data_8Z5B
# 
_entry.id   8Z5B 
# 
_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   8Z5B         pdb_00008z5b 10.2210/pdb8z5b/pdb 
WWPDB D_1300046751 ?            ?                   
# 
_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       2025-02-19 
# 
_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                        8Z5B 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-18 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_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              wangyajie@westlake.edu.cn 
_pdbx_contact_author.name_first         yajie 
_pdbx_contact_author.name_last          wang 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-6216-791X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Qian, H.' 1 ? 
'Wang, Y.' 2 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'The X-Ray crystal structure of multicopper oxidase from Bacillus freudenreichii' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Wang, Y.' 1 ? 
primary 'Qian, H.' 2 ? 
# 
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 'Multicopper oxidase' 63651.727 1   1.16.3.4 ? ? ? 
2 non-polymer syn 'MANGANESE (II) ION'  54.938    1   ?        ? ? ? 
3 non-polymer syn 'COPPER (II) ION'     63.546    2   ?        ? ? ? 
4 water       nat water                 18.015    627 ?        ? ? ? 
# 
_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       
;MGSSHHHHHHSSGLVPRGSHMASMTGGQQMGRGSMKIKNKRRMKVDPSNPETIPKYMDELPIPPVARPLAEIKGSPYYEI
AMRQVPHRFHRLFPPTTVWGYDGMLPGPTIKVQKDEKIYVRWKNKLPEKHLLPIDRTLHETAGPPDVRTVVHLHGANVAW
DSDGHPEAWFSRDFAKTGATFRRKVYEYTNKQMGATLWYHDHAIGITRLNVYSGLSGFYLIEDPVEKHLKLPKDGYDIPL
MIQDRSFRSDGSLSYPENTNPPAPVNPSVQPFFIGNTIAVNGKIWPKLTVEPRKYRFRILNASNTNAYTLRLGDGRKFYQ
ISTDGGLLTEPVELTTLPLEPAERSDVIIDFSQHKGKKLILQNTNAEGNMGIIMRFDVLQPLRGRDTSEIPAKLISEEQV
LYEHHADKTRLLKLDAIQDEYNRPVLLLDDRMWHDPVTEKPVIGDTEVWKLINVTNFAHPIHIHLIQFKILHRTPFDLER
FQQDGYIDYTGPPIEPAVHERGWKDTVKAEPGMVTSVIMKFTENPGEYVWHCHILEHEDYDMMRPMRVVEKEK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGSSHHHHHHSSGLVPRGSHMASMTGGQQMGRGSMKIKNKRRMKVDPSNPETIPKYMDELPIPPVARPLAEIKGSPYYEI
AMRQVPHRFHRLFPPTTVWGYDGMLPGPTIKVQKDEKIYVRWKNKLPEKHLLPIDRTLHETAGPPDVRTVVHLHGANVAW
DSDGHPEAWFSRDFAKTGATFRRKVYEYTNKQMGATLWYHDHAIGITRLNVYSGLSGFYLIEDPVEKHLKLPKDGYDIPL
MIQDRSFRSDGSLSYPENTNPPAPVNPSVQPFFIGNTIAVNGKIWPKLTVEPRKYRFRILNASNTNAYTLRLGDGRKFYQ
ISTDGGLLTEPVELTTLPLEPAERSDVIIDFSQHKGKKLILQNTNAEGNMGIIMRFDVLQPLRGRDTSEIPAKLISEEQV
LYEHHADKTRLLKLDAIQDEYNRPVLLLDDRMWHDPVTEKPVIGDTEVWKLINVTNFAHPIHIHLIQFKILHRTPFDLER
FQQDGYIDYTGPPIEPAVHERGWKDTVKAEPGMVTSVIMKFTENPGEYVWHCHILEHEDYDMMRPMRVVEKEK
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'MANGANESE (II) ION' MN  
3 'COPPER (II) ION'    CU  
4 water                HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   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  SER n 
1 13  GLY n 
1 14  LEU n 
1 15  VAL n 
1 16  PRO n 
1 17  ARG n 
1 18  GLY n 
1 19  SER n 
1 20  HIS n 
1 21  MET n 
1 22  ALA n 
1 23  SER n 
1 24  MET n 
1 25  THR n 
1 26  GLY n 
1 27  GLY n 
1 28  GLN n 
1 29  GLN n 
1 30  MET n 
1 31  GLY n 
1 32  ARG n 
1 33  GLY n 
1 34  SER n 
1 35  MET n 
1 36  LYS n 
1 37  ILE n 
1 38  LYS n 
1 39  ASN n 
1 40  LYS n 
1 41  ARG n 
1 42  ARG n 
1 43  MET n 
1 44  LYS n 
1 45  VAL n 
1 46  ASP n 
1 47  PRO n 
1 48  SER n 
1 49  ASN n 
1 50  PRO n 
1 51  GLU n 
1 52  THR n 
1 53  ILE n 
1 54  PRO n 
1 55  LYS n 
1 56  TYR n 
1 57  MET n 
1 58  ASP n 
1 59  GLU n 
1 60  LEU n 
1 61  PRO n 
1 62  ILE n 
1 63  PRO n 
1 64  PRO n 
1 65  VAL n 
1 66  ALA n 
1 67  ARG n 
1 68  PRO n 
1 69  LEU n 
1 70  ALA n 
1 71  GLU n 
1 72  ILE n 
1 73  LYS n 
1 74  GLY n 
1 75  SER n 
1 76  PRO n 
1 77  TYR n 
1 78  TYR n 
1 79  GLU n 
1 80  ILE n 
1 81  ALA n 
1 82  MET n 
1 83  ARG n 
1 84  GLN n 
1 85  VAL n 
1 86  PRO n 
1 87  HIS n 
1 88  ARG n 
1 89  PHE n 
1 90  HIS n 
1 91  ARG n 
1 92  LEU n 
1 93  PHE n 
1 94  PRO n 
1 95  PRO n 
1 96  THR n 
1 97  THR n 
1 98  VAL n 
1 99  TRP n 
1 100 GLY n 
1 101 TYR n 
1 102 ASP n 
1 103 GLY n 
1 104 MET n 
1 105 LEU n 
1 106 PRO n 
1 107 GLY n 
1 108 PRO n 
1 109 THR n 
1 110 ILE n 
1 111 LYS n 
1 112 VAL n 
1 113 GLN n 
1 114 LYS n 
1 115 ASP n 
1 116 GLU n 
1 117 LYS n 
1 118 ILE n 
1 119 TYR n 
1 120 VAL n 
1 121 ARG n 
1 122 TRP n 
1 123 LYS n 
1 124 ASN n 
1 125 LYS n 
1 126 LEU n 
1 127 PRO n 
1 128 GLU n 
1 129 LYS n 
1 130 HIS n 
1 131 LEU n 
1 132 LEU n 
1 133 PRO n 
1 134 ILE n 
1 135 ASP n 
1 136 ARG n 
1 137 THR n 
1 138 LEU n 
1 139 HIS n 
1 140 GLU n 
1 141 THR n 
1 142 ALA n 
1 143 GLY n 
1 144 PRO n 
1 145 PRO n 
1 146 ASP n 
1 147 VAL n 
1 148 ARG n 
1 149 THR n 
1 150 VAL n 
1 151 VAL n 
1 152 HIS n 
1 153 LEU n 
1 154 HIS n 
1 155 GLY n 
1 156 ALA n 
1 157 ASN n 
1 158 VAL n 
1 159 ALA n 
1 160 TRP n 
1 161 ASP n 
1 162 SER n 
1 163 ASP n 
1 164 GLY n 
1 165 HIS n 
1 166 PRO n 
1 167 GLU n 
1 168 ALA n 
1 169 TRP n 
1 170 PHE n 
1 171 SER n 
1 172 ARG n 
1 173 ASP n 
1 174 PHE n 
1 175 ALA n 
1 176 LYS n 
1 177 THR n 
1 178 GLY n 
1 179 ALA n 
1 180 THR n 
1 181 PHE n 
1 182 ARG n 
1 183 ARG n 
1 184 LYS n 
1 185 VAL n 
1 186 TYR n 
1 187 GLU n 
1 188 TYR n 
1 189 THR n 
1 190 ASN n 
1 191 LYS n 
1 192 GLN n 
1 193 MET n 
1 194 GLY n 
1 195 ALA n 
1 196 THR n 
1 197 LEU n 
1 198 TRP n 
1 199 TYR n 
1 200 HIS n 
1 201 ASP n 
1 202 HIS n 
1 203 ALA n 
1 204 ILE n 
1 205 GLY n 
1 206 ILE n 
1 207 THR n 
1 208 ARG n 
1 209 LEU n 
1 210 ASN n 
1 211 VAL n 
1 212 TYR n 
1 213 SER n 
1 214 GLY n 
1 215 LEU n 
1 216 SER n 
1 217 GLY n 
1 218 PHE n 
1 219 TYR n 
1 220 LEU n 
1 221 ILE n 
1 222 GLU n 
1 223 ASP n 
1 224 PRO n 
1 225 VAL n 
1 226 GLU n 
1 227 LYS n 
1 228 HIS n 
1 229 LEU n 
1 230 LYS n 
1 231 LEU n 
1 232 PRO n 
1 233 LYS n 
1 234 ASP n 
1 235 GLY n 
1 236 TYR n 
1 237 ASP n 
1 238 ILE n 
1 239 PRO n 
1 240 LEU n 
1 241 MET n 
1 242 ILE n 
1 243 GLN n 
1 244 ASP n 
1 245 ARG n 
1 246 SER n 
1 247 PHE n 
1 248 ARG n 
1 249 SER n 
1 250 ASP n 
1 251 GLY n 
1 252 SER n 
1 253 LEU n 
1 254 SER n 
1 255 TYR n 
1 256 PRO n 
1 257 GLU n 
1 258 ASN n 
1 259 THR n 
1 260 ASN n 
1 261 PRO n 
1 262 PRO n 
1 263 ALA n 
1 264 PRO n 
1 265 VAL n 
1 266 ASN n 
1 267 PRO n 
1 268 SER n 
1 269 VAL n 
1 270 GLN n 
1 271 PRO n 
1 272 PHE n 
1 273 PHE n 
1 274 ILE n 
1 275 GLY n 
1 276 ASN n 
1 277 THR n 
1 278 ILE n 
1 279 ALA n 
1 280 VAL n 
1 281 ASN n 
1 282 GLY n 
1 283 LYS n 
1 284 ILE n 
1 285 TRP n 
1 286 PRO n 
1 287 LYS n 
1 288 LEU n 
1 289 THR n 
1 290 VAL n 
1 291 GLU n 
1 292 PRO n 
1 293 ARG n 
1 294 LYS n 
1 295 TYR n 
1 296 ARG n 
1 297 PHE n 
1 298 ARG n 
1 299 ILE n 
1 300 LEU n 
1 301 ASN n 
1 302 ALA n 
1 303 SER n 
1 304 ASN n 
1 305 THR n 
1 306 ASN n 
1 307 ALA n 
1 308 TYR n 
1 309 THR n 
1 310 LEU n 
1 311 ARG n 
1 312 LEU n 
1 313 GLY n 
1 314 ASP n 
1 315 GLY n 
1 316 ARG n 
1 317 LYS n 
1 318 PHE n 
1 319 TYR n 
1 320 GLN n 
1 321 ILE n 
1 322 SER n 
1 323 THR n 
1 324 ASP n 
1 325 GLY n 
1 326 GLY n 
1 327 LEU n 
1 328 LEU n 
1 329 THR n 
1 330 GLU n 
1 331 PRO n 
1 332 VAL n 
1 333 GLU n 
1 334 LEU n 
1 335 THR n 
1 336 THR n 
1 337 LEU n 
1 338 PRO n 
1 339 LEU n 
1 340 GLU n 
1 341 PRO n 
1 342 ALA n 
1 343 GLU n 
1 344 ARG n 
1 345 SER n 
1 346 ASP n 
1 347 VAL n 
1 348 ILE n 
1 349 ILE n 
1 350 ASP n 
1 351 PHE n 
1 352 SER n 
1 353 GLN n 
1 354 HIS n 
1 355 LYS n 
1 356 GLY n 
1 357 LYS n 
1 358 LYS n 
1 359 LEU n 
1 360 ILE n 
1 361 LEU n 
1 362 GLN n 
1 363 ASN n 
1 364 THR n 
1 365 ASN n 
1 366 ALA n 
1 367 GLU n 
1 368 GLY n 
1 369 ASN n 
1 370 MET n 
1 371 GLY n 
1 372 ILE n 
1 373 ILE n 
1 374 MET n 
1 375 ARG n 
1 376 PHE n 
1 377 ASP n 
1 378 VAL n 
1 379 LEU n 
1 380 GLN n 
1 381 PRO n 
1 382 LEU n 
1 383 ARG n 
1 384 GLY n 
1 385 ARG n 
1 386 ASP n 
1 387 THR n 
1 388 SER n 
1 389 GLU n 
1 390 ILE n 
1 391 PRO n 
1 392 ALA n 
1 393 LYS n 
1 394 LEU n 
1 395 ILE n 
1 396 SER n 
1 397 GLU n 
1 398 GLU n 
1 399 GLN n 
1 400 VAL n 
1 401 LEU n 
1 402 TYR n 
1 403 GLU n 
1 404 HIS n 
1 405 HIS n 
1 406 ALA n 
1 407 ASP n 
1 408 LYS n 
1 409 THR n 
1 410 ARG n 
1 411 LEU n 
1 412 LEU n 
1 413 LYS n 
1 414 LEU n 
1 415 ASP n 
1 416 ALA n 
1 417 ILE n 
1 418 GLN n 
1 419 ASP n 
1 420 GLU n 
1 421 TYR n 
1 422 ASN n 
1 423 ARG n 
1 424 PRO n 
1 425 VAL n 
1 426 LEU n 
1 427 LEU n 
1 428 LEU n 
1 429 ASP n 
1 430 ASP n 
1 431 ARG n 
1 432 MET n 
1 433 TRP n 
1 434 HIS n 
1 435 ASP n 
1 436 PRO n 
1 437 VAL n 
1 438 THR n 
1 439 GLU n 
1 440 LYS n 
1 441 PRO n 
1 442 VAL n 
1 443 ILE n 
1 444 GLY n 
1 445 ASP n 
1 446 THR n 
1 447 GLU n 
1 448 VAL n 
1 449 TRP n 
1 450 LYS n 
1 451 LEU n 
1 452 ILE n 
1 453 ASN n 
1 454 VAL n 
1 455 THR n 
1 456 ASN n 
1 457 PHE n 
1 458 ALA n 
1 459 HIS n 
1 460 PRO n 
1 461 ILE n 
1 462 HIS n 
1 463 ILE n 
1 464 HIS n 
1 465 LEU n 
1 466 ILE n 
1 467 GLN n 
1 468 PHE n 
1 469 LYS n 
1 470 ILE n 
1 471 LEU n 
1 472 HIS n 
1 473 ARG n 
1 474 THR n 
1 475 PRO n 
1 476 PHE n 
1 477 ASP n 
1 478 LEU n 
1 479 GLU n 
1 480 ARG n 
1 481 PHE n 
1 482 GLN n 
1 483 GLN n 
1 484 ASP n 
1 485 GLY n 
1 486 TYR n 
1 487 ILE n 
1 488 ASP n 
1 489 TYR n 
1 490 THR n 
1 491 GLY n 
1 492 PRO n 
1 493 PRO n 
1 494 ILE n 
1 495 GLU n 
1 496 PRO n 
1 497 ALA n 
1 498 VAL n 
1 499 HIS n 
1 500 GLU n 
1 501 ARG n 
1 502 GLY n 
1 503 TRP n 
1 504 LYS n 
1 505 ASP n 
1 506 THR n 
1 507 VAL n 
1 508 LYS n 
1 509 ALA n 
1 510 GLU n 
1 511 PRO n 
1 512 GLY n 
1 513 MET n 
1 514 VAL n 
1 515 THR n 
1 516 SER n 
1 517 VAL n 
1 518 ILE n 
1 519 MET n 
1 520 LYS n 
1 521 PHE n 
1 522 THR n 
1 523 GLU n 
1 524 ASN n 
1 525 PRO n 
1 526 GLY n 
1 527 GLU n 
1 528 TYR n 
1 529 VAL n 
1 530 TRP n 
1 531 HIS n 
1 532 CYS n 
1 533 HIS n 
1 534 ILE n 
1 535 LEU n 
1 536 GLU n 
1 537 HIS n 
1 538 GLU n 
1 539 ASP n 
1 540 TYR n 
1 541 ASP n 
1 542 MET n 
1 543 MET n 
1 544 ARG n 
1 545 PRO n 
1 546 MET n 
1 547 ARG n 
1 548 VAL n 
1 549 VAL n 
1 550 GLU n 
1 551 LYS n 
1 552 GLU n 
1 553 LYS 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                   553 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Bacillus freudenreichii' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1783501 
_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' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_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 
CU  non-polymer         . 'COPPER (II) ION'    ? 'Cu 2'           63.546  
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 
MN  non-polymer         . 'MANGANESE (II) ION' ? 'Mn 2'           54.938  
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   1   ?   ?   ?   A . n 
A 1 2   GLY 2   2   ?   ?   ?   A . n 
A 1 3   SER 3   3   ?   ?   ?   A . n 
A 1 4   SER 4   4   ?   ?   ?   A . n 
A 1 5   HIS 5   5   ?   ?   ?   A . n 
A 1 6   HIS 6   6   ?   ?   ?   A . n 
A 1 7   HIS 7   7   ?   ?   ?   A . n 
A 1 8   HIS 8   8   ?   ?   ?   A . n 
A 1 9   HIS 9   9   ?   ?   ?   A . n 
A 1 10  HIS 10  10  ?   ?   ?   A . n 
A 1 11  SER 11  11  ?   ?   ?   A . n 
A 1 12  SER 12  12  ?   ?   ?   A . n 
A 1 13  GLY 13  13  ?   ?   ?   A . n 
A 1 14  LEU 14  14  ?   ?   ?   A . n 
A 1 15  VAL 15  15  ?   ?   ?   A . n 
A 1 16  PRO 16  16  ?   ?   ?   A . n 
A 1 17  ARG 17  17  ?   ?   ?   A . n 
A 1 18  GLY 18  18  ?   ?   ?   A . n 
A 1 19  SER 19  19  ?   ?   ?   A . n 
A 1 20  HIS 20  20  ?   ?   ?   A . n 
A 1 21  MET 21  21  ?   ?   ?   A . n 
A 1 22  ALA 22  22  ?   ?   ?   A . n 
A 1 23  SER 23  23  ?   ?   ?   A . n 
A 1 24  MET 24  24  ?   ?   ?   A . n 
A 1 25  THR 25  25  ?   ?   ?   A . n 
A 1 26  GLY 26  26  ?   ?   ?   A . n 
A 1 27  GLY 27  27  ?   ?   ?   A . n 
A 1 28  GLN 28  28  ?   ?   ?   A . n 
A 1 29  GLN 29  29  ?   ?   ?   A . n 
A 1 30  MET 30  30  ?   ?   ?   A . n 
A 1 31  GLY 31  31  ?   ?   ?   A . n 
A 1 32  ARG 32  32  ?   ?   ?   A . n 
A 1 33  GLY 33  33  ?   ?   ?   A . n 
A 1 34  SER 34  34  ?   ?   ?   A . n 
A 1 35  MET 35  35  ?   ?   ?   A . n 
A 1 36  LYS 36  36  ?   ?   ?   A . n 
A 1 37  ILE 37  37  ?   ?   ?   A . n 
A 1 38  LYS 38  38  ?   ?   ?   A . n 
A 1 39  ASN 39  39  ?   ?   ?   A . n 
A 1 40  LYS 40  40  ?   ?   ?   A . n 
A 1 41  ARG 41  41  ?   ?   ?   A . n 
A 1 42  ARG 42  42  ?   ?   ?   A . n 
A 1 43  MET 43  43  ?   ?   ?   A . n 
A 1 44  LYS 44  44  44  LYS LYS A . n 
A 1 45  VAL 45  45  45  VAL VAL A . n 
A 1 46  ASP 46  46  46  ASP ASP A . n 
A 1 47  PRO 47  47  47  PRO PRO A . n 
A 1 48  SER 48  48  48  SER SER A . n 
A 1 49  ASN 49  49  49  ASN ASN A . n 
A 1 50  PRO 50  50  50  PRO PRO A . n 
A 1 51  GLU 51  51  51  GLU GLU A . n 
A 1 52  THR 52  52  52  THR THR A . n 
A 1 53  ILE 53  53  53  ILE ILE A . n 
A 1 54  PRO 54  54  54  PRO PRO A . n 
A 1 55  LYS 55  55  55  LYS LYS A . n 
A 1 56  TYR 56  56  56  TYR TYR A . n 
A 1 57  MET 57  57  57  MET MET A . n 
A 1 58  ASP 58  58  58  ASP ASP A . n 
A 1 59  GLU 59  59  59  GLU GLU A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  PRO 61  61  61  PRO PRO A . n 
A 1 62  ILE 62  62  62  ILE ILE A . n 
A 1 63  PRO 63  63  63  PRO PRO A . n 
A 1 64  PRO 64  64  64  PRO PRO A . n 
A 1 65  VAL 65  65  65  VAL VAL A . n 
A 1 66  ALA 66  66  66  ALA ALA A . n 
A 1 67  ARG 67  67  67  ARG ARG A . n 
A 1 68  PRO 68  68  68  PRO PRO A . n 
A 1 69  LEU 69  69  69  LEU LEU A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  GLU 71  71  71  GLU GLU A . n 
A 1 72  ILE 72  72  72  ILE ILE A . n 
A 1 73  LYS 73  73  73  LYS LYS A . n 
A 1 74  GLY 74  74  74  GLY GLY A . n 
A 1 75  SER 75  75  75  SER SER A . n 
A 1 76  PRO 76  76  76  PRO PRO A . n 
A 1 77  TYR 77  77  77  TYR TYR A . n 
A 1 78  TYR 78  78  78  TYR TYR A . n 
A 1 79  GLU 79  79  79  GLU GLU A . n 
A 1 80  ILE 80  80  80  ILE ILE A . n 
A 1 81  ALA 81  81  81  ALA ALA A . n 
A 1 82  MET 82  82  82  MET MET A . n 
A 1 83  ARG 83  83  83  ARG ARG A . n 
A 1 84  GLN 84  84  84  GLN GLN A . n 
A 1 85  VAL 85  85  85  VAL VAL A . n 
A 1 86  PRO 86  86  86  PRO PRO A . n 
A 1 87  HIS 87  87  87  HIS HIS A . n 
A 1 88  ARG 88  88  88  ARG ARG A . n 
A 1 89  PHE 89  89  89  PHE PHE A . n 
A 1 90  HIS 90  90  90  HIS HIS A . n 
A 1 91  ARG 91  91  91  ARG ARG A . n 
A 1 92  LEU 92  92  92  LEU LEU A . n 
A 1 93  PHE 93  93  93  PHE PHE A . n 
A 1 94  PRO 94  94  94  PRO PRO A . n 
A 1 95  PRO 95  95  95  PRO PRO A . n 
A 1 96  THR 96  96  96  THR THR A . n 
A 1 97  THR 97  97  97  THR THR A . n 
A 1 98  VAL 98  98  98  VAL VAL A . n 
A 1 99  TRP 99  99  99  TRP TRP A . n 
A 1 100 GLY 100 100 100 GLY GLY A . n 
A 1 101 TYR 101 101 101 TYR TYR A . n 
A 1 102 ASP 102 102 102 ASP ASP A . n 
A 1 103 GLY 103 103 103 GLY GLY A . n 
A 1 104 MET 104 104 104 MET MET A . n 
A 1 105 LEU 105 105 105 LEU LEU A . n 
A 1 106 PRO 106 106 106 PRO PRO A . n 
A 1 107 GLY 107 107 107 GLY GLY A . n 
A 1 108 PRO 108 108 108 PRO PRO A . n 
A 1 109 THR 109 109 109 THR THR A . n 
A 1 110 ILE 110 110 110 ILE ILE A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 VAL 112 112 112 VAL VAL A . n 
A 1 113 GLN 113 113 113 GLN GLN A . n 
A 1 114 LYS 114 114 114 LYS LYS A . n 
A 1 115 ASP 115 115 115 ASP ASP A . n 
A 1 116 GLU 116 116 116 GLU GLU A . n 
A 1 117 LYS 117 117 117 LYS LYS A . n 
A 1 118 ILE 118 118 118 ILE ILE A . n 
A 1 119 TYR 119 119 119 TYR TYR A . n 
A 1 120 VAL 120 120 120 VAL VAL A . n 
A 1 121 ARG 121 121 121 ARG ARG A . n 
A 1 122 TRP 122 122 122 TRP TRP A . n 
A 1 123 LYS 123 123 123 LYS LYS A . n 
A 1 124 ASN 124 124 124 ASN ASN A . n 
A 1 125 LYS 125 125 125 LYS LYS A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 PRO 127 127 127 PRO PRO A . n 
A 1 128 GLU 128 128 128 GLU GLU A . n 
A 1 129 LYS 129 129 129 LYS LYS A . n 
A 1 130 HIS 130 130 130 HIS HIS A . n 
A 1 131 LEU 131 131 131 LEU LEU A . n 
A 1 132 LEU 132 132 132 LEU LEU A . n 
A 1 133 PRO 133 133 133 PRO PRO A . n 
A 1 134 ILE 134 134 134 ILE ILE A . n 
A 1 135 ASP 135 135 135 ASP ASP A . n 
A 1 136 ARG 136 136 136 ARG ARG A . n 
A 1 137 THR 137 137 137 THR THR A . n 
A 1 138 LEU 138 138 138 LEU LEU A . n 
A 1 139 HIS 139 139 139 HIS HIS A . n 
A 1 140 GLU 140 140 140 GLU GLU A . n 
A 1 141 THR 141 141 141 THR THR A . n 
A 1 142 ALA 142 142 142 ALA ALA A . n 
A 1 143 GLY 143 143 143 GLY GLY A . n 
A 1 144 PRO 144 144 144 PRO PRO A . n 
A 1 145 PRO 145 145 145 PRO PRO A . n 
A 1 146 ASP 146 146 146 ASP ASP A . n 
A 1 147 VAL 147 147 147 VAL VAL A . n 
A 1 148 ARG 148 148 148 ARG ARG A . n 
A 1 149 THR 149 149 149 THR THR A . n 
A 1 150 VAL 150 150 150 VAL VAL A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 HIS 152 152 152 HIS HIS A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 HIS 154 154 154 HIS HIS A . n 
A 1 155 GLY 155 155 155 GLY GLY A . n 
A 1 156 ALA 156 156 156 ALA ALA A . n 
A 1 157 ASN 157 157 157 ASN ASN A . n 
A 1 158 VAL 158 158 158 VAL VAL A . n 
A 1 159 ALA 159 159 159 ALA ALA A . n 
A 1 160 TRP 160 160 160 TRP TRP A . n 
A 1 161 ASP 161 161 161 ASP ASP A . n 
A 1 162 SER 162 162 162 SER SER A . n 
A 1 163 ASP 163 163 163 ASP ASP A . n 
A 1 164 GLY 164 164 164 GLY GLY A . n 
A 1 165 HIS 165 165 165 HIS HIS A . n 
A 1 166 PRO 166 166 166 PRO PRO A . n 
A 1 167 GLU 167 167 167 GLU GLU A . n 
A 1 168 ALA 168 168 168 ALA ALA A . n 
A 1 169 TRP 169 169 169 TRP TRP A . n 
A 1 170 PHE 170 170 170 PHE PHE A . n 
A 1 171 SER 171 171 171 SER SER A . n 
A 1 172 ARG 172 172 172 ARG ARG A . n 
A 1 173 ASP 173 173 173 ASP ASP A . n 
A 1 174 PHE 174 174 174 PHE PHE A . n 
A 1 175 ALA 175 175 175 ALA ALA A . n 
A 1 176 LYS 176 176 176 LYS LYS A . n 
A 1 177 THR 177 177 177 THR THR A . n 
A 1 178 GLY 178 178 178 GLY GLY A . n 
A 1 179 ALA 179 179 179 ALA ALA A . n 
A 1 180 THR 180 180 180 THR THR A . n 
A 1 181 PHE 181 181 181 PHE PHE A . n 
A 1 182 ARG 182 182 182 ARG ARG A . n 
A 1 183 ARG 183 183 183 ARG ARG A . n 
A 1 184 LYS 184 184 184 LYS LYS A . n 
A 1 185 VAL 185 185 185 VAL VAL A . n 
A 1 186 TYR 186 186 186 TYR TYR A . n 
A 1 187 GLU 187 187 187 GLU GLU A . n 
A 1 188 TYR 188 188 188 TYR TYR A . n 
A 1 189 THR 189 189 189 THR THR A . n 
A 1 190 ASN 190 190 190 ASN ASN A . n 
A 1 191 LYS 191 191 191 LYS LYS A . n 
A 1 192 GLN 192 192 192 GLN GLN A . n 
A 1 193 MET 193 193 193 MET MET A . n 
A 1 194 GLY 194 194 194 GLY GLY A . n 
A 1 195 ALA 195 195 195 ALA ALA A . n 
A 1 196 THR 196 196 196 THR THR A . n 
A 1 197 LEU 197 197 197 LEU LEU A . n 
A 1 198 TRP 198 198 198 TRP TRP A . n 
A 1 199 TYR 199 199 199 TYR TYR A . n 
A 1 200 HIS 200 200 200 HIS HIS A . n 
A 1 201 ASP 201 201 201 ASP ASP A . n 
A 1 202 HIS 202 202 202 HIS HIS A . n 
A 1 203 ALA 203 203 203 ALA ALA A . n 
A 1 204 ILE 204 204 204 ILE ILE A . n 
A 1 205 GLY 205 205 205 GLY GLY A . n 
A 1 206 ILE 206 206 206 ILE ILE A . n 
A 1 207 THR 207 207 207 THR THR A . n 
A 1 208 ARG 208 208 208 ARG ARG A . n 
A 1 209 LEU 209 209 209 LEU LEU A . n 
A 1 210 ASN 210 210 210 ASN ASN A . n 
A 1 211 VAL 211 211 211 VAL VAL A . n 
A 1 212 TYR 212 212 212 TYR TYR A . n 
A 1 213 SER 213 213 213 SER SER A . n 
A 1 214 GLY 214 214 214 GLY GLY A . n 
A 1 215 LEU 215 215 215 LEU LEU A . n 
A 1 216 SER 216 216 216 SER SER A . n 
A 1 217 GLY 217 217 217 GLY GLY A . n 
A 1 218 PHE 218 218 218 PHE PHE A . n 
A 1 219 TYR 219 219 219 TYR TYR A . n 
A 1 220 LEU 220 220 220 LEU LEU A . n 
A 1 221 ILE 221 221 221 ILE ILE A . n 
A 1 222 GLU 222 222 222 GLU GLU A . n 
A 1 223 ASP 223 223 223 ASP ASP A . n 
A 1 224 PRO 224 224 224 PRO PRO A . n 
A 1 225 VAL 225 225 225 VAL VAL A . n 
A 1 226 GLU 226 226 226 GLU GLU A . n 
A 1 227 LYS 227 227 227 LYS LYS A . n 
A 1 228 HIS 228 228 228 HIS HIS A . n 
A 1 229 LEU 229 229 229 LEU LEU A . n 
A 1 230 LYS 230 230 230 LYS LYS A . n 
A 1 231 LEU 231 231 231 LEU LEU A . n 
A 1 232 PRO 232 232 232 PRO PRO A . n 
A 1 233 LYS 233 233 233 LYS LYS A . n 
A 1 234 ASP 234 234 234 ASP ASP A . n 
A 1 235 GLY 235 235 235 GLY GLY A . n 
A 1 236 TYR 236 236 236 TYR TYR A . n 
A 1 237 ASP 237 237 237 ASP ASP A . n 
A 1 238 ILE 238 238 238 ILE ILE A . n 
A 1 239 PRO 239 239 239 PRO PRO A . n 
A 1 240 LEU 240 240 240 LEU LEU A . n 
A 1 241 MET 241 241 241 MET MET A . n 
A 1 242 ILE 242 242 242 ILE ILE A . n 
A 1 243 GLN 243 243 243 GLN GLN A . n 
A 1 244 ASP 244 244 244 ASP ASP A . n 
A 1 245 ARG 245 245 245 ARG ARG A . n 
A 1 246 SER 246 246 246 SER SER A . n 
A 1 247 PHE 247 247 247 PHE PHE A . n 
A 1 248 ARG 248 248 248 ARG ARG A . n 
A 1 249 SER 249 249 249 SER SER A . n 
A 1 250 ASP 250 250 250 ASP ASP A . n 
A 1 251 GLY 251 251 251 GLY GLY A . n 
A 1 252 SER 252 252 252 SER SER A . n 
A 1 253 LEU 253 253 253 LEU LEU A . n 
A 1 254 SER 254 254 254 SER SER A . n 
A 1 255 TYR 255 255 255 TYR TYR A . n 
A 1 256 PRO 256 256 256 PRO PRO A . n 
A 1 257 GLU 257 257 257 GLU GLU A . n 
A 1 258 ASN 258 258 258 ASN ASN A . n 
A 1 259 THR 259 259 259 THR THR A . n 
A 1 260 ASN 260 260 260 ASN ASN A . n 
A 1 261 PRO 261 261 261 PRO PRO A . n 
A 1 262 PRO 262 262 262 PRO PRO A . n 
A 1 263 ALA 263 263 263 ALA ALA A . n 
A 1 264 PRO 264 264 264 PRO PRO A . n 
A 1 265 VAL 265 265 265 VAL VAL A . n 
A 1 266 ASN 266 266 266 ASN ASN A . n 
A 1 267 PRO 267 267 267 PRO PRO A . n 
A 1 268 SER 268 268 268 SER SER A . n 
A 1 269 VAL 269 269 269 VAL VAL A . n 
A 1 270 GLN 270 270 270 GLN GLN A . n 
A 1 271 PRO 271 271 271 PRO PRO A . n 
A 1 272 PHE 272 272 272 PHE PHE A . n 
A 1 273 PHE 273 273 273 PHE PHE A . n 
A 1 274 ILE 274 274 274 ILE ILE A . n 
A 1 275 GLY 275 275 275 GLY GLY A . n 
A 1 276 ASN 276 276 276 ASN ASN A . n 
A 1 277 THR 277 277 277 THR THR A . n 
A 1 278 ILE 278 278 278 ILE ILE A . n 
A 1 279 ALA 279 279 279 ALA ALA A . n 
A 1 280 VAL 280 280 280 VAL VAL A . n 
A 1 281 ASN 281 281 281 ASN ASN A . n 
A 1 282 GLY 282 282 282 GLY GLY A . n 
A 1 283 LYS 283 283 283 LYS LYS A . n 
A 1 284 ILE 284 284 284 ILE ILE A . n 
A 1 285 TRP 285 285 285 TRP TRP A . n 
A 1 286 PRO 286 286 286 PRO PRO A . n 
A 1 287 LYS 287 287 287 LYS LYS A . n 
A 1 288 LEU 288 288 288 LEU LEU A . n 
A 1 289 THR 289 289 289 THR THR A . n 
A 1 290 VAL 290 290 290 VAL VAL A . n 
A 1 291 GLU 291 291 291 GLU GLU A . n 
A 1 292 PRO 292 292 292 PRO PRO A . n 
A 1 293 ARG 293 293 293 ARG ARG A . n 
A 1 294 LYS 294 294 294 LYS LYS A . n 
A 1 295 TYR 295 295 295 TYR TYR A . n 
A 1 296 ARG 296 296 296 ARG ARG A . n 
A 1 297 PHE 297 297 297 PHE PHE A . n 
A 1 298 ARG 298 298 298 ARG ARG A . n 
A 1 299 ILE 299 299 299 ILE ILE A . n 
A 1 300 LEU 300 300 300 LEU LEU A . n 
A 1 301 ASN 301 301 301 ASN ASN A . n 
A 1 302 ALA 302 302 302 ALA ALA A . n 
A 1 303 SER 303 303 303 SER SER A . n 
A 1 304 ASN 304 304 304 ASN ASN A . n 
A 1 305 THR 305 305 305 THR THR A . n 
A 1 306 ASN 306 306 306 ASN ASN A . n 
A 1 307 ALA 307 307 307 ALA ALA A . n 
A 1 308 TYR 308 308 308 TYR TYR A . n 
A 1 309 THR 309 309 309 THR THR A . n 
A 1 310 LEU 310 310 310 LEU LEU A . n 
A 1 311 ARG 311 311 311 ARG ARG A . n 
A 1 312 LEU 312 312 312 LEU LEU A . n 
A 1 313 GLY 313 313 313 GLY GLY A . n 
A 1 314 ASP 314 314 314 ASP ASP A . n 
A 1 315 GLY 315 315 315 GLY GLY A . n 
A 1 316 ARG 316 316 316 ARG ARG A . n 
A 1 317 LYS 317 317 317 LYS LYS A . n 
A 1 318 PHE 318 318 318 PHE PHE A . n 
A 1 319 TYR 319 319 319 TYR TYR A . n 
A 1 320 GLN 320 320 320 GLN GLN A . n 
A 1 321 ILE 321 321 321 ILE ILE A . n 
A 1 322 SER 322 322 322 SER SER A . n 
A 1 323 THR 323 323 323 THR THR A . n 
A 1 324 ASP 324 324 324 ASP ASP A . n 
A 1 325 GLY 325 325 325 GLY GLY A . n 
A 1 326 GLY 326 326 326 GLY GLY A . n 
A 1 327 LEU 327 327 327 LEU LEU A . n 
A 1 328 LEU 328 328 328 LEU LEU A . n 
A 1 329 THR 329 329 329 THR THR A . n 
A 1 330 GLU 330 330 330 GLU GLU A . n 
A 1 331 PRO 331 331 331 PRO PRO A . n 
A 1 332 VAL 332 332 332 VAL VAL A . n 
A 1 333 GLU 333 333 333 GLU GLU A . n 
A 1 334 LEU 334 334 334 LEU LEU A . n 
A 1 335 THR 335 335 335 THR THR A . n 
A 1 336 THR 336 336 336 THR THR A . n 
A 1 337 LEU 337 337 337 LEU LEU A . n 
A 1 338 PRO 338 338 338 PRO PRO A . n 
A 1 339 LEU 339 339 339 LEU LEU A . n 
A 1 340 GLU 340 340 340 GLU GLU A . n 
A 1 341 PRO 341 341 341 PRO PRO A . n 
A 1 342 ALA 342 342 342 ALA ALA A . n 
A 1 343 GLU 343 343 343 GLU GLU A . n 
A 1 344 ARG 344 344 344 ARG ARG A . n 
A 1 345 SER 345 345 345 SER SER A . n 
A 1 346 ASP 346 346 346 ASP ASP A . n 
A 1 347 VAL 347 347 347 VAL VAL A . n 
A 1 348 ILE 348 348 348 ILE ILE A . n 
A 1 349 ILE 349 349 349 ILE ILE A . n 
A 1 350 ASP 350 350 350 ASP ASP A . n 
A 1 351 PHE 351 351 351 PHE PHE A . n 
A 1 352 SER 352 352 352 SER SER A . n 
A 1 353 GLN 353 353 353 GLN GLN A . n 
A 1 354 HIS 354 354 354 HIS HIS A . n 
A 1 355 LYS 355 355 355 LYS LYS A . n 
A 1 356 GLY 356 356 356 GLY GLY A . n 
A 1 357 LYS 357 357 357 LYS LYS A . n 
A 1 358 LYS 358 358 358 LYS LYS A . n 
A 1 359 LEU 359 359 359 LEU LEU A . n 
A 1 360 ILE 360 360 360 ILE ILE A . n 
A 1 361 LEU 361 361 361 LEU LEU A . n 
A 1 362 GLN 362 362 362 GLN GLN A . n 
A 1 363 ASN 363 363 363 ASN ASN A . n 
A 1 364 THR 364 364 364 THR THR A . n 
A 1 365 ASN 365 365 365 ASN ASN A . n 
A 1 366 ALA 366 366 366 ALA ALA A . n 
A 1 367 GLU 367 367 367 GLU GLU A . n 
A 1 368 GLY 368 368 368 GLY GLY A . n 
A 1 369 ASN 369 369 369 ASN ASN A . n 
A 1 370 MET 370 370 370 MET MET A . n 
A 1 371 GLY 371 371 371 GLY GLY A . n 
A 1 372 ILE 372 372 372 ILE ILE A . n 
A 1 373 ILE 373 373 373 ILE ILE A . n 
A 1 374 MET 374 374 374 MET MET A . n 
A 1 375 ARG 375 375 375 ARG ARG A . n 
A 1 376 PHE 376 376 376 PHE PHE A . n 
A 1 377 ASP 377 377 377 ASP ASP A . n 
A 1 378 VAL 378 378 378 VAL VAL A . n 
A 1 379 LEU 379 379 379 LEU LEU A . n 
A 1 380 GLN 380 380 380 GLN GLN A . n 
A 1 381 PRO 381 381 381 PRO PRO A . n 
A 1 382 LEU 382 382 382 LEU LEU A . n 
A 1 383 ARG 383 383 383 ARG ARG A . n 
A 1 384 GLY 384 384 384 GLY GLY A . n 
A 1 385 ARG 385 385 385 ARG ARG A . n 
A 1 386 ASP 386 386 386 ASP ASP A . n 
A 1 387 THR 387 387 387 THR THR A . n 
A 1 388 SER 388 388 388 SER SER A . n 
A 1 389 GLU 389 389 389 GLU GLU A . n 
A 1 390 ILE 390 390 390 ILE ILE A . n 
A 1 391 PRO 391 391 391 PRO PRO A . n 
A 1 392 ALA 392 392 392 ALA ALA A . n 
A 1 393 LYS 393 393 393 LYS LYS A . n 
A 1 394 LEU 394 394 394 LEU LEU A . n 
A 1 395 ILE 395 395 395 ILE ILE A . n 
A 1 396 SER 396 396 396 SER SER A . n 
A 1 397 GLU 397 397 397 GLU GLU A . n 
A 1 398 GLU 398 398 398 GLU GLU A . n 
A 1 399 GLN 399 399 399 GLN GLN A . n 
A 1 400 VAL 400 400 400 VAL VAL A . n 
A 1 401 LEU 401 401 401 LEU LEU A . n 
A 1 402 TYR 402 402 402 TYR TYR A . n 
A 1 403 GLU 403 403 403 GLU GLU A . n 
A 1 404 HIS 404 404 404 HIS HIS A . n 
A 1 405 HIS 405 405 405 HIS HIS A . n 
A 1 406 ALA 406 406 406 ALA ALA A . n 
A 1 407 ASP 407 407 407 ASP ASP A . n 
A 1 408 LYS 408 408 408 LYS LYS A . n 
A 1 409 THR 409 409 409 THR THR A . n 
A 1 410 ARG 410 410 410 ARG ARG A . n 
A 1 411 LEU 411 411 411 LEU LEU A . n 
A 1 412 LEU 412 412 412 LEU LEU A . n 
A 1 413 LYS 413 413 413 LYS LYS A . n 
A 1 414 LEU 414 414 414 LEU LEU A . n 
A 1 415 ASP 415 415 415 ASP ASP A . n 
A 1 416 ALA 416 416 416 ALA ALA A . n 
A 1 417 ILE 417 417 417 ILE ILE A . n 
A 1 418 GLN 418 418 418 GLN GLN A . n 
A 1 419 ASP 419 419 419 ASP ASP A . n 
A 1 420 GLU 420 420 420 GLU GLU A . n 
A 1 421 TYR 421 421 421 TYR TYR A . n 
A 1 422 ASN 422 422 422 ASN ASN A . n 
A 1 423 ARG 423 423 423 ARG ARG A . n 
A 1 424 PRO 424 424 424 PRO PRO A . n 
A 1 425 VAL 425 425 425 VAL VAL A . n 
A 1 426 LEU 426 426 426 LEU LEU A . n 
A 1 427 LEU 427 427 427 LEU LEU A . n 
A 1 428 LEU 428 428 428 LEU LEU A . n 
A 1 429 ASP 429 429 429 ASP ASP A . n 
A 1 430 ASP 430 430 430 ASP ASP A . n 
A 1 431 ARG 431 431 431 ARG ARG A . n 
A 1 432 MET 432 432 432 MET MET A . n 
A 1 433 TRP 433 433 433 TRP TRP A . n 
A 1 434 HIS 434 434 434 HIS HIS A . n 
A 1 435 ASP 435 435 435 ASP ASP A . n 
A 1 436 PRO 436 436 436 PRO PRO A . n 
A 1 437 VAL 437 437 437 VAL VAL A . n 
A 1 438 THR 438 438 438 THR THR A . n 
A 1 439 GLU 439 439 439 GLU GLU A . n 
A 1 440 LYS 440 440 440 LYS LYS A . n 
A 1 441 PRO 441 441 441 PRO PRO A . n 
A 1 442 VAL 442 442 442 VAL VAL A . n 
A 1 443 ILE 443 443 443 ILE ILE A . n 
A 1 444 GLY 444 444 444 GLY GLY A . n 
A 1 445 ASP 445 445 445 ASP ASP A . n 
A 1 446 THR 446 446 446 THR THR A . n 
A 1 447 GLU 447 447 447 GLU GLU A . n 
A 1 448 VAL 448 448 448 VAL VAL A . n 
A 1 449 TRP 449 449 449 TRP TRP A . n 
A 1 450 LYS 450 450 450 LYS LYS A . n 
A 1 451 LEU 451 451 451 LEU LEU A . n 
A 1 452 ILE 452 452 452 ILE ILE A . n 
A 1 453 ASN 453 453 453 ASN ASN A . n 
A 1 454 VAL 454 454 454 VAL VAL A . n 
A 1 455 THR 455 455 455 THR THR A . n 
A 1 456 ASN 456 456 456 ASN ASN A . n 
A 1 457 PHE 457 457 457 PHE PHE A . n 
A 1 458 ALA 458 458 458 ALA ALA A . n 
A 1 459 HIS 459 459 459 HIS HIS A . n 
A 1 460 PRO 460 460 460 PRO PRO A . n 
A 1 461 ILE 461 461 461 ILE ILE A . n 
A 1 462 HIS 462 462 462 HIS HIS A . n 
A 1 463 ILE 463 463 463 ILE ILE A . n 
A 1 464 HIS 464 464 464 HIS HIS A . n 
A 1 465 LEU 465 465 465 LEU LEU A . n 
A 1 466 ILE 466 466 466 ILE ILE A . n 
A 1 467 GLN 467 467 467 GLN GLN A . n 
A 1 468 PHE 468 468 468 PHE PHE A . n 
A 1 469 LYS 469 469 469 LYS LYS A . n 
A 1 470 ILE 470 470 470 ILE ILE A . n 
A 1 471 LEU 471 471 471 LEU LEU A . n 
A 1 472 HIS 472 472 472 HIS HIS A . n 
A 1 473 ARG 473 473 473 ARG ARG A . n 
A 1 474 THR 474 474 474 THR THR A . n 
A 1 475 PRO 475 475 475 PRO PRO A . n 
A 1 476 PHE 476 476 476 PHE PHE A . n 
A 1 477 ASP 477 477 477 ASP ASP A . n 
A 1 478 LEU 478 478 478 LEU LEU A . n 
A 1 479 GLU 479 479 479 GLU GLU A . n 
A 1 480 ARG 480 480 480 ARG ARG A . n 
A 1 481 PHE 481 481 481 PHE PHE A . n 
A 1 482 GLN 482 482 482 GLN GLN A . n 
A 1 483 GLN 483 483 483 GLN GLN A . n 
A 1 484 ASP 484 484 484 ASP ASP A . n 
A 1 485 GLY 485 485 485 GLY GLY A . n 
A 1 486 TYR 486 486 486 TYR TYR A . n 
A 1 487 ILE 487 487 487 ILE ILE A . n 
A 1 488 ASP 488 488 488 ASP ASP A . n 
A 1 489 TYR 489 489 489 TYR TYR A . n 
A 1 490 THR 490 490 490 THR THR A . n 
A 1 491 GLY 491 491 491 GLY GLY A . n 
A 1 492 PRO 492 492 492 PRO PRO A . n 
A 1 493 PRO 493 493 493 PRO PRO A . n 
A 1 494 ILE 494 494 494 ILE ILE A . n 
A 1 495 GLU 495 495 495 GLU GLU A . n 
A 1 496 PRO 496 496 496 PRO PRO A . n 
A 1 497 ALA 497 497 497 ALA ALA A . n 
A 1 498 VAL 498 498 498 VAL VAL A . n 
A 1 499 HIS 499 499 499 HIS HIS A . n 
A 1 500 GLU 500 500 500 GLU GLU A . n 
A 1 501 ARG 501 501 501 ARG ARG A . n 
A 1 502 GLY 502 502 502 GLY GLY A . n 
A 1 503 TRP 503 503 503 TRP TRP A . n 
A 1 504 LYS 504 504 504 LYS LYS A . n 
A 1 505 ASP 505 505 505 ASP ASP A . n 
A 1 506 THR 506 506 506 THR THR A . n 
A 1 507 VAL 507 507 507 VAL VAL A . n 
A 1 508 LYS 508 508 508 LYS LYS A . n 
A 1 509 ALA 509 509 509 ALA ALA A . n 
A 1 510 GLU 510 510 510 GLU GLU A . n 
A 1 511 PRO 511 511 511 PRO PRO A . n 
A 1 512 GLY 512 512 512 GLY GLY A . n 
A 1 513 MET 513 513 513 MET MET A . n 
A 1 514 VAL 514 514 514 VAL VAL A . n 
A 1 515 THR 515 515 515 THR THR A . n 
A 1 516 SER 516 516 516 SER SER A . n 
A 1 517 VAL 517 517 517 VAL VAL A . n 
A 1 518 ILE 518 518 518 ILE ILE A . n 
A 1 519 MET 519 519 519 MET MET A . n 
A 1 520 LYS 520 520 520 LYS LYS A . n 
A 1 521 PHE 521 521 521 PHE PHE A . n 
A 1 522 THR 522 522 522 THR THR A . n 
A 1 523 GLU 523 523 523 GLU GLU A . n 
A 1 524 ASN 524 524 524 ASN ASN A . n 
A 1 525 PRO 525 525 525 PRO PRO A . n 
A 1 526 GLY 526 526 526 GLY GLY A . n 
A 1 527 GLU 527 527 527 GLU GLU A . n 
A 1 528 TYR 528 528 528 TYR TYR A . n 
A 1 529 VAL 529 529 529 VAL VAL A . n 
A 1 530 TRP 530 530 530 TRP TRP A . n 
A 1 531 HIS 531 531 531 HIS HIS A . n 
A 1 532 CYS 532 532 532 CYS CYS A . n 
A 1 533 HIS 533 533 533 HIS HIS A . n 
A 1 534 ILE 534 534 534 ILE ILE A . n 
A 1 535 LEU 535 535 535 LEU LEU A . n 
A 1 536 GLU 536 536 536 GLU GLU A . n 
A 1 537 HIS 537 537 537 HIS HIS A . n 
A 1 538 GLU 538 538 538 GLU GLU A . n 
A 1 539 ASP 539 539 539 ASP ASP A . n 
A 1 540 TYR 540 540 540 TYR TYR A . n 
A 1 541 ASP 541 541 541 ASP ASP A . n 
A 1 542 MET 542 542 542 MET MET A . n 
A 1 543 MET 543 543 543 MET MET A . n 
A 1 544 ARG 544 544 544 ARG ARG A . n 
A 1 545 PRO 545 545 545 PRO PRO A . n 
A 1 546 MET 546 546 546 MET MET A . n 
A 1 547 ARG 547 547 547 ARG ARG A . n 
A 1 548 VAL 548 548 548 VAL VAL A . n 
A 1 549 VAL 549 549 549 VAL VAL A . n 
A 1 550 GLU 550 550 550 GLU GLU A . n 
A 1 551 LYS 551 551 ?   ?   ?   A . n 
A 1 552 GLU 552 552 ?   ?   ?   A . n 
A 1 553 LYS 553 553 ?   ?   ?   A . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 CU ? ? CU ? ? 'SUBJECT OF INVESTIGATION' ? 
2 MN ? ? MN ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 MN  1   601  1   MN  MN  A . 
C 3 CU  1   602  2   CU  CU  A . 
D 3 CU  1   603  3   CU  CU  A . 
E 4 HOH 1   701  401 HOH HOH A . 
E 4 HOH 2   702  300 HOH HOH A . 
E 4 HOH 3   703  507 HOH HOH A . 
E 4 HOH 4   704  491 HOH HOH A . 
E 4 HOH 5   705  195 HOH HOH A . 
E 4 HOH 6   706  564 HOH HOH A . 
E 4 HOH 7   707  192 HOH HOH A . 
E 4 HOH 8   708  384 HOH HOH A . 
E 4 HOH 9   709  647 HOH HOH A . 
E 4 HOH 10  710  99  HOH HOH A . 
E 4 HOH 11  711  216 HOH HOH A . 
E 4 HOH 12  712  169 HOH HOH A . 
E 4 HOH 13  713  501 HOH HOH A . 
E 4 HOH 14  714  559 HOH HOH A . 
E 4 HOH 15  715  552 HOH HOH A . 
E 4 HOH 16  716  214 HOH HOH A . 
E 4 HOH 17  717  685 HOH HOH A . 
E 4 HOH 18  718  139 HOH HOH A . 
E 4 HOH 19  719  528 HOH HOH A . 
E 4 HOH 20  720  82  HOH HOH A . 
E 4 HOH 21  721  298 HOH HOH A . 
E 4 HOH 22  722  383 HOH HOH A . 
E 4 HOH 23  723  45  HOH HOH A . 
E 4 HOH 24  724  503 HOH HOH A . 
E 4 HOH 25  725  281 HOH HOH A . 
E 4 HOH 26  726  49  HOH HOH A . 
E 4 HOH 27  727  242 HOH HOH A . 
E 4 HOH 28  728  112 HOH HOH A . 
E 4 HOH 29  729  438 HOH HOH A . 
E 4 HOH 30  730  278 HOH HOH A . 
E 4 HOH 31  731  102 HOH HOH A . 
E 4 HOH 32  732  136 HOH HOH A . 
E 4 HOH 33  733  556 HOH HOH A . 
E 4 HOH 34  734  83  HOH HOH A . 
E 4 HOH 35  735  154 HOH HOH A . 
E 4 HOH 36  736  441 HOH HOH A . 
E 4 HOH 37  737  176 HOH HOH A . 
E 4 HOH 38  738  598 HOH HOH A . 
E 4 HOH 39  739  345 HOH HOH A . 
E 4 HOH 40  740  506 HOH HOH A . 
E 4 HOH 41  741  199 HOH HOH A . 
E 4 HOH 42  742  280 HOH HOH A . 
E 4 HOH 43  743  53  HOH HOH A . 
E 4 HOH 44  744  497 HOH HOH A . 
E 4 HOH 45  745  106 HOH HOH A . 
E 4 HOH 46  746  338 HOH HOH A . 
E 4 HOH 47  747  15  HOH HOH A . 
E 4 HOH 48  748  59  HOH HOH A . 
E 4 HOH 49  749  577 HOH HOH A . 
E 4 HOH 50  750  527 HOH HOH A . 
E 4 HOH 51  751  337 HOH HOH A . 
E 4 HOH 52  752  170 HOH HOH A . 
E 4 HOH 53  753  271 HOH HOH A . 
E 4 HOH 54  754  301 HOH HOH A . 
E 4 HOH 55  755  659 HOH HOH A . 
E 4 HOH 56  756  582 HOH HOH A . 
E 4 HOH 57  757  109 HOH HOH A . 
E 4 HOH 58  758  4   HOH HOH A . 
E 4 HOH 59  759  194 HOH HOH A . 
E 4 HOH 60  760  251 HOH HOH A . 
E 4 HOH 61  761  516 HOH HOH A . 
E 4 HOH 62  762  238 HOH HOH A . 
E 4 HOH 63  763  10  HOH HOH A . 
E 4 HOH 64  764  44  HOH HOH A . 
E 4 HOH 65  765  539 HOH HOH A . 
E 4 HOH 66  766  74  HOH HOH A . 
E 4 HOH 67  767  207 HOH HOH A . 
E 4 HOH 68  768  486 HOH HOH A . 
E 4 HOH 69  769  111 HOH HOH A . 
E 4 HOH 70  770  378 HOH HOH A . 
E 4 HOH 71  771  93  HOH HOH A . 
E 4 HOH 72  772  325 HOH HOH A . 
E 4 HOH 73  773  681 HOH HOH A . 
E 4 HOH 74  774  342 HOH HOH A . 
E 4 HOH 75  775  596 HOH HOH A . 
E 4 HOH 76  776  295 HOH HOH A . 
E 4 HOH 77  777  28  HOH HOH A . 
E 4 HOH 78  778  91  HOH HOH A . 
E 4 HOH 79  779  541 HOH HOH A . 
E 4 HOH 80  780  151 HOH HOH A . 
E 4 HOH 81  781  268 HOH HOH A . 
E 4 HOH 82  782  68  HOH HOH A . 
E 4 HOH 83  783  132 HOH HOH A . 
E 4 HOH 84  784  118 HOH HOH A . 
E 4 HOH 85  785  166 HOH HOH A . 
E 4 HOH 86  786  646 HOH HOH A . 
E 4 HOH 87  787  324 HOH HOH A . 
E 4 HOH 88  788  351 HOH HOH A . 
E 4 HOH 89  789  518 HOH HOH A . 
E 4 HOH 90  790  150 HOH HOH A . 
E 4 HOH 91  791  114 HOH HOH A . 
E 4 HOH 92  792  86  HOH HOH A . 
E 4 HOH 93  793  165 HOH HOH A . 
E 4 HOH 94  794  394 HOH HOH A . 
E 4 HOH 95  795  185 HOH HOH A . 
E 4 HOH 96  796  573 HOH HOH A . 
E 4 HOH 97  797  14  HOH HOH A . 
E 4 HOH 98  798  205 HOH HOH A . 
E 4 HOH 99  799  603 HOH HOH A . 
E 4 HOH 100 800  377 HOH HOH A . 
E 4 HOH 101 801  160 HOH HOH A . 
E 4 HOH 102 802  145 HOH HOH A . 
E 4 HOH 103 803  443 HOH HOH A . 
E 4 HOH 104 804  580 HOH HOH A . 
E 4 HOH 105 805  103 HOH HOH A . 
E 4 HOH 106 806  89  HOH HOH A . 
E 4 HOH 107 807  119 HOH HOH A . 
E 4 HOH 108 808  444 HOH HOH A . 
E 4 HOH 109 809  21  HOH HOH A . 
E 4 HOH 110 810  480 HOH HOH A . 
E 4 HOH 111 811  13  HOH HOH A . 
E 4 HOH 112 812  34  HOH HOH A . 
E 4 HOH 113 813  213 HOH HOH A . 
E 4 HOH 114 814  412 HOH HOH A . 
E 4 HOH 115 815  181 HOH HOH A . 
E 4 HOH 116 816  27  HOH HOH A . 
E 4 HOH 117 817  537 HOH HOH A . 
E 4 HOH 118 818  312 HOH HOH A . 
E 4 HOH 119 819  672 HOH HOH A . 
E 4 HOH 120 820  285 HOH HOH A . 
E 4 HOH 121 821  584 HOH HOH A . 
E 4 HOH 122 822  526 HOH HOH A . 
E 4 HOH 123 823  51  HOH HOH A . 
E 4 HOH 124 824  147 HOH HOH A . 
E 4 HOH 125 825  197 HOH HOH A . 
E 4 HOH 126 826  434 HOH HOH A . 
E 4 HOH 127 827  202 HOH HOH A . 
E 4 HOH 128 828  71  HOH HOH A . 
E 4 HOH 129 829  267 HOH HOH A . 
E 4 HOH 130 830  5   HOH HOH A . 
E 4 HOH 131 831  61  HOH HOH A . 
E 4 HOH 132 832  11  HOH HOH A . 
E 4 HOH 133 833  78  HOH HOH A . 
E 4 HOH 134 834  233 HOH HOH A . 
E 4 HOH 135 835  130 HOH HOH A . 
E 4 HOH 136 836  385 HOH HOH A . 
E 4 HOH 137 837  167 HOH HOH A . 
E 4 HOH 138 838  142 HOH HOH A . 
E 4 HOH 139 839  46  HOH HOH A . 
E 4 HOH 140 840  24  HOH HOH A . 
E 4 HOH 141 841  140 HOH HOH A . 
E 4 HOH 142 842  604 HOH HOH A . 
E 4 HOH 143 843  272 HOH HOH A . 
E 4 HOH 144 844  357 HOH HOH A . 
E 4 HOH 145 845  134 HOH HOH A . 
E 4 HOH 146 846  35  HOH HOH A . 
E 4 HOH 147 847  261 HOH HOH A . 
E 4 HOH 148 848  457 HOH HOH A . 
E 4 HOH 149 849  155 HOH HOH A . 
E 4 HOH 150 850  56  HOH HOH A . 
E 4 HOH 151 851  264 HOH HOH A . 
E 4 HOH 152 852  437 HOH HOH A . 
E 4 HOH 153 853  307 HOH HOH A . 
E 4 HOH 154 854  125 HOH HOH A . 
E 4 HOH 155 855  499 HOH HOH A . 
E 4 HOH 156 856  413 HOH HOH A . 
E 4 HOH 157 857  390 HOH HOH A . 
E 4 HOH 158 858  42  HOH HOH A . 
E 4 HOH 159 859  535 HOH HOH A . 
E 4 HOH 160 860  211 HOH HOH A . 
E 4 HOH 161 861  366 HOH HOH A . 
E 4 HOH 162 862  23  HOH HOH A . 
E 4 HOH 163 863  463 HOH HOH A . 
E 4 HOH 164 864  210 HOH HOH A . 
E 4 HOH 165 865  305 HOH HOH A . 
E 4 HOH 166 866  382 HOH HOH A . 
E 4 HOH 167 867  500 HOH HOH A . 
E 4 HOH 168 868  249 HOH HOH A . 
E 4 HOH 169 869  1   HOH HOH A . 
E 4 HOH 170 870  90  HOH HOH A . 
E 4 HOH 171 871  313 HOH HOH A . 
E 4 HOH 172 872  29  HOH HOH A . 
E 4 HOH 173 873  327 HOH HOH A . 
E 4 HOH 174 874  182 HOH HOH A . 
E 4 HOH 175 875  229 HOH HOH A . 
E 4 HOH 176 876  141 HOH HOH A . 
E 4 HOH 177 877  427 HOH HOH A . 
E 4 HOH 178 878  178 HOH HOH A . 
E 4 HOH 179 879  253 HOH HOH A . 
E 4 HOH 180 880  293 HOH HOH A . 
E 4 HOH 181 881  2   HOH HOH A . 
E 4 HOH 182 882  143 HOH HOH A . 
E 4 HOH 183 883  209 HOH HOH A . 
E 4 HOH 184 884  326 HOH HOH A . 
E 4 HOH 185 885  347 HOH HOH A . 
E 4 HOH 186 886  200 HOH HOH A . 
E 4 HOH 187 887  429 HOH HOH A . 
E 4 HOH 188 888  236 HOH HOH A . 
E 4 HOH 189 889  404 HOH HOH A . 
E 4 HOH 190 890  224 HOH HOH A . 
E 4 HOH 191 891  98  HOH HOH A . 
E 4 HOH 192 892  58  HOH HOH A . 
E 4 HOH 193 893  513 HOH HOH A . 
E 4 HOH 194 894  333 HOH HOH A . 
E 4 HOH 195 895  75  HOH HOH A . 
E 4 HOH 196 896  310 HOH HOH A . 
E 4 HOH 197 897  57  HOH HOH A . 
E 4 HOH 198 898  652 HOH HOH A . 
E 4 HOH 199 899  583 HOH HOH A . 
E 4 HOH 200 900  171 HOH HOH A . 
E 4 HOH 201 901  3   HOH HOH A . 
E 4 HOH 202 902  536 HOH HOH A . 
E 4 HOH 203 903  288 HOH HOH A . 
E 4 HOH 204 904  12  HOH HOH A . 
E 4 HOH 205 905  257 HOH HOH A . 
E 4 HOH 206 906  16  HOH HOH A . 
E 4 HOH 207 907  452 HOH HOH A . 
E 4 HOH 208 908  122 HOH HOH A . 
E 4 HOH 209 909  230 HOH HOH A . 
E 4 HOH 210 910  62  HOH HOH A . 
E 4 HOH 211 911  36  HOH HOH A . 
E 4 HOH 212 912  157 HOH HOH A . 
E 4 HOH 213 913  572 HOH HOH A . 
E 4 HOH 214 914  330 HOH HOH A . 
E 4 HOH 215 915  124 HOH HOH A . 
E 4 HOH 216 916  485 HOH HOH A . 
E 4 HOH 217 917  470 HOH HOH A . 
E 4 HOH 218 918  31  HOH HOH A . 
E 4 HOH 219 919  595 HOH HOH A . 
E 4 HOH 220 920  218 HOH HOH A . 
E 4 HOH 221 921  446 HOH HOH A . 
E 4 HOH 222 922  30  HOH HOH A . 
E 4 HOH 223 923  478 HOH HOH A . 
E 4 HOH 224 924  159 HOH HOH A . 
E 4 HOH 225 925  303 HOH HOH A . 
E 4 HOH 226 926  248 HOH HOH A . 
E 4 HOH 227 927  138 HOH HOH A . 
E 4 HOH 228 928  217 HOH HOH A . 
E 4 HOH 229 929  239 HOH HOH A . 
E 4 HOH 230 930  8   HOH HOH A . 
E 4 HOH 231 931  402 HOH HOH A . 
E 4 HOH 232 932  22  HOH HOH A . 
E 4 HOH 233 933  364 HOH HOH A . 
E 4 HOH 234 934  95  HOH HOH A . 
E 4 HOH 235 935  311 HOH HOH A . 
E 4 HOH 236 936  173 HOH HOH A . 
E 4 HOH 237 937  348 HOH HOH A . 
E 4 HOH 238 938  153 HOH HOH A . 
E 4 HOH 239 939  263 HOH HOH A . 
E 4 HOH 240 940  270 HOH HOH A . 
E 4 HOH 241 941  66  HOH HOH A . 
E 4 HOH 242 942  489 HOH HOH A . 
E 4 HOH 243 943  522 HOH HOH A . 
E 4 HOH 244 944  110 HOH HOH A . 
E 4 HOH 245 945  276 HOH HOH A . 
E 4 HOH 246 946  532 HOH HOH A . 
E 4 HOH 247 947  32  HOH HOH A . 
E 4 HOH 248 948  308 HOH HOH A . 
E 4 HOH 249 949  196 HOH HOH A . 
E 4 HOH 250 950  592 HOH HOH A . 
E 4 HOH 251 951  55  HOH HOH A . 
E 4 HOH 252 952  97  HOH HOH A . 
E 4 HOH 253 953  315 HOH HOH A . 
E 4 HOH 254 954  392 HOH HOH A . 
E 4 HOH 255 955  223 HOH HOH A . 
E 4 HOH 256 956  302 HOH HOH A . 
E 4 HOH 257 957  204 HOH HOH A . 
E 4 HOH 258 958  94  HOH HOH A . 
E 4 HOH 259 959  39  HOH HOH A . 
E 4 HOH 260 960  624 HOH HOH A . 
E 4 HOH 261 961  175 HOH HOH A . 
E 4 HOH 262 962  6   HOH HOH A . 
E 4 HOH 263 963  37  HOH HOH A . 
E 4 HOH 264 964  353 HOH HOH A . 
E 4 HOH 265 965  314 HOH HOH A . 
E 4 HOH 266 966  70  HOH HOH A . 
E 4 HOH 267 967  362 HOH HOH A . 
E 4 HOH 268 968  17  HOH HOH A . 
E 4 HOH 269 969  228 HOH HOH A . 
E 4 HOH 270 970  65  HOH HOH A . 
E 4 HOH 271 971  269 HOH HOH A . 
E 4 HOH 272 972  25  HOH HOH A . 
E 4 HOH 273 973  289 HOH HOH A . 
E 4 HOH 274 974  363 HOH HOH A . 
E 4 HOH 275 975  54  HOH HOH A . 
E 4 HOH 276 976  359 HOH HOH A . 
E 4 HOH 277 977  631 HOH HOH A . 
E 4 HOH 278 978  436 HOH HOH A . 
E 4 HOH 279 979  410 HOH HOH A . 
E 4 HOH 280 980  162 HOH HOH A . 
E 4 HOH 281 981  189 HOH HOH A . 
E 4 HOH 282 982  108 HOH HOH A . 
E 4 HOH 283 983  456 HOH HOH A . 
E 4 HOH 284 984  534 HOH HOH A . 
E 4 HOH 285 985  104 HOH HOH A . 
E 4 HOH 286 986  431 HOH HOH A . 
E 4 HOH 287 987  133 HOH HOH A . 
E 4 HOH 288 988  322 HOH HOH A . 
E 4 HOH 289 989  237 HOH HOH A . 
E 4 HOH 290 990  254 HOH HOH A . 
E 4 HOH 291 991  483 HOH HOH A . 
E 4 HOH 292 992  416 HOH HOH A . 
E 4 HOH 293 993  164 HOH HOH A . 
E 4 HOH 294 994  123 HOH HOH A . 
E 4 HOH 295 995  84  HOH HOH A . 
E 4 HOH 296 996  422 HOH HOH A . 
E 4 HOH 297 997  137 HOH HOH A . 
E 4 HOH 298 998  543 HOH HOH A . 
E 4 HOH 299 999  81  HOH HOH A . 
E 4 HOH 300 1000 304 HOH HOH A . 
E 4 HOH 301 1001 306 HOH HOH A . 
E 4 HOH 302 1002 73  HOH HOH A . 
E 4 HOH 303 1003 52  HOH HOH A . 
E 4 HOH 304 1004 188 HOH HOH A . 
E 4 HOH 305 1005 266 HOH HOH A . 
E 4 HOH 306 1006 355 HOH HOH A . 
E 4 HOH 307 1007 234 HOH HOH A . 
E 4 HOH 308 1008 40  HOH HOH A . 
E 4 HOH 309 1009 250 HOH HOH A . 
E 4 HOH 310 1010 85  HOH HOH A . 
E 4 HOH 311 1011 259 HOH HOH A . 
E 4 HOH 312 1012 546 HOH HOH A . 
E 4 HOH 313 1013 661 HOH HOH A . 
E 4 HOH 314 1014 19  HOH HOH A . 
E 4 HOH 315 1015 231 HOH HOH A . 
E 4 HOH 316 1016 116 HOH HOH A . 
E 4 HOH 317 1017 512 HOH HOH A . 
E 4 HOH 318 1018 201 HOH HOH A . 
E 4 HOH 319 1019 50  HOH HOH A . 
E 4 HOH 320 1020 340 HOH HOH A . 
E 4 HOH 321 1021 226 HOH HOH A . 
E 4 HOH 322 1022 220 HOH HOH A . 
E 4 HOH 323 1023 126 HOH HOH A . 
E 4 HOH 324 1024 403 HOH HOH A . 
E 4 HOH 325 1025 393 HOH HOH A . 
E 4 HOH 326 1026 146 HOH HOH A . 
E 4 HOH 327 1027 265 HOH HOH A . 
E 4 HOH 328 1028 373 HOH HOH A . 
E 4 HOH 329 1029 287 HOH HOH A . 
E 4 HOH 330 1030 440 HOH HOH A . 
E 4 HOH 331 1031 367 HOH HOH A . 
E 4 HOH 332 1032 350 HOH HOH A . 
E 4 HOH 333 1033 77  HOH HOH A . 
E 4 HOH 334 1034 451 HOH HOH A . 
E 4 HOH 335 1035 129 HOH HOH A . 
E 4 HOH 336 1036 232 HOH HOH A . 
E 4 HOH 337 1037 64  HOH HOH A . 
E 4 HOH 338 1038 120 HOH HOH A . 
E 4 HOH 339 1039 417 HOH HOH A . 
E 4 HOH 340 1040 48  HOH HOH A . 
E 4 HOH 341 1041 184 HOH HOH A . 
E 4 HOH 342 1042 686 HOH HOH A . 
E 4 HOH 343 1043 245 HOH HOH A . 
E 4 HOH 344 1044 563 HOH HOH A . 
E 4 HOH 345 1045 435 HOH HOH A . 
E 4 HOH 346 1046 177 HOH HOH A . 
E 4 HOH 347 1047 286 HOH HOH A . 
E 4 HOH 348 1048 33  HOH HOH A . 
E 4 HOH 349 1049 179 HOH HOH A . 
E 4 HOH 350 1050 107 HOH HOH A . 
E 4 HOH 351 1051 79  HOH HOH A . 
E 4 HOH 352 1052 397 HOH HOH A . 
E 4 HOH 353 1053 9   HOH HOH A . 
E 4 HOH 354 1054 215 HOH HOH A . 
E 4 HOH 355 1055 148 HOH HOH A . 
E 4 HOH 356 1056 277 HOH HOH A . 
E 4 HOH 357 1057 100 HOH HOH A . 
E 4 HOH 358 1058 328 HOH HOH A . 
E 4 HOH 359 1059 493 HOH HOH A . 
E 4 HOH 360 1060 198 HOH HOH A . 
E 4 HOH 361 1061 76  HOH HOH A . 
E 4 HOH 362 1062 648 HOH HOH A . 
E 4 HOH 363 1063 41  HOH HOH A . 
E 4 HOH 364 1064 460 HOH HOH A . 
E 4 HOH 365 1065 616 HOH HOH A . 
E 4 HOH 366 1066 161 HOH HOH A . 
E 4 HOH 367 1067 101 HOH HOH A . 
E 4 HOH 368 1068 38  HOH HOH A . 
E 4 HOH 369 1069 510 HOH HOH A . 
E 4 HOH 370 1070 591 HOH HOH A . 
E 4 HOH 371 1071 149 HOH HOH A . 
E 4 HOH 372 1072 69  HOH HOH A . 
E 4 HOH 373 1073 241 HOH HOH A . 
E 4 HOH 374 1074 396 HOH HOH A . 
E 4 HOH 375 1075 590 HOH HOH A . 
E 4 HOH 376 1076 80  HOH HOH A . 
E 4 HOH 377 1077 549 HOH HOH A . 
E 4 HOH 378 1078 96  HOH HOH A . 
E 4 HOH 379 1079 617 HOH HOH A . 
E 4 HOH 380 1080 7   HOH HOH A . 
E 4 HOH 381 1081 63  HOH HOH A . 
E 4 HOH 382 1082 190 HOH HOH A . 
E 4 HOH 383 1083 282 HOH HOH A . 
E 4 HOH 384 1084 439 HOH HOH A . 
E 4 HOH 385 1085 432 HOH HOH A . 
E 4 HOH 386 1086 316 HOH HOH A . 
E 4 HOH 387 1087 20  HOH HOH A . 
E 4 HOH 388 1088 299 HOH HOH A . 
E 4 HOH 389 1089 219 HOH HOH A . 
E 4 HOH 390 1090 504 HOH HOH A . 
E 4 HOH 391 1091 344 HOH HOH A . 
E 4 HOH 392 1092 375 HOH HOH A . 
E 4 HOH 393 1093 339 HOH HOH A . 
E 4 HOH 394 1094 335 HOH HOH A . 
E 4 HOH 395 1095 594 HOH HOH A . 
E 4 HOH 396 1096 358 HOH HOH A . 
E 4 HOH 397 1097 43  HOH HOH A . 
E 4 HOH 398 1098 235 HOH HOH A . 
E 4 HOH 399 1099 174 HOH HOH A . 
E 4 HOH 400 1100 158 HOH HOH A . 
E 4 HOH 401 1101 121 HOH HOH A . 
E 4 HOH 402 1102 606 HOH HOH A . 
E 4 HOH 403 1103 246 HOH HOH A . 
E 4 HOH 404 1104 678 HOH HOH A . 
E 4 HOH 405 1105 291 HOH HOH A . 
E 4 HOH 406 1106 332 HOH HOH A . 
E 4 HOH 407 1107 361 HOH HOH A . 
E 4 HOH 408 1108 290 HOH HOH A . 
E 4 HOH 409 1109 47  HOH HOH A . 
E 4 HOH 410 1110 465 HOH HOH A . 
E 4 HOH 411 1111 329 HOH HOH A . 
E 4 HOH 412 1112 152 HOH HOH A . 
E 4 HOH 413 1113 296 HOH HOH A . 
E 4 HOH 414 1114 131 HOH HOH A . 
E 4 HOH 415 1115 568 HOH HOH A . 
E 4 HOH 416 1116 454 HOH HOH A . 
E 4 HOH 417 1117 255 HOH HOH A . 
E 4 HOH 418 1118 360 HOH HOH A . 
E 4 HOH 419 1119 525 HOH HOH A . 
E 4 HOH 420 1120 18  HOH HOH A . 
E 4 HOH 421 1121 461 HOH HOH A . 
E 4 HOH 422 1122 368 HOH HOH A . 
E 4 HOH 423 1123 369 HOH HOH A . 
E 4 HOH 424 1124 244 HOH HOH A . 
E 4 HOH 425 1125 381 HOH HOH A . 
E 4 HOH 426 1126 632 HOH HOH A . 
E 4 HOH 427 1127 320 HOH HOH A . 
E 4 HOH 428 1128 533 HOH HOH A . 
E 4 HOH 429 1129 448 HOH HOH A . 
E 4 HOH 430 1130 309 HOH HOH A . 
E 4 HOH 431 1131 331 HOH HOH A . 
E 4 HOH 432 1132 72  HOH HOH A . 
E 4 HOH 433 1133 458 HOH HOH A . 
E 4 HOH 434 1134 421 HOH HOH A . 
E 4 HOH 435 1135 252 HOH HOH A . 
E 4 HOH 436 1136 317 HOH HOH A . 
E 4 HOH 437 1137 212 HOH HOH A . 
E 4 HOH 438 1138 346 HOH HOH A . 
E 4 HOH 439 1139 496 HOH HOH A . 
E 4 HOH 440 1140 668 HOH HOH A . 
E 4 HOH 441 1141 227 HOH HOH A . 
E 4 HOH 442 1142 423 HOH HOH A . 
E 4 HOH 443 1143 602 HOH HOH A . 
E 4 HOH 444 1144 442 HOH HOH A . 
E 4 HOH 445 1145 186 HOH HOH A . 
E 4 HOH 446 1146 400 HOH HOH A . 
E 4 HOH 447 1147 618 HOH HOH A . 
E 4 HOH 448 1148 660 HOH HOH A . 
E 4 HOH 449 1149 545 HOH HOH A . 
E 4 HOH 450 1150 343 HOH HOH A . 
E 4 HOH 451 1151 191 HOH HOH A . 
E 4 HOH 452 1152 87  HOH HOH A . 
E 4 HOH 453 1153 508 HOH HOH A . 
E 4 HOH 454 1154 356 HOH HOH A . 
E 4 HOH 455 1155 521 HOH HOH A . 
E 4 HOH 456 1156 409 HOH HOH A . 
E 4 HOH 457 1157 597 HOH HOH A . 
E 4 HOH 458 1158 530 HOH HOH A . 
E 4 HOH 459 1159 683 HOH HOH A . 
E 4 HOH 460 1160 495 HOH HOH A . 
E 4 HOH 461 1161 540 HOH HOH A . 
E 4 HOH 462 1162 524 HOH HOH A . 
E 4 HOH 463 1163 187 HOH HOH A . 
E 4 HOH 464 1164 473 HOH HOH A . 
E 4 HOH 465 1165 260 HOH HOH A . 
E 4 HOH 466 1166 386 HOH HOH A . 
E 4 HOH 467 1167 650 HOH HOH A . 
E 4 HOH 468 1168 128 HOH HOH A . 
E 4 HOH 469 1169 538 HOH HOH A . 
E 4 HOH 470 1170 388 HOH HOH A . 
E 4 HOH 471 1171 505 HOH HOH A . 
E 4 HOH 472 1172 426 HOH HOH A . 
E 4 HOH 473 1173 655 HOH HOH A . 
E 4 HOH 474 1174 352 HOH HOH A . 
E 4 HOH 475 1175 679 HOH HOH A . 
E 4 HOH 476 1176 477 HOH HOH A . 
E 4 HOH 477 1177 398 HOH HOH A . 
E 4 HOH 478 1178 475 HOH HOH A . 
E 4 HOH 479 1179 60  HOH HOH A . 
E 4 HOH 480 1180 674 HOH HOH A . 
E 4 HOH 481 1181 292 HOH HOH A . 
E 4 HOH 482 1182 557 HOH HOH A . 
E 4 HOH 483 1183 336 HOH HOH A . 
E 4 HOH 484 1184 519 HOH HOH A . 
E 4 HOH 485 1185 455 HOH HOH A . 
E 4 HOH 486 1186 92  HOH HOH A . 
E 4 HOH 487 1187 476 HOH HOH A . 
E 4 HOH 488 1188 645 HOH HOH A . 
E 4 HOH 489 1189 424 HOH HOH A . 
E 4 HOH 490 1190 638 HOH HOH A . 
E 4 HOH 491 1191 425 HOH HOH A . 
E 4 HOH 492 1192 514 HOH HOH A . 
E 4 HOH 493 1193 243 HOH HOH A . 
E 4 HOH 494 1194 628 HOH HOH A . 
E 4 HOH 495 1195 649 HOH HOH A . 
E 4 HOH 496 1196 419 HOH HOH A . 
E 4 HOH 497 1197 614 HOH HOH A . 
E 4 HOH 498 1198 405 HOH HOH A . 
E 4 HOH 499 1199 408 HOH HOH A . 
E 4 HOH 500 1200 656 HOH HOH A . 
E 4 HOH 501 1201 26  HOH HOH A . 
E 4 HOH 502 1202 665 HOH HOH A . 
E 4 HOH 503 1203 406 HOH HOH A . 
E 4 HOH 504 1204 651 HOH HOH A . 
E 4 HOH 505 1205 593 HOH HOH A . 
E 4 HOH 506 1206 635 HOH HOH A . 
E 4 HOH 507 1207 621 HOH HOH A . 
E 4 HOH 508 1208 180 HOH HOH A . 
E 4 HOH 509 1209 490 HOH HOH A . 
E 4 HOH 510 1210 620 HOH HOH A . 
E 4 HOH 511 1211 666 HOH HOH A . 
E 4 HOH 512 1212 494 HOH HOH A . 
E 4 HOH 513 1213 531 HOH HOH A . 
E 4 HOH 514 1214 172 HOH HOH A . 
E 4 HOH 515 1215 354 HOH HOH A . 
E 4 HOH 516 1216 511 HOH HOH A . 
E 4 HOH 517 1217 349 HOH HOH A . 
E 4 HOH 518 1218 653 HOH HOH A . 
E 4 HOH 519 1219 636 HOH HOH A . 
E 4 HOH 520 1220 684 HOH HOH A . 
E 4 HOH 521 1221 321 HOH HOH A . 
E 4 HOH 522 1222 544 HOH HOH A . 
E 4 HOH 523 1223 474 HOH HOH A . 
E 4 HOH 524 1224 670 HOH HOH A . 
E 4 HOH 525 1225 275 HOH HOH A . 
E 4 HOH 526 1226 639 HOH HOH A . 
E 4 HOH 527 1227 612 HOH HOH A . 
E 4 HOH 528 1228 484 HOH HOH A . 
E 4 HOH 529 1229 469 HOH HOH A . 
E 4 HOH 530 1230 482 HOH HOH A . 
E 4 HOH 531 1231 555 HOH HOH A . 
E 4 HOH 532 1232 615 HOH HOH A . 
E 4 HOH 533 1233 623 HOH HOH A . 
E 4 HOH 534 1234 127 HOH HOH A . 
E 4 HOH 535 1235 221 HOH HOH A . 
E 4 HOH 536 1236 682 HOH HOH A . 
E 4 HOH 537 1237 663 HOH HOH A . 
E 4 HOH 538 1238 262 HOH HOH A . 
E 4 HOH 539 1239 193 HOH HOH A . 
E 4 HOH 540 1240 633 HOH HOH A . 
E 4 HOH 541 1241 680 HOH HOH A . 
E 4 HOH 542 1242 479 HOH HOH A . 
E 4 HOH 543 1243 529 HOH HOH A . 
E 4 HOH 544 1244 240 HOH HOH A . 
E 4 HOH 545 1245 502 HOH HOH A . 
E 4 HOH 546 1246 642 HOH HOH A . 
E 4 HOH 547 1247 387 HOH HOH A . 
E 4 HOH 548 1248 671 HOH HOH A . 
E 4 HOH 549 1249 667 HOH HOH A . 
E 4 HOH 550 1250 445 HOH HOH A . 
E 4 HOH 551 1251 515 HOH HOH A . 
E 4 HOH 552 1252 607 HOH HOH A . 
E 4 HOH 553 1253 208 HOH HOH A . 
E 4 HOH 554 1254 433 HOH HOH A . 
E 4 HOH 555 1255 464 HOH HOH A . 
E 4 HOH 556 1256 471 HOH HOH A . 
E 4 HOH 557 1257 222 HOH HOH A . 
E 4 HOH 558 1258 428 HOH HOH A . 
E 4 HOH 559 1259 414 HOH HOH A . 
E 4 HOH 560 1260 420 HOH HOH A . 
E 4 HOH 561 1261 630 HOH HOH A . 
E 4 HOH 562 1262 144 HOH HOH A . 
E 4 HOH 563 1263 447 HOH HOH A . 
E 4 HOH 564 1264 283 HOH HOH A . 
E 4 HOH 565 1265 117 HOH HOH A . 
E 4 HOH 566 1266 487 HOH HOH A . 
E 4 HOH 567 1267 318 HOH HOH A . 
E 4 HOH 568 1268 600 HOH HOH A . 
E 4 HOH 569 1269 675 HOH HOH A . 
E 4 HOH 570 1270 370 HOH HOH A . 
E 4 HOH 571 1271 67  HOH HOH A . 
E 4 HOH 572 1272 566 HOH HOH A . 
E 4 HOH 573 1273 389 HOH HOH A . 
E 4 HOH 574 1274 279 HOH HOH A . 
E 4 HOH 575 1275 579 HOH HOH A . 
E 4 HOH 576 1276 625 HOH HOH A . 
E 4 HOH 577 1277 183 HOH HOH A . 
E 4 HOH 578 1278 605 HOH HOH A . 
E 4 HOH 579 1279 688 HOH HOH A . 
E 4 HOH 580 1280 247 HOH HOH A . 
E 4 HOH 581 1281 517 HOH HOH A . 
E 4 HOH 582 1282 550 HOH HOH A . 
E 4 HOH 583 1283 168 HOH HOH A . 
E 4 HOH 584 1284 273 HOH HOH A . 
E 4 HOH 585 1285 622 HOH HOH A . 
E 4 HOH 586 1286 418 HOH HOH A . 
E 4 HOH 587 1287 589 HOH HOH A . 
E 4 HOH 588 1288 411 HOH HOH A . 
E 4 HOH 589 1289 640 HOH HOH A . 
E 4 HOH 590 1290 488 HOH HOH A . 
E 4 HOH 591 1291 297 HOH HOH A . 
E 4 HOH 592 1292 453 HOH HOH A . 
E 4 HOH 593 1293 608 HOH HOH A . 
E 4 HOH 594 1294 105 HOH HOH A . 
E 4 HOH 595 1295 407 HOH HOH A . 
E 4 HOH 596 1296 569 HOH HOH A . 
E 4 HOH 597 1297 274 HOH HOH A . 
E 4 HOH 598 1298 553 HOH HOH A . 
E 4 HOH 599 1299 203 HOH HOH A . 
E 4 HOH 600 1300 509 HOH HOH A . 
E 4 HOH 601 1301 379 HOH HOH A . 
E 4 HOH 602 1302 294 HOH HOH A . 
E 4 HOH 603 1303 467 HOH HOH A . 
E 4 HOH 604 1304 654 HOH HOH A . 
E 4 HOH 605 1305 135 HOH HOH A . 
E 4 HOH 606 1306 462 HOH HOH A . 
E 4 HOH 607 1307 115 HOH HOH A . 
E 4 HOH 608 1308 523 HOH HOH A . 
E 4 HOH 609 1309 391 HOH HOH A . 
E 4 HOH 610 1310 492 HOH HOH A . 
E 4 HOH 611 1311 468 HOH HOH A . 
E 4 HOH 612 1312 450 HOH HOH A . 
E 4 HOH 613 1313 323 HOH HOH A . 
E 4 HOH 614 1314 380 HOH HOH A . 
E 4 HOH 615 1315 258 HOH HOH A . 
E 4 HOH 616 1316 586 HOH HOH A . 
E 4 HOH 617 1317 365 HOH HOH A . 
E 4 HOH 618 1318 587 HOH HOH A . 
E 4 HOH 619 1319 163 HOH HOH A . 
E 4 HOH 620 1320 558 HOH HOH A . 
E 4 HOH 621 1321 643 HOH HOH A . 
E 4 HOH 622 1322 561 HOH HOH A . 
E 4 HOH 623 1323 613 HOH HOH A . 
E 4 HOH 624 1324 256 HOH HOH A . 
E 4 HOH 625 1325 687 HOH HOH A . 
E 4 HOH 626 1326 372 HOH HOH A . 
E 4 HOH 627 1327 677 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 GLU 71 ? CG  ? A GLU 71 CG  
2 1 Y 1 A GLU 71 ? CD  ? A GLU 71 CD  
3 1 Y 1 A GLU 71 ? OE1 ? A GLU 71 OE1 
4 1 Y 1 A GLU 71 ? OE2 ? A GLU 71 OE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? '(1.20.1_4487: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? .                    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                     8Z5B 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     74.590 
_cell.length_a_esd                 ? 
_cell.length_b                     74.590 
_cell.length_b_esd                 ? 
_cell.length_c                     230.946 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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                         8Z5B 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                92 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 41 21 2' 
_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                   8Z5B 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.52 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          51.25 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              8.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M Tris pH 8.5, 20% v/v Ethanol' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            289.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 S 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-10-18 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9785 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL02U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9785 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL02U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8Z5B 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.4 
_reflns.d_resolution_low                               29.02 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     124244 
_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                           96.3 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                14.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          24.2 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_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                                    1.4 
_reflns_shell.d_res_low                                     1.45 
_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                             124244 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               0.03 
_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                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8Z5B 
_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                            1.40 
_refine.ls_d_res_low                             29.02 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     124244 
_refine.ls_number_reflns_R_free                  2000 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    96.29 
_refine.ls_percent_reflns_R_free                 1.61 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1587 
_refine.ls_R_factor_R_free                       0.1731 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1584 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_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                 16.33 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.16 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.40 
_refine_hist.d_res_low                        29.02 
_refine_hist.number_atoms_solvent             627 
_refine_hist.number_atoms_total               4756 
_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        4126 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         3 
_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' ? 0.008 ? 4271 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.041 ? 5822 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 6.554 ? 563  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.093 ? 625  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.011 ? 757  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.40 1.43  . . 123 7526 84.00  . . . . 0.3160 . . . . . . . . . . . 0.3682 
'X-RAY DIFFRACTION' 1.43 1.47  . . 129 7884 89.00  . . . . 0.2430 . . . . . . . . . . . 0.2716 
'X-RAY DIFFRACTION' 1.47 1.52  . . 133 8145 91.00  . . . . 0.1986 . . . . . . . . . . . 0.2168 
'X-RAY DIFFRACTION' 1.52 1.57  . . 138 8415 94.00  . . . . 0.1762 . . . . . . . . . . . 0.2010 
'X-RAY DIFFRACTION' 1.57 1.62  . . 142 8653 96.00  . . . . 0.1655 . . . . . . . . . . . 0.1950 
'X-RAY DIFFRACTION' 1.62 1.69  . . 143 8758 98.00  . . . . 0.1654 . . . . . . . . . . . 0.1707 
'X-RAY DIFFRACTION' 1.69 1.76  . . 144 8813 98.00  . . . . 0.1689 . . . . . . . . . . . 0.1661 
'X-RAY DIFFRACTION' 1.76 1.86  . . 147 8944 99.00  . . . . 0.1601 . . . . . . . . . . . 0.1869 
'X-RAY DIFFRACTION' 1.86 1.97  . . 147 8982 100.00 . . . . 0.1600 . . . . . . . . . . . 0.1888 
'X-RAY DIFFRACTION' 1.97 2.13  . . 147 9050 100.00 . . . . 0.1513 . . . . . . . . . . . 0.1664 
'X-RAY DIFFRACTION' 2.13 2.34  . . 149 9081 100.00 . . . . 0.1544 . . . . . . . . . . . 0.1679 
'X-RAY DIFFRACTION' 2.34 2.68  . . 149 9141 100.00 . . . . 0.1573 . . . . . . . . . . . 0.1830 
'X-RAY DIFFRACTION' 2.68 3.37  . . 152 9248 100.00 . . . . 0.1542 . . . . . . . . . . . 0.1453 
'X-RAY DIFFRACTION' 3.37 29.02 . . 157 9604 99.00  . . . . 0.1428 . . . . . . . . . . . 0.1621 
# 
_struct.entry_id                     8Z5B 
_struct.title                        'The X-Ray crystal structure of multicopper oxidase from Bacillus freudenreichii' 
_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        8Z5B 
_struct_keywords.text            'Oxidized polyphenol substrates, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    PDB 
_struct_ref.db_code                    8Z5B 
_struct_ref.pdbx_db_accession          8Z5B 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   ? 
_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              8Z5B 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 553 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             8Z5B 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  553 
_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       553 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_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 ASN A 49  ? ILE A 53  ? ASN A 49  ILE A 53  5 ? 5 
HELX_P HELX_P2  AA2 ALA A 159 ? ASP A 163 ? ALA A 159 ASP A 163 5 ? 5 
HELX_P HELX_P3  AA3 SER A 171 ? ALA A 175 ? SER A 171 ALA A 175 5 ? 5 
HELX_P HELX_P4  AA4 ILE A 206 ? SER A 213 ? ILE A 206 SER A 213 1 ? 8 
HELX_P HELX_P5  AA5 ASP A 223 ? LEU A 229 ? ASP A 223 LEU A 229 5 ? 7 
HELX_P HELX_P6  AA6 LYS A 233 ? GLY A 235 ? LYS A 233 GLY A 235 5 ? 3 
HELX_P HELX_P7  AA7 SER A 352 ? LYS A 355 ? SER A 352 LYS A 355 5 ? 4 
HELX_P HELX_P8  AA8 GLU A 367 ? MET A 370 ? GLU A 367 MET A 370 5 ? 4 
HELX_P HELX_P9  AA9 TYR A 402 ? ALA A 406 ? TYR A 402 ALA A 406 5 ? 5 
HELX_P HELX_P10 AB1 ASP A 477 ? GLY A 485 ? ASP A 477 GLY A 485 1 ? 9 
HELX_P HELX_P11 AB2 ILE A 534 ? ASP A 539 ? ILE A 534 ASP A 539 1 ? 6 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A HIS 154 ND1 ? ? ? 1_555 B MN . MN ? ? A HIS 154 A MN 601 1_555 ? ? ? ? ? ? ? 1.861 ? ? 
metalc2 metalc ? ? A HIS 200 NE2 ? ? ? 1_555 B MN . MN ? ? A HIS 200 A MN 601 1_555 ? ? ? ? ? ? ? 1.947 ? ? 
metalc3 metalc ? ? A HIS 202 NE2 ? ? ? 1_555 C CU . CU ? ? A HIS 202 A CU 602 1_555 ? ? ? ? ? ? ? 2.063 ? ? 
metalc4 metalc ? ? A HIS 459 ND1 ? ? ? 1_555 D CU . CU ? ? A HIS 459 A CU 603 1_555 ? ? ? ? ? ? ? 2.080 ? ? 
metalc5 metalc ? ? A HIS 464 NE2 ? ? ? 1_555 C CU . CU ? ? A HIS 464 A CU 602 1_555 ? ? ? ? ? ? ? 2.043 ? ? 
metalc6 metalc ? ? A HIS 531 NE2 ? ? ? 1_555 C CU . CU ? ? A HIS 531 A CU 602 1_555 ? ? ? ? ? ? ? 1.824 ? ? 
metalc7 metalc ? ? A CYS 532 SG  ? ? ? 1_555 D CU . CU ? ? A CYS 532 A CU 603 1_555 ? ? ? ? ? ? ? 2.213 ? ? 
metalc8 metalc ? ? A HIS 533 NE2 ? ? ? 1_555 B MN . MN ? ? A HIS 533 A MN 601 1_555 ? ? ? ? ? ? ? 2.180 ? ? 
metalc9 metalc ? ? A HIS 537 ND1 ? ? ? 1_555 D CU . CU ? ? A HIS 537 A CU 603 1_555 ? ? ? ? ? ? ? 2.035 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 ND1 ? A HIS 154 ? A HIS 154 ? 1_555 MN ? B MN . ? A MN 601 ? 1_555 NE2 ? A HIS 200 ? A HIS 200 ? 1_555 139.5 ? 
2 ND1 ? A HIS 154 ? A HIS 154 ? 1_555 MN ? B MN . ? A MN 601 ? 1_555 NE2 ? A HIS 533 ? A HIS 533 ? 1_555 109.2 ? 
3 NE2 ? A HIS 200 ? A HIS 200 ? 1_555 MN ? B MN . ? A MN 601 ? 1_555 NE2 ? A HIS 533 ? A HIS 533 ? 1_555 109.7 ? 
4 NE2 ? A HIS 202 ? A HIS 202 ? 1_555 CU ? C CU . ? A CU 602 ? 1_555 NE2 ? A HIS 464 ? A HIS 464 ? 1_555 117.1 ? 
5 NE2 ? A HIS 202 ? A HIS 202 ? 1_555 CU ? C CU . ? A CU 602 ? 1_555 NE2 ? A HIS 531 ? A HIS 531 ? 1_555 111.1 ? 
6 NE2 ? A HIS 464 ? A HIS 464 ? 1_555 CU ? C CU . ? A CU 602 ? 1_555 NE2 ? A HIS 531 ? A HIS 531 ? 1_555 105.1 ? 
7 ND1 ? A HIS 459 ? A HIS 459 ? 1_555 CU ? D CU . ? A CU 603 ? 1_555 SG  ? A CYS 532 ? A CYS 532 ? 1_555 125.9 ? 
8 ND1 ? A HIS 459 ? A HIS 459 ? 1_555 CU ? D CU . ? A CU 603 ? 1_555 ND1 ? A HIS 537 ? A HIS 537 ? 1_555 102.6 ? 
9 SG  ? A CYS 532 ? A CYS 532 ? 1_555 CU ? D CU . ? A CU 603 ? 1_555 ND1 ? A HIS 537 ? A HIS 537 ? 1_555 129.7 ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 LEU 105 A . ? LEU 105 A PRO 106 A ? PRO 106 A 1 -10.21 
2 PRO 144 A . ? PRO 144 A PRO 145 A ? PRO 145 A 1 1.62   
3 ASN 260 A . ? ASN 260 A PRO 261 A ? PRO 261 A 1 -0.33  
4 ASN 266 A . ? ASN 266 A PRO 267 A ? PRO 267 A 1 -14.59 
5 TYR 540 A . ? TYR 540 A ASP 541 A ? ASP 541 A 1 -4.85  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 4 ? 
AA3 ? 4 ? 
AA4 ? 7 ? 
AA5 ? 5 ? 
AA6 ? 5 ? 
AA7 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? parallel      
AA2 3 4 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? parallel      
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? parallel      
AA6 3 4 ? anti-parallel 
AA6 4 5 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ALA A 70  ? ILE A 72  ? ALA A 70  ILE A 72  
AA1 2 SER A 75  ? HIS A 87  ? SER A 75  HIS A 87  
AA1 3 THR A 96  ? TYR A 101 ? THR A 96  TYR A 101 
AA2 1 ALA A 70  ? ILE A 72  ? ALA A 70  ILE A 72  
AA2 2 SER A 75  ? HIS A 87  ? SER A 75  HIS A 87  
AA2 3 ILE A 118 ? ASN A 124 ? ILE A 118 ASN A 124 
AA2 4 VAL A 185 ? TYR A 188 ? VAL A 185 TYR A 188 
AA3 1 GLY A 107 ? GLN A 113 ? GLY A 107 GLN A 113 
AA3 2 SER A 216 ? GLU A 222 ? SER A 216 GLU A 222 
AA3 3 ALA A 195 ? ASP A 201 ? ALA A 195 ASP A 201 
AA3 4 VAL A 151 ? HIS A 154 ? VAL A 151 HIS A 154 
AA4 1 LYS A 283 ? ILE A 284 ? LYS A 283 ILE A 284 
AA4 2 THR A 277 ? VAL A 280 ? THR A 277 VAL A 280 
AA4 3 ASP A 237 ? ARG A 245 ? ASP A 237 ARG A 245 
AA4 4 LYS A 294 ? ASN A 301 ? LYS A 294 ASN A 301 
AA4 5 ARG A 344 ? ASP A 350 ? ARG A 344 ASP A 350 
AA4 6 PHE A 318 ? THR A 323 ? PHE A 318 THR A 323 
AA4 7 GLY A 326 ? LEU A 334 ? GLY A 326 LEU A 334 
AA5 1 LYS A 287 ? VAL A 290 ? LYS A 287 VAL A 290 
AA5 2 ILE A 372 ? VAL A 378 ? ILE A 372 VAL A 378 
AA5 3 LYS A 358 ? ASN A 363 ? LYS A 358 ASN A 363 
AA5 4 TYR A 308 ? LEU A 312 ? TYR A 308 LEU A 312 
AA5 5 LEU A 337 ? LEU A 339 ? LEU A 337 LEU A 339 
AA6 1 PRO A 424 ? LEU A 428 ? PRO A 424 LEU A 428 
AA6 2 LYS A 408 ? GLN A 418 ? LYS A 408 GLN A 418 
AA6 3 THR A 446 ? ASN A 453 ? THR A 446 ASN A 453 
AA6 4 MET A 513 ? LYS A 520 ? MET A 513 LYS A 520 
AA6 5 LYS A 469 ? PRO A 475 ? LYS A 469 PRO A 475 
AA7 1 THR A 506 ? ALA A 509 ? THR A 506 ALA A 509 
AA7 2 HIS A 459 ? ILE A 463 ? HIS A 459 ILE A 463 
AA7 3 GLY A 526 ? CYS A 532 ? GLY A 526 CYS A 532 
AA7 4 MET A 543 ? VAL A 548 ? MET A 543 VAL A 548 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ALA A 70  ? N ALA A 70  O TYR A 77  ? O TYR A 77  
AA1 2 3 N VAL A 85  ? N VAL A 85  O VAL A 98  ? O VAL A 98  
AA2 1 2 N ALA A 70  ? N ALA A 70  O TYR A 77  ? O TYR A 77  
AA2 2 3 N MET A 82  ? N MET A 82  O LYS A 123 ? O LYS A 123 
AA2 3 4 N VAL A 120 ? N VAL A 120 O TYR A 186 ? O TYR A 186 
AA3 1 2 N ILE A 110 ? N ILE A 110 O LEU A 220 ? O LEU A 220 
AA3 2 3 O TYR A 219 ? O TYR A 219 N LEU A 197 ? N LEU A 197 
AA3 3 4 O HIS A 200 ? O HIS A 200 N HIS A 152 ? N HIS A 152 
AA4 1 2 O LYS A 283 ? O LYS A 283 N VAL A 280 ? N VAL A 280 
AA4 2 3 O ALA A 279 ? O ALA A 279 N GLN A 243 ? N GLN A 243 
AA4 3 4 N LEU A 240 ? N LEU A 240 O ARG A 298 ? O ARG A 298 
AA4 4 5 N PHE A 297 ? N PHE A 297 O VAL A 347 ? O VAL A 347 
AA4 5 6 O ASP A 346 ? O ASP A 346 N ILE A 321 ? N ILE A 321 
AA4 6 7 N PHE A 318 ? N PHE A 318 O LEU A 334 ? O LEU A 334 
AA5 1 2 N LEU A 288 ? N LEU A 288 O ASP A 377 ? O ASP A 377 
AA5 2 3 O MET A 374 ? O MET A 374 N LEU A 361 ? N LEU A 361 
AA5 3 4 O GLN A 362 ? O GLN A 362 N ARG A 311 ? N ARG A 311 
AA5 4 5 N TYR A 308 ? N TYR A 308 O LEU A 339 ? O LEU A 339 
AA6 1 2 O LEU A 427 ? O LEU A 427 N ASP A 415 ? N ASP A 415 
AA6 2 3 N ARG A 410 ? N ARG A 410 O LYS A 450 ? O LYS A 450 
AA6 3 4 N LEU A 451 ? N LEU A 451 O THR A 515 ? O THR A 515 
AA6 4 5 O SER A 516 ? O SER A 516 N HIS A 472 ? N HIS A 472 
AA7 1 2 O ALA A 509 ? O ALA A 509 N HIS A 459 ? N HIS A 459 
AA7 2 3 N HIS A 462 ? N HIS A 462 O HIS A 531 ? O HIS A 531 
AA7 3 4 N TYR A 528 ? N TYR A 528 O MET A 546 ? O MET A 546 
# 
_pdbx_entry_details.entry_id                   8Z5B 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    1059 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    1176 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.03 
# 
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 ARG A 182 ? ? -133.45 -40.24  
2  1 HIS A 202 ? ? -142.09 23.66   
3  1 ASP A 234 ? ? 59.98   -123.09 
4  1 PRO A 271 ? ? -80.61  36.83   
5  1 THR A 305 ? ? -131.13 -39.92  
6  1 ALA A 342 ? ? 79.78   -9.76   
7  1 LEU A 465 ? ? 69.58   -35.62  
8  1 ASP A 484 ? ? -140.62 10.75   
9  1 TYR A 528 ? ? -125.55 -168.48 
10 1 TYR A 540 ? ? -157.50 88.83   
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 76.0109 37.6102 75.0910  0.1286 ? 0.0018  ? 0.0303  ? 0.1488 ? -0.0087 ? 0.0590 ? 3.3785 ? 0.6423  
? 0.2196  ? 1.7746 ? -0.5418 ? 0.9274 ? -0.0712 ? 0.4233  ? -0.0204 ? -0.1047 ? 0.0573 ? -0.0485 ? -0.0027 ? 0.0729  ? 0.0146  ? 
2 'X-RAY DIFFRACTION' ? refined 65.0159 27.9281 82.6293  0.0839 ? -0.0097 ? -0.0004 ? 0.1256 ? 0.0055  ? 0.1090 ? 1.1612 ? 0.1644  
? -0.0688 ? 1.1458 ? -0.2756 ? 0.6982 ? -0.0376 ? 0.1087  ? -0.0987 ? -0.0313 ? 0.0620 ? 0.1378  ? 0.0106  ? -0.0793 ? -0.0228 ? 
3 'X-RAY DIFFRACTION' ? refined 76.0783 41.5822 86.2860  0.1171 ? -0.0095 ? -0.0138 ? 0.1188 ? 0.0142  ? 0.0888 ? 1.0654 ? -0.5448 
? 0.1228  ? 1.9049 ? -0.7067 ? 0.6772 ? -0.0597 ? 0.0472  ? 0.0479  ? 0.1405  ? 0.0371 ? -0.0719 ? -0.1218 ? 0.0112  ? 0.0237  ? 
4 'X-RAY DIFFRACTION' ? refined 68.2518 50.3823 89.3502  0.1963 ? 0.0231  ? -0.0140 ? 0.1113 ? 0.0149  ? 0.1176 ? 1.5817 ? -0.2739 
? -0.1900 ? 1.4400 ? -0.4383 ? 1.0584 ? -0.0667 ? 0.0776  ? 0.2145  ? 0.2343  ? 0.0986 ? 0.0681  ? -0.2024 ? -0.1210 ? -0.0554 ? 
5 'X-RAY DIFFRACTION' ? refined 65.4847 29.5450 106.4608 0.3016 ? 0.0737  ? 0.0428  ? 0.2360 ? 0.0733  ? 0.1460 ? 1.4053 ? -0.4448 
? -0.2942 ? 1.3315 ? -0.1018 ? 0.6977 ? -0.1297 ? -0.1778 ? -0.1383 ? 0.5310  ? 0.1983 ? 0.1427  ? -0.1248 ? -0.0969 ? -0.0365 ? 
6 'X-RAY DIFFRACTION' ? refined 64.9875 44.0756 108.9792 0.3825 ? 0.0856  ? 0.0175  ? 0.2074 ? 0.0142  ? 0.1489 ? 0.0796 ? 0.0514  
? 0.0614  ? 0.3247 ? -0.4170 ? 3.0697 ? -0.0461 ? -0.0541 ? 0.0277  ? 0.4216  ? 0.1111 ? 0.0029  ? -0.3771 ? 0.2115  ? -0.0673 ? 
7 'X-RAY DIFFRACTION' ? refined 61.6820 32.4286 100.7821 0.2082 ? 0.0599  ? 0.0546  ? 0.1794 ? 0.0649  ? 0.1402 ? 1.2894 ? -0.3306 
? -0.0030 ? 1.3974 ? -0.3222 ? 1.3785 ? -0.0761 ? -0.0644 ? -0.1073 ? 0.2701  ? 0.1606 ? 0.2513  ? -0.1581 ? -0.1829 ? -0.0728 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 44 through 76 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 77 through 233 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 234 through 331 )
;
4 'X-RAY DIFFRACTION' 4 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 332 through 418 )
;
5 'X-RAY DIFFRACTION' 5 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 419 through 463 )
;
6 'X-RAY DIFFRACTION' 6 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 464 through 505 )
;
7 'X-RAY DIFFRACTION' 7 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 506 through 550 )
;
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       1327 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.49 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
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 1   ? A MET 1   
2  1 Y 1 A GLY 2   ? A GLY 2   
3  1 Y 1 A SER 3   ? A SER 3   
4  1 Y 1 A SER 4   ? A SER 4   
5  1 Y 1 A HIS 5   ? A HIS 5   
6  1 Y 1 A HIS 6   ? A HIS 6   
7  1 Y 1 A HIS 7   ? A HIS 7   
8  1 Y 1 A HIS 8   ? A HIS 8   
9  1 Y 1 A HIS 9   ? A HIS 9   
10 1 Y 1 A HIS 10  ? A HIS 10  
11 1 Y 1 A SER 11  ? A SER 11  
12 1 Y 1 A SER 12  ? A SER 12  
13 1 Y 1 A GLY 13  ? A GLY 13  
14 1 Y 1 A LEU 14  ? A LEU 14  
15 1 Y 1 A VAL 15  ? A VAL 15  
16 1 Y 1 A PRO 16  ? A PRO 16  
17 1 Y 1 A ARG 17  ? A ARG 17  
18 1 Y 1 A GLY 18  ? A GLY 18  
19 1 Y 1 A SER 19  ? A SER 19  
20 1 Y 1 A HIS 20  ? A HIS 20  
21 1 Y 1 A MET 21  ? A MET 21  
22 1 Y 1 A ALA 22  ? A ALA 22  
23 1 Y 1 A SER 23  ? A SER 23  
24 1 Y 1 A MET 24  ? A MET 24  
25 1 Y 1 A THR 25  ? A THR 25  
26 1 Y 1 A GLY 26  ? A GLY 26  
27 1 Y 1 A GLY 27  ? A GLY 27  
28 1 Y 1 A GLN 28  ? A GLN 28  
29 1 Y 1 A GLN 29  ? A GLN 29  
30 1 Y 1 A MET 30  ? A MET 30  
31 1 Y 1 A GLY 31  ? A GLY 31  
32 1 Y 1 A ARG 32  ? A ARG 32  
33 1 Y 1 A GLY 33  ? A GLY 33  
34 1 Y 1 A SER 34  ? A SER 34  
35 1 Y 1 A MET 35  ? A MET 35  
36 1 Y 1 A LYS 36  ? A LYS 36  
37 1 Y 1 A ILE 37  ? A ILE 37  
38 1 Y 1 A LYS 38  ? A LYS 38  
39 1 Y 1 A ASN 39  ? A ASN 39  
40 1 Y 1 A LYS 40  ? A LYS 40  
41 1 Y 1 A ARG 41  ? A ARG 41  
42 1 Y 1 A ARG 42  ? A ARG 42  
43 1 Y 1 A MET 43  ? A MET 43  
44 1 Y 1 A LYS 551 ? A LYS 551 
45 1 Y 1 A GLU 552 ? A GLU 552 
46 1 Y 1 A LYS 553 ? A LYS 553 
# 
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  
CU  CU   CU N N 74  
CYS N    N  N N 75  
CYS CA   C  N R 76  
CYS C    C  N N 77  
CYS O    O  N N 78  
CYS CB   C  N N 79  
CYS SG   S  N N 80  
CYS OXT  O  N N 81  
CYS H    H  N N 82  
CYS H2   H  N N 83  
CYS HA   H  N N 84  
CYS HB2  H  N N 85  
CYS HB3  H  N N 86  
CYS HG   H  N N 87  
CYS HXT  H  N N 88  
GLN N    N  N N 89  
GLN CA   C  N S 90  
GLN C    C  N N 91  
GLN O    O  N N 92  
GLN CB   C  N N 93  
GLN CG   C  N N 94  
GLN CD   C  N N 95  
GLN OE1  O  N N 96  
GLN NE2  N  N N 97  
GLN OXT  O  N N 98  
GLN H    H  N N 99  
GLN H2   H  N N 100 
GLN HA   H  N N 101 
GLN HB2  H  N N 102 
GLN HB3  H  N N 103 
GLN HG2  H  N N 104 
GLN HG3  H  N N 105 
GLN HE21 H  N N 106 
GLN HE22 H  N N 107 
GLN HXT  H  N N 108 
GLU N    N  N N 109 
GLU CA   C  N S 110 
GLU C    C  N N 111 
GLU O    O  N N 112 
GLU CB   C  N N 113 
GLU CG   C  N N 114 
GLU CD   C  N N 115 
GLU OE1  O  N N 116 
GLU OE2  O  N N 117 
GLU OXT  O  N N 118 
GLU H    H  N N 119 
GLU H2   H  N N 120 
GLU HA   H  N N 121 
GLU HB2  H  N N 122 
GLU HB3  H  N N 123 
GLU HG2  H  N N 124 
GLU HG3  H  N N 125 
GLU HE2  H  N N 126 
GLU HXT  H  N N 127 
GLY N    N  N N 128 
GLY CA   C  N N 129 
GLY C    C  N N 130 
GLY O    O  N N 131 
GLY OXT  O  N N 132 
GLY H    H  N N 133 
GLY H2   H  N N 134 
GLY HA2  H  N N 135 
GLY HA3  H  N N 136 
GLY HXT  H  N N 137 
HIS N    N  N N 138 
HIS CA   C  N S 139 
HIS C    C  N N 140 
HIS O    O  N N 141 
HIS CB   C  N N 142 
HIS CG   C  Y N 143 
HIS ND1  N  Y N 144 
HIS CD2  C  Y N 145 
HIS CE1  C  Y N 146 
HIS NE2  N  Y N 147 
HIS OXT  O  N N 148 
HIS H    H  N N 149 
HIS H2   H  N N 150 
HIS HA   H  N N 151 
HIS HB2  H  N N 152 
HIS HB3  H  N N 153 
HIS HD1  H  N N 154 
HIS HD2  H  N N 155 
HIS HE1  H  N N 156 
HIS HE2  H  N N 157 
HIS HXT  H  N N 158 
HOH O    O  N N 159 
HOH H1   H  N N 160 
HOH H2   H  N N 161 
ILE N    N  N N 162 
ILE CA   C  N S 163 
ILE C    C  N N 164 
ILE O    O  N N 165 
ILE CB   C  N S 166 
ILE CG1  C  N N 167 
ILE CG2  C  N N 168 
ILE CD1  C  N N 169 
ILE OXT  O  N N 170 
ILE H    H  N N 171 
ILE H2   H  N N 172 
ILE HA   H  N N 173 
ILE HB   H  N N 174 
ILE HG12 H  N N 175 
ILE HG13 H  N N 176 
ILE HG21 H  N N 177 
ILE HG22 H  N N 178 
ILE HG23 H  N N 179 
ILE HD11 H  N N 180 
ILE HD12 H  N N 181 
ILE HD13 H  N N 182 
ILE HXT  H  N N 183 
LEU N    N  N N 184 
LEU CA   C  N S 185 
LEU C    C  N N 186 
LEU O    O  N N 187 
LEU CB   C  N N 188 
LEU CG   C  N N 189 
LEU CD1  C  N N 190 
LEU CD2  C  N N 191 
LEU OXT  O  N N 192 
LEU H    H  N N 193 
LEU H2   H  N N 194 
LEU HA   H  N N 195 
LEU HB2  H  N N 196 
LEU HB3  H  N N 197 
LEU HG   H  N N 198 
LEU HD11 H  N N 199 
LEU HD12 H  N N 200 
LEU HD13 H  N N 201 
LEU HD21 H  N N 202 
LEU HD22 H  N N 203 
LEU HD23 H  N N 204 
LEU HXT  H  N N 205 
LYS N    N  N N 206 
LYS CA   C  N S 207 
LYS C    C  N N 208 
LYS O    O  N N 209 
LYS CB   C  N N 210 
LYS CG   C  N N 211 
LYS CD   C  N N 212 
LYS CE   C  N N 213 
LYS NZ   N  N N 214 
LYS OXT  O  N N 215 
LYS H    H  N N 216 
LYS H2   H  N N 217 
LYS HA   H  N N 218 
LYS HB2  H  N N 219 
LYS HB3  H  N N 220 
LYS HG2  H  N N 221 
LYS HG3  H  N N 222 
LYS HD2  H  N N 223 
LYS HD3  H  N N 224 
LYS HE2  H  N N 225 
LYS HE3  H  N N 226 
LYS HZ1  H  N N 227 
LYS HZ2  H  N N 228 
LYS HZ3  H  N N 229 
LYS HXT  H  N N 230 
MET N    N  N N 231 
MET CA   C  N S 232 
MET C    C  N N 233 
MET O    O  N N 234 
MET CB   C  N N 235 
MET CG   C  N N 236 
MET SD   S  N N 237 
MET CE   C  N N 238 
MET OXT  O  N N 239 
MET H    H  N N 240 
MET H2   H  N N 241 
MET HA   H  N N 242 
MET HB2  H  N N 243 
MET HB3  H  N N 244 
MET HG2  H  N N 245 
MET HG3  H  N N 246 
MET HE1  H  N N 247 
MET HE2  H  N N 248 
MET HE3  H  N N 249 
MET HXT  H  N N 250 
MN  MN   MN N N 251 
PHE N    N  N N 252 
PHE CA   C  N S 253 
PHE C    C  N N 254 
PHE O    O  N N 255 
PHE CB   C  N N 256 
PHE CG   C  Y N 257 
PHE CD1  C  Y N 258 
PHE CD2  C  Y N 259 
PHE CE1  C  Y N 260 
PHE CE2  C  Y N 261 
PHE CZ   C  Y N 262 
PHE OXT  O  N N 263 
PHE H    H  N N 264 
PHE H2   H  N N 265 
PHE HA   H  N N 266 
PHE HB2  H  N N 267 
PHE HB3  H  N N 268 
PHE HD1  H  N N 269 
PHE HD2  H  N N 270 
PHE HE1  H  N N 271 
PHE HE2  H  N N 272 
PHE HZ   H  N N 273 
PHE HXT  H  N N 274 
PRO N    N  N N 275 
PRO CA   C  N S 276 
PRO C    C  N N 277 
PRO O    O  N N 278 
PRO CB   C  N N 279 
PRO CG   C  N N 280 
PRO CD   C  N N 281 
PRO OXT  O  N N 282 
PRO H    H  N N 283 
PRO HA   H  N N 284 
PRO HB2  H  N N 285 
PRO HB3  H  N N 286 
PRO HG2  H  N N 287 
PRO HG3  H  N N 288 
PRO HD2  H  N N 289 
PRO HD3  H  N N 290 
PRO HXT  H  N N 291 
SER N    N  N N 292 
SER CA   C  N S 293 
SER C    C  N N 294 
SER O    O  N N 295 
SER CB   C  N N 296 
SER OG   O  N N 297 
SER OXT  O  N N 298 
SER H    H  N N 299 
SER H2   H  N N 300 
SER HA   H  N N 301 
SER HB2  H  N N 302 
SER HB3  H  N N 303 
SER HG   H  N N 304 
SER HXT  H  N N 305 
THR N    N  N N 306 
THR CA   C  N S 307 
THR C    C  N N 308 
THR O    O  N N 309 
THR CB   C  N R 310 
THR OG1  O  N N 311 
THR CG2  C  N N 312 
THR OXT  O  N N 313 
THR H    H  N N 314 
THR H2   H  N N 315 
THR HA   H  N N 316 
THR HB   H  N N 317 
THR HG1  H  N N 318 
THR HG21 H  N N 319 
THR HG22 H  N N 320 
THR HG23 H  N N 321 
THR HXT  H  N N 322 
TRP N    N  N N 323 
TRP CA   C  N S 324 
TRP C    C  N N 325 
TRP O    O  N N 326 
TRP CB   C  N N 327 
TRP CG   C  Y N 328 
TRP CD1  C  Y N 329 
TRP CD2  C  Y N 330 
TRP NE1  N  Y N 331 
TRP CE2  C  Y N 332 
TRP CE3  C  Y N 333 
TRP CZ2  C  Y N 334 
TRP CZ3  C  Y N 335 
TRP CH2  C  Y N 336 
TRP OXT  O  N N 337 
TRP H    H  N N 338 
TRP H2   H  N N 339 
TRP HA   H  N N 340 
TRP HB2  H  N N 341 
TRP HB3  H  N N 342 
TRP HD1  H  N N 343 
TRP HE1  H  N N 344 
TRP HE3  H  N N 345 
TRP HZ2  H  N N 346 
TRP HZ3  H  N N 347 
TRP HH2  H  N N 348 
TRP HXT  H  N N 349 
TYR N    N  N N 350 
TYR CA   C  N S 351 
TYR C    C  N N 352 
TYR O    O  N N 353 
TYR CB   C  N N 354 
TYR CG   C  Y N 355 
TYR CD1  C  Y N 356 
TYR CD2  C  Y N 357 
TYR CE1  C  Y N 358 
TYR CE2  C  Y N 359 
TYR CZ   C  Y N 360 
TYR OH   O  N N 361 
TYR OXT  O  N N 362 
TYR H    H  N N 363 
TYR H2   H  N N 364 
TYR HA   H  N N 365 
TYR HB2  H  N N 366 
TYR HB3  H  N N 367 
TYR HD1  H  N N 368 
TYR HD2  H  N N 369 
TYR HE1  H  N N 370 
TYR HE2  H  N N 371 
TYR HH   H  N N 372 
TYR HXT  H  N N 373 
VAL N    N  N N 374 
VAL CA   C  N S 375 
VAL C    C  N N 376 
VAL O    O  N N 377 
VAL CB   C  N N 378 
VAL CG1  C  N N 379 
VAL CG2  C  N N 380 
VAL OXT  O  N N 381 
VAL H    H  N N 382 
VAL H2   H  N N 383 
VAL HA   H  N N 384 
VAL HB   H  N N 385 
VAL HG11 H  N N 386 
VAL HG12 H  N N 387 
VAL HG13 H  N N 388 
VAL HG21 H  N N 389 
VAL HG22 H  N N 390 
VAL HG23 H  N N 391 
VAL HXT  H  N N 392 
# 
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 
# 
_pdbx_audit_support.funding_organization   'Other private' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8Z5B 
_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]   0.013407 
_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]   0.013407 
_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]   0.004330 
_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  
CU 
MN 
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   . LYS A 1 44  ? 99.539  38.285 75.048  1.00 43.88 ? 44   LYS A N   1 
ATOM   2    C  CA  . LYS A 1 44  ? 98.730  37.069 74.977  1.00 34.01 ? 44   LYS A CA  1 
ATOM   3    C  C   . LYS A 1 44  ? 97.608  37.113 76.024  1.00 35.79 ? 44   LYS A C   1 
ATOM   4    O  O   . LYS A 1 44  ? 97.863  37.344 77.213  1.00 34.37 ? 44   LYS A O   1 
ATOM   5    C  CB  . LYS A 1 44  ? 99.604  35.828 75.181  1.00 39.83 ? 44   LYS A CB  1 
ATOM   6    C  CG  . LYS A 1 44  ? 98.832  34.521 75.173  1.00 42.87 ? 44   LYS A CG  1 
ATOM   7    C  CD  . LYS A 1 44  ? 98.397  34.159 73.757  1.00 45.87 ? 44   LYS A CD  1 
ATOM   8    C  CE  . LYS A 1 44  ? 97.012  33.508 73.761  1.00 48.38 ? 44   LYS A CE  1 
ATOM   9    N  NZ  . LYS A 1 44  ? 96.260  33.784 72.498  1.00 50.44 ? 44   LYS A NZ  1 
ATOM   10   N  N   . VAL A 1 45  ? 96.373  36.892 75.581  1.00 29.37 ? 45   VAL A N   1 
ATOM   11   C  CA  . VAL A 1 45  ? 95.227  36.924 76.484  1.00 24.84 ? 45   VAL A CA  1 
ATOM   12   C  C   . VAL A 1 45  ? 95.095  35.553 77.132  1.00 26.50 ? 45   VAL A C   1 
ATOM   13   O  O   . VAL A 1 45  ? 94.893  34.542 76.449  1.00 26.33 ? 45   VAL A O   1 
ATOM   14   C  CB  . VAL A 1 45  ? 93.942  37.322 75.747  1.00 24.22 ? 45   VAL A CB  1 
ATOM   15   C  CG1 . VAL A 1 45  ? 92.755  37.318 76.719  1.00 22.25 ? 45   VAL A CG1 1 
ATOM   16   C  CG2 . VAL A 1 45  ? 94.104  38.688 75.101  1.00 24.79 ? 45   VAL A CG2 1 
ATOM   17   N  N   . ASP A 1 46  ? 95.245  35.519 78.449  1.00 21.44 ? 46   ASP A N   1 
ATOM   18   C  CA  . ASP A 1 46  ? 95.064  34.320 79.254  1.00 19.06 ? 46   ASP A CA  1 
ATOM   19   C  C   . ASP A 1 46  ? 93.733  34.481 79.971  1.00 19.53 ? 46   ASP A C   1 
ATOM   20   O  O   . ASP A 1 46  ? 93.617  35.333 80.864  1.00 19.02 ? 46   ASP A O   1 
ATOM   21   C  CB  . ASP A 1 46  ? 96.217  34.232 80.260  1.00 21.58 ? 46   ASP A CB  1 
ATOM   22   C  CG  . ASP A 1 46  ? 96.073  33.081 81.256  1.00 21.28 ? 46   ASP A CG  1 
ATOM   23   O  OD1 . ASP A 1 46  ? 95.047  32.371 81.260  1.00 20.17 ? 46   ASP A OD1 1 
ATOM   24   O  OD2 . ASP A 1 46  ? 97.019  32.884 82.044  1.00 26.49 ? 46   ASP A OD2 1 
ATOM   25   N  N   . PRO A 1 47  ? 92.710  33.709 79.612  1.00 17.25 ? 47   PRO A N   1 
ATOM   26   C  CA  . PRO A 1 47  ? 91.394  33.866 80.251  1.00 18.70 ? 47   PRO A CA  1 
ATOM   27   C  C   . PRO A 1 47  ? 91.421  33.787 81.766  1.00 19.07 ? 47   PRO A C   1 
ATOM   28   O  O   . PRO A 1 47  ? 90.520  34.338 82.414  1.00 16.54 ? 47   PRO A O   1 
ATOM   29   C  CB  . PRO A 1 47  ? 90.589  32.695 79.662  1.00 16.82 ? 47   PRO A CB  1 
ATOM   30   C  CG  . PRO A 1 47  ? 91.205  32.480 78.307  1.00 19.11 ? 47   PRO A CG  1 
ATOM   31   C  CD  . PRO A 1 47  ? 92.698  32.706 78.532  1.00 17.61 ? 47   PRO A CD  1 
ATOM   32   N  N   . SER A 1 48  ? 92.397  33.086 82.346  1.00 18.27 ? 48   SER A N   1 
ATOM   33   C  CA  . SER A 1 48  ? 92.480  32.923 83.790  1.00 18.54 ? 48   SER A CA  1 
ATOM   34   C  C   . SER A 1 48  ? 93.157  34.100 84.466  1.00 18.85 ? 48   SER A C   1 
ATOM   35   O  O   . SER A 1 48  ? 93.176  34.154 85.697  1.00 21.46 ? 48   SER A O   1 
ATOM   36   C  CB  . SER A 1 48  ? 93.232  31.641 84.169  1.00 17.71 ? 48   SER A CB  1 
ATOM   37   O  OG  . SER A 1 48  ? 94.615  31.697 83.840  1.00 21.01 ? 48   SER A OG  1 
ATOM   38   N  N   . ASN A 1 49  ? 93.702  35.041 83.697  1.00 18.95 ? 49   ASN A N   1 
ATOM   39   C  CA  . ASN A 1 49  ? 94.425  36.185 84.247  1.00 19.52 ? 49   ASN A CA  1 
ATOM   40   C  C   . ASN A 1 49  ? 93.746  37.459 83.777  1.00 16.27 ? 49   ASN A C   1 
ATOM   41   O  O   . ASN A 1 49  ? 94.039  37.956 82.675  1.00 20.11 ? 49   ASN A O   1 
ATOM   42   C  CB  . ASN A 1 49  ? 95.887  36.169 83.819  1.00 20.48 ? 49   ASN A CB  1 
ATOM   43   C  CG  . ASN A 1 49  ? 96.672  37.282 84.472  1.00 23.76 ? 49   ASN A CG  1 
ATOM   44   O  OD1 . ASN A 1 49  ? 96.084  38.174 85.092  1.00 22.20 ? 49   ASN A OD1 1 
ATOM   45   N  ND2 . ASN A 1 49  ? 97.988  37.267 84.305  1.00 24.41 ? 49   ASN A ND2 1 
ATOM   46   N  N   . PRO A 1 50  ? 92.841  38.023 84.576  1.00 17.91 ? 50   PRO A N   1 
ATOM   47   C  CA  . PRO A 1 50  ? 92.057  39.179 84.110  1.00 18.90 ? 50   PRO A CA  1 
ATOM   48   C  C   . PRO A 1 50  ? 92.892  40.397 83.783  1.00 19.06 ? 50   PRO A C   1 
ATOM   49   O  O   . PRO A 1 50  ? 92.410  41.258 83.040  1.00 19.54 ? 50   PRO A O   1 
ATOM   50   C  CB  . PRO A 1 50  ? 91.071  39.447 85.259  1.00 22.39 ? 50   PRO A CB  1 
ATOM   51   C  CG  . PRO A 1 50  ? 91.631  38.710 86.439  1.00 32.32 ? 50   PRO A CG  1 
ATOM   52   C  CD  . PRO A 1 50  ? 92.393  37.529 85.888  1.00 23.56 ? 50   PRO A CD  1 
ATOM   53   N  N   . GLU A 1 51  ? 94.125  40.497 84.297  1.00 20.38 ? 51   GLU A N   1 
ATOM   54   C  CA  . GLU A 1 51  ? 94.968  41.627 83.934  1.00 21.91 ? 51   GLU A CA  1 
ATOM   55   C  C   . GLU A 1 51  ? 95.430  41.569 82.480  1.00 24.48 ? 51   GLU A C   1 
ATOM   56   O  O   . GLU A 1 51  ? 95.907  42.583 81.958  1.00 26.06 ? 51   GLU A O   1 
ATOM   57   C  CB  . GLU A 1 51  ? 96.168  41.705 84.885  1.00 27.65 ? 51   GLU A CB  1 
ATOM   58   C  CG  . GLU A 1 51  ? 95.839  42.408 86.195  1.00 32.40 ? 51   GLU A CG  1 
ATOM   59   C  CD  . GLU A 1 51  ? 96.973  42.331 87.210  1.00 41.95 ? 51   GLU A CD  1 
ATOM   60   O  OE1 . GLU A 1 51  ? 98.061  41.808 86.872  1.00 46.30 ? 51   GLU A OE1 1 
ATOM   61   O  OE2 . GLU A 1 51  ? 96.776  42.806 88.348  1.00 50.73 ? 51   GLU A OE2 1 
ATOM   62   N  N   . THR A 1 52  ? 95.287  40.420 81.812  1.00 21.26 ? 52   THR A N   1 
ATOM   63   C  CA  . THR A 1 52  ? 95.623  40.298 80.398  1.00 19.82 ? 52   THR A CA  1 
ATOM   64   C  C   . THR A 1 52  ? 94.439  40.534 79.464  1.00 19.09 ? 52   THR A C   1 
ATOM   65   O  O   . THR A 1 52  ? 94.626  40.448 78.246  1.00 21.67 ? 52   THR A O   1 
ATOM   66   C  CB  . THR A 1 52  ? 96.216  38.916 80.081  1.00 20.02 ? 52   THR A CB  1 
ATOM   67   O  OG1 . THR A 1 52  ? 95.186  37.915 80.110  1.00 20.97 ? 52   THR A OG1 1 
ATOM   68   C  CG2 . THR A 1 52  ? 97.319  38.537 81.065  1.00 23.54 ? 52   THR A CG2 1 
ATOM   69   N  N   . ILE A 1 53  ? 93.242  40.809 79.985  1.00 18.23 ? 53   ILE A N   1 
ATOM   70   C  CA  . ILE A 1 53  ? 92.032  40.896 79.174  1.00 17.80 ? 53   ILE A CA  1 
ATOM   71   C  C   . ILE A 1 53  ? 91.781  42.365 78.841  1.00 18.65 ? 53   ILE A C   1 
ATOM   72   O  O   . ILE A 1 53  ? 91.477  43.151 79.751  1.00 21.14 ? 53   ILE A O   1 
ATOM   73   C  CB  . ILE A 1 53  ? 90.815  40.288 79.883  1.00 18.76 ? 53   ILE A CB  1 
ATOM   74   C  CG1 . ILE A 1 53  ? 91.036  38.807 80.174  1.00 18.65 ? 53   ILE A CG1 1 
ATOM   75   C  CG2 . ILE A 1 53  ? 89.563  40.493 79.042  1.00 19.00 ? 53   ILE A CG2 1 
ATOM   76   C  CD1 . ILE A 1 53  ? 90.104  38.245 81.283  1.00 19.69 ? 53   ILE A CD1 1 
ATOM   77   N  N   . PRO A 1 54  ? 91.865  42.772 77.576  1.00 19.16 ? 54   PRO A N   1 
ATOM   78   C  CA  . PRO A 1 54  ? 91.582  44.174 77.235  1.00 17.91 ? 54   PRO A CA  1 
ATOM   79   C  C   . PRO A 1 54  ? 90.091  44.440 77.334  1.00 19.23 ? 54   PRO A C   1 
ATOM   80   O  O   . PRO A 1 54  ? 89.285  43.785 76.671  1.00 19.52 ? 54   PRO A O   1 
ATOM   81   C  CB  . PRO A 1 54  ? 92.081  44.305 75.790  1.00 21.12 ? 54   PRO A CB  1 
ATOM   82   C  CG  . PRO A 1 54  ? 92.870  43.084 75.506  1.00 24.81 ? 54   PRO A CG  1 
ATOM   83   C  CD  . PRO A 1 54  ? 92.420  42.014 76.441  1.00 20.43 ? 54   PRO A CD  1 
ATOM   84   N  N   . LYS A 1 55  ? 89.732  45.415 78.153  1.00 17.24 ? 55   LYS A N   1 
ATOM   85   C  CA  A LYS A 1 55  ? 88.328  45.728 78.383  0.80 16.86 ? 55   LYS A CA  1 
ATOM   86   C  CA  B LYS A 1 55  ? 88.325  45.701 78.364  0.20 17.09 ? 55   LYS A CA  1 
ATOM   87   C  C   . LYS A 1 55  ? 87.730  46.458 77.186  1.00 18.55 ? 55   LYS A C   1 
ATOM   88   O  O   . LYS A 1 55  ? 88.433  47.103 76.397  1.00 18.64 ? 55   LYS A O   1 
ATOM   89   C  CB  A LYS A 1 55  ? 88.170  46.576 79.649  0.80 17.91 ? 55   LYS A CB  1 
ATOM   90   C  CB  B LYS A 1 55  ? 88.126  46.501 79.645  0.20 18.08 ? 55   LYS A CB  1 
ATOM   91   C  CG  A LYS A 1 55  ? 88.659  45.879 80.908  0.80 16.35 ? 55   LYS A CG  1 
ATOM   92   C  CG  B LYS A 1 55  ? 88.460  45.684 80.850  0.20 15.56 ? 55   LYS A CG  1 
ATOM   93   C  CD  A LYS A 1 55  ? 88.355  46.701 82.144  0.80 17.76 ? 55   LYS A CD  1 
ATOM   94   C  CD  B LYS A 1 55  ? 88.234  46.434 82.120  0.20 16.82 ? 55   LYS A CD  1 
ATOM   95   C  CE  A LYS A 1 55  ? 89.476  47.699 82.424  0.80 21.54 ? 55   LYS A CE  1 
ATOM   96   C  CE  B LYS A 1 55  ? 88.568  45.526 83.252  0.20 19.00 ? 55   LYS A CE  1 
ATOM   97   N  NZ  A LYS A 1 55  ? 90.747  47.002 82.822  0.80 25.86 ? 55   LYS A NZ  1 
ATOM   98   N  NZ  B LYS A 1 55  ? 88.340  46.148 84.547  0.20 20.84 ? 55   LYS A NZ  1 
ATOM   99   N  N   . TYR A 1 56  ? 86.403  46.345 77.065  1.00 15.10 ? 56   TYR A N   1 
ATOM   100  C  CA  . TYR A 1 56  ? 85.619  47.154 76.131  1.00 15.57 ? 56   TYR A CA  1 
ATOM   101  C  C   . TYR A 1 56  ? 85.885  46.803 74.672  1.00 17.53 ? 56   TYR A C   1 
ATOM   102  O  O   . TYR A 1 56  ? 85.721  47.638 73.783  1.00 21.29 ? 56   TYR A O   1 
ATOM   103  C  CB  . TYR A 1 56  ? 85.815  48.659 76.370  1.00 17.11 ? 56   TYR A CB  1 
ATOM   104  C  CG  . TYR A 1 56  ? 85.985  49.039 77.826  1.00 16.59 ? 56   TYR A CG  1 
ATOM   105  C  CD1 . TYR A 1 56  ? 85.022  48.723 78.768  1.00 16.71 ? 56   TYR A CD1 1 
ATOM   106  C  CD2 . TYR A 1 56  ? 87.113  49.736 78.254  1.00 16.57 ? 56   TYR A CD2 1 
ATOM   107  C  CE1 . TYR A 1 56  ? 85.174  49.096 80.100  1.00 17.12 ? 56   TYR A CE1 1 
ATOM   108  C  CE2 . TYR A 1 56  ? 87.270  50.101 79.584  1.00 20.68 ? 56   TYR A CE2 1 
ATOM   109  C  CZ  . TYR A 1 56  ? 86.302  49.756 80.505  1.00 16.82 ? 56   TYR A CZ  1 
ATOM   110  O  OH  . TYR A 1 56  ? 86.493  50.155 81.813  1.00 19.60 ? 56   TYR A OH  1 
ATOM   111  N  N   . MET A 1 57  ? 86.264  45.560 74.406  1.00 17.23 ? 57   MET A N   1 
ATOM   112  C  CA  . MET A 1 57  ? 86.471  45.110 73.033  1.00 17.77 ? 57   MET A CA  1 
ATOM   113  C  C   . MET A 1 57  ? 85.196  44.578 72.399  1.00 17.10 ? 57   MET A C   1 
ATOM   114  O  O   . MET A 1 57  ? 85.091  44.554 71.166  1.00 21.12 ? 57   MET A O   1 
ATOM   115  C  CB  . MET A 1 57  ? 87.519  43.999 73.011  1.00 21.04 ? 57   MET A CB  1 
ATOM   116  C  CG  . MET A 1 57  ? 88.925  44.481 73.260  1.00 24.97 ? 57   MET A CG  1 
ATOM   117  S  SD  . MET A 1 57  ? 90.126  43.316 72.606  1.00 29.91 ? 57   MET A SD  1 
ATOM   118  C  CE  . MET A 1 57  ? 90.465  44.105 71.054  1.00 35.34 ? 57   MET A CE  1 
ATOM   119  N  N   . ASP A 1 58  ? 84.230  44.163 73.209  1.00 15.27 ? 58   ASP A N   1 
ATOM   120  C  CA  . ASP A 1 58  ? 82.997  43.562 72.715  1.00 17.14 ? 58   ASP A CA  1 
ATOM   121  C  C   . ASP A 1 58  ? 81.841  44.539 72.851  1.00 18.18 ? 58   ASP A C   1 
ATOM   122  O  O   . ASP A 1 58  ? 81.640  45.127 73.915  1.00 17.37 ? 58   ASP A O   1 
ATOM   123  C  CB  . ASP A 1 58  ? 82.684  42.297 73.517  1.00 15.59 ? 58   ASP A CB  1 
ATOM   124  C  CG  . ASP A 1 58  ? 83.657  41.191 73.242  1.00 19.12 ? 58   ASP A CG  1 
ATOM   125  O  OD1 . ASP A 1 58  ? 83.451  40.465 72.253  1.00 22.89 ? 58   ASP A OD1 1 
ATOM   126  O  OD2 . ASP A 1 58  ? 84.668  41.071 73.971  1.00 17.37 ? 58   ASP A OD2 1 
ATOM   127  N  N   . GLU A 1 59  ? 81.077  44.696 71.772  1.00 16.78 ? 59   GLU A N   1 
ATOM   128  C  CA  . GLU A 1 59  ? 79.822  45.436 71.822  1.00 15.37 ? 59   GLU A CA  1 
ATOM   129  C  C   . GLU A 1 59  ? 78.773  44.553 72.492  1.00 17.31 ? 59   GLU A C   1 
ATOM   130  O  O   . GLU A 1 59  ? 78.564  43.402 72.092  1.00 17.19 ? 59   GLU A O   1 
ATOM   131  C  CB  . GLU A 1 59  ? 79.386  45.775 70.396  1.00 15.36 ? 59   GLU A CB  1 
ATOM   132  C  CG  . GLU A 1 59  ? 78.053  46.552 70.307  1.00 18.26 ? 59   GLU A CG  1 
ATOM   133  C  CD  . GLU A 1 59  ? 78.184  48.034 70.659  1.00 18.42 ? 59   GLU A CD  1 
ATOM   134  O  OE1 . GLU A 1 59  ? 79.304  48.572 70.648  1.00 21.48 ? 59   GLU A OE1 1 
ATOM   135  O  OE2 . GLU A 1 59  ? 77.153  48.681 70.936  1.00 21.71 ? 59   GLU A OE2 1 
ATOM   136  N  N   . LEU A 1 60  ? 78.132  45.089 73.529  1.00 14.53 ? 60   LEU A N   1 
ATOM   137  C  CA  . LEU A 1 60  ? 77.103  44.371 74.269  1.00 13.66 ? 60   LEU A CA  1 
ATOM   138  C  C   . LEU A 1 60  ? 76.083  43.749 73.315  1.00 13.73 ? 60   LEU A C   1 
ATOM   139  O  O   . LEU A 1 60  ? 75.477  44.474 72.513  1.00 15.70 ? 60   LEU A O   1 
ATOM   140  C  CB  . LEU A 1 60  ? 76.382  45.368 75.170  1.00 14.20 ? 60   LEU A CB  1 
ATOM   141  C  CG  . LEU A 1 60  ? 75.229  44.745 75.968  1.00 13.58 ? 60   LEU A CG  1 
ATOM   142  C  CD1 . LEU A 1 60  ? 75.767  44.213 77.302  1.00 16.56 ? 60   LEU A CD1 1 
ATOM   143  C  CD2 . LEU A 1 60  ? 74.154  45.779 76.206  1.00 17.15 ? 60   LEU A CD2 1 
ATOM   144  N  N   . PRO A 1 61  ? 75.843  42.439 73.394  1.00 14.84 ? 61   PRO A N   1 
ATOM   145  C  CA  . PRO A 1 61  ? 74.814  41.814 72.546  1.00 16.15 ? 61   PRO A CA  1 
ATOM   146  C  C   . PRO A 1 61  ? 73.449  41.910 73.203  1.00 14.22 ? 61   PRO A C   1 
ATOM   147  O  O   . PRO A 1 61  ? 73.318  41.949 74.424  1.00 15.43 ? 61   PRO A O   1 
ATOM   148  C  CB  . PRO A 1 61  ? 75.230  40.339 72.497  1.00 19.94 ? 61   PRO A CB  1 
ATOM   149  C  CG  . PRO A 1 61  ? 76.373  40.160 73.458  1.00 21.59 ? 61   PRO A CG  1 
ATOM   150  C  CD  . PRO A 1 61  ? 76.659  41.465 74.135  1.00 15.66 ? 61   PRO A CD  1 
ATOM   151  N  N   . ILE A 1 62  ? 72.418  41.924 72.365  1.00 15.25 ? 62   ILE A N   1 
ATOM   152  C  CA  . ILE A 1 62  ? 71.026  41.895 72.818  1.00 14.21 ? 62   ILE A CA  1 
ATOM   153  C  C   . ILE A 1 62  ? 70.495  40.490 72.563  1.00 13.97 ? 62   ILE A C   1 
ATOM   154  O  O   . ILE A 1 62  ? 70.472  40.059 71.401  1.00 15.47 ? 62   ILE A O   1 
ATOM   155  C  CB  . ILE A 1 62  ? 70.172  42.911 72.052  1.00 17.58 ? 62   ILE A CB  1 
ATOM   156  C  CG1 . ILE A 1 62  ? 70.845  44.276 72.023  1.00 22.17 ? 62   ILE A CG1 1 
ATOM   157  C  CG2 . ILE A 1 62  ? 68.746  42.915 72.616  1.00 17.99 ? 62   ILE A CG2 1 
ATOM   158  C  CD1 . ILE A 1 62  ? 70.860  44.927 73.344  1.00 24.30 ? 62   ILE A CD1 1 
ATOM   159  N  N   . PRO A 1 63  ? 70.062  39.757 73.580  1.00 13.39 ? 63   PRO A N   1 
ATOM   160  C  CA  . PRO A 1 63  ? 69.550  38.416 73.326  1.00 13.24 ? 63   PRO A CA  1 
ATOM   161  C  C   . PRO A 1 63  ? 68.366  38.478 72.380  1.00 13.84 ? 63   PRO A C   1 
ATOM   162  O  O   . PRO A 1 63  ? 67.534  39.395 72.459  1.00 16.50 ? 63   PRO A O   1 
ATOM   163  C  CB  . PRO A 1 63  ? 69.123  37.921 74.720  1.00 14.87 ? 63   PRO A CB  1 
ATOM   164  C  CG  . PRO A 1 63  ? 69.900  38.780 75.682  1.00 15.45 ? 63   PRO A CG  1 
ATOM   165  C  CD  . PRO A 1 63  ? 70.127  40.094 75.019  1.00 13.52 ? 63   PRO A CD  1 
ATOM   166  N  N   . PRO A 1 64  ? 68.253  37.518 71.475  1.00 14.76 ? 64   PRO A N   1 
ATOM   167  C  CA  . PRO A 1 64  ? 67.112  37.516 70.561  1.00 16.21 ? 64   PRO A CA  1 
ATOM   168  C  C   . PRO A 1 64  ? 65.848  37.169 71.312  1.00 15.53 ? 64   PRO A C   1 
ATOM   169  O  O   . PRO A 1 64  ? 65.884  36.584 72.392  1.00 16.75 ? 64   PRO A O   1 
ATOM   170  C  CB  . PRO A 1 64  ? 67.468  36.433 69.542  1.00 20.14 ? 64   PRO A CB  1 
ATOM   171  C  CG  . PRO A 1 64  ? 68.402  35.539 70.231  1.00 21.83 ? 64   PRO A CG  1 
ATOM   172  C  CD  . PRO A 1 64  ? 69.178  36.397 71.222  1.00 16.35 ? 64   PRO A CD  1 
ATOM   173  N  N   . VAL A 1 65  ? 64.720  37.557 70.731  1.00 15.59 ? 65   VAL A N   1 
ATOM   174  C  CA  . VAL A 1 65  ? 63.415  37.275 71.317  1.00 15.15 ? 65   VAL A CA  1 
ATOM   175  C  C   . VAL A 1 65  ? 62.960  35.879 70.907  1.00 17.66 ? 65   VAL A C   1 
ATOM   176  O  O   . VAL A 1 65  ? 63.024  35.509 69.729  1.00 19.36 ? 65   VAL A O   1 
ATOM   177  C  CB  . VAL A 1 65  ? 62.403  38.348 70.890  1.00 19.82 ? 65   VAL A CB  1 
ATOM   178  C  CG1 . VAL A 1 65  ? 60.998  37.992 71.367  1.00 18.64 ? 65   VAL A CG1 1 
ATOM   179  C  CG2 . VAL A 1 65  ? 62.830  39.715 71.437  1.00 22.43 ? 65   VAL A CG2 1 
ATOM   180  N  N   . ALA A 1 66  ? 62.513  35.088 71.881  1.00 17.16 ? 66   ALA A N   1 
ATOM   181  C  CA  . ALA A 1 66  ? 61.993  33.759 71.584  1.00 15.96 ? 66   ALA A CA  1 
ATOM   182  C  C   . ALA A 1 66  ? 60.740  33.861 70.726  1.00 17.29 ? 66   ALA A C   1 
ATOM   183  O  O   . ALA A 1 66  ? 59.908  34.750 70.915  1.00 18.54 ? 66   ALA A O   1 
ATOM   184  C  CB  . ALA A 1 66  ? 61.648  33.042 72.893  1.00 17.25 ? 66   ALA A CB  1 
ATOM   185  N  N   . ARG A 1 67  ? 60.614  32.935 69.775  1.00 18.69 ? 67   ARG A N   1 
ATOM   186  C  CA  . ARG A 1 67  ? 59.460  32.890 68.895  1.00 19.73 ? 67   ARG A CA  1 
ATOM   187  C  C   . ARG A 1 67  ? 58.682  31.618 69.149  1.00 19.57 ? 67   ARG A C   1 
ATOM   188  O  O   . ARG A 1 67  ? 59.278  30.534 69.220  1.00 23.03 ? 67   ARG A O   1 
ATOM   189  C  CB  . ARG A 1 67  ? 59.917  32.923 67.433  1.00 23.31 ? 67   ARG A CB  1 
ATOM   190  C  CG  . ARG A 1 67  ? 60.662  34.187 67.044  1.00 26.65 ? 67   ARG A CG  1 
ATOM   191  C  CD  . ARG A 1 67  ? 60.978  34.190 65.547  1.00 37.28 ? 67   ARG A CD  1 
ATOM   192  N  NE  . ARG A 1 67  ? 62.365  34.573 65.299  1.00 53.00 ? 67   ARG A NE  1 
ATOM   193  C  CZ  . ARG A 1 67  ? 63.408  33.758 65.409  1.00 57.06 ? 67   ARG A CZ  1 
ATOM   194  N  NH1 . ARG A 1 67  ? 63.266  32.494 65.790  1.00 52.33 ? 67   ARG A NH1 1 
ATOM   195  N  NH2 . ARG A 1 67  ? 64.629  34.226 65.154  1.00 52.00 ? 67   ARG A NH2 1 
ATOM   196  N  N   . PRO A 1 68  ? 57.366  31.710 69.288  1.00 20.04 ? 68   PRO A N   1 
ATOM   197  C  CA  . PRO A 1 68  ? 56.572  30.507 69.526  1.00 19.40 ? 68   PRO A CA  1 
ATOM   198  C  C   . PRO A 1 68  ? 56.567  29.603 68.309  1.00 23.81 ? 68   PRO A C   1 
ATOM   199  O  O   . PRO A 1 68  ? 56.696  30.052 67.167  1.00 25.88 ? 68   PRO A O   1 
ATOM   200  C  CB  . PRO A 1 68  ? 55.175  31.053 69.838  1.00 26.63 ? 68   PRO A CB  1 
ATOM   201  C  CG  . PRO A 1 68  ? 55.132  32.385 69.200  1.00 25.57 ? 68   PRO A CG  1 
ATOM   202  C  CD  . PRO A 1 68  ? 56.540  32.929 69.252  1.00 21.37 ? 68   PRO A CD  1 
ATOM   203  N  N   . LEU A 1 69  ? 56.425  28.307 68.574  1.00 22.27 ? 69   LEU A N   1 
ATOM   204  C  CA  . LEU A 1 69  ? 56.291  27.324 67.514  1.00 30.19 ? 69   LEU A CA  1 
ATOM   205  C  C   . LEU A 1 69  ? 54.851  27.156 67.083  1.00 27.96 ? 69   LEU A C   1 
ATOM   206  O  O   . LEU A 1 69  ? 54.599  26.772 65.932  1.00 31.99 ? 69   LEU A O   1 
ATOM   207  C  CB  . LEU A 1 69  ? 56.789  25.960 68.001  1.00 33.18 ? 69   LEU A CB  1 
ATOM   208  C  CG  . LEU A 1 69  ? 58.293  25.723 68.120  1.00 37.49 ? 69   LEU A CG  1 
ATOM   209  C  CD1 . LEU A 1 69  ? 58.551  24.218 68.071  1.00 44.51 ? 69   LEU A CD1 1 
ATOM   210  C  CD2 . LEU A 1 69  ? 59.091  26.462 67.050  1.00 44.79 ? 69   LEU A CD2 1 
ATOM   211  N  N   . ALA A 1 70  ? 53.888  27.406 67.975  1.00 26.62 ? 70   ALA A N   1 
ATOM   212  C  CA  . ALA A 1 70  ? 52.488  27.271 67.570  1.00 30.54 ? 70   ALA A CA  1 
ATOM   213  C  C   . ALA A 1 70  ? 51.649  28.278 68.344  1.00 26.48 ? 70   ALA A C   1 
ATOM   214  O  O   . ALA A 1 70  ? 52.145  28.960 69.239  1.00 24.27 ? 70   ALA A O   1 
ATOM   215  C  CB  . ALA A 1 70  ? 51.977  25.837 67.754  1.00 29.42 ? 70   ALA A CB  1 
ATOM   216  N  N   . GLU A 1 71  ? 50.371  28.376 67.981  1.00 30.37 ? 71   GLU A N   1 
ATOM   217  C  CA  . GLU A 1 71  ? 49.391  29.141 68.748  1.00 30.48 ? 71   GLU A CA  1 
ATOM   218  C  C   . GLU A 1 71  ? 48.092  28.350 68.763  1.00 28.31 ? 71   GLU A C   1 
ATOM   219  O  O   . GLU A 1 71  ? 47.503  28.096 67.706  1.00 32.62 ? 71   GLU A O   1 
ATOM   220  C  CB  . GLU A 1 71  ? 49.162  30.536 68.148  1.00 35.18 ? 71   GLU A CB  1 
ATOM   221  N  N   . ILE A 1 72  ? 47.638  27.961 69.954  1.00 32.85 ? 72   ILE A N   1 
ATOM   222  C  CA  . ILE A 1 72  ? 46.445  27.130 70.123  1.00 33.38 ? 72   ILE A CA  1 
ATOM   223  C  C   . ILE A 1 72  ? 45.349  27.957 70.778  1.00 31.64 ? 72   ILE A C   1 
ATOM   224  O  O   . ILE A 1 72  ? 45.478  28.350 71.944  1.00 35.53 ? 72   ILE A O   1 
ATOM   225  C  CB  . ILE A 1 72  ? 46.732  25.873 70.966  1.00 36.58 ? 72   ILE A CB  1 
ATOM   226  C  CG1 . ILE A 1 72  ? 47.990  25.144 70.478  1.00 36.11 ? 72   ILE A CG1 1 
ATOM   227  C  CG2 . ILE A 1 72  ? 45.514  24.960 70.986  1.00 34.87 ? 72   ILE A CG2 1 
ATOM   228  C  CD1 . ILE A 1 72  ? 47.980  24.820 68.978  1.00 39.05 ? 72   ILE A CD1 1 
ATOM   229  N  N   . LYS A 1 73  ? 44.251  28.180 70.050  1.00 30.79 ? 73   LYS A N   1 
ATOM   230  C  CA  . LYS A 1 73  ? 43.138  28.982 70.560  1.00 33.52 ? 73   LYS A CA  1 
ATOM   231  C  C   . LYS A 1 73  ? 43.641  30.307 71.131  1.00 30.24 ? 73   LYS A C   1 
ATOM   232  O  O   . LYS A 1 73  ? 43.216  30.750 72.200  1.00 37.53 ? 73   LYS A O   1 
ATOM   233  C  CB  . LYS A 1 73  ? 42.295  28.210 71.581  1.00 40.10 ? 73   LYS A CB  1 
ATOM   234  C  CG  . LYS A 1 73  ? 41.994  26.763 71.203  1.00 43.36 ? 73   LYS A CG  1 
ATOM   235  C  CD  . LYS A 1 73  ? 40.835  26.688 70.235  1.00 41.32 ? 73   LYS A CD  1 
ATOM   236  C  CE  . LYS A 1 73  ? 40.341  25.256 70.031  1.00 37.61 ? 73   LYS A CE  1 
ATOM   237  N  NZ  . LYS A 1 73  ? 39.630  25.143 68.726  1.00 40.96 ? 73   LYS A NZ  1 
ATOM   238  N  N   . GLY A 1 74  ? 44.573  30.930 70.416  1.00 33.70 ? 74   GLY A N   1 
ATOM   239  C  CA  . GLY A 1 74  ? 45.146  32.197 70.818  1.00 32.25 ? 74   GLY A CA  1 
ATOM   240  C  C   . GLY A 1 74  ? 46.283  32.137 71.821  1.00 32.29 ? 74   GLY A C   1 
ATOM   241  O  O   . GLY A 1 74  ? 46.827  33.194 72.167  1.00 35.50 ? 74   GLY A O   1 
ATOM   242  N  N   . SER A 1 75  ? 46.685  30.948 72.294  1.00 29.43 ? 75   SER A N   1 
ATOM   243  C  CA  . SER A 1 75  ? 47.769  30.853 73.273  1.00 25.75 ? 75   SER A CA  1 
ATOM   244  C  C   . SER A 1 75  ? 49.064  30.434 72.597  1.00 23.72 ? 75   SER A C   1 
ATOM   245  O  O   . SER A 1 75  ? 49.129  29.336 72.027  1.00 26.15 ? 75   SER A O   1 
ATOM   246  C  CB  . SER A 1 75  ? 47.433  29.860 74.380  1.00 27.89 ? 75   SER A CB  1 
ATOM   247  O  OG  . SER A 1 75  ? 46.333  30.296 75.152  1.00 38.27 ? 75   SER A OG  1 
ATOM   248  N  N   . PRO A 1 76  ? 50.112  31.241 72.669  1.00 22.19 ? 76   PRO A N   1 
ATOM   249  C  CA  . PRO A 1 76  ? 51.411  30.834 72.118  1.00 21.84 ? 76   PRO A CA  1 
ATOM   250  C  C   . PRO A 1 76  ? 51.989  29.609 72.823  1.00 23.76 ? 76   PRO A C   1 
ATOM   251  O  O   . PRO A 1 76  ? 51.826  29.424 74.036  1.00 20.78 ? 76   PRO A O   1 
ATOM   252  C  CB  . PRO A 1 76  ? 52.297  32.063 72.377  1.00 23.24 ? 76   PRO A CB  1 
ATOM   253  C  CG  . PRO A 1 76  ? 51.322  33.206 72.542  1.00 26.77 ? 76   PRO A CG  1 
