data_8YYF
# 
_entry.id   8YYF 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   8YYF         pdb_00008yyf 10.2210/pdb8yyf/pdb 
WWPDB D_1300046620 ?            ?                   
# 
_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       2025-02-12 
# 
_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                        8YYF 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-03 
_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              bgopal@iisc.ac.in 
_pdbx_contact_author.name_first         Balasubramanian 
_pdbx_contact_author.name_last          Gopal 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-9097-5052 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Singh, A.K.'    1 0000-0002-4415-5827 
'Chinnasamy, K.' 2 0000-0002-0300-5005 
'Gopal, B.'      3 0000-0001-9097-5052 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Biol.Chem. 
_citation.journal_id_ASTM           JBCHA3 
_citation.journal_id_CSD            0071 
_citation.journal_id_ISSN           1083-351X 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            301 
_citation.language                  ? 
_citation.page_first                108152 
_citation.page_last                 108152 
_citation.title                     'A physicochemical rationale for the varied catalytic efficiency in RNase J paralogues.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.jbc.2024.108152 
_citation.pdbx_database_id_PubMed   39742998 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Singh, A.K.'    1 ? 
primary 'Chinnasamy, K.' 2 ? 
primary 'Pahelkar, N.R.' 3 ? 
primary 'Gopal, B.'      4 ? 
# 
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 'Ribonuclease J 2' 64312.258 1   3.1.-.- H76A ? ? 
2 water   nat water              18.015    395 ?       ?    ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'RNase J2' 
# 
_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       
;MGSSHHHHHHSQDPMSLIKKKNKDIRIIPLGGVGEIAKNMYIVEVDDEMFMLDAGLMFPEDEMLGVDIVIPDIQYVIENK
ERLKGIFLTAGHEHAIGAVSYVLEQIDAPVYGSKLTIALVKEAMKARNIKKKVRYYTVNHDSIMRFKNVNVSFFNTTHSI
PDSLGVCIHTSYGSIVYTGEFKFDQSLHGHYAPDLKRMAEIGDEGVFALISDSTEAEKPGYNTPENIIEHHMYDAFAKVK
GRLIVSCYASNFVRIQQVLNIASQLNRKVSFLGRSLESSFNIARKMGYFDIPKDLLIPINEVENYPKNEVIIIATGMQGE
PVEALSQMARKKHKIMNIEEGDSIFLAITASANMEVIIADTLNELVRAGAHIIPNNKKIHASSHGCMEELKMMLNIMKPE
YFVPVQGEFKMQIAHAKLAAETGVAPEKIFLVEKGDVISYNGKDMILNEKVQSGNILIDGIGVGDVGNIVLRDRHLLAED
GIFIAVVTLDPKNRRIAAGPEIQSRGFVYVRESEELLKEAEEKVRKIVEEGLQEKRIEWSEIKQNMRDQISKLLFESTKR
RPMIIPVISEI
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGSSHHHHHHSQDPMSLIKKKNKDIRIIPLGGVGEIAKNMYIVEVDDEMFMLDAGLMFPEDEMLGVDIVIPDIQYVIENK
ERLKGIFLTAGHEHAIGAVSYVLEQIDAPVYGSKLTIALVKEAMKARNIKKKVRYYTVNHDSIMRFKNVNVSFFNTTHSI
PDSLGVCIHTSYGSIVYTGEFKFDQSLHGHYAPDLKRMAEIGDEGVFALISDSTEAEKPGYNTPENIIEHHMYDAFAKVK
GRLIVSCYASNFVRIQQVLNIASQLNRKVSFLGRSLESSFNIARKMGYFDIPKDLLIPINEVENYPKNEVIIIATGMQGE
PVEALSQMARKKHKIMNIEEGDSIFLAITASANMEVIIADTLNELVRAGAHIIPNNKKIHASSHGCMEELKMMLNIMKPE
YFVPVQGEFKMQIAHAKLAAETGVAPEKIFLVEKGDVISYNGKDMILNEKVQSGNILIDGIGVGDVGNIVLRDRHLLAED
GIFIAVVTLDPKNRRIAAGPEIQSRGFVYVRESEELLKEAEEKVRKIVEEGLQEKRIEWSEIKQNMRDQISKLLFESTKR
RPMIIPVISEI
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     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   GLY n 
1 3   SER n 
1 4   SER n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   HIS n 
1 10  HIS n 
1 11  SER n 
1 12  GLN n 
1 13  ASP n 
1 14  PRO n 
1 15  MET n 
1 16  SER n 
1 17  LEU n 
1 18  ILE n 
1 19  LYS n 
1 20  LYS n 
1 21  LYS n 
1 22  ASN n 
1 23  LYS n 
1 24  ASP n 
1 25  ILE n 
1 26  ARG n 
1 27  ILE n 
1 28  ILE n 
1 29  PRO n 
1 30  LEU n 
1 31  GLY n 
1 32  GLY n 
1 33  VAL n 
1 34  GLY n 
1 35  GLU n 
1 36  ILE n 
1 37  ALA n 
1 38  LYS n 
1 39  ASN n 
1 40  MET n 
1 41  TYR n 
1 42  ILE n 
1 43  VAL n 
1 44  GLU n 
1 45  VAL n 
1 46  ASP n 
1 47  ASP n 
1 48  GLU n 
1 49  MET n 
1 50  PHE n 
1 51  MET n 
1 52  LEU n 
1 53  ASP n 
1 54  ALA n 
1 55  GLY n 
1 56  LEU n 
1 57  MET n 
1 58  PHE n 
1 59  PRO n 
1 60  GLU n 
1 61  ASP n 
1 62  GLU n 
1 63  MET n 
1 64  LEU n 
1 65  GLY n 
1 66  VAL n 
1 67  ASP n 
1 68  ILE n 
1 69  VAL n 
1 70  ILE n 
1 71  PRO n 
1 72  ASP n 
1 73  ILE n 
1 74  GLN n 
1 75  TYR n 
1 76  VAL n 
1 77  ILE n 
1 78  GLU n 
1 79  ASN n 
1 80  LYS n 
1 81  GLU n 
1 82  ARG n 
1 83  LEU n 
1 84  LYS n 
1 85  GLY n 
1 86  ILE n 
1 87  PHE n 
1 88  LEU n 
1 89  THR n 
1 90  ALA n 
1 91  GLY n 
1 92  HIS n 
1 93  GLU n 
1 94  HIS n 
1 95  ALA n 
1 96  ILE n 
1 97  GLY n 
1 98  ALA n 
1 99  VAL n 
1 100 SER n 
1 101 TYR n 
1 102 VAL n 
1 103 LEU n 
1 104 GLU n 
1 105 GLN n 
1 106 ILE n 
1 107 ASP n 
1 108 ALA n 
1 109 PRO n 
1 110 VAL n 
1 111 TYR n 
1 112 GLY n 
1 113 SER n 
1 114 LYS n 
1 115 LEU n 
1 116 THR n 
1 117 ILE n 
1 118 ALA n 
1 119 LEU n 
1 120 VAL n 
1 121 LYS n 
1 122 GLU n 
1 123 ALA n 
1 124 MET n 
1 125 LYS n 
1 126 ALA n 
1 127 ARG n 
1 128 ASN n 
1 129 ILE n 
1 130 LYS n 
1 131 LYS n 
1 132 LYS n 
1 133 VAL n 
1 134 ARG n 
1 135 TYR n 
1 136 TYR n 
1 137 THR n 
1 138 VAL n 
1 139 ASN n 
1 140 HIS n 
1 141 ASP n 
1 142 SER n 
1 143 ILE n 
1 144 MET n 
1 145 ARG n 
1 146 PHE n 
1 147 LYS n 
1 148 ASN n 
1 149 VAL n 
1 150 ASN n 
1 151 VAL n 
1 152 SER n 
1 153 PHE n 
1 154 PHE n 
1 155 ASN n 
1 156 THR n 
1 157 THR n 
1 158 HIS n 
1 159 SER n 
1 160 ILE n 
1 161 PRO n 
1 162 ASP n 
1 163 SER n 
1 164 LEU n 
1 165 GLY n 
1 166 VAL n 
1 167 CYS n 
1 168 ILE n 
1 169 HIS n 
1 170 THR n 
1 171 SER n 
1 172 TYR n 
1 173 GLY n 
1 174 SER n 
1 175 ILE n 
1 176 VAL n 
1 177 TYR n 
1 178 THR n 
1 179 GLY n 
1 180 GLU n 
1 181 PHE n 
1 182 LYS n 
1 183 PHE n 
1 184 ASP n 
1 185 GLN n 
1 186 SER n 
1 187 LEU n 
1 188 HIS n 
1 189 GLY n 
1 190 HIS n 
1 191 TYR n 
1 192 ALA n 
1 193 PRO n 
1 194 ASP n 
1 195 LEU n 
1 196 LYS n 
1 197 ARG n 
1 198 MET n 
1 199 ALA n 
1 200 GLU n 
1 201 ILE n 
1 202 GLY n 
1 203 ASP n 
1 204 GLU n 
1 205 GLY n 
1 206 VAL n 
1 207 PHE n 
1 208 ALA n 
1 209 LEU n 
1 210 ILE n 
1 211 SER n 
1 212 ASP n 
1 213 SER n 
1 214 THR n 
1 215 GLU n 
1 216 ALA n 
1 217 GLU n 
1 218 LYS n 
1 219 PRO n 
1 220 GLY n 
1 221 TYR n 
1 222 ASN n 
1 223 THR n 
1 224 PRO n 
1 225 GLU n 
1 226 ASN n 
1 227 ILE n 
1 228 ILE n 
1 229 GLU n 
1 230 HIS n 
1 231 HIS n 
1 232 MET n 
1 233 TYR n 
1 234 ASP n 
1 235 ALA n 
1 236 PHE n 
1 237 ALA n 
1 238 LYS n 
1 239 VAL n 
1 240 LYS n 
1 241 GLY n 
1 242 ARG n 
1 243 LEU n 
1 244 ILE n 
1 245 VAL n 
1 246 SER n 
1 247 CYS n 
1 248 TYR n 
1 249 ALA n 
1 250 SER n 
1 251 ASN n 
1 252 PHE n 
1 253 VAL n 
1 254 ARG n 
1 255 ILE n 
1 256 GLN n 
1 257 GLN n 
1 258 VAL n 
1 259 LEU n 
1 260 ASN n 
1 261 ILE n 
1 262 ALA n 
1 263 SER n 
1 264 GLN n 
1 265 LEU n 
1 266 ASN n 
1 267 ARG n 
1 268 LYS n 
1 269 VAL n 
1 270 SER n 
1 271 PHE n 
1 272 LEU n 
1 273 GLY n 
1 274 ARG n 
1 275 SER n 
1 276 LEU n 
1 277 GLU n 
1 278 SER n 
1 279 SER n 
1 280 PHE n 
1 281 ASN n 
1 282 ILE n 
1 283 ALA n 
1 284 ARG n 
1 285 LYS n 
1 286 MET n 
1 287 GLY n 
1 288 TYR n 
1 289 PHE n 
1 290 ASP n 
1 291 ILE n 
1 292 PRO n 
1 293 LYS n 
1 294 ASP n 
1 295 LEU n 
1 296 LEU n 
1 297 ILE n 
1 298 PRO n 
1 299 ILE n 
1 300 ASN n 
1 301 GLU n 
1 302 VAL n 
1 303 GLU n 
1 304 ASN n 
1 305 TYR n 
1 306 PRO n 
1 307 LYS n 
1 308 ASN n 
1 309 GLU n 
1 310 VAL n 
1 311 ILE n 
1 312 ILE n 
1 313 ILE n 
1 314 ALA n 
1 315 THR n 
1 316 GLY n 
1 317 MET n 
1 318 GLN n 
1 319 GLY n 
1 320 GLU n 
1 321 PRO n 
1 322 VAL n 
1 323 GLU n 
1 324 ALA n 
1 325 LEU n 
1 326 SER n 
1 327 GLN n 
1 328 MET n 
1 329 ALA n 
1 330 ARG n 
1 331 LYS n 
1 332 LYS n 
1 333 HIS n 
1 334 LYS n 
1 335 ILE n 
1 336 MET n 
1 337 ASN n 
1 338 ILE n 
1 339 GLU n 
1 340 GLU n 
1 341 GLY n 
1 342 ASP n 
1 343 SER n 
1 344 ILE n 
1 345 PHE n 
1 346 LEU n 
1 347 ALA n 
1 348 ILE n 
1 349 THR n 
1 350 ALA n 
1 351 SER n 
1 352 ALA n 
1 353 ASN n 
1 354 MET n 
1 355 GLU n 
1 356 VAL n 
1 357 ILE n 
1 358 ILE n 
1 359 ALA n 
1 360 ASP n 
1 361 THR n 
1 362 LEU n 
1 363 ASN n 
1 364 GLU n 
1 365 LEU n 
1 366 VAL n 
1 367 ARG n 
1 368 ALA n 
1 369 GLY n 
1 370 ALA n 
1 371 HIS n 
1 372 ILE n 
1 373 ILE n 
1 374 PRO n 
1 375 ASN n 
1 376 ASN n 
1 377 LYS n 
1 378 LYS n 
1 379 ILE n 
1 380 HIS n 
1 381 ALA n 
1 382 SER n 
1 383 SER n 
1 384 HIS n 
1 385 GLY n 
1 386 CYS n 
1 387 MET n 
1 388 GLU n 
1 389 GLU n 
1 390 LEU n 
1 391 LYS n 
1 392 MET n 
1 393 MET n 
1 394 LEU n 
1 395 ASN n 
1 396 ILE n 
1 397 MET n 
1 398 LYS n 
1 399 PRO n 
1 400 GLU n 
1 401 TYR n 
1 402 PHE n 
1 403 VAL n 
1 404 PRO n 
1 405 VAL n 
1 406 GLN n 
1 407 GLY n 
1 408 GLU n 
1 409 PHE n 
1 410 LYS n 
1 411 MET n 
1 412 GLN n 
1 413 ILE n 
1 414 ALA n 
1 415 HIS n 
1 416 ALA n 
1 417 LYS n 
1 418 LEU n 
1 419 ALA n 
1 420 ALA n 
1 421 GLU n 
1 422 THR n 
1 423 GLY n 
1 424 VAL n 
1 425 ALA n 
1 426 PRO n 
1 427 GLU n 
1 428 LYS n 
1 429 ILE n 
1 430 PHE n 
1 431 LEU n 
1 432 VAL n 
1 433 GLU n 
1 434 LYS n 
1 435 GLY n 
1 436 ASP n 
1 437 VAL n 
1 438 ILE n 
1 439 SER n 
1 440 TYR n 
1 441 ASN n 
1 442 GLY n 
1 443 LYS n 
1 444 ASP n 
1 445 MET n 
1 446 ILE n 
1 447 LEU n 
1 448 ASN n 
1 449 GLU n 
1 450 LYS n 
1 451 VAL n 
1 452 GLN n 
1 453 SER n 
1 454 GLY n 
1 455 ASN n 
1 456 ILE n 
1 457 LEU n 
1 458 ILE n 
1 459 ASP n 
1 460 GLY n 
1 461 ILE n 
1 462 GLY n 
1 463 VAL n 
1 464 GLY n 
1 465 ASP n 
1 466 VAL n 
1 467 GLY n 
1 468 ASN n 
1 469 ILE n 
1 470 VAL n 
1 471 LEU n 
1 472 ARG n 
1 473 ASP n 
1 474 ARG n 
1 475 HIS n 
1 476 LEU n 
1 477 LEU n 
1 478 ALA n 
1 479 GLU n 
1 480 ASP n 
1 481 GLY n 
1 482 ILE n 
1 483 PHE n 
1 484 ILE n 
1 485 ALA n 
1 486 VAL n 
1 487 VAL n 
1 488 THR n 
1 489 LEU n 
1 490 ASP n 
1 491 PRO n 
1 492 LYS n 
1 493 ASN n 
1 494 ARG n 
1 495 ARG n 
1 496 ILE n 
1 497 ALA n 
1 498 ALA n 
1 499 GLY n 
1 500 PRO n 
1 501 GLU n 
1 502 ILE n 
1 503 GLN n 
1 504 SER n 
1 505 ARG n 
1 506 GLY n 
1 507 PHE n 
1 508 VAL n 
1 509 TYR n 
1 510 VAL n 
1 511 ARG n 
1 512 GLU n 
1 513 SER n 
1 514 GLU n 
1 515 GLU n 
1 516 LEU n 
1 517 LEU n 
1 518 LYS n 
1 519 GLU n 
1 520 ALA n 
1 521 GLU n 
1 522 GLU n 
1 523 LYS n 
1 524 VAL n 
1 525 ARG n 
1 526 LYS n 
1 527 ILE n 
1 528 VAL n 
1 529 GLU n 
1 530 GLU n 
1 531 GLY n 
1 532 LEU n 
1 533 GLN n 
1 534 GLU n 
1 535 LYS n 
1 536 ARG n 
1 537 ILE n 
1 538 GLU n 
1 539 TRP n 
1 540 SER n 
1 541 GLU n 
1 542 ILE n 
1 543 LYS n 
1 544 GLN n 
1 545 ASN n 
1 546 MET n 
1 547 ARG n 
1 548 ASP n 
1 549 GLN n 
1 550 ILE n 
1 551 SER n 
1 552 LYS n 
1 553 LEU n 
1 554 LEU n 
1 555 PHE n 
1 556 GLU n 
1 557 SER n 
1 558 THR n 
1 559 LYS n 
1 560 ARG n 
1 561 ARG n 
1 562 PRO n 
1 563 MET n 
1 564 ILE n 
1 565 ILE n 
1 566 PRO n 
1 567 VAL n 
1 568 ILE n 
1 569 SER n 
1 570 GLU n 
1 571 ILE 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                   571 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'rnj2, SERP0842' 
_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      'Staphylococcus aureus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1280 
_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 
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 
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   -13 ?   ?   ?   A . n 
A 1 2   GLY 2   -12 ?   ?   ?   A . n 
A 1 3   SER 3   -11 ?   ?   ?   A . n 
A 1 4   SER 4   -10 ?   ?   ?   A . n 
A 1 5   HIS 5   -9  ?   ?   ?   A . n 
A 1 6   HIS 6   -8  ?   ?   ?   A . n 
A 1 7   HIS 7   -7  ?   ?   ?   A . n 
A 1 8   HIS 8   -6  ?   ?   ?   A . n 
A 1 9   HIS 9   -5  ?   ?   ?   A . n 
A 1 10  HIS 10  -4  ?   ?   ?   A . n 
A 1 11  SER 11  -3  ?   ?   ?   A . n 
A 1 12  GLN 12  -2  ?   ?   ?   A . n 
A 1 13  ASP 13  -1  ?   ?   ?   A . n 
A 1 14  PRO 14  0   ?   ?   ?   A . n 
A 1 15  MET 15  1   ?   ?   ?   A . n 
A 1 16  SER 16  2   ?   ?   ?   A . n 
A 1 17  LEU 17  3   3   LEU LEU A . n 
A 1 18  ILE 18  4   4   ILE ILE A . n 
A 1 19  LYS 19  5   5   LYS LYS A . n 
A 1 20  LYS 20  6   6   LYS LYS A . n 
A 1 21  LYS 21  7   7   LYS LYS A . n 
A 1 22  ASN 22  8   8   ASN ASN A . n 
A 1 23  LYS 23  9   9   LYS LYS A . n 
A 1 24  ASP 24  10  10  ASP ASP A . n 
A 1 25  ILE 25  11  11  ILE ILE A . n 
A 1 26  ARG 26  12  12  ARG ARG A . n 
A 1 27  ILE 27  13  13  ILE ILE A . n 
A 1 28  ILE 28  14  14  ILE ILE A . n 
A 1 29  PRO 29  15  15  PRO PRO A . n 
A 1 30  LEU 30  16  16  LEU LEU A . n 
A 1 31  GLY 31  17  17  GLY GLY A . n 
A 1 32  GLY 32  18  18  GLY GLY A . n 
A 1 33  VAL 33  19  19  VAL VAL A . n 
A 1 34  GLY 34  20  20  GLY GLY A . n 
A 1 35  GLU 35  21  21  GLU GLU A . n 
A 1 36  ILE 36  22  22  ILE ILE A . n 
A 1 37  ALA 37  23  23  ALA ALA A . n 
A 1 38  LYS 38  24  24  LYS LYS A . n 
A 1 39  ASN 39  25  25  ASN ASN A . n 
A 1 40  MET 40  26  26  MET MET A . n 
A 1 41  TYR 41  27  27  TYR TYR A . n 
A 1 42  ILE 42  28  28  ILE ILE A . n 
A 1 43  VAL 43  29  29  VAL VAL A . n 
A 1 44  GLU 44  30  30  GLU GLU A . n 
A 1 45  VAL 45  31  31  VAL VAL A . n 
A 1 46  ASP 46  32  32  ASP ASP A . n 
A 1 47  ASP 47  33  33  ASP ASP A . n 
A 1 48  GLU 48  34  34  GLU GLU A . n 
A 1 49  MET 49  35  35  MET MET A . n 
A 1 50  PHE 50  36  36  PHE PHE A . n 
A 1 51  MET 51  37  37  MET MET A . n 
A 1 52  LEU 52  38  38  LEU LEU A . n 
A 1 53  ASP 53  39  39  ASP ASP A . n 
A 1 54  ALA 54  40  40  ALA ALA A . n 
A 1 55  GLY 55  41  41  GLY GLY A . n 
A 1 56  LEU 56  42  42  LEU LEU A . n 
A 1 57  MET 57  43  43  MET MET A . n 
A 1 58  PHE 58  44  44  PHE PHE A . n 
A 1 59  PRO 59  45  45  PRO PRO A . n 
A 1 60  GLU 60  46  46  GLU GLU A . n 
A 1 61  ASP 61  47  47  ASP ASP A . n 
A 1 62  GLU 62  48  48  GLU GLU A . n 
A 1 63  MET 63  49  49  MET MET A . n 
A 1 64  LEU 64  50  50  LEU LEU A . n 
A 1 65  GLY 65  51  51  GLY GLY A . n 
A 1 66  VAL 66  52  52  VAL VAL A . n 
A 1 67  ASP 67  53  53  ASP ASP A . n 
A 1 68  ILE 68  54  54  ILE ILE A . n 
A 1 69  VAL 69  55  55  VAL VAL A . n 
A 1 70  ILE 70  56  56  ILE ILE A . n 
A 1 71  PRO 71  57  57  PRO PRO A . n 
A 1 72  ASP 72  58  58  ASP ASP A . n 
A 1 73  ILE 73  59  59  ILE ILE A . n 
A 1 74  GLN 74  60  60  GLN GLN A . n 
A 1 75  TYR 75  61  61  TYR TYR A . n 
A 1 76  VAL 76  62  62  VAL VAL A . n 
A 1 77  ILE 77  63  63  ILE ILE A . n 
A 1 78  GLU 78  64  64  GLU GLU A . n 
A 1 79  ASN 79  65  65  ASN ASN A . n 
A 1 80  LYS 80  66  66  LYS LYS A . n 
A 1 81  GLU 81  67  67  GLU GLU A . n 
A 1 82  ARG 82  68  68  ARG ARG A . n 
A 1 83  LEU 83  69  69  LEU LEU A . n 
A 1 84  LYS 84  70  70  LYS LYS A . n 
A 1 85  GLY 85  71  71  GLY GLY A . n 
A 1 86  ILE 86  72  72  ILE ILE A . n 
A 1 87  PHE 87  73  73  PHE PHE A . n 
A 1 88  LEU 88  74  74  LEU LEU A . n 
A 1 89  THR 89  75  75  THR THR A . n 
A 1 90  ALA 90  76  76  ALA ALA A . n 
A 1 91  GLY 91  77  77  GLY GLY A . n 
A 1 92  HIS 92  78  78  HIS HIS A . n 
A 1 93  GLU 93  79  79  GLU GLU A . n 
A 1 94  HIS 94  80  80  HIS HIS A . n 
A 1 95  ALA 95  81  81  ALA ALA A . n 
A 1 96  ILE 96  82  82  ILE ILE A . n 
A 1 97  GLY 97  83  83  GLY GLY A . n 
A 1 98  ALA 98  84  84  ALA ALA A . n 
A 1 99  VAL 99  85  85  VAL VAL A . n 
A 1 100 SER 100 86  86  SER SER A . n 
A 1 101 TYR 101 87  87  TYR TYR A . n 
A 1 102 VAL 102 88  88  VAL VAL A . n 
A 1 103 LEU 103 89  89  LEU LEU A . n 
A 1 104 GLU 104 90  90  GLU GLU A . n 
A 1 105 GLN 105 91  91  GLN GLN A . n 
A 1 106 ILE 106 92  92  ILE ILE A . n 
A 1 107 ASP 107 93  93  ASP ASP A . n 
A 1 108 ALA 108 94  94  ALA ALA A . n 
A 1 109 PRO 109 95  95  PRO PRO A . n 
A 1 110 VAL 110 96  96  VAL VAL A . n 
A 1 111 TYR 111 97  97  TYR TYR A . n 
A 1 112 GLY 112 98  98  GLY GLY A . n 
A 1 113 SER 113 99  99  SER SER A . n 
A 1 114 LYS 114 100 100 LYS LYS A . n 
A 1 115 LEU 115 101 101 LEU LEU A . n 
A 1 116 THR 116 102 102 THR THR A . n 
A 1 117 ILE 117 103 103 ILE ILE A . n 
A 1 118 ALA 118 104 104 ALA ALA A . n 
A 1 119 LEU 119 105 105 LEU LEU A . n 
A 1 120 VAL 120 106 106 VAL VAL A . n 
A 1 121 LYS 121 107 107 LYS LYS A . n 
A 1 122 GLU 122 108 108 GLU GLU A . n 
A 1 123 ALA 123 109 109 ALA ALA A . n 
A 1 124 MET 124 110 110 MET MET A . n 
A 1 125 LYS 125 111 111 LYS LYS A . n 
A 1 126 ALA 126 112 112 ALA ALA A . n 
A 1 127 ARG 127 113 113 ARG ARG A . n 
A 1 128 ASN 128 114 114 ASN ASN A . n 
A 1 129 ILE 129 115 115 ILE ILE A . n 
A 1 130 LYS 130 116 116 LYS LYS A . n 
A 1 131 LYS 131 117 117 LYS LYS A . n 
A 1 132 LYS 132 118 118 LYS LYS A . n 
A 1 133 VAL 133 119 119 VAL VAL A . n 
A 1 134 ARG 134 120 120 ARG ARG A . n 
A 1 135 TYR 135 121 121 TYR TYR A . n 
A 1 136 TYR 136 122 122 TYR TYR A . n 
A 1 137 THR 137 123 123 THR THR A . n 
A 1 138 VAL 138 124 124 VAL VAL A . n 
A 1 139 ASN 139 125 125 ASN ASN A . n 
A 1 140 HIS 140 126 126 HIS HIS A . n 
A 1 141 ASP 141 127 127 ASP ASP A . n 
A 1 142 SER 142 128 128 SER SER A . n 
A 1 143 ILE 143 129 129 ILE ILE A . n 
A 1 144 MET 144 130 130 MET MET A . n 
A 1 145 ARG 145 131 131 ARG ARG A . n 
A 1 146 PHE 146 132 132 PHE PHE A . n 
A 1 147 LYS 147 133 133 LYS LYS A . n 
A 1 148 ASN 148 134 134 ASN ASN A . n 
A 1 149 VAL 149 135 135 VAL VAL A . n 
A 1 150 ASN 150 136 136 ASN ASN A . n 
A 1 151 VAL 151 137 137 VAL VAL A . n 
A 1 152 SER 152 138 138 SER SER A . n 
A 1 153 PHE 153 139 139 PHE PHE A . n 
A 1 154 PHE 154 140 140 PHE PHE A . n 
A 1 155 ASN 155 141 141 ASN ASN A . n 
A 1 156 THR 156 142 142 THR THR A . n 
A 1 157 THR 157 143 143 THR THR A . n 
A 1 158 HIS 158 144 144 HIS HIS A . n 
A 1 159 SER 159 145 145 SER SER A . n 
A 1 160 ILE 160 146 146 ILE ILE A . n 
A 1 161 PRO 161 147 147 PRO PRO A . n 
A 1 162 ASP 162 148 148 ASP ASP A . n 
A 1 163 SER 163 149 149 SER SER A . n 
A 1 164 LEU 164 150 150 LEU LEU A . n 
A 1 165 GLY 165 151 151 GLY GLY A . n 
A 1 166 VAL 166 152 152 VAL VAL A . n 
A 1 167 CYS 167 153 153 CYS CYS A . n 
A 1 168 ILE 168 154 154 ILE ILE A . n 
A 1 169 HIS 169 155 155 HIS HIS A . n 
A 1 170 THR 170 156 156 THR THR A . n 
A 1 171 SER 171 157 157 SER SER A . n 
A 1 172 TYR 172 158 158 TYR TYR A . n 
A 1 173 GLY 173 159 159 GLY GLY A . n 
A 1 174 SER 174 160 160 SER SER A . n 
A 1 175 ILE 175 161 161 ILE ILE A . n 
A 1 176 VAL 176 162 162 VAL VAL A . n 
A 1 177 TYR 177 163 163 TYR TYR A . n 
A 1 178 THR 178 164 164 THR THR A . n 
A 1 179 GLY 179 165 165 GLY GLY A . n 
A 1 180 GLU 180 166 166 GLU GLU A . n 
A 1 181 PHE 181 167 167 PHE PHE A . n 
A 1 182 LYS 182 168 168 LYS LYS A . n 
A 1 183 PHE 183 169 169 PHE PHE A . n 
A 1 184 ASP 184 170 170 ASP ASP A . n 
A 1 185 GLN 185 171 171 GLN GLN A . n 
A 1 186 SER 186 172 172 SER SER A . n 
A 1 187 LEU 187 173 173 LEU LEU A . n 
A 1 188 HIS 188 174 174 HIS HIS A . n 
A 1 189 GLY 189 175 175 GLY GLY A . n 
A 1 190 HIS 190 176 176 HIS HIS A . n 
A 1 191 TYR 191 177 177 TYR TYR A . n 
A 1 192 ALA 192 178 178 ALA ALA A . n 
A 1 193 PRO 193 179 179 PRO PRO A . n 
A 1 194 ASP 194 180 180 ASP ASP A . n 
A 1 195 LEU 195 181 181 LEU LEU A . n 
A 1 196 LYS 196 182 182 LYS LYS A . n 
A 1 197 ARG 197 183 183 ARG ARG A . n 
A 1 198 MET 198 184 184 MET MET A . n 
A 1 199 ALA 199 185 185 ALA ALA A . n 
A 1 200 GLU 200 186 186 GLU GLU A . n 
A 1 201 ILE 201 187 187 ILE ILE A . n 
A 1 202 GLY 202 188 188 GLY GLY A . n 
A 1 203 ASP 203 189 189 ASP ASP A . n 
A 1 204 GLU 204 190 190 GLU GLU A . n 
A 1 205 GLY 205 191 191 GLY GLY A . n 
A 1 206 VAL 206 192 192 VAL VAL A . n 
A 1 207 PHE 207 193 193 PHE PHE A . n 
A 1 208 ALA 208 194 194 ALA ALA A . n 
A 1 209 LEU 209 195 195 LEU LEU A . n 
A 1 210 ILE 210 196 196 ILE ILE A . n 
A 1 211 SER 211 197 197 SER SER A . n 
A 1 212 ASP 212 198 198 ASP ASP A . n 
A 1 213 SER 213 199 199 SER SER A . n 
A 1 214 THR 214 200 200 THR THR A . n 
A 1 215 GLU 215 201 201 GLU GLU A . n 
A 1 216 ALA 216 202 202 ALA ALA A . n 
A 1 217 GLU 217 203 203 GLU GLU A . n 
A 1 218 LYS 218 204 204 LYS LYS A . n 
A 1 219 PRO 219 205 205 PRO PRO A . n 
A 1 220 GLY 220 206 206 GLY GLY A . n 
A 1 221 TYR 221 207 207 TYR TYR A . n 
A 1 222 ASN 222 208 208 ASN ASN A . n 
A 1 223 THR 223 209 209 THR THR A . n 
A 1 224 PRO 224 210 210 PRO PRO A . n 
A 1 225 GLU 225 211 211 GLU GLU A . n 
A 1 226 ASN 226 212 212 ASN ASN A . n 
A 1 227 ILE 227 213 213 ILE ILE A . n 
A 1 228 ILE 228 214 214 ILE ILE A . n 
A 1 229 GLU 229 215 215 GLU GLU A . n 
A 1 230 HIS 230 216 216 HIS HIS A . n 
A 1 231 HIS 231 217 217 HIS HIS A . n 
A 1 232 MET 232 218 218 MET MET A . n 
A 1 233 TYR 233 219 219 TYR TYR A . n 
A 1 234 ASP 234 220 220 ASP ASP A . n 
A 1 235 ALA 235 221 221 ALA ALA A . n 
A 1 236 PHE 236 222 222 PHE PHE A . n 
A 1 237 ALA 237 223 223 ALA ALA A . n 
A 1 238 LYS 238 224 224 LYS LYS A . n 
A 1 239 VAL 239 225 225 VAL VAL A . n 
A 1 240 LYS 240 226 226 LYS LYS A . n 
A 1 241 GLY 241 227 227 GLY GLY A . n 
A 1 242 ARG 242 228 228 ARG ARG A . n 
A 1 243 LEU 243 229 229 LEU LEU A . n 
A 1 244 ILE 244 230 230 ILE ILE A . n 
A 1 245 VAL 245 231 231 VAL VAL A . n 
A 1 246 SER 246 232 232 SER SER A . n 
A 1 247 CYS 247 233 233 CYS CYS A . n 
A 1 248 TYR 248 234 234 TYR TYR A . n 
A 1 249 ALA 249 235 235 ALA ALA A . n 
A 1 250 SER 250 236 236 SER SER A . n 
A 1 251 ASN 251 237 237 ASN ASN A . n 
A 1 252 PHE 252 238 238 PHE PHE A . n 
A 1 253 VAL 253 239 239 VAL VAL A . n 
A 1 254 ARG 254 240 240 ARG ARG A . n 
A 1 255 ILE 255 241 241 ILE ILE A . n 
A 1 256 GLN 256 242 242 GLN GLN A . n 
A 1 257 GLN 257 243 243 GLN GLN A . n 
A 1 258 VAL 258 244 244 VAL VAL A . n 
A 1 259 LEU 259 245 245 LEU LEU A . n 
A 1 260 ASN 260 246 246 ASN ASN A . n 
A 1 261 ILE 261 247 247 ILE ILE A . n 
A 1 262 ALA 262 248 248 ALA ALA A . n 
A 1 263 SER 263 249 249 SER SER A . n 
A 1 264 GLN 264 250 250 GLN GLN A . n 
A 1 265 LEU 265 251 251 LEU LEU A . n 
A 1 266 ASN 266 252 252 ASN ASN A . n 
A 1 267 ARG 267 253 253 ARG ARG A . n 
A 1 268 LYS 268 254 254 LYS LYS A . n 
A 1 269 VAL 269 255 255 VAL VAL A . n 
A 1 270 SER 270 256 256 SER SER A . n 
A 1 271 PHE 271 257 257 PHE PHE A . n 
A 1 272 LEU 272 258 258 LEU LEU A . n 
A 1 273 GLY 273 259 259 GLY GLY A . n 
A 1 274 ARG 274 260 260 ARG ARG A . n 
A 1 275 SER 275 261 261 SER SER A . n 
A 1 276 LEU 276 262 262 LEU LEU A . n 
A 1 277 GLU 277 263 263 GLU GLU A . n 
A 1 278 SER 278 264 264 SER SER A . n 
A 1 279 SER 279 265 265 SER SER A . n 
A 1 280 PHE 280 266 266 PHE PHE A . n 
A 1 281 ASN 281 267 267 ASN ASN A . n 
A 1 282 ILE 282 268 268 ILE ILE A . n 
A 1 283 ALA 283 269 269 ALA ALA A . n 
A 1 284 ARG 284 270 270 ARG ARG A . n 
A 1 285 LYS 285 271 271 LYS LYS A . n 
A 1 286 MET 286 272 272 MET MET A . n 
A 1 287 GLY 287 273 273 GLY GLY A . n 
A 1 288 TYR 288 274 274 TYR TYR A . n 
A 1 289 PHE 289 275 275 PHE PHE A . n 
A 1 290 ASP 290 276 276 ASP ASP A . n 
A 1 291 ILE 291 277 277 ILE ILE A . n 
A 1 292 PRO 292 278 278 PRO PRO A . n 
A 1 293 LYS 293 279 279 LYS LYS A . n 
A 1 294 ASP 294 280 280 ASP ASP A . n 
A 1 295 LEU 295 281 281 LEU LEU A . n 
A 1 296 LEU 296 282 282 LEU LEU A . n 
A 1 297 ILE 297 283 283 ILE ILE A . n 
A 1 298 PRO 298 284 284 PRO PRO A . n 
A 1 299 ILE 299 285 285 ILE ILE A . n 
A 1 300 ASN 300 286 286 ASN ASN A . n 
A 1 301 GLU 301 287 287 GLU GLU A . n 
A 1 302 VAL 302 288 288 VAL VAL A . n 
A 1 303 GLU 303 289 289 GLU GLU A . n 
A 1 304 ASN 304 290 290 ASN ASN A . n 
A 1 305 TYR 305 291 291 TYR TYR A . n 
A 1 306 PRO 306 292 292 PRO PRO A . n 
A 1 307 LYS 307 293 293 LYS LYS A . n 
A 1 308 ASN 308 294 294 ASN ASN A . n 
A 1 309 GLU 309 295 295 GLU GLU A . n 
A 1 310 VAL 310 296 296 VAL VAL A . n 
A 1 311 ILE 311 297 297 ILE ILE A . n 
A 1 312 ILE 312 298 298 ILE ILE A . n 
A 1 313 ILE 313 299 299 ILE ILE A . n 
A 1 314 ALA 314 300 300 ALA ALA A . n 
A 1 315 THR 315 301 301 THR THR A . n 
A 1 316 GLY 316 302 302 GLY GLY A . n 
A 1 317 MET 317 303 303 MET MET A . n 
A 1 318 GLN 318 304 304 GLN GLN A . n 
A 1 319 GLY 319 305 305 GLY GLY A . n 
A 1 320 GLU 320 306 306 GLU GLU A . n 
A 1 321 PRO 321 307 307 PRO PRO A . n 
A 1 322 VAL 322 308 308 VAL VAL A . n 
A 1 323 GLU 323 309 309 GLU GLU A . n 
A 1 324 ALA 324 310 310 ALA ALA A . n 
A 1 325 LEU 325 311 311 LEU LEU A . n 
A 1 326 SER 326 312 312 SER SER A . n 
A 1 327 GLN 327 313 313 GLN GLN A . n 
A 1 328 MET 328 314 314 MET MET A . n 
A 1 329 ALA 329 315 315 ALA ALA A . n 
A 1 330 ARG 330 316 316 ARG ARG A . n 
A 1 331 LYS 331 317 317 LYS LYS A . n 
A 1 332 LYS 332 318 318 LYS LYS A . n 
A 1 333 HIS 333 319 319 HIS HIS A . n 
A 1 334 LYS 334 320 320 LYS LYS A . n 
A 1 335 ILE 335 321 321 ILE ILE A . n 
A 1 336 MET 336 322 322 MET MET A . n 
A 1 337 ASN 337 323 323 ASN ASN A . n 
A 1 338 ILE 338 324 324 ILE ILE A . n 
A 1 339 GLU 339 325 325 GLU GLU A . n 
A 1 340 GLU 340 326 326 GLU GLU A . n 
A 1 341 GLY 341 327 327 GLY GLY A . n 
A 1 342 ASP 342 328 328 ASP ASP A . n 
A 1 343 SER 343 329 329 SER SER A . n 
A 1 344 ILE 344 330 330 ILE ILE A . n 
A 1 345 PHE 345 331 331 PHE PHE A . n 
A 1 346 LEU 346 332 332 LEU LEU A . n 
A 1 347 ALA 347 333 333 ALA ALA A . n 
A 1 348 ILE 348 334 334 ILE ILE A . n 
A 1 349 THR 349 335 ?   ?   ?   A . n 
A 1 350 ALA 350 336 336 ALA ALA A . n 
A 1 351 SER 351 337 337 SER SER A . n 
A 1 352 ALA 352 338 338 ALA ALA A . n 
A 1 353 ASN 353 339 339 ASN ASN A . n 
A 1 354 MET 354 340 340 MET MET A . n 
A 1 355 GLU 355 341 341 GLU GLU A . n 
A 1 356 VAL 356 342 342 VAL VAL A . n 
A 1 357 ILE 357 343 343 ILE ILE A . n 
A 1 358 ILE 358 344 344 ILE ILE A . n 
A 1 359 ALA 359 345 345 ALA ALA A . n 
A 1 360 ASP 360 346 346 ASP ASP A . n 
A 1 361 THR 361 347 347 THR THR A . n 
A 1 362 LEU 362 348 348 LEU LEU A . n 
A 1 363 ASN 363 349 349 ASN ASN A . n 
A 1 364 GLU 364 350 350 GLU GLU A . n 
A 1 365 LEU 365 351 351 LEU LEU A . n 
A 1 366 VAL 366 352 352 VAL VAL A . n 
A 1 367 ARG 367 353 353 ARG ARG A . n 
A 1 368 ALA 368 354 354 ALA ALA A . n 
A 1 369 GLY 369 355 355 GLY GLY A . n 
A 1 370 ALA 370 356 356 ALA ALA A . n 
A 1 371 HIS 371 357 357 HIS HIS A . n 
A 1 372 ILE 372 358 358 ILE ILE A . n 
A 1 373 ILE 373 359 359 ILE ILE A . n 
A 1 374 PRO 374 360 360 PRO PRO A . n 
A 1 375 ASN 375 361 361 ASN ASN A . n 
A 1 376 ASN 376 362 362 ASN ASN A . n 
A 1 377 LYS 377 363 363 LYS LYS A . n 
A 1 378 LYS 378 364 364 LYS LYS A . n 
A 1 379 ILE 379 365 365 ILE ILE A . n 
A 1 380 HIS 380 366 366 HIS HIS A . n 
A 1 381 ALA 381 367 367 ALA ALA A . n 
A 1 382 SER 382 368 368 SER SER A . n 
A 1 383 SER 383 369 369 SER SER A . n 
A 1 384 HIS 384 370 370 HIS HIS A . n 
A 1 385 GLY 385 371 371 GLY GLY A . n 
A 1 386 CYS 386 372 372 CYS CYS A . n 
A 1 387 MET 387 373 373 MET MET A . n 
A 1 388 GLU 388 374 374 GLU GLU A . n 
A 1 389 GLU 389 375 375 GLU GLU A . n 
A 1 390 LEU 390 376 376 LEU LEU A . n 
A 1 391 LYS 391 377 377 LYS LYS A . n 
A 1 392 MET 392 378 378 MET MET A . n 
A 1 393 MET 393 379 379 MET MET A . n 
A 1 394 LEU 394 380 380 LEU LEU A . n 
A 1 395 ASN 395 381 381 ASN ASN A . n 
A 1 396 ILE 396 382 382 ILE ILE A . n 
A 1 397 MET 397 383 383 MET MET A . n 
A 1 398 LYS 398 384 384 LYS LYS A . n 
A 1 399 PRO 399 385 385 PRO PRO A . n 
A 1 400 GLU 400 386 386 GLU GLU A . n 
A 1 401 TYR 401 387 387 TYR TYR A . n 
A 1 402 PHE 402 388 388 PHE PHE A . n 
A 1 403 VAL 403 389 389 VAL VAL A . n 
A 1 404 PRO 404 390 390 PRO PRO A . n 
A 1 405 VAL 405 391 391 VAL VAL A . n 
A 1 406 GLN 406 392 392 GLN GLN A . n 
A 1 407 GLY 407 393 393 GLY GLY A . n 
A 1 408 GLU 408 394 394 GLU GLU A . n 
A 1 409 PHE 409 395 395 PHE PHE A . n 
A 1 410 LYS 410 396 396 LYS LYS A . n 
A 1 411 MET 411 397 397 MET MET A . n 
A 1 412 GLN 412 398 398 GLN GLN A . n 
A 1 413 ILE 413 399 399 ILE ILE A . n 
A 1 414 ALA 414 400 400 ALA ALA A . n 
A 1 415 HIS 415 401 401 HIS HIS A . n 
A 1 416 ALA 416 402 402 ALA ALA A . n 
A 1 417 LYS 417 403 403 LYS LYS A . n 
A 1 418 LEU 418 404 404 LEU LEU A . n 
A 1 419 ALA 419 405 405 ALA ALA A . n 
A 1 420 ALA 420 406 406 ALA ALA A . n 
A 1 421 GLU 421 407 407 GLU GLU A . n 
A 1 422 THR 422 408 408 THR THR A . n 
A 1 423 GLY 423 409 409 GLY GLY A . n 
A 1 424 VAL 424 410 410 VAL VAL A . n 
A 1 425 ALA 425 411 411 ALA ALA A . n 
A 1 426 PRO 426 412 412 PRO PRO A . n 
A 1 427 GLU 427 413 413 GLU GLU A . n 
A 1 428 LYS 428 414 414 LYS LYS A . n 
A 1 429 ILE 429 415 415 ILE ILE A . n 
A 1 430 PHE 430 416 416 PHE PHE A . n 
A 1 431 LEU 431 417 417 LEU LEU A . n 
A 1 432 VAL 432 418 418 VAL VAL A . n 
A 1 433 GLU 433 419 419 GLU GLU A . n 
A 1 434 LYS 434 420 420 LYS LYS A . n 
A 1 435 GLY 435 421 421 GLY GLY A . n 
A 1 436 ASP 436 422 422 ASP ASP A . n 
A 1 437 VAL 437 423 423 VAL VAL A . n 
A 1 438 ILE 438 424 424 ILE ILE A . n 
A 1 439 SER 439 425 425 SER SER A . n 
A 1 440 TYR 440 426 426 TYR TYR A . n 
A 1 441 ASN 441 427 427 ASN ASN A . n 
A 1 442 GLY 442 428 428 GLY GLY A . n 
A 1 443 LYS 443 429 429 LYS LYS A . n 
A 1 444 ASP 444 430 430 ASP ASP A . n 
A 1 445 MET 445 431 431 MET MET A . n 
A 1 446 ILE 446 432 432 ILE ILE A . n 
A 1 447 LEU 447 433 433 LEU LEU A . n 
A 1 448 ASN 448 434 434 ASN ASN A . n 
A 1 449 GLU 449 435 435 GLU GLU A . n 
A 1 450 LYS 450 436 436 LYS LYS A . n 
A 1 451 VAL 451 437 437 VAL VAL A . n 
A 1 452 GLN 452 438 438 GLN GLN A . n 
A 1 453 SER 453 439 439 SER SER A . n 
A 1 454 GLY 454 440 440 GLY GLY A . n 
A 1 455 ASN 455 441 441 ASN ASN A . n 
A 1 456 ILE 456 442 442 ILE ILE A . n 
A 1 457 LEU 457 443 443 LEU LEU A . n 
A 1 458 ILE 458 444 444 ILE ILE A . n 
A 1 459 ASP 459 445 445 ASP ASP A . n 
A 1 460 GLY 460 446 ?   ?   ?   A . n 
A 1 461 ILE 461 447 ?   ?   ?   A . n 
A 1 462 GLY 462 448 ?   ?   ?   A . n 
A 1 463 VAL 463 449 ?   ?   ?   A . n 
A 1 464 GLY 464 450 ?   ?   ?   A . n 
A 1 465 ASP 465 451 ?   ?   ?   A . n 
A 1 466 VAL 466 452 ?   ?   ?   A . n 
A 1 467 GLY 467 453 ?   ?   ?   A . n 
A 1 468 ASN 468 454 ?   ?   ?   A . n 
A 1 469 ILE 469 455 ?   ?   ?   A . n 
A 1 470 VAL 470 456 ?   ?   ?   A . n 
A 1 471 LEU 471 457 ?   ?   ?   A . n 
A 1 472 ARG 472 458 ?   ?   ?   A . n 
A 1 473 ASP 473 459 ?   ?   ?   A . n 
A 1 474 ARG 474 460 ?   ?   ?   A . n 
A 1 475 HIS 475 461 ?   ?   ?   A . n 
A 1 476 LEU 476 462 ?   ?   ?   A . n 
A 1 477 LEU 477 463 ?   ?   ?   A . n 
A 1 478 ALA 478 464 ?   ?   ?   A . n 
A 1 479 GLU 479 465 ?   ?   ?   A . n 
A 1 480 ASP 480 466 ?   ?   ?   A . n 
A 1 481 GLY 481 467 ?   ?   ?   A . n 
A 1 482 ILE 482 468 ?   ?   ?   A . n 
A 1 483 PHE 483 469 ?   ?   ?   A . n 
A 1 484 ILE 484 470 ?   ?   ?   A . n 
A 1 485 ALA 485 471 ?   ?   ?   A . n 
A 1 486 VAL 486 472 ?   ?   ?   A . n 
A 1 487 VAL 487 473 ?   ?   ?   A . n 
A 1 488 THR 488 474 ?   ?   ?   A . n 
A 1 489 LEU 489 475 ?   ?   ?   A . n 
A 1 490 ASP 490 476 ?   ?   ?   A . n 
A 1 491 PRO 491 477 ?   ?   ?   A . n 
A 1 492 LYS 492 478 ?   ?   ?   A . n 
A 1 493 ASN 493 479 ?   ?   ?   A . n 
A 1 494 ARG 494 480 ?   ?   ?   A . n 
A 1 495 ARG 495 481 ?   ?   ?   A . n 
A 1 496 ILE 496 482 ?   ?   ?   A . n 
A 1 497 ALA 497 483 ?   ?   ?   A . n 
A 1 498 ALA 498 484 ?   ?   ?   A . n 
A 1 499 GLY 499 485 ?   ?   ?   A . n 
A 1 500 PRO 500 486 ?   ?   ?   A . n 
A 1 501 GLU 501 487 ?   ?   ?   A . n 
A 1 502 ILE 502 488 ?   ?   ?   A . n 
A 1 503 GLN 503 489 ?   ?   ?   A . n 
A 1 504 SER 504 490 ?   ?   ?   A . n 
A 1 505 ARG 505 491 ?   ?   ?   A . n 
A 1 506 GLY 506 492 ?   ?   ?   A . n 
A 1 507 PHE 507 493 ?   ?   ?   A . n 
A 1 508 VAL 508 494 ?   ?   ?   A . n 
A 1 509 TYR 509 495 ?   ?   ?   A . n 
A 1 510 VAL 510 496 ?   ?   ?   A . n 
A 1 511 ARG 511 497 ?   ?   ?   A . n 
A 1 512 GLU 512 498 ?   ?   ?   A . n 
A 1 513 SER 513 499 ?   ?   ?   A . n 
A 1 514 GLU 514 500 ?   ?   ?   A . n 
A 1 515 GLU 515 501 ?   ?   ?   A . n 
A 1 516 LEU 516 502 ?   ?   ?   A . n 
A 1 517 LEU 517 503 ?   ?   ?   A . n 
A 1 518 LYS 518 504 ?   ?   ?   A . n 
A 1 519 GLU 519 505 ?   ?   ?   A . n 
A 1 520 ALA 520 506 ?   ?   ?   A . n 
A 1 521 GLU 521 507 ?   ?   ?   A . n 
A 1 522 GLU 522 508 ?   ?   ?   A . n 
A 1 523 LYS 523 509 ?   ?   ?   A . n 
A 1 524 VAL 524 510 ?   ?   ?   A . n 
A 1 525 ARG 525 511 ?   ?   ?   A . n 
A 1 526 LYS 526 512 ?   ?   ?   A . n 
A 1 527 ILE 527 513 ?   ?   ?   A . n 
A 1 528 VAL 528 514 ?   ?   ?   A . n 
A 1 529 GLU 529 515 ?   ?   ?   A . n 
A 1 530 GLU 530 516 ?   ?   ?   A . n 
A 1 531 GLY 531 517 ?   ?   ?   A . n 
A 1 532 LEU 532 518 ?   ?   ?   A . n 
A 1 533 GLN 533 519 ?   ?   ?   A . n 
A 1 534 GLU 534 520 ?   ?   ?   A . n 
A 1 535 LYS 535 521 ?   ?   ?   A . n 
A 1 536 ARG 536 522 ?   ?   ?   A . n 
A 1 537 ILE 537 523 ?   ?   ?   A . n 
A 1 538 GLU 538 524 ?   ?   ?   A . n 
A 1 539 TRP 539 525 ?   ?   ?   A . n 
A 1 540 SER 540 526 ?   ?   ?   A . n 
A 1 541 GLU 541 527 ?   ?   ?   A . n 
A 1 542 ILE 542 528 ?   ?   ?   A . n 
A 1 543 LYS 543 529 ?   ?   ?   A . n 
A 1 544 GLN 544 530 ?   ?   ?   A . n 
A 1 545 ASN 545 531 ?   ?   ?   A . n 
A 1 546 MET 546 532 ?   ?   ?   A . n 
A 1 547 ARG 547 533 ?   ?   ?   A . n 
A 1 548 ASP 548 534 ?   ?   ?   A . n 
A 1 549 GLN 549 535 ?   ?   ?   A . n 
A 1 550 ILE 550 536 ?   ?   ?   A . n 
A 1 551 SER 551 537 ?   ?   ?   A . n 
A 1 552 LYS 552 538 ?   ?   ?   A . n 
A 1 553 LEU 553 539 ?   ?   ?   A . n 
A 1 554 LEU 554 540 ?   ?   ?   A . n 
A 1 555 PHE 555 541 ?   ?   ?   A . n 
A 1 556 GLU 556 542 ?   ?   ?   A . n 
A 1 557 SER 557 543 ?   ?   ?   A . n 
A 1 558 THR 558 544 ?   ?   ?   A . n 
A 1 559 LYS 559 545 ?   ?   ?   A . n 
A 1 560 ARG 560 546 ?   ?   ?   A . n 
A 1 561 ARG 561 547 ?   ?   ?   A . n 
A 1 562 PRO 562 548 ?   ?   ?   A . n 
A 1 563 MET 563 549 ?   ?   ?   A . n 
A 1 564 ILE 564 550 ?   ?   ?   A . n 
A 1 565 ILE 565 551 ?   ?   ?   A . n 
A 1 566 PRO 566 552 ?   ?   ?   A . n 
A 1 567 VAL 567 553 ?   ?   ?   A . n 
A 1 568 ILE 568 554 ?   ?   ?   A . n 
A 1 569 SER 569 555 ?   ?   ?   A . n 
A 1 570 GLU 570 556 ?   ?   ?   A . n 
A 1 571 ILE 571 557 ?   ?   ?   A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 HOH 1   601 84  HOH HOH A . 
B 2 HOH 2   602 78  HOH HOH A . 
B 2 HOH 3   603 86  HOH HOH A . 
B 2 HOH 4   604 78  HOH HOH A . 
B 2 HOH 5   605 162 HOH HOH A . 
B 2 HOH 6   606 103 HOH HOH A . 
B 2 HOH 7   607 120 HOH HOH A . 
B 2 HOH 8   608 66  HOH HOH A . 
B 2 HOH 9   609 250 HOH HOH A . 
B 2 HOH 10  610 105 HOH HOH A . 
B 2 HOH 11  611 3   HOH HOH A . 
B 2 HOH 12  612 377 HOH HOH A . 
B 2 HOH 13  613 347 HOH HOH A . 
B 2 HOH 14  614 121 HOH HOH A . 
B 2 HOH 15  615 5   HOH HOH A . 
B 2 HOH 16  616 80  HOH HOH A . 
B 2 HOH 17  617 124 HOH HOH A . 
B 2 HOH 18  618 213 HOH HOH A . 
B 2 HOH 19  619 30  HOH HOH A . 
B 2 HOH 20  620 124 HOH HOH A . 
B 2 HOH 21  621 111 HOH HOH A . 
B 2 HOH 22  622 51  HOH HOH A . 
B 2 HOH 23  623 88  HOH HOH A . 
B 2 HOH 24  624 60  HOH HOH A . 
B 2 HOH 25  625 101 HOH HOH A . 
B 2 HOH 26  626 52  HOH HOH A . 
B 2 HOH 27  627 28  HOH HOH A . 
B 2 HOH 28  628 77  HOH HOH A . 
B 2 HOH 29  629 136 HOH HOH A . 
B 2 HOH 30  630 19  HOH HOH A . 
B 2 HOH 31  631 148 HOH HOH A . 
B 2 HOH 32  632 80  HOH HOH A . 
B 2 HOH 33  633 363 HOH HOH A . 
B 2 HOH 34  634 107 HOH HOH A . 
B 2 HOH 35  635 573 HOH HOH A . 
B 2 HOH 36  636 128 HOH HOH A . 
B 2 HOH 37  637 4   HOH HOH A . 
B 2 HOH 38  638 46  HOH HOH A . 
B 2 HOH 39  639 57  HOH HOH A . 
B 2 HOH 40  640 11  HOH HOH A . 
B 2 HOH 41  641 13  HOH HOH A . 
B 2 HOH 42  642 197 HOH HOH A . 
B 2 HOH 43  643 61  HOH HOH A . 
B 2 HOH 44  644 232 HOH HOH A . 
B 2 HOH 45  645 277 HOH HOH A . 
B 2 HOH 46  646 40  HOH HOH A . 
B 2 HOH 47  647 14  HOH HOH A . 
B 2 HOH 48  648 326 HOH HOH A . 
B 2 HOH 49  649 189 HOH HOH A . 
B 2 HOH 50  650 334 HOH HOH A . 
B 2 HOH 51  651 10  HOH HOH A . 
B 2 HOH 52  652 23  HOH HOH A . 
B 2 HOH 53  653 94  HOH HOH A . 
B 2 HOH 54  654 301 HOH HOH A . 
B 2 HOH 55  655 18  HOH HOH A . 
B 2 HOH 56  656 139 HOH HOH A . 
B 2 HOH 57  657 125 HOH HOH A . 
B 2 HOH 58  658 65  HOH HOH A . 
B 2 HOH 59  659 122 HOH HOH A . 
B 2 HOH 60  660 174 HOH HOH A . 
B 2 HOH 61  661 114 HOH HOH A . 
B 2 HOH 62  662 253 HOH HOH A . 
B 2 HOH 63  663 56  HOH HOH A . 
B 2 HOH 64  664 69  HOH HOH A . 
B 2 HOH 65  665 106 HOH HOH A . 
B 2 HOH 66  666 45  HOH HOH A . 
B 2 HOH 67  667 156 HOH HOH A . 
B 2 HOH 68  668 54  HOH HOH A . 
B 2 HOH 69  669 75  HOH HOH A . 
B 2 HOH 70  670 34  HOH HOH A . 
B 2 HOH 71  671 2   HOH HOH A . 
B 2 HOH 72  672 91  HOH HOH A . 
B 2 HOH 73  673 14  HOH HOH A . 
B 2 HOH 74  674 158 HOH HOH A . 
B 2 HOH 75  675 119 HOH HOH A . 
B 2 HOH 76  676 258 HOH HOH A . 
B 2 HOH 77  677 16  HOH HOH A . 
B 2 HOH 78  678 29  HOH HOH A . 
B 2 HOH 79  679 65  HOH HOH A . 
B 2 HOH 80  680 97  HOH HOH A . 
B 2 HOH 81  681 12  HOH HOH A . 
B 2 HOH 82  682 133 HOH HOH A . 
B 2 HOH 83  683 72  HOH HOH A . 
B 2 HOH 84  684 117 HOH HOH A . 
B 2 HOH 85  685 238 HOH HOH A . 
B 2 HOH 86  686 79  HOH HOH A . 
B 2 HOH 87  687 41  HOH HOH A . 
B 2 HOH 88  688 44  HOH HOH A . 
B 2 HOH 89  689 46  HOH HOH A . 
B 2 HOH 90  690 130 HOH HOH A . 
B 2 HOH 91  691 210 HOH HOH A . 
B 2 HOH 92  692 1   HOH HOH A . 
B 2 HOH 93  693 82  HOH HOH A . 
B 2 HOH 94  694 108 HOH HOH A . 
B 2 HOH 95  695 29  HOH HOH A . 
B 2 HOH 96  696 36  HOH HOH A . 
B 2 HOH 97  697 252 HOH HOH A . 
B 2 HOH 98  698 237 HOH HOH A . 
B 2 HOH 99  699 47  HOH HOH A . 
B 2 HOH 100 700 21  HOH HOH A . 
B 2 HOH 101 701 39  HOH HOH A . 
B 2 HOH 102 702 59  HOH HOH A . 
B 2 HOH 103 703 19  HOH HOH A . 
B 2 HOH 104 704 66  HOH HOH A . 
B 2 HOH 105 705 192 HOH HOH A . 
B 2 HOH 106 706 312 HOH HOH A . 
B 2 HOH 107 707 85  HOH HOH A . 
B 2 HOH 108 708 151 HOH HOH A . 
B 2 HOH 109 709 48  HOH HOH A . 
B 2 HOH 110 710 42  HOH HOH A . 
B 2 HOH 111 711 155 HOH HOH A . 
B 2 HOH 112 712 37  HOH HOH A . 
B 2 HOH 113 713 63  HOH HOH A . 
B 2 HOH 114 714 214 HOH HOH A . 
B 2 HOH 115 715 121 HOH HOH A . 
B 2 HOH 116 716 51  HOH HOH A . 
B 2 HOH 117 717 240 HOH HOH A . 
B 2 HOH 118 718 33  HOH HOH A . 
B 2 HOH 119 719 89  HOH HOH A . 
B 2 HOH 120 720 8   HOH HOH A . 
B 2 HOH 121 721 464 HOH HOH A . 
B 2 HOH 122 722 15  HOH HOH A . 
B 2 HOH 123 723 266 HOH HOH A . 
B 2 HOH 124 724 62  HOH HOH A . 
B 2 HOH 125 725 57  HOH HOH A . 
B 2 HOH 126 726 146 HOH HOH A . 
B 2 HOH 127 727 138 HOH HOH A . 
B 2 HOH 128 728 204 HOH HOH A . 
B 2 HOH 129 729 422 HOH HOH A . 
B 2 HOH 130 730 140 HOH HOH A . 
B 2 HOH 131 731 39  HOH HOH A . 
B 2 HOH 132 732 47  HOH HOH A . 
B 2 HOH 133 733 15  HOH HOH A . 
B 2 HOH 134 734 61  HOH HOH A . 
B 2 HOH 135 735 27  HOH HOH A . 
B 2 HOH 136 736 218 HOH HOH A . 
B 2 HOH 137 737 1   HOH HOH A . 
B 2 HOH 138 738 101 HOH HOH A . 
B 2 HOH 139 739 167 HOH HOH A . 
B 2 HOH 140 740 206 HOH HOH A . 
B 2 HOH 141 741 34  HOH HOH A . 
B 2 HOH 142 742 68  HOH HOH A . 
B 2 HOH 143 743 7   HOH HOH A . 
B 2 HOH 144 744 76  HOH HOH A . 
B 2 HOH 145 745 8   HOH HOH A . 
B 2 HOH 146 746 63  HOH HOH A . 
B 2 HOH 147 747 282 HOH HOH A . 
B 2 HOH 148 748 116 HOH HOH A . 
B 2 HOH 149 749 87  HOH HOH A . 
B 2 HOH 150 750 62  HOH HOH A . 
B 2 HOH 151 751 64  HOH HOH A . 
B 2 HOH 152 752 38  HOH HOH A . 
B 2 HOH 153 753 103 HOH HOH A . 
B 2 HOH 154 754 166 HOH HOH A . 
B 2 HOH 155 755 115 HOH HOH A . 
B 2 HOH 156 756 127 HOH HOH A . 
B 2 HOH 157 757 43  HOH HOH A . 
B 2 HOH 158 758 24  HOH HOH A . 
B 2 HOH 159 759 11  HOH HOH A . 
B 2 HOH 160 760 31  HOH HOH A . 
B 2 HOH 161 761 263 HOH HOH A . 
B 2 HOH 162 762 123 HOH HOH A . 
B 2 HOH 163 763 257 HOH HOH A . 
B 2 HOH 164 764 4   HOH HOH A . 
B 2 HOH 165 765 112 HOH HOH A . 
B 2 HOH 166 766 90  HOH HOH A . 
B 2 HOH 167 767 507 HOH HOH A . 
B 2 HOH 168 768 525 HOH HOH A . 
B 2 HOH 169 769 188 HOH HOH A . 
B 2 HOH 170 770 9   HOH HOH A . 
B 2 HOH 171 771 233 HOH HOH A . 
B 2 HOH 172 772 123 HOH HOH A . 
B 2 HOH 173 773 50  HOH HOH A . 
B 2 HOH 174 774 56  HOH HOH A . 
B 2 HOH 175 775 209 HOH HOH A . 
B 2 HOH 176 776 77  HOH HOH A . 
B 2 HOH 177 777 345 HOH HOH A . 
B 2 HOH 178 778 10  HOH HOH A . 
B 2 HOH 179 779 22  HOH HOH A . 
B 2 HOH 180 780 359 HOH HOH A . 
B 2 HOH 181 781 13  HOH HOH A . 
B 2 HOH 182 782 6   HOH HOH A . 
B 2 HOH 183 783 2   HOH HOH A . 
B 2 HOH 184 784 25  HOH HOH A . 
B 2 HOH 185 785 127 HOH HOH A . 
B 2 HOH 186 786 6   HOH HOH A . 
B 2 HOH 187 787 28  HOH HOH A . 
B 2 HOH 188 788 73  HOH HOH A . 
B 2 HOH 189 789 64  HOH HOH A . 
B 2 HOH 190 790 249 HOH HOH A . 
B 2 HOH 191 791 159 HOH HOH A . 
B 2 HOH 192 792 96  HOH HOH A . 
B 2 HOH 193 793 87  HOH HOH A . 
B 2 HOH 194 794 122 HOH HOH A . 
B 2 HOH 195 795 49  HOH HOH A . 
B 2 HOH 196 796 42  HOH HOH A . 
B 2 HOH 197 797 234 HOH HOH A . 
B 2 HOH 198 798 153 HOH HOH A . 
B 2 HOH 199 799 199 HOH HOH A . 
B 2 HOH 200 800 3   HOH HOH A . 
B 2 HOH 201 801 281 HOH HOH A . 
B 2 HOH 202 802 18  HOH HOH A . 
B 2 HOH 203 803 248 HOH HOH A . 
B 2 HOH 204 804 298 HOH HOH A . 
B 2 HOH 205 805 17  HOH HOH A . 
B 2 HOH 206 806 286 HOH HOH A . 
B 2 HOH 207 807 571 HOH HOH A . 
B 2 HOH 208 808 246 HOH HOH A . 
B 2 HOH 209 809 83  HOH HOH A . 
B 2 HOH 210 810 44  HOH HOH A . 
B 2 HOH 211 811 88  HOH HOH A . 
B 2 HOH 212 812 170 HOH HOH A . 
B 2 HOH 213 813 32  HOH HOH A . 
B 2 HOH 214 814 108 HOH HOH A . 
B 2 HOH 215 815 36  HOH HOH A . 
B 2 HOH 216 816 99  HOH HOH A . 
B 2 HOH 217 817 26  HOH HOH A . 
B 2 HOH 218 818 12  HOH HOH A . 
B 2 HOH 219 819 41  HOH HOH A . 
B 2 HOH 220 820 134 HOH HOH A . 
B 2 HOH 221 821 24  HOH HOH A . 
B 2 HOH 222 822 268 HOH HOH A . 
B 2 HOH 223 823 92  HOH HOH A . 
B 2 HOH 224 824 102 HOH HOH A . 
B 2 HOH 225 825 16  HOH HOH A . 
B 2 HOH 226 826 7   HOH HOH A . 
B 2 HOH 227 827 95  HOH HOH A . 
B 2 HOH 228 828 458 HOH HOH A . 
B 2 HOH 229 829 71  HOH HOH A . 
B 2 HOH 230 830 50  HOH HOH A . 
B 2 HOH 231 831 224 HOH HOH A . 
B 2 HOH 232 832 70  HOH HOH A . 
B 2 HOH 233 833 256 HOH HOH A . 
B 2 HOH 234 834 74  HOH HOH A . 
B 2 HOH 235 835 119 HOH HOH A . 
B 2 HOH 236 836 384 HOH HOH A . 
B 2 HOH 237 837 38  HOH HOH A . 
B 2 HOH 238 838 58  HOH HOH A . 
B 2 HOH 239 839 67  HOH HOH A . 
B 2 HOH 240 840 131 HOH HOH A . 
B 2 HOH 241 841 221 HOH HOH A . 
B 2 HOH 242 842 215 HOH HOH A . 
B 2 HOH 243 843 144 HOH HOH A . 
B 2 HOH 244 844 69  HOH HOH A . 
B 2 HOH 245 845 43  HOH HOH A . 
B 2 HOH 246 846 68  HOH HOH A . 
B 2 HOH 247 847 110 HOH HOH A . 
B 2 HOH 248 848 272 HOH HOH A . 
B 2 HOH 249 849 85  HOH HOH A . 
B 2 HOH 250 850 55  HOH HOH A . 
B 2 HOH 251 851 427 HOH HOH A . 
B 2 HOH 252 852 143 HOH HOH A . 
B 2 HOH 253 853 27  HOH HOH A . 
B 2 HOH 254 854 132 HOH HOH A . 
B 2 HOH 255 855 288 HOH HOH A . 
B 2 HOH 256 856 23  HOH HOH A . 
B 2 HOH 257 857 84  HOH HOH A . 
B 2 HOH 258 858 404 HOH HOH A . 
B 2 HOH 259 859 104 HOH HOH A . 
B 2 HOH 260 860 79  HOH HOH A . 
B 2 HOH 261 861 33  HOH HOH A . 
B 2 HOH 262 862 186 HOH HOH A . 
B 2 HOH 263 863 20  HOH HOH A . 
B 2 HOH 264 864 225 HOH HOH A . 
B 2 HOH 265 865 157 HOH HOH A . 
B 2 HOH 266 866 125 HOH HOH A . 
B 2 HOH 267 867 55  HOH HOH A . 
B 2 HOH 268 868 54  HOH HOH A . 
B 2 HOH 269 869 354 HOH HOH A . 
B 2 HOH 270 870 306 HOH HOH A . 
B 2 HOH 271 871 74  HOH HOH A . 
B 2 HOH 272 872 107 HOH HOH A . 
B 2 HOH 273 873 49  HOH HOH A . 
B 2 HOH 274 874 289 HOH HOH A . 
B 2 HOH 275 875 21  HOH HOH A . 
B 2 HOH 276 876 202 HOH HOH A . 
B 2 HOH 277 877 259 HOH HOH A . 
B 2 HOH 278 878 169 HOH HOH A . 
B 2 HOH 279 879 9   HOH HOH A . 
B 2 HOH 280 880 58  HOH HOH A . 
B 2 HOH 281 881 184 HOH HOH A . 
B 2 HOH 282 882 239 HOH HOH A . 
B 2 HOH 283 883 205 HOH HOH A . 
B 2 HOH 284 884 223 HOH HOH A . 
B 2 HOH 285 885 59  HOH HOH A . 
B 2 HOH 286 886 5   HOH HOH A . 
B 2 HOH 287 887 86  HOH HOH A . 
B 2 HOH 288 888 117 HOH HOH A . 
B 2 HOH 289 889 70  HOH HOH A . 
B 2 HOH 290 890 72  HOH HOH A . 
B 2 HOH 291 891 109 HOH HOH A . 
B 2 HOH 292 892 524 HOH HOH A . 
B 2 HOH 293 893 73  HOH HOH A . 
B 2 HOH 294 894 187 HOH HOH A . 
B 2 HOH 295 895 385 HOH HOH A . 
B 2 HOH 296 896 242 HOH HOH A . 
B 2 HOH 297 897 126 HOH HOH A . 
B 2 HOH 298 898 383 HOH HOH A . 
B 2 HOH 299 899 91  HOH HOH A . 
B 2 HOH 300 900 40  HOH HOH A . 
B 2 HOH 301 901 71  HOH HOH A . 
B 2 HOH 302 902 126 HOH HOH A . 
B 2 HOH 303 903 113 HOH HOH A . 
B 2 HOH 304 904 530 HOH HOH A . 
B 2 HOH 305 905 83  HOH HOH A . 
B 2 HOH 306 906 518 HOH HOH A . 
B 2 HOH 307 907 93  HOH HOH A . 
B 2 HOH 308 908 292 HOH HOH A . 
B 2 HOH 309 909 175 HOH HOH A . 
B 2 HOH 310 910 452 HOH HOH A . 
B 2 HOH 311 911 145 HOH HOH A . 
B 2 HOH 312 912 98  HOH HOH A . 
B 2 HOH 313 913 94  HOH HOH A . 
B 2 HOH 314 914 269 HOH HOH A . 
B 2 HOH 315 915 76  HOH HOH A . 
B 2 HOH 316 916 230 HOH HOH A . 
B 2 HOH 317 917 229 HOH HOH A . 
B 2 HOH 318 918 523 HOH HOH A . 
B 2 HOH 319 919 318 HOH HOH A . 
B 2 HOH 320 920 104 HOH HOH A . 
B 2 HOH 321 921 137 HOH HOH A . 
B 2 HOH 322 922 141 HOH HOH A . 
B 2 HOH 323 923 504 HOH HOH A . 
B 2 HOH 324 924 294 HOH HOH A . 
B 2 HOH 325 925 111 HOH HOH A . 
B 2 HOH 326 926 508 HOH HOH A . 
B 2 HOH 327 927 194 HOH HOH A . 
B 2 HOH 328 928 514 HOH HOH A . 
B 2 HOH 329 929 177 HOH HOH A . 
B 2 HOH 330 930 67  HOH HOH A . 
B 2 HOH 331 931 543 HOH HOH A . 
B 2 HOH 332 932 198 HOH HOH A . 
B 2 HOH 333 933 283 HOH HOH A . 
B 2 HOH 334 934 208 HOH HOH A . 
B 2 HOH 335 935 147 HOH HOH A . 
B 2 HOH 336 936 152 HOH HOH A . 
B 2 HOH 337 937 100 HOH HOH A . 
B 2 HOH 338 938 494 HOH HOH A . 
B 2 HOH 339 939 115 HOH HOH A . 
B 2 HOH 340 940 522 HOH HOH A . 
B 2 HOH 341 941 99  HOH HOH A . 
B 2 HOH 342 942 37  HOH HOH A . 
B 2 HOH 343 943 251 HOH HOH A . 
B 2 HOH 344 944 112 HOH HOH A . 
B 2 HOH 345 945 243 HOH HOH A . 
B 2 HOH 346 946 502 HOH HOH A . 
B 2 HOH 347 947 32  HOH HOH A . 
B 2 HOH 348 948 109 HOH HOH A . 
B 2 HOH 349 949 241 HOH HOH A . 
B 2 HOH 350 950 53  HOH HOH A . 
B 2 HOH 351 951 81  HOH HOH A . 
B 2 HOH 352 952 542 HOH HOH A . 
B 2 HOH 353 953 372 HOH HOH A . 
B 2 HOH 354 954 419 HOH HOH A . 
B 2 HOH 355 955 580 HOH HOH A . 
B 2 HOH 356 956 106 HOH HOH A . 
B 2 HOH 357 957 149 HOH HOH A . 
B 2 HOH 358 958 424 HOH HOH A . 
B 2 HOH 359 959 191 HOH HOH A . 
B 2 HOH 360 960 90  HOH HOH A . 
B 2 HOH 361 961 497 HOH HOH A . 
B 2 HOH 362 962 200 HOH HOH A . 
B 2 HOH 363 963 190 HOH HOH A . 
B 2 HOH 364 964 434 HOH HOH A . 
B 2 HOH 365 965 35  HOH HOH A . 
B 2 HOH 366 966 181 HOH HOH A . 
B 2 HOH 367 967 498 HOH HOH A . 
B 2 HOH 368 968 118 HOH HOH A . 
B 2 HOH 369 969 172 HOH HOH A . 
B 2 HOH 370 970 178 HOH HOH A . 
B 2 HOH 371 971 521 HOH HOH A . 
B 2 HOH 372 972 285 HOH HOH A . 
B 2 HOH 373 973 165 HOH HOH A . 
B 2 HOH 374 974 526 HOH HOH A . 
B 2 HOH 375 975 203 HOH HOH A . 
B 2 HOH 376 976 89  HOH HOH A . 
B 2 HOH 377 977 113 HOH HOH A . 
B 2 HOH 378 978 572 HOH HOH A . 
B 2 HOH 379 979 30  HOH HOH A . 
B 2 HOH 380 980 183 HOH HOH A . 
B 2 HOH 381 981 307 HOH HOH A . 
B 2 HOH 382 982 352 HOH HOH A . 
B 2 HOH 383 983 142 HOH HOH A . 
B 2 HOH 384 984 510 HOH HOH A . 
B 2 HOH 385 985 82  HOH HOH A . 
B 2 HOH 386 986 329 HOH HOH A . 
B 2 HOH 387 987 351 HOH HOH A . 
B 2 HOH 388 988 567 HOH HOH A . 
B 2 HOH 389 989 321 HOH HOH A . 
B 2 HOH 390 990 154 HOH HOH A . 
B 2 HOH 391 991 529 HOH HOH A . 
B 2 HOH 392 992 217 HOH HOH A . 
B 2 HOH 393 993 391 HOH HOH A . 
B 2 HOH 394 994 235 HOH HOH A . 
B 2 HOH 395 995 260 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A LEU 3   ? CG  ? A LEU 17  CG  
2   1 Y 1 A LEU 3   ? CD1 ? A LEU 17  CD1 
3   1 Y 1 A LEU 3   ? CD2 ? A LEU 17  CD2 
4   1 Y 1 A LYS 5   ? CG  ? A LYS 19  CG  
5   1 Y 1 A LYS 5   ? CD  ? A LYS 19  CD  
6   1 Y 1 A LYS 5   ? CE  ? A LYS 19  CE  
7   1 Y 1 A LYS 5   ? NZ  ? A LYS 19  NZ  
8   1 Y 1 A LYS 6   ? CG  ? A LYS 20  CG  
9   1 Y 1 A LYS 6   ? CD  ? A LYS 20  CD  
10  1 Y 1 A LYS 6   ? CE  ? A LYS 20  CE  
11  1 Y 1 A LYS 6   ? NZ  ? A LYS 20  NZ  
12  1 Y 1 A ASP 47  ? CG  ? A ASP 61  CG  
13  1 Y 1 A ASP 47  ? OD1 ? A ASP 61  OD1 
14  1 Y 1 A ASP 47  ? OD2 ? A ASP 61  OD2 
15  1 Y 1 A GLU 48  ? CB  ? A GLU 62  CB  
16  1 Y 1 A GLU 48  ? CG  ? A GLU 62  CG  
17  1 Y 1 A GLU 48  ? CD  ? A GLU 62  CD  
18  1 Y 1 A GLU 48  ? OE1 ? A GLU 62  OE1 
19  1 Y 1 A GLU 48  ? OE2 ? A GLU 62  OE2 
20  1 Y 1 A LEU 50  ? CG  ? A LEU 64  CG  
21  1 Y 1 A LEU 50  ? CD1 ? A LEU 64  CD1 
22  1 Y 1 A LEU 50  ? CD2 ? A LEU 64  CD2 
23  1 Y 1 A ASP 93  ? CG  ? A ASP 107 CG  
24  1 Y 1 A ASP 93  ? OD1 ? A ASP 107 OD1 
25  1 Y 1 A ASP 93  ? OD2 ? A ASP 107 OD2 
26  1 Y 1 A LYS 117 ? CG  ? A LYS 131 CG  
27  1 Y 1 A LYS 117 ? CD  ? A LYS 131 CD  
28  1 Y 1 A LYS 117 ? CE  ? A LYS 131 CE  
29  1 Y 1 A LYS 117 ? NZ  ? A LYS 131 NZ  
30  1 Y 1 A LYS 118 ? CG  ? A LYS 132 CG  
31  1 Y 1 A LYS 118 ? CD  ? A LYS 132 CD  
32  1 Y 1 A LYS 118 ? CE  ? A LYS 132 CE  
33  1 Y 1 A LYS 118 ? NZ  ? A LYS 132 NZ  
34  1 Y 1 A LYS 133 ? CD  ? A LYS 147 CD  
35  1 Y 1 A LYS 133 ? CE  ? A LYS 147 CE  
36  1 Y 1 A LYS 133 ? NZ  ? A LYS 147 NZ  
37  1 Y 1 A LYS 182 ? CG  ? A LYS 196 CG  
38  1 Y 1 A LYS 182 ? CD  ? A LYS 196 CD  
39  1 Y 1 A LYS 182 ? CE  ? A LYS 196 CE  
40  1 Y 1 A LYS 182 ? NZ  ? A LYS 196 NZ  
41  1 Y 1 A LYS 204 ? CG  ? A LYS 218 CG  
42  1 Y 1 A LYS 204 ? CD  ? A LYS 218 CD  
43  1 Y 1 A LYS 204 ? CE  ? A LYS 218 CE  
44  1 Y 1 A LYS 204 ? NZ  ? A LYS 218 NZ  
45  1 Y 1 A ARG 260 ? CG  ? A ARG 274 CG  
46  1 Y 1 A ARG 260 ? CD  ? A ARG 274 CD  
47  1 Y 1 A ARG 260 ? NE  ? A ARG 274 NE  
48  1 Y 1 A ARG 260 ? CZ  ? A ARG 274 CZ  
49  1 Y 1 A ARG 260 ? NH1 ? A ARG 274 NH1 
50  1 Y 1 A ARG 260 ? NH2 ? A ARG 274 NH2 
51  1 Y 1 A LEU 262 ? CG  ? A LEU 276 CG  
52  1 Y 1 A LEU 262 ? CD1 ? A LEU 276 CD1 
53  1 Y 1 A LEU 262 ? CD2 ? A LEU 276 CD2 
54  1 Y 1 A GLU 263 ? CG  ? A GLU 277 CG  
55  1 Y 1 A GLU 263 ? CD  ? A GLU 277 CD  
56  1 Y 1 A GLU 263 ? OE1 ? A GLU 277 OE1 
57  1 Y 1 A GLU 263 ? OE2 ? A GLU 277 OE2 
58  1 Y 1 A LYS 271 ? CG  ? A LYS 285 CG  
59  1 Y 1 A LYS 271 ? CD  ? A LYS 285 CD  
60  1 Y 1 A LYS 271 ? CE  ? A LYS 285 CE  
61  1 Y 1 A LYS 271 ? NZ  ? A LYS 285 NZ  
62  1 Y 1 A LYS 279 ? CG  ? A LYS 293 CG  
63  1 Y 1 A LYS 279 ? CD  ? A LYS 293 CD  
64  1 Y 1 A LYS 279 ? CE  ? A LYS 293 CE  
65  1 Y 1 A LYS 279 ? NZ  ? A LYS 293 NZ  
66  1 Y 1 A ASP 280 ? CG  ? A ASP 294 CG  
67  1 Y 1 A ASP 280 ? OD1 ? A ASP 294 OD1 
68  1 Y 1 A ASP 280 ? OD2 ? A ASP 294 OD2 
69  1 Y 1 A ASN 286 ? OD1 ? A ASN 300 OD1 
70  1 Y 1 A ASN 286 ? ND2 ? A ASN 300 ND2 
71  1 Y 1 A MET 303 ? CG  ? A MET 317 CG  
72  1 Y 1 A MET 303 ? SD  ? A MET 317 SD  
73  1 Y 1 A MET 303 ? CE  ? A MET 317 CE  
74  1 Y 1 A GLN 304 ? CG  ? A GLN 318 CG  
75  1 Y 1 A GLN 304 ? CD  ? A GLN 318 CD  
76  1 Y 1 A GLN 304 ? OE1 ? A GLN 318 OE1 
77  1 Y 1 A GLN 304 ? NE2 ? A GLN 318 NE2 
78  1 Y 1 A LYS 318 ? CG  ? A LYS 332 CG  
79  1 Y 1 A LYS 318 ? CD  ? A LYS 332 CD  
80  1 Y 1 A LYS 318 ? CE  ? A LYS 332 CE  
81  1 Y 1 A LYS 318 ? NZ  ? A LYS 332 NZ  
82  1 Y 1 A LYS 320 ? CG  ? A LYS 334 CG  
83  1 Y 1 A LYS 320 ? CD  ? A LYS 334 CD  
84  1 Y 1 A LYS 320 ? CE  ? A LYS 334 CE  
85  1 Y 1 A LYS 320 ? NZ  ? A LYS 334 NZ  
86  1 Y 1 A LEU 332 ? CD1 ? A LEU 346 CD1 
87  1 Y 1 A LEU 332 ? CD2 ? A LEU 346 CD2 
88  1 Y 1 A ILE 334 ? CG1 ? A ILE 348 CG1 
89  1 Y 1 A ILE 334 ? CG2 ? A ILE 348 CG2 
90  1 Y 1 A ILE 334 ? CD1 ? A ILE 348 CD1 
91  1 Y 1 A ASN 339 ? CG  ? A ASN 353 CG  
92  1 Y 1 A ASN 339 ? OD1 ? A ASN 353 OD1 
93  1 Y 1 A ASN 339 ? ND2 ? A ASN 353 ND2 
94  1 Y 1 A ARG 353 ? CZ  ? A ARG 367 CZ  
95  1 Y 1 A ARG 353 ? NH2 ? A ARG 367 NH2 
96  1 Y 1 A LYS 363 ? CG  ? A LYS 377 CG  
97  1 Y 1 A LYS 363 ? CD  ? A LYS 377 CD  
98  1 Y 1 A LYS 363 ? CE  ? A LYS 377 CE  
99  1 Y 1 A LYS 363 ? NZ  ? A LYS 377 NZ  
100 1 Y 1 A LYS 364 ? CG  ? A LYS 378 CG  
101 1 Y 1 A LYS 364 ? CD  ? A LYS 378 CD  
102 1 Y 1 A LYS 364 ? CE  ? A LYS 378 CE  
103 1 Y 1 A LYS 364 ? NZ  ? A LYS 378 NZ  
104 1 Y 1 A HIS 366 ? CD2 ? A HIS 380 CD2 
105 1 Y 1 A HIS 366 ? CE1 ? A HIS 380 CE1 
106 1 Y 1 A HIS 366 ? NE2 ? A HIS 380 NE2 
107 1 Y 1 A ASP 445 ? CG  ? A ASP 459 CG  
108 1 Y 1 A ASP 445 ? OD1 ? A ASP 459 OD1 
109 1 Y 1 A ASP 445 ? OD2 ? A ASP 459 OD2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5.8.0350 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? MOSFLM ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? SCALA  ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8YYF 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     57.040 
_cell.length_a_esd                 ? 
