 
VAL OXT    O N N 538 
VAL H      H N N 539 
VAL H2     H N N 540 
VAL HA     H N N 541 
VAL HB     H N N 542 
VAL HG11   H N N 543 
VAL HG12   H N N 544 
VAL HG13   H N N 545 
VAL HG21   H N N 546 
VAL HG22   H N N 547 
VAL HG23   H N N 548 
VAL HXT    H N N 549 
# 
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 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ARG N     CA     sing N N 13  
ARG N     H      sing N N 14  
ARG N     H2     sing N N 15  
ARG CA    C      sing N N 16  
ARG CA    CB     sing N N 17  
ARG CA    HA     sing N N 18  
ARG C     O      doub N N 19  
ARG C     OXT    sing N N 20  
ARG CB    CG     sing N N 21  
ARG CB    HB2    sing N N 22  
ARG CB    HB3    sing N N 23  
ARG CG    CD     sing N N 24  
ARG CG    HG2    sing N N 25  
ARG CG    HG3    sing N N 26  
ARG CD    NE     sing N N 27  
ARG CD    HD2    sing N N 28  
ARG CD    HD3    sing N N 29  
ARG NE    CZ     sing N N 30  
ARG NE    HE     sing N N 31  
ARG CZ    NH1    sing N N 32  
ARG CZ    NH2    doub N N 33  
ARG NH1   HH11   sing N N 34  
ARG NH1   HH12   sing N N 35  
ARG NH2   HH21   sing N N 36  
ARG NH2   HH22   sing N N 37  
ARG OXT   HXT    sing N N 38  
ASN N     CA     sing N N 39  
ASN N     H      sing N N 40  
ASN N     H2     sing N N 41  
ASN CA    C      sing N N 42  
ASN CA    CB     sing N N 43  
ASN CA    HA     sing N N 44  
ASN C     O      doub N N 45  
ASN C     OXT    sing N N 46  
ASN CB    CG     sing N N 47  
ASN CB    HB2    sing N N 48  
ASN CB    HB3    sing N N 49  
ASN CG    OD1    doub N N 50  
ASN CG    ND2    sing N N 51  
ASN ND2   HD21   sing N N 52  
ASN ND2   HD22   sing N N 53  
ASN OXT   HXT    sing N N 54  
ASP N     CA     sing N N 55  
ASP N     H      sing N N 56  
ASP N     H2     sing N N 57  
ASP CA    C      sing N N 58  
ASP CA    CB     sing N N 59  
ASP CA    HA     sing N N 60  
ASP C     O      doub N N 61  
ASP C     OXT    sing N N 62  
ASP CB    CG     sing N N 63  
ASP CB    HB2    sing N N 64  
ASP CB    HB3    sing N N 65  
ASP CG    OD1    doub N N 66  
ASP CG    OD2    sing N N 67  
ASP OD2   HD2    sing N N 68  
ASP OXT   HXT    sing N N 69  
CYS N     CA     sing N N 70  
CYS N     H      sing N N 71  
CYS N     H2     sing N N 72  
CYS CA    C      sing N N 73  
CYS CA    CB     sing N N 74  
CYS CA    HA     sing N N 75  
CYS C     O      doub N N 76  
CYS C     OXT    sing N N 77  
CYS CB    SG     sing N N 78  
CYS CB    HB2    sing N N 79  
CYS CB    HB3    sing N N 80  
CYS SG    HG     sing N N 81  
CYS OXT   HXT    sing N N 82  
FAD PA    O1A    doub N N 83  
FAD PA    O2A    sing N N 84  
FAD PA    O5B    sing N N 85  
FAD PA    O3P    sing N N 86  
FAD O2A   HOA2   sing N N 87  
FAD O5B   C5B    sing N N 88  
FAD C5B   C4B    sing N N 89  
FAD C5B   H51A   sing N N 90  
FAD C5B   H52A   sing N N 91  
FAD C4B   O4B    sing N N 92  
FAD C4B   C3B    sing N N 93  
FAD C4B   H4B    sing N N 94  
FAD O4B   C1B    sing N N 95  
FAD C3B   O3B    sing N N 96  
FAD C3B   C2B    sing N N 97  
FAD C3B   H3B    sing N N 98  
FAD O3B   HO3A   sing N N 99  
FAD C2B   O2B    sing N N 100 
FAD C2B   C1B    sing N N 101 
FAD C2B   H2B    sing N N 102 
FAD O2B   HO2A   sing N N 103 
FAD C1B   N9A    sing N N 104 
FAD C1B   H1B    sing N N 105 
FAD N9A   C8A    sing Y N 106 
FAD N9A   C4A    sing Y N 107 
FAD C8A   N7A    doub Y N 108 
FAD C8A   H8A    sing N N 109 
FAD N7A   C5A    sing Y N 110 
FAD C5A   C6A    sing Y N 111 
FAD C5A   C4A    doub Y N 112 
FAD C6A   N6A    sing N N 113 
FAD C6A   N1A    doub Y N 114 
FAD N6A   H61A   sing N N 115 
FAD N6A   H62A   sing N N 116 
FAD N1A   C2A    sing Y N 117 
FAD C2A   N3A    doub Y N 118 
FAD C2A   H2A    sing N N 119 
FAD N3A   C4A    sing Y N 120 
FAD N1    C2     sing N N 121 
FAD N1    C10    doub N N 122 
FAD C2    O2     doub N N 123 
FAD C2    N3     sing N N 124 
FAD N3    C4     sing N N 125 
FAD N3    HN3    sing N N 126 
FAD C4    O4     doub N N 127 
FAD C4    C4X    sing N N 128 
FAD C4X   N5     doub N N 129 
FAD C4X   C10    sing N N 130 
FAD N5    C5X    sing N N 131 
FAD C5X   C6     doub Y N 132 
FAD C5X   C9A    sing Y N 133 
FAD C6    C7     sing Y N 134 
FAD C6    H6     sing N N 135 
FAD C7    C7M    sing N N 136 
FAD C7    C8     doub Y N 137 
FAD C7M   HM71   sing N N 138 
FAD C7M   HM72   sing N N 139 
FAD C7M   HM73   sing N N 140 
FAD C8    C8M    sing N N 141 
FAD C8    C9     sing Y N 142 
FAD C8M   HM81   sing N N 143 
FAD C8M   HM82   sing N N 144 
FAD C8M   HM83   sing N N 145 
FAD C9    C9A    doub Y N 146 
FAD C9    H9     sing N N 147 
FAD C9A   N10    sing N N 148 
FAD N10   C10    sing N N 149 
FAD N10   "C1'"  sing N N 150 
FAD "C1'" "C2'"  sing N N 151 
FAD "C1'" "H1'1" sing N N 152 
FAD "C1'" "H1'2" sing N N 153 
FAD "C2'" "O2'"  sing N N 154 
FAD "C2'" "C3'"  sing N N 155 
FAD "C2'" "H2'"  sing N N 156 
FAD "O2'" "HO2'" sing N N 157 
FAD "C3'" "O3'"  sing N N 158 
FAD "C3'" "C4'"  sing N N 159 
FAD "C3'" "H3'"  sing N N 160 
FAD "O3'" "HO3'" sing N N 161 
FAD "C4'" "O4'"  sing N N 162 
FAD "C4'" "C5'"  sing N N 163 
FAD "C4'" "H4'"  sing N N 164 
FAD "O4'" "HO4'" sing N N 165 
FAD "C5'" "O5'"  sing N N 166 
FAD "C5'" "H5'1" sing N N 167 
FAD "C5'" "H5'2" sing N N 168 
FAD "O5'" P      sing N N 169 
FAD P     O1P    doub N N 170 
FAD P     O2P    sing N N 171 
FAD P     O3P    sing N N 172 
FAD O2P   HOP2   sing N N 173 
GLN N     CA     sing N N 174 
GLN N     H      sing N N 175 
GLN N     H2     sing N N 176 
GLN CA    C      sing N N 177 
GLN CA    CB     sing N N 178 
GLN CA    HA     sing N N 179 
GLN C     O      doub N N 180 
GLN C     OXT    sing N N 181 
GLN CB    CG     sing N N 182 
GLN CB    HB2    sing N N 183 
GLN CB    HB3    sing N N 184 
GLN CG    CD     sing N N 185 
GLN CG    HG2    sing N N 186 
GLN CG    HG3    sing N N 187 
GLN CD    OE1    doub N N 188 
GLN CD    NE2    sing N N 189 
GLN NE2   HE21   sing N N 190 
GLN NE2   HE22   sing N N 191 
GLN OXT   HXT    sing N N 192 
GLU N     CA     sing N N 193 
GLU N     H      sing N N 194 
GLU N     H2     sing N N 195 
GLU CA    C      sing N N 196 
GLU CA    CB     sing N N 197 
GLU CA    HA     sing N N 198 
GLU C     O      doub N N 199 
GLU C     OXT    sing N N 200 
GLU CB    CG     sing N N 201 
GLU CB    HB2    sing N N 202 
GLU CB    HB3    sing N N 203 
GLU CG    CD     sing N N 204 
GLU CG    HG2    sing N N 205 
GLU CG    HG3    sing N N 206 
GLU CD    OE1    doub N N 207 
GLU CD    OE2    sing N N 208 
GLU OE2   HE2    sing N N 209 
GLU OXT   HXT    sing N N 210 
GLY N     CA     sing N N 211 
GLY N     H      sing N N 212 
GLY N     H2     sing N N 213 
GLY CA    C      sing N N 214 
GLY CA    HA2    sing N N 215 
GLY CA    HA3    sing N N 216 
GLY C     O      doub N N 217 
GLY C     OXT    sing N N 218 
GLY OXT   HXT    sing N N 219 
HIS N     CA     sing N N 220 
HIS N     H      sing N N 221 
HIS N     H2     sing N N 222 
HIS CA    C      sing N N 223 
HIS CA    CB     sing N N 224 
HIS CA    HA     sing N N 225 
HIS C     O      doub N N 226 
HIS C     OXT    sing N N 227 
HIS CB    CG     sing N N 228 
HIS CB    HB2    sing N N 229 
HIS CB    HB3    sing N N 230 
HIS CG    ND1    sing Y N 231 
HIS CG    CD2    doub Y N 232 
HIS ND1   CE1    doub Y N 233 
HIS ND1   HD1    sing N N 234 
HIS CD2   NE2    sing Y N 235 
HIS CD2   HD2    sing N N 236 
HIS CE1   NE2    sing Y N 237 
HIS CE1   HE1    sing N N 238 
HIS NE2   HE2    sing N N 239 
HIS OXT   HXT    sing N N 240 
HOH O     H1     sing N N 241 
HOH O     H2     sing N N 242 
ILE N     CA     sing N N 243 
ILE N     H      sing N N 244 
ILE N     H2     sing N N 245 
ILE CA    C      sing N N 246 
ILE CA    CB     sing N N 247 
ILE CA    HA     sing N N 248 
ILE C     O      doub N N 249 
ILE C     OXT    sing N N 250 
ILE CB    CG1    sing N N 251 
ILE CB    CG2    sing N N 252 
ILE CB    HB     sing N N 253 
ILE CG1   CD1    sing N N 254 
ILE CG1   HG12   sing N N 255 
ILE CG1   HG13   sing N N 256 
ILE CG2   HG21   sing N N 257 
ILE CG2   HG22   sing N N 258 
ILE CG2   HG23   sing N N 259 
ILE CD1   HD11   sing N N 260 
ILE CD1   HD12   sing N N 261 
ILE CD1   HD13   sing N N 262 
ILE OXT   HXT    sing N N 263 
LEU N     CA     sing N N 264 
LEU N     H      sing N N 265 
LEU N     H2     sing N N 266 
LEU CA    C      sing N N 267 
LEU CA    CB     sing N N 268 
LEU CA    HA     sing N N 269 
LEU C     O      doub N N 270 
LEU C     OXT    sing N N 271 
LEU CB    CG     sing N N 272 
LEU CB    HB2    sing N N 273 
LEU CB    HB3    sing N N 274 
LEU CG    CD1    sing N N 275 
LEU CG    CD2    sing N N 276 
LEU CG    HG     sing N N 277 
LEU CD1   HD11   sing N N 278 
LEU CD1   HD12   sing N N 279 
LEU CD1   HD13   sing N N 280 
LEU CD2   HD21   sing N N 281 
LEU CD2   HD22   sing N N 282 
LEU CD2   HD23   sing N N 283 
LEU OXT   HXT    sing N N 284 
LYS N     CA     sing N N 285 
LYS N     H      sing N N 286 
LYS N     H2     sing N N 287 
LYS CA    C      sing N N 288 
LYS CA    CB     sing N N 289 
LYS CA    HA     sing N N 290 
LYS C     O      doub N N 291 
LYS C     OXT    sing N N 292 
LYS CB    CG     sing N N 293 
LYS CB    HB2    sing N N 294 
LYS CB    HB3    sing N N 295 
LYS CG    CD     sing N N 296 
LYS CG    HG2    sing N N 297 
LYS CG    HG3    sing N N 298 
LYS CD    CE     sing N N 299 
LYS CD    HD2    sing N N 300 
LYS CD    HD3    sing N N 301 
LYS CE    NZ     sing N N 302 
LYS CE    HE2    sing N N 303 
LYS CE    HE3    sing N N 304 
LYS NZ    HZ1    sing N N 305 
LYS NZ    HZ2    sing N N 306 
LYS NZ    HZ3    sing N N 307 
LYS OXT   HXT    sing N N 308 
MET N     CA     sing N N 309 
MET N     H      sing N N 310 
MET N     H2     sing N N 311 
MET CA    C      sing N N 312 
MET CA    CB     sing N N 313 
MET CA    HA     sing N N 314 
MET C     O      doub N N 315 
MET C     OXT    sing N N 316 
MET CB    CG     sing N N 317 
MET CB    HB2    sing N N 318 
MET CB    HB3    sing N N 319 
MET CG    SD     sing N N 320 
MET CG    HG2    sing N N 321 
MET CG    HG3    sing N N 322 
MET SD    CE     sing N N 323 
MET CE    HE1    sing N N 324 
MET CE    HE2    sing N N 325 
MET CE    HE3    sing N N 326 
MET OXT   HXT    sing N N 327 
NAI PA    O1A    doub N N 328 
NAI PA    O2A    sing N N 329 
NAI PA    O5B    sing N N 330 
NAI PA    O3     sing N N 331 
NAI O2A   HOA2   sing N N 332 
NAI O5B   C5B    sing N N 333 
NAI C5B   C4B    sing N N 334 
NAI C5B   H51A   sing N N 335 
NAI C5B   H52A   sing N N 336 
NAI C4B   O4B    sing N N 337 
NAI C4B   C3B    sing N N 338 
NAI C4B   H4B    sing N N 339 
NAI O4B   C1B    sing N N 340 
NAI C3B   O3B    sing N N 341 
NAI C3B   C2B    sing N N 342 
NAI C3B   H3B    sing N N 343 
NAI O3B   HO3A   sing N N 344 
NAI C2B   O2B    sing N N 345 
NAI C2B   C1B    sing N N 346 
NAI C2B   H2B    sing N N 347 
NAI O2B   HO2A   sing N N 348 
NAI C1B   N9A    sing N N 349 
NAI C1B   H1B    sing N N 350 
NAI N9A   C8A    sing Y N 351 
NAI N9A   C4A    sing Y N 352 
NAI C8A   N7A    doub Y N 353 
NAI C8A   H8A    sing N N 354 
NAI N7A   C5A    sing Y N 355 
NAI C5A   C6A    sing Y N 356 
NAI C5A   C4A    doub Y N 357 
NAI C6A   N6A    sing N N 358 
NAI C6A   N1A    doub Y N 359 
NAI N6A   H61A   sing N N 360 
NAI N6A   H62A   sing N N 361 
NAI N1A   C2A    sing Y N 362 
NAI C2A   N3A    doub Y N 363 
NAI C2A   H2A    sing N N 364 
NAI N3A   C4A    sing Y N 365 
NAI O3    PN     sing N N 366 
NAI PN    O1N    sing N N 367 
NAI PN    O2N    doub N N 368 
NAI PN    O5D    sing N N 369 
NAI O1N   HO1N   sing N N 370 
NAI O5D   C5D    sing N N 371 
NAI C5D   C4D    sing N N 372 
NAI C5D   H51N   sing N N 373 
NAI C5D   H52N   sing N N 374 
NAI C4D   O4D    sing N N 375 
NAI C4D   C3D    sing N N 376 
NAI C4D   H4D    sing N N 377 
NAI O4D   C1D    sing N N 378 
NAI C3D   O3D    sing N N 379 
NAI C3D   C2D    sing N N 380 
NAI C3D   H3D    sing N N 381 
NAI O3D   HO3N   sing N N 382 
NAI C2D   O2D    sing N N 383 
NAI C2D   C1D    sing N N 384 
NAI C2D   H2D    sing N N 385 
NAI O2D   HO2N   sing N N 386 
NAI C1D   N1N    sing N N 387 
NAI C1D   H1D    sing N N 388 
NAI N1N   C2N    sing N N 389 
NAI N1N   C6N    sing N N 390 
NAI C2N   C3N    doub N N 391 
NAI C2N   H2N    sing N N 392 
NAI C3N   C7N    sing N N 393 
NAI C3N   C4N    sing N N 394 
NAI C7N   O7N    doub N N 395 
NAI C7N   N7N    sing N N 396 
NAI N7N   H71N   sing N N 397 
NAI N7N   H72N   sing N N 398 
NAI C4N   C5N    sing N N 399 
NAI C4N   H4N    sing N N 400 
NAI C4N   H42N   sing N N 401 
NAI C5N   C6N    doub N N 402 
NAI C5N   H5N    sing N N 403 
NAI C6N   H6N    sing N N 404 
PHE N     CA     sing N N 405 
PHE N     H      sing N N 406 
PHE N     H2     sing N N 407 
PHE CA    C      sing N N 408 
PHE CA    CB     sing N N 409 
PHE CA    HA     sing N N 410 
PHE C     O      doub N N 411 
PHE C     OXT    sing N N 412 
PHE CB    CG     sing N N 413 
PHE CB    HB2    sing N N 414 
PHE CB    HB3    sing N N 415 
PHE CG    CD1    doub Y N 416 
PHE CG    CD2    sing Y N 417 
PHE CD1   CE1    sing Y N 418 
PHE CD1   HD1    sing N N 419 
PHE CD2   CE2    doub Y N 420 
PHE CD2   HD2    sing N N 421 
PHE CE1   CZ     doub Y N 422 
PHE CE1   HE1    sing N N 423 
PHE CE2   CZ     sing Y N 424 
PHE CE2   HE2    sing N N 425 
PHE CZ    HZ     sing N N 426 
PHE OXT   HXT    sing N N 427 
PRO N     CA     sing N N 428 
PRO N     CD     sing N N 429 
PRO N     H      sing N N 430 
PRO CA    C      sing N N 431 
PRO CA    CB     sing N N 432 
PRO CA    HA     sing N N 433 
PRO C     O      doub N N 434 
PRO C     OXT    sing N N 435 
PRO CB    CG     sing N N 436 
PRO CB    HB2    sing N N 437 
PRO CB    HB3    sing N N 438 
PRO CG    CD     sing N N 439 
PRO CG    HG2    sing N N 440 
PRO CG    HG3    sing N N 441 
PRO CD    HD2    sing N N 442 
PRO CD    HD3    sing N N 443 
PRO OXT   HXT    sing N N 444 
SER N     CA     sing N N 445 
SER N     H      sing N N 446 
SER N     H2     sing N N 447 
SER CA    C      sing N N 448 
SER CA    CB     sing N N 449 
SER CA    HA     sing N N 450 
SER C     O      doub N N 451 
SER C     OXT    sing N N 452 
SER CB    OG     sing N N 453 
SER CB    HB2    sing N N 454 
SER CB    HB3    sing N N 455 
SER OG    HG     sing N N 456 
SER OXT   HXT    sing N N 457 
THR N     CA     sing N N 458 
THR N     H      sing N N 459 
THR N     H2     sing N N 460 
THR CA    C      sing N N 461 
THR CA    CB     sing N N 462 
THR CA    HA     sing N N 463 
THR C     O      doub N N 464 
THR C     OXT    sing N N 465 
THR CB    OG1    sing N N 466 
THR CB    CG2    sing N N 467 
THR CB    HB     sing N N 468 
THR OG1   HG1    sing N N 469 
THR CG2   HG21   sing N N 470 
THR CG2   HG22   sing N N 471 
THR CG2   HG23   sing N N 472 
THR OXT   HXT    sing N N 473 
TRP N     CA     sing N N 474 
TRP N     H      sing N N 475 
TRP N     H2     sing N N 476 
TRP CA    C      sing N N 477 
TRP CA    CB     sing N N 478 
TRP CA    HA     sing N N 479 
TRP C     O      doub N N 480 
TRP C     OXT    sing N N 481 
TRP CB    CG     sing N N 482 
TRP CB    HB2    sing N N 483 
TRP CB    HB3    sing N N 484 
TRP CG    CD1    doub Y N 485 
TRP CG    CD2    sing Y N 486 
TRP CD1   NE1    sing Y N 487 
TRP CD1   HD1    sing N N 488 
TRP CD2   CE2    doub Y N 489 
TRP CD2   CE3    sing Y N 490 
TRP NE1   CE2    sing Y N 491 
TRP NE1   HE1    sing N N 492 
TRP CE2   CZ2    sing Y N 493 
TRP CE3   CZ3    doub Y N 494 
TRP CE3   HE3    sing N N 495 
TRP CZ2   CH2    doub Y N 496 
TRP CZ2   HZ2    sing N N 497 
TRP CZ3   CH2    sing Y N 498 
TRP CZ3   HZ3    sing N N 499 
TRP CH2   HH2    sing N N 500 
TRP OXT   HXT    sing N N 501 
TYR N     CA     sing N N 502 
TYR N     H      sing N N 503 
TYR N     H2     sing N N 504 
TYR CA    C      sing N N 505 
TYR CA    CB     sing N N 506 
TYR CA    HA     sing N N 507 
TYR C     O      doub N N 508 
TYR C     OXT    sing N N 509 
TYR CB    CG     sing N N 510 
TYR CB    HB2    sing N N 511 
TYR CB    HB3    sing N N 512 
TYR CG    CD1    doub Y N 513 
TYR CG    CD2    sing Y N 514 
TYR CD1   CE1    sing Y N 515 
TYR CD1   HD1    sing N N 516 
TYR CD2   CE2    doub Y N 517 
TYR CD2   HD2    sing N N 518 
TYR CE1   CZ     doub Y N 519 
TYR CE1   HE1    sing N N 520 
TYR CE2   CZ     sing Y N 521 
TYR CE2   HE2    sing N N 522 
TYR CZ    OH     sing N N 523 
TYR OH    HH     sing N N 524 
TYR OXT   HXT    sing N N 525 
VAL N     CA     sing N N 526 
VAL N     H      sing N N 527 
VAL N     H2     sing N N 528 
VAL CA    C      sing N N 529 
VAL CA    CB     sing N N 530 
VAL CA    HA     sing N N 531 
VAL C     O      doub N N 532 
VAL C     OXT    sing N N 533 
VAL CB    CG1    sing N N 534 
VAL CB    CG2    sing N N 535 
VAL CB    HB     sing N N 536 
VAL CG1   HG11   sing N N 537 
VAL CG1   HG12   sing N N 538 
VAL CG1   HG13   sing N N 539 
VAL CG2   HG21   sing N N 540 
VAL CG2   HG22   sing N N 541 
VAL CG2   HG23   sing N N 542 
VAL OXT   HXT    sing N N 543 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           21922804 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_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                    8YU4 
_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]   0.018896 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002272 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.018786 
_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]   0.009924 
_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 ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
P ? ? 9.51135 5.44231 ? ? 1.42069  35.72801 ? ? 0.0 
;2-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     . THR A 1 8   ? 18.61089  -20.95404 50.60433  1.000 111.97847 ? 2   THR A N     1 
ATOM   2    C CA    . THR A 1 8   ? 17.46028  -21.27492 49.76783  1.000 109.97043 ? 2   THR A CA    1 
ATOM   3    C C     . THR A 1 8   ? 17.48336  -20.51490 48.44609  1.000 107.26426 ? 2   THR A C     1 
ATOM   4    O O     . THR A 1 8   ? 18.13592  -20.93809 47.49187  1.000 105.62569 ? 2   THR A O     1 
ATOM   5    C CB    . THR A 1 8   ? 16.13313  -20.96718 50.48852  1.000 111.70674 ? 2   THR A CB    1 
ATOM   6    O OG1   . THR A 1 8   ? 16.16011  -19.62676 50.99586  1.000 112.83927 ? 2   THR A OG1   1 
ATOM   7    C CG2   . THR A 1 8   ? 15.90467  -21.94147 51.63339  1.000 113.30508 ? 2   THR A CG2   1 
ATOM   8    N N     . GLN A 1 9   ? 16.76938  -19.38733 48.41329  1.000 104.01035 ? 3   GLN A N     1 
ATOM   9    C CA    . GLN A 1 9   ? 16.52420  -18.61897 47.19654  1.000 97.31293  ? 3   GLN A CA    1 
ATOM   10   C C     . GLN A 1 9   ? 17.78985  -18.36669 46.38467  1.000 95.71385  ? 3   GLN A C     1 
ATOM   11   O O     . GLN A 1 9   ? 18.67609  -17.61915 46.80995  1.000 96.69250  ? 3   GLN A O     1 
ATOM   12   C CB    . GLN A 1 9   ? 15.85322  -17.28693 47.54713  1.000 95.08584  ? 3   GLN A CB    1 
ATOM   13   C CG    . GLN A 1 9   ? 16.40861  -16.60720 48.79386  1.000 99.49393  ? 3   GLN A CG    1 
ATOM   14   C CD    . GLN A 1 9   ? 17.38937  -15.49554 48.46626  1.000 95.81677  ? 3   GLN A CD    1 
ATOM   15   O OE1   . GLN A 1 9   ? 17.36238  -14.93020 47.37291  1.000 89.73787  ? 3   GLN A OE1   1 
ATOM   16   N NE2   . GLN A 1 9   ? 18.26688  -15.18223 49.41239  1.000 93.01855  ? 3   GLN A NE2   1 
ATOM   17   N N     . LYS A 1 10  ? 17.88364  -19.00245 45.21608  1.000 92.42327  ? 4   LYS A N     1 
ATOM   18   C CA    . LYS A 1 10  ? 18.98146  -18.73197 44.29429  1.000 87.52688  ? 4   LYS A CA    1 
ATOM   19   C C     . LYS A 1 10  ? 18.66735  -17.50951 43.43902  1.000 82.31317  ? 4   LYS A C     1 
ATOM   20   O O     . LYS A 1 10  ? 19.42146  -16.53044 43.43719  1.000 81.85708  ? 4   LYS A O     1 
ATOM   21   C CB    . LYS A 1 10  ? 19.24598  -19.96763 43.42346  1.000 85.63309  ? 4   LYS A CB    1 
ATOM   22   C CG    . LYS A 1 10  ? 20.40219  -19.85303 42.42352  1.000 81.74945  ? 4   LYS A CG    1 
ATOM   23   C CD    . LYS A 1 10  ? 19.95935  -19.28245 41.07605  1.000 77.90616  ? 4   LYS A CD    1 
ATOM   24   C CE    . LYS A 1 10  ? 18.65337  -19.91011 40.60582  1.000 74.07927  ? 4   LYS A CE    1 
ATOM   25   N NZ    . LYS A 1 10  ? 18.56493  -19.99725 39.12345  1.000 73.74551  ? 4   LYS A NZ    1 
ATOM   26   N N     . MET A 1 11  ? 17.55062  -17.56274 42.70547  1.000 75.15930  ? 5   MET A N     1 
ATOM   27   C CA    . MET A 1 11  ? 17.03859  -16.47323 41.87736  1.000 66.29812  ? 5   MET A CA    1 
ATOM   28   C C     . MET A 1 11  ? 17.93741  -16.17932 40.68167  1.000 64.22738  ? 5   MET A C     1 
ATOM   29   O O     . MET A 1 11  ? 19.15777  -16.04999 40.82121  1.000 63.55364  ? 5   MET A O     1 
ATOM   30   C CB    . MET A 1 11  ? 16.83752  -15.20625 42.71312  1.000 66.19496  ? 5   MET A CB    1 
ATOM   31   C CG    . MET A 1 11  ? 15.68821  -15.30010 43.70019  1.000 72.10128  ? 5   MET A CG    1 
ATOM   32   S SD    . MET A 1 11  ? 14.80300  -13.74139 43.87616  1.000 67.17177  ? 5   MET A SD    1 
ATOM   33   C CE    . MET A 1 11  ? 16.16607  -12.58091 43.84327  1.000 57.18857  ? 5   MET A CE    1 
ATOM   34   N N     . ASP A 1 12  ? 17.33486  -16.07128 39.49598  1.000 57.07877  ? 6   ASP A N     1 
ATOM   35   C CA    . ASP A 1 12  ? 18.10171  -15.72719 38.30473  1.000 54.61379  ? 6   ASP A CA    1 
ATOM   36   C C     . ASP A 1 12  ? 18.38721  -14.23228 38.23657  1.000 50.94968  ? 6   ASP A C     1 
ATOM   37   O O     . ASP A 1 12  ? 19.49395  -13.82752 37.86611  1.000 45.67812  ? 6   ASP A O     1 
ATOM   38   C CB    . ASP A 1 12  ? 17.35972  -16.18015 37.04637  1.000 57.84801  ? 6   ASP A CB    1 
ATOM   39   C CG    . ASP A 1 12  ? 17.03772  -17.66059 37.05832  1.000 57.81119  ? 6   ASP A CG    1 
ATOM   40   O OD1   . ASP A 1 12  ? 17.96426  -18.47372 36.85840  1.000 61.54145  ? 6   ASP A OD1   1 
ATOM   41   O OD2   . ASP A 1 12  ? 15.85693  -18.01141 37.26073  1.000 55.68114  ? 6   ASP A OD2   1 
ATOM   42   N N     . PHE A 1 13  ? 17.40821  -13.39991 38.58656  1.000 47.50035  ? 7   PHE A N     1 
ATOM   43   C CA    . PHE A 1 13  ? 17.55777  -11.95496 38.50245  1.000 48.80680  ? 7   PHE A CA    1 
ATOM   44   C C     . PHE A 1 13  ? 16.88919  -11.30061 39.70172  1.000 43.67515  ? 7   PHE A C     1 
ATOM   45   O O     . PHE A 1 13  ? 16.10122  -11.92180 40.41831  1.000 46.15851  ? 7   PHE A O     1 
ATOM   46   C CB    . PHE A 1 13  ? 16.95465  -11.39584 37.20513  1.000 42.51874  ? 7   PHE A CB    1 
ATOM   47   C CG    . PHE A 1 13  ? 17.36752  -12.14348 35.97245  1.000 43.47685  ? 7   PHE A CG    1 
ATOM   48   C CD1   . PHE A 1 13  ? 18.59573  -11.90509 35.38061  1.000 45.40374  ? 7   PHE A CD1   1 
ATOM   49   C CD2   . PHE A 1 13  ? 16.52775  -13.08819 35.40654  1.000 47.17606  ? 7   PHE A CD2   1 
ATOM   50   C CE1   . PHE A 1 13  ? 18.97897  -12.59390 34.24662  1.000 44.53447  ? 7   PHE A CE1   1 
ATOM   51   C CE2   . PHE A 1 13  ? 16.90520  -13.78033 34.27279  1.000 45.47089  ? 7   PHE A CE2   1 
ATOM   52   C CZ    . PHE A 1 13  ? 18.13272  -13.53418 33.69287  1.000 43.91093  ? 7   PHE A CZ    1 
ATOM   53   N N     . ASP A 1 14  ? 17.22354  -10.02738 39.91622  1.000 46.37297  ? 8   ASP A N     1 
ATOM   54   C CA    . ASP A 1 14  ? 16.50663  -9.23002  40.90281  1.000 40.28832  ? 8   ASP A CA    1 
ATOM   55   C C     . ASP A 1 14  ? 15.17376  -8.73687  40.35869  1.000 40.51301  ? 8   ASP A C     1 
ATOM   56   O O     . ASP A 1 14  ? 14.20909  -8.60070  41.11880  1.000 42.09527  ? 8   ASP A O     1 
ATOM   57   C CB    . ASP A 1 14  ? 17.36302  -8.04306  41.34882  1.000 43.98222  ? 8   ASP A CB    1 
ATOM   58   C CG    . ASP A 1 14  ? 18.62484  -8.47282  42.06995  1.000 46.31349  ? 8   ASP A CG    1 
ATOM   59   O OD1   . ASP A 1 14  ? 18.51382  -9.09442  43.14748  1.000 52.20762  ? 8   ASP A OD1   1 
ATOM   60   O OD2   . ASP A 1 14  ? 19.72790  -8.19070  41.55696  1.000 50.34058  ? 8   ASP A OD2   1 
ATOM   61   N N     . ALA A 1 15  ? 15.09983  -8.47601  39.05554  1.000 43.76214  ? 9   ALA A N     1 
ATOM   62   C CA    . ALA A 1 15  ? 13.87562  -8.00131  38.43211  1.000 41.48754  ? 9   ALA A CA    1 
ATOM   63   C C     . ALA A 1 15  ? 13.82259  -8.48788  36.99191  1.000 35.85874  ? 9   ALA A C     1 
ATOM   64   O O     . ALA A 1 15  ? 14.84910  -8.58923  36.31451  1.000 37.57128  ? 9   ALA A O     1 
ATOM   65   C CB    . ALA A 1 15  ? 13.77291  -6.47190  38.47764  1.000 39.69330  ? 9   ALA A CB    1 
ATOM   66   N N     . ILE A 1 16  ? 12.61173  -8.79226  36.53454  1.000 34.76309  ? 10  ILE A N     1 
ATOM   67   C CA    . ILE A 1 16  ? 12.35001  -9.15692  35.14751  1.000 38.02719  ? 10  ILE A CA    1 
ATOM   68   C C     . ILE A 1 16  ? 11.40417  -8.11827  34.56279  1.000 33.55027  ? 10  ILE A C     1 
ATOM   69   O O     . ILE A 1 16  ? 10.38307  -7.78765  35.17658  1.000 37.81088  ? 10  ILE A O     1 
ATOM   70   C CB    . ILE A 1 16  ? 11.75756  -10.57441 35.02879  1.000 35.71556  ? 10  ILE A CB    1 
ATOM   71   C CG1   . ILE A 1 16  ? 12.87511  -11.61611 34.96722  1.000 40.78135  ? 10  ILE A CG1   1 
ATOM   72   C CG2   . ILE A 1 16  ? 10.86479  -10.69293 33.79940  1.000 32.67749  ? 10  ILE A CG2   1 
ATOM   73   C CD1   . ILE A 1 16  ? 12.38133  -13.03972 35.08161  1.000 40.62586  ? 10  ILE A CD1   1 
ATOM   74   N N     . ILE A 1 17  ? 11.74600  -7.60082  33.38583  1.000 35.72673  ? 11  ILE A N     1 
ATOM   75   C CA    . ILE A 1 17  ? 10.96025  -6.57397  32.71159  1.000 37.14620  ? 11  ILE A CA    1 
ATOM   76   C C     . ILE A 1 17  ? 10.34374  -7.17887  31.45961  1.000 31.07319  ? 11  ILE A C     1 
ATOM   77   O O     . ILE A 1 17  ? 11.02174  -7.88640  30.70538  1.000 33.68252  ? 11  ILE A O     1 
ATOM   78   C CB    . ILE A 1 17  ? 11.81766  -5.34571  32.36191  1.000 34.43431  ? 11  ILE A CB    1 
ATOM   79   C CG1   . ILE A 1 17  ? 12.33872  -4.68267  33.63545  1.000 35.47390  ? 11  ILE A CG1   1 
ATOM   80   C CG2   . ILE A 1 17  ? 11.02017  -4.34881  31.53354  1.000 35.61581  ? 11  ILE A CG2   1 
ATOM   81   C CD1   . ILE A 1 17  ? 13.43842  -3.69322  33.38690  1.000 36.17948  ? 11  ILE A CD1   1 
ATOM   82   N N     . ILE A 1 18  ? 9.06117   -6.90826  31.24250  1.000 32.79503  ? 12  ILE A N     1 
ATOM   83   C CA    . ILE A 1 18  ? 8.36613   -7.31585  30.02846  1.000 37.30378  ? 12  ILE A CA    1 
ATOM   84   C C     . ILE A 1 18  ? 8.11055   -6.05720  29.21243  1.000 32.78297  ? 12  ILE A C     1 
ATOM   85   O O     . ILE A 1 18  ? 7.29897   -5.20721  29.59953  1.000 34.66792  ? 12  ILE A O     1 
ATOM   86   C CB    . ILE A 1 18  ? 7.05924   -8.05859  30.33120  1.000 35.98030  ? 12  ILE A CB    1 
ATOM   87   C CG1   . ILE A 1 18  ? 7.32107   -9.23918  31.26639  1.000 32.67385  ? 12  ILE A CG1   1 
ATOM   88   C CG2   . ILE A 1 18  ? 6.42829   -8.55353  29.04185  1.000 38.57594  ? 12  ILE A CG2   1 
ATOM   89   C CD1   . ILE A 1 18  ? 6.05985   -9.85811  31.82893  1.000 36.16646  ? 12  ILE A CD1   1 
ATOM   90   N N     . GLY A 1 19  ? 8.80574   -5.93250  28.08587  1.000 37.50724  ? 13  GLY A N     1 
ATOM   91   C CA    . GLY A 1 19  ? 8.65367   -4.77379  27.23026  1.000 35.11893  ? 13  GLY A CA    1 
ATOM   92   C C     . GLY A 1 19  ? 9.95172   -4.02441  27.01690  1.000 36.15997  ? 13  GLY A C     1 
ATOM   93   O O     . GLY A 1 19  ? 10.71638  -3.80939  27.96224  1.000 32.19378  ? 13  GLY A O     1 
ATOM   94   N N     . ALA A 1 20  ? 10.21362  -3.62568  25.77264  1.000 33.23360  ? 14  ALA A N     1 
ATOM   95   C CA    . ALA A 1 20  ? 11.40664  -2.86584  25.42159  1.000 31.08265  ? 14  ALA A CA    1 
ATOM   96   C C     . ALA A 1 20  ? 11.04702  -1.56175  24.71676  1.000 31.51675  ? 14  ALA A C     1 
ATOM   97   O O     . ALA A 1 20  ? 11.77131  -1.10449  23.83101  1.000 26.32603  ? 14  ALA A O     1 
ATOM   98   C CB    . ALA A 1 20  ? 12.34858  -3.70322  24.55839  1.000 28.93556  ? 14  ALA A CB    1 
ATOM   99   N N     . GLY A 1 21  ? 9.92227   -0.96667  25.09009  1.000 30.57873  ? 15  GLY A N     1 
ATOM   100  C CA    . GLY A 1 21  ? 9.52211   0.33884   24.60312  1.000 29.95147  ? 15  GLY A CA    1 
ATOM   101  C C     . GLY A 1 21  ? 10.01170  1.44724   25.50742  1.000 33.90733  ? 15  GLY A C     1 
ATOM   102  O O     . GLY A 1 21  ? 11.00929  1.30241   26.22028  1.000 35.64952  ? 15  GLY A O     1 
ATOM   103  N N     . PHE A 1 22  ? 9.29551   2.57480   25.48048  1.000 31.36212  ? 16  PHE A N     1 
ATOM   104  C CA    . PHE A 1 22  ? 9.64315   3.70237   26.34180  1.000 34.45728  ? 16  PHE A CA    1 
ATOM   105  C C     . PHE A 1 22  ? 9.70430   3.28051   27.80556  1.000 34.93218  ? 16  PHE A C     1 
ATOM   106  O O     . PHE A 1 22  ? 10.65045  3.61883   28.52574  1.000 34.37800  ? 16  PHE A O     1 
ATOM   107  C CB    . PHE A 1 22  ? 8.63051   4.83485   26.15837  1.000 33.73282  ? 16  PHE A CB    1 
ATOM   108  C CG    . PHE A 1 22  ? 9.10875   5.94476   25.26618  1.000 33.33966  ? 16  PHE A CG    1 
ATOM   109  C CD1   . PHE A 1 22  ? 9.99846   6.89709   25.73677  1.000 31.23110  ? 16  PHE A CD1   1 
ATOM   110  C CD2   . PHE A 1 22  ? 8.65711   6.04441   23.96086  1.000 33.05177  ? 16  PHE A CD2   1 
ATOM   111  C CE1   . PHE A 1 22  ? 10.43534  7.92257   24.91894  1.000 31.79083  ? 16  PHE A CE1   1 
ATOM   112  C CE2   . PHE A 1 22  ? 9.09017   7.06785   23.13797  1.000 32.20223  ? 16  PHE A CE2   1 
ATOM   113  C CZ    . PHE A 1 22  ? 9.98049   8.00804   23.61817  1.000 31.61663  ? 16  PHE A CZ    1 
ATOM   114  N N     . GLY A 1 23  ? 8.70130   2.52742   28.25919  1.000 31.60545  ? 17  GLY A N     1 
ATOM   115  C CA    . GLY A 1 23  ? 8.65486   2.14347   29.65991  1.000 33.95576  ? 17  GLY A CA    1 
ATOM   116  C C     . GLY A 1 23  ? 9.69389   1.10161   30.02637  1.000 32.71767  ? 17  GLY A C     1 
ATOM   117  O O     . GLY A 1 23  ? 10.33430  1.19512   31.07737  1.000 33.17585  ? 17  GLY A O     1 
ATOM   118  N N     . GLY A 1 24  ? 9.87794   0.09715   29.16835  1.000 33.80465  ? 18  GLY A N     1 
ATOM   119  C CA    . GLY A 1 24  ? 10.79018  -0.98497  29.49952  1.000 34.20572  ? 18  GLY A CA    1 
ATOM   120  C C     . GLY A 1 24  ? 12.24931  -0.57538  29.43863  1.000 34.30821  ? 18  GLY A C     1 
ATOM   121  O O     . GLY A 1 24  ? 13.06658  -1.04400  30.23611  1.000 33.65682  ? 18  GLY A O     1 
ATOM   122  N N     . LEU A 1 25  ? 12.59942  0.30010   28.49298  1.000 33.21713  ? 19  LEU A N     1 
ATOM   123  C CA    . LEU A 1 25  ? 13.99354  0.71020   28.34901  1.000 30.52184  ? 19  LEU A CA    1 
ATOM   124  C C     . LEU A 1 25  ? 14.46769  1.51269   29.55464  1.000 34.66159  ? 19  LEU A C     1 
ATOM   125  O O     . LEU A 1 25  ? 15.58879  1.31196   30.03642  1.000 36.71463  ? 19  LEU A O     1 
ATOM   126  C CB    . LEU A 1 25  ? 14.17738  1.51522   27.06262  1.000 34.11567  ? 19  LEU A CB    1 
ATOM   127  C CG    . LEU A 1 25  ? 14.08900  0.72808   25.75338  1.000 34.91850  ? 19  LEU A CG    1 
ATOM   128  C CD1   . LEU A 1 25  ? 14.19888  1.65927   24.55327  1.000 32.96098  ? 19  LEU A CD1   1 
ATOM   129  C CD2   . LEU A 1 25  ? 15.15800  -0.35116  25.70595  1.000 35.91666  ? 19  LEU A CD2   1 
ATOM   130  N N     . TYR A 1 26  ? 13.63368  2.42764   30.05556  1.000 33.20711  ? 20  TYR A N     1 
ATOM   131  C CA    . TYR A 1 26  ? 14.02712  3.20789   31.22418  1.000 34.72522  ? 20  TYR A CA    1 
ATOM   132  C C     . TYR A 1 26  ? 13.97110  2.37570   32.49835  1.000 36.60049  ? 20  TYR A C     1 
ATOM   133  O O     . TYR A 1 26  ? 14.78023  2.58652   33.40932  1.000 35.32363  ? 20  TYR A O     1 
ATOM   134  C CB    . TYR A 1 26  ? 13.14476  4.44904   31.36075  1.000 34.86032  ? 20  TYR A CB    1 
ATOM   135  C CG    . TYR A 1 26  ? 13.64224  5.42639   32.40271  1.000 34.67383  ? 20  TYR A CG    1 
ATOM   136  C CD1   . TYR A 1 26  ? 15.00069  5.66707   32.56068  1.000 34.68553  ? 20  TYR A CD1   1 
ATOM   137  C CD2   . TYR A 1 26  ? 12.75681  6.10703   33.22771  1.000 34.07688  ? 20  TYR A CD2   1 
ATOM   138  C CE1   . TYR A 1 26  ? 15.46423  6.55672   33.51088  1.000 36.64011  ? 20  TYR A CE1   1 
ATOM   139  C CE2   . TYR A 1 26  ? 13.21203  6.99990   34.18266  1.000 36.19924  ? 20  TYR A CE2   1 
ATOM   140  C CZ    . TYR A 1 26  ? 14.56681  7.22033   34.31859  1.000 38.84138  ? 20  TYR A CZ    1 
ATOM   141  O OH    . TYR A 1 26  ? 15.02881  8.10680   35.26452  1.000 38.94159  ? 20  TYR A OH    1 
ATOM   142  N N     . SER A 1 27  ? 13.02660  1.43540   32.58478  1.000 37.24011  ? 21  SER A N     1 
ATOM   143  C CA    . SER A 1 27  ? 13.00915  0.51127   33.71389  1.000 36.56155  ? 21  SER A CA    1 
ATOM   144  C C     . SER A 1 27  ? 14.30319  -0.28829  33.77963  1.000 37.39723  ? 21  SER A C     1 
ATOM   145  O O     . SER A 1 27  ? 14.83554  -0.53891  34.86736  1.000 37.15796  ? 21  SER A O     1 
ATOM   146  C CB    . SER A 1 27  ? 11.80565  -0.42683  33.60934  1.000 34.84755  ? 21  SER A CB    1 
ATOM   147  O OG    . SER A 1 27  ? 10.59134  0.26011   33.85441  1.000 35.37176  ? 21  SER A OG    1 
ATOM   148  N N     . LEU A 1 28  ? 14.82901  -0.68717  32.61941  1.000 36.37901  ? 22  LEU A N     1 
ATOM   149  C CA    . LEU A 1 28  ? 16.08786  -1.42292  32.58256  1.000 33.06811  ? 22  LEU A CA    1 
ATOM   150  C C     . LEU A 1 28  ? 17.25987  -0.53480  32.97915  1.000 40.78369  ? 22  LEU A C     1 
ATOM   151  O O     . LEU A 1 28  ? 18.13619  -0.95832  33.74124  1.000 33.87325  ? 22  LEU A O     1 
ATOM   152  C CB    . LEU A 1 28  ? 16.30395  -2.00773  31.18761  1.000 35.69520  ? 22  LEU A CB    1 
ATOM   153  C CG    . LEU A 1 28  ? 17.54143  -2.87844  30.97177  1.000 41.05867  ? 22  LEU A CG    1 
ATOM   154  C CD1   . LEU A 1 28  ? 17.57935  -4.01880  31.97367  1.000 45.42796  ? 22  LEU A CD1   1 
ATOM   155  C CD2   . LEU A 1 28  ? 17.56764  -3.40979  29.54834  1.000 37.96015  ? 22  LEU A CD2   1 
ATOM   156  N N     . LYS A 1 29  ? 17.29087  0.70074   32.47412  1.000 37.99923  ? 23  LYS A N     1 
ATOM   157  C CA    . LYS A 1 29  ? 18.39200  1.60500   32.78986  1.000 38.03795  ? 23  LYS A CA    1 
ATOM   158  C C     . LYS A 1 29  ? 18.40373  1.97274   34.26877  1.000 38.20900  ? 23  LYS A C     1 
ATOM   159  O O     . LYS A 1 29  ? 19.46747  2.00005   34.89892  1.000 42.26539  ? 23  LYS A O     1 
ATOM   160  C CB    . LYS A 1 29  ? 18.29691  2.86183   31.92459  1.000 36.62575  ? 23  LYS A CB    1 
ATOM   161  C CG    . LYS A 1 29  ? 19.27156  3.96165   32.31076  1.000 36.14616  ? 23  LYS A CG    1 
ATOM   162  C CD    . LYS A 1 29  ? 20.70775  3.52916   32.07661  1.000 40.60665  ? 23  LYS A CD    1 
ATOM   163  C CE    . LYS A 1 29  ? 21.69073  4.55770   32.61255  1.000 39.99966  ? 23  LYS A CE    1 
ATOM   164  N NZ    . LYS A 1 29  ? 23.09178  4.22653   32.23301  1.000 40.68968  ? 23  LYS A NZ    1 
ATOM   165  N N     . LYS A 1 30  ? 17.23032  2.24905   34.84082  1.000 38.29774  ? 24  LYS A N     1 
ATOM   166  C CA    . LYS A 1 30  ? 17.16297  2.68784   36.23108  1.000 38.23725  ? 24  LYS A CA    1 
ATOM   167  C C     . LYS A 1 30  ? 17.52926  1.55994   37.18862  1.000 42.68666  ? 24  LYS A C     1 
ATOM   168  O O     . LYS A 1 30  ? 18.31471  1.75590   38.12342  1.000 41.58975  ? 24  LYS A O     1 
ATOM   169  C CB    . LYS A 1 30  ? 15.76437  3.22214   36.54003  1.000 36.59227  ? 24  LYS A CB    1 
ATOM   170  C CG    . LYS A 1 30  ? 15.70267  4.14893   37.74250  1.000 47.41118  ? 24  LYS A CG    1 
ATOM   171  C CD    . LYS A 1 30  ? 16.16831  5.55000   37.38625  1.000 48.34357  ? 24  LYS A CD    1 
ATOM   172  C CE    . LYS A 1 30  ? 16.74420  6.26454   38.59759  1.000 49.16755  ? 24  LYS A CE    1 
ATOM   173  N NZ    . LYS A 1 30  ? 17.49066  7.49357   38.21017  1.000 54.55466  ? 24  LYS A NZ    1 
ATOM   174  N N     . LEU A 1 31  ? 16.97129  0.36765   36.96936  1.000 41.14055  ? 25  LEU A N     1 
ATOM   175  C CA    . LEU A 1 31  ? 17.17364  -0.72631  37.91401  1.000 38.45427  ? 25  LEU A CA    1 
ATOM   176  C C     . LEU A 1 31  ? 18.57762  -1.30962  37.80678  1.000 42.02757  ? 25  LEU A C     1 
ATOM   177  O O     . LEU A 1 31  ? 19.17592  -1.68725  38.82083  1.000 47.10730  ? 25  LEU A O     1 
ATOM   178  C CB    . LEU A 1 31  ? 16.12255  -1.81273  37.68739  1.000 39.18666  ? 25  LEU A CB    1 
ATOM   179  C CG    . LEU A 1 31  ? 14.67439  -1.43198  38.00455  1.000 39.62559  ? 25  LEU A CG    1 
ATOM   180  C CD1   . LEU A 1 31  ? 13.73756  -2.59912  37.72987  1.000 38.06474  ? 25  LEU A CD1   1 
ATOM   181  C CD2   . LEU A 1 31  ? 14.54519  -0.96405  39.44555  1.000 36.33747  ? 25  LEU A CD2   1 
ATOM   182  N N     . ARG A 1 32  ? 19.12317  -1.38804  36.59147  1.000 42.61769  ? 26  ARG A N     1 
ATOM   183  C CA    . ARG A 1 32  ? 20.40894  -2.05193  36.40111  1.000 41.25664  ? 26  ARG A CA    1 
ATOM   184  C C     . ARG A 1 32  ? 21.58432  -1.12636  36.69190  1.000 49.49516  ? 26  ARG A C     1 
ATOM   185  O O     . ARG A 1 32  ? 22.56016  -1.54338  37.32523  1.000 49.56480  ? 26  ARG A O     1 
ATOM   186  C CB    . ARG A 1 32  ? 20.51375  -2.59827  34.97727  1.000 45.87059  ? 26  ARG A CB    1 
ATOM   187  C CG    . ARG A 1 32  ? 21.74044  -3.46006  34.72970  1.000 43.55314  ? 26  ARG A CG    1 
ATOM   188  C CD    . ARG A 1 32  ? 22.02786  -3.58969  33.24282  1.000 47.26772  ? 26  ARG A CD    1 
ATOM   189  N NE    . ARG A 1 32  ? 22.51261  -2.34189  32.66404  1.000 46.35829  ? 26  ARG A NE    1 
ATOM   190  C CZ    . ARG A 1 32  ? 22.75283  -2.15798  31.37266  1.000 47.80061  ? 26  ARG A CZ    1 
ATOM   191  N NH1   . ARG A 1 32  ? 22.55544  -3.12231  30.48809  1.000 40.61643  ? 26  ARG A NH1   1 
ATOM   192  N NH2   . ARG A 1 32  ? 23.20145  -0.97642  30.95785  1.000 46.08180  ? 26  ARG A NH2   1 
ATOM   193  N N     . ASP A 1 33  ? 21.51750  0.12403   36.23863  1.000 41.87468  ? 27  ASP A N     1 
ATOM   194  C CA    . ASP A 1 33  ? 22.66348  1.02143   36.31416  1.000 48.07022  ? 27  ASP A CA    1 
ATOM   195  C C     . ASP A 1 33  ? 22.63780  1.95126   37.51804  1.000 47.50810  ? 27  ASP A C     1 
ATOM   196  O O     . ASP A 1 33  ? 23.70232  2.27196   38.05597  1.000 49.44672  ? 27  ASP A O     1 
ATOM   197  C CB    . ASP A 1 33  ? 22.76269  1.85886   35.03470  1.000 45.88482  ? 27  ASP A CB    1 
ATOM   198  C CG    . ASP A 1 33  ? 23.24601  1.04946   33.84848  1.000 49.86776  ? 27  ASP A CG    1 
ATOM   199  O OD1   . ASP A 1 33  ? 23.65370  -0.11395  34.04915  1.000 48.50788  ? 27  ASP A OD1   1 
ATOM   200  O OD2   . ASP A 1 33  ? 23.21819  1.57391   32.71574  1.000 53.74545  ? 27  ASP A OD2   1 
ATOM   201  N N     . ASP A 1 34  ? 21.46016  2.39388   37.95639  1.000 46.47304  ? 28  ASP A N     1 
ATOM   202  C CA    . ASP A 1 34  ? 21.37476  3.30894   39.08661  1.000 46.15978  ? 28  ASP A CA    1 
ATOM   203  C C     . ASP A 1 34  ? 21.15511  2.60038   40.41546  1.000 50.94592  ? 28  ASP A C     1 
ATOM   204  O O     . ASP A 1 34  ? 21.41854  3.19384   41.46784  1.000 53.28573  ? 28  ASP A O     1 
ATOM   205  C CB    . ASP A 1 34  ? 20.25535  4.32936   38.85823  1.000 43.12708  ? 28  ASP A CB    1 
ATOM   206  C CG    . ASP A 1 34  ? 20.58088  5.30892   37.74674  1.000 47.39237  ? 28  ASP A CG    1 
ATOM   207  O OD1   . ASP A 1 34  ? 21.76833  5.41345   37.37482  1.000 50.85326  ? 28  ASP A OD1   1 
ATOM   208  O OD2   . ASP A 1 34  ? 19.65166  5.97447   37.24450  1.000 53.29403  ? 28  ASP A OD2   1 
ATOM   209  N N     . PHE A 1 35  ? 20.68353  1.35440   40.39608  1.000 49.87394  ? 29  PHE A N     1 
ATOM   210  C CA    . PHE A 1 35  ? 20.51945  0.57006   41.61037  1.000 47.57823  ? 29  PHE A CA    1 
ATOM   211  C C     . PHE A 1 35  ? 21.32382  -0.72167  41.59055  1.000 46.82458  ? 29  PHE A C     1 
ATOM   212  O O     . PHE A 1 35  ? 21.24820  -1.49484  42.55309  1.000 50.06773  ? 29  PHE A O     1 
ATOM   213  C CB    . PHE A 1 35  ? 19.03451  0.26197   41.84972  1.000 45.84116  ? 29  PHE A CB    1 
ATOM   214  C CG    . PHE A 1 35  ? 18.23968  1.45130   42.31317  1.000 44.79685  ? 29  PHE A CG    1 
ATOM   215  C CD1   . PHE A 1 35  ? 17.81784  2.41419   41.41069  1.000 40.32235  ? 29  PHE A CD1   1 
ATOM   216  C CD2   . PHE A 1 35  ? 17.92403  1.61214   43.65283  1.000 47.87278  ? 29  PHE A CD2   1 
ATOM   217  C CE1   . PHE A 1 35  ? 17.09277  3.51191   41.83434  1.000 45.48386  ? 29  PHE A CE1   1 
ATOM   218  C CE2   . PHE A 1 35  ? 17.19804  2.70742   44.08234  1.000 46.31945  ? 29  PHE A CE2   1 
ATOM   219  C CZ    . PHE A 1 35  ? 16.78149  3.65804   43.17182  1.000 45.25940  ? 29  PHE A CZ    1 
ATOM   220  N N     . ASN A 1 36  ? 22.08509  -0.97421  40.52270  1.000 45.10164  ? 30  ASN A N     1 
ATOM   221  C CA    . ASN A 1 36  ? 23.01753  -2.10141  40.44300  1.000 50.44877  ? 30  ASN A CA    1 
ATOM   222  C C     . ASN A 1 36  ? 22.31685  -3.43877  40.67387  1.000 55.15608  ? 30  ASN A C     1 
ATOM   223  O O     . ASN A 1 36  ? 22.85497  -4.34005  41.32000  1.000 57.26833  ? 30  ASN A O     1 
ATOM   224  C CB    . ASN A 1 36  ? 24.18315  -1.91983  41.41722  1.000 55.30155  ? 30  ASN A CB    1 
ATOM   225  C CG    . ASN A 1 36  ? 25.27056  -1.02140  40.85974  1.000 64.13296  ? 30  ASN A CG    1 
ATOM   226  O OD1   . ASN A 1 36  ? 25.25963  0.19084   41.07215  1.000 60.19098  ? 30  ASN A OD1   1 
ATOM   227  N ND2   . ASN A 1 36  ? 26.21458  -1.61297  40.13689  1.000 68.55287  ? 30  ASN A ND2   1 
ATOM   228  N N     . LEU A 1 37  ? 21.10979  -3.57181  40.13776  1.000 47.95323  ? 31  LEU A N     1 
ATOM   229  C CA    . LEU A 1 37  ? 20.37102  -4.82070  40.22133  1.000 50.05949  ? 31  LEU A CA    1 
ATOM   230  C C     . LEU A 1 37  ? 20.62253  -5.67006  38.97958  1.000 47.86051  ? 31  LEU A C     1 
ATOM   231  O O     . LEU A 1 37  ? 21.00275  -5.16970  37.91840  1.000 49.52471  ? 31  LEU A O     1 
ATOM   232  C CB    . LEU A 1 37  ? 18.87347  -4.55481  40.38213  1.000 47.23101  ? 31  LEU A CB    1 
ATOM   233  C CG    . LEU A 1 37  ? 18.46488  -3.63295  41.53224  1.000 44.22712  ? 31  LEU A CG    1 
ATOM   234  C CD1   . LEU A 1 37  ? 16.95458  -3.46042  41.57108  1.000 49.16709  ? 31  LEU A CD1   1 
ATOM   235  C CD2   . LEU A 1 37  ? 18.97998  -4.16867  42.85865  1.000 54.60831  ? 31  LEU A CD2   1 
ATOM   236  N N     . LYS A 1 38  ? 20.41169  -6.97511  39.12884  1.000 49.30696  ? 32  LYS A N     1 
ATOM   237  C CA    . LYS A 1 38  ? 20.53687  -7.91569  38.02066  1.000 45.70439  ? 32  LYS A CA    1 
ATOM   238  C C     . LYS A 1 38  ? 19.17839  -8.02339  37.33783  1.000 42.52867  ? 32  LYS A C     1 
ATOM   239  O O     . LYS A 1 38  ? 18.22040  -8.53941  37.92239  1.000 40.81737  ? 32  LYS A O     1 
ATOM   240  C CB    . LYS A 1 38  ? 21.02511  -9.27348  38.51697  1.000 52.75953  ? 32  LYS A CB    1 
ATOM   241  C CG    . LYS A 1 38  ? 21.81292  -10.06024 37.48419  1.000 54.03573  ? 32  LYS A CG    1 
ATOM   242  C CD    . LYS A 1 38  ? 21.63982  -11.55358 37.68677  1.000 57.83577  ? 32  LYS A CD    1 
ATOM   243  C CE    . LYS A 1 38  ? 22.04199  -12.33439 36.44728  1.000 56.77932  ? 32  LYS A CE    1 
ATOM   244  N NZ    . LYS A 1 38  ? 21.50592  -13.72330 36.47855  1.000 59.94837  ? 32  LYS A NZ    1 
ATOM   245  N N     . VAL A 1 39  ? 19.09126  -7.52482  36.10568  1.000 43.43417  ? 33  VAL A N     1 
ATOM   246  C CA    . VAL A 1 39  ? 17.82242  -7.39165  35.40315  1.000 40.01553  ? 33  VAL A CA    1 
ATOM   247  C C     . VAL A 1 39  ? 17.91775  -8.06480  34.04106  1.000 41.10472  ? 33  VAL A C     1 
ATOM   248  O O     . VAL A 1 39  ? 18.98661  -8.12231  33.42472  1.000 38.35661  ? 33  VAL A O     1 
ATOM   249  C CB    . VAL A 1 39  ? 17.41297  -5.90735  35.24083  1.000 39.20729  ? 33  VAL A CB    1 
ATOM   250  C CG1   . VAL A 1 39  ? 15.94045  -5.79137  34.88735  1.000 40.23137  ? 33  VAL A CG1   1 
ATOM   251  C CG2   . VAL A 1 39  ? 17.72218  -5.11866  36.50483  1.000 40.92599  ? 33  VAL A CG2   1 
ATOM   252  N N     . ARG A 1 40  ? 16.78128  -8.58221  33.57632  1.000 39.82010  ? 34  ARG A N     1 
ATOM   253  C CA    . ARG A 1 40  ? 16.63518  -9.09188  32.21953  1.000 42.06815  ? 34  ARG A CA    1 
ATOM   254  C C     . ARG A 1 40  ? 15.28159  -8.65380  31.68422  1.000 39.00583  ? 34  ARG A C     1 
ATOM   255  O O     . ARG A 1 40  ? 14.26785  -8.78302  32.37700  1.000 38.33608  ? 34  ARG A O     1 
ATOM   256  C CB    . ARG A 1 40  ? 16.75486  -10.61991 32.17022  1.000 44.30656  ? 34  ARG A CB    1 
ATOM   257  C CG    . ARG A 1 40  ? 16.94052  -11.17972 30.76388  1.000 44.21700  ? 34  ARG A CG    1 
ATOM   258  C CD    . ARG A 1 40  ? 18.27899  -11.88722 30.61500  1.000 47.97021  ? 34  ARG A CD    1 
ATOM   259  N NE    . ARG A 1 40  ? 18.33343  -12.71834 29.41816  1.000 56.63675  ? 34  ARG A NE    1 
ATOM   260  C CZ    . ARG A 1 40  ? 18.92557  -12.36290 28.28610  1.000 55.76142  ? 34  ARG A CZ    1 
ATOM   261  N NH1   . ARG A 1 40  ? 19.53262  -11.19418 28.16095  1.000 51.62055  ? 34  ARG A NH1   1 
ATOM   262  N NH2   . ARG A 1 40  ? 18.91131  -13.20248 27.25474  1.000 52.75888  ? 34  ARG A NH2   1 
ATOM   263  N N     . ALA A 1 41  ? 15.26862  -8.13503  30.46023  1.000 40.89527  ? 35  ALA A N     1 
ATOM   264  C CA    . ALA A 1 41  ? 14.05154  -7.66446  29.81823  1.000 39.39215  ? 35  ALA A CA    1 
ATOM   265  C C     . ALA A 1 41  ? 13.70192  -8.55658  28.63387  1.000 36.71639  ? 35  ALA A C     1 
ATOM   266  O O     . ALA A 1 41  ? 14.58241  -9.12268  27.97972  1.000 38.24583  ? 35  ALA A O     1 
ATOM   267  C CB    . ALA A 1 41  ? 14.19729  -6.21171  29.35442  1.000 34.88501  ? 35  ALA A CB    1 
ATOM   268  N N     . PHE A 1 42  ? 12.40282  -8.67549  28.36284  1.000 35.95157  ? 36  PHE A N     1 
ATOM   269  C CA    . PHE A 1 42  ? 11.90011  -9.53161  27.29906  1.000 38.02246  ? 36  PHE A CA    1 
ATOM   270  C C     . PHE A 1 42  ? 10.92348  -8.76123  26.42269  1.000 34.84555  ? 36  PHE A C     1 
ATOM   271  O O     . PHE A 1 42  ? 10.21500  -7.86560  26.89060  1.000 36.10719  ? 36  PHE A O     1 
ATOM   272  C CB    . PHE A 1 42  ? 11.20319  -10.78110 27.85894  1.000 39.80505  ? 36  PHE A CB    1 
ATOM   273  C CG    . PHE A 1 42  ? 12.09250  -11.64801 28.70231  1.000 40.32546  ? 36  PHE A CG    1 
ATOM   274  C CD1   . PHE A 1 42  ? 12.23504  -11.40490 30.05818  1.000 41.28513  ? 36  PHE A CD1   1 
ATOM   275  C CD2   . PHE A 1 42  ? 12.78069  -12.71018 28.14081  1.000 38.50106  ? 36  PHE A CD2   1 
ATOM   276  C CE1   . PHE A 1 42  ? 13.05086  -12.20281 30.83796  1.000 41.79132  ? 36  PHE A CE1   1 
ATOM   277  C CE2   . PHE A 1 42  ? 13.59895  -13.51167 28.91494  1.000 42.54702  ? 36  PHE A CE2   1 
ATOM   278  C CZ    . PHE A 1 42  ? 13.73355  -13.25754 30.26516  1.000 42.26143  ? 36  PHE A CZ    1 
ATOM   279  N N     . ASP A 1 43  ? 10.88952  -9.12863  25.14313  1.000 37.01504  ? 37  ASP A N     1 
ATOM   280  C CA    . ASP A 1 43  ? 9.94878   -8.54977  24.19492  1.000 37.10880  ? 37  ASP A CA    1 
ATOM   281  C C     . ASP A 1 43  ? 9.84988   -9.46468  22.98345  1.000 35.69519  ? 37  ASP A C     1 
ATOM   282  O O     . ASP A 1 43  ? 10.84938  -10.05010 22.55977  1.000 34.56972  ? 37  ASP A O     1 
ATOM   283  C CB    . ASP A 1 43  ? 10.37612  -7.14196  23.76125  1.000 34.27058  ? 37  ASP A CB    1 
ATOM   284  C CG    . ASP A 1 43  ? 9.21709   -6.31791  23.23259  1.000 37.57706  ? 37  ASP A CG    1 
ATOM   285  O OD1   . ASP A 1 43  ? 8.47022   -6.82232  22.36706  1.000 39.44839  ? 37  ASP A OD1   1 
ATOM   286  O OD2   . ASP A 1 43  ? 9.05326   -5.16422  23.68070  1.000 36.97224  ? 37  ASP A OD2   1 
ATOM   287  N N     . ARG A 1 44  ? 8.63844   -9.58248  22.43382  1.000 35.74139  ? 38  ARG A N     1 
ATOM   288  C CA    . ARG A 1 44  ? 8.45637   -10.36052 21.21290  1.000 38.61981  ? 38  ARG A CA    1 
ATOM   289  C C     . ARG A 1 44  ? 9.14664   -9.70544  20.02523  1.000 41.25025  ? 38  ARG A C     1 
ATOM   290  O O     . ARG A 1 44  ? 9.51946   -10.39436 19.06851  1.000 40.37892  ? 38  ARG A O     1 
ATOM   291  C CB    . ARG A 1 44  ? 6.96762   -10.54167 20.91594  1.000 41.05455  ? 38  ARG A CB    1 
ATOM   292  C CG    . ARG A 1 44  ? 6.21833   -11.36738 21.94348  1.000 39.29279  ? 38  ARG A CG    1 
ATOM   293  C CD    . ARG A 1 44  ? 4.91983   -11.91009 21.37093  1.000 41.07101  ? 38  ARG A CD    1 
ATOM   294  N NE    . ARG A 1 44  ? 4.20637   -12.74783 22.32743  1.000 43.88856  ? 38  ARG A NE    1 
ATOM   295  C CZ    . ARG A 1 44  ? 3.39081   -12.28614 23.26546  1.000 41.09683  ? 38  ARG A CZ    1 
ATOM   296  N NH1   . ARG A 1 44  ? 3.16505   -10.99050 23.40857  1.000 44.23129  ? 38  ARG A NH1   1 
ATOM   297  N NH2   . ARG A 1 44  ? 2.78582   -13.14610 24.07984  1.000 41.61562  ? 38  ARG A NH2   1 
ATOM   298  N N     . ALA A 1 45  ? 9.32196   -8.38715  20.06853  1.000 41.54670  ? 39  ALA A N     1 
ATOM   299  C CA    . ALA A 1 45  ? 9.94249   -7.66660  18.96978  1.000 39.27893  ? 39  ALA A CA    1 
ATOM   300  C C     . ALA A 1 45  ? 11.40051  -8.08312  18.80282  1.000 40.26220  ? 39  ALA A C     1 
ATOM   301  O O     . ALA A 1 45  ? 12.04420  -8.58843  19.72599  1.000 42.22982  ? 39  ALA A O     1 
ATOM   302  C CB    . ALA A 1 45  ? 9.85494   -6.15945  19.20552  1.000 40.51134  ? 39  ALA A CB    1 
ATOM   303  N N     . THR A 1 46  ? 11.91843  -7.86551  17.59730  1.000 38.88254  ? 40  THR A N     1 
ATOM   304  C CA    . THR A 1 46  ? 13.32043  -8.11287  17.29406  1.000 38.95805  ? 40  THR A CA    1 
ATOM   305  C C     . THR A 1 46  ? 14.20519  -6.91255  17.60235  1.000 43.63369  ? 40  THR A C     1 
ATOM   306  O O     . THR A 1 46  ? 15.42203  -6.98829  17.40123  1.000 40.52450  ? 40  THR A O     1 
ATOM   307  C CB    . THR A 1 46  ? 13.48293  -8.50183  15.82058  1.000 42.45029  ? 40  THR A CB    1 
ATOM   308  O OG1   . THR A 1 46  ? 12.90302  -7.48744  14.99100  1.000 51.68513  ? 40  THR A OG1   1 
ATOM   309  C CG2   . THR A 1 46  ? 12.79293  -9.82726  15.53992  1.000 43.78774  ? 40  THR A CG2   1 
ATOM   310  N N     . GLU A 1 47  ? 13.62599  -5.81659  18.08689  1.000 38.87617  ? 41  GLU A N     1 
ATOM   311  C CA    . GLU A 1 47  ? 14.37025  -4.59194  18.34000  1.000 38.46726  ? 41  GLU A CA    1 
ATOM   312  C C     . GLU A 1 47  ? 13.57503  -3.74115  19.32052  1.000 35.14778  ? 41  GLU A C     1 
ATOM   313  O O     . GLU A 1 47  ? 12.36106  -3.90599  19.46944  1.000 32.75196  ? 41  GLU A O     1 
ATOM   314  C CB    . GLU A 1 47  ? 14.64269  -3.83405  17.03238  1.000 40.11700  ? 41  GLU A CB    1 
ATOM   315  C CG    . GLU A 1 47  ? 15.42956  -2.52827  17.15846  1.000 42.97722  ? 41  GLU A CG    1 
ATOM   316  C CD    . GLU A 1 47  ? 16.78792  -2.69258  17.82071  1.000 42.98636  ? 41  GLU A CD    1 
ATOM   317  O OE1   . GLU A 1 47  ? 16.84470  -2.83104  19.06008  1.000 43.05542  ? 41  GLU A OE1   1 
ATOM   318  O OE2   . GLU A 1 47  ? 17.80573  -2.67194  17.09589  1.000 51.51586  ? 41  GLU A OE2   1 
ATOM   319  N N     . VAL A 1 48  ? 14.28439  -2.83989  20.00706  1.000 34.15762  ? 42  VAL A N     1 
ATOM   320  C CA    . VAL A 1 48  ? 13.62437  -1.91806  20.92234  1.000 35.26968  ? 42  VAL A CA    1 
ATOM   321  C C     . VAL A 1 48  ? 12.67647  -1.00099  20.14910  1.000 31.50855  ? 42  VAL A C     1 
ATOM   322  O O     . VAL A 1 48  ? 12.75353  -0.86527  18.92221  1.000 34.29435  ? 42  VAL A O     1 
ATOM   323  C CB    . VAL A 1 48  ? 14.65804  -1.09559  21.70741  1.000 34.12393  ? 42  VAL A CB    1 
ATOM   324  C CG1   . VAL A 1 48  ? 15.60724  -2.01469  22.45736  1.000 31.24098  ? 42  VAL A CG1   1 
ATOM   325  C CG2   . VAL A 1 48  ? 15.42836  -0.17847  20.76755  1.000 30.33324  ? 42  VAL A CG2   1 
ATOM   326  N N     . GLY A 1 49  ? 11.76816  -0.36487  20.88515  1.000 33.36582  ? 43  GLY A N     1 
ATOM   327  C CA    . GLY A 1 49  ? 10.85906  0.58843   20.27934  1.000 34.18823  ? 43  GLY A CA    1 
ATOM   328  C C     . GLY A 1 49  ? 9.43207   0.51361   20.78207  1.000 31.52588  ? 43  GLY A C     1 
ATOM   329  O O     . GLY A 1 49  ? 8.75337   1.53997   20.88458  1.000 31.89162  ? 43  GLY A O     1 
ATOM   330  N N     . GLY A 1 50  ? 8.96262   -0.68952  21.09450  1.000 30.99572  ? 44  GLY A N     1 
ATOM   331  C CA    . GLY A 1 50  ? 7.58237   -0.83692  21.53236  1.000 32.09975  ? 44  GLY A CA    1 
ATOM   332  C C     . GLY A 1 50  ? 6.62688   -0.59538  20.37991  1.000 31.05798  ? 44  GLY A C     1 
ATOM   333  O O     . GLY A 1 50  ? 6.79267   -1.14470  19.28504  1.000 32.42219  ? 44  GLY A O     1 
ATOM   334  N N     . THR A 1 51  ? 5.61189   0.24149   20.62125  1.000 31.03044  ? 45  THR A N     1 
ATOM   335  C CA    . THR A 1 51  ? 4.65540   0.57314   19.56830  1.000 33.95574  ? 45  THR A CA    1 
ATOM   336  C C     . THR A 1 51  ? 5.34212   1.19559   18.36115  1.000 32.70705  ? 45  THR A C     1 
ATOM   337  O O     . THR A 1 51  ? 4.85842   1.05999   17.23146  1.000 35.22366  ? 45  THR A O     1 
ATOM   338  C CB    . THR A 1 51  ? 3.58423   1.52673   20.10131  1.000 39.11894  ? 45  THR A CB    1 
ATOM   339  O OG1   . THR A 1 51  ? 4.20493   2.56883   20.86509  1.000 43.02753  ? 45  THR A OG1   1 
ATOM   340  C CG2   . THR A 1 51  ? 2.58846   0.78389   20.97575  1.000 49.35562  ? 45  THR A CG2   1 
ATOM   341  N N     . TRP A 1 52  ? 6.46558   1.87890   18.57781  1.000 28.33017  ? 46  TRP A N     1 
ATOM   342  C CA    . TRP A 1 52  ? 7.18745   2.51639   17.48686  1.000 32.41807  ? 46  TRP A CA    1 
ATOM   343  C C     . TRP A 1 52  ? 7.95275   1.52239   16.62679  1.000 36.36966  ? 46  TRP A C     1 
ATOM   344  O O     . TRP A 1 52  ? 8.38952   1.88659   15.52972  1.000 31.59201  ? 46  TRP A O     1 
ATOM   345  C CB    . TRP A 1 52  ? 8.12088   3.57904   18.05853  1.000 29.43988  ? 46  TRP A CB    1 
ATOM   346  C CG    . TRP A 1 52  ? 7.34568   4.67265   18.70388  1.000 28.51553  ? 46  TRP A CG    1 
ATOM   347  C CD1   . TRP A 1 52  ? 7.17652   4.88733   20.04075  1.000 26.63880  ? 46  TRP A CD1   1 
ATOM   348  C CD2   . TRP A 1 52  ? 6.59285   5.68696   18.03455  1.000 27.11312  ? 46  TRP A CD2   1 
ATOM   349  N NE1   . TRP A 1 52  ? 6.37710   5.98760   20.24381  1.000 29.31880  ? 46  TRP A NE1   1 
ATOM   350  C CE2   . TRP A 1 52  ? 6.00595   6.49537   19.02616  1.000 30.19809  ? 46  TRP A CE2   1 
ATOM   351  C CE3   . TRP A 1 52  ? 6.36630   5.99573   16.69075  1.000 25.10897  ? 46  TRP A CE3   1 
ATOM   352  C CZ2   . TRP A 1 52  ? 5.20678   7.59117   18.71539  1.000 28.83450  ? 46  TRP A CZ2   1 
ATOM   353  C CZ3   . TRP A 1 52  ? 5.57360   7.08285   16.38503  1.000 29.64948  ? 46  TRP A CZ3   1 
ATOM   354  C CH2   . TRP A 1 52  ? 5.00672   7.86969   17.39155  1.000 31.68808  ? 46  TRP A CH2   1 
ATOM   355  N N     . PHE A 1 53  ? 8.12293   0.28663   17.09308  1.000 30.92917  ? 47  PHE A N     1 
ATOM   356  C CA    . PHE A 1 53  ? 8.60797   -0.79060  16.24191  1.000 34.51647  ? 47  PHE A CA    1 
ATOM   357  C C     . PHE A 1 53  ? 7.46354   -1.49034  15.51916  1.000 35.26564  ? 47  PHE A C     1 
ATOM   358  O O     . PHE A 1 53  ? 7.60145   -1.85589  14.34688  1.000 36.49638  ? 47  PHE A O     1 
ATOM   359  C CB    . PHE A 1 53  ? 9.40193   -1.80418  17.07290  1.000 33.84453  ? 47  PHE A CB    1 
ATOM   360  C CG    . PHE A 1 53  ? 9.74053   -3.06784  16.33168  1.000 34.92312  ? 47  PHE A CG    1 
ATOM   361  C CD1   . PHE A 1 53  ? 10.86990  -3.13449  15.53388  1.000 33.18152  ? 47  PHE A CD1   1 
ATOM   362  C CD2   . PHE A 1 53  ? 8.93514   -4.19181  16.43974  1.000 34.79542  ? 47  PHE A CD2   1 
ATOM   363  C CE1   . PHE A 1 53  ? 11.18706  -4.29535  14.85181  1.000 36.16027  ? 47  PHE A CE1   1 
ATOM   364  C CE2   . PHE A 1 53  ? 9.24639   -5.35440  15.75980  1.000 38.38889  ? 47  PHE A CE2   1 
ATOM   365  C CZ    . PHE A 1 53  ? 10.37362  -5.40660  14.96540  1.000 36.22362  ? 47  PHE A CZ    1 
ATOM   366  N N     . TRP A 1 54  ? 6.32905   -1.67191  16.19957  1.000 36.02798  ? 48  TRP A N     1 
ATOM   367  C CA    . TRP A 1 54  ? 5.20794   -2.40771  15.62446  1.000 34.74215  ? 48  TRP A CA    1 
ATOM   368  C C     . TRP A 1 54  ? 4.41713   -1.55363  14.63883  1.000 40.89357  ? 48  TRP A C     1 
ATOM   369  O O     . TRP A 1 54  ? 4.10536   -2.00175  13.53014  1.000 39.13853  ? 48  TRP A O     1 
ATOM   370  C CB    . TRP A 1 54  ? 4.28867   -2.91512  16.73787  1.000 32.23750  ? 48  TRP A CB    1 
ATOM   371  C CG    . TRP A 1 54  ? 4.93477   -3.89767  17.66592  1.000 36.69334  ? 48  TRP A CG    1 
ATOM   372  C CD1   . TRP A 1 54  ? 5.22310   -3.70978  18.98686  1.000 34.90657  ? 48  TRP A CD1   1 
ATOM   373  C CD2   . TRP A 1 54  ? 5.36676   -5.22575  17.34646  1.000 40.65378  ? 48  TRP A CD2   1 
ATOM   374  N NE1   . TRP A 1 54  ? 5.81144   -4.83617  19.50836  1.000 36.25265  ? 48  TRP A NE1   1 
ATOM   375  C CE2   . TRP A 1 54  ? 5.91086   -5.78172  18.52195  1.000 42.12249  ? 48  TRP A CE2   1 
ATOM   376  C CE3   . TRP A 1 54  ? 5.34874   -5.99766  16.18086  1.000 39.39931  ? 48  TRP A CE3   1 
ATOM   377  C CZ2   . TRP A 1 54  ? 6.43046   -7.07350  18.56566  1.000 43.54586  ? 48  TRP A CZ2   1 
ATOM   378  C CZ3   . TRP A 1 54  ? 5.86619   -7.28034  16.22648  1.000 46.00626  ? 48  TRP A CZ3   1 
ATOM   379  C CH2   . TRP A 1 54  ? 6.39986   -7.80474  17.41047  1.000 44.41283  ? 48  TRP A CH2   1 
ATOM   380  N N     . ASN A 1 55  ? 4.07883   -0.32527  15.02714  1.000 32.08933  ? 49  ASN A N     1 
ATOM   381  C CA    . ASN A 1 55  ? 3.19800   0.53332   14.23536  1.000 35.51371  ? 49  ASN A CA    1 
ATOM   382  C C     . ASN A 1 55  ? 4.03924   1.33198   13.24817  1.000 39.70292  ? 49  ASN A C     1 
ATOM   383  O O     . ASN A 1 55  ? 4.69570   2.30520   13.62214  1.000 40.54385  ? 49  ASN A O     1 
ATOM   384  C CB    . ASN A 1 55  ? 2.39383   1.45680   15.14325  1.000 37.52167  ? 49  ASN A CB    1 
ATOM   385  C CG    . ASN A 1 55  ? 1.26176   0.74026   15.84875  1.000 44.20200  ? 49  ASN A CG    1 
ATOM   386  O OD1   . ASN A 1 55  ? 0.30105   0.30150   15.21828  1.000 45.26904  ? 49  ASN A OD1   1 
ATOM   387  N ND2   . ASN A 1 55  ? 1.37016   0.61696   17.16630  1.000 43.27205  ? 49  ASN A ND2   1 
ATOM   388  N N     . GLN A 1 56  ? 4.00978   0.93064   11.97914  1.000 36.93991  ? 50  GLN A N     1 
ATOM   389  C CA    . GLN A 1 56  ? 4.72141   1.62602   10.91183  1.000 36.37177  ? 50  GLN A CA    1 
ATOM   390  C C     . GLN A 1 56  ? 3.78109   1.93615   9.75535   1.000 33.03981  ? 50  GLN A C     1 
ATOM   391  O O     . GLN A 1 56  ? 4.14492   1.81649   8.58186   1.000 33.34892  ? 50  GLN A O     1 
ATOM   392  C CB    . GLN A 1 56  ? 5.92352   0.81452   10.43193  1.000 37.30244  ? 50  GLN A CB    1 
ATOM   393  C CG    . GLN A 1 56  ? 5.64053   -0.66336  10.22012  1.000 38.51670  ? 50  GLN A CG    1 
ATOM   394  C CD    . GLN A 1 56  ? 6.85494   -1.42225  9.71814   1.000 43.72505  ? 50  GLN A CD    1 
ATOM   395  O OE1   . GLN A 1 56  ? 7.96834   -1.22742  10.20530  1.000 46.95577  ? 50  GLN A OE1   1 
ATOM   396  N NE2   . GLN A 1 56  ? 6.64543   -2.29222  8.73752   1.000 45.69613  ? 50  GLN A NE2   1 
ATOM   397  N N     . TYR A 1 57  ? 2.55576   2.34507   10.07323  1.000 33.54056  ? 51  TYR A N     1 
ATOM   398  C CA    . TYR A 1 57  ? 1.56437   2.67233   9.06235   1.000 28.90272  ? 51  TYR A CA    1 
ATOM   399  C C     . TYR A 1 57  ? 1.83963   4.05165   8.46663   1.000 27.84642  ? 51  TYR A C     1 
ATOM   400  O O     . TYR A 1 57  ? 2.56032   4.85945   9.05804   1.000 27.75976  ? 51  TYR A O     1 
ATOM   401  C CB    . TYR A 1 57  ? 0.16348   2.61298   9.67063   1.000 30.49149  ? 51  TYR A CB    1 
ATOM   402  C CG    . TYR A 1 57  ? -0.06639  3.54820   10.83832  1.000 28.32028  ? 51  TYR A CG    1 
ATOM   403  C CD1   . TYR A 1 57  ? -0.43447  4.87202   10.63327  1.000 29.94936  ? 51  TYR A CD1   1 
ATOM   404  C CD2   . TYR A 1 57  ? 0.07364   3.10332   12.14624  1.000 30.16329  ? 51  TYR A CD2   1 
ATOM   405  C CE1   . TYR A 1 57  ? -0.65113  5.72705   11.69518  1.000 27.43278  ? 51  TYR A CE1   1 
ATOM   406  C CE2   . TYR A 1 57  ? -0.14043  3.95200   13.21617  1.000 31.06989  ? 51  TYR A CE2   1 
ATOM   407  C CZ    . TYR A 1 57  ? -0.50210  5.26241   12.98419  1.000 32.14723  ? 51  TYR A CZ    1 
ATOM   408  O OH    . TYR A 1 57  ? -0.71770  6.11220   14.04396  1.000 35.89579  ? 51  TYR A OH    1 