ATOM   254  C  CD  . PRO A 1 76  ? 50.145  32.595 73.239  1.00 24.40 ? 76   PRO A CD  1 
ATOM   255  N  N   . TYR A 1 77  ? 52.677  28.768 72.036  1.00 19.46 ? 77   TYR A N   1 
ATOM   256  C  CA  . TYR A 1 77  ? 53.376  27.580 72.518  1.00 18.55 ? 77   TYR A CA  1 
ATOM   257  C  C   . TYR A 1 77  ? 54.835  27.691 72.104  1.00 17.39 ? 77   TYR A C   1 
ATOM   258  O  O   . TYR A 1 77  ? 55.138  27.851 70.903  1.00 20.68 ? 77   TYR A O   1 
ATOM   259  C  CB  . TYR A 1 77  ? 52.747  26.299 71.945  1.00 20.55 ? 77   TYR A CB  1 
ATOM   260  C  CG  . TYR A 1 77  ? 53.617  25.055 72.118  1.00 20.92 ? 77   TYR A CG  1 
ATOM   261  C  CD1 . TYR A 1 77  ? 53.660  24.368 73.327  1.00 19.67 ? 77   TYR A CD1 1 
ATOM   262  C  CD2 . TYR A 1 77  ? 54.424  24.595 71.074  1.00 26.15 ? 77   TYR A CD2 1 
ATOM   263  C  CE1 . TYR A 1 77  ? 54.476  23.250 73.492  1.00 21.02 ? 77   TYR A CE1 1 
ATOM   264  C  CE2 . TYR A 1 77  ? 55.234  23.474 71.225  1.00 27.29 ? 77   TYR A CE2 1 
ATOM   265  C  CZ  . TYR A 1 77  ? 55.240  22.795 72.430  1.00 23.36 ? 77   TYR A CZ  1 
ATOM   266  O  OH  . TYR A 1 77  ? 56.057  21.684 72.594  1.00 24.69 ? 77   TYR A OH  1 
ATOM   267  N  N   . TYR A 1 78  ? 55.720  27.629 73.103  1.00 17.62 ? 78   TYR A N   1 
ATOM   268  C  CA  . TYR A 1 78  ? 57.166  27.688 72.946  1.00 15.36 ? 78   TYR A CA  1 
ATOM   269  C  C   . TYR A 1 78  ? 57.776  26.336 73.305  1.00 19.40 ? 78   TYR A C   1 
ATOM   270  O  O   . TYR A 1 78  ? 57.275  25.601 74.168  1.00 18.17 ? 78   TYR A O   1 
ATOM   271  C  CB  . TYR A 1 78  ? 57.788  28.727 73.881  1.00 18.32 ? 78   TYR A CB  1 
ATOM   272  C  CG  . TYR A 1 78  ? 57.402  30.161 73.595  1.00 17.07 ? 78   TYR A CG  1 
ATOM   273  C  CD1 . TYR A 1 78  ? 56.220  30.706 74.104  1.00 19.69 ? 78   TYR A CD1 1 
ATOM   274  C  CD2 . TYR A 1 78  ? 58.234  30.976 72.822  1.00 18.24 ? 78   TYR A CD2 1 
ATOM   275  C  CE1 . TYR A 1 78  ? 55.878  32.029 73.854  1.00 18.20 ? 78   TYR A CE1 1 
ATOM   276  C  CE2 . TYR A 1 78  ? 57.905  32.284 72.562  1.00 17.55 ? 78   TYR A CE2 1 
ATOM   277  C  CZ  . TYR A 1 78  ? 56.733  32.810 73.083  1.00 17.71 ? 78   TYR A CZ  1 
ATOM   278  O  OH  . TYR A 1 78  ? 56.438  34.129 72.799  1.00 18.95 ? 78   TYR A OH  1 
ATOM   279  N  N   . GLU A 1 79  ? 58.885  26.031 72.650  1.00 19.13 ? 79   GLU A N   1 
ATOM   280  C  CA  . GLU A 1 79  ? 59.680  24.848 72.935  1.00 18.94 ? 79   GLU A CA  1 
ATOM   281  C  C   . GLU A 1 79  ? 61.127  25.293 73.014  1.00 16.58 ? 79   GLU A C   1 
ATOM   282  O  O   . GLU A 1 79  ? 61.682  25.778 72.019  1.00 19.64 ? 79   GLU A O   1 
ATOM   283  C  CB  . GLU A 1 79  ? 59.532  23.831 71.814  1.00 23.73 ? 79   GLU A CB  1 
ATOM   284  C  CG  . GLU A 1 79  ? 59.746  22.412 72.245  1.00 28.79 ? 79   GLU A CG  1 
ATOM   285  C  CD  . GLU A 1 79  ? 59.300  21.413 71.186  1.00 27.03 ? 79   GLU A CD  1 
ATOM   286  O  OE1 . GLU A 1 79  ? 58.088  21.307 70.890  1.00 26.15 ? 79   GLU A OE1 1 
ATOM   287  O  OE2 . GLU A 1 79  ? 60.203  20.780 70.601  1.00 33.58 ? 79   GLU A OE2 1 
ATOM   288  N  N   . ILE A 1 80  ? 61.730  25.158 74.186  1.00 16.80 ? 80   ILE A N   1 
ATOM   289  C  CA  . ILE A 1 80  ? 63.055  25.703 74.455  1.00 16.89 ? 80   ILE A CA  1 
ATOM   290  C  C   . ILE A 1 80  ? 63.913  24.583 75.017  1.00 17.34 ? 80   ILE A C   1 
ATOM   291  O  O   . ILE A 1 80  ? 63.572  24.000 76.052  1.00 18.30 ? 80   ILE A O   1 
ATOM   292  C  CB  . ILE A 1 80  ? 62.993  26.900 75.417  1.00 15.95 ? 80   ILE A CB  1 
ATOM   293  C  CG1 . ILE A 1 80  ? 62.250  28.058 74.738  1.00 21.68 ? 80   ILE A CG1 1 
ATOM   294  C  CG2 . ILE A 1 80  ? 64.414  27.331 75.866  1.00 15.82 ? 80   ILE A CG2 1 
ATOM   295  C  CD1 . ILE A 1 80  ? 61.952  29.224 75.645  1.00 20.45 ? 80   ILE A CD1 1 
ATOM   296  N  N   . ALA A 1 81  ? 64.997  24.258 74.316  1.00 17.62 ? 81   ALA A N   1 
ATOM   297  C  CA  . ALA A 1 81  ? 65.844  23.113 74.630  1.00 16.14 ? 81   ALA A CA  1 
ATOM   298  C  C   . ALA A 1 81  ? 67.160  23.576 75.235  1.00 15.92 ? 81   ALA A C   1 
ATOM   299  O  O   . ALA A 1 81  ? 67.844  24.441 74.674  1.00 18.38 ? 81   ALA A O   1 
ATOM   300  C  CB  . ALA A 1 81  ? 66.145  22.290 73.372  1.00 19.23 ? 81   ALA A CB  1 
ATOM   301  N  N   . MET A 1 82  ? 67.530  22.959 76.346  1.00 14.73 ? 82   MET A N   1 
ATOM   302  C  CA  . MET A 1 82  ? 68.814  23.192 76.983  1.00 15.21 ? 82   MET A CA  1 
ATOM   303  C  C   . MET A 1 82  ? 69.879  22.375 76.271  1.00 16.35 ? 82   MET A C   1 
ATOM   304  O  O   . MET A 1 82  ? 69.767  21.146 76.205  1.00 15.68 ? 82   MET A O   1 
ATOM   305  C  CB  . MET A 1 82  ? 68.716  22.727 78.430  1.00 16.69 ? 82   MET A CB  1 
ATOM   306  C  CG  . MET A 1 82  ? 67.677  23.468 79.240  1.00 15.45 ? 82   MET A CG  1 
ATOM   307  S  SD  . MET A 1 82  ? 67.314  22.592 80.776  1.00 16.72 ? 82   MET A SD  1 
ATOM   308  C  CE  . MET A 1 82  ? 65.539  22.427 80.757  1.00 16.68 ? 82   MET A CE  1 
ATOM   309  N  N   . ARG A 1 83  ? 70.905  23.049 75.728  1.00 15.11 ? 83   ARG A N   1 
ATOM   310  C  CA  . ARG A 1 83  ? 71.910  22.388 74.906  1.00 17.47 ? 83   ARG A CA  1 
ATOM   311  C  C   . ARG A 1 83  ? 73.308  22.844 75.305  1.00 15.51 ? 83   ARG A C   1 
ATOM   312  O  O   . ARG A 1 83  ? 73.518  23.994 75.684  1.00 15.17 ? 83   ARG A O   1 
ATOM   313  C  CB  . ARG A 1 83  ? 71.705  22.706 73.419  1.00 18.70 ? 83   ARG A CB  1 
ATOM   314  C  CG  . ARG A 1 83  ? 70.361  22.272 72.876  1.00 21.84 ? 83   ARG A CG  1 
ATOM   315  C  CD  . ARG A 1 83  ? 70.309  22.455 71.361  1.00 25.47 ? 83   ARG A CD  1 
ATOM   316  N  NE  . ARG A 1 83  ? 68.945  22.279 70.874  1.00 31.20 ? 83   ARG A NE  1 
ATOM   317  C  CZ  . ARG A 1 83  ? 68.392  21.096 70.639  1.00 35.91 ? 83   ARG A CZ  1 
ATOM   318  N  NH1 . ARG A 1 83  ? 69.047  19.968 70.876  1.00 34.43 ? 83   ARG A NH1 1 
ATOM   319  N  NH2 . ARG A 1 83  ? 67.148  21.040 70.163  1.00 32.22 ? 83   ARG A NH2 1 
ATOM   320  N  N   . GLN A 1 84  ? 74.272  21.934 75.189  1.00 16.01 ? 84   GLN A N   1 
ATOM   321  C  CA  . GLN A 1 84  ? 75.678  22.253 75.410  1.00 15.65 ? 84   GLN A CA  1 
ATOM   322  C  C   . GLN A 1 84  ? 76.278  22.777 74.112  1.00 16.35 ? 84   GLN A C   1 
ATOM   323  O  O   . GLN A 1 84  ? 76.230  22.092 73.080  1.00 18.61 ? 84   GLN A O   1 
ATOM   324  C  CB  . GLN A 1 84  ? 76.440  21.019 75.894  1.00 15.47 ? 84   GLN A CB  1 
ATOM   325  C  CG  . GLN A 1 84  ? 77.899  21.328 76.217  1.00 15.92 ? 84   GLN A CG  1 
ATOM   326  C  CD  . GLN A 1 84  ? 78.592  20.186 76.915  1.00 18.18 ? 84   GLN A CD  1 
ATOM   327  O  OE1 . GLN A 1 84  ? 78.337  19.940 78.097  1.00 19.47 ? 84   GLN A OE1 1 
ATOM   328  N  NE2 . GLN A 1 84  ? 79.467  19.487 76.210  1.00 19.77 ? 84   GLN A NE2 1 
ATOM   329  N  N   . VAL A 1 85  ? 76.824  23.991 74.163  1.00 15.39 ? 85   VAL A N   1 
ATOM   330  C  CA  . VAL A 1 85  ? 77.236  24.710 72.956  1.00 16.45 ? 85   VAL A CA  1 
ATOM   331  C  C   . VAL A 1 85  ? 78.475  25.533 73.260  1.00 15.12 ? 85   VAL A C   1 
ATOM   332  O  O   . VAL A 1 85  ? 78.773  25.837 74.423  1.00 15.56 ? 85   VAL A O   1 
ATOM   333  C  CB  . VAL A 1 85  ? 76.122  25.656 72.450  1.00 15.78 ? 85   VAL A CB  1 
ATOM   334  C  CG1 . VAL A 1 85  ? 74.926  24.869 71.955  1.00 17.47 ? 85   VAL A CG1 1 
ATOM   335  C  CG2 . VAL A 1 85  ? 75.687  26.622 73.539  1.00 17.05 ? 85   VAL A CG2 1 
ATOM   336  N  N   . PRO A 1 86  ? 79.183  25.970 72.225  1.00 16.09 ? 86   PRO A N   1 
ATOM   337  C  CA  . PRO A 1 86  ? 80.233  26.968 72.442  1.00 15.43 ? 86   PRO A CA  1 
ATOM   338  C  C   . PRO A 1 86  ? 79.670  28.377 72.549  1.00 15.75 ? 86   PRO A C   1 
ATOM   339  O  O   . PRO A 1 86  ? 78.687  28.739 71.900  1.00 19.67 ? 86   PRO A O   1 
ATOM   340  C  CB  . PRO A 1 86  ? 81.112  26.838 71.196  1.00 15.89 ? 86   PRO A CB  1 
ATOM   341  C  CG  . PRO A 1 86  ? 80.181  26.314 70.122  1.00 21.22 ? 86   PRO A CG  1 
ATOM   342  C  CD  . PRO A 1 86  ? 79.144  25.479 70.830  1.00 16.37 ? 86   PRO A CD  1 
ATOM   343  N  N   . HIS A 1 87  ? 80.331  29.188 73.372  1.00 15.56 ? 87   HIS A N   1 
ATOM   344  C  CA  . HIS A 1 87  ? 79.980  30.595 73.512  1.00 14.10 ? 87   HIS A CA  1 
ATOM   345  C  C   . HIS A 1 87  ? 81.282  31.335 73.757  1.00 14.45 ? 87   HIS A C   1 
ATOM   346  O  O   . HIS A 1 87  ? 82.093  30.895 74.578  1.00 16.54 ? 87   HIS A O   1 
ATOM   347  C  CB  . HIS A 1 87  ? 79.010  30.833 74.686  1.00 15.29 ? 87   HIS A CB  1 
ATOM   348  C  CG  . HIS A 1 87  ? 78.805  32.282 74.999  1.00 13.16 ? 87   HIS A CG  1 
ATOM   349  N  ND1 . HIS A 1 87  ? 77.955  33.075 74.260  1.00 15.97 ? 87   HIS A ND1 1 
ATOM   350  C  CD2 . HIS A 1 87  ? 79.365  33.090 75.932  1.00 14.41 ? 87   HIS A CD2 1 
ATOM   351  C  CE1 . HIS A 1 87  ? 77.993  34.312 74.733  1.00 15.55 ? 87   HIS A CE1 1 
ATOM   352  N  NE2 . HIS A 1 87  ? 78.840  34.348 75.750  1.00 13.55 ? 87   HIS A NE2 1 
ATOM   353  N  N   . ARG A 1 88  ? 81.484  32.458 73.076  1.00 14.64 ? 88   ARG A N   1 
ATOM   354  C  CA  . ARG A 1 88  ? 82.693  33.247 73.271  1.00 13.69 ? 88   ARG A CA  1 
ATOM   355  C  C   . ARG A 1 88  ? 82.398  34.367 74.261  1.00 16.90 ? 88   ARG A C   1 
ATOM   356  O  O   . ARG A 1 88  ? 81.525  35.210 74.013  1.00 16.88 ? 88   ARG A O   1 
ATOM   357  C  CB  . ARG A 1 88  ? 83.181  33.812 71.940  1.00 17.82 ? 88   ARG A CB  1 
ATOM   358  C  CG  . ARG A 1 88  ? 84.647  34.163 71.959  1.00 21.10 ? 88   ARG A CG  1 
ATOM   359  C  CD  . ARG A 1 88  ? 85.126  34.794 70.645  1.00 21.63 ? 88   ARG A CD  1 
ATOM   360  N  NE  . ARG A 1 88  ? 84.877  33.918 69.507  1.00 31.48 ? 88   ARG A NE  1 
ATOM   361  C  CZ  . ARG A 1 88  ? 85.659  32.916 69.127  1.00 30.42 ? 88   ARG A CZ  1 
ATOM   362  N  NH1 . ARG A 1 88  ? 86.789  32.633 69.758  1.00 30.54 ? 88   ARG A NH1 1 
ATOM   363  N  NH2 . ARG A 1 88  ? 85.316  32.196 68.064  1.00 33.62 ? 88   ARG A NH2 1 
ATOM   364  N  N   . PHE A 1 89  ? 83.112  34.378 75.384  1.00 14.23 ? 89   PHE A N   1 
ATOM   365  C  CA  . PHE A 1 89  ? 82.873  35.418 76.381  1.00 14.43 ? 89   PHE A CA  1 
ATOM   366  C  C   . PHE A 1 89  ? 83.651  36.699 76.133  1.00 16.51 ? 89   PHE A C   1 
ATOM   367  O  O   . PHE A 1 89  ? 83.371  37.701 76.797  1.00 14.86 ? 89   PHE A O   1 
ATOM   368  C  CB  . PHE A 1 89  ? 83.224  34.912 77.785  1.00 14.00 ? 89   PHE A CB  1 
ATOM   369  C  CG  . PHE A 1 89  ? 82.171  34.044 78.411  1.00 13.33 ? 89   PHE A CG  1 
ATOM   370  C  CD1 . PHE A 1 89  ? 81.101  34.591 79.113  1.00 14.94 ? 89   PHE A CD1 1 
ATOM   371  C  CD2 . PHE A 1 89  ? 82.243  32.657 78.273  1.00 13.40 ? 89   PHE A CD2 1 
ATOM   372  C  CE1 . PHE A 1 89  ? 80.129  33.760 79.707  1.00 15.29 ? 89   PHE A CE1 1 
ATOM   373  C  CE2 . PHE A 1 89  ? 81.260  31.827 78.843  1.00 14.20 ? 89   PHE A CE2 1 
ATOM   374  C  CZ  . PHE A 1 89  ? 80.219  32.383 79.575  1.00 13.82 ? 89   PHE A CZ  1 
ATOM   375  N  N   . HIS A 1 90  ? 84.633  36.684 75.241  1.00 13.39 ? 90   HIS A N   1 
ATOM   376  C  CA  . HIS A 1 90  ? 85.398  37.879 74.939  1.00 15.06 ? 90   HIS A CA  1 
ATOM   377  C  C   . HIS A 1 90  ? 85.963  37.727 73.532  1.00 15.35 ? 90   HIS A C   1 
ATOM   378  O  O   . HIS A 1 90  ? 86.281  36.615 73.097  1.00 16.97 ? 90   HIS A O   1 
ATOM   379  C  CB  . HIS A 1 90  ? 86.529  38.050 75.971  1.00 16.45 ? 90   HIS A CB  1 
ATOM   380  C  CG  . HIS A 1 90  ? 87.335  39.294 75.784  1.00 15.67 ? 90   HIS A CG  1 
ATOM   381  N  ND1 . HIS A 1 90  ? 88.395  39.361 74.905  1.00 16.91 ? 90   HIS A ND1 1 
ATOM   382  C  CD2 . HIS A 1 90  ? 87.260  40.513 76.379  1.00 15.54 ? 90   HIS A CD2 1 
ATOM   383  C  CE1 . HIS A 1 90  ? 88.921  40.573 74.948  1.00 17.71 ? 90   HIS A CE1 1 
ATOM   384  N  NE2 . HIS A 1 90  ? 88.256  41.288 75.840  1.00 17.56 ? 90   HIS A NE2 1 
ATOM   385  N  N   . ARG A 1 91  ? 86.114  38.858 72.839  1.00 16.51 ? 91   ARG A N   1 
ATOM   386  C  CA  . ARG A 1 91  ? 86.589  38.856 71.458  1.00 18.69 ? 91   ARG A CA  1 
ATOM   387  C  C   . ARG A 1 91  ? 87.870  38.046 71.282  1.00 17.56 ? 91   ARG A C   1 
ATOM   388  O  O   . ARG A 1 91  ? 88.075  37.414 70.236  1.00 20.75 ? 91   ARG A O   1 
ATOM   389  C  CB  . ARG A 1 91  ? 86.814  40.303 71.018  1.00 19.92 ? 91   ARG A CB  1 
ATOM   390  C  CG  . ARG A 1 91  ? 86.948  40.471 69.512  1.00 26.92 ? 91   ARG A CG  1 
ATOM   391  C  CD  . ARG A 1 91  ? 87.101  41.943 69.132  1.00 25.36 ? 91   ARG A CD  1 
ATOM   392  N  NE  . ARG A 1 91  ? 87.175  42.122 67.686  1.00 32.15 ? 91   ARG A NE  1 
ATOM   393  C  CZ  . ARG A 1 91  ? 86.119  42.366 66.922  1.00 32.98 ? 91   ARG A CZ  1 
ATOM   394  N  NH1 . ARG A 1 91  ? 84.904  42.444 67.435  1.00 35.58 ? 91   ARG A NH1 1 
ATOM   395  N  NH2 . ARG A 1 91  ? 86.291  42.541 65.611  1.00 36.26 ? 91   ARG A NH2 1 
ATOM   396  N  N   . LEU A 1 92  ? 88.772  38.087 72.267  1.00 17.50 ? 92   LEU A N   1 
ATOM   397  C  CA  . LEU A 1 92  ? 90.085  37.456 72.151  1.00 19.12 ? 92   LEU A CA  1 
ATOM   398  C  C   . LEU A 1 92  ? 90.188  36.129 72.900  1.00 18.26 ? 92   LEU A C   1 
ATOM   399  O  O   . LEU A 1 92  ? 91.287  35.581 73.006  1.00 21.85 ? 92   LEU A O   1 
ATOM   400  C  CB  . LEU A 1 92  ? 91.188  38.409 72.603  1.00 21.89 ? 92   LEU A CB  1 
ATOM   401  C  CG  . LEU A 1 92  ? 91.224  39.723 71.826  1.00 22.25 ? 92   LEU A CG  1 
ATOM   402  C  CD1 . LEU A 1 92  ? 92.339  40.615 72.364  1.00 23.96 ? 92   LEU A CD1 1 
ATOM   403  C  CD2 . LEU A 1 92  ? 91.456  39.427 70.351  1.00 25.86 ? 92   LEU A CD2 1 
ATOM   404  N  N   . PHE A 1 93  ? 89.091  35.624 73.445  1.00 16.94 ? 93   PHE A N   1 
ATOM   405  C  CA  . PHE A 1 93  ? 89.052  34.309 74.065  1.00 17.77 ? 93   PHE A CA  1 
ATOM   406  C  C   . PHE A 1 93  ? 88.823  33.237 73.002  1.00 16.48 ? 93   PHE A C   1 
ATOM   407  O  O   . PHE A 1 93  ? 88.214  33.500 71.956  1.00 19.92 ? 93   PHE A O   1 
ATOM   408  C  CB  . PHE A 1 93  ? 87.851  34.243 75.013  1.00 16.67 ? 93   PHE A CB  1 
ATOM   409  C  CG  . PHE A 1 93  ? 88.119  34.718 76.426  1.00 15.02 ? 93   PHE A CG  1 
ATOM   410  C  CD1 . PHE A 1 93  ? 89.095  35.662 76.720  1.00 16.46 ? 93   PHE A CD1 1 
ATOM   411  C  CD2 . PHE A 1 93  ? 87.344  34.220 77.466  1.00 16.00 ? 93   PHE A CD2 1 
ATOM   412  C  CE1 . PHE A 1 93  ? 89.294  36.078 78.042  1.00 16.26 ? 93   PHE A CE1 1 
ATOM   413  C  CE2 . PHE A 1 93  ? 87.535  34.643 78.769  1.00 17.15 ? 93   PHE A CE2 1 
ATOM   414  C  CZ  . PHE A 1 93  ? 88.518  35.572 79.060  1.00 17.17 ? 93   PHE A CZ  1 
ATOM   415  N  N   . PRO A 1 94  ? 89.237  31.998 73.264  1.00 18.54 ? 94   PRO A N   1 
ATOM   416  C  CA  . PRO A 1 94  ? 88.673  30.867 72.511  1.00 18.10 ? 94   PRO A CA  1 
ATOM   417  C  C   . PRO A 1 94  ? 87.225  30.653 72.915  1.00 19.65 ? 94   PRO A C   1 
ATOM   418  O  O   . PRO A 1 94  ? 86.767  31.205 73.928  1.00 18.23 ? 94   PRO A O   1 
ATOM   419  C  CB  . PRO A 1 94  ? 89.519  29.675 72.982  1.00 22.99 ? 94   PRO A CB  1 
ATOM   420  C  CG  . PRO A 1 94  ? 90.011  30.056 74.343  1.00 24.22 ? 94   PRO A CG  1 
ATOM   421  C  CD  . PRO A 1 94  ? 89.899  31.559 74.505  1.00 18.88 ? 94   PRO A CD  1 
ATOM   422  N  N   . PRO A 1 95  ? 86.473  29.829 72.195  1.00 18.14 ? 95   PRO A N   1 
ATOM   423  C  CA  . PRO A 1 95  ? 85.123  29.502 72.658  1.00 18.54 ? 95   PRO A CA  1 
ATOM   424  C  C   . PRO A 1 95  ? 85.164  28.722 73.965  1.00 17.51 ? 95   PRO A C   1 
ATOM   425  O  O   . PRO A 1 95  ? 86.084  27.938 74.222  1.00 19.27 ? 95   PRO A O   1 
ATOM   426  C  CB  . PRO A 1 95  ? 84.548  28.638 71.529  1.00 22.73 ? 95   PRO A CB  1 
ATOM   427  C  CG  . PRO A 1 95  ? 85.488  28.766 70.384  1.00 28.99 ? 95   PRO A CG  1 
ATOM   428  C  CD  . PRO A 1 95  ? 86.819  29.172 70.923  1.00 21.31 ? 95   PRO A CD  1 
ATOM   429  N  N   . THR A 1 96  ? 84.137  28.945 74.779  1.00 15.80 ? 96   THR A N   1 
ATOM   430  C  CA  . THR A 1 96  ? 83.930  28.266 76.059  1.00 15.35 ? 96   THR A CA  1 
ATOM   431  C  C   . THR A 1 96  ? 82.721  27.350 75.927  1.00 16.04 ? 96   THR A C   1 
ATOM   432  O  O   . THR A 1 96  ? 81.678  27.776 75.431  1.00 15.69 ? 96   THR A O   1 
ATOM   433  C  CB  . THR A 1 96  ? 83.633  29.302 77.156  1.00 14.25 ? 96   THR A CB  1 
ATOM   434  O  OG1 . THR A 1 96  ? 84.743  30.197 77.273  1.00 16.27 ? 96   THR A OG1 1 
ATOM   435  C  CG2 . THR A 1 96  ? 83.361  28.627 78.530  1.00 15.27 ? 96   THR A CG2 1 
ATOM   436  N  N   . THR A 1 97  ? 82.834  26.109 76.397  1.00 15.79 ? 97   THR A N   1 
ATOM   437  C  CA  . THR A 1 97  ? 81.654  25.251 76.424  1.00 14.54 ? 97   THR A CA  1 
ATOM   438  C  C   . THR A 1 97  ? 80.724  25.685 77.555  1.00 13.81 ? 97   THR A C   1 
ATOM   439  O  O   . THR A 1 97  ? 81.155  25.826 78.707  1.00 14.32 ? 97   THR A O   1 
ATOM   440  C  CB  . THR A 1 97  ? 82.092  23.808 76.614  1.00 15.40 ? 97   THR A CB  1 
ATOM   441  O  OG1 . THR A 1 97  ? 82.944  23.442 75.535  1.00 17.71 ? 97   THR A OG1 1 
ATOM   442  C  CG2 . THR A 1 97  ? 80.894  22.878 76.590  1.00 16.61 ? 97   THR A CG2 1 
ATOM   443  N  N   . VAL A 1 98  ? 79.449  25.916 77.217  1.00 14.47 ? 98   VAL A N   1 
ATOM   444  C  CA  . VAL A 1 98  ? 78.425  26.352 78.163  1.00 12.38 ? 98   VAL A CA  1 
ATOM   445  C  C   . VAL A 1 98  ? 77.152  25.544 77.928  1.00 13.59 ? 98   VAL A C   1 
ATOM   446  O  O   . VAL A 1 98  ? 77.035  24.778 76.964  1.00 13.38 ? 98   VAL A O   1 
ATOM   447  C  CB  . VAL A 1 98  ? 78.107  27.860 78.015  1.00 13.25 ? 98   VAL A CB  1 
ATOM   448  C  CG1 . VAL A 1 98  ? 79.368  28.699 78.181  1.00 14.20 ? 98   VAL A CG1 1 
ATOM   449  C  CG2 . VAL A 1 98  ? 77.467  28.140 76.643  1.00 14.96 ? 98   VAL A CG2 1 
ATOM   450  N  N   . TRP A 1 99  ? 76.186  25.750 78.820  1.00 13.00 ? 99   TRP A N   1 
ATOM   451  C  CA  . TRP A 1 99  ? 74.836  25.213 78.689  1.00 13.24 ? 99   TRP A CA  1 
ATOM   452  C  C   . TRP A 1 99  ? 73.897  26.385 78.463  1.00 13.35 ? 99   TRP A C   1 
ATOM   453  O  O   . TRP A 1 99  ? 73.867  27.315 79.277  1.00 14.35 ? 99   TRP A O   1 
ATOM   454  C  CB  . TRP A 1 99  ? 74.444  24.487 79.968  1.00 13.21 ? 99   TRP A CB  1 
ATOM   455  C  CG  . TRP A 1 99  ? 75.139  23.154 80.127  1.00 14.03 ? 99   TRP A CG  1 
ATOM   456  C  CD1 . TRP A 1 99  ? 75.982  22.531 79.222  1.00 15.73 ? 99   TRP A CD1 1 
ATOM   457  C  CD2 . TRP A 1 99  ? 75.006  22.263 81.231  1.00 12.46 ? 99   TRP A CD2 1 
ATOM   458  N  NE1 . TRP A 1 99  ? 76.371  21.297 79.720  1.00 15.82 ? 99   TRP A NE1 1 
ATOM   459  C  CE2 . TRP A 1 99  ? 75.787  21.113 80.948  1.00 13.98 ? 99   TRP A CE2 1 
ATOM   460  C  CE3 . TRP A 1 99  ? 74.270  22.315 82.429  1.00 14.42 ? 99   TRP A CE3 1 
ATOM   461  C  CZ2 . TRP A 1 99  ? 75.860  20.038 81.819  1.00 16.03 ? 99   TRP A CZ2 1 
ATOM   462  C  CZ3 . TRP A 1 99  ? 74.354  21.255 83.306  1.00 15.33 ? 99   TRP A CZ3 1 
ATOM   463  C  CH2 . TRP A 1 99  ? 75.153  20.126 82.997  1.00 14.39 ? 99   TRP A CH2 1 
ATOM   464  N  N   . GLY A 1 100 ? 73.165  26.362 77.358  1.00 13.14 ? 100  GLY A N   1 
ATOM   465  C  CA  . GLY A 1 100 ? 72.286  27.468 77.005  1.00 14.77 ? 100  GLY A CA  1 
ATOM   466  C  C   . GLY A 1 100 ? 70.888  27.022 76.635  1.00 13.32 ? 100  GLY A C   1 
ATOM   467  O  O   . GLY A 1 100 ? 70.702  26.021 75.938  1.00 14.61 ? 100  GLY A O   1 
ATOM   468  N  N   . TYR A 1 101 ? 69.901  27.779 77.110  1.00 13.02 ? 101  TYR A N   1 
ATOM   469  C  CA  . TYR A 1 101 ? 68.546  27.626 76.587  1.00 12.71 ? 101  TYR A CA  1 
ATOM   470  C  C   . TYR A 1 101 ? 68.526  27.993 75.108  1.00 15.16 ? 101  TYR A C   1 
ATOM   471  O  O   . TYR A 1 101 ? 69.000  29.065 74.715  1.00 14.97 ? 101  TYR A O   1 
ATOM   472  C  CB  . TYR A 1 101 ? 67.598  28.537 77.364  1.00 13.28 ? 101  TYR A CB  1 
ATOM   473  C  CG  . TYR A 1 101 ? 67.425  28.187 78.829  1.00 12.21 ? 101  TYR A CG  1 
ATOM   474  C  CD1 . TYR A 1 101 ? 66.788  27.015 79.223  1.00 13.79 ? 101  TYR A CD1 1 
ATOM   475  C  CD2 . TYR A 1 101 ? 67.873  29.039 79.820  1.00 13.15 ? 101  TYR A CD2 1 
ATOM   476  C  CE1 . TYR A 1 101 ? 66.604  26.710 80.568  1.00 12.50 ? 101  TYR A CE1 1 
ATOM   477  C  CE2 . TYR A 1 101 ? 67.669  28.755 81.166  1.00 12.08 ? 101  TYR A CE2 1 
ATOM   478  C  CZ  . TYR A 1 101 ? 67.067  27.567 81.536  1.00 13.81 ? 101  TYR A CZ  1 
ATOM   479  O  OH  . TYR A 1 101 ? 66.870  27.265 82.869  1.00 13.65 ? 101  TYR A OH  1 
ATOM   480  N  N   . ASP A 1 102 ? 68.016  27.075 74.281  1.00 14.33 ? 102  ASP A N   1 
ATOM   481  C  CA  . ASP A 1 102 ? 68.068  27.203 72.825  1.00 14.85 ? 102  ASP A CA  1 
ATOM   482  C  C   . ASP A 1 102 ? 69.505  27.408 72.343  1.00 16.36 ? 102  ASP A C   1 
ATOM   483  O  O   . ASP A 1 102 ? 69.754  28.055 71.316  1.00 17.54 ? 102  ASP A O   1 
ATOM   484  C  CB  . ASP A 1 102 ? 67.097  28.274 72.316  1.00 17.86 ? 102  ASP A CB  1 
ATOM   485  C  CG  . ASP A 1 102 ? 65.689  27.731 72.122  1.00 24.96 ? 102  ASP A CG  1 
ATOM   486  O  OD1 . ASP A 1 102 ? 65.504  26.489 72.212  1.00 25.52 ? 102  ASP A OD1 1 
ATOM   487  O  OD2 . ASP A 1 102 ? 64.776  28.553 71.894  1.00 28.45 ? 102  ASP A OD2 1 
ATOM   488  N  N   . GLY A 1 103 ? 70.470  26.856 73.087  1.00 15.46 ? 103  GLY A N   1 
ATOM   489  C  CA  . GLY A 1 103 ? 71.859  26.936 72.674  1.00 16.86 ? 103  GLY A CA  1 
ATOM   490  C  C   . GLY A 1 103 ? 72.426  28.336 72.627  1.00 16.78 ? 103  GLY A C   1 
ATOM   491  O  O   . GLY A 1 103 ? 73.333  28.595 71.823  1.00 18.57 ? 103  GLY A O   1 
ATOM   492  N  N   . MET A 1 104 ? 71.944  29.245 73.478  1.00 16.05 ? 104  MET A N   1 
ATOM   493  C  CA  . MET A 1 104 ? 72.487  30.596 73.510  1.00 17.15 ? 104  MET A CA  1 
ATOM   494  C  C   . MET A 1 104 ? 72.580  31.109 74.939  1.00 14.23 ? 104  MET A C   1 
ATOM   495  O  O   . MET A 1 104 ? 71.904  30.609 75.837  1.00 14.23 ? 104  MET A O   1 
ATOM   496  C  CB  . MET A 1 104 ? 71.677  31.462 72.578  1.00 18.31 ? 104  MET A CB  1 
ATOM   497  C  CG  . MET A 1 104 ? 70.324  31.758 73.152  1.00 15.85 ? 104  MET A CG  1 
ATOM   498  S  SD  . MET A 1 104 ? 69.348  32.762 71.974  1.00 20.49 ? 104  MET A SD  1 
ATOM   499  C  CE  . MET A 1 104 ? 69.082  31.624 70.608  1.00 23.15 ? 104  MET A CE  1 
ATOM   500  N  N   . LEU A 1 105 ? 73.489  32.064 75.147  1.00 13.82 ? 105  LEU A N   1 
ATOM   501  C  CA  . LEU A 1 105 ? 73.799  32.575 76.472  1.00 13.49 ? 105  LEU A CA  1 
ATOM   502  C  C   . LEU A 1 105 ? 73.868  34.088 76.315  1.00 12.78 ? 105  LEU A C   1 
ATOM   503  O  O   . LEU A 1 105 ? 74.734  34.592 75.560  1.00 14.19 ? 105  LEU A O   1 
ATOM   504  C  CB  . LEU A 1 105 ? 75.155  32.009 76.903  1.00 13.54 ? 105  LEU A CB  1 
ATOM   505  C  CG  . LEU A 1 105 ? 75.573  32.286 78.349  1.00 11.98 ? 105  LEU A CG  1 
ATOM   506  C  CD1 . LEU A 1 105 ? 76.654  31.302 78.759  1.00 15.03 ? 105  LEU A CD1 1 
ATOM   507  C  CD2 . LEU A 1 105 ? 76.102  33.700 78.531  1.00 14.62 ? 105  LEU A CD2 1 
ATOM   508  N  N   . PRO A 1 106 ? 73.020  34.856 77.009  1.00 11.82 ? 106  PRO A N   1 
ATOM   509  C  CA  . PRO A 1 106 ? 71.851  34.413 77.785  1.00 12.45 ? 106  PRO A CA  1 
ATOM   510  C  C   . PRO A 1 106 ? 70.852  33.696 76.896  1.00 12.65 ? 106  PRO A C   1 
ATOM   511  O  O   . PRO A 1 106 ? 70.890  33.761 75.657  1.00 13.18 ? 106  PRO A O   1 
ATOM   512  C  CB  . PRO A 1 106 ? 71.247  35.731 78.302  1.00 13.66 ? 106  PRO A CB  1 
ATOM   513  C  CG  . PRO A 1 106 ? 72.343  36.750 78.245  1.00 13.60 ? 106  PRO A CG  1 
ATOM   514  C  CD  . PRO A 1 106 ? 73.218  36.316 77.081  1.00 13.28 ? 106  PRO A CD  1 
ATOM   515  N  N   . GLY A 1 107 ? 69.921  32.989 77.534  1.00 12.61 ? 107  GLY A N   1 
ATOM   516  C  CA  . GLY A 1 107 ? 68.820  32.383 76.820  1.00 13.32 ? 107  GLY A CA  1 
ATOM   517  C  C   . GLY A 1 107 ? 67.987  33.441 76.117  1.00 13.86 ? 107  GLY A C   1 
ATOM   518  O  O   . GLY A 1 107 ? 68.127  34.642 76.376  1.00 14.03 ? 107  GLY A O   1 
ATOM   519  N  N   . PRO A 1 108 ? 67.138  33.032 75.178  1.00 14.28 ? 108  PRO A N   1 
ATOM   520  C  CA  . PRO A 1 108 ? 66.332  34.019 74.451  1.00 14.93 ? 108  PRO A CA  1 
ATOM   521  C  C   . PRO A 1 108 ? 65.367  34.729 75.391  1.00 13.55 ? 108  PRO A C   1 
ATOM   522  O  O   . PRO A 1 108 ? 64.889  34.161 76.372  1.00 14.59 ? 108  PRO A O   1 
ATOM   523  C  CB  . PRO A 1 108 ? 65.562  33.163 73.431  1.00 16.39 ? 108  PRO A CB  1 
ATOM   524  C  CG  . PRO A 1 108 ? 65.485  31.802 74.080  1.00 15.08 ? 108  PRO A CG  1 
ATOM   525  C  CD  . PRO A 1 108 ? 66.802  31.644 74.807  1.00 13.70 ? 108  PRO A CD  1 
ATOM   526  N  N   . THR A 1 109 ? 65.082  35.988 75.079  1.00 13.77 ? 109  THR A N   1 
ATOM   527  C  CA  . THR A 1 109 ? 64.139  36.753 75.885  1.00 13.38 ? 109  THR A CA  1 
ATOM   528  C  C   . THR A 1 109 ? 62.722  36.364 75.487  1.00 13.15 ? 109  THR A C   1 
ATOM   529  O  O   . THR A 1 109 ? 62.356  36.432 74.303  1.00 15.94 ? 109  THR A O   1 
ATOM   530  C  CB  . THR A 1 109 ? 64.359  38.240 75.624  1.00 13.79 ? 109  THR A CB  1 
ATOM   531  O  OG1 . THR A 1 109 ? 65.643  38.605 76.144  1.00 14.32 ? 109  THR A OG1 1 
ATOM   532  C  CG2 . THR A 1 109 ? 63.293  39.102 76.328  1.00 14.59 ? 109  THR A CG2 1 
ATOM   533  N  N   . ILE A 1 110 ? 61.912  35.955 76.475  1.00 13.88 ? 110  ILE A N   1 
ATOM   534  C  CA  . ILE A 1 110 ? 60.504  35.677 76.222  1.00 13.78 ? 110  ILE A CA  1 
ATOM   535  C  C   . ILE A 1 110 ? 59.707  36.929 76.537  1.00 15.78 ? 110  ILE A C   1 
ATOM   536  O  O   . ILE A 1 110 ? 59.914  37.545 77.583  1.00 15.04 ? 110  ILE A O   1 
ATOM   537  C  CB  . ILE A 1 110 ? 60.034  34.492 77.077  1.00 13.86 ? 110  ILE A CB  1 
ATOM   538  C  CG1 . ILE A 1 110 ? 60.869  33.250 76.746  1.00 15.00 ? 110  ILE A CG1 1 
ATOM   539  C  CG2 . ILE A 1 110 ? 58.535  34.270 76.894  1.00 16.84 ? 110  ILE A CG2 1 
ATOM   540  C  CD1 . ILE A 1 110 ? 60.681  32.089 77.762  1.00 17.24 ? 110  ILE A CD1 1 
ATOM   541  N  N   . LYS A 1 111 ? 58.821  37.337 75.628  1.00 15.22 ? 111  LYS A N   1 
ATOM   542  C  CA  . LYS A 1 111 ? 57.990  38.522 75.818  1.00 14.84 ? 111  LYS A CA  1 
ATOM   543  C  C   . LYS A 1 111 ? 56.521  38.142 75.793  1.00 17.04 ? 111  LYS A C   1 
ATOM   544  O  O   . LYS A 1 111 ? 56.052  37.511 74.837  1.00 18.82 ? 111  LYS A O   1 
ATOM   545  C  CB  . LYS A 1 111 ? 58.252  39.589 74.746  1.00 16.13 ? 111  LYS A CB  1 
ATOM   546  C  CG  . LYS A 1 111 ? 59.662  40.146 74.833  1.00 18.91 ? 111  LYS A CG  1 
ATOM   547  C  CD  . LYS A 1 111 ? 59.996  40.932 73.585  1.00 23.75 ? 111  LYS A CD  1 
ATOM   548  C  CE  . LYS A 1 111 ? 59.449  42.333 73.657  1.00 36.19 ? 111  LYS A CE  1 
ATOM   549  N  NZ  . LYS A 1 111 ? 60.279  43.257 72.818  1.00 40.54 ? 111  LYS A NZ  1 
ATOM   550  N  N   . VAL A 1 112 ? 55.783  38.570 76.818  1.00 16.51 ? 112  VAL A N   1 
ATOM   551  C  CA  . VAL A 1 112 ? 54.351  38.309 76.909  1.00 15.98 ? 112  VAL A CA  1 
ATOM   552  C  C   . VAL A 1 112 ? 53.649  39.579 77.348  1.00 17.09 ? 112  VAL A C   1 
ATOM   553  O  O   . VAL A 1 112 ? 54.278  40.524 77.831  1.00 18.67 ? 112  VAL A O   1 
ATOM   554  C  CB  . VAL A 1 112 ? 54.015  37.187 77.917  1.00 18.23 ? 112  VAL A CB  1 
ATOM   555  C  CG1 . VAL A 1 112 ? 54.686  35.896 77.530  1.00 17.84 ? 112  VAL A CG1 1 
ATOM   556  C  CG2 . VAL A 1 112 ? 54.421  37.593 79.340  1.00 18.43 ? 112  VAL A CG2 1 
ATOM   557  N  N   . GLN A 1 113 ? 52.339  39.604 77.151  1.00 17.96 ? 113  GLN A N   1 
ATOM   558  C  CA  . GLN A 1 113 ? 51.509  40.653 77.717  1.00 18.47 ? 113  GLN A CA  1 
ATOM   559  C  C   . GLN A 1 113 ? 50.964  40.208 79.067  1.00 18.85 ? 113  GLN A C   1 
ATOM   560  O  O   . GLN A 1 113 ? 50.788  39.014 79.324  1.00 18.16 ? 113  GLN A O   1 
ATOM   561  C  CB  . GLN A 1 113 ? 50.313  40.954 76.806  1.00 21.46 ? 113  GLN A CB  1 
ATOM   562  C  CG  . GLN A 1 113 ? 50.652  41.486 75.415  1.00 21.89 ? 113  GLN A CG  1 
ATOM   563  C  CD  . GLN A 1 113 ? 51.489  42.745 75.448  1.00 28.60 ? 113  GLN A CD  1 
ATOM   564  O  OE1 . GLN A 1 113 ? 51.046  43.780 75.934  1.00 32.39 ? 113  GLN A OE1 1 
ATOM   565  N  NE2 . GLN A 1 113 ? 52.705  42.661 74.929  1.00 34.62 ? 113  GLN A NE2 1 
ATOM   566  N  N   . LYS A 1 114 ? 50.656  41.192 79.919  1.00 18.33 ? 114  LYS A N   1 
ATOM   567  C  CA  . LYS A 1 114 ? 49.928  40.878 81.137  1.00 18.87 ? 114  LYS A CA  1 
ATOM   568  C  C   . LYS A 1 114 ? 48.670  40.106 80.778  1.00 18.51 ? 114  LYS A C   1 
ATOM   569  O  O   . LYS A 1 114 ? 47.942  40.476 79.851  1.00 20.30 ? 114  LYS A O   1 
ATOM   570  C  CB  . LYS A 1 114 ? 49.542  42.168 81.854  1.00 17.49 ? 114  LYS A CB  1 
ATOM   571  C  CG  . LYS A 1 114 ? 48.693  41.908 83.085  1.00 20.09 ? 114  LYS A CG  1 
ATOM   572  C  CD  . LYS A 1 114 ? 48.298  43.191 83.763  1.00 22.13 ? 114  LYS A CD  1 
ATOM   573  C  CE  . LYS A 1 114 ? 47.551  42.878 85.048  1.00 26.84 ? 114  LYS A CE  1 
ATOM   574  N  NZ  . LYS A 1 114 ? 47.064  44.120 85.715  1.00 35.39 ? 114  LYS A NZ  1 
ATOM   575  N  N   . ASP A 1 115 ? 48.429  39.022 81.515  1.00 18.63 ? 115  ASP A N   1 
ATOM   576  C  CA  . ASP A 1 115 ? 47.242  38.175 81.388  1.00 19.08 ? 115  ASP A CA  1 
ATOM   577  C  C   . ASP A 1 115 ? 47.251  37.301 80.134  1.00 21.12 ? 115  ASP A C   1 
ATOM   578  O  O   . ASP A 1 115 ? 46.251  36.616 79.862  1.00 24.63 ? 115  ASP A O   1 
ATOM   579  C  CB  . ASP A 1 115 ? 45.948  38.997 81.411  1.00 22.28 ? 115  ASP A CB  1 
ATOM   580  C  CG  . ASP A 1 115 ? 45.608  39.560 82.776  1.00 22.49 ? 115  ASP A CG  1 
ATOM   581  O  OD1 . ASP A 1 115 ? 46.272  39.250 83.777  1.00 25.30 ? 115  ASP A OD1 1 
ATOM   582  O  OD2 . ASP A 1 115 ? 44.691  40.415 82.833  1.00 31.98 ? 115  ASP A OD2 1 
ATOM   583  N  N   . GLU A 1 116 ? 48.344  37.277 79.370  1.00 20.30 ? 116  GLU A N   1 
ATOM   584  C  CA  . GLU A 1 116 ? 48.427  36.452 78.168  1.00 22.29 ? 116  GLU A CA  1 
ATOM   585  C  C   . GLU A 1 116 ? 48.976  35.086 78.566  1.00 21.44 ? 116  GLU A C   1 
ATOM   586  O  O   . GLU A 1 116 ? 50.135  34.968 78.962  1.00 20.59 ? 116  GLU A O   1 
ATOM   587  C  CB  . GLU A 1 116 ? 49.301  37.123 77.111  1.00 23.93 ? 116  GLU A CB  1 
ATOM   588  C  CG  . GLU A 1 116 ? 49.664  36.204 75.955  1.00 23.63 ? 116  GLU A CG  1 
ATOM   589  C  CD  . GLU A 1 116 ? 50.520  36.886 74.913  1.00 27.77 ? 116  GLU A CD  1 
ATOM   590  O  OE1 . GLU A 1 116 ? 51.389  37.702 75.295  1.00 22.66 ? 116  GLU A OE1 1 
ATOM   591  O  OE2 . GLU A 1 116 ? 50.357  36.564 73.719  1.00 29.23 ? 116  GLU A OE2 1 
ATOM   592  N  N   . LYS A 1 117 ? 48.150  34.055 78.469  1.00 20.16 ? 117  LYS A N   1 
ATOM   593  C  CA  . LYS A 1 117 ? 48.578  32.719 78.851  1.00 18.11 ? 117  LYS A CA  1 
ATOM   594  C  C   . LYS A 1 117 ? 49.454  32.134 77.746  1.00 20.33 ? 117  LYS A C   1 
ATOM   595  O  O   . LYS A 1 117 ? 49.105  32.213 76.561  1.00 23.01 ? 117  LYS A O   1 
ATOM   596  C  CB  . LYS A 1 117 ? 47.339  31.849 79.077  1.00 22.93 ? 117  LYS A CB  1 
ATOM   597  C  CG  . LYS A 1 117 ? 47.674  30.417 79.484  1.00 24.30 ? 117  LYS A CG  1 
ATOM   598  C  CD  . LYS A 1 117 ? 46.465  29.618 79.942  1.00 24.28 ? 117  LYS A CD  1 
ATOM   599  C  CE  . LYS A 1 117 ? 45.506  29.368 78.800  1.00 28.85 ? 117  LYS A CE  1 
ATOM   600  N  NZ  . LYS A 1 117 ? 44.217  28.763 79.248  1.00 31.94 ? 117  LYS A NZ  1 
ATOM   601  N  N   . ILE A 1 118 ? 50.595  31.562 78.133  1.00 18.63 ? 118  ILE A N   1 
ATOM   602  C  CA  . ILE A 1 118 ? 51.514  30.912 77.204  1.00 17.37 ? 118  ILE A CA  1 
ATOM   603  C  C   . ILE A 1 118 ? 51.878  29.540 77.743  1.00 19.38 ? 118  ILE A C   1 
ATOM   604  O  O   . ILE A 1 118 ? 51.718  29.250 78.932  1.00 18.47 ? 118  ILE A O   1 
ATOM   605  C  CB  . ILE A 1 118 ? 52.786  31.740 76.881  1.00 17.61 ? 118  ILE A CB  1 
ATOM   606  C  CG1 . ILE A 1 118 ? 53.744  31.757 78.068  1.00 15.75 ? 118  ILE A CG1 1 
ATOM   607  C  CG2 . ILE A 1 118 ? 52.405  33.148 76.427  1.00 19.34 ? 118  ILE A CG2 1 
ATOM   608  C  CD1 . ILE A 1 118 ? 55.158  32.167 77.653  1.00 16.89 ? 118  ILE A CD1 1 
ATOM   609  N  N   . TYR A 1 119 ? 52.355  28.682 76.842  1.00 16.99 ? 119  TYR A N   1 
ATOM   610  C  CA  . TYR A 1 119 ? 52.830  27.348 77.193  1.00 15.99 ? 119  TYR A CA  1 
ATOM   611  C  C   . TYR A 1 119 ? 54.288  27.224 76.786  1.00 17.09 ? 119  TYR A C   1 
ATOM   612  O  O   . TYR A 1 119 ? 54.671  27.652 75.690  1.00 18.26 ? 119  TYR A O   1 
ATOM   613  C  CB  . TYR A 1 119 ? 51.999  26.266 76.477  1.00 17.82 ? 119  TYR A CB  1 
ATOM   614  C  CG  . TYR A 1 119 ? 50.599  26.234 77.041  1.00 20.98 ? 119  TYR A CG  1 
ATOM   615  C  CD1 . TYR A 1 119 ? 50.310  25.466 78.159  1.00 22.14 ? 119  TYR A CD1 1 
ATOM   616  C  CD2 . TYR A 1 119 ? 49.599  27.032 76.507  1.00 21.86 ? 119  TYR A CD2 1 
ATOM   617  C  CE1 . TYR A 1 119 ? 49.055  25.465 78.719  1.00 21.24 ? 119  TYR A CE1 1 
ATOM   618  C  CE2 . TYR A 1 119 ? 48.329  27.040 77.056  1.00 23.63 ? 119  TYR A CE2 1 
ATOM   619  C  CZ  . TYR A 1 119 ? 48.074  26.248 78.160  1.00 19.74 ? 119  TYR A CZ  1 
ATOM   620  O  OH  . TYR A 1 119 ? 46.818  26.288 78.710  1.00 25.13 ? 119  TYR A OH  1 
ATOM   621  N  N   . VAL A 1 120 ? 55.101  26.625 77.653  1.00 15.72 ? 120  VAL A N   1 
ATOM   622  C  CA  . VAL A 1 120 ? 56.518  26.419 77.352  1.00 14.97 ? 120  VAL A CA  1 
ATOM   623  C  C   . VAL A 1 120 ? 56.899  24.979 77.656  1.00 17.81 ? 120  VAL A C   1 
ATOM   624  O  O   . VAL A 1 120 ? 56.821  24.543 78.813  1.00 17.19 ? 120  VAL A O   1 
ATOM   625  C  CB  . VAL A 1 120 ? 57.428  27.376 78.136  1.00 13.96 ? 120  VAL A CB  1 
ATOM   626  C  CG1 . VAL A 1 120 ? 58.858  27.149 77.722  1.00 15.44 ? 120  VAL A CG1 1 
ATOM   627  C  CG2 . VAL A 1 120 ? 57.036  28.820 77.897  1.00 19.05 ? 120  VAL A CG2 1 
ATOM   628  N  N   . ARG A 1 121 ? 57.342  24.251 76.635  1.00 16.78 ? 121  ARG A N   1 
ATOM   629  C  CA  . ARG A 1 121 ? 57.944  22.933 76.841  1.00 15.00 ? 121  ARG A CA  1 
ATOM   630  C  C   . ARG A 1 121 ? 59.452  23.136 77.029  1.00 17.91 ? 121  ARG A C   1 
ATOM   631  O  O   . ARG A 1 121 ? 60.180  23.370 76.062  1.00 16.55 ? 121  ARG A O   1 
ATOM   632  C  CB  . ARG A 1 121 ? 57.647  22.035 75.640  1.00 17.86 ? 121  ARG A CB  1 
ATOM   633  C  CG  . ARG A 1 121 ? 58.296  20.654 75.772  1.00 19.34 ? 121  ARG A CG  1 
ATOM   634  C  CD  . ARG A 1 121 ? 57.955  19.680 74.645  1.00 19.83 ? 121  ARG A CD  1 
ATOM   635  N  NE  . ARG A 1 121 ? 56.529  19.582 74.366  1.00 22.20 ? 121  ARG A NE  1 
ATOM   636  C  CZ  . ARG A 1 121 ? 55.798  18.580 74.827  1.00 22.86 ? 121  ARG A CZ  1 
ATOM   637  N  NH1 . ARG A 1 121 ? 56.334  17.656 75.612  1.00 23.72 ? 121  ARG A NH1 1 
ATOM   638  N  NH2 . ARG A 1 121 ? 54.495  18.536 74.549  1.00 20.61 ? 121  ARG A NH2 1 
ATOM   639  N  N   . TRP A 1 122 ? 59.927  23.065 78.273  1.00 15.68 ? 122  TRP A N   1 
ATOM   640  C  CA  . TRP A 1 122 ? 61.351  23.177 78.585  1.00 14.77 ? 122  TRP A CA  1 
ATOM   641  C  C   . TRP A 1 122 ? 61.957  21.783 78.474  1.00 17.11 ? 122  TRP A C   1 
ATOM   642  O  O   . TRP A 1 122 ? 61.511  20.859 79.155  1.00 17.30 ? 122  TRP A O   1 
ATOM   643  C  CB  . TRP A 1 122 ? 61.570  23.709 80.007  1.00 16.53 ? 122  TRP A CB  1 
ATOM   644  C  CG  . TRP A 1 122 ? 60.925  25.032 80.379  1.00 14.26 ? 122  TRP A CG  1 
ATOM   645  C  CD1 . TRP A 1 122 ? 59.814  25.213 81.171  1.00 15.08 ? 122  TRP A CD1 1 
ATOM   646  C  CD2 . TRP A 1 122 ? 61.404  26.346 80.062  1.00 13.86 ? 122  TRP A CD2 1 
ATOM   647  N  NE1 . TRP A 1 122 ? 59.560  26.562 81.330  1.00 15.55 ? 122  TRP A NE1 1 
ATOM   648  C  CE2 . TRP A 1 122 ? 60.516  27.276 80.660  1.00 13.90 ? 122  TRP A CE2 1 
ATOM   649  C  CE3 . TRP A 1 122 ? 62.488  26.830 79.311  1.00 15.13 ? 122  TRP A CE3 1 
ATOM   650  C  CZ2 . TRP A 1 122 ? 60.674  28.646 80.533  1.00 13.94 ? 122  TRP A CZ2 1 
ATOM   651  C  CZ3 . TRP A 1 122 ? 62.644  28.199 79.187  1.00 14.75 ? 122  TRP A CZ3 1 
ATOM   652  C  CH2 . TRP A 1 122 ? 61.753  29.089 79.809  1.00 15.15 ? 122  TRP A CH2 1 
ATOM   653  N  N   . LYS A 1 123 ? 62.970  21.628 77.622  1.00 14.72 ? 123  LYS A N   1 
ATOM   654  C  CA  . LYS A 1 123 ? 63.532  20.318 77.322  1.00 16.40 ? 123  LYS A CA  1 
ATOM   655  C  C   . LYS A 1 123 ? 64.975  20.246 77.792  1.00 15.84 ? 123  LYS A C   1 
ATOM   656  O  O   . LYS A 1 123 ? 65.764  21.155 77.532  1.00 16.36 ? 123  LYS A O   1 
ATOM   657  C  CB  . LYS A 1 123 ? 63.473  20.023 75.817  1.00 17.69 ? 123  LYS A CB  1 
ATOM   658  C  CG  . LYS A 1 123 ? 62.045  19.978 75.249  1.00 17.09 ? 123  LYS A CG  1 
ATOM   659  C  CD  . LYS A 1 123 ? 62.029  19.500 73.780  1.00 22.02 ? 123  LYS A CD  1 
ATOM   660  C  CE  . LYS A 1 123 ? 62.849  20.431 72.881  1.00 31.80 ? 123  LYS A CE  1 
ATOM   661  N  NZ  . LYS A 1 123 ? 62.811  19.989 71.441  1.00 39.18 ? 123  LYS A NZ  1 
ATOM   662  N  N   . ASN A 1 124 ? 65.324  19.138 78.446  1.00 16.03 ? 124  ASN A N   1 
ATOM   663  C  CA  . ASN A 1 124 ? 66.714  18.840 78.771  1.00 15.95 ? 124  ASN A CA  1 
ATOM   664  C  C   . ASN A 1 124 ? 67.287  18.051 77.592  1.00 15.78 ? 124  ASN A C   1 
ATOM   665  O  O   . ASN A 1 124 ? 66.974  16.874 77.405  1.00 16.62 ? 124  ASN A O   1 
ATOM   666  C  CB  . ASN A 1 124 ? 66.754  18.027 80.062  1.00 16.15 ? 124  ASN A CB  1 
ATOM   667  C  CG  . ASN A 1 124 ? 68.170  17.656 80.495  1.00 16.87 ? 124  ASN A CG  1 
ATOM   668  O  OD1 . ASN A 1 124 ? 69.061  17.469 79.670  1.00 16.24 ? 124  ASN A OD1 1 
ATOM   669  N  ND2 . ASN A 1 124 ? 68.328  17.389 81.780  1.00 14.94 ? 124  ASN A ND2 1 
ATOM   670  N  N   . LYS A 1 125 ? 68.147  18.703 76.810  1.00 14.35 ? 125  LYS A N   1 
ATOM   671  C  CA  . LYS A 1 125 ? 68.858  18.078 75.698  1.00 16.26 ? 125  LYS A CA  1 
ATOM   672  C  C   . LYS A 1 125 ? 70.359  18.148 75.959  1.00 17.76 ? 125  LYS A C   1 
ATOM   673  O  O   . LYS A 1 125 ? 71.163  18.248 75.037  1.00 18.69 ? 125  LYS A O   1 
ATOM   674  C  CB  . LYS A 1 125 ? 68.488  18.754 74.377  1.00 18.00 ? 125  LYS A CB  1 
ATOM   675  C  CG  . LYS A 1 125 ? 67.058  18.512 73.907  1.00 19.18 ? 125  LYS A CG  1 
ATOM   676  C  CD  . LYS A 1 125 ? 66.725  17.042 73.844  1.00 19.87 ? 125  LYS A CD  1 
ATOM   677  C  CE  . LYS A 1 125 ? 65.524  16.820 72.934  1.00 26.02 ? 125  LYS A CE  1 
ATOM   678  N  NZ  . LYS A 1 125 ? 65.460  15.422 72.432  1.00 29.43 ? 125  LYS A NZ  1 
ATOM   679  N  N   . LEU A 1 126 ? 70.740  18.106 77.215  1.00 16.12 ? 126  LEU A N   1 
ATOM   680  C  CA  . LEU A 1 126 ? 72.118  18.206 77.674  1.00 16.90 ? 126  LEU A CA  1 
ATOM   681  C  C   . LEU A 1 126 ? 72.797  16.841 77.702  1.00 18.25 ? 126  LEU A C   1 
ATOM   682  O  O   . LEU A 1 126 ? 72.134  15.800 77.629  1.00 19.30 ? 126  LEU A O   1 
ATOM   683  C  CB  . LEU A 1 126 ? 72.137  18.824 79.070  1.00 15.42 ? 126  LEU A CB  1 
ATOM   684  C  CG  . LEU A 1 126 ? 71.623  20.261 79.142  1.00 13.77 ? 126  LEU A CG  1 
ATOM   685  C  CD1 . LEU A 1 126 ? 71.429  20.631 80.600  1.00 17.28 ? 126  LEU A CD1 1 
ATOM   686  C  CD2 . LEU A 1 126 ? 72.583  21.261 78.469  1.00 15.19 ? 126  LEU A CD2 1 
ATOM   687  N  N   . PRO A 1 127 ? 74.130  16.813 77.783  1.00 18.87 ? 127  PRO A N   1 
ATOM   688  C  CA  . PRO A 1 127 ? 74.842  15.535 77.923  1.00 19.47 ? 127  PRO A CA  1 
ATOM   689  C  C   . PRO A 1 127 ? 74.577  14.898 79.278  1.00 18.11 ? 127  PRO A C   1 
ATOM   690  O  O   . PRO A 1 127 ? 73.946  15.469 80.169  1.00 19.93 ? 127  PRO A O   1 
ATOM   691  C  CB  . PRO A 1 127 ? 76.324  15.915 77.799  1.00 22.20 ? 127  PRO A CB  1 
ATOM   692  C  CG  . PRO A 1 127 ? 76.357  17.321 77.307  1.00 23.47 ? 127  PRO A CG  1 
ATOM   693  C  CD  . PRO A 1 127 ? 75.050  17.957 77.663  1.00 21.85 ? 127  PRO A CD  1 
ATOM   694  N  N   . GLU A 1 128 ? 75.087  13.668 79.420  1.00 20.68 ? 128  GLU A N   1 
ATOM   695  C  CA  . GLU A 1 128 ? 74.882  12.898 80.641  1.00 22.24 ? 128  GLU A CA  1 
ATOM   696  C  C   . GLU A 1 128 ? 75.799  13.316 81.774  1.00 23.96 ? 128  GLU A C   1 
ATOM   697  O  O   . GLU A 1 128 ? 75.475  13.060 82.939  1.00 24.29 ? 128  GLU A O   1 
ATOM   698  C  CB  . GLU A 1 128 ? 75.037  11.395 80.372  1.00 26.70 ? 128  GLU A CB  1 
ATOM   699  C  CG  . GLU A 1 128 ? 74.017  10.870 79.382  1.00 27.59 ? 128  GLU A CG  1 
ATOM   700  C  CD  . GLU A 1 128 ? 72.640  10.705 80.017  1.00 40.93 ? 128  GLU A CD  1 
ATOM   701  O  OE1 . GLU A 1 128 ? 71.650  11.190 79.422  1.00 42.80 ? 128  GLU A OE1 1 
ATOM   702  O  OE2 . GLU A 1 128 ? 72.546  10.088 81.105  1.00 41.23 ? 128  GLU A OE2 1 
ATOM   703  N  N   . LYS A 1 129 ? 76.914  13.960 81.473  1.00 20.79 ? 129  LYS A N   1 
ATOM   704  C  CA  . LYS A 1 129 ? 77.875  14.359 82.490  1.00 24.19 ? 129  LYS A CA  1 
ATOM   705  C  C   . LYS A 1 129 ? 77.865  15.873 82.631  1.00 19.07 ? 129  LYS A C   1 
ATOM   706  O  O   . LYS A 1 129 ? 77.702  16.602 81.649  1.00 20.62 ? 129  LYS A O   1 
ATOM   707  C  CB  . LYS A 1 129 ? 79.281  13.893 82.121  1.00 30.83 ? 129  LYS A CB  1 
ATOM   708  C  CG  . LYS A 1 129 ? 79.820  14.548 80.858  1.00 37.82 ? 129  LYS A CG  1 
ATOM   709  C  CD  . LYS A 1 129 ? 80.701  13.620 80.019  1.00 45.60 ? 129  LYS A CD  1 
ATOM   710  C  CE  . LYS A 1 129 ? 79.839  12.563 79.311  1.00 42.50 ? 129  LYS A CE  1 
ATOM   711  N  NZ  . LYS A 1 129 ? 78.584  13.198 78.755  1.00 30.58 ? 129  LYS A NZ  1 
ATOM   712  N  N   . HIS A 1 130 ? 78.016  16.340 83.860  1.00 17.47 ? 130  HIS A N   1 
ATOM   713  C  CA  . HIS A 1 130 ? 78.012  17.774 84.126  1.00 17.41 ? 130  HIS A CA  1 
ATOM   714  C  C   . HIS A 1 130 ? 79.299  18.447 83.652  1.00 17.47 ? 130  HIS A C   1 
ATOM   715  O  O   . HIS A 1 130 ? 80.369  17.839 83.607  1.00 19.73 ? 130  HIS A O   1 
ATOM   716  C  CB  . HIS A 1 130 ? 77.839  18.025 85.622  1.00 18.53 ? 130  HIS A CB  1 
ATOM   717  C  CG  . HIS A 1 130 ? 77.062  19.264 85.915  1.00 13.80 ? 130  HIS A CG  1 
ATOM   718  N  ND1 . HIS A 1 130 ? 77.544  20.528 85.659  1.00 16.23 ? 130  HIS A ND1 1 
ATOM   719  C  CD2 . HIS A 1 130 ? 75.793  19.425 86.365  1.00 15.57 ? 130  HIS A CD2 1 
ATOM   720  C  CE1 . HIS A 1 130 ? 76.616  21.420 85.968  1.00 15.90 ? 130  HIS A CE1 1 
ATOM   721  N  NE2 . HIS A 1 130 ? 75.545  20.776 86.397  1.00 15.66 ? 130  HIS A NE2 1 
ATOM   722  N  N   . LEU A 1 131 ? 79.185  19.740 83.328  1.00 15.12 ? 131  LEU A N   1 
ATOM   723  C  CA  . LEU A 1 131 ? 80.363  20.567 83.065  1.00 16.19 ? 131  LEU A CA  1 
ATOM   724  C  C   . LEU A 1 131 ? 81.189  20.830 84.321  1.00 15.69 ? 131  LEU A C   1 
ATOM   725  O  O   . LEU A 1 131 ? 82.415  20.995 84.230  1.00 18.19 ? 131  LEU A O   1 
ATOM   726  C  CB  . LEU A 1 131 ? 79.957  21.926 82.485  1.00 23.46 ? 131  LEU A CB  1 
ATOM   727  C  CG  . LEU A 1 131 ? 79.609  22.053 81.005  1.00 31.18 ? 131  LEU A CG  1 
ATOM   728  C  CD1 . LEU A 1 131 ? 79.065  23.468 80.710  1.00 24.16 ? 131  LEU A CD1 1 
ATOM   729  C  CD2 . LEU A 1 131 ? 80.848  21.780 80.192  1.00 23.58 ? 131  LEU A CD2 1 
ATOM   730  N  N   . LEU A 1 132 ? 80.552  20.886 85.490  1.00 15.56 ? 132  LEU A N   1 
ATOM   731  C  CA  . LEU A 1 132 ? 81.184  21.422 86.683  1.00 15.69 ? 132  LEU A CA  1 
ATOM   732  C  C   . LEU A 1 132 ? 81.248  20.372 87.789  1.00 14.89 ? 132  LEU A C   1 
ATOM   733  O  O   . LEU A 1 132 ? 80.554  19.351 87.722  1.00 16.91 ? 132  LEU A O   1 
ATOM   734  C  CB  . LEU A 1 132 ? 80.371  22.630 87.170  1.00 14.88 ? 132  LEU A CB  1 
ATOM   735  C  CG  . LEU A 1 132 ? 80.150  23.742 86.135  1.00 13.62 ? 132  LEU A CG  1 
ATOM   736  C  CD1 . LEU A 1 132 ? 79.406  24.872 86.830  1.00 14.73 ? 132  LEU A CD1 1 
ATOM   737  C  CD2 . LEU A 1 132 ? 81.441  24.269 85.535  1.00 15.38 ? 132  LEU A CD2 1 
ATOM   738  N  N   . PRO A 1 133 ? 82.097  20.570 88.808  1.00 16.09 ? 133  PRO A N   1 
ATOM   739  C  CA  . PRO A 1 133 ? 82.223  19.551 89.875  1.00 17.60 ? 133  PRO A CA  1 
ATOM   740  C  C   . PRO A 1 133 ? 80.969  19.431 90.750  1.00 14.47 ? 133  PRO A C   1 
ATOM   741  O  O   . PRO A 1 133 ? 80.425  20.427 91.228  1.00 16.25 ? 133  PRO A O   1 
ATOM   742  C  CB  . PRO A 1 133 ? 83.437  20.027 90.690  1.00 18.11 ? 133  PRO A CB  1 
ATOM   743  C  CG  . PRO A 1 133 ? 84.110  21.131 89.848  1.00 16.03 ? 133  PRO A CG  1 
ATOM   744  C  CD  . PRO A 1 133 ? 83.020  21.706 89.000  1.00 15.95 ? 133  PRO A CD  1 
ATOM   745  N  N   . ILE A 1 134 ? 80.529  18.198 90.973  1.00 15.92 ? 134  ILE A N   1 
ATOM   746  C  CA  . ILE A 1 134 ? 79.337  17.921 91.771  1.00 14.18 ? 134  ILE A CA  1 
ATOM   747  C  C   . ILE A 1 134 ? 79.758  17.441 93.154  1.00 14.20 ? 134  ILE A C   1 
ATOM   748  O  O   . ILE A 1 134 ? 80.558  16.507 93.287  1.00 15.64 ? 134  ILE A O   1 
ATOM   749  C  CB  . ILE A 1 134 ? 78.456  16.871 91.080  1.00 14.74 ? 134  ILE A CB  1 
ATOM   750  C  CG1 . ILE A 1 134 ? 77.828  17.473 89.827  1.00 17.41 ? 134  ILE A CG1 1 
ATOM   751  C  CG2 . ILE A 1 134 ? 77.388  16.320 92.048  1.00 18.07 ? 134  ILE A CG2 1 
ATOM   752  C  CD1 . ILE A 1 134 ? 76.988  16.449 89.045  1.00 17.38 ? 134  ILE A CD1 1 
ATOM   753  N  N   . ASP A 1 135 ? 79.227  18.099 94.190  1.00 16.27 ? 135  ASP A N   1 
ATOM   754  C  CA  . ASP A 1 135 ? 79.356  17.620 95.566  1.00 15.32 ? 135  ASP A CA  1 
ATOM   755  C  C   . ASP A 1 135 ? 78.263  16.582 95.785  1.00 15.30 ? 135  ASP A C   1 
ATOM   756  O  O   . ASP A 1 135 ? 77.063  16.914 95.749  1.00 15.40 ? 135  ASP A O   1 
ATOM   757  C  CB  . ASP A 1 135 ? 79.142  18.800 96.518  1.00 15.62 ? 135  ASP A CB  1 
ATOM   758  C  CG  . ASP A 1 135 ? 79.248  18.410 97.994  1.00 15.19 ? 135  ASP A CG  1 
ATOM   759  O  OD1 . ASP A 1 135 ? 78.975  17.260 98.350  1.00 16.63 ? 135  ASP A OD1 1 
ATOM   760  O  OD2 . ASP A 1 135 ? 79.600  19.283 98.826  1.00 16.57 ? 135  ASP A OD2 1 
ATOM   761  N  N   . ARG A 1 136 ? 78.678  15.349 96.051  1.00 16.10 ? 136  ARG A N   1 
ATOM   762  C  CA  . ARG A 1 136 ? 77.770  14.218 96.162  1.00 14.63 ? 136  ARG A CA  1 
ATOM   763  C  C   . ARG A 1 136 ? 77.185  14.034 97.562  1.00 17.50 ? 136  ARG A C   1 
ATOM   764  O  O   . ARG A 1 136 ? 76.524  13.018 97.822  1.00 19.37 ? 136  ARG A O   1 
ATOM   765  C  CB  . ARG A 1 136 ? 78.443  12.940 95.652  1.00 18.42 ? 136  ARG A CB  1 
ATOM   766  C  CG  . ARG A 1 136 ? 78.809  13.019 94.179  1.00 18.65 ? 136  ARG A CG  1 
ATOM   767  C  CD  . ARG A 1 136 ? 78.916  11.615 93.543  1.00 20.66 ? 136  ARG A CD  1 
ATOM   768  N  NE  . ARG A 1 136 ? 79.304  11.734 92.145  1.00 22.64 ? 136  ARG A NE  1 
ATOM   769  C  CZ  . ARG A 1 136 ? 78.445  11.940 91.154  1.00 23.31 ? 136  ARG A CZ  1 
ATOM   770  N  NH1 . ARG A 1 136 ? 77.141  12.041 91.379  1.00 21.08 ? 136  ARG A NH1 1 
ATOM   771  N  NH2 . ARG A 1 136 ? 78.906  12.090 89.918  1.00 24.13 ? 136  ARG A NH2 1 
ATOM   772  N  N   . THR A 1 137 ? 77.378  15.002 98.454  1.00 17.67 ? 137  THR A N   1 
ATOM   773  C  CA  . THR A 1 137 ? 76.775  14.955 99.778  1.00 17.08 ? 137  THR A CA  1 
ATOM   774  C  C   . THR A 1 137 ? 75.514  15.801 99.875  1.00 17.37 ? 137  THR A C   1 
ATOM   775  O  O   . THR A 1 137 ? 74.923  15.873 100.955 1.00 18.46 ? 137  THR A O   1 
ATOM   776  C  CB  . THR A 1 137 ? 77.778  15.385 100.861 1.00 17.61 ? 137  THR A CB  1 
ATOM   777  O  OG1 . THR A 1 137 ? 78.042  16.791 100.751 1.00 17.43 ? 137  THR A OG1 1 
ATOM   778  C  CG2 . THR A 1 137 ? 79.095  14.597 100.758 1.00 20.26 ? 137  THR A CG2 1 
ATOM   779  N  N   . LEU A 1 138 ? 75.098  16.431 98.781  1.00 15.75 ? 138  LEU A N   1 
ATOM   780  C  CA  . LEU A 1 138 ? 73.956  17.338 98.749  1.00 16.31 ? 138  LEU A CA  1 
ATOM   781  C  C   . LEU A 1 138 ? 72.704  16.588 98.276  1.00 18.17 ? 138  LEU A C   1 
ATOM   782  O  O   . LEU A 1 138 ? 72.715  15.370 98.076  1.00 19.31 ? 138  LEU A O   1 
ATOM   783  C  CB  . LEU A 1 138 ? 74.283  18.563 97.887  1.00 16.49 ? 138  LEU A CB  1 
ATOM   784  C  CG  . LEU A 1 138 ? 75.567  19.320 98.241  1.00 19.26 ? 138  LEU A CG  1 
ATOM   785  C  CD1 . LEU A 1 138 ? 75.609  20.644 97.487  1.00 15.82 ? 138  LEU A CD1 1 
ATOM   786  C  CD2 . LEU A 1 138 ? 75.717  19.558 99.724  1.00 19.08 ? 138  LEU A CD2 1 
ATOM   787  N  N   . HIS A 1 139 ? 71.589  17.307 98.144  1.00 17.35 ? 139  HIS A N   1 
ATOM   788  C  CA  . HIS A 1 139 ? 70.338  16.647 97.770  1.00 16.92 ? 139  HIS A CA  1 
ATOM   789  C  C   . HIS A 1 139 ? 70.411  16.102 96.342  1.00 15.98 ? 139  HIS A C   1 
ATOM   790  O  O   . HIS A 1 139 ? 70.760  16.817 95.397  1.00 16.71 ? 139  HIS A O   1 
ATOM   791  C  CB  . HIS A 1 139 ? 69.166  17.628 97.890  1.00 19.96 ? 139  HIS A CB  1 
ATOM   792  C  CG  . HIS A 1 139 ? 68.832  17.992 99.303  1.00 18.84 ? 139  HIS A CG  1 
ATOM   793  N  ND1 . HIS A 1 139 ? 68.729  19.301 99.725  1.00 34.07 ? 139  HIS A ND1 1 
ATOM   794  C  CD2 . HIS A 1 139 ? 68.613  17.225 100.393 1.00 25.95 ? 139  HIS A CD2 1 
ATOM   795  C  CE1 . HIS A 1 139 ? 68.443  19.319 101.014 1.00 27.89 ? 139  HIS A CE1 1 
ATOM   796  N  NE2 . HIS A 1 139 ? 68.360  18.074 101.443 1.00 32.86 ? 139  HIS A NE2 1 
ATOM   797  N  N   . GLU A 1 140 ? 70.125  14.803 96.203  1.00 16.46 ? 140  GLU A N   1 
ATOM   798  C  CA  . GLU A 1 140 ? 69.941  14.155 94.905  1.00 18.50 ? 140  GLU A CA  1 
ATOM   799  C  C   . GLU A 1 140 ? 71.222  14.069 94.081  1.00 16.00 ? 140  GLU A C   1 
ATOM   800  O  O   . GLU A 1 140 ? 71.167  14.020 92.849  1.00 18.79 ? 140  GLU A O   1 
ATOM   801  C  CB  . GLU A 1 140 ? 68.809  14.801 94.092  1.00 20.54 ? 140  GLU A CB  1 
ATOM   802  C  CG  . GLU A 1 140 ? 68.078  13.837 93.173  1.00 25.84 ? 140  GLU A CG  1 
ATOM   803  C  CD  . GLU A 1 140 ? 67.260  12.781 93.911  1.00 22.92 ? 140  GLU A CD  1 
ATOM   804  O  OE1 . GLU A 1 140 ? 67.055  11.701 93.340  1.00 32.98 ? 140  GLU A OE1 1 
ATOM   805  O  OE2 . GLU A 1 140 ? 66.768  13.059 95.022  1.00 30.29 ? 140  GLU A OE2 1 
ATOM   806  N  N   . THR A 1 141 ? 72.393  14.038 94.734  1.00 17.73 ? 141  THR A N   1 
ATOM   807  C  CA  . THR A 1 141 ? 73.661  14.024 94.011  1.00 16.56 ? 141  THR A CA  1 
ATOM   808  C  C   . THR A 1 141 ? 74.509  12.792 94.302  1.00 19.58 ? 141  THR A C   1 
ATOM   809  O  O   . THR A 1 141 ? 75.667  12.744 93.869  1.00 20.66 ? 141  THR A O   1 
ATOM   810  C  CB  . THR A 1 141 ? 74.490  15.287 94.292  1.00 16.90 ? 141  THR A CB  1 
ATOM   811  O  OG1 . THR A 1 141 ? 74.717  15.429 95.706  1.00 18.08 ? 141  THR A OG1 1 
ATOM   812  C  CG2 . THR A 1 141 ? 73.788  16.528 93.743  1.00 17.66 ? 141  THR A CG2 1 
ATOM   813  N  N   . ALA A 1 142 ? 73.978  11.791 94.997  1.00 18.66 ? 142  ALA A N   1 
ATOM   814  C  CA  . ALA A 1 142 ? 74.791  10.619 95.330  1.00 20.47 ? 142  ALA A CA  1 
ATOM   815  C  C   . ALA A 1 142 ? 75.238  9.844  94.092  1.00 25.89 ? 142  ALA A C   1 
ATOM   816  O  O   . ALA A 1 142 ? 76.332  9.260  94.088  1.00 25.20 ? 142  ALA A O   1 
ATOM   817  C  CB  . ALA A 1 142 ? 74.026  9.697  96.282  1.00 22.58 ? 142  ALA A CB  1 
ATOM   818  N  N   . GLY A 1 143 ? 74.414  9.803  93.046  1.00 25.40 ? 143  GLY A N   1 
ATOM   819  C  CA  . GLY A 1 143 ? 74.738  9.050  91.853  1.00 27.18 ? 143  GLY A CA  1 
ATOM   820  C  C   . GLY A 1 143 ? 73.954  9.538  90.653  1.00 26.23 ? 143  GLY A C   1 
ATOM   821  O  O   . GLY A 1 143 ? 73.398  10.638 90.667  1.00 22.03 ? 143  GLY A O   1 
ATOM   822  N  N   . PRO A 1 144 ? 73.869  8.720  89.596  1.00 28.95 ? 144  PRO A N   1 
ATOM   823  C  CA  . PRO A 1 144 ? 73.228  9.187  88.366  1.00 24.99 ? 144  PRO A CA  1 
ATOM   824  C  C   . PRO A 1 144 ? 71.724  9.249  88.542  1.00 26.44 ? 144  PRO A C   1 
ATOM   825  O  O   . PRO A 1 144 ? 71.143  8.478  89.326  1.00 25.35 ? 144  PRO A O   1 
ATOM   826  C  CB  . PRO A 1 144 ? 73.618  8.112  87.333  1.00 31.22 ? 144  PRO A CB  1 
ATOM   827  C  CG  . PRO A 1 144 ? 74.783  7.368  87.958  1.00 37.53 ? 144  PRO A CG  1 
ATOM   828  C  CD  . PRO A 1 144 ? 74.461  7.381  89.426  1.00 30.38 ? 144  PRO A CD  1 
ATOM   829  N  N   . PRO A 1 145 ? 71.039  10.131 87.810  1.00 21.36 ? 145  PRO A N   1 
ATOM   830  C  CA  . PRO A 1 145 ? 71.557  11.062 86.798  1.00 19.18 ? 145  PRO A CA  1 
ATOM   831  C  C   . PRO A 1 145 ? 72.194  12.295 87.421  1.00 20.45 ? 145  PRO A C   1 
ATOM   832  O  O   . PRO A 1 145 ? 71.653  12.883 88.361  1.00 19.70 ? 145  PRO A O   1 
ATOM   833  C  CB  . PRO A 1 145 ? 70.291  11.494 86.036  1.00 22.37 ? 145  PRO A CB  1 
ATOM   834  C  CG  . PRO A 1 145 ? 69.151  11.285 86.970  1.00 22.75 ? 145  PRO A CG  1 
ATOM   835  C  CD  . PRO A 1 145 ? 69.580  10.239 87.988  1.00 24.45 ? 145  PRO A CD  1 
ATOM   836  N  N   . ASP A 1 146 ? 73.344  12.705 86.883  1.00 18.82 ? 146  ASP A N   1 
ATOM   837  C  CA  . ASP A 1 146 ? 73.992  13.926 87.344  1.00 16.16 ? 146  ASP A CA  1 
ATOM   838  C  C   . ASP A 1 146 ? 73.344  15.179 86.779  1.00 17.46 ? 146  ASP A C   1 
ATOM   839  O  O   . ASP A 1 146 ? 73.341  16.211 87.449  1.00 17.81 ? 146  ASP A O   1 
ATOM   840  C  CB  . ASP A 1 146 ? 75.460  13.905 86.911  1.00 17.77 ? 146  ASP A CB  1 
ATOM   841  C  CG  . ASP A 1 146 ? 76.322  13.027 87.788  1.00 20.72 ? 146  ASP A CG  1 
ATOM   842  O  OD1 . ASP A 1 146 ? 75.823  12.432 88.759  1.00 21.85 ? 146  ASP A OD1 1 
ATOM   843  O  OD2 . ASP A 1 146 ? 77.527  12.936 87.494  1.00 22.74 ? 146  ASP A OD2 1 
ATOM   844  N  N   . VAL A 1 147 ? 72.833  15.137 85.552  1.00 15.46 ? 147  VAL A N   1 
ATOM   845  C  CA  . VAL A 1 147 ? 72.374  16.338 84.859  1.00 15.32 ? 147  VAL A CA  1 
ATOM   846  C  C   . VAL A 1 147 ? 70.850  16.373 84.961  1.00 15.56 ? 147  VAL A C   1 
ATOM   847  O  O   . VAL A 1 147 ? 70.110  15.785 84.155  1.00 19.35 ? 147  VAL A O   1 
ATOM   848  C  CB  . VAL A 1 147 ? 72.883  16.411 83.425  1.00 14.95 ? 147  VAL A CB  1 
ATOM   849  C  CG1 . VAL A 1 147 ? 72.382  17.701 82.790  1.00 16.26 ? 147  VAL A CG1 1 
ATOM   850  C  CG2 . VAL A 1 147 ? 74.429  16.326 83.408  1.00 16.19 ? 147  VAL A CG2 1 
ATOM   851  N  N   . ARG A 1 148 ? 70.376  17.067 85.983  1.00 14.11 ? 148  ARG A N   1 
ATOM   852  C  CA  . ARG A 1 148 ? 68.958  17.245 86.261  1.00 13.16 ? 148  ARG A CA  1 
ATOM   853  C  C   . ARG A 1 148 ? 68.630  18.723 86.173  1.00 12.99 ? 148  ARG A C   1 
ATOM   854  O  O   . ARG A 1 148 ? 69.396  19.558 86.660  1.00 14.43 ? 148  ARG A O   1 
ATOM   855  C  CB  . ARG A 1 148 ? 68.612  16.721 87.655  1.00 15.09 ? 148  ARG A CB  1 
ATOM   856  C  CG  . ARG A 1 148 ? 69.068  15.285 87.922  1.00 14.83 ? 148  ARG A CG  1 
ATOM   857  C  CD  . ARG A 1 148 ? 68.852  14.910 89.389  1.00 15.97 ? 148  ARG A CD  1 
ATOM   858  N  NE  . ARG A 1 148 ? 69.900  15.510 90.209  1.00 14.36 ? 148  ARG A NE  1 
ATOM   859  C  CZ  . ARG A 1 148 ? 69.720  16.546 91.023  1.00 15.04 ? 148  ARG A CZ  1 
ATOM   860  N  NH1 . ARG A 1 148 ? 68.518  17.098 91.192  1.00 15.04 ? 148  ARG A NH1 1 
ATOM   861  N  NH2 . ARG A 1 148 ? 70.763  17.035 91.695  1.00 14.53 ? 148  ARG A NH2 1 
ATOM   862  N  N   . THR A 1 149 ? 67.492  19.046 85.543  1.00 13.79 ? 149  THR A N   1 
ATOM   863  C  CA  . THR A 1 149 ? 67.169  20.439 85.274  1.00 13.69 ? 149  THR A CA  1 
ATOM   864  C  C   . THR A 1 149 ? 65.707  20.703 85.602  1.00 13.07 ? 149  THR A C   1 
ATOM   865  O  O   . THR A 1 149 ? 64.861  19.813 85.475  1.00 13.61 ? 149  THR A O   1 
ATOM   866  C  CB  . THR A 1 149 ? 67.375  20.778 83.795  1.00 13.23 ? 149  THR A CB  1 
ATOM   867  O  OG1 . THR A 1 149 ? 66.659  19.853 82.978  1.00 15.73 ? 149  THR A OG1 1 
ATOM   868  C  CG2 . THR A 1 149 ? 68.851  20.708 83.391  1.00 13.72 ? 149  THR A CG2 1 
ATOM   869  N  N   . VAL A 1 150 ? 65.410  21.948 85.989  1.00 13.18 ? 150  VAL A N   1 
ATOM   870  C  CA  . VAL A 1 150 ? 64.021  22.427 86.080  1.00 12.35 ? 150  VAL A CA  1 
ATOM   871  C  C   . VAL A 1 150 ? 64.068  23.945 85.974  1.00 13.13 ? 150  VAL A C   1 
ATOM   872  O  O   . VAL A 1 150 ? 64.995  24.573 86.475  1.00 13.05 ? 150  VAL A O   1 
ATOM   873  C  CB  . VAL A 1 150 ? 63.340  21.958 87.394  1.00 13.18 ? 150  VAL A CB  1 
ATOM   874  C  CG1 . VAL A 1 150 ? 63.929  22.651 88.627  1.00 16.32 ? 150  VAL A CG1 1 
ATOM   875  C  CG2 . VAL A 1 150 ? 61.824  22.184 87.349  1.00 14.91 ? 150  VAL A CG2 1 
ATOM   876  N  N   . VAL A 1 151 ? 63.075  24.546 85.324  1.00 13.07 ? 151  VAL A N   1 
ATOM   877  C  CA  . VAL A 1 151 ? 63.148  25.983 85.050  1.00 13.17 ? 151  VAL A CA  1 
ATOM   878  C  C   . VAL A 1 151 ? 62.162  26.706 85.954  1.00 13.21 ? 151  VAL A C   1 
ATOM   879  O  O   . VAL A 1 151 ? 60.964  26.381 85.951  1.00 13.68 ? 151  VAL A O   1 
ATOM   880  C  CB  . VAL A 1 151 ? 62.812  26.286 83.588  1.00 14.18 ? 151  VAL A CB  1 
ATOM   881  C  CG1 . VAL A 1 151 ? 62.972  27.799 83.318  1.00 15.54 ? 151  VAL A CG1 1 
ATOM   882  C  CG2 . VAL A 1 151 ? 63.659  25.460 82.632  1.00 15.96 ? 151  VAL A CG2 1 
ATOM   883  N  N   . HIS A 1 152 ? 62.666  27.672 86.733  1.00 12.71 ? 152  HIS A N   1 
ATOM   884  C  CA  . HIS A 1 152 ? 61.853  28.568 87.557  1.00 12.97 ? 152  HIS A CA  1 
ATOM   885  C  C   . HIS A 1 152 ? 61.759  29.924 86.871  1.00 12.78 ? 152  HIS A C   1 
ATOM   886  O  O   . HIS A 1 152 ? 62.788  30.492 86.453  1.00 13.31 ? 152  HIS A O   1 
ATOM   887  C  CB  . HIS A 1 152 ? 62.503  28.730 88.951  1.00 14.37 ? 152  HIS A CB  1 
ATOM   888  C  CG  . HIS A 1 152 ? 61.906  29.812 89.809  1.00 15.24 ? 152  HIS A CG  1 
ATOM   889  N  ND1 . HIS A 1 152 ? 60.576  29.815 90.186  1.00 15.27 ? 152  HIS A ND1 1 
ATOM   890  C  CD2 . HIS A 1 152 ? 62.461  30.897 90.413  1.00 14.23 ? 152  HIS A CD2 1 
ATOM   891  C  CE1 . HIS A 1 152 ? 60.331  30.873 90.942  1.00 16.28 ? 152  HIS A CE1 1 
ATOM   892  N  NE2 . HIS A 1 152 ? 61.461  31.536 91.108  1.00 18.09 ? 152  HIS A NE2 1 
ATOM   893  N  N   . LEU A 1 153 ? 60.530  30.417 86.733  1.00 12.33 ? 153  LEU A N   1 
ATOM   894  C  CA  . LEU A 1 153 ? 60.297  31.779 86.242  1.00 12.06 ? 153  LEU A CA  1 
ATOM   895  C  C   . LEU A 1 153 ? 60.258  32.670 87.479  1.00 11.72 ? 153  LEU A C   1 
ATOM   896  O  O   . LEU A 1 153 ? 59.282  32.688 88.240  1.00 13.50 ? 153  LEU A O   1 
ATOM   897  C  CB  . LEU A 1 153 ? 59.025  31.853 85.403  1.00 12.35 ? 153  LEU A CB  1 
ATOM   898  C  CG  . LEU A 1 153 ? 58.661  33.265 84.953  1.00 11.23 ? 153  LEU A CG  1 
ATOM   899  C  CD1 . LEU A 1 153 ? 59.819  33.905 84.201  1.00 14.64 ? 153  LEU A CD1 1 
ATOM   900  C  CD2 . LEU A 1 153 ? 57.409  33.222 84.091  1.00 15.35 ? 153  LEU A CD2 1 
ATOM   901  N  N   . HIS A 1 154 ? 61.362  33.350 87.723  1.00 12.71 ? 154  HIS A N   1 
ATOM   902  C  CA  . HIS A 1 154 ? 61.560  34.096 88.953  1.00 12.09 ? 154  HIS A CA  1 
ATOM   903  C  C   . HIS A 1 154 ? 60.661  35.323 88.979  1.00 13.44 ? 154  HIS A C   1 
ATOM   904  O  O   . HIS A 1 154 ? 60.764  36.206 88.111  1.00 14.65 ? 154  HIS A O   1 
ATOM   905  C  CB  . HIS A 1 154 ? 63.035  34.474 88.997  1.00 13.93 ? 154  HIS A CB  1 
ATOM   906  C  CG  . HIS A 1 154 ? 63.444  35.108 90.279  1.00 13.33 ? 154  HIS A CG  1 
ATOM   907  N  ND1 . HIS A 1 154 ? 64.370  34.546 91.135  1.00 14.02 ? 154  HIS A ND1 1 
ATOM   908  C  CD2 . HIS A 1 154 ? 62.992  36.225 90.887  1.00 13.63 ? 154  HIS A CD2 1 
ATOM   909  C  CE1 . HIS A 1 154 ? 64.510  35.340 92.189  1.00 14.04 ? 154  HIS A CE1 1 
ATOM   910  N  NE2 . HIS A 1 154 ? 63.680  36.357 92.066  1.00 15.60 ? 154  HIS A NE2 1 
ATOM   911  N  N   . GLY A 1 155 ? 59.813  35.379 90.000  1.00 12.78 ? 155  GLY A N   1 
ATOM   912  C  CA  . GLY A 1 155 ? 58.817  36.431 90.160  1.00 14.18 ? 155  GLY A CA  1 
ATOM   913  C  C   . GLY A 1 155 ? 57.437  36.081 89.648  1.00 14.72 ? 155  GLY A C   1 
ATOM   914  O  O   . GLY A 1 155 ? 56.512  36.895 89.782  1.00 16.42 ? 155  GLY A O   1 
ATOM   915  N  N   . ALA A 1 156 ? 57.249  34.884 89.110  1.00 13.62 ? 156  ALA A N   1 
ATOM   916  C  CA  . ALA A 1 156 ? 55.963  34.585 88.496  1.00 13.91 ? 156  ALA A CA  1 
ATOM   917  C  C   . ALA A 1 156 ? 54.863  34.365 89.531  1.00 16.30 ? 156  ALA A C   1 
ATOM   918  O  O   . ALA A 1 156 ? 55.024  33.624 90.504  1.00 16.84 ? 156  ALA A O   1 
ATOM   919  C  CB  . ALA A 1 156 ? 56.070  33.320 87.653  1.00 16.03 ? 156  ALA A CB  1 
ATOM   920  N  N   . ASN A 1 157 ? 53.711  34.958 89.277  1.00 15.57 ? 157  ASN A N   1 
ATOM   921  C  CA  . ASN A 1 157 ? 52.470  34.529 89.913  1.00 16.57 ? 157  ASN A CA  1 
ATOM   922  C  C   . ASN A 1 157 ? 51.979  33.366 89.064  1.00 18.33 ? 157  ASN A C   1 
ATOM   923  O  O   . ASN A 1 157 ? 51.394  33.569 87.997  1.00 18.37 ? 157  ASN A O   1 
ATOM   924  C  CB  . ASN A 1 157 ? 51.435  35.648 89.882  1.00 17.67 ? 157  ASN A CB  1 
ATOM   925  C  CG  . ASN A 1 157 ? 50.097  35.193 90.425  1.00 18.39 ? 157  ASN A CG  1 
ATOM   926  O  OD1 . ASN A 1 157 ? 50.048  34.288 91.271  1.00 19.82 ? 157  ASN A OD1 1 
ATOM   927  N  ND2 . ASN A 1 157 ? 49.003  35.783 89.942  1.00 19.76 ? 157  ASN A ND2 1 
ATOM   928  N  N   . VAL A 1 158 ? 52.225  32.141 89.518  1.00 16.23 ? 158  VAL A N   1 
ATOM   929  C  CA  . VAL A 1 158 ? 51.949  30.969 88.701  1.00 18.31 ? 158  VAL A CA  1 
ATOM   930  C  C   . VAL A 1 158 ? 51.596  29.800 89.603  1.00 18.12 ? 158  VAL A C   1 
ATOM   931  O  O   . VAL A 1 158 ? 52.106  29.679 90.721  1.00 18.15 ? 158  VAL A O   1 
ATOM   932  C  CB  . VAL A 1 158 ? 53.145  30.643 87.777  1.00 16.80 ? 158  VAL A CB  1 
ATOM   933  C  CG1 . VAL A 1 158 ? 54.316  30.023 88.572  1.00 16.42 ? 158  VAL A CG1 1 
ATOM   934  C  CG2 . VAL A 1 158 ? 52.708  29.713 86.661  1.00 18.24 ? 158  VAL A CG2 1 
ATOM   935  N  N   . ALA A 1 159 ? 50.707  28.943 89.100  1.00 17.69 ? 159  ALA A N   1 
ATOM   936  C  CA  . ALA A 1 159 ? 50.375  27.700 89.783  1.00 17.50 ? 159  ALA A CA  1 
ATOM   937  C  C   . ALA A 1 159 ? 51.642  26.887 90.039  1.00 17.26 ? 159  ALA A C   1 
ATOM   938  O  O   . ALA A 1 159 ? 52.583  26.897 89.250  1.00 18.13 ? 159  ALA A O   1 
ATOM   939  C  CB  . ALA A 1 159 ? 49.410  26.899 88.917  1.00 18.49 ? 159  ALA A CB  1 
ATOM   940  N  N   . TRP A 1 160 ? 51.638  26.157 91.162  1.00 18.26 ? 160  TRP A N   1 
ATOM   941  C  CA  . TRP A 1 160 ? 52.874  25.587 91.709  1.00 16.23 ? 160  TRP A CA  1 
ATOM   942  C  C   . TRP A 1 160 ? 53.529  24.589 90.764  1.00 17.27 ? 160  TRP A C   1 
ATOM   943  O  O   . TRP A 1 160 ? 54.757  24.458 90.763  1.00 16.31 ? 160  TRP A O   1 
ATOM   944  C  CB  . TRP A 1 160 ? 52.595  24.941 93.067  1.00 18.33 ? 160  TRP A CB  1 
ATOM   945  C  CG  . TRP A 1 160 ? 51.990  23.567 92.920  1.00 19.21 ? 160  TRP A CG  1 
ATOM   946  C  CD1 . TRP A 1 160 ? 50.673  23.267 92.751  1.00 21.65 ? 160  TRP A CD1 1 
ATOM   947  C  CD2 . TRP A 1 160 ? 52.700  22.320 92.853  1.00 22.13 ? 160  TRP A CD2 1 
ATOM   948  N  NE1 . TRP A 1 160 ? 50.512  21.907 92.612  1.00 22.34 ? 160  TRP A NE1 1 
ATOM   949  C  CE2 . TRP A 1 160 ? 51.744  21.309 92.664  1.00 22.77 ? 160  TRP A CE2 1 
ATOM   950  C  CE3 . TRP A 1 160 ? 54.054  21.970 92.929  1.00 24.33 ? 160  TRP A CE3 1 
ATOM   951  C  CZ2 . TRP A 1 160 ? 52.091  19.957 92.579  1.00 25.93 ? 160  TRP A CZ2 1 
ATOM   952  C  CZ3 . TRP A 1 160 ? 54.394  20.633 92.837  1.00 28.90 ? 160  TRP A CZ3 1 
ATOM   953  C  CH2 . TRP A 1 160 ? 53.420  19.650 92.657  1.00 27.35 ? 160  TRP A CH2 1 
ATOM   954  N  N   . ASP A 1 161 ? 52.737  23.880 89.957  1.00 16.94 ? 161  ASP A N   1 
ATOM   955  C  CA  . ASP A 1 161 ? 53.282  22.854 89.078  1.00 16.76 ? 161  ASP A CA  1 
ATOM   956  C  C   . ASP A 1 161 ? 53.931  23.410 87.819  1.00 17.70 ? 161  ASP A C   1 
ATOM   957  O  O   . ASP A 1 161 ? 54.466  22.635 87.013  1.00 17.90 ? 161  ASP A O   1 
ATOM   958  C  CB  . ASP A 1 161 ? 52.239  21.781 88.748  1.00 17.89 ? 161  ASP A CB  1 
ATOM   959  C  CG  . ASP A 1 161 ? 50.929  22.341 88.194  1.00 24.35 ? 161  ASP A CG  1 
ATOM   960  O  OD1 . ASP A 1 161 ? 50.586  23.533 88.402  1.00 20.56 ? 161  ASP A OD1 1 
ATOM   961  O  OD2 . ASP A 1 161 ? 50.187  21.538 87.577  1.00 25.11 ? 161  ASP A OD2 1 
ATOM   962  N  N   . SER A 1 162 ? 53.898  24.731 87.627  1.00 15.73 ? 162  SER A N   1 
ATOM   963  C  CA  . SER A 1 162 ? 54.685  25.397 86.602  1.00 15.60 ? 162  SER A CA  1 
ATOM   964  C  C   . SER A 1 162 ? 55.677  26.374 87.215  1.00 15.31 ? 162  SER A C   1 
ATOM   965  O  O   . SER A 1 162 ? 56.250  27.190 86.481  1.00 15.56 ? 162  SER A O   1 
ATOM   966  C  CB  . SER A 1 162 ? 53.791  26.120 85.589  1.00 16.27 ? 162  SER A CB  1 
ATOM   967  O  OG  . SER A 1 162 ? 53.068  25.195 84.776  1.00 18.12 ? 162  SER A OG  1 
ATOM   968  N  N   . ASP A 1 163 ? 55.897  26.314 88.533  1.00 15.80 ? 163  ASP A N   1 
ATOM   969  C  CA  . ASP A 1 163 ? 56.851  27.195 89.214  1.00 14.92 ? 163  ASP A CA  1 
ATOM   970  C  C   . ASP A 1 163 ? 58.289  26.707 89.141  1.00 14.81 ? 163  ASP A C   1 
ATOM   971  O  O   . ASP A 1 163 ? 59.192  27.436 89.559  1.00 16.39 ? 163  ASP A O   1 
ATOM   972  C  CB  . ASP A 1 163 ? 56.450  27.396 90.685  1.00 14.49 ? 163  ASP A CB  1 
ATOM   973  C  CG  . ASP A 1 163 ? 57.168  28.567 91.356  1.00 17.85 ? 163  ASP A CG  1 
ATOM   974  O  OD1 . ASP A 1 163 ? 57.203  29.666 90.774  1.00 18.47 ? 163  ASP A OD1 1 
ATOM   975  O  OD2 . ASP A 1 163 ? 57.642  28.405 92.505  1.00 18.79 ? 163  ASP A OD2 1 
ATOM   976  N  N   . GLY A 1 164 ? 58.533  25.483 88.670  1.00 14.94 ? 164  GLY A N   1 
ATOM   977  C  CA  . GLY A 1 164 ? 59.885  24.968 88.668  1.00 14.69 ? 164  GLY A CA  1 
ATOM   978  C  C   . GLY A 1 164 ? 60.362  24.567 90.052  1.00 14.36 ? 164  GLY A C   1 
ATOM   979  O  O   . GLY A 1 164 ? 61.477  24.906 90.469  1.00 14.93 ? 164  GLY A O   1 
ATOM   980  N  N   . HIS A 1 165 ? 59.504  23.858 90.777  1.00 14.11 ? 165  HIS A N   1 
ATOM   981  C  CA  . HIS A 1 165 ? 59.841  23.375 92.108  1.00 13.59 ? 165  HIS A CA  1 
ATOM   982  C  C   . HIS A 1 165 ? 61.166  22.616 92.058  1.00 14.24 ? 165  HIS A C   1 
ATOM   983  O  O   . HIS A 1 165 ? 61.414  21.869 91.101  1.00 14.21 ? 165  HIS A O   1 
ATOM   984  C  CB  . HIS A 1 165 ? 58.737  22.422 92.568  1.00 14.58 ? 165  HIS A CB  1 
ATOM   985  C  CG  . HIS A 1 165 ? 58.833  22.024 94.003  1.00 14.53 ? 165  HIS A CG  1 
ATOM   986  N  ND1 . HIS A 1 165 ? 59.627  20.982 94.436  1.00 15.47 ? 165  HIS A ND1 1 
ATOM   987  C  CD2 . HIS A 1 165 ? 58.232  22.531 95.108  1.00 16.23 ? 165  HIS A CD2 1 
ATOM   988  C  CE1 . HIS A 1 165 ? 59.509  20.864 95.748  1.00 15.19 ? 165  HIS A CE1 1 
ATOM   989  N  NE2 . HIS A 1 165 ? 58.663  21.787 96.181  1.00 16.31 ? 165  HIS A NE2 1 
ATOM   990  N  N   . PRO A 1 166 ? 62.039  22.777 93.060  1.00 14.06 ? 166  PRO A N   1 
ATOM   991  C  CA  . PRO A 1 166 ? 63.379  22.166 92.963  1.00 14.58 ? 166  PRO A CA  1 
ATOM   992  C  C   . PRO A 1 166 ? 63.356  20.653 92.864  1.00 14.25 ? 166  PRO A C   1 
ATOM   993  O  O   . PRO A 1 166 ? 64.337  20.071 92.372  1.00 14.37 ? 166  PRO A O   1 
ATOM   994  C  CB  . PRO A 1 166 ? 64.119  22.648 94.230  1.00 15.41 ? 166  PRO A CB  1 
ATOM   995  C  CG  . PRO A 1 166 ? 63.211  23.593 94.916  1.00 27.55 ? 166  PRO A CG  1 
ATOM   996  C  CD  . PRO A 1 166 ? 61.872  23.640 94.243  1.00 18.30 ? 166  PRO A CD  1 
ATOM   997  N  N   . GLU A 1 167 ? 62.281  19.994 93.309  1.00 14.54 ? 167  GLU A N   1 
ATOM   998  C  CA  . GLU A 1 167 ? 62.176  18.534 93.212  1.00 15.32 ? 167  GLU A CA  1 
ATOM   999  C  C   . GLU A 1 167 ? 61.368  18.098 91.995  1.00 12.64 ? 167  GLU A C   1 
ATOM   1000 O  O   . GLU A 1 167 ? 61.033  16.916 91.872  1.00 15.64 ? 167  GLU A O   1 
ATOM   1001 C  CB  . GLU A 1 167 ? 61.597  17.944 94.501  1.00 15.88 ? 167  GLU A CB  1 
ATOM   1002 C  CG  . GLU A 1 167 ? 62.538  18.067 95.678  1.00 17.01 ? 167  GLU A CG  1 
ATOM   1003 C  CD  . GLU A 1 167 ? 61.913  17.722 97.009  1.00 22.25 ? 167  GLU A CD  1 
ATOM   1004 O  OE1 . GLU A 1 167 ? 60.666  17.823 97.155  1.00 27.58 ? 167  GLU A OE1 1 
ATOM   1005 O  OE2 . GLU A 1 167 ? 62.687  17.375 97.928  1.00 21.88 ? 167  GLU A OE2 1 
ATOM   1006 N  N   . ALA A 1 168 ? 61.075  19.031 91.086  1.00 13.62 ? 168  ALA A N   1 
ATOM   1007 C  CA  . ALA A 1 168 ? 60.352  18.751 89.853  1.00 15.06 ? 168  ALA A CA  1 
ATOM   1008 C  C   . ALA A 1 168 ? 61.305  18.628 88.672  1.00 14.39 ? 168  ALA A C   1 
ATOM   1009 O  O   . ALA A 1 168 ? 60.895  18.796 87.521  1.00 15.77 ? 168  ALA A O   1 
ATOM   1010 C  CB  . ALA A 1 168 ? 59.280  19.826 89.614  1.00 14.49 ? 168  ALA A CB  1 
ATOM   1011 N  N   . TRP A 1 169 ? 62.577  18.356 88.944  1.00 13.73 ? 169  TRP A N   1 
ATOM   1012 C  CA  . TRP A 1 169 ? 63.596  18.290 87.912  1.00 13.67 ? 169  TRP A CA  1 
ATOM   1013 C  C   . TRP A 1 169 ? 63.397  17.061 87.021  1.00 14.15 ? 169  TRP A C   1 
ATOM   1014 O  O   . TRP A 1 169 ? 62.663  16.126 87.340  1.00 15.23 ? 169  TRP A O   1 
ATOM   1015 C  CB  . TRP A 1 169 ? 64.993  18.221 88.550  1.00 12.77 ? 169  TRP A CB  1 
ATOM   1016 C  CG  . TRP A 1 169 ? 65.109  17.113 89.577  1.00 15.88 ? 169  TRP A CG  1 
ATOM   1017 C  CD1 . TRP A 1 169 ? 64.995  17.240 90.940  1.00 15.27 ? 169  TRP A CD1 1 
ATOM   1018 C  CD2 . TRP A 1 169 ? 65.311  15.700 89.330  1.00 13.19 ? 169  TRP A CD2 1 
ATOM   1019 N  NE1 . TRP A 1 169 ? 65.115  16.014 91.541  1.00 16.03 ? 169  TRP A NE1 1 
ATOM   1020 C  CE2 . TRP A 1 169 ? 65.321  15.054 90.586  1.00 15.02 ? 169  TRP A CE2 1 
ATOM   1021 C  CE3 . TRP A 1 169 ? 65.512  14.923 88.170  1.00 14.93 ? 169  TRP A CE3 1 
ATOM   1022 C  CZ2 . TRP A 1 169 ? 65.494  13.676 90.721  1.00 17.74 ? 169  TRP A CZ2 1 
ATOM   1023 C  CZ3 . TRP A 1 169 ? 65.682  13.532 88.314  1.00 16.86 ? 169  TRP A CZ3 1 
ATOM   1024 C  CH2 . TRP A 1 169 ? 65.664  12.935 89.581  1.00 16.05 ? 169  TRP A CH2 1 
ATOM   1025 N  N   . PHE A 1 170 ? 64.132  17.060 85.908  1.00 14.05 ? 170  PHE A N   1 
ATOM   1026 C  CA  . PHE A 1 170 ? 64.110  15.975 84.938  1.00 14.28 ? 170  PHE A CA  1 
ATOM   1027 C  C   . PHE A 1 170 ? 65.493  15.855 84.307  1.00 13.84 ? 170  PHE A C   1 
ATOM   1028 O  O   . PHE A 1 170 ? 66.208  16.852 84.129  1.00 13.93 ? 170  PHE A O   1 
ATOM   1029 C  CB  . PHE A 1 170 ? 63.035  16.213 83.850  1.00 16.23 ? 170  PHE A CB  1 
ATOM   1030 C  CG  . PHE A 1 170 ? 62.970  17.637 83.337  1.00 12.95 ? 170  PHE A CG  1 
ATOM   1031 C  CD1 . PHE A 1 170 ? 62.218  18.598 84.014  1.00 14.17 ? 170  PHE A CD1 1 
ATOM   1032 C  CD2 . PHE A 1 170 ? 63.616  18.006 82.163  1.00 17.14 ? 170  PHE A CD2 1 
ATOM   1033 C  CE1 . PHE A 1 170 ? 62.135  19.897 83.558  1.00 14.67 ? 170  PHE A CE1 1 
ATOM   1034 C  CE2 . PHE A 1 170 ? 63.546  19.327 81.701  1.00 14.97 ? 170  PHE A CE2 1 
ATOM   1035 C  CZ  . PHE A 1 170 ? 62.808  20.266 82.396  1.00 16.81 ? 170  PHE A CZ  1 
ATOM   1036 N  N   . SER A 1 171 ? 65.863  14.611 84.005  1.00 14.12 ? 171  SER A N   1 
ATOM   1037 C  CA  . SER A 1 171 ? 67.071  14.317 83.249  1.00 13.81 ? 171  SER A CA  1 
ATOM   1038 C  C   . SER A 1 171 ? 66.762  14.403 81.756  1.00 15.07 ? 171  SER A C   1 
ATOM   1039 O  O   . SER A 1 171 ? 65.679  14.831 81.347  1.00 17.75 ? 171  SER A O   1 
ATOM   1040 C  CB  . SER A 1 171 ? 67.623  12.967 83.671  1.00 17.55 ? 171  SER A CB  1 
ATOM   1041 O  OG  . SER A 1 171 ? 66.706  11.954 83.334  1.00 18.17 ? 171  SER A OG  1 
ATOM   1042 N  N   . ARG A 1 172 ? 67.714  13.982 80.921  1.00 16.30 ? 172  ARG A N   1 
ATOM   1043 C  CA  . ARG A 1 172 ? 67.545  14.111 79.481  1.00 16.89 ? 172  ARG A CA  1 
ATOM   1044 C  C   . ARG A 1 172 ? 66.255  13.450 79.017  1.00 17.54 ? 172  ARG A C   1 
ATOM   1045 O  O   . ARG A 1 172 ? 65.984  12.292 79.343  1.00 18.44 ? 172  ARG A O   1 
ATOM   1046 C  CB  . ARG A 1 172 ? 68.733  13.486 78.765  1.00 21.49 ? 172  ARG A CB  1 
ATOM   1047 C  CG  . ARG A 1 172 ? 68.449  13.350 77.303  1.00 27.36 ? 172  ARG A CG  1 
ATOM   1048 C  CD  . ARG A 1 172 ? 69.181  14.398 76.551  1.00 26.29 ? 172  ARG A CD  1 
ATOM   1049 N  NE  . ARG A 1 172 ? 69.170  14.111 75.125  1.00 29.82 ? 172  ARG A NE  1 
ATOM   1050 C  CZ  . ARG A 1 172 ? 70.128  14.480 74.292  1.00 29.42 ? 172  ARG A CZ  1 
ATOM   1051 N  NH1 . ARG A 1 172 ? 71.224  15.081 74.726  1.00 30.41 ? 172  ARG A NH1 1 
ATOM   1052 N  NH2 . ARG A 1 172 ? 69.985  14.231 72.995  1.00 32.35 ? 172  ARG A NH2 1 
ATOM   1053 N  N   . ASP A 1 173 ? 65.452  14.205 78.256  1.00 17.80 ? 173  ASP A N   1 
ATOM   1054 C  CA  . ASP A 1 173 ? 64.215  13.697 77.663  1.00 17.92 ? 173  ASP A CA  1 
ATOM   1055 C  C   . ASP A 1 173 ? 63.250  13.151 78.709  1.00 20.05 ? 173  ASP A C   1 
ATOM   1056 O  O   . ASP A 1 173 ? 62.476  12.228 78.424  1.00 22.05 ? 173  ASP A O   1 
ATOM   1057 C  CB  . ASP A 1 173 ? 64.479  12.659 76.564  1.00 22.32 ? 173  ASP A CB  1 
ATOM   1058 C  CG  . ASP A 1 173 ? 65.213  13.248 75.372  1.00 30.68 ? 173  ASP A CG  1 
ATOM   1059 O  OD1 . ASP A 1 173 ? 64.969  14.428 75.042  1.00 26.69 ? 173  ASP A OD1 1 
ATOM   1060 O  OD2 . ASP A 1 173 ? 66.034  12.532 74.768  1.00 39.33 ? 173  ASP A OD2 1 
ATOM   1061 N  N   . PHE A 1 174 ? 63.302  13.707 79.928  1.00 18.33 ? 174  PHE A N   1 
ATOM   1062 C  CA  . PHE A 1 174 ? 62.402  13.281 81.014  1.00 17.86 ? 174  PHE A CA  1 
ATOM   1063 C  C   . PHE A 1 174 ? 62.597  11.816 81.411  1.00 18.73 ? 174  PHE A C   1 
ATOM   1064 O  O   . PHE A 1 174 ? 61.677  11.181 81.927  1.00 20.49 ? 174  PHE A O   1 
ATOM   1065 C  CB  . PHE A 1 174 ? 60.922  13.595 80.737  1.00 18.42 ? 174  PHE A CB  1 
ATOM   1066 C  CG  . PHE A 1 174 ? 60.673  15.012 80.269  1.00 16.19 ? 174  PHE A CG  1 
ATOM   1067 C  CD1 . PHE A 1 174 ? 60.635  16.059 81.183  1.00 16.76 ? 174  PHE A CD1 1 
ATOM   1068 C  CD2 . PHE A 1 174 ? 60.459  15.294 78.917  1.00 19.14 ? 174  PHE A CD2 1 
ATOM   1069 C  CE1 . PHE A 1 174 ? 60.411  17.378 80.755  1.00 16.96 ? 174  PHE A CE1 1 
ATOM   1070 C  CE2 . PHE A 1 174 ? 60.225  16.600 78.481  1.00 18.42 ? 174  PHE A CE2 1 
ATOM   1071 C  CZ  . PHE A 1 174 ? 60.197  17.634 79.400  1.00 16.15 ? 174  PHE A CZ  1 
ATOM   1072 N  N   . ALA A 1 175 ? 63.795  11.264 81.195  1.00 17.37 ? 175  ALA A N   1 
ATOM   1073 C  CA  . ALA A 1 175 ? 63.988  9.838  81.467  1.00 18.42 ? 175  ALA A CA  1 
ATOM   1074 C  C   . ALA A 1 175 ? 63.843  9.524  82.952  1.00 21.56 ? 175  ALA A C   1 
ATOM   1075 O  O   . ALA A 1 175 ? 63.329  8.456  83.323  1.00 20.93 ? 175  ALA A O   1 
ATOM   1076 C  CB  . ALA A 1 175 ? 65.345  9.367  80.942  1.00 22.48 ? 175  ALA A CB  1 
ATOM   1077 N  N   . LYS A 1 176 ? 64.323  10.417 83.812  1.00 18.82 ? 176  LYS A N   1 
ATOM   1078 C  CA  . LYS A 1 176 ? 64.119  10.318 85.247  1.00 17.79 ? 176  LYS A CA  1 
ATOM   1079 C  C   . LYS A 1 176 ? 63.628  11.675 85.728  1.00 15.64 ? 176  LYS A C   1 
ATOM   1080 O  O   . LYS A 1 176 ? 64.025  12.719 85.194  1.00 16.92 ? 176  LYS A O   1 
ATOM   1081 C  CB  . LYS A 1 176 ? 65.411  9.929  85.989  1.00 21.31 ? 176  LYS A CB  1 
ATOM   1082 C  CG  . LYS A 1 176 ? 65.165  9.667  87.471  1.00 33.52 ? 176  LYS A CG  1 
ATOM   1083 C  CD  . LYS A 1 176 ? 66.340  8.966  88.147  1.00 37.68 ? 176  LYS A CD  1 
ATOM   1084 C  CE  . LYS A 1 176 ? 66.309  9.199  89.654  1.00 30.10 ? 176  LYS A CE  1 
ATOM   1085 N  NZ  . LYS A 1 176 ? 67.267  8.332  90.385  1.00 43.73 ? 176  LYS A NZ  1 
ATOM   1086 N  N   . THR A 1 177 ? 62.705  11.653 86.692  1.00 16.90 ? 177  THR A N   1 
ATOM   1087 C  CA  . THR A 1 177 ? 62.095  12.879 87.181  1.00 17.34 ? 177  THR A CA  1 
ATOM   1088 C  C   . THR A 1 177 ? 62.043  12.860 88.705  1.00 16.73 ? 177  THR A C   1 
ATOM   1089 O  O   . THR A 1 177 ? 61.954  11.794 89.328  1.00 17.34 ? 177  THR A O   1 
ATOM   1090 C  CB  . THR A 1 177 ? 60.670  13.064 86.598  1.00 19.21 ? 177  THR A CB  1 
ATOM   1091 O  OG1 . THR A 1 177 ? 59.892  11.875 86.796  1.00 20.66 ? 177  THR A OG1 1 
ATOM   1092 C  CG2 . THR A 1 177 ? 60.744  13.349 85.097  1.00 19.10 ? 177  THR A CG2 1 
ATOM   1093 N  N   . GLY A 1 178 ? 62.078  14.061 89.299  1.00 16.16 ? 178  GLY A N   1 
ATOM   1094 C  CA  . GLY A 1 178 ? 61.959  14.191 90.740  1.00 16.84 ? 178  GLY A CA  1 
ATOM   1095 C  C   . GLY A 1 178 ? 60.523  14.024 91.254  1.00 15.03 ? 178  GLY A C   1 
ATOM   1096 O  O   . GLY A 1 178 ? 59.554  13.972 90.497  1.00 17.04 ? 178  GLY A O   1 
ATOM   1097 N  N   . ALA A 1 179 ? 60.413  13.965 92.586  1.00 16.69 ? 179  ALA A N   1 
ATOM   1098 C  CA  . ALA A 1 179 ? 59.161  13.607 93.248  1.00 19.21 ? 179  ALA A CA  1 
ATOM   1099 C  C   . ALA A 1 179 ? 58.014  14.577 92.954  1.00 18.89 ? 179  ALA A C   1 
ATOM   1100 O  O   . ALA A 1 179 ? 56.854  14.159 92.935  1.00 19.44 ? 179  ALA A O   1 
ATOM   1101 C  CB  . ALA A 1 179 ? 59.383  13.502 94.756  1.00 21.35 ? 179  ALA A CB  1 
ATOM   1102 N  N   . THR A 1 180 ? 58.294  15.867 92.748  1.00 16.09 ? 180  THR A N   1 
ATOM   1103 C  CA  . THR A 1 180 ? 57.211  16.822 92.512  1.00 15.32 ? 180  THR A CA  1 
ATOM   1104 C  C   . THR A 1 180 ? 56.968  17.098 91.030  1.00 16.98 ? 180  THR A C   1 
ATOM   1105 O  O   . THR A 1 180 ? 56.167  17.990 90.687  1.00 17.49 ? 180  THR A O   1 
ATOM   1106 C  CB  . THR A 1 180 ? 57.446  18.106 93.303  1.00 16.05 ? 180  THR A CB  1 
ATOM   1107 O  OG1 . THR A 1 180 ? 58.674  18.679 92.865  1.00 15.75 ? 180  THR A OG1 1 
ATOM   1108 C  CG2 . THR A 1 180 ? 57.542  17.795 94.814  1.00 18.19 ? 180  THR A CG2 1 
ATOM   1109 N  N   . PHE A 1 181 ? 57.620  16.345 90.145  1.00 16.96 ? 181  PHE A N   1 
ATOM   1110 C  CA  . PHE A 1 181 ? 57.419  16.528 88.707  1.00 16.42 ? 181  PHE A CA  1 
ATOM   1111 C  C   . PHE A 1 181 ? 55.955  16.318 88.336  1.00 16.23 ? 181  PHE A C   1 
ATOM   1112 O  O   . PHE A 1 181 ? 55.315  15.370 88.797  1.00 16.89 ? 181  PHE A O   1 
ATOM   1113 C  CB  . PHE A 1 181 ? 58.283  15.523 87.950  1.00 16.49 ? 181  PHE A CB  1 
ATOM   1114 C  CG  . PHE A 1 181 ? 58.119  15.590 86.469  1.00 16.56 ? 181  PHE A CG  1 
ATOM   1115 C  CD1 . PHE A 1 181 ? 58.853  16.522 85.739  1.00 17.29 ? 181  PHE A CD1 1 
ATOM   1116 C  CD2 . PHE A 1 181 ? 57.268  14.711 85.798  1.00 19.86 ? 181  PHE A CD2 1 
ATOM   1117 C  CE1 . PHE A 1 181 ? 58.723  16.605 84.358  1.00 19.09 ? 181  PHE A CE1 1 
ATOM   1118 C  CE2 . PHE A 1 181 ? 57.131  14.784 84.415  1.00 18.79 ? 181  PHE A CE2 1 
ATOM   1119 C  CZ  . PHE A 1 181 ? 57.865  15.743 83.693  1.00 18.97 ? 181  PHE A CZ  1 
ATOM   1120 N  N   . ARG A 1 182 ? 55.423  17.248 87.537  1.00 16.55 ? 182  ARG A N   1 
ATOM   1121 C  CA  . ARG A 1 182 ? 54.026  17.160 87.104  1.00 16.12 ? 182  ARG A CA  1 
ATOM   1122 C  C   . ARG A 1 182 ? 53.783  17.396 85.615  1.00 15.80 ? 182  ARG A C   1 
ATOM   1123 O  O   . ARG A 1 182 ? 52.931  16.731 85.021  1.00 17.04 ? 182  ARG A O   1 
ATOM   1124 C  CB  . ARG A 1 182 ? 53.172  18.187 87.863  1.00 18.23 ? 182  ARG A CB  1 
ATOM   1125 C  CG  . ARG A 1 182 ? 52.872  17.863 89.325  1.00 17.22 ? 182  ARG A CG  1 
ATOM   1126 C  CD  . ARG A 1 182 ? 52.214  16.510 89.500  1.00 18.49 ? 182  ARG A CD  1 
ATOM   1127 N  NE  . ARG A 1 182 ? 51.739  16.322 90.865  1.00 22.61 ? 182  ARG A NE  1 
ATOM   1128 C  CZ  . ARG A 1 182 ? 52.417  15.629 91.767  1.00 20.95 ? 182  ARG A CZ  1 
ATOM   1129 N  NH1 . ARG A 1 182 ? 53.617  15.147 91.494  1.00 19.88 ? 182  ARG A NH1 1 
ATOM   1130 N  NH2 . ARG A 1 182 ? 51.907  15.465 92.982  1.00 22.50 ? 182  ARG A NH2 1 
ATOM   1131 N  N   . ARG A 1 183 ? 54.477  18.362 85.016  1.00 17.20 ? 183  ARG A N   1 
ATOM   1132 C  CA  . ARG A 1 183 ? 54.137  18.853 83.680  1.00 17.82 ? 183  ARG A CA  1 
ATOM   1133 C  C   . ARG A 1 183 ? 55.393  18.915 82.837  1.00 18.22 ? 183  ARG A C   1 
ATOM   1134 O  O   . ARG A 1 183 ? 56.366  19.551 83.237  1.00 17.78 ? 183  ARG A O   1 
ATOM   1135 C  CB  . ARG A 1 183 ? 53.555  20.290 83.711  1.00 21.05 ? 183  ARG A CB  1 
ATOM   1136 C  CG  . ARG A 1 183 ? 52.347  20.524 84.619  1.00 19.87 ? 183  ARG A CG  1 
ATOM   1137 C  CD  . ARG A 1 183 ? 51.898  21.992 84.519  1.00 19.78 ? 183  ARG A CD  1 
ATOM   1138 N  NE  . ARG A 1 183 ? 51.375  22.307 83.191  1.00 19.56 ? 183  ARG A NE  1 
ATOM   1139 C  CZ  . ARG A 1 183 ? 50.154  22.760 82.949  1.00 19.39 ? 183  ARG A CZ  1 
ATOM   1140 N  NH1 . ARG A 1 183 ? 49.358  23.179 83.925  1.00 21.38 ? 183  ARG A NH1 1 
ATOM   1141 N  NH2 . ARG A 1 183 ? 49.705  22.786 81.695  1.00 23.41 ? 183  ARG A NH2 1 
ATOM   1142 N  N   . LYS A 1 184 ? 55.363  18.271 81.667  1.00 18.40 ? 184  LYS A N   1 
ATOM   1143 C  CA  . LYS A 1 184 ? 56.419  18.529 80.683  1.00 15.96 ? 184  LYS A CA  1 
ATOM   1144 C  C   . LYS A 1 184 ? 56.252  19.910 80.067  1.00 17.22 ? 184  LYS A C   1 
ATOM   1145 O  O   . LYS A 1 184 ? 57.244  20.597 79.777  1.00 19.31 ? 184  LYS A O   1 
ATOM   1146 C  CB  . LYS A 1 184 ? 56.336  17.463 79.591  1.00 18.60 ? 184  LYS A CB  1 
ATOM   1147 C  CG  . LYS A 1 184 ? 56.761  16.068 80.055  1.00 20.12 ? 184  LYS A CG  1 
ATOM   1148 C  CD  . LYS A 1 184 ? 56.670  15.039 78.936  1.00 22.54 ? 184  LYS A CD  1 
ATOM   1149 C  CE  . LYS A 1 184 ? 56.961  13.650 79.489  1.00 27.42 ? 184  LYS A CE  1 
ATOM   1150 N  NZ  . LYS A 1 184 ? 56.742  12.561 78.498  1.00 33.17 ? 184  LYS A NZ  1 
ATOM   1151 N  N   . VAL A 1 185 ? 55.014  20.314 79.824  1.00 18.15 ? 185  VAL A N   1 
ATOM   1152 C  CA  . VAL A 1 185 ? 54.704  21.609 79.232  1.00 16.73 ? 185  VAL A CA  1 
ATOM   1153 C  C   . VAL A 1 185 ? 54.164  22.492 80.348  1.00 15.57 ? 185  VAL A C   1 
ATOM   1154 O  O   . VAL A 1 185 ? 53.096  22.218 80.913  1.00 17.91 ? 185  VAL A O   1 
ATOM   1155 C  CB  . VAL A 1 185 ? 53.721  21.502 78.059  1.00 19.48 ? 185  VAL A CB  1 
ATOM   1156 C  CG1 . VAL A 1 185 ? 53.457  22.914 77.462  1.00 19.49 ? 185  VAL A CG1 1 
ATOM   1157 C  CG2 . VAL A 1 185 ? 54.240  20.538 77.006  1.00 21.00 ? 185  VAL A CG2 1 
ATOM   1158 N  N   . TYR A 1 186 ? 54.920  23.538 80.688  1.00 16.43 ? 186  TYR A N   1 
ATOM   1159 C  CA  . TYR A 1 186 ? 54.514  24.502 81.696  1.00 15.89 ? 186  TYR A CA  1 
ATOM   1160 C  C   . TYR A 1 186 ? 53.494  25.481 81.116  1.00 17.81 ? 186  TYR A C   1 
ATOM   1161 O  O   . TYR A 1 186 ? 53.423  25.705 79.897  1.00 17.26 ? 186  TYR A O   1 
ATOM   1162 C  CB  . TYR A 1 186 ? 55.744  25.273 82.199  1.00 18.23 ? 186  TYR A CB  1 
ATOM   1163 C  CG  . TYR A 1 186 ? 56.553  24.562 83.270  1.00 15.93 ? 186  TYR A CG  1 
ATOM   1164 C  CD1 . TYR A 1 186 ? 56.468  23.181 83.456  1.00 17.20 ? 186  TYR A CD1 1 
ATOM   1165 C  CD2 . TYR A 1 186 ? 57.390  25.278 84.100  1.00 16.82 ? 186  TYR A CD2 1 
ATOM   1166 C  CE1 . TYR A 1 186 ? 57.203  22.545 84.447  1.00 17.19 ? 186  TYR A CE1 1 
ATOM   1167 C  CE2 . TYR A 1 186 ? 58.132  24.665 85.086  1.00 15.20 ? 186  TYR A CE2 1 
ATOM   1168 C  CZ  . TYR A 1 186 ? 58.043  23.301 85.259  1.00 17.00 ? 186  TYR A CZ  1 
ATOM   1169 O  OH  . TYR A 1 186 ? 58.805  22.723 86.267  1.00 18.80 ? 186  TYR A OH  1 
ATOM   1170 N  N   . GLU A 1 187 ? 52.685  26.059 82.007  1.00 17.49 ? 187  GLU A N   1 
ATOM   1171 C  CA  . GLU A 1 187 ? 51.680  27.045 81.630  1.00 17.24 ? 187  GLU A CA  1 
ATOM   1172 C  C   . GLU A 1 187 ? 51.906  28.305 82.460  1.00 18.33 ? 187  GLU A C   1 
ATOM   1173 O  O   . GLU A 1 187 ? 51.863  28.261 83.700  1.00 18.12 ? 187  GLU A O   1 
ATOM   1174 C  CB  . GLU A 1 187 ? 50.275  26.483 81.865  1.00 19.73 ? 187  GLU A CB  1 
ATOM   1175 C  CG  . GLU A 1 187 ? 49.166  27.502 81.767  1.00 20.42 ? 187  GLU A CG  1 
ATOM   1176 C  CD  . GLU A 1 187 ? 47.874  26.930 82.272  1.00 20.98 ? 187  GLU A CD  1 
ATOM   1177 O  OE1 . GLU A 1 187 ? 47.661  27.031 83.493  1.00 24.54 ? 187  GLU A OE1 1 
ATOM   1178 O  OE2 . GLU A 1 187 ? 47.085  26.392 81.455  1.00 23.45 ? 187  GLU A OE2 1 
ATOM   1179 N  N   . TYR A 1 188 ? 52.164  29.424 81.787  1.00 16.11 ? 188  TYR A N   1 
ATOM   1180 C  CA  . TYR A 1 188 ? 52.338  30.702 82.468  1.00 15.63 ? 188  TYR A CA  1 
ATOM   1181 C  C   . TYR A 1 188 ? 51.107  31.552 82.184  1.00 17.30 ? 188  TYR A C   1 
ATOM   1182 O  O   . TYR A 1 188 ? 50.815  31.870 81.024  1.00 19.02 ? 188  TYR A O   1 
ATOM   1183 C  CB  . TYR A 1 188 ? 53.620  31.418 82.022  1.00 14.11 ? 188  TYR A CB  1 
ATOM   1184 C  CG  . TYR A 1 188 ? 54.863  30.626 82.354  1.00 14.60 ? 188  TYR A CG  1 
ATOM   1185 C  CD1 . TYR A 1 188 ? 55.203  30.350 83.676  1.00 15.73 ? 188  TYR A CD1 1 
ATOM   1186 C  CD2 . TYR A 1 188 ? 55.711  30.166 81.348  1.00 15.46 ? 188  TYR A CD2 1 
ATOM   1187 C  CE1 . TYR A 1 188 ? 56.349  29.623 83.983  1.00 13.23 ? 188  TYR A CE1 1 
ATOM   1188 C  CE2 . TYR A 1 188 ? 56.863  29.443 81.652  1.00 14.90 ? 188  TYR A CE2 1 
ATOM   1189 C  CZ  . TYR A 1 188 ? 57.165  29.162 82.965  1.00 13.50 ? 188  TYR A CZ  1 
ATOM   1190 O  OH  . TYR A 1 188 ? 58.325  28.454 83.220  1.00 14.76 ? 188  TYR A OH  1 
ATOM   1191 N  N   . THR A 1 189 ? 50.356  31.871 83.234  1.00 16.71 ? 189  THR A N   1 
ATOM   1192 C  CA  . THR A 1 189 ? 49.118  32.638 83.098  1.00 17.80 ? 189  THR A CA  1 
ATOM   1193 C  C   . THR A 1 189 ? 49.345  34.150 83.153  1.00 17.99 ? 189  THR A C   1 
ATOM   1194 O  O   . THR A 1 189 ? 48.535  34.903 82.608  1.00 19.80 ? 189  THR A O   1 
ATOM   1195 C  CB  . THR A 1 189 ? 48.125  32.189 84.169  1.00 19.33 ? 189  THR A CB  1 
ATOM   1196 O  OG1 . THR A 1 189 ? 48.828  32.040 85.403  1.00 19.26 ? 189  THR A OG1 1 
ATOM   1197 C  CG2 . THR A 1 189 ? 47.492  30.851 83.780  1.00 21.19 ? 189  THR A CG2 1 
ATOM   1198 N  N   . ASN A 1 190 ? 50.450  34.597 83.767  1.00 17.70 ? 190  ASN A N   1 
ATOM   1199 C  CA  . ASN A 1 190 ? 50.908  35.991 83.687  1.00 17.39 ? 190  ASN A CA  1 
ATOM   1200 C  C   . ASN A 1 190 ? 49.918  37.014 84.242  1.00 16.76 ? 190  ASN A C   1 
ATOM   1201 O  O   . ASN A 1 190 ? 49.879  38.162 83.782  1.00 19.30 ? 190  ASN A O   1 
ATOM   1202 C  CB  . ASN A 1 190 ? 51.380  36.364 82.275  1.00 19.08 ? 190  ASN A CB  1 
ATOM   1203 C  CG  . ASN A 1 190 ? 52.518  35.490 81.817  1.00 17.08 ? 190  ASN A CG  1 
ATOM   1204 O  OD1 . ASN A 1 190 ? 53.557  35.444 82.463  1.00 17.40 ? 190  ASN A OD1 1 
ATOM   1205 N  ND2 . ASN A 1 190 ? 52.342  34.807 80.689  1.00 17.51 ? 190  ASN A ND2 1 
ATOM   1206 N  N   . LYS A 1 191 ? 49.150  36.644 85.268  1.00 18.01 ? 191  LYS A N   1 
ATOM   1207 C  CA  . LYS A 1 191 ? 48.170  37.548 85.876  1.00 18.10 ? 191  LYS A CA  1 
ATOM   1208 C  C   . LYS A 1 191 ? 48.871  38.338 86.979  1.00 20.13 ? 191  LYS A C   1 
ATOM   1209 O  O   . LYS A 1 191 ? 48.762  38.049 88.170  1.00 21.28 ? 191  LYS A O   1 
ATOM   1210 C  CB  . LYS A 1 191 ? 46.989  36.746 86.401  1.00 20.20 ? 191  LYS A CB  1 
ATOM   1211 C  CG  . LYS A 1 191 ? 46.246  36.034 85.294  1.00 21.36 ? 191  LYS A CG  1 
ATOM   1212 C  CD  . LYS A 1 191 ? 44.909  35.509 85.811  1.00 30.79 ? 191  LYS A CD  1 
ATOM   1213 C  CE  . LYS A 1 191 ? 44.093  34.829 84.722  1.00 37.76 ? 191  LYS A CE  1 
ATOM   1214 N  NZ  . LYS A 1 191 ? 42.638  34.774 85.088  1.00 42.72 ? 191  LYS A NZ  1 
ATOM   1215 N  N   . GLN A 1 192 ? 49.638  39.343 86.558  1.00 19.66 ? 192  GLN A N   1 
ATOM   1216 C  CA  . GLN A 1 192 ? 50.424  40.145 87.485  1.00 20.24 ? 192  GLN A CA  1 
ATOM   1217 C  C   . GLN A 1 192 ? 50.820  41.426 86.765  1.00 19.69 ? 192  GLN A C   1 
ATOM   1218 O  O   . GLN A 1 192 ? 50.735  41.523 85.538  1.00 20.51 ? 192  GLN A O   1 
ATOM   1219 C  CB  . GLN A 1 192 ? 51.666  39.387 87.975  1.00 17.15 ? 192  GLN A CB  1 
ATOM   1220 C  CG  . GLN A 1 192 ? 52.672  39.042 86.893  1.00 17.35 ? 192  GLN A CG  1 
ATOM   1221 C  CD  . GLN A 1 192 ? 53.691  38.066 87.398  1.00 13.88 ? 192  GLN A CD  1 
ATOM   1222 O  OE1 . GLN A 1 192 ? 53.585  36.867 87.137  1.00 16.87 ? 192  GLN A OE1 1 
ATOM   1223 N  NE2 . GLN A 1 192 ? 54.705  38.563 88.100  1.00 15.69 ? 192  GLN A NE2 1 
ATOM   1224 N  N   . MET A 1 193 ? 51.265  42.406 87.547  1.00 18.86 ? 193  MET A N   1 
ATOM   1225 C  CA  . MET A 1 193 ? 51.738  43.666 86.983  1.00 21.98 ? 193  MET A CA  1 
ATOM   1226 C  C   . MET A 1 193 ? 52.869  43.406 86.001  1.00 18.35 ? 193  MET A C   1 
ATOM   1227 O  O   . MET A 1 193 ? 53.669  42.494 86.175  1.00 19.12 ? 193  MET A O   1 
ATOM   1228 C  CB  . MET A 1 193 ? 52.324  44.539 88.097  1.00 27.56 ? 193  MET A CB  1 
ATOM   1229 C  CG  . MET A 1 193 ? 51.359  44.893 89.194  1.00 31.28 ? 193  MET A CG  1 
ATOM   1230 S  SD  . MET A 1 193 ? 52.186  45.917 90.429  1.00 37.99 ? 193  MET A SD  1 
ATOM   1231 C  CE  . MET A 1 193 ? 52.796  47.282 89.414  1.00 33.98 ? 193  MET A CE  1 
ATOM   1232 N  N   . GLY A 1 194 ? 52.946  44.232 84.963  1.00 18.99 ? 194  GLY A N   1 
ATOM   1233 C  CA  . GLY A 1 194 ? 54.082  44.130 84.061  1.00 18.52 ? 194  GLY A CA  1 
ATOM   1234 C  C   . GLY A 1 194 ? 55.403  44.271 84.799  1.00 16.62 ? 194  GLY A C   1 
ATOM   1235 O  O   . GLY A 1 194 ? 55.536  45.059 85.741  1.00 17.44 ? 194  GLY A O   1 
ATOM   1236 N  N   . ALA A 1 195 ? 56.396  43.504 84.363  1.00 15.59 ? 195  ALA A N   1 
ATOM   1237 C  CA  . ALA A 1 195 ? 57.650  43.446 85.106  1.00 14.08 ? 195  ALA A CA  1 
ATOM   1238 C  C   . ALA A 1 195 ? 58.732  42.829 84.241  1.00 13.83 ? 195  ALA A C   1 
ATOM   1239 O  O   . ALA A 1 195 ? 58.451  42.094 83.282  1.00 14.99 ? 195  ALA A O   1 
ATOM   1240 C  CB  . ALA A 1 195 ? 57.520  42.622 86.395  1.00 15.90 ? 195  ALA A CB  1 
ATOM   1241 N  N   . THR A 1 196 ? 59.981  43.087 84.633  1.00 12.27 ? 196  THR A N   1 
ATOM   1242 C  CA  . THR A 1 196 ? 61.130  42.338 84.136  1.00 13.73 ? 196  THR A CA  1 
ATOM   1243 C  C   . THR A 1 196 ? 61.348  41.146 85.055  1.00 12.71 ? 196  THR A C   1 
ATOM   1244 O  O   . THR A 1 196 ? 61.777  41.312 86.202  1.00 14.55 ? 196  THR A O   1 
ATOM   1245 C  CB  . THR A 1 196 ? 62.380  43.213 84.132  1.00 13.00 ? 196  THR A CB  1 
ATOM   1246 O  OG1 . THR A 1 196 ? 62.130  44.369 83.322  1.00 14.13 ? 196  THR A OG1 1 
ATOM   1247 C  CG2 . THR A 1 196 ? 63.579  42.469 83.548  1.00 15.29 ? 196  THR A CG2 1 
ATOM   1248 N  N   . LEU A 1 197 ? 61.006  39.963 84.580  1.00 12.96 ? 197  LEU A N   1 
ATOM   1249 C  CA  . LEU A 1 197 ? 61.320  38.725 85.266  1.00 12.35 ? 197  LEU A CA  1 
ATOM   1250 C  C   . LEU A 1 197 ? 62.515  38.055 84.600  1.00 11.93 ? 197  LEU A C   1 
ATOM   1251 O  O   . LEU A 1 197 ? 63.098  38.552 83.625  1.00 12.37 ? 197  LEU A O   1 
ATOM   1252 C  CB  . LEU A 1 197 ? 60.107  37.785 85.296  1.00 15.30 ? 197  LEU A CB  1 
ATOM   1253 C  CG  . LEU A 1 197 ? 58.758  38.357 85.732  1.00 14.04 ? 197  LEU A CG  1 
ATOM   1254 C  CD1 . LEU A 1 197 ? 57.719  37.233 85.812  1.00 15.58 ? 197  LEU A CD1 1 
ATOM   1255 C  CD2 . LEU A 1 197 ? 58.903  39.079 87.064  1.00 15.14 ? 197  LEU A CD2 1 
ATOM   1256 N  N   . TRP A 1 198 ? 62.911  36.910 85.135  1.00 11.95 ? 198  TRP A N   1 
ATOM   1257 C  CA  . TRP A 1 198 ? 63.957  36.148 84.473  1.00 11.54 ? 198  TRP A CA  1 
ATOM   1258 C  C   . TRP A 1 198 ? 63.714  34.697 84.808  1.00 11.82 ? 198  TRP A C   1 
ATOM   1259 O  O   . TRP A 1 198 ? 63.063  34.394 85.806  1.00 12.78 ? 198  TRP A O   1 
ATOM   1260 C  CB  . TRP A 1 198 ? 65.350  36.642 84.878  1.00 11.43 ? 198  TRP A CB  1 
ATOM   1261 C  CG  . TRP A 1 198 ? 65.743  36.487 86.327  1.00 10.75 ? 198  TRP A CG  1 
ATOM   1262 C  CD1 . TRP A 1 198 ? 65.159  37.050 87.440  1.00 12.62 ? 198  TRP A CD1 1 
ATOM   1263 C  CD2 . TRP A 1 198 ? 66.883  35.758 86.803  1.00 11.01 ? 198  TRP A CD2 1 
ATOM   1264 N  NE1 . TRP A 1 198 ? 65.868  36.684 88.585  1.00 12.07 ? 198  TRP A NE1 1 
ATOM   1265 C  CE2 . TRP A 1 198 ? 66.924  35.893 88.207  1.00 12.12 ? 198  TRP A CE2 1 
ATOM   1266 C  CE3 . TRP A 1 198 ? 67.866  34.987 86.163  1.00 11.63 ? 198  TRP A CE3 1 
ATOM   1267 C  CZ2 . TRP A 1 198 ? 67.922  35.299 88.984  1.00 11.67 ? 198  TRP A CZ2 1 
ATOM   1268 C  CZ3 . TRP A 1 198 ? 68.858  34.385 86.939  1.00 11.49 ? 198  TRP A CZ3 1 
ATOM   1269 C  CH2 . TRP A 1 198 ? 68.867  34.544 88.339  1.00 11.72 ? 198  TRP A CH2 1 
ATOM   1270 N  N   . TYR A 1 199 ? 64.188  33.805 83.954  1.00 11.73 ? 199  TYR A N   1 
ATOM   1271 C  CA  . TYR A 1 199 ? 64.010  32.375 84.145  1.00 11.64 ? 199  TYR A CA  1 
ATOM   1272 C  C   . TYR A 1 199 ? 65.381  31.736 84.301  1.00 11.69 ? 199  TYR A C   1 
ATOM   1273 O  O   . TYR A 1 199 ? 66.358  32.186 83.698  1.00 11.62 ? 199  TYR A O   1 
ATOM   1274 C  CB  . TYR A 1 199 ? 63.189  31.732 83.017  1.00 12.01 ? 199  TYR A CB  1 
ATOM   1275 C  CG  . TYR A 1 199 ? 63.796  31.817 81.627  1.00 12.32 ? 199  TYR A CG  1 
ATOM   1276 C  CD1 . TYR A 1 199 ? 63.598  32.925 80.817  1.00 12.09 ? 199  TYR A CD1 1 
ATOM   1277 C  CD2 . TYR A 1 199 ? 64.547  30.769 81.117  1.00 12.45 ? 199  TYR A CD2 1 
ATOM   1278 C  CE1 . TYR A 1 199 ? 64.142  33.003 79.530  1.00 12.34 ? 199  TYR A CE1 1 
ATOM   1279 C  CE2 . TYR A 1 199 ? 65.086  30.822 79.833  1.00 12.49 ? 199  TYR A CE2 1 
ATOM   1280 C  CZ  . TYR A 1 199 ? 64.881  31.942 79.042  1.00 13.50 ? 199  TYR A CZ  1 
ATOM   1281 O  OH  . TYR A 1 199 ? 65.434  31.961 77.780  1.00 13.45 ? 199  TYR A OH  1 
ATOM   1282 N  N   . HIS A 1 200 ? 65.462  30.693 85.124  1.00 10.56 ? 200  HIS A N   1 
ATOM   1283 C  CA  . HIS A 1 200 ? 66.755  30.055 85.364  1.00 10.70 ? 200  HIS A CA  1 
ATOM   1284 C  C   . HIS A 1 200 ? 66.544  28.673 85.960  1.00 12.85 ? 200  HIS A C   1 
ATOM   1285 O  O   . HIS A 1 200 ? 65.469  28.331 86.465  1.00 12.20 ? 200  HIS A O   1 
ATOM   1286 C  CB  . HIS A 1 200 ? 67.637  30.912 86.291  1.00 11.38 ? 200  HIS A CB  1 
ATOM   1287 C  CG  . HIS A 1 200 ? 67.064  31.130 87.657  1.00 11.92 ? 200  HIS A CG  1 
ATOM   1288 N  ND1 . HIS A 1 200 ? 67.124  30.185 88.667  1.00 14.20 ? 200  HIS A ND1 1 
ATOM   1289 C  CD2 . HIS A 1 200 ? 66.435  32.204 88.182  1.00 11.33 ? 200  HIS A CD2 1 
ATOM   1290 C  CE1 . HIS A 1 200 ? 66.543  30.674 89.756  1.00 17.19 ? 200  HIS A CE1 1 
ATOM   1291 N  NE2 . HIS A 1 200 ? 66.126  31.903 89.494  1.00 14.30 ? 200  HIS A NE2 1 
ATOM   1292 N  N   . ASP A 1 201 ? 67.609  27.889 85.939  1.00 11.86 ? 201  ASP A N   1 
ATOM   1293 C  CA  . ASP A 1 201 ? 67.492  26.555 86.486  1.00 10.85 ? 201  ASP A CA  1 
ATOM   1294 C  C   . ASP A 1 201 ? 67.347  26.590 88.009  1.00 12.13 ? 201  ASP A C   1 
ATOM   1295 O  O   . ASP A 1 201 ? 67.841  27.496 88.692  1.00 13.34 ? 201  ASP A O   1 
ATOM   1296 C  CB  . ASP A 1 201 ? 68.719  25.735 86.128  1.00 12.38 ? 201  ASP A CB  1 
ATOM   1297 C  CG  . ASP A 1 201 ? 68.518  24.262 86.468  1.00 11.76 ? 201  ASP A CG  1 
ATOM   1298 O  OD1 . ASP A 1 201 ? 67.881  23.580 85.647  1.00 13.60 ? 201  ASP A OD1 1 
ATOM   1299 O  OD2 . ASP A 1 201 ? 68.936  23.829 87.549  1.00 13.51 ? 201  ASP A OD2 1 
ATOM   1300 N  N   . HIS A 1 202 ? 66.657  25.573 88.548  1.00 12.48 ? 202  HIS A N   1 
ATOM   1301 C  CA  . HIS A 1 202 ? 66.378  25.504 89.980  1.00 12.68 ? 202  HIS A CA  1 
ATOM   1302 C  C   . HIS A 1 202 ? 66.472  24.062 90.494  1.00 12.72 ? 202  HIS A C   1 
ATOM   1303 O  O   . HIS A 1 202 ? 65.854  23.736 91.515  1.00 13.45 ? 202  HIS A O   1 
ATOM   1304 C  CB  . HIS A 1 202 ? 64.980  26.112 90.257  1.00 14.49 ? 202  HIS A CB  1 
ATOM   1305 C  CG  . HIS A 1 202 ? 64.834  26.800 91.580  1.00 15.19 ? 202  HIS A CG  1 
ATOM   1306 N  ND1 . HIS A 1 202 ? 65.261  26.267 92.774  1.00 27.35 ? 202  HIS A ND1 1 
ATOM   1307 C  CD2 . HIS A 1 202 ? 64.249  27.986 91.889  1.00 23.60 ? 202  HIS A CD2 1 
ATOM   1308 C  CE1 . HIS A 1 202 ? 64.955  27.098 93.760  1.00 19.08 ? 202  HIS A CE1 1 
ATOM   1309 N  NE2 . HIS A 1 202 ? 64.347  28.147 93.250  1.00 23.69 ? 202  HIS A NE2 1 
ATOM   1310 N  N   . ALA A 1 203 ? 67.212  23.170 89.821  1.00 12.36 ? 203  ALA A N   1 
ATOM   1311 C  CA  . ALA A 1 203 ? 67.209  21.769 90.238  1.00 12.95 ? 203  ALA A CA  1 
ATOM   1312 C  C   . ALA A 1 203 ? 67.885  21.573 91.595  1.00 13.07 ? 203  ALA A C   1 
ATOM   1313 O  O   . ALA A 1 203 ? 68.985  22.082 91.844  1.00 13.12 ? 203  ALA A O   1 
ATOM   1314 C  CB  . ALA A 1 203 ? 67.910  20.913 89.196  1.00 14.14 ? 203  ALA A CB  1 
ATOM   1315 N  N   . ILE A 1 204 ? 67.246  20.790 92.465  1.00 13.17 ? 204  ILE A N   1 
ATOM   1316 C  CA  . ILE A 1 204 ? 67.742  20.689 93.831  1.00 12.48 ? 204  ILE A CA  1 
ATOM   1317 C  C   . ILE A 1 204 ? 69.150  20.103 93.837  1.00 12.85 ? 204  ILE A C   1 
ATOM   1318 O  O   . ILE A 1 204 ? 69.465  19.164 93.088  1.00 14.37 ? 204  ILE A O   1 
ATOM   1319 C  CB  . ILE A 1 204 ? 66.770  19.915 94.739  1.00 13.14 ? 204  ILE A CB  1 
ATOM   1320 C  CG1 . ILE A 1 204 ? 67.073  20.233 96.203  1.00 13.86 ? 204  ILE A CG1 1 
ATOM   1321 C  CG2 . ILE A 1 204 ? 66.793  18.406 94.424  1.00 13.17 ? 204  ILE A CG2 1 
ATOM   1322 C  CD1 . ILE A 1 204 ? 66.005  19.668 97.172  1.00 17.22 ? 204  ILE A CD1 1 
ATOM   1323 N  N   . GLY A 1 205 ? 70.005  20.660 94.702  1.00 12.06 ? 205  GLY A N   1 
ATOM   1324 C  CA  . GLY A 1 205 ? 71.354  20.154 94.917  1.00 13.41 ? 205  GLY A CA  1 
ATOM   1325 C  C   . GLY A 1 205 ? 72.416  20.696 93.973  1.00 13.23 ? 205  GLY A C   1 
ATOM   1326 O  O   . GLY A 1 205 ? 73.613  20.583 94.281  1.00 13.93 ? 205  GLY A O   1 
ATOM   1327 N  N   . ILE A 1 206 ? 72.025  21.236 92.822  1.00 12.37 ? 206  ILE A N   1 
ATOM   1328 C  CA  . ILE A 1 206 ? 72.971  21.629 91.788  1.00 12.58 ? 206  ILE A CA  1 
ATOM   1329 C  C   . ILE A 1 206 ? 72.591  22.950 91.137  1.00 13.26 ? 206  ILE A C   1 
ATOM   1330 O  O   . ILE A 1 206 ? 73.066  23.250 90.041  1.00 12.22 ? 206  ILE A O   1 
ATOM   1331 C  CB  . ILE A 1 206 ? 73.171  20.535 90.728  1.00 11.47 ? 206  ILE A CB  1 
ATOM   1332 C  CG1 . ILE A 1 206 ? 71.846  20.215 90.011  1.00 13.57 ? 206  ILE A CG1 1 
ATOM   1333 C  CG2 . ILE A 1 206 ? 73.858  19.295 91.336  1.00 15.43 ? 206  ILE A CG2 1 
ATOM   1334 C  CD1 . ILE A 1 206 ? 72.040  19.267 88.828  1.00 14.53 ? 206  ILE A CD1 1 
ATOM   1335 N  N   . THR A 1 207 ? 71.707  23.729 91.778  1.00 12.77 ? 207  THR A N   1 
ATOM   1336 C  CA  . THR A 1 207 ? 71.254  24.966 91.163  1.00 11.10 ? 207  THR A CA  1 
ATOM   1337 C  C   . THR A 1 207 ? 72.435  25.889 90.880  1.00 10.59 ? 207  THR A C   1 
ATOM   1338 O  O   . THR A 1 207 ? 72.488  26.537 89.828  1.00 11.53 ? 207  THR A O   1 
ATOM   1339 C  CB  . THR A 1 207 ? 70.226  25.642 92.065  1.00 12.82 ? 207  THR A CB  1 
ATOM   1340 O  OG1 . THR A 1 207 ? 69.031  24.850 92.048  1.00 14.43 ? 207  THR A OG1 1 
ATOM   1341 C  CG2 . THR A 1 207 ? 69.875  27.023 91.528  1.00 12.86 ? 207  THR A CG2 1 
ATOM   1342 N  N   . ARG A 1 208 ? 73.383  25.969 91.816  1.00 11.78 ? 208  ARG A N   1 
ATOM   1343 C  CA  . ARG A 1 208 ? 74.540  26.846 91.620  1.00 11.87 ? 208  ARG A CA  1 
ATOM   1344 C  C   . ARG A 1 208 ? 75.329  26.458 90.369  1.00 12.57 ? 208  ARG A C   1 
ATOM   1345 O  O   . ARG A 1 208 ? 75.874  27.330 89.663  1.00 12.74 ? 208  ARG A O   1 
ATOM   1346 C  CB  . ARG A 1 208 ? 75.449  26.816 92.863  1.00 12.55 ? 208  ARG A CB  1 
ATOM   1347 C  CG  . ARG A 1 208 ? 76.286  25.513 93.002  1.00 12.61 ? 208  ARG A CG  1 
ATOM   1348 C  CD  . ARG A 1 208 ? 76.776  25.297 94.424  1.00 12.32 ? 208  ARG A CD  1 
ATOM   1349 N  NE  . ARG A 1 208 ? 77.533  24.049 94.552  1.00 12.95 ? 208  ARG A NE  1 
ATOM   1350 C  CZ  . ARG A 1 208 ? 76.966  22.842 94.557  1.00 11.99 ? 208  ARG A CZ  1 
ATOM   1351 N  NH1 . ARG A 1 208 ? 75.638  22.691 94.488  1.00 12.65 ? 208  ARG A NH1 1 
ATOM   1352 N  NH2 . ARG A 1 208 ? 77.740  21.762 94.663  1.00 13.68 ? 208  ARG A NH2 1 
ATOM   1353 N  N   . LEU A 1 209 ? 75.394  25.158 90.077  1.00 11.48 ? 209  LEU A N   1 
ATOM   1354 C  CA  . LEU A 1 209 ? 76.166  24.686 88.925  1.00 11.36 ? 209  LEU A CA  1 
ATOM   1355 C  C   . LEU A 1 209 ? 75.406  24.926 87.632  1.00 11.08 ? 209  LEU A C   1 
ATOM   1356 O  O   . LEU A 1 209 ? 75.995  25.315 86.621  1.00 13.32 ? 209  LEU A O   1 
ATOM   1357 C  CB  . LEU A 1 209 ? 76.415  23.182 89.068  1.00 12.86 ? 209  LEU A CB  1 
ATOM   1358 C  CG  . LEU A 1 209 ? 77.077  22.694 90.369  1.00 12.22 ? 209  LEU A CG  1 
ATOM   1359 C  CD1 . LEU A 1 209 ? 77.241  21.168 90.368  1.00 12.36 ? 209  LEU A CD1 1 
ATOM   1360 C  CD2 . LEU A 1 209 ? 78.422  23.395 90.624  1.00 15.42 ? 209  LEU A CD2 1 
ATOM   1361 N  N   . ASN A 1 210 ? 74.097  24.686 87.640  1.00 10.63 ? 210  ASN A N   1 
ATOM   1362 C  CA  . ASN A 1 210 ? 73.340  24.806 86.405  1.00 11.25 ? 210  ASN A CA  1 
ATOM   1363 C  C   . ASN A 1 210 ? 73.202  26.267 85.989  1.00 11.39 ? 210  ASN A C   1 
ATOM   1364 O  O   . ASN A 1 210 ? 73.314  26.586 84.798  1.00 12.81 ? 210  ASN A O   1 
ATOM   1365 C  CB  . ASN A 1 210 ? 71.963  24.147 86.600  1.00 11.76 ? 210  ASN A CB  1 
ATOM   1366 C  CG  . ASN A 1 210 ? 72.056  22.629 86.650  1.00 12.39 ? 210  ASN A CG  1 
ATOM   1367 O  OD1 . ASN A 1 210 ? 73.131  22.066 86.445  1.00 14.45 ? 210  ASN A OD1 1 
ATOM   1368 N  ND2 . ASN A 1 210 ? 70.954  21.967 86.935  1.00 12.80 ? 210  ASN A ND2 1 
ATOM   1369 N  N   . VAL A 1 211 ? 72.994  27.171 86.954  1.00 10.50 ? 211  VAL A N   1 
ATOM   1370 C  CA  . VAL A 1 211 ? 72.975  28.597 86.611  1.00 11.45 ? 211  VAL A CA  1 
ATOM   1371 C  C   . VAL A 1 211 ? 74.360  29.070 86.168  1.00 11.90 ? 211  VAL A C   1 
ATOM   1372 O  O   . VAL A 1 211 ? 74.485  29.775 85.154  1.00 11.79 ? 211  VAL A O   1 
ATOM   1373 C  CB  . VAL A 1 211 ? 72.367  29.440 87.751  1.00 10.89 ? 211  VAL A CB  1 
ATOM   1374 C  CG1 . VAL A 1 211 ? 72.421  30.959 87.415  1.00 13.43 ? 211  VAL A CG1 1 
ATOM   1375 C  CG2 . VAL A 1 211 ? 70.922  28.983 88.008  1.00 11.55 ? 211  VAL A CG2 1 
ATOM   1376 N  N   . TYR A 1 212 ? 75.424  28.686 86.887  1.00 10.91 ? 212  TYR A N   1 
ATOM   1377 C  CA  . TYR A 1 212 ? 76.746  29.146 86.467  1.00 11.48 ? 212  TYR A CA  1 
ATOM   1378 C  C   . TYR A 1 212 ? 77.077  28.662 85.058  1.00 11.96 ? 212  TYR A C   1 
ATOM   1379 O  O   . TYR A 1 212 ? 77.704  29.389 84.276  1.00 12.39 ? 212  TYR A O   1 
ATOM   1380 C  CB  . TYR A 1 212 ? 77.787  28.609 87.450  1.00 10.96 ? 212  TYR A CB  1 
ATOM   1381 C  CG  . TYR A 1 212 ? 79.170  29.213 87.307  1.00 10.93 ? 212  TYR A CG  1 
ATOM   1382 C  CD1 . TYR A 1 212 ? 79.443  30.504 87.774  1.00 13.36 ? 212  TYR A CD1 1 
ATOM   1383 C  CD2 . TYR A 1 212 ? 80.181  28.526 86.654  1.00 12.26 ? 212  TYR A CD2 1 
ATOM   1384 C  CE1 . TYR A 1 212 ? 80.723  31.070 87.642  1.00 12.49 ? 212  TYR A CE1 1 
ATOM   1385 C  CE2 . TYR A 1 212 ? 81.461  29.084 86.521  1.00 11.83 ? 212  TYR A CE2 1 
ATOM   1386 C  CZ  . TYR A 1 212 ? 81.712  30.357 87.005  1.00 11.39 ? 212  TYR A CZ  1 
ATOM   1387 O  OH  . TYR A 1 212 ? 82.962  30.913 86.889  1.00 14.16 ? 212  TYR A OH  1 
ATOM   1388 N  N   . SER A 1 213 ? 76.619  27.458 84.698  1.00 11.60 ? 213  SER A N   1 
ATOM   1389 C  CA  . SER A 1 213 ? 76.907  26.919 83.373  1.00 11.58 ? 213  SER A CA  1 
ATOM   1390 C  C   . SER A 1 213 ? 76.251  27.693 82.240  1.00 11.34 ? 213  SER A C   1 
ATOM   1391 O  O   . SER A 1 213 ? 76.650  27.499 81.090  1.00 12.61 ? 213  SER A O   1 
ATOM   1392 C  CB  . SER A 1 213 ? 76.484  25.451 83.288  1.00 13.29 ? 213  SER A CB  1 
ATOM   1393 O  OG  . SER A 1 213 ? 77.243  24.658 84.187  1.00 16.21 ? 213  SER A OG  1 