_cell.length_b                     72.430 
_cell.length_b_esd                 ? 
_cell.length_c                     106.310 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8YYF 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_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                   8YYF 
_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             1.71 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          27.96 
_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          'BATCH MODE' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              5.6 
_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    '100mM tri-sodium citrate dihydrate pH 5.6, 20% PEG 4000, 20% Isopropanol, 40% Formamide' 
_exptl_crystal_grow.pdbx_pH_range   5.6-6.0 
_exptl_crystal_grow.temp            293 
# 
_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 PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-06-08 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.0 
_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                        'ELETTRA BEAMLINE 11.2C' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.0 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   11.2C 
_diffrn_source.pdbx_synchrotron_site       ELETTRA 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8YYF 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.39 
_reflns.d_resolution_low                               42.89 
_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                                     80710 
_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                           90.4 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                7.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.6 
_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                                   0.98 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.17 
_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                                    1.39 
_reflns_shell.d_res_low                                     1.47 
_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                             11475 
_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                               7.3 
_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                                  0.95 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          89.91 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            -0.05 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][2]                            -0.07 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            0.12 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               22.416 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.965 
_refine.correlation_coeff_Fo_to_Fc_free          0.954 
_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                                 8YYF 
_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                            1.39 
_refine.ls_d_res_low                             42.89 
_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                     76631 
_refine.ls_number_reflns_R_free                  4005 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    90.39 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.16676 
_refine.ls_R_factor_R_free                       0.20464 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.16473 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.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                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.072 
_refine.pdbx_overall_ESU_R_Free                  0.067 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             2.057 
_refine.overall_SU_ML                            0.038 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.39 
_refine_hist.d_res_low                        42.89 
_refine_hist.number_atoms_solvent             395 
_refine_hist.number_atoms_total               3757 
_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        3362 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_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' ? 0.010  0.012  3431  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.662  1.627  4642  ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.262  5.000  442   ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 18.576 10.000 11    ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 14.628 10.000 589   ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.102  0.200  533   ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.011  0.020  2544  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 10.094 2.122  1768  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 11.628 3.114  2207  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 7.886  2.115  1663  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 11.456 38.949 15015 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? 21.971 3.000  3431  ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.390 
_refine_ls_shell.d_res_low                        1.426 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             309 
_refine_ls_shell.number_reflns_R_work             6190 
_refine_ls_shell.percent_reflns_obs               99.98 
_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                  0.171 
_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   20 
_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                  0.237 
# 
_struct.entry_id                     8YYF 
_struct.title                        'RNase J2 mutant H76A' 
_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        8YYF 
_struct_keywords.text            'Ribonuclease, RNase J2, RNA BINDING PROTEIN' 
_struct_keywords.pdbx_keywords   'RNA BINDING PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    RNJ2_STAEQ 
_struct_ref.pdbx_db_accession          Q5HPR6 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSLIKKKNKDIRIIPLGGVGEIAKNMYIVEVDDEMFMLDAGLMFPEDEMLGVDIVIPDIQYVIENKERLKGIFLTHGHEH
AIGAVSYVLEQIDAPVYGSKLTIALVKEAMKARNIKKKVRYYTVNHDSIMRFKNVNVSFFNTTHSIPDSLGVCIHTSYGS
IVYTGEFKFDQSLHGHYAPDLKRMAEIGDEGVFALISDSTEAEKPGYNTPENIIEHHMYDAFAKVKGRLIVSCYASNFVR
IQQVLNIASQLNRKVSFLGRSLESSFNIARKMGYFDIPKDLLIPINEVENYPKNEVIIIATGMQGEPVEALSQMARKKHK
IMNIEEGDSIFLAITASANMEVIIADTLNELVRAGAHIIPNNKKIHASSHGCMEELKMMLNIMKPEYFVPVQGEFKMQIA
HAKLAAETGVAPEKIFLVEKGDVISYNGKDMILNEKVQSGNILIDGIGVGDVGNIVLRDRHLLAEDGIFIAVVTLDPKNR
RIAAGPEIQSRGFVYVRESEELLKEAEEKVRKIVEEGLQEKRIEWSEIKQNMRDQISKLLFESTKRRPMIIPVISEI
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8YYF 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 15 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 571 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q5HPR6 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  557 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       557 
# 
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 8YYF MET A 1  ? UNP Q5HPR6 ?   ?  'initiating methionine' -13 1  
1 8YYF GLY A 2  ? UNP Q5HPR6 ?   ?  'expression tag'        -12 2  
1 8YYF SER A 3  ? UNP Q5HPR6 ?   ?  'expression tag'        -11 3  
1 8YYF SER A 4  ? UNP Q5HPR6 ?   ?  'expression tag'        -10 4  
1 8YYF HIS A 5  ? UNP Q5HPR6 ?   ?  'expression tag'        -9  5  
1 8YYF HIS A 6  ? UNP Q5HPR6 ?   ?  'expression tag'        -8  6  
1 8YYF HIS A 7  ? UNP Q5HPR6 ?   ?  'expression tag'        -7  7  
1 8YYF HIS A 8  ? UNP Q5HPR6 ?   ?  'expression tag'        -6  8  
1 8YYF HIS A 9  ? UNP Q5HPR6 ?   ?  'expression tag'        -5  9  
1 8YYF HIS A 10 ? UNP Q5HPR6 ?   ?  'expression tag'        -4  10 
1 8YYF SER A 11 ? UNP Q5HPR6 ?   ?  'expression tag'        -3  11 
1 8YYF GLN A 12 ? UNP Q5HPR6 ?   ?  'expression tag'        -2  12 
1 8YYF ASP A 13 ? UNP Q5HPR6 ?   ?  'expression tag'        -1  13 
1 8YYF PRO A 14 ? UNP Q5HPR6 ?   ?  'expression tag'        0   14 
1 8YYF ALA A 90 ? UNP Q5HPR6 HIS 76 'engineered mutation'   76  15 
# 
_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 
# 
_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 ILE A 73  ? ASN A 79  ? ILE A 59  ASN A 65  1 ? 7  
HELX_P HELX_P2  AA2 HIS A 92  ? GLY A 97  ? HIS A 78  GLY A 83  1 ? 6  
HELX_P HELX_P3  AA3 ALA A 98  ? ILE A 106 ? ALA A 84  ILE A 92  1 ? 9  
HELX_P HELX_P4  AA4 SER A 113 ? ARG A 127 ? SER A 99  ARG A 113 1 ? 15 
HELX_P HELX_P5  AA5 HIS A 188 ? ALA A 192 ? HIS A 174 ALA A 178 5 ? 5  
HELX_P HELX_P6  AA6 ASP A 194 ? GLY A 205 ? ASP A 180 GLY A 191 1 ? 12 
HELX_P HELX_P7  AA7 PRO A 224 ? LYS A 238 ? PRO A 210 LYS A 224 1 ? 15 
HELX_P HELX_P8  AA8 ASN A 251 ? LEU A 265 ? ASN A 237 LEU A 251 1 ? 15 
HELX_P HELX_P9  AA9 GLY A 273 ? GLY A 287 ? GLY A 259 GLY A 273 1 ? 15 
HELX_P HELX_P10 AB1 PRO A 298 ? TYR A 305 ? PRO A 284 TYR A 291 5 ? 8  
HELX_P HELX_P11 AB2 PRO A 306 ? ASN A 308 ? PRO A 292 ASN A 294 5 ? 3  
HELX_P HELX_P12 AB3 GLU A 320 ? ARG A 330 ? GLU A 306 ARG A 316 1 ? 11 
HELX_P HELX_P13 AB4 SER A 351 ? ASN A 353 ? SER A 337 ASN A 339 5 ? 3  
HELX_P HELX_P14 AB5 MET A 354 ? ALA A 368 ? MET A 340 ALA A 354 1 ? 15 
HELX_P HELX_P15 AB6 CYS A 386 ? LYS A 398 ? CYS A 372 LYS A 384 1 ? 13 
HELX_P HELX_P16 AB7 GLU A 408 ? THR A 422 ? GLU A 394 THR A 408 1 ? 15 
HELX_P HELX_P17 AB8 ALA A 425 ? ILE A 429 ? ALA A 411 ILE A 415 5 ? 5  
# 
_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 ? 8 ? 
AA2 ? 2 ? 
AA3 ? 6 ? 
AA4 ? 5 ? 
# 
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 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? parallel      
AA3 5 6 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? parallel      
AA4 3 4 ? parallel      
AA4 4 5 ? 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 TYR A 135 ? THR A 137 ? TYR A 121 THR A 123 
AA1 2 VAL A 110 ? GLY A 112 ? VAL A 96  GLY A 98  
AA1 3 LEU A 83  ? PHE A 87  ? LEU A 69  PHE A 73  
AA1 4 GLU A 48  ? LEU A 52  ? GLU A 34  LEU A 38  
AA1 5 MET A 40  ? VAL A 45  ? MET A 26  VAL A 31  
AA1 6 ILE A 25  ? GLY A 31  ? ILE A 11  GLY A 17  
AA1 7 ASP A 436 ? TYR A 440 ? ASP A 422 TYR A 426 
AA1 8 MET A 445 ? LYS A 450 ? MET A 431 LYS A 436 
AA2 1 ILE A 68  ? PRO A 71  ? ILE A 54  PRO A 57  
AA2 2 ASN A 455 ? ILE A 458 ? ASN A 441 ILE A 444 
AA3 1 ILE A 143 ? ARG A 145 ? ILE A 129 ARG A 131 
AA3 2 ASN A 150 ? THR A 156 ? ASN A 136 THR A 142 
AA3 3 SER A 163 ? HIS A 169 ? SER A 149 HIS A 155 
AA3 4 SER A 174 ? TYR A 177 ? SER A 160 TYR A 163 
AA3 5 VAL A 206 ? ASP A 212 ? VAL A 192 ASP A 198 
AA3 6 TYR A 401 ? VAL A 405 ? TYR A 387 VAL A 391 
AA4 1 LYS A 268 ? LEU A 272 ? LYS A 254 LEU A 258 
AA4 2 VAL A 310 ? ALA A 314 ? VAL A 296 ALA A 300 
AA4 3 LEU A 243 ? CYS A 247 ? LEU A 229 CYS A 233 
AA4 4 SER A 343 ? ALA A 347 ? SER A 329 ALA A 333 
AA4 5 HIS A 371 ? ILE A 372 ? HIS A 357 ILE A 358 
# 
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 TYR A 136 ? O TYR A 122 N VAL A 110 ? N VAL A 96  
AA1 2 3 O TYR A 111 ? O TYR A 97  N ILE A 86  ? N ILE A 72  
AA1 3 4 O PHE A 87  ? O PHE A 73  N MET A 51  ? N MET A 37  
AA1 4 5 O LEU A 52  ? O LEU A 38  N TYR A 41  ? N TYR A 27  
AA1 5 6 O ILE A 42  ? O ILE A 28  N ILE A 28  ? N ILE A 14  
AA1 6 7 N ILE A 27  ? N ILE A 13  O ILE A 438 ? O ILE A 424 
AA1 7 8 N SER A 439 ? N SER A 425 O ILE A 446 ? O ILE A 432 
AA2 1 2 N ILE A 68  ? N ILE A 54  O ILE A 458 ? O ILE A 444 
AA3 1 2 N MET A 144 ? N MET A 130 O VAL A 151 ? O VAL A 137 
AA3 2 3 N PHE A 154 ? N PHE A 140 O GLY A 165 ? O GLY A 151 
AA3 3 4 N ILE A 168 ? N ILE A 154 O ILE A 175 ? O ILE A 161 
AA3 4 5 N VAL A 176 ? N VAL A 162 O ILE A 210 ? O ILE A 196 
AA3 5 6 N LEU A 209 ? N LEU A 195 O VAL A 403 ? O VAL A 389 
AA4 1 2 N LEU A 272 ? N LEU A 258 O ILE A 313 ? O ILE A 299 
AA4 2 3 O ALA A 314 ? O ALA A 300 N VAL A 245 ? N VAL A 231 
AA4 3 4 N SER A 246 ? N SER A 232 O ALA A 347 ? O ALA A 333 
AA4 4 5 N ILE A 344 ? N ILE A 330 O HIS A 371 ? O HIS A 357 
# 
_pdbx_entry_details.entry_id                   8YYF 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O A HOH 659 ? ? 1_555 O A HOH 745 ? ? 4_455 1.93 
2 1 O A HOH 745 ? ? 1_555 O A HOH 762 ? ? 4_555 2.05 
3 1 O A HOH 620 ? ? 1_555 O A HOH 713 ? ? 4_455 2.07 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             NE 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_1              12 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CZ 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_2              12 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             NH2 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_3              12 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                117.18 
_pdbx_validate_rmsd_angle.angle_target_value         120.30 
_pdbx_validate_rmsd_angle.angle_deviation            -3.12 
_pdbx_validate_rmsd_angle.angle_standard_deviation   0.50 
_pdbx_validate_rmsd_angle.linker_flag                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 23  ? ? -160.30 -160.51 
2 1 MET A 26  ? ? -163.80 113.91  
3 1 ASP A 32  ? ? 47.85   -125.99 
4 1 ASP A 39  ? ? 67.47   161.66  
5 1 ALA A 40  ? ? -155.43 70.82   
6 1 PHE A 132 ? ? -106.61 -168.81 
7 1 ALA A 333 ? ? -112.69 52.73   
8 1 GLN A 392 ? ? 50.61   70.09   
9 1 LYS A 429 ? ? -123.43 -54.90  
# 
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 -13 ? A MET 1   
2   1 Y 1 A GLY -12 ? A GLY 2   
3   1 Y 1 A SER -11 ? A SER 3   
4   1 Y 1 A SER -10 ? A SER 4   
5   1 Y 1 A HIS -9  ? A HIS 5   
6   1 Y 1 A HIS -8  ? A HIS 6   
7   1 Y 1 A HIS -7  ? A HIS 7   
8   1 Y 1 A HIS -6  ? A HIS 8   
9   1 Y 1 A HIS -5  ? A HIS 9   
10  1 Y 1 A HIS -4  ? A HIS 10  
11  1 Y 1 A SER -3  ? A SER 11  
12  1 Y 1 A GLN -2  ? A GLN 12  
13  1 Y 1 A ASP -1  ? A ASP 13  
14  1 Y 1 A PRO 0   ? A PRO 14  
15  1 Y 1 A MET 1   ? A MET 15  
16  1 Y 1 A SER 2   ? A SER 16  
17  1 Y 1 A THR 335 ? A THR 349 
18  1 Y 1 A GLY 446 ? A GLY 460 
19  1 Y 1 A ILE 447 ? A ILE 461 
20  1 Y 1 A GLY 448 ? A GLY 462 
21  1 Y 1 A VAL 449 ? A VAL 463 
22  1 Y 1 A GLY 450 ? A GLY 464 
23  1 Y 1 A ASP 451 ? A ASP 465 
24  1 Y 1 A VAL 452 ? A VAL 466 
25  1 Y 1 A GLY 453 ? A GLY 467 
26  1 Y 1 A ASN 454 ? A ASN 468 
27  1 Y 1 A ILE 455 ? A ILE 469 
28  1 Y 1 A VAL 456 ? A VAL 470 
29  1 Y 1 A LEU 457 ? A LEU 471 
30  1 Y 1 A ARG 458 ? A ARG 472 
31  1 Y 1 A ASP 459 ? A ASP 473 
32  1 Y 1 A ARG 460 ? A ARG 474 
33  1 Y 1 A HIS 461 ? A HIS 475 
34  1 Y 1 A LEU 462 ? A LEU 476 
35  1 Y 1 A LEU 463 ? A LEU 477 
36  1 Y 1 A ALA 464 ? A ALA 478 
37  1 Y 1 A GLU 465 ? A GLU 479 
38  1 Y 1 A ASP 466 ? A ASP 480 
39  1 Y 1 A GLY 467 ? A GLY 481 
40  1 Y 1 A ILE 468 ? A ILE 482 
41  1 Y 1 A PHE 469 ? A PHE 483 
42  1 Y 1 A ILE 470 ? A ILE 484 
43  1 Y 1 A ALA 471 ? A ALA 485 
44  1 Y 1 A VAL 472 ? A VAL 486 
45  1 Y 1 A VAL 473 ? A VAL 487 
46  1 Y 1 A THR 474 ? A THR 488 
47  1 Y 1 A LEU 475 ? A LEU 489 
48  1 Y 1 A ASP 476 ? A ASP 490 
49  1 Y 1 A PRO 477 ? A PRO 491 
50  1 Y 1 A LYS 478 ? A LYS 492 
51  1 Y 1 A ASN 479 ? A ASN 493 
52  1 Y 1 A ARG 480 ? A ARG 494 
53  1 Y 1 A ARG 481 ? A ARG 495 
54  1 Y 1 A ILE 482 ? A ILE 496 
55  1 Y 1 A ALA 483 ? A ALA 497 
56  1 Y 1 A ALA 484 ? A ALA 498 
57  1 Y 1 A GLY 485 ? A GLY 499 
58  1 Y 1 A PRO 486 ? A PRO 500 
59  1 Y 1 A GLU 487 ? A GLU 501 
60  1 Y 1 A ILE 488 ? A ILE 502 
61  1 Y 1 A GLN 489 ? A GLN 503 
62  1 Y 1 A SER 490 ? A SER 504 
63  1 Y 1 A ARG 491 ? A ARG 505 
64  1 Y 1 A GLY 492 ? A GLY 506 
65  1 Y 1 A PHE 493 ? A PHE 507 
66  1 Y 1 A VAL 494 ? A VAL 508 
67  1 Y 1 A TYR 495 ? A TYR 509 
68  1 Y 1 A VAL 496 ? A VAL 510 
69  1 Y 1 A ARG 497 ? A ARG 511 
70  1 Y 1 A GLU 498 ? A GLU 512 
71  1 Y 1 A SER 499 ? A SER 513 
72  1 Y 1 A GLU 500 ? A GLU 514 
73  1 Y 1 A GLU 501 ? A GLU 515 
74  1 Y 1 A LEU 502 ? A LEU 516 
75  1 Y 1 A LEU 503 ? A LEU 517 
76  1 Y 1 A LYS 504 ? A LYS 518 
77  1 Y 1 A GLU 505 ? A GLU 519 
78  1 Y 1 A ALA 506 ? A ALA 520 
79  1 Y 1 A GLU 507 ? A GLU 521 
80  1 Y 1 A GLU 508 ? A GLU 522 
81  1 Y 1 A LYS 509 ? A LYS 523 
82  1 Y 1 A VAL 510 ? A VAL 524 
83  1 Y 1 A ARG 511 ? A ARG 525 
84  1 Y 1 A LYS 512 ? A LYS 526 
85  1 Y 1 A ILE 513 ? A ILE 527 
86  1 Y 1 A VAL 514 ? A VAL 528 
87  1 Y 1 A GLU 515 ? A GLU 529 
88  1 Y 1 A GLU 516 ? A GLU 530 
89  1 Y 1 A GLY 517 ? A GLY 531 
90  1 Y 1 A LEU 518 ? A LEU 532 
91  1 Y 1 A GLN 519 ? A GLN 533 
92  1 Y 1 A GLU 520 ? A GLU 534 
93  1 Y 1 A LYS 521 ? A LYS 535 
94  1 Y 1 A ARG 522 ? A ARG 536 
95  1 Y 1 A ILE 523 ? A ILE 537 
96  1 Y 1 A GLU 524 ? A GLU 538 
97  1 Y 1 A TRP 525 ? A TRP 539 
98  1 Y 1 A SER 526 ? A SER 540 
99  1 Y 1 A GLU 527 ? A GLU 541 
100 1 Y 1 A ILE 528 ? A ILE 542 
101 1 Y 1 A LYS 529 ? A LYS 543 
102 1 Y 1 A GLN 530 ? A GLN 544 
103 1 Y 1 A ASN 531 ? A ASN 545 
104 1 Y 1 A MET 532 ? A MET 546 
105 1 Y 1 A ARG 533 ? A ARG 547 
106 1 Y 1 A ASP 534 ? A ASP 548 
107 1 Y 1 A GLN 535 ? A GLN 549 
108 1 Y 1 A ILE 536 ? A ILE 550 
109 1 Y 1 A SER 537 ? A SER 551 
110 1 Y 1 A LYS 538 ? A LYS 552 
111 1 Y 1 A LEU 539 ? A LEU 553 
112 1 Y 1 A LEU 540 ? A LEU 554 
113 1 Y 1 A PHE 541 ? A PHE 555 
114 1 Y 1 A GLU 542 ? A GLU 556 
115 1 Y 1 A SER 543 ? A SER 557 
116 1 Y 1 A THR 544 ? A THR 558 
117 1 Y 1 A LYS 545 ? A LYS 559 
118 1 Y 1 A ARG 546 ? A ARG 560 
119 1 Y 1 A ARG 547 ? A ARG 561 
120 1 Y 1 A PRO 548 ? A PRO 562 
121 1 Y 1 A MET 549 ? A MET 563 
122 1 Y 1 A ILE 550 ? A ILE 564 
123 1 Y 1 A ILE 551 ? A ILE 565 
124 1 Y 1 A PRO 552 ? A PRO 566 
125 1 Y 1 A VAL 553 ? A VAL 567 
126 1 Y 1 A ILE 554 ? A ILE 568 
127 1 Y 1 A SER 555 ? A SER 569 
128 1 Y 1 A GLU 556 ? A GLU 570 
129 1 Y 1 A ILE 557 ? A ILE 571 
# 
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  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
PHE N    N N N 250 
PHE CA   C N S 251 
PHE C    C N N 252 
PHE O    O N N 253 
PHE CB   C N N 254 
PHE CG   C Y N 255 
PHE CD1  C Y N 256 
PHE CD2  C Y N 257 
PHE CE1  C Y N 258 
PHE CE2  C Y N 259 
PHE CZ   C Y N 260 
PHE OXT  O N N 261 
PHE H    H N N 262 
PHE H2   H N N 263 
PHE HA   H N N 264 
PHE HB2  H N N 265 
PHE HB3  H N N 266 
PHE HD1  H N N 267 
PHE HD2  H N N 268 
PHE HE1  H N N 269 
PHE HE2  H N N 270 
PHE HZ   H N N 271 
PHE HXT  H N N 272 
PRO N    N N N 273 
PRO CA   C N S 274 
PRO C    C N N 275 
PRO O    O N N 276 
PRO CB   C N N 277 
PRO CG   C N N 278 
PRO CD   C N N 279 
PRO OXT  O N N 280 
PRO H    H N N 281 
PRO HA   H N N 282 
PRO HB2  H N N 283 
PRO HB3  H N N 284 
PRO HG2  H N N 285 
PRO HG3  H N N 286 
PRO HD2  H N N 287 
PRO HD3  H N N 288 
PRO HXT  H N N 289 
SER N    N N N 290 
SER CA   C N S 291 
SER C    C N N 292 
SER O    O N N 293 
SER CB   C N N 294 
SER OG   O N N 295 
SER OXT  O N N 296 
SER H    H N N 297 
SER H2   H N N 298 
SER HA   H N N 299 
SER HB2  H N N 300 
SER HB3  H N N 301 
SER HG   H N N 302 
SER HXT  H N N 303 
THR N    N N N 304 
THR CA   C N S 305 
THR C    C N N 306 
THR O    O N N 307 
THR CB   C N R 308 
THR OG1  O N N 309 
THR CG2  C N N 310 
THR OXT  O N N 311 
THR H    H N N 312 
THR H2   H N N 313 
THR HA   H N N 314 
THR HB   H N N 315 
THR HG1  H N N 316 
THR HG21 H N N 317 
THR HG22 H N N 318 
THR HG23 H N N 319 
THR HXT  H N N 320 
TRP N    N N N 321 
TRP CA   C N S 322 
TRP C    C N N 323 
TRP O    O N N 324 
TRP CB   C N N 325 
TRP CG   C Y N 326 
TRP CD1  C Y N 327 
TRP CD2  C Y N 328 
TRP NE1  N Y N 329 
TRP CE2  C Y N 330 
TRP CE3  C Y N 331 
TRP CZ2  C Y N 332 
TRP CZ3  C Y N 333 
TRP CH2  C Y N 334 
TRP OXT  O N N 335 
TRP H    H N N 336 
TRP H2   H N N 337 
TRP HA   H N N 338 
TRP HB2  H N N 339 
TRP HB3  H N N 340 
TRP HD1  H N N 341 
TRP HE1  H N N 342 
TRP HE3  H N N 343 
TRP HZ2  H N N 344 
TRP HZ3  H N N 345 
TRP HH2  H N N 346 
TRP HXT  H N N 347 
TYR N    N N N 348 
TYR CA   C N S 349 
TYR C    C N N 350 
TYR O    O N N 351 
TYR CB   C N N 352 
TYR CG   C Y N 353 
TYR CD1  C Y N 354 
TYR CD2  C Y N 355 
TYR CE1  C Y N 356 
TYR CE2  C Y N 357 
TYR CZ   C Y N 358 
TYR OH   O N N 359 
TYR OXT  O N N 360 
TYR H    H N N 361 
TYR H2   H N N 362 
TYR HA   H N N 363 
TYR HB2  H N N 364 
TYR HB3  H N N 365 
TYR HD1  H N N 366 
TYR HD2  H N N 367 
TYR HE1  H N N 368 
TYR HE2  H N N 369 
TYR HH   H N N 370 
TYR HXT  H N N 371 
VAL N    N N N 372 
VAL CA   C N S 373 
VAL C    C N N 374 
VAL O    O N N 375 
VAL CB   C N N 376 
VAL CG1  C N N 377 
VAL CG2  C N N 378 
VAL OXT  O N N 379 
VAL H    H N N 380 
VAL H2   H N N 381 
VAL HA   H N N 382 
VAL HB   H N N 383 
VAL HG11 H N N 384 
VAL HG12 H N N 385 
VAL HG13 H N N 386 
VAL HG21 H N N 387 
VAL HG22 H N N 388 
VAL HG23 H N N 389 
VAL HXT  H N N 390 
# 
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  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TRP N   CA   sing N N 306 
TRP N   H    sing N N 307 
TRP N   H2   sing N N 308 
TRP CA  C    sing N N 309 
TRP CA  CB   sing N N 310 
TRP CA  HA   sing N N 311 
TRP C   O    doub N N 312 
TRP C   OXT  sing N N 313 
TRP CB  CG   sing N N 314 
TRP CB  HB2  sing N N 315 
TRP CB  HB3  sing N N 316 
TRP CG  CD1  doub Y N 317 
TRP CG  CD2  sing Y N 318 
TRP CD1 NE1  sing Y N 319 
TRP CD1 HD1  sing N N 320 
TRP CD2 CE2  doub Y N 321 
TRP CD2 CE3  sing Y N 322 
TRP NE1 CE2  sing Y N 323 
TRP NE1 HE1  sing N N 324 
TRP CE2 CZ2  sing Y N 325 
TRP CE3 CZ3  doub Y N 326 
TRP CE3 HE3  sing N N 327 
TRP CZ2 CH2  doub Y N 328 
TRP CZ2 HZ2  sing N N 329 
TRP CZ3 CH2  sing Y N 330 
TRP CZ3 HZ3  sing N N 331 
TRP CH2 HH2  sing N N 332 
TRP OXT HXT  sing N N 333 
TYR N   CA   sing N N 334 
TYR N   H    sing N N 335 
TYR N   H2   sing N N 336 
TYR CA  C    sing N N 337 
TYR CA  CB   sing N N 338 
TYR CA  HA   sing N N 339 
TYR C   O    doub N N 340 
TYR C   OXT  sing N N 341 
TYR CB  CG   sing N N 342 
TYR CB  HB2  sing N N 343 
TYR CB  HB3  sing N N 344 
TYR CG  CD1  doub Y N 345 
TYR CG  CD2  sing Y N 346 
TYR CD1 CE1  sing Y N 347 
TYR CD1 HD1  sing N N 348 
TYR CD2 CE2  doub Y N 349 
TYR CD2 HD2  sing N N 350 
TYR CE1 CZ   doub Y N 351 
TYR CE1 HE1  sing N N 352 
TYR CE2 CZ   sing Y N 353 
TYR CE2 HE2  sing N N 354 
TYR CZ  OH   sing N N 355 
TYR OH  HH   sing N N 356 
TYR OXT HXT  sing N N 357 
VAL N   CA   sing N N 358 
VAL N   H    sing N N 359 
VAL N   H2   sing N N 360 
VAL CA  C    sing N N 361 
VAL CA  CB   sing N N 362 
VAL CA  HA   sing N N 363 
VAL C   O    doub N N 364 
VAL C   OXT  sing N N 365 
VAL CB  CG1  sing N N 366 
VAL CB  CG2  sing N N 367 
VAL CB  HB   sing N N 368 
VAL CG1 HG11 sing N N 369 
VAL CG1 HG12 sing N N 370 
VAL CG1 HG13 sing N N 371 
VAL CG2 HG21 sing N N 372 
VAL CG2 HG22 sing N N 373 
VAL CG2 HG23 sing N N 374 
VAL OXT HXT  sing N N 375 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Science and Engineering Research Board (SERB)'   India FA/DSTO-17-0001.03 1 
'Department of Science & Technology (DST, India)' India SP/DSTO-16-1668.03 2 
'Science and Engineering Research Board (SERB)'   India SP/SERB-23-0307.26 3 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   6K6W 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8YYF 
_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]   0.017532 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.013806 
_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]   0.009406 
_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 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . LEU A 1 17  ? 15.022  28.676  29.265  1.00 107.66 ? 3   LEU A N   1 
ATOM   2    C CA  . LEU A 1 17  ? 14.688  27.953  30.516  1.00 89.73  ? 3   LEU A CA  1 
ATOM   3    C C   . LEU A 1 17  ? 13.469  27.058  30.274  1.00 111.03 ? 3   LEU A C   1 
ATOM   4    O O   . LEU A 1 17  ? 13.342  26.031  30.946  1.00 208.51 ? 3   LEU A O   1 
ATOM   5    C CB  . LEU A 1 17  ? 14.413  28.993  31.615  1.00 109.65 ? 3   LEU A CB  1 
ATOM   6    N N   . ILE A 1 18  ? 12.593  27.472  29.371  1.00 219.88 ? 4   ILE A N   1 
ATOM   7    C CA  . ILE A 1 18  ? 11.336  26.718  29.121  1.00 390.14 ? 4   ILE A CA  1 
ATOM   8    C C   . ILE A 1 18  ? 11.448  25.968  27.790  1.00 429.65 ? 4   ILE A C   1 
ATOM   9    O O   . ILE A 1 18  ? 11.724  26.619  26.781  1.00 407.40 ? 4   ILE A O   1 
ATOM   10   C CB  . ILE A 1 18  ? 10.123  27.667  29.126  1.00 103.18 ? 4   ILE A CB  1 
ATOM   11   C CG1 . ILE A 1 18  ? 10.029  28.486  30.416  1.00 74.98  ? 4   ILE A CG1 1 
ATOM   12   C CG2 . ILE A 1 18  ? 8.839   26.897  28.855  1.00 48.25  ? 4   ILE A CG2 1 
ATOM   13   C CD1 . ILE A 1 18  ? 9.192   29.734  30.276  1.00 83.64  ? 4   ILE A CD1 1 
ATOM   14   N N   . LYS A 1 19  ? 11.250  24.655  27.827  1.00 156.80 ? 5   LYS A N   1 
ATOM   15   C CA  . LYS A 1 19  ? 11.231  23.868  26.575  1.00 150.39 ? 5   LYS A CA  1 
ATOM   16   C C   . LYS A 1 19  ? 9.780   23.784  26.095  1.00 112.93 ? 5   LYS A C   1 
ATOM   17   O O   . LYS A 1 19  ? 8.885   23.626  26.936  1.00 157.55 ? 5   LYS A O   1 
ATOM   18   C CB  . LYS A 1 19  ? 11.811  22.475  26.808  1.00 153.21 ? 5   LYS A CB  1 
ATOM   19   N N   . LYS A 1 20  ? 9.572   23.916  24.792  1.00 181.56 ? 6   LYS A N   1 
ATOM   20   C CA  . LYS A 1 20  ? 8.202   23.769  24.248  1.00 465.86 ? 6   LYS A CA  1 
ATOM   21   C C   . LYS A 1 20  ? 7.744   22.325  24.478  1.00 670.09 ? 6   LYS A C   1 
ATOM   22   O O   . LYS A 1 20  ? 8.546   21.410  24.296  1.00 648.10 ? 6   LYS A O   1 
ATOM   23   C CB  . LYS A 1 20  ? 8.157   24.141  22.765  1.00 90.75  ? 6   LYS A CB  1 
ATOM   24   N N   . LYS A 1 21  ? 6.500   22.128  24.876  1.00 87.00  ? 7   LYS A N   1 
ATOM   25   C CA  . LYS A 1 21  ? 5.985   20.772  25.113  1.00 25.37  ? 7   LYS A CA  1 
ATOM   26   C C   . LYS A 1 21  ? 4.694   20.570  24.320  1.00 18.55  ? 7   LYS A C   1 
ATOM   27   O O   . LYS A 1 21  ? 4.009   21.547  24.051  1.00 23.75  ? 7   LYS A O   1 
ATOM   28   C CB  . LYS A 1 21  ? 5.698   20.608  26.600  1.00 25.85  ? 7   LYS A CB  1 
ATOM   29   C CG  . LYS A 1 21  ? 5.339   19.201  27.042  1.00 44.16  ? 7   LYS A CG  1 
ATOM   30   C CD  . LYS A 1 21  ? 4.042   19.123  27.805  1.00 65.10  ? 7   LYS A CD  1 
ATOM   31   C CE  . LYS A 1 21  ? 3.603   17.693  28.045  1.00 48.30  ? 7   LYS A CE  1 
ATOM   32   N NZ  . LYS A 1 21  ? 2.131   17.598  28.149  1.00 37.37  ? 7   LYS A NZ  1 
ATOM   33   N N   . ASN A 1 22  ? 4.396   19.320  23.996  1.00 13.96  ? 8   ASN A N   1 
ATOM   34   C CA  . ASN A 1 22  ? 3.139   19.046  23.313  1.00 16.06  ? 8   ASN A CA  1 
ATOM   35   C C   . ASN A 1 22  ? 2.039   18.822  24.345  1.00 15.40  ? 8   ASN A C   1 
ATOM   36   O O   . ASN A 1 22  ? 2.297   18.262  25.422  1.00 19.86  ? 8   ASN A O   1 
ATOM   37   C CB  . ASN A 1 22  ? 3.299   17.826  22.408  1.00 13.29  ? 8   ASN A CB  1 
ATOM   38   C CG  . ASN A 1 22  ? 4.488   17.957  21.476  1.00 14.40  ? 8   ASN A CG  1 
ATOM   39   O OD1 . ASN A 1 22  ? 5.355   17.063  21.462  1.00 15.52  ? 8   ASN A OD1 1 
ATOM   40   N ND2 . ASN A 1 22  ? 4.566   19.055  20.729  1.00 15.75  ? 8   ASN A ND2 1 
ATOM   41   N N   . LYS A 1 23  ? 0.805   19.202  24.000  1.00 14.43  ? 9   LYS A N   1 
ATOM   42   C CA  . LYS A 1 23  ? -0.307  19.064  24.934  1.00 14.28  ? 9   LYS A CA  1 
ATOM   43   C C   . LYS A 1 23  ? -1.425  18.139  24.423  1.00 13.36  ? 9   LYS A C   1 
ATOM   44   O O   . LYS A 1 23  ? -1.772  17.156  25.088  1.00 15.62  ? 9   LYS A O   1 
ATOM   45   C CB  . LYS A 1 23  ? -0.864  20.439  25.308  1.00 16.29  ? 9   LYS A CB  1 
ATOM   46   C CG  . LYS A 1 23  ? -2.044  20.353  26.285  1.00 23.20  ? 9   LYS A CG  1 
ATOM   47   C CD  . LYS A 1 23  ? -2.407  21.631  27.034  1.00 35.30  ? 9   LYS A CD  1 
ATOM   48   C CE  . LYS A 1 23  ? -2.389  22.872  26.177  1.00 33.39  ? 9   LYS A CE  1 
ATOM   49   N NZ  . LYS A 1 23  ? -2.900  24.044  26.925  1.00 46.46  ? 9   LYS A NZ  1 
ATOM   50   N N   . ASP A 1 24  ? -1.990  18.451  23.244  1.00 11.67  ? 10  ASP A N   1 
ATOM   51   C CA  . ASP A 1 24  ? -3.174  17.760  22.759  1.00 13.31  ? 10  ASP A CA  1 
ATOM   52   C C   . ASP A 1 24  ? -2.844  16.995  21.465  1.00 12.51  ? 10  ASP A C   1 
ATOM   53   O O   . ASP A 1 24  ? -2.201  17.512  20.538  1.00 14.84  ? 10  ASP A O   1 
ATOM   54   C CB  . ASP A 1 24  ? -4.251  18.804  22.461  1.00 15.83  ? 10  ASP A CB  1 
ATOM   55   C CG  . ASP A 1 24  ? -4.768  19.544  23.694  1.00 19.65  ? 10  ASP A CG  1 
ATOM   56   O OD1 . ASP A 1 24  ? -5.072  18.863  24.680  1.00 22.16  ? 10  ASP A OD1 1 
ATOM   57   O OD2 . ASP A 1 24  ? -4.791  20.793  23.665  1.00 25.86  ? 10  ASP A OD2 1 
ATOM   58   N N   . ILE A 1 25  ? -3.243  15.716  21.436  1.00 12.07  ? 11  ILE A N   1 
ATOM   59   C CA  . ILE A 1 25  ? -3.035  14.851  20.290  1.00 10.79  ? 11  ILE A CA  1 
ATOM   60   C C   . ILE A 1 25  ? -4.406  14.480  19.784  1.00 8.79   ? 11  ILE A C   1 
ATOM   61   O O   . ILE A 1 25  ? -5.290  14.168  20.613  1.00 10.49  ? 11  ILE A O   1 
ATOM   62   C CB  . ILE A 1 25  ? -2.288  13.563  20.721  1.00 11.31  ? 11  ILE A CB  1 
ATOM   63   C CG1 . ILE A 1 25  ? -1.019  13.859  21.554  1.00 15.63  ? 11  ILE A CG1 1 
ATOM   64   C CG2 . ILE A 1 25  ? -2.035  12.654  19.508  1.00 12.35  ? 11  ILE A CG2 1 
ATOM   65   C CD1 . ILE A 1 25  ? 0.001   14.720  20.880  1.00 18.71  ? 11  ILE A CD1 1 
ATOM   66   N N   . ARG A 1 26  ? -4.526  14.402  18.436  1.00 9.65   ? 12  ARG A N   1 
ATOM   67   C CA  . ARG A 1 26  ? -5.715  13.823  17.786  1.00 8.87   ? 12  ARG A CA  1 
ATOM   68   C C   . ARG A 1 26  ? -5.263  12.787  16.773  1.00 7.13   ? 12  ARG A C   1 
ATOM   69   O O   . ARG A 1 26  ? -4.300  13.054  16.036  1.00 9.00   ? 12  ARG A O   1 
ATOM   70   C CB  . ARG A 1 26  ? -6.605  14.869  17.106  1.00 8.92   ? 12  ARG A CB  1 
ATOM   71   C CG  . ARG A 1 26  ? -7.203  15.839  18.131  1.00 11.42  ? 12  ARG A CG  1 
ATOM   72   C CD  . ARG A 1 26  ? -7.510  17.194  17.495  1.00 12.60  ? 12  ARG A CD  1 
ATOM   73   N NE  . ARG A 1 26  ? -8.609  17.091  16.521  1.00 10.48  ? 12  ARG A NE  1 
ATOM   74   C CZ  . ARG A 1 26  ? -9.920  17.081  16.806  1.00 10.24  ? 12  ARG A CZ  1 
ATOM   75   N NH1 . ARG A 1 26  ? -10.359 17.093  18.064  1.00 14.23  ? 12  ARG A NH1 1 
ATOM   76   N NH2 . ARG A 1 26  ? -10.765 17.066  15.779  1.00 11.37  ? 12  ARG A NH2 1 
ATOM   77   N N   . ILE A 1 27  ? -5.925  11.631  16.721  1.00 8.31   ? 13  ILE A N   1 
ATOM   78   C CA  . ILE A 1 27  ? -5.694  10.633  15.672  1.00 7.22   ? 13  ILE A CA  1 
ATOM   79   C C   . ILE A 1 27  ? -7.040  10.292  15.018  1.00 7.50   ? 13  ILE A C   1 
ATOM   80   O O   . ILE A 1 27  ? -7.963  9.931   15.760  1.00 8.80   ? 13  ILE A O   1 
ATOM   81   C CB  . ILE A 1 27  ? -5.046  9.332   16.246  1.00 8.45   ? 13  ILE A CB  1 
ATOM   82   C CG1 . ILE A 1 27  ? -3.667  9.646   16.871  1.00 8.80   ? 13  ILE A CG1 1 
ATOM   83   C CG2 . ILE A 1 27  ? -4.923  8.275   15.170  1.00 10.50  ? 13  ILE A CG2 1 
ATOM   84   C CD1 . ILE A 1 27  ? -3.116  8.510   17.761  1.00 11.92  ? 13  ILE A CD1 1 
ATOM   85   N N   . ILE A 1 28  ? -7.154  10.527  13.696  1.00 6.76   ? 14  ILE A N   1 
ATOM   86   C CA  . ILE A 1 28  ? -8.440  10.495  13.009  1.00 8.19   ? 14  ILE A CA  1 
ATOM   87   C C   . ILE A 1 28  ? -8.294  9.660   11.737  1.00 7.79   ? 14  ILE A C   1 
ATOM   88   O O   . ILE A 1 28  ? -7.651  10.130  10.796  1.00 7.98   ? 14  ILE A O   1 
ATOM   89   C CB  . ILE A 1 28  ? -8.915  11.909  12.613  1.00 7.84   ? 14  ILE A CB  1 
ATOM   90   C CG1 . ILE A 1 28  ? -9.003  12.796  13.869  1.00 9.32   ? 14  ILE A CG1 1 
ATOM   91   C CG2 . ILE A 1 28  ? -10.265 11.815  11.878  1.00 10.84  ? 14  ILE A CG2 1 
ATOM   92   C CD1 . ILE A 1 28  ? -9.190  14.274  13.577  1.00 10.83  ? 14  ILE A CD1 1 
ATOM   93   N N   . PRO A 1 29  ? -8.844  8.436   11.656  1.00 7.26   ? 15  PRO A N   1 
ATOM   94   C CA  . PRO A 1 29  ? -8.801  7.718   10.383  1.00 8.39   ? 15  PRO A CA  1 
ATOM   95   C C   . PRO A 1 29  ? -9.823  8.312   9.415   1.00 7.60   ? 15  PRO A C   1 
ATOM   96   O O   . PRO A 1 29  ? -11.022 8.398   9.741   1.00 8.65   ? 15  PRO A O   1 
ATOM   97   C CB  . PRO A 1 29  ? -9.154  6.268   10.816  1.00 8.55   ? 15  PRO A CB  1 
ATOM   98   C CG  . PRO A 1 29  ? -10.094 6.539   11.985  1.00 12.01  ? 15  PRO A CG  1 
ATOM   99   C CD  . PRO A 1 29  ? -9.459  7.683   12.771  1.00 8.57   ? 15  PRO A CD  1 
ATOM   100  N N   . LEU A 1 30  ? -9.391  8.711   8.225   1.00 7.38   ? 16  LEU A N   1 
ATOM   101  C CA  . LEU A 1 30  ? -10.319 9.118   7.171   1.00 6.84   ? 16  LEU A CA  1 
ATOM   102  C C   . LEU A 1 30  ? -10.495 8.035   6.119   1.00 7.10   ? 16  LEU A C   1 
ATOM   103  O O   . LEU A 1 30  ? -11.420 8.121   5.318   1.00 7.95   ? 16  LEU A O   1 
ATOM   104  C CB  . LEU A 1 30  ? -9.895  10.433  6.527   1.00 7.60   ? 16  LEU A CB  1 
ATOM   105  C CG  . LEU A 1 30  ? -10.005 11.642  7.450   1.00 8.13   ? 16  LEU A CG  1 
ATOM   106  C CD1 . LEU A 1 30  ? -9.570  12.892  6.682   1.00 8.92   ? 16  LEU A CD1 1 
ATOM   107  C CD2 . LEU A 1 30  ? -11.395 11.791  8.054   1.00 9.37   ? 16  LEU A CD2 1 
ATOM   108  N N   . GLY A 1 31  ? -9.638  7.009   6.146   1.00 7.06   ? 17  GLY A N   1 
ATOM   109  C CA  . GLY A 1 31  ? -9.756  5.853   5.256   1.00 6.95   ? 17  GLY A CA  1 
ATOM   110  C C   . GLY A 1 31  ? -8.912  4.739   5.849   1.00 6.31   ? 17  GLY A C   1 
ATOM   111  O O   . GLY A 1 31  ? -7.947  5.002   6.537   1.00 8.47   ? 17  GLY A O   1 
ATOM   112  N N   . GLY A 1 32  ? -9.331  3.487   5.585   1.00 7.34   ? 18  GLY A N   1 
ATOM   113  C CA  . GLY A 1 32  ? -8.503  2.331   5.916   1.00 6.85   ? 18  GLY A CA  1 
ATOM   114  C C   . GLY A 1 32  ? -9.007  1.531   7.095   1.00 8.18   ? 18  GLY A C   1 
ATOM   115  O O   . GLY A 1 32  ? -8.334  0.595   7.543   1.00 9.00   ? 18  GLY A O   1 
ATOM   116  N N   . VAL A 1 33  ? -10.175 1.904   7.670   1.00 8.33   ? 19  VAL A N   1 
ATOM   117  C CA  . VAL A 1 33  ? -10.738 1.107   8.769   1.00 9.85   ? 19  VAL A CA  1 
ATOM   118  C C   . VAL A 1 33  ? -12.171 0.789   8.340   1.00 10.46  ? 19  VAL A C   1 
ATOM   119  O O   . VAL A 1 33  ? -12.833 1.561   7.651   1.00 12.33  ? 19  VAL A O   1 
ATOM   120  C CB  . VAL A 1 33  ? -10.678 1.809   10.144  1.00 10.33  ? 19  VAL A CB  1 
ATOM   121  C CG1 . VAL A 1 33  ? -9.260  1.992   10.583  1.00 11.19  ? 19  VAL A CG1 1 
ATOM   122  C CG2 . VAL A 1 33  ? -11.396 3.165   10.104  1.00 10.50  ? 19  VAL A CG2 1 
ATOM   123  N N   . GLY A 1 34  ? -12.569 -0.448  8.629   1.00 12.04  ? 20  GLY A N   1 
ATOM   124  C CA  . GLY A 1 34  ? -13.865 -0.882  8.172   1.00 13.94  ? 20  GLY A CA  1 
ATOM   125  C C   . GLY A 1 34  ? -13.792 -1.334  6.719   1.00 14.37  ? 20  GLY A C   1 
ATOM   126  O O   . GLY A 1 34  ? -14.801 -1.468  6.046   1.00 18.21  ? 20  GLY A O   1 
ATOM   127  N N   . GLU A 1 35  ? -12.548 -1.512  6.237   1.00 10.37  ? 21  GLU A N   1 
ATOM   128  C CA  . GLU A 1 35  ? -12.249 -1.779  4.813   1.00 11.89  ? 21  GLU A CA  1 
ATOM   129  C C   . GLU A 1 35  ? -10.768 -2.163  4.635   1.00 10.79  ? 21  GLU A C   1 
ATOM   130  O O   . GLU A 1 35  ? -10.027 -1.971  5.583   1.00 11.72  ? 21  GLU A O   1 
ATOM   131  C CB  . GLU A 1 35  ? -12.566 -0.513  3.996   1.00 12.67  ? 21  GLU A CB  1 
ATOM   132  C CG  . GLU A 1 35  ? -11.662 0.668   4.326   1.00 11.72  ? 21  GLU A CG  1 
ATOM   133  C CD  . GLU A 1 35  ? -12.259 2.038   4.054   1.00 11.63  ? 21  GLU A CD  1 
ATOM   134  O OE1 . GLU A 1 35  ? -13.487 2.120   3.892   1.00 13.21  ? 21  GLU A OE1 1 
ATOM   135  O OE2 . GLU A 1 35  ? -11.495 3.007   4.011   1.00 11.13  ? 21  GLU A OE2 1 
ATOM   136  N N   . ILE A 1 36  ? -10.357 -2.533  3.409   1.00 17.93  ? 22  ILE A N   1 
ATOM   137  C CA  . ILE A 1 36  ? -8.985  -3.084  3.123   1.00 24.56  ? 22  ILE A CA  1 
ATOM   138  C C   . ILE A 1 36  ? -8.007  -2.260  2.245   1.00 27.56  ? 22  ILE A C   1 
ATOM   139  O O   . ILE A 1 36  ? -6.997  -2.827  1.754   1.00 28.73  ? 22  ILE A O   1 
ATOM   140  C CB  . ILE A 1 36  ? -9.210  -4.473  2.461   1.00 24.90  ? 22  ILE A CB  1 
ATOM   141  C CG1 . ILE A 1 36  ? -8.470  -5.557  3.243   1.00 29.53  ? 22  ILE A CG1 1 
ATOM   142  C CG2 . ILE A 1 36  ? -8.892  -4.503  0.973   1.00 21.33  ? 22  ILE A CG2 1 
ATOM   143  C CD1 . ILE A 1 36  ? -8.124  -5.140  4.641   1.00 21.67  ? 22  ILE A CD1 1 
ATOM   144  N N   . ALA A 1 37  ? -8.192  -1.005  2.074   1.00 13.90  ? 23  ALA A N   1 
ATOM   145  C CA  . ALA A 1 37  ? -7.365  -0.220  1.147   1.00 12.15  ? 23  ALA A CA  1 
ATOM   146  C C   . ALA A 1 37  ? -7.572  1.211   1.624   1.00 11.22  ? 23  ALA A C   1 
ATOM   147  O O   . ALA A 1 37  ? -7.971  1.367   2.760   1.00 13.57  ? 23  ALA A O   1 
ATOM   148  C CB  . ALA A 1 37  ? -7.873  -0.431  -0.258  1.00 14.56  ? 23  ALA A CB  1 
ATOM   149  N N   . LYS A 1 38  ? -7.291  2.201   0.788   1.00 9.87   ? 24  LYS A N   1 
ATOM   150  C CA  . LYS A 1 38  ? -7.628  3.626   1.099   1.00 8.46   ? 24  LYS A CA  1 
ATOM   151  C C   . LYS A 1 38  ? -7.090  4.091   2.466   1.00 7.92   ? 24  LYS A C   1 
ATOM   152  O O   . LYS A 1 38  ? -7.816  4.716   3.189   1.00 10.47  ? 24  LYS A O   1 
ATOM   153  C CB  . LYS A 1 38  ? -9.157  3.723   0.951   1.00 12.97  ? 24  LYS A CB  1 
ATOM   154  C CG  . LYS A 1 38  ? -9.750  5.122   0.958   1.00 14.18  ? 24  LYS A CG  1 
ATOM   155  C CD  . LYS A 1 38  ? -11.097 5.195   0.260   1.00 15.04  ? 24  LYS A CD  1 
ATOM   156  C CE  . LYS A 1 38  ? -12.127 4.204   0.761   1.00 13.94  ? 24  LYS A CE  1 
ATOM   157  N NZ  . LYS A 1 38  ? -12.697 4.583   2.078   1.00 13.47  ? 24  LYS A NZ  1 
ATOM   158  N N   . ASN A 1 39  ? -5.824  3.813   2.751   1.00 8.07   ? 25  ASN A N   1 
ATOM   159  C CA  . ASN A 1 39  ? -5.276  4.329   3.990   1.00 6.84   ? 25  ASN A CA  1 
ATOM   160  C C   . ASN A 1 39  ? -5.191  5.863   3.972   1.00 6.26   ? 25  ASN A C   1 
ATOM   161  O O   . ASN A 1 39  ? -4.651  6.473   3.075   1.00 7.41   ? 25  ASN A O   1 
ATOM   162  C CB  . ASN A 1 39  ? -3.870  3.746   4.250   1.00 7.67   ? 25  ASN A CB  1 
ATOM   163  C CG  . ASN A 1 39  ? -3.853  2.271   4.580   1.00 8.53   ? 25  ASN A CG  1 
ATOM   164  O OD1 . ASN A 1 39  ? -4.512  1.848   5.517   1.00 10.21  ? 25  ASN A OD1 1 
ATOM   165  N ND2 . ASN A 1 39  ? -3.142  1.504   3.769   1.00 13.40  ? 25  ASN A ND2 1 
ATOM   166  N N   . MET A 1 40  ? -5.665  6.461   5.073   1.00 6.97   ? 26  MET A N   1 
ATOM   167  C CA  . MET A 1 40  ? -5.439  7.894   5.292   1.00 5.84   ? 26  MET A CA  1 
ATOM   168  C C   . MET A 1 40  ? -5.719  8.187   6.760   1.00 6.35   ? 26  MET A C   1 
ATOM   169  O O   . MET A 1 40  ? -6.856  8.049   7.210   1.00 6.83   ? 26  MET A O   1 
ATOM   170  C CB  . MET A 1 40  ? -6.363  8.751   4.431   1.00 7.20   ? 26  MET A CB  1 
ATOM   171  C CG  . MET A 1 40  ? -6.061  10.239  4.680   1.00 7.24   ? 26  MET A CG  1 
ATOM   172  S SD  . MET A 1 40  ? -7.186  11.332  3.746   1.00 8.20   ? 26  MET A SD  1 
ATOM   173  C CE  . MET A 1 40  ? -6.549  11.206  2.060   1.00 8.14   ? 26  MET A CE  1 
ATOM   174  N N   . TYR A 1 41  ? -4.661  8.562   7.470   1.00 5.34   ? 27  TYR A N   1 
ATOM   175  C CA  . TYR A 1 41  ? -4.757  8.777   8.913   1.00 6.39   ? 27  TYR A CA  1 
ATOM   176  C C   . TYR A 1 41  ? -4.275  10.184  9.220   1.00 6.17   ? 27  TYR A C   1 
ATOM   177  O O   . TYR A 1 41  ? -3.142  10.519  8.916   1.00 7.77   ? 27  TYR A O   1 
ATOM   178  C CB  . TYR A 1 41  ? -3.961  7.730   9.709   1.00 7.31   ? 27  TYR A CB  1 
ATOM   179  C CG  . TYR A 1 41  ? -4.326  6.337   9.268   1.00 7.59   ? 27  TYR A CG  1 
ATOM   180  C CD1 . TYR A 1 41  ? -5.545  5.791   9.680   1.00 6.36   ? 27  TYR A CD1 1 
ATOM   181  C CD2 . TYR A 1 41  ? -3.540  5.617   8.376   1.00 6.17   ? 27  TYR A CD2 1 
ATOM   182  C CE1 . TYR A 1 41  ? -5.975  4.551   9.206   1.00 7.29   ? 27  TYR A CE1 1 
ATOM   183  C CE2 . TYR A 1 41  ? -3.949  4.379   7.904   1.00 8.03   ? 27  TYR A CE2 1 
ATOM   184  C CZ  . TYR A 1 41  ? -5.214  3.881   8.257   1.00 6.27   ? 27  TYR A CZ  1 
ATOM   185  O OH  . TYR A 1 41  ? -5.656  2.656   7.793   1.00 8.01   ? 27  TYR A OH  1 
ATOM   186  N N   . ILE A 1 42  ? -5.085  10.971  9.882   1.00 6.17   ? 28  ILE A N   1 
ATOM   187  C CA  . ILE A 1 42  ? -4.733  12.339  10.257  1.00 6.36   ? 28  ILE A CA  1 
ATOM   188  C C   . ILE A 1 42  ? -4.234  12.310  11.678  1.00 7.40   ? 28  ILE A C   1 
ATOM   189  O O   . ILE A 1 42  ? -4.939  11.804  12.569  1.00 8.99   ? 28  ILE A O   1 
ATOM   190  C CB  . ILE A 1 42  ? -5.929  13.304  10.091  1.00 8.37   ? 28  ILE A CB  1 
ATOM   191  C CG1 . ILE A 1 42  ? -6.532  13.209  8.686   1.00 8.79   ? 28  ILE A CG1 1 
ATOM   192  C CG2 . ILE A 1 42  ? -5.542  14.732  10.408  1.00 9.79   ? 28  ILE A CG2 1 
ATOM   193  C CD1 . ILE A 1 42  ? -5.593  13.448  7.515   1.00 9.72   ? 28  ILE A CD1 1 
ATOM   194  N N   . VAL A 1 43  ? -3.029  12.887  11.897  1.00 7.52   ? 29  VAL A N   1 
ATOM   195  C CA  . VAL A 1 43  ? -2.522  13.057  13.248  1.00 7.71   ? 29  VAL A CA  1 
ATOM   196  C C   . VAL A 1 43  ? -2.315  14.555  13.485  1.00 7.73   ? 29  VAL A C   1 
ATOM   197  O O   . VAL A 1 43  ? -1.724  15.229  12.655  1.00 9.08   ? 29  VAL A O   1 
ATOM   198  C CB  . VAL A 1 43  ? -1.204  12.303  13.412  1.00 8.04   ? 29  VAL A CB  1 
ATOM   199  C CG1 . VAL A 1 43  ? -0.589  12.626  14.782  1.00 11.17  ? 29  VAL A CG1 1 
ATOM   200  C CG2 . VAL A 1 43  ? -1.425  10.819  13.231  1.00 10.96  ? 29  VAL A CG2 1 
ATOM   201  N N   . GLU A 1 44  ? -2.868  15.052  14.606  1.00 8.11   ? 30  GLU A N   1 
ATOM   202  C CA  . GLU A 1 44  ? -2.641  16.419  15.015  1.00 8.30   ? 30  GLU A CA  1 
ATOM   203  C C   . GLU A 1 44  ? -1.912  16.432  16.348  1.00 9.43   ? 30  GLU A C   1 
ATOM   204  O O   . GLU A 1 44  ? -2.230  15.679  17.252  1.00 9.22   ? 30  GLU A O   1 
ATOM   205  C CB  . GLU A 1 44  ? -3.962  17.174  15.190  1.00 8.52   ? 30  GLU A CB  1 
ATOM   206  C CG  . GLU A 1 44  ? -4.825  17.159  13.947  1.00 10.65  ? 30  GLU A CG  1 
ATOM   207  C CD  . GLU A 1 44  ? -6.142  17.890  14.074  1.00 11.18  ? 30  GLU A CD  1 
ATOM   208  O OE1 . GLU A 1 44  ? -7.181  17.254  13.934  1.00 10.93  ? 30  GLU A OE1 1 
ATOM   209  O OE2 . GLU A 1 44  ? -6.096  19.115  14.379  1.00 12.08  ? 30  GLU A OE2 1 
ATOM   210  N N   . VAL A 1 45  ? -0.899  17.293  16.397  1.00 9.92   ? 31  VAL A N   1 
ATOM   211  C CA  . VAL A 1 45  ? -0.146  17.561  17.623  1.00 9.21   ? 31  VAL A CA  1 
ATOM   212  C C   . VAL A 1 45  ? -0.240  19.070  17.839  1.00 9.94   ? 31  VAL A C   1 
ATOM   213  O O   . VAL A 1 45  ? 0.321   19.852  17.077  1.00 10.98  ? 31  VAL A O   1 
ATOM   214  C CB  . VAL A 1 45  ? 1.313   17.091  17.554  1.00 9.96   ? 31  VAL A CB  1 
ATOM   215  C CG1 . VAL A 1 45  ? 1.999   17.363  18.889  1.00 11.81  ? 31  VAL A CG1 1 
ATOM   216  C CG2 . VAL A 1 45  ? 1.393   15.605  17.196  1.00 11.02  ? 31  VAL A CG2 1 
ATOM   217  N N   . ASP A 1 46  ? -1.087  19.452  18.822  1.00 11.88  ? 32  ASP A N   1 
ATOM   218  C CA  . ASP A 1 46  ? -1.493  20.844  18.996  1.00 10.43  ? 32  ASP A CA  1 
ATOM   219  C C   . ASP A 1 46  ? -1.914  21.400  17.634  1.00 12.81  ? 32  ASP A C   1 
ATOM   220  O O   . ASP A 1 46  ? -2.788  20.822  16.985  1.00 12.89  ? 32  ASP A O   1 
ATOM   221  C CB  . ASP A 1 46  ? -0.404  21.621  19.750  1.00 15.36  ? 32  ASP A CB  1 
ATOM   222  C CG  . ASP A 1 46  ? -0.207  20.966  21.112  1.00 17.28  ? 32  ASP A CG  1 
ATOM   223  O OD1 . ASP A 1 46  ? -1.250  20.787  21.827  1.00 17.05  ? 32  ASP A OD1 1 
ATOM   224  O OD2 . ASP A 1 46  ? 0.943   20.692  21.459  1.00 22.59  ? 32  ASP A OD2 1 
ATOM   225  N N   . ASP A 1 47  ? -1.325  22.531  17.202  1.00 11.77  ? 33  ASP A N   1 
ATOM   226  C CA  . ASP A 1 47  ? -1.807  23.242  16.023  1.00 12.76  ? 33  ASP A CA  1 
ATOM   227  C C   . ASP A 1 47  ? -1.136  22.772  14.726  1.00 11.33  ? 33  ASP A C   1 
ATOM   228  O O   . ASP A 1 47  ? -1.275  23.445  13.697  1.00 12.05  ? 33  ASP A O   1 
ATOM   229  C CB  . ASP A 1 47  ? -1.670  24.751  16.189  1.00 12.90  ? 33  ASP A CB  1 
ATOM   230  C CG  . ASP A 1 47  ? -0.258  25.240  16.435  1.00 18.42  ? 33  ASP A CG  1 
ATOM   231  O OD1 . ASP A 1 47  ? 0.640   24.402  16.705  1.00 25.17  ? 33  ASP A OD1 1 
ATOM   232  O OD2 . ASP A 1 47  ? -0.075  26.476  16.375  1.00 25.42  ? 33  ASP A OD2 1 
ATOM   233  N N   . GLU A 1 48  ? -0.517  21.576  14.709  1.00 10.96  ? 34  GLU A N   1 
ATOM   234  C CA  . GLU A 1 48  ? 0.100   21.031  13.499  1.00 9.27   ? 34  GLU A CA  1 
ATOM   235  C C   . GLU A 1 48  ? -0.630  19.730  13.154  1.00 9.65   ? 34  GLU A C   1 
ATOM   236  O O   . GLU A 1 48  ? -0.775  18.826  13.975  1.00 11.06  ? 34  GLU A O   1 
ATOM   237  C CB  . GLU A 1 48  ? 1.600   20.803  13.697  1.00 10.99  ? 34  GLU A CB  1 
ATOM   238  C CG  . GLU A 1 48  ? 2.341   22.135  13.743  1.00 14.40  ? 34  GLU A CG  1 
ATOM   239  C CD  . GLU A 1 48  ? 3.852   21.944  13.753  1.00 13.82  ? 34  GLU A CD  1 
ATOM   240  O OE1 . GLU A 1 48  ? 4.341   21.236  14.654  1.00 20.55  ? 34  GLU A OE1 1 
ATOM   241  O OE2 . GLU A 1 48  ? 4.528   22.491  12.861  1.00 20.22  ? 34  GLU A OE2 1 
ATOM   242  N N   . MET A 1 49  ? -1.028  19.639  11.886  1.00 8.78   ? 35  MET A N   1 
ATOM   243  C CA  . MET A 1 49  ? -1.728  18.490  11.354  1.00 8.25   ? 35  MET A CA  1 
ATOM   244  C C   . MET A 1 49  ? -0.873  17.820  10.272  1.00 8.19   ? 35  MET A C   1 
ATOM   245  O O   . MET A 1 49  ? -0.268  18.472  9.422   1.00 9.47   ? 35  MET A O   1 
ATOM   246  C CB  . MET A 1 49  ? -3.048  18.995  10.730  1.00 9.26   ? 35  MET A CB  1 
ATOM   247  C CG  . MET A 1 49  ? -3.879  17.864  10.102  1.00 9.19   ? 35  MET A CG  1 
ATOM   248  S SD  . MET A 1 49  ? -5.396  18.388  9.286   1.00 13.03  ? 35  MET A SD  1 
ATOM   249  C CE  . MET A 1 49  ? -6.417  18.860  10.657  1.00 16.54  ? 35  MET A CE  1 
ATOM   250  N N   . PHE A 1 50  ? -0.904  16.468  10.264  1.00 7.49   ? 36  PHE A N   1 
ATOM   251  C CA  . PHE A 1 50  ? -0.135  15.623  9.354   1.00 7.49   ? 36  PHE A CA  1 
ATOM   252  C C   . PHE A 1 50  ? -1.080  14.580  8.753   1.00 8.12   ? 36  PHE A C   1 
ATOM   253  O O   . PHE A 1 50  ? -1.881  13.978  9.467   1.00 9.98   ? 36  PHE A O   1 
ATOM   254  C CB  . PHE A 1 50  ? 0.993   14.939  10.133  1.00 8.60   ? 36  PHE A CB  1 
ATOM   255  C CG  . PHE A 1 50  ? 1.883   15.870  10.905  1.00 9.02   ? 36  PHE A CG  1 
ATOM   256  C CD1 . PHE A 1 50  ? 2.930   16.502  10.228  1.00 14.84  ? 36  PHE A CD1 1 
ATOM   257  C CD2 . PHE A 1 50  ? 1.613   16.250  12.209  1.00 10.96  ? 36  PHE A CD2 1 
ATOM   258  C CE1 . PHE A 1 50  ? 3.707   17.460  10.866  1.00 14.99  ? 36  PHE A CE1 1 
ATOM   259  C CE2 . PHE A 1 50  ? 2.409   17.202  12.862  1.00 13.39  ? 36  PHE A CE2 1 
ATOM   260  C CZ  . PHE A 1 50  ? 3.436   17.790  12.169  1.00 13.60  ? 36  PHE A CZ  1 
ATOM   261  N N   . MET A 1 51  ? -0.948  14.333  7.466   1.00 6.72   ? 37  MET A N   1 
ATOM   262  C CA  . MET A 1 51  ? -1.707  13.305  6.766   1.00 6.78   ? 37  MET A CA  1 
ATOM   263  C C   . MET A 1 51  ? -0.772  12.148  6.494   1.00 6.92   ? 37  MET A C   1 
ATOM   264  O O   . MET A 1 51  ? 0.248   12.325  5.803   1.00 7.49   ? 37  MET A O   1 
ATOM   265  C CB  . MET A 1 51  ? -2.275  13.870  5.470   1.00 7.69   ? 37  MET A CB  1 
ATOM   266  C CG  . MET A 1 51  ? -3.048  12.859  4.658   1.00 8.06   ? 37  MET A CG  1 
ATOM   267  S SD  . MET A 1 51  ? -3.610  13.511  3.041   1.00 8.64   ? 37  MET A SD  1 
ATOM   268  C CE  . MET A 1 51  ? -4.989  14.566  3.547   1.00 11.27  ? 37  MET A CE  1 
ATOM   269  N N   . LEU A 1 52  ? -1.132  10.986  7.022   1.00 6.11   ? 38  LEU A N   1 
ATOM   270  C CA  . LEU A 1 52  ? -0.367  9.753   6.856   1.00 6.94   ? 38  LEU A CA  1 
ATOM   271  C C   . LEU A 1 52  ? -1.050  8.837   5.838   1.00 6.79   ? 38  LEU A C   1 
ATOM   272  O O   . LEU A 1 52  ? -2.128  8.297   6.132   1.00 7.17   ? 38  LEU A O   1 
ATOM   273  C CB  . LEU A 1 52  ? -0.206  9.052   8.197   1.00 8.45   ? 38  LEU A CB  1 
ATOM   274  C CG  . LEU A 1 52  ? 0.414   9.866   9.315   1.00 9.40   ? 38  LEU A CG  1 
ATOM   275  C CD1 . LEU A 1 52  ? 0.610   9.074   10.581  1.00 9.94   ? 38  LEU A CD1 1 
ATOM   276  C CD2 . LEU A 1 52  ? 1.665   10.593  8.886   1.00 14.84  ? 38  LEU A CD2 1 
ATOM   277  N N   . ASP A 1 53  ? -0.449  8.779   4.649   1.00 5.98   ? 39  ASP A N   1 
ATOM   278  C CA  . ASP A 1 53  ? -0.962  8.104   3.458   1.00 5.28   ? 39  ASP A CA  1 
ATOM   279  C C   . ASP A 1 53  ? -2.221  8.778   2.890   1.00 6.23   ? 39  ASP A C   1 
ATOM   280  O O   . ASP A 1 53  ? -2.911  9.576   3.543   1.00 6.47   ? 39  ASP A O   1 
ATOM   281  C CB  . ASP A 1 53  ? -1.164  6.585   3.714   1.00 6.71   ? 39  ASP A CB  1 
ATOM   282  C CG  . ASP A 1 53  ? 0.162   5.833   3.691   1.00 6.78   ? 39  ASP A CG  1 
ATOM   283  O OD1 . ASP A 1 53  ? 1.114   6.366   3.155   1.00 8.90   ? 39  ASP A OD1 1 
ATOM   284  O OD2 . ASP A 1 53  ? 0.201   4.648   4.143   1.00 7.84   ? 39  ASP A OD2 1 
ATOM   285  N N   . ALA A 1 54  ? -2.473  8.436   1.625   1.00 5.96   ? 40  ALA A N   1 
ATOM   286  C CA  . ALA A 1 54  ? -3.642  8.926   0.920   1.00 6.61   ? 40  ALA A CA  1 
ATOM   287  C C   . ALA A 1 54  ? -3.995  7.953   -0.198  1.00 6.76   ? 40  ALA A C   1 
ATOM   288  O O   . ALA A 1 54  ? -3.727  8.180   -1.357  1.00 7.70   ? 40  ALA A O   1 
ATOM   289  C CB  . ALA A 1 54  ? -3.380  10.322  0.360   1.00 9.01   ? 40  ALA A CB  1 
ATOM   290  N N   . GLY A 1 55  ? -4.497  6.777   0.221   1.00 7.06   ? 41  GLY A N   1 
ATOM   291  C CA  . GLY A 1 55  ? -4.702  5.681   -0.707  1.00 6.53   ? 41  GLY A CA  1 
ATOM   292  C C   . GLY A 1 55  ? -6.054  5.713   -1.407  1.00 9.22   ? 41  GLY A C   1 
ATOM   293  O O   . GLY A 1 55  ? -6.951  6.488   -1.007  1.00 9.59   ? 41  GLY A O   1 
ATOM   294  N N   . LEU A 1 56  ? -6.183  4.831   -2.442  1.00 7.18   ? 42  LEU A N   1 
ATOM   295  C CA  . LEU A 1 56  ? -7.463  4.564   -3.078  1.00 8.41   ? 42  LEU A CA  1 
ATOM   296  C C   . LEU A 1 56  ? -7.960  3.176   -2.680  1.00 7.18   ? 42  LEU A C   1 
ATOM   297  O O   . LEU A 1 56  ? -7.232  2.391   -2.092  1.00 9.51   ? 42  LEU A O   1 
ATOM   298  C CB  . LEU A 1 56  ? -7.421  4.717   -4.613  1.00 8.49   ? 42  LEU A CB  1 
ATOM   299  C CG  . LEU A 1 56  ? -6.508  3.746   -5.378  1.00 9.15   ? 42  LEU A CG  1 
ATOM   300  C CD1 . LEU A 1 56  ? -7.093  2.311   -5.505  1.00 11.03  ? 42  LEU A CD1 1 
ATOM   301  C CD2 . LEU A 1 56  ? -6.265  4.295   -6.788  1.00 12.65  ? 42  LEU A CD2 1 
ATOM   302  N N   . MET A 1 57  ? -9.255  2.938   -3.006  1.00 8.64   ? 43  MET A N   1 
ATOM   303  C CA  . MET A 1 57  ? -9.838  1.613   -2.979  1.00 9.84   ? 43  MET A CA  1 
ATOM   304  C C   . MET A 1 57  ? -10.511 1.383   -4.317  1.00 12.84  ? 43  MET A C   1 
ATOM   305  O O   . MET A 1 57  ? -11.070 2.300   -4.910  1.00 12.37  ? 43  MET A O   1 
ATOM   306  C CB  . MET A 1 57  ? -10.868 1.540   -1.840  1.00 12.88  ? 43  MET A CB  1 
ATOM   307  C CG  . MET A 1 57  ? -11.569 0.176   -1.660  1.00 13.19  ? 43  MET A CG  1 
ATOM   308  S SD  . MET A 1 57  ? -12.762 0.325   -0.293  1.00 15.85  ? 43  MET A SD  1 
ATOM   309  C CE  . MET A 1 57  ? -14.133 1.007   -1.188  1.00 15.78  ? 43  MET A CE  1 
ATOM   310  N N   . PHE A 1 58  ? -10.454 0.127   -4.785  1.00 12.58  ? 44  PHE A N   1 
ATOM   311  C CA  . PHE A 1 58  ? -11.142 -0.193  -6.017  1.00 16.83  ? 44  PHE A CA  1 
ATOM   312  C C   . PHE A 1 58  ? -12.625 -0.391  -5.726  1.00 15.43  ? 44  PHE A C   1 
ATOM   313  O O   . PHE A 1 58  ? -12.993 -0.796  -4.624  1.00 18.11  ? 44  PHE A O   1 
ATOM   314  C CB  . PHE A 1 58  ? -10.421 -1.351  -6.719  1.00 19.47  ? 44  PHE A CB  1 