ATOM   409  N N     . PRO A 1 58  ? 1.28717   4.34327   7.28709   1.000 30.24944  ? 52  PRO A N     1 
ATOM   410  C CA    . PRO A 1 58  ? 1.52900   5.65431   6.66796   1.000 31.01048  ? 52  PRO A CA    1 
ATOM   411  C C     . PRO A 1 58  ? 0.97207   6.78646   7.51917   1.000 25.75079  ? 52  PRO A C     1 
ATOM   412  O O     . PRO A 1 58  ? -0.17823  6.74988   7.96039   1.000 29.36092  ? 52  PRO A O     1 
ATOM   413  C CB    . PRO A 1 58  ? 0.80308   5.55071   5.32078   1.000 32.52221  ? 52  PRO A CB    1 
ATOM   414  C CG    . PRO A 1 58  ? 0.68860   4.08747   5.05828   1.000 33.91420  ? 52  PRO A CG    1 
ATOM   415  C CD    . PRO A 1 58  ? 0.50922   3.45842   6.40217   1.000 29.31178  ? 52  PRO A CD    1 
ATOM   416  N N     . GLY A 1 59  ? 1.80486   7.79631   7.75084   1.000 27.84048  ? 53  GLY A N     1 
ATOM   417  C CA    . GLY A 1 59  ? 1.40475   8.95879   8.51421   1.000 28.33834  ? 53  GLY A CA    1 
ATOM   418  C C     . GLY A 1 59  ? 1.53396   8.83459   10.01501  1.000 28.10564  ? 53  GLY A C     1 
ATOM   419  O O     . GLY A 1 59  ? 1.07376   9.73219   10.73123  1.000 27.70609  ? 53  GLY A O     1 
ATOM   420  N N     . ALA A 1 60  ? 2.13594   7.75673   10.51500  1.000 23.96133  ? 54  ALA A N     1 
ATOM   421  C CA    . ALA A 1 60  ? 2.33313   7.59930   11.95122  1.000 28.19680  ? 54  ALA A CA    1 
ATOM   422  C C     . ALA A 1 60  ? 3.13877   8.76819   12.50064  1.000 28.21948  ? 54  ALA A C     1 
ATOM   423  O O     . ALA A 1 60  ? 4.27555   9.00396   12.08026  1.000 31.93642  ? 54  ALA A O     1 
ATOM   424  C CB    . ALA A 1 60  ? 3.03685   6.27590   12.24513  1.000 23.94305  ? 54  ALA A CB    1 
ATOM   425  N N     . LEU A 1 61  ? 2.54295   9.50401   13.43572  1.000 29.25518  ? 55  LEU A N     1 
ATOM   426  C CA    . LEU A 1 61  ? 3.13154   10.73729  13.93298  1.000 34.06502  ? 55  LEU A CA    1 
ATOM   427  C C     . LEU A 1 61  ? 2.75720   10.91219  15.39706  1.000 31.99329  ? 55  LEU A C     1 
ATOM   428  O O     . LEU A 1 61  ? 1.68597   10.48325  15.83402  1.000 33.34765  ? 55  LEU A O     1 
ATOM   429  C CB    . LEU A 1 61  ? 2.66268   11.94160  13.10541  1.000 28.71806  ? 55  LEU A CB    1 
ATOM   430  C CG    . LEU A 1 61  ? 3.35968   13.28487  13.32161  1.000 26.53282  ? 55  LEU A CG    1 
ATOM   431  C CD1   . LEU A 1 61  ? 4.76499   13.24940  12.75369  1.000 26.64965  ? 55  LEU A CD1   1 
ATOM   432  C CD2   . LEU A 1 61  ? 2.55409   14.40599  12.68356  1.000 27.43075  ? 55  LEU A CD2   1 
ATOM   433  N N     . SER A 1 62  ? 3.65082   11.54816  16.14951  1.000 28.99067  ? 56  SER A N     1 
ATOM   434  C CA    . SER A 1 62  ? 3.42388   11.74538  17.57305  1.000 34.19536  ? 56  SER A CA    1 
ATOM   435  C C     . SER A 1 62  ? 2.37463   12.82574  17.81415  1.000 28.04947  ? 56  SER A C     1 
ATOM   436  O O     . SER A 1 62  ? 2.17769   13.72971  16.99812  1.000 32.10971  ? 56  SER A O     1 
ATOM   437  C CB    . SER A 1 62  ? 4.72835   12.12434  18.27474  1.000 33.94496  ? 56  SER A CB    1 
ATOM   438  O OG    . SER A 1 62  ? 5.19023   13.39337  17.84347  1.000 30.33176  ? 56  SER A OG    1 
ATOM   439  N N     . ASP A 1 63  ? 1.69223   12.71784  18.95587  1.000 37.06094  ? 57  ASP A N     1 
ATOM   440  C CA    . ASP A 1 63  ? 0.74289   13.74779  19.36475  1.000 41.33742  ? 57  ASP A CA    1 
ATOM   441  C C     . ASP A 1 63  ? 1.45386   14.91756  20.03396  1.000 37.91525  ? 57  ASP A C     1 
ATOM   442  O O     . ASP A 1 63  ? 1.03318   16.07008  19.88594  1.000 41.02260  ? 57  ASP A O     1 
ATOM   443  C CB    . ASP A 1 63  ? -0.30313  13.14852  20.30746  1.000 41.41690  ? 57  ASP A CB    1 
ATOM   444  C CG    . ASP A 1 63  ? -1.53399  14.02105  20.45200  1.000 51.23049  ? 57  ASP A CG    1 
ATOM   445  O OD1   . ASP A 1 63  ? -1.41504  15.14097  20.99009  1.000 58.46080  ? 57  ASP A OD1   1 
ATOM   446  O OD2   . ASP A 1 63  ? -2.62505  13.58140  20.03386  1.000 62.11060  ? 57  ASP A OD2   1 
ATOM   447  N N     . SER A 1 64  ? 2.52516   14.64146  20.77181  1.000 32.29281  ? 58  SER A N     1 
ATOM   448  C CA    . SER A 1 64  ? 3.29674   15.68122  21.43394  1.000 34.61388  ? 58  SER A CA    1 
ATOM   449  C C     . SER A 1 64  ? 4.46630   16.11558  20.56015  1.000 30.13011  ? 58  SER A C     1 
ATOM   450  O O     . SER A 1 64  ? 4.95306   15.35934  19.71512  1.000 26.66420  ? 58  SER A O     1 
ATOM   451  C CB    . SER A 1 64  ? 3.81136   15.19609  22.78998  1.000 37.12042  ? 58  SER A CB    1 
ATOM   452  O OG    . SER A 1 64  ? 4.41419   13.92107  22.67744  1.000 39.88961  ? 58  SER A OG    1 
ATOM   453  N N     . GLU A 1 65  ? 4.91695   17.34797  20.77832  1.000 29.17347  ? 59  GLU A N     1 
ATOM   454  C CA    . GLU A 1 65  ? 5.98893   17.90760  19.97070  1.000 26.48204  ? 59  GLU A CA    1 
ATOM   455  C C     . GLU A 1 65  ? 7.29104   17.14002  20.19534  1.000 28.68438  ? 59  GLU A C     1 
ATOM   456  O O     . GLU A 1 65  ? 7.48480   16.47148  21.21480  1.000 26.61360  ? 59  GLU A O     1 
ATOM   457  C CB    . GLU A 1 65  ? 6.16609   19.39247  20.28703  1.000 26.78565  ? 59  GLU A CB    1 
ATOM   458  C CG    . GLU A 1 65  ? 4.96146   20.23725  19.88238  1.000 25.84638  ? 59  GLU A CG    1 
ATOM   459  C CD    . GLU A 1 65  ? 5.01040   21.64627  20.43773  1.000 34.87504  ? 59  GLU A CD    1 
ATOM   460  O OE1   . GLU A 1 65  ? 6.07620   22.29002  20.34397  1.000 35.79063  ? 59  GLU A OE1   1 
ATOM   461  O OE2   . GLU A 1 65  ? 3.97937   22.10967  20.96963  1.000 37.29213  ? 59  GLU A OE2   1 
ATOM   462  N N     . THR A 1 66  ? 8.19157   17.24872  19.21277  1.000 26.33899  ? 60  THR A N     1 
ATOM   463  C CA    . THR A 1 66  ? 9.39691   16.42236  19.19556  1.000 27.71473  ? 60  THR A CA    1 
ATOM   464  C C     . THR A 1 66  ? 10.25128  16.63730  20.43842  1.000 28.09398  ? 60  THR A C     1 
ATOM   465  O O     . THR A 1 66  ? 10.73951  15.67180  21.03759  1.000 31.34736  ? 60  THR A O     1 
ATOM   466  C CB    . THR A 1 66  ? 10.21726  16.71624  17.93890  1.000 27.88344  ? 60  THR A CB    1 
ATOM   467  O OG1   . THR A 1 66  ? 9.42036   16.46984  16.77563  1.000 27.61565  ? 60  THR A OG1   1 
ATOM   468  C CG2   . THR A 1 66  ? 11.45802  15.83493  17.89045  1.000 30.09487  ? 60  THR A CG2   1 
ATOM   469  N N     . HIS A 1 67  ? 10.44347  17.89389  20.84371  1.000 28.45105  ? 61  HIS A N     1 
ATOM   470  C CA    . HIS A 1 67  ? 11.33928  18.19059  21.95574  1.000 31.48563  ? 61  HIS A CA    1 
ATOM   471  C C     . HIS A 1 67  ? 10.80659  17.70844  23.29901  1.000 32.24744  ? 61  HIS A C     1 
ATOM   472  O O     . HIS A 1 67  ? 11.54130  17.76624  24.29088  1.000 31.02247  ? 61  HIS A O     1 
ATOM   473  C CB    . HIS A 1 67  ? 11.62055  19.69440  22.01667  1.000 32.27192  ? 61  HIS A CB    1 
ATOM   474  C CG    . HIS A 1 67  ? 10.43711  20.51870  22.41755  1.000 32.87182  ? 61  HIS A CG    1 
ATOM   475  N ND1   . HIS A 1 67  ? 9.40654   20.81274  21.55100  1.000 32.33094  ? 61  HIS A ND1   1 
ATOM   476  C CD2   . HIS A 1 67  ? 10.12589  21.12050  23.58992  1.000 33.71317  ? 61  HIS A CD2   1 
ATOM   477  C CE1   . HIS A 1 67  ? 8.50844   21.55491  22.17393  1.000 32.86225  ? 61  HIS A CE1   1 
ATOM   478  N NE2   . HIS A 1 67  ? 8.92103   21.75604  23.41248  1.000 33.76018  ? 61  HIS A NE2   1 
ATOM   479  N N     . LEU A 1 68  ? 9.56197   17.23218  23.35797  1.000 29.72632  ? 62  LEU A N     1 
ATOM   480  C CA    . LEU A 1 68  ? 8.98284   16.72468  24.59213  1.000 29.10800  ? 62  LEU A CA    1 
ATOM   481  C C     . LEU A 1 68  ? 8.63924   15.24460  24.55392  1.000 28.58568  ? 62  LEU A C     1 
ATOM   482  O O     . LEU A 1 68  ? 8.45868   14.64803  25.62084  1.000 31.34605  ? 62  LEU A O     1 
ATOM   483  C CB    . LEU A 1 68  ? 7.71477   17.51289  24.95473  1.000 31.44313  ? 62  LEU A CB    1 
ATOM   484  C CG    . LEU A 1 68  ? 7.95696   18.98425  25.28643  1.000 38.14618  ? 62  LEU A CG    1 
ATOM   485  C CD1   . LEU A 1 68  ? 6.64610   19.70281  25.52494  1.000 40.65256  ? 62  LEU A CD1   1 
ATOM   486  C CD2   . LEU A 1 68  ? 8.86603   19.10239  26.49704  1.000 33.53148  ? 62  LEU A CD2   1 
ATOM   487  N N     . TYR A 1 69  ? 8.54112   14.63734  23.37260  1.000 26.01618  ? 63  TYR A N     1 
ATOM   488  C CA    . TYR A 1 69  ? 8.26435   13.20493  23.26279  1.000 26.61720  ? 63  TYR A CA    1 
ATOM   489  C C     . TYR A 1 69  ? 9.58578   12.43568  23.26187  1.000 29.43000  ? 63  TYR A C     1 
ATOM   490  O O     . TYR A 1 69  ? 10.00496  11.83578  22.27023  1.000 32.76770  ? 63  TYR A O     1 
ATOM   491  C CB    . TYR A 1 69  ? 7.44116   12.91306  22.01551  1.000 31.87197  ? 63  TYR A CB    1 
ATOM   492  C CG    . TYR A 1 69  ? 6.84732   11.52509  22.00669  1.000 33.33379  ? 63  TYR A CG    1 
ATOM   493  C CD1   . TYR A 1 69  ? 5.84451   11.17431  22.89993  1.000 30.75113  ? 63  TYR A CD1   1 
ATOM   494  C CD2   . TYR A 1 69  ? 7.30134   10.56028  21.11841  1.000 28.78157  ? 63  TYR A CD2   1 
ATOM   495  C CE1   . TYR A 1 69  ? 5.30239   9.90607   22.90250  1.000 31.12930  ? 63  TYR A CE1   1 
ATOM   496  C CE2   . TYR A 1 69  ? 6.76676   9.28727   21.11496  1.000 29.09024  ? 63  TYR A CE2   1 
ATOM   497  C CZ    . TYR A 1 69  ? 5.76622   8.96564   22.00784  1.000 32.91772  ? 63  TYR A CZ    1 
ATOM   498  O OH    . TYR A 1 69  ? 5.22779   7.69955   22.00839  1.000 33.65308  ? 63  TYR A OH    1 
ATOM   499  N N     . CYS A 1 70  ? 10.24251  12.46297  24.41556  1.000 29.08907  ? 64  CYS A N     1 
ATOM   500  C CA    . CYS A 1 70  ? 11.57189  11.88243  24.56766  1.000 28.14587  ? 64  CYS A CA    1 
ATOM   501  C C     . CYS A 1 70  ? 11.87065  11.76210  26.05665  1.000 31.49133  ? 64  CYS A C     1 
ATOM   502  O O     . CYS A 1 70  ? 11.08420  12.19099  26.90686  1.000 31.20963  ? 64  CYS A O     1 
ATOM   503  C CB    . CYS A 1 70  ? 12.62813  12.73132  23.86001  1.000 30.28550  ? 64  CYS A CB    1 
ATOM   504  S SG    . CYS A 1 70  ? 12.69932  14.43786  24.45491  1.000 35.63920  ? 64  CYS A SG    1 
ATOM   505  N N     . TYR A 1 71  ? 13.02335  11.17705  26.36436  1.000 29.96761  ? 65  TYR A N     1 
ATOM   506  C CA    . TYR A 1 71  ? 13.47775  11.08170  27.74113  1.000 31.11532  ? 65  TYR A CA    1 
ATOM   507  C C     . TYR A 1 71  ? 14.02283  12.42229  28.21700  1.000 32.50792  ? 65  TYR A C     1 
ATOM   508  O O     . TYR A 1 71  ? 14.53107  13.22713  27.43135  1.000 34.01026  ? 65  TYR A O     1 
ATOM   509  C CB    . TYR A 1 71  ? 14.55838  10.01004  27.88214  1.000 31.76383  ? 65  TYR A CB    1 
ATOM   510  C CG    . TYR A 1 71  ? 14.05492  8.59246   27.74246  1.000 30.70480  ? 65  TYR A CG    1 
ATOM   511  C CD1   . TYR A 1 71  ? 13.05112  8.10552   28.56850  1.000 32.74116  ? 65  TYR A CD1   1 
ATOM   512  C CD2   . TYR A 1 71  ? 14.59230  7.73732   26.79044  1.000 31.56287  ? 65  TYR A CD2   1 
ATOM   513  C CE1   . TYR A 1 71  ? 12.59399  6.80703   28.44691  1.000 34.96069  ? 65  TYR A CE1   1 
ATOM   514  C CE2   . TYR A 1 71  ? 14.14122  6.43810   26.66109  1.000 33.86627  ? 65  TYR A CE2   1 
ATOM   515  C CZ    . TYR A 1 71  ? 13.14234  5.97836   27.49141  1.000 31.38629  ? 65  TYR A CZ    1 
ATOM   516  O OH    . TYR A 1 71  ? 12.69116  4.68458   27.36489  1.000 31.83695  ? 65  TYR A OH    1 
ATOM   517  N N     . SER A 1 72  ? 13.91440  12.65425  29.52415  1.000 36.80720  ? 66  SER A N     1 
ATOM   518  C CA    . SER A 1 72  ? 14.43973  13.85915  30.14519  1.000 37.91815  ? 66  SER A CA    1 
ATOM   519  C C     . SER A 1 72  ? 15.56258  13.59468  31.13569  1.000 38.71388  ? 66  SER A C     1 
ATOM   520  O O     . SER A 1 72  ? 16.16023  14.55616  31.63237  1.000 36.56042  ? 66  SER A O     1 
ATOM   521  C CB    . SER A 1 72  ? 13.32033  14.62450  30.86756  1.000 33.73030  ? 66  SER A CB    1 
ATOM   522  O OG    . SER A 1 72  ? 13.14143  14.13723  32.18484  1.000 34.17930  ? 66  SER A OG    1 
ATOM   523  N N     . TRP A 1 73  ? 15.87245  12.33188  31.43132  1.000 37.41965  ? 67  TRP A N     1 
ATOM   524  C CA    . TRP A 1 73  ? 16.85121  12.00018  32.45821  1.000 40.75016  ? 67  TRP A CA    1 
ATOM   525  C C     . TRP A 1 73  ? 18.28979  12.05039  31.96088  1.000 39.39444  ? 67  TRP A C     1 
ATOM   526  O O     . TRP A 1 73  ? 19.20850  12.05460  32.78663  1.000 40.04576  ? 67  TRP A O     1 
ATOM   527  C CB    . TRP A 1 73  ? 16.55283  10.61205  33.03218  1.000 39.49433  ? 67  TRP A CB    1 
ATOM   528  C CG    . TRP A 1 73  ? 16.45930  9.53429   31.99457  1.000 37.71364  ? 67  TRP A CG    1 
ATOM   529  C CD1   . TRP A 1 73  ? 15.33127  9.10754   31.35474  1.000 35.03467  ? 67  TRP A CD1   1 
ATOM   530  C CD2   . TRP A 1 73  ? 17.53509  8.73693   31.48489  1.000 40.35453  ? 67  TRP A CD2   1 
ATOM   531  N NE1   . TRP A 1 73  ? 15.63922  8.09868   30.47421  1.000 31.33180  ? 67  TRP A NE1   1 
ATOM   532  C CE2   . TRP A 1 73  ? 16.98537  7.85207   30.53512  1.000 36.38358  ? 67  TRP A CE2   1 
ATOM   533  C CE3   . TRP A 1 73  ? 18.90979  8.68742   31.73687  1.000 39.40484  ? 67  TRP A CE3   1 
ATOM   534  C CZ2   . TRP A 1 73  ? 17.76158  6.92864   29.83767  1.000 36.90033  ? 67  TRP A CZ2   1 
ATOM   535  C CZ3   . TRP A 1 73  ? 19.67873  7.76958   31.04340  1.000 39.19349  ? 67  TRP A CZ3   1 
ATOM   536  C CH2   . TRP A 1 73  ? 19.10243  6.90271   30.10547  1.000 37.87782  ? 67  TRP A CH2   1 
ATOM   537  N N     . ASP A 1 74  ? 18.51119  12.08670  30.64959  1.000 37.42723  ? 68  ASP A N     1 
ATOM   538  C CA    . ASP A 1 74  ? 19.85135  12.15616  30.07042  1.000 39.23152  ? 68  ASP A CA    1 
ATOM   539  C C     . ASP A 1 74  ? 20.01541  13.54471  29.45853  1.000 42.09158  ? 68  ASP A C     1 
ATOM   540  O O     . ASP A 1 74  ? 19.55456  13.80007  28.34189  1.000 38.76263  ? 68  ASP A O     1 
ATOM   541  C CB    . ASP A 1 74  ? 20.05583  11.05024  29.03728  1.000 38.94342  ? 68  ASP A CB    1 
ATOM   542  C CG    . ASP A 1 74  ? 21.50689  10.90654  28.60437  1.000 38.83703  ? 68  ASP A CG    1 
ATOM   543  O OD1   . ASP A 1 74  ? 22.28869  11.86778  28.76211  1.000 43.11382  ? 68  ASP A OD1   1 
ATOM   544  O OD2   . ASP A 1 74  ? 21.86755  9.82110   28.10380  1.000 40.62960  ? 68  ASP A OD2   1 
ATOM   545  N N     . LYS A 1 75  ? 20.68001  14.43890  30.19646  1.000 40.35486  ? 69  LYS A N     1 
ATOM   546  C CA    . LYS A 1 75  ? 20.85886  15.80779  29.72239  1.000 41.36043  ? 69  LYS A CA    1 
ATOM   547  C C     . LYS A 1 75  ? 21.71887  15.86276  28.46707  1.000 40.83993  ? 69  LYS A C     1 
ATOM   548  O O     . LYS A 1 75  ? 21.49515  16.71505  27.59943  1.000 40.92761  ? 69  LYS A O     1 
ATOM   549  C CB    . LYS A 1 75  ? 21.47653  16.66872  30.82479  1.000 41.91413  ? 69  LYS A CB    1 
ATOM   550  C CG    . LYS A 1 75  ? 20.87330  16.44237  32.20170  1.000 47.53156  ? 69  LYS A CG    1 
ATOM   551  C CD    . LYS A 1 75  ? 19.63507  17.29874  32.40662  1.000 52.42411  ? 69  LYS A CD    1 
ATOM   552  C CE    . LYS A 1 75  ? 19.94984  18.53436  33.23335  1.000 49.46039  ? 69  LYS A CE    1 
ATOM   553  N NZ    . LYS A 1 75  ? 18.87791  18.82198  34.22539  1.000 56.73780  ? 69  LYS A NZ    1 
ATOM   554  N N     . GLU A 1 76  ? 22.70514  14.97025  28.35238  1.000 38.06683  ? 70  GLU A N     1 
ATOM   555  C CA    . GLU A 1 76  ? 23.54411  14.94746  27.15861  1.000 38.71080  ? 70  GLU A CA    1 
ATOM   556  C C     . GLU A 1 76  ? 22.74748  14.51367  25.93471  1.000 45.02302  ? 70  GLU A C     1 
ATOM   557  O O     . GLU A 1 76  ? 22.94658  15.04531  24.83600  1.000 39.13472  ? 70  GLU A O     1 
ATOM   558  C CB    . GLU A 1 76  ? 24.74196  14.02294  27.37563  1.000 39.92138  ? 70  GLU A CB    1 
ATOM   559  C CG    . GLU A 1 76  ? 25.91198  14.67620  28.09385  1.000 54.18763  ? 70  GLU A CG    1 
ATOM   560  C CD    . GLU A 1 76  ? 25.62223  14.94064  29.55789  1.000 56.54062  ? 70  GLU A CD    1 
ATOM   561  O OE1   . GLU A 1 76  ? 25.05402  14.04986  30.22348  1.000 54.37574  ? 70  GLU A OE1   1 
ATOM   562  O OE2   . GLU A 1 76  ? 25.96139  16.03975  30.04352  1.000 61.92460  ? 70  GLU A OE2   1 
ATOM   563  N N     . LEU A 1 77  ? 21.84170  13.54768  26.10555  1.000 40.29359  ? 71  LEU A N     1 
ATOM   564  C CA    . LEU A 1 77  ? 20.99800  13.11794  24.99624  1.000 42.56124  ? 71  LEU A CA    1 
ATOM   565  C C     . LEU A 1 77  ? 20.06995  14.23392  24.53662  1.000 37.40854  ? 71  LEU A C     1 
ATOM   566  O O     . LEU A 1 77  ? 19.76266  14.33320  23.34316  1.000 38.61488  ? 71  LEU A O     1 
ATOM   567  C CB    . LEU A 1 77  ? 20.18869  11.88664  25.40312  1.000 40.89214  ? 71  LEU A CB    1 
ATOM   568  C CG    . LEU A 1 77  ? 19.57453  11.04896  24.28057  1.000 45.03205  ? 71  LEU A CG    1 
ATOM   569  C CD1   . LEU A 1 77  ? 20.55327  10.88019  23.12964  1.000 45.91006  ? 71  LEU A CD1   1 
ATOM   570  C CD2   . LEU A 1 77  ? 19.13954  9.69686   24.81930  1.000 49.03619  ? 71  LEU A CD2   1 
ATOM   571  N N     . LEU A 1 78  ? 19.61664  15.08037  25.46429  1.000 32.26730  ? 72  LEU A N     1 
ATOM   572  C CA    . LEU A 1 78  ? 18.76232  16.20438  25.09410  1.000 34.67073  ? 72  LEU A CA    1 
ATOM   573  C C     . LEU A 1 78  ? 19.50058  17.17180  24.17663  1.000 36.39159  ? 72  LEU A C     1 
ATOM   574  O O     . LEU A 1 78  ? 18.95920  17.61769  23.15844  1.000 32.91643  ? 72  LEU A O     1 
ATOM   575  C CB    . LEU A 1 78  ? 18.26993  16.92117  26.35215  1.000 35.56545  ? 72  LEU A CB    1 
ATOM   576  C CG    . LEU A 1 78  ? 17.21778  16.19419  27.19323  1.000 36.41240  ? 72  LEU A CG    1 
ATOM   577  C CD1   . LEU A 1 78  ? 17.00119  16.90814  28.51831  1.000 35.08593  ? 72  LEU A CD1   1 
ATOM   578  C CD2   . LEU A 1 78  ? 15.90879  16.07244  26.42704  1.000 36.10632  ? 72  LEU A CD2   1 
ATOM   579  N N     . GLN A 1 79  ? 20.74710  17.50506  24.52277  1.000 37.45753  ? 73  GLN A N     1 
ATOM   580  C CA    . GLN A 1 79  ? 21.54041  18.39509  23.68131  1.000 37.21265  ? 73  GLN A CA    1 
ATOM   581  C C     . GLN A 1 79  ? 21.89578  17.74223  22.35144  1.000 39.05316  ? 73  GLN A C     1 
ATOM   582  O O     . GLN A 1 79  ? 22.01628  18.43356  21.33338  1.000 35.36684  ? 73  GLN A O     1 
ATOM   583  C CB    . GLN A 1 79  ? 22.81078  18.81573  24.42090  1.000 42.03182  ? 73  GLN A CB    1 
ATOM   584  C CG    . GLN A 1 79  ? 22.55789  19.60952  25.69335  1.000 38.79027  ? 73  GLN A CG    1 
ATOM   585  C CD    . GLN A 1 79  ? 21.78279  20.88564  25.43864  1.000 39.49500  ? 73  GLN A CD    1 
ATOM   586  O OE1   . GLN A 1 79  ? 22.04258  21.59924  24.47012  1.000 41.93460  ? 73  GLN A OE1   1 
ATOM   587  N NE2   . GLN A 1 79  ? 20.82397  21.18028  26.30886  1.000 37.79530  ? 73  GLN A NE2   1 
ATOM   588  N N     . GLU A 1 80  ? 22.06276  16.42026  22.34219  1.000 31.43032  ? 74  GLU A N     1 
ATOM   589  C CA    . GLU A 1 80  ? 22.41987  15.67114  21.14503  1.000 36.47190  ? 74  GLU A CA    1 
ATOM   590  C C     . GLU A 1 80  ? 21.22166  15.36900  20.25297  1.000 40.82597  ? 74  GLU A C     1 
ATOM   591  O O     . GLU A 1 80  ? 21.41155  14.95559  19.10386  1.000 43.36683  ? 74  GLU A O     1 
ATOM   592  C CB    . GLU A 1 80  ? 23.10099  14.36127  21.55734  1.000 42.21265  ? 74  GLU A CB    1 
ATOM   593  C CG    . GLU A 1 80  ? 23.84780  13.63094  20.45515  1.000 46.73020  ? 74  GLU A CG    1 
ATOM   594  C CD    . GLU A 1 80  ? 24.36649  12.28160  20.91242  1.000 58.61920  ? 74  GLU A CD    1 
ATOM   595  O OE1   . GLU A 1 80  ? 25.09503  12.23632  21.92539  1.000 64.07675  ? 74  GLU A OE1   1 
ATOM   596  O OE2   . GLU A 1 80  ? 24.04145  11.26561  20.26314  1.000 62.59379  ? 74  GLU A OE2   1 
ATOM   597  N N     . MET A 1 81  ? 20.00462  15.58784  20.74185  1.000 39.18117  ? 75  MET A N     1 
ATOM   598  C CA    . MET A 1 81  ? 18.81582  15.07017  20.07863  1.000 42.59918  ? 75  MET A CA    1 
ATOM   599  C C     . MET A 1 81  ? 18.54411  15.77918  18.75726  1.000 39.15970  ? 75  MET A C     1 
ATOM   600  O O     . MET A 1 81  ? 18.73912  16.99094  18.62607  1.000 39.19999  ? 75  MET A O     1 
ATOM   601  C CB    . MET A 1 81  ? 17.60415  15.21092  20.99589  1.000 39.65513  ? 75  MET A CB    1 
ATOM   602  C CG    . MET A 1 81  ? 16.72031  13.98271  21.03685  1.000 36.82508  ? 75  MET A CG    1 
ATOM   603  S SD    . MET A 1 81  ? 15.22228  14.28002  21.98274  1.000 44.06947  ? 75  MET A SD    1 
ATOM   604  C CE    . MET A 1 81  ? 14.45832  15.57045  21.00315  1.000 37.22632  ? 75  MET A CE    1 
ATOM   605  N N     . GLU A 1 82  ? 18.07906  15.00730  17.77713  1.000 37.60423  ? 76  GLU A N     1 
ATOM   606  C CA    . GLU A 1 82  ? 17.65147  15.55299  16.49586  1.000 34.33686  ? 76  GLU A CA    1 
ATOM   607  C C     . GLU A 1 82  ? 16.22140  16.06436  16.61780  1.000 37.50286  ? 76  GLU A C     1 
ATOM   608  O O     . GLU A 1 82  ? 15.31225  15.30476  16.97043  1.000 33.69034  ? 76  GLU A O     1 
ATOM   609  C CB    . GLU A 1 82  ? 17.74738  14.49025  15.40259  1.000 37.06378  ? 76  GLU A CB    1 
ATOM   610  C CG    . GLU A 1 82  ? 17.06419  14.87697  14.09658  1.000 42.87526  ? 76  GLU A CG    1 
ATOM   611  C CD    . GLU A 1 82  ? 16.57585  13.67548  13.30739  1.000 52.98762  ? 76  GLU A CD    1 
ATOM   612  O OE1   . GLU A 1 82  ? 15.54920  13.08046  13.69788  1.000 47.15972  ? 76  GLU A OE1   1 
ATOM   613  O OE2   . GLU A 1 82  ? 17.21577  13.32746  12.29404  1.000 50.44352  ? 76  GLU A OE2   1 
ATOM   614  N N     . ILE A 1 83  ? 16.02411  17.35055  16.33629  1.000 32.42938  ? 77  ILE A N     1 
ATOM   615  C CA    . ILE A 1 83  ? 14.69077  17.93982  16.31268  1.000 30.07993  ? 77  ILE A CA    1 
ATOM   616  C C     . ILE A 1 83  ? 14.41897  18.41746  14.89221  1.000 31.84303  ? 77  ILE A C     1 
ATOM   617  O O     . ILE A 1 83  ? 14.55540  19.60636  14.58090  1.000 34.49081  ? 77  ILE A O     1 
ATOM   618  C CB    . ILE A 1 83  ? 14.55953  19.07999  17.33911  1.000 32.18706  ? 77  ILE A CB    1 
ATOM   619  C CG1   . ILE A 1 83  ? 14.99197  18.59274  18.72518  1.000 28.09824  ? 77  ILE A CG1   1 
ATOM   620  C CG2   . ILE A 1 83  ? 13.12774  19.59733  17.39083  1.000 30.66848  ? 77  ILE A CG2   1 
ATOM   621  C CD1   . ILE A 1 83  ? 14.76905  19.60045  19.83038  1.000 34.47761  ? 77  ILE A CD1   1 
ATOM   622  N N     . LYS A 1 84  ? 14.04174  17.48206  14.01980  1.000 25.75749  ? 78  LYS A N     1 
ATOM   623  C CA    . LYS A 1 84  ? 13.90680  17.77447  12.59734  1.000 31.67690  ? 78  LYS A CA    1 
ATOM   624  C C     . LYS A 1 84  ? 12.63539  18.56213  12.30423  1.000 32.95352  ? 78  LYS A C     1 
ATOM   625  O O     . LYS A 1 84  ? 12.67436  19.58295  11.60856  1.000 27.59391  ? 78  LYS A O     1 
ATOM   626  C CB    . LYS A 1 84  ? 13.92903  16.46837  11.80169  1.000 34.91007  ? 78  LYS A CB    1 
ATOM   627  C CG    . LYS A 1 84  ? 13.80396  16.63556  10.29797  1.000 36.63512  ? 78  LYS A CG    1 
ATOM   628  C CD    . LYS A 1 84  ? 14.22693  15.36627  9.56726   1.000 45.46176  ? 78  LYS A CD    1 
ATOM   629  C CE    . LYS A 1 84  ? 13.80156  14.11640  10.32648  1.000 44.59132  ? 78  LYS A CE    1 
ATOM   630  N NZ    . LYS A 1 84  ? 14.21049  12.86203  9.63434   1.000 43.05177  ? 78  LYS A NZ    1 
ATOM   631  N N     . ARG A 1 85  ? 11.50057  18.09977  12.81986  1.000 31.04894  ? 79  ARG A N     1 
ATOM   632  C CA    . ARG A 1 85  ? 10.22128  18.75954  12.61831  1.000 27.69163  ? 79  ARG A CA    1 
ATOM   633  C C     . ARG A 1 85  ? 9.54870   18.96126  13.96924  1.000 25.35865  ? 79  ARG A C     1 
ATOM   634  O O     . ARG A 1 85  ? 9.96735   18.40008  14.98561  1.000 27.19780  ? 79  ARG A O     1 
ATOM   635  C CB    . ARG A 1 85  ? 9.32249   17.95476  11.66752  1.000 27.17603  ? 79  ARG A CB    1 
ATOM   636  C CG    . ARG A 1 85  ? 9.54146   18.28926  10.19790  1.000 27.52376  ? 79  ARG A CG    1 
ATOM   637  C CD    . ARG A 1 85  ? 8.89942   17.26719  9.27296   1.000 33.95782  ? 79  ARG A CD    1 
ATOM   638  N NE    . ARG A 1 85  ? 9.18792   15.89601  9.67570   1.000 40.69926  ? 79  ARG A NE    1 
ATOM   639  C CZ    . ARG A 1 85  ? 9.86359   15.02571  8.93780   1.000 44.06559  ? 79  ARG A CZ    1 
ATOM   640  N NH1   . ARG A 1 85  ? 10.35556  15.35710  7.75491   1.000 32.34816  ? 79  ARG A NH1   1 
ATOM   641  N NH2   . ARG A 1 85  ? 10.05189  13.79230  9.39895   1.000 39.07378  ? 79  ARG A NH2   1 
ATOM   642  N N     . LYS A 1 86  ? 8.49862   19.78828  13.97217  1.000 26.84584  ? 80  LYS A N     1 
ATOM   643  C CA    . LYS A 1 86  ? 7.81029   20.10989  15.21965  1.000 25.12740  ? 80  LYS A CA    1 
ATOM   644  C C     . LYS A 1 86  ? 7.27234   18.85453  15.89279  1.000 26.80390  ? 80  LYS A C     1 
ATOM   645  O O     . LYS A 1 86  ? 7.26749   18.75413  17.12496  1.000 27.05765  ? 80  LYS A O     1 
ATOM   646  C CB    . LYS A 1 86  ? 6.67991   21.10420  14.95565  1.000 28.23472  ? 80  LYS A CB    1 
ATOM   647  C CG    . LYS A 1 86  ? 6.10817   21.73923  16.21294  1.000 29.37069  ? 80  LYS A CG    1 
ATOM   648  C CD    . LYS A 1 86  ? 5.33895   23.00977  15.88596  1.000 34.46868  ? 80  LYS A CD    1 
ATOM   649  C CE    . LYS A 1 86  ? 4.87271   23.71501  17.14955  1.000 41.17482  ? 80  LYS A CE    1 
ATOM   650  N NZ    . LYS A 1 86  ? 4.53573   25.14266  16.89132  1.000 45.67663  ? 80  LYS A NZ    1 
ATOM   651  N N     . TYR A 1 87  ? 6.81577   17.89000  15.10151  1.000 26.93927  ? 81  TYR A N     1 
ATOM   652  C CA    . TYR A 1 87  ? 6.40641   16.58625  15.59326  1.000 25.20781  ? 81  TYR A CA    1 
ATOM   653  C C     . TYR A 1 87  ? 7.25875   15.52239  14.91638  1.000 26.14292  ? 81  TYR A C     1 
ATOM   654  O O     . TYR A 1 87  ? 7.81181   15.73700  13.83447  1.000 31.39268  ? 81  TYR A O     1 
ATOM   655  C CB    . TYR A 1 87  ? 4.91128   16.34232  15.34747  1.000 21.68097  ? 81  TYR A CB    1 
ATOM   656  C CG    . TYR A 1 87  ? 4.03103   17.34643  16.05881  1.000 25.85232  ? 81  TYR A CG    1 
ATOM   657  C CD1   . TYR A 1 87  ? 3.81222   18.60884  15.52321  1.000 25.94279  ? 81  TYR A CD1   1 
ATOM   658  C CD2   . TYR A 1 87  ? 3.43641   17.04048  17.27543  1.000 30.44324  ? 81  TYR A CD2   1 
ATOM   659  C CE1   . TYR A 1 87  ? 3.01911   19.53264  16.17164  1.000 27.20264  ? 81  TYR A CE1   1 
ATOM   660  C CE2   . TYR A 1 87  ? 2.63782   17.96034  17.93152  1.000 28.66115  ? 81  TYR A CE2   1 
ATOM   661  C CZ    . TYR A 1 87  ? 2.43377   19.20425  17.37484  1.000 29.60657  ? 81  TYR A CZ    1 
ATOM   662  O OH    . TYR A 1 87  ? 1.64155   20.12493  18.02228  1.000 36.90149  ? 81  TYR A OH    1 
ATOM   663  N N     . ILE A 1 88  ? 7.38195   14.37444  15.57404  1.000 27.85031  ? 82  ILE A N     1 
ATOM   664  C CA    . ILE A 1 88  ? 8.35415   13.35639  15.19694  1.000 27.44867  ? 82  ILE A CA    1 
ATOM   665  C C     . ILE A 1 88  ? 7.61863   12.16464  14.59799  1.000 30.23958  ? 82  ILE A C     1 
ATOM   666  O O     . ILE A 1 88  ? 6.60471   11.70874  15.14205  1.000 30.91075  ? 82  ILE A O     1 
ATOM   667  C CB    . ILE A 1 88  ? 9.22637   12.94990  16.39951  1.000 25.58500  ? 82  ILE A CB    1 
ATOM   668  C CG1   . ILE A 1 88  ? 10.26742  11.90946  15.98605  1.000 29.38804  ? 82  ILE A CG1   1 
ATOM   669  C CG2   . ILE A 1 88  ? 8.36784   12.47906  17.57024  1.000 26.09293  ? 82  ILE A CG2   1 
ATOM   670  C CD1   . ILE A 1 88  ? 11.37460  11.71401  17.00429  1.000 28.24822  ? 82  ILE A CD1   1 
ATOM   671  N N     . SER A 1 89  ? 8.12030   11.67679  13.46607  1.000 28.10412  ? 83  SER A N     1 
ATOM   672  C CA    . SER A 1 89  ? 7.50870   10.56148  12.76461  1.000 31.17809  ? 83  SER A CA    1 
ATOM   673  C C     . SER A 1 89  ? 7.98544   9.23342   13.34870  1.000 30.96835  ? 83  SER A C     1 
ATOM   674  O O     . SER A 1 89  ? 8.93604   9.16979   14.13291  1.000 29.27926  ? 83  SER A O     1 
ATOM   675  C CB    . SER A 1 89  ? 7.82576   10.63145  11.27154  1.000 32.59148  ? 83  SER A CB    1 
ATOM   676  O OG    . SER A 1 89  ? 7.52356   11.91281  10.74775  1.000 42.60836  ? 83  SER A OG    1 
ATOM   677  N N     . GLN A 1 90  ? 7.30944   8.15787   12.94189  1.000 31.97930  ? 84  GLN A N     1 
ATOM   678  C CA    . GLN A 1 90  ? 7.61521   6.83460   13.48362  1.000 29.85242  ? 84  GLN A CA    1 
ATOM   679  C C     . GLN A 1 90  ? 9.05183   6.39320   13.23132  1.000 31.65417  ? 84  GLN A C     1 
ATOM   680  O O     . GLN A 1 90  ? 9.70027   5.92423   14.18324  1.000 28.53161  ? 84  GLN A O     1 
ATOM   681  C CB    . GLN A 1 90  ? 6.61929   5.80776   12.93391  1.000 31.78967  ? 84  GLN A CB    1 
ATOM   682  C CG    . GLN A 1 90  ? 6.94457   4.37583   13.32126  1.000 32.89573  ? 84  GLN A CG    1 
ATOM   683  C CD    . GLN A 1 90  ? 7.74411   3.64472   12.26087  1.000 35.34480  ? 84  GLN A CD    1 
ATOM   684  O OE1   . GLN A 1 90  ? 7.53771   3.84312   11.06370  1.000 40.49947  ? 84  GLN A OE1   1 
ATOM   685  N NE2   . GLN A 1 90  ? 8.66673   2.79486   12.69757  1.000 32.82991  ? 84  GLN A NE2   1 
ATOM   686  N N     . PRO A 1 91  ? 9.60590   6.48245   12.01422  1.000 29.53790  ? 85  PRO A N     1 
ATOM   687  C CA    . PRO A 1 91  ? 10.99985  6.04266   11.83453  1.000 32.18203  ? 85  PRO A CA    1 
ATOM   688  C C     . PRO A 1 91  ? 11.98767  6.82866   12.67422  1.000 36.26122  ? 85  PRO A C     1 
ATOM   689  O O     . PRO A 1 91  ? 13.04598  6.29568   13.03079  1.000 33.00077  ? 85  PRO A O     1 
ATOM   690  C CB    . PRO A 1 91  ? 11.24735  6.24764   10.33238  1.000 36.89242  ? 85  PRO A CB    1 
ATOM   691  C CG    . PRO A 1 91  ? 9.89585   6.29358   9.71725   1.000 36.91655  ? 85  PRO A CG    1 
ATOM   692  C CD    . PRO A 1 91  ? 9.01503   6.93080   10.73992  1.000 31.98281  ? 85  PRO A CD    1 
ATOM   693  N N     . ASP A 1 92  ? 11.66909  8.07950   13.01320  1.000 31.26825  ? 86  ASP A N     1 
ATOM   694  C CA    . ASP A 1 92  ? 12.57861  8.88580   13.81731  1.000 29.45327  ? 86  ASP A CA    1 
ATOM   695  C C     . ASP A 1 92  ? 12.45883  8.57696   15.30511  1.000 30.68667  ? 86  ASP A C     1 
ATOM   696  O O     . ASP A 1 92  ? 13.45800  8.65890   16.02827  1.000 27.99476  ? 86  ASP A O     1 
ATOM   697  C CB    . ASP A 1 92  ? 12.32875  10.37099  13.55676  1.000 29.32741  ? 86  ASP A CB    1 
ATOM   698  C CG    . ASP A 1 92  ? 12.65521  10.77289  12.13174  1.000 36.22436  ? 86  ASP A CG    1 
ATOM   699  O OD1   . ASP A 1 92  ? 13.51351  10.11234  11.50970  1.000 40.96688  ? 86  ASP A OD1   1 
ATOM   700  O OD2   . ASP A 1 92  ? 12.05201  11.74518  11.63147  1.000 34.57985  ? 86  ASP A OD2   1 
ATOM   701  N N     . VAL A 1 93  ? 11.26052  8.23020   15.78406  1.000 30.70419  ? 87  VAL A N     1 
ATOM   702  C CA    . VAL A 1 93  ? 11.13434  7.76843   17.16360  1.000 30.82141  ? 87  VAL A CA    1 
ATOM   703  C C     . VAL A 1 93  ? 11.86134  6.44435   17.34155  1.000 30.13462  ? 87  VAL A C     1 
ATOM   704  O O     . VAL A 1 93  ? 12.56844  6.23527   18.33488  1.000 31.12582  ? 87  VAL A O     1 
ATOM   705  C CB    . VAL A 1 93  ? 9.65536   7.64500   17.57330  1.000 28.72823  ? 87  VAL A CB    1 
ATOM   706  C CG1   . VAL A 1 93  ? 9.55470   7.25951   19.04214  1.000 32.32597  ? 87  VAL A CG1   1 
ATOM   707  C CG2   . VAL A 1 93  ? 8.91325   8.93530   17.31631  1.000 26.89719  ? 87  VAL A CG2   1 
ATOM   708  N N     . LEU A 1 94  ? 11.69192  5.52732   16.38586  1.000 31.37082  ? 88  LEU A N     1 
ATOM   709  C CA    . LEU A 1 94  ? 12.39116  4.24906   16.44849  1.000 31.44407  ? 88  LEU A CA    1 
ATOM   710  C C     . LEU A 1 94  ? 13.90085  4.45004   16.44599  1.000 34.07649  ? 88  LEU A C     1 
ATOM   711  O O     . LEU A 1 94  ? 14.62159  3.80766   17.21850  1.000 31.73380  ? 88  LEU A O     1 
ATOM   712  C CB    . LEU A 1 94  ? 11.96094  3.36308   15.27913  1.000 30.85025  ? 88  LEU A CB    1 
ATOM   713  C CG    . LEU A 1 94  ? 12.53757  1.94697   15.24229  1.000 30.77305  ? 88  LEU A CG    1 
ATOM   714  C CD1   . LEU A 1 94  ? 12.20632  1.20621   16.52648  1.000 32.38029  ? 88  LEU A CD1   1 
ATOM   715  C CD2   . LEU A 1 94  ? 12.02579  1.18280   14.03082  1.000 29.53297  ? 88  LEU A CD2   1 
ATOM   716  N N     . ALA A 1 95  ? 14.39688  5.34747   15.59049  1.000 31.28931  ? 89  ALA A N     1 
ATOM   717  C CA    . ALA A 1 95  ? 15.82775  5.63222   15.56813  1.000 32.51826  ? 89  ALA A CA    1 
ATOM   718  C C     . ALA A 1 95  ? 16.28657  6.25437   16.88104  1.000 34.93059  ? 89  ALA A C     1 
ATOM   719  O O     . ALA A 1 95  ? 17.40016  5.98638   17.34755  1.000 35.68074  ? 89  ALA A O     1 
ATOM   720  C CB    . ALA A 1 95  ? 16.16372  6.54826   14.39167  1.000 30.85683  ? 89  ALA A CB    1 
ATOM   721  N N     . TYR A 1 96  ? 15.43936  7.08428   17.49484  1.000 31.72632  ? 90  TYR A N     1 
ATOM   722  C CA    . TYR A 1 96  ? 15.79685  7.70034   18.76882  1.000 32.43661  ? 90  TYR A CA    1 
ATOM   723  C C     . TYR A 1 96  ? 15.92976  6.65286   19.86758  1.000 33.66003  ? 90  TYR A C     1 
ATOM   724  O O     . TYR A 1 96  ? 16.90837  6.65267   20.62356  1.000 31.37947  ? 90  TYR A O     1 
ATOM   725  C CB    . TYR A 1 96  ? 14.75820  8.75480   19.15392  1.000 29.17536  ? 90  TYR A CB    1 
ATOM   726  C CG    . TYR A 1 96  ? 14.84600  9.20081   20.59760  1.000 32.38501  ? 90  TYR A CG    1 
ATOM   727  C CD1   . TYR A 1 96  ? 15.84901  10.06524  21.01771  1.000 30.96528  ? 90  TYR A CD1   1 
ATOM   728  C CD2   . TYR A 1 96  ? 13.92538  8.75835   21.54011  1.000 28.79292  ? 90  TYR A CD2   1 
ATOM   729  C CE1   . TYR A 1 96  ? 15.93415  10.47585  22.33646  1.000 36.95479  ? 90  TYR A CE1   1 
ATOM   730  C CE2   . TYR A 1 96  ? 14.00247  9.16305   22.86045  1.000 29.40068  ? 90  TYR A CE2   1 
ATOM   731  C CZ    . TYR A 1 96  ? 15.00819  10.02200  23.25282  1.000 35.26532  ? 90  TYR A CZ    1 
ATOM   732  O OH    . TYR A 1 96  ? 15.08883  10.42897  24.56491  1.000 28.46234  ? 90  TYR A OH    1 
ATOM   733  N N     . LEU A 1 97  ? 14.95122  5.74935   19.97154  1.000 31.10488  ? 91  LEU A N     1 
ATOM   734  C CA    . LEU A 1 97  ? 14.99834  4.72783   21.01243  1.000 34.40259  ? 91  LEU A CA    1 
ATOM   735  C C     . LEU A 1 97  ? 16.13309  3.73761   20.78089  1.000 31.64341  ? 91  LEU A C     1 
ATOM   736  O O     . LEU A 1 97  ? 16.69385  3.20650   21.74643  1.000 34.95091  ? 91  LEU A O     1 
ATOM   737  C CB    . LEU A 1 97  ? 13.65570  4.00095   21.09591  1.000 27.45220  ? 91  LEU A CB    1 
ATOM   738  C CG    . LEU A 1 97  ? 12.50404  4.83430   21.66439  1.000 29.16217  ? 91  LEU A CG    1 
ATOM   739  C CD1   . LEU A 1 97  ? 11.18557  4.08019   21.57755  1.000 30.05444  ? 91  LEU A CD1   1 
ATOM   740  C CD2   . LEU A 1 97  ? 12.79964  5.24291   23.10174  1.000 27.22634  ? 91  LEU A CD2   1 
ATOM   741  N N     . LYS A 1 98  ? 16.48299  3.47415   19.51883  1.000 32.01335  ? 92  LYS A N     1 
ATOM   742  C CA    . LYS A 1 98  ? 17.65699  2.65336   19.23788  1.000 32.17070  ? 92  LYS A CA    1 
ATOM   743  C C     . LYS A 1 98  ? 18.92828  3.33712   19.72486  1.000 39.74427  ? 92  LYS A C     1 
ATOM   744  O O     . LYS A 1 98  ? 19.83287  2.68151   20.25595  1.000 35.22209  ? 92  LYS A O     1 
ATOM   745  C CB    . LYS A 1 98  ? 17.75246  2.35915   17.74053  1.000 36.77166  ? 92  LYS A CB    1 
ATOM   746  C CG    . LYS A 1 98  ? 16.72476  1.36934   17.21299  1.000 41.76300  ? 92  LYS A CG    1 
ATOM   747  C CD    . LYS A 1 98  ? 16.73320  1.35046   15.69002  1.000 38.13480  ? 92  LYS A CD    1 
ATOM   748  C CE    . LYS A 1 98  ? 15.79281  0.29557   15.13567  1.000 36.26246  ? 92  LYS A CE    1 
ATOM   749  N NZ    . LYS A 1 98  ? 15.96155  0.10536   13.66876  1.000 51.56007  ? 92  LYS A NZ    1 
ATOM   750  N N     . ARG A 1 99  ? 19.01376  4.65861   19.54810  1.000 36.43517  ? 93  ARG A N     1 
ATOM   751  C CA    . ARG A 1 99  ? 20.17072  5.40406   20.03314  1.000 35.87399  ? 93  ARG A CA    1 
ATOM   752  C C     . ARG A 1 99  ? 20.25414  5.35615   21.55407  1.000 39.10485  ? 93  ARG A C     1 
ATOM   753  O O     . ARG A 1 99  ? 21.35036  5.26982   22.12065  1.000 37.17858  ? 93  ARG A O     1 
ATOM   754  C CB    . ARG A 1 99  ? 20.10080  6.84915   19.53302  1.000 40.83548  ? 93  ARG A CB    1 
ATOM   755  C CG    . ARG A 1 99  ? 21.10374  7.81151   20.16004  1.000 50.16922  ? 93  ARG A CG    1 
ATOM   756  C CD    . ARG A 1 99  ? 22.53768  7.31742   20.03668  1.000 52.05357  ? 93  ARG A CD    1 
ATOM   757  N NE    . ARG A 1 99  ? 23.48741  8.30003   20.54461  1.000 54.69874  ? 93  ARG A NE    1 
ATOM   758  C CZ    . ARG A 1 99  ? 24.69040  8.00739   21.01930  1.000 57.20280  ? 93  ARG A CZ    1 
ATOM   759  N NH1   . ARG A 1 99  ? 25.12550  6.75949   21.07974  1.000 46.22699  ? 93  ARG A NH1   1 
ATOM   760  N NH2   . ARG A 1 99  ? 25.47398  8.99143   21.45090  1.000 59.75903  ? 93  ARG A NH2   1 
ATOM   761  N N     . VAL A 1 100 ? 19.10460  5.40502   22.23275  1.000 33.76403  ? 94  VAL A N     1 
ATOM   762  C CA    . VAL A 1 100 ? 19.09505  5.26812   23.68699  1.000 32.26398  ? 94  VAL A CA    1 
ATOM   763  C C     . VAL A 1 100 ? 19.67749  3.92107   24.09563  1.000 36.99493  ? 94  VAL A C     1 
ATOM   764  O O     . VAL A 1 100 ? 20.46939  3.82971   25.04213  1.000 36.27796  ? 94  VAL A O     1 
ATOM   765  C CB    . VAL A 1 100 ? 17.66761  5.45624   24.23390  1.000 35.24510  ? 94  VAL A CB    1 
ATOM   766  C CG1   . VAL A 1 100 ? 17.64574  5.25426   25.74110  1.000 39.06459  ? 94  VAL A CG1   1 
ATOM   767  C CG2   . VAL A 1 100 ? 17.13128  6.83181   23.86635  1.000 33.09939  ? 94  VAL A CG2   1 
ATOM   768  N N     . ALA A 1 101 ? 19.30213  2.85560   23.38312  1.000 34.82254  ? 95  ALA A N     1 
ATOM   769  C CA    . ALA A 1 101 ? 19.85027  1.53660   23.67726  1.000 37.67055  ? 95  ALA A CA    1 
ATOM   770  C C     . ALA A 1 101 ? 21.33203  1.45381   23.33542  1.000 40.30936  ? 95  ALA A C     1 
ATOM   771  O O     . ALA A 1 101 ? 22.08475  0.75107   24.01960  1.000 39.55886  ? 95  ALA A O     1 
ATOM   772  C CB    . ALA A 1 101 ? 19.06957  0.46208   22.92048  1.000 38.25730  ? 95  ALA A CB    1 
ATOM   773  N N     . ASP A 1 102 ? 21.76764  2.15813   22.28794  1.000 39.15177  ? 96  ASP A N     1 
ATOM   774  C CA    . ASP A 1 102 ? 23.18135  2.15263   21.92426  1.000 39.32288  ? 96  ASP A CA    1 
ATOM   775  C C     . ASP A 1 102 ? 24.02935  2.81254   23.00413  1.000 43.37778  ? 96  ASP A C     1 
ATOM   776  O O     . ASP A 1 102 ? 25.02344  2.23936   23.46559  1.000 41.08699  ? 96  ASP A O     1 
ATOM   777  C CB    . ASP A 1 102 ? 23.38486  2.86428   20.58599  1.000 39.58615  ? 96  ASP A CB    1 
ATOM   778  C CG    . ASP A 1 102 ? 22.77907  2.10946   19.42187  1.000 46.79765  ? 96  ASP A CG    1 
ATOM   779  O OD1   . ASP A 1 102 ? 22.36637  0.94689   19.61293  1.000 44.59376  ? 96  ASP A OD1   1 
ATOM   780  O OD2   . ASP A 1 102 ? 22.71993  2.68152   18.31303  1.000 50.39037  ? 96  ASP A OD2   1 
ATOM   781  N N     . LYS A 1 103 ? 23.64613  4.02237   23.41991  1.000 37.15646  ? 97  LYS A N     1 
ATOM   782  C CA    . LYS A 1 103 ? 24.47398  4.79260   24.34247  1.000 45.29884  ? 97  LYS A CA    1 
ATOM   783  C C     . LYS A 1 103 ? 24.59036  4.10856   25.69851  1.000 42.93382  ? 97  LYS A C     1 
ATOM   784  O O     . LYS A 1 103 ? 25.66835  4.09516   26.30426  1.000 43.34075  ? 97  LYS A O     1 
ATOM   785  C CB    . LYS A 1 103 ? 23.90108  6.20059   24.50488  1.000 42.40647  ? 97  LYS A CB    1 
ATOM   786  C CG    . LYS A 1 103 ? 24.77038  7.13490   25.33014  1.000 40.13960  ? 97  LYS A CG    1 
ATOM   787  C CD    . LYS A 1 103 ? 23.99616  8.36883   25.76479  1.000 42.90855  ? 97  LYS A CD    1 
ATOM   788  C CE    . LYS A 1 103 ? 24.73639  9.12821   26.85501  1.000 48.34399  ? 97  LYS A CE    1 
ATOM   789  N NZ    . LYS A 1 103 ? 24.34564  10.56410  26.88877  1.000 47.44436  ? 97  LYS A NZ    1 
ATOM   790  N N     . HIS A 1 104 ? 23.49709  3.53021   26.18986  1.000 41.61623  ? 98  HIS A N     1 
ATOM   791  C CA    . HIS A 1 104 ? 23.45137  2.99155   27.54091  1.000 39.24412  ? 98  HIS A CA    1 
ATOM   792  C C     . HIS A 1 104 ? 23.58290  1.47460   27.58669  1.000 37.82629  ? 98  HIS A C     1 
ATOM   793  O O     . HIS A 1 104 ? 23.33562  0.87759   28.63962  1.000 39.29435  ? 98  HIS A O     1 
ATOM   794  C CB    . HIS A 1 104 ? 22.16482  3.43953   28.23389  1.000 37.76755  ? 98  HIS A CB    1 
ATOM   795  C CG    . HIS A 1 104 ? 22.10059  4.91639   28.46924  1.000 43.96934  ? 98  HIS A CG    1 
ATOM   796  N ND1   . HIS A 1 104 ? 22.73313  5.52818   29.52997  1.000 42.66376  ? 98  HIS A ND1   1 
ATOM   797  C CD2   . HIS A 1 104 ? 21.49647  5.90627   27.77001  1.000 40.14577  ? 98  HIS A CD2   1 
ATOM   798  C CE1   . HIS A 1 104 ? 22.51388  6.82995   29.47957  1.000 42.61579  ? 98  HIS A CE1   1 
ATOM   799  N NE2   . HIS A 1 104 ? 21.76704  7.08575   28.42046  1.000 40.22282  ? 98  HIS A NE2   1 
ATOM   800  N N     . ASP A 1 105 ? 23.96470  0.84336   26.47507  1.000 43.01876  ? 99  ASP A N     1 
ATOM   801  C CA    . ASP A 1 105 ? 24.31881  -0.57724  26.44758  1.000 44.16105  ? 99  ASP A CA    1 
ATOM   802  C C     . ASP A 1 105 ? 23.19094  -1.44089  27.01214  1.000 42.76895  ? 99  ASP A C     1 
ATOM   803  O O     . ASP A 1 105 ? 23.38725  -2.26478  27.90784  1.000 46.33230  ? 99  ASP A O     1 
ATOM   804  C CB    . ASP A 1 105 ? 25.63133  -0.81315  27.20019  1.000 44.76788  ? 99  ASP A CB    1 
ATOM   805  C CG    . ASP A 1 105 ? 26.21778  -2.18717  26.94454  1.000 45.33401  ? 99  ASP A CG    1 
ATOM   806  O OD1   . ASP A 1 105 ? 25.97007  -2.75400  25.86068  1.000 49.10224  ? 99  ASP A OD1   1 
ATOM   807  O OD2   . ASP A 1 105 ? 26.93356  -2.69679  27.83090  1.000 55.07204  ? 99  ASP A OD2   1 
ATOM   808  N N     . LEU A 1 106 ? 21.98889  -1.24202  26.47351  1.000 41.96615  ? 100 LEU A N     1 
ATOM   809  C CA    . LEU A 1 106 ? 20.79877  -1.88865  27.01297  1.000 42.42453  ? 100 LEU A CA    1 
ATOM   810  C C     . LEU A 1 106 ? 20.50073  -3.23833  26.37355  1.000 39.21684  ? 100 LEU A C     1 
ATOM   811  O O     . LEU A 1 106 ? 19.91621  -4.10700  27.03175  1.000 41.04837  ? 100 LEU A O     1 
ATOM   812  C CB    . LEU A 1 106 ? 19.58133  -0.97413  26.84435  1.000 37.27741  ? 100 LEU A CB    1 
ATOM   813  C CG    . LEU A 1 106 ? 19.60195  0.34971   27.61146  1.000 40.65268  ? 100 LEU A CG    1 
ATOM   814  C CD1   . LEU A 1 106 ? 18.33811  1.14882   27.33222  1.000 33.14224  ? 100 LEU A CD1   1 
ATOM   815  C CD2   . LEU A 1 106 ? 19.77161  0.10778   29.10413  1.000 33.05137  ? 100 LEU A CD2   1 
ATOM   816  N N     . ARG A 1 107 ? 20.88839  -3.43909  25.11130  1.000 39.15918  ? 101 ARG A N     1 
ATOM   817  C CA    . ARG A 1 107 ? 20.49936  -4.64886  24.39334  1.000 38.53465  ? 101 ARG A CA    1 
ATOM   818  C C     . ARG A 1 107 ? 21.13261  -5.90942  24.96720  1.000 42.88016  ? 101 ARG A C     1 
ATOM   819  O O     . ARG A 1 107 ? 20.59294  -7.00252  24.76428  1.000 41.17633  ? 101 ARG A O     1 
ATOM   820  C CB    . ARG A 1 107 ? 20.85873  -4.52228  22.91290  1.000 39.80821  ? 101 ARG A CB    1 
ATOM   821  C CG    . ARG A 1 107 ? 19.96956  -3.56365  22.14165  1.000 41.25093  ? 101 ARG A CG    1 
ATOM   822  C CD    . ARG A 1 107 ? 20.21018  -3.67176  20.64530  1.000 43.53154  ? 101 ARG A CD    1 
ATOM   823  N NE    . ARG A 1 107 ? 19.62358  -2.55196  19.91918  1.000 40.68413  ? 101 ARG A NE    1 
ATOM   824  C CZ    . ARG A 1 107 ? 20.16324  -1.34301  19.84433  1.000 40.75009  ? 101 ARG A CZ    1 
ATOM   825  N NH1   . ARG A 1 107 ? 21.31052  -1.05974  20.43917  1.000 41.45560  ? 101 ARG A NH1   1 
ATOM   826  N NH2   . ARG A 1 107 ? 19.53607  -0.39401  19.15542  1.000 40.92790  ? 101 ARG A NH2   1 
ATOM   827  N N     . LYS A 1 108 ? 22.25764  -5.78855  25.67573  1.000 43.24191  ? 102 LYS A N     1 
ATOM   828  C CA    . LYS A 1 108 ? 22.89938  -6.96679  26.24693  1.000 44.03146  ? 102 LYS A CA    1 
ATOM   829  C C     . LYS A 1 108 ? 22.05495  -7.61649  27.33494  1.000 40.03674  ? 102 LYS A C     1 
ATOM   830  O O     . LYS A 1 108 ? 22.29906  -8.77734  27.68020  1.000 44.07581  ? 102 LYS A O     1 
ATOM   831  C CB    . LYS A 1 108 ? 24.27721  -6.60278  26.80332  1.000 37.99599  ? 102 LYS A CB    1 
ATOM   832  C CG    . LYS A 1 108 ? 24.24747  -5.92963  28.16544  1.000 44.75600  ? 102 LYS A CG    1 
ATOM   833  C CD    . LYS A 1 108 ? 25.64877  -5.55245  28.61793  1.000 42.14490  ? 102 LYS A CD    1 
ATOM   834  C CE    . LYS A 1 108 ? 25.62812  -4.85228  29.96586  1.000 46.82331  ? 102 LYS A CE    1 
ATOM   835  N NZ    . LYS A 1 108 ? 24.92532  -5.66238  30.99817  1.000 50.55273  ? 102 LYS A NZ    1 
ATOM   836  N N     . ASP A 1 109 ? 21.06749  -6.90116  27.87678  1.000 39.08189  ? 103 ASP A N     1 
ATOM   837  C CA    . ASP A 1 109 ? 20.18674  -7.43762  28.90745  1.000 39.90778  ? 103 ASP A CA    1 
ATOM   838  C C     . ASP A 1 109 ? 18.73570  -7.50200  28.44324  1.000 38.96307  ? 103 ASP A C     1 
ATOM   839  O O     . ASP A 1 109 ? 17.82236  -7.55630  29.27291  1.000 42.23913  ? 103 ASP A O     1 
ATOM   840  C CB    . ASP A 1 109 ? 20.30815  -6.61278  30.18904  1.000 39.95892  ? 103 ASP A CB    1 
ATOM   841  C CG    . ASP A 1 109 ? 21.64827  -6.80061  30.87220  1.000 43.56566  ? 103 ASP A CG    1 
ATOM   842  O OD1   . ASP A 1 109 ? 21.94916  -7.93906  31.28849  1.000 42.88347  ? 103 ASP A OD1   1 
ATOM   843  O OD2   . ASP A 1 109 ? 22.40525  -5.81420  30.98252  1.000 43.70363  ? 103 ASP A OD2   1 
ATOM   844  N N     . ILE A 1 110 ? 18.50610  -7.49490  27.13280  1.000 37.27592  ? 104 ILE A N     1 
ATOM   845  C CA    . ILE A 1 110 ? 17.17970  -7.66267  26.55252  1.000 35.04314  ? 104 ILE A CA    1 
ATOM   846  C C     . ILE A 1 110 ? 17.18403  -8.94222  25.73079  1.000 37.66320  ? 104 ILE A C     1 
ATOM   847  O O     . ILE A 1 110 ? 18.07838  -9.14965  24.90230  1.000 36.27701  ? 104 ILE A O     1 
ATOM   848  C CB    . ILE A 1 110 ? 16.77658  -6.46211  25.67647  1.000 38.02587  ? 104 ILE A CB    1 
ATOM   849  C CG1   . ILE A 1 110 ? 16.88781  -5.15615  26.46156  1.000 34.71178  ? 104 ILE A CG1   1 
ATOM   850  C CG2   . ILE A 1 110 ? 15.36203  -6.64354  25.14541  1.000 34.47439  ? 104 ILE A CG2   1 
ATOM   851  C CD1   . ILE A 1 110 ? 16.61553  -3.92274  25.62624  1.000 33.76947  ? 104 ILE A CD1   1 
ATOM   852  N N     . GLN A 1 111 ? 16.19156  -9.79686  25.96039  1.000 37.46944  ? 105 GLN A N     1 
ATOM   853  C CA    . GLN A 1 111 ? 16.01279  -11.01827 25.17934  1.000 39.63550  ? 105 GLN A CA    1 
ATOM   854  C C     . GLN A 1 111 ? 14.91221  -10.75778 24.15771  1.000 37.06938  ? 105 GLN A C     1 
ATOM   855  O O     . GLN A 1 111 ? 13.72418  -10.77261 24.48890  1.000 37.36291  ? 105 GLN A O     1 
ATOM   856  C CB    . GLN A 1 111 ? 15.67828  -12.20499 26.07639  1.000 40.09875  ? 105 GLN A CB    1 
ATOM   857  C CG    . GLN A 1 111 ? 15.93182  -13.55349 25.41871  1.000 42.09446  ? 105 GLN A CG    1 
ATOM   858  C CD    . GLN A 1 111 ? 15.86572  -14.70775 26.39936  1.000 45.16125  ? 105 GLN A CD    1 
ATOM   859  O OE1   . GLN A 1 111 ? 16.64259  -14.77417 27.35179  1.000 41.17764  ? 105 GLN A OE1   1 
ATOM   860  N NE2   . GLN A 1 111 ? 14.93691  -15.62801 26.16749  1.000 45.30201  ? 105 GLN A NE2   1 
ATOM   861  N N     . PHE A 1 112 ? 15.31306  -10.51261 22.91441  1.000 37.14763  ? 106 PHE A N     1 
ATOM   862  C CA    . PHE A 1 112 ? 14.36266  -10.24439 21.85010  1.000 40.05792  ? 106 PHE A CA    1 
ATOM   863  C C     . PHE A 1 112 ? 13.76965  -11.54946 21.32321  1.000 43.82027  ? 106 PHE A C     1 
ATOM   864  O O     . PHE A 1 112 ? 14.22659  -12.64933 21.64768  1.000 40.63652  ? 106 PHE A O     1 
ATOM   865  C CB    . PHE A 1 112 ? 15.03384  -9.46423  20.72102  1.000 37.76503  ? 106 PHE A CB    1 
ATOM   866  C CG    . PHE A 1 112 ? 15.43973  -8.07057  21.10668  1.000 39.70447  ? 106 PHE A CG    1 
ATOM   867  C CD1   . PHE A 1 112 ? 14.48347  -7.09881  21.35182  1.000 38.52654  ? 106 PHE A CD1   1 
ATOM   868  C CD2   . PHE A 1 112 ? 16.77766  -7.73282  21.22709  1.000 37.95427  ? 106 PHE A CD2   1 
ATOM   869  C CE1   . PHE A 1 112 ? 14.85434  -5.81517  21.70737  1.000 35.86847  ? 106 PHE A CE1   1 
ATOM   870  C CE2   . PHE A 1 112 ? 17.15480  -6.45159  21.58293  1.000 37.10250  ? 106 PHE A CE2   1 
ATOM   871  C CZ    . PHE A 1 112 ? 16.19215  -5.49213  21.82317  1.000 34.00278  ? 106 PHE A CZ    1 
ATOM   872  N N     . GLU A 1 113 ? 12.72808  -11.41098 20.49834  1.000 38.10980  ? 107 GLU A N     1 
ATOM   873  C CA    . GLU A 1 113 ? 12.03683  -12.54715 19.88456  1.000 46.68544  ? 107 GLU A CA    1 
ATOM   874  C C     . GLU A 1 113 ? 11.50901  -13.52461 20.93117  1.000 46.66681  ? 107 GLU A C     1 
ATOM   875  O O     . GLU A 1 113 ? 11.37508  -14.72186 20.66581  1.000 45.29795  ? 107 GLU A O     1 
ATOM   876  C CB    . GLU A 1 113 ? 12.94246  -13.27968 18.88885  1.000 45.96686  ? 107 GLU A CB    1 
ATOM   877  C CG    . GLU A 1 113 ? 13.75351  -12.36546 17.98612  1.000 52.55731  ? 107 GLU A CG    1 
ATOM   878  C CD    . GLU A 1 113 ? 13.99433  -12.96559 16.61519  1.000 53.62754  ? 107 GLU A CD    1 
ATOM   879  O OE1   . GLU A 1 113 ? 13.01331  -13.15802 15.86728  1.000 60.03592  ? 107 GLU A OE1   1 
ATOM   880  O OE2   . GLU A 1 113 ? 15.16573  -13.24526 16.28537  1.000 57.88117  ? 107 GLU A OE2   1 
ATOM   881  N N     . THR A 1 114 ? 11.20077  -13.02662 22.12677  1.000 41.35772  ? 108 THR A N     1 
ATOM   882  C CA    . THR A 1 114 ? 10.80626  -13.87127 23.24724  1.000 42.14711  ? 108 THR A CA    1 
ATOM   883  C C     . THR A 1 114 ? 9.55268   -13.29790 23.88725  1.000 43.22697  ? 108 THR A C     1 
ATOM   884  O O     . THR A 1 114 ? 9.58107   -12.18863 24.43021  1.000 40.60761  ? 108 THR A O     1 
ATOM   885  C CB    . THR A 1 114 ? 11.93349  -13.97913 24.27813  1.000 40.01235  ? 108 THR A CB    1 
ATOM   886  O OG1   . THR A 1 114 ? 13.15632  -14.32440 23.61525  1.000 39.69162  ? 108 THR A OG1   1 
ATOM   887  C CG2   . THR A 1 114 ? 11.60826  -15.04191 25.31256  1.000 42.64500  ? 108 THR A CG2   1 
ATOM   888  N N     . GLY A 1 115 ? 8.46097   -14.05178 23.82454  1.000 39.51012  ? 109 GLY A N     1 
ATOM   889  C CA    . GLY A 1 115 ? 7.20907   -13.66097 24.44963  1.000 39.56649  ? 109 GLY A CA    1 
ATOM   890  C C     . GLY A 1 115 ? 7.04030   -14.34347 25.79311  1.000 44.89686  ? 109 GLY A C     1 
ATOM   891  O O     . GLY A 1 115 ? 7.36959   -15.51966 25.95201  1.000 41.67791  ? 109 GLY A O     1 
ATOM   892  N N     . ILE A 1 116 ? 6.52801   -13.59020 26.76074  1.000 39.23740  ? 110 ILE A N     1 
ATOM   893  C CA    . ILE A 1 116 ? 6.28377   -14.10334 28.10303  1.000 39.48372  ? 110 ILE A CA    1 
ATOM   894  C C     . ILE A 1 116 ? 4.88951   -14.71440 28.13477  1.000 38.77140  ? 110 ILE A C     1 
ATOM   895  O O     . ILE A 1 116 ? 3.89318   -14.02339 27.89583  1.000 37.26822  ? 110 ILE A O     1 
ATOM   896  C CB    . ILE A 1 116 ? 6.42795   -12.99633 29.15760  1.000 42.74613  ? 110 ILE A CB    1 
ATOM   897  C CG1   . ILE A 1 116 ? 7.86667   -12.47445 29.18943  1.000 37.91379  ? 110 ILE A CG1   1 
ATOM   898  C CG2   . ILE A 1 116 ? 6.00367   -13.50479 30.52821  1.000 34.74667  ? 110 ILE A CG2   1 
ATOM   899  C CD1   . ILE A 1 116 ? 8.90766   -13.55604 29.37638  1.000 40.87512  ? 110 ILE A CD1   1 
ATOM   900  N N     . ARG A 1 117 ? 4.81735   -16.01218 28.42657  1.000 41.30502  ? 111 ARG A N     1 
ATOM   901  C CA    . ARG A 1 117 ? 3.53919   -16.71158 28.45308  1.000 40.16739  ? 111 ARG A CA    1 
ATOM   902  C C     . ARG A 1 117 ? 2.86639   -16.64588 29.81805  1.000 38.79435  ? 111 ARG A C     1 
ATOM   903  O O     . ARG A 1 117 ? 1.64535   -16.47252 29.89568  1.000 40.65792  ? 111 ARG A O     1 
ATOM   904  C CB    . ARG A 1 117 ? 3.72730   -18.17483 28.04158  1.000 45.18510  ? 111 ARG A CB    1 
ATOM   905  C CG    . ARG A 1 117 ? 2.42586   -18.95386 27.92187  1.000 43.89910  ? 111 ARG A CG    1 
ATOM   906  C CD    . ARG A 1 117 ? 2.61519   -20.42120 28.27592  1.000 51.12333  ? 111 ARG A CD    1 
ATOM   907  N NE    . ARG A 1 117 ? 3.62319   -21.06379 27.44160  1.000 47.16154  ? 111 ARG A NE    1 
ATOM   908  C CZ    . ARG A 1 117 ? 4.55103   -21.89575 27.89449  1.000 49.08184  ? 111 ARG A CZ    1 
ATOM   909  N NH1   . ARG A 1 117 ? 4.62899   -22.21278 29.17655  1.000 52.03523  ? 111 ARG A NH1   1 
ATOM   910  N NH2   . ARG A 1 117 ? 5.42183   -22.42401 27.03934  1.000 53.25220  ? 111 ARG A NH2   1 
ATOM   911  N N     . SER A 1 118 ? 3.63275   -16.77746 30.89869  1.000 40.61840  ? 112 SER A N     1 
ATOM   912  C CA    . SER A 1 118 ? 3.04460   -16.83642 32.22723  1.000 42.88053  ? 112 SER A CA    1 
ATOM   913  C C     . SER A 1 118 ? 4.01652   -16.27658 33.25421  1.000 42.05110  ? 112 SER A C     1 
ATOM   914  O O     . SER A 1 118 ? 5.23520   -16.30019 33.06124  1.000 39.72766  ? 112 SER A O     1 
ATOM   915  C CB    . SER A 1 118 ? 2.65797   -18.27152 32.60384  1.000 44.09322  ? 112 SER A CB    1 
ATOM   916  O OG    . SER A 1 118 ? 3.80778   -19.08743 32.74238  1.000 42.03017  ? 112 SER A OG    1 
ATOM   917  N N     . ALA A 1 119 ? 3.45523   -15.77459 34.35230  1.000 45.44428  ? 113 ALA A N     1 
ATOM   918  C CA    . ALA A 1 119 ? 4.22962   -15.31050 35.50000  1.000 45.92522  ? 113 ALA A CA    1 
ATOM   919  C C     . ALA A 1 119 ? 3.48022   -15.73202 36.75568  1.000 44.42687  ? 113 ALA A C     1 
ATOM   920  O O     . ALA A 1 119 ? 2.39084   -15.21922 37.03068  1.000 46.58610  ? 113 ALA A O     1 
ATOM   921  C CB    . ALA A 1 119 ? 4.43598   -13.79613 35.46341  1.000 44.68996  ? 113 ALA A CB    1 
ATOM   922  N N     . TYR A 1 120 ? 4.05152   -16.66932 37.50607  1.000 46.92858  ? 114 TYR A N     1 
ATOM   923  C CA    . TYR A 1 120 ? 3.43246   -17.20576 38.71059  1.000 47.70898  ? 114 TYR A CA    1 
ATOM   924  C C     . TYR A 1 120 ? 4.21729   -16.74399 39.92995  1.000 46.51407  ? 114 TYR A C     1 
ATOM   925  O O     . TYR A 1 120 ? 5.44496   -16.87808 39.96915  1.000 46.44553  ? 114 TYR A O     1 
ATOM   926  C CB    . TYR A 1 120 ? 3.38024   -18.73557 38.66917  1.000 47.11665  ? 114 TYR A CB    1 
ATOM   927  C CG    . TYR A 1 120 ? 2.39445   -19.30316 37.67094  1.000 52.53899  ? 114 TYR A CG    1 
ATOM   928  C CD1   . TYR A 1 120 ? 2.41613   -20.65083 37.33636  1.000 55.87308  ? 114 TYR A CD1   1 
ATOM   929  C CD2   . TYR A 1 120 ? 1.44644   -18.49312 37.05995  1.000 52.67457  ? 114 TYR A CD2   1 
ATOM   930  C CE1   . TYR A 1 120 ? 1.51868   -21.17658 36.42550  1.000 51.36039  ? 114 TYR A CE1   1 
ATOM   931  C CE2   . TYR A 1 120 ? 0.54742   -19.00987 36.14560  1.000 54.40214  ? 114 TYR A CE2   1 
ATOM   932  C CZ    . TYR A 1 120 ? 0.58656   -20.35127 35.83376  1.000 59.44482  ? 114 TYR A CZ    1 
ATOM   933  O OH    . TYR A 1 120 ? -0.30804  -20.86882 34.92538  1.000 56.96887  ? 114 TYR A OH    1 
ATOM   934  N N     . PHE A 1 121 ? 3.51076   -16.20580 40.92084  1.000 45.04064  ? 115 PHE A N     1 
ATOM   935  C CA    . PHE A 1 121 ? 4.15573   -15.74813 42.14340  1.000 48.20921  ? 115 PHE A CA    1 
ATOM   936  C C     . PHE A 1 121 ? 4.32499   -16.90894 43.11501  1.000 52.65172  ? 115 PHE A C     1 
ATOM   937  O O     . PHE A 1 121 ? 3.37456   -17.64947 43.38711  1.000 52.07655  ? 115 PHE A O     1 
ATOM   938  C CB    . PHE A 1 121 ? 3.34693   -14.62908 42.79788  1.000 48.29763  ? 115 PHE A CB    1 
ATOM   939  C CG    . PHE A 1 121 ? 4.05639   -13.96364 43.94435  1.000 52.73053  ? 115 PHE A CG    1 
ATOM   940  C CD1   . PHE A 1 121 ? 5.27681   -13.33710 43.75082  1.000 50.28695  ? 115 PHE A CD1   1 
ATOM   941  C CD2   . PHE A 1 121 ? 3.50963   -13.97536 45.21706  1.000 50.64303  ? 115 PHE A CD2   1 
ATOM   942  C CE1   . PHE A 1 121 ? 5.93522   -12.72760 44.80332  1.000 52.00124  ? 115 PHE A CE1   1 
ATOM   943  C CE2   . PHE A 1 121 ? 4.16370   -13.36836 46.27412  1.000 51.41802  ? 115 PHE A CE2   1 
ATOM   944  C CZ    . PHE A 1 121 ? 5.37759   -12.74332 46.06646  1.000 53.30100  ? 115 PHE A CZ    1 
ATOM   945  N N     . ASP A 1 122 ? 5.53785   -17.06156 43.63777  1.000 55.71948  ? 116 ASP A N     1 
ATOM   946  C CA    . ASP A 1 122 ? 5.86507   -18.10754 44.60352  1.000 58.51898  ? 116 ASP A CA    1 
ATOM   947  C C     . ASP A 1 122 ? 5.78910   -17.49116 45.99597  1.000 56.41379  ? 116 ASP A C     1 
ATOM   948  O O     . ASP A 1 122 ? 6.72171   -16.81783 46.43773  1.000 59.31014  ? 116 ASP A O     1 
ATOM   949  C CB    . ASP A 1 122 ? 7.24761   -18.68647 44.31871  1.000 60.24109  ? 116 ASP A CB    1 
ATOM   950  C CG    . ASP A 1 122 ? 7.55731   -19.91518 45.15686  1.000 65.84940  ? 116 ASP A CG    1 
ATOM   951  O OD1   . ASP A 1 122 ? 6.76137   -20.25127 46.05851  1.000 65.96707  ? 116 ASP A OD1   1 
ATOM   952  O OD2   . ASP A 1 122 ? 8.60726   -20.54625 44.91457  1.000 64.97583  ? 116 ASP A OD2   1 
ATOM   953  N N     . GLU A 1 123 ? 4.67476   -17.72892 46.69222  1.000 59.39488  ? 117 GLU A N     1 
ATOM   954  C CA    . GLU A 1 123 ? 4.50325   -17.17540 48.03093  1.000 64.42300  ? 117 GLU A CA    1 
ATOM   955  C C     . GLU A 1 123 ? 5.47688   -17.77270 49.03875  1.000 68.87876  ? 117 GLU A C     1 
ATOM   956  O O     . GLU A 1 123 ? 5.70896   -17.16624 50.09003  1.000 68.74127  ? 117 GLU A O     1 
ATOM   957  C CB    . GLU A 1 123 ? 3.06687   -17.38785 48.51058  1.000 64.27895  ? 117 GLU A CB    1 
ATOM   958  C CG    . GLU A 1 123 ? 2.01790   -16.69101 47.66075  1.000 57.76062  ? 117 GLU A CG    1 
ATOM   959  C CD    . GLU A 1 123 ? 0.61134   -16.90274 48.18492  1.000 61.40091  ? 117 GLU A CD    1 
ATOM   960  O OE1   . GLU A 1 123 ? 0.30689   -16.40798 49.29092  1.000 66.00636  ? 117 GLU A OE1   1 
ATOM   961  O OE2   . GLU A 1 123 ? -0.18856  -17.56681 47.49295  1.000 63.63192  ? 117 GLU A OE2   1 
ATOM   962  N N     . GLU A 1 124 ? 6.04750   -18.94298 48.74667  1.000 67.85405  ? 118 GLU A N     1 
ATOM   963  C CA    . GLU A 1 124 ? 7.01439   -19.54301 49.66019  1.000 74.36827  ? 118 GLU A CA    1 
ATOM   964  C C     . GLU A 1 124 ? 8.33049   -18.77469 49.64695  1.000 72.60584  ? 118 GLU A C     1 
ATOM   965  O O     . GLU A 1 124 ? 8.84012   -18.37636 50.70098  1.000 73.02017  ? 118 GLU A O     1 
ATOM   966  C CB    . GLU A 1 124 ? 7.24094   -21.01040 49.29376  1.000 76.21275  ? 118 GLU A CB    1 
ATOM   967  C CG    . GLU A 1 124 ? 7.43669   -21.92877 50.48873  1.000 80.47283  ? 118 GLU A CG    1 
ATOM   968  C CD    . GLU A 1 124 ? 6.14449   -22.20092 51.23165  1.000 89.26326  ? 118 GLU A CD    1 
ATOM   969  O OE1   . GLU A 1 124 ? 5.21889   -22.77867 50.62471  1.000 90.74568  ? 118 GLU A OE1   1 
ATOM   970  O OE2   . GLU A 1 124 ? 6.05404   -21.83825 52.42280  1.000 87.61072  ? 118 GLU A OE2   1 
ATOM   971  N N     . ASN A 1 125 ? 8.89463   -18.55481 48.45967  1.000 69.04598  ? 119 ASN A N     1 
ATOM   972  C CA    . ASN A 1 125 ? 10.15711  -17.84411 48.31716  1.000 69.90683  ? 119 ASN A CA    1 
ATOM   973  C C     . ASN A 1 125 ? 9.98196   -16.36052 48.02136  1.000 63.38737  ? 119 ASN A C     1 
ATOM   974  O O     . ASN A 1 125 ? 10.97748  -15.62890 48.01066  1.000 61.68009  ? 119 ASN A O     1 
ATOM   975  C CB    . ASN A 1 125 ? 11.00003  -18.47982 47.20679  1.000 69.79796  ? 119 ASN A CB    1 
ATOM   976  C CG    . ASN A 1 125 ? 10.95203  -19.99375 47.22868  1.000 74.27578  ? 119 ASN A CG    1 
ATOM   977  O OD1   . ASN A 1 125 ? 9.92558   -20.58979 47.55205  1.000 75.13540  ? 119 ASN A OD1   1 
ATOM   978  N ND2   . ASN A 1 125 ? 12.06522  -20.62515 46.87582  1.000 73.62805  ? 119 ASN A ND2   1 
ATOM   979  N N     . SER A 1 126 ? 8.75215   -15.90839 47.77110  1.000 61.22438  ? 120 SER A N     1 
ATOM   980  C CA    . SER A 1 126 ? 8.45043   -14.49811 47.51696  1.000 60.51097  ? 120 SER A CA    1 
ATOM   981  C C     . SER A 1 126 ? 9.18838   -13.97555 46.28330  1.000 58.82856  ? 120 SER A C     1 
ATOM   982  O O     . SER A 1 126 ? 9.77476   -12.89187 46.29590  1.000 54.18847  ? 120 SER A O     1 
ATOM   983  C CB    . SER A 1 126 ? 8.75530   -13.63758 48.74645  1.000 58.29553  ? 120 SER A CB    1 
ATOM   984  O OG    . SER A 1 126 ? 7.56409   -13.27081 49.42169  1.000 57.72718  ? 120 SER A OG    1 
ATOM   985  N N     . PHE A 1 127 ? 9.15530   -14.75801 45.20313  1.000 56.96292  ? 121 PHE A N     1 
ATOM   986  C CA    . PHE A 1 127 ? 9.60807   -14.28018 43.90256  1.000 54.00784  ? 121 PHE A CA    1 
ATOM   987  C C     . PHE A 1 127 ? 8.62969   -14.75350 42.83279  1.000 55.09296  ? 121 PHE A C     1 