ATOM   1394 N  N   . GLY A 1 214 ? 75.263  28.544 82.531  1.00 11.49 ? 214  GLY A N   1 
ATOM   1395 C  CA  . GLY A 1 214 ? 74.688  29.415 81.526  1.00 12.37 ? 214  GLY A CA  1 
ATOM   1396 C  C   . GLY A 1 214 ? 73.175  29.424 81.456  1.00 11.57 ? 214  GLY A C   1 
ATOM   1397 O  O   . GLY A 1 214 ? 72.621  30.134 80.611  1.00 13.08 ? 214  GLY A O   1 
ATOM   1398 N  N   . LEU A 1 215 ? 72.483  28.668 82.318  1.00 11.58 ? 215  LEU A N   1 
ATOM   1399 C  CA  . LEU A 1 215 ? 71.029  28.499 82.172  1.00 12.42 ? 215  LEU A CA  1 
ATOM   1400 C  C   . LEU A 1 215 ? 70.244  29.627 82.872  1.00 10.41 ? 215  LEU A C   1 
ATOM   1401 O  O   . LEU A 1 215 ? 69.725  29.471 83.986  1.00 12.82 ? 215  LEU A O   1 
ATOM   1402 C  CB  . LEU A 1 215 ? 70.623  27.117 82.673  1.00 11.64 ? 215  LEU A CB  1 
ATOM   1403 C  CG  . LEU A 1 215 ? 71.168  25.966 81.821  1.00 11.96 ? 215  LEU A CG  1 
ATOM   1404 C  CD1 . LEU A 1 215 ? 70.802  24.651 82.517  1.00 15.09 ? 215  LEU A CD1 1 
ATOM   1405 C  CD2 . LEU A 1 215 ? 70.625  25.991 80.399  1.00 14.54 ? 215  LEU A CD2 1 
ATOM   1406 N  N   . SER A 1 216 ? 70.132  30.774 82.183  1.00 11.54 ? 216  SER A N   1 
ATOM   1407 C  CA  . SER A 1 216 ? 69.280  31.890 82.616  1.00 11.83 ? 216  SER A CA  1 
ATOM   1408 C  C   . SER A 1 216 ? 68.927  32.729 81.395  1.00 12.47 ? 216  SER A C   1 
ATOM   1409 O  O   . SER A 1 216 ? 69.678  32.749 80.418  1.00 13.04 ? 216  SER A O   1 
ATOM   1410 C  CB  . SER A 1 216 ? 69.986  32.785 83.644  1.00 13.27 ? 216  SER A CB  1 
ATOM   1411 O  OG  . SER A 1 216 ? 71.197  33.259 83.111  1.00 14.43 ? 216  SER A OG  1 
ATOM   1412 N  N   . GLY A 1 217 ? 67.802  33.440 81.470  1.00 10.67 ? 217  GLY A N   1 
ATOM   1413 C  CA  . GLY A 1 217 ? 67.377  34.339 80.402  1.00 11.64 ? 217  GLY A CA  1 
ATOM   1414 C  C   . GLY A 1 217 ? 66.338  35.301 80.940  1.00 11.12 ? 217  GLY A C   1 
ATOM   1415 O  O   . GLY A 1 217 ? 65.860  35.163 82.068  1.00 12.43 ? 217  GLY A O   1 
ATOM   1416 N  N   . PHE A 1 218 ? 65.972  36.277 80.121  1.00 11.00 ? 218  PHE A N   1 
ATOM   1417 C  CA  . PHE A 1 218 ? 64.977  37.275 80.539  1.00 11.66 ? 218  PHE A CA  1 
ATOM   1418 C  C   . PHE A 1 218 ? 63.569  36.881 80.114  1.00 12.32 ? 218  PHE A C   1 
ATOM   1419 O  O   . PHE A 1 218 ? 63.363  36.216 79.083  1.00 12.86 ? 218  PHE A O   1 
ATOM   1420 C  CB  . PHE A 1 218 ? 65.271  38.632 79.889  1.00 12.15 ? 218  PHE A CB  1 
ATOM   1421 C  CG  . PHE A 1 218 ? 66.393  39.389 80.523  1.00 12.15 ? 218  PHE A CG  1 
ATOM   1422 C  CD1 . PHE A 1 218 ? 66.165  40.209 81.617  1.00 12.52 ? 218  PHE A CD1 1 
ATOM   1423 C  CD2 . PHE A 1 218 ? 67.668  39.334 79.970  1.00 12.36 ? 218  PHE A CD2 1 
ATOM   1424 C  CE1 . PHE A 1 218 ? 67.192  40.947 82.189  1.00 13.76 ? 218  PHE A CE1 1 
ATOM   1425 C  CE2 . PHE A 1 218 ? 68.720  40.054 80.544  1.00 13.21 ? 218  PHE A CE2 1 
ATOM   1426 C  CZ  . PHE A 1 218 ? 68.475  40.877 81.652  1.00 12.60 ? 218  PHE A CZ  1 
ATOM   1427 N  N   . TYR A 1 219 ? 62.580  37.352 80.891  1.00 11.17 ? 219  TYR A N   1 
ATOM   1428 C  CA  . TYR A 1 219 ? 61.174  37.112 80.575  1.00 12.19 ? 219  TYR A CA  1 
ATOM   1429 C  C   . TYR A 1 219 ? 60.448  38.398 80.924  1.00 12.84 ? 219  TYR A C   1 
ATOM   1430 O  O   . TYR A 1 219 ? 60.451  38.816 82.084  1.00 14.17 ? 219  TYR A O   1 
ATOM   1431 C  CB  . TYR A 1 219 ? 60.654  35.963 81.429  1.00 11.24 ? 219  TYR A CB  1 
ATOM   1432 C  CG  . TYR A 1 219 ? 59.221  35.517 81.236  1.00 12.01 ? 219  TYR A CG  1 
ATOM   1433 C  CD1 . TYR A 1 219 ? 58.159  36.262 81.734  1.00 14.76 ? 219  TYR A CD1 1 
ATOM   1434 C  CD2 . TYR A 1 219 ? 58.940  34.279 80.647  1.00 13.43 ? 219  TYR A CD2 1 
ATOM   1435 C  CE1 . TYR A 1 219 ? 56.833  35.804 81.611  1.00 14.12 ? 219  TYR A CE1 1 
ATOM   1436 C  CE2 . TYR A 1 219 ? 57.639  33.811 80.518  1.00 14.19 ? 219  TYR A CE2 1 
ATOM   1437 C  CZ  . TYR A 1 219 ? 56.597  34.566 81.003  1.00 13.23 ? 219  TYR A CZ  1 
ATOM   1438 O  OH  . TYR A 1 219 ? 55.311  34.079 80.899  1.00 16.08 ? 219  TYR A OH  1 
ATOM   1439 N  N   . LEU A 1 220 ? 59.851  39.050 79.935  1.00 13.43 ? 220  LEU A N   1 
ATOM   1440 C  CA  . LEU A 1 220 ? 59.305  40.386 80.112  1.00 15.45 ? 220  LEU A CA  1 
ATOM   1441 C  C   . LEU A 1 220 ? 57.791  40.349 79.988  1.00 15.77 ? 220  LEU A C   1 
ATOM   1442 O  O   . LEU A 1 220 ? 57.260  39.908 78.958  1.00 16.27 ? 220  LEU A O   1 
ATOM   1443 C  CB  . LEU A 1 220 ? 59.889  41.355 79.080  1.00 15.18 ? 220  LEU A CB  1 
ATOM   1444 C  CG  . LEU A 1 220 ? 61.404  41.273 78.909  1.00 14.17 ? 220  LEU A CG  1 
ATOM   1445 C  CD1 . LEU A 1 220 ? 61.845  42.299 77.875  1.00 16.33 ? 220  LEU A CD1 1 
ATOM   1446 C  CD2 . LEU A 1 220 ? 62.146  41.465 80.250  1.00 15.27 ? 220  LEU A CD2 1 
ATOM   1447 N  N   . ILE A 1 221 ? 57.093  40.838 81.013  1.00 14.12 ? 221  ILE A N   1 
ATOM   1448 C  CA  . ILE A 1 221 ? 55.640  40.971 80.976  1.00 15.54 ? 221  ILE A CA  1 
ATOM   1449 C  C   . ILE A 1 221 ? 55.326  42.439 80.732  1.00 14.91 ? 221  ILE A C   1 
ATOM   1450 O  O   . ILE A 1 221 ? 55.671  43.294 81.558  1.00 17.86 ? 221  ILE A O   1 
ATOM   1451 C  CB  . ILE A 1 221 ? 54.987  40.490 82.285  1.00 14.33 ? 221  ILE A CB  1 
ATOM   1452 C  CG1 . ILE A 1 221 ? 55.373  39.035 82.589  1.00 14.66 ? 221  ILE A CG1 1 
ATOM   1453 C  CG2 . ILE A 1 221 ? 53.463  40.701 82.221  1.00 18.01 ? 221  ILE A CG2 1 
ATOM   1454 C  CD1 . ILE A 1 221 ? 54.833  38.540 83.943  1.00 16.59 ? 221  ILE A CD1 1 
ATOM   1455 N  N   . GLU A 1 222 ? 54.682  42.747 79.600  1.00 16.31 ? 222  GLU A N   1 
ATOM   1456 C  CA  . GLU A 1 222 ? 54.352  44.127 79.288  1.00 16.91 ? 222  GLU A CA  1 
ATOM   1457 C  C   . GLU A 1 222 ? 53.076  44.543 80.014  1.00 24.02 ? 222  GLU A C   1 
ATOM   1458 O  O   . GLU A 1 222 ? 52.046  43.866 79.918  1.00 24.18 ? 222  GLU A O   1 
ATOM   1459 C  CB  . GLU A 1 222 ? 54.181  44.312 77.783  1.00 23.76 ? 222  GLU A CB  1 
ATOM   1460 C  CG  . GLU A 1 222 ? 53.871  45.761 77.418  1.00 22.32 ? 222  GLU A CG  1 
ATOM   1461 C  CD  . GLU A 1 222 ? 53.674  45.977 75.922  1.00 29.51 ? 222  GLU A CD  1 
ATOM   1462 O  OE1 . GLU A 1 222 ? 54.035  45.089 75.124  1.00 29.40 ? 222  GLU A OE1 1 
ATOM   1463 O  OE2 . GLU A 1 222 ? 53.128  47.037 75.552  1.00 36.14 ? 222  GLU A OE2 1 
ATOM   1464 N  N   . ASP A 1 223 ? 53.141  45.670 80.743  1.00 20.54 ? 223  ASP A N   1 
ATOM   1465 C  CA  . ASP A 1 223 ? 51.943  46.164 81.416  1.00 23.64 ? 223  ASP A CA  1 
ATOM   1466 C  C   . ASP A 1 223 ? 51.060  46.930 80.436  1.00 26.76 ? 223  ASP A C   1 
ATOM   1467 O  O   . ASP A 1 223 ? 51.568  47.627 79.553  1.00 23.94 ? 223  ASP A O   1 
ATOM   1468 C  CB  . ASP A 1 223 ? 52.336  47.075 82.579  1.00 25.47 ? 223  ASP A CB  1 
ATOM   1469 C  CG  . ASP A 1 223 ? 51.211  47.272 83.574  1.00 29.97 ? 223  ASP A CG  1 
ATOM   1470 O  OD1 . ASP A 1 223 ? 50.317  48.120 83.321  1.00 28.00 ? 223  ASP A OD1 1 
ATOM   1471 O  OD2 . ASP A 1 223 ? 51.181  46.513 84.574  1.00 28.18 ? 223  ASP A OD2 1 
ATOM   1472 N  N   . PRO A 1 224 ? 49.733  46.836 80.582  1.00 27.31 ? 224  PRO A N   1 
ATOM   1473 C  CA  . PRO A 1 224 ? 48.845  47.572 79.666  1.00 26.73 ? 224  PRO A CA  1 
ATOM   1474 C  C   . PRO A 1 224 ? 49.040  49.079 79.710  1.00 29.25 ? 224  PRO A C   1 
ATOM   1475 O  O   . PRO A 1 224 ? 48.710  49.770 78.739  1.00 30.01 ? 224  PRO A O   1 
ATOM   1476 C  CB  . PRO A 1 224 ? 47.436  47.169 80.130  1.00 33.08 ? 224  PRO A CB  1 
ATOM   1477 C  CG  . PRO A 1 224 ? 47.633  46.586 81.514  1.00 32.78 ? 224  PRO A CG  1 
ATOM   1478 C  CD  . PRO A 1 224 ? 48.977  45.929 81.460  1.00 29.10 ? 224  PRO A CD  1 
ATOM   1479 N  N   . VAL A 1 225 ? 49.587  49.604 80.805  1.00 24.86 ? 225  VAL A N   1 
ATOM   1480 C  CA  . VAL A 1 225 ? 49.808  51.040 80.925  1.00 30.04 ? 225  VAL A CA  1 
ATOM   1481 C  C   . VAL A 1 225 ? 50.836  51.531 79.906  1.00 28.31 ? 225  VAL A C   1 
ATOM   1482 O  O   . VAL A 1 225 ? 50.758  52.669 79.419  1.00 35.03 ? 225  VAL A O   1 
ATOM   1483 C  CB  . VAL A 1 225 ? 50.194  51.335 82.389  1.00 35.91 ? 225  VAL A CB  1 
ATOM   1484 C  CG1 . VAL A 1 225 ? 51.701  51.113 82.642  1.00 28.08 ? 225  VAL A CG1 1 
ATOM   1485 C  CG2 . VAL A 1 225 ? 49.750  52.691 82.794  1.00 46.42 ? 225  VAL A CG2 1 
ATOM   1486 N  N   . GLU A 1 226 ? 51.779  50.675 79.524  1.00 26.99 ? 226  GLU A N   1 
ATOM   1487 C  CA  . GLU A 1 226 ? 52.916  51.137 78.737  1.00 26.86 ? 226  GLU A CA  1 
ATOM   1488 C  C   . GLU A 1 226 ? 52.504  51.614 77.351  1.00 32.27 ? 226  GLU A C   1 
ATOM   1489 O  O   . GLU A 1 226 ? 53.160  52.492 76.786  1.00 29.55 ? 226  GLU A O   1 
ATOM   1490 C  CB  . GLU A 1 226 ? 53.949  50.026 78.632  1.00 27.99 ? 226  GLU A CB  1 
ATOM   1491 C  CG  . GLU A 1 226 ? 54.596  49.717 79.968  1.00 28.83 ? 226  GLU A CG  1 
ATOM   1492 C  CD  . GLU A 1 226 ? 55.533  48.559 79.883  1.00 28.21 ? 226  GLU A CD  1 
ATOM   1493 O  OE1 . GLU A 1 226 ? 56.555  48.710 79.183  1.00 25.31 ? 226  GLU A OE1 1 
ATOM   1494 O  OE2 . GLU A 1 226 ? 55.238  47.498 80.492  1.00 26.23 ? 226  GLU A OE2 1 
ATOM   1495 N  N   . LYS A 1 227 ? 51.428  51.049 76.794  1.00 35.07 ? 227  LYS A N   1 
ATOM   1496 C  CA  . LYS A 1 227 ? 50.960  51.466 75.478  1.00 43.79 ? 227  LYS A CA  1 
ATOM   1497 C  C   . LYS A 1 227 ? 50.634  52.948 75.440  1.00 40.85 ? 227  LYS A C   1 
ATOM   1498 O  O   . LYS A 1 227 ? 50.675  53.561 74.366  1.00 46.65 ? 227  LYS A O   1 
ATOM   1499 C  CB  . LYS A 1 227 ? 49.725  50.662 75.074  1.00 39.54 ? 227  LYS A CB  1 
ATOM   1500 C  CG  . LYS A 1 227 ? 49.839  50.019 73.706  1.00 48.06 ? 227  LYS A CG  1 
ATOM   1501 C  CD  . LYS A 1 227 ? 48.535  49.340 73.282  1.00 51.28 ? 227  LYS A CD  1 
ATOM   1502 C  CE  . LYS A 1 227 ? 47.552  49.210 74.445  1.00 45.23 ? 227  LYS A CE  1 
ATOM   1503 N  NZ  . LYS A 1 227 ? 47.758  47.907 75.155  1.00 53.74 ? 227  LYS A NZ  1 
ATOM   1504 N  N   . HIS A 1 228 ? 50.301  53.548 76.585  1.00 36.87 ? 228  HIS A N   1 
ATOM   1505 C  CA  . HIS A 1 228 ? 49.942  54.960 76.597  1.00 39.78 ? 228  HIS A CA  1 
ATOM   1506 C  C   . HIS A 1 228 ? 50.949  55.828 77.351  1.00 36.16 ? 228  HIS A C   1 
ATOM   1507 O  O   . HIS A 1 228 ? 50.687  57.009 77.602  1.00 43.78 ? 228  HIS A O   1 
ATOM   1508 C  CB  . HIS A 1 228 ? 48.505  55.131 77.090  1.00 46.89 ? 228  HIS A CB  1 
ATOM   1509 C  CG  . HIS A 1 228 ? 47.486  54.479 76.201  1.00 56.25 ? 228  HIS A CG  1 
ATOM   1510 N  ND1 . HIS A 1 228 ? 47.448  54.683 74.836  1.00 54.58 ? 228  HIS A ND1 1 
ATOM   1511 C  CD2 . HIS A 1 228 ? 46.487  53.606 76.477  1.00 54.16 ? 228  HIS A CD2 1 
ATOM   1512 C  CE1 . HIS A 1 228 ? 46.457  53.979 74.315  1.00 54.29 ? 228  HIS A CE1 1 
ATOM   1513 N  NE2 . HIS A 1 228 ? 45.860  53.314 75.289  1.00 56.33 ? 228  HIS A NE2 1 
ATOM   1514 N  N   . LEU A 1 229 ? 52.094  55.264 77.710  1.00 29.96 ? 229  LEU A N   1 
ATOM   1515 C  CA  . LEU A 1 229 ? 53.264  56.001 78.150  1.00 28.25 ? 229  LEU A CA  1 
ATOM   1516 C  C   . LEU A 1 229 ? 54.208  56.128 76.958  1.00 33.89 ? 229  LEU A C   1 
ATOM   1517 O  O   . LEU A 1 229 ? 53.993  55.536 75.895  1.00 31.97 ? 229  LEU A O   1 
ATOM   1518 C  CB  . LEU A 1 229 ? 53.979  55.223 79.266  1.00 30.35 ? 229  LEU A CB  1 
ATOM   1519 C  CG  . LEU A 1 229 ? 53.407  55.247 80.691  1.00 34.53 ? 229  LEU A CG  1 
ATOM   1520 C  CD1 . LEU A 1 229 ? 54.217  54.339 81.589  1.00 31.80 ? 229  LEU A CD1 1 
ATOM   1521 C  CD2 . LEU A 1 229 ? 53.363  56.662 81.252  1.00 38.21 ? 229  LEU A CD2 1 
ATOM   1522 N  N   . LYS A 1 230 ? 55.280  56.893 77.150  1.00 25.46 ? 230  LYS A N   1 
ATOM   1523 C  CA  . LYS A 1 230 ? 56.259  57.098 76.092  1.00 24.71 ? 230  LYS A CA  1 
ATOM   1524 C  C   . LYS A 1 230 ? 57.638  56.707 76.607  1.00 22.33 ? 230  LYS A C   1 
ATOM   1525 O  O   . LYS A 1 230 ? 58.607  57.453 76.437  1.00 25.78 ? 230  LYS A O   1 
ATOM   1526 C  CB  . LYS A 1 230 ? 56.242  58.550 75.616  1.00 25.65 ? 230  LYS A CB  1 
ATOM   1527 C  CG  . LYS A 1 230 ? 54.893  58.992 75.063  1.00 25.86 ? 230  LYS A CG  1 
ATOM   1528 C  CD  . LYS A 1 230 ? 54.987  60.382 74.467  1.00 31.59 ? 230  LYS A CD  1 
ATOM   1529 C  CE  . LYS A 1 230 ? 53.781  60.677 73.582  1.00 32.58 ? 230  LYS A CE  1 
ATOM   1530 N  NZ  . LYS A 1 230 ? 53.897  62.014 72.929  1.00 43.66 ? 230  LYS A NZ  1 
ATOM   1531 N  N   . LEU A 1 231 ? 57.729  55.551 77.259  1.00 20.65 ? 231  LEU A N   1 
ATOM   1532 C  CA  . LEU A 1 231 ? 59.021  55.072 77.717  1.00 20.43 ? 231  LEU A CA  1 
ATOM   1533 C  C   . LEU A 1 231 ? 59.876  54.694 76.508  1.00 24.82 ? 231  LEU A C   1 
ATOM   1534 O  O   . LEU A 1 231 ? 59.344  54.346 75.455  1.00 24.39 ? 231  LEU A O   1 
ATOM   1535 C  CB  . LEU A 1 231 ? 58.836  53.837 78.588  1.00 21.31 ? 231  LEU A CB  1 
ATOM   1536 C  CG  . LEU A 1 231 ? 58.011  54.052 79.862  1.00 22.64 ? 231  LEU A CG  1 
ATOM   1537 C  CD1 . LEU A 1 231 ? 57.799  52.751 80.576  1.00 23.43 ? 231  LEU A CD1 1 
ATOM   1538 C  CD2 . LEU A 1 231 ? 58.683  55.052 80.784  1.00 24.26 ? 231  LEU A CD2 1 
ATOM   1539 N  N   . PRO A 1 232 ? 61.202  54.766 76.621  1.00 21.37 ? 232  PRO A N   1 
ATOM   1540 C  CA  . PRO A 1 232 ? 62.040  54.293 75.513  1.00 18.28 ? 232  PRO A CA  1 
ATOM   1541 C  C   . PRO A 1 232 ? 61.709  52.842 75.210  1.00 19.01 ? 232  PRO A C   1 
ATOM   1542 O  O   . PRO A 1 232 ? 61.524  52.032 76.114  1.00 20.37 ? 232  PRO A O   1 
ATOM   1543 C  CB  . PRO A 1 232 ? 63.474  54.433 76.054  1.00 20.23 ? 232  PRO A CB  1 
ATOM   1544 C  CG  . PRO A 1 232 ? 63.369  55.495 77.139  1.00 20.03 ? 232  PRO A CG  1 
ATOM   1545 C  CD  . PRO A 1 232 ? 61.986  55.376 77.714  1.00 24.41 ? 232  PRO A CD  1 
ATOM   1546 N  N   . LYS A 1 233 ? 61.634  52.512 73.925  1.00 18.84 ? 233  LYS A N   1 
ATOM   1547 C  CA  . LYS A 1 233 ? 61.149  51.207 73.507  1.00 22.08 ? 233  LYS A CA  1 
ATOM   1548 C  C   . LYS A 1 233 ? 61.990  50.666 72.359  1.00 22.12 ? 233  LYS A C   1 
ATOM   1549 O  O   . LYS A 1 233 ? 62.888  51.334 71.837  1.00 20.92 ? 233  LYS A O   1 
ATOM   1550 C  CB  . LYS A 1 233 ? 59.667  51.235 73.097  1.00 24.86 ? 233  LYS A CB  1 
ATOM   1551 C  CG  . LYS A 1 233 ? 59.349  52.238 72.047  1.00 29.85 ? 233  LYS A CG  1 
ATOM   1552 C  CD  . LYS A 1 233 ? 57.832  52.346 71.885  1.00 37.20 ? 233  LYS A CD  1 
ATOM   1553 C  CE  . LYS A 1 233 ? 57.106  52.226 73.235  1.00 42.95 ? 233  LYS A CE  1 
ATOM   1554 N  NZ  . LYS A 1 233 ? 57.044  53.541 73.978  1.00 35.81 ? 233  LYS A NZ  1 
ATOM   1555 N  N   . ASP A 1 234 ? 61.702  49.412 72.001  1.00 22.87 ? 234  ASP A N   1 
ATOM   1556 C  CA  . ASP A 1 234 ? 62.301  48.743 70.841  1.00 25.13 ? 234  ASP A CA  1 
ATOM   1557 C  C   . ASP A 1 234 ? 63.810  48.696 71.031  1.00 22.38 ? 234  ASP A C   1 
ATOM   1558 O  O   . ASP A 1 234 ? 64.253  48.193 72.077  1.00 20.41 ? 234  ASP A O   1 
ATOM   1559 C  CB  . ASP A 1 234 ? 61.781  49.342 69.537  1.00 25.99 ? 234  ASP A CB  1 
ATOM   1560 C  CG  . ASP A 1 234 ? 60.282  49.191 69.400  1.00 31.79 ? 234  ASP A CG  1 
ATOM   1561 O  OD1 . ASP A 1 234 ? 59.747  48.155 69.863  1.00 39.77 ? 234  ASP A OD1 1 
ATOM   1562 O  OD2 . ASP A 1 234 ? 59.651  50.105 68.849  1.00 39.06 ? 234  ASP A OD2 1 
ATOM   1563 N  N   . GLY A 1 235 ? 64.617  49.229 70.117  1.00 20.63 ? 235  GLY A N   1 
ATOM   1564 C  CA  . GLY A 1 235 ? 66.057  49.156 70.265  1.00 18.98 ? 235  GLY A CA  1 
ATOM   1565 C  C   . GLY A 1 235 ? 66.618  50.030 71.364  1.00 17.56 ? 235  GLY A C   1 
ATOM   1566 O  O   . GLY A 1 235 ? 67.805  49.905 71.681  1.00 22.60 ? 235  GLY A O   1 
ATOM   1567 N  N   . TYR A 1 236 ? 65.792  50.890 71.959  1.00 17.85 ? 236  TYR A N   1 
ATOM   1568 C  CA  . TYR A 1 236 ? 66.187  51.735 73.075  1.00 17.15 ? 236  TYR A CA  1 
ATOM   1569 C  C   . TYR A 1 236 ? 65.742  51.158 74.414  1.00 18.37 ? 236  TYR A C   1 
ATOM   1570 O  O   . TYR A 1 236 ? 65.804  51.852 75.433  1.00 17.54 ? 236  TYR A O   1 
ATOM   1571 C  CB  . TYR A 1 236 ? 65.663  53.154 72.853  1.00 18.71 ? 236  TYR A CB  1 
ATOM   1572 C  CG  . TYR A 1 236 ? 66.102  53.653 71.496  1.00 17.85 ? 236  TYR A CG  1 
ATOM   1573 C  CD1 . TYR A 1 236 ? 67.399  54.105 71.300  1.00 19.11 ? 236  TYR A CD1 1 
ATOM   1574 C  CD2 . TYR A 1 236 ? 65.242  53.600 70.399  1.00 18.88 ? 236  TYR A CD2 1 
ATOM   1575 C  CE1 . TYR A 1 236 ? 67.829  54.533 70.062  1.00 19.32 ? 236  TYR A CE1 1 
ATOM   1576 C  CE2 . TYR A 1 236 ? 65.657  54.028 69.153  1.00 21.18 ? 236  TYR A CE2 1 
ATOM   1577 C  CZ  . TYR A 1 236 ? 66.954  54.483 69.001  1.00 19.41 ? 236  TYR A CZ  1 
ATOM   1578 O  OH  . TYR A 1 236 ? 67.382  54.904 67.761  1.00 22.07 ? 236  TYR A OH  1 
ATOM   1579 N  N   . ASP A 1 237 ? 65.315  49.897 74.427  1.00 15.72 ? 237  ASP A N   1 
ATOM   1580 C  CA  . ASP A 1 237 ? 64.914  49.163 75.632  1.00 14.93 ? 237  ASP A CA  1 
ATOM   1581 C  C   . ASP A 1 237 ? 65.784  47.909 75.662  1.00 15.17 ? 237  ASP A C   1 
ATOM   1582 O  O   . ASP A 1 237 ? 65.561  46.963 74.900  1.00 17.87 ? 237  ASP A O   1 
ATOM   1583 C  CB  . ASP A 1 237 ? 63.408  48.877 75.545  1.00 15.32 ? 237  ASP A CB  1 
ATOM   1584 C  CG  . ASP A 1 237 ? 62.889  47.981 76.631  1.00 17.63 ? 237  ASP A CG  1 
ATOM   1585 O  OD1 . ASP A 1 237 ? 63.643  47.661 77.573  1.00 17.63 ? 237  ASP A OD1 1 
ATOM   1586 O  OD2 . ASP A 1 237 ? 61.667  47.664 76.549  1.00 19.40 ? 237  ASP A OD2 1 
ATOM   1587 N  N   . ILE A 1 238 ? 66.786  47.913 76.535  1.00 13.24 ? 238  ILE A N   1 
ATOM   1588 C  CA  . ILE A 1 238 ? 67.902  46.973 76.447  1.00 13.87 ? 238  ILE A CA  1 
ATOM   1589 C  C   . ILE A 1 238 ? 68.055  46.246 77.778  1.00 12.75 ? 238  ILE A C   1 
ATOM   1590 O  O   . ILE A 1 238 ? 68.245  46.902 78.815  1.00 14.85 ? 238  ILE A O   1 
ATOM   1591 C  CB  . ILE A 1 238 ? 69.199  47.724 76.098  1.00 15.37 ? 238  ILE A CB  1 
ATOM   1592 C  CG1 . ILE A 1 238 ? 69.131  48.275 74.669  1.00 15.51 ? 238  ILE A CG1 1 
ATOM   1593 C  CG2 . ILE A 1 238 ? 70.438  46.803 76.285  1.00 14.56 ? 238  ILE A CG2 1 
ATOM   1594 C  CD1 . ILE A 1 238 ? 70.337  49.140 74.277  1.00 16.53 ? 238  ILE A CD1 1 
ATOM   1595 N  N   . PRO A 1 239 ? 68.056  44.913 77.802  1.00 13.55 ? 239  PRO A N   1 
ATOM   1596 C  CA  . PRO A 1 239 ? 68.279  44.185 79.057  1.00 13.23 ? 239  PRO A CA  1 
ATOM   1597 C  C   . PRO A 1 239 ? 69.772  44.051 79.301  1.00 13.90 ? 239  PRO A C   1 
ATOM   1598 O  O   . PRO A 1 239 ? 70.577  43.926 78.373  1.00 13.89 ? 239  PRO A O   1 
ATOM   1599 C  CB  . PRO A 1 239 ? 67.686  42.792 78.791  1.00 15.87 ? 239  PRO A CB  1 
ATOM   1600 C  CG  . PRO A 1 239 ? 67.121  42.795 77.415  1.00 23.36 ? 239  PRO A CG  1 
ATOM   1601 C  CD  . PRO A 1 239 ? 67.451  44.095 76.742  1.00 18.27 ? 239  PRO A CD  1 
ATOM   1602 N  N   . LEU A 1 240 ? 70.144  44.109 80.582  1.00 11.83 ? 240  LEU A N   1 
ATOM   1603 C  CA  . LEU A 1 240 ? 71.533  43.952 81.028  1.00 12.37 ? 240  LEU A CA  1 
ATOM   1604 C  C   . LEU A 1 240 ? 71.593  42.864 82.096  1.00 12.26 ? 240  LEU A C   1 
ATOM   1605 O  O   . LEU A 1 240 ? 71.245  43.124 83.253  1.00 13.39 ? 240  LEU A O   1 
ATOM   1606 C  CB  . LEU A 1 240 ? 72.113  45.258 81.593  1.00 12.64 ? 240  LEU A CB  1 
ATOM   1607 C  CG  . LEU A 1 240 ? 72.032  46.513 80.728  1.00 13.06 ? 240  LEU A CG  1 
ATOM   1608 C  CD1 . LEU A 1 240 ? 72.594  47.692 81.500  1.00 15.61 ? 240  LEU A CD1 1 
ATOM   1609 C  CD2 . LEU A 1 240 ? 72.823  46.347 79.410  1.00 14.67 ? 240  LEU A CD2 1 
ATOM   1610 N  N   . MET A 1 241 ? 72.056  41.671 81.731  1.00 11.96 ? 241  MET A N   1 
ATOM   1611 C  CA  . MET A 1 241 ? 72.274  40.582 82.689  1.00 12.65 ? 241  MET A CA  1 
ATOM   1612 C  C   . MET A 1 241 ? 73.726  40.629 83.159  1.00 11.36 ? 241  MET A C   1 
ATOM   1613 O  O   . MET A 1 241 ? 74.638  40.247 82.401  1.00 11.88 ? 241  MET A O   1 
ATOM   1614 C  CB  . MET A 1 241 ? 72.147  39.235 81.985  1.00 12.13 ? 241  MET A CB  1 
ATOM   1615 C  CG  . MET A 1 241 ? 72.205  38.067 82.993  1.00 13.35 ? 241  MET A CG  1 
ATOM   1616 S  SD  . MET A 1 241 ? 71.938  36.462 82.224  1.00 14.23 ? 241  MET A SD  1 
ATOM   1617 C  CE  . MET A 1 241 ? 70.169  36.268 82.350  1.00 17.83 ? 241  MET A CE  1 
ATOM   1618 N  N   . ILE A 1 242 ? 73.962  41.027 84.416  1.00 10.03 ? 242  ILE A N   1 
ATOM   1619 C  CA  . ILE A 1 242 ? 75.309  41.171 84.965  1.00 10.94 ? 242  ILE A CA  1 
ATOM   1620 C  C   . ILE A 1 242 ? 75.674  39.907 85.738  1.00 12.32 ? 242  ILE A C   1 
ATOM   1621 O  O   . ILE A 1 242 ? 74.916  39.478 86.619  1.00 12.26 ? 242  ILE A O   1 
ATOM   1622 C  CB  . ILE A 1 242 ? 75.415  42.407 85.870  1.00 11.16 ? 242  ILE A CB  1 
ATOM   1623 C  CG1 . ILE A 1 242 ? 74.961  43.680 85.139  1.00 12.41 ? 242  ILE A CG1 1 
ATOM   1624 C  CG2 . ILE A 1 242 ? 76.836  42.485 86.442  1.00 12.73 ? 242  ILE A CG2 1 
ATOM   1625 C  CD1 . ILE A 1 242 ? 74.737  44.826 86.084  1.00 14.99 ? 242  ILE A CD1 1 
ATOM   1626 N  N   . GLN A 1 243 ? 76.837  39.315 85.429  1.00 11.82 ? 243  GLN A N   1 
ATOM   1627 C  CA  . GLN A 1 243 ? 77.278  38.087 86.091  1.00 12.20 ? 243  GLN A CA  1 
ATOM   1628 C  C   . GLN A 1 243 ? 78.784  38.080 86.217  1.00 13.91 ? 243  GLN A C   1 
ATOM   1629 O  O   . GLN A 1 243 ? 79.486  38.442 85.269  1.00 15.89 ? 243  GLN A O   1 
ATOM   1630 C  CB  . GLN A 1 243 ? 76.935  36.853 85.247  1.00 11.40 ? 243  GLN A CB  1 
ATOM   1631 C  CG  . GLN A 1 243 ? 75.438  36.721 85.057  1.00 13.51 ? 243  GLN A CG  1 
ATOM   1632 C  CD  . GLN A 1 243 ? 75.079  35.505 84.244  1.00 13.07 ? 243  GLN A CD  1 
ATOM   1633 O  OE1 . GLN A 1 243 ? 75.511  35.363 83.084  1.00 15.51 ? 243  GLN A OE1 1 
ATOM   1634 N  NE2 . GLN A 1 243 ? 74.288  34.612 84.836  1.00 13.16 ? 243  GLN A NE2 1 
ATOM   1635 N  N   . ASP A 1 244 ? 79.293  37.591 87.343  1.00 11.75 ? 244  ASP A N   1 
ATOM   1636 C  CA  . ASP A 1 244 ? 80.740  37.427 87.467  1.00 11.91 ? 244  ASP A CA  1 
ATOM   1637 C  C   . ASP A 1 244 ? 81.143  35.994 87.133  1.00 13.47 ? 244  ASP A C   1 
ATOM   1638 O  O   . ASP A 1 244 ? 80.403  35.042 87.390  1.00 12.96 ? 244  ASP A O   1 
ATOM   1639 C  CB  . ASP A 1 244 ? 81.285  37.903 88.818  1.00 13.48 ? 244  ASP A CB  1 
ATOM   1640 C  CG  . ASP A 1 244 ? 80.697  37.185 90.007  1.00 15.00 ? 244  ASP A CG  1 
ATOM   1641 O  OD1 . ASP A 1 244 ? 79.549  36.716 89.952  1.00 14.50 ? 244  ASP A OD1 1 
ATOM   1642 O  OD2 . ASP A 1 244 ? 81.392  37.174 91.045  1.00 15.79 ? 244  ASP A OD2 1 
ATOM   1643 N  N   . ARG A 1 245 ? 82.318  35.855 86.518  1.00 12.70 ? 245  ARG A N   1 
ATOM   1644 C  CA  . ARG A 1 245 ? 82.754  34.558 86.016  1.00 11.41 ? 245  ARG A CA  1 
ATOM   1645 C  C   . ARG A 1 245 ? 84.254  34.447 86.180  1.00 12.85 ? 245  ARG A C   1 
ATOM   1646 O  O   . ARG A 1 245 ? 84.968  35.446 86.255  1.00 13.89 ? 245  ARG A O   1 
ATOM   1647 C  CB  . ARG A 1 245 ? 82.434  34.403 84.525  1.00 13.15 ? 245  ARG A CB  1 
ATOM   1648 C  CG  . ARG A 1 245 ? 80.928  34.317 84.228  1.00 12.88 ? 245  ARG A CG  1 
ATOM   1649 C  CD  . ARG A 1 245 ? 80.403  32.943 84.634  1.00 13.32 ? 245  ARG A CD  1 
ATOM   1650 N  NE  . ARG A 1 245 ? 78.981  32.710 84.389  1.00 15.12 ? 245  ARG A NE  1 
ATOM   1651 C  CZ  . ARG A 1 245 ? 78.004  32.902 85.269  1.00 11.46 ? 245  ARG A CZ  1 
ATOM   1652 N  NH1 . ARG A 1 245 ? 78.211  33.554 86.406  1.00 13.24 ? 245  ARG A NH1 1 
ATOM   1653 N  NH2 . ARG A 1 245 ? 76.787  32.415 85.007  1.00 13.31 ? 245  ARG A NH2 1 
ATOM   1654 N  N   . SER A 1 246 ? 84.715  33.207 86.240  1.00 13.71 ? 246  SER A N   1 
ATOM   1655 C  CA  . SER A 1 246 ? 86.140  32.932 86.168  1.00 12.54 ? 246  SER A CA  1 
ATOM   1656 C  C   . SER A 1 246 ? 86.389  31.794 85.189  1.00 13.57 ? 246  SER A C   1 
ATOM   1657 O  O   . SER A 1 246 ? 85.507  30.964 84.948  1.00 13.37 ? 246  SER A O   1 
ATOM   1658 C  CB  . SER A 1 246 ? 86.677  32.491 87.528  1.00 13.73 ? 246  SER A CB  1 
ATOM   1659 O  OG  . SER A 1 246 ? 86.567  33.558 88.461  1.00 16.16 ? 246  SER A OG  1 
ATOM   1660 N  N   . PHE A 1 247 ? 87.615  31.763 84.637  1.00 12.93 ? 247  PHE A N   1 
ATOM   1661 C  CA  . PHE A 1 247 ? 87.932  30.848 83.548  1.00 12.12 ? 247  PHE A CA  1 
ATOM   1662 C  C   . PHE A 1 247 ? 89.272  30.180 83.803  1.00 13.73 ? 247  PHE A C   1 
ATOM   1663 O  O   . PHE A 1 247 ? 90.151  30.750 84.452  1.00 14.97 ? 247  PHE A O   1 
ATOM   1664 C  CB  . PHE A 1 247 ? 88.012  31.614 82.215  1.00 14.62 ? 247  PHE A CB  1 
ATOM   1665 C  CG  . PHE A 1 247 ? 86.720  32.301 81.872  1.00 12.87 ? 247  PHE A CG  1 
ATOM   1666 C  CD1 . PHE A 1 247 ? 86.451  33.583 82.348  1.00 14.19 ? 247  PHE A CD1 1 
ATOM   1667 C  CD2 . PHE A 1 247 ? 85.769  31.659 81.120  1.00 14.64 ? 247  PHE A CD2 1 
ATOM   1668 C  CE1 . PHE A 1 247 ? 85.248  34.217 82.076  1.00 13.65 ? 247  PHE A CE1 1 
ATOM   1669 C  CE2 . PHE A 1 247 ? 84.550  32.269 80.852  1.00 15.10 ? 247  PHE A CE2 1 
ATOM   1670 C  CZ  . PHE A 1 247 ? 84.291  33.551 81.318  1.00 13.76 ? 247  PHE A CZ  1 
ATOM   1671 N  N   . ARG A 1 248 ? 89.427  28.979 83.251  1.00 14.94 ? 248  ARG A N   1 
ATOM   1672 C  CA  . ARG A 1 248 ? 90.737  28.362 83.195  1.00 15.24 ? 248  ARG A CA  1 
ATOM   1673 C  C   . ARG A 1 248 ? 91.520  28.931 82.009  1.00 14.25 ? 248  ARG A C   1 
ATOM   1674 O  O   . ARG A 1 248 ? 90.963  29.589 81.123  1.00 16.75 ? 248  ARG A O   1 
ATOM   1675 C  CB  . ARG A 1 248 ? 90.602  26.838 83.091  1.00 15.76 ? 248  ARG A CB  1 
ATOM   1676 C  CG  . ARG A 1 248 ? 89.757  26.211 84.213  1.00 17.05 ? 248  ARG A CG  1 
ATOM   1677 C  CD  . ARG A 1 248 ? 89.874  24.680 84.217  1.00 16.99 ? 248  ARG A CD  1 
ATOM   1678 N  NE  . ARG A 1 248 ? 88.974  24.087 85.207  1.00 17.49 ? 248  ARG A NE  1 
ATOM   1679 C  CZ  . ARG A 1 248 ? 87.773  23.589 84.941  1.00 19.95 ? 248  ARG A CZ  1 
ATOM   1680 N  NH1 . ARG A 1 248 ? 87.295  23.550 83.702  1.00 19.84 ? 248  ARG A NH1 1 
ATOM   1681 N  NH2 . ARG A 1 248 ? 87.045  23.080 85.939  1.00 22.97 ? 248  ARG A NH2 1 
ATOM   1682 N  N   . SER A 1 249 ? 92.830  28.666 81.974  1.00 15.57 ? 249  SER A N   1 
ATOM   1683 C  CA  . SER A 1 249 ? 93.669  29.176 80.897  1.00 16.74 ? 249  SER A CA  1 
ATOM   1684 C  C   . SER A 1 249 ? 93.236  28.713 79.508  1.00 18.76 ? 249  SER A C   1 
ATOM   1685 O  O   . SER A 1 249 ? 93.552  29.388 78.521  1.00 19.90 ? 249  SER A O   1 
ATOM   1686 C  CB  . SER A 1 249 ? 95.141  28.835 81.153  1.00 19.12 ? 249  SER A CB  1 
ATOM   1687 O  OG  . SER A 1 249 ? 95.332  27.433 81.029  1.00 20.46 ? 249  SER A OG  1 
ATOM   1688 N  N   . ASP A 1 250 ? 92.506  27.602 79.400  1.00 17.10 ? 250  ASP A N   1 
ATOM   1689 C  CA  . ASP A 1 250 ? 92.031  27.105 78.115  1.00 16.42 ? 250  ASP A CA  1 
ATOM   1690 C  C   . ASP A 1 250 ? 90.655  27.662 77.763  1.00 16.74 ? 250  ASP A C   1 
ATOM   1691 O  O   . ASP A 1 250 ? 90.062  27.241 76.766  1.00 19.83 ? 250  ASP A O   1 
ATOM   1692 C  CB  . ASP A 1 250 ? 92.038  25.567 78.094  1.00 17.26 ? 250  ASP A CB  1 
ATOM   1693 C  CG  . ASP A 1 250 ? 91.043  24.943 79.068  1.00 19.54 ? 250  ASP A CG  1 
ATOM   1694 O  OD1 . ASP A 1 250 ? 90.319  25.661 79.786  1.00 17.48 ? 250  ASP A OD1 1 
ATOM   1695 O  OD2 . ASP A 1 250 ? 91.034  23.685 79.151  1.00 21.49 ? 250  ASP A OD2 1 
ATOM   1696 N  N   . GLY A 1 251 ? 90.156  28.611 78.544  1.00 15.97 ? 251  GLY A N   1 
ATOM   1697 C  CA  . GLY A 1 251 ? 88.876  29.233 78.299  1.00 15.60 ? 251  GLY A CA  1 
ATOM   1698 C  C   . GLY A 1 251 ? 87.699  28.512 78.909  1.00 16.34 ? 251  GLY A C   1 
ATOM   1699 O  O   . GLY A 1 251 ? 86.589  29.046 78.866  1.00 15.67 ? 251  GLY A O   1 
ATOM   1700 N  N   . SER A 1 252 ? 87.901  27.344 79.506  1.00 15.59 ? 252  SER A N   1 
ATOM   1701 C  CA  . SER A 1 252 ? 86.767  26.639 80.098  1.00 13.84 ? 252  SER A CA  1 
ATOM   1702 C  C   . SER A 1 252 ? 86.264  27.380 81.342  1.00 16.10 ? 252  SER A C   1 
ATOM   1703 O  O   . SER A 1 252 ? 87.005  28.118 82.006  1.00 15.01 ? 252  SER A O   1 
ATOM   1704 C  CB  . SER A 1 252 ? 87.130  25.179 80.413  1.00 16.28 ? 252  SER A CB  1 
ATOM   1705 O  OG  . SER A 1 252 ? 88.164  25.080 81.368  1.00 16.60 ? 252  SER A OG  1 
ATOM   1706 N  N   . LEU A 1 253 ? 84.973  27.231 81.625  1.00 14.79 ? 253  LEU A N   1 
ATOM   1707 C  CA  . LEU A 1 253 ? 84.424  27.808 82.844  1.00 13.69 ? 253  LEU A CA  1 
ATOM   1708 C  C   . LEU A 1 253 ? 85.113  27.203 84.056  1.00 12.91 ? 253  LEU A C   1 
ATOM   1709 O  O   . LEU A 1 253 ? 85.211  25.976 84.183  1.00 15.57 ? 253  LEU A O   1 
ATOM   1710 C  CB  . LEU A 1 253 ? 82.922  27.520 82.931  1.00 15.64 ? 253  LEU A CB  1 
ATOM   1711 C  CG  . LEU A 1 253 ? 81.991  28.312 82.022  1.00 18.84 ? 253  LEU A CG  1 
ATOM   1712 C  CD1 . LEU A 1 253 ? 80.574  27.772 82.210  1.00 20.76 ? 253  LEU A CD1 1 
ATOM   1713 C  CD2 . LEU A 1 253 ? 82.036  29.772 82.346  1.00 17.87 ? 253  LEU A CD2 1 
ATOM   1714 N  N   . SER A 1 254 ? 85.539  28.059 84.975  1.00 13.22 ? 254  SER A N   1 
ATOM   1715 C  CA  . SER A 1 254 ? 86.183  27.607 86.197  1.00 14.72 ? 254  SER A CA  1 
ATOM   1716 C  C   . SER A 1 254 ? 85.213  27.769 87.356  1.00 13.79 ? 254  SER A C   1 
ATOM   1717 O  O   . SER A 1 254 ? 84.685  28.863 87.569  1.00 15.02 ? 254  SER A O   1 
ATOM   1718 C  CB  . SER A 1 254 ? 87.450  28.416 86.468  1.00 15.54 ? 254  SER A CB  1 
ATOM   1719 O  OG  . SER A 1 254 ? 88.097  27.890 87.627  1.00 16.08 ? 254  SER A OG  1 
ATOM   1720 N  N   . TYR A 1 255 ? 84.981  26.678 88.101  1.00 14.04 ? 255  TYR A N   1 
ATOM   1721 C  CA  . TYR A 1 255 ? 84.124  26.731 89.270  1.00 13.19 ? 255  TYR A CA  1 
ATOM   1722 C  C   . TYR A 1 255 ? 84.840  25.865 90.305  1.00 15.14 ? 255  TYR A C   1 
ATOM   1723 O  O   . TYR A 1 255 ? 85.432  24.842 89.935  1.00 15.93 ? 255  TYR A O   1 
ATOM   1724 C  CB  . TYR A 1 255 ? 82.715  26.173 88.941  1.00 12.27 ? 255  TYR A CB  1 
ATOM   1725 C  CG  . TYR A 1 255 ? 81.760  26.404 90.078  1.00 12.25 ? 255  TYR A CG  1 
ATOM   1726 C  CD1 . TYR A 1 255 ? 81.136  27.634 90.244  1.00 12.59 ? 255  TYR A CD1 1 
ATOM   1727 C  CD2 . TYR A 1 255 ? 81.562  25.411 91.051  1.00 12.66 ? 255  TYR A CD2 1 
ATOM   1728 C  CE1 . TYR A 1 255 ? 80.302  27.875 91.353  1.00 15.33 ? 255  TYR A CE1 1 
ATOM   1729 C  CE2 . TYR A 1 255 ? 80.737  25.626 92.140  1.00 12.00 ? 255  TYR A CE2 1 
ATOM   1730 C  CZ  . TYR A 1 255 ? 80.107  26.858 92.281  1.00 13.02 ? 255  TYR A CZ  1 
ATOM   1731 O  OH  . TYR A 1 255 ? 79.310  27.082 93.386  1.00 13.41 ? 255  TYR A OH  1 
ATOM   1732 N  N   . PRO A 1 256 ? 84.832  26.240 91.588  1.00 13.73 ? 256  PRO A N   1 
ATOM   1733 C  CA  . PRO A 1 256 ? 85.682  25.540 92.575  1.00 15.36 ? 256  PRO A CA  1 
ATOM   1734 C  C   . PRO A 1 256 ? 85.362  24.059 92.728  1.00 15.67 ? 256  PRO A C   1 
ATOM   1735 O  O   . PRO A 1 256 ? 84.199  23.657 92.773  1.00 15.40 ? 256  PRO A O   1 
ATOM   1736 C  CB  . PRO A 1 256 ? 85.402  26.274 93.897  1.00 16.60 ? 256  PRO A CB  1 
ATOM   1737 C  CG  . PRO A 1 256 ? 84.534  27.427 93.576  1.00 24.57 ? 256  PRO A CG  1 
ATOM   1738 C  CD  . PRO A 1 256 ? 84.161  27.434 92.136  1.00 14.85 ? 256  PRO A CD  1 
ATOM   1739 N  N   . GLU A 1 257 ? 86.418  23.255 92.877  1.00 16.07 ? 257  GLU A N   1 
ATOM   1740 C  CA  . GLU A 1 257 ? 86.242  21.862 93.236  1.00 14.85 ? 257  GLU A CA  1 
ATOM   1741 C  C   . GLU A 1 257 ? 86.031  21.692 94.736  1.00 15.05 ? 257  GLU A C   1 
ATOM   1742 O  O   . GLU A 1 257 ? 85.516  20.657 95.166  1.00 15.40 ? 257  GLU A O   1 
ATOM   1743 C  CB  . GLU A 1 257 ? 87.449  21.057 92.728  1.00 17.38 ? 257  GLU A CB  1 
ATOM   1744 C  CG  . GLU A 1 257 ? 88.685  21.153 93.609  1.00 19.27 ? 257  GLU A CG  1 
ATOM   1745 C  CD  . GLU A 1 257 ? 89.884  20.329 93.101  1.00 19.45 ? 257  GLU A CD  1 
ATOM   1746 O  OE1 . GLU A 1 257 ? 90.356  20.579 91.976  1.00 20.59 ? 257  GLU A OE1 1 
ATOM   1747 O  OE2 . GLU A 1 257 ? 90.305  19.390 93.823  1.00 22.59 ? 257  GLU A OE2 1 
ATOM   1748 N  N   . ASN A 1 258 ? 86.431  22.675 95.541  1.00 15.10 ? 258  ASN A N   1 
ATOM   1749 C  CA  . ASN A 1 258 ? 86.474  22.540 96.996  1.00 15.36 ? 258  ASN A CA  1 
ATOM   1750 C  C   . ASN A 1 258 ? 86.833  23.929 97.508  1.00 15.29 ? 258  ASN A C   1 
ATOM   1751 O  O   . ASN A 1 258 ? 87.161  24.830 96.728  1.00 17.37 ? 258  ASN A O   1 
ATOM   1752 C  CB  . ASN A 1 258 ? 87.522  21.487 97.389  1.00 16.53 ? 258  ASN A CB  1 
ATOM   1753 C  CG  . ASN A 1 258 ? 87.325  20.906 98.795  1.00 17.86 ? 258  ASN A CG  1 
ATOM   1754 O  OD1 . ASN A 1 258 ? 86.803  21.558 99.699  1.00 16.93 ? 258  ASN A OD1 1 
ATOM   1755 N  ND2 . ASN A 1 258 ? 87.737  19.650 98.968  1.00 19.19 ? 258  ASN A ND2 1 
ATOM   1756 N  N   . THR A 1 259 ? 86.761  24.096 98.824  1.00 17.33 ? 259  THR A N   1 
ATOM   1757 C  CA  . THR A 1 259 ? 87.203  25.321 99.470  1.00 18.51 ? 259  THR A CA  1 
ATOM   1758 C  C   . THR A 1 259 ? 88.729  25.356 99.565  1.00 17.11 ? 259  THR A C   1 
ATOM   1759 O  O   . THR A 1 259 ? 89.426  24.369 99.285  1.00 18.78 ? 259  THR A O   1 
ATOM   1760 C  CB  . THR A 1 259 ? 86.572  25.426 100.862 1.00 17.39 ? 259  THR A CB  1 
ATOM   1761 O  OG1 . THR A 1 259 ? 86.866  24.237 101.601 1.00 18.74 ? 259  THR A OG1 1 
ATOM   1762 C  CG2 . THR A 1 259 ? 85.066  25.524 100.732 1.00 17.25 ? 259  THR A CG2 1 
ATOM   1763 N  N   . ASN A 1 260 ? 89.250  26.516 99.944  1.00 20.35 ? 260  ASN A N   1 
ATOM   1764 C  CA  . ASN A 1 260 ? 90.674  26.677 100.249 1.00 20.68 ? 260  ASN A CA  1 
ATOM   1765 C  C   . ASN A 1 260 ? 90.771  27.371 101.595 1.00 23.16 ? 260  ASN A C   1 
ATOM   1766 O  O   . ASN A 1 260 ? 90.432  28.571 101.686 1.00 27.83 ? 260  ASN A O   1 
ATOM   1767 C  CB  . ASN A 1 260 ? 91.382  27.509 99.183  1.00 26.21 ? 260  ASN A CB  1 
ATOM   1768 C  CG  . ASN A 1 260 ? 91.664  26.727 97.903  1.00 36.27 ? 260  ASN A CG  1 
ATOM   1769 O  OD1 . ASN A 1 260 ? 92.613  25.939 97.841  1.00 38.56 ? 260  ASN A OD1 1 
ATOM   1770 N  ND2 . ASN A 1 260 ? 90.839  26.941 96.876  1.00 36.37 ? 260  ASN A ND2 1 
ATOM   1771 N  N   . PRO A 1 261 ? 91.227  26.685 102.651 1.00 24.44 ? 261  PRO A N   1 
ATOM   1772 C  CA  . PRO A 1 261 ? 91.664  25.278 102.693 1.00 21.32 ? 261  PRO A CA  1 
ATOM   1773 C  C   . PRO A 1 261 ? 90.519  24.299 102.446 1.00 22.83 ? 261  PRO A C   1 
ATOM   1774 O  O   . PRO A 1 261 ? 89.360  24.607 102.715 1.00 21.87 ? 261  PRO A O   1 
ATOM   1775 C  CB  . PRO A 1 261 ? 92.220  25.108 104.118 1.00 27.07 ? 261  PRO A CB  1 
ATOM   1776 C  CG  . PRO A 1 261 ? 92.045  26.413 104.825 1.00 33.43 ? 261  PRO A CG  1 
ATOM   1777 C  CD  . PRO A 1 261 ? 91.173  27.291 103.993 1.00 29.17 ? 261  PRO A CD  1 
ATOM   1778 N  N   . PRO A 1 262 ? 90.845  23.110 101.944 1.00 19.67 ? 262  PRO A N   1 
ATOM   1779 C  CA  . PRO A 1 262 ? 89.810  22.189 101.461 1.00 20.27 ? 262  PRO A CA  1 
ATOM   1780 C  C   . PRO A 1 262 ? 89.114  21.441 102.584 1.00 18.81 ? 262  PRO A C   1 
ATOM   1781 O  O   . PRO A 1 262 ? 89.712  21.101 103.610 1.00 22.35 ? 262  PRO A O   1 
ATOM   1782 C  CB  . PRO A 1 262 ? 90.606  21.193 100.600 1.00 20.74 ? 262  PRO A CB  1 
ATOM   1783 C  CG  . PRO A 1 262 ? 92.021  21.230 101.191 1.00 21.25 ? 262  PRO A CG  1 
ATOM   1784 C  CD  . PRO A 1 262 ? 92.215  22.648 101.640 1.00 22.91 ? 262  PRO A CD  1 
ATOM   1785 N  N   . ALA A 1 263 ? 87.833  21.159 102.346 1.00 19.59 ? 263  ALA A N   1 
ATOM   1786 C  CA  . ALA A 1 263 ? 87.089  20.231 103.165 1.00 19.38 ? 263  ALA A CA  1 
ATOM   1787 C  C   . ALA A 1 263 ? 87.549  18.817 102.833 1.00 19.34 ? 263  ALA A C   1 
ATOM   1788 O  O   . ALA A 1 263 ? 88.154  18.588 101.780 1.00 20.45 ? 263  ALA A O   1 
ATOM   1789 C  CB  . ALA A 1 263 ? 85.599  20.363 102.848 1.00 21.41 ? 263  ALA A CB  1 
ATOM   1790 N  N   . PRO A 1 264 ? 87.297  17.852 103.722 1.00 22.47 ? 264  PRO A N   1 
ATOM   1791 C  CA  . PRO A 1 264 ? 87.654  16.458 103.405 1.00 22.77 ? 264  PRO A CA  1 
ATOM   1792 C  C   . PRO A 1 264 ? 86.752  15.825 102.351 1.00 20.60 ? 264  PRO A C   1 
ATOM   1793 O  O   . PRO A 1 264 ? 87.083  14.740 101.846 1.00 23.00 ? 264  PRO A O   1 
ATOM   1794 C  CB  . PRO A 1 264 ? 87.525  15.739 104.761 1.00 26.83 ? 264  PRO A CB  1 
ATOM   1795 C  CG  . PRO A 1 264 ? 86.590  16.573 105.532 1.00 29.42 ? 264  PRO A CG  1 
ATOM   1796 C  CD  . PRO A 1 264 ? 86.825  18.004 105.107 1.00 24.82 ? 264  PRO A CD  1 
ATOM   1797 N  N   . VAL A 1 265 ? 85.626  16.452 102.040 1.00 20.80 ? 265  VAL A N   1 
ATOM   1798 C  CA  . VAL A 1 265 ? 84.717  16.005 100.985 1.00 19.71 ? 265  VAL A CA  1 
ATOM   1799 C  C   . VAL A 1 265 ? 85.278  16.483 99.653  1.00 16.72 ? 265  VAL A C   1 
ATOM   1800 O  O   . VAL A 1 265 ? 85.645  17.652 99.522  1.00 17.68 ? 265  VAL A O   1 
ATOM   1801 C  CB  . VAL A 1 265 ? 83.320  16.607 101.231 1.00 21.23 ? 265  VAL A CB  1 
ATOM   1802 C  CG1 . VAL A 1 265 ? 82.342  16.272 100.101 1.00 20.40 ? 265  VAL A CG1 1 
ATOM   1803 C  CG2 . VAL A 1 265 ? 82.771  16.165 102.586 1.00 22.04 ? 265  VAL A CG2 1 
ATOM   1804 N  N   . ASN A 1 266 ? 85.303  15.597 98.646  1.00 17.19 ? 266  ASN A N   1 
ATOM   1805 C  CA  . ASN A 1 266 ? 85.786  15.994 97.317  1.00 17.04 ? 266  ASN A CA  1 
ATOM   1806 C  C   . ASN A 1 266 ? 84.904  15.436 96.210  1.00 15.86 ? 266  ASN A C   1 
ATOM   1807 O  O   . ASN A 1 266 ? 84.680  14.219 96.174  1.00 16.94 ? 266  ASN A O   1 
ATOM   1808 C  CB  . ASN A 1 266 ? 87.203  15.467 97.094  1.00 17.96 ? 266  ASN A CB  1 
ATOM   1809 C  CG  . ASN A 1 266 ? 88.229  16.186 97.929  1.00 19.72 ? 266  ASN A CG  1 
ATOM   1810 O  OD1 . ASN A 1 266 ? 88.594  17.330 97.633  1.00 19.59 ? 266  ASN A OD1 1 
ATOM   1811 N  ND2 . ASN A 1 266 ? 88.679  15.532 98.998  1.00 19.33 ? 266  ASN A ND2 1 
ATOM   1812 N  N   . PRO A 1 267 ? 84.415  16.285 95.283  1.00 16.18 ? 267  PRO A N   1 
ATOM   1813 C  CA  . PRO A 1 267 ? 84.377  17.753 95.351  1.00 15.95 ? 267  PRO A CA  1 
ATOM   1814 C  C   . PRO A 1 267 ? 83.489  18.201 96.496  1.00 14.22 ? 267  PRO A C   1 
ATOM   1815 O  O   . PRO A 1 267 ? 82.666  17.409 96.979  1.00 16.58 ? 267  PRO A O   1 
ATOM   1816 C  CB  . PRO A 1 267 ? 83.755  18.179 94.003  1.00 16.96 ? 267  PRO A CB  1 
ATOM   1817 C  CG  . PRO A 1 267 ? 83.858  16.953 93.105  1.00 16.24 ? 267  PRO A CG  1 
ATOM   1818 C  CD  . PRO A 1 267 ? 83.837  15.766 94.026  1.00 17.45 ? 267  PRO A CD  1 
ATOM   1819 N  N   . SER A 1 268 ? 83.643  19.442 96.950  1.00 14.56 ? 268  SER A N   1 
ATOM   1820 C  CA  . SER A 1 268 ? 82.809  20.008 98.001  1.00 15.16 ? 268  SER A CA  1 
ATOM   1821 C  C   . SER A 1 268 ? 82.241  21.353 97.573  1.00 14.96 ? 268  SER A C   1 
ATOM   1822 O  O   . SER A 1 268 ? 82.934  22.177 96.948  1.00 15.91 ? 268  SER A O   1 
ATOM   1823 C  CB  . SER A 1 268 ? 83.629  20.207 99.287  1.00 17.64 ? 268  SER A CB  1 
ATOM   1824 O  OG  . SER A 1 268 ? 82.853  20.857 100.300 1.00 16.95 ? 268  SER A OG  1 
ATOM   1825 N  N   . VAL A 1 269 ? 80.979  21.582 97.947  1.00 14.43 ? 269  VAL A N   1 
ATOM   1826 C  CA  . VAL A 1 269 ? 80.397  22.915 97.912  1.00 14.23 ? 269  VAL A CA  1 
ATOM   1827 C  C   . VAL A 1 269 ? 81.288  23.902 98.673  1.00 14.20 ? 269  VAL A C   1 
ATOM   1828 O  O   . VAL A 1 269 ? 81.957  23.547 99.660  1.00 15.10 ? 269  VAL A O   1 
ATOM   1829 C  CB  . VAL A 1 269 ? 78.956  22.870 98.472  1.00 14.38 ? 269  VAL A CB  1 
ATOM   1830 C  CG1 . VAL A 1 269 ? 78.961  22.524 99.970  1.00 16.50 ? 269  VAL A CG1 1 
ATOM   1831 C  CG2 . VAL A 1 269 ? 78.188  24.176 98.188  1.00 14.90 ? 269  VAL A CG2 1 
ATOM   1832 N  N   . GLN A 1 270 ? 81.298  25.154 98.215  1.00 15.06 ? 270  GLN A N   1 
ATOM   1833 C  CA  . GLN A 1 270 ? 81.887  26.276 98.900  1.00 15.16 ? 270  GLN A CA  1 
ATOM   1834 C  C   . GLN A 1 270 ? 80.778  27.285 99.115  1.00 14.63 ? 270  GLN A C   1 
ATOM   1835 O  O   . GLN A 1 270 ? 79.986  27.494 98.187  1.00 15.92 ? 270  GLN A O   1 
ATOM   1836 C  CB  . GLN A 1 270 ? 82.949  26.902 97.983  1.00 15.71 ? 270  GLN A CB  1 
ATOM   1837 C  CG  . GLN A 1 270 ? 83.579  28.185 98.520  1.00 18.26 ? 270  GLN A CG  1 
ATOM   1838 C  CD  . GLN A 1 270 ? 84.746  28.633 97.656  1.00 14.76 ? 270  GLN A CD  1 
ATOM   1839 O  OE1 . GLN A 1 270 ? 85.901  28.328 97.990  1.00 17.93 ? 270  GLN A OE1 1 
ATOM   1840 N  NE2 . GLN A 1 270 ? 84.475  29.375 96.589  1.00 16.15 ? 270  GLN A NE2 1 
ATOM   1841 N  N   . PRO A 1 271 ? 80.662  27.912 100.294 1.00 15.66 ? 271  PRO A N   1 
ATOM   1842 C  CA  . PRO A 1 271 ? 79.491  28.775 100.537 1.00 16.36 ? 271  PRO A CA  1 
ATOM   1843 C  C   . PRO A 1 271 ? 79.587  30.173 99.935  1.00 15.76 ? 271  PRO A C   1 
ATOM   1844 O  O   . PRO A 1 271 ? 79.010  31.112 100.479 1.00 17.84 ? 271  PRO A O   1 
ATOM   1845 C  CB  . PRO A 1 271 ? 79.414  28.827 102.070 1.00 16.95 ? 271  PRO A CB  1 
ATOM   1846 C  CG  . PRO A 1 271 ? 80.893  28.728 102.483 1.00 17.51 ? 271  PRO A CG  1 
ATOM   1847 C  CD  . PRO A 1 271 ? 81.535  27.801 101.480 1.00 17.05 ? 271  PRO A CD  1 
ATOM   1848 N  N   . PHE A 1 272 ? 80.181  30.298 98.752  1.00 15.46 ? 272  PHE A N   1 
ATOM   1849 C  CA  . PHE A 1 272 ? 80.229  31.543 97.991  1.00 15.61 ? 272  PHE A CA  1 
ATOM   1850 C  C   . PHE A 1 272 ? 80.964  31.233 96.701  1.00 16.05 ? 272  PHE A C   1 
ATOM   1851 O  O   . PHE A 1 272 ? 81.737  30.272 96.617  1.00 15.59 ? 272  PHE A O   1 
ATOM   1852 C  CB  . PHE A 1 272 ? 80.985  32.653 98.759  1.00 15.81 ? 272  PHE A CB  1 
ATOM   1853 C  CG  . PHE A 1 272 ? 82.348  32.231 99.242  1.00 18.86 ? 272  PHE A CG  1 
ATOM   1854 C  CD1 . PHE A 1 272 ? 83.470  32.367 98.440  1.00 21.32 ? 272  PHE A CD1 1 
ATOM   1855 C  CD2 . PHE A 1 272 ? 82.496  31.679 100.501 1.00 19.81 ? 272  PHE A CD2 1 
ATOM   1856 C  CE1 . PHE A 1 272 ? 84.733  31.954 98.911  1.00 22.84 ? 272  PHE A CE1 1 
ATOM   1857 C  CE2 . PHE A 1 272 ? 83.741  31.285 100.972 1.00 23.27 ? 272  PHE A CE2 1 
ATOM   1858 C  CZ  . PHE A 1 272 ? 84.848  31.413 100.154 1.00 20.81 ? 272  PHE A CZ  1 
ATOM   1859 N  N   . PHE A 1 273 ? 80.722  32.060 95.694  1.00 14.09 ? 273  PHE A N   1 
ATOM   1860 C  CA  . PHE A 1 273 ? 81.567  32.082 94.511  1.00 14.15 ? 273  PHE A CA  1 
ATOM   1861 C  C   . PHE A 1 273 ? 81.722  33.528 94.088  1.00 14.89 ? 273  PHE A C   1 
ATOM   1862 O  O   . PHE A 1 273 ? 80.718  34.192 93.792  1.00 15.72 ? 273  PHE A O   1 
ATOM   1863 C  CB  . PHE A 1 273 ? 80.973  31.311 93.328  1.00 18.89 ? 273  PHE A CB  1 
ATOM   1864 C  CG  . PHE A 1 273 ? 81.786  31.506 92.075  1.00 20.26 ? 273  PHE A CG  1 
ATOM   1865 C  CD1 . PHE A 1 273 ? 82.947  30.792 91.890  1.00 20.32 ? 273  PHE A CD1 1 
ATOM   1866 C  CD2 . PHE A 1 273 ? 81.459  32.495 91.158  1.00 17.35 ? 273  PHE A CD2 1 
ATOM   1867 C  CE1 . PHE A 1 273 ? 83.741  31.004 90.769  1.00 19.00 ? 273  PHE A CE1 1 
ATOM   1868 C  CE2 . PHE A 1 273 ? 82.259  32.721 90.036  1.00 21.00 ? 273  PHE A CE2 1 
ATOM   1869 C  CZ  . PHE A 1 273 ? 83.397  31.978 89.863  1.00 19.43 ? 273  PHE A CZ  1 
ATOM   1870 N  N   . ILE A 1 274 ? 82.964  33.999 94.023  1.00 14.95 ? 274  ILE A N   1 
ATOM   1871 C  CA  . ILE A 1 274 ? 83.282  35.334 93.530  1.00 15.95 ? 274  ILE A CA  1 
ATOM   1872 C  C   . ILE A 1 274 ? 84.193  35.170 92.324  1.00 14.38 ? 274  ILE A C   1 
ATOM   1873 O  O   . ILE A 1 274 ? 85.296  34.618 92.442  1.00 16.44 ? 274  ILE A O   1 
ATOM   1874 C  CB  . ILE A 1 274 ? 83.948  36.188 94.618  1.00 16.75 ? 274  ILE A CB  1 
ATOM   1875 C  CG1 . ILE A 1 274 ? 83.028  36.308 95.849  1.00 16.84 ? 274  ILE A CG1 1 
ATOM   1876 C  CG2 . ILE A 1 274 ? 84.293  37.560 94.054  1.00 20.45 ? 274  ILE A CG2 1 
ATOM   1877 C  CD1 . ILE A 1 274 ? 81.721  37.048 95.569  1.00 21.20 ? 274  ILE A CD1 1 
ATOM   1878 N  N   . GLY A 1 275 ? 83.725  35.622 91.155  1.00 14.06 ? 275  GLY A N   1 
ATOM   1879 C  CA  . GLY A 1 275 ? 84.515  35.529 89.943  1.00 14.55 ? 275  GLY A CA  1 
ATOM   1880 C  C   . GLY A 1 275 ? 85.579  36.611 89.863  1.00 14.00 ? 275  GLY A C   1 
ATOM   1881 O  O   . GLY A 1 275 ? 85.675  37.501 90.709  1.00 15.62 ? 275  GLY A O   1 
ATOM   1882 N  N   . ASN A 1 276 ? 86.416  36.525 88.827  1.00 14.45 ? 276  ASN A N   1 
ATOM   1883 C  CA  . ASN A 1 276 ? 87.455  37.535 88.634  1.00 13.47 ? 276  ASN A CA  1 
ATOM   1884 C  C   . ASN A 1 276 ? 87.258  38.349 87.357  1.00 15.60 ? 276  ASN A C   1 
ATOM   1885 O  O   . ASN A 1 276 ? 88.137  39.145 86.984  1.00 15.02 ? 276  ASN A O   1 
ATOM   1886 C  CB  . ASN A 1 276 ? 88.870  36.946 88.713  1.00 15.25 ? 276  ASN A CB  1 
ATOM   1887 C  CG  . ASN A 1 276 ? 89.115  35.883 87.685  1.00 14.05 ? 276  ASN A CG  1 
ATOM   1888 O  OD1 . ASN A 1 276 ? 88.442  35.824 86.665  1.00 16.24 ? 276  ASN A OD1 1 
ATOM   1889 N  ND2 . ASN A 1 276 ? 90.111  35.045 87.935  1.00 22.60 ? 276  ASN A ND2 1 
ATOM   1890 N  N   . THR A 1 277 ? 86.121  38.167 86.690  1.00 12.95 ? 277  THR A N   1 
ATOM   1891 C  CA  . THR A 1 277 ? 85.704  39.015 85.587  1.00 12.40 ? 277  THR A CA  1 
ATOM   1892 C  C   . THR A 1 277 ? 84.223  39.298 85.779  1.00 12.83 ? 277  THR A C   1 
ATOM   1893 O  O   . THR A 1 277 ? 83.513  38.548 86.455  1.00 12.80 ? 277  THR A O   1 
ATOM   1894 C  CB  . THR A 1 277 ? 85.889  38.362 84.193  1.00 13.82 ? 277  THR A CB  1 
ATOM   1895 O  OG1 . THR A 1 277 ? 84.999  37.242 84.048  1.00 14.54 ? 277  THR A OG1 1 
ATOM   1896 C  CG2 . THR A 1 277 ? 87.338  37.904 83.967  1.00 15.32 ? 277  THR A CG2 1 
ATOM   1897 N  N   . ILE A 1 278 ? 83.757  40.389 85.169  1.00 12.81 ? 278  ILE A N   1 
ATOM   1898 C  CA  . ILE A 1 278 ? 82.328  40.681 85.087  1.00 12.21 ? 278  ILE A CA  1 
ATOM   1899 C  C   . ILE A 1 278 ? 81.911  40.670 83.626  1.00 13.62 ? 278  ILE A C   1 
ATOM   1900 O  O   . ILE A 1 278 ? 82.563  41.291 82.781  1.00 13.61 ? 278  ILE A O   1 
ATOM   1901 C  CB  . ILE A 1 278 ? 81.983  42.022 85.753  1.00 11.93 ? 278  ILE A CB  1 
ATOM   1902 C  CG1 . ILE A 1 278 ? 82.227  41.933 87.260  1.00 13.80 ? 278  ILE A CG1 1 
ATOM   1903 C  CG2 . ILE A 1 278 ? 80.516  42.370 85.491  1.00 14.67 ? 278  ILE A CG2 1 
ATOM   1904 C  CD1 . ILE A 1 278 ? 82.109  43.277 88.014  1.00 17.81 ? 278  ILE A CD1 1 
ATOM   1905 N  N   . ALA A 1 279 ? 80.841  39.959 83.339  1.00 12.89 ? 279  ALA A N   1 
ATOM   1906 C  CA  . ALA A 1 279 ? 80.237  39.911 82.023  1.00 12.18 ? 279  ALA A CA  1 
ATOM   1907 C  C   . ALA A 1 279 ? 78.846  40.530 82.069  1.00 14.07 ? 279  ALA A C   1 
ATOM   1908 O  O   . ALA A 1 279 ? 78.145  40.461 83.091  1.00 14.99 ? 279  ALA A O   1 
ATOM   1909 C  CB  . ALA A 1 279 ? 80.107  38.465 81.555  1.00 13.28 ? 279  ALA A CB  1 
ATOM   1910 N  N   . VAL A 1 280 ? 78.454  41.168 80.973  1.00 12.91 ? 280  VAL A N   1 
ATOM   1911 C  CA  . VAL A 1 280 ? 77.079  41.614 80.776  1.00 12.37 ? 280  VAL A CA  1 
ATOM   1912 C  C   . VAL A 1 280 ? 76.578  40.955 79.501  1.00 12.54 ? 280  VAL A C   1 
ATOM   1913 O  O   . VAL A 1 280 ? 77.251  41.013 78.465  1.00 12.17 ? 280  VAL A O   1 
ATOM   1914 C  CB  . VAL A 1 280 ? 76.956  43.152 80.710  1.00 11.98 ? 280  VAL A CB  1 
ATOM   1915 C  CG1 . VAL A 1 280 ? 75.501  43.570 80.831  1.00 12.78 ? 280  VAL A CG1 1 
ATOM   1916 C  CG2 . VAL A 1 280 ? 77.799  43.809 81.823  1.00 13.18 ? 280  VAL A CG2 1 
ATOM   1917 N  N   . ASN A 1 281 ? 75.424  40.288 79.589  1.00 12.21 ? 281  ASN A N   1 
ATOM   1918 C  CA  . ASN A 1 281 ? 74.879  39.559 78.436  1.00 11.40 ? 281  ASN A CA  1 
ATOM   1919 C  C   . ASN A 1 281 ? 75.926  38.654 77.798  1.00 12.13 ? 281  ASN A C   1 
ATOM   1920 O  O   . ASN A 1 281 ? 76.037  38.569 76.578  1.00 12.20 ? 281  ASN A O   1 
ATOM   1921 C  CB  . ASN A 1 281 ? 74.250  40.493 77.392  1.00 12.10 ? 281  ASN A CB  1 
ATOM   1922 C  CG  . ASN A 1 281 ? 73.052  41.238 77.942  1.00 12.86 ? 281  ASN A CG  1 
ATOM   1923 O  OD1 . ASN A 1 281 ? 72.634  40.983 79.072  1.00 13.64 ? 281  ASN A OD1 1 
ATOM   1924 N  ND2 . ASN A 1 281 ? 72.524  42.189 77.182  1.00 13.07 ? 281  ASN A ND2 1 
ATOM   1925 N  N   . GLY A 1 282 ? 76.715  37.990 78.636  1.00 12.66 ? 282  GLY A N   1 
ATOM   1926 C  CA  . GLY A 1 282 ? 77.642  36.990 78.139  1.00 12.42 ? 282  GLY A CA  1 
ATOM   1927 C  C   . GLY A 1 282 ? 78.923  37.514 77.538  1.00 13.16 ? 282  GLY A C   1 
ATOM   1928 O  O   . GLY A 1 282 ? 79.643  36.729 76.909  1.00 13.67 ? 282  GLY A O   1 
ATOM   1929 N  N   . LYS A 1 283 ? 79.237  38.801 77.709  1.00 12.19 ? 283  LYS A N   1 
ATOM   1930 C  CA  . LYS A 1 283 ? 80.505  39.346 77.227  1.00 11.73 ? 283  LYS A CA  1 
ATOM   1931 C  C   . LYS A 1 283 ? 81.220  40.067 78.362  1.00 13.41 ? 283  LYS A C   1 
ATOM   1932 O  O   . LYS A 1 283 ? 80.616  40.877 79.073  1.00 13.48 ? 283  LYS A O   1 
ATOM   1933 C  CB  . LYS A 1 283 ? 80.305  40.299 76.047  1.00 13.42 ? 283  LYS A CB  1 
ATOM   1934 C  CG  . LYS A 1 283 ? 79.640  39.628 74.831  1.00 14.40 ? 283  LYS A CG  1 
ATOM   1935 C  CD  . LYS A 1 283 ? 80.556  38.660 74.091  1.00 16.35 ? 283  LYS A CD  1 
ATOM   1936 C  CE  . LYS A 1 283 ? 79.830  38.068 72.895  1.00 19.66 ? 283  LYS A CE  1 
ATOM   1937 N  NZ  . LYS A 1 283 ? 80.600  37.010 72.205  1.00 19.80 ? 283  LYS A NZ  1 
ATOM   1938 N  N   . ILE A 1 284 ? 82.510  39.773 78.515  1.00 13.45 ? 284  ILE A N   1 
ATOM   1939 C  CA  . ILE A 1 284 ? 83.313  40.338 79.597  1.00 12.83 ? 284  ILE A CA  1 
ATOM   1940 C  C   . ILE A 1 284 ? 83.586  41.808 79.332  1.00 13.69 ? 284  ILE A C   1 
ATOM   1941 O  O   . ILE A 1 284 ? 84.079  42.178 78.256  1.00 14.84 ? 284  ILE A O   1 
ATOM   1942 C  CB  . ILE A 1 284 ? 84.619  39.554 79.736  1.00 12.94 ? 284  ILE A CB  1 
ATOM   1943 C  CG1 . ILE A 1 284 ? 84.342  38.147 80.265  1.00 13.47 ? 284  ILE A CG1 1 
ATOM   1944 C  CG2 . ILE A 1 284 ? 85.626  40.294 80.620  1.00 13.87 ? 284  ILE A CG2 1 
ATOM   1945 C  CD1 . ILE A 1 284 ? 85.511  37.219 80.057  1.00 15.28 ? 284  ILE A CD1 1 
ATOM   1946 N  N   . TRP A 1 285 ? 83.321  42.646 80.337  1.00 12.93 ? 285  TRP A N   1 
ATOM   1947 C  CA  . TRP A 1 285 ? 83.635  44.073 80.336  1.00 14.02 ? 285  TRP A CA  1 
ATOM   1948 C  C   . TRP A 1 285 ? 83.338  44.728 78.977  1.00 13.99 ? 285  TRP A C   1 
ATOM   1949 O  O   . TRP A 1 285 ? 84.243  45.233 78.311  1.00 15.23 ? 285  TRP A O   1 
ATOM   1950 C  CB  . TRP A 1 285 ? 85.075  44.325 80.779  1.00 13.84 ? 285  TRP A CB  1 
ATOM   1951 C  CG  . TRP A 1 285 ? 85.273  44.016 82.238  1.00 13.49 ? 285  TRP A CG  1 
ATOM   1952 C  CD1 . TRP A 1 285 ? 84.486  44.437 83.274  1.00 13.41 ? 285  TRP A CD1 1 
ATOM   1953 C  CD2 . TRP A 1 285 ? 86.300  43.184 82.823  1.00 13.55 ? 285  TRP A CD2 1 
ATOM   1954 N  NE1 . TRP A 1 285 ? 84.975  43.941 84.470  1.00 14.26 ? 285  TRP A NE1 1 
ATOM   1955 C  CE2 . TRP A 1 285 ? 86.090  43.184 84.217  1.00 13.52 ? 285  TRP A CE2 1 
ATOM   1956 C  CE3 . TRP A 1 285 ? 87.409  42.488 82.306  1.00 14.44 ? 285  TRP A CE3 1 
ATOM   1957 C  CZ2 . TRP A 1 285 ? 86.916  42.476 85.110  1.00 13.08 ? 285  TRP A CZ2 1 
ATOM   1958 C  CZ3 . TRP A 1 285 ? 88.247  41.785 83.201  1.00 15.06 ? 285  TRP A CZ3 1 
ATOM   1959 C  CH2 . TRP A 1 285 ? 87.970  41.769 84.583  1.00 14.81 ? 285  TRP A CH2 1 
ATOM   1960 N  N   . PRO A 1 286 ? 82.092  44.684 78.535  1.00 12.58 ? 286  PRO A N   1 
ATOM   1961 C  CA  . PRO A 1 286 ? 81.765  45.157 77.186  1.00 12.76 ? 286  PRO A CA  1 
ATOM   1962 C  C   . PRO A 1 286 ? 81.521  46.666 77.146  1.00 14.83 ? 286  PRO A C   1 
ATOM   1963 O  O   . PRO A 1 286 ? 81.480  47.369 78.167  1.00 15.04 ? 286  PRO A O   1 
ATOM   1964 C  CB  . PRO A 1 286 ? 80.483  44.386 76.877  1.00 12.58 ? 286  PRO A CB  1 
ATOM   1965 C  CG  . PRO A 1 286 ? 79.766  44.294 78.232  1.00 14.01 ? 286  PRO A CG  1 
ATOM   1966 C  CD  . PRO A 1 286 ? 80.897  44.231 79.278  1.00 12.47 ? 286  PRO A CD  1 
ATOM   1967 N  N   . LYS A 1 287 ? 81.404  47.171 75.915  1.00 13.60 ? 287  LYS A N   1 
ATOM   1968 C  CA  . LYS A 1 287 ? 80.950  48.527 75.665  1.00 15.32 ? 287  LYS A CA  1 
ATOM   1969 C  C   . LYS A 1 287 ? 79.614  48.465 74.945  1.00 15.70 ? 287  LYS A C   1 
ATOM   1970 O  O   . LYS A 1 287 ? 79.276  47.470 74.295  1.00 15.92 ? 287  LYS A O   1 
ATOM   1971 C  CB  . LYS A 1 287 ? 81.959  49.285 74.800  1.00 18.17 ? 287  LYS A CB  1 
ATOM   1972 C  CG  . LYS A 1 287 ? 82.151  48.602 73.444  1.00 20.82 ? 287  LYS A CG  1 
ATOM   1973 C  CD  . LYS A 1 287 ? 82.865  49.410 72.412  1.00 30.22 ? 287  LYS A CD  1 
ATOM   1974 C  CE  . LYS A 1 287 ? 83.200  48.501 71.242  1.00 27.15 ? 287  LYS A CE  1 
ATOM   1975 N  NZ  . LYS A 1 287 ? 82.115  48.411 70.227  1.00 32.01 ? 287  LYS A NZ  1 
ATOM   1976 N  N   . LEU A 1 288 ? 78.830  49.522 75.109  1.00 14.53 ? 288  LEU A N   1 
ATOM   1977 C  CA  . LEU A 1 288 ? 77.587  49.687 74.362  1.00 15.24 ? 288  LEU A CA  1 
ATOM   1978 C  C   . LEU A 1 288 ? 77.634  51.049 73.699  1.00 15.14 ? 288  LEU A C   1 
ATOM   1979 O  O   . LEU A 1 288 ? 77.763  52.072 74.377  1.00 16.58 ? 288  LEU A O   1 
ATOM   1980 C  CB  . LEU A 1 288 ? 76.366  49.567 75.282  1.00 14.68 ? 288  LEU A CB  1 
ATOM   1981 C  CG  . LEU A 1 288 ? 75.014  49.798 74.584  1.00 14.84 ? 288  LEU A CG  1 
ATOM   1982 C  CD1 . LEU A 1 288 ? 74.684  48.698 73.586  1.00 16.50 ? 288  LEU A CD1 1 
ATOM   1983 C  CD2 . LEU A 1 288 ? 73.875  49.934 75.619  1.00 17.78 ? 288  LEU A CD2 1 
ATOM   1984 N  N   . THR A 1 289 ? 77.522  51.071 72.382  1.00 15.49 ? 289  THR A N   1 
ATOM   1985 C  CA  . THR A 1 289 ? 77.551  52.320 71.640  1.00 16.19 ? 289  THR A CA  1 
ATOM   1986 C  C   . THR A 1 289 ? 76.125  52.851 71.553  1.00 17.61 ? 289  THR A C   1 
ATOM   1987 O  O   . THR A 1 289 ? 75.230  52.170 71.042  1.00 21.30 ? 289  THR A O   1 
ATOM   1988 C  CB  . THR A 1 289 ? 78.116  52.063 70.249  1.00 18.73 ? 289  THR A CB  1 
ATOM   1989 O  OG1 . THR A 1 289 ? 79.366  51.368 70.367  1.00 21.37 ? 289  THR A OG1 1 
ATOM   1990 C  CG2 . THR A 1 289 ? 78.370  53.370 69.528  1.00 20.06 ? 289  THR A CG2 1 
ATOM   1991 N  N   . VAL A 1 290 ? 75.913  54.052 72.075  1.00 15.56 ? 290  VAL A N   1 
ATOM   1992 C  CA  . VAL A 1 290 ? 74.584  54.626 72.232  1.00 17.49 ? 290  VAL A CA  1 
ATOM   1993 C  C   . VAL A 1 290 ? 74.520  55.987 71.548  1.00 17.22 ? 290  VAL A C   1 
ATOM   1994 O  O   . VAL A 1 290 ? 75.531  56.668 71.330  1.00 19.44 ? 290  VAL A O   1 
ATOM   1995 C  CB  . VAL A 1 290 ? 74.169  54.757 73.714  1.00 15.67 ? 290  VAL A CB  1 
ATOM   1996 C  CG1 . VAL A 1 290 ? 74.086  53.384 74.373  1.00 15.98 ? 290  VAL A CG1 1 
ATOM   1997 C  CG2 . VAL A 1 290 ? 75.145  55.691 74.493  1.00 16.93 ? 290  VAL A CG2 1 
ATOM   1998 N  N   . GLU A 1 291 ? 73.281  56.364 71.194  1.00 17.77 ? 291  GLU A N   1 
ATOM   1999 C  CA  . GLU A 1 291 ? 72.943  57.701 70.736  1.00 17.72 ? 291  GLU A CA  1 
ATOM   2000 C  C   . GLU A 1 291 ? 72.738  58.622 71.934  1.00 19.31 ? 291  GLU A C   1 
ATOM   2001 O  O   . GLU A 1 291 ? 72.455  58.155 73.043  1.00 17.77 ? 291  GLU A O   1 
ATOM   2002 C  CB  . GLU A 1 291 ? 71.635  57.665 69.943  1.00 22.47 ? 291  GLU A CB  1 
ATOM   2003 C  CG  . GLU A 1 291 ? 71.618  56.701 68.773  1.00 22.60 ? 291  GLU A CG  1 
ATOM   2004 C  CD  . GLU A 1 291 ? 70.240  56.585 68.128  1.00 22.06 ? 291  GLU A CD  1 
ATOM   2005 O  OE1 . GLU A 1 291 ? 69.498  57.598 68.084  1.00 23.51 ? 291  GLU A OE1 1 
ATOM   2006 O  OE2 . GLU A 1 291 ? 69.908  55.472 67.683  1.00 24.08 ? 291  GLU A OE2 1 
ATOM   2007 N  N   . PRO A 1 292 ? 72.869  59.943 71.739  1.00 17.73 ? 292  PRO A N   1 
ATOM   2008 C  CA  . PRO A 1 292 ? 72.671  60.925 72.829  1.00 21.27 ? 292  PRO A CA  1 
ATOM   2009 C  C   . PRO A 1 292 ? 71.186  61.199 73.066  1.00 20.47 ? 292  PRO A C   1 
ATOM   2010 O  O   . PRO A 1 292 ? 70.620  62.237 72.688  1.00 21.73 ? 292  PRO A O   1 
ATOM   2011 C  CB  . PRO A 1 292 ? 73.407  62.160 72.303  1.00 21.19 ? 292  PRO A CB  1 
ATOM   2012 C  CG  . PRO A 1 292 ? 73.263  62.068 70.809  1.00 22.51 ? 292  PRO A CG  1 
ATOM   2013 C  CD  . PRO A 1 292 ? 73.363  60.591 70.501  1.00 20.90 ? 292  PRO A CD  1 
ATOM   2014 N  N   . ARG A 1 293 ? 70.532  60.229 73.694  1.00 20.89 ? 293  ARG A N   1 
ATOM   2015 C  CA  . ARG A 1 293 ? 69.096  60.258 73.952  1.00 18.01 ? 293  ARG A CA  1 
ATOM   2016 C  C   . ARG A 1 293 ? 68.816  59.289 75.097  1.00 18.01 ? 293  ARG A C   1 
ATOM   2017 O  O   . ARG A 1 293 ? 69.739  58.737 75.708  1.00 17.54 ? 293  ARG A O   1 
ATOM   2018 C  CB  . ARG A 1 293 ? 68.305  59.885 72.700  1.00 19.70 ? 293  ARG A CB  1 
ATOM   2019 C  CG  . ARG A 1 293 ? 68.675  58.504 72.187  1.00 19.60 ? 293  ARG A CG  1 
ATOM   2020 C  CD  . ARG A 1 293 ? 67.567  57.945 71.334  1.00 25.44 ? 293  ARG A CD  1 
ATOM   2021 N  NE  . ARG A 1 293 ? 66.539  57.435 72.230  1.00 24.09 ? 293  ARG A NE  1 
ATOM   2022 C  CZ  . ARG A 1 293 ? 65.290  57.166 71.887  1.00 24.84 ? 293  ARG A CZ  1 
ATOM   2023 N  NH1 . ARG A 1 293 ? 64.843  57.379 70.654  1.00 27.54 ? 293  ARG A NH1 1 
ATOM   2024 N  NH2 . ARG A 1 293 ? 64.460  56.699 72.811  1.00 20.59 ? 293  ARG A NH2 1 
ATOM   2025 N  N   . LYS A 1 294 ? 67.537  59.072 75.381  1.00 17.66 ? 294  LYS A N   1 
ATOM   2026 C  CA  . LYS A 1 294 ? 67.140  58.275 76.532  1.00 15.95 ? 294  LYS A CA  1 
ATOM   2027 C  C   . LYS A 1 294 ? 66.962  56.814 76.154  1.00 16.03 ? 294  LYS A C   1 
ATOM   2028 O  O   . LYS A 1 294 ? 66.465  56.482 75.068  1.00 16.90 ? 294  LYS A O   1 
ATOM   2029 C  CB  . LYS A 1 294 ? 65.851  58.816 77.155  1.00 18.74 ? 294  LYS A CB  1 
ATOM   2030 C  CG  . LYS A 1 294 ? 65.984  60.232 77.691  1.00 19.57 ? 294  LYS A CG  1 
ATOM   2031 C  CD  . LYS A 1 294 ? 64.747  60.646 78.486  1.00 19.60 ? 294  LYS A CD  1 
ATOM   2032 C  CE  . LYS A 1 294 ? 63.502  60.927 77.645  1.00 21.54 ? 294  LYS A CE  1 
ATOM   2033 N  NZ  . LYS A 1 294 ? 63.726  61.674 76.365  1.00 19.99 ? 294  LYS A NZ  1 
ATOM   2034 N  N   . TYR A 1 295 ? 67.420  55.948 77.044  1.00 15.20 ? 295  TYR A N   1 
ATOM   2035 C  CA  . TYR A 1 295 ? 67.295  54.510 76.913  1.00 15.40 ? 295  TYR A CA  1 
ATOM   2036 C  C   . TYR A 1 295 ? 66.692  53.967 78.194  1.00 16.59 ? 295  TYR A C   1 
ATOM   2037 O  O   . TYR A 1 295 ? 66.903  54.519 79.282  1.00 16.10 ? 295  TYR A O   1 
ATOM   2038 C  CB  . TYR A 1 295 ? 68.687  53.862 76.810  1.00 13.77 ? 295  TYR A CB  1 
ATOM   2039 C  CG  . TYR A 1 295 ? 69.349  53.981 75.441  1.00 14.80 ? 295  TYR A CG  1 
ATOM   2040 C  CD1 . TYR A 1 295 ? 69.804  55.215 74.974  1.00 13.63 ? 295  TYR A CD1 1 
ATOM   2041 C  CD2 . TYR A 1 295 ? 69.533  52.865 74.622  1.00 14.98 ? 295  TYR A CD2 1 
ATOM   2042 C  CE1 . TYR A 1 295 ? 70.406  55.333 73.735  1.00 17.19 ? 295  TYR A CE1 1 
ATOM   2043 C  CE2 . TYR A 1 295 ? 70.147  52.977 73.380  1.00 16.45 ? 295  TYR A CE2 1 
ATOM   2044 C  CZ  . TYR A 1 295 ? 70.581  54.212 72.953  1.00 16.54 ? 295  TYR A CZ  1 
ATOM   2045 O  OH  . TYR A 1 295 ? 71.181  54.338 71.719  1.00 18.71 ? 295  TYR A OH  1 
ATOM   2046 N  N   . ARG A 1 296 ? 65.985  52.849 78.055  1.00 14.46 ? 296  ARG A N   1 
ATOM   2047 C  CA  . ARG A 1 296 ? 65.530  52.051 79.186  1.00 12.71 ? 296  ARG A CA  1 
ATOM   2048 C  C   . ARG A 1 296 ? 66.451  50.853 79.285  1.00 13.93 ? 296  ARG A C   1 
ATOM   2049 O  O   . ARG A 1 296 ? 66.660  50.145 78.295  1.00 15.08 ? 296  ARG A O   1 
ATOM   2050 C  CB  . ARG A 1 296 ? 64.115  51.552 78.915  1.00 14.48 ? 296  ARG A CB  1 
ATOM   2051 C  CG  . ARG A 1 296 ? 63.604  50.542 79.948  1.00 15.00 ? 296  ARG A CG  1 
ATOM   2052 C  CD  . ARG A 1 296 ? 62.133  50.212 79.658  1.00 14.29 ? 296  ARG A CD  1 
ATOM   2053 N  NE  . ARG A 1 296 ? 61.555  49.353 80.685  1.00 15.99 ? 296  ARG A NE  1 
ATOM   2054 C  CZ  . ARG A 1 296 ? 60.263  49.055 80.767  1.00 15.85 ? 296  ARG A CZ  1 
ATOM   2055 N  NH1 . ARG A 1 296 ? 59.380  49.547 79.913  1.00 19.26 ? 296  ARG A NH1 1 
ATOM   2056 N  NH2 . ARG A 1 296 ? 59.836  48.293 81.770  1.00 19.47 ? 296  ARG A NH2 1 
ATOM   2057 N  N   . PHE A 1 297 ? 67.009  50.630 80.466  1.00 12.98 ? 297  PHE A N   1 
ATOM   2058 C  CA  . PHE A 1 297 ? 67.834  49.455 80.704  1.00 12.35 ? 297  PHE A CA  1 
ATOM   2059 C  C   . PHE A 1 297 ? 67.169  48.593 81.763  1.00 12.04 ? 297  PHE A C   1 
ATOM   2060 O  O   . PHE A 1 297 ? 66.778  49.096 82.828  1.00 13.16 ? 297  PHE A O   1 
ATOM   2061 C  CB  . PHE A 1 297 ? 69.233  49.855 81.169  1.00 13.50 ? 297  PHE A CB  1 
ATOM   2062 C  CG  . PHE A 1 297 ? 70.031  50.511 80.104  1.00 13.44 ? 297  PHE A CG  1 
ATOM   2063 C  CD1 . PHE A 1 297 ? 70.539  49.756 79.056  1.00 13.58 ? 297  PHE A CD1 1 
ATOM   2064 C  CD2 . PHE A 1 297 ? 70.223  51.869 80.113  1.00 13.76 ? 297  PHE A CD2 1 
ATOM   2065 C  CE1 . PHE A 1 297 ? 71.243  50.360 78.034  1.00 13.83 ? 297  PHE A CE1 1 
ATOM   2066 C  CE2 . PHE A 1 297 ? 70.945  52.479 79.097  1.00 15.90 ? 297  PHE A CE2 1 
ATOM   2067 C  CZ  . PHE A 1 297 ? 71.454  51.729 78.066  1.00 13.51 ? 297  PHE A CZ  1 
ATOM   2068 N  N   . ARG A 1 298 ? 67.092  47.299 81.500  1.00 12.55 ? 298  ARG A N   1 
ATOM   2069 C  CA  . ARG A 1 298 ? 66.484  46.335 82.428  1.00 13.04 ? 298  ARG A CA  1 
ATOM   2070 C  C   . ARG A 1 298 ? 67.632  45.596 83.095  1.00 12.27 ? 298  ARG A C   1 
ATOM   2071 O  O   . ARG A 1 298 ? 68.195  44.655 82.525  1.00 12.97 ? 298  ARG A O   1 
ATOM   2072 C  CB  . ARG A 1 298 ? 65.569  45.377 81.667  1.00 12.06 ? 298  ARG A CB  1 
ATOM   2073 C  CG  . ARG A 1 298 ? 64.588  46.097 80.772  1.00 13.07 ? 298  ARG A CG  1 
ATOM   2074 C  CD  . ARG A 1 298 ? 63.565  45.158 80.216  1.00 14.57 ? 298  ARG A CD  1 
ATOM   2075 N  NE  . ARG A 1 298 ? 62.560  45.868 79.435  1.00 15.58 ? 298  ARG A NE  1 
ATOM   2076 C  CZ  . ARG A 1 298 ? 61.257  45.756 79.664  1.00 14.66 ? 298  ARG A CZ  1 
ATOM   2077 N  NH1 . ARG A 1 298 ? 60.806  45.058 80.690  1.00 17.34 ? 298  ARG A NH1 1 
ATOM   2078 N  NH2 . ARG A 1 298 ? 60.402  46.379 78.862  1.00 16.56 ? 298  ARG A NH2 1 
ATOM   2079 N  N   . ILE A 1 299 ? 67.990  46.008 84.302  1.00 11.86 ? 299  ILE A N   1 
ATOM   2080 C  CA  . ILE A 1 299 ? 69.250  45.590 84.909  1.00 12.50 ? 299  ILE A CA  1 
ATOM   2081 C  C   . ILE A 1 299 ? 68.995  44.452 85.880  1.00 12.67 ? 299  ILE A C   1 
ATOM   2082 O  O   . ILE A 1 299 ? 68.180  44.576 86.805  1.00 15.03 ? 299  ILE A O   1 
ATOM   2083 C  CB  . ILE A 1 299 ? 69.944  46.771 85.599  1.00 12.72 ? 299  ILE A CB  1 
ATOM   2084 C  CG1 . ILE A 1 299 ? 70.000  47.992 84.650  1.00 13.48 ? 299  ILE A CG1 1 
ATOM   2085 C  CG2 . ILE A 1 299 ? 71.322  46.346 86.105  1.00 16.07 ? 299  ILE A CG2 1 
ATOM   2086 C  CD1 . ILE A 1 299 ? 70.866  49.133 85.174  1.00 16.70 ? 299  ILE A CD1 1 
ATOM   2087 N  N   . LEU A 1 300 ? 69.666  43.334 85.656  1.00 11.67 ? 300  LEU A N   1 
ATOM   2088 C  CA  . LEU A 1 300 ? 69.495  42.141 86.473  1.00 11.01 ? 300  LEU A CA  1 
ATOM   2089 C  C   . LEU A 1 300 ? 70.851  41.667 86.954  1.00 11.15 ? 300  LEU A C   1 
ATOM   2090 O  O   . LEU A 1 300 ? 71.770  41.527 86.157  1.00 11.58 ? 300  LEU A O   1 
ATOM   2091 C  CB  . LEU A 1 300 ? 68.860  41.037 85.618  1.00 11.06 ? 300  LEU A CB  1 
ATOM   2092 C  CG  . LEU A 1 300 ? 68.994  39.583 86.102  1.00 12.03 ? 300  LEU A CG  1 
ATOM   2093 C  CD1 . LEU A 1 300 ? 68.196  39.321 87.391  1.00 13.23 ? 300  LEU A CD1 1 
ATOM   2094 C  CD2 . LEU A 1 300 ? 68.528  38.642 85.006  1.00 12.51 ? 300  LEU A CD2 1 
ATOM   2095 N  N   . ASN A 1 301 ? 70.974  41.386 88.248  1.00 11.85 ? 301  ASN A N   1 
ATOM   2096 C  CA  . ASN A 1 301 ? 72.142  40.671 88.757  1.00 10.89 ? 301  ASN A CA  1 
ATOM   2097 C  C   . ASN A 1 301 ? 71.807  39.183 88.727  1.00 11.57 ? 301  ASN A C   1 
ATOM   2098 O  O   . ASN A 1 301 ? 70.977  38.713 89.512  1.00 11.84 ? 301  ASN A O   1 
ATOM   2099 C  CB  . ASN A 1 301 ? 72.458  41.120 90.181  1.00 11.19 ? 301  ASN A CB  1 
ATOM   2100 C  CG  . ASN A 1 301 ? 73.685  40.418 90.751  1.00 13.19 ? 301  ASN A CG  1 
ATOM   2101 O  OD1 . ASN A 1 301 ? 74.187  39.488 90.137  1.00 12.94 ? 301  ASN A OD1 1 
ATOM   2102 N  ND2 . ASN A 1 301 ? 74.176  40.869 91.898  1.00 13.74 ? 301  ASN A ND2 1 
ATOM   2103 N  N   . ALA A 1 302 ? 72.415  38.447 87.797  1.00 10.83 ? 302  ALA A N   1 
ATOM   2104 C  CA  . ALA A 1 302 ? 72.223  37.008 87.707  1.00 10.47 ? 302  ALA A CA  1 
ATOM   2105 C  C   . ALA A 1 302 ? 73.464  36.234 88.150  1.00 11.83 ? 302  ALA A C   1 
ATOM   2106 O  O   . ALA A 1 302 ? 73.704  35.105 87.696  1.00 12.04 ? 302  ALA A O   1 
ATOM   2107 C  CB  . ALA A 1 302 ? 71.782  36.602 86.300  1.00 13.09 ? 302  ALA A CB  1 
ATOM   2108 N  N   . SER A 1 303 ? 74.251  36.823 89.047  1.00 11.19 ? 303  SER A N   1 
ATOM   2109 C  CA  . SER A 1 303 ? 75.441  36.192 89.604  1.00 11.11 ? 303  SER A CA  1 
ATOM   2110 C  C   . SER A 1 303 ? 75.040  35.145 90.635  1.00 11.54 ? 303  SER A C   1 
ATOM   2111 O  O   . SER A 1 303 ? 73.963  35.205 91.241  1.00 12.97 ? 303  SER A O   1 
ATOM   2112 C  CB  . SER A 1 303 ? 76.306  37.231 90.324  1.00 11.85 ? 303  SER A CB  1 
ATOM   2113 O  OG  . SER A 1 303 ? 76.684  38.258 89.395  1.00 12.99 ? 303  SER A OG  1 
ATOM   2114 N  N   . ASN A 1 304 ? 75.951  34.202 90.872  1.00 11.74 ? 304  ASN A N   1 
ATOM   2115 C  CA  . ASN A 1 304 ? 75.684  33.178 91.869  1.00 12.09 ? 304  ASN A CA  1 
ATOM   2116 C  C   . ASN A 1 304 ? 75.658  33.757 93.281  1.00 12.37 ? 304  ASN A C   1 
ATOM   2117 O  O   . ASN A 1 304 ? 74.807  33.370 94.097  1.00 12.70 ? 304  ASN A O   1 
ATOM   2118 C  CB  . ASN A 1 304 ? 76.772  32.105 91.799  1.00 13.44 ? 304  ASN A CB  1 
ATOM   2119 C  CG  . ASN A 1 304 ? 76.468  31.011 90.780  1.00 12.95 ? 304  ASN A CG  1 
ATOM   2120 O  OD1 . ASN A 1 304 ? 75.903  31.266 89.710  1.00 15.29 ? 304  ASN A OD1 1 
ATOM   2121 N  ND2 . ASN A 1 304 ? 76.832  29.779 91.110  1.00 12.97 ? 304  ASN A ND2 1 
ATOM   2122 N  N   . THR A 1 305 ? 76.638  34.619 93.619  1.00 12.60 ? 305  THR A N   1 
ATOM   2123 C  CA  . THR A 1 305 ? 76.814  35.179 94.968  1.00 12.61 ? 305  THR A CA  1 
ATOM   2124 C  C   . THR A 1 305 ? 76.993  36.689 94.957  1.00 12.13 ? 305  THR A C   1 
ATOM   2125 O  O   . THR A 1 305 ? 76.490  37.369 95.851  1.00 14.33 ? 305  THR A O   1 
ATOM   2126 C  CB  . THR A 1 305 ? 78.112  34.605 95.617  1.00 14.26 ? 305  THR A CB  1 
ATOM   2127 O  OG1 . THR A 1 305 ? 78.024  33.194 95.791  1.00 14.81 ? 305  THR A OG1 1 
ATOM   2128 C  CG2 . THR A 1 305 ? 78.386  35.258 96.980  1.00 16.28 ? 305  THR A CG2 1 
ATOM   2129 N  N   . ASN A 1 306 ? 77.741  37.218 93.992  1.00 13.38 ? 306  ASN A N   1 
ATOM   2130 C  CA  . ASN A 1 306 ? 78.271  38.574 94.095  1.00 13.23 ? 306  ASN A CA  1 
ATOM   2131 C  C   . ASN A 1 306 ? 77.175  39.626 93.972  1.00 12.10 ? 306  ASN A C   1 
ATOM   2132 O  O   . ASN A 1 306 ? 76.221  39.483 93.198  1.00 14.42 ? 306  ASN A O   1 
ATOM   2133 C  CB  . ASN A 1 306 ? 79.303  38.787 92.987  1.00 13.78 ? 306  ASN A CB  1 
ATOM   2134 C  CG  . ASN A 1 306 ? 80.436  39.718 93.394  1.00 18.17 ? 306  ASN A CG  1 
ATOM   2135 O  OD1 . ASN A 1 306 ? 80.367  40.417 94.404  1.00 18.46 ? 306  ASN A OD1 1 
ATOM   2136 N  ND2 . ASN A 1 306 ? 81.479  39.757 92.569  1.00 19.90 ? 306  ASN A ND2 1 
ATOM   2137 N  N   . ALA A 1 307 ? 77.327  40.698 94.737  1.00 14.28 ? 307  ALA A N   1 
ATOM   2138 C  CA  . ALA A 1 307 ? 76.438  41.845 94.671  1.00 14.38 ? 307  ALA A CA  1 
ATOM   2139 C  C   . ALA A 1 307 ? 77.187  43.047 94.112  1.00 15.13 ? 307  ALA A C   1 
ATOM   2140 O  O   . ALA A 1 307 ? 78.404  43.170 94.284  1.00 17.96 ? 307  ALA A O   1 
ATOM   2141 C  CB  . ALA A 1 307 ? 75.899  42.183 96.067  1.00 16.01 ? 307  ALA A CB  1 
ATOM   2142 N  N   . TYR A 1 308 ? 76.459  43.950 93.445  1.00 14.25 ? 308  TYR A N   1 
ATOM   2143 C  CA  . TYR A 1 308 ? 77.081  45.114 92.815  1.00 14.54 ? 308  TYR A CA  1 
ATOM   2144 C  C   . TYR A 1 308 ? 76.386  46.372 93.296  1.00 15.70 ? 308  TYR A C   1 
ATOM   2145 O  O   . TYR A 1 308 ? 75.211  46.350 93.651  1.00 18.25 ? 308  TYR A O   1 
ATOM   2146 C  CB  . TYR A 1 308 ? 76.998  45.041 91.268  1.00 14.14 ? 308  TYR A CB  1 
ATOM   2147 C  CG  . TYR A 1 308 ? 77.496  43.711 90.768  1.00 13.35 ? 308  TYR A CG  1 
ATOM   2148 C  CD1 . TYR A 1 308 ? 78.842  43.399 90.795  1.00 18.79 ? 308  TYR A CD1 1 
ATOM   2149 C  CD2 . TYR A 1 308 ? 76.617  42.745 90.364  1.00 15.17 ? 308  TYR A CD2 1 
ATOM   2150 C  CE1 . TYR A 1 308 ? 79.300  42.137 90.406  1.00 18.20 ? 308  TYR A CE1 1 
ATOM   2151 C  CE2 . TYR A 1 308 ? 77.056  41.495 89.952  1.00 15.00 ? 308  TYR A CE2 1 
ATOM   2152 C  CZ  . TYR A 1 308 ? 78.402  41.203 89.975  1.00 15.05 ? 308  TYR A CZ  1 
ATOM   2153 O  OH  . TYR A 1 308 ? 78.841  39.959 89.604  1.00 13.88 ? 308  TYR A OH  1 
ATOM   2154 N  N   . THR A 1 309 ? 77.117  47.471 93.329  1.00 14.88 ? 309  THR A N   1 
ATOM   2155 C  CA  . THR A 1 309 ? 76.489  48.777 93.493  1.00 15.70 ? 309  THR A CA  1 
ATOM   2156 C  C   . THR A 1 309 ? 76.800  49.615 92.262  1.00 14.90 ? 309  THR A C   1 
ATOM   2157 O  O   . THR A 1 309 ? 77.939  50.044 92.076  1.00 16.36 ? 309  THR A O   1 
ATOM   2158 C  CB  . THR A 1 309 ? 76.951  49.458 94.773  1.00 16.68 ? 309  THR A CB  1 
ATOM   2159 O  OG1 . THR A 1 309 ? 76.517  48.676 95.897  1.00 20.02 ? 309  THR A OG1 1 
ATOM   2160 C  CG2 . THR A 1 309 ? 76.315  50.810 94.867  1.00 19.87 ? 309  THR A CG2 1 
ATOM   2161 N  N   . LEU A 1 310 ? 75.792  49.835 91.422  1.00 13.93 ? 310  LEU A N   1 
ATOM   2162 C  CA  . LEU A 1 310 ? 76.006  50.510 90.151  1.00 14.19 ? 310  LEU A CA  1 
ATOM   2163 C  C   . LEU A 1 310 ? 76.121  52.015 90.333  1.00 15.19 ? 310  LEU A C   1 
ATOM   2164 O  O   . LEU A 1 310 ? 75.370  52.634 91.099  1.00 16.91 ? 310  LEU A O   1 
ATOM   2165 C  CB  . LEU A 1 310 ? 74.840  50.197 89.215  1.00 15.05 ? 310  LEU A CB  1 
ATOM   2166 C  CG  . LEU A 1 310 ? 74.991  48.906 88.407  1.00 16.93 ? 310  LEU A CG  1 
ATOM   2167 C  CD1 . LEU A 1 310 ? 75.084  47.679 89.309  1.00 16.70 ? 310  LEU A CD1 1 
ATOM   2168 C  CD2 . LEU A 1 310 ? 73.784  48.732 87.483  1.00 18.58 ? 310  LEU A CD2 1 
ATOM   2169 N  N   . ARG A 1 311 ? 77.064  52.598 89.600  1.00 15.27 ? 311  ARG A N   1 
ATOM   2170 C  CA  . ARG A 1 311 ? 77.228  54.045 89.523  1.00 15.21 ? 311  ARG A CA  1 
ATOM   2171 C  C   . ARG A 1 311 ? 77.587  54.398 88.086  1.00 17.91 ? 311  ARG A C   1 
ATOM   2172 O  O   . ARG A 1 311 ? 78.377  53.697 87.454  1.00 17.11 ? 311  ARG A O   1 
ATOM   2173 C  CB  . ARG A 1 311 ? 78.343  54.475 90.477  1.00 17.05 ? 311  ARG A CB  1 
ATOM   2174 C  CG  . ARG A 1 311 ? 78.480  55.970 90.629  1.00 19.79 ? 311  ARG A CG  1 
ATOM   2175 C  CD  . ARG A 1 311 ? 79.409  56.274 91.787  1.00 22.20 ? 311  ARG A CD  1 
ATOM   2176 N  NE  . ARG A 1 311 ? 79.516  57.703 92.054  1.00 29.92 ? 311  ARG A NE  1 
ATOM   2177 C  CZ  . ARG A 1 311 ? 80.534  58.438 91.645  1.00 28.60 ? 311  ARG A CZ  1 
ATOM   2178 N  NH1 . ARG A 1 311 ? 81.487  57.923 90.881  1.00 32.24 ? 311  ARG A NH1 1 
ATOM   2179 N  NH2 . ARG A 1 311 ? 80.602  59.719 92.010  1.00 27.19 ? 311  ARG A NH2 1 
ATOM   2180 N  N   . LEU A 1 312 ? 76.978  55.460 87.557  1.00 16.63 ? 312  LEU A N   1 
ATOM   2181 C  CA  . LEU A 1 312 ? 77.118  55.821 86.144  1.00 16.99 ? 312  LEU A CA  1 
ATOM   2182 C  C   . LEU A 1 312 ? 78.063  57.014 86.015  1.00 16.37 ? 312  LEU A C   1 
ATOM   2183 O  O   . LEU A 1 312 ? 77.719  58.133 86.421  1.00 18.24 ? 312  LEU A O   1 
ATOM   2184 C  CB  . LEU A 1 312 ? 75.751  56.188 85.589  1.00 18.12 ? 312  LEU A CB  1 
ATOM   2185 C  CG  . LEU A 1 312 ? 75.793  56.710 84.154  1.00 16.78 ? 312  LEU A CG  1 
ATOM   2186 C  CD1 . LEU A 1 312 ? 76.255  55.601 83.194  1.00 20.45 ? 312  LEU A CD1 1 
ATOM   2187 C  CD2 . LEU A 1 312 ? 74.420  57.273 83.759  1.00 19.86 ? 312  LEU A CD2 1 
ATOM   2188 N  N   . GLY A 1 313 ? 79.243  56.799 85.431  1.00 18.06 ? 313  GLY A N   1 
ATOM   2189 C  CA  . GLY A 1 313 ? 80.165  57.923 85.293  1.00 18.21 ? 313  GLY A CA  1 
ATOM   2190 C  C   . GLY A 1 313 ? 80.465  58.564 86.640  1.00 21.26 ? 313  GLY A C   1 
ATOM   2191 O  O   . GLY A 1 313 ? 80.558  57.874 87.663  1.00 22.91 ? 313  GLY A O   1 
ATOM   2192 N  N   . ASP A 1 314 ? 80.572  59.902 86.660  1.00 23.43 ? 314  ASP A N   1 
ATOM   2193 C  CA  . ASP A 1 314 ? 80.822  60.639 87.904  1.00 27.01 ? 314  ASP A CA  1 
ATOM   2194 C  C   . ASP A 1 314 ? 79.528  60.900 88.679  1.00 25.54 ? 314  ASP A C   1 
ATOM   2195 O  O   . ASP A 1 314 ? 79.097  62.038 88.890  1.00 28.34 ? 314  ASP A O   1 
ATOM   2196 C  CB  . ASP A 1 314 ? 81.609  61.922 87.658  1.00 31.64 ? 314  ASP A CB  1 
ATOM   2197 C  CG  . ASP A 1 314 ? 82.951  61.657 87.016  1.00 40.32 ? 314  ASP A CG  1 
ATOM   2198 O  OD1 . ASP A 1 314 ? 83.546  60.600 87.329  1.00 41.90 ? 314  ASP A OD1 1 
ATOM   2199 O  OD2 . ASP A 1 314 ? 83.436  62.533 86.258  1.00 43.00 ? 314  ASP A OD2 1 
ATOM   2200 N  N   . GLY A 1 315 ? 78.908  59.801 89.104  1.00 22.41 ? 315  GLY A N   1 
ATOM   2201 C  CA  . GLY A 1 315 ? 77.686  59.913 89.880  1.00 24.45 ? 315  GLY A CA  1 
ATOM   2202 C  C   . GLY A 1 315 ? 76.564  60.594 89.128  1.00 20.37 ? 315  GLY A C   1 
ATOM   2203 O  O   . GLY A 1 315 ? 75.817  61.387 89.716  1.00 25.57 ? 315  GLY A O   1 
ATOM   2204 N  N   . ARG A 1 316 ? 76.436  60.303 87.839  1.00 22.63 ? 316  ARG A N   1 
ATOM   2205 C  CA  . ARG A 1 316 ? 75.378  60.878 87.029  1.00 21.98 ? 316  ARG A CA  1 
ATOM   2206 C  C   . ARG A 1 316 ? 74.031  60.289 87.423  1.00 18.67 ? 316  ARG A C   1 
ATOM   2207 O  O   . ARG A 1 316 ? 73.925  59.125 87.825  1.00 19.74 ? 316  ARG A O   1 
ATOM   2208 C  CB  . ARG A 1 316 ? 75.634  60.604 85.547  1.00 21.73 ? 316  ARG A CB  1 
ATOM   2209 C  CG  . ARG A 1 316 ? 76.900  61.229 84.977  1.00 23.15 ? 316  ARG A CG  1 
ATOM   2210 C  CD  . ARG A 1 316 ? 77.027  62.708 85.317  1.00 23.92 ? 316  ARG A CD  1 
ATOM   2211 N  NE  . ARG A 1 316 ? 78.316  63.220 84.875  1.00 23.48 ? 316  ARG A NE  1 
ATOM   2212 C  CZ  . ARG A 1 316 ? 78.594  64.509 84.745  1.00 29.88 ? 316  ARG A CZ  1 
ATOM   2213 N  NH1 . ARG A 1 316 ? 77.704  65.438 85.045  1.00 39.24 ? 316  ARG A NH1 1 
ATOM   2214 N  NH2 . ARG A 1 316 ? 79.793  64.873 84.304  1.00 33.78 ? 316  ARG A NH2 1 
ATOM   2215 N  N   . LYS A 1 317 ? 72.994  61.105 87.283  1.00 20.28 ? 317  LYS A N   1 
ATOM   2216 C  CA  . LYS A 1 317 ? 71.646  60.705 87.648  1.00 21.07 ? 317  LYS A CA  1 
ATOM   2217 C  C   . LYS A 1 317 ? 71.049  59.764 86.609  1.00 21.09 ? 317  LYS A C   1 
ATOM   2218 O  O   . LYS A 1 317 ? 71.305  59.874 85.403  1.00 21.86 ? 317  LYS A O   1 
ATOM   2219 C  CB  . LYS A 1 317 ? 70.765  61.952 87.749  1.00 23.16 ? 317  LYS A CB  1 
ATOM   2220 C  CG  . LYS A 1 317 ? 71.137  62.867 88.911  1.00 29.29 ? 317  LYS A CG  1 
ATOM   2221 C  CD  . LYS A 1 317 ? 70.432  64.225 88.808  1.00 38.11 ? 317  LYS A CD  1 
ATOM   2222 C  CE  . LYS A 1 317 ? 71.114  65.309 89.658  1.00 42.07 ? 317  LYS A CE  1 
ATOM   2223 N  NZ  . LYS A 1 317 ? 72.146  64.772 90.602  1.00 44.84 ? 317  LYS A NZ  1 
ATOM   2224 N  N   . PHE A 1 318 ? 70.233  58.830 87.095  1.00 18.94 ? 318  PHE A N   1 
ATOM   2225 C  CA  . PHE A 1 318 ? 69.390  58.006 86.238  1.00 17.39 ? 318  PHE A CA  1 
ATOM   2226 C  C   . PHE A 1 318 ? 68.074  57.777 86.976  1.00 19.81 ? 318  PHE A C   1 
ATOM   2227 O  O   . PHE A 1 318 ? 67.933  58.139 88.144  1.00 19.87 ? 318  PHE A O   1 
ATOM   2228 C  CB  . PHE A 1 318 ? 70.062  56.689 85.829  1.00 18.68 ? 318  PHE A CB  1 
ATOM   2229 C  CG  . PHE A 1 318 ? 70.700  55.923 86.973  1.00 16.48 ? 318  PHE A CG  1 
ATOM   2230 C  CD1 . PHE A 1 318 ? 71.980  56.233 87.446  1.00 18.38 ? 318  PHE A CD1 1 
ATOM   2231 C  CD2 . PHE A 1 318 ? 70.009  54.886 87.585  1.00 17.09 ? 318  PHE A CD2 1 
ATOM   2232 C  CE1 . PHE A 1 318 ? 72.563  55.495 88.506  1.00 16.70 ? 318  PHE A CE1 1 
ATOM   2233 C  CE2 . PHE A 1 318 ? 70.590  54.152 88.625  1.00 18.35 ? 318  PHE A CE2 1 
ATOM   2234 C  CZ  . PHE A 1 318 ? 71.863  54.458 89.089  1.00 17.97 ? 318  PHE A CZ  1 
ATOM   2235 N  N   . TYR A 1 319 ? 67.073  57.243 86.273  1.00 16.00 ? 319  TYR A N   1 
ATOM   2236 C  CA  . TYR A 1 319 ? 65.694  57.288 86.773  1.00 15.30 ? 319  TYR A CA  1 
ATOM   2237 C  C   . TYR A 1 319 ? 65.114  55.889 86.866  1.00 16.30 ? 319  TYR A C   1 
ATOM   2238 O  O   . TYR A 1 319 ? 64.830  55.260 85.846  1.00 18.56 ? 319  TYR A O   1 
ATOM   2239 C  CB  . TYR A 1 319 ? 64.834  58.216 85.917  1.00 16.36 ? 319  TYR A CB  1 
ATOM   2240 C  CG  . TYR A 1 319 ? 65.349  59.613 86.073  1.00 19.35 ? 319  TYR A CG  1 
ATOM   2241 C  CD1 . TYR A 1 319 ? 66.402  60.065 85.295  1.00 18.91 ? 319  TYR A CD1 1 
ATOM   2242 C  CD2 . TYR A 1 319 ? 64.872  60.436 87.092  1.00 22.78 ? 319  TYR A CD2 1 
ATOM   2243 C  CE1 . TYR A 1 319 ? 66.932  61.330 85.486  1.00 22.11 ? 319  TYR A CE1 1 
ATOM   2244 C  CE2 . TYR A 1 319 ? 65.394  61.711 87.293  1.00 27.41 ? 319  TYR A CE2 1 
ATOM   2245 C  CZ  . TYR A 1 319 ? 66.423  62.142 86.488  1.00 26.16 ? 319  TYR A CZ  1 
ATOM   2246 O  OH  . TYR A 1 319 ? 66.959  63.391 86.669  1.00 33.46 ? 319  TYR A OH  1 
ATOM   2247 N  N   . GLN A 1 320 ? 64.931  55.411 88.087  1.00 15.54 ? 320  GLN A N   1 
ATOM   2248 C  CA  . GLN A 1 320 ? 64.358  54.091 88.287  1.00 15.81 ? 320  GLN A CA  1 
ATOM   2249 C  C   . GLN A 1 320 ? 62.871  54.122 87.963  1.00 16.84 ? 320  GLN A C   1 
ATOM   2250 O  O   . GLN A 1 320 ? 62.137  55.014 88.420  1.00 16.91 ? 320  GLN A O   1 
ATOM   2251 C  CB  . GLN A 1 320 ? 64.544  53.692 89.744  1.00 17.94 ? 320  GLN A CB  1 
ATOM   2252 C  CG  . GLN A 1 320 ? 64.146  52.261 90.020  1.00 17.44 ? 320  GLN A CG  1 
ATOM   2253 C  CD  . GLN A 1 320 ? 64.328  51.908 91.489  1.00 17.09 ? 320  GLN A CD  1 
ATOM   2254 O  OE1 . GLN A 1 320 ? 63.777  52.586 92.360  1.00 19.08 ? 320  GLN A OE1 1 
ATOM   2255 N  NE2 . GLN A 1 320 ? 65.065  50.837 91.769  1.00 17.42 ? 320  GLN A NE2 1 
ATOM   2256 N  N   . ILE A 1 321 ? 62.421  53.137 87.187  1.00 15.27 ? 321  ILE A N   1 
ATOM   2257 C  CA  . ILE A 1 321 ? 61.005  52.995 86.869  1.00 16.50 ? 321  ILE A CA  1 
ATOM   2258 C  C   . ILE A 1 321 ? 60.409  51.688 87.355  1.00 16.91 ? 321  ILE A C   1 
ATOM   2259 O  O   . ILE A 1 321 ? 59.170  51.579 87.414  1.00 17.16 ? 321  ILE A O   1 
ATOM   2260 C  CB  . ILE A 1 321 ? 60.711  53.211 85.368  1.00 14.78 ? 321  ILE A CB  1 
ATOM   2261 C  CG1 . ILE A 1 321 ? 61.371  52.127 84.519  1.00 15.90 ? 321  ILE A CG1 1 
ATOM   2262 C  CG2 . ILE A 1 321 ? 61.129  54.637 84.949  1.00 16.40 ? 321  ILE A CG2 1 
ATOM   2263 C  CD1 . ILE A 1 321 ? 60.904  52.164 83.057  1.00 18.82 ? 321  ILE A CD1 1 
ATOM   2264 N  N   . SER A 1 322 ? 61.230  50.708 87.737  1.00 15.18 ? 322  SER A N   1 
ATOM   2265 C  CA  . SER A 1 322 ? 60.645  49.477 88.270  1.00 15.07 ? 322  SER A CA  1 
ATOM   2266 C  C   . SER A 1 322 ? 61.641  48.797 89.185  1.00 13.87 ? 322  SER A C   1 
ATOM   2267 O  O   . SER A 1 322 ? 62.857  48.980 89.039  1.00 16.20 ? 322  SER A O   1 
ATOM   2268 C  CB  . SER A 1 322 ? 60.213  48.516 87.153  1.00 18.46 ? 322  SER A CB  1 
ATOM   2269 O  OG  . SER A 1 322 ? 61.350  48.006 86.470  1.00 17.69 ? 322  SER A OG  1 
ATOM   2270 N  N   . THR A 1 323 ? 61.097  47.993 90.100  1.00 15.35 ? 323  THR A N   1 
ATOM   2271 C  CA  . THR A 1 323 ? 61.808  47.020 90.931  1.00 14.99 ? 323  THR A CA  1 
ATOM   2272 C  C   . THR A 1 323 ? 61.369  45.627 90.478  1.00 15.37 ? 323  THR A C   1 
ATOM   2273 O  O   . THR A 1 323 ? 60.639  45.501 89.490  1.00 16.67 ? 323  THR A O   1 
ATOM   2274 C  CB  . THR A 1 323 ? 61.498  47.272 92.413  1.00 18.55 ? 323  THR A CB  1 
ATOM   2275 O  OG1 . THR A 1 323 ? 60.078  47.369 92.600  1.00 17.09 ? 323  THR A OG1 1 
ATOM   2276 C  CG2 . THR A 1 323 ? 62.127  48.588 92.857  1.00 20.40 ? 323  THR A CG2 1 
ATOM   2277 N  N   . ASP A 1 324 ? 61.788  44.585 91.222  1.00 14.57 ? 324  ASP A N   1 
ATOM   2278 C  CA  . ASP A 1 324 ? 61.572  43.195 90.798  1.00 15.02 ? 324  ASP A CA  1 
ATOM   2279 C  C   . ASP A 1 324 ? 60.157  42.968 90.282  1.00 16.98 ? 324  ASP A C   1 
ATOM   2280 O  O   . ASP A 1 324 ? 59.954  42.286 89.271  1.00 17.64 ? 324  ASP A O   1 
ATOM   2281 C  CB  . ASP A 1 324 ? 61.740  42.223 91.978  1.00 15.70 ? 324  ASP A CB  1 
ATOM   2282 C  CG  . ASP A 1 324 ? 63.057  42.353 92.726  1.00 15.01 ? 324  ASP A CG  1 
ATOM   2283 O  OD1 . ASP A 1 324 ? 64.080  42.762 92.159  1.00 15.64 ? 324  ASP A OD1 1 
ATOM   2284 O  OD2 . ASP A 1 324 ? 63.020  42.004 93.941  1.00 15.88 ? 324  ASP A OD2 1 
ATOM   2285 N  N   . GLY A 1 325 ? 59.159  43.448 91.021  1.00 16.05 ? 325  GLY A N   1 
ATOM   2286 C  CA  . GLY A 1 325 ? 57.778  43.109 90.779  1.00 17.62 ? 325  GLY A CA  1 
ATOM   2287 C  C   . GLY A 1 325 ? 57.005  44.001 89.862  1.00 17.33 ? 325  GLY A C   1 
ATOM   2288 O  O   . GLY A 1 325 ? 55.853  43.674 89.561  1.00 19.86 ? 325  GLY A O   1 
ATOM   2289 N  N   . GLY A 1 326 ? 57.538  45.135 89.461  1.00 17.76 ? 326  GLY A N   1 
ATOM   2290 C  CA  . GLY A 1 326 ? 56.811  45.950 88.511  1.00 23.05 ? 326  GLY A CA  1 
ATOM   2291 C  C   . GLY A 1 326 ? 57.079  47.429 88.679  1.00 21.13 ? 326  GLY A C   1 
ATOM   2292 O  O   . GLY A 1 326 ? 57.982  47.851 89.399  1.00 17.72 ? 326  GLY A O   1 
ATOM   2293 N  N   . LEU A 1 327 ? 56.284  48.201 87.953  1.00 18.93 ? 327  LEU A N   1 
ATOM   2294 C  CA  . LEU A 1 327 ? 56.513  49.631 87.844  1.00 19.54 ? 327  LEU A CA  1 
ATOM   2295 C  C   . LEU A 1 327 ? 56.234  50.341 89.158  1.00 21.48 ? 327  LEU A C   1 
ATOM   2296 O  O   . LEU A 1 327 ? 55.329  49.972 89.913  1.00 22.66 ? 327  LEU A O   1 
ATOM   2297 C  CB  . LEU A 1 327 ? 55.601  50.247 86.787  1.00 22.13 ? 327  LEU A CB  1 
ATOM   2298 C  CG  . LEU A 1 327 ? 55.918  49.865 85.337  1.00 19.86 ? 327  LEU A CG  1 
ATOM   2299 C  CD1 . LEU A 1 327 ? 54.696  50.201 84.439  1.00 21.20 ? 327  LEU A CD1 1 
ATOM   2300 C  CD2 . LEU A 1 327 ? 57.199  50.511 84.819  1.00 20.84 ? 327  LEU A CD2 1 
ATOM   2301 N  N   . LEU A 1 328 ? 57.011  51.391 89.411  1.00 20.27 ? 328  LEU A N   1 
ATOM   2302 C  CA  . LEU A 1 328 ? 56.807  52.258 90.560  1.00 22.21 ? 328  LEU A CA  1 
ATOM   2303 C  C   . LEU A 1 328 ? 55.648  53.216 90.319  1.00 24.58 ? 328  LEU A C   1 
ATOM   2304 O  O   . LEU A 1 328 ? 55.104  53.316 89.217  1.00 24.05 ? 328  LEU A O   1 
ATOM   2305 C  CB  . LEU A 1 328 ? 58.074  53.044 90.899  1.00 21.66 ? 328  LEU A CB  1 
ATOM   2306 C  CG  . LEU A 1 328 ? 59.370  52.237 91.005  1.00 19.17 ? 328  LEU A CG  1 
ATOM   2307 C  CD1 . LEU A 1 328 ? 60.566  53.164 91.186  1.00 21.62 ? 328  LEU A CD1 1 
ATOM   2308 C  CD2 . LEU A 1 328 ? 59.272  51.273 92.194  1.00 20.03 ? 328  LEU A CD2 1 
ATOM   2309 N  N   . THR A 1 329 ? 55.268  53.934 91.375  1.00 26.28 ? 329  THR A N   1 
ATOM   2310 C  CA  . THR A 1 329 ? 54.241  54.961 91.192  1.00 25.71 ? 329  THR A CA  1 
ATOM   2311 C  C   . THR A 1 329 ? 54.735  56.067 90.277  1.00 24.44 ? 329  THR A C   1 
ATOM   2312 O  O   . THR A 1 329 ? 53.967  56.608 89.480  1.00 25.45 ? 329  THR A O   1 
ATOM   2313 C  CB  . THR A 1 329 ? 53.795  55.546 92.530  1.00 30.59 ? 329  THR A CB  1 
ATOM   2314 O  OG1 . THR A 1 329 ? 54.946  55.939 93.286  1.00 39.87 ? 329  THR A OG1 1 
ATOM   2315 C  CG2 . THR A 1 329 ? 53.015  54.503 93.317  1.00 35.73 ? 329  THR A CG2 1 
ATOM   2316 N  N   . GLU A 1 330 ? 56.011  56.411 90.389  1.00 22.67 ? 330  GLU A N   1 
ATOM   2317 C  CA  . GLU A 1 330 ? 56.613  57.501 89.642  1.00 22.12 ? 330  GLU A CA  1 
ATOM   2318 C  C   . GLU A 1 330 ? 58.115  57.257 89.586  1.00 23.83 ? 330  GLU A C   1 
ATOM   2319 O  O   . GLU A 1 330 ? 58.656  56.520 90.421  1.00 21.06 ? 330  GLU A O   1 
ATOM   2320 C  CB  . GLU A 1 330 ? 56.258  58.847 90.297  1.00 25.31 ? 330  GLU A CB  1 
ATOM   2321 C  CG  . GLU A 1 330 ? 57.178  59.298 91.414  1.00 32.21 ? 330  GLU A CG  1 
ATOM   2322 C  CD  . GLU A 1 330 ? 56.796  60.668 91.926  1.00 40.77 ? 330  GLU A CD  1 
ATOM   2323 O  OE1 . GLU A 1 330 ? 55.877  60.727 92.766  1.00 39.99 ? 330  GLU A OE1 1 
ATOM   2324 O  OE2 . GLU A 1 330 ? 57.381  61.681 91.475  1.00 48.17 ? 330  GLU A OE2 1 
ATOM   2325 N  N   . PRO A 1 331 ? 58.805  57.790 88.581  1.00 20.63 ? 331  PRO A N   1 
ATOM   2326 C  CA  . PRO A 1 331 ? 60.252  57.565 88.502  1.00 19.38 ? 331  PRO A CA  1 
ATOM   2327 C  C   . PRO A 1 331 ? 60.966  58.141 89.716  1.00 19.43 ? 331  PRO A C   1 
ATOM   2328 O  O   . PRO A 1 331 ? 60.556  59.160 90.281  1.00 24.12 ? 331  PRO A O   1 
ATOM   2329 C  CB  . PRO A 1 331 ? 60.668  58.281 87.205  1.00 20.21 ? 331  PRO A CB  1 
ATOM   2330 C  CG  . PRO A 1 331 ? 59.387  58.392 86.408  1.00 19.13 ? 331  PRO A CG  1 
ATOM   2331 C  CD  . PRO A 1 331 ? 58.291  58.552 87.429  1.00 20.04 ? 331  PRO A CD  1 
ATOM   2332 N  N   . VAL A 1 332 ? 62.048  57.471 90.108  1.00 18.16 ? 332  VAL A N   1 
ATOM   2333 C  CA  . VAL A 1 332 ? 62.860  57.854 91.259  1.00 22.92 ? 332  VAL A CA  1 
ATOM   2334 C  C   . VAL A 1 332 ? 64.257  58.214 90.765  1.00 19.18 ? 332  VAL A C   1 
ATOM   2335 O  O   . VAL A 1 332 ? 64.924  57.393 90.126  1.00 18.20 ? 332  VAL A O   1 
ATOM   2336 C  CB  . VAL A 1 332 ? 62.928  56.711 92.285  1.00 23.87 ? 332  VAL A CB  1 
ATOM   2337 C  CG1 . VAL A 1 332 ? 63.854  57.067 93.434  1.00 27.03 ? 332  VAL A CG1 1 
ATOM   2338 C  CG2 . VAL A 1 332 ? 61.520  56.391 92.797  1.00 24.25 ? 332  VAL A CG2 1 
ATOM   2339 N  N   . GLU A 1 333 ? 64.709  59.425 91.070  1.00 20.10 ? 333  GLU A N   1 
ATOM   2340 C  CA  . GLU A 1 333 ? 66.077  59.817 90.746  1.00 19.61 ? 333  GLU A CA  1 
ATOM   2341 C  C   . GLU A 1 333 ? 67.067  59.052 91.613  1.00 19.75 ? 333  GLU A C   1 
ATOM   2342 O  O   . GLU A 1 333 ? 66.995  59.121 92.842  1.00 23.80 ? 333  GLU A O   1 
ATOM   2343 C  CB  . GLU A 1 333 ? 66.261  61.305 91.005  1.00 25.33 ? 333  GLU A CB  1 
ATOM   2344 C  CG  . GLU A 1 333 ? 67.465  61.893 90.304  1.00 24.86 ? 333  GLU A CG  1 
ATOM   2345 C  CD  . GLU A 1 333 ? 67.518  63.403 90.440  1.00 33.99 ? 333  GLU A CD  1 
ATOM   2346 O  OE1 . GLU A 1 333 ? 66.973  64.097 89.558  1.00 37.38 ? 333  GLU A OE1 1 
ATOM   2347 O  OE2 . GLU A 1 333 ? 68.097  63.884 91.437  1.00 37.12 ? 333  GLU A OE2 1 
ATOM   2348 N  N   . LEU A 1 334 ? 68.011  58.356 90.983  1.00 17.51 ? 334  LEU A N   1 
ATOM   2349 C  CA  . LEU A 1 334 ? 69.074  57.637 91.675  1.00 18.19 ? 334  LEU A CA  1 
ATOM   2350 C  C   . LEU A 1 334 ? 70.426  58.092 91.158  1.00 18.35 ? 334  LEU A C   1 
ATOM   2351 O  O   . LEU A 1 334 ? 70.562  58.510 90.000  1.00 19.46 ? 334  LEU A O   1 
ATOM   2352 C  CB  . LEU A 1 334 ? 69.002  56.124 91.456  1.00 18.91 ? 334  LEU A CB  1 
ATOM   2353 C  CG  . LEU A 1 334 ? 67.678  55.448 91.794  1.00 17.24 ? 334  LEU A CG  1 
ATOM   2354 C  CD1 . LEU A 1 334 ? 67.782  53.979 91.474  1.00 18.19 ? 334  LEU A CD1 1 
ATOM   2355 C  CD2 . LEU A 1 334 ? 67.348  55.629 93.273  1.00 22.39 ? 334  LEU A CD2 1 
ATOM   2356 N  N   . THR A 1 335 ? 71.436  57.999 92.025  1.00 19.92 ? 335  THR A N   1 
ATOM   2357 C  CA  . THR A 1 335 ? 72.827  58.037 91.586  1.00 19.84 ? 335  THR A CA  1 
ATOM   2358 C  C   . THR A 1 335 ? 73.592  56.761 91.896  1.00 19.87 ? 335  THR A C   1 
ATOM   2359 O  O   . THR A 1 335 ? 74.735  56.627 91.458  1.00 21.52 ? 335  THR A O   1 
ATOM   2360 C  CB  . THR A 1 335 ? 73.576  59.235 92.182  1.00 23.68 ? 335  THR A CB  1 
ATOM   2361 O  OG1 . THR A 1 335 ? 73.571  59.134 93.609  1.00 28.02 ? 335  THR A OG1 1 
ATOM   2362 C  CG2 . THR A 1 335 ? 72.913  60.558 91.758  1.00 21.32 ? 335  THR A CG2 1 
ATOM   2363 N  N   . THR A 1 336 ? 72.998  55.827 92.637  1.00 17.75 ? 336  THR A N   1 
ATOM   2364 C  CA  A THR A 1 336 ? 73.589  54.534 92.906  0.30 20.09 ? 336  THR A CA  1 
ATOM   2365 C  CA  B THR A 1 336 ? 73.594  54.520 92.891  0.70 19.93 ? 336  THR A CA  1 
ATOM   2366 C  C   . THR A 1 336 ? 72.484  53.483 92.914  1.00 20.33 ? 336  THR A C   1 
ATOM   2367 O  O   . THR A 1 336 ? 71.350  53.764 93.305  1.00 18.77 ? 336  THR A O   1 
ATOM   2368 C  CB  A THR A 1 336 ? 74.279  54.637 94.262  0.30 24.23 ? 336  THR A CB  1 
ATOM   2369 C  CB  B THR A 1 336 ? 74.376  54.418 94.226  0.70 22.17 ? 336  THR A CB  1 
ATOM   2370 O  OG1 A THR A 1 336 ? 75.575  55.235 94.104  0.30 29.01 ? 336  THR A OG1 1 
ATOM   2371 O  OG1 B THR A 1 336 ? 73.495  54.666 95.324  0.70 22.79 ? 336  THR A OG1 1 
ATOM   2372 C  CG2 A THR A 1 336 ? 74.391  53.335 94.892  0.30 20.36 ? 336  THR A CG2 1 
ATOM   2373 C  CG2 B THR A 1 336 ? 75.515  55.439 94.280  0.70 29.33 ? 336  THR A CG2 1 
ATOM   2374 N  N   . LEU A 1 337 ? 72.815  52.268 92.485  1.00 16.46 ? 337  LEU A N   1 
ATOM   2375 C  CA  . LEU A 1 337 ? 71.831  51.189 92.456  1.00 16.41 ? 337  LEU A CA  1 
ATOM   2376 C  C   . LEU A 1 337 ? 72.451  49.883 92.953  1.00 15.03 ? 337  LEU A C   1 
ATOM   2377 O  O   . LEU A 1 337 ? 73.103  49.172 92.174  1.00 16.20 ? 337  LEU A O   1 
ATOM   2378 C  CB  . LEU A 1 337 ? 71.262  51.033 91.049  1.00 15.50 ? 337  LEU A CB  1 
ATOM   2379 C  CG  . LEU A 1 337 ? 70.286  49.880 90.841  1.00 16.91 ? 337  LEU A CG  1 
ATOM   2380 C  CD1 . LEU A 1 337 ? 69.114  49.980 91.837  1.00 18.35 ? 337  LEU A CD1 1 
ATOM   2381 C  CD2 . LEU A 1 337 ? 69.800  49.850 89.388  1.00 17.85 ? 337  LEU A CD2 1 
ATOM   2382 N  N   . PRO A 1 338 ? 72.293  49.550 94.238  1.00 15.49 ? 338  PRO A N   1 
ATOM   2383 C  CA  . PRO A 1 338 ? 72.720  48.220 94.719  1.00 14.72 ? 338  PRO A CA  1 
ATOM   2384 C  C   . PRO A 1 338 ? 71.797  47.091 94.245  1.00 13.65 ? 338  PRO A C   1 
ATOM   2385 O  O   . PRO A 1 338 ? 70.568  47.221 94.228  1.00 17.10 ? 338  PRO A O   1 
ATOM   2386 C  CB  . PRO A 1 338 ? 72.763  48.373 96.247  1.00 18.61 ? 338  PRO A CB  1 
ATOM   2387 C  CG  . PRO A 1 338 ? 71.940  49.554 96.552  1.00 24.52 ? 338  PRO A CG  1 
ATOM   2388 C  CD  . PRO A 1 338 ? 71.783  50.410 95.317  1.00 17.87 ? 338  PRO A CD  1 
ATOM   2389 N  N   . LEU A 1 339 ? 72.410  45.983 93.820  1.00 13.00 ? 339  LEU A N   1 
ATOM   2390 C  CA  . LEU A 1 339 ? 71.673  44.805 93.372  1.00 13.38 ? 339  LEU A CA  1 
ATOM   2391 C  C   . LEU A 1 339 ? 72.374  43.548 93.872  1.00 15.05 ? 339  LEU A C   1 
ATOM   2392 O  O   . LEU A 1 339 ? 73.519  43.260 93.474  1.00 15.34 ? 339  LEU A O   1 
ATOM   2393 C  CB  . LEU A 1 339 ? 71.578  44.736 91.842  1.00 14.74 ? 339  LEU A CB  1 
ATOM   2394 C  CG  . LEU A 1 339 ? 70.774  45.836 91.154  1.00 16.23 ? 339  LEU A CG  1 
ATOM   2395 C  CD1 . LEU A 1 339 ? 71.088  45.762 89.657  1.00 17.18 ? 339  LEU A CD1 1 
ATOM   2396 C  CD2 . LEU A 1 339 ? 69.274  45.709 91.408  1.00 15.63 ? 339  LEU A CD2 1 
ATOM   2397 N  N   . GLU A 1 340 ? 71.670  42.786 94.711  1.00 13.48 ? 340  GLU A N   1 
ATOM   2398 C  CA  . GLU A 1 340 ? 72.090  41.446 95.105  1.00 13.64 ? 340  GLU A CA  1 
ATOM   2399 C  C   . GLU A 1 340 ? 71.700  40.454 94.018  1.00 12.37 ? 340  GLU A C   1 
ATOM   2400 O  O   . GLU A 1 340 ? 70.887  40.757 93.133  1.00 13.26 ? 340  GLU A O   1 
ATOM   2401 C  CB  . GLU A 1 340 ? 71.365  41.042 96.388  1.00 16.14 ? 340  GLU A CB  1 
ATOM   2402 C  CG  . GLU A 1 340 ? 71.721  41.873 97.626  1.00 16.43 ? 340  GLU A CG  1 
ATOM   2403 C  CD  . GLU A 1 340 ? 73.068  41.490 98.199  1.00 17.21 ? 340  GLU A CD  1 
ATOM   2404 O  OE1 . GLU A 1 340 ? 73.409  40.275 98.177  1.00 20.86 ? 340  GLU A OE1 1 
ATOM   2405 O  OE2 . GLU A 1 340 ? 73.772  42.406 98.679  1.00 20.10 ? 340  GLU A OE2 1 
ATOM   2406 N  N   . PRO A 1 341 ? 72.221  39.231 94.074  1.00 13.24 ? 341  PRO A N   1 
ATOM   2407 C  CA  . PRO A 1 341 ? 71.730  38.192 93.160  1.00 12.61 ? 341  PRO A CA  1 
ATOM   2408 C  C   . PRO A 1 341 ? 70.211  38.128 93.143  1.00 13.43 ? 341  PRO A C   1 
ATOM   2409 O  O   . PRO A 1 341 ? 69.540  38.134 94.188  1.00 13.85 ? 341  PRO A O   1 
ATOM   2410 C  CB  . PRO A 1 341 ? 72.338  36.903 93.716  1.00 13.53 ? 341  PRO A CB  1 
ATOM   2411 C  CG  . PRO A 1 341 ? 73.633  37.362 94.388  1.00 14.78 ? 341  PRO A CG  1 
ATOM   2412 C  CD  . PRO A 1 341 ? 73.379  38.786 94.892  1.00 13.40 ? 341  PRO A CD  1 
ATOM   2413 N  N   . ALA A 1 342 ? 69.672  38.081 91.926  1.00 12.10 ? 342  ALA A N   1 
ATOM   2414 C  CA  . ALA A 1 342 ? 68.276  37.947 91.525  1.00 12.43 ? 342  ALA A CA  1 
ATOM   2415 C  C   . ALA A 1 342 ? 67.498  39.249 91.603  1.00 11.92 ? 342  ALA A C   1 
ATOM   2416 O  O   . ALA A 1 342 ? 66.380  39.305 91.072  1.00 14.01 ? 342  ALA A O   1 
ATOM   2417 C  CB  . ALA A 1 342 ? 67.519  36.839 92.291  1.00 13.38 ? 342  ALA A CB  1 
ATOM   2418 N  N   . GLU A 1 343 ? 68.051  40.302 92.188  1.00 12.23 ? 343  GLU A N   1 
ATOM   2419 C  CA  . GLU A 1 343 ? 67.382  41.590 92.174  1.00 12.41 ? 343  GLU A CA  1 
ATOM   2420 C  C   . GLU A 1 343 ? 67.491  42.202 90.783  1.00 15.31 ? 343  GLU A C   1 
ATOM   2421 O  O   . GLU A 1 343 ? 68.479  42.008 90.056  1.00 14.12 ? 343  GLU A O   1 
ATOM   2422 C  CB  . GLU A 1 343 ? 68.054  42.532 93.169  1.00 13.83 ? 343  GLU A CB  1 
ATOM   2423 C  CG  . GLU A 1 343 ? 67.674  42.242 94.628  1.00 14.66 ? 343  GLU A CG  1 
ATOM   2424 C  CD  . GLU A 1 343 ? 68.059  43.373 95.535  1.00 15.46 ? 343  GLU A CD  1 
ATOM   2425 O  OE1 . GLU A 1 343 ? 69.275  43.609 95.728  1.00 19.28 ? 343  GLU A OE1 1 
ATOM   2426 O  OE2 . GLU A 1 343 ? 67.149  44.101 96.000  1.00 16.77 ? 343  GLU A OE2 1 
ATOM   2427 N  N   . ARG A 1 344 ? 66.460  42.952 90.409  1.00 14.47 ? 344  ARG A N   1 
ATOM   2428 C  CA  . ARG A 1 344 ? 66.519  43.678 89.152  1.00 14.41 ? 344  ARG A CA  1 
ATOM   2429 C  C   . ARG A 1 344 ? 65.772  44.994 89.269  1.00 12.70 ? 344  ARG A C   1 
ATOM   2430 O  O   . ARG A 1 344 ? 64.908  45.193 90.137  1.00 13.72 ? 344  ARG A O   1 
ATOM   2431 C  CB  . ARG A 1 344 ? 66.009  42.832 87.998  1.00 18.93 ? 344  ARG A CB  1 
ATOM   2432 C  CG  . ARG A 1 344 ? 64.646  42.334 88.203  1.00 19.56 ? 344  ARG A CG  1 
ATOM   2433 C  CD  . ARG A 1 344 ? 64.634  40.798 88.269  1.00 18.71 ? 344  ARG A CD  1 
ATOM   2434 N  NE  . ARG A 1 344 ? 63.265  40.343 88.459  1.00 14.51 ? 344  ARG A NE  1 
ATOM   2435 C  CZ  . ARG A 1 344 ? 62.762  39.852 89.577  1.00 13.84 ? 344  ARG A CZ  1 
ATOM   2436 N  NH1 . ARG A 1 344 ? 63.540  39.526 90.607  1.00 14.38 ? 344  ARG A NH1 1 
ATOM   2437 N  NH2 . ARG A 1 344 ? 61.453  39.609 89.635  1.00 13.93 ? 344  ARG A NH2 1 
ATOM   2438 N  N   . SER A 1 345 ? 66.133  45.906 88.375  1.00 13.14 ? 345  SER A N   1 
ATOM   2439 C  CA  . SER A 1 345 ? 65.494  47.202 88.329  1.00 12.37 ? 345  SER A CA  1 
ATOM   2440 C  C   . SER A 1 345 ? 65.614  47.746 86.924  1.00 13.03 ? 345  SER A C   1 
ATOM   2441 O  O   . SER A 1 345 ? 66.668  47.621 86.286  1.00 13.65 ? 345  SER A O   1 
ATOM   2442 C  CB  . SER A 1 345 ? 66.187  48.154 89.294  1.00 14.34 ? 345  SER A CB  1 
ATOM   2443 O  OG  . SER A 1 345 ? 65.532  49.396 89.274  1.00 14.93 ? 345  SER A OG  1 
ATOM   2444 N  N   . ASP A 1 346 ? 64.556  48.389 86.457  1.00 12.43 ? 346  ASP A N   1 
ATOM   2445 C  CA  . ASP A 1 346 ? 64.608  49.045 85.153  1.00 12.45 ? 346  ASP A CA  1 
ATOM   2446 C  C   . ASP A 1 346 ? 64.826  50.521 85.431  1.00 14.02 ? 346  ASP A C   1 
ATOM   2447 O  O   . ASP A 1 346 ? 64.166  51.098 86.313  1.00 13.71 ? 346  ASP A O   1 
ATOM   2448 C  CB  . ASP A 1 346 ? 63.273  48.889 84.425  1.00 14.76 ? 346  ASP A CB  1 
ATOM   2449 C  CG  . ASP A 1 346 ? 63.139  47.570 83.681  1.00 15.65 ? 346  ASP A CG  1 
ATOM   2450 O  OD1 . ASP A 1 346 ? 63.544  46.512 84.239  1.00 16.68 ? 346  ASP A OD1 1 
ATOM   2451 O  OD2 . ASP A 1 346 ? 62.417  47.540 82.659  1.00 18.06 ? 346  ASP A OD2 1 
ATOM   2452 N  N   . VAL A 1 347 ? 65.752  51.119 84.681  1.00 14.05 ? 347  VAL A N   1 
ATOM   2453 C  CA  . VAL A 1 347 ? 66.076  52.534 84.825  1.00 13.07 ? 347  VAL A CA  1 
ATOM   2454 C  C   . VAL A 1 347 ? 66.066  53.203 83.454  1.00 15.57 ? 347  VAL A C   1 
ATOM   2455 O  O   . VAL A 1 347 ? 66.244  52.567 82.414  1.00 15.56 ? 347  VAL A O   1 
ATOM   2456 C  CB  . VAL A 1 347 ? 67.450  52.774 85.500  1.00 15.56 ? 347  VAL A CB  1 
ATOM   2457 C  CG1 . VAL A 1 347 ? 67.522  52.097 86.873  1.00 14.01 ? 347  VAL A CG1 1 
ATOM   2458 C  CG2 . VAL A 1 347 ? 68.596  52.283 84.607  1.00 16.72 ? 347  VAL A CG2 1 
ATOM   2459 N  N   . ILE A 1 348 ? 65.860  54.513 83.451  1.00 13.77 ? 348  ILE A N   1 
ATOM   2460 C  CA  . ILE A 1 348 ? 66.048  55.304 82.241  1.00 15.70 ? 348  ILE A CA  1 
ATOM   2461 C  C   . ILE A 1 348 ? 67.323  56.104 82.426  1.00 16.92 ? 348  ILE A C   1 
ATOM   2462 O  O   . ILE A 1 348 ? 67.504  56.767 83.456  1.00 17.03 ? 348  ILE A O   1 
ATOM   2463 C  CB  . ILE A 1 348 ? 64.850  56.217 81.965  1.00 16.39 ? 348  ILE A CB  1 
ATOM   2464 C  CG1 . ILE A 1 348 ? 63.647  55.344 81.566  1.00 17.77 ? 348  ILE A CG1 1 
ATOM   2465 C  CG2 . ILE A 1 348 ? 65.183  57.204 80.842  1.00 18.60 ? 348  ILE A CG2 1 
ATOM   2466 C  CD1 . ILE A 1 348 ? 62.338  56.103 81.478  1.00 22.80 ? 348  ILE A CD1 1 
ATOM   2467 N  N   . ILE A 1 349 ? 68.216  56.019 81.443  1.00 15.55 ? 349  ILE A N   1 
ATOM   2468 C  CA  . ILE A 1 349 ? 69.422  56.837 81.402  1.00 16.43 ? 349  ILE A CA  1 
ATOM   2469 C  C   . ILE A 1 349 ? 69.296  57.772 80.215  1.00 17.45 ? 349  ILE A C   1 
ATOM   2470 O  O   . ILE A 1 349 ? 69.004  57.328 79.097  1.00 16.69 ? 349  ILE A O   1 
ATOM   2471 C  CB  . ILE A 1 349 ? 70.688  55.990 81.250  1.00 15.50 ? 349  ILE A CB  1 
ATOM   2472 C  CG1 . ILE A 1 349 ? 70.877  55.111 82.486  1.00 15.24 ? 349  ILE A CG1 1 
ATOM   2473 C  CG2 . ILE A 1 349 ? 71.896  56.922 81.029  1.00 16.98 ? 349  ILE A CG2 1 
ATOM   2474 C  CD1 . ILE A 1 349 ? 72.074  54.173 82.377  1.00 16.83 ? 349  ILE A CD1 1 
ATOM   2475 N  N   . ASP A 1 350 ? 69.482  59.069 80.453  1.00 17.44 ? 350  ASP A N   1 
ATOM   2476 C  CA  . ASP A 1 350 ? 69.494  60.068 79.391  1.00 18.62 ? 350  ASP A CA  1 
ATOM   2477 C  C   . ASP A 1 350 ? 70.944  60.380 79.030  1.00 22.58 ? 350  ASP A C   1 
ATOM   2478 O  O   . ASP A 1 350 ? 71.684  60.946 79.841  1.00 25.20 ? 350  ASP A O   1 
ATOM   2479 C  CB  . ASP A 1 350 ? 68.726  61.314 79.835  1.00 21.09 ? 350  ASP A CB  1 
ATOM   2480 C  CG  . ASP A 1 350 ? 68.518  62.311 78.714  1.00 22.00 ? 350  ASP A CG  1 
ATOM   2481 O  OD1 . ASP A 1 350 ? 69.069  62.115 77.608  1.00 21.73 ? 350  ASP A OD1 1 
ATOM   2482 O  OD2 . ASP A 1 350 ? 67.732  63.253 78.918  1.00 25.18 ? 350  ASP A OD2 1 
ATOM   2483 N  N   . PHE A 1 351 ? 71.354  59.982 77.827  1.00 18.58 ? 351  PHE A N   1 
ATOM   2484 C  CA  . PHE A 1 351 ? 72.704  60.271 77.349  1.00 19.88 ? 351  PHE A CA  1 
ATOM   2485 C  C   . PHE A 1 351 ? 72.800  61.587 76.585  1.00 22.54 ? 351  PHE A C   1 
ATOM   2486 O  O   . PHE A 1 351 ? 73.874  61.901 76.069  1.00 22.37 ? 351  PHE A O   1 
ATOM   2487 C  CB  . PHE A 1 351 ? 73.235  59.131 76.456  1.00 18.71 ? 351  PHE A CB  1 
ATOM   2488 C  CG  . PHE A 1 351 ? 73.354  57.786 77.150  1.00 18.19 ? 351  PHE A CG  1 
ATOM   2489 C  CD1 . PHE A 1 351 ? 74.379  57.538 78.052  1.00 16.69 ? 351  PHE A CD1 1 
ATOM   2490 C  CD2 . PHE A 1 351 ? 72.460  56.764 76.854  1.00 17.81 ? 351  PHE A CD2 1 
ATOM   2491 C  CE1 . PHE A 1 351 ? 74.507  56.314 78.664  1.00 16.69 ? 351  PHE A CE1 1 
ATOM   2492 C  CE2 . PHE A 1 351 ? 72.574  55.539 77.460  1.00 16.55 ? 351  PHE A CE2 1 
ATOM   2493 C  CZ  . PHE A 1 351 ? 73.604  55.315 78.384  1.00 15.53 ? 351  PHE A CZ  1 
ATOM   2494 N  N   . SER A 1 352 ? 71.707  62.353 76.469  1.00 22.00 ? 352  SER A N   1 
ATOM   2495 C  CA  . SER A 1 352 ? 71.720  63.527 75.601  1.00 21.60 ? 352  SER A CA  1 
ATOM   2496 C  C   . SER A 1 352 ? 72.668  64.612 76.101  1.00 26.18 ? 352  SER A C   1 
ATOM   2497 O  O   . SER A 1 352 ? 73.191  65.384 75.290  1.00 29.39 ? 352  SER A O   1 
ATOM   2498 C  CB  . SER A 1 352 ? 70.302  64.065 75.381  1.00 25.06 ? 352  SER A CB  1 
ATOM   2499 O  OG  . SER A 1 352 ? 69.731  64.560 76.571  1.00 27.69 ? 352  SER A OG  1 
ATOM   2500 N  N   . GLN A 1 353 ? 72.923  64.682 77.408  1.00 25.33 ? 353  GLN A N   1 
ATOM   2501 C  CA  . GLN A 1 353 ? 73.878  65.666 77.909  1.00 35.16 ? 353  GLN A CA  1 
ATOM   2502 C  C   . GLN A 1 353 ? 75.310  65.144 77.902  1.00 41.96 ? 353  GLN A C   1 
ATOM   2503 O  O   . GLN A 1 353 ? 76.215  65.831 78.387  1.00 35.63 ? 353  GLN A O   1 
ATOM   2504 C  CB  . GLN A 1 353 ? 73.498  66.151 79.313  1.00 41.32 ? 353  GLN A CB  1 
ATOM   2505 C  CG  . GLN A 1 353 ? 72.158  66.876 79.360  1.00 36.10 ? 353  GLN A CG  1 
ATOM   2506 C  CD  . GLN A 1 353 ? 72.024  67.924 78.277  1.00 43.63 ? 353  GLN A CD  1 
ATOM   2507 O  OE1 . GLN A 1 353 ? 72.700  68.957 78.302  1.00 47.99 ? 353  GLN A OE1 1 
ATOM   2508 N  NE2 . GLN A 1 353 ? 71.140  67.667 77.314  1.00 43.31 ? 353  GLN A NE2 1 
ATOM   2509 N  N   . HIS A 1 354 ? 75.531  63.954 77.353  1.00 32.65 ? 354  HIS A N   1 
ATOM   2510 C  CA  . HIS A 1 354 ? 76.823  63.287 77.417  1.00 27.72 ? 354  HIS A CA  1 
ATOM   2511 C  C   . HIS A 1 354 ? 77.349  62.973 76.022  1.00 29.91 ? 354  HIS A C   1 
ATOM   2512 O  O   . HIS A 1 354 ? 78.100  62.012 75.833  1.00 27.03 ? 354  HIS A O   1 
ATOM   2513 C  CB  . HIS A 1 354 ? 76.695  62.016 78.244  1.00 28.13 ? 354  HIS A CB  1 
ATOM   2514 C  CG  . HIS A 1 354 ? 76.290  62.264 79.662  1.00 33.52 ? 354  HIS A CG  1 
ATOM   2515 N  ND1 . HIS A 1 354 ? 76.982  63.114 80.498  1.00 37.72 ? 354  HIS A ND1 1 
ATOM   2516 C  CD2 . HIS A 1 354 ? 75.225  61.822 80.371  1.00 32.46 ? 354  HIS A CD2 1 
ATOM   2517 C  CE1 . HIS A 1 354 ? 76.389  63.143 81.678  1.00 34.03 ? 354  HIS A CE1 1 
ATOM   2518 N  NE2 . HIS A 1 354 ? 75.316  62.375 81.626  1.00 38.05 ? 354  HIS A NE2 1 
ATOM   2519 N  N   . LYS A 1 355 ? 76.948  63.763 75.034  1.00 28.36 ? 355  LYS A N   1 
ATOM   2520 C  CA  . LYS A 1 355 ? 77.357  63.505 73.664  1.00 22.96 ? 355  LYS A CA  1 
ATOM   2521 C  C   . LYS A 1 355 ? 78.871  63.493 73.559  1.00 27.51 ? 355  LYS A C   1 
ATOM   2522 O  O   . LYS A 1 355 ? 79.547  64.415 74.029  1.00 30.84 ? 355  LYS A O   1 
ATOM   2523 C  CB  . LYS A 1 355 ? 76.805  64.601 72.753  1.00 30.58 ? 355  LYS A CB  1 
ATOM   2524 C  CG  . LYS A 1 355 ? 76.650  64.185 71.318  1.00 29.50 ? 355  LYS A CG  1 
ATOM   2525 C  CD  . LYS A 1 355 ? 75.643  65.079 70.589  1.00 41.80 ? 355  LYS A CD  1 
ATOM   2526 C  CE  . LYS A 1 355 ? 76.345  66.125 69.765  1.00 47.07 ? 355  LYS A CE  1 
ATOM   2527 N  NZ  . LYS A 1 355 ? 75.518  66.555 68.603  1.00 51.55 ? 355  LYS A NZ  1 
ATOM   2528 N  N   . GLY A 1 356 ? 79.401  62.458 72.917  1.00 25.64 ? 356  GLY A N   1 
ATOM   2529 C  CA  . GLY A 1 356 ? 80.825  62.350 72.710  1.00 28.70 ? 356  GLY A CA  1 
ATOM   2530 C  C   . GLY A 1 356 ? 81.601  61.837 73.897  1.00 30.45 ? 356  GLY A C   1 
ATOM   2531 O  O   . GLY A 1 356 ? 82.836  61.841 73.856  1.00 33.86 ? 356  GLY A O   1 
ATOM   2532 N  N   . LYS A 1 357 ? 80.921  61.406 74.954  1.00 23.74 ? 357  LYS A N   1 
