data_8YRB
# 
_entry.id   8YRB 
# 
_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   8YRB         pdb_00008yrb 10.2210/pdb8yrb/pdb 
WWPDB D_1300046202 ?            ?                   
# 
_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       2025-04-02 
_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                        8YRB 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-21 
_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         Huilei 
_pdbx_contact_author.name_last          Yu 
_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'                     62032.055 1   ? 
L143P,A145S,A146S,N148H,K151V,F246Y,K326C,N386S,I388K,M390I,L426F,F432L,T433A,L435S,S438I,E488K,S489C,W490R,F505L ? ? 
2 non-polymer syn 'FLAVIN-ADENINE DINUCLEOTIDE'                               785.550   1   ? ? ? ? 
3 non-polymer syn 'NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE' 745.421   1   ? ? ? ? 
4 water       nat water                                                       18.015    390 ? ? ? ? 
# 
_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
MEIKRKYISQPDVLAYLKRVADKHDLRKDIQFETGIRSAYFDEENSFWNVTTENDEKFTARFLITALGPLSSPHLPVIKG
IETFKGELHHTSRWPKDVTFSGKRVGVIGTGSTGVQVITAIASQVKHLTVFQRSAQYSVPIGNVVMSETDVAKIKENYDQ
IWENVWNSALGYGLNESTLPTMSVSAEERDKIFEKAWQEGGGFRFMFETFGDIAVDETANIEAQNFIKKKISEIVKDPFV
AKKLTPTDLYACRPLCDSGYYEIFNRDNVSLEDVKANPIVEIKEDCVVTADGVEHKLDMLICATGFDAVDGSYKRIDIRG
KDGISIKDHWKDGPNSYLGMMVSNFPNMFMVFGPNGPLANSPPIIETQVRWIADLIGYAEDHQINQIEATKDAVDNWTNT
CSDIANKTLFAKAKCRIFGANVPGKKNTVYLYMGGLKEYRNQISEVSNNNYKGCLLKQSVKKTNLIES
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MHHHHHHTQKMDFDAIIIGAGFGGLYSLKKLRDDFNLKVRAFDRATEVGGTWFWNQYPGALSDSETHLYCYSWDKELLQE
MEIKRKYISQPDVLAYLKRVADKHDLRKDIQFETGIRSAYFDEENSFWNVTTENDEKFTARFLITALGPLSSPHLPVIKG
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 'FLAVIN-ADENINE DINUCLEOTIDE'                               FAD 
3 'NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE' NDP 
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 HIS n 
1 155 LEU n 
1 156 PRO n 
1 157 VAL 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 
NDP non-polymer         . 'NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE' ? 'C21 H30 N7 O17 P3' 745.421 
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   ?   ?   ?   A . n 
A 1 9   GLN 9   3   ?   ?   ?   A . n 
A 1 10  LYS 10  4   ?   ?   ?   A . n 
A 1 11  MET 11  5   ?   ?   ?   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 HIS 154 148 148 HIS HIS A . n 
A 1 155 LEU 155 149 149 LEU LEU A . n 
A 1 156 PRO 156 150 150 PRO PRO A . n 
A 1 157 VAL 157 151 151 VAL VAL 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 ?   ?   ?   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 NDP ? ? NDP ? ? '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 FAD 1   601  601 FAD FAD A . 
C 3 NDP 1   602  602 NDP NDP A . 
D 4 HOH 1   701  332 HOH HOH A . 
D 4 HOH 2   702  214 HOH HOH A . 
D 4 HOH 3   703  230 HOH HOH A . 
D 4 HOH 4   704  309 HOH HOH A . 
D 4 HOH 5   705  146 HOH HOH A . 
D 4 HOH 6   706  218 HOH HOH A . 
D 4 HOH 7   707  31  HOH HOH A . 
D 4 HOH 8   708  164 HOH HOH A . 
D 4 HOH 9   709  140 HOH HOH A . 
D 4 HOH 10  710  138 HOH HOH A . 
D 4 HOH 11  711  254 HOH HOH A . 
D 4 HOH 12  712  315 HOH HOH A . 
D 4 HOH 13  713  161 HOH HOH A . 
D 4 HOH 14  714  193 HOH HOH A . 
D 4 HOH 15  715  402 HOH HOH A . 
D 4 HOH 16  716  306 HOH HOH A . 
D 4 HOH 17  717  109 HOH HOH A . 
D 4 HOH 18  718  67  HOH HOH A . 
D 4 HOH 19  719  275 HOH HOH A . 
D 4 HOH 20  720  128 HOH HOH A . 
D 4 HOH 21  721  261 HOH HOH A . 
D 4 HOH 22  722  256 HOH HOH A . 
D 4 HOH 23  723  21  HOH HOH A . 
D 4 HOH 24  724  73  HOH HOH A . 
D 4 HOH 25  725  400 HOH HOH A . 
D 4 HOH 26  726  2   HOH HOH A . 
D 4 HOH 27  727  116 HOH HOH A . 
D 4 HOH 28  728  200 HOH HOH A . 
D 4 HOH 29  729  100 HOH HOH A . 
D 4 HOH 30  730  167 HOH HOH A . 
D 4 HOH 31  731  127 HOH HOH A . 
D 4 HOH 32  732  7   HOH HOH A . 
D 4 HOH 33  733  158 HOH HOH A . 
D 4 HOH 34  734  86  HOH HOH A . 
D 4 HOH 35  735  29  HOH HOH A . 
D 4 HOH 36  736  190 HOH HOH A . 
D 4 HOH 37  737  37  HOH HOH A . 
D 4 HOH 38  738  182 HOH HOH A . 
D 4 HOH 39  739  102 HOH HOH A . 
D 4 HOH 40  740  288 HOH HOH A . 
D 4 HOH 41  741  74  HOH HOH A . 
D 4 HOH 42  742  79  HOH HOH A . 
D 4 HOH 43  743  209 HOH HOH A . 
D 4 HOH 44  744  43  HOH HOH A . 
D 4 HOH 45  745  294 HOH HOH A . 
D 4 HOH 46  746  27  HOH HOH A . 
D 4 HOH 47  747  153 HOH HOH A . 
D 4 HOH 48  748  185 HOH HOH A . 
D 4 HOH 49  749  235 HOH HOH A . 
D 4 HOH 50  750  236 HOH HOH A . 
D 4 HOH 51  751  113 HOH HOH A . 
D 4 HOH 52  752  125 HOH HOH A . 
D 4 HOH 53  753  337 HOH HOH A . 
D 4 HOH 54  754  42  HOH HOH A . 
D 4 HOH 55  755  119 HOH HOH A . 
D 4 HOH 56  756  250 HOH HOH A . 
D 4 HOH 57  757  85  HOH HOH A . 
D 4 HOH 58  758  304 HOH HOH A . 
D 4 HOH 59  759  35  HOH HOH A . 
D 4 HOH 60  760  293 HOH HOH A . 
D 4 HOH 61  761  150 HOH HOH A . 
D 4 HOH 62  762  24  HOH HOH A . 
D 4 HOH 63  763  126 HOH HOH A . 
D 4 HOH 64  764  229 HOH HOH A . 
D 4 HOH 65  765  135 HOH HOH A . 
D 4 HOH 66  766  122 HOH HOH A . 
D 4 HOH 67  767  157 HOH HOH A . 
D 4 HOH 68  768  98  HOH HOH A . 
D 4 HOH 69  769  61  HOH HOH A . 
D 4 HOH 70  770  11  HOH HOH A . 
D 4 HOH 71  771  272 HOH HOH A . 
D 4 HOH 72  772  137 HOH HOH A . 
D 4 HOH 73  773  131 HOH HOH A . 
D 4 HOH 74  774  46  HOH HOH A . 
D 4 HOH 75  775  196 HOH HOH A . 
D 4 HOH 76  776  69  HOH HOH A . 
D 4 HOH 77  777  147 HOH HOH A . 
D 4 HOH 78  778  342 HOH HOH A . 
D 4 HOH 79  779  144 HOH HOH A . 
D 4 HOH 80  780  50  HOH HOH A . 
D 4 HOH 81  781  78  HOH HOH A . 
D 4 HOH 82  782  33  HOH HOH A . 
D 4 HOH 83  783  264 HOH HOH A . 
D 4 HOH 84  784  179 HOH HOH A . 
D 4 HOH 85  785  17  HOH HOH A . 
D 4 HOH 86  786  313 HOH HOH A . 
D 4 HOH 87  787  55  HOH HOH A . 
D 4 HOH 88  788  405 HOH HOH A . 
D 4 HOH 89  789  3   HOH HOH A . 
D 4 HOH 90  790  297 HOH HOH A . 
D 4 HOH 91  791  82  HOH HOH A . 
D 4 HOH 92  792  9   HOH HOH A . 
D 4 HOH 93  793  81  HOH HOH A . 
D 4 HOH 94  794  325 HOH HOH A . 
D 4 HOH 95  795  70  HOH HOH A . 
D 4 HOH 96  796  110 HOH HOH A . 
D 4 HOH 97  797  223 HOH HOH A . 
D 4 HOH 98  798  155 HOH HOH A . 
D 4 HOH 99  799  51  HOH HOH A . 
D 4 HOH 100 800  219 HOH HOH A . 
D 4 HOH 101 801  189 HOH HOH A . 
D 4 HOH 102 802  6   HOH HOH A . 
D 4 HOH 103 803  248 HOH HOH A . 
D 4 HOH 104 804  373 HOH HOH A . 
D 4 HOH 105 805  47  HOH HOH A . 
D 4 HOH 106 806  129 HOH HOH A . 
D 4 HOH 107 807  307 HOH HOH A . 
D 4 HOH 108 808  280 HOH HOH A . 
D 4 HOH 109 809  72  HOH HOH A . 
D 4 HOH 110 810  64  HOH HOH A . 
D 4 HOH 111 811  312 HOH HOH A . 
D 4 HOH 112 812  112 HOH HOH A . 
D 4 HOH 113 813  5   HOH HOH A . 
D 4 HOH 114 814  377 HOH HOH A . 
D 4 HOH 115 815  83  HOH HOH A . 
D 4 HOH 116 816  84  HOH HOH A . 
D 4 HOH 117 817  403 HOH HOH A . 
D 4 HOH 118 818  1   HOH HOH A . 
D 4 HOH 119 819  28  HOH HOH A . 
D 4 HOH 120 820  18  HOH HOH A . 
D 4 HOH 121 821  45  HOH HOH A . 
D 4 HOH 122 822  62  HOH HOH A . 
D 4 HOH 123 823  57  HOH HOH A . 
D 4 HOH 124 824  97  HOH HOH A . 
D 4 HOH 125 825  221 HOH HOH A . 
D 4 HOH 126 826  322 HOH HOH A . 
D 4 HOH 127 827  231 HOH HOH A . 
D 4 HOH 128 828  283 HOH HOH A . 
D 4 HOH 129 829  107 HOH HOH A . 
D 4 HOH 130 830  166 HOH HOH A . 
D 4 HOH 131 831  141 HOH HOH A . 
D 4 HOH 132 832  118 HOH HOH A . 
D 4 HOH 133 833  181 HOH HOH A . 
D 4 HOH 134 834  75  HOH HOH A . 
D 4 HOH 135 835  274 HOH HOH A . 
D 4 HOH 136 836  281 HOH HOH A . 
D 4 HOH 137 837  222 HOH HOH A . 
D 4 HOH 138 838  263 HOH HOH A . 
D 4 HOH 139 839  255 HOH HOH A . 
D 4 HOH 140 840  187 HOH HOH A . 
D 4 HOH 141 841  401 HOH HOH A . 
D 4 HOH 142 842  95  HOH HOH A . 
D 4 HOH 143 843  178 HOH HOH A . 
D 4 HOH 144 844  101 HOH HOH A . 
D 4 HOH 145 845  234 HOH HOH A . 
D 4 HOH 146 846  163 HOH HOH A . 
D 4 HOH 147 847  173 HOH HOH A . 
D 4 HOH 148 848  139 HOH HOH A . 
D 4 HOH 149 849  26  HOH HOH A . 
D 4 HOH 150 850  349 HOH HOH A . 
D 4 HOH 151 851  212 HOH HOH A . 
D 4 HOH 152 852  343 HOH HOH A . 
D 4 HOH 153 853  99  HOH HOH A . 
D 4 HOH 154 854  13  HOH HOH A . 
D 4 HOH 155 855  87  HOH HOH A . 
D 4 HOH 156 856  123 HOH HOH A . 
D 4 HOH 157 857  383 HOH HOH A . 
D 4 HOH 158 858  160 HOH HOH A . 
D 4 HOH 159 859  299 HOH HOH A . 
D 4 HOH 160 860  65  HOH HOH A . 
D 4 HOH 161 861  228 HOH HOH A . 
D 4 HOH 162 862  39  HOH HOH A . 
D 4 HOH 163 863  278 HOH HOH A . 
D 4 HOH 164 864  165 HOH HOH A . 
D 4 HOH 165 865  124 HOH HOH A . 
D 4 HOH 166 866  358 HOH HOH A . 
D 4 HOH 167 867  237 HOH HOH A . 
D 4 HOH 168 868  60  HOH HOH A . 
D 4 HOH 169 869  148 HOH HOH A . 
D 4 HOH 170 870  188 HOH HOH A . 
D 4 HOH 171 871  4   HOH HOH A . 
D 4 HOH 172 872  240 HOH HOH A . 
D 4 HOH 173 873  227 HOH HOH A . 
D 4 HOH 174 874  56  HOH HOH A . 
D 4 HOH 175 875  268 HOH HOH A . 
D 4 HOH 176 876  344 HOH HOH A . 
D 4 HOH 177 877  63  HOH HOH A . 
D 4 HOH 178 878  130 HOH HOH A . 
D 4 HOH 179 879  211 HOH HOH A . 
D 4 HOH 180 880  10  HOH HOH A . 
D 4 HOH 181 881  145 HOH HOH A . 
D 4 HOH 182 882  134 HOH HOH A . 
D 4 HOH 183 883  208 HOH HOH A . 
D 4 HOH 184 884  136 HOH HOH A . 
D 4 HOH 185 885  25  HOH HOH A . 
D 4 HOH 186 886  241 HOH HOH A . 
D 4 HOH 187 887  77  HOH HOH A . 
D 4 HOH 188 888  105 HOH HOH A . 
D 4 HOH 189 889  106 HOH HOH A . 
D 4 HOH 190 890  20  HOH HOH A . 
D 4 HOH 191 891  108 HOH HOH A . 
D 4 HOH 192 892  48  HOH HOH A . 
D 4 HOH 193 893  348 HOH HOH A . 
D 4 HOH 194 894  411 HOH HOH A . 
D 4 HOH 195 895  44  HOH HOH A . 
D 4 HOH 196 896  197 HOH HOH A . 
D 4 HOH 197 897  339 HOH HOH A . 
D 4 HOH 198 898  317 HOH HOH A . 
D 4 HOH 199 899  356 HOH HOH A . 
D 4 HOH 200 900  265 HOH HOH A . 
D 4 HOH 201 901  247 HOH HOH A . 
D 4 HOH 202 902  310 HOH HOH A . 
D 4 HOH 203 903  232 HOH HOH A . 
D 4 HOH 204 904  30  HOH HOH A . 
D 4 HOH 205 905  36  HOH HOH A . 
D 4 HOH 206 906  249 HOH HOH A . 
D 4 HOH 207 907  104 HOH HOH A . 
D 4 HOH 208 908  59  HOH HOH A . 
D 4 HOH 209 909  22  HOH HOH A . 
D 4 HOH 210 910  338 HOH HOH A . 
D 4 HOH 211 911  336 HOH HOH A . 
D 4 HOH 212 912  171 HOH HOH A . 
D 4 HOH 213 913  76  HOH HOH A . 
D 4 HOH 214 914  91  HOH HOH A . 
D 4 HOH 215 915  19  HOH HOH A . 
D 4 HOH 216 916  162 HOH HOH A . 
D 4 HOH 217 917  172 HOH HOH A . 
D 4 HOH 218 918  115 HOH HOH A . 
D 4 HOH 219 919  58  HOH HOH A . 
D 4 HOH 220 920  32  HOH HOH A . 
D 4 HOH 221 921  68  HOH HOH A . 
D 4 HOH 222 922  340 HOH HOH A . 
D 4 HOH 223 923  205 HOH HOH A . 
D 4 HOH 224 924  385 HOH HOH A . 
D 4 HOH 225 925  210 HOH HOH A . 
D 4 HOH 226 926  226 HOH HOH A . 
D 4 HOH 227 927  80  HOH HOH A . 
D 4 HOH 228 928  408 HOH HOH A . 
D 4 HOH 229 929  276 HOH HOH A . 
D 4 HOH 230 930  103 HOH HOH A . 
D 4 HOH 231 931  404 HOH HOH A . 
D 4 HOH 232 932  149 HOH HOH A . 
D 4 HOH 233 933  357 HOH HOH A . 
D 4 HOH 234 934  327 HOH HOH A . 
D 4 HOH 235 935  285 HOH HOH A . 
D 4 HOH 236 936  176 HOH HOH A . 
D 4 HOH 237 937  23  HOH HOH A . 
D 4 HOH 238 938  398 HOH HOH A . 
D 4 HOH 239 939  15  HOH HOH A . 
D 4 HOH 240 940  270 HOH HOH A . 
D 4 HOH 241 941  399 HOH HOH A . 
D 4 HOH 242 942  330 HOH HOH A . 
D 4 HOH 243 943  366 HOH HOH A . 
D 4 HOH 244 944  12  HOH HOH A . 
D 4 HOH 245 945  331 HOH HOH A . 
D 4 HOH 246 946  175 HOH HOH A . 
D 4 HOH 247 947  120 HOH HOH A . 
D 4 HOH 248 948  391 HOH HOH A . 
D 4 HOH 249 949  132 HOH HOH A . 
D 4 HOH 250 950  34  HOH HOH A . 
D 4 HOH 251 951  365 HOH HOH A . 
D 4 HOH 252 952  379 HOH HOH A . 
D 4 HOH 253 953  259 HOH HOH A . 
D 4 HOH 254 954  93  HOH HOH A . 
D 4 HOH 255 955  195 HOH HOH A . 
D 4 HOH 256 956  191 HOH HOH A . 
D 4 HOH 257 957  252 HOH HOH A . 
D 4 HOH 258 958  71  HOH HOH A . 
D 4 HOH 259 959  14  HOH HOH A . 
D 4 HOH 260 960  245 HOH HOH A . 
D 4 HOH 261 961  198 HOH HOH A . 
D 4 HOH 262 962  53  HOH HOH A . 
D 4 HOH 263 963  111 HOH HOH A . 
D 4 HOH 264 964  361 HOH HOH A . 
D 4 HOH 265 965  303 HOH HOH A . 
D 4 HOH 266 966  289 HOH HOH A . 
D 4 HOH 267 967  266 HOH HOH A . 
D 4 HOH 268 968  8   HOH HOH A . 
D 4 HOH 269 969  298 HOH HOH A . 
D 4 HOH 270 970  170 HOH HOH A . 
D 4 HOH 271 971  89  HOH HOH A . 
D 4 HOH 272 972  260 HOH HOH A . 
D 4 HOH 273 973  238 HOH HOH A . 
D 4 HOH 274 974  353 HOH HOH A . 
D 4 HOH 275 975  242 HOH HOH A . 
D 4 HOH 276 976  318 HOH HOH A . 
D 4 HOH 277 977  201 HOH HOH A . 
D 4 HOH 278 978  92  HOH HOH A . 
D 4 HOH 279 979  204 HOH HOH A . 
D 4 HOH 280 980  117 HOH HOH A . 
D 4 HOH 281 981  96  HOH HOH A . 
D 4 HOH 282 982  277 HOH HOH A . 
D 4 HOH 283 983  287 HOH HOH A . 
D 4 HOH 284 984  156 HOH HOH A . 
D 4 HOH 285 985  151 HOH HOH A . 
D 4 HOH 286 986  220 HOH HOH A . 
D 4 HOH 287 987  38  HOH HOH A . 
D 4 HOH 288 988  233 HOH HOH A . 
D 4 HOH 289 989  291 HOH HOH A . 
D 4 HOH 290 990  66  HOH HOH A . 
D 4 HOH 291 991  168 HOH HOH A . 
D 4 HOH 292 992  407 HOH HOH A . 
D 4 HOH 293 993  88  HOH HOH A . 
D 4 HOH 294 994  269 HOH HOH A . 
D 4 HOH 295 995  368 HOH HOH A . 
D 4 HOH 296 996  251 HOH HOH A . 
D 4 HOH 297 997  262 HOH HOH A . 
D 4 HOH 298 998  369 HOH HOH A . 
D 4 HOH 299 999  345 HOH HOH A . 
D 4 HOH 300 1000 381 HOH HOH A . 
D 4 HOH 301 1001 186 HOH HOH A . 
D 4 HOH 302 1002 301 HOH HOH A . 
D 4 HOH 303 1003 412 HOH HOH A . 
D 4 HOH 304 1004 121 HOH HOH A . 
D 4 HOH 305 1005 41  HOH HOH A . 
D 4 HOH 306 1006 392 HOH HOH A . 
D 4 HOH 307 1007 329 HOH HOH A . 
D 4 HOH 308 1008 203 HOH HOH A . 
D 4 HOH 309 1009 376 HOH HOH A . 
D 4 HOH 310 1010 225 HOH HOH A . 
D 4 HOH 311 1011 367 HOH HOH A . 
D 4 HOH 312 1012 142 HOH HOH A . 
D 4 HOH 313 1013 143 HOH HOH A . 
D 4 HOH 314 1014 406 HOH HOH A . 
D 4 HOH 315 1015 302 HOH HOH A . 
D 4 HOH 316 1016 152 HOH HOH A . 
D 4 HOH 317 1017 409 HOH HOH A . 
D 4 HOH 318 1018 324 HOH HOH A . 
D 4 HOH 319 1019 396 HOH HOH A . 
D 4 HOH 320 1020 258 HOH HOH A . 
D 4 HOH 321 1021 389 HOH HOH A . 
D 4 HOH 322 1022 282 HOH HOH A . 
D 4 HOH 323 1023 296 HOH HOH A . 
D 4 HOH 324 1024 346 HOH HOH A . 
D 4 HOH 325 1025 202 HOH HOH A . 
D 4 HOH 326 1026 395 HOH HOH A . 
D 4 HOH 327 1027 328 HOH HOH A . 
D 4 HOH 328 1028 394 HOH HOH A . 
D 4 HOH 329 1029 334 HOH HOH A . 
D 4 HOH 330 1030 397 HOH HOH A . 
D 4 HOH 331 1031 351 HOH HOH A . 
D 4 HOH 332 1032 253 HOH HOH A . 
D 4 HOH 333 1033 387 HOH HOH A . 
D 4 HOH 334 1034 305 HOH HOH A . 
D 4 HOH 335 1035 410 HOH HOH A . 
D 4 HOH 336 1036 386 HOH HOH A . 
D 4 HOH 337 1037 362 HOH HOH A . 
D 4 HOH 338 1038 273 HOH HOH A . 
D 4 HOH 339 1039 90  HOH HOH A . 
D 4 HOH 340 1040 375 HOH HOH A . 
D 4 HOH 341 1041 308 HOH HOH A . 
D 4 HOH 342 1042 314 HOH HOH A . 
D 4 HOH 343 1043 359 HOH HOH A . 
D 4 HOH 344 1044 180 HOH HOH A . 
D 4 HOH 345 1045 207 HOH HOH A . 
D 4 HOH 346 1046 352 HOH HOH A . 
D 4 HOH 347 1047 292 HOH HOH A . 
D 4 HOH 348 1048 154 HOH HOH A . 
D 4 HOH 349 1049 290 HOH HOH A . 
D 4 HOH 350 1050 206 HOH HOH A . 
D 4 HOH 351 1051 239 HOH HOH A . 
D 4 HOH 352 1052 184 HOH HOH A . 
D 4 HOH 353 1053 271 HOH HOH A . 
D 4 HOH 354 1054 216 HOH HOH A . 
D 4 HOH 355 1055 300 HOH HOH A . 
D 4 HOH 356 1056 279 HOH HOH A . 
D 4 HOH 357 1057 194 HOH HOH A . 
D 4 HOH 358 1058 333 HOH HOH A . 
D 4 HOH 359 1059 177 HOH HOH A . 
D 4 HOH 360 1060 183 HOH HOH A . 
D 4 HOH 361 1061 224 HOH HOH A . 
D 4 HOH 362 1062 341 HOH HOH A . 
D 4 HOH 363 1063 49  HOH HOH A . 
D 4 HOH 364 1064 257 HOH HOH A . 
D 4 HOH 365 1065 213 HOH HOH A . 
D 4 HOH 366 1066 215 HOH HOH A . 
D 4 HOH 367 1067 133 HOH HOH A . 
D 4 HOH 368 1068 159 HOH HOH A . 
D 4 HOH 369 1069 323 HOH HOH A . 
D 4 HOH 370 1070 355 HOH HOH A . 
D 4 HOH 371 1071 382 HOH HOH A . 
D 4 HOH 372 1072 370 HOH HOH A . 
D 4 HOH 373 1073 374 HOH HOH A . 
D 4 HOH 374 1074 354 HOH HOH A . 
D 4 HOH 375 1075 384 HOH HOH A . 
D 4 HOH 376 1076 192 HOH HOH A . 
D 4 HOH 377 1077 217 HOH HOH A . 
D 4 HOH 378 1078 243 HOH HOH A . 
D 4 HOH 379 1079 316 HOH HOH A . 
D 4 HOH 380 1080 246 HOH HOH A . 
D 4 HOH 381 1081 114 HOH HOH A . 
D 4 HOH 382 1082 319 HOH HOH A . 
D 4 HOH 383 1083 284 HOH HOH A . 
D 4 HOH 384 1084 380 HOH HOH A . 
D 4 HOH 385 1085 364 HOH HOH A . 
D 4 HOH 386 1086 320 HOH HOH A . 
D 4 HOH 387 1087 199 HOH HOH A . 
D 4 HOH 388 1088 311 HOH HOH A . 
D 4 HOH 389 1089 390 HOH HOH A . 
D 4 HOH 390 1090 174 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                   96.485 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8YRB 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     53.020 
_cell.length_a_esd                 ? 
_cell.length_b                     53.220 
_cell.length_b_esd                 ? 
_cell.length_c                     100.810 
_cell.length_c_esd                 ? 
_cell.volume                       282637.920 
_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                         8YRB 
_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                   8YRB 
_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             2.42 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          49.26 
_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; 0.2 M Monosaccharides (D-Glucose; D-Mannose; D-Galactose; L-Fucose; D-Xylose; N-Acetyl-D- Glucosamine)
;
_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                          28.36 
_reflns.entry_id                                       8YRB 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.78 
_reflns.d_resolution_low                               34.18 
_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                                     53646 
_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                           99.72 
_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                          13.8 
_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                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.08682 
_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                                    1.78 
_reflns_shell.d_res_low                                     1.844 
_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                             5319 
_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                                  0.608 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.359 
_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                               35.04 
_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                                 8YRB 
_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                            1.78 
_refine.ls_d_res_low                             34.18 
_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                     53637 
_refine.ls_number_reflns_R_free                  2656 
_refine.ls_number_reflns_R_work                  50981 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.75 
_refine.ls_percent_reflns_R_free                 4.95 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1886 
_refine.ls_R_factor_R_free                       0.2269 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1866 
_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                 25.2732 
_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                            0.2533 
_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                       1.78 
_refine_hist.d_res_low                        34.18 
_refine_hist.number_atoms_solvent             390 
_refine_hist.number_atoms_total               4589 
_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        4098 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         101 
_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' ? 0.0099  ? 4301 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.0157  ? 5843 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0632  ? 630  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0098  ? 740  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 11.2762 ? 567  ? 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' 1.78 1.81  . . 158 2638 100.00 . . . . 0.2989 . . . . . . . . . . . 0.3369 
'X-RAY DIFFRACTION' 1.81 1.85  . . 155 2611 100.00 . . . . 0.2805 . . . . . . . . . . . 0.3266 
'X-RAY DIFFRACTION' 1.85 1.88  . . 132 2728 99.97  . . . . 0.2701 . . . . . . . . . . . 0.3415 
'X-RAY DIFFRACTION' 1.88 1.93  . . 115 2659 99.32  . . . . 0.2893 . . . . . . . . . . . 0.3644 
'X-RAY DIFFRACTION' 1.93 1.97  . . 148 2708 99.72  . . . . 0.2496 . . . . . . . . . . . 0.3347 
'X-RAY DIFFRACTION' 1.97 2.02  . . 131 2628 100.00 . . . . 0.2227 . . . . . . . . . . . 0.2554 
'X-RAY DIFFRACTION' 2.02 2.07  . . 122 2693 99.68  . . . . 0.2304 . . . . . . . . . . . 0.2698 
'X-RAY DIFFRACTION' 2.07 2.14  . . 119 2698 99.89  . . . . 0.2217 . . . . . . . . . . . 0.2556 
'X-RAY DIFFRACTION' 2.14 2.20  . . 166 2676 100.00 . . . . 0.1935 . . . . . . . . . . . 0.2313 
'X-RAY DIFFRACTION' 2.20 2.28  . . 129 2648 99.28  . . . . 0.2127 . . . . . . . . . . . 0.2491 
'X-RAY DIFFRACTION' 2.28 2.37  . . 129 2688 99.96  . . . . 0.1986 . . . . . . . . . . . 0.2570 
'X-RAY DIFFRACTION' 2.37 2.48  . . 128 2698 100.00 . . . . 0.1898 . . . . . . . . . . . 0.2501 
'X-RAY DIFFRACTION' 2.48 2.61  . . 154 2654 100.00 . . . . 0.1985 . . . . . . . . . . . 0.2302 
'X-RAY DIFFRACTION' 2.61 2.78  . . 163 2692 99.93  . . . . 0.1986 . . . . . . . . . . . 0.2567 
'X-RAY DIFFRACTION' 2.78 2.99  . . 152 2684 100.00 . . . . 0.1878 . . . . . . . . . . . 0.2493 
'X-RAY DIFFRACTION' 2.99 3.29  . . 118 2722 99.89  . . . . 0.1901 . . . . . . . . . . . 0.2482 
'X-RAY DIFFRACTION' 3.29 3.77  . . 138 2694 99.40  . . . . 0.1677 . . . . . . . . . . . 0.2110 
'X-RAY DIFFRACTION' 3.77 4.75  . . 155 2703 99.51  . . . . 0.1417 . . . . . . . . . . . 0.1922 
'X-RAY DIFFRACTION' 4.75 34.18 . . 144 2759 98.84  . . . . 0.1608 . . . . . . . . . . . 0.1579 
# 
_struct.entry_id                     8YRB 
_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        8YRB 
_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              8YRB 
_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 8YRB MET A 1   ? UNP A0A0A8XFY0 ?   ?   'initiating methionine' -5  1  
1 8YRB HIS A 2   ? UNP A0A0A8XFY0 ?   ?   'expression tag'        -4  2  
1 8YRB HIS A 3   ? UNP A0A0A8XFY0 ?   ?   'expression tag'        -3  3  
1 8YRB HIS A 4   ? UNP A0A0A8XFY0 ?   ?   'expression tag'        -2  4  
1 8YRB HIS A 5   ? UNP A0A0A8XFY0 ?   ?   'expression tag'        -1  5  
1 8YRB HIS A 6   ? UNP A0A0A8XFY0 ?   ?   'expression tag'        0   6  
1 8YRB HIS A 7   ? UNP A0A0A8XFY0 ?   ?   'expression tag'        1   7  
1 8YRB PRO A 149 ? UNP A0A0A8XFY0 LEU 143 'engineered mutation'   143 8  
1 8YRB SER A 151 ? UNP A0A0A8XFY0 ALA 145 'engineered mutation'   145 9  
1 8YRB SER A 152 ? UNP A0A0A8XFY0 ALA 146 'engineered mutation'   146 10 
1 8YRB HIS A 154 ? UNP A0A0A8XFY0 ASN 148 'engineered mutation'   148 11 
1 8YRB VAL A 157 ? UNP A0A0A8XFY0 LYS 151 'engineered mutation'   151 12 
1 8YRB TYR A 252 ? UNP A0A0A8XFY0 PHE 246 'engineered mutation'   246 13 
1 8YRB CYS A 332 ? UNP A0A0A8XFY0 LYS 326 'engineered mutation'   326 14 
1 8YRB SER A 392 ? UNP A0A0A8XFY0 ASN 386 'engineered mutation'   386 15 
1 8YRB LYS A 394 ? UNP A0A0A8XFY0 ILE 388 'engineered mutation'   388 16 
1 8YRB ILE A 396 ? UNP A0A0A8XFY0 MET 390 'engineered mutation'   390 17 
1 8YRB PHE A 432 ? UNP A0A0A8XFY0 LEU 426 'engineered mutation'   426 18 
1 8YRB LEU A 438 ? UNP A0A0A8XFY0 PHE 432 'engineered mutation'   432 19 
1 8YRB ALA A 439 ? UNP A0A0A8XFY0 THR 433 'engineered mutation'   433 20 
1 8YRB SER A 441 ? UNP A0A0A8XFY0 LEU 435 'engineered mutation'   435 21 
1 8YRB ILE A 444 ? UNP A0A0A8XFY0 SER 438 'engineered mutation'   438 22 
1 8YRB LYS A 494 ? UNP A0A0A8XFY0 GLU 488 'engineered mutation'   488 23 
1 8YRB CYS A 495 ? UNP A0A0A8XFY0 SER 489 'engineered mutation'   489 24 
1 8YRB ARG A 496 ? UNP A0A0A8XFY0 TRP 490 'engineered mutation'   490 25 
1 8YRB LEU A 511 ? UNP A0A0A8XFY0 PHE 505 'engineered mutation'   505 26 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
_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 203 ? VAL A 205 ? SER A 197 VAL A 199 5 ? 3  
HELX_P HELX_P10 AB1 SER A 227 ? ASN A 237 ? SER A 221 ASN A 231 1 ? 11 
HELX_P HELX_P11 AB2 ASN A 237 ? ASN A 247 ? ASN A 231 ASN A 241 1 ? 11 
HELX_P HELX_P12 AB3 PRO A 260 ? VAL A 264 ? PRO A 254 VAL A 258 5 ? 5  
HELX_P HELX_P13 AB4 SER A 265 ? GLY A 280 ? SER A 259 GLY A 274 1 ? 16 
HELX_P HELX_P14 AB5 GLY A 281 ? GLU A 288 ? GLY A 275 GLU A 282 1 ? 8  
HELX_P HELX_P15 AB6 ASP A 296 ? VAL A 315 ? ASP A 290 VAL A 309 1 ? 20 
HELX_P HELX_P16 AB7 ASP A 317 ? LEU A 324 ? ASP A 311 LEU A 318 1 ? 8  
HELX_P HELX_P17 AB8 GLY A 339 ? PHE A 344 ? GLY A 333 PHE A 338 1 ? 6  
HELX_P HELX_P18 AB9 ASP A 390 ? ARG A 395 ? ASP A 384 ARG A 389 1 ? 6  
HELX_P HELX_P19 AC1 GLY A 400 ? ILE A 404 ? GLY A 394 ILE A 398 5 ? 5  
HELX_P HELX_P20 AC2 SER A 405 ? TRP A 410 ? SER A 399 TRP A 404 1 ? 6  
HELX_P HELX_P21 AC3 ASN A 440 ? HIS A 462 ? ASN A 434 HIS A 456 1 ? 23 
HELX_P HELX_P22 AC4 THR A 470 ? LYS A 487 ? THR A 464 LYS A 481 1 ? 18 
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 ? LYS A 363 ? ILE A 353 LYS A 357 
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 PHE A 127 ? O PHE A 121 N ASP A 122 ? N ASP A 116 
AA1 6 7 N PHE A 121 ? N PHE A 115 O ARG A 399 ? O ARG A 393 
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 HIS A 169 ? N HIS A 163 O CYS A 382 ? O CYS A 376 
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 ASP A 337 ? O ASP A 331 
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                   8YRB 
_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 ALA A 140 ? ? -118.97 66.38   
2 1 SER A 145 ? ? -97.52  -148.32 
3 1 ASP A 322 ? ? -174.30 -167.85 
4 1 CYS A 326 ? ? 58.95   -177.41 
5 1 ALA A 377 ? ? -93.56  48.59   
6 1 ASP A 396 ? ? 59.30   14.26   
7 1 LYS A 486 ? ? -73.50  -134.71 
8 1 ALA A 487 ? ? 49.12   -159.39 
9 1 ASN A 523 ? ? -101.00 48.37   
# 
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 THR 2   ? A THR 8   
9  1 Y 1 A GLN 3   ? A GLN 9   
10 1 Y 1 A LYS 4   ? A LYS 10  
11 1 Y 1 A MET 5   ? A MET 11  
12 1 Y 1 A CYS 489 ? A CYS 495 
13 1 Y 1 A ARG 490 ? A ARG 496 
14 1 Y 1 A ILE 491 ? A ILE 497 
15 1 Y 1 A PHE 492 ? A PHE 498 
16 1 Y 1 A GLY 493 ? A GLY 499 
17 1 Y 1 A ALA 494 ? A ALA 500 
18 1 Y 1 A ASN 495 ? A ASN 501 
19 1 Y 1 A VAL 496 ? A VAL 502 
20 1 Y 1 A PRO 497 ? A PRO 503 
21 1 Y 1 A GLY 498 ? A GLY 504 
22 1 Y 1 A LYS 499 ? A LYS 505 
23 1 Y 1 A LYS 500 ? A LYS 506 
24 1 Y 1 A ASN 501 ? A ASN 507 
25 1 Y 1 A VAL 534 ? A VAL 540 
26 1 Y 1 A LYS 535 ? A LYS 541 
27 1 Y 1 A LYS 536 ? A LYS 542 
28 1 Y 1 A THR 537 ? A THR 543 
29 1 Y 1 A ASN 538 ? A ASN 544 
30 1 Y 1 A LEU 539 ? A LEU 545 
31 1 Y 1 A ILE 540 ? A ILE 546 
32 1 Y 1 A GLU 541 ? A GLU 547 
33 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 
NDP PA     P N S 336 
NDP O1A    O N N 337 
NDP O2A    O N N 338 
NDP O5B    O N N 339 
NDP C5B    C N N 340 
NDP C4B    C N R 341 
NDP O4B    O N N 342 
NDP C3B    C N R 343 
NDP O3B    O N N 344 
NDP C2B    C N R 345 
NDP O2B    O N N 346 
NDP C1B    C N R 347 
NDP N9A    N Y N 348 
NDP C8A    C Y N 349 
NDP N7A    N Y N 350 
NDP C5A    C Y N 351 
NDP C6A    C Y N 352 
NDP N6A    N N N 353 
NDP N1A    N Y N 354 
NDP C2A    C Y N 355 
NDP N3A    N Y N 356 
NDP C4A    C Y N 357 
NDP O3     O N N 358 
NDP PN     P N S 359 
NDP O1N    O N N 360 
NDP O2N    O N N 361 
NDP O5D    O N N 362 
NDP C5D    C N N 363 
NDP C4D    C N R 364 
NDP O4D    O N N 365 
NDP C3D    C N S 366 
NDP O3D    O N N 367 
NDP C2D    C N R 368 
NDP O2D    O N N 369 
NDP C1D    C N R 370 
NDP N1N    N N N 371 
NDP C2N    C N N 372 
NDP C3N    C N N 373 
NDP C7N    C N N 374 
NDP O7N    O N N 375 
NDP N7N    N N N 376 
NDP C4N    C N N 377 
NDP C5N    C N N 378 
NDP C6N    C N N 379 
NDP P2B    P N N 380 
NDP O1X    O N N 381 
NDP O2X    O N N 382 
NDP O3X    O N N 383 
NDP HOA2   H N N 384 
NDP H51A   H N N 385 
NDP H52A   H N N 386 
NDP H4B    H N N 387 
NDP H3B    H N N 388 
NDP HO3A   H N N 389 
NDP H2B    H N N 390 
NDP H1B    H N N 391 
NDP H8A    H N N 392 
NDP H61A   H N N 393 
NDP H62A   H N N 394 
NDP H2A    H N N 395 
NDP H21N   H N N 396 
NDP H51N   H N N 397 
NDP H52N   H N N 398 
NDP H4D    H N N 399 
NDP H3D    H N N 400 
NDP HO3N   H N N 401 
NDP H2D    H N N 402 
NDP HO2N   H N N 403 
NDP H1D    H N N 404 
NDP H2N    H N N 405 
NDP H71N   H N N 406 
NDP H72N   H N N 407 
NDP H41N   H N N 408 
NDP H42N   H N N 409 
NDP H5N    H N N 410 
NDP H6N    H N N 411 
NDP HOP2   H N N 412 
NDP HOP3   H N N 413 
PHE N      N N N 414 
PHE CA     C N S 415 
PHE C      C N N 416 
PHE O      O N N 417 
PHE CB     C N N 418 
PHE CG     C Y N 419 
PHE CD1    C Y N 420 
PHE CD2    C Y N 421 
PHE CE1    C Y N 422 
PHE CE2    C Y N 423 
PHE CZ     C Y N 424 
PHE OXT    O N N 425 
PHE H      H N N 426 
PHE H2     H N N 427 
PHE HA     H N N 428 
PHE HB2    H N N 429 
PHE HB3    H N N 430 
PHE HD1    H N N 431 
PHE HD2    H N N 432 
PHE HE1    H N N 433 
PHE HE2    H N N 434 
PHE HZ     H N N 435 
PHE HXT    H N N 436 
PRO N      N N N 437 
PRO CA     C N S 438 
PRO C      C N N 439 
PRO O      O N N 440 
PRO CB     C N N 441 
PRO CG     C N N 442 
PRO CD     C N N 443 
PRO OXT    O N N 444 
PRO H      H N N 445 
PRO HA     H N N 446 
PRO HB2    H N N 447 
PRO HB3    H N N 448 
PRO HG2    H N N 449 
PRO HG3    H N N 450 
PRO HD2    H N N 451 
PRO HD3    H N N 452 
PRO HXT    H N N 453 
SER N      N N N 454 
SER CA     C N S 455 
SER C      C N N 456 
SER O      O N N 457 
SER CB     C N N 458 
SER OG     O N N 459 
SER OXT    O N N 460 
SER H      H N N 461 
SER H2     H N N 462 
SER HA     H N N 463 
SER HB2    H N N 464 
SER HB3    H N N 465 
SER HG     H N N 466 
SER HXT    H N N 467 
THR N      N N N 468 
THR CA     C N S 469 
THR C      C N N 470 
THR O      O N N 471 
THR CB     C N R 472 
THR OG1    O N N 473 
THR CG2    C N N 474 
THR OXT    O N N 475 
THR H      H N N 476 
THR H2     H N N 477 
THR HA     H N N 478 
THR HB     H N N 479 
THR HG1    H N N 480 
THR HG21   H N N 481 
THR HG22   H N N 482 
THR HG23   H N N 483 
THR HXT    H N N 484 
TRP N      N N N 485 
TRP CA     C N S 486 
TRP C      C N N 487 
TRP O      O N N 488 
TRP CB     C N N 489 
TRP CG     C Y N 490 
TRP CD1    C Y N 491 
TRP CD2    C Y N 492 
TRP NE1    N Y N 493 
TRP CE2    C Y N 494 
TRP CE3    C Y N 495 
TRP CZ2    C Y N 496 
TRP CZ3    C Y N 497 
TRP CH2    C Y N 498 
TRP OXT    O N N 499 
TRP H      H N N 500 
TRP H2     H N N 501 
TRP HA     H N N 502 
TRP HB2    H N N 503 
TRP HB3    H N N 504 
TRP HD1    H N N 505 
TRP HE1    H N N 506 
TRP HE3    H N N 507 
TRP HZ2    H N N 508 
TRP HZ3    H N N 509 
TRP HH2    H N N 510 
TRP HXT    H N N 511 
TYR N      N N N 512 
TYR CA     C N S 513 
TYR C      C N N 514 
TYR O      O N N 515 
TYR CB     C N N 516 
TYR CG     C Y N 517 
TYR CD1    C Y N 518 
TYR CD2    C Y N 519 
TYR CE1    C Y N 520 
TYR CE2    C Y N 521 
TYR CZ     C Y N 522 
TYR OH     O N N 523 
TYR OXT    O N N 524 
TYR H      H N N 525 
TYR H2     H N N 526 
TYR HA     H N N 527 
TYR HB2    H N N 528 
TYR HB3    H N N 529 
TYR HD1    H N N 530 
TYR HD2    H N N 531 
TYR HE1    H N N 532 
TYR HE2    H N N 533 
TYR HH     H N N 534 
TYR HXT    H N N 535 
VAL N      N N N 536 
VAL CA     C N S 537 
VAL C      C N N 538 
VAL O      O N N 539 
VAL CB     C N N 540 
VAL CG1    C N N 541 
VAL CG2    C N N 542 
VAL OXT    O N N 543 
VAL H      H N N 544 
VAL H2     H N N 545 
VAL HA     H N N 546 
VAL HB     H N N 547 
VAL HG11   H N N 548 
VAL HG12   H N N 549 
VAL HG13   H N N 550 
VAL HG21   H N N 551 
VAL HG22   H N N 552 
VAL HG23   H N N 553 
VAL HXT    H N N 554 
# 
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 
NDP PA    O1A    doub N N 328 
NDP PA    O2A    sing N N 329 
NDP PA    O5B    sing N N 330 
NDP PA    O3     sing N N 331 
NDP O2A   HOA2   sing N N 332 
NDP O5B   C5B    sing N N 333 
NDP C5B   C4B    sing N N 334 
NDP C5B   H51A   sing N N 335 
NDP C5B   H52A   sing N N 336 
NDP C4B   O4B    sing N N 337 
NDP C4B   C3B    sing N N 338 
NDP C4B   H4B    sing N N 339 
NDP O4B   C1B    sing N N 340 
NDP C3B   O3B    sing N N 341 
NDP C3B   C2B    sing N N 342 
NDP C3B   H3B    sing N N 343 
NDP O3B   HO3A   sing N N 344 
NDP C2B   O2B    sing N N 345 
NDP C2B   C1B    sing N N 346 
NDP C2B   H2B    sing N N 347 
NDP O2B   P2B    sing N N 348 
NDP C1B   N9A    sing N N 349 
NDP C1B   H1B    sing N N 350 
NDP N9A   C8A    sing Y N 351 
NDP N9A   C4A    sing Y N 352 
NDP C8A   N7A    doub Y N 353 
NDP C8A   H8A    sing N N 354 
NDP N7A   C5A    sing Y N 355 
NDP C5A   C6A    sing Y N 356 
NDP C5A   C4A    doub Y N 357 
NDP C6A   N6A    sing N N 358 
NDP C6A   N1A    doub Y N 359 
NDP N6A   H61A   sing N N 360 
NDP N6A   H62A   sing N N 361 
NDP N1A   C2A    sing Y N 362 
NDP C2A   N3A    doub Y N 363 
NDP C2A   H2A    sing N N 364 
NDP N3A   C4A    sing Y N 365 
NDP O3    PN     sing N N 366 
NDP PN    O1N    doub N N 367 
NDP PN    O2N    sing N N 368 
NDP PN    O5D    sing N N 369 
NDP O2N   H21N   sing N N 370 
NDP O5D   C5D    sing N N 371 
NDP C5D   C4D    sing N N 372 
NDP C5D   H51N   sing N N 373 
NDP C5D   H52N   sing N N 374 
NDP C4D   O4D    sing N N 375 
NDP C4D   C3D    sing N N 376 
NDP C4D   H4D    sing N N 377 
NDP O4D   C1D    sing N N 378 
NDP C3D   O3D    sing N N 379 
NDP C3D   C2D    sing N N 380 
NDP C3D   H3D    sing N N 381 
NDP O3D   HO3N   sing N N 382 
NDP C2D   O2D    sing N N 383 
NDP C2D   C1D    sing N N 384 
NDP C2D   H2D    sing N N 385 
NDP O2D   HO2N   sing N N 386 
NDP C1D   N1N    sing N N 387 
NDP C1D   H1D    sing N N 388 
NDP N1N   C2N    sing N N 389 
NDP N1N   C6N    sing N N 390 
NDP C2N   C3N    doub N N 391 
NDP C2N   H2N    sing N N 392 
NDP C3N   C7N    sing N N 393 
NDP C3N   C4N    sing N N 394 
NDP C7N   O7N    doub N N 395 
NDP C7N   N7N    sing N N 396 
NDP N7N   H71N   sing N N 397 
NDP N7N   H72N   sing N N 398 
NDP C4N   C5N    sing N N 399 
NDP C4N   H41N   sing N N 400 
NDP C4N   H42N   sing N N 401 
NDP C5N   C6N    doub N N 402 
NDP C5N   H5N    sing N N 403 
NDP C6N   H6N    sing N N 404 
NDP P2B   O1X    doub N N 405 
NDP P2B   O2X    sing N N 406 
NDP P2B   O3X    sing N N 407 
NDP O2X   HOP2   sing N N 408 
NDP O3X   HOP3   sing N N 409 
PHE N     CA     sing N N 410 
PHE N     H      sing N N 411 
PHE N     H2     sing N N 412 
PHE CA    C      sing N N 413 
PHE CA    CB     sing N N 414 
PHE CA    HA     sing N N 415 
PHE C     O      doub N N 416 
PHE C     OXT    sing N N 417 
PHE CB    CG     sing N N 418 
PHE CB    HB2    sing N N 419 
PHE CB    HB3    sing N N 420 
PHE CG    CD1    doub Y N 421 
PHE CG    CD2    sing Y N 422 
PHE CD1   CE1    sing Y N 423 
PHE CD1   HD1    sing N N 424 
PHE CD2   CE2    doub Y N 425 
PHE CD2   HD2    sing N N 426 
PHE CE1   CZ     doub Y N 427 
PHE CE1   HE1    sing N N 428 
PHE CE2   CZ     sing Y N 429 
PHE CE2   HE2    sing N N 430 
PHE CZ    HZ     sing N N 431 
PHE OXT   HXT    sing N N 432 
PRO N     CA     sing N N 433 
PRO N     CD     sing N N 434 
PRO N     H      sing N N 435 
PRO CA    C      sing N N 436 
PRO CA    CB     sing N N 437 
PRO CA    HA     sing N N 438 
PRO C     O      doub N N 439 
PRO C     OXT    sing N N 440 
PRO CB    CG     sing N N 441 
PRO CB    HB2    sing N N 442 
PRO CB    HB3    sing N N 443 
PRO CG    CD     sing N N 444 
PRO CG    HG2    sing N N 445 
PRO CG    HG3    sing N N 446 
PRO CD    HD2    sing N N 447 
PRO CD    HD3    sing N N 448 
PRO OXT   HXT    sing N N 449 
SER N     CA     sing N N 450 
SER N     H      sing N N 451 
SER N     H2     sing N N 452 
SER CA    C      sing N N 453 
SER CA    CB     sing N N 454 
SER CA    HA     sing N N 455 
SER C     O      doub N N 456 
SER C     OXT    sing N N 457 
SER CB    OG     sing N N 458 
SER CB    HB2    sing N N 459 
SER CB    HB3    sing N N 460 
SER OG    HG     sing N N 461 
SER OXT   HXT    sing N N 462 
THR N     CA     sing N N 463 
THR N     H      sing N N 464 
THR N     H2     sing N N 465 
THR CA    C      sing N N 466 
THR CA    CB     sing N N 467 
THR CA    HA     sing N N 468 
THR C     O      doub N N 469 
THR C     OXT    sing N N 470 
THR CB    OG1    sing N N 471 
THR CB    CG2    sing N N 472 
THR CB    HB     sing N N 473 
THR OG1   HG1    sing N N 474 
THR CG2   HG21   sing N N 475 
THR CG2   HG22   sing N N 476 
THR CG2   HG23   sing N N 477 
THR OXT   HXT    sing N N 478 
TRP N     CA     sing N N 479 
TRP N     H      sing N N 480 
TRP N     H2     sing N N 481 
TRP CA    C      sing N N 482 
TRP CA    CB     sing N N 483 
TRP CA    HA     sing N N 484 
TRP C     O      doub N N 485 
TRP C     OXT    sing N N 486 
TRP CB    CG     sing N N 487 
TRP CB    HB2    sing N N 488 
TRP CB    HB3    sing N N 489 
TRP CG    CD1    doub Y N 490 
TRP CG    CD2    sing Y N 491 
TRP CD1   NE1    sing Y N 492 
TRP CD1   HD1    sing N N 493 
TRP CD2   CE2    doub Y N 494 
TRP CD2   CE3    sing Y N 495 
TRP NE1   CE2    sing Y N 496 
TRP NE1   HE1    sing N N 497 
TRP CE2   CZ2    sing Y N 498 
TRP CE3   CZ3    doub Y N 499 
TRP CE3   HE3    sing N N 500 
TRP CZ2   CH2    doub Y N 501 
TRP CZ2   HZ2    sing N N 502 
TRP CZ3   CH2    sing Y N 503 
TRP CZ3   HZ3    sing N N 504 
TRP CH2   HH2    sing N N 505 
TRP OXT   HXT    sing N N 506 
TYR N     CA     sing N N 507 
TYR N     H      sing N N 508 
TYR N     H2     sing N N 509 
TYR CA    C      sing N N 510 
TYR CA    CB     sing N N 511 
TYR CA    HA     sing N N 512 
TYR C     O      doub N N 513 
TYR C     OXT    sing N N 514 
TYR CB    CG     sing N N 515 
TYR CB    HB2    sing N N 516 
TYR CB    HB3    sing N N 517 
TYR CG    CD1    doub Y N 518 
TYR CG    CD2    sing Y N 519 
TYR CD1   CE1    sing Y N 520 
TYR CD1   HD1    sing N N 521 
TYR CD2   CE2    doub Y N 522 
TYR CD2   HD2    sing N N 523 
TYR CE1   CZ     doub Y N 524 
TYR CE1   HE1    sing N N 525 
TYR CE2   CZ     sing Y N 526 
TYR CE2   HE2    sing N N 527 
TYR CZ    OH     sing N N 528 
TYR OH    HH     sing N N 529 
TYR OXT   HXT    sing N N 530 
VAL N     CA     sing N N 531 
VAL N     H      sing N N 532 
VAL N     H2     sing N N 533 
VAL CA    C      sing N N 534 
VAL CA    CB     sing N N 535 
VAL CA    HA     sing N N 536 
VAL C     O      doub N N 537 
VAL C     OXT    sing N N 538 
VAL CB    CG1    sing N N 539 
VAL CB    CG2    sing N N 540 
VAL CB    HB     sing N N 541 
VAL CG1   HG11   sing N N 542 
VAL CG1   HG12   sing N N 543 
VAL CG1   HG13   sing N N 544 
VAL CG2   HG21   sing N N 545 
VAL CG2   HG22   sing N N 546 
VAL CG2   HG23   sing N N 547 
VAL OXT   HXT    sing N N 548 
# 
_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                    8YRB 
_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]   0.018861 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002144 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.018790 
_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]   0.009984 
_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     . ASP A 1 12  ? 18.40194  -18.84582 37.88899  1.000 52.18757 ? 6    ASP A N     1 
ATOM   2    C CA    . ASP A 1 12  ? 18.05578  -17.93820 38.96580  1.000 36.25786 ? 6    ASP A CA    1 
ATOM   3    C C     . ASP A 1 12  ? 18.37108  -16.50809 38.48703  1.000 42.84694 ? 6    ASP A C     1 
ATOM   4    O O     . ASP A 1 12  ? 19.44536  -16.19752 37.95010  1.000 40.17216 ? 6    ASP A O     1 
ATOM   5    C CB    . ASP A 1 12  ? 18.80500  -18.27223 40.27877  1.000 38.63934 ? 6    ASP A CB    1 
ATOM   6    C CG    . ASP A 1 12  ? 17.85007  -18.47830 41.49650  1.000 50.02855 ? 6    ASP A CG    1 
ATOM   7    O OD1   . ASP A 1 12  ? 16.99309  -17.60643 41.77069  1.000 52.65753 ? 6    ASP A OD1   1 
ATOM   8    O OD2   . ASP A 1 12  ? 17.97278  -19.50935 42.21189  1.000 57.38456 ? 6    ASP A OD2   1 
ATOM   9    N N     . PHE A 1 13  ? 17.40293  -15.63372 38.65741  1.000 37.47488 ? 7    PHE A N     1 
ATOM   10   C CA    . PHE A 1 13  ? 17.64545  -14.21365 38.50426  1.000 36.27686 ? 7    PHE A CA    1 
ATOM   11   C C     . PHE A 1 13  ? 17.03870  -13.51166 39.69457  1.000 31.51981 ? 7    PHE A C     1 
ATOM   12   O O     . PHE A 1 13  ? 16.20691  -14.07881 40.40744  1.000 33.19111 ? 7    PHE A O     1 
ATOM   13   C CB    . PHE A 1 13  ? 17.03818  -13.67317 37.21621  1.000 32.74100 ? 7    PHE A CB    1 
ATOM   14   C CG    . PHE A 1 13  ? 17.54324  -14.34689 35.99903  1.000 30.59189 ? 7    PHE A CG    1 
ATOM   15   C CD1   . PHE A 1 13  ? 18.75576  -13.98394 35.45005  1.000 34.90526 ? 7    PHE A CD1   1 
ATOM   16   C CD2   . PHE A 1 13  ? 16.79195  -15.35275 35.38368  1.000 37.08141 ? 7    PHE A CD2   1 
ATOM   17   C CE1   . PHE A 1 13  ? 19.23652  -14.60070 34.31561  1.000 36.36238 ? 7    PHE A CE1   1 
ATOM   18   C CE2   . PHE A 1 13  ? 17.25726  -15.96916 34.23502  1.000 34.57961 ? 7    PHE A CE2   1 
ATOM   19   C CZ    . PHE A 1 13  ? 18.47999  -15.60109 33.70491  1.000 34.89076 ? 7    PHE A CZ    1 
ATOM   20   N N     . ASP A 1 14  ? 17.46400  -12.26411 39.90809  1.000 32.12648 ? 8    ASP A N     1 
ATOM   21   C CA    . ASP A 1 14  ? 16.73708  -11.41515 40.84067  1.000 28.74776 ? 8    ASP A CA    1 
ATOM   22   C C     . ASP A 1 14  ? 15.41721  -10.96875 40.23778  1.000 31.00160 ? 8    ASP A C     1 
ATOM   23   O O     . ASP A 1 14  ? 14.40239  -10.87766 40.93723  1.000 31.36658 ? 8    ASP A O     1 
ATOM   24   C CB    . ASP A 1 14  ? 17.59734  -10.20207 41.22259  1.000 32.41729 ? 8    ASP A CB    1 
ATOM   25   C CG    . ASP A 1 14  ? 18.86705  -10.60362 41.94667  1.000 35.41471 ? 8    ASP A CG    1 
ATOM   26   O OD1   . ASP A 1 14  ? 18.73894  -11.20226 43.02995  1.000 42.02315 ? 8    ASP A OD1   1 
ATOM   27   O OD2   . ASP A 1 14  ? 19.98210  -10.35632 41.43617  1.000 41.10144 ? 8    ASP A OD2   1 
ATOM   28   N N     . ALA A 1 15  ? 15.41344  -10.69826 38.93186  1.000 30.26737 ? 9    ALA A N     1 
ATOM   29   C CA    . ALA A 1 15  ? 14.23650  -10.18553 38.25860  1.000 29.76277 ? 9    ALA A CA    1 
ATOM   30   C C     . ALA A 1 15  ? 14.17839  -10.73438 36.84090  1.000 25.21768 ? 9    ALA A C     1 
ATOM   31   O O     . ALA A 1 15  ? 15.19350  -10.79481 36.14494  1.000 26.93700 ? 9    ALA A O     1 
ATOM   32   C CB    . ALA A 1 15  ? 14.24875  -8.65441  38.22135  1.000 28.76110 ? 9    ALA A CB    1 
ATOM   33   N N     . ILE A 1 16  ? 12.98510  -11.14751 36.44282  1.000 24.13783 ? 10   ILE A N     1 
ATOM   34   C CA    . ILE A 1 16  ? 12.65886  -11.44726 35.04990  1.000 29.00673 ? 10   ILE A CA    1 
ATOM   35   C C     . ILE A 1 16  ? 11.70545  -10.37860 34.53712  1.000 29.63088 ? 10   ILE A C     1 
ATOM   36   O O     . ILE A 1 16  ? 10.71325  -10.05626 35.19760  1.000 25.72098 ? 10   ILE A O     1 
ATOM   37   C CB    . ILE A 1 16  ? 12.04447  -12.85119 34.89669  1.000 27.43604 ? 10   ILE A CB    1 
ATOM   38   C CG1   . ILE A 1 16  ? 13.15629  -13.90397 34.95116  1.000 32.34698 ? 10   ILE A CG1   1 
ATOM   39   C CG2   . ILE A 1 16  ? 11.19552  -12.96742 33.60118  1.000 28.36080 ? 10   ILE A CG2   1 
ATOM   40   C CD1   . ILE A 1 16  ? 12.62273  -15.32324 34.95353  1.000 33.59017 ? 10   ILE A CD1   1 
ATOM   41   N N     . ILE A 1 17  ? 11.98223  -9.86854  33.33755  1.000 26.43655 ? 11   ILE A N     1 
ATOM   42   C CA    . ILE A 1 17  ? 11.16266  -8.84119  32.70137  1.000 24.05623 ? 11   ILE A CA    1 
ATOM   43   C C     . ILE A 1 17  ? 10.53975  -9.44353  31.44768  1.000 23.33587 ? 11   ILE A C     1 
ATOM   44   O O     . ILE A 1 17  ? 11.21896  -10.14712 30.69559  1.000 28.98335 ? 11   ILE A O     1 
ATOM   45   C CB    . ILE A 1 17  ? 12.01178  -7.61634  32.32240  1.000 25.12839 ? 11   ILE A CB    1 
ATOM   46   C CG1   . ILE A 1 17  ? 12.61630  -6.94264  33.57058  1.000 25.46277 ? 11   ILE A CG1   1 
ATOM   47   C CG2   . ILE A 1 17  ? 11.16307  -6.63728  31.48186  1.000 27.21280 ? 11   ILE A CG2   1 
ATOM   48   C CD1   . ILE A 1 17  ? 13.75264  -5.98279  33.17997  1.000 25.07249 ? 11   ILE A CD1   1 
ATOM   49   N N     . ILE A 1 18  ? 9.25366   -9.19134  31.23843  1.000 22.97442 ? 12   ILE A N     1 
ATOM   50   C CA    . ILE A 1 18  ? 8.55674   -9.54573  29.99994  1.000 25.54881 ? 12   ILE A CA    1 
ATOM   51   C C     . ILE A 1 18  ? 8.31824   -8.26151  29.21170  1.000 25.17169 ? 12   ILE A C     1 
ATOM   52   O O     . ILE A 1 18  ? 7.58644   -7.38335  29.67399  1.000 25.70494 ? 12   ILE A O     1 
ATOM   53   C CB    . ILE A 1 18  ? 7.22922   -10.26027 30.28338  1.000 26.72575 ? 12   ILE A CB    1 
ATOM   54   C CG1   . ILE A 1 18  ? 7.41846   -11.32333 31.37389  1.000 28.52588 ? 12   ILE A CG1   1 
ATOM   55   C CG2   . ILE A 1 18  ? 6.59985   -10.78948 29.00020  1.000 26.25411 ? 12   ILE A CG2   1 
ATOM   56   C CD1   . ILE A 1 18  ? 6.20385   -12.20213 31.56621  1.000 27.76699 ? 12   ILE A CD1   1 
ATOM   57   N N     . GLY A 1 19  ? 8.91974   -8.16258  28.03214  1.000 27.99194 ? 13   GLY A N     1 
ATOM   58   C CA    . GLY A 1 19  ? 8.70062   -7.02011  27.15341  1.000 25.58566 ? 13   GLY A CA    1 
ATOM   59   C C     . GLY A 1 19  ? 10.00485  -6.28113  26.95901  1.000 24.58385 ? 13   GLY A C     1 
ATOM   60   O O     . GLY A 1 19  ? 10.78755  -6.12902  27.89952  1.000 23.55739 ? 13   GLY A O     1 
ATOM   61   N N     . ALA A 1 20  ? 10.26555  -5.84384  25.71189  1.000 22.73331 ? 14   ALA A N     1 
ATOM   62   C CA    . ALA A 1 20  ? 11.46699  -5.07936  25.40245  1.000 23.89704 ? 14   ALA A CA    1 
ATOM   63   C C     . ALA A 1 20  ? 11.12238  -3.82215  24.61248  1.000 22.42225 ? 14   ALA A C     1 
ATOM   64   O O     . ALA A 1 20  ? 11.89582  -3.41219  23.75455  1.000 22.82108 ? 14   ALA A O     1 
ATOM   65   C CB    . ALA A 1 20  ? 12.49734  -5.92011  24.64008  1.000 23.57446 ? 14   ALA A CB    1 
ATOM   66   N N     . GLY A 1 21  ? 9.96255   -3.22301  24.90463  1.000 19.56242 ? 15   GLY A N     1 
ATOM   67   C CA    . GLY A 1 21  ? 9.59442   -1.91405  24.41104  1.000 22.06090 ? 15   GLY A CA    1 
ATOM   68   C C     . GLY A 1 21  ? 10.12469  -0.87572  25.37798  1.000 23.50828 ? 15   GLY A C     1 
ATOM   69   O O     . GLY A 1 21  ? 11.01871  -1.15345  26.18495  1.000 20.52503 ? 15   GLY A O     1 
ATOM   70   N N     . PHE A 1 22  ? 9.55189   0.33840   25.30117  1.000 22.09668 ? 16   PHE A N     1 
ATOM   71   C CA    . PHE A 1 22  ? 9.95119   1.42804   26.19866  1.000 21.08044 ? 16   PHE A CA    1 
ATOM   72   C C     . PHE A 1 22  ? 10.00452  0.95449   27.64314  1.000 23.52126 ? 16   PHE A C     1 
ATOM   73   O O     . PHE A 1 22  ? 10.93102  1.29215   28.39985  1.000 20.58104 ? 16   PHE A O     1 
ATOM   74   C CB    . PHE A 1 22  ? 8.95538   2.59246   26.11778  1.000 21.62937 ? 16   PHE A CB    1 
ATOM   75   C CG    . PHE A 1 22  ? 9.35644   3.71605   25.17287  1.000 24.72124 ? 16   PHE A CG    1 
ATOM   76   C CD1   . PHE A 1 22  ? 10.27064  4.66362   25.57792  1.000 22.60607 ? 16   PHE A CD1   1 
ATOM   77   C CD2   . PHE A 1 22  ? 8.73723   3.86480   23.92148  1.000 22.70894 ? 16   PHE A CD2   1 
ATOM   78   C CE1   . PHE A 1 22  ? 10.62561  5.70774   24.74803  1.000 23.09964 ? 16   PHE A CE1   1 
ATOM   79   C CE2   . PHE A 1 22  ? 9.08241   4.90650   23.09407  1.000 24.16284 ? 16   PHE A CE2   1 
ATOM   80   C CZ    . PHE A 1 22  ? 10.01800  5.84080   23.51005  1.000 24.14870 ? 16   PHE A CZ    1 
ATOM   81   N N     . GLY A 1 23  ? 8.96642   0.23629   28.06398  1.000 20.46513 ? 17   GLY A N     1 
ATOM   82   C CA    . GLY A 1 23  ? 8.86386   -0.10477  29.46801  1.000 21.81549 ? 17   GLY A CA    1 
ATOM   83   C C     . GLY A 1 23  ? 9.87742   -1.14243  29.89387  1.000 24.28935 ? 17   GLY A C     1 
ATOM   84   O O     . GLY A 1 23  ? 10.51160  -1.00016  30.94957  1.000 23.03094 ? 17   GLY A O     1 
ATOM   85   N N     . GLY A 1 24  ? 10.02142  -2.21440  29.10276  1.000 23.12633 ? 18   GLY A N     1 
ATOM   86   C CA    . GLY A 1 24  ? 10.94865  -3.28169  29.45815  1.000 21.28684 ? 18   GLY A CA    1 
ATOM   87   C C     . GLY A 1 24  ? 12.40672  -2.87682  29.37102  1.000 25.02533 ? 18   GLY A C     1 
ATOM   88   O O     . GLY A 1 24  ? 13.23151  -3.32878  30.17160  1.000 24.04798 ? 18   GLY A O     1 
ATOM   89   N N     . LEU A 1 25  ? 12.75248  -2.03345  28.39181  1.000 22.47818 ? 19   LEU A N     1 
ATOM   90   C CA    . LEU A 1 25  ? 14.15194  -1.63540  28.25131  1.000 23.73533 ? 19   LEU A CA    1 
ATOM   91   C C     . LEU A 1 25  ? 14.62487  -0.79651  29.43604  1.000 26.08361 ? 19   LEU A C     1 
ATOM   92   O O     . LEU A 1 25  ? 15.76210  -0.97417  29.91945  1.000 25.38776 ? 19   LEU A O     1 
ATOM   93   C CB    . LEU A 1 25  ? 14.36243  -0.85501  26.94666  1.000 23.25340 ? 19   LEU A CB    1 
ATOM   94   C CG    . LEU A 1 25  ? 14.23268  -1.61415  25.62567  1.000 24.11672 ? 19   LEU A CG    1 
ATOM   95   C CD1   . LEU A 1 25  ? 14.34425  -0.61276  24.47010  1.000 25.60286 ? 19   LEU A CD1   1 
ATOM   96   C CD2   . LEU A 1 25  ? 15.27389  -2.72417  25.49293  1.000 24.04012 ? 19   LEU A CD2   1 
ATOM   97   N N     . TYR A 1 26  ? 13.79764  0.13820   29.90777  1.000 21.52718 ? 20   TYR A N     1 
ATOM   98   C CA    . TYR A 1 26  ? 14.21155  0.93321   31.06597  1.000 22.08242 ? 20   TYR A CA    1 
ATOM   99   C C     . TYR A 1 26  ? 14.14055  0.11519   32.35784  1.000 27.12853 ? 20   TYR A C     1 
ATOM   100  O O     . TYR A 1 26  ? 14.99406  0.27914   33.23729  1.000 25.38128 ? 20   TYR A O     1 
ATOM   101  C CB    . TYR A 1 26  ? 13.34973  2.19834   31.19501  1.000 23.02279 ? 20   TYR A CB    1 
ATOM   102  C CG    . TYR A 1 26  ? 13.82438  3.16269   32.28462  1.000 23.81769 ? 20   TYR A CG    1 
ATOM   103  C CD1   . TYR A 1 26  ? 15.16787  3.45770   32.41032  1.000 26.59317 ? 20   TYR A CD1   1 
ATOM   104  C CD2   . TYR A 1 26  ? 12.92224  3.77841   33.15681  1.000 25.56482 ? 20   TYR A CD2   1 
ATOM   105  C CE1   . TYR A 1 26  ? 15.63249  4.35327   33.38037  1.000 28.36529 ? 20   TYR A CE1   1 
ATOM   106  C CE2   . TYR A 1 26  ? 13.36749  4.67358   34.12600  1.000 28.58213 ? 20   TYR A CE2   1 
ATOM   107  C CZ    . TYR A 1 26  ? 14.72422  4.95340   34.23281  1.000 30.67852 ? 20   TYR A CZ    1 
ATOM   108  O OH    . TYR A 1 26  ? 15.19500  5.84142   35.18303  1.000 30.33579 ? 20   TYR A OH    1 
ATOM   109  N N     . SER A 1 27  ? 13.14709  -0.77820  32.47929  1.000 25.15163 ? 21   SER A N     1 
ATOM   110  C CA    . SER A 1 27  ? 13.14503  -1.74726  33.57761  1.000 25.88189 ? 21   SER A CA    1 
ATOM   111  C C     . SER A 1 27  ? 14.48014  -2.46963  33.66022  1.000 25.44905 ? 21   SER A C     1 
ATOM   112  O O     . SER A 1 27  ? 15.06431  -2.61166  34.74151  1.000 25.79720 ? 21   SER A O     1 
ATOM   113  C CB    . SER A 1 27  ? 12.01460  -2.76844  33.37435  1.000 23.75312 ? 21   SER A CB    1 
ATOM   114  O OG    . SER A 1 27  ? 10.74738  -2.17572  33.54267  1.000 26.02766 ? 21   SER A OG    1 
ATOM   115  N N     . LEU A 1 28  ? 14.98898  -2.92433  32.51395  1.000 26.75252 ? 22   LEU A N     1 
ATOM   116  C CA    . LEU A 1 28  ? 16.21866  -3.70306  32.50814  1.000 25.97578 ? 22   LEU A CA    1 
ATOM   117  C C     . LEU A 1 28  ? 17.41516  -2.83491  32.88425  1.000 30.01019 ? 22   LEU A C     1 
ATOM   118  O O     . LEU A 1 28  ? 18.22095  -3.20791  33.74177  1.000 27.95061 ? 22   LEU A O     1 
ATOM   119  C CB    . LEU A 1 28  ? 16.40146  -4.32962  31.12770  1.000 25.75922 ? 22   LEU A CB    1 
ATOM   120  C CG    . LEU A 1 28  ? 17.70811  -5.04291  30.84519  1.000 27.87029 ? 22   LEU A CG    1 
ATOM   121  C CD1   . LEU A 1 28  ? 17.94597  -6.13795  31.88399  1.000 29.07002 ? 22   LEU A CD1   1 
ATOM   122  C CD2   . LEU A 1 28  ? 17.72275  -5.59506  29.40410  1.000 29.94962 ? 22   LEU A CD2   1 
ATOM   123  N N     . LYS A 1 29  ? 17.52727  -1.65247  32.27111  1.000 27.87502 ? 23   LYS A N     1 
ATOM   124  C CA    . LYS A 1 29  ? 18.63066  -0.75086  32.58364  1.000 28.82608 ? 23   LYS A CA    1 
ATOM   125  C C     . LYS A 1 29  ? 18.63575  -0.37373  34.06706  1.000 25.86135 ? 23   LYS A C     1 
ATOM   126  O O     . LYS A 1 29  ? 19.67889  -0.41567  34.72178  1.000 31.29493 ? 23   LYS A O     1 
ATOM   127  C CB    . LYS A 1 29  ? 18.52242  0.50074   31.69813  1.000 24.74556 ? 23   LYS A CB    1 
ATOM   128  C CG    . LYS A 1 29  ? 19.41884  1.68875   32.14003  1.000 28.11289 ? 23   LYS A CG    1 
ATOM   129  C CD    . LYS A 1 29  ? 20.84526  1.41377   31.83241  1.000 34.73938 ? 23   LYS A CD    1 
ATOM   130  C CE    . LYS A 1 29  ? 21.78725  2.45268   32.50759  1.000 34.45898 ? 23   LYS A CE    1 
ATOM   131  N NZ    . LYS A 1 29  ? 23.16289  2.21847   32.00511  1.000 33.90484 ? 23   LYS A NZ    1 
ATOM   132  N N     . LYS A 1 30  ? 17.47552  -0.03759  34.62452  1.000 26.18588 ? 24   LYS A N     1 
ATOM   133  C CA    . LYS A 1 30  ? 17.44771  0.44707   36.00715  1.000 25.73841 ? 24   LYS A CA    1 
ATOM   134  C C     . LYS A 1 30  ? 17.77535  -0.67705  36.98902  1.000 32.15529 ? 24   LYS A C     1 
ATOM   135  O O     . LYS A 1 30  ? 18.54259  -0.48461  37.94167  1.000 29.58729 ? 24   LYS A O     1 
ATOM   136  C CB    . LYS A 1 30  ? 16.07344  1.03075   36.32527  1.000 29.14019 ? 24   LYS A CB    1 
ATOM   137  C CG    . LYS A 1 30  ? 16.03073  1.87707   37.62965  1.000 37.49009 ? 24   LYS A CG    1 
ATOM   138  C CD    . LYS A 1 30  ? 16.54815  3.27995   37.28833  1.000 38.13972 ? 24   LYS A CD    1 
ATOM   139  C CE    . LYS A 1 30  ? 16.96261  4.08520   38.48398  1.000 41.90429 ? 24   LYS A CE    1 
ATOM   140  N NZ    . LYS A 1 30  ? 17.76407  5.20431   37.97312  1.000 37.31095 ? 24   LYS A NZ    1 
ATOM   141  N N     . LEU A 1 31  ? 17.18124  -1.85865  36.79253  1.000 28.12147 ? 25   LEU A N     1 
ATOM   142  C CA    . LEU A 1 31  ? 17.40981  -2.93112  37.76046  1.000 27.63068 ? 25   LEU A CA    1 
ATOM   143  C C     . LEU A 1 31  ? 18.81935  -3.49140  37.65025  1.000 30.47462 ? 25   LEU A C     1 
ATOM   144  O O     . LEU A 1 31  ? 19.41559  -3.86302  38.66713  1.000 31.87937 ? 25   LEU A O     1 
ATOM   145  C CB    . LEU A 1 31  ? 16.36749  -4.03475  37.57872  1.000 25.99189 ? 25   LEU A CB    1 
ATOM   146  C CG    . LEU A 1 31  ? 14.96210  -3.56692  37.94821  1.000 29.19070 ? 25   LEU A CG    1 
ATOM   147  C CD1   . LEU A 1 31  ? 13.94914  -4.63754  37.63692  1.000 26.37432 ? 25   LEU A CD1   1 
ATOM   148  C CD2   . LEU A 1 31  ? 14.91427  -3.17538  39.44325  1.000 28.29795 ? 25   LEU A CD2   1 
ATOM   149  N N     . ARG A 1 32  ? 19.37698  -3.53396  36.43961  1.000 28.78594 ? 26   ARG A N     1 
ATOM   150  C CA    . ARG A 1 32  ? 20.66950  -4.16818  36.22544  1.000 27.40524 ? 26   ARG A CA    1 
ATOM   151  C C     . ARG A 1 32  ? 21.81968  -3.22958  36.53831  1.000 36.59569 ? 26   ARG A C     1 
ATOM   152  O O     . ARG A 1 32  ? 22.76419  -3.60509  37.24682  1.000 32.51350 ? 26   ARG A O     1 
ATOM   153  C CB    . ARG A 1 32  ? 20.80284  -4.64868  34.78769  1.000 32.93318 ? 26   ARG A CB    1 
ATOM   154  C CG    . ARG A 1 32  ? 22.02652  -5.49960  34.55667  1.000 33.74008 ? 26   ARG A CG    1 
ATOM   155  C CD    . ARG A 1 32  ? 22.22756  -5.67611  33.06553  1.000 36.08989 ? 26   ARG A CD    1 
ATOM   156  N NE    . ARG A 1 32  ? 22.68451  -4.43702  32.43233  1.000 35.99388 ? 26   ARG A NE    1 
ATOM   157  C CZ    . ARG A 1 32  ? 22.87263  -4.29424  31.12434  1.000 33.97323 ? 26   ARG A CZ    1 
ATOM   158  N NH1   . ARG A 1 32  ? 22.59612  -5.27370  30.27615  1.000 30.90432 ? 26   ARG A NH1   1 
ATOM   159  N NH2   . ARG A 1 32  ? 23.34949  -3.13842  30.65440  1.000 33.06460 ? 26   ARG A NH2   1 
ATOM   160  N N     . ASP A 1 33  ? 21.76255  -2.00296  36.02492  1.000 30.16468 ? 27   ASP A N     1 
ATOM   161  C CA    . ASP A 1 33  ? 22.94369  -1.16070  36.08921  1.000 31.66346 ? 27   ASP A CA    1 
ATOM   162  C C     . ASP A 1 33  ? 22.94263  -0.22579  37.28760  1.000 34.96686 ? 27   ASP A C     1 
ATOM   163  O O     . ASP A 1 33  ? 24.01991  0.12601   37.77352  1.000 39.19891 ? 27   ASP A O     1 
ATOM   164  C CB    . ASP A 1 33  ? 23.08521  -0.36156  34.78531  1.000 34.15665 ? 27   ASP A CB    1 
ATOM   165  C CG    . ASP A 1 33  ? 23.41068  -1.24399  33.61114  1.000 36.95095 ? 27   ASP A CG    1 
ATOM   166  O OD1   . ASP A 1 33  ? 23.78160  -2.43270  33.83312  1.000 39.04488 ? 27   ASP A OD1   1 
ATOM   167  O OD2   . ASP A 1 33  ? 23.31115  -0.75712  32.46971  1.000 40.21047 ? 27   ASP A OD2   1 
ATOM   168  N N     . ASP A 1 34  ? 21.76820  0.17041   37.78790  1.000 32.29801 ? 28   ASP A N     1 
ATOM   169  C CA    . ASP A 1 34  ? 21.67698  1.03372   38.95881  1.000 32.87538 ? 28   ASP A CA    1 
ATOM   170  C C     . ASP A 1 34  ? 21.46225  0.27506   40.26043  1.000 37.24577 ? 28   ASP A C     1 
ATOM   171  O O     . ASP A 1 34  ? 21.84415  0.77520   41.31972  1.000 40.29088 ? 28   ASP A O     1 
ATOM   172  C CB    . ASP A 1 34  ? 20.54432  2.05125   38.79513  1.000 34.36743 ? 28   ASP A CB    1 
ATOM   173  C CG    . ASP A 1 34  ? 20.80036  3.03144   37.66127  1.000 46.23188 ? 28   ASP A CG    1 
ATOM   174  O OD1   . ASP A 1 34  ? 21.97390  3.19015   37.25829  1.000 48.27977 ? 28   ASP A OD1   1 
ATOM   175  O OD2   . ASP A 1 34  ? 19.82242  3.62909   37.15392  1.000 48.03987 ? 28   ASP A OD2   1 
ATOM   176  N N     . PHE A 1 35  ? 20.83140  -0.89822  40.23120  1.000 30.63954 ? 29   PHE A N     1 
ATOM   177  C CA    . PHE A 1 35  ? 20.65081  -1.67371  41.44701  1.000 34.01769 ? 29   PHE A CA    1 
ATOM   178  C C     . PHE A 1 35  ? 21.44051  -2.97018  41.41408  1.000 36.68441 ? 29   PHE A C     1 
ATOM   179  O O     . PHE A 1 35  ? 21.25743  -3.80308  42.30473  1.000 41.24462 ? 29   PHE A O     1 
ATOM   180  C CB    . PHE A 1 35  ? 19.16155  -1.94048  41.70954  1.000 30.57074 ? 29   PHE A CB    1 
ATOM   181  C CG    . PHE A 1 35  ? 18.40521  -0.72523  42.20081  1.000 35.81362 ? 29   PHE A CG    1 
ATOM   182  C CD1   . PHE A 1 35  ? 17.93363  0.22498   41.30086  1.000 32.01482 ? 29   PHE A CD1   1 
ATOM   183  C CD2   . PHE A 1 35  ? 18.18922  -0.51438  43.56031  1.000 37.95438 ? 29   PHE A CD2   1 
ATOM   184  C CE1   . PHE A 1 35  ? 17.25613  1.34390   41.73204  1.000 36.60589 ? 29   PHE A CE1   1 
ATOM   185  C CE2   . PHE A 1 35  ? 17.50273  0.60236   44.00388  1.000 36.68019 ? 29   PHE A CE2   1 
ATOM   186  C CZ    . PHE A 1 35  ? 17.03719  1.54399   43.09523  1.000 39.01294 ? 29   PHE A CZ    1 
ATOM   187  N N     . ASN A 1 36  ? 22.31711  -3.14060  40.41337  1.000 29.13491 ? 30   ASN A N     1 
ATOM   188  C CA    . ASN A 1 36  ? 23.23378  -4.27923  40.29411  1.000 36.20905 ? 30   ASN A CA    1 
ATOM   189  C C     . ASN A 1 36  ? 22.53046  -5.61592  40.52519  1.000 41.07318 ? 30   ASN A C     1 
ATOM   190  O O     . ASN A 1 36  ? 23.02838  -6.50197  41.22834  1.000 40.49237 ? 30   ASN A O     1 
ATOM   191  C CB    . ASN A 1 36  ? 24.43436  -4.10636  41.22920  1.000 43.58466 ? 30   ASN A CB    1 
ATOM   192  C CG    . ASN A 1 36  ? 25.22490  -2.86614  40.91175  1.000 44.67460 ? 30   ASN A CG    1 
ATOM   193  O OD1   . ASN A 1 36  ? 25.76607  -2.72539  39.81174  1.000 52.91486 ? 30   ASN A OD1   1 
ATOM   194  N ND2   . ASN A 1 36  ? 25.26777  -1.93580  41.85343  1.000 53.84112 ? 30   ASN A ND2   1 
ATOM   195  N N     . LEU A 1 37  ? 21.36838  -5.77758  39.91343  1.000 33.01752 ? 31   LEU A N     1 
ATOM   196  C CA    . LEU A 1 37  ? 20.66836  -7.04441  40.01591  1.000 34.53623 ? 31   LEU A CA    1 
ATOM   197  C C     . LEU A 1 37  ? 20.95871  -7.90862  38.79057  1.000 34.37616 ? 31   LEU A C     1 
ATOM   198  O O     . LEU A 1 37  ? 21.40875  -7.42862  37.74636  1.000 36.06943 ? 31   LEU A O     1 
ATOM   199  C CB    . LEU A 1 37  ? 19.16972  -6.83333  40.19657  1.000 37.26261 ? 31   LEU A CB    1 
ATOM   200  C CG    . LEU A 1 37  ? 18.74854  -5.99871  41.41014  1.000 38.45680 ? 31   LEU A CG    1 
ATOM   201  C CD1   . LEU A 1 37  ? 17.23943  -5.78032  41.39010  1.000 35.12671 ? 31   LEU A CD1   1 
ATOM   202  C CD2   . LEU A 1 37  ? 19.18732  -6.67675  42.70821  1.000 42.19559 ? 31   LEU A CD2   1 
ATOM   203  N N     . LYS A 1 38  ? 20.77793  -9.21084  38.96770  1.000 30.25931 ? 32   LYS A N     1 
ATOM   204  C CA    . LYS A 1 38  ? 20.84971  -10.16447 37.86966  1.000 33.84004 ? 32   LYS A CA    1 
ATOM   205  C C     . LYS A 1 38  ? 19.46935  -10.24752 37.23191  1.000 32.95009 ? 32   LYS A C     1 
ATOM   206  O O     . LYS A 1 38  ? 18.49289  -10.59566 37.89966  1.000 30.75114 ? 32   LYS A O     1 
ATOM   207  C CB    . LYS A 1 38  ? 21.31254  -11.52807 38.37790  1.000 37.41721 ? 32   LYS A CB    1 
ATOM   208  C CG    . LYS A 1 38  ? 21.48628  -12.55192 37.29155  1.000 47.83674 ? 32   LYS A CG    1 
ATOM   209  C CD    . LYS A 1 38  ? 22.87283  -12.45413 36.67891  1.000 55.47415 ? 32   LYS A CD    1 
ATOM   210  C CE    . LYS A 1 38  ? 22.90399  -13.12951 35.31144  1.000 62.97165 ? 32   LYS A CE    1 
ATOM   211  N NZ    . LYS A 1 38  ? 23.11306  -12.14903 34.19973  1.000 66.40267 ? 32   LYS A NZ    1 
ATOM   212  N N     . VAL A 1 39  ? 19.38284  -9.90033  35.95228  1.000 31.16981 ? 33   VAL A N     1 
ATOM   213  C CA    . VAL A 1 39  ? 18.10416  -9.71895  35.28758  1.000 29.37350 ? 33   VAL A CA    1 
ATOM   214  C C     . VAL A 1 39  ? 18.15664  -10.37762 33.91432  1.000 28.19579 ? 33   VAL A C     1 
ATOM   215  O O     . VAL A 1 39  ? 19.20798  -10.42517 33.26909  1.000 29.82176 ? 33   VAL A O     1 
ATOM   216  C CB    . VAL A 1 39  ? 17.77001  -8.20720  35.14181  1.000 28.34366 ? 33   VAL A CB    1 
ATOM   217  C CG1   . VAL A 1 39  ? 16.37430  -8.00400  34.61400  1.000 27.21308 ? 33   VAL A CG1   1 
ATOM   218  C CG2   . VAL A 1 39  ? 17.92953  -7.47124  36.49204  1.000 30.98341 ? 33   VAL A CG2   1 
ATOM   219  N N     . ARG A 1 40  ? 17.00089  -10.84124 33.45521  1.000 30.60730 ? 34   ARG A N     1 
ATOM   220  C CA    . ARG A 1 40  ? 16.80566  -11.24505 32.06533  1.000 28.95086 ? 34   ARG A CA    1 
ATOM   221  C C     . ARG A 1 40  ? 15.43231  -10.78531 31.59571  1.000 25.13034 ? 34   ARG A C     1 
ATOM   222  O O     . ARG A 1 40  ? 14.44466  -10.89483 32.32900  1.000 28.91153 ? 34   ARG A O     1 
ATOM   223  C CB    . ARG A 1 40  ? 16.93840  -12.76253 31.90337  1.000 29.21327 ? 34   ARG A CB    1 
ATOM   224  C CG    . ARG A 1 40  ? 17.08400  -13.23083 30.47621  1.000 31.44594 ? 34   ARG A CG    1 
ATOM   225  C CD    . ARG A 1 40  ? 17.87858  -14.53679 30.49921  1.000 46.22075 ? 34   ARG A CD    1 
ATOM   226  N NE    . ARG A 1 40  ? 18.23884  -15.00615 29.16828  1.000 48.93965 ? 34   ARG A NE    1 
ATOM   227  C CZ    . ARG A 1 40  ? 19.16308  -14.45808 28.39477  1.000 44.38063 ? 34   ARG A CZ    1 
ATOM   228  N NH1   . ARG A 1 40  ? 19.91864  -13.45731 28.82040  1.000 43.66067 ? 34   ARG A NH1   1 
ATOM   229  N NH2   . ARG A 1 40  ? 19.33238  -14.92566 27.16048  1.000 46.59396 ? 34   ARG A NH2   1 
ATOM   230  N N     . ALA A 1 41  ? 15.37319  -10.26042 30.38314  1.000 28.44235 ? 35   ALA A N     1 
ATOM   231  C CA    . ALA A 1 41  ? 14.12891  -9.83723  29.75569  1.000 26.70700 ? 35   ALA A CA    1 
ATOM   232  C C     . ALA A 1 41  ? 13.82175  -10.75590 28.57910  1.000 26.78025 ? 35   ALA A C     1 
ATOM   233  O O     . ALA A 1 41  ? 14.72881  -11.34612 27.99030  1.000 32.34472 ? 35   ALA A O     1 
ATOM   234  C CB    . ALA A 1 41  ? 14.21908  -8.38218  29.27762  1.000 24.39794 ? 35   ALA A CB    1 
ATOM   235  N N     . PHE A 1 42  ? 12.52859  -10.87602 28.26249  1.000 27.73645 ? 36   PHE A N     1 
ATOM   236  C CA    . PHE A 1 42  ? 12.03663  -11.75779 27.20360  1.000 29.92137 ? 36   PHE A CA    1 
ATOM   237  C C     . PHE A 1 42  ? 11.06848  -11.00816 26.30233  1.000 26.58570 ? 36   PHE A C     1 
ATOM   238  O O     . PHE A 1 42  ? 10.22130  -10.25499 26.79069  1.000 25.60996 ? 36   PHE A O     1 
ATOM   239  C CB    . PHE A 1 42  ? 11.32623  -12.98838 27.80317  1.000 25.59472 ? 36   PHE A CB    1 
ATOM   240  C CG    . PHE A 1 42  ? 12.24390  -13.86997 28.61228  1.000 26.24675 ? 36   PHE A CG    1 
ATOM   241  C CD1   . PHE A 1 42  ? 12.92821  -14.89927 28.01498  1.000 33.97767 ? 36   PHE A CD1   1 
ATOM   242  C CD2   . PHE A 1 42  ? 12.46526  -13.62018 29.96357  1.000 31.40647 ? 36   PHE A CD2   1 
ATOM   243  C CE1   . PHE A 1 42  ? 13.80689  -15.69492 28.74616  1.000 32.72988 ? 36   PHE A CE1   1 
ATOM   244  C CE2   . PHE A 1 42  ? 13.33657  -14.41800 30.70604  1.000 30.64717 ? 36   PHE A CE2   1 