ATOM   988  O O     . PHE A 1 127 ? 7.61666   -15.39687 43.12539  1.000 51.69536  ? 121 PHE A O     1 
ATOM   989  C CB    . PHE A 1 127 ? 11.06215  -14.69752 43.60162  1.000 55.45564  ? 121 PHE A CB    1 
ATOM   990  C CG    . PHE A 1 127 ? 11.32674  -16.19151 43.62316  1.000 58.54092  ? 121 PHE A CG    1 
ATOM   991  C CD1   . PHE A 1 127 ? 10.54517  -17.08613 42.90473  1.000 58.25499  ? 121 PHE A CD1   1 
ATOM   992  C CD2   . PHE A 1 127 ? 12.41151  -16.68858 44.32823  1.000 64.56094  ? 121 PHE A CD2   1 
ATOM   993  C CE1   . PHE A 1 127 ? 10.81543  -18.44107 42.92213  1.000 57.56806  ? 121 PHE A CE1   1 
ATOM   994  C CE2   . PHE A 1 127 ? 12.69088  -18.04216 44.34207  1.000 64.90226  ? 121 PHE A CE2   1 
ATOM   995  C CZ    . PHE A 1 127 ? 11.88905  -18.91911 43.64183  1.000 63.85788  ? 121 PHE A CZ    1 
ATOM   996  N N     . TRP A 1 128 ? 8.94695   -14.43847 41.58012  1.000 51.76497  ? 122 TRP A N     1 
ATOM   997  C CA    . TRP A 1 128 ? 8.07273   -14.70889 40.44851  1.000 44.34436  ? 122 TRP A CA    1 
ATOM   998  C C     . TRP A 1 128 ? 8.65844   -15.80527 39.56934  1.000 45.47827  ? 122 TRP A C     1 
ATOM   999  O O     . TRP A 1 128 ? 9.85984   -15.81082 39.28271  1.000 44.83769  ? 122 TRP A O     1 
ATOM   1000 C CB    . TRP A 1 128 ? 7.85427   -13.44230 39.61562  1.000 43.00770  ? 122 TRP A CB    1 
ATOM   1001 C CG    . TRP A 1 128 ? 6.84127   -12.50921 40.19864  1.000 40.02331  ? 122 TRP A CG    1 
ATOM   1002 C CD1   . TRP A 1 128 ? 7.07890   -11.46432 41.04324  1.000 42.47968  ? 122 TRP A CD1   1 
ATOM   1003 C CD2   . TRP A 1 128 ? 5.42642   -12.53369 39.97828  1.000 39.99504  ? 122 TRP A CD2   1 
ATOM   1004 N NE1   . TRP A 1 128 ? 5.89887   -10.83822 41.36464  1.000 41.10898  ? 122 TRP A NE1   1 
ATOM   1005 C CE2   . TRP A 1 128 ? 4.86958   -11.47541 40.72281  1.000 37.44330  ? 122 TRP A CE2   1 
ATOM   1006 C CE3   . TRP A 1 128 ? 4.57625   -13.34873 39.22467  1.000 42.21680  ? 122 TRP A CE3   1 
ATOM   1007 C CZ2   . TRP A 1 128 ? 3.50232   -11.21071 40.73498  1.000 39.15420  ? 122 TRP A CZ2   1 
ATOM   1008 C CZ3   . TRP A 1 128 ? 3.21965   -13.08411 39.23843  1.000 42.36263  ? 122 TRP A CZ3   1 
ATOM   1009 C CH2   . TRP A 1 128 ? 2.69612   -12.02450 39.98801  1.000 44.59211  ? 122 TRP A CH2   1 
ATOM   1010 N N     . ASN A 1 129 ? 7.80106   -16.73032 39.14267  1.000 46.73625  ? 123 ASN A N     1 
ATOM   1011 C CA    . ASN A 1 129 ? 8.16571   -17.77014 38.18280  1.000 48.89683  ? 123 ASN A CA    1 
ATOM   1012 C C     . ASN A 1 129 ? 7.66166   -17.32530 36.81459  1.000 43.72652  ? 123 ASN A C     1 
ATOM   1013 O O     . ASN A 1 129 ? 6.47320   -17.44760 36.50902  1.000 43.64555  ? 123 ASN A O     1 
ATOM   1014 C CB    . ASN A 1 129 ? 7.57947   -19.11995 38.58432  1.000 50.71577  ? 123 ASN A CB    1 
ATOM   1015 C CG    . ASN A 1 129 ? 8.32992   -19.76475 39.73173  1.000 48.70433  ? 123 ASN A CG    1 
ATOM   1016 O OD1   . ASN A 1 129 ? 9.56051   -19.79393 39.74595  1.000 51.00068  ? 123 ASN A OD1   1 
ATOM   1017 N ND2   . ASN A 1 129 ? 7.59009   -20.28944 40.70101  1.000 53.83400  ? 123 ASN A ND2   1 
ATOM   1018 N N     . VAL A 1 130 ? 8.56744   -16.80207 35.99366  1.000 45.98434  ? 124 VAL A N     1 
ATOM   1019 C CA    . VAL A 1 130 ? 8.23330   -16.29510 34.66794  1.000 49.70665  ? 124 VAL A CA    1 
ATOM   1020 C C     . VAL A 1 130 ? 8.61701   -17.34273 33.63392  1.000 44.62871  ? 124 VAL A C     1 
ATOM   1021 O O     . VAL A 1 130 ? 9.76324   -17.80831 33.60506  1.000 45.41019  ? 124 VAL A O     1 
ATOM   1022 C CB    . VAL A 1 130 ? 8.94223   -14.95941 34.38697  1.000 40.92569  ? 124 VAL A CB    1 
ATOM   1023 C CG1   . VAL A 1 130 ? 8.58452   -14.45219 33.00053  1.000 41.05579  ? 124 VAL A CG1   1 
ATOM   1024 C CG2   . VAL A 1 130 ? 8.57739   -13.93220 35.44773  1.000 39.85344  ? 124 VAL A CG2   1 
ATOM   1025 N N     . THR A 1 131 ? 7.66224   -17.71183 32.78409  1.000 40.53372  ? 125 THR A N     1 
ATOM   1026 C CA    . THR A 1 131 ? 7.87748   -18.68873 31.72613  1.000 43.99317  ? 125 THR A CA    1 
ATOM   1027 C C     . THR A 1 131 ? 7.62599   -18.03366 30.37687  1.000 42.88092  ? 125 THR A C     1 
ATOM   1028 O O     . THR A 1 131 ? 6.55227   -17.46668 30.14635  1.000 40.26881  ? 125 THR A O     1 
ATOM   1029 C CB    . THR A 1 131 ? 6.96263   -19.90538 31.89437  1.000 44.36581  ? 125 THR A CB    1 
ATOM   1030 O OG1   . THR A 1 131 ? 7.01059   -20.36193 33.25213  1.000 46.70638  ? 125 THR A OG1   1 
ATOM   1031 C CG2   . THR A 1 131 ? 7.39903   -21.02996 30.96802  1.000 45.96037  ? 125 THR A CG2   1 
ATOM   1032 N N     . THR A 1 132 ? 8.61396   -18.11412 29.49134  1.000 38.39566  ? 126 THR A N     1 
ATOM   1033 C CA    . THR A 1 132 ? 8.44449   -17.60133 28.14435  1.000 41.77138  ? 126 THR A CA    1 
ATOM   1034 C C     . THR A 1 132 ? 7.47903   -18.48851 27.36049  1.000 48.19361  ? 126 THR A C     1 
ATOM   1035 O O     . THR A 1 132 ? 7.07878   -19.57150 27.80231  1.000 44.73338  ? 126 THR A O     1 
ATOM   1036 C CB    . THR A 1 132 ? 9.79031   -17.52346 27.42285  1.000 44.98214  ? 126 THR A CB    1 
ATOM   1037 O OG1   . THR A 1 132 ? 10.17395  -18.82559 26.96366  1.000 51.85240  ? 126 THR A OG1   1 
ATOM   1038 C CG2   . THR A 1 132 ? 10.86249  -16.98710 28.35774  1.000 42.63884  ? 126 THR A CG2   1 
ATOM   1039 N N     . GLU A 1 133 ? 7.10994   -18.02205 26.16703  1.000 47.33051  ? 127 GLU A N     1 
ATOM   1040 C CA    . GLU A 1 133 ? 6.30378   -18.85428 25.28522  1.000 41.05560  ? 127 GLU A CA    1 
ATOM   1041 C C     . GLU A 1 133 ? 7.08467   -20.03458 24.72838  1.000 49.10453  ? 127 GLU A C     1 
ATOM   1042 O O     . GLU A 1 133 ? 6.48288   -20.90645 24.08845  1.000 47.53521  ? 127 GLU A O     1 
ATOM   1043 C CB    . GLU A 1 133 ? 5.74437   -18.02096 24.13367  1.000 44.42989  ? 127 GLU A CB    1 
ATOM   1044 C CG    . GLU A 1 133 ? 4.70826   -16.99740 24.56084  1.000 44.61041  ? 127 GLU A CG    1 
ATOM   1045 C CD    . GLU A 1 133 ? 4.30238   -16.08228 23.42636  1.000 52.64051  ? 127 GLU A CD    1 
ATOM   1046 O OE1   . GLU A 1 133 ? 5.11364   -15.88787 22.49778  1.000 55.74404  ? 127 GLU A OE1   1 
ATOM   1047 O OE2   . GLU A 1 133 ? 3.16663   -15.56455 23.45820  1.000 52.14099  ? 127 GLU A OE2   1 
ATOM   1048 N N     . ASN A 1 134 ? 8.39895   -20.08914 24.95218  1.000 51.78640  ? 128 ASN A N     1 
ATOM   1049 C CA    . ASN A 1 134 ? 9.20158   -21.19568 24.46005  1.000 50.70488  ? 128 ASN A CA    1 
ATOM   1050 C C     . ASN A 1 134 ? 9.66472   -22.09009 25.60313  1.000 54.23434  ? 128 ASN A C     1 
ATOM   1051 O O     . ASN A 1 134 ? 10.71515  -22.72863 25.49940  1.000 50.86009  ? 128 ASN A O     1 
ATOM   1052 C CB    . ASN A 1 134 ? 10.40206  -20.67711 23.67151  1.000 51.77104  ? 128 ASN A CB    1 
ATOM   1053 C CG    . ASN A 1 134 ? 10.55525  -21.36708 22.35016  1.000 63.11759  ? 128 ASN A CG    1 
ATOM   1054 O OD1   . ASN A 1 134 ? 10.71683  -22.57172 22.27915  1.000 67.74905  ? 128 ASN A OD1   1 
ATOM   1055 N ND2   . ASN A 1 134 ? 10.50298  -20.59528 21.28434  1.000 65.11549  ? 128 ASN A ND2   1 
ATOM   1056 N N     . ASP A 1 135 ? 8.93274   -22.08311 26.72049  1.000 49.97633  ? 129 ASP A N     1 
ATOM   1057 C CA    . ASP A 1 135 ? 9.14738   -22.96114 27.86898  1.000 54.01978  ? 129 ASP A CA    1 
ATOM   1058 C C     . ASP A 1 135 ? 10.44978  -22.67925 28.61000  1.000 51.61173  ? 129 ASP A C     1 
ATOM   1059 O O     . ASP A 1 135 ? 10.93213  -23.53555 29.35708  1.000 47.40551  ? 129 ASP A O     1 
ATOM   1060 C CB    . ASP A 1 135 ? 9.07882   -24.43762 27.45712  1.000 54.69692  ? 129 ASP A CB    1 
ATOM   1061 C CG    . ASP A 1 135 ? 7.74398   -24.80640 26.84060  1.000 55.46519  ? 129 ASP A CG    1 
ATOM   1062 O OD1   . ASP A 1 135 ? 6.69819   -24.56522 27.48065  1.000 60.47116  ? 129 ASP A OD1   1 
ATOM   1063 O OD2   . ASP A 1 135 ? 7.74015   -25.33860 25.71170  1.000 61.96259  ? 129 ASP A OD2   1 
ATOM   1064 N N     . GLU A 1 136 ? 11.03012  -21.49542 28.42750  1.000 49.02670  ? 130 GLU A N     1 
ATOM   1065 C CA    . GLU A 1 136 ? 12.16822  -21.08247 29.23680  1.000 48.61778  ? 130 GLU A CA    1 
ATOM   1066 C C     . GLU A 1 136 ? 11.66683  -20.44431 30.52607  1.000 46.82234  ? 130 GLU A C     1 
ATOM   1067 O O     . GLU A 1 136 ? 10.78302  -19.58326 30.49712  1.000 46.08399  ? 130 GLU A O     1 
ATOM   1068 C CB    . GLU A 1 136 ? 13.05410  -20.10445 28.46560  1.000 51.85469  ? 130 GLU A CB    1 
ATOM   1069 C CG    . GLU A 1 136 ? 14.54502  -20.37051 28.60314  1.000 52.77756  ? 130 GLU A CG    1 
ATOM   1070 C CD    . GLU A 1 136 ? 15.38768  -19.31504 27.91659  1.000 59.63654  ? 130 GLU A CD    1 
ATOM   1071 O OE1   . GLU A 1 136 ? 14.82959  -18.52813 27.12344  1.000 58.41189  ? 130 GLU A OE1   1 
ATOM   1072 O OE2   . GLU A 1 136 ? 16.60803  -19.26458 28.17743  1.000 62.98963  ? 130 GLU A OE2   1 
ATOM   1073 N N     . LYS A 1 137 ? 12.22515  -20.86856 31.65568  1.000 43.74621  ? 131 LYS A N     1 
ATOM   1074 C CA    . LYS A 1 137 ? 11.77100  -20.42972 32.96814  1.000 45.19304  ? 131 LYS A CA    1 
ATOM   1075 C C     . LYS A 1 137 ? 12.85521  -19.60070 33.64330  1.000 52.43884  ? 131 LYS A C     1 
ATOM   1076 O O     . LYS A 1 137 ? 14.01435  -20.02478 33.71841  1.000 53.33286  ? 131 LYS A O     1 
ATOM   1077 C CB    . LYS A 1 137 ? 11.39846  -21.62561 33.84707  1.000 49.00937  ? 131 LYS A CB    1 
ATOM   1078 C CG    . LYS A 1 137 ? 10.87100  -21.24306 35.21927  1.000 49.99640  ? 131 LYS A CG    1 
ATOM   1079 C CD    . LYS A 1 137 ? 10.73383  -22.45942 36.11955  1.000 54.74291  ? 131 LYS A CD    1 
ATOM   1080 C CE    . LYS A 1 137 ? 10.88302  -22.08352 37.58496  1.000 50.88888  ? 131 LYS A CE    1 
ATOM   1081 N NZ    . LYS A 1 137 ? 11.81605  -22.99816 38.29812  1.000 58.05938  ? 131 LYS A NZ    1 
ATOM   1082 N N     . PHE A 1 138 ? 12.47388  -18.42183 34.13188  1.000 49.84670  ? 132 PHE A N     1 
ATOM   1083 C CA    . PHE A 1 138 ? 13.36796  -17.54428 34.87095  1.000 49.71753  ? 132 PHE A CA    1 
ATOM   1084 C C     . PHE A 1 138 ? 12.72693  -17.17584 36.20057  1.000 49.61658  ? 132 PHE A C     1 
ATOM   1085 O O     . PHE A 1 138 ? 11.50011  -17.16290 36.33454  1.000 49.76199  ? 132 PHE A O     1 
ATOM   1086 C CB    . PHE A 1 138 ? 13.69218  -16.26613 34.08405  1.000 49.09543  ? 132 PHE A CB    1 
ATOM   1087 C CG    . PHE A 1 138 ? 14.34936  -16.51650 32.75726  1.000 43.98636  ? 132 PHE A CG    1 
ATOM   1088 C CD1   . PHE A 1 138 ? 15.72670  -16.62689 32.66105  1.000 46.40856  ? 132 PHE A CD1   1 
ATOM   1089 C CD2   . PHE A 1 138 ? 13.59052  -16.63229 31.60475  1.000 43.72709  ? 132 PHE A CD2   1 
ATOM   1090 C CE1   . PHE A 1 138 ? 16.33445  -16.85380 31.44062  1.000 50.44276  ? 132 PHE A CE1   1 
ATOM   1091 C CE2   . PHE A 1 138 ? 14.19214  -16.85866 30.38207  1.000 46.08723  ? 132 PHE A CE2   1 
ATOM   1092 C CZ    . PHE A 1 138 ? 15.56595  -16.96904 30.30022  1.000 49.67564  ? 132 PHE A CZ    1 
ATOM   1093 N N     . THR A 1 139 ? 13.57001  -16.87369 37.18320  1.000 48.63666  ? 133 THR A N     1 
ATOM   1094 C CA    . THR A 1 139 ? 13.12388  -16.46702 38.50717  1.000 50.95327  ? 133 THR A CA    1 
ATOM   1095 C C     . THR A 1 139 ? 13.63146  -15.06424 38.80803  1.000 43.45448  ? 133 THR A C     1 
ATOM   1096 O O     . THR A 1 139 ? 14.77894  -14.72845 38.49837  1.000 44.49559  ? 133 THR A O     1 
ATOM   1097 C CB    . THR A 1 139 ? 13.61157  -17.44135 39.58647  1.000 50.27503  ? 133 THR A CB    1 
ATOM   1098 O OG1   . THR A 1 139 ? 15.04003  -17.54014 39.53480  1.000 50.56478  ? 133 THR A OG1   1 
ATOM   1099 C CG2   . THR A 1 139 ? 13.00475  -18.82060 39.37210  1.000 52.71214  ? 133 THR A CG2   1 
ATOM   1100 N N     . ALA A 1 140 ? 12.77014  -14.24778 39.40923  1.000 43.67835  ? 134 ALA A N     1 
ATOM   1101 C CA    . ALA A 1 140 ? 13.13548  -12.88546 39.76637  1.000 46.16441  ? 134 ALA A CA    1 
ATOM   1102 C C     . ALA A 1 140 ? 12.26343  -12.42693 40.92367  1.000 42.84756  ? 134 ALA A C     1 
ATOM   1103 O O     . ALA A 1 140 ? 11.08798  -12.79030 41.01458  1.000 43.36718  ? 134 ALA A O     1 
ATOM   1104 C CB    . ALA A 1 140 ? 12.99086  -11.92928 38.57798  1.000 47.09975  ? 134 ALA A CB    1 
ATOM   1105 N N     . ARG A 1 141 ? 12.85677  -11.61921 41.80490  1.000 45.15756  ? 135 ARG A N     1 
ATOM   1106 C CA    . ARG A 1 141 ? 12.12195  -11.12035 42.96230  1.000 44.18753  ? 135 ARG A CA    1 
ATOM   1107 C C     . ARG A 1 141 ? 10.99643  -10.18197 42.54437  1.000 44.73628  ? 135 ARG A C     1 
ATOM   1108 O O     . ARG A 1 141 ? 9.88775   -10.25508 43.08635  1.000 41.96857  ? 135 ARG A O     1 
ATOM   1109 C CB    . ARG A 1 141 ? 13.07815  -10.41550 43.92464  1.000 49.75691  ? 135 ARG A CB    1 
ATOM   1110 C CG    . ARG A 1 141 ? 12.40112  -9.79954  45.13837  1.000 50.93671  ? 135 ARG A CG    1 
ATOM   1111 C CD    . ARG A 1 141 ? 12.25042  -10.80949 46.26336  1.000 58.05057  ? 135 ARG A CD    1 
ATOM   1112 N NE    . ARG A 1 141 ? 13.53298  -11.37371 46.66594  1.000 58.33504  ? 135 ARG A NE    1 
ATOM   1113 C CZ    . ARG A 1 141 ? 13.68821  -12.58087 47.19212  1.000 65.05842  ? 135 ARG A CZ    1 
ATOM   1114 N NH1   . ARG A 1 141 ? 12.65689  -13.38417 47.39543  1.000 59.60989  ? 135 ARG A NH1   1 
ATOM   1115 N NH2   . ARG A 1 141 ? 14.90892  -12.99246 47.52271  1.000 67.62533  ? 135 ARG A NH2   1 
ATOM   1116 N N     . PHE A 1 142 ? 11.25496  -9.30313  41.57946  1.000 42.59127  ? 136 PHE A N     1 
ATOM   1117 C CA    . PHE A 1 142 ? 10.29624  -8.29017  41.16778  1.000 42.92799  ? 136 PHE A CA    1 
ATOM   1118 C C     . PHE A 1 142 ? 9.94390   -8.45746  39.69593  1.000 39.15176  ? 136 PHE A C     1 
ATOM   1119 O O     . PHE A 1 142 ? 10.78153  -8.84900  38.87789  1.000 40.16126  ? 136 PHE A O     1 
ATOM   1120 C CB    . PHE A 1 142 ? 10.84680  -6.88097  41.41738  1.000 46.69207  ? 136 PHE A CB    1 
ATOM   1121 C CG    . PHE A 1 142 ? 11.20459  -6.61877  42.85199  1.000 45.37963  ? 136 PHE A CG    1 
ATOM   1122 C CD1   . PHE A 1 142 ? 10.21572  -6.46013  43.80825  1.000 45.83280  ? 136 PHE A CD1   1 
ATOM   1123 C CD2   . PHE A 1 142 ? 12.53006  -6.54066  43.24624  1.000 44.07415  ? 136 PHE A CD2   1 
ATOM   1124 C CE1   . PHE A 1 142 ? 10.54121  -6.22179  45.13048  1.000 45.94260  ? 136 PHE A CE1   1 
ATOM   1125 C CE2   . PHE A 1 142 ? 12.86247  -6.30295  44.56752  1.000 44.28903  ? 136 PHE A CE2   1 
ATOM   1126 C CZ    . PHE A 1 142 ? 11.86634  -6.14356  45.51048  1.000 45.82616  ? 136 PHE A CZ    1 
ATOM   1127 N N     . LEU A 1 143 ? 8.68971   -8.15630  39.36865  1.000 38.10183  ? 137 LEU A N     1 
ATOM   1128 C CA    . LEU A 1 143 ? 8.18522   -8.22502  38.00298  1.000 37.20603  ? 137 LEU A CA    1 
ATOM   1129 C C     . LEU A 1 143 ? 7.78644   -6.82513  37.56105  1.000 39.64782  ? 137 LEU A C     1 
ATOM   1130 O O     . LEU A 1 143 ? 6.87949   -6.22149  38.14424  1.000 40.67248  ? 137 LEU A O     1 
ATOM   1131 C CB    . LEU A 1 143 ? 6.99506   -9.18169  37.90012  1.000 36.99933  ? 137 LEU A CB    1 
ATOM   1132 C CG    . LEU A 1 143 ? 6.43453   -9.41079  36.49428  1.000 37.75156  ? 137 LEU A CG    1 
ATOM   1133 C CD1   . LEU A 1 143 ? 7.47301   -10.07248 35.60178  1.000 34.18900  ? 137 LEU A CD1   1 
ATOM   1134 C CD2   . LEU A 1 143 ? 5.15837   -10.23959 36.54725  1.000 33.85930  ? 137 LEU A CD2   1 
ATOM   1135 N N     . ILE A 1 144 ? 8.46344   -6.31221  36.53938  1.000 35.60100  ? 138 ILE A N     1 
ATOM   1136 C CA    . ILE A 1 144 ? 8.17885   -4.99769  35.97730  1.000 35.46315  ? 138 ILE A CA    1 
ATOM   1137 C C     . ILE A 1 144 ? 7.46662   -5.21749  34.65018  1.000 35.68365  ? 138 ILE A C     1 
ATOM   1138 O O     . ILE A 1 144 ? 8.05148   -5.75154  33.70006  1.000 37.03524  ? 138 ILE A O     1 
ATOM   1139 C CB    . ILE A 1 144 ? 9.45383   -4.16344  35.79670  1.000 39.45497  ? 138 ILE A CB    1 
ATOM   1140 C CG1   . ILE A 1 144 ? 10.30416  -4.19862  37.07018  1.000 34.32073  ? 138 ILE A CG1   1 
ATOM   1141 C CG2   . ILE A 1 144 ? 9.10475   -2.73005  35.42381  1.000 38.71731  ? 138 ILE A CG2   1 
ATOM   1142 C CD1   . ILE A 1 144 ? 9.59257   -3.67389  38.30069  1.000 37.03957  ? 138 ILE A CD1   1 
ATOM   1143 N N     . THR A 1 145 ? 6.20267   -4.81172  34.58121  1.000 37.10151  ? 139 THR A N     1 
ATOM   1144 C CA    . THR A 1 145 ? 5.38186   -4.99177  33.38900  1.000 35.03667  ? 139 THR A CA    1 
ATOM   1145 C C     . THR A 1 145 ? 5.24989   -3.65064  32.67526  1.000 36.11802  ? 139 THR A C     1 
ATOM   1146 O O     . THR A 1 145 ? 4.55334   -2.74939  33.15441  1.000 36.71501  ? 139 THR A O     1 
ATOM   1147 C CB    . THR A 1 145 ? 4.01039   -5.55682  33.75183  1.000 36.79579  ? 139 THR A CB    1 
ATOM   1148 O OG1   . THR A 1 145 ? 3.42359   -4.75996  34.78786  1.000 43.65281  ? 139 THR A OG1   1 
ATOM   1149 C CG2   . THR A 1 145 ? 4.13837   -6.99441  34.23621  1.000 39.00081  ? 139 THR A CG2   1 
ATOM   1150 N N     . ALA A 1 146 ? 5.91776   -3.52448  31.53386  1.000 33.50195  ? 140 ALA A N     1 
ATOM   1151 C CA    . ALA A 1 146 ? 5.85197   -2.33512  30.68870  1.000 35.73484  ? 140 ALA A CA    1 
ATOM   1152 C C     . ALA A 1 146 ? 5.20673   -2.73142  29.36134  1.000 36.62052  ? 140 ALA A C     1 
ATOM   1153 O O     . ALA A 1 146 ? 5.87024   -2.78213  28.32102  1.000 32.94680  ? 140 ALA A O     1 
ATOM   1154 C CB    . ALA A 1 146 ? 7.24527   -1.73093  30.48609  1.000 31.04886  ? 140 ALA A CB    1 
ATOM   1155 N N     . LEU A 1 147 ? 3.90175   -3.00566  29.40118  1.000 36.12086  ? 141 LEU A N     1 
ATOM   1156 C CA    . LEU A 1 147 ? 3.18552   -3.57192  28.26584  1.000 33.72486  ? 141 LEU A CA    1 
ATOM   1157 C C     . LEU A 1 147 ? 2.56944   -2.52495  27.34917  1.000 40.14326  ? 141 LEU A C     1 
ATOM   1158 O O     . LEU A 1 147 ? 2.15531   -2.87035  26.23772  1.000 40.33041  ? 141 LEU A O     1 
ATOM   1159 C CB    . LEU A 1 147 ? 2.08479   -4.51454  28.75972  1.000 37.40661  ? 141 LEU A CB    1 
ATOM   1160 C CG    . LEU A 1 147 ? 2.47928   -5.48105  29.87657  1.000 36.31341  ? 141 LEU A CG    1 
ATOM   1161 C CD1   . LEU A 1 147 ? 1.28615   -6.31124  30.32109  1.000 40.40805  ? 141 LEU A CD1   1 
ATOM   1162 C CD2   . LEU A 1 147 ? 3.61561   -6.37524  29.42273  1.000 38.53490  ? 141 LEU A CD2   1 
ATOM   1163 N N     . GLY A 1 148 ? 2.48627   -1.27021  27.78087  1.000 39.35927  ? 142 GLY A N     1 
ATOM   1164 C CA    . GLY A 1 148 ? 1.90542   -0.22922  26.96848  1.000 39.39323  ? 142 GLY A CA    1 
ATOM   1165 C C     . GLY A 1 148 ? 0.41705   -0.07142  27.19987  1.000 46.78087  ? 142 GLY A C     1 
ATOM   1166 O O     . GLY A 1 148 ? -0.19593  -0.79921  27.98707  1.000 52.11573  ? 142 GLY A O     1 
ATOM   1167 N N     . PRO A 1 149 ? -0.19642  0.89460   26.51060  1.000 47.66692  ? 143 PRO A N     1 
ATOM   1168 C CA    . PRO A 1 149 ? -1.62502  1.16110   26.70439  1.000 51.41274  ? 143 PRO A CA    1 
ATOM   1169 C C     . PRO A 1 149 ? -2.55357  0.44615   25.73653  1.000 52.79369  ? 143 PRO A C     1 
ATOM   1170 O O     . PRO A 1 149 ? -3.77688  0.53883   25.90889  1.000 57.67958  ? 143 PRO A O     1 
ATOM   1171 C CB    . PRO A 1 149 ? -1.69974  2.67787   26.49174  1.000 47.81416  ? 143 PRO A CB    1 
ATOM   1172 C CG    . PRO A 1 149 ? -0.66197  2.93161   25.43349  1.000 49.06803  ? 143 PRO A CG    1 
ATOM   1173 C CD    . PRO A 1 149 ? 0.42746   1.88536   25.61481  1.000 40.27666  ? 143 PRO A CD    1 
ATOM   1174 N N     . LEU A 1 150 ? -2.02447  -0.25036  24.73471  1.000 51.70051  ? 144 LEU A N     1 
ATOM   1175 C CA    . LEU A 1 150 ? -2.83371  -0.88599  23.70589  1.000 56.12634  ? 144 LEU A CA    1 
ATOM   1176 C C     . LEU A 1 150 ? -2.60950  -2.39094  23.72239  1.000 59.65472  ? 144 LEU A C     1 
ATOM   1177 O O     . LEU A 1 150 ? -1.48937  -2.86005  23.94880  1.000 53.56855  ? 144 LEU A O     1 
ATOM   1178 C CB    . LEU A 1 150 ? -2.50195  -0.32013  22.32128  1.000 59.60796  ? 144 LEU A CB    1 
ATOM   1179 C CG    . LEU A 1 150 ? -2.74112  1.18210   22.15086  1.000 55.25691  ? 144 LEU A CG    1 
ATOM   1180 C CD1   . LEU A 1 150 ? -2.29054  1.64966   20.77542  1.000 57.65857  ? 144 LEU A CD1   1 
ATOM   1181 C CD2   . LEU A 1 150 ? -4.20572  1.52297   22.38641  1.000 56.34945  ? 144 LEU A CD2   1 
ATOM   1182 N N     . SER A 1 151 ? -3.68172  -3.14330  23.47600  1.000 59.93816  ? 145 SER A N     1 
ATOM   1183 C CA    . SER A 1 151 ? -3.60956  -4.59889  23.47294  1.000 58.67741  ? 145 SER A CA    1 
ATOM   1184 C C     . SER A 1 151 ? -3.65704  -5.16345  22.05944  1.000 59.80443  ? 145 SER A C     1 
ATOM   1185 O O     . SER A 1 151 ? -3.08358  -4.58609  21.13006  1.000 58.86324  ? 145 SER A O     1 
ATOM   1186 C CB    . SER A 1 151 ? -4.74417  -5.19381  24.30704  1.000 60.80358  ? 145 SER A CB    1 
ATOM   1187 O OG    . SER A 1 151 ? -4.44407  -6.52522  24.68141  1.000 62.82861  ? 145 SER A OG    1 
ATOM   1188 N N     . SER A 1 152 ? -4.34371  -6.29134  21.89485  1.000 60.52271  ? 146 SER A N     1 
ATOM   1189 C CA    . SER A 1 152 ? -4.37657  -6.97302  20.61329  1.000 58.95928  ? 146 SER A CA    1 
ATOM   1190 C C     . SER A 1 152 ? -5.13842  -6.14371  19.57985  1.000 57.57723  ? 146 SER A C     1 
ATOM   1191 O O     . SER A 1 152 ? -6.04467  -5.38122  19.92788  1.000 57.82568  ? 146 SER A O     1 
ATOM   1192 C CB    . SER A 1 152 ? -5.02500  -8.34689  20.75905  1.000 62.62920  ? 146 SER A CB    1 
ATOM   1193 O OG    . SER A 1 152 ? -4.13801  -9.26353  21.37663  1.000 65.73568  ? 146 SER A OG    1 
ATOM   1194 N N     . PRO A 1 153 ? -4.77923  -6.26851  18.30221  1.000 55.20551  ? 147 PRO A N     1 
ATOM   1195 C CA    . PRO A 1 153 ? -5.47447  -5.50167  17.26161  1.000 50.46258  ? 147 PRO A CA    1 
ATOM   1196 C C     . PRO A 1 153 ? -6.95110  -5.86225  17.19406  1.000 53.14419  ? 147 PRO A C     1 
ATOM   1197 O O     . PRO A 1 153 ? -7.33158  -7.03185  17.28167  1.000 55.40061  ? 147 PRO A O     1 
ATOM   1198 C CB    . PRO A 1 153 ? -4.74028  -5.90192  15.97704  1.000 47.94570  ? 147 PRO A CB    1 
ATOM   1199 C CG    . PRO A 1 153 ? -3.39959  -6.37177  16.43588  1.000 52.95358  ? 147 PRO A CG    1 
ATOM   1200 C CD    . PRO A 1 153 ? -3.63221  -7.01990  17.76526  1.000 57.22761  ? 147 PRO A CD    1 
ATOM   1201 N N     . ASN A 1 154 ? -7.78458  -4.83704  17.03632  1.000 52.49221  ? 148 ASN A N     1 
ATOM   1202 C CA    . ASN A 1 154 ? -9.23132  -4.99888  16.94888  1.000 53.50482  ? 148 ASN A CA    1 
ATOM   1203 C C     . ASN A 1 154 ? -9.63672  -4.97882  15.47933  1.000 55.24822  ? 148 ASN A C     1 
ATOM   1204 O O     . ASN A 1 154 ? -9.56714  -3.93458  14.82311  1.000 50.67937  ? 148 ASN A O     1 
ATOM   1205 C CB    . ASN A 1 154 ? -9.94856  -3.90105  17.73136  1.000 52.04343  ? 148 ASN A CB    1 
ATOM   1206 C CG    . ASN A 1 154 ? -11.45728 -3.99070  17.61242  1.000 55.91309  ? 148 ASN A CG    1 
ATOM   1207 O OD1   . ASN A 1 154 ? -12.06256 -4.99733  17.97996  1.000 55.93495  ? 148 ASN A OD1   1 
ATOM   1208 N ND2   . ASN A 1 154 ? -12.07311 -2.93423  17.09469  1.000 52.17799  ? 148 ASN A ND2   1 
ATOM   1209 N N     . TRP A 1 155 ? -10.05587 -6.14313  14.96113  1.000 57.63783  ? 149 TRP A N     1 
ATOM   1210 C CA    . TRP A 1 155 ? -10.56665 -6.26271  13.60515  1.000 54.08347  ? 149 TRP A CA    1 
ATOM   1211 C C     . TRP A 1 155 ? -12.07588 -6.04061  13.58624  1.000 53.36227  ? 149 TRP A C     1 
ATOM   1212 O O     . TRP A 1 155 ? -12.76861 -6.35709  14.55885  1.000 56.03751  ? 149 TRP A O     1 
ATOM   1213 C CB    . TRP A 1 155 ? -10.25110 -7.64268  13.03404  1.000 51.75552  ? 149 TRP A CB    1 
ATOM   1214 C CG    . TRP A 1 155 ? -8.81472  -7.84367  12.65837  1.000 54.28312  ? 149 TRP A CG    1 
ATOM   1215 C CD1   . TRP A 1 155 ? -7.82126  -8.33469  13.45372  1.000 54.43598  ? 149 TRP A CD1   1 
ATOM   1216 C CD2   . TRP A 1 155 ? -8.21290  -7.57211  11.38624  1.000 53.72406  ? 149 TRP A CD2   1 
ATOM   1217 N NE1   . TRP A 1 155 ? -6.63729  -8.38086  12.75850  1.000 59.30887  ? 149 TRP A NE1   1 
ATOM   1218 C CE2   . TRP A 1 155 ? -6.85095  -7.91810  11.48671  1.000 56.80161  ? 149 TRP A CE2   1 
ATOM   1219 C CE3   . TRP A 1 155 ? -8.69282  -7.06773  10.17371  1.000 44.39640  ? 149 TRP A CE3   1 
ATOM   1220 C CZ2   . TRP A 1 155 ? -5.96442  -7.77768  10.42108  1.000 54.34608  ? 149 TRP A CZ2   1 
ATOM   1221 C CZ3   . TRP A 1 155 ? -7.81044  -6.92752  9.11740   1.000 42.92376  ? 149 TRP A CZ3   1 
ATOM   1222 C CH2   . TRP A 1 155 ? -6.46186  -7.28005  9.24840   1.000 43.88498  ? 149 TRP A CH2   1 
ATOM   1223 N N     . PRO A 1 156 ? -12.61820 -5.49420  12.49675  1.000 52.51091  ? 150 PRO A N     1 
ATOM   1224 C CA    . PRO A 1 156 ? -14.07409 -5.31137  12.41191  1.000 49.49463  ? 150 PRO A CA    1 
ATOM   1225 C C     . PRO A 1 156 ? -14.77410 -6.63920  12.15347  1.000 50.67944  ? 150 PRO A C     1 
ATOM   1226 O O     . PRO A 1 156 ? -14.43783 -7.36178  11.21219  1.000 46.83077  ? 150 PRO A O     1 
ATOM   1227 C CB    . PRO A 1 156 ? -14.24424 -4.34873  11.23129  1.000 49.17951  ? 150 PRO A CB    1 
ATOM   1228 C CG    . PRO A 1 156 ? -13.04612 -4.59555  10.37746  1.000 45.38026  ? 150 PRO A CG    1 
ATOM   1229 C CD    . PRO A 1 156 ? -11.92081 -4.96605  11.31028  1.000 47.91060  ? 150 PRO A CD    1 
ATOM   1230 N N     . ILE A 1 157 ? -15.74930 -6.96089  13.00213  1.000 55.91140  ? 151 ILE A N     1 
ATOM   1231 C CA    . ILE A 1 157 ? -16.54909 -8.16732  12.82428  1.000 46.30070  ? 151 ILE A CA    1 
ATOM   1232 C C     . ILE A 1 157 ? -17.49962 -7.94181  11.65667  1.000 47.91416  ? 151 ILE A C     1 
ATOM   1233 O O     . ILE A 1 157 ? -18.56724 -7.33795  11.81403  1.000 47.57069  ? 151 ILE A O     1 
ATOM   1234 C CB    . ILE A 1 157 ? -17.31394 -8.53438  14.10930  1.000 51.41361  ? 151 ILE A CB    1 
ATOM   1235 C CG1   . ILE A 1 157 ? -16.33059 -8.81517  15.25102  1.000 54.30265  ? 151 ILE A CG1   1 
ATOM   1236 C CG2   . ILE A 1 157 ? -18.23302 -9.72870  13.86713  1.000 48.33103  ? 151 ILE A CG2   1 
ATOM   1237 C CD1   . ILE A 1 157 ? -15.98584 -10.28025 15.43103  1.000 62.70040  ? 151 ILE A CD1   1 
ATOM   1238 N N     . ILE A 1 158 ? -17.11014 -8.41322  10.47503  1.000 45.83146  ? 152 ILE A N     1 
ATOM   1239 C CA    . ILE A 1 158 ? -17.87164 -8.21302  9.24895   1.000 45.21345  ? 152 ILE A CA    1 
ATOM   1240 C C     . ILE A 1 158 ? -17.96589 -9.54720  8.52375   1.000 44.33647  ? 152 ILE A C     1 
ATOM   1241 O O     . ILE A 1 158 ? -16.95225 -10.23104 8.34145   1.000 46.73556  ? 152 ILE A O     1 
ATOM   1242 C CB    . ILE A 1 158 ? -17.22592 -7.14265  8.34723   1.000 47.56517  ? 152 ILE A CB    1 
ATOM   1243 C CG1   . ILE A 1 158 ? -17.39668 -5.75329  8.96671   1.000 42.87824  ? 152 ILE A CG1   1 
ATOM   1244 C CG2   . ILE A 1 158 ? -17.82400 -7.18150  6.94997   1.000 41.80544  ? 152 ILE A CG2   1 
ATOM   1245 C CD1   . ILE A 1 158 ? -16.55116 -4.68327  8.31299   1.000 42.26497  ? 152 ILE A CD1   1 
ATOM   1246 N N     . LYS A 1 159 ? -19.18008 -9.91637  8.11819   1.000 46.68542  ? 153 LYS A N     1 
ATOM   1247 C CA    . LYS A 1 159 ? -19.39715 -11.19594 7.45535   1.000 46.82149  ? 153 LYS A CA    1 
ATOM   1248 C C     . LYS A 1 159 ? -18.60385 -11.27285 6.15728   1.000 44.45987  ? 153 LYS A C     1 
ATOM   1249 O O     . LYS A 1 159 ? -18.67501 -10.37329 5.31484   1.000 43.75830  ? 153 LYS A O     1 
ATOM   1250 C CB    . LYS A 1 159 ? -20.88647 -11.39938 7.17556   1.000 41.54619  ? 153 LYS A CB    1 
ATOM   1251 C CG    . LYS A 1 159 ? -21.18161 -12.53146 6.20341   1.000 51.35204  ? 153 LYS A CG    1 
ATOM   1252 C CD    . LYS A 1 159 ? -22.66894 -12.84114 6.13896   1.000 51.42866  ? 153 LYS A CD    1 
ATOM   1253 C CE    . LYS A 1 159 ? -23.44150 -11.71525 5.47198   1.000 47.41010  ? 153 LYS A CE    1 
ATOM   1254 N NZ    . LYS A 1 159 ? -24.80570 -12.15200 5.06381   1.000 55.37380  ? 153 LYS A NZ    1 
ATOM   1255 N N     . GLY A 1 160 ? -17.84131 -12.35258 6.00314   1.000 44.20328  ? 154 GLY A N     1 
ATOM   1256 C CA    . GLY A 1 160 ? -17.07008 -12.56056 4.79553   1.000 44.78165  ? 154 GLY A CA    1 
ATOM   1257 C C     . GLY A 1 160 ? -15.76562 -11.80399 4.72191   1.000 45.44725  ? 154 GLY A C     1 
ATOM   1258 O O     . GLY A 1 160 ? -15.24307 -11.60648 3.62108   1.000 45.93524  ? 154 GLY A O     1 
ATOM   1259 N N     . ILE A 1 161 ? -15.21539 -11.37347 5.86031   1.000 44.43794  ? 155 ILE A N     1 
ATOM   1260 C CA    . ILE A 1 161 ? -13.94973 -10.64677 5.82953   1.000 44.75637  ? 155 ILE A CA    1 
ATOM   1261 C C     . ILE A 1 161 ? -12.81969 -11.55059 5.35090   1.000 46.64734  ? 155 ILE A C     1 
ATOM   1262 O O     . ILE A 1 161 ? -11.87863 -11.08738 4.69415   1.000 45.10020  ? 155 ILE A O     1 
ATOM   1263 C CB    . ILE A 1 161 ? -13.64881 -10.02944 7.20974   1.000 50.62430  ? 155 ILE A CB    1 
ATOM   1264 C CG1   . ILE A 1 161 ? -12.35890 -9.20451  7.16166   1.000 48.93315  ? 155 ILE A CG1   1 
ATOM   1265 C CG2   . ILE A 1 161 ? -13.57164 -11.10689 8.28376   1.000 45.24478  ? 155 ILE A CG2   1 
ATOM   1266 C CD1   . ILE A 1 161 ? -12.42817 -7.91109  7.94370   1.000 41.81257  ? 155 ILE A CD1   1 
ATOM   1267 N N     . GLU A 1 162 ? -12.90049 -12.84806 5.64389   1.000 45.64448  ? 156 GLU A N     1 
ATOM   1268 C CA    . GLU A 1 162 ? -11.91059 -13.81781 5.19204   1.000 44.29741  ? 156 GLU A CA    1 
ATOM   1269 C C     . GLU A 1 162 ? -12.01888 -14.12962 3.70504   1.000 43.77836  ? 156 GLU A C     1 
ATOM   1270 O O     . GLU A 1 162 ? -11.18515 -14.88123 3.18713   1.000 44.84887  ? 156 GLU A O     1 
ATOM   1271 C CB    . GLU A 1 162 ? -12.04670 -15.10884 6.00255   1.000 48.33846  ? 156 GLU A CB    1 
ATOM   1272 C CG    . GLU A 1 162 ? -13.28176 -15.93600 5.66088   1.000 50.91643  ? 156 GLU A CG    1 
ATOM   1273 C CD    . GLU A 1 162 ? -14.56882 -15.33152 6.19675   1.000 50.94357  ? 156 GLU A CD    1 
ATOM   1274 O OE1   . GLU A 1 162 ? -14.49495 -14.43964 7.06781   1.000 52.30420  ? 156 GLU A OE1   1 
ATOM   1275 O OE2   . GLU A 1 162 ? -15.65599 -15.74786 5.74551   1.000 55.11236  ? 156 GLU A OE2   1 
ATOM   1276 N N     . THR A 1 163 ? -13.01402 -13.57622 3.01283   1.000 43.63284  ? 157 THR A N     1 
ATOM   1277 C CA    . THR A 1 163 ? -13.22243 -13.84085 1.59470   1.000 43.97323  ? 157 THR A CA    1 
ATOM   1278 C C     . THR A 1 163 ? -12.42499 -12.89852 0.70032   1.000 41.80901  ? 157 THR A C     1 
ATOM   1279 O O     . THR A 1 163 ? -12.07423 -13.27355 -0.42588  1.000 41.14365  ? 157 THR A O     1 
ATOM   1280 C CB    . THR A 1 163 ? -14.71920 -13.73845 1.26917   1.000 43.73914  ? 157 THR A CB    1 
ATOM   1281 O OG1   . THR A 1 163 ? -15.44136 -14.70521 2.04351   1.000 48.37936  ? 157 THR A OG1   1 
ATOM   1282 C CG2   . THR A 1 163 ? -14.98834 -13.99581 -0.20451  1.000 49.55639  ? 157 THR A CG2   1 
ATOM   1283 N N     . PHE A 1 164 ? -12.11102 -11.69818 1.18869   1.000 39.83931  ? 158 PHE A N     1 
ATOM   1284 C CA    . PHE A 1 164 ? -11.41208 -10.70174 0.38450   1.000 37.79165  ? 158 PHE A CA    1 
ATOM   1285 C C     . PHE A 1 164 ? -10.10863 -11.26117 -0.17447  1.000 36.69927  ? 158 PHE A C     1 
ATOM   1286 O O     . PHE A 1 164 ? -9.28094  -11.80287 0.56398   1.000 35.80430  ? 158 PHE A O     1 
ATOM   1287 C CB    . PHE A 1 164 ? -11.13451 -9.45549  1.22605   1.000 39.90607  ? 158 PHE A CB    1 
ATOM   1288 C CG    . PHE A 1 164 ? -10.76229 -8.24585  0.41615   1.000 36.43927  ? 158 PHE A CG    1 
ATOM   1289 C CD1   . PHE A 1 164 ? -11.63761 -7.72871  -0.52453  1.000 34.48141  ? 158 PHE A CD1   1 
ATOM   1290 C CD2   . PHE A 1 164 ? -9.53852  -7.62430  0.59825   1.000 31.30513  ? 158 PHE A CD2   1 
ATOM   1291 C CE1   . PHE A 1 164 ? -11.29755 -6.61512  -1.27013  1.000 31.54872  ? 158 PHE A CE1   1 
ATOM   1292 C CE2   . PHE A 1 164 ? -9.19287  -6.51146  -0.14298  1.000 30.07988  ? 158 PHE A CE2   1 
ATOM   1293 C CZ    . PHE A 1 164 ? -10.07293 -6.00648  -1.07899  1.000 30.76548  ? 158 PHE A CZ    1 
ATOM   1294 N N     . LYS A 1 165 ? -9.93326  -11.12960 -1.49017  1.000 32.59751  ? 159 LYS A N     1 
ATOM   1295 C CA    . LYS A 1 165 ? -8.75361  -11.63445 -2.17908  1.000 36.96818  ? 159 LYS A CA    1 
ATOM   1296 C C     . LYS A 1 165 ? -7.67788  -10.57657 -2.38440  1.000 37.43897  ? 159 LYS A C     1 
ATOM   1297 O O     . LYS A 1 165 ? -6.54175  -10.93008 -2.71796  1.000 35.29764  ? 159 LYS A O     1 
ATOM   1298 C CB    . LYS A 1 165 ? -9.14666  -12.22562 -3.53964  1.000 37.21523  ? 159 LYS A CB    1 
ATOM   1299 C CG    . LYS A 1 165 ? -9.65795  -13.65629 -3.47158  1.000 37.96238  ? 159 LYS A CG    1 
ATOM   1300 C CD    . LYS A 1 165 ? -9.86708  -14.23466 -4.86151  1.000 42.85311  ? 159 LYS A CD    1 
ATOM   1301 C CE    . LYS A 1 165 ? -10.01653 -15.74818 -4.81649  1.000 50.44607  ? 159 LYS A CE    1 
ATOM   1302 N NZ    . LYS A 1 165 ? -10.84371 -16.19766 -3.66262  1.000 48.61743  ? 159 LYS A NZ    1 
ATOM   1303 N N     . GLY A 1 166 ? -8.00228  -9.30020  -2.20339  1.000 31.96816  ? 160 GLY A N     1 
ATOM   1304 C CA    . GLY A 1 166 ? -7.02756  -8.24085  -2.33407  1.000 32.64283  ? 160 GLY A CA    1 
ATOM   1305 C C     . GLY A 1 166 ? -6.17802  -8.09552  -1.08597  1.000 32.02720  ? 160 GLY A C     1 
ATOM   1306 O O     . GLY A 1 166 ? -6.14844  -8.95423  -0.20274  1.000 34.94581  ? 160 GLY A O     1 
ATOM   1307 N N     . GLU A 1 167 ? -5.46979  -6.97151  -1.02163  1.000 33.21812  ? 161 GLU A N     1 
ATOM   1308 C CA    . GLU A 1 167 ? -4.63261  -6.68427  0.13463   1.000 31.69777  ? 161 GLU A CA    1 
ATOM   1309 C C     . GLU A 1 167 ? -5.49552  -6.28258  1.32437   1.000 31.44400  ? 161 GLU A C     1 
ATOM   1310 O O     . GLU A 1 167 ? -6.32697  -5.37556  1.22578   1.000 29.92061  ? 161 GLU A O     1 
ATOM   1311 C CB    . GLU A 1 167 ? -3.63375  -5.57583  -0.19262  1.000 34.17458  ? 161 GLU A CB    1 
ATOM   1312 C CG    . GLU A 1 167 ? -2.68131  -5.90973  -1.32751  1.000 32.82430  ? 161 GLU A CG    1 
ATOM   1313 C CD    . GLU A 1 167 ? -1.82773  -4.72617  -1.73298  1.000 34.42737  ? 161 GLU A CD    1 
ATOM   1314 O OE1   . GLU A 1 167 ? -0.86804  -4.40523  -1.00220  1.000 40.32219  ? 161 GLU A OE1   1 
ATOM   1315 O OE2   . GLU A 1 167 ? -2.11861  -4.11392  -2.78049  1.000 36.63291  ? 161 GLU A OE2   1 
ATOM   1316 N N     . LEU A 1 168 ? -5.29494  -6.96132  2.45098   1.000 32.31239  ? 162 LEU A N     1 
ATOM   1317 C CA    . LEU A 1 168 ? -6.01327  -6.68583  3.69120   1.000 31.00770  ? 162 LEU A CA    1 
ATOM   1318 C C     . LEU A 1 168 ? -4.97982  -6.41747  4.77716   1.000 33.64513  ? 162 LEU A C     1 
ATOM   1319 O O     . LEU A 1 168 ? -4.28895  -7.33991  5.22364   1.000 35.18282  ? 162 LEU A O     1 
ATOM   1320 C CB    . LEU A 1 168 ? -6.92379  -7.85403  4.06788   1.000 33.59379  ? 162 LEU A CB    1 
ATOM   1321 C CG    . LEU A 1 168 ? -7.80926  -7.67777  5.30266   1.000 40.44298  ? 162 LEU A CG    1 
ATOM   1322 C CD1   . LEU A 1 168 ? -8.85296  -6.59823  5.06413   1.000 32.35902  ? 162 LEU A CD1   1 
ATOM   1323 C CD2   . LEU A 1 168 ? -8.47156  -8.99465  5.67495   1.000 39.56725  ? 162 LEU A CD2   1 
ATOM   1324 N N     . HIS A 1 169 ? -4.87015  -5.15937  5.19744   1.000 32.61007  ? 163 HIS A N     1 
ATOM   1325 C CA    . HIS A 1 169 ? -3.85454  -4.73398  6.15067   1.000 36.09615  ? 163 HIS A CA    1 
ATOM   1326 C C     . HIS A 1 169 ? -4.50932  -4.08730  7.36129   1.000 34.29726  ? 163 HIS A C     1 
ATOM   1327 O O     . HIS A 1 169 ? -5.41455  -3.25922  7.21584   1.000 32.57675  ? 163 HIS A O     1 
ATOM   1328 C CB    . HIS A 1 169 ? -2.87407  -3.74499  5.51179   1.000 35.82172  ? 163 HIS A CB    1 
ATOM   1329 C CG    . HIS A 1 169 ? -2.22526  -4.25220  4.26212   1.000 38.50126  ? 163 HIS A CG    1 
ATOM   1330 N ND1   . HIS A 1 169 ? -1.60928  -5.48270  4.18913   1.000 39.01432  ? 163 HIS A ND1   1 
ATOM   1331 C CD2   . HIS A 1 169 ? -2.08942  -3.69015  3.03761   1.000 38.63860  ? 163 HIS A CD2   1 
ATOM   1332 C CE1   . HIS A 1 169 ? -1.12559  -5.65895  2.97242   1.000 38.99786  ? 163 HIS A CE1   1 
ATOM   1333 N NE2   . HIS A 1 169 ? -1.40315  -4.58573  2.25412   1.000 39.75627  ? 163 HIS A NE2   1 
ATOM   1334 N N     . HIS A 1 170 ? -4.04809  -4.46659  8.54917   1.000 36.66551  ? 164 HIS A N     1 
ATOM   1335 C CA    . HIS A 1 170 ? -4.34639  -3.72957  9.76690   1.000 36.87968  ? 164 HIS A CA    1 
ATOM   1336 C C     . HIS A 1 170 ? -3.20645  -2.75855  10.03833  1.000 34.76107  ? 164 HIS A C     1 
ATOM   1337 O O     . HIS A 1 170 ? -2.03475  -3.08815  9.83118   1.000 31.23031  ? 164 HIS A O     1 
ATOM   1338 C CB    . HIS A 1 170 ? -4.53144  -4.67779  10.95298  1.000 37.16646  ? 164 HIS A CB    1 
ATOM   1339 C CG    . HIS A 1 170 ? -5.20573  -4.04918  12.13330  1.000 40.74796  ? 164 HIS A CG    1 
ATOM   1340 N ND1   . HIS A 1 170 ? -4.58530  -3.11688  12.93667  1.000 40.52800  ? 164 HIS A ND1   1 
ATOM   1341 C CD2   . HIS A 1 170 ? -6.44713  -4.22050  12.64654  1.000 44.91285  ? 164 HIS A CD2   1 
ATOM   1342 C CE1   . HIS A 1 170 ? -5.41478  -2.74113  13.89375  1.000 41.83458  ? 164 HIS A CE1   1 
ATOM   1343 N NE2   . HIS A 1 170 ? -6.55170  -3.39552  13.74004  1.000 41.19769  ? 164 HIS A NE2   1 
ATOM   1344 N N     . THR A 1 171 ? -3.55741  -1.55285  10.49202  1.000 33.07302  ? 165 THR A N     1 
ATOM   1345 C CA    . THR A 1 171 ? -2.54561  -0.51985  10.69423  1.000 33.39290  ? 165 THR A CA    1 
ATOM   1346 C C     . THR A 1 171 ? -1.51344  -0.93264  11.73616  1.000 33.01186  ? 165 THR A C     1 
ATOM   1347 O O     . THR A 1 171 ? -0.37605  -0.44997  11.70684  1.000 35.00690  ? 165 THR A O     1 
ATOM   1348 C CB    . THR A 1 171 ? -3.20956  0.79499   11.09988  1.000 30.01125  ? 165 THR A CB    1 
ATOM   1349 O OG1   . THR A 1 171 ? -4.04046  0.57846   12.24716  1.000 35.20770  ? 165 THR A OG1   1 
ATOM   1350 C CG2   . THR A 1 171 ? -4.05830  1.33708   9.95722   1.000 28.78689  ? 165 THR A CG2   1 
ATOM   1351 N N     . SER A 1 172 ? -1.88428  -1.82380  12.65628  1.000 34.76966  ? 166 SER A N     1 
ATOM   1352 C CA    . SER A 1 172 ? -0.95039  -2.31000  13.66385  1.000 38.18716  ? 166 SER A CA    1 
ATOM   1353 C C     . SER A 1 172 ? 0.06982   -3.28929  13.10057  1.000 40.95217  ? 166 SER A C     1 
ATOM   1354 O O     . SER A 1 172 ? 1.12040   -3.49269  13.71951  1.000 42.23922  ? 166 SER A O     1 
ATOM   1355 C CB    . SER A 1 172 ? -1.71327  -2.97588  14.80918  1.000 39.86616  ? 166 SER A CB    1 
ATOM   1356 O OG    . SER A 1 172 ? -2.29751  -4.19401  14.38705  1.000 44.41131  ? 166 SER A OG    1 
ATOM   1357 N N     . ARG A 1 173 ? -0.21453  -3.90120  11.95484  1.000 37.14508  ? 167 ARG A N     1 
ATOM   1358 C CA    . ARG A 1 173 ? 0.69338   -4.83479  11.29731  1.000 44.32725  ? 167 ARG A CA    1 
ATOM   1359 C C     . ARG A 1 173 ? 0.94063   -4.39621  9.86214   1.000 41.16341  ? 167 ARG A C     1 
ATOM   1360 O O     . ARG A 1 173 ? 0.78616   -5.16454  8.91047   1.000 40.38117  ? 167 ARG A O     1 
ATOM   1361 C CB    . ARG A 1 173 ? 0.14254   -6.25728  11.34305  1.000 47.38768  ? 167 ARG A CB    1 
ATOM   1362 C CG    . ARG A 1 173 ? 0.26718   -6.93195  12.70081  1.000 51.62451  ? 167 ARG A CG    1 
ATOM   1363 C CD    . ARG A 1 173 ? 1.66390   -6.76821  13.27926  1.000 58.65122  ? 167 ARG A CD    1 
ATOM   1364 N NE    . ARG A 1 173 ? 2.42607   -8.00993  13.22354  1.000 60.06083  ? 167 ARG A NE    1 
ATOM   1365 C CZ    . ARG A 1 173 ? 3.74620   -8.07485  13.11775  1.000 65.16675  ? 167 ARG A CZ    1 
ATOM   1366 N NH1   . ARG A 1 173 ? 4.48922   -6.98210  13.05548  1.000 67.25549  ? 167 ARG A NH1   1 
ATOM   1367 N NH2   . ARG A 1 173 ? 4.33589   -9.26617  13.07488  1.000 68.54461  ? 167 ARG A NH2   1 
ATOM   1368 N N     . TRP A 1 174 ? 1.32782   -3.13927  9.69306   1.000 36.56072  ? 168 TRP A N     1 
ATOM   1369 C CA    . TRP A 1 174 ? 1.55065   -2.59573  8.35975   1.000 32.42645  ? 168 TRP A CA    1 
ATOM   1370 C C     . TRP A 1 174 ? 2.80256   -3.20794  7.74806   1.000 36.93215  ? 168 TRP A C     1 
ATOM   1371 O O     . TRP A 1 174 ? 3.89603   -3.04776  8.30607   1.000 36.83390  ? 168 TRP A O     1 
ATOM   1372 C CB    . TRP A 1 174 ? 1.67848   -1.07803  8.41020   1.000 34.43064  ? 168 TRP A CB    1 
ATOM   1373 C CG    . TRP A 1 174 ? 1.59861   -0.45090  7.05674   1.000 35.26972  ? 168 TRP A CG    1 
ATOM   1374 C CD1   . TRP A 1 174 ? 2.63185   0.05288   6.32199   1.000 31.41342  ? 168 TRP A CD1   1 
ATOM   1375 C CD2   . TRP A 1 174 ? 0.41903   -0.27469  6.26506   1.000 32.63171  ? 168 TRP A CD2   1 
ATOM   1376 N NE1   . TRP A 1 174 ? 2.16672   0.53981   5.12400   1.000 33.63045  ? 168 TRP A NE1   1 
ATOM   1377 C CE2   . TRP A 1 174 ? 0.81132   0.34860   5.06433   1.000 32.40793  ? 168 TRP A CE2   1 
ATOM   1378 C CE3   . TRP A 1 174 ? -0.93184  -0.58073  6.45674   1.000 35.40611  ? 168 TRP A CE3   1 
ATOM   1379 C CZ2   . TRP A 1 174 ? -0.09772  0.67317   4.06101   1.000 32.31251  ? 168 TRP A CZ2   1 
ATOM   1380 C CZ3   . TRP A 1 174 ? -1.83294  -0.25809  5.45892   1.000 35.01844  ? 168 TRP A CZ3   1 
ATOM   1381 C CH2   . TRP A 1 174 ? -1.41180  0.36165   4.27599   1.000 35.57163  ? 168 TRP A CH2   1 
ATOM   1382 N N     . PRO A 1 175 ? 2.70056   -3.89936  6.61922   1.000 37.12417  ? 169 PRO A N     1 
ATOM   1383 C CA    . PRO A 1 175 ? 3.88360   -4.51781  6.02122   1.000 38.18183  ? 169 PRO A CA    1 
ATOM   1384 C C     . PRO A 1 175 ? 4.68306   -3.52189  5.19468   1.000 36.33041  ? 169 PRO A C     1 
ATOM   1385 O O     . PRO A 1 175 ? 4.21087   -2.44480  4.82644   1.000 41.73585  ? 169 PRO A O     1 
ATOM   1386 C CB    . PRO A 1 175 ? 3.29548   -5.62115  5.13590   1.000 42.47842  ? 169 PRO A CB    1 
ATOM   1387 C CG    . PRO A 1 175 ? 1.91235   -5.14203  4.79081   1.000 44.62738  ? 169 PRO A CG    1 
ATOM   1388 C CD    . PRO A 1 175 ? 1.49100   -4.10089  5.80259   1.000 36.12451  ? 169 PRO A CD    1 
ATOM   1389 N N     . LYS A 1 176 ? 5.92335   -3.90551  4.91395   1.000 42.72346  ? 170 LYS A N     1 
ATOM   1390 C CA    . LYS A 1 176 ? 6.79072   -3.09406  4.07929   1.000 42.00930  ? 170 LYS A CA    1 
ATOM   1391 C C     . LYS A 1 176 ? 6.41847   -3.25735  2.60818   1.000 42.49834  ? 170 LYS A C     1 
ATOM   1392 O O     . LYS A 1 176 ? 5.70357   -4.18569  2.21985   1.000 48.85266  ? 170 LYS A O     1 
ATOM   1393 C CB    . LYS A 1 176 ? 8.25478   -3.47756  4.29880   1.000 44.93860  ? 170 LYS A CB    1 
ATOM   1394 C CG    . LYS A 1 176 ? 8.46107   -4.95243  4.61528   1.000 51.52648  ? 170 LYS A CG    1 
ATOM   1395 C CD    . LYS A 1 176 ? 9.81380   -5.45097  4.13183   1.000 51.36183  ? 170 LYS A CD    1 
ATOM   1396 C CE    . LYS A 1 176 ? 10.87262  -5.32334  5.21407   1.000 52.24230  ? 170 LYS A CE    1 
ATOM   1397 N NZ    . LYS A 1 176 ? 12.21397  -5.75017  4.72720   1.000 58.72232  ? 170 LYS A NZ    1 
ATOM   1398 N N     . ASP A 1 177 ? 6.90462   -2.32010  1.79097   1.000 38.60391  ? 171 ASP A N     1 
ATOM   1399 C CA    . ASP A 1 177 ? 6.80453   -2.38309  0.33220   1.000 40.84601  ? 171 ASP A CA    1 
ATOM   1400 C C     . ASP A 1 177 ? 5.36600   -2.26983  -0.16843  1.000 37.20562  ? 171 ASP A C     1 
ATOM   1401 O O     . ASP A 1 177 ? 5.04305   -2.75978  -1.25286  1.000 40.66572  ? 171 ASP A O     1 
ATOM   1402 C CB    . ASP A 1 177 ? 7.44672   -3.66254  -0.21340  1.000 38.49955  ? 171 ASP A CB    1 
ATOM   1403 C CG    . ASP A 1 177 ? 8.86966   -3.84958  0.26527   1.000 42.90522  ? 171 ASP A CG    1 
ATOM   1404 O OD1   . ASP A 1 177 ? 9.66998   -2.89965  0.14177   1.000 49.49934  ? 171 ASP A OD1   1 
ATOM   1405 O OD2   . ASP A 1 177 ? 9.18673   -4.94675  0.76916   1.000 44.21885  ? 171 ASP A OD2   1 
ATOM   1406 N N     . VAL A 1 178 ? 4.49145   -1.62523  0.59605   1.000 39.60827  ? 172 VAL A N     1 
ATOM   1407 C CA    . VAL A 1 178 ? 3.11142   -1.42806  0.16485   1.000 36.41120  ? 172 VAL A CA    1 
ATOM   1408 C C     . VAL A 1 178 ? 3.05972   -0.27081  -0.82405  1.000 37.09845  ? 172 VAL A C     1 
ATOM   1409 O O     . VAL A 1 178 ? 3.53029   0.83488   -0.53093  1.000 36.78513  ? 172 VAL A O     1 
ATOM   1410 C CB    . VAL A 1 178 ? 2.19319   -1.17069  1.36972   1.000 36.57655  ? 172 VAL A CB    1 
ATOM   1411 C CG1   . VAL A 1 178 ? 0.85354   -0.62241  0.90397   1.000 36.99187  ? 172 VAL A CG1   1 
ATOM   1412 C CG2   . VAL A 1 178 ? 1.99979   -2.44807  2.17071   1.000 35.98835  ? 172 VAL A CG2   1 
ATOM   1413 N N     . THR A 1 179 ? 2.48885   -0.52215  -1.99949  1.000 30.63198  ? 173 THR A N     1 
ATOM   1414 C CA    . THR A 1 179 ? 2.33875   0.48768   -3.03759  1.000 36.90115  ? 173 THR A CA    1 
ATOM   1415 C C     . THR A 1 179 ? 0.86626   0.83869   -3.20880  1.000 36.05014  ? 173 THR A C     1 
ATOM   1416 O O     . THR A 1 179 ? -0.00741  -0.02532  -3.08179  1.000 34.89870  ? 173 THR A O     1 
ATOM   1417 C CB    . THR A 1 179 ? 2.91742   0.00344   -4.37003  1.000 36.58446  ? 173 THR A CB    1 
ATOM   1418 O OG1   . THR A 1 179 ? 2.09976   -1.04958  -4.89428  1.000 45.66209  ? 173 THR A OG1   1 
ATOM   1419 C CG2   . THR A 1 179 ? 4.33673   -0.51242  -4.17802  1.000 41.78250  ? 173 THR A CG2   1 
ATOM   1420 N N     . PHE A 1 180 ? 0.59676   2.11291   -3.50318  1.000 30.83922  ? 174 PHE A N     1 
ATOM   1421 C CA    . PHE A 1 180 ? -0.76631  2.61289   -3.61197  1.000 29.86503  ? 174 PHE A CA    1 
ATOM   1422 C C     . PHE A 1 180 ? -1.17030  3.01845   -5.02157  1.000 31.83023  ? 174 PHE A C     1 
ATOM   1423 O O     . PHE A 1 180 ? -2.37060  3.13102   -5.28875  1.000 30.07713  ? 174 PHE A O     1 
ATOM   1424 C CB    . PHE A 1 180 ? -0.96510  3.82580   -2.68959  1.000 31.81346  ? 174 PHE A CB    1 
ATOM   1425 C CG    . PHE A 1 180 ? -0.69201  3.54407   -1.24026  1.000 33.16440  ? 174 PHE A CG    1 
ATOM   1426 C CD1   . PHE A 1 180 ? -1.58971  2.81305   -0.48070  1.000 31.56122  ? 174 PHE A CD1   1 
ATOM   1427 C CD2   . PHE A 1 180 ? 0.45700   4.02218   -0.63390  1.000 30.04695  ? 174 PHE A CD2   1 
ATOM   1428 C CE1   . PHE A 1 180 ? -1.34164  2.55736   0.85535   1.000 30.99283  ? 174 PHE A CE1   1 
ATOM   1429 C CE2   . PHE A 1 180 ? 0.71111   3.76948   0.70112   1.000 28.91942  ? 174 PHE A CE2   1 
ATOM   1430 C CZ    . PHE A 1 180 ? -0.18989  3.03652   1.44627   1.000 28.73286  ? 174 PHE A CZ    1 
ATOM   1431 N N     . SER A 1 181 ? -0.21178  3.23644   -5.92048  1.000 33.84461  ? 175 SER A N     1 
ATOM   1432 C CA    . SER A 1 181 ? -0.51312  3.83049   -7.21770  1.000 31.48628  ? 175 SER A CA    1 
ATOM   1433 C C     . SER A 1 181 ? -1.42368  2.92972   -8.04413  1.000 30.56273  ? 175 SER A C     1 
ATOM   1434 O O     . SER A 1 181 ? -1.18975  1.72332   -8.16132  1.000 29.61661  ? 175 SER A O     1 
ATOM   1435 C CB    . SER A 1 181 ? 0.78292   4.10950   -7.97827  1.000 33.91319  ? 175 SER A CB    1 
ATOM   1436 O OG    . SER A 1 181 ? 0.51412   4.63173   -9.26738  1.000 46.69744  ? 175 SER A OG    1 
ATOM   1437 N N     . GLY A 1 182 ? -2.46631  3.52739   -8.61924  1.000 27.66943  ? 176 GLY A N     1 
ATOM   1438 C CA    . GLY A 1 182 ? -3.38429  2.81683   -9.48626  1.000 28.82348  ? 176 GLY A CA    1 
ATOM   1439 C C     . GLY A 1 182 ? -4.35094  1.88576   -8.79161  1.000 33.15570  ? 176 GLY A C     1 
ATOM   1440 O O     . GLY A 1 182 ? -5.08138  1.15855   -9.47509  1.000 31.26333  ? 176 GLY A O     1 
ATOM   1441 N N     . LYS A 1 183 ? -4.38874  1.88487   -7.46289  1.000 26.85434  ? 177 LYS A N     1 
ATOM   1442 C CA    . LYS A 1 183 ? -5.22525  0.96410   -6.70939  1.000 28.86616  ? 177 LYS A CA    1 
ATOM   1443 C C     . LYS A 1 183 ? -6.44669  1.67404   -6.13855  1.000 27.78323  ? 177 LYS A C     1 
ATOM   1444 O O     . LYS A 1 183 ? -6.39970  2.85883   -5.79892  1.000 26.38639  ? 177 LYS A O     1 
ATOM   1445 C CB    . LYS A 1 183 ? -4.43312  0.32037   -5.56907  1.000 28.43168  ? 177 LYS A CB    1 
ATOM   1446 C CG    . LYS A 1 183 ? -3.44393  -0.74442  -6.00879  1.000 29.90727  ? 177 LYS A CG    1 
ATOM   1447 C CD    . LYS A 1 183 ? -2.62948  -1.24825  -4.82912  1.000 31.50857  ? 177 LYS A CD    1 
ATOM   1448 C CE    . LYS A 1 183 ? -1.42096  -2.04548  -5.29131  1.000 32.59134  ? 177 LYS A CE    1 
ATOM   1449 N NZ    . LYS A 1 183 ? -0.52630  -2.39923  -4.15237  1.000 32.26723  ? 177 LYS A NZ    1 
ATOM   1450 N N     . ARG A 1 184 ? -7.54553  0.92989   -6.03715  1.000 27.20949  ? 178 ARG A N     1 
ATOM   1451 C CA    . ARG A 1 184 ? -8.72281  1.37111   -5.30090  1.000 23.94265  ? 178 ARG A CA    1 
ATOM   1452 C C     . ARG A 1 184 ? -8.59188  0.89137   -3.86104  1.000 27.02309  ? 178 ARG A C     1 
ATOM   1453 O O     . ARG A 1 184 ? -8.53495  -0.31741  -3.60741  1.000 23.95102  ? 178 ARG A O     1 
ATOM   1454 C CB    . ARG A 1 184 ? -10.00352 0.83389   -5.93877  1.000 26.13621  ? 178 ARG A CB    1 
ATOM   1455 C CG    . ARG A 1 184 ? -10.35557 1.48617   -7.26456  1.000 23.02177  ? 178 ARG A CG    1 
ATOM   1456 C CD    . ARG A 1 184 ? -11.59680 0.86003   -7.88100  1.000 29.06782  ? 178 ARG A CD    1 
ATOM   1457 N NE    . ARG A 1 184 ? -12.03160 1.58007   -9.07197  1.000 35.94516  ? 178 ARG A NE    1 
ATOM   1458 C CZ    . ARG A 1 184 ? -12.76698 2.68348   -9.05352  1.000 38.76182  ? 178 ARG A CZ    1 
ATOM   1459 N NH1   . ARG A 1 184 ? -13.17840 3.22155   -7.91704  1.000 34.91381  ? 178 ARG A NH1   1 
ATOM   1460 N NH2   . ARG A 1 184 ? -13.09695 3.26255   -10.20429 1.000 46.05871  ? 178 ARG A NH2   1 
ATOM   1461 N N     . VAL A 1 185 ? -8.53860  1.83336   -2.92381  1.000 22.59123  ? 179 VAL A N     1 
ATOM   1462 C CA    . VAL A 1 185 ? -8.23423  1.54171   -1.52914  1.000 23.71956  ? 179 VAL A CA    1 
ATOM   1463 C C     . VAL A 1 185 ? -9.41205  1.96662   -0.66430  1.000 25.38137  ? 179 VAL A C     1 
ATOM   1464 O O     . VAL A 1 185 ? -10.06246 2.98147   -0.93788  1.000 30.06104  ? 179 VAL A O     1 
ATOM   1465 C CB    . VAL A 1 185 ? -6.93493  2.24833   -1.08437  1.000 25.35099  ? 179 VAL A CB    1 
ATOM   1466 C CG1   . VAL A 1 185 ? -6.64414  1.98676   0.38733   1.000 22.19557  ? 179 VAL A CG1   1 
ATOM   1467 C CG2   . VAL A 1 185 ? -5.76846  1.78950   -1.94792  1.000 23.44913  ? 179 VAL A CG2   1 
ATOM   1468 N N     . GLY A 1 186 ? -9.69265  1.17751   0.36828   1.000 23.76322  ? 180 GLY A N     1 
ATOM   1469 C CA    . GLY A 1 186 ? -10.69221 1.52584   1.35644   1.000 25.09799  ? 180 GLY A CA    1 
ATOM   1470 C C     . GLY A 1 186 ? -10.07963 1.54784   2.74284   1.000 27.23912  ? 180 GLY A C     1 
ATOM   1471 O O     . GLY A 1 186 ? -9.17841  0.76561   3.05427   1.000 25.92377  ? 180 GLY A O     1 
ATOM   1472 N N     . VAL A 1 187 ? -10.57106 2.46267   3.57455   1.000 24.67992  ? 181 VAL A N     1 
ATOM   1473 C CA    . VAL A 1 187 ? -10.10823 2.60716   4.94995   1.000 26.68356  ? 181 VAL A CA    1 
ATOM   1474 C C     . VAL A 1 187 ? -11.31761 2.52131   5.86830   1.000 26.66023  ? 181 VAL A C     1 
ATOM   1475 O O     . VAL A 1 187 ? -12.27383 3.28933   5.71237   1.000 28.64709  ? 181 VAL A O     1 
ATOM   1476 C CB    . VAL A 1 187 ? -9.35371  3.92907   5.17564   1.000 26.55085  ? 181 VAL A CB    1 
ATOM   1477 C CG1   . VAL A 1 187 ? -8.89736  4.03857   6.62325   1.000 24.82029  ? 181 VAL A CG1   1 
ATOM   1478 C CG2   . VAL A 1 187 ? -8.16406  4.03121   4.23212   1.000 25.74650  ? 181 VAL A CG2   1 
ATOM   1479 N N     . ILE A 1 188 ? -11.27737 1.59288   6.81899   1.000 27.56624  ? 182 ILE A N     1 
ATOM   1480 C CA    . ILE A 1 188 ? -12.31197 1.45654   7.83763   1.000 29.53915  ? 182 ILE A CA    1 
ATOM   1481 C C     . ILE A 1 188 ? -11.77463 2.04276   9.13520   1.000 32.84610  ? 182 ILE A C     1 
ATOM   1482 O O     . ILE A 1 188 ? -10.77996 1.55190   9.68303   1.000 32.73646  ? 182 ILE A O     1 
ATOM   1483 C CB    . ILE A 1 188 ? -12.73066 -0.00966  8.02641   1.000 32.73206  ? 182 ILE A CB    1 
ATOM   1484 C CG1   . ILE A 1 188 ? -13.21358 -0.60432  6.70071   1.000 34.76762  ? 182 ILE A CG1   1 
ATOM   1485 C CG2   . ILE A 1 188 ? -13.81165 -0.11797  9.09292   1.000 33.15666  ? 182 ILE A CG2   1 
ATOM   1486 C CD1   . ILE A 1 188 ? -13.79821 -1.99496  6.83347   1.000 30.03940  ? 182 ILE A CD1   1 
ATOM   1487 N N     . GLY A 1 189 ? -12.42708 3.09272   9.62601   1.000 31.21005  ? 183 GLY A N     1 
ATOM   1488 C CA    . GLY A 1 189 ? -12.00106 3.73614   10.85178  1.000 31.51881  ? 183 GLY A CA    1 
ATOM   1489 C C     . GLY A 1 189 ? -11.48122 5.14088   10.63199  1.000 33.20765  ? 183 GLY A C     1 
ATOM   1490 O O     . GLY A 1 189 ? -10.62203 5.36647   9.77387   1.000 27.48549  ? 183 GLY A O     1 
ATOM   1491 N N     . THR A 1 190 ? -11.99860 6.09610   11.39895  1.000 31.11616  ? 184 THR A N     1 
ATOM   1492 C CA    . THR A 1 190 ? -11.60529 7.49555   11.29939  1.000 27.89719  ? 184 THR A CA    1 
ATOM   1493 C C     . THR A 1 190 ? -11.13826 8.03054   12.64801  1.000 32.18919  ? 184 THR A C     1 
ATOM   1494 O O     . THR A 1 190 ? -11.41729 9.17361   13.01641  1.000 31.22847  ? 184 THR A O     1 
ATOM   1495 C CB    . THR A 1 190 ? -12.74648 8.34836   10.75027  1.000 31.10343  ? 184 THR A CB    1 
ATOM   1496 O OG1   . THR A 1 190 ? -13.87721 8.26211   11.62594  1.000 31.33983  ? 184 THR A OG1   1 
ATOM   1497 C CG2   . THR A 1 190 ? -13.14809 7.87499   9.36106   1.000 31.85778  ? 184 THR A CG2   1 
ATOM   1498 N N     . GLY A 1 191 ? -10.42402 7.20239   13.40402  1.000 31.35881  ? 185 GLY A N     1 
ATOM   1499 C CA    . GLY A 1 191 ? -9.78839  7.63785   14.62884  1.000 32.95548  ? 185 GLY A CA    1 
ATOM   1500 C C     . GLY A 1 191 ? -8.49210  8.36356   14.33453  1.000 30.97073  ? 185 GLY A C     1 
ATOM   1501 O O     . GLY A 1 191 ? -8.26030  8.85785   13.22847  1.000 34.06679  ? 185 GLY A O     1 
ATOM   1502 N N     . SER A 1 192 ? -7.62902  8.42501   15.35118  1.000 32.60445  ? 186 SER A N     1 
ATOM   1503 C CA    . SER A 1 192 ? -6.33838  9.08400   15.17551  1.000 32.81469  ? 186 SER A CA    1 
ATOM   1504 C C     . SER A 1 192 ? -5.49162  8.36642   14.13189  1.000 29.35891  ? 186 SER A C     1 
ATOM   1505 O O     . SER A 1 192 ? -4.85290  9.00912   13.29067  1.000 29.45578  ? 186 SER A O     1 
ATOM   1506 C CB    . SER A 1 192 ? -5.59679  9.15826   16.51029  1.000 33.54001  ? 186 SER A CB    1 
ATOM   1507 O OG    . SER A 1 192 ? -5.58301  7.89768   17.15659  1.000 44.98800  ? 186 SER A OG    1 
ATOM   1508 N N     . THR A 1 193 ? -5.47896  7.03226   14.16585  1.000 31.29158  ? 187 THR A N     1 
ATOM   1509 C CA    . THR A 1 193 ? -4.71244  6.27808   13.17951  1.000 31.63951  ? 187 THR A CA    1 
ATOM   1510 C C     . THR A 1 193 ? -5.34093  6.37966   11.79423  1.000 28.94895  ? 187 THR A C     1 
ATOM   1511 O O     . THR A 1 193 ? -4.63334  6.57249   10.79839  1.000 25.04951  ? 187 THR A O     1 
ATOM   1512 C CB    . THR A 1 193 ? -4.59726  4.81588   13.60964  1.000 34.85760  ? 187 THR A CB    1 
ATOM   1513 O OG1   . THR A 1 193 ? -3.96311  4.74191   14.89207  1.000 37.56897  ? 187 THR A OG1   1 
ATOM   1514 C CG2   . THR A 1 193 ? -3.77339  4.03224   12.60485  1.000 35.19691  ? 187 THR A CG2   1 
ATOM   1515 N N     . GLY A 1 194 ? -6.66716  6.25466   11.71079  1.000 24.63904  ? 188 GLY A N     1 
ATOM   1516 C CA    . GLY A 1 194 ? -7.32745  6.34524   10.41844  1.000 25.31951  ? 188 GLY A CA    1 
ATOM   1517 C C     . GLY A 1 194 ? -7.15676  7.70436   9.76810   1.000 24.72877  ? 188 GLY A C     1 
ATOM   1518 O O     . GLY A 1 194 ? -6.92673  7.80072   8.56042   1.000 24.11714  ? 188 GLY A O     1 
ATOM   1519 N N     . VAL A 1 195 ? -7.26044  8.77294   10.56129  1.000 27.76037  ? 189 VAL A N     1 
ATOM   1520 C CA    . VAL A 1 195 ? -7.06803  10.11937  10.02972  1.000 26.72106  ? 189 VAL A CA    1 
ATOM   1521 C C     . VAL A 1 195 ? -5.65720  10.27605  9.47437   1.000 26.96760  ? 189 VAL A C     1 
ATOM   1522 O O     . VAL A 1 195 ? -5.45534  10.86571  8.40495   1.000 28.24808  ? 189 VAL A O     1 
ATOM   1523 C CB    . VAL A 1 195 ? -7.37690  11.16601  11.11765  1.000 27.49408  ? 189 VAL A CB    1 
ATOM   1524 C CG1   . VAL A 1 195 ? -6.62910  12.46103  10.85355  1.000 25.64278  ? 189 VAL A CG1   1 
ATOM   1525 C CG2   . VAL A 1 195 ? -8.87683  11.41716  11.20242  1.000 26.31139  ? 189 VAL A CG2   1 
ATOM   1526 N N     . GLN A 1 196 ? -4.66178  9.73365   10.17962  1.000 26.72858  ? 190 GLN A N     1 
ATOM   1527 C CA    . GLN A 1 196 ? -3.28276  9.83515   9.71176   1.000 23.81761  ? 190 GLN A CA    1 
ATOM   1528 C C     . GLN A 1 196 ? -3.07628  9.05804   8.41679   1.000 24.24375  ? 190 GLN A C     1 
ATOM   1529 O O     . GLN A 1 196 ? -2.42390  9.55149   7.48926   1.000 25.83559  ? 190 GLN A O     1 
ATOM   1530 C CB    . GLN A 1 196 ? -2.32469  9.34063   10.79538  1.000 28.59645  ? 190 GLN A CB    1 
ATOM   1531 C CG    . GLN A 1 196 ? -2.10579  10.33532  11.92331  1.000 27.29574  ? 190 GLN A CG    1 
ATOM   1532 C CD    . GLN A 1 196 ? -1.28361  9.75964   13.05983  1.000 33.91553  ? 190 GLN A CD    1 
ATOM   1533 O OE1   . GLN A 1 196 ? -0.96148  8.57237   13.06988  1.000 34.82815  ? 190 GLN A OE1   1 
ATOM   1534 N NE2   . GLN A 1 196 ? -0.93831  10.60260  14.02500  1.000 34.02778  ? 190 GLN A NE2   1 
ATOM   1535 N N     . VAL A 1 197 ? -3.62741  7.84497   8.33312   1.000 25.25770  ? 191 VAL A N     1 
ATOM   1536 C CA    . VAL A 1 197 ? -3.48074  7.03767   7.12465   1.000 23.41356  ? 191 VAL A CA    1 
ATOM   1537 C C     . VAL A 1 197 ? -4.19088  7.69969   5.94995   1.000 23.74869  ? 191 VAL A C     1 
ATOM   1538 O O     . VAL A 1 197 ? -3.63741  7.80584   4.84929   1.000 29.05680  ? 191 VAL A O     1 
ATOM   1539 C CB    . VAL A 1 197 ? -4.00679  5.61059   7.36418   1.000 23.83266  ? 191 VAL A CB    1 
ATOM   1540 C CG1   . VAL A 1 197 ? -4.01453  4.82157   6.06301   1.000 25.95642  ? 191 VAL A CG1   1 
ATOM   1541 C CG2   . VAL A 1 197 ? -3.16919  4.90278   8.41487   1.000 26.01434  ? 191 VAL A CG2   1 
ATOM   1542 N N     . ILE A 1 198 ? -5.42713  8.15547   6.16751   1.000 26.54384  ? 192 ILE A N     1 
ATOM   1543 C CA    . ILE A 1 198 ? -6.22171  8.72358   5.07938   1.000 25.24285  ? 192 ILE A CA    1 
ATOM   1544 C C     . ILE A 1 198 ? -5.54180  9.96368   4.51215   1.000 25.42619  ? 192 ILE A C     1 
ATOM   1545 O O     . ILE A 1 198 ? -5.44800  10.14096  3.29138   1.000 27.27792  ? 192 ILE A O     1 
ATOM   1546 C CB    . ILE A 1 198 ? -7.64878  9.03348   5.56660   1.000 25.52018  ? 192 ILE A CB    1 
ATOM   1547 C CG1   . ILE A 1 198 ? -8.44866  7.73723   5.72003   1.000 25.95318  ? 192 ILE A CG1   1 
ATOM   1548 C CG2   . ILE A 1 198 ? -8.34535  10.00063  4.61704   1.000 24.50902  ? 192 ILE A CG2   1 
ATOM   1549 C CD1   . ILE A 1 198 ? -9.62554  7.85563   6.66497   1.000 28.98997  ? 192 ILE A CD1   1 
ATOM   1550 N N     . THR A 1 199 ? -5.05201  10.83852  5.39299   1.000 24.94181  ? 193 THR A N     1 
ATOM   1551 C CA    . THR A 1 199 ? -4.39044  12.05737  4.93883   1.000 27.73594  ? 193 THR A CA    1 
ATOM   1552 C C     . THR A 1 199 ? -3.10604  11.75220  4.17669   1.000 25.99512  ? 193 THR A C     1 
ATOM   1553 O O     . THR A 1 199 ? -2.72141  12.50868  3.27716   1.000 31.29870  ? 193 THR A O     1 
ATOM   1554 C CB    . THR A 1 199 ? -4.09570  12.96514  6.13571   1.000 28.38739  ? 193 THR A CB    1 
ATOM   1555 O OG1   . THR A 1 199 ? -5.28781  13.13148  6.91318   1.000 28.55737  ? 193 THR A OG1   1 
ATOM   1556 C CG2   . THR A 1 199 ? -3.60350  14.32998  5.67546   1.000 25.59446  ? 193 THR A CG2   1 
ATOM   1557 N N     . ALA A 1 200 ? -2.43890  10.64601  4.50612   1.000 27.46169  ? 194 ALA A N     1 
ATOM   1558 C CA    . ALA A 1 200 ? -1.14112  10.35646  3.90829   1.000 29.32556  ? 194 ALA A CA    1 
ATOM   1559 C C     . ALA A 1 200 ? -1.25331  9.65201   2.56054   1.000 31.50978  ? 194 ALA A C     1 
ATOM   1560 O O     . ALA A 1 200 ? -0.35489  9.79051   1.72296   1.000 29.92964  ? 194 ALA A O     1 
ATOM   1561 C CB    . ALA A 1 200 ? -0.30259  9.50821   4.86586   1.000 27.24462  ? 194 ALA A CB    1 
ATOM   1562 N N     . ILE A 1 201 ? -2.32925  8.90159   2.32462   1.000 27.25701  ? 195 ILE A N     1 
ATOM   1563 C CA    . ILE A 1 201 ? -2.41397  8.03023   1.15509   1.000 28.01081  ? 195 ILE A CA    1 
ATOM   1564 C C     . ILE A 1 201 ? -3.42546  8.49720   0.12030   1.000 28.18952  ? 195 ILE A C     1 
ATOM   1565 O O     . ILE A 1 201 ? -3.47144  7.91403   -0.97551  1.000 28.07631  ? 195 ILE A O     1 