ATOM   2533 C  CA  . LYS A 1 357 ? 81.566  60.889 76.155  1.00 22.27 ? 357  LYS A CA  1 
ATOM   2534 C  C   . LYS A 1 357 ? 81.526  59.369 76.184  1.00 20.24 ? 357  LYS A C   1 
ATOM   2535 O  O   . LYS A 1 357 ? 80.637  58.732 75.612  1.00 22.38 ? 357  LYS A O   1 
ATOM   2536 C  CB  . LYS A 1 357 ? 80.855  61.393 77.412  1.00 25.98 ? 357  LYS A CB  1 
ATOM   2537 C  CG  . LYS A 1 357 ? 81.075  62.871 77.703  1.00 32.61 ? 357  LYS A CG  1 
ATOM   2538 C  CD  . LYS A 1 357 ? 80.083  63.346 78.747  1.00 44.45 ? 357  LYS A CD  1 
ATOM   2539 C  CE  . LYS A 1 357 ? 80.730  63.639 80.093  1.00 45.71 ? 357  LYS A CE  1 
ATOM   2540 N  NZ  . LYS A 1 357 ? 79.725  64.267 81.023  1.00 44.73 ? 357  LYS A NZ  1 
ATOM   2541 N  N   . LYS A 1 358 ? 82.487  58.795 76.901  1.00 19.54 ? 358  LYS A N   1 
ATOM   2542 C  CA  . LYS A 1 358 ? 82.442  57.407 77.330  1.00 18.59 ? 358  LYS A CA  1 
ATOM   2543 C  C   . LYS A 1 358 ? 82.277  57.427 78.840  1.00 19.44 ? 358  LYS A C   1 
ATOM   2544 O  O   . LYS A 1 358 ? 83.012  58.146 79.535  1.00 23.35 ? 358  LYS A O   1 
ATOM   2545 C  CB  . LYS A 1 358 ? 83.736  56.674 76.960  1.00 21.31 ? 358  LYS A CB  1 
ATOM   2546 C  CG  . LYS A 1 358 ? 84.061  56.726 75.461  1.00 23.21 ? 358  LYS A CG  1 
ATOM   2547 C  CD  . LYS A 1 358 ? 85.319  55.921 75.145  1.00 25.22 ? 358  LYS A CD  1 
ATOM   2548 C  CE  . LYS A 1 358 ? 85.746  56.081 73.696  1.00 30.36 ? 358  LYS A CE  1 
ATOM   2549 N  NZ  . LYS A 1 358 ? 86.986  55.299 73.427  1.00 33.80 ? 358  LYS A NZ  1 
ATOM   2550 N  N   . LEU A 1 359 ? 81.280  56.695 79.327  1.00 17.36 ? 359  LEU A N   1 
ATOM   2551 C  CA  . LEU A 1 359 ? 80.930  56.644 80.742  1.00 17.57 ? 359  LEU A CA  1 
ATOM   2552 C  C   . LEU A 1 359 ? 81.063  55.216 81.232  1.00 16.80 ? 359  LEU A C   1 
ATOM   2553 O  O   . LEU A 1 359 ? 80.423  54.310 80.692  1.00 15.85 ? 359  LEU A O   1 
ATOM   2554 C  CB  . LEU A 1 359 ? 79.500  57.134 80.988  1.00 18.72 ? 359  LEU A CB  1 
ATOM   2555 C  CG  . LEU A 1 359 ? 79.086  58.451 80.334  1.00 23.09 ? 359  LEU A CG  1 
ATOM   2556 C  CD1 . LEU A 1 359 ? 77.568  58.560 80.397  1.00 26.64 ? 359  LEU A CD1 1 
ATOM   2557 C  CD2 . LEU A 1 359 ? 79.730  59.617 81.039  1.00 30.36 ? 359  LEU A CD2 1 
ATOM   2558 N  N   . ILE A 1 360 ? 81.868  55.012 82.266  1.00 16.93 ? 360  ILE A N   1 
ATOM   2559 C  CA  . ILE A 1 360 ? 81.978  53.685 82.860  1.00 17.28 ? 360  ILE A CA  1 
ATOM   2560 C  C   . ILE A 1 360 ? 80.844  53.461 83.849  1.00 15.32 ? 360  ILE A C   1 
ATOM   2561 O  O   . ILE A 1 360 ? 80.553  54.325 84.689  1.00 17.45 ? 360  ILE A O   1 
ATOM   2562 C  CB  . ILE A 1 360 ? 83.358  53.490 83.506  1.00 18.65 ? 360  ILE A CB  1 
ATOM   2563 C  CG1 . ILE A 1 360 ? 84.447  53.516 82.412  1.00 21.10 ? 360  ILE A CG1 1 
ATOM   2564 C  CG2 . ILE A 1 360 ? 83.387  52.174 84.272  1.00 18.32 ? 360  ILE A CG2 1 
ATOM   2565 C  CD1 . ILE A 1 360 ? 85.819  53.187 82.910  1.00 38.50 ? 360  ILE A CD1 1 
ATOM   2566 N  N   . LEU A 1 361 ? 80.167  52.322 83.711  1.00 15.43 ? 361  LEU A N   1 
ATOM   2567 C  CA  . LEU A 1 361 ? 79.241  51.814 84.712  1.00 15.40 ? 361  LEU A CA  1 
ATOM   2568 C  C   . LEU A 1 361 ? 80.096  51.034 85.701  1.00 16.04 ? 361  LEU A C   1 
ATOM   2569 O  O   . LEU A 1 361 ? 80.608  49.937 85.377  1.00 15.60 ? 361  LEU A O   1 
ATOM   2570 C  CB  . LEU A 1 361 ? 78.180  50.917 84.078  1.00 14.65 ? 361  LEU A CB  1 
ATOM   2571 C  CG  . LEU A 1 361 ? 77.081  50.449 85.040  1.00 14.44 ? 361  LEU A CG  1 
ATOM   2572 C  CD1 . LEU A 1 361 ? 76.175  51.628 85.438  1.00 16.60 ? 361  LEU A CD1 1 
ATOM   2573 C  CD2 . LEU A 1 361 ? 76.273  49.348 84.375  1.00 17.15 ? 361  LEU A CD2 1 
ATOM   2574 N  N   . GLN A 1 362 ? 80.262  51.627 86.885  1.00 15.19 ? 362  GLN A N   1 
ATOM   2575 C  CA  . GLN A 1 362 ? 81.081  51.100 87.962  1.00 15.49 ? 362  GLN A CA  1 
ATOM   2576 C  C   . GLN A 1 362 ? 80.263  50.170 88.845  1.00 16.34 ? 362  GLN A C   1 
ATOM   2577 O  O   . GLN A 1 362 ? 79.034  50.282 88.954  1.00 16.37 ? 362  GLN A O   1 
ATOM   2578 C  CB  . GLN A 1 362 ? 81.549  52.244 88.859  1.00 18.20 ? 362  GLN A CB  1 
ATOM   2579 C  CG  . GLN A 1 362 ? 82.345  53.329 88.176  1.00 19.51 ? 362  GLN A CG  1 
ATOM   2580 C  CD  . GLN A 1 362 ? 81.777  54.685 88.479  1.00 27.38 ? 362  GLN A CD  1 
ATOM   2581 O  OE1 . GLN A 1 362 ? 81.984  55.236 89.555  1.00 27.75 ? 362  GLN A OE1 1 
ATOM   2582 N  NE2 . GLN A 1 362 ? 81.061  55.241 87.523  1.00 24.32 ? 362  GLN A NE2 1 
ATOM   2583 N  N   . ASN A 1 363 ? 80.983  49.267 89.490  1.00 15.13 ? 363  ASN A N   1 
ATOM   2584 C  CA  . ASN A 1 363 ? 80.540  48.544 90.683  1.00 17.64 ? 363  ASN A CA  1 
ATOM   2585 C  C   . ASN A 1 363 ? 81.345  49.086 91.862  1.00 18.15 ? 363  ASN A C   1 
ATOM   2586 O  O   . ASN A 1 363 ? 82.510  48.717 92.057  1.00 17.70 ? 363  ASN A O   1 
ATOM   2587 C  CB  . ASN A 1 363 ? 80.793  47.050 90.533  1.00 15.62 ? 363  ASN A CB  1 
ATOM   2588 C  CG  . ASN A 1 363 ? 80.718  46.335 91.865  1.00 15.94 ? 363  ASN A CG  1 
ATOM   2589 O  OD1 . ASN A 1 363 ? 79.918  46.714 92.712  1.00 16.61 ? 363  ASN A OD1 1 
ATOM   2590 N  ND2 . ASN A 1 363 ? 81.526  45.282 92.043  1.00 16.28 ? 363  ASN A ND2 1 
ATOM   2591 N  N   . THR A 1 364 ? 80.721  49.937 92.673  1.00 17.54 ? 364  THR A N   1 
ATOM   2592 C  CA  . THR A 1 364 ? 81.476  50.578 93.746  1.00 19.05 ? 364  THR A CA  1 
ATOM   2593 C  C   . THR A 1 364 ? 81.756  49.651 94.925  1.00 16.91 ? 364  THR A C   1 
ATOM   2594 O  O   . THR A 1 364 ? 82.472  50.062 95.846  1.00 21.02 ? 364  THR A O   1 
ATOM   2595 C  CB  . THR A 1 364 ? 80.799  51.864 94.239  1.00 19.16 ? 364  THR A CB  1 
ATOM   2596 O  OG1 . THR A 1 364 ? 79.517  51.545 94.789  1.00 21.45 ? 364  THR A OG1 1 
ATOM   2597 C  CG2 . THR A 1 364 ? 80.618  52.839 93.067  1.00 19.84 ? 364  THR A CG2 1 
ATOM   2598 N  N   . ASN A 1 365 ? 81.242  48.415 94.903  1.00 17.74 ? 365  ASN A N   1 
ATOM   2599 C  CA  . ASN A 1 365 ? 81.527  47.472 95.987  1.00 18.40 ? 365  ASN A CA  1 
ATOM   2600 C  C   . ASN A 1 365 ? 82.954  46.935 95.959  1.00 27.29 ? 365  ASN A C   1 
ATOM   2601 O  O   . ASN A 1 365 ? 83.397  46.354 96.955  1.00 24.17 ? 365  ASN A O   1 
ATOM   2602 C  CB  . ASN A 1 365 ? 80.624  46.258 95.857  1.00 18.60 ? 365  ASN A CB  1 
ATOM   2603 C  CG  . ASN A 1 365 ? 79.213  46.540 96.261  1.00 18.46 ? 365  ASN A CG  1 
ATOM   2604 O  OD1 . ASN A 1 365 ? 78.885  47.643 96.690  1.00 20.90 ? 365  ASN A OD1 1 
ATOM   2605 N  ND2 . ASN A 1 365 ? 78.350  45.558 96.094  1.00 18.88 ? 365  ASN A ND2 1 
ATOM   2606 N  N   . ALA A 1 366 ? 83.672  47.083 94.850  1.00 20.48 ? 366  ALA A N   1 
ATOM   2607 C  CA  . ALA A 1 366 ? 84.965  46.443 94.683  1.00 19.45 ? 366  ALA A CA  1 
ATOM   2608 C  C   . ALA A 1 366 ? 85.945  47.417 94.055  1.00 22.58 ? 366  ALA A C   1 
ATOM   2609 O  O   . ALA A 1 366 ? 85.560  48.357 93.349  1.00 22.87 ? 366  ALA A O   1 
ATOM   2610 C  CB  . ALA A 1 366 ? 84.854  45.181 93.800  1.00 19.39 ? 366  ALA A CB  1 
ATOM   2611 N  N   . GLU A 1 367 ? 87.221  47.171 94.319  1.00 23.13 ? 367  GLU A N   1 
ATOM   2612 C  CA  . GLU A 1 367 ? 88.312  47.893 93.688  1.00 22.83 ? 367  GLU A CA  1 
ATOM   2613 C  C   . GLU A 1 367 ? 88.818  47.127 92.477  1.00 24.27 ? 367  GLU A C   1 
ATOM   2614 O  O   . GLU A 1 367 ? 88.495  45.955 92.261  1.00 24.03 ? 367  GLU A O   1 
ATOM   2615 C  CB  . GLU A 1 367 ? 89.470  48.114 94.667  1.00 34.37 ? 367  GLU A CB  1 
ATOM   2616 C  CG  . GLU A 1 367 ? 89.042  48.277 96.108  1.00 42.01 ? 367  GLU A CG  1 
ATOM   2617 C  CD  . GLU A 1 367 ? 88.404  49.628 96.332  1.00 45.92 ? 367  GLU A CD  1 
ATOM   2618 O  OE1 . GLU A 1 367 ? 89.037  50.645 95.962  1.00 54.22 ? 367  GLU A OE1 1 
ATOM   2619 O  OE2 . GLU A 1 367 ? 87.259  49.681 96.837  1.00 55.01 ? 367  GLU A OE2 1 
ATOM   2620 N  N   . GLY A 1 368 ? 89.661  47.808 91.699  1.00 24.29 ? 368  GLY A N   1 
ATOM   2621 C  CA  . GLY A 1 368 ? 90.282  47.155 90.569  1.00 22.68 ? 368  GLY A CA  1 
ATOM   2622 C  C   . GLY A 1 368 ? 89.284  46.795 89.480  1.00 17.60 ? 368  GLY A C   1 
ATOM   2623 O  O   . GLY A 1 368 ? 88.253  47.449 89.280  1.00 19.92 ? 368  GLY A O   1 
ATOM   2624 N  N   . ASN A 1 369 ? 89.623  45.731 88.747  1.00 19.77 ? 369  ASN A N   1 
ATOM   2625 C  CA  . ASN A 1 369 ? 88.823  45.368 87.583  1.00 19.46 ? 369  ASN A CA  1 
ATOM   2626 C  C   . ASN A 1 369 ? 87.401  44.964 87.956  1.00 15.80 ? 369  ASN A C   1 
ATOM   2627 O  O   . ASN A 1 369 ? 86.477  45.165 87.174  1.00 15.58 ? 369  ASN A O   1 
ATOM   2628 C  CB  . ASN A 1 369 ? 89.542  44.292 86.772  1.00 19.45 ? 369  ASN A CB  1 
ATOM   2629 C  CG  . ASN A 1 369 ? 90.718  44.867 85.989  1.00 21.05 ? 369  ASN A CG  1 
ATOM   2630 O  OD1 . ASN A 1 369 ? 90.588  45.941 85.398  1.00 26.02 ? 369  ASN A OD1 1 
ATOM   2631 N  ND2 . ASN A 1 369 ? 91.819  44.143 85.935  1.00 23.76 ? 369  ASN A ND2 1 
ATOM   2632 N  N   . MET A 1 370 ? 87.202  44.399 89.146  1.00 15.72 ? 370  MET A N   1 
ATOM   2633 C  CA  . MET A 1 370 ? 85.855  44.048 89.585  1.00 14.50 ? 370  MET A CA  1 
ATOM   2634 C  C   . MET A 1 370 ? 85.025  45.261 89.974  1.00 16.72 ? 370  MET A C   1 
ATOM   2635 O  O   . MET A 1 370 ? 83.831  45.110 90.259  1.00 16.99 ? 370  MET A O   1 
ATOM   2636 C  CB  . MET A 1 370 ? 85.912  43.029 90.728  1.00 16.18 ? 370  MET A CB  1 
ATOM   2637 C  CG  . MET A 1 370 ? 86.536  41.684 90.314  1.00 16.07 ? 370  MET A CG  1 
ATOM   2638 S  SD  . MET A 1 370 ? 85.634  40.798 89.033  1.00 16.87 ? 370  MET A SD  1 
ATOM   2639 C  CE  . MET A 1 370 ? 84.152  40.323 89.947  1.00 17.31 ? 370  MET A CE  1 
ATOM   2640 N  N   . GLY A 1 371 ? 85.621  46.445 90.002  1.00 15.48 ? 371  GLY A N   1 
ATOM   2641 C  CA  . GLY A 1 371 ? 84.895  47.688 90.113  1.00 15.93 ? 371  GLY A CA  1 
ATOM   2642 C  C   . GLY A 1 371 ? 84.348  48.206 88.805  1.00 15.30 ? 371  GLY A C   1 
ATOM   2643 O  O   . GLY A 1 371 ? 83.770  49.292 88.779  1.00 15.74 ? 371  GLY A O   1 
ATOM   2644 N  N   . ILE A 1 372 ? 84.513  47.464 87.713  1.00 14.44 ? 372  ILE A N   1 
ATOM   2645 C  CA  . ILE A 1 372 ? 84.067  47.888 86.386  1.00 15.61 ? 372  ILE A CA  1 
ATOM   2646 C  C   . ILE A 1 372 ? 83.043  46.889 85.876  1.00 14.92 ? 372  ILE A C   1 
ATOM   2647 O  O   . ILE A 1 372 ? 83.309  45.688 85.870  1.00 14.40 ? 372  ILE A O   1 
ATOM   2648 C  CB  . ILE A 1 372 ? 85.250  47.982 85.407  1.00 15.02 ? 372  ILE A CB  1 
ATOM   2649 C  CG1 . ILE A 1 372 ? 86.244  49.034 85.898  1.00 17.61 ? 372  ILE A CG1 1 
ATOM   2650 C  CG2 . ILE A 1 372 ? 84.770  48.306 83.968  1.00 16.64 ? 372  ILE A CG2 1 
ATOM   2651 C  CD1 . ILE A 1 372 ? 87.584  48.989 85.213  1.00 19.24 ? 372  ILE A CD1 1 
ATOM   2652 N  N   . ILE A 1 373 ? 81.892  47.378 85.418  1.00 14.21 ? 373  ILE A N   1 
ATOM   2653 C  CA  . ILE A 1 373 ? 80.897  46.513 84.792  1.00 14.18 ? 373  ILE A CA  1 
ATOM   2654 C  C   . ILE A 1 373 ? 80.952  46.658 83.278  1.00 13.95 ? 373  ILE A C   1 
ATOM   2655 O  O   . ILE A 1 373 ? 81.148  45.668 82.557  1.00 13.61 ? 373  ILE A O   1 
ATOM   2656 C  CB  . ILE A 1 373 ? 79.476  46.778 85.329  1.00 13.51 ? 373  ILE A CB  1 
ATOM   2657 C  CG1 . ILE A 1 373 ? 79.444  46.518 86.851  1.00 14.99 ? 373  ILE A CG1 1 
ATOM   2658 C  CG2 . ILE A 1 373 ? 78.433  45.946 84.572  1.00 14.57 ? 373  ILE A CG2 1 
ATOM   2659 C  CD1 . ILE A 1 373 ? 78.188  47.016 87.533  1.00 17.30 ? 373  ILE A CD1 1 
ATOM   2660 N  N   . MET A 1 374 ? 80.751  47.880 82.778  1.00 13.41 ? 374  MET A N   1 
ATOM   2661 C  CA  . MET A 1 374 ? 80.748  48.063 81.317  1.00 13.60 ? 374  MET A CA  1 
ATOM   2662 C  C   . MET A 1 374 ? 80.951  49.542 81.023  1.00 14.02 ? 374  MET A C   1 
ATOM   2663 O  O   . MET A 1 374 ? 81.054  50.362 81.932  1.00 14.83 ? 374  MET A O   1 
ATOM   2664 C  CB  . MET A 1 374 ? 79.444  47.537 80.705  1.00 14.24 ? 374  MET A CB  1 
ATOM   2665 C  CG  . MET A 1 374 ? 78.194  48.366 81.086  1.00 16.15 ? 374  MET A CG  1 
ATOM   2666 S  SD  . MET A 1 374 ? 76.645  47.708 80.425  1.00 15.26 ? 374  MET A SD  1 
ATOM   2667 C  CE  . MET A 1 374 ? 76.736  48.270 78.733  1.00 15.96 ? 374  MET A CE  1 
ATOM   2668 N  N   . ARG A 1 375 ? 81.007  49.885 79.743  1.00 13.90 ? 375  ARG A N   1 
ATOM   2669 C  CA  . ARG A 1 375 ? 81.180  51.265 79.325  1.00 14.38 ? 375  ARG A CA  1 
ATOM   2670 C  C   . ARG A 1 375 ? 80.113  51.642 78.305  1.00 15.77 ? 375  ARG A C   1 
ATOM   2671 O  O   . ARG A 1 375 ? 79.837  50.877 77.384  1.00 16.38 ? 375  ARG A O   1 
ATOM   2672 C  CB  . ARG A 1 375 ? 82.572  51.426 78.680  1.00 14.71 ? 375  ARG A CB  1 
ATOM   2673 C  CG  . ARG A 1 375 ? 83.050  52.881 78.551  1.00 15.05 ? 375  ARG A CG  1 
ATOM   2674 C  CD  . ARG A 1 375 ? 84.442  52.941 77.897  1.00 16.42 ? 375  ARG A CD  1 
ATOM   2675 N  NE  . ARG A 1 375 ? 84.359  52.575 76.486  1.00 18.57 ? 375  ARG A NE  1 
ATOM   2676 C  CZ  . ARG A 1 375 ? 85.398  52.282 75.714  1.00 18.20 ? 375  ARG A CZ  1 
ATOM   2677 N  NH1 . ARG A 1 375 ? 86.642  52.282 76.193  1.00 19.10 ? 375  ARG A NH1 1 
ATOM   2678 N  NH2 . ARG A 1 375 ? 85.185  51.982 74.431  1.00 19.68 ? 375  ARG A NH2 1 
ATOM   2679 N  N   . PHE A 1 376 ? 79.541  52.839 78.440  1.00 14.56 ? 376  PHE A N   1 
ATOM   2680 C  CA  . PHE A 1 376 ? 78.613  53.386 77.461  1.00 14.91 ? 376  PHE A CA  1 
ATOM   2681 C  C   . PHE A 1 376 ? 79.349  54.422 76.628  1.00 16.66 ? 376  PHE A C   1 
ATOM   2682 O  O   . PHE A 1 376 ? 79.918  55.374 77.175  1.00 17.50 ? 376  PHE A O   1 
ATOM   2683 C  CB  . PHE A 1 376 ? 77.433  54.062 78.165  1.00 16.26 ? 376  PHE A CB  1 
ATOM   2684 C  CG  . PHE A 1 376 ? 76.596  53.136 78.982  1.00 14.98 ? 376  PHE A CG  1 
ATOM   2685 C  CD1 . PHE A 1 376 ? 75.690  52.296 78.368  1.00 14.04 ? 376  PHE A CD1 1 
ATOM   2686 C  CD2 . PHE A 1 376 ? 76.683  53.139 80.366  1.00 14.23 ? 376  PHE A CD2 1 
ATOM   2687 C  CE1 . PHE A 1 376 ? 74.885  51.428 79.115  1.00 14.99 ? 376  PHE A CE1 1 
ATOM   2688 C  CE2 . PHE A 1 376 ? 75.873  52.295 81.130  1.00 15.90 ? 376  PHE A CE2 1 
ATOM   2689 C  CZ  . PHE A 1 376 ? 74.976  51.423 80.498  1.00 15.47 ? 376  PHE A CZ  1 
ATOM   2690 N  N   . ASP A 1 377 ? 79.342  54.246 75.315  1.00 16.07 ? 377  ASP A N   1 
ATOM   2691 C  CA  . ASP A 1 377 ? 80.038  55.154 74.405  1.00 18.02 ? 377  ASP A CA  1 
ATOM   2692 C  C   . ASP A 1 377 ? 78.991  55.987 73.680  1.00 18.01 ? 377  ASP A C   1 
ATOM   2693 O  O   . ASP A 1 377 ? 78.308  55.477 72.782  1.00 18.95 ? 377  ASP A O   1 
ATOM   2694 C  CB  . ASP A 1 377 ? 80.886  54.395 73.385  1.00 20.00 ? 377  ASP A CB  1 
ATOM   2695 C  CG  . ASP A 1 377 ? 81.976  53.553 74.012  1.00 20.54 ? 377  ASP A CG  1 
ATOM   2696 O  OD1 . ASP A 1 377 ? 82.221  53.663 75.235  1.00 20.59 ? 377  ASP A OD1 1 
ATOM   2697 O  OD2 . ASP A 1 377 ? 82.653  52.842 73.233  1.00 21.45 ? 377  ASP A OD2 1 
ATOM   2698 N  N   . VAL A 1 378 ? 78.878  57.272 74.033  1.00 17.99 ? 378  VAL A N   1 
ATOM   2699 C  CA  . VAL A 1 378 ? 77.819  58.089 73.447  1.00 19.65 ? 378  VAL A CA  1 
ATOM   2700 C  C   . VAL A 1 378 ? 78.345  58.667 72.144  1.00 19.82 ? 378  VAL A C   1 
ATOM   2701 O  O   . VAL A 1 378 ? 78.587  59.879 72.017  1.00 22.26 ? 378  VAL A O   1 
ATOM   2702 C  CB  . VAL A 1 378 ? 77.332  59.180 74.420  1.00 20.06 ? 378  VAL A CB  1 
ATOM   2703 C  CG1 . VAL A 1 378 ? 76.020  59.835 73.903  1.00 19.23 ? 378  VAL A CG1 1 
ATOM   2704 C  CG2 . VAL A 1 378 ? 77.157  58.607 75.830  1.00 18.69 ? 378  VAL A CG2 1 
ATOM   2705 N  N   . LEU A 1 379 ? 78.400  57.812 71.130  1.00 19.89 ? 379  LEU A N   1 
ATOM   2706 C  CA  . LEU A 1 379 ? 79.169  58.103 69.925  1.00 21.13 ? 379  LEU A CA  1 
ATOM   2707 C  C   . LEU A 1 379 ? 78.378  57.820 68.668  1.00 23.52 ? 379  LEU A C   1 
ATOM   2708 O  O   . LEU A 1 379 ? 78.884  58.079 67.569  1.00 26.38 ? 379  LEU A O   1 
ATOM   2709 C  CB  . LEU A 1 379 ? 80.458  57.266 69.895  1.00 23.81 ? 379  LEU A CB  1 
ATOM   2710 C  CG  . LEU A 1 379 ? 81.437  57.462 71.066  1.00 26.03 ? 379  LEU A CG  1 
ATOM   2711 C  CD1 . LEU A 1 379 ? 82.694  56.623 70.876  1.00 28.28 ? 379  LEU A CD1 1 
ATOM   2712 C  CD2 . LEU A 1 379 ? 81.815  58.924 71.227  1.00 32.75 ? 379  LEU A CD2 1 
ATOM   2713 N  N   . GLN A 1 380 ? 77.182  57.265 68.794  1.00 22.83 ? 380  GLN A N   1 
ATOM   2714 C  CA  . GLN A 1 380 ? 76.340  57.019 67.644  1.00 26.75 ? 380  GLN A CA  1 
ATOM   2715 C  C   . GLN A 1 380 ? 75.571  58.295 67.323  1.00 29.94 ? 380  GLN A C   1 
ATOM   2716 O  O   . GLN A 1 380 ? 74.973  58.891 68.224  1.00 26.41 ? 380  GLN A O   1 
ATOM   2717 C  CB  . GLN A 1 380 ? 75.353  55.904 67.976  1.00 25.22 ? 380  GLN A CB  1 
ATOM   2718 C  CG  . GLN A 1 380 ? 74.500  55.544 66.802  1.00 30.20 ? 380  GLN A CG  1 
ATOM   2719 C  CD  . GLN A 1 380 ? 75.319  54.864 65.724  1.00 37.94 ? 380  GLN A CD  1 
ATOM   2720 O  OE1 . GLN A 1 380 ? 76.310  54.188 66.022  1.00 45.29 ? 380  GLN A OE1 1 
ATOM   2721 N  NE2 . GLN A 1 380 ? 74.934  55.058 64.474  1.00 43.58 ? 380  GLN A NE2 1 
ATOM   2722 N  N   . PRO A 1 381 ? 75.603  58.777 66.085  1.00 27.98 ? 381  PRO A N   1 
ATOM   2723 C  CA  . PRO A 1 381 ? 74.762  59.929 65.743  1.00 26.15 ? 381  PRO A CA  1 
ATOM   2724 C  C   . PRO A 1 381 ? 73.292  59.631 66.000  1.00 32.23 ? 381  PRO A C   1 
ATOM   2725 O  O   . PRO A 1 381 ? 72.810  58.516 65.785  1.00 27.67 ? 381  PRO A O   1 
ATOM   2726 C  CB  . PRO A 1 381 ? 75.038  60.156 64.253  1.00 28.18 ? 381  PRO A CB  1 
ATOM   2727 C  CG  . PRO A 1 381 ? 76.250  59.312 63.917  1.00 35.61 ? 381  PRO A CG  1 
ATOM   2728 C  CD  . PRO A 1 381 ? 76.702  58.573 65.130  1.00 29.69 ? 381  PRO A CD  1 
ATOM   2729 N  N   . LEU A 1 382 ? 72.589  60.642 66.494  1.00 26.76 ? 382  LEU A N   1 
ATOM   2730 C  CA  . LEU A 1 382 ? 71.165  60.513 66.754  1.00 27.46 ? 382  LEU A CA  1 
ATOM   2731 C  C   . LEU A 1 382 ? 70.420  60.114 65.483  1.00 33.14 ? 382  LEU A C   1 
ATOM   2732 O  O   . LEU A 1 382 ? 70.559  60.755 64.431  1.00 31.37 ? 382  LEU A O   1 
ATOM   2733 C  CB  . LEU A 1 382 ? 70.644  61.850 67.270  1.00 30.80 ? 382  LEU A CB  1 
ATOM   2734 C  CG  . LEU A 1 382 ? 69.268  61.954 67.912  1.00 29.85 ? 382  LEU A CG  1 
ATOM   2735 C  CD1 . LEU A 1 382 ? 69.144  61.021 69.107  1.00 27.54 ? 382  LEU A CD1 1 
ATOM   2736 C  CD2 . LEU A 1 382 ? 68.998  63.398 68.300  1.00 31.98 ? 382  LEU A CD2 1 
ATOM   2737 N  N   . ARG A 1 383 ? 69.628  59.049 65.593  1.00 28.77 ? 383  ARG A N   1 
ATOM   2738 C  CA  . ARG A 1 383 ? 68.788  58.546 64.505  1.00 34.02 ? 383  ARG A CA  1 
ATOM   2739 C  C   . ARG A 1 383 ? 67.373  59.098 64.673  1.00 33.48 ? 383  ARG A C   1 
ATOM   2740 O  O   . ARG A 1 383 ? 66.435  58.388 65.032  1.00 50.57 ? 383  ARG A O   1 
ATOM   2741 C  CB  . ARG A 1 383 ? 68.747  57.019 64.545  1.00 37.15 ? 383  ARG A CB  1 
ATOM   2742 C  CG  . ARG A 1 383 ? 69.962  56.268 64.047  1.00 40.77 ? 383  ARG A CG  1 
ATOM   2743 C  CD  . ARG A 1 383 ? 69.933  54.855 64.614  1.00 39.01 ? 383  ARG A CD  1 
ATOM   2744 N  NE  . ARG A 1 383 ? 71.265  54.321 64.872  1.00 44.77 ? 383  ARG A NE  1 
ATOM   2745 C  CZ  . ARG A 1 383 ? 71.578  53.508 65.875  1.00 45.69 ? 383  ARG A CZ  1 
ATOM   2746 N  NH1 . ARG A 1 383 ? 70.712  53.223 66.834  1.00 50.35 ? 383  ARG A NH1 1 
ATOM   2747 N  NH2 . ARG A 1 383 ? 72.798  52.979 65.925  1.00 47.88 ? 383  ARG A NH2 1 
ATOM   2748 N  N   . GLY A 1 384 ? 67.224  60.389 64.426  1.00 41.54 ? 384  GLY A N   1 
ATOM   2749 C  CA  . GLY A 1 384 ? 65.932  61.022 64.556  1.00 38.91 ? 384  GLY A CA  1 
ATOM   2750 C  C   . GLY A 1 384 ? 65.550  61.294 66.001  1.00 36.01 ? 384  GLY A C   1 
ATOM   2751 O  O   . GLY A 1 384 ? 66.119  60.757 66.960  1.00 36.18 ? 384  GLY A O   1 
ATOM   2752 N  N   . ARG A 1 385 ? 64.528  62.131 66.143  1.00 34.58 ? 385  ARG A N   1 
ATOM   2753 C  CA  . ARG A 1 385 ? 64.254  62.789 67.410  1.00 31.04 ? 385  ARG A CA  1 
ATOM   2754 C  C   . ARG A 1 385 ? 63.845  61.790 68.479  1.00 29.09 ? 385  ARG A C   1 
ATOM   2755 O  O   . ARG A 1 385 ? 63.101  60.841 68.220  1.00 32.88 ? 385  ARG A O   1 
ATOM   2756 C  CB  . ARG A 1 385 ? 63.167  63.854 67.229  1.00 32.96 ? 385  ARG A CB  1 
ATOM   2757 C  CG  . ARG A 1 385 ? 63.148  64.901 68.346  1.00 42.13 ? 385  ARG A CG  1 
ATOM   2758 C  CD  . ARG A 1 385 ? 61.985  65.905 68.224  1.00 44.23 ? 385  ARG A CD  1 
ATOM   2759 N  NE  . ARG A 1 385 ? 60.696  65.317 68.576  1.00 48.19 ? 385  ARG A NE  1 
ATOM   2760 C  CZ  . ARG A 1 385 ? 60.257  65.142 69.819  1.00 48.94 ? 385  ARG A CZ  1 
ATOM   2761 N  NH1 . ARG A 1 385 ? 60.997  65.467 70.870  1.00 48.69 ? 385  ARG A NH1 1 
ATOM   2762 N  NH2 . ARG A 1 385 ? 59.057  64.598 70.015  1.00 54.08 ? 385  ARG A NH2 1 
ATOM   2763 N  N   . ASP A 1 386 ? 64.380  61.989 69.681  1.00 25.86 ? 386  ASP A N   1 
ATOM   2764 C  CA  . ASP A 1 386 ? 63.956  61.234 70.850  1.00 23.80 ? 386  ASP A CA  1 
ATOM   2765 C  C   . ASP A 1 386 ? 62.559  61.691 71.249  1.00 24.12 ? 386  ASP A C   1 
ATOM   2766 O  O   . ASP A 1 386 ? 62.385  62.789 71.786  1.00 30.05 ? 386  ASP A O   1 
ATOM   2767 C  CB  . ASP A 1 386 ? 64.921  61.507 71.995  1.00 22.58 ? 386  ASP A CB  1 
ATOM   2768 C  CG  . ASP A 1 386 ? 64.673  60.600 73.175  1.00 22.61 ? 386  ASP A CG  1 
ATOM   2769 O  OD1 . ASP A 1 386 ? 63.682  59.838 73.129  1.00 23.45 ? 386  ASP A OD1 1 
ATOM   2770 O  OD2 . ASP A 1 386 ? 65.383  60.746 74.190  1.00 21.78 ? 386  ASP A OD2 1 
ATOM   2771 N  N   . THR A 1 387 ? 61.564  60.852 71.000  1.00 28.13 ? 387  THR A N   1 
ATOM   2772 C  CA  . THR A 1 387 ? 60.197  61.161 71.395  1.00 27.05 ? 387  THR A CA  1 
ATOM   2773 C  C   . THR A 1 387 ? 59.823  60.522 72.722  1.00 26.15 ? 387  THR A C   1 
ATOM   2774 O  O   . THR A 1 387 ? 58.678  60.668 73.167  1.00 27.31 ? 387  THR A O   1 
ATOM   2775 C  CB  . THR A 1 387 ? 59.210  60.721 70.305  1.00 27.08 ? 387  THR A CB  1 
ATOM   2776 O  OG1 . THR A 1 387 ? 59.352  59.312 70.074  1.00 38.38 ? 387  THR A OG1 1 
ATOM   2777 C  CG2 . THR A 1 387 ? 59.492  61.470 69.009  1.00 32.55 ? 387  THR A CG2 1 
ATOM   2778 N  N   . SER A 1 388 ? 60.758  59.820 73.356  1.00 23.13 ? 388  SER A N   1 
ATOM   2779 C  CA  . SER A 1 388 ? 60.487  59.212 74.642  1.00 21.43 ? 388  SER A CA  1 
ATOM   2780 C  C   . SER A 1 388 ? 60.461  60.271 75.741  1.00 24.81 ? 388  SER A C   1 
ATOM   2781 O  O   . SER A 1 388 ? 61.012  61.371 75.606  1.00 23.60 ? 388  SER A O   1 
ATOM   2782 C  CB  . SER A 1 388 ? 61.511  58.117 74.947  1.00 21.80 ? 388  SER A CB  1 
ATOM   2783 O  OG  . SER A 1 388 ? 62.762  58.659 75.311  1.00 21.76 ? 388  SER A OG  1 
ATOM   2784 N  N   . GLU A 1 389 ? 59.789  59.931 76.841  1.00 23.16 ? 389  GLU A N   1 
ATOM   2785 C  CA  . GLU A 1 389 ? 59.666  60.832 77.975  1.00 23.86 ? 389  GLU A CA  1 
ATOM   2786 C  C   . GLU A 1 389 ? 59.837  60.062 79.268  1.00 24.76 ? 389  GLU A C   1 
ATOM   2787 O  O   . GLU A 1 389 ? 59.485  58.883 79.360  1.00 29.54 ? 389  GLU A O   1 
ATOM   2788 C  CB  . GLU A 1 389 ? 58.301  61.552 78.020  1.00 24.87 ? 389  GLU A CB  1 
ATOM   2789 C  CG  . GLU A 1 389 ? 58.016  62.426 76.802  1.00 29.19 ? 389  GLU A CG  1 
ATOM   2790 C  CD  . GLU A 1 389 ? 56.560  62.916 76.720  1.00 44.97 ? 389  GLU A CD  1 
ATOM   2791 O  OE1 . GLU A 1 389 ? 55.781  62.703 77.685  1.00 45.62 ? 389  GLU A OE1 1 
ATOM   2792 O  OE2 . GLU A 1 389 ? 56.206  63.548 75.691  1.00 49.82 ? 389  GLU A OE2 1 
ATOM   2793 N  N   . ILE A 1 390 ? 60.414  60.734 80.258  1.00 22.84 ? 390  ILE A N   1 
ATOM   2794 C  CA  . ILE A 1 390 ? 60.361  60.256 81.632  1.00 21.78 ? 390  ILE A CA  1 
ATOM   2795 C  C   . ILE A 1 390 ? 59.055  60.788 82.206  1.00 23.33 ? 390  ILE A C   1 
ATOM   2796 O  O   . ILE A 1 390 ? 58.917  62.000 82.406  1.00 25.66 ? 390  ILE A O   1 
ATOM   2797 C  CB  . ILE A 1 390 ? 61.583  60.691 82.457  1.00 23.28 ? 390  ILE A CB  1 
ATOM   2798 C  CG1 . ILE A 1 390 ? 62.874  60.102 81.875  1.00 24.78 ? 390  ILE A CG1 1 
ATOM   2799 C  CG2 . ILE A 1 390 ? 61.428  60.252 83.902  1.00 26.26 ? 390  ILE A CG2 1 
ATOM   2800 C  CD1 . ILE A 1 390 ? 64.091  60.969 82.125  1.00 31.47 ? 390  ILE A CD1 1 
ATOM   2801 N  N   . PRO A 1 391 ? 58.077  59.934 82.481  1.00 20.51 ? 391  PRO A N   1 
ATOM   2802 C  CA  . PRO A 1 391 ? 56.739  60.432 82.815  1.00 24.88 ? 391  PRO A CA  1 
ATOM   2803 C  C   . PRO A 1 391 ? 56.660  60.927 84.250  1.00 22.88 ? 391  PRO A C   1 
ATOM   2804 O  O   . PRO A 1 391 ? 57.473  60.582 85.108  1.00 24.52 ? 391  PRO A O   1 
ATOM   2805 C  CB  . PRO A 1 391 ? 55.838  59.213 82.614  1.00 27.14 ? 391  PRO A CB  1 
ATOM   2806 C  CG  . PRO A 1 391 ? 56.733  58.025 82.757  1.00 27.17 ? 391  PRO A CG  1 
ATOM   2807 C  CD  . PRO A 1 391 ? 58.165  58.463 82.476  1.00 20.08 ? 391  PRO A CD  1 
ATOM   2808 N  N   . ALA A 1 392 ? 55.629  61.736 84.499  1.00 23.47 ? 392  ALA A N   1 
ATOM   2809 C  CA  . ALA A 1 392 ? 55.371  62.217 85.850  1.00 27.31 ? 392  ALA A CA  1 
ATOM   2810 C  C   . ALA A 1 392 ? 54.839  61.110 86.738  1.00 30.49 ? 392  ALA A C   1 
ATOM   2811 O  O   . ALA A 1 392 ? 55.132  61.083 87.939  1.00 30.64 ? 392  ALA A O   1 
ATOM   2812 C  CB  . ALA A 1 392 ? 54.366  63.365 85.812  1.00 26.17 ? 392  ALA A CB  1 
ATOM   2813 N  N   . LYS A 1 393 ? 54.043  60.207 86.177  1.00 23.17 ? 393  LYS A N   1 
ATOM   2814 C  CA  . LYS A 1 393 ? 53.589  59.026 86.882  1.00 25.24 ? 393  LYS A CA  1 
ATOM   2815 C  C   . LYS A 1 393 ? 53.719  57.818 85.964  1.00 29.89 ? 393  LYS A C   1 
ATOM   2816 O  O   . LYS A 1 393 ? 53.565  57.916 84.740  1.00 28.27 ? 393  LYS A O   1 
ATOM   2817 C  CB  . LYS A 1 393 ? 52.136  59.160 87.353  1.00 32.87 ? 393  LYS A CB  1 
ATOM   2818 C  CG  . LYS A 1 393 ? 51.138  59.210 86.229  1.00 34.42 ? 393  LYS A CG  1 
ATOM   2819 C  CD  . LYS A 1 393 ? 49.714  59.130 86.764  1.00 30.00 ? 393  LYS A CD  1 
ATOM   2820 C  CE  . LYS A 1 393 ? 48.730  59.535 85.686  1.00 35.49 ? 393  LYS A CE  1 
ATOM   2821 N  NZ  . LYS A 1 393 ? 48.664  58.484 84.631  1.00 43.18 ? 393  LYS A NZ  1 
ATOM   2822 N  N   . LEU A 1 394 ? 53.964  56.664 86.570  1.00 22.78 ? 394  LEU A N   1 
ATOM   2823 C  CA  . LEU A 1 394 ? 54.056  55.418 85.813  1.00 29.78 ? 394  LEU A CA  1 
ATOM   2824 C  C   . LEU A 1 394 ? 52.771  54.598 85.838  1.00 30.39 ? 394  LEU A C   1 
ATOM   2825 O  O   . LEU A 1 394 ? 52.235  54.258 84.782  1.00 37.94 ? 394  LEU A O   1 
ATOM   2826 C  CB  . LEU A 1 394 ? 55.266  54.587 86.245  1.00 22.97 ? 394  LEU A CB  1 
ATOM   2827 C  CG  . LEU A 1 394 ? 56.612  55.270 86.031  1.00 20.95 ? 394  LEU A CG  1 
ATOM   2828 C  CD1 . LEU A 1 394 ? 57.625  54.822 87.048  1.00 20.43 ? 394  LEU A CD1 1 
ATOM   2829 C  CD2 . LEU A 1 394 ? 57.072  54.985 84.601  1.00 23.29 ? 394  LEU A CD2 1 
ATOM   2830 N  N   . ILE A 1 395 ? 52.293  54.222 87.018  1.00 37.87 ? 395  ILE A N   1 
ATOM   2831 C  CA  . ILE A 1 395 ? 51.045  53.482 87.120  1.00 33.24 ? 395  ILE A CA  1 
ATOM   2832 C  C   . ILE A 1 395 ? 49.968  54.373 87.717  1.00 32.43 ? 395  ILE A C   1 
ATOM   2833 O  O   . ILE A 1 395 ? 50.222  55.495 88.167  1.00 33.21 ? 395  ILE A O   1 
ATOM   2834 C  CB  . ILE A 1 395 ? 51.175  52.104 87.817  1.00 35.46 ? 395  ILE A CB  1 
ATOM   2835 C  CG1 . ILE A 1 395 ? 52.039  52.128 89.082  1.00 39.91 ? 395  ILE A CG1 1 
ATOM   2836 C  CG2 . ILE A 1 395 ? 51.748  51.074 86.837  1.00 39.64 ? 395  ILE A CG2 1 
ATOM   2837 C  CD1 . ILE A 1 395 ? 51.603  53.097 90.139  1.00 38.08 ? 395  ILE A CD1 1 
ATOM   2838 N  N   . SER A 1 396 ? 48.734  53.903 87.624  1.00 25.85 ? 396  SER A N   1 
ATOM   2839 C  CA  . SER A 1 396 ? 47.605  54.693 88.052  1.00 26.76 ? 396  SER A CA  1 
ATOM   2840 C  C   . SER A 1 396 ? 46.911  54.095 89.262  1.00 25.53 ? 396  SER A C   1 
ATOM   2841 O  O   . SER A 1 396 ? 45.912  54.655 89.715  1.00 26.86 ? 396  SER A O   1 
ATOM   2842 C  CB  . SER A 1 396 ? 46.619  54.857 86.894  1.00 30.18 ? 396  SER A CB  1 
ATOM   2843 O  OG  . SER A 1 396 ? 47.030  55.939 86.058  1.00 37.49 ? 396  SER A OG  1 
ATOM   2844 N  N   . GLU A 1 397 ? 47.406  52.964 89.775  1.00 24.60 ? 397  GLU A N   1 
ATOM   2845 C  CA  . GLU A 1 397 ? 46.872  52.344 90.981  1.00 25.07 ? 397  GLU A CA  1 
ATOM   2846 C  C   . GLU A 1 397 ? 48.007  51.798 91.825  1.00 24.42 ? 397  GLU A C   1 
ATOM   2847 O  O   . GLU A 1 397 ? 48.993  51.282 91.291  1.00 25.60 ? 397  GLU A O   1 
ATOM   2848 C  CB  . GLU A 1 397 ? 45.902  51.187 90.717  1.00 29.35 ? 397  GLU A CB  1 
ATOM   2849 C  CG  . GLU A 1 397 ? 44.953  51.385 89.593  1.00 30.30 ? 397  GLU A CG  1 
ATOM   2850 C  CD  . GLU A 1 397 ? 43.906  50.294 89.532  1.00 31.11 ? 397  GLU A CD  1 
ATOM   2851 O  OE1 . GLU A 1 397 ? 44.104  49.227 90.175  1.00 32.19 ? 397  GLU A OE1 1 
ATOM   2852 O  OE2 . GLU A 1 397 ? 42.887  50.517 88.852  1.00 29.46 ? 397  GLU A OE2 1 
ATOM   2853 N  N   . GLU A 1 398 ? 47.854  51.905 93.141  1.00 25.21 ? 398  GLU A N   1 
ATOM   2854 C  CA  . GLU A 1 398 ? 48.828  51.370 94.084  1.00 26.04 ? 398  GLU A CA  1 
ATOM   2855 C  C   . GLU A 1 398 ? 48.070  50.637 95.179  1.00 24.69 ? 398  GLU A C   1 
ATOM   2856 O  O   . GLU A 1 398 ? 47.076  51.145 95.695  1.00 27.20 ? 398  GLU A O   1 
ATOM   2857 C  CB  . GLU A 1 398 ? 49.654  52.517 94.689  1.00 32.33 ? 398  GLU A CB  1 
ATOM   2858 C  CG  . GLU A 1 398 ? 50.634  52.085 95.779  1.00 40.88 ? 398  GLU A CG  1 
ATOM   2859 C  CD  . GLU A 1 398 ? 51.303  53.263 96.484  1.00 45.50 ? 398  GLU A CD  1 
ATOM   2860 O  OE1 . GLU A 1 398 ? 52.336  53.041 97.156  1.00 52.66 ? 398  GLU A OE1 1 
ATOM   2861 O  OE2 . GLU A 1 398 ? 50.801  54.405 96.373  1.00 41.94 ? 398  GLU A OE2 1 
ATOM   2862 N  N   . GLN A 1 399 ? 48.529  49.435 95.523  1.00 27.60 ? 399  GLN A N   1 
ATOM   2863 C  CA  . GLN A 1 399 ? 47.974  48.680 96.640  1.00 28.44 ? 399  GLN A CA  1 
ATOM   2864 C  C   . GLN A 1 399 ? 48.852  48.934 97.854  1.00 25.38 ? 399  GLN A C   1 
ATOM   2865 O  O   . GLN A 1 399 ? 50.081  48.821 97.769  1.00 30.51 ? 399  GLN A O   1 
ATOM   2866 C  CB  . GLN A 1 399 ? 47.945  47.178 96.332  1.00 34.05 ? 399  GLN A CB  1 
ATOM   2867 C  CG  . GLN A 1 399 ? 47.363  46.298 97.462  1.00 35.93 ? 399  GLN A CG  1 
ATOM   2868 C  CD  . GLN A 1 399 ? 45.874  46.557 97.721  1.00 45.02 ? 399  GLN A CD  1 
ATOM   2869 O  OE1 . GLN A 1 399 ? 45.023  46.291 96.865  1.00 42.62 ? 399  GLN A OE1 1 
ATOM   2870 N  NE2 . GLN A 1 399 ? 45.551  47.050 98.917  1.00 39.63 ? 399  GLN A NE2 1 
ATOM   2871 N  N   . VAL A 1 400 ? 48.228  49.295 98.964  1.00 27.27 ? 400  VAL A N   1 
ATOM   2872 C  CA  . VAL A 1 400 ? 48.920  49.596 100.210 1.00 33.50 ? 400  VAL A CA  1 
ATOM   2873 C  C   . VAL A 1 400 ? 48.726  48.407 101.135 1.00 26.10 ? 400  VAL A C   1 
ATOM   2874 O  O   . VAL A 1 400 ? 47.607  47.891 101.258 1.00 27.67 ? 400  VAL A O   1 
ATOM   2875 C  CB  . VAL A 1 400 ? 48.351  50.871 100.855 1.00 31.28 ? 400  VAL A CB  1 
ATOM   2876 C  CG1 . VAL A 1 400 ? 49.021  51.126 102.202 1.00 39.36 ? 400  VAL A CG1 1 
ATOM   2877 C  CG2 . VAL A 1 400 ? 48.508  52.064 99.924  1.00 39.36 ? 400  VAL A CG2 1 
ATOM   2878 N  N   . LEU A 1 401 ? 49.805  47.974 101.792 1.00 26.77 ? 401  LEU A N   1 
ATOM   2879 C  CA  . LEU A 1 401 ? 49.715  46.995 102.868 1.00 28.28 ? 401  LEU A CA  1 
ATOM   2880 C  C   . LEU A 1 401 ? 50.278  47.602 104.150 1.00 27.37 ? 401  LEU A C   1 
ATOM   2881 O  O   . LEU A 1 401 ? 51.359  48.201 104.134 1.00 35.23 ? 401  LEU A O   1 
ATOM   2882 C  CB  . LEU A 1 401 ? 50.548  45.776 102.495 1.00 25.02 ? 401  LEU A CB  1 
ATOM   2883 C  CG  . LEU A 1 401 ? 49.970  44.913 101.375 1.00 25.14 ? 401  LEU A CG  1 
ATOM   2884 C  CD1 . LEU A 1 401 ? 50.907  43.744 101.068 1.00 27.65 ? 401  LEU A CD1 1 
ATOM   2885 C  CD2 . LEU A 1 401 ? 48.597  44.404 101.682 1.00 25.94 ? 401  LEU A CD2 1 
ATOM   2886 N  N   . TYR A 1 402 ? 49.572  47.417 105.262 1.00 28.62 ? 402  TYR A N   1 
ATOM   2887 C  CA  . TYR A 1 402 ? 49.955  48.013 106.539 1.00 30.61 ? 402  TYR A CA  1 
ATOM   2888 C  C   . TYR A 1 402 ? 50.413  46.949 107.524 1.00 29.43 ? 402  TYR A C   1 
ATOM   2889 O  O   . TYR A 1 402 ? 49.732  45.933 107.708 1.00 30.41 ? 402  TYR A O   1 
ATOM   2890 C  CB  . TYR A 1 402 ? 48.812  48.809 107.174 1.00 40.28 ? 402  TYR A CB  1 
ATOM   2891 C  CG  . TYR A 1 402 ? 48.425  50.052 106.415 1.00 43.26 ? 402  TYR A CG  1 
ATOM   2892 C  CD1 . TYR A 1 402 ? 49.248  51.175 106.422 1.00 42.02 ? 402  TYR A CD1 1 
ATOM   2893 C  CD2 . TYR A 1 402 ? 47.226  50.119 105.722 1.00 44.15 ? 402  TYR A CD2 1 
ATOM   2894 C  CE1 . TYR A 1 402 ? 48.893  52.326 105.743 1.00 46.37 ? 402  TYR A CE1 1 
ATOM   2895 C  CE2 . TYR A 1 402 ? 46.862  51.266 105.043 1.00 47.54 ? 402  TYR A CE2 1 
ATOM   2896 C  CZ  . TYR A 1 402 ? 47.700  52.364 105.056 1.00 48.62 ? 402  TYR A CZ  1 
ATOM   2897 O  OH  . TYR A 1 402 ? 47.337  53.506 104.376 1.00 53.98 ? 402  TYR A OH  1 
ATOM   2898 N  N   . GLU A 1 403 ? 51.542  47.221 108.188 1.00 31.27 ? 403  GLU A N   1 
ATOM   2899 C  CA  . GLU A 1 403 ? 52.084  46.301 109.191 1.00 31.12 ? 403  GLU A CA  1 
ATOM   2900 C  C   . GLU A 1 403 ? 51.054  45.935 110.256 1.00 34.55 ? 403  GLU A C   1 
ATOM   2901 O  O   . GLU A 1 403 ? 50.964  44.773 110.671 1.00 35.55 ? 403  GLU A O   1 
ATOM   2902 C  CB  . GLU A 1 403 ? 53.305  46.926 109.865 1.00 32.14 ? 403  GLU A CB  1 
ATOM   2903 C  CG  . GLU A 1 403 ? 54.223  45.907 110.539 1.00 37.82 ? 403  GLU A CG  1 
ATOM   2904 C  CD  . GLU A 1 403 ? 55.445  46.543 111.183 1.00 36.19 ? 403  GLU A CD  1 
ATOM   2905 O  OE1 . GLU A 1 403 ? 55.933  47.576 110.674 1.00 36.75 ? 403  GLU A OE1 1 
ATOM   2906 O  OE2 . GLU A 1 403 ? 55.964  45.961 112.163 1.00 45.42 ? 403  GLU A OE2 1 
ATOM   2907 N  N   . HIS A 1 404 ? 50.263  46.911 110.712 1.00 35.37 ? 404  HIS A N   1 
ATOM   2908 C  CA  . HIS A 1 404 ? 49.297  46.649 111.772 1.00 35.93 ? 404  HIS A CA  1 
ATOM   2909 C  C   . HIS A 1 404 ? 48.095  45.842 111.290 1.00 38.17 ? 404  HIS A C   1 
ATOM   2910 O  O   . HIS A 1 404 ? 47.271  45.443 112.116 1.00 42.70 ? 404  HIS A O   1 
ATOM   2911 C  CB  . HIS A 1 404 ? 48.853  47.956 112.430 1.00 42.05 ? 404  HIS A CB  1 
ATOM   2912 C  CG  . HIS A 1 404 ? 48.249  48.940 111.480 1.00 44.30 ? 404  HIS A CG  1 
ATOM   2913 N  ND1 . HIS A 1 404 ? 46.907  48.932 111.163 1.00 52.42 ? 404  HIS A ND1 1 
ATOM   2914 C  CD2 . HIS A 1 404 ? 48.799  49.951 110.767 1.00 43.46 ? 404  HIS A CD2 1 
ATOM   2915 C  CE1 . HIS A 1 404 ? 46.655  49.906 110.307 1.00 43.63 ? 404  HIS A CE1 1 
ATOM   2916 N  NE2 . HIS A 1 404 ? 47.786  50.536 110.046 1.00 47.14 ? 404  HIS A NE2 1 
ATOM   2917 N  N   . HIS A 1 405 ? 47.972  45.601 109.984 1.00 37.98 ? 405  HIS A N   1 
ATOM   2918 C  CA  . HIS A 1 405 ? 46.954  44.713 109.435 1.00 38.57 ? 405  HIS A CA  1 
ATOM   2919 C  C   . HIS A 1 405 ? 47.437  43.282 109.278 1.00 36.72 ? 405  HIS A C   1 
ATOM   2920 O  O   . HIS A 1 405 ? 46.712  42.461 108.704 1.00 39.14 ? 405  HIS A O   1 
ATOM   2921 C  CB  . HIS A 1 405 ? 46.478  45.206 108.066 1.00 38.94 ? 405  HIS A CB  1 
ATOM   2922 C  CG  . HIS A 1 405 ? 45.657  46.452 108.122 1.00 43.89 ? 405  HIS A CG  1 
ATOM   2923 N  ND1 . HIS A 1 405 ? 45.577  47.336 107.067 1.00 44.53 ? 405  HIS A ND1 1 
ATOM   2924 C  CD2 . HIS A 1 405 ? 44.878  46.963 109.104 1.00 38.33 ? 405  HIS A CD2 1 
ATOM   2925 C  CE1 . HIS A 1 405 ? 44.779  48.336 107.397 1.00 40.90 ? 405  HIS A CE1 1 
ATOM   2926 N  NE2 . HIS A 1 405 ? 44.343  48.134 108.626 1.00 43.99 ? 405  HIS A NE2 1 
ATOM   2927 N  N   . ALA A 1 406 ? 48.642  42.967 109.746 1.00 32.63 ? 406  ALA A N   1 
ATOM   2928 C  CA  . ALA A 1 406 ? 49.186  41.631 109.535 1.00 33.45 ? 406  ALA A CA  1 
ATOM   2929 C  C   . ALA A 1 406 ? 48.331  40.585 110.239 1.00 33.34 ? 406  ALA A C   1 
ATOM   2930 O  O   . ALA A 1 406 ? 48.025  40.703 111.428 1.00 35.27 ? 406  ALA A O   1 
ATOM   2931 C  CB  . ALA A 1 406 ? 50.630  41.560 110.032 1.00 35.47 ? 406  ALA A CB  1 
ATOM   2932 N  N   . ASP A 1 407 ? 47.913  39.577 109.479 1.00 32.39 ? 407  ASP A N   1 
ATOM   2933 C  CA  . ASP A 1 407 ? 47.218  38.430 110.041 1.00 33.69 ? 407  ASP A CA  1 
ATOM   2934 C  C   . ASP A 1 407 ? 48.202  37.476 110.697 1.00 33.47 ? 407  ASP A C   1 
ATOM   2935 O  O   . ASP A 1 407 ? 47.864  36.827 111.700 1.00 34.92 ? 407  ASP A O   1 
ATOM   2936 C  CB  . ASP A 1 407 ? 46.511  37.696 108.908 1.00 35.67 ? 407  ASP A CB  1 
ATOM   2937 C  CG  . ASP A 1 407 ? 45.361  38.491 108.336 1.00 34.48 ? 407  ASP A CG  1 
ATOM   2938 O  OD1 . ASP A 1 407 ? 44.475  38.918 109.121 1.00 35.87 ? 407  ASP A OD1 1 
ATOM   2939 O  OD2 . ASP A 1 407 ? 45.384  38.750 107.110 1.00 32.96 ? 407  ASP A OD2 1 
ATOM   2940 N  N   . LYS A 1 408 ? 49.408  37.363 110.136 1.00 31.77 ? 408  LYS A N   1 
ATOM   2941 C  CA  . LYS A 1 408 ? 50.450  36.534 110.741 1.00 31.54 ? 408  LYS A CA  1 
ATOM   2942 C  C   . LYS A 1 408 ? 51.804  37.226 110.621 1.00 31.21 ? 408  LYS A C   1 
ATOM   2943 O  O   . LYS A 1 408 ? 52.084  37.892 109.619 1.00 28.88 ? 408  LYS A O   1 
ATOM   2944 C  CB  . LYS A 1 408 ? 50.494  35.132 110.096 1.00 31.79 ? 408  LYS A CB  1 
ATOM   2945 C  CG  . LYS A 1 408 ? 50.769  33.978 111.075 1.00 43.00 ? 408  LYS A CG  1 
ATOM   2946 C  CD  . LYS A 1 408 ? 51.055  32.641 110.369 1.00 47.88 ? 408  LYS A CD  1 
ATOM   2947 C  CE  . LYS A 1 408 ? 49.790  32.038 109.706 1.00 52.34 ? 408  LYS A CE  1 
ATOM   2948 N  NZ  . LYS A 1 408 ? 50.050  30.949 108.654 1.00 32.44 ? 408  LYS A NZ  1 
ATOM   2949 N  N   . THR A 1 409 ? 52.631  37.082 111.656 1.00 30.62 ? 409  THR A N   1 
ATOM   2950 C  CA  . THR A 1 409 ? 54.002  37.580 111.673 1.00 29.56 ? 409  THR A CA  1 
ATOM   2951 C  C   . THR A 1 409 ? 54.950  36.417 111.942 1.00 29.27 ? 409  THR A C   1 
ATOM   2952 O  O   . THR A 1 409 ? 54.752  35.664 112.900 1.00 30.58 ? 409  THR A O   1 
ATOM   2953 C  CB  . THR A 1 409 ? 54.174  38.681 112.730 1.00 30.58 ? 409  THR A CB  1 
ATOM   2954 O  OG1 . THR A 1 409 ? 53.232  39.735 112.492 1.00 31.79 ? 409  THR A OG1 1 
ATOM   2955 C  CG2 . THR A 1 409 ? 55.587  39.247 112.702 1.00 33.48 ? 409  THR A CG2 1 
ATOM   2956 N  N   . ARG A 1 410 ? 55.966  36.266 111.096 1.00 27.69 ? 410  ARG A N   1 
ATOM   2957 C  CA  . ARG A 1 410 ? 56.940  35.181 111.203 1.00 27.32 ? 410  ARG A CA  1 
ATOM   2958 C  C   . ARG A 1 410 ? 58.314  35.730 111.555 1.00 26.80 ? 410  ARG A C   1 
ATOM   2959 O  O   . ARG A 1 410 ? 58.830  36.596 110.850 1.00 25.66 ? 410  ARG A O   1 
ATOM   2960 C  CB  . ARG A 1 410 ? 57.025  34.382 109.897 1.00 26.07 ? 410  ARG A CB  1 
ATOM   2961 C  CG  . ARG A 1 410 ? 55.684  34.051 109.279 1.00 26.42 ? 410  ARG A CG  1 
ATOM   2962 C  CD  . ARG A 1 410 ? 55.816  33.108 108.077 1.00 25.45 ? 410  ARG A CD  1 
ATOM   2963 N  NE  . ARG A 1 410 ? 54.499  32.721 107.588 1.00 26.08 ? 410  ARG A NE  1 
ATOM   2964 C  CZ  . ARG A 1 410 ? 53.839  31.634 107.959 1.00 27.25 ? 410  ARG A CZ  1 
ATOM   2965 N  NH1 . ARG A 1 410 ? 54.347  30.775 108.835 1.00 27.95 ? 410  ARG A NH1 1 
ATOM   2966 N  NH2 . ARG A 1 410 ? 52.623  31.417 107.467 1.00 28.44 ? 410  ARG A NH2 1 
ATOM   2967 N  N   . LEU A 1 411 ? 58.932  35.197 112.609 1.00 27.70 ? 411  LEU A N   1 
ATOM   2968 C  CA  . LEU A 1 411 ? 60.319  35.513 112.946 1.00 27.33 ? 411  LEU A CA  1 
ATOM   2969 C  C   . LEU A 1 411 ? 61.193  34.392 112.401 1.00 26.45 ? 411  LEU A C   1 
ATOM   2970 O  O   . LEU A 1 411 ? 61.099  33.247 112.858 1.00 27.23 ? 411  LEU A O   1 
ATOM   2971 C  CB  . LEU A 1 411 ? 60.494  35.675 114.458 1.00 29.04 ? 411  LEU A CB  1 
ATOM   2972 C  CG  . LEU A 1 411 ? 59.382  36.495 115.120 1.00 32.93 ? 411  LEU A CG  1 
ATOM   2973 C  CD1 . LEU A 1 411 ? 59.385  36.361 116.629 1.00 35.81 ? 411  LEU A CD1 1 
ATOM   2974 C  CD2 . LEU A 1 411 ? 59.536  37.962 114.719 1.00 36.88 ? 411  LEU A CD2 1 
ATOM   2975 N  N   . LEU A 1 412 ? 62.044  34.723 111.433 1.00 24.95 ? 412  LEU A N   1 
ATOM   2976 C  CA  . LEU A 1 412 ? 62.774  33.734 110.643 1.00 23.99 ? 412  LEU A CA  1 
ATOM   2977 C  C   . LEU A 1 412 ? 64.260  34.065 110.688 1.00 23.42 ? 412  LEU A C   1 
ATOM   2978 O  O   . LEU A 1 412 ? 64.695  35.062 110.105 1.00 22.51 ? 412  LEU A O   1 
ATOM   2979 C  CB  . LEU A 1 412 ? 62.253  33.719 109.202 1.00 22.75 ? 412  LEU A CB  1 
ATOM   2980 C  CG  . LEU A 1 412 ? 60.778  33.330 109.099 1.00 23.42 ? 412  LEU A CG  1 
ATOM   2981 C  CD1 . LEU A 1 412 ? 60.185  33.688 107.741 1.00 22.37 ? 412  LEU A CD1 1 
ATOM   2982 C  CD2 . LEU A 1 412 ? 60.618  31.837 109.406 1.00 24.18 ? 412  LEU A CD2 1 
ATOM   2983 N  N   . LYS A 1 413 ? 65.038  33.236 111.389 1.00 24.07 ? 413  LYS A N   1 
ATOM   2984 C  CA  . LYS A 1 413 ? 66.473  33.452 111.523 1.00 23.77 ? 413  LYS A CA  1 
ATOM   2985 C  C   . LYS A 1 413 ? 67.228  33.001 110.273 1.00 22.35 ? 413  LYS A C   1 
ATOM   2986 O  O   . LYS A 1 413 ? 66.853  32.033 109.601 1.00 22.02 ? 413  LYS A O   1 
ATOM   2987 C  CB  . LYS A 1 413 ? 67.004  32.665 112.733 1.00 25.15 ? 413  LYS A CB  1 
ATOM   2988 C  CG  . LYS A 1 413 ? 68.444  33.011 113.099 1.00 28.04 ? 413  LYS A CG  1 
ATOM   2989 C  CD  . LYS A 1 413 ? 68.952  32.304 114.352 1.00 30.09 ? 413  LYS A CD  1 
ATOM   2990 C  CE  . LYS A 1 413 ? 68.679  30.844 114.318 1.00 30.88 ? 413  LYS A CE  1 
ATOM   2991 N  NZ  . LYS A 1 413 ? 69.227  30.219 115.559 1.00 36.47 ? 413  LYS A NZ  1 
ATOM   2992 N  N   . LEU A 1 414 ? 68.305  33.720 109.966 1.00 21.67 ? 414  LEU A N   1 
ATOM   2993 C  CA  . LEU A 1 414 ? 69.280  33.326 108.952 1.00 20.57 ? 414  LEU A CA  1 
ATOM   2994 C  C   . LEU A 1 414 ? 70.585  33.056 109.687 1.00 22.02 ? 414  LEU A C   1 
ATOM   2995 O  O   . LEU A 1 414 ? 71.109  33.948 110.362 1.00 21.70 ? 414  LEU A O   1 
ATOM   2996 C  CB  . LEU A 1 414 ? 69.476  34.454 107.933 1.00 19.37 ? 414  LEU A CB  1 
ATOM   2997 C  CG  . LEU A 1 414 ? 68.244  35.226 107.453 1.00 19.42 ? 414  LEU A CG  1 
ATOM   2998 C  CD1 . LEU A 1 414 ? 68.609  36.345 106.469 1.00 17.98 ? 414  LEU A CD1 1 
ATOM   2999 C  CD2 . LEU A 1 414 ? 67.219  34.310 106.828 1.00 21.04 ? 414  LEU A CD2 1 
ATOM   3000 N  N   . ASP A 1 415 ? 71.098  31.826 109.593 1.00 21.33 ? 415  ASP A N   1 
ATOM   3001 C  CA  . ASP A 1 415 ? 72.241  31.447 110.413 1.00 22.20 ? 415  ASP A CA  1 
ATOM   3002 C  C   . ASP A 1 415 ? 73.019  30.361 109.678 1.00 21.74 ? 415  ASP A C   1 
ATOM   3003 O  O   . ASP A 1 415 ? 72.671  29.968 108.563 1.00 21.92 ? 415  ASP A O   1 
ATOM   3004 C  CB  . ASP A 1 415 ? 71.768  30.953 111.793 1.00 26.07 ? 415  ASP A CB  1 
ATOM   3005 C  CG  . ASP A 1 415 ? 72.861  31.008 112.876 1.00 25.58 ? 415  ASP A CG  1 
ATOM   3006 O  OD1 . ASP A 1 415 ? 74.025  31.361 112.589 1.00 31.63 ? 415  ASP A OD1 1 
ATOM   3007 O  OD2 . ASP A 1 415 ? 72.526  30.683 114.034 1.00 36.92 ? 415  ASP A OD2 1 
ATOM   3008 N  N   . ALA A 1 416 ? 74.105  29.918 110.292 1.00 25.69 ? 416  ALA A N   1 
ATOM   3009 C  CA  . ALA A 1 416 ? 74.869  28.773 109.816 1.00 25.92 ? 416  ALA A CA  1 
ATOM   3010 C  C   . ALA A 1 416 ? 75.200  27.859 110.987 1.00 28.83 ? 416  ALA A C   1 
ATOM   3011 O  O   . ALA A 1 416 ? 75.368  28.310 112.124 1.00 31.02 ? 416  ALA A O   1 
ATOM   3012 C  CB  . ALA A 1 416 ? 76.166  29.203 109.153 1.00 26.15 ? 416  ALA A CB  1 
ATOM   3013 N  N   . ILE A 1 417 ? 75.257  26.558 110.708 1.00 25.41 ? 417  ILE A N   1 
ATOM   3014 C  CA  . ILE A 1 417 ? 75.819  25.574 111.626 1.00 25.73 ? 417  ILE A CA  1 
ATOM   3015 C  C   . ILE A 1 417 ? 77.032  24.951 110.949 1.00 25.46 ? 417  ILE A C   1 
ATOM   3016 O  O   . ILE A 1 417 ? 77.349  25.261 109.807 1.00 27.19 ? 417  ILE A O   1 
ATOM   3017 C  CB  . ILE A 1 417 ? 74.805  24.501 112.063 1.00 30.12 ? 417  ILE A CB  1 
ATOM   3018 C  CG1 . ILE A 1 417 ? 74.482  23.563 110.891 1.00 34.97 ? 417  ILE A CG1 1 
ATOM   3019 C  CG2 . ILE A 1 417 ? 73.574  25.145 112.702 1.00 33.75 ? 417  ILE A CG2 1 
ATOM   3020 C  CD1 . ILE A 1 417 ? 73.379  22.566 111.179 1.00 35.61 ? 417  ILE A CD1 1 
ATOM   3021 N  N   . GLN A 1 418 ? 77.736  24.090 111.669 1.00 26.76 ? 418  GLN A N   1 
ATOM   3022 C  CA  . GLN A 1 418 ? 78.841  23.338 111.080 1.00 26.75 ? 418  GLN A CA  1 
ATOM   3023 C  C   . GLN A 1 418 ? 78.420  21.887 110.932 1.00 27.38 ? 418  GLN A C   1 
ATOM   3024 O  O   . GLN A 1 418 ? 77.797  21.320 111.838 1.00 28.58 ? 418  GLN A O   1 
ATOM   3025 C  CB  . GLN A 1 418 ? 80.119  23.423 111.937 1.00 28.04 ? 418  GLN A CB  1 
ATOM   3026 C  CG  . GLN A 1 418 ? 80.591  24.849 112.102 1.00 32.89 ? 418  GLN A CG  1 
ATOM   3027 C  CD  . GLN A 1 418 ? 81.241  25.388 110.829 1.00 31.77 ? 418  GLN A CD  1 
ATOM   3028 O  OE1 . GLN A 1 418 ? 80.812  26.404 110.283 1.00 37.68 ? 418  GLN A OE1 1 
ATOM   3029 N  NE2 . GLN A 1 418 ? 82.300  24.719 110.369 1.00 41.63 ? 418  GLN A NE2 1 
ATOM   3030 N  N   . ASP A 1 419 ? 78.745  21.290 109.782 1.00 23.17 ? 419  ASP A N   1 
ATOM   3031 C  CA  . ASP A 1 419 ? 78.449  19.882 109.570 1.00 22.30 ? 419  ASP A CA  1 
ATOM   3032 C  C   . ASP A 1 419 ? 79.579  19.011 110.123 1.00 23.51 ? 419  ASP A C   1 
ATOM   3033 O  O   . ASP A 1 419 ? 80.559  19.505 110.698 1.00 23.85 ? 419  ASP A O   1 
ATOM   3034 C  CB  . ASP A 1 419 ? 78.080  19.593 108.107 1.00 22.43 ? 419  ASP A CB  1 
ATOM   3035 C  CG  . ASP A 1 419 ? 79.256  19.673 107.152 1.00 20.80 ? 419  ASP A CG  1 
ATOM   3036 O  OD1 . ASP A 1 419 ? 80.422  19.729 107.577 1.00 21.51 ? 419  ASP A OD1 1 
ATOM   3037 O  OD2 . ASP A 1 419 ? 78.989  19.638 105.931 1.00 19.98 ? 419  ASP A OD2 1 
ATOM   3038 N  N   . GLU A 1 420 ? 79.443  17.692 109.945 1.00 23.05 ? 420  GLU A N   1 
ATOM   3039 C  CA  . GLU A 1 420 ? 80.428  16.754 110.474 1.00 28.99 ? 420  GLU A CA  1 
ATOM   3040 C  C   . GLU A 1 420 ? 81.774  16.876 109.781 1.00 22.85 ? 420  GLU A C   1 
ATOM   3041 O  O   . GLU A 1 420 ? 82.763  16.332 110.285 1.00 27.84 ? 420  GLU A O   1 
ATOM   3042 C  CB  . GLU A 1 420 ? 79.978  15.308 110.292 1.00 30.09 ? 420  GLU A CB  1 
ATOM   3043 C  CG  . GLU A 1 420 ? 79.763  14.916 108.842 1.00 32.22 ? 420  GLU A CG  1 
ATOM   3044 C  CD  . GLU A 1 420 ? 79.210  13.506 108.697 1.00 35.06 ? 420  GLU A CD  1 
ATOM   3045 O  OE1 . GLU A 1 420 ? 79.899  12.556 109.127 1.00 39.63 ? 420  GLU A OE1 1 
ATOM   3046 O  OE2 . GLU A 1 420 ? 78.107  13.360 108.126 1.00 43.11 ? 420  GLU A OE2 1 
ATOM   3047 N  N   . TYR A 1 421 ? 81.824  17.540 108.629 1.00 23.79 ? 421  TYR A N   1 
ATOM   3048 C  CA  . TYR A 1 421 ? 83.058  17.782 107.898 1.00 26.04 ? 421  TYR A CA  1 
ATOM   3049 C  C   . TYR A 1 421 ? 83.637  19.160 108.181 1.00 26.90 ? 421  TYR A C   1 
ATOM   3050 O  O   . TYR A 1 421 ? 84.536  19.604 107.458 1.00 29.87 ? 421  TYR A O   1 
ATOM   3051 C  CB  . TYR A 1 421 ? 82.809  17.620 106.398 1.00 24.09 ? 421  TYR A CB  1 
ATOM   3052 C  CG  . TYR A 1 421 ? 82.093  16.328 106.041 1.00 23.05 ? 421  TYR A CG  1 
ATOM   3053 C  CD1 . TYR A 1 421 ? 82.727  15.099 106.187 1.00 24.65 ? 421  TYR A CD1 1 
ATOM   3054 C  CD2 . TYR A 1 421 ? 80.787  16.338 105.564 1.00 25.41 ? 421  TYR A CD2 1 
ATOM   3055 C  CE1 . TYR A 1 421 ? 82.081  13.917 105.862 1.00 26.33 ? 421  TYR A CE1 1 
ATOM   3056 C  CE2 . TYR A 1 421 ? 80.135  15.161 105.233 1.00 23.96 ? 421  TYR A CE2 1 
ATOM   3057 C  CZ  . TYR A 1 421 ? 80.786  13.956 105.386 1.00 29.94 ? 421  TYR A CZ  1 
ATOM   3058 O  OH  . TYR A 1 421 ? 80.135  12.785 105.062 1.00 34.36 ? 421  TYR A OH  1 
ATOM   3059 N  N   . ASN A 1 422 ? 83.124  19.853 109.199 1.00 23.40 ? 422  ASN A N   1 
ATOM   3060 C  CA  . ASN A 1 422 ? 83.538  21.217 109.521 1.00 26.48 ? 422  ASN A CA  1 
ATOM   3061 C  C   . ASN A 1 422 ? 83.268  22.214 108.410 1.00 24.89 ? 422  ASN A C   1 
ATOM   3062 O  O   . ASN A 1 422 ? 83.977  23.212 108.285 1.00 27.85 ? 422  ASN A O   1 
ATOM   3063 C  CB  . ASN A 1 422 ? 84.972  21.316 110.047 1.00 28.40 ? 422  ASN A CB  1 
ATOM   3064 C  CG  . ASN A 1 422 ? 85.162  22.507 110.950 1.00 41.51 ? 422  ASN A CG  1 
ATOM   3065 O  OD1 . ASN A 1 422 ? 84.283  22.850 111.744 1.00 44.27 ? 422  ASN A OD1 1 
ATOM   3066 N  ND2 . ASN A 1 422 ? 86.332  23.131 110.861 1.00 47.66 ? 422  ASN A ND2 1 
ATOM   3067 N  N   . ARG A 1 423 ? 82.228  21.965 107.624 1.00 20.73 ? 423  ARG A N   1 
ATOM   3068 C  CA  . ARG A 1 423 ? 81.788  22.945 106.640 1.00 19.31 ? 423  ARG A CA  1 
ATOM   3069 C  C   . ARG A 1 423 ? 80.586  23.719 107.170 1.00 22.91 ? 423  ARG A C   1 
ATOM   3070 O  O   . ARG A 1 423 ? 79.766  23.174 107.914 1.00 22.08 ? 423  ARG A O   1 
ATOM   3071 C  CB  . ARG A 1 423 ? 81.355  22.259 105.337 1.00 19.07 ? 423  ARG A CB  1 
ATOM   3072 C  CG  . ARG A 1 423 ? 82.398  21.352 104.742 1.00 20.16 ? 423  ARG A CG  1 
ATOM   3073 C  CD  . ARG A 1 423 ? 81.916  20.730 103.434 1.00 19.31 ? 423  ARG A CD  1 
ATOM   3074 N  NE  . ARG A 1 423 ? 80.778  19.833 103.625 1.00 17.76 ? 423  ARG A NE  1 
ATOM   3075 C  CZ  . ARG A 1 423 ? 80.156  19.220 102.628 1.00 18.49 ? 423  ARG A CZ  1 
ATOM   3076 N  NH1 . ARG A 1 423 ? 80.580  19.334 101.377 1.00 16.54 ? 423  ARG A NH1 1 
ATOM   3077 N  NH2 . ARG A 1 423 ? 79.085  18.474 102.886 1.00 18.86 ? 423  ARG A NH2 1 
ATOM   3078 N  N   . PRO A 1 424 ? 80.440  24.987 106.802 1.00 22.34 ? 424  PRO A N   1 
ATOM   3079 C  CA  . PRO A 1 424 ? 79.199  25.698 107.130 1.00 21.61 ? 424  PRO A CA  1 
ATOM   3080 C  C   . PRO A 1 424 ? 78.019  25.104 106.379 1.00 20.78 ? 424  PRO A C   1 
ATOM   3081 O  O   . PRO A 1 424 ? 78.124  24.743 105.206 1.00 23.15 ? 424  PRO A O   1 
ATOM   3082 C  CB  . PRO A 1 424 ? 79.455  27.130 106.638 1.00 23.70 ? 424  PRO A CB  1 
ATOM   3083 C  CG  . PRO A 1 424 ? 80.891  27.188 106.217 1.00 30.67 ? 424  PRO A CG  1 
ATOM   3084 C  CD  . PRO A 1 424 ? 81.381  25.802 106.011 1.00 24.25 ? 424  PRO A CD  1 
ATOM   3085 N  N   . VAL A 1 425 ? 76.879  25.037 107.058 1.00 20.46 ? 425  VAL A N   1 
ATOM   3086 C  CA  . VAL A 1 425 ? 75.588  24.755 106.439 1.00 17.91 ? 425  VAL A CA  1 
ATOM   3087 C  C   . VAL A 1 425 ? 74.717  25.974 106.702 1.00 19.04 ? 425  VAL A C   1 
ATOM   3088 O  O   . VAL A 1 425 ? 74.461  26.319 107.864 1.00 19.61 ? 425  VAL A O   1 
ATOM   3089 C  CB  . VAL A 1 425 ? 74.932  23.499 107.040 1.00 20.13 ? 425  VAL A CB  1 
ATOM   3090 C  CG1 . VAL A 1 425 ? 73.748  23.057 106.178 1.00 20.01 ? 425  VAL A CG1 1 
ATOM   3091 C  CG2 . VAL A 1 425 ? 75.965  22.376 107.236 1.00 20.79 ? 425  VAL A CG2 1 
ATOM   3092 N  N   . LEU A 1 426 ? 74.266  26.627 105.641 1.00 18.49 ? 426  LEU A N   1 
ATOM   3093 C  CA  . LEU A 1 426 ? 73.489  27.850 105.786 1.00 16.95 ? 426  LEU A CA  1 
ATOM   3094 C  C   . LEU A 1 426 ? 72.031  27.448 105.943 1.00 17.42 ? 426  LEU A C   1 
ATOM   3095 O  O   . LEU A 1 426 ? 71.514  26.672 105.130 1.00 17.81 ? 426  LEU A O   1 
ATOM   3096 C  CB  . LEU A 1 426 ? 73.684  28.693 104.527 1.00 17.28 ? 426  LEU A CB  1 
ATOM   3097 C  CG  . LEU A 1 426 ? 74.871  29.685 104.535 1.00 18.84 ? 426  LEU A CG  1 
ATOM   3098 C  CD1 . LEU A 1 426 ? 74.754  30.727 105.620 1.00 20.45 ? 426  LEU A CD1 1 
ATOM   3099 C  CD2 . LEU A 1 426 ? 76.218  28.942 104.663 1.00 23.63 ? 426  LEU A CD2 1 
ATOM   3100 N  N   . LEU A 1 427 ? 71.366  27.964 106.989 1.00 17.76 ? 427  LEU A N   1 
ATOM   3101 C  CA  . LEU A 1 427 ? 70.040  27.502 107.385 1.00 18.97 ? 427  LEU A CA  1 
ATOM   3102 C  C   . LEU A 1 427 ? 69.078  28.650 107.647 1.00 20.95 ? 427  LEU A C   1 
ATOM   3103 O  O   . LEU A 1 427 ? 69.436  29.665 108.270 1.00 20.63 ? 427  LEU A O   1 
ATOM   3104 C  CB  . LEU A 1 427 ? 70.097  26.676 108.696 1.00 20.28 ? 427  LEU A CB  1 
ATOM   3105 C  CG  . LEU A 1 427 ? 70.860  25.356 108.680 1.00 21.76 ? 427  LEU A CG  1 
ATOM   3106 C  CD1 . LEU A 1 427 ? 70.700  24.681 110.036 1.00 24.09 ? 427  LEU A CD1 1 
ATOM   3107 C  CD2 . LEU A 1 427 ? 70.412  24.442 107.534 1.00 21.09 ? 427  LEU A CD2 1 
ATOM   3108 N  N   . LEU A 1 428 ? 67.841  28.450 107.187 1.00 18.22 ? 428  LEU A N   1 
ATOM   3109 C  CA  . LEU A 1 428 ? 66.703  29.286 107.540 1.00 18.63 ? 428  LEU A CA  1 
ATOM   3110 C  C   . LEU A 1 428 ? 65.983  28.670 108.741 1.00 21.09 ? 428  LEU A C   1 
ATOM   3111 O  O   . LEU A 1 428 ? 65.681  27.468 108.746 1.00 19.93 ? 428  LEU A O   1 
ATOM   3112 C  CB  . LEU A 1 428 ? 65.744  29.275 106.354 1.00 18.02 ? 428  LEU A CB  1 
ATOM   3113 C  CG  . LEU A 1 428 ? 66.356  29.767 105.045 1.00 17.07 ? 428  LEU A CG  1 
ATOM   3114 C  CD1 . LEU A 1 428 ? 65.352  29.635 103.911 1.00 16.65 ? 428  LEU A CD1 1 
ATOM   3115 C  CD2 . LEU A 1 428 ? 66.780  31.211 105.205 1.00 20.24 ? 428  LEU A CD2 1 
ATOM   3116 N  N   . ASP A 1 429 ? 65.723  29.485 109.773 1.00 20.54 ? 429  ASP A N   1 
ATOM   3117 C  CA  . ASP A 1 429 ? 64.794  29.102 110.855 1.00 21.58 ? 429  ASP A CA  1 
ATOM   3118 C  C   . ASP A 1 429 ? 65.232  27.815 111.549 1.00 23.92 ? 429  ASP A C   1 
ATOM   3119 O  O   . ASP A 1 429 ? 64.403  26.988 111.933 1.00 24.37 ? 429  ASP A O   1 
ATOM   3120 C  CB  . ASP A 1 429 ? 63.364  29.008 110.299 1.00 22.43 ? 429  ASP A CB  1 
ATOM   3121 C  CG  . ASP A 1 429 ? 62.303  28.763 111.357 1.00 29.02 ? 429  ASP A CG  1 
ATOM   3122 O  OD1 . ASP A 1 429 ? 62.383  29.341 112.473 1.00 31.80 ? 429  ASP A OD1 1 
ATOM   3123 O  OD2 . ASP A 1 429 ? 61.354  28.003 111.035 1.00 27.83 ? 429  ASP A OD2 1 
ATOM   3124 N  N   . ASP A 1 430 ? 66.548  27.636 111.701 1.00 22.98 ? 430  ASP A N   1 
ATOM   3125 C  CA  . ASP A 1 430 ? 67.119  26.482 112.406 1.00 22.64 ? 430  ASP A CA  1 
ATOM   3126 C  C   . ASP A 1 430 ? 66.777  25.155 111.749 1.00 24.61 ? 430  ASP A C   1 
ATOM   3127 O  O   . ASP A 1 430 ? 66.861  24.104 112.400 1.00 25.49 ? 430  ASP A O   1 
ATOM   3128 C  CB  . ASP A 1 430 ? 66.694  26.422 113.882 1.00 26.21 ? 430  ASP A CB  1 
ATOM   3129 C  CG  . ASP A 1 430 ? 67.198  27.585 114.680 1.00 35.41 ? 430  ASP A CG  1 
ATOM   3130 O  OD1 . ASP A 1 430 ? 68.425  27.814 114.644 1.00 38.53 ? 430  ASP A OD1 1 
ATOM   3131 O  OD2 . ASP A 1 430 ? 66.370  28.266 115.313 1.00 40.01 ? 430  ASP A OD2 1 
ATOM   3132 N  N   . ARG A 1 431 ? 66.361  25.170 110.489 1.00 22.34 ? 431  ARG A N   1 
ATOM   3133 C  CA  . ARG A 1 431 ? 65.802  23.977 109.878 1.00 21.57 ? 431  ARG A CA  1 
ATOM   3134 C  C   . ARG A 1 431 ? 66.454  23.702 108.538 1.00 21.80 ? 431  ARG A C   1 
ATOM   3135 O  O   . ARG A 1 431 ? 66.932  24.611 107.862 1.00 23.14 ? 431  ARG A O   1 
ATOM   3136 C  CB  . ARG A 1 431 ? 64.286  24.115 109.704 1.00 21.33 ? 431  ARG A CB  1 
ATOM   3137 C  CG  . ARG A 1 431 ? 63.544  23.967 111.039 1.00 22.65 ? 431  ARG A CG  1 
ATOM   3138 C  CD  . ARG A 1 431 ? 62.140  24.500 110.968 1.00 25.88 ? 431  ARG A CD  1 
ATOM   3139 N  NE  . ARG A 1 431 ? 61.379  24.071 112.135 1.00 31.01 ? 431  ARG A NE  1 
ATOM   3140 C  CZ  . ARG A 1 431 ? 61.464  24.652 113.322 1.00 35.25 ? 431  ARG A CZ  1 
ATOM   3141 N  NH1 . ARG A 1 431 ? 62.282  25.674 113.533 1.00 31.50 ? 431  ARG A NH1 1 
ATOM   3142 N  NH2 . ARG A 1 431 ? 60.705  24.206 114.320 1.00 33.89 ? 431  ARG A NH2 1 
ATOM   3143 N  N   . MET A 1 432 ? 66.465  22.432 108.161 1.00 22.16 ? 432  MET A N   1 
ATOM   3144 C  CA  . MET A 1 432 ? 66.950  22.023 106.857 1.00 20.79 ? 432  MET A CA  1 
ATOM   3145 C  C   . MET A 1 432 ? 65.783  21.865 105.892 1.00 18.90 ? 432  MET A C   1 
ATOM   3146 O  O   . MET A 1 432 ? 64.614  21.831 106.295 1.00 19.98 ? 432  MET A O   1 
ATOM   3147 C  CB  . MET A 1 432 ? 67.767  20.733 106.975 1.00 28.29 ? 432  MET A CB  1 
ATOM   3148 C  CG  . MET A 1 432 ? 69.042  20.941 107.764 1.00 29.40 ? 432  MET A CG  1 
ATOM   3149 S  SD  . MET A 1 432 ? 69.915  19.411 108.105 1.00 36.08 ? 432  MET A SD  1 
ATOM   3150 C  CE  . MET A 1 432 ? 71.450  20.066 108.770 1.00 42.33 ? 432  MET A CE  1 
ATOM   3151 N  N   . TRP A 1 433 ? 66.122  21.785 104.596 1.00 18.67 ? 433  TRP A N   1 
ATOM   3152 C  CA  . TRP A 1 433 ? 65.099  21.648 103.561 1.00 17.88 ? 433  TRP A CA  1 
ATOM   3153 C  C   . TRP A 1 433 ? 64.116  20.518 103.884 1.00 21.71 ? 433  TRP A C   1 
ATOM   3154 O  O   . TRP A 1 433 ? 62.899  20.680 103.727 1.00 20.74 ? 433  TRP A O   1 
ATOM   3155 C  CB  . TRP A 1 433 ? 65.776  21.399 102.213 1.00 19.56 ? 433  TRP A CB  1 
ATOM   3156 C  CG  . TRP A 1 433 ? 64.852  20.848 101.168 1.00 17.11 ? 433  TRP A CG  1 
ATOM   3157 C  CD1 . TRP A 1 433 ? 64.836  19.558 100.676 1.00 18.27 ? 433  TRP A CD1 1 
ATOM   3158 C  CD2 . TRP A 1 433 ? 63.792  21.545 100.502 1.00 17.67 ? 433  TRP A CD2 1 
ATOM   3159 N  NE1 . TRP A 1 433 ? 63.836  19.429 99.737  1.00 18.11 ? 433  TRP A NE1 1 
ATOM   3160 C  CE2 . TRP A 1 433 ? 63.181  20.630 99.612  1.00 17.22 ? 433  TRP A CE2 1 
ATOM   3161 C  CE3 . TRP A 1 433 ? 63.275  22.847 100.594 1.00 17.64 ? 433  TRP A CE3 1 
ATOM   3162 C  CZ2 . TRP A 1 433 ? 62.112  20.984 98.794  1.00 17.78 ? 433  TRP A CZ2 1 
ATOM   3163 C  CZ3 . TRP A 1 433 ? 62.218  23.206 99.767  1.00 19.00 ? 433  TRP A CZ3 1 
ATOM   3164 C  CH2 . TRP A 1 433 ? 61.632  22.270 98.890  1.00 19.40 ? 433  TRP A CH2 1 
ATOM   3165 N  N   . HIS A 1 434 ? 64.615  19.379 104.359 1.00 21.31 ? 434  HIS A N   1 
ATOM   3166 C  CA  . HIS A 1 434 ? 63.784  18.192 104.509 1.00 22.14 ? 434  HIS A CA  1 
ATOM   3167 C  C   . HIS A 1 434 ? 63.017  18.133 105.828 1.00 26.74 ? 434  HIS A C   1 
ATOM   3168 O  O   . HIS A 1 434 ? 62.227  17.203 106.033 1.00 26.04 ? 434  HIS A O   1 
ATOM   3169 C  CB  . HIS A 1 434 ? 64.641  16.936 104.308 1.00 25.55 ? 434  HIS A CB  1 
ATOM   3170 C  CG  . HIS A 1 434 ? 65.785  16.811 105.274 1.00 35.21 ? 434  HIS A CG  1 
ATOM   3171 N  ND1 . HIS A 1 434 ? 65.692  17.159 106.606 1.00 47.95 ? 434  HIS A ND1 1 
ATOM   3172 C  CD2 . HIS A 1 434 ? 67.055  16.371 105.092 1.00 46.61 ? 434  HIS A CD2 1 
ATOM   3173 C  CE1 . HIS A 1 434 ? 66.848  16.928 107.205 1.00 42.76 ? 434  HIS A CE1 1 
ATOM   3174 N  NE2 . HIS A 1 434 ? 67.696  16.461 106.306 1.00 47.71 ? 434  HIS A NE2 1 
ATOM   3175 N  N   . ASP A 1 435 ? 63.223  19.094 106.722 1.00 22.75 ? 435  ASP A N   1 
ATOM   3176 C  CA  . ASP A 1 435 ? 62.463  19.145 107.960 1.00 25.85 ? 435  ASP A CA  1 
ATOM   3177 C  C   . ASP A 1 435 ? 61.008  19.503 107.654 1.00 24.21 ? 435  ASP A C   1 
ATOM   3178 O  O   . ASP A 1 435 ? 60.722  20.176 106.660 1.00 23.19 ? 435  ASP A O   1 
ATOM   3179 C  CB  . ASP A 1 435 ? 63.077  20.212 108.854 1.00 23.58 ? 435  ASP A CB  1 
ATOM   3180 C  CG  . ASP A 1 435 ? 64.325  19.730 109.561 1.00 29.47 ? 435  ASP A CG  1 
ATOM   3181 O  OD1 . ASP A 1 435 ? 64.520  18.497 109.688 1.00 34.00 ? 435  ASP A OD1 1 
ATOM   3182 O  OD2 . ASP A 1 435 ? 65.160  20.582 109.913 1.00 26.47 ? 435  ASP A OD2 1 
ATOM   3183 N  N   . PRO A 1 436 ? 60.068  19.066 108.491 1.00 26.06 ? 436  PRO A N   1 
ATOM   3184 C  CA  . PRO A 1 436 ? 58.649  19.332 108.208 1.00 24.46 ? 436  PRO A CA  1 
ATOM   3185 C  C   . PRO A 1 436 ? 58.357  20.810 107.961 1.00 24.19 ? 436  PRO A C   1 
ATOM   3186 O  O   . PRO A 1 436 ? 58.917  21.698 108.610 1.00 24.71 ? 436  PRO A O   1 
ATOM   3187 C  CB  . PRO A 1 436 ? 57.928  18.809 109.455 1.00 27.87 ? 436  PRO A CB  1 
ATOM   3188 C  CG  . PRO A 1 436 ? 58.878  17.815 110.076 1.00 31.06 ? 436  PRO A CG  1 
ATOM   3189 C  CD  . PRO A 1 436 ? 60.266  18.144 109.626 1.00 29.00 ? 436  PRO A CD  1 
ATOM   3190 N  N   . VAL A 1 437 ? 57.472  21.058 106.991 1.00 24.92 ? 437  VAL A N   1 
ATOM   3191 C  CA  . VAL A 1 437 ? 57.137  22.422 106.599 1.00 22.56 ? 437  VAL A CA  1 
ATOM   3192 C  C   . VAL A 1 437 ? 56.598  23.210 107.789 1.00 23.37 ? 437  VAL A C   1 
ATOM   3193 O  O   . VAL A 1 437 ? 55.789  22.711 108.580 1.00 25.63 ? 437  VAL A O   1 
ATOM   3194 C  CB  . VAL A 1 437 ? 56.155  22.419 105.412 1.00 25.87 ? 437  VAL A CB  1 
ATOM   3195 C  CG1 . VAL A 1 437 ? 54.849  21.761 105.779 1.00 32.16 ? 437  VAL A CG1 1 
ATOM   3196 C  CG2 . VAL A 1 437 ? 55.893  23.843 104.937 1.00 27.34 ? 437  VAL A CG2 1 
ATOM   3197 N  N   . THR A 1 438 ? 57.065  24.459 107.918 1.00 24.15 ? 438  THR A N   1 
ATOM   3198 C  CA  . THR A 1 438 ? 56.581  25.375 108.938 1.00 23.70 ? 438  THR A CA  1 
ATOM   3199 C  C   . THR A 1 438 ? 55.938  26.633 108.374 1.00 23.33 ? 438  THR A C   1 
ATOM   3200 O  O   . THR A 1 438 ? 55.148  27.271 109.086 1.00 25.36 ? 438  THR A O   1 
ATOM   3201 C  CB  . THR A 1 438 ? 57.718  25.794 109.882 1.00 23.66 ? 438  THR A CB  1 
ATOM   3202 O  OG1 . THR A 1 438 ? 58.859  26.178 109.108 1.00 23.73 ? 438  THR A OG1 1 
ATOM   3203 C  CG2 . THR A 1 438 ? 58.126  24.627 110.784 1.00 25.37 ? 438  THR A CG2 1 
ATOM   3204 N  N   . GLU A 1 439 ? 56.265  27.031 107.140 1.00 22.27 ? 439  GLU A N   1 
ATOM   3205 C  CA  . GLU A 1 439 ? 55.636  28.198 106.523 1.00 22.06 ? 439  GLU A CA  1 
ATOM   3206 C  C   . GLU A 1 439 ? 54.456  27.707 105.696 1.00 23.18 ? 439  GLU A C   1 
ATOM   3207 O  O   . GLU A 1 439 ? 54.632  27.169 104.597 1.00 23.40 ? 439  GLU A O   1 
ATOM   3208 C  CB  . GLU A 1 439 ? 56.649  28.975 105.683 1.00 20.94 ? 439  GLU A CB  1 
ATOM   3209 C  CG  . GLU A 1 439 ? 57.566  29.812 106.562 1.00 21.78 ? 439  GLU A CG  1 
ATOM   3210 C  CD  . GLU A 1 439 ? 58.602  28.960 107.279 1.00 21.35 ? 439  GLU A CD  1 
ATOM   3211 O  OE1 . GLU A 1 439 ? 59.408  28.300 106.596 1.00 20.70 ? 439  GLU A OE1 1 
ATOM   3212 O  OE2 . GLU A 1 439 ? 58.524  28.869 108.525 1.00 23.79 ? 439  GLU A OE2 1 
ATOM   3213 N  N   . LYS A 1 440 ? 53.244  27.908 106.216 1.00 23.96 ? 440  LYS A N   1 
ATOM   3214 C  CA  . LYS A 1 440 ? 52.013  27.489 105.549 1.00 23.83 ? 440  LYS A CA  1 
ATOM   3215 C  C   . LYS A 1 440 ? 51.063  28.680 105.447 1.00 24.24 ? 440  LYS A C   1 
ATOM   3216 O  O   . LYS A 1 440 ? 50.024  28.723 106.115 1.00 25.44 ? 440  LYS A O   1 
ATOM   3217 C  CB  . LYS A 1 440 ? 51.351  26.308 106.265 1.00 25.80 ? 440  LYS A CB  1 
ATOM   3218 C  CG  . LYS A 1 440 ? 52.265  25.100 106.393 1.00 26.68 ? 440  LYS A CG  1 
ATOM   3219 C  CD  . LYS A 1 440 ? 51.643  24.078 107.319 1.00 32.50 ? 440  LYS A CD  1 
ATOM   3220 C  CE  . LYS A 1 440 ? 52.069  24.345 108.754 1.00 37.32 ? 440  LYS A CE  1 
ATOM   3221 N  NZ  . LYS A 1 440 ? 51.412  23.411 109.718 1.00 39.39 ? 440  LYS A NZ  1 
ATOM   3222 N  N   . PRO A 1 441 ? 51.402  29.676 104.625 1.00 24.16 ? 441  PRO A N   1 
ATOM   3223 C  CA  . PRO A 1 441 ? 50.538  30.864 104.509 1.00 24.06 ? 441  PRO A CA  1 
ATOM   3224 C  C   . PRO A 1 441 ? 49.169  30.537 103.928 1.00 25.37 ? 441  PRO A C   1 
ATOM   3225 O  O   . PRO A 1 441 ? 49.032  29.685 103.042 1.00 24.70 ? 441  PRO A O   1 
ATOM   3226 C  CB  . PRO A 1 441 ? 51.341  31.807 103.596 1.00 25.23 ? 441  PRO A CB  1 
ATOM   3227 C  CG  . PRO A 1 441 ? 52.367  30.932 102.932 1.00 24.30 ? 441  PRO A CG  1 
ATOM   3228 C  CD  . PRO A 1 441 ? 52.652  29.811 103.854 1.00 22.40 ? 441  PRO A CD  1 
ATOM   3229 N  N   . VAL A 1 442 ? 48.145  31.229 104.443 1.00 27.56 ? 442  VAL A N   1 
ATOM   3230 C  CA  . VAL A 1 442 ? 46.753  31.016 104.053 1.00 26.56 ? 442  VAL A CA  1 
ATOM   3231 C  C   . VAL A 1 442 ? 46.335  32.082 103.052 1.00 27.90 ? 442  VAL A C   1 
ATOM   3232 O  O   . VAL A 1 442 ? 46.548  33.281 103.281 1.00 29.35 ? 442  VAL A O   1 
ATOM   3233 C  CB  . VAL A 1 442 ? 45.819  31.035 105.276 1.00 27.93 ? 442  VAL A CB  1 
ATOM   3234 C  CG1 . VAL A 1 442 ? 44.404  30.711 104.836 1.00 34.47 ? 442  VAL A CG1 1 
ATOM   3235 C  CG2 . VAL A 1 442 ? 46.320  30.051 106.320 1.00 28.18 ? 442  VAL A CG2 1 
ATOM   3236 N  N   . ILE A 1 443 ? 45.708  31.647 101.957 1.00 26.58 ? 443  ILE A N   1 
ATOM   3237 C  CA  . ILE A 1 443 ? 45.158  32.580 100.978 1.00 27.66 ? 443  ILE A CA  1 
ATOM   3238 C  C   . ILE A 1 443 ? 44.240  33.584 101.669 1.00 27.61 ? 443  ILE A C   1 
ATOM   3239 O  O   . ILE A 1 443 ? 43.382  33.224 102.487 1.00 30.71 ? 443  ILE A O   1 
ATOM   3240 C  CB  . ILE A 1 443 ? 44.425  31.805 99.868  1.00 30.69 ? 443  ILE A CB  1 
ATOM   3241 C  CG1 . ILE A 1 443 ? 45.394  30.875 99.136  1.00 33.67 ? 443  ILE A CG1 1 
ATOM   3242 C  CG2 . ILE A 1 443 ? 43.703  32.765 98.916  1.00 32.91 ? 443  ILE A CG2 1 
ATOM   3243 C  CD1 . ILE A 1 443 ? 46.143  31.529 98.071  1.00 34.72 ? 443  ILE A CD1 1 
ATOM   3244 N  N   . GLY A 1 444 ? 44.416  34.856 101.322 1.00 27.38 ? 444  GLY A N   1 
ATOM   3245 C  CA  . GLY A 1 444 ? 43.697  35.946 101.932 1.00 30.09 ? 444  GLY A CA  1 
ATOM   3246 C  C   . GLY A 1 444 ? 44.427  36.629 103.064 1.00 31.56 ? 444  GLY A C   1 
ATOM   3247 O  O   . GLY A 1 444 ? 44.037  37.742 103.445 1.00 35.48 ? 444  GLY A O   1 
ATOM   3248 N  N   . ASP A 1 445 ? 45.481  36.016 103.596 1.00 28.15 ? 445  ASP A N   1 
ATOM   3249 C  CA  . ASP A 1 445 ? 46.168  36.548 104.761 1.00 27.55 ? 445  ASP A CA  1 
ATOM   3250 C  C   . ASP A 1 445 ? 47.256  37.531 104.343 1.00 26.59 ? 445  ASP A C   1 
ATOM   3251 O  O   . ASP A 1 445 ? 47.945  37.337 103.333 1.00 27.02 ? 445  ASP A O   1 
ATOM   3252 C  CB  . ASP A 1 445 ? 46.801  35.409 105.566 1.00 27.65 ? 445  ASP A CB  1 
ATOM   3253 C  CG  . ASP A 1 445 ? 45.874  34.846 106.629 1.00 31.34 ? 445  ASP A CG  1 
ATOM   3254 O  OD1 . ASP A 1 445 ? 44.647  35.113 106.577 1.00 33.30 ? 445  ASP A OD1 1 
ATOM   3255 O  OD2 . ASP A 1 445 ? 46.385  34.092 107.487 1.00 32.08 ? 445  ASP A OD2 1 
ATOM   3256 N  N   . THR A 1 446 ? 47.408  38.582 105.137 1.00 29.45 ? 446  THR A N   1 
ATOM   3257 C  CA  . THR A 1 446 ? 48.545  39.482 105.069 1.00 26.25 ? 446  THR A CA  1 
ATOM   3258 C  C   . THR A 1 446 ? 49.580  39.024 106.094 1.00 27.46 ? 446  THR A C   1 
ATOM   3259 O  O   . THR A 1 446 ? 49.252  38.760 107.270 1.00 28.53 ? 446  THR A O   1 
ATOM   3260 C  CB  . THR A 1 446 ? 48.092  40.917 105.358 1.00 27.82 ? 446  THR A CB  1 
ATOM   3261 O  OG1 . THR A 1 446 ? 47.175  41.343 104.339 1.00 30.62 ? 446  THR A OG1 1 
ATOM   3262 C  CG2 . THR A 1 446 ? 49.277  41.882 105.349 1.00 28.69 ? 446  THR A CG2 1 
ATOM   3263 N  N   . GLU A 1 447 ? 50.822  38.885 105.635 1.00 26.40 ? 447  GLU A N   1 
ATOM   3264 C  CA  . GLU A 1 447 ? 51.894  38.372 106.463 1.00 26.26 ? 447  GLU A CA  1 
ATOM   3265 C  C   . GLU A 1 447 ? 53.053  39.353 106.486 1.00 25.26 ? 447  GLU A C   1 
ATOM   3266 O  O   . GLU A 1 447 ? 53.378  39.989 105.472 1.00 23.93 ? 447  GLU A O   1 
ATOM   3267 C  CB  . GLU A 1 447 ? 52.376  36.997 105.990 1.00 24.06 ? 447  GLU A CB  1 
ATOM   3268 C  CG  . GLU A 1 447 ? 51.296  35.933 106.061 1.00 26.92 ? 447  GLU A CG  1 
ATOM   3269 C  CD  . GLU A 1 447 ? 51.844  34.516 106.035 1.00 26.01 ? 447  GLU A CD  1 
ATOM   3270 O  OE1 . GLU A 1 447 ? 53.041  34.330 105.729 1.00 24.79 ? 447  GLU A OE1 1 
ATOM   3271 O  OE2 . GLU A 1 447 ? 51.075  33.585 106.371 1.00 28.30 ? 447  GLU A OE2 1 
ATOM   3272 N  N   . VAL A 1 448 ? 53.650  39.487 107.663 1.00 24.49 ? 448  VAL A N   1 
ATOM   3273 C  CA  . VAL A 1 448 ? 54.917  40.184 107.849 1.00 24.16 ? 448  VAL A CA  1 
ATOM   3274 C  C   . VAL A 1 448 ? 55.968  39.137 108.184 1.00 23.62 ? 448  VAL A C   1 
ATOM   3275 O  O   . VAL A 1 448 ? 55.796  38.359 109.127 1.00 24.20 ? 448  VAL A O   1 
ATOM   3276 C  CB  . VAL A 1 448 ? 54.811  41.246 108.955 1.00 25.30 ? 448  VAL A CB  1 
ATOM   3277 C  CG1 . VAL A 1 448 ? 56.172  41.810 109.275 1.00 25.11 ? 448  VAL A CG1 1 
ATOM   3278 C  CG2 . VAL A 1 448 ? 53.864  42.371 108.519 1.00 25.81 ? 448  VAL A CG2 1 
ATOM   3279 N  N   . TRP A 1 449 ? 57.041  39.092 107.401 1.00 22.61 ? 449  TRP A N   1 
ATOM   3280 C  CA  . TRP A 1 449 ? 58.165  38.210 107.685 1.00 22.13 ? 449  TRP A CA  1 
ATOM   3281 C  C   . TRP A 1 449 ? 59.332  39.057 108.174 1.00 22.26 ? 449  TRP A C   1 
ATOM   3282 O  O   . TRP A 1 449 ? 59.705  40.038 107.523 1.00 22.23 ? 449  TRP A O   1 
ATOM   3283 C  CB  . TRP A 1 449 ? 58.592  37.424 106.440 1.00 21.30 ? 449  TRP A CB  1 
ATOM   3284 C  CG  . TRP A 1 449 ? 57.595  36.438 105.920 1.00 21.05 ? 449  TRP A CG  1 
ATOM   3285 C  CD1 . TRP A 1 449 ? 56.234  36.474 106.055 1.00 21.92 ? 449  TRP A CD1 1 
ATOM   3286 C  CD2 . TRP A 1 449 ? 57.891  35.275 105.133 1.00 20.13 ? 449  TRP A CD2 1 
ATOM   3287 N  NE1 . TRP A 1 449 ? 55.667  35.385 105.426 1.00 21.35 ? 449  TRP A NE1 1 
ATOM   3288 C  CE2 . TRP A 1 449 ? 56.666  34.645 104.841 1.00 20.84 ? 449  TRP A CE2 1 
ATOM   3289 C  CE3 . TRP A 1 449 ? 59.078  34.695 104.670 1.00 20.29 ? 449  TRP A CE3 1 
ATOM   3290 C  CZ2 . TRP A 1 449 ? 56.587  33.470 104.101 1.00 21.33 ? 449  TRP A CZ2 1 
ATOM   3291 C  CZ3 . TRP A 1 449 ? 59.000  33.515 103.923 1.00 20.62 ? 449  TRP A CZ3 1 
ATOM   3292 C  CH2 . TRP A 1 449 ? 57.763  32.923 103.646 1.00 19.20 ? 449  TRP A CH2 1 
ATOM   3293 N  N   . LYS A 1 450 ? 59.887  38.699 109.329 1.00 22.83 ? 450  LYS A N   1 
ATOM   3294 C  CA  . LYS A 1 450 ? 61.011  39.389 109.942 1.00 23.16 ? 450  LYS A CA  1 
ATOM   3295 C  C   . LYS A 1 450 ? 62.216  38.476 109.815 1.00 22.48 ? 450  LYS A C   1 
ATOM   3296 O  O   . LYS A 1 450 ? 62.295  37.443 110.494 1.00 22.75 ? 450  LYS A O   1 
ATOM   3297 C  CB  . LYS A 1 450 ? 60.707  39.702 111.409 1.00 24.75 ? 450  LYS A CB  1 
ATOM   3298 C  CG  . LYS A 1 450 ? 59.400  40.466 111.582 1.00 25.33 ? 450  LYS A CG  1 
ATOM   3299 C  CD  . LYS A 1 450 ? 59.398  41.248 112.904 1.00 31.24 ? 450  LYS A CD  1 
ATOM   3300 C  CE  . LYS A 1 450 ? 58.358  42.338 112.875 1.00 34.67 ? 450  LYS A CE  1 
ATOM   3301 N  NZ  . LYS A 1 450 ? 58.997  43.692 112.865 1.00 45.47 ? 450  LYS A NZ  1 
ATOM   3302 N  N   . LEU A 1 451 ? 63.160  38.873 108.973 1.00 21.72 ? 451  LEU A N   1 
ATOM   3303 C  CA  . LEU A 1 451 ? 64.347  38.088 108.656 1.00 21.02 ? 451  LEU A CA  1 
ATOM   3304 C  C   . LEU A 1 451 ? 65.458  38.538 109.595 1.00 21.70 ? 451  LEU A C   1 
ATOM   3305 O  O   . LEU A 1 451 ? 65.961  39.659 109.480 1.00 21.89 ? 451  LEU A O   1 
ATOM   3306 C  CB  . LEU A 1 451 ? 64.728  38.315 107.195 1.00 19.95 ? 451  LEU A CB  1 
ATOM   3307 C  CG  . LEU A 1 451 ? 63.594  38.034 106.211 1.00 20.53 ? 451  LEU A CG  1 
ATOM   3308 C  CD1 . LEU A 1 451 ? 63.978  38.502 104.801 1.00 21.04 ? 451  LEU A CD1 1 
ATOM   3309 C  CD2 . LEU A 1 451 ? 63.194  36.560 106.231 1.00 20.55 ? 451  LEU A CD2 1 
ATOM   3310 N  N   . ILE A 1 452 ? 65.803  37.681 110.550 1.00 22.19 ? 452  ILE A N   1 
ATOM   3311 C  CA  . ILE A 1 452 ? 66.741  38.012 111.619 1.00 23.11 ? 452  ILE A CA  1 
ATOM   3312 C  C   . ILE A 1 452 ? 68.094  37.469 111.187 1.00 22.47 ? 452  ILE A C   1 
ATOM   3313 O  O   . ILE A 1 452 ? 68.352  36.264 111.303 1.00 22.24 ? 452  ILE A O   1 
ATOM   3314 C  CB  . ILE A 1 452 ? 66.291  37.417 112.958 1.00 24.56 ? 452  ILE A CB  1 
ATOM   3315 C  CG1 . ILE A 1 452 ? 64.827  37.774 113.236 1.00 28.94 ? 452  ILE A CG1 1 
ATOM   3316 C  CG2 . ILE A 1 452 ? 67.231  37.845 114.060 1.00 26.92 ? 452  ILE A CG2 1 
ATOM   3317 C  CD1 . ILE A 1 452 ? 64.168  36.907 114.300 1.00 32.50 ? 452  ILE A CD1 1 
ATOM   3318 N  N   . ASN A 1 453 ? 68.975  38.336 110.681 1.00 22.25 ? 453  ASN A N   1 
ATOM   3319 C  CA  . ASN A 1 453 ? 70.235  37.851 110.121 1.00 21.61 ? 453  ASN A CA  1 
ATOM   3320 C  C   . ASN A 1 453 ? 71.301  37.853 111.204 1.00 22.59 ? 453  ASN A C   1 
ATOM   3321 O  O   . ASN A 1 453 ? 71.807  38.910 111.590 1.00 24.01 ? 453  ASN A O   1 
ATOM   3322 C  CB  . ASN A 1 453 ? 70.655  38.719 108.935 1.00 20.92 ? 453  ASN A CB  1 
ATOM   3323 C  CG  . ASN A 1 453 ? 71.858  38.145 108.183 1.00 20.19 ? 453  ASN A CG  1 
ATOM   3324 O  OD1 . ASN A 1 453 ? 72.524  37.217 108.655 1.00 20.31 ? 453  ASN A OD1 1 
ATOM   3325 N  ND2 . ASN A 1 453 ? 72.156  38.714 107.024 1.00 19.53 ? 453  ASN A ND2 1 
ATOM   3326 N  N   . VAL A 1 454 ? 71.678  36.659 111.664 1.00 22.67 ? 454  VAL A N   1 
ATOM   3327 C  CA  . VAL A 1 454 ? 72.672  36.540 112.718 1.00 23.71 ? 454  VAL A CA  1 
ATOM   3328 C  C   . VAL A 1 454 ? 74.050  36.205 112.181 1.00 27.55 ? 454  VAL A C   1 
ATOM   3329 O  O   . VAL A 1 454 ? 74.985  36.011 112.969 1.00 28.32 ? 454  VAL A O   1 
ATOM   3330 C  CB  . VAL A 1 454 ? 72.224  35.578 113.839 1.00 28.39 ? 454  VAL A CB  1 
ATOM   3331 C  CG1 . VAL A 1 454 ? 70.815  35.928 114.307 1.00 27.38 ? 454  VAL A CG1 1 
ATOM   3332 C  CG2 . VAL A 1 454 ? 72.267  34.163 113.366 1.00 27.45 ? 454  VAL A CG2 1 
ATOM   3333 N  N   . THR A 1 455 ? 74.207  36.130 110.858 1.00 23.03 ? 455  THR A N   1 
ATOM   3334 C  CA  . THR A 1 455 ? 75.513  35.980 110.232 1.00 24.42 ? 455  THR A CA  1 
ATOM   3335 C  C   . THR A 1 455 ? 76.143  37.356 110.012 1.00 25.45 ? 455  THR A C   1 
ATOM   3336 O  O   . THR A 1 455 ? 75.529  38.398 110.246 1.00 26.75 ? 455  THR A O   1 
ATOM   3337 C  CB  . THR A 1 455 ? 75.417  35.223 108.904 1.00 21.85 ? 455  THR A CB  1 
ATOM   3338 O  OG1 . THR A 1 455 ? 74.977  36.123 107.874 1.00 21.13 ? 455  THR A OG1 1 
ATOM   3339 C  CG2 . THR A 1 455 ? 74.465  34.034 108.984 1.00 25.31 ? 455  THR A CG2 1 
ATOM   3340 N  N   . ASN A 1 456 ? 77.376  37.353 109.507 1.00 25.56 ? 456  ASN A N   1 
ATOM   3341 C  CA  . ASN A 1 456 ? 78.124  38.581 109.277 1.00 29.26 ? 456  ASN A CA  1 
ATOM   3342 C  C   . ASN A 1 456 ? 77.990  39.089 107.848 1.00 28.19 ? 456  ASN A C   1 
ATOM   3343 O  O   . ASN A 1 456 ? 78.636  40.081 107.489 1.00 29.29 ? 456  ASN A O   1 
ATOM   3344 C  CB  . ASN A 1 456 ? 79.593  38.361 109.619 1.00 31.53 ? 456  ASN A CB  1 
ATOM   3345 C  CG  . ASN A 1 456 ? 79.815  38.152 111.104 1.00 35.32 ? 456  ASN A CG  1 
ATOM   3346 O  OD1 . ASN A 1 456 ? 79.075  38.683 111.945 1.00 40.33 ? 456  ASN A OD1 1 
ATOM   3347 N  ND2 . ASN A 1 456 ? 80.823  37.353 111.436 1.00 44.83 ? 456  ASN A ND2 1 
ATOM   3348 N  N   . PHE A 1 457 ? 77.158  38.447 107.037 1.00 23.37 ? 457  PHE A N   1 
ATOM   3349 C  CA  . PHE A 1 457 ? 77.003  38.805 105.631 1.00 24.48 ? 457  PHE A CA  1 
ATOM   3350 C  C   . PHE A 1 457 ? 75.532  38.947 105.265 1.00 20.57 ? 457  PHE A C   1 
ATOM   3351 O  O   . PHE A 1 457 ? 74.660  38.337 105.879 1.00 21.27 ? 457  PHE A O   1 
ATOM   3352 C  CB  . PHE A 1 457 ? 77.650  37.758 104.723 1.00 32.20 ? 457  PHE A CB  1 
ATOM   3353 C  CG  . PHE A 1 457 ? 79.073  37.456 105.077 1.00 37.98 ? 457  PHE A CG  1 
ATOM   3354 C  CD1 . PHE A 1 457 ? 80.092  38.309 104.676 1.00 40.48 ? 457  PHE A CD1 1 
ATOM   3355 C  CD2 . PHE A 1 457 ? 79.387  36.362 105.866 1.00 35.75 ? 457  PHE A CD2 1 
ATOM   3356 C  CE1 . PHE A 1 457 ? 81.410  38.045 105.016 1.00 40.57 ? 457  PHE A CE1 1 
ATOM   3357 C  CE2 . PHE A 1 457 ? 80.702  36.095 106.212 1.00 38.86 ? 457  PHE A CE2 1 
ATOM   3358 C  CZ  . PHE A 1 457 ? 81.711  36.941 105.786 1.00 41.71 ? 457  PHE A CZ  1 
ATOM   3359 N  N   . ALA A 1 458 ? 75.264  39.761 104.246 1.00 19.94 ? 458  ALA A N   1 
ATOM   3360 C  CA  . ALA A 1 458 ? 73.897  39.921 103.756 1.00 17.99 ? 458  ALA A CA  1 
ATOM   3361 C  C   . ALA A 1 458 ? 73.452  38.683 102.991 1.00 19.48 ? 458  ALA A C   1 
ATOM   3362 O  O   . ALA A 1 458 ? 74.252  38.025 102.324 1.00 19.53 ? 458  ALA A O   1 
ATOM   3363 C  CB  . ALA A 1 458 ? 73.800  41.130 102.816 1.00 21.24 ? 458  ALA A CB  1 
ATOM   3364 N  N   . HIS A 1 459 ? 72.154  38.369 103.078 1.00 16.91 ? 459  HIS A N   1 
ATOM   3365 C  CA  . HIS A 1 459 ? 71.570  37.279 102.283 1.00 16.14 ? 459  HIS A CA  1 
ATOM   3366 C  C   . HIS A 1 459 ? 70.392  37.824 101.488 1.00 15.99 ? 459  HIS A C   1 
ATOM   3367 O  O   . HIS A 1 459 ? 69.484  38.441 102.072 1.00 16.92 ? 459  HIS A O   1 
ATOM   3368 C  CB  . HIS A 1 459 ? 71.059  36.171 103.192 1.00 16.32 ? 459  HIS A CB  1 
ATOM   3369 C  CG  . HIS A 1 459 ? 72.137  35.548 104.007 1.00 16.64 ? 459  HIS A CG  1 
ATOM   3370 N  ND1 . HIS A 1 459 ? 72.933  34.517 103.550 1.00 16.18 ? 459  HIS A ND1 1 
ATOM   3371 C  CD2 . HIS A 1 459 ? 72.584  35.854 105.244 1.00 18.58 ? 459  HIS A CD2 1 
ATOM   3372 C  CE1 . HIS A 1 459 ? 73.814  34.210 104.480 1.00 16.72 ? 459  HIS A CE1 1 
ATOM   3373 N  NE2 . HIS A 1 459 ? 73.627  35.008 105.516 1.00 18.41 ? 459  HIS A NE2 1 
ATOM   3374 N  N   . PRO A 1 460 ? 70.381  37.655 100.173 1.00 15.29 ? 460  PRO A N   1 
ATOM   3375 C  CA  . PRO A 1 460 ? 69.216  38.049 99.379  1.00 15.15 ? 460  PRO A CA  1 
ATOM   3376 C  C   . PRO A 1 460 ? 68.138  36.979 99.419  1.00 15.54 ? 460  PRO A C   1 
ATOM   3377 O  O   . PRO A 1 460 ? 68.213  35.969 98.708  1.00 16.57 ? 460  PRO A O   1 
ATOM   3378 C  CB  . PRO A 1 460 ? 69.810  38.202 97.975  1.00 14.68 ? 460  PRO A CB  1 
ATOM   3379 C  CG  . PRO A 1 460 ? 70.934  37.168 97.942  1.00 14.56 ? 460  PRO A CG  1 
ATOM   3380 C  CD  . PRO A 1 460 ? 71.480  37.093 99.363  1.00 14.79 ? 460  PRO A CD  1 
ATOM   3381 N  N   . ILE A 1 461 ? 67.096  37.202 100.213 1.00 15.47 ? 461  ILE A N   1 
ATOM   3382 C  CA  . ILE A 1 461 ? 66.068  36.189 100.430 1.00 15.49 ? 461  ILE A CA  1 
ATOM   3383 C  C   . ILE A 1 461 ? 64.977  36.360 99.378  1.00 15.35 ? 461  ILE A C   1 
ATOM   3384 O  O   . ILE A 1 461 ? 64.448  37.466 99.187  1.00 15.65 ? 461  ILE A O   1 
ATOM   3385 C  CB  . ILE A 1 461 ? 65.487  36.316 101.845 1.00 16.54 ? 461  ILE A CB  1 
ATOM   3386 C  CG1 . ILE A 1 461 ? 66.561  36.135 102.906 1.00 16.97 ? 461  ILE A CG1 1 
ATOM   3387 C  CG2 . ILE A 1 461 ? 64.384  35.293 102.024 1.00 17.27 ? 461  ILE A CG2 1 
ATOM   3388 C  CD1 . ILE A 1 461 ? 67.319  34.834 102.786 1.00 17.44 ? 461  ILE A CD1 1 
ATOM   3389 N  N   . HIS A 1 462 ? 64.649  35.269 98.676  1.00 15.00 ? 462  HIS A N   1 
ATOM   3390 C  CA  . HIS A 1 462 ? 63.636  35.243 97.633  1.00 14.96 ? 462  HIS A CA  1 
ATOM   3391 C  C   . HIS A 1 462 ? 62.452  34.420 98.126  1.00 15.74 ? 462  HIS A C   1 
ATOM   3392 O  O   . HIS A 1 462 ? 62.622  33.291 98.597  1.00 15.60 ? 462  HIS A O   1 
ATOM   3393 C  CB  . HIS A 1 462 ? 64.226  34.645 96.340  1.00 14.40 ? 462  HIS A CB  1 
ATOM   3394 C  CG  . HIS A 1 462 ? 63.223  34.388 95.254  1.00 14.47 ? 462  HIS A CG  1 
ATOM   3395 N  ND1 . HIS A 1 462 ? 62.288  35.324 94.864  1.00 14.83 ? 462  HIS A ND1 1 
ATOM   3396 C  CD2 . HIS A 1 462 ? 63.068  33.332 94.410  1.00 14.49 ? 462  HIS A CD2 1 
ATOM   3397 C  CE1 . HIS A 1 462 ? 61.561  34.836 93.871  1.00 16.00 ? 462  HIS A CE1 1 
ATOM   3398 N  NE2 . HIS A 1 462 ? 62.019  33.629 93.572  1.00 18.11 ? 462  HIS A NE2 1 
ATOM   3399 N  N   . ILE A 1 463 ? 61.256  34.986 98.034  1.00 15.79 ? 463  ILE A N   1 
ATOM   3400 C  CA  . ILE A 1 463 ? 60.017  34.285 98.352  1.00 16.27 ? 463  ILE A CA  1 
ATOM   3401 C  C   . ILE A 1 463 ? 59.280  34.071 97.042  1.00 16.24 ? 463  ILE A C   1 
ATOM   3402 O  O   . ILE A 1 463 ? 59.112  35.015 96.263  1.00 16.40 ? 463  ILE A O   1 
ATOM   3403 C  CB  . ILE A 1 463 ? 59.146  35.098 99.325  1.00 17.01 ? 463  ILE A CB  1 
ATOM   3404 C  CG1 . ILE A 1 463 ? 59.908  35.384 100.615 1.00 17.58 ? 463  ILE A CG1 1 
ATOM   3405 C  CG2 . ILE A 1 463 ? 57.832  34.355 99.631  1.00 19.24 ? 463  ILE A CG2 1 
ATOM   3406 C  CD1 . ILE A 1 463 ? 59.157  36.340 101.560 1.00 19.96 ? 463  ILE A CD1 1 
ATOM   3407 N  N   . HIS A 1 464 ? 58.890  32.833 96.773  1.00 15.48 ? 464  HIS A N   1 
ATOM   3408 C  CA  . HIS A 1 464 ? 58.200  32.555 95.520  1.00 16.25 ? 464  HIS A CA  1 
ATOM   3409 C  C   . HIS A 1 464 ? 56.745  33.018 95.605  1.00 16.99 ? 464  HIS A C   1 
ATOM   3410 O  O   . HIS A 1 464 ? 56.263  33.448 96.651  1.00 18.18 ? 464  HIS A O   1 
ATOM   3411 C  CB  . HIS A 1 464 ? 58.239  31.062 95.189  1.00 16.59 ? 464  HIS A CB  1 
ATOM   3412 C  CG  . HIS A 1 464 ? 59.583  30.576 94.737  1.00 15.46 ? 464  HIS A CG  1 
ATOM   3413 N  ND1 . HIS A 1 464 ? 59.737  29.574 93.797  1.00 17.48 ? 464  HIS A ND1 1 
ATOM   3414 C  CD2 . HIS A 1 464 ? 60.830  30.893 95.162  1.00 15.45 ? 464  HIS A CD2 1 
ATOM   3415 C  CE1 . HIS A 1 464 ? 61.032  29.338 93.625  1.00 18.02 ? 464  HIS A CE1 1 
ATOM   3416 N  NE2 . HIS A 1 464 ? 61.713  30.127 94.439  1.00 15.62 ? 464  HIS A NE2 1 
ATOM   3417 N  N   . LEU A 1 465 ? 56.099  33.018 94.441  1.00 15.91 ? 465  LEU A N   1 
ATOM   3418 C  CA  . LEU A 1 465 ? 54.674  33.246 94.157  1.00 16.12 ? 465  LEU A CA  1 
ATOM   3419 C  C   . LEU A 1 465 ? 54.189  34.683 94.377  1.00 18.91 ? 465  LEU A C   1 
ATOM   3420 O  O   . LEU A 1 465 ? 53.519  35.233 93.489  1.00 19.09 ? 465  LEU A O   1 
ATOM   3421 C  CB  . LEU A 1 465 ? 53.798  32.290 94.989  1.00 18.35 ? 465  LEU A CB  1 
ATOM   3422 C  CG  . LEU A 1 465 ? 52.295  32.570 94.869  1.00 19.59 ? 465  LEU A CG  1 
ATOM   3423 C  CD1 . LEU A 1 465 ? 51.836  32.174 93.475  1.00 21.29 ? 465  LEU A CD1 1 
ATOM   3424 C  CD2 . LEU A 1 465 ? 51.530  31.791 95.934  1.00 22.02 ? 465  LEU A CD2 1 
ATOM   3425 N  N   . ILE A 1 466 ? 54.706  35.390 95.379  1.00 18.26 ? 466  ILE A N   1 
ATOM   3426 C  CA  . ILE A 1 466 ? 54.171  36.699 95.743  1.00 18.24 ? 466  ILE A CA  1 
ATOM   3427 C  C   . ILE A 1 466 ? 55.203  37.783 95.441  1.00 18.02 ? 466  ILE A C   1 
ATOM   3428 O  O   . ILE A 1 466 ? 56.350  37.512 95.092  1.00 18.40 ? 466  ILE A O   1 
ATOM   3429 C  CB  . ILE A 1 466 ? 53.678  36.772 97.211  1.00 20.48 ? 466  ILE A CB  1 
ATOM   3430 C  CG1 . ILE A 1 466 ? 54.740  36.242 98.163  1.00 21.60 ? 466  ILE A CG1 1 
ATOM   3431 C  CG2 . ILE A 1 466 ? 52.405  35.940 97.391  1.00 22.96 ? 466  ILE A CG2 1 
ATOM   3432 C  CD1 . ILE A 1 466 ? 55.854  37.250 98.506  1.00 19.03 ? 466  ILE A CD1 1 
ATOM   3433 N  N   . GLN A 1 467 ? 54.771  39.035 95.597  1.00 19.17 ? 467  GLN A N   1 
ATOM   3434 C  CA  . GLN A 1 467 ? 55.658  40.183 95.704  1.00 18.36 ? 467  GLN A CA  1 
ATOM   3435 C  C   . GLN A 1 467 ? 55.397  40.839 97.055  1.00 17.75 ? 467  GLN A C   1 
ATOM   3436 O  O   . GLN A 1 467 ? 54.298  40.735 97.610  1.00 21.34 ? 467  GLN A O   1 
ATOM   3437 C  CB  . GLN A 1 467 ? 55.428  41.183 94.555  1.00 18.43 ? 467  GLN A CB  1 
ATOM   3438 C  CG  . GLN A 1 467 ? 55.655  40.605 93.154  1.00 17.32 ? 467  GLN A CG  1 
ATOM   3439 C  CD  . GLN A 1 467 ? 57.125  40.389 92.829  1.00 18.17 ? 467  GLN A CD  1 
ATOM   3440 O  OE1 . GLN A 1 467 ? 57.981  41.186 93.231  1.00 18.24 ? 467  GLN A OE1 1 
ATOM   3441 N  NE2 . GLN A 1 467 ? 57.432  39.318 92.088  1.00 19.83 ? 467  GLN A NE2 1 
ATOM   3442 N  N   . PHE A 1 468 ? 56.433  41.450 97.620  1.00 17.09 ? 468  PHE A N   1 
ATOM   3443 C  CA  . PHE A 1 468 ? 56.312  42.067 98.931  1.00 17.11 ? 468  PHE A CA  1 
ATOM   3444 C  C   . PHE A 1 468 ? 56.830  43.500 98.891  1.00 18.66 ? 468  PHE A C   1 
ATOM   3445 O  O   . PHE A 1 468 ? 57.481  43.925 97.934  1.00 18.76 ? 468  PHE A O   1 
ATOM   3446 C  CB  . PHE A 1 468 ? 57.045  41.239 100.007 1.00 18.01 ? 468  PHE A CB  1 
ATOM   3447 C  CG  . PHE A 1 468 ? 58.485  40.911 99.664  1.00 15.05 ? 468  PHE A CG  1 
ATOM   3448 C  CD1 . PHE A 1 468 ? 59.458  41.903 99.695  1.00 16.15 ? 468  PHE A CD1 1 
ATOM   3449 C  CD2 . PHE A 1 468 ? 58.868  39.621 99.341  1.00 16.20 ? 468  PHE A CD2 1 
ATOM   3450 C  CE1 . PHE A 1 468 ? 60.781  41.633 99.387  1.00 16.55 ? 468  PHE A CE1 1 
ATOM   3451 C  CE2 . PHE A 1 468 ? 60.196  39.342 99.042  1.00 17.56 ? 468  PHE A CE2 1 
ATOM   3452 C  CZ  . PHE A 1 468 ? 61.146  40.358 99.065  1.00 17.02 ? 468  PHE A CZ  1 
ATOM   3453 N  N   . LYS A 1 469 ? 56.545  44.242 99.954  1.00 18.68 ? 469  LYS A N   1 
ATOM   3454 C  CA  . LYS A 1 469 ? 57.145  45.547 100.196 1.00 19.13 ? 469  LYS A CA  1 
ATOM   3455 C  C   . LYS A 1 469 ? 58.066  45.439 101.401 1.00 21.40 ? 469  LYS A C   1 
ATOM   3456 O  O   . LYS A 1 469 ? 57.719  44.793 102.404 1.00 19.66 ? 469  LYS A O   1 
ATOM   3457 C  CB  . LYS A 1 469 ? 56.068  46.596 100.482 1.00 21.07 ? 469  LYS A CB  1 
ATOM   3458 C  CG  . LYS A 1 469 ? 55.213  46.958 99.283  1.00 25.98 ? 469  LYS A CG  1 
ATOM   3459 C  CD  . LYS A 1 469 ? 56.017  47.688 98.239  1.00 27.50 ? 469  LYS A CD  1 
ATOM   3460 C  CE  . LYS A 1 469 ? 55.111  48.425 97.252  1.00 22.40 ? 469  LYS A CE  1 
ATOM   3461 N  NZ  . LYS A 1 469 ? 55.226  49.884 97.471  1.00 35.38 ? 469  LYS A NZ  1 
ATOM   3462 N  N   . ILE A 1 470 ? 59.237  46.065 101.304 1.00 18.19 ? 470  ILE A N   1 
ATOM   3463 C  CA  . ILE A 1 470 ? 60.144  46.154 102.445 1.00 19.92 ? 470  ILE A CA  1 
ATOM   3464 C  C   . ILE A 1 470 ? 59.576  47.180 103.418 1.00 20.87 ? 470  ILE A C   1 
ATOM   3465 O  O   . ILE A 1 470 ? 59.336  48.341 103.055 1.00 22.65 ? 470  ILE A O   1 
ATOM   3466 C  CB  . ILE A 1 470 ? 61.554  46.555 101.995 1.00 18.79 ? 470  ILE A CB  1 
ATOM   3467 C  CG1 . ILE A 1 470 ? 62.106  45.533 100.995 1.00 18.27 ? 470  ILE A CG1 1 
ATOM   3468 C  CG2 . ILE A 1 470 ? 62.485  46.612 103.213 1.00 21.65 ? 470  ILE A CG2 1 
ATOM   3469 C  CD1 . ILE A 1 470 ? 63.415  45.950 100.342 1.00 18.06 ? 470  ILE A CD1 1 
ATOM   3470 N  N   . LEU A 1 471 ? 59.352  46.756 104.663 1.00 22.48 ? 471  LEU A N   1 
ATOM   3471 C  CA  . LEU A 1 471 ? 58.855  47.684 105.669 1.00 21.78 ? 471  LEU A CA  1 
ATOM   3472 C  C   . LEU A 1 471 ? 59.998  48.480 106.271 1.00 20.25 ? 471  LEU A C   1 
ATOM   3473 O  O   . LEU A 1 471 ? 59.939  49.720 106.331 1.00 24.06 ? 471  LEU A O   1 
ATOM   3474 C  CB  . LEU A 1 471 ? 58.137  46.916 106.780 1.00 22.94 ? 471  LEU A CB  1 
ATOM   3475 C  CG  . LEU A 1 471 ? 56.796  46.289 106.418 1.00 24.28 ? 471  LEU A CG  1 
ATOM   3476 C  CD1 . LEU A 1 471 ? 56.340  45.383 107.570 1.00 27.43 ? 471  LEU A CD1 1 
ATOM   3477 C  CD2 . LEU A 1 471 ? 55.764  47.350 106.124 1.00 26.89 ? 471  LEU A CD2 1 
ATOM   3478 N  N   . HIS A 1 472 ? 61.033  47.784 106.739 1.00 21.57 ? 472  HIS A N   1 
ATOM   3479 C  CA  . HIS A 1 472 ? 62.117  48.495 107.432 1.00 21.07 ? 472  HIS A CA  1 
ATOM   3480 C  C   . HIS A 1 472 ? 63.185  47.488 107.827 1.00 20.43 ? 472  HIS A C   1 
ATOM   3481 O  O   . HIS A 1 472 ? 62.973  46.277 107.744 1.00 21.97 ? 472  HIS A O   1 
ATOM   3482 C  CB  . HIS A 1 472 ? 61.654  49.258 108.695 1.00 24.60 ? 472  HIS A CB  1 
ATOM   3483 C  CG  . HIS A 1 472 ? 60.590  48.554 109.482 1.00 25.77 ? 472  HIS A CG  1 
ATOM   3484 N  ND1 . HIS A 1 472 ? 60.808  47.368 110.152 1.00 25.58 ? 472  HIS A ND1 1 
ATOM   3485 C  CD2 . HIS A 1 472 ? 59.285  48.864 109.680 1.00 26.72 ? 472  HIS A CD2 1 
ATOM   3486 C  CE1 . HIS A 1 472 ? 59.686  46.981 110.734 1.00 27.73 ? 472  HIS A CE1 1 
ATOM   3487 N  NE2 . HIS A 1 472 ? 58.748  47.873 110.468 1.00 27.82 ? 472  HIS A NE2 1 
ATOM   3488 N  N   . ARG A 1 473 ? 64.345  47.999 108.246 1.00 20.99 ? 473  ARG A N   1 
ATOM   3489 C  CA  . ARG A 1 473 ? 65.389  47.177 108.859 1.00 21.41 ? 473  ARG A CA  1 
ATOM   3490 C  C   . ARG A 1 473 ? 65.799  47.799 110.190 1.00 22.06 ? 473  ARG A C   1 
ATOM   3491 O  O   . ARG A 1 473 ? 65.964  49.022 110.291 1.00 23.60 ? 473  ARG A O   1 
ATOM   3492 C  CB  . ARG A 1 473 ? 66.624  47.062 107.951 1.00 20.85 ? 473  ARG A CB  1 
ATOM   3493 C  CG  . ARG A 1 473 ? 66.328  46.469 106.577 1.00 20.06 ? 473  ARG A CG  1 
ATOM   3494 C  CD  . ARG A 1 473 ? 67.611  46.334 105.789 1.00 19.85 ? 473  ARG A CD  1 
ATOM   3495 N  NE  . ARG A 1 473 ? 67.406  45.717 104.479 1.00 18.95 ? 473  ARG A NE  1 
ATOM   3496 C  CZ  . ARG A 1 473 ? 67.121  46.403 103.378 1.00 18.70 ? 473  ARG A CZ  1 
ATOM   3497 N  NH1 . ARG A 1 473 ? 66.889  47.705 103.417 1.00 19.28 ? 473  ARG A NH1 1 
ATOM   3498 N  NH2 . ARG A 1 473 ? 67.043  45.762 102.215 1.00 17.93 ? 473  ARG A NH2 1 
ATOM   3499 N  N   . THR A 1 474 ? 65.979  46.957 111.207 1.00 22.12 ? 474  THR A N   1 
ATOM   3500 C  CA  . THR A 1 474 ? 66.261  47.440 112.563 1.00 25.17 ? 474  THR A CA  1 
ATOM   3501 C  C   . THR A 1 474 ? 67.494  46.728 113.103 1.00 23.32 ? 474  THR A C   1 
ATOM   3502 O  O   . THR A 1 474 ? 67.519  45.482 113.126 1.00 22.72 ? 474  THR A O   1 
ATOM   3503 C  CB  . THR A 1 474 ? 65.043  47.220 113.469 1.00 27.43 ? 474  THR A CB  1 
ATOM   3504 O  OG1 . THR A 1 474 ? 63.853  47.655 112.791 1.00 27.70 ? 474  THR A OG1 1 
ATOM   3505 C  CG2 . THR A 1 474 ? 65.169  48.025 114.770 1.00 24.28 ? 474  THR A CG2 1 
ATOM   3506 N  N   . PRO A 1 475 ? 68.530  47.450 113.532 1.00 24.29 ? 475  PRO A N   1 
ATOM   3507 C  CA  . PRO A 1 475 ? 69.728  46.785 114.051 1.00 24.66 ? 475  PRO A CA  1 
ATOM   3508 C  C   . PRO A 1 475 ? 69.472  46.182 115.423 1.00 24.90 ? 475  PRO A C   1 
ATOM   3509 O  O   . PRO A 1 475 ? 68.690  46.708 116.226 1.00 25.26 ? 475  PRO A O   1 
ATOM   3510 C  CB  . PRO A 1 475 ? 70.742  47.926 114.150 1.00 26.06 ? 475  PRO A CB  1 
ATOM   3511 C  CG  . PRO A 1 475 ? 69.897  49.140 114.443 1.00 28.46 ? 475  PRO A CG  1 
ATOM   3512 C  CD  . PRO A 1 475 ? 68.591  48.921 113.705 1.00 25.29 ? 475  PRO A CD  1 
ATOM   3513 N  N   . PHE A 1 476 ? 70.168  45.077 115.695 1.00 24.80 ? 476  PHE A N   1 
ATOM   3514 C  CA  . PHE A 1 476 ? 70.092  44.428 116.997 1.00 25.10 ? 476  PHE A CA  1 
ATOM   3515 C  C   . PHE A 1 476 ? 71.487  44.016 117.450 1.00 25.84 ? 476  PHE A C   1 
ATOM   3516 O  O   . PHE A 1 476 ? 72.434  43.962 116.666 1.00 26.18 ? 476  PHE A O   1 
ATOM   3517 C  CB  . PHE A 1 476 ? 69.095  43.249 117.007 1.00 24.19 ? 476  PHE A CB  1 
ATOM   3518 C  CG  . PHE A 1 476 ? 69.541  42.058 116.202 1.00 23.59 ? 476  PHE A CG  1 
ATOM   3519 C  CD1 . PHE A 1 476 ? 69.304  42.001 114.836 1.00 23.00 ? 476  PHE A CD1 1 
ATOM   3520 C  CD2 . PHE A 1 476 ? 70.193  40.991 116.809 1.00 23.85 ? 476  PHE A CD2 1 
ATOM   3521 C  CE1 . PHE A 1 476 ? 69.717  40.904 114.090 1.00 22.38 ? 476  PHE A CE1 1 
ATOM   3522 C  CE2 . PHE A 1 476 ? 70.601  39.885 116.079 1.00 23.46 ? 476  PHE A CE2 1 
ATOM   3523 C  CZ  . PHE A 1 476 ? 70.364  39.839 114.714 1.00 22.73 ? 476  PHE A CZ  1 
ATOM   3524 N  N   . ASP A 1 477 ? 71.594  43.718 118.739 1.00 26.41 ? 477  ASP A N   1 
ATOM   3525 C  CA  . ASP A 1 477 ? 72.857  43.344 119.373 1.00 27.29 ? 477  ASP A CA  1 
ATOM   3526 C  C   . ASP A 1 477 ? 73.157  41.881 119.052 1.00 27.83 ? 477  ASP A C   1 
ATOM   3527 O  O   . ASP A 1 477 ? 72.550  40.969 119.624 1.00 26.42 ? 477  ASP A O   1 
ATOM   3528 C  CB  . ASP A 1 477 ? 72.721  43.546 120.878 1.00 28.04 ? 477  ASP A CB  1 
ATOM   3529 C  CG  . ASP A 1 477 ? 74.029  43.333 121.640 1.00 29.17 ? 477  ASP A CG  1 
ATOM   3530 O  OD1 . ASP A 1 477 ? 74.858  42.494 121.222 1.00 34.00 ? 477  ASP A OD1 1 
ATOM   3531 O  OD2 . ASP A 1 477 ? 74.212  43.974 122.700 1.00 30.14 ? 477  ASP A OD2 1 
ATOM   3532 N  N   . LEU A 1 478 ? 74.136  41.656 118.173 1.00 26.95 ? 478  LEU A N   1 
ATOM   3533 C  CA  . LEU A 1 478 ? 74.441  40.304 117.712 1.00 30.62 ? 478  LEU A CA  1 
ATOM   3534 C  C   . LEU A 1 478 ? 74.957  39.416 118.842 1.00 29.55 ? 478  LEU A C   1 
ATOM   3535 O  O   . LEU A 1 478 ? 74.534  38.259 118.970 1.00 29.53 ? 478  LEU A O   1 
ATOM   3536 C  CB  . LEU A 1 478 ? 75.440  40.385 116.552 1.00 35.12 ? 478  LEU A CB  1 
ATOM   3537 C  CG  . LEU A 1 478 ? 74.947  39.942 115.175 1.00 47.01 ? 478  LEU A CG  1 
ATOM   3538 C  CD1 . LEU A 1 478 ? 76.111  39.703 114.223 1.00 43.26 ? 478  LEU A CD1 1 
ATOM   3539 C  CD2 . LEU A 1 478 ? 74.129  38.669 115.309 1.00 40.72 ? 478  LEU A CD2 1 
ATOM   3540 N  N   . GLU A 1 479 ? 75.865  39.925 119.679 1.00 30.99 ? 479  GLU A N   1 
ATOM   3541 C  CA  . GLU A 1 479 ? 76.392  39.085 120.753 1.00 33.37 ? 479  GLU A CA  1 
ATOM   3542 C  C   . GLU A 1 479 ? 75.300  38.687 121.741 1.00 29.56 ? 479  GLU A C   1 
ATOM   3543 O  O   . GLU A 1 479 ? 75.256  37.543 122.206 1.00 29.77 ? 479  GLU A O   1 
ATOM   3544 C  CB  . GLU A 1 479 ? 77.558  39.768 121.474 1.00 46.61 ? 479  GLU A CB  1 
ATOM   3545 C  CG  . GLU A 1 479 ? 78.923  39.546 120.814 1.00 48.77 ? 479  GLU A CG  1 
ATOM   3546 C  CD  . GLU A 1 479 ? 80.033  40.380 121.448 1.00 57.26 ? 479  GLU A CD  1 
ATOM   3547 O  OE1 . GLU A 1 479 ? 79.883  40.789 122.625 1.00 56.53 ? 479  GLU A OE1 1 
ATOM   3548 O  OE2 . GLU A 1 479 ? 81.059  40.620 120.765 1.00 60.80 ? 479  GLU A OE2 1 
ATOM   3549 N  N   . ARG A 1 480 ? 74.399  39.617 122.073 1.00 28.45 ? 480  ARG A N   1 
ATOM   3550 C  CA  . ARG A 1 480 ? 73.321  39.266 122.991 1.00 28.10 ? 480  ARG A CA  1 
ATOM   3551 C  C   . ARG A 1 480 ? 72.423  38.181 122.394 1.00 27.06 ? 480  ARG A C   1 
ATOM   3552 O  O   . ARG A 1 480 ? 72.024  37.231 123.092 1.00 27.03 ? 480  ARG A O   1 
ATOM   3553 C  CB  . ARG A 1 480 ? 72.517  40.515 123.343 1.00 28.09 ? 480  ARG A CB  1 
ATOM   3554 C  CG  . ARG A 1 480 ? 71.276  40.256 124.164 1.00 27.74 ? 480  ARG A CG  1 
ATOM   3555 C  CD  . ARG A 1 480 ? 71.605  39.491 125.431 1.00 28.36 ? 480  ARG A CD  1 
ATOM   3556 N  NE  . ARG A 1 480 ? 70.400  38.999 126.083 1.00 27.96 ? 480  ARG A NE  1 
ATOM   3557 C  CZ  . ARG A 1 480 ? 69.740  39.666 127.023 1.00 28.31 ? 480  ARG A CZ  1 
ATOM   3558 N  NH1 . ARG A 1 480 ? 70.120  40.877 127.411 1.00 29.04 ? 480  ARG A NH1 1 
ATOM   3559 N  NH2 . ARG A 1 480 ? 68.657  39.119 127.565 1.00 28.01 ? 480  ARG A NH2 1 
ATOM   3560 N  N   . PHE A 1 481 ? 72.093  38.298 121.101 1.00 26.28 ? 481  PHE A N   1 
ATOM   3561 C  CA  . PHE A 1 481 ? 71.300  37.245 120.487 1.00 25.42 ? 481  PHE A CA  1 
ATOM   3562 C  C   . PHE A 1 481 ? 72.028  35.919 120.547 1.00 28.82 ? 481  PHE A C   1 
ATOM   3563 O  O   . PHE A 1 481 ? 71.425  34.881 120.851 1.00 28.55 ? 481  PHE A O   1 
ATOM   3564 C  CB  . PHE A 1 481 ? 71.023  37.558 119.028 1.00 24.64 ? 481  PHE A CB  1 
ATOM   3565 C  CG  . PHE A 1 481 ? 70.043  36.608 118.413 1.00 27.33 ? 481  PHE A CG  1 
ATOM   3566 C  CD1 . PHE A 1 481 ? 68.688  36.836 118.529 1.00 24.35 ? 481  PHE A CD1 1 
ATOM   3567 C  CD2 . PHE A 1 481 ? 70.473  35.445 117.794 1.00 31.15 ? 481  PHE A CD2 1 
ATOM   3568 C  CE1 . PHE A 1 481 ? 67.763  35.946 117.987 1.00 31.62 ? 481  PHE A CE1 1 
ATOM   3569 C  CE2 . PHE A 1 481 ? 69.559  34.544 117.260 1.00 35.03 ? 481  PHE A CE2 1 
ATOM   3570 C  CZ  . PHE A 1 481 ? 68.197  34.818 117.335 1.00 28.85 ? 481  PHE A CZ  1 
ATOM   3571 N  N   . GLN A 1 482 ? 73.328  35.935 120.263 1.00 26.42 ? 482  GLN A N   1 
ATOM   3572 C  CA  . GLN A 1 482 ? 74.103  34.705 120.335 1.00 29.10 ? 482  GLN A CA  1 
ATOM   3573 C  C   . GLN A 1 482 ? 74.052  34.089 121.727 1.00 30.42 ? 482  GLN A C   1 
ATOM   3574 O  O   . GLN A 1 482 ? 74.088  32.859 121.860 1.00 35.04 ? 482  GLN A O   1 
ATOM   3575 C  CB  . GLN A 1 482 ? 75.543  34.965 119.884 1.00 33.53 ? 482  GLN A CB  1 
ATOM   3576 C  CG  . GLN A 1 482 ? 75.679  35.196 118.368 1.00 34.49 ? 482  GLN A CG  1 
ATOM   3577 C  CD  . GLN A 1 482 ? 76.987  35.882 117.969 1.00 38.02 ? 482  GLN A CD  1 
ATOM   3578 O  OE1 . GLN A 1 482 ? 77.807  36.239 118.823 1.00 53.62 ? 482  GLN A OE1 1 
ATOM   3579 N  NE2 . GLN A 1 482 ? 77.183  36.070 116.657 1.00 45.08 ? 482  GLN A NE2 1 
ATOM   3580 N  N   . GLN A 1 483 ? 73.963  34.920 122.769 1.00 27.96 ? 483  GLN A N   1 
ATOM   3581 C  CA  . GLN A 1 483 ? 73.931  34.392 124.133 1.00 28.57 ? 483  GLN A CA  1 
ATOM   3582 C  C   . GLN A 1 483 ? 72.604  33.712 124.446 1.00 27.90 ? 483  GLN A C   1 
ATOM   3583 O  O   . GLN A 1 483 ? 72.577  32.570 124.931 1.00 28.20 ? 483  GLN A O   1 
ATOM   3584 C  CB  . GLN A 1 483 ? 74.218  35.505 125.143 1.00 29.25 ? 483  GLN A CB  1 
ATOM   3585 C  CG  . GLN A 1 483 ? 74.648  35.003 126.536 1.00 31.66 ? 483  GLN A CG  1 
ATOM   3586 C  CD  . GLN A 1 483 ? 74.148  35.859 127.698 1.00 30.46 ? 483  GLN A CD  1 
ATOM   3587 O  OE1 . GLN A 1 483 ? 73.632  35.344 128.724 1.00 30.59 ? 483  GLN A OE1 1 
ATOM   3588 N  NE2 . GLN A 1 483 ? 74.290  37.174 127.548 1.00 33.53 ? 483  GLN A NE2 1 
ATOM   3589 N  N   . ASP A 1 484 ? 71.489  34.398 124.230 1.00 27.14 ? 484  ASP A N   1 
ATOM   3590 C  CA  . ASP A 1 484 ? 70.245  33.802 124.705 1.00 26.75 ? 484  ASP A CA  1 
ATOM   3591 C  C   . ASP A 1 484 ? 69.048  33.969 123.780 1.00 31.50 ? 484  ASP A C   1 
ATOM   3592 O  O   . ASP A 1 484 ? 67.915  33.685 124.195 1.00 27.84 ? 484  ASP A O   1 
ATOM   3593 C  CB  . ASP A 1 484 ? 69.950  34.243 126.156 1.00 27.29 ? 484  ASP A CB  1 
ATOM   3594 C  CG  . ASP A 1 484 ? 69.509  35.703 126.255 1.00 27.18 ? 484  ASP A CG  1 
ATOM   3595 O  OD1 . ASP A 1 484 ? 69.632  36.446 125.258 1.00 26.80 ? 484  ASP A OD1 1 
ATOM   3596 O  OD2 . ASP A 1 484 ? 69.076  36.117 127.346 1.00 27.57 ? 484  ASP A OD2 1 
ATOM   3597 N  N   . GLY A 1 485 ? 69.256  34.430 122.552 1.00 25.51 ? 485  GLY A N   1 
ATOM   3598 C  CA  . GLY A 1 485 ? 68.184  34.550 121.597 1.00 30.28 ? 485  GLY A CA  1 
ATOM   3599 C  C   . GLY A 1 485 ? 67.313  35.770 121.763 1.00 28.66 ? 485  GLY A C   1 
ATOM   3600 O  O   . GLY A 1 485 ? 66.338  35.921 121.014 1.00 32.42 ? 485  GLY A O   1 
ATOM   3601 N  N   . TYR A 1 486 ? 67.611  36.651 122.721 1.00 24.83 ? 486  TYR A N   1 
ATOM   3602 C  CA  . TYR A 1 486 ? 66.837  37.872 122.875 1.00 24.81 ? 486  TYR A CA  1 
ATOM   3603 C  C   . TYR A 1 486 ? 67.238  38.865 121.794 1.00 26.37 ? 486  TYR A C   1 
ATOM   3604 O  O   . TYR A 1 486 ? 68.435  39.047 121.540 1.00 24.90 ? 486  TYR A O   1 
ATOM   3605 C  CB  . TYR A 1 486 ? 67.088  38.489 124.255 1.00 25.66 ? 486  TYR A CB  1 
ATOM   3606 C  CG  . TYR A 1 486 ? 66.344  39.783 124.443 1.00 25.84 ? 486  TYR A CG  1 
ATOM   3607 C  CD1 . TYR A 1 486 ? 64.950  39.796 124.536 1.00 29.10 ? 486  TYR A CD1 1 
ATOM   3608 C  CD2 . TYR A 1 486 ? 67.021  40.999 124.558 1.00 26.44 ? 486  TYR A CD2 1 
ATOM   3609 C  CE1 . TYR A 1 486 ? 64.256  40.973 124.717 1.00 28.11 ? 486  TYR A CE1 1 
ATOM   3610 C  CE2 . TYR A 1 486 ? 66.332  42.180 124.734 1.00 26.76 ? 486  TYR A CE2 1 
ATOM   3611 C  CZ  . TYR A 1 486 ? 64.947  42.165 124.808 1.00 26.61 ? 486  TYR A CZ  1 
ATOM   3612 O  OH  . TYR A 1 486 ? 64.248  43.335 124.992 1.00 30.42 ? 486  TYR A OH  1 
ATOM   3613 N  N   . ILE A 1 487 ? 66.234  39.458 121.134 1.00 26.77 ? 487  ILE A N   1 
ATOM   3614 C  CA  . ILE A 1 487 ? 66.433  40.492 120.106 1.00 24.24 ? 487  ILE A CA  1 
ATOM   3615 C  C   . ILE A 1 487 ? 66.480  41.820 120.849 1.00 24.68 ? 487  ILE A C   1 
ATOM   3616 O  O   . ILE A 1 487 ? 65.439  42.359 121.238 1.00 25.80 ? 487  ILE A O   1 
ATOM   3617 C  CB  . ILE A 1 487 ? 65.276  40.566 119.100 1.00 25.36 ? 487  ILE A CB  1 
ATOM   3618 C  CG1 . ILE A 1 487 ? 65.055  39.331 118.272 1.00 41.07 ? 487  ILE A CG1 1 
ATOM   3619 C  CG2 . ILE A 1 487 ? 65.631  41.619 118.047 1.00 25.28 ? 487  ILE A CG2 1 
ATOM   3620 C  CD1 . ILE A 1 487 ? 66.197  38.619 118.072 1.00 34.44 ? 487  ILE A CD1 1 
ATOM   3621 N  N   . ASP A 1 488 ? 67.672  42.378 121.022 1.00 25.31 ? 488  ASP A N   1 
ATOM   3622 C  CA  . ASP A 1 488 ? 67.842  43.663 121.703 1.00 26.23 ? 488  ASP A CA  1 
ATOM   3623 C  C   . ASP A 1 488 ? 68.102  44.708 120.621 1.00 26.24 ? 488  ASP A C   1 
ATOM   3624 O  O   . ASP A 1 488 ? 69.215  44.811 120.106 1.00 26.45 ? 488  ASP A O   1 
ATOM   3625 C  CB  . ASP A 1 488 ? 69.025  43.590 122.664 1.00 27.13 ? 488  ASP A CB  1 
ATOM   3626 C  CG  . ASP A 1 488 ? 69.110  44.786 123.596 1.00 32.09 ? 488  ASP A CG  1 
ATOM   3627 O  OD1 . ASP A 1 488 ? 68.390  45.791 123.415 1.00 32.28 ? 488  ASP A OD1 1 
ATOM   3628 O  OD2 . ASP A 1 488 ? 69.956  44.735 124.505 1.00 40.55 ? 488  ASP A OD2 1 
ATOM   3629 N  N   . TYR A 1 489 ? 67.079  45.482 120.274 1.00 26.12 ? 489  TYR A N   1 
ATOM   3630 C  CA  . TYR A 1 489 ? 67.258  46.481 119.228 1.00 26.17 ? 489  TYR A CA  1 
ATOM   3631 C  C   . TYR A 1 489 ? 68.163  47.611 119.707 1.00 27.38 ? 489  TYR A C   1 
ATOM   3632 O  O   . TYR A 1 489 ? 68.012  48.119 120.819 1.00 28.24 ? 489  TYR A O   1 
ATOM   3633 C  CB  . TYR A 1 489 ? 65.907  47.024 118.763 1.00 27.69 ? 489  TYR A CB  1 
ATOM   3634 C  CG  . TYR A 1 489 ? 65.121  46.003 117.978 1.00 24.74 ? 489  TYR A CG  1 
ATOM   3635 C  CD1 . TYR A 1 489 ? 65.639  45.475 116.807 1.00 23.99 ? 489  TYR A CD1 1 
ATOM   3636 C  CD2 . TYR A 1 489 ? 63.886  45.547 118.411 1.00 30.65 ? 489  TYR A CD2 1 
ATOM   3637 C  CE1 . TYR A 1 489 ? 64.949  44.537 116.072 1.00 25.19 ? 489  TYR A CE1 1 
ATOM   3638 C  CE2 . TYR A 1 489 ? 63.183  44.602 117.680 1.00 32.86 ? 489  TYR A CE2 1 
ATOM   3639 C  CZ  . TYR A 1 489 ? 63.730  44.100 116.511 1.00 33.14 ? 489  TYR A CZ  1 
ATOM   3640 O  OH  . TYR A 1 489 ? 63.050  43.166 115.771 1.00 35.51 ? 489  TYR A OH  1 
ATOM   3641 N  N   . THR A 1 490 ? 69.118  48.000 118.862 1.00 27.54 ? 490  THR A N   1 
ATOM   3642 C  CA  . THR A 1 490 ? 70.134  48.979 119.233 1.00 28.82 ? 490  THR A CA  1 
ATOM   3643 C  C   . THR A 1 490 ? 69.912  50.314 118.544 1.00 30.56 ? 490  THR A C   1 
ATOM   3644 O  O   . THR A 1 490 ? 70.746  51.219 118.669 1.00 39.11 ? 490  THR A O   1 
ATOM   3645 C  CB  . THR A 1 490 ? 71.541  48.460 118.923 1.00 32.52 ? 490  THR A CB  1 
ATOM   3646 O  OG1 . THR A 1 490 ? 71.630  48.146 117.529 1.00 32.32 ? 490  THR A OG1 1 
ATOM   3647 C  CG2 . THR A 1 490 ? 71.851  47.214 119.742 1.00 30.71 ? 490  THR A CG2 1 
ATOM   3648 N  N   . GLY A 1 491 ? 68.816  50.448 117.811 1.00 28.56 ? 491  GLY A N   1 
ATOM   3649 C  CA  . GLY A 1 491 ? 68.481  51.682 117.151 1.00 33.23 ? 491  GLY A CA  1 
ATOM   3650 C  C   . GLY A 1 491 ? 67.075  51.617 116.601 1.00 30.22 ? 491  GLY A C   1 
ATOM   3651 O  O   . GLY A 1 491 ? 66.422  50.563 116.608 1.00 31.38 ? 491  GLY A O   1 
ATOM   3652 N  N   . PRO A 1 492 ? 66.588  52.747 116.097 1.00 33.41 ? 492  PRO A N   1 
ATOM   3653 C  CA  . PRO A 1 492 ? 65.246  52.792 115.517 1.00 35.68 ? 492  PRO A CA  1 
ATOM   3654 C  C   . PRO A 1 492 ? 65.212  52.064 114.186 1.00 29.12 ? 492  PRO A C   1 
ATOM   3655 O  O   . PRO A 1 492 ? 66.259  51.858 113.549 1.00 30.33 ? 492  PRO A O   1 
ATOM   3656 C  CB  . PRO A 1 492 ? 65.015  54.295 115.307 1.00 31.45 ? 492  PRO A CB  1 
ATOM   3657 C  CG  . PRO A 1 492 ? 66.384  54.850 115.073 1.00 34.41 ? 492  PRO A CG  1 
ATOM   3658 C  CD  . PRO A 1 492 ? 67.306  54.028 115.954 1.00 36.24 ? 492  PRO A CD  1 
ATOM   3659 N  N   . PRO A 1 493 ? 64.027  51.653 113.738 1.00 30.12 ? 493  PRO A N   1 
ATOM   3660 C  CA  . PRO A 1 493 ? 63.905  51.107 112.380 1.00 27.82 ? 493  PRO A CA  1 
ATOM   3661 C  C   . PRO A 1 493 ? 64.327  52.112 111.321 1.00 30.93 ? 493  PRO A C   1 
ATOM   3662 O  O   . PRO A 1 493 ? 64.130  53.324 111.459 1.00 30.32 ? 493  PRO A O   1 
ATOM   3663 C  CB  . PRO A 1 493 ? 62.420  50.737 112.261 1.00 26.34 ? 493  PRO A CB  1 
ATOM   3664 C  CG  . PRO A 1 493 ? 61.808  50.979 113.605 1.00 37.92 ? 493  PRO A CG  1 
ATOM   3665 C  CD  . PRO A 1 493 ? 62.729  51.818 114.412 1.00 39.64 ? 493  PRO A CD  1 
ATOM   3666 N  N   . ILE A 1 494 ? 64.936  51.587 110.263 1.00 26.72 ? 494  ILE A N   1 
ATOM   3667 C  CA  . ILE A 1 494 ? 65.415  52.369 109.129 1.00 27.63 ? 494  ILE A CA  1 
ATOM   3668 C  C   . ILE A 1 494 ? 64.551  52.019 107.924 1.00 25.65 ? 494  ILE A C   1 
ATOM   3669 O  O   . ILE A 1 494 ? 64.334  50.837 107.630 1.00 25.81 ? 494  ILE A O   1 
ATOM   3670 C  CB  . ILE A 1 494 ? 66.898  52.061 108.856 1.00 29.49 ? 494  ILE A CB  1 
ATOM   3671 C  CG1 . ILE A 1 494 ? 67.735  52.457 110.083 1.00 36.57 ? 494  ILE A CG1 1 
ATOM   3672 C  CG2 . ILE A 1 494 ? 67.371  52.778 107.586 1.00 33.37 ? 494  ILE A CG2 1 