ATOM   245  C CZ    . PHE A 1 42  ? 14.01004  -15.44994 30.08721  1.000 35.33198 ? 36   PHE A CZ    1 
ATOM   246  N N     . ASP A 1 43  ? 11.14940  -11.26106 24.99169  1.000 23.94626 ? 37   ASP A N     1 
ATOM   247  C CA    . ASP A 1 43  ? 10.14236  -10.73011 24.08162  1.000 25.58072 ? 37   ASP A CA    1 
ATOM   248  C C     . ASP A 1 43  ? 9.98898   -11.67244 22.89056  1.000 24.92219 ? 37   ASP A C     1 
ATOM   249  O O     . ASP A 1 43  ? 10.97752  -12.22475 22.40996  1.000 27.12544 ? 37   ASP A O     1 
ATOM   250  C CB    . ASP A 1 43  ? 10.51631  -9.32063  23.59417  1.000 29.96032 ? 37   ASP A CB    1 
ATOM   251  C CG    . ASP A 1 43  ? 9.30312   -8.53300  23.07125  1.000 29.28563 ? 37   ASP A CG    1 
ATOM   252  O OD1   . ASP A 1 43  ? 8.43393   -9.11912  22.38092  1.000 32.74205 ? 37   ASP A OD1   1 
ATOM   253  O OD2   . ASP A 1 43  ? 9.20027   -7.32487  23.37038  1.000 28.21892 ? 37   ASP A OD2   1 
ATOM   254  N N     . ARG A 1 44  ? 8.75339   -11.81544 22.41117  1.000 26.25693 ? 38   ARG A N     1 
ATOM   255  C CA    . ARG A 1 44  ? 8.50549   -12.60114 21.20124  1.000 28.10902 ? 38   ARG A CA    1 
ATOM   256  C C     . ARG A 1 44  ? 9.17393   -11.98461 19.98027  1.000 32.72211 ? 38   ARG A C     1 
ATOM   257  O O     . ARG A 1 44  ? 9.54764   -12.70276 19.04528  1.000 31.84049 ? 38   ARG A O     1 
ATOM   258  C CB    . ARG A 1 44  ? 7.00426   -12.72525 20.94357  1.000 36.87725 ? 38   ARG A CB    1 
ATOM   259  C CG    . ARG A 1 44  ? 6.30061   -13.70026 21.83184  1.000 29.88312 ? 38   ARG A CG    1 
ATOM   260  C CD    . ARG A 1 44  ? 4.86395   -13.88184 21.42757  1.000 41.32334 ? 38   ARG A CD    1 
ATOM   261  N NE    . ARG A 1 44  ? 4.20982   -14.81635 22.33236  1.000 34.72360 ? 38   ARG A NE    1 
ATOM   262  C CZ    . ARG A 1 44  ? 3.31745   -14.46849 23.24708  1.000 39.40557 ? 38   ARG A CZ    1 
ATOM   263  N NH1   . ARG A 1 44  ? 2.89759   -13.21731 23.36156  1.000 34.19555 ? 38   ARG A NH1   1 
ATOM   264  N NH2   . ARG A 1 44  ? 2.80701   -15.40602 24.04518  1.000 40.20276 ? 38   ARG A NH2   1 
ATOM   265  N N     . ALA A 1 45  ? 9.31117   -10.65842 19.96831  1.000 30.99258 ? 39   ALA A N     1 
ATOM   266  C CA    . ALA A 1 45  ? 9.89329   -9.92145  18.86161  1.000 31.38731 ? 39   ALA A CA    1 
ATOM   267  C C     . ALA A 1 45  ? 11.33518  -10.34553 18.61824  1.000 27.00393 ? 39   ALA A C     1 
ATOM   268  O O     . ALA A 1 45  ? 12.00792  -10.85688 19.50976  1.000 31.56506 ? 39   ALA A O     1 
ATOM   269  C CB    . ALA A 1 45  ? 9.84054   -8.41915  19.15964  1.000 30.38824 ? 39   ALA A CB    1 
ATOM   270  N N     . THR A 1 46  ? 11.83878  -10.08164 17.40178  1.000 27.60236 ? 40   THR A N     1 
ATOM   271  C CA    . THR A 1 46  ? 13.25345  -10.33051 17.10283  1.000 28.42189 ? 40   THR A CA    1 
ATOM   272  C C     . THR A 1 46  ? 14.15420  -9.15150  17.47588  1.000 33.32003 ? 40   THR A C     1 
ATOM   273  O O     . THR A 1 46  ? 15.37699  -9.27482  17.40452  1.000 29.36650 ? 40   THR A O     1 
ATOM   274  C CB    . THR A 1 46  ? 13.47823  -10.63120 15.60447  1.000 32.58466 ? 40   THR A CB    1 
ATOM   275  O OG1   . THR A 1 46  ? 12.83947  -9.61896  14.82398  1.000 37.94947 ? 40   THR A OG1   1 
ATOM   276  C CG2   . THR A 1 46  ? 12.90068  -11.99406 15.20027  1.000 33.22691 ? 40   THR A CG2   1 
ATOM   277  N N     . GLU A 1 47  ? 13.58949  -8.00502  17.84054  1.000 30.87759 ? 41   GLU A N     1 
ATOM   278  C CA    . GLU A 1 47  ? 14.38970  -6.81625  18.12581  1.000 29.73014 ? 41   GLU A CA    1 
ATOM   279  C C     . GLU A 1 47  ? 13.64305  -5.97679  19.15853  1.000 25.06996 ? 41   GLU A C     1 
ATOM   280  O O     . GLU A 1 47  ? 12.45917  -6.20459  19.42442  1.000 26.54301 ? 41   GLU A O     1 
ATOM   281  C CB    . GLU A 1 47  ? 14.67932  -6.05902  16.81188  1.000 32.98645 ? 41   GLU A CB    1 
ATOM   282  C CG    . GLU A 1 47  ? 15.51803  -4.75763  16.83774  1.000 37.51268 ? 41   GLU A CG    1 
ATOM   283  C CD    . GLU A 1 47  ? 16.90748  -4.77313  17.47307  1.000 31.21608 ? 41   GLU A CD    1 
ATOM   284  O OE1   . GLU A 1 47  ? 17.04714  -5.09824  18.64877  1.000 30.97003 ? 41   GLU A OE1   1 
ATOM   285  O OE2   . GLU A 1 47  ? 17.87409  -4.33129  16.80006  1.000 46.68593 ? 41   GLU A OE2   1 
ATOM   286  N N     . VAL A 1 48  ? 14.35155  -5.01849  19.76168  1.000 24.59084 ? 42   VAL A N     1 
ATOM   287  C CA    . VAL A 1 48  ? 13.73200  -4.14486  20.75403  1.000 26.22556 ? 42   VAL A CA    1 
ATOM   288  C C     . VAL A 1 48  ? 12.71057  -3.24494  20.05974  1.000 24.98919 ? 42   VAL A C     1 
ATOM   289  O O     . VAL A 1 48  ? 12.67841  -3.15882  18.83053  1.000 25.49114 ? 42   VAL A O     1 
ATOM   290  C CB    . VAL A 1 48  ? 14.76814  -3.29924  21.52979  1.000 25.70043 ? 42   VAL A CB    1 
ATOM   291  C CG1   . VAL A 1 48  ? 15.83289  -4.19518  22.15470  1.000 27.42560 ? 42   VAL A CG1   1 
ATOM   292  C CG2   . VAL A 1 48  ? 15.39313  -2.18937  20.63401  1.000 24.74461 ? 42   VAL A CG2   1 
ATOM   293  N N     . GLY A 1 49  ? 11.85042  -2.60759  20.84950  1.000 21.53757 ? 43   GLY A N     1 
ATOM   294  C CA    . GLY A 1 49  ? 10.99733  -1.55199  20.33808  1.000 23.99839 ? 43   GLY A CA    1 
ATOM   295  C C     . GLY A 1 49  ? 9.53403   -1.75559  20.67161  1.000 24.11073 ? 43   GLY A C     1 
ATOM   296  O O     . GLY A 1 49  ? 8.74807   -0.80831  20.63432  1.000 22.69617 ? 43   GLY A O     1 
ATOM   297  N N     . GLY A 1 50  ? 9.14635   -2.99200  20.97612  1.000 22.74905 ? 44   GLY A N     1 
ATOM   298  C CA    . GLY A 1 50  ? 7.75449   -3.23276  21.32719  1.000 21.63340 ? 44   GLY A CA    1 
ATOM   299  C C     . GLY A 1 50  ? 6.79534   -2.80742  20.23052  1.000 23.61803 ? 44   GLY A C     1 
ATOM   300  O O     . GLY A 1 50  ? 6.95388   -3.16464  19.05242  1.000 23.33103 ? 44   GLY A O     1 
ATOM   301  N N     . THR A 1 51  ? 5.76604   -2.04748  20.61509  1.000 21.11484 ? 45   THR A N     1 
ATOM   302  C CA    . THR A 1 51  ? 4.77505   -1.62041  19.62180  1.000 22.77915 ? 45   THR A CA    1 
ATOM   303  C C     . THR A 1 51  ? 5.42611   -0.95093  18.40722  1.000 21.45655 ? 45   THR A C     1 
ATOM   304  O O     . THR A 1 51  ? 4.90637   -1.06492  17.29167  1.000 24.43022 ? 45   THR A O     1 
ATOM   305  C CB    . THR A 1 51  ? 3.74398   -0.68973  20.28666  1.000 32.12552 ? 45   THR A CB    1 
ATOM   306  O OG1   . THR A 1 51  ? 2.64944   -0.46840  19.39282  1.000 39.80359 ? 45   THR A OG1   1 
ATOM   307  C CG2   . THR A 1 51  ? 4.34909   0.64928   20.60410  1.000 28.14911 ? 45   THR A CG2   1 
ATOM   308  N N     . TRP A 1 52  ? 6.57525   -0.28205  18.58631  1.000 21.16338 ? 46   TRP A N     1 
ATOM   309  C CA    . TRP A 1 52  ? 7.26628   0.37061   17.47698  1.000 22.48551 ? 46   TRP A CA    1 
ATOM   310  C C     . TRP A 1 52  ? 8.01327   -0.61640  16.58910  1.000 27.55989 ? 46   TRP A C     1 
ATOM   311  O O     . TRP A 1 52  ? 8.44418   -0.24482  15.48764  1.000 24.98404 ? 46   TRP A O     1 
ATOM   312  C CB    . TRP A 1 52  ? 8.22393   1.44273   18.03117  1.000 21.27542 ? 46   TRP A CB    1 
ATOM   313  C CG    . TRP A 1 52  ? 7.41641   2.49827   18.69744  1.000 22.81018 ? 46   TRP A CG    1 
ATOM   314  C CD1   . TRP A 1 52  ? 7.23738   2.69383   20.04838  1.000 19.03786 ? 46   TRP A CD1   1 
ATOM   315  C CD2   . TRP A 1 52  ? 6.62309   3.47281   18.04124  1.000 19.31104 ? 46   TRP A CD2   1 
ATOM   316  N NE1   . TRP A 1 52  ? 6.38960   3.75237   20.25246  1.000 21.61362 ? 46   TRP A NE1   1 
ATOM   317  C CE2   . TRP A 1 52  ? 6.00239   4.25120   19.03894  1.000 21.72204 ? 46   TRP A CE2   1 
ATOM   318  C CE3   . TRP A 1 52  ? 6.40061   3.79013   16.70469  1.000 18.12910 ? 46   TRP A CE3   1 
ATOM   319  C CZ2   . TRP A 1 52  ? 5.17672   5.32650   18.73714  1.000 24.06213 ? 46   TRP A CZ2   1 
ATOM   320  C CZ3   . TRP A 1 52  ? 5.58015   4.85942   16.41225  1.000 26.47682 ? 46   TRP A CZ3   1 
ATOM   321  C CH2   . TRP A 1 52  ? 4.96872   5.60678   17.42297  1.000 27.16163 ? 46   TRP A CH2   1 
ATOM   322  N N     . PHE A 1 53  ? 8.16049   -1.86186  17.03929  1.000 20.50149 ? 47   PHE A N     1 
ATOM   323  C CA    . PHE A 1 53  ? 8.62912   -2.92174  16.17451  1.000 24.78322 ? 47   PHE A CA    1 
ATOM   324  C C     . PHE A 1 53  ? 7.45928   -3.58675  15.44842  1.000 24.84250 ? 47   PHE A C     1 
ATOM   325  O O     . PHE A 1 53  ? 7.54415   -3.82942  14.24292  1.000 29.31009 ? 47   PHE A O     1 
ATOM   326  C CB    . PHE A 1 53  ? 9.42538   -3.95440  16.99764  1.000 25.69188 ? 47   PHE A CB    1 
ATOM   327  C CG    . PHE A 1 53  ? 9.73949   -5.21629  16.23186  1.000 27.29202 ? 47   PHE A CG    1 
ATOM   328  C CD1   . PHE A 1 53  ? 10.80798  -5.25025  15.35516  1.000 28.40438 ? 47   PHE A CD1   1 
ATOM   329  C CD2   . PHE A 1 53  ? 8.94463   -6.34958  16.38484  1.000 27.64804 ? 47   PHE A CD2   1 
ATOM   330  C CE1   . PHE A 1 53  ? 11.09273  -6.42476  14.64313  1.000 36.44517 ? 47   PHE A CE1   1 
ATOM   331  C CE2   . PHE A 1 53  ? 9.21844   -7.50345  15.65840  1.000 31.23375 ? 47   PHE A CE2   1 
ATOM   332  C CZ    . PHE A 1 53  ? 10.28609  -7.53349  14.79849  1.000 32.59814 ? 47   PHE A CZ    1 
ATOM   333  N N     . TRP A 1 54  ? 6.34335   -3.83742  16.15200  1.000 23.56980 ? 48   TRP A N     1 
ATOM   334  C CA    . TRP A 1 54  ? 5.22548   -4.57822  15.56748  1.000 25.64429 ? 48   TRP A CA    1 
ATOM   335  C C     . TRP A 1 54  ? 4.42048   -3.73351  14.57886  1.000 26.36653 ? 48   TRP A C     1 
ATOM   336  O O     . TRP A 1 54  ? 3.91908   -4.26477  13.58967  1.000 28.44512 ? 48   TRP A O     1 
ATOM   337  C CB    . TRP A 1 54  ? 4.26979   -5.07257  16.66450  1.000 23.80204 ? 48   TRP A CB    1 
ATOM   338  C CG    . TRP A 1 54  ? 4.87581   -6.04189  17.59524  1.000 27.43889 ? 48   TRP A CG    1 
ATOM   339  C CD1   . TRP A 1 54  ? 5.15982   -5.85187  18.92900  1.000 27.15894 ? 48   TRP A CD1   1 
ATOM   340  C CD2   . TRP A 1 54  ? 5.29651   -7.37520  17.27739  1.000 36.22145 ? 48   TRP A CD2   1 
ATOM   341  N NE1   . TRP A 1 54  ? 5.73462   -7.00133  19.45155  1.000 29.23721 ? 48   TRP A NE1   1 
ATOM   342  C CE2   . TRP A 1 54  ? 5.83755   -7.93998  18.45694  1.000 32.52556 ? 48   TRP A CE2   1 
ATOM   343  C CE3   . TRP A 1 54  ? 5.26245   -8.15057  16.10740  1.000 31.97300 ? 48   TRP A CE3   1 
ATOM   344  C CZ2   . TRP A 1 54  ? 6.34462   -9.24462  18.49623  1.000 32.23235 ? 48   TRP A CZ2   1 
ATOM   345  C CZ3   . TRP A 1 54  ? 5.76504   -9.45449  16.14834  1.000 35.62114 ? 48   TRP A CZ3   1 
ATOM   346  C CH2   . TRP A 1 54  ? 6.30330   -9.98119  17.33211  1.000 33.42751 ? 48   TRP A CH2   1 
ATOM   347  N N     . ASN A 1 55  ? 4.22325   -2.44015  14.85754  1.000 24.19533 ? 49   ASN A N     1 
ATOM   348  C CA    . ASN A 1 55  ? 3.24432   -1.63031  14.11404  1.000 25.24921 ? 49   ASN A CA    1 
ATOM   349  C C     . ASN A 1 55  ? 3.97471   -0.79141  13.08002  1.000 27.27943 ? 49   ASN A C     1 
ATOM   350  O O     . ASN A 1 55  ? 4.46420   0.29265   13.39908  1.000 32.85918 ? 49   ASN A O     1 
ATOM   351  C CB    . ASN A 1 55  ? 2.45974   -0.71945  15.05085  1.000 25.97560 ? 49   ASN A CB    1 
ATOM   352  C CG    . ASN A 1 55  ? 1.38930   -1.44956  15.77974  1.000 35.54590 ? 49   ASN A CG    1 
ATOM   353  O OD1   . ASN A 1 55  ? 0.42699   -1.91177  15.17335  1.000 33.55497 ? 49   ASN A OD1   1 
ATOM   354  N ND2   . ASN A 1 55  ? 1.56174   -1.60609  17.09514  1.000 33.44688 ? 49   ASN A ND2   1 
ATOM   355  N N     . GLN A 1 56  ? 4.00250   -1.24876  11.83095  1.000 22.75358 ? 50   GLN A N     1 
ATOM   356  C CA    . GLN A 1 56  ? 4.75957   -0.56409  10.78850  1.000 24.35095 ? 50   GLN A CA    1 
ATOM   357  C C     . GLN A 1 56  ? 3.85064   -0.19798  9.61695   1.000 24.53893 ? 50   GLN A C     1 
ATOM   358  O O     . GLN A 1 56  ? 4.23201   -0.22312  8.44761   1.000 24.86562 ? 50   GLN A O     1 
ATOM   359  C CB    . GLN A 1 56  ? 5.95479   -1.42266  10.38133  1.000 27.81239 ? 50   GLN A CB    1 
ATOM   360  C CG    . GLN A 1 56  ? 5.54220   -2.79049  9.88331   1.000 35.79038 ? 50   GLN A CG    1 
ATOM   361  C CD    . GLN A 1 56  ? 6.70597   -3.64850  9.37798   1.000 44.75467 ? 50   GLN A CD    1 
ATOM   362  O OE1   . GLN A 1 56  ? 6.55852   -4.40883  8.41253   1.000 48.64670 ? 50   GLN A OE1   1 
ATOM   363  N NE2   . GLN A 1 56  ? 7.84513   -3.55647  10.04424  1.000 44.77224 ? 50   GLN A NE2   1 
ATOM   364  N N     . TYR A 1 57  ? 2.64489   0.20685   9.94162   1.000 24.27916 ? 51   TYR A N     1 
ATOM   365  C CA    . TYR A 1 57  ? 1.65379   0.56714   8.94338   1.000 22.49563 ? 51   TYR A CA    1 
ATOM   366  C C     . TYR A 1 57  ? 1.93455   1.96049   8.38655   1.000 21.70825 ? 51   TYR A C     1 
ATOM   367  O O     . TYR A 1 57  ? 2.62522   2.78052   9.02992   1.000 21.74323 ? 51   TYR A O     1 
ATOM   368  C CB    . TYR A 1 57  ? 0.26514   0.45937   9.58368   1.000 21.12020 ? 51   TYR A CB    1 
ATOM   369  C CG    . TYR A 1 57  ? 0.01973   1.38526   10.76030  1.000 19.20490 ? 51   TYR A CG    1 
ATOM   370  C CD1   . TYR A 1 57  ? -0.31189  2.72063   10.55860  1.000 21.88161 ? 51   TYR A CD1   1 
ATOM   371  C CD2   . TYR A 1 57  ? 0.11649   0.91333   12.06069  1.000 22.49061 ? 51   TYR A CD2   1 
ATOM   372  C CE1   . TYR A 1 57  ? -0.55082  3.56433   11.62464  1.000 22.72899 ? 51   TYR A CE1   1 
ATOM   373  C CE2   . TYR A 1 57  ? -0.13280  1.74624   13.14079  1.000 25.98300 ? 51   TYR A CE2   1 
ATOM   374  C CZ    . TYR A 1 57  ? -0.46002  3.06179   12.91029  1.000 22.78321 ? 51   TYR A CZ    1 
ATOM   375  O OH    . TYR A 1 57  ? -0.70515  3.90102   13.96204  1.000 23.29767 ? 51   TYR A OH    1 
ATOM   376  N N     . PRO A 1 58  ? 1.39358   2.26709   7.20515   1.000 22.12090 ? 52   PRO A N     1 
ATOM   377  C CA    . PRO A 1 58  ? 1.62024   3.58380   6.59023   1.000 23.27652 ? 52   PRO A CA    1 
ATOM   378  C C     . PRO A 1 58  ? 1.06323   4.71948   7.43489   1.000 20.28107 ? 52   PRO A C     1 
ATOM   379  O O     . PRO A 1 58  ? -0.06258  4.65677   7.91373   1.000 21.91340 ? 52   PRO A O     1 
ATOM   380  C CB    . PRO A 1 58  ? 0.88251   3.48682   5.24117   1.000 27.17084 ? 52   PRO A CB    1 
ATOM   381  C CG    . PRO A 1 58  ? 0.49010   2.05488   5.05598   1.000 26.28765 ? 52   PRO A CG    1 
ATOM   382  C CD    . PRO A 1 58  ? 0.44355   1.43955   6.42523   1.000 24.34984 ? 52   PRO A CD    1 
ATOM   383  N N     . GLY A 1 59  ? 1.90160   5.73922   7.66110   1.000 22.63536 ? 53   GLY A N     1 
ATOM   384  C CA    . GLY A 1 59  ? 1.54412   6.90625   8.45255   1.000 23.27729 ? 53   GLY A CA    1 
ATOM   385  C C     . GLY A 1 59  ? 1.64241   6.77125   9.96470   1.000 20.91405 ? 53   GLY A C     1 
ATOM   386  O O     . GLY A 1 59  ? 1.24311   7.70656   10.68027  1.000 20.95569 ? 53   GLY A O     1 
ATOM   387  N N     . ALA A 1 60  ? 2.14811   5.65138   10.48643  1.000 18.19856 ? 54   ALA A N     1 
ATOM   388  C CA    . ALA A 1 60  ? 2.33149   5.52235   11.92973  1.000 21.28754 ? 54   ALA A CA    1 
ATOM   389  C C     . ALA A 1 60  ? 3.19221   6.67402   12.46318  1.000 23.17018 ? 54   ALA A C     1 
ATOM   390  O O     . ALA A 1 60  ? 4.26575   6.96068   11.93428  1.000 25.66842 ? 54   ALA A O     1 
ATOM   391  C CB    . ALA A 1 60  ? 3.00145   4.17077   12.25890  1.000 18.23742 ? 54   ALA A CB    1 
ATOM   392  N N     . LEU A 1 61  ? 2.70327   7.35030   13.49480  1.000 22.65186 ? 55   LEU A N     1 
ATOM   393  C CA    . LEU A 1 61  ? 3.26144   8.62766   13.91340  1.000 20.63774 ? 55   LEU A CA    1 
ATOM   394  C C     . LEU A 1 61  ? 2.96054   8.79157   15.39073  1.000 24.59267 ? 55   LEU A C     1 
ATOM   395  O O     . LEU A 1 61  ? 1.85790   8.45636   15.82409  1.000 23.99038 ? 55   LEU A O     1 
ATOM   396  C CB    . LEU A 1 61  ? 2.61536   9.80995   13.13018  1.000 19.46399 ? 55   LEU A CB    1 
ATOM   397  C CG    . LEU A 1 61  ? 3.23568   11.18847  13.31011  1.000 23.26593 ? 55   LEU A CG    1 
ATOM   398  C CD1   . LEU A 1 61  ? 4.62471   11.16883  12.75236  1.000 22.26550 ? 55   LEU A CD1   1 
ATOM   399  C CD2   . LEU A 1 61  ? 2.41136   12.32942  12.67013  1.000 20.49240 ? 55   LEU A CD2   1 
ATOM   400  N N     . SER A 1 62  ? 3.91616   9.32466   16.14943  1.000 20.96187 ? 56   SER A N     1 
ATOM   401  C CA    . SER A 1 62  ? 3.67568   9.61892   17.55632  1.000 19.29616 ? 56   SER A CA    1 
ATOM   402  C C     . SER A 1 62  ? 2.55199   10.63912  17.73985  1.000 21.28077 ? 56   SER A C     1 
ATOM   403  O O     . SER A 1 62  ? 2.27899   11.46652  16.87147  1.000 24.06875 ? 56   SER A O     1 
ATOM   404  C CB    . SER A 1 62  ? 4.94971   10.15273  18.23610  1.000 20.37776 ? 56   SER A CB    1 
ATOM   405  O OG    . SER A 1 62  ? 5.34510   11.44394  17.77072  1.000 21.81932 ? 56   SER A OG    1 
ATOM   406  N N     . ASP A 1 63  ? 1.89846   10.55712  18.89752  1.000 25.14411 ? 57   ASP A N     1 
ATOM   407  C CA    . ASP A 1 63  ? 0.90776   11.54135  19.31446  1.000 32.62603 ? 57   ASP A CA    1 
ATOM   408  C C     . ASP A 1 63  ? 1.55584   12.71486  20.04616  1.000 29.97030 ? 57   ASP A C     1 
ATOM   409  O O     . ASP A 1 63  ? 1.02788   13.83030  20.04479  1.000 29.37938 ? 57   ASP A O     1 
ATOM   410  C CB    . ASP A 1 63  ? -0.11638  10.85298  20.23127  1.000 35.01121 ? 57   ASP A CB    1 
ATOM   411  C CG    . ASP A 1 63  ? -1.31293  11.72326  20.52690  1.000 49.93000 ? 57   ASP A CG    1 
ATOM   412  O OD1   . ASP A 1 63  ? -2.01903  12.11564  19.56420  1.000 59.08866 ? 57   ASP A OD1   1 
ATOM   413  O OD2   . ASP A 1 63  ? -1.54613  12.01430  21.72164  1.000 46.13800 ? 57   ASP A OD2   1 
ATOM   414  N N     . SER A 1 64  ? 2.68686   12.48375  20.68580  1.000 22.72695 ? 58   SER A N     1 
ATOM   415  C CA    . SER A 1 64  ? 3.37891   13.56347  21.36828  1.000 24.59322 ? 58   SER A CA    1 
ATOM   416  C C     . SER A 1 64  ? 4.59387   14.01121  20.56834  1.000 21.37301 ? 58   SER A C     1 
ATOM   417  O O     . SER A 1 64  ? 5.12858   13.26291  19.75005  1.000 22.20980 ? 58   SER A O     1 
ATOM   418  C CB    . SER A 1 64  ? 3.76929   13.12203  22.77354  1.000 33.90125 ? 58   SER A CB    1 
ATOM   419  O OG    . SER A 1 64  ? 4.75377   12.12938  22.70497  1.000 33.58542 ? 58   SER A OG    1 
ATOM   420  N N     . GLU A 1 65  ? 5.01964   15.25115  20.82162  1.000 20.39438 ? 59   GLU A N     1 
ATOM   421  C CA    . GLU A 1 65  ? 6.09566   15.85539  20.05119  1.000 18.93961 ? 59   GLU A CA    1 
ATOM   422  C C     . GLU A 1 65  ? 7.39845   15.08226  20.25563  1.000 19.63859 ? 59   GLU A C     1 
ATOM   423  O O     . GLU A 1 65  ? 7.63592   14.49557  21.31464  1.000 20.42064 ? 59   GLU A O     1 
ATOM   424  C CB    . GLU A 1 65  ? 6.25060   17.32439  20.46247  1.000 17.94493 ? 59   GLU A CB    1 
ATOM   425  C CG    . GLU A 1 65  ? 5.04050   18.11815  20.01462  1.000 20.33985 ? 59   GLU A CG    1 
ATOM   426  C CD    . GLU A 1 65  ? 5.02605   19.54874  20.52062  1.000 32.48434 ? 59   GLU A CD    1 
ATOM   427  O OE1   . GLU A 1 65  ? 6.09285   20.20441  20.51401  1.000 30.39698 ? 59   GLU A OE1   1 
ATOM   428  O OE2   . GLU A 1 65  ? 3.93898   20.00193  20.94162  1.000 40.63935 ? 59   GLU A OE2   1 
ATOM   429  N N     . THR A 1 66  ? 8.23426   15.08516  19.21193  1.000 19.30991 ? 60   THR A N     1 
ATOM   430  C CA    . THR A 1 66  ? 9.43976   14.25571  19.16808  1.000 19.10483 ? 60   THR A CA    1 
ATOM   431  C C     . THR A 1 66  ? 10.32120  14.43617  20.39599  1.000 20.43305 ? 60   THR A C     1 
ATOM   432  O O     . THR A 1 66  ? 10.86389  13.46027  20.92793  1.000 21.10312 ? 60   THR A O     1 
ATOM   433  C CB    . THR A 1 66  ? 10.23702  14.61817  17.92727  1.000 18.51717 ? 60   THR A CB    1 
ATOM   434  O OG1   . THR A 1 66  ? 9.43481   14.36376  16.80740  1.000 18.91269 ? 60   THR A OG1   1 
ATOM   435  C CG2   . THR A 1 66  ? 11.55540  13.78252  17.82487  1.000 19.52931 ? 60   THR A CG2   1 
ATOM   436  N N     . HIS A 1 67  ? 10.50932  15.68193  20.82879  1.000 20.03775 ? 61   HIS A N     1 
ATOM   437  C CA    . HIS A 1 67  ? 11.46896  15.95257  21.89482  1.000 18.03018 ? 61   HIS A CA    1 
ATOM   438  C C     . HIS A 1 67  ? 10.99287  15.50560  23.26325  1.000 22.74905 ? 61   HIS A C     1 
ATOM   439  O O     . HIS A 1 67  ? 11.78248  15.56567  24.21193  1.000 24.10177 ? 61   HIS A O     1 
ATOM   440  C CB    . HIS A 1 67  ? 11.79697  17.45283  21.93947  1.000 22.66879 ? 61   HIS A CB    1 
ATOM   441  C CG    . HIS A 1 67  ? 10.63941  18.31165  22.35676  1.000 23.29078 ? 61   HIS A CG    1 
ATOM   442  N ND1   . HIS A 1 67  ? 9.56826   18.57487  21.52151  1.000 25.00006 ? 61   HIS A ND1   1 
ATOM   443  C CD2   . HIS A 1 67  ? 10.39013  18.97593  23.51109  1.000 24.08807 ? 61   HIS A CD2   1 
ATOM   444  C CE1   . HIS A 1 67  ? 8.70855   19.35802  22.15551  1.000 29.30899 ? 61   HIS A CE1   1 
ATOM   445  N NE2   . HIS A 1 67  ? 9.18434   19.61673  23.36297  1.000 23.58816 ? 61   HIS A NE2   1 
ATOM   446  N N     . LEU A 1 68  ? 9.73453   15.07585  23.38808  1.000 21.76674 ? 62   LEU A N     1 
ATOM   447  C CA    . LEU A 1 68  ? 9.16916   14.56899  24.63057  1.000 22.72700 ? 62   LEU A CA    1 
ATOM   448  C C     . LEU A 1 68  ? 8.82924   13.08202  24.56914  1.000 22.88719 ? 62   LEU A C     1 
ATOM   449  O O     . LEU A 1 68  ? 8.54181   12.48998  25.61202  1.000 25.87127 ? 62   LEU A O     1 
ATOM   450  C CB    . LEU A 1 68  ? 7.87612   15.32694  24.97358  1.000 25.70164 ? 62   LEU A CB    1 
ATOM   451  C CG    . LEU A 1 68  ? 8.05915   16.81317  25.27141  1.000 31.30833 ? 62   LEU A CG    1 
ATOM   452  C CD1   . LEU A 1 68  ? 6.70594   17.44766  25.56096  1.000 31.39406 ? 62   LEU A CD1   1 
ATOM   453  C CD2   . LEU A 1 68  ? 8.99723   16.94516  26.44227  1.000 27.61864 ? 62   LEU A CD2   1 
ATOM   454  N N     . TYR A 1 69  ? 8.79067   12.49035  23.37266  1.000 20.64991 ? 63   TYR A N     1 
ATOM   455  C CA    . TYR A 1 69  ? 8.44776   11.07300  23.22224  1.000 21.83503 ? 63   TYR A CA    1 
ATOM   456  C C     . TYR A 1 69  ? 9.72761   10.25091  23.25280  1.000 21.15602 ? 63   TYR A C     1 
ATOM   457  O O     . TYR A 1 69  ? 10.17936  9.69146   22.25381  1.000 22.44764 ? 63   TYR A O     1 
ATOM   458  C CB    . TYR A 1 69  ? 7.66202   10.84352  21.93271  1.000 19.88421 ? 63   TYR A CB    1 
ATOM   459  C CG    . TYR A 1 69  ? 7.06776   9.46363   21.95349  1.000 20.25367 ? 63   TYR A CG    1 
ATOM   460  C CD1   . TYR A 1 69  ? 6.10501   9.12032   22.91698  1.000 25.36181 ? 63   TYR A CD1   1 
ATOM   461  C CD2   . TYR A 1 69  ? 7.45145   8.51744   21.03091  1.000 24.07255 ? 63   TYR A CD2   1 
ATOM   462  C CE1   . TYR A 1 69  ? 5.55658   7.83962   22.97147  1.000 24.52450 ? 63   TYR A CE1   1 
ATOM   463  C CE2   . TYR A 1 69  ? 6.88345   7.22338   21.05089  1.000 22.11142 ? 63   TYR A CE2   1 
ATOM   464  C CZ    . TYR A 1 69  ? 5.95199   6.90435   22.03534  1.000 26.45159 ? 63   TYR A CZ    1 
ATOM   465  O OH    . TYR A 1 69  ? 5.39583   5.63841   22.07486  1.000 27.20901 ? 63   TYR A OH    1 
ATOM   466  N N     . CYS A 1 70  ? 10.35320  10.24170  24.43220  1.000 20.93260 ? 64   CYS A N     1 
ATOM   467  C CA    . CYS A 1 70  ? 11.69152  9.69418   24.56744  1.000 23.38858 ? 64   CYS A CA    1 
ATOM   468  C C     . CYS A 1 70  ? 12.02673  9.63997   26.04772  1.000 22.90284 ? 64   CYS A C     1 
ATOM   469  O O     . CYS A 1 70  ? 11.29924  10.17049  26.88955  1.000 22.57876 ? 64   CYS A O     1 
ATOM   470  C CB    . CYS A 1 70  ? 12.71128  10.53378  23.80447  1.000 25.54437 ? 64   CYS A CB    1 
ATOM   471  S SG    . CYS A 1 70  ? 12.76653  12.28930  24.46083  1.000 23.97111 ? 64   CYS A SG    1 
ATOM   472  N N     . TYR A 1 71  ? 13.13901  8.97874   26.35389  1.000 20.96411 ? 65   TYR A N     1 
ATOM   473  C CA    . TYR A 1 71  ? 13.60535  8.93312   27.73083  1.000 23.54332 ? 65   TYR A CA    1 
ATOM   474  C C     . TYR A 1 71  ? 14.21734  10.26565  28.15023  1.000 23.23747 ? 65   TYR A C     1 
ATOM   475  O O     . TYR A 1 71  ? 14.82393  10.97097  27.34964  1.000 27.10009 ? 65   TYR A O     1 
ATOM   476  C CB    . TYR A 1 71  ? 14.65763  7.86108   27.89373  1.000 22.65562 ? 65   TYR A CB    1 
ATOM   477  C CG    . TYR A 1 71  ? 14.15269  6.46012   27.67524  1.000 22.85831 ? 65   TYR A CG    1 
ATOM   478  C CD1   . TYR A 1 71  ? 13.18553  5.91745   28.49148  1.000 22.95365 ? 65   TYR A CD1   1 
ATOM   479  C CD2   . TYR A 1 71  ? 14.73765  5.65451   26.71421  1.000 22.85565 ? 65   TYR A CD2   1 
ATOM   480  C CE1   . TYR A 1 71  ? 12.76951  4.57602   28.31871  1.000 21.16155 ? 65   TYR A CE1   1 
ATOM   481  C CE2   . TYR A 1 71  ? 14.34464  4.32930   26.54938  1.000 22.42913 ? 65   TYR A CE2   1 
ATOM   482  C CZ    . TYR A 1 71  ? 13.35910  3.81326   27.34434  1.000 21.14375 ? 65   TYR A CZ    1 
ATOM   483  O OH    . TYR A 1 71  ? 12.98792  2.49792   27.14635  1.000 24.51235 ? 65   TYR A OH    1 
ATOM   484  N N     . SER A 1 72  ? 14.09166  10.57079  29.43796  1.000 26.30971 ? 66   SER A N     1 
ATOM   485  C CA    . SER A 1 72  ? 14.68689  11.76235  30.02960  1.000 25.15592 ? 66   SER A CA    1 
ATOM   486  C C     . SER A 1 72  ? 15.84322  11.45641  30.96897  1.000 28.76376 ? 66   SER A C     1 
ATOM   487  O O     . SER A 1 72  ? 16.51186  12.40088  31.42873  1.000 31.34448 ? 66   SER A O     1 
ATOM   488  C CB    . SER A 1 72  ? 13.63316  12.53253  30.81375  1.000 26.25383 ? 66   SER A CB    1 
ATOM   489  O OG    . SER A 1 72  ? 13.45966  11.88945  32.05007  1.000 29.59478 ? 66   SER A OG    1 
ATOM   490  N N     . TRP A 1 73  ? 16.10307  10.17633  31.25397  1.000 26.95250 ? 67   TRP A N     1 
ATOM   491  C CA    . TRP A 1 73  ? 17.04499  9.80661   32.31101  1.000 35.09842 ? 67   TRP A CA    1 
ATOM   492  C C     . TRP A 1 73  ? 18.49764  9.81112   31.86008  1.000 34.50803 ? 67   TRP A C     1 
ATOM   493  O O     . TRP A 1 73  ? 19.39331  9.75870   32.71402  1.000 33.69774 ? 67   TRP A O     1 
ATOM   494  C CB    . TRP A 1 73  ? 16.67756  8.41925   32.88100  1.000 31.73928 ? 67   TRP A CB    1 
ATOM   495  C CG    . TRP A 1 73  ? 16.60821  7.31821   31.87397  1.000 32.22825 ? 67   TRP A CG    1 
ATOM   496  C CD1   . TRP A 1 73  ? 15.48609  6.84629   31.26351  1.000 28.94674 ? 67   TRP A CD1   1 
ATOM   497  C CD2   . TRP A 1 73  ? 17.69549  6.53038   31.36908  1.000 31.64270 ? 67   TRP A CD2   1 
ATOM   498  N NE1   . TRP A 1 73  ? 15.80122  5.82724   30.41120  1.000 27.21181 ? 67   TRP A NE1   1 
ATOM   499  C CE2   . TRP A 1 73  ? 17.14629  5.60023   30.45931  1.000 29.59054 ? 67   TRP A CE2   1 
ATOM   500  C CE3   . TRP A 1 73  ? 19.07584  6.51867   31.59855  1.000 31.85273 ? 67   TRP A CE3   1 
ATOM   501  C CZ2   . TRP A 1 73  ? 17.92510  4.66115   29.77631  1.000 28.86241 ? 67   TRP A CZ2   1 
ATOM   502  C CZ3   . TRP A 1 73  ? 19.85719  5.56832   30.92726  1.000 37.19677 ? 67   TRP A CZ3   1 
ATOM   503  C CH2   . TRP A 1 73  ? 19.26972  4.66359   30.01490  1.000 35.19356 ? 67   TRP A CH2   1 
ATOM   504  N N     . ASP A 1 74  ? 18.75911  9.84456   30.55890  1.000 30.90810 ? 68   ASP A N     1 
ATOM   505  C CA    . ASP A 1 74  ? 20.11597  9.87701   30.02643  1.000 32.95862 ? 68   ASP A CA    1 
ATOM   506  C C     . ASP A 1 74  ? 20.32188  11.24099  29.36058  1.000 36.18573 ? 68   ASP A C     1 
ATOM   507  O O     . ASP A 1 74  ? 19.89033  11.46804  28.22237  1.000 29.49344 ? 68   ASP A O     1 
ATOM   508  C CB    . ASP A 1 74  ? 20.34695  8.71082   29.07286  1.000 32.55906 ? 68   ASP A CB    1 
ATOM   509  C CG    . ASP A 1 74  ? 21.76333  8.67443   28.50650  1.000 35.47197 ? 68   ASP A CG    1 
ATOM   510  O OD1   . ASP A 1 74  ? 22.46322  9.70935   28.57712  1.000 36.02992 ? 68   ASP A OD1   1 
ATOM   511  O OD2   . ASP A 1 74  ? 22.19348  7.59380   28.01792  1.000 38.70116 ? 68   ASP A OD2   1 
ATOM   512  N N     . LYS A 1 75  ? 21.01008  12.15171  30.06543  1.000 34.40030 ? 69   LYS A N     1 
ATOM   513  C CA    . LYS A 1 75  ? 21.13401  13.50860  29.53880  1.000 33.52346 ? 69   LYS A CA    1 
ATOM   514  C C     . LYS A 1 75  ? 22.00217  13.56703  28.29169  1.000 32.56177 ? 69   LYS A C     1 
ATOM   515  O O     . LYS A 1 75  ? 21.76333  14.41180  27.42409  1.000 33.30399 ? 69   LYS A O     1 
ATOM   516  C CB    . LYS A 1 75  ? 21.67036  14.45472  30.62024  1.000 34.03129 ? 69   LYS A CB    1 
ATOM   517  C CG    . LYS A 1 75  ? 20.78971  14.45352  31.85977  1.000 40.97952 ? 69   LYS A CG    1 
ATOM   518  C CD    . LYS A 1 75  ? 20.86702  15.77732  32.59576  1.000 47.72201 ? 69   LYS A CD    1 
ATOM   519  C CE    . LYS A 1 75  ? 19.62017  16.01367  33.42634  1.000 53.31379 ? 69   LYS A CE    1 
ATOM   520  N NZ    . LYS A 1 75  ? 19.62595  17.37338  34.03571  1.000 52.57956 ? 69   LYS A NZ    1 
ATOM   521  N N     . GLU A 1 76  ? 22.98607  12.67462  28.15948  1.000 29.16236 ? 70   GLU A N     1 
ATOM   522  C CA    . GLU A 1 76  ? 23.80234  12.66604  26.95236  1.000 34.22882 ? 70   GLU A CA    1 
ATOM   523  C C     . GLU A 1 76  ? 22.97416  12.26569  25.73833  1.000 36.88105 ? 70   GLU A C     1 
ATOM   524  O O     . GLU A 1 76  ? 23.09634  12.86424  24.66081  1.000 33.93355 ? 70   GLU A O     1 
ATOM   525  C CB    . GLU A 1 76  ? 25.00807  11.73977  27.12010  1.000 40.23039 ? 70   GLU A CB    1 
ATOM   526  C CG    . GLU A 1 76  ? 26.04203  12.24581  28.13581  1.000 51.99472 ? 70   GLU A CG    1 
ATOM   527  C CD    . GLU A 1 76  ? 25.95040  11.57765  29.50193  1.000 62.16264 ? 70   GLU A CD    1 
ATOM   528  O OE1   . GLU A 1 76  ? 26.98541  11.54049  30.21124  1.000 68.34868 ? 70   GLU A OE1   1 
ATOM   529  O OE2   . GLU A 1 76  ? 24.84947  11.11836  29.87949  1.000 70.76267 ? 70   GLU A OE2   1 
ATOM   530  N N     . LEU A 1 77  ? 22.11074  11.26840  25.90442  1.000 31.24828 ? 71   LEU A N     1 
ATOM   531  C CA    . LEU A 1 77  ? 21.18225  10.90639  24.84132  1.000 32.52981 ? 71   LEU A CA    1 
ATOM   532  C C     . LEU A 1 77  ? 20.29787  12.08227  24.43824  1.000 30.47976 ? 71   LEU A C     1 
ATOM   533  O O     . LEU A 1 77  ? 20.09888  12.32462  23.24484  1.000 30.17949 ? 71   LEU A O     1 
ATOM   534  C CB    . LEU A 1 77  ? 20.32435  9.73723   25.29249  1.000 30.76475 ? 71   LEU A CB    1 
ATOM   535  C CG    . LEU A 1 77  ? 19.72186  8.90430   24.18627  1.000 40.14323 ? 71   LEU A CG    1 
ATOM   536  C CD1   . LEU A 1 77  ? 20.74897  8.65071   23.08801  1.000 42.85685 ? 71   LEU A CD1   1 
ATOM   537  C CD2   . LEU A 1 77  ? 19.28627  7.61927   24.86979  1.000 40.58749 ? 71   LEU A CD2   1 
ATOM   538  N N     . LEU A 1 78  ? 19.74169  12.80590  25.41988  1.000 26.53627 ? 72   LEU A N     1 
ATOM   539  C CA    . LEU A 1 78  ? 18.93516  13.98295  25.09443  1.000 28.29478 ? 72   LEU A CA    1 
ATOM   540  C C     . LEU A 1 78  ? 19.71193  14.95005  24.21427  1.000 28.88975 ? 72   LEU A C     1 
ATOM   541  O O     . LEU A 1 78  ? 19.18107  15.43879  23.21763  1.000 30.23217 ? 72   LEU A O     1 
ATOM   542  C CB    . LEU A 1 78  ? 18.45189  14.68720  26.36418  1.000 28.54409 ? 72   LEU A CB    1 
ATOM   543  C CG    . LEU A 1 78  ? 17.40081  13.97713  27.21830  1.000 29.53569 ? 72   LEU A CG    1 
ATOM   544  C CD1   . LEU A 1 78  ? 17.18506  14.72757  28.53659  1.000 36.49590 ? 72   LEU A CD1   1 
ATOM   545  C CD2   . LEU A 1 78  ? 16.09835  13.82974  26.43905  1.000 29.59567 ? 72   LEU A CD2   1 
ATOM   546  N N     . GLN A 1 79  ? 20.98355  15.22606  24.54611  1.000 32.62335 ? 73   GLN A N     1 
ATOM   547  C CA    . GLN A 1 79  ? 21.75979  16.14544  23.70512  1.000 30.88310 ? 73   GLN A CA    1 
ATOM   548  C C     . GLN A 1 79  ? 22.06607  15.55691  22.33651  1.000 33.80523 ? 73   GLN A C     1 
ATOM   549  O O     . GLN A 1 79  ? 22.13840  16.29728  21.33780  1.000 30.76748 ? 73   GLN A O     1 
ATOM   550  C CB    . GLN A 1 79  ? 23.03704  16.56778  24.43471  1.000 35.99597 ? 73   GLN A CB    1 
ATOM   551  C CG    . GLN A 1 79  ? 22.70088  17.36410  25.69358  1.000 37.00952 ? 73   GLN A CG    1 
ATOM   552  C CD    . GLN A 1 79  ? 21.90784  18.62803  25.36340  1.000 35.88058 ? 73   GLN A CD    1 
ATOM   553  O OE1   . GLN A 1 79  ? 22.21226  19.31812  24.38530  1.000 32.16850 ? 73   GLN A OE1   1 
ATOM   554  N NE2   . GLN A 1 79  ? 20.88071  18.93455  26.17686  1.000 33.82748 ? 73   GLN A NE2   1 
ATOM   555  N N     . GLU A 1 80  ? 22.20063  14.23101  22.26483  1.000 31.63977 ? 74   GLU A N     1 
ATOM   556  C CA    . GLU A 1 80  ? 22.41242  13.49037  21.03154  1.000 31.65063 ? 74   GLU A CA    1 
ATOM   557  C C     . GLU A 1 80  ? 21.12071  13.31072  20.22507  1.000 32.04613 ? 74   GLU A C     1 
ATOM   558  O O     . GLU A 1 80  ? 21.20040  12.94099  19.05270  1.000 33.05143 ? 74   GLU A O     1 
ATOM   559  C CB    . GLU A 1 80  ? 23.02682  12.12481  21.38334  1.000 34.33852 ? 74   GLU A CB    1 
ATOM   560  C CG    . GLU A 1 80  ? 23.74373  11.35550  20.27226  1.000 49.01102 ? 74   GLU A CG    1 
ATOM   561  C CD    . GLU A 1 80  ? 24.08490  9.89560   20.68753  1.000 66.27903 ? 74   GLU A CD    1 
ATOM   562  O OE1   . GLU A 1 80  ? 24.89285  9.70027   21.62728  1.000 63.56415 ? 74   GLU A OE1   1 
ATOM   563  O OE2   . GLU A 1 80  ? 23.53855  8.93842   20.08576  1.000 63.57708 ? 74   GLU A OE2   1 
ATOM   564  N N     . MET A 1 81  ? 19.96085  13.60912  20.82042  1.000 36.21640 ? 75   MET A N     1 
ATOM   565  C CA    . MET A 1 81  ? 18.64925  13.36245  20.20784  1.000 37.98874 ? 75   MET A CA    1 
ATOM   566  C C     . MET A 1 81  ? 18.56873  13.85843  18.77701  1.000 32.75381 ? 75   MET A C     1 
ATOM   567  O O     . MET A 1 81  ? 18.78675  15.04208  18.49720  1.000 30.35431 ? 75   MET A O     1 
ATOM   568  C CB    . MET A 1 81  ? 17.52475  14.04488  21.00071  1.000 33.28526 ? 75   MET A CB    1 
ATOM   569  C CG    . MET A 1 81  ? 16.98546  13.25495  22.17247  1.000 36.54863 ? 75   MET A CG    1 
ATOM   570  S SD    . MET A 1 81  ? 15.79477  11.97824  21.66411  1.000 32.19545 ? 75   MET A SD    1 
ATOM   571  C CE    . MET A 1 81  ? 14.40414  12.93642  21.02663  1.000 30.73360 ? 75   MET A CE    1 
ATOM   572  N N     . GLU A 1 82  ? 18.16124  12.96579  17.88467  1.000 29.78946 ? 76   GLU A N     1 
ATOM   573  C CA    . GLU A 1 82  ? 17.77013  13.38802  16.54572  1.000 30.51708 ? 76   GLU A CA    1 
ATOM   574  C C     . GLU A 1 82  ? 16.33514  13.90118  16.61789  1.000 31.49224 ? 76   GLU A C     1 
ATOM   575  O O     . GLU A 1 82  ? 15.43055  13.16241  17.03253  1.000 28.41758 ? 76   GLU A O     1 
ATOM   576  C CB    . GLU A 1 82  ? 17.88273  12.21538  15.58222  1.000 32.00024 ? 76   GLU A CB    1 
ATOM   577  C CG    . GLU A 1 82  ? 17.81909  12.60421  14.12009  1.000 37.99977 ? 76   GLU A CG    1 
ATOM   578  C CD    . GLU A 1 82  ? 17.89241  11.38049  13.21630  1.000 54.73992 ? 76   GLU A CD    1 
ATOM   579  O OE1   . GLU A 1 82  ? 18.73122  10.47864  13.49871  1.000 49.84112 ? 76   GLU A OE1   1 
ATOM   580  O OE2   . GLU A 1 82  ? 17.11713  11.32615  12.23798  1.000 54.47844 ? 76   GLU A OE2   1 
ATOM   581  N N     . ILE A 1 83  ? 16.12369  15.16620  16.24170  1.000 27.92552 ? 77   ILE A N     1 
ATOM   582  C CA    . ILE A 1 83  ? 14.78753  15.75340  16.26043  1.000 23.97910 ? 77   ILE A CA    1 
ATOM   583  C C     . ILE A 1 83  ? 14.50737  16.24250  14.85356  1.000 25.51368 ? 77   ILE A C     1 
ATOM   584  O O     . ILE A 1 83  ? 14.76114  17.40177  14.52398  1.000 28.23824 ? 77   ILE A O     1 
ATOM   585  C CB    . ILE A 1 83  ? 14.66314  16.88885  17.29719  1.000 26.73328 ? 77   ILE A CB    1 
ATOM   586  C CG1   . ILE A 1 83  ? 15.04540  16.36257  18.67766  1.000 23.15893 ? 77   ILE A CG1   1 
ATOM   587  C CG2   . ILE A 1 83  ? 13.22302  17.43286  17.34391  1.000 22.13125 ? 77   ILE A CG2   1 
ATOM   588  C CD1   . ILE A 1 83  ? 14.88173  17.35334  19.76220  1.000 24.41956 ? 77   ILE A CD1   1 
ATOM   589  N N     . LYS A 1 84  ? 14.03742  15.34156  13.99663  1.000 20.24574 ? 78   LYS A N     1 
ATOM   590  C CA    . LYS A 1 84  ? 13.93034  15.66430  12.57900  1.000 23.79562 ? 78   LYS A CA    1 
ATOM   591  C C     . LYS A 1 84  ? 12.64529  16.45555  12.27833  1.000 24.27643 ? 78   LYS A C     1 
ATOM   592  O O     . LYS A 1 84  ? 12.67017  17.47501  11.57711  1.000 21.10218 ? 78   LYS A O     1 
ATOM   593  C CB    . LYS A 1 84  ? 13.99297  14.35198  11.78700  1.000 24.84886 ? 78   LYS A CB    1 
ATOM   594  C CG    . LYS A 1 84  ? 13.67089  14.46500  10.34130  1.000 27.56755 ? 78   LYS A CG    1 
ATOM   595  C CD    . LYS A 1 84  ? 13.97193  13.18521  9.56039   1.000 35.33520 ? 78   LYS A CD    1 
ATOM   596  C CE    . LYS A 1 84  ? 13.77763  11.91696  10.36356  1.000 38.69203 ? 78   LYS A CE    1 
ATOM   597  N NZ    . LYS A 1 84  ? 14.11997  10.66405  9.57126   1.000 35.62178 ? 78   LYS A NZ    1 
ATOM   598  N N     . ARG A 1 85  ? 11.50178  15.97494  12.75957  1.000 22.41014 ? 79   ARG A N     1 
ATOM   599  C CA    . ARG A 1 85  ? 10.22573  16.64883  12.55968  1.000 18.85676 ? 79   ARG A CA    1 
ATOM   600  C C     . ARG A 1 85  ? 9.58072   16.81108  13.92655  1.000 18.32147 ? 79   ARG A C     1 
ATOM   601  O O     . ARG A 1 85  ? 10.04161  16.22622  14.92377  1.000 20.48459 ? 79   ARG A O     1 
ATOM   602  C CB    . ARG A 1 85  ? 9.34340   15.85497  11.57477  1.000 19.90640 ? 79   ARG A CB    1 
ATOM   603  C CG    . ARG A 1 85  ? 9.73391   16.02479  10.10351  1.000 18.08260 ? 79   ARG A CG    1 
ATOM   604  C CD    . ARG A 1 85  ? 8.77914   15.25848  9.14850   1.000 23.92339 ? 79   ARG A CD    1 
ATOM   605  N NE    . ARG A 1 85  ? 8.93047   13.84563  9.47534   1.000 36.21128 ? 79   ARG A NE    1 
ATOM   606  C CZ    . ARG A 1 85  ? 9.81312   13.02574  8.91871   1.000 40.10275 ? 79   ARG A CZ    1 
ATOM   607  N NH1   . ARG A 1 85  ? 10.50092  13.38149  7.83116   1.000 28.47349 ? 79   ARG A NH1   1 
ATOM   608  N NH2   . ARG A 1 85  ? 10.01314  11.82008  9.46982   1.000 33.05753 ? 79   ARG A NH2   1 
ATOM   609  N N     . LYS A 1 86  ? 8.49117   17.58280  13.96436  1.000 18.45291 ? 80   LYS A N     1 
ATOM   610  C CA    . LYS A 1 86  ? 7.87293   17.94627  15.23638  1.000 20.54586 ? 80   LYS A CA    1 
ATOM   611  C C     . LYS A 1 86  ? 7.34493   16.73165  15.98244  1.000 18.01966 ? 80   LYS A C     1 
ATOM   612  O O     . LYS A 1 86  ? 7.34769   16.70875  17.22633  1.000 22.54549 ? 80   LYS A O     1 
ATOM   613  C CB    . LYS A 1 86  ? 6.75180   18.97192  14.99303  1.000 21.60704 ? 80   LYS A CB    1 
ATOM   614  C CG    . LYS A 1 86  ? 6.22913   19.59544  16.27268  1.000 21.32895 ? 80   LYS A CG    1 
ATOM   615  C CD    . LYS A 1 86  ? 5.36510   20.83099  15.90896  1.000 25.37512 ? 80   LYS A CD    1 
ATOM   616  C CE    . LYS A 1 86  ? 4.89389   21.56526  17.12499  1.000 33.14288 ? 80   LYS A CE    1 
ATOM   617  N NZ    . LYS A 1 86  ? 4.48394   22.94335  16.71531  1.000 40.34396 ? 80   LYS A NZ    1 
ATOM   618  N N     . TYR A 1 87  ? 6.88295   15.72904  15.24609  1.000 16.61302 ? 81   TYR A N     1 
ATOM   619  C CA    . TYR A 1 87  ? 6.42946   14.43654  15.72627  1.000 17.57232 ? 81   TYR A CA    1 
ATOM   620  C C     . TYR A 1 87  ? 7.30600   13.37193  15.09265  1.000 19.78405 ? 81   TYR A C     1 
ATOM   621  O O     . TYR A 1 87  ? 8.03888   13.64432  14.12853  1.000 21.37436 ? 81   TYR A O     1 
ATOM   622  C CB    . TYR A 1 87  ? 4.93081   14.20213  15.37792  1.000 17.39565 ? 81   TYR A CB    1 
ATOM   623  C CG    . TYR A 1 87  ? 4.09073   15.25041  16.06741  1.000 19.24708 ? 81   TYR A CG    1 
ATOM   624  C CD1   . TYR A 1 87  ? 3.93380   16.53109  15.52668  1.000 19.60644 ? 81   TYR A CD1   1 
ATOM   625  C CD2   . TYR A 1 87  ? 3.54319   14.98856  17.32584  1.000 22.81880 ? 81   TYR A CD2   1 
ATOM   626  C CE1   . TYR A 1 87  ? 3.19360   17.49189  16.20337  1.000 20.49609 ? 81   TYR A CE1   1 
ATOM   627  C CE2   . TYR A 1 87  ? 2.79950   15.95590  17.99883  1.000 24.62646 ? 81   TYR A CE2   1 
ATOM   628  C CZ    . TYR A 1 87  ? 2.63302   17.18635  17.44033  1.000 26.01632 ? 81   TYR A CZ    1 
ATOM   629  O OH    . TYR A 1 87  ? 1.90669   18.12253  18.15927  1.000 27.44752 ? 81   TYR A OH    1 
ATOM   630  N N     . ILE A 1 88  ? 7.24647   12.14154  15.60595  1.000 19.18347 ? 82   ILE A N     1 
ATOM   631  C CA    . ILE A 1 88  ? 8.25409   11.15375  15.20085  1.000 20.65987 ? 82   ILE A CA    1 
ATOM   632  C C     . ILE A 1 88  ? 7.58332   9.91164   14.60039  1.000 21.46286 ? 82   ILE A C     1 
ATOM   633  O O     . ILE A 1 88  ? 6.58450   9.39122   15.12663  1.000 18.80487 ? 82   ILE A O     1 
ATOM   634  C CB    . ILE A 1 88  ? 9.23519   10.81919  16.35435  1.000 17.97692 ? 82   ILE A CB    1 
ATOM   635  C CG1   . ILE A 1 88  ? 10.29153  9.82400   15.85649  1.000 19.09122 ? 82   ILE A CG1   1 
ATOM   636  C CG2   . ILE A 1 88  ? 8.51895   10.31807  17.61732  1.000 17.76891 ? 82   ILE A CG2   1 
ATOM   637  C CD1   . ILE A 1 88  ? 11.57927  9.76330   16.72561  1.000 19.59909 ? 82   ILE A CD1   1 
ATOM   638  N N     . SER A 1 89  ? 8.09179   9.50199   13.45085  1.000 18.57789 ? 83   SER A N     1 
ATOM   639  C CA    . SER A 1 89  ? 7.55823   8.38115   12.69153  1.000 20.88205 ? 83   SER A CA    1 
ATOM   640  C C     . SER A 1 89  ? 8.01211   7.07135   13.29668  1.000 23.05845 ? 83   SER A C     1 
ATOM   641  O O     . SER A 1 89  ? 9.04164   7.00796   13.96751  1.000 21.20375 ? 83   SER A O     1 
ATOM   642  C CB    . SER A 1 89  ? 8.05416   8.44578   11.24851  1.000 24.87553 ? 83   SER A CB    1 
ATOM   643  O OG    . SER A 1 89  ? 7.57491   9.62790   10.62794  1.000 35.21571 ? 83   SER A OG    1 
ATOM   644  N N     . GLN A 1 90  ? 7.27576   5.99957   12.96055  1.000 24.33116 ? 84   GLN A N     1 
ATOM   645  C CA    . GLN A 1 90  ? 7.58238   4.68071   13.50332  1.000 21.33913 ? 84   GLN A CA    1 
ATOM   646  C C     . GLN A 1 90  ? 9.01761   4.24878   13.21794  1.000 23.85190 ? 84   GLN A C     1 
ATOM   647  O O     . GLN A 1 90  ? 9.70153   3.80489   14.15930  1.000 19.96381 ? 84   GLN A O     1 
ATOM   648  C CB    . GLN A 1 90  ? 6.54298   3.65919   12.99098  1.000 21.81615 ? 84   GLN A CB    1 
ATOM   649  C CG    . GLN A 1 90  ? 6.88428   2.21230   13.31321  1.000 22.75589 ? 84   GLN A CG    1 
ATOM   650  C CD    . GLN A 1 90  ? 7.73028   1.54755   12.27758  1.000 26.13159 ? 84   GLN A CD    1 
ATOM   651  O OE1   . GLN A 1 90  ? 7.57833   1.81532   11.07618  1.000 28.48258 ? 84   GLN A OE1   1 
ATOM   652  N NE2   . GLN A 1 90  ? 8.57926   0.61160   12.71451  1.000 23.76241 ? 84   GLN A NE2   1 
ATOM   653  N N     . PRO A 1 91  ? 9.55081   4.36175   11.99784  1.000 23.23350 ? 85   PRO A N     1 
ATOM   654  C CA    . PRO A 1 91  ? 10.92923  3.90719   11.78816  1.000 22.82942 ? 85   PRO A CA    1 
ATOM   655  C C     . PRO A 1 91  ? 11.92461  4.66501   12.63862  1.000 24.16702 ? 85   PRO A C     1 
ATOM   656  O O     . PRO A 1 91  ? 12.93870  4.08621   13.06553  1.000 22.87881 ? 85   PRO A O     1 
ATOM   657  C CB    . PRO A 1 91  ? 11.16316  4.15820   10.28827  1.000 29.69981 ? 85   PRO A CB    1 
ATOM   658  C CG    . PRO A 1 91  ? 9.81042   4.23698   9.69752   1.000 32.45368 ? 85   PRO A CG    1 
ATOM   659  C CD    . PRO A 1 91  ? 8.95141   4.84909   10.74053  1.000 26.91789 ? 85   PRO A CD    1 
ATOM   660  N N     . ASP A 1 92  ? 11.62966  5.92964   12.95254  1.000 22.43073 ? 86   ASP A N     1 
ATOM   661  C CA    . ASP A 1 92  ? 12.56276  6.73699   13.73684  1.000 20.00204 ? 86   ASP A CA    1 
ATOM   662  C C     . ASP A 1 92  ? 12.46496  6.44797   15.22016  1.000 19.15064 ? 86   ASP A C     1 
ATOM   663  O O     . ASP A 1 92  ? 13.47350  6.52620   15.92059  1.000 20.92729 ? 86   ASP A O     1 
ATOM   664  C CB    . ASP A 1 92  ? 12.31113  8.20839   13.44165  1.000 22.33490 ? 86   ASP A CB    1 
ATOM   665  C CG    . ASP A 1 92  ? 12.72448  8.56105   12.03519  1.000 32.72636 ? 86   ASP A CG    1 
ATOM   666  O OD1   . ASP A 1 92  ? 13.54666  7.80451   11.46022  1.000 31.88637 ? 86   ASP A OD1   1 
ATOM   667  O OD2   . ASP A 1 92  ? 12.17014  9.50322   11.46652  1.000 29.38823 ? 86   ASP A OD2   1 
ATOM   668  N N     . VAL A 1 93  ? 11.27864  6.10803   15.72425  1.000 20.86774 ? 87   VAL A N     1 
ATOM   669  C CA    . VAL A 1 93  ? 11.20442  5.65852   17.10400  1.000 19.80465 ? 87   VAL A CA    1 
ATOM   670  C C     . VAL A 1 93  ? 11.93437  4.33666   17.24214  1.000 19.50076 ? 87   VAL A C     1 
ATOM   671  O O     . VAL A 1 93  ? 12.66125  4.10402   18.20676  1.000 19.93322 ? 87   VAL A O     1 
ATOM   672  C CB    . VAL A 1 93  ? 9.75401   5.49213   17.56942  1.000 18.91807 ? 87   VAL A CB    1 
ATOM   673  C CG1   . VAL A 1 93  ? 9.77913   4.98921   19.00136  1.000 21.72525 ? 87   VAL A CG1   1 
ATOM   674  C CG2   . VAL A 1 93  ? 8.94420   6.78722   17.47534  1.000 18.03543 ? 87   VAL A CG2   1 
ATOM   675  N N     . LEU A 1 94  ? 11.69872  3.43003   16.29179  1.000 21.84413 ? 88   LEU A N     1 
ATOM   676  C CA    . LEU A 1 94  ? 12.36465  2.13117   16.35151  1.000 26.53657 ? 88   LEU A CA    1 
ATOM   677  C C     . LEU A 1 94  ? 13.87909  2.31799   16.33602  1.000 21.57522 ? 88   LEU A C     1 
ATOM   678  O O     . LEU A 1 94  ? 14.60488  1.74647   17.16314  1.000 23.27414 ? 88   LEU A O     1 
ATOM   679  C CB    . LEU A 1 94  ? 11.89078  1.27553   15.17796  1.000 19.91380 ? 88   LEU A CB    1 
ATOM   680  C CG    . LEU A 1 94  ? 12.51527  -0.11807  15.10949  1.000 22.32666 ? 88   LEU A CG    1 
ATOM   681  C CD1   . LEU A 1 94  ? 12.22140  -0.83365  16.43025  1.000 26.08421 ? 88   LEU A CD1   1 
ATOM   682  C CD2   . LEU A 1 94  ? 11.96707  -0.87801  13.94446  1.000 23.62167 ? 88   LEU A CD2   1 
ATOM   683  N N     . ALA A 1 95  ? 14.36887  3.18717   15.45559  1.000 23.32021 ? 89   ALA A N     1 
ATOM   684  C CA    . ALA A 1 95  ? 15.79957  3.48348   15.43757  1.000 28.69337 ? 89   ALA A CA    1 
ATOM   685  C C     . ALA A 1 95  ? 16.28086  4.04431   16.77643  1.000 25.99183 ? 89   ALA A C     1 
ATOM   686  O O     . ALA A 1 95  ? 17.38136  3.70938   17.23931  1.000 25.92253 ? 89   ALA A O     1 
ATOM   687  C CB    . ALA A 1 95  ? 16.11101  4.44446   14.29127  1.000 26.02704 ? 89   ALA A CB    1 
ATOM   688  N N     . TYR A 1 96  ? 15.48346  4.91127   17.41059  1.000 20.01544 ? 90   TYR A N     1 
ATOM   689  C CA    . TYR A 1 96  ? 15.89678  5.48982   18.69096  1.000 25.47565 ? 90   TYR A CA    1 
ATOM   690  C C     . TYR A 1 96  ? 16.04183  4.41247   19.75724  1.000 24.10150 ? 90   TYR A C     1 
ATOM   691  O O     . TYR A 1 96  ? 17.06158  4.33965   20.45535  1.000 24.24080 ? 90   TYR A O     1 
ATOM   692  C CB    . TYR A 1 96  ? 14.88126  6.55280   19.13534  1.000 21.63778 ? 90   TYR A CB    1 
ATOM   693  C CG    . TYR A 1 96  ? 15.02980  6.99252   20.58764  1.000 24.22283 ? 90   TYR A CG    1 
ATOM   694  C CD1   . TYR A 1 96  ? 16.04498  7.89879   20.96985  1.000 21.56577 ? 90   TYR A CD1   1 
ATOM   695  C CD2   . TYR A 1 96  ? 14.13499  6.54315   21.56368  1.000 20.69410 ? 90   TYR A CD2   1 
ATOM   696  C CE1   . TYR A 1 96  ? 16.17505  8.29744   22.32264  1.000 21.93469 ? 90   TYR A CE1   1 
ATOM   697  C CE2   . TYR A 1 96  ? 14.24289  6.94656   22.89095  1.000 21.97486 ? 90   TYR A CE2   1 
ATOM   698  C CZ    . TYR A 1 96  ? 15.24394  7.84363   23.25553  1.000 22.29252 ? 90   TYR A CZ    1 
ATOM   699  O OH    . TYR A 1 96  ? 15.32854  8.23004   24.56008  1.000 22.58209 ? 90   TYR A OH    1 
ATOM   700  N N     . LEU A 1 97  ? 15.02739  3.55473   19.89622  1.000 21.92358 ? 91   LEU A N     1 
ATOM   701  C CA    . LEU A 1 97  ? 15.10906  2.51233   20.91534  1.000 24.21696 ? 91   LEU A CA    1 
ATOM   702  C C     . LEU A 1 97  ? 16.25048  1.52715   20.64549  1.000 22.99067 ? 91   LEU A C     1 
ATOM   703  O O     . LEU A 1 97  ? 16.88692  1.06907   21.59419  1.000 22.93731 ? 91   LEU A O     1 
ATOM   704  C CB    . LEU A 1 97  ? 13.76624  1.79151   21.05243  1.000 20.90542 ? 91   LEU A CB    1 
ATOM   705  C CG    . LEU A 1 97  ? 12.62856  2.70353   21.53568  1.000 22.44321 ? 91   LEU A CG    1 
ATOM   706  C CD1   . LEU A 1 97  ? 11.26890  1.96515   21.54490  1.000 19.39730 ? 91   LEU A CD1   1 
ATOM   707  C CD2   . LEU A 1 97  ? 12.92210  3.25065   22.95235  1.000 21.59759 ? 91   LEU A CD2   1 
ATOM   708  N N     . LYS A 1 98  ? 16.56583  1.25316   19.37526  1.000 25.22285 ? 92   LYS A N     1 
ATOM   709  C CA    . LYS A 1 98  ? 17.76522  0.47374   19.04352  1.000 24.89389 ? 92   LYS A CA    1 
ATOM   710  C C     . LYS A 1 98  ? 19.04107  1.17735   19.51086  1.000 28.07902 ? 92   LYS A C     1 
ATOM   711  O O     . LYS A 1 98  ? 19.96894  0.53431   20.03138  1.000 28.61513 ? 92   LYS A O     1 
ATOM   712  C CB    . LYS A 1 98  ? 17.79132  0.20924   17.53417  1.000 24.59731 ? 92   LYS A CB    1 
ATOM   713  C CG    . LYS A 1 98  ? 16.66352  -0.78900  17.05767  1.000 27.24181 ? 92   LYS A CG    1 
ATOM   714  C CD    . LYS A 1 98  ? 16.76061  -1.06160  15.54104  1.000 27.35241 ? 92   LYS A CD    1 
ATOM   715  C CE    . LYS A 1 98  ? 15.71207  -2.03894  15.07633  1.000 35.91316 ? 92   LYS A CE    1 
ATOM   716  N NZ    . LYS A 1 98  ? 15.83512  -2.38501  13.63090  1.000 44.68040 ? 92   LYS A NZ    1 
ATOM   717  N N     . ARG A 1 99  ? 19.10173  2.50137   19.35666  1.000 24.32452 ? 93   ARG A N     1 
ATOM   718  C CA    . ARG A 1 99  ? 20.26503  3.25220   19.80960  1.000 25.68625 ? 93   ARG A CA    1 
ATOM   719  C C     . ARG A 1 99  ? 20.41434  3.18353   21.32924  1.000 26.03725 ? 93   ARG A C     1 
ATOM   720  O O     . ARG A 1 99  ? 21.53019  3.01540   21.83322  1.000 24.32428 ? 93   ARG A O     1 
ATOM   721  C CB    . ARG A 1 99  ? 20.14099  4.69272   19.32043  1.000 24.88079 ? 93   ARG A CB    1 
ATOM   722  C CG    . ARG A 1 99  ? 21.15326  5.67177   19.86809  1.000 35.58166 ? 93   ARG A CG    1 
ATOM   723  C CD    . ARG A 1 99  ? 22.59465  5.26910   19.59450  1.000 44.90720 ? 93   ARG A CD    1 
ATOM   724  N NE    . ARG A 1 99  ? 23.49734  6.13886   20.34115  1.000 50.15024 ? 93   ARG A NE    1 
ATOM   725  C CZ    . ARG A 1 99  ? 24.61449  5.73048   20.92482  1.000 53.64189 ? 93   ARG A CZ    1 
ATOM   726  N NH1   . ARG A 1 99  ? 25.02060  4.47009   20.83631  1.000 51.65408 ? 93   ARG A NH1   1 
ATOM   727  N NH2   . ARG A 1 99  ? 25.33361  6.60290   21.62714  1.000 48.71127 ? 93   ARG A NH2   1 
ATOM   728  N N     . VAL A 1 100 ? 19.29844  3.27201   22.06888  1.000 23.29489 ? 94   VAL A N     1 
ATOM   729  C CA    . VAL A 1 100 ? 19.33285  3.11575   23.52762  1.000 22.40651 ? 94   VAL A CA    1 
ATOM   730  C C     . VAL A 1 100 ? 19.89260  1.75251   23.90939  1.000 29.66139 ? 94   VAL A C     1 
ATOM   731  O O     . VAL A 1 100 ? 20.74962  1.64949   24.79955  1.000 24.29307 ? 94   VAL A O     1 
ATOM   732  C CB    . VAL A 1 100 ? 17.93449  3.29519   24.13906  1.000 21.63131 ? 94   VAL A CB    1 
ATOM   733  C CG1   . VAL A 1 100 ? 17.98200  3.06156   25.64403  1.000 26.26133 ? 94   VAL A CG1   1 
ATOM   734  C CG2   . VAL A 1 100 ? 17.41802  4.68108   23.85497  1.000 21.71741 ? 94   VAL A CG2   1 
ATOM   735  N N     . ALA A 1 101 ? 19.39146  0.68764   23.26352  1.000 25.10647 ? 95   ALA A N     1 
ATOM   736  C CA    . ALA A 1 101 ? 19.89150  -0.65950  23.55264  1.000 26.36193 ? 95   ALA A CA    1 
ATOM   737  C C     . ALA A 1 101 ? 21.37507  -0.79404  23.19485  1.000 29.94840 ? 95   ALA A C     1 
ATOM   738  O O     . ALA A 1 101 ? 22.13215  -1.47097  23.90746  1.000 32.62399 ? 95   ALA A O     1 
ATOM   739  C CB    . ALA A 1 101 ? 19.04455  -1.71828  22.82302  1.000 24.45630 ? 95   ALA A CB    1 
ATOM   740  N N     . ASP A 1 102 ? 21.80306  -0.15988  22.09379  1.000 28.96375 ? 96   ASP A N     1 
ATOM   741  C CA    . ASP A 1 102 ? 23.21264  -0.13072  21.71987  1.000 30.01539 ? 96   ASP A CA    1 
ATOM   742  C C     . ASP A 1 102 ? 24.02712  0.50902   22.82654  1.000 29.28538 ? 96   ASP A C     1 
ATOM   743  O O     . ASP A 1 102 ? 24.99574  -0.06998  23.33119  1.000 31.97526 ? 96   ASP A O     1 
ATOM   744  C CB    . ASP A 1 102 ? 23.43252  0.66962   20.43219  1.000 32.25903 ? 96   ASP A CB    1 
ATOM   745  C CG    . ASP A 1 102 ? 22.84170  0.02045   19.17454  1.000 37.96359 ? 96   ASP A CG    1 
ATOM   746  O OD1   . ASP A 1 102 ? 22.46758  -1.16883  19.15325  1.000 36.91095 ? 96   ASP A OD1   1 
ATOM   747  O OD2   . ASP A 1 102 ? 22.78161  0.75001   18.16292  1.000 45.91188 ? 96   ASP A OD2   1 
ATOM   748  N N     . LYS A 1 103 ? 23.65287  1.73143   23.19547  1.000 27.66714 ? 97   LYS A N     1 
ATOM   749  C CA    . LYS A 1 103 ? 24.46699  2.51929   24.10681  1.000 29.52527 ? 97   LYS A CA    1 
ATOM   750  C C     . LYS A 1 103 ? 24.60143  1.84068   25.46218  1.000 33.83457 ? 97   LYS A C     1 
ATOM   751  O O     . LYS A 1 103 ? 25.67442  1.86951   26.07117  1.000 32.49468 ? 97   LYS A O     1 
ATOM   752  C CB    . LYS A 1 103 ? 23.86029  3.90871   24.27723  1.000 30.91744 ? 97   LYS A CB    1 
ATOM   753  C CG    . LYS A 1 103 ? 24.66560  4.82921   25.20551  1.000 33.08831 ? 97   LYS A CG    1 
ATOM   754  C CD    . LYS A 1 103 ? 24.04854  6.22593   25.35501  1.000 37.33036 ? 97   LYS A CD    1 
ATOM   755  C CE    . LYS A 1 103 ? 24.84386  6.95631   26.43986  1.000 38.66879 ? 97   LYS A CE    1 
ATOM   756  N NZ    . LYS A 1 103 ? 24.31180  8.30635   26.69337  1.000 44.06514 ? 97   LYS A NZ    1 
ATOM   757  N N     . HIS A 1 104 ? 23.52696  1.22690   25.95522  1.000 31.05146 ? 98   HIS A N     1 
ATOM   758  C CA    . HIS A 1 104 ? 23.52419  0.70142   27.31263  1.000 28.90219 ? 98   HIS A CA    1 
ATOM   759  C C     . HIS A 1 104 ? 23.68468  -0.81054  27.35684  1.000 25.91889 ? 98   HIS A C     1 
ATOM   760  O O     . HIS A 1 104 ? 23.37805  -1.42235  28.38174  1.000 30.27901 ? 98   HIS A O     1 
ATOM   761  C CB    . HIS A 1 104 ? 22.26110  1.13866   28.03621  1.000 29.55912 ? 98   HIS A CB    1 
ATOM   762  C CG    . HIS A 1 104 ? 22.23777  2.60837   28.28748  1.000 29.73093 ? 98   HIS A CG    1 
ATOM   763  N ND1   . HIS A 1 104 ? 22.91239  3.18588   29.34241  1.000 29.60710 ? 98   HIS A ND1   1 
ATOM   764  C CD2   . HIS A 1 104 ? 21.72165  3.63315   27.55922  1.000 30.24902 ? 98   HIS A CD2   1 
ATOM   765  C CE1   . HIS A 1 104 ? 22.76682  4.50114   29.28750  1.000 35.12010 ? 98   HIS A CE1   1 
ATOM   766  N NE2   . HIS A 1 104 ? 22.04196  4.79762   28.21860  1.000 33.20870 ? 98   HIS A NE2   1 
ATOM   767  N N     . ASP A 1 105 ? 24.13282  -1.41819  26.25748  1.000 33.00367 ? 99   ASP A N     1 
ATOM   768  C CA    . ASP A 1 105 ? 24.54950  -2.82307  26.25536  1.000 33.18164 ? 99   ASP A CA    1 
ATOM   769  C C     . ASP A 1 105 ? 23.42742  -3.71759  26.77974  1.000 36.58554 ? 99   ASP A C     1 
ATOM   770  O O     . ASP A 1 105 ? 23.63171  -4.61096  27.60517  1.000 31.06641 ? 99   ASP A O     1 
ATOM   771  C CB    . ASP A 1 105 ? 25.83764  -2.97241  27.07915  1.000 34.07934 ? 99   ASP A CB    1 
ATOM   772  C CG    . ASP A 1 105 ? 26.51834  -4.32369  26.90560  1.000 42.61288 ? 99   ASP A CG    1 
ATOM   773  O OD1   . ASP A 1 105 ? 26.29763  -5.01997  25.88992  1.000 39.59409 ? 99   ASP A OD1   1 
ATOM   774  O OD2   . ASP A 1 105 ? 27.31131  -4.66463  27.80729  1.000 48.85801 ? 99   ASP A OD2   1 
ATOM   775  N N     . LEU A 1 106 ? 22.21121  -3.45174  26.29975  1.000 28.75512 ? 100  LEU A N     1 
ATOM   776  C CA    . LEU A 1 106 ? 21.03545  -4.10395  26.84718  1.000 31.61436 ? 100  LEU A CA    1 
ATOM   777  C C     . LEU A 1 106 ? 20.76666  -5.47940  26.22485  1.000 28.56378 ? 100  LEU A C     1 
ATOM   778  O O     . LEU A 1 106 ? 20.23888  -6.36438  26.91083  1.000 28.51709 ? 100  LEU A O     1 
ATOM   779  C CB    . LEU A 1 106 ? 19.80760  -3.20873  26.63493  1.000 29.77271 ? 100  LEU A CB    1 
ATOM   780  C CG    . LEU A 1 106 ? 19.78911  -1.87759  27.39071  1.000 29.25079 ? 100  LEU A CG    1 
ATOM   781  C CD1   . LEU A 1 106 ? 18.43682  -1.17956  27.13078  1.000 26.14446 ? 100  LEU A CD1   1 
ATOM   782  C CD2   . LEU A 1 106 ? 20.06752  -2.03540  28.88974  1.000 26.10225 ? 100  LEU A CD2   1 
ATOM   783  N N     . ARG A 1 107 ? 21.09263  -5.68264  24.94260  1.000 28.65268 ? 101  ARG A N     1 
ATOM   784  C CA    . ARG A 1 107 ? 20.62500  -6.89334  24.25735  1.000 29.72156 ? 101  ARG A CA    1 
ATOM   785  C C     . ARG A 1 107 ? 21.21066  -8.16100  24.87051  1.000 28.89007 ? 101  ARG A C     1 
ATOM   786  O O     . ARG A 1 107 ? 20.58688  -9.22526  24.80648  1.000 30.11839 ? 101  ARG A O     1 
ATOM   787  C CB    . ARG A 1 107 ? 20.96641  -6.84197  22.76864  1.000 27.14989 ? 101  ARG A CB    1 
ATOM   788  C CG    . ARG A 1 107 ? 20.16215  -5.76829  22.00321  1.000 28.34850 ? 101  ARG A CG    1 
ATOM   789  C CD    . ARG A 1 107 ? 20.36779  -5.88134  20.52142  1.000 35.22161 ? 101  ARG A CD    1 
ATOM   790  N NE    . ARG A 1 107 ? 19.71387  -4.77827  19.82719  1.000 35.65276 ? 101  ARG A NE    1 
ATOM   791  C CZ    . ARG A 1 107 ? 20.23866  -3.56462  19.73672  1.000 36.03354 ? 101  ARG A CZ    1 
ATOM   792  N NH1   . ARG A 1 107 ? 21.40557  -3.26839  20.30011  1.000 33.66267 ? 101  ARG A NH1   1 
ATOM   793  N NH2   . ARG A 1 107 ? 19.59506  -2.63058  19.04650  1.000 32.62421 ? 101  ARG A NH2   1 
ATOM   794  N N     . LYS A 1 108 ? 22.38888  -8.06729  25.48474  1.000 32.11982 ? 102  LYS A N     1 
ATOM   795  C CA    . LYS A 1 108 ? 22.98469  -9.27477  26.03985  1.000 34.54860 ? 102  LYS A CA    1 
ATOM   796  C C     . LYS A 1 108 ? 22.11570  -9.88035  27.13166  1.000 35.29198 ? 102  LYS A C     1 
ATOM   797  O O     . LYS A 1 108 ? 22.23762  -11.07591 27.41756  1.000 35.54144 ? 102  LYS A O     1 
ATOM   798  C CB    . LYS A 1 108 ? 24.38714  -8.97305  26.56133  1.000 33.83964 ? 102  LYS A CB    1 
ATOM   799  C CG    . LYS A 1 108 ? 24.44232  -8.15591  27.82208  1.000 35.66169 ? 102  LYS A CG    1 
ATOM   800  C CD    . LYS A 1 108 ? 25.88306  -7.73087  28.11651  1.000 38.69741 ? 102  LYS A CD    1 
ATOM   801  C CE    . LYS A 1 108 ? 25.98233  -7.03769  29.46615  1.000 40.44682 ? 102  LYS A CE    1 
ATOM   802  N NZ    . LYS A 1 108 ? 25.21428  -7.81984  30.50414  1.000 47.57215 ? 102  LYS A NZ    1 
ATOM   803  N N     . ASP A 1 109 ? 21.21525  -9.09786  27.73051  1.000 32.42364 ? 103  ASP A N     1 
ATOM   804  C CA    . ASP A 1 109 ? 20.31630  -9.63019  28.75217  1.000 33.11555 ? 103  ASP A CA    1 
ATOM   805  C C     . ASP A 1 109 ? 18.86675  -9.67315  28.28747  1.000 29.44813 ? 103  ASP A C     1 
ATOM   806  O O     . ASP A 1 109 ? 17.94795  -9.78338  29.11173  1.000 31.90081 ? 103  ASP A O     1 
ATOM   807  C CB    . ASP A 1 109 ? 20.48588  -8.84513  30.05509  1.000 29.74719 ? 103  ASP A CB    1 
ATOM   808  C CG    . ASP A 1 109 ? 21.87872  -9.04678  30.66328  1.000 35.37845 ? 103  ASP A CG    1 
ATOM   809  O OD1   . ASP A 1 109 ? 22.25759  -10.22084 30.85945  1.000 37.88600 ? 103  ASP A OD1   1 
ATOM   810  O OD2   . ASP A 1 109 ? 22.60970  -8.05586  30.90608  1.000 34.69809 ? 103  ASP A OD2   1 
ATOM   811  N N     . ILE A 1 110 ? 18.64850  -9.65406  26.97372  1.000 28.77988 ? 104  ILE A N     1 
ATOM   812  C CA    . ILE A 1 110 ? 17.33623  -9.86194  26.37521  1.000 28.99037 ? 104  ILE A CA    1 
ATOM   813  C C     . ILE A 1 110 ? 17.37825  -11.13433 25.54260  1.000 31.49441 ? 104  ILE A C     1 
ATOM   814  O O     . ILE A 1 110 ? 18.25839  -11.30216 24.68949  1.000 31.03734 ? 104  ILE A O     1 
ATOM   815  C CB    . ILE A 1 110 ? 16.90991  -8.67101  25.49847  1.000 28.01585 ? 104  ILE A CB    1 
ATOM   816  C CG1   . ILE A 1 110 ? 16.98909  -7.35636  26.28381  1.000 30.56017 ? 104  ILE A CG1   1 
ATOM   817  C CG2   . ILE A 1 110 ? 15.48440  -8.89094  24.91126  1.000 27.09913 ? 104  ILE A CG2   1 
ATOM   818  C CD1   . ILE A 1 110 ? 16.70073  -6.12945  25.36677  1.000 25.65103 ? 104  ILE A CD1   1 
ATOM   819  N N     . GLN A 1 111 ? 16.41772  -12.01099 25.77757  1.000 27.58277 ? 105  GLN A N     1 
ATOM   820  C CA    . GLN A 1 111 ? 16.24951  -13.22434 24.98908  1.000 28.95044 ? 105  GLN A CA    1 
ATOM   821  C C     . GLN A 1 111 ? 15.10761  -12.96572 24.02024  1.000 31.16413 ? 105  GLN A C     1 
ATOM   822  O O     . GLN A 1 111 ? 13.94797  -12.88299 24.43670  1.000 29.11218 ? 105  GLN A O     1 
ATOM   823  C CB    . GLN A 1 111 ? 15.95329  -14.42180 25.89222  1.000 28.82453 ? 105  GLN A CB    1 
ATOM   824  C CG    . GLN A 1 111 ? 15.93424  -15.74397 25.16095  1.000 29.97380 ? 105  GLN A CG    1 
ATOM   825  C CD    . GLN A 1 111 ? 16.01614  -16.92622 26.11152  1.000 41.80730 ? 105  GLN A CD    1 
ATOM   826  O OE1   . GLN A 1 111 ? 16.77852  -16.90695 27.08832  1.000 41.00387 ? 105  GLN A OE1   1 
ATOM   827  N NE2   . GLN A 1 111 ? 15.24948  -17.97291 25.81844  1.000 38.21318 ? 105  GLN A NE2   1 
ATOM   828  N N     . PHE A 1 112 ? 15.44229  -12.79894 22.74136  1.000 27.76374 ? 106  PHE A N     1 
ATOM   829  C CA    . PHE A 1 112 ? 14.44460  -12.48674 21.73462  1.000 28.98168 ? 106  PHE A CA    1 
ATOM   830  C C     . PHE A 1 112 ? 13.79151  -13.76465 21.20274  1.000 32.83437 ? 106  PHE A C     1 
ATOM   831  O O     . PHE A 1 112 ? 14.20882  -14.88102 21.51299  1.000 33.04173 ? 106  PHE A O     1 
ATOM   832  C CB    . PHE A 1 112 ? 15.06366  -11.69182 20.59292  1.000 28.43770 ? 106  PHE A CB    1 
ATOM   833  C CG    . PHE A 1 112 ? 15.53938  -10.30999 20.98622  1.000 30.13757 ? 106  PHE A CG    1 
ATOM   834  C CD1   . PHE A 1 112 ? 14.64210  -9.26416  21.14956  1.000 29.48570 ? 106  PHE A CD1   1 
ATOM   835  C CD2   . PHE A 1 112 ? 16.87299  -10.08205 21.24814  1.000 31.55486 ? 106  PHE A CD2   1 
ATOM   836  C CE1   . PHE A 1 112 ? 15.08710  -7.98159  21.50745  1.000 29.34257 ? 106  PHE A CE1   1 
ATOM   837  C CE2   . PHE A 1 112 ? 17.31888  -8.80114  21.62056  1.000 30.64869 ? 106  PHE A CE2   1 
ATOM   838  C CZ    . PHE A 1 112 ? 16.42453  -7.75836  21.74770  1.000 25.17953 ? 106  PHE A CZ    1 
ATOM   839  N N     . GLU A 1 113 ? 12.71796  -13.58150 20.42669  1.000 31.10264 ? 107  GLU A N     1 
ATOM   840  C CA    . GLU A 1 113 ? 11.97686  -14.69455 19.81811  1.000 33.96072 ? 107  GLU A CA    1 
ATOM   841  C C     . GLU A 1 113 ? 11.51446  -15.69859 20.86025  1.000 40.41792 ? 107  GLU A C     1 
ATOM   842  O O     . GLU A 1 113 ? 11.47846  -16.90514 20.59910  1.000 36.42298 ? 107  GLU A O     1 
ATOM   843  C CB    . GLU A 1 113 ? 12.82169  -15.39718 18.75167  1.000 39.37494 ? 107  GLU A CB    1 
ATOM   844  C CG    . GLU A 1 113 ? 13.43982  -14.44415 17.76099  1.000 40.28205 ? 107  GLU A CG    1 
ATOM   845  C CD    . GLU A 1 113 ? 13.73462  -15.10166 16.42570  1.000 57.04919 ? 107  GLU A CD    1 
ATOM   846  O OE1   . GLU A 1 113 ? 14.92067  -15.09397 16.02006  1.000 54.40304 ? 107  GLU A OE1   1 
ATOM   847  O OE2   . GLU A 1 113 ? 12.78874  -15.62555 15.79237  1.000 54.96268 ? 107  GLU A OE2   1 
ATOM   848  N N     . THR A 1 114 ? 11.17348  -15.21023 22.05389  1.000 33.29418 ? 108  THR A N     1 
ATOM   849  C CA    . THR A 1 114 ? 10.85139  -16.08153 23.18046  1.000 32.48655 ? 108  THR A CA    1 
ATOM   850  C C     . THR A 1 114 ? 9.58968   -15.56012 23.84314  1.000 32.81957 ? 108  THR A C     1 
ATOM   851  O O     . THR A 1 114 ? 9.61380   -14.51926 24.51039  1.000 31.08120 ? 108  THR A O     1 
ATOM   852  C CB    . THR A 1 114 ? 12.00676  -16.14769 24.17673  1.000 30.83832 ? 108  THR A CB    1 
ATOM   853  O OG1   . THR A 1 114 ? 13.19575  -16.57714 23.50063  1.000 35.35096 ? 108  THR A OG1   1 
ATOM   854  C CG2   . THR A 1 114 ? 11.68697  -17.09663 25.32782  1.000 34.58030 ? 108  THR A CG2   1 
ATOM   855  N N     . GLY A 1 115 ? 8.48515   -16.26505 23.62910  1.000 28.74311 ? 109  GLY A N     1 
ATOM   856  C CA    . GLY A 1 115 ? 7.27358   -15.94425 24.32616  1.000 27.69379 ? 109  GLY A CA    1 
ATOM   857  C C     . GLY A 1 115 ? 7.29306   -16.59511 25.69658  1.000 35.55157 ? 109  GLY A C     1 
ATOM   858  O O     . GLY A 1 115 ? 7.80360   -17.70055 25.87288  1.000 33.53141 ? 109  GLY A O     1 
ATOM   859  N N     . ILE A 1 116 ? 6.76044   -15.87269 26.67577  1.000 31.27760 ? 110  ILE A N     1 
ATOM   860  C CA    . ILE A 1 116 ? 6.51222   -16.41454 28.00685  1.000 34.06232 ? 110  ILE A CA    1 
ATOM   861  C C     . ILE A 1 116 ? 5.11573   -17.01761 28.02194  1.000 32.69603 ? 110  ILE A C     1 
ATOM   862  O O     . ILE A 1 116 ? 4.13165   -16.31276 27.77928  1.000 29.41289 ? 110  ILE A O     1 
ATOM   863  C CB    . ILE A 1 116 ? 6.66097   -15.32825 29.08516  1.000 27.46293 ? 110  ILE A CB    1 
ATOM   864  C CG1   . ILE A 1 116 ? 8.08669   -14.75495 29.08529  1.000 27.04551 ? 110  ILE A CG1   1 