ATOM   1566 C CB    . ILE A 1 201 ? -2.72354  6.57291   1.55860   1.000 30.99287  ? 195 ILE A CB    1 
ATOM   1567 C CG1   . ILE A 1 201 ? -4.20663  6.41877   1.90634   1.000 24.55323  ? 195 ILE A CG1   1 
ATOM   1568 C CG2   . ILE A 1 201 ? -1.84097  6.14152   2.72308   1.000 24.48959  ? 195 ILE A CG2   1 
ATOM   1569 C CD1   . ILE A 1 201 ? -4.63670  4.98323   2.12388   1.000 25.72934  ? 195 ILE A CD1   1 
ATOM   1570 N N     . ALA A 1 202 ? -4.23184  9.51962   0.41660   1.000 28.24905  ? 196 ALA A N     1 
ATOM   1571 C CA    . ALA A 1 202 ? -5.28691  9.91716   -0.51233  1.000 27.23485  ? 196 ALA A CA    1 
ATOM   1572 C C     . ALA A 1 202 ? -4.71663  10.36813  -1.85170  1.000 30.08976  ? 196 ALA A C     1 
ATOM   1573 O O     . ALA A 1 202 ? -5.28854  10.07440  -2.90832  1.000 28.19362  ? 196 ALA A O     1 
ATOM   1574 C CB    . ALA A 1 202 ? -6.14053  11.02314  0.10326   1.000 26.30782  ? 196 ALA A CB    1 
ATOM   1575 N N     . SER A 1 203 ? -3.58936  11.07895  -1.83087  1.000 28.68358  ? 197 SER A N     1 
ATOM   1576 C CA    . SER A 1 203 ? -2.97667  11.56135  -3.06149  1.000 28.89101  ? 197 SER A CA    1 
ATOM   1577 C C     . SER A 1 203 ? -2.20587  10.48121  -3.80928  1.000 27.33408  ? 197 SER A C     1 
ATOM   1578 O O     . SER A 1 203 ? -1.76012  10.73163  -4.93401  1.000 31.12639  ? 197 SER A O     1 
ATOM   1579 C CB    . SER A 1 203 ? -2.04314  12.73706  -2.75789  1.000 30.21769  ? 197 SER A CB    1 
ATOM   1580 O OG    . SER A 1 203 ? -0.93299  12.32072  -1.98221  1.000 31.06872  ? 197 SER A OG    1 
ATOM   1581 N N     . GLN A 1 204 ? -2.04380  9.29382   -3.22509  1.000 28.68632  ? 198 GLN A N     1 
ATOM   1582 C CA    . GLN A 1 204 ? -1.25244  8.23159   -3.83147  1.000 26.78625  ? 198 GLN A CA    1 
ATOM   1583 C C     . GLN A 1 204 ? -2.09219  7.13457   -4.47362  1.000 30.00585  ? 198 GLN A C     1 
ATOM   1584 O O     . GLN A 1 204 ? -1.54393  6.32255   -5.22649  1.000 33.66370  ? 198 GLN A O     1 
ATOM   1585 C CB    . GLN A 1 204 ? -0.32591  7.59822   -2.78564  1.000 31.10323  ? 198 GLN A CB    1 
ATOM   1586 C CG    . GLN A 1 204 ? 0.57644   8.58366   -2.06551  1.000 32.14970  ? 198 GLN A CG    1 
ATOM   1587 C CD    . GLN A 1 204 ? 1.49949   7.90052   -1.07695  1.000 38.43608  ? 198 GLN A CD    1 
ATOM   1588 O OE1   . GLN A 1 204 ? 2.41571   7.17697   -1.46581  1.000 40.20643  ? 198 GLN A OE1   1 
ATOM   1589 N NE2   . GLN A 1 204 ? 1.26044   8.12447   0.21068   1.000 32.83434  ? 198 GLN A NE2   1 
ATOM   1590 N N     . VAL A 1 205 ? -3.39199  7.08529   -4.20143  1.000 26.91000  ? 199 VAL A N     1 
ATOM   1591 C CA    . VAL A 1 205 ? -4.23978  6.00346   -4.67312  1.000 23.99206  ? 199 VAL A CA    1 
ATOM   1592 C C     . VAL A 1 205 ? -5.04683  6.47493   -5.87517  1.000 28.09639  ? 199 VAL A C     1 
ATOM   1593 O O     . VAL A 1 205 ? -5.22116  7.67310   -6.11732  1.000 27.00586  ? 199 VAL A O     1 
ATOM   1594 C CB    . VAL A 1 205 ? -5.17170  5.48110   -3.55534  1.000 25.21728  ? 199 VAL A CB    1 
ATOM   1595 C CG1   . VAL A 1 205 ? -4.36254  5.09015   -2.33042  1.000 24.63517  ? 199 VAL A CG1   1 
ATOM   1596 C CG2   . VAL A 1 205 ? -6.21366  6.53086   -3.19785  1.000 28.69967  ? 199 VAL A CG2   1 
ATOM   1597 N N     . LYS A 1 206 ? -5.54669  5.50784   -6.64932  1.000 27.13613  ? 200 LYS A N     1 
ATOM   1598 C CA    . LYS A 1 206 ? -6.46313  5.83522   -7.73657  1.000 28.02034  ? 200 LYS A CA    1 
ATOM   1599 C C     . LYS A 1 206 ? -7.79687  6.33130   -7.19408  1.000 27.64757  ? 200 LYS A C     1 
ATOM   1600 O O     . LYS A 1 206 ? -8.35655  7.30952   -7.70240  1.000 27.30285  ? 200 LYS A O     1 
ATOM   1601 C CB    . LYS A 1 206 ? -6.67065  4.61799   -8.63785  1.000 26.82623  ? 200 LYS A CB    1 
ATOM   1602 C CG    . LYS A 1 206 ? -7.60341  4.86960   -9.81444  1.000 28.83402  ? 200 LYS A CG    1 
ATOM   1603 C CD    . LYS A 1 206 ? -7.46121  3.79227   -10.87826 1.000 31.68081  ? 200 LYS A CD    1 
ATOM   1604 C CE    . LYS A 1 206 ? -8.02102  2.46323   -10.39686 1.000 32.78021  ? 200 LYS A CE    1 
ATOM   1605 N NZ    . LYS A 1 206 ? -7.90034  1.40450   -11.43683 1.000 35.57651  ? 200 LYS A NZ    1 
ATOM   1606 N N     . HIS A 1 207 ? -8.32010  5.66908   -6.16484  1.000 28.56681  ? 201 HIS A N     1 
ATOM   1607 C CA    . HIS A 1 207 ? -9.54455  6.09955   -5.50748  1.000 28.86871  ? 201 HIS A CA    1 
ATOM   1608 C C     . HIS A 1 207 ? -9.51008  5.63191   -4.06164  1.000 28.34035  ? 201 HIS A C     1 
ATOM   1609 O O     . HIS A 1 207 ? -9.01704  4.53940   -3.76761  1.000 28.02885  ? 201 HIS A O     1 
ATOM   1610 C CB    . HIS A 1 207 ? -10.79169 5.55429   -6.21171  1.000 29.08465  ? 201 HIS A CB    1 
ATOM   1611 C CG    . HIS A 1 207 ? -12.07208 6.15108   -5.71584  1.000 30.61104  ? 201 HIS A CG    1 
ATOM   1612 N ND1   . HIS A 1 207 ? -12.62685 7.28597   -6.26744  1.000 33.69429  ? 201 HIS A ND1   1 
ATOM   1613 C CD2   . HIS A 1 207 ? -12.90298 5.77439   -4.71523  1.000 28.22047  ? 201 HIS A CD2   1 
ATOM   1614 C CE1   . HIS A 1 207 ? -13.74575 7.58094   -5.62998  1.000 33.70001  ? 201 HIS A CE1   1 
ATOM   1615 N NE2   . HIS A 1 207 ? -13.93613 6.67942   -4.68360  1.000 33.56771  ? 201 HIS A NE2   1 
ATOM   1616 N N     . LEU A 1 208 ? -10.02926 6.46642   -3.16540  1.000 26.63980  ? 202 LEU A N     1 
ATOM   1617 C CA    . LEU A 1 208 ? -10.06494 6.17094   -1.74018  1.000 26.76351  ? 202 LEU A CA    1 
ATOM   1618 C C     . LEU A 1 208 ? -11.49739 6.26781   -1.23891  1.000 28.80539  ? 202 LEU A C     1 
ATOM   1619 O O     . LEU A 1 208 ? -12.15774 7.29503   -1.42671  1.000 27.90695  ? 202 LEU A O     1 
ATOM   1620 C CB    . LEU A 1 208 ? -9.16680  7.12854   -0.95102  1.000 25.97316  ? 202 LEU A CB    1 
ATOM   1621 C CG    . LEU A 1 208 ? -9.11192  6.89464   0.56049   1.000 29.28851  ? 202 LEU A CG    1 
ATOM   1622 C CD1   . LEU A 1 208 ? -8.40979  5.58137   0.87681   1.000 22.57172  ? 202 LEU A CD1   1 
ATOM   1623 C CD2   . LEU A 1 208 ? -8.43055  8.05832   1.26732   1.000 28.26493  ? 202 LEU A CD2   1 
ATOM   1624 N N     . THR A 1 209 ? -11.97302 5.20085   -0.60625  1.000 27.23259  ? 203 THR A N     1 
ATOM   1625 C CA    . THR A 1 209 ? -13.27615 5.18520   0.04450   1.000 28.77112  ? 203 THR A CA    1 
ATOM   1626 C C     . THR A 1 209 ? -13.05858 5.11716   1.54877   1.000 26.45479  ? 203 THR A C     1 
ATOM   1627 O O     . THR A 1 209 ? -12.38853 4.20347   2.04153   1.000 27.63037  ? 203 THR A O     1 
ATOM   1628 C CB    . THR A 1 209 ? -14.12525 4.00492   -0.42716  1.000 28.87295  ? 203 THR A CB    1 
ATOM   1629 O OG1   . THR A 1 209 ? -14.24276 4.03551   -1.85485  1.000 28.65124  ? 203 THR A OG1   1 
ATOM   1630 C CG2   . THR A 1 209 ? -15.51432 4.07759   0.19033   1.000 28.26011  ? 203 THR A CG2   1 
ATOM   1631 N N     . VAL A 1 210 ? -13.61680 6.08186   2.27048   1.000 26.30044  ? 204 VAL A N     1 
ATOM   1632 C CA    . VAL A 1 210 ? -13.49623 6.15098   3.72079   1.000 26.89518  ? 204 VAL A CA    1 
ATOM   1633 C C     . VAL A 1 210 ? -14.79944 5.65298   4.32875   1.000 27.74178  ? 204 VAL A C     1 
ATOM   1634 O O     . VAL A 1 210 ? -15.86600 6.23526   4.09562   1.000 31.50233  ? 204 VAL A O     1 
ATOM   1635 C CB    . VAL A 1 210 ? -13.17308 7.57809   4.18927   1.000 26.91391  ? 204 VAL A CB    1 
ATOM   1636 C CG1   . VAL A 1 210 ? -13.17787 7.64945   5.70522   1.000 26.10758  ? 204 VAL A CG1   1 
ATOM   1637 C CG2   . VAL A 1 210 ? -11.82880 8.02619   3.63218   1.000 24.17126  ? 204 VAL A CG2   1 
ATOM   1638 N N     . PHE A 1 211 ? -14.71673 4.57183   5.10055   1.000 28.36493  ? 205 PHE A N     1 
ATOM   1639 C CA    . PHE A 1 211 ? -15.87444 3.98932   5.77588   1.000 28.60530  ? 205 PHE A CA    1 
ATOM   1640 C C     . PHE A 1 211 ? -15.89559 4.52496   7.20312   1.000 32.04574  ? 205 PHE A C     1 
ATOM   1641 O O     . PHE A 1 211 ? -15.16414 4.04516   8.07323   1.000 30.81688  ? 205 PHE A O     1 
ATOM   1642 C CB    . PHE A 1 211 ? -15.81590 2.46665   5.73492   1.000 29.79084  ? 205 PHE A CB    1 
ATOM   1643 C CG    . PHE A 1 211 ? -15.81073 1.90185   4.34209   1.000 28.20582  ? 205 PHE A CG    1 
ATOM   1644 C CD1   . PHE A 1 211 ? -16.98347 1.82535   3.60782   1.000 30.51155  ? 205 PHE A CD1   1 
ATOM   1645 C CD2   . PHE A 1 211 ? -14.63392 1.45424   3.76423   1.000 26.11902  ? 205 PHE A CD2   1 
ATOM   1646 C CE1   . PHE A 1 211 ? -16.98404 1.30932   2.32644   1.000 25.25477  ? 205 PHE A CE1   1 
ATOM   1647 C CE2   . PHE A 1 211 ? -14.62805 0.93630   2.48098   1.000 27.76154  ? 205 PHE A CE2   1 
ATOM   1648 C CZ    . PHE A 1 211 ? -15.80455 0.86411   1.76219   1.000 24.80514  ? 205 PHE A CZ    1 
ATOM   1649 N N     . GLN A 1 212 ? -16.74390 5.52048   7.43784   1.000 27.65503  ? 206 GLN A N     1 
ATOM   1650 C CA    . GLN A 1 212 ? -16.77661 6.26836   8.68763   1.000 28.59113  ? 206 GLN A CA    1 
ATOM   1651 C C     . GLN A 1 212 ? -18.01375 5.87610   9.48433   1.000 31.84724  ? 206 GLN A C     1 
ATOM   1652 O O     . GLN A 1 212 ? -19.14275 6.07857   9.02392   1.000 33.27478  ? 206 GLN A O     1 
ATOM   1653 C CB    . GLN A 1 212 ? -16.76903 7.77114   8.40757   1.000 29.40037  ? 206 GLN A CB    1 
ATOM   1654 C CG    . GLN A 1 212 ? -16.99389 8.64704   9.62618   1.000 30.63984  ? 206 GLN A CG    1 
ATOM   1655 C CD    . GLN A 1 212 ? -17.39157 10.05858  9.24789   1.000 30.55796  ? 206 GLN A CD    1 
ATOM   1656 O OE1   . GLN A 1 212 ? -16.53935 10.92885  9.07100   1.000 28.35502  ? 206 GLN A OE1   1 
ATOM   1657 N NE2   . GLN A 1 212 ? -18.69276 10.29169  9.11336   1.000 27.90699  ? 206 GLN A NE2   1 
ATOM   1658 N N     . ARG A 1 213 ? -17.79928 5.31754   10.67599  1.000 32.76142  ? 207 ARG A N     1 
ATOM   1659 C CA    . ARG A 1 213 ? -18.90296 4.99168   11.57161  1.000 39.64780  ? 207 ARG A CA    1 
ATOM   1660 C C     . ARG A 1 213 ? -19.24990 6.14730   12.50046  1.000 42.87281  ? 207 ARG A C     1 
ATOM   1661 O O     . ARG A 1 213 ? -20.43163 6.40345   12.75700  1.000 42.26711  ? 207 ARG A O     1 
ATOM   1662 C CB    . ARG A 1 213 ? -18.57000 3.74528   12.39741  1.000 38.62266  ? 207 ARG A CB    1 
ATOM   1663 C CG    . ARG A 1 213 ? -19.68227 3.32703   13.34928  1.000 44.69308  ? 207 ARG A CG    1 
ATOM   1664 C CD    . ARG A 1 213 ? -19.77795 1.81578   13.48348  1.000 45.68413  ? 207 ARG A CD    1 
ATOM   1665 N NE    . ARG A 1 213 ? -18.85068 1.29342   14.47989  1.000 51.79120  ? 207 ARG A NE    1 
ATOM   1666 C CZ    . ARG A 1 213 ? -18.77730 0.01917   14.83932  1.000 49.40748  ? 207 ARG A CZ    1 
ATOM   1667 N NH1   . ARG A 1 213 ? -19.56904 -0.89643  14.30553  1.000 56.21676  ? 207 ARG A NH1   1 
ATOM   1668 N NH2   . ARG A 1 213 ? -17.88932 -0.34512  15.75973  1.000 50.84310  ? 207 ARG A NH2   1 
ATOM   1669 N N     . SER A 1 214 ? -18.24191 6.85346   13.00641  1.000 36.98397  ? 208 SER A N     1 
ATOM   1670 C CA    . SER A 1 214 ? -18.45362 7.97507   13.91621  1.000 39.93486  ? 208 SER A CA    1 
ATOM   1671 C C     . SER A 1 214 ? -17.48240 9.08286   13.53747  1.000 36.81877  ? 208 SER A C     1 
ATOM   1672 O O     . SER A 1 214 ? -16.26743 8.92738   13.69754  1.000 35.25677  ? 208 SER A O     1 
ATOM   1673 C CB    . SER A 1 214 ? -18.25935 7.55226   15.37225  1.000 40.28073  ? 208 SER A CB    1 
ATOM   1674 O OG    . SER A 1 214 ? -18.56013 6.17861   15.54713  1.000 50.75347  ? 208 SER A OG    1 
ATOM   1675 N N     . ALA A 1 215 ? -18.01405 10.19063  13.02960  1.000 32.29673  ? 209 ALA A N     1 
ATOM   1676 C CA    . ALA A 1 215 ? -17.18189 11.34565  12.73036  1.000 32.09094  ? 209 ALA A CA    1 
ATOM   1677 C C     . ALA A 1 215 ? -16.68041 11.97760  14.02171  1.000 34.75425  ? 209 ALA A C     1 
ATOM   1678 O O     . ALA A 1 215 ? -17.43558 12.15091  14.98220  1.000 31.96087  ? 209 ALA A O     1 
ATOM   1679 C CB    . ALA A 1 215 ? -17.96429 12.36961  11.90995  1.000 31.46082  ? 209 ALA A CB    1 
ATOM   1680 N N     . GLN A 1 216 ? -15.39526 12.31573  14.04425  1.000 30.92344  ? 210 GLN A N     1 
ATOM   1681 C CA    . GLN A 1 216 ? -14.76543 12.91273  15.20957  1.000 31.88205  ? 210 GLN A CA    1 
ATOM   1682 C C     . GLN A 1 216 ? -14.20072 14.28043  14.85204  1.000 31.36461  ? 210 GLN A C     1 
ATOM   1683 O O     . GLN A 1 216 ? -13.96131 14.59413  13.68256  1.000 30.81141  ? 210 GLN A O     1 
ATOM   1684 C CB    . GLN A 1 216 ? -13.65050 12.01407  15.76405  1.000 37.06134  ? 210 GLN A CB    1 
ATOM   1685 C CG    . GLN A 1 216 ? -14.15270 10.77319  16.48749  1.000 35.33184  ? 210 GLN A CG    1 
ATOM   1686 C CD    . GLN A 1 216 ? -13.03560 9.99296   17.15231  1.000 47.20945  ? 210 GLN A CD    1 
ATOM   1687 O OE1   . GLN A 1 216 ? -12.75529 8.85141   16.78492  1.000 45.03878  ? 210 GLN A OE1   1 
ATOM   1688 N NE2   . GLN A 1 216 ? -12.39075 10.60663  18.13819  1.000 43.95998  ? 210 GLN A NE2   1 
ATOM   1689 N N     . TYR A 1 217 ? -13.99457 15.09635  15.88109  1.000 30.96611  ? 211 TYR A N     1 
ATOM   1690 C CA    . TYR A 1 217 ? -13.39436 16.40838  15.69965  1.000 32.69542  ? 211 TYR A CA    1 
ATOM   1691 C C     . TYR A 1 217 ? -11.88763 16.27372  15.53329  1.000 32.85382  ? 211 TYR A C     1 
ATOM   1692 O O     . TYR A 1 217 ? -11.24752 15.44631  16.18763  1.000 34.23342  ? 211 TYR A O     1 
ATOM   1693 C CB    . TYR A 1 217 ? -13.70936 17.31158  16.89205  1.000 36.25877  ? 211 TYR A CB    1 
ATOM   1694 C CG    . TYR A 1 217 ? -15.18649 17.55099  17.11076  1.000 38.41974  ? 211 TYR A CG    1 
ATOM   1695 C CD1   . TYR A 1 217 ? -15.83530 18.61833  16.50438  1.000 33.89805  ? 211 TYR A CD1   1 
ATOM   1696 C CD2   . TYR A 1 217 ? -15.93245 16.70836  17.92320  1.000 42.46540  ? 211 TYR A CD2   1 
ATOM   1697 C CE1   . TYR A 1 217 ? -17.18654 18.84067  16.70327  1.000 38.60231  ? 211 TYR A CE1   1 
ATOM   1698 C CE2   . TYR A 1 217 ? -17.28313 16.92173  18.12464  1.000 47.03476  ? 211 TYR A CE2   1 
ATOM   1699 C CZ    . TYR A 1 217 ? -17.90338 17.98834  17.51490  1.000 41.43244  ? 211 TYR A CZ    1 
ATOM   1700 O OH    . TYR A 1 217 ? -19.24625 18.19888  17.71971  1.000 49.69813  ? 211 TYR A OH    1 
ATOM   1701 N N     . SER A 1 218 ? -11.32298 17.09062  14.64842  1.000 33.55751  ? 212 SER A N     1 
ATOM   1702 C CA    . SER A 1 218 ? -9.88769  17.09600  14.41492  1.000 32.71473  ? 212 SER A CA    1 
ATOM   1703 C C     . SER A 1 218 ? -9.42344  18.52094  14.16388  1.000 32.42252  ? 212 SER A C     1 
ATOM   1704 O O     . SER A 1 218 ? -10.10343 19.29588  13.48563  1.000 31.09549  ? 212 SER A O     1 
ATOM   1705 C CB    . SER A 1 218 ? -9.50216  16.20198  13.22934  1.000 32.58253  ? 212 SER A CB    1 
ATOM   1706 O OG    . SER A 1 218 ? -8.09864  16.01140  13.17574  1.000 33.05301  ? 212 SER A OG    1 
ATOM   1707 N N     . VAL A 1 219 ? -8.26748  18.85583  14.71771  1.000 29.04704  ? 213 VAL A N     1 
ATOM   1708 C CA    . VAL A 1 219 ? -7.66674  20.17551  14.54740  1.000 29.65922  ? 213 VAL A CA    1 
ATOM   1709 C C     . VAL A 1 219 ? -6.34550  19.98314  13.82018  1.000 31.35788  ? 213 VAL A C     1 
ATOM   1710 O O     . VAL A 1 219 ? -5.78169  18.87464  13.81056  1.000 27.49270  ? 213 VAL A O     1 
ATOM   1711 C CB    . VAL A 1 219 ? -7.47899  20.89768  15.90201  1.000 33.53355  ? 213 VAL A CB    1 
ATOM   1712 C CG1   . VAL A 1 219 ? -8.80930  21.01791  16.62831  1.000 35.62504  ? 213 VAL A CG1   1 
ATOM   1713 C CG2   . VAL A 1 219 ? -6.46304  20.16074  16.75703  1.000 34.24892  ? 213 VAL A CG2   1 
ATOM   1714 N N     . PRO A 1 220 ? -5.82588  21.03049  13.17838  1.000 28.37684  ? 214 PRO A N     1 
ATOM   1715 C CA    . PRO A 1 220 ? -4.50931  20.91186  12.54607  1.000 27.71479  ? 214 PRO A CA    1 
ATOM   1716 C C     . PRO A 1 220 ? -3.43709  20.65287  13.59031  1.000 31.12093  ? 214 PRO A C     1 
ATOM   1717 O O     . PRO A 1 220 ? -3.52392  21.11452  14.72976  1.000 31.56545  ? 214 PRO A O     1 
ATOM   1718 C CB    . PRO A 1 220 ? -4.31091  22.27234  11.86502  1.000 25.89296  ? 214 PRO A CB    1 
ATOM   1719 C CG    . PRO A 1 220 ? -5.67945  22.85483  11.75269  1.000 29.54560  ? 214 PRO A CG    1 
ATOM   1720 C CD    . PRO A 1 220 ? -6.42579  22.35438  12.94732  1.000 29.30977  ? 214 PRO A CD    1 
ATOM   1721 N N     . ILE A 1 221 ? -2.42527  19.88185  13.19641  1.000 34.23348  ? 215 ILE A N     1 
ATOM   1722 C CA    . ILE A 1 221 ? -1.29433  19.64688  14.08405  1.000 33.59168  ? 215 ILE A CA    1 
ATOM   1723 C C     . ILE A 1 221 ? -0.18264  20.66784  13.86873  1.000 30.01845  ? 215 ILE A C     1 
ATOM   1724 O O     . ILE A 1 221 ? 0.60087   20.92029  14.79495  1.000 34.83737  ? 215 ILE A O     1 
ATOM   1725 C CB    . ILE A 1 221 ? -0.75983  18.21074  13.92231  1.000 29.43169  ? 215 ILE A CB    1 
ATOM   1726 C CG1   . ILE A 1 221 ? 0.03866   17.79613  15.16123  1.000 34.59359  ? 215 ILE A CG1   1 
ATOM   1727 C CG2   . ILE A 1 221 ? 0.07828   18.07666  12.65877  1.000 29.59987  ? 215 ILE A CG2   1 
ATOM   1728 C CD1   . ILE A 1 221 ? 0.69370   16.44079  15.04248  1.000 36.72361  ? 215 ILE A CD1   1 
ATOM   1729 N N     . GLY A 1 222 ? -0.11006  21.28128  12.69182  1.000 30.88303  ? 216 GLY A N     1 
ATOM   1730 C CA    . GLY A 1 222 ? 0.89908   22.29131  12.42431  1.000 34.84153  ? 216 GLY A CA    1 
ATOM   1731 C C     . GLY A 1 222 ? 2.31553   21.76060  12.39943  1.000 34.08772  ? 216 GLY A C     1 
ATOM   1732 O O     . GLY A 1 222 ? 3.23153   22.42742  12.89784  1.000 34.92827  ? 216 GLY A O     1 
ATOM   1733 N N     . ASN A 1 223 ? 2.51973   20.57424  11.83212  1.000 28.28509  ? 217 ASN A N     1 
ATOM   1734 C CA    . ASN A 1 223 ? 3.84978   19.97938  11.76040  1.000 26.00741  ? 217 ASN A CA    1 
ATOM   1735 C C     . ASN A 1 223 ? 4.68630   20.73368  10.73500  1.000 32.08710  ? 217 ASN A C     1 
ATOM   1736 O O     . ASN A 1 223 ? 4.45249   20.62209  9.52738   1.000 37.10648  ? 217 ASN A O     1 
ATOM   1737 C CB    . ASN A 1 223 ? 3.74862   18.50021  11.40263  1.000 23.32603  ? 217 ASN A CB    1 
ATOM   1738 C CG    . ASN A 1 223 ? 5.02647   17.74197  11.69973  1.000 26.59830  ? 217 ASN A CG    1 
ATOM   1739 O OD1   . ASN A 1 223 ? 5.85675   18.18861  12.49259  1.000 28.46231  ? 217 ASN A OD1   1 
ATOM   1740 N ND2   . ASN A 1 223 ? 5.19250   16.58879  11.06240  1.000 26.50654  ? 217 ASN A ND2   1 
ATOM   1741 N N     . VAL A 1 224 ? 5.66087   21.50487  11.21269  1.000 27.67710  ? 218 VAL A N     1 
ATOM   1742 C CA    . VAL A 1 224 ? 6.53506   22.28386  10.34941  1.000 28.89373  ? 218 VAL A CA    1 
ATOM   1743 C C     . VAL A 1 224 ? 7.97958   21.91007  10.65088  1.000 28.55112  ? 218 VAL A C     1 
ATOM   1744 O O     . VAL A 1 224 ? 8.29891   21.35729  11.70628  1.000 29.12806  ? 218 VAL A O     1 
ATOM   1745 C CB    . VAL A 1 224 ? 6.32124   23.80285  10.51831  1.000 29.73703  ? 218 VAL A CB    1 
ATOM   1746 C CG1   . VAL A 1 224 ? 4.92287   24.19862  10.06814  1.000 32.45446  ? 218 VAL A CG1   1 
ATOM   1747 C CG2   . VAL A 1 224 ? 6.56207   24.21697  11.96164  1.000 28.70526  ? 218 VAL A CG2   1 
ATOM   1748 N N     . VAL A 1 225 ? 8.86007   22.21770  9.69663   1.000 28.90092  ? 219 VAL A N     1 
ATOM   1749 C CA    . VAL A 1 225 ? 10.28444  21.99696  9.90633   1.000 26.98445  ? 219 VAL A CA    1 
ATOM   1750 C C     . VAL A 1 225 ? 10.79980  22.97454  10.95573  1.000 27.74618  ? 219 VAL A C     1 
ATOM   1751 O O     . VAL A 1 225 ? 10.32416  24.11257  11.07174  1.000 27.11641  ? 219 VAL A O     1 
ATOM   1752 C CB    . VAL A 1 225 ? 11.06710  22.13588  8.58735   1.000 26.55180  ? 219 VAL A CB    1 
ATOM   1753 C CG1   . VAL A 1 225 ? 10.72195  20.99743  7.64043   1.000 29.91151  ? 219 VAL A CG1   1 
ATOM   1754 C CG2   . VAL A 1 225 ? 10.78767  23.48477  7.93727   1.000 29.22334  ? 219 VAL A CG2   1 
ATOM   1755 N N     . MET A 1 226 ? 11.77988  22.52702  11.73369  1.000 27.44938  ? 220 MET A N     1 
ATOM   1756 C CA    . MET A 1 226 ? 12.35513  23.32478  12.80794  1.000 29.82389  ? 220 MET A CA    1 
ATOM   1757 C C     . MET A 1 226 ? 13.70200  23.87295  12.35418  1.000 32.30884  ? 220 MET A C     1 
ATOM   1758 O O     . MET A 1 226 ? 14.60934  23.10317  12.02083  1.000 31.42314  ? 220 MET A O     1 
ATOM   1759 C CB    . MET A 1 226 ? 12.51060  22.49056  14.07906  1.000 30.07100  ? 220 MET A CB    1 
ATOM   1760 C CG    . MET A 1 226 ? 11.20037  21.94509  14.62572  1.000 28.77163  ? 220 MET A CG    1 
ATOM   1761 S SD    . MET A 1 226 ? 10.17041  23.21380  15.38713  1.000 30.99909  ? 220 MET A SD    1 
ATOM   1762 C CE    . MET A 1 226 ? 11.03212  23.45277  16.93778  1.000 34.24520  ? 220 MET A CE    1 
ATOM   1763 N N     . SER A 1 227 ? 13.82791  25.19713  12.33935  1.000 35.05907  ? 221 SER A N     1 
ATOM   1764 C CA    . SER A 1 227 ? 15.08445  25.81898  11.95841  1.000 38.19334  ? 221 SER A CA    1 
ATOM   1765 C C     . SER A 1 227 ? 16.15047  25.55254  13.01998  1.000 38.11924  ? 221 SER A C     1 
ATOM   1766 O O     . SER A 1 227 ? 15.86402  25.11528  14.13850  1.000 39.26225  ? 221 SER A O     1 
ATOM   1767 C CB    . SER A 1 227 ? 14.90120  27.32265  11.75649  1.000 36.95452  ? 221 SER A CB    1 
ATOM   1768 O OG    . SER A 1 227 ? 14.73230  27.98595  12.99678  1.000 42.35249  ? 221 SER A OG    1 
ATOM   1769 N N     . GLU A 1 228 ? 17.40554  25.81818  12.65104  1.000 42.47695  ? 222 GLU A N     1 
ATOM   1770 C CA    . GLU A 1 228 ? 18.49589  25.65378  13.60560  1.000 43.39263  ? 222 GLU A CA    1 
ATOM   1771 C C     . GLU A 1 228 ? 18.36561  26.62791  14.76764  1.000 45.02013  ? 222 GLU A C     1 
ATOM   1772 O O     . GLU A 1 228 ? 18.76041  26.30621  15.89421  1.000 46.20656  ? 222 GLU A O     1 
ATOM   1773 C CB    . GLU A 1 228 ? 19.84414  25.83038  12.90507  1.000 48.50885  ? 222 GLU A CB    1 
ATOM   1774 C CG    . GLU A 1 228 ? 20.14427  24.77229  11.84874  1.000 51.41084  ? 222 GLU A CG    1 
ATOM   1775 C CD    . GLU A 1 228 ? 20.58911  23.44067  12.43558  1.000 59.73066  ? 222 GLU A CD    1 
ATOM   1776 O OE1   . GLU A 1 228 ? 20.43364  23.22970  13.65684  1.000 66.15194  ? 222 GLU A OE1   1 
ATOM   1777 O OE2   . GLU A 1 228 ? 21.09723  22.59785  11.66782  1.000 57.51741  ? 222 GLU A OE2   1 
ATOM   1778 N N     . THR A 1 229 ? 17.81135  27.81729  14.51808  1.000 42.23866  ? 223 THR A N     1 
ATOM   1779 C CA    . THR A 1 229 ? 17.54308  28.74663  15.60951  1.000 46.32040  ? 223 THR A CA    1 
ATOM   1780 C C     . THR A 1 229 ? 16.38268  28.27135  16.47377  1.000 45.84778  ? 223 THR A C     1 
ATOM   1781 O O     . THR A 1 229 ? 16.36564  28.53332  17.68114  1.000 48.22438  ? 223 THR A O     1 
ATOM   1782 C CB    . THR A 1 229 ? 17.25537  30.14435  15.06091  1.000 51.66034  ? 223 THR A CB    1 
ATOM   1783 O OG1   . THR A 1 229 ? 17.74723  30.24431  13.71872  1.000 50.87344  ? 223 THR A OG1   1 
ATOM   1784 C CG2   . THR A 1 229 ? 17.92966  31.20231  15.92335  1.000 50.61731  ? 223 THR A CG2   1 
ATOM   1785 N N     . ASP A 1 230 ? 15.40593  27.58050  15.87879  1.000 43.55309  ? 224 ASP A N     1 
ATOM   1786 C CA    . ASP A 1 230 ? 14.32898  26.99532  16.67158  1.000 43.70889  ? 224 ASP A CA    1 
ATOM   1787 C C     . ASP A 1 230 ? 14.85906  25.90604  17.59481  1.000 40.35599  ? 224 ASP A C     1 
ATOM   1788 O O     . ASP A 1 230 ? 14.42551  25.79080  18.74714  1.000 44.27306  ? 224 ASP A O     1 
ATOM   1789 C CB    . ASP A 1 230 ? 13.24325  26.42488  15.75634  1.000 41.32523  ? 224 ASP A CB    1 
ATOM   1790 C CG    . ASP A 1 230 ? 12.48936  27.49836  14.99513  1.000 49.94541  ? 224 ASP A CG    1 
ATOM   1791 O OD1   . ASP A 1 230 ? 12.31626  28.60929  15.53726  1.000 54.08203  ? 224 ASP A OD1   1 
ATOM   1792 O OD2   . ASP A 1 230 ? 12.06459  27.22687  13.85195  1.000 44.86246  ? 224 ASP A OD2   1 
ATOM   1793 N N     . VAL A 1 231 ? 15.80462  25.10417  17.10690  1.000 37.55145  ? 225 VAL A N     1 
ATOM   1794 C CA    . VAL A 1 231 ? 16.27888  23.94519  17.85855  1.000 39.43785  ? 225 VAL A CA    1 
ATOM   1795 C C     . VAL A 1 231 ? 17.28270  24.36275  18.92500  1.000 45.40948  ? 225 VAL A C     1 
ATOM   1796 O O     . VAL A 1 231 ? 17.10470  24.07262  20.11417  1.000 42.58155  ? 225 VAL A O     1 
ATOM   1797 C CB    . VAL A 1 231 ? 16.88147  22.90006  16.90303  1.000 37.88708  ? 225 VAL A CB    1 
ATOM   1798 C CG1   . VAL A 1 231 ? 17.60321  21.81536  17.68878  1.000 34.29282  ? 225 VAL A CG1   1 
ATOM   1799 C CG2   . VAL A 1 231 ? 15.79802  22.30493  16.02003  1.000 34.26090  ? 225 VAL A CG2   1 
ATOM   1800 N N     . ALA A 1 232 ? 18.35776  25.04094  18.50957  1.000 47.34525  ? 226 ALA A N     1 
ATOM   1801 C CA    . ALA A 1 232 ? 19.39555  25.44563  19.45286  1.000 53.29474  ? 226 ALA A CA    1 
ATOM   1802 C C     . ALA A 1 232 ? 18.82542  26.28055  20.58948  1.000 45.43560  ? 226 ALA A C     1 
ATOM   1803 O O     . ALA A 1 232 ? 19.32785  26.22374  21.71807  1.000 52.43756  ? 226 ALA A O     1 
ATOM   1804 C CB    . ALA A 1 232 ? 20.49416  26.22151  18.72652  1.000 52.48026  ? 226 ALA A CB    1 
ATOM   1805 N N     . LYS A 1 233 ? 17.77029  27.04763  20.32092  1.000 44.63954  ? 227 LYS A N     1 
ATOM   1806 C CA    . LYS A 1 233 ? 17.15259  27.81608  21.39092  1.000 47.12071  ? 227 LYS A CA    1 
ATOM   1807 C C     . LYS A 1 233 ? 16.36358  26.92796  22.35331  1.000 49.64753  ? 227 LYS A C     1 
ATOM   1808 O O     . LYS A 1 233 ? 16.26366  27.25363  23.54159  1.000 46.98724  ? 227 LYS A O     1 
ATOM   1809 C CB    . LYS A 1 233 ? 16.26373  28.91277  20.80299  1.000 49.84764  ? 227 LYS A CB    1 
ATOM   1810 C CG    . LYS A 1 233 ? 14.82831  28.49009  20.71244  1.000 54.20985  ? 227 LYS A CG    1 
ATOM   1811 C CD    . LYS A 1 233 ? 14.08091  29.01616  21.90761  1.000 55.96728  ? 227 LYS A CD    1 
ATOM   1812 C CE    . LYS A 1 233 ? 12.68760  28.45558  21.98800  1.000 59.99212  ? 227 LYS A CE    1 
ATOM   1813 N NZ    . LYS A 1 233 ? 12.01472  29.01085  23.19064  1.000 68.07439  ? 227 LYS A NZ    1 
ATOM   1814 N N     . ILE A 1 234 ? 15.76365  25.83456  21.86645  1.000 46.34120  ? 228 ILE A N     1 
ATOM   1815 C CA    . ILE A 1 234 ? 15.08125  24.90723  22.76845  1.000 36.79955  ? 228 ILE A CA    1 
ATOM   1816 C C     . ILE A 1 234 ? 16.08976  24.25535  23.70192  1.000 34.96975  ? 228 ILE A C     1 
ATOM   1817 O O     . ILE A 1 234 ? 15.86771  24.15390  24.91500  1.000 34.84071  ? 228 ILE A O     1 
ATOM   1818 C CB    . ILE A 1 234 ? 14.28816  23.85081  21.97185  1.000 33.16105  ? 228 ILE A CB    1 
ATOM   1819 C CG1   . ILE A 1 234 ? 12.95427  24.42049  21.48519  1.000 35.59108  ? 228 ILE A CG1   1 
ATOM   1820 C CG2   . ILE A 1 234 ? 14.04675  22.60215  22.81333  1.000 35.77080  ? 228 ILE A CG2   1 
ATOM   1821 C CD1   . ILE A 1 234 ? 12.31059  23.60032  20.38885  1.000 35.09661  ? 228 ILE A CD1   1 
ATOM   1822 N N     . LYS A 1 235 ? 17.22170  23.81524  23.14971  1.000 34.01034  ? 229 LYS A N     1 
ATOM   1823 C CA    . LYS A 1 235 ? 18.24459  23.16055  23.95559  1.000 37.06079  ? 229 LYS A CA    1 
ATOM   1824 C C     . LYS A 1 235 ? 18.89415  24.12903  24.93657  1.000 39.22048  ? 229 LYS A C     1 
ATOM   1825 O O     . LYS A 1 235 ? 19.39755  23.70353  25.98251  1.000 37.00148  ? 229 LYS A O     1 
ATOM   1826 C CB    . LYS A 1 235 ? 19.29192  22.53104  23.03801  1.000 33.91342  ? 229 LYS A CB    1 
ATOM   1827 C CG    . LYS A 1 235 ? 18.68527  21.61625  21.98261  1.000 38.77545  ? 229 LYS A CG    1 
ATOM   1828 C CD    . LYS A 1 235 ? 19.74398  20.88196  21.17891  1.000 36.19170  ? 229 LYS A CD    1 
ATOM   1829 C CE    . LYS A 1 235 ? 19.11943  19.75997  20.36292  1.000 33.35144  ? 229 LYS A CE    1 
ATOM   1830 N NZ    . LYS A 1 235 ? 20.06339  19.18799  19.36383  1.000 30.41256  ? 229 LYS A NZ    1 
ATOM   1831 N N     . GLU A 1 236 ? 18.88865  25.42824  24.62455  1.000 36.52743  ? 230 GLU A N     1 
ATOM   1832 C CA    . GLU A 1 236 ? 19.42305  26.42024  25.55087  1.000 41.88146  ? 230 GLU A CA    1 
ATOM   1833 C C     . GLU A 1 236 ? 18.53739  26.60441  26.77585  1.000 40.95964  ? 230 GLU A C     1 
ATOM   1834 O O     . GLU A 1 236 ? 19.02656  27.05337  27.81799  1.000 45.58580  ? 230 GLU A O     1 
ATOM   1835 C CB    . GLU A 1 236 ? 19.60282  27.76612  24.84494  1.000 42.05829  ? 230 GLU A CB    1 
ATOM   1836 C CG    . GLU A 1 236 ? 20.84595  27.86632  23.97531  1.000 46.46540  ? 230 GLU A CG    1 
ATOM   1837 C CD    . GLU A 1 236 ? 20.87055  29.13515  23.14290  1.000 57.82208  ? 230 GLU A CD    1 
ATOM   1838 O OE1   . GLU A 1 236 ? 20.26397  30.14070  23.56967  1.000 54.41529  ? 230 GLU A OE1   1 
ATOM   1839 O OE2   . GLU A 1 236 ? 21.49253  29.12671  22.05998  1.000 60.38457  ? 230 GLU A OE2   1 
ATOM   1840 N N     . ASN A 1 237 ? 17.25073  26.27252  26.67435  1.000 35.52816  ? 231 ASN A N     1 
ATOM   1841 C CA    . ASN A 1 237 ? 16.29566  26.45261  27.76089  1.000 33.66474  ? 231 ASN A CA    1 
ATOM   1842 C C     . ASN A 1 237 ? 15.63138  25.13111  28.13882  1.000 34.48695  ? 231 ASN A C     1 
ATOM   1843 O O     . ASN A 1 237 ? 14.51677  25.11382  28.66413  1.000 35.83162  ? 231 ASN A O     1 
ATOM   1844 C CB    . ASN A 1 237 ? 15.24722  27.49837  27.37882  1.000 30.37350  ? 231 ASN A CB    1 
ATOM   1845 C CG    . ASN A 1 237 ? 14.47767  28.02427  28.57555  1.000 40.76142  ? 231 ASN A CG    1 
ATOM   1846 O OD1   . ASN A 1 237 ? 15.06414  28.40684  29.58800  1.000 45.21391  ? 231 ASN A OD1   1 
ATOM   1847 N ND2   . ASN A 1 237 ? 13.15521  28.04379  28.46411  1.000 40.03625  ? 231 ASN A ND2   1 
ATOM   1848 N N     . TYR A 1 238 ? 16.31573  24.01239  27.88417  1.000 35.10548  ? 232 TYR A N     1 
ATOM   1849 C CA    . TYR A 1 238 ? 15.71228  22.70417  28.12075  1.000 35.36519  ? 232 TYR A CA    1 
ATOM   1850 C C     . TYR A 1 238 ? 15.43456  22.46358  29.59861  1.000 37.29257  ? 232 TYR A C     1 
ATOM   1851 O O     . TYR A 1 238 ? 14.49000  21.74265  29.94082  1.000 38.05770  ? 232 TYR A O     1 
ATOM   1852 C CB    . TYR A 1 238 ? 16.61453  21.60088  27.56722  1.000 37.53410  ? 232 TYR A CB    1 
ATOM   1853 C CG    . TYR A 1 238 ? 15.94189  20.71684  26.54033  1.000 36.06094  ? 232 TYR A CG    1 
ATOM   1854 C CD1   . TYR A 1 238 ? 14.59378  20.39908  26.64481  1.000 33.08546  ? 232 TYR A CD1   1 
ATOM   1855 C CD2   . TYR A 1 238 ? 16.65578  20.19876  25.46802  1.000 32.35372  ? 232 TYR A CD2   1 
ATOM   1856 C CE1   . TYR A 1 238 ? 13.97550  19.59095  25.70875  1.000 38.91130  ? 232 TYR A CE1   1 
ATOM   1857 C CE2   . TYR A 1 238 ? 16.04659  19.39018  24.52684  1.000 34.92933  ? 232 TYR A CE2   1 
ATOM   1858 C CZ    . TYR A 1 238 ? 14.70721  19.08945  24.65253  1.000 37.85206  ? 232 TYR A CZ    1 
ATOM   1859 O OH    . TYR A 1 238 ? 14.09864  18.28494  23.71798  1.000 34.34395  ? 232 TYR A OH    1 
ATOM   1860 N N     . ASP A 1 239 ? 16.23774  23.05469  30.48667  1.000 35.97790  ? 233 ASP A N     1 
ATOM   1861 C CA    . ASP A 1 239 ? 16.03555  22.84200  31.91663  1.000 38.20559  ? 233 ASP A CA    1 
ATOM   1862 C C     . ASP A 1 239 ? 14.71265  23.43660  32.38502  1.000 32.84867  ? 233 ASP A C     1 
ATOM   1863 O O     . ASP A 1 239 ? 13.96892  22.79416  33.13566  1.000 35.30286  ? 233 ASP A O     1 
ATOM   1864 C CB    . ASP A 1 239 ? 17.20448  23.43248  32.70563  1.000 42.07807  ? 233 ASP A CB    1 
ATOM   1865 C CG    . ASP A 1 239 ? 18.43248  22.54221  32.67985  1.000 48.72382  ? 233 ASP A CG    1 
ATOM   1866 O OD1   . ASP A 1 239 ? 18.26858  21.30420  32.68808  1.000 49.54492  ? 233 ASP A OD1   1 
ATOM   1867 O OD2   . ASP A 1 239 ? 19.56041  23.07840  32.65054  1.000 54.83965  ? 233 ASP A OD2   1 
ATOM   1868 N N     . GLN A 1 240 ? 14.39917  24.65996  31.95134  1.000 31.71676  ? 234 GLN A N     1 
ATOM   1869 C CA    . GLN A 1 240 ? 13.12835  25.27040  32.32767  1.000 31.69459  ? 234 GLN A CA    1 
ATOM   1870 C C     . GLN A 1 240 ? 11.95433  24.60190  31.62453  1.000 33.27325  ? 234 GLN A C     1 
ATOM   1871 O O     . GLN A 1 240 ? 10.85563  24.52936  32.18787  1.000 37.95056  ? 234 GLN A O     1 
ATOM   1872 C CB    . GLN A 1 240 ? 13.15045  26.76671  32.01513  1.000 35.26665  ? 234 GLN A CB    1 
ATOM   1873 C CG    . GLN A 1 240 ? 11.89273  27.50851  32.43797  1.000 36.72323  ? 234 GLN A CG    1 
ATOM   1874 C CD    . GLN A 1 240 ? 11.71222  27.53433  33.94227  1.000 37.66157  ? 234 GLN A CD    1 
ATOM   1875 O OE1   . GLN A 1 240 ? 12.63962  27.85777  34.68378  1.000 43.38063  ? 234 GLN A OE1   1 
ATOM   1876 N NE2   . GLN A 1 240 ? 10.51424  27.19127  34.40152  1.000 41.03309  ? 234 GLN A NE2   1 
ATOM   1877 N N     . ILE A 1 241 ? 12.16588  24.11107  30.40102  1.000 32.90983  ? 235 ILE A N     1 
ATOM   1878 C CA    . ILE A 1 241 ? 11.09264  23.45058  29.66305  1.000 34.99900  ? 235 ILE A CA    1 
ATOM   1879 C C     . ILE A 1 241 ? 10.61063  22.21677  30.41430  1.000 34.97007  ? 235 ILE A C     1 
ATOM   1880 O O     . ILE A 1 241 ? 9.40295   21.97178  30.52816  1.000 35.32326  ? 235 ILE A O     1 
ATOM   1881 C CB    . ILE A 1 241 ? 11.56364  23.10167  28.23845  1.000 38.98293  ? 235 ILE A CB    1 
ATOM   1882 C CG1   . ILE A 1 241 ? 11.64406  24.36335  27.37744  1.000 31.65623  ? 235 ILE A CG1   1 
ATOM   1883 C CG2   . ILE A 1 241 ? 10.63421  22.08305  27.59771  1.000 38.78453  ? 235 ILE A CG2   1 
ATOM   1884 C CD1   . ILE A 1 241 ? 12.29822  24.14027  26.03261  1.000 39.12429  ? 235 ILE A CD1   1 
ATOM   1885 N N     . TRP A 1 242 ? 11.54343  21.42748  30.95116  1.000 31.98489  ? 236 TRP A N     1 
ATOM   1886 C CA    . TRP A 1 242 ? 11.15141  20.22595  31.67844  1.000 36.17118  ? 236 TRP A CA    1 
ATOM   1887 C C     . TRP A 1 242 ? 10.58102  20.55737  33.05060  1.000 38.60557  ? 236 TRP A C     1 
ATOM   1888 O O     . TRP A 1 242 ? 9.67846   19.85942  33.52648  1.000 35.83838  ? 236 TRP A O     1 
ATOM   1889 C CB    . TRP A 1 242 ? 12.33998  19.27428  31.79796  1.000 36.51579  ? 236 TRP A CB    1 
ATOM   1890 C CG    . TRP A 1 242 ? 12.60045  18.53597  30.52757  1.000 35.51612  ? 236 TRP A CG    1 
ATOM   1891 C CD1   . TRP A 1 242 ? 13.67478  18.67858  29.69872  1.000 32.92030  ? 236 TRP A CD1   1 
ATOM   1892 C CD2   . TRP A 1 242 ? 11.75499  17.54997  29.92404  1.000 35.75682  ? 236 TRP A CD2   1 
ATOM   1893 N NE1   . TRP A 1 242 ? 13.55470  17.83514  28.62031  1.000 36.96941  ? 236 TRP A NE1   1 
ATOM   1894 C CE2   . TRP A 1 242 ? 12.38428  17.13198  28.73518  1.000 36.18631  ? 236 TRP A CE2   1 
ATOM   1895 C CE3   . TRP A 1 242 ? 10.52962  16.97483  30.27736  1.000 34.67516  ? 236 TRP A CE3   1 
ATOM   1896 C CZ2   . TRP A 1 242 ? 11.83077  16.16490  27.89803  1.000 35.40819  ? 236 TRP A CZ2   1 
ATOM   1897 C CZ3   . TRP A 1 242 ? 9.98091   16.01561  29.44341  1.000 35.19507  ? 236 TRP A CZ3   1 
ATOM   1898 C CH2   . TRP A 1 242 ? 10.63118  15.62097  28.26845  1.000 34.71216  ? 236 TRP A CH2   1 
ATOM   1899 N N     . GLU A 1 243 ? 11.08613  21.61074  33.69922  1.000 39.26394  ? 237 GLU A N     1 
ATOM   1900 C CA    . GLU A 1 243 ? 10.47366  22.06638  34.94263  1.000 37.05177  ? 237 GLU A CA    1 
ATOM   1901 C C     . GLU A 1 243 ? 9.02377   22.47525  34.72265  1.000 36.49476  ? 237 GLU A C     1 
ATOM   1902 O O     . GLU A 1 243 ? 8.18351   22.28933  35.61023  1.000 42.60867  ? 237 GLU A O     1 
ATOM   1903 C CB    . GLU A 1 243 ? 11.27175  23.23126  35.53227  1.000 38.89840  ? 237 GLU A CB    1 
ATOM   1904 C CG    . GLU A 1 243 ? 12.44979  22.81789  36.40761  1.000 49.22979  ? 237 GLU A CG    1 
ATOM   1905 C CD    . GLU A 1 243 ? 12.13313  21.64860  37.32300  1.000 58.89664  ? 237 GLU A CD    1 
ATOM   1906 O OE1   . GLU A 1 243 ? 11.12919  21.71824  38.06255  1.000 60.51959  ? 237 GLU A OE1   1 
ATOM   1907 O OE2   . GLU A 1 243 ? 12.89395  20.65937  37.30805  1.000 59.76429  ? 237 GLU A OE2   1 
ATOM   1908 N N     . ASN A 1 244 ? 8.71237   23.02759  33.54701  1.000 34.76989  ? 238 ASN A N     1 
ATOM   1909 C CA    . ASN A 1 244 ? 7.32605   23.33767  33.21465  1.000 36.68181  ? 238 ASN A CA    1 
ATOM   1910 C C     . ASN A 1 244 ? 6.50391   22.06595  33.04463  1.000 36.86148  ? 238 ASN A C     1 
ATOM   1911 O O     . ASN A 1 244 ? 5.31677   22.03641  33.38998  1.000 36.28560  ? 238 ASN A O     1 
ATOM   1912 C CB    . ASN A 1 244 ? 7.26929   24.18251  31.94200  1.000 36.19074  ? 238 ASN A CB    1 
ATOM   1913 C CG    . ASN A 1 244 ? 7.79567   25.58894  32.14975  1.000 38.47751  ? 238 ASN A CG    1 
ATOM   1914 O OD1   . ASN A 1 244 ? 8.03450   26.01558  33.27942  1.000 40.47437  ? 238 ASN A OD1   1 
ATOM   1915 N ND2   . ASN A 1 244 ? 7.98424   26.31644  31.05492  1.000 37.53693  ? 238 ASN A ND2   1 
ATOM   1916 N N     . VAL A 1 245 ? 7.11841   21.00611  32.51264  1.000 34.59807  ? 239 VAL A N     1 
ATOM   1917 C CA    . VAL A 1 245 ? 6.40233   19.74762  32.31425  1.000 37.66145  ? 239 VAL A CA    1 
ATOM   1918 C C     . VAL A 1 245 ? 6.00789   19.14509  33.65716  1.000 34.90666  ? 239 VAL A C     1 
ATOM   1919 O O     . VAL A 1 245 ? 4.84885   18.77196  33.87537  1.000 40.10089  ? 239 VAL A O     1 
ATOM   1920 C CB    . VAL A 1 245 ? 7.25354   18.76908  31.48439  1.000 34.54998  ? 239 VAL A CB    1 
ATOM   1921 C CG1   . VAL A 1 245 ? 6.70583   17.35443  31.60368  1.000 34.73917  ? 239 VAL A CG1   1 
ATOM   1922 C CG2   . VAL A 1 245 ? 7.29850   19.20767  30.02893  1.000 33.90579  ? 239 VAL A CG2   1 
ATOM   1923 N N     . TRP A 1 246 ? 6.96763   19.04605  34.58083  1.000 37.72974  ? 240 TRP A N     1 
ATOM   1924 C CA    . TRP A 1 246 ? 6.67830   18.48776  35.89692  1.000 38.54346  ? 240 TRP A CA    1 
ATOM   1925 C C     . TRP A 1 246 ? 5.69724   19.34532  36.68520  1.000 37.30481  ? 240 TRP A C     1 
ATOM   1926 O O     . TRP A 1 246 ? 5.04287   18.83600  37.60175  1.000 41.10474  ? 240 TRP A O     1 
ATOM   1927 C CB    . TRP A 1 246 ? 7.97262   18.31514  36.69662  1.000 37.58325  ? 240 TRP A CB    1 
ATOM   1928 C CG    . TRP A 1 246 ? 9.03799   17.52382  35.98786  1.000 36.90488  ? 240 TRP A CG    1 
ATOM   1929 C CD1   . TRP A 1 246 ? 10.31752  17.92224  35.73301  1.000 39.32727  ? 240 TRP A CD1   1 
ATOM   1930 C CD2   . TRP A 1 246 ? 8.91792   16.19790  35.45308  1.000 36.92784  ? 240 TRP A CD2   1 
ATOM   1931 N NE1   . TRP A 1 246 ? 10.99981  16.93197  35.06880  1.000 42.54925  ? 240 TRP A NE1   1 
ATOM   1932 C CE2   . TRP A 1 246 ? 10.16344  15.86262  34.88541  1.000 40.08131  ? 240 TRP A CE2   1 
ATOM   1933 C CE3   . TRP A 1 246 ? 7.87901   15.26328  35.39816  1.000 38.64513  ? 240 TRP A CE3   1 
ATOM   1934 C CZ2   . TRP A 1 246 ? 10.39750  14.63430  34.27056  1.000 41.73126  ? 240 TRP A CZ2   1 
ATOM   1935 C CZ3   . TRP A 1 246 ? 8.11335   14.04481  34.78633  1.000 37.09015  ? 240 TRP A CZ3   1 
ATOM   1936 C CH2   . TRP A 1 246 ? 9.36242   13.74133  34.23145  1.000 38.18550  ? 240 TRP A CH2   1 
ATOM   1937 N N     . ASN A 1 247 ? 5.57792   20.62853  36.35027  1.000 42.16058  ? 241 ASN A N     1 
ATOM   1938 C CA    . ASN A 1 247 ? 4.68333   21.54419  37.04381  1.000 40.40160  ? 241 ASN A CA    1 
ATOM   1939 C C     . ASN A 1 247 ? 3.33093   21.69079  36.35901  1.000 45.02976  ? 241 ASN A C     1 
ATOM   1940 O O     . ASN A 1 247 ? 2.51816   22.51144  36.79606  1.000 44.29486  ? 241 ASN A O     1 
ATOM   1941 C CB    . ASN A 1 247 ? 5.34313   22.92211  37.17353  1.000 43.49238  ? 241 ASN A CB    1 
ATOM   1942 C CG    . ASN A 1 247 ? 5.11383   23.55488  38.53121  1.000 53.47131  ? 241 ASN A CG    1 
ATOM   1943 O OD1   . ASN A 1 247 ? 5.68006   23.12173  39.53459  1.000 55.89807  ? 241 ASN A OD1   1 
ATOM   1944 N ND2   . ASN A 1 247 ? 4.28150   24.58854  38.56901  1.000 56.50225  ? 241 ASN A ND2   1 
ATOM   1945 N N     . SER A 1 248 ? 3.06651   20.91922  35.31000  1.000 38.55479  ? 242 SER A N     1 
ATOM   1946 C CA    . SER A 1 248 ? 1.85266   21.04545  34.51768  1.000 35.95637  ? 242 SER A CA    1 
ATOM   1947 C C     . SER A 1 248 ? 0.96134   19.82210  34.71374  1.000 40.37665  ? 242 SER A C     1 
ATOM   1948 O O     . SER A 1 248 ? 1.32287   18.85226  35.38670  1.000 38.01702  ? 242 SER A O     1 
ATOM   1949 C CB    . SER A 1 248 ? 2.19876   21.23964  33.04007  1.000 37.05230  ? 242 SER A CB    1 
ATOM   1950 O OG    . SER A 1 248 ? 2.86237   20.10098  32.51864  1.000 36.21025  ? 242 SER A OG    1 
ATOM   1951 N N     . ALA A 1 249 ? -0.22296  19.87642  34.10573  1.000 39.48197  ? 243 ALA A N     1 
ATOM   1952 C CA    . ALA A 1 249 ? -1.17079  18.77360  34.18503  1.000 41.66380  ? 243 ALA A CA    1 
ATOM   1953 C C     . ALA A 1 249 ? -1.00747  17.77262  33.05117  1.000 37.53988  ? 243 ALA A C     1 
ATOM   1954 O O     . ALA A 1 249 ? -1.23500  16.57520  33.25674  1.000 42.39810  ? 243 ALA A O     1 
ATOM   1955 C CB    . ALA A 1 249 ? -2.60568  19.30891  34.18880  1.000 43.12018  ? 243 ALA A CB    1 
ATOM   1956 N N     . LEU A 1 250 ? -0.61017  18.22944  31.86157  1.000 35.61714  ? 244 LEU A N     1 
ATOM   1957 C CA    . LEU A 1 250 ? -0.52492  17.36284  30.69519  1.000 38.80278  ? 244 LEU A CA    1 
ATOM   1958 C C     . LEU A 1 250 ? 0.89543   17.08904  30.22566  1.000 37.52521  ? 244 LEU A C     1 
ATOM   1959 O O     . LEU A 1 250 ? 1.10819   16.10603  29.50919  1.000 37.81733  ? 244 LEU A O     1 
ATOM   1960 C CB    . LEU A 1 250 ? -1.31967  17.96557  29.52833  1.000 36.76498  ? 244 LEU A CB    1 
ATOM   1961 C CG    . LEU A 1 250 ? -2.77514  18.31269  29.84117  1.000 36.98051  ? 244 LEU A CG    1 
ATOM   1962 C CD1   . LEU A 1 250 ? -3.33224  19.23927  28.78067  1.000 40.34841  ? 244 LEU A CD1   1 
ATOM   1963 C CD2   . LEU A 1 250 ? -3.61548  17.04843  29.95458  1.000 40.93249  ? 244 LEU A CD2   1 
ATOM   1964 N N     . GLY A 1 251 ? 1.86363   17.92126  30.60241  1.000 35.82856  ? 245 GLY A N     1 
ATOM   1965 C CA    . GLY A 1 251 ? 3.22644   17.71370  30.15559  1.000 32.68018  ? 245 GLY A CA    1 
ATOM   1966 C C     . GLY A 1 251 ? 3.44119   17.89799  28.67199  1.000 35.07284  ? 245 GLY A C     1 
ATOM   1967 O O     . GLY A 1 251 ? 4.38987   17.33628  28.11865  1.000 36.67129  ? 245 GLY A O     1 
ATOM   1968 N N     . TYR A 1 252 ? 2.58345   18.67026  28.00762  1.000 35.27754  ? 246 TYR A N     1 
ATOM   1969 C CA    . TYR A 1 252 ? 2.69401   18.92428  26.57849  1.000 37.67238  ? 246 TYR A CA    1 
ATOM   1970 C C     . TYR A 1 252 ? 3.35938   20.25986  26.26990  1.000 36.78113  ? 246 TYR A C     1 
ATOM   1971 O O     . TYR A 1 252 ? 3.36788   20.68247  25.10945  1.000 36.67063  ? 246 TYR A O     1 
ATOM   1972 C CB    . TYR A 1 252 ? 1.31004   18.86941  25.92707  1.000 36.72066  ? 246 TYR A CB    1 
ATOM   1973 C CG    . TYR A 1 252 ? 0.88418   17.48567  25.48889  1.000 37.93151  ? 246 TYR A CG    1 
ATOM   1974 C CD1   . TYR A 1 252 ? 0.42171   16.55560  26.41069  1.000 40.12121  ? 246 TYR A CD1   1 
ATOM   1975 C CD2   . TYR A 1 252 ? 0.93418   17.11323  24.15147  1.000 45.97459  ? 246 TYR A CD2   1 
ATOM   1976 C CE1   . TYR A 1 252 ? 0.02828   15.29041  26.01433  1.000 38.77911  ? 246 TYR A CE1   1 
ATOM   1977 C CE2   . TYR A 1 252 ? 0.54107   15.85129  23.74560  1.000 47.62294  ? 246 TYR A CE2   1 
ATOM   1978 C CZ    . TYR A 1 252 ? 0.09090   14.94380  24.68068  1.000 43.84531  ? 246 TYR A CZ    1 
ATOM   1979 O OH    . TYR A 1 252 ? -0.29994  13.68627  24.27949  1.000 41.95202  ? 246 TYR A OH    1 
ATOM   1980 N N     . GLY A 1 253 ? 3.92099   20.92806  27.27543  1.000 36.98406  ? 247 GLY A N     1 
ATOM   1981 C CA    . GLY A 1 253 ? 4.52297   22.22804  27.05812  1.000 39.10751  ? 247 GLY A CA    1 
ATOM   1982 C C     . GLY A 1 253 ? 3.53475   23.33617  26.78873  1.000 40.61495  ? 247 GLY A C     1 
ATOM   1983 O O     . GLY A 1 253 ? 3.89334   24.33444  26.15845  1.000 38.67476  ? 247 GLY A O     1 
ATOM   1984 N N     . LEU A 1 254 ? 2.29808   23.19196  27.25378  1.000 37.22903  ? 248 LEU A N     1 
ATOM   1985 C CA    . LEU A 1 254 ? 1.24670   24.15608  26.97598  1.000 38.22329  ? 248 LEU A CA    1 
ATOM   1986 C C     . LEU A 1 254 ? 1.13021   25.17638  28.09949  1.000 42.09192  ? 248 LEU A C     1 
ATOM   1987 O O     . LEU A 1 254 ? 1.50490   24.91724  29.24664  1.000 36.08392  ? 248 LEU A O     1 
ATOM   1988 C CB    . LEU A 1 254 ? -0.09729  23.44951  26.79147  1.000 37.38882  ? 248 LEU A CB    1 
ATOM   1989 C CG    . LEU A 1 254 ? -0.16170  22.31546  25.76584  1.000 36.74650  ? 248 LEU A CG    1 
ATOM   1990 C CD1   . LEU A 1 254 ? -1.49769  21.59496  25.85796  1.000 40.28316  ? 248 LEU A CD1   1 
ATOM   1991 C CD2   . LEU A 1 254 ? 0.06371   22.85269  24.36296  1.000 38.17755  ? 248 LEU A CD2   1 
ATOM   1992 N N     . ASN A 1 255 ? 0.60705   26.35223  27.75023  1.000 41.18540  ? 249 ASN A N     1 
ATOM   1993 C CA    . ASN A 1 255 ? 0.19866   27.34514  28.74112  1.000 43.81231  ? 249 ASN A CA    1 
ATOM   1994 C C     . ASN A 1 255 ? -1.23017  27.00535  29.15256  1.000 43.78949  ? 249 ASN A C     1 
ATOM   1995 O O     . ASN A 1 255 ? -2.20920  27.58354  28.67442  1.000 36.85411  ? 249 ASN A O     1 
ATOM   1996 C CB    . ASN A 1 255 ? 0.32037   28.75449  28.17659  1.000 41.89358  ? 249 ASN A CB    1 
ATOM   1997 C CG    . ASN A 1 255 ? 1.63716   28.98144  27.45925  1.000 45.43200  ? 249 ASN A CG    1 
ATOM   1998 O OD1   . ASN A 1 255 ? 2.70211   28.63723  27.97036  1.000 51.05989  ? 249 ASN A OD1   1 
ATOM   1999 N ND2   . ASN A 1 255 ? 1.57030   29.56346  26.26761  1.000 48.38484  ? 249 ASN A ND2   1 
ATOM   2000 N N     . GLU A 1 256 ? -1.33771  26.02328  30.04704  1.000 37.60754  ? 250 GLU A N     1 
ATOM   2001 C CA    . GLU A 1 256 ? -2.63369  25.48107  30.43291  1.000 38.15976  ? 250 GLU A CA    1 
ATOM   2002 C C     . GLU A 1 256 ? -3.50463  26.56468  31.05117  1.000 46.05134  ? 250 GLU A C     1 
ATOM   2003 O O     . GLU A 1 256 ? -3.17634  27.11652  32.10614  1.000 44.89883  ? 250 GLU A O     1 
ATOM   2004 C CB    . GLU A 1 256 ? -2.43624  24.31510  31.39836  1.000 38.69503  ? 250 GLU A CB    1 
ATOM   2005 C CG    . GLU A 1 256 ? -1.77000  23.11166  30.74280  1.000 38.94203  ? 250 GLU A CG    1 
ATOM   2006 C CD    . GLU A 1 256 ? -1.18133  22.13869  31.74134  1.000 42.09688  ? 250 GLU A CD    1 
ATOM   2007 O OE1   . GLU A 1 256 ? -1.22357  22.42896  32.95436  1.000 43.35011  ? 250 GLU A OE1   1 
ATOM   2008 O OE2   . GLU A 1 256 ? -0.67202  21.08283  31.30825  1.000 36.81196  ? 250 GLU A OE2   1 
ATOM   2009 N N     . SER A 1 257 ? -4.61853  26.85881  30.38765  1.000 43.68611  ? 251 SER A N     1 
ATOM   2010 C CA    . SER A 1 257 ? -5.42814  28.01999  30.71619  1.000 45.50374  ? 251 SER A CA    1 
ATOM   2011 C C     . SER A 1 257 ? -6.33091  27.75745  31.91468  1.000 44.50792  ? 251 SER A C     1 
ATOM   2012 O O     . SER A 1 257 ? -6.73834  26.62398  32.18390  1.000 42.89510  ? 251 SER A O     1 
ATOM   2013 C CB    . SER A 1 257 ? -6.27879  28.42919  29.51315  1.000 40.20412  ? 251 SER A CB    1 
ATOM   2014 O OG    . SER A 1 257 ? -7.07018  29.56648  29.80741  1.000 41.49027  ? 251 SER A OG    1 
ATOM   2015 N N     . THR A 1 258 ? -6.63245  28.83368  32.64123  1.000 44.41882  ? 252 THR A N     1 
ATOM   2016 C CA    . THR A 1 258 ? -7.65458  28.83577  33.67949  1.000 46.76560  ? 252 THR A CA    1 
ATOM   2017 C C     . THR A 1 258 ? -8.80288  29.77247  33.32829  1.000 44.77646  ? 252 THR A C     1 
ATOM   2018 O O     . THR A 1 258 ? -9.68446  30.00405  34.16448  1.000 52.32932  ? 252 THR A O     1 
ATOM   2019 C CB    . THR A 1 258 ? -7.05068  29.23353  35.03003  1.000 45.18029  ? 252 THR A CB    1 
ATOM   2020 O OG1   . THR A 1 258 ? -6.66291  30.61268  34.99345  1.000 43.96724  ? 252 THR A OG1   1 
ATOM   2021 C CG2   . THR A 1 258 ? -5.83032  28.37999  35.34212  1.000 48.66726  ? 252 THR A CG2   1 
ATOM   2022 N N     . LEU A 1 259 ? -8.81121  30.31140  32.11560  1.000 43.48652  ? 253 LEU A N     1 
ATOM   2023 C CA    . LEU A 1 259 ? -9.80383  31.29459  31.70155  1.000 44.08102  ? 253 LEU A CA    1 
ATOM   2024 C C     . LEU A 1 259 ? -11.09887 30.59622  31.30225  1.000 49.35118  ? 253 LEU A C     1 
ATOM   2025 O O     . LEU A 1 259 ? -11.07275 29.68872  30.46507  1.000 45.91871  ? 253 LEU A O     1 
ATOM   2026 C CB    . LEU A 1 259 ? -9.26894  32.11827  30.53257  1.000 41.39601  ? 253 LEU A CB    1 
ATOM   2027 C CG    . LEU A 1 259 ? -10.16402 33.19864  29.92413  1.000 49.47835  ? 253 LEU A CG    1 
ATOM   2028 C CD1   . LEU A 1 259 ? -10.21472 34.42587  30.82009  1.000 45.95020  ? 253 LEU A CD1   1 
ATOM   2029 C CD2   . LEU A 1 259 ? -9.67143  33.56531  28.53237  1.000 42.93931  ? 253 LEU A CD2   1 
ATOM   2030 N N     . PRO A 1 260 ? -12.23837 30.98193  31.87398  1.000 50.52043  ? 254 PRO A N     1 
ATOM   2031 C CA    . PRO A 1 260 ? -13.50799 30.37515  31.45727  1.000 49.63141  ? 254 PRO A CA    1 
ATOM   2032 C C     . PRO A 1 260 ? -13.87307 30.79361  30.04162  1.000 46.77056  ? 254 PRO A C     1 
ATOM   2033 O O     . PRO A 1 260 ? -13.62350 31.92731  29.62528  1.000 49.21608  ? 254 PRO A O     1 
ATOM   2034 C CB    . PRO A 1 260 ? -14.52002 30.90796  32.48171  1.000 50.80775  ? 254 PRO A CB    1 
ATOM   2035 C CG    . PRO A 1 260 ? -13.70828 31.56713  33.56252  1.000 52.83073  ? 254 PRO A CG    1 
ATOM   2036 C CD    . PRO A 1 260 ? -12.41894 31.98003  32.93885  1.000 50.62273  ? 254 PRO A CD    1 
ATOM   2037 N N     . THR A 1 261 ? -14.47352 29.85831  29.30100  1.000 45.36311  ? 255 THR A N     1 
ATOM   2038 C CA    . THR A 1 261 ? -14.77494 30.10747  27.89408  1.000 44.89763  ? 255 THR A CA    1 
ATOM   2039 C C     . THR A 1 261 ? -15.79689 31.22609  27.72970  1.000 44.45659  ? 255 THR A C     1 
ATOM   2040 O O     . THR A 1 261 ? -15.62781 32.11108  26.88266  1.000 49.52877  ? 255 THR A O     1 
ATOM   2041 C CB    . THR A 1 261 ? -15.27871 28.82659  27.22785  1.000 45.36367  ? 255 THR A CB    1 
ATOM   2042 O OG1   . THR A 1 261 ? -14.33943 27.76639  27.44655  1.000 42.52844  ? 255 THR A OG1   1 
ATOM   2043 C CG2   . THR A 1 261 ? -15.45581 29.03599  25.73159  1.000 40.61997  ? 255 THR A CG2   1 
ATOM   2044 N N     . MET A 1 262 ? -16.86008 31.20907  28.52945  1.000 50.02177  ? 256 MET A N     1 
ATOM   2045 C CA    . MET A 1 262 ? -17.94287 32.17318  28.39319  1.000 52.09744  ? 256 MET A CA    1 
ATOM   2046 C C     . MET A 1 262 ? -17.68911 33.46857  29.15454  1.000 54.51653  ? 256 MET A C     1 
ATOM   2047 O O     . MET A 1 262 ? -18.62648 34.24822  29.35278  1.000 56.71813  ? 256 MET A O     1 
ATOM   2048 C CB    . MET A 1 262 ? -19.26383 31.55012  28.85378  1.000 53.35487  ? 256 MET A CB    1 
ATOM   2049 C CG    . MET A 1 262 ? -19.53892 30.16869  28.27222  1.000 49.83909  ? 256 MET A CG    1 
ATOM   2050 S SD    . MET A 1 262 ? -19.40101 30.04916  26.47459  1.000 56.17951  ? 256 MET A SD    1 
ATOM   2051 C CE    . MET A 1 262 ? -20.34253 31.47414  25.93092  1.000 53.33150  ? 256 MET A CE    1 
ATOM   2052 N N     . SER A 1 263 ? -16.45346 33.71834  29.58004  1.000 54.29282  ? 257 SER A N     1 
ATOM   2053 C CA    . SER A 1 263 ? -16.10828 34.95267  30.27135  1.000 53.87989  ? 257 SER A CA    1 
ATOM   2054 C C     . SER A 1 263 ? -15.60328 36.03736  29.32913  1.000 56.17144  ? 257 SER A C     1 
ATOM   2055 O O     . SER A 1 263 ? -15.31654 37.14898  29.78520  1.000 59.94810  ? 257 SER A O     1 
ATOM   2056 C CB    . SER A 1 263 ? -15.05665 34.67729  31.35099  1.000 53.51984  ? 257 SER A CB    1 
ATOM   2057 O OG    . SER A 1 263 ? -13.79403 34.39506  30.77368  1.000 53.79947  ? 257 SER A OG    1 
ATOM   2058 N N     . VAL A 1 264 ? -15.48528 35.74481  28.03535  1.000 51.75532  ? 258 VAL A N     1 
ATOM   2059 C CA    . VAL A 1 264 ? -15.04611 36.71461  27.04338  1.000 48.28872  ? 258 VAL A CA    1 
ATOM   2060 C C     . VAL A 1 264 ? -16.12749 36.84233  25.97473  1.000 48.58990  ? 258 VAL A C     1 
ATOM   2061 O O     . VAL A 1 264 ? -17.05970 36.04167  25.89934  1.000 53.35743  ? 258 VAL A O     1 
ATOM   2062 C CB    . VAL A 1 264 ? -13.69170 36.33770  26.41011  1.000 48.01126  ? 258 VAL A CB    1 
ATOM   2063 C CG1   . VAL A 1 264 ? -12.67888 35.97684  27.48721  1.000 51.70168  ? 258 VAL A CG1   1 
ATOM   2064 C CG2   . VAL A 1 264 ? -13.86450 35.18948  25.42658  1.000 41.69319  ? 258 VAL A CG2   1 
ATOM   2065 N N     . SER A 1 265 ? -15.98719 37.87066  25.14249  1.000 50.23924  ? 259 SER A N     1 
ATOM   2066 C CA    . SER A 1 265 ? -16.94831 38.11388  24.07998  1.000 50.31066  ? 259 SER A CA    1 
ATOM   2067 C C     . SER A 1 265 ? -16.79850 37.07102  22.97298  1.000 51.91336  ? 259 SER A C     1 
ATOM   2068 O O     . SER A 1 265 ? -15.82605 36.31273  22.91618  1.000 48.74601  ? 259 SER A O     1 
ATOM   2069 C CB    . SER A 1 265 ? -16.77013 39.51946  23.50788  1.000 45.62493  ? 259 SER A CB    1 
ATOM   2070 O OG    . SER A 1 265 ? -15.47819 39.68043  22.94907  1.000 52.16845  ? 259 SER A OG    1 
ATOM   2071 N N     . ALA A 1 266 ? -17.78991 37.04143  22.07855  1.000 49.51501  ? 260 ALA A N     1 
ATOM   2072 C CA    . ALA A 1 266 ? -17.73364 36.12292  20.94663  1.000 52.12263  ? 260 ALA A CA    1 
ATOM   2073 C C     . ALA A 1 266 ? -16.57982 36.45872  20.01209  1.000 49.88755  ? 260 ALA A C     1 
ATOM   2074 O O     . ALA A 1 266 ? -15.98431 35.55686  19.41160  1.000 46.53375  ? 260 ALA A O     1 
ATOM   2075 C CB    . ALA A 1 266 ? -19.05915 36.14313  20.18508  1.000 43.76553  ? 260 ALA A CB    1 
ATOM   2076 N N     . GLU A 1 267 ? -16.24865 37.74470  19.87767  1.000 50.50259  ? 261 GLU A N     1 
ATOM   2077 C CA    . GLU A 1 267 ? -15.12123 38.13311  19.03726  1.000 51.95169  ? 261 GLU A CA    1 
ATOM   2078 C C     . GLU A 1 267 ? -13.79701 37.70613  19.65864  1.000 51.69164  ? 261 GLU A C     1 
ATOM   2079 O O     . GLU A 1 267 ? -12.90507 37.21529  18.95653  1.000 49.77191  ? 261 GLU A O     1 
ATOM   2080 C CB    . GLU A 1 267 ? -15.14294 39.64228  18.79813  1.000 56.27697  ? 261 GLU A CB    1 
ATOM   2081 C CG    . GLU A 1 267 ? -14.49144 40.07387  17.49616  1.000 60.11281  ? 261 GLU A CG    1 
ATOM   2082 C CD    . GLU A 1 267 ? -13.73873 41.38221  17.62984  1.000 68.85904  ? 261 GLU A CD    1 
ATOM   2083 O OE1   . GLU A 1 267 ? -13.90081 42.05924  18.66674  1.000 69.93258  ? 261 GLU A OE1   1 
ATOM   2084 O OE2   . GLU A 1 267 ? -12.98582 41.73452  16.69780  1.000 70.25343  ? 261 GLU A OE2   1 
ATOM   2085 N N     . GLU A 1 268 ? -13.64995 37.88451  20.97373  1.000 47.43839  ? 262 GLU A N     1 
ATOM   2086 C CA    . GLU A 1 268 ? -12.42486 37.45935  21.64330  1.000 49.66777  ? 262 GLU A CA    1 
ATOM   2087 C C     . GLU A 1 268 ? -12.33008 35.93983  21.70333  1.000 44.92386  ? 262 GLU A C     1 
ATOM   2088 O O     . GLU A 1 268 ? -11.24110 35.37322  21.55171  1.000 41.63454  ? 262 GLU A O     1 
ATOM   2089 C CB    . GLU A 1 268 ? -12.35894 38.06072  23.04762  1.000 48.78819  ? 262 GLU A CB    1 
ATOM   2090 C CG    . GLU A 1 268 ? -11.22611 37.52203  23.90807  1.000 50.76847  ? 262 GLU A CG    1 
ATOM   2091 C CD    . GLU A 1 268 ? -9.95952  38.34675  23.79253  1.000 59.99041  ? 262 GLU A CD    1 
ATOM   2092 O OE1   . GLU A 1 268 ? -9.52967  38.62580  22.65380  1.000 62.53962  ? 262 GLU A OE1   1 
ATOM   2093 O OE2   . GLU A 1 268 ? -9.39230  38.71533  24.84230  1.000 69.52636  ? 262 GLU A OE2   1 
ATOM   2094 N N     . ARG A 1 269 ? -13.46173 35.26486  21.92241  1.000 43.70575  ? 263 ARG A N     1 
ATOM   2095 C CA    . ARG A 1 269 ? -13.46968 33.80537  21.93113  1.000 45.16097  ? 263 ARG A CA    1 
ATOM   2096 C C     . ARG A 1 269 ? -13.03357 33.24440  20.58392  1.000 45.85751  ? 263 ARG A C     1 
ATOM   2097 O O     . ARG A 1 269 ? -12.35848 32.20986  20.52157  1.000 47.49639  ? 263 ARG A O     1 
ATOM   2098 C CB    . ARG A 1 269 ? -14.86280 33.29589  22.29875  1.000 47.87317  ? 263 ARG A CB    1 
ATOM   2099 C CG    . ARG A 1 269 ? -14.91944 31.82910  22.68544  1.000 48.27631  ? 263 ARG A CG    1 
ATOM   2100 C CD    . ARG A 1 269 ? -16.33662 31.42563  23.06284  1.000 47.82194  ? 263 ARG A CD    1 
ATOM   2101 N NE    . ARG A 1 269 ? -16.96350 32.40926  23.93802  1.000 54.58697  ? 263 ARG A NE    1 
ATOM   2102 C CZ    . ARG A 1 269 ? -18.05867 33.09340  23.63595  1.000 52.17626  ? 263 ARG A CZ    1 
ATOM   2103 N NH1   . ARG A 1 269 ? -18.68670 32.92004  22.48477  1.000 52.87727  ? 263 ARG A NH1   1 
ATOM   2104 N NH2   . ARG A 1 269 ? -18.53459 33.97510  24.51049  1.000 57.54746  ? 263 ARG A NH2   1 
ATOM   2105 N N     . ASP A 1 270 ? -13.41009 33.91539  19.49305  1.000 43.23912  ? 264 ASP A N     1 
ATOM   2106 C CA    . ASP A 1 270 ? -12.99093 33.47006  18.16870  1.000 42.89024  ? 264 ASP A CA    1 
ATOM   2107 C C     . ASP A 1 270 ? -11.49457 33.67131  17.96699  1.000 44.47212  ? 264 ASP A C     1 
ATOM   2108 O O     . ASP A 1 270 ? -10.82659 32.82902  17.35571  1.000 41.37304  ? 264 ASP A O     1 
ATOM   2109 C CB    . ASP A 1 270 ? -13.78160 34.21236  17.09196  1.000 46.14821  ? 264 ASP A CB    1 
ATOM   2110 C CG    . ASP A 1 270 ? -13.95780 33.39259  15.82989  1.000 53.62820  ? 264 ASP A CG    1 
ATOM   2111 O OD1   . ASP A 1 270 ? -14.89152 32.56458  15.78204  1.000 58.84432  ? 264 ASP A OD1   1 
ATOM   2112 O OD2   . ASP A 1 270 ? -13.16098 33.57443  14.88605  1.000 55.43726  ? 264 ASP A OD2   1 
ATOM   2113 N N     . LYS A 1 271 ? -10.95224 34.78260  18.47240  1.000 40.93222  ? 265 LYS A N     1 
ATOM   2114 C CA    . LYS A 1 271 ? -9.52211  35.04081  18.33490  1.000 43.76109  ? 265 LYS A CA    1 
ATOM   2115 C C     . LYS A 1 271 ? -8.69768  33.99086  19.06840  1.000 35.72969  ? 265 LYS A C     1 
ATOM   2116 O O     . LYS A 1 271 ? -7.63177  33.58255  18.59258  1.000 37.65427  ? 265 LYS A O     1 
ATOM   2117 C CB    . LYS A 1 271 ? -9.18776  36.43696  18.86112  1.000 45.44069  ? 265 LYS A CB    1 
ATOM   2118 C CG    . LYS A 1 271 ? -9.51565  37.57234  17.90759  1.000 52.09819  ? 265 LYS A CG    1 
ATOM   2119 C CD    . LYS A 1 271 ? -9.11497  38.91228  18.50562  1.000 61.74768  ? 265 LYS A CD    1 
ATOM   2120 C CE    . LYS A 1 271 ? -9.51367  40.06622  17.60256  1.000 68.39799  ? 265 LYS A CE    1 
ATOM   2121 N NZ    . LYS A 1 271 ? -9.32586  39.73465  16.16476  1.000 72.68714  ? 265 LYS A NZ    1 
ATOM   2122 N N     . ILE A 1 272 ? -9.17520  33.54335  20.23103  1.000 34.32064  ? 266 ILE A N     1 
ATOM   2123 C CA    . ILE A 1 272 ? -8.41528  32.58801  21.03004  1.000 34.65910  ? 266 ILE A CA    1 
ATOM   2124 C C     . ILE A 1 272 ? -8.43195  31.20977  20.37945  1.000 39.16910  ? 266 ILE A C     1 
ATOM   2125 O O     . ILE A 1 272 ? -7.40478  30.52238  20.32459  1.000 38.37772  ? 266 ILE A O     1 
ATOM   2126 C CB    . ILE A 1 272 ? -8.96127  32.55295  22.46913  1.000 36.27983  ? 266 ILE A CB    1 
ATOM   2127 C CG1   . ILE A 1 272 ? -8.67970  33.88325  23.17208  1.000 40.13188  ? 266 ILE A CG1   1 
ATOM   2128 C CG2   . ILE A 1 272 ? -8.34863  31.40530  23.25054  1.000 34.22457  ? 266 ILE A CG2   1 
ATOM   2129 C CD1   . ILE A 1 272 ? -9.32999  34.00830  24.53235  1.000 44.85783  ? 266 ILE A CD1   1 
ATOM   2130 N N     . PHE A 1 273 ? -9.59108  30.78465  19.87122  1.000 39.10943  ? 267 PHE A N     1 
ATOM   2131 C CA    . PHE A 1 273 ? -9.66178  29.50513  19.17265  1.000 37.66466  ? 267 PHE A CA    1 
ATOM   2132 C C     . PHE A 1 273 ? -8.84630  29.53470  17.88575  1.000 37.11570  ? 267 PHE A C     1 
ATOM   2133 O O     . PHE A 1 273 ? -8.17695  28.55214  17.54510  1.000 33.42660  ? 267 PHE A O     1 
ATOM   2134 C CB    . PHE A 1 273 ? -11.11769 29.14788  18.87312  1.000 37.64318  ? 267 PHE A CB    1 
ATOM   2135 C CG    . PHE A 1 273 ? -11.85742 28.56811  20.04562  1.000 36.99888  ? 267 PHE A CG    1 
ATOM   2136 C CD1   . PHE A 1 273 ? -11.26325 27.61546  20.85667  1.000 36.00595  ? 267 PHE A CD1   1 
ATOM   2137 C CD2   . PHE A 1 273 ? -13.15160 28.97174  20.33162  1.000 35.57098  ? 267 PHE A CD2   1 
ATOM   2138 C CE1   . PHE A 1 273 ? -11.94482 27.07948  21.93476  1.000 36.92117  ? 267 PHE A CE1   1 
ATOM   2139 C CE2   . PHE A 1 273 ? -13.83784 28.43990  21.40703  1.000 34.12734  ? 267 PHE A CE2   1 
ATOM   2140 C CZ    . PHE A 1 273 ? -13.23361 27.49345  22.20962  1.000 37.35343  ? 267 PHE A CZ    1 
ATOM   2141 N N     . GLU A 1 274 ? -8.88906  30.65533  17.16025  1.000 35.58902  ? 268 GLU A N     1 
ATOM   2142 C CA    . GLU A 1 274 ? -8.14431  30.76270  15.90943  1.000 35.42324  ? 268 GLU A CA    1 
ATOM   2143 C C     . GLU A 1 274 ? -6.64083  30.72415  16.15442  1.000 35.89013  ? 268 GLU A C     1 