ATOM   3673 C  CD1 . ILE A 1 494 ? 69.199  52.112 109.969 1.00 42.70 ? 494  ILE A CD1 1 
ATOM   3674 N  N   . GLU A 1 495 ? 64.051  53.040 107.228 1.00 25.80 ? 495  GLU A N   1 
ATOM   3675 C  CA  . GLU A 1 495 ? 63.186  52.790 106.085 1.00 23.19 ? 495  GLU A CA  1 
ATOM   3676 C  C   . GLU A 1 495 ? 63.987  52.129 104.974 1.00 23.57 ? 495  GLU A C   1 
ATOM   3677 O  O   . GLU A 1 495 ? 65.212  52.247 104.916 1.00 24.17 ? 495  GLU A O   1 
ATOM   3678 C  CB  . GLU A 1 495 ? 62.660  54.102 105.496 1.00 31.11 ? 495  GLU A CB  1 
ATOM   3679 C  CG  . GLU A 1 495 ? 63.709  55.191 105.371 1.00 40.29 ? 495  GLU A CG  1 
ATOM   3680 C  CD  . GLU A 1 495 ? 63.144  56.526 104.881 1.00 53.05 ? 495  GLU A CD  1 
ATOM   3681 O  OE1 . GLU A 1 495 ? 63.946  57.463 104.661 1.00 52.25 ? 495  GLU A OE1 1 
ATOM   3682 O  OE2 . GLU A 1 495 ? 61.907  56.632 104.689 1.00 50.62 ? 495  GLU A OE2 1 
ATOM   3683 N  N   . PRO A 1 496 ? 63.320  51.446 104.061 1.00 21.74 ? 496  PRO A N   1 
ATOM   3684 C  CA  . PRO A 1 496 ? 64.031  50.979 102.865 1.00 20.64 ? 496  PRO A CA  1 
ATOM   3685 C  C   . PRO A 1 496 ? 64.651  52.158 102.125 1.00 22.12 ? 496  PRO A C   1 
ATOM   3686 O  O   . PRO A 1 496 ? 64.131  53.273 102.140 1.00 22.98 ? 496  PRO A O   1 
ATOM   3687 C  CB  . PRO A 1 496 ? 62.934  50.300 102.036 1.00 21.84 ? 496  PRO A CB  1 
ATOM   3688 C  CG  . PRO A 1 496 ? 61.647  50.837 102.572 1.00 28.39 ? 496  PRO A CG  1 
ATOM   3689 C  CD  . PRO A 1 496 ? 61.882  51.131 104.016 1.00 26.35 ? 496  PRO A CD  1 
ATOM   3690 N  N   . ALA A 1 497 ? 65.791  51.903 101.484 1.00 22.42 ? 497  ALA A N   1 
ATOM   3691 C  CA  . ALA A 1 497 ? 66.452  52.938 100.703 1.00 22.24 ? 497  ALA A CA  1 
ATOM   3692 C  C   . ALA A 1 497 ? 65.626  53.288 99.462  1.00 20.85 ? 497  ALA A C   1 
ATOM   3693 O  O   . ALA A 1 497 ? 64.728  52.550 99.050  1.00 19.93 ? 497  ALA A O   1 
ATOM   3694 C  CB  . ALA A 1 497 ? 67.842  52.464 100.286 1.00 21.53 ? 497  ALA A CB  1 
ATOM   3695 N  N   . VAL A 1 498 ? 65.957  54.428 98.847  1.00 21.57 ? 498  VAL A N   1 
ATOM   3696 C  CA  . VAL A 1 498 ? 65.070  54.989 97.833  1.00 21.39 ? 498  VAL A CA  1 
ATOM   3697 C  C   . VAL A 1 498 ? 64.930  54.090 96.610  1.00 21.36 ? 498  VAL A C   1 
ATOM   3698 O  O   . VAL A 1 498 ? 63.941  54.204 95.876  1.00 20.59 ? 498  VAL A O   1 
ATOM   3699 C  CB  . VAL A 1 498 ? 65.498  56.406 97.395  1.00 25.26 ? 498  VAL A CB  1 
ATOM   3700 C  CG1 . VAL A 1 498 ? 65.226  57.429 98.520  1.00 29.89 ? 498  VAL A CG1 1 
ATOM   3701 C  CG2 . VAL A 1 498 ? 66.946  56.426 96.934  1.00 24.81 ? 498  VAL A CG2 1 
ATOM   3702 N  N   . HIS A 1 499 ? 65.886  53.192 96.367  1.00 19.52 ? 499  HIS A N   1 
ATOM   3703 C  CA  . HIS A 1 499 ? 65.856  52.338 95.185  1.00 18.41 ? 499  HIS A CA  1 
ATOM   3704 C  C   . HIS A 1 499 ? 65.149  51.004 95.427  1.00 17.46 ? 499  HIS A C   1 
ATOM   3705 O  O   . HIS A 1 499 ? 65.146  50.152 94.534  1.00 17.15 ? 499  HIS A O   1 
ATOM   3706 C  CB  . HIS A 1 499 ? 67.274  51.964 94.734  1.00 18.38 ? 499  HIS A CB  1 
ATOM   3707 C  CG  . HIS A 1 499 ? 68.027  51.194 95.767  1.00 18.54 ? 499  HIS A CG  1 
ATOM   3708 N  ND1 . HIS A 1 499 ? 68.641  51.789 96.846  1.00 24.42 ? 499  HIS A ND1 1 
ATOM   3709 C  CD2 . HIS A 1 499 ? 68.160  49.856 95.940  1.00 19.91 ? 499  HIS A CD2 1 
ATOM   3710 C  CE1 . HIS A 1 499 ? 69.161  50.850 97.618  1.00 22.93 ? 499  HIS A CE1 1 
ATOM   3711 N  NE2 . HIS A 1 499 ? 68.867  49.672 97.103  1.00 21.91 ? 499  HIS A NE2 1 
ATOM   3712 N  N   . GLU A 1 500 ? 64.584  50.770 96.607  1.00 17.67 ? 500  GLU A N   1 
ATOM   3713 C  CA  . GLU A 1 500 ? 64.013  49.462 96.924  1.00 17.48 ? 500  GLU A CA  1 
ATOM   3714 C  C   . GLU A 1 500 ? 62.652  49.611 97.579  1.00 18.53 ? 500  GLU A C   1 
ATOM   3715 O  O   . GLU A 1 500 ? 62.286  48.840 98.480  1.00 19.32 ? 500  GLU A O   1 
ATOM   3716 C  CB  . GLU A 1 500 ? 64.956  48.609 97.790  1.00 16.97 ? 500  GLU A CB  1 
ATOM   3717 C  CG  . GLU A 1 500 ? 65.486  49.370 99.016  1.00 17.99 ? 500  GLU A CG  1 
ATOM   3718 C  CD  . GLU A 1 500 ? 66.301  48.532 100.006 1.00 19.71 ? 500  GLU A CD  1 
ATOM   3719 O  OE1 . GLU A 1 500 ? 66.595  47.344 99.758  1.00 18.18 ? 500  GLU A OE1 1 
ATOM   3720 O  OE2 . GLU A 1 500 ? 66.633  49.106 101.063 1.00 20.63 ? 500  GLU A OE2 1 
ATOM   3721 N  N   . ARG A 1 501 ? 61.872  50.594 97.127  1.00 19.01 ? 501  ARG A N   1 
ATOM   3722 C  CA  . ARG A 1 501 ? 60.565  50.869 97.703  1.00 19.00 ? 501  ARG A CA  1 
ATOM   3723 C  C   . ARG A 1 501 ? 59.400  50.325 96.890  1.00 20.51 ? 501  ARG A C   1 
ATOM   3724 O  O   . ARG A 1 501 ? 58.259  50.400 97.349  1.00 22.76 ? 501  ARG A O   1 
ATOM   3725 C  CB  . ARG A 1 501 ? 60.400  52.355 98.027  1.00 23.01 ? 501  ARG A CB  1 
ATOM   3726 C  CG  . ARG A 1 501 ? 61.348  52.786 99.142  1.00 21.79 ? 501  ARG A CG  1 
ATOM   3727 C  CD  . ARG A 1 501 ? 61.403  54.291 99.301  1.00 25.40 ? 501  ARG A CD  1 
ATOM   3728 N  NE  . ARG A 1 501 ? 62.372  54.672 100.318 1.00 26.35 ? 501  ARG A NE  1 
ATOM   3729 C  CZ  . ARG A 1 501 ? 62.532  55.901 100.781 1.00 27.78 ? 501  ARG A CZ  1 
ATOM   3730 N  NH1 . ARG A 1 501 ? 61.811  56.911 100.318 1.00 33.35 ? 501  ARG A NH1 1 
ATOM   3731 N  NH2 . ARG A 1 501 ? 63.459  56.129 101.707 1.00 33.37 ? 501  ARG A NH2 1 
ATOM   3732 N  N   . GLY A 1 502 ? 59.648  49.729 95.730  1.00 17.79 ? 502  GLY A N   1 
ATOM   3733 C  CA  . GLY A 1 502 ? 58.595  49.117 94.955  1.00 18.34 ? 502  GLY A CA  1 
ATOM   3734 C  C   . GLY A 1 502 ? 58.329  47.678 95.374  1.00 16.66 ? 502  GLY A C   1 
ATOM   3735 O  O   . GLY A 1 502 ? 58.894  47.149 96.336  1.00 18.67 ? 502  GLY A O   1 
ATOM   3736 N  N   . TRP A 1 503 ? 57.458  47.029 94.611  1.00 17.11 ? 503  TRP A N   1 
ATOM   3737 C  CA  . TRP A 1 503 ? 57.180  45.621 94.878  1.00 16.10 ? 503  TRP A CA  1 
ATOM   3738 C  C   . TRP A 1 503 ? 58.397  44.781 94.502  1.00 16.59 ? 503  TRP A C   1 
ATOM   3739 O  O   . TRP A 1 503 ? 59.011  44.974 93.435  1.00 16.30 ? 503  TRP A O   1 
ATOM   3740 C  CB  . TRP A 1 503 ? 55.957  45.158 94.087  1.00 18.59 ? 503  TRP A CB  1 
ATOM   3741 C  CG  . TRP A 1 503 ? 54.720  45.765 94.592  1.00 19.99 ? 503  TRP A CG  1 
ATOM   3742 C  CD1 . TRP A 1 503 ? 54.062  46.842 94.070  1.00 20.26 ? 503  TRP A CD1 1 
ATOM   3743 C  CD2 . TRP A 1 503 ? 53.989  45.365 95.748  1.00 18.49 ? 503  TRP A CD2 1 
ATOM   3744 N  NE1 . TRP A 1 503 ? 52.960  47.130 94.830  1.00 22.19 ? 503  TRP A NE1 1 
ATOM   3745 C  CE2 . TRP A 1 503 ? 52.887  46.233 95.865  1.00 20.86 ? 503  TRP A CE2 1 
ATOM   3746 C  CE3 . TRP A 1 503 ? 54.150  44.344 96.694  1.00 21.36 ? 503  TRP A CE3 1 
ATOM   3747 C  CZ2 . TRP A 1 503 ? 51.957  46.125 96.891  1.00 22.16 ? 503  TRP A CZ2 1 
ATOM   3748 C  CZ3 . TRP A 1 503 ? 53.222  44.240 97.715  1.00 20.11 ? 503  TRP A CZ3 1 
ATOM   3749 C  CH2 . TRP A 1 503 ? 52.132  45.122 97.799  1.00 20.29 ? 503  TRP A CH2 1 
ATOM   3750 N  N   . LYS A 1 504 ? 58.751  43.843 95.382  1.00 16.25 ? 504  LYS A N   1 
ATOM   3751 C  CA  . LYS A 1 504 ? 59.976  43.070 95.243  1.00 15.31 ? 504  LYS A CA  1 
ATOM   3752 C  C   . LYS A 1 504 ? 59.745  41.612 95.608  1.00 15.15 ? 504  LYS A C   1 
ATOM   3753 O  O   . LYS A 1 504 ? 58.792  41.258 96.314  1.00 16.78 ? 504  LYS A O   1 
ATOM   3754 C  CB  . LYS A 1 504 ? 61.124  43.661 96.076  1.00 15.98 ? 504  LYS A CB  1 
ATOM   3755 C  CG  . LYS A 1 504 ? 61.713  44.915 95.417  1.00 16.46 ? 504  LYS A CG  1 
ATOM   3756 C  CD  . LYS A 1 504 ? 62.772  45.592 96.270  1.00 17.63 ? 504  LYS A CD  1 
ATOM   3757 C  CE  . LYS A 1 504 ? 64.019  44.715 96.466  1.00 15.36 ? 504  LYS A CE  1 
ATOM   3758 N  NZ  . LYS A 1 504 ? 64.501  44.024 95.216  1.00 16.17 ? 504  LYS A NZ  1 
ATOM   3759 N  N   . ASP A 1 505 ? 60.609  40.761 95.085  1.00 14.56 ? 505  ASP A N   1 
ATOM   3760 C  CA  . ASP A 1 505 ? 60.574  39.355 95.447  1.00 14.27 ? 505  ASP A CA  1 
ATOM   3761 C  C   . ASP A 1 505 ? 61.890  38.847 96.018  1.00 16.56 ? 505  ASP A C   1 
ATOM   3762 O  O   . ASP A 1 505 ? 61.956  37.688 96.452  1.00 14.89 ? 505  ASP A O   1 
ATOM   3763 C  CB  . ASP A 1 505 ? 60.102  38.462 94.288  1.00 16.96 ? 505  ASP A CB  1 
ATOM   3764 C  CG  . ASP A 1 505 ? 60.958  38.606 93.035  1.00 16.39 ? 505  ASP A CG  1 
ATOM   3765 O  OD1 . ASP A 1 505 ? 62.209  38.621 93.135  1.00 15.35 ? 505  ASP A OD1 1 
ATOM   3766 O  OD2 . ASP A 1 505 ? 60.344  38.622 91.951  1.00 17.27 ? 505  ASP A OD2 1 
ATOM   3767 N  N   . THR A 1 506 ? 62.929  39.673 96.039  1.00 15.16 ? 506  THR A N   1 
ATOM   3768 C  CA  . THR A 1 506 ? 64.232  39.317 96.570  1.00 15.61 ? 506  THR A CA  1 
ATOM   3769 C  C   . THR A 1 506 ? 64.683  40.516 97.383  1.00 14.69 ? 506  THR A C   1 
ATOM   3770 O  O   . THR A 1 506 ? 64.695  41.637 96.873  1.00 16.38 ? 506  THR A O   1 
ATOM   3771 C  CB  . THR A 1 506 ? 65.195  39.065 95.409  1.00 14.81 ? 506  THR A CB  1 
ATOM   3772 O  OG1 . THR A 1 506 ? 64.636  38.029 94.592  1.00 17.19 ? 506  THR A OG1 1 
ATOM   3773 C  CG2 . THR A 1 506 ? 66.545  38.604 95.936  1.00 15.96 ? 506  THR A CG2 1 
ATOM   3774 N  N   . VAL A 1 507 ? 65.047  40.292 98.638  1.00 15.21 ? 507  VAL A N   1 
ATOM   3775 C  CA  . VAL A 1 507 ? 65.355  41.384 99.562  1.00 16.29 ? 507  VAL A CA  1 
ATOM   3776 C  C   . VAL A 1 507 ? 66.730  41.176 100.188 1.00 16.59 ? 507  VAL A C   1 
ATOM   3777 O  O   . VAL A 1 507 ? 67.054  40.072 100.648 1.00 15.70 ? 507  VAL A O   1 
ATOM   3778 C  CB  . VAL A 1 507 ? 64.271  41.547 100.660 1.00 16.34 ? 507  VAL A CB  1 
ATOM   3779 C  CG1 . VAL A 1 507 ? 64.061  40.257 101.461 1.00 19.34 ? 507  VAL A CG1 1 
ATOM   3780 C  CG2 . VAL A 1 507 ? 64.637  42.702 101.593 1.00 19.38 ? 507  VAL A CG2 1 
ATOM   3781 N  N   . LYS A 1 508 ? 67.531  42.241 100.241 1.00 15.54 ? 508  LYS A N   1 
ATOM   3782 C  CA  . LYS A 1 508 ? 68.820  42.174 100.930 1.00 15.35 ? 508  LYS A CA  1 
ATOM   3783 C  C   . LYS A 1 508 ? 68.554  42.180 102.430 1.00 17.75 ? 508  LYS A C   1 
ATOM   3784 O  O   . LYS A 1 508 ? 68.168  43.210 102.998 1.00 18.56 ? 508  LYS A O   1 
ATOM   3785 C  CB  . LYS A 1 508 ? 69.695  43.363 100.538 1.00 17.45 ? 508  LYS A CB  1 
ATOM   3786 C  CG  . LYS A 1 508 ? 71.101  43.293 101.116 1.00 17.51 ? 508  LYS A CG  1 
ATOM   3787 C  CD  . LYS A 1 508 ? 71.821  44.607 100.972 1.00 19.77 ? 508  LYS A CD  1 
ATOM   3788 C  CE  . LYS A 1 508 ? 73.308  44.455 101.330 1.00 22.96 ? 508  LYS A CE  1 
ATOM   3789 N  NZ  . LYS A 1 508 ? 73.953  45.799 101.454 1.00 31.82 ? 508  LYS A NZ  1 
ATOM   3790 N  N   . ALA A 1 509 ? 68.771  41.045 103.078 1.00 15.56 ? 509  ALA A N   1 
ATOM   3791 C  CA  . ALA A 1 509 ? 68.656  40.946 104.530 1.00 16.22 ? 509  ALA A CA  1 
ATOM   3792 C  C   . ALA A 1 509 ? 70.031  41.247 105.125 1.00 18.42 ? 509  ALA A C   1 
ATOM   3793 O  O   . ALA A 1 509 ? 70.965  40.437 105.016 1.00 19.21 ? 509  ALA A O   1 
ATOM   3794 C  CB  . ALA A 1 509 ? 68.141  39.561 104.917 1.00 17.73 ? 509  ALA A CB  1 
ATOM   3795 N  N   . GLU A 1 510 ? 70.157  42.440 105.717 1.00 18.36 ? 510  GLU A N   1 
ATOM   3796 C  CA  . GLU A 1 510 ? 71.441  42.931 106.196 1.00 19.80 ? 510  GLU A CA  1 
ATOM   3797 C  C   . GLU A 1 510 ? 71.892  42.188 107.453 1.00 18.86 ? 510  GLU A C   1 
ATOM   3798 O  O   . GLU A 1 510 ? 71.073  41.845 108.310 1.00 21.63 ? 510  GLU A O   1 
ATOM   3799 C  CB  . GLU A 1 510 ? 71.325  44.411 106.550 1.00 20.80 ? 510  GLU A CB  1 
ATOM   3800 C  CG  . GLU A 1 510 ? 71.066  45.340 105.378 1.00 20.78 ? 510  GLU A CG  1 
ATOM   3801 C  CD  . GLU A 1 510 ? 72.311  45.613 104.563 1.00 26.64 ? 510  GLU A CD  1 
ATOM   3802 O  OE1 . GLU A 1 510 ? 73.321  44.895 104.730 1.00 28.61 ? 510  GLU A OE1 1 
ATOM   3803 O  OE2 . GLU A 1 510 ? 72.294  46.598 103.788 1.00 27.75 ? 510  GLU A OE2 1 
ATOM   3804 N  N   . PRO A 1 511 ? 73.203  41.992 107.614 1.00 22.64 ? 511  PRO A N   1 
ATOM   3805 C  CA  . PRO A 1 511 ? 73.710  41.332 108.825 1.00 22.79 ? 511  PRO A CA  1 
ATOM   3806 C  C   . PRO A 1 511 ? 73.457  42.176 110.066 1.00 23.88 ? 511  PRO A C   1 
ATOM   3807 O  O   . PRO A 1 511 ? 73.556  43.405 110.036 1.00 25.83 ? 511  PRO A O   1 
ATOM   3808 C  CB  . PRO A 1 511 ? 75.223  41.216 108.574 1.00 25.43 ? 511  PRO A CB  1 
ATOM   3809 C  CG  . PRO A 1 511 ? 75.528  41.967 107.392 1.00 25.42 ? 511  PRO A CG  1 
ATOM   3810 C  CD  . PRO A 1 511 ? 74.280  42.484 106.748 1.00 22.03 ? 511  PRO A CD  1 
ATOM   3811 N  N   . GLY A 1 512 ? 73.167  41.501 111.175 1.00 22.75 ? 512  GLY A N   1 
ATOM   3812 C  CA  . GLY A 1 512 ? 72.956  42.226 112.417 1.00 25.55 ? 512  GLY A CA  1 
ATOM   3813 C  C   . GLY A 1 512 ? 71.718  43.088 112.422 1.00 24.23 ? 512  GLY A C   1 
ATOM   3814 O  O   . GLY A 1 512 ? 71.610  44.012 113.234 1.00 25.22 ? 512  GLY A O   1 
ATOM   3815 N  N   . MET A 1 513 ? 70.772  42.797 111.532 1.00 23.76 ? 513  MET A N   1 
ATOM   3816 C  CA  . MET A 1 513 ? 69.527  43.534 111.430 1.00 22.22 ? 513  MET A CA  1 
ATOM   3817 C  C   . MET A 1 513 ? 68.383  42.545 111.278 1.00 21.53 ? 513  MET A C   1 
ATOM   3818 O  O   . MET A 1 513 ? 68.560  41.401 110.831 1.00 22.24 ? 513  MET A O   1 
ATOM   3819 C  CB  . MET A 1 513 ? 69.571  44.421 110.186 1.00 25.08 ? 513  MET A CB  1 
ATOM   3820 C  CG  . MET A 1 513 ? 70.759  45.364 110.109 1.00 22.72 ? 513  MET A CG  1 
ATOM   3821 S  SD  . MET A 1 513 ? 70.459  46.796 109.041 1.00 24.94 ? 513  MET A SD  1 
ATOM   3822 C  CE  . MET A 1 513 ? 69.444  47.905 110.036 1.00 24.67 ? 513  MET A CE  1 
ATOM   3823 N  N   . VAL A 1 514 ? 67.206  43.009 111.685 1.00 23.35 ? 514  VAL A N   1 
ATOM   3824 C  CA  . VAL A 1 514 ? 65.948  42.367 111.345 1.00 21.73 ? 514  VAL A CA  1 
ATOM   3825 C  C   . VAL A 1 514 ? 65.388  43.126 110.148 1.00 21.31 ? 514  VAL A C   1 
ATOM   3826 O  O   . VAL A 1 514 ? 65.133  44.334 110.236 1.00 22.40 ? 514  VAL A O   1 
ATOM   3827 C  CB  . VAL A 1 514 ? 64.971  42.384 112.533 1.00 22.91 ? 514  VAL A CB  1 
ATOM   3828 C  CG1 . VAL A 1 514 ? 63.634  41.749 112.124 1.00 23.54 ? 514  VAL A CG1 1 
ATOM   3829 C  CG2 . VAL A 1 514 ? 65.590  41.670 113.759 1.00 23.50 ? 514  VAL A CG2 1 
ATOM   3830 N  N   . THR A 1 515 ? 65.256  42.434 109.013 1.00 20.11 ? 515  THR A N   1 
ATOM   3831 C  CA  . THR A 1 515 ? 64.710  43.027 107.796 1.00 19.70 ? 515  THR A CA  1 
ATOM   3832 C  C   . THR A 1 515 ? 63.272  42.543 107.660 1.00 21.21 ? 515  THR A C   1 
ATOM   3833 O  O   . THR A 1 515 ? 63.030  41.336 107.548 1.00 20.48 ? 515  THR A O   1 
ATOM   3834 C  CB  . THR A 1 515 ? 65.526  42.566 106.592 1.00 20.41 ? 515  THR A CB  1 
ATOM   3835 O  OG1 . THR A 1 515 ? 66.851  43.108 106.677 1.00 20.59 ? 515  THR A OG1 1 
ATOM   3836 C  CG2 . THR A 1 515 ? 64.863  43.044 105.300 1.00 18.82 ? 515  THR A CG2 1 
ATOM   3837 N  N   . SER A 1 516 ? 62.322  43.465 107.698 1.00 22.78 ? 516  SER A N   1 
ATOM   3838 C  CA  . SER A 1 516 ? 60.909  43.126 107.724 1.00 24.27 ? 516  SER A CA  1 
ATOM   3839 C  C   . SER A 1 516 ? 60.288  43.471 106.386 1.00 22.61 ? 516  SER A C   1 
ATOM   3840 O  O   . SER A 1 516 ? 60.510  44.582 105.863 1.00 22.30 ? 516  SER A O   1 
ATOM   3841 C  CB  . SER A 1 516 ? 60.189  43.882 108.836 1.00 23.12 ? 516  SER A CB  1 
ATOM   3842 O  OG  . SER A 1 516 ? 60.650  43.420 110.101 1.00 25.36 ? 516  SER A OG  1 
ATOM   3843 N  N   . VAL A 1 517 ? 59.519  42.507 105.854 1.00 21.16 ? 517  VAL A N   1 
ATOM   3844 C  CA  . VAL A 1 517 ? 58.784  42.636 104.600 1.00 21.81 ? 517  VAL A CA  1 
ATOM   3845 C  C   . VAL A 1 517 ? 57.326  42.247 104.818 1.00 20.39 ? 517  VAL A C   1 
ATOM   3846 O  O   . VAL A 1 517 ? 56.983  41.502 105.747 1.00 21.39 ? 517  VAL A O   1 
ATOM   3847 C  CB  . VAL A 1 517 ? 59.404  41.800 103.449 1.00 20.29 ? 517  VAL A CB  1 
ATOM   3848 C  CG1 . VAL A 1 517 ? 60.880  42.160 103.238 1.00 22.30 ? 517  VAL A CG1 1 
ATOM   3849 C  CG2 . VAL A 1 517 ? 59.227  40.302 103.696 1.00 22.02 ? 517  VAL A CG2 1 
ATOM   3850 N  N   . ILE A 1 518 ? 56.451  42.785 103.960 1.00 21.72 ? 518  ILE A N   1 
ATOM   3851 C  CA  . ILE A 1 518 ? 55.021  42.552 104.072 1.00 21.48 ? 518  ILE A CA  1 
ATOM   3852 C  C   . ILE A 1 518 ? 54.467  42.114 102.724 1.00 20.93 ? 518  ILE A C   1 
ATOM   3853 O  O   . ILE A 1 518 ? 54.879  42.599 101.667 1.00 21.00 ? 518  ILE A O   1 
ATOM   3854 C  CB  . ILE A 1 518 ? 54.288  43.794 104.619 1.00 22.77 ? 518  ILE A CB  1 
ATOM   3855 C  CG1 . ILE A 1 518 ? 52.829  43.462 104.945 1.00 23.80 ? 518  ILE A CG1 1 
ATOM   3856 C  CG2 . ILE A 1 518 ? 54.402  44.937 103.618 1.00 23.56 ? 518  ILE A CG2 1 
ATOM   3857 C  CD1 . ILE A 1 518 ? 52.137  44.495 105.848 1.00 25.36 ? 518  ILE A CD1 1 
ATOM   3858 N  N   . MET A 1 519 ? 53.468  41.245 102.778 1.00 22.82 ? 519  MET A N   1 
ATOM   3859 C  CA  . MET A 1 519 ? 52.954  40.502 101.642 1.00 22.68 ? 519  MET A CA  1 
ATOM   3860 C  C   . MET A 1 519 ? 51.508  40.091 101.894 1.00 22.33 ? 519  MET A C   1 
ATOM   3861 O  O   . MET A 1 519 ? 51.063  40.013 103.039 1.00 22.83 ? 519  MET A O   1 
ATOM   3862 C  CB  . MET A 1 519 ? 53.978  39.402 101.461 1.00 25.29 ? 519  MET A CB  1 
ATOM   3863 C  CG  . MET A 1 519 ? 53.547  38.125 102.136 1.00 20.18 ? 519  MET A CG  1 
ATOM   3864 S  SD  . MET A 1 519 ? 55.031  37.104 102.147 1.00 22.00 ? 519  MET A SD  1 
ATOM   3865 C  CE  . MET A 1 519 ? 56.181  38.148 103.076 1.00 22.23 ? 519  MET A CE  1 
ATOM   3866 N  N   . LYS A 1 520 ? 50.765  39.839 100.819 1.00 22.47 ? 520  LYS A N   1 
ATOM   3867 C  CA  . LYS A 1 520 ? 49.422  39.286 100.942 1.00 24.53 ? 520  LYS A CA  1 
ATOM   3868 C  C   . LYS A 1 520 ? 49.227  38.177 99.921  1.00 28.53 ? 520  LYS A C   1 
ATOM   3869 O  O   . LYS A 1 520 ? 49.431  38.386 98.722  1.00 28.12 ? 520  LYS A O   1 
ATOM   3870 C  CB  . LYS A 1 520 ? 48.354  40.366 100.730 1.00 26.00 ? 520  LYS A CB  1 
ATOM   3871 C  CG  . LYS A 1 520 ? 46.905  39.858 100.742 1.00 28.25 ? 520  LYS A CG  1 
ATOM   3872 C  CD  . LYS A 1 520 ? 45.946  40.994 101.073 1.00 33.65 ? 520  LYS A CD  1 
ATOM   3873 C  CE  . LYS A 1 520 ? 44.501  40.514 101.075 1.00 35.45 ? 520  LYS A CE  1 
ATOM   3874 N  NZ  . LYS A 1 520 ? 43.525  41.612 100.766 1.00 38.56 ? 520  LYS A NZ  1 
ATOM   3875 N  N   . PHE A 1 521 ? 48.834  37.003 100.401 1.00 26.15 ? 521  PHE A N   1 
ATOM   3876 C  CA  . PHE A 1 521 ? 48.592  35.856 99.538  1.00 25.83 ? 521  PHE A CA  1 
ATOM   3877 C  C   . PHE A 1 521 ? 47.170  35.923 99.004  1.00 27.35 ? 521  PHE A C   1 
ATOM   3878 O  O   . PHE A 1 521 ? 46.228  36.146 99.770  1.00 28.77 ? 521  PHE A O   1 
ATOM   3879 C  CB  . PHE A 1 521 ? 48.809  34.575 100.349 1.00 25.01 ? 521  PHE A CB  1 
ATOM   3880 C  CG  . PHE A 1 521 ? 50.230  34.388 100.752 1.00 22.09 ? 521  PHE A CG  1 
ATOM   3881 C  CD1 . PHE A 1 521 ? 50.740  35.003 101.887 1.00 24.94 ? 521  PHE A CD1 1 
ATOM   3882 C  CD2 . PHE A 1 521 ? 51.087  33.659 99.956  1.00 24.04 ? 521  PHE A CD2 1 
ATOM   3883 C  CE1 . PHE A 1 521 ? 52.080  34.858 102.225 1.00 22.80 ? 521  PHE A CE1 1 
ATOM   3884 C  CE2 . PHE A 1 521 ? 52.427  33.515 100.286 1.00 24.26 ? 521  PHE A CE2 1 
ATOM   3885 C  CZ  . PHE A 1 521 ? 52.921  34.116 101.427 1.00 23.43 ? 521  PHE A CZ  1 
ATOM   3886 N  N   . THR A 1 522 ? 47.009  35.771 97.683  1.00 28.87 ? 522  THR A N   1 
ATOM   3887 C  CA  . THR A 1 522 ? 45.693  36.008 97.091  1.00 26.70 ? 522  THR A CA  1 
ATOM   3888 C  C   . THR A 1 522 ? 45.151  34.837 96.279  1.00 26.55 ? 522  THR A C   1 
ATOM   3889 O  O   . THR A 1 522 ? 43.928  34.699 96.142  1.00 29.60 ? 522  THR A O   1 
ATOM   3890 C  CB  . THR A 1 522 ? 45.686  37.252 96.190  1.00 31.70 ? 522  THR A CB  1 
ATOM   3891 O  OG1 . THR A 1 522 ? 46.664  37.104 95.158  1.00 31.40 ? 522  THR A OG1 1 
ATOM   3892 C  CG2 . THR A 1 522 ? 45.978  38.516 96.992  1.00 34.41 ? 522  THR A CG2 1 
ATOM   3893 N  N   . GLU A 1 523 ? 46.028  34.025 95.690  1.00 26.61 ? 523  GLU A N   1 
ATOM   3894 C  CA  . GLU A 1 523 ? 45.566  32.903 94.885  1.00 27.50 ? 523  GLU A CA  1 
ATOM   3895 C  C   . GLU A 1 523 ? 46.710  31.908 94.727  1.00 24.27 ? 523  GLU A C   1 
ATOM   3896 O  O   . GLU A 1 523 ? 47.819  32.111 95.230  1.00 25.03 ? 523  GLU A O   1 
ATOM   3897 C  CB  . GLU A 1 523 ? 45.079  33.369 93.515  1.00 30.57 ? 523  GLU A CB  1 
ATOM   3898 C  CG  . GLU A 1 523 ? 46.094  34.191 92.749  1.00 26.84 ? 523  GLU A CG  1 
ATOM   3899 C  CD  . GLU A 1 523 ? 45.543  34.633 91.409  1.00 34.52 ? 523  GLU A CD  1 
ATOM   3900 O  OE1 . GLU A 1 523 ? 44.339  34.411 91.145  1.00 41.30 ? 523  GLU A OE1 1 
ATOM   3901 O  OE2 . GLU A 1 523 ? 46.297  35.218 90.617  1.00 29.99 ? 523  GLU A OE2 1 
ATOM   3902 N  N   . ASN A 1 524 ? 46.420  30.828 94.005  1.00 25.02 ? 524  ASN A N   1 
ATOM   3903 C  CA  . ASN A 1 524 ? 47.377  29.776 93.660  1.00 23.53 ? 524  ASN A CA  1 
ATOM   3904 C  C   . ASN A 1 524 ? 47.913  29.011 94.869  1.00 23.13 ? 524  ASN A C   1 
ATOM   3905 O  O   . ASN A 1 524 ? 49.129  28.974 95.099  1.00 21.93 ? 524  ASN A O   1 
ATOM   3906 C  CB  . ASN A 1 524 ? 48.517  30.330 92.793  1.00 22.30 ? 524  ASN A CB  1 
ATOM   3907 C  CG  . ASN A 1 524 ? 48.046  30.694 91.408  1.00 23.58 ? 524  ASN A CG  1 
ATOM   3908 O  OD1 . ASN A 1 524 ? 47.255  29.963 90.807  1.00 23.84 ? 524  ASN A OD1 1 
ATOM   3909 N  ND2 . ASN A 1 524 ? 48.500  31.848 90.892  1.00 22.28 ? 524  ASN A ND2 1 
ATOM   3910 N  N   . PRO A 1 525 ? 47.052  28.359 95.650  1.00 24.67 ? 525  PRO A N   1 
ATOM   3911 C  CA  . PRO A 1 525 ? 47.569  27.463 96.693  1.00 25.34 ? 525  PRO A CA  1 
ATOM   3912 C  C   . PRO A 1 525 ? 48.358  26.314 96.080  1.00 24.47 ? 525  PRO A C   1 
ATOM   3913 O  O   . PRO A 1 525 ? 48.079  25.862 94.969  1.00 28.28 ? 525  PRO A O   1 
ATOM   3914 C  CB  . PRO A 1 525 ? 46.303  26.972 97.397  1.00 25.78 ? 525  PRO A CB  1 
ATOM   3915 C  CG  . PRO A 1 525 ? 45.225  27.081 96.360  1.00 29.82 ? 525  PRO A CG  1 
ATOM   3916 C  CD  . PRO A 1 525 ? 45.596  28.242 95.466  1.00 26.85 ? 525  PRO A CD  1 
ATOM   3917 N  N   . GLY A 1 526 ? 49.372  25.862 96.804  1.00 23.28 ? 526  GLY A N   1 
ATOM   3918 C  CA  . GLY A 1 526 ? 50.217  24.792 96.317  1.00 23.93 ? 526  GLY A CA  1 
ATOM   3919 C  C   . GLY A 1 526 ? 51.548  24.762 97.042  1.00 21.91 ? 526  GLY A C   1 
ATOM   3920 O  O   . GLY A 1 526 ? 51.761  25.449 98.040  1.00 23.92 ? 526  GLY A O   1 
ATOM   3921 N  N   . GLU A 1 527 ? 52.452  23.960 96.485  1.00 21.16 ? 527  GLU A N   1 
ATOM   3922 C  CA  . GLU A 1 527 ? 53.764  23.713 97.067  1.00 22.35 ? 527  GLU A CA  1 
ATOM   3923 C  C   . GLU A 1 527 ? 54.790  24.659 96.448  1.00 21.11 ? 527  GLU A C   1 
ATOM   3924 O  O   . GLU A 1 527 ? 55.144  24.526 95.270  1.00 21.29 ? 527  GLU A O   1 
ATOM   3925 C  CB  . GLU A 1 527 ? 54.148  22.261 96.802  1.00 24.30 ? 527  GLU A CB  1 
ATOM   3926 C  CG  . GLU A 1 527 ? 53.474  21.252 97.700  1.00 31.38 ? 527  GLU A CG  1 
ATOM   3927 C  CD  . GLU A 1 527 ? 53.786  21.501 99.166  1.00 35.97 ? 527  GLU A CD  1 
ATOM   3928 O  OE1 . GLU A 1 527 ? 54.985  21.672 99.503  1.00 35.07 ? 527  GLU A OE1 1 
ATOM   3929 O  OE2 . GLU A 1 527 ? 52.843  21.485 99.975  1.00 45.71 ? 527  GLU A OE2 1 
ATOM   3930 N  N   . TYR A 1 528 ? 55.299  25.599 97.241  1.00 18.54 ? 528  TYR A N   1 
ATOM   3931 C  CA  . TYR A 1 528 ? 56.322  26.528 96.791  1.00 17.06 ? 528  TYR A CA  1 
ATOM   3932 C  C   . TYR A 1 528 ? 57.511  26.465 97.738  1.00 16.10 ? 528  TYR A C   1 
ATOM   3933 O  O   . TYR A 1 528 ? 57.621  25.548 98.564  1.00 18.04 ? 528  TYR A O   1 
ATOM   3934 C  CB  . TYR A 1 528 ? 55.763  27.948 96.733  1.00 16.78 ? 528  TYR A CB  1 
ATOM   3935 C  CG  . TYR A 1 528 ? 54.613  28.107 95.773  1.00 17.48 ? 528  TYR A CG  1 
ATOM   3936 C  CD1 . TYR A 1 528 ? 53.299  27.890 96.176  1.00 18.57 ? 528  TYR A CD1 1 
ATOM   3937 C  CD2 . TYR A 1 528 ? 54.841  28.466 94.457  1.00 18.22 ? 528  TYR A CD2 1 
ATOM   3938 C  CE1 . TYR A 1 528 ? 52.242  28.059 95.286  1.00 19.34 ? 528  TYR A CE1 1 
ATOM   3939 C  CE2 . TYR A 1 528 ? 53.798  28.630 93.556  1.00 18.01 ? 528  TYR A CE2 1 
ATOM   3940 C  CZ  . TYR A 1 528 ? 52.497  28.427 93.972  1.00 19.02 ? 528  TYR A CZ  1 
ATOM   3941 O  OH  . TYR A 1 528 ? 51.451  28.587 93.091  1.00 20.24 ? 528  TYR A OH  1 
ATOM   3942 N  N   . VAL A 1 529 ? 58.431  27.411 97.612  1.00 15.89 ? 529  VAL A N   1 
ATOM   3943 C  CA  . VAL A 1 529 ? 59.638  27.446 98.432  1.00 17.14 ? 529  VAL A CA  1 
ATOM   3944 C  C   . VAL A 1 529 ? 59.977  28.906 98.717  1.00 15.00 ? 529  VAL A C   1 
ATOM   3945 O  O   . VAL A 1 529 ? 59.461  29.839 98.073  1.00 15.74 ? 529  VAL A O   1 
ATOM   3946 C  CB  . VAL A 1 529 ? 60.853  26.737 97.772  1.00 16.86 ? 529  VAL A CB  1 
ATOM   3947 C  CG1 . VAL A 1 529 ? 60.564  25.275 97.470  1.00 18.33 ? 529  VAL A CG1 1 
ATOM   3948 C  CG2 . VAL A 1 529 ? 61.286  27.482 96.518  1.00 19.44 ? 529  VAL A CG2 1 
ATOM   3949 N  N   . TRP A 1 530 ? 60.878  29.100 99.677  1.00 15.74 ? 530  TRP A N   1 
ATOM   3950 C  CA  . TRP A 1 530 ? 61.565  30.369 99.885  1.00 16.40 ? 530  TRP A CA  1 
ATOM   3951 C  C   . TRP A 1 530 ? 63.009  30.057 100.245 1.00 14.51 ? 530  TRP A C   1 
ATOM   3952 O  O   . TRP A 1 530 ? 63.304  28.976 100.766 1.00 15.32 ? 530  TRP A O   1 
ATOM   3953 C  CB  . TRP A 1 530 ? 60.857  31.257 100.932 1.00 15.51 ? 530  TRP A CB  1 
ATOM   3954 C  CG  . TRP A 1 530 ? 60.929  30.770 102.359 1.00 17.20 ? 530  TRP A CG  1 
ATOM   3955 C  CD1 . TRP A 1 530 ? 60.210  29.744 102.928 1.00 19.89 ? 530  TRP A CD1 1 
ATOM   3956 C  CD2 . TRP A 1 530 ? 61.748  31.313 103.396 1.00 16.11 ? 530  TRP A CD2 1 
ATOM   3957 N  NE1 . TRP A 1 530 ? 60.534  29.628 104.264 1.00 18.64 ? 530  TRP A NE1 1 
ATOM   3958 C  CE2 . TRP A 1 530 ? 61.468  30.584 104.578 1.00 16.47 ? 530  TRP A CE2 1 
ATOM   3959 C  CE3 . TRP A 1 530 ? 62.663  32.371 103.451 1.00 19.20 ? 530  TRP A CE3 1 
ATOM   3960 C  CZ2 . TRP A 1 530 ? 62.105  30.858 105.797 1.00 19.20 ? 530  TRP A CZ2 1 
ATOM   3961 C  CZ3 . TRP A 1 530 ? 63.293  32.648 104.653 1.00 18.28 ? 530  TRP A CZ3 1 
ATOM   3962 C  CH2 . TRP A 1 530 ? 63.010  31.895 105.812 1.00 18.15 ? 530  TRP A CH2 1 
ATOM   3963 N  N   . HIS A 1 531 ? 63.922  30.961 99.900  1.00 14.56 ? 531  HIS A N   1 
ATOM   3964 C  CA  . HIS A 1 531 ? 65.325  30.562 100.010 1.00 14.90 ? 531  HIS A CA  1 
ATOM   3965 C  C   . HIS A 1 531 ? 66.225  31.766 99.825  1.00 14.50 ? 531  HIS A C   1 
ATOM   3966 O  O   . HIS A 1 531 ? 65.823  32.787 99.261  1.00 14.75 ? 531  HIS A O   1 
ATOM   3967 C  CB  . HIS A 1 531 ? 65.686  29.486 98.963  1.00 14.61 ? 531  HIS A CB  1 
ATOM   3968 C  CG  . HIS A 1 531 ? 65.412  29.893 97.547  1.00 14.30 ? 531  HIS A CG  1 
ATOM   3969 N  ND1 . HIS A 1 531 ? 66.357  30.484 96.737  1.00 15.47 ? 531  HIS A ND1 1 
ATOM   3970 C  CD2 . HIS A 1 531 ? 64.280  29.809 96.809  1.00 17.19 ? 531  HIS A CD2 1 
ATOM   3971 C  CE1 . HIS A 1 531 ? 65.820  30.740 95.553  1.00 17.04 ? 531  HIS A CE1 1 
ATOM   3972 N  NE2 . HIS A 1 531 ? 64.560  30.348 95.575  1.00 18.28 ? 531  HIS A NE2 1 
ATOM   3973 N  N   . CYS A 1 532 ? 67.463  31.620 100.280 1.00 14.61 ? 532  CYS A N   1 
ATOM   3974 C  CA  . CYS A 1 532 ? 68.494  32.573 99.907  1.00 13.14 ? 532  CYS A CA  1 
ATOM   3975 C  C   . CYS A 1 532 ? 68.830  32.386 98.433  1.00 13.19 ? 532  CYS A C   1 
ATOM   3976 O  O   . CYS A 1 532 ? 68.871  31.252 97.934  1.00 15.02 ? 532  CYS A O   1 
ATOM   3977 C  CB  . CYS A 1 532 ? 69.738  32.360 100.772 1.00 13.80 ? 532  CYS A CB  1 
ATOM   3978 S  SG  . CYS A 1 532 ? 70.986  33.619 100.384 1.00 15.23 ? 532  CYS A SG  1 
ATOM   3979 N  N   . HIS A 1 533 ? 69.076  33.503 97.740  1.00 13.13 ? 533  HIS A N   1 
ATOM   3980 C  CA  . HIS A 1 533 ? 69.438  33.463 96.328  1.00 11.67 ? 533  HIS A CA  1 
ATOM   3981 C  C   . HIS A 1 533 ? 70.936  33.565 96.084  1.00 12.77 ? 533  HIS A C   1 
ATOM   3982 O  O   . HIS A 1 533 ? 71.371  33.686 94.934  1.00 13.34 ? 533  HIS A O   1 
ATOM   3983 C  CB  . HIS A 1 533 ? 68.680  34.505 95.503  1.00 12.48 ? 533  HIS A CB  1 
ATOM   3984 C  CG  . HIS A 1 533 ? 68.202  33.974 94.190  1.00 12.90 ? 533  HIS A CG  1 
ATOM   3985 N  ND1 . HIS A 1 533 ? 69.056  33.723 93.136  1.00 12.39 ? 533  HIS A ND1 1 
ATOM   3986 C  CD2 . HIS A 1 533 ? 66.959  33.659 93.754  1.00 14.57 ? 533  HIS A CD2 1 
ATOM   3987 C  CE1 . HIS A 1 533 ? 68.362  33.256 92.110  1.00 12.76 ? 533  HIS A CE1 1 
ATOM   3988 N  NE2 . HIS A 1 533 ? 67.085  33.214 92.455  1.00 16.71 ? 533  HIS A NE2 1 
ATOM   3989 N  N   . ILE A 1 534 ? 71.746  33.499 97.135  1.00 11.55 ? 534  ILE A N   1 
ATOM   3990 C  CA  . ILE A 1 534 ? 73.133  33.103 96.927  1.00 13.13 ? 534  ILE A CA  1 
ATOM   3991 C  C   . ILE A 1 534 ? 73.095  31.603 96.660  1.00 13.40 ? 534  ILE A C   1 
ATOM   3992 O  O   . ILE A 1 534 ? 72.695  30.820 97.524  1.00 12.59 ? 534  ILE A O   1 
ATOM   3993 C  CB  . ILE A 1 534 ? 74.002  33.466 98.138  1.00 14.14 ? 534  ILE A CB  1 
ATOM   3994 C  CG1 . ILE A 1 534 ? 74.148  34.996 98.209  1.00 13.96 ? 534  ILE A CG1 1 
ATOM   3995 C  CG2 . ILE A 1 534 ? 75.374  32.771 98.061  1.00 14.62 ? 534  ILE A CG2 1 
ATOM   3996 C  CD1 . ILE A 1 534 ? 74.693  35.536 99.550  1.00 14.64 ? 534  ILE A CD1 1 
ATOM   3997 N  N   . LEU A 1 535 ? 73.410  31.192 95.434  1.00 13.39 ? 535  LEU A N   1 
ATOM   3998 C  CA  . LEU A 1 535 ? 73.097  29.811 95.072  1.00 11.69 ? 535  LEU A CA  1 
ATOM   3999 C  C   . LEU A 1 535 ? 73.928  28.812 95.864  1.00 13.46 ? 535  LEU A C   1 
ATOM   4000 O  O   . LEU A 1 535 ? 73.464  27.690 96.142  1.00 13.41 ? 535  LEU A O   1 
ATOM   4001 C  CB  . LEU A 1 535 ? 73.265  29.609 93.563  1.00 13.88 ? 535  LEU A CB  1 
ATOM   4002 C  CG  . LEU A 1 535 ? 72.491  30.586 92.663  1.00 11.20 ? 535  LEU A CG  1 
ATOM   4003 C  CD1 . LEU A 1 535 ? 72.696  30.226 91.191  1.00 13.07 ? 535  LEU A CD1 1 
ATOM   4004 C  CD2 . LEU A 1 535 ? 71.000  30.604 93.020  1.00 13.31 ? 535  LEU A CD2 1 
ATOM   4005 N  N   . GLU A 1 536 ? 75.148  29.203 96.244  1.00 12.14 ? 536  GLU A N   1 
ATOM   4006 C  CA  . GLU A 1 536 ? 75.991  28.377 97.096  1.00 13.17 ? 536  GLU A CA  1 
ATOM   4007 C  C   . GLU A 1 536 ? 75.368  28.168 98.472  1.00 13.49 ? 536  GLU A C   1 
ATOM   4008 O  O   . GLU A 1 536 ? 75.725  27.204 99.158  1.00 17.22 ? 536  GLU A O   1 
ATOM   4009 C  CB  . GLU A 1 536 ? 77.360  29.034 97.225  1.00 14.68 ? 536  GLU A CB  1 
ATOM   4010 C  CG  . GLU A 1 536 ? 78.250  28.929 95.941  1.00 13.81 ? 536  GLU A CG  1 
ATOM   4011 C  CD  . GLU A 1 536 ? 77.788  29.717 94.723  1.00 15.89 ? 536  GLU A CD  1 
ATOM   4012 O  OE1 . GLU A 1 536 ? 77.088  30.738 94.871  1.00 15.63 ? 536  GLU A OE1 1 
ATOM   4013 O  OE2 . GLU A 1 536 ? 78.123  29.290 93.593  1.00 14.03 ? 536  GLU A OE2 1 
ATOM   4014 N  N   . HIS A 1 537 ? 74.498  29.073 98.917  1.00 12.71 ? 537  HIS A N   1 
ATOM   4015 C  CA  . HIS A 1 537 ? 73.766  28.902 100.172 1.00 13.85 ? 537  HIS A CA  1 
ATOM   4016 C  C   . HIS A 1 537 ? 72.508  28.089 99.969  1.00 13.84 ? 537  HIS A C   1 
ATOM   4017 O  O   . HIS A 1 537 ? 72.251  27.149 100.738 1.00 14.41 ? 537  HIS A O   1 
ATOM   4018 C  CB  . HIS A 1 537 ? 73.374  30.251 100.770 1.00 15.01 ? 537  HIS A CB  1 
ATOM   4019 C  CG  . HIS A 1 537 ? 74.537  31.088 101.171 1.00 14.99 ? 537  HIS A CG  1 
ATOM   4020 N  ND1 . HIS A 1 537 ? 74.387  32.361 101.666 1.00 17.03 ? 537  HIS A ND1 1 
ATOM   4021 C  CD2 . HIS A 1 537 ? 75.871  30.845 101.137 1.00 17.11 ? 537  HIS A CD2 1 
ATOM   4022 C  CE1 . HIS A 1 537 ? 75.576  32.874 101.918 1.00 17.22 ? 537  HIS A CE1 1 
ATOM   4023 N  NE2 . HIS A 1 537 ? 76.497  31.976 101.602 1.00 17.42 ? 537  HIS A NE2 1 
ATOM   4024 N  N   . GLU A 1 538 ? 71.747  28.401 98.912  1.00 13.35 ? 538  GLU A N   1 
ATOM   4025 C  CA  . GLU A 1 538 ? 70.539  27.651 98.570  1.00 13.89 ? 538  GLU A CA  1 
ATOM   4026 C  C   . GLU A 1 538 ? 70.812  26.155 98.513  1.00 15.75 ? 538  GLU A C   1 
ATOM   4027 O  O   . GLU A 1 538 ? 70.034  25.351 99.046  1.00 16.08 ? 538  GLU A O   1 
ATOM   4028 C  CB  . GLU A 1 538 ? 69.968  28.177 97.253  1.00 15.60 ? 538  GLU A CB  1 
ATOM   4029 C  CG  . GLU A 1 538 ? 68.814  27.384 96.706  1.00 18.22 ? 538  GLU A CG  1 
ATOM   4030 C  CD  . GLU A 1 538 ? 68.295  27.984 95.392  1.00 22.17 ? 538  GLU A CD  1 
ATOM   4031 O  OE1 . GLU A 1 538 ? 68.646  29.134 95.044  1.00 20.67 ? 538  GLU A OE1 1 
ATOM   4032 O  OE2 . GLU A 1 538 ? 67.572  27.278 94.678  1.00 26.39 ? 538  GLU A OE2 1 
ATOM   4033 N  N   . ASP A 1 539 ? 71.935  25.760 97.911  1.00 12.69 ? 539  ASP A N   1 
ATOM   4034 C  CA  . ASP A 1 539 ? 72.217  24.342 97.715  1.00 12.77 ? 539  ASP A CA  1 
ATOM   4035 C  C   . ASP A 1 539 ? 72.705  23.655 98.983  1.00 15.56 ? 539  ASP A C   1 
ATOM   4036 O  O   . ASP A 1 539 ? 72.786  22.421 98.996  1.00 15.45 ? 539  ASP A O   1 
ATOM   4037 C  CB  . ASP A 1 539 ? 73.288  24.216 96.629  1.00 15.52 ? 539  ASP A CB  1 
ATOM   4038 C  CG  . ASP A 1 539 ? 72.729  24.296 95.193  1.00 13.81 ? 539  ASP A CG  1 
ATOM   4039 O  OD1 . ASP A 1 539 ? 71.508  24.148 94.937  1.00 16.48 ? 539  ASP A OD1 1 
ATOM   4040 O  OD2 . ASP A 1 539 ? 73.552  24.532 94.278  1.00 14.28 ? 539  ASP A OD2 1 
ATOM   4041 N  N   . TYR A 1 540 ? 73.117  24.403 100.016 1.00 14.91 ? 540  TYR A N   1 
ATOM   4042 C  CA  . TYR A 1 540 ? 73.505  23.766 101.278 1.00 14.71 ? 540  TYR A CA  1 
ATOM   4043 C  C   . TYR A 1 540 ? 73.389  24.780 102.423 1.00 16.57 ? 540  TYR A C   1 
ATOM   4044 O  O   . TYR A 1 540 ? 74.394  25.363 102.833 1.00 17.49 ? 540  TYR A O   1 
ATOM   4045 C  CB  . TYR A 1 540 ? 74.930  23.252 101.161 1.00 15.66 ? 540  TYR A CB  1 
ATOM   4046 C  CG  . TYR A 1 540 ? 75.345  22.263 102.229 1.00 16.34 ? 540  TYR A CG  1 
ATOM   4047 C  CD1 . TYR A 1 540 ? 74.537  21.169 102.556 1.00 16.26 ? 540  TYR A CD1 1 
ATOM   4048 C  CD2 . TYR A 1 540 ? 76.559  22.402 102.890 1.00 16.56 ? 540  TYR A CD2 1 
ATOM   4049 C  CE1 . TYR A 1 540 ? 74.928  20.252 103.539 1.00 16.69 ? 540  TYR A CE1 1 
ATOM   4050 C  CE2 . TYR A 1 540 ? 76.965  21.486 103.870 1.00 19.15 ? 540  TYR A CE2 1 
ATOM   4051 C  CZ  . TYR A 1 540 ? 76.151  20.408 104.174 1.00 17.34 ? 540  TYR A CZ  1 
ATOM   4052 O  OH  . TYR A 1 540 ? 76.544  19.492 105.126 1.00 19.54 ? 540  TYR A OH  1 
ATOM   4053 N  N   . ASP A 1 541 ? 72.200  24.859 103.035 1.00 14.44 ? 541  ASP A N   1 
ATOM   4054 C  CA  . ASP A 1 541 ? 70.957  24.175 102.700 1.00 15.31 ? 541  ASP A CA  1 
ATOM   4055 C  C   . ASP A 1 541 ? 69.843  25.190 102.897 1.00 15.74 ? 541  ASP A C   1 
ATOM   4056 O  O   . ASP A 1 541 ? 68.867  24.922 103.624 1.00 15.04 ? 541  ASP A O   1 
ATOM   4057 C  CB  . ASP A 1 541 ? 70.776  22.972 103.634 1.00 16.32 ? 541  ASP A CB  1 
ATOM   4058 C  CG  . ASP A 1 541 ? 69.605  22.086 103.239 1.00 18.44 ? 541  ASP A CG  1 
ATOM   4059 O  OD1 . ASP A 1 541 ? 69.361  21.930 102.034 1.00 23.51 ? 541  ASP A OD1 1 
ATOM   4060 O  OD2 . ASP A 1 541 ? 68.946  21.537 104.152 1.00 21.70 ? 541  ASP A OD2 1 
ATOM   4061 N  N   . MET A 1 542 ? 70.016  26.389 102.339 1.00 14.60 ? 542  MET A N   1 
ATOM   4062 C  CA  . MET A 1 542 ? 69.290  27.551 102.847 1.00 14.81 ? 542  MET A CA  1 
ATOM   4063 C  C   . MET A 1 542 ? 68.021  27.807 102.021 1.00 13.55 ? 542  MET A C   1 
ATOM   4064 O  O   . MET A 1 542 ? 67.826  28.815 101.341 1.00 14.75 ? 542  MET A O   1 
ATOM   4065 C  CB  . MET A 1 542 ? 70.268  28.727 102.998 1.00 18.25 ? 542  MET A CB  1 
ATOM   4066 C  CG  . MET A 1 542 ? 69.757  29.945 103.727 1.00 18.70 ? 542  MET A CG  1 
ATOM   4067 S  SD  . MET A 1 542 ? 71.021  31.268 103.761 1.00 16.43 ? 542  MET A SD  1 
ATOM   4068 C  CE  . MET A 1 542 ? 70.806  31.939 105.404 1.00 22.07 ? 542  MET A CE  1 
ATOM   4069 N  N   . MET A 1 543 ? 67.145  26.806 102.084 1.00 14.69 ? 543  MET A N   1 
ATOM   4070 C  CA  . MET A 1 543 ? 65.898  26.740 101.337 1.00 14.98 ? 543  MET A CA  1 
ATOM   4071 C  C   . MET A 1 543 ? 64.888  25.956 102.162 1.00 14.90 ? 543  MET A C   1 
ATOM   4072 O  O   . MET A 1 543 ? 65.219  24.909 102.725 1.00 16.10 ? 543  MET A O   1 
ATOM   4073 C  CB  . MET A 1 543 ? 66.118  26.006 100.006 1.00 15.93 ? 543  MET A CB  1 
ATOM   4074 C  CG  . MET A 1 543 ? 64.871  25.867 99.149  1.00 15.94 ? 543  MET A CG  1 
ATOM   4075 S  SD  . MET A 1 543 ? 65.169  25.525 97.393  1.00 19.40 ? 543  MET A SD  1 
ATOM   4076 C  CE  . MET A 1 543 ? 65.631  23.805 97.498  1.00 19.09 ? 543  MET A CE  1 
ATOM   4077 N  N   . ARG A 1 544 ? 63.646  26.439 102.192 1.00 15.39 ? 544  ARG A N   1 
ATOM   4078 C  CA  . ARG A 1 544 ? 62.593  25.812 102.973 1.00 15.86 ? 544  ARG A CA  1 
ATOM   4079 C  C   . ARG A 1 544 ? 61.312  25.759 102.155 1.00 16.17 ? 544  ARG A C   1 
ATOM   4080 O  O   . ARG A 1 544 ? 61.074  26.622 101.289 1.00 16.43 ? 544  ARG A O   1 
ATOM   4081 C  CB  . ARG A 1 544 ? 62.331  26.611 104.261 1.00 18.09 ? 544  ARG A CB  1 
ATOM   4082 C  CG  . ARG A 1 544 ? 63.462  26.481 105.284 1.00 16.82 ? 544  ARG A CG  1 
ATOM   4083 C  CD  . ARG A 1 544 ? 63.430  25.148 105.989 1.00 19.10 ? 544  ARG A CD  1 
ATOM   4084 N  NE  . ARG A 1 544 ? 62.260  25.042 106.852 1.00 17.83 ? 544  ARG A NE  1 
ATOM   4085 C  CZ  . ARG A 1 544 ? 61.604  23.914 107.062 1.00 18.25 ? 544  ARG A CZ  1 
ATOM   4086 N  NH1 . ARG A 1 544 ? 62.004  22.770 106.521 1.00 21.28 ? 544  ARG A NH1 1 
ATOM   4087 N  NH2 . ARG A 1 544 ? 60.518  23.927 107.828 1.00 21.05 ? 544  ARG A NH2 1 
ATOM   4088 N  N   . PRO A 1 545 ? 60.470  24.760 102.396 1.00 16.73 ? 545  PRO A N   1 
ATOM   4089 C  CA  . PRO A 1 545 ? 59.163  24.736 101.724 1.00 17.70 ? 545  PRO A CA  1 
ATOM   4090 C  C   . PRO A 1 545 ? 58.266  25.875 102.206 1.00 18.74 ? 545  PRO A C   1 
ATOM   4091 O  O   . PRO A 1 545 ? 58.353  26.334 103.346 1.00 20.47 ? 545  PRO A O   1 
ATOM   4092 C  CB  . PRO A 1 545 ? 58.564  23.383 102.131 1.00 19.23 ? 545  PRO A CB  1 
ATOM   4093 C  CG  . PRO A 1 545 ? 59.389  22.885 103.269 1.00 25.05 ? 545  PRO A CG  1 
ATOM   4094 C  CD  . PRO A 1 545 ? 60.692  23.617 103.301 1.00 19.69 ? 545  PRO A CD  1 
ATOM   4095 N  N   . MET A 1 546 ? 57.406  26.328 101.301 1.00 18.75 ? 546  MET A N   1 
ATOM   4096 C  CA  . MET A 1 546 ? 56.272  27.210 101.573 1.00 20.18 ? 546  MET A CA  1 
ATOM   4097 C  C   . MET A 1 546 ? 55.012  26.589 101.012 1.00 20.56 ? 546  MET A C   1 
ATOM   4098 O  O   . MET A 1 546 ? 54.800  26.614 99.799  1.00 20.63 ? 546  MET A O   1 
ATOM   4099 C  CB  . MET A 1 546 ? 56.457  28.578 100.924 1.00 19.96 ? 546  MET A CB  1 
ATOM   4100 C  CG  . MET A 1 546 ? 55.550  29.678 101.501 1.00 18.44 ? 546  MET A CG  1 
ATOM   4101 S  SD  . MET A 1 546 ? 55.879  31.296 100.803 1.00 20.53 ? 546  MET A SD  1 
ATOM   4102 C  CE  . MET A 1 546 ? 55.588  31.033 99.031  1.00 21.24 ? 546  MET A CE  1 
ATOM   4103 N  N   . ARG A 1 547 ? 54.154  26.077 101.873 1.00 21.40 ? 547  ARG A N   1 
ATOM   4104 C  CA  . ARG A 1 547 ? 52.907  25.489 101.419 1.00 22.61 ? 547  ARG A CA  1 
ATOM   4105 C  C   . ARG A 1 547 ? 51.808  26.533 101.545 1.00 24.11 ? 547  ARG A C   1 
ATOM   4106 O  O   . ARG A 1 547 ? 51.358  26.834 102.652 1.00 25.62 ? 547  ARG A O   1 
ATOM   4107 C  CB  . ARG A 1 547 ? 52.575  24.249 102.234 1.00 25.25 ? 547  ARG A CB  1 
ATOM   4108 C  CG  . ARG A 1 547 ? 51.390  23.512 101.688 1.00 26.78 ? 547  ARG A CG  1 
ATOM   4109 C  CD  . ARG A 1 547 ? 50.933  22.439 102.653 1.00 32.95 ? 547  ARG A CD  1 
ATOM   4110 N  NE  . ARG A 1 547 ? 51.906  21.358 102.723 1.00 38.98 ? 547  ARG A NE  1 
ATOM   4111 C  CZ  . ARG A 1 547 ? 51.983  20.490 103.725 1.00 37.21 ? 547  ARG A CZ  1 
ATOM   4112 N  NH1 . ARG A 1 547 ? 51.140  20.534 104.744 1.00 40.96 ? 547  ARG A NH1 1 
ATOM   4113 N  NH2 . ARG A 1 547 ? 52.930  19.559 103.703 1.00 40.39 ? 547  ARG A NH2 1 
ATOM   4114 N  N   . VAL A 1 548 ? 51.358  27.071 100.423 1.00 22.61 ? 548  VAL A N   1 
ATOM   4115 C  CA  . VAL A 1 548 ? 50.270  28.044 100.439 1.00 24.46 ? 548  VAL A CA  1 
ATOM   4116 C  C   . VAL A 1 548 ? 48.952  27.278 100.432 1.00 25.61 ? 548  VAL A C   1 
ATOM   4117 O  O   . VAL A 1 548 ? 48.730  26.422 99.569  1.00 26.39 ? 548  VAL A O   1 
ATOM   4118 C  CB  . VAL A 1 548 ? 50.387  28.994 99.235  1.00 21.95 ? 548  VAL A CB  1 
ATOM   4119 C  CG1 . VAL A 1 548 ? 49.244  30.005 99.229  1.00 25.48 ? 548  VAL A CG1 1 
ATOM   4120 C  CG2 . VAL A 1 548 ? 51.731  29.707 99.272  1.00 23.05 ? 548  VAL A CG2 1 
ATOM   4121 N  N   . VAL A 1 549 ? 48.079  27.564 101.406 1.00 27.36 ? 549  VAL A N   1 
ATOM   4122 C  CA  . VAL A 1 549 ? 46.876  26.769 101.625 1.00 29.47 ? 549  VAL A CA  1 
ATOM   4123 C  C   . VAL A 1 549 ? 45.631  27.640 101.484 1.00 30.93 ? 549  VAL A C   1 
ATOM   4124 O  O   . VAL A 1 549 ? 45.673  28.861 101.649 1.00 30.64 ? 549  VAL A O   1 
ATOM   4125 C  CB  . VAL A 1 549 ? 46.881  26.049 102.991 1.00 34.57 ? 549  VAL A CB  1 
ATOM   4126 C  CG1 . VAL A 1 549 ? 48.072  25.120 103.098 1.00 28.18 ? 549  VAL A CG1 1 
ATOM   4127 C  CG2 . VAL A 1 549 ? 46.879  27.053 104.133 1.00 35.03 ? 549  VAL A CG2 1 
ATOM   4128 N  N   . GLU A 1 550 ? 44.511  26.992 101.171 1.00 34.71 ? 550  GLU A N   1 
ATOM   4129 C  CA  . GLU A 1 550 ? 43.240  27.698 101.029 1.00 42.80 ? 550  GLU A CA  1 
ATOM   4130 C  C   . GLU A 1 550 ? 42.665  27.977 102.404 1.00 40.83 ? 550  GLU A C   1 
ATOM   4131 O  O   . GLU A 1 550 ? 42.818  27.157 103.310 1.00 45.04 ? 550  GLU A O   1 
ATOM   4132 C  CB  . GLU A 1 550 ? 42.240  26.874 100.213 1.00 43.54 ? 550  GLU A CB  1 
ATOM   4133 C  CG  . GLU A 1 550 ? 42.480  26.961 98.712  1.00 46.10 ? 550  GLU A CG  1 
ATOM   4134 C  CD  . GLU A 1 550 ? 41.873  28.205 98.073  1.00 52.67 ? 550  GLU A CD  1 
ATOM   4135 O  OE1 . GLU A 1 550 ? 41.482  29.143 98.812  1.00 57.92 ? 550  GLU A OE1 1 
ATOM   4136 O  OE2 . GLU A 1 550 ? 41.832  28.262 96.824  1.00 48.92 ? 550  GLU A OE2 1 
HETATM 4137 MN MN  . MN  B 2 .   ? 65.575  33.150 90.884  0.68 12.86 ? 601  MN  A MN  1 
HETATM 4138 CU CU  . CU  C 3 .   ? 63.704  29.953 94.013  0.20 18.48 ? 602  CU  A CU  1 
HETATM 4139 CU CU  . CU  D 3 .   ? 72.624  33.361 101.849 0.65 10.17 ? 603  CU  A CU  1 
HETATM 4140 O  O   . HOH E 4 .   ? 64.989  44.981 85.344  1.00 32.43 ? 701  HOH A O   1 
HETATM 4141 O  O   . HOH E 4 .   ? 73.283  57.146 63.852  1.00 45.71 ? 702  HOH A O   1 
HETATM 4142 O  O   . HOH E 4 .   ? 67.266  12.983 72.678  1.00 42.23 ? 703  HOH A O   1 
HETATM 4143 O  O   . HOH E 4 .   ? 90.608  30.699 102.974 1.00 49.64 ? 704  HOH A O   1 
HETATM 4144 O  O   . HOH E 4 .   ? 84.934  24.286 86.546  1.00 32.19 ? 705  HOH A O   1 
HETATM 4145 O  O   . HOH E 4 .   ? 54.543  53.586 73.734  1.00 50.49 ? 706  HOH A O   1 
HETATM 4146 O  O   . HOH E 4 .   ? 52.212  49.938 98.569  1.00 34.90 ? 707  HOH A O   1 
HETATM 4147 O  O   . HOH E 4 .   ? 48.312  35.687 72.494  1.00 38.38 ? 708  HOH A O   1 
HETATM 4148 O  O   . HOH E 4 .   ? 51.801  56.603 97.165  1.00 48.89 ? 709  HOH A O   1 
HETATM 4149 O  O   . HOH E 4 .   ? 68.218  10.917 91.220  1.00 25.19 ? 710  HOH A O   1 
HETATM 4150 O  O   . HOH E 4 .   ? 73.639  46.915 116.571 1.00 39.50 ? 711  HOH A O   1 
HETATM 4151 O  O   . HOH E 4 .   ? 42.592  34.178 104.714 1.00 36.41 ? 712  HOH A O   1 
HETATM 4152 O  O   . HOH E 4 .   ? 63.585  31.490 113.155 1.00 27.12 ? 713  HOH A O   1 
HETATM 4153 O  O   . HOH E 4 .   ? 74.365  63.703 89.916  1.00 43.13 ? 714  HOH A O   1 
HETATM 4154 O  O   . HOH E 4 .   ? 45.175  37.295 89.633  1.00 50.99 ? 715  HOH A O   1 
HETATM 4155 O  O   . HOH E 4 .   ? 45.853  25.736 84.762  1.00 30.42 ? 716  HOH A O   1 
HETATM 4156 O  O   . HOH E 4 .   ? 44.851  24.457 101.027 1.00 53.16 ? 717  HOH A O   1 
HETATM 4157 O  O   . HOH E 4 .   ? 54.489  35.315 73.993  1.00 19.36 ? 718  HOH A O   1 
HETATM 4158 O  O   . HOH E 4 .   ? 76.702  15.267 107.105 1.00 49.45 ? 719  HOH A O   1 
HETATM 4159 O  O   . HOH E 4 .   ? 72.560  66.226 72.932  1.00 37.61 ? 720  HOH A O   1 
HETATM 4160 O  O   . HOH E 4 .   ? 48.686  32.710 106.815 1.00 26.29 ? 721  HOH A O   1 
HETATM 4161 O  O   . HOH E 4 .   ? 73.224  57.145 96.022  1.00 38.63 ? 722  HOH A O   1 
HETATM 4162 O  O   . HOH E 4 .   ? 88.607  51.572 82.319  1.00 29.82 ? 723  HOH A O   1 
HETATM 4163 O  O   . HOH E 4 .   ? 83.596  59.172 89.497  1.00 38.03 ? 724  HOH A O   1 
HETATM 4164 O  O   . HOH E 4 .   ? 71.314  52.260 70.167  1.00 29.48 ? 725  HOH A O   1 
HETATM 4165 O  O   . HOH E 4 .   ? 49.040  34.194 86.841  1.00 19.27 ? 726  HOH A O   1 
HETATM 4166 O  O   . HOH E 4 .   ? 68.818  64.520 85.247  1.00 36.98 ? 727  HOH A O   1 
HETATM 4167 O  O   . HOH E 4 .   ? 92.851  32.591 87.748  1.00 33.92 ? 728  HOH A O   1 
HETATM 4168 O  O   . HOH E 4 .   ? 64.087  49.972 117.588 1.00 38.65 ? 729  HOH A O   1 
HETATM 4169 O  O   . HOH E 4 .   ? 72.177  62.576 63.512  1.00 41.06 ? 730  HOH A O   1 
HETATM 4170 O  O   . HOH E 4 .   ? 82.461  46.429 99.387  1.00 40.76 ? 731  HOH A O   1 
HETATM 4171 O  O   . HOH E 4 .   ? 75.522  66.499 74.940  1.00 43.25 ? 732  HOH A O   1 
HETATM 4172 O  O   . HOH E 4 .   ? 73.775  47.376 99.383  1.00 36.13 ? 733  HOH A O   1 
HETATM 4173 O  O   . HOH E 4 .   ? 66.135  63.864 76.946  1.00 29.17 ? 734  HOH A O   1 
HETATM 4174 O  O   . HOH E 4 .   ? 75.619  57.425 89.134  1.00 18.40 ? 735  HOH A O   1 
HETATM 4175 O  O   . HOH E 4 .   ? 77.200  28.456 69.772  1.00 34.34 ? 736  HOH A O   1 
HETATM 4176 O  O   . HOH E 4 .   ? 71.368  20.341 98.301  1.00 24.50 ? 737  HOH A O   1 
HETATM 4177 O  O   . HOH E 4 .   ? 59.428  27.612 112.755 1.00 43.83 ? 738  HOH A O   1 
HETATM 4178 O  O   . HOH E 4 .   ? 63.317  36.556 67.352  1.00 33.56 ? 739  HOH A O   1 
HETATM 4179 O  O   . HOH E 4 .   ? 75.078  30.271 70.833  1.00 34.23 ? 740  HOH A O   1 
HETATM 4180 O  O   . HOH E 4 .   ? 74.908  48.366 69.633  1.00 35.36 ? 741  HOH A O   1 
HETATM 4181 O  O   . HOH E 4 .   ? 62.496  28.097 70.697  1.00 36.68 ? 742  HOH A O   1 
HETATM 4182 O  O   . HOH E 4 .   ? 68.347  23.401 100.119 1.00 27.18 ? 743  HOH A O   1 
HETATM 4183 O  O   . HOH E 4 .   ? 42.015  32.977 95.650  1.00 40.56 ? 744  HOH A O   1 
HETATM 4184 O  O   . HOH E 4 .   ? 91.729  43.954 82.238  1.00 23.00 ? 745  HOH A O   1 
HETATM 4185 O  O   . HOH E 4 .   ? 85.418  50.947 92.929  1.00 34.68 ? 746  HOH A O   1 
HETATM 4186 O  O   . HOH E 4 .   ? 58.774  11.733 89.171  1.00 23.39 ? 747  HOH A O   1 
HETATM 4187 O  O   . HOH E 4 .   ? 70.080  41.042 120.524 1.00 21.98 ? 748  HOH A O   1 
HETATM 4188 O  O   . HOH E 4 .   ? 49.256  54.757 79.971  1.00 39.54 ? 749  HOH A O   1 
HETATM 4189 O  O   . HOH E 4 .   ? 94.354  25.208 99.673  1.00 50.67 ? 750  HOH A O   1 
HETATM 4190 O  O   . HOH E 4 .   ? 52.617  39.199 73.512  1.00 32.02 ? 751  HOH A O   1 
HETATM 4191 O  O   . HOH E 4 .   ? 79.016  35.323 92.129  1.00 13.88 ? 752  HOH A O   1 
HETATM 4192 O  O   . HOH E 4 .   ? 58.700  25.812 105.907 1.00 18.88 ? 753  HOH A O   1 
HETATM 4193 O  O   . HOH E 4 .   ? 58.999  19.625 83.386  1.00 16.93 ? 754  HOH A O   1 
HETATM 4194 O  O   . HOH E 4 .   ? 96.132  36.408 72.745  1.00 47.24 ? 755  HOH A O   1 
HETATM 4195 O  O   . HOH E 4 .   ? 85.462  63.844 85.182  1.00 48.88 ? 756  HOH A O   1 
HETATM 4196 O  O   . HOH E 4 .   ? 67.341  24.654 94.448  1.00 17.39 ? 757  HOH A O   1 
HETATM 4197 O  O   . HOH E 4 .   ? 59.822  50.219 77.014  1.00 19.56 ? 758  HOH A O   1 
HETATM 4198 O  O   . HOH E 4 .   ? 77.661  8.644  96.290  1.00 36.09 ? 759  HOH A O   1 
HETATM 4199 O  O   . HOH E 4 .   ? 73.620  45.352 114.312 1.00 35.04 ? 760  HOH A O   1 
HETATM 4200 O  O   . HOH E 4 .   ? 59.066  10.752 81.973  1.00 41.72 ? 761  HOH A O   1 
HETATM 4201 O  O   . HOH E 4 .   ? 66.616  63.550 81.300  1.00 35.32 ? 762  HOH A O   1 
HETATM 4202 O  O   . HOH E 4 .   ? 58.958  20.096 85.978  1.00 15.26 ? 763  HOH A O   1 
HETATM 4203 O  O   . HOH E 4 .   ? 75.678  36.821 74.483  1.00 14.09 ? 764  HOH A O   1 
HETATM 4204 O  O   . HOH E 4 .   ? 65.825  45.957 124.064 1.00 44.78 ? 765  HOH A O   1 
HETATM 4205 O  O   . HOH E 4 .   ? 67.019  24.668 83.381  1.00 14.34 ? 766  HOH A O   1 
HETATM 4206 O  O   . HOH E 4 .   ? 84.044  21.059 75.917  1.00 34.70 ? 767  HOH A O   1 
HETATM 4207 O  O   . HOH E 4 .   ? 57.917  51.218 105.491 1.00 47.12 ? 768  HOH A O   1 
HETATM 4208 O  O   . HOH E 4 .   ? 70.633  45.290 97.269  1.00 17.67 ? 769  HOH A O   1 
HETATM 4209 O  O   . HOH E 4 .   ? 54.477  20.444 109.012 1.00 35.12 ? 770  HOH A O   1 
HETATM 4210 O  O   . HOH E 4 .   ? 49.308  26.661 92.753  1.00 22.92 ? 771  HOH A O   1 
HETATM 4211 O  O   . HOH E 4 .   ? 55.342  49.650 109.121 1.00 38.07 ? 772  HOH A O   1 
HETATM 4212 O  O   . HOH E 4 .   ? 66.872  17.359 110.175 1.00 57.05 ? 773  HOH A O   1 
HETATM 4213 O  O   . HOH E 4 .   ? 54.298  62.649 93.709  1.00 36.38 ? 774  HOH A O   1 
HETATM 4214 O  O   . HOH E 4 .   ? 53.933  49.822 92.175  1.00 31.36 ? 775  HOH A O   1 
HETATM 4215 O  O   . HOH E 4 .   ? 45.546  48.043 102.937 1.00 31.20 ? 776  HOH A O   1 
HETATM 4216 O  O   . HOH E 4 .   ? 89.285  34.039 84.876  1.00 15.31 ? 777  HOH A O   1 
HETATM 4217 O  O   . HOH E 4 .   ? 87.550  26.267 72.751  1.00 35.98 ? 778  HOH A O   1 
HETATM 4218 O  O   . HOH E 4 .   ? 76.253  42.953 124.077 1.00 36.76 ? 779  HOH A O   1 
HETATM 4219 O  O   . HOH E 4 .   ? 54.876  60.579 79.019  1.00 37.25 ? 780  HOH A O   1 
HETATM 4220 O  O   . HOH E 4 .   ? 58.782  28.109 85.826  1.00 13.70 ? 781  HOH A O   1 
HETATM 4221 O  O   . HOH E 4 .   ? 85.039  32.345 75.718  1.00 14.74 ? 782  HOH A O   1 
HETATM 4222 O  O   . HOH E 4 .   ? 47.801  21.951 86.456  1.00 26.58 ? 783  HOH A O   1 
HETATM 4223 O  O   . HOH E 4 .   ? 73.840  12.993 98.540  1.00 22.93 ? 784  HOH A O   1 
HETATM 4224 O  O   . HOH E 4 .   ? 46.112  34.277 81.676  1.00 29.26 ? 785  HOH A O   1 
HETATM 4225 O  O   . HOH E 4 .   ? 86.362  46.223 69.512  1.00 46.75 ? 786  HOH A O   1 
HETATM 4226 O  O   . HOH E 4 .   ? 49.820  44.422 78.220  1.00 31.48 ? 787  HOH A O   1 
HETATM 4227 O  O   . HOH E 4 .   ? 96.672  41.048 76.635  1.00 31.66 ? 788  HOH A O   1 
HETATM 4228 O  O   . HOH E 4 .   ? 52.879  50.161 105.133 1.00 47.27 ? 789  HOH A O   1 
HETATM 4229 O  O   . HOH E 4 .   ? 68.947  47.522 71.265  1.00 30.65 ? 790  HOH A O   1 
HETATM 4230 O  O   . HOH E 4 .   ? 73.839  45.830 70.889  1.00 31.08 ? 791  HOH A O   1 
HETATM 4231 O  O   . HOH E 4 .   ? 56.950  32.130 91.786  1.00 16.32 ? 792  HOH A O   1 
HETATM 4232 O  O   . HOH E 4 .   ? 76.304  62.363 92.161  1.00 45.11 ? 793  HOH A O   1 
HETATM 4233 O  O   . HOH E 4 .   ? 69.594  28.386 68.664  1.00 39.26 ? 794  HOH A O   1 
HETATM 4234 O  O   . HOH E 4 .   ? 87.185  33.292 91.054  1.00 22.82 ? 795  HOH A O   1 
HETATM 4235 O  O   . HOH E 4 .   ? 52.672  14.096 85.433  1.00 21.68 ? 796  HOH A O   1 
HETATM 4236 O  O   . HOH E 4 .   ? 87.411  28.791 100.157 1.00 19.66 ? 797  HOH A O   1 
HETATM 4237 O  O   . HOH E 4 .   ? 66.709  45.636 72.872  1.00 31.93 ? 798  HOH A O   1 
HETATM 4238 O  O   . HOH E 4 .   ? 57.240  62.921 72.936  1.00 47.23 ? 799  HOH A O   1 
HETATM 4239 O  O   . HOH E 4 .   ? 49.674  56.138 94.662  1.00 34.31 ? 800  HOH A O   1 
HETATM 4240 O  O   . HOH E 4 .   ? 49.376  38.144 96.049  1.00 41.35 ? 801  HOH A O   1 
HETATM 4241 O  O   . HOH E 4 .   ? 79.135  25.271 102.773 1.00 19.27 ? 802  HOH A O   1 
HETATM 4242 O  O   . HOH E 4 .   ? 90.719  26.114 74.414  1.00 35.72 ? 803  HOH A O   1 
HETATM 4243 O  O   . HOH E 4 .   ? 47.898  54.879 83.744  1.00 39.55 ? 804  HOH A O   1 
HETATM 4244 O  O   . HOH E 4 .   ? 87.319  26.774 76.309  1.00 21.24 ? 805  HOH A O   1 
HETATM 4245 O  O   . HOH E 4 .   ? 66.560  40.699 74.726  1.00 15.88 ? 806  HOH A O   1 
HETATM 4246 O  O   . HOH E 4 .   ? 75.906  44.697 104.012 1.00 37.28 ? 807  HOH A O   1 
HETATM 4247 O  O   . HOH E 4 .   ? 59.226  61.413 89.533  1.00 33.54 ? 808  HOH A O   1 
HETATM 4248 O  O   . HOH E 4 .   ? 62.910  45.889 87.052  1.00 19.01 ? 809  HOH A O   1 
HETATM 4249 O  O   . HOH E 4 .   ? 53.855  45.588 72.483  1.00 45.60 ? 810  HOH A O   1 
HETATM 4250 O  O   . HOH E 4 .   ? 57.019  30.524 110.027 1.00 24.55 ? 811  HOH A O   1 
HETATM 4251 O  O   . HOH E 4 .   ? 83.200  37.910 71.435  1.00 23.40 ? 812  HOH A O   1 
HETATM 4252 O  O   . HOH E 4 .   ? 92.933  30.038 75.980  1.00 30.93 ? 813  HOH A O   1 
HETATM 4253 O  O   . HOH E 4 .   ? 65.530  60.136 94.864  1.00 35.84 ? 814  HOH A O   1 
HETATM 4254 O  O   . HOH E 4 .   ? 51.697  40.918 98.293  1.00 21.68 ? 815  HOH A O   1 
HETATM 4255 O  O   . HOH E 4 .   ? 69.153  23.203 95.846  1.00 16.93 ? 816  HOH A O   1 
HETATM 4256 O  O   . HOH E 4 .   ? 56.359  58.301 79.181  1.00 27.36 ? 817  HOH A O   1 
HETATM 4257 O  O   . HOH E 4 .   ? 92.451  22.082 77.509  1.00 25.91 ? 818  HOH A O   1 
HETATM 4258 O  O   . HOH E 4 .   ? 56.657  20.395 68.793  1.00 49.80 ? 819  HOH A O   1 
HETATM 4259 O  O   . HOH E 4 .   ? 82.240  23.494 94.697  1.00 16.13 ? 820  HOH A O   1 
HETATM 4260 O  O   . HOH E 4 .   ? 59.520  15.460 97.779  1.00 44.52 ? 821  HOH A O   1 
HETATM 4261 O  O   . HOH E 4 .   ? 60.946  41.873 116.864 1.00 49.30 ? 822  HOH A O   1 
HETATM 4262 O  O   . HOH E 4 .   ? 75.317  32.916 81.954  1.00 15.73 ? 823  HOH A O   1 
HETATM 4263 O  O   . HOH E 4 .   ? 57.543  46.224 78.794  1.00 29.33 ? 824  HOH A O   1 
HETATM 4264 O  O   . HOH E 4 .   ? 65.065  56.431 66.302  1.00 38.95 ? 825  HOH A O   1 
HETATM 4265 O  O   . HOH E 4 .   ? 67.837  19.071 104.027 1.00 27.93 ? 826  HOH A O   1 
HETATM 4266 O  O   . HOH E 4 .   ? 77.885  7.656  92.557  1.00 36.94 ? 827  HOH A O   1 
HETATM 4267 O  O   . HOH E 4 .   ? 68.445  41.278 107.987 1.00 19.15 ? 828  HOH A O   1 
HETATM 4268 O  O   . HOH E 4 .   ? 73.444  31.922 83.817  1.00 12.55 ? 829  HOH A O   1 
HETATM 4269 O  O   . HOH E 4 .   ? 54.022  47.190 86.453  1.00 21.59 ? 830  HOH A O   1 
HETATM 4270 O  O   . HOH E 4 .   ? 87.999  27.463 96.509  1.00 19.69 ? 831  HOH A O   1 
HETATM 4271 O  O   . HOH E 4 .   ? 59.536  21.215 81.086  1.00 19.78 ? 832  HOH A O   1 
HETATM 4272 O  O   . HOH E 4 .   ? 67.056  62.864 74.444  1.00 23.46 ? 833  HOH A O   1 
HETATM 4273 O  O   . HOH E 4 .   ? 74.393  45.647 108.753 1.00 38.20 ? 834  HOH A O   1 
HETATM 4274 O  O   . HOH E 4 .   ? 44.638  40.149 104.549 1.00 35.63 ? 835  HOH A O   1 
HETATM 4275 O  O   . HOH E 4 .   ? 45.483  40.093 86.235  1.00 36.59 ? 836  HOH A O   1 
HETATM 4276 O  O   . HOH E 4 .   ? 89.234  43.554 91.228  1.00 28.46 ? 837  HOH A O   1 
HETATM 4277 O  O   . HOH E 4 .   ? 61.635  47.301 114.320 1.00 39.11 ? 838  HOH A O   1 
HETATM 4278 O  O   . HOH E 4 .   ? 62.807  41.685 121.162 1.00 38.21 ? 839  HOH A O   1 
HETATM 4279 O  O   . HOH E 4 .   ? 81.894  52.511 70.644  1.00 22.63 ? 840  HOH A O   1 
HETATM 4280 O  O   . HOH E 4 .   ? 74.117  13.257 90.781  1.00 18.87 ? 841  HOH A O   1 
HETATM 4281 O  O   . HOH E 4 .   ? 60.806  29.038 114.667 1.00 47.82 ? 842  HOH A O   1 
HETATM 4282 O  O   . HOH E 4 .   ? 73.675  19.181 74.567  1.00 20.14 ? 843  HOH A O   1 
HETATM 4283 O  O   . HOH E 4 .   ? 70.166  54.468 95.652  1.00 30.19 ? 844  HOH A O   1 
HETATM 4284 O  O   . HOH E 4 .   ? 57.876  30.315 88.218  1.00 15.29 ? 845  HOH A O   1 
HETATM 4285 O  O   . HOH E 4 .   ? 83.560  25.363 79.894  1.00 16.53 ? 846  HOH A O   1 
HETATM 4286 O  O   . HOH E 4 .   ? 50.964  48.037 76.866  1.00 30.88 ? 847  HOH A O   1 
HETATM 4287 O  O   . HOH E 4 .   ? 72.934  50.708 71.089  1.00 37.58 ? 848  HOH A O   1 
HETATM 4288 O  O   . HOH E 4 .   ? 97.892  26.661 81.543  1.00 26.05 ? 849  HOH A O   1 
HETATM 4289 O  O   . HOH E 4 .   ? 78.918  14.807 86.087  1.00 20.27 ? 850  HOH A O   1 
HETATM 4290 O  O   . HOH E 4 .   ? 48.130  23.638 89.578  1.00 24.01 ? 851  HOH A O   1 
HETATM 4291 O  O   . HOH E 4 .   ? 65.777  48.193 122.379 1.00 45.96 ? 852  HOH A O   1 
HETATM 4292 O  O   . HOH E 4 .   ? 44.866  24.426 78.313  1.00 20.41 ? 853  HOH A O   1 
HETATM 4293 O  O   . HOH E 4 .   ? 72.193  13.078 77.468  1.00 32.69 ? 854  HOH A O   1 
HETATM 4294 O  O   . HOH E 4 .   ? 43.754  29.576 74.632  1.00 44.16 ? 855  HOH A O   1 
HETATM 4295 O  O   . HOH E 4 .   ? 56.611  32.263 65.571  1.00 41.10 ? 856  HOH A O   1 
HETATM 4296 O  O   . HOH E 4 .   ? 50.881  58.137 83.079  1.00 32.95 ? 857  HOH A O   1 
HETATM 4297 O  O   . HOH E 4 .   ? 50.626  24.847 85.944  1.00 17.41 ? 858  HOH A O   1 
HETATM 4298 O  O   . HOH E 4 .   ? 89.819  22.871 90.595  1.00 21.91 ? 859  HOH A O   1 
HETATM 4299 O  O   . HOH E 4 .   ? 81.708  24.252 102.286 1.00 19.21 ? 860  HOH A O   1 
HETATM 4300 O  O   . HOH E 4 .   ? 42.999  30.950 80.339  1.00 37.93 ? 861  HOH A O   1 
HETATM 4301 O  O   . HOH E 4 .   ? 67.222  26.137 105.616 1.00 17.54 ? 862  HOH A O   1 
HETATM 4302 O  O   . HOH E 4 .   ? 83.591  41.254 69.513  1.00 45.52 ? 863  HOH A O   1 
HETATM 4303 O  O   . HOH E 4 .   ? 59.884  47.600 98.876  1.00 18.02 ? 864  HOH A O   1 
HETATM 4304 O  O   . HOH E 4 .   ? 79.238  17.974 79.767  1.00 24.87 ? 865  HOH A O   1 
HETATM 4305 O  O   . HOH E 4 .   ? 67.289  53.907 104.285 1.00 40.69 ? 866  HOH A O   1 
HETATM 4306 O  O   . HOH E 4 .   ? 87.244  22.957 89.140  1.00 19.60 ? 867  HOH A O   1 
HETATM 4307 O  O   . HOH E 4 .   ? 74.063  64.556 92.538  1.00 50.01 ? 868  HOH A O   1 
HETATM 4308 O  O   . HOH E 4 .   ? 71.806  33.790 92.148  1.00 14.75 ? 869  HOH A O   1 
HETATM 4309 O  O   . HOH E 4 .   ? 44.446  27.091 81.615  1.00 22.76 ? 870  HOH A O   1 
HETATM 4310 O  O   . HOH E 4 .   ? 61.016  19.672 102.019 1.00 31.89 ? 871  HOH A O   1 
HETATM 4311 O  O   . HOH E 4 .   ? 81.413  13.161 89.691  1.00 27.11 ? 872  HOH A O   1 
HETATM 4312 O  O   . HOH E 4 .   ? 71.483  20.445 101.153 1.00 30.08 ? 873  HOH A O   1 
HETATM 4313 O  O   . HOH E 4 .   ? 88.109  18.277 95.112  1.00 21.34 ? 874  HOH A O   1 
HETATM 4314 O  O   . HOH E 4 .   ? 75.766  38.408 125.602 1.00 26.02 ? 875  HOH A O   1 
HETATM 4315 O  O   . HOH E 4 .   ? 50.672  35.482 93.653  1.00 24.48 ? 876  HOH A O   1 
HETATM 4316 O  O   . HOH E 4 .   ? 50.743  39.622 113.624 1.00 43.91 ? 877  HOH A O   1 
HETATM 4317 O  O   . HOH E 4 .   ? 90.657  23.222 97.125  1.00 22.48 ? 878  HOH A O   1 
HETATM 4318 O  O   . HOH E 4 .   ? 71.637  35.455 73.638  1.00 17.65 ? 879  HOH A O   1 
HETATM 4319 O  O   . HOH E 4 .   ? 85.613  23.865 104.008 1.00 33.73 ? 880  HOH A O   1 
HETATM 4320 O  O   . HOH E 4 .   ? 67.257  36.885 77.687  1.00 12.75 ? 881  HOH A O   1 
HETATM 4321 O  O   . HOH E 4 .   ? 49.752  18.924 88.286  1.00 24.59 ? 882  HOH A O   1 
HETATM 4322 O  O   . HOH E 4 .   ? 68.422  9.831  83.055  1.00 27.37 ? 883  HOH A O   1 
HETATM 4323 O  O   . HOH E 4 .   ? 45.980  43.812 104.250 1.00 29.36 ? 884  HOH A O   1 
HETATM 4324 O  O   . HOH E 4 .   ? 76.163  36.108 102.779 1.00 29.91 ? 885  HOH A O   1 
HETATM 4325 O  O   . HOH E 4 .   ? 47.558  42.989 78.815  1.00 28.13 ? 886  HOH A O   1 
HETATM 4326 O  O   . HOH E 4 .   ? 77.251  35.861 123.062 1.00 44.18 ? 887  HOH A O   1 
HETATM 4327 O  O   . HOH E 4 .   ? 76.266  42.377 99.829  1.00 28.02 ? 888  HOH A O   1 
HETATM 4328 O  O   . HOH E 4 .   ? 49.206  22.286 105.601 1.00 47.95 ? 889  HOH A O   1 
HETATM 4329 O  O   . HOH E 4 .   ? 61.909  55.958 96.459  1.00 29.63 ? 890  HOH A O   1 
HETATM 4330 O  O   . HOH E 4 .   ? 54.607  41.445 88.547  1.00 18.31 ? 891  HOH A O   1 
HETATM 4331 O  O   . HOH E 4 .   ? 49.035  29.685 86.809  1.00 18.62 ? 892  HOH A O   1 
HETATM 4332 O  O   . HOH E 4 .   ? 70.119  25.707 114.129 1.00 44.63 ? 893  HOH A O   1 
HETATM 4333 O  O   . HOH E 4 .   ? 71.592  63.692 79.670  1.00 34.98 ? 894  HOH A O   1 
HETATM 4334 O  O   . HOH E 4 .   ? 52.669  36.442 72.227  1.00 25.84 ? 895  HOH A O   1 
HETATM 4335 O  O   . HOH E 4 .   ? 67.322  29.843 92.734  1.00 23.58 ? 896  HOH A O   1 
HETATM 4336 O  O   . HOH E 4 .   ? 75.588  33.093 87.631  1.00 13.24 ? 897  HOH A O   1 
HETATM 4337 O  O   . HOH E 4 .   ? 75.492  49.064 98.428  1.00 33.17 ? 898  HOH A O   1 
HETATM 4338 O  O   . HOH E 4 .   ? 45.179  32.557 109.436 1.00 43.44 ? 899  HOH A O   1 
HETATM 4339 O  O   . HOH E 4 .   ? 70.619  12.180 90.824  1.00 19.85 ? 900  HOH A O   1 
HETATM 4340 O  O   . HOH E 4 .   ? 62.624  45.468 111.003 1.00 23.61 ? 901  HOH A O   1 
HETATM 4341 O  O   . HOH E 4 .   ? 79.505  50.261 97.320  1.00 27.65 ? 902  HOH A O   1 
HETATM 4342 O  O   . HOH E 4 .   ? 65.970  47.673 93.633  1.00 26.90 ? 903  HOH A O   1 
HETATM 4343 O  O   . HOH E 4 .   ? 80.573  16.596 87.489  1.00 26.71 ? 904  HOH A O   1 
HETATM 4344 O  O   . HOH E 4 .   ? 97.994  30.333 82.480  1.00 33.13 ? 905  HOH A O   1 
HETATM 4345 O  O   . HOH E 4 .   ? 56.103  11.789 91.723  1.00 18.44 ? 906  HOH A O   1 
HETATM 4346 O  O   . HOH E 4 .   ? 51.566  43.773 113.179 1.00 39.87 ? 907  HOH A O   1 
HETATM 4347 O  O   . HOH E 4 .   ? 58.092  35.796 93.798  1.00 17.11 ? 908  HOH A O   1 
HETATM 4348 O  O   . HOH E 4 .   ? 56.050  12.726 89.154  1.00 20.19 ? 909  HOH A O   1 
HETATM 4349 O  O   . HOH E 4 .   ? 89.629  40.809 88.617  1.00 20.53 ? 910  HOH A O   1 
HETATM 4350 O  O   . HOH E 4 .   ? 58.278  55.973 93.109  1.00 26.01 ? 911  HOH A O   1 
HETATM 4351 O  O   . HOH E 4 .   ? 57.979  44.792 81.245  1.00 24.60 ? 912  HOH A O   1 
HETATM 4352 O  O   . HOH E 4 .   ? 90.034  25.910 87.585  1.00 23.78 ? 913  HOH A O   1 
HETATM 4353 O  O   . HOH E 4 .   ? 46.957  46.412 104.849 1.00 32.29 ? 914  HOH A O   1 
HETATM 4354 O  O   . HOH E 4 .   ? 73.291  44.961 97.718  1.00 19.72 ? 915  HOH A O   1 
HETATM 4355 O  O   . HOH E 4 .   ? 79.303  41.762 105.388 1.00 44.88 ? 916  HOH A O   1 
HETATM 4356 O  O   . HOH E 4 .   ? 62.521  6.511  81.520  1.00 42.50 ? 917  HOH A O   1 
HETATM 4357 O  O   . HOH E 4 .   ? 49.729  27.479 85.289  1.00 18.03 ? 918  HOH A O   1 
HETATM 4358 O  O   . HOH E 4 .   ? 60.804  26.707 92.474  1.00 26.50 ? 919  HOH A O   1 
HETATM 4359 O  O   . HOH E 4 .   ? 61.562  27.358 108.219 1.00 20.59 ? 920  HOH A O   1 
HETATM 4360 O  O   . HOH E 4 .   ? 95.727  29.673 85.388  1.00 39.41 ? 921  HOH A O   1 
HETATM 4361 O  O   . HOH E 4 .   ? 54.181  34.973 85.133  1.00 16.81 ? 922  HOH A O   1 
HETATM 4362 O  O   . HOH E 4 .   ? 93.794  36.034 71.886  1.00 39.81 ? 923  HOH A O   1 
HETATM 4363 O  O   . HOH E 4 .   ? 62.781  9.504  77.939  1.00 37.59 ? 924  HOH A O   1 
HETATM 4364 O  O   . HOH E 4 .   ? 58.639  35.843 73.141  1.00 17.35 ? 925  HOH A O   1 
HETATM 4365 O  O   . HOH E 4 .   ? 76.660  9.779  88.596  1.00 33.65 ? 926  HOH A O   1 
HETATM 4366 O  O   . HOH E 4 .   ? 91.911  44.315 89.473  1.00 28.17 ? 927  HOH A O   1 
HETATM 4367 O  O   . HOH E 4 .   ? 46.842  33.411 75.458  1.00 34.64 ? 928  HOH A O   1 
HETATM 4368 O  O   . HOH E 4 .   ? 58.704  49.559 100.627 1.00 23.49 ? 929  HOH A O   1 
HETATM 4369 O  O   . HOH E 4 .   ? 46.662  29.672 88.097  1.00 24.48 ? 930  HOH A O   1 
HETATM 4370 O  O   . HOH E 4 .   ? 73.802  52.879 68.526  1.00 39.72 ? 931  HOH A O   1 
HETATM 4371 O  O   . HOH E 4 .   ? 50.295  17.108 84.187  1.00 18.45 ? 932  HOH A O   1 
HETATM 4372 O  O   . HOH E 4 .   ? 81.207  10.329 105.841 1.00 35.45 ? 933  HOH A O   1 
HETATM 4373 O  O   . HOH E 4 .   ? 57.719  22.761 98.672  1.00 24.60 ? 934  HOH A O   1 
HETATM 4374 O  O   . HOH E 4 .   ? 84.783  51.458 90.224  1.00 25.49 ? 935  HOH A O   1 
HETATM 4375 O  O   . HOH E 4 .   ? 65.201  30.872 70.394  1.00 35.12 ? 936  HOH A O   1 
HETATM 4376 O  O   . HOH E 4 .   ? 91.959  21.841 105.100 1.00 32.32 ? 937  HOH A O   1 
HETATM 4377 O  O   . HOH E 4 .   ? 87.491  38.790 92.400  1.00 23.11 ? 938  HOH A O   1 
HETATM 4378 O  O   . HOH E 4 .   ? 53.633  61.268 90.293  1.00 32.22 ? 939  HOH A O   1 
HETATM 4379 O  O   . HOH E 4 .   ? 90.348  17.229 100.703 1.00 20.56 ? 940  HOH A O   1 
HETATM 4380 O  O   . HOH E 4 .   ? 75.646  46.027 96.634  1.00 20.09 ? 941  HOH A O   1 
HETATM 4381 O  O   . HOH E 4 .   ? 95.952  38.697 87.840  1.00 41.17 ? 942  HOH A O   1 
HETATM 4382 O  O   . HOH E 4 .   ? 63.458  64.195 77.558  1.00 38.95 ? 943  HOH A O   1 
HETATM 4383 O  O   . HOH E 4 .   ? 55.876  53.136 77.035  1.00 22.87 ? 944  HOH A O   1 
HETATM 4384 O  O   . HOH E 4 .   ? 81.028  40.883 70.906  1.00 31.38 ? 945  HOH A O   1 
HETATM 4385 O  O   . HOH E 4 .   ? 61.550  60.239 65.962  1.00 47.47 ? 946  HOH A O   1 
HETATM 4386 O  O   . HOH E 4 .   ? 59.058  33.806 92.197  1.00 19.25 ? 947  HOH A O   1 
HETATM 4387 O  O   . HOH E 4 .   ? 59.701  28.228 70.761  1.00 23.59 ? 948  HOH A O   1 
HETATM 4388 O  O   . HOH E 4 .   ? 64.377  45.672 92.850  1.00 15.51 ? 949  HOH A O   1 
HETATM 4389 O  O   . HOH E 4 .   ? 79.100  42.279 109.171 1.00 49.66 ? 950  HOH A O   1 
HETATM 4390 O  O   . HOH E 4 .   ? 75.232  38.956 129.502 1.00 23.19 ? 951  HOH A O   1 
HETATM 4391 O  O   . HOH E 4 .   ? 84.089  24.036 82.491  1.00 26.09 ? 952  HOH A O   1 
HETATM 4392 O  O   . HOH E 4 .   ? 85.074  32.550 95.180  1.00 26.70 ? 953  HOH A O   1 
HETATM 4393 O  O   . HOH E 4 .   ? 93.202  48.239 83.400  1.00 40.57 ? 954  HOH A O   1 
HETATM 4394 O  O   . HOH E 4 .   ? 86.299  37.083 68.084  1.00 31.98 ? 955  HOH A O   1 
HETATM 4395 O  O   . HOH E 4 .   ? 68.018  46.705 95.295  1.00 17.33 ? 956  HOH A O   1 
HETATM 4396 O  O   . HOH E 4 .   ? 74.388  21.105 71.197  1.00 34.85 ? 957  HOH A O   1 
HETATM 4397 O  O   . HOH E 4 .   ? 59.796  19.182 104.196 1.00 30.84 ? 958  HOH A O   1 
HETATM 4398 O  O   . HOH E 4 .   ? 80.409  21.647 93.779  1.00 18.17 ? 959  HOH A O   1 
HETATM 4399 O  O   . HOH E 4 .   ? 46.240  47.640 91.090  1.00 40.24 ? 960  HOH A O   1 
HETATM 4400 O  O   . HOH E 4 .   ? 78.539  35.690 70.813  1.00 30.07 ? 961  HOH A O   1 
HETATM 4401 O  O   . HOH E 4 .   ? 74.055  35.744 131.480 1.00 15.97 ? 962  HOH A O   1 
HETATM 4402 O  O   . HOH E 4 .   ? 72.868  32.940 80.621  1.00 15.05 ? 963  HOH A O   1 
HETATM 4403 O  O   . HOH E 4 .   ? 57.910  36.437 69.861  1.00 30.47 ? 964  HOH A O   1 
HETATM 4404 O  O   . HOH E 4 .   ? 87.971  26.678 104.031 1.00 27.85 ? 965  HOH A O   1 
HETATM 4405 O  O   . HOH E 4 .   ? 76.767  26.373 101.644 1.00 17.15 ? 966  HOH A O   1 
HETATM 4406 O  O   . HOH E 4 .   ? 61.486  43.058 125.495 1.00 35.56 ? 967  HOH A O   1 
HETATM 4407 O  O   . HOH E 4 .   ? 70.815  30.153 78.400  1.00 13.50 ? 968  HOH A O   1 
HETATM 4408 O  O   . HOH E 4 .   ? 49.061  34.523 96.010  1.00 22.15 ? 969  HOH A O   1 
HETATM 4409 O  O   . HOH E 4 .   ? 87.161  28.405 90.241  1.00 20.45 ? 970  HOH A O   1 
HETATM 4410 O  O   . HOH E 4 .   ? 61.015  43.937 87.168  1.00 17.63 ? 971  HOH A O   1 
HETATM 4411 O  O   . HOH E 4 .   ? 46.994  23.639 82.083  1.00 20.30 ? 972  HOH A O   1 
HETATM 4412 O  O   . HOH E 4 .   ? 57.148  50.592 77.160  1.00 23.56 ? 973  HOH A O   1 
HETATM 4413 O  O   . HOH E 4 .   ? 73.861  30.177 124.146 1.00 35.04 ? 974  HOH A O   1 
HETATM 4414 O  O   . HOH E 4 .   ? 81.432  14.874 96.770  1.00 17.47 ? 975  HOH A O   1 
HETATM 4415 O  O   . HOH E 4 .   ? 52.892  49.674 107.784 1.00 34.25 ? 976  HOH A O   1 
HETATM 4416 O  O   . HOH E 4 .   ? 63.668  10.073 90.779  1.00 42.45 ? 977  HOH A O   1 
HETATM 4417 O  O   . HOH E 4 .   ? 48.299  26.990 107.539 1.00 30.08 ? 978  HOH A O   1 
HETATM 4418 O  O   . HOH E 4 .   ? 60.468  60.274 92.882  1.00 41.59 ? 979  HOH A O   1 
HETATM 4419 O  O   . HOH E 4 .   ? 77.250  10.349 98.431  1.00 29.54 ? 980  HOH A O   1 
HETATM 4420 O  O   . HOH E 4 .   ? 63.557  16.938 78.692  1.00 16.45 ? 981  HOH A O   1 
HETATM 4421 O  O   . HOH E 4 .   ? 84.703  21.486 85.907  1.00 22.34 ? 982  HOH A O   1 
HETATM 4422 O  O   . HOH E 4 .   ? 69.045  6.679  88.695  1.00 41.40 ? 983  HOH A O   1 
HETATM 4423 O  O   . HOH E 4 .   ? 84.663  12.662 98.543  1.00 21.40 ? 984  HOH A O   1 
HETATM 4424 O  O   . HOH E 4 .   ? 85.147  43.182 75.829  1.00 15.99 ? 985  HOH A O   1 
HETATM 4425 O  O   . HOH E 4 .   ? 62.161  52.337 94.699  1.00 19.67 ? 986  HOH A O   1 
HETATM 4426 O  O   . HOH E 4 .   ? 90.311  18.595 104.796 1.00 31.00 ? 987  HOH A O   1 
HETATM 4427 O  O   . HOH E 4 .   ? 80.152  20.197 73.550  1.00 30.18 ? 988  HOH A O   1 
HETATM 4428 O  O   . HOH E 4 .   ? 68.521  40.747 69.453  1.00 23.39 ? 989  HOH A O   1 
HETATM 4429 O  O   . HOH E 4 .   ? 57.319  47.075 82.381  1.00 32.70 ? 990  HOH A O   1 
HETATM 4430 O  O   . HOH E 4 .   ? 68.916  59.433 94.914  1.00 41.66 ? 991  HOH A O   1 
HETATM 4431 O  O   . HOH E 4 .   ? 47.683  48.361 84.363  1.00 40.96 ? 992  HOH A O   1 
HETATM 4432 O  O   . HOH E 4 .   ? 82.487  40.585 96.292  1.00 33.47 ? 993  HOH A O   1 
HETATM 4433 O  O   . HOH E 4 .   ? 77.795  36.389 113.189 1.00 38.57 ? 994  HOH A O   1 
HETATM 4434 O  O   . HOH E 4 .   ? 87.417  12.897 99.705  1.00 22.51 ? 995  HOH A O   1 
HETATM 4435 O  O   . HOH E 4 .   ? 42.003  35.997 97.787  1.00 41.46 ? 996  HOH A O   1 
HETATM 4436 O  O   . HOH E 4 .   ? 74.877  11.026 84.837  1.00 29.18 ? 997  HOH A O   1 
HETATM 4437 O  O   . HOH E 4 .   ? 78.408  53.870 95.998  1.00 37.17 ? 998  HOH A O   1 
HETATM 4438 O  O   . HOH E 4 .   ? 69.653  60.157 83.102  1.00 24.84 ? 999  HOH A O   1 
HETATM 4439 O  O   . HOH E 4 .   ? 54.459  37.307 91.778  1.00 21.23 ? 1000 HOH A O   1 
HETATM 4440 O  O   . HOH E 4 .   ? 66.777  44.625 98.776  1.00 16.20 ? 1001 HOH A O   1 
HETATM 4441 O  O   . HOH E 4 .   ? 69.312  47.369 98.721  1.00 20.87 ? 1002 HOH A O   1 
HETATM 4442 O  O   . HOH E 4 .   ? 68.831  29.375 111.040 1.00 22.89 ? 1003 HOH A O   1 
HETATM 4443 O  O   . HOH E 4 .   ? 55.727  20.566 89.549  1.00 23.21 ? 1004 HOH A O   1 
HETATM 4444 O  O   . HOH E 4 .   ? 89.157  48.384 73.955  1.00 41.61 ? 1005 HOH A O   1 
HETATM 4445 O  O   . HOH E 4 .   ? 71.309  7.890  92.111  1.00 40.09 ? 1006 HOH A O   1 
HETATM 4446 O  O   . HOH E 4 .   ? 61.218  44.997 75.646  1.00 33.11 ? 1007 HOH A O   1 
HETATM 4447 O  O   . HOH E 4 .   ? 56.735  48.168 92.099  1.00 18.15 ? 1008 HOH A O   1 
HETATM 4448 O  O   . HOH E 4 .   ? 87.671  50.226 89.608  1.00 22.75 ? 1009 HOH A O   1 
HETATM 4449 O  O   . HOH E 4 .   ? 71.024  15.558 80.479  1.00 20.71 ? 1010 HOH A O   1 
HETATM 4450 O  O   . HOH E 4 .   ? 48.269  23.613 99.330  1.00 33.45 ? 1011 HOH A O   1 
HETATM 4451 O  O   . HOH E 4 .   ? 45.781  26.734 74.282  1.00 43.50 ? 1012 HOH A O   1 
HETATM 4452 O  O   . HOH E 4 .   ? 45.770  46.196 84.236  1.00 46.54 ? 1013 HOH A O   1 
HETATM 4453 O  O   . HOH E 4 .   ? 93.951  27.772 84.449  1.00 21.53 ? 1014 HOH A O   1 
HETATM 4454 O  O   . HOH E 4 .   ? 90.411  31.982 87.021  1.00 25.41 ? 1015 HOH A O   1 
HETATM 4455 O  O   . HOH E 4 .   ? 75.526  32.334 72.941  1.00 17.51 ? 1016 HOH A O   1 
HETATM 4456 O  O   . HOH E 4 .   ? 46.379  26.577 65.557  1.00 45.34 ? 1017 HOH A O   1 
HETATM 4457 O  O   . HOH E 4 .   ? 74.360  18.899 106.879 1.00 32.35 ? 1018 HOH A O   1 
HETATM 4458 O  O   . HOH E 4 .   ? 76.263  19.244 94.289  1.00 13.76 ? 1019 HOH A O   1 
HETATM 4459 O  O   . HOH E 4 .   ? 46.329  27.268 91.100  1.00 34.12 ? 1020 HOH A O   1 
HETATM 4460 O  O   . HOH E 4 .   ? 68.829  44.384 127.116 1.00 23.75 ? 1021 HOH A O   1 
HETATM 4461 O  O   . HOH E 4 .   ? 54.313  26.583 111.740 1.00 41.99 ? 1022 HOH A O   1 
HETATM 4462 O  O   . HOH E 4 .   ? 81.617  14.070 92.210  1.00 20.65 ? 1023 HOH A O   1 
HETATM 4463 O  O   . HOH E 4 .   ? 83.979  54.859 91.580  1.00 40.41 ? 1024 HOH A O   1 
HETATM 4464 O  O   . HOH E 4 .   ? 43.813  30.197 92.988  1.00 35.59 ? 1025 HOH A O   1 
HETATM 4465 O  O   . HOH E 4 .   ? 64.606  45.030 121.879 1.00 34.39 ? 1026 HOH A O   1 
HETATM 4466 O  O   . HOH E 4 .   ? 60.090  21.589 111.230 1.00 26.08 ? 1027 HOH A O   1 
HETATM 4467 O  O   . HOH E 4 .   ? 98.853  35.041 82.539  1.00 33.04 ? 1028 HOH A O   1 
HETATM 4468 O  O   . HOH E 4 .   ? 52.307  33.000 85.330  1.00 15.97 ? 1029 HOH A O   1 
HETATM 4469 O  O   . HOH E 4 .   ? 52.276  49.291 101.136 1.00 33.70 ? 1030 HOH A O   1 
HETATM 4470 O  O   . HOH E 4 .   ? 69.065  52.491 113.526 1.00 33.28 ? 1031 HOH A O   1 
HETATM 4471 O  O   . HOH E 4 .   ? 64.574  55.689 108.223 1.00 37.94 ? 1032 HOH A O   1 
HETATM 4472 O  O   . HOH E 4 .   ? 57.539  46.950 84.905  1.00 29.06 ? 1033 HOH A O   1 
HETATM 4473 O  O   . HOH E 4 .   ? 71.504  18.996 72.019  1.00 43.73 ? 1034 HOH A O   1 
HETATM 4474 O  O   . HOH E 4 .   ? 77.824  31.364 82.122  1.00 17.83 ? 1035 HOH A O   1 
HETATM 4475 O  O   . HOH E 4 .   ? 50.835  20.480 80.393  1.00 21.37 ? 1036 HOH A O   1 
HETATM 4476 O  O   . HOH E 4 .   ? 64.598  50.641 67.607  1.00 33.25 ? 1037 HOH A O   1 
HETATM 4477 O  O   . HOH E 4 .   ? 65.011  15.924 97.038  1.00 30.16 ? 1038 HOH A O   1 
HETATM 4478 O  O   . HOH E 4 .   ? 80.791  60.166 67.015  1.00 41.11 ? 1039 HOH A O   1 
HETATM 4479 O  O   . HOH E 4 .   ? 99.535  39.477 85.318  1.00 40.43 ? 1040 HOH A O   1 
HETATM 4480 O  O   . HOH E 4 .   ? 64.598  15.402 94.309  1.00 24.95 ? 1041 HOH A O   1 
HETATM 4481 O  O   . HOH E 4 .   ? 41.188  39.938 100.550 1.00 53.54 ? 1042 HOH A O   1 
HETATM 4482 O  O   . HOH E 4 .   ? 71.197  32.086 120.179 1.00 44.08 ? 1043 HOH A O   1 
HETATM 4483 O  O   . HOH E 4 .   ? 42.694  30.709 95.559  1.00 45.84 ? 1044 HOH A O   1 
HETATM 4484 O  O   . HOH E 4 .   ? 83.596  41.492 93.487  1.00 31.88 ? 1045 HOH A O   1 
HETATM 4485 O  O   . HOH E 4 .   ? 56.272  19.904 86.785  1.00 19.36 ? 1046 HOH A O   1 
HETATM 4486 O  O   . HOH E 4 .   ? 72.833  15.602 90.226  1.00 16.49 ? 1047 HOH A O   1 
HETATM 4487 O  O   . HOH E 4 .   ? 88.029  53.501 78.414  1.00 31.42 ? 1048 HOH A O   1 
HETATM 4488 O  O   . HOH E 4 .   ? 76.363  12.405 77.081  1.00 29.28 ? 1049 HOH A O   1 
HETATM 4489 O  O   . HOH E 4 .   ? 92.755  33.722 74.681  1.00 33.50 ? 1050 HOH A O   1 
HETATM 4490 O  O   . HOH E 4 .   ? 81.355  43.359 94.201  1.00 18.96 ? 1051 HOH A O   1 
HETATM 4491 O  O   . HOH E 4 .   ? 89.000  42.785 64.616  1.00 50.38 ? 1052 HOH A O   1 
HETATM 4492 O  O   . HOH E 4 .   ? 80.163  25.199 95.416  1.00 14.78 ? 1053 HOH A O   1 
HETATM 4493 O  O   . HOH E 4 .   ? 62.692  13.706 94.358  1.00 23.25 ? 1054 HOH A O   1 
HETATM 4494 O  O   . HOH E 4 .   ? 79.511  33.289 71.122  1.00 28.28 ? 1055 HOH A O   1 
HETATM 4495 O  O   . HOH E 4 .   ? 73.637  27.254 69.267  1.00 39.07 ? 1056 HOH A O   1 
HETATM 4496 O  O   . HOH E 4 .   ? 63.476  38.626 121.488 1.00 30.40 ? 1057 HOH A O   1 
HETATM 4497 O  O   . HOH E 4 .   ? 63.005  61.263 92.534  1.00 30.81 ? 1058 HOH A O   1 
HETATM 4498 O  O   . HOH E 4 .   ? 55.791  64.308 80.106  1.00 49.63 ? 1059 HOH A O   1 
HETATM 4499 O  O   . HOH E 4 .   ? 53.023  61.004 83.444  1.00 29.23 ? 1060 HOH A O   1 
HETATM 4500 O  O   . HOH E 4 .   ? 62.862  31.178 69.225  1.00 33.58 ? 1061 HOH A O   1 
HETATM 4501 O  O   . HOH E 4 .   ? 43.386  41.542 80.494  1.00 48.49 ? 1062 HOH A O   1 
HETATM 4502 O  O   . HOH E 4 .   ? 85.365  25.101 77.408  1.00 19.30 ? 1063 HOH A O   1 
HETATM 4503 O  O   . HOH E 4 .   ? 91.472  35.371 90.484  1.00 38.03 ? 1064 HOH A O   1 
HETATM 4504 O  O   . HOH E 4 .   ? 63.035  45.782 73.154  1.00 33.26 ? 1065 HOH A O   1 
HETATM 4505 O  O   . HOH E 4 .   ? 63.195  16.527 75.998  1.00 24.15 ? 1066 HOH A O   1 
HETATM 4506 O  O   . HOH E 4 .   ? 53.550  16.800 76.685  1.00 21.64 ? 1067 HOH A O   1 
HETATM 4507 O  O   . HOH E 4 .   ? 78.459  34.070 89.400  1.00 15.12 ? 1068 HOH A O   1 
HETATM 4508 O  O   . HOH E 4 .   ? 65.853  55.666 111.303 1.00 42.70 ? 1069 HOH A O   1 
HETATM 4509 O  O   . HOH E 4 .   ? 84.779  25.967 107.790 1.00 51.73 ? 1070 HOH A O   1 
HETATM 4510 O  O   . HOH E 4 .   ? 76.830  16.581 109.272 1.00 33.68 ? 1071 HOH A O   1 
HETATM 4511 O  O   . HOH E 4 .   ? 47.066  33.298 88.558  1.00 20.99 ? 1072 HOH A O   1 
HETATM 4512 O  O   . HOH E 4 .   ? 57.002  22.992 89.548  1.00 20.22 ? 1073 HOH A O   1 
HETATM 4513 O  O   . HOH E 4 .   ? 96.711  32.813 85.544  1.00 39.65 ? 1074 HOH A O   1 
HETATM 4514 O  O   . HOH E 4 .   ? 60.585  45.458 70.623  1.00 49.07 ? 1075 HOH A O   1 
HETATM 4515 O  O   . HOH E 4 .   ? 68.146  63.732 72.235  1.00 31.14 ? 1076 HOH A O   1 
HETATM 4516 O  O   . HOH E 4 .   ? 54.044  23.077 110.955 1.00 47.82 ? 1077 HOH A O   1 
HETATM 4517 O  O   . HOH E 4 .   ? 76.176  37.793 81.508  1.00 14.57 ? 1078 HOH A O   1 
HETATM 4518 O  O   . HOH E 4 .   ? 50.378  47.937 93.700  1.00 28.13 ? 1079 HOH A O   1 
HETATM 4519 O  O   . HOH E 4 .   ? 46.273  39.395 77.696  1.00 27.37 ? 1080 HOH A O   1 
HETATM 4520 O  O   . HOH E 4 .   ? 89.027  24.571 92.601  1.00 19.05 ? 1081 HOH A O   1 
HETATM 4521 O  O   . HOH E 4 .   ? 78.805  34.787 109.504 1.00 34.77 ? 1082 HOH A O   1 
HETATM 4522 O  O   . HOH E 4 .   ? 66.132  64.255 70.335  1.00 28.86 ? 1083 HOH A O   1 
HETATM 4523 O  O   . HOH E 4 .   ? 61.770  44.727 113.636 1.00 36.05 ? 1084 HOH A O   1 
HETATM 4524 O  O   . HOH E 4 .   ? 91.755  46.673 79.874  1.00 25.91 ? 1085 HOH A O   1 
HETATM 4525 O  O   . HOH E 4 .   ? 61.828  8.933  87.381  1.00 30.13 ? 1086 HOH A O   1 
HETATM 4526 O  O   . HOH E 4 .   ? 72.663  12.805 83.763  1.00 25.11 ? 1087 HOH A O   1 
HETATM 4527 O  O   . HOH E 4 .   ? 73.460  63.742 86.065  1.00 27.95 ? 1088 HOH A O   1 
HETATM 4528 O  O   . HOH E 4 .   ? 66.788  49.748 105.532 1.00 22.29 ? 1089 HOH A O   1 
HETATM 4529 O  O   . HOH E 4 .   ? 88.921  51.115 74.742  1.00 38.65 ? 1090 HOH A O   1 
HETATM 4530 O  O   . HOH E 4 .   ? 86.828  30.676 95.391  1.00 33.69 ? 1091 HOH A O   1 
HETATM 4531 O  O   . HOH E 4 .   ? 69.442  49.466 101.870 1.00 38.07 ? 1092 HOH A O   1 
HETATM 4532 O  O   . HOH E 4 .   ? 61.368  63.470 79.730  1.00 31.37 ? 1093 HOH A O   1 
HETATM 4533 O  O   . HOH E 4 .   ? 69.264  13.065 98.420  1.00 32.93 ? 1094 HOH A O   1 
HETATM 4534 O  O   . HOH E 4 .   ? 59.847  20.200 67.735  1.00 50.48 ? 1095 HOH A O   1 
HETATM 4535 O  O   . HOH E 4 .   ? 57.393  33.214 114.151 1.00 34.77 ? 1096 HOH A O   1 
HETATM 4536 O  O   . HOH E 4 .   ? 60.981  23.088 83.851  1.00 16.23 ? 1097 HOH A O   1 
HETATM 4537 O  O   . HOH E 4 .   ? 70.592  57.210 94.737  1.00 26.04 ? 1098 HOH A O   1 
HETATM 4538 O  O   . HOH E 4 .   ? 66.598  58.105 68.280  1.00 23.20 ? 1099 HOH A O   1 
HETATM 4539 O  O   . HOH E 4 .   ? 60.071  46.273 84.451  1.00 19.15 ? 1100 HOH A O   1 
HETATM 4540 O  O   . HOH E 4 .   ? 91.945  41.974 87.934  1.00 24.32 ? 1101 HOH A O   1 
HETATM 4541 O  O   . HOH E 4 .   ? 61.297  7.662  85.315  1.00 46.79 ? 1102 HOH A O   1 
HETATM 4542 O  O   . HOH E 4 .   ? 55.866  20.401 102.023 1.00 45.00 ? 1103 HOH A O   1 
HETATM 4543 O  O   . HOH E 4 .   ? 46.156  37.949 113.841 1.00 50.46 ? 1104 HOH A O   1 
HETATM 4544 O  O   . HOH E 4 .   ? 86.234  21.653 106.148 1.00 34.20 ? 1105 HOH A O   1 
HETATM 4545 O  O   . HOH E 4 .   ? 59.111  62.199 86.995  1.00 35.30 ? 1106 HOH A O   1 
HETATM 4546 O  O   . HOH E 4 .   ? 63.390  63.881 74.394  1.00 32.39 ? 1107 HOH A O   1 
HETATM 4547 O  O   . HOH E 4 .   ? 45.464  34.420 77.231  1.00 26.76 ? 1108 HOH A O   1 
HETATM 4548 O  O   . HOH E 4 .   ? 87.788  44.756 95.974  1.00 30.78 ? 1109 HOH A O   1 
HETATM 4549 O  O   . HOH E 4 .   ? 89.300  53.702 72.429  1.00 47.05 ? 1110 HOH A O   1 
HETATM 4550 O  O   . HOH E 4 .   ? 49.116  17.741 90.754  1.00 28.68 ? 1111 HOH A O   1 
HETATM 4551 O  O   . HOH E 4 .   ? 89.514  34.850 69.633  1.00 38.77 ? 1112 HOH A O   1 
HETATM 4552 O  O   . HOH E 4 .   ? 67.627  9.980  78.410  1.00 36.87 ? 1113 HOH A O   1 
HETATM 4553 O  O   . HOH E 4 .   ? 65.116  38.685 67.993  1.00 25.97 ? 1114 HOH A O   1 
HETATM 4554 O  O   . HOH E 4 .   ? 76.973  51.352 66.688  1.00 46.29 ? 1115 HOH A O   1 
HETATM 4555 O  O   . HOH E 4 .   ? 51.571  35.966 114.218 1.00 35.50 ? 1116 HOH A O   1 
HETATM 4556 O  O   . HOH E 4 .   ? 67.972  56.041 100.355 1.00 29.44 ? 1117 HOH A O   1 
HETATM 4557 O  O   . HOH E 4 .   ? 75.419  43.871 116.531 1.00 36.96 ? 1118 HOH A O   1 
HETATM 4558 O  O   . HOH E 4 .   ? 90.784  48.811 77.104  1.00 41.64 ? 1119 HOH A O   1 
HETATM 4559 O  O   . HOH E 4 .   ? 52.364  28.467 109.021 1.00 25.34 ? 1120 HOH A O   1 
HETATM 4560 O  O   . HOH E 4 .   ? 85.079  53.623 71.652  1.00 35.48 ? 1121 HOH A O   1 
HETATM 4561 O  O   . HOH E 4 .   ? 72.813  60.917 83.018  1.00 36.78 ? 1122 HOH A O   1 
HETATM 4562 O  O   . HOH E 4 .   ? 72.589  42.515 126.823 1.00 32.86 ? 1123 HOH A O   1 
HETATM 4563 O  O   . HOH E 4 .   ? 70.536  13.487 81.882  1.00 24.22 ? 1124 HOH A O   1 
HETATM 4564 O  O   . HOH E 4 .   ? 87.450  34.870 94.549  1.00 37.80 ? 1125 HOH A O   1 
HETATM 4565 O  O   . HOH E 4 .   ? 84.734  52.040 95.494  1.00 47.02 ? 1126 HOH A O   1 
HETATM 4566 O  O   . HOH E 4 .   ? 56.742  37.920 71.919  1.00 27.88 ? 1127 HOH A O   1 
HETATM 4567 O  O   . HOH E 4 .   ? 63.144  62.221 63.452  1.00 45.66 ? 1128 HOH A O   1 
HETATM 4568 O  O   . HOH E 4 .   ? 59.162  56.958 98.847  1.00 37.02 ? 1129 HOH A O   1 
HETATM 4569 O  O   . HOH E 4 .   ? 53.709  12.597 78.486  1.00 22.93 ? 1130 HOH A O   1 
HETATM 4570 O  O   . HOH E 4 .   ? 73.907  63.239 67.354  1.00 32.76 ? 1131 HOH A O   1 
HETATM 4571 O  O   . HOH E 4 .   ? 51.776  39.345 95.194  1.00 28.20 ? 1132 HOH A O   1 
HETATM 4572 O  O   . HOH E 4 .   ? 50.004  21.726 98.876  1.00 39.23 ? 1133 HOH A O   1 
HETATM 4573 O  O   . HOH E 4 .   ? 76.388  61.543 68.768  1.00 43.13 ? 1134 HOH A O   1 
HETATM 4574 O  O   . HOH E 4 .   ? 82.124  15.935 89.678  1.00 19.14 ? 1135 HOH A O   1 
HETATM 4575 O  O   . HOH E 4 .   ? 83.009  45.817 68.876  1.00 33.83 ? 1136 HOH A O   1 
HETATM 4576 O  O   . HOH E 4 .   ? 90.160  50.754 92.364  1.00 34.07 ? 1137 HOH A O   1 
HETATM 4577 O  O   . HOH E 4 .   ? 70.756  27.829 112.658 1.00 33.55 ? 1138 HOH A O   1 
HETATM 4578 O  O   . HOH E 4 .   ? 60.803  12.536 75.873  1.00 48.48 ? 1139 HOH A O   1 
HETATM 4579 O  O   . HOH E 4 .   ? 48.339  23.443 109.556 1.00 50.59 ? 1140 HOH A O   1 
HETATM 4580 O  O   . HOH E 4 .   ? 56.766  41.959 76.716  1.00 22.86 ? 1141 HOH A O   1 
HETATM 4581 O  O   . HOH E 4 .   ? 74.096  15.648 73.769  1.00 46.58 ? 1142 HOH A O   1 
HETATM 4582 O  O   . HOH E 4 .   ? 56.874  18.963 104.808 1.00 49.70 ? 1143 HOH A O   1 
HETATM 4583 O  O   . HOH E 4 .   ? 43.935  26.700 76.972  1.00 32.72 ? 1144 HOH A O   1 
HETATM 4584 O  O   . HOH E 4 .   ? 69.176  21.931 98.176  1.00 30.69 ? 1145 HOH A O   1 
HETATM 4585 O  O   . HOH E 4 .   ? 71.939  15.619 101.718 1.00 38.07 ? 1146 HOH A O   1 
HETATM 4586 O  O   . HOH E 4 .   ? 56.531  53.026 94.049  1.00 32.17 ? 1147 HOH A O   1 
HETATM 4587 O  O   . HOH E 4 .   ? 62.444  15.697 71.788  1.00 39.79 ? 1148 HOH A O   1 
HETATM 4588 O  O   . HOH E 4 .   ? 67.467  24.925 70.202  1.00 37.56 ? 1149 HOH A O   1 
HETATM 4589 O  O   . HOH E 4 .   ? 75.391  65.262 87.109  1.00 35.18 ? 1150 HOH A O   1 
HETATM 4590 O  O   . HOH E 4 .   ? 64.034  44.578 76.187  1.00 28.63 ? 1151 HOH A O   1 
HETATM 4591 O  O   . HOH E 4 .   ? 61.950  55.020 72.014  1.00 20.37 ? 1152 HOH A O   1 
HETATM 4592 O  O   . HOH E 4 .   ? 68.080  63.384 64.178  1.00 46.18 ? 1153 HOH A O   1 
HETATM 4593 O  O   . HOH E 4 .   ? 96.199  31.024 78.192  1.00 36.43 ? 1154 HOH A O   1 
HETATM 4594 O  O   . HOH E 4 .   ? 82.320  65.423 86.699  1.00 44.84 ? 1155 HOH A O   1 
HETATM 4595 O  O   . HOH E 4 .   ? 49.870  27.229 65.109  1.00 45.54 ? 1156 HOH A O   1 
HETATM 4596 O  O   . HOH E 4 .   ? 71.703  11.794 97.168  1.00 33.04 ? 1157 HOH A O   1 
HETATM 4597 O  O   . HOH E 4 .   ? 38.834  27.447 96.321  1.00 43.09 ? 1158 HOH A O   1 
HETATM 4598 O  O   . HOH E 4 .   ? 63.915  59.247 101.354 1.00 51.96 ? 1159 HOH A O   1 
HETATM 4599 O  O   . HOH E 4 .   ? 84.978  43.643 97.462  1.00 41.64 ? 1160 HOH A O   1 
HETATM 4600 O  O   . HOH E 4 .   ? 85.493  56.384 80.474  1.00 32.43 ? 1161 HOH A O   1 
HETATM 4601 O  O   . HOH E 4 .   ? 41.414  43.928 101.337 1.00 45.37 ? 1162 HOH A O   1 
HETATM 4602 O  O   . HOH E 4 .   ? 59.721  41.752 70.063  1.00 41.36 ? 1163 HOH A O   1 
HETATM 4603 O  O   . HOH E 4 .   ? 58.626  13.335 76.040  1.00 43.67 ? 1164 HOH A O   1 
HETATM 4604 O  O   . HOH E 4 .   ? 56.037  14.485 75.233  1.00 33.04 ? 1165 HOH A O   1 
HETATM 4605 O  O   . HOH E 4 .   ? 55.088  50.857 94.414  1.00 39.22 ? 1166 HOH A O   1 
HETATM 4606 O  O   . HOH E 4 .   ? 83.267  17.059 84.805  1.00 46.47 ? 1167 HOH A O   1 
HETATM 4607 O  O   . HOH E 4 .   ? 53.685  43.334 91.943  1.00 36.81 ? 1168 HOH A O   1 
HETATM 4608 O  O   . HOH E 4 .   ? 44.724  44.416 101.857 1.00 36.13 ? 1169 HOH A O   1 
HETATM 4609 O  O   . HOH E 4 .   ? 55.952  18.810 98.316  1.00 40.80 ? 1170 HOH A O   1 
HETATM 4610 O  O   . HOH E 4 .   ? 72.594  65.172 68.920  1.00 39.55 ? 1171 HOH A O   1 
HETATM 4611 O  O   . HOH E 4 .   ? 69.777  23.180 113.503 1.00 46.31 ? 1172 HOH A O   1 
HETATM 4612 O  O   . HOH E 4 .   ? 78.578  40.292 97.725  1.00 38.94 ? 1173 HOH A O   1 
HETATM 4613 O  O   . HOH E 4 .   ? 65.351  33.221 69.598  1.00 40.29 ? 1174 HOH A O   1 
HETATM 4614 O  O   . HOH E 4 .   ? 66.378  64.826 65.897  1.00 51.92 ? 1175 HOH A O   1 
HETATM 4615 O  O   . HOH E 4 .   ? 56.208  63.838 82.035  1.00 41.82 ? 1176 HOH A O   1 
HETATM 4616 O  O   . HOH E 4 .   ? 76.087  31.159 123.902 1.00 47.45 ? 1177 HOH A O   1 
HETATM 4617 O  O   . HOH E 4 .   ? 87.695  19.243 108.438 1.00 49.70 ? 1178 HOH A O   1 
HETATM 4618 O  O   . HOH E 4 .   ? 81.898  35.272 68.896  1.00 39.90 ? 1179 HOH A O   1 
HETATM 4619 O  O   . HOH E 4 .   ? 82.480  66.844 84.235  1.00 51.25 ? 1180 HOH A O   1 
HETATM 4620 O  O   . HOH E 4 .   ? 50.393  21.340 95.907  1.00 37.10 ? 1181 HOH A O   1 
HETATM 4621 O  O   . HOH E 4 .   ? 88.317  42.903 93.727  1.00 34.33 ? 1182 HOH A O   1 
HETATM 4622 O  O   . HOH E 4 .   ? 59.958  9.013  89.212  1.00 33.12 ? 1183 HOH A O   1 
HETATM 4623 O  O   . HOH E 4 .   ? 87.338  34.559 66.607  1.00 53.16 ? 1184 HOH A O   1 
HETATM 4624 O  O   . HOH E 4 .   ? 82.147  43.152 97.108  1.00 41.27 ? 1185 HOH A O   1 
HETATM 4625 O  O   . HOH E 4 .   ? 47.364  20.363 84.125  1.00 20.78 ? 1186 HOH A O   1 
HETATM 4626 O  O   . HOH E 4 .   ? 79.944  16.296 77.467  1.00 45.37 ? 1187 HOH A O   1 
HETATM 4627 O  O   . HOH E 4 .   ? 53.201  60.326 94.956  1.00 51.23 ? 1188 HOH A O   1 
HETATM 4628 O  O   . HOH E 4 .   ? 66.706  55.994 102.959 1.00 43.74 ? 1189 HOH A O   1 
HETATM 4629 O  O   . HOH E 4 .   ? 63.930  12.320 71.962  1.00 51.26 ? 1190 HOH A O   1 
HETATM 4630 O  O   . HOH E 4 .   ? 93.995  45.477 80.458  1.00 42.91 ? 1191 HOH A O   1 
HETATM 4631 O  O   . HOH E 4 .   ? 66.918  33.174 67.600  1.00 48.06 ? 1192 HOH A O   1 
HETATM 4632 O  O   . HOH E 4 .   ? 58.288  44.412 76.851  1.00 37.71 ? 1193 HOH A O   1 
HETATM 4633 O  O   . HOH E 4 .   ? 88.485  22.940 76.841  1.00 49.59 ? 1194 HOH A O   1 
HETATM 4634 O  O   . HOH E 4 .   ? 66.817  51.720 120.477 1.00 48.09 ? 1195 HOH A O   1 
HETATM 4635 O  O   . HOH E 4 .   ? 50.120  27.578 109.876 1.00 41.87 ? 1196 HOH A O   1 
HETATM 4636 O  O   . HOH E 4 .   ? 76.863  67.045 81.705  1.00 48.94 ? 1197 HOH A O   1 
HETATM 4637 O  O   . HOH E 4 .   ? 99.868  35.903 79.829  1.00 43.45 ? 1198 HOH A O   1 
HETATM 4638 O  O   . HOH E 4 .   ? 81.854  18.178 80.348  1.00 39.61 ? 1199 HOH A O   1 
HETATM 4639 O  O   . HOH E 4 .   ? 63.779  45.941 68.893  1.00 52.07 ? 1200 HOH A O   1 
HETATM 4640 O  O   . HOH E 4 .   ? 52.747  41.571 90.740  1.00 33.59 ? 1201 HOH A O   1 
HETATM 4641 O  O   . HOH E 4 .   ? 76.909  43.034 111.354 1.00 46.46 ? 1202 HOH A O   1 
HETATM 4642 O  O   . HOH E 4 .   ? 96.577  35.068 86.931  1.00 49.52 ? 1203 HOH A O   1 
HETATM 4643 O  O   . HOH E 4 .   ? 74.633  66.264 83.262  1.00 55.80 ? 1204 HOH A O   1 
HETATM 4644 O  O   . HOH E 4 .   ? 57.055  24.079 114.345 1.00 54.60 ? 1205 HOH A O   1 
HETATM 4645 O  O   . HOH E 4 .   ? 82.781  18.799 77.629  1.00 43.56 ? 1206 HOH A O   1 
HETATM 4646 O  O   . HOH E 4 .   ? 44.127  31.443 84.630  1.00 38.70 ? 1207 HOH A O   1 
HETATM 4647 O  O   . HOH E 4 .   ? 49.286  19.223 82.559  1.00 19.04 ? 1208 HOH A O   1 
HETATM 4648 O  O   . HOH E 4 .   ? 70.685  30.784 122.302 1.00 52.22 ? 1209 HOH A O   1 
HETATM 4649 O  O   . HOH E 4 .   ? 88.871  28.566 94.195  1.00 32.65 ? 1210 HOH A O   1 
HETATM 4650 O  O   . HOH E 4 .   ? 95.331  44.254 78.701  1.00 48.75 ? 1211 HOH A O   1 
HETATM 4651 O  O   . HOH E 4 .   ? 68.321  30.751 126.429 1.00 38.06 ? 1212 HOH A O   1 
HETATM 4652 O  O   . HOH E 4 .   ? 86.103  23.955 73.648  1.00 49.44 ? 1213 HOH A O   1 
HETATM 4653 O  O   . HOH E 4 .   ? 54.043  20.475 69.707  1.00 32.93 ? 1214 HOH A O   1 
HETATM 4654 O  O   . HOH E 4 .   ? 71.899  18.063 102.603 1.00 39.17 ? 1215 HOH A O   1 
HETATM 4655 O  O   . HOH E 4 .   ? 93.786  31.572 74.193  1.00 44.63 ? 1216 HOH A O   1 
HETATM 4656 O  O   . HOH E 4 .   ? 88.867  30.844 99.176  1.00 36.76 ? 1217 HOH A O   1 
HETATM 4657 O  O   . HOH E 4 .   ? 65.588  45.110 70.445  1.00 37.46 ? 1218 HOH A O   1 
HETATM 4658 O  O   . HOH E 4 .   ? 85.640  38.861 65.879  1.00 45.81 ? 1219 HOH A O   1 
HETATM 4659 O  O   . HOH E 4 .   ? 72.817  11.395 75.834  1.00 53.71 ? 1220 HOH A O   1 
HETATM 4660 O  O   . HOH E 4 .   ? 87.961  52.310 92.738  1.00 41.79 ? 1221 HOH A O   1 
HETATM 4661 O  O   . HOH E 4 .   ? 86.033  22.566 77.622  1.00 44.50 ? 1222 HOH A O   1 
HETATM 4662 O  O   . HOH E 4 .   ? 93.002  27.349 74.305  1.00 37.75 ? 1223 HOH A O   1 
HETATM 4663 O  O   . HOH E 4 .   ? 63.627  32.373 115.622 1.00 52.68 ? 1224 HOH A O   1 
HETATM 4664 O  O   . HOH E 4 .   ? 78.308  8.249  90.026  1.00 33.36 ? 1225 HOH A O   1 
HETATM 4665 O  O   . HOH E 4 .   ? 47.438  21.181 90.335  1.00 51.84 ? 1226 HOH A O   1 
HETATM 4666 O  O   . HOH E 4 .   ? 92.122  45.323 93.546  1.00 48.89 ? 1227 HOH A O   1 
HETATM 4667 O  O   . HOH E 4 .   ? 69.555  14.403 100.761 1.00 47.65 ? 1228 HOH A O   1 
HETATM 4668 O  O   . HOH E 4 .   ? 45.373  43.433 80.020  1.00 40.62 ? 1229 HOH A O   1 
HETATM 4669 O  O   . HOH E 4 .   ? 62.051  19.969 112.358 1.00 47.03 ? 1230 HOH A O   1 
HETATM 4670 O  O   . HOH E 4 .   ? 71.244  48.669 100.068 1.00 36.37 ? 1231 HOH A O   1 
HETATM 4671 O  O   . HOH E 4 .   ? 51.090  40.841 71.834  1.00 51.79 ? 1232 HOH A O   1 
HETATM 4672 O  O   . HOH E 4 .   ? 49.824  44.982 93.651  1.00 45.07 ? 1233 HOH A O   1 
HETATM 4673 O  O   . HOH E 4 .   ? 45.249  31.792 87.126  1.00 29.75 ? 1234 HOH A O   1 
HETATM 4674 O  O   . HOH E 4 .   ? 93.861  40.159 88.949  1.00 40.29 ? 1235 HOH A O   1 
HETATM 4675 O  O   . HOH E 4 .   ? 76.325  6.135  96.595  1.00 49.97 ? 1236 HOH A O   1 
HETATM 4676 O  O   . HOH E 4 .   ? 46.906  53.788 79.311  1.00 47.80 ? 1237 HOH A O   1 
HETATM 4677 O  O   . HOH E 4 .   ? 61.783  13.549 97.062  1.00 37.63 ? 1238 HOH A O   1 
HETATM 4678 O  O   . HOH E 4 .   ? 86.554  28.782 102.751 1.00 29.58 ? 1239 HOH A O   1 
HETATM 4679 O  O   . HOH E 4 .   ? 65.019  15.786 101.007 1.00 43.00 ? 1240 HOH A O   1 
HETATM 4680 O  O   . HOH E 4 .   ? 100.719 34.278 84.106  1.00 47.02 ? 1241 HOH A O   1 
HETATM 4681 O  O   . HOH E 4 .   ? 58.755  58.462 94.504  1.00 41.54 ? 1242 HOH A O   1 
HETATM 4682 O  O   . HOH E 4 .   ? 65.440  31.445 126.524 1.00 47.10 ? 1243 HOH A O   1 
HETATM 4683 O  O   . HOH E 4 .   ? 89.586  34.475 91.940  1.00 37.31 ? 1244 HOH A O   1 
HETATM 4684 O  O   . HOH E 4 .   ? 68.970  63.022 83.135  1.00 30.85 ? 1245 HOH A O   1 
HETATM 4685 O  O   . HOH E 4 .   ? 61.797  65.360 76.141  1.00 50.19 ? 1246 HOH A O   1 
HETATM 4686 O  O   . HOH E 4 .   ? 71.715  24.981 69.434  1.00 39.91 ? 1247 HOH A O   1 
HETATM 4687 O  O   . HOH E 4 .   ? 55.838  42.335 72.292  1.00 49.74 ? 1248 HOH A O   1 
HETATM 4688 O  O   . HOH E 4 .   ? 80.887  62.296 69.089  1.00 49.69 ? 1249 HOH A O   1 
HETATM 4689 O  O   . HOH E 4 .   ? 80.979  8.549  89.469  1.00 40.43 ? 1250 HOH A O   1 
HETATM 4690 O  O   . HOH E 4 .   ? 56.626  11.744 82.546  1.00 40.84 ? 1251 HOH A O   1 
HETATM 4691 O  O   . HOH E 4 .   ? 68.952  29.671 124.068 1.00 48.58 ? 1252 HOH A O   1 
HETATM 4692 O  O   . HOH E 4 .   ? 48.460  18.061 86.099  1.00 26.72 ? 1253 HOH A O   1 
HETATM 4693 O  O   . HOH E 4 .   ? 65.020  42.878 74.191  1.00 30.38 ? 1254 HOH A O   1 
HETATM 4694 O  O   . HOH E 4 .   ? 81.222  12.959 85.535  1.00 40.98 ? 1255 HOH A O   1 
HETATM 4695 O  O   . HOH E 4 .   ? 72.932  31.409 68.736  1.00 46.56 ? 1256 HOH A O   1 
HETATM 4696 O  O   . HOH E 4 .   ? 75.539  41.167 125.815 1.00 35.14 ? 1257 HOH A O   1 
HETATM 4697 O  O   . HOH E 4 .   ? 43.417  32.814 78.406  1.00 39.13 ? 1258 HOH A O   1 
HETATM 4698 O  O   . HOH E 4 .   ? 56.756  65.788 84.124  1.00 45.81 ? 1259 HOH A O   1 
HETATM 4699 O  O   . HOH E 4 .   ? 51.319  18.317 96.040  1.00 46.22 ? 1260 HOH A O   1 
HETATM 4700 O  O   . HOH E 4 .   ? 66.839  15.028 98.893  1.00 50.86 ? 1261 HOH A O   1 
HETATM 4701 O  O   . HOH E 4 .   ? 81.513  12.753 98.608  1.00 27.03 ? 1262 HOH A O   1 
HETATM 4702 O  O   . HOH E 4 .   ? 58.909  19.841 100.483 1.00 41.31 ? 1263 HOH A O   1 
HETATM 4703 O  O   . HOH E 4 .   ? 83.532  37.886 68.640  1.00 31.14 ? 1264 HOH A O   1 
HETATM 4704 O  O   . HOH E 4 .   ? 92.560  26.130 86.340  1.00 25.21 ? 1265 HOH A O   1 
HETATM 4705 O  O   . HOH E 4 .   ? 101.386 37.664 81.731  1.00 52.55 ? 1266 HOH A O   1 
HETATM 4706 O  O   . HOH E 4 .   ? 59.472  53.919 94.837  1.00 26.54 ? 1267 HOH A O   1 
HETATM 4707 O  O   . HOH E 4 .   ? 98.421  29.856 79.301  1.00 41.03 ? 1268 HOH A O   1 
HETATM 4708 O  O   . HOH E 4 .   ? 43.956  40.925 78.295  1.00 49.87 ? 1269 HOH A O   1 
HETATM 4709 O  O   . HOH E 4 .   ? 56.900  14.263 97.242  1.00 34.12 ? 1270 HOH A O   1 
HETATM 4710 O  O   . HOH E 4 .   ? 89.027  27.214 91.850  1.00 21.97 ? 1271 HOH A O   1 
HETATM 4711 O  O   . HOH E 4 .   ? 93.266  47.583 76.943  1.00 45.10 ? 1272 HOH A O   1 
HETATM 4712 O  O   . HOH E 4 .   ? 51.562  33.224 68.809  1.00 37.32 ? 1273 HOH A O   1 
HETATM 4713 O  O   . HOH E 4 .   ? 52.339  39.083 91.873  1.00 28.81 ? 1274 HOH A O   1 
HETATM 4714 O  O   . HOH E 4 .   ? 87.008  30.631 92.336  1.00 35.12 ? 1275 HOH A O   1 
HETATM 4715 O  O   . HOH E 4 .   ? 44.497  32.237 82.029  1.00 40.35 ? 1276 HOH A O   1 
HETATM 4716 O  O   . HOH E 4 .   ? 57.584  40.410 70.846  1.00 35.59 ? 1277 HOH A O   1 
HETATM 4717 O  O   . HOH E 4 .   ? 43.517  43.477 105.592 1.00 48.47 ? 1278 HOH A O   1 
HETATM 4718 O  O   . HOH E 4 .   ? 62.389  56.920 109.079 1.00 55.32 ? 1279 HOH A O   1 
HETATM 4719 O  O   . HOH E 4 .   ? 82.509  53.680 68.257  1.00 44.95 ? 1280 HOH A O   1 
HETATM 4720 O  O   . HOH E 4 .   ? 56.891  26.315 113.490 1.00 46.98 ? 1281 HOH A O   1 
HETATM 4721 O  O   . HOH E 4 .   ? 84.168  24.795 71.487  1.00 43.35 ? 1282 HOH A O   1 
HETATM 4722 O  O   . HOH E 4 .   ? 89.744  39.751 91.083  1.00 22.91 ? 1283 HOH A O   1 
HETATM 4723 O  O   . HOH E 4 .   ? 63.754  64.424 80.559  1.00 49.83 ? 1284 HOH A O   1 
HETATM 4724 O  O   . HOH E 4 .   ? 66.833  29.834 68.150  1.00 36.64 ? 1285 HOH A O   1 
HETATM 4725 O  O   . HOH E 4 .   ? 73.222  22.564 69.546  1.00 48.30 ? 1286 HOH A O   1 
HETATM 4726 O  O   . HOH E 4 .   ? 73.447  62.091 61.242  1.00 48.88 ? 1287 HOH A O   1 
HETATM 4727 O  O   . HOH E 4 .   ? 53.973  17.546 96.409  1.00 44.86 ? 1288 HOH A O   1 
HETATM 4728 O  O   . HOH E 4 .   ? 51.628  42.788 94.493  1.00 50.28 ? 1289 HOH A O   1 
HETATM 4729 O  O   . HOH E 4 .   ? 47.436  39.991 75.077  1.00 44.97 ? 1290 HOH A O   1 
HETATM 4730 O  O   . HOH E 4 .   ? 75.523  17.479 73.459  1.00 35.46 ? 1291 HOH A O   1 
HETATM 4731 O  O   . HOH E 4 .   ? 74.726  18.685 109.642 1.00 41.09 ? 1292 HOH A O   1 
HETATM 4732 O  O   . HOH E 4 .   ? 46.395  43.311 76.565  1.00 49.74 ? 1293 HOH A O   1 
HETATM 4733 O  O   . HOH E 4 .   ? 71.963  48.011 71.061  1.00 34.78 ? 1294 HOH A O   1 
HETATM 4734 O  O   . HOH E 4 .   ? 87.122  31.332 103.414 1.00 40.68 ? 1295 HOH A O   1 
HETATM 4735 O  O   . HOH E 4 .   ? 65.477  8.261  77.091  1.00 46.25 ? 1296 HOH A O   1 
HETATM 4736 O  O   . HOH E 4 .   ? 47.722  24.147 106.979 1.00 34.96 ? 1297 HOH A O   1 
HETATM 4737 O  O   . HOH E 4 .   ? 59.058  38.096 67.780  1.00 44.30 ? 1298 HOH A O   1 
HETATM 4738 O  O   . HOH E 4 .   ? 55.378  35.980 68.643  1.00 42.23 ? 1299 HOH A O   1 
HETATM 4739 O  O   . HOH E 4 .   ? 61.844  7.457  79.005  1.00 48.89 ? 1300 HOH A O   1 
HETATM 4740 O  O   . HOH E 4 .   ? 62.125  48.636 117.028 1.00 37.41 ? 1301 HOH A O   1 
HETATM 4741 O  O   . HOH E 4 .   ? 76.016  26.340 68.716  1.00 36.47 ? 1302 HOH A O   1 
HETATM 4742 O  O   . HOH E 4 .   ? 84.441  22.316 80.198  1.00 45.74 ? 1303 HOH A O   1 
HETATM 4743 O  O   . HOH E 4 .   ? 63.610  35.023 117.298 1.00 52.86 ? 1304 HOH A O   1 
HETATM 4744 O  O   . HOH E 4 .   ? 94.885  25.830 75.752  1.00 36.60 ? 1305 HOH A O   1 
HETATM 4745 O  O   . HOH E 4 .   ? 86.159  34.546 97.434  1.00 47.11 ? 1306 HOH A O   1 
HETATM 4746 O  O   . HOH E 4 .   ? 52.761  35.186 69.896  1.00 37.59 ? 1307 HOH A O   1 
HETATM 4747 O  O   . HOH E 4 .   ? 57.608  40.748 116.304 1.00 48.93 ? 1308 HOH A O   1 
HETATM 4748 O  O   . HOH E 4 .   ? 76.520  23.687 68.624  1.00 40.04 ? 1309 HOH A O   1 
HETATM 4749 O  O   . HOH E 4 .   ? 90.221  18.637 107.634 1.00 45.47 ? 1310 HOH A O   1 
HETATM 4750 O  O   . HOH E 4 .   ? 67.817  60.029 97.429  1.00 39.41 ? 1311 HOH A O   1 
HETATM 4751 O  O   . HOH E 4 .   ? 78.420  36.321 100.798 1.00 43.01 ? 1312 HOH A O   1 
HETATM 4752 O  O   . HOH E 4 .   ? 84.049  27.953 103.701 1.00 30.80 ? 1313 HOH A O   1 
HETATM 4753 O  O   . HOH E 4 .   ? 82.653  28.196 68.214  1.00 35.62 ? 1314 HOH A O   1 
HETATM 4754 O  O   . HOH E 4 .   ? 86.120  41.062 93.909  1.00 29.98 ? 1315 HOH A O   1 
HETATM 4755 O  O   . HOH E 4 .   ? 57.958  55.273 97.248  1.00 48.30 ? 1316 HOH A O   1 
HETATM 4756 O  O   . HOH E 4 .   ? 66.622  66.059 68.157  1.00 39.81 ? 1317 HOH A O   1 
HETATM 4757 O  O   . HOH E 4 .   ? 80.025  31.659 105.372 1.00 49.81 ? 1318 HOH A O   1 
HETATM 4758 O  O   . HOH E 4 .   ? 54.482  9.739  82.002  1.00 35.36 ? 1319 HOH A O   1 
HETATM 4759 O  O   . HOH E 4 .   ? 45.810  27.545 108.607 1.00 40.54 ? 1320 HOH A O   1 
HETATM 4760 O  O   . HOH E 4 .   ? 59.792  50.655 116.692 1.00 47.49 ? 1321 HOH A O   1 
HETATM 4761 O  O   . HOH E 4 .   ? 56.238  38.929 116.818 1.00 49.95 ? 1322 HOH A O   1 
HETATM 4762 O  O   . HOH E 4 .   ? 60.876  17.358 113.498 1.00 53.38 ? 1323 HOH A O   1 
HETATM 4763 O  O   . HOH E 4 .   ? 82.896  30.209 104.888 1.00 35.32 ? 1324 HOH A O   1 
HETATM 4764 O  O   . HOH E 4 .   ? 82.114  23.684 67.931  1.00 54.29 ? 1325 HOH A O   1 
HETATM 4765 O  O   . HOH E 4 .   ? 83.635  26.135 68.702  1.00 39.82 ? 1326 HOH A O   1 
HETATM 4766 O  O   . HOH E 4 .   ? 68.858  67.273 69.001  1.00 52.80 ? 1327 HOH A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . LYS A 44  ? 0.3930 0.6246 0.6497 -0.0046 0.0687  0.0686  44  LYS A N   
2    C CA  . LYS A 44  ? 0.2726 0.4963 0.5234 0.0050  0.0756  0.0531  44  LYS A CA  
3    C C   . LYS A 44  ? 0.3128 0.5071 0.5398 0.0030  0.0605  0.0522  44  LYS A C   
4    O O   . LYS A 44  ? 0.2963 0.4795 0.5299 -0.0010 0.0447  0.0615  44  LYS A O   
5    C CB  . LYS A 44  ? 0.3352 0.5626 0.6154 0.0139  0.0783  0.0470  44  LYS A CB  
6    C CG  . LYS A 44  ? 0.3788 0.5941 0.6561 0.0234  0.0832  0.0310  44  LYS A CG  
7    C CD  . LYS A 44  ? 0.4201 0.6448 0.6778 0.0271  0.1001  0.0128  44  LYS A CD  
8    C CE  . LYS A 44  ? 0.4653 0.6715 0.7014 0.0309  0.1008  -0.0002 44  LYS A CE  
9    N NZ  . LYS A 44  ? 0.4997 0.7139 0.7028 0.0288  0.1113  -0.0112 44  LYS A NZ  
10   N N   . VAL A 45  ? 0.2453 0.4278 0.4427 0.0053  0.0651  0.0404  45  VAL A N   
11   C CA  . VAL A 45  ? 0.2051 0.3606 0.3781 0.0038  0.0528  0.0384  45  VAL A CA  
12   C C   . VAL A 45  ? 0.2248 0.3709 0.4111 0.0117  0.0509  0.0317  45  VAL A C   
13   O O   . VAL A 45  ? 0.2192 0.3695 0.4118 0.0194  0.0625  0.0190  45  VAL A O   
14   C CB  . VAL A 45  ? 0.2111 0.3591 0.3502 0.0022  0.0574  0.0310  45  VAL A CB  
15   C CG1 . VAL A 45  ? 0.2022 0.3239 0.3194 0.0014  0.0460  0.0287  45  VAL A CG1 
16   C CG2 . VAL A 45  ? 0.2178 0.3759 0.3482 -0.0059 0.0584  0.0409  45  VAL A CG2 
17   N N   . ASP A 46  ? 0.1626 0.2970 0.3548 0.0091  0.0358  0.0406  46  ASP A N   
18   C CA  . ASP A 46  ? 0.1317 0.2563 0.3363 0.0148  0.0306  0.0393  46  ASP A CA  
19   C C   . ASP A 46  ? 0.1560 0.2583 0.3277 0.0116  0.0220  0.0372  46  ASP A C   
20   O O   . ASP A 46  ? 0.1573 0.2514 0.3139 0.0040  0.0098  0.0450  46  ASP A O   
21   C CB  . ASP A 46  ? 0.1517 0.2831 0.3852 0.0124  0.0185  0.0540  46  ASP A CB  
22   C CG  . ASP A 46  ? 0.1462 0.2684 0.3939 0.0164  0.0098  0.0581  46  ASP A CG  
23   O OD1 . ASP A 46  ? 0.1409 0.2495 0.3758 0.0206  0.0125  0.0497  46  ASP A OD1 
24   O OD2 . ASP A 46  ? 0.2009 0.3309 0.4749 0.0147  -0.0006 0.0715  46  ASP A OD2 
25   N N   . PRO A 47  ? 0.1339 0.2268 0.2946 0.0169  0.0283  0.0260  47  PRO A N   
26   C CA  . PRO A 47  ? 0.1684 0.2424 0.2997 0.0141  0.0215  0.0244  47  PRO A CA  
27   C C   . PRO A 47  ? 0.1763 0.2412 0.3070 0.0102  0.0067  0.0353  47  PRO A C   
28   O O   . PRO A 47  ? 0.1575 0.2097 0.2611 0.0055  0.0005  0.0357  47  PRO A O   
29   C CB  . PRO A 47  ? 0.1458 0.2146 0.2786 0.0213  0.0302  0.0120  47  PRO A CB  
30   C CG  . PRO A 47  ? 0.1646 0.2499 0.3114 0.0257  0.0445  0.0024  47  PRO A CG  
31   C CD  . PRO A 47  ? 0.1313 0.2317 0.3062 0.0252  0.0428  0.0127  47  PRO A CD  
32   N N   . SER A 48  ? 0.1540 0.2263 0.3141 0.0119  0.0010  0.0444  48  SER A N   
33   C CA  . SER A 48  ? 0.1592 0.2266 0.3188 0.0072  -0.0141 0.0568  48  SER A CA  
34   C C   . SER A 48  ? 0.1644 0.2361 0.3159 -0.0024 -0.0253 0.0655  48  SER A C   
35   O O   . SER A 48  ? 0.2010 0.2697 0.3447 -0.0085 -0.0387 0.0745  48  SER A O   
36   C CB  . SER A 48  ? 0.1335 0.2080 0.3315 0.0125  -0.0176 0.0658  48  SER A CB  
37   O OG  . SER A 48  ? 0.1588 0.2502 0.3894 0.0139  -0.0166 0.0714  48  SER A OG  
38   N N   . ASN A 49  ? 0.1625 0.2419 0.3155 -0.0047 -0.0204 0.0631  49  ASN A N   
39   C CA  . ASN A 49  ? 0.1694 0.2526 0.3196 -0.0144 -0.0311 0.0706  49  ASN A CA  
40   C C   . ASN A 49  ? 0.1403 0.2146 0.2633 -0.0189 -0.0275 0.0630  49  ASN A C   
41   O O   . ASN A 49  ? 0.1840 0.2664 0.3137 -0.0179 -0.0181 0.0609  49  ASN A O   
42   C CB  . ASN A 49  ? 0.1629 0.2659 0.3493 -0.0140 -0.0302 0.0788  49  ASN A CB  
43   C CG  . ASN A 49  ? 0.2029 0.3100 0.3898 -0.0252 -0.0436 0.0876  49  ASN A CG  
44   O OD1 . ASN A 49  ? 0.1972 0.2910 0.3554 -0.0329 -0.0516 0.0845  49  ASN A OD1 
45   N ND2 . ASN A 49  ? 0.1937 0.3191 0.4145 -0.0262 -0.0456 0.0974  49  ASN A ND2 
46   N N   . PRO A 50  ? 0.1760 0.2348 0.2698 -0.0239 -0.0342 0.0593  50  PRO A N   
47   C CA  . PRO A 50  ? 0.1994 0.2477 0.2712 -0.0267 -0.0301 0.0518  50  PRO A CA  