ATOM   865  C CG2   . ILE A 1 116 ? 6.17776   -15.82707 30.45409  1.000 31.59473 ? 110  ILE A CG2   1 
ATOM   866  C CD1   . ILE A 1 116 ? 9.16695   -15.81286 29.19488  1.000 32.07866 ? 110  ILE A CD1   1 
ATOM   867  N N     . ARG A 1 117 ? 5.03079   -18.32360 28.32542  1.000 30.12590 ? 111  ARG A N     1 
ATOM   868  C CA    . ARG A 1 117 ? 3.74758   -19.02562 28.40295  1.000 34.96531 ? 111  ARG A CA    1 
ATOM   869  C C     . ARG A 1 117 ? 3.11713   -18.96099 29.78316  1.000 33.67007 ? 111  ARG A C     1 
ATOM   870  O O     . ARG A 1 117 ? 1.89577   -18.81400 29.90253  1.000 30.42453 ? 111  ARG A O     1 
ATOM   871  C CB    . ARG A 1 117 ? 3.89922   -20.50310 28.00046  1.000 32.14436 ? 111  ARG A CB    1 
ATOM   872  C CG    . ARG A 1 117 ? 2.55070   -21.23799 27.92392  1.000 41.64135 ? 111  ARG A CG    1 
ATOM   873  C CD    . ARG A 1 117 ? 2.69796   -22.74911 28.18189  1.000 51.93145 ? 111  ARG A CD    1 
ATOM   874  N NE    . ARG A 1 117 ? 3.70830   -23.34547 27.31351  1.000 49.19245 ? 111  ARG A NE    1 
ATOM   875  C CZ    . ARG A 1 117 ? 4.71939   -24.10328 27.72140  1.000 47.74195 ? 111  ARG A CZ    1 
ATOM   876  N NH1   . ARG A 1 117 ? 4.88598   -24.41366 28.99584  1.000 48.56617 ? 111  ARG A NH1   1 
ATOM   877  N NH2   . ARG A 1 117 ? 5.58327   -24.56524 26.82437  1.000 38.79488 ? 111  ARG A NH2   1 
ATOM   878  N N     . SER A 1 118 ? 3.92091   -19.06104 30.83311  1.000 33.15500 ? 112  SER A N     1 
ATOM   879  C CA    . SER A 1 118 ? 3.35260   -19.10066 32.17024  1.000 36.69449 ? 112  SER A CA    1 
ATOM   880  C C     . SER A 1 118 ? 4.34447   -18.55234 33.18212  1.000 31.26383 ? 112  SER A C     1 
ATOM   881  O O     . SER A 1 118 ? 5.55995   -18.59195 32.98350  1.000 30.69252 ? 112  SER A O     1 
ATOM   882  C CB    . SER A 1 118 ? 2.96493   -20.54092 32.55549  1.000 34.48578 ? 112  SER A CB    1 
ATOM   883  O OG    . SER A 1 118 ? 4.12868   -21.34309 32.55304  1.000 37.57700 ? 112  SER A OG    1 
ATOM   884  N N     . ALA A 1 119 ? 3.80227   -18.04859 34.28056  1.000 35.01746 ? 113  ALA A N     1 
ATOM   885  C CA    . ALA A 1 119 ? 4.61225   -17.67121 35.42841  1.000 34.11549 ? 113  ALA A CA    1 
ATOM   886  C C     . ALA A 1 119 ? 3.82176   -18.06087 36.66445  1.000 36.29896 ? 113  ALA A C     1 
ATOM   887  O O     . ALA A 1 119 ? 2.68927   -17.60171 36.85175  1.000 33.96906 ? 113  ALA A O     1 
ATOM   888  C CB    . ALA A 1 119 ? 4.94176   -16.17591 35.41378  1.000 34.84289 ? 113  ALA A CB    1 
ATOM   889  N N     . TYR A 1 120 ? 4.39569   -18.94476 37.47279  1.000 35.36362 ? 114  TYR A N     1 
ATOM   890  C CA    . TYR A 1 120 ? 3.71843   -19.48366 38.64017  1.000 41.78342 ? 114  TYR A CA    1 
ATOM   891  C C     . TYR A 1 120 ? 4.47437   -19.03628 39.88092  1.000 31.79053 ? 114  TYR A C     1 
ATOM   892  O O     . TYR A 1 120 ? 5.68288   -19.26204 39.97681  1.000 34.01138 ? 114  TYR A O     1 
ATOM   893  C CB    . TYR A 1 120 ? 3.67368   -21.01642 38.60320  1.000 40.55230 ? 114  TYR A CB    1 
ATOM   894  C CG    . TYR A 1 120 ? 2.76835   -21.59555 37.53759  1.000 44.19623 ? 114  TYR A CG    1 
ATOM   895  C CD1   . TYR A 1 120 ? 1.75754   -20.83396 36.95706  1.000 46.77754 ? 114  TYR A CD1   1 
ATOM   896  C CD2   . TYR A 1 120 ? 2.87624   -22.93351 37.16512  1.000 50.23220 ? 114  TYR A CD2   1 
ATOM   897  C CE1   . TYR A 1 120 ? 0.93155   -21.36671 35.98084  1.000 49.57643 ? 114  TYR A CE1   1 
ATOM   898  C CE2   . TYR A 1 120 ? 2.04407   -23.47841 36.20585  1.000 45.20012 ? 114  TYR A CE2   1 
ATOM   899  C CZ    . TYR A 1 120 ? 1.06706   -22.69513 35.62438  1.000 55.26385 ? 114  TYR A CZ    1 
ATOM   900  O OH    . TYR A 1 120 ? 0.23378   -23.23480 34.67055  1.000 47.24552 ? 114  TYR A OH    1 
ATOM   901  N N     . PHE A 1 121 ? 3.76937   -18.41957 40.82888  1.000 32.95788 ? 115  PHE A N     1 
ATOM   902  C CA    . PHE A 1 121 ? 4.41488   -17.99589 42.06915  1.000 35.18195 ? 115  PHE A CA    1 
ATOM   903  C C     . PHE A 1 121 ? 4.57771   -19.15753 43.02968  1.000 40.89494 ? 115  PHE A C     1 
ATOM   904  O O     . PHE A 1 121 ? 3.61635   -19.88175 43.30381  1.000 40.13427 ? 115  PHE A O     1 
ATOM   905  C CB    . PHE A 1 121 ? 3.62747   -16.90639 42.77999  1.000 36.80154 ? 115  PHE A CB    1 
ATOM   906  C CG    . PHE A 1 121 ? 4.39510   -16.26203 43.90318  1.000 36.71484 ? 115  PHE A CG    1 
ATOM   907  C CD1   . PHE A 1 121 ? 5.64111   -15.69364 43.66788  1.000 34.34751 ? 115  PHE A CD1   1 
ATOM   908  C CD2   . PHE A 1 121 ? 3.89106   -16.25274 45.20036  1.000 40.70675 ? 115  PHE A CD2   1 
ATOM   909  C CE1   . PHE A 1 121 ? 6.35731   -15.08970 44.69011  1.000 38.29571 ? 115  PHE A CE1   1 
ATOM   910  C CE2   . PHE A 1 121 ? 4.60886   -15.66482 46.23957  1.000 39.70036 ? 115  PHE A CE2   1 
ATOM   911  C CZ    . PHE A 1 121 ? 5.84366   -15.08579 45.98939  1.000 42.15507 ? 115  PHE A CZ    1 
ATOM   912  N N     . ASP A 1 122 ? 5.79182   -19.29010 43.57220  1.000 40.29370 ? 116  ASP A N     1 
ATOM   913  C CA    . ASP A 1 122 ? 6.16735   -20.34075 44.52326  1.000 44.77799 ? 116  ASP A CA    1 
ATOM   914  C C     . ASP A 1 122 ? 6.11720   -19.72203 45.91663  1.000 40.82450 ? 116  ASP A C     1 
ATOM   915  O O     . ASP A 1 122 ? 7.03273   -19.00392 46.31384  1.000 47.37846 ? 116  ASP A O     1 
ATOM   916  C CB    . ASP A 1 122 ? 7.55538   -20.88460 44.18181  1.000 44.25798 ? 116  ASP A CB    1 
ATOM   917  C CG    . ASP A 1 122 ? 7.96570   -22.08512 45.04081  1.000 58.78775 ? 116  ASP A CG    1 
ATOM   918  O OD1   . ASP A 1 122 ? 8.68491   -22.96660 44.51171  1.000 54.34700 ? 116  ASP A OD1   1 
ATOM   919  O OD2   . ASP A 1 122 ? 7.60187   -22.13089 46.24124  1.000 51.68309 ? 116  ASP A OD2   1 
ATOM   920  N N     . GLU A 1 123 ? 5.04398   -19.99755 46.66218  1.000 48.14710 ? 117  GLU A N     1 
ATOM   921  C CA    . GLU A 1 123 ? 4.87449   -19.36941 47.97250  1.000 54.90551 ? 117  GLU A CA    1 
ATOM   922  C C     . GLU A 1 123 ? 5.85812   -19.90034 49.01614  1.000 57.45783 ? 117  GLU A C     1 
ATOM   923  O O     . GLU A 1 123 ? 6.19545   -19.18168 49.96597  1.000 60.31416 ? 117  GLU A O     1 
ATOM   924  C CB    . GLU A 1 123 ? 3.44294   -19.55572 48.45391  1.000 58.52559 ? 117  GLU A CB    1 
ATOM   925  C CG    . GLU A 1 123 ? 2.51711   -18.45663 48.00361  1.000 58.51532 ? 117  GLU A CG    1 
ATOM   926  C CD    . GLU A 1 123 ? 1.07369   -18.75089 48.33578  1.000 60.74565 ? 117  GLU A CD    1 
ATOM   927  O OE1   . GLU A 1 123 ? 0.44267   -19.53771 47.59398  1.000 59.84478 ? 117  GLU A OE1   1 
ATOM   928  O OE2   . GLU A 1 123 ? 0.57234   -18.19352 49.33440  1.000 67.81184 ? 117  GLU A OE2   1 
ATOM   929  N N     . GLU A 1 124 ? 6.31902   -21.14415 48.86740  1.000 59.50099 ? 118  GLU A N     1 
ATOM   930  C CA    . GLU A 1 124 ? 7.32704   -21.68219 49.77759  1.000 64.54182 ? 118  GLU A CA    1 
ATOM   931  C C     . GLU A 1 124 ? 8.62951   -20.89671 49.68018  1.000 62.19220 ? 118  GLU A C     1 
ATOM   932  O O     . GLU A 1 124 ? 9.17221   -20.43831 50.69241  1.000 61.31816 ? 118  GLU A O     1 
ATOM   933  C CB    . GLU A 1 124 ? 7.57917   -23.16060 49.46923  1.000 67.47992 ? 118  GLU A CB    1 
ATOM   934  C CG    . GLU A 1 124 ? 8.53776   -23.85066 50.43849  1.000 77.28846 ? 118  GLU A CG    1 
ATOM   935  C CD    . GLU A 1 124 ? 8.75005   -25.32482 50.11526  1.000 92.92917 ? 118  GLU A CD    1 
ATOM   936  O OE1   . GLU A 1 124 ? 7.74652   -26.04479 49.91329  1.000 97.66905 ? 118  GLU A OE1   1 
ATOM   937  O OE2   . GLU A 1 124 ? 9.92190   -25.76682 50.07635  1.000 99.25288 ? 118  GLU A OE2   1 
ATOM   938  N N     . ASN A 1 125 ? 9.14925   -20.73829 48.46405  1.000 57.87275 ? 119  ASN A N     1 
ATOM   939  C CA    . ASN A 1 125 ? 10.43160  -20.08980 48.24150  1.000 55.41566 ? 119  ASN A CA    1 
ATOM   940  C C     . ASN A 1 125 ? 10.30573  -18.59311 47.97000  1.000 48.56282 ? 119  ASN A C     1 
ATOM   941  O O     . ASN A 1 125 ? 11.33081  -17.90549 47.90088  1.000 40.25580 ? 119  ASN A O     1 
ATOM   942  C CB    . ASN A 1 125 ? 11.15143  -20.76077 47.06859  1.000 56.54573 ? 119  ASN A CB    1 
ATOM   943  C CG    . ASN A 1 125 ? 11.45438  -22.22667 47.32774  1.000 70.23384 ? 119  ASN A CG    1 
ATOM   944  O OD1   . ASN A 1 125 ? 10.54217  -23.04301 47.49344  1.000 68.75393 ? 119  ASN A OD1   1 
ATOM   945  N ND2   . ASN A 1 125 ? 12.73883  -22.56659 47.37589  1.000 70.58445 ? 119  ASN A ND2   1 
ATOM   946  N N     . SER A 1 126 ? 9.08055   -18.08247 47.82807  1.000 42.07030 ? 120  SER A N     1 
ATOM   947  C CA    . SER A 1 126 ? 8.82552   -16.67338 47.50851  1.000 43.56658 ? 120  SER A CA    1 
ATOM   948  C C     . SER A 1 126 ? 9.53670   -16.24027 46.21926  1.000 42.44219 ? 120  SER A C     1 
ATOM   949  O O     . SER A 1 126 ? 10.20769  -15.21086 46.16816  1.000 39.00760 ? 120  SER A O     1 
ATOM   950  C CB    . SER A 1 126 ? 9.21025   -15.76491 48.68052  1.000 49.75274 ? 120  SER A CB    1 
ATOM   951  O OG    . SER A 1 126 ? 8.10628   -15.54369 49.55316  1.000 52.41327 ? 120  SER A OG    1 
ATOM   952  N N     . PHE A 1 127 ? 9.38306   -17.03147 45.15867  1.000 40.38457 ? 121  PHE A N     1 
ATOM   953  C CA    . PHE A 1 127 ? 9.90809   -16.62778 43.86083  1.000 34.12277 ? 121  PHE A CA    1 
ATOM   954  C C     . PHE A 1 127 ? 8.98612   -17.11220 42.75801  1.000 39.67978 ? 121  PHE A C     1 
ATOM   955  O O     . PHE A 1 127 ? 8.00092   -17.81966 42.99676  1.000 37.55526 ? 121  PHE A O     1 
ATOM   956  C CB    . PHE A 1 127 ? 11.37999  -17.05020 43.65699  1.000 37.65013 ? 121  PHE A CB    1 
ATOM   957  C CG    . PHE A 1 127 ? 11.62693  -18.54158 43.54669  1.000 38.46673 ? 121  PHE A CG    1 
ATOM   958  C CD1   . PHE A 1 127 ? 10.93937  -19.34212 42.65435  1.000 46.87171 ? 121  PHE A CD1   1 
ATOM   959  C CD2   . PHE A 1 127 ? 12.64232  -19.11525 44.28423  1.000 48.91016 ? 121  PHE A CD2   1 
ATOM   960  C CE1   . PHE A 1 127 ? 11.20647  -20.70819 42.56552  1.000 49.07935 ? 121  PHE A CE1   1 
ATOM   961  C CE2   . PHE A 1 127 ? 12.92326  -20.47206 44.19044  1.000 50.83210 ? 121  PHE A CE2   1 
ATOM   962  C CZ    . PHE A 1 127 ? 12.20303  -21.26605 43.33024  1.000 54.57905 ? 121  PHE A CZ    1 
ATOM   963  N N     . TRP A 1 128 ? 9.30755   -16.68648 41.53908  1.000 36.36428 ? 122  TRP A N     1 
ATOM   964  C CA    . TRP A 1 128 ? 8.49499   -16.94735 40.36030  1.000 32.12478 ? 122  TRP A CA    1 
ATOM   965  C C     . TRP A 1 128 ? 9.15141   -18.01433 39.49551  1.000 30.00187 ? 122  TRP A C     1 
ATOM   966  O O     . TRP A 1 128 ? 10.34809  -17.92516 39.20676  1.000 32.19358 ? 122  TRP A O     1 
ATOM   967  C CB    . TRP A 1 128 ? 8.30527   -15.66102 39.54737  1.000 30.23115 ? 122  TRP A CB    1 
ATOM   968  C CG    . TRP A 1 128 ? 7.26727   -14.75310 40.10975  1.000 25.98211 ? 122  TRP A CG    1 
ATOM   969  C CD1   . TRP A 1 128 ? 7.46227   -13.69251 40.96665  1.000 27.88124 ? 122  TRP A CD1   1 
ATOM   970  C CD2   . TRP A 1 128 ? 5.86418   -14.82332 39.87411  1.000 24.52807 ? 122  TRP A CD2   1 
ATOM   971  N NE1   . TRP A 1 128 ? 6.25106   -13.10070 41.26782  1.000 29.36131 ? 122  TRP A NE1   1 
ATOM   972  C CE2   . TRP A 1 128 ? 5.25856   -13.78052 40.61366  1.000 28.46738 ? 122  TRP A CE2   1 
ATOM   973  C CE3   . TRP A 1 128 ? 5.05157   -15.67832 39.12657  1.000 28.67570 ? 122  TRP A CE3   1 
ATOM   974  C CZ2   . TRP A 1 128 ? 3.89218   -13.56062 40.60678  1.000 26.36201 ? 122  TRP A CZ2   1 
ATOM   975  C CZ3   . TRP A 1 128 ? 3.68264   -15.45584 39.13133  1.000 31.80231 ? 122  TRP A CZ3   1 
ATOM   976  C CH2   . TRP A 1 128 ? 3.12297   -14.41083 39.86424  1.000 33.03177 ? 122  TRP A CH2   1 
ATOM   977  N N     . ASN A 1 129 ? 8.36310   -19.02710 39.09724  1.000 34.29379 ? 123  ASN A N     1 
ATOM   978  C CA    . ASN A 1 129 ? 8.73462   -19.98852 38.05693  1.000 35.88785 ? 123  ASN A CA    1 
ATOM   979  C C     . ASN A 1 129 ? 8.11995   -19.51680 36.73714  1.000 33.04871 ? 123  ASN A C     1 
ATOM   980  O O     . ASN A 1 129 ? 6.89744   -19.46005 36.60482  1.000 30.82376 ? 123  ASN A O     1 
ATOM   981  C CB    . ASN A 1 129 ? 8.24538   -21.40360 38.37550  1.000 37.52083 ? 123  ASN A CB    1 
ATOM   982  C CG    . ASN A 1 129 ? 8.86424   -21.98277 39.62364  1.000 39.51142 ? 123  ASN A CG    1 
ATOM   983  O OD1   . ASN A 1 129 ? 10.08718  -22.10603 39.73214  1.000 40.21343 ? 123  ASN A OD1   1 
ATOM   984  N ND2   . ASN A 1 129 ? 8.01478   -22.35375 40.57994  1.000 50.84130 ? 123  ASN A ND2   1 
ATOM   985  N N     . VAL A 1 130 ? 8.96529   -19.17620 35.76969  1.000 33.29542 ? 124  VAL A N     1 
ATOM   986  C CA    . VAL A 1 130 ? 8.52310   -18.61319 34.49958  1.000 35.31582 ? 124  VAL A CA    1 
ATOM   987  C C     . VAL A 1 130 ? 8.88785   -19.59976 33.40787  1.000 30.13080 ? 124  VAL A C     1 
ATOM   988  O O     . VAL A 1 130 ? 10.04279  -20.02241 33.31584  1.000 34.54094 ? 124  VAL A O     1 
ATOM   989  C CB    . VAL A 1 130 ? 9.17350   -17.24548 34.22994  1.000 30.20927 ? 124  VAL A CB    1 
ATOM   990  C CG1   . VAL A 1 130 ? 8.68714   -16.68759 32.89266  1.000 28.76847 ? 124  VAL A CG1   1 
ATOM   991  C CG2   . VAL A 1 130 ? 8.87967   -16.29786 35.37920  1.000 29.90774 ? 124  VAL A CG2   1 
ATOM   992  N N     . THR A 1 131 ? 7.92621   -19.93984 32.56305  1.000 32.69540 ? 125  THR A N     1 
ATOM   993  C CA    . THR A 1 131 ? 8.17525   -20.92757 31.53046  1.000 32.92703 ? 125  THR A CA    1 
ATOM   994  C C     . THR A 1 131 ? 7.96563   -20.29927 30.16524  1.000 28.70436 ? 125  THR A C     1 
ATOM   995  O O     . THR A 1 131 ? 6.93414   -19.66932 29.93172  1.000 31.64761 ? 125  THR A O     1 
ATOM   996  C CB    . THR A 1 131 ? 7.26633   -22.14625 31.72719  1.000 35.16063 ? 125  THR A CB    1 
ATOM   997  O OG1   . THR A 1 131 ? 7.56449   -22.71757 33.01158  1.000 38.83430 ? 125  THR A OG1   1 
ATOM   998  C CG2   . THR A 1 131 ? 7.55285   -23.20207 30.65956  1.000 36.43702 ? 125  THR A CG2   1 
ATOM   999  N N     . THR A 1 132 ? 8.94072   -20.48208 29.27549  1.000 28.15859 ? 126  THR A N     1 
ATOM   1000 C CA    . THR A 1 132 ? 8.82189   -19.99356 27.90634  1.000 30.23691 ? 126  THR A CA    1 
ATOM   1001 C C     . THR A 1 132 ? 7.91452   -20.90998 27.08006  1.000 36.29753 ? 126  THR A C     1 
ATOM   1002 O O     . THR A 1 132 ? 7.49063   -21.98901 27.51636  1.000 34.80214 ? 126  THR A O     1 
ATOM   1003 C CB    . THR A 1 132 ? 10.19717  -19.87774 27.24877  1.000 33.10897 ? 126  THR A CB    1 
ATOM   1004 O OG1   . THR A 1 132 ? 10.68799  -21.17806 26.88027  1.000 33.58645 ? 126  THR A OG1   1 
ATOM   1005 C CG2   . THR A 1 132 ? 11.18822  -19.20942 28.18871  1.000 35.44427 ? 126  THR A CG2   1 
ATOM   1006 N N     . GLU A 1 133 ? 7.59138   -20.45626 25.86321  1.000 37.21203 ? 127  GLU A N     1 
ATOM   1007 C CA    . GLU A 1 133 ? 6.76474   -21.28173 24.99194  1.000 40.40413 ? 127  GLU A CA    1 
ATOM   1008 C C     . GLU A 1 133 ? 7.54162   -22.47412 24.45229  1.000 41.49418 ? 127  GLU A C     1 
ATOM   1009 O O     . GLU A 1 133 ? 6.92402   -23.40196 23.91536  1.000 40.17180 ? 127  GLU A O     1 
ATOM   1010 C CB    . GLU A 1 133 ? 6.20495   -20.46050 23.82875  1.000 34.36419 ? 127  GLU A CB    1 
ATOM   1011 C CG    . GLU A 1 133 ? 5.10752   -19.49216 24.23768  1.000 35.90339 ? 127  GLU A CG    1 
ATOM   1012 C CD    . GLU A 1 133 ? 4.73733   -18.50512 23.13537  1.000 46.65544 ? 127  GLU A CD    1 
ATOM   1013 O OE1   . GLU A 1 133 ? 5.52621   -18.33801 22.17331  1.000 47.09065 ? 127  GLU A OE1   1 
ATOM   1014 O OE2   . GLU A 1 133 ? 3.64961   -17.89655 23.24701  1.000 44.39188 ? 127  GLU A OE2   1 
ATOM   1015 N N     . ASN A 1 134 ? 8.87461   -22.45377 24.56901  1.000 37.34672 ? 128  ASN A N     1 
ATOM   1016 C CA    . ASN A 1 134 ? 9.74747   -23.56823 24.21650  1.000 42.44955 ? 128  ASN A CA    1 
ATOM   1017 C C     . ASN A 1 134 ? 10.15050  -24.39270 25.44753  1.000 42.73476 ? 128  ASN A C     1 
ATOM   1018 O O     . ASN A 1 134 ? 11.19834  -25.05079 25.43395  1.000 40.76863 ? 128  ASN A O     1 
ATOM   1019 C CB    . ASN A 1 134 ? 11.00044  -23.06035 23.48374  1.000 40.81658 ? 128  ASN A CB    1 
ATOM   1020 C CG    . ASN A 1 134 ? 10.68447  -21.99205 22.42812  1.000 53.69812 ? 128  ASN A CG    1 
ATOM   1021 O OD1   . ASN A 1 134 ? 10.09870  -22.28985 21.38804  1.000 53.71918 ? 128  ASN A OD1   1 
ATOM   1022 N ND2   . ASN A 1 134 ? 11.08449  -20.73977 22.69552  1.000 57.60565 ? 128  ASN A ND2   1 
ATOM   1023 N N     . ASP A 1 135 ? 9.35073   -24.33199 26.51817  1.000 41.40633 ? 129  ASP A N     1 
ATOM   1024 C CA    . ASP A 1 135 ? 9.48481   -25.12932 27.74052  1.000 41.29680 ? 129  ASP A CA    1 
ATOM   1025 C C     . ASP A 1 135 ? 10.75911  -24.84762 28.53543  1.000 43.93166 ? 129  ASP A C     1 
ATOM   1026 O O     . ASP A 1 135 ? 11.15664  -25.67594 29.36832  1.000 36.80583 ? 129  ASP A O     1 
ATOM   1027 C CB    . ASP A 1 135 ? 9.37944   -26.63336 27.44495  1.000 43.96304 ? 129  ASP A CB    1 
ATOM   1028 C CG    . ASP A 1 135 ? 8.11939   -26.97646 26.69647  1.000 52.24585 ? 129  ASP A CG    1 
ATOM   1029 O OD1   . ASP A 1 135 ? 7.02676   -26.72875 27.26002  1.000 50.71408 ? 129  ASP A OD1   1 
ATOM   1030 O OD2   . ASP A 1 135 ? 8.22510   -27.47327 25.54967  1.000 54.76269 ? 129  ASP A OD2   1 
ATOM   1031 N N     . GLU A 1 136 ? 11.40595  -23.69453 28.33686  1.000 40.39473 ? 130  GLU A N     1 
ATOM   1032 C CA    . GLU A 1 136 ? 12.50713  -23.30002 29.21157  1.000 38.47547 ? 130  GLU A CA    1 
ATOM   1033 C C     . GLU A 1 136 ? 11.94784  -22.72302 30.50740  1.000 35.63515 ? 130  GLU A C     1 
ATOM   1034 O O     . GLU A 1 136 ? 11.03559  -21.88873 30.48702  1.000 35.17343 ? 130  GLU A O     1 
ATOM   1035 C CB    . GLU A 1 136 ? 13.41230  -22.26379 28.55447  1.000 45.89877 ? 130  GLU A CB    1 
ATOM   1036 C CG    . GLU A 1 136 ? 14.53539  -22.79292 27.69286  1.000 48.74842 ? 130  GLU A CG    1 
ATOM   1037 C CD    . GLU A 1 136 ? 15.47118  -21.66978 27.25079  1.000 57.65544 ? 130  GLU A CD    1 
ATOM   1038 O OE1   . GLU A 1 136 ? 15.00605  -20.72640 26.56652  1.000 56.61695 ? 130  GLU A OE1   1 
ATOM   1039 O OE2   . GLU A 1 136 ? 16.66694  -21.72017 27.60407  1.000 60.39018 ? 130  GLU A OE2   1 
ATOM   1040 N N     . LYS A 1 137 ? 12.49891  -23.16018 31.63017  1.000 31.89231 ? 131  LYS A N     1 
ATOM   1041 C CA    . LYS A 1 137 ? 12.02592  -22.74727 32.94086  1.000 35.32247 ? 131  LYS A CA    1 
ATOM   1042 C C     . LYS A 1 137 ? 13.10622  -21.89829 33.59257  1.000 38.02261 ? 131  LYS A C     1 
ATOM   1043 O O     . LYS A 1 137 ? 14.28824  -22.26945 33.58125  1.000 38.31514 ? 131  LYS A O     1 
ATOM   1044 C CB    . LYS A 1 137 ? 11.68867  -23.95602 33.82293  1.000 40.62490 ? 131  LYS A CB    1 
ATOM   1045 C CG    . LYS A 1 137 ? 11.07131  -23.56521 35.15132  1.000 42.81171 ? 131  LYS A CG    1 
ATOM   1046 C CD    . LYS A 1 137 ? 11.84156  -24.21997 36.30526  1.000 52.38423 ? 131  LYS A CD    1 
ATOM   1047 C CE    . LYS A 1 137 ? 10.99101  -24.39095 37.55060  1.000 52.69938 ? 131  LYS A CE    1 
ATOM   1048 N NZ    . LYS A 1 137 ? 11.63355  -25.36928 38.45756  1.000 53.78225 ? 131  LYS A NZ    1 
ATOM   1049 N N     . PHE A 1 138 ? 12.69593  -20.75902 34.14269  1.000 34.85763 ? 132  PHE A N     1 
ATOM   1050 C CA    . PHE A 1 138 ? 13.57737  -19.82421 34.82912  1.000 37.18250 ? 132  PHE A CA    1 
ATOM   1051 C C     . PHE A 1 138 ? 12.94717  -19.44322 36.15588  1.000 33.96156 ? 132  PHE A C     1 
ATOM   1052 O O     . PHE A 1 138 ? 11.72359  -19.39706 36.27921  1.000 34.26066 ? 132  PHE A O     1 
ATOM   1053 C CB    . PHE A 1 138 ? 13.80384  -18.53877 34.01450  1.000 43.57480 ? 132  PHE A CB    1 
ATOM   1054 C CG    . PHE A 1 138 ? 14.45238  -18.76066 32.69095  1.000 36.57308 ? 132  PHE A CG    1 
ATOM   1055 C CD1   . PHE A 1 138 ? 15.82840  -18.74193 32.58546  1.000 38.78585 ? 132  PHE A CD1   1 
ATOM   1056 C CD2   . PHE A 1 138 ? 13.69163  -18.99242 31.55499  1.000 38.16043 ? 132  PHE A CD2   1 
ATOM   1057 C CE1   . PHE A 1 138 ? 16.44186  -18.93716 31.36522  1.000 42.03533 ? 132  PHE A CE1   1 
ATOM   1058 C CE2   . PHE A 1 138 ? 14.30419  -19.19239 30.32711  1.000 37.80659 ? 132  PHE A CE2   1 
ATOM   1059 C CZ    . PHE A 1 138 ? 15.67961  -19.16108 30.23799  1.000 33.82701 ? 132  PHE A CZ    1 
ATOM   1060 N N     . THR A 1 139 ? 13.78146  -19.11665 37.13864  1.000 36.24671 ? 133  THR A N     1 
ATOM   1061 C CA    . THR A 1 139 ? 13.27485  -18.70807 38.43640  1.000 38.44144 ? 133  THR A CA    1 
ATOM   1062 C C     . THR A 1 139 ? 13.77549  -17.30412 38.74943  1.000 32.24514 ? 133  THR A C     1 
ATOM   1063 O O     . THR A 1 139 ? 14.89359  -16.93274 38.37804  1.000 32.90820 ? 133  THR A O     1 
ATOM   1064 C CB    . THR A 1 139 ? 13.69050  -19.69161 39.54480  1.000 38.75160 ? 133  THR A CB    1 
ATOM   1065 O OG1   . THR A 1 139 ? 15.11652  -19.71326 39.66198  1.000 40.45000 ? 133  THR A OG1   1 
ATOM   1066 C CG2   . THR A 1 139 ? 13.18215  -21.09956 39.22116  1.000 39.46287 ? 133  THR A CG2   1 
ATOM   1067 N N     . ALA A 1 140 ? 12.93037  -16.52031 39.40209  1.000 32.56363 ? 134  ALA A N     1 
ATOM   1068 C CA    . ALA A 1 140 ? 13.35022  -15.16898 39.75432  1.000 37.02018 ? 134  ALA A CA    1 
ATOM   1069 C C     . ALA A 1 140 ? 12.53677  -14.67574 40.93563  1.000 29.01439 ? 134  ALA A C     1 
ATOM   1070 O O     . ALA A 1 140 ? 11.34147  -14.96253 41.04135  1.000 32.09452 ? 134  ALA A O     1 
ATOM   1071 C CB    . ALA A 1 140 ? 13.19885  -14.20948 38.56585  1.000 32.72785 ? 134  ALA A CB    1 
ATOM   1072 N N     . ARG A 1 141 ? 13.19871  -13.93036 41.82056  1.000 33.26738 ? 135  ARG A N     1 
ATOM   1073 C CA    . ARG A 1 141 ? 12.49652  -13.36356 42.96548  1.000 30.73166 ? 135  ARG A CA    1 
ATOM   1074 C C     . ARG A 1 141 ? 11.35527  -12.47031 42.50773  1.000 28.67906 ? 135  ARG A C     1 
ATOM   1075 O O     . ARG A 1 141 ? 10.23864  -12.56150 43.02821  1.000 30.09352 ? 135  ARG A O     1 
ATOM   1076 C CB    . ARG A 1 141 ? 13.46665  -12.56912 43.84158  1.000 34.81559 ? 135  ARG A CB    1 
ATOM   1077 C CG    . ARG A 1 141 ? 12.81527  -11.93197 45.06802  1.000 40.20643 ? 135  ARG A CG    1 
ATOM   1078 C CD    . ARG A 1 141 ? 12.50285  -12.96375 46.14864  1.000 47.41355 ? 135  ARG A CD    1 
ATOM   1079 N NE    . ARG A 1 141 ? 13.72780  -13.49852 46.73601  1.000 49.18004 ? 135  ARG A NE    1 
ATOM   1080 C CZ    . ARG A 1 141 ? 13.81772  -14.67717 47.33938  1.000 51.97764 ? 135  ARG A CZ    1 
ATOM   1081 N NH1   . ARG A 1 141 ? 12.78685  -15.50470 47.39391  1.000 41.52548 ? 135  ARG A NH1   1 
ATOM   1082 N NH2   . ARG A 1 141 ? 14.97270  -15.03416 47.89890  1.000 50.39975 ? 135  ARG A NH2   1 
ATOM   1083 N N     . PHE A 1 142 ? 11.60388  -11.61729 41.50758  1.000 29.70351 ? 136  PHE A N     1 
ATOM   1084 C CA    . PHE A 1 142 ? 10.60845  -10.64051 41.08754  1.000 26.92951 ? 136  PHE A CA    1 
ATOM   1085 C C     . PHE A 1 142 ? 10.26751  -10.79769 39.61490  1.000 28.35749 ? 136  PHE A C     1 
ATOM   1086 O O     . PHE A 1 142 ? 11.11649  -11.15460 38.79882  1.000 30.94004 ? 136  PHE A O     1 
ATOM   1087 C CB    . PHE A 1 142 ? 11.08979  -9.21578  41.31197  1.000 33.46305 ? 136  PHE A CB    1 
ATOM   1088 C CG    . PHE A 1 142 ? 11.40209  -8.92565  42.73572  1.000 32.56929 ? 136  PHE A CG    1 
ATOM   1089 C CD1   . PHE A 1 142 ? 10.38249  -8.85022  43.67768  1.000 32.24436 ? 136  PHE A CD1   1 
ATOM   1090 C CD2   . PHE A 1 142 ? 12.70957  -8.79543  43.13996  1.000 32.17825 ? 136  PHE A CD2   1 
ATOM   1091 C CE1   . PHE A 1 142 ? 10.68549  -8.61271  45.01696  1.000 33.72438 ? 136  PHE A CE1   1 
ATOM   1092 C CE2   . PHE A 1 142 ? 13.01243  -8.55704  44.46496  1.000 29.32356 ? 136  PHE A CE2   1 
ATOM   1093 C CZ    . PHE A 1 142 ? 11.99743  -8.45430  45.39106  1.000 33.21832 ? 136  PHE A CZ    1 
ATOM   1094 N N     . LEU A 1 143 ? 9.02382   -10.48398 39.28668  1.000 27.27010 ? 137  LEU A N     1 
ATOM   1095 C CA    . LEU A 1 143 ? 8.54571   -10.54991 37.91063  1.000 26.66703 ? 137  LEU A CA    1 
ATOM   1096 C C     . LEU A 1 143 ? 8.09886   -9.15587  37.49575  1.000 31.07612 ? 137  LEU A C     1 
ATOM   1097 O O     . LEU A 1 143 ? 7.18250   -8.59974  38.10661  1.000 29.41951 ? 137  LEU A O     1 
ATOM   1098 C CB    . LEU A 1 143 ? 7.38558   -11.53351 37.80303  1.000 28.26518 ? 137  LEU A CB    1 
ATOM   1099 C CG    . LEU A 1 143 ? 6.70943   -11.61393 36.44582  1.000 31.84543 ? 137  LEU A CG    1 
ATOM   1100 C CD1   . LEU A 1 143 ? 7.67355   -12.26272 35.46287  1.000 29.65338 ? 137  LEU A CD1   1 
ATOM   1101 C CD2   . LEU A 1 143 ? 5.42937   -12.39835 36.55346  1.000 24.96395 ? 137  LEU A CD2   1 
ATOM   1102 N N     . ILE A 1 144 ? 8.70332   -8.61546  36.43589  1.000 27.78163 ? 138  ILE A N     1 
ATOM   1103 C CA    . ILE A 1 144 ? 8.36052   -7.28425  35.93596  1.000 23.38058 ? 138  ILE A CA    1 
ATOM   1104 C C     . ILE A 1 144 ? 7.63261   -7.46853  34.61988  1.000 26.50759 ? 138  ILE A C     1 
ATOM   1105 O O     . ILE A 1 144 ? 8.21339   -7.98068  33.65542  1.000 27.93053 ? 138  ILE A O     1 
ATOM   1106 C CB    . ILE A 1 144 ? 9.60560   -6.40311  35.74686  1.000 22.32937 ? 138  ILE A CB    1 
ATOM   1107 C CG1   . ILE A 1 144 ? 10.57906  -6.49504  36.93534  1.000 29.80822 ? 138  ILE A CG1   1 
ATOM   1108 C CG2   . ILE A 1 144 ? 9.17588   -4.92472  35.47407  1.000 24.77495 ? 138  ILE A CG2   1 
ATOM   1109 C CD1   . ILE A 1 144 ? 9.99432   -6.05977  38.27918  1.000 31.69209 ? 138  ILE A CD1   1 
ATOM   1110 N N     . THR A 1 145 ? 6.37460   -7.04885  34.56625  1.000 27.37137 ? 139  THR A N     1 
ATOM   1111 C CA    . THR A 1 145 ? 5.57453   -7.19708  33.36121  1.000 25.31767 ? 139  THR A CA    1 
ATOM   1112 C C     . THR A 1 145 ? 5.47391   -5.83951  32.67972  1.000 26.79208 ? 139  THR A C     1 
ATOM   1113 O O     . THR A 1 145 ? 4.89745   -4.90172  33.24014  1.000 27.61486 ? 139  THR A O     1 
ATOM   1114 C CB    . THR A 1 145 ? 4.21167   -7.79130  33.69321  1.000 27.44431 ? 139  THR A CB    1 
ATOM   1115 O OG1   . THR A 1 145 ? 3.56555   -7.00978  34.71163  1.000 30.40297 ? 139  THR A OG1   1 
ATOM   1116 C CG2   . THR A 1 145 ? 4.37539   -9.27207  34.14670  1.000 30.12314 ? 139  THR A CG2   1 
ATOM   1117 N N     . ALA A 1 146 ? 6.08782   -5.73728  31.50226  1.000 24.49232 ? 140  ALA A N     1 
ATOM   1118 C CA    . ALA A 1 146 ? 6.10497   -4.51939  30.68582  1.000 23.43174 ? 140  ALA A CA    1 
ATOM   1119 C C     . ALA A 1 146 ? 5.43210   -4.83996  29.34630  1.000 23.83424 ? 140  ALA A C     1 
ATOM   1120 O O     . ALA A 1 146 ? 6.08453   -4.82685  28.30381  1.000 25.92978 ? 140  ALA A O     1 
ATOM   1121 C CB    . ALA A 1 146 ? 7.54065   -4.02030  30.48101  1.000 21.85603 ? 140  ALA A CB    1 
ATOM   1122 N N     . LEU A 1 147 ? 4.13221   -5.12057  29.38970  1.000 24.43785 ? 141  LEU A N     1 
ATOM   1123 C CA    . LEU A 1 147 ? 3.41595   -5.71350  28.26549  1.000 27.40689 ? 141  LEU A CA    1 
ATOM   1124 C C     . LEU A 1 147 ? 2.73016   -4.68008  27.38294  1.000 28.20393 ? 141  LEU A C     1 
ATOM   1125 O O     . LEU A 1 147 ? 2.18678   -5.05323  26.33959  1.000 29.08311 ? 141  LEU A O     1 
ATOM   1126 C CB    . LEU A 1 147 ? 2.34527   -6.69768  28.77186  1.000 25.44973 ? 141  LEU A CB    1 
ATOM   1127 C CG    . LEU A 1 147 ? 2.74499   -7.74575  29.81002  1.000 24.73154 ? 141  LEU A CG    1 
ATOM   1128 C CD1   . LEU A 1 147 ? 1.53433   -8.68749  30.18530  1.000 25.61295 ? 141  LEU A CD1   1 
ATOM   1129 C CD2   . LEU A 1 147 ? 3.95346   -8.52678  29.34469  1.000 28.93216 ? 141  LEU A CD2   1 
ATOM   1130 N N     . GLY A 1 148 ? 2.72385   -3.41170  27.77745  1.000 28.22424 ? 142  GLY A N     1 
ATOM   1131 C CA    . GLY A 1 148 ? 2.12614   -2.36354  26.97009  1.000 31.21715 ? 142  GLY A CA    1 
ATOM   1132 C C     . GLY A 1 148 ? 0.62091   -2.21163  27.13238  1.000 31.42265 ? 142  GLY A C     1 
ATOM   1133 O O     . GLY A 1 148 ? -0.02412  -2.94494  27.88478  1.000 35.12819 ? 142  GLY A O     1 
ATOM   1134 N N     . PRO A 1 149 ? 0.02786   -1.25354  26.41077  1.000 31.09101 ? 143  PRO A N     1 
ATOM   1135 C CA    . PRO A 1 149 ? -1.39183  -0.93548  26.61103  1.000 35.33575 ? 143  PRO A CA    1 
ATOM   1136 C C     . PRO A 1 149 ? -2.37458  -1.76741  25.79776  1.000 38.06871 ? 143  PRO A C     1 
ATOM   1137 O O     . PRO A 1 149 ? -3.57961  -1.69894  26.07867  1.000 42.57698 ? 143  PRO A O     1 
ATOM   1138 C CB    . PRO A 1 149 ? -1.46308  0.53408   26.17396  1.000 35.13068 ? 143  PRO A CB    1 
ATOM   1139 C CG    . PRO A 1 149 ? -0.47019  0.62043   25.06469  1.000 37.09570 ? 143  PRO A CG    1 
ATOM   1140 C CD    . PRO A 1 149 ? 0.66791   -0.33692  25.45120  1.000 32.76131 ? 143  PRO A CD    1 
ATOM   1141 N N     . LEU A 1 150 ? -1.91379  -2.52750  24.80626  1.000 33.01369 ? 144  LEU A N     1 
ATOM   1142 C CA    . LEU A 1 150 ? -2.78721  -3.19520  23.85082  1.000 37.22775 ? 144  LEU A CA    1 
ATOM   1143 C C     . LEU A 1 150 ? -2.57614  -4.70277  23.87722  1.000 36.60303 ? 144  LEU A C     1 
ATOM   1144 O O     . LEU A 1 150 ? -1.43754  -5.18024  23.93503  1.000 39.94310 ? 144  LEU A O     1 
ATOM   1145 C CB    . LEU A 1 150 ? -2.52658  -2.70095  22.42268  1.000 38.37187 ? 144  LEU A CB    1 
ATOM   1146 C CG    . LEU A 1 150 ? -2.63098  -1.21197  22.09898  1.000 43.14444 ? 144  LEU A CG    1 
ATOM   1147 C CD1   . LEU A 1 150 ? -1.97492  -0.98031  20.74104  1.000 44.33630 ? 144  LEU A CD1   1 
ATOM   1148 C CD2   . LEU A 1 150 ? -4.07406  -0.76074  22.10326  1.000 43.31600 ? 144  LEU A CD2   1 
ATOM   1149 N N     . SER A 1 151 ? -3.67561  -5.45115  23.77364  1.000 33.74383 ? 145  SER A N     1 
ATOM   1150 C CA    . SER A 1 151 ? -3.56829  -6.89463  23.61447  1.000 32.91601 ? 145  SER A CA    1 
ATOM   1151 C C     . SER A 1 151 ? -3.68645  -7.31613  22.14468  1.000 32.96892 ? 145  SER A C     1 
ATOM   1152 O O     . SER A 1 151 ? -3.27496  -6.57624  21.25159  1.000 32.06949 ? 145  SER A O     1 
ATOM   1153 C CB    . SER A 1 151 ? -4.62414  -7.59088  24.46698  1.000 41.95722 ? 145  SER A CB    1 
ATOM   1154 O OG    . SER A 1 151 ? -4.25256  -8.93946  24.67163  1.000 44.81224 ? 145  SER A OG    1 
ATOM   1155 N N     . SER A 1 152 ? -4.23852  -8.50237  21.88607  1.000 36.30462 ? 146  SER A N     1 
ATOM   1156 C CA    . SER A 1 152 ? -4.24129  -9.07578  20.54513  1.000 33.95028 ? 146  SER A CA    1 
ATOM   1157 C C     . SER A 1 152 ? -5.00170  -8.18841  19.55720  1.000 30.51673 ? 146  SER A C     1 
ATOM   1158 O O     . SER A 1 152 ? -5.99385  -7.55073  19.92002  1.000 31.92290 ? 146  SER A O     1 
ATOM   1159 C CB    . SER A 1 152 ? -4.87956  -10.46095 20.56485  1.000 39.97836 ? 146  SER A CB    1 
ATOM   1160 O OG    . SER A 1 152 ? -4.30316  -11.26209 21.57981  1.000 47.50401 ? 146  SER A OG    1 
ATOM   1161 N N     . PRO A 1 153 ? -4.56523  -8.14535  18.29969  1.000 29.63255 ? 147  PRO A N     1 
ATOM   1162 C CA    . PRO A 1 153 ? -5.33603  -7.41608  17.27748  1.000 29.08685 ? 147  PRO A CA    1 
ATOM   1163 C C     . PRO A 1 153 ? -6.74297  -7.96257  17.16886  1.000 31.59181 ? 147  PRO A C     1 
ATOM   1164 O O     . PRO A 1 153 ? -6.95572  -9.18091  17.14994  1.000 31.62025 ? 147  PRO A O     1 
ATOM   1165 C CB    . PRO A 1 153 ? -4.55988  -7.66060  15.97784  1.000 31.44900 ? 147  PRO A CB    1 
ATOM   1166 C CG    . PRO A 1 153 ? -3.35152  -8.40633  16.30835  1.000 36.31129 ? 147  PRO A CG    1 
ATOM   1167 C CD    . PRO A 1 153 ? -3.36116  -8.78885  17.76499  1.000 36.64177 ? 147  PRO A CD    1 
ATOM   1168 N N     . HIS A 1 154 ? -7.70733  -7.04954  17.06086  1.000 28.19877 ? 148  HIS A N     1 
ATOM   1169 C CA    . HIS A 1 154 ? -9.10219  -7.40490  16.82832  1.000 28.21579 ? 148  HIS A CA    1 
ATOM   1170 C C     . HIS A 1 154 ? -9.39203  -7.33138  15.33395  1.000 37.28511 ? 148  HIS A C     1 
ATOM   1171 O O     . HIS A 1 154 ? -9.27878  -6.25977  14.73109  1.000 27.67786 ? 148  HIS A O     1 
ATOM   1172 C CB    . HIS A 1 154 ? -10.05498 -6.48354  17.58909  1.000 34.99848 ? 148  HIS A CB    1 
ATOM   1173 C CG    . HIS A 1 154 ? -11.49880 -6.70770  17.24693  1.000 36.03994 ? 148  HIS A CG    1 
ATOM   1174 N ND1   . HIS A 1 154 ? -12.17863 -7.84641  17.62047  1.000 34.13125 ? 148  HIS A ND1   1 
ATOM   1175 C CD2   . HIS A 1 154 ? -12.38972 -5.94717  16.55939  1.000 44.03748 ? 148  HIS A CD2   1 
ATOM   1176 C CE1   . HIS A 1 154 ? -13.42280 -7.78472  17.17426  1.000 38.07135 ? 148  HIS A CE1   1 
ATOM   1177 N NE2   . HIS A 1 154 ? -13.57716 -6.64590  16.52104  1.000 39.66454 ? 148  HIS A NE2   1 
ATOM   1178 N N     . LEU A 1 155 ? -9.76697  -8.47853  14.73473  1.000 35.89836 ? 149  LEU A N     1 
ATOM   1179 C CA    . LEU A 1 155 ? -10.27343 -8.49166  13.36473  1.000 37.02438 ? 149  LEU A CA    1 
ATOM   1180 C C     . LEU A 1 155 ? -11.80035 -8.43110  13.37263  1.000 37.97506 ? 149  LEU A C     1 
ATOM   1181 O O     . LEU A 1 155 ? -12.43917 -9.05829  14.22829  1.000 37.45372 ? 149  LEU A O     1 
ATOM   1182 C CB    . LEU A 1 155 ? -9.82601  -9.75299  12.63100  1.000 39.81122 ? 149  LEU A CB    1 
ATOM   1183 C CG    . LEU A 1 155 ? -8.41681  -9.80420  12.03971  1.000 45.21734 ? 149  LEU A CG    1 
ATOM   1184 C CD1   . LEU A 1 155 ? -8.08297  -11.23250 11.65663  1.000 55.96507 ? 149  LEU A CD1   1 
ATOM   1185 C CD2   . LEU A 1 155 ? -8.31741  -8.91762  10.80392  1.000 44.83782 ? 149  LEU A CD2   1 
ATOM   1186 N N     . PRO A 1 156 ? -12.42543 -7.70385  12.44328  1.000 37.00491 ? 150  PRO A N     1 
ATOM   1187 C CA    . PRO A 1 156 ? -13.88962 -7.62857  12.45447  1.000 36.89325 ? 150  PRO A CA    1 
ATOM   1188 C C     . PRO A 1 156 ? -14.47946 -9.00143  12.15278  1.000 31.12791 ? 150  PRO A C     1 
ATOM   1189 O O     . PRO A 1 156 ? -13.94635 -9.76550  11.34410  1.000 32.90898 ? 150  PRO A O     1 
ATOM   1190 C CB    . PRO A 1 156 ? -14.20528 -6.60868  11.35407  1.000 41.22299 ? 150  PRO A CB    1 
ATOM   1191 C CG    . PRO A 1 156 ? -13.06357 -6.73583  10.38567  1.000 32.66049 ? 150  PRO A CG    1 
ATOM   1192 C CD    . PRO A 1 156 ? -11.85202 -7.15482  11.20160  1.000 38.27733 ? 150  PRO A CD    1 
ATOM   1193 N N     . VAL A 1 157 ? -15.55291 -9.34032  12.85908  1.000 39.59929 ? 151  VAL A N     1 
ATOM   1194 C CA    . VAL A 1 157 ? -16.25525 -10.59505 12.62585  1.000 33.22947 ? 151  VAL A CA    1 
ATOM   1195 C C     . VAL A 1 157 ? -17.27944 -10.31055 11.53178  1.000 30.92314 ? 151  VAL A C     1 
ATOM   1196 O O     . VAL A 1 157 ? -18.31202 -9.69225  11.77810  1.000 39.93010 ? 151  VAL A O     1 
ATOM   1197 C CB    . VAL A 1 157 ? -16.90758 -11.12389 13.90328  1.000 39.09780 ? 151  VAL A CB    1 
ATOM   1198 C CG1   . VAL A 1 157 ? -17.67297 -12.39365 13.61349  1.000 35.45470 ? 151  VAL A CG1   1 
ATOM   1199 C CG2   . VAL A 1 157 ? -15.86287 -11.29966 14.99600  1.000 35.83273 ? 151  VAL A CG2   1 
ATOM   1200 N N     . ILE A 1 158 ? -16.95970 -10.70870 10.30065  1.000 32.95984 ? 152  ILE A N     1 
ATOM   1201 C CA    . ILE A 1 158 ? -17.79569 -10.43860 9.14176   1.000 30.77488 ? 152  ILE A CA    1 
ATOM   1202 C C     . ILE A 1 158 ? -17.94937 -11.73431 8.36807   1.000 29.69063 ? 152  ILE A C     1 
ATOM   1203 O O     . ILE A 1 158 ? -16.95302 -12.36972 8.00215   1.000 32.57725 ? 152  ILE A O     1 
ATOM   1204 C CB    . ILE A 1 158 ? -17.22231 -9.32973  8.23580   1.000 29.81170 ? 152  ILE A CB    1 
ATOM   1205 C CG1   . ILE A 1 158 ? -17.13124 -8.00666  9.02165   1.000 30.64899 ? 152  ILE A CG1   1 
ATOM   1206 C CG2   . ILE A 1 158 ? -18.07442 -9.19002  6.94507   1.000 29.99520 ? 152  ILE A CG2   1 
ATOM   1207 C CD1   . ILE A 1 158 ? -16.38621 -6.89775  8.29295   1.000 37.85784 ? 152  ILE A CD1   1 
ATOM   1208 N N     . LYS A 1 159 ? -19.19755 -12.11202 8.10855   1.000 29.86850 ? 153  LYS A N     1 
ATOM   1209 C CA    . LYS A 1 159 ? -19.48357 -13.29315 7.31553   1.000 31.07138 ? 153  LYS A CA    1 
ATOM   1210 C C     . LYS A 1 159 ? -18.67636 -13.29635 6.02449   1.000 36.55791 ? 153  LYS A C     1 
ATOM   1211 O O     . LYS A 1 159 ? -18.68076 -12.31613 5.27562   1.000 29.41876 ? 153  LYS A O     1 
ATOM   1212 C CB    . LYS A 1 159 ? -20.97420 -13.36380 6.98393   1.000 31.97925 ? 153  LYS A CB    1 
ATOM   1213 C CG    . LYS A 1 159 ? -21.25575 -14.54897 6.09056   1.000 38.53155 ? 153  LYS A CG    1 
ATOM   1214 C CD    . LYS A 1 159 ? -22.72031 -14.88131 5.93519   1.000 44.19942 ? 153  LYS A CD    1 
ATOM   1215 C CE    . LYS A 1 159 ? -23.51415 -13.85936 5.19921   1.000 45.39210 ? 153  LYS A CE    1 
ATOM   1216 N NZ    . LYS A 1 159 ? -24.84755 -14.48288 4.89217   1.000 49.08965 ? 153  LYS A NZ    1 
ATOM   1217 N N     . GLY A 1 160 ? -17.98237 -14.40670 5.77510   1.000 30.20659 ? 154  GLY A N     1 
ATOM   1218 C CA    . GLY A 1 160 ? -17.21962 -14.57718 4.55465   1.000 31.42153 ? 154  GLY A CA    1 
ATOM   1219 C C     . GLY A 1 160 ? -15.85092 -13.93888 4.52679   1.000 27.71618 ? 154  GLY A C     1 
ATOM   1220 O O     . GLY A 1 160 ? -15.18431 -14.01040 3.48630   1.000 29.63904 ? 154  GLY A O     1 
ATOM   1221 N N     . ILE A 1 161 ? -15.38414 -13.34739 5.63407   1.000 30.00344 ? 155  ILE A N     1 
ATOM   1222 C CA    . ILE A 1 161 ? -14.10322 -12.64437 5.56624   1.000 31.92829 ? 155  ILE A CA    1 
ATOM   1223 C C     . ILE A 1 161 ? -12.98452 -13.59764 5.16224   1.000 33.58184 ? 155  ILE A C     1 
ATOM   1224 O O     . ILE A 1 161 ? -12.04466 -13.20185 4.46098   1.000 31.39183 ? 155  ILE A O     1 
ATOM   1225 C CB    . ILE A 1 161 ? -13.79433 -11.89068 6.88118   1.000 33.37803 ? 155  ILE A CB    1 
ATOM   1226 C CG1   . ILE A 1 161 ? -12.55875 -11.01112 6.68438   1.000 32.82877 ? 155  ILE A CG1   1 
ATOM   1227 C CG2   . ILE A 1 161 ? -13.65734 -12.83379 8.10125   1.000 33.27731 ? 155  ILE A CG2   1 
ATOM   1228 C CD1   . ILE A 1 161 ? -12.37718 -9.97519  7.77855   1.000 35.00354 ? 155  ILE A CD1   1 
ATOM   1229 N N     . GLU A 1 162 ? -13.11885 -14.88355 5.48993   1.000 31.04579 ? 156  GLU A N     1 
ATOM   1230 C CA    . GLU A 1 162 ? -12.08874 -15.84465 5.11947   1.000 32.55753 ? 156  GLU A CA    1 
ATOM   1231 C C     . GLU A 1 162 ? -12.11991 -16.22566 3.63870   1.000 35.10353 ? 156  GLU A C     1 
ATOM   1232 O O     . GLU A 1 162 ? -11.19289 -16.90308 3.17539   1.000 31.62564 ? 156  GLU A O     1 
ATOM   1233 C CB    . GLU A 1 162 ? -12.22750 -17.09007 5.99869   1.000 38.96935 ? 156  GLU A CB    1 
ATOM   1234 C CG    . GLU A 1 162 ? -13.42795 -17.99362 5.63845   1.000 35.33843 ? 156  GLU A CG    1 
ATOM   1235 C CD    . GLU A 1 162 ? -14.80108 -17.39375 5.96477   1.000 40.29018 ? 156  GLU A CD    1 
ATOM   1236 O OE1   . GLU A 1 162 ? -14.89494 -16.46249 6.80248   1.000 40.40099 ? 156  GLU A OE1   1 
ATOM   1237 O OE2   . GLU A 1 162 ? -15.79802 -17.88140 5.38128   1.000 46.06391 ? 156  GLU A OE2   1 
ATOM   1238 N N     . THR A 1 163 ? -13.13378 -15.79169 2.87388   1.000 29.93206 ? 157  THR A N     1 
ATOM   1239 C CA    . THR A 1 163 ? -13.17942 -16.09367 1.44609   1.000 28.25099 ? 157  THR A CA    1 
ATOM   1240 C C     . THR A 1 163 ? -12.44925 -15.06031 0.57454   1.000 27.88274 ? 157  THR A C     1 
ATOM   1241 O O     . THR A 1 163 ? -12.23684 -15.31747 -0.61347  1.000 25.92900 ? 157  THR A O     1 
ATOM   1242 C CB    . THR A 1 163 ? -14.64862 -16.21972 0.96719   1.000 33.77046 ? 157  THR A CB    1 
ATOM   1243 O OG1   . THR A 1 163 ? -15.27138 -14.92919 0.89127   1.000 29.23585 ? 157  THR A OG1   1 
ATOM   1244 C CG2   . THR A 1 163 ? -15.46295 -17.10330 1.93728   1.000 31.80444 ? 157  THR A CG2   1 
ATOM   1245 N N     . PHE A 1 164 ? -12.08333 -13.90113 1.12344   1.000 24.89921 ? 158  PHE A N     1 
ATOM   1246 C CA    . PHE A 1 164 ? -11.44134 -12.84847 0.33619   1.000 28.42742 ? 158  PHE A CA    1 
ATOM   1247 C C     . PHE A 1 164 ? -10.10223 -13.33512 -0.22460  1.000 27.79625 ? 158  PHE A C     1 
ATOM   1248 O O     . PHE A 1 164 ? -9.26894  -13.87831 0.50482   1.000 28.89611 ? 158  PHE A O     1 
ATOM   1249 C CB    . PHE A 1 164 ? -11.23576 -11.59299 1.21793   1.000 29.02325 ? 158  PHE A CB    1 
ATOM   1250 C CG    . PHE A 1 164 ? -10.77257 -10.37197 0.45471   1.000 26.20807 ? 158  PHE A CG    1 
ATOM   1251 C CD1   . PHE A 1 164 ? -11.60841 -9.73746  -0.45202  1.000 27.99083 ? 158  PHE A CD1   1 
ATOM   1252 C CD2   . PHE A 1 164 ? -9.49693  -9.84372  0.67239   1.000 23.09040 ? 158  PHE A CD2   1 
ATOM   1253 C CE1   . PHE A 1 164 ? -11.17400 -8.61831  -1.17000  1.000 26.51775 ? 158  PHE A CE1   1 
ATOM   1254 C CE2   . PHE A 1 164 ? -9.07153  -8.72954  -0.02431  1.000 23.04122 ? 158  PHE A CE2   1 
ATOM   1255 C CZ    . PHE A 1 164 ? -9.89693  -8.11819  -0.95616  1.000 23.10703 ? 158  PHE A CZ    1 
ATOM   1256 N N     . LYS A 1 165 ? -9.89912  -13.14291 -1.53231  1.000 23.32175 ? 159  LYS A N     1 
ATOM   1257 C CA    . LYS A 1 165 ? -8.71084  -13.63282 -2.21620  1.000 25.53634 ? 159  LYS A CA    1 
ATOM   1258 C C     . LYS A 1 165 ? -7.67979  -12.53695 -2.47539  1.000 26.64754 ? 159  LYS A C     1 
ATOM   1259 O O     . LYS A 1 165 ? -6.57933  -12.84248 -2.93997  1.000 27.85561 ? 159  LYS A O     1 
ATOM   1260 C CB    . LYS A 1 165 ? -9.09843  -14.28144 -3.55199  1.000 33.13112 ? 159  LYS A CB    1 
ATOM   1261 C CG    . LYS A 1 165 ? -9.78750  -15.63972 -3.41616  1.000 33.60349 ? 159  LYS A CG    1 
ATOM   1262 C CD    . LYS A 1 165 ? -9.74788  -16.39982 -4.73617  1.000 45.48272 ? 159  LYS A CD    1 
ATOM   1263 C CE    . LYS A 1 165 ? -9.84906  -17.90697 -4.50421  1.000 53.77776 ? 159  LYS A CE    1 
ATOM   1264 N NZ    . LYS A 1 165 ? -11.21536 -18.26937 -4.09274  1.000 51.02709 ? 159  LYS A NZ    1 
ATOM   1265 N N     . GLY A 1 166 ? -8.01806  -11.27707 -2.21933  1.000 25.03638 ? 160  GLY A N     1 
ATOM   1266 C CA    . GLY A 1 166 ? -7.04831  -10.20853 -2.33904  1.000 23.07327 ? 160  GLY A CA    1 
ATOM   1267 C C     . GLY A 1 166 ? -6.17208  -10.11812 -1.10241  1.000 22.22893 ? 160  GLY A C     1 
ATOM   1268 O O     . GLY A 1 166 ? -6.13903  -11.00561 -0.24907  1.000 24.43576 ? 160  GLY A O     1 
ATOM   1269 N N     . GLU A 1 167 ? -5.43912  -9.00849  -1.01838  1.000 22.03595 ? 161  GLU A N     1 
ATOM   1270 C CA    . GLU A 1 167 ? -4.59501  -8.74040  0.13477   1.000 22.20677 ? 161  GLU A CA    1 
ATOM   1271 C C     . GLU A 1 167 ? -5.43964  -8.29464  1.31217   1.000 22.74615 ? 161  GLU A C     1 
ATOM   1272 O O     . GLU A 1 167 ? -6.23481  -7.36748  1.19200   1.000 22.91158 ? 161  GLU A O     1 
ATOM   1273 C CB    . GLU A 1 167 ? -3.57954  -7.65860  -0.22218  1.000 23.29992 ? 161  GLU A CB    1 
ATOM   1274 C CG    . GLU A 1 167 ? -2.65116  -8.04893  -1.35089  1.000 28.22624 ? 161  GLU A CG    1 
ATOM   1275 C CD    . GLU A 1 167 ? -1.84655  -6.86063  -1.85580  1.000 30.53175 ? 161  GLU A CD    1 
ATOM   1276 O OE1   . GLU A 1 167 ? -0.88866  -6.44656  -1.16747  1.000 37.44242 ? 161  GLU A OE1   1 
ATOM   1277 O OE2   . GLU A 1 167 ? -2.18319  -6.33828  -2.93746  1.000 27.23497 ? 161  GLU A OE2   1 
ATOM   1278 N N     . LEU A 1 168 ? -5.23248  -8.92353  2.46281   1.000 21.13733 ? 162  LEU A N     1 
ATOM   1279 C CA    . LEU A 1 168 ? -6.01025  -8.62573  3.65748   1.000 21.19494 ? 162  LEU A CA    1 
ATOM   1280 C C     . LEU A 1 168 ? -5.07189  -8.57228  4.84863   1.000 23.66102 ? 162  LEU A C     1 
ATOM   1281 O O     . LEU A 1 168 ? -4.37546  -9.55687  5.12615   1.000 22.89287 ? 162  LEU A O     1 
ATOM   1282 C CB    . LEU A 1 168 ? -7.07280  -9.70542  3.86063   1.000 23.07054 ? 162  LEU A CB    1 
ATOM   1283 C CG    . LEU A 1 168 ? -7.90496  -9.62872  5.13072   1.000 32.50197 ? 162  LEU A CG    1 
ATOM   1284 C CD1   . LEU A 1 168 ? -8.99392  -8.61675  4.94185   1.000 32.17154 ? 162  LEU A CD1   1 
ATOM   1285 C CD2   . LEU A 1 168 ? -8.48710  -11.00043 5.44687   1.000 40.51783 ? 162  LEU A CD2   1 
ATOM   1286 N N     . HIS A 1 169 ? -5.02098  -7.43601  5.54061   1.000 24.40923 ? 163  HIS A N     1 
ATOM   1287 C CA    . HIS A 1 169 ? -4.08429  -7.28986  6.65530   1.000 26.37539 ? 163  HIS A CA    1 
ATOM   1288 C C     . HIS A 1 169 ? -4.70666  -6.43563  7.74338   1.000 25.24235 ? 163  HIS A C     1 
ATOM   1289 O O     . HIS A 1 169 ? -5.35915  -5.43650  7.44317   1.000 21.95675 ? 163  HIS A O     1 
ATOM   1290 C CB    . HIS A 1 169 ? -2.78243  -6.57651  6.24302   1.000 28.34801 ? 163  HIS A CB    1 
ATOM   1291 C CG    . HIS A 1 169 ? -2.18541  -7.05612  4.95972   1.000 31.30085 ? 163  HIS A CG    1 
ATOM   1292 N ND1   . HIS A 1 169 ? -2.10361  -6.25349  3.84578   1.000 37.47719 ? 163  HIS A ND1   1 
ATOM   1293 C CD2   . HIS A 1 169 ? -1.60455  -8.23547  4.62064   1.000 45.57271 ? 163  HIS A CD2   1 
ATOM   1294 C CE1   . HIS A 1 169 ? -1.52672  -6.92324  2.86252   1.000 44.08074 ? 163  HIS A CE1   1 
ATOM   1295 N NE2   . HIS A 1 169 ? -1.21546  -8.13061  3.30392   1.000 39.25427 ? 163  HIS A NE2   1 
ATOM   1296 N N     . HIS A 1 170 ? -4.48952  -6.82529  8.99433   1.000 25.05108 ? 164  HIS A N     1 
ATOM   1297 C CA    . HIS A 1 170 ? -4.65832  -5.90344  10.10182  1.000 26.31272 ? 164  HIS A CA    1 
ATOM   1298 C C     . HIS A 1 170 ? -3.44953  -4.96652  10.13929  1.000 23.86231 ? 164  HIS A C     1 
ATOM   1299 O O     . HIS A 1 170 ? -2.34632  -5.32205  9.71892   1.000 22.91949 ? 164  HIS A O     1 
ATOM   1300 C CB    . HIS A 1 170 ? -4.80815  -6.68348  11.41133  1.000 26.28918 ? 164  HIS A CB    1 
ATOM   1301 C CG    . HIS A 1 170 ? -5.26527  -5.87333  12.58185  1.000 25.69615 ? 164  HIS A CG    1 
ATOM   1302 N ND1   . HIS A 1 170 ? -4.41790  -5.05655  13.30090  1.000 26.70675 ? 164  HIS A ND1   1 
ATOM   1303 C CD2   . HIS A 1 170 ? -6.48296  -5.76546  13.17279  1.000 25.23475 ? 164  HIS A CD2   1 
ATOM   1304 C CE1   . HIS A 1 170 ? -5.09437  -4.47059  14.27421  1.000 26.09802 ? 164  HIS A CE1   1 
ATOM   1305 N NE2   . HIS A 1 170 ? -6.35065  -4.88550  14.21897  1.000 26.00915 ? 164  HIS A NE2   1 
ATOM   1306 N N     . THR A 1 171 ? -3.67811  -3.74133  10.60893  1.000 23.55950 ? 165  THR A N     1 
ATOM   1307 C CA    . THR A 1 171 ? -2.60094  -2.75947  10.63266  1.000 24.92277 ? 165  THR A CA    1 
ATOM   1308 C C     . THR A 1 171 ? -1.45045  -3.17443  11.53518  1.000 23.92198 ? 165  THR A C     1 
ATOM   1309 O O     . THR A 1 171 ? -0.32716  -2.68637  11.33485  1.000 19.71824 ? 165  THR A O     1 
ATOM   1310 C CB    . THR A 1 171 ? -3.13434  -1.39245  11.08154  1.000 20.37248 ? 165  THR A CB    1 
ATOM   1311 O OG1   . THR A 1 171 ? -3.83222  -1.51479  12.33701  1.000 23.92139 ? 165  THR A OG1   1 
ATOM   1312 C CG2   . THR A 1 171 ? -4.04692  -0.80791  10.02602  1.000 21.06676 ? 165  THR A CG2   1 
ATOM   1313 N N     . SER A 1 172 ? -1.71012  -4.01700  12.53829  1.000 23.85855 ? 166  SER A N     1 
ATOM   1314 C CA    . SER A 1 172 ? -0.64642  -4.50033  13.41875  1.000 23.92449 ? 166  SER A CA    1 
ATOM   1315 C C     . SER A 1 172 ? 0.17173   -5.61881  12.80482  1.000 28.03604 ? 166  SER A C     1 
ATOM   1316 O O     . SER A 1 172 ? 1.13624   -6.07168  13.44546  1.000 25.74751 ? 166  SER A O     1 
ATOM   1317 C CB    . SER A 1 172 ? -1.19858  -5.01643  14.74754  1.000 23.88702 ? 166  SER A CB    1 
ATOM   1318 O OG    . SER A 1 172 ? -2.02994  -6.14948  14.51988  1.000 32.20145 ? 166  SER A OG    1 
ATOM   1319 N N     . ARG A 1 173 ? -0.19956  -6.08300  11.61158  1.000 23.90019 ? 167  ARG A N     1 
ATOM   1320 C CA    . ARG A 1 173 ? 0.53210   -7.10586  10.86761  1.000 28.72175 ? 167  ARG A CA    1 
ATOM   1321 C C     . ARG A 1 173 ? 0.78440   -6.63330  9.45040   1.000 29.12197 ? 167  ARG A C     1 
ATOM   1322 O O     . ARG A 1 173 ? 0.49388   -7.32994  8.47539   1.000 25.34720 ? 167  ARG A O     1 
ATOM   1323 C CB    . ARG A 1 173 ? -0.23050  -8.42478  10.81921  1.000 31.19893 ? 167  ARG A CB    1 
ATOM   1324 C CG    . ARG A 1 173 ? -0.49920  -9.05180  12.18502  1.000 35.45848 ? 167  ARG A CG    1 
ATOM   1325 C CD    . ARG A 1 173 ? -1.84745  -9.76017  12.16839  1.000 55.14751 ? 167  ARG A CD    1 
ATOM   1326 N NE    . ARG A 1 173 ? -2.00679  -10.67832 13.29059  1.000 66.26854 ? 167  ARG A NE    1 
ATOM   1327 C CZ    . ARG A 1 173 ? -3.17700  -11.13666 13.71305  1.000 68.57504 ? 167  ARG A CZ    1 
ATOM   1328 N NH1   . ARG A 1 173 ? -4.30768  -10.81721 13.09652  1.000 65.30382 ? 167  ARG A NH1   1 
ATOM   1329 N NH2   . ARG A 1 173 ? -3.21444  -11.93456 14.77823  1.000 66.90889 ? 167  ARG A NH2   1 
ATOM   1330 N N     . TRP A 1 174 ? 1.28930   -5.41646  9.32239   1.000 24.11263 ? 168  TRP A N     1 
ATOM   1331 C CA    . TRP A 1 174 ? 1.48865   -4.82719  8.02121   1.000 23.79714 ? 168  TRP A CA    1 
ATOM   1332 C C     . TRP A 1 174 ? 2.71485   -5.46004  7.39470   1.000 28.98077 ? 168  TRP A C     1 
ATOM   1333 O O     . TRP A 1 174 ? 3.80327   -5.38452  7.97166   1.000 30.50344 ? 168  TRP A O     1 
ATOM   1334 C CB    . TRP A 1 174 ? 1.65388   -3.30361  8.12440   1.000 24.17519 ? 168  TRP A CB    1 
ATOM   1335 C CG    . TRP A 1 174 ? 1.61427   -2.61693  6.78885   1.000 24.77753 ? 168  TRP A CG    1 
ATOM   1336 C CD1   . TRP A 1 174 ? 2.66440   -2.17804  6.03724   1.000 24.95961 ? 168  TRP A CD1   1 
ATOM   1337 C CD2   . TRP A 1 174 ? 0.43970   -2.36497  6.02302   1.000 29.41374 ? 168  TRP A CD2   1 
ATOM   1338 N NE1   . TRP A 1 174 ? 2.19982   -1.61431  4.85077   1.000 26.74841 ? 168  TRP A NE1   1 
ATOM   1339 C CE2   . TRP A 1 174 ? 0.83873   -1.74614  4.81955   1.000 23.29201 ? 168  TRP A CE2   1 
ATOM   1340 C CE3   . TRP A 1 174 ? -0.91756  -2.62068  6.23365   1.000 32.91460 ? 168  TRP A CE3   1 
ATOM   1341 C CZ2   . TRP A 1 174 ? -0.07061  -1.35526  3.85124   1.000 30.62907 ? 168  TRP A CZ2   1 
ATOM   1342 C CZ3   . TRP A 1 174 ? -1.82085  -2.24066  5.25588   1.000 40.68653 ? 168  TRP A CZ3   1 
ATOM   1343 C CH2   . TRP A 1 174 ? -1.39387  -1.61814  4.08217   1.000 37.65296 ? 168  TRP A CH2   1 
ATOM   1344 N N     . PRO A 1 175 ? 2.59192   -6.09347  6.23940   1.000 29.17566 ? 169  PRO A N     1 
ATOM   1345 C CA    . PRO A 1 175 ? 3.74509   -6.76602  5.65440   1.000 32.56321 ? 169  PRO A CA    1 
ATOM   1346 C C     . PRO A 1 175 ? 4.67246   -5.75921  4.99702   1.000 30.57244 ? 169  PRO A C     1 
ATOM   1347 O O     . PRO A 1 175 ? 4.31400   -4.61228  4.72165   1.000 33.16281 ? 169  PRO A O     1 
ATOM   1348 C CB    . PRO A 1 175 ? 3.11077   -7.73066  4.64287   1.000 39.11607 ? 169  PRO A CB    1 
ATOM   1349 C CG    . PRO A 1 175 ? 1.84489   -7.05299  4.22785   1.000 33.72070 ? 169  PRO A CG    1 
ATOM   1350 C CD    . PRO A 1 175 ? 1.40791   -6.13136  5.36324   1.000 25.88841 ? 169  PRO A CD    1 
ATOM   1351 N N     . LYS A 1 176 ? 5.92026   -6.16965  4.81131   1.000 35.60220 ? 170  LYS A N     1 
ATOM   1352 C CA    . LYS A 1 176 ? 6.79475   -5.32490  4.02042   1.000 39.14188 ? 170  LYS A CA    1 
ATOM   1353 C C     . LYS A 1 176 ? 6.37466   -5.41221  2.55521   1.000 35.74186 ? 170  LYS A C     1 
ATOM   1354 O O     . LYS A 1 176 ? 5.66727   -6.33461  2.13917   1.000 38.16571 ? 170  LYS A O     1 
ATOM   1355 C CB    . LYS A 1 176 ? 8.25678   -5.75129  4.17734   1.000 45.27366 ? 170  LYS A CB    1 
ATOM   1356 C CG    . LYS A 1 176 ? 8.79675   -5.74542  5.61139   1.000 43.14562 ? 170  LYS A CG    1 
ATOM   1357 C CD    . LYS A 1 176 ? 9.56059   -4.46253  5.88322   1.000 55.60709 ? 170  LYS A CD    1 
ATOM   1358 C CE    . LYS A 1 176 ? 9.38605   -4.00164  7.30688   1.000 51.72674 ? 170  LYS A CE    1 
ATOM   1359 N NZ    . LYS A 1 176 ? 9.86288   -2.61139  7.48248   1.000 62.05103 ? 170  LYS A NZ    1 
ATOM   1360 N N     . ASP A 1 177 ? 6.80563   -4.43410  1.77362   1.000 34.89321 ? 171  ASP A N     1 
ATOM   1361 C CA    . ASP A 1 177 ? 6.71972   -4.48203  0.31807   1.000 35.01963 ? 171  ASP A CA    1 
ATOM   1362 C C     . ASP A 1 177 ? 5.31512   -4.28398  -0.23886  1.000 36.24285 ? 171  ASP A C     1 
ATOM   1363 O O     . ASP A 1 177 ? 5.06771   -4.65886  -1.39352  1.000 34.44291 ? 171  ASP A O     1 
ATOM   1364 C CB    . ASP A 1 177 ? 7.25073   -5.81619  -0.22923  1.000 30.43459 ? 171  ASP A CB    1 
ATOM   1365 C CG    . ASP A 1 177 ? 8.71859   -5.99478  0.02798   1.000 39.98328 ? 171  ASP A CG    1 
ATOM   1366 O OD1   . ASP A 1 177 ? 9.45604   -4.97440  -0.03681  1.000 39.79074 ? 171  ASP A OD1   1 
ATOM   1367 O OD2   . ASP A 1 177 ? 9.11154   -7.14201  0.34314   1.000 41.97906 ? 171  ASP A OD2   1 
ATOM   1368 N N     . VAL A 1 178 ? 4.37643   -3.72618  0.51725   1.000 29.77680 ? 172  VAL A N     1 
ATOM   1369 C CA    . VAL A 1 178 ? 3.03660   -3.51915  -0.03401  1.000 26.74324 ? 172  VAL A CA    1 
ATOM   1370 C C     . VAL A 1 178 ? 3.08284   -2.39901  -1.06115  1.000 25.21040 ? 172  VAL A C     1 
ATOM   1371 O O     . VAL A 1 178 ? 3.67305   -1.34178  -0.81833  1.000 28.35852 ? 172  VAL A O     1 
ATOM   1372 C CB    . VAL A 1 178 ? 2.04155   -3.19028  1.08873   1.000 30.70867 ? 172  VAL A CB    1 
ATOM   1373 C CG1   . VAL A 1 178 ? 0.70486   -2.74696  0.49575   1.000 29.62045 ? 172  VAL A CG1   1 
ATOM   1374 C CG2   . VAL A 1 178 ? 1.87577   -4.37724  2.00466   1.000 30.62341 ? 172  VAL A CG2   1 
ATOM   1375 N N     . THR A 1 179 ? 2.46530   -2.61760  -2.22330  1.000 26.17582 ? 173  THR A N     1 
ATOM   1376 C CA    . THR A 1 179 ? 2.31832   -1.56325  -3.21145  1.000 28.06507 ? 173  THR A CA    1 
ATOM   1377 C C     . THR A 1 179 ? 0.84488   -1.20382  -3.38280  1.000 26.95173 ? 173  THR A C     1 
ATOM   1378 O O     . THR A 1 179 ? -0.04763  -2.03662  -3.21135  1.000 25.58870 ? 173  THR A O     1 
ATOM   1379 C CB    . THR A 1 179 ? 2.91484   -1.93676  -4.57989  1.000 32.60466 ? 173  THR A CB    1 
ATOM   1380 O OG1   . THR A 1 179 ? 2.12396   -2.94224  -5.20187  1.000 34.81051 ? 173  THR A OG1   1 
ATOM   1381 C CG2   . THR A 1 179 ? 4.35261   -2.43562  -4.45823  1.000 35.16411 ? 173  THR A CG2   1 
ATOM   1382 N N     . PHE A 1 180 ? 0.60985   0.04563   -3.73247  1.000 25.86065 ? 174  PHE A N     1 
ATOM   1383 C CA    . PHE A 1 180 ? -0.73605  0.58942   -3.83093  1.000 24.74416 ? 174  PHE A CA    1 
ATOM   1384 C C     . PHE A 1 180 ? -1.15441  0.94480   -5.23575  1.000 26.82902 ? 174  PHE A C     1 
ATOM   1385 O O     . PHE A 1 180 ? -2.35058  0.95779   -5.51233  1.000 22.47079 ? 174  PHE A O     1 
ATOM   1386 C CB    . PHE A 1 180 ? -0.84733  1.85076   -2.95250  1.000 23.43041 ? 174  PHE A CB    1 
ATOM   1387 C CG    . PHE A 1 180 ? -0.69311  1.56102   -1.49200  1.000 24.72093 ? 174  PHE A CG    1 
ATOM   1388 C CD1   . PHE A 1 180 ? -1.62304  0.75416   -0.84404  1.000 27.16470 ? 174  PHE A CD1   1 
ATOM   1389 C CD2   . PHE A 1 180 ? 0.40720   2.03308   -0.78922  1.000 27.20652 ? 174  PHE A CD2   1 
ATOM   1390 C CE1   . PHE A 1 180 ? -1.48420  0.43460   0.52028   1.000 27.41323 ? 174  PHE A CE1   1 
ATOM   1391 C CE2   . PHE A 1 180 ? 0.56612   1.71786   0.57497   1.000 28.89051 ? 174  PHE A CE2   1 
ATOM   1392 C CZ    . PHE A 1 180 ? -0.39368  0.92587   1.22875   1.000 27.69143 ? 174  PHE A CZ    1 
ATOM   1393 N N     . SER A 1 181 ? -0.21388  1.25651   -6.12575  1.000 24.88157 ? 175  SER A N     1 
ATOM   1394 C CA    . SER A 1 181 ? -0.60142  1.82347   -7.41145  1.000 24.18401 ? 175  SER A CA    1 
ATOM   1395 C C     . SER A 1 181 ? -1.51620  0.86888   -8.16518  1.000 23.18232 ? 175  SER A C     1 
ATOM   1396 O O     . SER A 1 181 ? -1.28543  -0.34159  -8.18466  1.000 26.00589 ? 175  SER A O     1 
ATOM   1397 C CB    . SER A 1 181 ? 0.62443   2.11738   -8.26154  1.000 33.84526 ? 175  SER A CB    1 
ATOM   1398 O OG    . SER A 1 181 ? 1.37332   0.92652   -8.42336  1.000 42.63172 ? 175  SER A OG    1 
ATOM   1399 N N     . GLY A 1 182 ? -2.55020  1.42457   -8.79900  1.000 23.70953 ? 176  GLY A N     1 
ATOM   1400 C CA    . GLY A 1 182 ? -3.47818  0.63978   -9.59653  1.000 21.45969 ? 176  GLY A CA    1 
ATOM   1401 C C     . GLY A 1 182 ? -4.48878  -0.19001  -8.82306  1.000 21.02401 ? 176  GLY A C     1 
ATOM   1402 O O     . GLY A 1 182 ? -5.32410  -0.85410  -9.45773  1.000 21.38288 ? 176  GLY A O     1 
ATOM   1403 N N     . LYS A 1 183 ? -4.45815  -0.18947  -7.49042  1.000 21.08009 ? 177  LYS A N     1 
ATOM   1404 C CA    . LYS A 1 183 ? -5.32805  -1.07013  -6.70678  1.000 22.33912 ? 177  LYS A CA    1 
ATOM   1405 C C     . LYS A 1 183 ? -6.54708  -0.34120  -6.14112  1.000 20.64475 ? 177  LYS A C     1 
ATOM   1406 O O     . LYS A 1 183 ? -6.47281  0.84060   -5.79000  1.000 20.08806 ? 177  LYS A O     1 
ATOM   1407 C CB    . LYS A 1 183 ? -4.55822  -1.71369  -5.54706  1.000 20.08911 ? 177  LYS A CB    1 
ATOM   1408 C CG    . LYS A 1 183 ? -3.48808  -2.63951  -6.04149  1.000 22.19228 ? 177  LYS A CG    1 
ATOM   1409 C CD    . LYS A 1 183 ? -2.69018  -3.24839  -4.90528  1.000 21.01052 ? 177  LYS A CD    1 
ATOM   1410 C CE    . LYS A 1 183 ? -1.47364  -4.01099  -5.48467  1.000 21.27557 ? 177  LYS A CE    1 
ATOM   1411 N NZ    . LYS A 1 183 ? -0.71351  -4.64502  -4.35030  1.000 24.87370 ? 177  LYS A NZ    1 
ATOM   1412 N N     . ARG A 1 184 ? -7.67622  -1.06491  -6.09412  1.000 21.38918 ? 178  ARG A N     1 
ATOM   1413 C CA    . ARG A 1 184 ? -8.85029  -0.67903  -5.32281  1.000 19.27045 ? 178  ARG A CA    1 
ATOM   1414 C C     . ARG A 1 184 ? -8.65879  -1.14591  -3.87963  1.000 18.80776 ? 178  ARG A C     1 
ATOM   1415 O O     . ARG A 1 184 ? -8.52564  -2.35345  -3.61876  1.000 19.92410 ? 178  ARG A O     1 
ATOM   1416 C CB    . ARG A 1 184 ? -10.10641 -1.30630  -5.95927  1.000 19.45025 ? 178  ARG A CB    1 
ATOM   1417 C CG    . ARG A 1 184 ? -10.57673 -0.53445  -7.18373  1.000 23.13267 ? 178  ARG A CG    1 
ATOM   1418 C CD    . ARG A 1 184 ? -11.69549 -1.24894  -7.96006  1.000 21.60614 ? 178  ARG A CD    1 
ATOM   1419 N NE    . ARG A 1 184 ? -11.99435 -0.51599  -9.17913  1.000 29.81185 ? 178  ARG A NE    1 
ATOM   1420 C CZ    . ARG A 1 184 ? -12.64693 0.64147   -9.17773  1.000 38.59227 ? 178  ARG A CZ    1 
ATOM   1421 N NH1   . ARG A 1 184 ? -13.23099 1.10149   -8.07848  1.000 27.97056 ? 178  ARG A NH1   1 
ATOM   1422 N NH2   . ARG A 1 184 ? -12.73625 1.34218   -10.30699 1.000 49.11045 ? 178  ARG A NH2   1 
ATOM   1423 N N     . VAL A 1 185 ? -8.66154  -0.20529  -2.93031  1.000 20.07780 ? 179  VAL A N     1 
ATOM   1424 C CA    . VAL A 1 185 ? -8.32576  -0.50866  -1.54910  1.000 17.53466 ? 179  VAL A CA    1 
ATOM   1425 C C     . VAL A 1 185 ? -9.48653  -0.10884  -0.66203  1.000 16.69873 ? 179  VAL A C     1 
ATOM   1426 O O     . VAL A 1 185 ? -10.15833 0.89545   -0.93293  1.000 20.84070 ? 179  VAL A O     1 
ATOM   1427 C CB    . VAL A 1 185 ? -7.02910  0.23020   -1.14217  1.000 16.72723 ? 179  VAL A CB    1 
ATOM   1428 C CG1   . VAL A 1 185 ? -6.68116  -0.06309  0.31663   1.000 17.98488 ? 179  VAL A CG1   1 
ATOM   1429 C CG2   . VAL A 1 185 ? -5.85361  -0.17216  -2.09769  1.000 18.70776 ? 179  VAL A CG2   1 
ATOM   1430 N N     . GLY A 1 186 ? -9.73958  -0.90160  0.37593   1.000 20.03189 ? 180  GLY A N     1 
ATOM   1431 C CA    . GLY A 1 186 ? -10.72558 -0.56339  1.39079   1.000 19.87013 ? 180  GLY A CA    1 
ATOM   1432 C C     . GLY A 1 186 ? -10.03820 -0.49887  2.74158   1.000 21.49169 ? 180  GLY A C     1 
ATOM   1433 O O     . GLY A 1 186 ? -9.09454  -1.26045  3.01515   1.000 18.92963 ? 180  GLY A O     1 
ATOM   1434 N N     . VAL A 1 187 ? -10.51372 0.41800   3.59491   1.000 18.93593 ? 181  VAL A N     1 
ATOM   1435 C CA    . VAL A 1 187 ? -10.08291 0.51553   4.99028   1.000 16.93181 ? 181  VAL A CA    1 
ATOM   1436 C C     . VAL A 1 187 ? -11.31075 0.42103   5.86423   1.000 19.49653 ? 181  VAL A C     1 
ATOM   1437 O O     . VAL A 1 187 ? -12.24612 1.20384   5.68918   1.000 20.11383 ? 181  VAL A O     1 
ATOM   1438 C CB    . VAL A 1 187 ? -9.35103  1.82564   5.30961   1.000 18.60276 ? 181  VAL A CB    1 
ATOM   1439 C CG1   . VAL A 1 187 ? -8.99163  1.84863   6.81650   1.000 18.19061 ? 181  VAL A CG1   1 
ATOM   1440 C CG2   . VAL A 1 187 ? -8.12599  1.95201   4.47519   1.000 18.83180 ? 181  VAL A CG2   1 
ATOM   1441 N N     . ILE A 1 188 ? -11.31529 -0.53408  6.79197   1.000 20.41254 ? 182  ILE A N     1 
ATOM   1442 C CA    . ILE A 1 188 ? -12.35139 -0.60892  7.81713   1.000 20.15808 ? 182  ILE A CA    1 
ATOM   1443 C C     . ILE A 1 188 ? -11.75801 -0.04318  9.09751   1.000 21.79531 ? 182  ILE A C     1 
ATOM   1444 O O     . ILE A 1 188 ? -10.79162 -0.59670  9.62491   1.000 21.78280 ? 182  ILE A O     1 
ATOM   1445 C CB    . ILE A 1 188 ? -12.85165 -2.04351  8.04738   1.000 21.20022 ? 182  ILE A CB    1 
ATOM   1446 C CG1   . ILE A 1 188 ? -13.37991 -2.71570  6.76319   1.000 22.10772 ? 182  ILE A CG1   1 
ATOM   1447 C CG2   . ILE A 1 188 ? -13.95811 -2.03229  9.10224   1.000 21.47153 ? 182  ILE A CG2   1 
ATOM   1448 C CD1   . ILE A 1 188 ? -13.74078 -4.16982  7.00660   1.000 21.51903 ? 182  ILE A CD1   1 
ATOM   1449 N N     . GLY A 1 189 ? -12.32834 1.05248   9.59414   1.000 20.18266 ? 183  GLY A N     1 
ATOM   1450 C CA    . GLY A 1 189 ? -11.87404 1.62359   10.87353  1.000 20.35116 ? 183  GLY A CA    1 
ATOM   1451 C C     . GLY A 1 189 ? -11.38125 3.04348   10.65135  1.000 22.81315 ? 183  GLY A C     1 
ATOM   1452 O O     . GLY A 1 189 ? -10.63504 3.33649   9.72219   1.000 21.41327 ? 183  GLY A O     1 
ATOM   1453 N N     . THR A 1 190 ? -11.83485 3.95482   11.51215  1.000 23.39900 ? 184  THR A N     1 
ATOM   1454 C CA    . THR A 1 190 ? -11.49061 5.36350   11.37831  1.000 21.51394 ? 184  THR A CA    1 
ATOM   1455 C C     . THR A 1 190 ? -11.10713 5.93362   12.74491  1.000 20.57488 ? 184  THR A C     1 
ATOM   1456 O O     . THR A 1 190 ? -11.41190 7.07788   13.04577  1.000 22.79482 ? 184  THR A O     1 
ATOM   1457 C CB    . THR A 1 190 ? -12.63011 6.17004   10.73280  1.000 25.37918 ? 184  THR A CB    1 
ATOM   1458 O OG1   . THR A 1 190 ? -13.81423 6.11742   11.55158  1.000 28.28859 ? 184  THR A OG1   1 
ATOM   1459 C CG2   . THR A 1 190 ? -12.97380 5.67666   9.31116   1.000 22.41806 ? 184  THR A CG2   1 
ATOM   1460 N N     . GLY A 1 191 ? -10.48506 5.12174   13.59140  1.000 21.22773 ? 185  GLY A N     1 
ATOM   1461 C CA    . GLY A 1 191 ? -9.86213  5.61460   14.81022  1.000 22.76760 ? 185  GLY A CA    1 
ATOM   1462 C C     . GLY A 1 191 ? -8.49695  6.16630   14.45669  1.000 23.25918 ? 185  GLY A C     1 
ATOM   1463 O O     . GLY A 1 191 ? -8.18679  6.40270   13.28857  1.000 21.95765 ? 185  GLY A O     1 
ATOM   1464 N N     . SER A 1 192 ? -7.64879  6.32623   15.47937  1.000 21.90974 ? 186  SER A N     1 
ATOM   1465 C CA    . SER A 1 192 ? -6.34256  6.94605   15.25067  1.000 26.02910 ? 186  SER A CA    1 
ATOM   1466 C C     . SER A 1 192 ? -5.53166  6.20545   14.17960  1.000 22.60944 ? 186  SER A C     1 
ATOM   1467 O O     . SER A 1 192 ? -4.90315  6.83644   13.32050  1.000 21.32300 ? 186  SER A O     1 
ATOM   1468 C CB    . SER A 1 192 ? -5.57352  7.02344   16.57385  1.000 29.97526 ? 186  SER A CB    1 
ATOM   1469 O OG    . SER A 1 192 ? -5.47490  5.73696   17.14514  1.000 36.08999 ? 186  SER A OG    1 
ATOM   1470 N N     . THR A 1 193 ? -5.53166  4.86944   14.20398  1.000 20.89182 ? 187  THR A N     1 
ATOM   1471 C CA    . THR A 1 193 ? -4.78903  4.14056   13.17724  1.000 19.98951 ? 187  THR A CA    1 
ATOM   1472 C C     . THR A 1 193 ? -5.41636  4.31794   11.79314  1.000 20.72334 ? 187  THR A C     1 
ATOM   1473 O O     . THR A 1 193 ? -4.71578  4.58857   10.81778  1.000 18.37341 ? 187  THR A O     1 
ATOM   1474 C CB    . THR A 1 193 ? -4.69804  2.65523   13.52927  1.000 23.89168 ? 187  THR A CB    1 
ATOM   1475 O OG1   . THR A 1 193 ? -4.00120  2.50777   14.79493  1.000 24.71344 ? 187  THR A OG1   1 
ATOM   1476 C CG2   . THR A 1 193 ? -3.92569  1.93140   12.42838  1.000 22.13551 ? 187  THR A CG2   1 
ATOM   1477 N N     . GLY A 1 194 ? -6.73748  4.14398   11.67866  1.000 18.81755 ? 188  GLY A N     1 
ATOM   1478 C CA    . GLY A 1 194 ? -7.36689  4.28341   10.37214  1.000 17.90415 ? 188  GLY A CA    1 
ATOM   1479 C C     . GLY A 1 194 ? -7.14733  5.65631   9.77259   1.000 19.91578 ? 188  GLY A C     1 
ATOM   1480 O O     . GLY A 1 194 ? -6.86770  5.79506   8.57254   1.000 18.57606 ? 188  GLY A O     1 
ATOM   1481 N N     . VAL A 1 195 ? -7.26906  6.69611   10.59786  1.000 19.79407 ? 189  VAL A N     1 
ATOM   1482 C CA    . VAL A 1 195 ? -7.04839  8.04594   10.10043  1.000 19.98890 ? 189  VAL A CA    1 
ATOM   1483 C C     . VAL A 1 195 ? -5.62968  8.18123   9.55716   1.000 19.80645 ? 189  VAL A C     1 
ATOM   1484 O O     . VAL A 1 195 ? -5.42539  8.72516   8.46738   1.000 19.43419 ? 189  VAL A O     1 
ATOM   1485 C CB    . VAL A 1 195 ? -7.34475  9.06377   11.21079  1.000 23.22325 ? 189  VAL A CB    1 