ATOM   2144 O O     . GLU A 1 274 ? -5.88817  30.17531  15.34131  1.000 36.76067  ? 268 GLU A O     1 
ATOM   2145 C CB    . GLU A 1 274 ? -8.53801  32.04610  15.17695  1.000 34.07624  ? 268 GLU A CB    1 
ATOM   2146 C CG    . GLU A 1 274 ? -7.83023  32.25856  13.84819  1.000 35.39389  ? 268 GLU A CG    1 
ATOM   2147 C CD    . GLU A 1 274 ? -8.18513  31.20286  12.82136  1.000 35.82668  ? 268 GLU A CD    1 
ATOM   2148 O OE1   . GLU A 1 274 ? -9.34332  30.73589  12.82053  1.000 41.42375  ? 268 GLU A OE1   1 
ATOM   2149 O OE2   . GLU A 1 274 ? -7.30599  30.84040  12.01294  1.000 44.41919  ? 268 GLU A OE2   1 
ATOM   2150 N N     . LYS A 1 275 ? -6.18621  31.29933  17.26994  1.000 36.18009  ? 269 LYS A N     1 
ATOM   2151 C CA    . LYS A 1 275 ? -4.75997  31.29976  17.57972  1.000 38.18494  ? 269 LYS A CA    1 
ATOM   2152 C C     . LYS A 1 275 ? -4.24734  29.88126  17.80028  1.000 35.22070  ? 269 LYS A C     1 
ATOM   2153 O O     . LYS A 1 275 ? -3.19239  29.50063  17.27943  1.000 32.24492  ? 269 LYS A O     1 
ATOM   2154 C CB    . LYS A 1 275 ? -4.49686  32.17441  18.80597  1.000 39.54597  ? 269 LYS A CB    1 
ATOM   2155 C CG    . LYS A 1 275 ? -3.06200  32.15012  19.30335  1.000 43.89112  ? 269 LYS A CG    1 
ATOM   2156 C CD    . LYS A 1 275 ? -2.90508  33.01299  20.54564  1.000 39.08553  ? 269 LYS A CD    1 
ATOM   2157 C CE    . LYS A 1 275 ? -1.93681  32.39224  21.54029  1.000 49.33465  ? 269 LYS A CE    1 
ATOM   2158 N NZ    . LYS A 1 275 ? -0.52966  32.45371  21.05659  1.000 50.23277  ? 269 LYS A NZ    1 
ATOM   2159 N N     . ALA A 1 276 ? -4.98772  29.07909  18.56884  1.000 31.73205  ? 270 ALA A N     1 
ATOM   2160 C CA    . ALA A 1 276 ? -4.59668  27.68759  18.76569  1.000 35.06290  ? 270 ALA A CA    1 
ATOM   2161 C C     . ALA A 1 276 ? -4.77588  26.87133  17.49369  1.000 35.27270  ? 270 ALA A C     1 
ATOM   2162 O O     . ALA A 1 276 ? -3.99955  25.94299  17.24048  1.000 36.52954  ? 270 ALA A O     1 
ATOM   2163 C CB    . ALA A 1 276 ? -5.39848  27.06876  19.90903  1.000 33.86950  ? 270 ALA A CB    1 
ATOM   2164 N N     . TRP A 1 277 ? -5.79070  27.19808  16.68964  1.000 33.26190  ? 271 TRP A N     1 
ATOM   2165 C CA    . TRP A 1 277 ? -5.98332  26.51517  15.41462  1.000 36.95990  ? 271 TRP A CA    1 
ATOM   2166 C C     . TRP A 1 277 ? -4.79127  26.73205  14.49140  1.000 38.83851  ? 271 TRP A C     1 
ATOM   2167 O O     . TRP A 1 277 ? -4.35533  25.80565  13.79737  1.000 32.97534  ? 271 TRP A O     1 
ATOM   2168 C CB    . TRP A 1 277 ? -7.27380  27.00609  14.75661  1.000 34.93731  ? 271 TRP A CB    1 
ATOM   2169 C CG    . TRP A 1 277 ? -7.62198  26.31731  13.47107  1.000 33.69131  ? 271 TRP A CG    1 
ATOM   2170 C CD1   . TRP A 1 277 ? -7.24058  26.68585  12.21382  1.000 32.89924  ? 271 TRP A CD1   1 
ATOM   2171 C CD2   . TRP A 1 277 ? -8.44040  25.15105  13.31594  1.000 29.54931  ? 271 TRP A CD2   1 
ATOM   2172 N NE1   . TRP A 1 277 ? -7.76298  25.81653  11.28643  1.000 34.22000  ? 271 TRP A NE1   1 
ATOM   2173 C CE2   . TRP A 1 277 ? -8.50501  24.86646  11.93734  1.000 30.96880  ? 271 TRP A CE2   1 
ATOM   2174 C CE3   . TRP A 1 277 ? -9.12107  24.31781  14.20907  1.000 31.69069  ? 271 TRP A CE3   1 
ATOM   2175 C CZ2   . TRP A 1 277 ? -9.22073  23.78236  11.43098  1.000 29.00940  ? 271 TRP A CZ2   1 
ATOM   2176 C CZ3   . TRP A 1 277 ? -9.83314  23.24251  13.70365  1.000 30.48581  ? 271 TRP A CZ3   1 
ATOM   2177 C CH2   . TRP A 1 277 ? -9.87680  22.98527  12.32832  1.000 29.08683  ? 271 TRP A CH2   1 
ATOM   2178 N N     . GLN A 1 278 ? -4.24538  27.95055  14.47697  1.000 35.07060  ? 272 GLN A N     1 
ATOM   2179 C CA    . GLN A 1 278 ? -3.08915  28.23634  13.63394  1.000 36.54319  ? 272 GLN A CA    1 
ATOM   2180 C C     . GLN A 1 278 ? -1.83357  27.55588  14.16495  1.000 36.43081  ? 272 GLN A C     1 
ATOM   2181 O O     . GLN A 1 278 ? -1.03462  27.02175  13.38694  1.000 38.52783  ? 272 GLN A O     1 
ATOM   2182 C CB    . GLN A 1 278 ? -2.87638  29.74664  13.53192  1.000 38.35141  ? 272 GLN A CB    1 
ATOM   2183 C CG    . GLN A 1 278 ? -3.88759  30.46116  12.65059  1.000 40.64124  ? 272 GLN A CG    1 
ATOM   2184 C CD    . GLN A 1 278 ? -4.02943  29.81890  11.28529  1.000 44.92043  ? 272 GLN A CD    1 
ATOM   2185 O OE1   . GLN A 1 278 ? -3.04588  29.63271  10.56912  1.000 45.41073  ? 272 GLN A OE1   1 
ATOM   2186 N NE2   . GLN A 1 278 ? -5.25895  29.47838  10.91605  1.000 42.58481  ? 272 GLN A NE2   1 
ATOM   2187 N N     . GLU A 1 279 ? -1.63879  27.56840  15.48596  1.000 36.22289  ? 273 GLU A N     1 
ATOM   2188 C CA    . GLU A 1 279 ? -0.45131  26.94337  16.05968  1.000 38.40820  ? 273 GLU A CA    1 
ATOM   2189 C C     . GLU A 1 279 ? -0.51449  25.42564  15.94068  1.000 42.55550  ? 273 GLU A C     1 
ATOM   2190 O O     . GLU A 1 279 ? 0.49702   24.77765  15.64625  1.000 40.63587  ? 273 GLU A O     1 
ATOM   2191 C CB    . GLU A 1 279 ? -0.28834  27.36480  17.51994  1.000 37.86050  ? 273 GLU A CB    1 
ATOM   2192 C CG    . GLU A 1 279 ? 0.81626   26.62557  18.25746  1.000 45.80074  ? 273 GLU A CG    1 
ATOM   2193 C CD    . GLU A 1 279 ? 1.57489   27.51710  19.21853  1.000 51.15240  ? 273 GLU A CD    1 
ATOM   2194 O OE1   . GLU A 1 279 ? 0.93689   28.36857  19.87202  1.000 56.70737  ? 273 GLU A OE1   1 
ATOM   2195 O OE2   . GLU A 1 279 ? 2.80937   27.36442  19.32302  1.000 56.69463  ? 273 GLU A OE2   1 
ATOM   2196 N N     . GLY A 1 280 ? -1.68640  24.84411  16.16293  1.000 38.15821  ? 274 GLY A N     1 
ATOM   2197 C CA    . GLY A 1 280 ? -1.87616  23.41968  16.00422  1.000 37.09034  ? 274 GLY A CA    1 
ATOM   2198 C C     . GLY A 1 280 ? -1.78098  22.66888  17.32311  1.000 34.81637  ? 274 GLY A C     1 
ATOM   2199 O O     . GLY A 1 280 ? -1.20609  23.13884  18.30788  1.000 33.99091  ? 274 GLY A O     1 
ATOM   2200 N N     . GLY A 1 281 ? -2.36270  21.47306  17.33369  1.000 35.13310  ? 275 GLY A N     1 
ATOM   2201 C CA    . GLY A 1 281 ? -2.31089  20.61606  18.51856  1.000 30.35783  ? 275 GLY A CA    1 
ATOM   2202 C C     . GLY A 1 281 ? -3.69601  20.37747  19.08814  1.000 35.30913  ? 275 GLY A C     1 
ATOM   2203 O O     . GLY A 1 281 ? -4.47903  21.30116  19.30825  1.000 30.26009  ? 275 GLY A O     1 
ATOM   2204 N N     . GLY A 1 282 ? -3.99868  19.10179  19.33466  1.000 33.14968  ? 276 GLY A N     1 
ATOM   2205 C CA    . GLY A 1 282 ? -5.29534  18.75753  19.89689  1.000 34.30213  ? 276 GLY A CA    1 
ATOM   2206 C C     . GLY A 1 282 ? -5.42794  19.17716  21.34850  1.000 35.59443  ? 276 GLY A C     1 
ATOM   2207 O O     . GLY A 1 282 ? -6.43267  19.77324  21.74679  1.000 39.14897  ? 276 GLY A O     1 
ATOM   2208 N N     . PHE A 1 283 ? -4.41468  18.86833  22.16108  1.000 36.96436  ? 277 PHE A N     1 
ATOM   2209 C CA    . PHE A 1 283 ? -4.44306  19.27670  23.56110  1.000 38.12136  ? 277 PHE A CA    1 
ATOM   2210 C C     . PHE A 1 283 ? -4.32846  20.78832  23.70552  1.000 34.54322  ? 277 PHE A C     1 
ATOM   2211 O O     . PHE A 1 283 ? -4.84338  21.35781  24.67442  1.000 35.39127  ? 277 PHE A O     1 
ATOM   2212 C CB    . PHE A 1 283 ? -3.32455  18.57868  24.33480  1.000 40.82325  ? 277 PHE A CB    1 
ATOM   2213 C CG    . PHE A 1 283 ? -3.64998  17.16491  24.72461  1.000 39.32306  ? 277 PHE A CG    1 
ATOM   2214 C CD1   . PHE A 1 283 ? -4.52379  16.90295  25.76638  1.000 48.99055  ? 277 PHE A CD1   1 
ATOM   2215 C CD2   . PHE A 1 283 ? -3.08650  16.09780  24.04514  1.000 45.78372  ? 277 PHE A CD2   1 
ATOM   2216 C CE1   . PHE A 1 283 ? -4.82674  15.60202  26.12629  1.000 51.36806  ? 277 PHE A CE1   1 
ATOM   2217 C CE2   . PHE A 1 283 ? -3.38536  14.79482  24.40002  1.000 48.42131  ? 277 PHE A CE2   1 
ATOM   2218 C CZ    . PHE A 1 283 ? -4.25675  14.54723  25.44160  1.000 43.47666  ? 277 PHE A CZ    1 
ATOM   2219 N N     . ARG A 1 284 ? -3.66532  21.45238  22.75652  1.000 34.37681  ? 278 ARG A N     1 
ATOM   2220 C CA    . ARG A 1 284 ? -3.57340  22.90775  22.80121  1.000 36.39378  ? 278 ARG A CA    1 
ATOM   2221 C C     . ARG A 1 284 ? -4.93144  23.55433  22.56280  1.000 34.67354  ? 278 ARG A C     1 
ATOM   2222 O O     . ARG A 1 284 ? -5.29221  24.52310  23.24097  1.000 33.48375  ? 278 ARG A O     1 
ATOM   2223 C CB    . ARG A 1 284 ? -2.56108  23.40288  21.77022  1.000 30.47104  ? 278 ARG A CB    1 
ATOM   2224 C CG    . ARG A 1 284 ? -2.43761  24.91558  21.70747  1.000 35.66618  ? 278 ARG A CG    1 
ATOM   2225 C CD    . ARG A 1 284 ? -1.29228  25.33515  20.80593  1.000 35.26462  ? 278 ARG A CD    1 
ATOM   2226 N NE    . ARG A 1 284 ? -0.00432  25.25673  21.48524  1.000 44.40630  ? 278 ARG A NE    1 
ATOM   2227 C CZ    . ARG A 1 284 ? 0.92781   24.35133  21.22091  1.000 45.78459  ? 278 ARG A CZ    1 
ATOM   2228 N NH1   . ARG A 1 284 ? 0.74833   23.42487  20.29349  1.000 42.94315  ? 278 ARG A NH1   1 
ATOM   2229 N NH2   . ARG A 1 284 ? 2.06792   24.37485  21.90534  1.000 46.43869  ? 278 ARG A NH2   1 
ATOM   2230 N N     . PHE A 1 285 ? -5.69941  23.03233  21.60400  1.000 33.58290  ? 279 PHE A N     1 
ATOM   2231 C CA    . PHE A 1 285 ? -7.00628  23.61072  21.31203  1.000 36.15216  ? 279 PHE A CA    1 
ATOM   2232 C C     . PHE A 1 285 ? -7.96928  23.45491  22.48230  1.000 35.70335  ? 279 PHE A C     1 
ATOM   2233 O O     . PHE A 1 285 ? -8.85720  24.29440  22.66773  1.000 38.66280  ? 279 PHE A O     1 
ATOM   2234 C CB    . PHE A 1 285 ? -7.59548  22.97254  20.05408  1.000 35.47082  ? 279 PHE A CB    1 
ATOM   2235 C CG    . PHE A 1 285 ? -8.86778  23.61998  19.58746  1.000 34.00574  ? 279 PHE A CG    1 
ATOM   2236 C CD1   . PHE A 1 285 ? -8.83193  24.75338  18.79211  1.000 34.40768  ? 279 PHE A CD1   1 
ATOM   2237 C CD2   . PHE A 1 285 ? -10.09984 23.09718  19.94534  1.000 33.79075  ? 279 PHE A CD2   1 
ATOM   2238 C CE1   . PHE A 1 285 ? -10.00117 25.35256  18.36228  1.000 34.54988  ? 279 PHE A CE1   1 
ATOM   2239 C CE2   . PHE A 1 285 ? -11.27135 23.69239  19.51995  1.000 35.75554  ? 279 PHE A CE2   1 
ATOM   2240 C CZ    . PHE A 1 285 ? -11.22166 24.82133  18.72702  1.000 33.85997  ? 279 PHE A CZ    1 
ATOM   2241 N N     . MET A 1 286 ? -7.81136  22.40086  23.27980  1.000 35.62103  ? 280 MET A N     1 
ATOM   2242 C CA    . MET A 1 286 ? -8.71386  22.14236  24.39431  1.000 41.39059  ? 280 MET A CA    1 
ATOM   2243 C C     . MET A 1 286 ? -8.30577  22.86431  25.67236  1.000 42.25547  ? 280 MET A C     1 
ATOM   2244 O O     . MET A 1 286 ? -9.16292  23.40705  26.37831  1.000 44.60458  ? 280 MET A O     1 
ATOM   2245 C CB    . MET A 1 286 ? -8.77263  20.64575  24.68869  1.000 42.96741  ? 280 MET A CB    1 
ATOM   2246 C CG    . MET A 1 286 ? -9.91758  19.89487  24.06112  1.000 52.66038  ? 280 MET A CG    1 
ATOM   2247 S SD    . MET A 1 286 ? -10.44823 18.62915  25.22245  1.000 67.20094  ? 280 MET A SD    1 
ATOM   2248 C CE    . MET A 1 286 ? -9.24692  17.35687  24.86706  1.000 57.32170  ? 280 MET A CE    1 
ATOM   2249 N N     . PHE A 1 287 ? -7.01317  22.86396  25.99895  1.000 40.23682  ? 281 PHE A N     1 
ATOM   2250 C CA    . PHE A 1 287 ? -6.56320  23.25978  27.32375  1.000 39.05650  ? 281 PHE A CA    1 
ATOM   2251 C C     . PHE A 1 287 ? -5.66789  24.49028  27.34707  1.000 40.28725  ? 281 PHE A C     1 
ATOM   2252 O O     . PHE A 1 287 ? -5.40494  25.01325  28.43587  1.000 37.59777  ? 281 PHE A O     1 
ATOM   2253 C CB    . PHE A 1 287 ? -5.83684  22.08714  28.00181  1.000 34.17789  ? 281 PHE A CB    1 
ATOM   2254 C CG    . PHE A 1 287 ? -6.69222  20.85935  28.15294  1.000 40.78241  ? 281 PHE A CG    1 
ATOM   2255 C CD1   . PHE A 1 287 ? -7.76844  20.85166  29.02438  1.000 39.91363  ? 281 PHE A CD1   1 
ATOM   2256 C CD2   . PHE A 1 287 ? -6.43825  19.72341  27.40135  1.000 43.35327  ? 281 PHE A CD2   1 
ATOM   2257 C CE1   . PHE A 1 287 ? -8.56360  19.72877  29.15813  1.000 41.94365  ? 281 PHE A CE1   1 
ATOM   2258 C CE2   . PHE A 1 287 ? -7.22874  18.59619  27.53202  1.000 42.25199  ? 281 PHE A CE2   1 
ATOM   2259 C CZ    . PHE A 1 287 ? -8.29325  18.59978  28.41075  1.000 44.25469  ? 281 PHE A CZ    1 
ATOM   2260 N N     . GLU A 1 288 ? -5.19476  24.97047  26.19747  1.000 34.91121  ? 282 GLU A N     1 
ATOM   2261 C CA    . GLU A 1 288 ? -4.48512  26.24224  26.15271  1.000 37.27158  ? 282 GLU A CA    1 
ATOM   2262 C C     . GLU A 1 288 ? -5.40927  27.41046  25.83671  1.000 38.72695  ? 282 GLU A C     1 
ATOM   2263 O O     . GLU A 1 288 ? -5.10225  28.54895  26.21022  1.000 38.32989  ? 282 GLU A O     1 
ATOM   2264 C CB    . GLU A 1 288 ? -3.34803  26.18307  25.12389  1.000 34.91928  ? 282 GLU A CB    1 
ATOM   2265 C CG    . GLU A 1 288 ? -2.46376  27.42312  25.08822  1.000 36.07460  ? 282 GLU A CG    1 
ATOM   2266 C CD    . GLU A 1 288 ? -1.13317  27.17977  24.40267  1.000 41.61672  ? 282 GLU A CD    1 
ATOM   2267 O OE1   . GLU A 1 288 ? -0.21508  26.64277  25.05699  1.000 37.12978  ? 282 GLU A OE1   1 
ATOM   2268 O OE2   . GLU A 1 288 ? -1.00335  27.53067  23.21114  1.000 41.09535  ? 282 GLU A OE2   1 
ATOM   2269 N N     . THR A 1 289 ? -6.53878  27.15201  25.17566  1.000 38.77089  ? 283 THR A N     1 
ATOM   2270 C CA    . THR A 1 289 ? -7.49944  28.21273  24.89085  1.000 37.14882  ? 283 THR A CA    1 
ATOM   2271 C C     . THR A 1 289 ? -8.23414  28.63860  26.15596  1.000 41.82585  ? 283 THR A C     1 
ATOM   2272 O O     . THR A 1 289 ? -8.17849  29.80529  26.56201  1.000 41.22388  ? 283 THR A O     1 
ATOM   2273 C CB    . THR A 1 289 ? -8.49552  27.74675  23.82699  1.000 35.06863  ? 283 THR A CB    1 
ATOM   2274 O OG1   . THR A 1 289 ? -9.07294  26.49662  24.22540  1.000 37.45003  ? 283 THR A OG1   1 
ATOM   2275 C CG2   . THR A 1 289 ? -7.80346  27.57246  22.49007  1.000 33.84630  ? 283 THR A CG2   1 
ATOM   2276 N N     . PHE A 1 290 ? -8.93383  27.70109  26.79112  1.000 38.90285  ? 284 PHE A N     1 
ATOM   2277 C CA    . PHE A 1 290 ? -9.72581  27.98462  27.97718  1.000 40.85659  ? 284 PHE A CA    1 
ATOM   2278 C C     . PHE A 1 290 ? -9.56718  26.83405  28.96159  1.000 40.96525  ? 284 PHE A C     1 
ATOM   2279 O O     . PHE A 1 290 ? -9.04984  25.76587  28.62449  1.000 44.89241  ? 284 PHE A O     1 
ATOM   2280 C CB    . PHE A 1 290 ? -11.20020 28.20798  27.61868  1.000 40.19426  ? 284 PHE A CB    1 
ATOM   2281 C CG    . PHE A 1 290 ? -11.41942 29.31091  26.62075  1.000 36.48113  ? 284 PHE A CG    1 
ATOM   2282 C CD1   . PHE A 1 290 ? -11.36361 30.63850  27.01163  1.000 45.22928  ? 284 PHE A CD1   1 
ATOM   2283 C CD2   . PHE A 1 290 ? -11.67147 29.01973  25.28982  1.000 39.33849  ? 284 PHE A CD2   1 
ATOM   2284 C CE1   . PHE A 1 290 ? -11.56228 31.65527  26.09582  1.000 40.23473  ? 284 PHE A CE1   1 
ATOM   2285 C CE2   . PHE A 1 290 ? -11.87009 30.03185  24.36838  1.000 39.06609  ? 284 PHE A CE2   1 
ATOM   2286 C CZ    . PHE A 1 290 ? -11.81496 31.35177  24.77272  1.000 40.20480  ? 284 PHE A CZ    1 
ATOM   2287 N N     . GLY A 1 291 ? -10.02131 27.05879  30.19174  1.000 42.51888  ? 285 GLY A N     1 
ATOM   2288 C CA    . GLY A 1 291 ? -9.82907  26.11156  31.26739  1.000 39.22865  ? 285 GLY A CA    1 
ATOM   2289 C C     . GLY A 1 291 ? -11.02489 25.27324  31.65913  1.000 43.46560  ? 285 GLY A C     1 
ATOM   2290 O O     . GLY A 1 291 ? -10.91604 24.47090  32.59166  1.000 45.33295  ? 285 GLY A O     1 
ATOM   2291 N N     . ASP A 1 292 ? -12.16500 25.42098  30.97797  1.000 42.27093  ? 286 ASP A N     1 
ATOM   2292 C CA    . ASP A 1 292 ? -13.37373 24.68883  31.34130  1.000 44.10009  ? 286 ASP A CA    1 
ATOM   2293 C C     . ASP A 1 292 ? -14.00721 23.98977  30.14312  1.000 45.33873  ? 286 ASP A C     1 
ATOM   2294 O O     . ASP A 1 292 ? -15.19672 23.65854  30.18668  1.000 45.57742  ? 286 ASP A O     1 
ATOM   2295 C CB    . ASP A 1 292 ? -14.39331 25.62267  31.99814  1.000 44.38834  ? 286 ASP A CB    1 
ATOM   2296 C CG    . ASP A 1 292 ? -14.78137 26.78141  31.10151  1.000 48.12956  ? 286 ASP A CG    1 
ATOM   2297 O OD1   . ASP A 1 292 ? -14.01961 27.08631  30.15981  1.000 47.24663  ? 286 ASP A OD1   1 
ATOM   2298 O OD2   . ASP A 1 292 ? -15.84869 27.38618  31.33522  1.000 50.42819  ? 286 ASP A OD2   1 
ATOM   2299 N N     . ILE A 1 293 ? -13.24021 23.75712  29.07617  1.000 43.15202  ? 287 ILE A N     1 
ATOM   2300 C CA    . ILE A 1 293 ? -13.80075 23.13374  27.88121  1.000 42.43976  ? 287 ILE A CA    1 
ATOM   2301 C C     . ILE A 1 293 ? -14.23612 21.70260  28.17641  1.000 44.88194  ? 287 ILE A C     1 
ATOM   2302 O O     . ILE A 1 293 ? -15.27999 21.24450  27.69575  1.000 47.31639  ? 287 ILE A O     1 
ATOM   2303 C CB    . ILE A 1 293 ? -12.78653 23.20331  26.72362  1.000 39.79551  ? 287 ILE A CB    1 
ATOM   2304 C CG1   . ILE A 1 293 ? -12.81230 24.59335  26.08307  1.000 37.65527  ? 287 ILE A CG1   1 
ATOM   2305 C CG2   . ILE A 1 293 ? -13.07290 22.13513  25.67737  1.000 40.02332  ? 287 ILE A CG2   1 
ATOM   2306 C CD1   . ILE A 1 293 ? -11.76593 24.79369  25.01066  1.000 33.79634  ? 287 ILE A CD1   1 
ATOM   2307 N N     . ALA A 1 294 ? -13.46290 20.98289  28.98420  1.000 43.67749  ? 288 ALA A N     1 
ATOM   2308 C CA    . ALA A 1 294 ? -13.79289 19.61399  29.35441  1.000 48.90304  ? 288 ALA A CA    1 
ATOM   2309 C C     . ALA A 1 294 ? -14.70391 19.52714  30.57192  1.000 49.31300  ? 288 ALA A C     1 
ATOM   2310 O O     . ALA A 1 294 ? -15.01948 18.41716  31.01067  1.000 55.83712  ? 288 ALA A O     1 
ATOM   2311 C CB    . ALA A 1 294 ? -12.51146 18.81599  29.61656  1.000 48.13628  ? 288 ALA A CB    1 
ATOM   2312 N N     . VAL A 1 295 ? -15.14259 20.66020  31.12157  1.000 54.48863  ? 289 VAL A N     1 
ATOM   2313 C CA    . VAL A 1 295 ? -15.91821 20.69575  32.35541  1.000 54.76735  ? 289 VAL A CA    1 
ATOM   2314 C C     . VAL A 1 295 ? -17.31952 21.24987  32.12180  1.000 53.13187  ? 289 VAL A C     1 
ATOM   2315 O O     . VAL A 1 295 ? -18.31234 20.66762  32.56974  1.000 56.79070  ? 289 VAL A O     1 
ATOM   2316 C CB    . VAL A 1 295 ? -15.18931 21.50281  33.45337  1.000 51.59166  ? 289 VAL A CB    1 
ATOM   2317 C CG1   . VAL A 1 295 ? -16.03172 21.56515  34.71886  1.000 54.94593  ? 289 VAL A CG1   1 
ATOM   2318 C CG2   . VAL A 1 295 ? -13.82646 20.89204  33.74095  1.000 47.87277  ? 289 VAL A CG2   1 
ATOM   2319 N N     . ASP A 1 296 ? -17.41961 22.37567  31.42210  1.000 48.19807  ? 290 ASP A N     1 
ATOM   2320 C CA    . ASP A 1 296 ? -18.68761 23.06616  31.22658  1.000 50.08147  ? 290 ASP A CA    1 
ATOM   2321 C C     . ASP A 1 296 ? -19.28546 22.69318  29.87591  1.000 53.77662  ? 290 ASP A C     1 
ATOM   2322 O O     . ASP A 1 296 ? -18.58002 22.67551  28.86181  1.000 51.85984  ? 290 ASP A O     1 
ATOM   2323 C CB    . ASP A 1 296 ? -18.49811 24.58066  31.32605  1.000 53.93535  ? 290 ASP A CB    1 
ATOM   2324 C CG    . ASP A 1 296 ? -19.80724 25.33770  31.24652  1.000 55.01858  ? 290 ASP A CG    1 
ATOM   2325 O OD1   . ASP A 1 296 ? -20.62648 25.21269  32.18129  1.000 60.97762  ? 290 ASP A OD1   1 
ATOM   2326 O OD2   . ASP A 1 296 ? -20.01432 26.06213  30.25188  1.000 55.05262  ? 290 ASP A OD2   1 
ATOM   2327 N N     . GLU A 1 297 ? -20.58926 22.40084  29.86964  1.000 57.05478  ? 291 GLU A N     1 
ATOM   2328 C CA    . GLU A 1 297 ? -21.26219 22.01437  28.63270  1.000 54.53730  ? 291 GLU A CA    1 
ATOM   2329 C C     . GLU A 1 297 ? -21.32111 23.17290  27.64448  1.000 52.67995  ? 291 GLU A C     1 
ATOM   2330 O O     . GLU A 1 297 ? -21.07563 22.98690  26.44633  1.000 49.36051  ? 291 GLU A O     1 
ATOM   2331 C CB    . GLU A 1 297 ? -22.67012 21.50394  28.94055  1.000 63.19827  ? 291 GLU A CB    1 
ATOM   2332 C CG    . GLU A 1 297 ? -22.70802 20.18287  29.69247  1.000 61.91927  ? 291 GLU A CG    1 
ATOM   2333 C CD    . GLU A 1 297 ? -22.69248 20.36347  31.19695  1.000 72.30954  ? 291 GLU A CD    1 
ATOM   2334 O OE1   . GLU A 1 297 ? -22.40197 21.48530  31.66090  1.000 69.30743  ? 291 GLU A OE1   1 
ATOM   2335 O OE2   . GLU A 1 297 ? -22.97009 19.38188  31.91676  1.000 74.47023  ? 291 GLU A OE2   1 
ATOM   2336 N N     . THR A 1 298 ? -21.65612 24.37310  28.12558  1.000 51.14597  ? 292 THR A N     1 
ATOM   2337 C CA    . THR A 1 298 ? -21.70153 25.53765  27.24677  1.000 48.74812  ? 292 THR A CA    1 
ATOM   2338 C C     . THR A 1 298 ? -20.32913 25.82956  26.65412  1.000 46.55016  ? 292 THR A C     1 
ATOM   2339 O O     . THR A 1 298 ? -20.21535 26.19300  25.47731  1.000 46.54552  ? 292 THR A O     1 
ATOM   2340 C CB    . THR A 1 298 ? -22.22517 26.75378  28.01266  1.000 49.52228  ? 292 THR A CB    1 
ATOM   2341 O OG1   . THR A 1 298 ? -23.47223 26.42633  28.63823  1.000 52.09655  ? 292 THR A OG1   1 
ATOM   2342 C CG2   . THR A 1 298 ? -22.42960 27.93316  27.07309  1.000 45.90205  ? 292 THR A CG2   1 
ATOM   2343 N N     . ALA A 1 299 ? -19.27373 25.67039  27.45577  1.000 46.42699  ? 293 ALA A N     1 
ATOM   2344 C CA    . ALA A 1 299 ? -17.91952 25.84563  26.94356  1.000 45.64657  ? 293 ALA A CA    1 
ATOM   2345 C C     . ALA A 1 299 ? -17.58793 24.79388  25.89298  1.000 42.51568  ? 293 ALA A C     1 
ATOM   2346 O O     . ALA A 1 299 ? -17.01665 25.11187  24.84295  1.000 41.54719  ? 293 ALA A O     1 
ATOM   2347 C CB    . ALA A 1 299 ? -16.91595 25.78770  28.09450  1.000 44.99067  ? 293 ALA A CB    1 
ATOM   2348 N N     . ASN A 1 300 ? -17.94378 23.53404  26.15927  1.000 41.86428  ? 294 ASN A N     1 
ATOM   2349 C CA    . ASN A 1 300 ? -17.63775 22.45531  25.22464  1.000 42.20843  ? 294 ASN A CA    1 
ATOM   2350 C C     . ASN A 1 300 ? -18.33764 22.66261  23.88746  1.000 41.33013  ? 294 ASN A C     1 
ATOM   2351 O O     . ASN A 1 300 ? -17.75787 22.39808  22.82761  1.000 39.76600  ? 294 ASN A O     1 
ATOM   2352 C CB    . ASN A 1 300 ? -18.03434 21.11095  25.83580  1.000 46.42035  ? 294 ASN A CB    1 
ATOM   2353 C CG    . ASN A 1 300 ? -17.43088 19.93169  25.09764  1.000 48.25913  ? 294 ASN A CG    1 
ATOM   2354 O OD1   . ASN A 1 300 ? -17.99335 19.44537  24.11717  1.000 44.26703  ? 294 ASN A OD1   1 
ATOM   2355 N ND2   . ASN A 1 300 ? -16.28276 19.46101  25.57109  1.000 43.45404  ? 294 ASN A ND2   1 
ATOM   2356 N N     . ILE A 1 301 ? -19.58491 23.13661  23.91682  1.000 41.18302  ? 295 ILE A N     1 
ATOM   2357 C CA    . ILE A 1 301 ? -20.32434 23.36424  22.67922  1.000 43.35024  ? 295 ILE A CA    1 
ATOM   2358 C C     . ILE A 1 301 ? -19.67826 24.48223  21.86888  1.000 39.61465  ? 295 ILE A C     1 
ATOM   2359 O O     . ILE A 1 301 ? -19.63872 24.42930  20.63301  1.000 42.58308  ? 295 ILE A O     1 
ATOM   2360 C CB    . ILE A 1 301 ? -21.80366 23.65710  22.99582  1.000 45.17512  ? 295 ILE A CB    1 
ATOM   2361 C CG1   . ILE A 1 301 ? -22.55879 22.34904  23.24336  1.000 48.60342  ? 295 ILE A CG1   1 
ATOM   2362 C CG2   . ILE A 1 301 ? -22.46307 24.44475  21.87256  1.000 42.81081  ? 295 ILE A CG2   1 
ATOM   2363 C CD1   . ILE A 1 301 ? -23.89971 22.53297  23.92260  1.000 49.76033  ? 295 ILE A CD1   1 
ATOM   2364 N N     . GLU A 1 302 ? -19.14346 25.50018  22.54869  1.000 43.93969  ? 296 GLU A N     1 
ATOM   2365 C CA    . GLU A 1 302 ? -18.46366 26.58365  21.84490  1.000 42.16505  ? 296 GLU A CA    1 
ATOM   2366 C C     . GLU A 1 302 ? -17.23690 26.07402  21.09796  1.000 39.19713  ? 296 GLU A C     1 
ATOM   2367 O O     . GLU A 1 302 ? -16.97230 26.49316  19.96511  1.000 38.43061  ? 296 GLU A O     1 
ATOM   2368 C CB    . GLU A 1 302 ? -18.07417 27.68618  22.82923  1.000 46.98336  ? 296 GLU A CB    1 
ATOM   2369 C CG    . GLU A 1 302 ? -19.20490 28.64521  23.15885  1.000 50.40127  ? 296 GLU A CG    1 
ATOM   2370 C CD    . GLU A 1 302 ? -19.72450 29.37331  21.93557  1.000 53.24325  ? 296 GLU A CD    1 
ATOM   2371 O OE1   . GLU A 1 302 ? -18.94420 30.12304  21.31177  1.000 50.03201  ? 296 GLU A OE1   1 
ATOM   2372 O OE2   . GLU A 1 302 ? -20.91292 29.19335  21.59670  1.000 52.27458  ? 296 GLU A OE2   1 
ATOM   2373 N N     . ALA A 1 303 ? -16.47352 25.16966  21.71636  1.000 38.18537  ? 297 ALA A N     1 
ATOM   2374 C CA    . ALA A 1 303 ? -15.33233 24.57863  21.02647  1.000 37.77439  ? 297 ALA A CA    1 
ATOM   2375 C C     . ALA A 1 303 ? -15.77771 23.68928  19.87290  1.000 38.23431  ? 297 ALA A C     1 
ATOM   2376 O O     . ALA A 1 303 ? -15.08253 23.60440  18.85404  1.000 36.29865  ? 297 ALA A O     1 
ATOM   2377 C CB    . ALA A 1 303 ? -14.47249 23.78666  22.01105  1.000 35.50499  ? 297 ALA A CB    1 
ATOM   2378 N N     . GLN A 1 304 ? -16.92746 23.02408  20.01308  1.000 38.09142  ? 298 GLN A N     1 
ATOM   2379 C CA    . GLN A 1 304 ? -17.46372 22.22086  18.91856  1.000 34.31939  ? 298 GLN A CA    1 
ATOM   2380 C C     . GLN A 1 304 ? -17.80794 23.09478  17.72042  1.000 35.58499  ? 298 GLN A C     1 
ATOM   2381 O O     . GLN A 1 304 ? -17.44817 22.77943  16.58029  1.000 34.87854  ? 298 GLN A O     1 
ATOM   2382 C CB    . GLN A 1 304 ? -18.70516 21.45864  19.38369  1.000 36.41079  ? 298 GLN A CB    1 
ATOM   2383 C CG    . GLN A 1 304 ? -18.44874 20.37251  20.40750  1.000 43.67306  ? 298 GLN A CG    1 
ATOM   2384 C CD    . GLN A 1 304 ? -19.72806 19.90906  21.07695  1.000 50.27936  ? 298 GLN A CD    1 
ATOM   2385 O OE1   . GLN A 1 304 ? -20.78632 19.85649  20.45004  1.000 52.37184  ? 298 GLN A OE1   1 
ATOM   2386 N NE2   . GLN A 1 304 ? -19.64022 19.58501  22.36022  1.000 49.57558  ? 298 GLN A NE2   1 
ATOM   2387 N N     . ASN A 1 305 ? -18.50932 24.20509  17.96555  1.000 32.59211  ? 299 ASN A N     1 
ATOM   2388 C CA    . ASN A 1 305 ? -18.99195 25.04297  16.87373  1.000 35.96350  ? 299 ASN A CA    1 
ATOM   2389 C C     . ASN A 1 305 ? -17.84914 25.69234  16.10433  1.000 33.37251  ? 299 ASN A C     1 
ATOM   2390 O O     . ASN A 1 305 ? -18.00397 26.00193  14.91780  1.000 33.90020  ? 299 ASN A O     1 
ATOM   2391 C CB    . ASN A 1 305 ? -19.94499 26.10779  17.41680  1.000 37.48737  ? 299 ASN A CB    1 
ATOM   2392 C CG    . ASN A 1 305 ? -21.18760 25.50811  18.04733  1.000 44.28163  ? 299 ASN A CG    1 
ATOM   2393 O OD1   . ASN A 1 305 ? -21.54804 24.36408  17.76903  1.000 40.90835  ? 299 ASN A OD1   1 
ATOM   2394 N ND2   . ASN A 1 305 ? -21.84961 26.27918  18.90158  1.000 47.53383  ? 299 ASN A ND2   1 
ATOM   2395 N N     . PHE A 1 306 ? -16.70114 25.90815  16.75020  1.000 33.39080  ? 300 PHE A N     1 
ATOM   2396 C CA    . PHE A 1 306 ? -15.55983 26.45845  16.02724  1.000 34.94740  ? 300 PHE A CA    1 
ATOM   2397 C C     . PHE A 1 306 ? -14.99955 25.44631  15.03689  1.000 31.40591  ? 300 PHE A C     1 
ATOM   2398 O O     . PHE A 1 306 ? -14.69966 25.79387  13.88877  1.000 33.85872  ? 300 PHE A O     1 
ATOM   2399 C CB    . PHE A 1 306 ? -14.47381 26.91014  17.00285  1.000 31.68140  ? 300 PHE A CB    1 
ATOM   2400 C CG    . PHE A 1 306 ? -13.34035 27.64527  16.34283  1.000 34.56353  ? 300 PHE A CG    1 
ATOM   2401 C CD1   . PHE A 1 306 ? -13.39657 29.01889  16.17355  1.000 32.28037  ? 300 PHE A CD1   1 
ATOM   2402 C CD2   . PHE A 1 306 ? -12.22284 26.96402  15.88549  1.000 31.74014  ? 300 PHE A CD2   1 
ATOM   2403 C CE1   . PHE A 1 306 ? -12.36077 29.69979  15.56366  1.000 33.55602  ? 300 PHE A CE1   1 
ATOM   2404 C CE2   . PHE A 1 306 ? -11.18346 27.64022  15.27409  1.000 32.59577  ? 300 PHE A CE2   1 
ATOM   2405 C CZ    . PHE A 1 306 ? -11.25260 29.00983  15.11388  1.000 33.28859  ? 300 PHE A CZ    1 
ATOM   2406 N N     . ILE A 1 307 ? -14.84871 24.19052  15.46239  1.000 30.97969  ? 301 ILE A N     1 
ATOM   2407 C CA    . ILE A 1 307 ? -14.35235 23.15921  14.55742  1.000 31.40648  ? 301 ILE A CA    1 
ATOM   2408 C C     . ILE A 1 307 ? -15.38866 22.84866  13.48508  1.000 33.04908  ? 301 ILE A C     1 
ATOM   2409 O O     . ILE A 1 307 ? -15.04747 22.65374  12.31197  1.000 31.31926  ? 301 ILE A O     1 
ATOM   2410 C CB    . ILE A 1 307 ? -13.95525 21.89936  15.34762  1.000 32.37127  ? 301 ILE A CB    1 
ATOM   2411 C CG1   . ILE A 1 307 ? -12.92553 22.24892  16.42491  1.000 35.62292  ? 301 ILE A CG1   1 
ATOM   2412 C CG2   . ILE A 1 307 ? -13.40772 20.83142  14.41046  1.000 29.48321  ? 301 ILE A CG2   1 
ATOM   2413 C CD1   . ILE A 1 307 ? -12.60333 21.10269  17.36108  1.000 34.53816  ? 301 ILE A CD1   1 
ATOM   2414 N N     . LYS A 1 308 ? -16.66856 22.79838  13.86785  1.000 30.88320  ? 302 LYS A N     1 
ATOM   2415 C CA    . LYS A 1 308 ? -17.73052 22.59216  12.88725  1.000 33.37219  ? 302 LYS A CA    1 
ATOM   2416 C C     . LYS A 1 308 ? -17.71409 23.68222  11.82411  1.000 32.21315  ? 302 LYS A C     1 
ATOM   2417 O O     . LYS A 1 308 ? -17.86807 23.39988  10.63015  1.000 37.51086  ? 302 LYS A O     1 
ATOM   2418 C CB    . LYS A 1 308 ? -19.09049 22.55206  13.58486  1.000 37.18384  ? 302 LYS A CB    1 
ATOM   2419 C CG    . LYS A 1 308 ? -19.34956 21.29794  14.40313  1.000 35.69532  ? 302 LYS A CG    1 
ATOM   2420 C CD    . LYS A 1 308 ? -20.79121 21.26089  14.88852  1.000 40.97324  ? 302 LYS A CD    1 
ATOM   2421 C CE    . LYS A 1 308 ? -21.01223 20.14847  15.89737  1.000 49.18490  ? 302 LYS A CE    1 
ATOM   2422 N NZ    . LYS A 1 308 ? -22.39532 20.16562  16.44919  1.000 53.01272  ? 302 LYS A NZ    1 
ATOM   2423 N N     . LYS A 1 309 ? -17.52764 24.93631  12.24190  1.000 33.84453  ? 303 LYS A N     1 
ATOM   2424 C CA    . LYS A 1 309 ? -17.43351 26.03378  11.28551  1.000 35.74855  ? 303 LYS A CA    1 
ATOM   2425 C C     . LYS A 1 309 ? -16.20342 25.88475  10.39894  1.000 34.71541  ? 303 LYS A C     1 
ATOM   2426 O O     . LYS A 1 309 ? -16.24498 26.20595  9.20523   1.000 35.39702  ? 303 LYS A O     1 
ATOM   2427 C CB    . LYS A 1 309 ? -17.40835 27.36737  12.03244  1.000 32.12482  ? 303 LYS A CB    1 
ATOM   2428 C CG    . LYS A 1 309 ? -17.33665 28.59633  11.14611  1.000 42.56529  ? 303 LYS A CG    1 
ATOM   2429 C CD    . LYS A 1 309 ? -16.18897 29.49719  11.56957  1.000 47.18951  ? 303 LYS A CD    1 
ATOM   2430 C CE    . LYS A 1 309 ? -16.47718 30.95219  11.24168  1.000 55.41617  ? 303 LYS A CE    1 
ATOM   2431 N NZ    . LYS A 1 309 ? -15.23191 31.70568  10.93178  1.000 57.70238  ? 303 LYS A NZ    1 
ATOM   2432 N N     . LYS A 1 310 ? -15.09840 25.39342  10.96494  1.000 35.82884  ? 304 LYS A N     1 
ATOM   2433 C CA    . LYS A 1 310 ? -13.90150 25.15864  10.16396  1.000 33.73231  ? 304 LYS A CA    1 
ATOM   2434 C C     . LYS A 1 310 ? -14.13774 24.06231  9.13359   1.000 29.87069  ? 304 LYS A C     1 
ATOM   2435 O O     . LYS A 1 310 ? -13.63511 24.13951  8.00651   1.000 29.53470  ? 304 LYS A O     1 
ATOM   2436 C CB    . LYS A 1 310 ? -12.72487 24.79834  11.07074  1.000 32.83821  ? 304 LYS A CB    1 
ATOM   2437 C CG    . LYS A 1 310 ? -12.08990 25.98919  11.77040  1.000 31.41880  ? 304 LYS A CG    1 
ATOM   2438 C CD    . LYS A 1 310 ? -11.46337 26.94696  10.77054  1.000 35.13393  ? 304 LYS A CD    1 
ATOM   2439 C CE    . LYS A 1 310 ? -10.58023 27.96811  11.46811  1.000 33.90458  ? 304 LYS A CE    1 
ATOM   2440 N NZ    . LYS A 1 310 ? -9.99897  28.94437  10.50719  1.000 42.20404  ? 304 LYS A NZ    1 
ATOM   2441 N N     . ILE A 1 311 ? -14.90124 23.03163  9.50273   1.000 28.92911  ? 305 ILE A N     1 
ATOM   2442 C CA    . ILE A 1 311 ? -15.21434 21.96220  8.55860   1.000 31.21548  ? 305 ILE A CA    1 
ATOM   2443 C C     . ILE A 1 311 ? -16.03829 22.50639  7.39795   1.000 33.33278  ? 305 ILE A C     1 
ATOM   2444 O O     . ILE A 1 311 ? -15.71563 22.28274  6.22614   1.000 30.88325  ? 305 ILE A O     1 
ATOM   2445 C CB    . ILE A 1 311 ? -15.93837 20.80671  9.27351   1.000 34.80700  ? 305 ILE A CB    1 
ATOM   2446 C CG1   . ILE A 1 311 ? -14.99401 20.10749  10.25450  1.000 27.05679  ? 305 ILE A CG1   1 
ATOM   2447 C CG2   . ILE A 1 311 ? -16.48741 19.81210  8.26093   1.000 32.26157  ? 305 ILE A CG2   1 
ATOM   2448 C CD1   . ILE A 1 311 ? -15.69510 19.17534  11.21844  1.000 26.34532  ? 305 ILE A CD1   1 
ATOM   2449 N N     . SER A 1 312 ? -17.10728 23.24548  7.70722   1.000 32.27746  ? 306 SER A N     1 
ATOM   2450 C CA    . SER A 1 312 ? -17.97024 23.78646  6.66159   1.000 36.85699  ? 306 SER A CA    1 
ATOM   2451 C C     . SER A 1 312 ? -17.22669 24.72738  5.72255   1.000 32.10073  ? 306 SER A C     1 
ATOM   2452 O O     . SER A 1 312 ? -17.64829 24.89873  4.57346   1.000 38.13938  ? 306 SER A O     1 
ATOM   2453 C CB    . SER A 1 312 ? -19.16428 24.51199  7.28624   1.000 39.43836  ? 306 SER A CB    1 
ATOM   2454 O OG    . SER A 1 312 ? -18.78091 25.77464  7.80346   1.000 42.20249  ? 306 SER A OG    1 
ATOM   2455 N N     . GLU A 1 313 ? -16.13167 25.33403  6.17869   1.000 33.93560  ? 307 GLU A N     1 
ATOM   2456 C CA    . GLU A 1 313 ? -15.34093 26.21746  5.33172   1.000 33.20769  ? 307 GLU A CA    1 
ATOM   2457 C C     . GLU A 1 313 ? -14.30740 25.47176  4.49942   1.000 30.54533  ? 307 GLU A C     1 
ATOM   2458 O O     . GLU A 1 313 ? -14.01583 25.88716  3.37170   1.000 31.66282  ? 307 GLU A O     1 
ATOM   2459 C CB    . GLU A 1 313 ? -14.62974 27.27133  6.18488   1.000 34.15025  ? 307 GLU A CB    1 
ATOM   2460 C CG    . GLU A 1 313 ? -15.53693 28.36548  6.71809   1.000 35.74257  ? 307 GLU A CG    1 
ATOM   2461 C CD    . GLU A 1 313 ? -14.84929 29.22945  7.75410   1.000 45.88424  ? 307 GLU A CD    1 
ATOM   2462 O OE1   . GLU A 1 313 ? -13.62856 29.06116  7.95454   1.000 45.71016  ? 307 GLU A OE1   1 
ATOM   2463 O OE2   . GLU A 1 313 ? -15.52654 30.08154  8.36252   1.000 50.20712  ? 307 GLU A OE2   1 
ATOM   2464 N N     . ILE A 1 314 ? -13.74756 24.38305  5.02528   1.000 33.65608  ? 308 ILE A N     1 
ATOM   2465 C CA    . ILE A 1 314 ? -12.66869 23.68526  4.33020   1.000 33.45568  ? 308 ILE A CA    1 
ATOM   2466 C C     . ILE A 1 314 ? -13.22109 22.82011  3.20288   1.000 35.04160  ? 308 ILE A C     1 
ATOM   2467 O O     . ILE A 1 314 ? -12.85324 22.98648  2.03399   1.000 36.85881  ? 308 ILE A O     1 
ATOM   2468 C CB    . ILE A 1 314 ? -11.83342 22.85844  5.32487   1.000 32.54865  ? 308 ILE A CB    1 
ATOM   2469 C CG1   . ILE A 1 314 ? -11.00254 23.78711  6.21488   1.000 30.73318  ? 308 ILE A CG1   1 
ATOM   2470 C CG2   . ILE A 1 314 ? -10.93035 21.88624  4.58307   1.000 35.40182  ? 308 ILE A CG2   1 
ATOM   2471 C CD1   . ILE A 1 314 ? -10.40723 23.10401  7.42916   1.000 34.24193  ? 308 ILE A CD1   1 
ATOM   2472 N N     . VAL A 1 315 ? -14.10492 21.88121  3.53032   1.000 32.58790  ? 309 VAL A N     1 
ATOM   2473 C CA    . VAL A 1 315 ? -14.70142 21.02703  2.50732   1.000 33.16488  ? 309 VAL A CA    1 
ATOM   2474 C C     . VAL A 1 315 ? -15.83613 21.80133  1.84524   1.000 35.34849  ? 309 VAL A C     1 
ATOM   2475 O O     . VAL A 1 315 ? -16.73830 22.30833  2.52094   1.000 35.28150  ? 309 VAL A O     1 
ATOM   2476 C CB    . VAL A 1 315 ? -15.18008 19.68696  3.09448   1.000 36.72962  ? 309 VAL A CB    1 
ATOM   2477 C CG1   . VAL A 1 315 ? -15.19071 19.72582  4.61574   1.000 32.62595  ? 309 VAL A CG1   1 
ATOM   2478 C CG2   . VAL A 1 315 ? -16.53660 19.26943  2.52984   1.000 36.11908  ? 309 VAL A CG2   1 
ATOM   2479 N N     . LYS A 1 316 ? -15.77381 21.91887  0.51749   1.000 33.91812  ? 310 LYS A N     1 
ATOM   2480 C CA    . LYS A 1 316 ? -16.65051 22.83905  -0.19848  1.000 36.68416  ? 310 LYS A CA    1 
ATOM   2481 C C     . LYS A 1 316 ? -18.03212 22.25200  -0.45222  1.000 37.14714  ? 310 LYS A C     1 
ATOM   2482 O O     . LYS A 1 316 ? -19.01726 22.99762  -0.48103  1.000 38.89837  ? 310 LYS A O     1 
ATOM   2483 C CB    . LYS A 1 316 ? -15.99984 23.25447  -1.51904  1.000 40.89418  ? 310 LYS A CB    1 
ATOM   2484 C CG    . LYS A 1 316 ? -14.68006 23.99276  -1.34387  1.000 40.77147  ? 310 LYS A CG    1 
ATOM   2485 C CD    . LYS A 1 316 ? -14.80063 25.09519  -0.30086  1.000 40.30877  ? 310 LYS A CD    1 
ATOM   2486 C CE    . LYS A 1 316 ? -13.53044 25.92672  -0.21792  1.000 43.40561  ? 310 LYS A CE    1 
ATOM   2487 N NZ    . LYS A 1 316 ? -12.35967 25.10986  0.21009   1.000 45.75650  ? 310 LYS A NZ    1 
ATOM   2488 N N     . ASP A 1 317 ? -18.12757 20.94657  -0.64605  1.000 35.48126  ? 311 ASP A N     1 
ATOM   2489 C CA    . ASP A 1 317 ? -19.42542 20.30105  -0.78311  1.000 36.70360  ? 311 ASP A CA    1 
ATOM   2490 C C     . ASP A 1 317 ? -20.12300 20.30424  0.57063   1.000 34.97890  ? 311 ASP A C     1 
ATOM   2491 O O     . ASP A 1 317 ? -19.66091 19.61472  1.48957   1.000 32.14297  ? 311 ASP A O     1 
ATOM   2492 C CB    . ASP A 1 317 ? -19.25696 18.87284  -1.30514  1.000 34.70178  ? 311 ASP A CB    1 
ATOM   2493 C CG    . ASP A 1 317 ? -20.56957 18.25104  -1.75621  1.000 39.30024  ? 311 ASP A CG    1 
ATOM   2494 O OD1   . ASP A 1 317 ? -21.64097 18.68810  -1.28826  1.000 41.06826  ? 311 ASP A OD1   1 
ATOM   2495 O OD2   . ASP A 1 317 ? -20.52940 17.31900  -2.58578  1.000 42.84583  ? 311 ASP A OD2   1 
ATOM   2496 N N     . PRO A 1 318 ? -21.22114 21.04687  0.74544   1.000 39.10494  ? 312 PRO A N     1 
ATOM   2497 C CA    . PRO A 1 318 ? -21.85678 21.11119  2.07168   1.000 33.74727  ? 312 PRO A CA    1 
ATOM   2498 C C     . PRO A 1 318 ? -22.41867 19.78323  2.54148   1.000 30.70509  ? 312 PRO A C     1 
ATOM   2499 O O     . PRO A 1 318 ? -22.58644 19.59649  3.75281   1.000 36.06211  ? 312 PRO A O     1 
ATOM   2500 C CB    . PRO A 1 318 ? -22.96962 22.15063  1.87958   1.000 37.68918  ? 312 PRO A CB    1 
ATOM   2501 C CG    . PRO A 1 318 ? -23.26909 22.11342  0.41643   1.000 43.44412  ? 312 PRO A CG    1 
ATOM   2502 C CD    . PRO A 1 318 ? -21.96596 21.81355  -0.26874  1.000 37.36701  ? 312 PRO A CD    1 
ATOM   2503 N N     . PHE A 1 319 ? -22.70967 18.85525  1.62967   1.000 32.29232  ? 313 PHE A N     1 
ATOM   2504 C CA    . PHE A 1 319 ? -23.24648 17.56145  2.03158   1.000 32.16377  ? 313 PHE A CA    1 
ATOM   2505 C C     . PHE A 1 319 ? -22.15100 16.60764  2.48773   1.000 31.85265  ? 313 PHE A C     1 
ATOM   2506 O O     . PHE A 1 319 ? -22.40125 15.74600  3.33782   1.000 32.73870  ? 313 PHE A O     1 
ATOM   2507 C CB    . PHE A 1 319 ? -24.05244 16.95762  0.88214   1.000 36.97294  ? 313 PHE A CB    1 
ATOM   2508 C CG    . PHE A 1 319 ? -25.03817 17.91570  0.27904   1.000 43.54166  ? 313 PHE A CG    1 
ATOM   2509 C CD1   . PHE A 1 319 ? -26.28937 18.08719  0.84655   1.000 47.09608  ? 313 PHE A CD1   1 
ATOM   2510 C CD2   . PHE A 1 319 ? -24.70895 18.65854  -0.84219  1.000 44.38888  ? 313 PHE A CD2   1 
ATOM   2511 C CE1   . PHE A 1 319 ? -27.19641 18.97366  0.30171   1.000 43.61992  ? 313 PHE A CE1   1 
ATOM   2512 C CE2   . PHE A 1 319 ? -25.61164 19.54715  -1.39088  1.000 50.65573  ? 313 PHE A CE2   1 
ATOM   2513 C CZ    . PHE A 1 319 ? -26.85652 19.70432  -0.81661  1.000 42.70410  ? 313 PHE A CZ    1 
ATOM   2514 N N     . VAL A 1 320 ? -20.94052 16.74308  1.94330   1.000 32.16097  ? 314 VAL A N     1 
ATOM   2515 C CA    . VAL A 1 320 ? -19.80796 15.99432  2.47685   1.000 30.85308  ? 314 VAL A CA    1 
ATOM   2516 C C     . VAL A 1 320 ? -19.37971 16.57555  3.81819   1.000 29.41570  ? 314 VAL A C     1 
ATOM   2517 O O     . VAL A 1 320 ? -19.04309 15.83759  4.75205   1.000 30.54950  ? 314 VAL A O     1 
ATOM   2518 C CB    . VAL A 1 320 ? -18.64733 15.98098  1.46512   1.000 36.45932  ? 314 VAL A CB    1 
ATOM   2519 C CG1   . VAL A 1 320 ? -17.48411 15.15319  1.99881   1.000 30.77885  ? 314 VAL A CG1   1 
ATOM   2520 C CG2   . VAL A 1 320 ? -19.11984 15.44120  0.12269   1.000 31.78554  ? 314 VAL A CG2   1 
ATOM   2521 N N     . ALA A 1 321 ? -19.39301 17.90665  3.93725   1.000 29.54478  ? 315 ALA A N     1 
ATOM   2522 C CA    . ALA A 1 321 ? -19.08036 18.54400  5.21249   1.000 29.96814  ? 315 ALA A CA    1 
ATOM   2523 C C     . ALA A 1 321 ? -20.07446 18.13408  6.29046   1.000 34.34884  ? 315 ALA A C     1 
ATOM   2524 O O     . ALA A 1 321 ? -19.70112 17.95908  7.45657   1.000 30.63443  ? 315 ALA A O     1 
ATOM   2525 C CB    . ALA A 1 321 ? -19.06416 20.06360  5.05007   1.000 33.11379  ? 315 ALA A CB    1 
ATOM   2526 N N     . LYS A 1 322 ? -21.34799 17.98059  5.91838   1.000 33.01326  ? 316 LYS A N     1 
ATOM   2527 C CA    . LYS A 1 322 ? -22.34835 17.50790  6.86938   1.000 33.05579  ? 316 LYS A CA    1 
ATOM   2528 C C     . LYS A 1 322 ? -22.01580 16.10592  7.36200   1.000 31.39743  ? 316 LYS A C     1 
ATOM   2529 O O     . LYS A 1 322 ? -22.12011 15.81813  8.56026   1.000 32.34303  ? 316 LYS A O     1 
ATOM   2530 C CB    . LYS A 1 322 ? -23.73428 17.53643  6.22388   1.000 32.78658  ? 316 LYS A CB    1 
ATOM   2531 C CG    . LYS A 1 322 ? -24.88256 17.27724  7.18421   1.000 41.77244  ? 316 LYS A CG    1 
ATOM   2532 C CD    . LYS A 1 322 ? -26.20254 17.75777  6.59927   1.000 52.49294  ? 316 LYS A CD    1 
ATOM   2533 C CE    . LYS A 1 322 ? -27.37423 17.39529  7.49721   1.000 55.67664  ? 316 LYS A CE    1 
ATOM   2534 N NZ    . LYS A 1 322 ? -28.68027 17.72743  6.86316   1.000 59.04613  ? 316 LYS A NZ    1 
ATOM   2535 N N     . LYS A 1 323 ? -21.60606 15.22114  6.44936   1.000 36.04036  ? 317 LYS A N     1 
ATOM   2536 C CA    . LYS A 1 323 ? -21.24309 13.86303  6.83861   1.000 29.78869  ? 317 LYS A CA    1 
ATOM   2537 C C     . LYS A 1 323 ? -20.01707 13.84515  7.74288   1.000 30.06139  ? 317 LYS A C     1 
ATOM   2538 O O     . LYS A 1 323 ? -19.90798 12.98273  8.62178   1.000 32.48126  ? 317 LYS A O     1 
ATOM   2539 C CB    . LYS A 1 323 ? -20.99772 13.01306  5.59159   1.000 34.11328  ? 317 LYS A CB    1 
ATOM   2540 C CG    . LYS A 1 323 ? -21.41198 11.55957  5.73317   1.000 39.11420  ? 317 LYS A CG    1 
ATOM   2541 C CD    . LYS A 1 323 ? -21.22856 10.80435  4.42473   1.000 39.09631  ? 317 LYS A CD    1 
ATOM   2542 C CE    . LYS A 1 323 ? -22.16884 11.32209  3.34804   1.000 39.22640  ? 317 LYS A CE    1 
ATOM   2543 N NZ    . LYS A 1 323 ? -22.07485 10.52028  2.09623   1.000 38.78355  ? 317 LYS A NZ    1 
ATOM   2544 N N     . LEU A 1 324 ? -19.08878 14.78304  7.54702   1.000 29.31141  ? 318 LEU A N     1 
ATOM   2545 C CA    . LEU A 1 324 ? -17.88946 14.86157  8.37207   1.000 29.00359  ? 318 LEU A CA    1 
ATOM   2546 C C     . LEU A 1 324 ? -18.13651 15.51413  9.72459   1.000 33.09032  ? 318 LEU A C     1 
ATOM   2547 O O     . LEU A 1 324 ? -17.27657 15.41530  10.60666  1.000 35.80931  ? 318 LEU A O     1 
ATOM   2548 C CB    . LEU A 1 324 ? -16.79259 15.63770  7.63858   1.000 29.70672  ? 318 LEU A CB    1 
ATOM   2549 C CG    . LEU A 1 324 ? -16.12267 14.96054  6.44408   1.000 27.02519  ? 318 LEU A CG    1 
ATOM   2550 C CD1   . LEU A 1 324 ? -15.40877 15.99124  5.58309   1.000 26.38282  ? 318 LEU A CD1   1 
ATOM   2551 C CD2   . LEU A 1 324 ? -15.15477 13.88656  6.91456   1.000 27.24404  ? 318 LEU A CD2   1 
ATOM   2552 N N     . THR A 1 325 ? -19.27219 16.17195  9.90735   1.000 36.10546  ? 319 THR A N     1 
ATOM   2553 C CA    . THR A 1 325 ? -19.52895 16.90487  11.14065  1.000 33.75412  ? 319 THR A CA    1 
ATOM   2554 C C     . THR A 1 325 ? -20.01412 15.95039  12.22613  1.000 33.22306  ? 319 THR A C     1 
ATOM   2555 O O     . THR A 1 325 ? -20.98719 15.22076  12.01203  1.000 36.31316  ? 319 THR A O     1 
ATOM   2556 C CB    . THR A 1 325 ? -20.56166 18.00067  10.90528  1.000 31.71286  ? 319 THR A CB    1 
ATOM   2557 O OG1   . THR A 1 325 ? -20.08505 18.89204  9.88948   1.000 36.00665  ? 319 THR A OG1   1 
ATOM   2558 C CG2   . THR A 1 325 ? -20.80621 18.78353  12.18301  1.000 34.79436  ? 319 THR A CG2   1 
ATOM   2559 N N     . PRO A 1 326 ? -19.36773 15.92445  13.38974  1.000 34.82039  ? 320 PRO A N     1 
ATOM   2560 C CA    . PRO A 1 326 ? -19.78522 14.99048  14.44134  1.000 41.36785  ? 320 PRO A CA    1 
ATOM   2561 C C     . PRO A 1 326 ? -21.15025 15.35351  15.00641  1.000 44.24774  ? 320 PRO A C     1 
ATOM   2562 O O     . PRO A 1 326 ? -21.48114 16.52875  15.18477  1.000 41.48610  ? 320 PRO A O     1 
ATOM   2563 C CB    . PRO A 1 326 ? -18.68564 15.13468  15.50141  1.000 40.16041  ? 320 PRO A CB    1 
ATOM   2564 C CG    . PRO A 1 326 ? -17.51928 15.74005  14.76798  1.000 38.92696  ? 320 PRO A CG    1 
ATOM   2565 C CD    . PRO A 1 326 ? -18.13830 16.64729  13.75202  1.000 34.65542  ? 320 PRO A CD    1 
ATOM   2566 N N     . THR A 1 327 ? -21.94598 14.32290  15.28196  1.000 47.69237  ? 321 THR A N     1 
ATOM   2567 C CA    . THR A 1 327 ? -23.26400 14.48536  15.87920  1.000 52.87975  ? 321 THR A CA    1 
ATOM   2568 C C     . THR A 1 327 ? -23.23559 14.40121  17.39899  1.000 58.45456  ? 321 THR A C     1 
ATOM   2569 O O     . THR A 1 327 ? -24.29816 14.45449  18.02740  1.000 64.68241  ? 321 THR A O     1 
ATOM   2570 C CB    . THR A 1 327 ? -24.22979 13.43058  15.32849  1.000 56.95413  ? 321 THR A CB    1 
ATOM   2571 O OG1   . THR A 1 327 ? -23.81152 12.12748  15.75407  1.000 61.45722  ? 321 THR A OG1   1 
ATOM   2572 C CG2   . THR A 1 327 ? -24.25927 13.47644  13.80822  1.000 50.44254  ? 321 THR A CG2   1 
ATOM   2573 N N     . ASP A 1 328 ? -22.05365 14.26535  17.99763  1.000 61.01300  ? 322 ASP A N     1 
ATOM   2574 C CA    . ASP A 1 328 ? -21.94497 14.19811  19.44837  1.000 62.96863  ? 322 ASP A CA    1 
ATOM   2575 C C     . ASP A 1 328 ? -22.43283 15.49559  20.07855  1.000 62.87143  ? 322 ASP A C     1 
ATOM   2576 O O     . ASP A 1 328 ? -22.05849 16.58966  19.64629  1.000 64.06034  ? 322 ASP A O     1 
ATOM   2577 C CB    . ASP A 1 328 ? -20.49534 13.93014  19.85523  1.000 63.34801  ? 322 ASP A CB    1 
ATOM   2578 C CG    . ASP A 1 328 ? -20.19543 12.45323  20.01783  1.000 71.59449  ? 322 ASP A CG    1 
ATOM   2579 O OD1   . ASP A 1 328 ? -19.12086 12.12268  20.56216  1.000 76.47755  ? 322 ASP A OD1   1 
ATOM   2580 O OD2   . ASP A 1 328 ? -21.03046 11.62329  19.60225  1.000 75.58433  ? 322 ASP A OD2   1 
ATOM   2581 N N     . LEU A 1 329 ? -23.28212 15.37110  21.10053  1.000 66.50793  ? 323 LEU A N     1 
ATOM   2582 C CA    . LEU A 1 329 ? -23.70894 16.55294  21.84135  1.000 63.45744  ? 323 LEU A CA    1 
ATOM   2583 C C     . LEU A 1 329 ? -22.53801 17.17714  22.58824  1.000 59.91150  ? 323 LEU A C     1 
ATOM   2584 O O     . LEU A 1 329 ? -22.44426 18.40532  22.69583  1.000 56.82703  ? 323 LEU A O     1 
ATOM   2585 C CB    . LEU A 1 329 ? -24.83545 16.19043  22.80896  1.000 63.28094  ? 323 LEU A CB    1 
ATOM   2586 C CG    . LEU A 1 329 ? -25.37552 17.32319  23.68541  1.000 63.08183  ? 323 LEU A CG    1 
ATOM   2587 C CD1   . LEU A 1 329 ? -25.79672 18.51228  22.83334  1.000 64.37978  ? 323 LEU A CD1   1 
ATOM   2588 C CD2   . LEU A 1 329 ? -26.53421 16.83454  24.54010  1.000 59.69407  ? 323 LEU A CD2   1 
ATOM   2589 N N     . TYR A 1 330 ? -21.63231 16.34747  23.09977  1.000 64.61899  ? 324 TYR A N     1 
ATOM   2590 C CA    . TYR A 1 330 ? -20.44501 16.80834  23.80004  1.000 60.65499  ? 324 TYR A CA    1 
ATOM   2591 C C     . TYR A 1 330 ? -19.22144 16.10970  23.22588  1.000 56.57551  ? 324 TYR A C     1 
ATOM   2592 O O     . TYR A 1 330 ? -19.29302 14.96078  22.78153  1.000 57.91558  ? 324 TYR A O     1 
ATOM   2593 C CB    . TYR A 1 330 ? -20.56184 16.56136  25.30670  1.000 57.53281  ? 324 TYR A CB    1 
ATOM   2594 C CG    . TYR A 1 330 ? -21.77747 17.22591  25.91005  1.000 63.96593  ? 324 TYR A CG    1 
ATOM   2595 C CD1   . TYR A 1 330 ? -21.97867 18.59295  25.77745  1.000 61.56333  ? 324 TYR A CD1   1 
ATOM   2596 C CD2   . TYR A 1 330 ? -22.73136 16.48768  26.59571  1.000 65.06004  ? 324 TYR A CD2   1 
ATOM   2597 C CE1   . TYR A 1 330 ? -23.08996 19.20751  26.31708  1.000 63.38924  ? 324 TYR A CE1   1 
ATOM   2598 C CE2   . TYR A 1 330 ? -23.84706 17.09505  27.14132  1.000 64.66634  ? 324 TYR A CE2   1 
ATOM   2599 C CZ    . TYR A 1 330 ? -24.02075 18.45486  26.99922  1.000 66.78104  ? 324 TYR A CZ    1 
ATOM   2600 O OH    . TYR A 1 330 ? -25.12913 19.06495  27.54053  1.000 73.57434  ? 324 TYR A OH    1 
ATOM   2601 N N     . ALA A 1 331 ? -18.09618 16.82000  23.23275  1.000 54.39650  ? 325 ALA A N     1 
ATOM   2602 C CA    . ALA A 1 331 ? -16.88458 16.38892  22.54631  1.000 53.39333  ? 325 ALA A CA    1 
ATOM   2603 C C     . ALA A 1 331 ? -15.73111 16.31220  23.53441  1.000 59.53783  ? 325 ALA A C     1 
ATOM   2604 O O     . ALA A 1 331 ? -15.36186 17.32285  24.14245  1.000 58.57072  ? 325 ALA A O     1 
ATOM   2605 C CB    . ALA A 1 331 ? -16.53974 17.34544  21.40524  1.000 54.47332  ? 325 ALA A CB    1 
ATOM   2606 N N     . CYS A 1 332 ? -15.15315 15.12016  23.67751  1.000 67.50465  ? 326 CYS A N     1 
ATOM   2607 C CA    . CYS A 1 332 ? -13.98811 14.93971  24.53349  1.000 65.69023  ? 326 CYS A CA    1 
ATOM   2608 C C     . CYS A 1 332 ? -12.72848 15.43772  23.83569  1.000 70.42993  ? 326 CYS A C     1 
ATOM   2609 O O     . CYS A 1 332 ? -12.50184 16.64866  23.74553  1.000 71.24084  ? 326 CYS A O     1 
ATOM   2610 C CB    . CYS A 1 332 ? -13.83518 13.47083  24.93421  1.000 76.03844  ? 326 CYS A CB    1 
ATOM   2611 S SG    . CYS A 1 332 ? -13.47702 12.35054  23.56393  1.000 94.32538  ? 326 CYS A SG    1 
ATOM   2612 N N     . ARG A 1 333 ? -11.90540 14.51279  23.32534  1.000 71.08492  ? 327 ARG A N     1 
ATOM   2613 C CA    . ARG A 1 333 ? -10.63882 14.93991  22.74169  1.000 65.77634  ? 327 ARG A CA    1 
ATOM   2614 C C     . ARG A 1 333 ? -10.73302 14.99864  21.22788  1.000 60.41571  ? 327 ARG A C     1 
ATOM   2615 O O     . ARG A 1 333 ? -11.25590 14.06037  20.60739  1.000 61.45687  ? 327 ARG A O     1 
ATOM   2616 C CB    . ARG A 1 333 ? -9.50971  13.99589  23.14703  1.000 67.79837  ? 327 ARG A CB    1 
ATOM   2617 C CG    . ARG A 1 333 ? -8.12141  14.54838  22.85158  1.000 60.97454  ? 327 ARG A CG    1 
ATOM   2618 C CD    . ARG A 1 333 ? -7.16540  13.46543  22.38361  1.000 62.91667  ? 327 ARG A CD    1 
ATOM   2619 N NE    . ARG A 1 333 ? -7.20851  12.29020  23.24445  1.000 64.44193  ? 327 ARG A NE    1 
ATOM   2620 C CZ    . ARG A 1 333 ? -6.24106  11.38761  23.32832  1.000 67.02287  ? 327 ARG A CZ    1 
ATOM   2621 N NH1   . ARG A 1 333 ? -5.13283  11.49369  22.61371  1.000 64.85003  ? 327 ARG A NH1   1 
ATOM   2622 N NH2   . ARG A 1 333 ? -6.38777  10.35445  24.15260  1.000 78.70592  ? 327 ARG A NH2   1 
ATOM   2623 N N     . PRO A 1 334 ? -10.24544 16.06656  20.60352  1.000 55.38766  ? 328 PRO A N     1 
ATOM   2624 C CA    . PRO A 1 334 ? -10.14432 16.08141  19.14498  1.000 49.87731  ? 328 PRO A CA    1 
ATOM   2625 C C     . PRO A 1 334 ? -8.83836  15.45806  18.68291  1.000 51.63664  ? 328 PRO A C     1 
ATOM   2626 O O     . PRO A 1 334 ? -7.83908  15.42777  19.40604  1.000 46.47466  ? 328 PRO A O     1 
ATOM   2627 C CB    . PRO A 1 334 ? -10.19648 17.57500  18.79630  1.000 49.35616  ? 328 PRO A CB    1 
ATOM   2628 C CG    . PRO A 1 334 ? -9.94131  18.32149  20.09204  1.000 55.13612  ? 328 PRO A CG    1 
ATOM   2629 C CD    . PRO A 1 334 ? -9.77673  17.32656  21.20448  1.000 55.97564  ? 328 PRO A CD    1 
ATOM   2630 N N     . LEU A 1 335 ? -8.86309  14.94796  17.45629  1.000 41.93697  ? 329 LEU A N     1 
ATOM   2631 C CA    . LEU A 1 335 ? -7.67319  14.37292  16.85487  1.000 39.31122  ? 329 LEU A CA    1 
ATOM   2632 C C     . LEU A 1 335 ? -6.79650  15.48390  16.28065  1.000 37.29428  ? 329 LEU A C     1 
ATOM   2633 O O     . LEU A 1 335 ? -7.14983  16.66597  16.29892  1.000 35.24671  ? 329 LEU A O     1 
ATOM   2634 C CB    . LEU A 1 335 ? -8.06366  13.36016  15.78131  1.000 39.42792  ? 329 LEU A CB    1 
ATOM   2635 C CG    . LEU A 1 335 ? -9.22557  12.43094  16.14049  1.000 37.80826  ? 329 LEU A CG    1 
ATOM   2636 C CD1   . LEU A 1 335 ? -9.64874  11.60836  14.93499  1.000 34.37846  ? 329 LEU A CD1   1 
ATOM   2637 C CD2   . LEU A 1 335 ? -8.85045  11.52582  17.30459  1.000 35.59184  ? 329 LEU A CD2   1 
ATOM   2638 N N     . CYS A 1 336 ? -5.63033  15.10138  15.77091  1.000 35.18666  ? 330 CYS A N     1 
ATOM   2639 C CA    . CYS A 1 336 ? -4.73051  16.01373  15.08076  1.000 35.53533  ? 330 CYS A CA    1 
ATOM   2640 C C     . CYS A 1 336 ? -4.46332  15.47980  13.68221  1.000 31.83392  ? 330 CYS A C     1 
ATOM   2641 O O     . CYS A 1 336 ? -4.33348  14.26701  13.48799  1.000 38.12481  ? 330 CYS A O     1 
ATOM   2642 C CB    . CYS A 1 336 ? -3.41142  16.18491  15.84273  1.000 39.42450  ? 330 CYS A CB    1 
ATOM   2643 S SG    . CYS A 1 336 ? -3.60394  16.39927  17.62615  1.000 51.98723  ? 330 CYS A SG    1 
ATOM   2644 N N     . ASP A 1 337 ? -4.38307  16.38432  12.70864  1.000 24.78712  ? 331 ASP A N     1 
ATOM   2645 C CA    . ASP A 1 337 ? -4.22730  15.98521  11.31915  1.000 29.03758  ? 331 ASP A CA    1 
ATOM   2646 C C     . ASP A 1 337 ? -3.32891  16.97139  10.58847  1.000 30.38012  ? 331 ASP A C     1 
ATOM   2647 O O     . ASP A 1 337 ? -3.07627  18.08450  11.05599  1.000 28.20511  ? 331 ASP A O     1 
ATOM   2648 C CB    . ASP A 1 337 ? -5.58411  15.88062  10.61211  1.000 30.25496  ? 331 ASP A CB    1 
ATOM   2649 C CG    . ASP A 1 337 ? -6.22075  17.23333  10.35866  1.000 29.88257  ? 331 ASP A CG    1 
ATOM   2650 O OD1   . ASP A 1 337 ? -5.92741  17.84616  9.31162   1.000 31.38627  ? 331 ASP A OD1   1 
ATOM   2651 O OD2   . ASP A 1 337 ? -7.02515  17.67965  11.20154  1.000 32.58537  ? 331 ASP A OD2   1 
ATOM   2652 N N     . SER A 1 338 ? -2.85070  16.54037  9.42420   1.000 28.07251  ? 332 SER A N     1 
ATOM   2653 C CA    . SER A 1 338 ? -2.00545  17.34184  8.54923   1.000 31.89384  ? 332 SER A CA    1 
ATOM   2654 C C     . SER A 1 338 ? -2.68675  17.57526  7.20550   1.000 30.26599  ? 332 SER A C     1 
ATOM   2655 O O     . SER A 1 338 ? -2.04877  17.55436  6.15068   1.000 32.45726  ? 332 SER A O     1 
ATOM   2656 C CB    . SER A 1 338 ? -0.64199  16.68156  8.35561   1.000 33.12108  ? 332 SER A CB    1 
ATOM   2657 O OG    . SER A 1 338 ? 0.01974   16.49993  9.59687   1.000 33.11068  ? 332 SER A OG    1 
ATOM   2658 N N     . GLY A 1 339 ? -3.99933  17.79816  7.23227   1.000 29.88259  ? 333 GLY A N     1 
ATOM   2659 C CA    . GLY A 1 339 ? -4.75624  18.04633  6.02005   1.000 31.11796  ? 333 GLY A CA    1 
ATOM   2660 C C     . GLY A 1 339 ? -5.86081  17.03598  5.78214   1.000 28.50309  ? 333 GLY A C     1 
ATOM   2661 O O     . GLY A 1 339 ? -6.10479  16.63063  4.64224   1.000 33.04678  ? 333 GLY A O     1 
ATOM   2662 N N     . TYR A 1 340 ? -6.54665  16.63306  6.85385   1.000 29.93132  ? 334 TYR A N     1 
ATOM   2663 C CA    . TYR A 1 340 ? -7.54982  15.57655  6.74737   1.000 29.31598  ? 334 TYR A CA    1 
ATOM   2664 C C     . TYR A 1 340 ? -8.79514  16.05891  6.01291   1.000 30.77744  ? 334 TYR A C     1 
ATOM   2665 O O     . TYR A 1 340 ? -9.26759  15.40394  5.07703   1.000 31.82277  ? 334 TYR A O     1 
ATOM   2666 C CB    . TYR A 1 340 ? -7.91302  15.06357  8.14119   1.000 27.89610  ? 334 TYR A CB    1 
ATOM   2667 C CG    . TYR A 1 340 ? -9.02907  14.04288  8.16629   1.000 29.45454  ? 334 TYR A CG    1 
ATOM   2668 C CD1   . TYR A 1 340 ? -8.86410  12.78686  7.59691   1.000 30.12174  ? 334 TYR A CD1   1 
ATOM   2669 C CD2   . TYR A 1 340 ? -10.24643 14.33438  8.76750   1.000 29.30367  ? 334 TYR A CD2   1 
ATOM   2670 C CE1   . TYR A 1 340 ? -9.88278  11.85137  7.62168   1.000 22.44209  ? 334 TYR A CE1   1 
ATOM   2671 C CE2   . TYR A 1 340 ? -11.26994 13.40618  8.79705   1.000 25.51041  ? 334 TYR A CE2   1 
ATOM   2672 C CZ    . TYR A 1 340 ? -11.08269 12.16691  8.22346   1.000 27.14848  ? 334 TYR A CZ    1 
ATOM   2673 O OH    . TYR A 1 340 ? -12.10102 11.24162  8.25311   1.000 27.63176  ? 334 TYR A OH    1 
ATOM   2674 N N     . TYR A 1 341 ? -9.35075  17.19855  6.43114   1.000 29.16014  ? 335 TYR A N     1 
ATOM   2675 C CA    . TYR A 1 341 ? -10.59548 17.66866  5.83220   1.000 29.33559  ? 335 TYR A CA    1 
ATOM   2676 C C     . TYR A 1 341 ? -10.38977 18.13864  4.39869   1.000 31.36018  ? 335 TYR A C     1 
ATOM   2677 O O     . TYR A 1 341 ? -11.32030 18.06954  3.58737   1.000 33.56470  ? 335 TYR A O     1 
ATOM   2678 C CB    . TYR A 1 341 ? -11.19862 18.78216  6.68737   1.000 33.99124  ? 335 TYR A CB    1 
ATOM   2679 C CG    . TYR A 1 341 ? -11.66415 18.30056  8.04216   1.000 30.90292  ? 335 TYR A CG    1 
ATOM   2680 C CD1   . TYR A 1 341 ? -12.60808 17.28829  8.15064   1.000 27.49045  ? 335 TYR A CD1   1 
ATOM   2681 C CD2   . TYR A 1 341 ? -11.15269 18.84825  9.21125   1.000 26.16998  ? 335 TYR A CD2   1 
ATOM   2682 C CE1   . TYR A 1 341 ? -13.03552 16.83818  9.38364   1.000 27.56370  ? 335 TYR A CE1   1 
ATOM   2683 C CE2   . TYR A 1 341 ? -11.57478 18.40440  10.45187  1.000 28.86535  ? 335 TYR A CE2   1 
ATOM   2684 C CZ    . TYR A 1 341 ? -12.51727 17.39856  10.53080  1.000 28.74503  ? 335 TYR A CZ    1 
ATOM   2685 O OH    . TYR A 1 341 ? -12.94378 16.94980  11.75971  1.000 29.81737  ? 335 TYR A OH    1 
ATOM   2686 N N     . GLU A 1 342 ? -9.18311  18.60408  4.06510   1.000 29.35554  ? 336 GLU A N     1 
ATOM   2687 C CA    . GLU A 1 342 ? -8.89168  18.98487  2.68695   1.000 30.59498  ? 336 GLU A CA    1 
ATOM   2688 C C     . GLU A 1 342 ? -8.95306  17.78572  1.74897   1.000 32.24850  ? 336 GLU A C     1 
ATOM   2689 O O     . GLU A 1 342 ? -9.18257  17.94818  0.54449   1.000 31.49146  ? 336 GLU A O     1 
ATOM   2690 C CB    . GLU A 1 342 ? -7.51492  19.64470  2.60811   1.000 35.77461  ? 336 GLU A CB    1 
ATOM   2691 C CG    . GLU A 1 342 ? -7.44857  21.04660  3.19880   1.000 41.27904  ? 336 GLU A CG    1 
ATOM   2692 C CD    . GLU A 1 342 ? -7.23592  21.04612  4.69895   1.000 40.02393  ? 336 GLU A CD    1 
ATOM   2693 O OE1   . GLU A 1 342 ? -7.22623  19.95397  5.30278   1.000 35.50077  ? 336 GLU A OE1   1 
ATOM   2694 O OE2   . GLU A 1 342 ? -7.07379  22.14038  5.27599   1.000 44.57183  ? 336 GLU A OE2   1 
ATOM   2695 N N     . ILE A 1 343 ? -8.75223  16.57894  2.28307   1.000 28.87393  ? 337 ILE A N     1 
ATOM   2696 C CA    . ILE A 1 343 ? -8.72907  15.37489  1.45525   1.000 30.96781  ? 337 ILE A CA    1 
ATOM   2697 C C     . ILE A 1 343 ? -10.07061 15.16770  0.76307   1.000 29.50324  ? 337 ILE A C     1 
ATOM   2698 O O     . ILE A 1 343 ? -10.13108 14.74274  -0.39766  1.000 27.51131  ? 337 ILE A O     1 
ATOM   2699 C CB    . ILE A 1 343 ? -8.34012  14.15480  2.31403   1.000 30.13939  ? 337 ILE A CB    1 
ATOM   2700 C CG1   . ILE A 1 343 ? -6.83977  14.17090  2.62317   1.000 36.24958  ? 337 ILE A CG1   1 
ATOM   2701 C CG2   . ILE A 1 343 ? -8.76713  12.85272  1.65376   1.000 31.35171  ? 337 ILE A CG2   1 
ATOM   2702 C CD1   . ILE A 1 343 ? -5.96870  14.40821  1.40969   1.000 34.70132  ? 337 ILE A CD1   1 
ATOM   2703 N N     . PHE A 1 344 ? -11.16352 15.47388  1.45444   1.000 28.41278  ? 338 PHE A N     1 
ATOM   2704 C CA    . PHE A 1 344 ? -12.49468 15.16740  0.95015   1.000 27.71118  ? 338 PHE A CA    1 
ATOM   2705 C C     . PHE A 1 344 ? -12.96863 16.13395  -0.12785  1.000 33.20460  ? 338 PHE A C     1 
ATOM   2706 O O     . PHE A 1 344 ? -14.09267 15.98222  -0.61965  1.000 28.42114  ? 338 PHE A O     1 
ATOM   2707 C CB    . PHE A 1 344 ? -13.47989 15.12758  2.11764   1.000 24.93818  ? 338 PHE A CB    1 
ATOM   2708 C CG    . PHE A 1 344 ? -13.13856 14.08609  3.14272   1.000 26.90636  ? 338 PHE A CG    1 
ATOM   2709 C CD1   . PHE A 1 344 ? -13.56712 12.77789  2.98855   1.000 24.33426  ? 338 PHE A CD1   1 
ATOM   2710 C CD2   . PHE A 1 344 ? -12.36197 14.40672  4.24357   1.000 26.13776  ? 338 PHE A CD2   1 
ATOM   2711 C CE1   . PHE A 1 344 ? -13.24464 11.81416  3.92237   1.000 25.40992  ? 338 PHE A CE1   1 
ATOM   2712 C CE2   . PHE A 1 344 ? -12.03460 13.44595  5.18111   1.000 27.82157  ? 338 PHE A CE2   1 
ATOM   2713 C CZ    . PHE A 1 344 ? -12.47724 12.14873  5.02123   1.000 24.92343  ? 338 PHE A CZ    1 
ATOM   2714 N N     . ASN A 1 345 ? -12.14755 17.11181  -0.50785  1.000 28.24412  ? 339 ASN A N     1 
ATOM   2715 C CA    . ASN A 1 345 ? -12.40475 17.92224  -1.68952  1.000 34.11131  ? 339 ASN A CA    1 
ATOM   2716 C C     . ASN A 1 345 ? -11.87829 17.28062  -2.96565  1.000 32.96715  ? 339 ASN A C     1 
ATOM   2717 O O     . ASN A 1 345 ? -12.19586 17.76036  -4.05908  1.000 31.59962  ? 339 ASN A O     1 
ATOM   2718 C CB    . ASN A 1 345 ? -11.77614 19.31210  -1.53301  1.000 33.23072  ? 339 ASN A CB    1 
ATOM   2719 C CG    . ASN A 1 345 ? -12.50714 20.17489  -0.52657  1.000 32.63007  ? 339 ASN A CG    1 
ATOM   2720 O OD1   . ASN A 1 345 ? -13.72149 20.06440  -0.36257  1.000 34.22205  ? 339 ASN A OD1   1 
ATOM   2721 N ND2   . ASN A 1 345 ? -11.76862 21.04478  0.15246   1.000 30.34124  ? 339 ASN A ND2   1 
ATOM   2722 N N     . ARG A 1 346 ? -11.08812 16.21620  -2.85171  1.000 34.53377  ? 340 ARG A N     1 