ATOM   315  C CG  . PHE A 1 58  ? -9.046  -0.975  -7.200  1.00 26.85  ? 44  PHE A CG  1 
ATOM   316  C CD1 . PHE A 1 58  ? -8.899  -0.053  -8.224  1.00 28.67  ? 44  PHE A CD1 1 
ATOM   317  C CD2 . PHE A 1 58  ? -7.911  -1.506  -6.609  1.00 25.13  ? 44  PHE A CD2 1 
ATOM   318  C CE1 . PHE A 1 58  ? -7.638  0.303   -8.686  1.00 33.38  ? 44  PHE A CE1 1 
ATOM   319  C CE2 . PHE A 1 58  ? -6.645  -1.143  -7.064  1.00 36.43  ? 44  PHE A CE2 1 
ATOM   320  C CZ  . PHE A 1 58  ? -6.514  -0.239  -8.099  1.00 40.85  ? 44  PHE A CZ  1 
ATOM   321  N N   . PRO A 1 59  ? -13.516 -0.072  -6.699  1.00 20.26  ? 45  PRO A N   1 
ATOM   322  C CA  . PRO A 1 59  ? -14.967 -0.134  -6.477  1.00 24.15  ? 45  PRO A CA  1 
ATOM   323  C C   . PRO A 1 59  ? -15.478 -1.496  -5.999  1.00 24.30  ? 45  PRO A C   1 
ATOM   324  O O   . PRO A 1 59  ? -14.986 -2.541  -6.435  1.00 31.15  ? 45  PRO A O   1 
ATOM   325  C CB  . PRO A 1 59  ? -15.549 0.197   -7.859  1.00 33.58  ? 45  PRO A CB  1 
ATOM   326  C CG  . PRO A 1 59  ? -14.455 0.956   -8.566  1.00 31.80  ? 45  PRO A CG  1 
ATOM   327  C CD  . PRO A 1 59  ? -13.161 0.342   -8.064  1.00 27.97  ? 45  PRO A CD  1 
ATOM   328  N N   . GLU A 1 60  ? -16.453 -1.446  -5.084  1.00 34.83  ? 46  GLU A N   1 
ATOM   329  C CA  . GLU A 1 60  ? -17.111 -2.621  -4.550  1.00 48.18  ? 46  GLU A CA  1 
ATOM   330  C C   . GLU A 1 60  ? -18.043 -3.175  -5.624  1.00 61.12  ? 46  GLU A C   1 
ATOM   331  O O   . GLU A 1 60  ? -18.438 -2.433  -6.527  1.00 39.91  ? 46  GLU A O   1 
ATOM   332  C CB  . GLU A 1 60  ? -17.892 -2.197  -3.310  1.00 56.19  ? 46  GLU A CB  1 
ATOM   333  C CG  . GLU A 1 60  ? -17.262 -0.991  -2.631  1.00 54.38  ? 46  GLU A CG  1 
ATOM   334  C CD  . GLU A 1 60  ? -17.551 -0.815  -1.152  1.00 67.72  ? 46  GLU A CD  1 
ATOM   335  O OE1 . GLU A 1 60  ? -18.027 -1.776  -0.519  1.00 88.56  ? 46  GLU A OE1 1 
ATOM   336  O OE2 . GLU A 1 60  ? -17.300 0.307   -0.639  1.00 73.14  ? 46  GLU A OE2 1 
ATOM   337  N N   . ASP A 1 61  ? -18.384 -4.472  -5.507  1.00 51.75  ? 47  ASP A N   1 
ATOM   338  C CA  . ASP A 1 61  ? -19.186 -5.187  -6.494  1.00 70.18  ? 47  ASP A CA  1 
ATOM   339  C C   . ASP A 1 61  ? -20.421 -4.351  -6.816  1.00 82.70  ? 47  ASP A C   1 
ATOM   340  O O   . ASP A 1 61  ? -20.806 -4.198  -7.983  1.00 85.76  ? 47  ASP A O   1 
ATOM   341  C CB  . ASP A 1 61  ? -19.608 -6.577  -5.994  1.00 80.69  ? 47  ASP A CB  1 
ATOM   342  N N   . GLU A 1 62  ? -21.019 -3.799  -5.750  1.00 57.57  ? 48  GLU A N   1 
ATOM   343  C CA  . GLU A 1 62  ? -22.308 -3.119  -5.848  1.00 76.56  ? 48  GLU A CA  1 
ATOM   344  C C   . GLU A 1 62  ? -22.183 -1.709  -6.436  1.00 82.88  ? 48  GLU A C   1 
ATOM   345  O O   . GLU A 1 62  ? -23.159 -0.967  -6.406  1.00 81.50  ? 48  GLU A O   1 
ATOM   346  N N   . MET A 1 63  ? -21.002 -1.346  -6.968  1.00 64.85  ? 49  MET A N   1 
ATOM   347  C CA  . MET A 1 63  ? -20.754 -0.027  -7.542  1.00 66.01  ? 49  MET A CA  1 
ATOM   348  C C   . MET A 1 63  ? -20.663 -0.130  -9.068  1.00 71.43  ? 49  MET A C   1 
ATOM   349  O O   . MET A 1 63  ? -19.926 -0.973  -9.584  1.00 91.81  ? 49  MET A O   1 
ATOM   350  C CB  . MET A 1 63  ? -19.440 0.567   -7.015  1.00 75.07  ? 49  MET A CB  1 
ATOM   351  C CG  . MET A 1 63  ? -19.544 1.224   -5.644  1.00 73.13  ? 49  MET A CG  1 
ATOM   352  S SD  . MET A 1 63  ? -17.911 1.691   -4.972  1.00 49.49  ? 49  MET A SD  1 
ATOM   353  C CE  . MET A 1 63  ? -18.406 2.583   -3.493  1.00 91.36  ? 49  MET A CE  1 
ATOM   354  N N   . LEU A 1 64  ? -21.393 0.755   -9.770  1.00 53.44  ? 50  LEU A N   1 
ATOM   355  C CA  . LEU A 1 64  ? -21.389 0.814   -11.229 1.00 62.45  ? 50  LEU A CA  1 
ATOM   356  C C   . LEU A 1 64  ? -21.068 2.234   -11.690 1.00 70.21  ? 50  LEU A C   1 
ATOM   357  O O   . LEU A 1 64  ? -21.551 3.198   -11.101 1.00 64.60  ? 50  LEU A O   1 
ATOM   358  C CB  . LEU A 1 64  ? -22.766 0.369   -11.751 1.00 73.69  ? 50  LEU A CB  1 
ATOM   359  N N   . GLY A 1 65  ? -20.224 2.356   -12.728 1.00 68.17  ? 51  GLY A N   1 
ATOM   360  C CA  . GLY A 1 65  ? -19.867 3.637   -13.325 1.00 70.85  ? 51  GLY A CA  1 
ATOM   361  C C   . GLY A 1 65  ? -18.788 4.330   -12.496 1.00 59.51  ? 51  GLY A C   1 
ATOM   362  O O   . GLY A 1 65  ? -18.592 5.547   -12.583 1.00 45.22  ? 51  GLY A O   1 
ATOM   363  N N   . VAL A 1 66  ? -18.105 3.520   -11.686 1.00 54.87  ? 52  VAL A N   1 
ATOM   364  C CA  . VAL A 1 66  ? -17.091 4.065   -10.778 1.00 32.24  ? 52  VAL A CA  1 
ATOM   365  C C   . VAL A 1 66  ? -15.733 3.447   -11.124 1.00 27.57  ? 52  VAL A C   1 
ATOM   366  O O   . VAL A 1 66  ? -15.642 2.231   -11.308 1.00 26.43  ? 52  VAL A O   1 
ATOM   367  C CB  . VAL A 1 66  ? -17.455 3.827   -9.296  1.00 24.87  ? 52  VAL A CB  1 
ATOM   368  C CG1 . VAL A 1 66  ? -16.399 4.363   -8.325  1.00 28.12  ? 52  VAL A CG1 1 
ATOM   369  C CG2 . VAL A 1 66  ? -18.841 4.363   -8.957  1.00 29.64  ? 52  VAL A CG2 1 
ATOM   370  N N   . ASP A 1 67  ? -14.694 4.301   -11.231 1.00 24.04  ? 53  ASP A N   1 
ATOM   371  C CA  . ASP A 1 67  ? -13.311 3.873   -11.467 1.00 20.86  ? 53  ASP A CA  1 
ATOM   372  C C   . ASP A 1 67  ? -12.592 3.555   -10.148 1.00 19.39  ? 53  ASP A C   1 
ATOM   373  O O   . ASP A 1 67  ? -12.052 2.468   -9.967  1.00 23.14  ? 53  ASP A O   1 
ATOM   374  C CB  . ASP A 1 67  ? -12.550 4.908   -12.300 1.00 27.51  ? 53  ASP A CB  1 
ATOM   375  C CG  . ASP A 1 67  ? -12.943 4.950   -13.765 1.00 42.71  ? 53  ASP A CG  1 
ATOM   376  O OD1 . ASP A 1 67  ? -13.612 3.975   -14.239 1.00 45.89  ? 53  ASP A OD1 1 
ATOM   377  O OD2 . ASP A 1 67  ? -12.587 5.963   -14.417 1.00 48.65  ? 53  ASP A OD2 1 
ATOM   378  N N   . ILE A 1 68  ? -12.599 4.517   -9.218  1.00 17.52  ? 54  ILE A N   1 
ATOM   379  C CA  . ILE A 1 68  ? -11.900 4.348   -7.935  1.00 13.50  ? 54  ILE A CA  1 
ATOM   380  C C   . ILE A 1 68  ? -12.711 5.071   -6.861  1.00 13.19  ? 54  ILE A C   1 
ATOM   381  O O   . ILE A 1 68  ? -13.581 5.885   -7.161  1.00 14.06  ? 54  ILE A O   1 
ATOM   382  C CB  . ILE A 1 68  ? -10.419 4.841   -7.982  1.00 12.87  ? 54  ILE A CB  1 
ATOM   383  C CG1 . ILE A 1 68  ? -10.350 6.376   -8.079  1.00 14.67  ? 54  ILE A CG1 1 
ATOM   384  C CG2 . ILE A 1 68  ? -9.585  4.145   -9.066  1.00 14.78  ? 54  ILE A CG2 1 
ATOM   385  C CD1 . ILE A 1 68  ? -8.941  6.947   -7.903  1.00 13.68  ? 54  ILE A CD1 1 
ATOM   386  N N   . VAL A 1 69  ? -12.351 4.757   -5.612  1.00 9.61   ? 55  VAL A N   1 
ATOM   387  C CA  . VAL A 1 69  ? -12.924 5.363   -4.429  1.00 10.86  ? 55  VAL A CA  1 
ATOM   388  C C   . VAL A 1 69  ? -11.782 5.994   -3.632  1.00 9.08   ? 55  VAL A C   1 
ATOM   389  O O   . VAL A 1 69  ? -10.751 5.365   -3.395  1.00 10.99  ? 55  VAL A O   1 
ATOM   390  C CB  . VAL A 1 69  ? -13.660 4.297   -3.592  1.00 10.75  ? 55  VAL A CB  1 
ATOM   391  C CG1 . VAL A 1 69  ? -14.398 4.964   -2.440  1.00 11.54  ? 55  VAL A CG1 1 
ATOM   392  C CG2 . VAL A 1 69  ? -14.652 3.485   -4.446  1.00 13.72  ? 55  VAL A CG2 1 
ATOM   393  N N   . ILE A 1 70  ? -11.987 7.259   -3.224  1.00 9.06   ? 56  ILE A N   1 
ATOM   394  C CA  . ILE A 1 70  ? -10.964 7.949   -2.431  1.00 8.92   ? 56  ILE A CA  1 
ATOM   395  C C   . ILE A 1 70  ? -11.591 8.459   -1.153  1.00 7.63   ? 56  ILE A C   1 
ATOM   396  O O   . ILE A 1 70  ? -12.827 8.595   -1.029  1.00 8.25   ? 56  ILE A O   1 
ATOM   397  C CB  . ILE A 1 70  ? -10.290 9.084   -3.228  1.00 9.08   ? 56  ILE A CB  1 
ATOM   398  C CG1 . ILE A 1 70  ? -11.288 10.215  -3.515  1.00 11.31  ? 56  ILE A CG1 1 
ATOM   399  C CG2 . ILE A 1 70  ? -9.636  8.483   -4.498  1.00 10.05  ? 56  ILE A CG2 1 
ATOM   400  C CD1 . ILE A 1 70  ? -10.634 11.446  -4.227  1.00 13.31  ? 56  ILE A CD1 1 
ATOM   401  N N   . PRO A 1 71  ? -10.800 8.865   -0.146  1.00 7.34   ? 57  PRO A N   1 
ATOM   402  C CA  . PRO A 1 71  ? -11.400 9.441   1.068   1.00 7.34   ? 57  PRO A CA  1 
ATOM   403  C C   . PRO A 1 71  ? -11.978 10.840  0.849   1.00 8.28   ? 57  PRO A C   1 
ATOM   404  O O   . PRO A 1 71  ? -11.486 11.629  0.053   1.00 9.32   ? 57  PRO A O   1 
ATOM   405  C CB  . PRO A 1 71  ? -10.182 9.605   1.998   1.00 7.76   ? 57  PRO A CB  1 
ATOM   406  C CG  . PRO A 1 71  ? -9.220  8.538   1.485   1.00 8.61   ? 57  PRO A CG  1 
ATOM   407  C CD  . PRO A 1 71  ? -9.344  8.698   -0.028  1.00 9.63   ? 57  PRO A CD  1 
ATOM   408  N N   . ASP A 1 72  ? -13.035 11.132  1.627   1.00 7.94   ? 58  ASP A N   1 
ATOM   409  C CA  . ASP A 1 72  ? -13.541 12.487  1.817   1.00 8.20   ? 58  ASP A CA  1 
ATOM   410  C C   . ASP A 1 72  ? -12.568 13.219  2.749   1.00 8.65   ? 58  ASP A C   1 
ATOM   411  O O   . ASP A 1 72  ? -12.333 12.804  3.882   1.00 8.47   ? 58  ASP A O   1 
ATOM   412  C CB  . ASP A 1 72  ? -14.959 12.368  2.419   1.00 8.46   ? 58  ASP A CB  1 
ATOM   413  C CG  . ASP A 1 72  ? -15.646 13.705  2.617   1.00 9.94   ? 58  ASP A CG  1 
ATOM   414  O OD1 . ASP A 1 72  ? -15.034 14.772  2.410   1.00 10.61  ? 58  ASP A OD1 1 
ATOM   415  O OD2 . ASP A 1 72  ? -16.824 13.682  2.962   1.00 12.22  ? 58  ASP A OD2 1 
ATOM   416  N N   . ILE A 1 73  ? -11.997 14.332  2.256   1.00 7.46   ? 59  ILE A N   1 
ATOM   417  C CA  . ILE A 1 73  ? -11.053 15.097  3.052   1.00 6.78   ? 59  ILE A CA  1 
ATOM   418  C C   . ILE A 1 73  ? -11.600 16.446  3.503   1.00 7.86   ? 59  ILE A C   1 
ATOM   419  O O   . ILE A 1 73  ? -10.838 17.352  3.867   1.00 7.74   ? 59  ILE A O   1 
ATOM   420  C CB  . ILE A 1 73  ? -9.693  15.282  2.339   1.00 7.67   ? 59  ILE A CB  1 
ATOM   421  C CG1 . ILE A 1 73  ? -9.767  16.089  1.050   1.00 10.53  ? 59  ILE A CG1 1 
ATOM   422  C CG2 . ILE A 1 73  ? -9.013  13.930  2.144   1.00 9.30   ? 59  ILE A CG2 1 
ATOM   423  C CD1 . ILE A 1 73  ? -8.386  16.634  0.619   1.00 13.92  ? 59  ILE A CD1 1 
ATOM   424  N N   . GLN A 1 74  ? -12.938 16.589  3.528   1.00 7.37   ? 60  GLN A N   1 
ATOM   425  C CA  . GLN A 1 74  ? -13.527 17.840  3.965   1.00 7.21   ? 60  GLN A CA  1 
ATOM   426  C C   . GLN A 1 74  ? -12.964 18.303  5.315   1.00 7.52   ? 60  GLN A C   1 
ATOM   427  O O   . GLN A 1 74  ? -12.804 19.508  5.556   1.00 8.17   ? 60  GLN A O   1 
ATOM   428  C CB  . GLN A 1 74  ? -15.048 17.650  4.035   1.00 7.92   ? 60  GLN A CB  1 
ATOM   429  C CG  . GLN A 1 74  ? -15.794 18.862  4.625   1.00 8.23   ? 60  GLN A CG  1 
ATOM   430  C CD  . GLN A 1 74  ? -15.699 20.119  3.787   1.00 8.72   ? 60  GLN A CD  1 
ATOM   431  O OE1 . GLN A 1 74  ? -15.234 20.151  2.651   1.00 8.82   ? 60  GLN A OE1 1 
ATOM   432  N NE2 . GLN A 1 74  ? -16.198 21.206  4.397   1.00 9.60   ? 60  GLN A NE2 1 
ATOM   433  N N   . TYR A 1 75  ? -12.765 17.386  6.301   1.00 7.90   ? 61  TYR A N   1 
ATOM   434  C CA  . TYR A 1 75  ? -12.216 17.803  7.583   1.00 8.66   ? 61  TYR A CA  1 
ATOM   435  C C   . TYR A 1 75  ? -10.836 18.467  7.437   1.00 7.45   ? 61  TYR A C   1 
ATOM   436  O O   . TYR A 1 75  ? -10.553 19.482  8.091   1.00 8.67   ? 61  TYR A O   1 
ATOM   437  C CB  . TYR A 1 75  ? -12.102 16.609  8.540   1.00 9.03   ? 61  TYR A CB  1 
ATOM   438  C CG  . TYR A 1 75  ? -11.437 16.972  9.838   1.00 8.31   ? 61  TYR A CG  1 
ATOM   439  C CD1 . TYR A 1 75  ? -12.084 17.770  10.774  1.00 10.68  ? 61  TYR A CD1 1 
ATOM   440  C CD2 . TYR A 1 75  ? -10.087 16.645  10.031  1.00 10.32  ? 61  TYR A CD2 1 
ATOM   441  C CE1 . TYR A 1 75  ? -11.442 18.145  11.946  1.00 10.41  ? 61  TYR A CE1 1 
ATOM   442  C CE2 . TYR A 1 75  ? -9.450  17.001  11.218  1.00 9.60   ? 61  TYR A CE2 1 
ATOM   443  C CZ  . TYR A 1 75  ? -10.107 17.803  12.145  1.00 9.23   ? 61  TYR A CZ  1 
ATOM   444  O OH  . TYR A 1 75  ? -9.512  18.178  13.340  1.00 11.44  ? 61  TYR A OH  1 
ATOM   445  N N   . VAL A 1 76  ? -10.018 17.936  6.523   1.00 7.71   ? 62  VAL A N   1 
ATOM   446  C CA  . VAL A 1 76  ? -8.693  18.522  6.322   1.00 8.02   ? 62  VAL A CA  1 
ATOM   447  C C   . VAL A 1 76  ? -8.893  19.879  5.629   1.00 7.87   ? 62  VAL A C   1 
ATOM   448  O O   . VAL A 1 76  ? -8.225  20.840  6.036   1.00 9.67   ? 62  VAL A O   1 
ATOM   449  C CB  . VAL A 1 76  ? -7.828  17.598  5.442   1.00 8.96   ? 62  VAL A CB  1 
ATOM   450  C CG1 . VAL A 1 76  ? -6.419  18.149  5.159   1.00 8.96   ? 62  VAL A CG1 1 
ATOM   451  C CG2 . VAL A 1 76  ? -7.651  16.242  6.103   1.00 10.36  ? 62  VAL A CG2 1 
ATOM   452  N N   . ILE A 1 77  ? -9.782  19.986  4.600   1.00 7.35   ? 63  ILE A N   1 
ATOM   453  C CA  . ILE A 1 77  ? -9.988  21.266  3.941   1.00 8.61   ? 63  ILE A CA  1 
ATOM   454  C C   . ILE A 1 77  ? -10.420 22.324  4.964   1.00 8.50   ? 63  ILE A C   1 
ATOM   455  O O   . ILE A 1 77  ? -9.977  23.474  4.891   1.00 10.37  ? 63  ILE A O   1 
ATOM   456  C CB  . ILE A 1 77  ? -11.049 21.117  2.847   1.00 8.16   ? 63  ILE A CB  1 
ATOM   457  C CG1 . ILE A 1 77  ? -10.465 20.276  1.708   1.00 9.76   ? 63  ILE A CG1 1 
ATOM   458  C CG2 . ILE A 1 77  ? -11.502 22.508  2.340   1.00 10.39  ? 63  ILE A CG2 1 
ATOM   459  C CD1 . ILE A 1 77  ? -11.514 19.839  0.668   1.00 12.98  ? 63  ILE A CD1 1 
ATOM   460  N N   . GLU A 1 78  ? -11.300 21.963  5.930   1.00 10.16  ? 64  GLU A N   1 
ATOM   461  C CA  . GLU A 1 78  ? -11.841 22.918  6.889   1.00 9.68   ? 64  GLU A CA  1 
ATOM   462  C C   . GLU A 1 78  ? -10.740 23.436  7.790   1.00 9.65   ? 64  GLU A C   1 
ATOM   463  O O   . GLU A 1 78  ? -10.879 24.506  8.375   1.00 12.17  ? 64  GLU A O   1 
ATOM   464  C CB  . GLU A 1 78  ? -12.900 22.259  7.757   1.00 10.87  ? 64  GLU A CB  1 
ATOM   465  C CG  . GLU A 1 78  ? -14.227 22.093  7.051   1.00 10.80  ? 64  GLU A CG  1 
ATOM   466  C CD  . GLU A 1 78  ? -15.289 21.363  7.829   1.00 14.62  ? 64  GLU A CD  1 
ATOM   467  O OE1 . GLU A 1 78  ? -14.973 20.919  8.959   1.00 24.46  ? 64  GLU A OE1 1 
ATOM   468  O OE2 . GLU A 1 78  ? -16.387 21.158  7.259   1.00 12.12  ? 64  GLU A OE2 1 
ATOM   469  N N   . ASN A 1 79  ? -9.614  22.703  7.876   1.00 10.30  ? 65  ASN A N   1 
ATOM   470  C CA  . ASN A 1 79  ? -8.518  22.994  8.796   1.00 9.27   ? 65  ASN A CA  1 
ATOM   471  C C   . ASN A 1 79  ? -7.181  23.096  8.036   1.00 10.43  ? 65  ASN A C   1 
ATOM   472  O O   . ASN A 1 79  ? -6.123  22.951  8.655   1.00 10.44  ? 65  ASN A O   1 
ATOM   473  C CB  . ASN A 1 79  ? -8.509  21.915  9.876   1.00 8.97   ? 65  ASN A CB  1 
ATOM   474  C CG  . ASN A 1 79  ? -9.763  21.981  10.720  1.00 10.14  ? 65  ASN A CG  1 
ATOM   475  O OD1 . ASN A 1 79  ? -9.835  22.851  11.599  1.00 13.51  ? 65  ASN A OD1 1 
ATOM   476  N ND2 . ASN A 1 79  ? -10.680 21.045  10.513  1.00 11.22  ? 65  ASN A ND2 1 
ATOM   477  N N   . LYS A 1 80  ? -7.228  23.435  6.736   1.00 10.34  ? 66  LYS A N   1 
ATOM   478  C CA  . LYS A 1 80  ? -6.094  23.205  5.868   1.00 10.71  ? 66  LYS A CA  1 
ATOM   479  C C   . LYS A 1 80  ? -4.902  24.096  6.237   1.00 10.38  ? 66  LYS A C   1 
ATOM   480  O O   . LYS A 1 80  ? -3.777  23.750  5.887   1.00 12.55  ? 66  LYS A O   1 
ATOM   481  C CB  . LYS A 1 80  ? -6.482  23.377  4.398   1.00 12.43  ? 66  LYS A CB  1 
ATOM   482  C CG  . LYS A 1 80  ? -6.898  24.785  3.978   1.00 13.50  ? 66  LYS A CG  1 
ATOM   483  C CD  . LYS A 1 80  ? -7.399  24.809  2.525   1.00 15.79  ? 66  LYS A CD  1 
ATOM   484  C CE  . LYS A 1 80  ? -7.635  26.226  2.043   1.00 18.33  ? 66  LYS A CE  1 
ATOM   485  N NZ  . LYS A 1 80  ? -8.066  26.223  0.626   1.00 19.13  ? 66  LYS A NZ  1 
ATOM   486  N N   . GLU A 1 81  ? -5.151  25.267  6.872   1.00 11.70  ? 67  GLU A N   1 
ATOM   487  C CA  . GLU A 1 81  ? -4.058  26.156  7.288   1.00 14.50  ? 67  GLU A CA  1 
ATOM   488  C C   . GLU A 1 81  ? -3.098  25.457  8.255   1.00 13.70  ? 67  GLU A C   1 
ATOM   489  O O   . GLU A 1 81  ? -1.940  25.861  8.347   1.00 15.48  ? 67  GLU A O   1 
ATOM   490  C CB  . GLU A 1 81  ? -4.561  27.470  7.909   1.00 18.66  ? 67  GLU A CB  1 
ATOM   491  C CG  . GLU A 1 81  ? -5.403  27.265  9.166   1.00 25.74  ? 67  GLU A CG  1 
ATOM   492  C CD  . GLU A 1 81  ? -6.907  27.022  9.001   1.00 27.07  ? 67  GLU A CD  1 
ATOM   493  O OE1 . GLU A 1 81  ? -7.378  26.503  7.933   1.00 22.77  ? 67  GLU A OE1 1 
ATOM   494  O OE2 . GLU A 1 81  ? -7.630  27.352  9.968   1.00 27.17  ? 67  GLU A OE2 1 
ATOM   495  N N   . ARG A 1 82  ? -3.550  24.381  8.918   1.00 10.88  ? 68  ARG A N   1 
ATOM   496  C CA  . ARG A 1 82  ? -2.713  23.669  9.885   1.00 10.72  ? 68  ARG A CA  1 
ATOM   497  C C   . ARG A 1 82  ? -2.035  22.442  9.275   1.00 9.81   ? 68  ARG A C   1 
ATOM   498  O O   . ARG A 1 82  ? -1.199  21.844  9.955   1.00 10.62  ? 68  ARG A O   1 
ATOM   499  C CB  . ARG A 1 82  ? -3.522  23.215  11.117  1.00 12.12  ? 68  ARG A CB  1 
ATOM   500  C CG  . ARG A 1 82  ? -4.214  24.409  11.793  1.00 13.18  ? 68  ARG A CG  1 
ATOM   501  C CD  . ARG A 1 82  ? -4.587  24.105  13.223  1.00 13.52  ? 68  ARG A CD  1 
ATOM   502  N NE  . ARG A 1 82  ? -5.369  22.887  13.371  1.00 12.54  ? 68  ARG A NE  1 
ATOM   503  C CZ  . ARG A 1 82  ? -6.695  22.791  13.140  1.00 13.14  ? 68  ARG A CZ  1 
ATOM   504  N NH1 . ARG A 1 82  ? -7.410  23.836  12.726  1.00 14.50  ? 68  ARG A NH1 1 
ATOM   505  N NH2 . ARG A 1 82  ? -7.264  21.593  13.238  1.00 11.95  ? 68  ARG A NH2 1 
ATOM   506  N N   . LEU A 1 83  ? -2.339  22.090  8.013   1.00 10.19  ? 69  LEU A N   1 
ATOM   507  C CA  . LEU A 1 83  ? -1.727  20.898  7.423   1.00 9.52   ? 69  LEU A CA  1 
ATOM   508  C C   . LEU A 1 83  ? -0.265  21.188  7.086   1.00 10.62  ? 69  LEU A C   1 
ATOM   509  O O   . LEU A 1 83  ? -0.007  22.005  6.212   1.00 14.03  ? 69  LEU A O   1 
ATOM   510  C CB  . LEU A 1 83  ? -2.498  20.490  6.154   1.00 9.96   ? 69  LEU A CB  1 
ATOM   511  C CG  . LEU A 1 83  ? -1.983  19.220  5.472   1.00 9.08   ? 69  LEU A CG  1 
ATOM   512  C CD1 . LEU A 1 83  ? -2.123  17.986  6.374   1.00 10.39  ? 69  LEU A CD1 1 
ATOM   513  C CD2 . LEU A 1 83  ? -2.697  19.013  4.153   1.00 11.28  ? 69  LEU A CD2 1 
ATOM   514  N N   . LYS A 1 84  ? 0.667   20.420  7.677   1.00 9.75   ? 70  LYS A N   1 
ATOM   515  C CA  . LYS A 1 84  ? 2.090   20.655  7.508   1.00 9.51   ? 70  LYS A CA  1 
ATOM   516  C C   . LYS A 1 84  ? 2.727   19.701  6.514   1.00 11.98  ? 70  LYS A C   1 
ATOM   517  O O   . LYS A 1 84  ? 3.818   19.930  6.010   1.00 12.82  ? 70  LYS A O   1 
ATOM   518  C CB  . LYS A 1 84  ? 2.816   20.625  8.857   1.00 15.87  ? 70  LYS A CB  1 
ATOM   519  C CG  . LYS A 1 84  ? 2.383   21.670  9.879   1.00 16.05  ? 70  LYS A CG  1 
ATOM   520  C CD  . LYS A 1 84  ? 2.314   23.107  9.378   1.00 20.63  ? 70  LYS A CD  1 
ATOM   521  C CE  . LYS A 1 84  ? 1.600   24.034  10.354  1.00 26.53  ? 70  LYS A CE  1 
ATOM   522  N NZ  . LYS A 1 84  ? 1.014   25.268  9.746   1.00 31.07  ? 70  LYS A NZ  1 
ATOM   523  N N   . GLY A 1 85  ? 2.128   18.546  6.253   1.00 10.50  ? 71  GLY A N   1 
ATOM   524  C CA  . GLY A 1 85  ? 2.752   17.632  5.322   1.00 14.12  ? 71  GLY A CA  1 
ATOM   525  C C   . GLY A 1 85  ? 1.847   16.426  5.074   1.00 10.84  ? 71  GLY A C   1 
ATOM   526  O O   . GLY A 1 85  ? 0.955   16.079  5.864   1.00 10.57  ? 71  GLY A O   1 
ATOM   527  N N   . ILE A 1 86  ? 2.116   15.779  3.959   1.00 9.85   ? 72  ILE A N   1 
ATOM   528  C CA  . ILE A 1 86  ? 1.549   14.499  3.593   1.00 10.70  ? 72  ILE A CA  1 
ATOM   529  C C   . ILE A 1 86  ? 2.698   13.520  3.553   1.00 8.99   ? 72  ILE A C   1 
ATOM   530  O O   . ILE A 1 86  ? 3.652   13.718  2.803   1.00 9.44   ? 72  ILE A O   1 
ATOM   531  C CB  . ILE A 1 86  ? 0.880   14.597  2.202   1.00 11.74  ? 72  ILE A CB  1 
ATOM   532  C CG1 . ILE A 1 86  ? -0.240  15.643  2.163   1.00 13.14  ? 72  ILE A CG1 1 
ATOM   533  C CG2 . ILE A 1 86  ? 0.410   13.219  1.715   1.00 11.38  ? 72  ILE A CG2 1 
ATOM   534  C CD1 . ILE A 1 86  ? -0.637  16.061  0.786   1.00 14.64  ? 72  ILE A CD1 1 
ATOM   535  N N   . PHE A 1 87  ? 2.586   12.430  4.325   1.00 9.35   ? 73  PHE A N   1 
ATOM   536  C CA  . PHE A 1 87  ? 3.685   11.479  4.493   1.00 8.37   ? 73  PHE A CA  1 
ATOM   537  C C   . PHE A 1 87  ? 3.279   10.147  3.900   1.00 6.68   ? 73  PHE A C   1 
ATOM   538  O O   . PHE A 1 87  ? 2.219   9.637   4.294   1.00 8.38   ? 73  PHE A O   1 
ATOM   539  C CB  . PHE A 1 87  ? 4.049   11.297  5.977   1.00 9.62   ? 73  PHE A CB  1 
ATOM   540  C CG  . PHE A 1 87  ? 4.459   12.611  6.574   1.00 13.09  ? 73  PHE A CG  1 
ATOM   541  C CD1 . PHE A 1 87  ? 3.508   13.601  6.797   1.00 17.07  ? 73  PHE A CD1 1 
ATOM   542  C CD2 . PHE A 1 87  ? 5.781   12.963  6.694   1.00 12.96  ? 73  PHE A CD2 1 
ATOM   543  C CE1 . PHE A 1 87  ? 3.830   14.865  7.261   1.00 18.77  ? 73  PHE A CE1 1 
ATOM   544  C CE2 . PHE A 1 87  ? 6.102   14.205  7.229   1.00 13.55  ? 73  PHE A CE2 1 
ATOM   545  C CZ  . PHE A 1 87  ? 5.149   15.136  7.484   1.00 15.97  ? 73  PHE A CZ  1 
ATOM   546  N N   . LEU A 1 88  ? 3.996   9.691   2.858   1.00 6.36   ? 74  LEU A N   1 
ATOM   547  C CA  . LEU A 1 88  ? 3.580   8.506   2.113   1.00 7.04   ? 74  LEU A CA  1 
ATOM   548  C C   . LEU A 1 88  ? 4.506   7.334   2.342   1.00 7.32   ? 74  LEU A C   1 
ATOM   549  O O   . LEU A 1 88  ? 5.713   7.445   2.151   1.00 7.99   ? 74  LEU A O   1 
ATOM   550  C CB  . LEU A 1 88  ? 3.540   8.834   0.617   1.00 7.51   ? 74  LEU A CB  1 
ATOM   551  C CG  . LEU A 1 88  ? 2.674   10.047  0.242   1.00 7.48   ? 74  LEU A CG  1 
ATOM   552  C CD1 . LEU A 1 88  ? 2.812   10.358  -1.232  1.00 10.07  ? 74  LEU A CD1 1 
ATOM   553  C CD2 . LEU A 1 88  ? 1.220   9.782   0.611   1.00 8.64   ? 74  LEU A CD2 1 
ATOM   554  N N   . THR A 1 89  ? 3.947   6.220   2.840   1.00 7.21   ? 75  THR A N   1 
ATOM   555  C CA  . THR A 1 89  ? 4.778   5.112   3.293   1.00 7.60   ? 75  THR A CA  1 
ATOM   556  C C   . THR A 1 89  ? 5.379   4.298   2.141   1.00 7.23   ? 75  THR A C   1 
ATOM   557  O O   . THR A 1 89  ? 6.474   3.763   2.269   1.00 8.82   ? 75  THR A O   1 
ATOM   558  C CB  . THR A 1 89  ? 3.964   4.185   4.217   1.00 7.91   ? 75  THR A CB  1 
ATOM   559  O OG1 . THR A 1 89  ? 2.782   3.741   3.519   1.00 7.45   ? 75  THR A OG1 1 
ATOM   560  C CG2 . THR A 1 89  ? 3.631   4.896   5.508   1.00 8.50   ? 75  THR A CG2 1 
ATOM   561  N N   . ALA A 1 90  ? 4.703   4.184   1.001   1.00 6.68   ? 76  ALA A N   1 
ATOM   562  C CA  . ALA A 1 90  ? 5.166   3.323   -0.074  1.00 7.57   ? 76  ALA A CA  1 
ATOM   563  C C   . ALA A 1 90  ? 4.387   3.690   -1.335  1.00 7.53   ? 76  ALA A C   1 
ATOM   564  O O   . ALA A 1 90  ? 3.424   4.461   -1.266  1.00 9.53   ? 76  ALA A O   1 
ATOM   565  C CB  . ALA A 1 90  ? 4.970   1.863   0.259   1.00 9.06   ? 76  ALA A CB  1 
ATOM   566  N N   . GLY A 1 91  ? 4.785   3.151   -2.477  1.00 7.82   ? 77  GLY A N   1 
ATOM   567  C CA  . GLY A 1 91  ? 4.286   3.565   -3.775  1.00 9.34   ? 77  GLY A CA  1 
ATOM   568  C C   . GLY A 1 91  ? 3.092   2.772   -4.282  1.00 9.96   ? 77  GLY A C   1 
ATOM   569  O O   . GLY A 1 91  ? 2.739   2.989   -5.438  1.00 11.82  ? 77  GLY A O   1 
ATOM   570  N N   . HIS A 1 92  ? 2.499   1.915   -3.426  1.00 9.48   ? 78  HIS A N   1 
ATOM   571  C CA  . HIS A 1 92  ? 1.353   1.131   -3.853  1.00 8.79   ? 78  HIS A CA  1 
ATOM   572  C C   . HIS A 1 92  ? 0.058   1.947   -3.733  1.00 8.08   ? 78  HIS A C   1 
ATOM   573  O O   . HIS A 1 92  ? 0.016   2.999   -3.117  1.00 7.88   ? 78  HIS A O   1 
ATOM   574  C CB  . HIS A 1 92  ? 1.263   -0.190  -3.078  1.00 11.36  ? 78  HIS A CB  1 
ATOM   575  C CG  . HIS A 1 92  ? 1.260   0.035   -1.606  1.00 11.23  ? 78  HIS A CG  1 
ATOM   576  N ND1 . HIS A 1 92  ? 0.153   0.465   -0.920  1.00 16.18  ? 78  HIS A ND1 1 
ATOM   577  C CD2 . HIS A 1 92  ? 2.221   -0.197  -0.675  1.00 15.51  ? 78  HIS A CD2 1 
ATOM   578  C CE1 . HIS A 1 92  ? 0.450   0.534   0.372   1.00 13.92  ? 78  HIS A CE1 1 
ATOM   579  N NE2 . HIS A 1 92  ? 1.716   0.141   0.551   1.00 14.01  ? 78  HIS A NE2 1 
ATOM   580  N N   . GLU A 1 93  ? -0.979  1.443   -4.384  1.00 9.85   ? 79  GLU A N   1 
ATOM   581  C CA  . GLU A 1 93  ? -2.245  2.136   -4.488  1.00 9.05   ? 79  GLU A CA  1 
ATOM   582  C C   . GLU A 1 93  ? -2.906  2.418   -3.135  1.00 9.49   ? 79  GLU A C   1 
ATOM   583  O O   . GLU A 1 93  ? -3.614  3.419   -3.013  1.00 9.50   ? 79  GLU A O   1 
ATOM   584  C CB  . GLU A 1 93  ? -3.156  1.308   -5.404  1.00 15.19  ? 79  GLU A CB  1 
ATOM   585  C CG  . GLU A 1 93  ? -2.596  0.988   -6.789  1.00 27.41  ? 79  GLU A CG  1 
ATOM   586  C CD  . GLU A 1 93  ? -1.740  -0.273  -6.973  1.00 36.88  ? 79  GLU A CD  1 
ATOM   587  O OE1 . GLU A 1 93  ? -1.533  -0.691  -8.172  1.00 55.28  ? 79  GLU A OE1 1 
ATOM   588  O OE2 . GLU A 1 93  ? -1.258  -0.863  -5.946  1.00 19.34  ? 79  GLU A OE2 1 
ATOM   589  N N   . HIS A 1 94  ? -2.722  1.527   -2.158  1.00 9.02   ? 80  HIS A N   1 
ATOM   590  C CA  . HIS A 1 94  ? -3.311  1.734   -0.834  1.00 9.76   ? 80  HIS A CA  1 
ATOM   591  C C   . HIS A 1 94  ? -2.708  2.898   -0.069  1.00 8.47   ? 80  HIS A C   1 
ATOM   592  O O   . HIS A 1 94  ? -3.288  3.360   0.934   1.00 8.46   ? 80  HIS A O   1 
ATOM   593  C CB  . HIS A 1 94  ? -3.152  0.500   0.065   1.00 12.93  ? 80  HIS A CB  1 
ATOM   594  C CG  . HIS A 1 94  ? -3.920  -0.696  -0.328  1.00 14.82  ? 80  HIS A CG  1 
ATOM   595  N ND1 . HIS A 1 94  ? -3.810  -1.835  0.419   1.00 17.53  ? 80  HIS A ND1 1 
ATOM   596  C CD2 . HIS A 1 94  ? -4.700  -0.945  -1.416  1.00 13.83  ? 80  HIS A CD2 1 
ATOM   597  C CE1 . HIS A 1 94  ? -4.583  -2.761  -0.147  1.00 23.18  ? 80  HIS A CE1 1 
ATOM   598  N NE2 . HIS A 1 94  ? -5.082  -2.268  -1.299  1.00 16.50  ? 80  HIS A NE2 1 
ATOM   599  N N   . ALA A 1 95  ? -1.502  3.325   -0.509  1.00 7.25   ? 81  ALA A N   1 
ATOM   600  C CA  . ALA A 1 95  ? -0.799  4.426   0.123   1.00 8.07   ? 81  ALA A CA  1 
ATOM   601  C C   . ALA A 1 95  ? -0.879  5.724   -0.689  1.00 6.57   ? 81  ALA A C   1 
ATOM   602  O O   . ALA A 1 95  ? -0.958  6.810   -0.109  1.00 8.28   ? 81  ALA A O   1 
ATOM   603  C CB  . ALA A 1 95  ? 0.676   4.132   0.378   1.00 9.51   ? 81  ALA A CB  1 
ATOM   604  N N   . ILE A 1 96  ? -0.863  5.649   -2.012  1.00 6.98   ? 82  ILE A N   1 
ATOM   605  C CA  . ILE A 1 96  ? -0.745  6.866   -2.825  1.00 6.38   ? 82  ILE A CA  1 
ATOM   606  C C   . ILE A 1 96  ? -1.857  7.042   -3.846  1.00 8.47   ? 82  ILE A C   1 
ATOM   607  O O   . ILE A 1 96  ? -1.865  8.078   -4.508  1.00 8.38   ? 82  ILE A O   1 
ATOM   608  C CB  . ILE A 1 96  ? 0.610   6.956   -3.553  1.00 8.61   ? 82  ILE A CB  1 
ATOM   609  C CG1 . ILE A 1 96  ? 0.763   5.978   -4.709  1.00 8.15   ? 82  ILE A CG1 1 
ATOM   610  C CG2 . ILE A 1 96  ? 1.740   6.945   -2.539  1.00 10.31  ? 82  ILE A CG2 1 
ATOM   611  C CD1 . ILE A 1 96  ? 1.943   6.306   -5.606  1.00 12.60  ? 82  ILE A CD1 1 
ATOM   612  N N   . GLY A 1 97  ? -2.819  6.124   -3.962  1.00 8.86   ? 83  GLY A N   1 
ATOM   613  C CA  . GLY A 1 97  ? -3.805  6.241   -5.030  1.00 8.76   ? 83  GLY A CA  1 
ATOM   614  C C   . GLY A 1 97  ? -4.628  7.521   -5.084  1.00 8.38   ? 83  GLY A C   1 
ATOM   615  O O   . GLY A 1 97  ? -5.110  7.873   -6.165  1.00 10.80  ? 83  GLY A O   1 
ATOM   616  N N   . ALA A 1 98  ? -4.855  8.156   -3.918  1.00 8.33   ? 84  ALA A N   1 
ATOM   617  C CA  . ALA A 1 98  ? -5.665  9.370   -3.848  1.00 9.21   ? 84  ALA A CA  1 
ATOM   618  C C   . ALA A 1 98  ? -4.832  10.648  -3.864  1.00 8.27   ? 84  ALA A C   1 
ATOM   619  O O   . ALA A 1 98  ? -5.416  11.744  -3.845  1.00 9.30   ? 84  ALA A O   1 
ATOM   620  C CB  . ALA A 1 98  ? -6.584  9.342   -2.628  1.00 9.17   ? 84  ALA A CB  1 
ATOM   621  N N   . VAL A 1 99  ? -3.478  10.531  -3.869  1.00 7.15   ? 85  VAL A N   1 
ATOM   622  C CA  . VAL A 1 99  ? -2.654  11.719  -3.634  1.00 8.22   ? 85  VAL A CA  1 
ATOM   623  C C   . VAL A 1 99  ? -2.961  12.849  -4.642  1.00 7.91   ? 85  VAL A C   1 
ATOM   624  O O   . VAL A 1 99  ? -3.005  14.019  -4.253  1.00 8.88   ? 85  VAL A O   1 
ATOM   625  C CB  . VAL A 1 99  ? -1.135  11.405  -3.597  1.00 10.51  ? 85  VAL A CB  1 
ATOM   626  C CG1 . VAL A 1 99  ? -0.316  12.708  -3.682  1.00 12.38  ? 85  VAL A CG1 1 
ATOM   627  C CG2 . VAL A 1 99  ? -0.775  10.555  -2.399  1.00 13.01  ? 85  VAL A CG2 1 
ATOM   628  N N   . SER A 1 100 ? -3.104  12.513  -5.925  1.00 8.79   ? 86  SER A N   1 
ATOM   629  C CA  . SER A 1 100 ? -3.316  13.547  -6.918  1.00 8.77   ? 86  SER A CA  1 
ATOM   630  C C   . SER A 1 100 ? -4.621  14.291  -6.663  1.00 10.75  ? 86  SER A C   1 
ATOM   631  O O   . SER A 1 100 ? -4.699  15.507  -6.810  1.00 10.66  ? 86  SER A O   1 
ATOM   632  C CB  . SER A 1 100 ? -3.258  13.037  -8.337  1.00 11.23  ? 86  SER A CB  1 
ATOM   633  O OG  . SER A 1 100 ? -4.307  12.108  -8.579  1.00 13.07  ? 86  SER A OG  1 
ATOM   634  N N   . TYR A 1 101 ? -5.665  13.561  -6.245  1.00 9.07   ? 87  TYR A N   1 
ATOM   635  C CA  . TYR A 1 101 ? -6.938  14.166  -5.909  1.00 9.74   ? 87  TYR A CA  1 
ATOM   636  C C   . TYR A 1 101 ? -6.848  15.055  -4.676  1.00 9.87   ? 87  TYR A C   1 
ATOM   637  O O   . TYR A 1 101 ? -7.463  16.138  -4.629  1.00 11.84  ? 87  TYR A O   1 
ATOM   638  C CB  . TYR A 1 101 ? -7.938  13.029  -5.703  1.00 10.64  ? 87  TYR A CB  1 
ATOM   639  C CG  . TYR A 1 101 ? -8.156  12.216  -6.951  1.00 8.95   ? 87  TYR A CG  1 
ATOM   640  C CD1 . TYR A 1 101 ? -9.135  12.570  -7.893  1.00 10.87  ? 87  TYR A CD1 1 
ATOM   641  C CD2 . TYR A 1 101 ? -7.377  11.102  -7.217  1.00 10.74  ? 87  TYR A CD2 1 
ATOM   642  C CE1 . TYR A 1 101 ? -9.313  11.827  -9.057  1.00 13.28  ? 87  TYR A CE1 1 
ATOM   643  C CE2 . TYR A 1 101 ? -7.478  10.416  -8.416  1.00 12.45  ? 87  TYR A CE2 1 
ATOM   644  C CZ  . TYR A 1 101 ? -8.485  10.742  -9.324  1.00 12.28  ? 87  TYR A CZ  1 
ATOM   645  O OH  . TYR A 1 101 ? -8.614  10.024  -10.514 1.00 17.10  ? 87  TYR A OH  1 
ATOM   646  N N   . VAL A 1 102 ? -6.046  14.657  -3.683  1.00 8.69   ? 88  VAL A N   1 
ATOM   647  C CA  . VAL A 1 102 ? -5.826  15.479  -2.516  1.00 9.76   ? 88  VAL A CA  1 
ATOM   648  C C   . VAL A 1 102 ? -5.162  16.787  -2.944  1.00 9.54   ? 88  VAL A C   1 
ATOM   649  O O   . VAL A 1 102 ? -5.558  17.856  -2.490  1.00 10.95  ? 88  VAL A O   1 
ATOM   650  C CB  . VAL A 1 102 ? -4.978  14.745  -1.459  1.00 10.67  ? 88  VAL A CB  1 
ATOM   651  C CG1 . VAL A 1 102 ? -4.527  15.688  -0.332  1.00 11.17  ? 88  VAL A CG1 1 
ATOM   652  C CG2 . VAL A 1 102 ? -5.755  13.564  -0.912  1.00 10.11  ? 88  VAL A CG2 1 
ATOM   653  N N   . LEU A 1 103 ? -4.108  16.658  -3.781  1.00 8.50   ? 89  LEU A N   1 
ATOM   654  C CA  . LEU A 1 103 ? -3.332  17.833  -4.157  1.00 10.15  ? 89  LEU A CA  1 
ATOM   655  C C   . LEU A 1 103 ? -4.137  18.798  -5.015  1.00 10.43  ? 89  LEU A C   1 
ATOM   656  O O   . LEU A 1 103 ? -3.811  19.982  -5.088  1.00 12.62  ? 89  LEU A O   1 
ATOM   657  C CB  . LEU A 1 103 ? -2.023  17.436  -4.830  1.00 10.88  ? 89  LEU A CB  1 
ATOM   658  C CG  . LEU A 1 103 ? -1.010  16.825  -3.837  1.00 9.96   ? 89  LEU A CG  1 
ATOM   659  C CD1 . LEU A 1 103 ? 0.147   16.199  -4.624  1.00 11.94  ? 89  LEU A CD1 1 
ATOM   660  C CD2 . LEU A 1 103 ? -0.491  17.867  -2.812  1.00 11.97  ? 89  LEU A CD2 1 
ATOM   661  N N   . GLU A 1 104 ? -5.228  18.333  -5.629  1.00 11.89  ? 90  GLU A N   1 
ATOM   662  C CA  . GLU A 1 104 ? -6.061  19.281  -6.356  1.00 14.41  ? 90  GLU A CA  1 
ATOM   663  C C   . GLU A 1 104 ? -6.882  20.159  -5.415  1.00 12.62  ? 90  GLU A C   1 
ATOM   664  O O   . GLU A 1 104 ? -7.358  21.231  -5.824  1.00 18.43  ? 90  GLU A O   1 
ATOM   665  C CB  . GLU A 1 104 ? -7.025  18.555  -7.283  1.00 14.14  ? 90  GLU A CB  1 
ATOM   666  C CG  . GLU A 1 104 ? -6.390  17.848  -8.451  1.00 15.12  ? 90  GLU A CG  1 
ATOM   667  C CD  . GLU A 1 104 ? -7.476  17.188  -9.294  1.00 18.45  ? 90  GLU A CD  1 
ATOM   668  O OE1 . GLU A 1 104 ? -7.820  17.756  -10.340 1.00 21.80  ? 90  GLU A OE1 1 
ATOM   669  O OE2 . GLU A 1 104 ? -8.022  16.119  -8.881  1.00 17.55  ? 90  GLU A OE2 1 
ATOM   670  N N   . GLN A 1 105 ? -7.002  19.768  -4.146  1.00 12.83  ? 91  GLN A N   1 
ATOM   671  C CA  . GLN A 1 105 ? -7.889  20.399  -3.180  1.00 13.27  ? 91  GLN A CA  1 
ATOM   672  C C   . GLN A 1 105 ? -7.132  21.189  -2.117  1.00 14.25  ? 91  GLN A C   1 
ATOM   673  O O   . GLN A 1 105 ? -7.621  22.193  -1.624  1.00 18.06  ? 91  GLN A O   1 
ATOM   674  C CB  . GLN A 1 105 ? -8.704  19.319  -2.448  1.00 14.61  ? 91  GLN A CB  1 
ATOM   675  C CG  . GLN A 1 105 ? -9.548  18.444  -3.396  1.00 14.89  ? 91  GLN A CG  1 
ATOM   676  C CD  . GLN A 1 105 ? -10.242 17.316  -2.661  1.00 17.71  ? 91  GLN A CD  1 
ATOM   677  O OE1 . GLN A 1 105 ? -11.197 17.553  -1.921  1.00 16.43  ? 91  GLN A OE1 1 
ATOM   678  N NE2 . GLN A 1 105 ? -9.820  16.075  -2.896  1.00 17.28  ? 91  GLN A NE2 1 
ATOM   679  N N   . ILE A 1 106 ? -5.897  20.761  -1.763  1.00 14.45  ? 92  ILE A N   1 
ATOM   680  C CA  . ILE A 1 106 ? -5.109  21.375  -0.711  1.00 12.91  ? 92  ILE A CA  1 
ATOM   681  C C   . ILE A 1 106 ? -3.652  21.405  -1.190  1.00 13.76  ? 92  ILE A C   1 
ATOM   682  O O   . ILE A 1 106 ? -3.245  20.662  -2.077  1.00 16.77  ? 92  ILE A O   1 
ATOM   683  C CB  . ILE A 1 106 ? -5.323  20.698  0.669   1.00 14.07  ? 92  ILE A CB  1 
ATOM   684  C CG1 . ILE A 1 106 ? -4.935  19.212  0.710   1.00 16.64  ? 92  ILE A CG1 1 
ATOM   685  C CG2 . ILE A 1 106 ? -6.765  20.806  1.126   1.00 18.88  ? 92  ILE A CG2 1 
ATOM   686  C CD1 . ILE A 1 106 ? -3.442  18.960  0.548   1.00 20.16  ? 92  ILE A CD1 1 
ATOM   687  N N   . ASP A 1 107 ? -2.852  22.234  -0.517  1.00 17.84  ? 93  ASP A N   1 
ATOM   688  C CA  . ASP A 1 107 ? -1.424  22.344  -0.778  1.00 19.79  ? 93  ASP A CA  1 
ATOM   689  C C   . ASP A 1 107 ? -0.679  21.974  0.510   1.00 21.13  ? 93  ASP A C   1 
ATOM   690  O O   . ASP A 1 107 ? -0.919  22.560  1.582   1.00 21.21  ? 93  ASP A O   1 
ATOM   691  C CB  . ASP A 1 107 ? -1.120  23.749  -1.298  1.00 31.30  ? 93  ASP A CB  1 
ATOM   692  N N   . ALA A 1 108 ? 0.221   20.987  0.393   1.00 15.09  ? 94  ALA A N   1 
ATOM   693  C CA  . ALA A 1 108 ? 1.148   20.732  1.463   1.00 13.17  ? 94  ALA A CA  1 
ATOM   694  C C   . ALA A 1 108 ? 2.328   20.032  0.816   1.00 11.55  ? 94  ALA A C   1 
ATOM   695  O O   . ALA A 1 108 ? 2.144   19.378  -0.230  1.00 14.46  ? 94  ALA A O   1 
ATOM   696  C CB  . ALA A 1 108 ? 0.504   19.824  2.498   1.00 15.46  ? 94  ALA A CB  1 
ATOM   697  N N   . PRO A 1 109 ? 3.488   20.042  1.492   1.00 12.00  ? 95  PRO A N   1 
ATOM   698  C CA  . PRO A 1 109 ? 4.610   19.258  0.992   1.00 12.36  ? 95  PRO A CA  1 
ATOM   699  C C   . PRO A 1 109 ? 4.341   17.768  1.109   1.00 9.35   ? 95  PRO A C   1 
ATOM   700  O O   . PRO A 1 109 ? 3.616   17.298  2.013   1.00 11.82  ? 95  PRO A O   1 
ATOM   701  C CB  . PRO A 1 109 ? 5.765   19.613  1.922   1.00 15.32  ? 95  PRO A CB  1 
ATOM   702  C CG  . PRO A 1 109 ? 5.357   20.864  2.677   1.00 21.22  ? 95  PRO A CG  1 
ATOM   703  C CD  . PRO A 1 109 ? 3.828   20.860  2.667   1.00 15.33  ? 95  PRO A CD  1 
ATOM   704  N N   . VAL A 1 110 ? 4.947   17.010  0.191   1.00 9.54   ? 96  VAL A N   1 
ATOM   705  C CA  . VAL A 1 110 ? 4.722   15.575  0.049   1.00 8.60   ? 96  VAL A CA  1 
ATOM   706  C C   . VAL A 1 110 ? 6.034   14.882  0.335   1.00 7.65   ? 96  VAL A C   1 
ATOM   707  O O   . VAL A 1 110 ? 7.017   15.130  -0.375  1.00 9.58   ? 96  VAL A O   1 
ATOM   708  C CB  . VAL A 1 110 ? 4.207   15.233  -1.367  1.00 9.52   ? 96  VAL A CB  1 
ATOM   709  C CG1 . VAL A 1 110 ? 4.111   13.730  -1.566  1.00 10.06  ? 96  VAL A CG1 1 
ATOM   710  C CG2 . VAL A 1 110 ? 2.841   15.852  -1.624  1.00 12.26  ? 96  VAL A CG2 1 
ATOM   711  N N   . TYR A 1 111 ? 6.066   13.999  1.345   1.00 8.08   ? 97  TYR A N   1 
ATOM   712  C CA  . TYR A 1 111 ? 7.281   13.356  1.806   1.00 7.93   ? 97  TYR A CA  1 
ATOM   713  C C   . TYR A 1 111 ? 7.155   11.869  1.477   1.00 6.35   ? 97  TYR A C   1 
ATOM   714  O O   . TYR A 1 111 ? 6.145   11.219  1.817   1.00 9.39   ? 97  TYR A O   1 
ATOM   715  C CB  . TYR A 1 111 ? 7.466   13.501  3.315   1.00 7.26   ? 97  TYR A CB  1 
ATOM   716  C CG  . TYR A 1 111 ? 7.548   14.927  3.799   1.00 9.76   ? 97  TYR A CG  1 
ATOM   717  C CD1 . TYR A 1 111 ? 6.419   15.697  3.993   1.00 10.81  ? 97  TYR A CD1 1 
ATOM   718  C CD2 . TYR A 1 111 ? 8.786   15.519  4.059   1.00 11.31  ? 97  TYR A CD2 1 
ATOM   719  C CE1 . TYR A 1 111 ? 6.495   17.025  4.379   1.00 11.95  ? 97  TYR A CE1 1 
ATOM   720  C CE2 . TYR A 1 111 ? 8.879   16.839  4.485   1.00 10.87  ? 97  TYR A CE2 1 
ATOM   721  C CZ  . TYR A 1 111 ? 7.731   17.575  4.670   1.00 10.03  ? 97  TYR A CZ  1 
ATOM   722  O OH  . TYR A 1 111 ? 7.847   18.893  5.116   1.00 12.45  ? 97  TYR A OH  1 
ATOM   723  N N   . GLY A 1 112 ? 8.185   11.270  0.907   1.00 8.10   ? 98  GLY A N   1 
ATOM   724  C CA  . GLY A 1 112 ? 8.177   9.822   0.677   1.00 8.87   ? 98  GLY A CA  1 
ATOM   725  C C   . GLY A 1 112 ? 9.552   9.375   0.217   1.00 8.60   ? 98  GLY A C   1 
ATOM   726  O O   . GLY A 1 112 ? 10.432  10.189  -0.046  1.00 9.15   ? 98  GLY A O   1 
ATOM   727  N N   . SER A 1 113 ? 9.735   8.061   0.114   1.00 8.45   ? 99  SER A N   1 
ATOM   728  C CA  . SER A 1 113 ? 10.997  7.520   -0.396  1.00 7.60   ? 99  SER A CA  1 
ATOM   729  C C   . SER A 1 113 ? 11.211  7.911   -1.849  1.00 9.18   ? 99  SER A C   1 
ATOM   730  O O   . SER A 1 113 ? 10.318  8.377   -2.586  1.00 8.87   ? 99  SER A O   1 
ATOM   731  C CB  . SER A 1 113 ? 10.999  6.008   -0.271  1.00 9.19   ? 99  SER A CB  1 
ATOM   732  O OG  . SER A 1 113 ? 10.129  5.462   -1.261  1.00 9.75   ? 99  SER A OG  1 
ATOM   733  N N   . LYS A 1 114 ? 12.445  7.617   -2.317  1.00 9.50   ? 100 LYS A N   1 
ATOM   734  C CA  . LYS A 1 114 ? 12.799  7.921   -3.709  1.00 12.06  ? 100 LYS A CA  1 
ATOM   735  C C   . LYS A 1 114 ? 11.802  7.338   -4.708  1.00 9.51   ? 100 LYS A C   1 
ATOM   736  O O   . LYS A 1 114 ? 11.396  7.969   -5.675  1.00 10.38  ? 100 LYS A O   1 
ATOM   737  C CB  . LYS A 1 114 ? 14.241  7.425   -3.908  1.00 15.86  ? 100 LYS A CB  1 
ATOM   738  C CG  . LYS A 1 114 ? 14.708  7.298   -5.339  1.00 15.81  ? 100 LYS A CG  1 
ATOM   739  C CD  . LYS A 1 114 ? 16.147  6.738   -5.331  1.00 17.08  ? 100 LYS A CD  1 
ATOM   740  C CE  . LYS A 1 114 ? 16.563  6.584   -6.782  1.00 23.44  ? 100 LYS A CE  1 
ATOM   741  N NZ  . LYS A 1 114 ? 17.987  6.186   -6.900  1.00 30.36  ? 100 LYS A NZ  1 
ATOM   742  N N   . LEU A 1 115 ? 11.456  6.057   -4.514  1.00 9.12   ? 101 LEU A N   1 
ATOM   743  C CA  . LEU A 1 115 ? 10.513  5.427   -5.439  1.00 9.63   ? 101 LEU A CA  1 
ATOM   744  C C   . LEU A 1 115 ? 9.100   5.999   -5.292  1.00 8.51   ? 101 LEU A C   1 
ATOM   745  O O   . LEU A 1 115 ? 8.425   6.238   -6.300  1.00 9.97   ? 101 LEU A O   1 
ATOM   746  C CB  . LEU A 1 115 ? 10.480  3.896   -5.226  1.00 9.56   ? 101 LEU A CB  1 
ATOM   747  C CG  . LEU A 1 115 ? 9.481   3.149   -6.117  1.00 11.07  ? 101 LEU A CG  1 
ATOM   748  C CD1 . LEU A 1 115 ? 9.708   3.410   -7.616  1.00 12.04  ? 101 LEU A CD1 1 
ATOM   749  C CD2 . LEU A 1 115 ? 9.525   1.657   -5.791  1.00 11.61  ? 101 LEU A CD2 1 
ATOM   750  N N   . THR A 1 116 ? 8.669   6.179   -4.035  1.00 8.40   ? 102 THR A N   1 
ATOM   751  C CA  . THR A 1 116 ? 7.306   6.703   -3.826  1.00 9.19   ? 102 THR A CA  1 
ATOM   752  C C   . THR A 1 116 ? 7.117   8.084   -4.497  1.00 10.31  ? 102 THR A C   1 
ATOM   753  O O   . THR A 1 116 ? 6.120   8.317   -5.178  1.00 10.30  ? 102 THR A O   1 
ATOM   754  C CB  . THR A 1 116 ? 7.058   6.853   -2.319  1.00 7.78   ? 102 THR A CB  1 
ATOM   755  O OG1 . THR A 1 116 ? 7.127   5.519   -1.832  1.00 8.84   ? 102 THR A OG1 1 
ATOM   756  C CG2 . THR A 1 116 ? 5.700   7.432   -1.973  1.00 8.69   ? 102 THR A CG2 1 
ATOM   757  N N   . ILE A 1 117 ? 8.113   8.967   -4.365  1.00 9.03   ? 103 ILE A N   1 
ATOM   758  C CA  . ILE A 1 117 ? 8.011   10.289  -4.954  1.00 9.74   ? 103 ILE A CA  1 
ATOM   759  C C   . ILE A 1 117 ? 7.942   10.172  -6.474  1.00 11.16  ? 103 ILE A C   1 
ATOM   760  O O   . ILE A 1 117 ? 7.176   10.868  -7.120  1.00 10.80  ? 103 ILE A O   1 
ATOM   761  C CB  . ILE A 1 117 ? 9.196   11.163  -4.488  1.00 10.69  ? 103 ILE A CB  1 
ATOM   762  C CG1 . ILE A 1 117 ? 9.064   11.486  -2.996  1.00 11.95  ? 103 ILE A CG1 1 
ATOM   763  C CG2 . ILE A 1 117 ? 9.229   12.484  -5.307  1.00 12.16  ? 103 ILE A CG2 1 
ATOM   764  C CD1 . ILE A 1 117 ? 7.776   12.141  -2.565  1.00 14.54  ? 103 ILE A CD1 1 
ATOM   765  N N   . ALA A 1 118 ? 8.819   9.336   -7.080  1.00 10.35  ? 104 ALA A N   1 
ATOM   766  C CA  . ALA A 1 118 ? 8.794   9.205   -8.532  1.00 10.18  ? 104 ALA A CA  1 
ATOM   767  C C   . ALA A 1 118 ? 7.418   8.704   -9.001  1.00 11.55  ? 104 ALA A C   1 
ATOM   768  O O   . ALA A 1 118 ? 6.951   9.077   -10.088 1.00 12.09  ? 104 ALA A O   1 
ATOM   769  C CB  . ALA A 1 118 ? 9.875   8.242   -8.997  1.00 12.58  ? 104 ALA A CB  1 
ATOM   770  N N   . LEU A 1 119 ? 6.769   7.789   -8.246  1.00 9.61   ? 105 LEU A N   1 
ATOM   771  C CA  . LEU A 1 119 ? 5.487   7.264   -8.705  1.00 8.96   ? 105 LEU A CA  1 
ATOM   772  C C   . LEU A 1 119 ? 4.415   8.336   -8.550  1.00 10.81  ? 105 LEU A C   1 
ATOM   773  O O   . LEU A 1 119 ? 3.527   8.404   -9.397  1.00 13.14  ? 105 LEU A O   1 
ATOM   774  C CB  . LEU A 1 119 ? 5.140   5.962   -7.977  1.00 9.44   ? 105 LEU A CB  1 
ATOM   775  C CG  . LEU A 1 119 ? 6.055   4.780   -8.281  1.00 10.14  ? 105 LEU A CG  1 
ATOM   776  C CD1 . LEU A 1 119 ? 5.788   3.632   -7.311  1.00 13.27  ? 105 LEU A CD1 1 
ATOM   777  C CD2 . LEU A 1 119 ? 5.875   4.334   -9.716  1.00 15.04  ? 105 LEU A CD2 1 
ATOM   778  N N   . VAL A 1 120 ? 4.473   9.141   -7.470  1.00 10.57  ? 106 VAL A N   1 
ATOM   779  C CA  . VAL A 1 120 ? 3.483   10.212  -7.319  1.00 9.40   ? 106 VAL A CA  1 
ATOM   780  C C   . VAL A 1 120 ? 3.637   11.233  -8.469  1.00 10.40  ? 106 VAL A C   1 
ATOM   781  O O   . VAL A 1 120 ? 2.660   11.671  -9.106  1.00 12.80  ? 106 VAL A O   1 
ATOM   782  C CB  . VAL A 1 120 ? 3.569   10.921  -5.954  1.00 9.41   ? 106 VAL A CB  1 
ATOM   783  C CG1 . VAL A 1 120 ? 2.690   12.164  -5.929  1.00 10.02  ? 106 VAL A CG1 1 
ATOM   784  C CG2 . VAL A 1 120 ? 3.220   9.941   -4.836  1.00 9.73   ? 106 VAL A CG2 1 
ATOM   785  N N   . LYS A 1 121 ? 4.890   11.609  -8.780  1.00 12.74  ? 107 LYS A N   1 
ATOM   786  C CA  . LYS A 1 121 ? 5.134   12.553  -9.870  1.00 13.10  ? 107 LYS A CA  1 
ATOM   787  C C   . LYS A 1 121 ? 4.549   12.021  -11.178 1.00 17.14  ? 107 LYS A C   1 
ATOM   788  O O   . LYS A 1 121 ? 3.985   12.801  -11.962 1.00 17.81  ? 107 LYS A O   1 
ATOM   789  C CB  . LYS A 1 121 ? 6.643   12.815  -9.994  1.00 16.56  ? 107 LYS A CB  1 
ATOM   790  C CG  . LYS A 1 121 ? 7.189   13.719  -8.910  1.00 20.59  ? 107 LYS A CG  1 
ATOM   791  C CD  . LYS A 1 121 ? 8.709   13.905  -8.922  1.00 29.16  ? 107 LYS A CD  1 
ATOM   792  C CE  . LYS A 1 121 ? 9.200   15.108  -9.683  1.00 45.18  ? 107 LYS A CE  1 
ATOM   793  N NZ  . LYS A 1 121 ? 10.659  14.956  -9.959  1.00 37.22  ? 107 LYS A NZ  1 
ATOM   794  N N   . GLU A 1 122 ? 4.700   10.709  -11.446 1.00 14.70  ? 108 GLU A N   1 
ATOM   795  C CA  . GLU A 1 122 ? 4.127   10.108  -12.648 1.00 17.38  ? 108 GLU A CA  1 
ATOM   796  C C   . GLU A 1 122 ? 2.597   10.199  -12.663 1.00 16.05  ? 108 GLU A C   1 
ATOM   797  O O   . GLU A 1 122 ? 1.965   10.426  -13.721 1.00 17.58  ? 108 GLU A O   1 
ATOM   798  C CB  . GLU A 1 122 ? 4.620   8.668   -12.838 1.00 21.40  ? 108 GLU A CB  1 
ATOM   799  C CG  . GLU A 1 122 ? 4.118   7.977   -14.089 1.00 33.03  ? 108 GLU A CG  1 
ATOM   800  C CD  . GLU A 1 122 ? 4.431   8.710   -15.383 1.00 34.63  ? 108 GLU A CD  1 
ATOM   801  O OE1 . GLU A 1 122 ? 5.525   9.317   -15.465 1.00 30.58  ? 108 GLU A OE1 1 
ATOM   802  O OE2 . GLU A 1 122 ? 3.575   8.664   -16.294 1.00 51.31  ? 108 GLU A OE2 1 
ATOM   803  N N   . ALA A 1 123 ? 1.995   9.965   -11.486 1.00 13.34  ? 109 ALA A N   1 
ATOM   804  C CA  . ALA A 1 123 ? 0.535   9.977   -11.394 1.00 13.68  ? 109 ALA A CA  1 
ATOM   805  C C   . ALA A 1 123 ? 0.030   11.389  -11.709 1.00 13.96  ? 109 ALA A C   1 
ATOM   806  O O   . ALA A 1 123 ? -0.995  11.523  -12.334 1.00 14.43  ? 109 ALA A O   1 
ATOM   807  C CB  . ALA A 1 123 ? 0.038   9.549   -10.013 1.00 13.82  ? 109 ALA A CB  1 
ATOM   808  N N   . MET A 1 124 ? 0.704   12.437  -11.209 1.00 12.75  ? 110 MET A N   1 
ATOM   809  C CA  . MET A 1 124 ? 0.345   13.834  -11.440 1.00 13.72  ? 110 MET A CA  1 
ATOM   810  C C   . MET A 1 124 ? 0.464   14.117  -12.937 1.00 16.09  ? 110 MET A C   1 
ATOM   811  O O   . MET A 1 124 ? -0.432  14.758  -13.523 1.00 16.48  ? 110 MET A O   1 
ATOM   812  C CB  . MET A 1 124 ? 1.230   14.787  -10.630 1.00 14.50  ? 110 MET A CB  1 
ATOM   813  C CG  . MET A 1 124 ? 1.069   14.617  -9.139  1.00 13.62  ? 110 MET A CG  1 
ATOM   814  S SD  . MET A 1 124 ? -0.528  15.175  -8.580  1.00 15.56  ? 110 MET A SD  1 
ATOM   815  C CE  . MET A 1 124 ? -0.271  16.950  -8.470  1.00 20.24  ? 110 MET A CE  1 
ATOM   816  N N   . LYS A 1 125 ? 1.555   13.623  -13.569 1.00 16.80  ? 111 LYS A N   1 
ATOM   817  C CA  . LYS A 1 125 ? 1.784   13.816  -15.003 1.00 18.04  ? 111 LYS A CA  1 
ATOM   818  C C   . LYS A 1 125 ? 0.663   13.147  -15.789 1.00 16.84  ? 111 LYS A C   1 
ATOM   819  O O   . LYS A 1 125 ? 0.155   13.727  -16.765 1.00 20.69  ? 111 LYS A O   1 
ATOM   820  C CB  . LYS A 1 125 ? 3.180   13.326  -15.418 1.00 23.21  ? 111 LYS A CB  1 
ATOM   821  C CG  . LYS A 1 125 ? 3.511   13.470  -16.899 1.00 27.02  ? 111 LYS A CG  1 
ATOM   822  C CD  . LYS A 1 125 ? 4.984   13.395  -17.188 1.00 42.34  ? 111 LYS A CD  1 
ATOM   823  C CE  . LYS A 1 125 ? 5.518   11.981  -17.143 1.00 61.85  ? 111 LYS A CE  1 
ATOM   824  N NZ  . LYS A 1 125 ? 4.736   11.106  -18.047 1.00 72.45  ? 111 LYS A NZ  1 
ATOM   825  N N   . ALA A 1 126 ? 0.281   11.927  -15.389 1.00 16.11  ? 112 ALA A N   1 
ATOM   826  C CA  . ALA A 1 126 ? -0.700  11.145  -16.127 1.00 17.43  ? 112 ALA A CA  1 
ATOM   827  C C   . ALA A 1 126 ? -2.068  11.826  -16.143 1.00 18.35  ? 112 ALA A C   1 
ATOM   828  O O   . ALA A 1 126 ? -2.803  11.691  -17.120 1.00 21.98  ? 112 ALA A O   1 
ATOM   829  C CB  . ALA A 1 126 ? -0.763  9.727   -15.625 1.00 20.88  ? 112 ALA A CB  1 
ATOM   830  N N   . ARG A 1 127 ? -2.401  12.588  -15.084 1.00 17.13  ? 113 ARG A N   1 
ATOM   831  C CA  . ARG A 1 127 ? -3.671  13.297  -15.018 1.00 15.60  ? 113 ARG A CA  1 
ATOM   832  C C   . ARG A 1 127 ? -3.506  14.749  -15.471 1.00 18.62  ? 113 ARG A C   1 
ATOM   833  O O   . ARG A 1 127 ? -4.455  15.537  -15.380 1.00 19.31  ? 113 ARG A O   1 
ATOM   834  C CB  . ARG A 1 127 ? -4.202  13.326  -13.584 1.00 16.23  ? 113 ARG A CB  1 
ATOM   835  C CG  . ARG A 1 127 ? -4.545  11.935  -13.061 1.00 18.98  ? 113 ARG A CG  1 
ATOM   836  C CD  . ARG A 1 127 ? -5.282  11.965  -11.712 1.00 17.66  ? 113 ARG A CD  1 
ATOM   837  N NE  . ARG A 1 127 ? -6.556  12.690  -11.828 1.00 18.04  ? 113 ARG A NE  1 
ATOM   838  C CZ  . ARG A 1 127 ? -6.991  13.598  -10.947 1.00 17.13  ? 113 ARG A CZ  1 
ATOM   839  N NH1 . ARG A 1 127 ? -8.062  14.349  -11.182 1.00 17.76  ? 113 ARG A NH1 1 
ATOM   840  N NH2 . ARG A 1 127 ? -6.395  13.709  -9.769  1.00 14.45  ? 113 ARG A NH2 1 
ATOM   841  N N   . ASN A 1 128 ? -2.300  15.107  -15.926 1.00 18.78  ? 114 ASN A N   1 
ATOM   842  C CA  . ASN A 1 128 ? -2.001  16.426  -16.468 1.00 23.39  ? 114 ASN A CA  1 
ATOM   843  C C   . ASN A 1 128 ? -2.301  17.532  -15.454 1.00 20.04  ? 114 ASN A C   1 
ATOM   844  O O   . ASN A 1 128 ? -2.853  18.588  -15.808 1.00 25.13  ? 114 ASN A O   1 
ATOM   845  C CB  . ASN A 1 128 ? -2.802  16.664  -17.750 1.00 23.50  ? 114 ASN A CB  1 
ATOM   846  C CG  . ASN A 1 128 ? -2.184  17.767  -18.583 1.00 28.04  ? 114 ASN A CG  1 
ATOM   847  O OD1 . ASN A 1 128 ? -0.978  18.024  -18.489 1.00 38.71  ? 114 ASN A OD1 1 
ATOM   848  N ND2 . ASN A 1 128 ? -3.005  18.401  -19.406 1.00 27.58  ? 114 ASN A ND2 1 
ATOM   849  N N   . ILE A 1 129 ? -1.823  17.347  -14.215 1.00 16.11  ? 115 ILE A N   1 
ATOM   850  C CA  . ILE A 1 129 ? -1.986  18.339  -13.167 1.00 17.06  ? 115 ILE A CA  1 
ATOM   851  C C   . ILE A 1 129 ? -0.666  19.096  -13.066 1.00 19.15  ? 115 ILE A C   1 
ATOM   852  O O   . ILE A 1 129 ? 0.381   18.486  -12.817 1.00 24.85  ? 115 ILE A O   1 
ATOM   853  C CB  . ILE A 1 129 ? -2.365  17.661  -11.832 1.00 17.92  ? 115 ILE A CB  1 
ATOM   854  C CG1 . ILE A 1 129 ? -3.735  16.978  -11.938 1.00 21.85  ? 115 ILE A CG1 1 
ATOM   855  C CG2 . ILE A 1 129 ? -2.334  18.652  -10.659 1.00 21.92  ? 115 ILE A CG2 1 
ATOM   856  C CD1 . ILE A 1 129 ? -3.968  16.004  -10.813 1.00 22.73  ? 115 ILE A CD1 1 
ATOM   857  N N   . LYS A 1 130 ? -0.715  20.411  -13.313 1.00 24.38  ? 116 LYS A N   1 
ATOM   858  C CA  . LYS A 1 130 ? 0.540   21.138  -13.484 1.00 27.08  ? 116 LYS A CA  1 
ATOM   859  C C   . LYS A 1 130 ? 0.905   22.009  -12.287 1.00 25.23  ? 116 LYS A C   1 
ATOM   860  O O   . LYS A 1 130 ? 1.993   22.586  -12.292 1.00 27.08  ? 116 LYS A O   1 
ATOM   861  C CB  . LYS A 1 130 ? 0.491   21.996  -14.749 1.00 50.18  ? 116 LYS A CB  1 
ATOM   862  C CG  . LYS A 1 130 ? 0.728   21.220  -16.043 1.00 36.71  ? 116 LYS A CG  1 
ATOM   863  C CD  . LYS A 1 130 ? -0.409  21.306  -17.005 1.00 56.25  ? 116 LYS A CD  1 
ATOM   864  C CE  . LYS A 1 130 ? 0.056   21.081  -18.426 1.00 49.32  ? 116 LYS A CE  1 
ATOM   865  N NZ  . LYS A 1 130 ? 0.928   19.892  -18.584 1.00 54.08  ? 116 LYS A NZ  1 
ATOM   866  N N   . LYS A 1 131 ? 0.052   22.068  -11.256 1.00 22.21  ? 117 LYS A N   1 
ATOM   867  C CA  . LYS A 1 131 ? 0.400   22.798  -10.039 1.00 19.14  ? 117 LYS A CA  1 
ATOM   868  C C   . LYS A 1 131 ? 1.805   22.404  -9.536  1.00 23.43  ? 117 LYS A C   1 
ATOM   869  O O   . LYS A 1 131 ? 2.220   21.235  -9.566  1.00 23.07  ? 117 LYS A O   1 
ATOM   870  C CB  . LYS A 1 131 ? -0.627  22.513  -8.940  1.00 27.83  ? 117 LYS A CB  1 
ATOM   871  N N   . LYS A 1 132 ? 2.537   23.399  -9.017  1.00 20.00  ? 118 LYS A N   1 
ATOM   872  C CA  . LYS A 1 132 ? 3.812   23.172  -8.351  1.00 18.35  ? 118 LYS A CA  1 
ATOM   873  C C   . LYS A 1 132 ? 3.541   22.390  -7.061  1.00 19.75  ? 118 LYS A C   1 
ATOM   874  O O   . LYS A 1 132 ? 2.635   22.737  -6.303  1.00 25.65  ? 118 LYS A O   1 
ATOM   875  C CB  . LYS A 1 132 ? 4.543   24.493  -8.105  1.00 23.44  ? 118 LYS A CB  1 
ATOM   876  N N   . VAL A 1 133 ? 4.266   21.277  -6.875  1.00 17.34  ? 119 VAL A N   1 
ATOM   877  C CA  . VAL A 1 133 ? 4.197   20.469  -5.662  1.00 16.87  ? 119 VAL A CA  1 
ATOM   878  C C   . VAL A 1 133 ? 5.590   20.478  -5.038  1.00 12.72  ? 119 VAL A C   1 
ATOM   879  O O   . VAL A 1 133 ? 6.610   20.326  -5.731  1.00 16.68  ? 119 VAL A O   1 
ATOM   880  C CB  . VAL A 1 133 ? 3.769   19.021  -6.001  1.00 16.47  ? 119 VAL A CB  1 
ATOM   881  C CG1 . VAL A 1 133 ? 3.762   18.102  -4.797  1.00 17.56  ? 119 VAL A CG1 1 
ATOM   882  C CG2 . VAL A 1 133 ? 2.360   19.003  -6.591  1.00 21.58  ? 119 VAL A CG2 1 
ATOM   883  N N   . ARG A 1 134 ? 5.644   20.667  -3.724  1.00 12.53  ? 120 ARG A N   1 
ATOM   884  C CA  . ARG A 1 134 ? 6.900   20.549  -2.997  1.00 11.75  ? 120 ARG A CA  1 
ATOM   885  C C   . ARG A 1 134 ? 7.109   19.100  -2.558  1.00 10.01  ? 120 ARG A C   1 
ATOM   886  O O   . ARG A 1 134 ? 6.676   18.717  -1.460  1.00 11.48  ? 120 ARG A O   1 
ATOM   887  C CB  . ARG A 1 134 ? 6.993   21.457  -1.765  1.00 14.43  ? 120 ARG A CB  1 
ATOM   888  C CG  . ARG A 1 134 ? 8.404   21.433  -1.169  1.00 17.82  ? 120 ARG A CG  1 
ATOM   889  C CD  . ARG A 1 134 ? 8.826   22.427  -0.093  1.00 23.90  ? 120 ARG A CD  1 