ATOM   1486 C CG1   . VAL A 1 195 ? -6.63640  10.36537  10.95386  1.000 20.15400 ? 189  VAL A CG1   1 
ATOM   1487 C CG2   . VAL A 1 195 ? -8.86081  9.24023   11.36678  1.000 20.92623 ? 189  VAL A CG2   1 
ATOM   1488 N N     . GLN A 1 196 ? -4.63478  7.62520   10.25962  1.000 20.60817 ? 190  GLN A N     1 
ATOM   1489 C CA    . GLN A 1 196 ? -3.26020  7.73497   9.74614   1.000 19.12216 ? 190  GLN A CA    1 
ATOM   1490 C C     . GLN A 1 196 ? -3.07123  6.98272   8.43133   1.000 18.31511 ? 190  GLN A C     1 
ATOM   1491 O O     . GLN A 1 196 ? -2.42121  7.49046   7.50681   1.000 18.58563 ? 190  GLN A O     1 
ATOM   1492 C CB    . GLN A 1 196 ? -2.27050  7.23911   10.79915  1.000 20.54393 ? 190  GLN A CB    1 
ATOM   1493 C CG    . GLN A 1 196 ? -2.13242  8.21541   11.97831  1.000 21.19900 ? 190  GLN A CG    1 
ATOM   1494 C CD    . GLN A 1 196 ? -1.20434  7.73459   13.08049  1.000 25.80123 ? 190  GLN A CD    1 
ATOM   1495 O OE1   . GLN A 1 196 ? -0.79543  6.57350   13.13372  1.000 26.89552 ? 190  GLN A OE1   1 
ATOM   1496 N NE2   . GLN A 1 196 ? -0.81859  8.66664   13.94706  1.000 27.20445 ? 190  GLN A NE2   1 
ATOM   1497 N N     . VAL A 1 197 ? -3.62233  5.76310   8.32700   1.000 19.38730 ? 191  VAL A N     1 
ATOM   1498 C CA    . VAL A 1 197 ? -3.47066  4.97267   7.10708   1.000 17.78582 ? 191  VAL A CA    1 
ATOM   1499 C C     . VAL A 1 197 ? -4.17919  5.64723   5.94710   1.000 18.57178 ? 191  VAL A C     1 
ATOM   1500 O O     . VAL A 1 197 ? -3.61437  5.82133   4.86102   1.000 19.01591 ? 191  VAL A O     1 
ATOM   1501 C CB    . VAL A 1 197 ? -4.00476  3.54329   7.30331   1.000 15.69777 ? 191  VAL A CB    1 
ATOM   1502 C CG1   . VAL A 1 197 ? -3.97677  2.82515   5.96555   1.000 20.68702 ? 191  VAL A CG1   1 
ATOM   1503 C CG2   . VAL A 1 197 ? -3.13013  2.78685   8.26516   1.000 18.46376 ? 191  VAL A CG2   1 
ATOM   1504 N N     . ILE A 1 198 ? -5.43273  6.04259   6.16074   1.000 18.90980 ? 192  ILE A N     1 
ATOM   1505 C CA    . ILE A 1 198 ? -6.20727  6.63208   5.07674   1.000 18.77425 ? 192  ILE A CA    1 
ATOM   1506 C C     . ILE A 1 198 ? -5.50288  7.86962   4.53597   1.000 18.37625 ? 192  ILE A C     1 
ATOM   1507 O O     . ILE A 1 198 ? -5.39517  8.07869   3.31991   1.000 19.08335 ? 192  ILE A O     1 
ATOM   1508 C CB    . ILE A 1 198 ? -7.63626  6.93971   5.57608   1.000 18.18444 ? 192  ILE A CB    1 
ATOM   1509 C CG1   . ILE A 1 198 ? -8.42843  5.62709   5.78056   1.000 18.03973 ? 192  ILE A CG1   1 
ATOM   1510 C CG2   . ILE A 1 198 ? -8.37325  7.96088   4.67348   1.000 20.98845 ? 192  ILE A CG2   1 
ATOM   1511 C CD1   . ILE A 1 198 ? -9.64657  5.81125   6.73989   1.000 18.77766 ? 192  ILE A CD1   1 
ATOM   1512 N N     . THR A 1 199 ? -5.03758  8.72843   5.43848   1.000 19.99427 ? 193  THR A N     1 
ATOM   1513 C CA    . THR A 1 199 ? -4.40797  9.97323   5.01313   1.000 19.12775 ? 193  THR A CA    1 
ATOM   1514 C C     . THR A 1 199 ? -3.14764  9.68195   4.23257   1.000 20.22683 ? 193  THR A C     1 
ATOM   1515 O O     . THR A 1 199 ? -2.85229  10.36819  3.25005   1.000 21.34818 ? 193  THR A O     1 
ATOM   1516 C CB    . THR A 1 199 ? -4.08301  10.84235  6.23668   1.000 19.42872 ? 193  THR A CB    1 
ATOM   1517 O OG1   . THR A 1 199 ? -5.28482  11.10599  6.97416   1.000 21.74611 ? 193  THR A OG1   1 
ATOM   1518 C CG2   . THR A 1 199 ? -3.37958  12.16557  5.83126   1.000 20.75464 ? 193  THR A CG2   1 
ATOM   1519 N N     . ALA A 1 200 ? -2.40651  8.64641   4.64376   1.000 19.30803 ? 194  ALA A N     1 
ATOM   1520 C CA    . ALA A 1 200 ? -1.16360  8.28986   3.98821   1.000 18.68673 ? 194  ALA A CA    1 
ATOM   1521 C C     . ALA A 1 200 ? -1.36454  7.62105   2.62592   1.000 24.98385 ? 194  ALA A C     1 
ATOM   1522 O O     . ALA A 1 200 ? -0.53698  7.81575   1.73035   1.000 27.18145 ? 194  ALA A O     1 
ATOM   1523 C CB    . ALA A 1 200 ? -0.34829  7.36904   4.90502   1.000 21.98574 ? 194  ALA A CB    1 
ATOM   1524 N N     . ILE A 1 201 ? -2.41574  6.81892   2.42156   1.000 20.46496 ? 195  ILE A N     1 
ATOM   1525 C CA    . ILE A 1 201 ? -2.47904  6.01582   1.19905   1.000 19.94831 ? 195  ILE A CA    1 
ATOM   1526 C C     . ILE A 1 201 ? -3.43554  6.54776   0.13917   1.000 21.64995 ? 195  ILE A C     1 
ATOM   1527 O O     . ILE A 1 201 ? -3.32116  6.12955   -1.03036  1.000 20.72495 ? 195  ILE A O     1 
ATOM   1528 C CB    . ILE A 1 201 ? -2.78585  4.53396   1.50728   1.000 20.93376 ? 195  ILE A CB    1 
ATOM   1529 C CG1   . ILE A 1 201 ? -4.25855  4.31191   1.91814   1.000 19.82533 ? 195  ILE A CG1   1 
ATOM   1530 C CG2   . ILE A 1 201 ? -1.80552  4.00604   2.55555   1.000 22.69603 ? 195  ILE A CG2   1 
ATOM   1531 C CD1   . ILE A 1 201 ? -4.63741  2.78184   2.03576   1.000 18.37494 ? 195  ILE A CD1   1 
ATOM   1532 N N     . ALA A 1 202 ? -4.33094  7.49101   0.47060   1.000 19.43891 ? 196  ALA A N     1 
ATOM   1533 C CA    . ALA A 1 202 ? -5.37711  7.84083   -0.50055  1.000 22.69414 ? 196  ALA A CA    1 
ATOM   1534 C C     . ALA A 1 202 ? -4.78304  8.32013   -1.81993  1.000 20.89207 ? 196  ALA A C     1 
ATOM   1535 O O     . ALA A 1 202 ? -5.32446  8.03228   -2.88822  1.000 21.76609 ? 196  ALA A O     1 
ATOM   1536 C CB    . ALA A 1 202 ? -6.32095  8.91159   0.06350   1.000 21.00077 ? 196  ALA A CB    1 
ATOM   1537 N N     . SER A 1 203 ? -3.65599  9.04217   -1.77476  1.000 19.13744 ? 197  SER A N     1 
ATOM   1538 C CA    . SER A 1 203 ? -3.10015  9.56521   -3.02099  1.000 23.09623 ? 197  SER A CA    1 
ATOM   1539 C C     . SER A 1 203 ? -2.36685  8.51064   -3.83027  1.000 26.33908 ? 197  SER A C     1 
ATOM   1540 O O     . SER A 1 203 ? -1.99842  8.78298   -4.98360  1.000 27.89310 ? 197  SER A O     1 
ATOM   1541 C CB    . SER A 1 203 ? -2.12003  10.71236  -2.74719  1.000 26.85838 ? 197  SER A CB    1 
ATOM   1542 O OG    . SER A 1 203 ? -1.01803  10.23092  -1.99266  1.000 30.52552 ? 197  SER A OG    1 
ATOM   1543 N N     . GLN A 1 204 ? -2.14456  7.33466   -3.25446  1.000 22.63954 ? 198  GLN A N     1 
ATOM   1544 C CA    . GLN A 1 204 ? -1.35221  6.29159   -3.87682  1.000 24.79239 ? 198  GLN A CA    1 
ATOM   1545 C C     . GLN A 1 204 ? -2.19765  5.18793   -4.50718  1.000 28.49297 ? 198  GLN A C     1 
ATOM   1546 O O     . GLN A 1 204 ? -1.65970  4.39292   -5.29025  1.000 24.85685 ? 198  GLN A O     1 
ATOM   1547 C CB    . GLN A 1 204 ? -0.44174  5.64099   -2.84312  1.000 23.76172 ? 198  GLN A CB    1 
ATOM   1548 C CG    . GLN A 1 204 ? 0.51887   6.58616   -2.12268  1.000 27.25796 ? 198  GLN A CG    1 
ATOM   1549 C CD    . GLN A 1 204 ? 1.42941   5.82858   -1.15653  1.000 29.82756 ? 198  GLN A CD    1 
ATOM   1550 O OE1   . GLN A 1 204 ? 2.22858   4.98428   -1.57471  1.000 33.17778 ? 198  GLN A OE1   1 
ATOM   1551 N NE2   . GLN A 1 204 ? 1.28600   6.10290   0.14477   1.000 29.08233 ? 198  GLN A NE2   1 
ATOM   1552 N N     . VAL A 1 205 ? -3.48004  5.09721   -4.17271  1.000 21.25291 ? 199  VAL A N     1 
ATOM   1553 C CA    . VAL A 1 205 ? -4.32374  4.00604   -4.67464  1.000 21.21430 ? 199  VAL A CA    1 
ATOM   1554 C C     . VAL A 1 205 ? -5.11779  4.44944   -5.89770  1.000 22.46979 ? 199  VAL A C     1 
ATOM   1555 O O     . VAL A 1 205 ? -5.34056  5.63609   -6.14509  1.000 22.26950 ? 199  VAL A O     1 
ATOM   1556 C CB    . VAL A 1 205 ? -5.25449  3.45829   -3.56366  1.000 20.13877 ? 199  VAL A CB    1 
ATOM   1557 C CG1   . VAL A 1 205 ? -4.42308  2.95251   -2.39633  1.000 20.02971 ? 199  VAL A CG1   1 
ATOM   1558 C CG2   . VAL A 1 205 ? -6.26644  4.56959   -3.08930  1.000 21.88930 ? 199  VAL A CG2   1 
ATOM   1559 N N     . LYS A 1 206 ? -5.59315  3.46714   -6.67541  1.000 21.35765 ? 200  LYS A N     1 
ATOM   1560 C CA    . LYS A 1 206 ? -6.50869  3.80332   -7.75705  1.000 22.79867 ? 200  LYS A CA    1 
ATOM   1561 C C     . LYS A 1 206 ? -7.84665  4.27276   -7.20839  1.000 23.80107 ? 200  LYS A C     1 
ATOM   1562 O O     . LYS A 1 206 ? -8.44868  5.20904   -7.75048  1.000 21.28370 ? 200  LYS A O     1 
ATOM   1563 C CB    . LYS A 1 206 ? -6.71940  2.60616   -8.68833  1.000 21.07747 ? 200  LYS A CB    1 
ATOM   1564 C CG    . LYS A 1 206 ? -7.61420  2.92530   -9.86545  1.000 21.76273 ? 200  LYS A CG    1 
ATOM   1565 C CD    . LYS A 1 206 ? -7.55576  1.79726   -10.92337 1.000 25.56366 ? 200  LYS A CD    1 
ATOM   1566 C CE    . LYS A 1 206 ? -8.19791  0.53963   -10.38269 1.000 28.03517 ? 200  LYS A CE    1 
ATOM   1567 N NZ    . LYS A 1 206 ? -8.13213  -0.61610  -11.33971 1.000 35.98986 ? 200  LYS A NZ    1 
ATOM   1568 N N     . HIS A 1 207 ? -8.34930  3.61013   -6.16022  1.000 20.05104 ? 201  HIS A N     1 
ATOM   1569 C CA    . HIS A 1 207 ? -9.59252  4.04845   -5.52159  1.000 21.68125 ? 201  HIS A CA    1 
ATOM   1570 C C     . HIS A 1 207 ? -9.52965  3.61056   -4.06859  1.000 21.83044 ? 201  HIS A C     1 
ATOM   1571 O O     . HIS A 1 207 ? -8.96592  2.55207   -3.77628  1.000 20.38504 ? 201  HIS A O     1 
ATOM   1572 C CB    . HIS A 1 207 ? -10.84757 3.45645   -6.21437  1.000 22.39990 ? 201  HIS A CB    1 
ATOM   1573 C CG    . HIS A 1 207 ? -12.11909 4.09403   -5.74789  1.000 26.50579 ? 201  HIS A CG    1 
ATOM   1574 N ND1   . HIS A 1 207 ? -12.79436 3.65354   -4.63393  1.000 26.70652 ? 201  HIS A ND1   1 
ATOM   1575 C CD2   . HIS A 1 207 ? -12.78895 5.19050   -6.18840  1.000 25.92707 ? 201  HIS A CD2   1 
ATOM   1576 C CE1   . HIS A 1 207 ? -13.84087 4.43232   -4.41239  1.000 28.22326 ? 201  HIS A CE1   1 
ATOM   1577 N NE2   . HIS A 1 207 ? -13.85516 5.37882   -5.33135  1.000 26.49066 ? 201  HIS A NE2   1 
ATOM   1578 N N     . LEU A 1 208 ? -10.03230 4.45079   -3.15857  1.000 20.19830 ? 202  LEU A N     1 
ATOM   1579 C CA    . LEU A 1 208 ? -10.10390 4.11756   -1.73633  1.000 19.51281 ? 202  LEU A CA    1 
ATOM   1580 C C     . LEU A 1 208 ? -11.56256 4.16563   -1.29221  1.000 19.90620 ? 202  LEU A C     1 
ATOM   1581 O O     . LEU A 1 208 ? -12.24655 5.17328   -1.51074  1.000 21.03243 ? 202  LEU A O     1 
ATOM   1582 C CB    . LEU A 1 208 ? -9.26732  5.09737   -0.90553  1.000 16.85772 ? 202  LEU A CB    1 
ATOM   1583 C CG    . LEU A 1 208 ? -9.25232  4.85070   0.60183   1.000 18.85624 ? 202  LEU A CG    1 
ATOM   1584 C CD1   . LEU A 1 208 ? -8.53007  3.52696   0.90091   1.000 18.37389 ? 202  LEU A CD1   1 
ATOM   1585 C CD2   . LEU A 1 208 ? -8.55748  6.02361   1.33510   1.000 18.19476 ? 202  LEU A CD2   1 
ATOM   1586 N N     . THR A 1 209 ? -12.02792 3.10379   -0.65040  1.000 20.01330 ? 203  THR A N     1 
ATOM   1587 C CA    . THR A 1 209 ? -13.31209 3.11606   0.04658   1.000 18.65430 ? 203  THR A CA    1 
ATOM   1588 C C     . THR A 1 209 ? -13.03302 3.07268   1.52801   1.000 18.41097 ? 203  THR A C     1 
ATOM   1589 O O     . THR A 1 209 ? -12.31190 2.18439   2.00063   1.000 20.33859 ? 203  THR A O     1 
ATOM   1590 C CB    . THR A 1 209 ? -14.20390 1.92568   -0.32534  1.000 19.87804 ? 203  THR A CB    1 
ATOM   1591 O OG1   . THR A 1 209 ? -14.37965 1.90605   -1.74877  1.000 20.65067 ? 203  THR A OG1   1 
ATOM   1592 C CG2   . THR A 1 209 ? -15.55979 2.09877   0.34558   1.000 21.32392 ? 203  THR A CG2   1 
ATOM   1593 N N     . VAL A 1 210 ? -13.59491 4.02726   2.24983   1.000 18.01248 ? 204  VAL A N     1 
ATOM   1594 C CA    . VAL A 1 210 ? -13.47396 4.06575   3.70011   1.000 19.58836 ? 204  VAL A CA    1 
ATOM   1595 C C     . VAL A 1 210 ? -14.77970 3.56844   4.29682   1.000 20.96068 ? 204  VAL A C     1 
ATOM   1596 O O     . VAL A 1 210 ? -15.85359 4.11986   4.00912   1.000 21.75352 ? 204  VAL A O     1 
ATOM   1597 C CB    . VAL A 1 210 ? -13.14326 5.48166   4.17824   1.000 17.92855 ? 204  VAL A CB    1 
ATOM   1598 C CG1   . VAL A 1 210 ? -13.18123 5.52596   5.72007   1.000 18.72545 ? 204  VAL A CG1   1 
ATOM   1599 C CG2   . VAL A 1 210 ? -11.79444 5.90913   3.62990   1.000 18.51152 ? 204  VAL A CG2   1 
ATOM   1600 N N     . PHE A 1 211 ? -14.69253 2.51894   5.11703   1.000 22.26822 ? 205  PHE A N     1 
ATOM   1601 C CA    . PHE A 1 211 ? -15.85681 1.92931   5.78275   1.000 21.53063 ? 205  PHE A CA    1 
ATOM   1602 C C     . PHE A 1 211 ? -15.92125 2.43474   7.21766   1.000 20.01758 ? 205  PHE A C     1 
ATOM   1603 O O     . PHE A 1 211 ? -15.26831 1.90019   8.10996   1.000 22.67376 ? 205  PHE A O     1 
ATOM   1604 C CB    . PHE A 1 211 ? -15.81337 0.40626   5.71152   1.000 21.97484 ? 205  PHE A CB    1 
ATOM   1605 C CG    . PHE A 1 211 ? -15.81449 -0.14118  4.28164   1.000 22.52116 ? 205  PHE A CG    1 
ATOM   1606 C CD1   . PHE A 1 211 ? -17.00509 -0.22765  3.57428   1.000 23.16246 ? 205  PHE A CD1   1 
ATOM   1607 C CD2   . PHE A 1 211 ? -14.65360 -0.58153  3.67832   1.000 18.99412 ? 205  PHE A CD2   1 
ATOM   1608 C CE1   . PHE A 1 211 ? -17.03107 -0.73476  2.28051   1.000 19.66837 ? 205  PHE A CE1   1 
ATOM   1609 C CE2   . PHE A 1 211 ? -14.67748 -1.10145  2.33247   1.000 20.08856 ? 205  PHE A CE2   1 
ATOM   1610 C CZ    . PHE A 1 211 ? -15.86337 -1.17845  1.66740   1.000 23.30757 ? 205  PHE A CZ    1 
ATOM   1611 N N     . GLN A 1 212 ? -16.73600 3.44472   7.44441   1.000 19.88553 ? 206  GLN A N     1 
ATOM   1612 C CA    . GLN A 1 212 ? -16.75950 4.17265   8.70779   1.000 18.81301 ? 206  GLN A CA    1 
ATOM   1613 C C     . GLN A 1 212 ? -17.98081 3.75470   9.51515   1.000 22.70404 ? 206  GLN A C     1 
ATOM   1614 O O     . GLN A 1 212 ? -19.11200 4.04732   9.11226   1.000 23.69339 ? 206  GLN A O     1 
ATOM   1615 C CB    . GLN A 1 212 ? -16.78475 5.67317   8.42553   1.000 21.42997 ? 206  GLN A CB    1 
ATOM   1616 C CG    . GLN A 1 212 ? -17.04386 6.56164   9.68464   1.000 23.90092 ? 206  GLN A CG    1 
ATOM   1617 C CD    . GLN A 1 212 ? -17.48301 7.94380   9.27691   1.000 25.47187 ? 206  GLN A CD    1 
ATOM   1618 O OE1   . GLN A 1 212 ? -16.64427 8.78700   8.99934   1.000 25.86361 ? 206  GLN A OE1   1 
ATOM   1619 N NE2   . GLN A 1 212 ? -18.81269 8.18038   9.19528   1.000 24.15478 ? 206  GLN A NE2   1 
ATOM   1620 N N     . ARG A 1 213 ? -17.76010 3.10696   10.66304  1.000 22.54805 ? 207  ARG A N     1 
ATOM   1621 C CA    . ARG A 1 213 ? -18.88748 2.79274   11.54487  1.000 26.73548 ? 207  ARG A CA    1 
ATOM   1622 C C     . ARG A 1 213 ? -19.26748 3.96289   12.45152  1.000 31.74422 ? 207  ARG A C     1 
ATOM   1623 O O     . ARG A 1 213 ? -20.46119 4.19883   12.67299  1.000 28.83025 ? 207  ARG A O     1 
ATOM   1624 C CB    . ARG A 1 213 ? -18.59347 1.55314   12.39531  1.000 26.15711 ? 207  ARG A CB    1 
ATOM   1625 C CG    . ARG A 1 213 ? -19.86144 0.99325   13.09874  1.000 28.36445 ? 207  ARG A CG    1 
ATOM   1626 C CD    . ARG A 1 213 ? -19.65355 -0.41951  13.66041  1.000 29.83934 ? 207  ARG A CD    1 
ATOM   1627 N NE    . ARG A 1 213 ? -18.61125 -0.45799  14.68628  1.000 29.58290 ? 207  ARG A NE    1 
ATOM   1628 C CZ    . ARG A 1 213 ? -18.19066 -1.55672  15.29971  1.000 31.10816 ? 207  ARG A CZ    1 
ATOM   1629 N NH1   . ARG A 1 213 ? -18.69273 -2.75115  15.01117  1.000 34.98462 ? 207  ARG A NH1   1 
ATOM   1630 N NH2   . ARG A 1 213 ? -17.24757 -1.45633  16.22800  1.000 28.94227 ? 207  ARG A NH2   1 
ATOM   1631 N N     . SER A 1 214 ? -18.28776 4.73125   12.95607  1.000 26.22946 ? 208  SER A N     1 
ATOM   1632 C CA    . SER A 1 214 ? -18.54651 5.88318   13.81939  1.000 25.39280 ? 208  SER A CA    1 
ATOM   1633 C C     . SER A 1 214 ? -17.55423 6.99303   13.49111  1.000 24.23927 ? 208  SER A C     1 
ATOM   1634 O O     . SER A 1 214 ? -16.34694 6.80948   13.67629  1.000 25.89413 ? 208  SER A O     1 
ATOM   1635 C CB    . SER A 1 214 ? -18.41968 5.52488   15.31313  1.000 25.93093 ? 208  SER A CB    1 
ATOM   1636 O OG    . SER A 1 214 ? -19.11918 4.32854   15.67631  1.000 33.90592 ? 208  SER A OG    1 
ATOM   1637 N N     . ALA A 1 215 ? -18.05768 8.14112   13.05504  1.000 23.68952 ? 209  ALA A N     1 
ATOM   1638 C CA    . ALA A 1 215 ? -17.19434 9.29321   12.79126  1.000 23.73360 ? 209  ALA A CA    1 
ATOM   1639 C C     . ALA A 1 215 ? -16.61343 9.85920   14.08729  1.000 27.71019 ? 209  ALA A C     1 
ATOM   1640 O O     . ALA A 1 215 ? -17.32054 10.00102  15.08808  1.000 24.96156 ? 209  ALA A O     1 
ATOM   1641 C CB    . ALA A 1 215 ? -17.99539 10.37281  12.05220  1.000 25.92798 ? 209  ALA A CB    1 
ATOM   1642 N N     . GLN A 1 216 ? -15.31000 10.18607  14.08333  1.000 20.95612 ? 210  GLN A N     1 
ATOM   1643 C CA    . GLN A 1 216 ? -14.69588 10.76236  15.27412  1.000 22.87012 ? 210  GLN A CA    1 
ATOM   1644 C C     . GLN A 1 216 ? -14.18252 12.14833  14.92556  1.000 22.26139 ? 210  GLN A C     1 
ATOM   1645 O O     . GLN A 1 216 ? -14.05219 12.49888  13.75619  1.000 23.48688 ? 210  GLN A O     1 
ATOM   1646 C CB    . GLN A 1 216 ? -13.54957 9.87365   15.79791  1.000 28.88054 ? 210  GLN A CB    1 
ATOM   1647 C CG    . GLN A 1 216 ? -14.03254 8.50912   16.29948  1.000 28.47835 ? 210  GLN A CG    1 
ATOM   1648 C CD    . GLN A 1 216 ? -12.99140 7.82058   17.07760  1.000 35.71344 ? 210  GLN A CD    1 
ATOM   1649 O OE1   . GLN A 1 216 ? -12.31125 8.44701   17.90361  1.000 35.57629 ? 210  GLN A OE1   1 
ATOM   1650 N NE2   . GLN A 1 216 ? -12.81614 6.51772   16.82423  1.000 28.18876 ? 210  GLN A NE2   1 
ATOM   1651 N N     . TYR A 1 217 ? -13.94835 12.96024  15.96007  1.000 24.57025 ? 211  TYR A N     1 
ATOM   1652 C CA    . TYR A 1 217 ? -13.36227 14.27916  15.78179  1.000 25.05677 ? 211  TYR A CA    1 
ATOM   1653 C C     . TYR A 1 217 ? -11.86197 14.10738  15.57734  1.000 22.08108 ? 211  TYR A C     1 
ATOM   1654 O O     . TYR A 1 217 ? -11.23306 13.33421  16.28790  1.000 25.94292 ? 211  TYR A O     1 
ATOM   1655 C CB    . TYR A 1 217 ? -13.59666 15.12478  17.03555  1.000 26.06668 ? 211  TYR A CB    1 
ATOM   1656 C CG    . TYR A 1 217 ? -15.05624 15.42901  17.33652  1.000 27.75939 ? 211  TYR A CG    1 
ATOM   1657 C CD1   . TYR A 1 217 ? -15.75900 16.37388  16.61189  1.000 28.06638 ? 211  TYR A CD1   1 
ATOM   1658 C CD2   . TYR A 1 217 ? -15.72362 14.70194  18.31260  1.000 33.22030 ? 211  TYR A CD2   1 
ATOM   1659 C CE1   . TYR A 1 217 ? -17.11180 16.63544  16.91213  1.000 35.84919 ? 211  TYR A CE1   1 
ATOM   1660 C CE2   . TYR A 1 217 ? -17.05619 14.94838  18.61734  1.000 39.14122 ? 211  TYR A CE2   1 
ATOM   1661 C CZ    . TYR A 1 217 ? -17.74868 15.90167  17.91570  1.000 35.48020 ? 211  TYR A CZ    1 
ATOM   1662 O OH    . TYR A 1 217 ? -19.07776 16.10524  18.24043  1.000 37.89794 ? 211  TYR A OH    1 
ATOM   1663 N N     . SER A 1 218 ? -11.29668 14.85289  14.63533  1.000 24.73325 ? 212  SER A N     1 
ATOM   1664 C CA    . SER A 1 218 ? -9.85435  14.90842  14.45923  1.000 23.23553 ? 212  SER A CA    1 
ATOM   1665 C C     . SER A 1 218 ? -9.40876  16.34456  14.24364  1.000 24.38652 ? 212  SER A C     1 
ATOM   1666 O O     . SER A 1 218 ? -10.08364 17.11021  13.54804  1.000 21.67322 ? 212  SER A O     1 
ATOM   1667 C CB    . SER A 1 218 ? -9.38468  14.07104  13.26231  1.000 23.22892 ? 212  SER A CB    1 
ATOM   1668 O OG    . SER A 1 218 ? -7.97694  13.93736  13.30299  1.000 25.55951 ? 212  SER A OG    1 
ATOM   1669 N N     . VAL A 1 219 ? -8.25559  16.68756  14.81177  1.000 22.16457 ? 213  VAL A N     1 
ATOM   1670 C CA    . VAL A 1 219 ? -7.66491  18.01981  14.67849  1.000 19.25619 ? 213  VAL A CA    1 
ATOM   1671 C C     . VAL A 1 219 ? -6.31348  17.86805  13.97987  1.000 25.32194 ? 213  VAL A C     1 
ATOM   1672 O O     . VAL A 1 219 ? -5.74267  16.77091  13.95137  1.000 21.17568 ? 213  VAL A O     1 
ATOM   1673 C CB    . VAL A 1 219 ? -7.53084  18.71566  16.05239  1.000 23.36677 ? 213  VAL A CB    1 
ATOM   1674 C CG1   . VAL A 1 219 ? -8.89807  18.73584  16.74418  1.000 24.99633 ? 213  VAL A CG1   1 
ATOM   1675 C CG2   . VAL A 1 219 ? -6.49451  17.97509  16.95569  1.000 24.96774 ? 213  VAL A CG2   1 
ATOM   1676 N N     . PRO A 1 220 ? -5.77778  18.94485  13.38738  1.000 23.18050 ? 214  PRO A N     1 
ATOM   1677 C CA    . PRO A 1 220 ? -4.44813  18.84877  12.76183  1.000 21.22045 ? 214  PRO A CA    1 
ATOM   1678 C C     . PRO A 1 220 ? -3.38376  18.48590  13.78980  1.000 23.01768 ? 214  PRO A C     1 
ATOM   1679 O O     . PRO A 1 220 ? -3.40907  18.93386  14.94251  1.000 24.17866 ? 214  PRO A O     1 
ATOM   1680 C CB    . PRO A 1 220 ? -4.21423  20.25262  12.18077  1.000 23.16604 ? 214  PRO A CB    1 
ATOM   1681 C CG    . PRO A 1 220 ? -5.59273  20.88489  12.10482  1.000 23.76040 ? 214  PRO A CG    1 
ATOM   1682 C CD    . PRO A 1 220 ? -6.35680  20.29148  13.25436  1.000 19.87028 ? 214  PRO A CD    1 
ATOM   1683 N N     . ILE A 1 221 ? -2.43924  17.63753  13.36904  1.000 22.29463 ? 215  ILE A N     1 
ATOM   1684 C CA    . ILE A 1 221 ? -1.27157  17.40546  14.21521  1.000 22.74145 ? 215  ILE A CA    1 
ATOM   1685 C C     . ILE A 1 221 ? -0.18386  18.46263  13.98306  1.000 23.48710 ? 215  ILE A C     1 
ATOM   1686 O O     . ILE A 1 221 ? 0.61118   18.71229  14.89345  1.000 22.10708 ? 215  ILE A O     1 
ATOM   1687 C CB    . ILE A 1 221 ? -0.71318  15.98098  14.04450  1.000 22.23096 ? 215  ILE A CB    1 
ATOM   1688 C CG1   . ILE A 1 221 ? 0.25128   15.64381  15.20988  1.000 26.21250 ? 215  ILE A CG1   1 
ATOM   1689 C CG2   . ILE A 1 221 ? -0.07771  15.83290  12.66318  1.000 16.64625 ? 215  ILE A CG2   1 
ATOM   1690 C CD1   . ILE A 1 221 ? 0.76226   14.18513  15.21209  1.000 34.25426 ? 215  ILE A CD1   1 
ATOM   1691 N N     . GLY A 1 222 ? -0.14395  19.11364  12.80814  1.000 22.45926 ? 216  GLY A N     1 
ATOM   1692 C CA    . GLY A 1 222 ? 0.85292   20.16473  12.53041  1.000 20.62769 ? 216  GLY A CA    1 
ATOM   1693 C C     . GLY A 1 222 ? 2.30818   19.67791  12.50021  1.000 23.48201 ? 216  GLY A C     1 
ATOM   1694 O O     . GLY A 1 222 ? 3.19876   20.32369  13.07398  1.000 24.23181 ? 216  GLY A O     1 
ATOM   1695 N N     . ASN A 1 223 ? 2.56153   18.54071  11.85393  1.000 20.81788 ? 217  ASN A N     1 
ATOM   1696 C CA    . ASN A 1 223 ? 3.88980   17.91749  11.81988  1.000 23.21627 ? 217  ASN A CA    1 
ATOM   1697 C C     . ASN A 1 223 ? 4.74391   18.63709  10.78065  1.000 28.50770 ? 217  ASN A C     1 
ATOM   1698 O O     . ASN A 1 223 ? 4.48659   18.52869  9.57985   1.000 34.11290 ? 217  ASN A O     1 
ATOM   1699 C CB    . ASN A 1 223 ? 3.78532   16.42563  11.49843  1.000 20.38398 ? 217  ASN A CB    1 
ATOM   1700 C CG    . ASN A 1 223 ? 5.07867   15.69812  11.72574  1.000 19.83106 ? 217  ASN A CG    1 
ATOM   1701 O OD1   . ASN A 1 223 ? 5.93194   16.16635  12.48564  1.000 19.10469 ? 217  ASN A OD1   1 
ATOM   1702 N ND2   . ASN A 1 223 ? 5.23054   14.54810  11.09278  1.000 21.98867 ? 217  ASN A ND2   1 
ATOM   1703 N N     . VAL A 1 224 ? 5.75443   19.38353  11.23052  1.000 20.06946 ? 218  VAL A N     1 
ATOM   1704 C CA    . VAL A 1 224 ? 6.59535   20.16599  10.33433  1.000 21.25042 ? 218  VAL A CA    1 
ATOM   1705 C C     . VAL A 1 224 ? 8.04769   19.79632  10.60454  1.000 21.33227 ? 218  VAL A C     1 
ATOM   1706 O O     . VAL A 1 224 ? 8.38299   19.31208  11.68157  1.000 21.29808 ? 218  VAL A O     1 
ATOM   1707 C CB    . VAL A 1 224 ? 6.39790   21.68843  10.53350  1.000 20.92586 ? 218  VAL A CB    1 
ATOM   1708 C CG1   . VAL A 1 224 ? 5.05248   22.14110  9.97571   1.000 23.96023 ? 218  VAL A CG1   1 
ATOM   1709 C CG2   . VAL A 1 224 ? 6.47494   22.04412  11.98315  1.000 22.91095 ? 218  VAL A CG2   1 
ATOM   1710 N N     . VAL A 1 225 ? 8.92273   20.08246  9.63417   1.000 23.53917 ? 219  VAL A N     1 
ATOM   1711 C CA    . VAL A 1 225 ? 10.36059  19.87304  9.86728   1.000 22.37902 ? 219  VAL A CA    1 
ATOM   1712 C C     . VAL A 1 225 ? 10.82028  20.82783  10.95284  1.000 19.82154 ? 219  VAL A C     1 
ATOM   1713 O O     . VAL A 1 225 ? 10.28241  21.93792  11.10020  1.000 21.45865 ? 219  VAL A O     1 
ATOM   1714 C CB    . VAL A 1 225 ? 11.19481  20.07893  8.58600   1.000 23.71522 ? 219  VAL A CB    1 
ATOM   1715 C CG1   . VAL A 1 225 ? 10.88078  19.01707  7.56107   1.000 25.12374 ? 219  VAL A CG1   1 
ATOM   1716 C CG2   . VAL A 1 225 ? 10.95347  21.49493  7.97259   1.000 21.87347 ? 219  VAL A CG2   1 
ATOM   1717 N N     . MET A 1 226 ? 11.87474  20.42757  11.67715  1.000 21.11074 ? 220  MET A N     1 
ATOM   1718 C CA    . MET A 1 226 ? 12.44435  21.20774  12.77058  1.000 23.77712 ? 220  MET A CA    1 
ATOM   1719 C C     . MET A 1 226 ? 13.77984  21.80818  12.32377  1.000 24.82137 ? 220  MET A C     1 
ATOM   1720 O O     . MET A 1 226 ? 14.69781  21.07968  11.92960  1.000 22.40297 ? 220  MET A O     1 
ATOM   1721 C CB    . MET A 1 226 ? 12.62356  20.32863  14.01680  1.000 23.01162 ? 220  MET A CB    1 
ATOM   1722 C CG    . MET A 1 226 ? 11.28449  19.81598  14.54606  1.000 21.34317 ? 220  MET A CG    1 
ATOM   1723 S SD    . MET A 1 226 ? 10.25218  21.05133  15.41199  1.000 26.91601 ? 220  MET A SD    1 
ATOM   1724 C CE    . MET A 1 226 ? 11.15576  21.25695  16.97625  1.000 31.03064 ? 220  MET A CE    1 
ATOM   1725 N N     . SER A 1 227 ? 13.88580  23.13158  12.37946  1.000 25.31957 ? 221  SER A N     1 
ATOM   1726 C CA    . SER A 1 227 ? 15.13194  23.77679  11.98528  1.000 28.73514 ? 221  SER A CA    1 
ATOM   1727 C C     . SER A 1 227 ? 16.21811  23.50220  13.02329  1.000 30.75999 ? 221  SER A C     1 
ATOM   1728 O O     . SER A 1 227 ? 15.94028  23.14575  14.17574  1.000 29.38656 ? 221  SER A O     1 
ATOM   1729 C CB    . SER A 1 227 ? 14.90986  25.28640  11.81949  1.000 28.73370 ? 221  SER A CB    1 
ATOM   1730 O OG    . SER A 1 227 ? 14.75258  25.88154  13.10372  1.000 29.72874 ? 221  SER A OG    1 
ATOM   1731 N N     . GLU A 1 228 ? 17.47937  23.65341  12.61030  1.000 33.68211 ? 222  GLU A N     1 
ATOM   1732 C CA    . GLU A 1 228 ? 18.55245  23.46411  13.58791  1.000 37.47408 ? 222  GLU A CA    1 
ATOM   1733 C C     . GLU A 1 228 ? 18.42524  24.43031  14.75808  1.000 32.33539 ? 222  GLU A C     1 
ATOM   1734 O O     . GLU A 1 228 ? 18.74569  24.06325  15.89386  1.000 37.22694 ? 222  GLU A O     1 
ATOM   1735 C CB    . GLU A 1 228 ? 19.91845  23.57627  12.91872  1.000 42.06635 ? 222  GLU A CB    1 
ATOM   1736 C CG    . GLU A 1 228 ? 20.28300  22.32047  12.13626  1.000 40.75178 ? 222  GLU A CG    1 
ATOM   1737 C CD    . GLU A 1 228 ? 21.51557  22.50557  11.26799  1.000 64.82435 ? 222  GLU A CD    1 
ATOM   1738 O OE1   . GLU A 1 228 ? 21.36579  22.60459  10.02992  1.000 68.24250 ? 222  GLU A OE1   1 
ATOM   1739 O OE2   . GLU A 1 228 ? 22.63654  22.56928  11.82654  1.000 71.76055 ? 222  GLU A OE2   1 
ATOM   1740 N N     . THR A 1 229 ? 17.89752  25.63225  14.51102  1.000 34.15408 ? 223  THR A N     1 
ATOM   1741 C CA    . THR A 1 229 ? 17.58086  26.59148  15.57393  1.000 37.93940 ? 223  THR A CA    1 
ATOM   1742 C C     . THR A 1 229 ? 16.47643  26.08418  16.50025  1.000 35.87152 ? 223  THR A C     1 
ATOM   1743 O O     . THR A 1 229 ? 16.59899  26.17221  17.72628  1.000 44.62474 ? 223  THR A O     1 
ATOM   1744 C CB    . THR A 1 229 ? 17.14186  27.91733  14.94585  1.000 44.28595 ? 223  THR A CB    1 
ATOM   1745 O OG1   . THR A 1 229 ? 18.26792  28.56282  14.35903  1.000 45.04813 ? 223  THR A OG1   1 
ATOM   1746 C CG2   . THR A 1 229 ? 16.49850  28.84102  15.98773  1.000 41.47468 ? 223  THR A CG2   1 
ATOM   1747 N N     . ASP A 1 230 ? 15.34620  25.64659  15.92830  1.000 36.88505 ? 224  ASP A N     1 
ATOM   1748 C CA    . ASP A 1 230 ? 14.30242  24.98841  16.71098  1.000 32.82532 ? 224  ASP A CA    1 
ATOM   1749 C C     . ASP A 1 230 ? 14.92094  23.94945  17.65515  1.000 33.78636 ? 224  ASP A C     1 
ATOM   1750 O O     . ASP A 1 230 ? 14.64582  23.93600  18.86377  1.000 34.34387 ? 224  ASP A O     1 
ATOM   1751 C CB    . ASP A 1 230 ? 13.27414  24.32374  15.76507  1.000 30.77618 ? 224  ASP A CB    1 
ATOM   1752 C CG    . ASP A 1 230 ? 12.35610  25.33584  15.00239  1.000 45.28388 ? 224  ASP A CG    1 
ATOM   1753 O OD1   . ASP A 1 230 ? 11.77052  24.93289  13.95697  1.000 36.15853 ? 224  ASP A OD1   1 
ATOM   1754 O OD2   . ASP A 1 230 ? 12.15527  26.47879  15.47212  1.000 36.13753 ? 224  ASP A OD2   1 
ATOM   1755 N N     . VAL A 1 231 ? 15.79891  23.09923  17.11612  1.000 28.15180 ? 225  VAL A N     1 
ATOM   1756 C CA    . VAL A 1 231 ? 16.33546  21.96672  17.87143  1.000 27.45543 ? 225  VAL A CA    1 
ATOM   1757 C C     . VAL A 1 231 ? 17.31955  22.45008  18.92606  1.000 36.72275 ? 225  VAL A C     1 
ATOM   1758 O O     . VAL A 1 231 ? 17.32410  21.96574  20.06211  1.000 32.44240 ? 225  VAL A O     1 
ATOM   1759 C CB    . VAL A 1 231 ? 16.98495  20.96515  16.90241  1.000 26.86761 ? 225  VAL A CB    1 
ATOM   1760 C CG1   . VAL A 1 231 ? 17.78619  19.88288  17.65411  1.000 24.49460 ? 225  VAL A CG1   1 
ATOM   1761 C CG2   . VAL A 1 231 ? 15.90195  20.36092  15.96059  1.000 24.89115 ? 225  VAL A CG2   1 
ATOM   1762 N N     . ALA A 1 232 ? 18.16294  23.41875  18.56582  1.000 30.02185 ? 226  ALA A N     1 
ATOM   1763 C CA    . ALA A 1 232 ? 19.09915  23.97479  19.53533  1.000 36.41925 ? 226  ALA A CA    1 
ATOM   1764 C C     . ALA A 1 232 ? 18.36736  24.62982  20.69749  1.000 33.08093 ? 226  ALA A C     1 
ATOM   1765 O O     . ALA A 1 232 ? 18.78215  24.48709  21.84982  1.000 40.29880 ? 226  ALA A O     1 
ATOM   1766 C CB    . ALA A 1 232 ? 20.02876  24.98016  18.85123  1.000 38.86309 ? 226  ALA A CB    1 
ATOM   1767 N N     . LYS A 1 233 ? 17.26114  25.32439  20.43516  1.000 39.05640 ? 227  LYS A N     1 
ATOM   1768 C CA    . LYS A 1 233 ? 16.55529  25.96155  21.54640  1.000 40.00491 ? 227  LYS A CA    1 
ATOM   1769 C C     . LYS A 1 233 ? 16.03926  24.92105  22.53474  1.000 40.06226 ? 227  LYS A C     1 
ATOM   1770 O O     . LYS A 1 233 ? 16.13826  25.10187  23.76076  1.000 37.43566 ? 227  LYS A O     1 
ATOM   1771 C CB    . LYS A 1 233 ? 15.41137  26.82856  21.03657  1.000 39.64375 ? 227  LYS A CB    1 
ATOM   1772 C CG    . LYS A 1 233 ? 15.87347  28.03756  20.19659  1.000 52.96342 ? 227  LYS A CG    1 
ATOM   1773 C CD    . LYS A 1 233 ? 14.77695  29.10758  20.09317  1.000 67.22965 ? 227  LYS A CD    1 
ATOM   1774 C CE    . LYS A 1 233 ? 13.85459  28.85739  18.89023  1.000 66.63651 ? 227  LYS A CE    1 
ATOM   1775 N NZ    . LYS A 1 233 ? 12.95306  30.00315  18.53673  1.000 63.47073 ? 227  LYS A NZ    1 
ATOM   1776 N N     . ILE A 1 234 ? 15.50119  23.81795  22.01021  1.000 30.14075 ? 228  ILE A N     1 
ATOM   1777 C CA    . ILE A 1 234 ? 14.99716  22.73880  22.84908  1.000 24.86794 ? 228  ILE A CA    1 
ATOM   1778 C C     . ILE A 1 234 ? 16.12522  22.16413  23.69456  1.000 25.98217 ? 228  ILE A C     1 
ATOM   1779 O O     . ILE A 1 234 ? 16.02542  22.07083  24.92537  1.000 26.73596 ? 228  ILE A O     1 
ATOM   1780 C CB    . ILE A 1 234 ? 14.34676  21.65837  21.96737  1.000 21.18245 ? 228  ILE A CB    1 
ATOM   1781 C CG1   . ILE A 1 234 ? 12.94908  22.09595  21.50826  1.000 27.92161 ? 228  ILE A CG1   1 
ATOM   1782 C CG2   . ILE A 1 234 ? 14.25232  20.34010  22.72203  1.000 23.11117 ? 228  ILE A CG2   1 
ATOM   1783 C CD1   . ILE A 1 234 ? 12.38374  21.18462  20.41381  1.000 29.93260 ? 228  ILE A CD1   1 
ATOM   1784 N N     . LYS A 1 235 ? 17.23052  21.81203  23.04508  1.000 21.13080 ? 229  LYS A N     1 
ATOM   1785 C CA    . LYS A 1 235 ? 18.31323  21.12143  23.73344  1.000 27.46025 ? 229  LYS A CA    1 
ATOM   1786 C C     . LYS A 1 235 ? 18.98775  22.01961  24.76265  1.000 31.56067 ? 229  LYS A C     1 
ATOM   1787 O O     . LYS A 1 235 ? 19.39411  21.53314  25.82557  1.000 29.49851 ? 229  LYS A O     1 
ATOM   1788 C CB    . LYS A 1 235 ? 19.33600  20.61282  22.71742  1.000 26.35953 ? 229  LYS A CB    1 
ATOM   1789 C CG    . LYS A 1 235 ? 18.86500  19.34654  21.97364  1.000 27.66646 ? 229  LYS A CG    1 
ATOM   1790 C CD    . LYS A 1 235 ? 19.83417  18.85685  20.93868  1.000 26.88487 ? 229  LYS A CD    1 
ATOM   1791 C CE    . LYS A 1 235 ? 19.34509  17.52125  20.36010  1.000 27.95072 ? 229  LYS A CE    1 
ATOM   1792 N NZ    . LYS A 1 235 ? 20.23994  17.03054  19.28931  1.000 30.60174 ? 229  LYS A NZ    1 
ATOM   1793 N N     . GLU A 1 236 ? 19.08663  23.32428  24.48667  1.000 29.92594 ? 230  GLU A N     1 
ATOM   1794 C CA    . GLU A 1 236 ? 19.67431  24.21286  25.49645  1.000 33.95719 ? 230  GLU A CA    1 
ATOM   1795 C C     . GLU A 1 236 ? 18.76805  24.40440  26.69295  1.000 35.13456 ? 230  GLU A C     1 
ATOM   1796 O O     . GLU A 1 236 ? 19.24817  24.82412  27.75321  1.000 35.51489 ? 230  GLU A O     1 
ATOM   1797 C CB    . GLU A 1 236 ? 20.02390  25.58955  24.91025  1.000 37.66383 ? 230  GLU A CB    1 
ATOM   1798 C CG    . GLU A 1 236 ? 20.73651  25.51627  23.60437  1.000 47.28453 ? 230  GLU A CG    1 
ATOM   1799 C CD    . GLU A 1 236 ? 21.25565  26.85353  23.11483  1.000 63.63903 ? 230  GLU A CD    1 
ATOM   1800 O OE1   . GLU A 1 236 ? 22.08927  26.83416  22.18123  1.000 64.18932 ? 230  GLU A OE1   1 
ATOM   1801 O OE2   . GLU A 1 236 ? 20.82156  27.90804  23.63740  1.000 62.39279 ? 230  GLU A OE2   1 
ATOM   1802 N N     . ASN A 1 237 ? 17.47669  24.11083  26.55857  1.000 27.58996 ? 231  ASN A N     1 
ATOM   1803 C CA    . ASN A 1 237 ? 16.52027  24.32593  27.63366  1.000 25.08352 ? 231  ASN A CA    1 
ATOM   1804 C C     . ASN A 1 237 ? 15.91995  23.00779  28.13422  1.000 27.85798 ? 231  ASN A C     1 
ATOM   1805 O O     . ASN A 1 237 ? 14.85985  23.01406  28.76470  1.000 28.08091 ? 231  ASN A O     1 
ATOM   1806 C CB    . ASN A 1 237 ? 15.42489  25.28361  27.15876  1.000 27.36898 ? 231  ASN A CB    1 
ATOM   1807 C CG    . ASN A 1 237 ? 14.52552  25.77391  28.29021  1.000 30.92614 ? 231  ASN A CG    1 
ATOM   1808 O OD1   . ASN A 1 237 ? 14.99309  26.07865  29.38269  1.000 36.00150 ? 231  ASN A OD1   1 
ATOM   1809 N ND2   . ASN A 1 237 ? 13.22505  25.84956  28.02429  1.000 32.52314 ? 231  ASN A ND2   1 
ATOM   1810 N N     . TYR A 1 238 ? 16.60654  21.88392  27.91152  1.000 27.60659 ? 232  TYR A N     1 
ATOM   1811 C CA    . TYR A 1 238 ? 15.97238  20.58120  28.11166  1.000 27.99047 ? 232  TYR A CA    1 
ATOM   1812 C C     . TYR A 1 238 ? 15.68675  20.29653  29.58116  1.000 26.78393 ? 232  TYR A C     1 
ATOM   1813 O O     . TYR A 1 238 ? 14.68982  19.63276  29.89047  1.000 26.15719 ? 232  TYR A O     1 
ATOM   1814 C CB    . TYR A 1 238 ? 16.84459  19.48391  27.50646  1.000 29.04753 ? 232  TYR A CB    1 
ATOM   1815 C CG    . TYR A 1 238 ? 16.14498  18.57507  26.46794  1.000 24.95291 ? 232  TYR A CG    1 
ATOM   1816 C CD1   . TYR A 1 238 ? 14.79450  18.25216  26.57402  1.000 24.76636 ? 232  TYR A CD1   1 
ATOM   1817 C CD2   . TYR A 1 238 ? 16.85961  18.06359  25.39465  1.000 24.88496 ? 232  TYR A CD2   1 
ATOM   1818 C CE1   . TYR A 1 238 ? 14.17483  17.40460  25.60529  1.000 26.67458 ? 232  TYR A CE1   1 
ATOM   1819 C CE2   . TYR A 1 238 ? 16.25903  17.23146  24.43518  1.000 25.32871 ? 232  TYR A CE2   1 
ATOM   1820 C CZ    . TYR A 1 238 ? 14.92026  16.89590  24.55641  1.000 25.56038 ? 232  TYR A CZ    1 
ATOM   1821 O OH    . TYR A 1 238 ? 14.33978  16.07081  23.58400  1.000 22.32301 ? 232  TYR A OH    1 
ATOM   1822 N N     . ASP A 1 239 ? 16.52165  20.78151  30.51505  1.000 25.16187 ? 233  ASP A N     1 
ATOM   1823 C CA    . ASP A 1 239 ? 16.20372  20.52521  31.92833  1.000 27.25630 ? 233  ASP A CA    1 
ATOM   1824 C C     . ASP A 1 239 ? 14.88781  21.18035  32.31957  1.000 23.85021 ? 233  ASP A C     1 
ATOM   1825 O O     . ASP A 1 239 ? 14.05951  20.57666  33.00730  1.000 28.28926 ? 233  ASP A O     1 
ATOM   1826 C CB    . ASP A 1 239 ? 17.32006  21.01248  32.86000  1.000 29.20362 ? 233  ASP A CB    1 
ATOM   1827 C CG    . ASP A 1 239 ? 18.59697  20.18976  32.74704  1.000 42.89368 ? 233  ASP A CG    1 
ATOM   1828 O OD1   . ASP A 1 239 ? 18.58535  19.11310  32.11432  1.000 44.21708 ? 233  ASP A OD1   1 
ATOM   1829 O OD2   . ASP A 1 239 ? 19.63413  20.63337  33.28856  1.000 47.85030 ? 233  ASP A OD2   1 
ATOM   1830 N N     . GLN A 1 240 ? 14.66848  22.42516  31.89326  1.000 23.35691 ? 234  GLN A N     1 
ATOM   1831 C CA    . GLN A 1 240 ? 13.40414  23.06426  32.24056  1.000 22.95930 ? 234  GLN A CA    1 
ATOM   1832 C C     . GLN A 1 240 ? 12.23764  22.36038  31.56810  1.000 24.48776 ? 234  GLN A C     1 
ATOM   1833 O O     . GLN A 1 240 ? 11.15706  22.23834  32.15312  1.000 29.47961 ? 234  GLN A O     1 
ATOM   1834 C CB    . GLN A 1 240 ? 13.40879  24.53658  31.83870  1.000 25.86575 ? 234  GLN A CB    1 
ATOM   1835 C CG    . GLN A 1 240 ? 12.16132  25.27468  32.29300  1.000 27.71129 ? 234  GLN A CG    1 
ATOM   1836 C CD    . GLN A 1 240 ? 12.01099  25.31597  33.80214  1.000 40.71771 ? 234  GLN A CD    1 
ATOM   1837 O OE1   . GLN A 1 240 ? 12.96048  25.63324  34.51911  1.000 40.73940 ? 234  GLN A OE1   1 
ATOM   1838 N NE2   . GLN A 1 240 ? 10.82188  24.96168  34.29410  1.000 32.80795 ? 234  GLN A NE2   1 
ATOM   1839 N N     . ILE A 1 241 ? 12.44027  21.92420  30.32726  1.000 23.38095 ? 235  ILE A N     1 
ATOM   1840 C CA    . ILE A 1 241 ? 11.38786  21.23137  29.59542  1.000 24.40741 ? 235  ILE A CA    1 
ATOM   1841 C C     . ILE A 1 241 ? 10.94626  19.99560  30.36440  1.000 23.98692 ? 235  ILE A C     1 
ATOM   1842 O O     . ILE A 1 241 ? 9.74902   19.76353  30.55213  1.000 23.97432 ? 235  ILE A O     1 
ATOM   1843 C CB    . ILE A 1 241 ? 11.87380  20.90615  28.16377  1.000 25.27598 ? 235  ILE A CB    1 
ATOM   1844 C CG1   . ILE A 1 241 ? 11.81875  22.18006  27.30471  1.000 22.64507 ? 235  ILE A CG1   1 
ATOM   1845 C CG2   . ILE A 1 241 ? 11.07917  19.75139  27.54655  1.000 22.26165 ? 235  ILE A CG2   1 
ATOM   1846 C CD1   . ILE A 1 241 ? 12.52014  22.05866  25.95485  1.000 29.54688 ? 235  ILE A CD1   1 
ATOM   1847 N N     . TRP A 1 242 ? 11.89957  19.22534  30.88464  1.000 25.60167 ? 236  TRP A N     1 
ATOM   1848 C CA    . TRP A 1 242 ? 11.51625  18.05184  31.66892  1.000 27.03091 ? 236  TRP A CA    1 
ATOM   1849 C C     . TRP A 1 242 ? 10.92946  18.42217  33.02926  1.000 27.03514 ? 236  TRP A C     1 
ATOM   1850 O O     . TRP A 1 242 ? 10.02268  17.72936  33.51103  1.000 27.13709 ? 236  TRP A O     1 
ATOM   1851 C CB    . TRP A 1 242 ? 12.70869  17.10286  31.80382  1.000 29.83610 ? 236  TRP A CB    1 
ATOM   1852 C CG    . TRP A 1 242 ? 12.89848  16.36025  30.52777  1.000 26.50997 ? 236  TRP A CG    1 
ATOM   1853 C CD1   . TRP A 1 242 ? 13.92971  16.50437  29.63390  1.000 26.49114 ? 236  TRP A CD1   1 
ATOM   1854 C CD2   . TRP A 1 242 ? 11.99146  15.39949  29.94413  1.000 25.21277 ? 236  TRP A CD2   1 
ATOM   1855 N NE1   . TRP A 1 242 ? 13.71740  15.68133  28.53306  1.000 29.36451 ? 236  TRP A NE1   1 
ATOM   1856 C CE2   . TRP A 1 242 ? 12.54825  14.98941  28.71375  1.000 25.40652 ? 236  TRP A CE2   1 
ATOM   1857 C CE3   . TRP A 1 242 ? 10.76999  14.83880  30.35374  1.000 26.58995 ? 236  TRP A CE3   1 
ATOM   1858 C CZ2   . TRP A 1 242 ? 11.92777  14.04129  27.89387  1.000 30.46308 ? 236  TRP A CZ2   1 
ATOM   1859 C CZ3   . TRP A 1 242 ? 10.16778  13.88309  29.54382  1.000 25.82235 ? 236  TRP A CZ3   1 
ATOM   1860 C CH2   . TRP A 1 242 ? 10.73828  13.50869  28.32870  1.000 26.37092 ? 236  TRP A CH2   1 
ATOM   1861 N N     . GLU A 1 243 ? 11.37934  19.52209  33.65703  1.000 30.43838 ? 237  GLU A N     1 
ATOM   1862 C CA    . GLU A 1 243 ? 10.74351  19.92736  34.90448  1.000 28.77668 ? 237  GLU A CA    1 
ATOM   1863 C C     . GLU A 1 243 ? 9.26588   20.23099  34.68595  1.000 31.32753 ? 237  GLU A C     1 
ATOM   1864 O O     . GLU A 1 243 ? 8.42808   19.88518  35.52718  1.000 31.46727 ? 237  GLU A O     1 
ATOM   1865 C CB    . GLU A 1 243 ? 11.46978  21.13202  35.52683  1.000 31.57720 ? 237  GLU A CB    1 
ATOM   1866 C CG    . GLU A 1 243 ? 12.80495  20.76334  36.19419  1.000 38.62280 ? 237  GLU A CG    1 
ATOM   1867 C CD    . GLU A 1 243 ? 12.71026  19.61983  37.23796  1.000 52.63765 ? 237  GLU A CD    1 
ATOM   1868 O OE1   . GLU A 1 243 ? 11.70640  19.52177  37.98580  1.000 56.39189 ? 237  GLU A OE1   1 
ATOM   1869 O OE2   . GLU A 1 243 ? 13.64816  18.79150  37.28751  1.000 57.96837 ? 237  GLU A OE2   1 
ATOM   1870 N N     . ASN A 1 244 ? 8.92959   20.85802  33.54787  1.000 28.10879 ? 238  ASN A N     1 
ATOM   1871 C CA    . ASN A 1 244 ? 7.54212   21.15897  33.22596  1.000 25.72036 ? 238  ASN A CA    1 
ATOM   1872 C C     . ASN A 1 244 ? 6.72589   19.88669  33.03490  1.000 27.99159 ? 238  ASN A C     1 
ATOM   1873 O O     . ASN A 1 244 ? 5.54511   19.85401  33.38066  1.000 28.84753 ? 238  ASN A O     1 
ATOM   1874 C CB    . ASN A 1 244 ? 7.45978   22.00668  31.95017  1.000 25.76642 ? 238  ASN A CB    1 
ATOM   1875 C CG    . ASN A 1 244 ? 8.03215   23.41367  32.13816  1.000 26.38288 ? 238  ASN A CG    1 
ATOM   1876 O OD1   . ASN A 1 244 ? 8.32748   23.82818  33.26020  1.000 31.49906 ? 238  ASN A OD1   1 
ATOM   1877 N ND2   . ASN A 1 244 ? 8.20587   24.13600  31.03970  1.000 27.80100 ? 238  ASN A ND2   1 
ATOM   1878 N N     . VAL A 1 245 ? 7.33563   18.84223  32.47994  1.000 27.61197 ? 239  VAL A N     1 
ATOM   1879 C CA    . VAL A 1 245 ? 6.63263   17.56835  32.32361  1.000 26.51801 ? 239  VAL A CA    1 
ATOM   1880 C C     . VAL A 1 245 ? 6.24695   16.99889  33.68447  1.000 26.64618 ? 239  VAL A C     1 
ATOM   1881 O O     . VAL A 1 245 ? 5.08656   16.63493  33.92131  1.000 29.05757 ? 239  VAL A O     1 
ATOM   1882 C CB    . VAL A 1 245 ? 7.49215   16.57306  31.52572  1.000 30.21367 ? 239  VAL A CB    1 
ATOM   1883 C CG1   . VAL A 1 245 ? 6.89533   15.16193  31.65690  1.000 28.09555 ? 239  VAL A CG1   1 
ATOM   1884 C CG2   . VAL A 1 245 ? 7.56385   17.00991  30.04778  1.000 27.38247 ? 239  VAL A CG2   1 
ATOM   1885 N N     . TRP A 1 246 ? 7.22395   16.87507  34.59197  1.000 25.94353 ? 240  TRP A N     1 
ATOM   1886 C CA    . TRP A 1 246 ? 6.92559   16.31256  35.90831  1.000 28.72525 ? 240  TRP A CA    1 
ATOM   1887 C C     . TRP A 1 246 ? 5.88975   17.14365  36.67835  1.000 29.96658 ? 240  TRP A C     1 
ATOM   1888 O O     . TRP A 1 246 ? 5.15891   16.58857  37.51165  1.000 35.14369 ? 240  TRP A O     1 
ATOM   1889 C CB    . TRP A 1 246 ? 8.22439   16.13210  36.72875  1.000 26.17682 ? 240  TRP A CB    1 
ATOM   1890 C CG    . TRP A 1 246 ? 9.30710   15.34774  35.97267  1.000 25.40469 ? 240  TRP A CG    1 
ATOM   1891 C CD1   . TRP A 1 246 ? 10.57019  15.76075  35.66463  1.000 27.82340 ? 240  TRP A CD1   1 
ATOM   1892 C CD2   . TRP A 1 246 ? 9.17521   14.03166  35.42420  1.000 26.54616 ? 240  TRP A CD2   1 
ATOM   1893 N NE1   . TRP A 1 246 ? 11.23480  14.78038  34.95303  1.000 28.89997 ? 240  TRP A NE1   1 
ATOM   1894 C CE2   . TRP A 1 246 ? 10.39295  13.71149  34.79076  1.000 30.93531 ? 240  TRP A CE2   1 
ATOM   1895 C CE3   . TRP A 1 246 ? 8.14548   13.08957  35.41818  1.000 28.20931 ? 240  TRP A CE3   1 
ATOM   1896 C CZ2   . TRP A 1 246 ? 10.60538  12.48551  34.15680  1.000 30.52512 ? 240  TRP A CZ2   1 
ATOM   1897 C CZ3   . TRP A 1 246 ? 8.35483   11.87185  34.77703  1.000 29.91147 ? 240  TRP A CZ3   1 
ATOM   1898 C CH2   . TRP A 1 246 ? 9.56565   11.58356  34.15478  1.000 31.20673 ? 240  TRP A CH2   1 
ATOM   1899 N N     . ASN A 1 247 ? 5.78304   18.43819  36.40201  1.000 33.78330 ? 241  ASN A N     1 
ATOM   1900 C CA    . ASN A 1 247 ? 4.83730   19.31142  37.08878  1.000 34.12196 ? 241  ASN A CA    1 
ATOM   1901 C C     . ASN A 1 247 ? 3.48953   19.43816  36.39882  1.000 35.65690 ? 241  ASN A C     1 
ATOM   1902 O O     . ASN A 1 247 ? 2.67891   20.27129  36.82378  1.000 38.38277 ? 241  ASN A O     1 
ATOM   1903 C CB    . ASN A 1 247 ? 5.43461   20.70629  37.26375  1.000 38.55259 ? 241  ASN A CB    1 
ATOM   1904 C CG    . ASN A 1 247 ? 6.22931   20.83186  38.53250  1.000 45.89581 ? 241  ASN A CG    1 
ATOM   1905 O OD1   . ASN A 1 247 ? 6.54161   19.83413  39.19108  1.000 48.30715 ? 241  ASN A OD1   1 
ATOM   1906 N ND2   . ASN A 1 247 ? 6.55079   22.06218  38.90061  1.000 62.07163 ? 241  ASN A ND2   1 
ATOM   1907 N N     . SER A 1 248 ? 3.21021   18.63037  35.37998  1.000 30.92889 ? 242  SER A N     1 
ATOM   1908 C CA    . SER A 1 248 ? 2.00743   18.77850  34.56447  1.000 29.95126 ? 242  SER A CA    1 
ATOM   1909 C C     . SER A 1 248 ? 1.09542   17.56918  34.73431  1.000 27.67848 ? 242  SER A C     1 
ATOM   1910 O O     . SER A 1 248 ? 1.49952   16.51971  35.24591  1.000 30.56496 ? 242  SER A O     1 
ATOM   1911 C CB    . SER A 1 248 ? 2.37735   18.93306  33.08194  1.000 28.24899 ? 242  SER A CB    1 
ATOM   1912 O OG    . SER A 1 248 ? 2.96680   17.72320  32.62640  1.000 26.75810 ? 242  SER A OG    1 
ATOM   1913 N N     . ALA A 1 249 ? -0.14704  17.71199  34.26627  1.000 27.67298 ? 243  ALA A N     1 
ATOM   1914 C CA    . ALA A 1 249 ? -1.05096  16.57565  34.29604  1.000 29.11534 ? 243  ALA A CA    1 
ATOM   1915 C C     . ALA A 1 249 ? -0.80380  15.63758  33.11829  1.000 27.03235 ? 243  ALA A C     1 
ATOM   1916 O O     . ALA A 1 249 ? -0.93406  14.41641  33.26682  1.000 30.50509 ? 243  ALA A O     1 
ATOM   1917 C CB    . ALA A 1 249 ? -2.51399  17.04161  34.31199  1.000 32.79992 ? 243  ALA A CB    1 
ATOM   1918 N N     . LEU A 1 250 ? -0.42433  16.16855  31.95009  1.000 25.52996 ? 244  LEU A N     1 
ATOM   1919 C CA    . LEU A 1 250 ? -0.35786  15.33514  30.74661  1.000 25.97714 ? 244  LEU A CA    1 
ATOM   1920 C C     . LEU A 1 250 ? 1.04456   15.00078  30.26678  1.000 25.58624 ? 244  LEU A C     1 
ATOM   1921 O O     . LEU A 1 250 ? 1.20401   14.01773  29.53157  1.000 24.90933 ? 244  LEU A O     1 
ATOM   1922 C CB    . LEU A 1 250 ? -1.10772  16.00860  29.58477  1.000 26.78586 ? 244  LEU A CB    1 
ATOM   1923 C CG    . LEU A 1 250 ? -2.59804  16.17281  29.83381  1.000 29.96624 ? 244  LEU A CG    1 
ATOM   1924 C CD1   . LEU A 1 250 ? -3.13626  17.08697  28.77691  1.000 28.98872 ? 244  LEU A CD1   1 
ATOM   1925 C CD2   . LEU A 1 250 ? -3.31676  14.86041  29.78489  1.000 36.38239 ? 244  LEU A CD2   1 
ATOM   1926 N N     . GLY A 1 251 ? 2.05896   15.77882  30.64064  1.000 23.75531 ? 245  GLY A N     1 
ATOM   1927 C CA    . GLY A 1 251 ? 3.40886   15.49862  30.17659  1.000 24.80181 ? 245  GLY A CA    1 
ATOM   1928 C C     . GLY A 1 251 ? 3.62771   15.69118  28.69533  1.000 27.46168 ? 245  GLY A C     1 
ATOM   1929 O O     . GLY A 1 251 ? 4.58051   15.13535  28.13566  1.000 25.77876 ? 245  GLY A O     1 
ATOM   1930 N N     . TYR A 1 252 ? 2.79952   16.50264  28.05803  1.000 23.96695 ? 246  TYR A N     1 
ATOM   1931 C CA    . TYR A 1 252 ? 2.86001   16.75442  26.62745  1.000 23.74861 ? 246  TYR A CA    1 
ATOM   1932 C C     . TYR A 1 252 ? 3.52985   18.07829  26.29284  1.000 25.72165 ? 246  TYR A C     1 
ATOM   1933 O O     . TYR A 1 252 ? 3.57471   18.45780  25.11734  1.000 27.28683 ? 246  TYR A O     1 
ATOM   1934 C CB    . TYR A 1 252 ? 1.44101   16.73084  26.06637  1.000 25.88625 ? 246  TYR A CB    1 
ATOM   1935 C CG    . TYR A 1 252 ? 1.04749   15.38820  25.51798  1.000 26.86162 ? 246  TYR A CG    1 
ATOM   1936 C CD1   . TYR A 1 252 ? 0.79141   14.32626  26.36022  1.000 26.17772 ? 246  TYR A CD1   1 
ATOM   1937 C CD2   . TYR A 1 252 ? 0.84575   15.20610  24.14823  1.000 34.80867 ? 246  TYR A CD2   1 
ATOM   1938 C CE1   . TYR A 1 252 ? 0.42115   13.07784  25.85570  1.000 26.16982 ? 246  TYR A CE1   1 
ATOM   1939 C CE2   . TYR A 1 252 ? 0.46334   13.96574  23.63740  1.000 33.86923 ? 246  TYR A CE2   1 
ATOM   1940 C CZ    . TYR A 1 252 ? 0.26050   12.90272  24.50542  1.000 36.44289 ? 246  TYR A CZ    1 
ATOM   1941 O OH    . TYR A 1 252 ? -0.12304  11.65825  24.03260  1.000 32.58793 ? 246  TYR A OH    1 
ATOM   1942 N N     . GLY A 1 253 ? 4.03429   18.79685  27.29604  1.000 24.87063 ? 247  GLY A N     1 
ATOM   1943 C CA    . GLY A 1 253 ? 4.65472   20.08441  27.05515  1.000 29.24926 ? 247  GLY A CA    1 
ATOM   1944 C C     . GLY A 1 253 ? 3.67981   21.21354  26.81288  1.000 30.84383 ? 247  GLY A C     1 
ATOM   1945 O O     . GLY A 1 253 ? 4.07377   22.26013  26.29691  1.000 30.80752 ? 247  GLY A O     1 
ATOM   1946 N N     . LEU A 1 254 ? 2.42212   21.03196  27.17802  1.000 24.42940 ? 248  LEU A N     1 
ATOM   1947 C CA    . LEU A 1 254 ? 1.38489   22.02250  26.94747  1.000 27.61901 ? 248  LEU A CA    1 
ATOM   1948 C C     . LEU A 1 254 ? 1.37888   23.07084  28.05600  1.000 31.52211 ? 248  LEU A C     1 
ATOM   1949 O O     . LEU A 1 254 ? 1.84134   22.82993  29.17253  1.000 30.48807 ? 248  LEU A O     1 
ATOM   1950 C CB    . LEU A 1 254 ? 0.03113   21.34874  26.90677  1.000 25.48183 ? 248  LEU A CB    1 
ATOM   1951 C CG    . LEU A 1 254 ? -0.03846  20.18691  25.91652  1.000 25.16487 ? 248  LEU A CG    1 
ATOM   1952 C CD1   . LEU A 1 254 ? -1.37968  19.55439  26.06158  1.000 29.86640 ? 248  LEU A CD1   1 
ATOM   1953 C CD2   . LEU A 1 254 ? 0.15459   20.75070  24.51792  1.000 28.39563 ? 248  LEU A CD2   1 
ATOM   1954 N N     . ASN A 1 255 ? 0.80883   24.23536  27.73985  1.000 29.80745 ? 249  ASN A N     1 
ATOM   1955 C CA    . ASN A 1 255 ? 0.40323   25.19773  28.77087  1.000 32.62307 ? 249  ASN A CA    1 
ATOM   1956 C C     . ASN A 1 255 ? -1.00800  24.80693  29.17417  1.000 33.02313 ? 249  ASN A C     1 
ATOM   1957 O O     . ASN A 1 255 ? -1.98621  25.21255  28.55744  1.000 31.89522 ? 249  ASN A O     1 
ATOM   1958 C CB    . ASN A 1 255 ? 0.46387   26.62760  28.24977  1.000 32.77487 ? 249  ASN A CB    1 
ATOM   1959 C CG    . ASN A 1 255 ? 1.73125   26.90941  27.48627  1.000 42.86050 ? 249  ASN A CG    1 
ATOM   1960 O OD1   . ASN A 1 255 ? 2.83149   26.62122  27.96874  1.000 47.34197 ? 249  ASN A OD1   1 
ATOM   1961 N ND2   . ASN A 1 255 ? 1.59361   27.45553  26.27486  1.000 41.89912 ? 249  ASN A ND2   1 
ATOM   1962 N N     . GLU A 1 256 ? -1.11632  23.98761  30.21241  1.000 27.04680 ? 250  GLU A N     1 
ATOM   1963 C CA    . GLU A 1 256 ? -2.40077  23.40568  30.56415  1.000 30.52559 ? 250  GLU A CA    1 
ATOM   1964 C C     . GLU A 1 256 ? -3.32798  24.45870  31.17926  1.000 37.99522 ? 250  GLU A C     1 
ATOM   1965 O O     . GLU A 1 256 ? -3.05161  25.01410  32.25002  1.000 30.08496 ? 250  GLU A O     1 
ATOM   1966 C CB    . GLU A 1 256 ? -2.16988  22.22007  31.48756  1.000 33.87818 ? 250  GLU A CB    1 
ATOM   1967 C CG    . GLU A 1 256 ? -1.40243  21.10639  30.74963  1.000 27.87805 ? 250  GLU A CG    1 
ATOM   1968 C CD    . GLU A 1 256 ? -0.96183  19.96490  31.64900  1.000 37.07657 ? 250  GLU A CD    1 
ATOM   1969 O OE1   . GLU A 1 256 ? -1.10492  20.08570  32.89569  1.000 36.57967 ? 250  GLU A OE1   1 
ATOM   1970 O OE2   . GLU A 1 256 ? -0.49622  18.93672  31.08875  1.000 29.30129 ? 250  GLU A OE2   1 
ATOM   1971 N N     . SER A 1 257 ? -4.43550  24.72300  30.49580  1.000 31.16304 ? 251  SER A N     1 
ATOM   1972 C CA    . SER A 1 257 ? -5.27217  25.87967  30.79326  1.000 30.60332 ? 251  SER A CA    1 
ATOM   1973 C C     . SER A 1 257 ? -6.13774  25.64374  32.02762  1.000 31.67892 ? 251  SER A C     1 
ATOM   1974 O O     . SER A 1 257 ? -6.58695  24.52922  32.29284  1.000 35.16604 ? 251  SER A O     1 
ATOM   1975 C CB    . SER A 1 257 ? -6.16848  26.18625  29.59139  1.000 31.95577 ? 251  SER A CB    1 
ATOM   1976 O OG    . SER A 1 257 ? -7.01384  27.29961  29.84897  1.000 35.03466 ? 251  SER A OG    1 
ATOM   1977 N N     . THR A 1 258 ? -6.39179  26.72308  32.77306  1.000 39.96155 ? 252  THR A N     1 
ATOM   1978 C CA    . THR A 1 258 ? -7.41956  26.73888  33.81267  1.000 32.73459 ? 252  THR A CA    1 
ATOM   1979 C C     . THR A 1 258 ? -8.61683  27.60401  33.42412  1.000 38.51576 ? 252  THR A C     1 
ATOM   1980 O O     . THR A 1 258 ? -9.53988  27.75913  34.22828  1.000 43.01782 ? 252  THR A O     1 
ATOM   1981 C CB    . THR A 1 258 ? -6.84026  27.24615  35.14156  1.000 37.62947 ? 252  THR A CB    1 
ATOM   1982 O OG1   . THR A 1 258 ? -6.29276  28.54486  34.94031  1.000 37.77197 ? 252  THR A OG1   1 
ATOM   1983 C CG2   . THR A 1 258 ? -5.73226  26.30666  35.66787  1.000 38.47171 ? 252  THR A CG2   1 
ATOM   1984 N N     . LEU A 1 259 ? -8.62104  28.14919  32.20652  1.000 35.08229 ? 253  LEU A N     1 
ATOM   1985 C CA    . LEU A 1 259 ? -9.61099  29.12679  31.75283  1.000 32.58587 ? 253  LEU A CA    1 
ATOM   1986 C C     . LEU A 1 259 ? -10.93027 28.44729  31.39207  1.000 41.47651 ? 253  LEU A C     1 
ATOM   1987 O O     . LEU A 1 259 ? -10.94061 27.52495  30.55306  1.000 36.66443 ? 253  LEU A O     1 
ATOM   1988 C CB    . LEU A 1 259 ? -9.05215  29.87669  30.54576  1.000 35.05076 ? 253  LEU A CB    1 
ATOM   1989 C CG    . LEU A 1 259 ? -9.91588  30.93879  29.86457  1.000 37.70063 ? 253  LEU A CG    1 
ATOM   1990 C CD1   . LEU A 1 259 ? -10.02279 32.14142  30.79126  1.000 39.36222 ? 253  LEU A CD1   1 
ATOM   1991 C CD2   . LEU A 1 259 ? -9.38266  31.35850  28.48227  1.000 34.53420 ? 253  LEU A CD2   1 
ATOM   1992 N N     . PRO A 1 260 ? -12.05582 28.85451  31.98098  1.000 39.42814 ? 254  PRO A N     1 
ATOM   1993 C CA    . PRO A 1 260 ? -13.33445 28.21265  31.64434  1.000 35.84176 ? 254  PRO A CA    1 
ATOM   1994 C C     . PRO A 1 260 ? -13.81499 28.66221  30.27244  1.000 37.80112 ? 254  PRO A C     1 
ATOM   1995 O O     . PRO A 1 260 ? -13.74389 29.84578  29.94167  1.000 37.71714 ? 254  PRO A O     1 
ATOM   1996 C CB    . PRO A 1 260 ? -14.27910 28.68773  32.75826  1.000 43.26321 ? 254  PRO A CB    1 
ATOM   1997 C CG    . PRO A 1 260 ? -13.34059 29.27672  33.84388  1.000 40.80364 ? 254  PRO A CG    1 
ATOM   1998 C CD    . PRO A 1 260 ? -12.20894 29.84936  33.05940  1.000 41.24515 ? 254  PRO A CD    1 
ATOM   1999 N N     . THR A 1 261 ? -14.29937 27.69193  29.47436  1.000 35.03171 ? 255  THR A N     1 
ATOM   2000 C CA    . THR A 1 261 ? -14.63697 27.94256  28.07068  1.000 37.45328 ? 255  THR A CA    1 
ATOM   2001 C C     . THR A 1 261 ? -15.63735 29.09302  27.91880  1.000 36.22382 ? 255  THR A C     1 
ATOM   2002 O O     . THR A 1 261 ? -15.47889 29.95332  27.04487  1.000 40.82326 ? 255  THR A O     1 
ATOM   2003 C CB    . THR A 1 261 ? -15.19098 26.65913  27.42910  1.000 34.47557 ? 255  THR A CB    1 
ATOM   2004 O OG1   . THR A 1 261 ? -14.23830 25.58714  27.54698  1.000 30.71677 ? 255  THR A OG1   1 
ATOM   2005 C CG2   . THR A 1 261 ? -15.52866 26.87225  25.94585  1.000 30.08535 ? 255  THR A CG2   1 
ATOM   2006 N N     . MET A 1 262 ? -16.65887 29.13368  28.76827  1.000 37.86495 ? 256  MET A N     1 
ATOM   2007 C CA    . MET A 1 262 ? -17.75498 30.08809  28.63211  1.000 42.05329 ? 256  MET A CA    1 
ATOM   2008 C C     . MET A 1 262 ? -17.46632 31.43225  29.29268  1.000 44.18270 ? 256  MET A C     1 
ATOM   2009 O O     . MET A 1 262 ? -18.29507 32.34658  29.19279  1.000 46.69565 ? 256  MET A O     1 
ATOM   2010 C CB    . MET A 1 262 ? -19.02880 29.47299  29.21335  1.000 41.70448 ? 256  MET A CB    1 
ATOM   2011 C CG    . MET A 1 262 ? -19.42314 28.15363  28.56715  1.000 42.51951 ? 256  MET A CG    1 
ATOM   2012 S SD    . MET A 1 262 ? -19.35427 28.08227  26.75288  1.000 45.23897 ? 256  MET A SD    1 
ATOM   2013 C CE    . MET A 1 262 ? -20.16298 29.60615  26.23490  1.000 41.49534 ? 256  MET A CE    1 
ATOM   2014 N N     . SER A 1 263 ? -16.30572 31.59281  29.92857  1.000 46.91017 ? 257  SER A N     1 
ATOM   2015 C CA    . SER A 1 263 ? -15.94758 32.85032  30.57782  1.000 47.23747 ? 257  SER A CA    1 
ATOM   2016 C C     . SER A 1 263 ? -15.42185 33.90681  29.60969  1.000 47.39077 ? 257  SER A C     1 
ATOM   2017 O O     . SER A 1 263 ? -15.15856 35.04086  30.03572  1.000 47.57802 ? 257  SER A O     1 
ATOM   2018 C CB    . SER A 1 263 ? -14.90101 32.59597  31.66527  1.000 46.11690 ? 257  SER A CB    1 
ATOM   2019 O OG    . SER A 1 263 ? -13.62188 32.40326  31.08038  1.000 47.53216 ? 257  SER A OG    1 
ATOM   2020 N N     . VAL A 1 264 ? -15.26329 33.57889  28.32865  1.000 41.80127 ? 258  VAL A N     1 
ATOM   2021 C CA    . VAL A 1 264 ? -14.80671 34.53153  27.32656  1.000 38.79175 ? 258  VAL A CA    1 
ATOM   2022 C C     . VAL A 1 264 ? -15.92991 34.72722  26.30565  1.000 39.19048 ? 258  VAL A C     1 
ATOM   2023 O O     . VAL A 1 264 ? -16.90408 33.97940  26.26955  1.000 43.95466 ? 258  VAL A O     1 
ATOM   2024 C CB    . VAL A 1 264 ? -13.50092 34.07431  26.64486  1.000 42.82213 ? 258  VAL A CB    1 
ATOM   2025 C CG1   . VAL A 1 264 ? -12.39207 33.87096  27.70295  1.000 41.10591 ? 258  VAL A CG1   1 
ATOM   2026 C CG2   . VAL A 1 264 ? -13.74590 32.78841  25.84307  1.000 41.43016 ? 258  VAL A CG2   1 
ATOM   2027 N N     . SER A 1 265 ? -15.79047 35.75823  25.48410  1.000 38.24932 ? 259  SER A N     1 
ATOM   2028 C CA    . SER A 1 265 ? -16.77552 36.00340  24.44286  1.000 44.09411 ? 259  SER A CA    1 
ATOM   2029 C C     . SER A 1 265 ? -16.69395 34.93498  23.35184  1.000 46.33232 ? 259  SER A C     1 
ATOM   2030 O O     . SER A 1 265 ? -15.75905 34.12729  23.29547  1.000 42.19194 ? 259  SER A O     1 
ATOM   2031 C CB    . SER A 1 265 ? -16.55632 37.37313  23.82054  1.000 44.65228 ? 259  SER A CB    1 
ATOM   2032 O OG    . SER A 1 265 ? -15.29028 37.41897  23.19917  1.000 42.16969 ? 259  SER A OG    1 
ATOM   2033 N N     . ALA A 1 266 ? -17.68678 34.95991  22.45531  1.000 44.45957 ? 260  ALA A N     1 
ATOM   2034 C CA    . ALA A 1 266 ? -17.66143 34.08700  21.28282  1.000 43.27737 ? 260  ALA A CA    1 
ATOM   2035 C C     . ALA A 1 266 ? -16.45123 34.37225  20.40188  1.000 46.14580 ? 260  ALA A C     1 
ATOM   2036 O O     . ALA A 1 266 ? -15.79165 33.43689  19.92378  1.000 39.53877 ? 260  ALA A O     1 
ATOM   2037 C CB    . ALA A 1 266 ? -18.95426 34.24398  20.47473  1.000 43.78390 ? 260  ALA A CB    1 
ATOM   2038 N N     . GLU A 1 267 ? -16.14506 35.65580  20.16626  1.000 42.96427 ? 261  GLU A N     1 
ATOM   2039 C CA    . GLU A 1 267 ? -15.01494 36.00074  19.30246  1.000 43.65744 ? 261  GLU A CA    1 
ATOM   2040 C C     . GLU A 1 267 ? -13.68678 35.56284  19.91446  1.000 44.05790 ? 261  GLU A C     1 
ATOM   2041 O O     . GLU A 1 267 ? -12.80358 35.06623  19.19971  1.000 39.55951 ? 261  GLU A O     1 
ATOM   2042 C CB    . GLU A 1 267 ? -14.98999 37.50620  19.00933  1.000 48.49874 ? 261  GLU A CB    1 
ATOM   2043 C CG    . GLU A 1 267 ? -16.34061 38.10359  18.60124  1.000 60.95768 ? 261  GLU A CG    1 
ATOM   2044 C CD    . GLU A 1 267 ? -17.17609 38.57519  19.79681  1.000 65.42192 ? 261  GLU A CD    1 
ATOM   2045 O OE1   . GLU A 1 267 ? -17.19359 39.80395  20.06670  1.000 63.75309 ? 261  GLU A OE1   1 
ATOM   2046 O OE2   . GLU A 1 267 ? -17.82045 37.72179  20.45724  1.000 64.35320 ? 261  GLU A OE2   1 
ATOM   2047 N N     . GLU A 1 268 ? -13.52150 35.74199  21.22960  1.000 37.62824 ? 262  GLU A N     1 
ATOM   2048 C CA    . GLU A 1 268 ? -12.27173 35.33604  21.86701  1.000 37.22714 ? 262  GLU A CA    1 
ATOM   2049 C C     . GLU A 1 268 ? -12.14584 33.82027  21.92115  1.000 36.00234 ? 262  GLU A C     1 
ATOM   2050 O O     . GLU A 1 268 ? -11.04291 33.27818  21.78225  1.000 35.41989 ? 262  GLU A O     1 
ATOM   2051 C CB    . GLU A 1 268 ? -12.15852 35.92875  23.27138  1.000 38.40346 ? 262  GLU A CB    1 
ATOM   2052 C CG    . GLU A 1 268 ? -10.73556 35.86554  23.82927  1.000 47.42580 ? 262  GLU A CG    1 
ATOM   2053 C CD    . GLU A 1 268 ? -10.67066 36.14278  25.32329  1.000 65.59721 ? 262  GLU A CD    1 
ATOM   2054 O OE1   . GLU A 1 268 ? -11.34991 37.09173  25.78627  1.000 71.32750 ? 262  GLU A OE1   1 
ATOM   2055 O OE2   . GLU A 1 268 ? -9.94595  35.40408  26.03375  1.000 62.96025 ? 262  GLU A OE2   1 
ATOM   2056 N N     . ARG A 1 269 ? -13.26224 33.11972  22.11414  1.000 36.04004 ? 263  ARG A N     1 
ATOM   2057 C CA    . ARG A 1 269 ? -13.23067 31.66171  22.14072  1.000 33.34587 ? 263  ARG A CA    1 
ATOM   2058 C C     . ARG A 1 269 ? -12.82229 31.08935  20.78538  1.000 34.19943 ? 263  ARG A C     1 
ATOM   2059 O O     . ARG A 1 269 ? -12.06371 30.11073  20.71655  1.000 31.68161 ? 263  ARG A O     1 
ATOM   2060 C CB    . ARG A 1 269 ? -14.59282 31.13343  22.57812  1.000 38.49202 ? 263  ARG A CB    1 
ATOM   2061 C CG    . ARG A 1 269 ? -14.67136 29.63589  22.76215  1.000 33.92507 ? 263  ARG A CG    1 
ATOM   2062 C CD    . ARG A 1 269 ? -16.09095 29.17864  23.06580  1.000 38.17319 ? 263  ARG A CD    1 
ATOM   2063 N NE    . ARG A 1 269 ? -16.62498 29.84434  24.24172  1.000 49.62710 ? 263  ARG A NE    1 
ATOM   2064 C CZ    . ARG A 1 269 ? -17.52342 30.82006  24.23171  1.000 49.60070 ? 263  ARG A CZ    1 
ATOM   2065 N NH1   . ARG A 1 269 ? -18.17852 31.15734  23.13044  1.000 47.71464 ? 263  ARG A NH1   1 
ATOM   2066 N NH2   . ARG A 1 269 ? -17.77882 31.46827  25.36008  1.000 48.14924 ? 263  ARG A NH2   1 
ATOM   2067 N N     . ASP A 1 270 ? -13.30057 31.69854  19.69877  1.000 32.66220 ? 264  ASP A N     1 
ATOM   2068 C CA    . ASP A 1 270 ? -12.92251 31.25338  18.36445  1.000 38.25344 ? 264  ASP A CA    1 
ATOM   2069 C C     . ASP A 1 270 ? -11.43383 31.47195  18.11190  1.000 37.26122 ? 264  ASP A C     1 
ATOM   2070 O O     . ASP A 1 270 ? -10.76423 30.61451  17.52022  1.000 30.97071 ? 264  ASP A O     1 
ATOM   2071 C CB    . ASP A 1 270 ? -13.75694 31.99250  17.32419  1.000 38.30202 ? 264  ASP A CB    1 
ATOM   2072 C CG    . ASP A 1 270 ? -13.46973 31.52994  15.92747  1.000 48.46709 ? 264  ASP A CG    1 
ATOM   2073 O OD1   . ASP A 1 270 ? -13.89042 30.39821  15.58982  1.000 46.83802 ? 264  ASP A OD1   1 
ATOM   2074 O OD2   . ASP A 1 270 ? -12.78683 32.27318  15.19092  1.000 52.47373 ? 264  ASP A OD2   1 
ATOM   2075 N N     . LYS A 1 271 ? -10.90176 32.62383  18.53382  1.000 32.62408 ? 265  LYS A N     1 
ATOM   2076 C CA    . LYS A 1 271 ? -9.46843  32.88527  18.38278  1.000 32.13274 ? 265  LYS A CA    1 
ATOM   2077 C C     . LYS A 1 271 ? -8.62784  31.86347  19.14338  1.000 26.73044 ? 265  LYS A C     1 
ATOM   2078 O O     . LYS A 1 271 ? -7.55872  31.45767  18.67296  1.000 29.73044 ? 265  LYS A O     1 
ATOM   2079 C CB    . LYS A 1 271 ? -9.11450  34.29469  18.87411  1.000 34.28126 ? 265  LYS A CB    1 
ATOM   2080 C CG    . LYS A 1 271 ? -9.73227  35.42445  18.07556  1.000 49.63136 ? 265  LYS A CG    1 
ATOM   2081 C CD    . LYS A 1 271 ? -8.74878  35.97377  17.04786  1.000 61.14607 ? 265  LYS A CD    1 
ATOM   2082 C CE    . LYS A 1 271 ? -9.45935  36.80311  15.99093  1.000 63.11078 ? 265  LYS A CE    1 
ATOM   2083 N NZ    . LYS A 1 271 ? -9.88262  38.10369  16.58287  1.000 65.88137 ? 265  LYS A NZ    1 
ATOM   2084 N N     . ILE A 1 272 ? -9.07731  31.46488  20.33144  1.000 28.25158 ? 266  ILE A N     1 
ATOM   2085 C CA    . ILE A 1 272 ? -8.32301  30.51445  21.13791  1.000 29.17485 ? 266  ILE A CA    1 
ATOM   2086 C C     . ILE A 1 272 ? -8.32526  29.13660  20.47427  1.000 30.36089 ? 266  ILE A C     1 
ATOM   2087 O O     . ILE A 1 272 ? -7.27920  28.49025  20.34648  1.000 27.58691 ? 266  ILE A O     1 
ATOM   2088 C CB    . ILE A 1 272 ? -8.88325  30.47348  22.57569  1.000 26.07971 ? 266  ILE A CB    1 
ATOM   2089 C CG1   . ILE A 1 272 ? -8.62263  31.80689  23.29193  1.000 31.07104 ? 266  ILE A CG1   1 
ATOM   2090 C CG2   . ILE A 1 272 ? -8.26835  29.33316  23.39651  1.000 26.24999 ? 266  ILE A CG2   1 
ATOM   2091 C CD1   . ILE A 1 272 ? -9.26002  31.88824  24.67384  1.000 34.99445 ? 266  ILE A CD1   1 
ATOM   2092 N N     . PHE A 1 273 ? -9.50156  28.65690  20.06092  1.000 28.84999 ? 267  PHE A N     1 
ATOM   2093 C CA    . PHE A 1 273 ? -9.54798  27.38740  19.33029  1.000 27.66706 ? 267  PHE A CA    1 
ATOM   2094 C C     . PHE A 1 273 ? -8.72351  27.46028  18.04711  1.000 28.31493 ? 267  PHE A C     1 
ATOM   2095 O O     . PHE A 1 273 ? -7.98279  26.52429  17.71681  1.000 28.11465 ? 267  PHE A O     1 
ATOM   2096 C CB    . PHE A 1 273 ? -10.99165 27.02338  19.00906  1.000 27.11021 ? 267  PHE A CB    1 
ATOM   2097 C CG    . PHE A 1 273 ? -11.75497 26.47821  20.16810  1.000 26.11889 ? 267  PHE A CG    1 
ATOM   2098 C CD1   . PHE A 1 273 ? -11.22139 25.49282  20.97405  1.000 27.46730 ? 267  PHE A CD1   1 
ATOM   2099 C CD2   . PHE A 1 273 ? -13.04074 26.92157  20.41330  1.000 30.59230 ? 267  PHE A CD2   1 
ATOM   2100 C CE1   . PHE A 1 273 ? -11.95513 24.95016  22.02632  1.000 27.90831 ? 267  PHE A CE1   1 
ATOM   2101 C CE2   . PHE A 1 273 ? -13.77868 26.40305  21.45796  1.000 27.01291 ? 267  PHE A CE2   1 
ATOM   2102 C CZ    . PHE A 1 273 ? -13.24399 25.42544  22.27190  1.000 28.41775 ? 267  PHE A CZ    1 
ATOM   2103 N N     . GLU A 1 274 ? -8.81492  28.56991  17.31285  1.000 25.36279 ? 268  GLU A N     1 
ATOM   2104 C CA    . GLU A 1 274 ? -8.09107  28.64813  16.04976  1.000 30.20357 ? 268  GLU A CA    1 
ATOM   2105 C C     . GLU A 1 274 ? -6.57882  28.60454  16.27139  1.000 27.85706 ? 268  GLU A C     1 
ATOM   2106 O O     . GLU A 1 274 ? -5.85182  28.02335  15.46729  1.000 29.06265 ? 268  GLU A O     1 