ATOM   2723 C CA    . ARG A 1 346 ? -10.47868 15.59589  -4.01796  1.000 34.91614  ? 340 ARG A CA    1 
ATOM   2724 C C     . ARG A 1 346 ? -11.50993 14.81186  -4.82101  1.000 35.30827  ? 340 ARG A C     1 
ATOM   2725 O O     . ARG A 1 346 ? -12.51946 14.33901  -4.29153  1.000 34.27509  ? 340 ARG A O     1 
ATOM   2726 C CB    . ARG A 1 346 ? -9.34023  14.66786  -3.59435  1.000 34.81876  ? 340 ARG A CB    1 
ATOM   2727 C CG    . ARG A 1 346 ? -8.20997  15.35948  -2.85058  1.000 34.96082  ? 340 ARG A CG    1 
ATOM   2728 C CD    . ARG A 1 346 ? -7.14471  14.35980  -2.42992  1.000 32.60220  ? 340 ARG A CD    1 
ATOM   2729 N NE    . ARG A 1 346 ? -6.68549  13.55572  -3.55605  1.000 35.86168  ? 340 ARG A NE    1 
ATOM   2730 C CZ    . ARG A 1 346 ? -5.60554  13.82658  -4.27595  1.000 33.76112  ? 340 ARG A CZ    1 
ATOM   2731 N NH1   . ARG A 1 346 ? -4.83915  14.87076  -4.00562  1.000 26.40306  ? 340 ARG A NH1   1 
ATOM   2732 N NH2   . ARG A 1 346 ? -5.28616  13.02988  -5.29193  1.000 31.32962  ? 340 ARG A NH2   1 
ATOM   2733 N N     . ASP A 1 347 ? -11.23517 14.66842  -6.11943  1.000 35.10793  ? 341 ASP A N     1 
ATOM   2734 C CA    . ASP A 1 347 ? -12.12875 13.92837  -7.00164  1.000 36.81402  ? 341 ASP A CA    1 
ATOM   2735 C C     . ASP A 1 347 ? -12.03959 12.42211  -6.79257  1.000 34.17872  ? 341 ASP A C     1 
ATOM   2736 O O     . ASP A 1 347 ? -12.94178 11.69645  -7.22423  1.000 34.22525  ? 341 ASP A O     1 
ATOM   2737 C CB    . ASP A 1 347 ? -11.81821 14.26230  -8.46239  1.000 39.39656  ? 341 ASP A CB    1 
ATOM   2738 C CG    . ASP A 1 347 ? -12.42329 15.58074  -8.90311  1.000 51.12085  ? 341 ASP A CG    1 
ATOM   2739 O OD1   . ASP A 1 347 ? -13.23986 16.14815  -8.14837  1.000 51.20242  ? 341 ASP A OD1   1 
ATOM   2740 O OD2   . ASP A 1 347 ? -12.07897 16.05174  -10.00675 1.000 59.85715  ? 341 ASP A OD2   1 
ATOM   2741 N N     . ASN A 1 348 ? -10.98124 11.93569  -6.14175  1.000 31.73010  ? 342 ASN A N     1 
ATOM   2742 C CA    . ASN A 1 348 ? -10.75313 10.50499  -5.97882  1.000 28.80367  ? 342 ASN A CA    1 
ATOM   2743 C C     . ASN A 1 348 ? -11.02876 10.02240  -4.55781  1.000 30.75009  ? 342 ASN A C     1 
ATOM   2744 O O     . ASN A 1 348 ? -10.51825 8.97242   -4.15490  1.000 29.85094  ? 342 ASN A O     1 
ATOM   2745 C CB    . ASN A 1 348 ? -9.32351  10.14896  -6.39178  1.000 29.27186  ? 342 ASN A CB    1 
ATOM   2746 C CG    . ASN A 1 348 ? -8.28742  10.63833  -5.39664  1.000 32.95570  ? 342 ASN A CG    1 
ATOM   2747 O OD1   . ASN A 1 348 ? -8.46476  11.67465  -4.75648  1.000 33.38357  ? 342 ASN A OD1   1 
ATOM   2748 N ND2   . ASN A 1 348 ? -7.19671  9.89093   -5.26171  1.000 35.23512  ? 342 ASN A ND2   1 
ATOM   2749 N N     . VAL A 1 349 ? -11.82935 10.75964  -3.79163  1.000 26.94961  ? 343 VAL A N     1 
ATOM   2750 C CA    . VAL A 1 349 ? -12.14552 10.40317  -2.41365  1.000 25.22811  ? 343 VAL A CA    1 
ATOM   2751 C C     . VAL A 1 349 ? -13.65808 10.35579  -2.25493  1.000 34.88109  ? 343 VAL A C     1 
ATOM   2752 O O     . VAL A 1 349 ? -14.35456 11.31603  -2.60367  1.000 27.74203  ? 343 VAL A O     1 
ATOM   2753 C CB    . VAL A 1 349 ? -11.53041 11.39370  -1.40674  1.000 28.53560  ? 343 VAL A CB    1 
ATOM   2754 C CG1   . VAL A 1 349 ? -11.97486 11.05357  0.00771   1.000 27.09629  ? 343 VAL A CG1   1 
ATOM   2755 C CG2   . VAL A 1 349 ? -10.01324 11.38126  -1.50827  1.000 27.15257  ? 343 VAL A CG2   1 
ATOM   2756 N N     . SER A 1 350 ? -14.16095 9.24231   -1.72654  1.000 29.99425  ? 344 SER A N     1 
ATOM   2757 C CA    . SER A 1 350 ? -15.57547 9.06896   -1.42776  1.000 33.03137  ? 344 SER A CA    1 
ATOM   2758 C C     . SER A 1 350 ? -15.73354 8.77389   0.05606   1.000 31.34753  ? 344 SER A C     1 
ATOM   2759 O O     . SER A 1 350 ? -15.03205 7.91416   0.59965   1.000 30.60869  ? 344 SER A O     1 
ATOM   2760 C CB    . SER A 1 350 ? -16.18568 7.93766   -2.26114  1.000 32.93077  ? 344 SER A CB    1 
ATOM   2761 O OG    . SER A 1 350 ? -16.10548 8.22090   -3.64691  1.000 37.90771  ? 344 SER A OG    1 
ATOM   2762 N N     . LEU A 1 351 ? -16.64607 9.48874   0.70710   1.000 28.16110  ? 345 LEU A N     1 
ATOM   2763 C CA    . LEU A 1 351 ? -16.92900 9.29872   2.12362   1.000 30.32447  ? 345 LEU A CA    1 
ATOM   2764 C C     . LEU A 1 351 ? -18.24428 8.54407   2.26852   1.000 35.25137  ? 345 LEU A C     1 
ATOM   2765 O O     . LEU A 1 351 ? -19.27680 8.98225   1.74923   1.000 32.30518  ? 345 LEU A O     1 
ATOM   2766 C CB    . LEU A 1 351 ? -16.99518 10.63884  2.85537   1.000 26.81078  ? 345 LEU A CB    1 
ATOM   2767 C CG    . LEU A 1 351 ? -17.40730 10.56495  4.32725   1.000 31.82974  ? 345 LEU A CG    1 
ATOM   2768 C CD1   . LEU A 1 351 ? -16.41897 9.72590   5.12258   1.000 28.53340  ? 345 LEU A CD1   1 
ATOM   2769 C CD2   . LEU A 1 351 ? -17.53366 11.95623  4.92375   1.000 28.42781  ? 345 LEU A CD2   1 
ATOM   2770 N N     . GLU A 1 352 ? -18.20450 7.41718   2.97357   1.000 34.57013  ? 346 GLU A N     1 
ATOM   2771 C CA    . GLU A 1 352 ? -19.37431 6.57274   3.18791   1.000 36.68408  ? 346 GLU A CA    1 
ATOM   2772 C C     . GLU A 1 352 ? -19.73881 6.61378   4.66673   1.000 35.14808  ? 346 GLU A C     1 
ATOM   2773 O O     . GLU A 1 352 ? -18.96974 6.14831   5.51454   1.000 33.36255  ? 346 GLU A O     1 
ATOM   2774 C CB    . GLU A 1 352 ? -19.10461 5.14129   2.72831   1.000 35.82324  ? 346 GLU A CB    1 
ATOM   2775 C CG    . GLU A 1 352 ? -19.30009 4.91961   1.23848   1.000 40.33799  ? 346 GLU A CG    1 
ATOM   2776 C CD    . GLU A 1 352 ? -20.76231 4.90136   0.84040   1.000 43.69399  ? 346 GLU A CD    1 
ATOM   2777 O OE1   . GLU A 1 352 ? -21.59287 4.43027   1.64468   1.000 44.96754  ? 346 GLU A OE1   1 
ATOM   2778 O OE2   . GLU A 1 352 ? -21.08176 5.35633   -0.27703  1.000 42.52477  ? 346 GLU A OE2   1 
ATOM   2779 N N     . ASP A 1 353 ? -20.90442 7.17677   4.97384   1.000 35.33211  ? 347 ASP A N     1 
ATOM   2780 C CA    . ASP A 1 353 ? -21.43456 7.16008   6.33537   1.000 32.33305  ? 347 ASP A CA    1 
ATOM   2781 C C     . ASP A 1 353 ? -21.90886 5.74619   6.63712   1.000 37.31618  ? 347 ASP A C     1 
ATOM   2782 O O     . ASP A 1 353 ? -23.00542 5.34562   6.24043   1.000 40.44803  ? 347 ASP A O     1 
ATOM   2783 C CB    . ASP A 1 353 ? -22.56723 8.17027   6.48278   1.000 39.18186  ? 347 ASP A CB    1 
ATOM   2784 C CG    . ASP A 1 353 ? -23.07483 8.28525   7.91261   1.000 40.98675  ? 347 ASP A CG    1 
ATOM   2785 O OD1   . ASP A 1 353 ? -22.55828 7.57678   8.80240   1.000 42.49727  ? 347 ASP A OD1   1 
ATOM   2786 O OD2   . ASP A 1 353 ? -23.99767 9.09240   8.14698   1.000 53.38359  ? 347 ASP A OD2   1 
ATOM   2787 N N     . VAL A 1 354 ? -21.07577 4.97669   7.34564   1.000 34.96750  ? 348 VAL A N     1 
ATOM   2788 C CA    . VAL A 1 354 ? -21.38505 3.57763   7.61400   1.000 38.66415  ? 348 VAL A CA    1 
ATOM   2789 C C     . VAL A 1 354 ? -22.24707 3.40008   8.85858   1.000 43.42724  ? 348 VAL A C     1 
ATOM   2790 O O     . VAL A 1 354 ? -22.60480 2.26463   9.20109   1.000 46.04770  ? 348 VAL A O     1 
ATOM   2791 C CB    . VAL A 1 354 ? -20.07328 2.76320   7.68437   1.000 40.39460  ? 348 VAL A CB    1 
ATOM   2792 C CG1   . VAL A 1 354 ? -19.60160 2.57103   9.11471   1.000 35.65376  ? 348 VAL A CG1   1 
ATOM   2793 C CG2   . VAL A 1 354 ? -20.24831 1.43224   6.99085   1.000 44.34002  ? 348 VAL A CG2   1 
ATOM   2794 N N     . LYS A 1 355 ? -22.61352 4.48774   9.53797   1.000 47.01215  ? 349 LYS A N     1 
ATOM   2795 C CA    . LYS A 1 355 ? -23.63216 4.37954   10.57594  1.000 45.24519  ? 349 LYS A CA    1 
ATOM   2796 C C     . LYS A 1 355 ? -25.02840 4.33682   9.96790   1.000 47.79191  ? 349 LYS A C     1 
ATOM   2797 O O     . LYS A 1 355 ? -25.86431 3.52431   10.37924  1.000 45.71180  ? 349 LYS A O     1 
ATOM   2798 C CB    . LYS A 1 355 ? -23.51699 5.54040   11.56413  1.000 50.25725  ? 349 LYS A CB    1 
ATOM   2799 C CG    . LYS A 1 355 ? -24.49873 5.45239   12.72431  1.000 49.05669  ? 349 LYS A CG    1 
ATOM   2800 C CD    . LYS A 1 355 ? -24.14927 6.43200   13.83199  1.000 56.84000  ? 349 LYS A CD    1 
ATOM   2801 C CE    . LYS A 1 355 ? -24.60236 7.84092   13.48608  1.000 56.13619  ? 349 LYS A CE    1 
ATOM   2802 N NZ    . LYS A 1 355 ? -25.00858 8.60353   14.69884  1.000 62.67030  ? 349 LYS A NZ    1 
ATOM   2803 N N     . ALA A 1 356 ? -25.29317 5.19897   8.98393   1.000 43.21892  ? 350 ALA A N     1 
ATOM   2804 C CA    . ALA A 1 356 ? -26.57815 5.18261   8.29620   1.000 46.20861  ? 350 ALA A CA    1 
ATOM   2805 C C     . ALA A 1 356 ? -26.61524 4.14834   7.17846   1.000 46.73356  ? 350 ALA A C     1 
ATOM   2806 O O     . ALA A 1 356 ? -27.69640 3.66823   6.82019   1.000 45.26585  ? 350 ALA A O     1 
ATOM   2807 C CB    . ALA A 1 356 ? -26.89180 6.57051   7.73531   1.000 47.32156  ? 350 ALA A CB    1 
ATOM   2808 N N     . ASN A 1 357 ? -25.45758 3.79585   6.62091   1.000 38.15845  ? 351 ASN A N     1 
ATOM   2809 C CA    . ASN A 1 357 ? -25.35134 2.82633   5.53021   1.000 36.61937  ? 351 ASN A CA    1 
ATOM   2810 C C     . ASN A 1 357 ? -24.28313 1.81148   5.91616   1.000 40.59724  ? 351 ASN A C     1 
ATOM   2811 O O     . ASN A 1 357 ? -23.14848 1.86453   5.42244   1.000 40.37568  ? 351 ASN A O     1 
ATOM   2812 C CB    . ASN A 1 357 ? -25.02664 3.52401   4.20793   1.000 36.86784  ? 351 ASN A CB    1 
ATOM   2813 C CG    . ASN A 1 357 ? -24.94623 2.56189   3.03986   1.000 41.82123  ? 351 ASN A CG    1 
ATOM   2814 O OD1   . ASN A 1 357 ? -25.66658 1.56514   2.98811   1.000 38.91781  ? 351 ASN A OD1   1 
ATOM   2815 N ND2   . ASN A 1 357 ? -24.07042 2.86304   2.08768   1.000 38.14324  ? 351 ASN A ND2   1 
ATOM   2816 N N     . PRO A 1 358 ? -24.61444 0.86801   6.79509   1.000 38.87203  ? 352 PRO A N     1 
ATOM   2817 C CA    . PRO A 1 358 ? -23.58501 -0.00533  7.36999   1.000 38.69850  ? 352 PRO A CA    1 
ATOM   2818 C C     . PRO A 1 358 ? -23.04308 -1.01376  6.36964   1.000 39.23444  ? 352 PRO A C     1 
ATOM   2819 O O     . PRO A 1 358 ? -23.68888 -1.37507  5.38396   1.000 35.83292  ? 352 PRO A O     1 
ATOM   2820 C CB    . PRO A 1 358 ? -24.31160 -0.71417  8.52182   1.000 39.12099  ? 352 PRO A CB    1 
ATOM   2821 C CG    . PRO A 1 358 ? -25.62437 0.00203   8.68675   1.000 37.73547  ? 352 PRO A CG    1 
ATOM   2822 C CD    . PRO A 1 358 ? -25.94526 0.60993   7.36555   1.000 41.00382  ? 352 PRO A CD    1 
ATOM   2823 N N     . ILE A 1 359 ? -21.82178 -1.46746  6.64844   1.000 35.91351  ? 353 ILE A N     1 
ATOM   2824 C CA    . ILE A 1 359 ? -21.23318 -2.57464  5.90470   1.000 37.35481  ? 353 ILE A CA    1 
ATOM   2825 C C     . ILE A 1 359 ? -21.90269 -3.86498  6.35553   1.000 36.74439  ? 353 ILE A C     1 
ATOM   2826 O O     . ILE A 1 359 ? -21.90208 -4.19934  7.54591   1.000 36.53748  ? 353 ILE A O     1 
ATOM   2827 C CB    . ILE A 1 359 ? -19.71440 -2.63670  6.11303   1.000 37.76600  ? 353 ILE A CB    1 
ATOM   2828 C CG1   . ILE A 1 359 ? -19.02609 -1.45050  5.43666   1.000 35.25277  ? 353 ILE A CG1   1 
ATOM   2829 C CG2   . ILE A 1 359 ? -19.15564 -3.94731  5.58075   1.000 35.53078  ? 353 ILE A CG2   1 
ATOM   2830 C CD1   . ILE A 1 359 ? -17.67402 -1.11398  6.02823   1.000 34.05742  ? 353 ILE A CD1   1 
ATOM   2831 N N     . VAL A 1 360 ? -22.48435 -4.59143  5.40751   1.000 38.75444  ? 354 VAL A N     1 
ATOM   2832 C CA    . VAL A 1 360 ? -23.17025 -5.83793  5.71287   1.000 38.52892  ? 354 VAL A CA    1 
ATOM   2833 C C     . VAL A 1 360 ? -22.39006 -7.06372  5.25830   1.000 39.91718  ? 354 VAL A C     1 
ATOM   2834 O O     . VAL A 1 360 ? -22.69247 -8.17391  5.72370   1.000 44.63224  ? 354 VAL A O     1 
ATOM   2835 C CB    . VAL A 1 360 ? -24.58671 -5.85318  5.10407   1.000 40.89628  ? 354 VAL A CB    1 
ATOM   2836 C CG1   . VAL A 1 360 ? -25.44888 -4.78039  5.74874   1.000 36.14973  ? 354 VAL A CG1   1 
ATOM   2837 C CG2   . VAL A 1 360 ? -24.51052 -5.64328  3.60483   1.000 38.84550  ? 354 VAL A CG2   1 
ATOM   2838 N N     . GLU A 1 361 ? -21.39691 -6.90363  4.38784   1.000 36.99104  ? 355 GLU A N     1 
ATOM   2839 C CA    . GLU A 1 361 ? -20.66106 -8.01770  3.80864   1.000 37.65654  ? 355 GLU A CA    1 
ATOM   2840 C C     . GLU A 1 361 ? -19.51355 -7.45945  2.98436   1.000 39.78744  ? 355 GLU A C     1 
ATOM   2841 O O     . GLU A 1 361 ? -19.60613 -6.35342  2.44575   1.000 41.76667  ? 355 GLU A O     1 
ATOM   2842 C CB    . GLU A 1 361 ? -21.56814 -8.88683  2.92593   1.000 38.37788  ? 355 GLU A CB    1 
ATOM   2843 C CG    . GLU A 1 361 ? -21.01393 -10.26155 2.59755   1.000 46.20846  ? 355 GLU A CG    1 
ATOM   2844 C CD    . GLU A 1 361 ? -21.67844 -10.87362 1.37903   1.000 53.27207  ? 355 GLU A CD    1 
ATOM   2845 O OE1   . GLU A 1 361 ? -22.49145 -10.17888 0.73257   1.000 51.00761  ? 355 GLU A OE1   1 
ATOM   2846 O OE2   . GLU A 1 361 ? -21.38962 -12.04795 1.06769   1.000 51.99245  ? 355 GLU A OE2   1 
ATOM   2847 N N     . ILE A 1 362 ? -18.42793 -8.22357  2.90483   1.000 40.18634  ? 356 ILE A N     1 
ATOM   2848 C CA    . ILE A 1 362 ? -17.37329 -7.97357  1.93190   1.000 40.54429  ? 356 ILE A CA    1 
ATOM   2849 C C     . ILE A 1 362 ? -17.07145 -9.28871  1.22701   1.000 39.14342  ? 356 ILE A C     1 
ATOM   2850 O O     . ILE A 1 362 ? -17.10613 -10.36044 1.84306   1.000 38.99711  ? 356 ILE A O     1 
ATOM   2851 C CB    . ILE A 1 362 ? -16.10042 -7.36138  2.56688   1.000 48.12348  ? 356 ILE A CB    1 
ATOM   2852 C CG1   . ILE A 1 362 ? -15.21267 -8.41765  3.22174   1.000 43.93398  ? 356 ILE A CG1   1 
ATOM   2853 C CG2   . ILE A 1 362 ? -16.46260 -6.29242  3.59103   1.000 45.60451  ? 356 ILE A CG2   1 
ATOM   2854 C CD1   . ILE A 1 362 ? -13.88171 -7.85803  3.69151   1.000 53.03959  ? 356 ILE A CD1   1 
ATOM   2855 N N     . LYS A 1 363 ? -16.81858 -9.21024  -0.07638  1.000 35.56732  ? 357 LYS A N     1 
ATOM   2856 C CA    . LYS A 1 363 ? -16.60883 -10.38487 -0.90021  1.000 38.11775  ? 357 LYS A CA    1 
ATOM   2857 C C     . LYS A 1 363 ? -15.16376 -10.40708 -1.40358  1.000 37.02150  ? 357 LYS A C     1 
ATOM   2858 O O     . LYS A 1 363 ? -14.29581 -9.70303  -0.86716  1.000 39.49802  ? 357 LYS A O     1 
ATOM   2859 C CB    . LYS A 1 363 ? -17.64409 -10.39305 -2.02910  1.000 37.24635  ? 357 LYS A CB    1 
ATOM   2860 C CG    . LYS A 1 363 ? -19.08416 -10.41782 -1.53397  1.000 43.52984  ? 357 LYS A CG    1 
ATOM   2861 C CD    . LYS A 1 363 ? -20.02029 -9.69227  -2.48674  1.000 45.94069  ? 357 LYS A CD    1 
ATOM   2862 C CE    . LYS A 1 363 ? -20.40085 -10.56982 -3.66663  1.000 56.89291  ? 357 LYS A CE    1 
ATOM   2863 N NZ    . LYS A 1 363 ? -20.90033 -11.90423 -3.23198  1.000 57.85793  ? 357 LYS A NZ    1 
ATOM   2864 N N     . GLU A 1 364 ? -14.90753 -11.21222 -2.43735  1.000 39.36939  ? 358 GLU A N     1 
ATOM   2865 C CA    . GLU A 1 364 ? -13.54426 -11.39484 -2.92157  1.000 39.15085  ? 358 GLU A CA    1 
ATOM   2866 C C     . GLU A 1 364 ? -12.95238 -10.12259 -3.51361  1.000 33.55534  ? 358 GLU A C     1 
ATOM   2867 O O     . GLU A 1 364 ? -11.72538 -10.01888 -3.61768  1.000 36.03351  ? 358 GLU A O     1 
ATOM   2868 C CB    . GLU A 1 364 ? -13.49934 -12.51542 -3.96298  1.000 37.86190  ? 358 GLU A CB    1 
ATOM   2869 C CG    . GLU A 1 364 ? -14.25946 -12.21022 -5.24485  1.000 41.99564  ? 358 GLU A CG    1 
ATOM   2870 C CD    . GLU A 1 364 ? -13.72430 -12.97952 -6.43815  1.000 45.45415  ? 358 GLU A CD    1 
ATOM   2871 O OE1   . GLU A 1 364 ? -12.49792 -12.94118 -6.67092  1.000 45.60371  ? 358 GLU A OE1   1 
ATOM   2872 O OE2   . GLU A 1 364 ? -14.52969 -13.62315 -7.14321  1.000 49.30596  ? 358 GLU A OE2   1 
ATOM   2873 N N     . ASP A 1 365 ? -13.78542 -9.15172  -3.89764  1.000 32.60670  ? 359 ASP A N     1 
ATOM   2874 C CA    . ASP A 1 365 ? -13.27146 -7.96489  -4.56765  1.000 28.88177  ? 359 ASP A CA    1 
ATOM   2875 C C     . ASP A 1 365 ? -13.95217 -6.67075  -4.13817  1.000 31.61740  ? 359 ASP A C     1 
ATOM   2876 O O     . ASP A 1 365 ? -13.75847 -5.64548  -4.80393  1.000 29.00560  ? 359 ASP A O     1 
ATOM   2877 C CB    . ASP A 1 365 ? -13.39949 -8.11623  -6.09074  1.000 33.10068  ? 359 ASP A CB    1 
ATOM   2878 C CG    . ASP A 1 365 ? -14.83639 -8.33846  -6.54061  1.000 39.45995  ? 359 ASP A CG    1 
ATOM   2879 O OD1   . ASP A 1 365 ? -15.72517 -8.49034  -5.67569  1.000 38.28938  ? 359 ASP A OD1   1 
ATOM   2880 O OD2   . ASP A 1 365 ? -15.07892 -8.35694  -7.76556  1.000 37.94438  ? 359 ASP A OD2   1 
ATOM   2881 N N     . CYS A 1 366 ? -14.73140 -6.66684  -3.05927  1.000 32.41619  ? 360 CYS A N     1 
ATOM   2882 C CA    . CYS A 1 366 ? -15.51452 -5.47828  -2.75517  1.000 30.36490  ? 360 CYS A CA    1 
ATOM   2883 C C     . CYS A 1 366 ? -15.95129 -5.47884  -1.29865  1.000 32.81123  ? 360 CYS A C     1 
ATOM   2884 O O     . CYS A 1 366 ? -15.91720 -6.50430  -0.61328  1.000 32.14108  ? 360 CYS A O     1 
ATOM   2885 C CB    . CYS A 1 366 ? -16.74434 -5.38340  -3.66254  1.000 31.67994  ? 360 CYS A CB    1 
ATOM   2886 S SG    . CYS A 1 366 ? -17.95871 -6.68701  -3.35744  1.000 38.37310  ? 360 CYS A SG    1 
ATOM   2887 N N     . VAL A 1 367 ? -16.36260 -4.29729  -0.84398  1.000 33.10123  ? 361 VAL A N     1 
ATOM   2888 C CA    . VAL A 1 367 ? -17.08635 -4.11283  0.40769   1.000 33.23407  ? 361 VAL A CA    1 
ATOM   2889 C C     . VAL A 1 367 ? -18.51785 -3.73652  0.05266   1.000 34.35944  ? 361 VAL A C     1 
ATOM   2890 O O     . VAL A 1 367 ? -18.74305 -2.79930  -0.72290  1.000 31.59428  ? 361 VAL A O     1 
ATOM   2891 C CB    . VAL A 1 367 ? -16.43645 -3.02927  1.28646   1.000 33.33429  ? 361 VAL A CB    1 
ATOM   2892 C CG1   . VAL A 1 367 ? -17.35311 -2.65957  2.44150   1.000 30.75082  ? 361 VAL A CG1   1 
ATOM   2893 C CG2   . VAL A 1 367 ? -15.08212 -3.49280  1.80014   1.000 31.48422  ? 361 VAL A CG2   1 
ATOM   2894 N N     . VAL A 1 368 ? -19.48209 -4.46702  0.60600   1.000 33.93014  ? 362 VAL A N     1 
ATOM   2895 C CA    . VAL A 1 368 ? -20.89595 -4.26152  0.31098   1.000 33.91378  ? 362 VAL A CA    1 
ATOM   2896 C C     . VAL A 1 368 ? -21.54382 -3.56069  1.49550   1.000 33.84760  ? 362 VAL A C     1 
ATOM   2897 O O     . VAL A 1 368 ? -21.42437 -4.01841  2.63867   1.000 35.70776  ? 362 VAL A O     1 
ATOM   2898 C CB    . VAL A 1 368 ? -21.61070 -5.58840  0.00198   1.000 35.40184  ? 362 VAL A CB    1 
ATOM   2899 C CG1   . VAL A 1 368 ? -23.01719 -5.32194  -0.51546  1.000 38.62614  ? 362 VAL A CG1   1 
ATOM   2900 C CG2   . VAL A 1 368 ? -20.81378 -6.39799  -1.00585  1.000 34.92690  ? 362 VAL A CG2   1 
ATOM   2901 N N     . THR A 1 369 ? -22.22816 -2.45407  1.22182   1.000 31.03469  ? 363 THR A N     1 
ATOM   2902 C CA    . THR A 1 369 ? -22.96211 -1.71755  2.23549   1.000 35.53657  ? 363 THR A CA    1 
ATOM   2903 C C     . THR A 1 369 ? -24.42627 -2.15482  2.23138   1.000 37.87263  ? 363 THR A C     1 
ATOM   2904 O O     . THR A 1 369 ? -24.86219 -2.95552  1.40057   1.000 38.58837  ? 363 THR A O     1 
ATOM   2905 C CB    . THR A 1 369 ? -22.82759 -0.20988  2.00841   1.000 34.92602  ? 363 THR A CB    1 
ATOM   2906 O OG1   . THR A 1 369 ? -22.87829 0.07296   0.60456   1.000 33.34032  ? 363 THR A OG1   1 
ATOM   2907 C CG2   . THR A 1 369 ? -21.50899 0.29810   2.57435   1.000 36.71482  ? 363 THR A CG2   1 
ATOM   2908 N N     . ALA A 1 370 ? -25.19651 -1.61455  3.17988   1.000 38.72427  ? 364 ALA A N     1 
ATOM   2909 C CA    . ALA A 1 370 ? -26.58613 -2.03457  3.33542   1.000 39.76540  ? 364 ALA A CA    1 
ATOM   2910 C C     . ALA A 1 370 ? -27.43876 -1.64895  2.13342   1.000 35.62011  ? 364 ALA A C     1 
ATOM   2911 O O     . ALA A 1 370 ? -28.45668 -2.29726  1.86617   1.000 42.99781  ? 364 ALA A O     1 
ATOM   2912 C CB    . ALA A 1 370 ? -27.17608 -1.44048  4.61388   1.000 41.62396  ? 364 ALA A CB    1 
ATOM   2913 N N     . ASP A 1 371 ? -27.04749 -0.60944  1.39981   1.000 32.98152  ? 365 ASP A N     1 
ATOM   2914 C CA    . ASP A 1 371 ? -27.78746 -0.18820  0.21722   1.000 37.06425  ? 365 ASP A CA    1 
ATOM   2915 C C     . ASP A 1 371 ? -27.54816 -1.08993  -0.98778  1.000 37.97261  ? 365 ASP A C     1 
ATOM   2916 O O     . ASP A 1 371 ? -28.10194 -0.82271  -2.05936  1.000 40.98250  ? 365 ASP A O     1 
ATOM   2917 C CB    . ASP A 1 371 ? -27.43042 1.25933   -0.13664  1.000 34.18802  ? 365 ASP A CB    1 
ATOM   2918 C CG    . ASP A 1 371 ? -25.94214 1.45784   -0.36341  1.000 34.14998  ? 365 ASP A CG    1 
ATOM   2919 O OD1   . ASP A 1 371 ? -25.17212 0.49102   -0.18679  1.000 33.45274  ? 365 ASP A OD1   1 
ATOM   2920 O OD2   . ASP A 1 371 ? -25.54054 2.58676   -0.71415  1.000 34.17629  ? 365 ASP A OD2   1 
ATOM   2921 N N     . GLY A 1 372 ? -26.74502 -2.14364  -0.84221  1.000 38.85506  ? 366 GLY A N     1 
ATOM   2922 C CA    . GLY A 1 372 ? -26.44692 -3.04519  -1.93213  1.000 35.50727  ? 366 GLY A CA    1 
ATOM   2923 C C     . GLY A 1 372 ? -25.26953 -2.64475  -2.79381  1.000 36.93399  ? 366 GLY A C     1 
ATOM   2924 O O     . GLY A 1 372 ? -24.84942 -3.43835  -3.64549  1.000 37.52085  ? 366 GLY A O     1 
ATOM   2925 N N     . VAL A 1 373 ? -24.72019 -1.44592  -2.59948  1.000 36.19842  ? 367 VAL A N     1 
ATOM   2926 C CA    . VAL A 1 373 ? -23.61405 -0.97835  -3.42602  1.000 35.17465  ? 367 VAL A CA    1 
ATOM   2927 C C     . VAL A 1 373 ? -22.36660 -1.79744  -3.12502  1.000 32.92630  ? 367 VAL A C     1 
ATOM   2928 O O     . VAL A 1 373 ? -21.99167 -1.98752  -1.96015  1.000 30.53234  ? 367 VAL A O     1 
ATOM   2929 C CB    . VAL A 1 373 ? -23.36494 0.51907   -3.19198  1.000 36.39783  ? 367 VAL A CB    1 
ATOM   2930 C CG1   . VAL A 1 373 ? -22.10380 0.97063   -3.91415  1.000 37.13795  ? 367 VAL A CG1   1 
ATOM   2931 C CG2   . VAL A 1 373 ? -24.56565 1.33444   -3.64774  1.000 38.90576  ? 367 VAL A CG2   1 
ATOM   2932 N N     . GLU A 1 374 ? -21.71801 -2.28751  -4.17784  1.000 33.34175  ? 368 GLU A N     1 
ATOM   2933 C CA    . GLU A 1 374 ? -20.45374 -3.00253  -4.06560  1.000 30.66949  ? 368 GLU A CA    1 
ATOM   2934 C C     . GLU A 1 374 ? -19.31419 -2.01712  -4.29335  1.000 34.97618  ? 368 GLU A C     1 
ATOM   2935 O O     . GLU A 1 374 ? -19.16993 -1.47291  -5.39392  1.000 34.63125  ? 368 GLU A O     1 
ATOM   2936 C CB    . GLU A 1 374 ? -20.38003 -4.15050  -5.07243  1.000 34.62217  ? 368 GLU A CB    1 
ATOM   2937 C CG    . GLU A 1 374 ? -21.38545 -5.26208  -4.81869  1.000 35.57849  ? 368 GLU A CG    1 
ATOM   2938 C CD    . GLU A 1 374 ? -21.16789 -6.46631  -5.71357  1.000 41.15930  ? 368 GLU A CD    1 
ATOM   2939 O OE1   . GLU A 1 374 ? -20.43764 -6.34050  -6.71909  1.000 38.94873  ? 368 GLU A OE1   1 
ATOM   2940 O OE2   . GLU A 1 374 ? -21.72887 -7.54022  -5.41057  1.000 37.86869  ? 368 GLU A OE2   1 
ATOM   2941 N N     . HIS A 1 375 ? -18.51323 -1.78675  -3.25534  1.000 31.37553  ? 369 HIS A N     1 
ATOM   2942 C CA    . HIS A 1 375 ? -17.36923 -0.88008  -3.33507  1.000 31.77815  ? 369 HIS A CA    1 
ATOM   2943 C C     . HIS A 1 375 ? -16.14104 -1.70342  -3.70044  1.000 27.66020  ? 369 HIS A C     1 
ATOM   2944 O O     . HIS A 1 375 ? -15.51966 -2.32961  -2.83911  1.000 29.36217  ? 369 HIS A O     1 
ATOM   2945 C CB    . HIS A 1 375 ? -17.17766 -0.13645  -2.01826  1.000 27.17647  ? 369 HIS A CB    1 
ATOM   2946 C CG    . HIS A 1 375 ? -18.37607 0.65353   -1.59248  1.000 33.42440  ? 369 HIS A CG    1 
ATOM   2947 N ND1   . HIS A 1 375 ? -18.60337 1.94643   -2.01256  1.000 33.49236  ? 369 HIS A ND1   1 
ATOM   2948 C CD2   . HIS A 1 375 ? -19.41640 0.33148   -0.78770  1.000 33.74536  ? 369 HIS A CD2   1 
ATOM   2949 C CE1   . HIS A 1 375 ? -19.73005 2.38800   -1.48249  1.000 35.55551  ? 369 HIS A CE1   1 
ATOM   2950 N NE2   . HIS A 1 375 ? -20.24322 1.42739   -0.73523  1.000 36.49113  ? 369 HIS A NE2   1 
ATOM   2951 N N     . LYS A 1 376 ? -15.78721 -1.69858  -4.98300  1.000 27.44096  ? 370 LYS A N     1 
ATOM   2952 C CA    . LYS A 1 376 ? -14.68342 -2.51994  -5.46231  1.000 31.30498  ? 370 LYS A CA    1 
ATOM   2953 C C     . LYS A 1 376 ? -13.35432 -1.97269  -4.95652  1.000 26.00144  ? 370 LYS A C     1 
ATOM   2954 O O     . LYS A 1 376 ? -13.05905 -0.78362  -5.11001  1.000 28.08097  ? 370 LYS A O     1 
ATOM   2955 C CB    . LYS A 1 376 ? -14.69801 -2.57878  -6.98858  1.000 26.87937  ? 370 LYS A CB    1 
ATOM   2956 C CG    . LYS A 1 376 ? -15.81173 -3.45583  -7.54656  1.000 32.09988  ? 370 LYS A CG    1 
ATOM   2957 C CD    . LYS A 1 376 ? -15.83359 -3.44587  -9.06401  1.000 39.04235  ? 370 LYS A CD    1 
ATOM   2958 C CE    . LYS A 1 376 ? -17.10732 -4.08423  -9.59965  1.000 40.93378  ? 370 LYS A CE    1 
ATOM   2959 N NZ    . LYS A 1 376 ? -17.20674 -5.52198  -9.21954  1.000 33.49875  ? 370 LYS A NZ    1 
ATOM   2960 N N     . LEU A 1 377 ? -12.55067 -2.84518  -4.35223  1.000 29.65946  ? 371 LEU A N     1 
ATOM   2961 C CA    . LEU A 1 377 ? -11.31262 -2.44455  -3.70114  1.000 26.15709  ? 371 LEU A CA    1 
ATOM   2962 C C     . LEU A 1 377 ? -10.18226 -3.39078  -4.07430  1.000 29.80106  ? 371 LEU A C     1 
ATOM   2963 O O     . LEU A 1 377 ? -10.36923 -4.61048  -4.12773  1.000 26.35027  ? 371 LEU A O     1 
ATOM   2964 C CB    . LEU A 1 377 ? -11.47084 -2.42339  -2.17401  1.000 28.01445  ? 371 LEU A CB    1 
ATOM   2965 C CG    . LEU A 1 377 ? -12.50444 -1.46896  -1.57417  1.000 29.04133  ? 371 LEU A CG    1 
ATOM   2966 C CD1   . LEU A 1 377 ? -12.56492 -1.64452  -0.06636  1.000 25.43399  ? 371 LEU A CD1   1 
ATOM   2967 C CD2   . LEU A 1 377 ? -12.17546 -0.02852  -1.93288  1.000 26.93301  ? 371 LEU A CD2   1 
ATOM   2968 N N     . ASP A 1 378 ? -9.00814  -2.81676  -4.33177  1.000 28.16899  ? 372 ASP A N     1 
ATOM   2969 C CA    . ASP A 1 378 ? -7.77942  -3.59133  -4.42824  1.000 28.33662  ? 372 ASP A CA    1 
ATOM   2970 C C     . ASP A 1 378 ? -7.09205  -3.75306  -3.08250  1.000 30.35319  ? 372 ASP A C     1 
ATOM   2971 O O     . ASP A 1 378 ? -6.24649  -4.64323  -2.93199  1.000 28.68729  ? 372 ASP A O     1 
ATOM   2972 C CB    . ASP A 1 378 ? -6.80641  -2.92897  -5.40826  1.000 27.57970  ? 372 ASP A CB    1 
ATOM   2973 C CG    . ASP A 1 378 ? -7.37792  -2.80763  -6.80115  1.000 29.96612  ? 372 ASP A CG    1 
ATOM   2974 O OD1   . ASP A 1 378 ? -7.67316  -3.85576  -7.40970  1.000 31.49333  ? 372 ASP A OD1   1 
ATOM   2975 O OD2   . ASP A 1 378 ? -7.53227  -1.66657  -7.28538  1.000 28.42552  ? 372 ASP A OD2   1 
ATOM   2976 N N     . MET A 1 379 ? -7.44407  -2.92045  -2.10600  1.000 27.38951  ? 373 MET A N     1 
ATOM   2977 C CA    . MET A 1 379 ? -6.78806  -2.91720  -0.80742  1.000 25.74849  ? 373 MET A CA    1 
ATOM   2978 C C     . MET A 1 379 ? -7.76664  -2.39869  0.23362   1.000 25.65157  ? 373 MET A C     1 
ATOM   2979 O O     . MET A 1 379 ? -8.43056  -1.38186  0.01008   1.000 24.47128  ? 373 MET A O     1 
ATOM   2980 C CB    . MET A 1 379 ? -5.52531  -2.05055  -0.83881  1.000 24.50409  ? 373 MET A CB    1 
ATOM   2981 C CG    . MET A 1 379 ? -4.76879  -1.98704  0.47180   1.000 29.34945  ? 373 MET A CG    1 
ATOM   2982 S SD    . MET A 1 379 ? -3.57755  -0.63628  0.47406   1.000 31.84004  ? 373 MET A SD    1 
ATOM   2983 C CE    . MET A 1 379 ? -2.37763  -1.25865  -0.69918  1.000 31.83965  ? 373 MET A CE    1 
ATOM   2984 N N     . LEU A 1 380 ? -7.85558  -3.09926  1.36100   1.000 23.45689  ? 374 LEU A N     1 
ATOM   2985 C CA    . LEU A 1 380 ? -8.72453  -2.71396  2.46576   1.000 28.96224  ? 374 LEU A CA    1 
ATOM   2986 C C     . LEU A 1 380 ? -7.87028  -2.53026  3.71083   1.000 25.76977  ? 374 LEU A C     1 
ATOM   2987 O O     . LEU A 1 380 ? -7.24319  -3.48464  4.18343   1.000 30.43271  ? 374 LEU A O     1 
ATOM   2988 C CB    . LEU A 1 380 ? -9.81512  -3.76178  2.70235   1.000 24.45543  ? 374 LEU A CB    1 
ATOM   2989 C CG    . LEU A 1 380 ? -10.82406 -3.45394  3.81145   1.000 31.48794  ? 374 LEU A CG    1 
ATOM   2990 C CD1   . LEU A 1 380 ? -11.51853 -2.12772  3.55181   1.000 25.02826  ? 374 LEU A CD1   1 
ATOM   2991 C CD2   . LEU A 1 380 ? -11.84137 -4.57914  3.94197   1.000 29.21588  ? 374 LEU A CD2   1 
ATOM   2992 N N     . ILE A 1 381 ? -7.84258  -1.30688  4.23397   1.000 30.21600  ? 375 ILE A N     1 
ATOM   2993 C CA    . ILE A 1 381 ? -7.05125  -0.96499  5.41023   1.000 27.09640  ? 375 ILE A CA    1 
ATOM   2994 C C     . ILE A 1 381 ? -7.98174  -0.86155  6.60836   1.000 27.54205  ? 375 ILE A C     1 
ATOM   2995 O O     . ILE A 1 381 ? -8.97873  -0.12934  6.56965   1.000 29.25127  ? 375 ILE A O     1 
ATOM   2996 C CB    . ILE A 1 381 ? -6.27796  0.34769   5.20085   1.000 25.76049  ? 375 ILE A CB    1 
ATOM   2997 C CG1   . ILE A 1 381 ? -5.39027  0.24931   3.95881   1.000 29.12944  ? 375 ILE A CG1   1 
ATOM   2998 C CG2   . ILE A 1 381 ? -5.44795  0.67742   6.43424   1.000 25.08678  ? 375 ILE A CG2   1 
ATOM   2999 C CD1   . ILE A 1 381 ? -4.72564  1.55471   3.57921   1.000 25.16592  ? 375 ILE A CD1   1 
ATOM   3000 N N     . CYS A 1 382 ? -7.65810  -1.58852  7.67241   1.000 29.65064  ? 376 CYS A N     1 
ATOM   3001 C CA    . CYS A 1 382 ? -8.46022  -1.60899  8.89210   1.000 32.68353  ? 376 CYS A CA    1 
ATOM   3002 C C     . CYS A 1 382 ? -7.72856  -0.81642  9.97110   1.000 34.30420  ? 376 CYS A C     1 
ATOM   3003 O O     . CYS A 1 382 ? -6.79390  -1.31962  10.60093  1.000 34.21905  ? 376 CYS A O     1 
ATOM   3004 C CB    . CYS A 1 382 ? -8.73444  -3.04215  9.33858   1.000 35.24254  ? 376 CYS A CB    1 
ATOM   3005 S SG    . CYS A 1 382 ? -9.80844  -3.97073  8.21893   1.000 39.06666  ? 376 CYS A SG    1 
ATOM   3006 N N     . ALA A 1 383 ? -8.15081  0.42633   10.16937  1.000 30.45356  ? 377 ALA A N     1 
ATOM   3007 C CA    . ALA A 1 383 ? -7.69698  1.25341   11.28828  1.000 34.25017  ? 377 ALA A CA    1 
ATOM   3008 C C     . ALA A 1 383 ? -8.72836  1.24269   12.40836  1.000 40.19874  ? 377 ALA A C     1 
ATOM   3009 O O     . ALA A 1 383 ? -9.18976  2.28432   12.87368  1.000 37.45486  ? 377 ALA A O     1 
ATOM   3010 C CB    . ALA A 1 383 ? -7.41474  2.67398   10.81467  1.000 32.36962  ? 377 ALA A CB    1 
ATOM   3011 N N     . THR A 1 384 ? -9.09797  0.04224   12.85196  1.000 43.87619  ? 378 THR A N     1 
ATOM   3012 C CA    . THR A 1 384 ? -10.24948 -0.15903  13.71979  1.000 43.12881  ? 378 THR A CA    1 
ATOM   3013 C C     . THR A 1 384 ? -9.88816  -0.23040  15.19908  1.000 48.20170  ? 378 THR A C     1 
ATOM   3014 O O     . THR A 1 384 ? -10.74660 -0.57571  16.01680  1.000 51.98784  ? 378 THR A O     1 
ATOM   3015 C CB    . THR A 1 384 ? -10.99898 -1.42649  13.30430  1.000 44.42244  ? 378 THR A CB    1 
ATOM   3016 O OG1   . THR A 1 384 ? -10.05971 -2.41737  12.86822  1.000 44.99220  ? 378 THR A OG1   1 
ATOM   3017 C CG2   . THR A 1 384 ? -11.96418 -1.12077  12.16991  1.000 42.85304  ? 378 THR A CG2   1 
ATOM   3018 N N     . GLY A 1 385 ? -8.65019  0.07818   15.56183  1.000 46.95666  ? 379 GLY A N     1 
ATOM   3019 C CA    . GLY A 1 385 ? -8.29337  0.20999   16.96046  1.000 52.71490  ? 379 GLY A CA    1 
ATOM   3020 C C     . GLY A 1 385 ? -7.75025  -1.06190  17.58370  1.000 53.46730  ? 379 GLY A C     1 
ATOM   3021 O O     . GLY A 1 385 ? -7.34039  -2.01464  16.91344  1.000 49.96179  ? 379 GLY A O     1 
ATOM   3022 N N     . PHE A 1 386 ? -7.75257  -1.06026  18.91622  1.000 55.29672  ? 380 PHE A N     1 
ATOM   3023 C CA    . PHE A 1 386 ? -7.16926  -2.12939  19.71213  1.000 55.49175  ? 380 PHE A CA    1 
ATOM   3024 C C     . PHE A 1 386 ? -8.10430  -2.46857  20.86345  1.000 55.81465  ? 380 PHE A C     1 
ATOM   3025 O O     . PHE A 1 386 ? -9.12218  -1.80730  21.08494  1.000 55.95479  ? 380 PHE A O     1 
ATOM   3026 C CB    . PHE A 1 386 ? -5.79470  -1.73465  20.27017  1.000 53.65946  ? 380 PHE A CB    1 
ATOM   3027 C CG    . PHE A 1 386 ? -4.78555  -1.38024  19.21871  1.000 54.10155  ? 380 PHE A CG    1 
ATOM   3028 C CD1   . PHE A 1 386 ? -4.76523  -0.11502  18.65361  1.000 53.38608  ? 380 PHE A CD1   1 
ATOM   3029 C CD2   . PHE A 1 386 ? -3.84468  -2.30663  18.80850  1.000 53.87102  ? 380 PHE A CD2   1 
ATOM   3030 C CE1   . PHE A 1 386 ? -3.83452  0.21275   17.68820  1.000 51.31434  ? 380 PHE A CE1   1 
ATOM   3031 C CE2   . PHE A 1 386 ? -2.91079  -1.98417  17.84819  1.000 52.70342  ? 380 PHE A CE2   1 
ATOM   3032 C CZ    . PHE A 1 386 ? -2.90539  -0.72313  17.28566  1.000 49.75994  ? 380 PHE A CZ    1 
ATOM   3033 N N     . ASP A 1 387 ? -7.74232  -3.51196  21.60510  1.000 57.71714  ? 381 ASP A N     1 
ATOM   3034 C CA    . ASP A 1 387 ? -8.41134  -3.80719  22.85971  1.000 59.89142  ? 381 ASP A CA    1 
ATOM   3035 C C     . ASP A 1 387 ? -7.91329  -2.85770  23.94819  1.000 59.22585  ? 381 ASP A C     1 
ATOM   3036 O O     . ASP A 1 387 ? -6.93529  -2.12576  23.77371  1.000 57.70964  ? 381 ASP A O     1 
ATOM   3037 C CB    . ASP A 1 387 ? -8.18205  -5.26284  23.26532  1.000 61.65991  ? 381 ASP A CB    1 
ATOM   3038 C CG    . ASP A 1 387 ? -8.71749  -6.24576  22.24218  1.000 65.27292  ? 381 ASP A CG    1 
ATOM   3039 O OD1   . ASP A 1 387 ? -9.85119  -6.04575  21.75889  1.000 65.82561  ? 381 ASP A OD1   1 
ATOM   3040 O OD2   . ASP A 1 387 ? -8.00544  -7.22072  21.92296  1.000 64.51920  ? 381 ASP A OD2   1 
ATOM   3041 N N     . ALA A 1 388 ? -8.59820  -2.87782  25.08859  1.000 60.22196  ? 382 ALA A N     1 
ATOM   3042 C CA    . ALA A 1 388 ? -8.28462  -1.95188  26.16551  1.000 62.90803  ? 382 ALA A CA    1 
ATOM   3043 C C     . ALA A 1 388 ? -6.91084  -2.25988  26.76462  1.000 56.23914  ? 382 ALA A C     1 
ATOM   3044 O O     . ALA A 1 388 ? -6.26740  -3.26376  26.44473  1.000 57.18308  ? 382 ALA A O     1 
ATOM   3045 C CB    . ALA A 1 388 ? -9.36648  -1.99988  27.24288  1.000 62.41669  ? 382 ALA A CB    1 
ATOM   3046 N N     . VAL A 1 389 ? -6.46685  -1.36927  27.65614  1.000 56.96822  ? 383 VAL A N     1 
ATOM   3047 C CA    . VAL A 1 389 ? -5.11324  -1.45856  28.20071  1.000 56.92960  ? 383 VAL A CA    1 
ATOM   3048 C C     . VAL A 1 389 ? -4.94135  -2.73277  29.01935  1.000 56.58150  ? 383 VAL A C     1 
ATOM   3049 O O     . VAL A 1 389 ? -3.89411  -3.38950  28.95954  1.000 54.28231  ? 383 VAL A O     1 
ATOM   3050 C CB    . VAL A 1 389 ? -4.78905  -0.19883  29.02734  1.000 59.25448  ? 383 VAL A CB    1 
ATOM   3051 C CG1   . VAL A 1 389 ? -5.95853  0.16426   29.93214  1.000 56.68861  ? 383 VAL A CG1   1 
ATOM   3052 C CG2   . VAL A 1 389 ? -3.51483  -0.39698  29.83704  1.000 56.46854  ? 383 VAL A CG2   1 
ATOM   3053 N N     . ASP A 1 390 ? -5.96812  -3.11336  29.78360  1.000 58.02983  ? 384 ASP A N     1 
ATOM   3054 C CA    . ASP A 1 390 ? -5.87895  -4.32067  30.59744  1.000 58.28267  ? 384 ASP A CA    1 
ATOM   3055 C C     . ASP A 1 390 ? -5.76221  -5.58201  29.75269  1.000 57.98372  ? 384 ASP A C     1 
ATOM   3056 O O     . ASP A 1 390 ? -5.40504  -6.63843  30.28530  1.000 54.53611  ? 384 ASP A O     1 
ATOM   3057 C CB    . ASP A 1 390 ? -7.09441  -4.42601  31.51977  1.000 60.82654  ? 384 ASP A CB    1 
ATOM   3058 C CG    . ASP A 1 390 ? -8.40009  -4.19563  30.78820  1.000 63.88038  ? 384 ASP A CG    1 
ATOM   3059 O OD1   . ASP A 1 390 ? -8.48883  -3.20342  30.03660  1.000 62.84039  ? 384 ASP A OD1   1 
ATOM   3060 O OD2   . ASP A 1 390 ? -9.33500  -5.00510  30.96132  1.000 66.58875  ? 384 ASP A OD2   1 
ATOM   3061 N N     . GLY A 1 391 ? -6.05268  -5.49649  28.45279  1.000 57.87930  ? 385 GLY A N     1 
ATOM   3062 C CA    . GLY A 1 391 ? -5.95102  -6.67150  27.60332  1.000 56.52115  ? 385 GLY A CA    1 
ATOM   3063 C C     . GLY A 1 391 ? -4.54106  -7.22480  27.52926  1.000 53.36683  ? 385 GLY A C     1 
ATOM   3064 O O     . GLY A 1 391 ? -4.34427  -8.44145  27.49171  1.000 56.05521  ? 385 GLY A O     1 
ATOM   3065 N N     . SER A 1 392 ? -3.54019  -6.33960  27.49862  1.000 50.41146  ? 386 SER A N     1 
ATOM   3066 C CA    . SER A 1 392 ? -2.15391  -6.79563  27.47280  1.000 48.73345  ? 386 SER A CA    1 
ATOM   3067 C C     . SER A 1 392 ? -1.80014  -7.57900  28.72934  1.000 45.13364  ? 386 SER A C     1 
ATOM   3068 O O     . SER A 1 392 ? -0.94612  -8.47178  28.68511  1.000 41.38186  ? 386 SER A O     1 
ATOM   3069 C CB    . SER A 1 392 ? -1.20834  -5.60534  27.30650  1.000 47.36581  ? 386 SER A CB    1 
ATOM   3070 O OG    . SER A 1 392 ? -1.61260  -4.77549  26.23189  1.000 50.09444  ? 386 SER A OG    1 
ATOM   3071 N N     . TYR A 1 393 ? -2.44557  -7.26591  29.85357  1.000 43.37205  ? 387 TYR A N     1 
ATOM   3072 C CA    . TYR A 1 393 ? -2.19226  -7.99819  31.08887  1.000 46.29774  ? 387 TYR A CA    1 
ATOM   3073 C C     . TYR A 1 393 ? -2.95688  -9.31610  31.11503  1.000 51.52582  ? 387 TYR A C     1 
ATOM   3074 O O     . TYR A 1 393 ? -2.39389  -10.36196 31.45687  1.000 49.81876  ? 387 TYR A O     1 
ATOM   3075 C CB    . TYR A 1 393 ? -2.55890  -7.13018  32.29344  1.000 49.76725  ? 387 TYR A CB    1 
ATOM   3076 C CG    . TYR A 1 393 ? -1.53171  -6.06245  32.57844  1.000 53.27065  ? 387 TYR A CG    1 
ATOM   3077 C CD1   . TYR A 1 393 ? -0.46841  -6.30733  33.43561  1.000 42.59673  ? 387 TYR A CD1   1 
ATOM   3078 C CD2   . TYR A 1 393 ? -1.61123  -4.81720  31.96952  1.000 46.29209  ? 387 TYR A CD2   1 
ATOM   3079 C CE1   . TYR A 1 393 ? 0.47864   -5.33739  33.69064  1.000 45.99503  ? 387 TYR A CE1   1 
ATOM   3080 C CE2   . TYR A 1 393 ? -0.66802  -3.84037  32.21730  1.000 44.13280  ? 387 TYR A CE2   1 
ATOM   3081 C CZ    . TYR A 1 393 ? 0.37488   -4.10550  33.07820  1.000 40.24965  ? 387 TYR A CZ    1 
ATOM   3082 O OH    . TYR A 1 393 ? 1.31745   -3.13443  33.32402  1.000 45.11498  ? 387 TYR A OH    1 
ATOM   3083 N N     . LYS A 1 394 ? -4.24098  -9.28557  30.74922  1.000 51.16192  ? 388 LYS A N     1 
ATOM   3084 C CA    . LYS A 1 394 ? -5.02700  -10.51207 30.69012  1.000 57.71396  ? 388 LYS A CA    1 
ATOM   3085 C C     . LYS A 1 394 ? -4.54670  -11.45367 29.59413  1.000 55.06298  ? 388 LYS A C     1 
ATOM   3086 O O     . LYS A 1 394 ? -4.82699  -12.65518 29.66088  1.000 56.89708  ? 388 LYS A O     1 
ATOM   3087 C CB    . LYS A 1 394 ? -6.50580  -10.18114 30.48703  1.000 54.20351  ? 388 LYS A CB    1 
ATOM   3088 C CG    . LYS A 1 394 ? -7.04420  -9.14976  31.46401  1.000 50.95631  ? 388 LYS A CG    1 
ATOM   3089 C CD    . LYS A 1 394 ? -8.51189  -9.39181  31.77390  1.000 55.56225  ? 388 LYS A CD    1 
ATOM   3090 C CE    . LYS A 1 394 ? -9.28806  -8.08761  31.80056  1.000 57.92503  ? 388 LYS A CE    1 
ATOM   3091 N NZ    . LYS A 1 394 ? -10.74419 -8.30569  32.01527  1.000 58.59674  ? 388 LYS A NZ    1 
ATOM   3092 N N     . ARG A 1 395 ? -3.83263  -10.93944 28.59038  1.000 48.46204  ? 389 ARG A N     1 
ATOM   3093 C CA    . ARG A 1 395 ? -3.23642  -11.79887 27.57592  1.000 49.49673  ? 389 ARG A CA    1 
ATOM   3094 C C     . ARG A 1 395 ? -2.03933  -12.57880 28.10239  1.000 46.89999  ? 389 ARG A C     1 
ATOM   3095 O O     . ARG A 1 395 ? -1.54216  -13.46460 27.39910  1.000 50.29368  ? 389 ARG A O     1 
ATOM   3096 C CB    . ARG A 1 395 ? -2.82188  -10.96912 26.35883  1.000 54.39440  ? 389 ARG A CB    1 
ATOM   3097 C CG    . ARG A 1 395 ? -3.41515  -11.45652 25.04592  1.000 58.62957  ? 389 ARG A CG    1 
ATOM   3098 C CD    . ARG A 1 395 ? -4.93183  -11.32789 25.03366  1.000 62.70281  ? 389 ARG A CD    1 
ATOM   3099 N NE    . ARG A 1 395 ? -5.36863  -9.98561  24.66795  1.000 69.65375  ? 389 ARG A NE    1 
ATOM   3100 C CZ    . ARG A 1 395 ? -6.61697  -9.54991  24.77071  1.000 71.13197  ? 389 ARG A CZ    1 
ATOM   3101 N NH1   . ARG A 1 395 ? -7.58568  -10.32807 25.22486  1.000 72.68660  ? 389 ARG A NH1   1 
ATOM   3102 N NH2   . ARG A 1 395 ? -6.90113  -8.30282  24.40633  1.000 62.94777  ? 389 ARG A NH2   1 
ATOM   3103 N N     . ILE A 1 396 ? -1.56513  -12.26893 29.30657  1.000 42.39003  ? 390 ILE A N     1 
ATOM   3104 C CA    . ILE A 1 396 ? -0.50402  -13.02328 29.95994  1.000 44.36798  ? 390 ILE A CA    1 
ATOM   3105 C C     . ILE A 1 396 ? -1.11314  -13.80298 31.11608  1.000 45.40746  ? 390 ILE A C     1 
ATOM   3106 O O     . ILE A 1 396 ? -2.06234  -13.35154 31.76712  1.000 50.36267  ? 390 ILE A O     1 
ATOM   3107 C CB    . ILE A 1 396 ? 0.63842   -12.11158 30.45799  1.000 46.96338  ? 390 ILE A CB    1 
ATOM   3108 C CG1   . ILE A 1 396 ? 0.94756   -11.02257 29.42994  1.000 45.02819  ? 390 ILE A CG1   1 
ATOM   3109 C CG2   . ILE A 1 396 ? 1.88856   -12.92780 30.75186  1.000 43.58761  ? 390 ILE A CG2   1 
ATOM   3110 C CD1   . ILE A 1 396 ? 1.90608   -9.96508  29.93666  1.000 43.48612  ? 390 ILE A CD1   1 
ATOM   3111 N N     . ASP A 1 397 ? -0.56010  -14.98969 31.36839  1.000 46.43391  ? 391 ASP A N     1 
ATOM   3112 C CA    . ASP A 1 397 ? -1.03062  -15.85464 32.45036  1.000 49.69405  ? 391 ASP A CA    1 
ATOM   3113 C C     . ASP A 1 397 ? -0.33173  -15.43890 33.74282  1.000 48.47309  ? 391 ASP A C     1 
ATOM   3114 O O     . ASP A 1 397 ? 0.65661   -16.03196 34.17906  1.000 49.11937  ? 391 ASP A O     1 
ATOM   3115 C CB    . ASP A 1 397 ? -0.77864  -17.31784 32.10938  1.000 47.51600  ? 391 ASP A CB    1 
ATOM   3116 C CG    . ASP A 1 397 ? -1.55911  -18.26631 32.99474  1.000 54.49731  ? 391 ASP A CG    1 
ATOM   3117 O OD1   . ASP A 1 397 ? -2.34890  -17.78610 33.83426  1.000 56.80792  ? 391 ASP A OD1   1 
ATOM   3118 O OD2   . ASP A 1 397 ? -1.38455  -19.49449 32.85092  1.000 53.37490  ? 391 ASP A OD2   1 
ATOM   3119 N N     . ILE A 1 398 ? -0.87024  -14.39569 34.36730  1.000 51.11447  ? 392 ILE A N     1 
ATOM   3120 C CA    . ILE A 1 398 ? -0.29744  -13.81161 35.57537  1.000 51.56008  ? 392 ILE A CA    1 
ATOM   3121 C C     . ILE A 1 398 ? -1.09933  -14.29797 36.77415  1.000 49.06010  ? 392 ILE A C     1 
ATOM   3122 O O     . ILE A 1 398 ? -2.30724  -14.05067 36.86247  1.000 51.42531  ? 392 ILE A O     1 
ATOM   3123 C CB    . ILE A 1 398 ? -0.29313  -12.27680 35.50618  1.000 50.56836  ? 392 ILE A CB    1 
ATOM   3124 C CG1   . ILE A 1 398 ? 0.51767   -11.79800 34.30000  1.000 47.13845  ? 392 ILE A CG1   1 
ATOM   3125 C CG2   . ILE A 1 398 ? 0.25796   -11.68739 36.79641  1.000 50.10828  ? 392 ILE A CG2   1 
ATOM   3126 C CD1   . ILE A 1 398 ? 0.53516   -10.29359 34.13613  1.000 46.23829  ? 392 ILE A CD1   1 
ATOM   3127 N N     . ARG A 1 399 ? -0.43041  -14.97833 37.70328  1.000 45.62829  ? 393 ARG A N     1 
ATOM   3128 C CA    . ARG A 1 399 ? -1.06316  -15.49055 38.91247  1.000 54.60407  ? 393 ARG A CA    1 
ATOM   3129 C C     . ARG A 1 399 ? -0.24333  -15.07085 40.12343  1.000 50.18269  ? 393 ARG A C     1 
ATOM   3130 O O     . ARG A 1 399 ? 0.96126   -15.33660 40.18278  1.000 45.06862  ? 393 ARG A O     1 
ATOM   3131 C CB    . ARG A 1 399 ? -1.19585  -17.01720 38.86461  1.000 52.00282  ? 393 ARG A CB    1 
ATOM   3132 C CG    . ARG A 1 399 ? -2.08672  -17.53352 37.74365  1.000 57.80328  ? 393 ARG A CG    1 
ATOM   3133 C CD    . ARG A 1 399 ? -2.65654  -18.90633 38.07313  1.000 59.71121  ? 393 ARG A CD    1 
ATOM   3134 N NE    . ARG A 1 399 ? -3.99493  -19.09584 37.52556  1.000 67.21662  ? 393 ARG A NE    1 
ATOM   3135 C CZ    . ARG A 1 399 ? -4.25980  -19.30290 36.24254  1.000 66.70638  ? 393 ARG A CZ    1 
ATOM   3136 N NH1   . ARG A 1 399 ? -3.29521  -19.38165 35.34090  1.000 65.40638  ? 393 ARG A NH1   1 
ATOM   3137 N NH2   . ARG A 1 399 ? -5.52450  -19.44119 35.85515  1.000 62.70860  ? 393 ARG A NH2   1 
ATOM   3138 N N     . GLY A 1 400 ? -0.89587  -14.42098 41.08490  1.000 49.67031  ? 394 GLY A N     1 
ATOM   3139 C CA    . GLY A 1 400 ? -0.22107  -13.96158 42.28423  1.000 55.50287  ? 394 GLY A CA    1 
ATOM   3140 C C     . GLY A 1 400 ? -0.49098  -14.83680 43.49054  1.000 56.82186  ? 394 GLY A C     1 
ATOM   3141 O O     . GLY A 1 400 ? -0.31666  -16.05747 43.42532  1.000 57.96205  ? 394 GLY A O     1 
ATOM   3142 N N     . LYS A 1 401 ? -0.91128  -14.22607 44.59806  1.000 56.88665  ? 395 LYS A N     1 
ATOM   3143 C CA    . LYS A 1 401 ? -1.29651  -14.98808 45.77710  1.000 63.06600  ? 395 LYS A CA    1 
ATOM   3144 C C     . LYS A 1 401 ? -2.45082  -15.92578 45.43860  1.000 64.41016  ? 395 LYS A C     1 
ATOM   3145 O O     . LYS A 1 401 ? -3.15584  -15.74399 44.44544  1.000 60.34460  ? 395 LYS A O     1 
ATOM   3146 C CB    . LYS A 1 401 ? -1.69914  -14.05123 46.91622  1.000 59.74939  ? 395 LYS A CB    1 
ATOM   3147 C CG    . LYS A 1 401 ? -0.52817  -13.46545 47.68597  1.000 59.25554  ? 395 LYS A CG    1 
ATOM   3148 C CD    . LYS A 1 401 ? -0.97838  -12.83044 48.99611  1.000 62.36440  ? 395 LYS A CD    1 
ATOM   3149 C CE    . LYS A 1 401 ? -2.24589  -12.01079 48.81640  1.000 64.08248  ? 395 LYS A CE    1 
ATOM   3150 N NZ    . LYS A 1 401 ? -2.46312  -11.06718 49.94736  1.000 67.23490  ? 395 LYS A NZ    1 
ATOM   3151 N N     . ASP A 1 402 ? -2.60538  -16.97499 46.25136  1.000 66.06868  ? 396 ASP A N     1 
ATOM   3152 C CA    . ASP A 1 402 ? -3.68612  -17.95511 46.12189  1.000 60.25555  ? 396 ASP A CA    1 
ATOM   3153 C C     . ASP A 1 402 ? -3.86408  -18.51378 44.71016  1.000 61.83822  ? 396 ASP A C     1 
ATOM   3154 O O     . ASP A 1 402 ? -4.66127  -19.43398 44.50286  1.000 64.82305  ? 396 ASP A O     1 
ATOM   3155 C CB    . ASP A 1 402 ? -5.01148  -17.34693 46.58950  1.000 59.51411  ? 396 ASP A CB    1 
ATOM   3156 C CG    . ASP A 1 402 ? -5.29133  -17.60501 48.05386  1.000 68.23317  ? 396 ASP A CG    1 
ATOM   3157 O OD1   . ASP A 1 402 ? -4.88563  -16.77617 48.89289  1.000 68.88193  ? 396 ASP A OD1   1 
ATOM   3158 O OD2   . ASP A 1 402 ? -5.92131  -18.63785 48.36587  1.000 72.73452  ? 396 ASP A OD2   1 
ATOM   3159 N N     . GLY A 1 403 ? -3.14087  -17.97140 43.73590  1.000 61.57639  ? 397 GLY A N     1 
ATOM   3160 C CA    . GLY A 1 403 ? -3.26625  -18.39208 42.36087  1.000 60.91478  ? 397 GLY A CA    1 
ATOM   3161 C C     . GLY A 1 403 ? -4.32075  -17.67670 41.54489  1.000 58.61908  ? 397 GLY A C     1 
ATOM   3162 O O     . GLY A 1 403 ? -4.64652  -18.15145 40.45106  1.000 61.69842  ? 397 GLY A O     1 
ATOM   3163 N N     . ILE A 1 404 ? -4.87713  -16.56112 42.03048  1.000 56.08324  ? 398 ILE A N     1 
ATOM   3164 C CA    . ILE A 1 404 ? -5.85166  -15.82992 41.22427  1.000 59.94515  ? 398 ILE A CA    1 
ATOM   3165 C C     . ILE A 1 404 ? -5.15020  -15.23131 40.01559  1.000 58.97448  ? 398 ILE A C     1 
ATOM   3166 O O     . ILE A 1 404 ? -4.06962  -14.63998 40.13300  1.000 55.79437  ? 398 ILE A O     1 
ATOM   3167 C CB    . ILE A 1 404 ? -6.58077  -14.73350 42.02446  1.000 61.74908  ? 398 ILE A CB    1 
ATOM   3168 C CG1   . ILE A 1 404 ? -6.95161  -15.15618 43.45074  1.000 63.10417  ? 398 ILE A CG1   1 
ATOM   3169 C CG2   . ILE A 1 404 ? -7.82484  -14.26879 41.27141  1.000 58.09269  ? 398 ILE A CG2   1 
ATOM   3170 C CD1   . ILE A 1 404 ? -5.97824  -14.71631 44.50161  1.000 62.28374  ? 398 ILE A CD1   1 
ATOM   3171 N N     . SER A 1 405 ? -5.75684  -15.39648 38.84559  1.000 63.15521  ? 399 SER A N     1 
ATOM   3172 C CA    . SER A 1 405 ? -5.21585  -14.82879 37.62267  1.000 57.91597  ? 399 SER A CA    1 
ATOM   3173 C C     . SER A 1 405 ? -5.65758  -13.37936 37.46546  1.000 57.23576  ? 399 SER A C     1 
ATOM   3174 O O     . SER A 1 405 ? -6.71510  -12.97352 37.95500  1.000 55.37175  ? 399 SER A O     1 
ATOM   3175 C CB    . SER A 1 405 ? -5.66058  -15.64346 36.40655  1.000 59.46096  ? 399 SER A CB    1 
ATOM   3176 O OG    . SER A 1 405 ? -6.97104  -15.28198 36.00517  1.000 56.94288  ? 399 SER A OG    1 
ATOM   3177 N N     . ILE A 1 406 ? -4.82635  -12.59124 36.77728  1.000 57.60595  ? 400 ILE A N     1 
ATOM   3178 C CA    . ILE A 1 406 ? -5.20836  -11.22257 36.45006  1.000 53.01325  ? 400 ILE A CA    1 
ATOM   3179 C C     . ILE A 1 406 ? -6.42433  -11.20613 35.53560  1.000 54.28368  ? 400 ILE A C     1 
ATOM   3180 O O     . ILE A 1 406 ? -7.14956  -10.20647 35.48279  1.000 58.25129  ? 400 ILE A O     1 
ATOM   3181 C CB    . ILE A 1 406 ? -4.01649  -10.46512 35.82476  1.000 54.03925  ? 400 ILE A CB    1 
ATOM   3182 C CG1   . ILE A 1 406 ? -4.21017  -8.95288  35.96113  1.000 55.61413  ? 400 ILE A CG1   1 
ATOM   3183 C CG2   . ILE A 1 406 ? -3.82171  -10.86216 34.36897  1.000 53.85841  ? 400 ILE A CG2   1 
ATOM   3184 C CD1   . ILE A 1 406 ? -3.57934  -8.36641  37.20476  1.000 51.73180  ? 400 ILE A CD1   1 
ATOM   3185 N N     . LYS A 1 407 ? -6.66756  -12.30294 34.81220  1.000 56.46795  ? 401 LYS A N     1 
ATOM   3186 C CA    . LYS A 1 407 ? -7.92116  -12.45523 34.08282  1.000 58.87453  ? 401 LYS A CA    1 
ATOM   3187 C C     . LYS A 1 407 ? -9.10771  -12.42836 35.03809  1.000 58.14576  ? 401 LYS A C     1 
ATOM   3188 O O     . LYS A 1 407 ? -10.11684 -11.76555 34.77124  1.000 54.65918  ? 401 LYS A O     1 
ATOM   3189 C CB    . LYS A 1 407 ? -7.89570  -13.76145 33.28394  1.000 59.05705  ? 401 LYS A CB    1 
ATOM   3190 C CG    . LYS A 1 407 ? -8.51713  -13.70569 31.88796  1.000 61.02103  ? 401 LYS A CG    1 
ATOM   3191 C CD    . LYS A 1 407 ? -9.82679  -12.94037 31.85648  1.000 62.08812  ? 401 LYS A CD    1 
ATOM   3192 C CE    . LYS A 1 407 ? -10.32501 -12.74806 30.43720  1.000 60.25564  ? 401 LYS A CE    1 
ATOM   3193 N NZ    . LYS A 1 407 ? -11.42578 -11.74723 30.37569  1.000 68.56875  ? 401 LYS A NZ    1 
ATOM   3194 N N     . ASP A 1 408 ? -8.99812  -13.13337 36.16512  1.000 58.89022  ? 402 ASP A N     1 
ATOM   3195 C CA    . ASP A 1 408 ? -10.09899 -13.19948 37.11950  1.000 60.08180  ? 402 ASP A CA    1 
ATOM   3196 C C     . ASP A 1 408 ? -10.19173 -11.92878 37.95672  1.000 59.33841  ? 402 ASP A C     1 
ATOM   3197 O O     . ASP A 1 408 ? -11.28349 -11.38287 38.14811  1.000 57.70053  ? 402 ASP A O     1 
ATOM   3198 C CB    . ASP A 1 408 ? -9.93501  -14.42300 38.02270  1.000 59.06295  ? 402 ASP A CB    1 
ATOM   3199 C CG    . ASP A 1 408 ? -10.08038 -15.72882 37.26728  1.000 64.56691  ? 402 ASP A CG    1 
ATOM   3200 O OD1   . ASP A 1 408 ? -10.79371 -15.74953 36.24265  1.000 68.36328  ? 402 ASP A OD1   1 
ATOM   3201 O OD2   . ASP A 1 408 ? -9.48158  -16.73559 37.69909  1.000 69.49080  ? 402 ASP A OD2   1 
ATOM   3202 N N     . HIS A 1 409 ? -9.05480  -11.44425 38.46471  1.000 57.49109  ? 403 HIS A N     1 
ATOM   3203 C CA    . HIS A 1 409 ? -9.07451  -10.27672 39.34127  1.000 57.98799  ? 403 HIS A CA    1 
ATOM   3204 C C     . HIS A 1 409 ? -9.56552  -9.03075  38.61514  1.000 57.21265  ? 403 HIS A C     1 
ATOM   3205 O O     . HIS A 1 409 ? -10.12718 -8.12714  39.24481  1.000 57.99049  ? 403 HIS A O     1 
ATOM   3206 C CB    . HIS A 1 409 ? -7.68283  -10.03725 39.92802  1.000 59.93016  ? 403 HIS A CB    1 
ATOM   3207 C CG    . HIS A 1 409 ? -7.61279  -8.86657  40.85874  1.000 64.71811  ? 403 HIS A CG    1 
ATOM   3208 N ND1   . HIS A 1 409 ? -8.56410  -8.62739  41.82703  1.000 61.58193  ? 403 HIS A ND1   1 
ATOM   3209 C CD2   . HIS A 1 409 ? -6.70469  -7.86840  40.96941  1.000 58.87388  ? 403 HIS A CD2   1 
ATOM   3210 C CE1   . HIS A 1 409 ? -8.24519  -7.53238  42.49384  1.000 65.34303  ? 403 HIS A CE1   1 
ATOM   3211 N NE2   . HIS A 1 409 ? -7.12099  -7.05253  41.99331  1.000 60.66297  ? 403 HIS A NE2   1 
ATOM   3212 N N     . TRP A 1 410 ? -9.37154  -8.96379  37.29860  1.000 58.30459  ? 404 TRP A N     1 
ATOM   3213 C CA    . TRP A 1 410 ? -9.81543  -7.83370  36.49246  1.000 61.83299  ? 404 TRP A CA    1 
ATOM   3214 C C     . TRP A 1 410 ? -10.95540 -8.21376  35.55166  1.000 62.12342  ? 404 TRP A C     1 
ATOM   3215 O O     . TRP A 1 410 ? -11.07353 -7.65700  34.45790  1.000 64.97835  ? 404 TRP A O     1 
ATOM   3216 C CB    . TRP A 1 410 ? -8.64874  -7.25166  35.69622  1.000 60.35421  ? 404 TRP A CB    1 
ATOM   3217 C CG    . TRP A 1 410 ? -7.75550  -6.35201  36.49240  1.000 60.13301  ? 404 TRP A CG    1 
ATOM   3218 C CD1   . TRP A 1 410 ? -7.94813  -5.92760  37.77469  1.000 60.79436  ? 404 TRP A CD1   1 
ATOM   3219 C CD2   . TRP A 1 410 ? -6.52755  -5.75931  36.05363  1.000 59.90285  ? 404 TRP A CD2   1 
ATOM   3220 N NE1   . TRP A 1 410 ? -6.91404  -5.10945  38.16249  1.000 58.16803  ? 404 TRP A NE1   1 
ATOM   3221 C CE2   . TRP A 1 410 ? -6.02915  -4.99010  37.12329  1.000 58.69065  ? 404 TRP A CE2   1 
ATOM   3222 C CE3   . TRP A 1 410 ? -5.80091  -5.80538  34.85994  1.000 59.21447  ? 404 TRP A CE3   1 
ATOM   3223 C CZ2   . TRP A 1 410 ? -4.83767  -4.27333  37.03528  1.000 56.99812  ? 404 TRP A CZ2   1 
ATOM   3224 C CZ3   . TRP A 1 410 ? -4.61851  -5.09343  34.77482  1.000 59.21699  ? 404 TRP A CZ3   1 
ATOM   3225 C CH2   . TRP A 1 410 ? -4.14875  -4.33793  35.85551  1.000 55.72946  ? 404 TRP A CH2   1 
ATOM   3226 N N     . LYS A 1 411 ? -11.80418 -9.15910  35.96436  1.000 63.45411  ? 405 LYS A N     1 
ATOM   3227 C CA    . LYS A 1 411 ? -12.90670 -9.58596  35.10991  1.000 66.07110  ? 405 LYS A CA    1 
ATOM   3228 C C     . LYS A 1 411 ? -13.91996 -8.47361  34.87435  1.000 69.57298  ? 405 LYS A C     1 
ATOM   3229 O O     . LYS A 1 411 ? -14.65879 -8.52321  33.88487  1.000 67.58678  ? 405 LYS A O     1 
ATOM   3230 C CB    . LYS A 1 411 ? -13.60689 -10.80604 35.71359  1.000 66.64251  ? 405 LYS A CB    1 
ATOM   3231 C CG    . LYS A 1 411 ? -14.24539 -10.55891 37.07178  1.000 68.99212  ? 405 LYS A CG    1 
ATOM   3232 C CD    . LYS A 1 411 ? -14.43912 -11.86129 37.83458  1.000 67.39707  ? 405 LYS A CD    1 
ATOM   3233 C CE    . LYS A 1 411 ? -15.07218 -11.61958 39.19633  1.000 63.46287  ? 405 LYS A CE    1 
ATOM   3234 N NZ    . LYS A 1 411 ? -16.55460 -11.50187 39.10807  1.000 65.15734  ? 405 LYS A NZ    1 
ATOM   3235 N N     . ASP A 1 412 ? -13.96953 -7.47307  35.75305  1.000 67.20050  ? 406 ASP A N     1 
ATOM   3236 C CA    . ASP A 1 412 ? -14.89642 -6.35679  35.62348  1.000 65.72089  ? 406 ASP A CA    1 
ATOM   3237 C C     . ASP A 1 412 ? -14.19795 -5.05902  35.23943  1.000 70.32636  ? 406 ASP A C     1 
ATOM   3238 O O     . ASP A 1 412 ? -14.83007 -3.99767  35.25486  1.000 70.81170  ? 406 ASP A O     1 
ATOM   3239 C CB    . ASP A 1 412 ? -15.67300 -6.16339  36.92751  1.000 70.01613  ? 406 ASP A CB    1 
ATOM   3240 C CG    . ASP A 1 412 ? -16.66855 -7.27566  37.18299  1.000 70.80744  ? 406 ASP A CG    1 
ATOM   3241 O OD1   . ASP A 1 412 ? -16.83876 -8.13794  36.29606  1.000 74.97903  ? 406 ASP A OD1   1 
ATOM   3242 O OD2   . ASP A 1 412 ? -17.27897 -7.28932  38.27219  1.000 70.07357  ? 406 ASP A OD2   1 
ATOM   3243 N N     . GLY A 1 413 ? -12.91425 -5.11537  34.89748  1.000 64.82782  ? 407 GLY A N     1 
ATOM   3244 C CA    . GLY A 1 413 ? -12.15790 -3.92812  34.58363  1.000 64.55659  ? 407 GLY A CA    1 
ATOM   3245 C C     . GLY A 1 413 ? -10.93295 -3.79519  35.46388  1.000 63.46207  ? 407 GLY A C     1 
ATOM   3246 O O     . GLY A 1 413 ? -10.81612 -4.44552  36.50725  1.000 62.66225  ? 407 GLY A O     1 
ATOM   3247 N N     . PRO A 1 414 ? -9.99205  -2.94485  35.05997  1.000 60.36926  ? 408 PRO A N     1 
ATOM   3248 C CA    . PRO A 1 414 ? -8.74477  -2.81348  35.81975  1.000 60.65062  ? 408 PRO A CA    1 
ATOM   3249 C C     . PRO A 1 414 ? -8.89770  -1.90724  37.03167  1.000 61.08494  ? 408 PRO A C     1 
ATOM   3250 O O     . PRO A 1 414 ? -9.59171  -0.88805  36.99376  1.000 64.12124  ? 408 PRO A O     1 
ATOM   3251 C CB    . PRO A 1 414 ? -7.77758  -2.20840  34.79608  1.000 58.68634  ? 408 PRO A CB    1 
ATOM   3252 C CG    . PRO A 1 414 ? -8.65923  -1.40195  33.90249  1.000 64.99493  ? 408 PRO A CG    1 
ATOM   3253 C CD    . PRO A 1 414 ? -9.98450  -2.12647  33.83411  1.000 65.36592  ? 408 PRO A CD    1 
ATOM   3254 N N     . ASN A 1 415 ? -8.23656  -2.29977  38.11861  1.000 61.14490  ? 409 ASN A N     1 
ATOM   3255 C CA    . ASN A 1 415 ? -8.12114  -1.48238  39.31671  1.000 58.44843  ? 409 ASN A CA    1 
ATOM   3256 C C     . ASN A 1 415 ? -6.71547  -1.64867  39.87274  1.000 59.32509  ? 409 ASN A C     1 
ATOM   3257 O O     . ASN A 1 415 ? -6.09126  -2.70074  39.71004  1.000 58.56794  ? 409 ASN A O     1 
ATOM   3258 C CB    . ASN A 1 415 ? -9.16795  -1.85897  40.37731  1.000 57.59618  ? 409 ASN A CB    1 
ATOM   3259 C CG    . ASN A 1 415 ? -9.21084  -3.34978  40.65646  1.000 59.63464  ? 409 ASN A CG    1 
ATOM   3260 O OD1   . ASN A 1 415 ? -8.22687  -3.94076  41.10086  1.000 63.23062  ? 409 ASN A OD1   1 
ATOM   3261 N ND2   . ASN A 1 415 ? -10.35856 -3.96528  40.39894  1.000 68.17093  ? 409 ASN A ND2   1 
ATOM   3262 N N     . SER A 1 416 ? -6.21828  -0.60363  40.52798  1.000 52.31635  ? 410 SER A N     1 
ATOM   3263 C CA    . SER A 1 416 ? -4.83770  -0.60844  40.99019  1.000 52.63346  ? 410 SER A CA    1 
ATOM   3264 C C     . SER A 1 416 ? -4.63997  0.49415   42.02012  1.000 50.19978  ? 410 SER A C     1 
ATOM   3265 O O     . SER A 1 416 ? -5.53198  1.30591   42.27690  1.000 49.47754  ? 410 SER A O     1 
ATOM   3266 C CB    . SER A 1 416 ? -3.86632  -0.43679  39.81914  1.000 53.23525  ? 410 SER A CB    1 
ATOM   3267 O OG    . SER A 1 416 ? -3.77284  0.92436   39.44419  1.000 50.13648  ? 410 SER A OG    1 
ATOM   3268 N N     . TYR A 1 417 ? -3.44533  0.50555   42.60813  1.000 47.27552  ? 411 TYR A N     1 
ATOM   3269 C CA    . TYR A 1 417 ? -3.01828  1.52947   43.55509  1.000 47.56601  ? 411 TYR A CA    1 
ATOM   3270 C C     . TYR A 1 417 ? -1.99297  2.41241   42.85367  1.000 44.54988  ? 411 TYR A C     1 
ATOM   3271 O O     . TYR A 1 417 ? -0.91350  1.94052   42.48028  1.000 42.28938  ? 411 TYR A O     1 
ATOM   3272 C CB    . TYR A 1 417 ? -2.43512  0.89663   44.81744  1.000 50.69780  ? 411 TYR A CB    1 
ATOM   3273 C CG    . TYR A 1 417 ? -2.16836  1.87972   45.93588  1.000 47.09124  ? 411 TYR A CG    1 
ATOM   3274 C CD1   . TYR A 1 417 ? -3.06149  2.90518   46.21354  1.000 47.43146  ? 411 TYR A CD1   1 
ATOM   3275 C CD2   . TYR A 1 417 ? -1.02144  1.78217   46.71293  1.000 50.52323  ? 411 TYR A CD2   1 
ATOM   3276 C CE1   . TYR A 1 417 ? -2.82090  3.80530   47.23446  1.000 48.76100  ? 411 TYR A CE1   1 
ATOM   3277 C CE2   . TYR A 1 417 ? -0.77182  2.67807   47.73635  1.000 55.22488  ? 411 TYR A CE2   1 
ATOM   3278 C CZ    . TYR A 1 417 ? -1.67533  3.68732   47.99265  1.000 50.41666  ? 411 TYR A CZ    1 
ATOM   3279 O OH    . TYR A 1 417 ? -1.43260  4.58151   49.01008  1.000 55.04896  ? 411 TYR A OH    1 
ATOM   3280 N N     . LEU A 1 418 ? -2.33972  3.68673   42.66529  1.000 46.24083  ? 412 LEU A N     1 
ATOM   3281 C CA    . LEU A 1 418 ? -1.48662  4.68012   42.01170  1.000 45.61736  ? 412 LEU A CA    1 
ATOM   3282 C C     . LEU A 1 418 ? -1.13843  4.30240   40.57450  1.000 44.58670  ? 412 LEU A C     1 
ATOM   3283 O O     . LEU A 1 418 ? -0.17589  4.83023   40.00856  1.000 40.37529  ? 412 LEU A O     1 
ATOM   3284 C CB    . LEU A 1 418 ? -0.20052  4.92785   42.81054  1.000 45.76249  ? 412 LEU A CB    1 
ATOM   3285 C CG    . LEU A 1 418 ? -0.30775  5.00937   44.33441  1.000 47.06809  ? 412 LEU A CG    1 
ATOM   3286 C CD1   . LEU A 1 418 ? 1.06522   5.22905   44.94945  1.000 42.47622  ? 412 LEU A CD1   1 
ATOM   3287 C CD2   . LEU A 1 418 ? -1.26947  6.10851   44.75536  1.000 45.07606  ? 412 LEU A CD2   1 
ATOM   3288 N N     . GLY A 1 419 ? -1.90572  3.40250   39.96312  1.000 47.33073  ? 413 GLY A N     1 
ATOM   3289 C CA    . GLY A 1 419 ? -1.61227  2.97558   38.61054  1.000 42.27830  ? 413 GLY A CA    1 
ATOM   3290 C C     . GLY A 1 419 ? -0.39446  2.09462   38.46363  1.000 42.15202  ? 413 GLY A C     1 
ATOM   3291 O O     . GLY A 1 419 ? 0.03708   1.84483   37.33408  1.000 41.68605  ? 413 GLY A O     1 
ATOM   3292 N N     . MET A 1 420 ? 0.17106   1.60700   39.56775  1.000 37.85812  ? 414 MET A N     1 
ATOM   3293 C CA    . MET A 1 420 ? 1.40799   0.83734   39.52741  1.000 40.31199  ? 414 MET A CA    1 
ATOM   3294 C C     . MET A 1 420 ? 1.34877   -0.49491  40.25926  1.000 42.00936  ? 414 MET A C     1 
ATOM   3295 O O     . MET A 1 420 ? 2.14479   -1.38353  39.93247  1.000 38.80592  ? 414 MET A O     1 
ATOM   3296 C CB    . MET A 1 420 ? 2.56771   1.65943   40.11130  1.000 40.66195  ? 414 MET A CB    1 
ATOM   3297 C CG    . MET A 1 420 ? 3.02980   2.80404   39.22508  1.000 40.59535  ? 414 MET A CG    1 
ATOM   3298 S SD    . MET A 1 420 ? 4.24291   3.86149   40.03895  1.000 42.12183  ? 414 MET A SD    1 
ATOM   3299 C CE    . MET A 1 420 ? 3.25171   4.55929   41.35730  1.000 38.97854  ? 414 MET A CE    1 
ATOM   3300 N N     . MET A 1 421 ? 0.45290   -0.67061  41.22840  1.000 44.02835  ? 415 MET A N     1 