48   C C   . PRO A 50  ? 0.1965 0.2502 0.2775 -0.0337 -0.0332 0.0561  50  PRO A C   
49   O O   . PRO A 50  ? 0.2069 0.2561 0.2793 -0.0346 -0.0274 0.0527  50  PRO A O   
50   C CB  . PRO A 50  ? 0.2582 0.2904 0.3020 -0.0305 -0.0374 0.0471  50  PRO A CB  
51   C CG  . PRO A 50  ? 0.3803 0.4176 0.4301 -0.0333 -0.0487 0.0548  50  PRO A CG  
52   C CD  . PRO A 50  ? 0.2545 0.3057 0.3351 -0.0263 -0.0443 0.0618  50  PRO A CD  
53   N N   . GLU A 51  ? 0.2030 0.2673 0.3039 -0.0391 -0.0428 0.0650  51  GLU A N   
54   C CA  . GLU A 51  ? 0.2159 0.2866 0.3300 -0.0465 -0.0458 0.0704  51  GLU A CA  
55   C C   . GLU A 51  ? 0.2366 0.3236 0.3700 -0.0417 -0.0319 0.0738  51  GLU A C   
56   O O   . GLU A 51  ? 0.2519 0.3442 0.3940 -0.0475 -0.0317 0.0789  51  GLU A O   
57   C CB  . GLU A 51  ? 0.2798 0.3592 0.4116 -0.0543 -0.0608 0.0796  51  GLU A CB  
58   C CG  . GLU A 51  ? 0.3525 0.4170 0.4614 -0.0641 -0.0758 0.0751  51  GLU A CG  
59   C CD  . GLU A 51  ? 0.4652 0.5402 0.5887 -0.0728 -0.0926 0.0845  51  GLU A CD  
60   O OE1 . GLU A 51  ? 0.5031 0.5971 0.6589 -0.0710 -0.0928 0.0961  51  GLU A OE1 
61   O OE2 . GLU A 51  ? 0.5862 0.6518 0.6894 -0.0817 -0.1056 0.0800  51  GLU A OE2 
62   N N   . THR A 52  ? 0.1908 0.2862 0.3310 -0.0318 -0.0201 0.0706  52  THR A N   
63   C CA  . THR A 52  ? 0.1623 0.2748 0.3159 -0.0272 -0.0050 0.0708  52  THR A CA  
64   C C   . THR A 52  ? 0.1633 0.2693 0.2929 -0.0244 0.0054  0.0627  52  THR A C   
65   O O   . THR A 52  ? 0.1887 0.3105 0.3242 -0.0216 0.0182  0.0622  52  THR A O   
66   C CB  . THR A 52  ? 0.1518 0.2791 0.3296 -0.0181 0.0034  0.0695  52  THR A CB  
67   O OG1 . THR A 52  ? 0.1725 0.2883 0.3358 -0.0106 0.0080  0.0591  52  THR A OG1 
68   C CG2 . THR A 52  ? 0.1850 0.3195 0.3898 -0.0202 -0.0082 0.0795  52  THR A CG2 
69   N N   . ILE A 53  ? 0.1680 0.2535 0.2713 -0.0252 0.0006  0.0566  53  ILE A N   
70   C CA  . ILE A 53  ? 0.1714 0.2510 0.2539 -0.0220 0.0091  0.0497  53  ILE A CA  
71   C C   . ILE A 53  ? 0.1861 0.2612 0.2615 -0.0291 0.0066  0.0550  53  ILE A C   
72   O O   . ILE A 53  ? 0.2257 0.2842 0.2933 -0.0341 -0.0037 0.0549  53  ILE A O   
73   C CB  . ILE A 53  ? 0.1962 0.2579 0.2587 -0.0181 0.0065  0.0410  53  ILE A CB  
74   C CG1 . ILE A 53  ? 0.1899 0.2554 0.2634 -0.0113 0.0086  0.0377  53  ILE A CG1 
75   C CG2 . ILE A 53  ? 0.2073 0.2639 0.2507 -0.0158 0.0138  0.0354  53  ILE A CG2 
76   C CD1 . ILE A 53  ? 0.2136 0.2624 0.2721 -0.0099 0.0020  0.0339  53  ILE A CD1 
77   N N   . PRO A 54  ? 0.1868 0.2762 0.2651 -0.0299 0.0155  0.0597  54  PRO A N   
78   C CA  . PRO A 54  ? 0.1734 0.2582 0.2488 -0.0368 0.0122  0.0676  54  PRO A CA  
79   C C   . PRO A 54  ? 0.2036 0.2700 0.2571 -0.0348 0.0110  0.0614  54  PRO A C   
80   O O   . PRO A 54  ? 0.2103 0.2803 0.2511 -0.0296 0.0186  0.0560  54  PRO A O   
81   C CB  . PRO A 54  ? 0.2028 0.3129 0.2867 -0.0379 0.0233  0.0760  54  PRO A CB  
82   C CG  . PRO A 54  ? 0.2398 0.3680 0.3349 -0.0321 0.0321  0.0712  54  PRO A CG  
83   C CD  . PRO A 54  ? 0.1916 0.3047 0.2800 -0.0256 0.0286  0.0593  54  PRO A CD  
84   N N   . LYS A 55  ? 0.1855 0.2329 0.2365 -0.0393 0.0015  0.0615  55  LYS A N   
85   C CA  A LYS A 55  ? 0.1924 0.2218 0.2265 -0.0370 0.0004  0.0552  55  LYS A CA  
86   C CA  B LYS A 55  ? 0.1952 0.2250 0.2292 -0.0368 0.0006  0.0552  55  LYS A CA  
87   C C   . LYS A 55  ? 0.2117 0.2470 0.2461 -0.0383 0.0049  0.0638  55  LYS A C   
88   O O   . LYS A 55  ? 0.2038 0.2528 0.2518 -0.0434 0.0060  0.0762  55  LYS A O   
89   C CB  A LYS A 55  ? 0.2133 0.2212 0.2462 -0.0412 -0.0099 0.0504  55  LYS A CB  
90   C CB  B LYS A 55  ? 0.2157 0.2237 0.2477 -0.0407 -0.0095 0.0499  55  LYS A CB  
91   C CG  A LYS A 55  ? 0.1963 0.1998 0.2251 -0.0413 -0.0159 0.0431  55  LYS A CG  
92   C CG  B LYS A 55  ? 0.1872 0.1909 0.2130 -0.0397 -0.0144 0.0420  55  LYS A CG  
93   C CD  A LYS A 55  ? 0.2232 0.2067 0.2450 -0.0460 -0.0251 0.0353  55  LYS A CD  
94   C CD  B LYS A 55  ? 0.2117 0.1964 0.2309 -0.0444 -0.0237 0.0345  55  LYS A CD  
95   C CE  A LYS A 55  ? 0.2654 0.2485 0.3046 -0.0554 -0.0344 0.0404  55  LYS A CE  
96   C CE  B LYS A 55  ? 0.2421 0.2270 0.2530 -0.0442 -0.0287 0.0294  55  LYS A CE  
97   N NZ  A LYS A 55  ? 0.3122 0.3094 0.3610 -0.0582 -0.0393 0.0449  55  LYS A NZ  
98   N NZ  B LYS A 55  ? 0.2744 0.2437 0.2737 -0.0495 -0.0373 0.0202  55  LYS A NZ  
99   N N   . TYR A 56  ? 0.1757 0.2020 0.1959 -0.0340 0.0069  0.0588  56  TYR A N   
100  C CA  . TYR A 56  ? 0.1808 0.2092 0.2017 -0.0355 0.0082  0.0680  56  TYR A CA  
101  C C   . TYR A 56  ? 0.1973 0.2519 0.2169 -0.0365 0.0159  0.0768  56  TYR A C   
102  O O   . TYR A 56  ? 0.2401 0.3036 0.2654 -0.0410 0.0158  0.0906  56  TYR A O   
103  C CB  . TYR A 56  ? 0.1984 0.2154 0.2363 -0.0419 0.0007  0.0769  56  TYR A CB  
104  C CG  . TYR A 56  ? 0.1983 0.1932 0.2387 -0.0431 -0.0069 0.0663  56  TYR A CG  
105  C CD1 . TYR A 56  ? 0.2102 0.1881 0.2364 -0.0382 -0.0075 0.0524  56  TYR A CD1 
106  C CD2 . TYR A 56  ? 0.1933 0.1862 0.2499 -0.0503 -0.0136 0.0703  56  TYR A CD2 
107  C CE1 . TYR A 56  ? 0.2217 0.1819 0.2468 -0.0404 -0.0140 0.0416  56  TYR A CE1 
108  C CE2 . TYR A 56  ? 0.2519 0.2258 0.3082 -0.0528 -0.0214 0.0591  56  TYR A CE2 
109  C CZ  . TYR A 56  ? 0.2140 0.1724 0.2527 -0.0478 -0.0212 0.0442  56  TYR A CZ  
110  O OH  . TYR A 56  ? 0.2555 0.1978 0.2913 -0.0515 -0.0286 0.0323  56  TYR A OH  
111  N N   . MET A 57  ? 0.1914 0.2593 0.2039 -0.0326 0.0229  0.0690  57  MET A N   
112  C CA  . MET A 57  ? 0.1911 0.2852 0.1989 -0.0333 0.0320  0.0730  57  MET A CA  
113  C C   . MET A 57  ? 0.1880 0.2840 0.1776 -0.0302 0.0350  0.0675  57  MET A C   
114  O O   . MET A 57  ? 0.2346 0.3508 0.2171 -0.0327 0.0399  0.0725  57  MET A O   
115  C CB  . MET A 57  ? 0.2265 0.3341 0.2390 -0.0301 0.0391  0.0648  57  MET A CB  
116  C CG  . MET A 57  ? 0.2667 0.3822 0.2998 -0.0343 0.0378  0.0734  57  MET A CG  
117  S SD  . MET A 57  ? 0.3172 0.4598 0.3596 -0.0308 0.0505  0.0678  57  MET A SD  
118  C CE  . MET A 57  ? 0.3779 0.5459 0.4191 -0.0369 0.0570  0.0809  57  MET A CE  
119  N N   . ASP A 58  ? 0.1741 0.2503 0.1559 -0.0253 0.0314  0.0572  58  ASP A N   
120  C CA  . ASP A 58  ? 0.2024 0.2796 0.1693 -0.0225 0.0333  0.0512  58  ASP A CA  
121  C C   . ASP A 58  ? 0.2196 0.2842 0.1869 -0.0236 0.0268  0.0590  58  ASP A C   
122  O O   . ASP A 58  ? 0.2137 0.2581 0.1882 -0.0224 0.0216  0.0580  58  ASP A O   
123  C CB  . ASP A 58  ? 0.1884 0.2541 0.1499 -0.0161 0.0345  0.0352  58  ASP A CB  
124  C CG  . ASP A 58  ? 0.2279 0.3064 0.1923 -0.0138 0.0415  0.0268  58  ASP A CG  
125  O OD1 . ASP A 58  ? 0.2734 0.3666 0.2297 -0.0132 0.0479  0.0205  58  ASP A OD1 
126  O OD2 . ASP A 58  ? 0.2027 0.2780 0.1792 -0.0129 0.0407  0.0263  58  ASP A OD2 
127  N N   . GLU A 59  ? 0.1999 0.2776 0.1601 -0.0260 0.0271  0.0661  59  GLU A N   
128  C CA  . GLU A 59  ? 0.1844 0.2520 0.1475 -0.0258 0.0212  0.0733  59  GLU A CA  
129  C C   . GLU A 59  ? 0.2162 0.2704 0.1711 -0.0197 0.0212  0.0592  59  GLU A C   
130  O O   . GLU A 59  ? 0.2158 0.2788 0.1585 -0.0182 0.0250  0.0495  59  GLU A O   
131  C CB  . GLU A 59  ? 0.1788 0.2652 0.1395 -0.0298 0.0193  0.0833  59  GLU A CB  
132  C CG  . GLU A 59  ? 0.2154 0.2951 0.1834 -0.0298 0.0125  0.0934  59  GLU A CG  
133  C CD  . GLU A 59  ? 0.2137 0.2824 0.2039 -0.0318 0.0071  0.1082  59  GLU A CD  
134  O OE1 . GLU A 59  ? 0.2487 0.3198 0.2477 -0.0351 0.0073  0.1133  59  GLU A OE1 
135  O OE2 . GLU A 59  ? 0.2552 0.3124 0.2572 -0.0299 0.0025  0.1144  59  GLU A OE2 
136  N N   . LEU A 60  ? 0.1854 0.2186 0.1481 -0.0165 0.0176  0.0575  60  LEU A N   
137  C CA  . LEU A 60  ? 0.1802 0.2014 0.1373 -0.0111 0.0181  0.0463  60  LEU A CA  
138  C C   . LEU A 60  ? 0.1796 0.2136 0.1285 -0.0114 0.0182  0.0472  60  LEU A C   
139  O O   . LEU A 60  ? 0.2001 0.2426 0.1536 -0.0144 0.0146  0.0597  60  LEU A O   
140  C CB  . LEU A 60  ? 0.1895 0.1918 0.1582 -0.0087 0.0150  0.0479  60  LEU A CB  
141  C CG  . LEU A 60  ? 0.1865 0.1784 0.1510 -0.0033 0.0167  0.0380  60  LEU A CG  
142  C CD1 . LEU A 60  ? 0.2303 0.2100 0.1888 -0.0011 0.0187  0.0258  60  LEU A CD1 
143  C CD2 . LEU A 60  ? 0.2303 0.2126 0.2089 -0.0010 0.0148  0.0432  60  LEU A CD2 
144  N N   . PRO A 61  ? 0.1964 0.2321 0.1353 -0.0091 0.0211  0.0349  61  PRO A N   
145  C CA  . PRO A 61  ? 0.2118 0.2585 0.1434 -0.0103 0.0200  0.0338  61  PRO A CA  
146  C C   . PRO A 61  ? 0.1892 0.2238 0.1272 -0.0067 0.0173  0.0340  61  PRO A C   
147  O O   . PRO A 61  ? 0.2084 0.2264 0.1515 -0.0024 0.0187  0.0289  61  PRO A O   
148  C CB  . PRO A 61  ? 0.2615 0.3117 0.1843 -0.0090 0.0244  0.0187  61  PRO A CB  
149  C CG  . PRO A 61  ? 0.2843 0.3242 0.2117 -0.0061 0.0275  0.0135  61  PRO A CG  
150  C CD  . PRO A 61  ? 0.2098 0.2395 0.1457 -0.0063 0.0248  0.0228  61  PRO A CD  
151  N N   . ILE A 62  ? 0.1987 0.2442 0.1363 -0.0091 0.0134  0.0400  62  ILE A N   
152  C CA  . ILE A 62  ? 0.1851 0.2235 0.1312 -0.0060 0.0111  0.0408  62  ILE A CA  
153  C C   . ILE A 62  ? 0.1833 0.2271 0.1205 -0.0068 0.0112  0.0300  62  ILE A C   
154  O O   . ILE A 62  ? 0.1998 0.2606 0.1273 -0.0121 0.0087  0.0297  62  ILE A O   
155  C CB  . ILE A 62  ? 0.2211 0.2689 0.1781 -0.0086 0.0049  0.0574  62  ILE A CB  
156  C CG1 . ILE A 62  ? 0.2767 0.3214 0.2444 -0.0094 0.0037  0.0696  62  ILE A CG1 
157  C CG2 . ILE A 62  ? 0.2242 0.2647 0.1945 -0.0043 0.0035  0.0582  62  ILE A CG2 
158  C CD1 . ILE A 62  ? 0.3065 0.3292 0.2875 -0.0035 0.0068  0.0654  62  ILE A CD1 
159  N N   . PRO A 63  ? 0.1791 0.2104 0.1195 -0.0026 0.0139  0.0212  63  PRO A N   
160  C CA  . PRO A 63  ? 0.1772 0.2125 0.1134 -0.0040 0.0132  0.0117  63  PRO A CA  
161  C C   . PRO A 63  ? 0.1796 0.2282 0.1179 -0.0082 0.0068  0.0182  63  PRO A C   
162  O O   . PRO A 63  ? 0.2093 0.2584 0.1592 -0.0070 0.0037  0.0300  63  PRO A O   
163  C CB  . PRO A 63  ? 0.2005 0.2204 0.1441 0.0010  0.0165  0.0070  63  PRO A CB  
164  C CG  . PRO A 63  ? 0.2112 0.2197 0.1560 0.0045  0.0201  0.0090  63  PRO A CG  
165  C CD  . PRO A 63  ? 0.1842 0.1980 0.1314 0.0028  0.0177  0.0191  63  PRO A CD  
166  N N   . PRO A 64  ? 0.1905 0.2506 0.1196 -0.0132 0.0041  0.0103  64  PRO A N   
167  C CA  . PRO A 64  ? 0.2037 0.2784 0.1338 -0.0187 -0.0038 0.0163  64  PRO A CA  
168  C C   . PRO A 64  ? 0.1925 0.2593 0.1382 -0.0159 -0.0056 0.0175  64  PRO A C   
169  O O   . PRO A 64  ? 0.2109 0.2631 0.1624 -0.0112 -0.0004 0.0105  64  PRO A O   
170  C CB  . PRO A 64  ? 0.2546 0.3416 0.1689 -0.0250 -0.0049 0.0023  64  PRO A CB  
171  C CG  . PRO A 64  ? 0.2808 0.3543 0.1944 -0.0206 0.0027  -0.0125 64  PRO A CG  
172  C CD  . PRO A 64  ? 0.2138 0.2747 0.1328 -0.0143 0.0081  -0.0053 64  PRO A CD  
173  N N   . VAL A 65  ? 0.1867 0.2653 0.1404 -0.0194 -0.0132 0.0284  65  VAL A N   
174  C CA  . VAL A 65  ? 0.1763 0.2514 0.1479 -0.0174 -0.0151 0.0315  65  VAL A CA  
175  C C   . VAL A 65  ? 0.2077 0.2875 0.1757 -0.0231 -0.0194 0.0197  65  VAL A C   
176  O O   . VAL A 65  ? 0.2287 0.3230 0.1837 -0.0310 -0.0260 0.0154  65  VAL A O   
177  C CB  . VAL A 65  ? 0.2265 0.3129 0.2138 -0.0182 -0.0220 0.0498  65  VAL A CB  
178  C CG1 . VAL A 65  ? 0.2045 0.2912 0.2127 -0.0167 -0.0241 0.0534  65  VAL A CG1 
179  C CG2 . VAL A 65  ? 0.2595 0.3370 0.2559 -0.0117 -0.0170 0.0597  65  VAL A CG2 
180  N N   . ALA A 66  ? 0.2015 0.2695 0.1810 -0.0198 -0.0157 0.0142  66  ALA A N   
181  C CA  . ALA A 66  ? 0.1848 0.2549 0.1667 -0.0254 -0.0204 0.0040  66  ALA A CA  
182  C C   . ALA A 66  ? 0.1933 0.2804 0.1833 -0.0323 -0.0315 0.0121  66  ALA A C   
183  O O   . ALA A 66  ? 0.2024 0.2948 0.2074 -0.0299 -0.0335 0.0276  66  ALA A O   
184  C CB  . ALA A 66  ? 0.2008 0.2565 0.1980 -0.0207 -0.0146 0.0019  66  ALA A CB  
185  N N   . ARG A 67  ? 0.2110 0.3070 0.1924 -0.0412 -0.0391 0.0009  67  ARG A N   
186  C CA  . ARG A 67  ? 0.2162 0.3300 0.2034 -0.0499 -0.0517 0.0071  67  ARG A CA  
187  C C   . ARG A 67  ? 0.2109 0.3200 0.2127 -0.0539 -0.0556 -0.0020 67  ARG A C   
188  O O   . ARG A 67  ? 0.2601 0.3586 0.2564 -0.0552 -0.0526 -0.0198 67  ARG A O   
189  C CB  . ARG A 67  ? 0.2638 0.3959 0.2260 -0.0594 -0.0591 0.0011  67  ARG A CB  
190  C CG  . ARG A 67  ? 0.3078 0.4480 0.2570 -0.0572 -0.0566 0.0130  67  ARG A CG  
191  C CD  . ARG A 67  ? 0.4431 0.6066 0.3666 -0.0684 -0.0644 0.0092  67  ARG A CD  
192  N NE  . ARG A 67  ? 0.6488 0.8125 0.5523 -0.0662 -0.0557 0.0047  67  ARG A NE  
193  C CZ  . ARG A 67  ? 0.7075 0.8601 0.6004 -0.0635 -0.0459 -0.0159 67  ARG A CZ  
194  N NH1 . ARG A 67  ? 0.6498 0.7906 0.5480 -0.0637 -0.0448 -0.0348 67  ARG A NH1 
195  N NH2 . ARG A 67  ? 0.6472 0.7982 0.5303 -0.0597 -0.0365 -0.0162 67  ARG A NH2 
196  N N   . PRO A 68  ? 0.2070 0.3238 0.2306 -0.0561 -0.0623 0.0104  68  PRO A N   
197  C CA  . PRO A 68  ? 0.1942 0.3076 0.2351 -0.0610 -0.0668 0.0036  68  PRO A CA  
198  C C   . PRO A 68  ? 0.2515 0.3740 0.2791 -0.0734 -0.0782 -0.0128 68  PRO A C   
199  O O   . PRO A 68  ? 0.2785 0.4180 0.2868 -0.0802 -0.0860 -0.0131 68  PRO A O   
200  C CB  . PRO A 68  ? 0.2731 0.3973 0.3413 -0.0604 -0.0714 0.0235  68  PRO A CB  
201  C CG  . PRO A 68  ? 0.2569 0.3957 0.3190 -0.0596 -0.0754 0.0380  68  PRO A CG  
202  C CD  . PRO A 68  ? 0.2149 0.3442 0.2529 -0.0538 -0.0660 0.0322  68  PRO A CD  
203  N N   . LEU A 69  ? 0.2321 0.3434 0.2707 -0.0769 -0.0791 -0.0269 69  LEU A N   
204  C CA  . LEU A 69  ? 0.3330 0.4504 0.3636 -0.0892 -0.0901 -0.0457 69  LEU A CA  
205  C C   . LEU A 69  ? 0.2936 0.4266 0.3421 -0.0993 -0.1051 -0.0371 69  LEU A C   
206  O O   . LEU A 69  ? 0.3443 0.4911 0.3802 -0.1117 -0.1177 -0.0484 69  LEU A O   
207  C CB  . LEU A 69  ? 0.3747 0.4709 0.4149 -0.0884 -0.0850 -0.0651 69  LEU A CB  
208  C CG  . LEU A 69  ? 0.4396 0.5219 0.4632 -0.0817 -0.0733 -0.0808 69  LEU A CG  
209  C CD1 . LEU A 69  ? 0.5295 0.5967 0.5650 -0.0857 -0.0742 -0.1038 69  LEU A CD1 
210  C CD2 . LEU A 69  ? 0.5380 0.6352 0.5285 -0.0836 -0.0727 -0.0869 69  LEU A CD2 
211  N N   . ALA A 70  ? 0.2671 0.3996 0.3448 -0.0949 -0.1040 -0.0179 70  ALA A N   
212  C CA  . ALA A 70  ? 0.3041 0.4534 0.4029 -0.1046 -0.1186 -0.0078 70  ALA A CA  
213  C C   . ALA A 70  ? 0.2420 0.3986 0.3655 -0.0964 -0.1145 0.0189  70  ALA A C   
214  O O   . ALA A 70  ? 0.2175 0.3639 0.3407 -0.0839 -0.1001 0.0264  70  ALA A O   
215  C CB  . ALA A 70  ? 0.2861 0.4260 0.4058 -0.1123 -0.1243 -0.0202 70  ALA A CB  
216  N N   . GLU A 71  ? 0.2777 0.4528 0.4234 -0.1037 -0.1273 0.0324  71  GLU A N   
217  C CA  . GLU A 71  ? 0.2658 0.4488 0.4436 -0.0962 -0.1231 0.0564  71  GLU A CA  
218  C C   . GLU A 71  ? 0.2282 0.4151 0.4322 -0.1021 -0.1298 0.0599  71  GLU A C   
219  O O   . GLU A 71  ? 0.2816 0.4787 0.4793 -0.1111 -0.1426 0.0567  71  GLU A O   
220  C CB  . GLU A 71  ? 0.3219 0.5202 0.4947 -0.0926 -0.1261 0.0734  71  GLU A CB  
221  N N   . ILE A 72  ? 0.2790 0.4582 0.5109 -0.0967 -0.1201 0.0666  72  ILE A N   
222  C CA  . ILE A 72  ? 0.2769 0.4576 0.5340 -0.1014 -0.1239 0.0705  72  ILE A CA  
223  C C   . ILE A 72  ? 0.2426 0.4328 0.5267 -0.0926 -0.1166 0.0933  72  ILE A C   
224  O O   . ILE A 72  ? 0.2898 0.4746 0.5855 -0.0819 -0.1010 0.1011  72  ILE A O   
225  C CB  . ILE A 72  ? 0.3196 0.4830 0.5872 -0.1028 -0.1178 0.0604  72  ILE A CB  
226  C CG1 . ILE A 72  ? 0.3266 0.4762 0.5692 -0.1087 -0.1216 0.0364  72  ILE A CG1 
227  C CG2 . ILE A 72  ? 0.2891 0.4547 0.5809 -0.1092 -0.1237 0.0641  72  ILE A CG2 
228  C CD1 . ILE A 72  ? 0.3685 0.5256 0.5895 -0.1201 -0.1370 0.0203  72  ILE A CD1 
229  N N   . LYS A 73  ? 0.2239 0.4278 0.5182 -0.0972 -0.1272 0.1030  73  LYS A N   
230  C CA  . LYS A 73  ? 0.2465 0.4592 0.5681 -0.0891 -0.1210 0.1242  73  LYS A CA  
231  C C   . LYS A 73  ? 0.2060 0.4173 0.5258 -0.0758 -0.1076 0.1328  73  LYS A C   
232  O O   . LYS A 73  ? 0.2923 0.5016 0.6321 -0.0652 -0.0929 0.1426  73  LYS A O   
233  C CB  . LYS A 73  ? 0.3217 0.5307 0.6711 -0.0874 -0.1132 0.1297  73  LYS A CB  
234  C CG  . LYS A 73  ? 0.3631 0.5687 0.7156 -0.1000 -0.1244 0.1188  73  LYS A CG  
235  C CD  . LYS A 73  ? 0.3288 0.5490 0.6924 -0.1089 -0.1400 0.1256  73  LYS A CD  
236  C CE  . LYS A 73  ? 0.2795 0.4963 0.6531 -0.1205 -0.1495 0.1163  73  LYS A CE  
237  N NZ  . LYS A 73  ? 0.3181 0.5489 0.6895 -0.1321 -0.1684 0.1150  73  LYS A NZ  
238  N N   . GLY A 74  ? 0.2580 0.4701 0.5525 -0.0765 -0.1121 0.1279  74  GLY A N   
239  C CA  . GLY A 74  ? 0.2414 0.4511 0.5329 -0.0648 -0.1012 0.1349  74  GLY A CA  
240  C C   . GLY A 74  ? 0.2492 0.4460 0.5315 -0.0574 -0.0867 0.1253  74  GLY A C   
241  O O   . GLY A 74  ? 0.2919 0.4859 0.5711 -0.0476 -0.0775 0.1293  74  GLY A O   
242  N N   . SER A 75  ? 0.2173 0.4052 0.4959 -0.0619 -0.0846 0.1129  75  SER A N   
243  C CA  . SER A 75  ? 0.1801 0.3523 0.4461 -0.0546 -0.0696 0.1039  75  SER A CA  
244  C C   . SER A 75  ? 0.1718 0.3305 0.3992 -0.0591 -0.0743 0.0853  75  SER A C   
245  O O   . SER A 75  ? 0.2052 0.3618 0.4267 -0.0699 -0.0848 0.0736  75  SER A O   
246  C CB  . SER A 75  ? 0.2037 0.3692 0.4868 -0.0543 -0.0603 0.1033  75  SER A CB  
247  O OG  . SER A 75  ? 0.3242 0.4970 0.6331 -0.0470 -0.0504 0.1176  75  SER A OG  
248  N N   . PRO A 76  ? 0.1637 0.3129 0.3665 -0.0514 -0.0663 0.0811  76  PRO A N   
249  C CA  . PRO A 76  ? 0.1749 0.3121 0.3430 -0.0546 -0.0682 0.0634  76  PRO A CA  
250  C C   . PRO A 76  ? 0.2067 0.3258 0.3702 -0.0551 -0.0617 0.0496  76  PRO A C   
251  O O   . PRO A 76  ? 0.1669 0.2786 0.3443 -0.0488 -0.0501 0.0546  76  PRO A O   
252  C CB  . PRO A 76  ? 0.2004 0.3311 0.3517 -0.0443 -0.0581 0.0660  76  PRO A CB  
253  C CG  . PRO A 76  ? 0.2321 0.3759 0.4090 -0.0388 -0.0571 0.0852  76  PRO A CG  
254  C CD  . PRO A 76  ? 0.1897 0.3392 0.3983 -0.0394 -0.0551 0.0921  76  PRO A CD  
255  N N   . TYR A 77  ? 0.1693 0.3138 0.2562 -0.0435 -0.0780 0.0301  77  TYR A N   
256  C CA  . TYR A 77  ? 0.1627 0.2975 0.2445 -0.0459 -0.0723 0.0209  77  TYR A CA  
257  C C   . TYR A 77  ? 0.1586 0.2835 0.2188 -0.0453 -0.0687 0.0154  77  TYR A C   
258  O O   . TYR A 77  ? 0.2044 0.3312 0.2502 -0.0488 -0.0744 0.0137  77  TYR A O   
259  C CB  . TYR A 77  ? 0.1855 0.3240 0.2711 -0.0541 -0.0789 0.0151  77  TYR A CB  
260  C CG  . TYR A 77  ? 0.1970 0.3239 0.2739 -0.0573 -0.0741 0.0046  77  TYR A CG  
261  C CD1 . TYR A 77  ? 0.1796 0.3006 0.2671 -0.0554 -0.0665 0.0034  77  TYR A CD1 
262  C CD2 . TYR A 77  ? 0.2713 0.3931 0.3291 -0.0617 -0.0767 -0.0036 77  TYR A CD2 
263  C CE1 . TYR A 77  ? 0.2026 0.3126 0.2834 -0.0577 -0.0622 -0.0053 77  TYR A CE1 
264  C CE2 . TYR A 77  ? 0.2916 0.4025 0.3429 -0.0637 -0.0718 -0.0131 77  TYR A CE2 
265  C CZ  . TYR A 77  ? 0.2396 0.3446 0.3033 -0.0617 -0.0649 -0.0137 77  TYR A CZ  
266  O OH  . TYR A 77  ? 0.2619 0.3557 0.3206 -0.0633 -0.0601 -0.0223 77  TYR A OH  
267  N N   . TYR A 78  ? 0.1654 0.2805 0.2235 -0.0410 -0.0593 0.0131  78  TYR A N   
268  C CA  . TYR A 78  ? 0.1455 0.2513 0.1867 -0.0399 -0.0545 0.0083  78  TYR A CA  
269  C C   . TYR A 78  ? 0.2001 0.2978 0.2393 -0.0423 -0.0502 -0.0004 78  TYR A C   
270  O O   . TYR A 78  ? 0.1806 0.2771 0.2325 -0.0424 -0.0477 -0.0009 78  TYR A O   
271  C CB  . TYR A 78  ? 0.1847 0.2855 0.2259 -0.0329 -0.0475 0.0130  78  TYR A CB  
272  C CG  . TYR A 78  ? 0.1667 0.2726 0.2092 -0.0296 -0.0503 0.0214  78  TYR A CG  
273  C CD1 . TYR A 78  ? 0.1923 0.3047 0.2510 -0.0266 -0.0515 0.0285  78  TYR A CD1 
274  C CD2 . TYR A 78  ? 0.1868 0.2910 0.2153 -0.0292 -0.0512 0.0228  78  TYR A CD2 
275  C CE1 . TYR A 78  ? 0.1713 0.2875 0.2326 -0.0228 -0.0538 0.0365  78  TYR A CE1 
276  C CE2 . TYR A 78  ? 0.1762 0.2840 0.2065 -0.0261 -0.0537 0.0311  78  TYR A CE2 
277  C CZ  . TYR A 78  ? 0.1709 0.2842 0.2177 -0.0227 -0.0551 0.0378  78  TYR A CZ  
278  O OH  . TYR A 78  ? 0.1849 0.3009 0.2344 -0.0191 -0.0574 0.0463  78  TYR A OH  
279  N N   . GLU A 79  ? 0.2036 0.2956 0.2276 -0.0438 -0.0486 -0.0068 79  GLU A N   
280  C CA  . GLU A 79  ? 0.2050 0.2882 0.2264 -0.0450 -0.0437 -0.0149 79  GLU A CA  
281  C C   . GLU A 79  ? 0.1809 0.2579 0.1910 -0.0413 -0.0376 -0.0163 79  GLU A C   
282  O O   . GLU A 79  ? 0.2237 0.3021 0.2206 -0.0424 -0.0390 -0.0174 79  GLU A O   
283  C CB  . GLU A 79  ? 0.2680 0.3510 0.2826 -0.0518 -0.0485 -0.0233 79  GLU A CB  
284  C CG  . GLU A 79  ? 0.3330 0.4080 0.3529 -0.0538 -0.0450 -0.0307 79  GLU A CG  
285  C CD  . GLU A 79  ? 0.3122 0.3870 0.3277 -0.0612 -0.0509 -0.0391 79  GLU A CD  
286  O OE1 . GLU A 79  ? 0.2961 0.3781 0.3192 -0.0657 -0.0583 -0.0372 79  GLU A OE1 
287  O OE2 . GLU A 79  ? 0.4014 0.4690 0.4054 -0.0626 -0.0480 -0.0478 79  GLU A OE2 
288  N N   . ILE A 80  ? 0.1840 0.2548 0.1993 -0.0372 -0.0310 -0.0155 80  ILE A N   
289  C CA  . ILE A 80  ? 0.1893 0.2554 0.1970 -0.0334 -0.0256 -0.0153 80  ILE A CA  
290  C C   . ILE A 80  ? 0.1970 0.2554 0.2065 -0.0327 -0.0203 -0.0209 80  ILE A C   
291  O O   . ILE A 80  ? 0.2066 0.2621 0.2265 -0.0316 -0.0183 -0.0197 80  ILE A O   
292  C CB  . ILE A 80  ? 0.1758 0.2424 0.1878 -0.0285 -0.0235 -0.0074 80  ILE A CB  
293  C CG1 . ILE A 80  ? 0.2464 0.3202 0.2570 -0.0286 -0.0286 -0.0016 80  ILE A CG1 
294  C CG2 . ILE A 80  ? 0.1780 0.2392 0.1840 -0.0252 -0.0181 -0.0076 80  ILE A CG2 
295  C CD1 . ILE A 80  ? 0.2288 0.3027 0.2454 -0.0238 -0.0267 0.0057  80  ILE A CD1 
296  N N   . ALA A 81  ? 0.2047 0.2599 0.2047 -0.0334 -0.0178 -0.0266 81  ALA A N   
297  C CA  . ALA A 81  ? 0.1876 0.2357 0.1899 -0.0328 -0.0130 -0.0325 81  ALA A CA  
298  C C   . ALA A 81  ? 0.1863 0.2316 0.1871 -0.0283 -0.0077 -0.0303 81  ALA A C   
299  O O   . ALA A 81  ? 0.2193 0.2672 0.2116 -0.0276 -0.0069 -0.0292 81  ALA A O   
300  C CB  . ALA A 81  ? 0.2302 0.2764 0.2240 -0.0366 -0.0133 -0.0416 81  ALA A CB  
301  N N   . MET A 82  ? 0.1700 0.2102 0.1793 -0.0257 -0.0044 -0.0296 82  MET A N   
302  C CA  . MET A 82  ? 0.1769 0.2147 0.1865 -0.0219 0.0000  -0.0279 82  MET A CA  
303  C C   . MET A 82  ? 0.1931 0.2279 0.2002 -0.0220 0.0037  -0.0348 82  MET A C   
304  O O   . MET A 82  ? 0.1846 0.2146 0.1965 -0.0230 0.0048  -0.0400 82  MET A O   
305  C CB  . MET A 82  ? 0.1936 0.2274 0.2130 -0.0195 0.0014  -0.0242 82  MET A CB  
306  C CG  . MET A 82  ? 0.1762 0.2125 0.1984 -0.0189 -0.0008 -0.0178 82  MET A CG  
307  S SD  . MET A 82  ? 0.1903 0.2219 0.2229 -0.0173 0.0012  -0.0143 82  MET A SD  
308  C CE  . MET A 82  ? 0.1864 0.2216 0.2256 -0.0202 -0.0016 -0.0126 82  MET A CE  
309  N N   . ARG A 83  ? 0.1788 0.2162 0.1791 -0.0210 0.0061  -0.0350 83  ARG A N   
310  C CA  . ARG A 83  ? 0.2103 0.2462 0.2075 -0.0208 0.0106  -0.0417 83  ARG A CA  
311  C C   . ARG A 83  ? 0.1841 0.2214 0.1839 -0.0174 0.0148  -0.0388 83  ARG A C   
312  O O   . ARG A 83  ? 0.1792 0.2199 0.1772 -0.0166 0.0135  -0.0326 83  ARG A O   
313  C CB  . ARG A 83  ? 0.2289 0.2685 0.2131 -0.0244 0.0097  -0.0460 83  ARG A CB  
314  C CG  . ARG A 83  ? 0.2697 0.3092 0.2509 -0.0286 0.0045  -0.0492 83  ARG A CG  
315  C CD  . ARG A 83  ? 0.3195 0.3623 0.2859 -0.0324 0.0036  -0.0541 83  ARG A CD  
316  N NE  . ARG A 83  ? 0.3924 0.4370 0.3559 -0.0370 -0.0033 -0.0555 83  ARG A NE  
317  C CZ  . ARG A 83  ? 0.4529 0.4929 0.4186 -0.0400 -0.0047 -0.0628 83  ARG A CZ  
318  N NH1 . ARG A 83  ? 0.4349 0.4672 0.4062 -0.0385 0.0006  -0.0694 83  ARG A NH1 
319  N NH2 . ARG A 83  ? 0.4059 0.4489 0.3693 -0.0448 -0.0118 -0.0633 83  ARG A NH2 
320  N N   . GLN A 84  ? 0.1898 0.2242 0.1944 -0.0154 0.0198  -0.0435 84  GLN A N   
321  C CA  . GLN A 84  ? 0.1831 0.2201 0.1916 -0.0123 0.0240  -0.0413 84  GLN A CA  
322  C C   . GLN A 84  ? 0.1936 0.2355 0.1922 -0.0137 0.0275  -0.0444 84  GLN A C   
323  O O   . GLN A 84  ? 0.2247 0.2651 0.2174 -0.0152 0.0305  -0.0521 84  GLN A O   
324  C CB  . GLN A 84  ? 0.1783 0.2108 0.1988 -0.0089 0.0280  -0.0442 84  GLN A CB  
325  C CG  . GLN A 84  ? 0.1802 0.2168 0.2078 -0.0056 0.0317  -0.0409 84  GLN A CG  
326  C CD  . GLN A 84  ? 0.2055 0.2381 0.2473 -0.0016 0.0344  -0.0414 84  GLN A CD  
327  O OE1 . GLN A 84  ? 0.2203 0.2501 0.2693 -0.0003 0.0310  -0.0363 84  GLN A OE1 
328  N NE2 . GLN A 84  ? 0.2242 0.2566 0.2704 0.0006  0.0408  -0.0471 84  GLN A NE2 
329  N N   . VAL A 85  ? 0.1804 0.2278 0.1764 -0.0137 0.0274  -0.0385 85  VAL A N   
330  C CA  . VAL A 85  ? 0.1958 0.2484 0.1810 -0.0158 0.0301  -0.0393 85  VAL A CA  
331  C C   . VAL A 85  ? 0.1755 0.2331 0.1658 -0.0143 0.0329  -0.0339 85  VAL A C   
332  O O   . VAL A 85  ? 0.1782 0.2352 0.1777 -0.0125 0.0306  -0.0286 85  VAL A O   
333  C CB  . VAL A 85  ? 0.1904 0.2450 0.1642 -0.0193 0.0245  -0.0361 85  VAL A CB  
334  C CG1 . VAL A 85  ? 0.2146 0.2661 0.1831 -0.0218 0.0213  -0.0416 85  VAL A CG1 
335  C CG2 . VAL A 85  ? 0.2050 0.2594 0.1833 -0.0186 0.0195  -0.0279 85  VAL A CG2 
336  N N   . PRO A 86  ? 0.1884 0.2510 0.1721 -0.0155 0.0376  -0.0347 86  PRO A N   
337  C CA  . PRO A 86  ? 0.1766 0.2448 0.1649 -0.0152 0.0395  -0.0283 86  PRO A CA  
338  C C   . PRO A 86  ? 0.1825 0.2517 0.1643 -0.0179 0.0340  -0.0210 86  PRO A C   
339  O O   . PRO A 86  ? 0.2361 0.3047 0.2067 -0.0204 0.0309  -0.0209 86  PRO A O   
340  C CB  . PRO A 86  ? 0.1824 0.2557 0.1655 -0.0158 0.0475  -0.0321 86  PRO A CB  
341  C CG  . PRO A 86  ? 0.2557 0.3263 0.2242 -0.0180 0.0475  -0.0388 86  PRO A CG  
342  C CD  . PRO A 86  ? 0.1954 0.2590 0.1677 -0.0172 0.0422  -0.0419 86  PRO A CD  
343  N N   . HIS A 87  ? 0.1769 0.2477 0.1665 -0.0175 0.0327  -0.0148 87  HIS A N   
344  C CA  . HIS A 87  ? 0.1599 0.2306 0.1450 -0.0198 0.0284  -0.0080 87  HIS A CA  
345  C C   . HIS A 87  ? 0.1604 0.2355 0.1531 -0.0204 0.0308  -0.0033 87  HIS A C   
346  O O   . HIS A 87  ? 0.1827 0.2587 0.1871 -0.0184 0.0316  -0.0035 87  HIS A O   
347  C CB  . HIS A 87  ? 0.1762 0.2410 0.1636 -0.0189 0.0219  -0.0056 87  HIS A CB  
348  C CG  . HIS A 87  ? 0.1504 0.2140 0.1357 -0.0206 0.0182  0.0010  87  HIS A CG  
349  N ND1 . HIS A 87  ? 0.1891 0.2525 0.1653 -0.0224 0.0159  0.0038  87  HIS A ND1 
350  C CD2 . HIS A 87  ? 0.1647 0.2268 0.1559 -0.0208 0.0163  0.0053  87  HIS A CD2 
351  C CE1 . HIS A 87  ? 0.1842 0.2452 0.1615 -0.0233 0.0133  0.0095  87  HIS A CE1 
352  N NE2 . HIS A 87  ? 0.1564 0.2163 0.1422 -0.0226 0.0135  0.0100  87  HIS A NE2 
353  N N   . ARG A 88  ? 0.1637 0.2418 0.1507 -0.0233 0.0315  0.0014  88  ARG A N   
354  C CA  . ARG A 88  ? 0.1477 0.2300 0.1425 -0.0248 0.0335  0.0064  88  ARG A CA  
355  C C   . ARG A 88  ? 0.1892 0.2665 0.1864 -0.0261 0.0270  0.0119  88  ARG A C   
356  O O   . ARG A 88  ? 0.1929 0.2665 0.1819 -0.0276 0.0237  0.0150  88  ARG A O   
357  C CB  . ARG A 88  ? 0.2003 0.2885 0.1882 -0.0276 0.0388  0.0088  88  ARG A CB  
358  C CG  . ARG A 88  ? 0.2359 0.3310 0.2349 -0.0288 0.0435  0.0122  88  ARG A CG  
359  C CD  . ARG A 88  ? 0.2429 0.3442 0.2347 -0.0319 0.0496  0.0156  88  ARG A CD  
360  N NE  . ARG A 88  ? 0.3705 0.4742 0.3512 -0.0310 0.0553  0.0097  88  ARG A NE  
361  C CZ  . ARG A 88  ? 0.3540 0.4627 0.3393 -0.0287 0.0630  0.0040  88  ARG A CZ  
362  N NH1 . ARG A 88  ? 0.3482 0.4615 0.3507 -0.0269 0.0661  0.0044  88  ARG A NH1 
363  N NH2 . ARG A 88  ? 0.3986 0.5078 0.3710 -0.0283 0.0679  -0.0022 88  ARG A NH2 
364  N N   . PHE A 89  ? 0.1518 0.2288 0.1601 -0.0255 0.0250  0.0130  89  PHE A N   
365  C CA  . PHE A 89  ? 0.1560 0.2271 0.1653 -0.0270 0.0191  0.0169  89  PHE A CA  
366  C C   . PHE A 89  ? 0.1808 0.2538 0.1926 -0.0310 0.0194  0.0227  89  PHE A C   
367  O O   . PHE A 89  ? 0.1622 0.2290 0.1733 -0.0326 0.0148  0.0256  89  PHE A O   
368  C CB  . PHE A 89  ? 0.1482 0.2174 0.1663 -0.0252 0.0157  0.0157  89  PHE A CB  
369  C CG  . PHE A 89  ? 0.1426 0.2065 0.1573 -0.0220 0.0133  0.0120  89  PHE A CG  
370  C CD1 . PHE A 89  ? 0.1675 0.2239 0.1763 -0.0218 0.0089  0.0127  89  PHE A CD1 
371  C CD2 . PHE A 89  ? 0.1415 0.2078 0.1598 -0.0191 0.0162  0.0077  89  PHE A CD2 
372  C CE1 . PHE A 89  ? 0.1740 0.2263 0.1808 -0.0191 0.0073  0.0099  89  PHE A CE1 
373  C CE2 . PHE A 89  ? 0.1540 0.2153 0.1702 -0.0166 0.0142  0.0048  89  PHE A CE2 
374  C CZ  . PHE A 89  ? 0.1532 0.2080 0.1638 -0.0168 0.0098  0.0062  89  PHE A CZ  
375  N N   . HIS A 90  ? 0.1373 0.2185 0.1528 -0.0326 0.0250  0.0241  90  HIS A N   
376  C CA  . HIS A 90  ? 0.1566 0.2402 0.1755 -0.0369 0.0258  0.0302  90  HIS A CA  
377  C C   . HIS A 90  ? 0.1582 0.2504 0.1746 -0.0380 0.0337  0.0313  90  HIS A C   
378  O O   . HIS A 90  ? 0.1764 0.2741 0.1942 -0.0354 0.0389  0.0267  90  HIS A O   
379  C CB  . HIS A 90  ? 0.1686 0.2546 0.2018 -0.0384 0.0235  0.0317  90  HIS A CB  
380  C CG  . HIS A 90  ? 0.1563 0.2442 0.1949 -0.0436 0.0235  0.0380  90  HIS A CG  
381  N ND1 . HIS A 90  ? 0.1663 0.2643 0.2117 -0.0458 0.0300  0.0411  90  HIS A ND1 
382  C CD2 . HIS A 90  ? 0.1569 0.2377 0.1960 -0.0472 0.0182  0.0416  90  HIS A CD2 
383  C CE1 . HIS A 90  ? 0.1751 0.2725 0.2254 -0.0510 0.0284  0.0470  90  HIS A CE1 
384  N NE2 . HIS A 90  ? 0.1781 0.2644 0.2245 -0.0519 0.0211  0.0471  90  HIS A NE2 
385  N N   . ARG A 91  ? 0.1739 0.2667 0.1868 -0.0420 0.0349  0.0376  91  ARG A N   
386  C CA  . ARG A 91  ? 0.2004 0.3012 0.2085 -0.0436 0.0427  0.0397  91  ARG A CA  
387  C C   . ARG A 91  ? 0.1788 0.2899 0.1983 -0.0427 0.0499  0.0373  91  ARG A C   
388  O O   . ARG A 91  ? 0.2190 0.3363 0.2329 -0.0416 0.0576  0.0347  91  ARG A O   
389  C CB  . ARG A 91  ? 0.2167 0.3166 0.2236 -0.0486 0.0424  0.0485  91  ARG A CB  
390  C CG  . ARG A 91  ? 0.3066 0.4129 0.3034 -0.0506 0.0495  0.0520  91  ARG A CG  
391  C CD  . ARG A 91  ? 0.2877 0.3920 0.2838 -0.0557 0.0486  0.0620  91  ARG A CD  
392  N NE  . ARG A 91  ? 0.3760 0.4848 0.3606 -0.0571 0.0547  0.0655  91  ARG A NE  
393  C CZ  . ARG A 91  ? 0.3933 0.4974 0.3622 -0.0564 0.0522  0.0671  91  ARG A CZ  
394  N NH1 . ARG A 91  ? 0.4303 0.5279 0.3938 -0.0552 0.0451  0.0668  91  ARG A NH1 
395  N NH2 . ARG A 91  ? 0.4376 0.5438 0.3963 -0.0570 0.0568  0.0694  91  ARG A NH2 
396  N N   . LEU A 92  ? 0.1719 0.2855 0.2076 -0.0431 0.0478  0.0383  92  LEU A N   
397  C CA  . LEU A 92  ? 0.1837 0.3085 0.2341 -0.0423 0.0544  0.0376  92  LEU A CA  
398  C C   . LEU A 92  ? 0.1700 0.2954 0.2284 -0.0371 0.0536  0.0312  92  LEU A C   
399  O O   . LEU A 92  ? 0.2074 0.3418 0.2811 -0.0356 0.0579  0.0309  92  LEU A O   
400  C CB  . LEU A 92  ? 0.2121 0.3417 0.2777 -0.0470 0.0529  0.0444  92  LEU A CB  
401  C CG  . LEU A 92  ? 0.2187 0.3480 0.2787 -0.0525 0.0546  0.0518  92  LEU A CG  
402  C CD1 . LEU A 92  ? 0.2332 0.3668 0.3102 -0.0577 0.0525  0.0581  92  LEU A CD1 
403  C CD2 . LEU A 92  ? 0.2643 0.4015 0.3166 -0.0523 0.0653  0.0523  92  LEU A CD2 
404  N N   . PHE A 93  ? 0.1591 0.2755 0.2091 -0.0342 0.0482  0.0267  93  PHE A N   
405  C CA  . PHE A 93  ? 0.1677 0.2835 0.2238 -0.0292 0.0477  0.0209  93  PHE A CA  
406  C C   . PHE A 93  ? 0.1531 0.2708 0.2022 -0.0259 0.0556  0.0146  93  PHE A C   
407  O O   . PHE A 93  ? 0.2021 0.3185 0.2363 -0.0275 0.0585  0.0138  93  PHE A O   
408  C CB  . PHE A 93  ? 0.1600 0.2649 0.2085 -0.0280 0.0393  0.0190  93  PHE A CB  
409  C CG  . PHE A 93  ? 0.1373 0.2393 0.1943 -0.0292 0.0314  0.0221  93  PHE A CG  
410  C CD1 . PHE A 93  ? 0.1508 0.2572 0.2175 -0.0333 0.0297  0.0275  93  PHE A CD1 
411  C CD2 . PHE A 93  ? 0.1530 0.2475 0.2074 -0.0267 0.0256  0.0195  93  PHE A CD2 
412  C CE1 . PHE A 93  ? 0.1475 0.2503 0.2199 -0.0349 0.0217  0.0294  93  PHE A CE1 
413  C CE2 . PHE A 93  ? 0.1671 0.2584 0.2263 -0.0281 0.0183  0.0218  93  PHE A CE2 
414  C CZ  . PHE A 93  ? 0.1631 0.2584 0.2309 -0.0322 0.0161  0.0265  93  PHE A CZ  
415  N N   . PRO A 94  ? 0.1752 0.2952 0.2340 -0.0214 0.0587  0.0099  94  PRO A N   
416  C CA  . PRO A 94  ? 0.1735 0.2908 0.2235 -0.0181 0.0639  0.0020  94  PRO A CA  
417  C C   . PRO A 94  ? 0.2006 0.3073 0.2385 -0.0177 0.0568  -0.0009 94  PRO A C   
418  O O   . PRO A 94  ? 0.1840 0.2858 0.2227 -0.0188 0.0487  0.0028  94  PRO A O   
419  C CB  . PRO A 94  ? 0.2284 0.3494 0.2957 -0.0131 0.0675  -0.0011 94  PRO A CB  
420  C CG  . PRO A 94  ? 0.2388 0.3610 0.3204 -0.0136 0.0599  0.0048  94  PRO A CG  
421  C CD  . PRO A 94  ? 0.1731 0.2949 0.2493 -0.0192 0.0546  0.0113  94  PRO A CD  
422  N N   . PRO A 95  ? 0.1865 0.2893 0.2136 -0.0162 0.0596  -0.0076 95  PRO A N   
423  C CA  . PRO A 95  ? 0.1973 0.2910 0.2161 -0.0157 0.0528  -0.0102 95  PRO A CA  
424  C C   . PRO A 95  ? 0.1813 0.2713 0.2127 -0.0123 0.0488  -0.0109 95  PRO A C   
425  O O   . PRO A 95  ? 0.1980 0.2914 0.2428 -0.0092 0.0527  -0.0123 95  PRO A O   
426  C CB  . PRO A 95  ? 0.2550 0.3467 0.2619 -0.0152 0.0575  -0.0181 95  PRO A CB  
427  C CG  . PRO A 95  ? 0.3324 0.4318 0.3371 -0.0160 0.0667  -0.0190 95  PRO A CG  
428  C CD  . PRO A 95  ? 0.2272 0.3338 0.2488 -0.0152 0.0692  -0.0135 95  PRO A CD  
429  N N   . THR A 96  ? 0.1633 0.2466 0.1904 -0.0129 0.0413  -0.0093 96  THR A N   
430  C CA  . THR A 96  ? 0.1564 0.2350 0.1918 -0.0102 0.0368  -0.0092 96  THR A CA  
431  C C   . THR A 96  ? 0.1697 0.2415 0.1982 -0.0091 0.0358  -0.0146 96  THR A C   
432  O O   . THR A 96  ? 0.1702 0.2393 0.1866 -0.0114 0.0335  -0.0154 96  THR A O   
433  C CB  . THR A 96  ? 0.1435 0.2194 0.1783 -0.0121 0.0294  -0.0033 96  THR A CB  
434  O OG1 . THR A 96  ? 0.1650 0.2469 0.2065 -0.0141 0.0296  0.0016  96  THR A OG1 
435  C CG2 . THR A 96  ? 0.1560 0.2271 0.1970 -0.0097 0.0246  -0.0027 96  THR A CG2 
436  N N   . THR A 97  ? 0.1645 0.2335 0.2018 -0.0058 0.0369  -0.0178 97  THR A N   
437  C CA  . THR A 97  ? 0.1528 0.2146 0.1851 -0.0053 0.0351  -0.0222 97  THR A CA  
438  C C   . THR A 97  ? 0.1457 0.2031 0.1760 -0.0061 0.0279  -0.0178 97  THR A C   
439  O O   . THR A 97  ? 0.1496 0.2069 0.1874 -0.0049 0.0249  -0.0131 97  THR A O   
440  C CB  . THR A 97  ? 0.1608 0.2201 0.2043 -0.0015 0.0388  -0.0264 97  THR A CB  
441  O OG1 . THR A 97  ? 0.1882 0.2514 0.2332 -0.0004 0.0465  -0.0312 97  THR A OG1 
442  C CG2 . THR A 97  ? 0.1801 0.2316 0.2195 -0.0017 0.0372  -0.0312 97  THR A CG2 
443  N N   . VAL A 98  ? 0.1585 0.2126 0.1786 -0.0082 0.0253  -0.0191 98  VAL A N   
444  C CA  . VAL A 98  ? 0.1341 0.1843 0.1518 -0.0088 0.0196  -0.0154 98  VAL A CA  
445  C C   . VAL A 98  ? 0.1520 0.1979 0.1664 -0.0094 0.0185  -0.0193 98  VAL A C   
446  O O   . VAL A 98  ? 0.1502 0.1957 0.1623 -0.0099 0.0213  -0.0252 98  VAL A O   
447  C CB  . VAL A 98  ? 0.1473 0.1992 0.1570 -0.0112 0.0168  -0.0111 98  VAL A CB  
448  C CG1 . VAL A 98  ? 0.1568 0.2127 0.1701 -0.0117 0.0177  -0.0073 98  VAL A CG1 
449  C CG2 . VAL A 98  ? 0.1717 0.2254 0.1713 -0.0136 0.0177  -0.0135 98  VAL A CG2 
450  N N   . TRP A 99  ? 0.1457 0.1884 0.1597 -0.0095 0.0144  -0.0161 99  TRP A N   
451  C CA  . TRP A 99  ? 0.1504 0.1901 0.1624 -0.0106 0.0125  -0.0183 99  TRP A CA  
452  C C   . TRP A 99  ? 0.1536 0.1952 0.1583 -0.0125 0.0092  -0.0152 99  TRP A C   
453  O O   . TRP A 99  ? 0.1666 0.2077 0.1710 -0.0117 0.0074  -0.0103 99  TRP A O   
454  C CB  . TRP A 99  ? 0.1491 0.1845 0.1684 -0.0089 0.0113  -0.0162 99  TRP A CB  
455  C CG  . TRP A 99  ? 0.1575 0.1901 0.1854 -0.0070 0.0142  -0.0190 99  TRP A CG  
456  C CD1 . TRP A 99  ? 0.1781 0.2114 0.2082 -0.0063 0.0182  -0.0242 99  TRP A CD1 
457  C CD2 . TRP A 99  ? 0.1364 0.1646 0.1723 -0.0052 0.0137  -0.0167 99  TRP A CD2 
458  N NE1 . TRP A 99  ? 0.1772 0.2064 0.2174 -0.0039 0.0201  -0.0253 99  TRP A NE1 
459  C CE2 . TRP A 99  ? 0.1537 0.1797 0.1976 -0.0033 0.0170  -0.0203 99  TRP A CE2 
460  C CE3 . TRP A 99  ? 0.1617 0.1875 0.1987 -0.0050 0.0112  -0.0117 99  TRP A CE3 
461  C CZ2 . TRP A 99  ? 0.1781 0.1994 0.2315 -0.0013 0.0173  -0.0183 99  TRP A CZ2 
462  C CZ3 . TRP A 99  ? 0.1720 0.1936 0.2170 -0.0033 0.0116  -0.0096 99  TRP A CZ3 
463  C CH2 . TRP A 99  ? 0.1579 0.1772 0.2115 -0.0015 0.0143  -0.0125 99  TRP A CH2 
464  N N   . GLY A 100 ? 0.1524 0.1958 0.1510 -0.0148 0.0083  -0.0181 100 GLY A N   
465  C CA  . GLY A 100 ? 0.1742 0.2200 0.1669 -0.0163 0.0048  -0.0145 100 GLY A CA  
466  C C   . GLY A 100 ? 0.1559 0.2022 0.1482 -0.0181 0.0016  -0.0161 100 GLY A C   
467  O O   . GLY A 100 ? 0.1726 0.2185 0.1640 -0.0200 0.0019  -0.0217 100 GLY A O   
468  N N   . TYR A 101 ? 0.1513 0.1983 0.1450 -0.0178 -0.0015 -0.0113 101 TYR A N   
469  C CA  . TYR A 101 ? 0.1465 0.1963 0.1403 -0.0198 -0.0053 -0.0115 101 TYR A CA  
470  C C   . TYR A 101 ? 0.1792 0.2334 0.1636 -0.0227 -0.0074 -0.0128 101 TYR A C   
471  O O   . TYR A 101 ? 0.1781 0.2341 0.1568 -0.0224 -0.0073 -0.0092 101 TYR A O   
472  C CB  . TYR A 101 ? 0.1521 0.2025 0.1502 -0.0181 -0.0073 -0.0054 101 TYR A CB  
473  C CG  . TYR A 101 ? 0.1372 0.1837 0.1429 -0.0156 -0.0052 -0.0038 101 TYR A CG  
474  C CD1 . TYR A 101 ? 0.1553 0.2008 0.1678 -0.0164 -0.0050 -0.0059 101 TYR A CD1 
475  C CD2 . TYR A 101 ? 0.1502 0.1937 0.1555 -0.0129 -0.0035 -0.0002 101 TYR A CD2 
476  C CE1 . TYR A 101 ? 0.1381 0.1803 0.1565 -0.0143 -0.0028 -0.0036 101 TYR A CE1 
477  C CE2 . TYR A 101 ? 0.1364 0.1764 0.1463 -0.0109 -0.0015 0.0013  101 TYR A CE2 
478  C CZ  . TYR A 101 ? 0.1563 0.1958 0.1725 -0.0115 -0.0010 -0.0001 101 TYR A CZ  
479  O OH  . TYR A 101 ? 0.1541 0.1905 0.1740 -0.0097 0.0013  0.0022  101 TYR A OH  
480  N N   . ASP A 102 ? 0.1689 0.2244 0.1510 -0.0259 -0.0093 -0.0180 102 ASP A N   
481  C CA  . ASP A 102 ? 0.1781 0.2374 0.1488 -0.0292 -0.0112 -0.0206 102 ASP A CA  
482  C C   . ASP A 102 ? 0.1998 0.2586 0.1632 -0.0285 -0.0060 -0.0225 102 ASP A C   
483  O O   . ASP A 102 ? 0.2170 0.2796 0.1699 -0.0303 -0.0065 -0.0212 102 ASP A O   
484  C CB  . ASP A 102 ? 0.2154 0.2804 0.1830 -0.0304 -0.0169 -0.0142 102 ASP A CB  
485  C CG  . ASP A 102 ? 0.3026 0.3708 0.2749 -0.0331 -0.0227 -0.0151 102 ASP A CG  
486  O OD1 . ASP A 102 ? 0.3095 0.3748 0.2853 -0.0349 -0.0222 -0.0215 102 ASP A OD1 
487  O OD2 . ASP A 102 ? 0.3447 0.4181 0.3183 -0.0334 -0.0277 -0.0090 102 ASP A OD2 
488  N N   . GLY A 103 ? 0.1878 0.2424 0.1571 -0.0260 -0.0009 -0.0248 103 GLY A N   
489  C CA  . GLY A 103 ? 0.2068 0.2618 0.1721 -0.0252 0.0045  -0.0267 103 GLY A CA  
490  C C   . GLY A 103 ? 0.2059 0.2639 0.1678 -0.0245 0.0049  -0.0199 103 GLY A C   
491  O O   . GLY A 103 ? 0.2298 0.2905 0.1851 -0.0254 0.0085  -0.0207 103 GLY A O   
492  N N   . MET A 104 ? 0.1953 0.2526 0.1619 -0.0231 0.0018  -0.0133 104 MET A N   
493  C CA  . MET A 104 ? 0.2095 0.2681 0.1740 -0.0227 0.0022  -0.0070 104 MET A CA  
494  C C   . MET A 104 ? 0.1710 0.2257 0.1439 -0.0200 0.0018  -0.0031 104 MET A C   
495  O O   . MET A 104 ? 0.1700 0.2218 0.1489 -0.0185 0.0004  -0.0038 104 MET A O   
496  C CB  . MET A 104 ? 0.2257 0.2878 0.1824 -0.0248 -0.0019 -0.0027 104 MET A CB  
497  C CG  . MET A 104 ? 0.1930 0.2543 0.1550 -0.0238 -0.0069 0.0007  104 MET A CG  
498  S SD  . MET A 104 ? 0.2525 0.3190 0.2070 -0.0259 -0.0125 0.0068  104 MET A SD  
499  C CE  . MET A 104 ? 0.2882 0.3592 0.2324 -0.0302 -0.0141 0.0000  104 MET A CE  
500  N N   . LEU A 105 ? 0.1659 0.2203 0.1389 -0.0197 0.0033  0.0007  105 LEU A N   
501  C CA  . LEU A 105 ? 0.1610 0.2112 0.1402 -0.0178 0.0030  0.0035  105 LEU A CA  
502  C C   . LEU A 105 ? 0.1532 0.2028 0.1297 -0.0186 0.0016  0.0093  105 LEU A C   
503  O O   . LEU A 105 ? 0.1712 0.2235 0.1446 -0.0205 0.0035  0.0111  105 LEU A O   
504  C CB  . LEU A 105 ? 0.1599 0.2105 0.1440 -0.0172 0.0064  0.0012  105 LEU A CB  
505  C CG  . LEU A 105 ? 0.1395 0.1861 0.1294 -0.0157 0.0054  0.0032  105 LEU A CG  
506  C CD1 . LEU A 105 ? 0.1755 0.2235 0.1719 -0.0147 0.0079  0.0006  105 LEU A CD1 
507  C CD2 . LEU A 105 ? 0.1737 0.2191 0.1625 -0.0170 0.0045  0.0077  105 LEU A CD2 
508  N N   . PRO A 106 ? 0.1419 0.1874 0.1201 -0.0172 -0.0011 0.0126  106 PRO A N   
509  C CA  . PRO A 106 ? 0.1493 0.1926 0.1311 -0.0151 -0.0027 0.0116  106 PRO A CA  
510  C C   . PRO A 106 ? 0.1509 0.1985 0.1312 -0.0159 -0.0045 0.0099  106 PRO A C   
511  O O   . PRO A 106 ? 0.1582 0.2101 0.1327 -0.0181 -0.0052 0.0102  106 PRO A O   
512  C CB  . PRO A 106 ? 0.1658 0.2047 0.1486 -0.0136 -0.0043 0.0163  106 PRO A CB  
513  C CG  . PRO A 106 ? 0.1664 0.2030 0.1473 -0.0150 -0.0035 0.0188  106 PRO A CG  
514  C CD  . PRO A 106 ? 0.1616 0.2041 0.1390 -0.0176 -0.0020 0.0179  106 PRO A CD  
515  N N   . GLY A 107 ? 0.1491 0.1959 0.1342 -0.0146 -0.0053 0.0083  107 GLY A N   
516  C CA  . GLY A 107 ? 0.1566 0.2075 0.1420 -0.0159 -0.0079 0.0071  107 GLY A CA  
517  C C   . GLY A 107 ? 0.1630 0.2170 0.1467 -0.0161 -0.0115 0.0124  107 GLY A C   
518  O O   . GLY A 107 ? 0.1661 0.2174 0.1497 -0.0146 -0.0114 0.0170  107 GLY A O   
519  N N   . PRO A 108 ? 0.1671 0.2263 0.1493 -0.0182 -0.0151 0.0119  108 PRO A N   
520  C CA  . PRO A 108 ? 0.1744 0.2375 0.1555 -0.0184 -0.0194 0.0180  108 PRO A CA  
521  C C   . PRO A 108 ? 0.1542 0.2156 0.1451 -0.0147 -0.0200 0.0226  108 PRO A C   
522  O O   . PRO A 108 ? 0.1655 0.2253 0.1637 -0.0130 -0.0183 0.0206  108 PRO A O   
523  C CB  . PRO A 108 ? 0.1915 0.2610 0.1701 -0.0218 -0.0238 0.0155  108 PRO A CB  
524  C CG  . PRO A 108 ? 0.1739 0.2414 0.1575 -0.0222 -0.0217 0.0089  108 PRO A CG  
525  C CD  . PRO A 108 ? 0.1589 0.2205 0.1413 -0.0205 -0.0160 0.0061  108 PRO A CD  
526  N N   . THR A 109 ? 0.1568 0.2183 0.1479 -0.0133 -0.0220 0.0292  109 THR A N   
527  C CA  . THR A 109 ? 0.1493 0.2089 0.1502 -0.0093 -0.0219 0.0335  109 THR A CA  
528  C C   . THR A 109 ? 0.1412 0.2087 0.1497 -0.0094 -0.0264 0.0356  109 THR A C   
529  O O   . THR A 109 ? 0.1755 0.2495 0.1807 -0.0120 -0.0317 0.0385  109 THR A O   
530  C CB  . THR A 109 ? 0.1559 0.2122 0.1556 -0.0076 -0.0224 0.0399  109 THR A CB  
531  O OG1 . THR A 109 ? 0.1669 0.2158 0.1615 -0.0078 -0.0184 0.0378  109 THR A OG1 
532  C CG2 . THR A 109 ? 0.1632 0.2174 0.1739 -0.0029 -0.0222 0.0445  109 THR A CG2 
533  N N   . ILE A 110 ? 0.1470 0.2146 0.1657 -0.0071 -0.0245 0.0345  110 ILE A N   
534  C CA  . ILE A 110 ? 0.1396 0.2153 0.1686 -0.0070 -0.0285 0.0374  110 ILE A CA  
535  C C   . ILE A 110 ? 0.1617 0.2374 0.2003 -0.0021 -0.0284 0.0444  110 ILE A C   
536  O O   . ILE A 110 ? 0.1542 0.2224 0.1950 0.0019  -0.0229 0.0444  110 ILE A O   
537  C CB  . ILE A 110 ? 0.1380 0.2144 0.1741 -0.0074 -0.0258 0.0329  110 ILE A CB  
538  C CG1 . ILE A 110 ? 0.1557 0.2308 0.1833 -0.0118 -0.0257 0.0259  110 ILE A CG1 
539  C CG2 . ILE A 110 ? 0.1682 0.2538 0.2177 -0.0074 -0.0297 0.0365  110 ILE A CG2 
540  C CD1 . ILE A 110 ? 0.1827 0.2558 0.2165 -0.0119 -0.0220 0.0217  110 ILE A CD1 
541  N N   . LYS A 111 ? 0.1502 0.2339 0.1941 -0.0023 -0.0345 0.0505  111 LYS A N   
542  C CA  . LYS A 111 ? 0.1414 0.2258 0.1967 0.0028  -0.0348 0.0581  111 LYS A CA  
543  C C   . LYS A 111 ? 0.1604 0.2554 0.2315 0.0037  -0.0382 0.0614  111 LYS A C   
544  O O   . LYS A 111 ? 0.1799 0.2843 0.2510 -0.0007 -0.0453 0.0622  111 LYS A O   
545  C CB  . LYS A 111 ? 0.1594 0.2442 0.2094 0.0026  -0.0395 0.0649  111 LYS A CB  
546  C CG  . LYS A 111 ? 0.2023 0.2767 0.2394 0.0020  -0.0356 0.0629  111 LYS A CG  
547  C CD  . LYS A 111 ? 0.2655 0.3418 0.2952 0.0001  -0.0406 0.0695  111 LYS A CD  
548  C CE  . LYS A 111 ? 0.4208 0.4941 0.4603 0.0051  -0.0412 0.0782  111 LYS A CE  
549  N NZ  . LYS A 111 ? 0.4804 0.5498 0.5102 0.0034  -0.0429 0.0837  111 LYS A NZ  
550  N N   . VAL A 112 ? 0.1497 0.2435 0.2343 0.0092  -0.0331 0.0633  112 VAL A N   
551  C CA  . VAL A 112 ? 0.1333 0.2378 0.2361 0.0108  -0.0351 0.0673  112 VAL A CA  
552  C C   . VAL A 112 ? 0.1433 0.2466 0.2596 0.0181  -0.0321 0.0740  112 VAL A C   
553  O O   . VAL A 112 ? 0.1686 0.2609 0.2797 0.0219  -0.0271 0.0738  112 VAL A O   
554  C CB  . VAL A 112 ? 0.1596 0.2650 0.2681 0.0100  -0.0298 0.0618  112 VAL A CB  
555  C CG1 . VAL A 112 ? 0.1585 0.2639 0.2554 0.0032  -0.0323 0.0551  112 VAL A CG1 
556  C CG2 . VAL A 112 ? 0.1663 0.2607 0.2732 0.0150  -0.0196 0.0587  112 VAL A CG2 
557  N N   . GLN A 113 ? 0.1443 0.2592 0.2789 0.0201  -0.0354 0.0800  113 GLN A N   
558  C CA  . GLN A 113 ? 0.1452 0.2601 0.2966 0.0279  -0.0310 0.0859  113 GLN A CA  
559  C C   . GLN A 113 ? 0.1469 0.2611 0.3083 0.0313  -0.0215 0.0820  113 GLN A C   
560  O O   . GLN A 113 ? 0.1363 0.2555 0.2983 0.0271  -0.0211 0.0779  113 GLN A O   
561  C CB  . GLN A 113 ? 0.1724 0.3017 0.3412 0.0289  -0.0395 0.0956  113 GLN A CB  
562  C CG  . GLN A 113 ? 0.1814 0.3111 0.3393 0.0255  -0.0488 0.1002  113 GLN A CG  
563  C CD  . GLN A 113 ? 0.2727 0.3906 0.4235 0.0297  -0.0460 0.1032  113 GLN A CD  
564  O OE1 . GLN A 113 ? 0.3191 0.4313 0.4803 0.0363  -0.0410 0.1065  113 GLN A OE1 
565  N NE2 . GLN A 113 ? 0.3578 0.4692 0.4884 0.0250  -0.0481 0.1001  113 GLN A NE2 
566  N N   . LYS A 114 ? 0.1396 0.2474 0.3093 0.0389  -0.0136 0.0836  114 LYS A N   
567  C CA  . LYS A 114 ? 0.1421 0.2513 0.3234 0.0428  -0.0042 0.0814  114 LYS A CA  
568  C C   . LYS A 114 ? 0.1252 0.2520 0.3261 0.0410  -0.0085 0.0861  114 LYS A C   
569  O O   . LYS A 114 ? 0.1433 0.2766 0.3513 0.0401  -0.0157 0.0916  114 LYS A O   
570  C CB  . LYS A 114 ? 0.1239 0.2259 0.3146 0.0518  0.0040  0.0837  114 LYS A CB  
571  C CG  . LYS A 114 ? 0.1518 0.2564 0.3552 0.0564  0.0147  0.0819  114 LYS A CG  
572  C CD  . LYS A 114 ? 0.1794 0.2740 0.3876 0.0642  0.0232  0.0820  114 LYS A CD  
573  C CE  . LYS A 114 ? 0.2372 0.3317 0.4510 0.0670  0.0346  0.0782  114 LYS A CE  
574  N NZ  . LYS A 114 ? 0.3470 0.4321 0.5655 0.0744  0.0431  0.0775  114 LYS A NZ  
575  N N   . ASP A 115 ? 0.1249 0.2549 0.3279 0.0384  -0.0038 0.0818  115 ASP A N   
576  C CA  . ASP A 115 ? 0.1223 0.2640 0.3388 0.0349  -0.0060 0.0836  115 ASP A CA  
577  C C   . ASP A 115 ? 0.1463 0.2966 0.3596 0.0265  -0.0184 0.0840  115 ASP A C   
578  O O   . ASP A 115 ? 0.1843 0.3437 0.4079 0.0228  -0.0219 0.0853  115 ASP A O   
579  C CB  . ASP A 115 ? 0.1562 0.3017 0.3888 0.0398  -0.0041 0.0890  115 ASP A CB  
580  C CG  . ASP A 115 ? 0.1595 0.2980 0.3971 0.0471  0.0093  0.0873  115 ASP A CG  
581  O OD1 . ASP A 115 ? 0.2005 0.3317 0.4292 0.0481  0.0175  0.0820  115 ASP A OD1 
582  O OD2 . ASP A 115 ? 0.2751 0.4149 0.5250 0.0520  0.0118  0.0914  115 ASP A OD2 
583  N N   . GLU A 116 ? 0.1419 0.2893 0.3403 0.0230  -0.0250 0.0825  116 GLU A N   
584  C CA  . GLU A 116 ? 0.1671 0.3210 0.3589 0.0147  -0.0361 0.0815  116 GLU A CA  
585  C C   . GLU A 116 ? 0.1600 0.3112 0.3434 0.0089  -0.0341 0.0738  116 GLU A C   
586  O O   . GLU A 116 ? 0.1594 0.2980 0.3248 0.0085  -0.0295 0.0676  116 GLU A O   
587  C CB  . GLU A 116 ? 0.1940 0.3444 0.3709 0.0135  -0.0433 0.0831  116 GLU A CB  
588  C CG  . GLU A 116 ? 0.1929 0.3474 0.3573 0.0046  -0.0531 0.0798  116 GLU A CG  
589  C CD  . GLU A 116 ? 0.2525 0.4027 0.3999 0.0033  -0.0589 0.0814  116 GLU A CD  
590  O OE1 . GLU A 116 ? 0.1950 0.3335 0.3324 0.0073  -0.0531 0.0807  116 GLU A OE1 
591  O OE2 . GLU A 116 ? 0.2719 0.4269 0.4118 -0.0024 -0.0677 0.0816  116 GLU A OE2 
592  N N   . LYS A 117 ? 0.1371 0.2974 0.3314 0.0041  -0.0370 0.0734  117 LYS A N   
593  C CA  . LYS A 117 ? 0.1139 0.2714 0.3027 -0.0015 -0.0351 0.0667  117 LYS A CA  
594  C C   . LYS A 117 ? 0.1494 0.3034 0.3198 -0.0085 -0.0433 0.0613  117 LYS A C   
595  O O   . LYS A 117 ? 0.1803 0.3426 0.3514 -0.0122 -0.0536 0.0638  117 LYS A O   
596  C CB  . LYS A 117 ? 0.1667 0.3324 0.3719 -0.0045 -0.0351 0.0677  117 LYS A CB  
597  C CG  . LYS A 117 ? 0.1856 0.3491 0.3887 -0.0106 -0.0333 0.0619  117 LYS A CG  
598  C CD  . LYS A 117 ? 0.1783 0.3472 0.3968 -0.0127 -0.0310 0.0630  117 LYS A CD  
599  C CE  . LYS A 117 ? 0.2312 0.4089 0.4562 -0.0176 -0.0414 0.0644  117 LYS A CE  
600  N NZ  . LYS A 117 ? 0.2623 0.4466 0.5046 -0.0190 -0.0391 0.0668  117 LYS A NZ  
601  N N   . ILE A 118 ? 0.1374 0.2795 0.2911 -0.0101 -0.0387 0.0539  118 ILE A N   
602  C CA  . ILE A 118 ? 0.1286 0.2663 0.2649 -0.0162 -0.0443 0.0477  118 ILE A CA  
603  C C   . ILE A 118 ? 0.1568 0.2890 0.2905 -0.0203 -0.0407 0.0408  118 ILE A C   
604  O O   . ILE A 118 ? 0.1439 0.2731 0.2846 -0.0177 -0.0328 0.0411  118 ILE A O   
605  C CB  . ILE A 118 ? 0.1414 0.2694 0.2584 -0.0139 -0.0432 0.0460  118 ILE A CB  
606  C CG1 . ILE A 118 ? 0.1246 0.2404 0.2336 -0.0102 -0.0333 0.0422  118 ILE A CG1 
607  C CG2 . ILE A 118 ? 0.1605 0.2928 0.2814 -0.0094 -0.0463 0.0538  118 ILE A CG2 
608  C CD1 . ILE A 118 ? 0.1486 0.2552 0.2382 -0.0104 -0.0330 0.0388  118 ILE A CD1 
609  N N   . TYR A 119 ? 0.1305 0.2611 0.2539 -0.0268 -0.0464 0.0349  119 TYR A N   
610  C CA  . TYR A 119 ? 0.1212 0.2451 0.2411 -0.0308 -0.0436 0.0279  119 TYR A CA  
611  C C   . TYR A 119 ? 0.1455 0.2589 0.2449 -0.0315 -0.0425 0.0214  119 TYR A C   
612  O O   . TYR A 119 ? 0.1637 0.2783 0.2518 -0.0332 -0.0479 0.0204  119 TYR A O   
613  C CB  . TYR A 119 ? 0.1391 0.2702 0.2677 -0.0386 -0.0511 0.0255  119 TYR A CB  
614  C CG  . TYR A 119 ? 0.1680 0.3097 0.3196 -0.0382 -0.0510 0.0320  119 TYR A CG  
615  C CD1 . TYR A 119 ? 0.1799 0.3192 0.3423 -0.0381 -0.0439 0.0321  119 TYR A CD1 
616  C CD2 . TYR A 119 ? 0.1712 0.3254 0.3342 -0.0373 -0.0572 0.0389  119 TYR A CD2 
617  C CE1 . TYR A 119 ? 0.1578 0.3074 0.3419 -0.0374 -0.0424 0.0384  119 TYR A CE1 
618  C CE2 . TYR A 119 ? 0.1838 0.3466 0.3675 -0.0358 -0.0554 0.0446  119 TYR A CE2 
619  C CZ  . TYR A 119 ? 0.1318 0.2924 0.3257 -0.0360 -0.0478 0.0441  119 TYR A CZ  
620  O OH  . TYR A 119 ? 0.1925 0.3593 0.4031 -0.0339 -0.0444 0.0490  119 TYR A OH  
621  N N   . VAL A 120 ? 0.1329 0.2367 0.2278 -0.0303 -0.0354 0.0175  120 VAL A N   
622  C CA  . VAL A 120 ? 0.1321 0.2265 0.2101 -0.0306 -0.0337 0.0115  120 VAL A CA  
623  C C   . VAL A 120 ? 0.1701 0.2581 0.2486 -0.0340 -0.0313 0.0054  120 VAL A C   
624  O O   . VAL A 120 ? 0.1609 0.2454 0.2467 -0.0321 -0.0256 0.0069  120 VAL A O   
625  C CB  . VAL A 120 ? 0.1240 0.2119 0.1946 -0.0245 -0.0274 0.0137  120 VAL A CB  
626  C CG1 . VAL A 120 ? 0.1502 0.2306 0.2057 -0.0253 -0.0261 0.0081  120 VAL A CG1 
627  C CG2 . VAL A 120 ? 0.1865 0.2792 0.2580 -0.0209 -0.0291 0.0199  120 VAL A CG2 
628  N N   . ARG A 121 ? 0.1605 0.2463 0.2306 -0.0388 -0.0352 -0.0014 121 ARG A N   
629  C CA  . ARG A 121 ? 0.1411 0.2186 0.2102 -0.0412 -0.0323 -0.0080 121 ARG A CA  
630  C C   . ARG A 121 ? 0.1850 0.2541 0.2414 -0.0375 -0.0271 -0.0108 121 ARG A C   
631  O O   . ARG A 121 ? 0.1722 0.2404 0.2162 -0.0385 -0.0288 -0.0147 121 ARG A O   
632  C CB  . ARG A 121 ? 0.1779 0.2564 0.2445 -0.0483 -0.0387 -0.0150 121 ARG A CB  
633  C CG  . ARG A 121 ? 0.2003 0.2686 0.2661 -0.0506 -0.0355 -0.0226 121 ARG A CG  
634  C CD  . ARG A 121 ? 0.2075 0.2750 0.2711 -0.0580 -0.0414 -0.0308 121 ARG A CD  
635  N NE  . ARG A 121 ? 0.2306 0.3072 0.3056 -0.0630 -0.0485 -0.0281 121 ARG A NE  
636  C CZ  . ARG A 121 ? 0.2346 0.3100 0.3241 -0.0669 -0.0489 -0.0287 121 ARG A CZ  
637  N NH1 . ARG A 121 ? 0.2475 0.3127 0.3412 -0.0658 -0.0426 -0.0310 121 ARG A NH1 
638  N NH2 . ARG A 121 ? 0.1988 0.2839 0.3002 -0.0717 -0.0557 -0.0258 121 ARG A NH2 
639  N N   . TRP A 122 ? 0.1575 0.2212 0.2170 -0.0335 -0.0208 -0.0083 122 TRP A N   
640  C CA  . TRP A 122 ? 0.1516 0.2081 0.2017 -0.0302 -0.0162 -0.0103 122 TRP A CA  
641  C C   . TRP A 122 ? 0.1833 0.2328 0.2339 -0.0325 -0.0146 -0.0167 122 TRP A C   
642  O O   . TRP A 122 ? 0.1835 0.2301 0.2439 -0.0336 -0.0131 -0.0162 122 TRP A O   
643  C CB  . TRP A 122 ? 0.1737 0.2278 0.2264 -0.0252 -0.0111 -0.0046 122 TRP A CB  
644  C CG  . TRP A 122 ? 0.1429 0.2020 0.1971 -0.0221 -0.0111 0.0016  122 TRP A CG  
645  C CD1 . TRP A 122 ? 0.1485 0.2114 0.2131 -0.0208 -0.0096 0.0066  122 TRP A CD1 
646  C CD2 . TRP A 122 ? 0.1402 0.2002 0.1861 -0.0195 -0.0117 0.0035  122 TRP A CD2 
647  N NE1 . TRP A 122 ? 0.1540 0.2197 0.2171 -0.0172 -0.0092 0.0109  122 TRP A NE1 
648  C CE2 . TRP A 122 ? 0.1376 0.2012 0.1894 -0.0165 -0.0107 0.0093  122 TRP A CE2 
649  C CE3 . TRP A 122 ? 0.1607 0.2188 0.1953 -0.0194 -0.0125 0.0011  122 TRP A CE3 
650  C CZ2 . TRP A 122 ? 0.1394 0.2036 0.1865 -0.0135 -0.0110 0.0124  122 TRP A CZ2 
651  C CZ3 . TRP A 122 ? 0.1570 0.2164 0.1869 -0.0169 -0.0129 0.0049  122 TRP A CZ3 
652  C CH2 . TRP A 122 ? 0.1593 0.2210 0.1955 -0.0139 -0.0123 0.0103  122 TRP A CH2 
653  N N   . LYS A 123 ? 0.1574 0.2037 0.1980 -0.0330 -0.0144 -0.0226 123 LYS A N   
654  C CA  . LYS A 123 ? 0.1809 0.2201 0.2220 -0.0351 -0.0127 -0.0298 123 LYS A CA  
655  C C   . LYS A 123 ? 0.1770 0.2104 0.2145 -0.0308 -0.0073 -0.0305 123 LYS A C   
656  O O   . LYS A 123 ? 0.1857 0.2212 0.2148 -0.0285 -0.0063 -0.0295 123 LYS A O   
657  C CB  . LYS A 123 ? 0.1997 0.2401 0.2323 -0.0397 -0.0165 -0.0375 123 LYS A CB  
658  C CG  . LYS A 123 ? 0.1887 0.2354 0.2252 -0.0449 -0.0233 -0.0373 123 LYS A CG  
659  C CD  . LYS A 123 ? 0.2546 0.3011 0.2811 -0.0504 -0.0275 -0.0461 123 LYS A CD  
660  C CE  . LYS A 123 ? 0.3828 0.4322 0.3933 -0.0490 -0.0272 -0.0470 123 LYS A CE  
661  N NZ  . LYS A 123 ? 0.4804 0.5299 0.4785 -0.0545 -0.0310 -0.0557 123 LYS A NZ  
662  N N   . ASN A 124 ? 0.1793 0.2057 0.2243 -0.0301 -0.0041 -0.0319 124 ASN A N   
663  C CA  . ASN A 124 ? 0.1804 0.2014 0.2241 -0.0263 0.0004  -0.0331 124 ASN A CA  
664  C C   . ASN A 124 ? 0.1810 0.1980 0.2206 -0.0283 0.0014  -0.0426 124 ASN A C   
665  O O   . ASN A 124 ? 0.1916 0.2028 0.2371 -0.0309 0.0015  -0.0476 124 ASN A O   
666  C CB  . ASN A 124 ? 0.1812 0.1967 0.2356 -0.0244 0.0030  -0.0290 124 ASN A CB  
667  C CG  . ASN A 124 ? 0.1917 0.2023 0.2472 -0.0203 0.0069  -0.0290 124 ASN A CG  
668  O OD1 . ASN A 124 ? 0.1853 0.1945 0.2370 -0.0197 0.0087  -0.0349 124 ASN A OD1 
669  N ND2 . ASN A 124 ? 0.1659 0.1740 0.2278 -0.0177 0.0085  -0.0226 124 ASN A ND2 
670  N N   . LYS A 125 ? 0.1654 0.1851 0.1949 -0.0272 0.0027  -0.0452 125 LYS A N   
671  C CA  . LYS A 125 ? 0.1925 0.2089 0.2163 -0.0283 0.0052  -0.0544 125 LYS A CA  
672  C C   . LYS A 125 ? 0.2119 0.2267 0.2362 -0.0234 0.0108  -0.0540 125 LYS A C   
673  O O   . LYS A 125 ? 0.2258 0.2415 0.2427 -0.0230 0.0139  -0.0592 125 LYS A O   
674  C CB  . LYS A 125 ? 0.2171 0.2392 0.2275 -0.0319 0.0020  -0.0579 125 LYS A CB  
675  C CG  . LYS A 125 ? 0.2315 0.2555 0.2417 -0.0375 -0.0043 -0.0597 125 LYS A CG  
676  C CD  . LYS A 125 ? 0.2406 0.2564 0.2579 -0.0404 -0.0040 -0.0668 125 LYS A CD  
677  C CE  . LYS A 125 ? 0.3189 0.3373 0.3323 -0.0472 -0.0107 -0.0713 125 LYS A CE  
678  N NZ  . LYS A 125 ? 0.3646 0.3737 0.3798 -0.0510 -0.0101 -0.0817 125 LYS A NZ  
679  N N   . LEU A 126 ? 0.1886 0.2018 0.2219 -0.0197 0.0122  -0.0475 126 LEU A N   
680  C CA  . LEU A 126 ? 0.1975 0.2105 0.2341 -0.0151 0.0163  -0.0453 126 LEU A CA  
681  C C   . LEU A 126 ? 0.2140 0.2195 0.2599 -0.0130 0.0205  -0.0501 126 LEU A C   
682  O O   . LEU A 126 ? 0.2278 0.2268 0.2786 -0.0151 0.0200  -0.0540 126 LEU A O   
683  C CB  . LEU A 126 ? 0.1766 0.1916 0.2176 -0.0126 0.0147  -0.0358 126 LEU A CB  
684  C CG  . LEU A 126 ? 0.1563 0.1777 0.1892 -0.0136 0.0114  -0.0309 126 LEU A CG  
685  C CD1 . LEU A 126 ? 0.1994 0.2206 0.2365 -0.0116 0.0102  -0.0230 126 LEU A CD1 
686  C CD2 . LEU A 126 ? 0.1752 0.2016 0.2004 -0.0129 0.0128  -0.0313 126 LEU A CD2 
687  N N   . PRO A 127 ? 0.2205 0.2265 0.2699 -0.0089 0.0247  -0.0499 127 PRO A N   
688  C CA  . PRO A 127 ? 0.2267 0.2256 0.2875 -0.0058 0.0290  -0.0532 127 PRO A CA  
689  C C   . PRO A 127 ? 0.2071 0.2012 0.2796 -0.0041 0.0272  -0.0462 127 PRO A C   
690  O O   . PRO A 127 ? 0.2297 0.2267 0.3011 -0.0050 0.0232  -0.0388 127 PRO A O   
691  C CB  . PRO A 127 ? 0.2590 0.2626 0.3220 -0.0016 0.0333  -0.0524 127 PRO A CB  
692  C CG  . PRO A 127 ? 0.2762 0.2885 0.3270 -0.0035 0.0318  -0.0506 127 PRO A CG  
693  C CD  . PRO A 127 ? 0.2574 0.2711 0.3018 -0.0071 0.0258  -0.0466 127 PRO A CD  
694  N N   . GLU A 128 ? 0.2383 0.2249 0.3225 -0.0014 0.0306  -0.0486 128 GLU A N   
695  C CA  . GLU A 128 ? 0.2559 0.2370 0.3519 0.0002  0.0292  -0.0416 128 GLU A CA  
696  C C   . GLU A 128 ? 0.2744 0.2600 0.3758 0.0045  0.0283  -0.0318 128 GLU A C   
697  O O   . GLU A 128 ? 0.2776 0.2611 0.3841 0.0050  0.0258  -0.0237 128 GLU A O   
698  C CB  . GLU A 128 ? 0.3123 0.2823 0.4198 0.0014  0.0329  -0.0473 128 GLU A CB  
699  C CG  . GLU A 128 ? 0.3272 0.2914 0.4296 -0.0039 0.0326  -0.0571 128 GLU A CG  
700  C CD  . GLU A 128 ? 0.4964 0.4586 0.6002 -0.0084 0.0279  -0.0525 128 GLU A CD  
701  O OE1 . GLU A 128 ? 0.5219 0.4877 0.6165 -0.0135 0.0247  -0.0558 128 GLU A OE1 
702  O OE2 . GLU A 128 ? 0.4980 0.4557 0.6128 -0.0068 0.0275  -0.0450 128 GLU A OE2 
703  N N   . LYS A 129 ? 0.2326 0.2247 0.3326 0.0072  0.0302  -0.0320 129 LYS A N   
704  C CA  . LYS A 129 ? 0.2722 0.2693 0.3778 0.0108  0.0286  -0.0231 129 LYS A CA  
705  C C   . LYS A 129 ? 0.2083 0.2142 0.3023 0.0089  0.0254  -0.0197 129 LYS A C   
706  O O   . LYS A 129 ? 0.2299 0.2395 0.3142 0.0066  0.0264  -0.0249 129 LYS A O   
707  C CB  . LYS A 129 ? 0.3522 0.3505 0.4688 0.0156  0.0332  -0.0251 129 LYS A CB  
708  C CG  . LYS A 129 ? 0.4411 0.4452 0.5507 0.0151  0.0372  -0.0324 129 LYS A CG  
709  C CD  . LYS A 129 ? 0.5374 0.5383 0.6568 0.0189  0.0445  -0.0397 129 LYS A CD  
710  C CE  . LYS A 129 ? 0.5024 0.4923 0.6202 0.0169  0.0470  -0.0490 129 LYS A CE  
711  N NZ  . LYS A 129 ? 0.3568 0.3473 0.4578 0.0106  0.0436  -0.0528 129 LYS A NZ  
712  N N   . HIS A 130 ? 0.1870 0.1955 0.2814 0.0097  0.0215  -0.0108 130 HIS A N   
713  C CA  . HIS A 130 ? 0.1874 0.2027 0.2713 0.0079  0.0183  -0.0075 130 HIS A CA  
714  C C   . HIS A 130 ? 0.1853 0.2077 0.2707 0.0093  0.0197  -0.0082 130 HIS A C   
715  O O   . HIS A 130 ? 0.2097 0.2333 0.3065 0.0127  0.0221  -0.0078 130 HIS A O   
716  C CB  . HIS A 130 ? 0.2020 0.2172 0.2849 0.0081  0.0139  0.0014  130 HIS A CB  
717  C CG  . HIS A 130 ? 0.1455 0.1632 0.2156 0.0051  0.0112  0.0030  130 HIS A CG  
718  N ND1 . HIS A 130 ? 0.1767 0.2000 0.2400 0.0041  0.0100  0.0027  130 HIS A ND1 
719  C CD2 . HIS A 130 ? 0.1708 0.1859 0.2347 0.0031  0.0100  0.0045  130 HIS A CD2 
720  C CE1 . HIS A 130 ? 0.1759 0.1990 0.2291 0.0019  0.0081  0.0039  130 HIS A CE1 
721  N NE2 . HIS A 130 ? 0.1742 0.1929 0.2278 0.0014  0.0083  0.0049  130 HIS A NE2 
722  N N   . LEU A 131 ? 0.1574 0.1848 0.2322 0.0067  0.0183  -0.0084 131 LEU A N   
723  C CA  . LEU A 131 ? 0.1681 0.2028 0.2441 0.0072  0.0188  -0.0073 131 LEU A CA  
724  C C   . LEU A 131 ? 0.1588 0.1966 0.2407 0.0086  0.0147  0.0005  131 LEU A C   
725  O O   . LEU A 131 ? 0.1857 0.2296 0.2757 0.0101  0.0154  0.0021  131 LEU A O   
726  C CB  . LEU A 131 ? 0.2633 0.3014 0.3267 0.0037  0.0179  -0.0085 131 LEU A CB  
727  C CG  . LEU A 131 ? 0.3631 0.4020 0.4196 0.0019  0.0217  -0.0154 131 LEU A CG  
728  C CD1 . LEU A 131 ? 0.2774 0.3189 0.3218 -0.0014 0.0192  -0.0140 131 LEU A CD1 
729  C CD2 . LEU A 131 ? 0.2631 0.3065 0.3262 0.0038  0.0270  -0.0184 131 LEU A CD2 
730  N N   . LEU A 132 ? 0.1596 0.1941 0.2375 0.0079  0.0103  0.0055  132 LEU A N   
731  C CA  . LEU A 132 ? 0.1602 0.1976 0.2383 0.0079  0.0052  0.0125  132 LEU A CA  
732  C C   . LEU A 132 ? 0.1487 0.1828 0.2341 0.0103  0.0029  0.0182  132 LEU A C   
733  O O   . LEU A 132 ? 0.1753 0.2035 0.2638 0.0114  0.0052  0.0170  132 LEU A O   
734  C CB  . LEU A 132 ? 0.1552 0.1914 0.2189 0.0046  0.0020  0.0136  132 LEU A CB  
735  C CG  . LEU A 132 ? 0.1410 0.1795 0.1969 0.0021  0.0037  0.0092  132 LEU A CG  
736  C CD1 . LEU A 132 ? 0.1599 0.1961 0.2037 -0.0003 0.0004  0.0111  132 LEU A CD1 
737  C CD2 . LEU A 132 ? 0.1592 0.2046 0.2206 0.0019  0.0045  0.0088  132 LEU A CD2 
738  N N   . PRO A 133 ? 0.1616 0.1994 0.2503 0.0109  -0.0019 0.0249  133 PRO A N   
739  C CA  . PRO A 133 ? 0.1794 0.2145 0.2749 0.0133  -0.0046 0.0317  133 PRO A CA  
740  C C   . PRO A 133 ? 0.1455 0.1741 0.2300 0.0117  -0.0060 0.0344  133 PRO A C   
741  O O   . PRO A 133 ? 0.1728 0.2011 0.2436 0.0088  -0.0082 0.0346  133 PRO A O   
742  C CB  . PRO A 133 ? 0.1822 0.2243 0.2816 0.0133  -0.0106 0.0381  133 PRO A CB  
743  C CG  . PRO A 133 ? 0.1539 0.2027 0.2527 0.0114  -0.0097 0.0338  133 PRO A CG  
744  C CD  . PRO A 133 ? 0.1582 0.2029 0.2451 0.0090  -0.0056 0.0268  133 PRO A CD  
745  N N   . ILE A 134 ? 0.1636 0.1866 0.2549 0.0136  -0.0042 0.0366  134 ILE A N   
746  C CA  . ILE A 134 ? 0.1461 0.1633 0.2293 0.0122  -0.0044 0.0398  134 ILE A CA  
747  C C   . ILE A 134 ? 0.1460 0.1630 0.2306 0.0134  -0.0090 0.0498  134 ILE A C   
748  O O   . ILE A 134 ? 0.1596 0.1768 0.2580 0.0166  -0.0099 0.0541  134 ILE A O   
749  C CB  . ILE A 134 ? 0.1532 0.1640 0.2428 0.0126  0.0005  0.0358  134 ILE A CB  
750  C CG1 . ILE A 134 ? 0.1886 0.2000 0.2728 0.0104  0.0039  0.0266  134 ILE A CG1 
751  C CG2 . ILE A 134 ? 0.1985 0.2037 0.2842 0.0115  0.0004  0.0414  134 ILE A CG2 
752  C CD1 . ILE A 134 ? 0.1884 0.1936 0.2785 0.0100  0.0080  0.0215  134 ILE A CD1 
753  N N   . ASP A 135 ? 0.1772 0.1937 0.2473 0.0110  -0.0118 0.0536  135 ASP A N   
754  C CA  . ASP A 135 ? 0.1664 0.1817 0.2339 0.0114  -0.0159 0.0634  135 ASP A CA  
755  C C   . ASP A 135 ? 0.1677 0.1761 0.2375 0.0117  -0.0119 0.0661  135 ASP A C   
756  O O   . ASP A 135 ? 0.1730 0.1786 0.2336 0.0094  -0.0084 0.0630  135 ASP A O   
757  C CB  . ASP A 135 ? 0.1760 0.1928 0.2246 0.0083  -0.0194 0.0649  135 ASP A CB  
758  C CG  . ASP A 135 ? 0.1732 0.1891 0.2151 0.0081  -0.0239 0.0750  135 ASP A CG  
759  O OD1 . ASP A 135 ? 0.1902 0.2026 0.2390 0.0098  -0.0226 0.0811  135 ASP A OD1 
760  O OD2 . ASP A 135 ? 0.1943 0.2126 0.2228 0.0059  -0.0288 0.0768  135 ASP A OD2 
761  N N   . ARG A 136 ? 0.1744 0.1803 0.2572 0.0144  -0.0125 0.0723  136 ARG A N   
762  C CA  . ARG A 136 ? 0.1562 0.1549 0.2449 0.0146  -0.0086 0.0751  136 ARG A CA  
763  C C   . ARG A 136 ? 0.1966 0.1931 0.2751 0.0131  -0.0102 0.0850  136 ARG A C   
764  O O   . ARG A 136 ? 0.2203 0.2109 0.3047 0.0132  -0.0074 0.0896  136 ARG A O   
765  C CB  . ARG A 136 ? 0.1985 0.1938 0.3077 0.0184  -0.0075 0.0764  136 ARG A CB  
766  C CG  . ARG A 136 ? 0.1981 0.1943 0.3160 0.0195  -0.0040 0.0655  136 ARG A CG  
767  C CD  . ARG A 136 ? 0.2199 0.2089 0.3562 0.0225  0.0000  0.0639  136 ARG A CD  
768  N NE  . ARG A 136 ? 0.2426 0.2327 0.3849 0.0235  0.0038  0.0529  136 ARG A NE  
769  C CZ  . ARG A 136 ? 0.2537 0.2413 0.3907 0.0207  0.0077  0.0432  136 ARG A CZ  
770  N NH1 . ARG A 136 ? 0.2295 0.2139 0.3575 0.0169  0.0084  0.0430  136 ARG A NH1 
771  N NH2 . ARG A 136 ? 0.2624 0.2516 0.4029 0.0216  0.0110  0.0338  136 ARG A NH2 
772  N N   . THR A 137 ? 0.2027 0.2034 0.2652 0.0115  -0.0142 0.0879  137 THR A N   
773  C CA  . THR A 137 ? 0.2004 0.1992 0.2495 0.0097  -0.0149 0.0963  137 THR A CA  
774  C C   . THR A 137 ? 0.2094 0.2072 0.2433 0.0068  -0.0103 0.0913  137 THR A C   
775  O O   . THR A 137 ? 0.2280 0.2245 0.2491 0.0052  -0.0095 0.0972  137 THR A O   
776  C CB  . THR A 137 ? 0.2087 0.2120 0.2483 0.0096  -0.0226 0.1034  137 THR A CB  
777  O OG1 . THR A 137 ? 0.2092 0.2168 0.2362 0.0076  -0.0248 0.0964  137 THR A OG1 
778  C CG2 . THR A 137 ? 0.2356 0.2416 0.2927 0.0130  -0.0277 0.1090  137 THR A CG2 
779  N N   . LEU A 138 ? 0.1881 0.1867 0.2235 0.0061  -0.0070 0.0811  138 LEU A N   
780  C CA  . LEU A 138 ? 0.1992 0.1978 0.2227 0.0039  -0.0029 0.0760  138 LEU A CA  
781  C C   . LEU A 138 ? 0.2211 0.2163 0.2530 0.0031  0.0032  0.0749  138 LEU A C   
782  O O   . LEU A 138 ? 0.2322 0.2240 0.2777 0.0038  0.0041  0.0782  138 LEU A O   
783  C CB  . LEU A 138 ? 0.2016 0.2036 0.2214 0.0035  -0.0039 0.0667  138 LEU A CB  
784  C CG  . LEU A 138 ? 0.2374 0.2431 0.2512 0.0035  -0.0101 0.0672  138 LEU A CG  
785  C CD1 . LEU A 138 ? 0.1949 0.2029 0.2032 0.0024  -0.0100 0.0585  138 LEU A CD1 
786  C CD2 . LEU A 138 ? 0.2403 0.2456 0.2392 0.0024  -0.0135 0.0742  138 LEU A CD2 
787  N N   . HIS A 139 ? 0.2128 0.2088 0.2376 0.0014  0.0073  0.0706  139 HIS A N   
788  C CA  . HIS A 139 ? 0.2052 0.1992 0.2385 0.0001  0.0126  0.0702  139 HIS A CA  
789  C C   . HIS A 139 ? 0.1887 0.1817 0.2370 0.0001  0.0126  0.0634  139 HIS A C   
790  O O   . HIS A 139 ? 0.1971 0.1927 0.2449 0.0004  0.0113  0.0557  139 HIS A O   
791  C CB  . HIS A 139 ? 0.2461 0.2425 0.2699 -0.0013 0.0168  0.0671  139 HIS A CB  
792  C CG  . HIS A 139 ? 0.2368 0.2331 0.2459 -0.0015 0.0188  0.0734  139 HIS A CG  
793  N ND1 . HIS A 139 ? 0.4343 0.4323 0.4280 -0.0013 0.0194  0.0701  139 HIS A ND1 
794  C CD2 . HIS A 139 ? 0.3284 0.3227 0.3349 -0.0020 0.0206  0.0827  139 HIS A CD2 
795  C CE1 . HIS A 139 ? 0.3605 0.3574 0.3418 -0.0017 0.0218  0.0764  139 HIS A CE1 
796  N NE2 . HIS A 139 ? 0.4217 0.4168 0.4100 -0.0022 0.0225  0.0845  139 HIS A NE2 
797  N N   . GLU A 140 ? 0.1918 0.1804 0.2532 -0.0004 0.0142  0.0663  140 GLU A N   
798  C CA  . GLU A 140 ? 0.2138 0.2001 0.2888 -0.0012 0.0151  0.0593  140 GLU A CA  
799  C C   . GLU A 140 ? 0.1805 0.1666 0.2609 0.0012  0.0122  0.0543  140 GLU A C   
800  O O   . GLU A 140 ? 0.2141 0.1999 0.3000 0.0006  0.0129  0.0458  140 GLU A O   
801  C CB  . GLU A 140 ? 0.2391 0.2286 0.3126 -0.0038 0.0174  0.0522  140 GLU A CB  
802  C CG  . GLU A 140 ? 0.3030 0.2891 0.3899 -0.0063 0.0190  0.0481  140 GLU A CG  
803  C CD  . GLU A 140 ? 0.2647 0.2467 0.3597 -0.0084 0.0217  0.0556  140 GLU A CD  
804  O OE1 . GLU A 140 ? 0.3895 0.3662 0.4974 -0.0101 0.0222  0.0537  140 GLU A OE1 
805  O OE2 . GLU A 140 ? 0.3596 0.3436 0.4477 -0.0086 0.0238  0.0630  140 GLU A OE2 
806  N N   . THR A 141 ? 0.2026 0.1892 0.2817 0.0039  0.0090  0.0595  141 THR A N   
807  C CA  . THR A 141 ? 0.1852 0.1732 0.2707 0.0065  0.0068  0.0554  141 THR A CA  
808  C C   . THR A 141 ? 0.2205 0.2041 0.3195 0.0095  0.0057  0.0612  141 THR A C   
809  O O   . THR A 141 ? 0.2312 0.2168 0.3369 0.0123  0.0040  0.0592  141 THR A O   
810  C CB  . THR A 141 ? 0.1911 0.1855 0.2654 0.0073  0.0032  0.0550  141 THR A CB  
811  O OG1 . THR A 141 ? 0.2086 0.2038 0.2745 0.0075  0.0002  0.0643  141 THR A OG1 
812  C CG2 . THR A 141 ? 0.2032 0.2010 0.2667 0.0050  0.0045  0.0480  141 THR A CG2 
813  N N   . ALA A 142 ? 0.2088 0.1869 0.3133 0.0091  0.0069  0.0686  142 ALA A N   
814  C CA  . ALA A 142 ? 0.2287 0.2021 0.3470 0.0123  0.0056  0.0753  142 ALA A CA  
815  C C   . ALA A 142 ? 0.2937 0.2624 0.4278 0.0143  0.0080  0.0673  142 ALA A C   
816  O O   . ALA A 142 ? 0.2814 0.2490 0.4270 0.0184  0.0067  0.0701  142 ALA A O   
817  C CB  . ALA A 142 ? 0.2565 0.2240 0.3776 0.0109  0.0069  0.0853  142 ALA A CB  
818  N N   . GLY A 143 ? 0.2879 0.2540 0.4230 0.0116  0.0115  0.0575  143 GLY A N   
819  C CA  . GLY A 143 ? 0.3082 0.2688 0.4558 0.0129  0.0143  0.0488  143 GLY A CA  
820  C C   . GLY A 143 ? 0.2978 0.2594 0.4395 0.0092  0.0165  0.0369  143 GLY A C   
821  O O   . GLY A 143 ? 0.2467 0.2149 0.3754 0.0067  0.0155  0.0353  143 GLY A O   
822  N N   . PRO A 144 ? 0.3314 0.2861 0.4825 0.0088  0.0194  0.0283  144 PRO A N   
823  C CA  . PRO A 144 ? 0.2829 0.2393 0.4274 0.0052  0.0207  0.0167  144 PRO A CA  
824  C C   . PRO A 144 ? 0.3026 0.2586 0.4432 -0.0002 0.0203  0.0176  144 PRO A C   
825  O O   . PRO A 144 ? 0.2883 0.2391 0.4357 -0.0015 0.0206  0.0246  144 PRO A O   
826  C CB  . PRO A 144 ? 0.3608 0.3084 0.5168 0.0063  0.0239  0.0078  144 PRO A CB  
827  C CG  . PRO A 144 ? 0.4378 0.3816 0.6065 0.0121  0.0246  0.0145  144 PRO A CG  
828  C CD  . PRO A 144 ? 0.3472 0.2923 0.5149 0.0119  0.0216  0.0281  144 PRO A CD  
829  N N   . PRO A 145 ? 0.2397 0.2015 0.3704 -0.0035 0.0196  0.0110  145 PRO A N   
830  C CA  . PRO A 145 ? 0.2131 0.1808 0.3349 -0.0028 0.0193  0.0029  145 PRO A CA  
831  C C   . PRO A 145 ? 0.2296 0.2058 0.3417 -0.0003 0.0174  0.0081  145 PRO A C   
832  O O   . PRO A 145 ? 0.2209 0.2007 0.3269 -0.0012 0.0160  0.0150  145 PRO A O   
833  C CB  . PRO A 145 ? 0.2545 0.2250 0.3703 -0.0081 0.0183  -0.0029 145 PRO A CB  
834  C CG  . PRO A 145 ? 0.2586 0.2287 0.3772 -0.0108 0.0178  0.0045  145 PRO A CG  
835  C CD  . PRO A 145 ? 0.2790 0.2420 0.4078 -0.0084 0.0191  0.0125  145 PRO A CD  
836  N N   . ASP A 146 ? 0.2083 0.1878 0.3190 0.0026  0.0178  0.0045  146 ASP A N   
837  C CA  . ASP A 146 ? 0.1749 0.1622 0.2767 0.0042  0.0157  0.0084  146 ASP A CA  
838  C C   . ASP A 146 ? 0.1936 0.1869 0.2830 0.0013  0.0147  0.0044  146 ASP A C   
839  O O   . ASP A 146 ? 0.1992 0.1973 0.2802 0.0014  0.0127  0.0088  146 ASP A O   
840  C CB  . ASP A 146 ? 0.1930 0.1824 0.2998 0.0080  0.0166  0.0062  146 ASP A CB  
841  C CG  . ASP A 146 ? 0.2274 0.2138 0.3460 0.0119  0.0162  0.0134  146 ASP A CG  
842  O OD1 . ASP A 146 ? 0.2421 0.2243 0.3638 0.0116  0.0150  0.0206  146 ASP A OD1 
843  O OD2 . ASP A 146 ? 0.2500 0.2387 0.3754 0.0154  0.0172  0.0125  146 ASP A OD2 
844  N N   . VAL A 147 ? 0.1689 0.1618 0.2566 -0.0012 0.0158  -0.0039 147 VAL A N   
845  C CA  . VAL A 147 ? 0.1688 0.1678 0.2455 -0.0035 0.0146  -0.0075 147 VAL A CA  
846  C C   . VAL A 147 ? 0.1723 0.1713 0.2475 -0.0071 0.0134  -0.0067 147 VAL A C   
847  O O   . VAL A 147 ? 0.2202 0.2168 0.2981 -0.0102 0.0135  -0.0122 147 VAL A O   
848  C CB  . VAL A 147 ? 0.1645 0.1648 0.2387 -0.0039 0.0162  -0.0162 147 VAL A CB  
849  C CG1 . VAL A 147 ? 0.1827 0.1895 0.2455 -0.0063 0.0144  -0.0180 147 VAL A CG1 
850  C CG2 . VAL A 147 ? 0.1784 0.1797 0.2569 0.0001  0.0183  -0.0161 147 VAL A CG2 
851  N N   . ARG A 148 ? 0.1545 0.1562 0.2255 -0.0069 0.0124  0.0000  148 ARG A N   
852  C CA  . ARG A 148 ? 0.1421 0.1453 0.2127 -0.0096 0.0119  0.0021  148 ARG A CA  
853  C C   . ARG A 148 ? 0.1410 0.1506 0.2019 -0.0096 0.0107  0.0026  148 ARG A C   
854  O O   . ARG A 148 ? 0.1608 0.1721 0.2153 -0.0073 0.0103  0.0051  148 ARG A O   
855  C CB  . ARG A 148 ? 0.1661 0.1665 0.2407 -0.0089 0.0131  0.0102  148 ARG A CB  
856  C CG  . ARG A 148 ? 0.1617 0.1550 0.2468 -0.0082 0.0143  0.0117  148 ARG A CG  
857  C CD  . ARG A 148 ? 0.1763 0.1675 0.2632 -0.0073 0.0152  0.0213  148 ARG A CD  
858  N NE  . ARG A 148 ? 0.1576 0.1506 0.2375 -0.0040 0.0140  0.0260  148 ARG A NE  
859  C CZ  . ARG A 148 ? 0.1683 0.1653 0.2377 -0.0035 0.0136  0.0300  148 ARG A CZ  
860  N NH1 . ARG A 148 ? 0.1688 0.1685 0.2343 -0.0054 0.0151  0.0305  148 ARG A NH1 
861  N NH2 . ARG A 148 ? 0.1635 0.1617 0.2268 -0.0011 0.0117  0.0334  148 ARG A NH2 
862  N N   . THR A 149 ? 0.1501 0.1630 0.2106 -0.0123 0.0097  0.0004  149 THR A N   
863  C CA  . THR A 149 ? 0.1497 0.1682 0.2024 -0.0121 0.0084  0.0006  149 THR A CA  
864  C C   . THR A 149 ? 0.1397 0.1615 0.1955 -0.0135 0.0085  0.0037  149 THR A C   
865  O O   . THR A 149 ? 0.1439 0.1653 0.2080 -0.0162 0.0085  0.0033  149 THR A O   
866  C CB  . THR A 149 ? 0.1442 0.1654 0.1930 -0.0137 0.0064  -0.0057 149 THR A CB  
867  O OG1 . THR A 149 ? 0.1743 0.1948 0.2286 -0.0172 0.0053  -0.0102 149 THR A OG1 
868  C CG2 . THR A 149 ? 0.1520 0.1715 0.1977 -0.0120 0.0073  -0.0088 149 THR A CG2 
869  N N   . VAL A 150 ? 0.1419 0.1671 0.1919 -0.0118 0.0087  0.0066  150 VAL A N   
870  C CA  . VAL A 150 ? 0.1286 0.1586 0.1822 -0.0126 0.0090  0.0090  150 VAL A CA  
871  C C   . VAL A 150 ? 0.1400 0.1728 0.1861 -0.0104 0.0085  0.0097  150 VAL A C   
872  O O   . VAL A 150 ? 0.1426 0.1725 0.1809 -0.0082 0.0092  0.0103  150 VAL A O   
873  C CB  . VAL A 150 ? 0.1378 0.1666 0.1964 -0.0120 0.0128  0.0146  150 VAL A CB  
874  C CG1 . VAL A 150 ? 0.1814 0.2075 0.2310 -0.0086 0.0154  0.0183  150 VAL A CG1 
875  C CG2 . VAL A 150 ? 0.1551 0.1899 0.2215 -0.0132 0.0136  0.0168  150 VAL A CG2 
876  N N   . VAL A 151 ? 0.1365 0.1747 0.1855 -0.0112 0.0068  0.0098  151 VAL A N   
877  C CA  . VAL A 151 ? 0.1391 0.1793 0.1819 -0.0091 0.0060  0.0104  151 VAL A CA  
878  C C   . VAL A 151 ? 0.1380 0.1800 0.1838 -0.0066 0.0092  0.0148  151 VAL A C   
879  O O   . VAL A 151 ? 0.1392 0.1859 0.1946 -0.0075 0.0097  0.0168  151 VAL A O   
880  C CB  . VAL A 151 ? 0.1500 0.1953 0.1935 -0.0113 0.0015  0.0081  151 VAL A CB  
881  C CG1 . VAL A 151 ? 0.1690 0.2153 0.2063 -0.0090 0.0006  0.0098  151 VAL A CG1 
882  C CG2 . VAL A 151 ? 0.1741 0.2178 0.2145 -0.0141 -0.0007 0.0029  151 VAL A CG2 
883  N N   . HIS A 152 ? 0.1356 0.1737 0.1735 -0.0035 0.0115  0.0159  152 HIS A N   
884  C CA  . HIS A 152 ? 0.1386 0.1770 0.1771 -0.0004 0.0153  0.0189  152 HIS A CA  
885  C C   . HIS A 152 ? 0.1365 0.1760 0.1730 0.0013  0.0134  0.0188  152 HIS A C   
886  O O   . HIS A 152 ? 0.1470 0.1832 0.1756 0.0010  0.0111  0.0169  152 HIS A O   
887  C CB  . HIS A 152 ? 0.1617 0.1934 0.1910 0.0016  0.0192  0.0197  152 HIS A CB  
888  C CG  . HIS A 152 ? 0.1742 0.2042 0.2005 0.0050  0.0238  0.0211  152 HIS A CG  
889  N ND1 . HIS A 152 ? 0.1704 0.2046 0.2052 0.0066  0.0281  0.0239  152 HIS A ND1 
890  C CD2 . HIS A 152 ? 0.1669 0.1908 0.1829 0.0072  0.0251  0.0199  152 HIS A CD2 
891  C CE1 . HIS A 152 ? 0.1861 0.2168 0.2157 0.0102  0.0325  0.0240  152 HIS A CE1 
892  N NE2 . HIS A 152 ? 0.2153 0.2391 0.2330 0.0104  0.0306  0.0213  152 HIS A NE2 
893  N N   . LEU A 153 ? 0.1263 0.1709 0.1713 0.0029  0.0144  0.0214  153 LEU A N   
894  C CA  . LEU A 153 ? 0.1229 0.1679 0.1676 0.0054  0.0133  0.0226  153 LEU A CA  
895  C C   . LEU A 153 ? 0.1221 0.1610 0.1621 0.0095  0.0191  0.0231  153 LEU A C   
896  O O   . LEU A 153 ? 0.1420 0.1827 0.1881 0.0119  0.0242  0.0251  153 LEU A O   
897  C CB  . LEU A 153 ? 0.1193 0.1734 0.1767 0.0052  0.0107  0.0255  153 LEU A CB  
898  C CG  . LEU A 153 ? 0.1041 0.1590 0.1634 0.0085  0.0097  0.0282  153 LEU A CG  
899  C CD1 . LEU A 153 ? 0.1525 0.2028 0.2010 0.0073  0.0058  0.0265  153 LEU A CD1 
900  C CD2 . LEU A 153 ? 0.1482 0.2136 0.2214 0.0080  0.0060  0.0319  153 LEU A CD2 
901  N N   . HIS A 154 ? 0.1409 0.1723 0.1696 0.0099  0.0187  0.0209  154 HIS A N   
902  C CA  . HIS A 154 ? 0.1383 0.1620 0.1592 0.0127  0.0237  0.0198  154 HIS A CA  
903  C C   . HIS A 154 ? 0.1540 0.1769 0.1798 0.0169  0.0266  0.0213  154 HIS A C   
904  O O   . HIS A 154 ? 0.1688 0.1914 0.1963 0.0175  0.0233  0.0221  154 HIS A O   
905  C CB  . HIS A 154 ? 0.1678 0.1846 0.1768 0.0109  0.0208  0.0171  154 HIS A CB  
906  C CG  . HIS A 154 ? 0.1666 0.1748 0.1652 0.0125  0.0244  0.0151  154 HIS A CG  
907  N ND1 . HIS A 154 ? 0.1797 0.1841 0.1689 0.0107  0.0242  0.0136  154 HIS A ND1 
908  C CD2 . HIS A 154 ? 0.1732 0.1756 0.1690 0.0159  0.0285  0.0141  154 HIS A CD2 
909  C CE1 . HIS A 154 ? 0.1857 0.1824 0.1653 0.0122  0.0273  0.0116  154 HIS A CE1 
910  N NE2 . HIS A 154 ? 0.2049 0.1997 0.1882 0.0154  0.0304  0.0114  154 HIS A NE2 
911  N N   . GLY A 155 ? 0.1450 0.1673 0.1732 0.0200  0.0333  0.0219  155 GLY A N   
912  C CA  . GLY A 155 ? 0.1604 0.1824 0.1958 0.0249  0.0378  0.0233  155 GLY A CA  
913  C C   . GLY A 155 ? 0.1577 0.1909 0.2107 0.0263  0.0385  0.0277  155 GLY A C   
914  O O   . GLY A 155 ? 0.1759 0.2103 0.2377 0.0310  0.0426  0.0296  155 GLY A O   
915  N N   . ALA A 156 ? 0.1390 0.1804 0.1983 0.0224  0.0347  0.0293  156 ALA A N   
916  C CA  . ALA A 156 ? 0.1329 0.1857 0.2098 0.0227  0.0337  0.0335  156 ALA A CA  
917  C C   . ALA A 156 ? 0.1589 0.2154 0.2449 0.0258  0.0422  0.0357  156 ALA A C   
918  O O   . ALA A 156 ? 0.1686 0.2226 0.2488 0.0247  0.0469  0.0347  156 ALA A O   
919  C CB  . ALA A 156 ? 0.1564 0.2158 0.2369 0.0170  0.0272  0.0337  156 ALA A CB  
920  N N   . ASN A 157 ? 0.1422 0.2057 0.2436 0.0295  0.0441  0.0394  157 ASN A N   
921  C CA  . ASN A 157 ? 0.1474 0.2191 0.2633 0.0314  0.0509  0.0428  157 ASN A CA  
922  C C   . ASN A 157 ? 0.1616 0.2447 0.2900 0.0259  0.0443  0.0457  157 ASN A C   
923  O O   . ASN A 157 ? 0.1551 0.2467 0.2960 0.0253  0.0379  0.0488  157 ASN A O   
924  C CB  . ASN A 157 ? 0.1551 0.2309 0.2852 0.0378  0.0551  0.0460  157 ASN A CB  
925  C CG  . ASN A 157 ? 0.1546 0.2412 0.3029 0.0397  0.0621  0.0503  157 ASN A CG  
926  O OD1 . ASN A 157 ? 0.1736 0.2605 0.3187 0.0375  0.0675  0.0499  157 ASN A OD1 
927  N ND2 . ASN A 157 ? 0.1620 0.2583 0.3305 0.0436  0.0622  0.0551  157 ASN A ND2 
928  N N   . VAL A 158 ? 0.1364 0.2192 0.2612 0.0216  0.0453  0.0448  158 VAL A N   
929  C CA  . VAL A 158 ? 0.1569 0.2476 0.2910 0.0155  0.0385  0.0461  158 VAL A CA  
930  C C   . VAL A 158 ? 0.1526 0.2450 0.2908 0.0130  0.0441  0.0476  158 VAL A C   
931  O O   . VAL A 158 ? 0.1596 0.2442 0.2859 0.0144  0.0507  0.0464  158 VAL A O   
932  C CB  . VAL A 158 ? 0.1439 0.2292 0.2652 0.0112  0.0297  0.0419  158 VAL A CB  
933  C CG1 . VAL A 158 ? 0.1480 0.2228 0.2530 0.0096  0.0323  0.0383  158 VAL A CG1 
934  C CG2 . VAL A 158 ? 0.1558 0.2497 0.2877 0.0054  0.0217  0.0425  158 VAL A CG2 
935  N N   . ALA A 159 ? 0.1381 0.2409 0.2933 0.0089  0.0410  0.0506  159 ALA A N   
936  C CA  . ALA A 159 ? 0.1332 0.2377 0.2941 0.0052  0.0450  0.0527  159 ALA A CA  
937  C C   . ALA A 159 ? 0.1394 0.2330 0.2835 0.0020  0.0434  0.0489  159 ALA A C   
938  O O   . ALA A 159 ? 0.1555 0.2439 0.2895 0.0002  0.0363  0.0447  159 ALA A O   
939  C CB  . ALA A 159 ? 0.1351 0.2514 0.3161 -0.0001 0.0390  0.0553  159 ALA A CB  
940  N N   . TRP A 160 ? 0.1538 0.2443 0.2957 0.0014  0.0504  0.0511  160 TRP A N   
941  C CA  . TRP A 160 ? 0.1375 0.2169 0.2623 0.0001  0.0505  0.0487  160 TRP A CA  
942  C C   . TRP A 160 ? 0.1515 0.2285 0.2763 -0.0054 0.0419  0.0457  160 TRP A C   
943  O O   . TRP A 160 ? 0.1470 0.2152 0.2575 -0.0056 0.0393  0.0422  160 TRP A O   
944  C CB  . TRP A 160 ? 0.1648 0.2428 0.2888 0.0002  0.0594  0.0532  160 TRP A CB  
945  C CG  . TRP A 160 ? 0.1693 0.2521 0.3085 -0.0055 0.0584  0.0568  160 TRP A CG  
946  C CD1 . TRP A 160 ? 0.1896 0.2834 0.3494 -0.0074 0.0603  0.0610  160 TRP A CD1 
947  C CD2 . TRP A 160 ? 0.2093 0.2858 0.3456 -0.0101 0.0547  0.0563  160 TRP A CD2 
948  N NE1 . TRP A 160 ? 0.1952 0.2892 0.3643 -0.0135 0.0580  0.0629  160 TRP A NE1 
949  C CE2 . TRP A 160 ? 0.2089 0.2920 0.3641 -0.0151 0.0547  0.0600  160 TRP A CE2 
950  C CE3 . TRP A 160 ? 0.2457 0.3118 0.3668 -0.0105 0.0513  0.0532  160 TRP A CE3 
951  C CZ2 . TRP A 160 ? 0.2496 0.3277 0.4080 -0.0203 0.0519  0.0604  160 TRP A CZ2 
952  C CZ3 . TRP A 160 ? 0.3037 0.3657 0.4287 -0.0151 0.0487  0.0540  160 TRP A CZ3 
953  C CH2 . TRP A 160 ? 0.2763 0.3435 0.4194 -0.0198 0.0491  0.0573  160 TRP A CH2 
954  N N   . ASP A 161 ? 0.1394 0.2239 0.2802 -0.0099 0.0375  0.0465  161 ASP A N   
955  C CA  . ASP A 161 ? 0.1382 0.2194 0.2791 -0.0154 0.0302  0.0427  161 ASP A CA  
956  C C   . ASP A 161 ? 0.1531 0.2332 0.2864 -0.0157 0.0222  0.0372  161 ASP A C   
957  O O   . ASP A 161 ? 0.1573 0.2341 0.2886 -0.0199 0.0165  0.0329  161 ASP A O   
958  C CB  . ASP A 161 ? 0.1440 0.2321 0.3038 -0.0212 0.0283  0.0450  161 ASP A CB  
959  C CG  . ASP A 161 ? 0.2159 0.3172 0.3922 -0.0214 0.0264  0.0478  161 ASP A CG  
960  O OD1 . ASP A 161 ? 0.1666 0.2721 0.3426 -0.0161 0.0295  0.0498  161 ASP A OD1 
961  O OD2 . ASP A 161 ? 0.2184 0.3259 0.4097 -0.0273 0.0218  0.0482  161 ASP A OD2 
962  N N   . SER A 162 ? 0.1289 0.2112 0.2577 -0.0113 0.0221  0.0373  162 SER A N   
963  C CA  . SER A 162 ? 0.1313 0.2113 0.2500 -0.0109 0.0158  0.0330  162 SER A CA  
964  C C   . SER A 162 ? 0.1356 0.2077 0.2386 -0.0060 0.0193  0.0319  162 SER A C   
965  O O   . SER A 162 ? 0.1418 0.2124 0.2371 -0.0049 0.0153  0.0295  162 SER A O   
966  C CB  . SER A 162 ? 0.1334 0.2231 0.2615 -0.0110 0.0107  0.0344  162 SER A CB  
967  O OG  . SER A 162 ? 0.1505 0.2472 0.2908 -0.0169 0.0049  0.0341  162 SER A OG  
968  N N   . ASP A 163 ? 0.1452 0.2122 0.2429 -0.0035 0.0263  0.0337  163 ASP A N   
969  C CA  . ASP A 163 ? 0.1419 0.2010 0.2241 0.0004  0.0292  0.0322  163 ASP A CA  
970  C C   . ASP A 163 ? 0.1471 0.1984 0.2172 -0.0014 0.0261  0.0288  163 ASP A C   
971  O O   . ASP A 163 ? 0.1733 0.2185 0.2309 0.0010  0.0269  0.0272  163 ASP A O   
972  C CB  . ASP A 163 ? 0.1378 0.1949 0.2178 0.0036  0.0379  0.0354  163 ASP A CB  
973  C CG  . ASP A 163 ? 0.1879 0.2376 0.2529 0.0078  0.0408  0.0334  163 ASP A CG  
974  O OD1 . ASP A 163 ? 0.1962 0.2458 0.2600 0.0100  0.0386  0.0318  163 ASP A OD1 
975  O OD2 . ASP A 163 ? 0.2053 0.2490 0.2597 0.0086  0.0452  0.0338  163 ASP A OD2 
976  N N   . GLY A 164 ? 0.1475 0.1986 0.2215 -0.0054 0.0229  0.0275  164 GLY A N   
977  C CA  . GLY A 164 ? 0.1498 0.1939 0.2145 -0.0064 0.0208  0.0247  164 GLY A CA  
978  C C   . GLY A 164 ? 0.1495 0.1880 0.2080 -0.0050 0.0254  0.0275  164 GLY A C   
979  O O   . GLY A 164 ? 0.1624 0.1954 0.2095 -0.0035 0.0250  0.0264  164 GLY A O   
980  N N   . HIS A 165 ? 0.1432 0.1836 0.2093 -0.0058 0.0296  0.0317  165 HIS A N   
981  C CA  . HIS A 165 ? 0.1402 0.1758 0.2003 -0.0050 0.0340  0.0355  165 HIS A CA  
982  C C   . HIS A 165 ? 0.1523 0.1817 0.2071 -0.0061 0.0304  0.0341  165 HIS A C   
983  O O   . HIS A 165 ? 0.1498 0.1790 0.2112 -0.0087 0.0264  0.0313  165 HIS A O   
984  C CB  . HIS A 165 ? 0.1475 0.1867 0.2199 -0.0071 0.0381  0.0404  165 HIS A CB  
985  C CG  . HIS A 165 ? 0.1502 0.1857 0.2163 -0.0062 0.0438  0.0458  165 HIS A CG  
986  N ND1 . HIS A 165 ? 0.1648 0.1946 0.2284 -0.0077 0.0426  0.0482  165 HIS A ND1 
987  C CD2 . HIS A 165 ? 0.1728 0.2096 0.2342 -0.0038 0.0509  0.0496  165 HIS A CD2 
988  C CE1 . HIS A 165 ? 0.1641 0.1922 0.2210 -0.0066 0.0481  0.0539  165 HIS A CE1 
989  N NE2 . HIS A 165 ? 0.1776 0.2098 0.2323 -0.0044 0.0535  0.0544  165 HIS A NE2 
990  N N   . PRO A 166 ? 0.1556 0.1800 0.1986 -0.0043 0.0317  0.0360  166 PRO A N   
991  C CA  . PRO A 166 ? 0.1651 0.1846 0.2044 -0.0047 0.0277  0.0350  166 PRO A CA  
992  C C   . PRO A 166 ? 0.1581 0.1756 0.2079 -0.0071 0.0273  0.0373  166 PRO A C   
993  O O   . PRO A 166 ? 0.1602 0.1745 0.2114 -0.0075 0.0238  0.0350  166 PRO A O   
994  C CB  . PRO A 166 ? 0.1815 0.1971 0.2069 -0.0026 0.0290  0.0379  166 PRO A CB  
995  C CG  . PRO A 166 ? 0.3366 0.3539 0.3564 -0.0010 0.0340  0.0390  166 PRO A CG  
996  C CD  . PRO A 166 ? 0.2133 0.2364 0.2454 -0.0016 0.0363  0.0384  166 PRO A CD  
997  N N   . GLU A 167 ? 0.1584 0.1776 0.2164 -0.0088 0.0311  0.0416  167 GLU A N   
998  C CA  . GLU A 167 ? 0.1655 0.1819 0.2349 -0.0115 0.0308  0.0439  167 GLU A CA  
999  C C   . GLU A 167 ? 0.1260 0.1456 0.2087 -0.0150 0.0287  0.0397  167 GLU A C   
1000 O O   . GLU A 167 ? 0.1611 0.1784 0.2549 -0.0180 0.0288  0.0411  167 GLU A O   
1001 C CB  . GLU A 167 ? 0.1724 0.1879 0.2430 -0.0120 0.0360  0.0523  167 GLU A CB  
1002 C CG  . GLU A 167 ? 0.1926 0.2040 0.2498 -0.0095 0.0367  0.0569  167 GLU A CG  
1003 C CD  . GLU A 167 ? 0.2599 0.2712 0.3143 -0.0097 0.0426  0.0654  167 GLU A CD  
1004 O OE1 . GLU A 167 ? 0.3238 0.3399 0.3844 -0.0108 0.0476  0.0673  167 GLU A OE1 
1005 O OE2 . GLU A 167 ? 0.2594 0.2665 0.3054 -0.0088 0.0422  0.0706  167 GLU A OE2 
1006 N N   . ALA A 168 ? 0.1372 0.1618 0.2186 -0.0147 0.0264  0.0346  168 ALA A N   
1007 C CA  . ALA A 168 ? 0.1507 0.1791 0.2424 -0.0182 0.0231  0.0302  168 ALA A CA  
1008 C C   . ALA A 168 ? 0.1443 0.1697 0.2326 -0.0189 0.0182  0.0230  168 ALA A C   
1009 O O   . ALA A 168 ? 0.1596 0.1888 0.2510 -0.0212 0.0146  0.0182  168 ALA A O   
1010 C CB  . ALA A 168 ? 0.1400 0.1768 0.2338 -0.0176 0.0238  0.0306  168 ALA A CB  
1011 N N   . TRP A 169 ? 0.1400 0.1594 0.2221 -0.0169 0.0180  0.0225  169 TRP A N   
1012 C CA  . TRP A 169 ? 0.1413 0.1581 0.2199 -0.0168 0.0146  0.0159  169 TRP A CA  
1013 C C   . TRP A 169 ? 0.1453 0.1589 0.2335 -0.0205 0.0129  0.0112  169 TRP A C   
1014 O O   . TRP A 169 ? 0.1562 0.1679 0.2545 -0.0232 0.0140  0.0137  169 TRP A O   
1015 C CB  . TRP A 169 ? 0.1337 0.1457 0.2059 -0.0135 0.0152  0.0176  169 TRP A CB  
1016 C CG  . TRP A 169 ? 0.1729 0.1796 0.2508 -0.0133 0.0174  0.0234  169 TRP A CG  
1017 C CD1 . TRP A 169 ? 0.1666 0.1729 0.2406 -0.0117 0.0200  0.0309  169 TRP A CD1 
1018 C CD2 . TRP A 169 ? 0.1374 0.1380 0.2256 -0.0149 0.0173  0.0225  169 TRP A CD2 
1019 N NE1 . TRP A 169 ? 0.1756 0.1766 0.2568 -0.0123 0.0213  0.0357  169 TRP A NE1 
1020 C CE2 . TRP A 169 ? 0.1610 0.1580 0.2518 -0.0141 0.0197  0.0307  169 TRP A CE2 
1021 C CE3 . TRP A 169 ? 0.1585 0.1555 0.2533 -0.0169 0.0157  0.0154  169 TRP A CE3 
1022 C CZ2 . TRP A 169 ? 0.1942 0.1841 0.2956 -0.0150 0.0203  0.0328  169 TRP A CZ2 
1023 C CZ3 . TRP A 169 ? 0.1821 0.1713 0.2873 -0.0178 0.0167  0.0163  169 TRP A CZ3 
1024 C CH2 . TRP A 169 ? 0.1717 0.1575 0.2808 -0.0168 0.0189  0.0254  169 TRP A CH2 
1025 N N   . PHE A 170 ? 0.1457 0.1580 0.2303 -0.0208 0.0104  0.0042  170 PHE A N   
1026 C CA  . PHE A 170 ? 0.1480 0.1559 0.2388 -0.0242 0.0088  -0.0024 170 PHE A CA  
1027 C C   . PHE A 170 ? 0.1456 0.1495 0.2310 -0.0220 0.0089  -0.0079 170 PHE A C   
1028 O O   . PHE A 170 ? 0.1486 0.1559 0.2247 -0.0193 0.0086  -0.0084 170 PHE A O   
1029 C CB  . PHE A 170 ? 0.1703 0.1839 0.2626 -0.0287 0.0052  -0.0069 170 PHE A CB  
1030 C CG  . PHE A 170 ? 0.1294 0.1506 0.2121 -0.0273 0.0031  -0.0073 170 PHE A CG  
1031 C CD1 . PHE A 170 ? 0.1428 0.1702 0.2254 -0.0258 0.0039  -0.0011 170 PHE A CD1 
1032 C CD2 . PHE A 170 ? 0.1851 0.2070 0.2592 -0.0276 0.0009  -0.0138 170 PHE A CD2 
1033 C CE1 . PHE A 170 ? 0.1495 0.1829 0.2248 -0.0243 0.0021  -0.0011 170 PHE A CE1 
1034 C CE2 . PHE A 170 ? 0.1581 0.1866 0.2240 -0.0265 -0.0010 -0.0131 170 PHE A CE2 
1035 C CZ  . PHE A 170 ? 0.1792 0.2131 0.2462 -0.0248 -0.0007 -0.0067 170 PHE A CZ  
1036 N N   . SER A 171 ? 0.1493 0.1456 0.2415 -0.0230 0.0098  -0.0119 171 SER A N   
1037 C CA  . SER A 171 ? 0.1476 0.1399 0.2371 -0.0211 0.0107  -0.0184 171 SER A CA  
1038 C C   . SER A 171 ? 0.1648 0.1587 0.2491 -0.0248 0.0085  -0.0278 171 SER A C   
1039 O O   . SER A 171 ? 0.1975 0.1968 0.2801 -0.0285 0.0054  -0.0284 171 SER A O   
1040 C CB  . SER A 171 ? 0.1948 0.1775 0.2946 -0.0198 0.0132  -0.0180 171 SER A CB  
1041 O OG  . SER A 171 ? 0.2016 0.1791 0.3099 -0.0245 0.0125  -0.0213 171 SER A OG  
1042 N N   . ARG A 172 ? 0.1826 0.1723 0.2645 -0.0238 0.0102  -0.0353 172 ARG A N   
1043 C CA  . ARG A 172 ? 0.1923 0.1835 0.2661 -0.0272 0.0085  -0.0445 172 ARG A CA  
1044 C C   . ARG A 172 ? 0.1996 0.1891 0.2778 -0.0334 0.0050  -0.0483 172 ARG A C   
1045 O O   . ARG A 172 ? 0.2100 0.1917 0.2989 -0.0350 0.0059  -0.0493 172 ARG A O   
1046 C CB  . ARG A 172 ? 0.2530 0.2382 0.3254 -0.0250 0.0124  -0.0524 172 ARG A CB  
1047 C CG  . ARG A 172 ? 0.3303 0.3152 0.3941 -0.0294 0.0110  -0.0629 172 ARG A CG  
1048 C CD  . ARG A 172 ? 0.3187 0.3104 0.3696 -0.0277 0.0119  -0.0647 172 ARG A CD  
1049 N NE  . ARG A 172 ? 0.3673 0.3573 0.4083 -0.0313 0.0119  -0.0755 172 ARG A NE  
1050 C CZ  . ARG A 172 ? 0.3649 0.3568 0.3961 -0.0295 0.0155  -0.0803 172 ARG A CZ  
1051 N NH1 . ARG A 172 ? 0.3760 0.3714 0.4080 -0.0243 0.0193  -0.0753 172 ARG A NH1 
1052 N NH2 . ARG A 172 ? 0.4062 0.3967 0.4263 -0.0334 0.0153  -0.0902 172 ARG A NH2 
1053 N N   . ASP A 173 ? 0.2028 0.1999 0.2736 -0.0370 0.0006  -0.0499 173 ASP A N   
1054 C CA  . ASP A 173 ? 0.2030 0.2006 0.2774 -0.0437 -0.0041 -0.0539 173 ASP A CA  
1055 C C   . ASP A 173 ? 0.2254 0.2220 0.3143 -0.0454 -0.0045 -0.0471 173 ASP A C   
1056 O O   . ASP A 173 ? 0.2494 0.2421 0.3462 -0.0509 -0.0069 -0.0508 173 ASP A O   
1057 C CB  . ASP A 173 ? 0.2624 0.2516 0.3342 -0.0473 -0.0041 -0.0659 173 ASP A CB  
1058 C CG  . ASP A 173 ? 0.3727 0.3645 0.4285 -0.0468 -0.0038 -0.0729 173 ASP A CG  
1059 O OD1 . ASP A 173 ? 0.3218 0.3235 0.3687 -0.0468 -0.0068 -0.0694 173 ASP A OD1 
1060 O OD2 . ASP A 173 ? 0.4860 0.4699 0.5384 -0.0461 -0.0001 -0.0816 173 ASP A OD2 
1061 N N   . PHE A 174 ? 0.2015 0.2014 0.2937 -0.0412 -0.0021 -0.0372 174 PHE A N   
1062 C CA  . PHE A 174 ? 0.1913 0.1912 0.2961 -0.0424 -0.0013 -0.0295 174 PHE A CA  
1063 C C   . PHE A 174 ? 0.2024 0.1911 0.3183 -0.0436 0.0012  -0.0307 174 PHE A C   
1064 O O   . PHE A 174 ? 0.2211 0.2086 0.3487 -0.0471 0.0009  -0.0268 174 PHE A O   
1065 C CB  . PHE A 174 ? 0.1938 0.2023 0.3038 -0.0475 -0.0059 -0.0278 174 PHE A CB  
1066 C CG  . PHE A 174 ? 0.1651 0.1843 0.2656 -0.0462 -0.0087 -0.0264 174 PHE A CG  
1067 C CD1 . PHE A 174 ? 0.1711 0.1960 0.2699 -0.0415 -0.0063 -0.0182 174 PHE A CD1 
1068 C CD2 . PHE A 174 ? 0.2037 0.2267 0.2968 -0.0498 -0.0140 -0.0332 174 PHE A CD2 
1069 C CE1 . PHE A 174 ? 0.1732 0.2067 0.2645 -0.0401 -0.0088 -0.0166 174 PHE A CE1 
1070 C CE2 . PHE A 174 ? 0.1940 0.2266 0.2792 -0.0486 -0.0168 -0.0308 174 PHE A CE2 
1071 C CZ  . PHE A 174 ? 0.1636 0.2011 0.2488 -0.0436 -0.0141 -0.0224 174 PHE A CZ  
1072 N N   . ALA A 175 ? 0.1887 0.1689 0.3023 -0.0406 0.0040  -0.0354 175 ALA A N   
1073 C CA  . ALA A 175 ? 0.2022 0.1704 0.3273 -0.0415 0.0063  -0.0370 175 ALA A CA  
1074 C C   . ALA A 175 ? 0.2393 0.2058 0.3740 -0.0393 0.0091  -0.0254 175 ALA A C   
1075 O O   . ALA A 175 ? 0.2296 0.1891 0.3767 -0.0424 0.0098  -0.0235 175 ALA A O   
1076 C CB  . ALA A 175 ? 0.2574 0.2174 0.3792 -0.0377 0.0095  -0.0441 175 ALA A CB  
1077 N N   . LYS A 176 ? 0.2046 0.1769 0.3334 -0.0342 0.0108  -0.0176 176 LYS A N   
1078 C CA  . LYS A 176 ? 0.1897 0.1623 0.3239 -0.0323 0.0132  -0.0062 176 LYS A CA  
1079 C C   . LYS A 176 ? 0.1615 0.1452 0.2874 -0.0310 0.0127  -0.0007 176 LYS A C   
1080 O O   . LYS A 176 ? 0.1794 0.1688 0.2945 -0.0290 0.0112  -0.0040 176 LYS A O   
1081 C CB  . LYS A 176 ? 0.2362 0.2025 0.3711 -0.0266 0.0159  -0.0019 176 LYS A CB  
1082 C CG  . LYS A 176 ? 0.3894 0.3550 0.5292 -0.0254 0.0181  0.0103  176 LYS A CG  
1083 C CD  . LYS A 176 ? 0.4433 0.4013 0.5871 -0.0207 0.0198  0.0150  176 LYS A CD  
1084 C CE  . LYS A 176 ? 0.3471 0.3078 0.4886 -0.0185 0.0211  0.0277  176 LYS A CE  
1085 N NZ  . LYS A 176 ? 0.5202 0.4734 0.6680 -0.0149 0.0221  0.0342  176 LYS A NZ  
1086 N N   . THR A 177 ? 0.1747 0.1614 0.3061 -0.0323 0.0142  0.0077  177 THR A N   
1087 C CA  . THR A 177 ? 0.1791 0.1757 0.3043 -0.0310 0.0147  0.0125  177 THR A CA  
1088 C C   . THR A 177 ? 0.1713 0.1676 0.2967 -0.0285 0.0188  0.0231  177 THR A C   
1089 O O   . THR A 177 ? 0.1781 0.1683 0.3123 -0.0298 0.0208  0.0280  177 THR A O   
1090 C CB  . THR A 177 ? 0.1982 0.2020 0.3299 -0.0361 0.0125  0.0109  177 THR A CB  
1091 O OG1 . THR A 177 ? 0.2130 0.2129 0.3591 -0.0408 0.0131  0.0130  177 THR A OG1 
1092 C CG2 . THR A 177 ? 0.1975 0.2033 0.3247 -0.0383 0.0077  0.0009  177 THR A CG2 
1093 N N   . GLY A 178 ? 0.1655 0.1680 0.2807 -0.0252 0.0201  0.0267  178 GLY A N   
1094 C CA  . GLY A 178 ? 0.1748 0.1778 0.2871 -0.0230 0.0241  0.0361  178 GLY A CA  
1095 C C   . GLY A 178 ? 0.1474 0.1552 0.2685 -0.0261 0.0274  0.0416  178 GLY A C   
1096 O O   . GLY A 178 ? 0.1684 0.1807 0.2984 -0.0298 0.0259  0.0384  178 GLY A O   
1097 N N   . ALA A 179 ? 0.1695 0.1768 0.2877 -0.0245 0.0320  0.0504  179 ALA A N   
1098 C CA  . ALA A 179 ? 0.1971 0.2082 0.3247 -0.0273 0.0366  0.0572  179 ALA A CA  
1099 C C   . ALA A 179 ? 0.1888 0.2102 0.3187 -0.0278 0.0379  0.0558  179 ALA A C   
1100 O O   . ALA A 179 ? 0.1897 0.2157 0.3331 -0.0316 0.0399  0.0586  179 ALA A O   
1101 C CB  . ALA A 179 ? 0.2275 0.2364 0.3476 -0.0249 0.0416  0.0669  179 ALA A CB  
1102 N N   . THR A 180 ? 0.1559 0.1812 0.2743 -0.0242 0.0369  0.0520  180 THR A N   
1103 C CA  . THR A 180 ? 0.1417 0.1766 0.2636 -0.0239 0.0384  0.0514  180 THR A CA  
1104 C C   . THR A 180 ? 0.1597 0.1985 0.2870 -0.0261 0.0321  0.0439  180 THR A C   
1105 O O   . THR A 180 ? 0.1624 0.2096 0.2926 -0.0254 0.0320  0.0433  180 THR A O   
1106 C CB  . THR A 180 ? 0.1553 0.1919 0.2627 -0.0187 0.0421  0.0529  180 THR A CB  
1107 O OG1 . THR A 180 ? 0.1571 0.1893 0.2519 -0.0162 0.0377  0.0475  180 THR A OG1 
1108 C CG2 . THR A 180 ? 0.1856 0.2190 0.2864 -0.0173 0.0486  0.0607  180 THR A CG2 
1109 N N   . PHE A 181 ? 0.1608 0.1941 0.2897 -0.0286 0.0270  0.0384  181 PHE A N   
1110 C CA  . PHE A 181 ? 0.1518 0.1884 0.2837 -0.0313 0.0208  0.0310  181 PHE A CA  
1111 C C   . PHE A 181 ? 0.1414 0.1864 0.2889 -0.0358 0.0198  0.0325  181 PHE A C   
1112 O O   . PHE A 181 ? 0.1459 0.1903 0.3056 -0.0394 0.0221  0.0366  181 PHE A O   
1113 C CB  . PHE A 181 ? 0.1555 0.1836 0.2873 -0.0337 0.0170  0.0249  181 PHE A CB  
1114 C CG  . PHE A 181 ? 0.1553 0.1858 0.2881 -0.0370 0.0108  0.0167  181 PHE A CG  
1115 C CD1 . PHE A 181 ? 0.1683 0.2001 0.2887 -0.0343 0.0081  0.0118  181 PHE A CD1 
1116 C CD2 . PHE A 181 ? 0.1927 0.2241 0.3380 -0.0433 0.0076  0.0140  181 PHE A CD2 
1117 C CE1 . PHE A 181 ? 0.1907 0.2249 0.3097 -0.0375 0.0024  0.0047  181 PHE A CE1 
1118 C CE2 . PHE A 181 ? 0.1788 0.2125 0.3227 -0.0468 0.0013  0.0061  181 PHE A CE2 
1119 C CZ  . PHE A 181 ? 0.1851 0.2204 0.3151 -0.0437 -0.0011 0.0016  181 PHE A CZ  
1120 N N   . ARG A 182 ? 0.1425 0.1958 0.2903 -0.0357 0.0162  0.0299  182 ARG A N   
1121 C CA  . ARG A 182 ? 0.1285 0.1917 0.2922 -0.0399 0.0141  0.0315  182 ARG A CA  
1122 C C   . ARG A 182 ? 0.1225 0.1905 0.2873 -0.0433 0.0056  0.0251  182 ARG A C   
1123 O O   . ARG A 182 ? 0.1324 0.2047 0.3103 -0.0494 0.0013  0.0240  182 ARG A O   
1124 C CB  . ARG A 182 ? 0.1509 0.2234 0.3184 -0.0359 0.0193  0.0381  182 ARG A CB  
1125 C CG  . ARG A 182 ? 0.1373 0.2087 0.3082 -0.0343 0.0283  0.0458  182 ARG A CG  
1126 C CD  . ARG A 182 ? 0.1481 0.2193 0.3350 -0.0404 0.0290  0.0490  182 ARG A CD  
1127 N NE  . ARG A 182 ? 0.1986 0.2711 0.3895 -0.0389 0.0380  0.0575  182 ARG A NE  
1128 C CZ  . ARG A 182 ? 0.1828 0.2461 0.3671 -0.0383 0.0422  0.0609  182 ARG A CZ  
1129 N NH1 . ARG A 182 ? 0.1761 0.2288 0.3505 -0.0382 0.0384  0.0565  182 ARG A NH1 
1130 N NH2 . ARG A 182 ? 0.2028 0.2664 0.3857 -0.0363 0.0493  0.0676  182 ARG A NH2 
1131 N N   . ARG A 183 ? 0.1448 0.2127 0.2960 -0.0399 0.0029  0.0213  183 ARG A N   
1132 C CA  . ARG A 183 ? 0.1506 0.2250 0.3014 -0.0424 -0.0048 0.0171  183 ARG A CA  
1133 C C   . ARG A 183 ? 0.1634 0.2305 0.2982 -0.0419 -0.0081 0.0097  183 ARG A C   
1134 O O   . ARG A 183 ? 0.1634 0.2260 0.2860 -0.0367 -0.0048 0.0100  183 ARG A O   
1135 C CB  . ARG A 183 ? 0.1882 0.2723 0.3394 -0.0380 -0.0045 0.0216  183 ARG A CB  
1136 C CG  . ARG A 183 ? 0.1653 0.2579 0.3317 -0.0366 0.0005  0.0294  183 ARG A CG  
1137 C CD  . ARG A 183 ? 0.1615 0.2622 0.3279 -0.0315 0.0006  0.0328  183 ARG A CD  
1138 N NE  . ARG A 183 ? 0.1545 0.2635 0.3253 -0.0347 -0.0085 0.0311  183 ARG A NE  
1139 C CZ  . ARG A 183 ? 0.1431 0.2645 0.3293 -0.0350 -0.0109 0.0359  183 ARG A CZ  
1140 N NH1 . ARG A 183 ? 0.1623 0.2897 0.3605 -0.0310 -0.0037 0.0425  183 ARG A NH1 
1141 N NH2 . ARG A 183 ? 0.1902 0.3190 0.3803 -0.0394 -0.0206 0.0342  183 ARG A NH2 
1142 N N   . LYS A 184 ? 0.1660 0.2323 0.3007 -0.0474 -0.0144 0.0031  184 LYS A N   
1143 C CA  . LYS A 184 ? 0.1418 0.2037 0.2608 -0.0469 -0.0175 -0.0039 184 LYS A CA  
1144 C C   . LYS A 184 ? 0.1573 0.2274 0.2695 -0.0445 -0.0209 -0.0021 184 LYS A C   
1145 O O   . LYS A 184 ? 0.1894 0.2565 0.2879 -0.0411 -0.0202 -0.0040 184 LYS A O   
1146 C CB  . LYS A 184 ? 0.1761 0.2348 0.2959 -0.0538 -0.0230 -0.0120 184 LYS A CB  
1147 C CG  . LYS A 184 ? 0.1974 0.2449 0.3222 -0.0557 -0.0195 -0.0151 184 LYS A CG  
1148 C CD  . LYS A 184 ? 0.2295 0.2724 0.3546 -0.0627 -0.0248 -0.0245 184 LYS A CD  
1149 C CE  . LYS A 184 ? 0.2924 0.3237 0.4256 -0.0645 -0.0210 -0.0264 184 LYS A CE  
1150 N NZ  . LYS A 184 ? 0.3665 0.3918 0.5020 -0.0718 -0.0258 -0.0360 184 LYS A NZ  
1151 N N   . VAL A 185 ? 0.1621 0.2428 0.2848 -0.0464 -0.0248 0.0019  185 VAL A N   
1152 C CA  . VAL A 185 ? 0.1425 0.2316 0.2615 -0.0441 -0.0285 0.0049  185 VAL A CA  
1153 C C   . VAL A 185 ? 0.1236 0.2173 0.2506 -0.0384 -0.0229 0.0131  185 VAL A C   
1154 O O   . VAL A 185 ? 0.1459 0.2457 0.2888 -0.0394 -0.0214 0.0177  185 VAL A O   
1155 C CB  . VAL A 185 ? 0.1722 0.2708 0.2972 -0.0501 -0.0379 0.0038  185 VAL A CB  
1156 C CG1 . VAL A 185 ? 0.1708 0.2779 0.2919 -0.0470 -0.0419 0.0083  185 VAL A CG1 
1157 C CG2 . VAL A 185 ? 0.1964 0.2892 0.3122 -0.0562 -0.0427 -0.0056 185 VAL A CG2 
1158 N N   . TYR A 186 ? 0.1393 0.2296 0.2554 -0.0325 -0.0193 0.0146  186 TYR A N   
1159 C CA  . TYR A 186 ? 0.1300 0.2228 0.2508 -0.0266 -0.0136 0.0211  186 TYR A CA  
1160 C C   . TYR A 186 ? 0.1479 0.2518 0.2772 -0.0255 -0.0179 0.0257  186 TYR A C   
1161 O O   . TYR A 186 ? 0.1405 0.2487 0.2666 -0.0283 -0.0256 0.0242  186 TYR A O   
1162 C CB  . TYR A 186 ? 0.1676 0.2519 0.2733 -0.0215 -0.0092 0.0202  186 TYR A CB  
1163 C CG  . TYR A 186 ? 0.1431 0.2182 0.2439 -0.0204 -0.0031 0.0188  186 TYR A CG  
1164 C CD1 . TYR A 186 ? 0.1581 0.2306 0.2648 -0.0244 -0.0027 0.0171  186 TYR A CD1 
1165 C CD2 . TYR A 186 ? 0.1598 0.2287 0.2505 -0.0156 0.0017  0.0197  186 TYR A CD2 
1166 C CE1 . TYR A 186 ? 0.1619 0.2262 0.2648 -0.0232 0.0025  0.0172  186 TYR A CE1 
1167 C CE2 . TYR A 186 ? 0.1434 0.2048 0.2293 -0.0147 0.0063  0.0194  186 TYR A CE2 
1168 C CZ  . TYR A 186 ? 0.1649 0.2242 0.2570 -0.0183 0.0067  0.0185  186 TYR A CZ  
1169 O OH  . TYR A 186 ? 0.1917 0.2436 0.2792 -0.0170 0.0109  0.0193  186 TYR A OH  
1170 N N   . GLU A 187 ? 0.1385 0.2471 0.2789 -0.0213 -0.0127 0.0317  187 GLU A N   
1171 C CA  . GLU A 187 ? 0.1283 0.2473 0.2796 -0.0188 -0.0155 0.0372  187 GLU A CA  
1172 C C   . GLU A 187 ? 0.1447 0.2599 0.2920 -0.0111 -0.0084 0.0403  187 GLU A C   
1173 O O   . GLU A 187 ? 0.1427 0.2542 0.2916 -0.0078 0.0002  0.0415  187 GLU A O   
1174 C CB  . GLU A 187 ? 0.1488 0.2789 0.3220 -0.0213 -0.0156 0.0416  187 GLU A CB  
1175 C CG  . GLU A 187 ? 0.1486 0.2903 0.3371 -0.0174 -0.0164 0.0486  187 GLU A CG  
1176 C CD  . GLU A 187 ? 0.1446 0.2969 0.3558 -0.0191 -0.0139 0.0533  187 GLU A CD  
1177 O OE1 . GLU A 187 ? 0.1893 0.3390 0.4040 -0.0147 -0.0037 0.0556  187 GLU A OE1 
1178 O OE2 . GLU A 187 ? 0.1716 0.3299 0.3897 -0.0243 -0.0216 0.0529  187 GLU A OE2 
1179 N N   . TYR A 188 ? 0.1184 0.2339 0.2597 -0.0083 -0.0120 0.0415  188 TYR A N   
1180 C CA  . TYR A 188 ? 0.1149 0.2259 0.2531 -0.0012 -0.0060 0.0441  188 TYR A CA  
1181 C C   . TYR A 188 ? 0.1269 0.2485 0.2819 0.0022  -0.0077 0.0507  188 TYR A C   
1182 O O   . TYR A 188 ? 0.1454 0.2739 0.3033 0.0003  -0.0162 0.0531  188 TYR A O   
1183 C CB  . TYR A 188 ? 0.1048 0.2066 0.2245 -0.0001 -0.0078 0.0411  188 TYR A CB  
1184 C CG  . TYR A 188 ? 0.1192 0.2113 0.2243 -0.0027 -0.0058 0.0350  188 TYR A CG  
1185 C CD1 . TYR A 188 ? 0.1367 0.2221 0.2387 -0.0006 0.0020  0.0338  188 TYR A CD1 
1186 C CD2 . TYR A 188 ? 0.1342 0.2243 0.2287 -0.0072 -0.0115 0.0308  188 TYR A CD2 
1187 C CE1 . TYR A 188 ? 0.1118 0.1890 0.2019 -0.0027 0.0032  0.0293  188 TYR A CE1 
1188 C CE2 . TYR A 188 ? 0.1337 0.2154 0.2169 -0.0089 -0.0093 0.0257  188 TYR A CE2 
1189 C CZ  . TYR A 188 ? 0.1184 0.1940 0.2004 -0.0066 -0.0024 0.0253  188 TYR A CZ  
1190 O OH  . TYR A 188 ? 0.1402 0.2082 0.2123 -0.0081 -0.0011 0.0211  188 TYR A OH  
1191 N N   . THR A 189 ? 0.1148 0.2386 0.2814 0.0070  0.0005  0.0540  189 THR A N   
1192 C CA  . THR A 189 ? 0.1186 0.2532 0.3046 0.0112  0.0004  0.0608  189 THR A CA  
1193 C C   . THR A 189 ? 0.1241 0.2532 0.3063 0.0183  0.0029  0.0629  189 THR A C   
1194 O O   . THR A 189 ? 0.1396 0.2771 0.3357 0.0213  -0.0005 0.0688  189 THR A O   
1195 C CB  . THR A 189 ? 0.1306 0.2711 0.3329 0.0130  0.0089  0.0635  189 THR A CB  
1196 O OG1 . THR A 189 ? 0.1379 0.2668 0.3272 0.0151  0.0187  0.0596  189 THR A OG1 
1197 C CG2 . THR A 189 ? 0.1472 0.2971 0.3608 0.0055  0.0038  0.0639  189 THR A CG2 
1198 N N   . ASN A 190 ? 0.1310 0.2461 0.2952 0.0206  0.0081  0.0584  190 ASN A N   
1199 C CA  . ASN A 190 ? 0.1320 0.2394 0.2895 0.0259  0.0091  0.0592  190 ASN A CA  
1200 C C   . ASN A 190 ? 0.1179 0.2278 0.2910 0.0337  0.0156  0.0638  190 ASN A C   
1201 O O   . ASN A 190 ? 0.1500 0.2580 0.3255 0.0378  0.0136  0.0671  190 ASN A O   
1202 C CB  . ASN A 190 ? 0.1550 0.2637 0.3063 0.0229  -0.0014 0.0607  190 ASN A CB  
1203 C CG  . ASN A 190 ? 0.1371 0.2409 0.2710 0.0164  -0.0057 0.0550  190 ASN A CG  
1204 O OD1 . ASN A 190 ? 0.1496 0.2424 0.2691 0.0165  -0.0011 0.0501  190 ASN A OD1 
1205 N ND2 . ASN A 190 ? 0.1394 0.2514 0.2746 0.0107  -0.0145 0.0555  190 ASN A ND2 
1206 N N   . LYS A 191 ? 0.1291 0.2426 0.3127 0.0361  0.0242  0.0643  191 LYS A N   
1207 C CA  . LYS A 191 ? 0.1240 0.2403 0.3235 0.0440  0.0322  0.0681  191 LYS A CA  
1208 C C   . LYS A 191 ? 0.1600 0.2604 0.3444 0.0490  0.0420  0.0629  191 LYS A C   
1209 O O   . LYS A 191 ? 0.1768 0.2736 0.3580 0.0508  0.0519  0.0600  191 LYS A O   
1210 C CB  . LYS A 191 ? 0.1429 0.2684 0.3563 0.0427  0.0364  0.0700  191 LYS A CB  
1211 C CG  . LYS A 191 ? 0.1496 0.2876 0.3745 0.0367  0.0256  0.0738  191 LYS A CG  
1212 C CD  . LYS A 191 ? 0.2617 0.4070 0.5011 0.0362  0.0299  0.0762  191 LYS A CD  
1213 C CE  . LYS A 191 ? 0.3419 0.4994 0.5932 0.0301  0.0191  0.0797  191 LYS A CE  
1214 N NZ  . LYS A 191 ? 0.3964 0.5617 0.6653 0.0317  0.0228  0.0838  191 LYS A NZ  
1215 N N   . GLN A 192 ? 0.1608 0.2513 0.3347 0.0508  0.0388  0.0617  192 GLN A N   
1216 C CA  . GLN A 192 ? 0.1789 0.2532 0.3370 0.0544  0.0463  0.0561  192 GLN A CA  
1217 C C   . GLN A 192 ? 0.1749 0.2420 0.3311 0.0572  0.0418  0.0578  192 GLN A C   
1218 O O   . GLN A 192 ? 0.1810 0.2551 0.3433 0.0550  0.0323  0.0629  192 GLN A O   
1219 C CB  . GLN A 192 ? 0.1502 0.2155 0.2859 0.0488  0.0461  0.0495  192 GLN A CB  
1220 C CG  . GLN A 192 ? 0.1565 0.2211 0.2815 0.0425  0.0354  0.0488  192 GLN A CG  
1221 C CD  . GLN A 192 ? 0.1200 0.1790 0.2283 0.0373  0.0356  0.0434  192 GLN A CD  
1222 O OE1 . GLN A 192 ? 0.1545 0.2210 0.2653 0.0326  0.0324  0.0437  192 GLN A OE1 
1223 N NE2 . GLN A 192 ? 0.1528 0.1988 0.2446 0.0379  0.0388  0.0384  192 GLN A NE2 
1224 N N   . MET A 193 ? 0.1722 0.2249 0.3193 0.0616  0.0488  0.0536  193 MET A N   
1225 C CA  . MET A 193 ? 0.2157 0.2591 0.3602 0.0641  0.0455  0.0549  193 MET A CA  
1226 C C   . MET A 193 ? 0.1747 0.2167 0.3057 0.0571  0.0352  0.0548  193 MET A C   
1227 O O   . MET A 193 ? 0.1894 0.2303 0.3066 0.0513  0.0335  0.0503  193 MET A O   
1228 C CB  . MET A 193 ? 0.2966 0.3224 0.4283 0.0677  0.0542  0.0479  193 MET A CB  
1229 C CG  . MET A 193 ? 0.3411 0.3654 0.4820 0.0750  0.0663  0.0462  193 MET A CG  
1230 S SD  . MET A 193 ? 0.4402 0.4417 0.5616 0.0779  0.0753  0.0364  193 MET A SD  
1231 C CE  . MET A 193 ? 0.3926 0.3837 0.5149 0.0788  0.0680  0.0392  193 MET A CE  
1232 N N   . GLY A 194 ? 0.1815 0.2232 0.3168 0.0578  0.0287  0.0601  194 GLY A N   
1233 C CA  . GLY A 194 ? 0.1811 0.2203 0.3024 0.0516  0.0203  0.0599  194 GLY A CA  
1234 C C   . GLY A 194 ? 0.1685 0.1930 0.2700 0.0491  0.0236  0.0522  194 GLY A C   
1235 O O   . GLY A 194 ? 0.1840 0.1964 0.2821 0.0531  0.0307  0.0482  194 GLY A O   
1236 N N   . ALA A 195 ? 0.1593 0.1850 0.2479 0.0424  0.0184  0.0498  195 ALA A N   
1237 C CA  . ALA A 195 ? 0.1498 0.1640 0.2210 0.0394  0.0209  0.0427  195 ALA A CA  
1238 C C   . ALA A 195 ? 0.1492 0.1662 0.2100 0.0327  0.0138  0.0423  195 ALA A C   
1239 O O   . ALA A 195 ? 0.1589 0.1870 0.2237 0.0297  0.0083  0.0455  195 ALA A O   
1240 C CB  . ALA A 195 ? 0.1747 0.1880 0.2416 0.0397  0.0275  0.0372  195 ALA A CB  