ATOM   2107 C CB    . GLU A 1 274 ? -8.50619  29.90866  15.28813  1.000 29.55478 ? 268  GLU A CB    1 
ATOM   2108 C CG    . GLU A 1 274 ? -7.75923  30.15744  13.98132  1.000 32.42222 ? 268  GLU A CG    1 
ATOM   2109 C CD    . GLU A 1 274 ? -8.16076  29.19024  12.86433  1.000 32.89569 ? 268  GLU A CD    1 
ATOM   2110 O OE1   . GLU A 1 274 ? -9.24822  28.58546  12.93188  1.000 38.95624 ? 268  GLU A OE1   1 
ATOM   2111 O OE2   . GLU A 1 274 ? -7.39739  29.05982  11.88732  1.000 43.60239 ? 268  GLU A OE2   1 
ATOM   2112 N N     . LYS A 1 275 ? -6.09412  29.19240  17.35995  1.000 26.98747 ? 269  LYS A N     1 
ATOM   2113 C CA    . LYS A 1 275 ? -4.66366  29.15047  17.65034  1.000 29.62214 ? 269  LYS A CA    1 
ATOM   2114 C C     . LYS A 1 275 ? -4.18359  27.71681  17.87345  1.000 29.25410 ? 269  LYS A C     1 
ATOM   2115 O O     . LYS A 1 275 ? -3.12934  27.31042  17.36525  1.000 27.35653 ? 269  LYS A O     1 
ATOM   2116 C CB    . LYS A 1 275 ? -4.37592  30.01196  18.88029  1.000 34.49434 ? 269  LYS A CB    1 
ATOM   2117 C CG    . LYS A 1 275 ? -2.91878  30.12545  19.25833  1.000 40.77562 ? 269  LYS A CG    1 
ATOM   2118 C CD    . LYS A 1 275 ? -2.68593  31.37256  20.10133  1.000 48.87836 ? 269  LYS A CD    1 
ATOM   2119 C CE    . LYS A 1 275 ? -1.19904  31.67174  20.22741  1.000 55.00107 ? 269  LYS A CE    1 
ATOM   2120 N NZ    . LYS A 1 275 ? -0.57733  30.68326  21.16088  1.000 44.03133 ? 269  LYS A NZ    1 
ATOM   2121 N N     . ALA A 1 276 ? -4.94417  26.94204  18.65269  1.000 24.22571 ? 270  ALA A N     1 
ATOM   2122 C CA    . ALA A 1 276 ? -4.60318  25.54175  18.89707  1.000 25.41952 ? 270  ALA A CA    1 
ATOM   2123 C C     . ALA A 1 276 ? -4.67787  24.72467  17.61657  1.000 26.97567 ? 270  ALA A C     1 
ATOM   2124 O O     . ALA A 1 276 ? -3.82206  23.86507  17.36130  1.000 27.87852 ? 270  ALA A O     1 
ATOM   2125 C CB    . ALA A 1 276 ? -5.54097  24.96279  19.94942  1.000 26.89433 ? 270  ALA A CB    1 
ATOM   2126 N N     . TRP A 1 277 ? -5.68895  24.99524  16.79805  1.000 22.86746 ? 271  TRP A N     1 
ATOM   2127 C CA    . TRP A 1 277 ? -5.87800  24.26521  15.55056  1.000 23.93559 ? 271  TRP A CA    1 
ATOM   2128 C C     . TRP A 1 277 ? -4.69480  24.47429  14.60981  1.000 25.24136 ? 271  TRP A C     1 
ATOM   2129 O O     . TRP A 1 277 ? -4.19130  23.51189  14.01521  1.000 24.73497 ? 271  TRP A O     1 
ATOM   2130 C CB    . TRP A 1 277 ? -7.20910  24.71842  14.91227  1.000 23.94803 ? 271  TRP A CB    1 
ATOM   2131 C CG    . TRP A 1 277 ? -7.55517  24.05952  13.61912  1.000 25.43724 ? 271  TRP A CG    1 
ATOM   2132 C CD1   . TRP A 1 277 ? -7.12931  24.41090  12.36570  1.000 23.98411 ? 271  TRP A CD1   1 
ATOM   2133 C CD2   . TRP A 1 277 ? -8.39628  22.91528  13.44791  1.000 21.87156 ? 271  TRP A CD2   1 
ATOM   2134 N NE1   . TRP A 1 277 ? -7.66786  23.55334  11.43293  1.000 23.74255 ? 271  TRP A NE1   1 
ATOM   2135 C CE2   . TRP A 1 277 ? -8.45785  22.63927  12.07250  1.000 23.51327 ? 271  TRP A CE2   1 
ATOM   2136 C CE3   . TRP A 1 277 ? -9.13664  22.12365  14.32402  1.000 22.53960 ? 271  TRP A CE3   1 
ATOM   2137 C CZ2   . TRP A 1 277 ? -9.18973  21.55044  11.55931  1.000 23.55735 ? 271  TRP A CZ2   1 
ATOM   2138 C CZ3   . TRP A 1 277 ? -9.85274  21.05926  13.81978  1.000 23.55082 ? 271  TRP A CZ3   1 
ATOM   2139 C CH2   . TRP A 1 277 ? -9.87080  20.78835  12.45320  1.000 22.27076 ? 271  TRP A CH2   1 
ATOM   2140 N N     . GLN A 1 278 ? -4.20050  25.72005  14.50072  1.000 23.04428 ? 272  GLN A N     1 
ATOM   2141 C CA    . GLN A 1 278 ? -3.04302  25.99992  13.64475  1.000 27.86426 ? 272  GLN A CA    1 
ATOM   2142 C C     . GLN A 1 278 ? -1.74871  25.41004  14.20513  1.000 27.53183 ? 272  GLN A C     1 
ATOM   2143 O O     . GLN A 1 278 ? -0.90505  24.93960  13.43879  1.000 29.42599 ? 272  GLN A O     1 
ATOM   2144 C CB    . GLN A 1 278 ? -2.85784  27.50584  13.46432  1.000 30.35418 ? 272  GLN A CB    1 
ATOM   2145 C CG    . GLN A 1 278 ? -3.92490  28.15273  12.63440  1.000 36.62638 ? 272  GLN A CG    1 
ATOM   2146 C CD    . GLN A 1 278 ? -3.96256  27.62224  11.21195  1.000 41.05558 ? 272  GLN A CD    1 
ATOM   2147 O OE1   . GLN A 1 278 ? -2.92085  27.40331  10.59309  1.000 42.43467 ? 272  GLN A OE1   1 
ATOM   2148 N NE2   . GLN A 1 278 ? -5.17057  27.46132  10.66916  1.000 35.91717 ? 272  GLN A NE2   1 
ATOM   2149 N N     . GLU A 1 279 ? -1.55097  25.47414  15.52294  1.000 26.91309 ? 273  GLU A N     1 
ATOM   2150 C CA    . GLU A 1 279 ? -0.37319  24.84621  16.12631  1.000 26.96059 ? 273  GLU A CA    1 
ATOM   2151 C C     . GLU A 1 279 ? -0.44004  23.32348  16.02155  1.000 30.25441 ? 273  GLU A C     1 
ATOM   2152 O O     . GLU A 1 279 ? 0.58275   22.65630  15.79550  1.000 29.29008 ? 273  GLU A O     1 
ATOM   2153 C CB    . GLU A 1 279 ? -0.24520  25.29487  17.58616  1.000 28.40129 ? 273  GLU A CB    1 
ATOM   2154 C CG    . GLU A 1 279 ? 0.77705   24.53397  18.42978  1.000 38.16381 ? 273  GLU A CG    1 
ATOM   2155 C CD    . GLU A 1 279 ? 2.21326   24.96741  18.23812  1.000 48.39081 ? 273  GLU A CD    1 
ATOM   2156 O OE1   . GLU A 1 279 ? 3.10481   24.28600  18.79560  1.000 54.18267 ? 273  GLU A OE1   1 
ATOM   2157 O OE2   . GLU A 1 279 ? 2.45881   25.96917  17.53306  1.000 61.05028 ? 273  GLU A OE2   1 
ATOM   2158 N N     . GLY A 1 280 ? -1.62697  22.75815  16.16765  1.000 25.11634 ? 274  GLY A N     1 
ATOM   2159 C CA    . GLY A 1 280 ? -1.82928  21.32926  16.03206  1.000 24.46504 ? 274  GLY A CA    1 
ATOM   2160 C C     . GLY A 1 280 ? -1.67228  20.57114  17.33802  1.000 27.73292 ? 274  GLY A C     1 
ATOM   2161 O O     . GLY A 1 280 ? -1.03905  21.02338  18.29105  1.000 27.93434 ? 274  GLY A O     1 
ATOM   2162 N N     . GLY A 1 281 ? -2.25085  19.37263  17.36609  1.000 26.02831 ? 275  GLY A N     1 
ATOM   2163 C CA    . GLY A 1 281 ? -2.14379  18.42986  18.48820  1.000 25.17246 ? 275  GLY A CA    1 
ATOM   2164 C C     . GLY A 1 281 ? -3.49500  18.21801  19.14166  1.000 29.40881 ? 275  GLY A C     1 
ATOM   2165 O O     . GLY A 1 281 ? -4.24576  19.16037  19.39929  1.000 24.98308 ? 275  GLY A O     1 
ATOM   2166 N N     . GLY A 1 282 ? -3.80927  16.94715  19.43081  1.000 29.43288 ? 276  GLY A N     1 
ATOM   2167 C CA    . GLY A 1 282 ? -5.10122  16.63095  20.02864  1.000 28.54065 ? 276  GLY A CA    1 
ATOM   2168 C C     . GLY A 1 282 ? -5.20048  17.07842  21.48170  1.000 28.75772 ? 276  GLY A C     1 
ATOM   2169 O O     . GLY A 1 282 ? -6.17701  17.71129  21.88713  1.000 27.18794 ? 276  GLY A O     1 
ATOM   2170 N N     . PHE A 1 283 ? -4.20598  16.72849  22.29585  1.000 30.00593 ? 277  PHE A N     1 
ATOM   2171 C CA    . PHE A 1 283 ? -4.26233  17.17532  23.68058  1.000 25.11252 ? 277  PHE A CA    1 
ATOM   2172 C C     . PHE A 1 283 ? -4.16725  18.68964  23.75552  1.000 26.12611 ? 277  PHE A C     1 
ATOM   2173 O O     . PHE A 1 283 ? -4.77840  19.30684  24.63601  1.000 26.93764 ? 277  PHE A O     1 
ATOM   2174 C CB    . PHE A 1 283 ? -3.16846  16.49765  24.50835  1.000 26.13077 ? 277  PHE A CB    1 
ATOM   2175 C CG    . PHE A 1 283 ? -3.55165  15.09737  24.95267  1.000 33.81428 ? 277  PHE A CG    1 
ATOM   2176 C CD1   . PHE A 1 283 ? -4.57803  14.90386  25.85251  1.000 36.50859 ? 277  PHE A CD1   1 
ATOM   2177 C CD2   . PHE A 1 283 ? -2.91385  13.99074  24.42787  1.000 38.86218 ? 277  PHE A CD2   1 
ATOM   2178 C CE1   . PHE A 1 283 ? -4.93702  13.61343  26.25485  1.000 49.66961 ? 277  PHE A CE1   1 
ATOM   2179 C CE2   . PHE A 1 283 ? -3.27158  12.70352  24.81705  1.000 43.83832 ? 277  PHE A CE2   1 
ATOM   2180 C CZ    . PHE A 1 283 ? -4.28077  12.51796  25.73356  1.000 41.58222 ? 277  PHE A CZ    1 
ATOM   2181 N N     . ARG A 1 284 ? -3.44056  19.30630  22.82433  1.000 24.88126 ? 278  ARG A N     1 
ATOM   2182 C CA    . ARG A 1 284 ? -3.39075  20.76043  22.79820  1.000 24.89555 ? 278  ARG A CA    1 
ATOM   2183 C C     . ARG A 1 284 ? -4.78271  21.34019  22.62640  1.000 26.64966 ? 278  ARG A C     1 
ATOM   2184 O O     . ARG A 1 284 ? -5.19679  22.23867  23.36950  1.000 23.56945 ? 278  ARG A O     1 
ATOM   2185 C CB    . ARG A 1 284 ? -2.49375  21.25136  21.66683  1.000 23.92278 ? 278  ARG A CB    1 
ATOM   2186 C CG    . ARG A 1 284 ? -2.22935  22.75656  21.76335  1.000 27.62880 ? 278  ARG A CG    1 
ATOM   2187 C CD    . ARG A 1 284 ? -1.13339  23.21999  20.83825  1.000 28.11733 ? 278  ARG A CD    1 
ATOM   2188 N NE    . ARG A 1 284 ? 0.18996   23.11230  21.46883  1.000 28.67640 ? 278  ARG A NE    1 
ATOM   2189 C CZ    . ARG A 1 284 ? 1.10048   22.16983  21.24126  1.000 30.89358 ? 278  ARG A CZ    1 
ATOM   2190 N NH1   . ARG A 1 284 ? 0.96813   21.29308  20.26148  1.000 31.43588 ? 278  ARG A NH1   1 
ATOM   2191 N NH2   . ARG A 1 284 ? 2.20073   22.13855  21.98838  1.000 35.54984 ? 278  ARG A NH2   1 
ATOM   2192 N N     . PHE A 1 285 ? -5.51812  20.84029  21.63934  1.000 26.96265 ? 279  PHE A N     1 
ATOM   2193 C CA    . PHE A 1 285 ? -6.82967  21.41743  21.36325  1.000 23.13295 ? 279  PHE A CA    1 
ATOM   2194 C C     . PHE A 1 285 ? -7.77042  21.23325  22.54726  1.000 25.54921 ? 279  PHE A C     1 
ATOM   2195 O O     . PHE A 1 285 ? -8.59901  22.11002  22.83213  1.000 31.29548 ? 279  PHE A O     1 
ATOM   2196 C CB    . PHE A 1 285 ? -7.40744  20.80085  20.08373  1.000 22.63262 ? 279  PHE A CB    1 
ATOM   2197 C CG    . PHE A 1 285 ? -8.66318  21.46421  19.62841  1.000 27.73919 ? 279  PHE A CG    1 
ATOM   2198 C CD1   . PHE A 1 285 ? -8.61301  22.56094  18.78935  1.000 23.95804 ? 279  PHE A CD1   1 
ATOM   2199 C CD2   . PHE A 1 285 ? -9.89752  20.98778  20.03620  1.000 27.29285 ? 279  PHE A CD2   1 
ATOM   2200 C CE1   . PHE A 1 285 ? -9.79292  23.21473  18.38560  1.000 24.42162 ? 279  PHE A CE1   1 
ATOM   2201 C CE2   . PHE A 1 285 ? -11.07839 21.62697  19.63266  1.000 27.05891 ? 279  PHE A CE2   1 
ATOM   2202 C CZ    . PHE A 1 285 ? -11.02406 22.73263  18.79249  1.000 24.93108 ? 279  PHE A CZ    1 
ATOM   2203 N N     . MET A 1 286 ? -7.64041  20.12040  23.25884  1.000 25.47683 ? 280  MET A N     1 
ATOM   2204 C CA    . MET A 1 286 ? -8.56112  19.74948  24.32607  1.000 27.94112 ? 280  MET A CA    1 
ATOM   2205 C C     . MET A 1 286 ? -8.20992  20.39085  25.66669  1.000 33.17174 ? 280  MET A C     1 
ATOM   2206 O O     . MET A 1 286 ? -9.11730  20.68117  26.46287  1.000 31.73868 ? 280  MET A O     1 
ATOM   2207 C CB    . MET A 1 286 ? -8.58841  18.21543  24.41752  1.000 32.09582 ? 280  MET A CB    1 
ATOM   2208 C CG    . MET A 1 286 ? -9.94560  17.58620  24.70708  1.000 45.90170 ? 280  MET A CG    1 
ATOM   2209 S SD    . MET A 1 286 ? -9.88901  15.88570  25.37184  1.000 48.81725 ? 280  MET A SD    1 
ATOM   2210 C CE    . MET A 1 286 ? -10.57710 15.02022  23.96684  1.000 48.67719 ? 280  MET A CE    1 
ATOM   2211 N N     . PHE A 1 287 ? -6.92489  20.65753  25.92677  1.000 28.80295 ? 281  PHE A N     1 
ATOM   2212 C CA    . PHE A 1 287 ? -6.49750  21.03548  27.26872  1.000 27.19203 ? 281  PHE A CA    1 
ATOM   2213 C C     . PHE A 1 287 ? -5.62029  22.28488  27.34736  1.000 28.65880 ? 281  PHE A C     1 
ATOM   2214 O O     . PHE A 1 287 ? -5.40590  22.78592  28.45573  1.000 29.33969 ? 281  PHE A O     1 
ATOM   2215 C CB    . PHE A 1 287 ? -5.77953  19.85456  27.95185  1.000 26.67321 ? 281  PHE A CB    1 
ATOM   2216 C CG    . PHE A 1 287 ? -6.67689  18.65271  28.18963  1.000 29.77352 ? 281  PHE A CG    1 
ATOM   2217 C CD1   . PHE A 1 287 ? -7.75771  18.74221  29.06065  1.000 31.96881 ? 281  PHE A CD1   1 
ATOM   2218 C CD2   . PHE A 1 287 ? -6.44056  17.44765  27.53725  1.000 28.32341 ? 281  PHE A CD2   1 
ATOM   2219 C CE1   . PHE A 1 287 ? -8.58942  17.65932  29.28685  1.000 33.54224 ? 281  PHE A CE1   1 
ATOM   2220 C CE2   . PHE A 1 287 ? -7.27576  16.33704  27.74992  1.000 31.69440 ? 281  PHE A CE2   1 
ATOM   2221 C CZ    . PHE A 1 287 ? -8.34691  16.44396  28.62926  1.000 37.05034 ? 281  PHE A CZ    1 
ATOM   2222 N N     . GLU A 1 288 ? -5.11695  22.81196  26.23768  1.000 27.32992 ? 282  GLU A N     1 
ATOM   2223 C CA    . GLU A 1 288 ? -4.35927  24.06160  26.28131  1.000 28.57318 ? 282  GLU A CA    1 
ATOM   2224 C C     . GLU A 1 288 ? -5.24447  25.25691  25.95108  1.000 30.50125 ? 282  GLU A C     1 
ATOM   2225 O O     . GLU A 1 288 ? -4.87185  26.40127  26.23187  1.000 32.85741 ? 282  GLU A O     1 
ATOM   2226 C CB    . GLU A 1 288 ? -3.17339  23.99450  25.29885  1.000 25.68358 ? 282  GLU A CB    1 
ATOM   2227 C CG    . GLU A 1 288 ? -2.33152  25.28562  25.15931  1.000 29.60612 ? 282  GLU A CG    1 
ATOM   2228 C CD    . GLU A 1 288 ? -1.01069  25.05493  24.45752  1.000 27.06013 ? 282  GLU A CD    1 
ATOM   2229 O OE1   . GLU A 1 288 ? -0.08573  24.50917  25.07833  1.000 29.82325 ? 282  GLU A OE1   1 
ATOM   2230 O OE2   . GLU A 1 288 ? -0.90817  25.39398  23.25987  1.000 31.78320 ? 282  GLU A OE2   1 
ATOM   2231 N N     . THR A 1 289 ? -6.39117  25.00125  25.33110  1.000 27.73215 ? 283  THR A N     1 
ATOM   2232 C CA    . THR A 1 289 ? -7.36690  26.05026  25.02866  1.000 29.18939 ? 283  THR A CA    1 
ATOM   2233 C C     . THR A 1 289 ? -8.09320  26.50833  26.28839  1.000 28.92091 ? 283  THR A C     1 
ATOM   2234 O O     . THR A 1 289 ? -8.05968  27.68554  26.65239  1.000 30.57393 ? 283  THR A O     1 
ATOM   2235 C CB    . THR A 1 289 ? -8.36413  25.51500  24.00389  1.000 28.41036 ? 283  THR A CB    1 
ATOM   2236 O OG1   . THR A 1 289 ? -8.87707  24.25403  24.47704  1.000 26.85529 ? 283  THR A OG1   1 
ATOM   2237 C CG2   . THR A 1 289 ? -7.68765  25.33855  22.66161  1.000 29.36246 ? 283  THR A CG2   1 
ATOM   2238 N N     . PHE A 1 290 ? -8.75587  25.58320  26.96395  1.000 31.68246 ? 284  PHE A N     1 
ATOM   2239 C CA    . PHE A 1 290 ? -9.58765  25.89572  28.11208  1.000 32.06835 ? 284  PHE A CA    1 
ATOM   2240 C C     . PHE A 1 290 ? -9.44999  24.76627  29.10978  1.000 35.53046 ? 284  PHE A C     1 
ATOM   2241 O O     . PHE A 1 290 ? -8.99054  23.67440  28.77280  1.000 37.65043 ? 284  PHE A O     1 
ATOM   2242 C CB    . PHE A 1 290 ? -11.06137 26.07707  27.70755  1.000 31.21456 ? 284  PHE A CB    1 
ATOM   2243 C CG    . PHE A 1 290 ? -11.28114 27.15809  26.70265  1.000 28.14535 ? 284  PHE A CG    1 
ATOM   2244 C CD1   . PHE A 1 290 ? -11.29491 28.48483  27.09698  1.000 29.40529 ? 284  PHE A CD1   1 
ATOM   2245 C CD2   . PHE A 1 290 ? -11.51112 26.85496  25.36552  1.000 31.14022 ? 284  PHE A CD2   1 
ATOM   2246 C CE1   . PHE A 1 290 ? -11.50828 29.50864  26.16934  1.000 34.14229 ? 284  PHE A CE1   1 
ATOM   2247 C CE2   . PHE A 1 290 ? -11.73165 27.86950  24.43868  1.000 29.80477 ? 284  PHE A CE2   1 
ATOM   2248 C CZ    . PHE A 1 290 ? -11.72170 29.21048  24.85947  1.000 35.75693 ? 284  PHE A CZ    1 
ATOM   2249 N N     . GLY A 1 291 ? -9.88306  25.01165  30.34246  1.000 32.63716 ? 285  GLY A N     1 
ATOM   2250 C CA    . GLY A 1 291 ? -9.69118  24.03016  31.38380  1.000 29.22874 ? 285  GLY A CA    1 
ATOM   2251 C C     . GLY A 1 291 ? -10.85674 23.13129  31.69169  1.000 32.48554 ? 285  GLY A C     1 
ATOM   2252 O O     . GLY A 1 291 ? -10.71604 22.25498  32.54774  1.000 40.44961 ? 285  GLY A O     1 
ATOM   2253 N N     . ASP A 1 292 ? -12.00688 23.29241  31.01803  1.000 30.55483 ? 286  ASP A N     1 
ATOM   2254 C CA    . ASP A 1 292 ? -13.19740 22.53484  31.40041  1.000 36.48420 ? 286  ASP A CA    1 
ATOM   2255 C C     . ASP A 1 292 ? -13.85512 21.80580  30.22802  1.000 33.23398 ? 286  ASP A C     1 
ATOM   2256 O O     . ASP A 1 292 ? -15.01566 21.40307  30.33586  1.000 36.25894 ? 286  ASP A O     1 
ATOM   2257 C CB    . ASP A 1 292 ? -14.21548 23.45315  32.09476  1.000 40.19109 ? 286  ASP A CB    1 
ATOM   2258 C CG    . ASP A 1 292 ? -14.60649 24.65204  31.24771  1.000 40.08632 ? 286  ASP A CG    1 
ATOM   2259 O OD1   . ASP A 1 292 ? -13.94386 24.91186  30.22123  1.000 41.77768 ? 286  ASP A OD1   1 
ATOM   2260 O OD2   . ASP A 1 292 ? -15.57456 25.35633  31.61872  1.000 41.77885 ? 286  ASP A OD2   1 
ATOM   2261 N N     . ILE A 1 293 ? -13.12270 21.55689  29.14032  1.000 34.46457 ? 287  ILE A N     1 
ATOM   2262 C CA    . ILE A 1 293 ? -13.72397 20.92442  27.96379  1.000 28.54287 ? 287  ILE A CA    1 
ATOM   2263 C C     . ILE A 1 293 ? -14.13888 19.48585  28.25229  1.000 32.82129 ? 287  ILE A C     1 
ATOM   2264 O O     . ILE A 1 293 ? -15.15953 19.00430  27.73204  1.000 33.51396 ? 287  ILE A O     1 
ATOM   2265 C CB    . ILE A 1 293 ? -12.73557 21.02842  26.78979  1.000 31.87934 ? 287  ILE A CB    1 
ATOM   2266 C CG1   . ILE A 1 293 ? -12.70940 22.47983  26.32975  1.000 35.33762 ? 287  ILE A CG1   1 
ATOM   2267 C CG2   . ILE A 1 293 ? -13.16935 20.11434  25.62776  1.000 31.01248 ? 287  ILE A CG2   1 
ATOM   2268 C CD1   . ILE A 1 293 ? -11.71583 22.78140  25.21788  1.000 30.86518 ? 287  ILE A CD1   1 
ATOM   2269 N N     . ALA A 1 294 ? -13.38877 18.78064  29.09764  1.000 32.84877 ? 288  ALA A N     1 
ATOM   2270 C CA    . ALA A 1 294 ? -13.67778 17.39502  29.44088  1.000 34.35641 ? 288  ALA A CA    1 
ATOM   2271 C C     . ALA A 1 294 ? -14.57230 17.26165  30.67454  1.000 37.25430 ? 288  ALA A C     1 
ATOM   2272 O O     . ALA A 1 294 ? -14.81110 16.13966  31.13882  1.000 39.12131 ? 288  ALA A O     1 
ATOM   2273 C CB    . ALA A 1 294 ? -12.36748 16.62789  29.65140  1.000 39.94113 ? 288  ALA A CB    1 
ATOM   2274 N N     . VAL A 1 295 ? -15.09539 18.37611  31.18589  1.000 39.06677 ? 289  VAL A N     1 
ATOM   2275 C CA    . VAL A 1 295 ? -15.77104 18.41632  32.47633  1.000 42.21647 ? 289  VAL A CA    1 
ATOM   2276 C C     . VAL A 1 295 ? -17.17476 19.00355  32.35170  1.000 44.47076 ? 289  VAL A C     1 
ATOM   2277 O O     . VAL A 1 295 ? -18.13315 18.47120  32.92489  1.000 45.57580 ? 289  VAL A O     1 
ATOM   2278 C CB    . VAL A 1 295 ? -14.92872 19.21714  33.48061  1.000 42.91998 ? 289  VAL A CB    1 
ATOM   2279 C CG1   . VAL A 1 295 ? -15.73937 19.51356  34.71852  1.000 46.74076 ? 289  VAL A CG1   1 
ATOM   2280 C CG2   . VAL A 1 295 ? -13.66958 18.44252  33.81483  1.000 37.61135 ? 289  VAL A CG2   1 
ATOM   2281 N N     . ASP A 1 296 ? -17.30020 20.09225  31.59926  1.000 38.99384 ? 290  ASP A N     1 
ATOM   2282 C CA    . ASP A 1 296 ? -18.55044 20.83104  31.42809  1.000 41.96355 ? 290  ASP A CA    1 
ATOM   2283 C C     . ASP A 1 296 ? -19.15742 20.56467  30.05093  1.000 46.45646 ? 290  ASP A C     1 
ATOM   2284 O O     . ASP A 1 296 ? -18.52539 20.84088  29.02207  1.000 39.91417 ? 290  ASP A O     1 
ATOM   2285 C CB    . ASP A 1 296 ? -18.29990 22.32350  31.62733  1.000 43.56652 ? 290  ASP A CB    1 
ATOM   2286 C CG    . ASP A 1 296 ? -19.57521 23.12815  31.67622  1.000 49.26211 ? 290  ASP A CG    1 
ATOM   2287 O OD1   . ASP A 1 296 ? -20.28455 23.07351  32.70787  1.000 57.23601 ? 290  ASP A OD1   1 
ATOM   2288 O OD2   . ASP A 1 296 ? -19.85509 23.82272  30.67048  1.000 46.59704 ? 290  ASP A OD2   1 
ATOM   2289 N N     . GLU A 1 297 ? -20.39848 20.06339  30.03689  1.000 45.76616 ? 291  GLU A N     1 
ATOM   2290 C CA    . GLU A 1 297 ? -21.07749 19.75568  28.77521  1.000 43.38207 ? 291  GLU A CA    1 
ATOM   2291 C C     . GLU A 1 297 ? -21.14793 20.97164  27.86206  1.000 40.64679 ? 291  GLU A C     1 
ATOM   2292 O O     . GLU A 1 297 ? -20.92667 20.86396  26.65073  1.000 38.52535 ? 291  GLU A O     1 
ATOM   2293 C CB    . GLU A 1 297 ? -22.49445 19.23690  29.03498  1.000 47.70360 ? 291  GLU A CB    1 
ATOM   2294 C CG    . GLU A 1 297 ? -22.61387 17.73234  29.23277  1.000 59.65963 ? 291  GLU A CG    1 
ATOM   2295 C CD    . GLU A 1 297 ? -22.87593 17.36523  30.68640  1.000 73.18477 ? 291  GLU A CD    1 
ATOM   2296 O OE1   . GLU A 1 297 ? -22.55360 18.19035  31.56916  1.000 75.79794 ? 291  GLU A OE1   1 
ATOM   2297 O OE2   . GLU A 1 297 ? -23.38094 16.24853  30.95234  1.000 73.95872 ? 291  GLU A OE2   1 
ATOM   2298 N N     . THR A 1 298 ? -21.49909 22.13572  28.41086  1.000 38.83719 ? 292  THR A N     1 
ATOM   2299 C CA    . THR A 1 298 ? -21.61905 23.31123  27.56010  1.000 37.57646 ? 292  THR A CA    1 
ATOM   2300 C C     . THR A 1 298 ? -20.27939 23.67980  26.94402  1.000 39.68447 ? 292  THR A C     1 
ATOM   2301 O O     . THR A 1 298 ? -20.20209 24.04437  25.76247  1.000 38.41081 ? 292  THR A O     1 
ATOM   2302 C CB    . THR A 1 298 ? -22.19475 24.48601  28.34657  1.000 44.42365 ? 292  THR A CB    1 
ATOM   2303 O OG1   . THR A 1 298 ? -23.56251 24.20444  28.65586  1.000 44.21847 ? 292  THR A OG1   1 
ATOM   2304 C CG2   . THR A 1 298 ? -22.12705 25.75607  27.51003  1.000 43.99319 ? 292  THR A CG2   1 
ATOM   2305 N N     . ALA A 1 299 ? -19.20993 23.59100  27.72895  1.000 36.31351 ? 293  ALA A N     1 
ATOM   2306 C CA    . ALA A 1 299 ? -17.88531 23.82474  27.17886  1.000 37.66003 ? 293  ALA A CA    1 
ATOM   2307 C C     . ALA A 1 299 ? -17.55541 22.78515  26.11110  1.000 29.17995 ? 293  ALA A C     1 
ATOM   2308 O O     . ALA A 1 299 ? -17.03121 23.11907  25.04891  1.000 33.98454 ? 293  ALA A O     1 
ATOM   2309 C CB    . ALA A 1 299 ? -16.84544 23.79688  28.29658  1.000 34.69274 ? 293  ALA A CB    1 
ATOM   2310 N N     . ASN A 1 300 ? -17.83813 21.51526  26.39157  1.000 32.13871 ? 294  ASN A N     1 
ATOM   2311 C CA    . ASN A 1 300 ? -17.56835 20.45376  25.42408  1.000 31.13218 ? 294  ASN A CA    1 
ATOM   2312 C C     . ASN A 1 300 ? -18.28061 20.70363  24.09830  1.000 37.87528 ? 294  ASN A C     1 
ATOM   2313 O O     . ASN A 1 300 ? -17.74248 20.40348  23.02393  1.000 30.81400 ? 294  ASN A O     1 
ATOM   2314 C CB    . ASN A 1 300 ? -17.98690 19.10851  26.00293  1.000 30.13295 ? 294  ASN A CB    1 
ATOM   2315 C CG    . ASN A 1 300 ? -17.40736 17.93377  25.23309  1.000 35.58925 ? 294  ASN A CG    1 
ATOM   2316 O OD1   . ASN A 1 300 ? -18.00438 17.47798  24.26758  1.000 32.40818 ? 294  ASN A OD1   1 
ATOM   2317 N ND2   . ASN A 1 300 ? -16.28376 17.39331  25.70157  1.000 32.74389 ? 294  ASN A ND2   1 
ATOM   2318 N N     . ILE A 1 301 ? -19.50785 21.22598  24.14827  1.000 36.95125 ? 295  ILE A N     1 
ATOM   2319 C CA    . ILE A 1 301 ? -20.22758 21.46018  22.90138  1.000 34.09756 ? 295  ILE A CA    1 
ATOM   2320 C C     . ILE A 1 301 ? -19.55240 22.55105  22.07418  1.000 29.33192 ? 295  ILE A C     1 
ATOM   2321 O O     . ILE A 1 301 ? -19.52185 22.46700  20.84065  1.000 29.95608 ? 295  ILE A O     1 
ATOM   2322 C CB    . ILE A 1 301 ? -21.71043 21.78491  23.17561  1.000 34.98859 ? 295  ILE A CB    1 
ATOM   2323 C CG1   . ILE A 1 301 ? -22.44718 20.52167  23.63100  1.000 38.99005 ? 295  ILE A CG1   1 
ATOM   2324 C CG2   . ILE A 1 301 ? -22.33744 22.42033  21.93457  1.000 34.34540 ? 295  ILE A CG2   1 
ATOM   2325 C CD1   . ILE A 1 301 ? -23.82865 20.79703  24.25799  1.000 35.15214 ? 295  ILE A CD1   1 
ATOM   2326 N N     . GLU A 1 302 ? -18.98839 23.58374  22.71728  1.000 30.92241 ? 296  GLU A N     1 
ATOM   2327 C CA    . GLU A 1 302 ? -18.25580 24.60270  21.94969  1.000 28.68912 ? 296  GLU A CA    1 
ATOM   2328 C C     . GLU A 1 302 ? -17.05943 24.00138  21.20937  1.000 33.76209 ? 296  GLU A C     1 
ATOM   2329 O O     . GLU A 1 302 ? -16.70026 24.45176  20.11007  1.000 29.84906 ? 296  GLU A O     1 
ATOM   2330 C CB    . GLU A 1 302 ? -17.73861 25.71173  22.85483  1.000 31.60766 ? 296  GLU A CB    1 
ATOM   2331 C CG    . GLU A 1 302 ? -18.81040 26.50232  23.49254  1.000 41.72534 ? 296  GLU A CG    1 
ATOM   2332 C CD    . GLU A 1 302 ? -19.59292 27.24991  22.46368  1.000 39.39132 ? 296  GLU A CD    1 
ATOM   2333 O OE1   . GLU A 1 302 ? -18.97150 28.04184  21.71398  1.000 37.34569 ? 296  GLU A OE1   1 
ATOM   2334 O OE2   . GLU A 1 302 ? -20.81934 27.01089  22.39600  1.000 47.17447 ? 296  GLU A OE2   1 
ATOM   2335 N N     . ALA A 1 303 ? -16.37220 23.05041  21.84182  1.000 29.65831 ? 297  ALA A N     1 
ATOM   2336 C CA    . ALA A 1 303 ? -15.23953 22.40383  21.18722  1.000 25.96905 ? 297  ALA A CA    1 
ATOM   2337 C C     . ALA A 1 303 ? -15.71191 21.58612  19.98375  1.000 25.95274 ? 297  ALA A C     1 
ATOM   2338 O O     . ALA A 1 303 ? -15.15506 21.70722  18.88280  1.000 25.70979 ? 297  ALA A O     1 
ATOM   2339 C CB    . ALA A 1 303 ? -14.49676 21.52154  22.18950  1.000 29.79677 ? 297  ALA A CB    1 
ATOM   2340 N N     . GLN A 1 304 ? -16.77146 20.78448  20.17388  1.000 26.72598 ? 298  GLN A N     1 
ATOM   2341 C CA    . GLN A 1 304 ? -17.36584 20.02099  19.07617  1.000 25.83254 ? 298  GLN A CA    1 
ATOM   2342 C C     . GLN A 1 304 ? -17.71965 20.92380  17.90948  1.000 24.99133 ? 298  GLN A C     1 
ATOM   2343 O O     . GLN A 1 304 ? -17.39001 20.63468  16.75653  1.000 25.37984 ? 298  GLN A O     1 
ATOM   2344 C CB    . GLN A 1 304 ? -18.64656 19.30686  19.53330  1.000 29.86944 ? 298  GLN A CB    1 
ATOM   2345 C CG    . GLN A 1 304 ? -18.57462 18.41586  20.75241  1.000 36.55778 ? 298  GLN A CG    1 
ATOM   2346 C CD    . GLN A 1 304 ? -19.96975 17.99873  21.19946  1.000 37.03636 ? 298  GLN A CD    1 
ATOM   2347 O OE1   . GLN A 1 304 ? -20.94222 18.17799  20.45454  1.000 41.08571 ? 298  GLN A OE1   1 
ATOM   2348 N NE2   . GLN A 1 304 ? -20.08052 17.45146  22.39950  1.000 33.81573 ? 298  GLN A NE2   1 
ATOM   2349 N N     . ASN A 1 305 ? -18.45252 22.00800  18.19024  1.000 27.16408 ? 299  ASN A N     1 
ATOM   2350 C CA    . ASN A 1 305 ? -18.94513 22.86413  17.12578  1.000 27.41839 ? 299  ASN A CA    1 
ATOM   2351 C C     . ASN A 1 305 ? -17.80465 23.50738  16.34573  1.000 27.10219 ? 299  ASN A C     1 
ATOM   2352 O O     . ASN A 1 305 ? -17.92147 23.72488  15.13017  1.000 24.37976 ? 299  ASN A O     1 
ATOM   2353 C CB    . ASN A 1 305 ? -19.86102 23.93165  17.72058  1.000 28.33741 ? 299  ASN A CB    1 
ATOM   2354 C CG    . ASN A 1 305 ? -21.19541 23.36349  18.17597  1.000 31.62890 ? 299  ASN A CG    1 
ATOM   2355 O OD1   . ASN A 1 305 ? -21.52112 22.18934  17.93608  1.000 28.99661 ? 299  ASN A OD1   1 
ATOM   2356 N ND2   . ASN A 1 305 ? -21.94940 24.18475  18.89539  1.000 35.39531 ? 299  ASN A ND2   1 
ATOM   2357 N N     . PHE A 1 306 ? -16.69033 23.81788  17.01708  1.000 25.27095 ? 300  PHE A N     1 
ATOM   2358 C CA    . PHE A 1 306 ? -15.56058 24.36636  16.28335  1.000 24.35203 ? 300  PHE A CA    1 
ATOM   2359 C C     . PHE A 1 306 ? -15.04583 23.35689  15.26714  1.000 24.04017 ? 300  PHE A C     1 
ATOM   2360 O O     . PHE A 1 306 ? -14.74764 23.72125  14.12272  1.000 25.04528 ? 300  PHE A O     1 
ATOM   2361 C CB    . PHE A 1 306 ? -14.42403 24.78479  17.23142  1.000 24.81487 ? 300  PHE A CB    1 
ATOM   2362 C CG    . PHE A 1 306 ? -13.28544 25.47954  16.53076  1.000 25.72054 ? 300  PHE A CG    1 
ATOM   2363 C CD1   . PHE A 1 306 ? -12.25609 24.75142  15.93431  1.000 26.03639 ? 300  PHE A CD1   1 
ATOM   2364 C CD2   . PHE A 1 306 ? -13.23233 26.85889  16.45346  1.000 27.05778 ? 300  PHE A CD2   1 
ATOM   2365 C CE1   . PHE A 1 306 ? -11.21960 25.39859  15.28570  1.000 25.99139 ? 300  PHE A CE1   1 
ATOM   2366 C CE2   . PHE A 1 306 ? -12.20852 27.50059  15.79748  1.000 27.42667 ? 300  PHE A CE2   1 
ATOM   2367 C CZ    . PHE A 1 306 ? -11.19020 26.78235  15.22948  1.000 26.55401 ? 300  PHE A CZ    1 
ATOM   2368 N N     . ILE A 1 307 ? -14.92087 22.09551  15.67537  1.000 23.78168 ? 301  ILE A N     1 
ATOM   2369 C CA    . ILE A 1 307 ? -14.37795 21.08284  14.77204  1.000 25.33872 ? 301  ILE A CA    1 
ATOM   2370 C C     . ILE A 1 307 ? -15.38245 20.76615  13.66297  1.000 24.13456 ? 301  ILE A C     1 
ATOM   2371 O O     . ILE A 1 307 ? -15.01043 20.61616  12.49085  1.000 21.83314 ? 301  ILE A O     1 
ATOM   2372 C CB    . ILE A 1 307 ? -13.96603 19.81970  15.54683  1.000 24.04882 ? 301  ILE A CB    1 
ATOM   2373 C CG1   . ILE A 1 307 ? -12.89455 20.16148  16.57235  1.000 25.13136 ? 301  ILE A CG1   1 
ATOM   2374 C CG2   . ILE A 1 307 ? -13.43926 18.72749  14.57895  1.000 21.83782 ? 301  ILE A CG2   1 
ATOM   2375 C CD1   . ILE A 1 307 ? -12.58968 18.97925  17.53411  1.000 25.65618 ? 301  ILE A CD1   1 
ATOM   2376 N N     . LYS A 1 308 ? -16.67512 20.69760  14.00012  1.000 23.44151 ? 302  LYS A N     1 
ATOM   2377 C CA    . LYS A 1 308 ? -17.68457 20.48343  12.95582  1.000 25.35485 ? 302  LYS A CA    1 
ATOM   2378 C C     . LYS A 1 308 ? -17.65606 21.60433  11.92560  1.000 26.30796 ? 302  LYS A C     1 
ATOM   2379 O O     . LYS A 1 308 ? -17.87881 21.37231  10.73046  1.000 24.10520 ? 302  LYS A O     1 
ATOM   2380 C CB    . LYS A 1 308 ? -19.08638 20.38560  13.57915  1.000 31.43585 ? 302  LYS A CB    1 
ATOM   2381 C CG    . LYS A 1 308 ? -19.30333 19.20619  14.46751  1.000 32.93693 ? 302  LYS A CG    1 
ATOM   2382 C CD    . LYS A 1 308 ? -20.73545 19.17120  15.03425  1.000 33.38984 ? 302  LYS A CD    1 
ATOM   2383 C CE    . LYS A 1 308 ? -20.92852 17.91575  15.88004  1.000 39.50091 ? 302  LYS A CE    1 
ATOM   2384 N NZ    . LYS A 1 308 ? -22.27526 17.80648  16.52002  1.000 42.50665 ? 302  LYS A NZ    1 
ATOM   2385 N N     . LYS A 1 309 ? -17.39574 22.83376  12.36469  1.000 25.65680 ? 303  LYS A N     1 
ATOM   2386 C CA    . LYS A 1 309 ? -17.35105 23.90908  11.39098  1.000 25.35745 ? 303  LYS A CA    1 
ATOM   2387 C C     . LYS A 1 309 ? -16.13231 23.76452  10.48895  1.000 26.20502 ? 303  LYS A C     1 
ATOM   2388 O O     . LYS A 1 309 ? -16.22767 23.98528  9.27776   1.000 24.71451 ? 303  LYS A O     1 
ATOM   2389 C CB    . LYS A 1 309 ? -17.36943 25.27401  12.08948  1.000 28.38599 ? 303  LYS A CB    1 
ATOM   2390 C CG    . LYS A 1 309 ? -17.09017 26.40607  11.11237  1.000 31.55475 ? 303  LYS A CG    1 
ATOM   2391 C CD    . LYS A 1 309 ? -16.69948 27.75868  11.76263  1.000 46.21136 ? 303  LYS A CD    1 
ATOM   2392 C CE    . LYS A 1 309 ? -15.81036 27.67722  13.02221  1.000 52.77977 ? 303  LYS A CE    1 
ATOM   2393 N NZ    . LYS A 1 309 ? -14.64171 26.71154  12.99518  1.000 52.94267 ? 303  LYS A NZ    1 
ATOM   2394 N N     . LYS A 1 310 ? -14.99137 23.33825  11.05015  1.000 26.29001 ? 304  LYS A N     1 
ATOM   2395 C CA    . LYS A 1 310 ? -13.83018 23.05371  10.20766  1.000 24.53152 ? 304  LYS A CA    1 
ATOM   2396 C C     . LYS A 1 310 ? -14.13954 21.96197  9.18928   1.000 24.18117 ? 304  LYS A C     1 
ATOM   2397 O O     . LYS A 1 310 ? -13.79173 22.09726  8.00516   1.000 25.87563 ? 304  LYS A O     1 
ATOM   2398 C CB    . LYS A 1 310 ? -12.64428 22.63535  11.08133  1.000 23.58193 ? 304  LYS A CB    1 
ATOM   2399 C CG    . LYS A 1 310 ? -12.09563 23.80206  11.91412  1.000 23.08358 ? 304  LYS A CG    1 
ATOM   2400 C CD    . LYS A 1 310 ? -11.40297 24.80936  10.99093  1.000 28.11217 ? 304  LYS A CD    1 
ATOM   2401 C CE    . LYS A 1 310 ? -10.60786 25.82941  11.78919  1.000 28.42552 ? 304  LYS A CE    1 
ATOM   2402 N NZ    . LYS A 1 310 ? -9.87099  26.74890  10.87088  1.000 33.58446 ? 304  LYS A NZ    1 
ATOM   2403 N N     . ILE A 1 311 ? -14.79479 20.86888  9.62785   1.000 21.64915 ? 305  ILE A N     1 
ATOM   2404 C CA    . ILE A 1 311 ? -15.14352 19.79757  8.69208   1.000 20.54951 ? 305  ILE A CA    1 
ATOM   2405 C C     . ILE A 1 311 ? -15.95925 20.35539  7.53598   1.000 28.04108 ? 305  ILE A C     1 
ATOM   2406 O O     . ILE A 1 311 ? -15.68743 20.06638  6.35680   1.000 22.34205 ? 305  ILE A O     1 
ATOM   2407 C CB    . ILE A 1 311 ? -15.90979 18.66574  9.40409   1.000 24.60766 ? 305  ILE A CB    1 
ATOM   2408 C CG1   . ILE A 1 311 ? -14.99797 17.94485  10.42360  1.000 22.89792 ? 305  ILE A CG1   1 
ATOM   2409 C CG2   . ILE A 1 311 ? -16.50463 17.66768  8.35260   1.000 24.01303 ? 305  ILE A CG2   1 
ATOM   2410 C CD1   . ILE A 1 311 ? -15.72489 16.97198  11.38024  1.000 24.70197 ? 305  ILE A CD1   1 
ATOM   2411 N N     . SER A 1 312 ? -16.98544 21.15455  7.86188   1.000 23.57821 ? 306  SER A N     1 
ATOM   2412 C CA    . SER A 1 312 ? -17.85692 21.71763  6.83445   1.000 26.03944 ? 306  SER A CA    1 
ATOM   2413 C C     . SER A 1 312 ? -17.11626 22.69097  5.93289   1.000 23.66286 ? 306  SER A C     1 
ATOM   2414 O O     . SER A 1 312 ? -17.51294 22.87169  4.78040   1.000 27.53708 ? 306  SER A O     1 
ATOM   2415 C CB    . SER A 1 312 ? -19.05294 22.44254  7.47796   1.000 30.06873 ? 306  SER A CB    1 
ATOM   2416 O OG    . SER A 1 312 ? -18.63400 23.70548  7.99309   1.000 33.67322 ? 306  SER A OG    1 
ATOM   2417 N N     . GLU A 1 313 ? -16.05144 23.35546  6.42228   1.000 25.70501 ? 307  GLU A N     1 
ATOM   2418 C CA    . GLU A 1 313 ? -15.28235 24.20710  5.50799   1.000 23.94688 ? 307  GLU A CA    1 
ATOM   2419 C C     . GLU A 1 313 ? -14.30904 23.41183  4.62932   1.000 24.51032 ? 307  GLU A C     1 
ATOM   2420 O O     . GLU A 1 313 ? -14.10154 23.76382  3.46442   1.000 26.66577 ? 307  GLU A O     1 
ATOM   2421 C CB    . GLU A 1 313 ? -14.51417 25.28641  6.28414   1.000 26.05148 ? 307  GLU A CB    1 
ATOM   2422 C CG    . GLU A 1 313 ? -15.44112 26.18175  7.09534   1.000 34.73473 ? 307  GLU A CG    1 
ATOM   2423 C CD    . GLU A 1 313 ? -14.71183 27.05268  8.12264   1.000 46.39562 ? 307  GLU A CD    1 
ATOM   2424 O OE1   . GLU A 1 313 ? -15.36842 27.94899  8.68816   1.000 46.10228 ? 307  GLU A OE1   1 
ATOM   2425 O OE2   . GLU A 1 313 ? -13.49578 26.84710  8.36233   1.000 43.04160 ? 307  GLU A OE2   1 
ATOM   2426 N N     . ILE A 1 314 ? -13.66500 22.38054  5.17778   1.000 22.56855 ? 308  ILE A N     1 
ATOM   2427 C CA    . ILE A 1 314 ? -12.65801 21.63612  4.41663   1.000 24.88511 ? 308  ILE A CA    1 
ATOM   2428 C C     . ILE A 1 314 ? -13.31408 20.77159  3.33956   1.000 25.40337 ? 308  ILE A C     1 
ATOM   2429 O O     . ILE A 1 314 ? -12.88303 20.74559  2.17820   1.000 25.38751 ? 308  ILE A O     1 
ATOM   2430 C CB    . ILE A 1 314 ? -11.79431 20.79685  5.37644   1.000 23.92901 ? 308  ILE A CB    1 
ATOM   2431 C CG1   . ILE A 1 314 ? -10.97652 21.71931  6.28747   1.000 23.40513 ? 308  ILE A CG1   1 
ATOM   2432 C CG2   . ILE A 1 314 ? -10.90047 19.78346  4.59752   1.000 24.51525 ? 308  ILE A CG2   1 
ATOM   2433 C CD1   . ILE A 1 314 ? -10.47673 21.05816  7.57109   1.000 23.43069 ? 308  ILE A CD1   1 
ATOM   2434 N N     . VAL A 1 315 ? -14.36043 20.05049  3.70637   1.000 20.73544 ? 309  VAL A N     1 
ATOM   2435 C CA    . VAL A 1 315 ? -14.95132 19.03441  2.84328   1.000 21.60582 ? 309  VAL A CA    1 
ATOM   2436 C C     . VAL A 1 315 ? -16.02032 19.72955  2.00970   1.000 23.81728 ? 309  VAL A C     1 
ATOM   2437 O O     . VAL A 1 315 ? -17.05978 20.11425  2.54516   1.000 25.26783 ? 309  VAL A O     1 
ATOM   2438 C CB    . VAL A 1 315 ? -15.54285 17.88823  3.67211   1.000 21.43124 ? 309  VAL A CB    1 
ATOM   2439 C CG1   . VAL A 1 315 ? -16.13633 16.81403  2.77529   1.000 20.60013 ? 309  VAL A CG1   1 
ATOM   2440 C CG2   . VAL A 1 315 ? -14.44821 17.28243  4.63074   1.000 19.55655 ? 309  VAL A CG2   1 
ATOM   2441 N N     . LYS A 1 316 ? -15.78079 19.85416  0.70205   1.000 21.78718 ? 310  LYS A N     1 
ATOM   2442 C CA    . LYS A 1 316 ? -16.58258 20.78332  -0.10953  1.000 29.33775 ? 310  LYS A CA    1 
ATOM   2443 C C     . LYS A 1 316 ? -17.98386 20.25152  -0.39759  1.000 31.32159 ? 310  LYS A C     1 
ATOM   2444 O O     . LYS A 1 316 ? -18.93538 21.03994  -0.51011  1.000 30.02849 ? 310  LYS A O     1 
ATOM   2445 C CB    . LYS A 1 316 ? -15.84873 21.09416  -1.40976  1.000 28.89667 ? 310  LYS A CB    1 
ATOM   2446 C CG    . LYS A 1 316 ? -14.52814 21.86931  -1.19967  1.000 31.43910 ? 310  LYS A CG    1 
ATOM   2447 C CD    . LYS A 1 316 ? -14.73970 22.97300  -0.16913  1.000 33.14941 ? 310  LYS A CD    1 
ATOM   2448 C CE    . LYS A 1 316 ? -13.59621 23.97897  -0.15303  1.000 40.37922 ? 310  LYS A CE    1 
ATOM   2449 N NZ    . LYS A 1 316 ? -12.33536 23.41861  0.41133   1.000 43.01862 ? 310  LYS A NZ    1 
ATOM   2450 N N     . ASP A 1 317 ? -18.13431 18.94543  -0.52213  1.000 24.17683 ? 311  ASP A N     1 
ATOM   2451 C CA    . ASP A 1 317 ? -19.44064 18.31728  -0.71805  1.000 25.22992 ? 311  ASP A CA    1 
ATOM   2452 C C     . ASP A 1 317 ? -20.17168 18.24819  0.62418   1.000 25.87084 ? 311  ASP A C     1 
ATOM   2453 O O     . ASP A 1 317 ? -19.75382 17.50065  1.51404   1.000 24.18739 ? 311  ASP A O     1 
ATOM   2454 C CB    . ASP A 1 317 ? -19.23657 16.92389  -1.34674  1.000 30.96529 ? 311  ASP A CB    1 
ATOM   2455 C CG    . ASP A 1 317 ? -20.55108 16.14940  -1.59044  1.000 35.84021 ? 311  ASP A CG    1 
ATOM   2456 O OD1   . ASP A 1 317 ? -21.44267 16.13144  -0.71677  1.000 30.89090 ? 311  ASP A OD1   1 
ATOM   2457 O OD2   . ASP A 1 317 ? -20.64588 15.46526  -2.63976  1.000 36.79082 ? 311  ASP A OD2   1 
ATOM   2458 N N     . PRO A 1 318 ? -21.26726 18.98898  0.82565   1.000 28.34018 ? 312  PRO A N     1 
ATOM   2459 C CA    . PRO A 1 318 ? -21.90327 18.98327  2.15939   1.000 24.78906 ? 312  PRO A CA    1 
ATOM   2460 C C     . PRO A 1 318 ? -22.44316 17.63967  2.58867   1.000 22.27146 ? 312  PRO A C     1 
ATOM   2461 O O     . PRO A 1 318 ? -22.64539 17.42292  3.79338   1.000 26.32080 ? 312  PRO A O     1 
ATOM   2462 C CB    . PRO A 1 318 ? -23.03645 20.02474  2.00659   1.000 28.40136 ? 312  PRO A CB    1 
ATOM   2463 C CG    . PRO A 1 318 ? -23.40075 19.90619  0.51501   1.000 27.52991 ? 312  PRO A CG    1 
ATOM   2464 C CD    . PRO A 1 318 ? -22.03634 19.80527  -0.14673  1.000 26.62709 ? 312  PRO A CD    1 
ATOM   2465 N N     . PHE A 1 319 ? -22.70374 16.72076  1.65583   1.000 20.76622 ? 313  PHE A N     1 
ATOM   2466 C CA    . PHE A 1 319 ? -23.27006 15.44074  2.04875   1.000 23.25417 ? 313  PHE A CA    1 
ATOM   2467 C C     . PHE A 1 319 ? -22.18054 14.50941  2.54734   1.000 23.77606 ? 313  PHE A C     1 
ATOM   2468 O O     . PHE A 1 319 ? -22.40187 13.73244  3.48437   1.000 22.68830 ? 313  PHE A O     1 
ATOM   2469 C CB    . PHE A 1 319 ? -24.03205 14.84993  0.86051   1.000 27.15779 ? 313  PHE A CB    1 
ATOM   2470 C CG    . PHE A 1 319 ? -25.04635 15.80708  0.31423   1.000 34.69092 ? 313  PHE A CG    1 
ATOM   2471 C CD1   . PHE A 1 319 ? -26.19084 16.11036  1.05123   1.000 38.80155 ? 313  PHE A CD1   1 
ATOM   2472 C CD2   . PHE A 1 319 ? -24.79344 16.50628  -0.86328  1.000 30.34380 ? 313  PHE A CD2   1 
ATOM   2473 C CE1   . PHE A 1 319 ? -27.11398 17.03847  0.58249   1.000 36.45932 ? 313  PHE A CE1   1 
ATOM   2474 C CE2   . PHE A 1 319 ? -25.71665 17.44234  -1.34802  1.000 39.45788 ? 313  PHE A CE2   1 
ATOM   2475 C CZ    . PHE A 1 319 ? -26.87876 17.70866  -0.61656  1.000 35.44965 ? 313  PHE A CZ    1 
ATOM   2476 N N     . VAL A 1 320 ? -20.99910 14.60964  1.94304   1.000 22.49155 ? 314  VAL A N     1 
ATOM   2477 C CA    . VAL A 1 320 ? -19.82413 13.92647  2.48390   1.000 21.45794 ? 314  VAL A CA    1 
ATOM   2478 C C     . VAL A 1 320 ? -19.42506 14.53716  3.82948   1.000 20.96463 ? 314  VAL A C     1 
ATOM   2479 O O     . VAL A 1 320 ? -19.14789 13.81385  4.79612   1.000 23.23483 ? 314  VAL A O     1 
ATOM   2480 C CB    . VAL A 1 320 ? -18.65998 13.98014  1.47155   1.000 24.60600 ? 314  VAL A CB    1 
ATOM   2481 C CG1   . VAL A 1 320 ? -17.39394 13.32477  2.08126   1.000 23.13785 ? 314  VAL A CG1   1 
ATOM   2482 C CG2   . VAL A 1 320 ? -19.02695 13.29157  0.16850   1.000 24.28889 ? 314  VAL A CG2   1 
ATOM   2483 N N     . ALA A 1 321 ? -19.39945 15.87848  3.92833   1.000 21.15918 ? 315  ALA A N     1 
ATOM   2484 C CA    . ALA A 1 321 ? -19.10421 16.52705  5.21044   1.000 22.42227 ? 315  ALA A CA    1 
ATOM   2485 C C     . ALA A 1 321 ? -20.04546 16.04331  6.32270   1.000 24.44748 ? 315  ALA A C     1 
ATOM   2486 O O     . ALA A 1 321 ? -19.61835 15.78030  7.45375   1.000 21.62202 ? 315  ALA A O     1 
ATOM   2487 C CB    . ALA A 1 321 ? -19.20594 18.04811  5.04807   1.000 22.27798 ? 315  ALA A CB    1 
ATOM   2488 N N     . LYS A 1 322 ? -21.34358 15.96426  6.02246   1.000 24.44325 ? 316  LYS A N     1 
ATOM   2489 C CA    . LYS A 1 322 ? -22.31794 15.46221  6.99276   1.000 26.43413 ? 316  LYS A CA    1 
ATOM   2490 C C     . LYS A 1 322 ? -21.95112 14.06927  7.47668   1.000 23.20207 ? 316  LYS A C     1 
ATOM   2491 O O     . LYS A 1 322 ? -21.99455 13.78041  8.67350   1.000 24.99561 ? 316  LYS A O     1 
ATOM   2492 C CB    . LYS A 1 322 ? -23.71220 15.44583  6.34254   1.000 24.85709 ? 316  LYS A CB    1 
ATOM   2493 C CG    . LYS A 1 322 ? -24.83810 15.02329  7.25226   1.000 32.85858 ? 316  LYS A CG    1 
ATOM   2494 C CD    . LYS A 1 322 ? -26.18020 15.46624  6.62028   1.000 40.77135 ? 316  LYS A CD    1 
ATOM   2495 C CE    . LYS A 1 322 ? -27.37015 15.21024  7.53667   1.000 46.08048 ? 316  LYS A CE    1 
ATOM   2496 N NZ    . LYS A 1 322 ? -28.66818 15.35279  6.80549   1.000 50.84755 ? 316  LYS A NZ    1 
ATOM   2497 N N     . LYS A 1 323 ? -21.62048 13.17036  6.54592   1.000 23.01751 ? 317  LYS A N     1 
ATOM   2498 C CA    . LYS A 1 323 ? -21.24535 11.80686  6.91057   1.000 23.59406 ? 317  LYS A CA    1 
ATOM   2499 C C     . LYS A 1 323 ? -20.01223 11.76619  7.81829   1.000 25.82294 ? 317  LYS A C     1 
ATOM   2500 O O     . LYS A 1 323 ? -19.90363 10.88135  8.67906   1.000 22.47877 ? 317  LYS A O     1 
ATOM   2501 C CB    . LYS A 1 323 ? -21.01195 11.01458  5.62811   1.000 24.39398 ? 317  LYS A CB    1 
ATOM   2502 C CG    . LYS A 1 323 ? -21.22334 9.52729   5.77010   1.000 30.79733 ? 317  LYS A CG    1 
ATOM   2503 C CD    . LYS A 1 323 ? -21.07242 8.85648   4.39929   1.000 28.23965 ? 317  LYS A CD    1 
ATOM   2504 C CE    . LYS A 1 323 ? -22.31156 8.94380   3.54479   1.000 29.30329 ? 317  LYS A CE    1 
ATOM   2505 N NZ    . LYS A 1 323 ? -22.06356 8.25434   2.18967   1.000 30.44904 ? 317  LYS A NZ    1 
ATOM   2506 N N     . LEU A 1 324 ? -19.09349 12.71858  7.66097   1.000 23.61232 ? 318  LEU A N     1 
ATOM   2507 C CA    . LEU A 1 324 ? -17.88278 12.74182  8.48455   1.000 22.60205 ? 318  LEU A CA    1 
ATOM   2508 C C     . LEU A 1 324 ? -18.08998 13.39204  9.82726   1.000 24.75475 ? 318  LEU A C     1 
ATOM   2509 O O     . LEU A 1 324 ? -17.13995 13.44499  10.61228  1.000 25.74373 ? 318  LEU A O     1 
ATOM   2510 C CB    . LEU A 1 324 ? -16.77437 13.52322  7.77453   1.000 20.87554 ? 318  LEU A CB    1 
ATOM   2511 C CG    . LEU A 1 324 ? -16.18753 12.80099  6.57971   1.000 21.10087 ? 318  LEU A CG    1 
ATOM   2512 C CD1   . LEU A 1 324 ? -15.54159 13.83123  5.66863   1.000 22.28533 ? 318  LEU A CD1   1 
ATOM   2513 C CD2   . LEU A 1 324 ? -15.10919 11.74775  7.07151   1.000 21.77823 ? 318  LEU A CD2   1 
ATOM   2514 N N     . THR A 1 325 ? -19.26955 13.96029  10.07640  1.000 24.15693 ? 319  THR A N     1 
ATOM   2515 C CA    . THR A 1 325 ? -19.47930 14.80017  11.23845  1.000 26.91202 ? 319  THR A CA    1 
ATOM   2516 C C     . THR A 1 325 ? -20.00790 13.95333  12.38607  1.000 24.46685 ? 319  THR A C     1 
ATOM   2517 O O     . THR A 1 325 ? -21.04761 13.28931  12.22966  1.000 25.34611 ? 319  THR A O     1 
ATOM   2518 C CB    . THR A 1 325 ? -20.43737 15.94343  10.91134  1.000 24.00714 ? 319  THR A CB    1 
ATOM   2519 O OG1   . THR A 1 325 ? -19.82512 16.77531  9.91887   1.000 28.99844 ? 319  THR A OG1   1 
ATOM   2520 C CG2   . THR A 1 325 ? -20.68261 16.80004  12.16614  1.000 27.09914 ? 319  THR A CG2   1 
ATOM   2521 N N     . PRO A 1 326 ? -19.32664 13.89873  13.52531  1.000 24.04006 ? 320  PRO A N     1 
ATOM   2522 C CA    . PRO A 1 326 ? -19.77139 13.01485  14.60254  1.000 28.21795 ? 320  PRO A CA    1 
ATOM   2523 C C     . PRO A 1 326 ? -21.08381 13.48737  15.19715  1.000 38.00832 ? 320  PRO A C     1 
ATOM   2524 O O     . PRO A 1 326 ? -21.51545 14.62339  15.00353  1.000 31.24879 ? 320  PRO A O     1 
ATOM   2525 C CB    . PRO A 1 326 ? -18.64576 13.10119  15.64479  1.000 30.26558 ? 320  PRO A CB    1 
ATOM   2526 C CG    . PRO A 1 326 ? -17.44223 13.63047  14.89040  1.000 29.35028 ? 320  PRO A CG    1 
ATOM   2527 C CD    . PRO A 1 326 ? -18.04200 14.56459  13.84951  1.000 29.58566 ? 320  PRO A CD    1 
ATOM   2528 N N     . THR A 1 327 ? -21.69768 12.59467  15.98188  1.000 39.56945 ? 321  THR A N     1 
ATOM   2529 C CA    . THR A 1 327 ? -22.85371 12.95711  16.81473  1.000 49.66733 ? 321  THR A CA    1 
ATOM   2530 C C     . THR A 1 327 ? -22.67993 12.47081  18.26273  1.000 56.40522 ? 321  THR A C     1 
ATOM   2531 O O     . THR A 1 327 ? -23.43156 11.62075  18.73491  1.000 62.26871 ? 321  THR A O     1 
ATOM   2532 C CB    . THR A 1 327 ? -24.14095 12.39847  16.21660  1.000 48.41876 ? 321  THR A CB    1 
ATOM   2533 O OG1   . THR A 1 327 ? -23.93890 11.00976  15.89899  1.000 50.50243 ? 321  THR A OG1   1 
ATOM   2534 C CG2   . THR A 1 327 ? -24.52744 13.18958  14.97374  1.000 50.45976 ? 321  THR A CG2   1 
ATOM   2535 N N     . ASP A 1 328 ? -21.70297 13.04378  18.98268  1.000 51.45538 ? 322  ASP A N     1 
ATOM   2536 C CA    . ASP A 1 328 ? -21.49004 12.73184  20.39779  1.000 56.48455 ? 322  ASP A CA    1 
ATOM   2537 C C     . ASP A 1 328 ? -20.41038 13.60461  21.04978  1.000 51.72807 ? 322  ASP A C     1 
ATOM   2538 O O     . ASP A 1 328 ? -19.99277 14.61867  20.47683  1.000 43.90767 ? 322  ASP A O     1 
ATOM   2539 C CB    . ASP A 1 328 ? -21.17637 11.23709  20.55910  1.000 57.20836 ? 322  ASP A CB    1 
ATOM   2540 C CG    . ASP A 1 328 ? -19.97320 10.78951  19.74650  1.000 63.45604 ? 322  ASP A CG    1 
ATOM   2541 O OD1   . ASP A 1 328 ? -19.16704 11.65104  19.32612  1.000 56.40821 ? 322  ASP A OD1   1 
ATOM   2542 O OD2   . ASP A 1 328 ? -19.85969 9.56369   19.50240  1.000 67.37038 ? 322  ASP A OD2   1 
ATOM   2543 N N     . LEU A 1 329 ? -19.96669 13.24026  22.25469  1.000 43.01855 ? 323  LEU A N     1 
ATOM   2544 C CA    . LEU A 1 329 ? -19.07318 14.11569  23.00744  1.000 43.22193 ? 323  LEU A CA    1 
ATOM   2545 C C     . LEU A 1 329 ? -17.66666 14.13729  22.40779  1.000 43.38289 ? 323  LEU A C     1 
ATOM   2546 O O     . LEU A 1 329 ? -17.17494 13.13856  21.87888  1.000 47.18448 ? 323  LEU A O     1 
ATOM   2547 C CB    . LEU A 1 329 ? -18.99759 13.66919  24.46827  1.000 46.38215 ? 323  LEU A CB    1 
ATOM   2548 C CG    . LEU A 1 329 ? -20.22462 13.88039  25.35962  1.000 44.57472 ? 323  LEU A CG    1 
ATOM   2549 C CD1   . LEU A 1 329 ? -20.04743 13.10724  26.66189  1.000 51.74344 ? 323  LEU A CD1   1 
ATOM   2550 C CD2   . LEU A 1 329 ? -20.43650 15.33653  25.64372  1.000 40.60279 ? 323  LEU A CD2   1 
ATOM   2551 N N     . TYR A 1 330 ? -17.01878 15.30069  22.48716  1.000 43.87424 ? 324  TYR A N     1 
ATOM   2552 C CA    . TYR A 1 330 ? -15.58396 15.40421  22.20727  1.000 45.96724 ? 324  TYR A CA    1 
ATOM   2553 C C     . TYR A 1 330 ? -14.83880 14.88673  23.43688  1.000 44.60359 ? 324  TYR A C     1 
ATOM   2554 O O     . TYR A 1 330 ? -14.41935 15.64125  24.31636  1.000 41.30014 ? 324  TYR A O     1 
ATOM   2555 C CB    . TYR A 1 330 ? -15.19191 16.84094  21.87235  1.000 38.56761 ? 324  TYR A CB    1 
ATOM   2556 C CG    . TYR A 1 330 ? -13.72891 17.03596  21.51860  1.000 41.38354 ? 324  TYR A CG    1 
ATOM   2557 C CD1   . TYR A 1 330 ? -13.11823 16.25893  20.53026  1.000 43.91794 ? 324  TYR A CD1   1 
ATOM   2558 C CD2   . TYR A 1 330 ? -12.95714 18.00800  22.15938  1.000 43.78810 ? 324  TYR A CD2   1 
ATOM   2559 C CE1   . TYR A 1 330 ? -11.77572 16.42802  20.19977  1.000 42.76062 ? 324  TYR A CE1   1 
ATOM   2560 C CE2   . TYR A 1 330 ? -11.60038 18.19108  21.83521  1.000 43.32861 ? 324  TYR A CE2   1 
ATOM   2561 C CZ    . TYR A 1 330 ? -11.02085 17.39108  20.85199  1.000 40.84000 ? 324  TYR A CZ    1 
ATOM   2562 O OH    . TYR A 1 330 ? -9.69404  17.55031  20.51685  1.000 40.59983 ? 324  TYR A OH    1 
ATOM   2563 N N     . ALA A 1 331 ? -14.67434 13.56622  23.50278  1.000 45.93903 ? 325  ALA A N     1 
ATOM   2564 C CA    . ALA A 1 331 ? -14.11574 12.95675  24.70056  1.000 49.88143 ? 325  ALA A CA    1 
ATOM   2565 C C     . ALA A 1 331 ? -13.14486 11.84108  24.32058  1.000 59.08496 ? 325  ALA A C     1 
ATOM   2566 O O     . ALA A 1 331 ? -12.91074 11.56481  23.13723  1.000 48.53122 ? 325  ALA A O     1 
ATOM   2567 C CB    . ALA A 1 331 ? -15.24291 12.46161  25.61771  1.000 49.92724 ? 325  ALA A CB    1 
ATOM   2568 N N     . CYS A 1 332 ? -12.58142 11.19659  25.35623  1.000 62.84378 ? 326  CYS A N     1 
ATOM   2569 C CA    . CYS A 1 332 ? -11.51982 10.18800  25.25792  1.000 65.56003 ? 326  CYS A CA    1 
ATOM   2570 C C     . CYS A 1 332 ? -10.26760 10.75297  24.57639  1.000 63.47649 ? 326  CYS A C     1 
ATOM   2571 O O     . CYS A 1 332 ? -10.21817 11.94609  24.25661  1.000 58.57104 ? 326  CYS A O     1 
ATOM   2572 C CB    . CYS A 1 332 ? -12.03487 8.92160   24.55234  1.000 59.38228 ? 326  CYS A CB    1 
ATOM   2573 S SG    . CYS A 1 332 ? -13.77461 8.45597   24.96312  1.000 75.69901 ? 326  CYS A SG    1 
ATOM   2574 N N     . ARG A 1 333 ? -9.24339  9.92211   24.37568  1.000 58.63496 ? 327  ARG A N     1 
ATOM   2575 C CA    . ARG A 1 333 ? -7.99054  10.40322  23.80371  1.000 56.00669 ? 327  ARG A CA    1 
ATOM   2576 C C     . ARG A 1 333 ? -8.24119  11.13361  22.48092  1.000 55.50905 ? 327  ARG A C     1 
ATOM   2577 O O     . ARG A 1 333 ? -8.87037  10.57087  21.57192  1.000 56.17811 ? 327  ARG A O     1 
ATOM   2578 C CB    . ARG A 1 333 ? -7.00862  9.25053   23.59184  1.000 49.09085 ? 327  ARG A CB    1 
ATOM   2579 C CG    . ARG A 1 333 ? -5.62979  9.68345   23.10321  1.000 51.07207 ? 327  ARG A CG    1 
ATOM   2580 C CD    . ARG A 1 333 ? -4.59409  8.62569   23.40828  1.000 59.03553 ? 327  ARG A CD    1 
ATOM   2581 N NE    . ARG A 1 333 ? -3.26054  9.02828   22.98228  1.000 58.73045 ? 327  ARG A NE    1 
ATOM   2582 C CZ    . ARG A 1 333 ? -2.18949  9.04199   23.76055  1.000 59.90010 ? 327  ARG A CZ    1 
ATOM   2583 N NH1   . ARG A 1 333 ? -2.27233  8.79195   25.05981  1.000 58.52315 ? 327  ARG A NH1   1 
ATOM   2584 N NH2   . ARG A 1 333 ? -1.00509  9.31786   23.22234  1.000 60.63819 ? 327  ARG A NH2   1 
ATOM   2585 N N     . PRO A 1 334 ? -7.77356  12.36873  22.33777  1.000 48.34661 ? 328  PRO A N     1 
ATOM   2586 C CA    . PRO A 1 334 ? -8.06162  13.14390  21.12013  1.000 52.55741 ? 328  PRO A CA    1 
ATOM   2587 C C     . PRO A 1 334 ? -7.26340  12.66607  19.90656  1.000 40.93747 ? 328  PRO A C     1 
ATOM   2588 O O     . PRO A 1 334 ? -6.09484  12.27462  20.01833  1.000 47.49769 ? 328  PRO A O     1 
ATOM   2589 C CB    . PRO A 1 334 ? -7.66143  14.56617  21.52789  1.000 45.09496 ? 328  PRO A CB    1 
ATOM   2590 C CG    . PRO A 1 334 ? -6.54339  14.30714  22.55680  1.000 45.87889 ? 328  PRO A CG    1 
ATOM   2591 C CD    . PRO A 1 334 ? -7.09123  13.17665  23.36038  1.000 48.87137 ? 328  PRO A CD    1 
ATOM   2592 N N     . LEU A 1 335 ? -7.91647  12.71811  18.73860  1.000 36.84786 ? 329  LEU A N     1 
ATOM   2593 C CA    . LEU A 1 335 ? -7.37874  12.25515  17.45133  1.000 35.72499 ? 329  LEU A CA    1 
ATOM   2594 C C     . LEU A 1 335 ? -6.68192  13.39331  16.70853  1.000 29.64639 ? 329  LEU A C     1 
ATOM   2595 O O     . LEU A 1 335 ? -7.13506  14.53697  16.76116  1.000 30.16638 ? 329  LEU A O     1 
ATOM   2596 C CB    . LEU A 1 335 ? -8.49269  11.71257  16.55864  1.000 34.13650 ? 329  LEU A CB    1 
ATOM   2597 C CG    . LEU A 1 335 ? -8.66019  10.19406  16.37507  1.000 36.21648 ? 329  LEU A CG    1 
ATOM   2598 C CD1   . LEU A 1 335 ? -9.05353  9.51984   17.65200  1.000 37.33930 ? 329  LEU A CD1   1 
ATOM   2599 C CD2   . LEU A 1 335 ? -9.62363  9.78759   15.23199  1.000 30.43840 ? 329  LEU A CD2   1 
ATOM   2600 N N     . CYS A 1 336 ? -5.59204  13.07849  15.98809  1.000 26.94631 ? 330  CYS A N     1 
ATOM   2601 C CA    . CYS A 1 336 ? -4.87071  14.08891  15.21665  1.000 26.93851 ? 330  CYS A CA    1 
ATOM   2602 C C     . CYS A 1 336 ? -4.51523  13.51574  13.85977  1.000 23.87171 ? 330  CYS A C     1 
ATOM   2603 O O     . CYS A 1 336 ? -4.28049  12.31414  13.72688  1.000 29.24202 ? 330  CYS A O     1 
ATOM   2604 C CB    . CYS A 1 336 ? -3.54987  14.55341  15.86359  1.000 39.36553 ? 330  CYS A CB    1 
ATOM   2605 S SG    . CYS A 1 336 ? -3.47585  14.34838  17.58701  1.000 57.26436 ? 330  CYS A SG    1 
ATOM   2606 N N     . ASP A 1 337 ? -4.43041  14.38554  12.85641  1.000 18.64480 ? 331  ASP A N     1 
ATOM   2607 C CA    . ASP A 1 337 ? -4.20188  13.91163  11.49835  1.000 21.96896 ? 331  ASP A CA    1 
ATOM   2608 C C     . ASP A 1 337 ? -3.30185  14.86886  10.72546  1.000 21.17089 ? 331  ASP A C     1 
ATOM   2609 O O     . ASP A 1 337 ? -3.07233  16.01128  11.11810  1.000 20.68168 ? 331  ASP A O     1 
ATOM   2610 C CB    . ASP A 1 337 ? -5.52078  13.75581  10.73221  1.000 21.89940 ? 331  ASP A CB    1 
ATOM   2611 C CG    . ASP A 1 337 ? -6.21007  15.11019  10.45934  1.000 22.37057 ? 331  ASP A CG    1 
ATOM   2612 O OD1   . ASP A 1 337 ? -5.91933  15.80368  9.43302   1.000 23.37685 ? 331  ASP A OD1   1 
ATOM   2613 O OD2   . ASP A 1 337 ? -7.05815  15.48326  11.29963  1.000 25.34387 ? 331  ASP A OD2   1 
ATOM   2614 N N     . SER A 1 338 ? -2.81611  14.38831  9.57939   1.000 21.76356 ? 332  SER A N     1 
ATOM   2615 C CA    . SER A 1 338 ? -1.95815  15.17817  8.69898   1.000 22.74159 ? 332  SER A CA    1 
ATOM   2616 C C     . SER A 1 338 ? -2.64009  15.41965  7.36512   1.000 24.39476 ? 332  SER A C     1 
ATOM   2617 O O     . SER A 1 338 ? -1.98315  15.44794  6.32297   1.000 27.07364 ? 332  SER A O     1 
ATOM   2618 C CB    . SER A 1 338 ? -0.57987  14.52603  8.47162   1.000 22.18198 ? 332  SER A CB    1 
ATOM   2619 O OG    . SER A 1 338 ? 0.15761   14.31440  9.68038   1.000 23.59074 ? 332  SER A OG    1 
ATOM   2620 N N     . GLY A 1 339 ? -3.97462  15.60604  7.38563   1.000 23.13706 ? 333  GLY A N     1 
ATOM   2621 C CA    . GLY A 1 339 ? -4.68653  15.96863  6.17075   1.000 22.58128 ? 333  GLY A CA    1 
ATOM   2622 C C     . GLY A 1 339 ? -5.83127  15.00346  5.89559   1.000 22.19283 ? 333  GLY A C     1 
ATOM   2623 O O     . GLY A 1 339 ? -6.08822  14.65167  4.74561   1.000 22.16961 ? 333  GLY A O     1 
ATOM   2624 N N     . TYR A 1 340 ? -6.50552  14.56363  6.95573   1.000 19.89227 ? 334  TYR A N     1 
ATOM   2625 C CA    . TYR A 1 340 ? -7.52727  13.52049  6.82396   1.000 20.81507 ? 334  TYR A CA    1 
ATOM   2626 C C     . TYR A 1 340 ? -8.78077  14.02320  6.12446   1.000 21.71966 ? 334  TYR A C     1 
ATOM   2627 O O     . TYR A 1 340 ? -9.28971  13.36717  5.20656   1.000 21.08598 ? 334  TYR A O     1 
ATOM   2628 C CB    . TYR A 1 340 ? -7.90310  12.99792  8.19610   1.000 19.32781 ? 334  TYR A CB    1 
ATOM   2629 C CG    . TYR A 1 340 ? -9.00423  11.96889  8.23294   1.000 21.81676 ? 334  TYR A CG    1 
ATOM   2630 C CD1   . TYR A 1 340 ? -8.82462  10.69139  7.69554   1.000 17.46183 ? 334  TYR A CD1   1 
ATOM   2631 C CD2   . TYR A 1 340 ? -10.22368 12.25933  8.83957   1.000 19.57233 ? 334  TYR A CD2   1 
ATOM   2632 C CE1   . TYR A 1 340 ? -9.83953  9.73958   7.74196   1.000 17.55674 ? 334  TYR A CE1   1 
ATOM   2633 C CE2   . TYR A 1 340 ? -11.23515 11.31355  8.90335   1.000 19.65651 ? 334  TYR A CE2   1 
ATOM   2634 C CZ    . TYR A 1 340 ? -11.05031 10.06754  8.35335   1.000 21.38534 ? 334  TYR A CZ    1 
ATOM   2635 O OH    . TYR A 1 340 ? -12.03921 9.11919   8.46808   1.000 20.86344 ? 334  TYR A OH    1 
ATOM   2636 N N     . TYR A 1 341 ? -9.35313  15.13607  6.59514   1.000 22.90875 ? 335  TYR A N     1 
ATOM   2637 C CA    . TYR A 1 341 ? -10.62890 15.54479  5.99292   1.000 22.50321 ? 335  TYR A CA    1 
ATOM   2638 C C     . TYR A 1 341 ? -10.43670 15.94976  4.54540   1.000 25.18433 ? 335  TYR A C     1 
ATOM   2639 O O     . TYR A 1 341 ? -11.33793 15.75338  3.71691   1.000 23.86129 ? 335  TYR A O     1 
ATOM   2640 C CB    . TYR A 1 341 ? -11.29230 16.67376  6.81328   1.000 24.11593 ? 335  TYR A CB    1 
ATOM   2641 C CG    . TYR A 1 341 ? -11.73235 16.19031  8.18774   1.000 25.08096 ? 335  TYR A CG    1 
ATOM   2642 C CD1   . TYR A 1 341 ? -12.62397 15.11845  8.31380   1.000 21.15067 ? 335  TYR A CD1   1 
ATOM   2643 C CD2   . TYR A 1 341 ? -11.22777 16.76735  9.34940   1.000 22.75261 ? 335  TYR A CD2   1 
ATOM   2644 C CE1   . TYR A 1 341 ? -13.01959 14.66787  9.53665   1.000 23.17026 ? 335  TYR A CE1   1 
ATOM   2645 C CE2   . TYR A 1 341 ? -11.62182 16.32463  10.59823  1.000 26.83078 ? 335  TYR A CE2   1 
ATOM   2646 C CZ    . TYR A 1 341 ? -12.51698 15.26715  10.68231  1.000 28.02269 ? 335  TYR A CZ    1 
ATOM   2647 O OH    . TYR A 1 341 ? -12.90322 14.85088  11.92520  1.000 25.42137 ? 335  TYR A OH    1 
ATOM   2648 N N     . GLU A 1 342 ? -9.26296  16.48456  4.21099   1.000 23.26105 ? 336  GLU A N     1 
ATOM   2649 C CA    . GLU A 1 342 ? -8.99351  16.86146  2.83011   1.000 23.78145 ? 336  GLU A CA    1 
ATOM   2650 C C     . GLU A 1 342 ? -9.06821  15.67514  1.88628   1.000 24.50199 ? 336  GLU A C     1 
ATOM   2651 O O     . GLU A 1 342 ? -9.35023  15.85587  0.69316   1.000 20.61950 ? 336  GLU A O     1 
ATOM   2652 C CB    . GLU A 1 342 ? -7.61203  17.52416  2.72948   1.000 29.83049 ? 336  GLU A CB    1 
ATOM   2653 C CG    . GLU A 1 342 ? -7.54836  18.92102  3.37267   1.000 29.07466 ? 336  GLU A CG    1 
ATOM   2654 C CD    . GLU A 1 342 ? -7.20045  18.93746  4.86223   1.000 34.42537 ? 336  GLU A CD    1 
ATOM   2655 O OE1   . GLU A 1 342 ? -7.22596  17.88505  5.54220   1.000 29.39294 ? 336  GLU A OE1   1 
ATOM   2656 O OE2   . GLU A 1 342 ? -6.93907  20.04480  5.37563   1.000 37.00449 ? 336  GLU A OE2   1 
ATOM   2657 N N     . ILE A 1 343 ? -8.76345  14.47306  2.38629   1.000 21.60709 ? 337  ILE A N     1 
ATOM   2658 C CA    . ILE A 1 343 ? -8.75740  13.27787  1.54765   1.000 25.98555 ? 337  ILE A CA    1 
ATOM   2659 C C     . ILE A 1 343 ? -10.11406 13.07648  0.88355   1.000 20.40265 ? 337  ILE A C     1 
ATOM   2660 O O     . ILE A 1 343 ? -10.20449 12.59288  -0.25012  1.000 19.72906 ? 337  ILE A O     1 
ATOM   2661 C CB    . ILE A 1 343 ? -8.37346  12.04721  2.39744   1.000 24.77209 ? 337  ILE A CB    1 
ATOM   2662 C CG1   . ILE A 1 343 ? -6.87642  12.05602  2.74199   1.000 30.32798 ? 337  ILE A CG1   1 
ATOM   2663 C CG2   . ILE A 1 343 ? -8.82884  10.74088  1.71831   1.000 28.60394 ? 337  ILE A CG2   1 
ATOM   2664 C CD1   . ILE A 1 343 ? -5.98709  12.37971  1.57598   1.000 27.69976 ? 337  ILE A CD1   1 
ATOM   2665 N N     . PHE A 1 344 ? -11.19205 13.44692  1.57719   1.000 22.09010 ? 338  PHE A N     1 
ATOM   2666 C CA    . PHE A 1 344 ? -12.52839 13.12216  1.07317   1.000 19.60208 ? 338  PHE A CA    1 
ATOM   2667 C C     . PHE A 1 344 ? -12.97390 14.06205  -0.02798  1.000 20.94554 ? 338  PHE A C     1 
ATOM   2668 O O     . PHE A 1 344 ? -14.03392 13.83560  -0.62545  1.000 24.80168 ? 338  PHE A O     1 
ATOM   2669 C CB    . PHE A 1 344 ? -13.50608 13.08213  2.25883   1.000 17.61328 ? 338  PHE A CB    1 
ATOM   2670 C CG    . PHE A 1 344 ? -13.16570 11.99182  3.22233   1.000 17.14800 ? 338  PHE A CG    1 
ATOM   2671 C CD1   . PHE A 1 344 ? -13.59502 10.67145  2.98709   1.000 17.88218 ? 338  PHE A CD1   1 
ATOM   2672 C CD2   . PHE A 1 344 ? -12.30960 12.22761  4.27397   1.000 20.88980 ? 338  PHE A CD2   1 
ATOM   2673 C CE1   . PHE A 1 344 ? -13.25005 9.64358   3.84029   1.000 20.08821 ? 338  PHE A CE1   1 
ATOM   2674 C CE2   . PHE A 1 344 ? -11.93783 11.18739  5.12277   1.000 19.42990 ? 338  PHE A CE2   1 
ATOM   2675 C CZ    . PHE A 1 344 ? -12.41959 9.90224   4.91368   1.000 22.94972 ? 338  PHE A CZ    1 
ATOM   2676 N N     . ASN A 1 345 ? -12.16714 15.07181  -0.35774  1.000 21.16160 ? 339  ASN A N     1 
ATOM   2677 C CA    . ASN A 1 345 ? -12.44321 15.86458  -1.55225  1.000 22.20080 ? 339  ASN A CA    1 
ATOM   2678 C C     . ASN A 1 345 ? -11.91239 15.19740  -2.81831  1.000 21.45004 ? 339  ASN A C     1 
ATOM   2679 O O     . ASN A 1 345 ? -12.23015 15.64847  -3.92756  1.000 23.42922 ? 339  ASN A O     1 
ATOM   2680 C CB    . ASN A 1 345 ? -11.81884 17.25388  -1.43198  1.000 23.00267 ? 339  ASN A CB    1 
ATOM   2681 C CG    . ASN A 1 345 ? -12.50645 18.11567  -0.37803  1.000 27.16270 ? 339  ASN A CG    1 
ATOM   2682 O OD1   . ASN A 1 345 ? -13.73108 18.04259  -0.18508  1.000 27.80850 ? 339  ASN A OD1   1 
ATOM   2683 N ND2   . ASN A 1 345 ? -11.72555 18.96481  0.27960   1.000 24.45957 ? 339  ASN A ND2   1 
ATOM   2684 N N     . ARG A 1 346 ? -11.13815 14.12455  -2.69233  1.000 20.93719 ? 340  ARG A N     1 
ATOM   2685 C CA    . ARG A 1 346 ? -10.50533 13.55584  -3.87792  1.000 21.32554 ? 340  ARG A CA    1 
ATOM   2686 C C     . ARG A 1 346 ? -11.52551 12.76951  -4.69540  1.000 24.35780 ? 340  ARG A C     1 
ATOM   2687 O O     . ARG A 1 346 ? -12.43418 12.12754  -4.15562  1.000 24.55554 ? 340  ARG A O     1 
ATOM   2688 C CB    . ARG A 1 346 ? -9.32769  12.63060  -3.49619  1.000 21.70348 ? 340  ARG A CB    1 
ATOM   2689 C CG    . ARG A 1 346 ? -8.13482  13.30265  -2.74344  1.000 22.10487 ? 340  ARG A CG    1 
ATOM   2690 C CD    . ARG A 1 346 ? -7.13576  12.18749  -2.27760  1.000 24.74907 ? 340  ARG A CD    1 
ATOM   2691 N NE    . ARG A 1 346 ? -6.71443  11.39074  -3.42702  1.000 25.70608 ? 340  ARG A NE    1 
ATOM   2692 C CZ    . ARG A 1 346 ? -5.74312  11.75885  -4.25031  1.000 28.36921 ? 340  ARG A CZ    1 
ATOM   2693 N NH1   . ARG A 1 346 ? -4.91401  12.75133  -3.93800  1.000 24.03576 ? 340  ARG A NH1   1 
ATOM   2694 N NH2   . ARG A 1 346 ? -5.56791  11.08698  -5.38525  1.000 26.07630 ? 340  ARG A NH2   1 
ATOM   2695 N N     . ASP A 1 347 ? -11.32632 12.76113  -6.01109  1.000 24.33427 ? 341  ASP A N     1 
ATOM   2696 C CA    . ASP A 1 347 ? -12.22727 12.00284  -6.87158  1.000 27.27237 ? 341  ASP A CA    1 
ATOM   2697 C C     . ASP A 1 347 ? -12.06291 10.50140  -6.72515  1.000 27.14879 ? 341  ASP A C     1 
ATOM   2698 O O     . ASP A 1 347 ? -12.92583 9.74160   -7.18548  1.000 24.50265 ? 341  ASP A O     1 
ATOM   2699 C CB    . ASP A 1 347 ? -12.02818 12.36530  -8.34245  1.000 37.82979 ? 341  ASP A CB    1 
ATOM   2700 C CG    . ASP A 1 347 ? -12.50420 13.77584  -8.67057  1.000 59.49898 ? 341  ASP A CG    1 
ATOM   2701 O OD1   . ASP A 1 347 ? -11.69337 14.55885  -9.23225  1.000 60.68698 ? 341  ASP A OD1   1 
ATOM   2702 O OD2   . ASP A 1 347 ? -13.67400 14.09931  -8.34835  1.000 64.48417 ? 341  ASP A OD2   1 
ATOM   2703 N N     . ASN A 1 348 ? -11.00445 10.03402  -6.08404  1.000 24.85102 ? 342  ASN A N     1 
ATOM   2704 C CA    . ASN A 1 348 ? -10.82128 8.59342   -6.01136  1.000 22.85931 ? 342  ASN A CA    1 
ATOM   2705 C C     . ASN A 1 348 ? -11.13410 8.03779   -4.63383  1.000 23.17858 ? 342  ASN A C     1 
ATOM   2706 O O     . ASN A 1 348 ? -10.66717 6.94750   -4.30943  1.000 21.30404 ? 342  ASN A O     1 
ATOM   2707 C CB    . ASN A 1 348 ? -9.38886  8.24789   -6.43893  1.000 23.20194 ? 342  ASN A CB    1 
ATOM   2708 C CG    . ASN A 1 348 ? -8.34753  8.61111   -5.37680  1.000 28.87261 ? 342  ASN A CG    1 
ATOM   2709 O OD1   . ASN A 1 348 ? -8.49117  9.60058   -4.64862  1.000 24.80527 ? 342  ASN A OD1   1 
ATOM   2710 N ND2   . ASN A 1 348 ? -7.24107  7.82420   -5.32143  1.000 23.77692 ? 342  ASN A ND2   1 
ATOM   2711 N N     . VAL A 1 349 ? -11.86634 8.78132   -3.79477  1.000 17.91857 ? 343  VAL A N     1 
ATOM   2712 C CA    . VAL A 1 349 ? -12.19284 8.34955   -2.43381  1.000 17.51221 ? 343  VAL A CA    1 
ATOM   2713 C C     . VAL A 1 349 ? -13.70764 8.28623   -2.26460  1.000 21.76829 ? 343  VAL A C     1 
ATOM   2714 O O     . VAL A 1 349 ? -14.40771 9.26209   -2.57247  1.000 24.63590 ? 343  VAL A O     1 
ATOM   2715 C CB    . VAL A 1 349 ? -11.59148 9.29132   -1.37714  1.000 20.80489 ? 343  VAL A CB    1 
ATOM   2716 C CG1   . VAL A 1 349 ? -12.00033 8.82107   0.03452   1.000 20.05738 ? 343  VAL A CG1   1 
ATOM   2717 C CG2   . VAL A 1 349 ? -10.08673 9.29959   -1.48987  1.000 20.60151 ? 343  VAL A CG2   1 
ATOM   2718 N N     . SER A 1 350 ? -14.20180 7.16106   -1.72624  1.000 20.07896 ? 344  SER A N     1 
ATOM   2719 C CA    . SER A 1 350 ? -15.61508 6.97622   -1.38140  1.000 20.46313 ? 344  SER A CA    1 
ATOM   2720 C C     . SER A 1 350 ? -15.74771 6.69379   0.10584   1.000 23.93272 ? 344  SER A C     1 
ATOM   2721 O O     . SER A 1 350 ? -15.05231 5.81905   0.63864   1.000 21.55151 ? 344  SER A O     1 
ATOM   2722 C CB    . SER A 1 350 ? -16.24990 5.80680   -2.14451  1.000 26.36009 ? 344  SER A CB    1 
ATOM   2723 O OG    . SER A 1 350 ? -16.30661 6.05663   -3.52997  1.000 29.72641 ? 344  SER A OG    1 
ATOM   2724 N N     . LEU A 1 351 ? -16.64462 7.41313   0.77368   1.000 18.08149 ? 345  LEU A N     1 
ATOM   2725 C CA    . LEU A 1 351 ? -16.93430 7.15871   2.17765   1.000 20.48785 ? 345  LEU A CA    1 
ATOM   2726 C C     . LEU A 1 351 ? -18.25334 6.39575   2.30101   1.000 24.16803 ? 345  LEU A C     1 