ATOM   890  N NE  . ARG A 1 134 ? 8.842   23.765  -0.634  1.00 27.13  ? 120 ARG A NE  1 
ATOM   891  C CZ  . ARG A 1 134 ? 8.899   24.899  0.072   1.00 34.21  ? 120 ARG A CZ  1 
ATOM   892  N NH1 . ARG A 1 134 ? 8.754   24.896  1.392   1.00 31.42  ? 120 ARG A NH1 1 
ATOM   893  N NH2 . ARG A 1 134 ? 9.059   26.041  -0.578  1.00 27.83  ? 120 ARG A NH2 1 
ATOM   894  N N   . TYR A 1 135 ? 7.796   18.326  -3.403  1.00 9.56   ? 121 TYR A N   1 
ATOM   895  C CA  . TYR A 1 135 ? 8.193   16.987  -3.012  1.00 8.63   ? 121 TYR A CA  1 
ATOM   896  C C   . TYR A 1 135 ? 9.421   16.999  -2.123  1.00 9.48   ? 121 TYR A C   1 
ATOM   897  O O   . TYR A 1 135 ? 10.344  17.805  -2.352  1.00 10.62  ? 121 TYR A O   1 
ATOM   898  C CB  . TYR A 1 135 ? 8.497   16.116  -4.233  1.00 9.69   ? 121 TYR A CB  1 
ATOM   899  C CG  . TYR A 1 135 ? 7.341   15.943  -5.176  1.00 8.95   ? 121 TYR A CG  1 
ATOM   900  C CD1 . TYR A 1 135 ? 6.281   15.112  -4.819  1.00 11.43  ? 121 TYR A CD1 1 
ATOM   901  C CD2 . TYR A 1 135 ? 7.262   16.629  -6.367  1.00 9.98   ? 121 TYR A CD2 1 
ATOM   902  C CE1 . TYR A 1 135 ? 5.188   14.958  -5.668  1.00 14.50  ? 121 TYR A CE1 1 
ATOM   903  C CE2 . TYR A 1 135 ? 6.163   16.536  -7.192  1.00 12.61  ? 121 TYR A CE2 1 
ATOM   904  C CZ  . TYR A 1 135 ? 5.152   15.644  -6.870  1.00 13.34  ? 121 TYR A CZ  1 
ATOM   905  O OH  . TYR A 1 135 ? 4.064   15.531  -7.711  1.00 17.13  ? 121 TYR A OH  1 
ATOM   906  N N   . TYR A 1 136 ? 9.475   16.097  -1.151  1.00 8.37   ? 122 TYR A N   1 
ATOM   907  C CA  . TYR A 1 136 ? 10.679  15.852  -0.353  1.00 9.40   ? 122 TYR A CA  1 
ATOM   908  C C   . TYR A 1 136 ? 10.930  14.355  -0.380  1.00 9.99   ? 122 TYR A C   1 
ATOM   909  O O   . TYR A 1 136 ? 10.185  13.581  0.226   1.00 10.08  ? 122 TYR A O   1 
ATOM   910  C CB  . TYR A 1 136 ? 10.482  16.141  1.146   1.00 10.94  ? 122 TYR A CB  1 
ATOM   911  C CG  . TYR A 1 136 ? 10.487  17.561  1.632   1.00 15.29  ? 122 TYR A CG  1 
ATOM   912  C CD1 . TYR A 1 136 ? 11.598  18.017  2.344   1.00 15.10  ? 122 TYR A CD1 1 
ATOM   913  C CD2 . TYR A 1 136 ? 9.392   18.425  1.460   1.00 16.95  ? 122 TYR A CD2 1 
ATOM   914  C CE1 . TYR A 1 136 ? 11.639  19.312  2.843   1.00 16.63  ? 122 TYR A CE1 1 
ATOM   915  C CE2 . TYR A 1 136 ? 9.410   19.705  1.996   1.00 16.78  ? 122 TYR A CE2 1 
ATOM   916  C CZ  . TYR A 1 136 ? 10.546  20.136  2.663   1.00 16.45  ? 122 TYR A CZ  1 
ATOM   917  O OH  . TYR A 1 136 ? 10.558  21.413  3.167   1.00 21.08  ? 122 TYR A OH  1 
ATOM   918  N N   . THR A 1 137 ? 12.030  13.980  -1.007  1.00 9.06   ? 123 THR A N   1 
ATOM   919  C CA  . THR A 1 137 ? 12.468  12.594  -0.907  1.00 9.39   ? 123 THR A CA  1 
ATOM   920  C C   . THR A 1 137 ? 13.203  12.377  0.418   1.00 9.76   ? 123 THR A C   1 
ATOM   921  O O   . THR A 1 137 ? 14.179  13.065  0.735   1.00 14.56  ? 123 THR A O   1 
ATOM   922  C CB  . THR A 1 137 ? 13.439  12.270  -2.057  1.00 10.59  ? 123 THR A CB  1 
ATOM   923  O OG1 . THR A 1 137 ? 12.702  12.362  -3.267  1.00 13.71  ? 123 THR A OG1 1 
ATOM   924  C CG2 . THR A 1 137 ? 14.060  10.877  -1.960  1.00 13.32  ? 123 THR A CG2 1 
ATOM   925  N N   . VAL A 1 138 ? 12.669  11.439  1.204   1.00 9.24   ? 124 VAL A N   1 
ATOM   926  C CA  . VAL A 1 138 ? 13.209  11.087  2.506   1.00 9.68   ? 124 VAL A CA  1 
ATOM   927  C C   . VAL A 1 138 ? 13.732  9.647   2.463   1.00 10.60  ? 124 VAL A C   1 
ATOM   928  O O   . VAL A 1 138 ? 13.392  8.849   1.603   1.00 10.17  ? 124 VAL A O   1 
ATOM   929  C CB  . VAL A 1 138 ? 12.197  11.258  3.667   1.00 9.85   ? 124 VAL A CB  1 
ATOM   930  C CG1 . VAL A 1 138 ? 11.788  12.707  3.835   1.00 13.14  ? 124 VAL A CG1 1 
ATOM   931  C CG2 . VAL A 1 138 ? 10.953  10.402  3.481   1.00 10.78  ? 124 VAL A CG2 1 
ATOM   932  N N   . ASN A 1 139 ? 14.584  9.344   3.446   1.00 10.39  ? 125 ASN A N   1 
ATOM   933  C CA  . ASN A 1 139 ? 15.020  7.978   3.651   1.00 10.86  ? 125 ASN A CA  1 
ATOM   934  C C   . ASN A 1 139 ? 15.074  7.751   5.160   1.00 10.24  ? 125 ASN A C   1 
ATOM   935  O O   . ASN A 1 139 ? 14.723  8.625   5.969   1.00 11.41  ? 125 ASN A O   1 
ATOM   936  C CB  . ASN A 1 139 ? 16.380  7.738   2.971   1.00 11.77  ? 125 ASN A CB  1 
ATOM   937  C CG  . ASN A 1 139 ? 17.504  8.618   3.455   1.00 12.35  ? 125 ASN A CG  1 
ATOM   938  O OD1 . ASN A 1 139 ? 17.600  8.959   4.613   1.00 14.39  ? 125 ASN A OD1 1 
ATOM   939  N ND2 . ASN A 1 139 ? 18.305  9.104   2.529   1.00 23.43  ? 125 ASN A ND2 1 
ATOM   940  N N   . HIS A 1 140 ? 15.597  6.585   5.559   1.00 11.63  ? 126 HIS A N   1 
ATOM   941  C CA  . HIS A 1 140 ? 15.560  6.262   6.974   1.00 12.45  ? 126 HIS A CA  1 
ATOM   942  C C   . HIS A 1 140 ? 16.522  7.077   7.833   1.00 13.24  ? 126 HIS A C   1 
ATOM   943  O O   . HIS A 1 140 ? 16.420  6.998   9.052   1.00 15.79  ? 126 HIS A O   1 
ATOM   944  C CB  . HIS A 1 140 ? 15.757  4.767   7.184   1.00 12.95  ? 126 HIS A CB  1 
ATOM   945  C CG  . HIS A 1 140 ? 17.144  4.262   6.863   1.00 13.46  ? 126 HIS A CG  1 
ATOM   946  N ND1 . HIS A 1 140 ? 17.539  2.976   7.182   1.00 18.53  ? 126 HIS A ND1 1 
ATOM   947  C CD2 . HIS A 1 140 ? 18.214  4.869   6.273   1.00 15.45  ? 126 HIS A CD2 1 
ATOM   948  C CE1 . HIS A 1 140 ? 18.815  2.800   6.804   1.00 19.36  ? 126 HIS A CE1 1 
ATOM   949  N NE2 . HIS A 1 140 ? 19.234  3.957   6.212   1.00 22.46  ? 126 HIS A NE2 1 
ATOM   950  N N   . ASP A 1 141 ? 17.368  7.917   7.200   1.00 12.18  ? 127 ASP A N   1 
ATOM   951  C CA  . ASP A 1 141 ? 18.164  8.840   7.993   1.00 16.04  ? 127 ASP A CA  1 
ATOM   952  C C   . ASP A 1 141 ? 17.546  10.240  8.096   1.00 13.90  ? 127 ASP A C   1 
ATOM   953  O O   . ASP A 1 141 ? 18.041  11.059  8.842   1.00 18.35  ? 127 ASP A O   1 
ATOM   954  C CB  . ASP A 1 141 ? 19.595  8.915   7.461   1.00 16.35  ? 127 ASP A CB  1 
ATOM   955  C CG  . ASP A 1 141 ? 20.334  7.593   7.637   1.00 23.67  ? 127 ASP A CG  1 
ATOM   956  O OD1 . ASP A 1 141 ? 20.121  6.902   8.680   1.00 20.60  ? 127 ASP A OD1 1 
ATOM   957  O OD2 . ASP A 1 141 ? 21.128  7.256   6.746   1.00 27.62  ? 127 ASP A OD2 1 
ATOM   958  N N   . SER A 1 142 ? 16.404  10.513  7.425   1.00 12.04  ? 128 SER A N   1 
ATOM   959  C CA  . SER A 1 142 ? 15.845  11.856  7.368   1.00 12.01  ? 128 SER A CA  1 
ATOM   960  C C   . SER A 1 142 ? 15.133  12.157  8.689   1.00 11.88  ? 128 SER A C   1 
ATOM   961  O O   . SER A 1 142 ? 14.368  11.340  9.192   1.00 14.18  ? 128 SER A O   1 
ATOM   962  C CB  . SER A 1 142 ? 14.834  11.900  6.250   1.00 12.77  ? 128 SER A CB  1 
ATOM   963  O OG  . SER A 1 142 ? 15.427  11.655  4.978   1.00 12.53  ? 128 SER A OG  1 
ATOM   964  N N   . ILE A 1 143 ? 15.270  13.390  9.187   1.00 12.87  ? 129 ILE A N   1 
ATOM   965  C CA  . ILE A 1 143 ? 14.500  13.898  10.319  1.00 14.58  ? 129 ILE A CA  1 
ATOM   966  C C   . ILE A 1 143 ? 13.923  15.238  9.871   1.00 13.18  ? 129 ILE A C   1 
ATOM   967  O O   . ILE A 1 143 ? 14.641  16.202  9.572   1.00 15.81  ? 129 ILE A O   1 
ATOM   968  C CB  . ILE A 1 143 ? 15.349  14.042  11.600  1.00 15.73  ? 129 ILE A CB  1 
ATOM   969  C CG1 . ILE A 1 143 ? 15.890  12.671  12.050  1.00 17.58  ? 129 ILE A CG1 1 
ATOM   970  C CG2 . ILE A 1 143 ? 14.451  14.641  12.690  1.00 15.53  ? 129 ILE A CG2 1 
ATOM   971  C CD1 . ILE A 1 143 ? 16.804  12.703  13.273  1.00 23.17  ? 129 ILE A CD1 1 
ATOM   972  N N   . MET A 1 144 ? 12.606  15.266  9.697   1.00 11.12  ? 130 MET A N   1 
ATOM   973  C CA  . MET A 1 144 ? 11.931  16.476  9.229   1.00 11.84  ? 130 MET A CA  1 
ATOM   974  C C   . MET A 1 144 ? 11.431  17.265  10.445  1.00 12.76  ? 130 MET A C   1 
ATOM   975  O O   . MET A 1 144 ? 10.747  16.703  11.310  1.00 12.68  ? 130 MET A O   1 
ATOM   976  C CB  . MET A 1 144 ? 10.729  16.062  8.346   1.00 12.74  ? 130 MET A CB  1 
ATOM   977  C CG  . MET A 1 144 ? 11.111  15.257  7.074   1.00 12.81  ? 130 MET A CG  1 
ATOM   978  S SD  . MET A 1 144 ? 12.112  16.247  5.842   1.00 18.52  ? 130 MET A SD  1 
ATOM   979  C CE  . MET A 1 144 ? 13.749  15.612  6.164   1.00 19.24  ? 130 MET A CE  1 
ATOM   980  N N   . ARG A 1 145 ? 11.807  18.531  10.536  1.00 13.51  ? 131 ARG A N   1 
ATOM   981  C CA  . ARG A 1 145 ? 11.605  19.327  11.744  1.00 14.68  ? 131 ARG A CA  1 
ATOM   982  C C   . ARG A 1 145 ? 10.479  20.329  11.508  1.00 13.37  ? 131 ARG A C   1 
ATOM   983  O O   . ARG A 1 145 ? 10.535  21.083  10.553  1.00 17.75  ? 131 ARG A O   1 
ATOM   984  C CB  . ARG A 1 145 ? 12.928  20.029  12.080  1.00 15.41  ? 131 ARG A CB  1 
ATOM   985  C CG  . ARG A 1 145 ? 14.030  19.043  12.441  1.00 19.75  ? 131 ARG A CG  1 
ATOM   986  C CD  . ARG A 1 145 ? 15.251  19.739  13.011  1.00 24.32  ? 131 ARG A CD  1 
ATOM   987  N NE  . ARG A 1 145 ? 16.135  18.745  13.607  1.00 39.70  ? 131 ARG A NE  1 
ATOM   988  C CZ  . ARG A 1 145 ? 16.730  17.747  12.974  1.00 42.75  ? 131 ARG A CZ  1 
ATOM   989  N NH1 . ARG A 1 145 ? 16.633  17.618  11.661  1.00 57.80  ? 131 ARG A NH1 1 
ATOM   990  N NH2 . ARG A 1 145 ? 17.442  16.881  13.670  1.00 46.00  ? 131 ARG A NH2 1 
ATOM   991  N N   . PHE A 1 146 ? 9.402   20.210  12.305  1.00 12.66  ? 132 PHE A N   1 
ATOM   992  C CA  . PHE A 1 146 ? 8.248   21.110  12.245  1.00 13.89  ? 132 PHE A CA  1 
ATOM   993  C C   . PHE A 1 146 ? 8.338   22.003  13.491  1.00 15.62  ? 132 PHE A C   1 
ATOM   994  O O   . PHE A 1 146 ? 9.330   21.994  14.202  1.00 20.08  ? 132 PHE A O   1 
ATOM   995  C CB  . PHE A 1 146 ? 6.936   20.330  12.050  1.00 15.21  ? 132 PHE A CB  1 
ATOM   996  C CG  . PHE A 1 146 ? 6.996   19.544  10.775  1.00 12.94  ? 132 PHE A CG  1 
ATOM   997  C CD1 . PHE A 1 146 ? 6.574   20.109  9.576   1.00 13.87  ? 132 PHE A CD1 1 
ATOM   998  C CD2 . PHE A 1 146 ? 7.441   18.219  10.800  1.00 11.30  ? 132 PHE A CD2 1 
ATOM   999  C CE1 . PHE A 1 146 ? 6.653   19.386  8.396   1.00 12.67  ? 132 PHE A CE1 1 
ATOM   1000 C CE2 . PHE A 1 146 ? 7.517   17.515  9.618   1.00 10.57  ? 132 PHE A CE2 1 
ATOM   1001 C CZ  . PHE A 1 146 ? 7.118   18.086  8.426   1.00 12.63  ? 132 PHE A CZ  1 
ATOM   1002 N N   . LYS A 1 147 ? 7.284   22.759  13.795  1.00 14.89  ? 133 LYS A N   1 
ATOM   1003 C CA  . LYS A 1 147 ? 7.320   23.662  14.934  1.00 18.96  ? 133 LYS A CA  1 
ATOM   1004 C C   . LYS A 1 147 ? 7.237   22.877  16.240  1.00 19.31  ? 133 LYS A C   1 
ATOM   1005 O O   . LYS A 1 147 ? 7.961   23.193  17.189  1.00 52.23  ? 133 LYS A O   1 
ATOM   1006 C CB  . LYS A 1 147 ? 6.171   24.667  14.809  1.00 21.07  ? 133 LYS A CB  1 
ATOM   1007 C CG  . LYS A 1 147 ? 6.032   25.691  15.925  1.00 30.71  ? 133 LYS A CG  1 
ATOM   1008 N N   . ASN A 1 148 ? 6.369   21.856  16.271  1.00 20.09  ? 134 ASN A N   1 
ATOM   1009 C CA  . ASN A 1 148 ? 5.923   21.203  17.501  1.00 27.36  ? 134 ASN A CA  1 
ATOM   1010 C C   . ASN A 1 148 ? 6.608   19.854  17.679  1.00 20.24  ? 134 ASN A C   1 
ATOM   1011 O O   . ASN A 1 148 ? 6.697   19.330  18.784  1.00 21.15  ? 134 ASN A O   1 
ATOM   1012 C CB  . ASN A 1 148 ? 4.424   20.863  17.455  1.00 28.28  ? 134 ASN A CB  1 
ATOM   1013 C CG  . ASN A 1 148 ? 3.501   22.070  17.428  1.00 25.31  ? 134 ASN A CG  1 
ATOM   1014 O OD1 . ASN A 1 148 ? 2.317   21.901  17.161  1.00 34.25  ? 134 ASN A OD1 1 
ATOM   1015 N ND2 . ASN A 1 148 ? 3.995   23.279  17.676  1.00 26.97  ? 134 ASN A ND2 1 
ATOM   1016 N N   . VAL A 1 149 ? 7.028   19.259  16.554  1.00 14.32  ? 135 VAL A N   1 
ATOM   1017 C CA  . VAL A 1 149 ? 7.413   17.855  16.496  1.00 11.98  ? 135 VAL A CA  1 
ATOM   1018 C C   . VAL A 1 149 ? 8.486   17.713  15.414  1.00 11.99  ? 135 VAL A C   1 
ATOM   1019 O O   . VAL A 1 149 ? 8.614   18.522  14.474  1.00 13.55  ? 135 VAL A O   1 
ATOM   1020 C CB  . VAL A 1 149 ? 6.240   16.935  16.094  1.00 15.15  ? 135 VAL A CB  1 
ATOM   1021 C CG1 . VAL A 1 149 ? 5.134   16.953  17.127  1.00 17.29  ? 135 VAL A CG1 1 
ATOM   1022 C CG2 . VAL A 1 149 ? 5.722   17.218  14.700  1.00 17.10  ? 135 VAL A CG2 1 
ATOM   1023 N N   . ASN A 1 150 ? 9.165   16.567  15.506  1.00 13.03  ? 136 ASN A N   1 
ATOM   1024 C CA  . ASN A 1 150 ? 10.097  16.071  14.483  1.00 12.43  ? 136 ASN A CA  1 
ATOM   1025 C C   . ASN A 1 150 ? 9.545   14.748  13.981  1.00 10.44  ? 136 ASN A C   1 
ATOM   1026 O O   . ASN A 1 150 ? 8.877   14.066  14.757  1.00 12.19  ? 136 ASN A O   1 
ATOM   1027 C CB  . ASN A 1 150 ? 11.481  15.776  15.073  1.00 14.77  ? 136 ASN A CB  1 
ATOM   1028 C CG  . ASN A 1 150 ? 12.161  17.047  15.531  1.00 19.30  ? 136 ASN A CG  1 
ATOM   1029 O OD1 . ASN A 1 150 ? 12.033  18.100  14.907  1.00 20.25  ? 136 ASN A OD1 1 
ATOM   1030 N ND2 . ASN A 1 150 ? 12.807  16.961  16.679  1.00 27.09  ? 136 ASN A ND2 1 
ATOM   1031 N N   . VAL A 1 151 ? 9.711   14.492  12.677  1.00 9.83   ? 137 VAL A N   1 
ATOM   1032 C CA  . VAL A 1 151 ? 9.224   13.263  12.071  1.00 10.90  ? 137 VAL A CA  1 
ATOM   1033 C C   . VAL A 1 151 ? 10.422  12.505  11.497  1.00 10.87  ? 137 VAL A C   1 
ATOM   1034 O O   . VAL A 1 151 ? 11.175  13.041  10.701  1.00 11.69  ? 137 VAL A O   1 
ATOM   1035 C CB  . VAL A 1 151 ? 8.179   13.545  10.974  1.00 10.41  ? 137 VAL A CB  1 
ATOM   1036 C CG1 . VAL A 1 151 ? 7.695   12.228  10.375  1.00 12.02  ? 137 VAL A CG1 1 
ATOM   1037 C CG2 . VAL A 1 151 ? 7.001   14.355  11.500  1.00 11.42  ? 137 VAL A CG2 1 
ATOM   1038 N N   . SER A 1 152 ? 10.510  11.196  11.838  1.00 10.32  ? 138 SER A N   1 
ATOM   1039 C CA  . SER A 1 152 ? 11.581  10.338  11.325  1.00 10.52  ? 138 SER A CA  1 
ATOM   1040 C C   . SER A 1 152 ? 10.945  9.126   10.639  1.00 8.91   ? 138 SER A C   1 
ATOM   1041 O O   . SER A 1 152 ? 9.716   8.996   10.622  1.00 9.56   ? 138 SER A O   1 
ATOM   1042 C CB  . SER A 1 152 ? 12.544  9.934   12.426  1.00 11.79  ? 138 SER A CB  1 
ATOM   1043 O OG  . SER A 1 152 ? 11.922  9.091   13.426  1.00 12.74  ? 138 SER A OG  1 
ATOM   1044 N N   . PHE A 1 153 ? 11.772  8.274   10.031  1.00 10.58  ? 139 PHE A N   1 
ATOM   1045 C CA  . PHE A 1 153 ? 11.293  7.204   9.169   1.00 8.46   ? 139 PHE A CA  1 
ATOM   1046 C C   . PHE A 1 153 ? 12.147  5.973   9.385   1.00 10.15  ? 139 PHE A C   1 
ATOM   1047 O O   . PHE A 1 153 ? 13.332  6.074   9.770   1.00 13.86  ? 139 PHE A O   1 
ATOM   1048 C CB  . PHE A 1 153 ? 11.394  7.634   7.697   1.00 10.72  ? 139 PHE A CB  1 
ATOM   1049 C CG  . PHE A 1 153 ? 10.688  8.939   7.407   1.00 9.20   ? 139 PHE A CG  1 
ATOM   1050 C CD1 . PHE A 1 153 ? 9.337   8.967   7.062   1.00 10.47  ? 139 PHE A CD1 1 
ATOM   1051 C CD2 . PHE A 1 153 ? 11.344  10.153  7.541   1.00 10.98  ? 139 PHE A CD2 1 
ATOM   1052 C CE1 . PHE A 1 153 ? 8.690   10.164  6.820   1.00 10.82  ? 139 PHE A CE1 1 
ATOM   1053 C CE2 . PHE A 1 153 ? 10.690  11.366  7.350   1.00 10.35  ? 139 PHE A CE2 1 
ATOM   1054 C CZ  . PHE A 1 153 ? 9.345   11.373  7.037   1.00 12.36  ? 139 PHE A CZ  1 
ATOM   1055 N N   . PHE A 1 154 ? 11.573  4.820   9.061   1.00 9.69   ? 140 PHE A N   1 
ATOM   1056 C CA  . PHE A 1 154 ? 12.278  3.554   9.197   1.00 8.60   ? 140 PHE A CA  1 
ATOM   1057 C C   . PHE A 1 154 ? 11.887  2.631   8.068   1.00 8.35   ? 140 PHE A C   1 
ATOM   1058 O O   . PHE A 1 154 ? 10.724  2.604   7.663   1.00 9.58   ? 140 PHE A O   1 
ATOM   1059 C CB  . PHE A 1 154 ? 12.111  2.934   10.585  1.00 11.23  ? 140 PHE A CB  1 
ATOM   1060 C CG  . PHE A 1 154 ? 10.673  2.666   10.971  1.00 9.08   ? 140 PHE A CG  1 
ATOM   1061 C CD1 . PHE A 1 154 ? 9.925   3.660   11.591  1.00 9.62   ? 140 PHE A CD1 1 
ATOM   1062 C CD2 . PHE A 1 154 ? 10.062  1.445   10.701  1.00 9.71   ? 140 PHE A CD2 1 
ATOM   1063 C CE1 . PHE A 1 154 ? 8.617   3.418   11.990  1.00 11.56  ? 140 PHE A CE1 1 
ATOM   1064 C CE2 . PHE A 1 154 ? 8.757   1.195   11.115  1.00 10.76  ? 140 PHE A CE2 1 
ATOM   1065 C CZ  . PHE A 1 154 ? 8.045   2.191   11.768  1.00 11.41  ? 140 PHE A CZ  1 
ATOM   1066 N N   . ASN A 1 155 ? 12.841  1.857   7.533   1.00 9.23   ? 141 ASN A N   1 
ATOM   1067 C CA  . ASN A 1 155 ? 12.528  0.936   6.454   1.00 10.35  ? 141 ASN A CA  1 
ATOM   1068 C C   . ASN A 1 155 ? 11.629  -0.192  6.958   1.00 10.02  ? 141 ASN A C   1 
ATOM   1069 O O   . ASN A 1 155 ? 11.829  -0.774  8.038   1.00 10.29  ? 141 ASN A O   1 
ATOM   1070 C CB  . ASN A 1 155 ? 13.821  0.270   5.972   1.00 13.12  ? 141 ASN A CB  1 
ATOM   1071 C CG  . ASN A 1 155 ? 14.882  1.146   5.323   1.00 14.82  ? 141 ASN A CG  1 
ATOM   1072 O OD1 . ASN A 1 155 ? 16.069  0.796   5.256   1.00 23.36  ? 141 ASN A OD1 1 
ATOM   1073 N ND2 . ASN A 1 155 ? 14.559  2.311   4.877   1.00 11.60  ? 141 ASN A ND2 1 
ATOM   1074 N N   . THR A 1 156 ? 10.624  -0.481  6.133   1.00 10.69  ? 142 THR A N   1 
ATOM   1075 C CA  . THR A 1 156 ? 9.786   -1.648  6.335   1.00 9.40   ? 142 THR A CA  1 
ATOM   1076 C C   . THR A 1 156 ? 9.906   -2.574  5.135   1.00 11.95  ? 142 THR A C   1 
ATOM   1077 O O   . THR A 1 156 ? 10.414  -2.195  4.074   1.00 13.55  ? 142 THR A O   1 
ATOM   1078 C CB  . THR A 1 156 ? 8.309   -1.234  6.532   1.00 9.50   ? 142 THR A CB  1 
ATOM   1079 O OG1 . THR A 1 156 ? 7.988   -0.424  5.386   1.00 10.71  ? 142 THR A OG1 1 
ATOM   1080 C CG2 . THR A 1 156 ? 8.040   -0.446  7.816   1.00 9.60   ? 142 THR A CG2 1 
ATOM   1081 N N   . THR A 1 157 ? 9.413   -3.813  5.335   1.00 10.79  ? 143 THR A N   1 
ATOM   1082 C CA  . THR A 1 157 ? 9.371   -4.792  4.255   1.00 12.09  ? 143 THR A CA  1 
ATOM   1083 C C   . THR A 1 157 ? 7.960   -4.918  3.716   1.00 11.18  ? 143 THR A C   1 
ATOM   1084 O O   . THR A 1 157 ? 6.997   -5.155  4.436   1.00 11.40  ? 143 THR A O   1 
ATOM   1085 C CB  . THR A 1 157 ? 9.776   -6.181  4.796   1.00 11.04  ? 143 THR A CB  1 
ATOM   1086 O OG1 . THR A 1 157 ? 11.097  -6.084  5.346   1.00 14.00  ? 143 THR A OG1 1 
ATOM   1087 C CG2 . THR A 1 157 ? 9.781   -7.251  3.717   1.00 14.89  ? 143 THR A CG2 1 
ATOM   1088 N N   . HIS A 1 158 ? 7.872   -4.840  2.392   1.00 13.31  ? 144 HIS A N   1 
ATOM   1089 C CA  . HIS A 1 158 ? 6.598   -4.947  1.703   1.00 12.84  ? 144 HIS A CA  1 
ATOM   1090 C C   . HIS A 1 158 ? 6.870   -5.610  0.338   1.00 12.95  ? 144 HIS A C   1 
ATOM   1091 O O   . HIS A 1 158 ? 8.010   -5.949  0.051   1.00 17.89  ? 144 HIS A O   1 
ATOM   1092 C CB  . HIS A 1 158 ? 6.005   -3.543  1.568   1.00 18.16  ? 144 HIS A CB  1 
ATOM   1093 C CG  . HIS A 1 158 ? 4.598   -3.494  1.094   1.00 19.36  ? 144 HIS A CG  1 
ATOM   1094 N ND1 . HIS A 1 158 ? 4.280   -3.352  -0.235  1.00 23.65  ? 144 HIS A ND1 1 
ATOM   1095 C CD2 . HIS A 1 158 ? 3.431   -3.622  1.767   1.00 20.24  ? 144 HIS A CD2 1 
ATOM   1096 C CE1 . HIS A 1 158 ? 2.958   -3.360  -0.362  1.00 21.04  ? 144 HIS A CE1 1 
ATOM   1097 N NE2 . HIS A 1 158 ? 2.403   -3.512  0.859   1.00 21.99  ? 144 HIS A NE2 1 
ATOM   1098 N N   . SER A 1 159 ? 5.876   -5.661  -0.560  1.00 12.00  ? 145 SER A N   1 
ATOM   1099 C CA  . SER A 1 159 ? 6.041   -6.182  -1.920  1.00 12.80  ? 145 SER A CA  1 
ATOM   1100 C C   . SER A 1 159 ? 6.552   -5.129  -2.904  1.00 11.42  ? 145 SER A C   1 
ATOM   1101 O O   . SER A 1 159 ? 6.965   -5.490  -4.018  1.00 16.26  ? 145 SER A O   1 
ATOM   1102 C CB  . SER A 1 159 ? 4.767   -6.809  -2.435  1.00 14.72  ? 145 SER A CB  1 
ATOM   1103 O OG  . SER A 1 159 ? 3.644   -5.952  -2.213  1.00 28.26  ? 145 SER A OG  1 
ATOM   1104 N N   . ILE A 1 160 ? 6.567   -3.852  -2.481  1.00 10.56  ? 146 ILE A N   1 
ATOM   1105 C CA  . ILE A 1 160 ? 7.197   -2.786  -3.242  1.00 9.69   ? 146 ILE A CA  1 
ATOM   1106 C C   . ILE A 1 160 ? 8.382   -2.336  -2.410  1.00 10.89  ? 146 ILE A C   1 
ATOM   1107 O O   . ILE A 1 160 ? 8.291   -2.310  -1.168  1.00 12.46  ? 146 ILE A O   1 
ATOM   1108 C CB  . ILE A 1 160 ? 6.179   -1.657  -3.574  1.00 9.85   ? 146 ILE A CB  1 
ATOM   1109 C CG1 . ILE A 1 160 ? 6.684   -0.741  -4.670  1.00 9.77   ? 146 ILE A CG1 1 
ATOM   1110 C CG2 . ILE A 1 160 ? 5.818   -0.833  -2.369  1.00 11.54  ? 146 ILE A CG2 1 
ATOM   1111 C CD1 . ILE A 1 160 ? 5.630   0.239   -5.176  1.00 13.35  ? 146 ILE A CD1 1 
ATOM   1112 N N   . PRO A 1 161 ? 9.532   -2.058  -3.058  1.00 11.07  ? 147 PRO A N   1 
ATOM   1113 C CA  . PRO A 1 161 ? 10.698  -1.598  -2.317  1.00 12.05  ? 147 PRO A CA  1 
ATOM   1114 C C   . PRO A 1 161 ? 10.567  -0.140  -1.888  1.00 8.98   ? 147 PRO A C   1 
ATOM   1115 O O   . PRO A 1 161 ? 9.613   0.565   -2.263  1.00 11.48  ? 147 PRO A O   1 
ATOM   1116 C CB  . PRO A 1 161 ? 11.865  -1.848  -3.280  1.00 15.65  ? 147 PRO A CB  1 
ATOM   1117 C CG  . PRO A 1 161 ? 11.258  -1.673  -4.632  1.00 14.42  ? 147 PRO A CG  1 
ATOM   1118 C CD  . PRO A 1 161 ? 9.824   -2.180  -4.491  1.00 11.67  ? 147 PRO A CD  1 
ATOM   1119 N N   . ASP A 1 162 ? 11.467  0.274   -1.012  1.00 11.93  ? 148 ASP A N   1 
ATOM   1120 C CA  . ASP A 1 162 ? 11.572  1.656   -0.552  1.00 10.53  ? 148 ASP A CA  1 
ATOM   1121 C C   . ASP A 1 162 ? 10.280  2.008   0.189   1.00 10.27  ? 148 ASP A C   1 
ATOM   1122 O O   . ASP A 1 162 ? 9.694   3.088   0.014   1.00 10.97  ? 148 ASP A O   1 
ATOM   1123 C CB  . ASP A 1 162 ? 11.796  2.625   -1.718  1.00 14.05  ? 148 ASP A CB  1 
ATOM   1124 C CG  . ASP A 1 162 ? 13.216  2.712   -2.249  1.00 23.35  ? 148 ASP A CG  1 
ATOM   1125 O OD1 . ASP A 1 162 ? 13.457  3.660   -3.054  1.00 23.74  ? 148 ASP A OD1 1 
ATOM   1126 O OD2 . ASP A 1 162 ? 14.036  1.851   -1.895  1.00 20.28  ? 148 ASP A OD2 1 
ATOM   1127 N N   . SER A 1 163 ? 9.854   1.103   1.086   1.00 9.48   ? 149 SER A N   1 
ATOM   1128 C CA  . SER A 1 163 ? 8.742   1.370   1.989   1.00 8.68   ? 149 SER A CA  1 
ATOM   1129 C C   . SER A 1 163 ? 9.252   1.858   3.336   1.00 8.00   ? 149 SER A C   1 
ATOM   1130 O O   . SER A 1 163 ? 10.295  1.406   3.829   1.00 8.52   ? 149 SER A O   1 
ATOM   1131 C CB  . SER A 1 163 ? 7.849   0.160   2.085   1.00 12.28  ? 149 SER A CB  1 
ATOM   1132 O OG  . SER A 1 163 ? 8.514   -0.976  2.596   1.00 14.88  ? 149 SER A OG  1 
ATOM   1133 N N   . LEU A 1 164 ? 8.512   2.781   3.935   1.00 7.69   ? 150 LEU A N   1 
ATOM   1134 C CA  . LEU A 1 164 ? 8.937   3.445   5.161   1.00 7.38   ? 150 LEU A CA  1 
ATOM   1135 C C   . LEU A 1 164 ? 7.780   3.499   6.154   1.00 8.40   ? 150 LEU A C   1 
ATOM   1136 O O   . LEU A 1 164 ? 6.645   3.817   5.766   1.00 10.85  ? 150 LEU A O   1 
ATOM   1137 C CB  . LEU A 1 164 ? 9.366   4.893   4.870   1.00 8.73   ? 150 LEU A CB  1 
ATOM   1138 C CG  . LEU A 1 164 ? 10.647  5.080   4.047   1.00 9.07   ? 150 LEU A CG  1 
ATOM   1139 C CD1 . LEU A 1 164 ? 10.827  6.515   3.656   1.00 9.46   ? 150 LEU A CD1 1 
ATOM   1140 C CD2 . LEU A 1 164 ? 11.892  4.593   4.796   1.00 9.74   ? 150 LEU A CD2 1 
ATOM   1141 N N   . GLY A 1 165 ? 8.049   3.205   7.427   1.00 8.01   ? 151 GLY A N   1 
ATOM   1142 C CA  . GLY A 1 165 ? 7.176   3.600   8.516   1.00 6.75   ? 151 GLY A CA  1 
ATOM   1143 C C   . GLY A 1 165 ? 7.492   5.042   8.909   1.00 7.88   ? 151 GLY A C   1 
ATOM   1144 O O   . GLY A 1 165 ? 8.564   5.592   8.620   1.00 8.41   ? 151 GLY A O   1 
ATOM   1145 N N   . VAL A 1 166 ? 6.523   5.653   9.618   1.00 8.61   ? 152 VAL A N   1 
ATOM   1146 C CA  . VAL A 1 166 ? 6.621   7.051   10.012  1.00 8.37   ? 152 VAL A CA  1 
ATOM   1147 C C   . VAL A 1 166 ? 6.554   7.112   11.530  1.00 8.86   ? 152 VAL A C   1 
ATOM   1148 O O   . VAL A 1 166 ? 5.720   6.457   12.183  1.00 9.53   ? 152 VAL A O   1 
ATOM   1149 C CB  . VAL A 1 166 ? 5.437   7.870   9.429   1.00 7.38   ? 152 VAL A CB  1 
ATOM   1150 C CG1 . VAL A 1 166 ? 5.548   9.322   9.860   1.00 10.93  ? 152 VAL A CG1 1 
ATOM   1151 C CG2 . VAL A 1 166 ? 5.358   7.780   7.909   1.00 9.95   ? 152 VAL A CG2 1 
ATOM   1152 N N   . CYS A 1 167 ? 7.447   7.943   12.089  1.00 9.07   ? 153 CYS A N   1 
ATOM   1153 C CA  . CYS A 1 167 ? 7.565   8.081   13.537  1.00 9.29   ? 153 CYS A CA  1 
ATOM   1154 C C   . CYS A 1 167 ? 7.482   9.566   13.884  1.00 10.17  ? 153 CYS A C   1 
ATOM   1155 O O   . CYS A 1 167 ? 8.395   10.333  13.564  1.00 11.12  ? 153 CYS A O   1 
ATOM   1156 C CB  . CYS A 1 167 ? 8.882   7.454   14.013  1.00 12.95  ? 153 CYS A CB  1 
ATOM   1157 S SG  . CYS A 1 167 ? 9.179   7.553   15.799  1.00 14.18  ? 153 CYS A SG  1 
ATOM   1158 N N   . ILE A 1 168 ? 6.339   9.997   14.461  1.00 9.49   ? 154 ILE A N   1 
ATOM   1159 C CA  . ILE A 1 168 ? 6.141   11.387  14.884  1.00 9.49   ? 154 ILE A CA  1 
ATOM   1160 C C   . ILE A 1 168 ? 6.588   11.475  16.344  1.00 9.96   ? 154 ILE A C   1 
ATOM   1161 O O   . ILE A 1 168 ? 6.000   10.859  17.218  1.00 12.11  ? 154 ILE A O   1 
ATOM   1162 C CB  . ILE A 1 168 ? 4.681   11.858  14.702  1.00 8.94   ? 154 ILE A CB  1 
ATOM   1163 C CG1 . ILE A 1 168 ? 4.274   11.716  13.227  1.00 10.44  ? 154 ILE A CG1 1 
ATOM   1164 C CG2 . ILE A 1 168 ? 4.503   13.308  15.195  1.00 12.13  ? 154 ILE A CG2 1 
ATOM   1165 C CD1 . ILE A 1 168 ? 2.780   11.938  12.994  1.00 12.15  ? 154 ILE A CD1 1 
ATOM   1166 N N   . HIS A 1 169 ? 7.623   12.284  16.589  1.00 10.61  ? 155 HIS A N   1 
ATOM   1167 C CA  . HIS A 1 169 ? 8.148   12.365  17.954  1.00 11.03  ? 155 HIS A CA  1 
ATOM   1168 C C   . HIS A 1 169 ? 7.382   13.427  18.742  1.00 11.89  ? 155 HIS A C   1 
ATOM   1169 O O   . HIS A 1 169 ? 7.310   14.578  18.281  1.00 15.62  ? 155 HIS A O   1 
ATOM   1170 C CB  . HIS A 1 169 ? 9.656   12.716  17.922  1.00 11.97  ? 155 HIS A CB  1 
ATOM   1171 C CG  . HIS A 1 169 ? 10.477  11.658  17.255  1.00 14.16  ? 155 HIS A CG  1 
ATOM   1172 N ND1 . HIS A 1 169 ? 11.094  10.627  17.926  1.00 16.52  ? 155 HIS A ND1 1 
ATOM   1173 C CD2 . HIS A 1 169 ? 10.675  11.454  15.906  1.00 13.06  ? 155 HIS A CD2 1 
ATOM   1174 C CE1 . HIS A 1 169 ? 11.716  9.828   17.043  1.00 15.65  ? 155 HIS A CE1 1 
ATOM   1175 N NE2 . HIS A 1 169 ? 11.459  10.335  15.763  1.00 13.60  ? 155 HIS A NE2 1 
ATOM   1176 N N   . THR A 1 170 ? 6.865   13.057  19.936  1.00 13.14  ? 156 THR A N   1 
ATOM   1177 C CA  . THR A 1 170 ? 6.154   14.028  20.771  1.00 13.40  ? 156 THR A CA  1 
ATOM   1178 C C   . THR A 1 170 ? 6.733   13.979  22.175  1.00 13.41  ? 156 THR A C   1 
ATOM   1179 O O   . THR A 1 170 ? 7.419   13.006  22.517  1.00 13.69  ? 156 THR A O   1 
ATOM   1180 C CB  . THR A 1 170 ? 4.632   13.830  20.821  1.00 13.44  ? 156 THR A CB  1 
ATOM   1181 O OG1 . THR A 1 170 ? 4.292   12.877  21.819  1.00 12.87  ? 156 THR A OG1 1 
ATOM   1182 C CG2 . THR A 1 170 ? 4.066   13.399  19.482  1.00 13.12  ? 156 THR A CG2 1 
ATOM   1183 N N   . SER A 1 171 ? 6.340   14.957  23.010  1.00 14.93  ? 157 SER A N   1 
ATOM   1184 C CA  . SER A 1 171 ? 6.824   14.946  24.390  1.00 15.84  ? 157 SER A CA  1 
ATOM   1185 C C   . SER A 1 171 ? 6.162   13.845  25.247  1.00 15.69  ? 157 SER A C   1 
ATOM   1186 O O   . SER A 1 171 ? 6.613   13.552  26.359  1.00 19.83  ? 157 SER A O   1 
ATOM   1187 C CB  . SER A 1 171 ? 6.796   16.332  24.968  1.00 18.26  ? 157 SER A CB  1 
ATOM   1188 O OG  . SER A 1 171 ? 5.489   16.830  24.903  1.00 20.18  ? 157 SER A OG  1 
ATOM   1189 N N   . TYR A 1 172 ? 5.141   13.147  24.709  1.00 14.59  ? 158 TYR A N   1 
ATOM   1190 C CA  . TYR A 1 172 ? 4.551   11.973  25.325  1.00 14.13  ? 158 TYR A CA  1 
ATOM   1191 C C   . TYR A 1 172 ? 5.184   10.659  24.853  1.00 12.93  ? 158 TYR A C   1 
ATOM   1192 O O   . TYR A 1 172 ? 4.842   9.606   25.383  1.00 16.77  ? 158 TYR A O   1 
ATOM   1193 C CB  . TYR A 1 172 ? 3.058   11.896  24.992  1.00 13.61  ? 158 TYR A CB  1 
ATOM   1194 C CG  . TYR A 1 172 ? 2.257   13.082  25.471  1.00 13.63  ? 158 TYR A CG  1 
ATOM   1195 C CD1 . TYR A 1 172 ? 2.217   13.424  26.826  1.00 14.76  ? 158 TYR A CD1 1 
ATOM   1196 C CD2 . TYR A 1 172 ? 1.479   13.845  24.594  1.00 14.09  ? 158 TYR A CD2 1 
ATOM   1197 C CE1 . TYR A 1 172 ? 1.433   14.481  27.273  1.00 14.14  ? 158 TYR A CE1 1 
ATOM   1198 C CE2 . TYR A 1 172 ? 0.670   14.879  25.048  1.00 14.93  ? 158 TYR A CE2 1 
ATOM   1199 C CZ  . TYR A 1 172 ? 0.644   15.195  26.397  1.00 15.67  ? 158 TYR A CZ  1 
ATOM   1200 O OH  . TYR A 1 172 ? -0.137  16.199  26.884  1.00 16.03  ? 158 TYR A OH  1 
ATOM   1201 N N   . GLY A 1 173 ? 6.084   10.737  23.852  1.00 13.59  ? 159 GLY A N   1 
ATOM   1202 C CA  . GLY A 1 173 ? 6.609   9.568   23.167  1.00 13.28  ? 159 GLY A CA  1 
ATOM   1203 C C   . GLY A 1 173 ? 6.132   9.555   21.714  1.00 12.26  ? 159 GLY A C   1 
ATOM   1204 O O   . GLY A 1 173 ? 5.358   10.422  21.285  1.00 13.74  ? 159 GLY A O   1 
ATOM   1205 N N   . SER A 1 174 ? 6.580   8.542   20.964  1.00 11.90  ? 160 SER A N   1 
ATOM   1206 C CA  . SER A 1 174 ? 6.402   8.536   19.518  1.00 10.14  ? 160 SER A CA  1 
ATOM   1207 C C   . SER A 1 174 ? 4.977   8.097   19.180  1.00 11.02  ? 160 SER A C   1 
ATOM   1208 O O   . SER A 1 174 ? 4.404   7.199   19.809  1.00 11.73  ? 160 SER A O   1 
ATOM   1209 C CB  . SER A 1 174 ? 7.388   7.602   18.880  1.00 14.29  ? 160 SER A CB  1 
ATOM   1210 O OG  . SER A 1 174 ? 8.670   8.200   18.976  1.00 23.30  ? 160 SER A OG  1 
ATOM   1211 N N   . ILE A 1 175 ? 4.490   8.635   18.048  1.00 10.27  ? 161 ILE A N   1 
ATOM   1212 C CA  . ILE A 1 175 ? 3.316   8.094   17.351  1.00 10.77  ? 161 ILE A CA  1 
ATOM   1213 C C   . ILE A 1 175 ? 3.851   7.419   16.106  1.00 8.39   ? 161 ILE A C   1 
ATOM   1214 O O   . ILE A 1 175 ? 4.411   8.087   15.219  1.00 10.18  ? 161 ILE A O   1 
ATOM   1215 C CB  . ILE A 1 175 ? 2.309   9.210   17.010  1.00 10.56  ? 161 ILE A CB  1 
ATOM   1216 C CG1 . ILE A 1 175 ? 1.865   9.951   18.279  1.00 12.33  ? 161 ILE A CG1 1 
ATOM   1217 C CG2 . ILE A 1 175 ? 1.109   8.637   16.197  1.00 11.43  ? 161 ILE A CG2 1 
ATOM   1218 C CD1 . ILE A 1 175 ? 1.164   11.286  18.018  1.00 15.07  ? 161 ILE A CD1 1 
ATOM   1219 N N   . VAL A 1 176 ? 3.762   6.092   16.072  1.00 8.92   ? 162 VAL A N   1 
ATOM   1220 C CA  . VAL A 1 176 ? 4.355   5.309   14.972  1.00 8.35   ? 162 VAL A CA  1 
ATOM   1221 C C   . VAL A 1 176 ? 3.252   4.758   14.089  1.00 8.60   ? 162 VAL A C   1 
ATOM   1222 O O   . VAL A 1 176 ? 2.318   4.152   14.585  1.00 10.07  ? 162 VAL A O   1 
ATOM   1223 C CB  . VAL A 1 176 ? 5.180   4.170   15.566  1.00 9.81   ? 162 VAL A CB  1 
ATOM   1224 C CG1 . VAL A 1 176 ? 5.680   3.216   14.481  1.00 9.93   ? 162 VAL A CG1 1 
ATOM   1225 C CG2 . VAL A 1 176 ? 6.334   4.722   16.396  1.00 10.71  ? 162 VAL A CG2 1 
ATOM   1226 N N   . TYR A 1 177 ? 3.366   5.009   12.779  1.00 8.04   ? 163 TYR A N   1 
ATOM   1227 C CA  . TYR A 1 177 ? 2.483   4.443   11.769  1.00 8.35   ? 163 TYR A CA  1 
ATOM   1228 C C   . TYR A 1 177 ? 3.327   3.493   10.910  1.00 8.13   ? 163 TYR A C   1 
ATOM   1229 O O   . TYR A 1 177 ? 4.320   3.882   10.323  1.00 9.23   ? 163 TYR A O   1 
ATOM   1230 C CB  . TYR A 1 177 ? 1.841   5.556   10.914  1.00 8.60   ? 163 TYR A CB  1 
ATOM   1231 C CG  . TYR A 1 177 ? 1.088   5.047   9.714   1.00 7.14   ? 163 TYR A CG  1 
ATOM   1232 C CD1 . TYR A 1 177 ? 0.139   4.032   9.807   1.00 6.94   ? 163 TYR A CD1 1 
ATOM   1233 C CD2 . TYR A 1 177 ? 1.349   5.608   8.475   1.00 8.06   ? 163 TYR A CD2 1 
ATOM   1234 C CE1 . TYR A 1 177 ? -0.552  3.611   8.685   1.00 8.42   ? 163 TYR A CE1 1 
ATOM   1235 C CE2 . TYR A 1 177 ? 0.632   5.219   7.348   1.00 8.12   ? 163 TYR A CE2 1 
ATOM   1236 C CZ  . TYR A 1 177 ? -0.315  4.206   7.446   1.00 8.17   ? 163 TYR A CZ  1 
ATOM   1237 O OH  . TYR A 1 177 ? -0.967  3.793   6.323   1.00 8.77   ? 163 TYR A OH  1 
ATOM   1238 N N   . THR A 1 178 ? 2.921   2.210   10.869  1.00 8.98   ? 164 THR A N   1 
ATOM   1239 C CA  . THR A 1 178 ? 3.697   1.191   10.200  1.00 9.24   ? 164 THR A CA  1 
ATOM   1240 C C   . THR A 1 178 ? 3.578   1.224   8.694   1.00 8.39   ? 164 THR A C   1 
ATOM   1241 O O   . THR A 1 178 ? 4.412   0.698   8.002   1.00 9.90   ? 164 THR A O   1 
ATOM   1242 C CB  . THR A 1 178 ? 3.294   -0.213  10.684  1.00 8.51   ? 164 THR A CB  1 
ATOM   1243 O OG1 . THR A 1 178 ? 1.903   -0.426  10.380  1.00 8.75   ? 164 THR A OG1 1 
ATOM   1244 C CG2 . THR A 1 178 ? 3.475   -0.344  12.191  1.00 11.13  ? 164 THR A CG2 1 
ATOM   1245 N N   . GLY A 1 179 ? 2.500   1.818   8.184   1.00 8.66   ? 165 GLY A N   1 
ATOM   1246 C CA  . GLY A 1 179 ? 2.045   1.484   6.840   1.00 7.94   ? 165 GLY A CA  1 
ATOM   1247 C C   . GLY A 1 179 ? 1.761   -0.022  6.717   1.00 8.22   ? 165 GLY A C   1 
ATOM   1248 O O   . GLY A 1 179 ? 1.561   -0.738  7.722   1.00 10.88  ? 165 GLY A O   1 
ATOM   1249 N N   . GLU A 1 180 ? 1.767   -0.489  5.475   1.00 9.06   ? 166 GLU A N   1 
ATOM   1250 C CA  . GLU A 1 180 ? 1.629   -1.904  5.220   1.00 10.31  ? 166 GLU A CA  1 
ATOM   1251 C C   . GLU A 1 180 ? 3.004   -2.549  5.335   1.00 8.26   ? 166 GLU A C   1 
ATOM   1252 O O   . GLU A 1 180 ? 3.966   -2.050  4.766   1.00 10.26  ? 166 GLU A O   1 
ATOM   1253 C CB  . GLU A 1 180 ? 0.856   -2.068  3.915   1.00 12.26  ? 166 GLU A CB  1 
ATOM   1254 C CG  . GLU A 1 180 ? -0.569  -1.477  4.047   1.00 16.83  ? 166 GLU A CG  1 
ATOM   1255 C CD  . GLU A 1 180 ? -1.541  -1.626  2.883   1.00 15.55  ? 166 GLU A CD  1 
ATOM   1256 O OE1 . GLU A 1 180 ? -1.072  -2.062  1.783   1.00 16.25  ? 166 GLU A OE1 1 
ATOM   1257 O OE2 . GLU A 1 180 ? -2.779  -1.293  3.069   1.00 19.83  ? 166 GLU A OE2 1 
ATOM   1258 N N   . PHE A 1 181 ? 3.070   -3.721  6.013   1.00 9.00   ? 167 PHE A N   1 
ATOM   1259 C CA  . PHE A 1 181 ? 4.374   -4.319  6.225   1.00 7.94   ? 167 PHE A CA  1 
ATOM   1260 C C   . PHE A 1 181 ? 4.195   -5.791  6.555   1.00 9.35   ? 167 PHE A C   1 
ATOM   1261 O O   . PHE A 1 181 ? 3.132   -6.205  7.006   1.00 9.75   ? 167 PHE A O   1 
ATOM   1262 C CB  . PHE A 1 181 ? 5.121   -3.670  7.399   1.00 10.96  ? 167 PHE A CB  1 
ATOM   1263 C CG  . PHE A 1 181 ? 4.559   -4.045  8.753   1.00 8.73   ? 167 PHE A CG  1 
ATOM   1264 C CD1 . PHE A 1 181 ? 3.475   -3.393  9.306   1.00 9.09   ? 167 PHE A CD1 1 
ATOM   1265 C CD2 . PHE A 1 181 ? 5.099   -5.120  9.450   1.00 9.04   ? 167 PHE A CD2 1 
ATOM   1266 C CE1 . PHE A 1 181 ? 2.935   -3.799  10.504  1.00 10.03  ? 167 PHE A CE1 1 
ATOM   1267 C CE2 . PHE A 1 181 ? 4.558   -5.549  10.651  1.00 9.22   ? 167 PHE A CE2 1 
ATOM   1268 C CZ  . PHE A 1 181 ? 3.488   -4.867  11.197  1.00 10.52  ? 167 PHE A CZ  1 
ATOM   1269 N N   . LYS A 1 182 ? 5.288   -6.529  6.370   1.00 9.86   ? 168 LYS A N   1 
ATOM   1270 C CA  . LYS A 1 182 ? 5.427   -7.910  6.832   1.00 9.75   ? 168 LYS A CA  1 
ATOM   1271 C C   . LYS A 1 182 ? 6.887   -8.089  7.263   1.00 11.49  ? 168 LYS A C   1 
ATOM   1272 O O   . LYS A 1 182 ? 7.694   -7.169  7.209   1.00 13.16  ? 168 LYS A O   1 
ATOM   1273 C CB  . LYS A 1 182 ? 4.965   -8.879  5.733   1.00 12.77  ? 168 LYS A CB  1 
ATOM   1274 C CG  . LYS A 1 182 ? 5.828   -8.925  4.481   1.00 12.36  ? 168 LYS A CG  1 
ATOM   1275 C CD  . LYS A 1 182 ? 5.399   -10.107 3.608   1.00 13.11  ? 168 LYS A CD  1 
ATOM   1276 C CE  . LYS A 1 182 ? 5.974   -10.138 2.203   1.00 17.09  ? 168 LYS A CE  1 
ATOM   1277 N NZ  . LYS A 1 182 ? 5.424   -11.282 1.439   1.00 16.57  ? 168 LYS A NZ  1 
ATOM   1278 N N   . PHE A 1 183 ? 7.212   -9.272  7.800   1.00 11.34  ? 169 PHE A N   1 
ATOM   1279 C CA  . PHE A 1 183 ? 8.613   -9.617  8.035   1.00 12.31  ? 169 PHE A CA  1 
ATOM   1280 C C   . PHE A 1 183 ? 8.924   -10.912 7.297   1.00 17.36  ? 169 PHE A C   1 
ATOM   1281 O O   . PHE A 1 183 ? 8.293   -11.937 7.552   1.00 21.81  ? 169 PHE A O   1 
ATOM   1282 C CB  . PHE A 1 183 ? 8.912   -9.790  9.538   1.00 13.46  ? 169 PHE A CB  1 
ATOM   1283 C CG  . PHE A 1 183 ? 8.880   -8.494  10.310  1.00 10.11  ? 169 PHE A CG  1 
ATOM   1284 C CD1 . PHE A 1 183 ? 9.815   -7.485  10.114  1.00 12.52  ? 169 PHE A CD1 1 
ATOM   1285 C CD2 . PHE A 1 183 ? 7.851   -8.261  11.218  1.00 11.39  ? 169 PHE A CD2 1 
ATOM   1286 C CE1 . PHE A 1 183 ? 9.739   -6.283  10.829  1.00 13.16  ? 169 PHE A CE1 1 
ATOM   1287 C CE2 . PHE A 1 183 ? 7.797   -7.095  11.962  1.00 11.59  ? 169 PHE A CE2 1 
ATOM   1288 C CZ  . PHE A 1 183 ? 8.713   -6.080  11.738  1.00 11.71  ? 169 PHE A CZ  1 
ATOM   1289 N N   . ASP A 1 184 ? 9.958   -10.847 6.447   1.00 13.47  ? 170 ASP A N   1 
ATOM   1290 C CA  . ASP A 1 184 ? 10.349  -11.992 5.632   1.00 12.85  ? 170 ASP A CA  1 
ATOM   1291 C C   . ASP A 1 184 ? 11.871  -11.923 5.476   1.00 14.90  ? 170 ASP A C   1 
ATOM   1292 O O   . ASP A 1 184 ? 12.382  -11.078 4.750   1.00 18.00  ? 170 ASP A O   1 
ATOM   1293 C CB  . ASP A 1 184 ? 9.640   -11.893 4.278   1.00 15.94  ? 170 ASP A CB  1 
ATOM   1294 C CG  . ASP A 1 184 ? 9.952   -13.042 3.327   1.00 19.27  ? 170 ASP A CG  1 
ATOM   1295 O OD1 . ASP A 1 184 ? 10.962  -13.779 3.586   1.00 20.23  ? 170 ASP A OD1 1 
ATOM   1296 O OD2 . ASP A 1 184 ? 9.199   -13.211 2.349   1.00 15.50  ? 170 ASP A OD2 1 
ATOM   1297 N N   . GLN A 1 185 ? 12.590  -12.871 6.100   1.00 16.65  ? 171 GLN A N   1 
ATOM   1298 C CA  . GLN A 1 185 ? 14.054  -12.877 6.074   1.00 17.98  ? 171 GLN A CA  1 
ATOM   1299 C C   . GLN A 1 185 ? 14.619  -13.159 4.677   1.00 18.77  ? 171 GLN A C   1 
ATOM   1300 O O   . GLN A 1 185 ? 15.822  -12.989 4.443   1.00 24.75  ? 171 GLN A O   1 
ATOM   1301 C CB  . GLN A 1 185 ? 14.621  -13.790 7.176   1.00 23.33  ? 171 GLN A CB  1 
ATOM   1302 C CG  . GLN A 1 185 ? 14.426  -13.249 8.605   1.00 31.75  ? 171 GLN A CG  1 
ATOM   1303 C CD  . GLN A 1 185 ? 14.986  -14.089 9.743   1.00 31.18  ? 171 GLN A CD  1 
ATOM   1304 O OE1 . GLN A 1 185 ? 16.207  -14.248 9.892   1.00 27.59  ? 171 GLN A OE1 1 
ATOM   1305 N NE2 . GLN A 1 185 ? 14.094  -14.600 10.594  1.00 31.20  ? 171 GLN A NE2 1 
ATOM   1306 N N   . SER A 1 186 ? 13.786  -13.582 3.725   1.00 17.52  ? 172 SER A N   1 
ATOM   1307 C CA  . SER A 1 186 ? 14.270  -13.863 2.381   1.00 17.66  ? 172 SER A CA  1 
ATOM   1308 C C   . SER A 1 186 ? 14.277  -12.619 1.480   1.00 19.47  ? 172 SER A C   1 
ATOM   1309 O O   . SER A 1 186 ? 14.835  -12.688 0.381   1.00 24.64  ? 172 SER A O   1 
ATOM   1310 C CB  . SER A 1 186 ? 13.505  -15.017 1.749   1.00 19.55  ? 172 SER A CB  1 
ATOM   1311 O OG  . SER A 1 186 ? 12.239  -14.562 1.279   1.00 20.14  ? 172 SER A OG  1 
ATOM   1312 N N   . LEU A 1 187 ? 13.659  -11.500 1.926   1.00 18.65  ? 173 LEU A N   1 
ATOM   1313 C CA  . LEU A 1 187 ? 13.710  -10.231 1.190   1.00 19.13  ? 173 LEU A CA  1 
ATOM   1314 C C   . LEU A 1 187 ? 14.842  -9.352  1.741   1.00 19.97  ? 173 LEU A C   1 
ATOM   1315 O O   . LEU A 1 187 ? 14.943  -9.150  2.945   1.00 26.46  ? 173 LEU A O   1 
ATOM   1316 C CB  . LEU A 1 187 ? 12.346  -9.525  1.293   1.00 17.90  ? 173 LEU A CB  1 
ATOM   1317 C CG  . LEU A 1 187 ? 11.187  -10.243 0.592   1.00 16.68  ? 173 LEU A CG  1 
ATOM   1318 C CD1 . LEU A 1 187 ? 9.840   -9.553  0.860   1.00 17.29  ? 173 LEU A CD1 1 
ATOM   1319 C CD2 . LEU A 1 187 ? 11.448  -10.350 -0.906  1.00 20.43  ? 173 LEU A CD2 1 
ATOM   1320 N N   . HIS A 1 188 ? 15.666  -8.780  0.849   1.00 19.21  ? 174 HIS A N   1 
ATOM   1321 C CA  . HIS A 1 188 ? 16.872  -8.059  1.253   1.00 17.94  ? 174 HIS A CA  1 
ATOM   1322 C C   . HIS A 1 188 ? 16.940  -6.743  0.483   1.00 16.79  ? 174 HIS A C   1 
ATOM   1323 O O   . HIS A 1 188 ? 15.988  -6.379  -0.213  1.00 18.45  ? 174 HIS A O   1 
ATOM   1324 C CB  . HIS A 1 188 ? 18.136  -8.866  0.921   1.00 29.63  ? 174 HIS A CB  1 
ATOM   1325 C CG  . HIS A 1 188 ? 18.137  -10.299 1.369   1.00 39.66  ? 174 HIS A CG  1 
ATOM   1326 N ND1 . HIS A 1 188 ? 18.065  -10.696 2.686   1.00 48.06  ? 174 HIS A ND1 1 
ATOM   1327 C CD2 . HIS A 1 188 ? 18.243  -11.438 0.628   1.00 46.49  ? 174 HIS A CD2 1 
ATOM   1328 C CE1 . HIS A 1 188 ? 18.116  -12.028 2.748   1.00 34.34  ? 174 HIS A CE1 1 
ATOM   1329 N NE2 . HIS A 1 188 ? 18.221  -12.503 1.491   1.00 41.31  ? 174 HIS A NE2 1 
ATOM   1330 N N   . GLY A 1 189 ? 18.049  -5.997  0.615   1.00 21.12  ? 175 GLY A N   1 
ATOM   1331 C CA  . GLY A 1 189 ? 18.270  -4.813  -0.194  1.00 23.91  ? 175 GLY A CA  1 
ATOM   1332 C C   . GLY A 1 189 ? 17.211  -3.764  0.122   1.00 20.43  ? 175 GLY A C   1 
ATOM   1333 O O   . GLY A 1 189 ? 17.037  -3.380  1.278   1.00 20.32  ? 175 GLY A O   1 
ATOM   1334 N N   . HIS A 1 190 ? 16.508  -3.310  -0.920  1.00 16.49  ? 176 HIS A N   1 
ATOM   1335 C CA  . HIS A 1 190 ? 15.529  -2.255  -0.772  1.00 15.08  ? 176 HIS A CA  1 
ATOM   1336 C C   . HIS A 1 190 ? 14.221  -2.762  -0.129  1.00 13.54  ? 176 HIS A C   1 
ATOM   1337 O O   . HIS A 1 190 ? 13.287  -1.958  0.008   1.00 15.90  ? 176 HIS A O   1 
ATOM   1338 C CB  . HIS A 1 190 ? 15.315  -1.560  -2.118  1.00 18.01  ? 176 HIS A CB  1 
ATOM   1339 C CG  . HIS A 1 190 ? 16.464  -0.723  -2.584  1.00 24.19  ? 176 HIS A CG  1 
ATOM   1340 N ND1 . HIS A 1 190 ? 16.405  0.645   -2.610  1.00 30.21  ? 176 HIS A ND1 1 
ATOM   1341 C CD2 . HIS A 1 190 ? 17.695  -1.080  -3.044  1.00 29.82  ? 176 HIS A CD2 1 
ATOM   1342 C CE1 . HIS A 1 190 ? 17.548  1.134   -3.081  1.00 32.92  ? 176 HIS A CE1 1 
ATOM   1343 N NE2 . HIS A 1 190 ? 18.361  0.076   -3.357  1.00 30.64  ? 176 HIS A NE2 1 
ATOM   1344 N N   . TYR A 1 191 ? 14.167  -4.058  0.219   1.00 14.05  ? 177 TYR A N   1 
ATOM   1345 C CA  . TYR A 1 191 ? 13.025  -4.634  0.933   1.00 15.73  ? 177 TYR A CA  1 
ATOM   1346 C C   . TYR A 1 191 ? 13.358  -4.910  2.401   1.00 14.62  ? 177 TYR A C   1 
ATOM   1347 O O   . TYR A 1 191 ? 12.501  -5.382  3.153   1.00 14.83  ? 177 TYR A O   1 
ATOM   1348 C CB  . TYR A 1 191 ? 12.567  -5.964  0.308   1.00 15.28  ? 177 TYR A CB  1 
ATOM   1349 C CG  . TYR A 1 191 ? 12.115  -5.829  -1.108  1.00 13.32  ? 177 TYR A CG  1 
ATOM   1350 C CD1 . TYR A 1 191 ? 10.813  -5.477  -1.404  1.00 14.38  ? 177 TYR A CD1 1 
ATOM   1351 C CD2 . TYR A 1 191 ? 12.993  -6.052  -2.157  1.00 17.41  ? 177 TYR A CD2 1 
ATOM   1352 C CE1 . TYR A 1 191 ? 10.404  -5.315  -2.720  1.00 16.33  ? 177 TYR A CE1 1 
ATOM   1353 C CE2 . TYR A 1 191 ? 12.562  -5.949  -3.466  1.00 18.79  ? 177 TYR A CE2 1 
ATOM   1354 C CZ  . TYR A 1 191 ? 11.280  -5.552  -3.760  1.00 22.65  ? 177 TYR A CZ  1 
ATOM   1355 O OH  . TYR A 1 191 ? 10.900  -5.476  -5.075  1.00 24.65  ? 177 TYR A OH  1 
ATOM   1356 N N   . ALA A 1 192 ? 14.624  -4.680  2.802   1.00 16.03  ? 178 ALA A N   1 
ATOM   1357 C CA  . ALA A 1 192 ? 15.065  -5.072  4.133   1.00 14.94  ? 178 ALA A CA  1 
ATOM   1358 C C   . ALA A 1 192 ? 14.477  -4.149  5.197   1.00 13.67  ? 178 ALA A C   1 
ATOM   1359 O O   . ALA A 1 192 ? 14.412  -2.929  5.023   1.00 17.63  ? 178 ALA A O   1 
ATOM   1360 C CB  . ALA A 1 192 ? 16.575  -5.043  4.230   1.00 17.62  ? 178 ALA A CB  1 
ATOM   1361 N N   . PRO A 1 193 ? 14.066  -4.716  6.361   1.00 16.06  ? 179 PRO A N   1 
ATOM   1362 C CA  . PRO A 1 193 ? 13.487  -3.906  7.441   1.00 15.26  ? 179 PRO A CA  1 
ATOM   1363 C C   . PRO A 1 193 ? 14.568  -3.360  8.349   1.00 17.50  ? 179 PRO A C   1 
ATOM   1364 O O   . PRO A 1 193 ? 15.648  -3.952  8.465   1.00 22.98  ? 179 PRO A O   1 
ATOM   1365 C CB  . PRO A 1 193 ? 12.644  -4.925  8.207   1.00 17.31  ? 179 PRO A CB  1 
ATOM   1366 C CG  . PRO A 1 193 ? 13.466  -6.230  8.072   1.00 18.47  ? 179 PRO A CG  1 
ATOM   1367 C CD  . PRO A 1 193 ? 14.042  -6.161  6.665   1.00 14.14  ? 179 PRO A CD  1 
ATOM   1368 N N   . ASP A 1 194 ? 14.256  -2.225  8.969   1.00 14.90  ? 180 ASP A N   1 
ATOM   1369 C CA  . ASP A 1 194 ? 15.158  -1.613  9.937   1.00 15.56  ? 180 ASP A CA  1 
ATOM   1370 C C   . ASP A 1 194 ? 14.903  -2.135  11.351  1.00 14.91  ? 180 ASP A C   1 
ATOM   1371 O O   . ASP A 1 194 ? 14.436  -1.376  12.169  1.00 14.14  ? 180 ASP A O   1 
ATOM   1372 C CB  . ASP A 1 194 ? 15.037  -0.093  9.903   1.00 17.61  ? 180 ASP A CB  1 
ATOM   1373 C CG  . ASP A 1 194 ? 15.855  0.540   8.811   1.00 18.88  ? 180 ASP A CG  1 
ATOM   1374 O OD1 . ASP A 1 194 ? 16.822  -0.099  8.325   1.00 26.90  ? 180 ASP A OD1 1 
ATOM   1375 O OD2 . ASP A 1 194 ? 15.562  1.686   8.497   1.00 15.42  ? 180 ASP A OD2 1 
ATOM   1376 N N   . LEU A 1 195 ? 15.266  -3.381  11.652  1.00 15.15  ? 181 LEU A N   1 
ATOM   1377 C CA  . LEU A 1 195 ? 14.940  -3.966  12.952  1.00 15.52  ? 181 LEU A CA  1 
ATOM   1378 C C   . LEU A 1 195 ? 15.644  -3.243  14.100  1.00 15.72  ? 181 LEU A C   1 
ATOM   1379 O O   . LEU A 1 195 ? 15.058  -3.102  15.169  1.00 16.88  ? 181 LEU A O   1 
ATOM   1380 C CB  . LEU A 1 195 ? 15.310  -5.451  12.958  1.00 15.24  ? 181 LEU A CB  1 
ATOM   1381 C CG  . LEU A 1 195 ? 14.518  -6.335  12.000  1.00 20.46  ? 181 LEU A CG  1 
ATOM   1382 C CD1 . LEU A 1 195 ? 14.977  -7.785  12.076  1.00 28.15  ? 181 LEU A CD1 1 
ATOM   1383 C CD2 . LEU A 1 195 ? 13.040  -6.194  12.311  1.00 24.49  ? 181 LEU A CD2 1 
ATOM   1384 N N   . LYS A 1 196 ? 16.918  -2.852  13.911  1.00 16.00  ? 182 LYS A N   1 
ATOM   1385 C CA  . LYS A 1 196 ? 17.656  -2.151  14.968  1.00 19.59  ? 182 LYS A CA  1 
ATOM   1386 C C   . LYS A 1 196 ? 17.040  -0.773  15.206  1.00 16.25  ? 182 LYS A C   1 
ATOM   1387 O O   . LYS A 1 196 ? 16.837  -0.340  16.349  1.00 17.20  ? 182 LYS A O   1 
ATOM   1388 C CB  . LYS A 1 196 ? 19.160  -2.065  14.661  1.00 21.06  ? 182 LYS A CB  1 
ATOM   1389 N N   . ARG A 1 197 ? 16.718  -0.062  14.133  1.00 16.06  ? 183 ARG A N   1 
ATOM   1390 C CA  . ARG A 1 197 ? 16.106  1.280   14.287  1.00 16.26  ? 183 ARG A CA  1 
ATOM   1391 C C   . ARG A 1 197 ? 14.724  1.134   14.942  1.00 14.53  ? 183 ARG A C   1 
ATOM   1392 O O   . ARG A 1 197 ? 14.395  1.953   15.793  1.00 16.69  ? 183 ARG A O   1 
ATOM   1393 C CB  . ARG A 1 197 ? 16.009  2.026   12.951  1.00 18.09  ? 183 ARG A CB  1 
ATOM   1394 C CG  . ARG A 1 197 ? 17.310  2.068   12.167  1.00 25.59  ? 183 ARG A CG  1 
ATOM   1395 C CD  . ARG A 1 197 ? 18.033  3.379   12.323  1.00 38.34  ? 183 ARG A CD  1 
ATOM   1396 N NE  . ARG A 1 197 ? 19.122  3.454   11.360  1.00 38.63  ? 183 ARG A NE  1 
ATOM   1397 C CZ  . ARG A 1 197 ? 19.209  4.362   10.400  1.00 33.06  ? 183 ARG A CZ  1 
ATOM   1398 N NH1 . ARG A 1 197 ? 18.273  5.285   10.283  1.00 25.52  ? 183 ARG A NH1 1 
ATOM   1399 N NH2 . ARG A 1 197 ? 20.244  4.358   9.579   1.00 29.19  ? 183 ARG A NH2 1 
ATOM   1400 N N   . MET A 1 198 ? 14.005  0.075   14.591  1.00 14.74  ? 184 MET A N   1 
ATOM   1401 C CA  . MET A 1 198 ? 12.695  -0.110  15.211  1.00 12.96  ? 184 MET A CA  1 
ATOM   1402 C C   . MET A 1 198 ? 12.848  -0.396  16.717  1.00 12.68  ? 184 MET A C   1 
ATOM   1403 O O   . MET A 1 198 ? 12.074  0.142   17.524  1.00 13.86  ? 184 MET A O   1 
ATOM   1404 C CB  . MET A 1 198 ? 11.891  -1.239  14.550  1.00 13.64  ? 184 MET A CB  1 
ATOM   1405 C CG  . MET A 1 198 ? 11.411  -0.915  13.144  1.00 14.83  ? 184 MET A CG  1 
ATOM   1406 S SD  . MET A 1 198 ? 10.500  -2.375  12.535  1.00 24.86  ? 184 MET A SD  1 
ATOM   1407 C CE  . MET A 1 198 ? 10.806  -2.304  10.770  1.00 27.22  ? 184 MET A CE  1 
ATOM   1408 N N   . ALA A 1 199 ? 13.880  -1.176  17.094  1.00 14.80  ? 185 ALA A N   1 
ATOM   1409 C CA  . ALA A 1 199 ? 14.107  -1.449  18.508  1.00 16.05  ? 185 ALA A CA  1 
ATOM   1410 C C   . ALA A 1 199 ? 14.444  -0.187  19.293  1.00 15.52  ? 185 ALA A C   1 
ATOM   1411 O O   . ALA A 1 199 ? 14.015  -0.032  20.443  1.00 17.12  ? 185 ALA A O   1 
ATOM   1412 C CB  . ALA A 1 199 ? 15.208  -2.455  18.662  1.00 16.40  ? 185 ALA A CB  1 
ATOM   1413 N N   . GLU A 1 200 ? 15.198  0.712   18.659  1.00 14.92  ? 186 GLU A N   1 
ATOM   1414 C CA  . GLU A 1 200 ? 15.564  1.990   19.245  1.00 16.59  ? 186 GLU A CA  1 
ATOM   1415 C C   . GLU A 1 200 ? 14.319  2.833   19.473  1.00 14.26  ? 186 GLU A C   1 
ATOM   1416 O O   . GLU A 1 200 ? 14.158  3.483   20.500  1.00 16.40  ? 186 GLU A O   1 
ATOM   1417 C CB  . GLU A 1 200 ? 16.566  2.707   18.332  1.00 18.17  ? 186 GLU A CB  1 
ATOM   1418 C CG  . GLU A 1 200 ? 17.932  2.070   18.407  1.00 24.19  ? 186 GLU A CG  1 
ATOM   1419 C CD  . GLU A 1 200 ? 18.913  2.511   17.330  1.00 30.08  ? 186 GLU A CD  1 
ATOM   1420 O OE1 . GLU A 1 200 ? 18.521  3.324   16.447  1.00 31.71  ? 186 GLU A OE1 1 
ATOM   1421 O OE2 . GLU A 1 200 ? 20.074  2.057   17.383  1.00 40.51  ? 186 GLU A OE2 1 
ATOM   1422 N N   . ILE A 1 201 ? 13.427  2.877   18.466  1.00 13.66  ? 187 ILE A N   1 
ATOM   1423 C CA  . ILE A 1 201 ? 12.155  3.586   18.605  1.00 12.84  ? 187 ILE A CA  1 
ATOM   1424 C C   . ILE A 1 201 ? 11.331  3.054   19.792  1.00 12.02  ? 187 ILE A C   1 
ATOM   1425 O O   . ILE A 1 201 ? 10.862  3.835   20.633  1.00 15.31  ? 187 ILE A O   1 
ATOM   1426 C CB  . ILE A 1 201 ? 11.345  3.514   17.294  1.00 12.30  ? 187 ILE A CB  1 
ATOM   1427 C CG1 . ILE A 1 201 ? 12.049  4.325   16.208  1.00 14.19  ? 187 ILE A CG1 1 
ATOM   1428 C CG2 . ILE A 1 201 ? 9.922   4.048   17.513  1.00 12.84  ? 187 ILE A CG2 1 
ATOM   1429 C CD1 . ILE A 1 201 ? 11.502  4.014   14.799  1.00 16.20  ? 187 ILE A CD1 1 
ATOM   1430 N N   . GLY A 1 202 ? 11.220  1.725   19.903  1.00 15.54  ? 188 GLY A N   1 
ATOM   1431 C CA  . GLY A 1 202 ? 10.488  1.089   20.975  1.00 14.20  ? 188 GLY A CA  1 
ATOM   1432 C C   . GLY A 1 202 ? 11.134  1.388   22.337  1.00 14.08  ? 188 GLY A C   1 
ATOM   1433 O O   . GLY A 1 202 ? 10.418  1.665   23.307  1.00 17.71  ? 188 GLY A O   1 
ATOM   1434 N N   . ASP A 1 203 ? 12.482  1.383   22.423  1.00 16.22  ? 189 ASP A N   1 
ATOM   1435 C CA  . ASP A 1 203 ? 13.174  1.614   23.694  1.00 18.48  ? 189 ASP A CA  1 
ATOM   1436 C C   . ASP A 1 203 ? 13.032  3.067   24.146  1.00 18.67  ? 189 ASP A C   1 
ATOM   1437 O O   . ASP A 1 203 ? 12.970  3.340   25.351  1.00 21.42  ? 189 ASP A O   1 
ATOM   1438 C CB  . ASP A 1 203 ? 14.666  1.281   23.557  1.00 19.22  ? 189 ASP A CB  1 
ATOM   1439 C CG  . ASP A 1 203 ? 14.950  -0.218  23.441  1.00 19.51  ? 189 ASP A CG  1 
ATOM   1440 O OD1 . ASP A 1 203 ? 14.032  -1.022  23.660  1.00 26.09  ? 189 ASP A OD1 1 
ATOM   1441 O OD2 . ASP A 1 203 ? 16.102  -0.582  23.096  1.00 28.64  ? 189 ASP A OD2 1 
ATOM   1442 N N   . GLU A 1 204 ? 13.031  4.007   23.187  1.00 18.35  ? 190 GLU A N   1 
ATOM   1443 C CA  . GLU A 1 204 ? 12.906  5.430   23.507  1.00 17.13  ? 190 GLU A CA  1 
ATOM   1444 C C   . GLU A 1 204 ? 11.504  5.742   24.024  1.00 17.44  ? 190 GLU A C   1 
ATOM   1445 O O   . GLU A 1 204 ? 11.333  6.617   24.864  1.00 21.01  ? 190 GLU A O   1 
ATOM   1446 C CB  . GLU A 1 204 ? 13.308  6.326   22.331  1.00 19.85  ? 190 GLU A CB  1 
ATOM   1447 C CG  . GLU A 1 204 ? 14.821  6.301   22.160  1.00 23.92  ? 190 GLU A CG  1 
ATOM   1448 C CD  . GLU A 1 204 ? 15.395  6.886   20.883  1.00 30.47  ? 190 GLU A CD  1 
ATOM   1449 O OE1 . GLU A 1 204 ? 14.603  7.357   20.060  1.00 44.23  ? 190 GLU A OE1 1 
ATOM   1450 O OE2 . GLU A 1 204 ? 16.635  6.847   20.707  1.00 38.21  ? 190 GLU A OE2 1 
ATOM   1451 N N   . GLY A 1 205 ? 10.498  4.987   23.576  1.00 14.92  ? 191 GLY A N   1 
ATOM   1452 C CA  . GLY A 1 205 ? 9.171   5.084   24.139  1.00 15.46  ? 191 GLY A CA  1 
ATOM   1453 C C   . GLY A 1 205 ? 8.143   5.456   23.058  1.00 13.17  ? 191 GLY A C   1 
ATOM   1454 O O   . GLY A 1 205 ? 8.169   6.541   22.499  1.00 13.67  ? 191 GLY A O   1 
ATOM   1455 N N   . VAL A 1 206 ? 7.252   4.507   22.779  1.00 12.83  ? 192 VAL A N   1 
ATOM   1456 C CA  . VAL A 1 206 ? 6.169   4.685   21.819  1.00 10.75  ? 192 VAL A CA  1 
ATOM   1457 C C   . VAL A 1 206 ? 4.869   4.956   22.591  1.00 12.57  ? 192 VAL A C   1 
ATOM   1458 O O   . VAL A 1 206 ? 4.382   4.138   23.369  1.00 14.18  ? 192 VAL A O   1 
ATOM   1459 C CB  . VAL A 1 206 ? 6.066   3.438   20.908  1.00 12.79  ? 192 VAL A CB  1 
ATOM   1460 C CG1 . VAL A 1 206 ? 4.871   3.572   19.976  1.00 11.51  ? 192 VAL A CG1 1 
ATOM   1461 C CG2 . VAL A 1 206 ? 7.343   3.286   20.085  1.00 12.13  ? 192 VAL A CG2 1 
ATOM   1462 N N   . PHE A 1 207 ? 4.332   6.169   22.396  1.00 11.41  ? 193 PHE A N   1 
ATOM   1463 C CA  . PHE A 1 207 ? 3.036   6.564   22.926  1.00 10.71  ? 193 PHE A CA  1 
ATOM   1464 C C   . PHE A 1 207 ? 1.884   5.835   22.238  1.00 11.60  ? 193 PHE A C   1 