1241 N N   . THR A 196 ? 0.1373 0.1442 0.1846 0.0301  0.0144  0.0378  196 THR A N   
1242 C CA  . THR A 196 ? 0.1587 0.1676 0.1955 0.0240  0.0099  0.0357  196 THR A CA  
1243 C C   . THR A 196 ? 0.1472 0.1573 0.1786 0.0222  0.0128  0.0306  196 THR A C   
1244 O O   . THR A 196 ? 0.1757 0.1773 0.1999 0.0230  0.0171  0.0262  196 THR A O   
1245 C CB  . THR A 196 ? 0.1562 0.1545 0.1833 0.0219  0.0090  0.0341  196 THR A CB  
1246 O OG1 . THR A 196 ? 0.1693 0.1654 0.2021 0.0237  0.0068  0.0398  196 THR A OG1 
1247 C CG2 . THR A 196 ? 0.1869 0.1887 0.2053 0.0160  0.0050  0.0326  196 THR A CG2 
1248 N N   . LEU A 197 ? 0.1456 0.1660 0.1807 0.0198  0.0103  0.0314  197 LEU A N   
1249 C CA  . LEU A 197 ? 0.1389 0.1607 0.1695 0.0175  0.0120  0.0275  197 LEU A CA  
1250 C C   . LEU A 197 ? 0.1359 0.1589 0.1585 0.0124  0.0076  0.0256  197 LEU A C   
1251 O O   . LEU A 197 ? 0.1424 0.1655 0.1622 0.0106  0.0037  0.0271  197 LEU A O   
1252 C CB  . LEU A 197 ? 0.1695 0.2008 0.2109 0.0181  0.0130  0.0293  197 LEU A CB  
1253 C CG  . LEU A 197 ? 0.1489 0.1824 0.2022 0.0233  0.0174  0.0323  197 LEU A CG  
1254 C CD1 . LEU A 197 ? 0.1614 0.2051 0.2255 0.0226  0.0182  0.0339  197 LEU A CD1 
1255 C CD2 . LEU A 197 ? 0.1684 0.1913 0.2157 0.0270  0.0246  0.0292  197 LEU A CD2 
1256 N N   . TRP A 198 ? 0.1370 0.1609 0.1562 0.0104  0.0086  0.0225  198 TRP A N   
1257 C CA  . TRP A 198 ? 0.1328 0.1588 0.1468 0.0062  0.0051  0.0207  198 TRP A CA  
1258 C C   . TRP A 198 ? 0.1342 0.1641 0.1509 0.0048  0.0060  0.0190  198 TRP A C   
1259 O O   . TRP A 198 ? 0.1456 0.1747 0.1651 0.0067  0.0098  0.0192  198 TRP A O   
1260 C CB  . TRP A 198 ? 0.1370 0.1556 0.1416 0.0050  0.0052  0.0184  198 TRP A CB  
1261 C CG  . TRP A 198 ? 0.1324 0.1446 0.1315 0.0058  0.0086  0.0158  198 TRP A CG  
1262 C CD1 . TRP A 198 ? 0.1584 0.1651 0.1562 0.0089  0.0127  0.0153  198 TRP A CD1 
1263 C CD2 . TRP A 198 ? 0.1381 0.1489 0.1315 0.0034  0.0078  0.0135  198 TRP A CD2 
1264 N NE1 . TRP A 198 ? 0.1556 0.1576 0.1454 0.0080  0.0142  0.0128  198 TRP A NE1 
1265 C CE2 . TRP A 198 ? 0.1560 0.1607 0.1438 0.0047  0.0108  0.0121  198 TRP A CE2 
1266 C CE3 . TRP A 198 ? 0.1449 0.1592 0.1378 0.0004  0.0051  0.0126  198 TRP A CE3 
1267 C CZ2 . TRP A 198 ? 0.1530 0.1556 0.1349 0.0029  0.0100  0.0106  198 TRP A CZ2 
1268 C CZ3 . TRP A 198 ? 0.1452 0.1574 0.1340 -0.0008 0.0050  0.0111  198 TRP A CZ3 
1269 C CH2 . TRP A 198 ? 0.1517 0.1583 0.1352 0.0004  0.0069  0.0105  198 TRP A CH2 
1270 N N   . TYR A 199 ? 0.1318 0.1659 0.1479 0.0014  0.0029  0.0175  199 TYR A N   
1271 C CA  . TYR A 199 ? 0.1286 0.1655 0.1482 -0.0003 0.0033  0.0158  199 TYR A CA  
1272 C C   . TYR A 199 ? 0.1325 0.1660 0.1458 -0.0021 0.0032  0.0128  199 TYR A C   
1273 O O   . TYR A 199 ? 0.1336 0.1661 0.1418 -0.0032 0.0015  0.0119  199 TYR A O   
1274 C CB  . TYR A 199 ? 0.1286 0.1731 0.1548 -0.0026 -0.0002 0.0160  199 TYR A CB  
1275 C CG  . TYR A 199 ? 0.1333 0.1803 0.1546 -0.0054 -0.0043 0.0146  199 TYR A CG  
1276 C CD1 . TYR A 199 ? 0.1301 0.1792 0.1500 -0.0049 -0.0069 0.0176  199 TYR A CD1 
1277 C CD2 . TYR A 199 ? 0.1358 0.1831 0.1540 -0.0083 -0.0051 0.0106  199 TYR A CD2 
1278 C CE1 . TYR A 199 ? 0.1343 0.1862 0.1483 -0.0077 -0.0103 0.0169  199 TYR A CE1 
1279 C CE2 . TYR A 199 ? 0.1374 0.1871 0.1500 -0.0108 -0.0079 0.0089  199 TYR A CE2 
1280 C CZ  . TYR A 199 ? 0.1504 0.2027 0.1601 -0.0107 -0.0105 0.0122  199 TYR A CZ  
1281 O OH  . TYR A 199 ? 0.1511 0.2061 0.1537 -0.0135 -0.0129 0.0109  199 TYR A OH  
1282 N N   . HIS A 200 ? 0.1180 0.1501 0.1329 -0.0023 0.0052  0.0120  200 HIS A N   
1283 C CA  . HIS A 200 ? 0.1221 0.1513 0.1330 -0.0034 0.0050  0.0100  200 HIS A CA  
1284 C C   . HIS A 200 ? 0.1479 0.1769 0.1635 -0.0039 0.0065  0.0099  200 HIS A C   
1285 O O   . HIS A 200 ? 0.1376 0.1677 0.1582 -0.0034 0.0084  0.0117  200 HIS A O   
1286 C CB  . HIS A 200 ? 0.1350 0.1588 0.1386 -0.0021 0.0059  0.0105  200 HIS A CB  
1287 C CG  . HIS A 200 ? 0.1437 0.1639 0.1453 0.0000  0.0089  0.0122  200 HIS A CG  
1288 N ND1 . HIS A 200 ? 0.1732 0.1919 0.1746 0.0001  0.0107  0.0131  200 HIS A ND1 
1289 C CD2 . HIS A 200 ? 0.1380 0.1553 0.1371 0.0021  0.0110  0.0131  200 HIS A CD2 
1290 C CE1 . HIS A 200 ? 0.2133 0.2289 0.2109 0.0020  0.0139  0.0144  200 HIS A CE1 
1291 N NE2 . HIS A 200 ? 0.1776 0.1920 0.1738 0.0034  0.0145  0.0139  200 HIS A NE2 
1292 N N   . ASP A 201 ? 0.1361 0.1635 0.1510 -0.0048 0.0060  0.0082  201 ASP A N   
1293 C CA  . ASP A 201 ? 0.1220 0.1482 0.1420 -0.0052 0.0073  0.0087  201 ASP A CA  
1294 C C   . ASP A 201 ? 0.1402 0.1631 0.1576 -0.0035 0.0097  0.0124  201 ASP A C   
1295 O O   . ASP A 201 ? 0.1588 0.1791 0.1688 -0.0022 0.0098  0.0133  201 ASP A O   
1296 C CB  . ASP A 201 ? 0.1415 0.1665 0.1626 -0.0058 0.0064  0.0064  201 ASP A CB  
1297 C CG  . ASP A 201 ? 0.1318 0.1549 0.1602 -0.0063 0.0075  0.0068  201 ASP A CG  
1298 O OD1 . ASP A 201 ? 0.1529 0.1773 0.1867 -0.0082 0.0072  0.0041  201 ASP A OD1 
1299 O OD2 . ASP A 201 ? 0.1549 0.1749 0.1834 -0.0051 0.0085  0.0100  201 ASP A OD2 
1300 N N   . HIS A 202 ? 0.1428 0.1654 0.1659 -0.0039 0.0116  0.0144  202 HIS A N   
1301 C CA  . HIS A 202 ? 0.1473 0.1673 0.1673 -0.0025 0.0146  0.0185  202 HIS A CA  
1302 C C   . HIS A 202 ? 0.1466 0.1647 0.1721 -0.0034 0.0155  0.0211  202 HIS A C   
1303 O O   . HIS A 202 ? 0.1561 0.1733 0.1816 -0.0030 0.0186  0.0252  202 HIS A O   
1304 C CB  . HIS A 202 ? 0.1688 0.1912 0.1904 -0.0016 0.0178  0.0201  202 HIS A CB  
1305 C CG  . HIS A 202 ? 0.1816 0.2009 0.1947 0.0005  0.0214  0.0225  202 HIS A CG  
1306 N ND1 . HIS A 202 ? 0.3387 0.3545 0.3461 0.0007  0.0229  0.0255  202 HIS A ND1 
1307 C CD2 . HIS A 202 ? 0.2896 0.3086 0.2985 0.0026  0.0239  0.0222  202 HIS A CD2 
1308 C CE1 . HIS A 202 ? 0.2377 0.2511 0.2362 0.0025  0.0263  0.0264  202 HIS A CE1 
1309 N NE2 . HIS A 202 ? 0.2952 0.3100 0.2948 0.0038  0.0273  0.0241  202 HIS A NE2 
1310 N N   . ALA A 203 ? 0.1405 0.1578 0.1712 -0.0044 0.0133  0.0190  203 ALA A N   
1311 C CA  . ALA A 203 ? 0.1466 0.1612 0.1844 -0.0051 0.0143  0.0217  203 ALA A CA  
1312 C C   . ALA A 203 ? 0.1509 0.1623 0.1834 -0.0035 0.0147  0.0270  203 ALA A C   
1313 O O   . ALA A 203 ? 0.1539 0.1646 0.1800 -0.0023 0.0125  0.0270  203 ALA A O   
1314 C CB  . ALA A 203 ? 0.1597 0.1732 0.2042 -0.0060 0.0124  0.0175  203 ALA A CB  
1315 N N   . ILE A 204 ? 0.1517 0.1614 0.1873 -0.0039 0.0173  0.0322  204 ILE A N   
1316 C CA  . ILE A 204 ? 0.1463 0.1534 0.1745 -0.0027 0.0177  0.0382  204 ILE A CA  
1317 C C   . ILE A 204 ? 0.1511 0.1560 0.1813 -0.0018 0.0141  0.0392  204 ILE A C   
1318 O O   . ILE A 204 ? 0.1671 0.1707 0.2080 -0.0020 0.0133  0.0374  204 ILE A O   
1319 C CB  . ILE A 204 ? 0.1540 0.1601 0.1852 -0.0036 0.0218  0.0444  204 ILE A CB  
1320 C CG1 . ILE A 204 ? 0.1680 0.1723 0.1863 -0.0024 0.0227  0.0502  204 ILE A CG1 
1321 C CG2 . ILE A 204 ? 0.1509 0.1541 0.1955 -0.0049 0.0215  0.0464  204 ILE A CG2 
1322 C CD1 . ILE A 204 ? 0.2105 0.2145 0.2292 -0.0032 0.0281  0.0568  204 ILE A CD1 
1323 N N   . GLY A 205 ? 0.1444 0.1490 0.1647 -0.0007 0.0118  0.0419  205 GLY A N   
1324 C CA  . GLY A 205 ? 0.1610 0.1647 0.1837 0.0004  0.0078  0.0444  205 GLY A CA  
1325 C C   . GLY A 205 ? 0.1572 0.1635 0.1820 0.0010  0.0048  0.0391  205 GLY A C   
1326 O O   . GLY A 205 ? 0.1654 0.1726 0.1912 0.0020  0.0012  0.0415  205 GLY A O   
1327 N N   . ILE A 206 ? 0.1451 0.1532 0.1715 0.0002  0.0060  0.0326  206 ILE A N   
1328 C CA  . ILE A 206 ? 0.1460 0.1568 0.1753 0.0005  0.0041  0.0277  206 ILE A CA  
1329 C C   . ILE A 206 ? 0.1562 0.1691 0.1786 -0.0006 0.0044  0.0231  206 ILE A C   
1330 O O   . ILE A 206 ? 0.1413 0.1567 0.1663 -0.0009 0.0040  0.0187  206 ILE A O   
1331 C CB  . ILE A 206 ? 0.1280 0.1382 0.1696 0.0009  0.0054  0.0244  206 ILE A CB  
1332 C CG1 . ILE A 206 ? 0.1540 0.1632 0.1985 -0.0009 0.0081  0.0209  206 ILE A CG1 
1333 C CG2 . ILE A 206 ? 0.1762 0.1837 0.2265 0.0026  0.0047  0.0294  206 ILE A CG2 
1334 C CD1 . ILE A 206 ? 0.1633 0.1712 0.2175 -0.0012 0.0091  0.0157  206 ILE A CD1 
1335 N N   . THR A 207 ? 0.1530 0.1651 0.1670 -0.0010 0.0057  0.0242  207 THR A N   
1336 C CA  . THR A 207 ? 0.1330 0.1465 0.1420 -0.0015 0.0061  0.0204  207 THR A CA  
1337 C C   . THR A 207 ? 0.1275 0.1422 0.1326 -0.0018 0.0031  0.0186  207 THR A C   
1338 O O   . THR A 207 ? 0.1386 0.1553 0.1443 -0.0025 0.0029  0.0151  207 THR A O   
1339 C CB  . THR A 207 ? 0.1580 0.1697 0.1593 -0.0011 0.0085  0.0222  207 THR A CB  
1340 O OG1 . THR A 207 ? 0.1761 0.1884 0.1837 -0.0013 0.0117  0.0236  207 THR A OG1 
1341 C CG2 . THR A 207 ? 0.1599 0.1722 0.1566 -0.0011 0.0088  0.0188  207 THR A CG2 
1342 N N   . ARG A 208 ? 0.1442 0.1580 0.1453 -0.0017 0.0004  0.0214  208 ARG A N   
1343 C CA  . ARG A 208 ? 0.1457 0.1610 0.1444 -0.0027 -0.0028 0.0201  208 ARG A CA  
1344 C C   . ARG A 208 ? 0.1499 0.1693 0.1583 -0.0026 -0.0029 0.0177  208 ARG A C   
1345 O O   . ARG A 208 ? 0.1517 0.1732 0.1593 -0.0037 -0.0037 0.0154  208 ARG A O   
1346 C CB  . ARG A 208 ? 0.1560 0.1705 0.1502 -0.0031 -0.0067 0.0240  208 ARG A CB  
1347 C CG  . ARG A 208 ? 0.1526 0.1696 0.1568 -0.0019 -0.0084 0.0277  208 ARG A CG  
1348 C CD  . ARG A 208 ? 0.1513 0.1672 0.1498 -0.0021 -0.0122 0.0333  208 ARG A CD  
1349 N NE  . ARG A 208 ? 0.1548 0.1730 0.1644 -0.0004 -0.0140 0.0378  208 ARG A NE  
1350 C CZ  . ARG A 208 ? 0.1410 0.1572 0.1573 0.0013  -0.0112 0.0402  208 ARG A CZ  
1351 N NH1 . ARG A 208 ? 0.1515 0.1643 0.1647 0.0011  -0.0067 0.0389  208 ARG A NH1 
1352 N NH2 . ARG A 208 ? 0.1582 0.1757 0.1858 0.0031  -0.0129 0.0445  208 ARG A NH2 
1353 N N   . LEU A 209 ? 0.1329 0.1530 0.1504 -0.0014 -0.0016 0.0182  209 LEU A N   
1354 C CA  . LEU A 209 ? 0.1273 0.1507 0.1537 -0.0010 -0.0007 0.0153  209 LEU A CA  
1355 C C   . LEU A 209 ? 0.1238 0.1479 0.1494 -0.0019 0.0019  0.0104  209 LEU A C   
1356 O O   . LEU A 209 ? 0.1506 0.1780 0.1774 -0.0025 0.0025  0.0075  209 LEU A O   
1357 C CB  . LEU A 209 ? 0.1433 0.1655 0.1798 0.0009  0.0003  0.0169  209 LEU A CB  
1358 C CG  . LEU A 209 ? 0.1348 0.1563 0.1732 0.0021  -0.0027 0.0232  209 LEU A CG  
1359 C CD1 . LEU A 209 ? 0.1332 0.1528 0.1835 0.0044  -0.0013 0.0251  209 LEU A CD1 
1360 C CD2 . LEU A 209 ? 0.1736 0.1997 0.2124 0.0019  -0.0065 0.0250  209 LEU A CD2 
1361 N N   . ASN A 210 ? 0.1194 0.1413 0.1434 -0.0023 0.0033  0.0098  210 ASN A N   
1362 C CA  . ASN A 210 ? 0.1267 0.1501 0.1507 -0.0035 0.0048  0.0056  210 ASN A CA  
1363 C C   . ASN A 210 ? 0.1303 0.1555 0.1469 -0.0045 0.0038  0.0050  210 ASN A C   
1364 O O   . ASN A 210 ? 0.1476 0.1755 0.1635 -0.0056 0.0042  0.0021  210 ASN A O   
1365 C CB  . ASN A 210 ? 0.1331 0.1544 0.1592 -0.0040 0.0059  0.0060  210 ASN A CB  
1366 C CG  . ASN A 210 ? 0.1390 0.1578 0.1738 -0.0036 0.0071  0.0056  210 ASN A CG  
1367 O OD1 . ASN A 210 ? 0.1637 0.1822 0.2032 -0.0025 0.0073  0.0047  210 ASN A OD1 
1368 N ND2 . ASN A 210 ? 0.1438 0.1606 0.1821 -0.0044 0.0081  0.0067  210 ASN A ND2 
1369 N N   . VAL A 211 ? 0.1217 0.1448 0.1323 -0.0043 0.0028  0.0078  211 VAL A N   
1370 C CA  . VAL A 211 ? 0.1356 0.1591 0.1403 -0.0051 0.0020  0.0075  211 VAL A CA  
1371 C C   . VAL A 211 ? 0.1405 0.1662 0.1455 -0.0060 0.0007  0.0070  211 VAL A C   
1372 O O   . VAL A 211 ? 0.1388 0.1667 0.1424 -0.0072 0.0009  0.0058  211 VAL A O   
1373 C CB  . VAL A 211 ? 0.1320 0.1515 0.1303 -0.0044 0.0019  0.0095  211 VAL A CB  
1374 C CG1 . VAL A 211 ? 0.1663 0.1846 0.1594 -0.0050 0.0011  0.0091  211 VAL A CG1 
1375 C CG2 . VAL A 211 ? 0.1400 0.1589 0.1399 -0.0034 0.0042  0.0102  211 VAL A CG2 
1376 N N   . TYR A 212 ? 0.1270 0.1530 0.1346 -0.0057 -0.0006 0.0086  212 TYR A N   
1377 C CA  . TYR A 212 ? 0.1323 0.1617 0.1423 -0.0069 -0.0017 0.0086  212 TYR A CA  
1378 C C   . TYR A 212 ? 0.1352 0.1690 0.1502 -0.0069 0.0010  0.0057  212 TYR A C   
1379 O O   . TYR A 212 ? 0.1397 0.1766 0.1543 -0.0084 0.0015  0.0053  212 TYR A O   
1380 C CB  . TYR A 212 ? 0.1240 0.1543 0.1383 -0.0063 -0.0040 0.0113  212 TYR A CB  
1381 C CG  . TYR A 212 ? 0.1209 0.1554 0.1388 -0.0079 -0.0060 0.0123  212 TYR A CG  
1382 C CD1 . TYR A 212 ? 0.1544 0.1870 0.1661 -0.0103 -0.0090 0.0132  212 TYR A CD1 
1383 C CD2 . TYR A 212 ? 0.1325 0.1726 0.1605 -0.0070 -0.0045 0.0120  212 TYR A CD2 
1384 C CE1 . TYR A 212 ? 0.1403 0.1773 0.1568 -0.0125 -0.0111 0.0144  212 TYR A CE1 
1385 C CE2 . TYR A 212 ? 0.1236 0.1689 0.1569 -0.0086 -0.0060 0.0135  212 TYR A CE2 
1386 C CZ  . TYR A 212 ? 0.1204 0.1644 0.1481 -0.0116 -0.0096 0.0149  212 TYR A CZ  
1387 O OH  . TYR A 212 ? 0.1516 0.2009 0.1856 -0.0139 -0.0114 0.0167  212 TYR A OH  
1388 N N   . SER A 213 ? 0.1293 0.1629 0.1485 -0.0057 0.0030  0.0036  213 SER A N   
1389 C CA  . SER A 213 ? 0.1269 0.1637 0.1493 -0.0058 0.0060  -0.0003 213 SER A CA  
1390 C C   . SER A 213 ? 0.1257 0.1639 0.1413 -0.0077 0.0066  -0.0022 213 SER A C   
1391 O O   . SER A 213 ? 0.1407 0.1821 0.1563 -0.0084 0.0090  -0.0052 213 SER A O   
1392 C CB  . SER A 213 ? 0.1475 0.1820 0.1754 -0.0045 0.0078  -0.0028 213 SER A CB  
1393 O OG  . SER A 213 ? 0.1822 0.2158 0.2179 -0.0024 0.0075  -0.0003 213 SER A OG  
1394 N N   . GLY A 214 ? 0.1303 0.1663 0.1401 -0.0084 0.0046  -0.0003 214 GLY A N   
1395 C CA  . GLY A 214 ? 0.1427 0.1804 0.1468 -0.0100 0.0044  -0.0006 214 GLY A CA  
1396 C C   . GLY A 214 ? 0.1337 0.1701 0.1358 -0.0100 0.0032  -0.0005 214 GLY A C   
1397 O O   . GLY A 214 ? 0.1536 0.1919 0.1516 -0.0112 0.0022  0.0000  214 GLY A O   
1398 N N   . LEU A 215 ? 0.1336 0.1674 0.1391 -0.0088 0.0031  -0.0004 215 LEU A N   
1399 C CA  . LEU A 215 ? 0.1439 0.1780 0.1501 -0.0091 0.0023  -0.0004 215 LEU A CA  
1400 C C   . LEU A 215 ? 0.1197 0.1521 0.1236 -0.0080 0.0015  0.0033  215 LEU A C   
1401 O O   . LEU A 215 ? 0.1506 0.1803 0.1562 -0.0066 0.0024  0.0049  215 LEU A O   
1402 C CB  . LEU A 215 ? 0.1325 0.1649 0.1447 -0.0088 0.0033  -0.0017 215 LEU A CB  
1403 C CG  . LEU A 215 ? 0.1355 0.1684 0.1506 -0.0098 0.0044  -0.0063 215 LEU A CG  
1404 C CD1 . LEU A 215 ? 0.1739 0.2034 0.1962 -0.0093 0.0053  -0.0066 215 LEU A CD1 
1405 C CD2 . LEU A 215 ? 0.1682 0.2043 0.1799 -0.0122 0.0033  -0.0098 215 LEU A CD2 
1406 N N   . SER A 216 ? 0.1348 0.1686 0.1350 -0.0085 0.0003  0.0046  216 SER A N   
1407 C CA  . SER A 216 ? 0.1394 0.1714 0.1387 -0.0071 -0.0001 0.0077  216 SER A CA  
1408 C C   . SER A 216 ? 0.1472 0.1823 0.1445 -0.0080 -0.0021 0.0093  216 SER A C   
1409 O O   . SER A 216 ? 0.1545 0.1922 0.1486 -0.0100 -0.0026 0.0084  216 SER A O   
1410 C CB  . SER A 216 ? 0.1606 0.1872 0.1563 -0.0060 0.0006  0.0090  216 SER A CB  
1411 O OG  . SER A 216 ? 0.1761 0.2031 0.1691 -0.0077 -0.0002 0.0089  216 SER A OG  
1412 N N   . GLY A 217 ? 0.1235 0.1588 0.1230 -0.0065 -0.0028 0.0122  217 GLY A N   
1413 C CA  . GLY A 217 ? 0.1352 0.1734 0.1337 -0.0070 -0.0053 0.0152  217 GLY A CA  
1414 C C   . GLY A 217 ? 0.1279 0.1640 0.1305 -0.0040 -0.0050 0.0188  217 GLY A C   
1415 O O   . GLY A 217 ? 0.1444 0.1776 0.1501 -0.0017 -0.0024 0.0183  217 GLY A O   
1416 N N   . PHE A 218 ? 0.1258 0.1635 0.1285 -0.0037 -0.0073 0.0228  218 PHE A N   
1417 C CA  . PHE A 218 ? 0.1330 0.1686 0.1414 -0.0002 -0.0068 0.0266  218 PHE A CA  
1418 C C   . PHE A 218 ? 0.1361 0.1793 0.1528 0.0006  -0.0090 0.0289  218 PHE A C   
1419 O O   . PHE A 218 ? 0.1408 0.1909 0.1570 -0.0023 -0.0127 0.0288  218 PHE A O   
1420 C CB  . PHE A 218 ? 0.1409 0.1738 0.1470 0.0001  -0.0084 0.0310  218 PHE A CB  
1421 C CG  . PHE A 218 ? 0.1455 0.1697 0.1465 -0.0001 -0.0061 0.0297  218 PHE A CG  
1422 C CD1 . PHE A 218 ? 0.1523 0.1683 0.1550 0.0030  -0.0033 0.0295  218 PHE A CD1 
1423 C CD2 . PHE A 218 ? 0.1502 0.1746 0.1449 -0.0036 -0.0069 0.0289  218 PHE A CD2 
1424 C CE1 . PHE A 218 ? 0.1726 0.1801 0.1703 0.0021  -0.0021 0.0279  218 PHE A CE1 
1425 C CE2 . PHE A 218 ? 0.1645 0.1817 0.1559 -0.0045 -0.0055 0.0281  218 PHE A CE2 
1426 C CZ  . PHE A 218 ? 0.1592 0.1676 0.1519 -0.0019 -0.0036 0.0275  218 PHE A CZ  
1427 N N   . TYR A 219 ? 0.1193 0.1613 0.1438 0.0046  -0.0066 0.0310  219 TYR A N   
1428 C CA  . TYR A 219 ? 0.1259 0.1759 0.1613 0.0057  -0.0086 0.0342  219 TYR A CA  
1429 C C   . TYR A 219 ? 0.1327 0.1800 0.1752 0.0107  -0.0067 0.0387  219 TYR A C   
1430 O O   . TYR A 219 ? 0.1518 0.1919 0.1946 0.0140  -0.0012 0.0371  219 TYR A O   
1431 C CB  . TYR A 219 ? 0.1114 0.1636 0.1519 0.0057  -0.0056 0.0312  219 TYR A CB  
1432 C CG  . TYR A 219 ? 0.1139 0.1752 0.1673 0.0061  -0.0071 0.0341  219 TYR A CG  
1433 C CD1 . TYR A 219 ? 0.1445 0.2074 0.2089 0.0107  -0.0045 0.0382  219 TYR A CD1 
1434 C CD2 . TYR A 219 ? 0.1288 0.1970 0.1846 0.0018  -0.0107 0.0322  219 TYR A CD2 
1435 C CE1 . TYR A 219 ? 0.1284 0.2012 0.2071 0.0110  -0.0058 0.0412  219 TYR A CE1 
1436 C CE2 . TYR A 219 ? 0.1311 0.2081 0.2000 0.0013  -0.0126 0.0348  219 TYR A CE2 
1437 C CZ  . TYR A 219 ? 0.1140 0.1939 0.1948 0.0059  -0.0102 0.0396  219 TYR A CZ  
1438 O OH  . TYR A 219 ? 0.1417 0.2317 0.2376 0.0053  -0.0119 0.0425  219 TYR A OH  
1439 N N   . LEU A 220 ? 0.1367 0.1891 0.1845 0.0113  -0.0112 0.0445  220 LEU A N   
1440 C CA  . LEU A 220 ? 0.1611 0.2098 0.2160 0.0164  -0.0098 0.0494  220 LEU A CA  
1441 C C   . LEU A 220 ? 0.1568 0.2149 0.2276 0.0194  -0.0111 0.0542  220 LEU A C   
1442 O O   . LEU A 220 ? 0.1583 0.2267 0.2330 0.0167  -0.0176 0.0575  220 LEU A O   
1443 C CB  . LEU A 220 ? 0.1602 0.2067 0.2098 0.0152  -0.0140 0.0540  220 LEU A CB  
1444 C CG  . LEU A 220 ? 0.1542 0.1948 0.1896 0.0111  -0.0138 0.0502  220 LEU A CG  
1445 C CD1 . LEU A 220 ? 0.1832 0.2223 0.2150 0.0100  -0.0174 0.0561  220 LEU A CD1 
1446 C CD2 . LEU A 220 ? 0.1733 0.2029 0.2040 0.0124  -0.0077 0.0446  220 LEU A CD2 
1447 N N   . ILE A 221 ? 0.1339 0.1886 0.2139 0.0249  -0.0051 0.0546  221 ILE A N   
1448 C CA  . ILE A 221 ? 0.1429 0.2067 0.2408 0.0288  -0.0052 0.0599  221 ILE A CA  
1449 C C   . ILE A 221 ? 0.1340 0.1937 0.2390 0.0340  -0.0052 0.0658  221 ILE A C   
1450 O O   . ILE A 221 ? 0.1762 0.2239 0.2783 0.0379  0.0010  0.0635  221 ILE A O   
1451 C CB  . ILE A 221 ? 0.1253 0.1890 0.2303 0.0318  0.0028  0.0566  221 ILE A CB  
1452 C CG1 . ILE A 221 ? 0.1310 0.1972 0.2289 0.0266  0.0031  0.0512  221 ILE A CG1 
1453 C CG2 . ILE A 221 ? 0.1613 0.2356 0.2875 0.0362  0.0032  0.0628  221 ILE A CG2 
1454 C CD1 . ILE A 221 ? 0.1540 0.2195 0.2568 0.0291  0.0115  0.0486  221 ILE A CD1 
1455 N N   . GLU A 222 ? 0.1457 0.2145 0.2595 0.0340  -0.0125 0.0736  222 GLU A N   
1456 C CA  . GLU A 222 ? 0.1517 0.2170 0.2738 0.0392  -0.0132 0.0806  222 GLU A CA  
1457 C C   . GLU A 222 ? 0.2341 0.3023 0.3761 0.0467  -0.0077 0.0835  222 GLU A C   
1458 O O   . GLU A 222 ? 0.2274 0.3087 0.3828 0.0468  -0.0095 0.0861  222 GLU A O   
1459 C CB  . GLU A 222 ? 0.2351 0.3095 0.3584 0.0364  -0.0236 0.0888  222 GLU A CB  
1460 C CG  . GLU A 222 ? 0.2152 0.2854 0.3476 0.0418  -0.0247 0.0975  222 GLU A CG  
1461 C CD  . GLU A 222 ? 0.3029 0.3826 0.4357 0.0389  -0.0355 0.1070  222 GLU A CD  
1462 O OE1 . GLU A 222 ? 0.3029 0.3900 0.4243 0.0320  -0.0417 0.1054  222 GLU A OE1 
1463 O OE2 . GLU A 222 ? 0.3840 0.4626 0.5267 0.0430  -0.0371 0.1146  222 GLU A OE2 
1464 N N   . ASP A 223 ? 0.1932 0.2491 0.3379 0.0528  -0.0008 0.0830  223 ASP A N   
1465 C CA  . ASP A 223 ? 0.2253 0.2833 0.3895 0.0608  0.0056  0.0856  223 ASP A CA  
1466 C C   . ASP A 223 ? 0.2563 0.3223 0.4381 0.0645  -0.0006 0.0968  223 ASP A C   
1467 O O   . ASP A 223 ? 0.2239 0.2859 0.3999 0.0629  -0.0067 0.1014  223 ASP A O   
1468 C CB  . ASP A 223 ? 0.2559 0.2963 0.4154 0.0660  0.0159  0.0798  223 ASP A CB  
1469 C CG  . ASP A 223 ? 0.3071 0.3489 0.4828 0.0736  0.0256  0.0791  223 ASP A CG  
1470 O OD1 . ASP A 223 ? 0.2765 0.3201 0.4674 0.0785  0.0259  0.0845  223 ASP A OD1 
1471 O OD2 . ASP A 223 ? 0.2862 0.3279 0.4567 0.0728  0.0324  0.0723  223 ASP A OD2 
1472 N N   . PRO A 224 ? 0.2549 0.3303 0.4525 0.0667  0.0012  0.0988  224 PRO A N   
1473 C CA  . PRO A 224 ? 0.2418 0.3231 0.4508 0.0677  -0.0047 0.1068  224 PRO A CA  
1474 C C   . PRO A 224 ? 0.2778 0.3455 0.4880 0.0729  -0.0016 0.1090  224 PRO A C   
1475 O O   . PRO A 224 ? 0.2849 0.3553 0.4999 0.0727  -0.0081 0.1165  224 PRO A O   
1476 C CB  . PRO A 224 ? 0.3129 0.4048 0.5391 0.0699  -0.0009 0.1073  224 PRO A CB  
1477 C CG  . PRO A 224 ? 0.3118 0.3988 0.5348 0.0718  0.0099  0.0989  224 PRO A CG  
1478 C CD  . PRO A 224 ? 0.2725 0.3552 0.4779 0.0673  0.0074  0.0947  224 PRO A CD  
1479 N N   . VAL A 225 ? 0.2291 0.2815 0.4342 0.0772  0.0081  0.1025  225 VAL A N   
1480 C CA  . VAL A 225 ? 0.2994 0.3370 0.5051 0.0818  0.0115  0.1034  225 VAL A CA  
1481 C C   . VAL A 225 ? 0.2831 0.3151 0.4775 0.0777  0.0034  0.1079  225 VAL A C   
1482 O O   . VAL A 225 ? 0.3689 0.3947 0.5674 0.0797  0.0016  0.1130  225 VAL A O   
1483 C CB  . VAL A 225 ? 0.3807 0.4028 0.5808 0.0861  0.0236  0.0936  225 VAL A CB  
1484 C CG1 . VAL A 225 ? 0.2919 0.3022 0.4728 0.0826  0.0238  0.0882  225 VAL A CG1 
1485 C CG2 . VAL A 225 ? 0.5150 0.5256 0.7230 0.0923  0.0297  0.0933  225 VAL A CG2 
1486 N N   . GLU A 226 ? 0.2700 0.3048 0.4505 0.0717  -0.0016 0.1067  226 GLU A N   
1487 C CA  . GLU A 226 ? 0.2753 0.3028 0.4426 0.0675  -0.0073 0.1098  226 GLU A CA  
1488 C C   . GLU A 226 ? 0.3399 0.3755 0.5109 0.0652  -0.0164 0.1195  226 GLU A C   
1489 O O   . GLU A 226 ? 0.3104 0.3374 0.4751 0.0639  -0.0189 0.1233  226 GLU A O   
1490 C CB  . GLU A 226 ? 0.2939 0.3242 0.4453 0.0612  -0.0103 0.1061  226 GLU A CB  
1491 C CG  . GLU A 226 ? 0.3122 0.3310 0.4523 0.0607  -0.0011 0.0937  226 GLU A CG  
1492 C CD  . GLU A 226 ? 0.3091 0.3313 0.4313 0.0525  -0.0036 0.0872  226 GLU A CD  
1493 O OE1 . GLU A 226 ? 0.2778 0.2966 0.3873 0.0474  -0.0081 0.0882  226 GLU A OE1 
1494 O OE2 . GLU A 226 ? 0.2821 0.3107 0.4037 0.0514  -0.0007 0.0815  226 GLU A OE2 
1495 N N   . LYS A 227 ? 0.3667 0.4184 0.5474 0.0642  -0.0214 0.1235  227 LYS A N   
1496 C CA  . LYS A 227 ? 0.4733 0.5332 0.6572 0.0620  -0.0302 0.1327  227 LYS A CA  
1497 C C   . LYS A 227 ? 0.4360 0.4865 0.6297 0.0674  -0.0278 0.1377  227 LYS A C   
1498 O O   . LYS A 227 ? 0.5094 0.5615 0.7015 0.0654  -0.0344 0.1455  227 LYS A O   
1499 C CB  . LYS A 227 ? 0.4099 0.4875 0.6049 0.0606  -0.0350 0.1354  227 LYS A CB  
1500 C CG  . LYS A 227 ? 0.5173 0.6065 0.7024 0.0530  -0.0461 0.1396  227 LYS A CG  
1501 C CD  . LYS A 227 ? 0.5486 0.6541 0.7458 0.0516  -0.0514 0.1425  227 LYS A CD  
1502 C CE  . LYS A 227 ? 0.4653 0.5726 0.6807 0.0574  -0.0435 0.1395  227 LYS A CE  
1503 N NZ  . LYS A 227 ? 0.5732 0.6842 0.7842 0.0546  -0.0404 0.1314  227 LYS A NZ  
1504 N N   . HIS A 228 ? 0.3856 0.4262 0.5890 0.0742  -0.0183 0.1334  228 HIS A N   
1505 C CA  . HIS A 228 ? 0.4223 0.4534 0.6359 0.0797  -0.0156 0.1375  228 HIS A CA  
1506 C C   . HIS A 228 ? 0.3861 0.3963 0.5916 0.0818  -0.0086 0.1319  228 HIS A C   
1507 O O   . HIS A 228 ? 0.4834 0.4829 0.6973 0.0869  -0.0046 0.1331  228 HIS A O   
1508 C CB  . HIS A 228 ? 0.5034 0.5410 0.7374 0.0859  -0.0112 0.1385  228 HIS A CB  
1509 C CG  . HIS A 228 ? 0.6122 0.6695 0.8556 0.0834  -0.0193 0.1455  228 HIS A CG  
1510 N ND1 . HIS A 228 ? 0.5893 0.6539 0.8306 0.0794  -0.0297 0.1547  228 HIS A ND1 
1511 C CD2 . HIS A 228 ? 0.5778 0.6485 0.8317 0.0837  -0.0187 0.1445  228 HIS A CD2 
1512 C CE1 . HIS A 228 ? 0.5771 0.6585 0.8272 0.0775  -0.0355 0.1587  228 HIS A CE1 
1513 N NE2 . HIS A 228 ? 0.5988 0.6842 0.8573 0.0799  -0.0291 0.1528  228 HIS A NE2 
1514 N N   . LEU A 229 ? 0.3150 0.3189 0.5045 0.0778  -0.0074 0.1256  229 LEU A N   
1515 C CA  . LEU A 229 ? 0.3033 0.2881 0.4819 0.0772  -0.0035 0.1213  229 LEU A CA  
1516 C C   . LEU A 229 ? 0.3785 0.3640 0.5451 0.0705  -0.0118 0.1278  229 LEU A C   
1517 O O   . LEU A 229 ? 0.3499 0.3503 0.5145 0.0663  -0.0197 0.1339  229 LEU A O   
1518 C CB  . LEU A 229 ? 0.3356 0.3139 0.5036 0.0763  0.0027  0.1109  229 LEU A CB  
1519 C CG  . LEU A 229 ? 0.3887 0.3604 0.5628 0.0824  0.0135  0.1019  229 LEU A CG  
1520 C CD1 . LEU A 229 ? 0.3601 0.3273 0.5211 0.0802  0.0179  0.0928  229 LEU A CD1 
1521 C CD2 . LEU A 229 ? 0.4398 0.3938 0.6182 0.0873  0.0197  0.0992  229 LEU A CD2 
1522 N N   . LYS A 230 ? 0.2802 0.2493 0.4380 0.0689  -0.0095 0.1258  230 LYS A N   
1523 C CA  . LYS A 230 ? 0.2748 0.2433 0.4208 0.0622  -0.0160 0.1316  230 LYS A CA  
1524 C C   . LYS A 230 ? 0.2530 0.2119 0.3835 0.0574  -0.0135 0.1248  230 LYS A C   
1525 O O   . LYS A 230 ? 0.3030 0.2499 0.4265 0.0541  -0.0135 0.1257  230 LYS A O   
1526 C CB  . LYS A 230 ? 0.2881 0.2468 0.4399 0.0640  -0.0166 0.1380  230 LYS A CB  
1527 C CG  . LYS A 230 ? 0.2822 0.2504 0.4501 0.0688  -0.0194 0.1457  230 LYS A CG  
1528 C CD  . LYS A 230 ? 0.3563 0.3152 0.5289 0.0699  -0.0209 0.1532  230 LYS A CD  
1529 C CE  . LYS A 230 ? 0.3601 0.3317 0.5463 0.0728  -0.0263 0.1633  230 LYS A CE  
1530 N NZ  . LYS A 230 ? 0.5018 0.4648 0.6924 0.0737  -0.0282 0.1716  230 LYS A NZ  
1531 N N   . LEU A 231 ? 0.2315 0.1954 0.3575 0.0568  -0.0114 0.1183  231 LEU A N   
1532 C CA  . LEU A 231 ? 0.2360 0.1923 0.3477 0.0519  -0.0096 0.1125  231 LEU A CA  
1533 C C   . LEU A 231 ? 0.2930 0.2576 0.3923 0.0439  -0.0168 0.1181  231 LEU A C   
1534 O O   . LEU A 231 ? 0.2825 0.2617 0.3826 0.0424  -0.0229 0.1245  231 LEU A O   
1535 C CB  . LEU A 231 ? 0.2466 0.2100 0.3532 0.0513  -0.0060 0.1018  231 LEU A CB  
1536 C CG  . LEU A 231 ? 0.2624 0.2188 0.3789 0.0588  0.0023  0.0953  231 LEU A CG  
1537 C CD1 . LEU A 231 ? 0.2711 0.2367 0.3824 0.0575  0.0052  0.0868  231 LEU A CD1 
1538 C CD2 . LEU A 231 ? 0.2915 0.2267 0.4037 0.0599  0.0087  0.0886  231 LEU A CD2 
1539 N N   . PRO A 232 ? 0.2565 0.2130 0.3422 0.0377  -0.0155 0.1133  232 PRO A N   
1540 C CA  . PRO A 232 ? 0.2186 0.1841 0.2919 0.0302  -0.0209 0.1175  232 PRO A CA  
1541 C C   . PRO A 232 ? 0.2240 0.2067 0.2917 0.0278  -0.0237 0.1142  232 PRO A C   
1542 O O   . PRO A 232 ? 0.2409 0.2253 0.3077 0.0288  -0.0201 0.1047  232 PRO A O   
1543 C CB  . PRO A 232 ? 0.2507 0.2052 0.3127 0.0246  -0.0173 0.1100  232 PRO A CB  
1544 C CG  . PRO A 232 ? 0.2517 0.1879 0.3215 0.0291  -0.0119 0.1060  232 PRO A CG  
1545 C CD  . PRO A 232 ? 0.3023 0.2409 0.3842 0.0372  -0.0094 0.1046  232 PRO A CD  
1546 N N   . LYS A 233 ? 0.2192 0.2142 0.2824 0.0245  -0.0302 0.1221  233 LYS A N   
1547 C CA  . LYS A 233 ? 0.2562 0.2673 0.3155 0.0224  -0.0339 0.1198  233 LYS A CA  
1548 C C   . LYS A 233 ? 0.2592 0.2784 0.3030 0.0150  -0.0380 0.1219  233 LYS A C   
1549 O O   . LYS A 233 ? 0.2480 0.2618 0.2851 0.0117  -0.0380 0.1264  233 LYS A O   
1550 C CB  . LYS A 233 ? 0.2834 0.3047 0.3565 0.0271  -0.0385 0.1268  233 LYS A CB  
1551 C CG  . LYS A 233 ? 0.3455 0.3674 0.4211 0.0270  -0.0423 0.1352  233 LYS A CG  
1552 C CD  . LYS A 233 ? 0.4306 0.4611 0.5216 0.0318  -0.0452 0.1390  233 LYS A CD  
1553 C CE  . LYS A 233 ? 0.5000 0.5269 0.6051 0.0385  -0.0394 0.1338  233 LYS A CE  
1554 N NZ  . LYS A 233 ? 0.4114 0.4226 0.5265 0.0445  -0.0334 0.1342  233 LYS A NZ  
1555 N N   . ASP A 234 ? 0.2656 0.3326 0.2707 0.0041  -0.0505 0.0787  234 ASP A N   
1556 C CA  . ASP A 234 ? 0.3005 0.3669 0.2876 0.0023  -0.0567 0.0743  234 ASP A CA  
1557 C C   . ASP A 234 ? 0.2721 0.3326 0.2456 0.0017  -0.0485 0.0692  234 ASP A C   
1558 O O   . ASP A 234 ? 0.2463 0.3045 0.2246 0.0003  -0.0432 0.0643  234 ASP A O   
1559 C CB  . ASP A 234 ? 0.3128 0.3818 0.2929 0.0041  -0.0646 0.0805  234 ASP A CB  
1560 C CG  . ASP A 234 ? 0.3784 0.4542 0.3753 0.0040  -0.0745 0.0853  234 ASP A CG  
1561 O OD1 . ASP A 234 ? 0.4746 0.5532 0.4832 0.0013  -0.0788 0.0814  234 ASP A OD1 
1562 O OD2 . ASP A 234 ? 0.4684 0.5472 0.4687 0.0064  -0.0780 0.0935  234 ASP A OD2 
1563 N N   . GLY A 235 ? 0.2558 0.3141 0.2140 0.0030  -0.0467 0.0713  235 GLY A N   
1564 C CA  . GLY A 235 ? 0.2395 0.2935 0.1883 0.0024  -0.0388 0.0679  235 GLY A CA  
1565 C C   . GLY A 235 ? 0.2195 0.2699 0.1778 0.0021  -0.0304 0.0698  235 GLY A C   
1566 O O   . GLY A 235 ? 0.2856 0.3329 0.2403 0.0008  -0.0248 0.0669  235 GLY A O   
1567 N N   . TYR A 236 ? 0.2194 0.2692 0.1897 0.0035  -0.0300 0.0745  236 TYR A N   
1568 C CA  . TYR A 236 ? 0.2102 0.2537 0.1878 0.0038  -0.0233 0.0753  236 TYR A CA  
1569 C C   . TYR A 236 ? 0.2233 0.2649 0.2097 0.0037  -0.0217 0.0705  236 TYR A C   
1570 O O   . TYR A 236 ? 0.2136 0.2483 0.2046 0.0051  -0.0171 0.0708  236 TYR A O   
1571 C CB  . TYR A 236 ? 0.2289 0.2704 0.2115 0.0066  -0.0224 0.0837  236 TYR A CB  
1572 C CG  . TYR A 236 ? 0.2205 0.2643 0.1935 0.0071  -0.0236 0.0894  236 TYR A CG  
1573 C CD1 . TYR A 236 ? 0.2394 0.2795 0.2072 0.0059  -0.0185 0.0907  236 TYR A CD1 
1574 C CD2 . TYR A 236 ? 0.2328 0.2825 0.2020 0.0089  -0.0301 0.0939  236 TYR A CD2 
1575 C CE1 . TYR A 236 ? 0.2443 0.2867 0.2031 0.0072  -0.0179 0.0972  236 TYR A CE1 
1576 C CE2 . TYR A 236 ? 0.2656 0.3164 0.2228 0.0104  -0.0307 0.0995  236 TYR A CE2 
1577 C CZ  . TYR A 236 ? 0.2461 0.2933 0.1980 0.0098  -0.0236 0.1013  236 TYR A CZ  
1578 O OH  . TYR A 236 ? 0.2834 0.3314 0.2238 0.0120  -0.0224 0.1072  236 TYR A OH  
1579 N N   . ASP A 237 ? 0.1876 0.2341 0.1756 0.0024  -0.0255 0.0661  237 ASP A N   
1580 C CA  . ASP A 237 ? 0.1751 0.2207 0.1714 0.0024  -0.0235 0.0623  237 ASP A CA  
1581 C C   . ASP A 237 ? 0.1803 0.2262 0.1700 -0.0007 -0.0241 0.0550  237 ASP A C   
1582 O O   . ASP A 237 ? 0.2137 0.2642 0.2010 -0.0023 -0.0297 0.0525  237 ASP A O   
1583 C CB  . ASP A 237 ? 0.1735 0.2258 0.1828 0.0039  -0.0278 0.0664  237 ASP A CB  
1584 C CG  . ASP A 237 ? 0.1989 0.2522 0.2187 0.0041  -0.0255 0.0641  237 ASP A CG  
1585 O OD1 . ASP A 237 ? 0.2023 0.2499 0.2176 0.0039  -0.0203 0.0593  237 ASP A OD1 
1586 O OD2 . ASP A 237 ? 0.2144 0.2744 0.2483 0.0049  -0.0291 0.0684  237 ASP A OD2 
1587 N N   . ILE A 238 ? 0.1588 0.1988 0.1454 -0.0013 -0.0190 0.0513  238 ILE A N   
1588 C CA  . ILE A 238 ? 0.1691 0.2090 0.1489 -0.0039 -0.0186 0.0456  238 ILE A CA  
1589 C C   . ILE A 238 ? 0.1547 0.1914 0.1385 -0.0042 -0.0159 0.0412  238 ILE A C   
1590 O O   . ILE A 238 ? 0.1831 0.2133 0.1679 -0.0027 -0.0123 0.0417  238 ILE A O   
1591 C CB  . ILE A 238 ? 0.1913 0.2281 0.1645 -0.0048 -0.0155 0.0468  238 ILE A CB  
1592 C CG1 . ILE A 238 ? 0.1940 0.2343 0.1610 -0.0039 -0.0174 0.0517  238 ILE A CG1 
1593 C CG2 . ILE A 238 ? 0.1824 0.2189 0.1519 -0.0068 -0.0136 0.0416  238 ILE A CG2 
1594 C CD1 . ILE A 238 ? 0.2088 0.2469 0.1724 -0.0044 -0.0132 0.0554  238 ILE A CD1 
1595 N N   . PRO A 239 ? 0.1635 0.2032 0.1483 -0.0057 -0.0177 0.0368  239 PRO A N   
1596 C CA  . PRO A 239 ? 0.1594 0.1960 0.1474 -0.0056 -0.0148 0.0335  239 PRO A CA  
1597 C C   . PRO A 239 ? 0.1712 0.2043 0.1527 -0.0072 -0.0127 0.0299  239 PRO A C   
1598 O O   . PRO A 239 ? 0.1721 0.2073 0.1483 -0.0086 -0.0133 0.0290  239 PRO A O   
1599 C CB  . PRO A 239 ? 0.1894 0.2308 0.1826 -0.0070 -0.0184 0.0309  239 PRO A CB  
1600 C CG  . PRO A 239 ? 0.2834 0.3293 0.2751 -0.0079 -0.0245 0.0321  239 PRO A CG  
1601 C CD  . PRO A 239 ? 0.2215 0.2666 0.2061 -0.0068 -0.0236 0.0358  239 PRO A CD  
1602 N N   . LEU A 240 ? 0.1468 0.1741 0.1286 -0.0063 -0.0100 0.0286  240 LEU A N   
1603 C CA  . LEU A 240 ? 0.1559 0.1798 0.1343 -0.0080 -0.0091 0.0258  240 LEU A CA  
1604 C C   . LEU A 240 ? 0.1546 0.1768 0.1344 -0.0074 -0.0082 0.0226  240 LEU A C   
1605 O O   . LEU A 240 ? 0.1714 0.1874 0.1499 -0.0049 -0.0066 0.0231  240 LEU A O   
1606 C CB  . LEU A 240 ? 0.1628 0.1790 0.1387 -0.0077 -0.0088 0.0275  240 LEU A CB  
1607 C CG  . LEU A 240 ? 0.1681 0.1842 0.1438 -0.0079 -0.0091 0.0319  240 LEU A CG  
1608 C CD1 . LEU A 240 ? 0.2042 0.2102 0.1786 -0.0079 -0.0096 0.0327  240 LEU A CD1 
1609 C CD2 . LEU A 240 ? 0.1863 0.2094 0.1617 -0.0101 -0.0091 0.0333  240 LEU A CD2 
1610 N N   . MET A 241 ? 0.1490 0.1754 0.1301 -0.0091 -0.0088 0.0197  241 MET A N   
1611 C CA  . MET A 241 ? 0.1576 0.1825 0.1406 -0.0087 -0.0079 0.0172  241 MET A CA  
1612 C C   . MET A 241 ? 0.1430 0.1649 0.1236 -0.0099 -0.0080 0.0157  241 MET A C   
1613 O O   . MET A 241 ? 0.1480 0.1737 0.1296 -0.0116 -0.0081 0.0146  241 MET A O   
1614 C CB  . MET A 241 ? 0.1482 0.1782 0.1347 -0.0100 -0.0091 0.0145  241 MET A CB  
1615 C CG  . MET A 241 ? 0.1627 0.1912 0.1533 -0.0095 -0.0078 0.0129  241 MET A CG  
1616 S SD  . MET A 241 ? 0.1708 0.2029 0.1668 -0.0110 -0.0099 0.0094  241 MET A SD  
1617 C CE  . MET A 241 ? 0.2124 0.2468 0.2182 -0.0107 -0.0115 0.0127  241 MET A CE  
1618 N N   . ILE A 242 ? 0.1297 0.1443 0.1072 -0.0085 -0.0082 0.0159  242 ILE A N   
1619 C CA  . ILE A 242 ? 0.1426 0.1537 0.1192 -0.0100 -0.0104 0.0150  242 ILE A CA  
1620 C C   . ILE A 242 ? 0.1597 0.1709 0.1375 -0.0093 -0.0102 0.0131  242 ILE A C   
1621 O O   . ILE A 242 ? 0.1611 0.1687 0.1360 -0.0065 -0.0087 0.0132  242 ILE A O   
1622 C CB  . ILE A 242 ? 0.1511 0.1517 0.1212 -0.0089 -0.0128 0.0155  242 ILE A CB  
1623 C CG1 . ILE A 242 ? 0.1673 0.1671 0.1371 -0.0091 -0.0126 0.0179  242 ILE A CG1 
1624 C CG2 . ILE A 242 ? 0.1718 0.1688 0.1429 -0.0112 -0.0174 0.0147  242 ILE A CG2 
1625 C CD1 . ILE A 242 ? 0.2068 0.1939 0.1689 -0.0068 -0.0144 0.0178  242 ILE A CD1 
1626 N N   . GLN A 243 ? 0.1504 0.1657 0.1331 -0.0114 -0.0111 0.0124  243 GLN A N   
1627 C CA  . GLN A 243 ? 0.1542 0.1699 0.1394 -0.0107 -0.0110 0.0112  243 GLN A CA  
1628 C C   . GLN A 243 ? 0.1737 0.1906 0.1640 -0.0127 -0.0137 0.0119  243 GLN A C   
1629 O O   . GLN A 243 ? 0.1954 0.2173 0.1911 -0.0146 -0.0130 0.0133  243 GLN A O   
1630 C CB  . GLN A 243 ? 0.1404 0.1625 0.1305 -0.0108 -0.0081 0.0095  243 GLN A CB  
1631 C CG  . GLN A 243 ? 0.1672 0.1896 0.1565 -0.0096 -0.0067 0.0095  243 GLN A CG  
1632 C CD  . GLN A 243 ? 0.1587 0.1852 0.1528 -0.0102 -0.0060 0.0072  243 GLN A CD  
1633 O OE1 . GLN A 243 ? 0.1888 0.2184 0.1822 -0.0112 -0.0060 0.0053  243 GLN A OE1 
1634 N NE2 . GLN A 243 ? 0.1586 0.1842 0.1570 -0.0092 -0.0053 0.0076  243 GLN A NE2 
1635 N N   . ASP A 244 ? 0.1479 0.1610 0.1375 -0.0118 -0.0164 0.0118  244 ASP A N   
1636 C CA  . ASP A 244 ? 0.1463 0.1620 0.1441 -0.0137 -0.0196 0.0133  244 ASP A CA  
1637 C C   . ASP A 244 ? 0.1614 0.1836 0.1669 -0.0129 -0.0160 0.0129  244 ASP A C   
1638 O O   . ASP A 244 ? 0.1560 0.1774 0.1589 -0.0108 -0.0135 0.0113  244 ASP A O   
1639 C CB  . ASP A 244 ? 0.1708 0.1777 0.1638 -0.0137 -0.0269 0.0137  244 ASP A CB  
1640 C CG  . ASP A 244 ? 0.1955 0.1959 0.1788 -0.0100 -0.0271 0.0126  244 ASP A CG  
1641 O OD1 . ASP A 244 ? 0.1905 0.1910 0.1695 -0.0074 -0.0216 0.0119  244 ASP A OD1 
1642 O OD2 . ASP A 244 ? 0.2086 0.2030 0.1884 -0.0095 -0.0334 0.0131  244 ASP A OD2 
1643 N N   . ARG A 245 ? 0.1459 0.1746 0.1621 -0.0142 -0.0153 0.0150  245 ARG A N   
1644 C CA  . ARG A 245 ? 0.1254 0.1596 0.1485 -0.0126 -0.0108 0.0145  245 ARG A CA  
1645 C C   . ARG A 245 ? 0.1377 0.1766 0.1740 -0.0134 -0.0124 0.0185  245 ARG A C   
1646 O O   . ARG A 245 ? 0.1486 0.1885 0.1907 -0.0159 -0.0163 0.0219  245 ARG A O   
1647 C CB  . ARG A 245 ? 0.1464 0.1849 0.1683 -0.0118 -0.0046 0.0129  245 ARG A CB  
1648 C CG  . ARG A 245 ? 0.1475 0.1826 0.1594 -0.0112 -0.0038 0.0093  245 ARG A CG  
1649 C CD  . ARG A 245 ? 0.1535 0.1865 0.1659 -0.0096 -0.0029 0.0066  245 ARG A CD  
1650 N NE  . ARG A 245 ? 0.1787 0.2094 0.1862 -0.0094 -0.0028 0.0041  245 ARG A NE  
1651 C CZ  . ARG A 245 ? 0.1344 0.1616 0.1393 -0.0092 -0.0043 0.0051  245 ARG A CZ  
1652 N NH1 . ARG A 245 ? 0.1590 0.1829 0.1611 -0.0088 -0.0064 0.0076  245 ARG A NH1 
1653 N NH2 . ARG A 245 ? 0.1578 0.1845 0.1633 -0.0091 -0.0039 0.0038  245 ARG A NH2 
1654 N N   . SER A 246 ? 0.1455 0.1872 0.1881 -0.0113 -0.0098 0.0185  246 SER A N   
1655 C CA  . SER A 246 ? 0.1234 0.1716 0.1815 -0.0111 -0.0095 0.0230  246 SER A CA  
1656 C C   . SER A 246 ? 0.1336 0.1861 0.1959 -0.0075 -0.0007 0.0220  246 SER A C   
1657 O O   . SER A 246 ? 0.1351 0.1838 0.1889 -0.0055 0.0023  0.0171  246 SER A O   
1658 C CB  . SER A 246 ? 0.1377 0.1836 0.2003 -0.0113 -0.0164 0.0251  246 SER A CB  
1659 O OG  . SER A 246 ? 0.1726 0.2123 0.2289 -0.0140 -0.0254 0.0255  246 SER A OG  
1660 N N   . PHE A 247 ? 0.1182 0.1782 0.1947 -0.0064 0.0032  0.0269  247 PHE A N   
1661 C CA  . PHE A 247 ? 0.1064 0.1693 0.1849 -0.0016 0.0130  0.0260  247 PHE A CA  
1662 C C   . PHE A 247 ? 0.1184 0.1878 0.2155 0.0007  0.0152  0.0317  247 PHE A C   
1663 O O   . PHE A 247 ? 0.1277 0.2020 0.2393 -0.0021 0.0096  0.0380  247 PHE A O   
1664 C CB  . PHE A 247 ? 0.1380 0.2042 0.2132 -0.0005 0.0197  0.0275  247 PHE A CB  
1665 C CG  . PHE A 247 ? 0.1233 0.1840 0.1815 -0.0025 0.0175  0.0228  247 PHE A CG  
1666 C CD1 . PHE A 247 ? 0.1405 0.2005 0.1980 -0.0070 0.0111  0.0249  247 PHE A CD1 
1667 C CD2 . PHE A 247 ? 0.1524 0.2078 0.1960 0.0001  0.0207  0.0162  247 PHE A CD2 
1668 C CE1 . PHE A 247 ? 0.1400 0.1953 0.1835 -0.0083 0.0093  0.0213  247 PHE A CE1 
1669 C CE2 . PHE A 247 ? 0.1641 0.2153 0.1945 -0.0019 0.0177  0.0127  247 PHE A CE2 
1670 C CZ  . PHE A 247 ? 0.1468 0.1985 0.1775 -0.0058 0.0127  0.0155  247 PHE A CZ  
1671 N N   . ARG A 248 ? 0.1340 0.2025 0.2311 0.0059  0.0228  0.0294  248 ARG A N   
1672 C CA  . ARG A 248 ? 0.1293 0.2047 0.2449 0.0096  0.0278  0.0355  248 ARG A CA  
1673 C C   . ARG A 248 ? 0.1121 0.1948 0.2347 0.0125  0.0373  0.0409  248 ARG A C   
1674 O O   . ARG A 248 ? 0.1488 0.2294 0.2583 0.0126  0.0408  0.0386  248 ARG A O   
1675 C CB  . ARG A 248 ? 0.1386 0.2088 0.2513 0.0147  0.0328  0.0309  248 ARG A CB  
1676 C CG  . ARG A 248 ? 0.1595 0.2225 0.2658 0.0123  0.0249  0.0266  248 ARG A CG  
1677 C CD  . ARG A 248 ? 0.1592 0.2180 0.2685 0.0173  0.0295  0.0242  248 ARG A CD  
1678 N NE  . ARG A 248 ? 0.1698 0.2217 0.2732 0.0151  0.0231  0.0210  248 ARG A NE  
1679 C CZ  . ARG A 248 ? 0.2081 0.2514 0.2985 0.0149  0.0233  0.0139  248 ARG A CZ  
1680 N NH1 . ARG A 248 ? 0.2119 0.2508 0.2912 0.0166  0.0283  0.0079  248 ARG A NH1 
1681 N NH2 . ARG A 248 ? 0.2486 0.2871 0.3373 0.0132  0.0183  0.0133  248 ARG A NH2 
1682 N N   . SER A 249 ? 0.1187 0.2102 0.2629 0.0155  0.0421  0.0492  249 SER A N   
1683 C CA  . SER A 249 ? 0.1275 0.2270 0.2814 0.0192  0.0528  0.0565  249 SER A CA  
1684 C C   . SER A 249 ? 0.1617 0.2552 0.2958 0.0266  0.0654  0.0510  249 SER A C   
1685 O O   . SER A 249 ? 0.1751 0.2726 0.3084 0.0294  0.0739  0.0558  249 SER A O   
1686 C CB  . SER A 249 ? 0.1441 0.2548 0.3276 0.0218  0.0563  0.0673  249 SER A CB  
1687 O OG  . SER A 249 ? 0.1624 0.2699 0.3450 0.0288  0.0634  0.0644  249 SER A OG  
1688 N N   . ASP A 250 ? 0.1498 0.2327 0.2671 0.0299  0.0664  0.0413  250 ASP A N   
1689 C CA  . ASP A 250 ? 0.1516 0.2256 0.2468 0.0368  0.0760  0.0345  250 ASP A CA  
1690 C C   . ASP A 250 ? 0.1662 0.2321 0.2378 0.0330  0.0700  0.0264  250 ASP A C   
1691 O O   . ASP A 250 ? 0.2156 0.2719 0.2659 0.0377  0.0745  0.0192  250 ASP A O   
1692 C CB  . ASP A 250 ? 0.1665 0.2319 0.2576 0.0428  0.0799  0.0282  250 ASP A CB  
1693 C CG  . ASP A 250 ? 0.1997 0.2573 0.2853 0.0375  0.0684  0.0206  250 ASP A CG  
1694 O OD1 . ASP A 250 ? 0.1740 0.2326 0.2576 0.0300  0.0582  0.0199  250 ASP A OD1 
1695 O OD2 . ASP A 250 ? 0.2272 0.2776 0.3118 0.0416  0.0705  0.0161  250 ASP A OD2 
1696 N N   . GLY A 251 ? 0.1544 0.2232 0.2291 0.0249  0.0596  0.0278  251 GLY A N   
1697 C CA  . GLY A 251 ? 0.1580 0.2207 0.2139 0.0211  0.0538  0.0218  251 GLY A CA  
1698 C C   . GLY A 251 ? 0.1738 0.2274 0.2195 0.0183  0.0458  0.0130  251 GLY A C   
1699 O O   . GLY A 251 ? 0.1706 0.2203 0.2043 0.0147  0.0400  0.0090  251 GLY A O   
1700 N N   . SER A 252 ? 0.1630 0.2139 0.2153 0.0199  0.0453  0.0109  252 SER A N   
1701 C CA  . SER A 252 ? 0.1460 0.1887 0.1910 0.0173  0.0383  0.0040  252 SER A CA  
1702 C C   . SER A 252 ? 0.1721 0.2176 0.2218 0.0106  0.0290  0.0066  252 SER A C   
1703 O O   . SER A 252 ? 0.1523 0.2047 0.2135 0.0083  0.0266  0.0132  252 SER A O   
1704 C CB  . SER A 252 ? 0.1763 0.2147 0.2278 0.0210  0.0406  0.0018  252 SER A CB  
1705 O OG  . SER A 252 ? 0.1714 0.2174 0.2418 0.0207  0.0402  0.0092  252 SER A OG  
1706 N N   . LEU A 253 ? 0.1608 0.2000 0.2011 0.0079  0.0236  0.0015  253 LEU A N   
1707 C CA  . LEU A 253 ? 0.1459 0.1859 0.1883 0.0033  0.0163  0.0037  253 LEU A CA  
1708 C C   . LEU A 253 ? 0.1315 0.1731 0.1859 0.0035  0.0141  0.0076  253 LEU A C   
1709 O O   . LEU A 253 ? 0.1650 0.2034 0.2233 0.0061  0.0161  0.0060  253 LEU A O   
1710 C CB  . LEU A 253 ? 0.1759 0.2094 0.2092 0.0015  0.0126  -0.0013 253 LEU A CB  
1711 C CG  . LEU A 253 ? 0.2207 0.2527 0.2425 0.0001  0.0116  -0.0042 253 LEU A CG  
1712 C CD1 . LEU A 253 ? 0.2479 0.2745 0.2663 -0.0016 0.0076  -0.0081 253 LEU A CD1 
1713 C CD2 . LEU A 253 ? 0.2072 0.2435 0.2283 -0.0026 0.0093  0.0001  253 LEU A CD2 
1714 N N   . SER A 254 ? 0.1328 0.1778 0.1919 0.0008  0.0090  0.0126  254 SER A N   
1715 C CA  . SER A 254 ? 0.1483 0.1942 0.2167 0.0010  0.0050  0.0167  254 SER A CA  
1716 C C   . SER A 254 ? 0.1413 0.1814 0.2011 -0.0008 -0.0009 0.0160  254 SER A C   
1717 O O   . SER A 254 ? 0.1603 0.1986 0.2119 -0.0033 -0.0044 0.0158  254 SER A O   
1718 C CB  . SER A 254 ? 0.1526 0.2052 0.2327 -0.0004 0.0019  0.0230  254 SER A CB  
1719 O OG  . SER A 254 ? 0.1564 0.2095 0.2452 0.0000  -0.0032 0.0270  254 SER A OG  
1720 N N   . TYR A 255 ? 0.1451 0.1818 0.2066 0.0010  -0.0011 0.0164  255 TYR A N   
1721 C CA  . TYR A 255 ? 0.1388 0.1700 0.1922 0.0006  -0.0051 0.0173  255 TYR A CA  
1722 C C   . TYR A 255 ? 0.1614 0.1922 0.2217 0.0029  -0.0073 0.0217  255 TYR A C   
1723 O O   . TYR A 255 ? 0.1670 0.2002 0.2379 0.0049  -0.0037 0.0221  255 TYR A O   
1724 C CB  . TYR A 255 ? 0.1304 0.1573 0.1786 0.0008  -0.0016 0.0136  255 TYR A CB  
1725 C CG  . TYR A 255 ? 0.1344 0.1565 0.1746 0.0012  -0.0037 0.0159  255 TYR A CG  
1726 C CD1 . TYR A 255 ? 0.1426 0.1630 0.1726 -0.0001 -0.0057 0.0156  255 TYR A CD1 
1727 C CD2 . TYR A 255 ? 0.1397 0.1587 0.1824 0.0036  -0.0031 0.0193  255 TYR A CD2 
1728 C CE1 . TYR A 255 ? 0.1821 0.1971 0.2032 0.0018  -0.0063 0.0183  255 TYR A CE1 
1729 C CE2 . TYR A 255 ? 0.1359 0.1502 0.1700 0.0053  -0.0035 0.0227  255 TYR A CE2 
1730 C CZ  . TYR A 255 ? 0.1533 0.1654 0.1761 0.0046  -0.0048 0.0220  255 TYR A CZ  
1731 O OH  . TYR A 255 ? 0.1634 0.1699 0.1761 0.0077  -0.0038 0.0256  255 TYR A OH  
1732 N N   . PRO A 256 ? 0.1470 0.1741 0.2006 0.0032  -0.0132 0.0251  256 PRO A N   
1733 C CA  . PRO A 256 ? 0.1656 0.1928 0.2252 0.0054  -0.0170 0.0301  256 PRO A CA  
1734 C C   . PRO A 256 ? 0.1682 0.1937 0.2336 0.0084  -0.0119 0.0312  256 PRO A C   
1735 O O   . PRO A 256 ? 0.1679 0.1891 0.2280 0.0090  -0.0081 0.0297  256 PRO A O   
1736 C CB  . PRO A 256 ? 0.1887 0.2089 0.2333 0.0059  -0.0241 0.0323  256 PRO A CB  
1737 C CG  . PRO A 256 ? 0.2946 0.3116 0.3273 0.0040  -0.0237 0.0285  256 PRO A CG  
1738 C CD  . PRO A 256 ? 0.1677 0.1898 0.2068 0.0020  -0.0172 0.0244  256 PRO A CD  
1739 N N   . GLU A 257 ? 0.1679 0.1968 0.2461 0.0103  -0.0124 0.0348  257 GLU A N   
1740 C CA  . GLU A 257 ? 0.1512 0.1776 0.2355 0.0135  -0.0088 0.0371  257 GLU A CA  
1741 C C   . GLU A 257 ? 0.1582 0.1796 0.2342 0.0158  -0.0133 0.0427  257 GLU A C   
1742 O O   . GLU A 257 ? 0.1631 0.1808 0.2410 0.0184  -0.0097 0.0453  257 GLU A O   
1743 C CB  . GLU A 257 ? 0.1756 0.2074 0.2774 0.0155  -0.0064 0.0389  257 GLU A CB  
1744 C CG  . GLU A 257 ? 0.1956 0.2315 0.3051 0.0166  -0.0135 0.0459  257 GLU A CG  
1745 C CD  . GLU A 257 ? 0.1890 0.2313 0.3187 0.0194  -0.0100 0.0490  257 GLU A CD  
1746 O OE1 . GLU A 257 ? 0.1993 0.2466 0.3366 0.0191  -0.0051 0.0465  257 GLU A OE1 
1747 O OE2 . GLU A 257 ? 0.2263 0.2681 0.3638 0.0225  -0.0112 0.0543  257 GLU A OE2 
1748 N N   . ASN A 258 ? 0.1625 0.1826 0.2287 0.0152  -0.0215 0.0449  258 ASN A N   
1749 C CA  . ASN A 258 ? 0.1713 0.1854 0.2267 0.0185  -0.0271 0.0505  258 ASN A CA  
1750 C C   . ASN A 258 ? 0.1759 0.1869 0.2182 0.0167  -0.0369 0.0496  258 ASN A C   
1751 O O   . ASN A 258 ? 0.1996 0.2146 0.2459 0.0128  -0.0387 0.0459  258 ASN A O   
1752 C CB  . ASN A 258 ? 0.1803 0.1978 0.2499 0.0210  -0.0292 0.0564  258 ASN A CB  
1753 C CG  . ASN A 258 ? 0.2029 0.2136 0.2621 0.0257  -0.0320 0.0630  258 ASN A CG  
1754 O OD1 . ASN A 258 ? 0.2006 0.2035 0.2391 0.0274  -0.0359 0.0638  258 ASN A OD1 
1755 N ND2 . ASN A 258 ? 0.2146 0.2273 0.2872 0.0286  -0.0294 0.0680  258 ASN A ND2 
1756 N N   . THR A 259 ? 0.2101 0.2128 0.2357 0.0200  -0.0432 0.0531  259 THR A N   
1757 C CA  . THR A 259 ? 0.2318 0.2284 0.2431 0.0189  -0.0548 0.0521  259 THR A CA  
1758 C C   . THR A 259 ? 0.2072 0.2095 0.2336 0.0166  -0.0656 0.0554  259 THR A C   
1759 O O   . THR A 259 ? 0.2189 0.2295 0.2651 0.0172  -0.0633 0.0594  259 THR A O   
1760 C CB  . THR A 259 ? 0.2308 0.2142 0.2156 0.0245  -0.0576 0.0545  259 THR A CB  
1761 O OG1 . THR A 259 ? 0.2471 0.2303 0.2347 0.0288  -0.0573 0.0612  259 THR A OG1 
1762 C CG2 . THR A 259 ? 0.2345 0.2135 0.2075 0.0267  -0.0463 0.0524  259 THR A CG2 
1763 N N   . ASN A 260 ? 0.2522 0.2500 0.2708 0.0140  -0.0776 0.0539  260 ASN A N   
1764 C CA  . ASN A 260 ? 0.2505 0.2523 0.2829 0.0115  -0.0909 0.0580  260 ASN A CA  
1765 C C   . ASN A 260 ? 0.2951 0.2823 0.3027 0.0133  -0.1057 0.0579  260 ASN A C   
1766 O O   . ASN A 260 ? 0.3624 0.3407 0.3543 0.0113  -0.1108 0.0527  260 ASN A O   
1767 C CB  . ASN A 260 ? 0.3107 0.3219 0.3633 0.0053  -0.0928 0.0565  260 ASN A CB  
1768 C CG  . ASN A 260 ? 0.4247 0.4503 0.5030 0.0046  -0.0801 0.0579  260 ASN A CG  
1769 O OD1 . ASN A 260 ? 0.4440 0.4782 0.5429 0.0055  -0.0807 0.0636  260 ASN A OD1 
1770 N ND2 . ASN A 260 ? 0.4262 0.4535 0.5024 0.0036  -0.0687 0.0528  260 ASN A ND2 
1771 N N   . PRO A 261 ? 0.3145 0.2976 0.3164 0.0174  -0.1132 0.0634  261 PRO A N   
1772 C CA  . PRO A 261 ? 0.2662 0.2582 0.2856 0.0203  -0.1084 0.0703  261 PRO A CA  
1773 C C   . PRO A 261 ? 0.2865 0.2788 0.3019 0.0246  -0.0912 0.0703  261 PRO A C   
1774 O O   . PRO A 261 ? 0.2849 0.2679 0.2782 0.0272  -0.0852 0.0670  261 PRO A O   
1775 C CB  . PRO A 261 ? 0.3471 0.3304 0.3510 0.0238  -0.1199 0.0734  261 PRO A CB  
1776 C CG  . PRO A 261 ? 0.4411 0.4105 0.4185 0.0227  -0.1284 0.0664  261 PRO A CG  
1777 C CD  . PRO A 261 ? 0.3897 0.3569 0.3618 0.0202  -0.1231 0.0608  261 PRO A CD  
1778 N N   . PRO A 262 ? 0.2355 0.2380 0.2737 0.0255  -0.0834 0.0744  262 PRO A N   
1779 C CA  . PRO A 262 ? 0.2421 0.2456 0.2824 0.0280  -0.0675 0.0736  262 PRO A CA  
1780 C C   . PRO A 262 ? 0.2324 0.2268 0.2554 0.0345  -0.0648 0.0787  262 PRO A C   
1781 O O   . PRO A 262 ? 0.2805 0.2711 0.2976 0.0381  -0.0733 0.0849  262 PRO A O   
1782 C CB  . PRO A 262 ? 0.2339 0.2496 0.3045 0.0272  -0.0621 0.0763  262 PRO A CB  
1783 C CG  . PRO A 262 ? 0.2354 0.2551 0.3169 0.0271  -0.0756 0.0825  262 PRO A CG  
1784 C CD  . PRO A 262 ? 0.2635 0.2774 0.3296 0.0238  -0.0886 0.0796  262 PRO A CD  
1785 N N   . ALA A 263 ? 0.2455 0.2369 0.2619 0.0360  -0.0525 0.0769  263 ALA A N   
1786 C CA  . ALA A 263 ? 0.2477 0.2332 0.2553 0.0421  -0.0458 0.0831  263 ALA A CA  
1787 C C   . ALA A 263 ? 0.2366 0.2293 0.2689 0.0429  -0.0408 0.0880  263 ALA A C   
1788 O O   . ALA A 263 ? 0.2404 0.2420 0.2947 0.0390  -0.0393 0.0848  263 ALA A O   
1789 C CB  . ALA A 263 ? 0.2771 0.2593 0.2771 0.0425  -0.0340 0.0803  263 ALA A CB  
1790 N N   . PRO A 264 ? 0.2790 0.2672 0.3075 0.0485  -0.0377 0.0962  264 PRO A N   
1791 C CA  . PRO A 264 ? 0.2730 0.2667 0.3255 0.0496  -0.0322 0.1009  264 PRO A CA  
1792 C C   . PRO A 264 ? 0.2396 0.2356 0.3074 0.0471  -0.0196 0.0969  264 PRO A C   
1793 O O   . PRO A 264 ? 0.2618 0.2613 0.3507 0.0473  -0.0152 0.0985  264 PRO A O   
1794 C CB  . PRO A 264 ? 0.3307 0.3173 0.3714 0.0567  -0.0327 0.1116  264 PRO A CB  
1795 C CG  . PRO A 264 ? 0.3765 0.3536 0.3877 0.0597  -0.0321 0.1114  264 PRO A CG  
1796 C CD  . PRO A 264 ? 0.3215 0.2988 0.3228 0.0550  -0.0399 0.1022  264 PRO A CD  
1797 N N   . VAL A 265 ? 0.2465 0.2397 0.3040 0.0452  -0.0144 0.0921  265 VAL A N   
1798 C CA  . VAL A 265 ? 0.2276 0.2226 0.2986 0.0420  -0.0049 0.0874  265 VAL A CA  
1799 C C   . VAL A 265 ? 0.1840 0.1854 0.2657 0.0367  -0.0066 0.0781  265 VAL A C   
1800 O O   . VAL A 265 ? 0.1989 0.2021 0.2709 0.0344  -0.0126 0.0739  265 VAL A O   
1801 C CB  . VAL A 265 ? 0.2533 0.2437 0.3095 0.0423  0.0003  0.0870  265 VAL A CB  
1802 C CG1 . VAL A 265 ? 0.2374 0.2297 0.3079 0.0381  0.0078  0.0819  265 VAL A CG1 
1803 C CG2 . VAL A 265 ? 0.2698 0.2535 0.3139 0.0490  0.0037  0.0976  265 VAL A CG2 
1804 N N   . ASN A 266 ? 0.1830 0.1867 0.2835 0.0351  -0.0011 0.0748  266 ASN A N   
1805 C CA  . ASN A 266 ? 0.1767 0.1854 0.2852 0.0313  -0.0010 0.0663  266 ASN A CA  
1806 C C   . ASN A 266 ? 0.1599 0.1661 0.2764 0.0290  0.0060  0.0599  266 ASN A C   
1807 O O   . ASN A 266 ? 0.1709 0.1733 0.2993 0.0306  0.0102  0.0620  266 ASN A O   
1808 C CB  . ASN A 266 ? 0.1817 0.1953 0.3053 0.0331  -0.0030 0.0683  266 ASN A CB  
1809 C CG  . ASN A 266 ? 0.2044 0.2219 0.3231 0.0339  -0.0125 0.0732  266 ASN A CG  
1810 O OD1 . ASN A 266 ? 0.2033 0.2244 0.3167 0.0309  -0.0173 0.0697  266 ASN A OD1 
1811 N ND2 . ASN A 266 ? 0.1994 0.2154 0.3197 0.0379  -0.0160 0.0817  266 ASN A ND2 
1812 N N   . PRO A 267 ? 0.1655 0.1730 0.2762 0.0252  0.0065  0.0522  267 PRO A N   
1813 C CA  . PRO A 267 ? 0.1665 0.1767 0.2628 0.0230  0.0022  0.0499  267 PRO A CA  
1814 C C   . PRO A 267 ? 0.1508 0.1568 0.2326 0.0244  0.0013  0.0548  267 PRO A C   
1815 O O   . PRO A 267 ? 0.1812 0.1833 0.2656 0.0263  0.0058  0.0593  267 PRO A O   
1816 C CB  . PRO A 267 ? 0.1792 0.1900 0.2751 0.0192  0.0051  0.0413  267 PRO A CB  
1817 C CG  . PRO A 267 ? 0.1662 0.1747 0.2761 0.0198  0.0096  0.0378  267 PRO A CG  
1818 C CD  . PRO A 267 ? 0.1800 0.1848 0.2983 0.0230  0.0110  0.0449  267 PRO A CD  
1819 N N   . SER A 268 ? 0.1602 0.1662 0.2268 0.0240  -0.0039 0.0544  268 SER A N   
1820 C CA  . SER A 268 ? 0.1755 0.1759 0.2245 0.0265  -0.0040 0.0582  268 SER A CA  
1821 C C   . SER A 268 ? 0.1770 0.1770 0.2143 0.0238  -0.0050 0.0526  268 SER A C   
1822 O O   . SER A 268 ? 0.1879 0.1914 0.2253 0.0206  -0.0097 0.0477  268 SER A O   
1823 C CB  . SER A 268 ? 0.2121 0.2089 0.2492 0.0304  -0.0111 0.0640  268 SER A CB  
1824 O OG  . SER A 268 ? 0.2132 0.2023 0.2284 0.0341  -0.0110 0.0668  268 SER A OG  
1825 N N   . VAL A 269 ? 0.1746 0.1706 0.2032 0.0254  -0.0001 0.0544  269 VAL A N   
1826 C CA  . VAL A 269 ? 0.1778 0.1713 0.1917 0.0247  -0.0010 0.0511  269 VAL A CA  
1827 C C   . VAL A 269 ? 0.1846 0.1736 0.1815 0.0262  -0.0097 0.0507  269 VAL A C   
1828 O O   . VAL A 269 ? 0.1993 0.1845 0.1900 0.0297  -0.0140 0.0554  269 VAL A O   
1829 C CB  . VAL A 269 ? 0.1831 0.1726 0.1908 0.0283  0.0067  0.0558  269 VAL A CB  
1830 C CG1 . VAL A 269 ? 0.2168 0.1991 0.2109 0.0354  0.0080  0.0642  269 VAL A CG1 
1831 C CG2 . VAL A 269 ? 0.1938 0.1818 0.1905 0.0274  0.0075  0.0520  269 VAL A CG2 
1832 N N   . GLN A 270 ? 0.1980 0.1866 0.1877 0.0233  -0.0132 0.0453  270 GLN A N   
1833 C CA  . GLN A 270 ? 0.2072 0.1891 0.1796 0.0242  -0.0220 0.0440  270 GLN A CA  
1834 C C   . GLN A 270 ? 0.2084 0.1834 0.1640 0.0263  -0.0186 0.0423  270 GLN A C   
1835 O O   . GLN A 270 ? 0.2206 0.2004 0.1841 0.0236  -0.0128 0.0396  270 GLN A O   
1836 C CB  . GLN A 270 ? 0.2084 0.1967 0.1917 0.0183  -0.0287 0.0394  270 GLN A CB  
1837 C CG  . GLN A 270 ? 0.2477 0.2291 0.2170 0.0175  -0.0394 0.0374  270 GLN A CG  
1838 C CD  . GLN A 270 ? 0.1953 0.1847 0.1808 0.0117  -0.0456 0.0352  270 GLN A CD  
1839 O OE1 . GLN A 270 ? 0.2318 0.2237 0.2257 0.0110  -0.0531 0.0382  270 GLN A OE1 
1840 N NE2 . GLN A 270 ? 0.2098 0.2034 0.2005 0.0079  -0.0426 0.0312  270 GLN A NE2 
1841 N N   . PRO A 271 ? 0.2334 0.1964 0.1652 0.0316  -0.0220 0.0437  271 PRO A N   
1842 C CA  . PRO A 271 ? 0.2501 0.2057 0.1658 0.0352  -0.0163 0.0429  271 PRO A CA  
1843 C C   . PRO A 271 ? 0.2447 0.1983 0.1558 0.0314  -0.0213 0.0362  271 PRO A C   
1844 O O   . PRO A 271 ? 0.2813 0.2240 0.1725 0.0355  -0.0207 0.0350  271 PRO A O   
1845 C CB  . PRO A 271 ? 0.2711 0.2126 0.1602 0.0438  -0.0175 0.0471  271 PRO A CB  
1846 C CG  . PRO A 271 ? 0.2795 0.2189 0.1668 0.0419  -0.0310 0.0462  271 PRO A CG  
1847 C CD  . PRO A 271 ? 0.2586 0.2133 0.1759 0.0354  -0.0307 0.0466  271 PRO A CD  
1848 N N   . PHE A 272 ? 0.2313 0.1950 0.1611 0.0241  -0.0244 0.0325  272 PHE A N   
1849 C CA  . PHE A 272 ? 0.2332 0.1971 0.1629 0.0199  -0.0277 0.0273  272 PHE A CA  
1850 C C   . PHE A 272 ? 0.2267 0.2037 0.1795 0.0132  -0.0288 0.0255  272 PHE A C   
1851 O O   . PHE A 272 ? 0.2147 0.1978 0.1799 0.0121  -0.0299 0.0275  272 PHE A O   
1852 C CB  . PHE A 272 ? 0.2454 0.1973 0.1578 0.0204  -0.0392 0.0247  272 PHE A CB  
1853 C CG  . PHE A 272 ? 0.2827 0.2348 0.1991 0.0188  -0.0497 0.0262  272 PHE A CG  
1854 C CD1 . PHE A 272 ? 0.3042 0.2657 0.2402 0.0121  -0.0560 0.0252  272 PHE A CD1 
1855 C CD2 . PHE A 272 ? 0.3027 0.2462 0.2040 0.0245  -0.0527 0.0296  272 PHE A CD2 
1856 C CE1 . PHE A 272 ? 0.3207 0.2836 0.2636 0.0109  -0.0658 0.0279  272 PHE A CE1 
1857 C CE2 . PHE A 272 ? 0.3449 0.2888 0.2507 0.0232  -0.0634 0.0316  272 PHE A CE2 
1858 C CZ  . PHE A 272 ? 0.3027 0.2571 0.2310 0.0161  -0.0699 0.0308  272 PHE A CZ  
1859 N N   . PHE A 273 ? 0.1991 0.1798 0.1566 0.0094  -0.0277 0.0221  273 PHE A N   
1860 C CA  . PHE A 273 ? 0.1907 0.1815 0.1655 0.0039  -0.0293 0.0205  273 PHE A CA  
1861 C C   . PHE A 273 ? 0.2021 0.1905 0.1733 0.0009  -0.0336 0.0179  273 PHE A C   
1862 O O   . PHE A 273 ? 0.2158 0.2015 0.1801 0.0016  -0.0296 0.0162  273 PHE A O   
1863 C CB  . PHE A 273 ? 0.2433 0.2434 0.2312 0.0025  -0.0210 0.0197  273 PHE A CB  
1864 C CG  . PHE A 273 ? 0.2534 0.2620 0.2544 -0.0018 -0.0215 0.0179  273 PHE A CG  
1865 C CD1 . PHE A 273 ? 0.2481 0.2624 0.2617 -0.0026 -0.0229 0.0195  273 PHE A CD1 
1866 C CD2 . PHE A 273 ? 0.2162 0.2266 0.2165 -0.0042 -0.0205 0.0157  273 PHE A CD2 
1867 C CE1 . PHE A 273 ? 0.2248 0.2468 0.2502 -0.0053 -0.0218 0.0191  273 PHE A CE1 
1868 C CE2 . PHE A 273 ? 0.2563 0.2741 0.2673 -0.0072 -0.0200 0.0153  273 PHE A CE2 
1869 C CZ  . PHE A 273 ? 0.2305 0.2540 0.2538 -0.0074 -0.0203 0.0172  273 PHE A CZ  
1870 N N   . ILE A 274 ? 0.2001 0.1898 0.1781 -0.0025 -0.0416 0.0182  274 ILE A N   
1871 C CA  . ILE A 274 ? 0.2128 0.2012 0.1920 -0.0063 -0.0461 0.0167  274 ILE A CA  
1872 C C   . ILE A 274 ? 0.1816 0.1829 0.1818 -0.0105 -0.0444 0.0185  274 ILE A C   
1873 O O   . ILE A 274 ? 0.2018 0.2083 0.2145 -0.0116 -0.0479 0.0214  274 ILE A O   
1874 C CB  . ILE A 274 ? 0.2304 0.2069 0.1992 -0.0066 -0.0583 0.0163  274 ILE A CB  
1875 C CG1 . ILE A 274 ? 0.2448 0.2065 0.1884 -0.0006 -0.0586 0.0145  274 ILE A CG1 
1876 C CG2 . ILE A 274 ? 0.2763 0.2512 0.2494 -0.0111 -0.0632 0.0152  274 ILE A CG2 
1877 C CD1 . ILE A 274 ? 0.3054 0.2622 0.2380 0.0018  -0.0514 0.0121  274 ILE A CD1 
1878 N N   . GLY A 275 ? 0.1746 0.1810 0.1787 -0.0121 -0.0384 0.0174  275 GLY A N   
1879 C CA  . GLY A 275 ? 0.1714 0.1891 0.1924 -0.0148 -0.0350 0.0195  275 GLY A CA  
1880 C C   . GLY A 275 ? 0.1609 0.1793 0.1916 -0.0188 -0.0420 0.0225  275 GLY A C   
1881 O O   . GLY A 275 ? 0.1870 0.1959 0.2104 -0.0201 -0.0509 0.0219  275 GLY A O   
1882 N N   . ASN A 276 ? 0.1574 0.1867 0.2051 -0.0205 -0.0379 0.0262  276 ASN A N   
1883 C CA  . ASN A 276 ? 0.1394 0.1713 0.2012 -0.0246 -0.0435 0.0308  276 ASN A CA  
1884 C C   . ASN A 276 ? 0.1635 0.2002 0.2289 -0.0259 -0.0369 0.0325  276 ASN A C   
1885 O O   . ASN A 276 ? 0.1498 0.1907 0.2304 -0.0292 -0.0392 0.0379  276 ASN A O   
1886 C CB  . ASN A 276 ? 0.1518 0.1926 0.2349 -0.0256 -0.0457 0.0366  276 ASN A CB  
1887 C CG  . ASN A 276 ? 0.1299 0.1816 0.2222 -0.0223 -0.0338 0.0384  276 ASN A CG  
1888 O OD1 . ASN A 276 ? 0.1593 0.2130 0.2448 -0.0204 -0.0246 0.0362  276 ASN A OD1 
1889 N ND2 . ASN A 276 ? 0.2310 0.2891 0.3386 -0.0213 -0.0344 0.0425  276 ASN A ND2 
1890 N N   . THR A 277 ? 0.1344 0.1705 0.1871 -0.0233 -0.0292 0.0287  277 THR A N   
1891 C CA  . THR A 277 ? 0.1272 0.1655 0.1784 -0.0239 -0.0242 0.0298  277 THR A CA  
1892 C C   . THR A 277 ? 0.1415 0.1717 0.1743 -0.0224 -0.0238 0.0246  277 THR A C   
1893 O O   . THR A 277 ? 0.1457 0.1717 0.1690 -0.0201 -0.0240 0.0207  277 THR A O   
1894 C CB  . THR A 277 ? 0.1403 0.1885 0.1964 -0.0213 -0.0134 0.0316  277 THR A CB  
1895 O OG1 . THR A 277 ? 0.1536 0.2004 0.1983 -0.0179 -0.0090 0.0261  277 THR A OG1 
1896 C CG2 . THR A 277 ? 0.1498 0.2069 0.2252 -0.0212 -0.0111 0.0376  277 THR A CG2 
1897 N N   . ILE A 278 ? 0.1428 0.1715 0.1724 -0.0235 -0.0228 0.0256  278 ILE A N   
1898 C CA  . ILE A 278 ? 0.1418 0.1652 0.1569 -0.0216 -0.0210 0.0220  278 ILE A CA  
1899 C C   . ILE A 278 ? 0.1575 0.1879 0.1722 -0.0205 -0.0137 0.0231  278 ILE A C   
1900 O O   . ILE A 278 ? 0.1533 0.1885 0.1754 -0.0218 -0.0115 0.0277  278 ILE A O   
1901 C CB  . ILE A 278 ? 0.1437 0.1567 0.1528 -0.0228 -0.0269 0.0217  278 ILE A CB  
1902 C CG1 . ILE A 278 ? 0.1727 0.1758 0.1761 -0.0226 -0.0346 0.0192  278 ILE A CG1 
1903 C CG2 . ILE A 278 ? 0.1835 0.1931 0.1808 -0.0203 -0.0234 0.0196  278 ILE A CG2 
1904 C CD1 . ILE A 278 ? 0.2304 0.2200 0.2262 -0.0235 -0.0420 0.0182  278 ILE A CD1 
1905 N N   . ALA A 279 ? 0.1510 0.1817 0.1571 -0.0180 -0.0105 0.0195  279 ALA A N   
1906 C CA  . ALA A 279 ? 0.1420 0.1770 0.1438 -0.0167 -0.0058 0.0194  279 ALA A CA  
1907 C C   . ALA A 279 ? 0.1702 0.2008 0.1636 -0.0161 -0.0072 0.0182  279 ALA A C   
1908 O O   . ALA A 279 ? 0.1848 0.2100 0.1746 -0.0153 -0.0096 0.0162  279 ALA A O   
1909 C CB  . ALA A 279 ? 0.1555 0.1936 0.1556 -0.0145 -0.0023 0.0160  279 ALA A CB  
1910 N N   . VAL A 280 ? 0.1557 0.1888 0.1461 -0.0157 -0.0052 0.0203  280 VAL A N   
1911 C CA  . VAL A 280 ? 0.1516 0.1826 0.1358 -0.0147 -0.0062 0.0198  280 VAL A CA  
1912 C C   . VAL A 280 ? 0.1538 0.1895 0.1332 -0.0133 -0.0043 0.0185  280 VAL A C   
1913 O O   . VAL A 280 ? 0.1486 0.1877 0.1263 -0.0127 -0.0013 0.0203  280 VAL A O   
1914 C CB  . VAL A 280 ? 0.1478 0.1755 0.1319 -0.0155 -0.0073 0.0238  280 VAL A CB  
1915 C CG1 . VAL A 280 ? 0.1604 0.1852 0.1399 -0.0138 -0.0083 0.0236  280 VAL A CG1 
1916 C CG2 . VAL A 280 ? 0.1636 0.1850 0.1520 -0.0173 -0.0105 0.0246  280 VAL A CG2 
1917 N N   . ASN A 281 ? 0.1506 0.1856 0.1278 -0.0125 -0.0062 0.0155  281 ASN A N   
1918 C CA  . ASN A 281 ? 0.1413 0.1787 0.1132 -0.0115 -0.0069 0.0131  281 ASN A CA  
1919 C C   . ASN A 281 ? 0.1510 0.1897 0.1202 -0.0104 -0.0039 0.0107  281 ASN A C   
1920 O O   . ASN A 281 ? 0.1544 0.1939 0.1152 -0.0086 -0.0026 0.0103  281 ASN A O   
1921 C CB  . ASN A 281 ? 0.1517 0.1904 0.1179 -0.0108 -0.0081 0.0162  281 ASN A CB  
1922 C CG  . ASN A 281 ? 0.1603 0.1979 0.1303 -0.0111 -0.0108 0.0186  281 ASN A CG  
1923 O OD1 . ASN A 281 ? 0.1691 0.2046 0.1446 -0.0112 -0.0110 0.0177  281 ASN A OD1 
1924 N ND2 . ASN A 281 ? 0.1637 0.2024 0.1306 -0.0104 -0.0119 0.0223  281 ASN A ND2 
1925 N N   . GLY A 282 ? 0.1559 0.1942 0.1311 -0.0108 -0.0023 0.0094  282 GLY A N   
1926 C CA  . GLY A 282 ? 0.1528 0.1920 0.1271 -0.0090 0.0011  0.0071  282 GLY A CA  
1927 C C   . GLY A 282 ? 0.1607 0.2033 0.1360 -0.0077 0.0065  0.0113  282 GLY A C   
1928 O O   . GLY A 282 ? 0.1678 0.2111 0.1407 -0.0049 0.0109  0.0100  282 GLY A O   
1929 N N   . LYS A 283 ? 0.1464 0.1907 0.1261 -0.0094 0.0066  0.0169  283 LYS A N   
1930 C CA  . LYS A 283 ? 0.1373 0.1858 0.1226 -0.0087 0.0118  0.0228  283 LYS A CA  
1931 C C   . LYS A 283 ? 0.1540 0.2028 0.1528 -0.0123 0.0090  0.0266  283 LYS A C   
1932 O O   . LYS A 283 ? 0.1562 0.2010 0.1550 -0.0146 0.0040  0.0266  283 LYS A O   
1933 C CB  . LYS A 283 ? 0.1606 0.2106 0.1387 -0.0072 0.0146  0.0272  283 LYS A CB  
1934 C CG  . LYS A 283 ? 0.1792 0.2273 0.1407 -0.0032 0.0160  0.0233  283 LYS A CG  
1935 C CD  . LYS A 283 ? 0.2051 0.2539 0.1620 0.0014  0.0230  0.0222  283 LYS A CD  
1936 C CE  . LYS A 283 ? 0.2554 0.2992 0.1922 0.0057  0.0226  0.0172  283 LYS A CE  
1937 N NZ  . LYS A 283 ? 0.2608 0.3022 0.1894 0.0113  0.0293  0.0144  283 LYS A NZ  
1938 N N   . ILE A 284 ? 0.1494 0.2022 0.1594 -0.0122 0.0118  0.0298  284 ILE A N   
1939 C CA  . ILE A 284 ? 0.1369 0.1896 0.1608 -0.0159 0.0072  0.0332  284 ILE A CA  
1940 C C   . ILE A 284 ? 0.1458 0.1988 0.1757 -0.0184 0.0064  0.0397  284 ILE A C   
1941 O O   . ILE A 284 ? 0.1574 0.2158 0.1905 -0.0168 0.0128  0.0456  284 ILE A O   
1942 C CB  . ILE A 284 ? 0.1321 0.1903 0.1690 -0.0151 0.0102  0.0359  284 ILE A CB  
1943 C CG1 . ILE A 284 ? 0.1411 0.1972 0.1736 -0.0132 0.0095  0.0295  284 ILE A CG1 
1944 C CG2 . ILE A 284 ? 0.1379 0.1971 0.1919 -0.0193 0.0045  0.0412  284 ILE A CG2 
1945 C CD1 . ILE A 284 ? 0.1585 0.2204 0.2017 -0.0106 0.0149  0.0320  284 ILE A CD1 
1946 N N   . TRP A 285 ? 0.1377 0.1841 0.1693 -0.0218 -0.0013 0.0390  285 TRP A N   
1947 C CA  . TRP A 285 ? 0.1498 0.1940 0.1891 -0.0250 -0.0042 0.0446  285 TRP A CA  
1948 C C   . TRP A 285 ? 0.1492 0.1973 0.1851 -0.0232 0.0024  0.0495  285 TRP A C   
1949 O O   . TRP A 285 ? 0.1591 0.2129 0.2068 -0.0237 0.0066  0.0575  285 TRP A O   
1950 C CB  . TRP A 285 ? 0.1399 0.1871 0.1990 -0.0284 -0.0072 0.0503  285 TRP A CB  
1951 C CG  . TRP A 285 ? 0.1372 0.1777 0.1975 -0.0306 -0.0166 0.0457  285 TRP A CG  
1952 C CD1 . TRP A 285 ? 0.1441 0.1728 0.1927 -0.0313 -0.0241 0.0401  285 TRP A CD1 
1953 C CD2 . TRP A 285 ? 0.1328 0.1773 0.2047 -0.0314 -0.0190 0.0466  285 TRP A CD2 
1954 N NE1 . TRP A 285 ? 0.1557 0.1801 0.2060 -0.0324 -0.0314 0.0373  285 TRP A NE1 
1955 C CE2 . TRP A 285 ? 0.1379 0.1723 0.2035 -0.0328 -0.0290 0.0414  285 TRP A CE2 
1956 C CE3 . TRP A 285 ? 0.1351 0.1906 0.2228 -0.0304 -0.0134 0.0521  285 TRP A CE3 
1957 C CZ2 . TRP A 285 ? 0.1296 0.1645 0.2031 -0.0338 -0.0347 0.0413  285 TRP A CZ2 
1958 C CZ3 . TRP A 285 ? 0.1390 0.1959 0.2373 -0.0315 -0.0187 0.0523  285 TRP A CZ3 
1959 C CH2 . TRP A 285 ? 0.1417 0.1885 0.2324 -0.0333 -0.0298 0.0468  285 TRP A CH2 
1960 N N   . PRO A 286 ? 0.1373 0.1829 0.1579 -0.0207 0.0034  0.0457  286 PRO A N   
1961 C CA  . PRO A 286 ? 0.1405 0.1896 0.1549 -0.0182 0.0091  0.0502  286 PRO A CA  
1962 C C   . PRO A 286 ? 0.1667 0.2119 0.1847 -0.0204 0.0067  0.0554  286 PRO A C   
1963 O O   . PRO A 286 ? 0.1700 0.2082 0.1934 -0.0236 0.0001  0.0544  286 PRO A O   
1964 C CB  . PRO A 286 ? 0.1442 0.1915 0.1422 -0.0152 0.0087  0.0434  286 PRO A CB  
1965 C CG  . PRO A 286 ? 0.1648 0.2055 0.1621 -0.0172 0.0018  0.0376  286 PRO A CG  
1966 C CD  . PRO A 286 ? 0.1416 0.1811 0.1510 -0.0200 -0.0010 0.0381  286 PRO A CD  
1967 N N   . LYS A 287 ? 0.1512 0.2001 0.1653 -0.0180 0.0122  0.0613  287 LYS A N   
1968 C CA  . LYS A 287 ? 0.1739 0.2193 0.1890 -0.0190 0.0108  0.0665  287 LYS A CA  
1969 C C   . LYS A 287 ? 0.1845 0.2291 0.1829 -0.0155 0.0111  0.0641  287 LYS A C   
1970 O O   . LYS A 287 ? 0.1901 0.2381 0.1767 -0.0121 0.0136  0.0605  287 LYS A O   
1971 C CB  . LYS A 287 ? 0.2043 0.2551 0.2309 -0.0191 0.0170  0.0777  287 LYS A CB  
1972 C CG  . LYS A 287 ? 0.2389 0.2972 0.2552 -0.0135 0.0265  0.0809  287 LYS A CG  
1973 C CD  . LYS A 287 ? 0.3538 0.4173 0.3771 -0.0117 0.0347  0.0933  287 LYS A CD  
1974 C CE  . LYS A 287 ? 0.3173 0.3865 0.3278 -0.0048 0.0447  0.0950  287 LYS A CE  
1975 N NZ  . LYS A 287 ? 0.3878 0.4545 0.3738 0.0003  0.0456  0.0928  287 LYS A NZ  
1976 N N   . LEU A 288 ? 0.1716 0.2110 0.1694 -0.0162 0.0076  0.0658  288 LEU A N   
1977 C CA  . LEU A 288 ? 0.1847 0.2242 0.1701 -0.0131 0.0072  0.0658  288 LEU A CA  
1978 C C   . LEU A 288 ? 0.1824 0.2212 0.1716 -0.0129 0.0092  0.0751  288 LEU A C   
1979 O O   . LEU A 288 ? 0.1994 0.2321 0.1987 -0.0157 0.0064  0.0775  288 LEU A O   
1980 C CB  . LEU A 288 ? 0.1807 0.2147 0.1624 -0.0132 0.0014  0.0591  288 LEU A CB  
1981 C CG  . LEU A 288 ? 0.1854 0.2202 0.1583 -0.0103 -0.0002 0.0601  288 LEU A CG  
1982 C CD1 . LEU A 288 ? 0.2084 0.2488 0.1697 -0.0077 0.0003  0.0575  288 LEU A CD1 
1983 C CD2 . LEU A 288 ? 0.2240 0.2533 0.1982 -0.0102 -0.0045 0.0559  288 LEU A CD2 
1984 N N   . THR A 289 ? 0.1883 0.2320 0.1684 -0.0092 0.0137  0.0804  289 THR A N   
1985 C CA  . THR A 289 ? 0.1961 0.2399 0.1791 -0.0083 0.0165  0.0906  289 THR A CA  
1986 C C   . THR A 289 ? 0.2177 0.2579 0.1935 -0.0068 0.0115  0.0898  289 THR A C   
1987 O O   . THR A 289 ? 0.2682 0.3106 0.2306 -0.0039 0.0092  0.0860  289 THR A O   
1988 C CB  . THR A 289 ? 0.2291 0.2794 0.2032 -0.0039 0.0244  0.0974  289 THR A CB  
1989 O OG1 . THR A 289 ? 0.2588 0.3132 0.2399 -0.0044 0.0298  0.0975  289 THR A OG1 
1990 C CG2 . THR A 289 ? 0.2438 0.2947 0.2237 -0.0030 0.0287  0.1100  289 THR A CG2 
1991 N N   . VAL A 290 ? 0.1904 0.2246 0.1761 -0.0088 0.0092  0.0935  290 VAL A N   
1992 C CA  . VAL A 290 ? 0.2173 0.2473 0.1998 -0.0072 0.0049  0.0929  290 VAL A CA  
1993 C C   . VAL A 290 ? 0.2131 0.2414 0.1999 -0.0061 0.0068  0.1036  290 VAL A C   
1994 O O   . VAL A 290 ? 0.2381 0.2659 0.2346 -0.0079 0.0106  0.1109  290 VAL A O   
1995 C CB  . VAL A 290 ? 0.1952 0.2165 0.1837 -0.0092 0.0002  0.0857  290 VAL A CB  
1996 C CG1 . VAL A 290 ? 0.2000 0.2233 0.1838 -0.0096 -0.0015 0.0761  290 VAL A CG1 
1997 C CG2 . VAL A 290 ? 0.2096 0.2226 0.2111 -0.0130 -0.0003 0.0878  290 VAL A CG2 
1998 N N   . GLU A 291 ? 0.2221 0.2499 0.2032 -0.0030 0.0040  0.1053  291 GLU A N   
1999 C CA  . GLU A 291 ? 0.2210 0.2457 0.2068 -0.0015 0.0047  0.1148  291 GLU A CA  
2000 C C   . GLU A 291 ? 0.2409 0.2544 0.2384 -0.0035 0.0021  0.1128  291 GLU A C   
2001 O O   . GLU A 291 ? 0.2228 0.2316 0.2206 -0.0044 -0.0008 0.1037  291 GLU A O   
2002 C CB  . GLU A 291 ? 0.2830 0.3119 0.2588 0.0028  0.0017  0.1171  291 GLU A CB  
2003 C CG  . GLU A 291 ? 0.2873 0.3243 0.2471 0.0055  0.0020  0.1167  291 GLU A CG  
2004 C CD  . GLU A 291 ? 0.2824 0.3219 0.2339 0.0089  -0.0040 0.1161  291 GLU A CD  
2005 O OE1 . GLU A 291 ? 0.2994 0.3363 0.2574 0.0104  -0.0057 0.1208  291 GLU A OE1 
2006 O OE2 . GLU A 291 ? 0.3107 0.3542 0.2500 0.0101  -0.0076 0.1109  291 GLU A OE2 
2007 N N   . PRO A 292 ? 0.2199 0.2276 0.2261 -0.0036 0.0033  0.1213  292 PRO A N   
2008 C CA  . PRO A 292 ? 0.2663 0.2602 0.2817 -0.0047 0.0005  0.1192  292 PRO A CA  
2009 C C   . PRO A 292 ? 0.2585 0.2493 0.2700 -0.0001 -0.0016 0.1177  292 PRO A C   
2010 O O   . PRO A 292 ? 0.2744 0.2615 0.2898 0.0026  -0.0011 0.1250  292 PRO A O   
2011 C CB  . PRO A 292 ? 0.2627 0.2527 0.2896 -0.0065 0.0028  0.1302  292 PRO A CB  
2012 C CG  . PRO A 292 ? 0.2777 0.2799 0.2978 -0.0031 0.0070  0.1364  292 PRO A CG  
2013 C CD  . PRO A 292 ? 0.2579 0.2704 0.2657 -0.0025 0.0078  0.1319  292 PRO A CD  
2014 N N   . ARG A 293 ? 0.2653 0.2580 0.2705 0.0012  -0.0034 0.1089  293 ARG A N   
2015 C CA  . ARG A 293 ? 0.2294 0.2218 0.2331 0.0059  -0.0047 0.1078  293 ARG A CA  
2016 C C   . ARG A 293 ? 0.2312 0.2215 0.2316 0.0060  -0.0057 0.0974  293 ARG A C   
2017 O O   . ARG A 293 ? 0.2266 0.2144 0.2253 0.0025  -0.0060 0.0911  293 ARG A O   
2018 C CB  . ARG A 293 ? 0.2481 0.2533 0.2471 0.0085  -0.0059 0.1135  293 ARG A CB  
2019 C CG  . ARG A 293 ? 0.2464 0.2620 0.2365 0.0066  -0.0069 0.1090  293 ARG A CG  
2020 C CD  . ARG A 293 ? 0.3189 0.3441 0.3035 0.0094  -0.0109 0.1110  293 ARG A CD  
2021 N NE  . ARG A 293 ? 0.3003 0.3253 0.2897 0.0107  -0.0132 0.1054  293 ARG A NE  
2022 C CZ  . ARG A 293 ? 0.3068 0.3383 0.2986 0.0133  -0.0174 0.1076  293 ARG A CZ  
2023 N NH1 . ARG A 293 ? 0.3402 0.3780 0.3280 0.0150  -0.0213 0.1147  293 ARG A NH1 
2024 N NH2 . ARG A 293 ? 0.2506 0.2821 0.2497 0.0145  -0.0179 0.1035  293 ARG A NH2 
2025 N N   . LYS A 294 ? 0.2260 0.2182 0.2267 0.0102  -0.0059 0.0965  294 LYS A N   
2026 C CA  . LYS A 294 ? 0.2060 0.1954 0.2048 0.0115  -0.0055 0.0884  294 LYS A CA  
2027 C C   . LYS A 294 ? 0.2037 0.2060 0.1994 0.0098  -0.0073 0.0850  294 LYS A C   
2028 O O   . LYS A 294 ? 0.2111 0.2242 0.2066 0.0100  -0.0098 0.0892  294 LYS A O   
2029 C CB  . LYS A 294 ? 0.2417 0.2257 0.2448 0.0177  -0.0032 0.0901  294 LYS A CB  
2030 C CG  . LYS A 294 ? 0.2572 0.2249 0.2615 0.0202  -0.0012 0.0918  294 LYS A CG  
2031 C CD  . LYS A 294 ? 0.2590 0.2198 0.2659 0.0278  0.0027  0.0925  294 LYS A CD  
2032 C CE  . LYS A 294 ? 0.2768 0.2482 0.2934 0.0318  0.0032  0.1017  294 LYS A CE  
2033 N NZ  . LYS A 294 ? 0.2543 0.2305 0.2745 0.0298  0.0004  0.1101  294 LYS A NZ  
2034 N N   . TYR A 295 ? 0.1950 0.1951 0.1875 0.0081  -0.0069 0.0773  295 TYR A N   
2035 C CA  . TYR A 295 ? 0.1950 0.2047 0.1854 0.0066  -0.0085 0.0730  295 TYR A CA  
2036 C C   . TYR A 295 ? 0.2110 0.2166 0.2027 0.0091  -0.0065 0.0681  295 TYR A C   
2037 O O   . TYR A 295 ? 0.2095 0.2031 0.1990 0.0111  -0.0040 0.0655  295 TYR A O   
2038 C CB  . TYR A 295 ? 0.1757 0.1865 0.1611 0.0020  -0.0088 0.0686  295 TYR A CB  
2039 C CG  . TYR A 295 ? 0.1874 0.2049 0.1699 0.0001  -0.0093 0.0734  295 TYR A CG  
2040 C CD1 . TYR A 295 ? 0.1731 0.1867 0.1580 -0.0001 -0.0079 0.0800  295 TYR A CD1 
2041 C CD2 . TYR A 295 ? 0.1888 0.2151 0.1653 -0.0010 -0.0106 0.0714  295 TYR A CD2 
2042 C CE1 . TYR A 295 ? 0.2173 0.2369 0.1989 -0.0009 -0.0068 0.0857  295 TYR A CE1 
2043 C CE2 . TYR A 295 ? 0.2077 0.2387 0.1785 -0.0013 -0.0097 0.0760  295 TYR A CE2 
2044 C CZ  . TYR A 295 ? 0.2090 0.2371 0.1824 -0.0010 -0.0073 0.0836  295 TYR A CZ  
2045 O OH  . TYR A 295 ? 0.2369 0.2697 0.2042 -0.0004 -0.0050 0.0894  295 TYR A OH  
2046 N N   . ARG A 296 ? 0.1799 0.1949 0.1746 0.0092  -0.0080 0.0669  296 ARG A N   
2047 C CA  . ARG A 296 ? 0.1576 0.1710 0.1543 0.0111  -0.0055 0.0630  296 ARG A CA  
2048 C C   . ARG A 296 ? 0.1738 0.1900 0.1656 0.0069  -0.0070 0.0566  296 ARG A C   
2049 O O   . ARG A 296 ? 0.1858 0.2104 0.1767 0.0038  -0.0107 0.0561  296 ARG A O   
2050 C CB  . ARG A 296 ? 0.1731 0.1963 0.1806 0.0134  -0.0065 0.0672  296 ARG A CB  
2051 C CG  . ARG A 296 ? 0.1779 0.2020 0.1901 0.0151  -0.0035 0.0647  296 ARG A CG  
2052 C CD  . ARG A 296 ? 0.1603 0.1945 0.1881 0.0173  -0.0047 0.0710  296 ARG A CD  
2053 N NE  . ARG A 296 ? 0.1790 0.2144 0.2143 0.0197  -0.0002 0.0708  296 ARG A NE  
2054 C CZ  . ARG A 296 ? 0.1689 0.2123 0.2213 0.0224  0.0007  0.0773  296 ARG A CZ  
2055 N NH1 . ARG A 296 ? 0.2056 0.2566 0.2696 0.0230  -0.0033 0.0842  296 ARG A NH1 
2056 N NH2 . ARG A 296 ? 0.2122 0.2561 0.2714 0.0250  0.0063  0.0780  296 ARG A NH2 
2057 N N   . PHE A 297 ? 0.1660 0.1740 0.1534 0.0074  -0.0045 0.0518  297 PHE A N   
2058 C CA  . PHE A 297 ? 0.1583 0.1686 0.1424 0.0041  -0.0056 0.0463  297 PHE A CA  
2059 C C   . PHE A 297 ? 0.1538 0.1635 0.1402 0.0069  -0.0028 0.0444  297 PHE A C   
2060 O O   . PHE A 297 ? 0.1718 0.1725 0.1556 0.0115  0.0012  0.0448  297 PHE A O   
2061 C CB  . PHE A 297 ? 0.1777 0.1795 0.1555 0.0017  -0.0061 0.0429  297 PHE A CB  
2062 C CG  . PHE A 297 ? 0.1761 0.1803 0.1542 -0.0015 -0.0079 0.0458  297 PHE A CG  
2063 C CD1 . PHE A 297 ? 0.1748 0.1886 0.1528 -0.0043 -0.0090 0.0458  297 PHE A CD1 
2064 C CD2 . PHE A 297 ? 0.1827 0.1790 0.1611 -0.0009 -0.0079 0.0491  297 PHE A CD2 
2065 C CE1 . PHE A 297 ? 0.1772 0.1934 0.1548 -0.0061 -0.0091 0.0499  297 PHE A CE1 
2066 C CE2 . PHE A 297 ? 0.2081 0.2073 0.1886 -0.0036 -0.0086 0.0534  297 PHE A CE2 
2067 C CZ  . PHE A 297 ? 0.1746 0.1842 0.1546 -0.0059 -0.0087 0.0542  297 PHE A CZ  
2068 N N   . ARG A 298 ? 0.1563 0.1741 0.1463 0.0045  -0.0045 0.0424  298 ARG A N   
2069 C CA  . ARG A 298 ? 0.1608 0.1795 0.1553 0.0067  -0.0017 0.0417  298 ARG A CA  
2070 C C   . ARG A 298 ? 0.1548 0.1693 0.1422 0.0047  -0.0016 0.0361  298 ARG A C   
2071 O O   . ARG A 298 ? 0.1615 0.1817 0.1498 0.0008  -0.0046 0.0332  298 ARG A O   
2072 C CB  . ARG A 298 ? 0.1408 0.1708 0.1467 0.0050  -0.0049 0.0438  298 ARG A CB  
2073 C CG  . ARG A 298 ? 0.1494 0.1847 0.1625 0.0059  -0.0074 0.0495  298 ARG A CG  
2074 C CD  . ARG A 298 ? 0.1606 0.2059 0.1869 0.0043  -0.0119 0.0519  298 ARG A CD  
2075 N NE  . ARG A 298 ? 0.1689 0.2196 0.2036 0.0055  -0.0153 0.0582  298 ARG A NE  
2076 C CZ  . ARG A 298 ? 0.1496 0.2062 0.2012 0.0079  -0.0148 0.0646  298 ARG A CZ  
2077 N NH1 . ARG A 298 ? 0.1802 0.2374 0.2414 0.0099  -0.0097 0.0660  298 ARG A NH1 
2078 N NH2 . ARG A 298 ? 0.1689 0.2312 0.2290 0.0086  -0.0192 0.0707  298 ARG A NH2 
2079 N N   . ILE A 299 ? 0.1557 0.1595 0.1353 0.0077  0.0013  0.0345  299 ILE A N   
2080 C CA  . ILE A 299 ? 0.1681 0.1666 0.1402 0.0056  -0.0003 0.0296  299 ILE A CA  
2081 C C   . ILE A 299 ? 0.1703 0.1686 0.1426 0.0079  0.0026  0.0286  299 ILE A C   
2082 O O   . ILE A 299 ? 0.2026 0.1957 0.1728 0.0134  0.0075  0.0310  299 ILE A O   
2083 C CB  . ILE A 299 ? 0.1788 0.1638 0.1408 0.0070  -0.0013 0.0280  299 ILE A CB  
2084 C CG1 . ILE A 299 ? 0.1877 0.1727 0.1520 0.0054  -0.0032 0.0306  299 ILE A CG1 
2085 C CG2 . ILE A 299 ? 0.2241 0.2052 0.1811 0.0038  -0.0051 0.0237  299 ILE A CG2 
2086 C CD1 . ILE A 299 ? 0.2354 0.2069 0.1923 0.0050  -0.0061 0.0288  299 ILE A CD1 
2087 N N   . LEU A 300 ? 0.1549 0.1586 0.1298 0.0042  0.0004  0.0259  300 LEU A N   
2088 C CA  . LEU A 300 ? 0.1458 0.1502 0.1225 0.0057  0.0028  0.0255  300 LEU A CA  
2089 C C   . LEU A 300 ? 0.1509 0.1515 0.1213 0.0036  0.0002  0.0215  300 LEU A C   
2090 O O   . LEU A 300 ? 0.1542 0.1591 0.1267 -0.0007 -0.0034 0.0193  300 LEU A O   
2091 C CB  . LEU A 300 ? 0.1384 0.1540 0.1279 0.0031  0.0018  0.0266  300 LEU A CB  
2092 C CG  . LEU A 300 ? 0.1484 0.1662 0.1424 0.0025  0.0027  0.0255  300 LEU A CG  
2093 C CD1 . LEU A 300 ? 0.1644 0.1785 0.1597 0.0079  0.0088  0.0297  300 LEU A CD1 
2094 C CD2 . LEU A 300 ? 0.1476 0.1744 0.1531 -0.0013 -0.0008 0.0250  300 LEU A CD2 
2095 N N   . ASN A 301 ? 0.1647 0.1577 0.1278 0.0073  0.0022  0.0211  301 ASN A N   
2096 C CA  . ASN A 301 ? 0.1543 0.1453 0.1141 0.0055  -0.0007 0.0182  301 ASN A CA  
2097 C C   . ASN A 301 ? 0.1574 0.1559 0.1263 0.0051  0.0017  0.0192  301 ASN A C   
2098 O O   . ASN A 301 ? 0.1611 0.1581 0.1305 0.0093  0.0064  0.0223  301 ASN A O   
2099 C CB  . ASN A 301 ? 0.1677 0.1450 0.1125 0.0100  -0.0010 0.0173  301 ASN A CB  
2100 C CG  . ASN A 301 ? 0.1946 0.1699 0.1365 0.0082  -0.0054 0.0149  301 ASN A CG  
2101 O OD1 . ASN A 301 ? 0.1849 0.1696 0.1371 0.0043  -0.0064 0.0145  301 ASN A OD1 
2102 N ND2 . ASN A 301 ? 0.2108 0.1731 0.1381 0.0113  -0.0086 0.0133  301 ASN A ND2 
2103 N N   . ALA A 302 ? 0.1429 0.1492 0.1195 0.0005  -0.0010 0.0171  302 ALA A N   
2104 C CA  . ALA A 302 ? 0.1335 0.1452 0.1189 -0.0004 0.0001  0.0171  302 ALA A CA  
2105 C C   . ALA A 302 ? 0.1517 0.1621 0.1357 -0.0014 -0.0016 0.0149  302 ALA A C   
2106 O O   . ALA A 302 ? 0.1502 0.1654 0.1418 -0.0033 -0.0019 0.0136  302 ALA A O   
2107 C CB  . ALA A 302 ? 0.1611 0.1809 0.1555 -0.0038 -0.0016 0.0160  302 ALA A CB  
2108 N N   . SER A 303 ? 0.1491 0.1523 0.1237 0.0000  -0.0036 0.0146  303 SER A N   
2109 C CA  . SER A 303 ? 0.1489 0.1506 0.1227 -0.0006 -0.0063 0.0135  303 SER A CA  
2110 C C   . SER A 303 ? 0.1553 0.1546 0.1284 0.0030  -0.0032 0.0158  303 SER A C   
2111 O O   . SER A 303 ? 0.1757 0.1718 0.1454 0.0070  0.0012  0.0188  303 SER A O   
2112 C CB  . SER A 303 ? 0.1644 0.1577 0.1281 -0.0003 -0.0113 0.0127  303 SER A CB  
2113 O OG  . SER A 303 ? 0.1773 0.1726 0.1435 -0.0037 -0.0138 0.0118  303 SER A OG  
2114 N N   . ASN A 304 ? 0.1561 0.1570 0.1331 0.0021  -0.0049 0.0154  304 ASN A N   
2115 C CA  . ASN A 304 ? 0.1614 0.1599 0.1380 0.0056  -0.0021 0.0185  304 ASN A CA  
2116 C C   . ASN A 304 ? 0.1741 0.1617 0.1342 0.0108  -0.0025 0.0204  304 ASN A C   
2117 O O   . ASN A 304 ? 0.1808 0.1649 0.1368 0.0157  0.0029  0.0244  304 ASN A O   
2118 C CB  . ASN A 304 ? 0.1747 0.1768 0.1591 0.0038  -0.0043 0.0178  304 ASN A CB  
2119 C CG  . ASN A 304 ? 0.1613 0.1708 0.1599 0.0014  -0.0016 0.0166  304 ASN A CG  
2120 O OD1 . ASN A 304 ? 0.1883 0.2016 0.1910 -0.0010 -0.0010 0.0145  304 ASN A OD1 
2121 N ND2 . ASN A 304 ? 0.1591 0.1693 0.1643 0.0021  -0.0007 0.0179  304 ASN A ND2 
2122 N N   . THR A 305 ? 0.1823 0.1637 0.1327 0.0100  -0.0093 0.0180  305 THR A N   
2123 C CA  . THR A 305 ? 0.1933 0.1613 0.1245 0.0149  -0.0123 0.0184  305 THR A CA  
2124 C C   . THR A 305 ? 0.1936 0.1533 0.1141 0.0143  -0.0174 0.0152  305 THR A C   
2125 O O   . THR A 305 ? 0.2316 0.1787 0.1341 0.0198  -0.0166 0.0150  305 THR A O   
2126 C CB  . THR A 305 ? 0.2153 0.1814 0.1452 0.0142  -0.0194 0.0185  305 THR A CB  
2127 O OG1 . THR A 305 ? 0.2174 0.1893 0.1560 0.0154  -0.0151 0.0219  305 THR A OG1 
2128 C CG2 . THR A 305 ? 0.2537 0.2040 0.1608 0.0190  -0.0252 0.0179  305 THR A CG2 
2129 N N   . ASN A 306 ? 0.2041 0.1694 0.1349 0.0082  -0.0223 0.0129  306 ASN A N   
2130 C CA  . ASN A 306 ? 0.2077 0.1642 0.1307 0.0065  -0.0296 0.0102  306 ASN A CA  
2131 C C   . ASN A 306 ? 0.1983 0.1486 0.1127 0.0094  -0.0254 0.0096  306 ASN A C   
2132 O O   . ASN A 306 ? 0.2223 0.1807 0.1448 0.0095  -0.0181 0.0112  306 ASN A O   
2133 C CB  . ASN A 306 ? 0.2057 0.1720 0.1457 -0.0005 -0.0339 0.0099  306 ASN A CB  
2134 C CG  . ASN A 306 ? 0.2648 0.2232 0.2025 -0.0035 -0.0449 0.0086  306 ASN A CG  
2135 O OD1 . ASN A 306 ? 0.2792 0.2224 0.1998 -0.0006 -0.0504 0.0064  306 ASN A OD1 
2136 N ND2 . ASN A 306 ? 0.2777 0.2456 0.2329 -0.0092 -0.0481 0.0101  306 ASN A ND2 
2137 N N   . ALA A 307 ? 0.2366 0.1715 0.1347 0.0118  -0.0309 0.0071  307 ALA A N   
2138 C CA  . ALA A 307 ? 0.2435 0.1701 0.1326 0.0149  -0.0277 0.0061  307 ALA A CA  
2139 C C   . ALA A 307 ? 0.2528 0.1760 0.1462 0.0095  -0.0358 0.0038  307 ALA A C   
2140 O O   . ALA A 307 ? 0.2884 0.2092 0.1847 0.0051  -0.0456 0.0023  307 ALA A O   
2141 C CB  . ALA A 307 ? 0.2788 0.1868 0.1425 0.0238  -0.0264 0.0050  307 ALA A CB  
2142 N N   . TYR A 308 ? 0.2410 0.1641 0.1364 0.0097  -0.0319 0.0042  308 TYR A N   
2143 C CA  . TYR A 308 ? 0.2434 0.1640 0.1451 0.0045  -0.0384 0.0032  308 TYR A CA  
2144 C C   . TYR A 308 ? 0.2689 0.1725 0.1549 0.0094  -0.0382 0.0010  308 TYR A C   
2145 O O   . TYR A 308 ? 0.3057 0.2055 0.1820 0.0164  -0.0298 0.0019  308 TYR A O   
2146 C CB  . TYR A 308 ? 0.2258 0.1640 0.1475 -0.0006 -0.0339 0.0066  308 TYR A CB  
2147 C CG  . TYR A 308 ? 0.2063 0.1599 0.1410 -0.0037 -0.0320 0.0083  308 TYR A CG  
2148 C CD1 . TYR A 308 ? 0.2714 0.2281 0.2144 -0.0082 -0.0386 0.0083  308 TYR A CD1 
2149 C CD2 . TYR A 308 ? 0.2246 0.1882 0.1635 -0.0017 -0.0242 0.0098  308 TYR A CD2 
2150 C CE1 . TYR A 308 ? 0.2560 0.2254 0.2100 -0.0098 -0.0361 0.0098  308 TYR A CE1 
2151 C CE2 . TYR A 308 ? 0.2152 0.1902 0.1644 -0.0039 -0.0227 0.0105  308 TYR A CE2 
2152 C CZ  . TYR A 308 ? 0.2128 0.1904 0.1687 -0.0076 -0.0281 0.0104  308 TYR A CZ  
2153 O OH  . TYR A 308 ? 0.1914 0.1791 0.1571 -0.0089 -0.0260 0.0111  308 TYR A OH  
2154 N N   . THR A 309 ? 0.2626 0.1554 0.1472 0.0060  -0.0474 -0.0013 309 THR A N   
2155 C CA  . THR A 309 ? 0.2818 0.1593 0.1553 0.0097  -0.0471 -0.0032 309 THR A CA  
2156 C C   . THR A 309 ? 0.2629 0.1482 0.1548 0.0031  -0.0487 -0.0003 309 THR A C   
2157 O O   . THR A 309 ? 0.2788 0.1628 0.1801 -0.0035 -0.0582 -0.0005 309 THR A O   
2158 C CB  . THR A 309 ? 0.3100 0.1625 0.1614 0.0129  -0.0571 -0.0091 309 THR A CB  
2159 O OG1 . THR A 309 ? 0.3614 0.2064 0.1928 0.0207  -0.0534 -0.0108 309 THR A OG1 
2160 C CG2 . THR A 309 ? 0.3596 0.1953 0.2000 0.0170  -0.0564 -0.0114 309 THR A CG2 
2161 N N   . LEU A 310 ? 0.2457 0.1396 0.1440 0.0049  -0.0396 0.0032  310 LEU A N   
2162 C CA  . LEU A 310 ? 0.2403 0.1435 0.1555 -0.0006 -0.0397 0.0072  310 LEU A CA  
2163 C C   . LEU A 310 ? 0.2603 0.1463 0.1706 -0.0006 -0.0452 0.0057  310 LEU A C   
2164 O O   . LEU A 310 ? 0.2932 0.1624 0.1868 0.0062  -0.0437 0.0026  310 LEU A O   
2165 C CB  . LEU A 310 ? 0.2440 0.1616 0.1663 0.0018  -0.0294 0.0115  310 LEU A CB  
2166 C CG  . LEU A 310 ? 0.2570 0.1947 0.1917 -0.0016 -0.0258 0.0140  310 LEU A CG  
2167 C CD1 . LEU A 310 ? 0.2560 0.1941 0.1844 0.0006  -0.0253 0.0115  310 LEU A CD1 
2168 C CD2 . LEU A 310 ? 0.2720 0.2213 0.2128 0.0005  -0.0181 0.0179  310 LEU A CD2 
2169 N N   . ARG A 311 ? 0.2548 0.1447 0.1807 -0.0079 -0.0510 0.0085  311 ARG A N   
2170 C CA  . ARG A 311 ? 0.2583 0.1342 0.1853 -0.0094 -0.0563 0.0086  311 ARG A CA  
2171 C C   . ARG A 311 ? 0.2799 0.1716 0.2289 -0.0153 -0.0539 0.0162  311 ARG A C   
2172 O O   . ARG A 311 ? 0.2598 0.1674 0.2230 -0.0203 -0.0537 0.0198  311 ARG A O   
2173 C CB  . ARG A 311 ? 0.2889 0.1475 0.2114 -0.0129 -0.0701 0.0038  311 ARG A CB  
2174 C CG  . ARG A 311 ? 0.3307 0.1697 0.2515 -0.0140 -0.0774 0.0023  311 ARG A CG  
2175 C CD  . ARG A 311 ? 0.3714 0.1897 0.2824 -0.0161 -0.0926 -0.0042 311 ARG A CD  
2176 N NE  . ARG A 311 ? 0.4781 0.2736 0.3852 -0.0169 -0.1012 -0.0071 311 ARG A NE  
2177 C CZ  . ARG A 311 ? 0.4550 0.2491 0.3826 -0.0257 -0.1113 -0.0037 311 ARG A CZ  
2178 N NH1 . ARG A 311 ? 0.4852 0.3007 0.4391 -0.0337 -0.1122 0.0036  311 ARG A NH1 
2179 N NH2 . ARG A 311 ? 0.4469 0.2170 0.3694 -0.0262 -0.1203 -0.0073 311 ARG A NH2 
2180 N N   . LEU A 312 ? 0.2647 0.1518 0.2155 -0.0139 -0.0510 0.0191  312 LEU A N   
2181 C CA  . LEU A 312 ? 0.2584 0.1602 0.2271 -0.0178 -0.0469 0.0273  312 LEU A CA  
2182 C C   . LEU A 312 ? 0.2497 0.1418 0.2303 -0.0235 -0.0550 0.0301  312 LEU A C   
2183 O O   . LEU A 312 ? 0.2815 0.1556 0.2559 -0.0215 -0.0583 0.0282  312 LEU A O   
2184 C CB  . LEU A 312 ? 0.2733 0.1776 0.2377 -0.0122 -0.0385 0.0300  312 LEU A CB  
2185 C CG  . LEU A 312 ? 0.2472 0.1639 0.2266 -0.0151 -0.0348 0.0388  312 LEU A CG  
2186 C CD1 . LEU A 312 ? 0.2835 0.2216 0.2718 -0.0183 -0.0308 0.0426  312 LEU A CD1 
2187 C CD2 . LEU A 312 ? 0.2880 0.2038 0.2629 -0.0093 -0.0285 0.0415  312 LEU A CD2 
2188 N N   . GLY A 313 ? 0.2612 0.1650 0.2601 -0.0303 -0.0576 0.0353  313 GLY A N   
2189 C CA  . GLY A 313 ? 0.2605 0.1563 0.2751 -0.0364 -0.0653 0.0395  313 GLY A CA  
2190 C C   . GLY A 313 ? 0.3108 0.1815 0.3153 -0.0370 -0.0781 0.0315  313 GLY A C   
2191 O O   . GLY A 313 ? 0.3386 0.2026 0.3293 -0.0351 -0.0828 0.0241  313 GLY A O   
2192 N N   . ASP A 314 ? 0.3419 0.1968 0.3515 -0.0391 -0.0840 0.0328  314 ASP A N   
2193 C CA  . ASP A 314 ? 0.4004 0.2275 0.3981 -0.0393 -0.0974 0.0243  314 ASP A CA  
2194 C C   . ASP A 314 ? 0.3976 0.2063 0.3663 -0.0294 -0.0937 0.0159  314 ASP A C   
2195 O O   . ASP A 314 ? 0.4419 0.2310 0.4040 -0.0268 -0.0962 0.0138  314 ASP A O   
2196 C CB  . ASP A 314 ? 0.4562 0.2725 0.4735 -0.0464 -0.1070 0.0289  314 ASP A CB  
2197 C CG  . ASP A 314 ? 0.5500 0.3840 0.5978 -0.0557 -0.1105 0.0381  314 ASP A CG  
2198 O OD1 . ASP A 314 ? 0.5660 0.4104 0.6154 -0.0574 -0.1126 0.0367  314 ASP A OD1 
2199 O OD2 . ASP A 314 ? 0.5745 0.4149 0.6444 -0.0597 -0.1097 0.0465  314 ASP A OD2 
2200 N N   . GLY A 315 ? 0.3612 0.1766 0.3135 -0.0234 -0.0871 0.0118  315 GLY A N   
2201 C CA  . GLY A 315 ? 0.4010 0.2009 0.3270 -0.0131 -0.0818 0.0052  315 GLY A CA  
2202 C C   . GLY A 315 ? 0.3478 0.1503 0.2757 -0.0083 -0.0711 0.0100  315 GLY A C   
2203 O O   . GLY A 315 ? 0.4260 0.2078 0.3378 -0.0013 -0.0702 0.0057  315 GLY A O   
2204 N N   . ARG A 316 ? 0.3622 0.1888 0.3087 -0.0113 -0.0632 0.0190  316 ARG A N   
2205 C CA  . ARG A 316 ? 0.3512 0.1827 0.3011 -0.0070 -0.0538 0.0247  316 ARG A CA  
2206 C C   . ARG A 316 ? 0.3141 0.1474 0.2480 0.0025  -0.0441 0.0221  316 ARG A C   
2207 O O   . ARG A 316 ? 0.3271 0.1687 0.2541 0.0042  -0.0416 0.0193  316 ARG A O   
2208 C CB  . ARG A 316 ? 0.3327 0.1894 0.3036 -0.0123 -0.0486 0.0349  316 ARG A CB  
2209 C CG  . ARG A 316 ? 0.3435 0.2018 0.3345 -0.0211 -0.0554 0.0406  316 ARG A CG  
2210 C CD  . ARG A 316 ? 0.3603 0.1957 0.3529 -0.0218 -0.0623 0.0399  316 ARG A CD  
2211 N NE  . ARG A 316 ? 0.3467 0.1838 0.3614 -0.0310 -0.0696 0.0460  316 ARG A NE  
2212 C CZ  . ARG A 316 ? 0.4290 0.2520 0.4542 -0.0339 -0.0749 0.0494  316 ARG A CZ  
2213 N NH1 . ARG A 316 ? 0.5574 0.3621 0.5713 -0.0281 -0.0740 0.0465  316 ARG A NH1 
2214 N NH2 . ARG A 316 ? 0.4690 0.2965 0.5182 -0.0426 -0.0808 0.0565  316 ARG A NH2 
2215 N N   . LYS A 317 ? 0.3380 0.1639 0.2684 0.0089  -0.0382 0.0242  317 LYS A N   
2216 C CA  . LYS A 317 ? 0.3515 0.1786 0.2703 0.0186  -0.0283 0.0236  317 LYS A CA  
2217 C C   . LYS A 317 ? 0.3384 0.1933 0.2698 0.0176  -0.0207 0.0306  317 LYS A C   
2218 O O   . LYS A 317 ? 0.3379 0.2078 0.2851 0.0122  -0.0207 0.0374  317 LYS A O   
2219 C CB  . LYS A 317 ? 0.3850 0.1959 0.2992 0.0258  -0.0245 0.0248  317 LYS A CB  
2220 C CG  . LYS A 317 ? 0.4793 0.2581 0.3756 0.0290  -0.0316 0.0161  317 LYS A CG  
2221 C CD  . LYS A 317 ? 0.5968 0.3592 0.4920 0.0350  -0.0285 0.0181  317 LYS A CD  
2222 C CE  . LYS A 317 ? 0.6621 0.3918 0.5444 0.0349  -0.0392 0.0099  317 LYS A CE  
2223 N NZ  . LYS A 317 ? 0.7052 0.4242 0.5745 0.0309  -0.0501 0.0010  317 LYS A NZ  
2224 N N   . PHE A 318 ? 0.3118 0.1725 0.2356 0.0234  -0.0142 0.0291  318 PHE A N   
2225 C CA  . PHE A 318 ? 0.2809 0.1644 0.2154 0.0240  -0.0074 0.0352  318 PHE A CA  
2226 C C   . PHE A 318 ? 0.3155 0.1953 0.2420 0.0339  0.0012  0.0352  318 PHE A C   
2227 O O   . PHE A 318 ? 0.3282 0.1882 0.2385 0.0405  0.0026  0.0301  318 PHE A O   
2228 C CB  . PHE A 318 ? 0.2893 0.1905 0.2298 0.0175  -0.0096 0.0347  318 PHE A CB  
2229 C CG  . PHE A 318 ? 0.2679 0.1615 0.1968 0.0174  -0.0126 0.0276  318 PHE A CG  
2230 C CD1 . PHE A 318 ? 0.2970 0.1791 0.2221 0.0126  -0.0214 0.0230  318 PHE A CD1 
2231 C CD2 . PHE A 318 ? 0.2761 0.1742 0.1990 0.0223  -0.0072 0.0262  318 PHE A CD2 
2232 C CE1 . PHE A 318 ? 0.2818 0.1571 0.1956 0.0127  -0.0252 0.0168  318 PHE A CE1 
2233 C CE2 . PHE A 318 ? 0.2981 0.1894 0.2096 0.0227  -0.0098 0.0205  318 PHE A CE2 
2234 C CZ  . PHE A 318 ? 0.2990 0.1788 0.2050 0.0181  -0.0191 0.0156  318 PHE A CZ  
2235 N N   . TYR A 319 ? 0.2573 0.1552 0.1954 0.0356  0.0070  0.0416  319 TYR A N   
2236 C CA  . TYR A 319 ? 0.2495 0.1456 0.1864 0.0454  0.0161  0.0448  319 TYR A CA  
2237 C C   . TYR A 319 ? 0.2548 0.1670 0.1974 0.0461  0.0203  0.0467  319 TYR A C   
2238 O O   . TYR A 319 ? 0.2721 0.2038 0.2294 0.0415  0.0190  0.0513  319 TYR A O   
2239 C CB  . TYR A 319 ? 0.2574 0.1577 0.2064 0.0480  0.0189  0.0526  319 TYR A CB  
2240 C CG  . TYR A 319 ? 0.3043 0.1847 0.2463 0.0487  0.0157  0.0504  319 TYR A CG  
2241 C CD1 . TYR A 319 ? 0.2965 0.1781 0.2438 0.0401  0.0079  0.0505  319 TYR A CD1 
2242 C CD2 . TYR A 319 ? 0.3595 0.2179 0.2883 0.0582  0.0205  0.0476  319 TYR A CD2 
2243 C CE1 . TYR A 319 ? 0.3450 0.2073 0.2879 0.0399  0.0040  0.0486  319 TYR A CE1 
2244 C CE2 . TYR A 319 ? 0.4276 0.2648 0.3491 0.0586  0.0163  0.0444  319 TYR A CE2 
2245 C CZ  . TYR A 319 ? 0.4081 0.2477 0.3380 0.0489  0.0075  0.0451  319 TYR A CZ  
2246 O OH  . TYR A 319 ? 0.5091 0.3276 0.4346 0.0484  0.0025  0.0425  319 TYR A OH  
2247 N N   . GLN A 320 ? 0.2525 0.1554 0.1827 0.0521  0.0250  0.0432  320 GLN A N   
2248 C CA  . GLN A 320 ? 0.2490 0.1659 0.1857 0.0532  0.0297  0.0457  320 GLN A CA  
2249 C C   . GLN A 320 ? 0.2533 0.1810 0.2055 0.0591  0.0376  0.0547  320 GLN A C   
2250 O O   . GLN A 320 ? 0.2590 0.1758 0.2076 0.0680  0.0445  0.0575  320 GLN A O   
2251 C CB  . GLN A 320 ? 0.2872 0.1893 0.2050 0.0594  0.0336  0.0407  320 GLN A CB  
2252 C CG  . GLN A 320 ? 0.2741 0.1897 0.1986 0.0598  0.0379  0.0432  320 GLN A CG  
2253 C CD  . GLN A 320 ? 0.2818 0.1819 0.1855 0.0669  0.0424  0.0392  320 GLN A CD  
2254 O OE1 . GLN A 320 ? 0.3171 0.2010 0.2067 0.0774  0.0498  0.0395  320 GLN A OE1 
2255 N NE2 . GLN A 320 ? 0.2856 0.1900 0.1862 0.0623  0.0384  0.0359  320 GLN A NE2 
2256 N N   . ILE A 321 ? 0.2206 0.1690 0.1905 0.0545  0.0364  0.0594  321 ILE A N   
2257 C CA  . ILE A 321 ? 0.2257 0.1869 0.2144 0.0590  0.0422  0.0687  321 ILE A CA  
2258 C C   . ILE A 321 ? 0.2244 0.1959 0.2222 0.0605  0.0470  0.0718  321 ILE A C   
2259 O O   . ILE A 321 ? 0.2194 0.1992 0.2334 0.0660  0.0538  0.0805  321 ILE A O   
2260 C CB  . ILE A 321 ? 0.1932 0.1696 0.1986 0.0529  0.0354  0.0737  321 ILE A CB  
2261 C CG1 . ILE A 321 ? 0.2016 0.1912 0.2113 0.0429  0.0266  0.0706  321 ILE A CG1 
2262 C CG2 . ILE A 321 ? 0.2196 0.1853 0.2183 0.0531  0.0328  0.0730  321 ILE A CG2 
2263 C CD1 . ILE A 321 ? 0.2286 0.2334 0.2530 0.0383  0.0199  0.0760  321 ILE A CD1 
2264 N N   . SER A 322 ? 0.2053 0.1765 0.1949 0.0562  0.0441  0.0659  322 SER A N   
2265 C CA  . SER A 322 ? 0.1980 0.1779 0.1969 0.0581  0.0493  0.0697  322 SER A CA  
2266 C C   . SER A 322 ? 0.1917 0.1623 0.1730 0.0573  0.0489  0.0625  322 SER A C   
2267 O O   . SER A 322 ? 0.2278 0.1916 0.1960 0.0518  0.0413  0.0548  322 SER A O   
2268 C CB  . SER A 322 ? 0.2263 0.2269 0.2483 0.0503  0.0430  0.0736  322 SER A CB  
2269 O OG  . SER A 322 ? 0.2176 0.2209 0.2337 0.0410  0.0331  0.0663  322 SER A OG  
2270 N N   . THR A 323 ? 0.2096 0.1810 0.1926 0.0630  0.0572  0.0664  323 THR A N   
2271 C CA  . THR A 323 ? 0.2103 0.1773 0.1818 0.0624  0.0575  0.0622  323 THR A CA  
2272 C C   . THR A 323 ? 0.2015 0.1868 0.1955 0.0571  0.0564  0.0668  323 THR A C   
2273 O O   . THR A 323 ? 0.2060 0.2056 0.2218 0.0533  0.0535  0.0719  323 THR A O   
2274 C CB  . THR A 323 ? 0.2669 0.2178 0.2201 0.0746  0.0688  0.0636  323 THR A CB  
2275 O OG1 . THR A 323 ? 0.2412 0.1982 0.2098 0.0829  0.0805  0.0743  323 THR A OG1 
2276 C CG2 . THR A 323 ? 0.3060 0.2354 0.2338 0.0787  0.0669  0.0565  323 THR A CG2 
2277 N N   . ASP A 324 ? 0.1937 0.1776 0.1824 0.0573  0.0581  0.0654  324 ASP A N   
2278 C CA  . ASP A 324 ? 0.1877 0.1867 0.1964 0.0512  0.0555  0.0684  324 ASP A CA  
2279 C C   . ASP A 324 ? 0.1983 0.2118 0.2352 0.0519  0.0589  0.0785  324 ASP A C   
2280 O O   . ASP A 324 ? 0.1959 0.2227 0.2518 0.0439  0.0510  0.0792  324 ASP A O   
2281 C CB  . ASP A 324 ? 0.2000 0.1946 0.2021 0.0554  0.0620  0.0699  324 ASP A CB  
2282 C CG  . ASP A 324 ? 0.2055 0.1850 0.1798 0.0561  0.0589  0.0612  324 ASP A CG  
2283 O OD1 . ASP A 324 ? 0.2174 0.1937 0.1831 0.0498  0.0493  0.0532  324 ASP A OD1 
2284 O OD2 . ASP A 324 ? 0.2236 0.1944 0.1856 0.0636  0.0667  0.0635  324 ASP A OD2 
2285 N N   . GLY A 325 ? 0.1862 0.1971 0.2266 0.0619  0.0708  0.0869  325 GLY A N   
2286 C CA  . GLY A 325 ? 0.1912 0.2164 0.2617 0.0637  0.0758  0.0988  325 GLY A CA  
2287 C C   . GLY A 325 ? 0.1802 0.2127 0.2656 0.0632  0.0729  0.1031  325 GLY A C   
2288 O O   . GLY A 325 ? 0.1981 0.2442 0.3122 0.0636  0.0750  0.1136  325 GLY A O   
2289 N N   . GLY A 326 ? 0.1940 0.2178 0.2628 0.0629  0.0686  0.0968  326 GLY A N   
2290 C CA  . GLY A 326 ? 0.2535 0.2849 0.3373 0.0621  0.0651  0.1016  326 GLY A CA  
2291 C C   . GLY A 326 ? 0.2405 0.2575 0.3049 0.0680  0.0681  0.0984  326 GLY A C   
2292 O O   . GLY A 326 ? 0.2117 0.2120 0.2495 0.0709  0.0701  0.0906  326 GLY A O   
2293 N N   . LEU A 327 ? 0.2054 0.2290 0.2848 0.0691  0.0671  0.1046  327 LEU A N   
2294 C CA  . LEU A 327 ? 0.2220 0.2335 0.2869 0.0731  0.0678  0.1020  327 LEU A CA  
2295 C C   . LEU A 327 ? 0.2573 0.2519 0.3068 0.0862  0.0822  0.1036  327 LEU A C   
2296 O O   . LEU A 327 ? 0.2678 0.2657 0.3273 0.0939  0.0938  0.1116  327 LEU A O   
2297 C CB  . LEU A 327 ? 0.2435 0.2670 0.3303 0.0722  0.0640  0.1100  327 LEU A CB  
2298 C CG  . LEU A 327 ? 0.2075 0.2438 0.3033 0.0603  0.0485  0.1076  327 LEU A CG  
2299 C CD1 . LEU A 327 ? 0.2106 0.2614 0.3333 0.0606  0.0452  0.1184  327 LEU A CD1 
2300 C CD2 . LEU A 327 ? 0.2309 0.2569 0.3041 0.0551  0.0410  0.0977  327 LEU A CD2 
2301 N N   . LEU A 328 ? 0.2566 0.2325 0.2812 0.0886  0.0811  0.0957  328 LEU A N   
2302 C CA  . LEU A 328 ? 0.2943 0.2500 0.2996 0.1015  0.0931  0.0954  328 LEU A CA  
2303 C C   . LEU A 328 ? 0.3182 0.2782 0.3376 0.1066  0.0997  0.1028  328 LEU A C   
2304 O O   . LEU A 328 ? 0.2980 0.2745 0.3412 0.1013  0.0939  0.1087  328 LEU A O   
2305 C CB  . LEU A 328 ? 0.3050 0.2385 0.2794 0.1003  0.0871  0.0830  328 LEU A CB  
2306 C CG  . LEU A 328 ? 0.2786 0.2103 0.2395 0.0912  0.0775  0.0735  328 LEU A CG  
2307 C CD1 . LEU A 328 ? 0.3246 0.2359 0.2609 0.0890  0.0698  0.0629  328 LEU A CD1 
2308 C CD2 . LEU A 328 ? 0.2939 0.2218 0.2455 0.0972  0.0858  0.0741  328 LEU A CD2 
2309 N N   . THR A 329 ? 0.3503 0.2953 0.3530 0.1164  0.1112  0.1019  329 THR A N   
2310 C CA  . THR A 329 ? 0.3390 0.2860 0.3519 0.1208  0.1176  0.1080  329 THR A CA  
2311 C C   . THR A 329 ? 0.3256 0.2664 0.3366 0.1175  0.1079  0.1041  329 THR A C   
2312 O O   . THR A 329 ? 0.3277 0.2801 0.3589 0.1162  0.1071  0.1108  329 THR A O   
2313 C CB  . THR A 329 ? 0.4139 0.3432 0.4053 0.1322  0.1318  0.1080  329 THR A CB  
2314 O OG1 . THR A 329 ? 0.5517 0.4554 0.5077 0.1355  0.1289  0.0960  329 THR A OG1 
2315 C CG2 . THR A 329 ? 0.4734 0.4120 0.4722 0.1353  0.1429  0.1165  329 THR A CG2 
2316 N N   . GLU A 330 ? 0.3172 0.2396 0.3044 0.1159  0.1005  0.0940  330 GLU A N   
2317 C CA  . GLU A 330 ? 0.3148 0.2280 0.2975 0.1126  0.0918  0.0903  330 GLU A CA  
2318 C C   . GLU A 330 ? 0.3465 0.2482 0.3108 0.1058  0.0809  0.0809  330 GLU A C   
2319 O O   . GLU A 330 ? 0.3186 0.2139 0.2675 0.1059  0.0816  0.0750  330 GLU A O   
2320 C CB  . GLU A 330 ? 0.3665 0.2606 0.3347 0.1214  0.0992  0.0880  330 GLU A CB  
2321 C CG  . GLU A 330 ? 0.4752 0.3401 0.4086 0.1261  0.0992  0.0765  330 GLU A CG  
2322 C CD  . GLU A 330 ? 0.5942 0.4403 0.5145 0.1340  0.1049  0.0743  330 GLU A CD  
2323 O OE1 . GLU A 330 ? 0.5865 0.4308 0.5023 0.1429  0.1175  0.0780  330 GLU A OE1 
2324 O OE2 . GLU A 330 ? 0.6936 0.5273 0.6092 0.1313  0.0971  0.0699  330 GLU A OE2 
2325 N N   . PRO A 331 ? 0.3041 0.2081 0.2716 0.0965  0.0697  0.0783  331 PRO A N   
2326 C CA  . PRO A 331 ? 0.2949 0.1930 0.2483 0.0866  0.0587  0.0683  331 PRO A CA  
2327 C C   . PRO A 331 ? 0.3145 0.1844 0.2394 0.0920  0.0595  0.0588  331 PRO A C   
2328 O O   . PRO A 331 ? 0.3837 0.2347 0.2978 0.1017  0.0656  0.0584  331 PRO A O   
2329 C CB  . PRO A 331 ? 0.3000 0.2044 0.2637 0.0784  0.0495  0.0700  331 PRO A CB  
2330 C CG  . PRO A 331 ? 0.2729 0.1943 0.2599 0.0813  0.0536  0.0813  331 PRO A CG  
2331 C CD  . PRO A 331 ? 0.2872 0.2010 0.2732 0.0945  0.0668  0.0856  331 PRO A CD  
2332 N N   . VAL A 332 ? 0.2881 0.1652 0.2368 0.0768  0.0183  0.0412  332 VAL A N   
2333 C CA  . VAL A 332 ? 0.3630 0.2137 0.2942 0.0773  0.0177  0.0303  332 VAL A CA  
2334 C C   . VAL A 332 ? 0.3185 0.1615 0.2488 0.0682  0.0085  0.0283  332 VAL A C   
2335 O O   . VAL A 332 ? 0.3005 0.1576 0.2334 0.0595  0.0029  0.0294  332 VAL A O   
2336 C CB  . VAL A 332 ? 0.3797 0.2304 0.2968 0.0764  0.0195  0.0227  332 VAL A CB  
2337 C CG1 . VAL A 332 ? 0.4349 0.2600 0.3322 0.0763  0.0168  0.0113  332 VAL A CG1 
2338 C CG2 . VAL A 332 ? 0.3810 0.2397 0.3008 0.0855  0.0299  0.0258  332 VAL A CG2 
2339 N N   . GLU A 333 ? 0.3387 0.1591 0.2660 0.0702  0.0074  0.0253  333 GLU A N   
2340 C CA  . GLU A 333 ? 0.3353 0.1467 0.2629 0.0612  -0.0011 0.0231  333 GLU A CA  
2341 C C   . GLU A 333 ? 0.3443 0.1493 0.2569 0.0551  -0.0065 0.0124  333 GLU A C   
2342 O O   . GLU A 333 ? 0.4063 0.1946 0.3032 0.0595  -0.0048 0.0030  333 GLU A O   
2343 C CB  . GLU A 333 ? 0.4161 0.2020 0.3443 0.0646  -0.0008 0.0213  333 GLU A CB  
2344 C CG  . GLU A 333 ? 0.4088 0.1900 0.3456 0.0554  -0.0084 0.0240  333 GLU A CG  
2345 C CD  . GLU A 333 ? 0.5315 0.2874 0.4725 0.0588  -0.0074 0.0239  333 GLU A CD  
2346 O OE1 . GLU A 333 ? 0.5681 0.3285 0.5236 0.0628  -0.0038 0.0354  333 GLU A OE1 
2347 O OE2 . GLU A 333 ? 0.5818 0.3159 0.5127 0.0571  -0.0104 0.0122  333 GLU A OE2 
2348 N N   . LEU A 334 ? 0.3101 0.1281 0.2272 0.0457  -0.0129 0.0140  334 LEU A N   
2349 C CA  . LEU A 334 ? 0.3236 0.1378 0.2298 0.0396  -0.0191 0.0056  334 LEU A CA  
2350 C C   . LEU A 334 ? 0.3241 0.1350 0.2379 0.0305  -0.0272 0.0062  334 LEU A C   
2351 O O   . LEU A 334 ? 0.3303 0.1503 0.2587 0.0275  -0.0274 0.0151  334 LEU A O   
2352 C CB  . LEU A 334 ? 0.3258 0.1609 0.2316 0.0368  -0.0185 0.0069  334 LEU A CB  
2353 C CG  . LEU A 334 ? 0.3030 0.1466 0.2056 0.0438  -0.0104 0.0082  334 LEU A CG  
2354 C CD1 . LEU A 334 ? 0.3081 0.1705 0.2126 0.0391  -0.0110 0.0094  334 LEU A CD1 
2355 C CD2 . LEU A 334 ? 0.3801 0.2053 0.2654 0.0508  -0.0068 0.0001  334 LEU A CD2 
2356 N N   . THR A 335 ? 0.3512 0.1503 0.2554 0.0262  -0.0338 -0.0027 335 THR A N   
2357 C CA  . THR A 335 ? 0.3463 0.1482 0.2592 0.0164  -0.0420 -0.0019 335 THR A CA  
2358 C C   . THR A 335 ? 0.3445 0.1578 0.2525 0.0119  -0.0462 -0.0053 335 THR A C   
2359 O O   . THR A 335 ? 0.3602 0.1800 0.2775 0.0042  -0.0521 -0.0036 335 THR A O   
2360 C CB  . THR A 335 ? 0.4032 0.1816 0.3150 0.0132  -0.0483 -0.0082 335 THR A CB  
2361 O OG1 . THR A 335 ? 0.4701 0.2324 0.3621 0.0164  -0.0509 -0.0201 335 THR A OG1 
2362 C CG2 . THR A 335 ? 0.3749 0.1407 0.2946 0.0174  -0.0437 -0.0036 335 THR A CG2 
2363 N N   . THR A 336 ? 0.3213 0.1372 0.2161 0.0168  -0.0429 -0.0093 336 THR A N   
2364 C CA  A THR A 336 ? 0.3486 0.1754 0.2393 0.0138  -0.0457 -0.0112 336 THR A CA  
2365 C CA  B THR A 336 ? 0.3464 0.1736 0.2373 0.0138  -0.0457 -0.0111 336 THR A CA  
2366 C C   . THR A 336 ? 0.3491 0.1876 0.2356 0.0192  -0.0377 -0.0089 336 THR A C   
2367 O O   . THR A 336 ? 0.3333 0.1662 0.2137 0.0263  -0.0313 -0.0092 336 THR A O   
2368 C CB  A THR A 336 ? 0.4114 0.2222 0.2869 0.0136  -0.0525 -0.0207 336 THR A CB  
2369 C CB  B THR A 336 ? 0.3843 0.1979 0.2603 0.0130  -0.0528 -0.0203 336 THR A CB  
2370 O OG1 A THR A 336 ? 0.4705 0.2770 0.3547 0.0057  -0.0619 -0.0220 336 THR A OG1 
2371 O OG1 B THR A 336 ? 0.4031 0.2019 0.2611 0.0210  -0.0488 -0.0262 336 THR A OG1 
2372 C CG2 A THR A 336 ? 0.3632 0.1814 0.2290 0.0149  -0.0526 -0.0226 336 THR A CG2 
2373 C CG2 B THR A 336 ? 0.4767 0.2790 0.3586 0.0064  -0.0622 -0.0234 336 THR A CG2 
2374 N N   . LEU A 337 ? 0.2934 0.1478 0.1843 0.0158  -0.0378 -0.0065 337 LEU A N   
2375 C CA  . LEU A 337 ? 0.2897 0.1550 0.1787 0.0194  -0.0309 -0.0044 337 LEU A CA  
2376 C C   . LEU A 337 ? 0.2724 0.1424 0.1563 0.0175  -0.0328 -0.0068 337 LEU A C   
2377 O O   . LEU A 337 ? 0.2800 0.1623 0.1732 0.0125  -0.0346 -0.0044 337 LEU A O   
2378 C CB  . LEU A 337 ? 0.2677 0.1501 0.1710 0.0176  -0.0273 0.0027  337 LEU A CB  
2379 C CG  . LEU A 337 ? 0.2806 0.1763 0.1856 0.0194  -0.0214 0.0047  337 LEU A CG  
2380 C CD1 . LEU A 337 ? 0.3041 0.1922 0.2007 0.0268  -0.0152 0.0035  337 LEU A CD1 
2381 C CD2 . LEU A 337 ? 0.2825 0.1950 0.2005 0.0169  -0.0199 0.0108  337 LEU A CD2 
2382 N N   . PRO A 338 ? 0.2866 0.1467 0.1553 0.0219  -0.0321 -0.0111 338 PRO A N   
2383 C CA  . PRO A 338 ? 0.2767 0.1417 0.1409 0.0213  -0.0326 -0.0115 338 PRO A CA  
2384 C C   . PRO A 338 ? 0.2567 0.1346 0.1273 0.0222  -0.0248 -0.0073 338 PRO A C   
2385 O O   . PRO A 338 ? 0.2997 0.1791 0.1707 0.0261  -0.0179 -0.0053 338 PRO A O   
2386 C CB  . PRO A 338 ? 0.3377 0.1874 0.1819 0.0264  -0.0341 -0.0166 338 PRO A CB  
2387 C CG  . PRO A 338 ? 0.4187 0.2567 0.2564 0.0313  -0.0308 -0.0190 338 PRO A CG  
2388 C CD  . PRO A 338 ? 0.3274 0.1703 0.1813 0.0281  -0.0307 -0.0157 338 PRO A CD  
2389 N N   . LEU A 339 ? 0.2431 0.1306 0.1202 0.0183  -0.0260 -0.0060 339 LEU A N   
2390 C CA  . LEU A 339 ? 0.2422 0.1404 0.1259 0.0179  -0.0197 -0.0032 339 LEU A CA  
2391 C C   . LEU A 339 ? 0.2641 0.1625 0.1452 0.0173  -0.0205 -0.0035 339 LEU A C   
2392 O O   . LEU A 339 ? 0.2648 0.1667 0.1513 0.0137  -0.0255 -0.0040 339 LEU A O   
2393 C CB  . LEU A 339 ? 0.2498 0.1618 0.1483 0.0129  -0.0194 -0.0010 339 LEU A CB  
2394 C CG  . LEU A 339 ? 0.2660 0.1811 0.1696 0.0137  -0.0180 0.0013  339 LEU A CG  
2395 C CD1 . LEU A 339 ? 0.2696 0.1982 0.1848 0.0085  -0.0197 0.0034  339 LEU A CD1 
2396 C CD2 . LEU A 339 ? 0.2574 0.1750 0.1614 0.0178  -0.0112 0.0034  339 LEU A CD2 
2397 N N   . GLU A 340 ? 0.2474 0.1427 0.1219 0.0212  -0.0149 -0.0021 340 GLU A N   
2398 C CA  . GLU A 340 ? 0.2494 0.1454 0.1234 0.0212  -0.0137 -0.0006 340 GLU A CA  
2399 C C   . GLU A 340 ? 0.2247 0.1317 0.1135 0.0169  -0.0095 0.0006  340 GLU A C   
2400 O O   . GLU A 340 ? 0.2307 0.1453 0.1278 0.0146  -0.0070 0.0008  340 GLU A O   
2401 C CB  . GLU A 340 ? 0.2878 0.1762 0.1493 0.0271  -0.0079 0.0016  340 GLU A CB  
2402 C CG  . GLU A 340 ? 0.3020 0.1780 0.1445 0.0323  -0.0118 -0.0007 340 GLU A CG  
2403 C CD  . GLU A 340 ? 0.3152 0.1876 0.1512 0.0321  -0.0196 -0.0013 340 GLU A CD  
2404 O OE1 . GLU A 340 ? 0.3582 0.2348 0.1997 0.0315  -0.0181 0.0021  340 GLU A OE1 
2405 O OE2 . GLU A 340 ? 0.3573 0.2227 0.1837 0.0326  -0.0275 -0.0053 340 GLU A OE2 
2406 N N   . PRO A 341 ? 0.2344 0.1422 0.1266 0.0159  -0.0086 0.0015  341 PRO A N   
2407 C CA  . PRO A 341 ? 0.2196 0.1351 0.1243 0.0119  -0.0040 0.0015  341 PRO A CA  
2408 C C   . PRO A 341 ? 0.2277 0.1465 0.1359 0.0119  0.0024  0.0033  341 PRO A C   
2409 O O   . PRO A 341 ? 0.2373 0.1505 0.1384 0.0163  0.0069  0.0064  341 PRO A O   
2410 C CB  . PRO A 341 ? 0.2328 0.1437 0.1375 0.0132  -0.0024 0.0032  341 PRO A CB  
2411 C CG  . PRO A 341 ? 0.2531 0.1590 0.1494 0.0161  -0.0094 0.0034  341 PRO A CG  
2412 C CD  . PRO A 341 ? 0.2405 0.1424 0.1262 0.0182  -0.0127 0.0023  341 PRO A CD  
2413 N N   . ALA A 342 ? 0.2038 0.1328 0.1232 0.0071  0.0028  0.0016  342 ALA A N   
2414 C CA  . ALA A 342 ? 0.2026 0.1393 0.1306 0.0051  0.0072  0.0029  342 ALA A CA  
2415 C C   . ALA A 342 ? 0.1959 0.1352 0.1218 0.0082  0.0074  0.0049  342 ALA A C   
2416 O O   . ALA A 342 ? 0.2160 0.1648 0.1513 0.0064  0.0097  0.0064  342 ALA A O   
2417 C CB  . ALA A 342 ? 0.2145 0.1481 0.1458 0.0057  0.0143  0.0060  342 ALA A CB  
2418 N N   . GLU A 343 ? 0.2061 0.1375 0.1211 0.0125  0.0045  0.0048  343 GLU A N   
2419 C CA  . GLU A 343 ? 0.2085 0.1406 0.1222 0.0158  0.0048  0.0062  343 GLU A CA  
2420 C C   . GLU A 343 ? 0.2391 0.1812 0.1612 0.0117  0.0002  0.0056  343 GLU A C   
2421 O O   . GLU A 343 ? 0.2227 0.1672 0.1464 0.0077  -0.0043 0.0033  343 GLU A O   
2422 C CB  . GLU A 343 ? 0.2360 0.1544 0.1350 0.0208  0.0023  0.0048  343 GLU A CB  
2423 C CG  . GLU A 343 ? 0.2539 0.1624 0.1407 0.0269  0.0077  0.0061  343 GLU A CG  
2424 C CD  . GLU A 343 ? 0.2737 0.1689 0.1448 0.0323  0.0052  0.0036  343 GLU A CD  
2425 O OE1 . GLU A 343 ? 0.3266 0.2153 0.1908 0.0309  -0.0022 0.0003  343 GLU A OE1 
2426 O OE2 . GLU A 343 ? 0.2930 0.1845 0.1596 0.0378  0.0103  0.0045  343 GLU A OE2 
2427 N N   . ARG A 344 ? 0.2244 0.1731 0.1522 0.0134  0.0020  0.0085  344 ARG A N   
2428 C CA  . ARG A 344 ? 0.2183 0.1764 0.1526 0.0107  -0.0023 0.0095  344 ARG A CA  
2429 C C   . ARG A 344 ? 0.1969 0.1538 0.1319 0.0159  -0.0009 0.0133  344 ARG A C   
2430 O O   . ARG A 344 ? 0.2116 0.1645 0.1451 0.0213  0.0045  0.0152  344 ARG A O   
2431 C CB  . ARG A 344 ? 0.2669 0.2404 0.2120 0.0049  -0.0030 0.0093  344 ARG A CB  
2432 C CG  . ARG A 344 ? 0.2696 0.2505 0.2233 0.0052  0.0015  0.0117  344 ARG A CG  
2433 C CD  . ARG A 344 ? 0.2571 0.2392 0.2147 0.0004  0.0034  0.0086  344 ARG A CD  