ATOM   2727 O O     . LEU A 1 351 ? -19.29132 6.85004   1.79016   1.000 23.48527 ? 345  LEU A O     1 
ATOM   2728 C CB    . LEU A 1 351 ? -17.00769 8.48153   2.96751   1.000 17.48803 ? 345  LEU A CB    1 
ATOM   2729 C CG    . LEU A 1 351 ? -17.36439 8.39850   4.45564   1.000 22.14218 ? 345  LEU A CG    1 
ATOM   2730 C CD1   . LEU A 1 351 ? -16.33381 7.59540   5.27965   1.000 20.20806 ? 345  LEU A CD1   1 
ATOM   2731 C CD2   . LEU A 1 351 ? -17.50989 9.84603   5.03201   1.000 23.56774 ? 345  LEU A CD2   1 
ATOM   2732 N N     . GLU A 1 352 ? -18.21971 5.26875   3.00320   1.000 22.87884 ? 346  GLU A N     1 
ATOM   2733 C CA    . GLU A 1 352 ? -19.40032 4.44551   3.26503   1.000 26.56693 ? 346  GLU A CA    1 
ATOM   2734 C C     . GLU A 1 352 ? -19.71131 4.51169   4.76150   1.000 26.96935 ? 346  GLU A C     1 
ATOM   2735 O O     . GLU A 1 352 ? -18.87309 4.14031   5.59101   1.000 25.54857 ? 346  GLU A O     1 
ATOM   2736 C CB    . GLU A 1 352 ? -19.16186 2.99292   2.83528   1.000 27.69867 ? 346  GLU A CB    1 
ATOM   2737 C CG    . GLU A 1 352 ? -19.43169 2.80137   1.39442   1.000 29.03649 ? 346  GLU A CG    1 
ATOM   2738 C CD    . GLU A 1 352 ? -20.91334 2.91155   1.02459   1.000 40.55552 ? 346  GLU A CD    1 
ATOM   2739 O OE1   . GLU A 1 352 ? -21.78957 2.78044   1.90611   1.000 36.50958 ? 346  GLU A OE1   1 
ATOM   2740 O OE2   . GLU A 1 352 ? -21.19466 3.14895   -0.16902  1.000 42.90174 ? 346  GLU A OE2   1 
ATOM   2741 N N     . ASP A 1 353 ? -20.91976 4.96342   5.10528   1.000 25.38119 ? 347  ASP A N     1 
ATOM   2742 C CA    . ASP A 1 353 ? -21.42260 4.97073   6.48025   1.000 23.99360 ? 347  ASP A CA    1 
ATOM   2743 C C     . ASP A 1 353 ? -21.97128 3.59121   6.79158   1.000 26.79468 ? 347  ASP A C     1 
ATOM   2744 O O     . ASP A 1 353 ? -23.10658 3.26879   6.40648   1.000 30.30664 ? 347  ASP A O     1 
ATOM   2745 C CB    . ASP A 1 353 ? -22.49363 6.05439   6.63438   1.000 29.74071 ? 347  ASP A CB    1 
ATOM   2746 C CG    . ASP A 1 353 ? -23.10566 6.11682   8.02999   1.000 33.06250 ? 347  ASP A CG    1 
ATOM   2747 O OD1   . ASP A 1 353 ? -22.92704 5.19007   8.85188   1.000 31.59686 ? 347  ASP A OD1   1 
ATOM   2748 O OD2   . ASP A 1 353 ? -23.80686 7.12490   8.29090   1.000 38.25627 ? 347  ASP A OD2   1 
ATOM   2749 N N     . VAL A 1 354 ? -21.19680 2.77106   7.51132   1.000 23.10934 ? 348  VAL A N     1 
ATOM   2750 C CA    . VAL A 1 354 ? -21.60875 1.37662   7.70875   1.000 23.27501 ? 348  VAL A CA    1 
ATOM   2751 C C     . VAL A 1 354 ? -22.32308 1.25781   9.05324   1.000 28.06980 ? 348  VAL A C     1 
ATOM   2752 O O     . VAL A 1 354 ? -22.45787 0.16121   9.60451   1.000 30.46361 ? 348  VAL A O     1 
ATOM   2753 C CB    . VAL A 1 354 ? -20.43411 0.36797   7.61881   1.000 24.90567 ? 348  VAL A CB    1 
ATOM   2754 C CG1   . VAL A 1 354 ? -19.94458 0.23208   6.16465   1.000 37.20267 ? 348  VAL A CG1   1 
ATOM   2755 C CG2   . VAL A 1 354 ? -19.30701 0.59462   8.65375   1.000 27.16710 ? 348  VAL A CG2   1 
ATOM   2756 N N     . LYS A 1 355 ? -22.74737 2.39053   9.61269   1.000 28.31761 ? 349  LYS A N     1 
ATOM   2757 C CA    . LYS A 1 355 ? -23.79069 2.35371   10.63127  1.000 31.45162 ? 349  LYS A CA    1 
ATOM   2758 C C     . LYS A 1 355 ? -25.15375 2.36097   9.94935   1.000 34.98704 ? 349  LYS A C     1 
ATOM   2759 O O     . LYS A 1 355 ? -26.01176 1.52076   10.23517  1.000 35.47582 ? 349  LYS A O     1 
ATOM   2760 C CB    . LYS A 1 355 ? -23.66516 3.54960   11.58586  1.000 39.69489 ? 349  LYS A CB    1 
ATOM   2761 C CG    . LYS A 1 355 ? -24.65747 3.52228   12.75573  1.000 42.92792 ? 349  LYS A CG    1 
ATOM   2762 C CD    . LYS A 1 355 ? -24.65408 4.84079   13.53166  1.000 51.40484 ? 349  LYS A CD    1 
ATOM   2763 C CE    . LYS A 1 355 ? -25.40450 4.69154   14.86276  1.000 64.22890 ? 349  LYS A CE    1 
ATOM   2764 N NZ    . LYS A 1 355 ? -26.88907 4.53631   14.69322  1.000 58.20061 ? 349  LYS A NZ    1 
ATOM   2765 N N     . ALA A 1 356 ? -25.33590 3.28414   9.00422   1.000 29.68934 ? 350  ALA A N     1 
ATOM   2766 C CA    . ALA A 1 356 ? -26.54332 3.34677   8.19352   1.000 31.87913 ? 350  ALA A CA    1 
ATOM   2767 C C     . ALA A 1 356 ? -26.60313 2.23343   7.14819   1.000 37.14664 ? 350  ALA A C     1 
ATOM   2768 O O     . ALA A 1 356 ? -27.69617 1.78198   6.78631   1.000 32.55018 ? 350  ALA A O     1 
ATOM   2769 C CB    . ALA A 1 356 ? -26.61007 4.70448   7.50747   1.000 30.78086 ? 350  ALA A CB    1 
ATOM   2770 N N     . ASN A 1 357 ? -25.45403 1.76926   6.66753   1.000 27.03060 ? 351  ASN A N     1 
ATOM   2771 C CA    . ASN A 1 357 ? -25.38119 0.84143   5.53676   1.000 25.61717 ? 351  ASN A CA    1 
ATOM   2772 C C     . ASN A 1 357 ? -24.36275 -0.23640  5.87548   1.000 28.11928 ? 351  ASN A C     1 
ATOM   2773 O O     . ASN A 1 357 ? -23.24309 -0.23910  5.33499   1.000 26.69143 ? 351  ASN A O     1 
ATOM   2774 C CB    . ASN A 1 357 ? -25.02834 1.60519   4.25882   1.000 27.39212 ? 351  ASN A CB    1 
ATOM   2775 C CG    . ASN A 1 357 ? -25.01537 0.72089   3.02459   1.000 29.92961 ? 351  ASN A CG    1 
ATOM   2776 O OD1   . ASN A 1 357 ? -25.80971 -0.22486  2.90340   1.000 28.99558 ? 351  ASN A OD1   1 
ATOM   2777 N ND2   . ASN A 1 357 ? -24.08993 1.01395   2.09841   1.000 30.21236 ? 351  ASN A ND2   1 
ATOM   2778 N N     . PRO A 1 358 ? -24.70917 -1.15691  6.78163   1.000 27.00335 ? 352  PRO A N     1 
ATOM   2779 C CA    . PRO A 1 358 ? -23.70941 -2.06291  7.35837   1.000 28.22113 ? 352  PRO A CA    1 
ATOM   2780 C C     . PRO A 1 358 ? -23.07631 -3.01915  6.35443   1.000 28.44328 ? 352  PRO A C     1 
ATOM   2781 O O     . PRO A 1 358 ? -23.65619 -3.39932  5.33382   1.000 28.28483 ? 352  PRO A O     1 
ATOM   2782 C CB    . PRO A 1 358 ? -24.50433 -2.83310  8.43224   1.000 28.92216 ? 352  PRO A CB    1 
ATOM   2783 C CG    . PRO A 1 358 ? -25.73093 -1.91834  8.71820   1.000 31.63428 ? 352  PRO A CG    1 
ATOM   2784 C CD    . PRO A 1 358 ? -26.05175 -1.38126  7.36116   1.000 33.07658 ? 352  PRO A CD    1 
ATOM   2785 N N     . ILE A 1 359 ? -21.86269 -3.44038  6.69039   1.000 22.79070 ? 353  ILE A N     1 
ATOM   2786 C CA    . ILE A 1 359 ? -21.24265 -4.53806  5.95334   1.000 24.78524 ? 353  ILE A CA    1 
ATOM   2787 C C     . ILE A 1 359 ? -21.97783 -5.82260  6.32237   1.000 30.02152 ? 353  ILE A C     1 
ATOM   2788 O O     . ILE A 1 359 ? -22.09671 -6.15926  7.50595   1.000 27.03492 ? 353  ILE A O     1 
ATOM   2789 C CB    . ILE A 1 359 ? -19.75425 -4.65594  6.29091   1.000 26.11287 ? 353  ILE A CB    1 
ATOM   2790 C CG1   . ILE A 1 359 ? -18.97197 -3.40229  5.87000   1.000 26.78173 ? 353  ILE A CG1   1 
ATOM   2791 C CG2   . ILE A 1 359 ? -19.16041 -5.91578  5.64901   1.000 25.50046 ? 353  ILE A CG2   1 
ATOM   2792 C CD1   . ILE A 1 359 ? -17.60188 -3.31627  6.54615   1.000 23.99251 ? 353  ILE A CD1   1 
ATOM   2793 N N     . VAL A 1 360 ? -22.45126 -6.56650  5.31917   1.000 25.64134 ? 354  VAL A N     1 
ATOM   2794 C CA    . VAL A 1 360 ? -23.14306 -7.81474  5.60906   1.000 26.26159 ? 354  VAL A CA    1 
ATOM   2795 C C     . VAL A 1 360 ? -22.38746 -9.05069  5.11553   1.000 31.84146 ? 354  VAL A C     1 
ATOM   2796 O O     . VAL A 1 360 ? -22.68405 -10.16530 5.57997   1.000 29.59713 ? 354  VAL A O     1 
ATOM   2797 C CB    . VAL A 1 360 ? -24.58115 -7.78921  5.04621   1.000 30.90406 ? 354  VAL A CB    1 
ATOM   2798 C CG1   . VAL A 1 360 ? -25.37051 -6.66335  5.73358   1.000 28.65754 ? 354  VAL A CG1   1 
ATOM   2799 C CG2   . VAL A 1 360 ? -24.61835 -7.66073  3.52332   1.000 30.79659 ? 354  VAL A CG2   1 
ATOM   2800 N N     . GLU A 1 361 ? -21.40579 -8.89930  4.22834   1.000 28.40284 ? 355  GLU A N     1 
ATOM   2801 C CA    . GLU A 1 361 ? -20.71824 -10.06399 3.68969   1.000 29.27972 ? 355  GLU A CA    1 
ATOM   2802 C C     . GLU A 1 361 ? -19.38767 -9.62924  3.07390   1.000 24.08788 ? 355  GLU A C     1 
ATOM   2803 O O     . GLU A 1 361 ? -19.26936 -8.51737  2.56646   1.000 25.88564 ? 355  GLU A O     1 
ATOM   2804 C CB    . GLU A 1 361 ? -21.61277 -10.77127 2.63957   1.000 29.96533 ? 355  GLU A CB    1 
ATOM   2805 C CG    . GLU A 1 361 ? -21.25459 -12.21760 2.47201   1.000 34.65362 ? 355  GLU A CG    1 
ATOM   2806 C CD    . GLU A 1 361 ? -21.80298 -12.85306 1.20014   1.000 40.40848 ? 355  GLU A CD    1 
ATOM   2807 O OE1   . GLU A 1 361 ? -22.58980 -12.20608 0.46498   1.000 41.32828 ? 355  GLU A OE1   1 
ATOM   2808 O OE2   . GLU A 1 361 ? -21.42769 -14.01288 0.93499   1.000 41.93400 ? 355  GLU A OE2   1 
ATOM   2809 N N     . ILE A 1 362 ? -18.39653 -10.51740 3.11142   1.000 24.63183 ? 356  ILE A N     1 
ATOM   2810 C CA    . ILE A 1 362 ? -17.20352 -10.39077 2.28125   1.000 23.61116 ? 356  ILE A CA    1 
ATOM   2811 C C     . ILE A 1 362 ? -17.14117 -11.60312 1.35797   1.000 26.17384 ? 356  ILE A C     1 
ATOM   2812 O O     . ILE A 1 362 ? -17.32821 -12.74022 1.81112   1.000 24.62583 ? 356  ILE A O     1 
ATOM   2813 C CB    . ILE A 1 362 ? -15.93036 -10.26264 3.13796   1.000 24.11922 ? 356  ILE A CB    1 
ATOM   2814 C CG1   . ILE A 1 362 ? -15.83616 -8.84093  3.70284   1.000 23.71527 ? 356  ILE A CG1   1 
ATOM   2815 C CG2   . ILE A 1 362 ? -14.68543 -10.58832 2.29806   1.000 22.12253 ? 356  ILE A CG2   1 
ATOM   2816 C CD1   . ILE A 1 362 ? -14.65309 -8.67098  4.69851   1.000 25.88722 ? 356  ILE A CD1   1 
ATOM   2817 N N     . LYS A 1 363 ? -16.89856 -11.36606 0.06668   1.000 24.93350 ? 357  LYS A N     1 
ATOM   2818 C CA    . LYS A 1 363 ? -16.73448 -12.45143 -0.90816  1.000 27.68734 ? 357  LYS A CA    1 
ATOM   2819 C C     . LYS A 1 363 ? -15.32691 -12.41979 -1.49594  1.000 28.51773 ? 357  LYS A C     1 
ATOM   2820 O O     . LYS A 1 363 ? -14.47598 -11.62777 -1.08189  1.000 27.75693 ? 357  LYS A O     1 
ATOM   2821 C CB    . LYS A 1 363 ? -17.79230 -12.34857 -2.01052  1.000 26.27626 ? 357  LYS A CB    1 
ATOM   2822 C CG    . LYS A 1 363 ? -19.18549 -12.11236 -1.45170  1.000 32.29208 ? 357  LYS A CG    1 
ATOM   2823 C CD    . LYS A 1 363 ? -20.26249 -12.16477 -2.55144  1.000 33.59553 ? 357  LYS A CD    1 
ATOM   2824 C CE    . LYS A 1 363 ? -20.55543 -13.60502 -2.94578  1.000 41.61506 ? 357  LYS A CE    1 
ATOM   2825 N NZ    . LYS A 1 363 ? -21.59576 -13.65180 -4.02791  1.000 48.52920 ? 357  LYS A NZ    1 
ATOM   2826 N N     . GLU A 1 364 ? -15.07973 -13.27928 -2.49026  1.000 26.62747 ? 358  GLU A N     1 
ATOM   2827 C CA    . GLU A 1 364 ? -13.69488 -13.43765 -2.93844  1.000 29.99065 ? 358  GLU A CA    1 
ATOM   2828 C C     . GLU A 1 364 ? -13.08458 -12.14431 -3.47871  1.000 26.01028 ? 358  GLU A C     1 
ATOM   2829 O O     . GLU A 1 364 ? -11.85641 -12.01458 -3.47164  1.000 25.31817 ? 358  GLU A O     1 
ATOM   2830 C CB    . GLU A 1 364 ? -13.58699 -14.52800 -4.00577  1.000 30.33272 ? 358  GLU A CB    1 
ATOM   2831 C CG    . GLU A 1 364 ? -14.27158 -14.19001 -5.29800  1.000 35.76418 ? 358  GLU A CG    1 
ATOM   2832 C CD    . GLU A 1 364 ? -13.96138 -15.21472 -6.38033  1.000 46.27020 ? 358  GLU A CD    1 
ATOM   2833 O OE1   . GLU A 1 364 ? -12.77149 -15.35630 -6.75746  1.000 43.54001 ? 358  GLU A OE1   1 
ATOM   2834 O OE2   . GLU A 1 364 ? -14.91708 -15.86055 -6.86292  1.000 54.60333 ? 358  GLU A OE2   1 
ATOM   2835 N N     . ASP A 1 365 ? -13.90248 -11.18504 -3.95306  1.000 24.63952 ? 359  ASP A N     1 
ATOM   2836 C CA    . ASP A 1 365 ? -13.37391 -9.97589  -4.56577  1.000 22.45273 ? 359  ASP A CA    1 
ATOM   2837 C C     . ASP A 1 365 ? -14.02987 -8.69408  -4.06146  1.000 22.70878 ? 359  ASP A C     1 
ATOM   2838 O O     . ASP A 1 365 ? -13.88160 -7.65004  -4.70842  1.000 23.15315 ? 359  ASP A O     1 
ATOM   2839 C CB    . ASP A 1 365 ? -13.55423 -10.07304 -6.09200  1.000 24.24425 ? 359  ASP A CB    1 
ATOM   2840 C CG    . ASP A 1 365 ? -15.00948 -10.37572 -6.49033  1.000 35.64970 ? 359  ASP A CG    1 
ATOM   2841 O OD1   . ASP A 1 365 ? -15.32481 -10.31548 -7.69436  1.000 31.91940 ? 359  ASP A OD1   1 
ATOM   2842 O OD2   . ASP A 1 365 ? -15.86587 -10.57229 -5.59036  1.000 32.81482 ? 359  ASP A OD2   1 
ATOM   2843 N N     . CYS A 1 366 ? -14.76837 -8.72413  -2.95082  1.000 22.63712 ? 360  CYS A N     1 
ATOM   2844 C CA    . CYS A 1 366 ? -15.52950 -7.52582  -2.62273  1.000 22.24752 ? 360  CYS A CA    1 
ATOM   2845 C C     . CYS A 1 366 ? -15.98413 -7.58034  -1.17080  1.000 24.15994 ? 360  CYS A C     1 
ATOM   2846 O O     . CYS A 1 366 ? -15.93631 -8.62687  -0.50672  1.000 22.61032 ? 360  CYS A O     1 
ATOM   2847 C CB    . CYS A 1 366 ? -16.76402 -7.35148  -3.51858  1.000 22.67122 ? 360  CYS A CB    1 
ATOM   2848 S SG    . CYS A 1 366 ? -17.93510 -8.76655  -3.30685  1.000 27.55570 ? 360  CYS A SG    1 
ATOM   2849 N N     . VAL A 1 367 ? -16.34318 -6.39377  -0.68363  1.000 23.06165 ? 361  VAL A N     1 
ATOM   2850 C CA    . VAL A 1 367 ? -17.05904 -6.17736  0.56287   1.000 24.17624 ? 361  VAL A CA    1 
ATOM   2851 C C     . VAL A 1 367 ? -18.48120 -5.84413  0.13641   1.000 25.37103 ? 361  VAL A C     1 
ATOM   2852 O O     . VAL A 1 367 ? -18.66645 -4.97154  -0.71821  1.000 25.10205 ? 361  VAL A O     1 
ATOM   2853 C CB    . VAL A 1 367 ? -16.44003 -5.00561  1.36036   1.000 18.65310 ? 361  VAL A CB    1 
ATOM   2854 C CG1   . VAL A 1 367 ? -17.44526 -4.44109  2.39143   1.000 24.01997 ? 361  VAL A CG1   1 
ATOM   2855 C CG2   . VAL A 1 367 ? -15.10314 -5.42481  2.00374   1.000 20.52220 ? 361  VAL A CG2   1 
ATOM   2856 N N     . VAL A 1 368 ? -19.48347 -6.54981  0.68871   1.000 25.22622 ? 362  VAL A N     1 
ATOM   2857 C CA    . VAL A 1 368 ? -20.88874 -6.31135  0.34126   1.000 22.69569 ? 362  VAL A CA    1 
ATOM   2858 C C     . VAL A 1 368 ? -21.56069 -5.55561  1.47807   1.000 21.84694 ? 362  VAL A C     1 
ATOM   2859 O O     . VAL A 1 368 ? -21.47401 -5.96854  2.64202   1.000 25.67762 ? 362  VAL A O     1 
ATOM   2860 C CB    . VAL A 1 368 ? -21.65743 -7.61831  0.05812   1.000 21.83003 ? 362  VAL A CB    1 
ATOM   2861 C CG1   . VAL A 1 368 ? -23.06159 -7.27272  -0.50768  1.000 24.60495 ? 362  VAL A CG1   1 
ATOM   2862 C CG2   . VAL A 1 368 ? -20.90239 -8.50082  -0.92807  1.000 25.31625 ? 362  VAL A CG2   1 
ATOM   2863 N N     . THR A 1 369 ? -22.25295 -4.46540  1.14867   1.000 22.73958 ? 363  THR A N     1 
ATOM   2864 C CA    . THR A 1 369 ? -22.99573 -3.73827  2.16723   1.000 25.38785 ? 363  THR A CA    1 
ATOM   2865 C C     . THR A 1 369 ? -24.47435 -4.11815  2.08819   1.000 28.81908 ? 363  THR A C     1 
ATOM   2866 O O     . THR A 1 369 ? -24.92301 -4.79183  1.15129   1.000 25.68650 ? 363  THR A O     1 
ATOM   2867 C CB    . THR A 1 369 ? -22.84467 -2.21493  2.03039   1.000 23.29152 ? 363  THR A CB    1 
ATOM   2868 O OG1   . THR A 1 369 ? -22.77556 -1.82814  0.65462   1.000 23.17114 ? 363  THR A OG1   1 
ATOM   2869 C CG2   . THR A 1 369 ? -21.50380 -1.73992  2.71784   1.000 25.15056 ? 363  THR A CG2   1 
ATOM   2870 N N     . ALA A 1 370 ? -25.23717 -3.62340  3.07674   1.000 27.19311 ? 364  ALA A N     1 
ATOM   2871 C CA    . ALA A 1 370 ? -26.61523 -4.06161  3.26617   1.000 26.98175 ? 364  ALA A CA    1 
ATOM   2872 C C     . ALA A 1 370 ? -27.49649 -3.67457  2.09427   1.000 25.16389 ? 364  ALA A C     1 
ATOM   2873 O O     . ALA A 1 370 ? -28.48506 -4.36201  1.82925   1.000 30.98869 ? 364  ALA A O     1 
ATOM   2874 C CB    . ALA A 1 370 ? -27.18328 -3.49137  4.57134   1.000 27.65582 ? 364  ALA A CB    1 
ATOM   2875 N N     . ASP A 1 371 ? -27.16705 -2.58520  1.38250   1.000 25.93585 ? 365  ASP A N     1 
ATOM   2876 C CA    . ASP A 1 371 ? -27.89388 -2.19658  0.17290   1.000 29.54769 ? 365  ASP A CA    1 
ATOM   2877 C C     . ASP A 1 371 ? -27.63957 -3.16426  -0.99846  1.000 26.00350 ? 365  ASP A C     1 
ATOM   2878 O O     . ASP A 1 371 ? -28.19999 -2.99080  -2.07510  1.000 29.45570 ? 365  ASP A O     1 
ATOM   2879 C CB    . ASP A 1 371 ? -27.54124 -0.75461  -0.24335  1.000 29.57668 ? 365  ASP A CB    1 
ATOM   2880 C CG    . ASP A 1 371 ? -26.02649 -0.52497  -0.41624  1.000 32.34178 ? 365  ASP A CG    1 
ATOM   2881 O OD1   . ASP A 1 371 ? -25.25801 -1.50605  -0.33577  1.000 24.43573 ? 365  ASP A OD1   1 
ATOM   2882 O OD2   . ASP A 1 371 ? -25.61234 0.64013   -0.65188  1.000 30.70953 ? 365  ASP A OD2   1 
ATOM   2883 N N     . GLY A 1 372 ? -26.82408 -4.18883  -0.82180  1.000 26.45854 ? 366  GLY A N     1 
ATOM   2884 C CA    . GLY A 1 372 ? -26.53359 -5.10299  -1.91065  1.000 28.28790 ? 366  GLY A CA    1 
ATOM   2885 C C     . GLY A 1 372 ? -25.34608 -4.71375  -2.77515  1.000 33.09827 ? 366  GLY A C     1 
ATOM   2886 O O     . GLY A 1 372 ? -24.95412 -5.50006  -3.64413  1.000 25.31740 ? 366  GLY A O     1 
ATOM   2887 N N     . VAL A 1 373 ? -24.73161 -3.55007  -2.54282  1.000 25.70272 ? 367  VAL A N     1 
ATOM   2888 C CA    . VAL A 1 373 ? -23.64122 -3.10243  -3.41057  1.000 27.73696 ? 367  VAL A CA    1 
ATOM   2889 C C     . VAL A 1 373 ? -22.38590 -3.91244  -3.10975  1.000 25.15624 ? 367  VAL A C     1 
ATOM   2890 O O     . VAL A 1 373 ? -21.99584 -4.05464  -1.94948  1.000 22.14769 ? 367  VAL A O     1 
ATOM   2891 C CB    . VAL A 1 373 ? -23.37669 -1.60585  -3.22350  1.000 25.47689 ? 367  VAL A CB    1 
ATOM   2892 C CG1   . VAL A 1 373 ? -22.07780 -1.18362  -3.93168  1.000 24.34386 ? 367  VAL A CG1   1 
ATOM   2893 C CG2   . VAL A 1 373 ? -24.52872 -0.78969  -3.75220  1.000 26.98990 ? 367  VAL A CG2   1 
ATOM   2894 N N     . GLU A 1 374 ? -21.74062 -4.42403  -4.16549  1.000 23.26175 ? 368  GLU A N     1 
ATOM   2895 C CA    . GLU A 1 374 ? -20.45473 -5.11629  -4.06189  1.000 24.71833 ? 368  GLU A CA    1 
ATOM   2896 C C     . GLU A 1 374 ? -19.35561 -4.08574  -4.30696  1.000 25.64543 ? 368  GLU A C     1 
ATOM   2897 O O     . GLU A 1 374 ? -19.22907 -3.56422  -5.42052  1.000 22.15128 ? 368  GLU A O     1 
ATOM   2898 C CB    . GLU A 1 374 ? -20.38066 -6.24216  -5.09011  1.000 26.29883 ? 368  GLU A CB    1 
ATOM   2899 C CG    . GLU A 1 374 ? -21.44297 -7.31451  -4.88981  1.000 26.27623 ? 368  GLU A CG    1 
ATOM   2900 C CD    . GLU A 1 374 ? -21.23091 -8.55847  -5.75748  1.000 39.12908 ? 368  GLU A CD    1 
ATOM   2901 O OE1   . GLU A 1 374 ? -20.45168 -8.48432  -6.74080  1.000 32.48330 ? 368  GLU A OE1   1 
ATOM   2902 O OE2   . GLU A 1 374 ? -21.86593 -9.59721  -5.45187  1.000 36.33796 ? 368  GLU A OE2   1 
ATOM   2903 N N     . HIS A 1 375 ? -18.58451 -3.77406  -3.25934  1.000 23.26797 ? 369  HIS A N     1 
ATOM   2904 C CA    . HIS A 1 375 ? -17.42726 -2.89122  -3.35862  1.000 23.49227 ? 369  HIS A CA    1 
ATOM   2905 C C     . HIS A 1 375 ? -16.22866 -3.75245  -3.72662  1.000 21.22983 ? 369  HIS A C     1 
ATOM   2906 O O     . HIS A 1 375 ? -15.70346 -4.48327  -2.89178  1.000 19.93825 ? 369  HIS A O     1 
ATOM   2907 C CB    . HIS A 1 375 ? -17.20035 -2.15902  -2.03635  1.000 22.49963 ? 369  HIS A CB    1 
ATOM   2908 C CG    . HIS A 1 375 ? -18.41562 -1.42669  -1.57618  1.000 22.99213 ? 369  HIS A CG    1 
ATOM   2909 N ND1   . HIS A 1 375 ? -18.66882 -0.11974  -1.92352  1.000 23.68755 ? 369  HIS A ND1   1 
ATOM   2910 C CD2   . HIS A 1 375 ? -19.46769 -1.83342  -0.82770  1.000 23.64634 ? 369  HIS A CD2   1 
ATOM   2911 C CE1   . HIS A 1 375 ? -19.82586 0.25165   -1.40492  1.000 32.68315 ? 369  HIS A CE1   1 
ATOM   2912 N NE2   . HIS A 1 375 ? -20.33588 -0.77442  -0.74552  1.000 29.80300 ? 369  HIS A NE2   1 
ATOM   2913 N N     . LYS A 1 376 ? -15.81183 -3.66665  -4.98270  1.000 22.17941 ? 370  LYS A N     1 
ATOM   2914 C CA    . LYS A 1 376 ? -14.74960 -4.53847  -5.47457  1.000 23.09413 ? 370  LYS A CA    1 
ATOM   2915 C C     . LYS A 1 376 ? -13.41522 -4.03604  -4.95855  1.000 21.00259 ? 370  LYS A C     1 
ATOM   2916 O O     . LYS A 1 376 ? -13.09946 -2.84794  -5.09758  1.000 20.00622 ? 370  LYS A O     1 
ATOM   2917 C CB    . LYS A 1 376 ? -14.77856 -4.54640  -6.99000  1.000 21.96810 ? 370  LYS A CB    1 
ATOM   2918 C CG    . LYS A 1 376 ? -15.98842 -5.34118  -7.53421  1.000 22.05800 ? 370  LYS A CG    1 
ATOM   2919 C CD    . LYS A 1 376 ? -15.92281 -5.38817  -9.04898  1.000 29.44369 ? 370  LYS A CD    1 
ATOM   2920 C CE    . LYS A 1 376 ? -17.16599 -6.03995  -9.68757  1.000 27.55385 ? 370  LYS A CE    1 
ATOM   2921 N NZ    . LYS A 1 376 ? -17.19546 -7.51829  -9.49304  1.000 26.02718 ? 370  LYS A NZ    1 
ATOM   2922 N N     . LEU A 1 377 ? -12.62923 -4.93629  -4.36259  1.000 20.53972 ? 371  LEU A N     1 
ATOM   2923 C CA    . LEU A 1 377 ? -11.37337 -4.54860  -3.72451  1.000 22.32437 ? 371  LEU A CA    1 
ATOM   2924 C C     . LEU A 1 377 ? -10.23519 -5.49128  -4.09699  1.000 23.38278 ? 371  LEU A C     1 
ATOM   2925 O O     . LEU A 1 377 ? -10.40741 -6.72183  -4.13845  1.000 21.88788 ? 371  LEU A O     1 
ATOM   2926 C CB    . LEU A 1 377 ? -11.50156 -4.54672  -2.20125  1.000 20.91500 ? 371  LEU A CB    1 
ATOM   2927 C CG    . LEU A 1 377 ? -12.50241 -3.56232  -1.59010  1.000 19.99369 ? 371  LEU A CG    1 
ATOM   2928 C CD1   . LEU A 1 377 ? -12.48466 -3.79478  -0.08275  1.000 19.53720 ? 371  LEU A CD1   1 
ATOM   2929 C CD2   . LEU A 1 377 ? -12.19963 -2.09253  -1.92850  1.000 18.43366 ? 371  LEU A CD2   1 
ATOM   2930 N N     . ASP A 1 378 ? -9.06428  -4.90083  -4.32096  1.000 18.88308 ? 372  ASP A N     1 
ATOM   2931 C CA    . ASP A 1 378 ? -7.80940  -5.64550  -4.40426  1.000 21.54286 ? 372  ASP A CA    1 
ATOM   2932 C C     . ASP A 1 378 ? -7.14407  -5.85753  -3.04904  1.000 24.30174 ? 372  ASP A C     1 
ATOM   2933 O O     . ASP A 1 378 ? -6.32147  -6.77381  -2.89544  1.000 21.90513 ? 372  ASP A O     1 
ATOM   2934 C CB    . ASP A 1 378 ? -6.85151  -4.88423  -5.30944  1.000 19.06468 ? 372  ASP A CB    1 
ATOM   2935 C CG    . ASP A 1 378 ? -7.39126  -4.79726  -6.71804  1.000 23.34981 ? 372  ASP A CG    1 
ATOM   2936 O OD1   . ASP A 1 378 ? -7.58874  -5.86825  -7.32134  1.000 23.63326 ? 372  ASP A OD1   1 
ATOM   2937 O OD2   . ASP A 1 378 ? -7.57475  -3.67049  -7.23192  1.000 23.66765 ? 372  ASP A OD2   1 
ATOM   2938 N N     . MET A 1 379 ? -7.47789  -5.02703  -2.08356  1.000 19.66541 ? 373  MET A N     1 
ATOM   2939 C CA    . MET A 1 379 ? -6.80676  -4.97802  -0.79783  1.000 19.26614 ? 373  MET A CA    1 
ATOM   2940 C C     . MET A 1 379 ? -7.80729  -4.47210  0.21940   1.000 19.21507 ? 373  MET A C     1 
ATOM   2941 O O     . MET A 1 379 ? -8.54020  -3.50911  -0.05894  1.000 19.00827 ? 373  MET A O     1 
ATOM   2942 C CB    . MET A 1 379 ? -5.55230  -4.06603  -0.88315  1.000 20.49734 ? 373  MET A CB    1 
ATOM   2943 C CG    . MET A 1 379 ? -4.82962  -4.00420  0.41316   1.000 22.69286 ? 373  MET A CG    1 
ATOM   2944 S SD    . MET A 1 379 ? -3.54371  -2.70511  0.40960   1.000 25.00543 ? 373  MET A SD    1 
ATOM   2945 C CE    . MET A 1 379 ? -2.51075  -3.32555  -0.90251  1.000 28.55826 ? 373  MET A CE    1 
ATOM   2946 N N     . LEU A 1 380 ? -7.85786  -5.13170  1.37986   1.000 19.17643 ? 374  LEU A N     1 
ATOM   2947 C CA    . LEU A 1 380 ? -8.71948  -4.72680  2.48147   1.000 19.47888 ? 374  LEU A CA    1 
ATOM   2948 C C     . LEU A 1 380 ? -7.87652  -4.56910  3.73341   1.000 18.74800 ? 374  LEU A C     1 
ATOM   2949 O O     . LEU A 1 380 ? -7.23451  -5.52714  4.18403   1.000 21.47561 ? 374  LEU A O     1 
ATOM   2950 C CB    . LEU A 1 380 ? -9.85116  -5.75650  2.71887   1.000 19.55250 ? 374  LEU A CB    1 
ATOM   2951 C CG    . LEU A 1 380 ? -10.84942 -5.37201  3.82262   1.000 24.92119 ? 374  LEU A CG    1 
ATOM   2952 C CD1   . LEU A 1 380 ? -11.57437 -4.02727  3.56142   1.000 19.73801 ? 374  LEU A CD1   1 
ATOM   2953 C CD2   . LEU A 1 380 ? -11.81333 -6.57261  4.05903   1.000 20.13185 ? 374  LEU A CD2   1 
ATOM   2954 N N     . ILE A 1 381 ? -7.83393  -3.34605  4.27111   1.000 18.93648 ? 375  ILE A N     1 
ATOM   2955 C CA    . ILE A 1 381 ? -7.03309  -3.03292  5.44841   1.000 19.36611 ? 375  ILE A CA    1 
ATOM   2956 C C     . ILE A 1 381 ? -7.92665  -2.94848  6.66421   1.000 21.98463 ? 375  ILE A C     1 
ATOM   2957 O O     . ILE A 1 381 ? -8.85811  -2.14584  6.69150   1.000 18.56261 ? 375  ILE A O     1 
ATOM   2958 C CB    . ILE A 1 381 ? -6.26218  -1.71584  5.26355   1.000 19.51747 ? 375  ILE A CB    1 
ATOM   2959 C CG1   . ILE A 1 381 ? -5.41170  -1.78972  4.00879   1.000 22.77817 ? 375  ILE A CG1   1 
ATOM   2960 C CG2   . ILE A 1 381 ? -5.44645  -1.41172  6.49564   1.000 20.47375 ? 375  ILE A CG2   1 
ATOM   2961 C CD1   . ILE A 1 381 ? -4.77437  -0.44760  3.63523   1.000 21.60005 ? 375  ILE A CD1   1 
ATOM   2962 N N     . CYS A 1 382 ? -7.64037  -3.75914  7.68257   1.000 20.58914 ? 376  CYS A N     1 
ATOM   2963 C CA    . CYS A 1 382 ? -8.44266  -3.73965  8.90194   1.000 23.39215 ? 376  CYS A CA    1 
ATOM   2964 C C     . CYS A 1 382 ? -7.72256  -2.90397  9.93615   1.000 23.47519 ? 376  CYS A C     1 
ATOM   2965 O O     . CYS A 1 382 ? -6.78401  -3.38194  10.57486  1.000 21.66138 ? 376  CYS A O     1 
ATOM   2966 C CB    . CYS A 1 382 ? -8.70080  -5.14293  9.43019   1.000 23.92378 ? 376  CYS A CB    1 
ATOM   2967 S SG    . CYS A 1 382 ? -9.75416  -6.01902  8.24397   1.000 28.85649 ? 376  CYS A SG    1 
ATOM   2968 N N     . ALA A 1 383 ? -8.16924  -1.65947  10.08135  1.000 19.80718 ? 377  ALA A N     1 
ATOM   2969 C CA    . ALA A 1 383 ? -7.72592  -0.77382  11.15962  1.000 21.88905 ? 377  ALA A CA    1 
ATOM   2970 C C     . ALA A 1 383 ? -8.68552  -0.87403  12.34174  1.000 24.08542 ? 377  ALA A C     1 
ATOM   2971 O O     . ALA A 1 383 ? -9.19059  0.13126   12.84545  1.000 22.14298 ? 377  ALA A O     1 
ATOM   2972 C CB    . ALA A 1 383 ? -7.63395  0.66251   10.63816  1.000 21.76360 ? 377  ALA A CB    1 
ATOM   2973 N N     . THR A 1 384 ? -9.00606  -2.10767  12.75468  1.000 23.47115 ? 378  THR A N     1 
ATOM   2974 C CA    . THR A 1 384 ? -10.15186 -2.33831  13.62728  1.000 23.88925 ? 378  THR A CA    1 
ATOM   2975 C C     . THR A 1 384 ? -9.78512  -2.47861  15.10506  1.000 26.95105 ? 378  THR A C     1 
ATOM   2976 O O     . THR A 1 384 ? -10.63400 -2.88580  15.90771  1.000 26.72403 ? 378  THR A O     1 
ATOM   2977 C CB    . THR A 1 384 ? -10.92760 -3.57267  13.14651  1.000 23.65379 ? 378  THR A CB    1 
ATOM   2978 O OG1   . THR A 1 384 ? -10.00866 -4.61073  12.80299  1.000 25.34675 ? 378  THR A OG1   1 
ATOM   2979 C CG2   . THR A 1 384 ? -11.68962 -3.19630  11.89589  1.000 22.33367 ? 378  THR A CG2   1 
ATOM   2980 N N     . GLY A 1 385 ? -8.56325  -2.13813  15.48908  1.000 24.03958 ? 379  GLY A N     1 
ATOM   2981 C CA    . GLY A 1 385 ? -8.25687  -2.01776  16.90635  1.000 27.00181 ? 379  GLY A CA    1 
ATOM   2982 C C     . GLY A 1 385 ? -7.73991  -3.29698  17.53483  1.000 26.70292 ? 379  GLY A C     1 
ATOM   2983 O O     . GLY A 1 385 ? -7.33092  -4.24503  16.86284  1.000 27.69099 ? 379  GLY A O     1 
ATOM   2984 N N     . PHE A 1 386 ? -7.76466  -3.30134  18.87641  1.000 25.18866 ? 380  PHE A N     1 
ATOM   2985 C CA    . PHE A 1 386 ? -7.10774  -4.31409  19.69321  1.000 28.01756 ? 380  PHE A CA    1 
ATOM   2986 C C     . PHE A 1 386 ? -7.97089  -4.66017  20.89846  1.000 35.31677 ? 380  PHE A C     1 
ATOM   2987 O O     . PHE A 1 386 ? -8.81769  -3.87586  21.31925  1.000 38.11544 ? 380  PHE A O     1 
ATOM   2988 C CB    . PHE A 1 386 ? -5.75489  -3.82646  20.20386  1.000 28.57055 ? 380  PHE A CB    1 
ATOM   2989 C CG    . PHE A 1 386 ? -4.79520  -3.48270  19.12044  1.000 27.79675 ? 380  PHE A CG    1 
ATOM   2990 C CD1   . PHE A 1 386 ? -4.84866  -2.22766  18.50843  1.000 26.52949 ? 380  PHE A CD1   1 
ATOM   2991 C CD2   . PHE A 1 386 ? -3.83206  -4.38675  18.72365  1.000 26.31631 ? 380  PHE A CD2   1 
ATOM   2992 C CE1   . PHE A 1 386 ? -3.96457  -1.89873  17.50630  1.000 28.09171 ? 380  PHE A CE1   1 
ATOM   2993 C CE2   . PHE A 1 386 ? -2.93177  -4.05562  17.73287  1.000 29.88509 ? 380  PHE A CE2   1 
ATOM   2994 C CZ    . PHE A 1 386 ? -2.99871  -2.79714  17.12816  1.000 27.42357 ? 380  PHE A CZ    1 
ATOM   2995 N N     . ASP A 1 387 ? -7.72064  -5.83873  21.47259  1.000 38.73759 ? 381  ASP A N     1 
ATOM   2996 C CA    . ASP A 1 387 ? -8.31374  -6.17984  22.76131  1.000 39.60403 ? 381  ASP A CA    1 
ATOM   2997 C C     . ASP A 1 387 ? -7.73818  -5.28232  23.86700  1.000 42.00405 ? 381  ASP A C     1 
ATOM   2998 O O     . ASP A 1 387 ? -6.65226  -4.71965  23.72890  1.000 36.12624 ? 381  ASP A O     1 
ATOM   2999 C CB    . ASP A 1 387 ? -8.07882  -7.66086  23.06517  1.000 38.03744 ? 381  ASP A CB    1 
ATOM   3000 C CG    . ASP A 1 387 ? -8.71540  -8.56349  22.02324  1.000 49.93659 ? 381  ASP A CG    1 
ATOM   3001 O OD1   . ASP A 1 387 ? -9.72710  -8.12931  21.41832  1.000 43.00967 ? 381  ASP A OD1   1 
ATOM   3002 O OD2   . ASP A 1 387 ? -8.21440  -9.69346  21.81209  1.000 54.11085 ? 381  ASP A OD2   1 
ATOM   3003 N N     . ALA A 1 388 ? -8.49098  -5.14421  24.97042  1.000 38.43873 ? 382  ALA A N     1 
ATOM   3004 C CA    . ALA A 1 388 ? -8.16706  -4.16989  26.01527  1.000 40.89659 ? 382  ALA A CA    1 
ATOM   3005 C C     . ALA A 1 388 ? -6.88368  -4.55516  26.76011  1.000 38.76897 ? 382  ALA A C     1 
ATOM   3006 O O     . ALA A 1 388 ? -6.33486  -5.64637  26.59097  1.000 38.94023 ? 382  ALA A O     1 
ATOM   3007 C CB    . ALA A 1 388 ? -9.32825  -4.01294  27.00035  1.000 43.24400 ? 382  ALA A CB    1 
ATOM   3008 N N     . VAL A 1 389 ? -6.41274  -3.62898  27.60621  1.000 37.94641 ? 383  VAL A N     1 
ATOM   3009 C CA    . VAL A 1 389 ? -5.06267  -3.73032  28.17025  1.000 40.81220 ? 383  VAL A CA    1 
ATOM   3010 C C     . VAL A 1 389 ? -4.87724  -5.02538  28.96191  1.000 40.39741 ? 383  VAL A C     1 
ATOM   3011 O O     . VAL A 1 389 ? -3.79520  -5.63456  28.93762  1.000 42.11059 ? 383  VAL A O     1 
ATOM   3012 C CB    . VAL A 1 389 ? -4.75145  -2.48585  29.02881  1.000 41.46629 ? 383  VAL A CB    1 
ATOM   3013 C CG1   . VAL A 1 389 ? -5.84819  -2.24228  30.05361  1.000 43.21353 ? 383  VAL A CG1   1 
ATOM   3014 C CG2   . VAL A 1 389 ? -3.39774  -2.63577  29.72974  1.000 40.40827 ? 383  VAL A CG2   1 
ATOM   3015 N N     . ASP A 1 390 ? -5.91735  -5.46782  29.67886  1.000 42.87170 ? 384  ASP A N     1 
ATOM   3016 C CA    . ASP A 1 390 ? -5.78502  -6.63424  30.55223  1.000 46.82093 ? 384  ASP A CA    1 
ATOM   3017 C C     . ASP A 1 390 ? -5.62511  -7.92854  29.76819  1.000 41.46908 ? 384  ASP A C     1 
ATOM   3018 O O     . ASP A 1 390 ? -5.22881  -8.94569  30.35372  1.000 39.77356 ? 384  ASP A O     1 
ATOM   3019 C CB    . ASP A 1 390 ? -7.00006  -6.77045  31.49103  1.000 46.00050 ? 384  ASP A CB    1 
ATOM   3020 C CG    . ASP A 1 390 ? -8.33582  -6.63418  30.76299  1.000 52.67739 ? 384  ASP A CG    1 
ATOM   3021 O OD1   . ASP A 1 390 ? -8.65163  -5.52602  30.26090  1.000 47.14835 ? 384  ASP A OD1   1 
ATOM   3022 O OD2   . ASP A 1 390 ? -9.07182  -7.65168  30.70382  1.000 57.50865 ? 384  ASP A OD2   1 
ATOM   3023 N N     . GLY A 1 391 ? -5.92276  -7.90730  28.46434  1.000 41.68652 ? 385  GLY A N     1 
ATOM   3024 C CA    . GLY A 1 391 ? -5.75560  -9.09804  27.64387  1.000 40.24116 ? 385  GLY A CA    1 
ATOM   3025 C C     . GLY A 1 391 ? -4.31733  -9.57449  27.54194  1.000 37.00568 ? 385  GLY A C     1 
ATOM   3026 O O     . GLY A 1 391 ? -4.06246  -10.77032 27.40506  1.000 38.76530 ? 385  GLY A O     1 
ATOM   3027 N N     . SER A 1 392 ? -3.35394  -8.65428  27.57293  1.000 31.87717 ? 386  SER A N     1 
ATOM   3028 C CA    . SER A 1 392 ? -1.96973  -9.11136  27.51275  1.000 32.64294 ? 386  SER A CA    1 
ATOM   3029 C C     . SER A 1 392 ? -1.59475  -9.88159  28.76891  1.000 31.85373 ? 386  SER A C     1 
ATOM   3030 O O     . SER A 1 392 ? -0.73434  -10.77125 28.72405  1.000 31.14234 ? 386  SER A O     1 
ATOM   3031 C CB    . SER A 1 392 ? -1.02607  -7.93650  27.30564  1.000 38.84104 ? 386  SER A CB    1 
ATOM   3032 O OG    . SER A 1 392 ? -1.29223  -7.29818  26.06857  1.000 34.06298 ? 386  SER A OG    1 
ATOM   3033 N N     . TYR A 1 393 ? -2.22766  -9.54429  29.88917  1.000 30.13479 ? 387  TYR A N     1 
ATOM   3034 C CA    . TYR A 1 393 ? -2.02475  -10.26329 31.14353  1.000 29.73257 ? 387  TYR A CA    1 
ATOM   3035 C C     . TYR A 1 393 ? -2.76284  -11.60174 31.13789  1.000 38.67025 ? 387  TYR A C     1 
ATOM   3036 O O     . TYR A 1 393 ? -2.19337  -12.64318 31.48926  1.000 40.08885 ? 387  TYR A O     1 
ATOM   3037 C CB    . TYR A 1 393 ? -2.49789  -9.38836  32.29852  1.000 35.55483 ? 387  TYR A CB    1 
ATOM   3038 C CG    . TYR A 1 393 ? -1.43122  -8.36355  32.62907  1.000 34.48655 ? 387  TYR A CG    1 
ATOM   3039 C CD1   . TYR A 1 393 ? -0.41401  -8.66777  33.51136  1.000 32.63611 ? 387  TYR A CD1   1 
ATOM   3040 C CD2   . TYR A 1 393 ? -1.41587  -7.11872  31.99799  1.000 36.92875 ? 387  TYR A CD2   1 
ATOM   3041 C CE1   . TYR A 1 393 ? 0.58278   -7.74916  33.79292  1.000 36.99341 ? 387  TYR A CE1   1 
ATOM   3042 C CE2   . TYR A 1 393 ? -0.41303  -6.19046  32.26296  1.000 32.07022 ? 387  TYR A CE2   1 
ATOM   3043 C CZ    . TYR A 1 393 ? 0.57519   -6.51283  33.16549  1.000 30.27699 ? 387  TYR A CZ    1 
ATOM   3044 O OH    . TYR A 1 393 ? 1.57637   -5.62297  33.43592  1.000 31.19542 ? 387  TYR A OH    1 
ATOM   3045 N N     . LYS A 1 394 ? -4.03353  -11.58783 30.73443  1.000 34.05359 ? 388  LYS A N     1 
ATOM   3046 C CA    . LYS A 1 394 ? -4.83797  -12.80470 30.75062  1.000 39.48573 ? 388  LYS A CA    1 
ATOM   3047 C C     . LYS A 1 394 ? -4.37492  -13.82010 29.71901  1.000 44.03745 ? 388  LYS A C     1 
ATOM   3048 O O     . LYS A 1 394 ? -4.71991  -14.99864 29.84183  1.000 49.09451 ? 388  LYS A O     1 
ATOM   3049 C CB    . LYS A 1 394 ? -6.30495  -12.47110 30.51145  1.000 36.42352 ? 388  LYS A CB    1 
ATOM   3050 C CG    . LYS A 1 394 ? -6.92485  -11.67796 31.62225  1.000 35.76829 ? 388  LYS A CG    1 
ATOM   3051 C CD    . LYS A 1 394 ? -8.16539  -11.00523 31.13247  1.000 40.19900 ? 388  LYS A CD    1 
ATOM   3052 C CE    . LYS A 1 394 ? -9.24883  -10.99345 32.17938  1.000 50.22295 ? 388  LYS A CE    1 
ATOM   3053 N NZ    . LYS A 1 394 ? -10.51573 -10.45288 31.61768  1.000 47.74370 ? 388  LYS A NZ    1 
ATOM   3054 N N     . ARG A 1 395 ? -3.61452  -13.39620 28.70417  1.000 35.99669 ? 389  ARG A N     1 
ATOM   3055 C CA    . ARG A 1 395 ? -3.10544  -14.33407 27.71261  1.000 36.71909 ? 389  ARG A CA    1 
ATOM   3056 C C     . ARG A 1 395 ? -1.83283  -15.02962 28.16213  1.000 40.55433 ? 389  ARG A C     1 
ATOM   3057 O O     . ARG A 1 395 ? -1.36636  -15.93270 27.46549  1.000 43.39557 ? 389  ARG A O     1 
ATOM   3058 C CB    . ARG A 1 395 ? -2.88040  -13.62172 26.37650  1.000 39.54267 ? 389  ARG A CB    1 
ATOM   3059 C CG    . ARG A 1 395 ? -4.20550  -13.30011 25.70988  1.000 54.00821 ? 389  ARG A CG    1 
ATOM   3060 C CD    . ARG A 1 395 ? -4.10355  -12.88067 24.25944  1.000 56.28503 ? 389  ARG A CD    1 
ATOM   3061 N NE    . ARG A 1 395 ? -5.40852  -12.43551 23.77063  1.000 67.30195 ? 389  ARG A NE    1 
ATOM   3062 C CZ    . ARG A 1 395 ? -6.39788  -13.23719 23.39409  1.000 73.80683 ? 389  ARG A CZ    1 
ATOM   3063 N NH1   . ARG A 1 395 ? -6.26569  -14.55486 23.40633  1.000 71.57837 ? 389  ARG A NH1   1 
ATOM   3064 N NH2   . ARG A 1 395 ? -7.55081  -12.70239 22.99811  1.000 74.78589 ? 389  ARG A NH2   1 
ATOM   3065 N N     . ILE A 1 396 ? -1.25759  -14.63604 29.29759  1.000 37.74188 ? 390  ILE A N     1 
ATOM   3066 C CA    . ILE A 1 396 ? -0.22167  -15.41362 29.96376  1.000 34.56229 ? 390  ILE A CA    1 
ATOM   3067 C C     . ILE A 1 396 ? -0.87385  -16.17779 31.10780  1.000 35.93284 ? 390  ILE A C     1 
ATOM   3068 O O     . ILE A 1 396 ? -1.74563  -15.64808 31.80622  1.000 38.91864 ? 390  ILE A O     1 
ATOM   3069 C CB    . ILE A 1 396 ? 0.91845   -14.51904 30.49563  1.000 34.36856 ? 390  ILE A CB    1 
ATOM   3070 C CG1   . ILE A 1 396 ? 1.28690   -13.44256 29.47001  1.000 38.99049 ? 390  ILE A CG1   1 
ATOM   3071 C CG2   . ILE A 1 396 ? 2.15116   -15.37514 30.81960  1.000 37.30088 ? 390  ILE A CG2   1 
ATOM   3072 C CD1   . ILE A 1 396 ? 2.40735   -12.48667 29.95468  1.000 34.22261 ? 390  ILE A CD1   1 
ATOM   3073 N N     . ASP A 1 397 ? -0.44307  -17.41432 31.31846  1.000 36.14798 ? 391  ASP A N     1 
ATOM   3074 C CA    . ASP A 1 397 ? -0.94269  -18.19950 32.44748  1.000 39.37601 ? 391  ASP A CA    1 
ATOM   3075 C C     . ASP A 1 397 ? -0.18298  -17.76939 33.69141  1.000 34.10029 ? 391  ASP A C     1 
ATOM   3076 O O     . ASP A 1 397 ? 0.83047   -18.35588 34.05648  1.000 37.58021 ? 391  ASP A O     1 
ATOM   3077 C CB    . ASP A 1 397 ? -0.79331  -19.69232 32.18388  1.000 39.00441 ? 391  ASP A CB    1 
ATOM   3078 C CG    . ASP A 1 397 ? -1.56189  -20.53787 33.18748  1.000 47.40784 ? 391  ASP A CG    1 
ATOM   3079 O OD1   . ASP A 1 397 ? -2.40311  -19.97808 33.93043  1.000 49.90232 ? 391  ASP A OD1   1 
ATOM   3080 O OD2   . ASP A 1 397 ? -1.32264  -21.76123 33.23188  1.000 50.22925 ? 391  ASP A OD2   1 
ATOM   3081 N N     . ILE A 1 398 ? -0.67459  -16.71998 34.34280  1.000 38.05678 ? 392  ILE A N     1 
ATOM   3082 C CA    . ILE A 1 398 ? -0.03753  -16.16939 35.53595  1.000 40.61857 ? 392  ILE A CA    1 
ATOM   3083 C C     . ILE A 1 398 ? -0.81612  -16.65244 36.74802  1.000 37.96051 ? 392  ILE A C     1 
ATOM   3084 O O     . ILE A 1 398 ? -2.00023  -16.32676 36.89755  1.000 44.02301 ? 392  ILE A O     1 
ATOM   3085 C CB    . ILE A 1 398 ? -0.00001  -14.63135 35.50749  1.000 41.08936 ? 392  ILE A CB    1 
ATOM   3086 C CG1   . ILE A 1 398 ? 0.58601   -14.11581 34.18957  1.000 33.62725 ? 392  ILE A CG1   1 
ATOM   3087 C CG2   . ILE A 1 398 ? 0.78952   -14.10895 36.72310  1.000 38.55933 ? 392  ILE A CG2   1 
ATOM   3088 C CD1   . ILE A 1 398 ? 0.84490   -12.60038 34.17247  1.000 38.20873 ? 392  ILE A CD1   1 
ATOM   3089 N N     . ARG A 1 399 ? -0.15616  -17.39896 37.62794  1.000 39.42812 ? 393  ARG A N     1 
ATOM   3090 C CA    . ARG A 1 399 ? -0.80738  -17.93634 38.81553  1.000 48.52070 ? 393  ARG A CA    1 
ATOM   3091 C C     . ARG A 1 399 ? -0.08576  -17.41286 40.04687  1.000 40.30253 ? 393  ARG A C     1 
ATOM   3092 O O     . ARG A 1 399 ? 1.12532   -17.61441 40.19096  1.000 38.11855 ? 393  ARG A O     1 
ATOM   3093 C CB    . ARG A 1 399 ? -0.82313  -19.46689 38.79870  1.000 45.21970 ? 393  ARG A CB    1 
ATOM   3094 C CG    . ARG A 1 399 ? -1.60026  -20.02665 37.60938  1.000 49.24634 ? 393  ARG A CG    1 
ATOM   3095 C CD    . ARG A 1 399 ? -1.91266  -21.51232 37.72728  1.000 56.70793 ? 393  ARG A CD    1 
ATOM   3096 N NE    . ARG A 1 399 ? -3.35242  -21.73814 37.72349  1.000 63.43642 ? 393  ARG A NE    1 
ATOM   3097 C CZ    . ARG A 1 399 ? -4.09618  -21.77086 36.62471  1.000 63.92792 ? 393  ARG A CZ    1 
ATOM   3098 N NH1   . ARG A 1 399 ? -3.55239  -21.70522 35.41910  1.000 61.53224 ? 393  ARG A NH1   1 
ATOM   3099 N NH2   . ARG A 1 399 ? -5.41741  -21.88630 36.73739  1.000 66.41244 ? 393  ARG A NH2   1 
ATOM   3100 N N     . GLY A 1 400 ? -0.82907  -16.73583 40.92123  1.000 40.22867 ? 394  GLY A N     1 
ATOM   3101 C CA    . GLY A 1 400 ? -0.27400  -16.20990 42.15394  1.000 41.20729 ? 394  GLY A CA    1 
ATOM   3102 C C     . GLY A 1 400 ? -0.59267  -17.04845 43.37561  1.000 49.02367 ? 394  GLY A C     1 
ATOM   3103 O O     . GLY A 1 400 ? -0.45310  -18.27385 43.33934  1.000 51.09295 ? 394  GLY A O     1 
ATOM   3104 N N     . LYS A 1 401 ? -1.01294  -16.40075 44.46265  1.000 52.59959 ? 395  LYS A N     1 
ATOM   3105 C CA    . LYS A 1 401 ? -1.29931  -17.11285 45.70465  1.000 53.55466 ? 395  LYS A CA    1 
ATOM   3106 C C     . LYS A 1 401 ? -2.47965  -18.06458 45.53809  1.000 54.18807 ? 395  LYS A C     1 
ATOM   3107 O O     . LYS A 1 401 ? -3.46201  -17.75649 44.85259  1.000 51.40511 ? 395  LYS A O     1 
ATOM   3108 C CB    . LYS A 1 401 ? -1.57807  -16.11855 46.83583  1.000 50.56717 ? 395  LYS A CB    1 
ATOM   3109 C CG    . LYS A 1 401 ? -0.33646  -15.43468 47.39639  1.000 50.20321 ? 395  LYS A CG    1 
ATOM   3110 C CD    . LYS A 1 401 ? -0.62708  -14.68292 48.70120  1.000 61.17537 ? 395  LYS A CD    1 
ATOM   3111 C CE    . LYS A 1 401 ? -2.07955  -14.19902 48.75627  1.000 61.77082 ? 395  LYS A CE    1 
ATOM   3112 N NZ    . LYS A 1 401 ? -2.32057  -13.23332 49.86702  1.000 60.90697 ? 395  LYS A NZ    1 
ATOM   3113 N N     . ASP A 1 402 ? -2.37767  -19.23248 46.18038  1.000 55.49427 ? 396  ASP A N     1 
ATOM   3114 C CA    . ASP A 1 402 ? -3.38231  -20.28899 46.10433  1.000 54.99330 ? 396  ASP A CA    1 
ATOM   3115 C C     . ASP A 1 402 ? -3.60715  -20.77854 44.67782  1.000 57.57411 ? 396  ASP A C     1 
ATOM   3116 O O     . ASP A 1 402 ? -4.59547  -21.47439 44.41497  1.000 56.74137 ? 396  ASP A O     1 
ATOM   3117 C CB    . ASP A 1 402 ? -4.71744  -19.84227 46.72629  1.000 51.89670 ? 396  ASP A CB    1 
ATOM   3118 C CG    . ASP A 1 402 ? -4.54007  -19.15909 48.07630  1.000 67.08911 ? 396  ASP A CG    1 
ATOM   3119 O OD1   . ASP A 1 402 ? -5.36504  -18.27694 48.42242  1.000 67.88709 ? 396  ASP A OD1   1 
ATOM   3120 O OD2   . ASP A 1 402 ? -3.59052  -19.53326 48.80420  1.000 70.10970 ? 396  ASP A OD2   1 
ATOM   3121 N N     . GLY A 1 403 ? -2.70995  -20.43562 43.75112  1.000 57.68277 ? 397  GLY A N     1 
ATOM   3122 C CA    . GLY A 1 403 ? -2.83861  -20.80703 42.35688  1.000 53.44562 ? 397  GLY A CA    1 
ATOM   3123 C C     . GLY A 1 403 ? -3.82936  -19.99928 41.54551  1.000 52.16273 ? 397  GLY A C     1 
ATOM   3124 O O     . GLY A 1 403 ? -4.10452  -20.37354 40.40257  1.000 53.78255 ? 397  GLY A O     1 
ATOM   3125 N N     . ILE A 1 404 ? -4.38057  -18.90850 42.08692  1.000 49.42286 ? 398  ILE A N     1 
ATOM   3126 C CA    . ILE A 1 404 ? -5.37744  -18.14167 41.34610  1.000 51.01759 ? 398  ILE A CA    1 
ATOM   3127 C C     . ILE A 1 404 ? -4.75148  -17.58493 40.06898  1.000 51.97877 ? 398  ILE A C     1 
ATOM   3128 O O     . ILE A 1 404 ? -3.57938  -17.18267 40.05537  1.000 46.08845 ? 398  ILE A O     1 
ATOM   3129 C CB    . ILE A 1 404 ? -5.96035  -17.02744 42.23281  1.000 46.84453 ? 398  ILE A CB    1 
ATOM   3130 C CG1   . ILE A 1 404 ? -7.02390  -16.22848 41.47398  1.000 52.58929 ? 398  ILE A CG1   1 
ATOM   3131 C CG2   . ILE A 1 404 ? -4.85940  -16.11146 42.76124  1.000 50.57482 ? 398  ILE A CG2   1 
ATOM   3132 C CD1   . ILE A 1 404 ? -7.45965  -14.95725 42.20511  1.000 57.81272 ? 398  ILE A CD1   1 
ATOM   3133 N N     . SER A 1 405 ? -5.51667  -17.60496 38.97348  1.000 51.14183 ? 399  SER A N     1 
ATOM   3134 C CA    . SER A 1 405 ? -5.06382  -17.09552 37.68469  1.000 50.80812 ? 399  SER A CA    1 
ATOM   3135 C C     . SER A 1 405 ? -5.53652  -15.66181 37.49786  1.000 46.04132 ? 399  SER A C     1 
ATOM   3136 O O     . SER A 1 405 ? -6.57770  -15.26082 38.01936  1.000 50.40793 ? 399  SER A O     1 
ATOM   3137 C CB    . SER A 1 405 ? -5.56533  -17.96362 36.52912  1.000 50.24871 ? 399  SER A CB    1 
ATOM   3138 O OG    . SER A 1 405 ? -6.91139  -17.66594 36.20164  1.000 52.91175 ? 399  SER A OG    1 
ATOM   3139 N N     . ILE A 1 406 ? -4.74865  -14.87997 36.75645  1.000 49.81801 ? 400  ILE A N     1 
ATOM   3140 C CA    . ILE A 1 406 ? -5.15126  -13.50186 36.50929  1.000 44.31670 ? 400  ILE A CA    1 
ATOM   3141 C C     . ILE A 1 406 ? -6.38884  -13.45034 35.62013  1.000 41.16364 ? 400  ILE A C     1 
ATOM   3142 O O     . ILE A 1 406 ? -7.18558  -12.51192 35.72019  1.000 50.23158 ? 400  ILE A O     1 
ATOM   3143 C CB    . ILE A 1 406 ? -3.96685  -12.69230 35.93846  1.000 49.55828 ? 400  ILE A CB    1 
ATOM   3144 C CG1   . ILE A 1 406 ? -3.96955  -11.26857 36.50023  1.000 45.07061 ? 400  ILE A CG1   1 
ATOM   3145 C CG2   . ILE A 1 406 ? -3.95990  -12.70566 34.42131  1.000 45.47769 ? 400  ILE A CG2   1 
ATOM   3146 C CD1   . ILE A 1 406 ? -2.76858  -10.46412 36.10072  1.000 48.49874 ? 400  ILE A CD1   1 
ATOM   3147 N N     . LYS A 1 407 ? -6.59618  -14.45582 34.76326  1.000 48.32502 ? 401  LYS A N     1 
ATOM   3148 C CA    . LYS A 1 407 ? -7.86897  -14.56419 34.05322  1.000 45.77787 ? 401  LYS A CA    1 
ATOM   3149 C C     . LYS A 1 407 ? -9.02756  -14.51861 35.03478  1.000 48.41190 ? 401  LYS A C     1 
ATOM   3150 O O     . LYS A 1 407 ? -9.97116  -13.73886 34.87522  1.000 48.56691 ? 401  LYS A O     1 
ATOM   3151 C CB    . LYS A 1 407 ? -7.93620  -15.86425 33.25587  1.000 47.74370 ? 401  LYS A CB    1 
ATOM   3152 C CG    . LYS A 1 407 ? -6.95153  -15.99147 32.14358  1.000 52.05580 ? 401  LYS A CG    1 
ATOM   3153 C CD    . LYS A 1 407 ? -7.51067  -16.92823 31.07796  1.000 57.09079 ? 401  LYS A CD    1 
ATOM   3154 C CE    . LYS A 1 407 ? -6.66187  -18.16949 30.95736  1.000 59.42608 ? 401  LYS A CE    1 
ATOM   3155 N NZ    . LYS A 1 407 ? -5.24298  -17.81863 30.65016  1.000 64.91972 ? 401  LYS A NZ    1 
ATOM   3156 N N     . ASP A 1 408 ? -8.94722  -15.34671 36.07825  1.000 51.77269 ? 402  ASP A N     1 
ATOM   3157 C CA    . ASP A 1 408 ? -10.01370 -15.43080 37.06809  1.000 50.05783 ? 402  ASP A CA    1 
ATOM   3158 C C     . ASP A 1 408 ? -10.02038 -14.21498 37.98439  1.000 50.21669 ? 402  ASP A C     1 
ATOM   3159 O O     . ASP A 1 408 ? -11.08637 -13.66587 38.28826  1.000 49.82486 ? 402  ASP A O     1 
ATOM   3160 C CB    . ASP A 1 408 ? -9.84508  -16.71084 37.88734  1.000 48.77732 ? 402  ASP A CB    1 
ATOM   3161 C CG    . ASP A 1 408 ? -10.09350 -17.96536 37.07128  1.000 55.60418 ? 402  ASP A CG    1 
ATOM   3162 O OD1   . ASP A 1 408 ? -10.83416 -17.89670 36.06468  1.000 51.56721 ? 402  ASP A OD1   1 
ATOM   3163 O OD2   . ASP A 1 408 ? -9.53806  -19.02090 37.43653  1.000 55.20230 ? 402  ASP A OD2   1 
ATOM   3164 N N     . HIS A 1 409 ? -8.83865  -13.79639 38.45282  1.000 46.26975 ? 403  HIS A N     1 
ATOM   3165 C CA    . HIS A 1 409 ? -8.74681  -12.63204 39.32994  1.000 47.21849 ? 403  HIS A CA    1 
ATOM   3166 C C     . HIS A 1 409 ? -9.34055  -11.38832 38.67046  1.000 46.35901 ? 403  HIS A C     1 
ATOM   3167 O O     . HIS A 1 409 ? -9.98585  -10.56992 39.33856  1.000 46.10840 ? 403  HIS A O     1 
ATOM   3168 C CB    . HIS A 1 409 ? -7.28552  -12.40358 39.72410  1.000 47.18426 ? 403  HIS A CB    1 
ATOM   3169 C CG    . HIS A 1 409 ? -7.08649  -11.30098 40.71844  1.000 54.65526 ? 403  HIS A CG    1 
ATOM   3170 N ND1   . HIS A 1 409 ? -7.36940  -11.44412 42.06062  1.000 53.67821 ? 403  HIS A ND1   1 
ATOM   3171 C CD2   . HIS A 1 409 ? -6.61929  -10.03808 40.56428  1.000 49.99975 ? 403  HIS A CD2   1 
ATOM   3172 C CE1   . HIS A 1 409 ? -7.10000  -10.31136 42.68637  1.000 56.25762 ? 403  HIS A CE1   1 
ATOM   3173 N NE2   . HIS A 1 409 ? -6.64451  -9.44180  41.80094  1.000 51.03120 ? 403  HIS A NE2   1 
ATOM   3174 N N     . TRP A 1 410 ? -9.15318  -11.24451 37.35614  1.000 45.79745 ? 404  TRP A N     1 
ATOM   3175 C CA    . TRP A 1 410 ? -9.61423  -10.08903 36.59147  1.000 49.96916 ? 404  TRP A CA    1 
ATOM   3176 C C     . TRP A 1 410 ? -10.77594 -10.41801 35.65025  1.000 53.04017 ? 404  TRP A C     1 
ATOM   3177 O O     . TRP A 1 410 ? -10.87978 -9.82262  34.57607  1.000 51.44128 ? 404  TRP A O     1 
ATOM   3178 C CB    . TRP A 1 410 ? -8.45449  -9.49550  35.78558  1.000 45.60481 ? 404  TRP A CB    1 
ATOM   3179 C CG    . TRP A 1 410 ? -7.53611  -8.60171  36.55151  1.000 45.23099 ? 404  TRP A CG    1 
ATOM   3180 C CD1   . TRP A 1 410 ? -7.70251  -8.15379  37.82738  1.000 43.40091 ? 404  TRP A CD1   1 
ATOM   3181 C CD2   . TRP A 1 410 ? -6.30080  -8.04083  36.08607  1.000 42.62592 ? 404  TRP A CD2   1 
ATOM   3182 N NE1   . TRP A 1 410 ? -6.65240  -7.34549  38.18292  1.000 45.35267 ? 404  TRP A NE1   1 
ATOM   3183 C CE2   . TRP A 1 410 ? -5.78025  -7.25838  37.12937  1.000 46.05523 ? 404  TRP A CE2   1 
ATOM   3184 C CE3   . TRP A 1 410 ? -5.58621  -8.12501  34.88318  1.000 44.98220 ? 404  TRP A CE3   1 
ATOM   3185 C CZ2   . TRP A 1 410 ? -4.57584  -6.56272  37.01345  1.000 43.82575 ? 404  TRP A CZ2   1 
ATOM   3186 C CZ3   . TRP A 1 410 ? -4.39184  -7.43367  34.76867  1.000 45.18314 ? 404  TRP A CZ3   1 
ATOM   3187 C CH2   . TRP A 1 410 ? -3.89692  -6.66639  35.83080  1.000 42.80636 ? 404  TRP A CH2   1 
ATOM   3188 N N     . LYS A 1 411 ? -11.66204 -11.35158 36.02966  1.000 55.66434 ? 405  LYS A N     1 
ATOM   3189 C CA    . LYS A 1 411 ? -12.75724 -11.72828 35.13302  1.000 54.10382 ? 405  LYS A CA    1 
ATOM   3190 C C     . LYS A 1 411 ? -13.58685 -10.51585 34.74461  1.000 60.36880 ? 405  LYS A C     1 
ATOM   3191 O O     . LYS A 1 411 ? -14.09437 -10.43328 33.61670  1.000 60.60437 ? 405  LYS A O     1 
ATOM   3192 C CB    . LYS A 1 411 ? -13.68609 -12.75485 35.78298  1.000 59.14949 ? 405  LYS A CB    1 
ATOM   3193 C CG    . LYS A 1 411 ? -14.11557 -12.39934 37.20119  1.000 62.75071 ? 405  LYS A CG    1 
ATOM   3194 C CD    . LYS A 1 411 ? -14.27859 -13.62737 38.07164  1.000 67.54354 ? 405  LYS A CD    1 
ATOM   3195 C CE    . LYS A 1 411 ? -15.30541 -13.38237 39.16357  1.000 70.65645 ? 405  LYS A CE    1 
ATOM   3196 N NZ    . LYS A 1 411 ? -16.66484 -13.82029 38.73791  1.000 73.77498 ? 405  LYS A NZ    1 
ATOM   3197 N N     . ASP A 1 412 ? -13.74380 -9.57620  35.68002  1.000 52.55693 ? 406  ASP A N     1 
ATOM   3198 C CA    . ASP A 1 412 ? -14.61105 -8.41383  35.55574  1.000 57.53123 ? 406  ASP A CA    1 
ATOM   3199 C C     . ASP A 1 412 ? -13.83693 -7.13920  35.24006  1.000 59.52077 ? 406  ASP A C     1 
ATOM   3200 O O     . ASP A 1 412 ? -14.34135 -6.03572  35.47216  1.000 59.80717 ? 406  ASP A O     1 
ATOM   3201 C CB    . ASP A 1 412 ? -15.40503 -8.22176  36.84656  1.000 56.54908 ? 406  ASP A CB    1 
ATOM   3202 C CG    . ASP A 1 412 ? -16.32480 -9.38410  37.13998  1.000 64.80827 ? 406  ASP A CG    1 
ATOM   3203 O OD1   . ASP A 1 412 ? -16.76734 -10.04498 36.17597  1.000 62.33077 ? 406  ASP A OD1   1 
ATOM   3204 O OD2   . ASP A 1 412 ? -16.60183 -9.63155  38.33432  1.000 65.77115 ? 406  ASP A OD2   1 
ATOM   3205 N N     . GLY A 1 413 ? -12.62088 -7.26371  34.73037  1.000 58.91318 ? 407  GLY A N     1 
ATOM   3206 C CA    . GLY A 1 413 ? -11.81430 -6.10229  34.45561  1.000 57.74534 ? 407  GLY A CA    1 
ATOM   3207 C C     . GLY A 1 413 ? -10.66873 -5.96174  35.43165  1.000 52.81481 ? 407  GLY A C     1 
ATOM   3208 O O     . GLY A 1 413 ? -10.66389 -6.53540  36.52799  1.000 48.89578 ? 407  GLY A O     1 
ATOM   3209 N N     . PRO A 1 414 ? -9.67414  -5.17424  35.04563  1.000 49.39015 ? 408  PRO A N     1 
ATOM   3210 C CA    . PRO A 1 414 ? -8.46195  -5.05808  35.85669  1.000 49.26985 ? 408  PRO A CA    1 
ATOM   3211 C C     . PRO A 1 414 ? -8.65760  -4.15823  37.06417  1.000 46.37840 ? 408  PRO A C     1 
ATOM   3212 O O     . PRO A 1 414 ? -9.36615  -3.15061  37.01475  1.000 50.98670 ? 408  PRO A O     1 
ATOM   3213 C CB    . PRO A 1 414 ? -7.45617  -4.46204  34.86688  1.000 42.64244 ? 408  PRO A CB    1 
ATOM   3214 C CG    . PRO A 1 414 ? -8.30162  -3.56204  34.04213  1.000 50.03203 ? 408  PRO A CG    1 
ATOM   3215 C CD    . PRO A 1 414 ? -9.62467  -4.30318  33.86055  1.000 52.36851 ? 408  PRO A CD    1 
ATOM   3216 N N     . ASN A 1 415 ? -8.02854  -4.55000  38.16792  1.000 46.25520 ? 409  ASN A N     1 
ATOM   3217 C CA    . ASN A 1 415 ? -7.94174  -3.71662  39.35773  1.000 43.73638 ? 409  ASN A CA    1 
ATOM   3218 C C     . ASN A 1 415 ? -6.57103  -3.94052  39.96757  1.000 42.19093 ? 409  ASN A C     1 
ATOM   3219 O O     . ASN A 1 415 ? -6.05352  -5.06204  39.93989  1.000 48.45092 ? 409  ASN A O     1 
ATOM   3220 C CB    . ASN A 1 415 ? -9.05581  -4.03371  40.37046  1.000 46.97025 ? 409  ASN A CB    1 
ATOM   3221 C CG    . ASN A 1 415 ? -8.99673  -5.47204  40.88982  1.000 48.86280 ? 409  ASN A CG    1 
ATOM   3222 O OD1   . ASN A 1 415 ? -8.47162  -6.36780  40.22958  1.000 50.49592 ? 409  ASN A OD1   1 
ATOM   3223 N ND2   . ASN A 1 415 ? -9.56755  -5.69585  42.06967  1.000 53.81126 ? 409  ASN A ND2   1 
ATOM   3224 N N     . SER A 1 416 ? -5.97938  -2.87671  40.50610  1.000 40.36235 ? 410  SER A N     1 
ATOM   3225 C CA    . SER A 1 416 ? -4.62083  -2.94526  41.01591  1.000 36.99550 ? 410  SER A CA    1 
ATOM   3226 C C     . SER A 1 416 ? -4.40477  -1.83312  42.02554  1.000 36.36576 ? 410  SER A C     1 
ATOM   3227 O O     . SER A 1 416 ? -5.25542  -0.96479  42.22099  1.000 38.64509 ? 410  SER A O     1 
ATOM   3228 C CB    . SER A 1 416 ? -3.58990  -2.80337  39.89213  1.000 41.87412 ? 410  SER A CB    1 
ATOM   3229 O OG    . SER A 1 416 ? -3.56631  -1.46468  39.44320  1.000 35.23581 ? 410  SER A OG    1 
ATOM   3230 N N     . TYR A 1 417 ? -3.23929  -1.86544  42.65440  1.000 34.56999 ? 411  TYR A N     1 
ATOM   3231 C CA    . TYR A 1 417 ? -2.78799  -0.80506  43.54325  1.000 38.80387 ? 411  TYR A CA    1 
ATOM   3232 C C     . TYR A 1 417 ? -1.78758  0.07405   42.79040  1.000 30.51297 ? 411  TYR A C     1 
ATOM   3233 O O     . TYR A 1 417 ? -0.76062  -0.41702  42.31252  1.000 34.49537 ? 411  TYR A O     1 
ATOM   3234 C CB    . TYR A 1 417 ? -2.17837  -1.40949  44.81109  1.000 37.04414 ? 411  TYR A CB    1 
ATOM   3235 C CG    . TYR A 1 417 ? -1.85159  -0.42382  45.91948  1.000 33.94326 ? 411  TYR A CG    1 
ATOM   3236 C CD1   . TYR A 1 417 ? -2.68858  0.66456   46.19263  1.000 38.70237 ? 411  TYR A CD1   1 
ATOM   3237 C CD2   . TYR A 1 417 ? -0.72149  -0.59920  46.70314  1.000 38.85083 ? 411  TYR A CD2   1 
ATOM   3238 C CE1   . TYR A 1 417 ? -2.38411  1.56777   47.20103  1.000 42.49952 ? 411  TYR A CE1   1 
ATOM   3239 C CE2   . TYR A 1 417 ? -0.40640  0.28932   47.72250  1.000 43.02724 ? 411  TYR A CE2   1 
ATOM   3240 C CZ    . TYR A 1 417 ? -1.24441  1.36807   47.97590  1.000 44.82513 ? 411  TYR A CZ    1 
ATOM   3241 O OH    . TYR A 1 417 ? -0.91616  2.24504   48.99550  1.000 44.58307 ? 411  TYR A OH    1 
ATOM   3242 N N     . LEU A 1 418 ? -2.10611  1.36072   42.66499  1.000 35.58237 ? 412  LEU A N     1 
ATOM   3243 C CA    . LEU A 1 418 ? -1.28667  2.37975   42.00764  1.000 32.74258 ? 412  LEU A CA    1 
ATOM   3244 C C     . LEU A 1 418 ? -1.02523  2.08647   40.52895  1.000 33.02240 ? 412  LEU A C     1 
ATOM   3245 O O     . LEU A 1 418 ? -0.15713  2.71894   39.92760  1.000 31.88830 ? 412  LEU A O     1 
ATOM   3246 C CB    . LEU A 1 418 ? 0.04561   2.57714   42.72739  1.000 34.22072 ? 412  LEU A CB    1 
ATOM   3247 C CG    . LEU A 1 418 ? -0.05718  2.79483   44.24517  1.000 32.19547 ? 412  LEU A CG    1 
ATOM   3248 C CD1   . LEU A 1 418 ? 1.31416   3.04627   44.79947  1.000 31.62168 ? 412  LEU A CD1   1 
ATOM   3249 C CD2   . LEU A 1 418 ? -1.02468  3.95030   44.56904  1.000 34.31781 ? 412  LEU A CD2   1 
ATOM   3250 N N     . GLY A 1 419 ? -1.72625  1.12087   39.93820  1.000 31.47794 ? 413  GLY A N     1 
ATOM   3251 C CA    . GLY A 1 419 ? -1.41233  0.67354   38.59555  1.000 31.57811 ? 413  GLY A CA    1 
ATOM   3252 C C     . GLY A 1 419 ? -0.20518  -0.22850  38.49047  1.000 30.58260 ? 413  GLY A C     1 
ATOM   3253 O O     . GLY A 1 419 ? 0.22505   -0.53741  37.37322  1.000 32.86512 ? 413  GLY A O     1 
ATOM   3254 N N     . MET A 1 420 ? 0.36094   -0.67329  39.61063  1.000 28.20554 ? 414  MET A N     1 
ATOM   3255 C CA    . MET A 1 420 ? 1.60951   -1.42352  39.57078  1.000 26.98502 ? 414  MET A CA    1 
ATOM   3256 C C     . MET A 1 420 ? 1.56080   -2.78000  40.26959  1.000 30.86450 ? 414  MET A C     1 
ATOM   3257 O O     . MET A 1 420 ? 2.41763   -3.62013  39.98509  1.000 29.73582 ? 414  MET A O     1 
ATOM   3258 C CB    . MET A 1 420 ? 2.73846   -0.58938  40.20198  1.000 27.56930 ? 414  MET A CB    1 
ATOM   3259 C CG    . MET A 1 420 ? 3.10079   0.64906   39.37174  1.000 31.46088 ? 414  MET A CG    1 
ATOM   3260 S SD    . MET A 1 420 ? 4.52288   1.55480   40.02876  1.000 30.27761 ? 414  MET A SD    1 
ATOM   3261 C CE    . MET A 1 420 ? 3.64887   2.54599   41.25193  1.000 30.82799 ? 414  MET A CE    1 
ATOM   3262 N N     . MET A 1 421 ? 0.60975   -3.02333  41.16676  1.000 32.18063 ? 415  MET A N     1 
ATOM   3263 C CA    . MET A 1 421 ? 0.62504   -4.22516  41.99577  1.000 31.53045 ? 415  MET A CA    1 
ATOM   3264 C C     . MET A 1 421 ? -0.76753  -4.83210  42.02886  1.000 33.14738 ? 415  MET A C     1 
ATOM   3265 O O     . MET A 1 421 ? -1.76502  -4.11230  42.08901  1.000 38.05131 ? 415  MET A O     1 
ATOM   3266 C CB    . MET A 1 421 ? 1.09400   -3.92983  43.43232  1.000 33.28741 ? 415  MET A CB    1 
ATOM   3267 C CG    . MET A 1 421 ? 2.54737   -3.52495  43.56212  1.000 37.69996 ? 415  MET A CG    1 
ATOM   3268 S SD    . MET A 1 421 ? 2.91182   -2.68229  45.13570  1.000 41.82075 ? 415  MET A SD    1 
ATOM   3269 C CE    . MET A 1 421 ? 3.19508   -4.10974  46.20591  1.000 46.21538 ? 415  MET A CE    1 
ATOM   3270 N N     . VAL A 1 422 ? -0.83395  -6.15819  41.97365  1.000 35.40047 ? 416  VAL A N     1 
ATOM   3271 C CA    . VAL A 1 422 ? -2.09775  -6.88256  41.88575  1.000 37.99812 ? 416  VAL A CA    1 
ATOM   3272 C C     . VAL A 1 422 ? -2.22050  -7.77818  43.10435  1.000 40.99478 ? 416  VAL A C     1 
ATOM   3273 O O     . VAL A 1 422 ? -1.33751  -8.60517  43.35363  1.000 36.96361 ? 416  VAL A O     1 
ATOM   3274 C CB    . VAL A 1 422 ? -2.19081  -7.72235  40.60081  1.000 40.24375 ? 416  VAL A CB    1 
ATOM   3275 C CG1   . VAL A 1 422 ? -3.61288  -8.27107  40.43029  1.000 39.60927 ? 416  VAL A CG1   1 
ATOM   3276 C CG2   . VAL A 1 422 ? -1.78629  -6.88058  39.40432  1.000 37.88383 ? 416  VAL A CG2   1 
ATOM   3277 N N     . SER A 1 423 ? -3.30962  -7.61013  43.85547  1.000 44.37432 ? 417  SER A N     1 
ATOM   3278 C CA    . SER A 1 423 ? -3.57141  -8.48649  44.99420  1.000 50.00287 ? 417  SER A CA    1 
ATOM   3279 C C     . SER A 1 423 ? -3.57218  -9.94191  44.53994  1.000 44.19400 ? 417  SER A C     1 
ATOM   3280 O O     . SER A 1 423 ? -4.07373  -10.26475 43.46019  1.000 46.91345 ? 417  SER A O     1 
ATOM   3281 C CB    . SER A 1 423 ? -4.91412  -8.13009  45.64266  1.000 46.44941 ? 417  SER A CB    1 
ATOM   3282 O OG    . SER A 1 423 ? -4.95421  -8.56871  46.99662  1.000 58.48964 ? 417  SER A OG    1 
ATOM   3283 N N     . ASN A 1 424 ? -2.98893  -10.81472 45.36389  1.000 47.35785 ? 418  ASN A N     1 
ATOM   3284 C CA    . ASN A 1 424 ? -2.78256  -12.25603 45.14857  1.000 46.18130 ? 418  ASN A CA    1 
ATOM   3285 C C     . ASN A 1 424 ? -1.58129  -12.54223 44.24794  1.000 47.50376 ? 418  ASN A C     1 
ATOM   3286 O O     . ASN A 1 424 ? -1.31120  -13.72046 43.97317  1.000 40.94041 ? 418  ASN A O     1 
ATOM   3287 C CB    . ASN A 1 424 ? -4.00740  -12.98077 44.55562  1.000 51.80528 ? 418  ASN A CB    1 
ATOM   3288 C CG    . ASN A 1 424 ? -5.21320  -12.97968 45.49281  1.000 55.57961 ? 418  ASN A CG    1 
ATOM   3289 O OD1   . ASN A 1 424 ? -5.08394  -13.17722 46.70422  1.000 55.27476 ? 418  ASN A OD1   1 
ATOM   3290 N ND2   . ASN A 1 424 ? -6.39616  -12.76225 44.92529  1.000 59.27957 ? 418  ASN A ND2   1 
ATOM   3291 N N     . PHE A 1 425 ? -0.84522  -11.52732 43.78252  1.000 40.40456 ? 419  PHE A N     1 
ATOM   3292 C CA    . PHE A 1 425 ? 0.25522   -11.72257 42.83403  1.000 40.70629 ? 419  PHE A CA    1 
ATOM   3293 C C     . PHE A 1 425 ? 1.49746   -11.05999 43.41324  1.000 42.92296 ? 419  PHE A C     1 
ATOM   3294 O O     . PHE A 1 425 ? 1.87926   -9.95102  43.01456  1.000 41.20234 ? 419  PHE A O     1 
ATOM   3295 C CB    . PHE A 1 425 ? -0.13127  -11.20032 41.44490  1.000 41.66740 ? 419  PHE A CB    1 
ATOM   3296 C CG    . PHE A 1 425 ? -1.24624  -11.99784 40.80002  1.000 40.68292 ? 419  PHE A CG    1 
ATOM   3297 C CD1   . PHE A 1 425 ? -0.96498  -13.11744 40.02047  1.000 39.19206 ? 419  PHE A CD1   1 
ATOM   3298 C CD2   . PHE A 1 425 ? -2.57151  -11.69641 41.06611  1.000 37.81707 ? 419  PHE A CD2   1 
ATOM   3299 C CE1   . PHE A 1 425 ? -1.99167  -13.87173 39.47345  1.000 40.85627 ? 419  PHE A CE1   1 
ATOM   3300 C CE2   . PHE A 1 425 ? -3.60315  -12.45492 40.52305  1.000 41.73980 ? 419  PHE A CE2   1 
ATOM   3301 C CZ    . PHE A 1 425 ? -3.31430  -13.53740 39.72364  1.000 38.33609 ? 419  PHE A CZ    1 
ATOM   3302 N N     . PRO A 1 426 ? 2.15707   -11.71750 44.36440  1.000 39.49252 ? 420  PRO A N     1 
ATOM   3303 C CA    . PRO A 1 426 ? 3.27477   -11.09201 45.06818  1.000 32.72134 ? 420  PRO A CA    1 
ATOM   3304 C C     . PRO A 1 426 ? 4.54261   -11.07267 44.23687  1.000 32.27838 ? 420  PRO A C     1 
ATOM   3305 O O     . PRO A 1 426 ? 4.80558   -11.97009 43.43908  1.000 37.09878 ? 420  PRO A O     1 
ATOM   3306 C CB    . PRO A 1 426 ? 3.46552   -11.99752 46.29664  1.000 40.88185 ? 420  PRO A CB    1 
ATOM   3307 C CG    . PRO A 1 426 ? 2.23637   -12.89296 46.32144  1.000 44.07443 ? 420  PRO A CG    1 
ATOM   3308 C CD    . PRO A 1 426 ? 1.90739   -13.07276 44.87853  1.000 43.83300 ? 420  PRO A CD    1 
ATOM   3309 N N     . ASN A 1 427 ? 5.35697   -10.05235 44.48048  1.000 30.50558 ? 421  ASN A N     1 
ATOM   3310 C CA    . ASN A 1 427 ? 6.64183   -9.89589  43.81691  1.000 33.05631 ? 421  ASN A CA    1 
ATOM   3311 C C     . ASN A 1 427 ? 6.46982   -9.69986  42.31626  1.000 27.35525 ? 421  ASN A C     1 
ATOM   3312 O O     . ASN A 1 427 ? 7.39790   -9.95595  41.55832  1.000 29.87038 ? 421  ASN A O     1 
ATOM   3313 C CB    . ASN A 1 427 ? 7.55578   -11.10016 44.07457  1.000 27.86910 ? 421  ASN A CB    1 
ATOM   3314 C CG    . ASN A 1 427 ? 7.98815   -11.20375 45.51593  1.000 35.03894 ? 421  ASN A CG    1 
ATOM   3315 O OD1   . ASN A 1 427 ? 7.49325   -10.47301 46.36435  1.000 37.81441 ? 421  ASN A OD1   1 
ATOM   3316 N ND2   . ASN A 1 427 ? 8.90452   -12.11268 45.80170  1.000 36.70468 ? 421  ASN A ND2   1 
ATOM   3317 N N     . MET A 1 428 ? 5.27044   -9.33474  41.88256  1.000 29.98589 ? 422  MET A N     1 
ATOM   3318 C CA    . MET A 1 428 ? 5.01073   -8.96088  40.49645  1.000 30.40477 ? 422  MET A CA    1 
ATOM   3319 C C     . MET A 1 428 ? 4.72384   -7.47166  40.43232  1.000 31.05353 ? 422  MET A C     1 
ATOM   3320 O O     . MET A 1 428 ? 3.90490   -6.95530  41.20226  1.000 34.24987 ? 422  MET A O     1 
ATOM   3321 C CB    . MET A 1 428 ? 3.83565   -9.74142  39.90737  1.000 30.15705 ? 422  MET A CB    1 
ATOM   3322 C CG    . MET A 1 428 ? 3.53243   -9.33974  38.45391  1.000 32.00610 ? 422  MET A CG    1 
ATOM   3323 S SD    . MET A 1 428 ? 2.16361   -10.28425 37.72599  1.000 35.40728 ? 422  MET A SD    1 
ATOM   3324 C CE    . MET A 1 428 ? 0.78577   -9.20002  38.06037  1.000 33.32023 ? 422  MET A CE    1 
ATOM   3325 N N     . PHE A 1 429 ? 5.39116   -6.78850  39.50610  1.000 30.39347 ? 423  PHE A N     1 
ATOM   3326 C CA    . PHE A 1 429 ? 5.24587   -5.35060  39.33111  1.000 27.00369 ? 423  PHE A CA    1 
ATOM   3327 C C     . PHE A 1 429 ? 4.98190   -5.06079  37.86602  1.000 27.12450 ? 423  PHE A C     1 
ATOM   3328 O O     . PHE A 1 429 ? 5.71405   -5.53742  36.99879  1.000 25.71488 ? 423  PHE A O     1 
ATOM   3329 C CB    . PHE A 1 429 ? 6.49771   -4.62107  39.78957  1.000 25.08096 ? 423  PHE A CB    1 
ATOM   3330 C CG    . PHE A 1 429 ? 6.78823   -4.81646  41.25093  1.000 28.05648 ? 423  PHE A CG    1 
ATOM   3331 C CD1   . PHE A 1 429 ? 6.06877   -4.12294  42.20681  1.000 34.37668 ? 423  PHE A CD1   1 
ATOM   3332 C CD2   . PHE A 1 429 ? 7.71318   -5.72857  41.65312  1.000 29.55336 ? 423  PHE A CD2   1 
ATOM   3333 C CE1   . PHE A 1 429 ? 6.32902   -4.30755  43.55630  1.000 35.54490 ? 423  PHE A CE1   1 
ATOM   3334 C CE2   . PHE A 1 429 ? 7.96489   -5.92519  42.99325  1.000 36.60866 ? 423  PHE A CE2   1 
ATOM   3335 C CZ    . PHE A 1 429 ? 7.26832   -5.20837  43.94263  1.000 34.73188 ? 423  PHE A CZ    1 
ATOM   3336 N N     . MET A 1 430 ? 3.95154   -4.27665  37.61248  1.000 28.14377 ? 424  MET A N     1 
ATOM   3337 C CA    . MET A 1 430 ? 3.52507   -3.95070  36.26436  1.000 28.70560 ? 424  MET A CA    1 
ATOM   3338 C C     . MET A 1 430 ? 4.12566   -2.60725  35.87490  1.000 29.50786 ? 424  MET A C     1 
ATOM   3339 O O     . MET A 1 430 ? 4.14268   -1.67113  36.68708  1.000 25.97863 ? 424  MET A O     1 
ATOM   3340 C CB    . MET A 1 430 ? 2.00862   -3.84615  36.20418  1.000 27.58712 ? 424  MET A CB    1 
ATOM   3341 C CG    . MET A 1 430 ? 1.27990   -5.19586  36.33554  1.000 30.01911 ? 424  MET A CG    1 
ATOM   3342 S SD    . MET A 1 430 ? -0.51813  -5.04965  36.35650  1.000 33.54268 ? 424  MET A SD    1 
ATOM   3343 C CE    . MET A 1 430 ? -0.85402  -3.74254  37.53347  1.000 39.09857 ? 424  MET A CE    1 
ATOM   3344 N N     . VAL A 1 431 ? 4.59701   -2.51029  34.63373  1.000 26.55476 ? 425  VAL A N     1 
ATOM   3345 C CA    . VAL A 1 431 ? 5.02011   -1.24624  34.04003  1.000 24.72897 ? 425  VAL A CA    1 
ATOM   3346 C C     . VAL A 1 431 ? 4.01852   -0.90010  32.94421  1.000 25.12409 ? 425  VAL A C     1 
ATOM   3347 O O     . VAL A 1 431 ? 3.67551   -1.76041  32.12244  1.000 26.39580 ? 425  VAL A O     1 