ATOM   1465 O O   . PHE A 1 207 ? 0.995   5.321   22.923  1.00 11.93  ? 193 PHE A O   1 
ATOM   1466 C CB  . PHE A 1 207 ? 2.909   8.078   22.831  1.00 14.29  ? 193 PHE A CB  1 
ATOM   1467 C CG  . PHE A 1 207 ? 1.547   8.586   23.186  1.00 14.10  ? 193 PHE A CG  1 
ATOM   1468 C CD1 . PHE A 1 207 ? 1.163   8.588   24.522  1.00 17.89  ? 193 PHE A CD1 1 
ATOM   1469 C CD2 . PHE A 1 207 ? 0.646   9.023   22.207  1.00 20.46  ? 193 PHE A CD2 1 
ATOM   1470 C CE1 . PHE A 1 207 ? -0.088  9.070   24.890  1.00 21.92  ? 193 PHE A CE1 1 
ATOM   1471 C CE2 . PHE A 1 207 ? -0.620  9.476   22.571  1.00 22.94  ? 193 PHE A CE2 1 
ATOM   1472 C CZ  . PHE A 1 207 ? -0.973  9.500   23.912  1.00 24.35  ? 193 PHE A CZ  1 
ATOM   1473 N N   . ALA A 1 208 ? 1.876   5.767   20.883  1.00 10.61  ? 194 ALA A N   1 
ATOM   1474 C CA  . ALA A 1 208 ? 0.780   5.104   20.186  1.00 11.96  ? 194 ALA A CA  1 
ATOM   1475 C C   . ALA A 1 208 ? 1.359   4.447   18.945  1.00 9.89   ? 194 ALA A C   1 
ATOM   1476 O O   . ALA A 1 208 ? 2.184   5.058   18.250  1.00 11.22  ? 194 ALA A O   1 
ATOM   1477 C CB  . ALA A 1 208 ? -0.326  6.096   19.773  1.00 11.62  ? 194 ALA A CB  1 
ATOM   1478 N N   . LEU A 1 209 ? 0.934   3.200   18.714  1.00 9.69   ? 195 LEU A N   1 
ATOM   1479 C CA  . LEU A 1 209 ? 1.244   2.485   17.482  1.00 10.14  ? 195 LEU A CA  1 
ATOM   1480 C C   . LEU A 1 209 ? -0.035  2.286   16.664  1.00 7.72   ? 195 LEU A C   1 
ATOM   1481 O O   . LEU A 1 209 ? -1.081  1.873   17.197  1.00 9.81   ? 195 LEU A O   1 
ATOM   1482 C CB  . LEU A 1 209 ? 1.797   1.107   17.865  1.00 10.59  ? 195 LEU A CB  1 
ATOM   1483 C CG  . LEU A 1 209 ? 2.113   0.177   16.685  1.00 9.98   ? 195 LEU A CG  1 
ATOM   1484 C CD1 . LEU A 1 209 ? 3.259   0.691   15.809  1.00 12.19  ? 195 LEU A CD1 1 
ATOM   1485 C CD2 . LEU A 1 209 ? 2.453   -1.243  17.187  1.00 11.53  ? 195 LEU A CD2 1 
ATOM   1486 N N   . ILE A 1 210 ? 0.067   2.614   15.349  1.00 7.24   ? 196 ILE A N   1 
ATOM   1487 C CA  . ILE A 1 210 ? -1.004  2.527   14.363  1.00 7.33   ? 196 ILE A CA  1 
ATOM   1488 C C   . ILE A 1 210 ? -0.508  1.479   13.338  1.00 7.54   ? 196 ILE A C   1 
ATOM   1489 O O   . ILE A 1 210 ? 0.497   1.731   12.655  1.00 8.30   ? 196 ILE A O   1 
ATOM   1490 C CB  . ILE A 1 210 ? -1.236  3.907   13.699  1.00 8.47   ? 196 ILE A CB  1 
ATOM   1491 C CG1 . ILE A 1 210 ? -1.520  4.976   14.767  1.00 8.78   ? 196 ILE A CG1 1 
ATOM   1492 C CG2 . ILE A 1 210 ? -2.334  3.774   12.672  1.00 10.84  ? 196 ILE A CG2 1 
ATOM   1493 C CD1 . ILE A 1 210 ? -1.444  6.398   14.225  1.00 9.89   ? 196 ILE A CD1 1 
ATOM   1494 N N   . SER A 1 211 ? -1.119  0.267   13.326  1.00 7.67   ? 197 SER A N   1 
ATOM   1495 C CA  . SER A 1 211 ? -0.511  -0.860  12.625  1.00 8.23   ? 197 SER A CA  1 
ATOM   1496 C C   . SER A 1 211 ? -1.510  -1.612  11.744  1.00 8.85   ? 197 SER A C   1 
ATOM   1497 O O   . SER A 1 211 ? -2.698  -1.668  12.025  1.00 8.77   ? 197 SER A O   1 
ATOM   1498 C CB  . SER A 1 211 ? 0.128   -1.777  13.667  1.00 10.17  ? 197 SER A CB  1 
ATOM   1499 O OG  . SER A 1 211 ? 0.816   -2.838  12.973  1.00 10.67  ? 197 SER A OG  1 
ATOM   1500 N N   . ASP A 1 212 ? -0.997  -2.209  10.663  1.00 9.10   ? 198 ASP A N   1 
ATOM   1501 C CA  . ASP A 1 212 ? -1.704  -2.925  9.609   1.00 10.27  ? 198 ASP A CA  1 
ATOM   1502 C C   . ASP A 1 212 ? -2.347  -4.237  10.076  1.00 8.93   ? 198 ASP A C   1 
ATOM   1503 O O   . ASP A 1 212 ? -1.665  -5.162  10.475  1.00 10.16  ? 198 ASP A O   1 
ATOM   1504 C CB  . ASP A 1 212 ? -0.668  -3.267  8.537   1.00 9.74   ? 198 ASP A CB  1 
ATOM   1505 C CG  . ASP A 1 212 ? -1.199  -3.965  7.282   1.00 9.71   ? 198 ASP A CG  1 
ATOM   1506 O OD1 . ASP A 1 212 ? -2.449  -4.181  7.176   1.00 9.93   ? 198 ASP A OD1 1 
ATOM   1507 O OD2 . ASP A 1 212 ? -0.366  -4.193  6.374   1.00 10.12  ? 198 ASP A OD2 1 
ATOM   1508 N N   . SER A 1 213 ? -3.704  -4.329  9.945   1.00 7.96   ? 199 SER A N   1 
ATOM   1509 C CA  . SER A 1 213 ? -4.439  -5.462  10.509  1.00 9.20   ? 199 SER A CA  1 
ATOM   1510 C C   . SER A 1 213 ? -4.839  -6.493  9.460   1.00 9.28   ? 199 SER A C   1 
ATOM   1511 O O   . SER A 1 213 ? -5.550  -7.446  9.787   1.00 10.14  ? 199 SER A O   1 
ATOM   1512 C CB  . SER A 1 213 ? -5.700  -4.975  11.155  1.00 7.97   ? 199 SER A CB  1 
ATOM   1513 O OG  . SER A 1 213 ? -5.436  -3.966  12.151  1.00 8.40   ? 199 SER A OG  1 
ATOM   1514 N N   . THR A 1 214 ? -4.452  -6.280  8.195   1.00 8.73   ? 200 THR A N   1 
ATOM   1515 C CA  . THR A 1 214 ? -5.003  -7.021  7.075   1.00 9.70   ? 200 THR A CA  1 
ATOM   1516 C C   . THR A 1 214 ? -5.009  -8.559  7.286   1.00 9.93   ? 200 THR A C   1 
ATOM   1517 O O   . THR A 1 214 ? -6.022  -9.204  7.029   1.00 12.41  ? 200 THR A O   1 
ATOM   1518 C CB  . THR A 1 214 ? -4.225  -6.775  5.770   1.00 9.40   ? 200 THR A CB  1 
ATOM   1519 O OG1 . THR A 1 214 ? -4.157  -5.383  5.476   1.00 11.64  ? 200 THR A OG1 1 
ATOM   1520 C CG2 . THR A 1 214 ? -4.859  -7.483  4.593   1.00 12.16  ? 200 THR A CG2 1 
ATOM   1521 N N   . GLU A 1 215 ? -3.891  -9.109  7.783   1.00 10.77  ? 201 GLU A N   1 
ATOM   1522 C CA  . GLU A 1 215 ? -3.733  -10.541 8.015   1.00 10.70  ? 201 GLU A CA  1 
ATOM   1523 C C   . GLU A 1 215 ? -3.716  -10.908 9.508   1.00 11.67  ? 201 GLU A C   1 
ATOM   1524 O O   . GLU A 1 215 ? -3.234  -12.012 9.856   1.00 12.36  ? 201 GLU A O   1 
ATOM   1525 C CB  . GLU A 1 215 ? -2.463  -11.037 7.319   1.00 12.01  ? 201 GLU A CB  1 
ATOM   1526 C CG  . GLU A 1 215 ? -2.563  -10.944 5.792   1.00 14.58  ? 201 GLU A CG  1 
ATOM   1527 C CD  . GLU A 1 215 ? -3.561  -11.869 5.112   1.00 22.97  ? 201 GLU A CD  1 
ATOM   1528 O OE1 . GLU A 1 215 ? -3.989  -12.824 5.738   1.00 25.85  ? 201 GLU A OE1 1 
ATOM   1529 O OE2 . GLU A 1 215 ? -3.898  -11.630 3.938   1.00 36.90  ? 201 GLU A OE2 1 
ATOM   1530 N N   . ALA A 1 216 ? -4.293  -10.061 10.383  1.00 11.40  ? 202 ALA A N   1 
ATOM   1531 C CA  . ALA A 1 216 ? -4.278  -10.350 11.800  1.00 10.93  ? 202 ALA A CA  1 
ATOM   1532 C C   . ALA A 1 216 ? -5.079  -11.604 12.190  1.00 11.22  ? 202 ALA A C   1 
ATOM   1533 O O   . ALA A 1 216 ? -4.871  -12.103 13.301  1.00 13.37  ? 202 ALA A O   1 
ATOM   1534 C CB  . ALA A 1 216 ? -4.762  -9.138  12.563  1.00 11.93  ? 202 ALA A CB  1 
ATOM   1535 N N   . GLU A 1 217 ? -5.936  -12.101 11.322  1.00 12.85  ? 203 GLU A N   1 
ATOM   1536 C CA  . GLU A 1 217 ? -6.703  -13.305 11.640  1.00 14.98  ? 203 GLU A CA  1 
ATOM   1537 C C   . GLU A 1 217 ? -5.908  -14.577 11.330  1.00 16.51  ? 203 GLU A C   1 
ATOM   1538 O O   . GLU A 1 217 ? -6.384  -15.666 11.684  1.00 20.03  ? 203 GLU A O   1 
ATOM   1539 C CB  . GLU A 1 217 ? -7.991  -13.327 10.815  1.00 14.11  ? 203 GLU A CB  1 
ATOM   1540 C CG  . GLU A 1 217 ? -8.974  -12.195 11.105  1.00 15.73  ? 203 GLU A CG  1 
ATOM   1541 C CD  . GLU A 1 217 ? -10.024 -12.112 10.012  1.00 17.45  ? 203 GLU A CD  1 
ATOM   1542 O OE1 . GLU A 1 217 ? -9.726  -11.681 8.836   1.00 18.14  ? 203 GLU A OE1 1 
ATOM   1543 O OE2 . GLU A 1 217 ? -11.169 -12.488 10.296  1.00 24.50  ? 203 GLU A OE2 1 
ATOM   1544 N N   . LYS A 1 218 ? -4.764  -14.454 10.612  1.00 14.50  ? 204 LYS A N   1 
ATOM   1545 C CA  . LYS A 1 218 ? -4.066  -15.612 10.060  1.00 14.77  ? 204 LYS A CA  1 
ATOM   1546 C C   . LYS A 1 218 ? -2.929  -16.030 10.991  1.00 18.12  ? 204 LYS A C   1 
ATOM   1547 O O   . LYS A 1 218 ? -1.963  -15.291 11.198  1.00 15.76  ? 204 LYS A O   1 
ATOM   1548 C CB  . LYS A 1 218 ? -3.507  -15.277 8.670   1.00 15.98  ? 204 LYS A CB  1 
ATOM   1549 N N   . PRO A 1 219 ? -2.962  -17.257 11.591  1.00 16.88  ? 205 PRO A N   1 
ATOM   1550 C CA  . PRO A 1 219 ? -1.877  -17.653 12.498  1.00 17.28  ? 205 PRO A CA  1 
ATOM   1551 C C   . PRO A 1 219 ? -0.546  -17.758 11.760  1.00 14.79  ? 205 PRO A C   1 
ATOM   1552 O O   . PRO A 1 219 ? -0.537  -17.969 10.546  1.00 18.67  ? 205 PRO A O   1 
ATOM   1553 C CB  . PRO A 1 219 ? -2.324  -19.027 13.051  1.00 20.70  ? 205 PRO A CB  1 
ATOM   1554 C CG  . PRO A 1 219 ? -3.846  -18.994 12.885  1.00 23.75  ? 205 PRO A CG  1 
ATOM   1555 C CD  . PRO A 1 219 ? -4.109  -18.185 11.622  1.00 21.97  ? 205 PRO A CD  1 
ATOM   1556 N N   . GLY A 1 220 ? 0.532   -17.648 12.530  1.00 16.32  ? 206 GLY A N   1 
ATOM   1557 C CA  . GLY A 1 220 ? 1.889   -17.928 12.072  1.00 14.79  ? 206 GLY A CA  1 
ATOM   1558 C C   . GLY A 1 220 ? 2.438   -16.734 11.275  1.00 14.03  ? 206 GLY A C   1 
ATOM   1559 O O   . GLY A 1 220 ? 2.276   -15.550 11.654  1.00 14.81  ? 206 GLY A O   1 
ATOM   1560 N N   . TYR A 1 221 ? 3.232   -17.078 10.240  1.00 14.12  ? 207 TYR A N   1 
ATOM   1561 C CA  . TYR A 1 221 ? 3.979   -16.127 9.428   1.00 15.59  ? 207 TYR A CA  1 
ATOM   1562 C C   . TYR A 1 221 ? 3.532   -16.277 7.983   1.00 15.40  ? 207 TYR A C   1 
ATOM   1563 O O   . TYR A 1 221 ? 3.185   -17.360 7.537   1.00 15.11  ? 207 TYR A O   1 
ATOM   1564 C CB  . TYR A 1 221 ? 5.504   -16.368 9.446   1.00 13.85  ? 207 TYR A CB  1 
ATOM   1565 C CG  . TYR A 1 221 ? 6.184   -16.217 10.777  1.00 18.08  ? 207 TYR A CG  1 
ATOM   1566 C CD1 . TYR A 1 221 ? 6.060   -17.185 11.766  1.00 17.00  ? 207 TYR A CD1 1 
ATOM   1567 C CD2 . TYR A 1 221 ? 6.882   -15.061 11.092  1.00 18.35  ? 207 TYR A CD2 1 
ATOM   1568 C CE1 . TYR A 1 221 ? 6.669   -17.041 13.022  1.00 18.17  ? 207 TYR A CE1 1 
ATOM   1569 C CE2 . TYR A 1 221 ? 7.506   -14.903 12.316  1.00 19.66  ? 207 TYR A CE2 1 
ATOM   1570 C CZ  . TYR A 1 221 ? 7.408   -15.902 13.282  1.00 18.22  ? 207 TYR A CZ  1 
ATOM   1571 O OH  . TYR A 1 221 ? 8.061   -15.671 14.462  1.00 22.26  ? 207 TYR A OH  1 
ATOM   1572 N N   . ASN A 1 222 ? 3.655   -15.197 7.192   1.00 15.32  ? 208 ASN A N   1 
ATOM   1573 C CA  . ASN A 1 222 ? 3.565   -15.372 5.748   1.00 15.34  ? 208 ASN A CA  1 
ATOM   1574 C C   . ASN A 1 222 ? 4.632   -16.366 5.284   1.00 16.25  ? 208 ASN A C   1 
ATOM   1575 O O   . ASN A 1 222 ? 5.748   -16.446 5.810   1.00 17.42  ? 208 ASN A O   1 
ATOM   1576 C CB  . ASN A 1 222 ? 3.873   -14.072 5.013   1.00 18.34  ? 208 ASN A CB  1 
ATOM   1577 C CG  . ASN A 1 222 ? 2.727   -13.094 5.089   1.00 17.71  ? 208 ASN A CG  1 
ATOM   1578 O OD1 . ASN A 1 222 ? 2.870   -12.050 5.731   1.00 17.94  ? 208 ASN A OD1 1 
ATOM   1579 N ND2 . ASN A 1 222 ? 1.609   -13.418 4.452   1.00 17.98  ? 208 ASN A ND2 1 
ATOM   1580 N N   . THR A 1 223 ? 4.275   -17.127 4.263   1.00 15.74  ? 209 THR A N   1 
ATOM   1581 C CA  . THR A 1 223 ? 5.257   -17.985 3.632   1.00 18.24  ? 209 THR A CA  1 
ATOM   1582 C C   . THR A 1 223 ? 6.353   -17.090 3.052   1.00 15.61  ? 209 THR A C   1 
ATOM   1583 O O   . THR A 1 223 ? 6.060   -16.104 2.345   1.00 15.58  ? 209 THR A O   1 
ATOM   1584 C CB  . THR A 1 223 ? 4.579   -18.764 2.499   1.00 19.16  ? 209 THR A CB  1 
ATOM   1585 O OG1 . THR A 1 223 ? 3.487   -19.541 3.010   1.00 19.95  ? 209 THR A OG1 1 
ATOM   1586 C CG2 . THR A 1 223 ? 5.557   -19.686 1.814   1.00 20.51  ? 209 THR A CG2 1 
ATOM   1587 N N   . PRO A 1 224 ? 7.644   -17.373 3.336   1.00 16.58  ? 210 PRO A N   1 
ATOM   1588 C CA  . PRO A 1 224 ? 8.763   -16.584 2.813   1.00 15.13  ? 210 PRO A CA  1 
ATOM   1589 C C   . PRO A 1 224 ? 8.729   -16.536 1.282   1.00 14.24  ? 210 PRO A C   1 
ATOM   1590 O O   . PRO A 1 224 ? 8.363   -17.511 0.634   1.00 12.68  ? 210 PRO A O   1 
ATOM   1591 C CB  . PRO A 1 224 ? 10.007  -17.355 3.270   1.00 22.07  ? 210 PRO A CB  1 
ATOM   1592 C CG  . PRO A 1 224 ? 9.526   -18.147 4.462   1.00 20.33  ? 210 PRO A CG  1 
ATOM   1593 C CD  . PRO A 1 224 ? 8.077   -18.477 4.213   1.00 18.21  ? 210 PRO A CD  1 
ATOM   1594 N N   . GLU A 1 225 ? 9.092   -15.396 0.709   1.00 14.86  ? 211 GLU A N   1 
ATOM   1595 C CA  . GLU A 1 225 ? 9.021   -15.228 -0.745  1.00 12.82  ? 211 GLU A CA  1 
ATOM   1596 C C   . GLU A 1 225 ? 9.913   -16.214 -1.504  1.00 15.04  ? 211 GLU A C   1 
ATOM   1597 O O   . GLU A 1 225 ? 9.563   -16.605 -2.614  1.00 14.52  ? 211 GLU A O   1 
ATOM   1598 C CB  . GLU A 1 225 ? 9.287   -13.760 -1.116  1.00 16.31  ? 211 GLU A CB  1 
ATOM   1599 C CG  . GLU A 1 225 ? 8.157   -12.809 -0.681  1.00 14.02  ? 211 GLU A CG  1 
ATOM   1600 C CD  . GLU A 1 225 ? 6.875   -12.903 -1.478  1.00 16.71  ? 211 GLU A CD  1 
ATOM   1601 O OE1 . GLU A 1 225 ? 6.815   -13.718 -2.416  1.00 14.95  ? 211 GLU A OE1 1 
ATOM   1602 O OE2 . GLU A 1 225 ? 5.925   -12.129 -1.167  1.00 19.58  ? 211 GLU A OE2 1 
ATOM   1603 N N   . ASN A 1 226 ? 11.020  -16.699 -0.908  1.00 16.11  ? 212 ASN A N   1 
ATOM   1604 C CA  . ASN A 1 226 ? 11.860  -17.674 -1.634  1.00 16.63  ? 212 ASN A CA  1 
ATOM   1605 C C   . ASN A 1 226 ? 11.067  -18.963 -1.879  1.00 15.65  ? 212 ASN A C   1 
ATOM   1606 O O   . ASN A 1 226 ? 11.217  -19.639 -2.881  1.00 19.57  ? 212 ASN A O   1 
ATOM   1607 C CB  . ASN A 1 226 ? 13.189  -17.958 -0.899  1.00 14.61  ? 212 ASN A CB  1 
ATOM   1608 C CG  . ASN A 1 226 ? 13.055  -18.620 0.471   1.00 22.36  ? 212 ASN A CG  1 
ATOM   1609 O OD1 . ASN A 1 226 ? 12.309  -18.151 1.321   1.00 18.42  ? 212 ASN A OD1 1 
ATOM   1610 N ND2 . ASN A 1 226 ? 13.797  -19.686 0.690   1.00 27.20  ? 212 ASN A ND2 1 
ATOM   1611 N N   . ILE A 1 227 ? 10.287  -19.365 -0.877  1.00 17.34  ? 213 ILE A N   1 
ATOM   1612 C CA  . ILE A 1 227 ? 9.516   -20.594 -0.932  1.00 17.71  ? 213 ILE A CA  1 
ATOM   1613 C C   . ILE A 1 227 ? 8.339   -20.395 -1.885  1.00 14.81  ? 213 ILE A C   1 
ATOM   1614 O O   . ILE A 1 227 ? 8.037   -21.268 -2.684  1.00 16.12  ? 213 ILE A O   1 
ATOM   1615 C CB  . ILE A 1 227 ? 9.072   -21.004 0.488   1.00 18.63  ? 213 ILE A CB  1 
ATOM   1616 C CG1 . ILE A 1 227 ? 10.291  -21.343 1.344   1.00 19.67  ? 213 ILE A CG1 1 
ATOM   1617 C CG2 . ILE A 1 227 ? 8.063   -22.146 0.473   1.00 19.66  ? 213 ILE A CG2 1 
ATOM   1618 C CD1 . ILE A 1 227 ? 9.964   -21.714 2.784   1.00 22.08  ? 213 ILE A CD1 1 
ATOM   1619 N N   . ILE A 1 228 ? 7.735   -19.199 -1.875  1.00 13.68  ? 214 ILE A N   1 
ATOM   1620 C CA  . ILE A 1 228 ? 6.690   -18.887 -2.846  1.00 13.57  ? 214 ILE A CA  1 
ATOM   1621 C C   . ILE A 1 228 ? 7.256   -19.008 -4.268  1.00 15.44  ? 214 ILE A C   1 
ATOM   1622 O O   . ILE A 1 228 ? 6.601   -19.592 -5.133  1.00 13.84  ? 214 ILE A O   1 
ATOM   1623 C CB  . ILE A 1 228 ? 6.091   -17.480 -2.586  1.00 14.56  ? 214 ILE A CB  1 
ATOM   1624 C CG1 . ILE A 1 228 ? 5.120   -17.494 -1.397  1.00 15.91  ? 214 ILE A CG1 1 
ATOM   1625 C CG2 . ILE A 1 228 ? 5.349   -16.971 -3.830  1.00 14.05  ? 214 ILE A CG2 1 
ATOM   1626 C CD1 . ILE A 1 228 ? 4.831   -16.117 -0.910  1.00 21.88  ? 214 ILE A CD1 1 
ATOM   1627 N N   . GLU A 1 229 ? 8.456   -18.484 -4.502  1.00 13.26  ? 215 GLU A N   1 
ATOM   1628 C CA  . GLU A 1 229 ? 9.025   -18.485 -5.853  1.00 14.04  ? 215 GLU A CA  1 
ATOM   1629 C C   . GLU A 1 229 ? 9.308   -19.927 -6.291  1.00 13.98  ? 215 GLU A C   1 
ATOM   1630 O O   . GLU A 1 229 ? 9.085   -20.255 -7.459  1.00 14.62  ? 215 GLU A O   1 
ATOM   1631 C CB  . GLU A 1 229 ? 10.323  -17.683 -5.899  1.00 12.63  ? 215 GLU A CB  1 
ATOM   1632 C CG  . GLU A 1 229 ? 10.948  -17.565 -7.294  1.00 13.66  ? 215 GLU A CG  1 
ATOM   1633 C CD  . GLU A 1 229 ? 12.141  -16.617 -7.366  1.00 17.51  ? 215 GLU A CD  1 
ATOM   1634 O OE1 . GLU A 1 229 ? 12.487  -16.038 -6.333  1.00 21.52  ? 215 GLU A OE1 1 
ATOM   1635 O OE2 . GLU A 1 229 ? 12.731  -16.473 -8.431  1.00 21.53  ? 215 GLU A OE2 1 
ATOM   1636 N N   . HIS A 1 230 ? 9.780   -20.776 -5.354  1.00 14.48  ? 216 HIS A N   1 
ATOM   1637 C CA  . HIS A 1 230 ? 10.011  -22.190 -5.661  1.00 15.37  ? 216 HIS A CA  1 
ATOM   1638 C C   . HIS A 1 230 ? 8.718   -22.886 -6.107  1.00 13.64  ? 216 HIS A C   1 
ATOM   1639 O O   . HIS A 1 230 ? 8.695   -23.658 -7.078  1.00 15.32  ? 216 HIS A O   1 
ATOM   1640 C CB  . HIS A 1 230 ? 10.753  -22.872 -4.494  1.00 14.85  ? 216 HIS A CB  1 
ATOM   1641 C CG  . HIS A 1 230 ? 12.161  -22.355 -4.338  1.00 23.98  ? 216 HIS A CG  1 
ATOM   1642 N ND1 . HIS A 1 230 ? 12.961  -22.611 -3.236  1.00 32.60  ? 216 HIS A ND1 1 
ATOM   1643 C CD2 . HIS A 1 230 ? 12.904  -21.560 -5.176  1.00 33.07  ? 216 HIS A CD2 1 
ATOM   1644 C CE1 . HIS A 1 230 ? 14.141  -22.010 -3.394  1.00 43.36  ? 216 HIS A CE1 1 
ATOM   1645 N NE2 . HIS A 1 230 ? 14.129  -21.348 -4.593  1.00 35.96  ? 216 HIS A NE2 1 
ATOM   1646 N N   . HIS A 1 231 ? 7.634   -22.624 -5.378  1.00 14.77  ? 217 HIS A N   1 
ATOM   1647 C CA  . HIS A 1 231 ? 6.343   -23.188 -5.678  1.00 14.38  ? 217 HIS A CA  1 
ATOM   1648 C C   . HIS A 1 231 ? 5.805   -22.654 -7.000  1.00 12.99  ? 217 HIS A C   1 
ATOM   1649 O O   . HIS A 1 231 ? 5.183   -23.415 -7.729  1.00 14.57  ? 217 HIS A O   1 
ATOM   1650 C CB  . HIS A 1 231 ? 5.385   -22.992 -4.502  1.00 18.18  ? 217 HIS A CB  1 
ATOM   1651 C CG  . HIS A 1 231 ? 5.722   -23.963 -3.402  1.00 29.31  ? 217 HIS A CG  1 
ATOM   1652 N ND1 . HIS A 1 231 ? 6.763   -23.823 -2.504  1.00 41.94  ? 217 HIS A ND1 1 
ATOM   1653 C CD2 . HIS A 1 231 ? 5.146   -25.171 -3.137  1.00 30.29  ? 217 HIS A CD2 1 
ATOM   1654 C CE1 . HIS A 1 231 ? 6.787   -24.876 -1.692  1.00 32.75  ? 217 HIS A CE1 1 
ATOM   1655 N NE2 . HIS A 1 231 ? 5.797   -25.717 -2.063  1.00 36.31  ? 217 HIS A NE2 1 
ATOM   1656 N N   . MET A 1 232 ? 6.022   -21.360 -7.289  1.00 12.85  ? 218 MET A N   1 
ATOM   1657 C CA  . MET A 1 232 ? 5.616   -20.838 -8.594  1.00 12.82  ? 218 MET A CA  1 
ATOM   1658 C C   . MET A 1 232 ? 6.377   -21.526 -9.722  1.00 12.46  ? 218 MET A C   1 
ATOM   1659 O O   . MET A 1 232 ? 5.771   -21.833 -10.743 1.00 13.06  ? 218 MET A O   1 
ATOM   1660 C CB  . MET A 1 232 ? 5.919   -19.339 -8.653  1.00 13.51  ? 218 MET A CB  1 
ATOM   1661 C CG  . MET A 1 232 ? 4.916   -18.520 -7.835  1.00 13.66  ? 218 MET A CG  1 
ATOM   1662 S SD  . MET A 1 232 ? 5.502   -16.824 -7.546  1.00 14.32  ? 218 MET A SD  1 
ATOM   1663 C CE  . MET A 1 232 ? 5.440   -16.150 -9.208  1.00 14.80  ? 218 MET A CE  1 
ATOM   1664 N N   . TYR A 1 233 ? 7.694   -21.760 -9.553  1.00 12.07  ? 219 TYR A N   1 
ATOM   1665 C CA  . TYR A 1 233 ? 8.432   -22.478 -10.589 1.00 11.71  ? 219 TYR A CA  1 
ATOM   1666 C C   . TYR A 1 233 ? 7.767   -23.840 -10.825 1.00 12.17  ? 219 TYR A C   1 
ATOM   1667 O O   . TYR A 1 233 ? 7.545   -24.223 -11.977 1.00 12.80  ? 219 TYR A O   1 
ATOM   1668 C CB  . TYR A 1 233 ? 9.908   -22.639 -10.186 1.00 11.64  ? 219 TYR A CB  1 
ATOM   1669 C CG  . TYR A 1 233 ? 10.636  -23.514 -11.184 1.00 11.73  ? 219 TYR A CG  1 
ATOM   1670 C CD1 . TYR A 1 233 ? 11.352  -22.974 -12.243 1.00 14.52  ? 219 TYR A CD1 1 
ATOM   1671 C CD2 . TYR A 1 233 ? 10.602  -24.906 -11.075 1.00 12.81  ? 219 TYR A CD2 1 
ATOM   1672 C CE1 . TYR A 1 233 ? 11.983  -23.774 -13.187 1.00 12.82  ? 219 TYR A CE1 1 
ATOM   1673 C CE2 . TYR A 1 233 ? 11.190  -25.713 -12.034 1.00 13.39  ? 219 TYR A CE2 1 
ATOM   1674 C CZ  . TYR A 1 233 ? 11.888  -25.144 -13.098 1.00 12.64  ? 219 TYR A CZ  1 
ATOM   1675 O OH  . TYR A 1 233 ? 12.483  -25.974 -14.022 1.00 17.00  ? 219 TYR A OH  1 
ATOM   1676 N N   . ASP A 1 234 ? 7.506   -24.594 -9.752  1.00 12.26  ? 220 ASP A N   1 
ATOM   1677 C CA  . ASP A 1 234 ? 6.945   -25.930 -9.950  1.00 11.64  ? 220 ASP A CA  1 
ATOM   1678 C C   . ASP A 1 234 ? 5.600   -25.876 -10.686 1.00 13.81  ? 220 ASP A C   1 
ATOM   1679 O O   . ASP A 1 234 ? 5.320   -26.693 -11.569 1.00 15.90  ? 220 ASP A O   1 
ATOM   1680 C CB  . ASP A 1 234 ? 6.759   -26.652 -8.609  1.00 15.60  ? 220 ASP A CB  1 
ATOM   1681 C CG  . ASP A 1 234 ? 8.063   -27.070 -7.931  1.00 17.42  ? 220 ASP A CG  1 
ATOM   1682 O OD1 . ASP A 1 234 ? 9.122   -27.088 -8.583  1.00 21.51  ? 220 ASP A OD1 1 
ATOM   1683 O OD2 . ASP A 1 234 ? 8.011   -27.282 -6.737  1.00 24.38  ? 220 ASP A OD2 1 
ATOM   1684 N N   . ALA A 1 235 ? 4.764   -24.895 -10.345 1.00 13.59  ? 221 ALA A N   1 
ATOM   1685 C CA  . ALA A 1 235 ? 3.439   -24.783 -10.948 1.00 13.79  ? 221 ALA A CA  1 
ATOM   1686 C C   . ALA A 1 235 ? 3.603   -24.350 -12.416 1.00 14.88  ? 221 ALA A C   1 
ATOM   1687 O O   . ALA A 1 235 ? 2.927   -24.865 -13.309 1.00 16.68  ? 221 ALA A O   1 
ATOM   1688 C CB  . ALA A 1 235 ? 2.643   -23.750 -10.165 1.00 16.59  ? 221 ALA A CB  1 
ATOM   1689 N N   . PHE A 1 236 ? 4.499   -23.393 -12.678 1.00 13.22  ? 222 PHE A N   1 
ATOM   1690 C CA  . PHE A 1 236 ? 4.625   -22.843 -14.021 1.00 12.28  ? 222 PHE A CA  1 
ATOM   1691 C C   . PHE A 1 236 ? 5.259   -23.871 -14.944 1.00 14.19  ? 222 PHE A C   1 
ATOM   1692 O O   . PHE A 1 236 ? 4.941   -23.895 -16.134 1.00 14.45  ? 222 PHE A O   1 
ATOM   1693 C CB  . PHE A 1 236 ? 5.420   -21.540 -14.062 1.00 11.66  ? 222 PHE A CB  1 
ATOM   1694 C CG  . PHE A 1 236 ? 4.805   -20.346 -13.366 1.00 12.73  ? 222 PHE A CG  1 
ATOM   1695 C CD1 . PHE A 1 236 ? 3.590   -20.435 -12.701 1.00 14.11  ? 222 PHE A CD1 1 
ATOM   1696 C CD2 . PHE A 1 236 ? 5.469   -19.129 -13.432 1.00 14.17  ? 222 PHE A CD2 1 
ATOM   1697 C CE1 . PHE A 1 236 ? 3.066   -19.323 -12.038 1.00 15.88  ? 222 PHE A CE1 1 
ATOM   1698 C CE2 . PHE A 1 236 ? 4.917   -18.015 -12.802 1.00 15.30  ? 222 PHE A CE2 1 
ATOM   1699 C CZ  . PHE A 1 236 ? 3.736   -18.133 -12.101 1.00 14.92  ? 222 PHE A CZ  1 
ATOM   1700 N N   . ALA A 1 237 ? 6.134   -24.745 -14.399 1.00 13.10  ? 223 ALA A N   1 
ATOM   1701 C CA  . ALA A 1 237 ? 6.791   -25.751 -15.234 1.00 13.82  ? 223 ALA A CA  1 
ATOM   1702 C C   . ALA A 1 237 ? 5.773   -26.758 -15.801 1.00 15.39  ? 223 ALA A C   1 
ATOM   1703 O O   . ALA A 1 237 ? 6.052   -27.394 -16.834 1.00 20.45  ? 223 ALA A O   1 
ATOM   1704 C CB  . ALA A 1 237 ? 7.867   -26.475 -14.433 1.00 16.37  ? 223 ALA A CB  1 
ATOM   1705 N N   . LYS A 1 238 ? 4.618   -26.921 -15.138 1.00 15.96  ? 224 LYS A N   1 
ATOM   1706 C CA  . LYS A 1 238 ? 3.595   -27.885 -15.559 1.00 19.05  ? 224 LYS A CA  1 
ATOM   1707 C C   . LYS A 1 238 ? 2.643   -27.292 -16.601 1.00 20.66  ? 224 LYS A C   1 
ATOM   1708 O O   . LYS A 1 238 ? 1.869   -28.024 -17.202 1.00 24.89  ? 224 LYS A O   1 
ATOM   1709 C CB  . LYS A 1 238 ? 2.689   -28.306 -14.393 1.00 22.87  ? 224 LYS A CB  1 
ATOM   1710 C CG  . LYS A 1 238 ? 3.329   -29.122 -13.271 1.00 28.57  ? 224 LYS A CG  1 
ATOM   1711 C CD  . LYS A 1 238 ? 2.357   -29.360 -12.111 1.00 27.29  ? 224 LYS A CD  1 
ATOM   1712 C CE  . LYS A 1 238 ? 2.918   -30.203 -10.988 1.00 48.53  ? 224 LYS A CE  1 
ATOM   1713 N NZ  . LYS A 1 238 ? 4.073   -29.551 -10.324 1.00 74.52  ? 224 LYS A NZ  1 
ATOM   1714 N N   . VAL A 1 239 ? 2.697   -25.963 -16.834 1.00 15.23  ? 225 VAL A N   1 
ATOM   1715 C CA  . VAL A 1 239 ? 1.752   -25.317 -17.747 1.00 16.47  ? 225 VAL A CA  1 
ATOM   1716 C C   . VAL A 1 239 ? 2.107   -25.654 -19.197 1.00 16.71  ? 225 VAL A C   1 
ATOM   1717 O O   . VAL A 1 239 ? 3.218   -25.377 -19.643 1.00 19.08  ? 225 VAL A O   1 
ATOM   1718 C CB  . VAL A 1 239 ? 1.763   -23.781 -17.547 1.00 14.78  ? 225 VAL A CB  1 
ATOM   1719 C CG1 . VAL A 1 239 ? 0.921   -23.059 -18.585 1.00 14.44  ? 225 VAL A CG1 1 
ATOM   1720 C CG2 . VAL A 1 239 ? 1.245   -23.406 -16.163 1.00 16.55  ? 225 VAL A CG2 1 
ATOM   1721 N N   . LYS A 1 240 ? 1.114   -26.157 -19.954 1.00 19.62  ? 226 LYS A N   1 
ATOM   1722 C CA  . LYS A 1 240 ? 1.372   -26.636 -21.310 1.00 21.40  ? 226 LYS A CA  1 
ATOM   1723 C C   . LYS A 1 240 ? 1.109   -25.594 -22.392 1.00 17.88  ? 226 LYS A C   1 
ATOM   1724 O O   . LYS A 1 240 ? 1.729   -25.709 -23.454 1.00 20.74  ? 226 LYS A O   1 
ATOM   1725 C CB  . LYS A 1 240 ? 0.635   -27.943 -21.591 1.00 25.80  ? 226 LYS A CB  1 
ATOM   1726 C CG  . LYS A 1 240 ? 1.231   -29.124 -20.828 1.00 27.99  ? 226 LYS A CG  1 
ATOM   1727 C CD  . LYS A 1 240 ? 2.737   -29.252 -21.076 1.00 50.20  ? 226 LYS A CD  1 
ATOM   1728 C CE  . LYS A 1 240 ? 3.539   -29.839 -19.930 1.00 57.24  ? 226 LYS A CE  1 
ATOM   1729 N NZ  . LYS A 1 240 ? 2.944   -31.103 -19.450 1.00 59.12  ? 226 LYS A NZ  1 
ATOM   1730 N N   . GLY A 1 241 ? 0.272   -24.559 -22.111 1.00 16.49  ? 227 GLY A N   1 
ATOM   1731 C CA  . GLY A 1 241 ? 0.090   -23.503 -23.102 1.00 17.12  ? 227 GLY A CA  1 
ATOM   1732 C C   . GLY A 1 241 ? 0.483   -22.163 -22.495 1.00 15.74  ? 227 GLY A C   1 
ATOM   1733 O O   . GLY A 1 241 ? 1.498   -22.042 -21.827 1.00 16.06  ? 227 GLY A O   1 
ATOM   1734 N N   . ARG A 1 242 ? -0.346  -21.170 -22.755 1.00 15.99  ? 228 ARG A N   1 
ATOM   1735 C CA  . ARG A 1 242 ? -0.001  -19.820 -22.276 1.00 16.22  ? 228 ARG A CA  1 
ATOM   1736 C C   . ARG A 1 242 ? -0.259  -19.712 -20.778 1.00 12.61  ? 228 ARG A C   1 
ATOM   1737 O O   . ARG A 1 242 ? -1.096  -20.424 -20.262 1.00 13.75  ? 228 ARG A O   1 
ATOM   1738 C CB  . ARG A 1 242 ? -0.794  -18.735 -23.021 1.00 14.28  ? 228 ARG A CB  1 
ATOM   1739 C CG  . ARG A 1 242 ? -0.733  -18.779 -24.542 1.00 24.22  ? 228 ARG A CG  1 
ATOM   1740 C CD  . ARG A 1 242 ? -1.353  -17.528 -25.144 1.00 37.67  ? 228 ARG A CD  1 
ATOM   1741 N NE  . ARG A 1 242 ? -2.697  -17.220 -24.670 1.00 27.46  ? 228 ARG A NE  1 
ATOM   1742 C CZ  . ARG A 1 242 ? -3.380  -16.129 -25.001 1.00 26.18  ? 228 ARG A CZ  1 
ATOM   1743 N NH1 . ARG A 1 242 ? -4.595  -15.930 -24.518 1.00 19.57  ? 228 ARG A NH1 1 
ATOM   1744 N NH2 . ARG A 1 242 ? -2.845  -15.242 -25.819 1.00 21.11  ? 228 ARG A NH2 1 
ATOM   1745 N N   . LEU A 1 243 ? 0.531   -18.850 -20.153 1.00 12.52  ? 229 LEU A N   1 
ATOM   1746 C CA  . LEU A 1 243 ? 0.262   -18.542 -18.760 1.00 12.64  ? 229 LEU A CA  1 
ATOM   1747 C C   . LEU A 1 243 ? -0.040  -17.055 -18.616 1.00 12.10  ? 229 LEU A C   1 
ATOM   1748 O O   . LEU A 1 243 ? 0.663   -16.193 -19.185 1.00 12.75  ? 229 LEU A O   1 
ATOM   1749 C CB  . LEU A 1 243 ? 1.528   -18.925 -17.969 1.00 12.48  ? 229 LEU A CB  1 
ATOM   1750 C CG  . LEU A 1 243 ? 1.485   -18.529 -16.494 1.00 13.30  ? 229 LEU A CG  1 
ATOM   1751 C CD1 . LEU A 1 243 ? 0.375   -19.246 -15.754 1.00 15.62  ? 229 LEU A CD1 1 
ATOM   1752 C CD2 . LEU A 1 243 ? 2.838   -18.813 -15.874 1.00 16.31  ? 229 LEU A CD2 1 
ATOM   1753 N N   . ILE A 1 244 ? -1.115  -16.783 -17.864 1.00 11.72  ? 230 ILE A N   1 
ATOM   1754 C CA  . ILE A 1 244 ? -1.468  -15.416 -17.493 1.00 13.47  ? 230 ILE A CA  1 
ATOM   1755 C C   . ILE A 1 244 ? -1.322  -15.311 -15.981 1.00 11.80  ? 230 ILE A C   1 
ATOM   1756 O O   . ILE A 1 244 ? -1.942  -16.092 -15.246 1.00 14.01  ? 230 ILE A O   1 
ATOM   1757 C CB  . ILE A 1 244 ? -2.910  -15.079 -17.942 1.00 14.36  ? 230 ILE A CB  1 
ATOM   1758 C CG1 . ILE A 1 244 ? -2.983  -15.046 -19.476 1.00 19.74  ? 230 ILE A CG1 1 
ATOM   1759 C CG2 . ILE A 1 244 ? -3.320  -13.710 -17.403 1.00 17.23  ? 230 ILE A CG2 1 
ATOM   1760 C CD1 . ILE A 1 244 ? -3.129  -16.365 -20.168 1.00 32.30  ? 230 ILE A CD1 1 
ATOM   1761 N N   . VAL A 1 245 ? -0.503  -14.358 -15.538 1.00 12.42  ? 231 VAL A N   1 
ATOM   1762 C CA  . VAL A 1 245 ? -0.354  -14.078 -14.130 1.00 11.17  ? 231 VAL A CA  1 
ATOM   1763 C C   . VAL A 1 245 ? -1.111  -12.778 -13.857 1.00 11.97  ? 231 VAL A C   1 
ATOM   1764 O O   . VAL A 1 245 ? -0.830  -11.737 -14.462 1.00 13.82  ? 231 VAL A O   1 
ATOM   1765 C CB  . VAL A 1 245 ? 1.147   -13.906 -13.828 1.00 11.68  ? 231 VAL A CB  1 
ATOM   1766 C CG1 . VAL A 1 245 ? 1.339   -13.358 -12.398 1.00 14.14  ? 231 VAL A CG1 1 
ATOM   1767 C CG2 . VAL A 1 245 ? 1.923   -15.200 -14.075 1.00 14.84  ? 231 VAL A CG2 1 
ATOM   1768 N N   . SER A 1 246 ? -2.028  -12.842 -12.892 1.00 12.28  ? 232 SER A N   1 
ATOM   1769 C CA  . SER A 1 246 ? -2.857  -11.707 -12.536 1.00 15.58  ? 232 SER A CA  1 
ATOM   1770 C C   . SER A 1 246 ? -2.367  -11.209 -11.186 1.00 14.31  ? 232 SER A C   1 
ATOM   1771 O O   . SER A 1 246 ? -2.368  -11.954 -10.219 1.00 17.45  ? 232 SER A O   1 
ATOM   1772 C CB  . SER A 1 246 ? -4.303  -12.130 -12.507 1.00 19.79  ? 232 SER A CB  1 
ATOM   1773 O OG  . SER A 1 246 ? -5.121  -11.147 -11.927 1.00 24.82  ? 232 SER A OG  1 
ATOM   1774 N N   . CYS A 1 247 ? -1.802  -9.988  -11.162 1.00 14.15  ? 233 CYS A N   1 
ATOM   1775 C CA  . CYS A 1 247 ? -1.277  -9.422  -9.918  1.00 16.78  ? 233 CYS A CA  1 
ATOM   1776 C C   . CYS A 1 247 ? -1.321  -7.895  -9.975  1.00 16.38  ? 233 CYS A C   1 
ATOM   1777 O O   . CYS A 1 247 ? -1.562  -7.324  -11.038 1.00 17.78  ? 233 CYS A O   1 
ATOM   1778 C CB  . CYS A 1 247 ? 0.138   -9.890  -9.585  1.00 18.33  ? 233 CYS A CB  1 
ATOM   1779 S SG  . CYS A 1 247 ? 1.426   -9.288  -10.699 1.00 19.69  ? 233 CYS A SG  1 
ATOM   1780 N N   . TYR A 1 248 ? -1.081  -7.277  -8.809  1.00 16.10  ? 234 TYR A N   1 
ATOM   1781 C CA  . TYR A 1 248 ? -0.950  -5.817  -8.755  1.00 15.29  ? 234 TYR A CA  1 
ATOM   1782 C C   . TYR A 1 248 ? 0.332   -5.345  -9.443  1.00 14.54  ? 234 TYR A C   1 
ATOM   1783 O O   . TYR A 1 248 ? 1.391   -5.971  -9.329  1.00 15.04  ? 234 TYR A O   1 
ATOM   1784 C CB  . TYR A 1 248 ? -1.009  -5.303  -7.308  1.00 17.99  ? 234 TYR A CB  1 
ATOM   1785 C CG  . TYR A 1 248 ? -2.420  -5.221  -6.790  1.00 26.03  ? 234 TYR A CG  1 
ATOM   1786 C CD1 . TYR A 1 248 ? -2.970  -3.994  -6.473  1.00 33.15  ? 234 TYR A CD1 1 
ATOM   1787 C CD2 . TYR A 1 248 ? -3.207  -6.350  -6.626  1.00 22.20  ? 234 TYR A CD2 1 
ATOM   1788 C CE1 . TYR A 1 248 ? -4.262  -3.881  -5.985  1.00 45.40  ? 234 TYR A CE1 1 
ATOM   1789 C CE2 . TYR A 1 248 ? -4.495  -6.262  -6.113  1.00 30.00  ? 234 TYR A CE2 1 
ATOM   1790 C CZ  . TYR A 1 248 ? -5.026  -5.020  -5.819  1.00 33.52  ? 234 TYR A CZ  1 
ATOM   1791 O OH  . TYR A 1 248 ? -6.297  -4.874  -5.325  1.00 41.21  ? 234 TYR A OH  1 
ATOM   1792 N N   . ALA A 1 249 ? 0.248   -4.184  -10.113 1.00 17.65  ? 235 ALA A N   1 
ATOM   1793 C CA  . ALA A 1 249 ? 1.414   -3.611  -10.773 1.00 18.09  ? 235 ALA A CA  1 
ATOM   1794 C C   . ALA A 1 249 ? 2.447   -3.228  -9.715  1.00 14.47  ? 235 ALA A C   1 
ATOM   1795 O O   . ALA A 1 249 ? 3.640   -3.155  -10.001 1.00 17.91  ? 235 ALA A O   1 
ATOM   1796 C CB  . ALA A 1 249 ? 0.981   -2.417  -11.566 1.00 19.37  ? 235 ALA A CB  1 
ATOM   1797 N N   . SER A 1 250 ? 1.986   -2.988  -8.475  1.00 14.03  ? 236 SER A N   1 
ATOM   1798 C CA  . SER A 1 250 ? 2.887   -2.633  -7.376  1.00 14.13  ? 236 SER A CA  1 
ATOM   1799 C C   . SER A 1 250 ? 3.499   -3.830  -6.660  1.00 12.96  ? 236 SER A C   1 
ATOM   1800 O O   . SER A 1 250 ? 4.328   -3.613  -5.763  1.00 13.31  ? 236 SER A O   1 
ATOM   1801 C CB  . SER A 1 250 ? 2.150   -1.799  -6.363  1.00 16.98  ? 236 SER A CB  1 
ATOM   1802 O OG  . SER A 1 250 ? 0.968   -2.459  -5.950  1.00 20.12  ? 236 SER A OG  1 
ATOM   1803 N N   . ASN A 1 251 ? 3.143   -5.059  -7.072  1.00 12.41  ? 237 ASN A N   1 
ATOM   1804 C CA  . ASN A 1 251 ? 3.758   -6.241  -6.467  1.00 12.34  ? 237 ASN A CA  1 
ATOM   1805 C C   . ASN A 1 251 ? 5.089   -6.535  -7.178  1.00 11.61  ? 237 ASN A C   1 
ATOM   1806 O O   . ASN A 1 251 ? 5.139   -7.436  -8.031  1.00 11.13  ? 237 ASN A O   1 
ATOM   1807 C CB  . ASN A 1 251 ? 2.808   -7.446  -6.503  1.00 12.88  ? 237 ASN A CB  1 
ATOM   1808 C CG  . ASN A 1 251 ? 3.282   -8.531  -5.545  1.00 12.19  ? 237 ASN A CG  1 
ATOM   1809 O OD1 . ASN A 1 251 ? 4.471   -8.594  -5.209  1.00 13.13  ? 237 ASN A OD1 1 
ATOM   1810 N ND2 . ASN A 1 251 ? 2.385   -9.414  -5.115  1.00 15.93  ? 237 ASN A ND2 1 
ATOM   1811 N N   . PHE A 1 252 ? 6.109   -5.735  -6.876  1.00 11.21  ? 238 PHE A N   1 
ATOM   1812 C CA  . PHE A 1 252 ? 7.380   -5.864  -7.578  1.00 9.68   ? 238 PHE A CA  1 
ATOM   1813 C C   . PHE A 1 252 ? 8.018   -7.216  -7.276  1.00 11.58  ? 238 PHE A C   1 
ATOM   1814 O O   . PHE A 1 252 ? 8.697   -7.767  -8.139  1.00 13.16  ? 238 PHE A O   1 
ATOM   1815 C CB  . PHE A 1 252 ? 8.350   -4.747  -7.209  1.00 12.57  ? 238 PHE A CB  1 
ATOM   1816 C CG  . PHE A 1 252 ? 8.052   -3.382  -7.778  1.00 12.92  ? 238 PHE A CG  1 
ATOM   1817 C CD1 . PHE A 1 252 ? 6.823   -3.066  -8.363  1.00 13.25  ? 238 PHE A CD1 1 
ATOM   1818 C CD2 . PHE A 1 252 ? 9.044   -2.403  -7.738  1.00 13.61  ? 238 PHE A CD2 1 
ATOM   1819 C CE1 . PHE A 1 252 ? 6.574   -1.798  -8.878  1.00 16.94  ? 238 PHE A CE1 1 
ATOM   1820 C CE2 . PHE A 1 252 ? 8.801   -1.128  -8.246  1.00 17.03  ? 238 PHE A CE2 1 
ATOM   1821 C CZ  . PHE A 1 252 ? 7.577   -0.834  -8.810  1.00 15.80  ? 238 PHE A CZ  1 
ATOM   1822 N N   . VAL A 1 253 ? 7.858   -7.721  -6.044  1.00 11.71  ? 239 VAL A N   1 
ATOM   1823 C CA  . VAL A 1 253 ? 8.425   -9.016  -5.726  1.00 12.84  ? 239 VAL A CA  1 
ATOM   1824 C C   . VAL A 1 253 ? 7.846   -10.076 -6.673  1.00 12.54  ? 239 VAL A C   1 
ATOM   1825 O O   . VAL A 1 253 ? 8.600   -10.902 -7.199  1.00 12.92  ? 239 VAL A O   1 
ATOM   1826 C CB  . VAL A 1 253 ? 8.140   -9.371  -4.251  1.00 12.66  ? 239 VAL A CB  1 
ATOM   1827 C CG1 . VAL A 1 253 ? 8.471   -10.843 -3.946  1.00 14.22  ? 239 VAL A CG1 1 
ATOM   1828 C CG2 . VAL A 1 253 ? 8.922   -8.470  -3.325  1.00 16.70  ? 239 VAL A CG2 1 
ATOM   1829 N N   . ARG A 1 254 ? 6.522   -10.094 -6.834  1.00 11.42  ? 240 ARG A N   1 
ATOM   1830 C CA  . ARG A 1 254 ? 5.909   -11.106 -7.699  1.00 11.94  ? 240 ARG A CA  1 
ATOM   1831 C C   . ARG A 1 254 ? 6.379   -10.948 -9.149  1.00 11.77  ? 240 ARG A C   1 
ATOM   1832 O O   . ARG A 1 254 ? 6.681   -11.935 -9.848  1.00 13.65  ? 240 ARG A O   1 
ATOM   1833 C CB  . ARG A 1 254 ? 4.389   -11.105 -7.532  1.00 13.84  ? 240 ARG A CB  1 
ATOM   1834 C CG  . ARG A 1 254 ? 3.645   -12.300 -8.133  1.00 16.56  ? 240 ARG A CG  1 
ATOM   1835 C CD  . ARG A 1 254 ? 3.721   -13.531 -7.232  1.00 17.79  ? 240 ARG A CD  1 
ATOM   1836 N NE  . ARG A 1 254 ? 3.078   -13.406 -5.928  1.00 19.11  ? 240 ARG A NE  1 
ATOM   1837 C CZ  . ARG A 1 254 ? 3.661   -13.341 -4.724  1.00 20.23  ? 240 ARG A CZ  1 
ATOM   1838 N NH1 . ARG A 1 254 ? 4.976   -13.338 -4.581  1.00 16.14  ? 240 ARG A NH1 1 
ATOM   1839 N NH2 . ARG A 1 254 ? 2.906   -13.217 -3.644  1.00 24.06  ? 240 ARG A NH2 1 
ATOM   1840 N N   . ILE A 1 255 ? 6.460   -9.702  -9.623  1.00 12.95  ? 241 ILE A N   1 
ATOM   1841 C CA  . ILE A 1 255 ? 6.897   -9.471  -10.998 1.00 12.48  ? 241 ILE A CA  1 
ATOM   1842 C C   . ILE A 1 255 ? 8.312   -10.015 -11.188 1.00 12.24  ? 241 ILE A C   1 
ATOM   1843 O O   . ILE A 1 255 ? 8.559   -10.719 -12.173 1.00 13.44  ? 241 ILE A O   1 
ATOM   1844 C CB  . ILE A 1 255 ? 6.790   -7.966  -11.347 1.00 13.65  ? 241 ILE A CB  1 
ATOM   1845 C CG1 . ILE A 1 255 ? 5.313   -7.547  -11.367 1.00 15.78  ? 241 ILE A CG1 1 
ATOM   1846 C CG2 . ILE A 1 255 ? 7.501   -7.672  -12.686 1.00 15.83  ? 241 ILE A CG2 1 
ATOM   1847 C CD1 . ILE A 1 255 ? 5.128   -6.035  -11.396 1.00 19.66  ? 241 ILE A CD1 1 
ATOM   1848 N N   . GLN A 1 256 ? 9.206   -9.757  -10.209 1.00 11.79  ? 242 GLN A N   1 
ATOM   1849 C CA  . GLN A 1 256 ? 10.589  -10.224 -10.316 1.00 11.53  ? 242 GLN A CA  1 
ATOM   1850 C C   . GLN A 1 256 ? 10.634  -11.761 -10.335 1.00 11.11  ? 242 GLN A C   1 
ATOM   1851 O O   . GLN A 1 256 ? 11.418  -12.318 -11.101 1.00 13.49  ? 242 GLN A O   1 
ATOM   1852 C CB  . GLN A 1 256 ? 11.442  -9.662  -9.163  1.00 13.63  ? 242 GLN A CB  1 
ATOM   1853 C CG  . GLN A 1 256 ? 12.911  -10.083 -9.228  1.00 13.91  ? 242 GLN A CG  1 
ATOM   1854 C CD  . GLN A 1 256 ? 13.611  -9.486  -10.427 1.00 15.43  ? 242 GLN A CD  1 
ATOM   1855 O OE1 . GLN A 1 256 ? 13.812  -8.270  -10.498 1.00 17.92  ? 242 GLN A OE1 1 
ATOM   1856 N NE2 . GLN A 1 256 ? 14.016  -10.315 -11.377 1.00 18.63  ? 242 GLN A NE2 1 
ATOM   1857 N N   . GLN A 1 257 ? 9.799   -12.426 -9.530  1.00 11.89  ? 243 GLN A N   1 
ATOM   1858 C CA  . GLN A 1 257 ? 9.739   -13.888 -9.517  1.00 10.06  ? 243 GLN A CA  1 
ATOM   1859 C C   . GLN A 1 257 ? 9.315   -14.401 -10.891 1.00 12.43  ? 243 GLN A C   1 
ATOM   1860 O O   . GLN A 1 257 ? 9.914   -15.356 -11.389 1.00 12.35  ? 243 GLN A O   1 
ATOM   1861 C CB  . GLN A 1 257 ? 8.751   -14.358 -8.453  1.00 11.25  ? 243 GLN A CB  1 
ATOM   1862 C CG  . GLN A 1 257 ? 9.229   -14.059 -7.029  1.00 12.27  ? 243 GLN A CG  1 
ATOM   1863 C CD  . GLN A 1 257 ? 8.136   -14.186 -5.997  1.00 11.15  ? 243 GLN A CD  1 
ATOM   1864 O OE1 . GLN A 1 257 ? 6.949   -14.056 -6.311  1.00 13.31  ? 243 GLN A OE1 1 
ATOM   1865 N NE2 . GLN A 1 257 ? 8.543   -14.475 -4.774  1.00 13.28  ? 243 GLN A NE2 1 
ATOM   1866 N N   . VAL A 1 258 ? 8.294   -13.781 -11.509 1.00 10.31  ? 244 VAL A N   1 
ATOM   1867 C CA  . VAL A 1 258 ? 7.861   -14.211 -12.834 1.00 12.07  ? 244 VAL A CA  1 
ATOM   1868 C C   . VAL A 1 258 ? 8.991   -14.050 -13.848 1.00 12.21  ? 244 VAL A C   1 
ATOM   1869 O O   . VAL A 1 258 ? 9.203   -14.932 -14.677 1.00 12.82  ? 244 VAL A O   1 
ATOM   1870 C CB  . VAL A 1 258 ? 6.587   -13.472 -13.292 1.00 12.16  ? 244 VAL A CB  1 
ATOM   1871 C CG1 . VAL A 1 258 ? 6.208   -13.861 -14.730 1.00 15.40  ? 244 VAL A CG1 1 
ATOM   1872 C CG2 . VAL A 1 258 ? 5.441   -13.744 -12.315 1.00 14.07  ? 244 VAL A CG2 1 
ATOM   1873 N N   . LEU A 1 259 ? 9.727   -12.933 -13.797 1.00 12.58  ? 245 LEU A N   1 
ATOM   1874 C CA  . LEU A 1 259 ? 10.842  -12.699 -14.713 1.00 14.33  ? 245 LEU A CA  1 
ATOM   1875 C C   . LEU A 1 259 ? 11.875  -13.815 -14.543 1.00 12.54  ? 245 LEU A C   1 
ATOM   1876 O O   . LEU A 1 259 ? 12.335  -14.395 -15.553 1.00 15.82  ? 245 LEU A O   1 
ATOM   1877 C CB  . LEU A 1 259 ? 11.499  -11.328 -14.462 1.00 15.21  ? 245 LEU A CB  1 
ATOM   1878 C CG  . LEU A 1 259 ? 10.610  -10.110 -14.672 1.00 18.70  ? 245 LEU A CG  1 
ATOM   1879 C CD1 . LEU A 1 259 ? 11.352  -8.835  -14.316 1.00 20.33  ? 245 LEU A CD1 1 
ATOM   1880 C CD2 . LEU A 1 259 ? 10.137  -10.022 -16.108 1.00 21.37  ? 245 LEU A CD2 1 
ATOM   1881 N N   . ASN A 1 260 ? 12.250  -14.101 -13.276 1.00 12.25  ? 246 ASN A N   1 
ATOM   1882 C CA  . ASN A 1 260 ? 13.255  -15.128 -13.046 1.00 14.36  ? 246 ASN A CA  1 
ATOM   1883 C C   . ASN A 1 260 ? 12.775  -16.479 -13.578 1.00 12.92  ? 246 ASN A C   1 
ATOM   1884 O O   . ASN A 1 260 ? 13.548  -17.198 -14.223 1.00 14.44  ? 246 ASN A O   1 
ATOM   1885 C CB  . ASN A 1 260 ? 13.456  -15.333 -11.558 1.00 12.18  ? 246 ASN A CB  1 
ATOM   1886 C CG  . ASN A 1 260 ? 14.040  -14.128 -10.846 1.00 14.19  ? 246 ASN A CG  1 
ATOM   1887 O OD1 . ASN A 1 260 ? 14.585  -13.216 -11.470 1.00 17.12  ? 246 ASN A OD1 1 
ATOM   1888 N ND2 . ASN A 1 260 ? 14.005  -14.172 -9.512  1.00 16.42  ? 246 ASN A ND2 1 
ATOM   1889 N N   . ILE A 1 261 ? 11.517  -16.878 -13.299 1.00 11.73  ? 247 ILE A N   1 
ATOM   1890 C CA  . ILE A 1 261 ? 11.029  -18.195 -13.677 1.00 12.01  ? 247 ILE A CA  1 
ATOM   1891 C C   . ILE A 1 261 ? 10.919  -18.282 -15.208 1.00 11.65  ? 247 ILE A C   1 
ATOM   1892 O O   . ILE A 1 261 ? 11.246  -19.329 -15.814 1.00 15.42  ? 247 ILE A O   1 
ATOM   1893 C CB  . ILE A 1 261 ? 9.709   -18.496 -12.945 1.00 11.58  ? 247 ILE A CB  1 
ATOM   1894 C CG1 . ILE A 1 261 ? 9.949   -18.604 -11.441 1.00 13.31  ? 247 ILE A CG1 1 
ATOM   1895 C CG2 . ILE A 1 261 ? 9.027   -19.747 -13.489 1.00 13.14  ? 247 ILE A CG2 1 
ATOM   1896 C CD1 . ILE A 1 261 ? 8.665   -18.519 -10.602 1.00 14.28  ? 247 ILE A CD1 1 
ATOM   1897 N N   . ALA A 1 262 ? 10.468  -17.186 -15.854 1.00 11.96  ? 248 ALA A N   1 
ATOM   1898 C CA  . ALA A 1 262 ? 10.309  -17.183 -17.285 1.00 13.48  ? 248 ALA A CA  1 
ATOM   1899 C C   . ALA A 1 262 ? 11.658  -17.492 -17.940 1.00 14.17  ? 248 ALA A C   1 
ATOM   1900 O O   . ALA A 1 262 ? 11.721  -18.327 -18.855 1.00 14.89  ? 248 ALA A O   1 
ATOM   1901 C CB  . ALA A 1 262 ? 9.851   -15.832 -17.737 1.00 13.33  ? 248 ALA A CB  1 
ATOM   1902 N N   . SER A 1 263 ? 12.735  -16.890 -17.408 1.00 15.75  ? 249 SER A N   1 
ATOM   1903 C CA  . SER A 1 263 ? 14.082  -17.092 -17.936 1.00 15.89  ? 249 SER A CA  1 
ATOM   1904 C C   . SER A 1 263 ? 14.461  -18.577 -17.807 1.00 16.84  ? 249 SER A C   1 
ATOM   1905 O O   . SER A 1 263 ? 14.998  -19.184 -18.737 1.00 21.78  ? 249 SER A O   1 
ATOM   1906 C CB  . SER A 1 263 ? 15.038  -16.175 -17.210 1.00 24.63  ? 249 SER A CB  1 
ATOM   1907 O OG  . SER A 1 263 ? 16.293  -16.222 -17.824 1.00 31.20  ? 249 SER A OG  1 
ATOM   1908 N N   . GLN A 1 264 ? 14.086  -19.203 -16.694 1.00 15.69  ? 250 GLN A N   1 
ATOM   1909 C CA  . GLN A 1 264 ? 14.429  -20.600 -16.452 1.00 17.90  ? 250 GLN A CA  1 
ATOM   1910 C C   . GLN A 1 264 ? 13.635  -21.562 -17.321 1.00 14.68  ? 250 GLN A C   1 
ATOM   1911 O O   . GLN A 1 264 ? 14.109  -22.671 -17.563 1.00 16.79  ? 250 GLN A O   1 
ATOM   1912 C CB  . GLN A 1 264 ? 14.204  -20.934 -14.980 1.00 16.79  ? 250 GLN A CB  1 
ATOM   1913 C CG  . GLN A 1 264 ? 15.193  -20.197 -14.079 1.00 20.38  ? 250 GLN A CG  1 
ATOM   1914 C CD  . GLN A 1 264 ? 14.853  -20.228 -12.613 1.00 23.07  ? 250 GLN A CD  1 
ATOM   1915 O OE1 . GLN A 1 264 ? 14.557  -21.272 -12.032 1.00 22.45  ? 250 GLN A OE1 1 
ATOM   1916 N NE2 . GLN A 1 264 ? 14.895  -19.063 -11.982 1.00 29.78  ? 250 GLN A NE2 1 
ATOM   1917 N N   . LEU A 1 265 ? 12.450  -21.133 -17.795 1.00 16.37  ? 251 LEU A N   1 
ATOM   1918 C CA  . LEU A 1 265 ? 11.573  -22.023 -18.536 1.00 14.08  ? 251 LEU A CA  1 
ATOM   1919 C C   . LEU A 1 265 ? 11.541  -21.664 -20.025 1.00 16.63  ? 251 LEU A C   1 
ATOM   1920 O O   . LEU A 1 265 ? 10.657  -22.154 -20.716 1.00 19.02  ? 251 LEU A O   1 
ATOM   1921 C CB  . LEU A 1 265 ? 10.143  -21.995 -17.955 1.00 14.35  ? 251 LEU A CB  1 
ATOM   1922 C CG  . LEU A 1 265 ? 9.992   -22.576 -16.546 1.00 14.88  ? 251 LEU A CG  1 
ATOM   1923 C CD1 . LEU A 1 265 ? 8.563   -22.390 -16.031 1.00 17.28  ? 251 LEU A CD1 1 
ATOM   1924 C CD2 . LEU A 1 265 ? 10.422  -24.039 -16.537 1.00 14.79  ? 251 LEU A CD2 1 
ATOM   1925 N N   . ASN A 1 266 ? 12.458  -20.781 -20.467 1.00 19.37  ? 252 ASN A N   1 
ATOM   1926 C CA  . ASN A 1 266 ? 12.518  -20.324 -21.850 1.00 17.31  ? 252 ASN A CA  1 
ATOM   1927 C C   . ASN A 1 266 ? 11.155  -19.798 -22.305 1.00 17.22  ? 252 ASN A C   1 
ATOM   1928 O O   . ASN A 1 266 ? 10.718  -20.030 -23.431 1.00 22.44  ? 252 ASN A O   1 
ATOM   1929 C CB  . ASN A 1 266 ? 13.154  -21.373 -22.778 1.00 20.32  ? 252 ASN A CB  1 
ATOM   1930 C CG  . ASN A 1 266 ? 14.616  -21.660 -22.446 1.00 21.16  ? 252 ASN A CG  1 
ATOM   1931 O OD1 . ASN A 1 266 ? 15.400  -20.764 -22.128 1.00 31.50  ? 252 ASN A OD1 1 
ATOM   1932 N ND2 . ASN A 1 266 ? 15.024  -22.910 -22.537 1.00 30.68  ? 252 ASN A ND2 1 
ATOM   1933 N N   . ARG A 1 267 ? 10.528  -18.981 -21.456 1.00 16.70  ? 253 ARG A N   1 
ATOM   1934 C CA  . ARG A 1 267 ? 9.352   -18.206 -21.829 1.00 16.47  ? 253 ARG A CA  1 
ATOM   1935 C C   . ARG A 1 267 ? 9.739   -16.722 -21.847 1.00 13.94  ? 253 ARG A C   1 
ATOM   1936 O O   . ARG A 1 267 ? 10.617  -16.261 -21.102 1.00 18.30  ? 253 ARG A O   1 
ATOM   1937 C CB  . ARG A 1 267 ? 8.203   -18.451 -20.839 1.00 16.53  ? 253 ARG A CB  1 
ATOM   1938 C CG  . ARG A 1 267 ? 7.669   -19.889 -20.846 1.00 18.43  ? 253 ARG A CG  1 
ATOM   1939 C CD  . ARG A 1 267 ? 6.451   -19.963 -19.920 1.00 22.08  ? 253 ARG A CD  1 
ATOM   1940 N NE  . ARG A 1 267 ? 5.769   -21.244 -19.973 1.00 27.62  ? 253 ARG A NE  1 
ATOM   1941 C CZ  . ARG A 1 267 ? 4.547   -21.447 -20.444 1.00 60.84  ? 253 ARG A CZ  1 
ATOM   1942 N NH1 . ARG A 1 267 ? 3.826   -20.436 -20.893 1.00 147.70 ? 253 ARG A NH1 1 
ATOM   1943 N NH2 . ARG A 1 267 ? 4.060   -22.677 -20.427 1.00 17.14  ? 253 ARG A NH2 1 
ATOM   1944 N N   . LYS A 1 268 ? 9.106   -15.983 -22.764 1.00 15.22  ? 254 LYS A N   1 
ATOM   1945 C CA  . LYS A 1 268 ? 9.159   -14.523 -22.783 1.00 13.78  ? 254 LYS A CA  1 
ATOM   1946 C C   . LYS A 1 268 ? 8.081   -14.001 -21.839 1.00 14.03  ? 254 LYS A C   1 
ATOM   1947 O O   . LYS A 1 268 ? 7.164   -14.736 -21.514 1.00 18.26  ? 254 LYS A O   1 
ATOM   1948 C CB  . LYS A 1 268 ? 8.889   -13.994 -24.188 1.00 16.33  ? 254 LYS A CB  1 
ATOM   1949 C CG  . LYS A 1 268 ? 9.827   -14.521 -25.264 1.00 20.40  ? 254 LYS A CG  1 
ATOM   1950 C CD  . LYS A 1 268 ? 11.266  -14.241 -24.965 1.00 20.77  ? 254 LYS A CD  1 
ATOM   1951 C CE  . LYS A 1 268 ? 12.192  -14.630 -26.091 1.00 27.00  ? 254 LYS A CE  1 
ATOM   1952 N NZ  . LYS A 1 268 ? 13.524  -14.044 -25.844 1.00 33.04  ? 254 LYS A NZ  1 
ATOM   1953 N N   . VAL A 1 269 ? 8.206   -12.711 -21.500 1.00 13.95  ? 255 VAL A N   1 
ATOM   1954 C CA  . VAL A 1 269 ? 7.276   -12.056 -20.589 1.00 15.13  ? 255 VAL A CA  1 
ATOM   1955 C C   . VAL A 1 269 ? 6.735   -10.818 -21.289 1.00 16.87  ? 255 VAL A C   1 
ATOM   1956 O O   . VAL A 1 269 ? 7.491   -10.103 -21.972 1.00 17.19  ? 255 VAL A O   1 
ATOM   1957 C CB  . VAL A 1 269 ? 7.931   -11.713 -19.229 1.00 13.98  ? 255 VAL A CB  1 
ATOM   1958 C CG1 . VAL A 1 269 ? 6.958   -10.960 -18.316 1.00 16.21  ? 255 VAL A CG1 1 
ATOM   1959 C CG2 . VAL A 1 269 ? 8.392   -12.982 -18.517 1.00 14.12  ? 255 VAL A CG2 1 
ATOM   1960 N N   . SER A 1 270 ? 5.407   -10.620 -21.160 1.00 15.05  ? 256 SER A N   1 
ATOM   1961 C CA  . SER A 1 270 ? 4.821   -9.417  -21.728 1.00 14.85  ? 256 SER A CA  1 
ATOM   1962 C C   . SER A 1 270 ? 3.855   -8.831  -20.707 1.00 13.91  ? 256 SER A C   1 
ATOM   1963 O O   . SER A 1 270 ? 3.176   -9.574  -20.003 1.00 17.54  ? 256 SER A O   1 
ATOM   1964 C CB  . SER A 1 270 ? 4.076   -9.746  -22.985 1.00 18.58  ? 256 SER A CB  1 
ATOM   1965 O OG  . SER A 1 270 ? 3.873   -8.543  -23.703 1.00 21.03  ? 256 SER A OG  1 
ATOM   1966 N N   . PHE A 1 271 ? 3.796   -7.488  -20.667 1.00 15.58  ? 257 PHE A N   1 
ATOM   1967 C CA  . PHE A 1 271 ? 2.888   -6.806  -19.760 1.00 17.20  ? 257 PHE A CA  1 
ATOM   1968 C C   . PHE A 1 271 ? 1.616   -6.374  -20.472 1.00 14.74  ? 257 PHE A C   1 
ATOM   1969 O O   . PHE A 1 271 ? 1.679   -5.800  -21.567 1.00 19.08  ? 257 PHE A O   1 
ATOM   1970 C CB  . PHE A 1 271 ? 3.536   -5.576  -19.143 1.00 17.17  ? 257 PHE A CB  1 
ATOM   1971 C CG  . PHE A 1 271 ? 4.818   -5.792  -18.381 1.00 23.60  ? 257 PHE A CG  1 
ATOM   1972 C CD1 . PHE A 1 271 ? 4.869   -6.658  -17.317 1.00 38.90  ? 257 PHE A CD1 1 
ATOM   1973 C CD2 . PHE A 1 271 ? 5.915   -4.971  -18.619 1.00 29.92  ? 257 PHE A CD2 1 
ATOM   1974 C CE1 . PHE A 1 271 ? 6.031   -6.787  -16.566 1.00 36.04  ? 257 PHE A CE1 1 
ATOM   1975 C CE2 . PHE A 1 271 ? 7.064   -5.073  -17.853 1.00 29.45  ? 257 PHE A CE2 1 
ATOM   1976 C CZ  . PHE A 1 271 ? 7.136   -6.021  -16.857 1.00 32.61  ? 257 PHE A CZ  1 
ATOM   1977 N N   . LEU A 1 272 ? 0.500   -6.638  -19.799 1.00 16.62  ? 258 LEU A N   1 
ATOM   1978 C CA  . LEU A 1 272 ? -0.827  -6.193  -20.192 1.00 18.98  ? 258 LEU A CA  1 
ATOM   1979 C C   . LEU A 1 272 ? -1.373  -5.275  -19.106 1.00 19.03  ? 258 LEU A C   1 
ATOM   1980 O O   . LEU A 1 272 ? -1.617  -5.717  -17.966 1.00 20.93  ? 258 LEU A O   1 
ATOM   1981 C CB  . LEU A 1 272 ? -1.746  -7.400  -20.407 1.00 17.39  ? 258 LEU A CB  1 
ATOM   1982 C CG  . LEU A 1 272 ? -3.131  -7.112  -20.982 1.00 17.82  ? 258 LEU A CG  1 
ATOM   1983 C CD1 . LEU A 1 272 ? -3.032  -6.650  -22.426 1.00 23.63  ? 258 LEU A CD1 1 
ATOM   1984 C CD2 . LEU A 1 272 ? -4.046  -8.327  -20.884 1.00 29.10  ? 258 LEU A CD2 1 
ATOM   1985 N N   . GLY A 1 273 ? -1.508  -3.989  -19.454 1.00 24.49  ? 259 GLY A N   1 
ATOM   1986 C CA  . GLY A 1 273 ? -2.103  -2.997  -18.564 1.00 24.80  ? 259 GLY A CA  1 
ATOM   1987 C C   . GLY A 1 273 ? -1.226  -1.760  -18.379 1.00 31.08  ? 259 GLY A C   1 
ATOM   1988 O O   . GLY A 1 273 ? -0.046  -1.892  -18.083 1.00 32.82  ? 259 GLY A O   1 
ATOM   1989 N N   . ARG A 1 274 ? -1.838  -0.569  -18.477 1.00 38.32  ? 260 ARG A N   1 
ATOM   1990 C CA  . ARG A 1 274 ? -1.124  0.701   -18.506 1.00 40.01  ? 260 ARG A CA  1 
ATOM   1991 C C   . ARG A 1 274 ? -0.392  0.932   -17.186 1.00 30.98  ? 260 ARG A C   1 
ATOM   1992 O O   . ARG A 1 274 ? 0.681   1.531   -17.169 1.00 40.25  ? 260 ARG A O   1 
ATOM   1993 C CB  . ARG A 1 274 ? -2.048  1.863   -18.916 1.00 36.44  ? 260 ARG A CB  1 
ATOM   1994 N N   . SER A 1 275 ? -0.983  0.435   -16.096 1.00 34.74  ? 261 SER A N   1 
ATOM   1995 C CA  . SER A 1 275 ? -0.437  0.517   -14.746 1.00 43.95  ? 261 SER A CA  1 
ATOM   1996 C C   . SER A 1 275 ? 0.930   -0.172  -14.651 1.00 40.05  ? 261 SER A C   1 
ATOM   1997 O O   . SER A 1 275 ? 1.834   0.331   -13.985 1.00 37.57  ? 261 SER A O   1 
ATOM   1998 C CB  . SER A 1 275 ? -1.419  -0.051  -13.730 1.00 51.84  ? 261 SER A CB  1 
ATOM   1999 O OG  . SER A 1 275 ? -1.607  -1.450  -13.937 1.00 41.18  ? 261 SER A OG  1 
ATOM   2000 N N   . LEU A 1 276 ? 1.071   -1.352  -15.269 1.00 39.51  ? 262 LEU A N   1 
ATOM   2001 C CA  . LEU A 1 276 ? 2.318   -2.101  -15.171 1.00 45.62  ? 262 LEU A CA  1 
ATOM   2002 C C   . LEU A 1 276 ? 3.417   -1.414  -15.987 1.00 57.44  ? 262 LEU A C   1 
ATOM   2003 O O   . LEU A 1 276 ? 4.526   -1.222  -15.489 1.00 32.18  ? 262 LEU A O   1 
ATOM   2004 C CB  . LEU A 1 276 ? 2.121   -3.555  -15.629 1.00 30.62  ? 262 LEU A CB  1 
ATOM   2005 N N   . GLU A 1 277 ? 3.122   -1.069  -17.246 1.00 46.74  ? 263 GLU A N   1 
ATOM   2006 C CA  . GLU A 1 277 ? 4.104   -0.437  -18.116 1.00 68.20  ? 263 GLU A CA  1 
ATOM   2007 C C   . GLU A 1 277 ? 4.746   0.763   -17.411 1.00 84.17  ? 263 GLU A C   1 
ATOM   2008 O O   . GLU A 1 277 ? 5.974   0.855   -17.359 1.00 33.66  ? 263 GLU A O   1 
ATOM   2009 C CB  . GLU A 1 277 ? 3.471   -0.056  -19.458 1.00 53.91  ? 263 GLU A CB  1 
ATOM   2010 N N   . SER A 1 278 ? 3.890   1.638   -16.851 1.00 67.75  ? 264 SER A N   1 
ATOM   2011 C CA  . SER A 1 278 ? 4.250   2.904   -16.225 1.00 97.55  ? 264 SER A CA  1 
ATOM   2012 C C   . SER A 1 278 ? 5.145   2.673   -15.005 1.00 67.47  ? 264 SER A C   1 
ATOM   2013 O O   . SER A 1 278 ? 6.213   3.268   -14.877 1.00 69.52  ? 264 SER A O   1 
ATOM   2014 C CB  . SER A 1 278 ? 3.008   3.668   -15.804 1.00 73.19  ? 264 SER A CB  1 
ATOM   2015 O OG  . SER A 1 278 ? 2.673   3.293   -14.465 1.00 86.77  ? 264 SER A OG  1 
ATOM   2016 N N   . SER A 1 279 ? 4.656   1.865   -14.056 1.00 44.24  ? 265 SER A N   1 
ATOM   2017 C CA  . SER A 1 279 ? 5.383   1.653   -12.808 1.00 36.70  ? 265 SER A CA  1 
ATOM   2018 C C   . SER A 1 279 ? 6.688   0.907   -13.090 1.00 26.13  ? 265 SER A C   1 
ATOM   2019 O O   . SER A 1 279 ? 7.715   1.189   -12.481 1.00 23.24  ? 265 SER A O   1 
ATOM   2020 C CB  . SER A 1 279 ? 4.561   0.936   -11.763 1.00 41.36  ? 265 SER A CB  1 
ATOM   2021 O OG  . SER A 1 279 ? 4.407   -0.438  -12.114 1.00 48.87  ? 265 SER A OG  1 
ATOM   2022 N N   . PHE A 1 280 ? 6.640   -0.056  -14.024 1.00 23.22  ? 266 PHE A N   1 
ATOM   2023 C CA  . PHE A 1 280 ? 7.802   -0.867  -14.332 1.00 22.66  ? 266 PHE A CA  1 
ATOM   2024 C C   . PHE A 1 280 ? 8.904   -0.023  -14.965 1.00 28.64  ? 266 PHE A C   1 
ATOM   2025 O O   . PHE A 1 280 ? 10.081  -0.131  -14.555 1.00 25.17  ? 266 PHE A O   1 
ATOM   2026 C CB  . PHE A 1 280 ? 7.422   -2.028  -15.255 1.00 22.97  ? 266 PHE A CB  1 
ATOM   2027 C CG  . PHE A 1 280 ? 8.516   -3.057  -15.398 1.00 29.75  ? 266 PHE A CG  1 
ATOM   2028 C CD1 . PHE A 1 280 ? 8.726   -4.020  -14.403 1.00 25.71  ? 266 PHE A CD1 1 
ATOM   2029 C CD2 . PHE A 1 280 ? 9.381   -3.032  -16.488 1.00 25.26  ? 266 PHE A CD2 1 
ATOM   2030 C CE1 . PHE A 1 280 ? 9.760   -4.934  -14.525 1.00 24.99  ? 266 PHE A CE1 1 
ATOM   2031 C CE2 . PHE A 1 280 ? 10.406  -3.963  -16.606 1.00 31.13  ? 266 PHE A CE2 1 
ATOM   2032 C CZ  . PHE A 1 280 ? 10.582  -4.924  -15.628 1.00 26.31  ? 266 PHE A CZ  1 
ATOM   2033 N N   . ASN A 1 281 ? 8.503   0.829   -15.935 1.00 22.95  ? 267 ASN A N   1 
ATOM   2034 C CA  . ASN A 1 281 ? 9.432   1.695   -16.652 1.00 27.95  ? 267 ASN A CA  1 
ATOM   2035 C C   . ASN A 1 281 ? 10.184  2.566   -15.647 1.00 24.53  ? 267 ASN A C   1 
ATOM   2036 O O   . ASN A 1 281 ? 11.416  2.716   -15.709 1.00 28.43  ? 267 ASN A O   1 
ATOM   2037 C CB  . ASN A 1 281 ? 8.719   2.542   -17.708 1.00 33.95  ? 267 ASN A CB  1 
ATOM   2038 C CG  . ASN A 1 281 ? 9.609   3.605   -18.318 1.00 51.11  ? 267 ASN A CG  1 