ATOM   3301 C CA    . MET A 1 421 ? 0.41200   -1.87786  42.04105  1.000 45.26043  ? 415 MET A CA    1 
ATOM   3302 C C     . MET A 1 421 ? -0.99677  -2.44972  42.05268  1.000 46.40280  ? 415 MET A C     1 
ATOM   3303 O O     . MET A 1 421 ? -1.97971  -1.70412  42.08373  1.000 50.38236  ? 415 MET A O     1 
ATOM   3304 C CB    . MET A 1 421 ? 0.87487   -1.59461  43.47509  1.000 46.09667  ? 415 MET A CB    1 
ATOM   3305 C CG    . MET A 1 421 ? 2.18214   -0.82393  43.55660  1.000 50.87468  ? 415 MET A CG    1 
ATOM   3306 S SD    . MET A 1 421 ? 2.44794   -0.05723  45.16423  1.000 52.13281  ? 415 MET A SD    1 
ATOM   3307 C CE    . MET A 1 421 ? 3.30391   -1.37501  46.02001  1.000 55.92040  ? 415 MET A CE    1 
ATOM   3308 N N     . VAL A 1 422 ? -1.08692  -3.77700  42.03287  1.000 47.32124  ? 416 VAL A N     1 
ATOM   3309 C CA    . VAL A 1 422 ? -2.35793  -4.48987  42.00290  1.000 51.60058  ? 416 VAL A CA    1 
ATOM   3310 C C     . VAL A 1 422 ? -2.43668  -5.38337  43.23175  1.000 51.63481  ? 416 VAL A C     1 
ATOM   3311 O O     . VAL A 1 422 ? -1.48053  -6.10306  43.54365  1.000 49.54317  ? 416 VAL A O     1 
ATOM   3312 C CB    . VAL A 1 422 ? -2.51237  -5.32003  40.71523  1.000 54.47489  ? 416 VAL A CB    1 
ATOM   3313 C CG1   . VAL A 1 422 ? -3.92199  -5.87540  40.60725  1.000 52.27281  ? 416 VAL A CG1   1 
ATOM   3314 C CG2   . VAL A 1 422 ? -2.17166  -4.47852  39.49564  1.000 49.82857  ? 416 VAL A CG2   1 
ATOM   3315 N N     . SER A 1 423 ? -3.57148  -5.33459  43.92638  1.000 54.81221  ? 417 SER A N     1 
ATOM   3316 C CA    . SER A 1 423 ? -3.77271  -6.20081  45.07924  1.000 56.49099  ? 417 SER A CA    1 
ATOM   3317 C C     . SER A 1 423 ? -3.80949  -7.65897  44.63910  1.000 56.07624  ? 417 SER A C     1 
ATOM   3318 O O     . SER A 1 423 ? -4.28937  -7.98052  43.54856  1.000 57.50277  ? 417 SER A O     1 
ATOM   3319 C CB    . SER A 1 423 ? -5.06660  -5.82919  45.80514  1.000 54.41148  ? 417 SER A CB    1 
ATOM   3320 O OG    . SER A 1 423 ? -6.19984  -6.34904  45.13234  1.000 64.16913  ? 417 SER A OG    1 
ATOM   3321 N N     . ASN A 1 424 ? -3.28650  -8.53704  45.49912  1.000 56.00542  ? 418 ASN A N     1 
ATOM   3322 C CA    . ASN A 1 424 ? -3.12486  -9.97518  45.28083  1.000 55.77769  ? 418 ASN A CA    1 
ATOM   3323 C C     . ASN A 1 424 ? -2.00478  -10.30617 44.30247  1.000 55.37317  ? 418 ASN A C     1 
ATOM   3324 O O     . ASN A 1 424 ? -1.85684  -11.47294 43.91581  1.000 52.55305  ? 418 ASN A O     1 
ATOM   3325 C CB    . ASN A 1 424 ? -4.41977  -10.64470 44.80157  1.000 56.60515  ? 418 ASN A CB    1 
ATOM   3326 C CG    . ASN A 1 424 ? -5.42576  -10.83788 45.91684  1.000 63.23611  ? 418 ASN A CG    1 
ATOM   3327 O OD1   . ASN A 1 424 ? -6.62196  -10.98773 45.66906  1.000 66.95422  ? 418 ASN A OD1   1 
ATOM   3328 N ND2   . ASN A 1 424 ? -4.94583  -10.83717 47.15396  1.000 64.89391  ? 418 ASN A ND2   1 
ATOM   3329 N N     . PHE A 1 425 ? -1.20703  -9.32123  43.89103  1.000 53.57582  ? 419 PHE A N     1 
ATOM   3330 C CA    . PHE A 1 425 ? -0.08996  -9.53208  42.96936  1.000 52.37521  ? 419 PHE A CA    1 
ATOM   3331 C C     . PHE A 1 425 ? 1.14155   -8.84448  43.54251  1.000 51.99778  ? 419 PHE A C     1 
ATOM   3332 O O     . PHE A 1 425 ? 1.51456   -7.74501  43.11061  1.000 52.75743  ? 419 PHE A O     1 
ATOM   3333 C CB    . PHE A 1 425 ? -0.42220  -9.01542  41.56858  1.000 52.06969  ? 419 PHE A CB    1 
ATOM   3334 C CG    . PHE A 1 425 ? -1.58105  -9.72179  40.92348  1.000 50.53850  ? 419 PHE A CG    1 
ATOM   3335 C CD1   . PHE A 1 425 ? -2.88026  -9.30744  41.16008  1.000 51.04600  ? 419 PHE A CD1   1 
ATOM   3336 C CD2   . PHE A 1 425 ? -1.37126  -10.80397 40.08532  1.000 51.52156  ? 419 PHE A CD2   1 
ATOM   3337 C CE1   . PHE A 1 425 ? -3.94949  -9.95550  40.57275  1.000 55.44694  ? 419 PHE A CE1   1 
ATOM   3338 C CE2   . PHE A 1 425 ? -2.43721  -11.45711 39.49317  1.000 53.32966  ? 419 PHE A CE2   1 
ATOM   3339 C CZ    . PHE A 1 425 ? -3.72792  -11.03190 39.73804  1.000 53.59970  ? 419 PHE A CZ    1 
ATOM   3340 N N     . PRO A 1 426 ? 1.80047   -9.46637  44.51771  1.000 49.42284  ? 420 PRO A N     1 
ATOM   3341 C CA    . PRO A 1 426 ? 2.94312   -8.81473  45.16498  1.000 49.91303  ? 420 PRO A CA    1 
ATOM   3342 C C     . PRO A 1 426 ? 4.16471   -8.77733  44.26108  1.000 48.98774  ? 420 PRO A C     1 
ATOM   3343 O O     . PRO A 1 426 ? 4.32441   -9.59744  43.35337  1.000 50.84582  ? 420 PRO A O     1 
ATOM   3344 C CB    . PRO A 1 426 ? 3.19963   -9.68497  46.40377  1.000 52.96835  ? 420 PRO A CB    1 
ATOM   3345 C CG    . PRO A 1 426 ? 1.99213   -10.58182 46.52896  1.000 53.13496  ? 420 PRO A CG    1 
ATOM   3346 C CD    . PRO A 1 426 ? 1.47860   -10.75859 45.14133  1.000 51.96585  ? 420 PRO A CD    1 
ATOM   3347 N N     . ASN A 1 427 ? 5.03099   -7.79668  44.52496  1.000 48.97880  ? 421 ASN A N     1 
ATOM   3348 C CA    . ASN A 1 427 ? 6.29932   -7.60752  43.82133  1.000 47.27682  ? 421 ASN A CA    1 
ATOM   3349 C C     . ASN A 1 427 ? 6.11474   -7.37973  42.32454  1.000 43.58588  ? 421 ASN A C     1 
ATOM   3350 O O     . ASN A 1 427 ? 7.06694   -7.52404  41.55112  1.000 41.81513  ? 421 ASN A O     1 
ATOM   3351 C CB    . ASN A 1 427 ? 7.24859   -8.78619  44.06288  1.000 46.77650  ? 421 ASN A CB    1 
ATOM   3352 C CG    . ASN A 1 427 ? 7.61326   -8.94621  45.52303  1.000 51.65853  ? 421 ASN A CG    1 
ATOM   3353 O OD1   . ASN A 1 427 ? 6.92181   -8.43773  46.40381  1.000 52.95721  ? 421 ASN A OD1   1 
ATOM   3354 N ND2   . ASN A 1 427 ? 8.70652   -9.65127  45.78793  1.000 53.59773  ? 421 ASN A ND2   1 
ATOM   3355 N N     . MET A 1 428 ? 4.90615   -7.02642  41.89706  1.000 39.29899  ? 422 MET A N     1 
ATOM   3356 C CA    . MET A 1 428 ? 4.62306   -6.69359  40.50720  1.000 42.64355  ? 422 MET A CA    1 
ATOM   3357 C C     . MET A 1 428 ? 4.33868   -5.20137  40.41880  1.000 43.50948  ? 422 MET A C     1 
ATOM   3358 O O     . MET A 1 428 ? 3.44050   -4.69541  41.10097  1.000 41.56896  ? 422 MET A O     1 
ATOM   3359 C CB    . MET A 1 428 ? 3.44049   -7.49968  39.97051  1.000 43.31524  ? 422 MET A CB    1 
ATOM   3360 C CG    . MET A 1 428 ? 3.19971   -7.31270  38.48018  1.000 45.18156  ? 422 MET A CG    1 
ATOM   3361 S SD    . MET A 1 428 ? 1.66452   -8.06409  37.90872  1.000 44.65716  ? 422 MET A SD    1 
ATOM   3362 C CE    . MET A 1 428 ? 0.48558   -6.78242  38.32397  1.000 37.24940  ? 422 MET A CE    1 
ATOM   3363 N N     . PHE A 1 429 ? 5.10294   -4.50214  39.58564  1.000 40.62699  ? 423 PHE A N     1 
ATOM   3364 C CA    . PHE A 1 429 ? 4.97135   -3.06228  39.41843  1.000 40.81922  ? 423 PHE A CA    1 
ATOM   3365 C C     . PHE A 1 429 ? 4.69255   -2.75211  37.95616  1.000 39.04337  ? 423 PHE A C     1 
ATOM   3366 O O     . PHE A 1 429 ? 5.41401   -3.21906  37.06812  1.000 37.20587  ? 423 PHE A O     1 
ATOM   3367 C CB    . PHE A 1 429 ? 6.23059   -2.34035  39.90125  1.000 39.22827  ? 423 PHE A CB    1 
ATOM   3368 C CG    . PHE A 1 429 ? 6.54176   -2.58322  41.35036  1.000 40.38945  ? 423 PHE A CG    1 
ATOM   3369 C CD1   . PHE A 1 429 ? 5.79141   -1.97525  42.34329  1.000 37.76957  ? 423 PHE A CD1   1 
ATOM   3370 C CD2   . PHE A 1 429 ? 7.57233   -3.43075  41.72045  1.000 40.03818  ? 423 PHE A CD2   1 
ATOM   3371 C CE1   . PHE A 1 429 ? 6.06960   -2.19999  43.67857  1.000 44.55900  ? 423 PHE A CE1   1 
ATOM   3372 C CE2   . PHE A 1 429 ? 7.85505   -3.66003  43.05465  1.000 42.72146  ? 423 PHE A CE2   1 
ATOM   3373 C CZ    . PHE A 1 429 ? 7.10247   -3.04306  44.03421  1.000 41.38455  ? 423 PHE A CZ    1 
ATOM   3374 N N     . MET A 1 430 ? 3.64718   -1.96791  37.71392  1.000 39.08758  ? 424 MET A N     1 
ATOM   3375 C CA    . MET A 1 430 ? 3.17601   -1.67241  36.36904  1.000 41.40765  ? 424 MET A CA    1 
ATOM   3376 C C     . MET A 1 430 ? 3.69813   -0.31163  35.92695  1.000 43.36710  ? 424 MET A C     1 
ATOM   3377 O O     . MET A 1 430 ? 3.58614   0.67307   36.66559  1.000 39.33963  ? 424 MET A O     1 
ATOM   3378 C CB    . MET A 1 430 ? 1.64796   -1.69170  36.31918  1.000 37.66061  ? 424 MET A CB    1 
ATOM   3379 C CG    . MET A 1 430 ? 1.04233   -3.08334  36.41880  1.000 34.71291  ? 424 MET A CG    1 
ATOM   3380 S SD    . MET A 1 430 ? -0.76028  -3.06155  36.41325  1.000 45.45087  ? 424 MET A SD    1 
ATOM   3381 C CE    . MET A 1 430 ? -1.08763  -1.55103  37.31714  1.000 44.14776  ? 424 MET A CE    1 
ATOM   3382 N N     . VAL A 1 431 ? 4.26811   -0.26186  34.72601  1.000 40.45168  ? 425 VAL A N     1 
ATOM   3383 C CA    . VAL A 1 431 ? 4.73177   0.97759   34.11396  1.000 38.42282  ? 425 VAL A CA    1 
ATOM   3384 C C     . VAL A 1 431 ? 3.74761   1.35538   33.01662  1.000 41.92269  ? 425 VAL A C     1 
ATOM   3385 O O     . VAL A 1 431 ? 3.46670   0.54709   32.12256  1.000 39.07719  ? 425 VAL A O     1 
ATOM   3386 C CB    . VAL A 1 431 ? 6.15906   0.83658   33.55719  1.000 40.19221  ? 425 VAL A CB    1 
ATOM   3387 C CG1   . VAL A 1 431 ? 6.50103   2.02183   32.66572  1.000 40.37161  ? 425 VAL A CG1   1 
ATOM   3388 C CG2   . VAL A 1 431 ? 7.16133   0.71612   34.69639  1.000 36.17665  ? 425 VAL A CG2   1 
ATOM   3389 N N     . PHE A 1 432 ? 3.22216   2.58094   33.09080  1.000 39.46612  ? 426 PHE A N     1 
ATOM   3390 C CA    . PHE A 1 432 ? 2.19093   3.06195   32.16878  1.000 38.73155  ? 426 PHE A CA    1 
ATOM   3391 C C     . PHE A 1 432 ? 0.96806   2.14698   32.18471  1.000 44.28078  ? 426 PHE A C     1 
ATOM   3392 O O     . PHE A 1 432 ? 0.32779   1.91418   31.15749  1.000 45.88278  ? 426 PHE A O     1 
ATOM   3393 C CB    . PHE A 1 432 ? 2.73860   3.21744   30.74744  1.000 39.38681  ? 426 PHE A CB    1 
ATOM   3394 C CG    . PHE A 1 432 ? 1.98594   4.21611   29.91409  1.000 38.66842  ? 426 PHE A CG    1 
ATOM   3395 C CD1   . PHE A 1 432 ? 1.50564   5.38627   30.47788  1.000 39.95228  ? 426 PHE A CD1   1 
ATOM   3396 C CD2   . PHE A 1 432 ? 1.75716   3.98364   28.56806  1.000 41.48225  ? 426 PHE A CD2   1 
ATOM   3397 C CE1   . PHE A 1 432 ? 0.81228   6.30638   29.71571  1.000 42.56867  ? 426 PHE A CE1   1 
ATOM   3398 C CE2   . PHE A 1 432 ? 1.06476   4.90074   27.79992  1.000 44.34439  ? 426 PHE A CE2   1 
ATOM   3399 C CZ    . PHE A 1 432 ? 0.59065   6.06311   28.37498  1.000 35.74004  ? 426 PHE A CZ    1 
ATOM   3400 N N     . GLY A 1 433 ? 0.64109   1.62228   33.36531  1.000 40.88816  ? 427 GLY A N     1 
ATOM   3401 C CA    . GLY A 1 433 ? -0.49846  0.75122   33.51173  1.000 43.45250  ? 427 GLY A CA    1 
ATOM   3402 C C     . GLY A 1 433 ? -1.79404  1.52219   33.62984  1.000 48.92260  ? 427 GLY A C     1 
ATOM   3403 O O     . GLY A 1 433 ? -1.83968  2.75783   33.55095  1.000 44.41807  ? 427 GLY A O     1 
ATOM   3404 N N     . PRO A 1 434 ? -2.88340  0.78330   33.82460  1.000 50.56045  ? 428 PRO A N     1 
ATOM   3405 C CA    . PRO A 1 434 ? -4.19809  1.42064   33.95924  1.000 49.14341  ? 428 PRO A CA    1 
ATOM   3406 C C     . PRO A 1 434 ? -4.28732  2.24127   35.23752  1.000 50.80642  ? 428 PRO A C     1 
ATOM   3407 O O     . PRO A 1 434 ? -3.44641  2.15329   36.13430  1.000 50.35859  ? 428 PRO A O     1 
ATOM   3408 C CB    . PRO A 1 434 ? -5.16916  0.23704   33.98487  1.000 49.47479  ? 428 PRO A CB    1 
ATOM   3409 C CG    . PRO A 1 434 ? -4.34456  -0.91452  34.46089  1.000 54.75903  ? 428 PRO A CG    1 
ATOM   3410 C CD    . PRO A 1 434 ? -2.96517  -0.68455  33.91599  1.000 52.48594  ? 428 PRO A CD    1 
ATOM   3411 N N     . ASN A 1 435 ? -5.34405  3.05467   35.30499  1.000 46.04251  ? 429 ASN A N     1 
ATOM   3412 C CA    . ASN A 1 435 ? -5.59685  3.94959   36.43647  1.000 50.84244  ? 429 ASN A CA    1 
ATOM   3413 C C     . ASN A 1 435 ? -4.45184  4.93721   36.64537  1.000 52.06156  ? 429 ASN A C     1 
ATOM   3414 O O     . ASN A 1 435 ? -4.18867  5.37247   37.76927  1.000 49.00474  ? 429 ASN A O     1 
ATOM   3415 C CB    . ASN A 1 435 ? -5.87132  3.16277   37.72239  1.000 54.80218  ? 429 ASN A CB    1 
ATOM   3416 C CG    . ASN A 1 435 ? -6.66615  1.89587   37.47124  1.000 56.34806  ? 429 ASN A CG    1 
ATOM   3417 O OD1   . ASN A 1 435 ? -6.14477  0.78743   37.59295  1.000 56.89538  ? 429 ASN A OD1   1 
ATOM   3418 N ND2   . ASN A 1 435 ? -7.93538  2.05471   37.11535  1.000 58.02405  ? 429 ASN A ND2   1 
ATOM   3419 N N     . GLY A 1 436 ? -3.76633  5.29898   35.56348  1.000 53.29224  ? 430 GLY A N     1 
ATOM   3420 C CA    . GLY A 1 436 ? -2.69375  6.26168   35.62317  1.000 42.98277  ? 430 GLY A CA    1 
ATOM   3421 C C     . GLY A 1 436 ? -3.15032  7.63797   35.18648  1.000 47.00920  ? 430 GLY A C     1 
ATOM   3422 O O     . GLY A 1 436 ? -4.33205  7.86592   34.90935  1.000 47.14283  ? 430 GLY A O     1 
ATOM   3423 N N     . PRO A 1 437 ? -2.22026  8.58362   35.11055  1.000 44.54039  ? 431 PRO A N     1 
ATOM   3424 C CA    . PRO A 1 437 ? -2.58674  9.95256   34.74220  1.000 42.59548  ? 431 PRO A CA    1 
ATOM   3425 C C     . PRO A 1 437 ? -2.76726  10.11017  33.23892  1.000 45.16598  ? 431 PRO A C     1 
ATOM   3426 O O     . PRO A 1 437 ? -2.22902  9.35285   32.42942  1.000 42.85943  ? 431 PRO A O     1 
ATOM   3427 C CB    . PRO A 1 437 ? -1.40452  10.78969  35.24318  1.000 41.35345  ? 431 PRO A CB    1 
ATOM   3428 C CG    . PRO A 1 437 ? -0.25584  9.83833   35.35327  1.000 43.67673  ? 431 PRO A CG    1 
ATOM   3429 C CD    . PRO A 1 437 ? -0.77211  8.42447   35.32707  1.000 42.83810  ? 431 PRO A CD    1 
ATOM   3430 N N     . LEU A 1 438 ? -3.55513  11.12064  32.87786  1.000 48.10547  ? 432 LEU A N     1 
ATOM   3431 C CA    . LEU A 1 438 ? -3.78830  11.48699  31.48219  1.000 48.01659  ? 432 LEU A CA    1 
ATOM   3432 C C     . LEU A 1 438 ? -2.84668  12.63885  31.15029  1.000 44.95982  ? 432 LEU A C     1 
ATOM   3433 O O     . LEU A 1 438 ? -3.14335  13.80081  31.43865  1.000 47.10627  ? 432 LEU A O     1 
ATOM   3434 C CB    . LEU A 1 438 ? -5.24993  11.86248  31.25413  1.000 45.14882  ? 432 LEU A CB    1 
ATOM   3435 C CG    . LEU A 1 438 ? -5.77067  11.91999  29.81297  1.000 51.38739  ? 432 LEU A CG    1 
ATOM   3436 C CD1   . LEU A 1 438 ? -5.50687  13.27756  29.17218  1.000 43.37240  ? 432 LEU A CD1   1 
ATOM   3437 C CD2   . LEU A 1 438 ? -5.16320  10.80546  28.97387  1.000 54.06624  ? 432 LEU A CD2   1 
ATOM   3438 N N     . ALA A 1 439 ? -1.70900  12.31223  30.54536  1.000 42.08656  ? 433 ALA A N     1 
ATOM   3439 C CA    . ALA A 1 439 ? -0.69664  13.30539  30.21315  1.000 40.55026  ? 433 ALA A CA    1 
ATOM   3440 C C     . ALA A 1 439 ? 0.23430   12.71061  29.16462  1.000 38.19756  ? 433 ALA A C     1 
ATOM   3441 O O     . ALA A 1 439 ? 0.02085   11.59757  28.67587  1.000 35.41958  ? 433 ALA A O     1 
ATOM   3442 C CB    . ALA A 1 439 ? 0.07329   13.74807  31.46085  1.000 39.21867  ? 433 ALA A CB    1 
ATOM   3443 N N     . ASN A 1 440 ? 1.27303   13.47011  28.81982  1.000 37.70776  ? 434 ASN A N     1 
ATOM   3444 C CA    . ASN A 1 440 ? 2.28799   12.97837  27.89814  1.000 38.97197  ? 434 ASN A CA    1 
ATOM   3445 C C     . ASN A 1 440 ? 2.94332   11.72523  28.46661  1.000 38.69588  ? 434 ASN A C     1 
ATOM   3446 O O     . ASN A 1 440 ? 3.21641   11.63690  29.66662  1.000 39.26499  ? 434 ASN A O     1 
ATOM   3447 C CB    . ASN A 1 440 ? 3.33573   14.06234  27.63891  1.000 37.25061  ? 434 ASN A CB    1 
ATOM   3448 C CG    . ASN A 1 440 ? 4.11590   13.82827  26.36012  1.000 35.63753  ? 434 ASN A CG    1 
ATOM   3449 O OD1   . ASN A 1 440 ? 3.68581   13.07866  25.48373  1.000 38.40208  ? 434 ASN A OD1   1 
ATOM   3450 N ND2   . ASN A 1 440 ? 5.26738   14.47838  26.24380  1.000 39.54756  ? 434 ASN A ND2   1 
ATOM   3451 N N     . SER A 1 441 ? 3.19360   10.74624  27.59081  1.000 35.47243  ? 435 SER A N     1 
ATOM   3452 C CA    . SER A 1 441 ? 3.60204   9.42600   28.07098  1.000 39.91220  ? 435 SER A CA    1 
ATOM   3453 C C     . SER A 1 441 ? 5.00602   9.41147   28.66577  1.000 36.75024  ? 435 SER A C     1 
ATOM   3454 O O     . SER A 1 441 ? 5.17188   8.86789   29.77224  1.000 35.69511  ? 435 SER A O     1 
ATOM   3455 C CB    . SER A 1 441 ? 3.45505   8.39590   26.94740  1.000 34.52835  ? 435 SER A CB    1 
ATOM   3456 O OG    . SER A 1 441 ? 2.09183   8.18280   26.62789  1.000 47.18358  ? 435 SER A OG    1 
ATOM   3457 N N     . PRO A 1 442 ? 6.04395   9.94232   28.01391  1.000 38.11462  ? 436 PRO A N     1 
ATOM   3458 C CA    . PRO A 1 442 ? 7.40322   9.84612   28.58270  1.000 37.05296  ? 436 PRO A CA    1 
ATOM   3459 C C     . PRO A 1 442 ? 7.50247   10.43938  29.98094  1.000 35.88843  ? 436 PRO A C     1 
ATOM   3460 O O     . PRO A 1 442 ? 8.16424   9.84404   30.84512  1.000 36.39364  ? 436 PRO A O     1 
ATOM   3461 C CB    . PRO A 1 442 ? 8.26571   10.61739  27.57126  1.000 36.96360  ? 436 PRO A CB    1 
ATOM   3462 C CG    . PRO A 1 442 ? 7.54621   10.44075  26.28970  1.000 34.91458  ? 436 PRO A CG    1 
ATOM   3463 C CD    . PRO A 1 442 ? 6.08461   10.49467  26.64345  1.000 33.82609  ? 436 PRO A CD    1 
ATOM   3464 N N     . PRO A 1 443 ? 6.87943   11.59698  30.26718  1.000 36.90232  ? 437 PRO A N     1 
ATOM   3465 C CA    . PRO A 1 443 ? 6.91441   12.07442  31.66263  1.000 36.52864  ? 437 PRO A CA    1 
ATOM   3466 C C     . PRO A 1 443 ? 6.21275   11.14468  32.63742  1.000 37.41423  ? 437 PRO A C     1 
ATOM   3467 O O     . PRO A 1 443 ? 6.66347   11.00376  33.78103  1.000 32.95473  ? 437 PRO A O     1 
ATOM   3468 C CB    . PRO A 1 443 ? 6.22723   13.44482  31.58845  1.000 34.95395  ? 437 PRO A CB    1 
ATOM   3469 C CG    . PRO A 1 443 ? 6.35473   13.86530  30.18701  1.000 35.30182  ? 437 PRO A CG    1 
ATOM   3470 C CD    . PRO A 1 443 ? 6.28836   12.61644  29.37835  1.000 35.27420  ? 437 PRO A CD    1 
ATOM   3471 N N     . ILE A 1 444 ? 5.11485   10.50974  32.22289  1.000 34.29651  ? 438 ILE A N     1 
ATOM   3472 C CA    . ILE A 1 444 ? 4.44306   9.54831   33.09307  1.000 32.67498  ? 438 ILE A CA    1 
ATOM   3473 C C     . ILE A 1 444 ? 5.33147   8.33276   33.32211  1.000 33.78733  ? 438 ILE A C     1 
ATOM   3474 O O     . ILE A 1 444 ? 5.48115   7.85519   34.45313  1.000 37.45420  ? 438 ILE A O     1 
ATOM   3475 C CB    . ILE A 1 444 ? 3.08082   9.14340   32.50149  1.000 34.39493  ? 438 ILE A CB    1 
ATOM   3476 C CG1   . ILE A 1 444 ? 2.14919   10.35320  32.41314  1.000 38.82486  ? 438 ILE A CG1   1 
ATOM   3477 C CG2   . ILE A 1 444 ? 2.44341   8.03981   33.33428  1.000 34.10567  ? 438 ILE A CG2   1 
ATOM   3478 C CD1   . ILE A 1 444 ? 0.89621   10.09368  31.60168  1.000 37.82275  ? 438 ILE A CD1   1 
ATOM   3479 N N     . ILE A 1 445 ? 5.93768   7.81976   32.24931  1.000 32.99767  ? 439 ILE A N     1 
ATOM   3480 C CA    . ILE A 1 445 ? 6.79117   6.63890   32.35646  1.000 33.94274  ? 439 ILE A CA    1 
ATOM   3481 C C     . ILE A 1 445 ? 7.97996   6.92124   33.26756  1.000 37.67280  ? 439 ILE A C     1 
ATOM   3482 O O     . ILE A 1 445 ? 8.32002   6.11604   34.14291  1.000 36.44466  ? 439 ILE A O     1 
ATOM   3483 C CB    . ILE A 1 445 ? 7.24389   6.18260   30.95771  1.000 34.92319  ? 439 ILE A CB    1 
ATOM   3484 C CG1   . ILE A 1 445 ? 6.15428   5.33491   30.29617  1.000 38.48401  ? 439 ILE A CG1   1 
ATOM   3485 C CG2   . ILE A 1 445 ? 8.55888   5.42119   31.03834  1.000 39.99885  ? 439 ILE A CG2   1 
ATOM   3486 C CD1   . ILE A 1 445 ? 6.13186   5.43581   28.78687  1.000 40.49683  ? 439 ILE A CD1   1 
ATOM   3487 N N     . GLU A 1 446 ? 8.62658   8.07451   33.07712  1.000 37.90435  ? 440 GLU A N     1 
ATOM   3488 C CA    . GLU A 1 446 ? 9.77028   8.43203   33.91101  1.000 35.04619  ? 440 GLU A CA    1 
ATOM   3489 C C     . GLU A 1 446 ? 9.36684   8.57321   35.37261  1.000 36.70095  ? 440 GLU A C     1 
ATOM   3490 O O     . GLU A 1 446 ? 10.11266  8.17058   36.27339  1.000 35.57290  ? 440 GLU A O     1 
ATOM   3491 C CB    . GLU A 1 446 ? 10.39882  9.73127   33.40921  1.000 37.70338  ? 440 GLU A CB    1 
ATOM   3492 C CG    . GLU A 1 446 ? 11.34136  9.56344   32.23426  1.000 33.23643  ? 440 GLU A CG    1 
ATOM   3493 C CD    . GLU A 1 446 ? 12.01608  10.86458  31.85259  1.000 38.97178  ? 440 GLU A CD    1 
ATOM   3494 O OE1   . GLU A 1 446 ? 11.77241  11.88218  32.53384  1.000 42.83847  ? 440 GLU A OE1   1 
ATOM   3495 O OE2   . GLU A 1 446 ? 12.79066  10.87126  30.87508  1.000 38.33037  ? 440 GLU A OE2   1 
ATOM   3496 N N     . THR A 1 447 ? 8.18972   9.14877   35.62599  1.000 35.98574  ? 441 THR A N     1 
ATOM   3497 C CA    . THR A 1 447 ? 7.72803   9.32678   36.99832  1.000 34.37612  ? 441 THR A CA    1 
ATOM   3498 C C     . THR A 1 447 ? 7.50875   7.98497   37.68712  1.000 40.24570  ? 441 THR A C     1 
ATOM   3499 O O     . THR A 1 447 ? 7.90304   7.79953   38.84479  1.000 37.13566  ? 441 THR A O     1 
ATOM   3500 C CB    . THR A 1 447 ? 6.44117   10.15276  37.00942  1.000 36.86568  ? 441 THR A CB    1 
ATOM   3501 O OG1   . THR A 1 447 ? 6.72238   11.48711  36.56770  1.000 42.59815  ? 441 THR A OG1   1 
ATOM   3502 C CG2   . THR A 1 447 ? 5.84726   10.20185  38.40383  1.000 40.55165  ? 441 THR A CG2   1 
ATOM   3503 N N     . GLN A 1 448 ? 6.89172   7.03163   36.98616  1.000 34.81162  ? 442 GLN A N     1 
ATOM   3504 C CA    . GLN A 1 448 ? 6.58400   5.74542   37.60216  1.000 32.95112  ? 442 GLN A CA    1 
ATOM   3505 C C     . GLN A 1 448 ? 7.83633   4.89282   37.77021  1.000 36.26676  ? 442 GLN A C     1 
ATOM   3506 O O     . GLN A 1 448 ? 7.98175   4.18873   38.77619  1.000 38.53101  ? 442 GLN A O     1 
ATOM   3507 C CB    . GLN A 1 448 ? 5.53320   5.00956   36.77109  1.000 35.18072  ? 442 GLN A CB    1 
ATOM   3508 C CG    . GLN A 1 448 ? 4.19549   5.73210   36.70075  1.000 40.45011  ? 442 GLN A CG    1 
ATOM   3509 C CD    . GLN A 1 448 ? 3.30385   5.21193   35.59077  1.000 34.38420  ? 442 GLN A CD    1 
ATOM   3510 O OE1   . GLN A 1 448 ? 3.77061   4.55893   34.65808  1.000 36.96540  ? 442 GLN A OE1   1 
ATOM   3511 N NE2   . GLN A 1 448 ? 2.01232   5.50503   35.68365  1.000 32.37675  ? 442 GLN A NE2   1 
ATOM   3512 N N     . VAL A 1 449 ? 8.75291   4.94448   36.80077  1.000 37.51570  ? 443 VAL A N     1 
ATOM   3513 C CA    . VAL A 1 449 ? 9.96567   4.13516   36.88388  1.000 31.18626  ? 443 VAL A CA    1 
ATOM   3514 C C     . VAL A 1 449 ? 10.84154  4.59902   38.04246  1.000 38.31620  ? 443 VAL A C     1 
ATOM   3515 O O     . VAL A 1 449 ? 11.41108  3.77989   38.77413  1.000 35.06958  ? 443 VAL A O     1 
ATOM   3516 C CB    . VAL A 1 449 ? 10.72308  4.17063   35.54349  1.000 29.31670  ? 443 VAL A CB    1 
ATOM   3517 C CG1   . VAL A 1 449 ? 12.13875  3.64113   35.71013  1.000 32.02847  ? 443 VAL A CG1   1 
ATOM   3518 C CG2   . VAL A 1 449 ? 9.97370   3.36739   34.49127  1.000 35.50565  ? 443 VAL A CG2   1 
ATOM   3519 N N     . ARG A 1 450 ? 10.95833  5.91563   38.23476  1.000 35.58436  ? 444 ARG A N     1 
ATOM   3520 C CA    . ARG A 1 450 ? 11.72312  6.42939   39.36713  1.000 35.56333  ? 444 ARG A CA    1 
ATOM   3521 C C     . ARG A 1 450 ? 11.06433  6.05988   40.69009  1.000 36.12250  ? 444 ARG A C     1 
ATOM   3522 O O     . ARG A 1 450 ? 11.75167  5.71058   41.65701  1.000 40.37783  ? 444 ARG A O     1 
ATOM   3523 C CB    . ARG A 1 450 ? 11.87779  7.94546   39.25269  1.000 37.90086  ? 444 ARG A CB    1 
ATOM   3524 C CG    . ARG A 1 450 ? 13.11868  8.39091   38.49941  1.000 41.85243  ? 444 ARG A CG    1 
ATOM   3525 C CD    . ARG A 1 450 ? 13.15027  9.90213   38.33989  1.000 40.02730  ? 444 ARG A CD    1 
ATOM   3526 N NE    . ARG A 1 450 ? 13.53399  10.29708  36.99024  1.000 47.84864  ? 444 ARG A NE    1 
ATOM   3527 C CZ    . ARG A 1 450 ? 12.77640  11.02014  36.17705  1.000 47.66881  ? 444 ARG A CZ    1 
ATOM   3528 N NH1   . ARG A 1 450 ? 11.58321  11.45503  36.54779  1.000 47.75634  ? 444 ARG A NH1   1 
ATOM   3529 N NH2   . ARG A 1 450 ? 13.22694  11.31363  34.96081  1.000 50.35052  ? 444 ARG A NH2   1 
ATOM   3530 N N     . TRP A 1 451 ? 9.73266   6.13112   40.74969  1.000 36.71539  ? 445 TRP A N     1 
ATOM   3531 C CA    . TRP A 1 451 ? 9.01900   5.77089   41.97040  1.000 40.49127  ? 445 TRP A CA    1 
ATOM   3532 C C     . TRP A 1 451 ? 9.17784   4.28919   42.28844  1.000 43.82560  ? 445 TRP A C     1 
ATOM   3533 O O     . TRP A 1 451 ? 9.41565   3.91845   43.44421  1.000 44.07653  ? 445 TRP A O     1 
ATOM   3534 C CB    . TRP A 1 451 ? 7.54119   6.13611   41.83245  1.000 41.45146  ? 445 TRP A CB    1 
ATOM   3535 C CG    . TRP A 1 451 ? 6.77954   6.11835   43.12231  1.000 46.50910  ? 445 TRP A CG    1 
ATOM   3536 C CD1   . TRP A 1 451 ? 6.53918   7.17911   43.94603  1.000 48.91791  ? 445 TRP A CD1   1 
ATOM   3537 C CD2   . TRP A 1 451 ? 6.14658   4.98591   43.73170  1.000 47.92306  ? 445 TRP A CD2   1 
ATOM   3538 N NE1   . TRP A 1 451 ? 5.79954   6.77766   45.03179  1.000 52.37350  ? 445 TRP A NE1   1 
ATOM   3539 C CE2   . TRP A 1 451 ? 5.54588   5.43556   44.92444  1.000 48.14270  ? 445 TRP A CE2   1 
ATOM   3540 C CE3   . TRP A 1 451 ? 6.03194   3.63564   43.38617  1.000 47.60663  ? 445 TRP A CE3   1 
ATOM   3541 C CZ2   . TRP A 1 451 ? 4.84145   4.58378   45.77290  1.000 54.42707  ? 445 TRP A CZ2   1 
ATOM   3542 C CZ3   . TRP A 1 451 ? 5.33187   2.79162   44.22990  1.000 46.88584  ? 445 TRP A CZ3   1 
ATOM   3543 C CH2   . TRP A 1 451 ? 4.74599   3.26876   45.40891  1.000 50.86910  ? 445 TRP A CH2   1 
ATOM   3544 N N     . ILE A 1 452 ? 9.04766   3.42804   41.27657  1.000 42.95174  ? 446 ILE A N     1 
ATOM   3545 C CA    . ILE A 1 452 ? 9.18704   1.99098   41.49686  1.000 43.16396  ? 446 ILE A CA    1 
ATOM   3546 C C     . ILE A 1 452 ? 10.61148  1.65116   41.91614  1.000 39.90279  ? 446 ILE A C     1 
ATOM   3547 O O     . ILE A 1 452 ? 10.83133  0.84686   42.83064  1.000 38.34414  ? 446 ILE A O     1 
ATOM   3548 C CB    . ILE A 1 452 ? 8.76634   1.21531   40.23392  1.000 39.18291  ? 446 ILE A CB    1 
ATOM   3549 C CG1   . ILE A 1 452 ? 7.24850   1.27570   40.04777  1.000 34.30507  ? 446 ILE A CG1   1 
ATOM   3550 C CG2   . ILE A 1 452 ? 9.24222   -0.22841  40.30360  1.000 35.69323  ? 446 ILE A CG2   1 
ATOM   3551 C CD1   . ILE A 1 452 ? 6.80341   1.11746   38.60884  1.000 36.21365  ? 446 ILE A CD1   1 
ATOM   3552 N N     . ALA A 1 453 ? 11.60067  2.26435   41.26179  1.000 37.77725  ? 447 ALA A N     1 
ATOM   3553 C CA    . ALA A 1 453 ? 12.99423  1.96951   41.57868  1.000 39.60549  ? 447 ALA A CA    1 
ATOM   3554 C C     . ALA A 1 453 ? 13.35119  2.41425   42.99169  1.000 45.67049  ? 447 ALA A C     1 
ATOM   3555 O O     . ALA A 1 453 ? 14.11193  1.73196   43.68853  1.000 42.01521  ? 447 ALA A O     1 
ATOM   3556 C CB    . ALA A 1 453 ? 13.91520  2.63400   40.55702  1.000 39.51802  ? 447 ALA A CB    1 
ATOM   3557 N N     . ASP A 1 454 ? 12.81509  3.55535   43.43156  1.000 42.71515  ? 448 ASP A N     1 
ATOM   3558 C CA    . ASP A 1 454 ? 13.08386  4.01975   44.78886  1.000 46.76976  ? 448 ASP A CA    1 
ATOM   3559 C C     . ASP A 1 454 ? 12.47937  3.07940   45.82354  1.000 48.47467  ? 448 ASP A C     1 
ATOM   3560 O O     . ASP A 1 454 ? 13.07383  2.84814   46.88277  1.000 47.63847  ? 448 ASP A O     1 
ATOM   3561 C CB    . ASP A 1 454 ? 12.54706  5.43824   44.97592  1.000 43.06970  ? 448 ASP A CB    1 
ATOM   3562 C CG    . ASP A 1 454 ? 13.48453  6.49297   44.42570  1.000 44.78345  ? 448 ASP A CG    1 
ATOM   3563 O OD1   . ASP A 1 454 ? 14.63742  6.14931   44.09037  1.000 45.48685  ? 448 ASP A OD1   1 
ATOM   3564 O OD2   . ASP A 1 454 ? 13.06859  7.66637   44.32956  1.000 48.01190  ? 448 ASP A OD2   1 
ATOM   3565 N N     . LEU A 1 455 ? 11.29731  2.53020   45.53546  1.000 43.77552  ? 449 LEU A N     1 
ATOM   3566 C CA    . LEU A 1 455 ? 10.67721  1.58177   46.45470  1.000 46.93530  ? 449 LEU A CA    1 
ATOM   3567 C C     . LEU A 1 455 ? 11.45569  0.27260   46.50292  1.000 49.03281  ? 449 LEU A C     1 
ATOM   3568 O O     . LEU A 1 455 ? 11.60154  -0.33057  47.57266  1.000 50.64054  ? 449 LEU A O     1 
ATOM   3569 C CB    . LEU A 1 455 ? 9.22406   1.33587   46.04599  1.000 48.66640  ? 449 LEU A CB    1 
ATOM   3570 C CG    . LEU A 1 455 ? 8.44917   0.20591   46.73123  1.000 49.42836  ? 449 LEU A CG    1 
ATOM   3571 C CD1   . LEU A 1 455 ? 8.49133   0.33436   48.24771  1.000 50.09655  ? 449 LEU A CD1   1 
ATOM   3572 C CD2   . LEU A 1 455 ? 7.01253   0.17595   46.23721  1.000 46.13010  ? 449 LEU A CD2   1 
ATOM   3573 N N     . ILE A 1 456 ? 11.96660  -0.18015  45.35624  1.000 47.41743  ? 450 ILE A N     1 
ATOM   3574 C CA    . ILE A 1 456 ? 12.75153  -1.41010  45.33026  1.000 47.12092  ? 450 ILE A CA    1 
ATOM   3575 C C     . ILE A 1 456 ? 14.07938  -1.21021  46.05200  1.000 51.19720  ? 450 ILE A C     1 
ATOM   3576 O O     . ILE A 1 456 ? 14.55204  -2.10049  46.76965  1.000 48.36070  ? 450 ILE A O     1 
ATOM   3577 C CB    . ILE A 1 456 ? 12.94884  -1.88179  43.87801  1.000 41.78881  ? 450 ILE A CB    1 
ATOM   3578 C CG1   . ILE A 1 456 ? 11.61625  -2.35537  43.29182  1.000 43.18786  ? 450 ILE A CG1   1 
ATOM   3579 C CG2   . ILE A 1 456 ? 13.98448  -2.99200  43.80555  1.000 40.71643  ? 450 ILE A CG2   1 
ATOM   3580 C CD1   . ILE A 1 456 ? 11.69595  -2.76373  41.83648  1.000 43.78427  ? 450 ILE A CD1   1 
ATOM   3581 N N     . GLY A 1 457 ? 14.69849  -0.03988  45.88268  1.000 52.80595  ? 451 GLY A N     1 
ATOM   3582 C CA    . GLY A 1 457 ? 15.89781  0.26458   46.64632  1.000 46.97287  ? 451 GLY A CA    1 
ATOM   3583 C C     . GLY A 1 457 ? 15.61627  0.39481   48.13084  1.000 52.09629  ? 451 GLY A C     1 
ATOM   3584 O O     . GLY A 1 457 ? 16.40245  -0.06379  48.96474  1.000 57.87138  ? 451 GLY A O     1 
ATOM   3585 N N     . TYR A 1 458 ? 14.49218  1.02646   48.48028  1.000 52.48101  ? 452 TYR A N     1 
ATOM   3586 C CA    . TYR A 1 458 ? 14.04505  1.05191   49.86905  1.000 52.11724  ? 452 TYR A CA    1 
ATOM   3587 C C     . TYR A 1 458 ? 13.79548  -0.35570  50.39243  1.000 59.60801  ? 452 TYR A C     1 
ATOM   3588 O O     . TYR A 1 458 ? 13.95626  -0.61307  51.59123  1.000 62.32981  ? 452 TYR A O     1 
ATOM   3589 C CB    . TYR A 1 458 ? 12.78073  1.90906   49.98180  1.000 51.91847  ? 452 TYR A CB    1 
ATOM   3590 C CG    . TYR A 1 458 ? 12.11767  1.92848   51.34358  1.000 59.03523  ? 452 TYR A CG    1 
ATOM   3591 C CD1   . TYR A 1 458 ? 12.45554  2.88922   52.28791  1.000 62.27720  ? 452 TYR A CD1   1 
ATOM   3592 C CD2   . TYR A 1 458 ? 11.12895  1.00804   51.67197  1.000 58.01580  ? 452 TYR A CD2   1 
ATOM   3593 C CE1   . TYR A 1 458 ? 11.84329  2.92000   53.52810  1.000 65.48481  ? 452 TYR A CE1   1 
ATOM   3594 C CE2   . TYR A 1 458 ? 10.51318  1.02991   52.90998  1.000 63.03950  ? 452 TYR A CE2   1 
ATOM   3595 C CZ    . TYR A 1 458 ? 10.87366  1.98791   53.83366  1.000 65.11979  ? 452 TYR A CZ    1 
ATOM   3596 O OH    . TYR A 1 458 ? 10.26199  2.01449   55.06636  1.000 66.28455  ? 452 TYR A OH    1 
ATOM   3597 N N     . ALA A 1 459 ? 13.41012  -1.27803  49.50785  1.000 54.52959  ? 453 ALA A N     1 
ATOM   3598 C CA    . ALA A 1 459 ? 13.18345  -2.65857  49.91847  1.000 58.03930  ? 453 ALA A CA    1 
ATOM   3599 C C     . ALA A 1 459 ? 14.49834  -3.39282  50.14655  1.000 61.49580  ? 453 ALA A C     1 
ATOM   3600 O O     . ALA A 1 459 ? 14.62008  -4.18146  51.09135  1.000 61.42640  ? 453 ALA A O     1 
ATOM   3601 C CB    . ALA A 1 459 ? 12.34113  -3.38209  48.86818  1.000 57.05299  ? 453 ALA A CB    1 
ATOM   3602 N N     . GLU A 1 460 ? 15.49363  -3.14540  49.29148  1.000 58.72707  ? 454 GLU A N     1 
ATOM   3603 C CA    . GLU A 1 460 ? 16.76556  -3.85141  49.40199  1.000 60.76361  ? 454 GLU A CA    1 
ATOM   3604 C C     . GLU A 1 460 ? 17.51977  -3.47115  50.66992  1.000 67.69893  ? 454 GLU A C     1 
ATOM   3605 O O     . GLU A 1 460 ? 18.28774  -4.28315  51.19859  1.000 66.54037  ? 454 GLU A O     1 
ATOM   3606 C CB    . GLU A 1 460 ? 17.62639  -3.56820  48.17093  1.000 60.64840  ? 454 GLU A CB    1 
ATOM   3607 C CG    . GLU A 1 460 ? 18.77624  -4.54029  47.97383  1.000 69.26948  ? 454 GLU A CG    1 
ATOM   3608 C CD    . GLU A 1 460 ? 18.52454  -5.51642  46.84249  1.000 71.92125  ? 454 GLU A CD    1 
ATOM   3609 O OE1   . GLU A 1 460 ? 17.35001  -5.87156  46.61102  1.000 69.03936  ? 454 GLU A OE1   1 
ATOM   3610 O OE2   . GLU A 1 460 ? 19.50179  -5.92537  46.18127  1.000 72.51630  ? 454 GLU A OE2   1 
ATOM   3611 N N     . ASP A 1 461 ? 17.31718  -2.25372  51.17188  1.000 63.14430  ? 455 ASP A N     1 
ATOM   3612 C CA    . ASP A 1 461 ? 18.04460  -1.78381  52.34446  1.000 67.61801  ? 455 ASP A CA    1 
ATOM   3613 C C     . ASP A 1 461 ? 17.37732  -2.19647  53.65037  1.000 64.82492  ? 455 ASP A C     1 
ATOM   3614 O O     . ASP A 1 461 ? 18.06923  -2.51006  54.62509  1.000 72.61018  ? 455 ASP A O     1 
ATOM   3615 C CB    . ASP A 1 461 ? 18.19114  -0.26095  52.29407  1.000 62.70083  ? 455 ASP A CB    1 
ATOM   3616 C CG    . ASP A 1 461 ? 19.00796  0.20472   51.10677  1.000 65.56779  ? 455 ASP A CG    1 
ATOM   3617 O OD1   . ASP A 1 461 ? 19.47312  -0.65705  50.33150  1.000 67.47262  ? 455 ASP A OD1   1 
ATOM   3618 O OD2   . ASP A 1 461 ? 19.18339  1.43078   50.94671  1.000 67.31244  ? 455 ASP A OD2   1 
ATOM   3619 N N     . HIS A 1 462 ? 16.04761  -2.20287  53.69176  1.000 65.05769  ? 456 HIS A N     1 
ATOM   3620 C CA    . HIS A 1 462 ? 15.30750  -2.56074  54.89318  1.000 64.85091  ? 456 HIS A CA    1 
ATOM   3621 C C     . HIS A 1 462 ? 15.00894  -4.05292  54.97495  1.000 65.03007  ? 456 HIS A C     1 
ATOM   3622 O O     . HIS A 1 462 ? 14.24744  -4.47282  55.85282  1.000 68.38030  ? 456 HIS A O     1 
ATOM   3623 C CB    . HIS A 1 462 ? 14.00682  -1.75410  54.97328  1.000 63.81823  ? 456 HIS A CB    1 
ATOM   3624 C CG    . HIS A 1 462 ? 14.21651  -0.27494  55.09799  1.000 67.39189  ? 456 HIS A CG    1 
ATOM   3625 N ND1   . HIS A 1 462 ? 15.29929  0.37579   54.54588  1.000 70.54080  ? 456 HIS A ND1   1 
ATOM   3626 C CD2   . HIS A 1 462 ? 13.48381  0.67900   55.72047  1.000 68.94699  ? 456 HIS A CD2   1 
ATOM   3627 C CE1   . HIS A 1 462 ? 15.22230  1.66597   54.81813  1.000 70.69433  ? 456 HIS A CE1   1 
ATOM   3628 N NE2   . HIS A 1 462 ? 14.13052  1.87630   55.53090  1.000 69.54920  ? 456 HIS A NE2   1 
ATOM   3629 N N     . GLN A 1 463 ? 15.58703  -4.85202  54.07547  1.000 62.82850  ? 457 GLN A N     1 
ATOM   3630 C CA    . GLN A 1 463 ? 15.51142  -6.31341  54.12480  1.000 67.40159  ? 457 GLN A CA    1 
ATOM   3631 C C     . GLN A 1 463 ? 14.06604  -6.81012  54.11756  1.000 70.58242  ? 457 GLN A C     1 
ATOM   3632 O O     . GLN A 1 463 ? 13.66548  -7.64220  54.93419  1.000 75.24491  ? 457 GLN A O     1 
ATOM   3633 C CB    . GLN A 1 463 ? 16.27183  -6.86113  55.33528  1.000 69.47041  ? 457 GLN A CB    1 
ATOM   3634 C CG    . GLN A 1 463 ? 17.78378  -6.84129  55.17788  1.000 71.52933  ? 457 GLN A CG    1 
ATOM   3635 C CD    . GLN A 1 463 ? 18.50672  -7.25411  56.44372  1.000 77.74240  ? 457 GLN A CD    1 
ATOM   3636 O OE1   . GLN A 1 463 ? 18.46634  -6.55177  57.45335  1.000 77.69607  ? 457 GLN A OE1   1 
ATOM   3637 N NE2   . GLN A 1 463 ? 19.17414  -8.40077  56.39564  1.000 74.49541  ? 457 GLN A NE2   1 
ATOM   3638 N N     . ILE A 1 464 ? 13.27811  -6.29334  53.17961  1.000 68.45542  ? 458 ILE A N     1 
ATOM   3639 C CA    . ILE A 1 464 ? 11.92709  -6.78075  52.93334  1.000 68.95247  ? 458 ILE A CA    1 
ATOM   3640 C C     . ILE A 1 464 ? 11.91080  -7.45335  51.56768  1.000 66.83110  ? 458 ILE A C     1 
ATOM   3641 O O     . ILE A 1 464 ? 12.61140  -7.02474  50.64233  1.000 67.58385  ? 458 ILE A O     1 
ATOM   3642 C CB    . ILE A 1 464 ? 10.87503  -5.65521  53.02844  1.000 65.79486  ? 458 ILE A CB    1 
ATOM   3643 C CG1   . ILE A 1 464 ? 10.91440  -4.75025  51.79644  1.000 61.67249  ? 458 ILE A CG1   1 
ATOM   3644 C CG2   . ILE A 1 464 ? 11.08154  -4.84280  54.30044  1.000 67.17705  ? 458 ILE A CG2   1 
ATOM   3645 C CD1   . ILE A 1 464 ? 10.23257  -3.41019  51.98974  1.000 70.12470  ? 458 ILE A CD1   1 
ATOM   3646 N N     . ASN A 1 465 ? 11.13074  -8.52689  51.45110  1.000 67.38919  ? 459 ASN A N     1 
ATOM   3647 C CA    . ASN A 1 465 ? 11.12759  -9.35000  50.25134  1.000 62.88118  ? 459 ASN A CA    1 
ATOM   3648 C C     . ASN A 1 465 ? 9.76854   -9.43761  49.57358  1.000 58.77394  ? 459 ASN A C     1 
ATOM   3649 O O     . ASN A 1 465 ? 9.65407   -10.10551 48.53944  1.000 59.79156  ? 459 ASN A O     1 
ATOM   3650 C CB    . ASN A 1 465 ? 11.62907  -10.76426 50.58034  1.000 64.67880  ? 459 ASN A CB    1 
ATOM   3651 C CG    . ASN A 1 465 ? 10.63005  -11.56568 51.39369  1.000 67.12000  ? 459 ASN A CG    1 
ATOM   3652 O OD1   . ASN A 1 465 ? 9.79280   -11.00489 52.10106  1.000 68.25489  ? 459 ASN A OD1   1 
ATOM   3653 N ND2   . ASN A 1 465 ? 10.71987  -12.88675 51.30301  1.000 72.04764  ? 459 ASN A ND2   1 
ATOM   3654 N N     . GLN A 1 466 ? 8.74022   -8.78983  50.11575  1.000 55.47535  ? 460 GLN A N     1 
ATOM   3655 C CA    . GLN A 1 466 ? 7.40901   -8.83441  49.52754  1.000 54.59048  ? 460 GLN A CA    1 
ATOM   3656 C C     . GLN A 1 466 ? 6.74270   -7.47649  49.68067  1.000 60.31211  ? 460 GLN A C     1 
ATOM   3657 O O     . GLN A 1 466 ? 6.64550   -6.95065  50.79340  1.000 58.95813  ? 460 GLN A O     1 
ATOM   3658 C CB    . GLN A 1 466 ? 6.55099   -9.92692  50.17672  1.000 55.97543  ? 460 GLN A CB    1 
ATOM   3659 C CG    . GLN A 1 466 ? 5.17225   -10.08073 49.55694  1.000 53.24043  ? 460 GLN A CG    1 
ATOM   3660 C CD    . GLN A 1 466 ? 4.60412   -11.47431 49.73690  1.000 53.50530  ? 460 GLN A CD    1 
ATOM   3661 O OE1   . GLN A 1 466 ? 5.34220   -12.45901 49.77318  1.000 48.70380  ? 460 GLN A OE1   1 
ATOM   3662 N NE2   . GLN A 1 466 ? 3.28464   -11.56451 49.84875  1.000 53.14214  ? 460 GLN A NE2   1 
ATOM   3663 N N     . ILE A 1 467 ? 6.29206   -6.91394  48.56094  1.000 53.26829  ? 461 ILE A N     1 
ATOM   3664 C CA    . ILE A 1 467 ? 5.61164   -5.62484  48.52886  1.000 52.70077  ? 461 ILE A CA    1 
ATOM   3665 C C     . ILE A 1 467 ? 4.26909   -5.81634  47.83981  1.000 53.13473  ? 461 ILE A C     1 
ATOM   3666 O O     . ILE A 1 467 ? 4.21362   -6.32185  46.71356  1.000 50.01670  ? 461 ILE A O     1 
ATOM   3667 C CB    . ILE A 1 467 ? 6.44398   -4.55359  47.79805  1.000 53.10125  ? 461 ILE A CB    1 
ATOM   3668 C CG1   . ILE A 1 467 ? 7.88439   -4.54467  48.31553  1.000 48.99545  ? 461 ILE A CG1   1 
ATOM   3669 C CG2   . ILE A 1 467 ? 5.80637   -3.18405  47.95956  1.000 50.69010  ? 461 ILE A CG2   1 
ATOM   3670 C CD1   . ILE A 1 467 ? 8.81947   -3.66860  47.50731  1.000 49.56825  ? 461 ILE A CD1   1 
ATOM   3671 N N     . GLU A 1 468 ? 3.19202   -5.41063  48.50887  1.000 51.81429  ? 462 GLU A N     1 
ATOM   3672 C CA    . GLU A 1 468 ? 1.85185   -5.60846  47.97694  1.000 51.80934  ? 462 GLU A CA    1 
ATOM   3673 C C     . GLU A 1 468 ? 0.93482   -4.50154  48.47369  1.000 55.24491  ? 462 GLU A C     1 
ATOM   3674 O O     . GLU A 1 468 ? 0.95842   -4.14991  49.65606  1.000 59.46260  ? 462 GLU A O     1 
ATOM   3675 C CB    . GLU A 1 468 ? 1.29048   -6.97689  48.38079  1.000 55.10697  ? 462 GLU A CB    1 
ATOM   3676 C CG    . GLU A 1 468 ? -0.16556  -7.18800  48.00220  1.000 55.42725  ? 462 GLU A CG    1 
ATOM   3677 C CD    . GLU A 1 468 ? -0.71404  -8.50390  48.51135  1.000 59.08683  ? 462 GLU A CD    1 
ATOM   3678 O OE1   . GLU A 1 468 ? 0.02323   -9.22479  49.21505  1.000 56.32260  ? 462 GLU A OE1   1 
ATOM   3679 O OE2   . GLU A 1 468 ? -1.88366  -8.81657  48.20941  1.000 62.90669  ? 462 GLU A OE2   1 
ATOM   3680 N N     . ALA A 1 469 ? 0.12727   -3.96235  47.56386  1.000 48.07563  ? 463 ALA A N     1 
ATOM   3681 C CA    . ALA A 1 469 ? -0.85708  -2.95350  47.92406  1.000 56.52226  ? 463 ALA A CA    1 
ATOM   3682 C C     . ALA A 1 469 ? -2.09662  -3.61172  48.51520  1.000 61.29082  ? 463 ALA A C     1 
ATOM   3683 O O     . ALA A 1 469 ? -2.54787  -4.65895  48.04238  1.000 63.54813  ? 463 ALA A O     1 
ATOM   3684 C CB    . ALA A 1 469 ? -1.23890  -2.11676  46.70322  1.000 56.91218  ? 463 ALA A CB    1 
ATOM   3685 N N     . THR A 1 470 ? -2.64494  -2.99167  49.55630  1.000 60.22692  ? 464 THR A N     1 
ATOM   3686 C CA    . THR A 1 470 ? -3.82586  -3.53391  50.20783  1.000 56.45681  ? 464 THR A CA    1 
ATOM   3687 C C     . THR A 1 470 ? -5.05553  -3.37024  49.31917  1.000 59.39287  ? 464 THR A C     1 
ATOM   3688 O O     . THR A 1 470 ? -5.07511  -2.57911  48.37161  1.000 60.90376  ? 464 THR A O     1 
ATOM   3689 C CB    . THR A 1 470 ? -4.07031  -2.84625  51.55176  1.000 60.45296  ? 464 THR A CB    1 
ATOM   3690 O OG1   . THR A 1 470 ? -4.42437  -1.47510  51.33236  1.000 59.62363  ? 464 THR A OG1   1 
ATOM   3691 C CG2   . THR A 1 470 ? -2.82554  -2.90962  52.41951  1.000 57.04419  ? 464 THR A CG2   1 
ATOM   3692 N N     . LYS A 1 471 ? -6.09575  -4.14265  49.64058  1.000 53.94378  ? 465 LYS A N     1 
ATOM   3693 C CA    . LYS A 1 471 ? -7.36287  -4.00747  48.93054  1.000 60.15690  ? 465 LYS A CA    1 
ATOM   3694 C C     . LYS A 1 471 ? -7.97207  -2.62971  49.15728  1.000 59.20250  ? 465 LYS A C     1 
ATOM   3695 O O     . LYS A 1 471 ? -8.55804  -2.04130  48.24094  1.000 57.81519  ? 465 LYS A O     1 
ATOM   3696 C CB    . LYS A 1 471 ? -8.32955  -5.10638  49.37543  1.000 62.66575  ? 465 LYS A CB    1 
ATOM   3697 C CG    . LYS A 1 471 ? -9.77453  -4.88221  48.95803  1.000 67.10459  ? 465 LYS A CG    1 
ATOM   3698 C CD    . LYS A 1 471 ? -10.42603 -6.17427  48.49342  1.000 69.02103  ? 465 LYS A CD    1 
ATOM   3699 C CE    . LYS A 1 471 ? -11.60141 -5.89738  47.56978  1.000 62.59669  ? 465 LYS A CE    1 
ATOM   3700 N NZ    . LYS A 1 471 ? -12.55831 -4.92446  48.16559  1.000 68.25708  ? 465 LYS A NZ    1 
ATOM   3701 N N     . ASP A 1 472 ? -7.82794  -2.09138  50.37054  1.000 62.45195  ? 466 ASP A N     1 
ATOM   3702 C CA    . ASP A 1 472 ? -8.41647  -0.79336  50.68070  1.000 60.58812  ? 466 ASP A CA    1 
ATOM   3703 C C     . ASP A 1 472 ? -7.69085  0.34349   49.97170  1.000 59.14931  ? 466 ASP A C     1 
ATOM   3704 O O     . ASP A 1 472 ? -8.32179  1.33844   49.59774  1.000 52.78648  ? 466 ASP A O     1 
ATOM   3705 C CB    . ASP A 1 472 ? -8.41403  -0.56754  52.19217  1.000 63.93065  ? 466 ASP A CB    1 
ATOM   3706 C CG    . ASP A 1 472 ? -9.33171  -1.52694  52.92455  1.000 68.54452  ? 466 ASP A CG    1 
ATOM   3707 O OD1   . ASP A 1 472 ? -9.97918  -2.35888  52.25406  1.000 66.32671  ? 466 ASP A OD1   1 
ATOM   3708 O OD2   . ASP A 1 472 ? -9.40454  -1.45076  54.16930  1.000 71.77951  ? 466 ASP A OD2   1 
ATOM   3709 N N     . ALA A 1 473 ? -6.37491  0.22152   49.78061  1.000 55.75343  ? 467 ALA A N     1 
ATOM   3710 C CA    . ALA A 1 473 ? -5.63748  1.26116   49.06934  1.000 57.28468  ? 467 ALA A CA    1 
ATOM   3711 C C     . ALA A 1 473 ? -6.04494  1.32012   47.60303  1.000 57.39248  ? 467 ALA A C     1 
ATOM   3712 O O     . ALA A 1 473 ? -6.12841  2.40706   47.01885  1.000 55.67353  ? 467 ALA A O     1 
ATOM   3713 C CB    . ALA A 1 473 ? -4.13382  1.02448   49.19906  1.000 53.79553  ? 467 ALA A CB    1 
ATOM   3714 N N     . VAL A 1 474 ? -6.29949  0.16099   46.99243  1.000 53.86128  ? 468 VAL A N     1 
ATOM   3715 C CA    . VAL A 1 474 ? -6.75558  0.13104   45.60521  1.000 52.11807  ? 468 VAL A CA    1 
ATOM   3716 C C     . VAL A 1 474 ? -8.12938  0.77933   45.48872  1.000 54.90341  ? 468 VAL A C     1 
ATOM   3717 O O     . VAL A 1 474 ? -8.37863  1.59640   44.59404  1.000 57.61753  ? 468 VAL A O     1 
ATOM   3718 C CB    . VAL A 1 474 ? -6.76456  -1.31496  45.07638  1.000 54.39644  ? 468 VAL A CB    1 
ATOM   3719 C CG1   . VAL A 1 474 ? -7.63296  -1.42672  43.83172  1.000 53.35542  ? 468 VAL A CG1   1 
ATOM   3720 C CG2   . VAL A 1 474 ? -5.34628  -1.78444  44.78909  1.000 49.01727  ? 468 VAL A CG2   1 
ATOM   3721 N N     . ASP A 1 475 ? -9.04038  0.42946   46.40056  1.000 53.87314  ? 469 ASP A N     1 
ATOM   3722 C CA    . ASP A 1 475 ? -10.37513 1.01740   46.37544  1.000 56.39028  ? 469 ASP A CA    1 
ATOM   3723 C C     . ASP A 1 475 ? -10.34306 2.50035   46.72062  1.000 60.17206  ? 469 ASP A C     1 
ATOM   3724 O O     . ASP A 1 475 ? -11.20947 3.25790   46.26919  1.000 62.33560  ? 469 ASP A O     1 
ATOM   3725 C CB    . ASP A 1 475 ? -11.29789 0.26229   47.33075  1.000 58.98244  ? 469 ASP A CB    1 
ATOM   3726 C CG    . ASP A 1 475 ? -11.59958 -1.14493  46.85427  1.000 64.06823  ? 469 ASP A CG    1 
ATOM   3727 O OD1   . ASP A 1 475 ? -10.66215 -1.83484  46.40228  1.000 66.17245  ? 469 ASP A OD1   1 
ATOM   3728 O OD2   . ASP A 1 475 ? -12.77367 -1.56196  46.92982  1.000 66.20058  ? 469 ASP A OD2   1 
ATOM   3729 N N     . ASN A 1 476 ? -9.36154  2.93256   47.51607  1.000 56.48014  ? 470 ASN A N     1 
ATOM   3730 C CA    . ASN A 1 476 ? -9.18592  4.36133   47.75421  1.000 57.38073  ? 470 ASN A CA    1 
ATOM   3731 C C     . ASN A 1 476 ? -8.74767  5.07608   46.48250  1.000 55.21272  ? 470 ASN A C     1 
ATOM   3732 O O     . ASN A 1 476 ? -9.15626  6.21565   46.23001  1.000 54.50630  ? 470 ASN A O     1 
ATOM   3733 C CB    . ASN A 1 476 ? -8.17147  4.58889   48.87511  1.000 63.50405  ? 470 ASN A CB    1 
ATOM   3734 C CG    . ASN A 1 476 ? -8.78661  4.46113   50.25473  1.000 69.81090  ? 470 ASN A CG    1 
ATOM   3735 O OD1   . ASN A 1 476 ? -9.72363  3.69097   50.46164  1.000 66.31060  ? 470 ASN A OD1   1 
ATOM   3736 N ND2   . ASN A 1 476 ? -8.25995  5.22013   51.20865  1.000 75.83098  ? 470 ASN A ND2   1 
ATOM   3737 N N     . TRP A 1 477 ? -7.91682  4.41951   45.66945  1.000 58.12070  ? 471 TRP A N     1 
ATOM   3738 C CA    . TRP A 1 477 ? -7.49364  5.00937   44.40397  1.000 54.63172  ? 471 TRP A CA    1 
ATOM   3739 C C     . TRP A 1 477 ? -8.65390  5.09761   43.42098  1.000 54.76397  ? 471 TRP A C     1 
ATOM   3740 O O     . TRP A 1 477 ? -8.77365  6.08079   42.68022  1.000 56.27272  ? 471 TRP A O     1 
ATOM   3741 C CB    . TRP A 1 477 ? -6.34448  4.19679   43.80807  1.000 49.89079  ? 471 TRP A CB    1 
ATOM   3742 C CG    . TRP A 1 477 ? -5.67388  4.86119   42.64599  1.000 54.81580  ? 471 TRP A CG    1 
ATOM   3743 C CD1   . TRP A 1 477 ? -5.63122  4.41122   41.35864  1.000 51.20249  ? 471 TRP A CD1   1 
ATOM   3744 C CD2   . TRP A 1 477 ? -4.94618  6.09567   42.66367  1.000 54.17421  ? 471 TRP A CD2   1 
ATOM   3745 N NE1   . TRP A 1 477 ? -4.92352  5.28853   40.57348  1.000 49.49556  ? 471 TRP A NE1   1 
ATOM   3746 C CE2   . TRP A 1 477 ? -4.49255  6.33131   41.35055  1.000 51.37366  ? 471 TRP A CE2   1 
ATOM   3747 C CE3   . TRP A 1 477 ? -4.63472  7.02432   43.66164  1.000 52.72944  ? 471 TRP A CE3   1 
ATOM   3748 C CZ2   . TRP A 1 477 ? -3.74398  7.45575   41.00976  1.000 47.87077  ? 471 TRP A CZ2   1 
ATOM   3749 C CZ3   . TRP A 1 477 ? -3.89215  8.14068   43.32091  1.000 53.79888  ? 471 TRP A CZ3   1 
ATOM   3750 C CH2   . TRP A 1 477 ? -3.45511  8.34650   42.00637  1.000 54.10367  ? 471 TRP A CH2   1 
ATOM   3751 N N     . THR A 1 478 ? -9.51649  4.07805   43.39858  1.000 51.99733  ? 472 THR A N     1 
ATOM   3752 C CA    . THR A 1 478 ? -10.68130 4.11145   42.52003  1.000 55.00825  ? 472 THR A CA    1 
ATOM   3753 C C     . THR A 1 478 ? -11.61779 5.25320   42.89463  1.000 57.69812  ? 472 THR A C     1 
ATOM   3754 O O     . THR A 1 478 ? -12.20191 5.90167   42.01806  1.000 54.84883  ? 472 THR A O     1 
ATOM   3755 C CB    . THR A 1 478 ? -11.41934 2.77298   42.57454  1.000 55.47396  ? 472 THR A CB    1 
ATOM   3756 O OG1   . THR A 1 478 ? -10.49352 1.70431   42.34074  1.000 58.55397  ? 472 THR A OG1   1 
ATOM   3757 C CG2   . THR A 1 478 ? -12.51676 2.72361   41.52114  1.000 53.40634  ? 472 THR A CG2   1 
ATOM   3758 N N     . ASN A 1 479 ? -11.77013 5.51622   44.19493  1.000 56.63155  ? 473 ASN A N     1 
ATOM   3759 C CA    . ASN A 1 479 ? -12.60218 6.63279   44.63008  1.000 56.94085  ? 473 ASN A CA    1 
ATOM   3760 C C     . ASN A 1 479 ? -11.99116 7.96659   44.22073  1.000 54.85852  ? 473 ASN A C     1 
ATOM   3761 O O     . ASN A 1 479 ? -12.70730 8.87586   43.78596  1.000 57.00552  ? 473 ASN A O     1 
ATOM   3762 C CB    . ASN A 1 479 ? -12.80502 6.57925   46.14400  1.000 59.29577  ? 473 ASN A CB    1 
ATOM   3763 C CG    . ASN A 1 479 ? -13.58777 5.35877   46.58518  1.000 64.82634  ? 473 ASN A CG    1 
ATOM   3764 O OD1   . ASN A 1 479 ? -14.43485 4.85092   45.85070  1.000 68.54659  ? 473 ASN A OD1   1 
ATOM   3765 N ND2   . ASN A 1 479 ? -13.30839 4.88186   47.79275  1.000 67.09200  ? 473 ASN A ND2   1 
ATOM   3766 N N     . THR A 1 480 ? -10.66858 8.10005   44.35054  1.000 53.77037  ? 474 THR A N     1 
ATOM   3767 C CA    . THR A 1 480 ? -10.00727 9.34464   43.97116  1.000 54.80570  ? 474 THR A CA    1 
ATOM   3768 C C     . THR A 1 480 ? -10.14930 9.61255   42.47806  1.000 55.01636  ? 474 THR A C     1 
ATOM   3769 O O     . THR A 1 480 ? -10.35720 10.75823  42.06187  1.000 56.21544  ? 474 THR A O     1 
ATOM   3770 C CB    . THR A 1 480 ? -8.53099  9.29693   44.36741  1.000 55.97003  ? 474 THR A CB    1 
ATOM   3771 O OG1   . THR A 1 480 ? -8.41476  8.90003   45.73950  1.000 57.41504  ? 474 THR A OG1   1 
ATOM   3772 C CG2   . THR A 1 480 ? -7.88229  10.66249  44.18382  1.000 51.58317  ? 474 THR A CG2   1 
ATOM   3773 N N     . CYS A 1 481 ? -10.04535 8.56622   41.65591  1.000 56.19590  ? 475 CYS A N     1 
ATOM   3774 C CA    . CYS A 1 481 ? -10.17465 8.74620   40.21373  1.000 52.60892  ? 475 CYS A CA    1 
ATOM   3775 C C     . CYS A 1 481 ? -11.61434 9.05376   39.81982  1.000 54.51811  ? 475 CYS A C     1 
ATOM   3776 O O     . CYS A 1 481 ? -11.85888 9.91521   38.96718  1.000 55.14906  ? 475 CYS A O     1 
ATOM   3777 C CB    . CYS A 1 481 ? -9.67025  7.50206   39.48341  1.000 51.47032  ? 475 CYS A CB    1 
ATOM   3778 S SG    . CYS A 1 481 ? -7.89956  7.19185   39.67168  1.000 49.07285  ? 475 CYS A SG    1 
ATOM   3779 N N     . SER A 1 482 ? -12.58091 8.36191   40.42857  1.000 57.07551  ? 476 SER A N     1 
ATOM   3780 C CA    . SER A 1 482 ? -13.98188 8.61607   40.10680  1.000 53.85256  ? 476 SER A CA    1 
ATOM   3781 C C     . SER A 1 482 ? -14.42326 9.98727   40.60265  1.000 57.90522  ? 476 SER A C     1 
ATOM   3782 O O     . SER A 1 482 ? -15.22257 10.66286  39.94416  1.000 57.23844  ? 476 SER A O     1 
ATOM   3783 C CB    . SER A 1 482 ? -14.86710 7.52085   40.70085  1.000 57.91917  ? 476 SER A CB    1 
ATOM   3784 O OG    . SER A 1 482 ? -14.45831 7.19013   42.01576  1.000 63.92230  ? 476 SER A OG    1 
ATOM   3785 N N     . ASP A 1 483 ? -13.91475 10.41442  41.76163  1.000 58.14722  ? 477 ASP A N     1 
ATOM   3786 C CA    . ASP A 1 483 ? -14.26269 11.73368  42.28036  1.000 59.27878  ? 477 ASP A CA    1 
ATOM   3787 C C     . ASP A 1 483 ? -13.78712 12.83572  41.34275  1.000 60.28662  ? 477 ASP A C     1 
ATOM   3788 O O     . ASP A 1 483 ? -14.48413 13.83764  41.14408  1.000 56.20737  ? 477 ASP A O     1 
ATOM   3789 C CB    . ASP A 1 483 ? -13.66613 11.92349  43.67508  1.000 61.79646  ? 477 ASP A CB    1 
ATOM   3790 C CG    . ASP A 1 483 ? -14.68419 11.71650  44.77828  1.000 67.38918  ? 477 ASP A CG    1 
ATOM   3791 O OD1   . ASP A 1 483 ? -15.70050 12.44176  44.79424  1.000 70.93129  ? 477 ASP A OD1   1 
ATOM   3792 O OD2   . ASP A 1 483 ? -14.46807 10.82840  45.62996  1.000 65.87243  ? 477 ASP A OD2   1 
ATOM   3793 N N     . ILE A 1 484 ? -12.60331 12.66637  40.75383  1.000 58.01509  ? 478 ILE A N     1 
ATOM   3794 C CA    . ILE A 1 484 ? -12.08284 13.66468  39.82641  1.000 57.98637  ? 478 ILE A CA    1 
ATOM   3795 C C     . ILE A 1 484 ? -12.77361 13.55805  38.47235  1.000 61.08770  ? 478 ILE A C     1 
ATOM   3796 O O     . ILE A 1 484 ? -13.11226 14.57386  37.85430  1.000 60.81374  ? 478 ILE A O     1 
ATOM   3797 C CB    . ILE A 1 484 ? -10.55536 13.51860  39.69734  1.000 55.87718  ? 478 ILE A CB    1 
ATOM   3798 C CG1   . ILE A 1 484 ? -9.87464  13.80158  41.03843  1.000 51.12022  ? 478 ILE A CG1   1 
ATOM   3799 C CG2   . ILE A 1 484 ? -10.01535 14.44544  38.61865  1.000 55.91260  ? 478 ILE A CG2   1 
ATOM   3800 C CD1   . ILE A 1 484 ? -8.40661  13.43759  41.06600  1.000 54.25102  ? 478 ILE A CD1   1 
ATOM   3801 N N     . ALA A 1 485 ? -13.00224 12.33187  37.99469  1.000 57.37108  ? 479 ALA A N     1 
ATOM   3802 C CA    . ALA A 1 485 ? -13.56742 12.14859  36.66124  1.000 57.03743  ? 479 ALA A CA    1 
ATOM   3803 C C     . ALA A 1 485 ? -15.01788 12.61099  36.59720  1.000 60.22130  ? 479 ALA A C     1 
ATOM   3804 O O     . ALA A 1 485 ? -15.45977 13.13876  35.57016  1.000 62.26401  ? 479 ALA A O     1 
ATOM   3805 C CB    . ALA A 1 485 ? -13.45307 10.68454  36.23838  1.000 53.84230  ? 479 ALA A CB    1 
ATOM   3806 N N     . ASN A 1 486 ? -15.77604 12.42441  37.67981  1.000 60.63421  ? 480 ASN A N     1 
ATOM   3807 C CA    . ASN A 1 486 ? -17.17707 12.82953  37.68085  1.000 58.92256  ? 480 ASN A CA    1 
ATOM   3808 C C     . ASN A 1 486 ? -17.35619 14.34198  37.71399  1.000 63.90509  ? 480 ASN A C     1 
ATOM   3809 O O     . ASN A 1 486 ? -18.49130 14.81583  37.59538  1.000 66.45744  ? 480 ASN A O     1 
ATOM   3810 C CB    . ASN A 1 486 ? -17.91032 12.18476  38.85762  1.000 65.70412  ? 480 ASN A CB    1 
ATOM   3811 C CG    . ASN A 1 486 ? -18.16462 10.70494  38.64111  1.000 67.13124  ? 480 ASN A CG    1 
ATOM   3812 O OD1   . ASN A 1 486 ? -17.90970 9.88311   39.52034  1.000 74.34446  ? 480 ASN A OD1   1 
ATOM   3813 N ND2   . ASN A 1 486 ? -18.66494 10.35802  37.46047  1.000 70.34665  ? 480 ASN A ND2   1 
ATOM   3814 N N     . LYS A 1 487 ? -16.27717 15.10321  37.87692  1.000 61.51790  ? 481 LYS A N     1 
ATOM   3815 C CA    . LYS A 1 487 ? -16.29886 16.54588  37.68314  1.000 63.74629  ? 481 LYS A CA    1 
ATOM   3816 C C     . LYS A 1 487 ? -16.06814 16.93721  36.23041  1.000 63.84881  ? 481 LYS A C     1 
ATOM   3817 O O     . LYS A 1 487 ? -16.03721 18.13273  35.92078  1.000 65.20126  ? 481 LYS A O     1 
ATOM   3818 C CB    . LYS A 1 487 ? -15.23580 17.21631  38.56038  1.000 61.76781  ? 481 LYS A CB    1 
ATOM   3819 C CG    . LYS A 1 487 ? -15.55455 17.24202  40.04476  1.000 64.48265  ? 481 LYS A CG    1 
ATOM   3820 C CD    . LYS A 1 487 ? -14.35561 17.73422  40.84183  1.000 66.95439  ? 481 LYS A CD    1 
ATOM   3821 C CE    . LYS A 1 487 ? -14.63548 17.72926  42.33407  1.000 66.78636  ? 481 LYS A CE    1 
ATOM   3822 N NZ    . LYS A 1 487 ? -15.45891 18.89842  42.74585  1.000 72.16120  ? 481 LYS A NZ    1 
ATOM   3823 N N     . THR A 1 488 ? -15.91072 15.96150  35.33991  1.000 60.49095  ? 482 THR A N     1 
ATOM   3824 C CA    . THR A 1 488 ? -15.49097 16.19107  33.96745  1.000 63.31834  ? 482 THR A CA    1 
ATOM   3825 C C     . THR A 1 488 ? -16.54301 15.66746  32.99870  1.000 68.51652  ? 482 THR A C     1 
ATOM   3826 O O     . THR A 1 488 ? -17.21444 14.66585  33.26570  1.000 73.00143  ? 482 THR A O     1 
ATOM   3827 C CB    . THR A 1 488 ? -14.14261 15.50346  33.69037  1.000 64.37052  ? 482 THR A CB    1 
ATOM   3828 O OG1   . THR A 1 488 ? -13.25825 15.71889  34.79723  1.000 64.59759  ? 482 THR A OG1   1 
ATOM   3829 C CG2   . THR A 1 488 ? -13.49910 16.04673  32.42596  1.000 70.35987  ? 482 THR A CG2   1 
ATOM   3830 N N     . LEU A 1 489 ? -16.68064 16.35942  31.86478  1.000 66.77542  ? 483 LEU A N     1 
ATOM   3831 C CA    . LEU A 1 489 ? -17.53273 15.88194  30.78286  1.000 64.65264  ? 483 LEU A CA    1 
ATOM   3832 C C     . LEU A 1 489 ? -16.99952 14.61266  30.13499  1.000 72.26249  ? 483 LEU A C     1 
ATOM   3833 O O     . LEU A 1 489 ? -17.73325 13.97141  29.37484  1.000 75.91604  ? 483 LEU A O     1 
ATOM   3834 C CB    . LEU A 1 489 ? -17.69195 16.96661  29.71657  1.000 60.58252  ? 483 LEU A CB    1 
ATOM   3835 C CG    . LEU A 1 489 ? -18.47846 18.21492  30.11495  1.000 61.50215  ? 483 LEU A CG    1 
ATOM   3836 C CD1   . LEU A 1 489 ? -18.24788 19.33408  29.11247  1.000 54.96755  ? 483 LEU A CD1   1 
ATOM   3837 C CD2   . LEU A 1 489 ? -19.95745 17.88897  30.23088  1.000 64.08847  ? 483 LEU A CD2   1 
ATOM   3838 N N     . PHE A 1 490 ? -15.74779 14.23965  30.41481  1.000 73.10364  ? 484 PHE A N     1 
ATOM   3839 C CA    . PHE A 1 490 ? -15.16915 13.03291  29.83599  1.000 75.48030  ? 484 PHE A CA    1 
ATOM   3840 C C     . PHE A 1 490 ? -15.92908 11.77702  30.24108  1.000 80.39104  ? 484 PHE A C     1 
ATOM   3841 O O     . PHE A 1 490 ? -15.78742 10.74042  29.58321  1.000 82.80423  ? 484 PHE A O     1 
ATOM   3842 C CB    . PHE A 1 490 ? -13.70279 12.90428  30.25100  1.000 74.41417  ? 484 PHE A CB    1 
ATOM   3843 C CG    . PHE A 1 490 ? -12.75353 13.72390  29.41888  1.000 76.63134  ? 484 PHE A CG    1 
ATOM   3844 C CD1   . PHE A 1 490 ? -13.17337 14.88882  28.79729  1.000 75.71873  ? 484 PHE A CD1   1 
ATOM   3845 C CD2   . PHE A 1 490 ? -11.43395 13.33027  29.26851  1.000 77.11347  ? 484 PHE A CD2   1 
ATOM   3846 C CE1   . PHE A 1 490 ? -12.29745 15.64002  28.03593  1.000 76.86743  ? 484 PHE A CE1   1 
ATOM   3847 C CE2   . PHE A 1 490 ? -10.55352 14.07755  28.50937  1.000 76.81369  ? 484 PHE A CE2   1 
ATOM   3848 C CZ    . PHE A 1 490 ? -10.98595 15.23394  27.89253  1.000 76.00716  ? 484 PHE A CZ    1 
ATOM   3849 N N     . ALA A 1 491 ? -16.72366 11.84226  31.31123  1.000 79.91131  ? 485 ALA A N     1 
ATOM   3850 C CA    . ALA A 1 491 ? -17.53521 10.69772  31.70684  1.000 79.66945  ? 485 ALA A CA    1 
ATOM   3851 C C     . ALA A 1 491 ? -18.80480 10.59739  30.87038  1.000 82.04353  ? 485 ALA A C     1 
ATOM   3852 O O     . ALA A 1 491 ? -19.25601 9.49085   30.55401  1.000 85.04260  ? 485 ALA A O     1 
ATOM   3853 C CB    . ALA A 1 491 ? -17.88333 10.78841  33.19288  1.000 78.48721  ? 485 ALA A CB    1 
ATOM   3854 N N     . LYS A 1 492 ? -19.38929 11.73980  30.50170  1.000 76.69365  ? 486 LYS A N     1 
ATOM   3855 C CA    . LYS A 1 492 ? -20.64003 11.72806  29.74923  1.000 78.64974  ? 486 LYS A CA    1 
ATOM   3856 C C     . LYS A 1 492 ? -20.44509 11.11944  28.36593  1.000 82.82038  ? 486 LYS A C     1 
ATOM   3857 O O     . LYS A 1 492 ? -21.16223 10.19076  27.97572  1.000 86.78274  ? 486 LYS A O     1 
ATOM   3858 C CB    . LYS A 1 492 ? -21.19662 13.14783  29.63920  1.000 73.54851  ? 486 LYS A CB    1 
ATOM   3859 C CG    . LYS A 1 492 ? -22.69886 13.20794  29.41753  1.000 73.54383  ? 486 LYS A CG    1 
ATOM   3860 C CD    . LYS A 1 492 ? -23.23025 14.62329  29.58221  1.000 69.49030  ? 486 LYS A CD    1 
ATOM   3861 C CE    . LYS A 1 492 ? -22.80293 15.23268  30.90687  1.000 74.73284  ? 486 LYS A CE    1 
ATOM   3862 N NZ    . LYS A 1 492 ? -23.63956 14.74051  32.03459  1.000 71.30295  ? 486 LYS A NZ    1 
ATOM   3863 N N     . ALA A 1 493 ? -19.47175 11.62738  27.61047  1.000 82.09913  ? 487 ALA A N     1 
ATOM   3864 C CA    . ALA A 1 493 ? -19.22539 11.14451  26.25713  1.000 84.96075  ? 487 ALA A CA    1 
ATOM   3865 C C     . ALA A 1 493 ? -18.51541 9.79666   26.27007  1.000 86.62882  ? 487 ALA A C     1 
ATOM   3866 O O     . ALA A 1 493 ? -18.59930 9.05319   27.25314  1.000 86.60721  ? 487 ALA A O     1 
ATOM   3867 C CB    . ALA A 1 493 ? -18.40840 12.16743  25.46551  1.000 75.05597  ? 487 ALA A CB    1 
ATOM   3868 N N     . LYS A 1 494 ? -17.81800 9.47705   25.18297  1.000 89.63161  ? 488 LYS A N     1 
ATOM   3869 C CA    . LYS A 1 494 ? -17.11504 8.20274   25.05283  1.000 87.20233  ? 488 LYS A CA    1 
ATOM   3870 C C     . LYS A 1 494 ? -16.11111 7.99131   26.18199  1.000 89.98091  ? 488 LYS A C     1 
ATOM   3871 O O     . LYS A 1 494 ? -15.18719 8.78448   26.35971  1.000 89.72384  ? 488 LYS A O     1 
ATOM   3872 C CB    . LYS A 1 494 ? -16.39806 8.12300   23.70266  1.000 85.96971  ? 488 LYS A CB    1 
ATOM   3873 C CG    . LYS A 1 494 ? -17.12247 8.81709   22.55990  1.000 85.41400  ? 488 LYS A CG    1 
ATOM   3874 C CD    . LYS A 1 494 ? -18.13727 7.89394   21.90605  1.000 83.45939  ? 488 LYS A CD    1 
ATOM   3875 C CE    . LYS A 1 494 ? -19.31275 8.67378   21.34304  1.000 83.59719  ? 488 LYS A CE    1 
ATOM   3876 N NZ    . LYS A 1 494 ? -18.93453 9.44376   20.12603  1.000 80.30948  ? 488 LYS A NZ    1 
ATOM   3877 N N     . ASN A 1 507 ? -17.72521 0.61287   40.37743  1.000 91.50518  ? 501 ASN A N     1 
ATOM   3878 C CA    . ASN A 1 507 ? -17.32179 0.47726   38.98286  1.000 89.20525  ? 501 ASN A CA    1 