ATOM   3348 C CB    . VAL A 1 431 ? 6.46014   -1.33184  33.50148  1.000 21.66421 ? 425  VAL A CB    1 
ATOM   3349 C CG1   . VAL A 1 431 ? 6.82144   -0.03908  32.70279  1.000 25.98075 ? 425  VAL A CG1   1 
ATOM   3350 C CG2   . VAL A 1 431 ? 7.43554   -1.60385  34.63993  1.000 23.97323 ? 425  VAL A CG2   1 
ATOM   3351 N N     . PHE A 1 432 ? 3.51688   0.34282   32.96726  1.000 26.56131 ? 426  PHE A N     1 
ATOM   3352 C CA    . PHE A 1 432 ? 2.44369   0.79812   32.08843  1.000 30.49368 ? 426  PHE A CA    1 
ATOM   3353 C C     . PHE A 1 432 ? 1.23567   -0.13789  32.17672  1.000 33.08275 ? 426  PHE A C     1 
ATOM   3354 O O     . PHE A 1 432 ? 0.56649   -0.42433  31.18037  1.000 32.08559 ? 426  PHE A O     1 
ATOM   3355 C CB    . PHE A 1 432 ? 2.94165   0.93823   30.63790  1.000 29.05007 ? 426  PHE A CB    1 
ATOM   3356 C CG    . PHE A 1 432 ? 2.22826   2.00996   29.82916  1.000 32.96485 ? 426  PHE A CG    1 
ATOM   3357 C CD1   . PHE A 1 432 ? 1.92760   3.24988   30.38077  1.000 34.94112 ? 426  PHE A CD1   1 
ATOM   3358 C CD2   . PHE A 1 432 ? 1.87284   1.77010   28.50795  1.000 31.44620 ? 426  PHE A CD2   1 
ATOM   3359 C CE1   . PHE A 1 432 ? 1.27098   4.22588   29.64255  1.000 35.88981 ? 426  PHE A CE1   1 
ATOM   3360 C CE2   . PHE A 1 432 ? 1.20190   2.74157   27.75920  1.000 37.30501 ? 426  PHE A CE2   1 
ATOM   3361 C CZ    . PHE A 1 432 ? 0.89691   3.96451   28.32717  1.000 34.66206 ? 426  PHE A CZ    1 
ATOM   3362 N N     . GLY A 1 433 ? 0.95028   -0.62133  33.38736  1.000 32.86701 ? 427  GLY A N     1 
ATOM   3363 C CA    . GLY A 1 433 ? -0.16367  -1.52408  33.58501  1.000 34.25989 ? 427  GLY A CA    1 
ATOM   3364 C C     . GLY A 1 433 ? -1.49155  -0.79280  33.64569  1.000 36.52862 ? 427  GLY A C     1 
ATOM   3365 O O     . GLY A 1 433 ? -1.57037  0.44168   33.61013  1.000 37.96965 ? 427  GLY A O     1 
ATOM   3366 N N     . PRO A 1 434 ? -2.57069  -1.56574  33.74805  1.000 42.02612 ? 428  PRO A N     1 
ATOM   3367 C CA    . PRO A 1 434 ? -3.90762  -0.96386  33.88089  1.000 41.26521 ? 428  PRO A CA    1 
ATOM   3368 C C     . PRO A 1 434 ? -4.01407  -0.10933  35.14062  1.000 39.91861 ? 428  PRO A C     1 
ATOM   3369 O O     . PRO A 1 434 ? -3.19222  -0.18351  36.05562  1.000 38.61758 ? 428  PRO A O     1 
ATOM   3370 C CB    . PRO A 1 434 ? -4.84237  -2.18117  33.94312  1.000 40.79492 ? 428  PRO A CB    1 
ATOM   3371 C CG    . PRO A 1 434 ? -3.94694  -3.29179  34.47552  1.000 40.30391 ? 428  PRO A CG    1 
ATOM   3372 C CD    . PRO A 1 434 ? -2.61802  -3.03944  33.80061  1.000 42.06981 ? 428  PRO A CD    1 
ATOM   3373 N N     . ASN A 1 435 ? -5.06197  0.71938   35.17569  1.000 35.84988 ? 429  ASN A N     1 
ATOM   3374 C CA    . ASN A 1 435 ? -5.33988  1.60341   36.31741  1.000 42.02691 ? 429  ASN A CA    1 
ATOM   3375 C C     . ASN A 1 435 ? -4.17175  2.54950   36.58534  1.000 42.82939 ? 429  ASN A C     1 
ATOM   3376 O O     . ASN A 1 435 ? -3.84686  2.85559   37.73565  1.000 40.83295 ? 429  ASN A O     1 
ATOM   3377 C CB    . ASN A 1 435 ? -5.68602  0.81586   37.59504  1.000 43.53514 ? 429  ASN A CB    1 
ATOM   3378 C CG    . ASN A 1 435 ? -6.43816  -0.48261  37.31907  1.000 45.83006 ? 429  ASN A CG    1 
ATOM   3379 O OD1   . ASN A 1 435 ? -5.94463  -1.56774  37.63662  1.000 46.86401 ? 429  ASN A OD1   1 
ATOM   3380 N ND2   . ASN A 1 435 ? -7.62782  -0.38072  36.72619  1.000 40.91978 ? 429  ASN A ND2   1 
ATOM   3381 N N     . GLY A 1 436 ? -3.51095  2.99393   35.51731  1.000 37.56088 ? 430  GLY A N     1 
ATOM   3382 C CA    . GLY A 1 436 ? -2.43373  3.95595   35.62187  1.000 27.70822 ? 430  GLY A CA    1 
ATOM   3383 C C     . GLY A 1 436 ? -2.88937  5.30482   35.08431  1.000 33.06409 ? 430  GLY A C     1 
ATOM   3384 O O     . GLY A 1 436 ? -4.05423  5.48410   34.72746  1.000 36.51015 ? 430  GLY A O     1 
ATOM   3385 N N     . PRO A 1 437 ? -2.00250  6.29158   35.03855  1.000 32.23123 ? 431  PRO A N     1 
ATOM   3386 C CA    . PRO A 1 437 ? -2.42781  7.62953   34.62143  1.000 29.44800 ? 431  PRO A CA    1 
ATOM   3387 C C     . PRO A 1 437 ? -2.63676  7.76728   33.12064  1.000 34.71932 ? 431  PRO A C     1 
ATOM   3388 O O     . PRO A 1 437 ? -2.20804  6.94870   32.31278  1.000 31.56413 ? 431  PRO A O     1 
ATOM   3389 C CB    . PRO A 1 437 ? -1.30253  8.53733   35.12318  1.000 30.27988 ? 431  PRO A CB    1 
ATOM   3390 C CG    . PRO A 1 437 ? -0.09943  7.63064   35.19957  1.000 32.19169 ? 431  PRO A CG    1 
ATOM   3391 C CD    . PRO A 1 437 ? -0.58088  6.22927   35.40460  1.000 31.00979 ? 431  PRO A CD    1 
ATOM   3392 N N     . LEU A 1 438 ? -3.39858  8.80306   32.77145  1.000 33.91296 ? 432  LEU A N     1 
ATOM   3393 C CA    . LEU A 1 438 ? -3.55658  9.24983   31.38918  1.000 36.36055 ? 432  LEU A CA    1 
ATOM   3394 C C     . LEU A 1 438 ? -2.57160  10.39595  31.19667  1.000 34.76660 ? 432  LEU A C     1 
ATOM   3395 O O     . LEU A 1 438 ? -2.82569  11.52336  31.61648  1.000 37.62428 ? 432  LEU A O     1 
ATOM   3396 C CB    . LEU A 1 438 ? -4.99273  9.68011   31.10776  1.000 37.55832 ? 432  LEU A CB    1 
ATOM   3397 C CG    . LEU A 1 438 ? -5.21930  10.24697  29.70709  1.000 42.80797 ? 432  LEU A CG    1 
ATOM   3398 C CD1   . LEU A 1 438 ? -5.46753  9.12028   28.75069  1.000 47.57569 ? 432  LEU A CD1   1 
ATOM   3399 C CD2   . LEU A 1 438 ? -6.37264  11.21352  29.70191  1.000 50.30952 ? 432  LEU A CD2   1 
ATOM   3400 N N     . ALA A 1 439 ? -1.42203  10.08691  30.61410  1.000 30.72277 ? 433  ALA A N     1 
ATOM   3401 C CA    . ALA A 1 439 ? -0.36836  11.06281  30.37943  1.000 27.35011 ? 433  ALA A CA    1 
ATOM   3402 C C     . ALA A 1 439 ? 0.46234   10.52546  29.22680  1.000 29.80990 ? 433  ALA A C     1 
ATOM   3403 O O     . ALA A 1 439 ? 0.19623   9.43267   28.71075  1.000 29.75441 ? 433  ALA A O     1 
ATOM   3404 C CB    . ALA A 1 439 ? 0.47526   11.29231  31.63969  1.000 26.49687 ? 433  ALA A CB    1 
ATOM   3405 N N     . ASN A 1 440 ? 1.47060   11.30018  28.82520  1.000 24.45149 ? 434  ASN A N     1 
ATOM   3406 C CA    . ASN A 1 440 ? 2.45137   10.81659  27.85770  1.000 28.93555 ? 434  ASN A CA    1 
ATOM   3407 C C     . ASN A 1 440 ? 3.18333   9.59834   28.41552  1.000 27.43160 ? 434  ASN A C     1 
ATOM   3408 O O     . ASN A 1 440 ? 3.61435   9.60634   29.57100  1.000 26.70801 ? 434  ASN A O     1 
ATOM   3409 C CB    . ASN A 1 440 ? 3.47067   11.91104  27.54469  1.000 24.72029 ? 434  ASN A CB    1 
ATOM   3410 C CG    . ASN A 1 440 ? 4.14572   11.66971  26.21697  1.000 29.84599 ? 434  ASN A CG    1 
ATOM   3411 O OD1   . ASN A 1 440 ? 3.60004   10.97096  25.37948  1.000 34.33704 ? 434  ASN A OD1   1 
ATOM   3412 N ND2   . ASN A 1 440 ? 5.33079   12.20153  26.03860  1.000 34.27876 ? 434  ASN A ND2   1 
ATOM   3413 N N     . SER A 1 441 ? 3.35907   8.54166   27.59431  1.000 24.37385 ? 435  SER A N     1 
ATOM   3414 C CA    . SER A 1 441 ? 3.73986   7.26341   28.19846  1.000 30.14253 ? 435  SER A CA    1 
ATOM   3415 C C     . SER A 1 441 ? 5.16867   7.23350   28.71740  1.000 26.30087 ? 435  SER A C     1 
ATOM   3416 O O     . SER A 1 441 ? 5.38928   6.63834   29.78315  1.000 23.23709 ? 435  SER A O     1 
ATOM   3417 C CB    . SER A 1 441 ? 3.52156   6.08098   27.24169  1.000 32.35013 ? 435  SER A CB    1 
ATOM   3418 O OG    . SER A 1 441 ? 4.05835   6.27373   25.95180  1.000 35.90131 ? 435  SER A OG    1 
ATOM   3419 N N     . PRO A 1 442 ? 6.18337   7.76608   28.03045  1.000 24.96142 ? 436  PRO A N     1 
ATOM   3420 C CA    . PRO A 1 442 ? 7.53844   7.56944   28.54116  1.000 26.64376 ? 436  PRO A CA    1 
ATOM   3421 C C     . PRO A 1 442 ? 7.72478   8.17551   29.92821  1.000 25.66307 ? 436  PRO A C     1 
ATOM   3422 O O     . PRO A 1 442 ? 8.32236   7.50651   30.79152  1.000 23.91601 ? 436  PRO A O     1 
ATOM   3423 C CB    . PRO A 1 442 ? 8.44008   8.20150   27.46244  1.000 26.08609 ? 436  PRO A CB    1 
ATOM   3424 C CG    . PRO A 1 442 ? 7.59526   8.08834   26.19675  1.000 28.67004 ? 436  PRO A CG    1 
ATOM   3425 C CD    . PRO A 1 442 ? 6.19718   8.37710   26.67411  1.000 27.02610 ? 436  PRO A CD    1 
ATOM   3426 N N     . PRO A 1 443 ? 7.16653   9.36455   30.23461  1.000 24.96066 ? 437  PRO A N     1 
ATOM   3427 C CA    . PRO A 1 443 ? 7.23788   9.84232   31.63561  1.000 27.27088 ? 437  PRO A CA    1 
ATOM   3428 C C     . PRO A 1 443 ? 6.51302   8.92015   32.61571  1.000 26.73743 ? 437  PRO A C     1 
ATOM   3429 O O     . PRO A 1 443 ? 6.92638   8.78576   33.77705  1.000 26.75345 ? 437  PRO A O     1 
ATOM   3430 C CB    . PRO A 1 443 ? 6.54081   11.21522  31.56197  1.000 27.14288 ? 437  PRO A CB    1 
ATOM   3431 C CG    . PRO A 1 443 ? 6.80488   11.66210  30.15926  1.000 30.84046 ? 437  PRO A CG    1 
ATOM   3432 C CD    . PRO A 1 443 ? 6.61485   10.42737  29.36025  1.000 25.01021 ? 437  PRO A CD    1 
ATOM   3433 N N     . ILE A 1 444 ? 5.44211   8.25649   32.17838  1.000 24.19418 ? 438  ILE A N     1 
ATOM   3434 C CA    . ILE A 1 444 ? 4.75431   7.33110   33.07967  1.000 22.60358 ? 438  ILE A CA    1 
ATOM   3435 C C     . ILE A 1 444 ? 5.63266   6.13307   33.37244  1.000 26.70582 ? 438  ILE A C     1 
ATOM   3436 O O     . ILE A 1 444 ? 5.79928   5.74463   34.53848  1.000 22.67524 ? 438  ILE A O     1 
ATOM   3437 C CB    . ILE A 1 444 ? 3.40070   6.89406   32.50466  1.000 24.32292 ? 438  ILE A CB    1 
ATOM   3438 C CG1   . ILE A 1 444 ? 2.47098   8.08674   32.34698  1.000 27.94742 ? 438  ILE A CG1   1 
ATOM   3439 C CG2   . ILE A 1 444 ? 2.77472   5.83093   33.37159  1.000 27.29694 ? 438  ILE A CG2   1 
ATOM   3440 C CD1   . ILE A 1 444 ? 1.13949   7.75515   31.66931  1.000 25.68918 ? 438  ILE A CD1   1 
ATOM   3441 N N     . ILE A 1 445 ? 6.19479   5.53308   32.31105  1.000 23.32226 ? 439  ILE A N     1 
ATOM   3442 C CA    . ILE A 1 445 ? 7.04344   4.35148   32.44660  1.000 24.66082 ? 439  ILE A CA    1 
ATOM   3443 C C     . ILE A 1 445 ? 8.25136   4.65773   33.32933  1.000 29.68064 ? 439  ILE A C     1 
ATOM   3444 O O     . ILE A 1 445 ? 8.63512   3.85146   34.18860  1.000 27.87219 ? 439  ILE A O     1 
ATOM   3445 C CB    . ILE A 1 445 ? 7.46338   3.85762   31.04670  1.000 26.56413 ? 439  ILE A CB    1 
ATOM   3446 C CG1   . ILE A 1 445 ? 6.31689   3.08766   30.37624  1.000 30.18524 ? 439  ILE A CG1   1 
ATOM   3447 C CG2   . ILE A 1 445 ? 8.76996   3.06299   31.09743  1.000 28.82657 ? 439  ILE A CG2   1 
ATOM   3448 C CD1   . ILE A 1 445 ? 6.29274   3.27594   28.83899  1.000 32.50643 ? 439  ILE A CD1   1 
ATOM   3449 N N     . GLU A 1 446 ? 8.87917   5.82789   33.13079  1.000 27.92406 ? 440  GLU A N     1 
ATOM   3450 C CA    . GLU A 1 446 ? 10.03628  6.16826   33.94875  1.000 26.13951 ? 440  GLU A CA    1 
ATOM   3451 C C     . GLU A 1 446 ? 9.63322   6.32030   35.40656  1.000 27.79787 ? 440  GLU A C     1 
ATOM   3452 O O     . GLU A 1 446 ? 10.37175  5.91405   36.30643  1.000 27.80573 ? 440  GLU A O     1 
ATOM   3453 C CB    . GLU A 1 446 ? 10.68264  7.46032   33.44364  1.000 30.61377 ? 440  GLU A CB    1 
ATOM   3454 C CG    . GLU A 1 446 ? 11.37913  7.33032   32.10863  1.000 23.81186 ? 440  GLU A CG    1 
ATOM   3455 C CD    . GLU A 1 446 ? 12.14847  8.58156   31.76941  1.000 28.18869 ? 440  GLU A CD    1 
ATOM   3456 O OE1   . GLU A 1 446 ? 12.21569  9.49260   32.61614  1.000 36.62334 ? 440  GLU A OE1   1 
ATOM   3457 O OE2   . GLU A 1 446 ? 12.69632  8.67257   30.67164  1.000 28.90670 ? 440  GLU A OE2   1 
ATOM   3458 N N     . THR A 1 447 ? 8.45752   6.90560   35.65310  1.000 25.08951 ? 441  THR A N     1 
ATOM   3459 C CA    . THR A 1 447 ? 7.97903   7.08960   37.01854  1.000 28.48794 ? 441  THR A CA    1 
ATOM   3460 C C     . THR A 1 447 ? 7.76461   5.74106   37.69963  1.000 31.81123 ? 441  THR A C     1 
ATOM   3461 O O     . THR A 1 447 ? 8.19079   5.52685   38.84242  1.000 28.33178 ? 441  THR A O     1 
ATOM   3462 C CB    . THR A 1 447 ? 6.68201   7.91008   36.97083  1.000 33.55451 ? 441  THR A CB    1 
ATOM   3463 O OG1   . THR A 1 447 ? 6.98335   9.23183   36.49825  1.000 29.34178 ? 441  THR A OG1   1 
ATOM   3464 C CG2   . THR A 1 447 ? 6.00764   8.00600   38.34045  1.000 30.71692 ? 441  THR A CG2   1 
ATOM   3465 N N     . GLN A 1 448 ? 7.13153   4.80614   36.98715  1.000 26.74808 ? 442  GLN A N     1 
ATOM   3466 C CA    . GLN A 1 448 ? 6.81746   3.50737   37.56043  1.000 26.27922 ? 442  GLN A CA    1 
ATOM   3467 C C     . GLN A 1 448 ? 8.06405   2.64866   37.73276  1.000 28.06690 ? 442  GLN A C     1 
ATOM   3468 O O     . GLN A 1 448 ? 8.20112   1.96458   38.75146  1.000 28.25964 ? 442  GLN A O     1 
ATOM   3469 C CB    . GLN A 1 448 ? 5.77942   2.81132   36.67584  1.000 25.27368 ? 442  GLN A CB    1 
ATOM   3470 C CG    . GLN A 1 448 ? 4.43637   3.57202   36.63658  1.000 24.56998 ? 442  GLN A CG    1 
ATOM   3471 C CD    . GLN A 1 448 ? 3.47923   2.99719   35.62495  1.000 27.02597 ? 442  GLN A CD    1 
ATOM   3472 O OE1   . GLN A 1 448 ? 3.90697   2.36932   34.67565  1.000 29.87720 ? 442  GLN A OE1   1 
ATOM   3473 N NE2   . GLN A 1 448 ? 2.18899   3.25843   35.79018  1.000 26.98680 ? 442  GLN A NE2   1 
ATOM   3474 N N     . VAL A 1 449 ? 8.96622   2.65507   36.74186  1.000 25.14578 ? 443  VAL A N     1 
ATOM   3475 C CA    . VAL A 1 449 ? 10.19344  1.86379   36.83268  1.000 26.31565 ? 443  VAL A CA    1 
ATOM   3476 C C     . VAL A 1 449 ? 11.03401  2.34682   38.00885  1.000 31.75196 ? 443  VAL A C     1 
ATOM   3477 O O     . VAL A 1 449 ? 11.61136  1.54802   38.76447  1.000 24.88289 ? 443  VAL A O     1 
ATOM   3478 C CB    . VAL A 1 449 ? 10.97650  1.92606   35.50669  1.000 23.68228 ? 443  VAL A CB    1 
ATOM   3479 C CG1   . VAL A 1 449 ? 12.37388  1.37308   35.69189  1.000 26.58601 ? 443  VAL A CG1   1 
ATOM   3480 C CG2   . VAL A 1 449 ? 10.27418  1.09514   34.40010  1.000 23.39591 ? 443  VAL A CG2   1 
ATOM   3481 N N     . ARG A 1 450 ? 11.10827  3.66614   38.19269  1.000 29.90563 ? 444  ARG A N     1 
ATOM   3482 C CA    . ARG A 1 450 ? 11.90092  4.16422   39.30723  1.000 28.88011 ? 444  ARG A CA    1 
ATOM   3483 C C     . ARG A 1 450 ? 11.25477  3.82902   40.63828  1.000 29.08047 ? 444  ARG A C     1 
ATOM   3484 O O     . ARG A 1 450 ? 11.95747  3.46618   41.58681  1.000 33.67967 ? 444  ARG A O     1 
ATOM   3485 C CB    . ARG A 1 450 ? 12.16508  5.66074   39.16591  1.000 34.08166 ? 444  ARG A CB    1 
ATOM   3486 C CG    . ARG A 1 450 ? 13.20889  5.95040   38.11799  1.000 33.89931 ? 444  ARG A CG    1 
ATOM   3487 C CD    . ARG A 1 450 ? 13.78906  7.38053   38.16123  1.000 32.96776 ? 444  ARG A CD    1 
ATOM   3488 N NE    . ARG A 1 450 ? 12.82436  8.32760   37.62202  1.000 37.19557 ? 444  ARG A NE    1 
ATOM   3489 C CZ    . ARG A 1 450 ? 12.79428  8.76814   36.36717  1.000 38.35542 ? 444  ARG A CZ    1 
ATOM   3490 N NH1   . ARG A 1 450 ? 13.63724  8.31308   35.44803  1.000 35.07272 ? 444  ARG A NH1   1 
ATOM   3491 N NH2   . ARG A 1 450 ? 11.86163  9.65888   36.01247  1.000 38.16317 ? 444  ARG A NH2   1 
ATOM   3492 N N     . TRP A 1 451 ? 9.92494   3.89778   40.72759  1.000 24.73725 ? 445  TRP A N     1 
ATOM   3493 C CA    . TRP A 1 451 ? 9.26482   3.50524   41.96973  1.000 29.58623 ? 445  TRP A CA    1 
ATOM   3494 C C     . TRP A 1 451 ? 9.48330   2.02376   42.25680  1.000 33.02091 ? 445  TRP A C     1 
ATOM   3495 O O     . TRP A 1 451 ? 9.87924   1.64415   43.36942  1.000 31.97393 ? 445  TRP A O     1 
ATOM   3496 C CB    . TRP A 1 451 ? 7.77558   3.81220   41.89183  1.000 28.65324 ? 445  TRP A CB    1 
ATOM   3497 C CG    . TRP A 1 451 ? 7.03032   3.74768   43.20809  1.000 27.20827 ? 445  TRP A CG    1 
ATOM   3498 C CD1   . TRP A 1 451 ? 6.83348   4.77830   44.07955  1.000 35.78531 ? 445  TRP A CD1   1 
ATOM   3499 C CD2   . TRP A 1 451 ? 6.35142   2.60853   43.77160  1.000 32.24004 ? 445  TRP A CD2   1 
ATOM   3500 N NE1   . TRP A 1 451 ? 6.08102   4.34783   45.15616  1.000 37.05970 ? 445  TRP A NE1   1 
ATOM   3501 C CE2   . TRP A 1 451 ? 5.76900   3.02473   44.98505  1.000 35.10120 ? 445  TRP A CE2   1 
ATOM   3502 C CE3   . TRP A 1 451 ? 6.19005   1.28076   43.37037  1.000 32.58495 ? 445  TRP A CE3   1 
ATOM   3503 C CZ2   . TRP A 1 451 ? 5.04254   2.15437   45.80700  1.000 40.41561 ? 445  TRP A CZ2   1 
ATOM   3504 C CZ3   . TRP A 1 451 ? 5.45148   0.42167   44.17500  1.000 37.31636 ? 445  TRP A CZ3   1 
ATOM   3505 C CH2   . TRP A 1 451 ? 4.88728   0.86834   45.38385  1.000 37.62208 ? 445  TRP A CH2   1 
ATOM   3506 N N     . ILE A 1 452 ? 9.23088   1.16350   41.26090  1.000 27.79774 ? 446  ILE A N     1 
ATOM   3507 C CA    . ILE A 1 452 ? 9.38996   -0.27791  41.47560  1.000 26.50113 ? 446  ILE A CA    1 
ATOM   3508 C C     . ILE A 1 452 ? 10.81373  -0.60309  41.91136  1.000 27.64720 ? 446  ILE A C     1 
ATOM   3509 O O     . ILE A 1 452 ? 11.04038  -1.35186  42.87160  1.000 31.24585 ? 446  ILE A O     1 
ATOM   3510 C CB    . ILE A 1 452 ? 8.99740   -1.04614  40.19672  1.000 28.20461 ? 446  ILE A CB    1 
ATOM   3511 C CG1   . ILE A 1 452 ? 7.49299   -0.93039  39.94960  1.000 25.07060 ? 446  ILE A CG1   1 
ATOM   3512 C CG2   . ILE A 1 452 ? 9.40825   -2.53267  40.28774  1.000 23.11787 ? 446  ILE A CG2   1 
ATOM   3513 C CD1   . ILE A 1 452 ? 7.08925   -1.15571  38.47152  1.000 24.90123 ? 446  ILE A CD1   1 
ATOM   3514 N N     . ALA A 1 453 ? 11.79894  -0.00456  41.24563  1.000 27.99065 ? 447  ALA A N     1 
ATOM   3515 C CA    . ALA A 1 453 ? 13.18667  -0.32477  41.54862  1.000 29.87056 ? 447  ALA A CA    1 
ATOM   3516 C C     . ALA A 1 453 ? 13.58564  0.14010   42.94756  1.000 37.02467 ? 447  ALA A C     1 
ATOM   3517 O O     . ALA A 1 453 ? 14.33935  -0.55093  43.64832  1.000 30.45767 ? 447  ALA A O     1 
ATOM   3518 C CB    . ALA A 1 453 ? 14.10266  0.29214   40.49774  1.000 27.43929 ? 447  ALA A CB    1 
ATOM   3519 N N     . ASP A 1 454 ? 13.09648  1.30645   43.37581  1.000 32.46440 ? 448  ASP A N     1 
ATOM   3520 C CA    . ASP A 1 454 ? 13.38456  1.74306   44.74288  1.000 34.23691 ? 448  ASP A CA    1 
ATOM   3521 C C     . ASP A 1 454 ? 12.75908  0.80086   45.76397  1.000 36.59861 ? 448  ASP A C     1 
ATOM   3522 O O     . ASP A 1 454 ? 13.34983  0.53380   46.82138  1.000 37.99952 ? 448  ASP A O     1 
ATOM   3523 C CB    . ASP A 1 454 ? 12.87033  3.17315   44.97313  1.000 33.27984 ? 448  ASP A CB    1 
ATOM   3524 C CG    . ASP A 1 454 ? 13.78291  4.24893   44.39309  1.000 39.46930 ? 448  ASP A CG    1 
ATOM   3525 O OD1   . ASP A 1 454 ? 14.95609  3.98298   44.07915  1.000 40.73558 ? 448  ASP A OD1   1 
ATOM   3526 O OD2   . ASP A 1 454 ? 13.30037  5.39159   44.25202  1.000 42.05198 ? 448  ASP A OD2   1 
ATOM   3527 N N     . LEU A 1 455 ? 11.54242  0.31910   45.49059  1.000 29.08556 ? 449  LEU A N     1 
ATOM   3528 C CA    . LEU A 1 455 ? 10.92119  -0.67546  46.36027  1.000 34.65699 ? 449  LEU A CA    1 
ATOM   3529 C C     . LEU A 1 455 ? 11.73217  -1.96734  46.40876  1.000 39.81958 ? 449  LEU A C     1 
ATOM   3530 O O     . LEU A 1 455 ? 11.93510  -2.54314  47.48565  1.000 35.96551 ? 449  LEU A O     1 
ATOM   3531 C CB    . LEU A 1 455 ? 9.49689   -0.96548  45.89304  1.000 32.21265 ? 449  LEU A CB    1 
ATOM   3532 C CG    . LEU A 1 455 ? 8.74634   -2.09385  46.60155  1.000 38.87991 ? 449  LEU A CG    1 
ATOM   3533 C CD1   . LEU A 1 455 ? 8.89549   -2.02599  48.11775  1.000 40.58711 ? 449  LEU A CD1   1 
ATOM   3534 C CD2   . LEU A 1 455 ? 7.29020   -2.03606  46.23399  1.000 36.40028 ? 449  LEU A CD2   1 
ATOM   3535 N N     . ILE A 1 456 ? 12.18848  -2.45568  45.25789  1.000 31.79929 ? 450  ILE A N     1 
ATOM   3536 C CA    . ILE A 1 456 ? 13.00605  -3.66543  45.26981  1.000 28.64935 ? 450  ILE A CA    1 
ATOM   3537 C C     . ILE A 1 456 ? 14.30003  -3.43343  46.04295  1.000 36.30695 ? 450  ILE A C     1 
ATOM   3538 O O     . ILE A 1 456 ? 14.75440  -4.31033  46.79350  1.000 43.06745 ? 450  ILE A O     1 
ATOM   3539 C CB    . ILE A 1 456 ? 13.25831  -4.14909  43.82914  1.000 31.73753 ? 450  ILE A CB    1 
ATOM   3540 C CG1   . ILE A 1 456 ? 11.95652  -4.72750  43.26829  1.000 31.38757 ? 450  ILE A CG1   1 
ATOM   3541 C CG2   . ILE A 1 456 ? 14.35358  -5.19294  43.81330  1.000 30.49940 ? 450  ILE A CG2   1 
ATOM   3542 C CD1   . ILE A 1 456 ? 11.98810  -4.99048  41.77513  1.000 29.16730 ? 450  ILE A CD1   1 
ATOM   3543 N N     . GLY A 1 457 ? 14.90193  -2.24767  45.90289  1.000 37.20281 ? 451  GLY A N     1 
ATOM   3544 C CA    . GLY A 1 457 ? 16.10914  -1.94574  46.65743  1.000 38.32818 ? 451  GLY A CA    1 
ATOM   3545 C C     . GLY A 1 457 ? 15.85596  -1.89858  48.15239  1.000 40.41325 ? 451  GLY A C     1 
ATOM   3546 O O     . GLY A 1 457 ? 16.65781  -2.40077  48.94644  1.000 44.81015 ? 451  GLY A O     1 
ATOM   3547 N N     . TYR A 1 458 ? 14.72600  -1.31096  48.54810  1.000 40.54641 ? 452  TYR A N     1 
ATOM   3548 C CA    . TYR A 1 458 ? 14.29941  -1.30504  49.94147  1.000 41.56220 ? 452  TYR A CA    1 
ATOM   3549 C C     . TYR A 1 458 ? 14.16366  -2.72222  50.47891  1.000 49.49701 ? 452  TYR A C     1 
ATOM   3550 O O     . TYR A 1 458 ? 14.51264  -2.99771  51.63487  1.000 47.39672 ? 452  TYR A O     1 
ATOM   3551 C CB    . TYR A 1 458 ? 12.97386  -0.55912  50.03706  1.000 39.25586 ? 452  TYR A CB    1 
ATOM   3552 C CG    . TYR A 1 458 ? 12.33252  -0.45812  51.39681  1.000 46.20218 ? 452  TYR A CG    1 
ATOM   3553 C CD1   . TYR A 1 458 ? 12.64805  0.59552   52.25575  1.000 55.00915 ? 452  TYR A CD1   1 
ATOM   3554 C CD2   . TYR A 1 458 ? 11.35588  -1.35938  51.79714  1.000 44.55719 ? 452  TYR A CD2   1 
ATOM   3555 C CE1   . TYR A 1 458 ? 12.03329  0.72395   53.49766  1.000 54.66251 ? 452  TYR A CE1   1 
ATOM   3556 C CE2   . TYR A 1 458 ? 10.73895  -1.24480  53.03561  1.000 51.34661 ? 452  TYR A CE2   1 
ATOM   3557 C CZ    . TYR A 1 458 ? 11.08172  -0.19977  53.88022  1.000 57.04884 ? 452  TYR A CZ    1 
ATOM   3558 O OH    . TYR A 1 458 ? 10.46869  -0.07335  55.10560  1.000 63.61425 ? 452  TYR A OH    1 
ATOM   3559 N N     . ALA A 1 459 ? 13.65437  -3.63751  49.65062  1.000 44.25083 ? 453  ALA A N     1 
ATOM   3560 C CA    . ALA A 1 459 ? 13.45726  -5.00544  50.10763  1.000 45.82620 ? 453  ALA A CA    1 
ATOM   3561 C C     . ALA A 1 459 ? 14.78698  -5.71569  50.30624  1.000 48.99333 ? 453  ALA A C     1 
ATOM   3562 O O     . ALA A 1 459 ? 14.93559  -6.49186  51.25332  1.000 45.87494 ? 453  ALA A O     1 
ATOM   3563 C CB    . ALA A 1 459 ? 12.57505  -5.77365  49.12717  1.000 42.21732 ? 453  ALA A CB    1 
ATOM   3564 N N     . GLU A 1 460 ? 15.76089  -5.47994  49.41884  1.000 46.46056 ? 454  GLU A N     1 
ATOM   3565 C CA    . GLU A 1 460 ? 17.08567  -6.06019  49.62479  1.000 50.58269 ? 454  GLU A CA    1 
ATOM   3566 C C     . GLU A 1 460 ? 17.72948  -5.51351  50.89008  1.000 58.58132 ? 454  GLU A C     1 
ATOM   3567 O O     . GLU A 1 460 ? 18.37990  -6.25448  51.63689  1.000 52.31253 ? 454  GLU A O     1 
ATOM   3568 C CB    . GLU A 1 460 ? 17.99295  -5.79801  48.42204  1.000 48.89762 ? 454  GLU A CB    1 
ATOM   3569 C CG    . GLU A 1 460 ? 19.06136  -6.87988  48.23428  1.000 66.96166 ? 454  GLU A CG    1 
ATOM   3570 C CD    . GLU A 1 460 ? 19.27508  -7.30792  46.77772  1.000 76.91107 ? 454  GLU A CD    1 
ATOM   3571 O OE1   . GLU A 1 460 ? 18.35161  -7.91269  46.17785  1.000 68.22842 ? 454  GLU A OE1   1 
ATOM   3572 O OE2   . GLU A 1 460 ? 20.38454  -7.06278  46.24542  1.000 74.97816 ? 454  GLU A OE2   1 
ATOM   3573 N N     . ASP A 1 461 ? 17.55202  -4.21467  51.14773  1.000 55.22173 ? 455  ASP A N     1 
ATOM   3574 C CA    . ASP A 1 461 ? 18.15028  -3.59207  52.32394  1.000 58.82721 ? 455  ASP A CA    1 
ATOM   3575 C C     . ASP A 1 461 ? 17.53628  -4.12311  53.61720  1.000 56.35847 ? 455  ASP A C     1 
ATOM   3576 O O     . ASP A 1 461 ? 18.23428  -4.26399  54.62609  1.000 62.57833 ? 455  ASP A O     1 
ATOM   3577 C CB    . ASP A 1 461 ? 17.99222  -2.07288  52.22996  1.000 59.05041 ? 455  ASP A CB    1 
ATOM   3578 C CG    . ASP A 1 461 ? 18.86683  -1.45502  51.14356  1.000 62.19762 ? 455  ASP A CG    1 
ATOM   3579 O OD1   . ASP A 1 461 ? 18.92765  -0.20938  51.07510  1.000 68.30584 ? 455  ASP A OD1   1 
ATOM   3580 O OD2   . ASP A 1 461 ? 19.51158  -2.20096  50.37489  1.000 70.64233 ? 455  ASP A OD2   1 
ATOM   3581 N N     . HIS A 1 462 ? 16.23529  -4.41706  53.61018  1.000 55.27278 ? 456  HIS A N     1 
ATOM   3582 C CA    . HIS A 1 462 ? 15.50614  -4.85306  54.79404  1.000 53.31411 ? 456  HIS A CA    1 
ATOM   3583 C C     . HIS A 1 462 ? 15.20583  -6.34814  54.77513  1.000 51.51950 ? 456  HIS A C     1 
ATOM   3584 O O     . HIS A 1 462 ? 14.32792  -6.80960  55.51635  1.000 52.79050 ? 456  HIS A O     1 
ATOM   3585 C CB    . HIS A 1 462 ? 14.21324  -4.05259  54.93255  1.000 53.01260 ? 456  HIS A CB    1 
ATOM   3586 C CG    . HIS A 1 462 ? 14.43654  -2.61305  55.26360  1.000 60.09075 ? 456  HIS A CG    1 
ATOM   3587 N ND1   . HIS A 1 462 ? 15.65335  -1.99072  55.07973  1.000 66.42780 ? 456  HIS A ND1   1 
ATOM   3588 C CD2   . HIS A 1 462 ? 13.60721  -1.67562  55.77970  1.000 62.60593 ? 456  HIS A CD2   1 
ATOM   3589 C CE1   . HIS A 1 462 ? 15.56065  -0.72960  55.45893  1.000 66.88588 ? 456  HIS A CE1   1 
ATOM   3590 N NE2   . HIS A 1 462 ? 14.33022  -0.51346  55.88960  1.000 67.19735 ? 456  HIS A NE2   1 
ATOM   3591 N N     . GLN A 1 463 ? 15.91143  -7.10101  53.93070  1.000 53.78951 ? 457  GLN A N     1 
ATOM   3592 C CA    . GLN A 1 463 ? 15.77737  -8.55396  53.81447  1.000 54.02908 ? 457  GLN A CA    1 
ATOM   3593 C C     . GLN A 1 463 ? 14.31520  -9.00534  53.76156  1.000 55.88728 ? 457  GLN A C     1 
ATOM   3594 O O     . GLN A 1 463 ? 13.90520  -9.94087  54.45176  1.000 54.32810 ? 457  GLN A O     1 
ATOM   3595 C CB    . GLN A 1 463 ? 16.52760  -9.24646  54.95153  1.000 63.94788 ? 457  GLN A CB    1 
ATOM   3596 C CG    . GLN A 1 463 ? 17.99858  -8.83873  55.04767  1.000 69.93142 ? 457  GLN A CG    1 
ATOM   3597 C CD    . GLN A 1 463 ? 18.88849  -9.94111  55.60884  1.000 83.05742 ? 457  GLN A CD    1 
ATOM   3598 O OE1   . GLN A 1 463 ? 18.43309  -10.79529 56.36968  1.000 89.71349 ? 457  GLN A OE1   1 
ATOM   3599 N NE2   . GLN A 1 463 ? 20.16522  -9.92382  55.23434  1.000 85.68111 ? 457  GLN A NE2   1 
ATOM   3600 N N     . ILE A 1 464 ? 13.51734  -8.32149  52.92068  1.000 51.82901 ? 458  ILE A N     1 
ATOM   3601 C CA    . ILE A 1 464 ? 12.13157  -8.69152  52.62903  1.000 49.56805 ? 458  ILE A CA    1 
ATOM   3602 C C     . ILE A 1 464 ? 12.11034  -9.49029  51.33696  1.000 46.76320 ? 458  ILE A C     1 
ATOM   3603 O O     . ILE A 1 464 ? 12.75837  -9.10983  50.35765  1.000 43.13443 ? 458  ILE A O     1 
ATOM   3604 C CB    . ILE A 1 464 ? 11.22683  -7.44683  52.52141  1.000 50.74877 ? 458  ILE A CB    1 
ATOM   3605 C CG1   . ILE A 1 464 ? 11.14127  -6.74552  53.87807  1.000 54.13044 ? 458  ILE A CG1   1 
ATOM   3606 C CG2   . ILE A 1 464 ? 9.84770   -7.81105  51.97459  1.000 56.65267 ? 458  ILE A CG2   1 
ATOM   3607 C CD1   . ILE A 1 464 ? 10.33053  -5.47853  53.87296  1.000 56.72919 ? 458  ILE A CD1   1 
ATOM   3608 N N     . ASN A 1 465 ? 11.38182  -10.60759 51.32740  1.000 48.83548 ? 459  ASN A N     1 
ATOM   3609 C CA    . ASN A 1 465 ? 11.41926  -11.51164 50.18101  1.000 49.20142 ? 459  ASN A CA    1 
ATOM   3610 C C     . ASN A 1 465 ? 10.06517  -11.69694 49.51470  1.000 39.41927 ? 459  ASN A C     1 
ATOM   3611 O O     . ASN A 1 465 ? 9.97841   -12.41639 48.51071  1.000 38.97322 ? 459  ASN A O     1 
ATOM   3612 C CB    . ASN A 1 465 ? 11.99263  -12.88295 50.58822  1.000 49.09466 ? 459  ASN A CB    1 
ATOM   3613 C CG    . ASN A 1 465 ? 11.07242  -13.66896 51.51855  1.000 53.18595 ? 459  ASN A CG    1 
ATOM   3614 O OD1   . ASN A 1 465 ? 10.21002  -13.11500 52.20531  1.000 56.16757 ? 459  ASN A OD1   1 
ATOM   3615 N ND2   . ASN A 1 465 ? 11.27006  -14.97841 51.54729  1.000 57.98218 ? 459  ASN A ND2   1 
ATOM   3616 N N     . GLN A 1 466 ? 9.01295   -11.07462 50.03977  1.000 37.60888 ? 460  GLN A N     1 
ATOM   3617 C CA    . GLN A 1 466 ? 7.69226   -11.12753 49.43757  1.000 43.78866 ? 460  GLN A CA    1 
ATOM   3618 C C     . GLN A 1 466 ? 7.01080   -9.78107  49.65032  1.000 45.75485 ? 460  GLN A C     1 
ATOM   3619 O O     . GLN A 1 466 ? 6.90222   -9.30337  50.78648  1.000 46.68536 ? 460  GLN A O     1 
ATOM   3620 C CB    . GLN A 1 466 ? 6.85954   -12.28239 50.01484  1.000 41.46722 ? 460  GLN A CB    1 
ATOM   3621 C CG    . GLN A 1 466 ? 5.51779   -12.47999 49.33835  1.000 43.50132 ? 460  GLN A CG    1 
ATOM   3622 C CD    . GLN A 1 466 ? 4.94716   -13.87469 49.52955  1.000 41.33860 ? 460  GLN A CD    1 
ATOM   3623 O OE1   . GLN A 1 466 ? 5.68529   -14.85911 49.56141  1.000 46.69547 ? 460  GLN A OE1   1 
ATOM   3624 N NE2   . GLN A 1 466 ? 3.62733   -13.96294 49.65675  1.000 44.36024 ? 460  GLN A NE2   1 
ATOM   3625 N N     . ILE A 1 467 ? 6.58427   -9.16575  48.54753  1.000 38.52132 ? 461  ILE A N     1 
ATOM   3626 C CA    . ILE A 1 467 ? 5.86773   -7.89432  48.53403  1.000 42.64243 ? 461  ILE A CA    1 
ATOM   3627 C C     . ILE A 1 467 ? 4.51887   -8.10671  47.86697  1.000 42.87059 ? 461  ILE A C     1 
ATOM   3628 O O     . ILE A 1 467 ? 4.44763   -8.66909  46.76764  1.000 46.88296 ? 461  ILE A O     1 
ATOM   3629 C CB    . ILE A 1 467 ? 6.66908   -6.80241  47.80043  1.000 37.54964 ? 461  ILE A CB    1 
ATOM   3630 C CG1   . ILE A 1 467 ? 8.13772   -6.82503  48.25031  1.000 42.82901 ? 461  ILE A CG1   1 
ATOM   3631 C CG2   . ILE A 1 467 ? 5.98962   -5.44621  47.96127  1.000 41.42615 ? 461  ILE A CG2   1 
ATOM   3632 C CD1   . ILE A 1 467 ? 9.09357   -5.95634  47.42675  1.000 34.15711 ? 461  ILE A CD1   1 
ATOM   3633 N N     . GLU A 1 468 ? 3.45359   -7.63800  48.50643  1.000 41.00440 ? 462  GLU A N     1 
ATOM   3634 C CA    . GLU A 1 468 ? 2.12767   -7.86294  47.95270  1.000 44.90470 ? 462  GLU A CA    1 
ATOM   3635 C C     . GLU A 1 468 ? 1.18059   -6.75002  48.37774  1.000 49.31477 ? 462  GLU A C     1 
ATOM   3636 O O     . GLU A 1 468 ? 1.22377   -6.29837  49.52175  1.000 49.48062 ? 462  GLU A O     1 
ATOM   3637 C CB    . GLU A 1 468 ? 1.57830   -9.22704  48.38247  1.000 49.31369 ? 462  GLU A CB    1 
ATOM   3638 C CG    . GLU A 1 468 ? 0.43197   -9.73188  47.51836  1.000 48.64437 ? 462  GLU A CG    1 
ATOM   3639 C CD    . GLU A 1 468 ? -0.45331  -10.74456 48.22337  1.000 60.19633 ? 462  GLU A CD    1 
ATOM   3640 O OE1   . GLU A 1 468 ? 0.04497   -11.46999 49.12246  1.000 59.15942 ? 462  GLU A OE1   1 
ATOM   3641 O OE2   . GLU A 1 468 ? -1.65858  -10.78730 47.88694  1.000 58.11469 ? 462  GLU A OE2   1 
ATOM   3642 N N     . ALA A 1 469 ? 0.32763   -6.31523  47.44962  1.000 43.37512 ? 463  ALA A N     1 
ATOM   3643 C CA    . ALA A 1 469 ? -0.70218  -5.33270  47.76242  1.000 46.90957 ? 463  ALA A CA    1 
ATOM   3644 C C     . ALA A 1 469 ? -1.91476  -5.99815  48.41114  1.000 47.99910 ? 463  ALA A C     1 
ATOM   3645 O O     . ALA A 1 469 ? -2.33680  -7.08998  48.02035  1.000 49.06728 ? 463  ALA A O     1 
ATOM   3646 C CB    . ALA A 1 469 ? -1.14371  -4.58446  46.49863  1.000 38.90786 ? 463  ALA A CB    1 
ATOM   3647 N N     . THR A 1 470 ? -2.49403  -5.31090  49.39575  1.000 46.57642 ? 464  THR A N     1 
ATOM   3648 C CA    . THR A 1 470 ? -3.69158  -5.80649  50.06180  1.000 46.04644 ? 464  THR A CA    1 
ATOM   3649 C C     . THR A 1 470 ? -4.93225  -5.54032  49.21552  1.000 47.72469 ? 464  THR A C     1 
ATOM   3650 O O     . THR A 1 470 ? -4.98329  -4.58490  48.43369  1.000 49.44583 ? 464  THR A O     1 
ATOM   3651 C CB    . THR A 1 470 ? -3.86038  -5.13925  51.42591  1.000 47.42265 ? 464  THR A CB    1 
ATOM   3652 O OG1   . THR A 1 470 ? -4.10846  -3.73561  51.24653  1.000 45.03031 ? 464  THR A OG1   1 
ATOM   3653 C CG2   . THR A 1 470 ? -2.59408  -5.32574  52.26282  1.000 39.51170 ? 464  THR A CG2   1 
ATOM   3654 N N     . LYS A 1 471 ? -5.94579  -6.39756  49.38301  1.000 48.36869 ? 465  LYS A N     1 
ATOM   3655 C CA    . LYS A 1 471 ? -7.22509  -6.16812  48.71493  1.000 49.94357 ? 465  LYS A CA    1 
ATOM   3656 C C     . LYS A 1 471 ? -7.77896  -4.78264  49.03067  1.000 52.76264 ? 465  LYS A C     1 
ATOM   3657 O O     . LYS A 1 471 ? -8.40031  -4.13557  48.17410  1.000 49.66210 ? 465  LYS A O     1 
ATOM   3658 C CB    . LYS A 1 471 ? -8.23374  -7.24381  49.12626  1.000 53.62706 ? 465  LYS A CB    1 
ATOM   3659 C CG    . LYS A 1 471 ? -9.58179  -7.10340  48.43291  1.000 68.87616 ? 465  LYS A CG    1 
ATOM   3660 C CD    . LYS A 1 471 ? -10.49180 -8.30004  48.69551  1.000 75.74766 ? 465  LYS A CD    1 
ATOM   3661 C CE    . LYS A 1 471 ? -11.59500 -8.39600  47.64565  1.000 74.04223 ? 465  LYS A CE    1 
ATOM   3662 N NZ    . LYS A 1 471 ? -12.73424 -7.48904  47.95476  1.000 78.64516 ? 465  LYS A NZ    1 
ATOM   3663 N N     . ASP A 1 472 ? -7.56280  -4.31414  50.26199  1.000 48.70658 ? 466  ASP A N     1 
ATOM   3664 C CA    . ASP A 1 472 ? -8.11954  -3.03442  50.68381  1.000 52.24396 ? 466  ASP A CA    1 
ATOM   3665 C C     . ASP A 1 472 ? -7.42129  -1.87324  49.98872  1.000 46.41741 ? 466  ASP A C     1 
ATOM   3666 O O     . ASP A 1 472 ? -8.05135  -0.85817  49.68380  1.000 44.07758 ? 466  ASP A O     1 
ATOM   3667 C CB    . ASP A 1 472 ? -8.00983  -2.89106  52.20233  1.000 52.74096 ? 466  ASP A CB    1 
ATOM   3668 C CG    . ASP A 1 472 ? -9.08009  -3.68748  52.94751  1.000 63.11040 ? 466  ASP A CG    1 
ATOM   3669 O OD1   . ASP A 1 472 ? -9.89010  -4.38341  52.29424  1.000 63.07368 ? 466  ASP A OD1   1 
ATOM   3670 O OD2   . ASP A 1 472 ? -9.10934  -3.62468  54.19451  1.000 72.36541 ? 466  ASP A OD2   1 
ATOM   3671 N N     . ALA A 1 473 ? -6.11512  -1.99437  49.75158  1.000 43.44131 ? 467  ALA A N     1 
ATOM   3672 C CA    . ALA A 1 473 ? -5.41561  -0.92279  49.05202  1.000 41.94480 ? 467  ALA A CA    1 
ATOM   3673 C C     . ALA A 1 473 ? -5.80762  -0.89410  47.57662  1.000 44.86401 ? 467  ALA A C     1 
ATOM   3674 O O     . ALA A 1 473 ? -5.94616  0.18609   46.99058  1.000 42.06421 ? 467  ALA A O     1 
ATOM   3675 C CB    . ALA A 1 473 ? -3.90603  -1.08149  49.22069  1.000 40.24636 ? 467  ALA A CB    1 
ATOM   3676 N N     . VAL A 1 474 ? -6.02472  -2.07068  46.97195  1.000 39.65035 ? 468  VAL A N     1 
ATOM   3677 C CA    . VAL A 1 474 ? -6.51626  -2.12555  45.59484  1.000 41.04846 ? 468  VAL A CA    1 
ATOM   3678 C C     . VAL A 1 474 ? -7.87465  -1.45376  45.50052  1.000 47.85858 ? 468  VAL A C     1 
ATOM   3679 O O     . VAL A 1 474 ? -8.11358  -0.59838  44.63892  1.000 42.12308 ? 468  VAL A O     1 
ATOM   3680 C CB    . VAL A 1 474 ? -6.58398  -3.58000  45.09634  1.000 41.61296 ? 468  VAL A CB    1 
ATOM   3681 C CG1   . VAL A 1 474 ? -7.39512  -3.66485  43.80814  1.000 42.15236 ? 468  VAL A CG1   1 
ATOM   3682 C CG2   . VAL A 1 474 ? -5.18855  -4.15618  44.89423  1.000 42.00428 ? 468  VAL A CG2   1 
ATOM   3683 N N     . ASP A 1 475 ? -8.79017  -1.83507  46.39296  1.000 48.21701 ? 469  ASP A N     1 
ATOM   3684 C CA    . ASP A 1 475 ? -10.12339 -1.25224  46.36422  1.000 47.94569 ? 469  ASP A CA    1 
ATOM   3685 C C     . ASP A 1 475 ? -10.08651 0.23563   46.69813  1.000 48.01827 ? 469  ASP A C     1 
ATOM   3686 O O     . ASP A 1 475 ? -10.90418 1.00033   46.17709  1.000 48.39154 ? 469  ASP A O     1 
ATOM   3687 C CB    . ASP A 1 475 ? -11.04439 -2.01680  47.31914  1.000 53.08850 ? 469  ASP A CB    1 
ATOM   3688 C CG    . ASP A 1 475 ? -11.36895 -3.42316  46.81916  1.000 61.62930 ? 469  ASP A CG    1 
ATOM   3689 O OD1   . ASP A 1 475 ? -10.92735 -3.77810  45.70765  1.000 69.05016 ? 469  ASP A OD1   1 
ATOM   3690 O OD2   . ASP A 1 475 ? -12.05370 -4.18245  47.54073  1.000 65.89102 ? 469  ASP A OD2   1 
ATOM   3691 N N     . ASN A 1 476 ? -9.13720  0.67555   47.53389  1.000 41.56330 ? 470  ASN A N     1 
ATOM   3692 C CA    . ASN A 1 476 ? -8.99671  2.10998   47.76121  1.000 49.15691 ? 470  ASN A CA    1 
ATOM   3693 C C     . ASN A 1 476 ? -8.54273  2.82164   46.48764  1.000 45.61774 ? 470  ASN A C     1 
ATOM   3694 O O     . ASN A 1 476 ? -8.99066  3.93837   46.19985  1.000 46.60724 ? 470  ASN A O     1 
ATOM   3695 C CB    . ASN A 1 476 ? -8.01181  2.37348   48.90173  1.000 51.51630 ? 470  ASN A CB    1 
ATOM   3696 C CG    . ASN A 1 476 ? -7.84153  3.86748   49.20655  1.000 62.85758 ? 470  ASN A CG    1 
ATOM   3697 O OD1   . ASN A 1 476 ? -7.25851  4.62128   48.42008  1.000 61.84793 ? 470  ASN A OD1   1 
ATOM   3698 N ND2   . ASN A 1 476 ? -8.34052  4.29352   50.36824  1.000 64.89684 ? 470  ASN A ND2   1 
ATOM   3699 N N     . TRP A 1 477 ? -7.63496  2.19708   45.72732  1.000 46.58382 ? 471  TRP A N     1 
ATOM   3700 C CA    . TRP A 1 477 ? -7.18170  2.78096   44.46222  1.000 40.79253 ? 471  TRP A CA    1 
ATOM   3701 C C     . TRP A 1 477 ? -8.32367  2.85847   43.45742  1.000 39.76678 ? 471  TRP A C     1 
ATOM   3702 O O     . TRP A 1 477 ? -8.50769  3.88463   42.79321  1.000 44.57408 ? 471  TRP A O     1 
ATOM   3703 C CB    . TRP A 1 477 ? -6.00337  1.97172   43.89090  1.000 44.13832 ? 471  TRP A CB    1 
ATOM   3704 C CG    . TRP A 1 477 ? -5.36290  2.60905   42.66151  1.000 38.85157 ? 471  TRP A CG    1 
ATOM   3705 C CD1   . TRP A 1 477 ? -5.32962  2.09344   41.39007  1.000 38.03406 ? 471  TRP A CD1   1 
ATOM   3706 C CD2   . TRP A 1 477 ? -4.68094  3.87625   42.59703  1.000 35.50938 ? 471  TRP A CD2   1 
ATOM   3707 N NE1   . TRP A 1 477 ? -4.68140  2.96605   40.54186  1.000 32.30619 ? 471  TRP A NE1   1 
ATOM   3708 C CE2   . TRP A 1 477 ? -4.27506  4.06619   41.25279  1.000 34.23695 ? 471  TRP A CE2   1 
ATOM   3709 C CE3   . TRP A 1 477 ? -4.38009  4.86916   43.53875  1.000 40.41155 ? 471  TRP A CE3   1 
ATOM   3710 C CZ2   . TRP A 1 477 ? -3.57908  5.20441   40.83344  1.000 31.93206 ? 471  TRP A CZ2   1 
ATOM   3711 C CZ3   . TRP A 1 477 ? -3.68809  6.00844   43.11909  1.000 44.35713 ? 471  TRP A CZ3   1 
ATOM   3712 C CH2   . TRP A 1 477 ? -3.30517  6.16348   41.76730  1.000 37.80499 ? 471  TRP A CH2   1 
ATOM   3713 N N     . THR A 1 478 ? -9.10944  1.78485   43.34320  1.000 41.12804 ? 472  THR A N     1 
ATOM   3714 C CA    . THR A 1 478 ? -10.28660 1.79304   42.48588  1.000 40.35514 ? 472  THR A CA    1 
ATOM   3715 C C     . THR A 1 478 ? -11.22454 2.95023   42.82676  1.000 47.91608 ? 472  THR A C     1 
ATOM   3716 O O     . THR A 1 478 ? -11.77670 3.59480   41.92450  1.000 44.97103 ? 472  THR A O     1 
ATOM   3717 C CB    . THR A 1 478 ? -11.00591 0.45434   42.60298  1.000 39.13765 ? 472  THR A CB    1 
ATOM   3718 O OG1   . THR A 1 478 ? -10.12066 -0.59224  42.18180  1.000 41.09394 ? 472  THR A OG1   1 
ATOM   3719 C CG2   . THR A 1 478 ? -12.25610 0.43759   41.73124  1.000 44.99457 ? 472  THR A CG2   1 
ATOM   3720 N N     . ASN A 1 479 ? -11.40105 3.24728   44.12288  1.000 44.82862 ? 473  ASN A N     1 
ATOM   3721 C CA    . ASN A 1 479 ? -12.28282 4.35052   44.50905  1.000 47.28744 ? 473  ASN A CA    1 
ATOM   3722 C C     . ASN A 1 479 ? -11.70028 5.69899   44.12358  1.000 43.27676 ? 473  ASN A C     1 
ATOM   3723 O O     . ASN A 1 479 ? -12.43060 6.57625   43.64486  1.000 45.07099 ? 473  ASN A O     1 
ATOM   3724 C CB    . ASN A 1 479 ? -12.57258 4.31617   46.01220  1.000 50.79672 ? 473  ASN A CB    1 
ATOM   3725 C CG    . ASN A 1 479 ? -13.19132 3.01845   46.44341  1.000 59.77441 ? 473  ASN A CG    1 
ATOM   3726 O OD1   . ASN A 1 479 ? -12.94001 2.53570   47.54550  1.000 68.29584 ? 473  ASN A OD1   1 
ATOM   3727 N ND2   . ASN A 1 479 ? -14.01806 2.43800   45.57194  1.000 61.79840 ? 473  ASN A ND2   1 
ATOM   3728 N N     . THR A 1 480 ? -10.39812 5.88271   44.34657  1.000 42.54547 ? 474  THR A N     1 
ATOM   3729 C CA    . THR A 1 480 ? -9.71557  7.11142   43.95075  1.000 43.33674 ? 474  THR A CA    1 
ATOM   3730 C C     . THR A 1 480 ? -9.90095  7.38808   42.46177  1.000 44.38917 ? 474  THR A C     1 
ATOM   3731 O O     . THR A 1 480 ? -10.26010 8.50442   42.06759  1.000 43.59006 ? 474  THR A O     1 
ATOM   3732 C CB    . THR A 1 480 ? -8.22941  7.01812   44.31167  1.000 42.88557 ? 474  THR A CB    1 
ATOM   3733 O OG1   . THR A 1 480 ? -8.09590  6.77715   45.71635  1.000 46.96324 ? 474  THR A OG1   1 
ATOM   3734 C CG2   . THR A 1 480 ? -7.47221  8.30858   43.94795  1.000 41.86664 ? 474  THR A CG2   1 
ATOM   3735 N N     . CYS A 1 481 ? -9.67241  6.37453   41.61901  1.000 43.83920 ? 475  CYS A N     1 
ATOM   3736 C CA    . CYS A 1 481 ? -9.88566  6.54704   40.18401  1.000 39.02486 ? 475  CYS A CA    1 
ATOM   3737 C C     . CYS A 1 481 ? -11.35326 6.81985   39.87275  1.000 44.49990 ? 475  CYS A C     1 
ATOM   3738 O O     . CYS A 1 481 ? -11.67210 7.70689   39.07479  1.000 40.49565 ? 475  CYS A O     1 
ATOM   3739 C CB    . CYS A 1 481 ? -9.40839  5.30654   39.42626  1.000 42.02080 ? 475  CYS A CB    1 
ATOM   3740 S SG    . CYS A 1 481 ? -7.66417  4.87529   39.61423  1.000 40.59409 ? 475  CYS A SG    1 
ATOM   3741 N N     . SER A 1 482 ? -12.26293 6.06075   40.49261  1.000 47.32556 ? 476  SER A N     1 
ATOM   3742 C CA    . SER A 1 482 ? -13.68479 6.22234   40.20770  1.000 42.54345 ? 476  SER A CA    1 
ATOM   3743 C C     . SER A 1 482 ? -14.16424 7.62138   40.56454  1.000 43.78523 ? 476  SER A C     1 
ATOM   3744 O O     . SER A 1 482 ? -14.92994 8.23333   39.80976  1.000 38.89184 ? 476  SER A O     1 
ATOM   3745 C CB    . SER A 1 482 ? -14.49082 5.17627   40.97078  1.000 46.26710 ? 476  SER A CB    1 
ATOM   3746 O OG    . SER A 1 482 ? -15.65202 4.83017   40.24708  1.000 52.53422 ? 476  SER A OG    1 
ATOM   3747 N N     . ASP A 1 483 ? -13.71803 8.14288   41.71106  1.000 42.97104 ? 477  ASP A N     1 
ATOM   3748 C CA    . ASP A 1 483 ? -14.10821 9.48733   42.12781  1.000 50.26560 ? 477  ASP A CA    1 
ATOM   3749 C C     . ASP A 1 483 ? -13.61164 10.53191  41.13847  1.000 49.51832 ? 477  ASP A C     1 
ATOM   3750 O O     . ASP A 1 483 ? -14.34315 11.46104  40.77350  1.000 44.89860 ? 477  ASP A O     1 
ATOM   3751 C CB    . ASP A 1 483 ? -13.56572 9.79310   43.52989  1.000 49.33870 ? 477  ASP A CB    1 
ATOM   3752 C CG    . ASP A 1 483 ? -14.37395 9.12999   44.64455  1.000 59.40098 ? 477  ASP A CG    1 
ATOM   3753 O OD1   . ASP A 1 483 ? -15.35805 8.41155   44.34632  1.000 59.13542 ? 477  ASP A OD1   1 
ATOM   3754 O OD2   . ASP A 1 483 ? -14.00840 9.32610   45.82675  1.000 61.05281 ? 477  ASP A OD2   1 
ATOM   3755 N N     . ILE A 1 484 ? -12.35176 10.41304  40.71910  1.000 45.78071 ? 478  ILE A N     1 
ATOM   3756 C CA    . ILE A 1 484 ? -11.81037 11.37688  39.77002  1.000 43.53256 ? 478  ILE A CA    1 
ATOM   3757 C C     . ILE A 1 484 ? -12.53903 11.29925  38.43511  1.000 41.60290 ? 478  ILE A C     1 
ATOM   3758 O O     . ILE A 1 484 ? -12.96856 12.32683  37.89672  1.000 43.42488 ? 478  ILE A O     1 
ATOM   3759 C CB    . ILE A 1 484 ? -10.29984 11.17791  39.60136  1.000 41.41439 ? 478  ILE A CB    1 
ATOM   3760 C CG1   . ILE A 1 484 ? -9.60487  11.52914  40.90804  1.000 40.59574 ? 478  ILE A CG1   1 
ATOM   3761 C CG2   . ILE A 1 484 ? -9.79762  12.00851  38.44043  1.000 46.26266 ? 478  ILE A CG2   1 
ATOM   3762 C CD1   . ILE A 1 484 ? -8.15429  11.11153  40.95552  1.000 46.57685 ? 478  ILE A CD1   1 
ATOM   3763 N N     . ALA A 1 485 ? -12.70377 10.08621  37.88732  1.000 39.56985 ? 479  ALA A N     1 
ATOM   3764 C CA    . ALA A 1 485 ? -13.30051 9.96449   36.55842  1.000 42.87308 ? 479  ALA A CA    1 
ATOM   3765 C C     . ALA A 1 485 ? -14.74980 10.43185  36.53569  1.000 50.47245 ? 479  ALA A C     1 
ATOM   3766 O O     . ALA A 1 485 ? -15.21181 10.95418  35.51475  1.000 45.60309 ? 479  ALA A O     1 
ATOM   3767 C CB    . ALA A 1 485 ? -13.20360 8.52534   36.04614  1.000 42.69628 ? 479  ALA A CB    1 
ATOM   3768 N N     . ASN A 1 486 ? -15.47939 10.27712  37.64718  1.000 47.29731 ? 480  ASN A N     1 
ATOM   3769 C CA    . ASN A 1 486 ? -16.88703 10.67183  37.65480  1.000 46.55436 ? 480  ASN A CA    1 
ATOM   3770 C C     . ASN A 1 486 ? -17.08119 12.17869  37.70689  1.000 45.24329 ? 480  ASN A C     1 
ATOM   3771 O O     . ASN A 1 486 ? -18.20590 12.65034  37.51360  1.000 45.86857 ? 480  ASN A O     1 
ATOM   3772 C CB    . ASN A 1 486 ? -17.60757 10.01315  38.82734  1.000 51.60092 ? 480  ASN A CB    1 
ATOM   3773 C CG    . ASN A 1 486 ? -17.87003 8.54460   38.58038  1.000 55.29238 ? 480  ASN A CG    1 
ATOM   3774 O OD1   . ASN A 1 486 ? -18.40080 8.16253   37.53374  1.000 57.09771 ? 480  ASN A OD1   1 
ATOM   3775 N ND2   . ASN A 1 486 ? -17.49126 7.70773   39.54123  1.000 63.86215 ? 480  ASN A ND2   1 
ATOM   3776 N N     . LYS A 1 487 ? -16.03185 12.94513  37.97378  1.000 38.87486 ? 481  LYS A N     1 
ATOM   3777 C CA    . LYS A 1 487 ? -16.12335 14.37867  37.76814  1.000 42.83489 ? 481  LYS A CA    1 
ATOM   3778 C C     . LYS A 1 487 ? -15.92787 14.76843  36.30554  1.000 43.32631 ? 481  LYS A C     1 
ATOM   3779 O O     . LYS A 1 487 ? -15.90086 15.96213  36.00298  1.000 44.36299 ? 481  LYS A O     1 
ATOM   3780 C CB    . LYS A 1 487 ? -15.09035 15.09529  38.63903  1.000 46.65406 ? 481  LYS A CB    1 
ATOM   3781 C CG    . LYS A 1 487 ? -15.10600 14.64820  40.10123  1.000 49.97208 ? 481  LYS A CG    1 
ATOM   3782 C CD    . LYS A 1 487 ? -14.22995 15.54655  40.97316  1.000 49.29174 ? 481  LYS A CD    1 
ATOM   3783 C CE    . LYS A 1 487 ? -14.69199 15.51938  42.43127  1.000 56.18197 ? 481  LYS A CE    1 
ATOM   3784 N NZ    . LYS A 1 487 ? -15.91740 14.68456  42.61023  1.000 59.06427 ? 481  LYS A NZ    1 
ATOM   3785 N N     . THR A 1 488 ? -15.78217 13.80796  35.39283  1.000 38.40692 ? 482  THR A N     1 
ATOM   3786 C CA    . THR A 1 488 ? -15.44877 14.12912  34.01153  1.000 47.74839 ? 482  THR A CA    1 
ATOM   3787 C C     . THR A 1 488 ? -16.50250 13.56724  33.07740  1.000 49.68921 ? 482  THR A C     1 
ATOM   3788 O O     . THR A 1 488 ? -17.23522 12.63628  33.42144  1.000 50.41403 ? 482  THR A O     1 
ATOM   3789 C CB    . THR A 1 488 ? -14.09808 13.54586  33.57747  1.000 48.77518 ? 482  THR A CB    1 
ATOM   3790 O OG1   . THR A 1 488 ? -14.16575 12.11805  33.63227  1.000 53.00705 ? 482  THR A OG1   1 
ATOM   3791 C CG2   . THR A 1 488 ? -12.98765 14.02000  34.51129  1.000 48.00854 ? 482  THR A CG2   1 
ATOM   3792 N N     . LEU A 1 489 ? -16.54507 14.12853  31.86786  1.000 46.53567 ? 483  LEU A N     1 
ATOM   3793 C CA    . LEU A 1 489 ? -17.38303 13.57276  30.81781  1.000 49.29496 ? 483  LEU A CA    1 
ATOM   3794 C C     . LEU A 1 489 ? -16.80873 12.28821  30.24118  1.000 58.88786 ? 483  LEU A C     1 
ATOM   3795 O O     . LEU A 1 489 ? -17.48462 11.62765  29.44730  1.000 58.67236 ? 483  LEU A O     1 
ATOM   3796 C CB    . LEU A 1 489 ? -17.55958 14.60173  29.70837  1.000 49.18766 ? 483  LEU A CB    1 
ATOM   3797 C CG    . LEU A 1 489 ? -18.17468 15.91911  30.15949  1.000 47.37166 ? 483  LEU A CG    1 
ATOM   3798 C CD1   . LEU A 1 489 ? -18.01771 16.91850  29.06003  1.000 36.34591 ? 483  LEU A CD1   1 
ATOM   3799 C CD2   . LEU A 1 489 ? -19.63101 15.72458  30.48640  1.000 52.92779 ? 483  LEU A CD2   1 
ATOM   3800 N N     . PHE A 1 490 ? -15.57354 11.93476  30.60753  1.000 59.28048 ? 484  PHE A N     1 
ATOM   3801 C CA    . PHE A 1 490 ? -14.96958 10.70427  30.11307  1.000 61.29741 ? 484  PHE A CA    1 
ATOM   3802 C C     . PHE A 1 490 ? -15.61641 9.48610   30.74378  1.000 67.22838 ? 484  PHE A C     1 
ATOM   3803 O O     . PHE A 1 490 ? -15.65400 8.41600   30.12514  1.000 71.96143 ? 484  PHE A O     1 
ATOM   3804 C CB    . PHE A 1 490 ? -13.46915 10.69473  30.39085  1.000 64.45179 ? 484  PHE A CB    1 
ATOM   3805 C CG    . PHE A 1 490 ? -12.67664 11.62016  29.50805  1.000 73.20020 ? 484  PHE A CG    1 
ATOM   3806 C CD1   . PHE A 1 490 ? -11.29342 11.61916  29.55769  1.000 71.64204 ? 484  PHE A CD1   1 
ATOM   3807 C CD2   . PHE A 1 490 ? -13.31235 12.49319  28.63238  1.000 72.34370 ? 484  PHE A CD2   1 
ATOM   3808 C CE1   . PHE A 1 490 ? -10.55647 12.46378  28.74757  1.000 74.30703 ? 484  PHE A CE1   1 
ATOM   3809 C CE2   . PHE A 1 490 ? -12.58139 13.34613  27.82172  1.000 73.30267 ? 484  PHE A CE2   1 
ATOM   3810 C CZ    . PHE A 1 490 ? -11.20130 13.33077  27.87738  1.000 72.41554 ? 484  PHE A CZ    1 
ATOM   3811 N N     . ALA A 1 491 ? -16.11026 9.62514   31.97754  1.000 66.10921 ? 485  ALA A N     1 
ATOM   3812 C CA    . ALA A 1 491 ? -16.91792 8.56962   32.57754  1.000 65.71410 ? 485  ALA A CA    1 
ATOM   3813 C C     . ALA A 1 491 ? -18.10814 8.22895   31.68960  1.000 71.24780 ? 485  ALA A C     1 
ATOM   3814 O O     . ALA A 1 491 ? -18.40705 7.05023   31.46266  1.000 74.07192 ? 485  ALA A O     1 
ATOM   3815 C CB    . ALA A 1 491 ? -17.38083 8.99305   33.97017  1.000 61.57724 ? 485  ALA A CB    1 
ATOM   3816 N N     . LYS A 1 492 ? -18.78421 9.24843   31.15613  1.000 70.19540 ? 486  LYS A N     1 
ATOM   3817 C CA    . LYS A 1 492 ? -19.80139 9.04484   30.13014  1.000 70.80527 ? 486  LYS A CA    1 
ATOM   3818 C C     . LYS A 1 492 ? -19.12478 8.69689   28.80669  1.000 74.85225 ? 486  LYS A C     1 
ATOM   3819 O O     . LYS A 1 492 ? -18.20566 7.86965   28.77808  1.000 76.26894 ? 486  LYS A O     1 
ATOM   3820 C CB    . LYS A 1 492 ? -20.67703 10.29602  29.99477  1.000 66.72127 ? 486  LYS A CB    1 
ATOM   3821 C CG    . LYS A 1 492 ? -22.03500 10.06394  29.33786  1.000 71.07213 ? 486  LYS A CG    1 
ATOM   3822 C CD    . LYS A 1 492 ? -22.63980 11.37181  28.85750  1.000 69.79519 ? 486  LYS A CD    1 
ATOM   3823 C CE    . LYS A 1 492 ? -22.65646 12.40921  29.97292  1.000 69.84279 ? 486  LYS A CE    1 
ATOM   3824 N NZ    . LYS A 1 492 ? -23.11661 13.73819  29.48805  1.000 65.34956 ? 486  LYS A NZ    1 
ATOM   3825 N N     . ALA A 1 493 ? -19.56925 9.32281   27.71248  1.000 72.72410 ? 487  ALA A N     1 
ATOM   3826 C CA    . ALA A 1 493 ? -18.95876 9.17980   26.39342  1.000 73.91776 ? 487  ALA A CA    1 
ATOM   3827 C C     . ALA A 1 493 ? -18.72610 7.72575   25.99317  1.000 77.47219 ? 487  ALA A C     1 
ATOM   3828 O O     . ALA A 1 493 ? -19.35151 6.80727   26.53374  1.000 79.90340 ? 487  ALA A O     1 
ATOM   3829 C CB    . ALA A 1 493 ? -17.63686 9.94570   26.34172  1.000 68.95600 ? 487  ALA A CB    1 
ATOM   3830 N N     . LYS A 1 494 ? -17.82319 7.51080   25.04508  1.000 77.46660 ? 488  LYS A N     1 
ATOM   3831 C CA    . LYS A 1 494 ? -17.51532 6.16946   24.57774  1.000 77.49057 ? 488  LYS A CA    1 
ATOM   3832 C C     . LYS A 1 494 ? -16.30959 5.61081   25.32801  1.000 80.97144 ? 488  LYS A C     1 
ATOM   3833 O O     . LYS A 1 494 ? -16.27892 4.43624   25.69177  1.000 86.15832 ? 488  LYS A O     1 
ATOM   3834 C CB    . LYS A 1 494 ? -17.25626 6.18484   23.07069  1.000 78.42502 ? 488  LYS A CB    1 
ATOM   3835 C CG    . LYS A 1 494 ? -16.74397 4.87174   22.50114  1.000 83.48143 ? 488  LYS A CG    1 
ATOM   3836 C CD    . LYS A 1 494 ? -17.27799 4.64606   21.09364  1.000 77.97697 ? 488  LYS A CD    1 
ATOM   3837 C CE    . LYS A 1 494 ? -16.30136 5.18540   20.05437  1.000 72.95352 ? 488  LYS A CE    1 
ATOM   3838 N NZ    . LYS A 1 494 ? -16.83077 5.06917   18.66362  1.000 52.18267 ? 488  LYS A NZ    1 
ATOM   3839 N N     . THR A 1 508 ? -14.82591 -1.84448  37.97296  1.000 67.51802 ? 502  THR A N     1 
ATOM   3840 C CA    . THR A 1 508 ? -13.40967 -1.54131  37.74989  1.000 72.97227 ? 502  THR A CA    1 
ATOM   3841 C C     . THR A 1 508 ? -13.22725 -0.28107  36.88012  1.000 70.56064 ? 502  THR A C     1 
ATOM   3842 O O     . THR A 1 508 ? -14.06532 0.01487   36.02151  1.000 65.97134 ? 502  THR A O     1 
ATOM   3843 C CB    . THR A 1 508 ? -12.66802 -2.73230  37.08228  1.000 68.49415 ? 502  THR A CB    1 
ATOM   3844 O OG1   . THR A 1 508 ? -13.20655 -2.96065  35.77594  1.000 68.82616 ? 502  THR A OG1   1 
ATOM   3845 C CG2   . THR A 1 508 ? -12.80562 -4.00719  37.91630  1.000 63.58515 ? 502  THR A CG2   1 
ATOM   3846 N N     . VAL A 1 509 ? -12.12991 0.44761   37.11338  1.000 66.70733 ? 503  VAL A N     1 
ATOM   3847 C CA    . VAL A 1 509 ? -11.82980 1.72030   36.44932  1.000 61.51048 ? 503  VAL A CA    1 
ATOM   3848 C C     . VAL A 1 509 ? -10.45284 1.60762   35.79233  1.000 57.69554 ? 503  VAL A C     1 
ATOM   3849 O O     . VAL A 1 509 ? -9.43935  1.43780   36.48693  1.000 50.88538 ? 503  VAL A O     1 
ATOM   3850 C CB    . VAL A 1 509 ? -11.87155 2.90272   37.43798  1.000 61.40621 ? 503  VAL A CB    1 
ATOM   3851 C CG1   . VAL A 1 509 ? -11.67360 4.24458   36.71420  1.000 49.75466 ? 503  VAL A CG1   1 
ATOM   3852 C CG2   . VAL A 1 509 ? -13.17734 2.90310   38.22245  1.000 58.24871 ? 503  VAL A CG2   1 
ATOM   3853 N N     . TYR A 1 510 ? -10.41139 1.74296   34.45718  1.000 53.50556 ? 504  TYR A N     1 
ATOM   3854 C CA    . TYR A 1 510 ? -9.20451  1.38909   33.70666  1.000 49.95152 ? 504  TYR A CA    1 
ATOM   3855 C C     . TYR A 1 510 ? -8.09309  2.43073   33.83731  1.000 45.00917 ? 504  TYR A C     1 
ATOM   3856 O O     . TYR A 1 510 ? -6.91418  2.08301   33.71827  1.000 45.93983 ? 504  TYR A O     1 
ATOM   3857 C CB    . TYR A 1 510 ? -9.54068  1.17079   32.22717  1.000 54.75253 ? 504  TYR A CB    1 
ATOM   3858 C CG    . TYR A 1 510 ? -10.04015 -0.22247  31.87083  1.000 64.31712 ? 504  TYR A CG    1 
ATOM   3859 C CD1   . TYR A 1 510 ? -11.35123 -0.60735  32.14004  1.000 70.41030 ? 504  TYR A CD1   1 
ATOM   3860 C CD2   . TYR A 1 510 ? -9.20352  -1.14664  31.25394  1.000 64.68023 ? 504  TYR A CD2   1 
ATOM   3861 C CE1   . TYR A 1 510 ? -11.81414 -1.87627  31.80591  1.000 70.98399 ? 504  TYR A CE1   1 
ATOM   3862 C CE2   . TYR A 1 510 ? -9.65893  -2.41698  30.91378  1.000 66.07432 ? 504  TYR A CE2   1 
ATOM   3863 C CZ    . TYR A 1 510 ? -10.96613 -2.77496  31.19253  1.000 67.57369 ? 504  TYR A CZ    1 
ATOM   3864 O OH    . TYR A 1 510 ? -11.42431 -4.03502  30.86463  1.000 73.86780 ? 504  TYR A OH    1 
ATOM   3865 N N     . LEU A 1 511 ? -8.42144  3.70152   34.05629  1.000 43.04773 ? 505  LEU A N     1 
ATOM   3866 C CA    . LEU A 1 511 ? -7.39921  4.74227   34.13051  1.000 38.90761 ? 505  LEU A CA    1 
ATOM   3867 C C     . LEU A 1 511 ? -7.56187  5.58073   35.38738  1.000 39.45012 ? 505  LEU A C     1 
ATOM   3868 O O     . LEU A 1 511 ? -8.66793  5.75389   35.89968  1.000 44.19219 ? 505  LEU A O     1 
ATOM   3869 C CB    . LEU A 1 511 ? -7.44583  5.68491   32.92236  1.000 42.41537 ? 505  LEU A CB    1 
ATOM   3870 C CG    . LEU A 1 511 ? -6.62018  5.40815   31.66466  1.000 42.48232 ? 505  LEU A CG    1 
ATOM   3871 C CD1   . LEU A 1 511 ? -6.60995  3.95668   31.31121  1.000 51.41597 ? 505  LEU A CD1   1 
ATOM   3872 C CD2   . LEU A 1 511 ? -7.18458  6.21725   30.51146  1.000 49.02752 ? 505  LEU A CD2   1 
ATOM   3873 N N     . TYR A 1 512 ? -6.43863  6.11490   35.86174  1.000 33.51830 ? 506  TYR A N     1 
ATOM   3874 C CA    . TYR A 1 512 ? -6.39559  7.18192   36.85629  1.000 39.85348 ? 506  TYR A CA    1 
ATOM   3875 C C     . TYR A 1 512 ? -6.27884  8.52057   36.12714  1.000 43.49505 ? 506  TYR A C     1 
ATOM   3876 O O     . TYR A 1 512 ? -5.32995  8.72865   35.36149  1.000 35.47687 ? 506  TYR A O     1 
ATOM   3877 C CB    . TYR A 1 512 ? -5.21077  6.96357   37.79595  1.000 35.09683 ? 506  TYR A CB    1 
ATOM   3878 C CG    . TYR A 1 512 ? -4.89491  8.12586   38.70986  1.000 38.55576 ? 506  TYR A CG    1 
ATOM   3879 C CD1   . TYR A 1 512 ? -5.56968  8.29602   39.90636  1.000 31.27073 ? 506  TYR A CD1   1 
ATOM   3880 C CD2   . TYR A 1 512 ? -3.91406  9.04900   38.37208  1.000 33.44622 ? 506  TYR A CD2   1 
ATOM   3881 C CE1   . TYR A 1 512 ? -5.28795  9.35755   40.73446  1.000 38.56931 ? 506  TYR A CE1   1 
ATOM   3882 C CE2   . TYR A 1 512 ? -3.63076  10.11708  39.18661  1.000 37.36609 ? 506  TYR A CE2   1 
ATOM   3883 C CZ    . TYR A 1 512 ? -4.31485  10.27009  40.37415  1.000 41.23627 ? 506  TYR A CZ    1 
ATOM   3884 O OH    . TYR A 1 512 ? -4.03676  11.33900  41.19874  1.000 37.69693 ? 506  TYR A OH    1 
ATOM   3885 N N     . MET A 1 513 ? -7.21950  9.43502   36.37935  1.000 36.79004 ? 507  MET A N     1 
ATOM   3886 C CA    . MET A 1 513 ? -7.32686  10.66374  35.59647  1.000 39.75241 ? 507  MET A CA    1 
ATOM   3887 C C     . MET A 1 513 ? -6.86694  11.91374  36.33972  1.000 40.30774 ? 507  MET A C     1 
ATOM   3888 O O     . MET A 1 513 ? -7.21543  13.02765  35.92331  1.000 34.10690 ? 507  MET A O     1 
ATOM   3889 C CB    . MET A 1 513 ? -8.76392  10.87030  35.12090  1.000 42.39169 ? 507  MET A CB    1 
ATOM   3890 C CG    . MET A 1 513 ? -9.45185  9.61506   34.68609  1.000 45.99368 ? 507  MET A CG    1 
ATOM   3891 S SD    . MET A 1 513 ? -10.32103 9.84560   33.15517  1.000 71.05358 ? 507  MET A SD    1 
ATOM   3892 C CE    . MET A 1 513 ? -8.93365  9.56482   32.06753  1.000 53.38533 ? 507  MET A CE    1 
ATOM   3893 N N     . GLY A 1 514 ? -6.10773  11.76253  37.42480  1.000 36.14055 ? 508  GLY A N     1 
ATOM   3894 C CA    . GLY A 1 514 ? -5.64830  12.92157  38.17904  1.000 36.30262 ? 508  GLY A CA    1 
ATOM   3895 C C     . GLY A 1 514 ? -4.42110  13.60187  37.62477  1.000 33.50990 ? 508  GLY A C     1 
ATOM   3896 O O     . GLY A 1 514 ? -4.04070  14.66878  38.11611  1.000 34.80713 ? 508  GLY A O     1 
ATOM   3897 N N     . GLY A 1 515 ? -3.79012  13.01776  36.61330  1.000 37.70675 ? 509  GLY A N     1 
ATOM   3898 C CA    . GLY A 1 515 ? -2.61469  13.61632  36.01438  1.000 33.50364 ? 509  GLY A CA    1 
ATOM   3899 C C     . GLY A 1 515 ? -1.31635  13.01617  36.54191  1.000 34.73220 ? 509  GLY A C     1 
ATOM   3900 O O     . GLY A 1 515 ? -1.25370  12.42960  37.61998  1.000 33.96051 ? 509  GLY A O     1 
ATOM   3901 N N     . LEU A 1 516 ? -0.25272  13.22199  35.75983  1.000 28.87588 ? 510  LEU A N     1 
ATOM   3902 C CA    . LEU A 1 516 ? 1.08103   12.72695  36.08546  1.000 34.92401 ? 510  LEU A CA    1 
ATOM   3903 C C     . LEU A 1 516 ? 1.60348   13.29742  37.40455  1.000 32.36114 ? 510  LEU A C     1 
ATOM   3904 O O     . LEU A 1 516 ? 2.17930   12.56911  38.22962  1.000 32.51553 ? 510  LEU A O     1 
ATOM   3905 C CB    . LEU A 1 516 ? 2.02334   13.09269  34.93622  1.000 30.68418 ? 510  LEU A CB    1 
ATOM   3906 C CG    . LEU A 1 516 ? 3.47073   12.63090  35.07545  1.000 27.66718 ? 510  LEU A CG    1 
ATOM   3907 C CD1   . LEU A 1 516 ? 3.52575   11.12533  35.28618  1.000 28.24137 ? 510  LEU A CD1   1 
ATOM   3908 C CD2   . LEU A 1 516 ? 4.27444   13.08091  33.86797  1.000 29.43993 ? 510  LEU A CD2   1 
ATOM   3909 N N     . LYS A 1 517 ? 1.41638   14.59576  37.62002  1.000 30.70805 ? 511  LYS A N     1 
ATOM   3910 C CA    . LYS A 1 517 ? 1.91642   15.21140  38.84894  1.000 32.35411 ? 511  LYS A CA    1 
ATOM   3911 C C     . LYS A 1 517 ? 1.22108   14.62107  40.06858  1.000 29.41276 ? 511  LYS A C     1 
ATOM   3912 O O     . LYS A 1 517 ? 1.87427   14.20439  41.03285  1.000 35.00504 ? 511  LYS A O     1 
ATOM   3913 C CB    . LYS A 1 517 ? 1.74123   16.72971  38.79884  1.000 36.05765 ? 511  LYS A CB    1 
ATOM   3914 C CG    . LYS A 1 517 ? 2.34352   17.46304  40.01948  1.000 36.60811 ? 511  LYS A CG    1 
ATOM   3915 C CD    . LYS A 1 517 ? 1.99380   18.95028  40.01576  1.000 41.92713 ? 511  LYS A CD    1 
ATOM   3916 C CE    . LYS A 1 517 ? 2.62191   19.66249  41.21450  1.000 49.29725 ? 511  LYS A CE    1 
ATOM   3917 N NZ    . LYS A 1 517 ? 2.30581   21.12634  41.21297  1.000 50.97698 ? 511  LYS A NZ    1 
ATOM   3918 N N     . GLU A 1 518 ? -0.10389  14.54755  40.03615  1.000 35.82988 ? 512  GLU A N     1 
ATOM   3919 C CA    . GLU A 1 518 ? -0.80053  13.98805  41.18521  1.000 37.00954 ? 512  GLU A CA    1 
ATOM   3920 C C     . GLU A 1 518 ? -0.55664  12.49056  41.32070  1.000 38.11285 ? 512  GLU A C     1 
ATOM   3921 O O     . GLU A 1 518 ? -0.46614  11.98809  42.44666  1.000 41.31889 ? 512  GLU A O     1 
ATOM   3922 C CB    . GLU A 1 518 ? -2.28210  14.32130  41.09456  1.000 42.41520 ? 512  GLU A CB    1 
ATOM   3923 C CG    . GLU A 1 518 ? -2.55675  15.81261  41.19848  1.000 43.69313 ? 512  GLU A CG    1 
ATOM   3924 C CD    . GLU A 1 518 ? -1.85294  16.46445  42.39497  1.000 58.89716 ? 512  GLU A CD    1 
ATOM   3925 O OE1   . GLU A 1 518 ? -1.28534  17.57364  42.21612  1.000 60.42587 ? 512  GLU A OE1   1 
ATOM   3926 O OE2   . GLU A 1 518 ? -1.87649  15.86849  43.50769  1.000 48.20695 ? 512  GLU A OE2   1 
ATOM   3927 N N     . TYR A 1 519 ? -0.40543  11.76282  40.20471  1.000 33.59077 ? 513  TYR A N     1 
ATOM   3928 C CA    . TYR A 1 519 ? 0.00494   10.35854  40.30352  1.000 35.37208 ? 513  TYR A CA    1 
ATOM   3929 C C     . TYR A 1 519 ? 1.32550   10.21694  41.04927  1.000 31.82069 ? 513  TYR A C     1 
ATOM   3930 O O     . TYR A 1 519 ? 1.46852   9.36259   41.92893  1.000 35.55962 ? 513  TYR A O     1 
ATOM   3931 C CB    . TYR A 1 519 ? 0.14558   9.73554   38.91448  1.000 32.52071 ? 513  TYR A CB    1 
ATOM   3932 C CG    . TYR A 1 519 ? 0.54923   8.26628   38.89967  1.000 30.03161 ? 513  TYR A CG    1 
ATOM   3933 C CD1   . TYR A 1 519 ? -0.33060  7.27985   39.35079  1.000 30.96256 ? 513  TYR A CD1   1 
ATOM   3934 C CD2   . TYR A 1 519 ? 1.78251   7.86355   38.41587  1.000 28.79890 ? 513  TYR A CD2   1 
ATOM   3935 C CE1   . TYR A 1 519 ? 0.01513   5.92864   39.30752  1.000 29.64187 ? 513  TYR A CE1   1 
ATOM   3936 C CE2   . TYR A 1 519 ? 2.13428   6.51844   38.37136  1.000 28.52920 ? 513  TYR A CE2   1 
ATOM   3937 C CZ    . TYR A 1 519 ? 1.24006   5.55946   38.81035  1.000 27.51298 ? 513  TYR A CZ    1 
ATOM   3938 O OH    . TYR A 1 519 ? 1.57448   4.21496   38.77923  1.000 28.67353 ? 513  TYR A OH    1 
ATOM   3939 N N     . ARG A 1 520 ? 2.31540   11.02958  40.69395  1.000 28.99821 ? 514  ARG A N     1 
ATOM   3940 C CA    . ARG A 1 520 ? 3.60287   10.93078  41.36112  1.000 31.62893 ? 514  ARG A CA    1 
ATOM   3941 C C     . ARG A 1 520 ? 3.48607   11.29537  42.83811  1.000 37.94221 ? 514  ARG A C     1 
ATOM   3942 O O     . ARG A 1 520 ? 4.17079   10.69999  43.68008  1.000 32.59163 ? 514  ARG A O     1 
ATOM   3943 C CB    . ARG A 1 520 ? 4.62406   11.81325  40.64150  1.000 34.09369 ? 514  ARG A CB    1 
ATOM   3944 C CG    . ARG A 1 520 ? 4.97275   11.25819  39.26207  1.000 31.02191 ? 514  ARG A CG    1 
ATOM   3945 C CD    . ARG A 1 520 ? 5.68562   12.23591  38.36070  1.000 32.89740 ? 514  ARG A CD    1 
ATOM   3946 N NE    . ARG A 1 520 ? 6.88754   12.78015  38.99587  1.000 35.79391 ? 514  ARG A NE    1 
ATOM   3947 C CZ    . ARG A 1 520 ? 8.06508   12.16858  39.02637  1.000 40.01260 ? 514  ARG A CZ    1 
ATOM   3948 N NH1   . ARG A 1 520 ? 8.23622   10.96192  38.49527  1.000 34.79478 ? 514  ARG A NH1   1 
ATOM   3949 N NH2   . ARG A 1 520 ? 9.09683   12.77848  39.60489  1.000 42.08321 ? 514  ARG A NH2   1 
ATOM   3950 N N     . ASN A 1 521 ? 2.61589   12.25746  43.16700  1.000 37.41135 ? 515  ASN A N     1 
ATOM   3951 C CA    . ASN A 1 521 ? 2.31711   12.55067  44.56765  1.000 37.32190 ? 515  ASN A CA    1 
ATOM   3952 C C     . ASN A 1 521 ? 1.73855   11.34187  45.26784  1.000 34.09012 ? 515  ASN A C     1 
ATOM   3953 O O     . ASN A 1 521 ? 2.16170   10.99488  46.37462  1.000 45.98694 ? 515  ASN A O     1 
ATOM   3954 C CB    . ASN A 1 521 ? 1.33644   13.71536  44.66355  1.000 40.17424 ? 515  ASN A CB    1 
ATOM   3955 C CG    . ASN A 1 521 ? 2.01328   15.03326  44.53593  1.000 48.81416 ? 515  ASN A CG    1 
ATOM   3956 O OD1   . ASN A 1 521 ? 3.11087   15.22579  45.06409  1.000 51.33097 ? 515  ASN A OD1   1 
ATOM   3957 N ND2   . ASN A 1 521 ? 1.36730   15.96845  43.84459  1.000 48.42569 ? 515  ASN A ND2   1 
ATOM   3958 N N     . GLN A 1 522 ? 0.73973   10.71135  44.64340  1.000 36.59669 ? 516  GLN A N     1 
ATOM   3959 C CA    . GLN A 1 522 ? 0.08370   9.54249   45.21410  1.000 43.35714 ? 516  GLN A CA    1 
ATOM   3960 C C     . GLN A 1 522 ? 1.08963   8.44815   45.54231  1.000 43.95358 ? 516  GLN A C     1 
ATOM   3961 O O     . GLN A 1 522 ? 1.09499   7.91394   46.65756  1.000 45.58431 ? 516  GLN A O     1 
ATOM   3962 C CB    . GLN A 1 522 ? -0.97499  9.01252   44.24522  1.000 40.86724 ? 516  GLN A CB    1 
ATOM   3963 C CG    . GLN A 1 522 ? -2.21275  9.88766   44.13479  1.000 45.07349 ? 516  GLN A CG    1 
ATOM   3964 C CD    . GLN A 1 522 ? -2.90056  10.10758  45.46684  1.000 57.22002 ? 516  GLN A CD    1 
ATOM   3965 O OE1   . GLN A 1 522 ? -3.70368  9.27572   45.90063  1.000 58.22620 ? 516  GLN A OE1   1 
ATOM   3966 N NE2   . GLN A 1 522 ? -2.59819  11.23482  46.12312  1.000 56.54540 ? 516  GLN A NE2   1 
ATOM   3967 N N     . ILE A 1 523 ? 1.96567   8.10213   44.59057  1.000 35.51342 ? 517  ILE A N     1 