ATOM   2039 O OD1 . ASN A 1 281 ? 10.402  3.312   -19.210 1.00 68.51  ? 267 ASN A OD1 1 
ATOM   2040 N ND2 . ASN A 1 281 ? 9.479   4.838   -17.846 1.00 69.17  ? 267 ASN A ND2 1 
ATOM   2041 N N   . ILE A 1 282 ? 9.427   3.167   -14.719 1.00 25.06  ? 268 ILE A N   1 
ATOM   2042 C CA  . ILE A 1 282 ? 10.019  4.081   -13.755 1.00 23.47  ? 268 ILE A CA  1 
ATOM   2043 C C   . ILE A 1 282 ? 10.961  3.286   -12.867 1.00 19.38  ? 268 ILE A C   1 
ATOM   2044 O O   . ILE A 1 282 ? 12.088  3.699   -12.617 1.00 21.74  ? 268 ILE A O   1 
ATOM   2045 C CB  . ILE A 1 282 ? 8.914   4.813   -12.959 1.00 22.04  ? 268 ILE A CB  1 
ATOM   2046 C CG1 . ILE A 1 282 ? 8.214   5.819   -13.878 1.00 31.72  ? 268 ILE A CG1 1 
ATOM   2047 C CG2 . ILE A 1 282 ? 9.466   5.474   -11.693 1.00 26.17  ? 268 ILE A CG2 1 
ATOM   2048 C CD1 . ILE A 1 282 ? 6.857   6.171   -13.436 1.00 36.96  ? 268 ILE A CD1 1 
ATOM   2049 N N   . ALA A 1 283 ? 10.453  2.169   -12.321 1.00 18.81  ? 269 ALA A N   1 
ATOM   2050 C CA  . ALA A 1 283 ? 11.262  1.357   -11.445 1.00 18.02  ? 269 ALA A CA  1 
ATOM   2051 C C   . ALA A 1 283 ? 12.490  0.792   -12.184 1.00 22.62  ? 269 ALA A C   1 
ATOM   2052 O O   . ALA A 1 283 ? 13.583  0.735   -11.613 1.00 23.15  ? 269 ALA A O   1 
ATOM   2053 C CB  . ALA A 1 283 ? 10.395  0.297   -10.829 1.00 19.40  ? 269 ALA A CB  1 
ATOM   2054 N N   . ARG A 1 284 ? 12.335  0.395   -13.448 1.00 26.99  ? 270 ARG A N   1 
ATOM   2055 C CA  . ARG A 1 284 ? 13.478  -0.160  -14.170 1.00 35.06  ? 270 ARG A CA  1 
ATOM   2056 C C   . ARG A 1 284 ? 14.589  0.881   -14.335 1.00 34.34  ? 270 ARG A C   1 
ATOM   2057 O O   . ARG A 1 284 ? 15.766  0.571   -14.123 1.00 29.00  ? 270 ARG A O   1 
ATOM   2058 C CB  . ARG A 1 284 ? 13.026  -0.702  -15.525 1.00 56.50  ? 270 ARG A CB  1 
ATOM   2059 C CG  . ARG A 1 284 ? 14.147  -1.126  -16.457 1.00 58.65  ? 270 ARG A CG  1 
ATOM   2060 C CD  . ARG A 1 284 ? 13.497  -1.395  -17.798 1.00 59.14  ? 270 ARG A CD  1 
ATOM   2061 N NE  . ARG A 1 284 ? 14.229  -2.413  -18.532 1.00 99.17  ? 270 ARG A NE  1 
ATOM   2062 C CZ  . ARG A 1 284 ? 13.737  -3.061  -19.577 1.00 116.80 ? 270 ARG A CZ  1 
ATOM   2063 N NH1 . ARG A 1 284 ? 12.561  -2.710  -20.067 1.00 83.32  ? 270 ARG A NH1 1 
ATOM   2064 N NH2 . ARG A 1 284 ? 14.429  -4.036  -20.143 1.00 133.45 ? 270 ARG A NH2 1 
ATOM   2065 N N   . LYS A 1 285 ? 14.215  2.109   -14.721 1.00 27.28  ? 271 LYS A N   1 
ATOM   2066 C CA  . LYS A 1 285 ? 15.203  3.154   -14.953 1.00 32.35  ? 271 LYS A CA  1 
ATOM   2067 C C   . LYS A 1 285 ? 15.971  3.433   -13.661 1.00 44.89  ? 271 LYS A C   1 
ATOM   2068 O O   . LYS A 1 285 ? 17.151  3.777   -13.698 1.00 55.78  ? 271 LYS A O   1 
ATOM   2069 C CB  . LYS A 1 285 ? 14.526  4.433   -15.453 1.00 36.50  ? 271 LYS A CB  1 
ATOM   2070 N N   . MET A 1 286 ? 15.288  3.253   -12.522 1.00 30.39  ? 272 MET A N   1 
ATOM   2071 C CA  . MET A 1 286 ? 15.855  3.571   -11.225 1.00 36.01  ? 272 MET A CA  1 
ATOM   2072 C C   . MET A 1 286 ? 16.637  2.387   -10.656 1.00 32.68  ? 272 MET A C   1 
ATOM   2073 O O   . MET A 1 286 ? 17.271  2.513   -9.620  1.00 35.07  ? 272 MET A O   1 
ATOM   2074 C CB  . MET A 1 286 ? 14.749  4.050   -10.265 1.00 28.05  ? 272 MET A CB  1 
ATOM   2075 C CG  . MET A 1 286 ? 14.103  5.349   -10.722 1.00 37.06  ? 272 MET A CG  1 
ATOM   2076 S SD  . MET A 1 286 ? 12.656  5.858   -9.765  1.00 30.48  ? 272 MET A SD  1 
ATOM   2077 C CE  . MET A 1 286 ? 13.452  6.207   -8.205  1.00 28.94  ? 272 MET A CE  1 
ATOM   2078 N N   . GLY A 1 287 ? 16.576  1.225   -11.325 1.00 30.81  ? 273 GLY A N   1 
ATOM   2079 C CA  . GLY A 1 287 ? 17.447  0.092   -11.026 1.00 26.81  ? 273 GLY A CA  1 
ATOM   2080 C C   . GLY A 1 287 ? 16.801  -0.992  -10.160 1.00 24.97  ? 273 GLY A C   1 
ATOM   2081 O O   . GLY A 1 287 ? 17.516  -1.805  -9.581  1.00 28.35  ? 273 GLY A O   1 
ATOM   2082 N N   . TYR A 1 288 ? 15.457  -0.984  -10.038 1.00 23.74  ? 274 TYR A N   1 
ATOM   2083 C CA  . TYR A 1 288 ? 14.797  -1.849  -9.058  1.00 20.49  ? 274 TYR A CA  1 
ATOM   2084 C C   . TYR A 1 288 ? 14.593  -3.288  -9.541  1.00 19.70  ? 274 TYR A C   1 
ATOM   2085 O O   . TYR A 1 288 ? 14.154  -4.123  -8.748  1.00 22.28  ? 274 TYR A O   1 
ATOM   2086 C CB  . TYR A 1 288 ? 13.456  -1.262  -8.622  1.00 17.64  ? 274 TYR A CB  1 
ATOM   2087 C CG  . TYR A 1 288 ? 13.600  -0.035  -7.745  1.00 20.81  ? 274 TYR A CG  1 
ATOM   2088 C CD1 . TYR A 1 288 ? 13.933  -0.146  -6.404  1.00 20.42  ? 274 TYR A CD1 1 
ATOM   2089 C CD2 . TYR A 1 288 ? 13.367  1.228   -8.269  1.00 21.57  ? 274 TYR A CD2 1 
ATOM   2090 C CE1 . TYR A 1 288 ? 14.051  0.982   -5.596  1.00 21.97  ? 274 TYR A CE1 1 
ATOM   2091 C CE2 . TYR A 1 288 ? 13.482  2.364   -7.484  1.00 23.14  ? 274 TYR A CE2 1 
ATOM   2092 C CZ  . TYR A 1 288 ? 13.860  2.232   -6.157  1.00 18.87  ? 274 TYR A CZ  1 
ATOM   2093 O OH  . TYR A 1 288 ? 13.991  3.380   -5.412  1.00 25.26  ? 274 TYR A OH  1 
ATOM   2094 N N   . PHE A 1 289 ? 14.867  -3.587  -10.818 1.00 20.56  ? 275 PHE A N   1 
ATOM   2095 C CA  . PHE A 1 289 ? 14.601  -4.933  -11.352 1.00 22.45  ? 275 PHE A CA  1 
ATOM   2096 C C   . PHE A 1 289 ? 15.855  -5.568  -11.947 1.00 23.86  ? 275 PHE A C   1 
ATOM   2097 O O   . PHE A 1 289 ? 16.713  -4.851  -12.463 1.00 26.22  ? 275 PHE A O   1 
ATOM   2098 C CB  . PHE A 1 289 ? 13.518  -4.894  -12.432 1.00 19.20  ? 275 PHE A CB  1 
ATOM   2099 C CG  . PHE A 1 289 ? 12.138  -4.770  -11.848 1.00 16.27  ? 275 PHE A CG  1 
ATOM   2100 C CD1 . PHE A 1 289 ? 11.479  -5.877  -11.281 1.00 17.91  ? 275 PHE A CD1 1 
ATOM   2101 C CD2 . PHE A 1 289 ? 11.473  -3.543  -11.847 1.00 15.77  ? 275 PHE A CD2 1 
ATOM   2102 C CE1 . PHE A 1 289 ? 10.211  -5.746  -10.699 1.00 16.36  ? 275 PHE A CE1 1 
ATOM   2103 C CE2 . PHE A 1 289 ? 10.230  -3.414  -11.231 1.00 18.43  ? 275 PHE A CE2 1 
ATOM   2104 C CZ  . PHE A 1 289 ? 9.584   -4.519  -10.694 1.00 18.62  ? 275 PHE A CZ  1 
ATOM   2105 N N   . ASP A 1 290 ? 15.943  -6.908  -11.859 1.00 21.11  ? 276 ASP A N   1 
ATOM   2106 C CA  . ASP A 1 290 ? 16.952  -7.705  -12.551 1.00 25.61  ? 276 ASP A CA  1 
ATOM   2107 C C   . ASP A 1 290 ? 16.307  -8.361  -13.773 1.00 23.11  ? 276 ASP A C   1 
ATOM   2108 O O   . ASP A 1 290 ? 15.527  -9.312  -13.647 1.00 22.22  ? 276 ASP A O   1 
ATOM   2109 C CB  . ASP A 1 290 ? 17.580  -8.719  -11.585 1.00 28.61  ? 276 ASP A CB  1 
ATOM   2110 C CG  . ASP A 1 290 ? 18.434  -9.762  -12.283 1.00 52.21  ? 276 ASP A CG  1 
ATOM   2111 O OD1 . ASP A 1 290 ? 19.245  -9.366  -13.156 1.00 72.85  ? 276 ASP A OD1 1 
ATOM   2112 O OD2 . ASP A 1 290 ? 18.288  -10.957 -11.949 1.00 73.47  ? 276 ASP A OD2 1 
ATOM   2113 N N   . ILE A 1 291 ? 16.601  -7.808  -14.955 1.00 22.98  ? 277 ILE A N   1 
ATOM   2114 C CA  . ILE A 1 291 ? 15.888  -8.164  -16.177 1.00 22.16  ? 277 ILE A CA  1 
ATOM   2115 C C   . ILE A 1 291 ? 16.896  -8.754  -17.156 1.00 25.78  ? 277 ILE A C   1 
ATOM   2116 O O   . ILE A 1 291 ? 17.722  -8.000  -17.655 1.00 28.01  ? 277 ILE A O   1 
ATOM   2117 C CB  . ILE A 1 291 ? 15.180  -6.935  -16.803 1.00 29.42  ? 277 ILE A CB  1 
ATOM   2118 C CG1 . ILE A 1 291 ? 14.306  -6.178  -15.800 1.00 35.73  ? 277 ILE A CG1 1 
ATOM   2119 C CG2 . ILE A 1 291 ? 14.389  -7.330  -18.046 1.00 29.48  ? 277 ILE A CG2 1 
ATOM   2120 C CD1 . ILE A 1 291 ? 14.029  -4.750  -16.199 1.00 53.87  ? 277 ILE A CD1 1 
ATOM   2121 N N   . PRO A 1 292 ? 16.826  -10.068 -17.478 1.00 32.31  ? 278 PRO A N   1 
ATOM   2122 C CA  . PRO A 1 292 ? 17.610  -10.640 -18.580 1.00 34.25  ? 278 PRO A CA  1 
ATOM   2123 C C   . PRO A 1 292 ? 17.327  -9.968  -19.923 1.00 49.93  ? 278 PRO A C   1 
ATOM   2124 O O   . PRO A 1 292 ? 16.213  -9.492  -20.165 1.00 37.48  ? 278 PRO A O   1 
ATOM   2125 C CB  . PRO A 1 292 ? 17.173  -12.116 -18.622 1.00 36.22  ? 278 PRO A CB  1 
ATOM   2126 C CG  . PRO A 1 292 ? 16.635  -12.401 -17.226 1.00 43.03  ? 278 PRO A CG  1 
ATOM   2127 C CD  . PRO A 1 292 ? 16.048  -11.085 -16.753 1.00 39.91  ? 278 PRO A CD  1 
ATOM   2128 N N   . LYS A 1 293 ? 18.371  -9.907  -20.764 1.00 48.28  ? 279 LYS A N   1 
ATOM   2129 C CA  . LYS A 1 293 ? 18.280  -9.483  -22.153 1.00 49.20  ? 279 LYS A CA  1 
ATOM   2130 C C   . LYS A 1 293 ? 17.314  -10.407 -22.894 1.00 40.29  ? 279 LYS A C   1 
ATOM   2131 O O   . LYS A 1 293 ? 17.266  -11.618 -22.643 1.00 35.64  ? 279 LYS A O   1 
ATOM   2132 C CB  . LYS A 1 293 ? 19.663  -9.497  -22.828 1.00 46.42  ? 279 LYS A CB  1 
ATOM   2133 N N   . ASP A 1 294 ? 16.558  -9.803  -23.819 1.00 28.15  ? 280 ASP A N   1 
ATOM   2134 C CA  . ASP A 1 294 ? 15.641  -10.487 -24.718 1.00 33.76  ? 280 ASP A CA  1 
ATOM   2135 C C   . ASP A 1 294 ? 14.483  -11.164 -23.973 1.00 32.32  ? 280 ASP A C   1 
ATOM   2136 O O   . ASP A 1 294 ? 13.825  -12.010 -24.575 1.00 36.71  ? 280 ASP A O   1 
ATOM   2137 C CB  . ASP A 1 294 ? 16.364  -11.463 -25.657 1.00 35.61  ? 280 ASP A CB  1 
ATOM   2138 N N   . LEU A 1 295 ? 14.230  -10.843 -22.684 1.00 23.71  ? 281 LEU A N   1 
ATOM   2139 C CA  . LEU A 1 295 ? 13.161  -11.549 -21.980 1.00 15.73  ? 281 LEU A CA  1 
ATOM   2140 C C   . LEU A 1 295 ? 11.802  -10.873 -22.240 1.00 19.42  ? 281 LEU A C   1 
ATOM   2141 O O   . LEU A 1 295 ? 10.813  -11.565 -22.501 1.00 19.72  ? 281 LEU A O   1 
ATOM   2142 C CB  . LEU A 1 295 ? 13.477  -11.625 -20.475 1.00 23.83  ? 281 LEU A CB  1 
ATOM   2143 C CG  . LEU A 1 295 ? 12.424  -12.313 -19.605 1.00 24.63  ? 281 LEU A CG  1 
ATOM   2144 C CD1 . LEU A 1 295 ? 12.346  -13.795 -19.934 1.00 22.98  ? 281 LEU A CD1 1 
ATOM   2145 C CD2 . LEU A 1 295 ? 12.717  -12.130 -18.131 1.00 27.20  ? 281 LEU A CD2 1 
ATOM   2146 N N   . LEU A 1 296 ? 11.750  -9.532  -22.145 1.00 19.33  ? 282 LEU A N   1 
ATOM   2147 C CA  . LEU A 1 296 ? 10.499  -8.794  -22.293 1.00 18.76  ? 282 LEU A CA  1 
ATOM   2148 C C   . LEU A 1 296 ? 10.161  -8.596  -23.775 1.00 23.08  ? 282 LEU A C   1 
ATOM   2149 O O   . LEU A 1 296 ? 11.039  -8.257  -24.584 1.00 26.78  ? 282 LEU A O   1 
ATOM   2150 C CB  . LEU A 1 296 ? 10.672  -7.425  -21.631 1.00 22.29  ? 282 LEU A CB  1 
ATOM   2151 C CG  . LEU A 1 296 ? 9.952   -7.163  -20.319 1.00 34.44  ? 282 LEU A CG  1 
ATOM   2152 C CD1 . LEU A 1 296 ? 10.131  -8.303  -19.349 1.00 30.33  ? 282 LEU A CD1 1 
ATOM   2153 C CD2 . LEU A 1 296 ? 10.439  -5.849  -19.718 1.00 30.01  ? 282 LEU A CD2 1 
ATOM   2154 N N   . ILE A 1 297 ? 8.884   -8.805  -24.111 1.00 18.22  ? 283 ILE A N   1 
ATOM   2155 C CA  . ILE A 1 297 ? 8.403   -8.571  -25.465 1.00 23.20  ? 283 ILE A CA  1 
ATOM   2156 C C   . ILE A 1 297 ? 7.183   -7.655  -25.400 1.00 23.28  ? 283 ILE A C   1 
ATOM   2157 O O   . ILE A 1 297 ? 6.455   -7.667  -24.392 1.00 21.56  ? 283 ILE A O   1 
ATOM   2158 C CB  . ILE A 1 297 ? 8.066   -9.879  -26.209 1.00 19.21  ? 283 ILE A CB  1 
ATOM   2159 C CG1 . ILE A 1 297 ? 6.976   -10.684 -25.505 1.00 20.44  ? 283 ILE A CG1 1 
ATOM   2160 C CG2 . ILE A 1 297 ? 9.324   -10.709 -26.469 1.00 23.30  ? 283 ILE A CG2 1 
ATOM   2161 C CD1 . ILE A 1 297 ? 6.485   -11.845 -26.295 1.00 16.30  ? 283 ILE A CD1 1 
ATOM   2162 N N   . PRO A 1 298 ? 6.920   -6.839  -26.455 1.00 23.62  ? 284 PRO A N   1 
ATOM   2163 C CA  . PRO A 1 298 ? 5.668   -6.080  -26.555 1.00 24.24  ? 284 PRO A CA  1 
ATOM   2164 C C   . PRO A 1 298 ? 4.438   -6.979  -26.678 1.00 23.25  ? 284 PRO A C   1 
ATOM   2165 O O   . PRO A 1 298 ? 4.492   -8.039  -27.286 1.00 22.88  ? 284 PRO A O   1 
ATOM   2166 C CB  . PRO A 1 298 ? 5.817   -5.240  -27.840 1.00 30.59  ? 284 PRO A CB  1 
ATOM   2167 C CG  . PRO A 1 298 ? 7.014   -5.802  -28.562 1.00 37.51  ? 284 PRO A CG  1 
ATOM   2168 C CD  . PRO A 1 298 ? 7.851   -6.566  -27.559 1.00 31.91  ? 284 PRO A CD  1 
ATOM   2169 N N   . ILE A 1 299 ? 3.321   -6.584  -26.052 1.00 28.91  ? 285 ILE A N   1 
ATOM   2170 C CA  . ILE A 1 299 ? 2.110   -7.403  -26.040 1.00 26.70  ? 285 ILE A CA  1 
ATOM   2171 C C   . ILE A 1 299 ? 1.647   -7.748  -27.463 1.00 24.82  ? 285 ILE A C   1 
ATOM   2172 O O   . ILE A 1 299 ? 1.023   -8.792  -27.663 1.00 27.77  ? 285 ILE A O   1 
ATOM   2173 C CB  . ILE A 1 299 ? 0.994   -6.748  -25.185 1.00 31.18  ? 285 ILE A CB  1 
ATOM   2174 C CG1 . ILE A 1 299 ? -0.178  -7.695  -24.894 1.00 28.17  ? 285 ILE A CG1 1 
ATOM   2175 C CG2 . ILE A 1 299 ? 0.529   -5.429  -25.796 1.00 32.34  ? 285 ILE A CG2 1 
ATOM   2176 C CD1 . ILE A 1 299 ? 0.085   -8.713  -23.791 1.00 28.65  ? 285 ILE A CD1 1 
ATOM   2177 N N   . ASN A 1 300 ? 1.921   -6.863  -28.443 1.00 30.53  ? 286 ASN A N   1 
ATOM   2178 C CA  . ASN A 1 300 ? 1.559   -7.075  -29.843 1.00 25.08  ? 286 ASN A CA  1 
ATOM   2179 C C   . ASN A 1 300 ? 2.325   -8.247  -30.460 1.00 33.73  ? 286 ASN A C   1 
ATOM   2180 O O   . ASN A 1 300 ? 1.892   -8.814  -31.465 1.00 45.16  ? 286 ASN A O   1 
ATOM   2181 C CB  . ASN A 1 300 ? 1.731   -5.812  -30.707 1.00 24.52  ? 286 ASN A CB  1 
ATOM   2182 C CG  . ASN A 1 300 ? 3.050   -5.099  -30.467 1.00 43.37  ? 286 ASN A CG  1 
ATOM   2183 N N   . GLU A 1 301 ? 3.469   -8.587  -29.867 1.00 28.26  ? 287 GLU A N   1 
ATOM   2184 C CA  . GLU A 1 301 ? 4.330   -9.629  -30.404 1.00 24.31  ? 287 GLU A CA  1 
ATOM   2185 C C   . GLU A 1 301 ? 4.006   -11.002 -29.807 1.00 23.30  ? 287 GLU A C   1 
ATOM   2186 O O   . GLU A 1 301 ? 4.484   -11.998 -30.333 1.00 31.57  ? 287 GLU A O   1 
ATOM   2187 C CB  . GLU A 1 301 ? 5.811   -9.277  -30.200 1.00 29.66  ? 287 GLU A CB  1 
ATOM   2188 C CG  . GLU A 1 301 ? 6.298   -8.151  -31.088 1.00 46.16  ? 287 GLU A CG  1 
ATOM   2189 C CD  . GLU A 1 301 ? 6.970   -8.587  -32.380 1.00 68.43  ? 287 GLU A CD  1 
ATOM   2190 O OE1 . GLU A 1 301 ? 7.118   -9.816  -32.598 1.00 61.13  ? 287 GLU A OE1 1 
ATOM   2191 O OE2 . GLU A 1 301 ? 7.385   -7.687  -33.156 1.00 94.05  ? 287 GLU A OE2 1 
ATOM   2192 N N   . VAL A 1 302 ? 3.187   -11.070 -28.748 1.00 22.50  ? 288 VAL A N   1 
ATOM   2193 C CA  . VAL A 1 302 ? 2.901   -12.325 -28.055 1.00 21.80  ? 288 VAL A CA  1 
ATOM   2194 C C   . VAL A 1 302 ? 2.350   -13.393 -29.007 1.00 19.48  ? 288 VAL A C   1 
ATOM   2195 O O   . VAL A 1 302 ? 2.688   -14.568 -28.887 1.00 25.41  ? 288 VAL A O   1 
ATOM   2196 C CB  . VAL A 1 302 ? 1.934   -12.096 -26.870 1.00 19.70  ? 288 VAL A CB  1 
ATOM   2197 C CG1 . VAL A 1 302 ? 1.317   -13.392 -26.351 1.00 28.13  ? 288 VAL A CG1 1 
ATOM   2198 C CG2 . VAL A 1 302 ? 2.629   -11.331 -25.741 1.00 23.76  ? 288 VAL A CG2 1 
ATOM   2199 N N   . GLU A 1 303 ? 1.444   -13.022 -29.924 1.00 23.75  ? 289 GLU A N   1 
ATOM   2200 C CA  . GLU A 1 303 ? 0.808   -14.044 -30.759 1.00 22.91  ? 289 GLU A CA  1 
ATOM   2201 C C   . GLU A 1 303 ? 1.779   -14.615 -31.807 1.00 26.43  ? 289 GLU A C   1 
ATOM   2202 O O   . GLU A 1 303 ? 1.397   -15.541 -32.510 1.00 27.69  ? 289 GLU A O   1 
ATOM   2203 C CB  . GLU A 1 303 ? -0.496  -13.584 -31.424 1.00 31.57  ? 289 GLU A CB  1 
ATOM   2204 C CG  . GLU A 1 303 ? -0.261  -12.569 -32.534 1.00 35.53  ? 289 GLU A CG  1 
ATOM   2205 C CD  . GLU A 1 303 ? -1.362  -12.292 -33.553 1.00 52.17  ? 289 GLU A CD  1 
ATOM   2206 O OE1 . GLU A 1 303 ? -2.447  -12.925 -33.508 1.00 45.78  ? 289 GLU A OE1 1 
ATOM   2207 O OE2 . GLU A 1 303 ? -1.110  -11.452 -34.424 1.00 47.30  ? 289 GLU A OE2 1 
ATOM   2208 N N   . ASN A 1 304 ? 3.025   -14.110 -31.892 1.00 27.21  ? 290 ASN A N   1 
ATOM   2209 C CA  . ASN A 1 304 ? 4.043   -14.577 -32.834 1.00 27.34  ? 290 ASN A CA  1 
ATOM   2210 C C   . ASN A 1 304 ? 4.940   -15.669 -32.242 1.00 33.85  ? 290 ASN A C   1 
ATOM   2211 O O   . ASN A 1 304 ? 5.872   -16.125 -32.900 1.00 49.67  ? 290 ASN A O   1 
ATOM   2212 C CB  . ASN A 1 304 ? 4.907   -13.407 -33.312 1.00 25.77  ? 290 ASN A CB  1 
ATOM   2213 C CG  . ASN A 1 304 ? 4.074   -12.406 -34.080 1.00 28.56  ? 290 ASN A CG  1 
ATOM   2214 O OD1 . ASN A 1 304 ? 3.097   -12.790 -34.730 1.00 38.18  ? 290 ASN A OD1 1 
ATOM   2215 N ND2 . ASN A 1 304 ? 4.450   -11.137 -34.004 1.00 35.62  ? 290 ASN A ND2 1 
ATOM   2216 N N   . TYR A 1 305 ? 4.650   -16.074 -31.004 1.00 24.36  ? 291 TYR A N   1 
ATOM   2217 C CA  . TYR A 1 305 ? 5.379   -17.131 -30.320 1.00 21.35  ? 291 TYR A CA  1 
ATOM   2218 C C   . TYR A 1 305 ? 4.461   -18.332 -30.088 1.00 21.26  ? 291 TYR A C   1 
ATOM   2219 O O   . TYR A 1 305 ? 3.232   -18.191 -30.001 1.00 25.29  ? 291 TYR A O   1 
ATOM   2220 C CB  . TYR A 1 305 ? 5.922   -16.631 -28.977 1.00 22.90  ? 291 TYR A CB  1 
ATOM   2221 C CG  . TYR A 1 305 ? 7.024   -15.608 -29.075 1.00 25.02  ? 291 TYR A CG  1 
ATOM   2222 C CD1 . TYR A 1 305 ? 6.737   -14.269 -29.331 1.00 28.58  ? 291 TYR A CD1 1 
ATOM   2223 C CD2 . TYR A 1 305 ? 8.356   -15.976 -28.944 1.00 24.80  ? 291 TYR A CD2 1 
ATOM   2224 C CE1 . TYR A 1 305 ? 7.742   -13.325 -29.445 1.00 32.10  ? 291 TYR A CE1 1 
ATOM   2225 C CE2 . TYR A 1 305 ? 9.373   -15.036 -29.054 1.00 23.25  ? 291 TYR A CE2 1 
ATOM   2226 C CZ  . TYR A 1 305 ? 9.066   -13.710 -29.312 1.00 27.48  ? 291 TYR A CZ  1 
ATOM   2227 O OH  . TYR A 1 305 ? 10.057  -12.763 -29.408 1.00 47.83  ? 291 TYR A OH  1 
ATOM   2228 N N   . PRO A 1 306 ? 5.032   -19.555 -29.978 1.00 20.95  ? 292 PRO A N   1 
ATOM   2229 C CA  . PRO A 1 306 ? 4.301   -20.717 -29.472 1.00 24.28  ? 292 PRO A CA  1 
ATOM   2230 C C   . PRO A 1 306 ? 3.681   -20.353 -28.117 1.00 19.76  ? 292 PRO A C   1 
ATOM   2231 O O   . PRO A 1 306 ? 4.248   -19.571 -27.315 1.00 20.36  ? 292 PRO A O   1 
ATOM   2232 C CB  . PRO A 1 306 ? 5.379   -21.817 -29.314 1.00 21.50  ? 292 PRO A CB  1 
ATOM   2233 C CG  . PRO A 1 306 ? 6.509   -21.395 -30.252 1.00 20.57  ? 292 PRO A CG  1 
ATOM   2234 C CD  . PRO A 1 306 ? 6.440   -19.874 -30.317 1.00 22.15  ? 292 PRO A CD  1 
ATOM   2235 N N   . LYS A 1 307 ? 2.512   -20.950 -27.857 1.00 19.75  ? 293 LYS A N   1 
ATOM   2236 C CA  . LYS A 1 307 ? 1.764   -20.624 -26.644 1.00 15.82  ? 293 LYS A CA  1 
ATOM   2237 C C   . LYS A 1 307 ? 2.572   -20.953 -25.395 1.00 17.42  ? 293 LYS A C   1 
ATOM   2238 O O   . LYS A 1 307 ? 2.452   -20.236 -24.395 1.00 18.63  ? 293 LYS A O   1 
ATOM   2239 C CB  . LYS A 1 307 ? 0.453   -21.423 -26.644 1.00 20.17  ? 293 LYS A CB  1 
ATOM   2240 C CG  . LYS A 1 307 ? -0.517  -20.959 -27.731 1.00 25.05  ? 293 LYS A CG  1 
ATOM   2241 C CD  . LYS A 1 307 ? -1.847  -21.634 -27.658 1.00 33.48  ? 293 LYS A CD  1 
ATOM   2242 C CE  . LYS A 1 307 ? -2.856  -21.092 -28.647 1.00 44.40  ? 293 LYS A CE  1 
ATOM   2243 N NZ  . LYS A 1 307 ? -4.006  -22.027 -28.739 1.00 55.70  ? 293 LYS A NZ  1 
ATOM   2244 N N   . ASN A 1 308 ? 3.380   -22.014 -25.474 1.00 19.26  ? 294 ASN A N   1 
ATOM   2245 C CA  . ASN A 1 308 ? 4.146   -22.463 -24.315 1.00 20.73  ? 294 ASN A CA  1 
ATOM   2246 C C   . ASN A 1 308 ? 5.423   -21.641 -24.128 1.00 20.13  ? 294 ASN A C   1 
ATOM   2247 O O   . ASN A 1 308 ? 6.193   -21.927 -23.197 1.00 20.64  ? 294 ASN A O   1 
ATOM   2248 C CB  . ASN A 1 308 ? 4.422   -23.977 -24.349 1.00 21.68  ? 294 ASN A CB  1 
ATOM   2249 C CG  . ASN A 1 308 ? 5.373   -24.407 -25.462 1.00 25.85  ? 294 ASN A CG  1 
ATOM   2250 O OD1 . ASN A 1 308 ? 6.006   -23.594 -26.145 1.00 27.36  ? 294 ASN A OD1 1 
ATOM   2251 N ND2 . ASN A 1 308 ? 5.451   -25.711 -25.676 1.00 30.05  ? 294 ASN A ND2 1 
ATOM   2252 N N   . GLU A 1 309 ? 5.591   -20.552 -24.892 1.00 16.51  ? 295 GLU A N   1 
ATOM   2253 C CA  . GLU A 1 309 ? 6.766   -19.717 -24.742 1.00 15.74  ? 295 GLU A CA  1 
ATOM   2254 C C   . GLU A 1 309 ? 6.432   -18.313 -24.245 1.00 16.26  ? 295 GLU A C   1 
ATOM   2255 O O   . GLU A 1 309 ? 7.319   -17.449 -24.332 1.00 16.54  ? 295 GLU A O   1 
ATOM   2256 C CB  . GLU A 1 309 ? 7.533   -19.636 -26.065 1.00 20.62  ? 295 GLU A CB  1 
ATOM   2257 C CG  . GLU A 1 309 ? 8.224   -20.964 -26.408 1.00 27.11  ? 295 GLU A CG  1 
ATOM   2258 C CD  . GLU A 1 309 ? 9.119   -20.948 -27.636 1.00 39.70  ? 295 GLU A CD  1 
ATOM   2259 O OE1 . GLU A 1 309 ? 9.505   -19.834 -28.062 1.00 31.39  ? 295 GLU A OE1 1 
ATOM   2260 O OE2 . GLU A 1 309 ? 9.391   -22.049 -28.170 1.00 52.20  ? 295 GLU A OE2 1 
ATOM   2261 N N   . VAL A 1 310 ? 5.225   -18.114 -23.655 1.00 16.40  ? 296 VAL A N   1 
ATOM   2262 C CA  . VAL A 1 310 ? 4.829   -16.778 -23.219 1.00 20.76  ? 296 VAL A CA  1 
ATOM   2263 C C   . VAL A 1 310 ? 4.202   -16.807 -21.826 1.00 15.96  ? 296 VAL A C   1 
ATOM   2264 O O   . VAL A 1 310 ? 3.419   -17.692 -21.496 1.00 15.72  ? 296 VAL A O   1 
ATOM   2265 C CB  . VAL A 1 310 ? 3.888   -16.110 -24.256 1.00 23.83  ? 296 VAL A CB  1 
ATOM   2266 C CG1 . VAL A 1 310 ? 4.568   -15.919 -25.623 1.00 27.85  ? 296 VAL A CG1 1 
ATOM   2267 C CG2 . VAL A 1 310 ? 2.567   -16.869 -24.432 1.00 28.74  ? 296 VAL A CG2 1 
ATOM   2268 N N   . ILE A 1 311 ? 4.566   -15.785 -21.040 1.00 16.60  ? 297 ILE A N   1 
ATOM   2269 C CA  . ILE A 1 311 ? 3.840   -15.408 -19.834 1.00 13.79  ? 297 ILE A CA  1 
ATOM   2270 C C   . ILE A 1 311 ? 3.361   -13.975 -20.000 1.00 14.88  ? 297 ILE A C   1 
ATOM   2271 O O   . ILE A 1 311 ? 4.156   -13.101 -20.269 1.00 18.57  ? 297 ILE A O   1 
ATOM   2272 C CB  . ILE A 1 311 ? 4.724   -15.517 -18.581 1.00 14.00  ? 297 ILE A CB  1 
ATOM   2273 C CG1 . ILE A 1 311 ? 5.367   -16.897 -18.467 1.00 14.13  ? 297 ILE A CG1 1 
ATOM   2274 C CG2 . ILE A 1 311 ? 3.889   -15.184 -17.345 1.00 16.21  ? 297 ILE A CG2 1 
ATOM   2275 C CD1 . ILE A 1 311 ? 6.219   -17.083 -17.173 1.00 18.81  ? 297 ILE A CD1 1 
ATOM   2276 N N   . ILE A 1 312 ? 2.065   -13.761 -19.756 1.00 14.50  ? 298 ILE A N   1 
ATOM   2277 C CA  . ILE A 1 312 ? 1.476   -12.424 -19.780 1.00 15.31  ? 298 ILE A CA  1 
ATOM   2278 C C   . ILE A 1 312 ? 1.243   -12.033 -18.321 1.00 13.50  ? 298 ILE A C   1 
ATOM   2279 O O   . ILE A 1 312 ? 0.554   -12.762 -17.626 1.00 14.96  ? 298 ILE A O   1 
ATOM   2280 C CB  . ILE A 1 312 ? 0.143   -12.441 -20.573 1.00 17.95  ? 298 ILE A CB  1 
ATOM   2281 C CG1 . ILE A 1 312 ? 0.354   -12.764 -22.068 1.00 18.00  ? 298 ILE A CG1 1 
ATOM   2282 C CG2 . ILE A 1 312 ? -0.587  -11.111 -20.428 1.00 18.65  ? 298 ILE A CG2 1 
ATOM   2283 C CD1 . ILE A 1 312 ? 0.472   -14.203 -22.399 1.00 29.88  ? 298 ILE A CD1 1 
ATOM   2284 N N   . ILE A 1 313 ? 1.777   -10.891 -17.903 1.00 14.58  ? 299 ILE A N   1 
ATOM   2285 C CA  . ILE A 1 313 ? 1.433   -10.351 -16.593 1.00 12.29  ? 299 ILE A CA  1 
ATOM   2286 C C   . ILE A 1 313 ? 0.343   -9.319  -16.837 1.00 13.58  ? 299 ILE A C   1 
ATOM   2287 O O   . ILE A 1 313 ? 0.597   -8.308  -17.506 1.00 13.77  ? 299 ILE A O   1 
ATOM   2288 C CB  . ILE A 1 313 ? 2.682   -9.743  -15.904 1.00 12.80  ? 299 ILE A CB  1 
ATOM   2289 C CG1 . ILE A 1 313 ? 3.802   -10.780 -15.786 1.00 14.43  ? 299 ILE A CG1 1 
ATOM   2290 C CG2 . ILE A 1 313 ? 2.326   -9.140  -14.546 1.00 15.49  ? 299 ILE A CG2 1 
ATOM   2291 C CD1 . ILE A 1 313 ? 5.053   -10.222 -15.162 1.00 16.80  ? 299 ILE A CD1 1 
ATOM   2292 N N   . ALA A 1 314 ? -0.836  -9.593  -16.256 1.00 14.84  ? 300 ALA A N   1 
ATOM   2293 C CA  . ALA A 1 314 ? -2.029  -8.799  -16.525 1.00 15.48  ? 300 ALA A CA  1 
ATOM   2294 C C   . ALA A 1 314 ? -2.405  -8.065  -15.243 1.00 14.41  ? 300 ALA A C   1 
ATOM   2295 O O   . ALA A 1 314 ? -2.843  -8.656  -14.272 1.00 16.36  ? 300 ALA A O   1 
ATOM   2296 C CB  . ALA A 1 314 ? -3.168  -9.681  -16.964 1.00 15.66  ? 300 ALA A CB  1 
ATOM   2297 N N   . THR A 1 315 ? -2.155  -6.782  -15.269 1.00 21.46  ? 301 THR A N   1 
ATOM   2298 C CA  . THR A 1 315 ? -2.565  -5.930  -14.144 1.00 37.40  ? 301 THR A CA  1 
ATOM   2299 C C   . THR A 1 315 ? -3.763  -5.169  -14.707 1.00 67.60  ? 301 THR A C   1 
ATOM   2300 O O   . THR A 1 315 ? -4.022  -5.244  -15.911 1.00 50.18  ? 301 THR A O   1 
ATOM   2301 C CB  . THR A 1 315 ? -1.362  -5.103  -13.695 1.00 26.10  ? 301 THR A CB  1 
ATOM   2302 O OG1 . THR A 1 315 ? -1.102  -4.166  -14.737 1.00 32.86  ? 301 THR A OG1 1 
ATOM   2303 C CG2 . THR A 1 315 ? -0.125  -5.940  -13.452 1.00 33.16  ? 301 THR A CG2 1 
ATOM   2304 N N   . GLY A 1 316 ? -4.455  -4.417  -13.886 1.00 111.94 ? 302 GLY A N   1 
ATOM   2305 C CA  . GLY A 1 316 ? -5.616  -3.755  -14.482 1.00 117.46 ? 302 GLY A CA  1 
ATOM   2306 C C   . GLY A 1 316 ? -5.217  -2.472  -15.172 1.00 193.34 ? 302 GLY A C   1 
ATOM   2307 O O   . GLY A 1 316 ? -4.024  -2.141  -15.173 1.00 104.09 ? 302 GLY A O   1 
ATOM   2308 N N   . MET A 1 317 ? -6.179  -1.819  -15.794 1.00 175.48 ? 303 MET A N   1 
ATOM   2309 C CA  . MET A 1 317 ? -5.909  -0.539  -16.489 1.00 137.24 ? 303 MET A CA  1 
ATOM   2310 C C   . MET A 1 317 ? -5.599  0.488   -15.415 1.00 303.99 ? 303 MET A C   1 
ATOM   2311 O O   . MET A 1 317 ? -4.664  1.285   -15.577 1.00 160.70 ? 303 MET A O   1 
ATOM   2312 C CB  . MET A 1 317 ? -7.157  -0.068  -17.234 1.00 150.06 ? 303 MET A CB  1 
ATOM   2313 N N   . GLN A 1 318 ? -6.374  0.428   -14.346 1.00 273.56 ? 304 GLN A N   1 
ATOM   2314 C CA  . GLN A 1 318 ? -6.177  1.384   -13.239 1.00 233.17 ? 304 GLN A CA  1 
ATOM   2315 C C   . GLN A 1 318 ? -5.365  0.704   -12.148 1.00 246.16 ? 304 GLN A C   1 
ATOM   2316 O O   . GLN A 1 318 ? -5.114  1.333   -11.122 1.00 237.69 ? 304 GLN A O   1 
ATOM   2317 C CB  . GLN A 1 318 ? -7.567  1.812   -12.770 1.00 172.27 ? 304 GLN A CB  1 
ATOM   2318 N N   . GLY A 1 319 ? -4.973  -0.549  -12.384 1.00 210.16 ? 305 GLY A N   1 
ATOM   2319 C CA  . GLY A 1 319 ? -4.169  -1.285  -11.401 1.00 216.83 ? 305 GLY A CA  1 
ATOM   2320 C C   . GLY A 1 319 ? -4.956  -2.391  -10.708 1.00 273.90 ? 305 GLY A C   1 
ATOM   2321 O O   . GLY A 1 319 ? -4.355  -3.079  -9.898  1.00 261.45 ? 305 GLY A O   1 
ATOM   2322 N N   . GLU A 1 320 ? -6.249  -2.531  -11.027 1.00 273.71 ? 306 GLU A N   1 
ATOM   2323 C CA  . GLU A 1 320 ? -7.092  -3.608  -10.414 1.00 573.39 ? 306 GLU A CA  1 
ATOM   2324 C C   . GLU A 1 320 ? -6.997  -4.870  -11.287 1.00 41.96  ? 306 GLU A C   1 
ATOM   2325 O O   . GLU A 1 320 ? -7.662  -4.896  -12.328 1.00 44.60  ? 306 GLU A O   1 
ATOM   2326 C CB  . GLU A 1 320 ? -8.527  -3.113  -10.249 1.00 123.39 ? 306 GLU A CB  1 
ATOM   2327 C CG  . GLU A 1 320 ? -9.286  -3.892  -9.186  1.00 124.05 ? 306 GLU A CG  1 
ATOM   2328 C CD  . GLU A 1 320 ? -9.467  -5.380  -9.450  1.00 130.30 ? 306 GLU A CD  1 
ATOM   2329 O OE1 . GLU A 1 320 ? -8.717  -6.189  -8.872  1.00 89.72  ? 306 GLU A OE1 1 
ATOM   2330 O OE2 . GLU A 1 320 ? -10.374 -5.720  -10.222 1.00 155.57 ? 306 GLU A OE2 1 
ATOM   2331 N N   . PRO A 1 321 ? -6.293  -5.937  -10.874 1.00 20.22  ? 307 PRO A N   1 
ATOM   2332 C CA  . PRO A 1 321 ? -6.042  -7.066  -11.784 1.00 16.61  ? 307 PRO A CA  1 
ATOM   2333 C C   . PRO A 1 321 ? -7.288  -7.895  -12.108 1.00 15.99  ? 307 PRO A C   1 
ATOM   2334 O O   . PRO A 1 321 ? -7.446  -8.360  -13.230 1.00 14.96  ? 307 PRO A O   1 
ATOM   2335 C CB  . PRO A 1 321 ? -5.017  -7.948  -11.055 1.00 19.30  ? 307 PRO A CB  1 
ATOM   2336 C CG  . PRO A 1 321 ? -5.196  -7.568  -9.587  1.00 27.56  ? 307 PRO A CG  1 
ATOM   2337 C CD  . PRO A 1 321 ? -5.645  -6.117  -9.567  1.00 22.91  ? 307 PRO A CD  1 
ATOM   2338 N N   . VAL A 1 322 ? -8.203  -8.078  -11.148 1.00 14.75  ? 308 VAL A N   1 
ATOM   2339 C CA  . VAL A 1 322 ? -9.352  -8.955  -11.382 1.00 16.45  ? 308 VAL A CA  1 
ATOM   2340 C C   . VAL A 1 322 ? -10.297 -8.451  -12.480 1.00 16.08  ? 308 VAL A C   1 
ATOM   2341 O O   . VAL A 1 322 ? -10.776 -9.254  -13.288 1.00 16.48  ? 308 VAL A O   1 
ATOM   2342 C CB  . VAL A 1 322 ? -10.083 -9.239  -10.062 1.00 17.00  ? 308 VAL A CB  1 
ATOM   2343 C CG1 . VAL A 1 322 ? -11.242 -10.200 -10.277 1.00 19.94  ? 308 VAL A CG1 1 
ATOM   2344 C CG2 . VAL A 1 322 ? -9.109  -9.847  -9.075  1.00 23.04  ? 308 VAL A CG2 1 
ATOM   2345 N N   . GLU A 1 323 ? -10.527 -7.147  -12.549 1.00 18.92  ? 309 GLU A N   1 
ATOM   2346 C CA  . GLU A 1 323 ? -11.369 -6.560  -13.573 1.00 22.24  ? 309 GLU A CA  1 
ATOM   2347 C C   . GLU A 1 323 ? -10.797 -6.913  -14.945 1.00 19.72  ? 309 GLU A C   1 
ATOM   2348 O O   . GLU A 1 323 ? -11.559 -7.258  -15.844 1.00 18.33  ? 309 GLU A O   1 
ATOM   2349 C CB  . GLU A 1 323 ? -11.388 -5.042  -13.361 1.00 34.10  ? 309 GLU A CB  1 
ATOM   2350 C CG  . GLU A 1 323 ? -11.842 -4.213  -14.551 1.00 47.29  ? 309 GLU A CG  1 
ATOM   2351 C CD  . GLU A 1 323 ? -10.797 -3.568  -15.461 1.00 53.88  ? 309 GLU A CD  1 
ATOM   2352 O OE1 . GLU A 1 323 ? -11.186 -3.136  -16.546 1.00 72.68  ? 309 GLU A OE1 1 
ATOM   2353 O OE2 . GLU A 1 323 ? -9.612  -3.429  -15.082 1.00 46.26  ? 309 GLU A OE2 1 
ATOM   2354 N N   . ALA A 1 324 ? -9.464  -6.770  -15.116 1.00 16.65  ? 310 ALA A N   1 
ATOM   2355 C CA  . ALA A 1 324 ? -8.858  -7.084  -16.401 1.00 15.59  ? 310 ALA A CA  1 
ATOM   2356 C C   . ALA A 1 324 ? -9.043  -8.565  -16.723 1.00 14.17  ? 310 ALA A C   1 
ATOM   2357 O O   . ALA A 1 324 ? -9.362  -8.919  -17.867 1.00 15.17  ? 310 ALA A O   1 
ATOM   2358 C CB  . ALA A 1 324 ? -7.395  -6.694  -16.386 1.00 18.07  ? 310 ALA A CB  1 
ATOM   2359 N N   . LEU A 1 325 ? -8.867  -9.433  -15.728 1.00 12.71  ? 311 LEU A N   1 
ATOM   2360 C CA  . LEU A 1 325 ? -9.023  -10.908 -15.909 1.00 12.11  ? 311 LEU A CA  1 
ATOM   2361 C C   . LEU A 1 325 ? -10.468 -11.246 -16.305 1.00 12.53  ? 311 LEU A C   1 
ATOM   2362 O O   . LEU A 1 325 ? -10.660 -12.086 -17.161 1.00 12.93  ? 311 LEU A O   1 
ATOM   2363 C CB  . LEU A 1 325 ? -8.631  -11.590 -14.593 1.00 14.74  ? 311 LEU A CB  1 
ATOM   2364 C CG  . LEU A 1 325 ? -8.402  -13.094 -14.662 1.00 29.26  ? 311 LEU A CG  1 
ATOM   2365 C CD1 . LEU A 1 325 ? -7.293  -13.430 -15.642 1.00 18.16  ? 311 LEU A CD1 1 
ATOM   2366 C CD2 . LEU A 1 325 ? -8.056  -13.621 -13.280 1.00 18.62  ? 311 LEU A CD2 1 
ATOM   2367 N N   . SER A 1 326 ? -11.424 -10.572 -15.690 1.00 12.66  ? 312 SER A N   1 
ATOM   2368 C CA  . SER A 1 326 ? -12.827 -10.751 -16.034 1.00 14.74  ? 312 SER A CA  1 
ATOM   2369 C C   . SER A 1 326 ? -13.083 -10.354 -17.481 1.00 14.00  ? 312 SER A C   1 
ATOM   2370 O O   . SER A 1 326 ? -13.697 -11.123 -18.229 1.00 15.96  ? 312 SER A O   1 
ATOM   2371 C CB  . SER A 1 326 ? -13.680 -9.973  -15.108 1.00 16.83  ? 312 SER A CB  1 
ATOM   2372 O OG  . SER A 1 326 ? -15.028 -10.152 -15.545 1.00 20.37  ? 312 SER A OG  1 
ATOM   2373 N N   . GLN A 1 327 ? -12.526 -9.204  -17.886 1.00 11.87  ? 313 GLN A N   1 
ATOM   2374 C CA  . GLN A 1 327 ? -12.661 -8.828  -19.292 1.00 13.83  ? 313 GLN A CA  1 
ATOM   2375 C C   . GLN A 1 327 ? -12.085 -9.891  -20.230 1.00 11.84  ? 313 GLN A C   1 
ATOM   2376 O O   . GLN A 1 327 ? -12.693 -10.252 -21.249 1.00 12.87  ? 313 GLN A O   1 
ATOM   2377 C CB  . GLN A 1 327 ? -11.978 -7.493  -19.584 1.00 14.37  ? 313 GLN A CB  1 
ATOM   2378 C CG  . GLN A 1 327 ? -12.629 -6.328  -18.836 1.00 18.15  ? 313 GLN A CG  1 
ATOM   2379 C CD  . GLN A 1 327 ? -11.921 -5.028  -19.089 1.00 26.84  ? 313 GLN A CD  1 
ATOM   2380 O OE1 . GLN A 1 327 ? -10.985 -4.957  -19.874 1.00 37.35  ? 313 GLN A OE1 1 
ATOM   2381 N NE2 . GLN A 1 327 ? -12.426 -3.964  -18.481 1.00 40.27  ? 313 GLN A NE2 1 
ATOM   2382 N N   . MET A 1 328 ? -10.866 -10.358 -19.928 1.00 11.22  ? 314 MET A N   1 
ATOM   2383 C CA  . MET A 1 328 ? -10.228 -11.358 -20.770 1.00 11.75  ? 314 MET A CA  1 
ATOM   2384 C C   . MET A 1 328 ? -11.036 -12.659 -20.810 1.00 12.96  ? 314 MET A C   1 
ATOM   2385 O O   . MET A 1 328 ? -11.166 -13.314 -21.857 1.00 13.62  ? 314 MET A O   1 
ATOM   2386 C CB  . MET A 1 328 ? -8.819  -11.706 -20.256 1.00 11.88  ? 314 MET A CB  1 
ATOM   2387 C CG  . MET A 1 328 ? -7.865  -10.557 -20.287 1.00 12.83  ? 314 MET A CG  1 
ATOM   2388 S SD  . MET A 1 328 ? -6.230  -10.984 -19.522 1.00 19.18  ? 314 MET A SD  1 
ATOM   2389 C CE  . MET A 1 328 ? -5.477  -11.775 -20.941 1.00 20.21  ? 314 MET A CE  1 
ATOM   2390 N N   . ALA A 1 329 ? -11.595 -13.059 -19.665 1.00 12.69  ? 315 ALA A N   1 
ATOM   2391 C CA  . ALA A 1 329 ? -12.353 -14.302 -19.584 1.00 12.65  ? 315 ALA A CA  1 
ATOM   2392 C C   . ALA A 1 329 ? -13.635 -14.235 -20.430 1.00 14.69  ? 315 ALA A C   1 
ATOM   2393 O O   . ALA A 1 329 ? -14.050 -15.233 -21.026 1.00 16.82  ? 315 ALA A O   1 
ATOM   2394 C CB  . ALA A 1 329 ? -12.762 -14.565 -18.158 1.00 15.34  ? 315 ALA A CB  1 
ATOM   2395 N N   . ARG A 1 330 ? -14.254 -13.071 -20.472 1.00 15.09  ? 316 ARG A N   1 
ATOM   2396 C CA  . ARG A 1 330 ? -15.505 -12.886 -21.251 1.00 14.73  ? 316 ARG A CA  1 
ATOM   2397 C C   . ARG A 1 330 ? -15.173 -12.487 -22.696 1.00 13.08  ? 316 ARG A C   1 
ATOM   2398 O O   . ARG A 1 330 ? -16.115 -12.286 -23.448 1.00 15.89  ? 316 ARG A O   1 
ATOM   2399 C CB  . ARG A 1 330 ? -16.338 -11.818 -20.555 1.00 15.34  ? 316 ARG A CB  1 
ATOM   2400 C CG  . ARG A 1 330 ? -16.993 -12.353 -19.291 1.00 19.40  ? 316 ARG A CG  1 
ATOM   2401 C CD  . ARG A 1 330 ? -17.704 -11.293 -18.494 1.00 22.86  ? 316 ARG A CD  1 
ATOM   2402 N NE  . ARG A 1 330 ? -16.796 -10.252 -18.064 1.00 67.23  ? 316 ARG A NE  1 
ATOM   2403 C CZ  . ARG A 1 330 ? -16.889 -8.986  -18.436 1.00 56.68  ? 316 ARG A CZ  1 
ATOM   2404 N NH1 . ARG A 1 330 ? -17.851 -8.610  -19.261 1.00 55.88  ? 316 ARG A NH1 1 
ATOM   2405 N NH2 . ARG A 1 330 ? -16.022 -8.102  -17.983 1.00 59.75  ? 316 ARG A NH2 1 
ATOM   2406 N N   . LYS A 1 331 ? -13.895 -12.381 -23.050 1.00 13.85  ? 317 LYS A N   1 
ATOM   2407 C CA  . LYS A 1 331 ? -13.429 -12.065 -24.409 1.00 14.33  ? 317 LYS A CA  1 
ATOM   2408 C C   . LYS A 1 331 ? -13.848 -10.633 -24.795 1.00 12.11  ? 317 LYS A C   1 
ATOM   2409 O O   . LYS A 1 331 ? -14.124 -10.331 -25.976 1.00 15.93  ? 317 LYS A O   1 
ATOM   2410 C CB  . LYS A 1 331 ? -13.955 -13.131 -25.382 1.00 15.12  ? 317 LYS A CB  1 
ATOM   2411 C CG  . LYS A 1 331 ? -13.421 -14.527 -25.058 1.00 19.59  ? 317 LYS A CG  1 
ATOM   2412 C CD  . LYS A 1 331 ? -13.933 -15.638 -26.006 1.00 22.88  ? 317 LYS A CD  1 
ATOM   2413 C CE  . LYS A 1 331 ? -13.374 -17.004 -25.645 1.00 24.75  ? 317 LYS A CE  1 
ATOM   2414 N NZ  . LYS A 1 331 ? -13.896 -17.403 -24.326 1.00 33.12  ? 317 LYS A NZ  1 
ATOM   2415 N N   . LYS A 1 332 ? -13.848 -9.724  -23.809 1.00 14.51  ? 318 LYS A N   1 
ATOM   2416 C CA  . LYS A 1 332 ? -14.238 -8.327  -23.939 1.00 16.18  ? 318 LYS A CA  1 
ATOM   2417 C C   . LYS A 1 332 ? -13.029 -7.412  -23.841 1.00 17.10  ? 318 LYS A C   1 
ATOM   2418 O O   . LYS A 1 332 ? -13.144 -6.183  -23.900 1.00 23.04  ? 318 LYS A O   1 
ATOM   2419 C CB  . LYS A 1 332 ? -15.236 -7.916  -22.836 1.00 20.37  ? 318 LYS A CB  1 
ATOM   2420 N N   . HIS A 1 333 ? -11.843 -7.984  -23.584 1.00 14.63  ? 319 HIS A N   1 
ATOM   2421 C CA  . HIS A 1 333 ? -10.671 -7.148  -23.433 1.00 16.86  ? 319 HIS A CA  1 
ATOM   2422 C C   . HIS A 1 333 ? -10.280 -6.549  -24.792 1.00 18.91  ? 319 HIS A C   1 
ATOM   2423 O O   . HIS A 1 333 ? -10.351 -7.215  -25.836 1.00 19.40  ? 319 HIS A O   1 
ATOM   2424 C CB  . HIS A 1 333 ? -9.537  -7.945  -22.788 1.00 14.60  ? 319 HIS A CB  1 
ATOM   2425 C CG  . HIS A 1 333 ? -8.445  -7.071  -22.240 1.00 14.13  ? 319 HIS A CG  1 
ATOM   2426 N ND1 . HIS A 1 333 ? -7.476  -6.416  -22.997 1.00 17.20  ? 319 HIS A ND1 1 
ATOM   2427 C CD2 . HIS A 1 333 ? -8.208  -6.724  -20.944 1.00 19.73  ? 319 HIS A CD2 1 
ATOM   2428 C CE1 . HIS A 1 333 ? -6.682  -5.724  -22.186 1.00 18.53  ? 319 HIS A CE1 1 
ATOM   2429 N NE2 . HIS A 1 333 ? -7.131  -5.888  -20.914 1.00 20.73  ? 319 HIS A NE2 1 
ATOM   2430 N N   . LYS A 1 334 ? -9.882  -5.274  -24.754 1.00 21.27  ? 320 LYS A N   1 
ATOM   2431 C CA  . LYS A 1 334 ? -9.523  -4.550  -25.975 1.00 24.49  ? 320 LYS A CA  1 
ATOM   2432 C C   . LYS A 1 334 ? -8.268  -5.111  -26.649 1.00 26.52  ? 320 LYS A C   1 
ATOM   2433 O O   . LYS A 1 334 ? -8.122  -5.017  -27.865 1.00 28.92  ? 320 LYS A O   1 
ATOM   2434 C CB  . LYS A 1 334 ? -9.331  -3.049  -25.711 1.00 28.98  ? 320 LYS A CB  1 
ATOM   2435 N N   . ILE A 1 335 ? -7.335  -5.645  -25.859 1.00 22.89  ? 321 ILE A N   1 
ATOM   2436 C CA  . ILE A 1 335 ? -5.995  -5.916  -26.360 1.00 22.81  ? 321 ILE A CA  1 
ATOM   2437 C C   . ILE A 1 335 ? -5.782  -7.424  -26.493 1.00 17.69  ? 321 ILE A C   1 
ATOM   2438 O O   . ILE A 1 335 ? -5.274  -7.897  -27.498 1.00 22.70  ? 321 ILE A O   1 
ATOM   2439 C CB  . ILE A 1 335 ? -4.942  -5.244  -25.451 1.00 25.23  ? 321 ILE A CB  1 
ATOM   2440 C CG1 . ILE A 1 335 ? -5.144  -3.724  -25.404 1.00 26.60  ? 321 ILE A CG1 1 
ATOM   2441 C CG2 . ILE A 1 335 ? -3.523  -5.618  -25.878 1.00 25.00  ? 321 ILE A CG2 1 
ATOM   2442 C CD1 . ILE A 1 335 ? -4.077  -2.977  -24.636 1.00 38.66  ? 321 ILE A CD1 1 
ATOM   2443 N N   . MET A 1 336 ? -6.127  -8.197  -25.450 1.00 16.85  ? 322 MET A N   1 
ATOM   2444 C CA  . MET A 1 336 ? -5.860  -9.629  -25.447 1.00 16.96  ? 322 MET A CA  1 
ATOM   2445 C C   . MET A 1 336 ? -6.885  -10.364 -24.589 1.00 14.52  ? 322 MET A C   1 
ATOM   2446 O O   . MET A 1 336 ? -7.173  -9.911  -23.464 1.00 15.36  ? 322 MET A O   1 
ATOM   2447 C CB  . MET A 1 336 ? -4.471  -9.894  -24.848 1.00 20.69  ? 322 MET A CB  1 
ATOM   2448 C CG  . MET A 1 336 ? -4.195  -11.349 -24.555 1.00 27.83  ? 322 MET A CG  1 
ATOM   2449 S SD  . MET A 1 336 ? -2.457  -11.680 -24.257 1.00 40.20  ? 322 MET A SD  1 
ATOM   2450 C CE  . MET A 1 336 ? -1.830  -11.412 -25.919 1.00 54.13  ? 322 MET A CE  1 
ATOM   2451 N N   . ASN A 1 337 ? -7.385  -11.490 -25.114 1.00 15.68  ? 323 ASN A N   1 
ATOM   2452 C CA  . ASN A 1 337 ? -8.416  -12.251 -24.434 1.00 14.36  ? 323 ASN A CA  1 
ATOM   2453 C C   . ASN A 1 337 ? -7.923  -13.646 -24.082 1.00 16.93  ? 323 ASN A C   1 
ATOM   2454 O O   . ASN A 1 337 ? -6.946  -14.147 -24.654 1.00 19.24  ? 323 ASN A O   1 
ATOM   2455 C CB  . ASN A 1 337 ? -9.681  -12.323 -25.276 1.00 13.35  ? 323 ASN A CB  1 
ATOM   2456 C CG  . ASN A 1 337 ? -10.358 -10.974 -25.261 1.00 14.84  ? 323 ASN A CG  1 
ATOM   2457 O OD1 . ASN A 1 337 ? -10.668 -10.477 -24.193 1.00 14.81  ? 323 ASN A OD1 1 
ATOM   2458 N ND2 . ASN A 1 337 ? -10.635 -10.414 -26.431 1.00 17.44  ? 323 ASN A ND2 1 
ATOM   2459 N N   . ILE A 1 338 ? -8.649  -14.269 -23.152 1.00 15.50  ? 324 ILE A N   1 
ATOM   2460 C CA  . ILE A 1 338 ? -8.361  -15.653 -22.762 1.00 14.99  ? 324 ILE A CA  1 
ATOM   2461 C C   . ILE A 1 338 ? -8.820  -16.579 -23.879 1.00 15.59  ? 324 ILE A C   1 
ATOM   2462 O O   . ILE A 1 338 ? -9.859  -16.348 -24.531 1.00 19.83  ? 324 ILE A O   1 
ATOM   2463 C CB  . ILE A 1 338 ? -9.086  -16.039 -21.449 1.00 18.45  ? 324 ILE A CB  1 
ATOM   2464 C CG1 . ILE A 1 338 ? -8.585  -15.295 -20.210 1.00 30.10  ? 324 ILE A CG1 1 
ATOM   2465 C CG2 . ILE A 1 338 ? -9.097  -17.550 -21.175 1.00 22.49  ? 324 ILE A CG2 1 
ATOM   2466 C CD1 . ILE A 1 338 ? -7.146  -15.462 -19.994 1.00 28.49  ? 324 ILE A CD1 1 
ATOM   2467 N N   . GLU A 1 339 ? -8.067  -17.666 -24.055 1.00 16.15  ? 325 GLU A N   1 
ATOM   2468 C CA  . GLU A 1 339 ? -8.418  -18.762 -24.961 1.00 15.77  ? 325 GLU A CA  1 
ATOM   2469 C C   . GLU A 1 339 ? -8.520  -20.056 -24.167 1.00 18.87  ? 325 GLU A C   1 
ATOM   2470 O O   . GLU A 1 339 ? -7.807  -20.266 -23.192 1.00 20.91  ? 325 GLU A O   1 
ATOM   2471 C CB  . GLU A 1 339 ? -7.358  -18.944 -26.049 1.00 22.65  ? 325 GLU A CB  1 
ATOM   2472 C CG  . GLU A 1 339 ? -7.074  -17.644 -26.773 1.00 35.97  ? 325 GLU A CG  1 
ATOM   2473 C CD  . GLU A 1 339 ? -5.979  -17.680 -27.816 1.00 35.01  ? 325 GLU A CD  1 
ATOM   2474 O OE1 . GLU A 1 339 ? -4.986  -18.427 -27.645 1.00 46.92  ? 325 GLU A OE1 1 
ATOM   2475 O OE2 . GLU A 1 339 ? -6.118  -16.910 -28.777 1.00 64.88  ? 325 GLU A OE2 1 
ATOM   2476 N N   . GLU A 1 340 ? -9.274  -21.005 -24.723 1.00 20.89  ? 326 GLU A N   1 
ATOM   2477 C CA  . GLU A 1 340 ? -9.323  -22.343 -24.157 1.00 21.58  ? 326 GLU A CA  1 
ATOM   2478 C C   . GLU A 1 340 ? -7.899  -22.893 -24.040 1.00 19.50  ? 326 GLU A C   1 
ATOM   2479 O O   . GLU A 1 340 ? -7.073  -22.760 -24.944 1.00 20.07  ? 326 GLU A O   1 
ATOM   2480 C CB  . GLU A 1 340 ? -10.210 -23.203 -25.058 1.00 26.18  ? 326 GLU A CB  1 
ATOM   2481 C CG  . GLU A 1 340 ? -10.259 -24.674 -24.673 1.00 41.35  ? 326 GLU A CG  1 
ATOM   2482 C CD  . GLU A 1 340 ? -11.355 -25.401 -25.433 1.00 59.63  ? 326 GLU A CD  1 
ATOM   2483 O OE1 . GLU A 1 340 ? -11.380 -26.642 -25.384 1.00 61.20  ? 326 GLU A OE1 1 
ATOM   2484 O OE2 . GLU A 1 340 ? -12.194 -24.718 -26.062 1.00 54.64  ? 326 GLU A OE2 1 
ATOM   2485 N N   . GLY A 1 341 ? -7.621  -23.464 -22.871 1.00 17.96  ? 327 GLY A N   1 
ATOM   2486 C CA  . GLY A 1 341 ? -6.324  -24.047 -22.573 1.00 19.05  ? 327 GLY A CA  1 
ATOM   2487 C C   . GLY A 1 341 ? -5.300  -23.099 -21.935 1.00 15.25  ? 327 GLY A C   1 
ATOM   2488 O O   . GLY A 1 341 ? -4.278  -23.577 -21.431 1.00 18.38  ? 327 GLY A O   1 
ATOM   2489 N N   . ASP A 1 342 ? -5.568  -21.785 -21.872 1.00 16.81  ? 328 ASP A N   1 
ATOM   2490 C CA  . ASP A 1 342 ? -4.734  -20.898 -21.067 1.00 15.09  ? 328 ASP A CA  1 
ATOM   2491 C C   . ASP A 1 342 ? -4.755  -21.337 -19.606 1.00 14.95  ? 328 ASP A C   1 
ATOM   2492 O O   . ASP A 1 342 ? -5.745  -21.848 -19.112 1.00 16.49  ? 328 ASP A O   1 
ATOM   2493 C CB  . ASP A 1 342 ? -5.312  -19.489 -21.109 1.00 16.87  ? 328 ASP A CB  1 
ATOM   2494 C CG  . ASP A 1 342 ? -5.024  -18.728 -22.384 1.00 15.81  ? 328 ASP A CG  1 
ATOM   2495 O OD1 . ASP A 1 342 ? -4.179  -19.202 -23.243 1.00 18.41  ? 328 ASP A OD1 1 
ATOM   2496 O OD2 . ASP A 1 342 ? -5.616  -17.639 -22.541 1.00 17.03  ? 328 ASP A OD2 1 
ATOM   2497 N N   . SER A 1 343 ? -3.658  -21.013 -18.919 1.00 13.91  ? 329 SER A N   1 
ATOM   2498 C CA  . SER A 1 343 ? -3.604  -21.248 -17.483 1.00 12.20  ? 329 SER A CA  1 
ATOM   2499 C C   . SER A 1 343 ? -3.448  -19.914 -16.768 1.00 11.85  ? 329 SER A C   1 
ATOM   2500 O O   . SER A 1 343 ? -2.806  -19.017 -17.324 1.00 14.59  ? 329 SER A O   1 
ATOM   2501 C CB  . SER A 1 343 ? -2.431  -22.165 -17.115 1.00 13.03  ? 329 SER A CB  1 
ATOM   2502 O OG  . SER A 1 343 ? -2.540  -23.447 -17.723 1.00 15.44  ? 329 SER A OG  1 
ATOM   2503 N N   . ILE A 1 344 ? -4.039  -19.807 -15.556 1.00 12.47  ? 330 ILE A N   1 
ATOM   2504 C CA  . ILE A 1 344 ? -4.121  -18.550 -14.824 1.00 12.70  ? 330 ILE A CA  1 
ATOM   2505 C C   . ILE A 1 344 ? -3.499  -18.735 -13.445 1.00 12.96  ? 330 ILE A C   1 
ATOM   2506 O O   . ILE A 1 344 ? -3.888  -19.657 -12.710 1.00 14.79  ? 330 ILE A O   1 
ATOM   2507 C CB  . ILE A 1 344 ? -5.594  -18.141 -14.629 1.00 15.50  ? 330 ILE A CB  1 
ATOM   2508 C CG1 . ILE A 1 344 ? -6.435  -18.271 -15.898 1.00 23.22  ? 330 ILE A CG1 1 
ATOM   2509 C CG2 . ILE A 1 344 ? -5.682  -16.770 -13.998 1.00 17.98  ? 330 ILE A CG2 1 
ATOM   2510 C CD1 . ILE A 1 344 ? -5.919  -17.473 -17.038 1.00 21.35  ? 330 ILE A CD1 1 
ATOM   2511 N N   . PHE A 1 345 ? -2.585  -17.814 -13.092 1.00 13.51  ? 331 PHE A N   1 
ATOM   2512 C CA  . PHE A 1 345 ? -2.064  -17.774 -11.734 1.00 12.04  ? 331 PHE A CA  1 
ATOM   2513 C C   . PHE A 1 345 ? -2.628  -16.535 -11.082 1.00 12.87  ? 331 PHE A C   1 
ATOM   2514 O O   . PHE A 1 345 ? -2.335  -15.421 -11.546 1.00 14.34  ? 331 PHE A O   1 
ATOM   2515 C CB  . PHE A 1 345 ? -0.527  -17.715 -11.750 1.00 14.92  ? 331 PHE A CB  1 
ATOM   2516 C CG  . PHE A 1 345 ? 0.093   -17.733 -10.371 1.00 18.36  ? 331 PHE A CG  1 
ATOM   2517 C CD1 . PHE A 1 345 ? 0.096   -18.899 -9.616  1.00 20.86  ? 331 PHE A CD1 1 
ATOM   2518 C CD2 . PHE A 1 345 ? 0.703   -16.603 -9.838  1.00 20.32  ? 331 PHE A CD2 1 
ATOM   2519 C CE1 . PHE A 1 345 ? 0.662   -18.923 -8.347  1.00 24.62  ? 331 PHE A CE1 1 
ATOM   2520 C CE2 . PHE A 1 345 ? 1.248   -16.631 -8.553  1.00 22.15  ? 331 PHE A CE2 1 
ATOM   2521 C CZ  . PHE A 1 345 ? 1.204   -17.779 -7.799  1.00 22.19  ? 331 PHE A CZ  1 
ATOM   2522 N N   . LEU A 1 346 ? -3.464  -16.723 -10.043 1.00 15.16  ? 332 LEU A N   1 
ATOM   2523 C CA  . LEU A 1 346 ? -4.117  -15.547 -9.476  1.00 19.87  ? 332 LEU A CA  1 
ATOM   2524 C C   . LEU A 1 346 ? -3.331  -15.086 -8.253  1.00 28.53  ? 332 LEU A C   1 
ATOM   2525 O O   . LEU A 1 346 ? -3.332  -15.761 -7.238  1.00 30.83  ? 332 LEU A O   1 
ATOM   2526 C CB  . LEU A 1 346 ? -5.636  -15.746 -9.274  1.00 26.61  ? 332 LEU A CB  1 
ATOM   2527 C CG  . LEU A 1 346 ? -6.427  -14.521 -8.781  1.00 28.56  ? 332 LEU A CG  1 
ATOM   2528 N N   . ALA A 1 347 ? -2.610  -13.960 -8.415  1.00 30.05  ? 333 ALA A N   1 
ATOM   2529 C CA  . ALA A 1 347 ? -1.636  -13.520 -7.431  1.00 34.99  ? 333 ALA A CA  1 
ATOM   2530 C C   . ALA A 1 347 ? -2.111  -12.230 -6.770  1.00 33.86  ? 333 ALA A C   1 
ATOM   2531 O O   . ALA A 1 347 ? -1.361  -11.252 -6.764  1.00 54.33  ? 333 ALA A O   1 
ATOM   2532 C CB  . ALA A 1 347 ? -0.276  -13.358 -8.097  1.00 33.13  ? 333 ALA A CB  1 
ATOM   2533 N N   . ILE A 1 348 ? -3.353  -12.235 -6.242  1.00 57.18  ? 334 ILE A N   1 
ATOM   2534 C CA  . ILE A 1 348 ? -3.933  -11.035 -5.633  1.00 57.98  ? 334 ILE A CA  1 
ATOM   2535 C C   . ILE A 1 348 ? -4.518  -11.382 -4.256  1.00 73.42  ? 334 ILE A C   1 
ATOM   2536 O O   . ILE A 1 348 ? -4.758  -12.590 -4.041  1.00 64.66  ? 334 ILE A O   1 
ATOM   2537 C CB  . ILE A 1 348 ? -4.979  -10.340 -6.546  1.00 62.26  ? 334 ILE A CB  1 
ATOM   2538 N N   . ALA A 1 350 ? -7.650  -11.214 -1.325  1.00 61.50  ? 336 ALA A N   1 
ATOM   2539 C CA  . ALA A 1 350 ? -9.131  -11.169 -1.366  1.00 65.93  ? 336 ALA A CA  1 
ATOM   2540 C C   . ALA A 1 350 ? -9.667  -10.406 -0.157  1.00 64.50  ? 336 ALA A C   1 
ATOM   2541 O O   . ALA A 1 350 ? -9.272  -10.671 0.972   1.00 78.53  ? 336 ALA A O   1 
ATOM   2542 C CB  . ALA A 1 350 ? -9.687  -12.571 -1.413  1.00 63.17  ? 336 ALA A CB  1 
ATOM   2543 N N   . SER A 1 351 ? -10.584 -9.470  -0.421  1.00 55.03  ? 337 SER A N   1 
ATOM   2544 C CA  . SER A 1 351 ? -11.245 -8.673  0.601   1.00 45.72  ? 337 SER A CA  1 
ATOM   2545 C C   . SER A 1 351 ? -12.755 -8.788  0.430   1.00 32.81  ? 337 SER A C   1 
ATOM   2546 O O   . SER A 1 351 ? -13.221 -9.256  -0.603  1.00 34.98  ? 337 SER A O   1 
ATOM   2547 C CB  . SER A 1 351 ? -10.831 -7.249  0.497   1.00 52.42  ? 337 SER A CB  1 
ATOM   2548 O OG  . SER A 1 351 ? -11.059 -6.736  -0.807  1.00 70.40  ? 337 SER A OG  1 
ATOM   2549 N N   . ALA A 1 352 ? -13.507 -8.370  1.456   1.00 28.83  ? 338 ALA A N   1 
ATOM   2550 C CA  . ALA A 1 352 ? -14.958 -8.493  1.426   1.00 50.97  ? 338 ALA A CA  1 
ATOM   2551 C C   . ALA A 1 352 ? -15.450 -7.701  0.222   1.00 67.23  ? 338 ALA A C   1 
ATOM   2552 O O   . ALA A 1 352 ? -16.326 -8.156  -0.516  1.00 45.44  ? 338 ALA A O   1 
ATOM   2553 C CB  . ALA A 1 352 ? -15.565 -8.003  2.721   1.00 46.50  ? 338 ALA A CB  1 
ATOM   2554 N N   . ASN A 1 353 ? -14.800 -6.549  0.024   1.00 75.87  ? 339 ASN A N   1 
ATOM   2555 C CA  . ASN A 1 353 ? -14.998 -5.674  -1.117  1.00 87.46  ? 339 ASN A CA  1 
ATOM   2556 C C   . ASN A 1 353 ? -14.880 -6.423  -2.448  1.00 96.02  ? 339 ASN A C   1 
ATOM   2557 O O   . ASN A 1 353 ? -15.548 -6.033  -3.396  1.00 73.05  ? 339 ASN A O   1 
ATOM   2558 C CB  . ASN A 1 353 ? -14.071 -4.449  -1.102  1.00 56.94  ? 339 ASN A CB  1 
ATOM   2559 N N   . MET A 1 354 ? -14.084 -7.504  -2.534  1.00 126.10 ? 340 MET A N   1 
ATOM   2560 C CA  . MET A 1 354 ? -13.743 -8.073  -3.838  1.00 137.92 ? 340 MET A CA  1 
ATOM   2561 C C   . MET A 1 354 ? -14.164 -9.529  -3.987  1.00 137.11 ? 340 MET A C   1 
ATOM   2562 O O   . MET A 1 354 ? -13.881 -10.138 -5.010  1.00 118.40 ? 340 MET A O   1 
ATOM   2563 C CB  . MET A 1 354 ? -12.232 -8.057  -4.068  1.00 91.80  ? 340 MET A CB  1 
ATOM   2564 C CG  . MET A 1 354 ? -11.622 -6.688  -3.956  1.00 96.24  ? 340 MET A CG  1 
ATOM   2565 S SD  . MET A 1 354 ? -11.618 -5.642  -5.411  1.00 52.52  ? 340 MET A SD  1 
ATOM   2566 C CE  . MET A 1 354 ? -12.242 -6.730  -6.687  1.00 59.38  ? 340 MET A CE  1 
ATOM   2567 N N   . GLU A 1 355 ? -14.843 -10.085 -2.989  1.00 136.26 ? 341 GLU A N   1 
ATOM   2568 C CA  . GLU A 1 355 ? -15.016 -11.527 -2.996  1.00 89.10  ? 341 GLU A CA  1 
ATOM   2569 C C   . GLU A 1 355 ? -15.964 -11.970 -4.116  1.00 73.73  ? 341 GLU A C   1 
ATOM   2570 O O   . GLU A 1 355 ? -15.765 -13.033 -4.707  1.00 47.01  ? 341 GLU A O   1 
ATOM   2571 C CB  . GLU A 1 355 ? -15.407 -12.018 -1.603  1.00 106.45 ? 341 GLU A CB  1 
ATOM   2572 C CG  . GLU A 1 355 ? -16.805 -11.611 -1.173  1.00 95.48  ? 341 GLU A CG  1 
ATOM   2573 C CD  . GLU A 1 355 ? -17.087 -11.840 0.305   1.00 81.87  ? 341 GLU A CD  1 
ATOM   2574 O OE1 . GLU A 1 355 ? -18.137 -11.364 0.795   1.00 40.01  ? 341 GLU A OE1 1 
ATOM   2575 O OE2 . GLU A 1 355 ? -16.266 -12.522 0.957   1.00 33.14  ? 341 GLU A OE2 1 
ATOM   2576 N N   . VAL A 1 356 ? -16.973 -11.143 -4.424  1.00 53.06  ? 342 VAL A N   1 
ATOM   2577 C CA  . VAL A 1 356 ? -17.950 -11.464 -5.454  1.00 57.00  ? 342 VAL A CA  1 
ATOM   2578 C C   . VAL A 1 356 ? -17.327 -11.452 -6.853  1.00 25.69  ? 342 VAL A C   1 
ATOM   2579 O O   . VAL A 1 356 ? -17.520 -12.396 -7.640  1.00 21.15  ? 342 VAL A O   1 
ATOM   2580 C CB  . VAL A 1 356 ? -19.197 -10.562 -5.374  1.00 41.39  ? 342 VAL A CB  1 
ATOM   2581 C CG1 . VAL A 1 356 ? -20.098 -10.675 -6.603  1.00 31.23  ? 342 VAL A CG1 1 
ATOM   2582 C CG2 . VAL A 1 356 ? -19.987 -10.802 -4.100  1.00 39.07  ? 342 VAL A CG2 1 
ATOM   2583 N N   . ILE A 1 357 ? -16.595 -10.390 -7.187  1.00 25.68  ? 343 ILE A N   1 
ATOM   2584 C CA  . ILE A 1 357 ? -16.019 -10.317 -8.559  1.00 26.86  ? 343 ILE A CA  1 
ATOM   2585 C C   . ILE A 1 357 ? -15.013 -11.464 -8.742  1.00 24.64  ? 343 ILE A C   1 
ATOM   2586 O O   . ILE A 1 357 ? -14.938 -11.994 -9.839  1.00 22.50  ? 343 ILE A O   1 
ATOM   2587 C CB  . ILE A 1 357 ? -15.385 -8.942  -8.846  1.00 27.44  ? 343 ILE A CB  1 
ATOM   2588 C CG1 . ILE A 1 357 ? -16.298 -7.810  -8.369  1.00 36.83  ? 343 ILE A CG1 1 
ATOM   2589 C CG2 . ILE A 1 357 ? -15.026 -8.802  -10.315 1.00 28.88  ? 343 ILE A CG2 1 
ATOM   2590 C CD1 . ILE A 1 357 ? -17.543 -7.623  -9.211  1.00 41.26  ? 343 ILE A CD1 1 
ATOM   2591 N N   . ILE A 1 358 ? -14.263 -11.797 -7.692  1.00 20.82  ? 344 ILE A N   1 
ATOM   2592 C CA  . ILE A 1 358 ? -13.326 -12.912 -7.813  1.00 22.34  ? 344 ILE A CA  1 
ATOM   2593 C C   . ILE A 1 358 ? -14.070 -14.208 -8.144  1.00 19.27  ? 344 ILE A C   1 
ATOM   2594 O O   . ILE A 1 358 ? -13.688 -14.891 -9.085  1.00 17.70  ? 344 ILE A O   1 
ATOM   2595 C CB  . ILE A 1 358 ? -12.413 -13.067 -6.582  1.00 25.33  ? 344 ILE A CB  1 
ATOM   2596 C CG1 . ILE A 1 358 ? -11.407 -11.915 -6.476  1.00 32.61  ? 344 ILE A CG1 1 
ATOM   2597 C CG2 . ILE A 1 358 ? -11.684 -14.405 -6.622  1.00 26.36  ? 344 ILE A CG2 1 
ATOM   2598 C CD1 . ILE A 1 358 ? -10.686 -11.891 -5.140  1.00 35.77  ? 344 ILE A CD1 1 
ATOM   2599 N N   . ALA A 1 359 ? -15.161 -14.508 -7.414  1.00 18.48  ? 345 ALA A N   1 
ATOM   2600 C CA  . ALA A 1 359 ? -15.937 -15.726 -7.645  1.00 18.73  ? 345 ALA A CA  1 
ATOM   2601 C C   . ALA A 1 359 ? -16.504 -15.776 -9.074  1.00 16.42  ? 345 ALA A C   1 
ATOM   2602 O O   . ALA A 1 359 ? -16.353 -16.776 -9.791  1.00 17.09  ? 345 ALA A O   1 
ATOM   2603 C CB  . ALA A 1 359 ? -17.022 -15.807 -6.586  1.00 22.38  ? 345 ALA A CB  1 
ATOM   2604 N N   . ASP A 1 360 ? -17.027 -14.637 -9.542  1.00 14.83  ? 346 ASP A N   1 
ATOM   2605 C CA  . ASP A 1 360 ? -17.645 -14.550 -10.853 1.00 15.12  ? 346 ASP A CA  1 
ATOM   2606 C C   . ASP A 1 360 ? -16.572 -14.749 -11.929 1.00 15.08  ? 346 ASP A C   1 
ATOM   2607 O O   . ASP A 1 360 ? -16.765 -15.433 -12.934 1.00 16.62  ? 346 ASP A O   1 
ATOM   2608 C CB  . ASP A 1 360 ? -18.275 -13.168 -11.059 1.00 16.91  ? 346 ASP A CB  1 
ATOM   2609 C CG  . ASP A 1 360 ? -19.503 -12.895 -10.188 1.00 24.11  ? 346 ASP A CG  1 
ATOM   2610 O OD1 . ASP A 1 360 ? -20.056 -13.872 -9.612  1.00 27.02  ? 346 ASP A OD1 1 
ATOM   2611 O OD2 . ASP A 1 360 ? -19.866 -11.704 -10.034 1.00 37.24  ? 346 ASP A OD2 1 
ATOM   2612 N N   . THR A 1 361 ? -15.382 -14.175 -11.692 1.00 15.54  ? 347 THR A N   1 
ATOM   2613 C CA  . THR A 1 361 ? -14.323 -14.238 -12.686 1.00 15.83  ? 347 THR A CA  1 