ATOM   3879 C C     . ASN A 1 507 ? -15.81662 0.66549   38.83182  1.000 87.62202  ? 501 ASN A C     1 
ATOM   3880 O O     . ASN A 1 507 ? -15.11875 0.95507   39.80322  1.000 86.23934  ? 501 ASN A O     1 
ATOM   3881 C CB    . ASN A 1 507 ? -18.07386 1.48207   38.10526  1.000 86.14741  ? 501 ASN A CB    1 
ATOM   3882 C CG    . ASN A 1 507 ? -17.42039 2.85227   38.09082  1.000 87.79052  ? 501 ASN A CG    1 
ATOM   3883 O OD1   . ASN A 1 507 ? -17.04211 3.38605   39.13426  1.000 84.24798  ? 501 ASN A OD1   1 
ATOM   3884 N ND2   . ASN A 1 507 ? -17.28563 3.42930   36.90238  1.000 87.64942  ? 501 ASN A ND2   1 
ATOM   3885 N N     . THR A 1 508 ? -15.32009 0.50054   37.60990  1.000 85.56516  ? 502 THR A N     1 
ATOM   3886 C CA    . THR A 1 508 ? -13.90488 0.67082   37.31295  1.000 80.72919  ? 502 THR A CA    1 
ATOM   3887 C C     . THR A 1 508 ? -13.68042 2.01539   36.63121  1.000 80.63281  ? 502 THR A C     1 
ATOM   3888 O O     . THR A 1 508 ? -14.43569 2.39883   35.73128  1.000 81.07129  ? 502 THR A O     1 
ATOM   3889 C CB    . THR A 1 508 ? -13.38367 -0.47669  36.44079  1.000 79.44990  ? 502 THR A CB    1 
ATOM   3890 O OG1   . THR A 1 508 ? -11.99765 -0.26600  36.14074  1.000 81.59308  ? 502 THR A OG1   1 
ATOM   3891 C CG2   . THR A 1 508 ? -14.18128 -0.59942  35.14503  1.000 80.79967  ? 502 THR A CG2   1 
ATOM   3892 N N     . VAL A 1 509 ? -12.65860 2.73723   37.08218  1.000 74.16569  ? 503 VAL A N     1 
ATOM   3893 C CA    . VAL A 1 509 ? -12.28177 4.02821   36.51801  1.000 70.08596  ? 503 VAL A CA    1 
ATOM   3894 C C     . VAL A 1 509 ? -10.91476 3.86228   35.87102  1.000 70.56683  ? 503 VAL A C     1 
ATOM   3895 O O     . VAL A 1 509 ? -9.94047  3.49995   36.54248  1.000 67.44848  ? 503 VAL A O     1 
ATOM   3896 C CB    . VAL A 1 509 ? -12.26739 5.13317   37.58425  1.000 67.95914  ? 503 VAL A CB    1 
ATOM   3897 C CG1   . VAL A 1 509 ? -12.22345 6.50286   36.92558  1.000 65.30131  ? 503 VAL A CG1   1 
ATOM   3898 C CG2   . VAL A 1 509 ? -13.48615 5.00840   38.48522  1.000 69.53016  ? 503 VAL A CG2   1 
ATOM   3899 N N     . TYR A 1 510 ? -10.84160 4.13306   34.56752  1.000 67.43164  ? 504 TYR A N     1 
ATOM   3900 C CA    . TYR A 1 510 ? -9.66299  3.76066   33.79438  1.000 60.01202  ? 504 TYR A CA    1 
ATOM   3901 C C     . TYR A 1 510 ? -8.51395  4.74914   33.94647  1.000 58.06897  ? 504 TYR A C     1 
ATOM   3902 O O     . TYR A 1 510 ? -7.35026  4.35315   33.82083  1.000 54.01584  ? 504 TYR A O     1 
ATOM   3903 C CB    . TYR A 1 510 ? -10.03117 3.62235   32.31622  1.000 65.83678  ? 504 TYR A CB    1 
ATOM   3904 C CG    . TYR A 1 510 ? -10.69672 2.30990   31.97115  1.000 69.62204  ? 504 TYR A CG    1 
ATOM   3905 C CD1   . TYR A 1 510 ? -12.00424 2.04915   32.35889  1.000 76.44543  ? 504 TYR A CD1   1 
ATOM   3906 C CD2   . TYR A 1 510 ? -10.01764 1.33131   31.25772  1.000 74.56399  ? 504 TYR A CD2   1 
ATOM   3907 C CE1   . TYR A 1 510 ? -12.61712 0.85072   32.04586  1.000 78.51573  ? 504 TYR A CE1   1 
ATOM   3908 C CE2   . TYR A 1 510 ? -10.62213 0.12942   30.94007  1.000 71.88966  ? 504 TYR A CE2   1 
ATOM   3909 C CZ    . TYR A 1 510 ? -11.92173 -0.10528  31.33653  1.000 74.48068  ? 504 TYR A CZ    1 
ATOM   3910 O OH    . TYR A 1 510 ? -12.52844 -1.29982  31.02273  1.000 78.05704  ? 504 TYR A OH    1 
ATOM   3911 N N     . LEU A 1 511 ? -8.80345  6.02178   34.20995  1.000 55.53349  ? 505 LEU A N     1 
ATOM   3912 C CA    . LEU A 1 511 ? -7.78928  7.06658   34.17360  1.000 52.94254  ? 505 LEU A CA    1 
ATOM   3913 C C     . LEU A 1 511 ? -7.84540  7.92669   35.42734  1.000 51.15276  ? 505 LEU A C     1 
ATOM   3914 O O     . LEU A 1 511 ? -8.92788  8.22419   35.94140  1.000 50.88422  ? 505 LEU A O     1 
ATOM   3915 C CB    . LEU A 1 511 ? -7.96706  7.96212   32.93710  1.000 53.38744  ? 505 LEU A CB    1 
ATOM   3916 C CG    . LEU A 1 511 ? -7.04294  7.77908   31.72904  1.000 54.03310  ? 505 LEU A CG    1 
ATOM   3917 C CD1   . LEU A 1 511 ? -6.86497  6.31488   31.36831  1.000 55.76680  ? 505 LEU A CD1   1 
ATOM   3918 C CD2   . LEU A 1 511 ? -7.58015  8.55737   30.53799  1.000 51.09506  ? 505 LEU A CD2   1 
ATOM   3919 N N     . TYR A 1 512 ? -6.66981  8.32342   35.91181  1.000 46.24543  ? 506 TYR A N     1 
ATOM   3920 C CA    . TYR A 1 512 ? -6.55169  9.37888   36.91000  1.000 47.78010  ? 506 TYR A CA    1 
ATOM   3921 C C     . TYR A 1 512 ? -6.45855  10.71011  36.17438  1.000 48.85940  ? 506 TYR A C     1 
ATOM   3922 O O     . TYR A 1 512 ? -5.58900  10.88868  35.31480  1.000 47.55234  ? 506 TYR A O     1 
ATOM   3923 C CB    . TYR A 1 512 ? -5.33013  9.16124   37.80293  1.000 49.63921  ? 506 TYR A CB    1 
ATOM   3924 C CG    . TYR A 1 512 ? -5.02006  10.33044  38.71455  1.000 49.19444  ? 506 TYR A CG    1 
ATOM   3925 C CD1   . TYR A 1 512 ? -5.66724  10.47553  39.93515  1.000 46.50739  ? 506 TYR A CD1   1 
ATOM   3926 C CD2   . TYR A 1 512 ? -4.07885  11.28754  38.35530  1.000 47.89704  ? 506 TYR A CD2   1 
ATOM   3927 C CE1   . TYR A 1 512 ? -5.38762  11.54156  40.77120  1.000 52.89059  ? 506 TYR A CE1   1 
ATOM   3928 C CE2   . TYR A 1 512 ? -3.79476  12.35676  39.18344  1.000 52.20897  ? 506 TYR A CE2   1 
ATOM   3929 C CZ    . TYR A 1 512 ? -4.45097  12.47876  40.38999  1.000 52.33944  ? 506 TYR A CZ    1 
ATOM   3930 O OH    . TYR A 1 512 ? -4.16865  13.54184  41.21729  1.000 53.35636  ? 506 TYR A OH    1 
ATOM   3931 N N     . MET A 1 513 ? -7.35180  11.64115  36.50700  1.000 47.83718  ? 507 MET A N     1 
ATOM   3932 C CA    . MET A 1 513 ? -7.52567  12.85671  35.72255  1.000 50.70314  ? 507 MET A CA    1 
ATOM   3933 C C     . MET A 1 513 ? -7.11123  14.11518  36.47764  1.000 47.14311  ? 507 MET A C     1 
ATOM   3934 O O     . MET A 1 513 ? -7.57058  15.21195  36.14353  1.000 48.18444  ? 507 MET A O     1 
ATOM   3935 C CB    . MET A 1 513 ? -8.97690  12.96808  35.26065  1.000 48.32438  ? 507 MET A CB    1 
ATOM   3936 C CG    . MET A 1 513 ? -9.52462  11.67633  34.68366  1.000 49.83793  ? 507 MET A CG    1 
ATOM   3937 S SD    . MET A 1 513 ? -9.83172  11.79198  32.91648  1.000 67.89964  ? 507 MET A SD    1 
ATOM   3938 C CE    . MET A 1 513 ? -11.51737 12.38586  32.93856  1.000 59.64174  ? 507 MET A CE    1 
ATOM   3939 N N     . GLY A 1 514 ? -6.24547  13.98401  37.48128  1.000 47.27613  ? 508 GLY A N     1 
ATOM   3940 C CA    . GLY A 1 514 ? -5.78466  15.13316  38.23404  1.000 45.61534  ? 508 GLY A CA    1 
ATOM   3941 C C     . GLY A 1 514 ? -4.59206  15.85674  37.65664  1.000 48.26403  ? 508 GLY A C     1 
ATOM   3942 O O     . GLY A 1 514 ? -4.21338  16.91381  38.16907  1.000 45.34461  ? 508 GLY A O     1 
ATOM   3943 N N     . GLY A 1 515 ? -3.98778  15.32057  36.60290  1.000 48.31973  ? 509 GLY A N     1 
ATOM   3944 C CA    . GLY A 1 515 ? -2.82857  15.92596  35.98289  1.000 46.32049  ? 509 GLY A CA    1 
ATOM   3945 C C     . GLY A 1 515 ? -1.52978  15.28357  36.43968  1.000 44.17933  ? 509 GLY A C     1 
ATOM   3946 O O     . GLY A 1 515 ? -1.47001  14.53151  37.41537  1.000 42.79445  ? 509 GLY A O     1 
ATOM   3947 N N     . LEU A 1 516 ? -0.46289  15.60120  35.70243  1.000 40.28212  ? 510 LEU A N     1 
ATOM   3948 C CA    . LEU A 1 516 ? 0.84368   15.02719  36.00849  1.000 39.60802  ? 510 LEU A CA    1 
ATOM   3949 C C     . LEU A 1 516 ? 1.38525   15.54698  37.33445  1.000 43.51128  ? 510 LEU A C     1 
ATOM   3950 O O     . LEU A 1 516 ? 1.95629   14.78093  38.11954  1.000 44.13909  ? 510 LEU A O     1 
ATOM   3951 C CB    . LEU A 1 516 ? 1.82667   15.32519  34.87748  1.000 31.07453  ? 510 LEU A CB    1 
ATOM   3952 C CG    . LEU A 1 516 ? 3.25506   14.81931  35.08952  1.000 38.04636  ? 510 LEU A CG    1 
ATOM   3953 C CD1   . LEU A 1 516 ? 3.27733   13.30668  35.26703  1.000 37.89926  ? 510 LEU A CD1   1 
ATOM   3954 C CD2   . LEU A 1 516 ? 4.15208   15.24557  33.94038  1.000 38.32116  ? 510 LEU A CD2   1 
ATOM   3955 N N     . LYS A 1 517 ? 1.21863   16.84431  37.60145  1.000 45.51067  ? 511 LYS A N     1 
ATOM   3956 C CA    . LYS A 1 517 ? 1.74216   17.41845  38.83725  1.000 41.97328  ? 511 LYS A CA    1 
ATOM   3957 C C     . LYS A 1 517 ? 1.01998   16.85603  40.05520  1.000 45.61594  ? 511 LYS A C     1 
ATOM   3958 O O     . LYS A 1 517 ? 1.65622   16.46722  41.04181  1.000 46.68450  ? 511 LYS A O     1 
ATOM   3959 C CB    . LYS A 1 517 ? 1.62822   18.94264  38.80083  1.000 45.17370  ? 511 LYS A CB    1 
ATOM   3960 C CG    . LYS A 1 517 ? 2.37700   19.64009  39.92687  1.000 50.18361  ? 511 LYS A CG    1 
ATOM   3961 C CD    . LYS A 1 517 ? 1.59622   20.82752  40.46612  1.000 53.02514  ? 511 LYS A CD    1 
ATOM   3962 C CE    . LYS A 1 517 ? 2.35662   22.12720  40.25965  1.000 56.91717  ? 511 LYS A CE    1 
ATOM   3963 N NZ    . LYS A 1 517 ? 1.70084   23.27216  40.95113  1.000 62.93342  ? 511 LYS A NZ    1 
ATOM   3964 N N     . GLU A 1 518 ? -0.31341  16.80478  40.00523  1.000 44.73518  ? 512 GLU A N     1 
ATOM   3965 C CA    . GLU A 1 518 ? -1.06843  16.27856  41.13680  1.000 47.52568  ? 512 GLU A CA    1 
ATOM   3966 C C     . GLU A 1 518 ? -0.87720  14.77540  41.29160  1.000 47.33073  ? 512 GLU A C     1 
ATOM   3967 O O     . GLU A 1 518 ? -0.93148  14.26089  42.41412  1.000 46.27634  ? 512 GLU A O     1 
ATOM   3968 C CB    . GLU A 1 518 ? -2.55111  16.61868  40.98769  1.000 45.24844  ? 512 GLU A CB    1 
ATOM   3969 C CG    . GLU A 1 518 ? -2.87152  18.09250  41.19659  1.000 50.86419  ? 512 GLU A CG    1 
ATOM   3970 C CD    . GLU A 1 518 ? -2.26406  18.65288  42.47029  1.000 56.89022  ? 512 GLU A CD    1 
ATOM   3971 O OE1   . GLU A 1 518 ? -2.37212  17.99519  43.52656  1.000 58.68264  ? 512 GLU A OE1   1 
ATOM   3972 O OE2   . GLU A 1 518 ? -1.67691  19.75375  42.41517  1.000 57.90890  ? 512 GLU A OE2   1 
ATOM   3973 N N     . TYR A 1 519 ? -0.65517  14.05679  40.18713  1.000 46.48761  ? 513 TYR A N     1 
ATOM   3974 C CA    . TYR A 1 519 ? -0.32555  12.63861  40.28964  1.000 45.47614  ? 513 TYR A CA    1 
ATOM   3975 C C     . TYR A 1 519 ? 1.01423   12.44293  40.98383  1.000 48.04855  ? 513 TYR A C     1 
ATOM   3976 O O     . TYR A 1 519 ? 1.16800   11.53879  41.81339  1.000 47.40681  ? 513 TYR A O     1 
ATOM   3977 C CB    . TYR A 1 519 ? -0.30538  11.99412  38.90362  1.000 44.23549  ? 513 TYR A CB    1 
ATOM   3978 C CG    . TYR A 1 519 ? 0.13343   10.54622  38.90789  1.000 45.93261  ? 513 TYR A CG    1 
ATOM   3979 C CD1   . TYR A 1 519 ? -0.72645  9.54074   39.33126  1.000 48.32040  ? 513 TYR A CD1   1 
ATOM   3980 C CD2   . TYR A 1 519 ? 1.40804   10.18465  38.48976  1.000 39.39270  ? 513 TYR A CD2   1 
ATOM   3981 C CE1   . TYR A 1 519 ? -0.32966  8.21538   39.33636  1.000 43.40173  ? 513 TYR A CE1   1 
ATOM   3982 C CE2   . TYR A 1 519 ? 1.81372   8.86212   38.49142  1.000 38.13823  ? 513 TYR A CE2   1 
ATOM   3983 C CZ    . TYR A 1 519 ? 0.94088   7.88201   38.91554  1.000 45.07443  ? 513 TYR A CZ    1 
ATOM   3984 O OH    . TYR A 1 519 ? 1.33875   6.56428   38.91975  1.000 41.04174  ? 513 TYR A OH    1 
ATOM   3985 N N     . ARG A 1 520 ? 1.99836   13.28286  40.65427  1.000 43.73062  ? 514 ARG A N     1 
ATOM   3986 C CA    . ARG A 1 520 ? 3.28340   13.21999  41.33906  1.000 44.87380  ? 514 ARG A CA    1 
ATOM   3987 C C     . ARG A 1 520 ? 3.15059   13.60884  42.80480  1.000 46.73078  ? 514 ARG A C     1 
ATOM   3988 O O     . ARG A 1 520 ? 3.91618   13.12311  43.64424  1.000 47.04292  ? 514 ARG A O     1 
ATOM   3989 C CB    . ARG A 1 520 ? 4.29892   14.11909  40.63336  1.000 46.97712  ? 514 ARG A CB    1 
ATOM   3990 C CG    . ARG A 1 520 ? 4.81225   13.54935  39.32070  1.000 45.87757  ? 514 ARG A CG    1 
ATOM   3991 C CD    . ARG A 1 520 ? 5.46657   14.61732  38.45981  1.000 45.67286  ? 514 ARG A CD    1 
ATOM   3992 N NE    . ARG A 1 520 ? 6.71647   15.09755  39.03685  1.000 45.96684  ? 514 ARG A NE    1 
ATOM   3993 C CZ    . ARG A 1 520 ? 7.88119   14.47270  38.92916  1.000 47.70200  ? 514 ARG A CZ    1 
ATOM   3994 N NH1   . ARG A 1 520 ? 7.99460   13.32906  38.27344  1.000 46.48327  ? 514 ARG A NH1   1 
ATOM   3995 N NH2   . ARG A 1 520 ? 8.95935   15.00833  39.49436  1.000 45.55927  ? 514 ARG A NH2   1 
ATOM   3996 N N     . ASN A 1 521 ? 2.19008   14.47788  43.13008  1.000 52.88344  ? 515 ASN A N     1 
ATOM   3997 C CA    . ASN A 1 521 ? 1.91913   14.79231  44.52874  1.000 49.39073  ? 515 ASN A CA    1 
ATOM   3998 C C     . ASN A 1 521 ? 1.33568   13.58909  45.25783  1.000 48.56484  ? 515 ASN A C     1 
ATOM   3999 O O     . ASN A 1 521 ? 1.67018   13.33833  46.42160  1.000 52.97684  ? 515 ASN A O     1 
ATOM   4000 C CB    . ASN A 1 521 ? 0.96607   15.98377  44.62533  1.000 47.14130  ? 515 ASN A CB    1 
ATOM   4001 C CG    . ASN A 1 521 ? 1.67703   17.31469  44.49091  1.000 55.34250  ? 515 ASN A CG    1 
ATOM   4002 O OD1   . ASN A 1 521 ? 2.89450   17.40142  44.64776  1.000 60.51215  ? 515 ASN A OD1   1 
ATOM   4003 N ND2   . ASN A 1 521 ? 0.91620   18.36324  44.19926  1.000 54.16352  ? 515 ASN A ND2   1 
ATOM   4004 N N     . GLN A 1 522 ? 0.46250   12.83397  44.58700  1.000 48.56360  ? 516 GLN A N     1 
ATOM   4005 C CA    . GLN A 1 522 ? -0.17836  11.68633  45.22160  1.000 50.38547  ? 516 GLN A CA    1 
ATOM   4006 C C     . GLN A 1 522 ? 0.84260   10.61568  45.58529  1.000 52.94268  ? 516 GLN A C     1 
ATOM   4007 O O     . GLN A 1 522 ? 0.88337   10.14161  46.72656  1.000 53.75165  ? 516 GLN A O     1 
ATOM   4008 C CB    . GLN A 1 522 ? -1.25322  11.11104  44.29813  1.000 51.15590  ? 516 GLN A CB    1 
ATOM   4009 C CG    . GLN A 1 522 ? -2.46740  12.00668  44.11682  1.000 54.78004  ? 516 GLN A CG    1 
ATOM   4010 C CD    . GLN A 1 522 ? -3.09757  12.40595  45.43468  1.000 58.74795  ? 516 GLN A CD    1 
ATOM   4011 O OE1   . GLN A 1 522 ? -3.58803  11.56023  46.18225  1.000 60.82373  ? 516 GLN A OE1   1 
ATOM   4012 N NE2   . GLN A 1 522 ? -3.08702  13.70094  45.72761  1.000 65.01047  ? 516 GLN A NE2   1 
ATOM   4013 N N     . ILE A 1 523 ? 1.68077   10.22132  44.62325  1.000 51.92457  ? 517 ILE A N     1 
ATOM   4014 C CA    . ILE A 1 523 ? 2.64589   9.15945   44.87667  1.000 50.98788  ? 517 ILE A CA    1 
ATOM   4015 C C     . ILE A 1 523 ? 3.79323   9.63219   45.75934  1.000 53.82334  ? 517 ILE A C     1 
ATOM   4016 O O     . ILE A 1 523 ? 4.48194   8.80395   46.36620  1.000 51.19679  ? 517 ILE A O     1 
ATOM   4017 C CB    . ILE A 1 523 ? 3.17592   8.58699   43.54912  1.000 48.79334  ? 517 ILE A CB    1 
ATOM   4018 C CG1   . ILE A 1 523 ? 4.04135   9.61860   42.82517  1.000 49.01407  ? 517 ILE A CG1   1 
ATOM   4019 C CG2   . ILE A 1 523 ? 2.02109   8.13966   42.66357  1.000 47.28644  ? 517 ILE A CG2   1 
ATOM   4020 C CD1   . ILE A 1 523 ? 4.77285   9.05678   41.63011  1.000 41.10432  ? 517 ILE A CD1   1 
ATOM   4021 N N     . SER A 1 524 ? 4.02133   10.94488  45.85131  1.000 54.05030  ? 518 SER A N     1 
ATOM   4022 C CA    . SER A 1 524 ? 5.04508   11.44754  46.76220  1.000 52.57877  ? 518 SER A CA    1 
ATOM   4023 C C     . SER A 1 524 ? 4.60223   11.30937  48.21268  1.000 56.66613  ? 518 SER A C     1 
ATOM   4024 O O     . SER A 1 524 ? 5.41022   10.96921  49.08495  1.000 54.04368  ? 518 SER A O     1 
ATOM   4025 C CB    . SER A 1 524 ? 5.37300   12.90509  46.43942  1.000 54.41891  ? 518 SER A CB    1 
ATOM   4026 O OG    . SER A 1 524 ? 5.80205   13.04743  45.09666  1.000 55.55238  ? 518 SER A OG    1 
ATOM   4027 N N     . GLU A 1 525 ? 3.32181   11.57159  48.48830  1.000 55.99009  ? 519 GLU A N     1 
ATOM   4028 C CA    . GLU A 1 525 ? 2.80333   11.40016  49.84141  1.000 58.78110  ? 519 GLU A CA    1 
ATOM   4029 C C     . GLU A 1 525 ? 2.89073   9.94556   50.28245  1.000 60.59320  ? 519 GLU A C     1 
ATOM   4030 O O     . GLU A 1 525 ? 3.12581   9.65899   51.46211  1.000 61.78528  ? 519 GLU A O     1 
ATOM   4031 C CB    . GLU A 1 525 ? 1.35942   11.89616  49.91608  1.000 58.44276  ? 519 GLU A CB    1 
ATOM   4032 C CG    . GLU A 1 525 ? 0.91933   12.32916  51.30439  1.000 69.44870  ? 519 GLU A CG    1 
ATOM   4033 C CD    . GLU A 1 525 ? -0.25639  13.28489  51.26912  1.000 76.81263  ? 519 GLU A CD    1 
ATOM   4034 O OE1   . GLU A 1 525 ? -0.44327  14.03621  52.24883  1.000 89.60687  ? 519 GLU A OE1   1 
ATOM   4035 O OE2   . GLU A 1 525 ? -0.99365  13.28484  50.26112  1.000 73.96207  ? 519 GLU A OE2   1 
ATOM   4036 N N     . VAL A 1 526 ? 2.70264   9.01278   49.34769  1.000 55.20885  ? 520 VAL A N     1 
ATOM   4037 C CA    . VAL A 1 526 ? 2.81863   7.59575   49.67558  1.000 54.84873  ? 520 VAL A CA    1 
ATOM   4038 C C     . VAL A 1 526 ? 4.25609   7.25390   50.04648  1.000 55.71668  ? 520 VAL A C     1 
ATOM   4039 O O     . VAL A 1 526 ? 4.52049   6.68195   51.11000  1.000 60.68744  ? 520 VAL A O     1 
ATOM   4040 C CB    . VAL A 1 526 ? 2.31658   6.73179   48.50479  1.000 52.46057  ? 520 VAL A CB    1 
ATOM   4041 C CG1   . VAL A 1 526 ? 2.63637   5.26589   48.75128  1.000 54.11625  ? 520 VAL A CG1   1 
ATOM   4042 C CG2   . VAL A 1 526 ? 0.82270   6.93143   48.30100  1.000 52.83916  ? 520 VAL A CG2   1 
ATOM   4043 N N     . SER A 1 527 ? 5.20795   7.61302   49.18049  1.000 52.17406  ? 521 SER A N     1 
ATOM   4044 C CA    . SER A 1 527 ? 6.60770   7.29277   49.44174  1.000 50.68694  ? 521 SER A CA    1 
ATOM   4045 C C     . SER A 1 527 ? 7.12659   7.99755   50.68846  1.000 57.42063  ? 521 SER A C     1 
ATOM   4046 O O     . SER A 1 527 ? 8.01943   7.47767   51.36742  1.000 55.12191  ? 521 SER A O     1 
ATOM   4047 C CB    . SER A 1 527 ? 7.46509   7.65939   48.23005  1.000 51.39745  ? 521 SER A CB    1 
ATOM   4048 O OG    . SER A 1 527 ? 7.26109   9.00935   47.85080  1.000 50.63514  ? 521 SER A OG    1 
ATOM   4049 N N     . ASN A 1 528 ? 6.58344   9.17363   51.00856  1.000 59.51859  ? 522 ASN A N     1 
ATOM   4050 C CA    . ASN A 1 528 ? 7.02219   9.89044   52.20096  1.000 62.51757  ? 522 ASN A CA    1 
ATOM   4051 C C     . ASN A 1 528 ? 6.43526   9.28322   53.46977  1.000 61.98766  ? 522 ASN A C     1 
ATOM   4052 O O     . ASN A 1 528 ? 7.11414   9.21941   54.50061  1.000 67.31105  ? 522 ASN A O     1 
ATOM   4053 C CB    . ASN A 1 528 ? 6.64563   11.36880  52.09526  1.000 55.84235  ? 522 ASN A CB    1 
ATOM   4054 C CG    . ASN A 1 528 ? 7.57483   12.14278  51.18156  1.000 56.81196  ? 522 ASN A CG    1 
ATOM   4055 O OD1   . ASN A 1 528 ? 8.75079   11.80577  51.04333  1.000 60.50224  ? 522 ASN A OD1   1 
ATOM   4056 N ND2   . ASN A 1 528 ? 7.05101   13.18821  50.55262  1.000 60.81987  ? 522 ASN A ND2   1 
ATOM   4057 N N     . ASN A 1 529 ? 5.18374   8.83174   53.41541  1.000 61.34506  ? 523 ASN A N     1 
ATOM   4058 C CA    . ASN A 1 529 ? 4.50687   8.25137   54.57559  1.000 60.12681  ? 523 ASN A CA    1 
ATOM   4059 C C     . ASN A 1 529 ? 4.74294   6.75286   54.69978  1.000 59.72066  ? 523 ASN A C     1 
ATOM   4060 O O     . ASN A 1 529 ? 3.81854   6.00021   55.02324  1.000 57.39443  ? 523 ASN A O     1 
ATOM   4061 C CB    . ASN A 1 529 ? 3.01505   8.56116   54.50866  1.000 61.34575  ? 523 ASN A CB    1 
ATOM   4062 C CG    . ASN A 1 529 ? 2.70238   9.99891   54.87414  1.000 68.48327  ? 523 ASN A CG    1 
ATOM   4063 O OD1   . ASN A 1 529 ? 2.32260   10.80061  54.02066  1.000 66.19365  ? 523 ASN A OD1   1 
ATOM   4064 N ND2   . ASN A 1 529 ? 2.86147   10.33281  56.14982  1.000 71.48738  ? 523 ASN A ND2   1 
ATOM   4065 N N     . ASN A 1 530 ? 5.97222   6.30043   54.44014  1.000 57.99833  ? 524 ASN A N     1 
ATOM   4066 C CA    . ASN A 1 530 ? 6.36657   4.90041   54.61703  1.000 61.34268  ? 524 ASN A CA    1 
ATOM   4067 C C     . ASN A 1 530 ? 5.51103   3.95808   53.77230  1.000 60.64390  ? 524 ASN A C     1 
ATOM   4068 O O     . ASN A 1 530 ? 5.18921   2.84317   54.18943  1.000 61.98368  ? 524 ASN A O     1 
ATOM   4069 C CB    . ASN A 1 530 ? 6.32394   4.49747   56.09258  1.000 64.67539  ? 524 ASN A CB    1 
ATOM   4070 C CG    . ASN A 1 530 ? 7.57811   4.89916   56.84029  1.000 67.44619  ? 524 ASN A CG    1 
ATOM   4071 O OD1   . ASN A 1 530 ? 7.51767   5.62329   57.83355  1.000 68.58952  ? 524 ASN A OD1   1 
ATOM   4072 N ND2   . ASN A 1 530 ? 8.72574   4.43101   56.36413  1.000 71.60504  ? 524 ASN A ND2   1 
ATOM   4073 N N     . TYR A 1 531 ? 5.14318   4.41298   52.57284  1.000 56.73013  ? 525 TYR A N     1 
ATOM   4074 C CA    . TYR A 1 531 ? 4.39166   3.60624   51.60942  1.000 55.49300  ? 525 TYR A CA    1 
ATOM   4075 C C     . TYR A 1 531 ? 3.08512   3.09210   52.21228  1.000 57.50477  ? 525 TYR A C     1 
ATOM   4076 O O     . TYR A 1 531 ? 2.80565   1.89109   52.22093  1.000 58.18440  ? 525 TYR A O     1 
ATOM   4077 C CB    . TYR A 1 531 ? 5.24925   2.45643   51.07556  1.000 51.97494  ? 525 TYR A CB    1 
ATOM   4078 C CG    . TYR A 1 531 ? 6.44609   2.93028   50.28511  1.000 51.53921  ? 525 TYR A CG    1 
ATOM   4079 C CD1   . TYR A 1 531 ? 6.29413   3.45893   49.01036  1.000 45.98750  ? 525 TYR A CD1   1 
ATOM   4080 C CD2   . TYR A 1 531 ? 7.72547   2.86820   50.82085  1.000 53.07219  ? 525 TYR A CD2   1 
ATOM   4081 C CE1   . TYR A 1 531 ? 7.38409   3.90069   48.28593  1.000 45.58203  ? 525 TYR A CE1   1 
ATOM   4082 C CE2   . TYR A 1 531 ? 8.82206   3.30950   50.10481  1.000 52.57294  ? 525 TYR A CE2   1 
ATOM   4083 C CZ    . TYR A 1 531 ? 8.64545   3.82402   48.83764  1.000 46.08312  ? 525 TYR A CZ    1 
ATOM   4084 O OH    . TYR A 1 531 ? 9.73294   4.26461   48.11913  1.000 45.39250  ? 525 TYR A OH    1 
ATOM   4085 N N     . LYS A 1 532 ? 2.28094   4.02223   52.72481  1.000 56.76068  ? 526 LYS A N     1 
ATOM   4086 C CA    . LYS A 1 532 ? 0.97934   3.66056   53.26738  1.000 52.56548  ? 526 LYS A CA    1 
ATOM   4087 C C     . LYS A 1 532 ? 0.10632   3.05706   52.17485  1.000 60.05464  ? 526 LYS A C     1 
ATOM   4088 O O     . LYS A 1 532 ? 0.13164   3.49389   51.02084  1.000 58.21658  ? 526 LYS A O     1 
ATOM   4089 C CB    . LYS A 1 532 ? 0.29981   4.88287   53.88923  1.000 54.89107  ? 526 LYS A CB    1 
ATOM   4090 C CG    . LYS A 1 532 ? 0.00647   6.01467   52.91694  1.000 59.25760  ? 526 LYS A CG    1 
ATOM   4091 C CD    . LYS A 1 532 ? -1.03016  6.96954   53.48865  1.000 59.22601  ? 526 LYS A CD    1 
ATOM   4092 C CE    . LYS A 1 532 ? -1.63108  7.85208   52.40756  1.000 62.45753  ? 526 LYS A CE    1 
ATOM   4093 N NZ    . LYS A 1 532 ? -2.56413  8.86334   52.97676  1.000 59.63321  ? 526 LYS A NZ    1 
ATOM   4094 N N     . GLY A 1 533 ? -0.66226  2.03530   52.54455  1.000 55.48902  ? 527 GLY A N     1 
ATOM   4095 C CA    . GLY A 1 533 ? -1.40350  1.25020   51.58620  1.000 57.23294  ? 527 GLY A CA    1 
ATOM   4096 C C     . GLY A 1 533 ? -0.66162  0.04497   51.05262  1.000 57.13999  ? 527 GLY A C     1 
ATOM   4097 O O     . GLY A 1 533 ? -1.28853  -0.82504  50.43446  1.000 60.66838  ? 527 GLY A O     1 
ATOM   4098 N N     . CYS A 1 534 ? 0.64720   -0.03287  51.26710  1.000 60.40540  ? 528 CYS A N     1 
ATOM   4099 C CA    . CYS A 1 534 ? 1.45414   -1.17454  50.86777  1.000 57.80875  ? 528 CYS A CA    1 
ATOM   4100 C C     . CYS A 1 534 ? 1.80713   -2.02073  52.08616  1.000 62.26423  ? 528 CYS A C     1 
ATOM   4101 O O     . CYS A 1 534 ? 1.82325   -1.54235  53.22316  1.000 61.73906  ? 528 CYS A O     1 
ATOM   4102 C CB    . CYS A 1 534 ? 2.73144   -0.71654  50.15751  1.000 59.05809  ? 528 CYS A CB    1 
ATOM   4103 S SG    . CYS A 1 534 ? 2.48354   0.59418   48.93722  1.000 62.60721  ? 528 CYS A SG    1 
ATOM   4104 N N     . LEU A 1 535 ? 2.09034   -3.29657  51.83263  1.000 65.03047  ? 529 LEU A N     1 
ATOM   4105 C CA    . LEU A 1 535 ? 2.42598   -4.25741  52.87943  1.000 62.77995  ? 529 LEU A CA    1 
ATOM   4106 C C     . LEU A 1 535 ? 3.85789   -4.72880  52.66237  1.000 65.34177  ? 529 LEU A C     1 
ATOM   4107 O O     . LEU A 1 535 ? 4.14658   -5.42379  51.68218  1.000 64.59265  ? 529 LEU A O     1 
ATOM   4108 C CB    . LEU A 1 535 ? 1.45004   -5.43267  52.87612  1.000 58.77080  ? 529 LEU A CB    1 
ATOM   4109 C CG    . LEU A 1 535 ? -0.00171  -5.07765  53.20219  1.000 57.99998  ? 529 LEU A CG    1 
ATOM   4110 C CD1   . LEU A 1 535 ? -0.87171  -6.32470  53.24457  1.000 63.57548  ? 529 LEU A CD1   1 
ATOM   4111 C CD2   . LEU A 1 535 ? -0.08792  -4.31224  54.51533  1.000 64.98149  ? 529 LEU A CD2   1 
ATOM   4112 N N     . LEU A 1 536 ? 4.74847   -4.35644  53.57869  1.000 59.81896  ? 530 LEU A N     1 
ATOM   4113 C CA    . LEU A 1 536 ? 6.16945   -4.67298  53.48023  1.000 64.41566  ? 530 LEU A CA    1 
ATOM   4114 C C     . LEU A 1 536 ? 6.47691   -5.83250  54.42223  1.000 67.68007  ? 530 LEU A C     1 
ATOM   4115 O O     . LEU A 1 536 ? 6.47206   -5.66499  55.64623  1.000 70.14006  ? 530 LEU A O     1 
ATOM   4116 C CB    . LEU A 1 536 ? 7.02359   -3.45085  53.81533  1.000 64.64591  ? 530 LEU A CB    1 
ATOM   4117 C CG    . LEU A 1 536 ? 6.85602   -2.18500  52.96552  1.000 64.15185  ? 530 LEU A CG    1 
ATOM   4118 C CD1   . LEU A 1 536 ? 6.59625   -2.52959  51.50490  1.000 58.65009  ? 530 LEU A CD1   1 
ATOM   4119 C CD2   . LEU A 1 536 ? 5.76054   -1.27708  53.51608  1.000 64.48505  ? 530 LEU A CD2   1 
ATOM   4120 N N     . LYS A 1 537 ? 6.74803   -7.00373  53.85095  1.000 65.38618  ? 531 LYS A N     1 
ATOM   4121 C CA    . LYS A 1 537 ? 7.02979   -8.20220  54.63021  1.000 66.23906  ? 531 LYS A CA    1 
ATOM   4122 C C     . LYS A 1 537 ? 8.53265   -8.36389  54.81706  1.000 67.99227  ? 531 LYS A C     1 
ATOM   4123 O O     . LYS A 1 537 ? 9.28793   -8.37846  53.84000  1.000 64.79557  ? 531 LYS A O     1 
ATOM   4124 C CB    . LYS A 1 537 ? 6.44810   -9.43990  53.94621  1.000 64.65088  ? 531 LYS A CB    1 
ATOM   4125 C CG    . LYS A 1 537 ? 4.94230   -9.39612  53.75827  1.000 67.88246  ? 531 LYS A CG    1 
ATOM   4126 C CD    . LYS A 1 537 ? 4.24430   -10.37313 54.68943  1.000 73.15782  ? 531 LYS A CD    1 
ATOM   4127 C CE    . LYS A 1 537 ? 2.73379   -10.25384 54.58028  1.000 74.02240  ? 531 LYS A CE    1 
ATOM   4128 N NZ    . LYS A 1 537 ? 2.30649   -8.84557  54.35536  1.000 66.58624  ? 531 LYS A NZ    1 
ATOM   4129 N N     . GLN A 1 538 ? 8.95834   -8.49382  56.07069  1.000 71.42587  ? 532 GLN A N     1 
ATOM   4130 C CA    . GLN A 1 538 ? 10.36960  -8.64782  56.38096  1.000 70.96160  ? 532 GLN A CA    1 
ATOM   4131 C C     . GLN A 1 538 ? 10.79642  -10.10748 56.24933  1.000 77.57889  ? 532 GLN A C     1 
ATOM   4132 O O     . GLN A 1 538 ? 9.97426   -11.02754 56.23650  1.000 78.52330  ? 532 GLN A O     1 
ATOM   4133 C CB    . GLN A 1 538 ? 10.66742  -8.13953  57.79134  1.000 74.30180  ? 532 GLN A CB    1 
ATOM   4134 C CG    . GLN A 1 538 ? 10.01418  -6.80866  58.12349  1.000 69.90160  ? 532 GLN A CG    1 
ATOM   4135 C CD    . GLN A 1 538 ? 10.89832  -5.62437  57.78610  1.000 71.79732  ? 532 GLN A CD    1 
ATOM   4136 O OE1   . GLN A 1 538 ? 12.11727  -5.75659  57.67303  1.000 70.21377  ? 532 GLN A OE1   1 
ATOM   4137 N NE2   . GLN A 1 538 ? 10.28632  -4.45701  57.62235  1.000 74.75709  ? 532 GLN A NE2   1 
ATOM   4138 N N     . SER A 1 539 ? 12.10664  -10.30965 56.15363  1.000 77.54467  ? 533 SER A N     1 
ATOM   4139 C CA    . SER A 1 539 ? 12.66702  -11.64962 56.02011  1.000 84.23569  ? 533 SER A CA    1 
ATOM   4140 C C     . SER A 1 539 ? 13.58334  -11.98308 57.19338  1.000 84.84020  ? 533 SER A C     1 
ATOM   4141 O O     . SER A 1 539 ? 14.38294  -11.15283 57.62550  1.000 83.90769  ? 533 SER A O     1 
ATOM   4142 C CB    . SER A 1 539 ? 13.43130  -11.78181 54.70125  1.000 84.12881  ? 533 SER A CB    1 
ATOM   4143 O OG    . SER A 1 539 ? 13.76968  -13.13295 54.44124  1.000 86.25038  ? 533 SER A OG    1 
HETATM 4144 P PA    . NAI B 2 .   ? -9.56962  4.06651   17.63189  1.000 55.07131  ? 601 NAI A PA    1 
HETATM 4145 O O1A   . NAI B 2 .   ? -10.17879 3.05349   18.57060  1.000 50.93176  ? 601 NAI A O1A   1 
HETATM 4146 O O2A   . NAI B 2 .   ? -9.20545  5.44291   18.13216  1.000 51.29148  ? 601 NAI A O2A   1 
HETATM 4147 O O5B   . NAI B 2 .   ? -10.54180 4.22547   16.36502  1.000 51.61868  ? 601 NAI A O5B   1 
HETATM 4148 C C5B   . NAI B 2 .   ? -11.18116 3.08430   15.80676  1.000 43.88713  ? 601 NAI A C5B   1 
HETATM 4149 C C4B   . NAI B 2 .   ? -12.02431 3.53955   14.62634  1.000 44.41837  ? 601 NAI A C4B   1 
HETATM 4150 O O4B   . NAI B 2 .   ? -12.47536 2.40358   13.88712  1.000 45.22243  ? 601 NAI A O4B   1 
HETATM 4151 C C3B   . NAI B 2 .   ? -13.25029 4.30046   15.10059  1.000 43.23317  ? 601 NAI A C3B   1 
HETATM 4152 O O3B   . NAI B 2 .   ? -13.36950 5.51661   14.35952  1.000 42.71894  ? 601 NAI A O3B   1 
HETATM 4153 C C2B   . NAI B 2 .   ? -14.41983 3.39412   14.78481  1.000 44.28180  ? 601 NAI A C2B   1 
HETATM 4154 O O2B   . NAI B 2 .   ? -15.53122 4.15681   14.30836  1.000 48.46612  ? 601 NAI A O2B   1 
HETATM 4155 C C1B   . NAI B 2 .   ? -13.88859 2.47341   13.70019  1.000 44.30827  ? 601 NAI A C1B   1 
HETATM 4156 N N9A   . NAI B 2 .   ? -14.47891 1.11820   13.80427  1.000 49.17720  ? 601 NAI A N9A   1 
HETATM 4157 C C8A   . NAI B 2 .   ? -14.21853 0.20681   14.76004  1.000 45.78876  ? 601 NAI A C8A   1 
HETATM 4158 N N7A   . NAI B 2 .   ? -14.93015 -0.93052  14.55168  1.000 45.84405  ? 601 NAI A N7A   1 
HETATM 4159 C C5A   . NAI B 2 .   ? -15.66440 -0.75047  13.43849  1.000 46.95754  ? 601 NAI A C5A   1 
HETATM 4160 C C6A   . NAI B 2 .   ? -16.63455 -1.54987  12.65572  1.000 44.81443  ? 601 NAI A C6A   1 
HETATM 4161 N N6A   . NAI B 2 .   ? -16.97115 -2.80668  13.03380  1.000 52.53908  ? 601 NAI A N6A   1 
HETATM 4162 N N1A   . NAI B 2 .   ? -17.17072 -0.98227  11.55230  1.000 42.86196  ? 601 NAI A N1A   1 
HETATM 4163 C C2A   . NAI B 2 .   ? -16.84566 0.26486   11.16469  1.000 41.10571  ? 601 NAI A C2A   1 
HETATM 4164 N N3A   . NAI B 2 .   ? -15.97426 1.04543   11.82706  1.000 42.58441  ? 601 NAI A N3A   1 
HETATM 4165 C C4A   . NAI B 2 .   ? -15.36333 0.60238   12.95099  1.000 46.26437  ? 601 NAI A C4A   1 
HETATM 4166 O O3    . NAI B 2 .   ? -8.28999  3.40077   16.92257  1.000 56.08146  ? 601 NAI A O3    1 
HETATM 4167 P PN    . NAI B 2 .   ? -6.89321  4.17577   16.75874  1.000 51.09456  ? 601 NAI A PN    1 
HETATM 4168 O O1N   . NAI B 2 .   ? -7.15345  5.41262   15.93343  1.000 39.96898  ? 601 NAI A O1N   1 
HETATM 4169 O O2N   . NAI B 2 .   ? -5.85230  3.17708   16.31495  1.000 50.93973  ? 601 NAI A O2N   1 
HETATM 4170 O O5D   . NAI B 2 .   ? -6.57307  4.61891   18.27035  1.000 54.60758  ? 601 NAI A O5D   1 
HETATM 4171 C C5D   . NAI B 2 .   ? -5.87710  3.75517   19.16512  1.000 55.12119  ? 601 NAI A C5D   1 
HETATM 4172 C C4D   . NAI B 2 .   ? -5.47567  4.55565   20.39540  1.000 61.29058  ? 601 NAI A C4D   1 
HETATM 4173 O O4D   . NAI B 2 .   ? -4.09875  4.91194   20.27320  1.000 68.33728  ? 601 NAI A O4D   1 
HETATM 4174 C C3D   . NAI B 2 .   ? -6.28718  5.83812   20.47917  1.000 63.68823  ? 601 NAI A C3D   1 
HETATM 4175 O O3D   . NAI B 2 .   ? -6.95542  5.91875   21.74106  1.000 70.55931  ? 601 NAI A O3D   1 
HETATM 4176 C C2D   . NAI B 2 .   ? -5.28877  6.96913   20.35142  1.000 63.63954  ? 601 NAI A C2D   1 
HETATM 4177 O O2D   . NAI B 2 .   ? -5.41496  7.87024   21.45478  1.000 72.28363  ? 601 NAI A O2D   1 
HETATM 4178 C C1D   . NAI B 2 .   ? -3.91328  6.32485   20.35923  1.000 64.37835  ? 601 NAI A C1D   1 
HETATM 4179 N N1N   . NAI B 2 .   ? -3.16286  6.77500   19.18912  1.000 60.10691  ? 601 NAI A N1N   1 
HETATM 4180 C C2N   . NAI B 2 .   ? -2.62944  7.99749   19.18781  1.000 57.03562  ? 601 NAI A C2N   1 
HETATM 4181 C C3N   . NAI B 2 .   ? -1.91160  8.47386   18.10042  1.000 56.74766  ? 601 NAI A C3N   1 
HETATM 4182 C C7N   . NAI B 2 .   ? -1.33468  9.85393   18.16150  1.000 57.40256  ? 601 NAI A C7N   1 
HETATM 4183 O O7N   . NAI B 2 .   ? -0.97780  10.29289  19.24052  1.000 57.32783  ? 601 NAI A O7N   1 
HETATM 4184 N N7N   . NAI B 2 .   ? -1.24148  10.56719  17.04063  1.000 52.10345  ? 601 NAI A N7N   1 
HETATM 4185 C C4N   . NAI B 2 .   ? -1.71238  7.63546   16.86075  1.000 49.10397  ? 601 NAI A C4N   1 
HETATM 4186 C C5N   . NAI B 2 .   ? -2.34510  6.33041   16.99174  1.000 51.31283  ? 601 NAI A C5N   1 
HETATM 4187 C C6N   . NAI B 2 .   ? -3.04293  5.96077   18.13522  1.000 57.35526  ? 601 NAI A C6N   1 
HETATM 4188 P PA    . FAD C 3 .   ? 4.86712   -0.03270  24.26260  1.000 30.76344  ? 602 FAD A PA    1 
HETATM 4189 O O1A   . FAD C 3 .   ? 5.69918   0.93014   23.44959  1.000 35.09346  ? 602 FAD A O1A   1 
HETATM 4190 O O2A   . FAD C 3 .   ? 3.50074   -0.45237  23.77733  1.000 37.74179  ? 602 FAD A O2A   1 
HETATM 4191 O O5B   . FAD C 3 .   ? 5.73370   -1.36280  24.49830  1.000 34.87801  ? 602 FAD A O5B   1 
HETATM 4192 C C5B   . FAD C 3 .   ? 5.09205   -2.58273  24.84889  1.000 35.14465  ? 602 FAD A C5B   1 
HETATM 4193 C C4B   . FAD C 3 .   ? 6.02376   -3.72366  24.48051  1.000 35.96351  ? 602 FAD A C4B   1 
HETATM 4194 O O4B   . FAD C 3 .   ? 5.83800   -4.82775  25.36872  1.000 36.36239  ? 602 FAD A O4B   1 
HETATM 4195 C C3B   . FAD C 3 .   ? 5.73946   -4.21600  23.06955  1.000 34.51583  ? 602 FAD A C3B   1 
HETATM 4196 O O3B   . FAD C 3 .   ? 6.92001   -4.10750  22.27051  1.000 31.90900  ? 602 FAD A O3B   1 
HETATM 4197 C C2B   . FAD C 3 .   ? 5.35811   -5.67246  23.22909  1.000 37.56391  ? 602 FAD A C2B   1 
HETATM 4198 O O2B   . FAD C 3 .   ? 5.97855   -6.46948  22.21734  1.000 34.41921  ? 602 FAD A O2B   1 
HETATM 4199 C C1B   . FAD C 3 .   ? 5.88604   -6.03312  24.60766  1.000 36.43786  ? 602 FAD A C1B   1 
HETATM 4200 N N9A   . FAD C 3 .   ? 5.07647   -7.10698  25.23134  1.000 37.76673  ? 602 FAD A N9A   1 
HETATM 4201 C C8A   . FAD C 3 .   ? 3.79389   -7.02713  25.63335  1.000 38.43456  ? 602 FAD A C8A   1 
HETATM 4202 N N7A   . FAD C 3 .   ? 3.37683   -8.21063  26.15576  1.000 37.22264  ? 602 FAD A N7A   1 
HETATM 4203 C C5A   . FAD C 3 .   ? 4.41078   -9.07086  26.08739  1.000 34.69666  ? 602 FAD A C5A   1 
HETATM 4204 C C6A   . FAD C 3 .   ? 4.66009   -10.48337 26.45985  1.000 35.98956  ? 602 FAD A C6A   1 
HETATM 4205 N N6A   . FAD C 3 .   ? 3.69054   -11.24005 27.02856  1.000 37.77365  ? 602 FAD A N6A   1 
HETATM 4206 N N1A   . FAD C 3 .   ? 5.88765   -10.99292 26.21183  1.000 39.22841  ? 602 FAD A N1A   1 
HETATM 4207 C C2A   . FAD C 3 .   ? 6.86263   -10.25665 25.64699  1.000 38.23992  ? 602 FAD A C2A   1 
HETATM 4208 N N3A   . FAD C 3 .   ? 6.70613   -8.97143  25.28474  1.000 34.52281  ? 602 FAD A N3A   1 
HETATM 4209 C C4A   . FAD C 3 .   ? 5.52521   -8.33683  25.47438  1.000 31.73528  ? 602 FAD A C4A   1 
HETATM 4210 N N1    . FAD C 3 .   ? 1.55537   9.11343   23.79121  1.000 40.11539  ? 602 FAD A N1    1 
HETATM 4211 C C2    . FAD C 3 .   ? 1.80000   10.37265  24.23015  1.000 39.89800  ? 602 FAD A C2    1 
HETATM 4212 O O2    . FAD C 3 .   ? 1.72774   10.60822  25.45465  1.000 44.51406  ? 602 FAD A O2    1 
HETATM 4213 N N3    . FAD C 3 .   ? 2.11480   11.37901  23.39945  1.000 38.24959  ? 602 FAD A N3    1 
HETATM 4214 C C4    . FAD C 3 .   ? 2.20995   11.20527  22.07766  1.000 40.49032  ? 602 FAD A C4    1 
HETATM 4215 O O4    . FAD C 3 .   ? 2.51033   12.16316  21.33870  1.000 41.29752  ? 602 FAD A O4    1 
HETATM 4216 C C4X   . FAD C 3 .   ? 1.95920   9.85642   21.51353  1.000 38.68195  ? 602 FAD A C4X   1 
HETATM 4217 N N5    . FAD C 3 .   ? 2.03560   9.60105   20.18959  1.000 41.14086  ? 602 FAD A N5    1 
HETATM 4218 C C5X   . FAD C 3 .   ? 1.79971   8.35651   19.71319  1.000 39.85066  ? 602 FAD A C5X   1 
HETATM 4219 C C6    . FAD C 3 .   ? 1.88020   8.12098   18.34645  1.000 40.97522  ? 602 FAD A C6    1 
HETATM 4220 C C7    . FAD C 3 .   ? 1.64652   6.84928   17.83796  1.000 46.48725  ? 602 FAD A C7    1 
HETATM 4221 C C7M   . FAD C 3 .   ? 1.74205   6.60278   16.35469  1.000 41.16097  ? 602 FAD A C7M   1 
HETATM 4222 C C8    . FAD C 3 .   ? 1.29781   5.73568   18.75917  1.000 43.98317  ? 602 FAD A C8    1 
HETATM 4223 C C8M   . FAD C 3 .   ? 1.03939   4.35807   18.20864  1.000 41.16279  ? 602 FAD A C8M   1 
HETATM 4224 C C9    . FAD C 3 .   ? 1.21057   5.96635   20.12796  1.000 45.94472  ? 602 FAD A C9    1 
HETATM 4225 C C9A   . FAD C 3 .   ? 1.44946   7.23827   20.63729  1.000 40.46228  ? 602 FAD A C9A   1 
HETATM 4226 N N10   . FAD C 3 .   ? 1.36825   7.47924   22.02501  1.000 39.77384  ? 602 FAD A N10   1 
HETATM 4227 C C10   . FAD C 3 .   ? 1.61283   8.79220   22.48046  1.000 38.79594  ? 602 FAD A C10   1 
HETATM 4228 C "C1'" . FAD C 3 .   ? 1.02174   6.39045   22.95265  1.000 39.66250  ? 602 FAD A "C1'" 1 
HETATM 4229 C "C2'" . FAD C 3 .   ? 2.17242   5.98748   23.88455  1.000 48.82748  ? 602 FAD A "C2'" 1 
HETATM 4230 O "O2'" . FAD C 3 .   ? 3.02245   7.09903   24.18798  1.000 43.67640  ? 602 FAD A "O2'" 1 
HETATM 4231 C "C3'" . FAD C 3 .   ? 3.06284   4.89847   23.30605  1.000 45.78479  ? 602 FAD A "C3'" 1 
HETATM 4232 O "O3'" . FAD C 3 .   ? 2.39833   3.63477   23.40387  1.000 48.28243  ? 602 FAD A "O3'" 1 
HETATM 4233 C "C4'" . FAD C 3 .   ? 4.37760   4.86997   24.08483  1.000 32.70495  ? 602 FAD A "C4'" 1 
HETATM 4234 O "O4'" . FAD C 3 .   ? 5.43491   4.40541   23.23709  1.000 38.63263  ? 602 FAD A "O4'" 1 
HETATM 4235 C "C5'" . FAD C 3 .   ? 4.30032   4.00321   25.33992  1.000 37.09202  ? 602 FAD A "C5'" 1 
HETATM 4236 O "O5'" . FAD C 3 .   ? 5.15030   2.87370   25.15890  1.000 36.55561  ? 602 FAD A "O5'" 1 
HETATM 4237 P P     . FAD C 3 .   ? 5.45179   1.81083   26.33216  1.000 31.78253  ? 602 FAD A P     1 
HETATM 4238 O O1P   . FAD C 3 .   ? 6.93448   1.52577   26.37739  1.000 27.93164  ? 602 FAD A O1P   1 
HETATM 4239 O O2P   . FAD C 3 .   ? 4.71675   2.20823   27.58946  1.000 28.97250  ? 602 FAD A O2P   1 
HETATM 4240 O O3P   . FAD C 3 .   ? 4.72413   0.48884   25.77875  1.000 33.30877  ? 602 FAD A O3P   1 
HETATM 4241 O O     . HOH D 4 .   ? -25.72506 1.82579   11.92670  1.000 52.93317  ? 701 HOH A O     1 
HETATM 4242 O O     . HOH D 4 .   ? 24.22177  -3.81927  24.79169  1.000 42.68827  ? 702 HOH A O     1 
HETATM 4243 O O     . HOH D 4 .   ? -11.25278 15.06680  -11.93642 1.000 61.44473  ? 703 HOH A O     1 
HETATM 4244 O O     . HOH D 4 .   ? -1.68272  21.38233  40.76069  1.000 58.20798  ? 704 HOH A O     1 
HETATM 4245 O O     . HOH D 4 .   ? 1.85996   22.29004  17.20628  1.000 43.67180  ? 705 HOH A O     1 
HETATM 4246 O O     . HOH D 4 .   ? -20.00331 6.70696   -1.83537  1.000 48.80722  ? 706 HOH A O     1 
HETATM 4247 O O     . HOH D 4 .   ? 10.24214  13.06557  12.28607  1.000 28.00948  ? 707 HOH A O     1 
HETATM 4248 O O     . HOH D 4 .   ? -20.62630 8.10276   10.03052  1.000 39.63546  ? 708 HOH A O     1 
HETATM 4249 O O     . HOH D 4 .   ? 21.25340  3.06163   16.50269  1.000 40.91777  ? 709 HOH A O     1 
HETATM 4250 O O     . HOH D 4 .   ? 0.50328   -1.58750  24.03806  1.000 50.73581  ? 710 HOH A O     1 
HETATM 4251 O O     . HOH D 4 .   ? 10.83739  -12.68667 14.99975  1.000 59.57319  ? 711 HOH A O     1 
HETATM 4252 O O     . HOH D 4 .   ? -14.58651 7.48973   14.94953  1.000 40.63473  ? 712 HOH A O     1 
HETATM 4253 O O     . HOH D 4 .   ? -8.36670  7.68580   18.04298  1.000 46.22282  ? 713 HOH A O     1 
HETATM 4254 O O     . HOH D 4 .   ? 8.13358   22.88541  19.24188  1.000 35.84623  ? 714 HOH A O     1 
HETATM 4255 O O     . HOH D 4 .   ? 20.14468  -9.50294  31.66130  1.000 45.43710  ? 715 HOH A O     1 
HETATM 4256 O O     . HOH D 4 .   ? 2.05323   -9.62450  50.60270  1.000 60.27798  ? 716 HOH A O     1 
HETATM 4257 O O     . HOH D 4 .   ? 19.22035  4.99546   16.09646  1.000 42.95769  ? 717 HOH A O     1 
HETATM 4258 O O     . HOH D 4 .   ? -9.19130  -8.23204  16.28290  1.000 56.05114  ? 718 HOH A O     1 
HETATM 4259 O O     . HOH D 4 .   ? 7.40866   14.76787  11.63986  1.000 29.36601  ? 719 HOH A O     1 
HETATM 4260 O O     . HOH D 4 .   ? -17.52363 -6.33805  -6.94867  1.000 37.34102  ? 720 HOH A O     1 
HETATM 4261 O O     . HOH D 4 .   ? 12.278    27.818    25.310    1.000 50.10064  ? 721 HOH A O     1 
HETATM 4262 O O     . HOH D 4 .   ? 4.39813   -4.55307  12.67467  1.000 45.07449  ? 722 HOH A O     1 
HETATM 4263 O O     . HOH D 4 .   ? -25.26438 9.98419   6.23461   1.000 53.96324  ? 723 HOH A O     1 
HETATM 4264 O O     . HOH D 4 .   ? -22.17478 15.54313  -2.11308  1.000 49.18305  ? 724 HOH A O     1 
HETATM 4265 O O     . HOH D 4 .   ? 0.87738   -5.24658  41.76006  1.000 46.83642  ? 725 HOH A O     1 
HETATM 4266 O O     . HOH D 4 .   ? -18.60242 16.18433  -3.64409  1.000 49.39550  ? 726 HOH A O     1 
HETATM 4267 O O     . HOH D 4 .   ? 1.26836   28.87044  22.28136  1.000 50.23399  ? 727 HOH A O     1 
HETATM 4268 O O     . HOH D 4 .   ? -20.39526 -4.60002  -8.49851  1.000 44.45174  ? 728 HOH A O     1 
HETATM 4269 O O     . HOH D 4 .   ? -8.88560  2.23159   -13.57381 1.000 44.84808  ? 729 HOH A O     1 
HETATM 4270 O O     . HOH D 4 .   ? -4.35949  12.89835  34.49070  1.000 51.81292  ? 730 HOH A O     1 
HETATM 4271 O O     . HOH D 4 .   ? -6.84176  31.90784  26.33381  1.000 36.15595  ? 731 HOH A O     1 
HETATM 4272 O O     . HOH D 4 .   ? -6.27003  -4.79390  42.68668  1.000 53.99255  ? 732 HOH A O     1 
HETATM 4273 O O     . HOH D 4 .   ? -25.22718 8.91220   10.34786  1.000 51.14482  ? 733 HOH A O     1 
HETATM 4274 O O     . HOH D 4 .   ? 11.31183  -3.03585  2.06022   1.000 43.07154  ? 734 HOH A O     1 
HETATM 4275 O O     . HOH D 4 .   ? 17.47662  8.47939   35.78564  1.000 37.67608  ? 735 HOH A O     1 
HETATM 4276 O O     . HOH D 4 .   ? 3.33108   23.50516  30.28443  1.000 44.82628  ? 736 HOH A O     1 
HETATM 4277 O O     . HOH D 4 .   ? 7.67087   3.26693   8.60056   1.000 52.60730  ? 737 HOH A O     1 
HETATM 4278 O O     . HOH D 4 .   ? 2.20901   26.62843  24.31064  1.000 47.40346  ? 738 HOH A O     1 
HETATM 4279 O O     . HOH D 4 .   ? 2.74129   24.63877  14.04103  1.000 27.59066  ? 739 HOH A O     1 
HETATM 4280 O O     . HOH D 4 .   ? -14.26614 3.97387   -12.34532 1.000 47.72403  ? 740 HOH A O     1 
HETATM 4281 O O     . HOH D 4 .   ? 8.24887   -7.23889  1.34060   1.000 41.78428  ? 741 HOH A O     1 
HETATM 4282 O O     . HOH D 4 .   ? 19.79511  -8.67481  23.02190  1.000 44.35251  ? 742 HOH A O     1 
HETATM 4283 O O     . HOH D 4 .   ? 13.99242  4.24868   11.83701  1.000 34.21068  ? 743 HOH A O     1 
HETATM 4284 O O     . HOH D 4 .   ? -17.42661 28.85019  19.09726  1.000 40.29854  ? 744 HOH A O     1 
HETATM 4285 O O     . HOH D 4 .   ? -3.86586  -4.99653  -4.42500  1.000 40.86227  ? 745 HOH A O     1 
HETATM 4286 O O     . HOH D 4 .   ? -10.94003 -0.70891  43.07361  1.000 55.25952  ? 746 HOH A O     1 
HETATM 4287 O O     . HOH D 4 .   ? -3.30738  29.83729  28.14670  1.000 41.42989  ? 747 HOH A O     1 
HETATM 4288 O O     . HOH D 4 .   ? 2.06435   -1.63280  31.38456  1.000 36.92592  ? 748 HOH A O     1 
HETATM 4289 O O     . HOH D 4 .   ? -8.24600  -4.99995  44.37856  1.000 55.83503  ? 749 HOH A O     1 
HETATM 4290 O O     . HOH D 4 .   ? 16.74020  11.57923  10.47758  1.000 55.41099  ? 750 HOH A O     1 
HETATM 4291 O O     . HOH D 4 .   ? -5.67730  31.52719  28.87134  1.000 44.02228  ? 751 HOH A O     1 
HETATM 4292 O O     . HOH D 4 .   ? 19.41298  6.86249   34.83109  1.000 44.36069  ? 752 HOH A O     1 
HETATM 4293 O O     . HOH D 4 .   ? -15.46007 3.30693   10.54002  1.000 43.47965  ? 753 HOH A O     1 
HETATM 4294 O O     . HOH D 4 .   ? 14.39913  30.06647  31.46620  1.000 40.93624  ? 754 HOH A O     1 
HETATM 4295 O O     . HOH D 4 .   ? -10.27683 23.51191  29.02199  1.000 39.64508  ? 755 HOH A O     1 
HETATM 4296 O O     . HOH D 4 .   ? -7.06715  -6.31515  -6.81899  1.000 34.88251  ? 756 HOH A O     1 
HETATM 4297 O O     . HOH D 4 .   ? 10.98505  13.20203  20.25490  1.000 34.30758  ? 757 HOH A O     1 
HETATM 4298 O O     . HOH D 4 .   ? -15.95345 19.21348  -1.40486  1.000 36.16648  ? 758 HOH A O     1 
HETATM 4299 O O     . HOH D 4 .   ? -19.27442 23.51977  3.06740   1.000 31.84032  ? 759 HOH A O     1 
HETATM 4300 O O     . HOH D 4 .   ? 2.61957   6.22160   -3.88704  1.000 41.19073  ? 760 HOH A O     1 
HETATM 4301 O O     . HOH D 4 .   ? -5.43585  1.25296   -12.29035 1.000 34.65571  ? 761 HOH A O     1 
HETATM 4302 O O     . HOH D 4 .   ? -11.20330 7.11296   18.35872  1.000 53.87263  ? 762 HOH A O     1 
HETATM 4303 O O     . HOH D 4 .   ? -17.44046 29.31251  30.56201  1.000 51.02477  ? 763 HOH A O     1 
HETATM 4304 O O     . HOH D 4 .   ? -19.99705 9.11990   -0.76759  1.000 42.85108  ? 764 HOH A O     1 
HETATM 4305 O O     . HOH D 4 .   ? 5.68686   7.80259   10.22333  1.000 37.99662  ? 765 HOH A O     1 
HETATM 4306 O O     . HOH D 4 .   ? 10.17653  17.31511  6.00643   1.000 35.37369  ? 766 HOH A O     1 
HETATM 4307 O O     . HOH D 4 .   ? 2.30997   -1.58275  11.65027  1.000 34.52173  ? 767 HOH A O     1 
HETATM 4308 O O     . HOH D 4 .   ? -17.80065 -10.11093 -5.59105  1.000 46.35173  ? 768 HOH A O     1 
HETATM 4309 O O     . HOH D 4 .   ? -12.13688 3.13564   -3.16124  1.000 22.78795  ? 769 HOH A O     1 
HETATM 4310 O O     . HOH D 4 .   ? -11.60860 23.16619  34.77651  1.000 58.16361  ? 770 HOH A O     1 
HETATM 4311 O O     . HOH D 4 .   ? -6.64050  24.34868  30.85369  1.000 41.03263  ? 771 HOH A O     1 
HETATM 4312 O O     . HOH D 4 .   ? -8.70065  4.78818   13.56672  1.000 35.24925  ? 772 HOH A O     1 
HETATM 4313 O O     . HOH D 4 .   ? -14.15207 11.84071  9.81601   1.000 27.41988  ? 773 HOH A O     1 
HETATM 4314 O O     . HOH D 4 .   ? 0.49606   -9.10040  26.55291  1.000 44.39157  ? 774 HOH A O     1 
HETATM 4315 O O     . HOH D 4 .   ? 12.40830  -18.76601 25.53318  1.000 56.05983  ? 775 HOH A O     1 
HETATM 4316 O O     . HOH D 4 .   ? -30.57638 0.12726   -2.28168  1.000 47.37946  ? 776 HOH A O     1 
HETATM 4317 O O     . HOH D 4 .   ? 0.69345   12.21061  9.82307   1.000 29.11291  ? 777 HOH A O     1 
HETATM 4318 O O     . HOH D 4 .   ? 7.94471   25.91083  35.94495  1.000 47.91285  ? 778 HOH A O     1 
HETATM 4319 O O     . HOH D 4 .   ? 23.51565  -4.29589  37.65616  1.000 48.96750  ? 779 HOH A O     1 
HETATM 4320 O O     . HOH D 4 .   ? -15.41226 6.13948   12.16198  1.000 35.63689  ? 780 HOH A O     1 
HETATM 4321 O O     . HOH D 4 .   ? -16.78873 3.69389   -2.91779  1.000 35.68569  ? 781 HOH A O     1 
HETATM 4322 O O     . HOH D 4 .   ? 1.30363   -3.23854  -2.38421  1.000 35.66029  ? 782 HOH A O     1 
HETATM 4323 O O     . HOH D 4 .   ? 10.34679  -3.30279  21.13244  1.000 36.82505  ? 783 HOH A O     1 
HETATM 4324 O O     . HOH D 4 .   ? 7.58630   2.78864   23.00454  1.000 28.78190  ? 784 HOH A O     1 
HETATM 4325 O O     . HOH D 4 .   ? -13.79400 10.91920  12.39835  1.000 35.48978  ? 785 HOH A O     1 
HETATM 4326 O O     . HOH D 4 .   ? 2.63580   7.10087   2.28406   1.000 44.21852  ? 786 HOH A O     1 
HETATM 4327 O O     . HOH D 4 .   ? -2.74987  12.67863  0.59117   1.000 34.73736  ? 787 HOH A O     1 
HETATM 4328 O O     . HOH D 4 .   ? 10.898    29.261    12.529    1.000 48.19361  ? 788 HOH A O     1 
HETATM 4329 O O     . HOH D 4 .   ? -22.97357 3.24635   -1.18727  1.000 39.64372  ? 789 HOH A O     1 
HETATM 4330 O O     . HOH D 4 .   ? 15.96729  20.85671  12.65917  1.000 34.26131  ? 790 HOH A O     1 
HETATM 4331 O O     . HOH D 4 .   ? -22.66985 7.51090   2.96759   1.000 41.36999  ? 791 HOH A O     1 
HETATM 4332 O O     . HOH D 4 .   ? -12.57319 -15.63518 -1.67611  1.000 45.69702  ? 792 HOH A O     1 
HETATM 4333 O O     . HOH D 4 .   ? 15.13043  10.74701  15.66380  1.000 33.71781  ? 793 HOH A O     1 
HETATM 4334 O O     . HOH D 4 .   ? -19.86024 21.58029  9.72064   1.000 39.09994  ? 794 HOH A O     1 
HETATM 4335 O O     . HOH D 4 .   ? -2.16576  1.04639   14.40174  1.000 35.08055  ? 795 HOH A O     1 
HETATM 4336 O O     . HOH D 4 .   ? 5.21735   5.12675   9.48260   1.000 34.85297  ? 796 HOH A O     1 
HETATM 4337 O O     . HOH D 4 .   ? -13.50275 2.06192   -5.49480  1.000 42.92050  ? 797 HOH A O     1 
HETATM 4338 O O     . HOH D 4 .   ? 6.05616   17.52364  40.05607  1.000 49.62441  ? 798 HOH A O     1 
HETATM 4339 O O     . HOH D 4 .   ? 9.01694   5.48500   45.80381  1.000 44.65076  ? 799 HOH A O     1 
HETATM 4340 O O     . HOH D 4 .   ? -1.81250  18.19075  38.10211  1.000 47.90792  ? 800 HOH A O     1 
HETATM 4341 O O     . HOH D 4 .   ? 4.28472   0.34380   29.53497  1.000 38.49595  ? 801 HOH A O     1 
HETATM 4342 O O     . HOH D 4 .   ? 22.58263  -1.73261  23.02323  1.000 40.67595  ? 802 HOH A O     1 
HETATM 4343 O O     . HOH D 4 .   ? -4.44643  17.29115  2.58702   1.000 30.12600  ? 803 HOH A O     1 
HETATM 4344 O O     . HOH D 4 .   ? -14.563   -6.422    -9.610    1.000 35.02402  ? 804 HOH A O     1 
HETATM 4345 O O     . HOH D 4 .   ? 20.37512  19.48939  28.39559  1.000 42.29623  ? 805 HOH A O     1 
HETATM 4346 O O     . HOH D 4 .   ? -1.16538  11.96083  7.66305   1.000 25.36324  ? 806 HOH A O     1 
HETATM 4347 O O     . HOH D 4 .   ? -17.09844 3.94379   16.54079  1.000 49.83276  ? 807 HOH A O     1 
HETATM 4348 O O     . HOH D 4 .   ? -11.50212 21.98032  30.61907  1.000 45.05702  ? 808 HOH A O     1 
HETATM 4349 O O     . HOH D 4 .   ? 3.18391   -2.35620  21.83037  1.000 39.82181  ? 809 HOH A O     1 
HETATM 4350 O O     . HOH D 4 .   ? 17.23905  12.37845  27.96016  1.000 36.21347  ? 810 HOH A O     1 
HETATM 4351 O O     . HOH D 4 .   ? -3.71070  4.70571   32.88454  1.000 44.88879  ? 811 HOH A O     1 
HETATM 4352 O O     . HOH D 4 .   ? -24.75397 14.65186  4.25271   1.000 40.62448  ? 812 HOH A O     1 
HETATM 4353 O O     . HOH D 4 .   ? 1.04758   0.23590   -7.08776  1.000 37.06356  ? 813 HOH A O     1 
HETATM 4354 O O     . HOH D 4 .   ? -0.36476  13.37201  15.99232  1.000 41.20237  ? 814 HOH A O     1 
HETATM 4355 O O     . HOH D 4 .   ? 8.83482   9.57275   40.74094  1.000 36.35466  ? 815 HOH A O     1 
HETATM 4356 O O     . HOH D 4 .   ? -8.48085  20.02352  11.18165  1.000 30.09911  ? 816 HOH A O     1 
HETATM 4357 O O     . HOH D 4 .   ? 13.45261  14.79310  14.99641  1.000 28.94868  ? 817 HOH A O     1 
HETATM 4358 O O     . HOH D 4 .   ? 0.79922   -5.07304  44.71328  1.000 47.55368  ? 818 HOH A O     1 
HETATM 4359 O O     . HOH D 4 .   ? -2.74248  28.77235  21.46077  1.000 38.47307  ? 819 HOH A O     1 
HETATM 4360 O O     . HOH D 4 .   ? 11.12328  19.12695  39.02220  1.000 57.30166  ? 820 HOH A O     1 
HETATM 4361 O O     . HOH D 4 .   ? 1.23095   21.04523  29.29203  1.000 37.71568  ? 821 HOH A O     1 
HETATM 4362 O O     . HOH D 4 .   ? 17.99584  -10.93073 22.33890  1.000 44.71742  ? 822 HOH A O     1 
HETATM 4363 O O     . HOH D 4 .   ? -8.01273  19.18221  8.05515   1.000 34.77150  ? 823 HOH A O     1 
HETATM 4364 O O     . HOH D 4 .   ? -9.56038  -11.99433 3.45758   1.000 44.96618  ? 824 HOH A O     1 
HETATM 4365 O O     . HOH D 4 .   ? -17.54332 11.87143  -0.41522  1.000 31.17105  ? 825 HOH A O     1 
HETATM 4366 O O     . HOH D 4 .   ? -3.46830  -9.06153  2.44969   1.000 38.99862  ? 826 HOH A O     1 
HETATM 4367 O O     . HOH D 4 .   ? 8.83614   -24.16374 31.07978  1.000 42.28683  ? 827 HOH A O     1 
HETATM 4368 O O     . HOH D 4 .   ? -7.29357  24.39209  3.63378   1.000 44.11888  ? 828 HOH A O     1 
HETATM 4369 O O     . HOH D 4 .   ? 16.12752  12.99911  25.00122  1.000 37.17721  ? 829 HOH A O     1 
HETATM 4370 O O     . HOH D 4 .   ? 16.54565  26.22372  31.03977  1.000 33.39625  ? 830 HOH A O     1 
HETATM 4371 O O     . HOH D 4 .   ? 0.01891   5.04512   33.75994  1.000 39.32627  ? 831 HOH A O     1 
HETATM 4372 O O     . HOH D 4 .   ? -20.08047 38.25731  23.16355  1.000 48.50071  ? 832 HOH A O     1 
HETATM 4373 O O     . HOH D 4 .   ? -20.02716 11.85239  0.70515   1.000 35.69478  ? 833 HOH A O     1 
HETATM 4374 O O     . HOH D 4 .   ? -9.18091  -7.01989  -4.96980  1.000 30.78816  ? 834 HOH A O     1 
HETATM 4375 O O     . HOH D 4 .   ? -14.71557 14.25858  10.87027  1.000 30.88601  ? 835 HOH A O     1 
HETATM 4376 O O     . HOH D 4 .   ? 4.56936   22.91197  23.61103  1.000 44.09225  ? 836 HOH A O     1 
HETATM 4377 O O     . HOH D 4 .   ? -22.96517 -2.16351  -6.70769  1.000 41.39070  ? 837 HOH A O     1 
HETATM 4378 O O     . HOH D 4 .   ? -15.09848 13.14851  -0.58645  1.000 31.87206  ? 838 HOH A O     1 
HETATM 4379 O O     . HOH D 4 .   ? -3.00391  13.72053  9.22130   1.000 29.15076  ? 839 HOH A O     1 
HETATM 4380 O O     . HOH D 4 .   ? 24.23970  5.07085   18.32670  1.000 53.86581  ? 840 HOH A O     1 
HETATM 4381 O O     . HOH D 4 .   ? 4.05132   21.21710  30.09465  1.000 40.03390  ? 841 HOH A O     1 
HETATM 4382 O O     . HOH D 4 .   ? -6.15392  1.27638   14.22500  1.000 42.36280  ? 842 HOH A O     1 
HETATM 4383 O O     . HOH D 4 .   ? -25.93708 -6.04127  -3.98528  1.000 40.56025  ? 843 HOH A O     1 
HETATM 4384 O O     . HOH D 4 .   ? -1.72254  -0.57741  -9.75587  1.000 36.84622  ? 844 HOH A O     1 
HETATM 4385 O O     . HOH D 4 .   ? 16.21881  9.24192   11.72927  1.000 46.12794  ? 845 HOH A O     1 
HETATM 4386 O O     . HOH D 4 .   ? 7.98666   -1.12801  27.17956  1.000 29.66408  ? 846 HOH A O     1 
HETATM 4387 O O     . HOH D 4 .   ? 3.95655   -8.48639  22.21922  1.000 41.77524  ? 847 HOH A O     1 
HETATM 4388 O O     . HOH D 4 .   ? 2.58650   3.85456   -4.59506  1.000 37.48253  ? 848 HOH A O     1 
HETATM 4389 O O     . HOH D 4 .   ? 0.95258   7.21388   -6.30427  1.000 39.38598  ? 849 HOH A O     1 
HETATM 4390 O O     . HOH D 4 .   ? -1.79168  6.52532   32.37269  1.000 43.65024  ? 850 HOH A O     1 
HETATM 4391 O O     . HOH D 4 .   ? -18.67022 -12.91809 1.29757   1.000 42.09236  ? 851 HOH A O     1 
HETATM 4392 O O     . HOH D 4 .   ? 15.75508  3.62877   47.53322  1.000 54.84337  ? 852 HOH A O     1 
HETATM 4393 O O     . HOH D 4 .   ? 17.95495  26.42662  9.89851   1.000 41.61750  ? 853 HOH A O     1 
HETATM 4394 O O     . HOH D 4 .   ? -0.80160  14.16322  11.06922  1.000 30.00437  ? 854 HOH A O     1 
HETATM 4395 O O     . HOH D 4 .   ? -20.25875 11.83222  15.48318  1.000 42.30529  ? 855 HOH A O     1 
HETATM 4396 O O     . HOH D 4 .   ? 2.81461   15.90172  9.19074   1.000 27.52666  ? 856 HOH A O     1 
HETATM 4397 O O     . HOH D 4 .   ? -1.51392  13.61409  13.45453  1.000 32.37535  ? 857 HOH A O     1 
HETATM 4398 O O     . HOH D 4 .   ? 3.50791   19.04327  22.66145  1.000 32.76396  ? 858 HOH A O     1 
HETATM 4399 O O     . HOH D 4 .   ? -6.14527  34.82383  16.42709  1.000 38.34624  ? 859 HOH A O     1 
HETATM 4400 O O     . HOH D 4 .   ? 10.32280  7.89398   45.25184  1.000 50.45995  ? 860 HOH A O     1 
HETATM 4401 O O     . HOH D 4 .   ? 17.85722  19.83824  30.20581  1.000 43.96419  ? 861 HOH A O     1 
HETATM 4402 O O     . HOH D 4 .   ? -2.18019  -6.69932  8.35388   1.000 41.91316  ? 862 HOH A O     1 
HETATM 4403 O O     . HOH D 4 .   ? 16.31968  -9.76489  17.42391  1.000 46.27542  ? 863 HOH A O     1 
HETATM 4404 O O     . HOH D 4 .   ? 13.67925  16.56338  33.94696  1.000 51.48074  ? 864 HOH A O     1 
HETATM 4405 O O     . HOH D 4 .   ? -16.68975 0.60076   -6.55972  1.000 37.40817  ? 865 HOH A O     1 
HETATM 4406 O O     . HOH D 4 .   ? 10.97999  15.43228  13.92086  1.000 29.09811  ? 866 HOH A O     1 
HETATM 4407 O O     . HOH D 4 .   ? 9.27964   20.27878  18.66928  1.000 33.51440  ? 867 HOH A O     1 
HETATM 4408 O O     . HOH D 4 .   ? 15.02799  29.34366  33.84868  1.000 49.17341  ? 868 HOH A O     1 
HETATM 4409 O O     . HOH D 4 .   ? 22.43242  13.52449  32.37100  1.000 49.34301  ? 869 HOH A O     1 
HETATM 4410 O O     . HOH D 4 .   ? 0.74192   19.55107  9.71944   1.000 36.10133  ? 870 HOH A O     1 
HETATM 4411 O O     . HOH D 4 .   ? -16.59768 -13.56706 -2.99356  1.000 43.70438  ? 871 HOH A O     1 
HETATM 4412 O O     . HOH D 4 .   ? 3.36617   2.16950   2.96022   1.000 39.11871  ? 872 HOH A O     1 
HETATM 4413 O O     . HOH D 4 .   ? -1.49077  20.95903  10.05976  1.000 30.95221  ? 873 HOH A O     1 
HETATM 4414 O O     . HOH D 4 .   ? -5.03648  30.12575  22.11121  1.000 36.06549  ? 874 HOH A O     1 
HETATM 4415 O O     . HOH D 4 .   ? 10.16227  12.48443  29.75005  1.000 43.22792  ? 875 HOH A O     1 
HETATM 4416 O O     . HOH D 4 .   ? -4.39848  20.42060  8.95462   1.000 31.10112  ? 876 HOH A O     1 
HETATM 4417 O O     . HOH D 4 .   ? 9.66578   26.91768  37.28240  1.000 51.70438  ? 877 HOH A O     1 
HETATM 4418 O O     . HOH D 4 .   ? 14.80358  12.60244  18.23380  1.000 38.01059  ? 878 HOH A O     1 
HETATM 4419 O O     . HOH D 4 .   ? 6.19950   25.29261  28.83542  1.000 44.73568  ? 879 HOH A O     1 
HETATM 4420 O O     . HOH D 4 .   ? 9.36229   -1.34632  -2.44337  1.000 48.40298  ? 880 HOH A O     1 
HETATM 4421 O O     . HOH D 4 .   ? -9.08635  -7.74655  26.43305  1.000 70.58320  ? 881 HOH A O     1 
HETATM 4422 O O     . HOH D 4 .   ? 4.31299   17.62367  41.95907  1.000 47.55522  ? 882 HOH A O     1 
HETATM 4423 O O     . HOH D 4 .   ? 4.74886   11.12063  9.66690   1.000 34.96495  ? 883 HOH A O     1 
HETATM 4424 O O     . HOH D 4 .   ? 18.78697  24.77397  30.06690  1.000 41.57913  ? 884 HOH A O     1 
HETATM 4425 O O     . HOH D 4 .   ? 3.16341   -4.63919  44.21630  1.000 40.55295  ? 885 HOH A O     1 
HETATM 4426 O O     . HOH D 4 .   ? -19.39768 1.54186   -6.22348  1.000 45.09694  ? 886 HOH A O     1 
HETATM 4427 O O     . HOH D 4 .   ? 0.75717   26.44289  32.35046  1.000 47.47317  ? 887 HOH A O     1 
HETATM 4428 O O     . HOH D 4 .   ? -15.70102 5.07536   -7.54959  1.000 46.74298  ? 888 HOH A O     1 
HETATM 4429 O O     . HOH D 4 .   ? -16.15734 3.99751   -10.01044 1.000 52.16891  ? 889 HOH A O     1 
HETATM 4430 O O     . HOH D 4 .   ? -20.91839 26.30787  13.74559  1.000 49.15961  ? 890 HOH A O     1 
HETATM 4431 O O     . HOH D 4 .   ? 18.68088  11.12919  35.76500  1.000 50.66530  ? 891 HOH A O     1 
HETATM 4432 O O     . HOH D 4 .   ? -15.89383 30.94019  18.32466  1.000 48.37173  ? 892 HOH A O     1 
HETATM 4433 O O     . HOH D 4 .   ? 17.35746  10.27480  13.97503  1.000 48.43727  ? 893 HOH A O     1 
HETATM 4434 O O     . HOH D 4 .   ? 20.41750  23.40533  29.29890  1.000 39.81777  ? 894 HOH A O     1 
HETATM 4435 O O     . HOH D 4 .   ? -22.84261 4.79470   -3.50680  1.000 50.46672  ? 895 HOH A O     1 
HETATM 4436 O O     . HOH D 4 .   ? -17.89134 -17.57035 2.17582   1.000 53.84174  ? 896 HOH A O     1 
HETATM 4437 O O     . HOH D 4 .   ? -4.70003  33.71985  14.54492  1.000 44.37821  ? 897 HOH A O     1 
HETATM 4438 O O     . HOH D 4 .   ? -7.58411  25.89641  6.03055   1.000 45.41543  ? 898 HOH A O     1 
HETATM 4439 O O     . HOH D 4 .   ? -14.70832 -15.86021 -3.29925  1.000 51.01378  ? 899 HOH A O     1 
HETATM 4440 O O     . HOH D 4 .   ? -21.49543 23.17532  4.95934   1.000 38.91918  ? 900 HOH A O     1 
HETATM 4441 O O     . HOH D 4 .   ? 15.46355  5.49312   10.01620  1.000 45.40735  ? 901 HOH A O     1 
HETATM 4442 O O     . HOH D 4 .   ? -13.58328 20.56865  20.89653  1.000 50.82673  ? 902 HOH A O     1 
HETATM 4443 O O     . HOH D 4 .   ? -17.79084 -17.08548 -0.10902  1.000 48.00347  ? 903 HOH A O     1 
HETATM 4444 O O     . HOH D 4 .   ? -18.24947 -14.20055 -0.73952  1.000 53.23253  ? 904 HOH A O     1 
HETATM 4445 O O     . HOH D 4 .   ? 18.11955  -6.01866  14.60998  1.000 61.10174  ? 905 HOH A O     1 
HETATM 4446 O O     . HOH D 4 .   ? -22.04479 22.90774  10.47231  1.000 48.25324  ? 906 HOH A O     1 
HETATM 4447 O O     . HOH D 4 .   ? 20.56604  6.73780   14.65055  1.000 43.98367  ? 907 HOH A O     1 
HETATM 4448 O O     . HOH D 4 .   ? -4.78140  3.67392   -13.20893 1.000 44.65071  ? 908 HOH A O     1 
HETATM 4449 O O     . HOH D 4 .   ? -25.19307 8.27905   4.07894   1.000 43.63253  ? 909 HOH A O     1 
HETATM 4450 O O     . HOH D 4 .   ? -30.88289 1.57647   -4.19813  1.000 53.95244  ? 910 HOH A O     1 
HETATM 4451 O O     . HOH D 4 .   ? -2.00068  20.60777  38.23736  1.000 46.42280  ? 911 HOH A O     1 
HETATM 4452 O O     . HOH D 4 .   ? 2.86752   13.19285  8.89676   1.000 33.51911  ? 912 HOH A O     1 
HETATM 4453 O O     . HOH D 4 .   ? 3.83955   -11.17369 18.17416  1.000 53.98703  ? 913 HOH A O     1 
HETATM 4454 O O     . HOH D 4 .   ? -4.709    29.623    6.350     1.000 44.73520  ? 914 HOH A O     1 
HETATM 4455 O O     . HOH D 4 .   ? -7.35718  -12.56103 4.98768   1.000 49.12623  ? 915 HOH A O     1 
HETATM 4456 O O     . HOH D 4 .   ? 3.11913   -9.05677  18.90789  1.000 45.89964  ? 916 HOH A O     1 
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