ATOM   3968 C CA    . ILE A 1 523 ? 2.84798   6.96832   44.84992  1.000 32.58904 ? 517  ILE A CA    1 
ATOM   3969 C C     . ILE A 1 523 ? 3.99046   7.36831   45.77557  1.000 37.75622 ? 517  ILE A C     1 
ATOM   3970 O O     . ILE A 1 523 ? 4.56955   6.50623   46.44357  1.000 37.38364 ? 517  ILE A O     1 
ATOM   3971 C CB    . ILE A 1 523 ? 3.38318   6.35317   43.53799  1.000 31.19379 ? 517  ILE A CB    1 
ATOM   3972 C CG1   . ILE A 1 523 ? 4.30012   7.33424   42.79074  1.000 35.09124 ? 517  ILE A CG1   1 
ATOM   3973 C CG2   . ILE A 1 523 ? 2.21018   5.84807   42.65498  1.000 26.33837 ? 517  ILE A CG2   1 
ATOM   3974 C CD1   . ILE A 1 523 ? 5.06108   6.68268   41.57971  1.000 30.49947 ? 517  ILE A CD1   1 
ATOM   3975 N N     . SER A 1 524 ? 4.32025   8.66305   45.84058  1.000 37.32368 ? 518  SER A N     1 
ATOM   3976 C CA    . SER A 1 524 ? 5.37946   9.12088   46.73801  1.000 38.28749 ? 518  SER A CA    1 
ATOM   3977 C C     . SER A 1 524 ? 4.93881   9.03378   48.19277  1.000 41.22971 ? 518  SER A C     1 
ATOM   3978 O O     . SER A 1 524 ? 5.73692   8.67878   49.07197  1.000 43.10286 ? 518  SER A O     1 
ATOM   3979 C CB    . SER A 1 524 ? 5.77284   10.55238  46.39056  1.000 43.86805 ? 518  SER A CB    1 
ATOM   3980 O OG    . SER A 1 524 ? 6.61433   10.57699  45.25591  1.000 49.26095 ? 518  SER A OG    1 
ATOM   3981 N N     . GLU A 1 525 ? 3.67099   9.35528   48.46019  1.000 44.37043 ? 519  GLU A N     1 
ATOM   3982 C CA    . GLU A 1 525 ? 3.12095   9.17389   49.79864  1.000 45.87709 ? 519  GLU A CA    1 
ATOM   3983 C C     . GLU A 1 525 ? 3.18806   7.71763   50.22585  1.000 48.34167 ? 519  GLU A C     1 
ATOM   3984 O O     . GLU A 1 525 ? 3.44843   7.42324   51.39978  1.000 46.08626 ? 519  GLU A O     1 
ATOM   3985 C CB    . GLU A 1 525 ? 1.68032   9.67484   49.86069  1.000 40.28964 ? 519  GLU A CB    1 
ATOM   3986 C CG    . GLU A 1 525 ? 1.57788   11.19733  50.00079  1.000 54.67703 ? 519  GLU A CG    1 
ATOM   3987 C CD    . GLU A 1 525 ? 0.21380   11.76274  49.60640  1.000 71.19617 ? 519  GLU A CD    1 
ATOM   3988 O OE1   . GLU A 1 525 ? -0.79807  11.02259  49.68936  1.000 73.65403 ? 519  GLU A OE1   1 
ATOM   3989 O OE2   . GLU A 1 525 ? 0.16142   12.95330  49.20829  1.000 70.54591 ? 519  GLU A OE2   1 
ATOM   3990 N N     . VAL A 1 526 ? 2.95207   6.79239   49.28699  1.000 42.70655 ? 520  VAL A N     1 
ATOM   3991 C CA    . VAL A 1 526 ? 2.99780   5.37104   49.61261  1.000 41.49694 ? 520  VAL A CA    1 
ATOM   3992 C C     . VAL A 1 526 ? 4.41696   4.96141   49.97232  1.000 44.78590 ? 520  VAL A C     1 
ATOM   3993 O O     . VAL A 1 526 ? 4.65095   4.31147   50.99770  1.000 47.34170 ? 520  VAL A O     1 
ATOM   3994 C CB    . VAL A 1 526 ? 2.44138   4.52413   48.45268  1.000 40.89944 ? 520  VAL A CB    1 
ATOM   3995 C CG1   . VAL A 1 526 ? 2.78849   3.05091   48.66319  1.000 40.55081 ? 520  VAL A CG1   1 
ATOM   3996 C CG2   . VAL A 1 526 ? 0.93020   4.71117   48.32584  1.000 41.84535 ? 520  VAL A CG2   1 
ATOM   3997 N N     . SER A 1 527 ? 5.39733   5.36428   49.16207  1.000 40.78646 ? 521  SER A N     1 
ATOM   3998 C CA    . SER A 1 527 ? 6.77008   4.98600   49.48262  1.000 37.89323 ? 521  SER A CA    1 
ATOM   3999 C C     . SER A 1 527 ? 7.28823   5.73588   50.71120  1.000 44.70592 ? 521  SER A C     1 
ATOM   4000 O O     . SER A 1 527 ? 8.09121   5.19174   51.47415  1.000 40.86954 ? 521  SER A O     1 
ATOM   4001 C CB    . SER A 1 527 ? 7.68819   5.21678   48.28267  1.000 40.55788 ? 521  SER A CB    1 
ATOM   4002 O OG    . SER A 1 527 ? 7.57474   6.54467   47.79153  1.000 41.49973 ? 521  SER A OG    1 
ATOM   4003 N N     . ASN A 1 528 ? 6.83829   6.96833   50.93976  1.000 46.37805 ? 522  ASN A N     1 
ATOM   4004 C CA    . ASN A 1 528 ? 7.33617   7.68664   52.11078  1.000 50.06290 ? 522  ASN A CA    1 
ATOM   4005 C C     . ASN A 1 528 ? 6.75444   7.15863   53.41708  1.000 53.20116 ? 522  ASN A C     1 
ATOM   4006 O O     . ASN A 1 528 ? 7.38643   7.31990   54.46641  1.000 53.33925 ? 522  ASN A O     1 
ATOM   4007 C CB    . ASN A 1 528 ? 7.06502   9.17855   51.97662  1.000 45.46544 ? 522  ASN A CB    1 
ATOM   4008 C CG    . ASN A 1 528 ? 8.00594   9.83779   50.99855  1.000 47.76663 ? 522  ASN A CG    1 
ATOM   4009 O OD1   . ASN A 1 528 ? 9.21664   9.60964   51.03843  1.000 53.00015 ? 522  ASN A OD1   1 
ATOM   4010 N ND2   . ASN A 1 528 ? 7.46455   10.68217  50.13160  1.000 52.90333 ? 522  ASN A ND2   1 
ATOM   4011 N N     . ASN A 1 529 ? 5.59136   6.51849   53.37318  1.000 50.98599 ? 523  ASN A N     1 
ATOM   4012 C CA    . ASN A 1 529 ? 4.94483   5.94346   54.55357  1.000 53.09139 ? 523  ASN A CA    1 
ATOM   4013 C C     . ASN A 1 529 ? 5.15700   4.43550   54.64029  1.000 46.97739 ? 523  ASN A C     1 
ATOM   4014 O O     . ASN A 1 529 ? 4.21184   3.68872   54.86362  1.000 47.29920 ? 523  ASN A O     1 
ATOM   4015 C CB    . ASN A 1 529 ? 3.45886   6.28667   54.55270  1.000 52.35963 ? 523  ASN A CB    1 
ATOM   4016 C CG    . ASN A 1 529 ? 3.20520   7.77206   54.73054  1.000 60.54287 ? 523  ASN A CG    1 
ATOM   4017 O OD1   . ASN A 1 529 ? 2.74084   8.46445   53.81676  1.000 59.92110 ? 523  ASN A OD1   1 
ATOM   4018 N ND2   . ASN A 1 529 ? 3.50592   8.27375   55.92417  1.000 69.82622 ? 523  ASN A ND2   1 
ATOM   4019 N N     . ASN A 1 530 ? 6.40706   3.98788   54.47637  1.000 49.68438 ? 524  ASN A N     1 
ATOM   4020 C CA    . ASN A 1 530 ? 6.79078   2.57577   54.60338  1.000 51.54634 ? 524  ASN A CA    1 
ATOM   4021 C C     . ASN A 1 530 ? 5.89053   1.66474   53.77378  1.000 51.68420 ? 524  ASN A C     1 
ATOM   4022 O O     . ASN A 1 530 ? 5.48662   0.58315   54.21001  1.000 50.25626 ? 524  ASN A O     1 
ATOM   4023 C CB    . ASN A 1 530 ? 6.81058   2.12738   56.06893  1.000 58.79170 ? 524  ASN A CB    1 
ATOM   4024 C CG    . ASN A 1 530 ? 7.48722   3.13893   56.98668  1.000 61.21647 ? 524  ASN A CG    1 
ATOM   4025 O OD1   . ASN A 1 530 ? 8.71360   3.19113   57.06438  1.000 69.13071 ? 524  ASN A OD1   1 
ATOM   4026 N ND2   . ASN A 1 530 ? 6.68807   3.92838   57.70331  1.000 60.11024 ? 524  ASN A ND2   1 
ATOM   4027 N N     . TYR A 1 531 ? 5.57437   2.11316   52.55816  1.000 47.59181 ? 525  TYR A N     1 
ATOM   4028 C CA    . TYR A 1 531 ? 4.82396   1.31967   51.58429  1.000 47.35781 ? 525  TYR A CA    1 
ATOM   4029 C C     . TYR A 1 531 ? 3.48519   0.85433   52.15259  1.000 46.23738 ? 525  TYR A C     1 
ATOM   4030 O O     . TYR A 1 531 ? 3.13483   -0.32609  52.09889  1.000 47.30048 ? 525  TYR A O     1 
ATOM   4031 C CB    . TYR A 1 531 ? 5.67112   0.15247   51.07155  1.000 41.59621 ? 525  TYR A CB    1 
ATOM   4032 C CG    . TYR A 1 531 ? 6.86682   0.64519   50.28615  1.000 42.42990 ? 525  TYR A CG    1 
ATOM   4033 C CD1   . TYR A 1 531 ? 6.69665   1.19227   49.00862  1.000 37.00530 ? 525  TYR A CD1   1 
ATOM   4034 C CD2   . TYR A 1 531 ? 8.15358   0.62467   50.82816  1.000 38.74040 ? 525  TYR A CD2   1 
ATOM   4035 C CE1   . TYR A 1 531 ? 7.77246   1.66540   48.28440  1.000 33.41634 ? 525  TYR A CE1   1 
ATOM   4036 C CE2   . TYR A 1 531 ? 9.24006   1.10729   50.10669  1.000 38.27957 ? 525  TYR A CE2   1 
ATOM   4037 C CZ    . TYR A 1 531 ? 9.02687   1.62763   48.82651  1.000 35.51573 ? 525  TYR A CZ    1 
ATOM   4038 O OH    . TYR A 1 531 ? 10.07032  2.10017   48.09049  1.000 35.45989 ? 525  TYR A OH    1 
ATOM   4039 N N     . LYS A 1 532 ? 2.74024   1.81358   52.70945  1.000 50.31051 ? 526  LYS A N     1 
ATOM   4040 C CA    . LYS A 1 532 ? 1.37242   1.56974   53.15520  1.000 51.11969 ? 526  LYS A CA    1 
ATOM   4041 C C     . LYS A 1 532 ? 0.58648   0.81973   52.08829  1.000 51.26537 ? 526  LYS A C     1 
ATOM   4042 O O     . LYS A 1 532 ? 0.67920   1.12366   50.89590  1.000 46.60205 ? 526  LYS A O     1 
ATOM   4043 C CB    . LYS A 1 532 ? 0.68001   2.90066   53.46958  1.000 56.49325 ? 526  LYS A CB    1 
ATOM   4044 C CG    . LYS A 1 532 ? -0.67505  2.76052   54.15745  1.000 67.34665 ? 526  LYS A CG    1 
ATOM   4045 C CD    . LYS A 1 532 ? -1.07854  4.04281   54.89605  1.000 75.15368 ? 526  LYS A CD    1 
ATOM   4046 C CE    . LYS A 1 532 ? -1.18313  3.83589   56.41189  1.000 72.54091 ? 526  LYS A CE    1 
ATOM   4047 N NZ    . LYS A 1 532 ? 0.13928   3.92813   57.11684  1.000 66.07681 ? 526  LYS A NZ    1 
ATOM   4048 N N     . GLY A 1 533 ? -0.19055  -0.16650  52.52106  1.000 49.08718 ? 527  GLY A N     1 
ATOM   4049 C CA    . GLY A 1 533 ? -0.96879  -0.96294  51.59871  1.000 46.33125 ? 527  GLY A CA    1 
ATOM   4050 C C     . GLY A 1 533 ? -0.25671  -2.17665  51.04069  1.000 48.49552 ? 527  GLY A C     1 
ATOM   4051 O O     . GLY A 1 533 ? -0.88966  -2.97426  50.33594  1.000 47.82122 ? 527  GLY A O     1 
ATOM   4052 N N     . CYS A 1 534 ? 1.02768   -2.35241  51.33988  1.000 49.84511 ? 528  CYS A N     1 
ATOM   4053 C CA    . CYS A 1 534 ? 1.80684   -3.49382  50.87164  1.000 48.47754 ? 528  CYS A CA    1 
ATOM   4054 C C     . CYS A 1 534 ? 2.13677   -4.41333  52.04042  1.000 53.32099 ? 528  CYS A C     1 
ATOM   4055 O O     . CYS A 1 534 ? 2.67519   -3.96124  53.05843  1.000 51.56353 ? 528  CYS A O     1 
ATOM   4056 C CB    . CYS A 1 534 ? 3.10237   -3.03336  50.20099  1.000 50.42241 ? 528  CYS A CB    1 
ATOM   4057 S SG    . CYS A 1 534 ? 2.88717   -1.77821  48.90573  1.000 47.47111 ? 528  CYS A SG    1 
ATOM   4058 N N     . LEU A 1 535 ? 1.82474   -5.69998  51.88652  1.000 53.50413 ? 529  LEU A N     1 
ATOM   4059 C CA    . LEU A 1 535 ? 2.25475   -6.71282  52.84398  1.000 52.34756 ? 529  LEU A CA    1 
ATOM   4060 C C     . LEU A 1 535 ? 3.71131   -7.05664  52.57290  1.000 50.90664 ? 529  LEU A C     1 
ATOM   4061 O O     . LEU A 1 535 ? 4.06089   -7.47479  51.46408  1.000 49.90580 ? 529  LEU A O     1 
ATOM   4062 C CB    . LEU A 1 535 ? 1.38346   -7.96219  52.74299  1.000 50.00442 ? 529  LEU A CB    1 
ATOM   4063 C CG    . LEU A 1 535 ? -0.06488  -7.87543  53.23530  1.000 58.09900 ? 529  LEU A CG    1 
ATOM   4064 C CD1   . LEU A 1 535 ? -0.93159  -8.97066  52.59763  1.000 59.01553 ? 529  LEU A CD1   1 
ATOM   4065 C CD2   . LEU A 1 535 ? -0.12565  -7.95311  54.75001  1.000 61.91423 ? 529  LEU A CD2   1 
ATOM   4066 N N     . LEU A 1 536 ? 4.55941   -6.88098  53.57722  1.000 51.00719 ? 530  LEU A N     1 
ATOM   4067 C CA    . LEU A 1 536 ? 5.97838   -7.17491  53.46815  1.000 46.93830 ? 530  LEU A CA    1 
ATOM   4068 C C     . LEU A 1 536 ? 6.29647   -8.37438  54.34789  1.000 58.88098 ? 530  LEU A C     1 
ATOM   4069 O O     . LEU A 1 536 ? 5.94042   -8.39210  55.52951  1.000 64.86196 ? 530  LEU A O     1 
ATOM   4070 C CB    . LEU A 1 536 ? 6.81379   -5.96730  53.88681  1.000 44.39463 ? 530  LEU A CB    1 
ATOM   4071 C CG    . LEU A 1 536 ? 6.48096   -4.66105  53.16918  1.000 51.31509 ? 530  LEU A CG    1 
ATOM   4072 C CD1   . LEU A 1 536 ? 7.19966   -3.50191  53.81883  1.000 52.72953 ? 530  LEU A CD1   1 
ATOM   4073 C CD2   . LEU A 1 536 ? 6.82576   -4.74276  51.68343  1.000 53.19126 ? 530  LEU A CD2   1 
ATOM   4074 N N     . LYS A 1 537 ? 6.94832   -9.37960  53.77509  1.000 56.94925 ? 531  LYS A N     1 
ATOM   4075 C CA    . LYS A 1 537 ? 7.25293   -10.61507 54.48601  1.000 54.13217 ? 531  LYS A CA    1 
ATOM   4076 C C     . LYS A 1 537 ? 8.75411   -10.68816 54.70602  1.000 55.02712 ? 531  LYS A C     1 
ATOM   4077 O O     . LYS A 1 537 ? 9.53498   -10.54842 53.75807  1.000 51.12886 ? 531  LYS A O     1 
ATOM   4078 C CB    . LYS A 1 537 ? 6.74719   -11.83822 53.71879  1.000 55.17894 ? 531  LYS A CB    1 
ATOM   4079 C CG    . LYS A 1 537 ? 7.23913   -13.18445 54.25040  1.000 61.93705 ? 531  LYS A CG    1 
ATOM   4080 C CD    . LYS A 1 537 ? 6.30763   -14.31632 53.82181  1.000 60.42765 ? 531  LYS A CD    1 
ATOM   4081 C CE    . LYS A 1 537 ? 7.07649   -15.53286 53.33591  1.000 68.78826 ? 531  LYS A CE    1 
ATOM   4082 N NZ    . LYS A 1 537 ? 6.16756   -16.69871 53.07494  1.000 71.09893 ? 531  LYS A NZ    1 
ATOM   4083 N N     . GLN A 1 538 ? 9.15164   -10.88515 55.95398  1.000 56.24245 ? 532  GLN A N     1 
ATOM   4084 C CA    . GLN A 1 538 ? 10.55477  -11.00258 56.30960  1.000 61.00289 ? 532  GLN A CA    1 
ATOM   4085 C C     . GLN A 1 538 ? 11.01482  -12.45257 56.19479  1.000 65.17361 ? 532  GLN A C     1 
ATOM   4086 O O     . GLN A 1 538 ? 10.21225  -13.39212 56.16519  1.000 66.26246 ? 532  GLN A O     1 
ATOM   4087 C CB    . GLN A 1 538 ? 10.78498  -10.49715 57.73708  1.000 65.18208 ? 532  GLN A CB    1 
ATOM   4088 C CG    . GLN A 1 538 ? 10.30713  -9.06610  58.00674  1.000 67.65865 ? 532  GLN A CG    1 
ATOM   4089 C CD    . GLN A 1 538 ? 11.37569  -8.01523  57.75254  1.000 65.62120 ? 532  GLN A CD    1 
ATOM   4090 O OE1   . GLN A 1 538 ? 12.50743  -8.33422  57.39042  1.000 64.68567 ? 532  GLN A OE1   1 
ATOM   4091 N NE2   . GLN A 1 538 ? 11.02035  -6.75443  57.95723  1.000 63.73556 ? 532  GLN A NE2   1 
ATOM   4092 N N     . SER A 1 539 ? 12.32869  -12.62320 56.12814  1.000 71.55110 ? 533  SER A N     1 
ATOM   4093 C CA    . SER A 1 539 ? 12.93704  -13.94024 56.29635  1.000 85.28415 ? 533  SER A CA    1 
ATOM   4094 C C     . SER A 1 539 ? 14.38143  -13.79786 56.76653  1.000 88.18154 ? 533  SER A C     1 
ATOM   4095 O O     . SER A 1 539 ? 15.18538  -13.12771 56.11475  1.000 83.92623 ? 533  SER A O     1 
ATOM   4096 C CB    . SER A 1 539 ? 12.88181  -14.74702 54.99755  1.000 82.46803 ? 533  SER A CB    1 
ATOM   4097 O OG    . SER A 1 539 ? 13.34045  -16.07175 55.21440  1.000 80.50713 ? 533  SER A OG    1 
HETATM 4098 P PA    . FAD B 2 .   ? 4.94619   -2.22390  24.09118  1.000 24.66014 ? 601  FAD A PA    1 
HETATM 4099 O O1A   . FAD B 2 .   ? 5.74642   -1.31225  23.26451  1.000 24.01671 ? 601  FAD A O1A   1 
HETATM 4100 O O2A   . FAD B 2 .   ? 3.56841   -2.67195  23.63962  1.000 25.51793 ? 601  FAD A O2A   1 
HETATM 4101 O O5B   . FAD B 2 .   ? 5.82572   -3.47292  24.39437  1.000 22.91955 ? 601  FAD A O5B   1 
HETATM 4102 C C5B   . FAD B 2 .   ? 5.24371   -4.65408  24.97488  1.000 26.95354 ? 601  FAD A C5B   1 
HETATM 4103 C C4B   . FAD B 2 .   ? 6.08585   -5.83505  24.56722  1.000 26.24839 ? 601  FAD A C4B   1 
HETATM 4104 O O4B   . FAD B 2 .   ? 5.72207   -6.96283  25.39940  1.000 29.42196 ? 601  FAD A O4B   1 
HETATM 4105 C C3B   . FAD B 2 .   ? 5.84678   -6.25935  23.10755  1.000 27.33179 ? 601  FAD A C3B   1 
HETATM 4106 O O3B   . FAD B 2 .   ? 7.03532   -6.23881  22.32418  1.000 26.20905 ? 601  FAD A O3B   1 
HETATM 4107 C C2B   . FAD B 2 .   ? 5.29426   -7.69021  23.22922  1.000 30.71672 ? 601  FAD A C2B   1 
HETATM 4108 O O2B   . FAD B 2 .   ? 5.79113   -8.54521  22.20608  1.000 28.08914 ? 601  FAD A O2B   1 
HETATM 4109 C C1B   . FAD B 2 .   ? 5.82672   -8.11504  24.59913  1.000 32.97453 ? 601  FAD A C1B   1 
HETATM 4110 N N9A   . FAD B 2 .   ? 5.08377   -9.23236  25.19827  1.000 27.54874 ? 601  FAD A N9A   1 
HETATM 4111 C C8A   . FAD B 2 .   ? 3.76535   -9.28107  25.57245  1.000 30.76482 ? 601  FAD A C8A   1 
HETATM 4112 N N7A   . FAD B 2 .   ? 3.38555   -10.44967 26.04078  1.000 29.74370 ? 601  FAD A N7A   1 
HETATM 4113 C C5A   . FAD B 2 .   ? 4.53008   -11.23025 25.94582  1.000 28.48648 ? 601  FAD A C5A   1 
HETATM 4114 C C6A   . FAD B 2 .   ? 4.80170   -12.57568 26.28527  1.000 28.70693 ? 601  FAD A C6A   1 
HETATM 4115 N N6A   . FAD B 2 .   ? 3.89286   -13.41588 26.79194  1.000 29.46139 ? 601  FAD A N6A   1 
HETATM 4116 N N1A   . FAD B 2 .   ? 6.05087   -13.03905 26.05842  1.000 27.02014 ? 601  FAD A N1A   1 
HETATM 4117 C C2A   . FAD B 2 .   ? 6.96377   -12.20953 25.54174  1.000 30.29955 ? 601  FAD A C2A   1 
HETATM 4118 N N3A   . FAD B 2 .   ? 6.82666   -10.92374 25.19631  1.000 25.02737 ? 601  FAD A N3A   1 
HETATM 4119 C C4A   . FAD B 2 .   ? 5.58152   -10.49156 25.42745  1.000 24.93679 ? 601  FAD A C4A   1 
HETATM 4120 N N1    . FAD B 2 .   ? 1.74407   6.71841   23.74945  1.000 38.94401 ? 601  FAD A N1    1 
HETATM 4121 C C2    . FAD B 2 .   ? 2.00188   7.95579   24.28158  1.000 38.52714 ? 601  FAD A C2    1 
HETATM 4122 O O2    . FAD B 2 .   ? 1.97812   8.16683   25.49626  1.000 42.36956 ? 601  FAD A O2    1 
HETATM 4123 N N3    . FAD B 2 .   ? 2.29640   9.01616   23.44544  1.000 32.83693 ? 601  FAD A N3    1 
HETATM 4124 C C4    . FAD B 2 .   ? 2.36318   8.96599   22.06336  1.000 35.81268 ? 601  FAD A C4    1 
HETATM 4125 O O4    . FAD B 2 .   ? 2.66170   9.97145   21.42636  1.000 34.90260 ? 601  FAD A O4    1 
HETATM 4126 C C4X   . FAD B 2 .   ? 2.08248   7.65314   21.50184  1.000 38.80964 ? 601  FAD A C4X   1 
HETATM 4127 N N5    . FAD B 2 .   ? 2.11338   7.51707   20.19280  1.000 37.22584 ? 601  FAD A N5    1 
HETATM 4128 C C5X   . FAD B 2 .   ? 1.83835   6.26008   19.66004  1.000 35.05387 ? 601  FAD A C5X   1 
HETATM 4129 C C6    . FAD B 2 .   ? 1.85948   6.10108   18.27523  1.000 37.29633 ? 601  FAD A C6    1 
HETATM 4130 C C7    . FAD B 2 .   ? 1.61005   4.86242   17.68905  1.000 40.68873 ? 601  FAD A C7    1 
HETATM 4131 C C7M   . FAD B 2 .   ? 1.64593   4.72632   16.18706  1.000 33.42792 ? 601  FAD A C7M   1 
HETATM 4132 C C8    . FAD B 2 .   ? 1.31924   3.75661   18.50400  1.000 40.37242 ? 601  FAD A C8    1 
HETATM 4133 C C8M   . FAD B 2 .   ? 1.05275   2.40316   17.89814  1.000 38.39682 ? 601  FAD A C8M   1 
HETATM 4134 C C9    . FAD B 2 .   ? 1.29774   3.90962   19.88845  1.000 34.35802 ? 601  FAD A C9    1 
HETATM 4135 C C9A   . FAD B 2 .   ? 1.55686   5.14701   20.47367  1.000 35.35997 ? 601  FAD A C9A   1 
HETATM 4136 N N10   . FAD B 2 .   ? 1.54189   5.33871   21.87575  1.000 36.33367 ? 601  FAD A N10   1 
HETATM 4137 C C10   . FAD B 2 .   ? 1.79210   6.58536   22.42316  1.000 38.06318 ? 601  FAD A C10   1 
HETATM 4138 C "C1'" . FAD B 2 .   ? 1.26764   4.21617   22.79389  1.000 33.33632 ? 601  FAD A "C1'" 1 
HETATM 4139 C "C2'" . FAD B 2 .   ? 2.45659   3.25643   22.94252  1.000 33.21644 ? 601  FAD A "C2'" 1 
HETATM 4140 O "O2'" . FAD B 2 .   ? 1.98661   1.93143   23.19833  1.000 32.83754 ? 601  FAD A "O2'" 1 
HETATM 4141 C "C3'" . FAD B 2 .   ? 3.32714   3.67810   24.13021  1.000 28.65502 ? 601  FAD A "C3'" 1 
HETATM 4142 O "O3'" . FAD B 2 .   ? 3.83487   4.99171   23.90104  1.000 30.09331 ? 601  FAD A "O3'" 1 
HETATM 4143 C "C4'" . FAD B 2 .   ? 4.54548   2.79247   24.41524  1.000 26.54500 ? 601  FAD A "C4'" 1 
HETATM 4144 O "O4'" . FAD B 2 .   ? 5.31127   2.61484   23.22388  1.000 27.12322 ? 601  FAD A "O4'" 1 
HETATM 4145 C "C5'" . FAD B 2 .   ? 4.25463   1.44411   25.04805  1.000 25.21859 ? 601  FAD A "C5'" 1 
HETATM 4146 O "O5'" . FAD B 2 .   ? 5.50651   0.79650   25.35187  1.000 24.82284 ? 601  FAD A "O5'" 1 
HETATM 4147 P P     . FAD B 2 .   ? 5.56701   -0.46923  26.31185  1.000 23.93366 ? 601  FAD A P     1 
HETATM 4148 O O1P   . FAD B 2 .   ? 7.00368   -0.92755  26.42956  1.000 21.48452 ? 601  FAD A O1P   1 
HETATM 4149 O O2P   . FAD B 2 .   ? 4.90727   -0.12465  27.56874  1.000 26.07663 ? 601  FAD A O2P   1 
HETATM 4150 O O3P   . FAD B 2 .   ? 4.72146   -1.61346  25.53992  1.000 24.23129 ? 601  FAD A O3P   1 
HETATM 4151 P PA    . NDP C 3 .   ? -9.61515  1.76904   17.65348  1.000 28.02483 ? 602  NDP A PA    1 
HETATM 4152 O O1A   . NDP C 3 .   ? -10.16851 0.62068   18.42619  1.000 29.28840 ? 602  NDP A O1A   1 
HETATM 4153 O O2A   . NDP C 3 .   ? -9.35732  3.08535   18.34393  1.000 30.55476 ? 602  NDP A O2A   1 
HETATM 4154 O O5B   . NDP C 3 .   ? -10.58507 2.07909   16.32947  1.000 27.33165 ? 602  NDP A O5B   1 
HETATM 4155 C C5B   . NDP C 3 .   ? -11.08957 0.85201   15.84693  1.000 22.44312 ? 602  NDP A C5B   1 
HETATM 4156 C C4B   . NDP C 3 .   ? -11.86486 1.28970   14.58069  1.000 23.91678 ? 602  NDP A C4B   1 
HETATM 4157 O O4B   . NDP C 3 .   ? -12.37688 0.18088   13.83114  1.000 24.60862 ? 602  NDP A O4B   1 
HETATM 4158 C C3B   . NDP C 3 .   ? -13.03590 2.20064   15.01778  1.000 23.47735 ? 602  NDP A C3B   1 
HETATM 4159 O O3B   . NDP C 3 .   ? -13.36502 3.04798   13.97383  1.000 22.15921 ? 602  NDP A O3B   1 
HETATM 4160 C C2B   . NDP C 3 .   ? -14.19366 1.17335   15.10834  1.000 25.19776 ? 602  NDP A C2B   1 
HETATM 4161 O O2B   . NDP C 3 .   ? -15.39843 1.68643   14.85930  1.000 25.62359 ? 602  NDP A O2B   1 
HETATM 4162 C C1B   . NDP C 3 .   ? -13.80795 0.28852   13.85123  1.000 23.98526 ? 602  NDP A C1B   1 
HETATM 4163 N N9A   . NDP C 3 .   ? -14.35169 -1.09985  13.94182  1.000 27.37448 ? 602  NDP A N9A   1 
HETATM 4164 C C8A   . NDP C 3 .   ? -14.03284 -2.09158  14.88383  1.000 28.81527 ? 602  NDP A C8A   1 
HETATM 4165 N N7A   . NDP C 3 .   ? -14.68438 -3.24770  14.67836  1.000 29.82094 ? 602  NDP A N7A   1 
HETATM 4166 C C5A   . NDP C 3 .   ? -15.45335 -2.99145  13.54268  1.000 27.68483 ? 602  NDP A C5A   1 
HETATM 4167 C C6A   . NDP C 3 .   ? -16.35999 -3.77484  12.82911  1.000 26.82325 ? 602  NDP A C6A   1 
HETATM 4168 N N6A   . NDP C 3 .   ? -16.61830 -5.07901  13.22079  1.000 30.46938 ? 602  NDP A N6A   1 
HETATM 4169 N N1A   . NDP C 3 .   ? -17.00327 -3.27401  11.72879  1.000 28.99375 ? 602  NDP A N1A   1 
HETATM 4170 C C2A   . NDP C 3 .   ? -16.71910 -2.00506  11.37857  1.000 26.49635 ? 602  NDP A C2A   1 
HETATM 4171 N N3A   . NDP C 3 .   ? -15.86832 -1.12879  11.96944  1.000 26.24242 ? 602  NDP A N3A   1 
HETATM 4172 C C4A   . NDP C 3 .   ? -15.24482 -1.66057  13.06443  1.000 26.43743 ? 602  NDP A C4A   1 
HETATM 4173 O O3    . NDP C 3 .   ? -8.21247  1.04123   17.10156  1.000 27.81626 ? 602  NDP A O3    1 
HETATM 4174 P PN    . NDP C 3 .   ? -7.00341  1.99780   16.62971  1.000 24.95339 ? 602  NDP A PN    1 
HETATM 4175 O O1N   . NDP C 3 .   ? -5.92789  1.09848   16.18584  1.000 25.33584 ? 602  NDP A O1N   1 
HETATM 4176 O O2N   . NDP C 3 .   ? -7.36781  3.23264   15.83034  1.000 24.81025 ? 602  NDP A O2N   1 
HETATM 4177 O O5D   . NDP C 3 .   ? -6.27757  2.68264   18.03864  1.000 30.20079 ? 602  NDP A O5D   1 
HETATM 4178 C C5D   . NDP C 3 .   ? -6.12157  1.61891   18.92041  1.000 38.68215 ? 602  NDP A C5D   1 
HETATM 4179 C C4D   . NDP C 3 .   ? -5.62049  2.16778   20.23380  1.000 45.00418 ? 602  NDP A C4D   1 
HETATM 4180 O O4D   . NDP C 3 .   ? -4.34118  2.75899   20.03490  1.000 45.33097 ? 602  NDP A O4D   1 
HETATM 4181 C C3D   . NDP C 3 .   ? -6.57597  3.34393   20.67523  1.000 48.29659 ? 602  NDP A C3D   1 
HETATM 4182 O O3D   . NDP C 3 .   ? -6.83217  3.19770   22.02270  1.000 58.27489 ? 602  NDP A O3D   1 
HETATM 4183 C C2D   . NDP C 3 .   ? -5.70633  4.56881   20.43933  1.000 53.41767 ? 602  NDP A C2D   1 
HETATM 4184 O O2D   . NDP C 3 .   ? -5.96349  5.60646   21.32307  1.000 58.27106 ? 602  NDP A O2D   1 
HETATM 4185 C C1D   . NDP C 3 .   ? -4.35581  3.94528   20.81021  1.000 54.32392 ? 602  NDP A C1D   1 
HETATM 4186 N N1N   . NDP C 3 .   ? -3.27100  4.81401   20.39289  1.000 55.50258 ? 602  NDP A N1N   1 
HETATM 4187 C C2N   . NDP C 3 .   ? -3.00536  4.95471   19.04749  1.000 47.65152 ? 602  NDP A C2N   1 
HETATM 4188 C C3N   . NDP C 3 .   ? -2.15189  5.92086   18.62149  1.000 52.22588 ? 602  NDP A C3N   1 
HETATM 4189 C C7N   . NDP C 3 .   ? -1.94526  5.97740   17.19565  1.000 54.26267 ? 602  NDP A C7N   1 
HETATM 4190 O O7N   . NDP C 3 .   ? -1.32152  6.88320   16.62695  1.000 65.21267 ? 602  NDP A O7N   1 
HETATM 4191 N N7N   . NDP C 3 .   ? -2.48659  4.91976   16.44794  1.000 45.70267 ? 602  NDP A N7N   1 
HETATM 4192 C C4N   . NDP C 3 .   ? -1.46252  6.87369   19.55288  1.000 55.92267 ? 602  NDP A C4N   1 
HETATM 4193 C C5N   . NDP C 3 .   ? -1.62693  6.47243   20.99131  1.000 58.64267 ? 602  NDP A C5N   1 
HETATM 4194 C C6N   . NDP C 3 .   ? -2.47995  5.50473   21.36164  1.000 59.36017 ? 602  NDP A C6N   1 
HETATM 4195 P P2B   . NDP C 3 .   ? -16.40028 2.04404   16.29446  1.000 31.25850 ? 602  NDP A P2B   1 
HETATM 4196 O O1X   . NDP C 3 .   ? -16.07914 0.83404   17.12412  1.000 31.84029 ? 602  NDP A O1X   1 
HETATM 4197 O O2X   . NDP C 3 .   ? -17.80232 2.13346   15.68878  1.000 30.00346 ? 602  NDP A O2X   1 
HETATM 4198 O O3X   . NDP C 3 .   ? -15.77281 3.33833   16.69742  1.000 29.84915 ? 602  NDP A O3X   1 
HETATM 4199 O O     . HOH D 4 .   ? -5.72140  5.30814   46.75260  1.000 46.88835 ? 701  HOH A O     1 
HETATM 4200 O O     . HOH D 4 .   ? 21.16554  0.68974   16.42081  1.000 38.43131 ? 702  HOH A O     1 
HETATM 4201 O O     . HOH D 4 .   ? 9.21246   -2.94023  11.92837  1.000 39.90252 ? 703  HOH A O     1 
HETATM 4202 O O     . HOH D 4 .   ? -21.96433 25.62129  23.99725  1.000 38.89127 ? 704  HOH A O     1 
HETATM 4203 O O     . HOH D 4 .   ? 17.74807  17.54936  30.48102  1.000 35.25622 ? 705  HOH A O     1 
HETATM 4204 O O     . HOH D 4 .   ? 16.91355  9.64655   10.51591  1.000 45.52254 ? 706  HOH A O     1 
HETATM 4205 O O     . HOH D 4 .   ? 16.81007  -20.22168 36.69915  1.000 36.34386 ? 707  HOH A O     1 
HETATM 4206 O O     . HOH D 4 .   ? 24.02100  2.82815   18.11118  1.000 38.50653 ? 708  HOH A O     1 
HETATM 4207 O O     . HOH D 4 .   ? -25.12356 8.07682   6.43470   1.000 44.94008 ? 709  HOH A O     1 
HETATM 4208 O O     . HOH D 4 .   ? 0.19868   -3.20363  30.33712  1.000 31.04753 ? 710  HOH A O     1 
HETATM 4209 O O     . HOH D 4 .   ? 1.09954   -6.89861  25.08686  1.000 35.71052 ? 711  HOH A O     1 
HETATM 4210 O O     . HOH D 4 .   ? -0.36274  7.21462   27.72941  1.000 40.91883 ? 712  HOH A O     1 
HETATM 4211 O O     . HOH D 4 .   ? 2.28389   24.32446  24.30867  1.000 35.65348 ? 713  HOH A O     1 
HETATM 4212 O O     . HOH D 4 .   ? 23.64190  -6.31660  37.46807  1.000 39.89504 ? 714  HOH A O     1 
HETATM 4213 O O     . HOH D 4 .   ? 14.21845  28.32567  12.86778  1.000 46.26363 ? 715  HOH A O     1 
HETATM 4214 O O     . HOH D 4 .   ? -20.06935 4.65546   -1.84061  1.000 46.17853 ? 716  HOH A O     1 
HETATM 4215 O O     . HOH D 4 .   ? -20.71156 -11.77091 -6.00978  1.000 41.78121 ? 717  HOH A O     1 
HETATM 4216 O O     . HOH D 4 .   ? -2.29478  0.93625   15.79435  1.000 30.45340 ? 718  HOH A O     1 
HETATM 4217 O O     . HOH D 4 .   ? 12.68471  -20.99153 25.32253  1.000 47.15065 ? 719  HOH A O     1 
HETATM 4218 O O     . HOH D 4 .   ? -17.31219 -11.28151 -8.94685  1.000 33.43202 ? 720  HOH A O     1 
HETATM 4219 O O     . HOH D 4 .   ? -25.23349 6.95586   10.39578  1.000 45.50374 ? 721  HOH A O     1 
HETATM 4220 O O     . HOH D 4 .   ? 13.60928  14.46293  34.06844  1.000 42.06721 ? 722  HOH A O     1 
HETATM 4221 O O     . HOH D 4 .   ? 17.65599  6.42382   35.73082  1.000 29.43548 ? 723  HOH A O     1 
HETATM 4222 O O     . HOH D 4 .   ? 11.14099  10.91848  20.22964  1.000 27.19670 ? 724  HOH A O     1 
HETATM 4223 O O     . HOH D 4 .   ? 9.17604   19.29246  38.30125  1.000 48.72637 ? 725  HOH A O     1 
HETATM 4224 O O     . HOH D 4 .   ? 10.35322  11.14262  12.22782  1.000 21.65294 ? 726  HOH A O     1 
HETATM 4225 O O     . HOH D 4 .   ? -17.38325 26.74972  19.19651  1.000 33.05555 ? 727  HOH A O     1 
HETATM 4226 O O     . HOH D 4 .   ? -23.73260 -10.87743 7.81067   1.000 34.44493 ? 728  HOH A O     1 
HETATM 4227 O O     . HOH D 4 .   ? -15.88468 -6.75661  15.39818  1.000 41.01608 ? 729  HOH A O     1 
HETATM 4228 O O     . HOH D 4 .   ? 3.70851   21.61973  30.45638  1.000 41.08704 ? 730  HOH A O     1 
HETATM 4229 O O     . HOH D 4 .   ? -9.12748  -0.02446  -13.63477 1.000 40.09504 ? 731  HOH A O     1 
HETATM 4230 O O     . HOH D 4 .   ? -14.61739 5.00934   15.11931  1.000 26.91373 ? 732  HOH A O     1 
HETATM 4231 O O     . HOH D 4 .   ? 10.91742  5.73688   45.16852  1.000 37.70311 ? 733  HOH A O     1 
HETATM 4232 O O     . HOH D 4 .   ? -22.28235 19.84647  18.69095  1.000 39.71543 ? 734  HOH A O     1 
HETATM 4233 O O     . HOH D 4 .   ? -4.52784  15.34358  2.81432   1.000 24.96595 ? 735  HOH A O     1 
HETATM 4234 O O     . HOH D 4 .   ? -12.62288 -17.59564 -1.76182  1.000 41.64218 ? 736  HOH A O     1 
HETATM 4235 O O     . HOH D 4 .   ? 1.33151   18.93216  29.26370  1.000 25.35691 ? 737  HOH A O     1 
HETATM 4236 O O     . HOH D 4 .   ? -16.70287 12.25971  42.19224  1.000 47.58996 ? 738  HOH A O     1 
HETATM 4237 O O     . HOH D 4 .   ? 1.89304   20.36383  16.86973  1.000 30.68869 ? 739  HOH A O     1 
HETATM 4238 O O     . HOH D 4 .   ? 19.751    22.872    8.018     1.000 33.00353 ? 740  HOH A O     1 
HETATM 4239 O O     . HOH D 4 .   ? 24.34763  -6.05588  24.52426  1.000 33.02094 ? 741  HOH A O     1 
HETATM 4240 O O     . HOH D 4 .   ? -4.01191  -7.24141  -4.55897  1.000 31.63377 ? 742  HOH A O     1 
HETATM 4241 O O     . HOH D 4 .   ? -18.86337 -4.42593  10.30138  1.000 39.70482 ? 743  HOH A O     1 
HETATM 4242 O O     . HOH D 4 .   ? 16.31024  10.63396  24.88327  1.000 29.70258 ? 744  HOH A O     1 
HETATM 4243 O O     . HOH D 4 .   ? -13.54985 -0.27025  -5.12662  1.000 36.87575 ? 745  HOH A O     1 
HETATM 4244 O O     . HOH D 4 .   ? 2.30923   -3.92889  31.57248  1.000 29.79616 ? 746  HOH A O     1 
HETATM 4245 O O     . HOH D 4 .   ? -4.18773  10.99737  34.69089  1.000 42.34355 ? 747  HOH A O     1 
HETATM 4246 O O     . HOH D 4 .   ? -7.22295  22.23367  3.94795   1.000 42.28935 ? 748  HOH A O     1 
HETATM 4247 O O     . HOH D 4 .   ? 8.13663   0.74014   8.74057   1.000 43.44802 ? 749  HOH A O     1 
HETATM 4248 O O     . HOH D 4 .   ? -28.39232 0.08679   3.32407   1.000 33.00888 ? 750  HOH A O     1 
HETATM 4249 O O     . HOH D 4 .   ? -18.97195 -14.91668 1.24841   1.000 32.33876 ? 751  HOH A O     1 
HETATM 4250 O O     . HOH D 4 .   ? -5.54476  29.27674  28.90507  1.000 38.61518 ? 752  HOH A O     1 
HETATM 4251 O O     . HOH D 4 .   ? 16.08295  7.08707   11.58157  1.000 43.00585 ? 753  HOH A O     1 
HETATM 4252 O O     . HOH D 4 .   ? -19.29667 21.34030  3.23650   1.000 28.28715 ? 754  HOH A O     1 
HETATM 4253 O O     . HOH D 4 .   ? 1.28308   -7.77579  41.63107  1.000 37.58245 ? 755  HOH A O     1 
HETATM 4254 O O     . HOH D 4 .   ? 19.54867  4.44623   34.65222  1.000 36.91634 ? 756  HOH A O     1 
HETATM 4255 O O     . HOH D 4 .   ? -17.85053 -12.31250 -5.77494  1.000 33.53504 ? 757  HOH A O     1 
HETATM 4256 O O     . HOH D 4 .   ? 3.71098   -23.83091 31.29427  1.000 47.09286 ? 758  HOH A O     1 
HETATM 4257 O O     . HOH D 4 .   ? -15.32702 1.37495   10.70313  1.000 25.93907 ? 759  HOH A O     1 
HETATM 4258 O O     . HOH D 4 .   ? -16.11065 14.71231  -2.01393  1.000 38.08949 ? 760  HOH A O     1 
HETATM 4259 O O     . HOH D 4 .   ? 20.68234  22.26517  16.14303  1.000 46.82043 ? 761  HOH A O     1 
HETATM 4260 O O     . HOH D 4 .   ? -2.08545  -1.14656  14.30192  1.000 25.77584 ? 762  HOH A O     1 
HETATM 4261 O O     . HOH D 4 .   ? -8.30666  5.51477   18.12137  1.000 29.55666 ? 763  HOH A O     1 
HETATM 4262 O O     . HOH D 4 .   ? -14.08511 3.11814   18.74152  1.000 40.75236 ? 764  HOH A O     1 
HETATM 4263 O O     . HOH D 4 .   ? 14.78652  4.01566   41.42354  1.000 37.73323 ? 765  HOH A O     1 
HETATM 4264 O O     . HOH D 4 .   ? -6.52254  29.83597  26.34159  1.000 36.77742 ? 766  HOH A O     1 
HETATM 4265 O O     . HOH D 4 .   ? -17.35331 27.18035  30.84794  1.000 40.90290 ? 767  HOH A O     1 
HETATM 4266 O O     . HOH D 4 .   ? 0.84404   0.57886   21.21022  1.000 35.93295 ? 768  HOH A O     1 
HETATM 4267 O O     . HOH D 4 .   ? 3.16805   -4.50193  21.74707  1.000 31.20251 ? 769  HOH A O     1 
HETATM 4268 O O     . HOH D 4 .   ? 2.82892   22.70688  14.20858  1.000 23.99092 ? 770  HOH A O     1 
HETATM 4269 O O     . HOH D 4 .   ? -12.79485 -12.13751 11.73342  1.000 37.49505 ? 771  HOH A O     1 
HETATM 4270 O O     . HOH D 4 .   ? -19.79327 36.43492  23.16801  1.000 41.99084 ? 772  HOH A O     1 
HETATM 4271 O O     . HOH D 4 .   ? 0.61653   -3.48457  24.11994  1.000 37.02353 ? 773  HOH A O     1 
HETATM 4272 O O     . HOH D 4 .   ? 13.97087  2.04471   11.68833  1.000 29.20860 ? 774  HOH A O     1 
HETATM 4273 O O     . HOH D 4 .   ? 18.09527  16.68393  15.25935  1.000 34.90536 ? 775  HOH A O     1 
HETATM 4274 O O     . HOH D 4 .   ? 2.33092   0.04826   35.72175  1.000 34.35316 ? 776  HOH A O     1 
HETATM 4275 O O     . HOH D 4 .   ? -16.98508 31.06768  19.51207  1.000 40.62584 ? 777  HOH A O     1 
HETATM 4276 O O     . HOH D 4 .   ? 19.92737  -10.95694 22.61364  1.000 39.37834 ? 778  HOH A O     1 
HETATM 4277 O O     . HOH D 4 .   ? -11.69242 4.68660   18.43922  1.000 39.72411 ? 779  HOH A O     1 
HETATM 4278 O O     . HOH D 4 .   ? -7.11755  -8.44812  -6.73140  1.000 27.96630 ? 780  HOH A O     1 
HETATM 4279 O O     . HOH D 4 .   ? 16.11007  18.89499  12.60781  1.000 26.99790 ? 781  HOH A O     1 
HETATM 4280 O O     . HOH D 4 .   ? 2.33233   -3.70845  11.48951  1.000 26.26144 ? 782  HOH A O     1 
HETATM 4281 O O     . HOH D 4 .   ? 15.22481  26.88197  33.77348  1.000 35.36000 ? 783  HOH A O     1 
HETATM 4282 O O     . HOH D 4 .   ? -10.72889 -3.05988  43.06945  1.000 47.74000 ? 784  HOH A O     1 
HETATM 4283 O O     . HOH D 4 .   ? -7.99251  17.06721  8.26948   1.000 29.17352 ? 785  HOH A O     1 
HETATM 4284 O O     . HOH D 4 .   ? 2.95026   4.16654   -4.03724  1.000 38.16518 ? 786  HOH A O     1 
HETATM 4285 O O     . HOH D 4 .   ? -10.09983 21.23899  29.07648  1.000 33.95086 ? 787  HOH A O     1 
HETATM 4286 O O     . HOH D 4 .   ? -11.24369 26.01805  7.13924   1.000 46.96400 ? 788  HOH A O     1 
HETATM 4287 O O     . HOH D 4 .   ? 7.70271   0.50214   22.88777  1.000 23.84864 ? 789  HOH A O     1 
HETATM 4288 O O     . HOH D 4 .   ? 4.53629   25.49150  26.21384  1.000 46.66240 ? 790  HOH A O     1 
HETATM 4289 O O     . HOH D 4 .   ? -22.97064 1.45897   -1.28874  1.000 28.89682 ? 791  HOH A O     1 
HETATM 4290 O O     . HOH D 4 .   ? 4.56160   -1.96652  29.50711  1.000 27.09647 ? 792  HOH A O     1 
HETATM 4291 O O     . HOH D 4 .   ? -14.52903 -8.45508  -9.48110  1.000 27.11212 ? 793  HOH A O     1 
HETATM 4292 O O     . HOH D 4 .   ? -24.18663 -6.61205  9.15360   1.000 42.37326 ? 794  HOH A O     1 
HETATM 4293 O O     . HOH D 4 .   ? -16.77921 1.66095   -2.96237  1.000 28.76192 ? 795  HOH A O     1 
HETATM 4294 O O     . HOH D 4 .   ? -0.25702  11.27487  15.95581  1.000 32.27582 ? 796  HOH A O     1 
HETATM 4295 O O     . HOH D 4 .   ? -5.04794  21.29858  17.95196  1.000 35.46961 ? 797  HOH A O     1 
HETATM 4296 O O     . HOH D 4 .   ? -29.40812 -6.22948  3.55405   1.000 35.92066 ? 798  HOH A O     1 
HETATM 4297 O O     . HOH D 4 .   ? -14.79861 12.16746  11.06346  1.000 24.85686 ? 799  HOH A O     1 
HETATM 4298 O O     . HOH D 4 .   ? -1.93522  -4.88659  27.11686  1.000 35.70283 ? 800  HOH A O     1 
HETATM 4299 O O     . HOH D 4 .   ? 0.07980   -8.02105  0.81379   1.000 35.09890 ? 801  HOH A O     1 
HETATM 4300 O O     . HOH D 4 .   ? -14.18545 9.74041   10.00246  1.000 22.34938 ? 802  HOH A O     1 
HETATM 4301 O O     . HOH D 4 .   ? 20.640    20.340    8.729     1.000 39.00196 ? 803  HOH A O     1 
HETATM 4302 O O     . HOH D 4 .   ? 6.923     -29.802   26.035    1.000 61.40267 ? 804  HOH A O     1 
HETATM 4303 O O     . HOH D 4 .   ? 8.30687   20.96081  19.14235  1.000 27.61818 ? 805  HOH A O     1 
HETATM 4304 O O     . HOH D 4 .   ? 0.90407   -1.79963  -7.52184  1.000 30.45960 ? 806  HOH A O     1 
HETATM 4305 O O     . HOH D 4 .   ? -14.13071 -0.59085  18.37008  1.000 47.17941 ? 807  HOH A O     1 
HETATM 4306 O O     . HOH D 4 .   ? -17.98115 -4.74035  16.72224  1.000 45.87907 ? 808  HOH A O     1 
HETATM 4307 O O     . HOH D 4 .   ? -0.68752  12.11676  11.03972  1.000 25.27571 ? 809  HOH A O     1 
HETATM 4308 O O     . HOH D 4 .   ? -7.99860  17.13719  -1.28893  1.000 36.46035 ? 810  HOH A O     1 
HETATM 4309 O O     . HOH D 4 .   ? -20.60919 -6.52796  9.75565   1.000 45.70128 ? 811  HOH A O     1 
HETATM 4310 O O     . HOH D 4 .   ? -4.70452  9.68666   14.30691  1.000 32.17870 ? 812  HOH A O     1 
HETATM 4311 O O     . HOH D 4 .   ? -12.20996 1.04883   -3.15634  1.000 23.15934 ? 813  HOH A O     1 
HETATM 4312 O O     . HOH D 4 .   ? 14.66138  11.36329  34.44004  1.000 51.14267 ? 814  HOH A O     1 
HETATM 4313 O O     . HOH D 4 .   ? -1.59611  15.86371  37.91565  1.000 33.24367 ? 815  HOH A O     1 
HETATM 4314 O O     . HOH D 4 .   ? -2.77669  10.63209  0.53531   1.000 27.02402 ? 816  HOH A O     1 
HETATM 4315 O O     . HOH D 4 .   ? -22.74223 -1.38428  11.83638  1.000 47.35855 ? 817  HOH A O     1 
HETATM 4316 O O     . HOH D 4 .   ? 8.11196   -3.29808  27.21929  1.000 22.06304 ? 818  HOH A O     1 
HETATM 4317 O O     . HOH D 4 .   ? -15.57857 4.10533   12.10921  1.000 23.91241 ? 819  HOH A O     1 
HETATM 4318 O O     . HOH D 4 .   ? 4.47357   18.94433  29.99256  1.000 29.58377 ? 820  HOH A O     1 
HETATM 4319 O O     . HOH D 4 .   ? 0.74915   10.19551  9.65491   1.000 24.86535 ? 821  HOH A O     1 
HETATM 4320 O O     . HOH D 4 .   ? 9.23014   3.20267   45.72969  1.000 31.88095 ? 822  HOH A O     1 
HETATM 4321 O O     . HOH D 4 .   ? -19.83310 19.51186  9.83866   1.000 28.76787 ? 823  HOH A O     1 
HETATM 4322 O O     . HOH D 4 .   ? 5.30020   3.15692   9.47901   1.000 24.91286 ? 824  HOH A O     1 
HETATM 4323 O O     . HOH D 4 .   ? -2.02959  6.92010   29.57123  1.000 39.40812 ? 825  HOH A O     1 
HETATM 4324 O O     . HOH D 4 .   ? 16.50630  15.13023  31.74897  1.000 42.63379 ? 826  HOH A O     1 
HETATM 4325 O O     . HOH D 4 .   ? 8.07536   20.95813  25.49061  1.000 38.81408 ? 827  HOH A O     1 
HETATM 4326 O O     . HOH D 4 .   ? -23.54559 16.87129  14.26869  1.000 46.84000 ? 828  HOH A O     1 
HETATM 4327 O O     . HOH D 4 .   ? -20.85957 6.30011   10.28621  1.000 35.96937 ? 829  HOH A O     1 
HETATM 4328 O O     . HOH D 4 .   ? -13.99722 37.72452  26.18654  1.000 45.90415 ? 830  HOH A O     1 
HETATM 4329 O O     . HOH D 4 .   ? -24.78340 12.52067  4.14155   1.000 31.05317 ? 831  HOH A O     1 
HETATM 4330 O O     . HOH D 4 .   ? -20.05393 7.12819   -0.83949  1.000 36.97288 ? 832  HOH A O     1 
HETATM 4331 O O     . HOH D 4 .   ? -19.98882 -10.48235 -8.57627  1.000 39.35470 ? 833  HOH A O     1 
HETATM 4332 O O     . HOH D 4 .   ? -1.39634  4.31807   32.26520  1.000 35.32050 ? 834  HOH A O     1 
HETATM 4333 O O     . HOH D 4 .   ? 5.97369   -21.47766 34.97451  1.000 38.16285 ? 835  HOH A O     1 
HETATM 4334 O O     . HOH D 4 .   ? -25.72873 -0.36644  12.22123  1.000 43.58999 ? 836  HOH A O     1 
HETATM 4335 O O     . HOH D 4 .   ? 11.20634  -5.50918  2.02195   1.000 40.80132 ? 837  HOH A O     1 
HETATM 4336 O O     . HOH D 4 .   ? -6.76213  -10.19236 24.62362  1.000 44.37709 ? 838  HOH A O     1 
HETATM 4337 O O     . HOH D 4 .   ? -9.57655  -14.06183 3.23946   1.000 39.45178 ? 839  HOH A O     1 
HETATM 4338 O O     . HOH D 4 .   ? -6.60876  -13.35390 1.12100   1.000 40.86378 ? 840  HOH A O     1 
HETATM 4339 O O     . HOH D 4 .   ? -7.85707  -0.51230  40.60379  1.000 46.33872 ? 841  HOH A O     1 
HETATM 4340 O O     . HOH D 4 .   ? -16.14497 17.12092  -1.15821  1.000 28.42480 ? 842  HOH A O     1 
HETATM 4341 O O     . HOH D 4 .   ? -6.03688  -6.85184  42.54274  1.000 43.55601 ? 843  HOH A O     1 
HETATM 4342 O O     . HOH D 4 .   ? -2.61847  26.57197  21.43673  1.000 32.43847 ? 844  HOH A O     1 
HETATM 4343 O O     . HOH D 4 .   ? -1.16195  -9.39454  7.67557   1.000 44.01315 ? 845  HOH A O     1 
HETATM 4344 O O     . HOH D 4 .   ? 9.18401   -26.41292 31.16194  1.000 36.22157 ? 846  HOH A O     1 
HETATM 4345 O O     . HOH D 4 .   ? -1.03269  28.90036  16.50981  1.000 34.85592 ? 847  HOH A O     1 
HETATM 4346 O O     . HOH D 4 .   ? 8.46042   -25.28494 33.52312  1.000 39.64798 ? 848  HOH A O     1 
HETATM 4347 O O     . HOH D 4 .   ? -13.61716 8.76373   12.41737  1.000 26.07726 ? 849  HOH A O     1 
HETATM 4348 O O     . HOH D 4 .   ? 13.40793  -19.32947 23.26765  1.000 43.78891 ? 850  HOH A O     1 
HETATM 4349 O O     . HOH D 4 .   ? 0.76716   -11.30021 26.35534  1.000 37.22870 ? 851  HOH A O     1 
HETATM 4350 O O     . HOH D 4 .   ? 16.74750  -11.68351 17.41065  1.000 41.48083 ? 852  HOH A O     1 
HETATM 4351 O O     . HOH D 4 .   ? 6.02905   15.33344  39.82504  1.000 34.05431 ? 853  HOH A O     1 
HETATM 4352 O O     . HOH D 4 .   ? -8.69218  2.81592   13.43020  1.000 21.35182 ? 854  HOH A O     1 
HETATM 4353 O O     . HOH D 4 .   ? 10.38604  10.36407  29.50050  1.000 29.39086 ? 855  HOH A O     1 
HETATM 4354 O O     . HOH D 4 .   ? 20.32865  -12.15609 31.33417  1.000 34.86960 ? 856  HOH A O     1 
HETATM 4355 O O     . HOH D 4 .   ? -0.76654  -5.40702  21.03918  1.000 44.76462 ? 857  HOH A O     1 
HETATM 4356 O O     . HOH D 4 .   ? 19.20151  2.49634   15.52956  1.000 34.05235 ? 858  HOH A O     1 
HETATM 4357 O O     . HOH D 4 .   ? 0.96801   4.80383   -6.09383  1.000 39.40940 ? 859  HOH A O     1 
HETATM 4358 O O     . HOH D 4 .   ? -6.32024  22.06197  31.04248  1.000 31.17514 ? 860  HOH A O     1 
HETATM 4359 O O     . HOH D 4 .   ? -20.05366 1.38183   17.13610  1.000 41.64097 ? 861  HOH A O     1 
HETATM 4360 O O     . HOH D 4 .   ? 17.39650  10.22106  28.08984  1.000 29.06994 ? 862  HOH A O     1 
HETATM 4361 O O     . HOH D 4 .   ? -12.50282 -9.77108  38.46823  1.000 57.00552 ? 863  HOH A O     1 
HETATM 4362 O O     . HOH D 4 .   ? 4.16395   22.26958  33.29691  1.000 42.18365 ? 864  HOH A O     1 
HETATM 4363 O O     . HOH D 4 .   ? -26.05131 -8.01199  -4.13097  1.000 36.99788 ? 865  HOH A O     1 
HETATM 4364 O O     . HOH D 4 .   ? 8.60398   -18.33615 21.77213  1.000 46.05651 ? 866  HOH A O     1 
HETATM 4365 O O     . HOH D 4 .   ? -12.13662 28.31650  10.45690  1.000 51.73731 ? 867  HOH A O     1 
HETATM 4366 O O     . HOH D 4 .   ? 0.28105   2.69029   33.84093  1.000 33.25446 ? 868  HOH A O     1 
HETATM 4367 O O     . HOH D 4 .   ? -23.93741 -9.79268  -3.59669  1.000 35.81446 ? 869  HOH A O     1 
HETATM 4368 O O     . HOH D 4 .   ? 20.44795  17.21955  28.33434  1.000 35.61118 ? 870  HOH A O     1 
HETATM 4369 O O     . HOH D 4 .   ? 7.46331   12.68673  11.54610  1.000 24.49439 ? 871  HOH A O     1 
HETATM 4370 O O     . HOH D 4 .   ? 0.21604   -22.58910 31.05580  1.000 44.71104 ? 872  HOH A O     1 
HETATM 4371 O O     . HOH D 4 .   ? -20.18294 27.06357  19.39773  1.000 48.68673 ? 873  HOH A O     1 
HETATM 4372 O O     . HOH D 4 .   ? 1.37417   -5.26111  -2.60185  1.000 30.06860 ? 874  HOH A O     1 
HETATM 4373 O O     . HOH D 4 .   ? 1.18154   26.91819  22.20090  1.000 44.18915 ? 875  HOH A O     1 
HETATM 4374 O O     . HOH D 4 .   ? -14.91824 7.78425   -6.27789  1.000 40.76525 ? 876  HOH A O     1 
HETATM 4375 O O     . HOH D 4 .   ? 10.39299  -5.55148  21.19192  1.000 25.67271 ? 877  HOH A O     1 
HETATM 4376 O O     . HOH D 4 .   ? 4.18494   -6.88200  12.64061  1.000 35.69408 ? 878  HOH A O     1 
HETATM 4377 O O     . HOH D 4 .   ? -7.27492  -1.01131  27.11057  1.000 41.01663 ? 879  HOH A O     1 
HETATM 4378 O O     . HOH D 4 .   ? -8.84884  -2.68652  -9.59367  1.000 26.61454 ? 880  HOH A O     1 
HETATM 4379 O O     . HOH D 4 .   ? -3.00121  27.73020  27.84227  1.000 36.42637 ? 881  HOH A O     1 
HETATM 4380 O O     . HOH D 4 .   ? -8.54535  -0.93556  20.16525  1.000 32.03934 ? 882  HOH A O     1 
HETATM 4381 O O     . HOH D 4 .   ? 12.31450  -27.61889 25.24567  1.000 42.10727 ? 883  HOH A O     1 
HETATM 4382 O O     . HOH D 4 .   ? -7.32675  7.08648   -9.51448  1.000 37.45177 ? 884  HOH A O     1 
HETATM 4383 O O     . HOH D 4 .   ? -8.34317  17.98223  11.36195  1.000 25.38525 ? 885  HOH A O     1 
HETATM 4384 O O     . HOH D 4 .   ? -15.50092 25.64629  1.91479   1.000 42.69197 ? 886  HOH A O     1 
HETATM 4385 O O     . HOH D 4 .   ? 9.24881   7.46594   40.58734  1.000 31.65160 ? 887  HOH A O     1 
HETATM 4386 O O     . HOH D 4 .   ? -16.63300 -15.60933 -2.79230  1.000 30.81475 ? 888  HOH A O     1 
HETATM 4387 O O     . HOH D 4 .   ? -22.83628 5.45358   3.09905   1.000 29.55350 ? 889  HOH A O     1 
HETATM 4388 O O     . HOH D 4 .   ? -17.62890 -8.34573  -6.83328  1.000 28.04601 ? 890  HOH A O     1 
HETATM 4389 O O     . HOH D 4 .   ? 2.63234   1.79022   -4.63898  1.000 32.70867 ? 891  HOH A O     1 
HETATM 4390 O O     . HOH D 4 .   ? 5.74845   5.66692   9.91099   1.000 31.20985 ? 892  HOH A O     1 
HETATM 4391 O O     . HOH D 4 .   ? -14.24306 11.71178  18.47423  1.000 35.31595 ? 893  HOH A O     1 
HETATM 4392 O O     . HOH D 4 .   ? 15.88974  1.59961   47.43966  1.000 41.80934 ? 894  HOH A O     1 
HETATM 4393 O O     . HOH D 4 .   ? 15.26192  8.70852   15.77955  1.000 25.00444 ? 895  HOH A O     1 
HETATM 4394 O O     . HOH D 4 .   ? -18.37818 14.16107  -3.70918  1.000 48.56488 ? 896  HOH A O     1 
HETATM 4395 O O     . HOH D 4 .   ? 6.62240   22.67547  21.78286  1.000 49.29472 ? 897  HOH A O     1 
HETATM 4396 O O     . HOH D 4 .   ? -26.64855 3.05718   0.39820   1.000 47.69442 ? 898  HOH A O     1 
HETATM 4397 O O     . HOH D 4 .   ? 1.93004   -8.01789  15.34747  1.000 44.28401 ? 899  HOH A O     1 
HETATM 4398 O O     . HOH D 4 .   ? -0.11330  20.34110  37.31697  1.000 44.06114 ? 900  HOH A O     1 
HETATM 4399 O O     . HOH D 4 .   ? 4.22138   -7.40082  9.92260   1.000 42.48428 ? 901  HOH A O     1 
HETATM 4400 O O     . HOH D 4 .   ? -9.61093  8.12854   37.17163  1.000 40.03778 ? 902  HOH A O     1 
HETATM 4401 O O     . HOH D 4 .   ? -21.59209 10.72212  11.13371  1.000 39.82074 ? 903  HOH A O     1 
HETATM 4402 O O     . HOH D 4 .   ? -1.15360  10.02674  7.73768   1.000 23.55630 ? 904  HOH A O     1 
HETATM 4403 O O     . HOH D 4 .   ? 9.30429   18.18744  18.71243  1.000 26.57629 ? 905  HOH A O     1 
HETATM 4404 O O     . HOH D 4 .   ? 17.52329  10.49840  19.15599  1.000 34.54813 ? 906  HOH A O     1 
HETATM 4405 O O     . HOH D 4 .   ? -5.47593  -0.73028  -12.36278 1.000 28.49811 ? 907  HOH A O     1 
HETATM 4406 O O     . HOH D 4 .   ? 14.39860  27.88560  31.50343  1.000 39.26309 ? 908  HOH A O     1 
HETATM 4407 O O     . HOH D 4 .   ? -2.98465  11.54556  9.39266   1.000 23.52791 ? 909  HOH A O     1 
HETATM 4408 O O     . HOH D 4 .   ? 15.37680  -7.09572  46.78467  1.000 41.59196 ? 910  HOH A O     1 
HETATM 4409 O O     . HOH D 4 .   ? -10.99472 -13.75139 32.20968  1.000 52.50875 ? 911  HOH A O     1 
HETATM 4410 O O     . HOH D 4 .   ? 4.81763   -2.30788  3.11012   1.000 36.91435 ? 912  HOH A O     1 
HETATM 4411 O O     . HOH D 4 .   ? -20.12150 9.94398   0.94201   1.000 32.75969 ? 913  HOH A O     1 
HETATM 4412 O O     . HOH D 4 .   ? 22.73304  -4.09999  22.95122  1.000 34.77731 ? 914  HOH A O     1 
HETATM 4413 O O     . HOH D 4 .   ? -1.53240  11.54217  13.52319  1.000 24.96067 ? 915  HOH A O     1 
HETATM 4414 O O     . HOH D 4 .   ? -22.25020 13.19574  -1.95257  1.000 37.26382 ? 916  HOH A O     1 
HETATM 4415 O O     . HOH D 4 .   ? 3.73799   -6.99257  44.06216  1.000 35.04467 ? 917  HOH A O     1 
HETATM 4416 O O     . HOH D 4 .   ? 1.43252   18.18957  20.98543  1.000 36.66533 ? 918  HOH A O     1 
HETATM 4417 O O     . HOH D 4 .   ? 16.75127  24.23159  31.10323  1.000 30.66993 ? 919  HOH A O     1 
HETATM 4418 O O     . HOH D 4 .   ? -15.24564 11.09748  -0.53154  1.000 23.94693 ? 920  HOH A O     1 
HETATM 4419 O O     . HOH D 4 .   ? 2.96120   13.85257  9.27105   1.000 25.17941 ? 921  HOH A O     1 
HETATM 4420 O O     . HOH D 4 .   ? -16.60309 36.07438  32.29330  1.000 49.59148 ? 922  HOH A O     1 
HETATM 4421 O O     . HOH D 4 .   ? 18.16325  -13.36871 22.01794  1.000 38.36193 ? 923  HOH A O     1 
HETATM 4422 O O     . HOH D 4 .   ? -12.69830 0.52059   19.78587  1.000 51.90343 ? 924  HOH A O     1 
HETATM 4423 O O     . HOH D 4 .   ? 0.88722   -7.28223  44.60374  1.000 37.36807 ? 925  HOH A O     1 
HETATM 4424 O O     . HOH D 4 .   ? 13.03529  7.52772   8.64519   1.000 42.94085 ? 926  HOH A O     1 
HETATM 4425 O O     . HOH D 4 .   ? -3.33325  -11.08530 2.41445   1.000 29.83769 ? 927  HOH A O     1 
HETATM 4426 O O     . HOH D 4 .   ? -2.83933  13.31175  -5.85249  1.000 46.32701 ? 928  HOH A O     1 
HETATM 4427 O O     . HOH D 4 .   ? -0.20008  13.66660  4.93256   1.000 40.13751 ? 929  HOH A O     1 
HETATM 4428 O O     . HOH D 4 .   ? 3.88124   -10.69106 22.01290  1.000 35.23332 ? 930  HOH A O     1 
HETATM 4429 O O     . HOH D 4 .   ? 15.90064  -11.62171 46.96066  1.000 50.67849 ? 931  HOH A O     1 
HETATM 4430 O O     . HOH D 4 .   ? 0.96441   24.14537  32.20303  1.000 36.01200 ? 932  HOH A O     1 
HETATM 4431 O O     . HOH D 4 .   ? -8.33664  1.69335   39.14221  1.000 49.91000 ? 933  HOH A O     1 
HETATM 4432 O O     . HOH D 4 .   ? -22.80261 -15.55084 -1.09667  1.000 45.82015 ? 934  HOH A O     1 
HETATM 4433 O O     . HOH D 4 .   ? 9.194     23.926    13.101    1.000 32.35231 ? 935  HOH A O     1 
HETATM 4434 O O     . HOH D 4 .   ? -20.90039 8.56660   12.67854  1.000 35.05484 ? 936  HOH A O     1 
HETATM 4435 O O     . HOH D 4 .   ? 3.50665   16.88340  22.68405  1.000 26.25357 ? 937  HOH A O     1 
HETATM 4436 O O     . HOH D 4 .   ? -11.99110 34.60712  32.02286  1.000 47.40966 ? 938  HOH A O     1 
HETATM 4437 O O     . HOH D 4 .   ? 13.48279  12.63308  14.87857  1.000 20.73291 ? 939  HOH A O     1 
HETATM 4438 O O     . HOH D 4 .   ? 21.29220  19.29254  17.79937  1.000 40.38227 ? 940  HOH A O     1 
HETATM 4439 O O     . HOH D 4 .   ? -5.01231  12.75942  33.08053  1.000 43.94111 ? 941  HOH A O     1 
HETATM 4440 O O     . HOH D 4 .   ? -20.51114 24.07226  13.84912  1.000 43.76411 ? 942  HOH A O     1 
HETATM 4441 O O     . HOH D 4 .   ? 6.60646   -6.00931  12.55167  1.000 45.17267 ? 943  HOH A O     1 
HETATM 4442 O O     . HOH D 4 .   ? -17.65753 9.89179   -0.38195  1.000 23.95494 ? 944  HOH A O     1 
HETATM 4443 O O     . HOH D 4 .   ? 22.25780  -10.00331 43.22963  1.000 49.77177 ? 945  HOH A O     1 
HETATM 4444 O O     . HOH D 4 .   ? 4.35329   1.11973   5.85317   1.000 34.71017 ? 946  HOH A O     1 
HETATM 4445 O O     . HOH D 4 .   ? -2.89358  4.32220   -8.59844  1.000 33.95825 ? 947  HOH A O     1 
HETATM 4446 O O     . HOH D 4 .   ? -6.83533  -20.22302 38.99425  1.000 53.88898 ? 948  HOH A O     1 
HETATM 4447 O O     . HOH D 4 .   ? 7.68744   20.44036  28.57283  1.000 33.39157 ? 949  HOH A O     1 
HETATM 4448 O O     . HOH D 4 .   ? -1.49503  18.75170  10.22497  1.000 23.00416 ? 950  HOH A O     1 
HETATM 4449 O O     . HOH D 4 .   ? 17.18162  -22.22704 33.07468  1.000 49.31803 ? 951  HOH A O     1 
HETATM 4450 O O     . HOH D 4 .   ? -23.71147 -12.27258 -2.51929  1.000 46.28045 ? 952  HOH A O     1 
HETATM 4451 O O     . HOH D 4 .   ? -5.06606  29.25957  32.08646  1.000 42.94790 ? 953  HOH A O     1 
HETATM 4452 O O     . HOH D 4 .   ? 4.88300   8.84354   9.73059   1.000 32.06009 ? 954  HOH A O     1 
HETATM 4453 O O     . HOH D 4 .   ? -11.15842 -6.29546  24.49454  1.000 48.70811 ? 955  HOH A O     1 
HETATM 4454 O O     . HOH D 4 .   ? -21.25333 -10.34521 9.26283   1.000 41.28392 ? 956  HOH A O     1 
HETATM 4455 O O     . HOH D 4 .   ? -11.80408 -2.30644  18.55084  1.000 42.29117 ? 957  HOH A O     1 
HETATM 4456 O O     . HOH D 4 .   ? -1.23424  17.72516  21.67406  1.000 27.34728 ? 958  HOH A O     1 
HETATM 4457 O O     . HOH D 4 .   ? -6.15873  -0.93027  14.05833  1.000 23.02244 ? 959  HOH A O     1 
HETATM 4458 O O     . HOH D 4 .   ? -11.51977 25.59832  33.85365  1.000 39.85452 ? 960  HOH A O     1 
HETATM 4459 O O     . HOH D 4 .   ? 14.88221  18.22321  34.59487  1.000 35.27520 ? 961  HOH A O     1 
HETATM 4460 O O     . HOH D 4 .   ? 15.05246  10.40847  18.03786  1.000 29.19834 ? 962  HOH A O     1 
HETATM 4461 O O     . HOH D 4 .   ? -6.19095  32.77669  16.40791  1.000 32.19831 ? 963  HOH A O     1 
HETATM 4462 O O     . HOH D 4 .   ? 8.940     -3.459    -2.539    1.000 46.74860 ? 964  HOH A O     1 
HETATM 4463 O O     . HOH D 4 .   ? 18.88576  22.55371  30.19761  1.000 37.18674 ? 965  HOH A O     1 
HETATM 4464 O O     . HOH D 4 .   ? 18.07996  24.28541  9.76912   1.000 33.77701 ? 966  HOH A O     1 
HETATM 4465 O O     . HOH D 4 .   ? -5.10325  30.95976  11.94834  1.000 44.55915 ? 967  HOH A O     1 
HETATM 4466 O O     . HOH D 4 .   ? 11.04410  13.26795  13.91874  1.000 20.22337 ? 968  HOH A O     1 
HETATM 4467 O O     . HOH D 4 .   ? 9.66222   -11.09634 15.63010  1.000 41.84492 ? 969  HOH A O     1 
HETATM 4468 O O     . HOH D 4 .   ? 4.47022   5.62797   6.14151   1.000 33.16159 ? 970  HOH A O     1 
HETATM 4469 O O     . HOH D 4 .   ? -11.12872 19.83916  30.83961  1.000 33.23012 ? 971  HOH A O     1 
HETATM 4470 O O     . HOH D 4 .   ? 22.42830  11.16427  32.50236  1.000 39.35977 ? 972  HOH A O     1 
HETATM 4471 O O     . HOH D 4 .   ? 4.50394   15.33409  41.89536  1.000 39.84518 ? 973  HOH A O     1 
HETATM 4472 O O     . HOH D 4 .   ? -28.38903 3.27999   12.43167  1.000 53.22492 ? 974  HOH A O     1 
HETATM 4473 O O     . HOH D 4 .   ? -20.72329 -3.69660  13.02851  1.000 38.50220 ? 975  HOH A O     1 
HETATM 4474 O O     . HOH D 4 .   ? 18.96576  8.83298   35.52956  1.000 42.57708 ? 976  HOH A O     1 
HETATM 4475 O O     . HOH D 4 .   ? 3.78839   19.86325  6.99138   1.000 36.60872 ? 977  HOH A O     1 
HETATM 4476 O O     . HOH D 4 .   ? -4.45974  10.40927  16.73880  1.000 30.52383 ? 978  HOH A O     1 
HETATM 4477 O O     . HOH D 4 .   ? 3.48950   0.06274   2.72671   1.000 40.41986 ? 979  HOH A O     1 
HETATM 4478 O O     . HOH D 4 .   ? -1.97185  15.03585  20.85277  1.000 37.90841 ? 980  HOH A O     1 
HETATM 4479 O O     . HOH D 4 .   ? 15.40030  -16.01118 43.77077  1.000 34.86458 ? 981  HOH A O     1 
HETATM 4480 O O     . HOH D 4 .   ? 10.63042  9.39922   39.45618  1.000 39.25335 ? 982  HOH A O     1 
HETATM 4481 O O     . HOH D 4 .   ? 2.66982   4.96324   2.57185   1.000 35.11592 ? 983  HOH A O     1 
HETATM 4482 O O     . HOH D 4 .   ? -16.73825 -1.37458  -6.73077  1.000 29.44845 ? 984  HOH A O     1 
HETATM 4483 O O     . HOH D 4 .   ? -20.27713 9.77171   15.70622  1.000 38.14424 ? 985  HOH A O     1 
HETATM 4484 O O     . HOH D 4 .   ? 1.13423   -2.00631  21.96330  1.000 39.15079 ? 986  HOH A O     1 
HETATM 4485 O O     . HOH D 4 .   ? 0.73674   17.35265  9.74670   1.000 21.55211 ? 987  HOH A O     1 
HETATM 4486 O O     . HOH D 4 .   ? 20.76794  21.77932  28.52233  1.000 45.94757 ? 988  HOH A O     1 
HETATM 4487 O O     . HOH D 4 .   ? 3.717     -6.610    -3.290    1.000 41.83985 ? 989  HOH A O     1 
HETATM 4488 O O     . HOH D 4 .   ? -23.00023 -3.95019  -6.89074  1.000 31.30061 ? 990  HOH A O     1 
HETATM 4489 O O     . HOH D 4 .   ? -6.99570  22.20660  8.78636   1.000 37.12008 ? 991  HOH A O     1 
HETATM 4490 O O     . HOH D 4 .   ? -11.17665 12.84224  -11.69927 1.000 52.50301 ? 992  HOH A O     1 
HETATM 4491 O O     . HOH D 4 .   ? -4.92895  27.97216  22.22252  1.000 29.42847 ? 993  HOH A O     1 
HETATM 4492 O O     . HOH D 4 .   ? 6.78278   22.89452  28.64188  1.000 36.99689 ? 994  HOH A O     1 
HETATM 4493 O O     . HOH D 4 .   ? 8.83614   15.70337  40.45381  1.000 56.27866 ? 995  HOH A O     1 
HETATM 4494 O O     . HOH D 4 .   ? -2.12291  10.15451  17.22090  1.000 45.41958 ? 996  HOH A O     1 
HETATM 4495 O O     . HOH D 4 .   ? -18.93191 -6.68925  12.03568  1.000 41.99837 ? 997  HOH A O     1 
HETATM 4496 O O     . HOH D 4 .   ? -20.49298 -16.14479 -5.42713  1.000 48.71220 ? 998  HOH A O     1 
HETATM 4497 O O     . HOH D 4 .   ? -12.26830 29.65622  13.08725  1.000 51.47801 ? 999  HOH A O     1 
HETATM 4498 O O     . HOH D 4 .   ? 9.93784   24.68007  37.23166  1.000 47.33133 ? 1000 HOH A O     1 
HETATM 4499 O O     . HOH D 4 .   ? 11.84853  12.41236  38.23184  1.000 44.30398 ? 1001 HOH A O     1 
HETATM 4500 O O     . HOH D 4 .   ? 0.96545   27.74569  15.46326  1.000 38.59589 ? 1002 HOH A O     1 
HETATM 4501 O O     . HOH D 4 .   ? -14.19886 3.99450   -9.57037  1.000 51.21226 ? 1003 HOH A O     1 
HETATM 4502 O O     . HOH D 4 .   ? -1.90507  -2.88851  -9.88412  1.000 34.78258 ? 1004 HOH A O     1 
HETATM 4503 O O     . HOH D 4 .   ? -4.17771  18.36934  9.04657   1.000 25.72406 ? 1005 HOH A O     1 
HETATM 4504 O O     . HOH D 4 .   ? 18.27797  26.85836  11.65542  1.000 42.98977 ? 1006 HOH A O     1 
HETATM 4505 O O     . HOH D 4 .   ? -4.47252  29.04699  24.59648  1.000 43.32567 ? 1007 HOH A O     1 
HETATM 4506 O O     . HOH D 4 .   ? -7.97947  -7.40082  44.19486  1.000 48.20284 ? 1008 HOH A O     1 
HETATM 4507 O O     . HOH D 4 .   ? -27.44039 1.64180   -3.01851  1.000 48.49166 ? 1009 HOH A O     1 
HETATM 4508 O O     . HOH D 4 .   ? -19.25518 -0.45470  -6.02378  1.000 39.49763 ? 1010 HOH A O     1 
HETATM 4509 O O     . HOH D 4 .   ? -24.05661 4.47790   0.24177   1.000 46.99985 ? 1011 HOH A O     1 
HETATM 4510 O O     . HOH D 4 .   ? 1.50745   -3.79953  19.47530  1.000 43.74774 ? 1012 HOH A O     1 
HETATM 4511 O O     . HOH D 4 .   ? 15.87238  0.75021   12.79332  1.000 36.57705 ? 1013 HOH A O     1 
HETATM 4512 O O     . HOH D 4 .   ? -23.602   15.652    -4.042    1.000 46.22725 ? 1014 HOH A O     1 
HETATM 4513 O O     . HOH D 4 .   ? -15.90581 2.92533   -7.51476  1.000 39.13375 ? 1015 HOH A O     1 
HETATM 4514 O O     . HOH D 4 .   ? -11.38988 6.26956   -8.88678  1.000 39.88714 ? 1016 HOH A O     1 
HETATM 4515 O O     . HOH D 4 .   ? 22.14728  -14.38611 31.84028  1.000 51.12566 ? 1017 HOH A O     1 
HETATM 4516 O O     . HOH D 4 .   ? 1.69475   27.12775  13.22607  1.000 39.02119 ? 1018 HOH A O     1 
HETATM 4517 O O     . HOH D 4 .   ? 1.64353   22.07564  33.43384  1.000 46.48538 ? 1019 HOH A O     1 
HETATM 4518 O O     . HOH D 4 .   ? -0.84958  27.46439  19.95280  1.000 47.20068 ? 1020 HOH A O     1 
HETATM 4519 O O     . HOH D 4 .   ? 11.26680  24.56360  19.15745  1.000 40.56441 ? 1021 HOH A O     1 
HETATM 4520 O O     . HOH D 4 .   ? 15.62382  6.04599   40.54434  1.000 46.39761 ? 1022 HOH A O     1 
HETATM 4521 O O     . HOH D 4 .   ? -1.16567  2.05247   21.23146  1.000 44.42492 ? 1023 HOH A O     1 
HETATM 4522 O O     . HOH D 4 .   ? 7.321     24.297    15.223    1.000 44.51889 ? 1024 HOH A O     1 
HETATM 4523 O O     . HOH D 4 .   ? -17.88159 -14.96465 -5.25738  1.000 42.26284 ? 1025 HOH A O     1 
HETATM 4524 O O     . HOH D 4 .   ? -10.87990 8.78922   -9.85609  1.000 43.61101 ? 1026 HOH A O     1 
HETATM 4525 O O     . HOH D 4 .   ? 1.39153   -6.51737  22.37076  1.000 44.11134 ? 1027 HOH A O     1 
HETATM 4526 O O     . HOH D 4 .   ? -2.41486  2.84988   23.22050  1.000 47.78561 ? 1028 HOH A O     1 
HETATM 4527 O O     . HOH D 4 .   ? 10.30328  7.96657   8.79837   1.000 45.10556 ? 1029 HOH A O     1 
HETATM 4528 O O     . HOH D 4 .   ? -5.82127  15.25088  0.15889   1.000 41.33663 ? 1030 HOH A O     1 
HETATM 4529 O O     . HOH D 4 .   ? 4.53469   0.74052   -6.63444  1.000 44.34888 ? 1031 HOH A O     1 
HETATM 4530 O O     . HOH D 4 .   ? -15.58931 29.01099  18.79389  1.000 40.20352 ? 1032 HOH A O     1 
HETATM 4531 O O     . HOH D 4 .   ? -21.69699 -0.72910  16.65017  1.000 52.02686 ? 1033 HOH A O     1 
HETATM 4532 O O     . HOH D 4 .   ? 12.22817  13.69963  41.30913  1.000 49.20290 ? 1034 HOH A O     1 
HETATM 4533 O O     . HOH D 4 .   ? -4.29539  3.48733   -11.32374 1.000 42.41244 ? 1035 HOH A O     1 
HETATM 4534 O O     . HOH D 4 .   ? 1.51979   17.69797  7.50251   1.000 41.97020 ? 1036 HOH A O     1 
HETATM 4535 O O     . HOH D 4 .   ? -2.23867  6.59685   -8.24554  1.000 46.66267 ? 1037 HOH A O     1 
HETATM 4536 O O     . HOH D 4 .   ? -22.11952 8.91229   -1.48755  1.000 47.53303 ? 1038 HOH A O     1 
HETATM 4537 O O     . HOH D 4 .   ? 0.16107   11.12567  5.80118   1.000 27.97462 ? 1039 HOH A O     1 
HETATM 4538 O O     . HOH D 4 .   ? 4.41345   23.45067  35.61292  1.000 54.13177 ? 1040 HOH A O     1 
HETATM 4539 O O     . HOH D 4 .   ? -7.64967  19.74474  9.13310   1.000 35.64307 ? 1041 HOH A O     1 
HETATM 4540 O O     . HOH D 4 .   ? -24.65108 10.97596  1.40394   1.000 41.64623 ? 1042 HOH A O     1 
HETATM 4541 O O     . HOH D 4 .   ? 6.18344   7.10528   8.05477   1.000 48.42995 ? 1043 HOH A O     1 
HETATM 4542 O O     . HOH D 4 .   ? -22.47494 2.63501   -3.78068  1.000 42.21234 ? 1044 HOH A O     1 
HETATM 4543 O O     . HOH D 4 .   ? -18.32750 -16.37697 -1.01252  1.000 41.09977 ? 1045 HOH A O     1 
HETATM 4544 O O     . HOH D 4 .   ? -22.38294 11.37457  -0.09946  1.000 40.87450 ? 1046 HOH A O     1 
HETATM 4545 O O     . HOH D 4 .   ? 1.661     21.140    8.995     1.000 31.91080 ? 1047 HOH A O     1 
HETATM 4546 O O     . HOH D 4 .   ? -28.25576 -13.36790 3.37233   1.000 44.51662 ? 1048 HOH A O     1 
HETATM 4547 O O     . HOH D 4 .   ? 2.735     24.498    12.106    1.000 39.44960 ? 1049 HOH A O     1 
HETATM 4548 O O     . HOH D 4 .   ? -21.02059 23.80919  11.10153  1.000 47.66743 ? 1050 HOH A O     1 
HETATM 4549 O O     . HOH D 4 .   ? -4.13415  -10.62448 -5.08174  1.000 42.36100 ? 1051 HOH A O     1 
HETATM 4550 O O     . HOH D 4 .   ? -4.37262  31.57088  14.59895  1.000 39.21452 ? 1052 HOH A O     1 
HETATM 4551 O O     . HOH D 4 .   ? 17.14871  24.86548  33.79858  1.000 45.13371 ? 1053 HOH A O     1 
HETATM 4552 O O     . HOH D 4 .   ? -20.79994 -17.03083 -2.08717  1.000 39.32201 ? 1054 HOH A O     1 
HETATM 4553 O O     . HOH D 4 .   ? -21.82438 20.85636  10.86256  1.000 43.77274 ? 1055 HOH A O     1 
HETATM 4554 O O     . HOH D 4 .   ? -22.51414 22.94674  8.72574   1.000 52.99629 ? 1056 HOH A O     1 
HETATM 4555 O O     . HOH D 4 .   ? -1.55003  18.67758  37.92173  1.000 41.25846 ? 1057 HOH A O     1 
HETATM 4556 O O     . HOH D 4 .   ? -2.01905  29.22653  25.71318  1.000 46.09105 ? 1058 HOH A O     1 
HETATM 4557 O O     . HOH D 4 .   ? 15.82896  3.60229   10.20103  1.000 43.23487 ? 1059 HOH A O     1 
HETATM 4558 O O     . HOH D 4 .   ? -21.31372 21.31963  5.14074   1.000 33.86566 ? 1060 HOH A O     1 
HETATM 4559 O O     . HOH D 4 .   ? 1.70014   -13.00872 19.42360  1.000 48.35684 ? 1061 HOH A O     1 
HETATM 4560 O O     . HOH D 4 .   ? -25.82596 19.95657  16.65980  1.000 60.14071 ? 1062 HOH A O     1 
HETATM 4561 O O     . HOH D 4 .   ? 2.98370   11.03450  8.88984   1.000 28.10898 ? 1063 HOH A O     1 
HETATM 4562 O O     . HOH D 4 .   ? 18.42232  19.28060  13.71955  1.000 41.55710 ? 1064 HOH A O     1 
HETATM 4563 O O     . HOH D 4 .   ? -25.28582 6.38941   4.11919   1.000 42.81005 ? 1065 HOH A O     1 
HETATM 4564 O O     . HOH D 4 .   ? -18.48102 10.23834  -2.92216  1.000 45.09217 ? 1066 HOH A O     1 
HETATM 4565 O O     . HOH D 4 .   ? 20.50453  4.61595   14.56126  1.000 39.04025 ? 1067 HOH A O     1 
HETATM 4566 O O     . HOH D 4 .   ? 13.55027  9.86534   19.70957  1.000 33.95814 ? 1068 HOH A O     1 
HETATM 4567 O O     . HOH D 4 .   ? 11.64355  -3.94781  11.92417  1.000 50.50860 ? 1069 HOH A O     1 
HETATM 4568 O O     . HOH D 4 .   ? -24.79481 19.89249  19.76580  1.000 48.09797 ? 1070 HOH A O     1 
HETATM 4569 O O     . HOH D 4 .   ? -14.60973 -14.18473 11.19627  1.000 44.95534 ? 1071 HOH A O     1 
HETATM 4570 O O     . HOH D 4 .   ? 9.24537   23.19495  20.43953  1.000 45.34029 ? 1072 HOH A O     1 
HETATM 4571 O O     . HOH D 4 .   ? -29.79211 1.06062   -2.23223  1.000 51.53208 ? 1073 HOH A O     1 
HETATM 4572 O O     . HOH D 4 .   ? -12.453   20.174    -3.847    1.000 45.67358 ? 1074 HOH A O     1 
HETATM 4573 O O     . HOH D 4 .   ? 12.38629  0.64217   10.38860  1.000 42.13365 ? 1075 HOH A O     1 
HETATM 4574 O O     . HOH D 4 .   ? -25.43584 -8.86994  8.76706   1.000 37.25807 ? 1076 HOH A O     1 
HETATM 4575 O O     . HOH D 4 .   ? -11.81512 35.97808  12.92889  1.000 55.13013 ? 1077 HOH A O     1 
HETATM 4576 O O     . HOH D 4 .   ? -17.93326 -19.72241 1.90677   1.000 49.40588 ? 1078 HOH A O     1 
HETATM 4577 O O     . HOH D 4 .   ? -2.13153  30.95210  14.96370  1.000 39.24089 ? 1079 HOH A O     1 
HETATM 4578 O O     . HOH D 4 .   ? 3.800     -8.841    -2.363    1.000 43.83346 ? 1080 HOH A O     1 
HETATM 4579 O O     . HOH D 4 .   ? -6.34190  32.74302  26.55277  1.000 35.45533 ? 1081 HOH A O     1 
HETATM 4580 O O     . HOH D 4 .   ? 8.44111   6.61627   7.35351   1.000 42.78833 ? 1082 HOH A O     1 
HETATM 4581 O O     . HOH D 4 .   ? 2.40221   9.91747   5.85675   1.000 43.53935 ? 1083 HOH A O     1 
HETATM 4582 O O     . HOH D 4 .   ? -24.15270 -12.97560 9.31206   1.000 44.41341 ? 1084 HOH A O     1 
HETATM 4583 O O     . HOH D 4 .   ? -4.48761  1.76589   -13.30085 1.000 42.20933 ? 1085 HOH A O     1 
HETATM 4584 O O     . HOH D 4 .   ? -7.89011  33.94004  14.58591  1.000 44.93362 ? 1086 HOH A O     1 
HETATM 4585 O O     . HOH D 4 .   ? -17.42207 -19.12865 -0.37653  1.000 51.81721 ? 1087 HOH A O     1 
HETATM 4586 O O     . HOH D 4 .   ? -28.34885 -8.63171  4.65351   1.000 45.82315 ? 1088 HOH A O     1 
HETATM 4587 O O     . HOH D 4 .   ? -27.171   -4.730    -8.303    1.000 51.27397 ? 1089 HOH A O     1 
HETATM 4588 O O     . HOH D 4 .   ? -27.91495 -8.60525  7.10452   1.000 42.94494 ? 1090 HOH A O     1 
# 