ATOM   2614 C C   . THR A 1 361 ? -13.810 -15.680 -12.792 1.00 13.50  ? 347 THR A C   1 
ATOM   2615 O O   . THR A 1 361 ? -13.528 -16.190 -13.884 1.00 16.93  ? 347 THR A O   1 
ATOM   2616 C CB  . THR A 1 361 ? -13.203 -13.273 -12.276 1.00 15.94  ? 347 THR A CB  1 
ATOM   2617 O OG1 . THR A 1 361 ? -13.768 -11.959 -12.248 1.00 19.97  ? 347 THR A OG1 1 
ATOM   2618 C CG2 . THR A 1 361 ? -12.066 -13.284 -13.269 1.00 16.68  ? 347 THR A CG2 1 
ATOM   2619 N N   . LEU A 1 362 ? -13.650 -16.357 -11.636 1.00 14.72  ? 348 LEU A N   1 
ATOM   2620 C CA  . LEU A 1 362 ? -13.230 -17.756 -11.689 1.00 16.03  ? 348 LEU A CA  1 
ATOM   2621 C C   . LEU A 1 362 ? -14.245 -18.636 -12.433 1.00 14.21  ? 348 LEU A C   1 
ATOM   2622 O O   . LEU A 1 362 ? -13.833 -19.510 -13.202 1.00 16.68  ? 348 LEU A O   1 
ATOM   2623 C CB  . LEU A 1 362 ? -13.010 -18.271 -10.259 1.00 18.91  ? 348 LEU A CB  1 
ATOM   2624 C CG  . LEU A 1 362 ? -11.858 -17.629 -9.476  1.00 22.52  ? 348 LEU A CG  1 
ATOM   2625 C CD1 . LEU A 1 362 ? -11.802 -18.245 -8.094  1.00 28.81  ? 348 LEU A CD1 1 
ATOM   2626 C CD2 . LEU A 1 362 ? -10.523 -17.823 -10.176 1.00 25.76  ? 348 LEU A CD2 1 
ATOM   2627 N N   . ASN A 1 363 ? -15.543 -18.375 -12.225 1.00 15.17  ? 349 ASN A N   1 
ATOM   2628 C CA  . ASN A 1 363 ? -16.558 -19.120 -12.959 1.00 15.92  ? 349 ASN A CA  1 
ATOM   2629 C C   . ASN A 1 363 ? -16.431 -18.828 -14.456 1.00 17.04  ? 349 ASN A C   1 
ATOM   2630 O O   . ASN A 1 363 ? -16.510 -19.746 -15.234 1.00 18.49  ? 349 ASN A O   1 
ATOM   2631 C CB  . ASN A 1 363 ? -17.960 -18.842 -12.431 1.00 14.81  ? 349 ASN A CB  1 
ATOM   2632 C CG  . ASN A 1 363 ? -18.209 -19.433 -11.067 1.00 18.26  ? 349 ASN A CG  1 
ATOM   2633 O OD1 . ASN A 1 363 ? -17.644 -20.473 -10.702 1.00 23.23  ? 349 ASN A OD1 1 
ATOM   2634 N ND2 . ASN A 1 363 ? -19.040 -18.754 -10.302 1.00 20.86  ? 349 ASN A ND2 1 
ATOM   2635 N N   . GLU A 1 364 ? -16.210 -17.556 -14.821 1.00 15.03  ? 350 GLU A N   1 
ATOM   2636 C CA  . GLU A 1 364 ? -16.084 -17.161 -16.226 1.00 15.84  ? 350 GLU A CA  1 
ATOM   2637 C C   . GLU A 1 364 ? -14.898 -17.895 -16.857 1.00 16.16  ? 350 GLU A C   1 
ATOM   2638 O O   . GLU A 1 364 ? -14.956 -18.333 -17.992 1.00 18.08  ? 350 GLU A O   1 
ATOM   2639 C CB  . GLU A 1 364 ? -15.894 -15.647 -16.349 1.00 17.64  ? 350 GLU A CB  1 
ATOM   2640 C CG  . GLU A 1 364 ? -17.107 -14.785 -15.940 1.00 18.76  ? 350 GLU A CG  1 
ATOM   2641 C CD  . GLU A 1 364 ? -16.920 -13.293 -15.609 1.00 25.72  ? 350 GLU A CD  1 
ATOM   2642 O OE1 . GLU A 1 364 ? -15.768 -12.766 -15.670 1.00 23.26  ? 350 GLU A OE1 1 
ATOM   2643 O OE2 . GLU A 1 364 ? -17.946 -12.616 -15.265 1.00 28.00  ? 350 GLU A OE2 1 
ATOM   2644 N N   . LEU A 1 365 ? -13.782 -17.997 -16.125 1.00 16.21  ? 351 LEU A N   1 
ATOM   2645 C CA  . LEU A 1 365 ? -12.575 -18.615 -16.657 1.00 16.49  ? 351 LEU A CA  1 
ATOM   2646 C C   . LEU A 1 365 ? -12.805 -20.108 -16.861 1.00 16.47  ? 351 LEU A C   1 
ATOM   2647 O O   . LEU A 1 365 ? -12.393 -20.646 -17.881 1.00 19.96  ? 351 LEU A O   1 
ATOM   2648 C CB  . LEU A 1 365 ? -11.414 -18.413 -15.654 1.00 19.19  ? 351 LEU A CB  1 
ATOM   2649 C CG  . LEU A 1 365 ? -10.856 -16.986 -15.627 1.00 18.07  ? 351 LEU A CG  1 
ATOM   2650 C CD1 . LEU A 1 365 ? -9.982  -16.696 -14.386 1.00 21.00  ? 351 LEU A CD1 1 
ATOM   2651 C CD2 . LEU A 1 365 ? -10.084 -16.680 -16.907 1.00 18.43  ? 351 LEU A CD2 1 
ATOM   2652 N N   . VAL A 1 366 ? -13.435 -20.773 -15.879 1.00 17.36  ? 352 VAL A N   1 
ATOM   2653 C CA  . VAL A 1 366 ? -13.742 -22.179 -16.087 1.00 21.50  ? 352 VAL A CA  1 
ATOM   2654 C C   . VAL A 1 366 ? -14.662 -22.359 -17.305 1.00 20.21  ? 352 VAL A C   1 
ATOM   2655 O O   . VAL A 1 366 ? -14.405 -23.284 -18.089 1.00 25.96  ? 352 VAL A O   1 
ATOM   2656 C CB  . VAL A 1 366 ? -14.287 -22.847 -14.804 1.00 20.53  ? 352 VAL A CB  1 
ATOM   2657 C CG1 . VAL A 1 366 ? -14.693 -24.284 -15.066 1.00 31.52  ? 352 VAL A CG1 1 
ATOM   2658 C CG2 . VAL A 1 366 ? -13.261 -22.795 -13.685 1.00 28.28  ? 352 VAL A CG2 1 
ATOM   2659 N N   . ARG A 1 367 ? -15.673 -21.474 -17.476 1.00 18.20  ? 353 ARG A N   1 
ATOM   2660 C CA  . ARG A 1 367 ? -16.595 -21.526 -18.627 1.00 17.86  ? 353 ARG A CA  1 
ATOM   2661 C C   . ARG A 1 367 ? -15.847 -21.377 -19.961 1.00 22.14  ? 353 ARG A C   1 
ATOM   2662 O O   . ARG A 1 367 ? -16.205 -22.011 -20.957 1.00 24.07  ? 353 ARG A O   1 
ATOM   2663 C CB  . ARG A 1 367 ? -17.741 -20.501 -18.480 1.00 30.54  ? 353 ARG A CB  1 
ATOM   2664 C CG  . ARG A 1 367 ? -19.002 -20.815 -19.287 1.00 58.35  ? 353 ARG A CG  1 
ATOM   2665 C CD  . ARG A 1 367 ? -20.284 -20.058 -18.925 1.00 80.40  ? 353 ARG A CD  1 
ATOM   2666 N NE  . ARG A 1 367 ? -20.044 -18.793 -18.225 1.00 99.82  ? 353 ARG A NE  1 
ATOM   2667 N NH1 . ARG A 1 367 ? -22.798 -18.101 -17.484 1.00 134.06 ? 353 ARG A NH1 1 
ATOM   2668 N N   . ALA A 1 368 ? -14.797 -20.546 -19.969 1.00 20.78  ? 354 ALA A N   1 
ATOM   2669 C CA  . ALA A 1 368 ? -13.975 -20.306 -21.151 1.00 20.97  ? 354 ALA A CA  1 
ATOM   2670 C C   . ALA A 1 368 ? -12.969 -21.428 -21.427 1.00 21.19  ? 354 ALA A C   1 
ATOM   2671 O O   . ALA A 1 368 ? -12.248 -21.346 -22.418 1.00 26.99  ? 354 ALA A O   1 
ATOM   2672 C CB  . ALA A 1 368 ? -13.260 -18.987 -20.967 1.00 26.28  ? 354 ALA A CB  1 
ATOM   2673 N N   . GLY A 1 369 ? -12.865 -22.435 -20.549 1.00 20.50  ? 355 GLY A N   1 
ATOM   2674 C CA  . GLY A 1 369 ? -11.937 -23.527 -20.803 1.00 19.87  ? 355 GLY A CA  1 
ATOM   2675 C C   . GLY A 1 369 ? -10.516 -23.219 -20.318 1.00 18.88  ? 355 GLY A C   1 
ATOM   2676 O O   . GLY A 1 369 ? -9.541  -23.838 -20.748 1.00 21.41  ? 355 GLY A O   1 
ATOM   2677 N N   . ALA A 1 370 ? -10.378 -22.235 -19.429 1.00 18.02  ? 356 ALA A N   1 
ATOM   2678 C CA  . ALA A 1 370 ? -9.057  -21.940 -18.894 1.00 17.90  ? 356 ALA A CA  1 
ATOM   2679 C C   . ALA A 1 370 ? -8.863  -22.793 -17.653 1.00 20.22  ? 356 ALA A C   1 
ATOM   2680 O O   . ALA A 1 370 ? -9.833  -23.271 -17.066 1.00 22.19  ? 356 ALA A O   1 
ATOM   2681 C CB  . ALA A 1 370 ? -8.891  -20.474 -18.542 1.00 19.34  ? 356 ALA A CB  1 
ATOM   2682 N N   . HIS A 1 371 ? -7.597  -22.892 -17.264 1.00 17.27  ? 357 HIS A N   1 
ATOM   2683 C CA  . HIS A 1 371 ? -7.161  -23.695 -16.140 1.00 17.86  ? 357 HIS A CA  1 
ATOM   2684 C C   . HIS A 1 371 ? -6.612  -22.770 -15.054 1.00 15.71  ? 357 HIS A C   1 
ATOM   2685 O O   . HIS A 1 371 ? -5.624  -22.056 -15.261 1.00 19.79  ? 357 HIS A O   1 
ATOM   2686 C CB  . HIS A 1 371 ? -6.075  -24.686 -16.561 1.00 19.06  ? 357 HIS A CB  1 
ATOM   2687 C CG  . HIS A 1 371 ? -6.462  -25.579 -17.698 1.00 27.45  ? 357 HIS A CG  1 
ATOM   2688 N ND1 . HIS A 1 371 ? -7.335  -26.637 -17.567 1.00 31.92  ? 357 HIS A ND1 1 
ATOM   2689 C CD2 . HIS A 1 371 ? -6.067  -25.521 -19.003 1.00 34.50  ? 357 HIS A CD2 1 
ATOM   2690 C CE1 . HIS A 1 371 ? -7.481  -27.222 -18.756 1.00 45.81  ? 357 HIS A CE1 1 
ATOM   2691 N NE2 . HIS A 1 371 ? -6.688  -26.552 -19.663 1.00 36.59  ? 357 HIS A NE2 1 
ATOM   2692 N N   . ILE A 1 372 ? -7.259  -22.772 -13.890 1.00 17.85  ? 358 ILE A N   1 
ATOM   2693 C CA  . ILE A 1 372 ? -6.814  -21.996 -12.737 1.00 16.44  ? 358 ILE A CA  1 
ATOM   2694 C C   . ILE A 1 372 ? -5.796  -22.848 -11.992 1.00 17.21  ? 358 ILE A C   1 
ATOM   2695 O O   . ILE A 1 372 ? -6.108  -23.973 -11.588 1.00 19.64  ? 358 ILE A O   1 
ATOM   2696 C CB  . ILE A 1 372 ? -7.983  -21.666 -11.789 1.00 17.99  ? 358 ILE A CB  1 
ATOM   2697 C CG1 . ILE A 1 372 ? -9.238  -21.129 -12.494 1.00 30.35  ? 358 ILE A CG1 1 
ATOM   2698 C CG2 . ILE A 1 372 ? -7.510  -20.749 -10.681 1.00 19.70  ? 358 ILE A CG2 1 
ATOM   2699 C CD1 . ILE A 1 372 ? -8.973  -20.028 -13.479 1.00 34.51  ? 358 ILE A CD1 1 
ATOM   2700 N N   . ILE A 1 373 ? -4.602  -22.297 -11.792 1.00 14.84  ? 359 ILE A N   1 
ATOM   2701 C CA  . ILE A 1 373 ? -3.591  -23.002 -11.024 1.00 15.88  ? 359 ILE A CA  1 
ATOM   2702 C C   . ILE A 1 373 ? -4.062  -23.018 -9.576  1.00 20.31  ? 359 ILE A C   1 
ATOM   2703 O O   . ILE A 1 373 ? -4.389  -21.986 -9.007  1.00 19.14  ? 359 ILE A O   1 
ATOM   2704 C CB  . ILE A 1 373 ? -2.229  -22.314 -11.224 1.00 15.83  ? 359 ILE A CB  1 
ATOM   2705 C CG1 . ILE A 1 373 ? -1.731  -22.498 -12.661 1.00 15.21  ? 359 ILE A CG1 1 
ATOM   2706 C CG2 . ILE A 1 373 ? -1.187  -22.797 -10.193 1.00 17.34  ? 359 ILE A CG2 1 
ATOM   2707 C CD1 . ILE A 1 373 ? -0.493  -21.695 -12.976 1.00 16.66  ? 359 ILE A CD1 1 
ATOM   2708 N N   . PRO A 1 374 ? -4.179  -24.207 -8.943  1.00 23.43  ? 360 PRO A N   1 
ATOM   2709 C CA  . PRO A 1 374 ? -4.677  -24.269 -7.570  1.00 28.97  ? 360 PRO A CA  1 
ATOM   2710 C C   . PRO A 1 374 ? -3.731  -23.562 -6.599  1.00 27.09  ? 360 PRO A C   1 
ATOM   2711 O O   . PRO A 1 374 ? -2.518  -23.516 -6.837  1.00 23.85  ? 360 PRO A O   1 
ATOM   2712 C CB  . PRO A 1 374 ? -4.744  -25.772 -7.234  1.00 28.05  ? 360 PRO A CB  1 
ATOM   2713 C CG  . PRO A 1 374 ? -4.216  -26.525 -8.442  1.00 29.52  ? 360 PRO A CG  1 
ATOM   2714 C CD  . PRO A 1 374 ? -3.815  -25.517 -9.509  1.00 23.29  ? 360 PRO A CD  1 
ATOM   2715 N N   . ASN A 1 375 ? -4.305  -23.009 -5.520  1.00 30.59  ? 361 ASN A N   1 
ATOM   2716 C CA  . ASN A 1 375 ? -3.515  -22.539 -4.392  1.00 39.06  ? 361 ASN A CA  1 
ATOM   2717 C C   . ASN A 1 375 ? -2.979  -23.735 -3.602  1.00 30.87  ? 361 ASN A C   1 
ATOM   2718 O O   . ASN A 1 375 ? -3.647  -24.749 -3.426  1.00 43.19  ? 361 ASN A O   1 
ATOM   2719 C CB  . ASN A 1 375 ? -4.259  -21.516 -3.523  1.00 54.25  ? 361 ASN A CB  1 
ATOM   2720 C CG  . ASN A 1 375 ? -4.319  -20.124 -4.125  1.00 58.95  ? 361 ASN A CG  1 
ATOM   2721 O OD1 . ASN A 1 375 ? -3.863  -19.888 -5.245  1.00 67.09  ? 361 ASN A OD1 1 
ATOM   2722 N ND2 . ASN A 1 375 ? -4.878  -19.183 -3.382  1.00 68.90  ? 361 ASN A ND2 1 
ATOM   2723 N N   . ASN A 1 376 ? -1.742  -23.581 -3.135  1.00 35.24  ? 362 ASN A N   1 
ATOM   2724 C CA  . ASN A 1 376 ? -1.071  -24.571 -2.313  1.00 34.15  ? 362 ASN A CA  1 
ATOM   2725 C C   . ASN A 1 376 ? -1.505  -24.329 -0.870  1.00 42.37  ? 362 ASN A C   1 
ATOM   2726 O O   . ASN A 1 376 ? -1.375  -23.212 -0.362  1.00 32.94  ? 362 ASN A O   1 
ATOM   2727 C CB  . ASN A 1 376 ? 0.439   -24.533 -2.573  1.00 45.30  ? 362 ASN A CB  1 
ATOM   2728 C CG  . ASN A 1 376 ? 1.282   -25.453 -1.712  1.00 46.27  ? 362 ASN A CG  1 
ATOM   2729 O OD1 . ASN A 1 376 ? 0.790   -26.157 -0.832  1.00 52.68  ? 362 ASN A OD1 1 
ATOM   2730 N ND2 . ASN A 1 376 ? 2.580   -25.429 -1.957  1.00 62.52  ? 362 ASN A ND2 1 
ATOM   2731 N N   . LYS A 1 377 ? -2.050  -25.380 -0.239  1.00 58.21  ? 363 LYS A N   1 
ATOM   2732 C CA  . LYS A 1 377 ? -2.542  -25.305 1.130   1.00 54.62  ? 363 LYS A CA  1 
ATOM   2733 C C   . LYS A 1 377 ? -1.412  -24.873 2.075   1.00 66.11  ? 363 LYS A C   1 
ATOM   2734 O O   . LYS A 1 377 ? -1.660  -24.121 3.018   1.00 61.70  ? 363 LYS A O   1 
ATOM   2735 C CB  . LYS A 1 377 ? -3.246  -26.611 1.526   1.00 54.51  ? 363 LYS A CB  1 
ATOM   2736 N N   . LYS A 1 378 ? -0.166  -25.259 1.750   1.00 53.41  ? 364 LYS A N   1 
ATOM   2737 C CA  . LYS A 1 378 ? 0.993   -24.975 2.592   1.00 41.86  ? 364 LYS A CA  1 
ATOM   2738 C C   . LYS A 1 378 ? 1.421   -23.508 2.475   1.00 32.83  ? 364 LYS A C   1 
ATOM   2739 O O   . LYS A 1 378 ? 2.230   -23.047 3.277   1.00 38.88  ? 364 LYS A O   1 
ATOM   2740 C CB  . LYS A 1 378 ? 2.165   -25.920 2.280   1.00 40.82  ? 364 LYS A CB  1 
ATOM   2741 N N   . ILE A 1 379 ? 0.869   -22.795 1.485   1.00 30.69  ? 365 ILE A N   1 
ATOM   2742 C CA  . ILE A 1 379 ? 1.284   -21.444 1.142   1.00 33.00  ? 365 ILE A CA  1 
ATOM   2743 C C   . ILE A 1 379 ? 0.238   -20.423 1.589   1.00 39.77  ? 365 ILE A C   1 
ATOM   2744 O O   . ILE A 1 379 ? -0.951  -20.573 1.304   1.00 36.63  ? 365 ILE A O   1 
ATOM   2745 C CB  . ILE A 1 379 ? 1.585   -21.332 -0.366  1.00 33.27  ? 365 ILE A CB  1 
ATOM   2746 C CG1 . ILE A 1 379 ? 2.824   -22.151 -0.747  1.00 49.85  ? 365 ILE A CG1 1 
ATOM   2747 C CG2 . ILE A 1 379 ? 1.733   -19.876 -0.780  1.00 43.94  ? 365 ILE A CG2 1 
ATOM   2748 C CD1 . ILE A 1 379 ? 3.481   -21.700 -2.023  1.00 43.20  ? 365 ILE A CD1 1 
ATOM   2749 N N   . HIS A 1 380 ? 0.713   -19.393 2.313   1.00 27.06  ? 366 HIS A N   1 
ATOM   2750 C CA  . HIS A 1 380 ? -0.044  -18.171 2.567   1.00 27.75  ? 366 HIS A CA  1 
ATOM   2751 C C   . HIS A 1 380 ? 0.830   -17.026 2.072   1.00 33.38  ? 366 HIS A C   1 
ATOM   2752 O O   . HIS A 1 380 ? 1.901   -16.813 2.615   1.00 24.87  ? 366 HIS A O   1 
ATOM   2753 C CB  . HIS A 1 380 ? -0.379  -17.994 4.066   1.00 32.41  ? 366 HIS A CB  1 
ATOM   2754 C CG  . HIS A 1 380 ? -1.340  -16.894 4.398   1.00 43.99  ? 366 HIS A CG  1 
ATOM   2755 N ND1 . HIS A 1 380 ? -1.033  -15.551 4.371   1.00 43.49  ? 366 HIS A ND1 1 
ATOM   2756 N N   . ALA A 1 381 ? 0.393   -16.342 1.009   1.00 27.62  ? 367 ALA A N   1 
ATOM   2757 C CA  . ALA A 1 381 ? 1.150   -15.282 0.353   1.00 28.31  ? 367 ALA A CA  1 
ATOM   2758 C C   . ALA A 1 381 ? 0.384   -13.974 0.535   1.00 27.00  ? 367 ALA A C   1 
ATOM   2759 O O   . ALA A 1 381 ? -0.781  -13.906 0.144   1.00 28.78  ? 367 ALA A O   1 
ATOM   2760 C CB  . ALA A 1 381 ? 1.272   -15.599 -1.127  1.00 28.28  ? 367 ALA A CB  1 
ATOM   2761 N N   . SER A 1 382 ? 0.950   -12.991 1.251   1.00 18.42  ? 368 SER A N   1 
ATOM   2762 C CA  . SER A 1 382 ? 0.391   -11.643 1.266   1.00 18.03  ? 368 SER A CA  1 
ATOM   2763 C C   . SER A 1 382 ? 1.513   -10.623 1.468   1.00 15.57  ? 368 SER A C   1 
ATOM   2764 O O   . SER A 1 382 ? 2.616   -10.969 1.842   1.00 15.93  ? 368 SER A O   1 
ATOM   2765 C CB  . SER A 1 382 ? -0.651  -11.498 2.401   1.00 22.98  ? 368 SER A CB  1 
ATOM   2766 O OG  . SER A 1 382 ? -0.020  -11.218 3.637   1.00 28.67  ? 368 SER A OG  1 
ATOM   2767 N N   . SER A 1 383 ? 1.191   -9.335  1.304   1.00 14.76  ? 369 SER A N   1 
ATOM   2768 C CA  . SER A 1 383 ? 2.105   -8.259  1.637   1.00 13.93  ? 369 SER A CA  1 
ATOM   2769 C C   . SER A 1 383 ? 2.005   -7.786  3.092   1.00 13.20  ? 369 SER A C   1 
ATOM   2770 O O   . SER A 1 383 ? 2.624   -6.780  3.425   1.00 18.47  ? 369 SER A O   1 
ATOM   2771 C CB  . SER A 1 383 ? 1.869   -7.082  0.723   1.00 19.00  ? 369 SER A CB  1 
ATOM   2772 O OG  . SER A 1 383 ? 1.988   -7.489  -0.626  1.00 23.65  ? 369 SER A OG  1 
ATOM   2773 N N   . HIS A 1 384 ? 1.258   -8.502  3.937   1.00 12.49  ? 370 HIS A N   1 
ATOM   2774 C CA  . HIS A 1 384 ? 0.868   -7.995  5.234   1.00 11.16  ? 370 HIS A CA  1 
ATOM   2775 C C   . HIS A 1 384 ? 1.174   -9.021  6.311   1.00 11.13  ? 370 HIS A C   1 
ATOM   2776 O O   . HIS A 1 384 ? 0.825   -10.207 6.137   1.00 12.37  ? 370 HIS A O   1 
ATOM   2777 C CB  . HIS A 1 384 ? -0.626  -7.707  5.275   1.00 10.29  ? 370 HIS A CB  1 
ATOM   2778 C CG  . HIS A 1 384 ? -1.118  -6.836  4.171   1.00 8.63   ? 370 HIS A CG  1 
ATOM   2779 N ND1 . HIS A 1 384 ? -1.103  -5.447  4.245   1.00 11.38  ? 370 HIS A ND1 1 
ATOM   2780 C CD2 . HIS A 1 384 ? -1.524  -7.174  2.916   1.00 9.85   ? 370 HIS A CD2 1 
ATOM   2781 C CE1 . HIS A 1 384 ? -1.565  -4.965  3.079   1.00 12.95  ? 370 HIS A CE1 1 
ATOM   2782 N NE2 . HIS A 1 384 ? -1.824  -6.021  2.224   1.00 12.49  ? 370 HIS A NE2 1 
ATOM   2783 N N   . GLY A 1 385 ? 1.724   -8.554  7.443   1.00 9.47   ? 371 GLY A N   1 
ATOM   2784 C CA  . GLY A 1 385 ? 2.075   -9.495  8.501   1.00 11.60  ? 371 GLY A CA  1 
ATOM   2785 C C   . GLY A 1 385 ? 0.911   -10.333 8.996   1.00 11.33  ? 371 GLY A C   1 
ATOM   2786 O O   . GLY A 1 385 ? -0.170  -9.842  9.286   1.00 11.21  ? 371 GLY A O   1 
ATOM   2787 N N   . CYS A 1 386 ? 1.176   -11.649 9.129   1.00 10.85  ? 372 CYS A N   1 
ATOM   2788 C CA  . CYS A 1 386 ? 0.286   -12.560 9.858   1.00 11.30  ? 372 CYS A CA  1 
ATOM   2789 C C   . CYS A 1 386 ? 0.517   -12.392 11.349  1.00 12.10  ? 372 CYS A C   1 
ATOM   2790 O O   . CYS A 1 386 ? 1.318   -11.556 11.776  1.00 12.14  ? 372 CYS A O   1 
ATOM   2791 C CB  . CYS A 1 386 ? 0.460   -13.986 9.373   1.00 12.30  ? 372 CYS A CB  1 
ATOM   2792 S SG  . CYS A 1 386 ? 0.077   -14.216 7.617   1.00 14.87  ? 372 CYS A SG  1 
ATOM   2793 N N   . MET A 1 387 ? -0.182  -13.200 12.174  1.00 12.98  ? 373 MET A N   1 
ATOM   2794 C CA  . MET A 1 387 ? -0.168  -12.958 13.605  1.00 12.15  ? 373 MET A CA  1 
ATOM   2795 C C   . MET A 1 387 ? 1.231   -12.774 14.197  1.00 13.73  ? 373 MET A C   1 
ATOM   2796 O O   . MET A 1 387 ? 1.472   -11.881 15.005  1.00 12.61  ? 373 MET A O   1 
ATOM   2797 C CB  . MET A 1 387 ? -0.872  -14.083 14.366  1.00 13.79  ? 373 MET A CB  1 
ATOM   2798 C CG  . MET A 1 387 ? -2.383  -14.055 14.232  1.00 15.13  ? 373 MET A CG  1 
ATOM   2799 S SD  . MET A 1 387 ? -3.071  -15.388 15.281  1.00 19.21  ? 373 MET A SD  1 
ATOM   2800 C CE  . MET A 1 387 ? -4.773  -15.386 14.726  1.00 18.80  ? 373 MET A CE  1 
ATOM   2801 N N   . GLU A 1 388 ? 2.162   -13.682 13.870  1.00 11.92  ? 374 GLU A N   1 
ATOM   2802 C CA  . GLU A 1 388 ? 3.458   -13.640 14.527  1.00 14.79  ? 374 GLU A CA  1 
ATOM   2803 C C   . GLU A 1 388 ? 4.266   -12.395 14.115  1.00 12.73  ? 374 GLU A C   1 
ATOM   2804 O O   . GLU A 1 388 ? 5.026   -11.837 14.897  1.00 13.70  ? 374 GLU A O   1 
ATOM   2805 C CB  . GLU A 1 388 ? 4.230   -14.937 14.232  1.00 13.60  ? 374 GLU A CB  1 
ATOM   2806 C CG  . GLU A 1 388 ? 3.648   -16.194 14.871  1.00 17.22  ? 374 GLU A CG  1 
ATOM   2807 C CD  . GLU A 1 388 ? 3.535   -16.082 16.389  1.00 21.75  ? 374 GLU A CD  1 
ATOM   2808 O OE1 . GLU A 1 388 ? 4.497   -15.595 17.019  1.00 23.34  ? 374 GLU A OE1 1 
ATOM   2809 O OE2 . GLU A 1 388 ? 2.465   -16.443 16.923  1.00 26.72  ? 374 GLU A OE2 1 
ATOM   2810 N N   . GLU A 1 389 ? 4.087   -11.963 12.862  1.00 12.52  ? 375 GLU A N   1 
ATOM   2811 C CA  . GLU A 1 389 ? 4.722   -10.736 12.362  1.00 12.20  ? 375 GLU A CA  1 
ATOM   2812 C C   . GLU A 1 389 ? 4.153   -9.476  13.040  1.00 9.98   ? 375 GLU A C   1 
ATOM   2813 O O   . GLU A 1 389 ? 4.892   -8.569  13.397  1.00 11.50  ? 375 GLU A O   1 
ATOM   2814 C CB  . GLU A 1 389 ? 4.584   -10.662 10.838  1.00 11.42  ? 375 GLU A CB  1 
ATOM   2815 C CG  . GLU A 1 389 ? 5.373   -11.731 10.106  1.00 13.59  ? 375 GLU A CG  1 
ATOM   2816 C CD  . GLU A 1 389 ? 4.770   -12.052 8.741   1.00 13.01  ? 375 GLU A CD  1 
ATOM   2817 O OE1 . GLU A 1 389 ? 3.817   -12.851 8.684   1.00 14.27  ? 375 GLU A OE1 1 
ATOM   2818 O OE2 . GLU A 1 389 ? 5.170   -11.410 7.749   1.00 14.48  ? 375 GLU A OE2 1 
ATOM   2819 N N   . LEU A 1 390 ? 2.812   -9.458  13.262  1.00 10.18  ? 376 LEU A N   1 
ATOM   2820 C CA  . LEU A 1 390 ? 2.210   -8.323  13.930  1.00 10.45  ? 376 LEU A CA  1 
ATOM   2821 C C   . LEU A 1 390 ? 2.675   -8.296  15.384  1.00 11.32  ? 376 LEU A C   1 
ATOM   2822 O O   . LEU A 1 390 ? 2.902   -7.239  15.933  1.00 11.46  ? 376 LEU A O   1 
ATOM   2823 C CB  . LEU A 1 390 ? 0.699   -8.419  13.767  1.00 10.01  ? 376 LEU A CB  1 
ATOM   2824 C CG  . LEU A 1 390 ? 0.193   -8.345  12.333  1.00 9.20   ? 376 LEU A CG  1 
ATOM   2825 C CD1 . LEU A 1 390 ? -1.322  -8.354  12.274  1.00 9.91   ? 376 LEU A CD1 1 
ATOM   2826 C CD2 . LEU A 1 390 ? 0.762   -7.140  11.595  1.00 11.15  ? 376 LEU A CD2 1 
ATOM   2827 N N   . LYS A 1 391 ? 2.768   -9.495  16.010  1.00 13.44  ? 377 LYS A N   1 
ATOM   2828 C CA  . LYS A 1 391 ? 3.259   -9.540  17.387  1.00 11.87  ? 377 LYS A CA  1 
ATOM   2829 C C   . LYS A 1 391 ? 4.726   -9.105  17.495  1.00 14.62  ? 377 LYS A C   1 
ATOM   2830 O O   . LYS A 1 391 ? 5.114   -8.438  18.454  1.00 13.99  ? 377 LYS A O   1 
ATOM   2831 C CB  . LYS A 1 391 ? 3.078   -10.946 17.992  1.00 14.41  ? 377 LYS A CB  1 
ATOM   2832 C CG  . LYS A 1 391 ? 1.606   -11.269 18.274  1.00 15.38  ? 377 LYS A CG  1 
ATOM   2833 C CD  . LYS A 1 391 ? 1.430   -12.544 19.119  1.00 22.27  ? 377 LYS A CD  1 
ATOM   2834 C CE  . LYS A 1 391 ? 1.841   -13.809 18.408  1.00 24.68  ? 377 LYS A CE  1 
ATOM   2835 N NZ  . LYS A 1 391 ? 1.615   -15.040 19.227  1.00 31.77  ? 377 LYS A NZ  1 
ATOM   2836 N N   . MET A 1 392 ? 5.538   -9.472  16.479  1.00 14.11  ? 378 MET A N   1 
ATOM   2837 C CA  . MET A 1 392 ? 6.905   -8.985  16.411  1.00 14.28  ? 378 MET A CA  1 
ATOM   2838 C C   . MET A 1 392 ? 6.963   -7.447  16.443  1.00 12.02  ? 378 MET A C   1 
ATOM   2839 O O   . MET A 1 392 ? 7.709   -6.846  17.206  1.00 14.98  ? 378 MET A O   1 
ATOM   2840 C CB  . MET A 1 392 ? 7.548   -9.552  15.137  1.00 16.73  ? 378 MET A CB  1 
ATOM   2841 C CG  . MET A 1 392 ? 8.991   -9.188  14.939  1.00 22.22  ? 378 MET A CG  1 
ATOM   2842 S SD  . MET A 1 392 ? 9.709   -10.300 13.624  1.00 24.21  ? 378 MET A SD  1 
ATOM   2843 C CE  . MET A 1 392 ? 11.143  -9.328  13.153  1.00 30.00  ? 378 MET A CE  1 
ATOM   2844 N N   . MET A 1 393 ? 6.127   -6.778  15.619  1.00 11.12  ? 379 MET A N   1 
ATOM   2845 C CA  . MET A 1 393 ? 6.077   -5.323  15.595  1.00 12.07  ? 379 MET A CA  1 
ATOM   2846 C C   . MET A 1 393 ? 5.610   -4.791  16.959  1.00 12.24  ? 379 MET A C   1 
ATOM   2847 O O   . MET A 1 393 ? 6.198   -3.841  17.496  1.00 12.16  ? 379 MET A O   1 
ATOM   2848 C CB  . MET A 1 393 ? 5.146   -4.841  14.457  1.00 10.74  ? 379 MET A CB  1 
ATOM   2849 C CG  . MET A 1 393 ? 5.019   -3.322  14.374  1.00 12.13  ? 379 MET A CG  1 
ATOM   2850 S SD  . MET A 1 393 ? 6.579   -2.497  13.890  1.00 12.68  ? 379 MET A SD  1 
ATOM   2851 C CE  . MET A 1 393 ? 6.591   -2.805  12.123  1.00 13.10  ? 379 MET A CE  1 
ATOM   2852 N N   . LEU A 1 394 ? 4.564   -5.423  17.540  1.00 11.56  ? 380 LEU A N   1 
ATOM   2853 C CA  . LEU A 1 394 ? 4.082   -4.959  18.846  1.00 12.16  ? 380 LEU A CA  1 
ATOM   2854 C C   . LEU A 1 394 ? 5.146   -5.150  19.951  1.00 13.82  ? 380 LEU A C   1 
ATOM   2855 O O   . LEU A 1 394 ? 5.276   -4.329  20.841  1.00 13.30  ? 380 LEU A O   1 
ATOM   2856 C CB  . LEU A 1 394 ? 2.813   -5.758  19.155  1.00 10.83  ? 380 LEU A CB  1 
ATOM   2857 C CG  . LEU A 1 394 ? 1.530   -5.209  18.528  1.00 12.24  ? 380 LEU A CG  1 
ATOM   2858 C CD1 . LEU A 1 394 ? 0.545   -6.334  18.254  1.00 13.52  ? 380 LEU A CD1 1 
ATOM   2859 C CD2 . LEU A 1 394 ? 0.963   -4.129  19.486  1.00 12.16  ? 380 LEU A CD2 1 
ATOM   2860 N N   . ASN A 1 395 ? 5.935   -6.231  19.893  1.00 12.63  ? 381 ASN A N   1 
ATOM   2861 C CA  . ASN A 1 395 ? 6.931   -6.495  20.924  1.00 14.97  ? 381 ASN A CA  1 
ATOM   2862 C C   . ASN A 1 395 ? 8.136   -5.581  20.794  1.00 14.64  ? 381 ASN A C   1 
ATOM   2863 O O   . ASN A 1 395 ? 8.783   -5.248  21.788  1.00 16.96  ? 381 ASN A O   1 
ATOM   2864 C CB  . ASN A 1 395 ? 7.306   -7.982  20.925  1.00 15.35  ? 381 ASN A CB  1 
ATOM   2865 C CG  . ASN A 1 395 ? 6.259   -8.822  21.616  1.00 16.10  ? 381 ASN A CG  1 
ATOM   2866 O OD1 . ASN A 1 395 ? 5.627   -8.382  22.578  1.00 19.32  ? 381 ASN A OD1 1 
ATOM   2867 N ND2 . ASN A 1 395 ? 6.085   -10.034 21.139  1.00 22.51  ? 381 ASN A ND2 1 
ATOM   2868 N N   . ILE A 1 396 ? 8.474   -5.193  19.542  1.00 13.22  ? 382 ILE A N   1 
ATOM   2869 C CA  . ILE A 1 396 ? 9.580   -4.273  19.307  1.00 13.69  ? 382 ILE A CA  1 
ATOM   2870 C C   . ILE A 1 396 ? 9.196   -2.853  19.744  1.00 11.74  ? 382 ILE A C   1 
ATOM   2871 O O   . ILE A 1 396 ? 9.977   -2.116  20.347  1.00 13.61  ? 382 ILE A O   1 
ATOM   2872 C CB  . ILE A 1 396 ? 9.963   -4.319  17.820  1.00 15.64  ? 382 ILE A CB  1 
ATOM   2873 C CG1 . ILE A 1 396 ? 10.576  -5.665  17.411  1.00 15.70  ? 382 ILE A CG1 1 
ATOM   2874 C CG2 . ILE A 1 396 ? 10.880  -3.154  17.519  1.00 23.82  ? 382 ILE A CG2 1 
ATOM   2875 C CD1 . ILE A 1 396 ? 10.631  -5.804  15.906  1.00 21.44  ? 382 ILE A CD1 1 
ATOM   2876 N N   . MET A 1 397 ? 7.941   -2.470  19.452  1.00 12.41  ? 383 MET A N   1 
ATOM   2877 C CA  . MET A 1 397 ? 7.529   -1.075  19.681  1.00 11.41  ? 383 MET A CA  1 
ATOM   2878 C C   . MET A 1 397 ? 7.052   -0.830  21.120  1.00 12.28  ? 383 MET A C   1 
ATOM   2879 O O   . MET A 1 397 ? 7.147   0.297   21.595  1.00 13.10  ? 383 MET A O   1 
ATOM   2880 C CB  . MET A 1 397 ? 6.376   -0.716  18.715  1.00 11.74  ? 383 MET A CB  1 
ATOM   2881 C CG  . MET A 1 397 ? 6.854   -0.686  17.265  1.00 11.80  ? 383 MET A CG  1 
ATOM   2882 S SD  . MET A 1 397 ? 7.893   0.813   17.043  1.00 13.43  ? 383 MET A SD  1 
ATOM   2883 C CE  . MET A 1 397 ? 8.602   0.586   15.395  1.00 13.93  ? 383 MET A CE  1 
ATOM   2884 N N   . LYS A 1 398 ? 6.483   -1.859  21.761  1.00 13.90  ? 384 LYS A N   1 
ATOM   2885 C CA  . LYS A 1 398 ? 6.031   -1.744  23.158  1.00 15.30  ? 384 LYS A CA  1 
ATOM   2886 C C   . LYS A 1 398 ? 5.169   -0.496  23.350  1.00 14.66  ? 384 LYS A C   1 
ATOM   2887 O O   . LYS A 1 398 ? 5.468   0.380   24.171  1.00 14.77  ? 384 LYS A O   1 
ATOM   2888 C CB  . LYS A 1 398 ? 7.206   -1.714  24.150  1.00 16.18  ? 384 LYS A CB  1 
ATOM   2889 C CG  . LYS A 1 398 ? 7.925   -3.046  24.207  1.00 18.35  ? 384 LYS A CG  1 
ATOM   2890 C CD  . LYS A 1 398 ? 9.293   -2.955  24.880  1.00 19.06  ? 384 LYS A CD  1 
ATOM   2891 C CE  . LYS A 1 398 ? 10.313  -2.183  24.047  1.00 23.13  ? 384 LYS A CE  1 
ATOM   2892 N NZ  . LYS A 1 398 ? 11.705  -2.320  24.561  1.00 25.89  ? 384 LYS A NZ  1 
ATOM   2893 N N   . PRO A 1 399 ? 4.075   -0.329  22.563  1.00 14.09  ? 385 PRO A N   1 
ATOM   2894 C CA  . PRO A 1 399 ? 3.357   0.946   22.641  1.00 13.27  ? 385 PRO A CA  1 
ATOM   2895 C C   . PRO A 1 399 ? 2.490   1.038   23.890  1.00 11.46  ? 385 PRO A C   1 
ATOM   2896 O O   . PRO A 1 399 ? 1.991   0.026   24.393  1.00 14.44  ? 385 PRO A O   1 
ATOM   2897 C CB  . PRO A 1 399 ? 2.415   0.878   21.425  1.00 11.12  ? 385 PRO A CB  1 
ATOM   2898 C CG  . PRO A 1 399 ? 2.191   -0.624  21.213  1.00 11.72  ? 385 PRO A CG  1 
ATOM   2899 C CD  . PRO A 1 399 ? 3.524   -1.260  21.566  1.00 12.33  ? 385 PRO A CD  1 
ATOM   2900 N N   . GLU A 1 400 ? 2.275   2.277   24.341  1.00 11.69  ? 386 GLU A N   1 
ATOM   2901 C CA  . GLU A 1 400 ? 1.344   2.477   25.457  1.00 11.68  ? 386 GLU A CA  1 
ATOM   2902 C C   . GLU A 1 400 ? -0.093  2.307   24.944  1.00 12.83  ? 386 GLU A C   1 
ATOM   2903 O O   . GLU A 1 400 ? -0.885  1.589   25.560  1.00 13.59  ? 386 GLU A O   1 
ATOM   2904 C CB  . GLU A 1 400 ? 1.492   3.863   26.066  1.00 13.01  ? 386 GLU A CB  1 
ATOM   2905 C CG  . GLU A 1 400 ? 0.630   4.018   27.326  1.00 14.25  ? 386 GLU A CG  1 
ATOM   2906 C CD  . GLU A 1 400 ? 0.725   5.366   28.017  1.00 16.14  ? 386 GLU A CD  1 
ATOM   2907 O OE1 . GLU A 1 400 ? 1.455   6.249   27.525  1.00 20.16  ? 386 GLU A OE1 1 
ATOM   2908 O OE2 . GLU A 1 400 ? 0.008   5.557   29.018  1.00 21.41  ? 386 GLU A OE2 1 
ATOM   2909 N N   . TYR A 1 401 ? -0.456  3.002   23.843  1.00 11.01  ? 387 TYR A N   1 
ATOM   2910 C CA  . TYR A 1 401 ? -1.793  2.907   23.239  1.00 9.95   ? 387 TYR A CA  1 
ATOM   2911 C C   . TYR A 1 401 ? -1.656  2.240   21.862  1.00 8.99   ? 387 TYR A C   1 
ATOM   2912 O O   . TYR A 1 401 ? -0.617  2.332   21.194  1.00 9.90   ? 387 TYR A O   1 
ATOM   2913 C CB  . TYR A 1 401 ? -2.354  4.318   23.044  1.00 10.72  ? 387 TYR A CB  1 
ATOM   2914 C CG  . TYR A 1 401 ? -2.663  4.981   24.365  1.00 11.06  ? 387 TYR A CG  1 
ATOM   2915 C CD1 . TYR A 1 401 ? -3.880  4.751   24.968  1.00 11.09  ? 387 TYR A CD1 1 
ATOM   2916 C CD2 . TYR A 1 401 ? -1.744  5.805   25.031  1.00 13.54  ? 387 TYR A CD2 1 
ATOM   2917 C CE1 . TYR A 1 401 ? -4.208  5.330   26.184  1.00 12.25  ? 387 TYR A CE1 1 
ATOM   2918 C CE2 . TYR A 1 401 ? -2.044  6.383   26.270  1.00 13.53  ? 387 TYR A CE2 1 
ATOM   2919 C CZ  . TYR A 1 401 ? -3.299  6.147   26.841  1.00 14.21  ? 387 TYR A CZ  1 
ATOM   2920 O OH  . TYR A 1 401 ? -3.666  6.678   28.081  1.00 16.60  ? 387 TYR A OH  1 
ATOM   2921 N N   . PHE A 1 402 ? -2.742  1.599   21.429  1.00 9.92   ? 388 PHE A N   1 
ATOM   2922 C CA  . PHE A 1 402 ? -2.714  0.847   20.176  1.00 9.37   ? 388 PHE A CA  1 
ATOM   2923 C C   . PHE A 1 402 ? -3.969  1.089   19.355  1.00 9.12   ? 388 PHE A C   1 
ATOM   2924 O O   . PHE A 1 402 ? -5.069  1.011   19.874  1.00 10.12  ? 388 PHE A O   1 
ATOM   2925 C CB  . PHE A 1 402 ? -2.512  -0.647  20.484  1.00 9.88   ? 388 PHE A CB  1 
ATOM   2926 C CG  . PHE A 1 402 ? -2.452  -1.487  19.241  1.00 9.63   ? 388 PHE A CG  1 
ATOM   2927 C CD1 . PHE A 1 402 ? -1.421  -1.289  18.305  1.00 11.21  ? 388 PHE A CD1 1 
ATOM   2928 C CD2 . PHE A 1 402 ? -3.414  -2.444  18.968  1.00 11.26  ? 388 PHE A CD2 1 
ATOM   2929 C CE1 . PHE A 1 402 ? -1.392  -2.037  17.135  1.00 12.98  ? 388 PHE A CE1 1 
ATOM   2930 C CE2 . PHE A 1 402 ? -3.369  -3.217  17.802  1.00 11.11  ? 388 PHE A CE2 1 
ATOM   2931 C CZ  . PHE A 1 402 ? -2.344  -3.004  16.892  1.00 11.25  ? 388 PHE A CZ  1 
ATOM   2932 N N   . VAL A 1 403 ? -3.739  1.406   18.070  1.00 9.01   ? 389 VAL A N   1 
ATOM   2933 C CA  . VAL A 1 403 ? -4.811  1.702   17.149  1.00 8.26   ? 389 VAL A CA  1 
ATOM   2934 C C   . VAL A 1 403 ? -4.680  0.794   15.931  1.00 8.80   ? 389 VAL A C   1 
ATOM   2935 O O   . VAL A 1 403 ? -3.909  1.077   14.994  1.00 9.26   ? 389 VAL A O   1 
ATOM   2936 C CB  . VAL A 1 403 ? -4.822  3.184   16.737  1.00 9.58   ? 389 VAL A CB  1 
ATOM   2937 C CG1 . VAL A 1 403 ? -6.043  3.493   15.876  1.00 10.52  ? 389 VAL A CG1 1 
ATOM   2938 C CG2 . VAL A 1 403 ? -4.743  4.085   17.948  1.00 11.36  ? 389 VAL A CG2 1 
ATOM   2939 N N   . PRO A 1 404 ? -5.361  -0.377  15.898  1.00 8.98   ? 390 PRO A N   1 
ATOM   2940 C CA  . PRO A 1 404 ? -5.236  -1.233  14.720  1.00 7.44   ? 390 PRO A CA  1 
ATOM   2941 C C   . PRO A 1 404 ? -6.000  -0.634  13.548  1.00 9.21   ? 390 PRO A C   1 
ATOM   2942 O O   . PRO A 1 404 ? -7.191  -0.309  13.675  1.00 9.05   ? 390 PRO A O   1 
ATOM   2943 C CB  . PRO A 1 404 ? -5.879  -2.551  15.200  1.00 10.87  ? 390 PRO A CB  1 
ATOM   2944 C CG  . PRO A 1 404 ? -6.861  -2.139  16.282  1.00 11.06  ? 390 PRO A CG  1 
ATOM   2945 C CD  . PRO A 1 404 ? -6.184  -0.966  16.980  1.00 11.30  ? 390 PRO A CD  1 
ATOM   2946 N N   . VAL A 1 405 ? -5.329  -0.544  12.392  1.00 8.26   ? 391 VAL A N   1 
ATOM   2947 C CA  . VAL A 1 405 ? -5.969  0.027   11.205  1.00 8.43   ? 391 VAL A CA  1 
ATOM   2948 C C   . VAL A 1 405 ? -5.769  -0.932  10.030  1.00 8.15   ? 391 VAL A C   1 
ATOM   2949 O O   . VAL A 1 405 ? -5.337  -2.060  10.195  1.00 8.59   ? 391 VAL A O   1 
ATOM   2950 C CB  . VAL A 1 405 ? -5.446  1.461   10.894  1.00 6.79   ? 391 VAL A CB  1 
ATOM   2951 C CG1 . VAL A 1 405 ? -5.728  2.373   12.086  1.00 9.65   ? 391 VAL A CG1 1 
ATOM   2952 C CG2 . VAL A 1 405 ? -3.965  1.409   10.515  1.00 8.32   ? 391 VAL A CG2 1 
ATOM   2953 N N   . GLN A 1 406 ? -6.126  -0.473  8.823   1.00 7.84   ? 392 GLN A N   1 
ATOM   2954 C CA  . GLN A 1 406 ? -6.049  -1.286  7.614   1.00 8.38   ? 392 GLN A CA  1 
ATOM   2955 C C   . GLN A 1 406 ? -6.736  -2.630  7.835   1.00 8.60   ? 392 GLN A C   1 
ATOM   2956 O O   . GLN A 1 406 ? -6.117  -3.708  7.865   1.00 10.23  ? 392 GLN A O   1 
ATOM   2957 C CB  . GLN A 1 406 ? -4.637  -1.434  7.027   1.00 8.32   ? 392 GLN A CB  1 
ATOM   2958 C CG  . GLN A 1 406 ? -4.605  -2.069  5.653   1.00 11.77  ? 392 GLN A CG  1 
ATOM   2959 C CD  . GLN A 1 406 ? -5.583  -1.590  4.639   1.00 12.92  ? 392 GLN A CD  1 
ATOM   2960 O OE1 . GLN A 1 406 ? -6.025  -2.384  3.803   1.00 15.82  ? 392 GLN A OE1 1 
ATOM   2961 N NE2 . GLN A 1 406 ? -5.880  -0.298  4.665   1.00 14.66  ? 392 GLN A NE2 1 
ATOM   2962 N N   . GLY A 1 407 ? -8.053  -2.582  7.942   1.00 10.30  ? 393 GLY A N   1 
ATOM   2963 C CA  . GLY A 1 407 ? -8.811  -3.821  8.046   1.00 11.72  ? 393 GLY A CA  1 
ATOM   2964 C C   . GLY A 1 407 ? -10.291 -3.570  8.253   1.00 10.37  ? 393 GLY A C   1 
ATOM   2965 O O   . GLY A 1 407 ? -10.705 -2.543  8.719   1.00 10.20  ? 393 GLY A O   1 
ATOM   2966 N N   . GLU A 1 408 ? -11.067 -4.583  7.832   1.00 11.73  ? 394 GLU A N   1 
ATOM   2967 C CA  . GLU A 1 408 ? -12.433 -4.687  8.273   1.00 12.16  ? 394 GLU A CA  1 
ATOM   2968 C C   . GLU A 1 408 ? -12.444 -4.798  9.801   1.00 11.33  ? 394 GLU A C   1 
ATOM   2969 O O   . GLU A 1 408 ? -11.433 -5.110  10.468  1.00 10.60  ? 394 GLU A O   1 
ATOM   2970 C CB  . GLU A 1 408 ? -13.057 -5.910  7.602   1.00 15.95  ? 394 GLU A CB  1 
ATOM   2971 C CG  . GLU A 1 408 ? -13.032 -5.791  6.067   1.00 20.58  ? 394 GLU A CG  1 
ATOM   2972 C CD  . GLU A 1 408 ? -13.222 -7.010  5.175   1.00 33.99  ? 394 GLU A CD  1 
ATOM   2973 O OE1 . GLU A 1 408 ? -13.728 -8.018  5.677   1.00 24.29  ? 394 GLU A OE1 1 
ATOM   2974 O OE2 . GLU A 1 408 ? -12.811 -6.949  3.970   1.00 43.36  ? 394 GLU A OE2 1 
ATOM   2975 N N   . PHE A 1 409 ? -13.615 -4.552  10.385  1.00 14.78  ? 395 PHE A N   1 
ATOM   2976 C CA  . PHE A 1 409 ? -13.672 -4.533  11.830  1.00 12.10  ? 395 PHE A CA  1 
ATOM   2977 C C   . PHE A 1 409 ? -13.186 -5.861  12.443  1.00 13.78  ? 395 PHE A C   1 
ATOM   2978 O O   . PHE A 1 409 ? -12.476 -5.847  13.440  1.00 12.11  ? 395 PHE A O   1 
ATOM   2979 C CB  . PHE A 1 409 ? -15.083 -4.152  12.310  1.00 15.79  ? 395 PHE A CB  1 
ATOM   2980 C CG  . PHE A 1 409 ? -15.097 -3.644  13.725  1.00 20.14  ? 395 PHE A CG  1 
ATOM   2981 C CD1 . PHE A 1 409 ? -14.538 -2.400  14.042  1.00 28.41  ? 395 PHE A CD1 1 
ATOM   2982 C CD2 . PHE A 1 409 ? -15.647 -4.396  14.750  1.00 25.48  ? 395 PHE A CD2 1 
ATOM   2983 C CE1 . PHE A 1 409 ? -14.567 -1.917  15.340  1.00 31.21  ? 395 PHE A CE1 1 
ATOM   2984 C CE2 . PHE A 1 409 ? -15.663 -3.907  16.055  1.00 31.45  ? 395 PHE A CE2 1 
ATOM   2985 C CZ  . PHE A 1 409 ? -15.138 -2.672  16.339  1.00 27.32  ? 395 PHE A CZ  1 
ATOM   2986 N N   . LYS A 1 410 ? -13.533 -7.016  11.838  1.00 13.67  ? 396 LYS A N   1 
ATOM   2987 C CA  . LYS A 1 410 ? -13.094 -8.299  12.399  1.00 13.52  ? 396 LYS A CA  1 
ATOM   2988 C C   . LYS A 1 410 ? -11.560 -8.418  12.423  1.00 12.97  ? 396 LYS A C   1 
ATOM   2989 O O   . LYS A 1 410 ? -10.984 -9.066  13.282  1.00 13.59  ? 396 LYS A O   1 
ATOM   2990 C CB  . LYS A 1 410 ? -13.712 -9.457  11.621  1.00 13.95  ? 396 LYS A CB  1 
ATOM   2991 C CG  . LYS A 1 410 ? -13.358 -9.532  10.137  1.00 17.28  ? 396 LYS A CG  1 
ATOM   2992 C CD  . LYS A 1 410 ? -14.196 -10.587 9.421   1.00 23.52  ? 396 LYS A CD  1 
ATOM   2993 C CE  . LYS A 1 410 ? -13.741 -10.895 8.010   1.00 28.67  ? 396 LYS A CE  1 
ATOM   2994 N NZ  . LYS A 1 410 ? -14.609 -11.923 7.371   1.00 35.38  ? 396 LYS A NZ  1 
ATOM   2995 N N   . MET A 1 411 ? -10.910 -7.776  11.430  1.00 12.44  ? 397 MET A N   1 
ATOM   2996 C CA  . MET A 1 411 ? -9.459  -7.798  11.365  1.00 11.03  ? 397 MET A CA  1 
ATOM   2997 C C   . MET A 1 411 ? -8.884  -6.894  12.451  1.00 9.95   ? 397 MET A C   1 
ATOM   2998 O O   . MET A 1 411 ? -7.865  -7.237  13.080  1.00 10.55  ? 397 MET A O   1 
ATOM   2999 C CB  . MET A 1 411 ? -8.999  -7.301  9.989   1.00 10.13  ? 397 MET A CB  1 
ATOM   3000 C CG  . MET A 1 411 ? -9.357  -8.247  8.864   1.00 12.38  ? 397 MET A CG  1 
ATOM   3001 S SD  . MET A 1 411 ? -9.185  -7.474  7.258   1.00 14.42  ? 397 MET A SD  1 
ATOM   3002 C CE  . MET A 1 411 ? -9.872  -8.763  6.223   1.00 18.00  ? 397 MET A CE  1 
ATOM   3003 N N   . GLN A 1 412 ? -9.508  -5.704  12.641  1.00 10.69  ? 398 GLN A N   1 
ATOM   3004 C CA  . GLN A 1 412 ? -9.092  -4.816  13.714  1.00 9.49   ? 398 GLN A CA  1 
ATOM   3005 C C   . GLN A 1 412 ? -9.195  -5.511  15.080  1.00 11.12  ? 398 GLN A C   1 
ATOM   3006 O O   . GLN A 1 412 ? -8.298  -5.372  15.910  1.00 11.24  ? 398 GLN A O   1 
ATOM   3007 C CB  . GLN A 1 412 ? -9.918  -3.528  13.707  1.00 10.80  ? 398 GLN A CB  1 
ATOM   3008 C CG  . GLN A 1 412 ? -9.671  -2.667  12.469  1.00 10.87  ? 398 GLN A CG  1 
ATOM   3009 C CD  . GLN A 1 412 ? -10.655 -1.525  12.420  1.00 12.14  ? 398 GLN A CD  1 
ATOM   3010 O OE1 . GLN A 1 412 ? -11.736 -1.666  11.862  1.00 14.12  ? 398 GLN A OE1 1 
ATOM   3011 N NE2 . GLN A 1 412 ? -10.322 -0.415  13.042  1.00 12.89  ? 398 GLN A NE2 1 
ATOM   3012 N N   . ILE A 1 413 ? -10.339 -6.191  15.326  1.00 11.48  ? 399 ILE A N   1 
ATOM   3013 C CA  . ILE A 1 413 ? -10.485 -6.961  16.564  1.00 11.22  ? 399 ILE A CA  1 
ATOM   3014 C C   . ILE A 1 413 ? -9.398  -8.044  16.707  1.00 10.76  ? 399 ILE A C   1 
ATOM   3015 O O   . ILE A 1 413 ? -8.857  -8.203  17.777  1.00 11.57  ? 399 ILE A O   1 
ATOM   3016 C CB  . ILE A 1 413 ? -11.897 -7.593  16.706  1.00 14.94  ? 399 ILE A CB  1 
ATOM   3017 C CG1 . ILE A 1 413 ? -12.995 -6.530  16.826  1.00 19.13  ? 399 ILE A CG1 1 
ATOM   3018 C CG2 . ILE A 1 413 ? -11.938 -8.570  17.883  1.00 18.78  ? 399 ILE A CG2 1 
ATOM   3019 C CD1 . ILE A 1 413 ? -14.397 -7.072  16.565  1.00 25.26  ? 399 ILE A CD1 1 
ATOM   3020 N N   . ALA A 1 414 ? -9.119  -8.800  15.628  1.00 11.23  ? 400 ALA A N   1 
ATOM   3021 C CA  . ALA A 1 414 ? -8.094  -9.827  15.735  1.00 11.19  ? 400 ALA A CA  1 
ATOM   3022 C C   . ALA A 1 414 ? -6.751  -9.201  16.125  1.00 11.50  ? 400 ALA A C   1 
ATOM   3023 O O   . ALA A 1 414 ? -5.988  -9.758  16.908  1.00 13.46  ? 400 ALA A O   1 
ATOM   3024 C CB  . ALA A 1 414 ? -7.955  -10.596 14.457  1.00 12.04  ? 400 ALA A CB  1 
ATOM   3025 N N   . HIS A 1 415 ? -6.453  -7.988  15.561  1.00 11.16  ? 401 HIS A N   1 
ATOM   3026 C CA  . HIS A 1 415 ? -5.180  -7.330  15.833  1.00 9.69   ? 401 HIS A CA  1 
ATOM   3027 C C   . HIS A 1 415 ? -5.165  -6.805  17.268  1.00 10.18  ? 401 HIS A C   1 
ATOM   3028 O O   . HIS A 1 415 ? -4.161  -6.921  17.957  1.00 11.38  ? 401 HIS A O   1 
ATOM   3029 C CB  . HIS A 1 415 ? -4.968  -6.179  14.832  1.00 9.79   ? 401 HIS A CB  1 
ATOM   3030 C CG  . HIS A 1 415 ? -3.546  -5.743  14.668  1.00 8.62   ? 401 HIS A CG  1 
ATOM   3031 N ND1 . HIS A 1 415 ? -3.165  -4.859  13.640  1.00 8.31   ? 401 HIS A ND1 1 
ATOM   3032 C CD2 . HIS A 1 415 ? -2.413  -6.091  15.355  1.00 10.60  ? 401 HIS A CD2 1 
ATOM   3033 C CE1 . HIS A 1 415 ? -1.834  -4.736  13.696  1.00 10.07  ? 401 HIS A CE1 1 
ATOM   3034 N NE2 . HIS A 1 415 ? -1.346  -5.477  14.749  1.00 10.72  ? 401 HIS A NE2 1 
ATOM   3035 N N   . ALA A 1 416 ? -6.318  -6.287  17.754  1.00 10.96  ? 402 ALA A N   1 
ATOM   3036 C CA  . ALA A 1 416 ? -6.421  -5.861  19.139  1.00 12.23  ? 402 ALA A CA  1 
ATOM   3037 C C   . ALA A 1 416 ? -6.142  -7.050  20.089  1.00 11.78  ? 402 ALA A C   1 
ATOM   3038 O O   . ALA A 1 416 ? -5.455  -6.878  21.105  1.00 12.83  ? 402 ALA A O   1 
ATOM   3039 C CB  . ALA A 1 416 ? -7.798  -5.320  19.407  1.00 11.52  ? 402 ALA A CB  1 
ATOM   3040 N N   . LYS A 1 417 ? -6.637  -8.257  19.741  1.00 11.01  ? 403 LYS A N   1 
ATOM   3041 C CA  . LYS A 1 417 ? -6.368  -9.457  20.548  1.00 12.90  ? 403 LYS A CA  1 
ATOM   3042 C C   . LYS A 1 417 ? -4.864  -9.747  20.627  1.00 12.53  ? 403 LYS A C   1 
ATOM   3043 O O   . LYS A 1 417 ? -4.336  -10.038 21.706  1.00 15.84  ? 403 LYS A O   1 
ATOM   3044 C CB  . LYS A 1 417 ? -7.156  -10.658 20.023  1.00 13.84  ? 403 LYS A CB  1 
ATOM   3045 C CG  . LYS A 1 417 ? -8.676  -10.590 20.226  1.00 17.74  ? 403 LYS A CG  1 
ATOM   3046 C CD  . LYS A 1 417 ? -9.522  -11.709 19.547  1.00 20.32  ? 403 LYS A CD  1 
ATOM   3047 C CE  . LYS A 1 417 ? -11.002 -11.535 19.858  1.00 22.38  ? 403 LYS A CE  1 
ATOM   3048 N NZ  . LYS A 1 417 ? -11.892 -12.467 19.084  1.00 22.43  ? 403 LYS A NZ  1 
ATOM   3049 N N   . LEU A 1 418 ? -4.151  -9.584  19.502  1.00 12.43  ? 404 LEU A N   1 
ATOM   3050 C CA  . LEU A 1 418 ? -2.710  -9.756  19.491  1.00 12.67  ? 404 LEU A CA  1 
ATOM   3051 C C   . LEU A 1 418 ? -2.060  -8.741  20.420  1.00 13.97  ? 404 LEU A C   1 
ATOM   3052 O O   . LEU A 1 418 ? -1.101  -9.024  21.140  1.00 15.65  ? 404 LEU A O   1 
ATOM   3053 C CB  . LEU A 1 418 ? -2.147  -9.617  18.059  1.00 12.84  ? 404 LEU A CB  1 
ATOM   3054 C CG  . LEU A 1 418 ? -2.717  -10.603 17.050  1.00 13.26  ? 404 LEU A CG  1 
ATOM   3055 C CD1 . LEU A 1 418 ? -2.142  -10.362 15.641  1.00 14.42  ? 404 LEU A CD1 1 
ATOM   3056 C CD2 . LEU A 1 418 ? -2.388  -12.029 17.500  1.00 15.80  ? 404 LEU A CD2 1 
ATOM   3057 N N   . ALA A 1 419 ? -2.453  -7.462  20.320  1.00 12.02  ? 405 ALA A N   1 
ATOM   3058 C CA  . ALA A 1 419 ? -1.816  -6.450  21.167  1.00 12.79  ? 405 ALA A CA  1 
ATOM   3059 C C   . ALA A 1 419 ? -2.000  -6.768  22.651  1.00 12.87  ? 405 ALA A C   1 
ATOM   3060 O O   . ALA A 1 419 ? -1.056  -6.603  23.426  1.00 14.26  ? 405 ALA A O   1 
ATOM   3061 C CB  . ALA A 1 419 ? -2.363  -5.078  20.875  1.00 13.40  ? 405 ALA A CB  1 
ATOM   3062 N N   . ALA A 1 420 ? -3.220  -7.190  23.027  1.00 13.81  ? 406 ALA A N   1 
ATOM   3063 C CA  . ALA A 1 420 ? -3.466  -7.578  24.422  1.00 14.97  ? 406 ALA A CA  1 
ATOM   3064 C C   . ALA A 1 420 ? -2.535  -8.733  24.812  1.00 15.00  ? 406 ALA A C   1 
ATOM   3065 O O   . ALA A 1 420 ? -2.013  -8.742  25.920  1.00 19.32  ? 406 ALA A O   1 
ATOM   3066 C CB  . ALA A 1 420 ? -4.928  -7.917  24.620  1.00 16.65  ? 406 ALA A CB  1 
ATOM   3067 N N   . GLU A 1 421 ? -2.329  -9.697  23.901  1.00 14.42  ? 407 GLU A N   1 
ATOM   3068 C CA  . GLU A 1 421 ? -1.474  -10.841 24.207  1.00 16.71  ? 407 GLU A CA  1 
ATOM   3069 C C   . GLU A 1 421 ? -0.043  -10.357 24.493  1.00 18.05  ? 407 GLU A C   1 
ATOM   3070 O O   . GLU A 1 421 ? 0.659   -10.907 25.357  1.00 20.79  ? 407 GLU A O   1 
ATOM   3071 C CB  . GLU A 1 421 ? -1.565  -11.791 23.013  1.00 20.64  ? 407 GLU A CB  1 
ATOM   3072 C CG  . GLU A 1 421 ? -0.622  -12.969 23.019  1.00 27.70  ? 407 GLU A CG  1 
ATOM   3073 C CD  . GLU A 1 421 ? -0.862  -13.889 21.828  1.00 29.92  ? 407 GLU A CD  1 
ATOM   3074 O OE1 . GLU A 1 421 ? -0.073  -14.841 21.674  1.00 49.63  ? 407 GLU A OE1 1 
ATOM   3075 O OE2 . GLU A 1 421 ? -1.829  -13.636 21.030  1.00 32.11  ? 407 GLU A OE2 1 
ATOM   3076 N N   . THR A 1 422 ? 0.403   -9.314  23.768  1.00 15.51  ? 408 THR A N   1 
ATOM   3077 C CA  . THR A 1 422 ? 1.783   -8.858  23.912  1.00 15.49  ? 408 THR A CA  1 
ATOM   3078 C C   . THR A 1 422 ? 1.942   -7.973  25.140  1.00 17.57  ? 408 THR A C   1 
ATOM   3079 O O   . THR A 1 422 ? 3.063   -7.545  25.452  1.00 19.28  ? 408 THR A O   1 
ATOM   3080 C CB  . THR A 1 422 ? 2.313   -8.135  22.665  1.00 17.86  ? 408 THR A CB  1 
ATOM   3081 O OG1 . THR A 1 422 ? 1.652   -6.869  22.496  1.00 15.98  ? 408 THR A OG1 1 
ATOM   3082 C CG2 . THR A 1 422 ? 2.216   -8.981  21.417  1.00 16.56  ? 408 THR A CG2 1 
ATOM   3083 N N   . GLY A 1 423 ? 0.820   -7.623  25.782  1.00 16.32  ? 409 GLY A N   1 
ATOM   3084 C CA  . GLY A 1 423 ? 0.907   -6.818  26.985  1.00 17.67  ? 409 GLY A CA  1 
ATOM   3085 C C   . GLY A 1 423 ? 0.408   -5.377  26.870  1.00 18.01  ? 409 GLY A C   1 
ATOM   3086 O O   . GLY A 1 423 ? 0.531   -4.603  27.822  1.00 20.67  ? 409 GLY A O   1 
ATOM   3087 N N   . VAL A 1 424 ? -0.215  -5.000  25.740  1.00 16.33  ? 410 VAL A N   1 
ATOM   3088 C CA  . VAL A 1 424 ? -0.828  -3.685  25.705  1.00 14.67  ? 410 VAL A CA  1 
ATOM   3089 C C   . VAL A 1 424 ? -2.041  -3.735  26.641  1.00 15.14  ? 410 VAL A C   1 
ATOM   3090 O O   . VAL A 1 424 ? -2.817  -4.687  26.566  1.00 15.99  ? 410 VAL A O   1 
ATOM   3091 C CB  . VAL A 1 424 ? -1.215  -3.265  24.266  1.00 15.20  ? 410 VAL A CB  1 
ATOM   3092 C CG1 . VAL A 1 424 ? -1.917  -1.916  24.277  1.00 13.68  ? 410 VAL A CG1 1 
ATOM   3093 C CG2 . VAL A 1 424 ? 0.018   -3.170  23.377  1.00 13.74  ? 410 VAL A CG2 1 
ATOM   3094 N N   . ALA A 1 425 ? -2.213  -2.695  27.479  1.00 15.66  ? 411 ALA A N   1 
ATOM   3095 C CA  . ALA A 1 425 ? -3.387  -2.673  28.349  1.00 15.73  ? 411 ALA A CA  1 
ATOM   3096 C C   . ALA A 1 425 ? -4.649  -2.646  27.489  1.00 17.42  ? 411 ALA A C   1 
ATOM   3097 O O   . ALA A 1 425 ? -4.750  -1.786  26.606  1.00 15.19  ? 411 ALA A O   1 
ATOM   3098 C CB  . ALA A 1 425 ? -3.299  -1.466  29.277  1.00 18.32  ? 411 ALA A CB  1 
ATOM   3099 N N   . PRO A 1 426 ? -5.653  -3.531  27.741  1.00 18.51  ? 412 PRO A N   1 
ATOM   3100 C CA  . PRO A 1 426 ? -6.856  -3.593  26.900  1.00 19.58  ? 412 PRO A CA  1 
ATOM   3101 C C   . PRO A 1 426 ? -7.632  -2.276  26.807  1.00 18.28  ? 412 PRO A C   1 
ATOM   3102 O O   . PRO A 1 426 ? -8.186  -1.979  25.750  1.00 17.68  ? 412 PRO A O   1 
ATOM   3103 C CB  . PRO A 1 426 ? -7.717  -4.730  27.484  1.00 23.61  ? 412 PRO A CB  1 
ATOM   3104 C CG  . PRO A 1 426 ? -7.086  -5.024  28.831  1.00 32.44  ? 412 PRO A CG  1 
ATOM   3105 C CD  . PRO A 1 426 ? -5.639  -4.601  28.767  1.00 21.44  ? 412 PRO A CD  1 
ATOM   3106 N N   . GLU A 1 427 ? -7.657  -1.496  27.899  1.00 17.56  ? 413 GLU A N   1 
ATOM   3107 C CA  . GLU A 1 427 ? -8.387  -0.238  27.882  1.00 16.35  ? 413 GLU A CA  1 
ATOM   3108 C C   . GLU A 1 427 ? -7.650  0.850   27.106  1.00 16.10  ? 413 GLU A C   1 
ATOM   3109 O O   . GLU A 1 427 ? -8.199  1.951   26.943  1.00 16.81  ? 413 GLU A O   1 
ATOM   3110 C CB  . GLU A 1 427 ? -8.677  0.193   29.316  1.00 20.73  ? 413 GLU A CB  1 
ATOM   3111 C CG  . GLU A 1 427 ? -7.486  0.747   30.065  1.00 24.43  ? 413 GLU A CG  1 
ATOM   3112 C CD  . GLU A 1 427 ? -6.475  -0.168  30.747  1.00 37.31  ? 413 GLU A CD  1 
ATOM   3113 O OE1 . GLU A 1 427 ? -6.655  -1.462  30.737  1.00 29.72  ? 413 GLU A OE1 1 
ATOM   3114 O OE2 . GLU A 1 427 ? -5.501  0.430   31.308  1.00 32.79  ? 413 GLU A OE2 1 
ATOM   3115 N N   . LYS A 1 428 ? -6.394  0.562   26.709  1.00 13.43  ? 414 LYS A N   1 
ATOM   3116 C CA  . LYS A 1 428 ? -5.598  1.460   25.868  1.00 14.05  ? 414 LYS A CA  1 
ATOM   3117 C C   . LYS A 1 428 ? -5.584  1.035   24.392  1.00 11.59  ? 414 LYS A C   1 
ATOM   3118 O O   . LYS A 1 428 ? -4.808  1.588   23.597  1.00 12.36  ? 414 LYS A O   1 
ATOM   3119 C CB  . LYS A 1 428 ? -4.199  1.616   26.485  1.00 12.49  ? 414 LYS A CB  1 
ATOM   3120 C CG  . LYS A 1 428 ? -4.220  2.272   27.866  1.00 12.66  ? 414 LYS A CG  1 
ATOM   3121 C CD  . LYS A 1 428 ? -2.825  2.611   28.359  1.00 13.08  ? 414 LYS A CD  1 
ATOM   3122 C CE  . LYS A 1 428 ? -2.863  3.226   29.739  1.00 17.08  ? 414 LYS A CE  1 
ATOM   3123 N NZ  . LYS A 1 428 ? -1.480  3.556   30.204  1.00 19.24  ? 414 LYS A NZ  1 
ATOM   3124 N N   . ILE A 1 429 ? -6.475  0.120   24.019  1.00 12.74  ? 415 ILE A N   1 
ATOM   3125 C CA  . ILE A 1 429 ? -6.649  -0.280  22.630  1.00 11.53  ? 415 ILE A CA  1 
ATOM   3126 C C   . ILE A 1 429 ? -7.910  0.379   22.099  1.00 10.65  ? 415 ILE A C   1 
ATOM   3127 O O   . ILE A 1 429 ? -8.995  0.246   22.689  1.00 13.32  ? 415 ILE A O   1 
ATOM   3128 C CB  . ILE A 1 429 ? -6.753  -1.812  22.478  1.00 11.50  ? 415 ILE A CB  1 
ATOM   3129 C CG1 . ILE A 1 429 ? -5.486  -2.498  22.999  1.00 13.74  ? 415 ILE A CG1 1 
ATOM   3130 C CG2 . ILE A 1 429 ? -7.063  -2.164  21.019  1.00 13.96  ? 415 ILE A CG2 1 
ATOM   3131 C CD1 . ILE A 1 429 ? -5.629  -4.029  23.117  1.00 16.16  ? 415 ILE A CD1 1 
ATOM   3132 N N   . PHE A 1 430 ? -7.789  1.095   20.971  1.00 12.05  ? 416 PHE A N   1 
ATOM   3133 C CA  . PHE A 1 430 ? -8.906  1.849   20.397  1.00 11.88  ? 416 PHE A CA  1 
ATOM   3134 C C   . PHE A 1 430 ? -9.307  1.258   19.061  1.00 12.12  ? 416 PHE A C   1 
ATOM   3135 O O   . PHE A 1 430 ? -8.498  1.252   18.145  1.00 16.46  ? 416 PHE A O   1 
ATOM   3136 C CB  . PHE A 1 430 ? -8.543  3.344   20.307  1.00 12.80  ? 416 PHE A CB  1 
ATOM   3137 C CG  . PHE A 1 430 ? -8.647  4.027   21.652  1.00 14.25  ? 416 PHE A CG  1 
ATOM   3138 C CD1 . PHE A 1 430 ? -7.635  3.919   22.589  1.00 14.46  ? 416 PHE A CD1 1 
ATOM   3139 C CD2 . PHE A 1 430 ? -9.800  4.734   21.997  1.00 15.73  ? 416 PHE A CD2 1 
ATOM   3140 C CE1 . PHE A 1 430 ? -7.755  4.493   23.835  1.00 13.75  ? 416 PHE A CE1 1 
ATOM   3141 C CE2 . PHE A 1 430 ? -9.920  5.335   23.245  1.00 16.14  ? 416 PHE A CE2 1 
ATOM   3142 C CZ  . PHE A 1 430 ? -8.909  5.183   24.175  1.00 15.39  ? 416 PHE A CZ  1 
ATOM   3143 N N   . LEU A 1 431 ? -10.554 0.799   18.956  1.00 11.79  ? 417 LEU A N   1 
ATOM   3144 C CA  . LEU A 1 431 ? -11.100 0.225   17.734  1.00 13.95  ? 417 LEU A CA  1 
ATOM   3145 C C   . LEU A 1 431 ? -11.969 1.293   17.110  1.00 14.25  ? 417 LEU A C   1 
ATOM   3146 O O   . LEU A 1 431 ? -13.036 1.573   17.657  1.00 17.70  ? 417 LEU A O   1 
ATOM   3147 C CB  . LEU A 1 431 ? -12.016 -0.963  18.074  1.00 17.26  ? 417 LEU A CB  1 
ATOM   3148 C CG  . LEU A 1 431 ? -11.370 -2.207  18.672  1.00 19.07  ? 417 LEU A CG  1 
ATOM   3149 C CD1 . LEU A 1 431 ? -12.442 -3.214  19.097  1.00 24.84  ? 417 LEU A CD1 1 
ATOM   3150 C CD2 . LEU A 1 431 ? -10.429 -2.843  17.674  1.00 23.59  ? 417 LEU A CD2 1 
ATOM   3151 N N   . VAL A 1 432 ? -11.520 1.842   15.997  1.00 10.78  ? 418 VAL A N   1 
ATOM   3152 C CA  . VAL A 1 432 ? -12.119 3.045   15.437  1.00 13.12  ? 418 VAL A CA  1 
ATOM   3153 C C   . VAL A 1 432 ? -12.760 2.777   14.087  1.00 11.84  ? 418 VAL A C   1 
ATOM   3154 O O   . VAL A 1 432 ? -12.366 1.846   13.382  1.00 12.22  ? 418 VAL A O   1 
ATOM   3155 C CB  . VAL A 1 432 ? -11.120 4.221   15.331  1.00 18.03  ? 418 VAL A CB  1 
ATOM   3156 C CG1 . VAL A 1 432 ? -10.738 4.683   16.725  1.00 28.74  ? 418 VAL A CG1 1 
ATOM   3157 C CG2 . VAL A 1 432 ? -9.895  3.834   14.509  1.00 22.42  ? 418 VAL A CG2 1 
ATOM   3158 N N   . GLU A 1 433 ? -13.711 3.681   13.761  1.00 10.95  ? 419 GLU A N   1 
ATOM   3159 C CA  . GLU A 1 433 ? -14.369 3.735   12.472  1.00 11.18  ? 419 GLU A CA  1 
ATOM   3160 C C   . GLU A 1 433 ? -13.938 5.019   11.778  1.00 9.17   ? 419 GLU A C   1 
ATOM   3161 O O   . GLU A 1 433 ? -13.436 5.933   12.420  1.00 9.18   ? 419 GLU A O   1 
ATOM   3162 C CB  . GLU A 1 433 ? -15.900 3.790   12.583  1.00 13.59  ? 419 GLU A CB  1 
ATOM   3163 C CG  . GLU A 1 433 ? -16.434 2.594   13.337  1.00 18.47  ? 419 GLU A CG  1 
ATOM   3164 C CD  . GLU A 1 433 ? -17.937 2.667   13.547  1.00 29.92  ? 419 GLU A CD  1 
ATOM   3165 O OE1 . GLU A 1 433 ? -18.535 3.542   12.939  1.00 39.84  ? 419 GLU A OE1 1 
ATOM   3166 O OE2 . GLU A 1 433 ? -18.466 1.874   14.318  1.00 46.40  ? 419 GLU A OE2 1 
ATOM   3167 N N   . LYS A 1 434 ? -14.167 5.087   10.460  1.00 8.70   ? 420 LYS A N   1 
ATOM   3168 C CA  . LYS A 1 434 ? -13.844 6.298   9.716   1.00 8.08   ? 420 LYS A CA  1 
ATOM   3169 C C   . LYS A 1 434 ? -14.517 7.489   10.398  1.00 9.83   ? 420 LYS A C   1 
ATOM   3170 O O   . LYS A 1 434 ? -15.723 7.494   10.734  1.00 9.65   ? 420 LYS A O   1 
ATOM   3171 C CB  . LYS A 1 434 ? -14.209 6.197   8.237   1.00 10.05  ? 420 LYS A CB  1 
ATOM   3172 C CG  . LYS A 1 434 ? -13.326 5.245   7.424   1.00 10.81  ? 420 LYS A CG  1 
ATOM   3173 C CD  . LYS A 1 434 ? -13.735 5.140   5.936   1.00 11.18  ? 420 LYS A CD  1 
ATOM   3174 C CE  . LYS A 1 434 ? -15.091 4.483   5.726   1.00 13.19  ? 420 LYS A CE  1 
ATOM   3175 N NZ  . LYS A 1 434 ? -15.080 3.030   6.027   1.00 16.05  ? 420 LYS A NZ  1 
ATOM   3176 N N   . GLY A 1 435 ? -13.771 8.586   10.539  1.00 9.14   ? 421 GLY A N   1 
ATOM   3177 C CA  . GLY A 1 435 ? -14.243 9.843   11.102  1.00 9.01   ? 421 GLY A CA  1 
ATOM   3178 C C   . GLY A 1 435 ? -14.172 9.920   12.619  1.00 7.84   ? 421 GLY A C   1 
ATOM   3179 O O   . GLY A 1 435 ? -14.405 10.989  13.169  1.00 9.59   ? 421 GLY A O   1 
ATOM   3180 N N   . ASP A 1 436 ? -13.849 8.812   13.304  1.00 7.82   ? 422 ASP A N   1 
ATOM   3181 C CA  . ASP A 1 436 ? -13.695 8.898   14.750  1.00 9.29   ? 422 ASP A CA  1 
ATOM   3182 C C   . ASP A 1 436 ? -12.487 9.744   15.106  1.00 8.02   ? 422 ASP A C   1 
ATOM   3183 O O   . ASP A 1 436 ? -11.456 9.661   14.451  1.00 10.48  ? 422 ASP A O   1 
ATOM   3184 C CB  . ASP A 1 436 ? -13.512 7.497   15.362  1.00 10.27  ? 422 ASP A CB  1 
ATOM   3185 C CG  . ASP A 1 436 ? -14.809 6.708   15.505  1.00 13.33  ? 422 ASP A CG  1 
ATOM   3186 O OD1 . ASP A 1 436 ? -15.872 7.284   15.383  1.00 16.38  ? 422 ASP A OD1 1 
ATOM   3187 O OD2 . ASP A 1 436 ? -14.733 5.469   15.694  1.00 14.24  ? 422 ASP A OD2 1 
ATOM   3188 N N   . VAL A 1 437 ? -12.578 10.460  16.229  1.00 8.18   ? 423 VAL A N   1 
ATOM   3189 C CA  . VAL A 1 437 ? -11.454 11.196  16.764  1.00 7.76   ? 423 VAL A CA  1 
ATOM   3190 C C   . VAL A 1 437 ? -10.969 10.571  18.069  1.00 9.60   ? 423 VAL A C   1 
ATOM   3191 O O   . VAL A 1 437 ? -11.664 10.655  19.083  1.00 9.91   ? 423 VAL A O   1 
ATOM   3192 C CB  . VAL A 1 437 ? -11.828 12.680  16.994  1.00 8.98   ? 423 VAL A CB  1 
ATOM   3193 C CG1 . VAL A 1 437 ? -10.622 13.428  17.508  1.00 9.99   ? 423 VAL A CG1 1 
ATOM   3194 C CG2 . VAL A 1 437 ? -12.438 13.354  15.754  1.00 10.36  ? 423 VAL A CG2 1 
ATOM   3195 N N   . ILE A 1 438 ? -9.763  9.996   18.066  1.00 8.90   ? 424 ILE A N   1 
ATOM   3196 C CA  . ILE A 1 438 ? -9.106  9.578   19.290  1.00 9.14   ? 424 ILE A CA  1 
ATOM   3197 C C   . ILE A 1 438 ? -8.339  10.816  19.737  1.00 9.37   ? 424 ILE A C   1 
ATOM   3198 O O   . ILE A 1 438 ? -7.605  11.429  18.937  1.00 11.37  ? 424 ILE A O   1 
ATOM   3199 C CB  . ILE A 1 438 ? -8.158  8.384   19.033  1.00 11.58  ? 424 ILE A CB  1 
ATOM   3200 C CG1 . ILE A 1 438 ? -8.833  7.126   18.503  1.00 14.34  ? 424 ILE A CG1 1 
ATOM   3201 C CG2 . ILE A 1 438 ? -7.373  8.109   20.295  1.00 14.07  ? 424 ILE A CG2 1 
ATOM   3202 C CD1 . ILE A 1 438 ? -7.832  6.179   17.822  1.00 17.28  ? 424 ILE A CD1 1 
ATOM   3203 N N   . SER A 1 439 ? -8.484  11.221  21.003  1.00 9.65   ? 425 SER A N   1 
ATOM   3204 C CA  . SER A 1 439 ? -7.787  12.426  21.472  1.00 11.87  ? 425 SER A CA  1 
ATOM   3205 C C   . SER A 1 439 ? -7.143  12.216  22.837  1.00 9.03   ? 425 SER A C   1 
ATOM   3206 O O   . SER A 1 439 ? -7.671  11.464  23.668  1.00 12.43  ? 425 SER A O   1 
ATOM   3207 C CB  . SER A 1 439 ? -8.635  13.676  21.426  1.00 14.64  ? 425 SER A CB  1 
ATOM   3208 O OG  . SER A 1 439 ? -9.725  13.591  22.299  1.00 16.13  ? 425 SER A OG  1 
ATOM   3209 N N   . TYR A 1 440 ? -5.996  12.875  23.076  1.00 9.59   ? 426 TYR A N   1 
ATOM   3210 C CA  . TYR A 1 440 ? -5.269  12.799  24.337  1.00 9.89   ? 426 TYR A CA  1 
ATOM   3211 C C   . TYR A 1 440 ? -4.955  14.221  24.799  1.00 12.12  ? 426 TYR A C   1 
ATOM   3212 O O   . TYR A 1 440 ? -4.573  15.071  23.980  1.00 15.11  ? 426 TYR A O   1 
ATOM   3213 C CB  . TYR A 1 440 ? -3.970  12.029  24.146  1.00 13.88  ? 426 TYR A CB  1 
ATOM   3214 C CG  . TYR A 1 440 ? -3.209  11.717  25.400  1.00 15.49  ? 426 TYR A CG  1 
ATOM   3215 C CD1 . TYR A 1 440 ? -3.753  10.853  26.335  1.00 13.80  ? 426 TYR A CD1 1 
ATOM   3216 C CD2 . TYR A 1 440 ? -1.942  12.228  25.648  1.00 16.64  ? 426 TYR A CD2 1 
ATOM   3217 C CE1 . TYR A 1 440 ? -3.036  10.466  27.463  1.00 15.27  ? 426 TYR A CE1 1 
ATOM   3218 C CE2 . TYR A 1 440 ? -1.209  11.856  26.771  1.00 17.26  ? 426 TYR A CE2 1 
ATOM   3219 C CZ  . TYR A 1 440 ? -1.766  10.979  27.683  1.00 14.24  ? 426 TYR A CZ  1 
ATOM   3220 O OH  . TYR A 1 440 ? -1.092  10.584  28.806  1.00 22.08  ? 426 TYR A OH  1 
ATOM   3221 N N   . ASN A 1 441 ? -5.078  14.463  26.119  1.00 13.31  ? 427 ASN A N   1 
ATOM   3222 C CA  . ASN A 1 441 ? -4.831  15.800  26.669  1.00 14.51  ? 427 ASN A CA  1 
ATOM   3223 C C   . ASN A 1 441 ? -3.730  15.757  27.726  1.00 18.48  ? 427 ASN A C   1 
ATOM   3224 O O   . ASN A 1 441 ? -3.626  16.703  28.508  1.00 19.52  ? 427 ASN A O   1 
ATOM   3225 C CB  . ASN A 1 441 ? -6.094  16.364  27.337  1.00 14.58  ? 427 ASN A CB  1 
ATOM   3226 C CG  . ASN A 1 441 ? -6.517  15.539  28.533  1.00 16.30  ? 427 ASN A CG  1 
ATOM   3227 O OD1 . ASN A 1 441 ? -6.020  14.446  28.731  1.00 14.50  ? 427 ASN A OD1 1 
ATOM   3228 N ND2 . ASN A 1 441 ? -7.473  16.017  29.301  1.00 19.51  ? 427 ASN A ND2 1 
ATOM   3229 N N   . GLY A 1 442 ? -2.958  14.666  27.794  1.00 16.20  ? 428 GLY A N   1 
ATOM   3230 C CA  . GLY A 1 442 ? -1.898  14.488  28.783  1.00 15.84  ? 428 GLY A CA  1 
ATOM   3231 C C   . GLY A 1 442 ? -2.377  13.737  30.025  1.00 19.78  ? 428 GLY A C   1 
ATOM   3232 O O   . GLY A 1 442 ? -1.562  13.476  30.917  1.00 23.63  ? 428 GLY A O   1 
ATOM   3233 N N   . LYS A 1 443 ? -3.694  13.488  30.126  1.00 17.55  ? 429 LYS A N   1 
ATOM   3234 C CA  . LYS A 1 443 ? -4.281  12.795  31.268  1.00 21.39  ? 429 LYS A CA  1 
ATOM   3235 C C   . LYS A 1 443 ? -5.048  11.568  30.774  1.00 23.17  ? 429 LYS A C   1 
ATOM   3236 O O   . LYS A 1 443 ? -4.763  10.447  31.175  1.00 28.97  ? 429 LYS A O   1 
ATOM   3237 C CB  . LYS A 1 443 ? -5.156  13.732  32.121  1.00 23.83  ? 429 LYS A CB  1 
ATOM   3238 C CG  . LYS A 1 443 ? -4.509  15.025  32.627  1.00 27.49  ? 429 LYS A CG  1 
ATOM   3239 C CD  . LYS A 1 443 ? -5.480  16.208  32.861  1.00 33.12  ? 429 LYS A CD  1 
ATOM   3240 C CE  . LYS A 1 443 ? -4.790  17.556  32.752  1.00 55.18  ? 429 LYS A CE  1 
ATOM   3241 N NZ  . LYS A 1 443 ? -5.560  18.501  31.905  1.00 42.42  ? 429 LYS A NZ  1 
ATOM   3242 N N   . ASP A 1 444 ? -5.994  11.768  29.840  1.00 16.58  ? 430 ASP A N   1 
ATOM   3243 C CA  . ASP A 1 444 ? -6.860  10.678  29.405  1.00 16.27  ? 430 ASP A CA  1 
ATOM   3244 C C   . ASP A 1 444 ? -6.894  10.602  27.879  1.00 12.39  ? 430 ASP A C   1 
ATOM   3245 O O   . ASP A 1 444 ? -6.885  11.643  27.232  1.00 13.01  ? 430 ASP A O   1 
ATOM   3246 C CB  . ASP A 1 444 ? -8.297  10.907  29.885  1.00 15.09  ? 430 ASP A CB  1 
ATOM   3247 C CG  . ASP A 1 444 ? -8.427  10.813  31.401  1.00 19.69  ? 430 ASP A CG  1 
ATOM   3248 O OD1 . ASP A 1 444 ? -8.365  9.700   31.882  1.00 26.99  ? 430 ASP A OD1 1 
ATOM   3249 O OD2 . ASP A 1 444 ? -8.499  11.870  32.071  1.00 20.91  ? 430 ASP A OD2 1 
ATOM   3250 N N   . MET A 1 445 ? -6.935  9.377   27.352  1.00 14.02  ? 431 MET A N   1 
ATOM   3251 C CA  A MET A 1 445 ? -7.190  9.132   25.936  0.50 12.74  ? 431 MET A CA  1 
ATOM   3252 C CA  B MET A 1 445 ? -7.196  9.124   25.948  0.50 13.63  ? 431 MET A CA  1 
ATOM   3253 C C   . MET A 1 445 ? -8.678  8.804   25.794  1.00 12.23  ? 431 MET A C   1 
ATOM   3254 O O   . MET A 1 445 ? -9.217  7.917   26.472  1.00 14.70  ? 431 MET A O   1 
ATOM   3255 C CB  A MET A 1 445 ? -6.310  8.015   25.340  0.50 12.85  ? 431 MET A CB  1 
ATOM   3256 C CB  B MET A 1 445 ? -6.371  7.929   25.478  0.50 14.99  ? 431 MET A CB  1 
ATOM   3257 C CG  A MET A 1 445 ? -6.516  7.783   23.811  0.50 9.60   ? 431 MET A CG  1 
ATOM   3258 C CG  B MET A 1 445 ? -5.097  8.343   24.794  0.50 28.00  ? 431 MET A CG  1 
ATOM   3259 S SD  A MET A 1 445 ? -5.355  6.794   22.766  0.50 20.35  ? 431 MET A SD  1 
ATOM   3260 S SD  B MET A 1 445 ? -5.390  8.972   23.111  0.50 12.38  ? 431 MET A SD  1 
ATOM   3261 C CE  A MET A 1 445 ? -3.899  7.835   22.854  0.50 15.18  ? 431 MET A CE  1 
ATOM   3262 C CE  B MET A 1 445 ? -4.079  8.049   22.304  0.50 20.58  ? 431 MET A CE  1 
ATOM   3263 N N   . ILE A 1 446 ? -9.332  9.533   24.888  1.00 11.42  ? 432 ILE A N   1 
ATOM   3264 C CA  . ILE A 1 446 ? -10.782 9.436   24.756  1.00 11.85  ? 432 ILE A CA  1 
ATOM   3265 C C   . ILE A 1 446 ? -11.168 9.285   23.290  1.00 10.77  ? 432 ILE A C   1 
ATOM   3266 O O   . ILE A 1 446 ? -10.387 9.550   22.364  1.00 11.23  ? 432 ILE A O   1 
ATOM   3267 C CB  . ILE A 1 446 ? -11.448 10.695  25.360  1.00 11.73  ? 432 ILE A CB  1 
ATOM   3268 C CG1 . ILE A 1 446 ? -11.141 11.950  24.530  1.00 12.05  ? 432 ILE A CG1 1 
ATOM   3269 C CG2 . ILE A 1 446 ? -11.082 10.842  26.832  1.00 14.25  ? 432 ILE A CG2 1 
ATOM   3270 C CD1 . ILE A 1 446 ? -11.817 13.214  25.027  1.00 12.94  ? 432 ILE A CD1 1 
ATOM   3271 N N   . LEU A 1 447 ? -12.431 8.899   23.095  1.00 11.16  ? 433 LEU A N   1 
ATOM   3272 C CA  . LEU A 1 447 ? -13.021 8.741   21.780  1.00 11.97  ? 433 LEU A CA  1 
ATOM   3273 C C   . LEU A 1 447 ? -14.395 9.377   21.898  1.00 11.69  ? 433 LEU A C   1 
ATOM   3274 O O   . LEU A 1 447 ? -15.375 8.683   22.134  1.00 17.91  ? 433 LEU A O   1 
ATOM   3275 C CB  . LEU A 1 447 ? -13.042 7.248   21.472  1.00 15.49  ? 433 LEU A CB  1 
ATOM   3276 C CG  . LEU A 1 447 ? -13.633 6.820   20.145  1.00 21.71  ? 433 LEU A CG  1 
ATOM   3277 C CD1 . LEU A 1 447 ? -12.971 7.574   19.027  1.00 23.62  ? 433 LEU A CD1 1 
ATOM   3278 C CD2 . LEU A 1 447 ? -13.435 5.322   19.902  1.00 27.12  ? 433 LEU A CD2 1 
ATOM   3279 N N   . ASN A 1 448 ? -14.432 10.703  21.670  1.00 12.16  ? 434 ASN A N   1 
ATOM   3280 C CA  . ASN A 1 448 ? -15.554 11.520  22.116  1.00 13.33  ? 434 ASN A CA  1 
ATOM   3281 C C   . ASN A 1 448 ? -15.998 12.514  21.043  1.00 14.81  ? 434 ASN A C   1 
ATOM   3282 O O   . ASN A 1 448 ? -16.737 13.444  21.353  1.00 16.92  ? 434 ASN A O   1 
ATOM   3283 C CB  . ASN A 1 448 ? -15.237 12.272  23.420  1.00 14.78  ? 434 ASN A CB  1 
ATOM   3284 C CG  . ASN A 1 448 ? -16.448 12.926  24.067  1.00 16.15  ? 434 ASN A CG  1 
ATOM   3285 O OD1 . ASN A 1 448 ? -16.408 14.120  24.392  1.00 21.42  ? 434 ASN A OD1 1 
ATOM   3286 N ND2 . ASN A 1 448 ? -17.502 12.159  24.260  1.00 16.13  ? 434 ASN A ND2 1 
ATOM   3287 N N   . GLU A 1 449 ? -15.577 12.310  19.786  1.00 11.75  ? 435 GLU A N   1 
ATOM   3288 C CA  . GLU A 1 449 ? -15.917 13.261  18.739  1.00 13.06  ? 435 GLU A CA  1 
ATOM   3289 C C   . GLU A 1 449 ? -15.851 12.490  17.432  1.00 10.90  ? 435 GLU A C   1 
ATOM   3290 O O   . GLU A 1 449 ? -15.151 11.493  17.326  1.00 11.85  ? 435 GLU A O   1 
ATOM   3291 C CB  . GLU A 1 449 ? -14.901 14.421  18.803  1.00 12.20  ? 435 GLU A CB  1 
ATOM   3292 C CG  . GLU A 1 449 ? -14.939 15.501  17.710  1.00 14.37  ? 435 GLU A CG  1 
ATOM   3293 C CD  . GLU A 1 449 ? -13.795 16.502  17.750  1.00 16.67  ? 435 GLU A CD  1 
ATOM   3294 O OE1 . GLU A 1 449 ? -13.077 16.516  18.758  1.00 16.13  ? 435 GLU A OE1 1 
ATOM   3295 O OE2 . GLU A 1 449 ? -13.615 17.230  16.751  1.00 18.97  ? 435 GLU A OE2 1 
ATOM   3296 N N   . LYS A 1 450 ? -16.588 12.983  16.450  1.00 12.07  ? 436 LYS A N   1 
ATOM   3297 C CA  . LYS A 1 450 ? -16.584 12.485  15.088  1.00 11.89  ? 436 LYS A CA  1 
ATOM   3298 C C   . LYS A 1 450 ? -16.431 13.691  14.178  1.00 12.00  ? 436 LYS A C   1 
ATOM   3299 O O   . LYS A 1 450 ? -16.950 14.781  14.474  1.00 15.82  ? 436 LYS A O   1 
ATOM   3300 C CB  . LYS A 1 450 ? -17.888 11.740  14.796  1.00 14.85  ? 436 LYS A CB  1 
ATOM   3301 C CG  . LYS A 1 450 ? -18.043 10.448  15.596  1.00 21.33  ? 436 LYS A CG  1 
ATOM   3302 C CD  . LYS A 1 450 ? -19.242 9.610   15.212  1.00 33.14  ? 436 LYS A CD  1 
ATOM   3303 C CE  . LYS A 1 450 ? -19.223 8.237   15.856  1.00 42.79  ? 436 LYS A CE  1 
ATOM   3304 N NZ  . LYS A 1 450 ? -19.415 8.330   17.316  1.00 48.47  ? 436 LYS A NZ  1 
ATOM   3305 N N   . VAL A 1 451 ? -15.715 13.495  13.062  1.00 9.41   ? 437 VAL A N   1 
ATOM   3306 C CA  . VAL A 1 451 ? -15.612 14.477  11.972  1.00 8.70   ? 437 VAL A CA  1 
ATOM   3307 C C   . VAL A 1 451 ? -16.213 13.853  10.720  1.00 8.89   ? 437 VAL A C   1 
ATOM   3308 O O   . VAL A 1 451 ? -16.431 12.636  10.660  1.00 10.41  ? 437 VAL A O   1 
ATOM   3309 C CB  . VAL A 1 451 ? -14.155 14.920  11.731  1.00 9.89   ? 437 VAL A CB  1 
ATOM   3310 C CG1 . VAL A 1 451 ? -13.533 15.552  12.974  1.00 14.40  ? 437 VAL A CG1 1 
ATOM   3311 C CG2 . VAL A 1 451 ? -13.288 13.806  11.196  1.00 10.79  ? 437 VAL A CG2 1 
ATOM   3312 N N   . GLN A 1 452 ? -16.391 14.683  9.678   1.00 8.85   ? 438 GLN A N   1 
ATOM   3313 C CA  . GLN A 1 452 ? -16.933 14.160  8.441   1.00 9.00   ? 438 GLN A CA  1 
ATOM   3314 C C   . GLN A 1 452 ? -15.956 13.164  7.823   1.00 8.79   ? 438 GLN A C   1 
ATOM   3315 O O   . GLN A 1 452 ? -14.721 13.353  7.807   1.00 8.59   ? 438 GLN A O   1 
ATOM   3316 C CB  . GLN A 1 452 ? -17.177 15.325  7.490   1.00 9.19   ? 438 GLN A CB  1 
ATOM   3317 C CG  . GLN A 1 452 ? -17.858 14.944  6.192   1.00 10.02  ? 438 GLN A CG  1 
ATOM   3318 C CD  . GLN A 1 452 ? -18.266 16.126  5.319   1.00 8.77   ? 438 GLN A CD  1 
ATOM   3319 O OE1 . GLN A 1 452 ? -18.151 16.049  4.080   1.00 11.27  ? 438 GLN A OE1 1 
ATOM   3320 N NE2 . GLN A 1 452 ? -18.854 17.135  5.921   1.00 9.20   ? 438 GLN A NE2 1 
ATOM   3321 N N   . SER A 1 453 ? -16.509 12.087  7.290   1.00 8.78   ? 439 SER A N   1 
ATOM   3322 C CA  . SER A 1 453 ? -15.722 11.111  6.547   1.00 10.18  ? 439 SER A CA  1 
ATOM   3323 C C   . SER A 1 453 ? -16.618 10.374  5.572   1.00 8.87   ? 439 SER A C   1 
ATOM   3324 O O   . SER A 1 453 ? -17.843 10.389  5.679   1.00 11.59  ? 439 SER A O   1 
ATOM   3325 C CB  . SER A 1 453 ? -15.083 10.104  7.482   1.00 10.08  ? 439 SER A CB  1 
ATOM   3326 O OG  . SER A 1 453 ? -16.046 9.260   8.103   1.00 11.90  ? 439 SER A OG  1 
ATOM   3327 N N   . GLY A 1 454 ? -16.011 9.627   4.660   1.00 10.51  ? 440 GLY A N   1 
ATOM   3328 C CA  . GLY A 1 454 ? -16.798 8.877   3.722   1.00 12.01  ? 440 GLY A CA  1 
ATOM   3329 C C   . GLY A 1 454 ? -16.041 8.523   2.456   1.00 8.52   ? 440 GLY A C   1 
ATOM   3330 O O   . GLY A 1 454 ? -14.815 8.687   2.361   1.00 9.67   ? 440 GLY A O   1 
ATOM   3331 N N   . ASN A 1 455 ? -16.768 7.842   1.579   1.00 11.23  ? 441 ASN A N   1 
ATOM   3332 C CA  . ASN A 1 455 ? -16.249 7.275   0.347   1.00 9.56   ? 441 ASN A CA  1 
ATOM   3333 C C   . ASN A 1 455 ? -16.637 8.208   -0.777  1.00 10.59  ? 441 ASN A C   1 
ATOM   3334 O O   . ASN A 1 455 ? -17.847 8.301   -1.050  1.00 15.62  ? 441 ASN A O   1 
ATOM   3335 C CB  . ASN A 1 455 ? -16.809 5.865   0.096   1.00 12.21  ? 441 ASN A CB  1 
ATOM   3336 C CG  . ASN A 1 455 ? -16.232 4.810   1.018   1.00 13.46  ? 441 ASN A CG  1 
ATOM   3337 O OD1 . ASN A 1 455 ? -15.371 5.110   1.846   1.00 16.16  ? 441 ASN A OD1 1 
ATOM   3338 N ND2 . ASN A 1 455 ? -16.546 3.552   0.760   1.00 15.36  ? 441 ASN A ND2 1 
ATOM   3339 N N   . ILE A 1 456 ? -15.654 8.763   -1.476  1.00 9.98   ? 442 ILE A N   1 
ATOM   3340 C CA  . ILE A 1 456 ? -15.862 9.591   -2.639  1.00 9.52   ? 442 ILE A CA  1 
ATOM   3341 C C   . ILE A 1 456 ? -15.680 8.729   -3.887  1.00 10.63  ? 442 ILE A C   1 
ATOM   3342 O O   . ILE A 1 456 ? -14.623 8.140   -4.106  1.00 10.98  ? 442 ILE A O   1 
ATOM   3343 C CB  . ILE A 1 456 ? -14.877 10.777  -2.641  1.00 11.93  ? 442 ILE A CB  1 
ATOM   3344 C CG1 . ILE A 1 456 ? -14.996 11.647  -1.373  1.00 14.46  ? 442 ILE A CG1 1 
ATOM   3345 C CG2 . ILE A 1 456 ? -15.026 11.601  -3.920  1.00 15.21  ? 442 ILE A CG2 1 
ATOM   3346 C CD1 . ILE A 1 456 ? -16.344 12.257  -1.148  1.00 15.39  ? 442 ILE A CD1 1 
ATOM   3347 N N   . LEU A 1 457 ? -16.720 8.743   -4.734  1.00 13.45  ? 443 LEU A N   1 
ATOM   3348 C CA  . LEU A 1 457 ? -16.712 7.935   -5.945  1.00 13.68  ? 443 LEU A CA  1 
ATOM   3349 C C   . LEU A 1 457 ? -16.134 8.758   -7.100  1.00 13.52  ? 443 LEU A C   1 
ATOM   3350 O O   . LEU A 1 457 ? -16.656 9.832   -7.412  1.00 18.36  ? 443 LEU A O   1 
ATOM   3351 C CB  . LEU A 1 457 ? -18.150 7.480   -6.234  1.00 16.78  ? 443 LEU A CB  1 
ATOM   3352 C CG  . LEU A 1 457 ? -18.662 6.176   -5.633  1.00 32.27  ? 443 LEU A CG  1 
ATOM   3353 C CD1 . LEU A 1 457 ? -18.153 5.863   -4.242  1.00 25.93  ? 443 LEU A CD1 1 
ATOM   3354 C CD2 . LEU A 1 457 ? -20.189 6.174   -5.685  1.00 24.67  ? 443 LEU A CD2 1 
ATOM   3355 N N   . ILE A 1 458 ? -15.073 8.237   -7.748  1.00 14.03  ? 444 ILE A N   1 
ATOM   3356 C CA  . ILE A 1 458 ? -14.482 8.848   -8.948  1.00 16.73  ? 444 ILE A CA  1 
ATOM   3357 C C   . ILE A 1 458 ? -14.832 8.038   -10.203 1.00 21.40  ? 444 ILE A C   1 
ATOM   3358 O O   . ILE A 1 458 ? -14.525 6.849   -10.274 1.00 24.35  ? 444 ILE A O   1 
ATOM   3359 C CB  . ILE A 1 458 ? -12.951 8.982   -8.791  1.00 16.36  ? 444 ILE A CB  1 
ATOM   3360 C CG1 . ILE A 1 458 ? -12.545 9.655   -7.477  1.00 15.08  ? 444 ILE A CG1 1 
ATOM   3361 C CG2 . ILE A 1 458 ? -12.266 9.634   -10.003 1.00 19.36  ? 444 ILE A CG2 1 
ATOM   3362 C CD1 . ILE A 1 458 ? -12.987 11.083  -7.336  1.00 18.53  ? 444 ILE A CD1 1 
ATOM   3363 N N   . ASP A 1 459 ? -15.343 8.720   -11.229 1.00 32.65  ? 445 ASP A N   1 
ATOM   3364 C CA  . ASP A 1 459 ? -15.680 8.055   -12.487 1.00 37.37  ? 445 ASP A CA  1 
ATOM   3365 C C   . ASP A 1 459 ? -14.889 8.710   -13.619 1.00 52.35  ? 445 ASP A C   1 
ATOM   3366 O O   . ASP A 1 459 ? -14.340 9.792   -13.333 1.00 44.72  ? 445 ASP A O   1 
ATOM   3367 C CB  . ASP A 1 459 ? -17.180 8.129   -12.782 1.00 56.26  ? 445 ASP A CB  1 
HETATM 3368 O O   . HOH B 2 .   ? 12.835  7.302   18.739  1.00 31.59  ? 601 HOH A O   1 
HETATM 3369 O O   . HOH B 2 .   ? -7.855  -6.345  -6.267  1.00 43.79  ? 602 HOH A O   1 
HETATM 3370 O O   . HOH B 2 .   ? 2.968   21.283  20.332  1.00 26.13  ? 603 HOH A O   1 
HETATM 3371 O O   . HOH B 2 .   ? 3.664   -12.886 -0.952  1.00 28.23  ? 604 HOH A O   1 
HETATM 3372 O O   . HOH B 2 .   ? 8.790   23.055  3.345   1.00 28.50  ? 605 HOH A O   1 
HETATM 3373 O O   . HOH B 2 .   ? 3.781   4.595   -12.729 1.00 33.28  ? 606 HOH A O   1 
HETATM 3374 O O   . HOH B 2 .   ? -12.161 -16.773 -22.735 1.00 32.47  ? 607 HOH A O   1 
HETATM 3375 O O   . HOH B 2 .   ? 15.007  1.819   0.348   1.00 39.15  ? 608 HOH A O   1 
HETATM 3376 O O   . HOH B 2 .   ? 17.834  19.415  10.484  1.00 30.48  ? 609 HOH A O   1 
HETATM 3377 O O   . HOH B 2 .   ? 14.185  -8.983  5.282   1.00 34.15  ? 610 HOH A O   1 
HETATM 3378 O O   . HOH B 2 .   ? -0.530  -8.998  -6.221  1.00 14.69  ? 611 HOH A O   1 
HETATM 3379 O O   . HOH B 2 .   ? -8.211  -12.844 1.669   1.00 47.70  ? 612 HOH A O   1 
HETATM 3380 O O   . HOH B 2 .   ? -4.694  -22.426 -25.735 1.00 40.61  ? 613 HOH A O   1 
HETATM 3381 O O   . HOH B 2 .   ? -3.397  22.294  22.138  1.00 30.82  ? 614 HOH A O   1 
HETATM 3382 O O   . HOH B 2 .   ? -11.859 -13.231 12.643  1.00 24.47  ? 615 HOH A O   1 
HETATM 3383 O O   . HOH B 2 .   ? -14.641 -15.052 -3.570  1.00 26.51  ? 616 HOH A O   1 
HETATM 3384 O O   . HOH B 2 .   ? -16.192 4.025   17.258  1.00 68.99  ? 617 HOH A O   1 
HETATM 3385 O O   . HOH B 2 .   ? 16.999  -1.710  6.313   1.00 27.67  ? 618 HOH A O   1 
HETATM 3386 O O   . HOH B 2 .   ? -8.929  14.297  31.269  1.00 19.34  ? 619 HOH A O   1 
HETATM 3387 O O   . HOH B 2 .   ? -13.262 19.098  -2.227  1.00 32.45  ? 620 HOH A O   1 
HETATM 3388 O O   . HOH B 2 .   ? 11.646  -7.542  -6.472  1.00 24.94  ? 621 HOH A O   1 
HETATM 3389 O O   . HOH B 2 .   ? 10.386  6.574   20.067  1.00 18.47  ? 622 HOH A O   1 
HETATM 3390 O O   . HOH B 2 .   ? 16.034  18.200  8.649   1.00 39.32  ? 623 HOH A O   1 
HETATM 3391 O O   . HOH B 2 .   ? 14.153  -24.953 -15.762 1.00 15.91  ? 624 HOH A O   1 
HETATM 3392 O O   . HOH B 2 .   ? 7.559   -14.732 6.634   1.00 27.59  ? 625 HOH A O   1 
HETATM 3393 O O   . HOH B 2 .   ? 12.981  6.721   13.026  1.00 23.48  ? 626 HOH A O   1 
HETATM 3394 O O   . HOH B 2 .   ? -3.777  9.670   -9.433  1.00 25.44  ? 627 HOH A O   1 
HETATM 3395 O O   . HOH B 2 .   ? -1.662  7.722   29.450  1.00 22.30  ? 628 HOH A O   1 
HETATM 3396 O O   . HOH B 2 .   ? 0.720   -4.096  -3.889  1.00 33.47  ? 629 HOH A O   1 
HETATM 3397 O O   . HOH B 2 .   ? -10.056 26.334  10.259  1.00 27.57  ? 630 HOH A O   1 
HETATM 3398 O O   . HOH B 2 .   ? -5.850  20.041  26.922  1.00 26.20  ? 631 HOH A O   1 
HETATM 3399 O O   . HOH B 2 .   ? 17.472  -11.587 5.976   1.00 42.29  ? 632 HOH A O   1 
HETATM 3400 O O   . HOH B 2 .   ? -10.245 5.943   27.916  1.00 32.44  ? 633 HOH A O   1 
HETATM 3401 O O   . HOH B 2 .   ? 18.004  -14.676 7.986   1.00 35.46  ? 634 HOH A O   1 
HETATM 3402 O O   . HOH B 2 .   ? 6.488   -29.061 -11.845 1.00 29.85  ? 635 HOH A O   1 
HETATM 3403 O O   . HOH B 2 .   ? 13.018  -3.935  -6.355  1.00 28.66  ? 636 HOH A O   1 
HETATM 3404 O O   . HOH B 2 .   ? 3.055   -3.566  -3.220  1.00 23.45  ? 637 HOH A O   1 
HETATM 3405 O O   . HOH B 2 .   ? -8.832  0.745   15.479  1.00 14.65  ? 638 HOH A O   1 
HETATM 3406 O O   . HOH B 2 .   ? -17.780 10.365  9.789   1.00 21.01  ? 639 HOH A O   1 
HETATM 3407 O O   . HOH B 2 .   ? 7.680   6.155   0.911   1.00 9.33   ? 640 HOH A O   1 
HETATM 3408 O O   . HOH B 2 .   ? 9.723   24.326  -3.080  1.00 21.98  ? 641 HOH A O   1 
HETATM 3409 O O   . HOH B 2 .   ? -0.508  -25.173 -7.374  1.00 28.66  ? 642 HOH A O   1 
HETATM 3410 O O   . HOH B 2 .   ? 10.077  19.594  6.389   1.00 21.35  ? 643 HOH A O   1 
HETATM 3411 O O   . HOH B 2 .   ? -17.276 -0.664  6.609   1.00 40.33  ? 644 HOH A O   1 
HETATM 3412 O O   . HOH B 2 .   ? -6.808  20.135  -10.980 1.00 31.92  ? 645 HOH A O   1 
HETATM 3413 O O   . HOH B 2 .   ? -6.153  -13.455 7.162   1.00 26.31  ? 646 HOH A O   1 
HETATM 3414 O O   . HOH B 2 .   ? -14.639 18.473  0.666   1.00 14.96  ? 647 HOH A O   1 
HETATM 3415 O O   . HOH B 2 .   ? 17.932  0.128   21.284  1.00 39.84  ? 648 HOH A O   1 
HETATM 3416 O O   . HOH B 2 .   ? 12.470  21.664  5.017   1.00 24.32  ? 649 HOH A O   1 
HETATM 3417 O O   . HOH B 2 .   ? 7.685   21.563  5.199   1.00 42.96  ? 650 HOH A O   1 
HETATM 3418 O O   . HOH B 2 .   ? 6.573   -13.434 2.818   1.00 16.60  ? 651 HOH A O   1 
HETATM 3419 O O   . HOH B 2 .   ? 4.059   17.079  -9.897  1.00 20.90  ? 652 HOH A O   1 
HETATM 3420 O O   . HOH B 2 .   ? 7.934   17.720  21.155  1.00 25.73  ? 653 HOH A O   1 
HETATM 3421 O O   . HOH B 2 .   ? 1.948   27.745  9.332   1.00 43.90  ? 654 HOH A O   1 
HETATM 3422 O O   . HOH B 2 .   ? -12.498 15.172  21.003  1.00 20.30  ? 655 HOH A O   1 
HETATM 3423 O O   . HOH B 2 .   ? 3.602   -4.783  -23.134 1.00 30.78  ? 656 HOH A O   1 
HETATM 3424 O O   . HOH B 2 .   ? -2.240  -25.857 -16.585 1.00 30.29  ? 657 HOH A O   1 
HETATM 3425 O O   . HOH B 2 .   ? -20.574 -16.397 -10.361 1.00 24.56  ? 658 HOH A O   1 
HETATM 3426 O O   . HOH B 2 .   ? -10.278 24.784  0.132   1.00 26.33  ? 659 HOH A O   1 
HETATM 3427 O O   . HOH B 2 .   ? -11.493 -15.050 19.709  1.00 28.06  ? 660 HOH A O   1 
HETATM 3428 O O   . HOH B 2 .   ? 16.672  -14.416 -0.552  1.00 42.46  ? 661 HOH A O   1 
HETATM 3429 O O   . HOH B 2 .   ? -10.071 11.078  -12.516 1.00 30.05  ? 662 HOH A O   1 
HETATM 3430 O O   . HOH B 2 .   ? -17.590 18.820  7.856   1.00 13.76  ? 663 HOH A O   1 
HETATM 3431 O O   . HOH B 2 .   ? 0.501   -17.582 15.467  1.00 22.15  ? 664 HOH A O   1 
HETATM 3432 O O   . HOH B 2 .   ? -7.795  -15.982 13.961  1.00 35.24  ? 665 HOH A O   1 
HETATM 3433 O O   . HOH B 2 .   ? 3.159   20.866  -2.238  1.00 18.64  ? 666 HOH A O   1 
HETATM 3434 O O   . HOH B 2 .   ? 11.075  20.420  15.897  1.00 33.25  ? 667 HOH A O   1 
HETATM 3435 O O   . HOH B 2 .   ? 14.746  8.874   10.225  1.00 13.77  ? 668 HOH A O   1 
HETATM 3436 O O   . HOH B 2 .   ? -17.208 -11.221 7.586   1.00 23.94  ? 669 HOH A O   1 
HETATM 3437 O O   . HOH B 2 .   ? 14.366  7.030   -0.140  1.00 15.49  ? 670 HOH A O   1 
HETATM 3438 O O   . HOH B 2 .   ? -5.356  -9.775  -14.244 1.00 19.74  ? 671 HOH A O   1 
HETATM 3439 O O   . HOH B 2 .   ? -2.740  -6.962  28.027  1.00 21.84  ? 672 HOH A O   1 
HETATM 3440 O O   . HOH B 2 .   ? 2.402   1.078   3.217   1.00 14.79  ? 673 HOH A O   1 
HETATM 3441 O O   . HOH B 2 .   ? 13.573  -6.850  -8.204  1.00 26.69  ? 674 HOH A O   1 
HETATM 3442 O O   . HOH B 2 .   ? -12.953 -19.917 -24.702 1.00 32.52  ? 675 HOH A O   1 
HETATM 3443 O O   . HOH B 2 .   ? -17.418 1.904   5.237   1.00 44.92  ? 676 HOH A O   1 
HETATM 3444 O O   . HOH B 2 .   ? 5.459   0.558   5.448   1.00 15.39  ? 677 HOH A O   1 
HETATM 3445 O O   . HOH B 2 .   ? -5.029  7.344   -8.826  1.00 20.77  ? 678 HOH A O   1 
HETATM 3446 O O   . HOH B 2 .   ? 11.815  -0.859  2.170   1.00 16.53  ? 679 HOH A O   1 
HETATM 3447 O O   . HOH B 2 .   ? 4.812   -10.314 -2.853  1.00 23.36  ? 680 HOH A O   1 
HETATM 3448 O O   . HOH B 2 .   ? 13.120  -18.544 3.883   1.00 29.93  ? 681 HOH A O   1 
HETATM 3449 O O   . HOH B 2 .   ? -10.068 -15.632 -27.143 1.00 21.29  ? 682 HOH A O   1 
HETATM 3450 O O   . HOH B 2 .   ? 5.643   -27.201 -5.404  1.00 35.62  ? 683 HOH A O   1 
HETATM 3451 O O   . HOH B 2 .   ? -3.503  -19.417 -8.900  1.00 25.82  ? 684 HOH A O   1 
HETATM 3452 O O   . HOH B 2 .   ? -11.912 -24.963 -17.542 1.00 32.33  ? 685 HOH A O   1 
HETATM 3453 O O   . HOH B 2 .   ? -0.410  25.674  12.394  1.00 28.22  ? 686 HOH A O   1 
HETATM 3454 O O   . HOH B 2 .   ? -17.210 8.280   12.876  1.00 20.59  ? 687 HOH A O   1 
HETATM 3455 O O   . HOH B 2 .   ? 5.159   22.296  6.165   1.00 21.60  ? 688 HOH A O   1 
HETATM 3456 O O   . HOH B 2 .   ? -13.824 0.085   11.848  1.00 18.18  ? 689 HOH A O   1 
HETATM 3457 O O   . HOH B 2 .   ? 20.416  8.046   11.137  1.00 44.96  ? 690 HOH A O   1 
HETATM 3458 O O   . HOH B 2 .   ? -3.138  -26.054 -21.412 1.00 27.30  ? 691 HOH A O   1 
HETATM 3459 O O   . HOH B 2 .   ? 8.497   10.199  -12.034 1.00 25.81  ? 692 HOH A O   1 
HETATM 3460 O O   . HOH B 2 .   ? -17.785 6.125   9.589   1.00 21.63  ? 693 HOH A O   1 
HETATM 3461 O O   . HOH B 2 .   ? 1.906   18.694  -10.507 1.00 21.34  ? 694 HOH A O   1 
HETATM 3462 O O   . HOH B 2 .   ? -18.013 -14.117 -24.155 1.00 19.24  ? 695 HOH A O   1 
HETATM 3463 O O   . HOH B 2 .   ? 15.693  4.469   3.647   1.00 14.25  ? 696 HOH A O   1 
HETATM 3464 O O   . HOH B 2 .   ? 4.098   -21.123 5.152   1.00 30.55  ? 697 HOH A O   1 
HETATM 3465 O O   . HOH B 2 .   ? 14.558  25.047  33.187  1.00 33.06  ? 698 HOH A O   1 
HETATM 3466 O O   . HOH B 2 .   ? -12.117 12.431  21.111  1.00 13.12  ? 699 HOH A O   1 
HETATM 3467 O O   . HOH B 2 .   ? -13.040 14.555  6.017   1.00 10.08  ? 700 HOH A O   1 
HETATM 3468 O O   . HOH B 2 .   ? -7.046  -11.176 8.641   1.00 16.01  ? 701 HOH A O   1 
HETATM 3469 O O   . HOH B 2 .   ? -6.709  26.786  12.483  1.00 20.83  ? 702 HOH A O   1 
HETATM 3470 O O   . HOH B 2 .   ? -12.647 7.169   3.062   1.00 9.34   ? 703 HOH A O   1 
HETATM 3471 O O   . HOH B 2 .   ? 12.465  -2.400  21.458  1.00 22.91  ? 704 HOH A O   1 
HETATM 3472 O O   . HOH B 2 .   ? -7.598  4.416   27.982  1.00 30.59  ? 705 HOH A O   1 
HETATM 3473 O O   . HOH B 2 .   ? -1.783  21.780  -4.663  1.00 30.05  ? 706 HOH A O   1 
HETATM 3474 O O   . HOH B 2 .   ? 3.109   -2.392  25.059  1.00 25.51  ? 707 HOH A O   1 
HETATM 3475 O O   . HOH B 2 .   ? -20.199 6.949   -1.479  1.00 26.20  ? 708 HOH A O   1 
HETATM 3476 O O   . HOH B 2 .   ? 7.782   1.996   24.008  1.00 14.18  ? 709 HOH A O   1 
HETATM 3477 O O   . HOH B 2 .   ? 9.796   -3.056  1.008   1.00 15.26  ? 710 HOH A O   1 
HETATM 3478 O O   . HOH B 2 .   ? 1.064   15.735  -18.408 1.00 36.80  ? 711 HOH A O   1 
HETATM 3479 O O   . HOH B 2 .   ? -13.482 21.055  11.265  1.00 21.69  ? 712 HOH A O   1 
HETATM 3480 O O   . HOH B 2 .   ? 14.022  15.757  1.279   1.00 24.40  ? 713 HOH A O   1 
HETATM 3481 O O   . HOH B 2 .   ? 2.540   6.290   -10.856 1.00 27.92  ? 714 HOH A O   1 
HETATM 3482 O O   . HOH B 2 .   ? -7.074  -10.305 4.735   1.00 29.85  ? 715 HOH A O   1 
HETATM 3483 O O   . HOH B 2 .   ? -15.658 1.289   2.415   1.00 17.16  ? 716 HOH A O   1 
HETATM 3484 O O   . HOH B 2 .   ? -13.108 10.216  4.721   1.00 8.85   ? 717 HOH A O   1 
HETATM 3485 O O   . HOH B 2 .   ? 0.704   2.898   -7.295  1.00 23.84  ? 718 HOH A O   1 
HETATM 3486 O O   . HOH B 2 .   ? -14.466 -8.254  -27.756 1.00 18.65  ? 719 HOH A O   1 
HETATM 3487 O O   . HOH B 2 .   ? -1.606  -7.584  8.623   1.00 10.03  ? 720 HOH A O   1 
HETATM 3488 O O   . HOH B 2 .   ? -11.777 -7.609  -28.163 1.00 31.16  ? 721 HOH A O   1 
HETATM 3489 O O   . HOH B 2 .   ? -1.746  -23.173 -20.415 1.00 16.50  ? 722 HOH A O   1 
HETATM 3490 O O   . HOH B 2 .   ? 11.177  4.284   27.222  1.00 44.93  ? 723 HOH A O   1 
HETATM 3491 O O   . HOH B 2 .   ? 5.789   -5.976  -22.315 1.00 23.39  ? 724 HOH A O   1 
HETATM 3492 O O   . HOH B 2 .   ? -3.877  20.755  14.314  1.00 14.18  ? 725 HOH A O   1 
HETATM 3493 O O   . HOH B 2 .   ? -15.697 17.438  14.948  1.00 23.14  ? 726 HOH A O   1 
HETATM 3494 O O   . HOH B 2 .   ? 16.834  13.934  4.290   1.00 23.55  ? 727 HOH A O   1 
HETATM 3495 O O   . HOH B 2 .   ? 1.114   -25.504 -26.143 1.00 36.03  ? 728 HOH A O   1 
HETATM 3496 O O   . HOH B 2 .   ? -4.263  19.359  28.946  1.00 44.01  ? 729 HOH A O   1 
HETATM 3497 O O   . HOH B 2 .   ? -12.708 19.743  17.472  1.00 28.93  ? 730 HOH A O   1 
HETATM 3498 O O   . HOH B 2 .   ? -8.827  15.014  24.497  1.00 18.40  ? 731 HOH A O   1 
HETATM 3499 O O   . HOH B 2 .   ? 1.362   -4.757  14.894  1.00 11.55  ? 732 HOH A O   1 
HETATM 3500 O O   . HOH B 2 .   ? 4.218   -0.478  2.499   1.00 21.88  ? 733 HOH A O   1 
HETATM 3501 O O   . HOH B 2 .   ? -12.033 -11.340 14.467  1.00 18.50  ? 734 HOH A O   1 
HETATM 3502 O O   . HOH B 2 .   ? -11.263 25.922  4.717   1.00 14.54  ? 735 HOH A O   1 
HETATM 3503 O O   . HOH B 2 .   ? 0.788   -18.632 8.105   1.00 30.74  ? 736 HOH A O   1 
HETATM 3504 O O   . HOH B 2 .   ? -4.711  -4.623  2.829   1.00 14.36  ? 737 HOH A O   1 
HETATM 3505 O O   . HOH B 2 .   ? 4.529   15.507  -12.233 1.00 21.08  ? 738 HOH A O   1 
HETATM 3506 O O   . HOH B 2 .   ? 7.213   -11.471 19.050  1.00 48.75  ? 739 HOH A O   1 
HETATM 3507 O O   . HOH B 2 .   ? -13.375 -4.901  2.184   1.00 33.20  ? 740 HOH A O   1 
HETATM 3508 O O   . HOH B 2 .   ? 0.361   -25.650 -12.598 1.00 23.16  ? 741 HOH A O   1 
HETATM 3509 O O   . HOH B 2 .   ? 4.875   -19.542 7.231   1.00 24.18  ? 742 HOH A O   1 
HETATM 3510 O O   . HOH B 2 .   ? -2.516  -5.690  -0.446  1.00 28.53  ? 743 HOH A O   1 
HETATM 3511 O O   . HOH B 2 .   ? -2.842  -21.561 -23.912 1.00 20.65  ? 744 HOH A O   1 
HETATM 3512 O O   . HOH B 2 .   ? 16.739  12.000  0.932   1.00 34.68  ? 745 HOH A O   1 
HETATM 3513 O O   . HOH B 2 .   ? 5.246   -26.436 -21.227 1.00 32.89  ? 746 HOH A O   1 
HETATM 3514 O O   . HOH B 2 .   ? 15.205  -12.048 -14.072 1.00 31.93  ? 747 HOH A O   1 
HETATM 3515 O O   . HOH B 2 .   ? -7.168  17.121  24.069  1.00 22.58  ? 748 HOH A O   1 
HETATM 3516 O O   . HOH B 2 .   ? 3.887   9.420   28.003  1.00 33.79  ? 749 HOH A O   1 
HETATM 3517 O O   . HOH B 2 .   ? 6.179   -23.756 -18.637 1.00 20.91  ? 750 HOH A O   1 
HETATM 3518 O O   . HOH B 2 .   ? -14.791 -25.853 -19.124 1.00 39.08  ? 751 HOH A O   1 
HETATM 3519 O O   . HOH B 2 .   ? 11.658  -8.561  6.517   1.00 18.36  ? 752 HOH A O   1 
HETATM 3520 O O   . HOH B 2 .   ? -17.779 -22.762 -9.099  1.00 41.54  ? 753 HOH A O   1 
HETATM 3521 O O   . HOH B 2 .   ? 14.669  -1.217  2.824   1.00 27.09  ? 754 HOH A O   1 
HETATM 3522 O O   . HOH B 2 .   ? 8.372   -6.465  24.277  1.00 38.18  ? 755 HOH A O   1 
HETATM 3523 O O   . HOH B 2 .   ? -9.980  -3.707  -22.433 1.00 28.13  ? 756 HOH A O   1 
HETATM 3524 O O   . HOH B 2 .   ? -7.486  20.478  16.395  1.00 25.13  ? 757 HOH A O   1 
HETATM 3525 O O   . HOH B 2 .   ? -16.581 16.370  0.704   1.00 18.99  ? 758 HOH A O   1 
HETATM 3526 O O   . HOH B 2 .   ? -10.665 -12.222 16.573  1.00 23.54  ? 759 HOH A O   1 
HETATM 3527 O O   . HOH B 2 .   ? -0.451  8.776   -6.829  1.00 19.18  ? 760 HOH A O   1 
HETATM 3528 O O   . HOH B 2 .   ? 5.305   -9.506  25.131  1.00 38.63  ? 761 HOH A O   1 
HETATM 3529 O O   . HOH B 2 .   ? -10.258 23.144  -1.790  1.00 35.27  ? 762 HOH A O   1 
HETATM 3530 O O   . HOH B 2 .   ? 9.604   21.655  7.966   1.00 33.45  ? 763 HOH A O   1 
HETATM 3531 O O   . HOH B 2 .   ? 14.496  11.129  -5.042  1.00 18.06  ? 764 HOH A O   1 
HETATM 3532 O O   . HOH B 2 .   ? -10.068 20.800  14.183  1.00 24.28  ? 765 HOH A O   1 
HETATM 3533 O O   . HOH B 2 .   ? -5.812  -12.519 16.416  1.00 29.61  ? 766 HOH A O   1 
HETATM 3534 O O   . HOH B 2 .   ? 10.995  -28.224 -14.817 1.00 35.98  ? 767 HOH A O   1 
HETATM 3535 O O   . HOH B 2 .   ? 11.487  -24.842 -20.736 1.00 34.72  ? 768 HOH A O   1 
HETATM 3536 O O   . HOH B 2 .   ? 15.414  -9.534  -1.850  1.00 36.07  ? 769 HOH A O   1 
HETATM 3537 O O   . HOH B 2 .   ? 8.568   -4.622  8.029   1.00 13.35  ? 770 HOH A O   1 
HETATM 3538 O O   . HOH B 2 .   ? 15.464  4.778   11.076  1.00 34.25  ? 771 HOH A O   1 
HETATM 3539 O O   . HOH B 2 .   ? 16.620  -4.663  -3.389  1.00 28.32  ? 772 HOH A O   1 
HETATM 3540 O O   . HOH B 2 .   ? -9.524  27.383  6.331   1.00 23.65  ? 773 HOH A O   1 
HETATM 3541 O O   . HOH B 2 .   ? 1.603   -17.082 -27.984 1.00 29.98  ? 774 HOH A O   1 
HETATM 3542 O O   . HOH B 2 .   ? -5.723  -11.479 23.694  1.00 30.42  ? 775 HOH A O   1 
HETATM 3543 O O   . HOH B 2 .   ? 12.741  10.143  -6.869  1.00 22.24  ? 776 HOH A O   1 
HETATM 3544 O O   . HOH B 2 .   ? -1.180  24.605  5.184   1.00 33.37  ? 777 HOH A O   1 
HETATM 3545 O O   . HOH B 2 .   ? -8.647  13.814  26.840  1.00 15.70  ? 778 HOH A O   1 
HETATM 3546 O O   . HOH B 2 .   ? -0.388  -0.402  27.501  1.00 17.45  ? 779 HOH A O   1 
HETATM 3547 O O   . HOH B 2 .   ? -18.922 9.974   -9.093  1.00 36.53  ? 780 HOH A O   1 
HETATM 3548 O O   . HOH B 2 .   ? -0.480  2.175   2.956   1.00 13.51  ? 781 HOH A O   1 
HETATM 3549 O O   . HOH B 2 .   ? 6.191   -13.167 17.105  1.00 21.00  ? 782 HOH A O   1 
HETATM 3550 O O   . HOH B 2 .   ? -1.249  -8.811  -0.032  1.00 25.18  ? 783 HOH A O   1 
HETATM 3551 O O   . HOH B 2 .   ? -6.717  7.992   -11.064 1.00 27.42  ? 784 HOH A O   1 
HETATM 3552 O O   . HOH B 2 .   ? 10.546  23.390  30.265  1.00 27.65  ? 785 HOH A O   1 
HETATM 3553 O O   . HOH B 2 .   ? -0.944  -3.169  -0.825  1.00 29.32  ? 786 HOH A O   1 
HETATM 3554 O O   . HOH B 2 .   ? -6.628  7.100   29.015  1.00 25.46  ? 787 HOH A O   1 
HETATM 3555 O O   . HOH B 2 .   ? 3.756   -25.682 -6.783  1.00 28.74  ? 788 HOH A O   1 
HETATM 3556 O O   . HOH B 2 .   ? 3.862   -27.503 -24.007 1.00 42.18  ? 789 HOH A O   1 
HETATM 3557 O O   . HOH B 2 .   ? -8.161  -24.884 -9.843  1.00 39.63  ? 790 HOH A O   1 
HETATM 3558 O O   . HOH B 2 .   ? -16.562 -10.968 -13.291 1.00 39.40  ? 791 HOH A O   1 
HETATM 3559 O O   . HOH B 2 .   ? -16.186 -19.204 -8.310  1.00 35.04  ? 792 HOH A O   1 
HETATM 3560 O O   . HOH B 2 .   ? -18.976 10.422  -4.268  1.00 22.34  ? 793 HOH A O   1 
HETATM 3561 O O   . HOH B 2 .   ? -15.995 -1.231  1.407   1.00 31.51  ? 794 HOH A O   1 
HETATM 3562 O O   . HOH B 2 .   ? -5.922  -4.370  -18.818 1.00 26.20  ? 795 HOH A O   1 
HETATM 3563 O O   . HOH B 2 .   ? -17.508 7.174   6.810   1.00 18.23  ? 796 HOH A O   1 
HETATM 3564 O O   . HOH B 2 .   ? -9.454  14.912  -13.615 1.00 35.03  ? 797 HOH A O   1 
HETATM 3565 O O   . HOH B 2 .   ? 13.288  -16.764 -21.996 1.00 22.30  ? 798 HOH A O   1 
HETATM 3566 O O   . HOH B 2 .   ? 14.440  -5.517  16.577  1.00 26.04  ? 799 HOH A O   1 
HETATM 3567 O O   . HOH B 2 .   ? 12.850  2.028   2.593   1.00 23.34  ? 800 HOH A O   1 
HETATM 3568 O O   . HOH B 2 .   ? 11.550  23.766  13.814  1.00 44.72  ? 801 HOH A O   1 
HETATM 3569 O O   . HOH B 2 .   ? -9.210  -2.011  -3.335  1.00 25.22  ? 802 HOH A O   1 
HETATM 3570 O O   . HOH B 2 .   ? -7.074  -12.005 -27.920 1.00 37.82  ? 803 HOH A O   1 
HETATM 3571 O O   . HOH B 2 .   ? -17.652 0.216   -10.936 1.00 49.88  ? 804 HOH A O   1 
HETATM 3572 O O   . HOH B 2 .   ? 4.034   6.650   26.330  1.00 31.01  ? 805 HOH A O   1 
HETATM 3573 O O   . HOH B 2 .   ? 17.446  1.125   -7.110  1.00 46.38  ? 806 HOH A O   1 
HETATM 3574 O O   . HOH B 2 .   ? 4.920   24.318  25.876  1.00 37.88  ? 807 HOH A O   1 
HETATM 3575 O O   . HOH B 2 .   ? 1.058   25.118  -5.926  1.00 36.33  ? 808 HOH A O   1 
HETATM 3576 O O   . HOH B 2 .   ? 16.300  -16.762 -13.487 1.00 40.11  ? 809 HOH A O   1 
HETATM 3577 O O   . HOH B 2 .   ? -15.777 -7.086  10.031  1.00 22.76  ? 810 HOH A O   1 
HETATM 3578 O O   . HOH B 2 .   ? 15.779  -2.148  -13.157 1.00 30.20  ? 811 HOH A O   1 
HETATM 3579 O O   . HOH B 2 .   ? -8.204  12.172  -14.140 1.00 37.96  ? 812 HOH A O   1 
HETATM 3580 O O   . HOH B 2 .   ? -20.498 16.551  8.221   1.00 20.34  ? 813 HOH A O   1 
HETATM 3581 O O   . HOH B 2 .   ? -11.571 13.917  -1.707  1.00 17.73  ? 814 HOH A O   1 
HETATM 3582 O O   . HOH B 2 .   ? 4.486   0.605   26.883  1.00 36.18  ? 815 HOH A O   1 
HETATM 3583 O O   . HOH B 2 .   ? 9.825   -8.400  18.423  1.00 29.84  ? 816 HOH A O   1 
HETATM 3584 O O   . HOH B 2 .   ? -2.724  9.214   -12.094 1.00 23.13  ? 817 HOH A O   1 
HETATM 3585 O O   . HOH B 2 .   ? 7.660   2.673   -2.612  1.00 11.10  ? 818 HOH A O   1 
HETATM 3586 O O   . HOH B 2 .   ? -15.847 -3.769  8.714   1.00 19.84  ? 819 HOH A O   1 
HETATM 3587 O O   . HOH B 2 .   ? -7.423  11.554  34.743  1.00 42.97  ? 820 HOH A O   1 
HETATM 3588 O O   . HOH B 2 .   ? 11.395  -14.280 -4.288  1.00 19.21  ? 821 HOH A O   1 
HETATM 3589 O O   . HOH B 2 .   ? 15.155  -14.904 -6.221  1.00 35.00  ? 822 HOH A O   1 
HETATM 3590 O O   . HOH B 2 .   ? -16.904 12.692  -6.991  1.00 24.67  ? 823 HOH A O   1 
HETATM 3591 O O   . HOH B 2 .   ? -19.683 -19.764 -7.658  1.00 25.44  ? 824 HOH A O   1 
HETATM 3592 O O   . HOH B 2 .   ? -3.994  24.062  1.427   1.00 24.48  ? 825 HOH A O   1 
HETATM 3593 O O   . HOH B 2 .   ? 3.490   -4.716  23.140  1.00 22.06  ? 826 HOH A O   1 
HETATM 3594 O O   . HOH B 2 .   ? 9.727   16.172  18.506  1.00 31.19  ? 827 HOH A O   1 
HETATM 3595 O O   . HOH B 2 .   ? -1.164  28.474  7.343   1.00 42.00  ? 828 HOH A O   1 
HETATM 3596 O O   . HOH B 2 .   ? -1.652  -15.236 18.609  1.00 31.97  ? 829 HOH A O   1 
HETATM 3597 O O   . HOH B 2 .   ? 10.137  8.637   22.065  1.00 25.40  ? 830 HOH A O   1 
HETATM 3598 O O   . HOH B 2 .   ? -15.318 -3.153  3.723   1.00 29.91  ? 831 HOH A O   1 
HETATM 3599 O O   . HOH B 2 .   ? -19.472 7.168   2.440   1.00 22.49  ? 832 HOH A O   1 
HETATM 3600 O O   . HOH B 2 .   ? 9.426   12.078  24.423  1.00 35.61  ? 833 HOH A O   1 
HETATM 3601 O O   . HOH B 2 .   ? 2.764   -27.381 -8.871  1.00 28.89  ? 834 HOH A O   1 
HETATM 3602 O O   . HOH B 2 .   ? -9.088  17.308  20.686  1.00 28.28  ? 835 HOH A O   1 
HETATM 3603 O O   . HOH B 2 .   ? -10.256 -26.615 -21.323 1.00 43.80  ? 836 HOH A O   1 
HETATM 3604 O O   . HOH B 2 .   ? 18.286  1.628   3.534   1.00 25.86  ? 837 HOH A O   1 
HETATM 3605 O O   . HOH B 2 .   ? 17.451  14.979  8.049   1.00 43.96  ? 838 HOH A O   1 
HETATM 3606 O O   . HOH B 2 .   ? -18.691 14.804  17.368  1.00 21.15  ? 839 HOH A O   1 
HETATM 3607 O O   . HOH B 2 .   ? -9.775  16.155  -6.532  1.00 19.67  ? 840 HOH A O   1 
HETATM 3608 O O   . HOH B 2 .   ? 1.396   26.098  -8.929  1.00 40.43  ? 841 HOH A O   1 
HETATM 3609 O O   . HOH B 2 .   ? 9.155   14.172  27.682  1.00 57.95  ? 842 HOH A O   1 
HETATM 3610 O O   . HOH B 2 .   ? 14.206  -7.972  -21.773 1.00 31.48  ? 843 HOH A O   1 
HETATM 3611 O O   . HOH B 2 .   ? 3.638   -19.957 9.850   1.00 24.90  ? 844 HOH A O   1 
HETATM 3612 O O   . HOH B 2 .   ? -15.448 2.871   9.021   1.00 16.81  ? 845 HOH A O   1 
HETATM 3613 O O   . HOH B 2 .   ? 1.521   9.112   28.177  1.00 39.67  ? 846 HOH A O   1 
HETATM 3614 O O   . HOH B 2 .   ? 13.834  19.491  8.630   1.00 22.76  ? 847 HOH A O   1 
HETATM 3615 O O   . HOH B 2 .   ? 16.312  4.172   -2.550  1.00 36.98  ? 848 HOH A O   1 
HETATM 3616 O O   . HOH B 2 .   ? -1.610  -26.806 -19.041 1.00 26.73  ? 849 HOH A O   1 
HETATM 3617 O O   . HOH B 2 .   ? -13.117 26.421  8.362   1.00 22.01  ? 850 HOH A O   1 
HETATM 3618 O O   . HOH B 2 .   ? 11.268  -18.232 -25.700 1.00 45.42  ? 851 HOH A O   1 
HETATM 3619 O O   . HOH B 2 .   ? -12.418 1.383   21.164  1.00 26.12  ? 852 HOH A O   1 
HETATM 3620 O O   . HOH B 2 .   ? -2.738  9.882   -7.212  1.00 20.97  ? 853 HOH A O   1 
HETATM 3621 O O   . HOH B 2 .   ? -11.018 -20.315 -27.007 1.00 36.50  ? 854 HOH A O   1 
HETATM 3622 O O   . HOH B 2 .   ? -9.356  28.775  -0.124  1.00 30.97  ? 855 HOH A O   1 
HETATM 3623 O O   . HOH B 2 .   ? -13.067 15.922  -0.002  1.00 21.19  ? 856 HOH A O   1 
HETATM 3624 O O   . HOH B 2 .   ? 18.901  11.611  4.853   1.00 22.27  ? 857 HOH A O   1 
HETATM 3625 O O   . HOH B 2 .   ? 0.957   0.647   -9.064  1.00 34.74  ? 858 HOH A O   1 
HETATM 3626 O O   . HOH B 2 .   ? -17.181 -23.048 -12.105 1.00 32.20  ? 859 HOH A O   1 
HETATM 3627 O O   . HOH B 2 .   ? 18.383  -1.374  18.665  1.00 36.40  ? 860 HOH A O   1 
HETATM 3628 O O   . HOH B 2 .   ? -5.640  17.035  -19.613 1.00 30.25  ? 861 HOH A O   1 
HETATM 3629 O O   . HOH B 2 .   ? -6.122  17.969  -14.945 1.00 31.40  ? 862 HOH A O   1 
HETATM 3630 O O   . HOH B 2 .   ? 10.495  -13.936 14.474  1.00 29.36  ? 863 HOH A O   1 
HETATM 3631 O O   . HOH B 2 .   ? -8.402  18.672  28.280  1.00 33.27  ? 864 HOH A O   1 
HETATM 3632 O O   . HOH B 2 .   ? 2.134   -10.307 -1.629  1.00 31.75  ? 865 HOH A O   1 
HETATM 3633 O O   . HOH B 2 .   ? 12.379  14.755  18.662  1.00 35.94  ? 866 HOH A O   1 
HETATM 3634 O O   . HOH B 2 .   ? -15.764 17.613  9.773   1.00 16.80  ? 867 HOH A O   1 
HETATM 3635 O O   . HOH B 2 .   ? -0.165  0.864   29.990  1.00 25.88  ? 868 HOH A O   1 
HETATM 3636 O O   . HOH B 2 .   ? 1.360   6.848   -15.379 1.00 31.97  ? 869 HOH A O   1 
HETATM 3637 O O   . HOH B 2 .   ? 19.668  2.540   -12.579 1.00 45.98  ? 870 HOH A O   1 
HETATM 3638 O O   . HOH B 2 .   ? -7.622  -8.561  2.379   1.00 41.57  ? 871 HOH A O   1 
HETATM 3639 O O   . HOH B 2 .   ? 14.605  -12.242 -7.258  1.00 35.02  ? 872 HOH A O   1 
HETATM 3640 O O   . HOH B 2 .   ? 9.017   10.668  20.700  1.00 20.64  ? 873 HOH A O   1 
HETATM 3641 O O   . HOH B 2 .   ? 18.883  10.222  11.631  1.00 40.05  ? 874 HOH A O   1 
HETATM 3642 O O   . HOH B 2 .   ? -14.118 15.818  23.350  1.00 23.81  ? 875 HOH A O   1 
HETATM 3643 O O   . HOH B 2 .   ? -20.177 -14.671 -6.686  1.00 29.53  ? 876 HOH A O   1 
HETATM 3644 O O   . HOH B 2 .   ? 5.476   19.905  -9.300  1.00 27.68  ? 877 HOH A O   1 
HETATM 3645 O O   . HOH B 2 .   ? -1.029  -15.834 -28.188 1.00 31.43  ? 878 HOH A O   1 
HETATM 3646 O O   . HOH B 2 .   ? -4.274  18.606  18.463  1.00 19.55  ? 879 HOH A O   1 
HETATM 3647 O O   . HOH B 2 .   ? 18.025  -0.787  11.462  1.00 20.36  ? 880 HOH A O   1 
HETATM 3648 O O   . HOH B 2 .   ? 3.385   23.707  -3.493  1.00 36.32  ? 881 HOH A O   1 
HETATM 3649 O O   . HOH B 2 .   ? -3.001  22.396  -11.146 1.00 35.67  ? 882 HOH A O   1 
HETATM 3650 O O   . HOH B 2 .   ? 2.829   16.971  -13.892 1.00 32.30  ? 883 HOH A O   1 
HETATM 3651 O O   . HOH B 2 .   ? 10.357  13.059  21.601  1.00 30.47  ? 884 HOH A O   1 
HETATM 3652 O O   . HOH B 2 .   ? 18.550  -3.367  11.352  1.00 40.63  ? 885 HOH A O   1 
HETATM 3653 O O   . HOH B 2 .   ? -2.114  -1.547  -3.061  1.00 25.47  ? 886 HOH A O   1 
HETATM 3654 O O   . HOH B 2 .   ? 3.793   -14.270 1.311   1.00 24.61  ? 887 HOH A O   1 
HETATM 3655 O O   . HOH B 2 .   ? -6.757  16.721  21.572  1.00 25.16  ? 888 HOH A O   1 
HETATM 3656 O O   . HOH B 2 .   ? -19.662 -15.956 -13.905 1.00 31.89  ? 889 HOH A O   1 
HETATM 3657 O O   . HOH B 2 .   ? -19.571 12.066  7.773   1.00 19.30  ? 890 HOH A O   1 
HETATM 3658 O O   . HOH B 2 .   ? 2.866   -24.293 -27.525 1.00 28.38  ? 891 HOH A O   1 
HETATM 3659 O O   . HOH B 2 .   ? -10.918 2.033   24.364  1.00 50.17  ? 892 HOH A O   1 
HETATM 3660 O O   . HOH B 2 .   ? 19.602  -6.769  3.203   1.00 60.00  ? 893 HOH A O   1 
HETATM 3661 O O   . HOH B 2 .   ? -8.415  -3.599  -17.974 1.00 42.63  ? 894 HOH A O   1 
HETATM 3662 O O   . HOH B 2 .   ? -19.127 15.318  12.247  1.00 46.31  ? 895 HOH A O   1 
HETATM 3663 O O   . HOH B 2 .   ? -2.480  -17.212 -0.032  1.00 40.74  ? 896 HOH A O   1 
HETATM 3664 O O   . HOH B 2 .   ? 4.967   14.107  29.041  1.00 34.76  ? 897 HOH A O   1 
HETATM 3665 O O   . HOH B 2 .   ? 1.305   23.236  23.574  1.00 44.90  ? 898 HOH A O   1 
HETATM 3666 O O   . HOH B 2 .   ? 12.861  22.549  8.848   1.00 55.06  ? 899 HOH A O   1 
HETATM 3667 O O   . HOH B 2 .   ? 2.028   -1.757  27.348  1.00 30.88  ? 900 HOH A O   1 
HETATM 3668 O O   . HOH B 2 .   ? 5.373   -23.868 3.403   1.00 37.44  ? 901 HOH A O   1 
HETATM 3669 O O   . HOH B 2 .   ? -14.435 23.271  11.139  1.00 31.50  ? 902 HOH A O   1 
HETATM 3670 O O   . HOH B 2 .   ? 13.018  -14.200 -1.870  1.00 27.32  ? 903 HOH A O   1 
HETATM 3671 O O   . HOH B 2 .   ? 2.143   22.801  26.436  1.00 33.52  ? 904 HOH A O   1 
HETATM 3672 O O   . HOH B 2 .   ? 6.398   6.726   25.600  1.00 35.65  ? 905 HOH A O   1 
HETATM 3673 O O   . HOH B 2 .   ? -7.556  -23.257 -5.027  1.00 34.79  ? 906 HOH A O   1 
HETATM 3674 O O   . HOH B 2 .   ? -15.950 11.938  -10.825 1.00 41.44  ? 907 HOH A O   1 
HETATM 3675 O O   . HOH B 2 .   ? -4.397  -27.926 -16.721 1.00 42.50  ? 908 HOH A O   1 
HETATM 3676 O O   . HOH B 2 .   ? 3.388   -3.263  -25.331 1.00 40.66  ? 909 HOH A O   1 
HETATM 3677 O O   . HOH B 2 .   ? 4.948   21.038  -11.637 1.00 39.90  ? 910 HOH A O   1 
HETATM 3678 O O   . HOH B 2 .   ? -17.180 -16.597 -24.688 1.00 29.69  ? 911 HOH A O   1 
HETATM 3679 O O   . HOH B 2 .   ? 7.780   23.498  -5.299  1.00 41.15  ? 912 HOH A O   1 
HETATM 3680 O O   . HOH B 2 .   ? -11.168 26.651  2.006   1.00 27.14  ? 913 HOH A O   1 
HETATM 3681 O O   . HOH B 2 .   ? -10.187 20.288  16.777  1.00 32.56  ? 914 HOH A O   1 
HETATM 3682 O O   . HOH B 2 .   ? 10.370  -25.980 -4.605  1.00 43.40  ? 915 HOH A O   1 
HETATM 3683 O O   . HOH B 2 .   ? 5.399   -13.397 20.720  1.00 35.36  ? 916 HOH A O   1 
HETATM 3684 O O   . HOH B 2 .   ? 11.292  -7.223  20.441  1.00 32.11  ? 917 HOH A O   1 
HETATM 3685 O O   . HOH B 2 .   ? -3.934  -26.107 -13.272 1.00 46.34  ? 918 HOH A O   1 
HETATM 3686 O O   . HOH B 2 .   ? 10.131  18.756  18.670  1.00 41.11  ? 919 HOH A O   1 
HETATM 3687 O O   . HOH B 2 .   ? -13.583 17.595  -4.479  1.00 23.46  ? 920 HOH A O   1 
HETATM 3688 O O   . HOH B 2 .   ? 16.133  -7.422  -3.557  1.00 28.51  ? 921 HOH A O   1 
HETATM 3689 O O   . HOH B 2 .   ? -7.487  23.255  16.326  1.00 30.83  ? 922 HOH A O   1 
HETATM 3690 O O   . HOH B 2 .   ? -3.738  24.039  30.340  1.00 23.41  ? 923 HOH A O   1 
HETATM 3691 O O   . HOH B 2 .   ? -17.605 -24.323 -16.757 1.00 32.99  ? 924 HOH A O   1 
HETATM 3692 O O   . HOH B 2 .   ? 0.796   21.759  -2.997  1.00 31.10  ? 925 HOH A O   1 
HETATM 3693 O O   . HOH B 2 .   ? -5.014  24.005  16.718  1.00 30.23  ? 926 HOH A O   1 
HETATM 3694 O O   . HOH B 2 .   ? 16.719  0.122   1.761   1.00 36.77  ? 927 HOH A O   1 
HETATM 3695 O O   . HOH B 2 .   ? 10.482  25.352  15.920  1.00 57.67  ? 928 HOH A O   1 
HETATM 3696 O O   . HOH B 2 .   ? -4.169  22.994  19.481  1.00 38.81  ? 929 HOH A O   1 
HETATM 3697 O O   . HOH B 2 .   ? 7.563   -18.950 7.638   1.00 22.52  ? 930 HOH A O   1 
HETATM 3698 O O   . HOH B 2 .   ? 15.800  -22.361 2.043   1.00 62.32  ? 931 HOH A O   1 
HETATM 3699 O O   . HOH B 2 .   ? 18.145  -20.429 -17.299 1.00 46.75  ? 932 HOH A O   1 
HETATM 3700 O O   . HOH B 2 .   ? 15.362  -3.340  -5.341  1.00 40.56  ? 933 HOH A O   1 
HETATM 3701 O O   . HOH B 2 .   ? -1.264  -27.035 -5.098  1.00 44.21  ? 934 HOH A O   1 
HETATM 3702 O O   . HOH B 2 .   ? -7.073  28.477  4.811   1.00 33.83  ? 935 HOH A O   1 
HETATM 3703 O O   . HOH B 2 .   ? -15.718 0.453   10.387  1.00 32.15  ? 936 HOH A O   1 
HETATM 3704 O O   . HOH B 2 .   ? 17.110  7.599   -10.237 1.00 45.85  ? 937 HOH A O   1 
HETATM 3705 O O   . HOH B 2 .   ? 1.111   23.749  -1.964  1.00 33.49  ? 938 HOH A O   1 
HETATM 3706 O O   . HOH B 2 .   ? 0.628   6.812   -12.962 1.00 35.03  ? 939 HOH A O   1 
HETATM 3707 O O   . HOH B 2 .   ? -5.366  -6.503  1.050   1.00 27.99  ? 940 HOH A O   1 
HETATM 3708 O O   . HOH B 2 .   ? 2.105   26.145  13.264  1.00 32.44  ? 941 HOH A O   1 
HETATM 3709 O O   . HOH B 2 .   ? 18.229  4.153   2.556   1.00 22.70  ? 942 HOH A O   1 
HETATM 3710 O O   . HOH B 2 .   ? -13.269 14.849  -3.933  1.00 25.00  ? 943 HOH A O   1 
HETATM 3711 O O   . HOH B 2 .   ? 2.111   -21.731 -6.236  1.00 38.90  ? 944 HOH A O   1 
HETATM 3712 O O   . HOH B 2 .   ? 13.460  5.188   -17.767 1.00 61.88  ? 945 HOH A O   1 
HETATM 3713 O O   . HOH B 2 .   ? 14.038  7.497   16.223  1.00 41.62  ? 946 HOH A O   1 
HETATM 3714 O O   . HOH B 2 .   ? -1.717  4.290   -7.173  1.00 24.09  ? 947 HOH A O   1 
HETATM 3715 O O   . HOH B 2 .   ? -15.292 18.863  12.235  1.00 25.50  ? 948 HOH A O   1 
HETATM 3716 O O   . HOH B 2 .   ? -7.137  -2.404  -22.627 1.00 37.66  ? 949 HOH A O   1 
HETATM 3717 O O   . HOH B 2 .   ? 16.363  8.948   12.450  1.00 25.25  ? 950 HOH A O   1 
HETATM 3718 O O   . HOH B 2 .   ? 16.639  -17.009 1.273   1.00 46.28  ? 951 HOH A O   1 
HETATM 3719 O O   . HOH B 2 .   ? -18.248 -15.632 -19.766 1.00 39.69  ? 952 HOH A O   1 
HETATM 3720 O O   . HOH B 2 .   ? 7.046   -0.187  27.762  1.00 39.70  ? 953 HOH A O   1 
HETATM 3721 O O   . HOH B 2 .   ? 17.148  3.391   0.159   1.00 41.98  ? 954 HOH A O   1 
HETATM 3722 O O   . HOH B 2 .   ? -4.410  27.600  3.734   1.00 41.32  ? 955 HOH A O   1 
HETATM 3723 O O   . HOH B 2 .   ? 12.975  -9.744  8.800   1.00 29.11  ? 956 HOH A O   1 
HETATM 3724 O O   . HOH B 2 .   ? -17.468 17.955  24.935  1.00 29.99  ? 957 HOH A O   1 
HETATM 3725 O O   . HOH B 2 .   ? 15.170  5.361   13.788  1.00 40.97  ? 958 HOH A O   1 
HETATM 3726 O O   . HOH B 2 .   ? -19.951 12.590  18.641  1.00 56.89  ? 959 HOH A O   1 
HETATM 3727 O O   . HOH B 2 .   ? -11.928 14.320  -9.842  1.00 34.31  ? 960 HOH A O   1 
HETATM 3728 O O   . HOH B 2 .   ? -20.655 10.553  -6.753  1.00 36.58  ? 961 HOH A O   1 
HETATM 3729 O O   . HOH B 2 .   ? -5.016  -14.165 18.453  1.00 30.98  ? 962 HOH A O   1 
HETATM 3730 O O   . HOH B 2 .   ? -17.551 18.523  16.774  1.00 40.67  ? 963 HOH A O   1 
HETATM 3731 O O   . HOH B 2 .   ? -8.692  -12.362 4.845   1.00 41.61  ? 964 HOH A O   1 
HETATM 3732 O O   . HOH B 2 .   ? 14.008  4.602   1.423   1.00 18.92  ? 965 HOH A O   1 
HETATM 3733 O O   . HOH B 2 .   ? -16.547 -26.836 -17.245 1.00 37.28  ? 966 HOH A O   1 
HETATM 3734 O O   . HOH B 2 .   ? 13.588  -4.582  21.410  1.00 37.03  ? 967 HOH A O   1 
HETATM 3735 O O   . HOH B 2 .   ? -20.563 13.846  9.417   1.00 30.59  ? 968 HOH A O   1 
HETATM 3736 O O   . HOH B 2 .   ? -11.032 16.831  24.796  1.00 35.16  ? 969 HOH A O   1 
HETATM 3737 O O   . HOH B 2 .   ? -11.972 14.473  -6.261  1.00 28.49  ? 970 HOH A O   1 
HETATM 3738 O O   . HOH B 2 .   ? -4.826  21.399  -9.304  1.00 30.93  ? 971 HOH A O   1 
HETATM 3739 O O   . HOH B 2 .   ? 19.393  -4.247  -3.981  1.00 43.40  ? 972 HOH A O   1 
HETATM 3740 O O   . HOH B 2 .   ? 12.783  19.442  6.431   1.00 38.04  ? 973 HOH A O   1 
HETATM 3741 O O   . HOH B 2 .   ? 18.089  -6.870  14.989  1.00 75.91  ? 974 HOH A O   1 
HETATM 3742 O O   . HOH B 2 .   ? 6.531   -22.058 4.774   1.00 33.15  ? 975 HOH A O   1 
HETATM 3743 O O   . HOH B 2 .   ? 16.932  18.014  6.375   1.00 23.84  ? 976 HOH A O   1 
HETATM 3744 O O   . HOH B 2 .   ? 3.916   24.104  4.805   1.00 32.48  ? 977 HOH A O   1 
HETATM 3745 O O   . HOH B 2 .   ? -8.202  20.101  20.344  1.00 34.86  ? 978 HOH A O   1 
HETATM 3746 O O   . HOH B 2 .   ? -0.641  6.391   -8.382  1.00 24.81  ? 979 HOH A O   1 
HETATM 3747 O O   . HOH B 2 .   ? 12.499  -9.605  -5.051  1.00 39.41  ? 980 HOH A O   1 
HETATM 3748 O O   . HOH B 2 .   ? -5.175  -8.155  28.971  1.00 36.10  ? 981 HOH A O   1 
HETATM 3749 O O   . HOH B 2 .   ? 7.082   27.676  25.834  1.00 32.64  ? 982 HOH A O   1 
HETATM 3750 O O   . HOH B 2 .   ? -1.626  -18.529 16.984  1.00 42.04  ? 983 HOH A O   1 
HETATM 3751 O O   . HOH B 2 .   ? -4.664  27.016  16.551  1.00 39.98  ? 984 HOH A O   1 
HETATM 3752 O O   . HOH B 2 .   ? -8.214  -13.774 16.088  1.00 24.60  ? 985 HOH A O   1 
HETATM 3753 O O   . HOH B 2 .   ? -18.426 16.907  18.709  1.00 38.27  ? 986 HOH A O   1 
HETATM 3754 O O   . HOH B 2 .   ? -1.459  -26.748 -14.178 1.00 42.83  ? 987 HOH A O   1 
HETATM 3755 O O   . HOH B 2 .   ? -9.578  3.537   31.137  1.00 45.81  ? 988 HOH A O   1 
HETATM 3756 O O   . HOH B 2 .   ? -12.292 -26.802 -15.058 1.00 41.77  ? 989 HOH A O   1 
HETATM 3757 O O   . HOH B 2 .   ? 0.221   -26.650 -9.641  1.00 28.51  ? 990 HOH A O   1 
HETATM 3758 O O   . HOH B 2 .   ? 12.625  8.568   -11.756 1.00 34.73  ? 991 HOH A O   1 
HETATM 3759 O O   . HOH B 2 .   ? 7.006   23.310  7.838   1.00 37.68  ? 992 HOH A O   1 
HETATM 3760 O O   . HOH B 2 .   ? -5.665  -7.200  31.344  1.00 41.69  ? 993 HOH A O   1 
HETATM 3761 O O   . HOH B 2 .   ? 13.883  -8.103  15.847  1.00 28.13  ? 994 HOH A O   1 
HETATM 3762 O O   . HOH B 2 .   ? -5.335  -16.852 18.554  1.00 48.08  ? 995 HOH A O   1 
# 