2434 N NE  . ARG A 344 ? 0.1974 0.1878 0.1662 -0.0002 0.0079  0.0117  344 ARG A NE  
2435 C CZ  . ARG A 344 ? 0.1907 0.1753 0.1599 0.0026  0.0145  0.0142  344 ARG A CZ  
2436 N NH1 . ARG A 344 ? 0.2062 0.1763 0.1639 0.0057  0.0171  0.0132  344 ARG A NH1 
2437 N NH2 . ARG A 344 ? 0.1840 0.1788 0.1664 0.0021  0.0187  0.0182  344 ARG A NH2 
2438 N N   . SER A 345 ? 0.2005 0.1608 0.1381 0.0149  -0.0052 0.0150  345 SER A N   
2439 C CA  . SER A 345 ? 0.1903 0.1493 0.1303 0.0199  -0.0041 0.0194  345 SER A CA  
2440 C C   . SER A 345 ? 0.1924 0.1629 0.1398 0.0169  -0.0084 0.0233  345 SER A C   
2441 O O   . SER A 345 ? 0.2004 0.1721 0.1461 0.0123  -0.0125 0.0218  345 SER A O   
2442 C CB  . SER A 345 ? 0.2253 0.1651 0.1544 0.0241  -0.0047 0.0170  345 SER A CB  
2443 O OG  . SER A 345 ? 0.2330 0.1694 0.1648 0.0296  -0.0028 0.0208  345 SER A OG  
2444 N N   . ASP A 346 ? 0.1791 0.1585 0.1347 0.0202  -0.0071 0.0291  346 ASP A N   
2445 C CA  . ASP A 346 ? 0.1738 0.1640 0.1352 0.0186  -0.0110 0.0346  346 ASP A CA  
2446 C C   . ASP A 346 ? 0.1985 0.1758 0.1585 0.0239  -0.0106 0.0382  346 ASP A C   
2447 O O   . ASP A 346 ? 0.1978 0.1657 0.1574 0.0305  -0.0062 0.0389  346 ASP A O   
2448 C CB  . ASP A 346 ? 0.1929 0.2023 0.1656 0.0193  -0.0109 0.0399  346 ASP A CB  
2449 C CG  . ASP A 346 ? 0.1982 0.2227 0.1736 0.0122  -0.0137 0.0365  346 ASP A CG  
2450 O OD1 . ASP A 346 ? 0.2146 0.2335 0.1857 0.0088  -0.0123 0.0298  346 ASP A OD1 
2451 O OD2 . ASP A 346 ? 0.2203 0.2627 0.2033 0.0105  -0.0169 0.0405  346 ASP A OD2 
2452 N N   . VAL A 347 ? 0.1994 0.1756 0.1590 0.0211  -0.0144 0.0406  347 VAL A N   
2453 C CA  . VAL A 347 ? 0.1912 0.1541 0.1512 0.0248  -0.0144 0.0444  347 VAL A CA  
2454 C C   . VAL A 347 ? 0.2164 0.1913 0.1838 0.0239  -0.0168 0.0537  347 VAL A C   
2455 O O   . VAL A 347 ? 0.2106 0.2016 0.1790 0.0193  -0.0194 0.0553  347 VAL A O   
2456 C CB  . VAL A 347 ? 0.2311 0.1764 0.1837 0.0219  -0.0168 0.0387  347 VAL A CB  
2457 C CG1 . VAL A 347 ? 0.2186 0.1523 0.1615 0.0231  -0.0151 0.0301  347 VAL A CG1 
2458 C CG2 . VAL A 347 ? 0.2426 0.1965 0.1960 0.0147  -0.0207 0.0389  347 VAL A CG2 
2459 N N   . ILE A 348 ? 0.1951 0.1612 0.1669 0.0289  -0.0156 0.0599  348 ILE A N   
2460 C CA  . ILE A 348 ? 0.2147 0.1888 0.1929 0.0285  -0.0176 0.0700  348 ILE A CA  
2461 C C   . ILE A 348 ? 0.2363 0.1933 0.2131 0.0257  -0.0189 0.0696  348 ILE A C   
2462 O O   . ILE A 348 ? 0.2454 0.1817 0.2201 0.0283  -0.0177 0.0654  348 ILE A O   
2463 C CB  . ILE A 348 ? 0.2192 0.1973 0.2062 0.0363  -0.0153 0.0795  348 ILE A CB  
2464 C CG1 . ILE A 348 ? 0.2279 0.2280 0.2191 0.0373  -0.0155 0.0810  348 ILE A CG1 
2465 C CG2 . ILE A 348 ? 0.2440 0.2260 0.2368 0.0365  -0.0169 0.0912  348 ILE A CG2 
2466 C CD1 . ILE A 348 ? 0.2862 0.2922 0.2881 0.0459  -0.0129 0.0900  348 ILE A CD1 
2467 N N   . ILE A 349 ? 0.2157 0.1816 0.1937 0.0202  -0.0213 0.0736  349 ILE A N   
2468 C CA  . ILE A 349 ? 0.2301 0.1835 0.2109 0.0168  -0.0224 0.0759  349 ILE A CA  
2469 C C   . ILE A 349 ? 0.2378 0.1989 0.2263 0.0184  -0.0217 0.0897  349 ILE A C   
2470 O O   . ILE A 349 ? 0.2214 0.2031 0.2095 0.0178  -0.0221 0.0957  349 ILE A O   
2471 C CB  . ILE A 349 ? 0.2179 0.1757 0.1953 0.0093  -0.0246 0.0708  349 ILE A CB  
2472 C CG1 . ILE A 349 ? 0.2201 0.1690 0.1900 0.0083  -0.0256 0.0583  349 ILE A CG1 
2473 C CG2 . ILE A 349 ? 0.2375 0.1860 0.2217 0.0054  -0.0257 0.0757  349 ILE A CG2 
2474 C CD1 . ILE A 349 ? 0.2392 0.1934 0.2069 0.0020  -0.0275 0.0535  349 ILE A CD1 
2475 N N   . ASP A 350 ? 0.2410 0.1853 0.2362 0.0206  -0.0207 0.0949  350 ASP A N   
2476 C CA  . ASP A 350 ? 0.2517 0.2003 0.2555 0.0221  -0.0196 0.1094  350 ASP A CA  
2477 C C   . ASP A 350 ? 0.3019 0.2463 0.3099 0.0149  -0.0204 0.1123  350 ASP A C   
2478 O O   . ASP A 350 ? 0.3405 0.2647 0.3521 0.0119  -0.0215 0.1075  350 ASP A O   
2479 C CB  . ASP A 350 ? 0.2862 0.2183 0.2969 0.0296  -0.0171 0.1144  350 ASP A CB  
2480 C CG  . ASP A 350 ? 0.2927 0.2314 0.3117 0.0322  -0.0152 0.1283  350 ASP A CG  
2481 O OD1 . ASP A 350 ? 0.2840 0.2389 0.3029 0.0278  -0.0156 0.1342  350 ASP A OD1 
2482 O OD2 . ASP A 350 ? 0.3343 0.2638 0.3585 0.0387  -0.0126 0.1310  350 ASP A OD2 
2483 N N   . PHE A 351 ? 0.2448 0.2089 0.2522 0.0119  -0.0200 0.1198  351 PHE A N   
2484 C CA  . PHE A 351 ? 0.2595 0.2231 0.2727 0.0055  -0.0194 0.1248  351 PHE A CA  
2485 C C   . PHE A 351 ? 0.2908 0.2519 0.3138 0.0069  -0.0163 0.1373  351 PHE A C   
2486 O O   . PHE A 351 ? 0.2859 0.2489 0.3153 0.0019  -0.0147 0.1422  351 PHE A O   
2487 C CB  . PHE A 351 ? 0.2397 0.2254 0.2458 0.0017  -0.0189 0.1241  351 PHE A CB  
2488 C CG  . PHE A 351 ? 0.2352 0.2233 0.2326 -0.0007 -0.0209 0.1089  351 PHE A CG  
2489 C CD1 . PHE A 351 ? 0.2193 0.1956 0.2190 -0.0056 -0.0227 0.1001  351 PHE A CD1 
2490 C CD2 . PHE A 351 ? 0.2288 0.2315 0.2165 0.0017  -0.0215 0.1043  351 PHE A CD2 
2491 C CE1 . PHE A 351 ? 0.2212 0.1996 0.2133 -0.0071 -0.0242 0.0878  351 PHE A CE1 
2492 C CE2 . PHE A 351 ? 0.2147 0.2185 0.1957 -0.0005 -0.0228 0.0915  351 PHE A CE2 
2493 C CZ  . PHE A 351 ? 0.2054 0.1966 0.1883 -0.0045 -0.0238 0.0837  351 PHE A CZ  
2494 N N   . SER A 352 ? 0.2841 0.2426 0.3091 0.0138  -0.0149 0.1412  352 SER A N   
2495 C CA  . SER A 352 ? 0.2760 0.2355 0.3090 0.0155  -0.0116 0.1519  352 SER A CA  
2496 C C   . SER A 352 ? 0.3377 0.2752 0.3818 0.0114  -0.0107 0.1527  352 SER A C   
2497 O O   . SER A 352 ? 0.3747 0.3152 0.4267 0.0097  -0.0079 0.1619  352 SER A O   
2498 C CB  . SER A 352 ? 0.3187 0.2812 0.3522 0.0239  -0.0106 0.1561  352 SER A CB  
2499 O OG  . SER A 352 ? 0.3583 0.2997 0.3942 0.0280  -0.0108 0.1502  352 SER A OG  
2500 N N   . GLN A 353 ? 0.3338 0.2496 0.3788 0.0095  -0.0133 0.1428  353 GLN A N   
2501 C CA  . GLN A 353 ? 0.4618 0.3569 0.5171 0.0042  -0.0137 0.1414  353 GLN A CA  
2502 C C   . GLN A 353 ? 0.5449 0.4443 0.6049 -0.0052 -0.0159 0.1395  353 GLN A C   
2503 O O   . GLN A 353 ? 0.4666 0.3506 0.5364 -0.0111 -0.0175 0.1370  353 GLN A O   
2504 C CB  . GLN A 353 ? 0.5496 0.4174 0.6030 0.0066  -0.0159 0.1305  353 GLN A CB  
2505 C CG  . GLN A 353 ? 0.4862 0.3475 0.5379 0.0164  -0.0127 0.1330  353 GLN A CG  
2506 C CD  . GLN A 353 ? 0.5767 0.4435 0.6374 0.0185  -0.0088 0.1460  353 GLN A CD  
2507 O OE1 . GLN A 353 ? 0.6338 0.4859 0.7037 0.0148  -0.0080 0.1483  353 GLN A OE1 
2508 N NE2 . GLN A 353 ? 0.5663 0.4546 0.6247 0.0241  -0.0068 0.1546  353 GLN A NE2 
2509 N N   . HIS A 354 ? 0.4222 0.3425 0.4758 -0.0069 -0.0160 0.1405  354 HIS A N   
2510 C CA  . HIS A 354 ? 0.3566 0.2824 0.4141 -0.0149 -0.0178 0.1382  354 HIS A CA  
2511 C C   . HIS A 354 ? 0.3759 0.3257 0.4347 -0.0162 -0.0130 0.1485  354 HIS A C   
2512 O O   . HIS A 354 ? 0.3360 0.2982 0.3929 -0.0202 -0.0130 0.1471  354 HIS A O   
2513 C CB  . HIS A 354 ? 0.3653 0.2917 0.4119 -0.0155 -0.0222 0.1269  354 HIS A CB  
2514 C CG  . HIS A 354 ? 0.4424 0.3461 0.4852 -0.0140 -0.0265 0.1140  354 HIS A CG  
2515 N ND1 . HIS A 354 ? 0.4999 0.3814 0.5518 -0.0188 -0.0302 0.1098  354 HIS A ND1 
2516 C CD2 . HIS A 354 ? 0.4344 0.3341 0.4650 -0.0079 -0.0272 0.1047  354 HIS A CD2 
2517 C CE1 . HIS A 354 ? 0.4620 0.3263 0.5047 -0.0154 -0.0331 0.0975  354 HIS A CE1 
2518 N NE2 . HIS A 354 ? 0.5134 0.3886 0.5436 -0.0085 -0.0307 0.0949  354 HIS A NE2 
2519 N N   . LYS A 355 ? 0.3532 0.3098 0.4144 -0.0123 -0.0086 0.1587  355 LYS A N   
2520 C CA  . LYS A 355 ? 0.2777 0.2569 0.3377 -0.0123 -0.0038 0.1681  355 LYS A CA  
2521 C C   . LYS A 355 ? 0.3306 0.3122 0.4025 -0.0198 -0.0021 0.1705  355 LYS A C   
2522 O O   . LYS A 355 ? 0.3728 0.3396 0.4595 -0.0244 -0.0029 0.1716  355 LYS A O   
2523 C CB  . LYS A 355 ? 0.3721 0.3540 0.4357 -0.0074 -0.0001 0.1793  355 LYS A CB  
2524 C CG  . LYS A 355 ? 0.3530 0.3595 0.4082 -0.0042 0.0038  0.1871  355 LYS A CG  
2525 C CD  . LYS A 355 ? 0.5081 0.5174 0.5629 0.0024  0.0054  0.1961  355 LYS A CD  
2526 C CE  . LYS A 355 ? 0.5704 0.5810 0.6368 0.0013  0.0104  0.2090  355 LYS A CE  
2527 N NZ  . LYS A 355 ? 0.6244 0.6485 0.6859 0.0079  0.0126  0.2193  355 LYS A NZ  
2528 N N   . GLY A 356 ? 0.3025 0.3033 0.3683 -0.0210 0.0005  0.1712  356 GLY A N   
2529 C CA  . GLY A 356 ? 0.3353 0.3423 0.4130 -0.0272 0.0032  0.1744  356 GLY A CA  
2530 C C   . GLY A 356 ? 0.3584 0.3556 0.4431 -0.0337 -0.0019 0.1650  356 GLY A C   
2531 O O   . GLY A 356 ? 0.3955 0.3970 0.4939 -0.0394 -0.0004 0.1674  356 GLY A O   
2532 N N   . LYS A 357 ? 0.2803 0.2649 0.3568 -0.0329 -0.0080 0.1547  357 LYS A N   
2533 C CA  . LYS A 357 ? 0.2636 0.2377 0.3448 -0.0388 -0.0142 0.1448  357 LYS A CA  
2534 C C   . LYS A 357 ? 0.2379 0.2263 0.3048 -0.0366 -0.0142 0.1343  357 LYS A C   
2535 O O   . LYS A 357 ? 0.2666 0.2660 0.3179 -0.0309 -0.0117 0.1333  357 LYS A O   
2536 C CB  . LYS A 357 ? 0.3195 0.2695 0.3979 -0.0377 -0.0210 0.1348  357 LYS A CB  
2537 C CG  . LYS A 357 ? 0.4049 0.3372 0.4968 -0.0400 -0.0221 0.1370  357 LYS A CG  
2538 C CD  . LYS A 357 ? 0.5650 0.4747 0.6492 -0.0362 -0.0265 0.1279  357 LYS A CD  
2539 C CE  . LYS A 357 ? 0.5859 0.4753 0.6755 -0.0421 -0.0342 0.1157  357 LYS A CE  
2540 N NZ  . LYS A 357 ? 0.5842 0.4507 0.6649 -0.0370 -0.0366 0.1072  357 LYS A NZ  
2541 N N   . LYS A 358 ? 0.2272 0.2149 0.3002 -0.0413 -0.0176 0.1258  358 LYS A N   
2542 C CA  . LYS A 358 ? 0.2171 0.2114 0.2779 -0.0393 -0.0192 0.1131  358 LYS A CA  
2543 C C   . LYS A 358 ? 0.2348 0.2101 0.2937 -0.0405 -0.0277 0.1003  358 LYS A C   
2544 O O   . LYS A 358 ? 0.2840 0.2472 0.3561 -0.0461 -0.0327 0.0998  358 LYS A O   
2545 C CB  . LYS A 358 ? 0.2434 0.2532 0.3131 -0.0425 -0.0160 0.1144  358 LYS A CB  
2546 C CG  . LYS A 358 ? 0.2605 0.2891 0.3321 -0.0412 -0.0064 0.1278  358 LYS A CG  
2547 C CD  . LYS A 358 ? 0.2780 0.3222 0.3582 -0.0432 -0.0020 0.1282  358 LYS A CD  
2548 C CE  . LYS A 358 ? 0.3362 0.3985 0.4188 -0.0418 0.0085  0.1423  358 LYS A CE  
2549 N NZ  . LYS A 358 ? 0.3718 0.4490 0.4637 -0.0428 0.0139  0.1426  358 LYS A NZ  
2550 N N   . LEU A 359 ? 0.2149 0.1874 0.2572 -0.0355 -0.0292 0.0905  359 LEU A N   
2551 C CA  . LEU A 359 ? 0.2255 0.1806 0.2616 -0.0350 -0.0359 0.0786  359 LEU A CA  
2552 C C   . LEU A 359 ? 0.2165 0.1783 0.2434 -0.0336 -0.0370 0.0685  359 LEU A C   
2553 O O   . LEU A 359 ? 0.2043 0.1773 0.2207 -0.0297 -0.0329 0.0671  359 LEU A O   
2554 C CB  . LEU A 359 ? 0.2472 0.1913 0.2728 -0.0293 -0.0356 0.0772  359 LEU A CB  
2555 C CG  . LEU A 359 ? 0.3018 0.2407 0.3347 -0.0283 -0.0330 0.0887  359 LEU A CG  
2556 C CD1 . LEU A 359 ? 0.3517 0.2869 0.3734 -0.0208 -0.0314 0.0876  359 LEU A CD1 
2557 C CD2 . LEU A 359 ? 0.3964 0.3156 0.4416 -0.0331 -0.0374 0.0887  359 LEU A CD2 
2558 N N   . ILE A 360 ? 0.2192 0.1738 0.2501 -0.0370 -0.0431 0.0616  360 ILE A N   
2559 C CA  . ILE A 360 ? 0.2251 0.1839 0.2475 -0.0351 -0.0445 0.0527  360 ILE A CA  
2560 C C   . ILE A 360 ? 0.2100 0.1558 0.2164 -0.0305 -0.0468 0.0438  360 ILE A C   
2561 O O   . ILE A 360 ? 0.2433 0.1723 0.2475 -0.0305 -0.0512 0.0407  360 ILE A O   
2562 C CB  . ILE A 360 ? 0.2384 0.1978 0.2722 -0.0400 -0.0501 0.0504  360 ILE A CB  
2563 C CG1 . ILE A 360 ? 0.2582 0.2345 0.3089 -0.0436 -0.0455 0.0601  360 ILE A CG1 
2564 C CG2 . ILE A 360 ? 0.2368 0.1980 0.2611 -0.0370 -0.0520 0.0416  360 ILE A CG2 
2565 C CD1 . ILE A 360 ? 0.4722 0.4538 0.5370 -0.0478 -0.0502 0.0593  360 ILE A CD1 
2566 N N   . LEU A 361 ? 0.2124 0.1659 0.2081 -0.0263 -0.0431 0.0400  361 LEU A N   
2567 C CA  . LEU A 361 ? 0.2197 0.1638 0.2017 -0.0221 -0.0444 0.0318  361 LEU A CA  
2568 C C   . LEU A 361 ? 0.2290 0.1704 0.2099 -0.0233 -0.0491 0.0255  361 LEU A C   
2569 O O   . LEU A 361 ? 0.2190 0.1719 0.2019 -0.0234 -0.0469 0.0249  361 LEU A O   
2570 C CB  . LEU A 361 ? 0.2095 0.1638 0.1833 -0.0183 -0.0387 0.0313  361 LEU A CB  
2571 C CG  . LEU A 361 ? 0.2136 0.1594 0.1754 -0.0139 -0.0387 0.0247  361 LEU A CG  
2572 C CD1 . LEU A 361 ? 0.2460 0.1795 0.2051 -0.0110 -0.0391 0.0259  361 LEU A CD1 
2573 C CD2 . LEU A 361 ? 0.2454 0.2035 0.2027 -0.0120 -0.0339 0.0237  361 LEU A CD2 
2574 N N   . GLN A 362 ? 0.2245 0.1505 0.2021 -0.0239 -0.0555 0.0208  362 GLN A N   
2575 C CA  . GLN A 362 ? 0.2302 0.1523 0.2060 -0.0250 -0.0619 0.0152  362 GLN A CA  
2576 C C   . GLN A 362 ? 0.2480 0.1651 0.2076 -0.0195 -0.0606 0.0090  362 GLN A C   
2577 O O   . GLN A 362 ? 0.2536 0.1651 0.2032 -0.0154 -0.0565 0.0076  362 GLN A O   
2578 C CB  . GLN A 362 ? 0.2694 0.1758 0.2463 -0.0284 -0.0703 0.0121  362 GLN A CB  
2579 C CG  . GLN A 362 ? 0.2797 0.1875 0.2741 -0.0347 -0.0724 0.0183  362 GLN A CG  
2580 C CD  . GLN A 362 ? 0.3864 0.2760 0.3781 -0.0350 -0.0742 0.0170  362 GLN A CD  
2581 O OE1 . GLN A 362 ? 0.3981 0.2719 0.3845 -0.0364 -0.0818 0.0100  362 GLN A OE1 
2582 N NE2 . GLN A 362 ? 0.3459 0.2375 0.3408 -0.0333 -0.0675 0.0236  362 GLN A NE2 
2583 N N   . ASN A 363 ? 0.2322 0.1520 0.1906 -0.0194 -0.0641 0.0062  363 ASN A N   
2584 C CA  . ASN A 363 ? 0.2717 0.1835 0.2150 -0.0149 -0.0654 0.0007  363 ASN A CA  
2585 C C   . ASN A 363 ? 0.2829 0.1841 0.2227 -0.0168 -0.0756 -0.0034 363 ASN A C   
2586 O O   . ASN A 363 ? 0.2722 0.1800 0.2204 -0.0196 -0.0813 -0.0025 363 ASN A O   
2587 C CB  . ASN A 363 ? 0.2420 0.1647 0.1867 -0.0129 -0.0618 0.0014  363 ASN A CB  
2588 C CG  . ASN A 363 ? 0.2529 0.1679 0.1846 -0.0090 -0.0648 -0.0025 363 ASN A CG  
2589 O OD1 . ASN A 363 ? 0.2702 0.1731 0.1877 -0.0059 -0.0652 -0.0059 363 ASN A OD1 
2590 N ND2 . ASN A 363 ? 0.2534 0.1756 0.1896 -0.0083 -0.0660 -0.0013 363 ASN A ND2 
2591 N N   . THR A 364 ? 0.2847 0.1698 0.2119 -0.0150 -0.0781 -0.0082 364 THR A N   
2592 C CA  . THR A 364 ? 0.3093 0.1829 0.2317 -0.0175 -0.0889 -0.0135 364 THR A CA  
2593 C C   . THR A 364 ? 0.2870 0.1593 0.1962 -0.0141 -0.0935 -0.0171 364 THR A C   
2594 O O   . THR A 364 ? 0.3432 0.2079 0.2474 -0.0162 -0.1040 -0.0217 364 THR A O   
2595 C CB  . THR A 364 ? 0.3204 0.1750 0.2326 -0.0166 -0.0903 -0.0187 364 THR A CB  
2596 O OG1 . THR A 364 ? 0.3580 0.2052 0.2519 -0.0088 -0.0834 -0.0216 364 THR A OG1 
2597 C CG2 . THR A 364 ? 0.3236 0.1794 0.2508 -0.0199 -0.0863 -0.0135 364 THR A CG2 
2598 N N   . ASN A 365 ? 0.2969 0.1762 0.2008 -0.0091 -0.0864 -0.0149 365 ASN A N   
2599 C CA  . ASN A 365 ? 0.3094 0.1880 0.2017 -0.0053 -0.0900 -0.0164 365 ASN A CA  
2600 C C   . ASN A 365 ? 0.4135 0.3039 0.3195 -0.0087 -0.0975 -0.0134 365 ASN A C   
2601 O O   . ASN A 365 ? 0.3772 0.2666 0.2744 -0.0060 -0.1034 -0.0142 365 ASN A O   
2602 C CB  . ASN A 365 ? 0.3121 0.1954 0.1990 0.0003  -0.0797 -0.0137 365 ASN A CB  
2603 C CG  . ASN A 365 ? 0.3192 0.1918 0.1905 0.0052  -0.0728 -0.0162 365 ASN A CG  
2604 O OD1 . ASN A 365 ? 0.3570 0.2174 0.2196 0.0056  -0.0754 -0.0206 365 ASN A OD1 
2605 N ND2 . ASN A 365 ? 0.3237 0.2007 0.1929 0.0090  -0.0637 -0.0135 365 ASN A ND2 
2606 N N   . ALA A 366 ? 0.3161 0.2186 0.2435 -0.0138 -0.0968 -0.0090 366 ALA A N   
2607 C CA  . ALA A 366 ? 0.2931 0.2095 0.2365 -0.0159 -0.1013 -0.0047 366 ALA A CA  
2608 C C   . ALA A 366 ? 0.3240 0.2464 0.2875 -0.0236 -0.1068 -0.0025 366 ALA A C   
2609 O O   . ALA A 366 ? 0.3274 0.2462 0.2953 -0.0269 -0.1036 -0.0021 366 ALA A O   
2610 C CB  . ALA A 366 ? 0.2853 0.2143 0.2369 -0.0127 -0.0908 0.0001  366 ALA A CB  
2611 N N   . GLU A 367 ? 0.3231 0.2556 0.3001 -0.0263 -0.1150 0.0001  367 GLU A N   
2612 C CA  . GLU A 367 ? 0.3082 0.2503 0.3091 -0.0338 -0.1196 0.0041  367 GLU A CA  
2613 C C   . GLU A 367 ? 0.3139 0.2745 0.3338 -0.0330 -0.1102 0.0118  367 GLU A C   
2614 O O   . GLU A 367 ? 0.3108 0.2764 0.3260 -0.0268 -0.1023 0.0131  367 GLU A O   
2615 C CB  . GLU A 367 ? 0.4513 0.3958 0.4588 -0.0377 -0.1349 0.0029  367 GLU A CB  
2616 C CG  . GLU A 367 ? 0.5613 0.4905 0.5442 -0.0340 -0.1398 -0.0047 367 GLU A CG  
2617 C CD  . GLU A 367 ? 0.6201 0.5319 0.5929 -0.0367 -0.1402 -0.0109 367 GLU A CD  
2618 O OE1 . GLU A 367 ? 0.7195 0.6321 0.7086 -0.0439 -0.1442 -0.0100 367 GLU A OE1 
2619 O OE2 . GLU A 367 ? 0.7474 0.6451 0.6975 -0.0314 -0.1358 -0.0160 367 GLU A OE2 
2620 N N   . GLY A 368 ? 0.3033 0.2739 0.3456 -0.0393 -0.1110 0.0169  368 GLY A N   
2621 C CA  . GLY A 368 ? 0.2707 0.2596 0.3314 -0.0383 -0.1021 0.0243  368 GLY A CA  
2622 C C   . GLY A 368 ? 0.2092 0.1982 0.2615 -0.0344 -0.0880 0.0250  368 GLY A C   
2623 O O   . GLY A 368 ? 0.2463 0.2243 0.2864 -0.0348 -0.0852 0.0224  368 GLY A O   
2624 N N   . ASN A 369 ? 0.2297 0.2320 0.2895 -0.0303 -0.0794 0.0286  369 ASN A N   
2625 C CA  . ASN A 369 ? 0.2271 0.2318 0.2805 -0.0274 -0.0668 0.0291  369 ASN A CA  
2626 C C   . ASN A 369 ? 0.1929 0.1842 0.2231 -0.0232 -0.0641 0.0227  369 ASN A C   
2627 O O   . ASN A 369 ? 0.1933 0.1828 0.2159 -0.0228 -0.0573 0.0221  369 ASN A O   
2628 C CB  . ASN A 369 ? 0.2179 0.2380 0.2831 -0.0236 -0.0582 0.0328  369 ASN A CB  
2629 C CG  . ASN A 369 ? 0.2252 0.2606 0.3139 -0.0277 -0.0567 0.0407  369 ASN A CG  
2630 O OD1 . ASN A 369 ? 0.2869 0.3223 0.3795 -0.0325 -0.0557 0.0440  369 ASN A OD1 
2631 N ND2 . ASN A 369 ? 0.2497 0.2985 0.3548 -0.0252 -0.0553 0.0446  369 ASN A ND2 
2632 N N   . MET A 370 ? 0.1983 0.1812 0.2176 -0.0200 -0.0693 0.0186  370 MET A N   
2633 C CA  . MET A 370 ? 0.1938 0.1645 0.1928 -0.0162 -0.0664 0.0135  370 MET A CA  
2634 C C   . MET A 370 ? 0.2298 0.1877 0.2179 -0.0186 -0.0701 0.0106  370 MET A C   
2635 O O   . MET A 370 ? 0.2413 0.1901 0.2140 -0.0155 -0.0667 0.0071  370 MET A O   
2636 C CB  . MET A 370 ? 0.2194 0.1855 0.2100 -0.0114 -0.0695 0.0115  370 MET A CB  
2637 C CG  . MET A 370 ? 0.2113 0.1878 0.2116 -0.0075 -0.0638 0.0142  370 MET A CG  
2638 S SD  . MET A 370 ? 0.2216 0.2007 0.2187 -0.0051 -0.0499 0.0125  370 MET A SD  
2639 C CE  . MET A 370 ? 0.2392 0.2032 0.2154 -0.0019 -0.0487 0.0079  370 MET A CE  
2640 N N   . GLY A 371 ? 0.2115 0.1682 0.2085 -0.0239 -0.0766 0.0121  371 GLY A N   
2641 C CA  . GLY A 371 ? 0.2237 0.1682 0.2135 -0.0262 -0.0785 0.0100  371 GLY A CA  
2642 C C   . GLY A 371 ? 0.2125 0.1615 0.2072 -0.0275 -0.0705 0.0141  371 GLY A C   
2643 O O   . GLY A 371 ? 0.2224 0.1619 0.2137 -0.0290 -0.0713 0.0138  371 GLY A O   
2644 N N   . ILE A 372 ? 0.1946 0.1576 0.1964 -0.0264 -0.0626 0.0180  372 ILE A N   
2645 C CA  . ILE A 372 ? 0.2061 0.1758 0.2113 -0.0273 -0.0551 0.0226  372 ILE A CA  
2646 C C   . ILE A 372 ? 0.2000 0.1730 0.1939 -0.0227 -0.0474 0.0201  372 ILE A C   
2647 O O   . ILE A 372 ? 0.1917 0.1702 0.1851 -0.0201 -0.0446 0.0181  372 ILE A O   
2648 C CB  . ILE A 372 ? 0.1875 0.1723 0.2111 -0.0305 -0.0524 0.0296  372 ILE A CB  
2649 C CG1 . ILE A 372 ? 0.2164 0.1984 0.2543 -0.0364 -0.0607 0.0325  372 ILE A CG1 
2650 C CG2 . ILE A 372 ? 0.2050 0.1981 0.2292 -0.0304 -0.0438 0.0350  372 ILE A CG2 
2651 C CD1 . ILE A 372 ? 0.2246 0.2227 0.2839 -0.0396 -0.0588 0.0398  372 ILE A CD1 
2652 N N   . ILE A 373 ? 0.1947 0.1645 0.1808 -0.0217 -0.0441 0.0204  373 ILE A N   
2653 C CA  . ILE A 373 ? 0.1954 0.1703 0.1729 -0.0187 -0.0376 0.0184  373 ILE A CA  
2654 C C   . ILE A 373 ? 0.1867 0.1746 0.1687 -0.0198 -0.0319 0.0234  373 ILE A C   
2655 O O   . ILE A 373 ? 0.1792 0.1768 0.1610 -0.0187 -0.0268 0.0221  373 ILE A O   
2656 C CB  . ILE A 373 ? 0.1943 0.1592 0.1599 -0.0161 -0.0378 0.0154  373 ILE A CB  
2657 C CG1 . ILE A 373 ? 0.2197 0.1720 0.1780 -0.0141 -0.0423 0.0104  373 ILE A CG1 
2658 C CG2 . ILE A 373 ? 0.2072 0.1794 0.1669 -0.0142 -0.0319 0.0138  373 ILE A CG2 
2659 C CD1 . ILE A 373 ? 0.2562 0.1974 0.2038 -0.0112 -0.0422 0.0081  373 ILE A CD1 
2660 N N   . MET A 374 ? 0.1788 0.1666 0.1641 -0.0216 -0.0322 0.0292  374 MET A N   
2661 C CA  . MET A 374 ? 0.1761 0.1770 0.1636 -0.0220 -0.0266 0.0353  374 MET A CA  
2662 C C   . MET A 374 ? 0.1795 0.1782 0.1752 -0.0246 -0.0281 0.0436  374 MET A C   
2663 O O   . MET A 374 ? 0.1928 0.1788 0.1920 -0.0262 -0.0335 0.0432  374 MET A O   
2664 C CB  . MET A 374 ? 0.1867 0.1919 0.1624 -0.0193 -0.0232 0.0327  374 MET A CB  
2665 C CG  . MET A 374 ? 0.2154 0.2122 0.1861 -0.0179 -0.0257 0.0336  374 MET A CG  
2666 S SD  . MET A 374 ? 0.2050 0.2095 0.1652 -0.0154 -0.0231 0.0310  374 MET A SD  
2667 C CE  . MET A 374 ? 0.2085 0.2284 0.1694 -0.0160 -0.0198 0.0398  374 MET A CE  
2668 N N   . ARG A 375 ? 0.1733 0.1835 0.1713 -0.0249 -0.0231 0.0511  375 ARG A N   
2669 C CA  . ARG A 375 ? 0.1771 0.1857 0.1836 -0.0271 -0.0232 0.0609  375 ARG A CA  
2670 C C   . ARG A 375 ? 0.1952 0.2101 0.1938 -0.0243 -0.0197 0.0664  375 ARG A C   
2671 O O   . ARG A 375 ? 0.2014 0.2292 0.1919 -0.0223 -0.0154 0.0659  375 ARG A O   
2672 C CB  . ARG A 375 ? 0.1730 0.1923 0.1936 -0.0303 -0.0199 0.0682  375 ARG A CB  
2673 C CG  . ARG A 375 ? 0.1742 0.1889 0.2089 -0.0343 -0.0211 0.0784  375 ARG A CG  
2674 C CD  . ARG A 375 ? 0.1819 0.2095 0.2326 -0.0377 -0.0168 0.0865  375 ARG A CD  
2675 N NE  . ARG A 375 ? 0.2056 0.2499 0.2502 -0.0345 -0.0077 0.0928  375 ARG A NE  
2676 C CZ  . ARG A 375 ? 0.1931 0.2523 0.2463 -0.0350 -0.0009 0.0988  375 ARG A CZ  
2677 N NH1 . ARG A 375 ? 0.1977 0.2589 0.2692 -0.0388 -0.0023 0.1002  375 ARG A NH1 
2678 N NH2 . ARG A 375 ? 0.2105 0.2835 0.2537 -0.0314 0.0073  0.1036  375 ARG A NH2 
2679 N N   . PHE A 376 ? 0.1821 0.1880 0.1832 -0.0240 -0.0218 0.0719  376 PHE A N   
2680 C CA  . PHE A 376 ? 0.1858 0.1984 0.1823 -0.0211 -0.0190 0.0798  376 PHE A CA  
2681 C C   . PHE A 376 ? 0.2028 0.2197 0.2103 -0.0234 -0.0158 0.0931  376 PHE A C   
2682 O O   . PHE A 376 ? 0.2134 0.2185 0.2332 -0.0266 -0.0182 0.0966  376 PHE A O   
2683 C CB  . PHE A 376 ? 0.2083 0.2077 0.2017 -0.0182 -0.0224 0.0785  376 PHE A CB  
2684 C CG  . PHE A 376 ? 0.1967 0.1922 0.1802 -0.0157 -0.0245 0.0673  376 PHE A CG  
2685 C CD1 . PHE A 376 ? 0.1838 0.1915 0.1580 -0.0132 -0.0228 0.0651  376 PHE A CD1 
2686 C CD2 . PHE A 376 ? 0.1926 0.1721 0.1760 -0.0160 -0.0282 0.0594  376 PHE A CD2 
2687 C CE1 . PHE A 376 ? 0.1993 0.2037 0.1665 -0.0114 -0.0242 0.0558  376 PHE A CE1 
2688 C CE2 . PHE A 376 ? 0.2179 0.1941 0.1922 -0.0132 -0.0291 0.0506  376 PHE A CE2 
2689 C CZ  . PHE A 376 ? 0.2105 0.1993 0.1779 -0.0112 -0.0267 0.0491  376 PHE A CZ  
2690 N N   . ASP A 377 ? 0.1914 0.2249 0.1943 -0.0218 -0.0105 0.1004  377 ASP A N   
2691 C CA  . ASP A 377 ? 0.2107 0.2507 0.2232 -0.0234 -0.0059 0.1148  377 ASP A CA  
2692 C C   . ASP A 377 ? 0.2114 0.2537 0.2191 -0.0195 -0.0051 0.1249  377 ASP A C   
2693 O O   . ASP A 377 ? 0.2232 0.2795 0.2174 -0.0159 -0.0032 0.1260  377 ASP A O   
2694 C CB  . ASP A 377 ? 0.2306 0.2887 0.2404 -0.0235 0.0009  0.1174  377 ASP A CB  
2695 C CG  . ASP A 377 ? 0.2353 0.2932 0.2520 -0.0264 0.0008  0.1089  377 ASP A CG  
2696 O OD1 . ASP A 377 ? 0.2377 0.2818 0.2626 -0.0291 -0.0051 0.1025  377 ASP A OD1 
2697 O OD2 . ASP A 377 ? 0.2429 0.3150 0.2573 -0.0255 0.0072  0.1098  377 ASP A OD2 
2698 N N   . VAL A 378 ? 0.2120 0.2408 0.2308 -0.0202 -0.0067 0.1326  378 VAL A N   
2699 C CA  . VAL A 378 ? 0.2338 0.2635 0.2494 -0.0155 -0.0062 0.1427  378 VAL A CA  
2700 C C   . VAL A 378 ? 0.2303 0.2726 0.2500 -0.0150 0.0000  0.1542  378 VAL A C   
2701 O O   . VAL A 378 ? 0.2597 0.2941 0.2919 -0.0155 0.0015  0.1622  378 VAL A O   
2702 C CB  . VAL A 378 ? 0.2433 0.2510 0.2679 -0.0149 -0.0100 0.1430  378 VAL A CB  
2703 C CG1 . VAL A 378 ? 0.2335 0.2433 0.2538 -0.0080 -0.0095 0.1475  378 VAL A CG1 
2704 C CG2 . VAL A 378 ? 0.2316 0.2255 0.2531 -0.0158 -0.0153 0.1263  378 VAL A CG2 
2705 N N   . LEU A 379 ? 0.2290 0.2903 0.2364 -0.0131 0.0035  0.1537  379 LEU A N   
2706 C CA  . LEU A 379 ? 0.2395 0.3138 0.2494 -0.0128 0.0102  0.1626  379 LEU A CA  
2707 C C   . LEU A 379 ? 0.2698 0.3601 0.2637 -0.0073 0.0118  0.1637  379 LEU A C   
2708 O O   . LEU A 379 ? 0.3026 0.4039 0.2957 -0.0059 0.0173  0.1714  379 LEU A O   
2709 C CB  . LEU A 379 ? 0.2702 0.3521 0.2826 -0.0166 0.0145  0.1604  379 LEU A CB  
2710 C CG  . LEU A 379 ? 0.2966 0.3653 0.3270 -0.0231 0.0125  0.1594  379 LEU A CG  
2711 C CD1 . LEU A 379 ? 0.3199 0.4000 0.3545 -0.0260 0.0178  0.1586  379 LEU A CD1 
2712 C CD2 . LEU A 379 ? 0.3793 0.4361 0.4287 -0.0257 0.0122  0.1681  379 LEU A CD2 
2713 N N   . GLN A 380 ? 0.2645 0.3567 0.2462 -0.0045 0.0068  0.1561  380 GLN A N   
2714 C CA  . GLN A 380 ? 0.3140 0.4207 0.2817 -0.0001 0.0065  0.1563  380 GLN A CA  
2715 C C   . GLN A 380 ? 0.3531 0.4569 0.3275 0.0035  0.0054  0.1664  380 GLN A C   
2716 O O   . GLN A 380 ? 0.3100 0.4005 0.2929 0.0040  0.0018  0.1664  380 GLN A O   
2717 C CB  . GLN A 380 ? 0.2977 0.4076 0.2529 0.0006  0.0010  0.1435  380 GLN A CB  
2718 C CG  . GLN A 380 ? 0.3605 0.4853 0.3019 0.0039  -0.0006 0.1422  380 GLN A CG  
2719 C CD  . GLN A 380 ? 0.4582 0.5951 0.3881 0.0038  0.0045  0.1407  380 GLN A CD  
2720 O OE1 . GLN A 380 ? 0.5519 0.6876 0.4814 0.0012  0.0083  0.1358  380 GLN A OE1 
2721 N NE2 . GLN A 380 ? 0.5288 0.6775 0.4495 0.0070  0.0050  0.1453  380 GLN A NE2 
2722 N N   . PRO A 381 ? 0.3257 0.4406 0.2969 0.0064  0.0087  0.1755  381 PRO A N   
2723 C CA  . PRO A 381 ? 0.3010 0.4145 0.2779 0.0104  0.0074  0.1853  381 PRO A CA  
2724 C C   . PRO A 381 ? 0.3795 0.4948 0.3503 0.0134  0.0008  0.1793  381 PRO A C   
2725 O O   . PRO A 381 ? 0.3229 0.4480 0.2805 0.0133  -0.0025 0.1697  381 PRO A O   
2726 C CB  . PRO A 381 ? 0.3241 0.4528 0.2937 0.0131  0.0118  0.1945  381 PRO A CB  
2727 C CG  . PRO A 381 ? 0.4180 0.5533 0.3817 0.0102  0.0169  0.1907  381 PRO A CG  
2728 C CD  . PRO A 381 ? 0.3451 0.4705 0.3126 0.0057  0.0153  0.1800  381 PRO A CD  
2729 N N   . LEU A 382 ? 0.3100 0.4151 0.2916 0.0161  -0.0010 0.1848  382 LEU A N   
2730 C CA  . LEU A 382 ? 0.3189 0.4263 0.2982 0.0196  -0.0064 0.1811  382 LEU A CA  
2731 C C   . LEU A 382 ? 0.3880 0.5158 0.3552 0.0224  -0.0088 0.1828  382 LEU A C   
2732 O O   . LEU A 382 ? 0.3633 0.4993 0.3294 0.0249  -0.0062 0.1934  382 LEU A O   
2733 C CB  . LEU A 382 ? 0.3609 0.4549 0.3546 0.0231  -0.0061 0.1892  382 LEU A CB  
2734 C CG  . LEU A 382 ? 0.3488 0.4397 0.3456 0.0272  -0.0104 0.1863  382 LEU A CG  
2735 C CD1 . LEU A 382 ? 0.3230 0.4061 0.3173 0.0247  -0.0133 0.1732  382 LEU A CD1 
2736 C CD2 . LEU A 382 ? 0.3761 0.4520 0.3871 0.0311  -0.0082 0.1954  382 LEU A CD2 
2737 N N   . ARG A 383 ? 0.3332 0.4689 0.2913 0.0219  -0.0140 0.1722  383 ARG A N   
2738 C CA  . ARG A 383 ? 0.3973 0.5514 0.3437 0.0237  -0.0180 0.1714  383 ARG A CA  
2739 C C   . ARG A 383 ? 0.3870 0.5439 0.3411 0.0279  -0.0226 0.1758  383 ARG A C   
2740 O O   . ARG A 383 ? 0.6023 0.7640 0.5549 0.0275  -0.0278 0.1678  383 ARG A O   
2741 C CB  . ARG A 383 ? 0.4392 0.5995 0.3728 0.0198  -0.0213 0.1565  383 ARG A CB  
2742 C CG  . ARG A 383 ? 0.4880 0.6507 0.4103 0.0166  -0.0171 0.1514  383 ARG A CG  
2743 C CD  . ARG A 383 ? 0.4685 0.6301 0.3835 0.0126  -0.0198 0.1355  383 ARG A CD  
2744 N NE  . ARG A 383 ? 0.5444 0.7002 0.4565 0.0096  -0.0144 0.1307  383 ARG A NE  
2745 C CZ  . ARG A 383 ? 0.5584 0.7059 0.4716 0.0062  -0.0147 0.1204  383 ARG A CZ  
2746 N NH1 . ARG A 383 ? 0.6175 0.7598 0.5357 0.0054  -0.0196 0.1144  383 ARG A NH1 
2747 N NH2 . ARG A 383 ? 0.5880 0.7332 0.4979 0.0039  -0.0096 0.1168  383 ARG A NH2 
2748 N N   . GLY A 384 ? 0.4869 0.6408 0.4507 0.0322  -0.0202 0.1890  384 GLY A N   
2749 C CA  . GLY A 384 ? 0.4498 0.6063 0.4224 0.0371  -0.0234 0.1947  384 GLY A CA  
2750 C C   . GLY A 384 ? 0.4143 0.5543 0.3994 0.0380  -0.0233 0.1909  384 GLY A C   
2751 O O   . GLY A 384 ? 0.4205 0.5487 0.4055 0.0344  -0.0224 0.1816  384 GLY A O   
2752 N N   . ARG A 385 ? 0.3928 0.5325 0.3886 0.0436  -0.0242 0.1984  385 ARG A N   
2753 C CA  . ARG A 385 ? 0.3499 0.4709 0.3587 0.0464  -0.0220 0.1980  385 ARG A CA  
2754 C C   . ARG A 385 ? 0.3268 0.4445 0.3342 0.0444  -0.0249 0.1853  385 ARG A C   
2755 O O   . ARG A 385 ? 0.3713 0.5048 0.3734 0.0433  -0.0297 0.1798  385 ARG A O   
2756 C CB  . ARG A 385 ? 0.3696 0.4929 0.3897 0.0537  -0.0219 0.2090  385 ARG A CB  
2757 C CG  . ARG A 385 ? 0.4892 0.5890 0.5227 0.0575  -0.0175 0.2111  385 ARG A CG  
2758 C CD  . ARG A 385 ? 0.5110 0.6131 0.5564 0.0656  -0.0169 0.2214  385 ARG A CD  
2759 N NE  . ARG A 385 ? 0.5564 0.6700 0.6046 0.0686  -0.0207 0.2174  385 ARG A NE  
2760 C CZ  . ARG A 385 ? 0.5679 0.6699 0.6217 0.0705  -0.0196 0.2099  385 ARG A CZ  
2761 N NH1 . ARG A 385 ? 0.5724 0.6498 0.6277 0.0696  -0.0156 0.2043  385 ARG A NH1 
2762 N NH2 . ARG A 385 ? 0.6271 0.7429 0.6849 0.0732  -0.0227 0.2080  385 ARG A NH2 
2763 N N   . ASP A 386 ? 0.2911 0.3879 0.3033 0.0435  -0.0219 0.1804  386 ASP A N   
2764 C CA  . ASP A 386 ? 0.2670 0.3578 0.2796 0.0430  -0.0236 0.1700  386 ASP A CA  
2765 C C   . ASP A 386 ? 0.2669 0.3598 0.2898 0.0499  -0.0242 0.1736  386 ASP A C   
2766 O O   . ASP A 386 ? 0.3438 0.4214 0.3765 0.0550  -0.0205 0.1787  386 ASP A O   
2767 C CB  . ASP A 386 ? 0.2590 0.3253 0.2736 0.0411  -0.0203 0.1652  386 ASP A CB  
2768 C CG  . ASP A 386 ? 0.2622 0.3225 0.2745 0.0401  -0.0217 0.1542  386 ASP A CG  
2769 O OD1 . ASP A 386 ? 0.2682 0.3432 0.2795 0.0412  -0.0249 0.1510  386 ASP A OD1 
2770 O OD2 . ASP A 386 ? 0.2581 0.2983 0.2710 0.0387  -0.0198 0.1495  386 ASP A OD2 
2771 N N   . THR A 387 ? 0.3119 0.4234 0.3336 0.0500  -0.0286 0.1707  387 THR A N   
2772 C CA  . THR A 387 ? 0.2926 0.4091 0.3259 0.0563  -0.0290 0.1742  387 THR A CA  
2773 C C   . THR A 387 ? 0.2829 0.3915 0.3192 0.0569  -0.0283 0.1653  387 THR A C   
2774 O O   . THR A 387 ? 0.2925 0.4058 0.3393 0.0624  -0.0277 0.1675  387 THR A O   
2775 C CB  . THR A 387 ? 0.2843 0.4275 0.3172 0.0562  -0.0347 0.1780  387 THR A CB  
2776 O OG1 . THR A 387 ? 0.4269 0.5820 0.4493 0.0492  -0.0396 0.1678  387 THR A OG1 
2777 C CG2 . THR A 387 ? 0.3520 0.5027 0.3819 0.0572  -0.0349 0.1884  387 THR A CG2 
2778 N N   . SER A 388 ? 0.2511 0.3488 0.2790 0.0518  -0.0278 0.1559  388 SER A N   
2779 C CA  . SER A 388 ? 0.2319 0.3210 0.2614 0.0527  -0.0266 0.1479  388 SER A CA  
2780 C C   . SER A 388 ? 0.2802 0.3454 0.3170 0.0594  -0.0207 0.1495  388 SER A C   
2781 O O   . SER A 388 ? 0.2691 0.3199 0.3076 0.0611  -0.0179 0.1544  388 SER A O   
2782 C CB  . SER A 388 ? 0.2418 0.3270 0.2594 0.0453  -0.0282 0.1379  388 SER A CB  
2783 O OG  . SER A 388 ? 0.2496 0.3142 0.2631 0.0436  -0.0252 0.1370  388 SER A OG  
2784 N N   . GLU A 389 ? 0.2596 0.3198 0.3005 0.0635  -0.0184 0.1449  389 GLU A N   
2785 C CA  . GLU A 389 ? 0.2748 0.3112 0.3207 0.0706  -0.0121 0.1440  389 GLU A CA  
2786 C C   . GLU A 389 ? 0.2920 0.3162 0.3324 0.0707  -0.0098 0.1341  389 GLU A C   
2787 O O   . GLU A 389 ? 0.3483 0.3873 0.3870 0.0681  -0.0123 0.1305  389 GLU A O   
2788 C CB  . GLU A 389 ? 0.2809 0.3235 0.3404 0.0795  -0.0087 0.1510  389 GLU A CB  
2789 C CG  . GLU A 389 ? 0.3298 0.3837 0.3956 0.0810  -0.0103 0.1620  389 GLU A CG  
2790 C CD  . GLU A 389 ? 0.5207 0.5869 0.6010 0.0892  -0.0082 0.1697  389 GLU A CD  
2791 O OE1 . GLU A 389 ? 0.5277 0.5916 0.6142 0.0945  -0.0041 0.1664  389 GLU A OE1 
2792 O OE2 . GLU A 389 ? 0.5764 0.6545 0.6622 0.0908  -0.0100 0.1796  389 GLU A OE2 
2793 N N   . ILE A 390 ? 0.2782 0.2744 0.3151 0.0734  -0.0054 0.1295  390 ILE A N   
2794 C CA  . ILE A 390 ? 0.2717 0.2529 0.3031 0.0760  -0.0013 0.1195  390 ILE A CA  
2795 C C   . ILE A 390 ? 0.2883 0.2686 0.3296 0.0867  0.0051  0.1224  390 ILE A C   
2796 O O   . ILE A 390 ? 0.3215 0.2864 0.3668 0.0920  0.0089  0.1242  390 ILE A O   
2797 C CB  . ILE A 390 ? 0.3039 0.2557 0.3249 0.0727  -0.0001 0.1101  390 ILE A CB  
2798 C CG1 . ILE A 390 ? 0.3242 0.2799 0.3374 0.0614  -0.0060 0.1068  390 ILE A CG1 
2799 C CG2 . ILE A 390 ? 0.3495 0.2864 0.3618 0.0747  0.0042  0.0971  390 ILE A CG2 
2800 C CD1 . ILE A 390 ? 0.4178 0.3499 0.4282 0.0583  -0.0065 0.1049  390 ILE A CD1 
2801 N N   . PRO A 391 ? 0.2453 0.2422 0.2916 0.0892  0.0067  0.1219  391 PRO A N   
2802 C CA  . PRO A 391 ? 0.2947 0.2969 0.3537 0.0988  0.0128  0.1265  391 PRO A CA  
2803 C C   . PRO A 391 ? 0.2802 0.2556 0.3335 0.1064  0.0219  0.1184  391 PRO A C   
2804 O O   . PRO A 391 ? 0.3123 0.2685 0.3510 0.1039  0.0230  0.1080  391 PRO A O   
2805 C CB  . PRO A 391 ? 0.3111 0.3415 0.3784 0.0975  0.0108  0.1287  391 PRO A CB  
2806 C CG  . PRO A 391 ? 0.3166 0.3461 0.3696 0.0857  0.0066  0.1169  391 PRO A CG  
2807 C CD  . PRO A 391 ? 0.2368 0.2489 0.2773 0.0802  0.0030  0.1138  391 PRO A CD  
2808 N N   . ALA A 392 ? 0.2843 0.2595 0.3480 0.1152  0.0283  0.1223  392 ALA A N   
2809 C CA  . ALA A 392 ? 0.3427 0.2948 0.4003 0.1231  0.0378  0.1142  392 ALA A CA  
2810 C C   . ALA A 392 ? 0.3817 0.3403 0.4367 0.1254  0.0430  0.1092  392 ALA A C   
2811 O O   . ALA A 392 ? 0.3954 0.3324 0.4363 0.1283  0.0489  0.0988  392 ALA A O   
2812 C CB  . ALA A 392 ? 0.3240 0.2761 0.3943 0.1321  0.0436  0.1205  392 ALA A CB  
2813 N N   . LYS A 393 ? 0.2745 0.2631 0.3428 0.1239  0.0409  0.1164  393 LYS A N   
2814 C CA  . LYS A 393 ? 0.2976 0.2957 0.3657 0.1238  0.0449  0.1125  393 LYS A CA  
2815 C C   . LYS A 393 ? 0.3467 0.3706 0.4185 0.1111  0.0350  0.1132  393 LYS A C   
2816 O O   . LYS A 393 ? 0.3162 0.3595 0.3985 0.1080  0.0272  0.1220  393 LYS A O   
2817 C CB  . LYS A 393 ? 0.3849 0.3953 0.4685 0.1331  0.0543  0.1177  393 LYS A CB  
2818 C CG  . LYS A 393 ? 0.3868 0.4282 0.4929 0.1323  0.0497  0.1301  393 LYS A CG  
2819 C CD  . LYS A 393 ? 0.3207 0.3763 0.4429 0.1394  0.0589  0.1348  393 LYS A CD  
2820 C CE  . LYS A 393 ? 0.3746 0.4560 0.5178 0.1398  0.0544  0.1471  393 LYS A CE  
2821 N NZ  . LYS A 393 ? 0.4592 0.5697 0.6117 0.1296  0.0426  0.1513  393 LYS A NZ  
2822 N N   . LEU A 394 ? 0.2597 0.2836 0.3224 0.1041  0.0356  0.1038  394 LEU A N   
2823 C CA  . LEU A 394 ? 0.3400 0.3858 0.4059 0.0921  0.0272  0.1027  394 LEU A CA  
2824 C C   . LEU A 394 ? 0.3331 0.4042 0.4173 0.0923  0.0296  0.1073  394 LEU A C   
2825 O O   . LEU A 394 ? 0.4153 0.5123 0.5138 0.0877  0.0222  0.1139  394 LEU A O   
2826 C CB  . LEU A 394 ? 0.2651 0.2963 0.3114 0.0827  0.0245  0.0903  394 LEU A CB  
2827 C CG  . LEU A 394 ? 0.2512 0.2622 0.2826 0.0800  0.0200  0.0864  394 LEU A CG  
2828 C CD1 . LEU A 394 ? 0.2581 0.2476 0.2706 0.0764  0.0215  0.0744  394 LEU A CD1 
2829 C CD2 . LEU A 394 ? 0.2743 0.3021 0.3085 0.0713  0.0099  0.0901  394 LEU A CD2 
2830 N N   . ILE A 395 ? 0.4300 0.4950 0.5138 0.0967  0.0396  0.1039  395 ILE A N   
2831 C CA  . ILE A 395 ? 0.3567 0.4456 0.4607 0.0969  0.0432  0.1093  395 ILE A CA  
2832 C C   . ILE A 395 ? 0.3417 0.4315 0.4591 0.1116  0.0545  0.1175  395 ILE A C   
2833 O O   . ILE A 395 ? 0.3616 0.4300 0.4700 0.1216  0.0601  0.1171  395 ILE A O   
2834 C CB  . ILE A 395 ? 0.3869 0.4754 0.4852 0.0890  0.0457  0.1015  395 ILE A CB  
2835 C CG1 . ILE A 395 ? 0.4613 0.5198 0.5352 0.0919  0.0530  0.0917  395 ILE A CG1 
2836 C CG2 . ILE A 395 ? 0.4364 0.5367 0.5331 0.0744  0.0335  0.0972  395 ILE A CG2 
2837 C CD1 . ILE A 395 ? 0.4448 0.4873 0.5147 0.1062  0.0654  0.0932  395 ILE A CD1 
2838 N N   . SER A 396 ? 0.2417 0.3576 0.3830 0.1128  0.0572  0.1255  396 SER A N   
2839 C CA  . SER A 396 ? 0.2454 0.3674 0.4041 0.1270  0.0679  0.1351  396 SER A CA  
2840 C C   . SER A 396 ? 0.2281 0.3506 0.3912 0.1314  0.0814  0.1342  396 SER A C   
2841 O O   . SER A 396 ? 0.2417 0.3658 0.4131 0.1387  0.0904  0.1392  396 SER A O   
2842 C CB  . SER A 396 ? 0.2703 0.4226 0.4536 0.1245  0.0599  0.1463  396 SER A CB  
2843 O OG  . SER A 396 ? 0.3674 0.5126 0.5447 0.1262  0.0532  0.1492  396 SER A OG  
2844 N N   . GLU A 397 ? 0.2224 0.3392 0.3732 0.1219  0.0815  0.1256  397 GLU A N   
2845 C CA  . GLU A 397 ? 0.2286 0.3437 0.3804 0.1257  0.0950  0.1249  397 GLU A CA  
2846 C C   . GLU A 397 ? 0.2393 0.3278 0.3608 0.1210  0.0964  0.1125  397 GLU A C   
2847 O O   . GLU A 397 ? 0.2599 0.3434 0.3693 0.1095  0.0851  0.1055  397 GLU A O   
2848 C CB  . GLU A 397 ? 0.2635 0.4094 0.4422 0.1177  0.0942  0.1315  397 GLU A CB  
2849 C CG  . GLU A 397 ? 0.2558 0.4320 0.4635 0.1157  0.0861  0.1419  397 GLU A CG  
2850 C CD  . GLU A 397 ? 0.2495 0.4512 0.4814 0.1069  0.0859  0.1469  397 GLU A CD  
2851 O OE1 . GLU A 397 ? 0.2647 0.4641 0.4942 0.1012  0.0908  0.1427  397 GLU A OE1 
2852 O OE2 . GLU A 397 ? 0.2146 0.4373 0.4674 0.1054  0.0807  0.1549  397 GLU A OE2 
2853 N N   . GLU A 398 ? 0.2586 0.3312 0.3679 0.1306  0.1107  0.1102  398 GLU A N   
2854 C CA  . GLU A 398 ? 0.2866 0.3355 0.3672 0.1276  0.1130  0.0996  398 GLU A CA  
2855 C C   . GLU A 398 ? 0.2668 0.3205 0.3510 0.1319  0.1274  0.1031  398 GLU A C   
2856 O O   . GLU A 398 ? 0.2944 0.3519 0.3872 0.1418  0.1384  0.1093  398 GLU A O   
2857 C CB  . GLU A 398 ? 0.3861 0.4032 0.4391 0.1365  0.1152  0.0914  398 GLU A CB  
2858 C CG  . GLU A 398 ? 0.5131 0.5054 0.5350 0.1351  0.1175  0.0806  398 GLU A CG  
2859 C CD  . GLU A 398 ? 0.5906 0.5518 0.5864 0.1446  0.1203  0.0720  398 GLU A CD  
2860 O OE1 . GLU A 398 ? 0.6970 0.6375 0.6663 0.1416  0.1175  0.0621  398 GLU A OE1 
2861 O OE2 . GLU A 398 ? 0.5448 0.5022 0.5464 0.1533  0.1239  0.0748  398 GLU A OE2 
2862 N N   . GLN A 399 ? 0.3069 0.3589 0.3829 0.1224  0.1260  0.0992  399 GLN A N   
2863 C CA  . GLN A 399 ? 0.3171 0.3706 0.3929 0.1260  0.1400  0.1027  399 GLN A CA  
2864 C C   . GLN A 399 ? 0.3009 0.3235 0.3399 0.1329  0.1460  0.0936  399 GLN A C   
2865 O O   . GLN A 399 ? 0.3788 0.3844 0.3962 0.1263  0.1358  0.0841  399 GLN A O   
2866 C CB  . GLN A 399 ? 0.3786 0.4473 0.4677 0.1116  0.1352  0.1045  399 GLN A CB  
2867 C CG  . GLN A 399 ? 0.4009 0.4720 0.4921 0.1142  0.1502  0.1099  399 GLN A CG  
2868 C CD  . GLN A 399 ? 0.5041 0.5897 0.6166 0.1192  0.1576  0.1200  399 GLN A CD  
2869 O OE1 . GLN A 399 ? 0.4546 0.5659 0.5989 0.1132  0.1531  0.1272  399 GLN A OE1 
2870 N NE2 . GLN A 399 ? 0.4472 0.5166 0.5419 0.1299  0.1685  0.1203  399 GLN A NE2 
2871 N N   . VAL A 400 ? 0.3315 0.3445 0.3603 0.1416  0.1571  0.0954  400 VAL A N   
2872 C CA  . VAL A 400 ? 0.4320 0.4163 0.4245 0.1472  0.1608  0.0868  400 VAL A CA  
2873 C C   . VAL A 400 ? 0.3394 0.3252 0.3269 0.1444  0.1675  0.0901  400 VAL A C   
2874 O O   . VAL A 400 ? 0.3462 0.3497 0.3555 0.1441  0.1747  0.1000  400 VAL A O   
2875 C CB  . VAL A 400 ? 0.4112 0.3829 0.3942 0.1585  0.1676  0.0862  400 VAL A CB  
2876 C CG1 . VAL A 400 ? 0.5352 0.4792 0.4810 0.1633  0.1706  0.0772  400 VAL A CG1 
2877 C CG2 . VAL A 400 ? 0.5120 0.4816 0.5019 0.1609  0.1610  0.0840  400 VAL A CG2 
2878 N N   . LEU A 401 ? 0.3634 0.3306 0.3231 0.1422  0.1645  0.0824  401 LEU A N   
2879 C CA  . LEU A 401 ? 0.3872 0.3509 0.3366 0.1416  0.1707  0.0853  401 LEU A CA  
2880 C C   . LEU A 401 ? 0.3964 0.3339 0.3094 0.1495  0.1724  0.0776  401 LEU A C   
2881 O O   . LEU A 401 ? 0.5093 0.4290 0.4003 0.1493  0.1638  0.0672  401 LEU A O   
2882 C CB  . LEU A 401 ? 0.3446 0.3116 0.2946 0.1306  0.1642  0.0840  401 LEU A CB  
2883 C CG  . LEU A 401 ? 0.3252 0.3190 0.3112 0.1207  0.1627  0.0916  401 LEU A CG  
2884 C CD1 . LEU A 401 ? 0.3582 0.3513 0.3409 0.1096  0.1564  0.0891  401 LEU A CD1 
2885 C CD2 . LEU A 401 ? 0.3214 0.3325 0.3318 0.1212  0.1718  0.1029  401 LEU A CD2 
2886 N N   . TYR A 402 ? 0.4149 0.3506 0.3220 0.1559  0.1826  0.0827  402 TYR A N   
2887 C CA  . TYR A 402 ? 0.4587 0.3719 0.3324 0.1641  0.1850  0.0760  402 TYR A CA  
2888 C C   . TYR A 402 ? 0.4513 0.3586 0.3085 0.1625  0.1859  0.0769  402 TYR A C   
2889 O O   . TYR A 402 ? 0.4535 0.3748 0.3271 0.1607  0.1930  0.0868  402 TYR A O   
2890 C CB  . TYR A 402 ? 0.5806 0.4939 0.4561 0.1750  0.1968  0.0803  402 TYR A CB  
2891 C CG  . TYR A 402 ? 0.6141 0.5286 0.5008 0.1787  0.1961  0.0785  402 TYR A CG  
2892 C CD1 . TYR A 402 ? 0.6122 0.5065 0.4777 0.1810  0.1890  0.0668  402 TYR A CD1 
2893 C CD2 . TYR A 402 ? 0.6072 0.5433 0.5268 0.1798  0.2021  0.0888  402 TYR A CD2 
2894 C CE1 . TYR A 402 ? 0.6636 0.5580 0.5402 0.1846  0.1886  0.0656  402 TYR A CE1 
2895 C CE2 . TYR A 402 ? 0.6461 0.5837 0.5766 0.1837  0.2013  0.0881  402 TYR A CE2 
2896 C CZ  . TYR A 402 ? 0.6740 0.5903 0.5829 0.1864  0.1949  0.0766  402 TYR A CZ  
2897 O OH  . TYR A 402 ? 0.7376 0.6548 0.6586 0.1904  0.1943  0.0765  402 TYR A OH  
2898 N N   . GLU A 403 ? 0.4919 0.3787 0.3176 0.1634  0.1786  0.0668  403 GLU A N   
2899 C CA  . GLU A 403 ? 0.4982 0.3785 0.3058 0.1629  0.1782  0.0673  403 GLU A CA  
2900 C C   . GLU A 403 ? 0.5401 0.4248 0.3478 0.1708  0.1922  0.0762  403 GLU A C   
2901 O O   . GLU A 403 ? 0.5491 0.4404 0.3611 0.1684  0.1958  0.0833  403 GLU A O   
2902 C CB  . GLU A 403 ? 0.5298 0.3879 0.3035 0.1645  0.1684  0.0549  403 GLU A CB  
2903 C CG  . GLU A 403 ? 0.6086 0.4618 0.3666 0.1609  0.1630  0.0543  403 GLU A CG  
2904 C CD  . GLU A 403 ? 0.6049 0.4384 0.3318 0.1617  0.1518  0.0421  403 GLU A CD  
2905 O OE1 . GLU A 403 ? 0.6164 0.4411 0.3388 0.1602  0.1438  0.0330  403 GLU A OE1 
2906 O OE2 . GLU A 403 ? 0.7295 0.5575 0.4385 0.1630  0.1502  0.0419  403 GLU A OE2 
2907 N N   . HIS A 404 ? 0.5532 0.4341 0.3566 0.1803  0.2005  0.0762  404 HIS A N   
2908 C CA  . HIS A 404 ? 0.5599 0.4440 0.3614 0.1889  0.2145  0.0844  404 HIS A CA  
2909 C C   . HIS A 404 ? 0.5685 0.4761 0.4058 0.1864  0.2239  0.0985  404 HIS A C   
2910 O O   . HIS A 404 ? 0.6235 0.5361 0.4630 0.1924  0.2357  0.1071  404 HIS A O   
2911 C CB  . HIS A 404 ? 0.6470 0.5190 0.4317 0.2001  0.2209  0.0795  404 HIS A CB  
2912 C CG  . HIS A 404 ? 0.6671 0.5449 0.4712 0.2013  0.2218  0.0792  404 HIS A CG  
2913 N ND1 . HIS A 404 ? 0.7546 0.6501 0.5870 0.2047  0.2329  0.0904  404 HIS A ND1 
2914 C CD2 . HIS A 404 ? 0.6605 0.5295 0.4614 0.1994  0.2129  0.0698  404 HIS A CD2 
2915 C CE1 . HIS A 404 ? 0.6384 0.5360 0.4835 0.2054  0.2307  0.0880  404 HIS A CE1 
2916 N NE2 . HIS A 404 ? 0.6945 0.5759 0.5209 0.2023  0.2189  0.0756  404 HIS A NE2 
2917 N N   . HIS A 405 ? 0.5517 0.4741 0.4173 0.1776  0.2186  0.1011  405 HIS A N   
2918 C CA  . HIS A 405 ? 0.5392 0.4852 0.4411 0.1725  0.2247  0.1135  405 HIS A CA  
2919 C C   . HIS A 405 ? 0.5111 0.4632 0.4210 0.1624  0.2205  0.1169  405 HIS A C   
2920 O O   . HIS A 405 ? 0.5247 0.4961 0.4662 0.1556  0.2233  0.1260  405 HIS A O   
2921 C CB  . HIS A 405 ? 0.5292 0.4905 0.4599 0.1680  0.2208  0.1148  405 HIS A CB  
2922 C CG  . HIS A 405 ? 0.5909 0.5521 0.5244 0.1777  0.2273  0.1155  405 HIS A CG  
2923 N ND1 . HIS A 405 ? 0.5931 0.5593 0.5397 0.1767  0.2219  0.1127  405 HIS A ND1 
2924 C CD2 . HIS A 405 ? 0.5250 0.4816 0.4498 0.1890  0.2393  0.1189  405 HIS A CD2 
2925 C CE1 . HIS A 405 ? 0.5476 0.5120 0.4943 0.1868  0.2300  0.1145  405 HIS A CE1 
2926 N NE2 . HIS A 405 ? 0.5931 0.5516 0.5265 0.1944  0.2409  0.1180  405 HIS A NE2 
2927 N N   . ALA A 406 ? 0.4733 0.4098 0.3567 0.1607  0.2134  0.1098  406 ALA A N   
2928 C CA  . ALA A 406 ? 0.4797 0.4207 0.3706 0.1510  0.2089  0.1126  406 ALA A CA  
2929 C C   . ALA A 406 ? 0.4706 0.4214 0.3749 0.1520  0.2202  0.1249  406 ALA A C   
2930 O O   . ALA A 406 ? 0.5029 0.4467 0.3903 0.1616  0.2288  0.1278  406 ALA A O   
2931 C CB  . ALA A 406 ? 0.5222 0.4445 0.3810 0.1505  0.1994  0.1033  406 ALA A CB  
2932 N N   . ASP A 407 ? 0.4426 0.4100 0.3783 0.1419  0.2201  0.1320  407 ASP A N   
2933 C CA  . ASP A 407 ? 0.4509 0.4273 0.4020 0.1405  0.2293  0.1436  407 ASP A CA  
2934 C C   . ASP A 407 ? 0.4581 0.4230 0.3905 0.1383  0.2264  0.1428  407 ASP A C   
2935 O O   . ASP A 407 ? 0.4781 0.4421 0.4066 0.1428  0.2353  0.1508  407 ASP A O   
2936 C CB  . ASP A 407 ? 0.4553 0.4526 0.4473 0.1285  0.2280  0.1499  407 ASP A CB  
2937 C CG  . ASP A 407 ? 0.4274 0.4400 0.4426 0.1308  0.2318  0.1534  407 ASP A CG  
2938 O OD1 . ASP A 407 ? 0.4449 0.4592 0.4590 0.1407  0.2428  0.1596  407 ASP A OD1 
2939 O OD2 . ASP A 407 ? 0.3990 0.4215 0.4320 0.1232  0.2235  0.1499  407 ASP A OD2 
2940 N N   . LYS A 408 ? 0.4428 0.3995 0.3647 0.1317  0.2142  0.1342  408 LYS A N   
2941 C CA  . LYS A 408 ? 0.4501 0.3953 0.3530 0.1302  0.2102  0.1330  408 LYS A CA  
2942 C C   . LYS A 408 ? 0.4604 0.3903 0.3352 0.1308  0.1978  0.1202  408 LYS A C   
2943 O O   . LYS A 408 ? 0.4290 0.3599 0.3085 0.1267  0.1901  0.1131  408 LYS A O   
2944 C CB  . LYS A 408 ? 0.4417 0.3960 0.3703 0.1180  0.2084  0.1389  408 LYS A CB  
2945 C CG  . LYS A 408 ? 0.5879 0.5369 0.5091 0.1191  0.2129  0.1461  408 LYS A CG  
2946 C CD  . LYS A 408 ? 0.6407 0.5944 0.5842 0.1064  0.2091  0.1497  408 LYS A CD  
2947 C CE  . LYS A 408 ? 0.6780 0.6493 0.6613 0.0984  0.2152  0.1582  408 LYS A CE  
2948 N NZ  . LYS A 408 ? 0.4162 0.3920 0.4243 0.0835  0.2087  0.1583  408 LYS A NZ  
2949 N N   . THR A 409 ? 0.4670 0.3833 0.3132 0.1360  0.1956  0.1177  409 THR A N   
2950 C CA  . THR A 409 ? 0.4671 0.3690 0.2870 0.1358  0.1828  0.1063  409 THR A CA  
2951 C C   . THR A 409 ? 0.4666 0.3647 0.2809 0.1310  0.1777  0.1084  409 THR A C   
2952 O O   . THR A 409 ? 0.4846 0.3827 0.2945 0.1349  0.1847  0.1163  409 THR A O   
2953 C CB  . THR A 409 ? 0.4949 0.3835 0.2834 0.1470  0.1832  0.0999  409 THR A CB  
2954 O OG1 . THR A 409 ? 0.5070 0.3987 0.3022 0.1519  0.1891  0.0989  409 THR A OG1 
2955 C CG2 . THR A 409 ? 0.5444 0.4191 0.3086 0.1455  0.1685  0.0876  409 THR A CG2 
2956 N N   . ARG A 410 ? 0.4472 0.3424 0.2623 0.1230  0.1660  0.1021  410 ARG A N   
2957 C CA  . ARG A 410 ? 0.4448 0.3365 0.2567 0.1181  0.1602  0.1039  410 ARG A CA  
2958 C C   . ARG A 410 ? 0.4520 0.3307 0.2355 0.1201  0.1475  0.0939  410 ARG A C   
2959 O O   . ARG A 410 ? 0.4403 0.3151 0.2196 0.1177  0.1385  0.0844  410 ARG A O   
2960 C CB  . ARG A 410 ? 0.4174 0.3169 0.2561 0.1061  0.1569  0.1057  410 ARG A CB  
2961 C CG  . ARG A 410 ? 0.4065 0.3205 0.2768 0.1018  0.1664  0.1132  410 ARG A CG  
2962 C CD  . ARG A 410 ? 0.3834 0.3040 0.2796 0.0890  0.1627  0.1148  410 ARG A CD  
2963 N NE  . ARG A 410 ? 0.3758 0.3113 0.3037 0.0841  0.1711  0.1222  410 ARG A NE  
2964 C CZ  . ARG A 410 ? 0.3829 0.3239 0.3285 0.0816  0.1790  0.1322  410 ARG A CZ  
2965 N NH1 . ARG A 410 ? 0.3981 0.3309 0.3328 0.0841  0.1809  0.1368  410 ARG A NH1 
2966 N NH2 . ARG A 410 ? 0.3831 0.3386 0.3587 0.0767  0.1851  0.1379  410 ARG A NH2 
2967 N N   . LEU A 411 ? 0.4713 0.3440 0.2371 0.1241  0.1463  0.0965  411 LEU A N   
2968 C CA  . LEU A 411 ? 0.4778 0.3405 0.2202 0.1246  0.1331  0.0882  411 LEU A CA  
2969 C C   . LEU A 411 ? 0.4626 0.3269 0.2156 0.1167  0.1267  0.0912  411 LEU A C   
2970 O O   . LEU A 411 ? 0.4694 0.3366 0.2284 0.1167  0.1323  0.1009  411 LEU A O   
2971 C CB  . LEU A 411 ? 0.5107 0.3666 0.2260 0.1340  0.1349  0.0891  411 LEU A CB  
2972 C CG  . LEU A 411 ? 0.5628 0.4179 0.2704 0.1428  0.1455  0.0896  411 LEU A CG  
2973 C CD1 . LEU A 411 ? 0.6089 0.4593 0.2924 0.1519  0.1502  0.0933  411 LEU A CD1 
2974 C CD2 . LEU A 411 ? 0.6183 0.4664 0.3165 0.1437  0.1386  0.0772  411 LEU A CD2 
2975 N N   . LEU A 412 ? 0.4434 0.3057 0.1990 0.1104  0.1152  0.0833  412 LEU A N   
2976 C CA  . LEU A 412 ? 0.4258 0.2900 0.1955 0.1023  0.1097  0.0856  412 LEU A CA  
2977 C C   . LEU A 412 ? 0.4264 0.2838 0.1797 0.1013  0.0949  0.0778  412 LEU A C   
2978 O O   . LEU A 412 ? 0.4175 0.2719 0.1661 0.0993  0.0863  0.0681  412 LEU A O   
2979 C CB  . LEU A 412 ? 0.3999 0.2706 0.1940 0.0942  0.1112  0.0847  412 LEU A CB  
2980 C CG  . LEU A 412 ? 0.3984 0.2782 0.2131 0.0937  0.1251  0.0930  412 LEU A CG  
2981 C CD1 . LEU A 412 ? 0.3757 0.2630 0.2114 0.0867  0.1255  0.0905  412 LEU A CD1 
2982 C CD2 . LEU A 412 ? 0.4027 0.2851 0.2311 0.0911  0.1315  0.1038  412 LEU A CD2 
2983 N N   . LYS A 413 ? 0.4378 0.2933 0.1836 0.1028  0.0917  0.0825  413 LYS A N   
2984 C CA  . LYS A 413 ? 0.4399 0.2910 0.1723 0.1020  0.0774  0.0766  413 LYS A CA  
2985 C C   . LYS A 413 ? 0.4159 0.2685 0.1648 0.0938  0.0701  0.0750  413 LYS A C   
2986 O O   . LYS A 413 ? 0.4039 0.2598 0.1728 0.0893  0.0762  0.0814  413 LYS A O   
2987 C CB  . LYS A 413 ? 0.4620 0.3121 0.1817 0.1068  0.0770  0.0838  413 LYS A CB  
2988 C CG  . LYS A 413 ? 0.5048 0.3518 0.2087 0.1070  0.0620  0.0780  413 LYS A CG  
2989 C CD  . LYS A 413 ? 0.5355 0.3826 0.2253 0.1122  0.0611  0.0856  413 LYS A CD  
2990 C CE  . LYS A 413 ? 0.5392 0.3895 0.2448 0.1115  0.0697  0.0984  413 LYS A CE  
2991 N NZ  . LYS A 413 ? 0.6149 0.4652 0.3054 0.1171  0.0681  0.1062  413 LYS A NZ  
2992 N N   . LEU A 414 ? 0.4109 0.2608 0.1519 0.0918  0.0569  0.0662  414 LEU A N   
2993 C CA  . LEU A 414 ? 0.3925 0.2435 0.1457 0.0854  0.0482  0.0646  414 LEU A CA  
2994 C C   . LEU A 414 ? 0.4149 0.2650 0.1569 0.0875  0.0379  0.0653  414 LEU A C   
2995 O O   . LEU A 414 ? 0.4173 0.2651 0.1421 0.0901  0.0298  0.0589  414 LEU A O   
2996 C CB  . LEU A 414 ? 0.3768 0.2270 0.1323 0.0810  0.0410  0.0543  414 LEU A CB  
2997 C CG  . LEU A 414 ? 0.3757 0.2266 0.1355 0.0808  0.0488  0.0514  414 LEU A CG  
2998 C CD1 . LEU A 414 ? 0.3574 0.2072 0.1187 0.0766  0.0402  0.0417  414 LEU A CD1 
2999 C CD2 . LEU A 414 ? 0.3880 0.2439 0.1674 0.0777  0.0606  0.0593  414 LEU A CD2 
3000 N N   . ASP A 415 ? 0.4021 0.2539 0.1546 0.0864  0.0381  0.0733  415 ASP A N   
3001 C CA  . ASP A 415 ? 0.4161 0.2686 0.1590 0.0893  0.0296  0.0764  415 ASP A CA  
3002 C C   . ASP A 415 ? 0.4037 0.2577 0.1645 0.0860  0.0270  0.0818  415 ASP A C   
3003 O O   . ASP A 415 ? 0.4002 0.2537 0.1790 0.0813  0.0315  0.0819  415 ASP A O   
3004 C CB  . ASP A 415 ? 0.4696 0.3216 0.1995 0.0960  0.0368  0.0846  415 ASP A CB  
3005 C CG  . ASP A 415 ? 0.4688 0.3218 0.1812 0.1000  0.0264  0.0856  415 ASP A CG  
3006 O OD1 . ASP A 415 ? 0.5448 0.3998 0.2572 0.0973  0.0134  0.0806  415 ASP A OD1 
3007 O OD2 . ASP A 415 ? 0.6170 0.4696 0.3161 0.1057  0.0315  0.0921  415 ASP A OD2 
3008 N N   . ALA A 416 ? 0.4546 0.3106 0.2108 0.0885  0.0191  0.0859  416 ALA A N   
3009 C CA  . ALA A 416 ? 0.4517 0.3086 0.2245 0.0873  0.0176  0.0927  416 ALA A CA  
3010 C C   . ALA A 416 ? 0.4903 0.3481 0.2570 0.0928  0.0186  0.1036  416 ALA A C   
3011 O O   . ALA A 416 ? 0.5242 0.3835 0.2710 0.0970  0.0145  0.1039  416 ALA A O   
3012 C CB  . ALA A 416 ? 0.4519 0.3121 0.2297 0.0846  0.0042  0.0869  416 ALA A CB  
3013 N N   . ILE A 417 ? 0.4419 0.2980 0.2256 0.0926  0.0245  0.1125  417 ILE A N   
3014 C CA  . ILE A 417 ? 0.4463 0.3031 0.2282 0.0975  0.0239  0.1236  417 ILE A CA  
3015 C C   . ILE A 417 ? 0.4369 0.2950 0.2353 0.0965  0.0165  0.1255  417 ILE A C   
3016 O O   . ILE A 417 ? 0.4548 0.3130 0.2652 0.0922  0.0132  0.1184  417 ILE A O   
3017 C CB  . ILE A 417 ? 0.5012 0.3539 0.2893 0.0993  0.0383  0.1338  417 ILE A CB  
3018 C CG1 . ILE A 417 ? 0.5552 0.4034 0.3702 0.0942  0.0460  0.1351  417 ILE A CG1 
3019 C CG2 . ILE A 417 ? 0.5520 0.4046 0.3256 0.1010  0.0464  0.1322  417 ILE A CG2 
3020 C CD1 . ILE A 417 ? 0.5613 0.4057 0.3862 0.0941  0.0603  0.1439  417 ILE A CD1 
3021 N N   . GLN A 418 ? 0.4530 0.3122 0.2517 0.1010  0.0140  0.1354  418 GLN A N   
3022 C CA  . GLN A 418 ? 0.4465 0.3065 0.2633 0.1012  0.0089  0.1387  418 GLN A CA  
3023 C C   . GLN A 418 ? 0.4511 0.3041 0.2852 0.1020  0.0207  0.1477  418 GLN A C   
3024 O O   . GLN A 418 ? 0.4694 0.3199 0.2968 0.1052  0.0282  0.1561  418 GLN A O   
3025 C CB  . GLN A 418 ? 0.4637 0.3308 0.2711 0.1057  -0.0044 0.1434  418 GLN A CB  
3026 C CG  . GLN A 418 ? 0.5278 0.4020 0.3199 0.1038  -0.0169 0.1339  418 GLN A CG  
3027 C CD  . GLN A 418 ? 0.5076 0.3850 0.3146 0.0993  -0.0234 0.1251  418 GLN A CD  
3028 O OE1 . GLN A 418 ? 0.5840 0.4610 0.3865 0.0951  -0.0240 0.1147  418 GLN A OE1 
3029 N NE2 . GLN A 418 ? 0.6255 0.5060 0.4503 0.1007  -0.0281 0.1296  418 GLN A NE2 
3030 N N   . ASP A 419 ? 0.3722 0.2896 0.2184 0.0757  -0.0676 0.0662  419 ASP A N   
3031 C CA  . ASP A 419 ? 0.3548 0.2743 0.2181 0.0763  -0.0593 0.0743  419 ASP A CA  
3032 C C   . ASP A 419 ? 0.3703 0.2883 0.2346 0.0813  -0.0686 0.0782  419 ASP A C   
3033 O O   . ASP A 419 ? 0.3796 0.2959 0.2309 0.0845  -0.0820 0.0747  419 ASP A O   
3034 C CB  . ASP A 419 ? 0.3419 0.2742 0.2361 0.0667  -0.0526 0.0699  419 ASP A CB  
3035 C CG  . ASP A 419 ? 0.3105 0.2545 0.2255 0.0602  -0.0625 0.0612  419 ASP A CG  
3036 O OD1 . ASP A 419 ? 0.3209 0.2644 0.2321 0.0627  -0.0745 0.0594  419 ASP A OD1 
3037 O OD2 . ASP A 419 ? 0.2894 0.2441 0.2258 0.0527  -0.0579 0.0562  419 ASP A OD2 
3038 N N   . GLU A 420 ? 0.3585 0.2775 0.2398 0.0822  -0.0616 0.0855  420 GLU A N   
3039 C CA  . GLU A 420 ? 0.4335 0.3506 0.3173 0.0880  -0.0688 0.0910  420 GLU A CA  
3040 C C   . GLU A 420 ? 0.3457 0.2742 0.2483 0.0832  -0.0818 0.0822  420 GLU A C   
3041 O O   . GLU A 420 ? 0.4089 0.3370 0.3118 0.0886  -0.0909 0.0855  420 GLU A O   
3042 C CB  . GLU A 420 ? 0.4418 0.3572 0.3442 0.0890  -0.0573 0.1001  420 GLU A CB  
3043 C CG  . GLU A 420 ? 0.4539 0.3806 0.3895 0.0787  -0.0514 0.0933  420 GLU A CG  
3044 C CD  . GLU A 420 ? 0.4848 0.4083 0.4391 0.0792  -0.0394 0.1013  420 GLU A CD  
3045 O OE1 . GLU A 420 ? 0.5424 0.4619 0.5017 0.0847  -0.0420 0.1079  420 GLU A OE1 
3046 O OE2 . GLU A 420 ? 0.5824 0.5078 0.5480 0.0739  -0.0278 0.1007  420 GLU A OE2 
3047 N N   . TYR A 421 ? 0.3486 0.2876 0.2677 0.0737  -0.0822 0.0719  421 TYR A N   
3048 C CA  . TYR A 421 ? 0.3671 0.3175 0.3047 0.0687  -0.0931 0.0634  421 TYR A CA  
3049 C C   . TYR A 421 ? 0.3826 0.3336 0.3058 0.0675  -0.1048 0.0557  421 TYR A C   
3050 O O   . TYR A 421 ? 0.4113 0.3725 0.3511 0.0617  -0.1123 0.0477  421 TYR A O   
3051 C CB  . TYR A 421 ? 0.3294 0.2913 0.2946 0.0593  -0.0857 0.0571  421 TYR A CB  
3052 C CG  . TYR A 421 ? 0.3114 0.2724 0.2919 0.0591  -0.0735 0.0628  421 TYR A CG  
3053 C CD1 . TYR A 421 ? 0.3275 0.2877 0.3216 0.0629  -0.0744 0.0677  421 TYR A CD1 
3054 C CD2 . TYR A 421 ? 0.3405 0.3014 0.3234 0.0553  -0.0613 0.0630  421 TYR A CD2 
3055 C CE1 . TYR A 421 ? 0.3442 0.3023 0.3540 0.0623  -0.0631 0.0722  421 TYR A CE1 
3056 C CE2 . TYR A 421 ? 0.3171 0.2771 0.3163 0.0544  -0.0507 0.0672  421 TYR A CE2 
3057 C CZ  . TYR A 421 ? 0.3891 0.3471 0.4016 0.0577  -0.0515 0.0715  421 TYR A CZ  
3058 O OH  . TYR A 421 ? 0.4398 0.3958 0.4700 0.0564  -0.0406 0.0751  421 TYR A OH  
3059 N N   . ASN A 422 ? 0.3518 0.2917 0.2454 0.0728  -0.1058 0.0576  422 ASN A N   
3060 C CA  . ASN A 422 ? 0.3965 0.3346 0.2749 0.0716  -0.1161 0.0495  422 ASN A CA  
3061 C C   . ASN A 422 ? 0.3698 0.3150 0.2608 0.0621  -0.1126 0.0409  422 ASN A C   
3062 O O   . ASN A 422 ? 0.4062 0.3541 0.2978 0.0584  -0.1222 0.0327  422 ASN A O   
3063 C CB  . ASN A 422 ? 0.4186 0.3613 0.2992 0.0728  -0.1310 0.0455  422 ASN A CB  
3064 C CG  . ASN A 422 ? 0.5932 0.5310 0.4529 0.0729  -0.1364 0.0389  422 ASN A CG  
3065 O OD1 . ASN A 422 ? 0.6398 0.5671 0.4750 0.0771  -0.1303 0.0413  422 ASN A OD1 
3066 N ND2 . ASN A 422 ? 0.6650 0.6104 0.5355 0.0683  -0.1475 0.0303  422 ASN A ND2 
3067 N N   . ARG A 423 ? 0.3129 0.2609 0.2137 0.0584  -0.0990 0.0429  423 ARG A N   
3068 C CA  . ARG A 423 ? 0.2904 0.2441 0.1990 0.0509  -0.0946 0.0363  423 ARG A CA  
3069 C C   . ARG A 423 ? 0.3471 0.2906 0.2327 0.0538  -0.0872 0.0380  423 ARG A C   
3070 O O   . ARG A 423 ? 0.3442 0.2792 0.2156 0.0599  -0.0798 0.0457  423 ARG A O   
3071 C CB  . ARG A 423 ? 0.2751 0.2400 0.2094 0.0449  -0.0848 0.0364  423 ARG A CB  
3072 C CG  . ARG A 423 ? 0.2777 0.2524 0.2359 0.0426  -0.0893 0.0350  423 ARG A CG  
3073 C CD  . ARG A 423 ? 0.2557 0.2408 0.2370 0.0368  -0.0796 0.0335  423 ARG A CD  
3074 N NE  . ARG A 423 ? 0.2381 0.2185 0.2181 0.0392  -0.0687 0.0400  423 ARG A NE  
3075 C CZ  . ARG A 423 ? 0.2388 0.2268 0.2369 0.0347  -0.0600 0.0387  423 ARG A CZ  
3076 N NH1 . ARG A 423 ? 0.2038 0.2042 0.2205 0.0284  -0.0606 0.0315  423 ARG A NH1 
3077 N NH2 . ARG A 423 ? 0.2453 0.2285 0.2430 0.0366  -0.0503 0.0446  423 ARG A NH2 
3078 N N   . PRO A 424 ? 0.3409 0.2846 0.2232 0.0498  -0.0879 0.0316  424 PRO A N   
3079 C CA  . PRO A 424 ? 0.3406 0.2758 0.2048 0.0523  -0.0789 0.0334  424 PRO A CA  
3080 C C   . PRO A 424 ? 0.3237 0.2651 0.2009 0.0502  -0.0650 0.0384  424 PRO A C   
3081 O O   . PRO A 424 ? 0.3415 0.2955 0.2427 0.0439  -0.0628 0.0363  424 PRO A O   
3082 C CB  . PRO A 424 ? 0.3664 0.3026 0.2314 0.0473  -0.0830 0.0251  424 PRO A CB  
3083 C CG  . PRO A 424 ? 0.4466 0.3907 0.3280 0.0425  -0.0950 0.0192  424 PRO A CG  
3084 C CD  . PRO A 424 ? 0.3574 0.3093 0.2546 0.0429  -0.0959 0.0232  424 PRO A CD  
3085 N N   . VAL A 425 ? 0.3278 0.2606 0.1889 0.0556  -0.0555 0.0445  425 VAL A N   
3086 C CA  . VAL A 425 ? 0.2903 0.2284 0.1620 0.0537  -0.0421 0.0486  425 VAL A CA  
3087 C C   . VAL A 425 ? 0.3122 0.2439 0.1674 0.0559  -0.0369 0.0476  425 VAL A C   
3088 O O   . VAL A 425 ? 0.3323 0.2506 0.1622 0.0631  -0.0361 0.0502  425 VAL A O   
3089 C CB  . VAL A 425 ? 0.3200 0.2541 0.1908 0.0585  -0.0335 0.0581  425 VAL A CB  
3090 C CG1 . VAL A 425 ? 0.3089 0.2522 0.1991 0.0544  -0.0214 0.0607  425 VAL A CG1 
3091 C CG2 . VAL A 425 ? 0.3253 0.2602 0.2044 0.0595  -0.0403 0.0600  425 VAL A CG2 
3092 N N   . LEU A 426 ? 0.2977 0.2384 0.1662 0.0505  -0.0333 0.0441  426 LEU A N   
3093 C CA  . LEU A 426 ? 0.2846 0.2196 0.1399 0.0525  -0.0285 0.0431  426 LEU A CA  
3094 C C   . LEU A 426 ? 0.2905 0.2258 0.1456 0.0559  -0.0149 0.0506  426 LEU A C   
3095 O O   . LEU A 426 ? 0.2844 0.2317 0.1607 0.0519  -0.0093 0.0531  426 LEU A O   
3096 C CB  . LEU A 426 ? 0.2800 0.2255 0.1511 0.0456  -0.0306 0.0373  426 LEU A CB  
3097 C CG  . LEU A 426 ? 0.3026 0.2440 0.1692 0.0432  -0.0418 0.0297  426 LEU A CG  
3098 C CD1 . LEU A 426 ? 0.3371 0.2620 0.1779 0.0488  -0.0434 0.0276  426 LEU A CD1 
3099 C CD2 . LEU A 426 ? 0.3602 0.3040 0.2337 0.0413  -0.0526 0.0272  426 LEU A CD2 
3100 N N   . LEU A 427 ? 0.3069 0.2293 0.1388 0.0632  -0.0093 0.0539  427 LEU A N   
3101 C CA  . LEU A 427 ? 0.3233 0.2442 0.1532 0.0677  0.0043  0.0624  427 LEU A CA  
3102 C C   . LEU A 427 ? 0.3547 0.2697 0.1715 0.0720  0.0120  0.0628  427 LEU A C   
3103 O O   . LEU A 427 ? 0.3620 0.2648 0.1572 0.0757  0.0076  0.0583  427 LEU A O   
3104 C CB  . LEU A 427 ? 0.3501 0.2590 0.1617 0.0753  0.0065  0.0693  427 LEU A CB  
3105 C CG  . LEU A 427 ? 0.3638 0.2762 0.1868 0.0735  0.0017  0.0719  427 LEU A CG  
3106 C CD1 . LEU A 427 ? 0.4047 0.3040 0.2067 0.0827  0.0063  0.0808  427 LEU A CD1 
3107 C CD2 . LEU A 427 ? 0.3394 0.2671 0.1948 0.0663  0.0070  0.0734  427 LEU A CD2 
3108 N N   . LEU A 428 ? 0.3125 0.2361 0.1435 0.0715  0.0236  0.0680  428 LEU A N   
3109 C CA  . LEU A 428 ? 0.3228 0.2415 0.1436 0.0770  0.0340  0.0711  428 LEU A CA  
3110 C C   . LEU A 428 ? 0.3622 0.2710 0.1681 0.0851  0.0447  0.0800  428 LEU A C   
3111 O O   . LEU A 428 ? 0.3412 0.2554 0.1604 0.0840  0.0498  0.0864  428 LEU A O   
3112 C CB  . LEU A 428 ? 0.3003 0.2363 0.1479 0.0721  0.0405  0.0727  428 LEU A CB  
3113 C CG  . LEU A 428 ? 0.2790 0.2269 0.1428 0.0643  0.0315  0.0655  428 LEU A CG  
3114 C CD1 . LEU A 428 ? 0.2592 0.2253 0.1481 0.0604  0.0375  0.0676  428 LEU A CD1 
3115 C CD2 . LEU A 428 ? 0.3279 0.2659 0.1752 0.0665  0.0270  0.0601  428 LEU A CD2 
3116 N N   . ASP A 429 ? 0.3659 0.2628 0.1519 0.0910  0.0473  0.0772  429 ASP A N   
3117 C CA  . ASP A 429 ? 0.3827 0.2744 0.1627 0.0973  0.0588  0.0827  429 ASP A CA  
3118 C C   . ASP A 429 ? 0.4141 0.3031 0.1918 0.0985  0.0579  0.0875  429 ASP A C   
3119 O O   . ASP A 429 ? 0.4164 0.3075 0.2022 0.1008  0.0687  0.0952  429 ASP A O   
3120 C CB  . ASP A 429 ? 0.3829 0.2858 0.1835 0.0969  0.0721  0.0889  429 ASP A CB  
3121 C CG  . ASP A 429 ? 0.4695 0.3675 0.2658 0.1038  0.0848  0.0945  429 ASP A CG  
3122 O OD1 . ASP A 429 ? 0.5170 0.4014 0.2899 0.1106  0.0853  0.0918  429 ASP A OD1 
3123 O OD2 . ASP A 429 ? 0.4439 0.3522 0.2613 0.1025  0.0946  0.1018  429 ASP A OD2 
3124 N N   . ASP A 430 ? 0.4069 0.2913 0.1750 0.0971  0.0450  0.0833  430 ASP A N   
3125 C CA  . ASP A 430 ? 0.4050 0.2861 0.1693 0.0990  0.0425  0.0876  430 ASP A CA  
3126 C C   . ASP A 430 ? 0.4186 0.3093 0.2071 0.0953  0.0485  0.0959  430 ASP A C   
3127 O O   . ASP A 430 ? 0.4308 0.3186 0.2192 0.0979  0.0514  0.1022  430 ASP A O   
3128 C CB  . ASP A 430 ? 0.4602 0.3307 0.2048 0.1074  0.0492  0.0906  430 ASP A CB  
3129 C CG  . ASP A 430 ? 0.5893 0.4482 0.3078 0.1119  0.0422  0.0822  430 ASP A CG  
3130 O OD1 . ASP A 430 ? 0.6323 0.4887 0.3431 0.1098  0.0281  0.0757  430 ASP A OD1 
3131 O OD2 . ASP A 430 ? 0.6535 0.5060 0.3605 0.1176  0.0506  0.0819  430 ASP A OD2 
3132 N N   . ARG A 431 ? 0.3790 0.2811 0.1888 0.0896  0.0509  0.0966  431 ARG A N   
3133 C CA  . ARG A 431 ? 0.3578 0.2691 0.1926 0.0862  0.0589  0.1046  431 ARG A CA  
3134 C C   . ARG A 431 ? 0.3477 0.2729 0.2077 0.0764  0.0493  0.0974  431 ARG A C   
3135 O O   . ARG A 431 ? 0.3631 0.2929 0.2234 0.0725  0.0407  0.0887  431 ARG A O   
3136 C CB  . ARG A 431 ? 0.3479 0.2662 0.1964 0.0864  0.0732  0.1091  431 ARG A CB  
3137 C CG  . ARG A 431 ? 0.3714 0.2811 0.2082 0.0935  0.0833  0.1136  431 ARG A CG  
3138 C CD  . ARG A 431 ? 0.4074 0.3227 0.2533 0.0952  0.0953  0.1158  431 ARG A CD  
3139 N NE  . ARG A 431 ? 0.4763 0.3852 0.3168 0.1018  0.1065  0.1221  431 ARG A NE  
3140 C CZ  . ARG A 431 ? 0.5429 0.4394 0.3572 0.1096  0.1068  0.1202  431 ARG A CZ  
3141 N NH1 . ARG A 431 ? 0.5053 0.3940 0.2975 0.1111  0.0964  0.1118  431 ARG A NH1 
3142 N NH2 . ARG A 431 ? 0.5283 0.4201 0.3393 0.1160  0.1181  0.1269  431 ARG A NH2 
3143 N N   . MET A 432 ? 0.3427 0.2744 0.2250 0.0722  0.0513  0.1005  432 MET A N   
3144 C CA  . MET A 432 ? 0.3116 0.2577 0.2207 0.0626  0.0438  0.0930  432 MET A CA  
3145 C C   . MET A 432 ? 0.2738 0.2349 0.2096 0.0569  0.0517  0.0927  432 MET A C   
3146 O O   . MET A 432 ? 0.2871 0.2475 0.2246 0.0600  0.0636  0.0998  432 MET A O   
3147 C CB  . MET A 432 ? 0.4043 0.3482 0.3223 0.0614  0.0401  0.0950  432 MET A CB  
3148 C CG  . MET A 432 ? 0.4301 0.3624 0.3245 0.0664  0.0295  0.0939  432 MET A CG  
3149 S SD  . MET A 432 ? 0.5133 0.4414 0.4161 0.0675  0.0266  0.0989  432 MET A SD  
3150 C CE  . MET A 432 ? 0.6040 0.5235 0.4807 0.0721  0.0106  0.0942  432 MET A CE  
3151 N N   . TRP A 433 ? 0.2592 0.2345 0.2158 0.0488  0.0446  0.0843  433 TRP A N   
3152 C CA  . TRP A 433 ? 0.2352 0.2269 0.2174 0.0430  0.0495  0.0824  433 TRP A CA  
3153 C C   . TRP A 433 ? 0.2777 0.2702 0.2771 0.0427  0.0611  0.0900  433 TRP A C   
3154 O O   . TRP A 433 ? 0.2591 0.2593 0.2698 0.0424  0.0696  0.0931  433 TRP A O   
3155 C CB  . TRP A 433 ? 0.2457 0.2509 0.2464 0.0348  0.0401  0.0726  433 TRP A CB  
3156 C CG  . TRP A 433 ? 0.1996 0.2217 0.2289 0.0285  0.0438  0.0698  433 TRP A CG  
3157 C CD1 . TRP A 433 ? 0.2044 0.2325 0.2572 0.0230  0.0445  0.0676  433 TRP A CD1 
3158 C CD2 . TRP A 433 ? 0.1994 0.2346 0.2375 0.0271  0.0470  0.0687  433 TRP A CD2 
3159 N NE1 . TRP A 433 ? 0.1894 0.2340 0.2647 0.0178  0.0471  0.0641  433 TRP A NE1 
3160 C CE2 . TRP A 433 ? 0.1792 0.2291 0.2460 0.0204  0.0484  0.0652  433 TRP A CE2 
3161 C CE3 . TRP A 433 ? 0.2032 0.2388 0.2282 0.0312  0.0488  0.0705  433 TRP A CE3 
3162 C CZ2 . TRP A 433 ? 0.1756 0.2420 0.2579 0.0178  0.0504  0.0632  433 TRP A CZ2 
3163 C CZ3 . TRP A 433 ? 0.2098 0.2614 0.2506 0.0289  0.0515  0.0694  433 TRP A CZ3 
3164 C CH2 . TRP A 433 ? 0.2001 0.2676 0.2692 0.0224  0.0520  0.0660  433 TRP A CH2 
3165 N N   . HIS A 434 ? 0.2739 0.2588 0.2769 0.0431  0.0618  0.0937  434 HIS A N   
3166 C CA  . HIS A 434 ? 0.2767 0.2630 0.3014 0.0413  0.0724  0.1002  434 HIS A CA  
3167 C C   . HIS A 434 ? 0.3439 0.3176 0.3547 0.0495  0.0855  0.1131  434 HIS A C   
3168 O O   . HIS A 434 ? 0.3285 0.3028 0.3581 0.0484  0.0962  0.1200  434 HIS A O   
3169 C CB  . HIS A 434 ? 0.3162 0.3000 0.3544 0.0378  0.0682  0.0984  434 HIS A CB  
3170 C CG  . HIS A 434 ? 0.4517 0.4199 0.4661 0.0444  0.0634  0.1025  434 HIS A CG  
3171 N ND1 . HIS A 434 ? 0.6271 0.5806 0.6141 0.0538  0.0685  0.1121  434 HIS A ND1 
3172 C CD2 . HIS A 434 ? 0.5971 0.5627 0.6110 0.0432  0.0535  0.0981  434 HIS A CD2 
3173 C CE1 . HIS A 434 ? 0.5704 0.5133 0.5409 0.0582  0.0612  0.1134  434 HIS A CE1 
3174 N NE2 . HIS A 434 ? 0.6250 0.5753 0.6124 0.0518  0.0520  0.1052  434 HIS A NE2 
3175 N N   . ASP A 435 ? 0.3077 0.2700 0.2867 0.0577  0.0853  0.1162  435 ASP A N   
3176 C CA  . ASP A 435 ? 0.3563 0.3069 0.3191 0.0664  0.0983  0.1280  435 ASP A CA  
3177 C C   . ASP A 435 ? 0.3265 0.2877 0.3055 0.0652  0.1094  0.1307  435 ASP A C   
3178 O O   . ASP A 435 ? 0.3052 0.2802 0.2960 0.0601  0.1046  0.1227  435 ASP A O   
3179 C CB  . ASP A 435 ? 0.3449 0.2819 0.2690 0.0750  0.0935  0.1278  435 ASP A CB  
3180 C CG  . ASP A 435 ? 0.4301 0.3543 0.3354 0.0791  0.0856  0.1292  435 ASP A CG  
3181 O OD1 . ASP A 435 ? 0.4837 0.4059 0.4022 0.0780  0.0883  0.1346  435 ASP A OD1 
3182 O OD2 . ASP A 435 ? 0.4031 0.3200 0.2827 0.0828  0.0757  0.1241  435 ASP A OD2 
3183 N N   . PRO A 436 ? 0.3513 0.3070 0.3319 0.0701  0.1247  0.1424  436 PRO A N   
3184 C CA  . PRO A 436 ? 0.3207 0.2880 0.3208 0.0688  0.1358  0.1454  436 PRO A CA  
3185 C C   . PRO A 436 ? 0.3204 0.2921 0.3067 0.0716  0.1327  0.1400  436 PRO A C   
3186 O O   . PRO A 436 ? 0.3411 0.3012 0.2963 0.0781  0.1271  0.1364  436 PRO A O   
3187 C CB  . PRO A 436 ? 0.3678 0.3264 0.3646 0.0758  0.1468  0.1526  436 PRO A CB  
3188 C CG  . PRO A 436 ? 0.4153 0.3616 0.4031 0.0775  0.1443  0.1560  436 PRO A CG  
3189 C CD  . PRO A 436 ? 0.3958 0.3383 0.3676 0.0756  0.1301  0.1500  436 PRO A CD  
3190 N N   . VAL A 437 ? 0.3148 0.3046 0.3274 0.0659  0.1341  0.1366  437 VAL A N   
3191 C CA  . VAL A 437 ? 0.2857 0.2815 0.2899 0.0681  0.1314  0.1320  437 VAL A CA  
3192 C C   . VAL A 437 ? 0.3081 0.2911 0.2887 0.0786  0.1385  0.1354  437 VAL A C   
3193 O O   . VAL A 437 ? 0.3361 0.3155 0.3223 0.0825  0.1483  0.1414  437 VAL A O   
3194 C CB  . VAL A 437 ? 0.3083 0.3273 0.3474 0.0610  0.1318  0.1286  437 VAL A CB  
3195 C CG1 . VAL A 437 ? 0.3784 0.4029 0.4406 0.0615  0.1460  0.1372  437 VAL A CG1 
3196 C CG2 . VAL A 437 ? 0.3277 0.3529 0.3582 0.0637  0.1281  0.1243  437 VAL A CG2 
3197 N N   . THR A 438 ? 0.3287 0.3047 0.2841 0.0829  0.1320  0.1298  438 THR A N   
3198 C CA  . THR A 438 ? 0.3337 0.2985 0.2684 0.0920  0.1366  0.1295  438 THR A CA  
3199 C C   . THR A 438 ? 0.3255 0.2977 0.2632 0.0934  0.1368  0.1264  438 THR A C   
3200 O O   . THR A 438 ? 0.3556 0.3221 0.2858 0.1006  0.1439  0.1281  438 THR A O   
3201 C CB  . THR A 438 ? 0.3510 0.2971 0.2508 0.0971  0.1292  0.1249  438 THR A CB  
3202 O OG1 . THR A 438 ? 0.3539 0.3008 0.2469 0.0922  0.1164  0.1183  438 THR A OG1 
3203 C CG2 . THR A 438 ? 0.3777 0.3148 0.2716 0.0990  0.1313  0.1297  438 THR A CG2 
3204 N N   . GLU A 439 ? 0.3048 0.2891 0.2524 0.0874  0.1295  0.1222  439 GLU A N   
3205 C CA  . GLU A 439 ? 0.2976 0.2905 0.2502 0.0889  0.1297  0.1200  439 GLU A CA  
3206 C C   . GLU A 439 ? 0.2927 0.3071 0.2807 0.0845  0.1354  0.1242  439 GLU A C   
3207 O O   . GLU A 439 ? 0.2828 0.3141 0.2922 0.0764  0.1310  0.1225  439 GLU A O   
3208 C CB  . GLU A 439 ? 0.2863 0.2804 0.2289 0.0857  0.1184  0.1133  439 GLU A CB  
3209 C CG  . GLU A 439 ? 0.3152 0.2880 0.2244 0.0910  0.1128  0.1079  439 GLU A CG  
3210 C CD  . GLU A 439 ? 0.3187 0.2793 0.2131 0.0902  0.1080  0.1071  439 GLU A CD  
3211 O OE1 . GLU A 439 ? 0.3064 0.2726 0.2076 0.0840  0.1009  0.1063  439 GLU A OE1 
3212 O OE2 . GLU A 439 ? 0.3598 0.3065 0.2376 0.0963  0.1121  0.1083  439 GLU A OE2 
3213 N N   . LYS A 440 ? 0.3001 0.3148 0.2954 0.0897  0.1446  0.1288  440 LYS A N   
3214 C CA  . LYS A 440 ? 0.2806 0.3150 0.3100 0.0858  0.1492  0.1324  440 LYS A CA  
3215 C C   . LYS A 440 ? 0.2841 0.3222 0.3146 0.0916  0.1523  0.1335  440 LYS A C   
3216 O O   . LYS A 440 ? 0.2987 0.3339 0.3340 0.0967  0.1613  0.1389  440 LYS A O   
3217 C CB  . LYS A 440 ? 0.3017 0.3338 0.3449 0.0855  0.1582  0.1388  440 LYS A CB  
3218 C CG  . LYS A 440 ? 0.3144 0.3417 0.3576 0.0804  0.1560  0.1388  440 LYS A CG  
3219 C CD  . LYS A 440 ? 0.3875 0.4082 0.4391 0.0825  0.1662  0.1461  440 LYS A CD  
3220 C CE  . LYS A 440 ? 0.4673 0.4656 0.4850 0.0924  0.1703  0.1485  440 LYS A CE  
3221 N NZ  . LYS A 440 ? 0.4934 0.4853 0.5180 0.0959  0.1813  0.1565  440 LYS A NZ  
3222 N N   . PRO A 441 ? 0.2826 0.3266 0.3088 0.0913  0.1452  0.1289  441 PRO A N   
3223 C CA  . PRO A 441 ? 0.2802 0.3268 0.3072 0.0974  0.1481  0.1305  441 PRO A CA  
3224 C C   . PRO A 441 ? 0.2792 0.3458 0.3388 0.0947  0.1515  0.1347  441 PRO A C   
3225 O O   . PRO A 441 ? 0.2564 0.3412 0.3410 0.0862  0.1468  0.1330  441 PRO A O   
3226 C CB  . PRO A 441 ? 0.2968 0.3470 0.3150 0.0961  0.1388  0.1249  441 PRO A CB  
3227 C CG  . PRO A 441 ? 0.2809 0.3385 0.3039 0.0875  0.1308  0.1207  441 PRO A CG  
3228 C CD  . PRO A 441 ? 0.2623 0.3087 0.2802 0.0863  0.1348  0.1227  441 PRO A CD  
3229 N N   . VAL A 442 ? 0.3083 0.3711 0.3676 0.1021  0.1592  0.1395  442 VAL A N   
3230 C CA  . VAL A 442 ? 0.2803 0.3600 0.3686 0.1006  0.1631  0.1441  442 VAL A CA  
3231 C C   . VAL A 442 ? 0.2901 0.3835 0.3864 0.1018  0.1579  0.1430  442 VAL A C   
3232 O O   . VAL A 442 ? 0.3188 0.4009 0.3953 0.1092  0.1589  0.1431  442 VAL A O   
3233 C CB  . VAL A 442 ? 0.3030 0.3706 0.3877 0.1082  0.1758  0.1512  442 VAL A CB  
3234 C CG1 . VAL A 442 ? 0.3688 0.4549 0.4859 0.1055  0.1794  0.1558  442 VAL A CG1 
3235 C CG2 . VAL A 442 ? 0.3150 0.3675 0.3882 0.1085  0.1808  0.1527  442 VAL A CG2 
3236 N N   . ILE A 443 ? 0.2557 0.3729 0.3811 0.0948  0.1523  0.1418  443 ILE A N   
3237 C CA  . ILE A 443 ? 0.2611 0.3935 0.3964 0.0963  0.1473  0.1417  443 ILE A CA  
3238 C C   . ILE A 443 ? 0.2655 0.3890 0.3946 0.1062  0.1568  0.1485  443 ILE A C   
3239 O O   . ILE A 443 ? 0.3039 0.4230 0.4397 0.1088  0.1664  0.1537  443 ILE A O   
3240 C CB  . ILE A 443 ? 0.2794 0.4385 0.4481 0.0876  0.1403  0.1389  443 ILE A CB  
3241 C CG1 . ILE A 443 ? 0.3128 0.4799 0.4866 0.0782  0.1303  0.1311  443 ILE A CG1 
3242 C CG2 . ILE A 443 ? 0.2987 0.4740 0.4778 0.0902  0.1354  0.1397  443 ILE A CG2 
3243 C CD1 . ILE A 443 ? 0.3256 0.5010 0.4926 0.0773  0.1196  0.1261  443 ILE A CD1 
3244 N N   . GLY A 444 ? 0.2675 0.3883 0.3845 0.1120  0.1546  0.1486  444 GLY A N   
3245 C CA  . GLY A 444 ? 0.3082 0.4185 0.4167 0.1220  0.1632  0.1543  444 GLY A CA  
3246 C C   . GLY A 444 ? 0.3471 0.4292 0.4228 0.1298  0.1692  0.1537  444 GLY A C   
3247 O O   . GLY A 444 ? 0.4036 0.4754 0.4690 0.1384  0.1750  0.1568  444 GLY A O   
3248 N N   . ASP A 445 ? 0.3136 0.3831 0.3729 0.1271  0.1675  0.1491  445 ASP A N   
3249 C CA  . ASP A 445 ? 0.3255 0.3681 0.3531 0.1342  0.1723  0.1470  445 ASP A CA  
3250 C C   . ASP A 445 ? 0.3225 0.3567 0.3310 0.1354  0.1653  0.1412  445 ASP A C   
3251 O O   . ASP A 445 ? 0.3219 0.3680 0.3367 0.1288  0.1559  0.1375  445 ASP A O   
3252 C CB  . ASP A 445 ? 0.3332 0.3660 0.3513 0.1309  0.1732  0.1449  445 ASP A CB  
3253 C CG  . ASP A 445 ? 0.3806 0.4075 0.4025 0.1350  0.1845  0.1511  445 ASP A CG  
3254 O OD1 . ASP A 445 ? 0.3972 0.4324 0.4357 0.1381  0.1909  0.1571  445 ASP A OD1 
3255 O OD2 . ASP A 445 ? 0.3983 0.4132 0.4074 0.1348  0.1867  0.1502  445 ASP A OD2 
3256 N N   . THR A 446 ? 0.3734 0.3866 0.3588 0.1440  0.1704  0.1402  446 THR A N   
3257 C CA  . THR A 446 ? 0.3453 0.3440 0.3081 0.1455  0.1653  0.1336  446 THR A CA  
3258 C C   . THR A 446 ? 0.3756 0.3547 0.3130 0.1448  0.1640  0.1274  446 THR A C   
3259 O O   . THR A 446 ? 0.3972 0.3633 0.3234 0.1495  0.1713  0.1287  446 THR A O   
3260 C CB  . THR A 446 ? 0.3729 0.3588 0.3254 0.1551  0.1717  0.1355  446 THR A CB  
3261 O OG1 . THR A 446 ? 0.3940 0.3993 0.3702 0.1557  0.1718  0.1418  446 THR A OG1 
3262 C CG2 . THR A 446 ? 0.3976 0.3662 0.3265 0.1566  0.1673  0.1283  446 THR A CG2 
3263 N N   . GLU A 447 ? 0.3654 0.3434 0.2942 0.1387  0.1544  0.1210  447 GLU A N   
3264 C CA  . GLU A 447 ? 0.3765 0.3385 0.2829 0.1366  0.1508  0.1151  447 GLU A CA  
3265 C C   . GLU A 447 ? 0.3772 0.3226 0.2599 0.1372  0.1446  0.1075  447 GLU A C   
3266 O O   . GLU A 447 ? 0.3560 0.3084 0.2448 0.1348  0.1397  0.1065  447 GLU A O   
3267 C CB  . GLU A 447 ? 0.3399 0.3155 0.2589 0.1271  0.1444  0.1148  447 GLU A CB  
3268 C CG  . GLU A 447 ? 0.3638 0.3535 0.3057 0.1258  0.1508  0.1217  447 GLU A CG  
3269 C CD  . GLU A 447 ? 0.3484 0.3435 0.2963 0.1182  0.1470  0.1212  447 GLU A CD  
3270 O OE1 . GLU A 447 ? 0.3374 0.3295 0.2751 0.1131  0.1382  0.1158  447 GLU A OE1 
3271 O OE2 . GLU A 447 ? 0.3705 0.3717 0.3331 0.1176  0.1533  0.1265  447 GLU A OE2 
3272 N N   . VAL A 448 ? 0.3838 0.3073 0.2394 0.1407  0.1450  0.1025  448 VAL A N   
3273 C CA  . VAL A 448 ? 0.3937 0.2996 0.2246 0.1399  0.1375  0.0942  448 VAL A CA  
3274 C C   . VAL A 448 ? 0.3908 0.2943 0.2125 0.1336  0.1290  0.0901  448 VAL A C   
3275 O O   . VAL A 448 ? 0.4018 0.3005 0.2171 0.1356  0.1322  0.0915  448 VAL A O   
3276 C CB  . VAL A 448 ? 0.4248 0.3063 0.2300 0.1494  0.1436  0.0909  448 VAL A CB  
3277 C CG1 . VAL A 448 ? 0.4378 0.3000 0.2161 0.1480  0.1350  0.0814  448 VAL A CG1 
3278 C CG2 . VAL A 448 ? 0.4276 0.3107 0.2423 0.1557  0.1517  0.0951  448 VAL A CG2 
3279 N N   . TRP A 449 ? 0.3767 0.2837 0.1986 0.1263  0.1184  0.0861  449 TRP A N   
3280 C CA  . TRP A 449 ? 0.3752 0.2784 0.1873 0.1205  0.1091  0.0820  449 TRP A CA  
3281 C C   . TRP A 449 ? 0.3930 0.2751 0.1775 0.1217  0.1016  0.0736  449 TRP A C   
3282 O O   . TRP A 449 ? 0.3944 0.2732 0.1769 0.1209  0.0986  0.0710  449 TRP A O   
3283 C CB  . TRP A 449 ? 0.3511 0.2739 0.1842 0.1111  0.1017  0.0836  449 TRP A CB  
3284 C CG  . TRP A 449 ? 0.3321 0.2757 0.1919 0.1088  0.1073  0.0908  449 TRP A CG  
3285 C CD1 . TRP A 449 ? 0.3362 0.2872 0.2096 0.1136  0.1179  0.0968  449 TRP A CD1 
3286 C CD2 . TRP A 449 ? 0.3092 0.2691 0.1864 0.1008  0.1024  0.0926  449 TRP A CD2 
3287 N NE1 . TRP A 449 ? 0.3139 0.2848 0.2124 0.1087  0.1195  0.1019  449 TRP A NE1 
3288 C CE2 . TRP A 449 ? 0.3048 0.2813 0.2057 0.1009  0.1104  0.0993  449 TRP A CE2 
3289 C CE3 . TRP A 449 ? 0.3114 0.2730 0.1866 0.0939  0.0921  0.0893  449 TRP A CE3 
3290 C CZ2 . TRP A 449 ? 0.2978 0.2923 0.2202 0.0940  0.1090  0.1023  449 TRP A CZ2 
3291 C CZ3 . TRP A 449 ? 0.3016 0.2813 0.2004 0.0867  0.0893  0.0908  449 TRP A CZ3 
3292 C CH2 . TRP A 449 ? 0.2710 0.2665 0.1920 0.0869  0.0981  0.0973  449 TRP A CH2 
3293 N N   . LYS A 450 ? 0.4121 0.2798 0.1755 0.1239  0.0987  0.0696  450 LYS A N   
3294 C CA  . LYS A 450 ? 0.4323 0.2796 0.1680 0.1251  0.0903  0.0607  450 LYS A CA  
3295 C C   . LYS A 450 ? 0.4229 0.2737 0.1577 0.1178  0.0778  0.0578  450 LYS A C   
3296 O O   . LYS A 450 ? 0.4266 0.2787 0.1593 0.1180  0.0772  0.0597  450 LYS A O   
3297 C CB  . LYS A 450 ? 0.4668 0.2955 0.1783 0.1341  0.0956  0.0581  450 LYS A CB  
3298 C CG  . LYS A 450 ? 0.4738 0.3001 0.1886 0.1419  0.1092  0.0622  450 LYS A CG  
3299 C CD  . LYS A 450 ? 0.5666 0.3691 0.2514 0.1508  0.1120  0.0567  450 LYS A CD  
3300 C CE  . LYS A 450 ? 0.6114 0.4083 0.2977 0.1580  0.1235  0.0589  450 LYS A CE  
3301 N NZ  . LYS A 450 ? 0.7609 0.5387 0.4280 0.1598  0.1197  0.0497  450 LYS A NZ  
3302 N N   . LEU A 451 ? 0.4125 0.2640 0.1488 0.1121  0.0680  0.0538  451 LEU A N   
3303 C CA  . LEU A 451 ? 0.4000 0.2572 0.1414 0.1043  0.0550  0.0506  451 LEU A CA  
3304 C C   . LEU A 451 ? 0.4236 0.2616 0.1391 0.1057  0.0448  0.0411  451 LEU A C   
3305 O O   . LEU A 451 ? 0.4308 0.2592 0.1418 0.1044  0.0395  0.0333  451 LEU A O   
3306 C CB  . LEU A 451 ? 0.3722 0.2452 0.1406 0.0953  0.0488  0.0493  451 LEU A CB  
3307 C CG  . LEU A 451 ? 0.3648 0.2574 0.1580 0.0943  0.0577  0.0576  451 LEU A CG  
3308 C CD1 . LEU A 451 ? 0.3596 0.2654 0.1744 0.0871  0.0517  0.0558  451 LEU A CD1 
3309 C CD2 . LEU A 451 ? 0.3571 0.2624 0.1612 0.0928  0.0609  0.0639  451 LEU A CD2 
3310 N N   . ILE A 452 ? 0.4359 0.2693 0.1381 0.1080  0.0418  0.0411  452 ILE A N   
3311 C CA  . ILE A 452 ? 0.4618 0.2780 0.1384 0.1106  0.0321  0.0323  452 ILE A CA  
3312 C C   . ILE A 452 ? 0.4502 0.2716 0.1320 0.1033  0.0169  0.0286  452 ILE A C   
3313 O O   . ILE A 452 ? 0.4414 0.2721 0.1316 0.1012  0.0145  0.0328  452 ILE A O   
3314 C CB  . ILE A 452 ? 0.4862 0.2969 0.1499 0.1175  0.0376  0.0348  452 ILE A CB  
3315 C CG1 . ILE A 452 ? 0.5417 0.3512 0.2067 0.1243  0.0539  0.0404  452 ILE A CG1 
3316 C CG2 . ILE A 452 ? 0.5306 0.3245 0.1679 0.1206  0.0270  0.0253  452 ILE A CG2 
3317 C CD1 . ILE A 452 ? 0.5884 0.3977 0.2486 0.1302  0.0621  0.0465  452 ILE A CD1 
3318 N N   . ASN A 453 ? 0.4459 0.2651 0.1344 0.0972  0.0066  0.0197  453 ASN A N   
3319 C CA  . ASN A 453 ? 0.4295 0.2581 0.1335 0.0885  -0.0071 0.0161  453 ASN A CA  
3320 C C   . ASN A 453 ? 0.4538 0.2694 0.1351 0.0906  -0.0200 0.0080  453 ASN A C   
3321 O O   . ASN A 453 ? 0.4802 0.2825 0.1495 0.0908  -0.0266 -0.0018 453 ASN A O   
3322 C CB  . ASN A 453 ? 0.4111 0.2463 0.1375 0.0804  -0.0109 0.0119  453 ASN A CB  
3323 C CG  . ASN A 453 ? 0.3907 0.2389 0.1376 0.0713  -0.0226 0.0096  453 ASN A CG  
3324 O OD1 . ASN A 453 ? 0.3930 0.2430 0.1357 0.0710  -0.0301 0.0094  453 ASN A OD1 
3325 N ND2 . ASN A 453 ? 0.3722 0.2291 0.1410 0.0643  -0.0240 0.0083  453 ASN A ND2 
3326 N N   . VAL A 454 ? 0.4549 0.2747 0.1318 0.0920  -0.0241 0.0120  454 VAL A N   
3327 C CA  . VAL A 454 ? 0.4766 0.2878 0.1365 0.0939  -0.0364 0.0053  454 VAL A CA  
3328 C C   . VAL A 454 ? 0.5179 0.3371 0.1916 0.0864  -0.0522 0.0008  454 VAL A C   
3329 O O   . VAL A 454 ? 0.5308 0.3473 0.1977 0.0867  -0.0634 -0.0045 454 VAL A O   
3330 C CB  . VAL A 454 ? 0.5390 0.3502 0.1895 0.1005  -0.0300 0.0117  454 VAL A CB  
3331 C CG1 . VAL A 454 ? 0.5316 0.3363 0.1723 0.1077  -0.0137 0.0164  454 VAL A CG1 
3332 C CG2 . VAL A 454 ? 0.5157 0.3421 0.1851 0.0975  -0.0282 0.0208  454 VAL A CG2 
3333 N N   . THR A 455 ? 0.4452 0.2796 0.1503 0.0776  -0.0515 0.0025  455 THR A N   
3334 C CA  . THR A 455 ? 0.4528 0.2969 0.1782 0.0692  -0.0645 -0.0024 455 THR A CA  
3335 C C   . THR A 455 ? 0.4671 0.3042 0.1958 0.0643  -0.0717 -0.0129 455 THR A C   
3336 O O   . THR A 455 ? 0.4914 0.3165 0.2084 0.0673  -0.0660 -0.0161 455 THR A O   
3337 C CB  . THR A 455 ? 0.4033 0.2670 0.1598 0.0624  -0.0598 0.0041  455 THR A CB  
3338 O OG1 . THR A 455 ? 0.3876 0.2556 0.1595 0.0580  -0.0534 0.0035  455 THR A OG1 
3339 C CG2 . THR A 455 ? 0.4452 0.3149 0.2016 0.0667  -0.0491 0.0146  455 THR A CG2 
3340 N N   . ASN A 456 ? 0.4596 0.3046 0.2071 0.0567  -0.0834 -0.0180 456 ASN A N   
3341 C CA  . ASN A 456 ? 0.5060 0.3451 0.2608 0.0509  -0.0910 -0.0278 456 ASN A CA  
3342 C C   . ASN A 456 ? 0.4796 0.3292 0.2621 0.0437  -0.0842 -0.0251 456 ASN A C   
3343 O O   . ASN A 456 ? 0.4910 0.3373 0.2846 0.0380  -0.0890 -0.0317 456 ASN A O   
3344 C CB  . ASN A 456 ? 0.5321 0.3737 0.2921 0.0470  -0.1082 -0.0350 456 ASN A CB  
3345 C CG  . ASN A 456 ? 0.5945 0.4236 0.3239 0.0546  -0.1172 -0.0397 456 ASN A CG  
3346 O OD1 . ASN A 456 ? 0.6722 0.4856 0.3746 0.0618  -0.1126 -0.0421 456 ASN A OD1 
3347 N ND2 . ASN A 456 ? 0.7115 0.5475 0.4441 0.0540  -0.1297 -0.0407 456 ASN A ND2 
3348 N N   . PHE A 457 ? 0.4107 0.2727 0.2045 0.0439  -0.0730 -0.0155 457 PHE A N   
3349 C CA  . PHE A 457 ? 0.4125 0.2866 0.2312 0.0379  -0.0666 -0.0119 457 PHE A CA  
3350 C C   . PHE A 457 ? 0.3635 0.2389 0.1793 0.0423  -0.0519 -0.0044 457 PHE A C   
3351 O O   . PHE A 457 ? 0.3779 0.2510 0.1795 0.0487  -0.0457 0.0002  457 PHE A O   
3352 C CB  . PHE A 457 ? 0.4961 0.3893 0.3380 0.0322  -0.0695 -0.0084 457 PHE A CB  
3353 C CG  . PHE A 457 ? 0.5672 0.4616 0.4143 0.0285  -0.0836 -0.0145 457 PHE A CG  
3354 C CD1 . PHE A 457 ? 0.5940 0.4883 0.4557 0.0219  -0.0907 -0.0208 457 PHE A CD1 
3355 C CD2 . PHE A 457 ? 0.5418 0.4369 0.3796 0.0320  -0.0896 -0.0137 457 PHE A CD2 
3356 C CE1 . PHE A 457 ? 0.5921 0.4887 0.4609 0.0184  -0.1041 -0.0266 457 PHE A CE1 
3357 C CE2 . PHE A 457 ? 0.5787 0.4757 0.4221 0.0293  -0.1033 -0.0190 457 PHE A CE2 
3358 C CZ  . PHE A 457 ? 0.6090 0.5073 0.4684 0.0223  -0.1108 -0.0258 457 PHE A CZ  
3359 N N   . ALA A 458 ? 0.3490 0.2289 0.1796 0.0391  -0.0461 -0.0026 458 ALA A N   
3360 C CA  . ALA A 458 ? 0.3226 0.2067 0.1543 0.0431  -0.0330 0.0049  458 ALA A CA  
3361 C C   . ALA A 458 ? 0.3303 0.2338 0.1760 0.0418  -0.0287 0.0122  458 ALA A C   
3362 O O   . ALA A 458 ? 0.3215 0.2374 0.1831 0.0360  -0.0342 0.0118  458 ALA A O   
3363 C CB  . ALA A 458 ? 0.3593 0.2437 0.2038 0.0403  -0.0286 0.0055  458 ALA A CB  
3364 N N   . HIS A 459 ? 0.2985 0.2046 0.1394 0.0471  -0.0185 0.0187  459 HIS A N   
3365 C CA  . HIS A 459 ? 0.2775 0.2021 0.1336 0.0456  -0.0136 0.0251  459 HIS A CA  
3366 C C   . HIS A 459 ? 0.2703 0.2027 0.1345 0.0477  -0.0035 0.0308  459 HIS A C   
3367 O O   . HIS A 459 ? 0.2895 0.2120 0.1414 0.0540  0.0037  0.0329  459 HIS A O   
3368 C CB  . HIS A 459 ? 0.2840 0.2066 0.1295 0.0501  -0.0109 0.0283  459 HIS A CB  
3369 C CG  . HIS A 459 ? 0.2933 0.2092 0.1299 0.0494  -0.0207 0.0241  459 HIS A CG  
3370 N ND1 . HIS A 459 ? 0.2789 0.2061 0.1299 0.0444  -0.0269 0.0237  459 HIS A ND1 
3371 C CD2 . HIS A 459 ? 0.3306 0.2298 0.1453 0.0535  -0.0260 0.0197  459 HIS A CD2 
3372 C CE1 . HIS A 459 ? 0.2927 0.2109 0.1318 0.0457  -0.0356 0.0201  459 HIS A CE1 
3373 N NE2 . HIS A 459 ? 0.3272 0.2287 0.1438 0.0511  -0.0357 0.0175  459 HIS A NE2 
3374 N N   . PRO A 460 ? 0.2491 0.1988 0.1330 0.0432  -0.0028 0.0334  460 PRO A N   
3375 C CA  . PRO A 460 ? 0.2412 0.2010 0.1334 0.0457  0.0059  0.0394  460 PRO A CA  
3376 C C   . PRO A 460 ? 0.2411 0.2117 0.1378 0.0480  0.0118  0.0443  460 PRO A C   
3377 O O   . PRO A 460 ? 0.2442 0.2304 0.1550 0.0438  0.0099  0.0448  460 PRO A O   
3378 C CB  . PRO A 460 ? 0.2245 0.1988 0.1343 0.0398  0.0028  0.0395  460 PRO A CB  
3379 C CG  . PRO A 460 ? 0.2195 0.1986 0.1351 0.0342  -0.0055 0.0350  460 PRO A CG  
3380 C CD  . PRO A 460 ? 0.2340 0.1951 0.1328 0.0361  -0.0102 0.0306  460 PRO A CD  
3381 N N   . ILE A 461 ? 0.2464 0.2092 0.1324 0.0546  0.0196  0.0478  461 ILE A N   
3382 C CA  . ILE A 461 ? 0.2423 0.2135 0.1330 0.0569  0.0260  0.0527  461 ILE A CA  
3383 C C   . ILE A 461 ? 0.2291 0.2178 0.1365 0.0575  0.0320  0.0579  461 ILE A C   
3384 O O   . ILE A 461 ? 0.2344 0.2205 0.1398 0.0615  0.0365  0.0604  461 ILE A O   
3385 C CB  . ILE A 461 ? 0.2677 0.2222 0.1387 0.0644  0.0324  0.0545  461 ILE A CB  
3386 C CG1 . ILE A 461 ? 0.2848 0.2227 0.1373 0.0645  0.0254  0.0492  461 ILE A CG1 
3387 C CG2 . ILE A 461 ? 0.2711 0.2350 0.1499 0.0665  0.0405  0.0608  461 ILE A CG2 
3388 C CD1 . ILE A 461 ? 0.2855 0.2310 0.1460 0.0593  0.0186  0.0480  461 ILE A CD1 
3389 N N   . HIS A 462 ? 0.2129 0.2196 0.1374 0.0536  0.0316  0.0593  462 HIS A N   
3390 C CA  . HIS A 462 ? 0.2000 0.2263 0.1420 0.0536  0.0353  0.0633  462 HIS A CA  
3391 C C   . HIS A 462 ? 0.2059 0.2376 0.1543 0.0562  0.0428  0.0678  462 HIS A C   
3392 O O   . HIS A 462 ? 0.2039 0.2346 0.1541 0.0538  0.0422  0.0668  462 HIS A O   
3393 C CB  . HIS A 462 ? 0.1819 0.2258 0.1395 0.0466  0.0282  0.0599  462 HIS A CB  
3394 C CG  . HIS A 462 ? 0.1694 0.2354 0.1449 0.0461  0.0302  0.0627  462 HIS A CG  
3395 N ND1 . HIS A 462 ? 0.1712 0.2431 0.1493 0.0510  0.0350  0.0679  462 HIS A ND1 
3396 C CD2 . HIS A 462 ? 0.1581 0.2423 0.1501 0.0412  0.0271  0.0603  462 HIS A CD2 
3397 C CE1 . HIS A 462 ? 0.1730 0.2667 0.1682 0.0494  0.0343  0.0689  462 HIS A CE1 
3398 N NE2 . HIS A 462 ? 0.1945 0.2957 0.1980 0.0432  0.0294  0.0638  462 HIS A NE2 
3399 N N   . ILE A 463 ? 0.2032 0.2404 0.1563 0.0614  0.0504  0.0732  463 ILE A N   
3400 C CA  . ILE A 463 ? 0.2029 0.2485 0.1669 0.0637  0.0583  0.0782  463 ILE A CA  
3401 C C   . ILE A 463 ? 0.1863 0.2570 0.1737 0.0609  0.0568  0.0795  463 ILE A C   
3402 O O   . ILE A 463 ? 0.1853 0.2629 0.1750 0.0629  0.0556  0.0809  463 ILE A O   
3403 C CB  . ILE A 463 ? 0.2201 0.2535 0.1726 0.0726  0.0688  0.0836  463 ILE A CB  
3404 C CG1 . ILE A 463 ? 0.2446 0.2526 0.1709 0.0758  0.0692  0.0811  463 ILE A CG1 
3405 C CG2 . ILE A 463 ? 0.2402 0.2837 0.2070 0.0749  0.0781  0.0897  463 ILE A CG2 
3406 C CD1 . ILE A 463 ? 0.2845 0.2780 0.1957 0.0853  0.0794  0.0850  463 ILE A CD1 
3407 N N   . HIS A 464 ? 0.2385 0.1908 0.1590 0.0604  0.0417  0.0533  464 HIS A N   
3408 C CA  . HIS A 464 ? 0.2420 0.2038 0.1716 0.0512  0.0439  0.0574  464 HIS A CA  
3409 C C   . HIS A 464 ? 0.2447 0.2201 0.1809 0.0447  0.0513  0.0649  464 HIS A C   
3410 O O   . HIS A 464 ? 0.2611 0.2366 0.1929 0.0481  0.0551  0.0669  464 HIS A O   
3411 C CB  . HIS A 464 ? 0.2581 0.2024 0.1699 0.0467  0.0414  0.0584  464 HIS A CB  
3412 C CG  . HIS A 464 ? 0.2483 0.1838 0.1552 0.0543  0.0348  0.0520  464 HIS A CG  
3413 N ND1 . HIS A 464 ? 0.2807 0.2055 0.1779 0.0512  0.0325  0.0522  464 HIS A ND1 
3414 C CD2 . HIS A 464 ? 0.2478 0.1838 0.1553 0.0656  0.0300  0.0458  464 HIS A CD2 
3415 C CE1 . HIS A 464 ? 0.2900 0.2109 0.1836 0.0622  0.0270  0.0462  464 HIS A CE1 
3416 N NE2 . HIS A 464 ? 0.2543 0.1841 0.1550 0.0705  0.0253  0.0425  464 HIS A NE2 
3417 N N   . LEU A 465 ? 0.2225 0.2119 0.1702 0.0364  0.0534  0.0690  465 LEU A N   
3418 C CA  . LEU A 465 ? 0.2163 0.2247 0.1716 0.0285  0.0600  0.0774  465 LEU A CA  
3419 C C   . LEU A 465 ? 0.2412 0.2672 0.2102 0.0356  0.0651  0.0791  465 LEU A C   
3420 O O   . LEU A 465 ? 0.2320 0.2776 0.2156 0.0326  0.0680  0.0829  465 LEU A O   
3421 C CB  . LEU A 465 ? 0.2527 0.2544 0.1903 0.0212  0.0629  0.0833  465 LEU A CB  
3422 C CG  . LEU A 465 ? 0.2567 0.2828 0.2048 0.0126  0.0665  0.0880  465 LEU A CG  
3423 C CD1 . LEU A 465 ? 0.2722 0.3080 0.2287 0.0001  0.0637  0.0881  465 LEU A CD1 
3424 C CD2 . LEU A 465 ? 0.2949 0.3152 0.2265 0.0056  0.0674  0.0905  465 LEU A CD2 
3425 N N   . ILE A 466 ? 0.2375 0.2546 0.2016 0.0461  0.0648  0.0750  466 ILE A N   
3426 C CA  . ILE A 466 ? 0.2320 0.2593 0.2016 0.0540  0.0702  0.0770  466 ILE A CA  
3427 C C   . ILE A 466 ? 0.2294 0.2509 0.2045 0.0604  0.0664  0.0701  466 ILE A C   
3428 O O   . ILE A 466 ? 0.2367 0.2498 0.2125 0.0590  0.0597  0.0638  466 ILE A O   
3429 C CB  . ILE A 466 ? 0.2671 0.2882 0.2228 0.0600  0.0744  0.0793  466 ILE A CB  
3430 C CG1 . ILE A 466 ? 0.2940 0.2915 0.2350 0.0629  0.0688  0.0728  466 ILE A CG1 
3431 C CG2 . ILE A 466 ? 0.2948 0.3285 0.2493 0.0513  0.0772  0.0857  466 ILE A CG2 
3432 C CD1 . ILE A 466 ? 0.2657 0.2519 0.2053 0.0714  0.0648  0.0653  466 ILE A CD1 
3433 N N   . GLN A 467 ? 0.2420 0.2677 0.2185 0.0677  0.0708  0.0715  467 GLN A N   
3434 C CA  . GLN A 467 ? 0.2368 0.2507 0.2101 0.0735  0.0678  0.0654  467 GLN A CA  
3435 C C   . GLN A 467 ? 0.2388 0.2400 0.1958 0.0829  0.0715  0.0656  467 GLN A C   
3436 O O   . GLN A 467 ? 0.2831 0.2915 0.2362 0.0870  0.0783  0.0718  467 GLN A O   
3437 C CB  . GLN A 467 ? 0.2307 0.2545 0.2150 0.0738  0.0695  0.0665  467 GLN A CB  
3438 C CG  . GLN A 467 ? 0.2070 0.2437 0.2074 0.0645  0.0661  0.0664  467 GLN A CG  
3439 C CD  . GLN A 467 ? 0.2201 0.2484 0.2218 0.0604  0.0577  0.0586  467 GLN A CD  
3440 O OE1 . GLN A 467 ? 0.2271 0.2442 0.2216 0.0632  0.0543  0.0533  467 GLN A OE1 
3441 N NE2 . GLN A 467 ? 0.2367 0.2709 0.2457 0.0538  0.0543  0.0580  467 GLN A NE2 
3442 N N   . PHE A 468 ? 0.2399 0.2231 0.1862 0.0856  0.0668  0.0590  468 PHE A N   
3443 C CA  . PHE A 468 ? 0.2518 0.2187 0.1795 0.0940  0.0695  0.0584  468 PHE A CA  
3444 C C   . PHE A 468 ? 0.2801 0.2315 0.1973 0.0974  0.0681  0.0544  468 PHE A C   
3445 O O   . PHE A 468 ? 0.2784 0.2316 0.2029 0.0918  0.0638  0.0512  468 PHE A O   
3446 C CB  . PHE A 468 ? 0.2705 0.2256 0.1881 0.0928  0.0648  0.0545  468 PHE A CB  
3447 C CG  . PHE A 468 ? 0.2329 0.1849 0.1540 0.0868  0.0555  0.0476  468 PHE A CG  
3448 C CD1 . PHE A 468 ? 0.2521 0.1946 0.1669 0.0858  0.0506  0.0421  468 PHE A CD1 
3449 C CD2 . PHE A 468 ? 0.2430 0.2015 0.1709 0.0823  0.0515  0.0470  468 PHE A CD2 
3450 C CE1 . PHE A 468 ? 0.2549 0.2006 0.1736 0.0803  0.0421  0.0365  468 PHE A CE1 
3451 C CE2 . PHE A 468 ? 0.2593 0.2181 0.1896 0.0794  0.0434  0.0411  468 PHE A CE2 
3452 C CZ  . PHE A 468 ? 0.2547 0.2101 0.1820 0.0784  0.0387  0.0361  468 PHE A CZ  
3453 N N   . LYS A 469 ? 0.2927 0.2270 0.1901 0.1061  0.0718  0.0546  469 LYS A N   
3454 C CA  . LYS A 469 ? 0.3125 0.2233 0.1911 0.1083  0.0696  0.0501  469 LYS A CA  
3455 C C   . LYS A 469 ? 0.3528 0.2453 0.2151 0.1064  0.0643  0.0448  469 LYS A C   
3456 O O   . LYS A 469 ? 0.3329 0.2242 0.1899 0.1108  0.0667  0.0465  469 LYS A O   
3457 C CB  . LYS A 469 ? 0.3457 0.2463 0.2084 0.1216  0.0784  0.0547  469 LYS A CB  
3458 C CG  . LYS A 469 ? 0.3981 0.3154 0.2735 0.1250  0.0835  0.0600  469 LYS A CG  
3459 C CD  . LYS A 469 ? 0.4194 0.3290 0.2963 0.1174  0.0778  0.0556  469 LYS A CD  
3460 C CE  . LYS A 469 ? 0.3513 0.2684 0.2313 0.1247  0.0838  0.0607  469 LYS A CE  
3461 N NZ  . LYS A 469 ? 0.5366 0.4210 0.3868 0.1323  0.0850  0.0587  469 LYS A NZ  
3462 N N   . ILE A 470 ? 0.3192 0.1990 0.1729 0.0989  0.0568  0.0387  470 ILE A N   
3463 C CA  . ILE A 470 ? 0.3529 0.2154 0.1884 0.0964  0.0513  0.0339  470 ILE A CA  
3464 C C   . ILE A 470 ? 0.3837 0.2185 0.1906 0.1056  0.0567  0.0349  470 ILE A C   
3465 O O   . ILE A 470 ? 0.4166 0.2350 0.2089 0.1081  0.0592  0.0351  470 ILE A O   
3466 C CB  . ILE A 470 ? 0.3393 0.2009 0.1739 0.0837  0.0415  0.0279  470 ILE A CB  
3467 C CG1 . ILE A 470 ? 0.3140 0.2040 0.1760 0.0771  0.0368  0.0271  470 ILE A CG1 
3468 C CG2 . ILE A 470 ? 0.3864 0.2339 0.2023 0.0802  0.0355  0.0235  470 ILE A CG2 
3469 C CD1 . ILE A 470 ? 0.3083 0.2048 0.1730 0.0649  0.0279  0.0223  470 ILE A CD1 
3470 N N   . LEU A 471 ? 0.4104 0.2374 0.2063 0.1115  0.0588  0.0355  471 LEU A N   
3471 C CA  . LEU A 471 ? 0.4207 0.2198 0.1869 0.1213  0.0640  0.0362  471 LEU A CA  
3472 C C   . LEU A 471 ? 0.4189 0.1909 0.1597 0.1133  0.0564  0.0299  471 LEU A C   
3473 O O   . LEU A 471 ? 0.4852 0.2294 0.1997 0.1153  0.0578  0.0289  471 LEU A O   
3474 C CB  . LEU A 471 ? 0.4352 0.2374 0.1990 0.1303  0.0694  0.0396  471 LEU A CB  
3475 C CG  . LEU A 471 ? 0.4382 0.2646 0.2196 0.1384  0.0784  0.0471  471 LEU A CG  
3476 C CD1 . LEU A 471 ? 0.4779 0.3080 0.2564 0.1428  0.0816  0.0497  471 LEU A CD1 
3477 C CD2 . LEU A 471 ? 0.4766 0.2978 0.2474 0.1506  0.0871  0.0515  471 LEU A CD2 
3478 N N   . HIS A 472 ? 0.4317 0.2105 0.1773 0.1042  0.0483  0.0260  472 HIS A N   
3479 C CA  . HIS A 472 ? 0.4412 0.1975 0.1617 0.0951  0.0407  0.0206  472 HIS A CA  
3480 C C   . HIS A 472 ? 0.4230 0.1975 0.1557 0.0871  0.0321  0.0175  472 HIS A C   
3481 O O   . HIS A 472 ? 0.4278 0.2245 0.1824 0.0911  0.0331  0.0194  472 HIS A O   
3482 C CB  . HIS A 472 ? 0.5093 0.2307 0.1946 0.1037  0.0453  0.0208  472 HIS A CB  
3483 C CG  . HIS A 472 ? 0.5216 0.2474 0.2100 0.1182  0.0537  0.0252  472 HIS A CG  
3484 N ND1 . HIS A 472 ? 0.5101 0.2511 0.2107 0.1177  0.0515  0.0251  472 HIS A ND1 
3485 C CD2 . HIS A 472 ? 0.5385 0.2576 0.2191 0.1335  0.0645  0.0303  472 HIS A CD2 
3486 C CE1 . HIS A 472 ? 0.5372 0.2794 0.2368 0.1302  0.0603  0.0299  472 HIS A CE1 
3487 N NE2 . HIS A 472 ? 0.5456 0.2771 0.2342 0.1402  0.0685  0.0333  472 HIS A NE2 
3488 N N   . ARG A 473 ? 0.4390 0.2036 0.1551 0.0756  0.0234  0.0129  473 ARG A N   
3489 C CA  . ARG A 473 ? 0.4374 0.2172 0.1590 0.0700  0.0152  0.0101  473 ARG A CA  
3490 C C   . ARG A 473 ? 0.4655 0.2182 0.1546 0.0670  0.0121  0.0076  473 ARG A C   
3491 O O   . ARG A 473 ? 0.5026 0.2290 0.1651 0.0600  0.0109  0.0059  473 ARG A O   
3492 C CB  . ARG A 473 ? 0.4162 0.2220 0.1538 0.0566  0.0057  0.0073  473 ARG A CB  
3493 C CG  . ARG A 473 ? 0.3875 0.2191 0.1556 0.0586  0.0080  0.0093  473 ARG A CG  
3494 C CD  . ARG A 473 ? 0.3711 0.2296 0.1533 0.0465  -0.0014 0.0065  473 ARG A CD  
3495 N NE  . ARG A 473 ? 0.3424 0.2250 0.1526 0.0485  0.0004  0.0082  473 ARG A NE  
3496 C CZ  . ARG A 473 ? 0.3375 0.2199 0.1532 0.0438  0.0025  0.0089  473 ARG A CZ  
3497 N NH1 . ARG A 473 ? 0.3606 0.2174 0.1545 0.0385  0.0040  0.0085  473 ARG A NH1 
3498 N NH2 . ARG A 473 ? 0.3113 0.2173 0.1525 0.0449  0.0033  0.0102  473 ARG A NH2 
3499 N N   . THR A 474 ? 0.4650 0.2218 0.1536 0.0717  0.0106  0.0074  474 THR A N   
3500 C CA  . THR A 474 ? 0.5226 0.2534 0.1804 0.0701  0.0084  0.0054  474 THR A CA  
3501 C C   . THR A 474 ? 0.4910 0.2415 0.1536 0.0631  -0.0017 0.0028  474 THR A C   
3502 O O   . THR A 474 ? 0.4690 0.2419 0.1524 0.0703  -0.0019 0.0040  474 THR A O   
3503 C CB  . THR A 474 ? 0.5610 0.2730 0.2083 0.0857  0.0183  0.0085  474 THR A CB  
3504 O OG1 . THR A 474 ? 0.5656 0.2709 0.2160 0.0947  0.0281  0.0121  474 THR A OG1 
3505 C CG2 . THR A 474 ? 0.5453 0.2224 0.1549 0.0848  0.0176  0.0066  474 THR A CG2 
3506 N N   . PRO A 475 ? 0.5124 0.2557 0.1548 0.0491  -0.0103 -0.0004 475 PRO A N   
3507 C CA  . PRO A 475 ? 0.5076 0.2746 0.1549 0.0431  -0.0202 -0.0023 475 PRO A CA  
3508 C C   . PRO A 475 ? 0.5186 0.2733 0.1541 0.0531  -0.0184 -0.0019 475 PRO A C   
3509 O O   . PRO A 475 ? 0.5422 0.2634 0.1541 0.0584  -0.0123 -0.0013 475 PRO A O   
3510 C CB  . PRO A 475 ? 0.5356 0.2949 0.1597 0.0232  -0.0291 -0.0051 475 PRO A CB  
3511 C CG  . PRO A 475 ? 0.5922 0.3049 0.1841 0.0230  -0.0226 -0.0051 475 PRO A CG  
3512 C CD  . PRO A 475 ? 0.5477 0.2569 0.1564 0.0386  -0.0112 -0.0021 475 PRO A CD  
3513 N N   . PHE A 476 ? 0.5035 0.2851 0.1537 0.0564  -0.0240 -0.0021 476 PHE A N   
3514 C CA  . PHE A 476 ? 0.5142 0.2865 0.1531 0.0649  -0.0238 -0.0018 476 PHE A CA  
3515 C C   . PHE A 476 ? 0.5152 0.3125 0.1542 0.0585  -0.0353 -0.0036 476 PHE A C   
3516 O O   . PHE A 476 ? 0.5042 0.3325 0.1579 0.0507  -0.0425 -0.0044 476 PHE A O   
3517 C CB  . PHE A 476 ? 0.4970 0.2709 0.1513 0.0815  -0.0156 0.0012  476 PHE A CB  
3518 C CG  . PHE A 476 ? 0.4694 0.2760 0.1508 0.0862  -0.0187 0.0019  476 PHE A CG  
3519 C CD1 . PHE A 476 ? 0.4497 0.2716 0.1526 0.0853  -0.0163 0.0029  476 PHE A CD1 
3520 C CD2 . PHE A 476 ? 0.4678 0.2878 0.1506 0.0927  -0.0240 0.0017  476 PHE A CD2 
3521 C CE1 . PHE A 476 ? 0.4257 0.2745 0.1501 0.0905  -0.0190 0.0035  476 PHE A CE1 
3522 C CE2 . PHE A 476 ? 0.4476 0.2934 0.1504 0.0992  -0.0266 0.0023  476 PHE A CE2 
3523 C CZ  . PHE A 476 ? 0.4269 0.2865 0.1501 0.0980  -0.0241 0.0032  476 PHE A CZ  
3524 N N   . ASP A 477 ? 0.5319 0.3172 0.1541 0.0627  -0.0369 -0.0039 477 ASP A N   
3525 C CA  . ASP A 477 ? 0.5370 0.3445 0.1556 0.0582  -0.0476 -0.0051 477 ASP A CA  
3526 C C   . ASP A 477 ? 0.5257 0.3635 0.1681 0.0719  -0.0491 -0.0038 477 ASP A C   
3527 O O   . ASP A 477 ? 0.5120 0.3384 0.1536 0.0859  -0.0443 -0.0024 477 ASP A O   
3528 C CB  . ASP A 477 ? 0.5652 0.3448 0.1555 0.0591  -0.0477 -0.0058 477 ASP A CB  
3529 C CG  . ASP A 477 ? 0.5740 0.3760 0.1584 0.0524  -0.0590 -0.0067 477 ASP A CG  
3530 O OD1 . ASP A 477 ? 0.6167 0.4562 0.2191 0.0566  -0.0654 -0.0062 477 ASP A OD1 
3531 O OD2 . ASP A 477 ? 0.5985 0.3829 0.1638 0.0438  -0.0607 -0.0077 477 ASP A OD2 
3532 N N   . LEU A 478 ? 0.4960 0.3714 0.1566 0.0679  -0.0561 -0.0040 478 LEU A N   
3533 C CA  . LEU A 478 ? 0.5269 0.4291 0.2076 0.0823  -0.0573 -0.0028 478 LEU A CA  
3534 C C   . LEU A 478 ? 0.5151 0.4219 0.1858 0.0928  -0.0619 -0.0024 478 LEU A C   
3535 O O   . LEU A 478 ? 0.5156 0.4167 0.1897 0.1088  -0.0581 -0.0011 478 LEU A O   
3536 C CB  . LEU A 478 ? 0.5639 0.5068 0.2638 0.0758  -0.0639 -0.0031 478 LEU A CB  
3537 C CG  . LEU A 478 ? 0.7039 0.6554 0.4267 0.0819  -0.0584 -0.0021 478 LEU A CG  
3538 C CD1 . LEU A 478 ? 0.6354 0.6322 0.3763 0.0801  -0.0659 -0.0022 478 LEU A CD1 
3539 C CD2 . LEU A 478 ? 0.6281 0.5648 0.3542 0.1004  -0.0518 -0.0005 478 LEU A CD2 
3540 N N   . GLU A 479 ? 0.5353 0.4509 0.1911 0.0835  -0.0702 -0.0034 479 GLU A N   
3541 C CA  . GLU A 479 ? 0.5646 0.4875 0.2159 0.0927  -0.0738 -0.0028 479 GLU A CA  
3542 C C   . GLU A 479 ? 0.5340 0.4171 0.1719 0.1021  -0.0657 -0.0024 479 GLU A C   
3543 O O   . GLU A 479 ? 0.5355 0.4186 0.1772 0.1160  -0.0642 -0.0014 479 GLU A O   
3544 C CB  . GLU A 479 ? 0.7287 0.6716 0.3706 0.0776  -0.0835 -0.0034 479 GLU A CB  
3545 C CG  . GLU A 479 ? 0.7320 0.7279 0.3930 0.0736  -0.0921 -0.0022 479 GLU A CG  
3546 C CD  . GLU A 479 ? 0.8363 0.8529 0.4864 0.0536  -0.1018 -0.0018 479 GLU A CD  
3547 O OE1 . GLU A 479 ? 0.8419 0.8352 0.4708 0.0476  -0.1024 -0.0025 479 GLU A OE1 
3548 O OE2 . GLU A 479 ? 0.8637 0.9194 0.5269 0.0430  -0.1086 -0.0006 479 GLU A OE2 
3549 N N   . ARG A 480 ? 0.5369 0.3854 0.1587 0.0948  -0.0599 -0.0031 480 ARG A N   
3550 C CA  . ARG A 480 ? 0.5474 0.3619 0.1585 0.1035  -0.0515 -0.0022 480 ARG A CA  
3551 C C   . ARG A 480 ? 0.5315 0.3412 0.1555 0.1178  -0.0439 -0.0001 480 ARG A C   
3552 O O   . ARG A 480 ? 0.5357 0.3341 0.1574 0.1281  -0.0405 0.0010  480 ARG A O   
3553 C CB  . ARG A 480 ? 0.5642 0.3455 0.1577 0.0943  -0.0457 -0.0030 480 ARG A CB  
3554 C CG  . ARG A 480 ? 0.5733 0.3227 0.1581 0.1035  -0.0357 -0.0016 480 ARG A CG  
3555 C CD  . ARG A 480 ? 0.5839 0.3314 0.1622 0.1094  -0.0384 -0.0016 480 ARG A CD  
3556 N NE  . ARG A 480 ? 0.5888 0.3111 0.1625 0.1191  -0.0288 0.0002  480 ARG A NE  
3557 C CZ  . ARG A 480 ? 0.6078 0.3027 0.1652 0.1173  -0.0237 0.0000  480 ARG A CZ  
3558 N NH1 . ARG A 480 ? 0.6257 0.3099 0.1680 0.1062  -0.0267 -0.0019 480 ARG A NH1 
3559 N NH2 . ARG A 480 ? 0.6103 0.2881 0.1660 0.1264  -0.0151 0.0021  480 ARG A NH2 
3560 N N   . PHE A 481 ? 0.5147 0.3322 0.1515 0.1173  -0.0411 0.0006  481 PHE A N   
3561 C CA  . PHE A 481 ? 0.5006 0.3154 0.1499 0.1284  -0.0344 0.0029  481 PHE A CA  
3562 C C   . PHE A 481 ? 0.5354 0.3678 0.1917 0.1394  -0.0393 0.0031  481 PHE A C   
3563 O O   . PHE A 481 ? 0.5371 0.3553 0.1922 0.1487  -0.0344 0.0046  481 PHE A O   
3564 C CB  . PHE A 481 ? 0.4795 0.3071 0.1497 0.1238  -0.0314 0.0033  481 PHE A CB  
3565 C CG  . PHE A 481 ? 0.5125 0.3332 0.1926 0.1323  -0.0238 0.0061  481 PHE A CG  
3566 C CD1 . PHE A 481 ? 0.4834 0.2817 0.1601 0.1320  -0.0138 0.0085  481 PHE A CD1 
3567 C CD2 . PHE A 481 ? 0.5526 0.3888 0.2422 0.1411  -0.0266 0.0067  481 PHE A CD2 
3568 C CE1 . PHE A 481 ? 0.5744 0.3683 0.2589 0.1374  -0.0072 0.0117  481 PHE A CE1 
3569 C CE2 . PHE A 481 ? 0.6036 0.4296 0.2978 0.1468  -0.0200 0.0095  481 PHE A CE2 
3570 C CZ  . PHE A 481 ? 0.5325 0.3387 0.2251 0.1434  -0.0105 0.0120  481 PHE A CZ  
3571 N N   . GLN A 482 ? 0.4918 0.3558 0.1563 0.1377  -0.0483 0.0017  482 GLN A N   
3572 C CA  . GLN A 482 ? 0.5171 0.3994 0.1893 0.1495  -0.0521 0.0018  482 GLN A CA  
3573 C C   . GLN A 482 ? 0.5442 0.4090 0.2027 0.1560  -0.0516 0.0017  482 GLN A C   
3574 O O   . GLN A 482 ? 0.6037 0.4650 0.2627 0.1683  -0.0503 0.0021  482 GLN A O   
3575 C CB  . GLN A 482 ? 0.5551 0.4793 0.2394 0.1456  -0.0614 0.0009  482 GLN A CB  
3576 C CG  . GLN A 482 ? 0.5544 0.5001 0.2560 0.1428  -0.0617 0.0010  482 GLN A CG  
3577 C CD  . GLN A 482 ? 0.5818 0.5687 0.2939 0.1324  -0.0705 0.0003  482 GLN A CD  
3578 O OE1 . GLN A 482 ? 0.7772 0.7774 0.4828 0.1258  -0.0767 0.0000  482 GLN A OE1 
3579 N NE2 . GLN A 482 ? 0.6588 0.6671 0.3871 0.1295  -0.0710 0.0003  482 GLN A NE2 
3580 N N   . GLN A 483 ? 0.5224 0.3735 0.1664 0.1476  -0.0525 0.0011  483 GLN A N   
3581 C CA  . GLN A 483 ? 0.5400 0.3749 0.1707 0.1530  -0.0523 0.0011  483 GLN A CA  
3582 C C   . GLN A 483 ? 0.5449 0.3465 0.1687 0.1597  -0.0428 0.0024  483 GLN A C   
3583 O O   . GLN A 483 ? 0.5527 0.3462 0.1726 0.1698  -0.0418 0.0026  483 GLN A O   
3584 C CB  . GLN A 483 ? 0.5554 0.3844 0.1716 0.1411  -0.0558 0.0000  483 GLN A CB  
3585 C CG  . GLN A 483 ? 0.5914 0.4155 0.1961 0.1458  -0.0589 -0.0002 483 GLN A CG  
3586 C CD  . GLN A 483 ? 0.5917 0.3883 0.1773 0.1373  -0.0566 -0.0008 483 GLN A CD  
3587 O OE1 . GLN A 483 ? 0.6045 0.3786 0.1794 0.1436  -0.0529 -0.0005 483 GLN A OE1 
3588 N NE2 . GLN A 483 ? 0.6326 0.4291 0.2123 0.1228  -0.0587 -0.0019 483 GLN A NE2 
3589 N N   . ASP A 484 ? 0.5428 0.3248 0.1636 0.1537  -0.0355 0.0033  484 ASP A N   
3590 C CA  . ASP A 484 ? 0.5493 0.3039 0.1632 0.1581  -0.0266 0.0051  484 ASP A CA  
3591 C C   . ASP A 484 ? 0.6099 0.3562 0.2308 0.1558  -0.0179 0.0073  484 ASP A C   
3592 O O   . ASP A 484 ? 0.5718 0.2987 0.1873 0.1566  -0.0098 0.0092  484 ASP A O   
3593 C CB  . ASP A 484 ? 0.5686 0.3026 0.1657 0.1556  -0.0249 0.0046  484 ASP A CB  
3594 C CG  . ASP A 484 ? 0.5727 0.2965 0.1634 0.1460  -0.0219 0.0044  484 ASP A CG  
3595 O OD1 . ASP A 484 ? 0.5619 0.2963 0.1600 0.1402  -0.0226 0.0041  484 ASP A OD1 
3596 O OD2 . ASP A 484 ? 0.5889 0.2928 0.1657 0.1444  -0.0188 0.0042  484 ASP A OD2 
3597 N N   . GLY A 485 ? 0.5245 0.2871 0.1576 0.1523  -0.0192 0.0075  485 GLY A N   
3598 C CA  . GLY A 485 ? 0.5838 0.3418 0.2250 0.1504  -0.0114 0.0101  485 GLY A CA  
3599 C C   . GLY A 485 ? 0.5696 0.3141 0.2052 0.1442  -0.0048 0.0111  485 GLY A C   
3600 O O   . GLY A 485 ? 0.6154 0.3579 0.2585 0.1431  0.0027  0.0139  485 GLY A O   
3601 N N   . TYR A 486 ? 0.5288 0.2637 0.1510 0.1403  -0.0068 0.0091  486 TYR A N   
3602 C CA  . TYR A 486 ? 0.5363 0.2556 0.1508 0.1356  -0.0004 0.0096  486 TYR A CA  
3603 C C   . TYR A 486 ? 0.5512 0.2804 0.1704 0.1285  -0.0030 0.0084  486 TYR A C   
3604 O O   . TYR A 486 ? 0.5262 0.2718 0.1479 0.1230  -0.0125 0.0056  486 TYR A O   
3605 C CB  . TYR A 486 ? 0.5589 0.2613 0.1549 0.1331  -0.0023 0.0074  486 TYR A CB  
3606 C CG  . TYR A 486 ? 0.5712 0.2543 0.1565 0.1298  0.0042  0.0076  486 TYR A CG  
3607 C CD1 . TYR A 486 ? 0.6156 0.2876 0.2023 0.1357  0.0155  0.0108  486 TYR A CD1 
3608 C CD2 . TYR A 486 ? 0.5851 0.2614 0.1580 0.1206  -0.0008 0.0047  486 TYR A CD2 
3609 C CE1 . TYR A 486 ? 0.6121 0.2670 0.1888 0.1356  0.0217  0.0111  486 TYR A CE1 
3610 C CE2 . TYR A 486 ? 0.6007 0.2549 0.1611 0.1189  0.0053  0.0047  486 TYR A CE2 
3611 C CZ  . TYR A 486 ? 0.6015 0.2452 0.1642 0.1279  0.0167  0.0080  486 TYR A CZ  
3612 O OH  . TYR A 486 ? 0.6612 0.2835 0.2110 0.1291  0.0230  0.0084  486 TYR A OH  
3613 N N   . ILE A 487 ? 0.5566 0.2798 0.1809 0.1279  0.0054  0.0105  487 ILE A N   
3614 C CA  . ILE A 487 ? 0.5193 0.2496 0.1520 0.1200  0.0044  0.0091  487 ILE A CA  
3615 C C   . ILE A 487 ? 0.5413 0.2476 0.1489 0.1149  0.0045  0.0071  487 ILE A C   
3616 O O   . ILE A 487 ? 0.5655 0.2517 0.1632 0.1194  0.0133  0.0089  487 ILE A O   
3617 C CB  . ILE A 487 ? 0.5274 0.2607 0.1753 0.1228  0.0138  0.0126  487 ILE A CB  
3618 C CG1 . ILE A 487 ? 0.7128 0.4652 0.3824 0.1262  0.0148  0.0150  487 ILE A CG1 
3619 C CG2 . ILE A 487 ? 0.5220 0.2617 0.1769 0.1144  0.0116  0.0108  487 ILE A CG2 
3620 C CD1 . ILE A 487 ? 0.6211 0.3897 0.2977 0.1253  0.0057  0.0126  487 ILE A CD1 
3621 N N   . ASP A 488 ? 0.5511 0.2609 0.1498 0.1048  -0.0052 0.0035  488 ASP A N   
3622 C CA  . ASP A 488 ? 0.5789 0.2644 0.1532 0.0965  -0.0065 0.0013  488 ASP A CA  
3623 C C   . ASP A 488 ? 0.5796 0.2653 0.1521 0.0863  -0.0084 0.0000  488 ASP A C   
3624 O O   . ASP A 488 ? 0.5726 0.2795 0.1527 0.0750  -0.0178 -0.0020 488 ASP A O   
3625 C CB  . ASP A 488 ? 0.5921 0.2824 0.1562 0.0890  -0.0167 -0.0014 488 ASP A CB  
3626 C CG  . ASP A 488 ? 0.6727 0.3348 0.2118 0.0803  -0.0173 -0.0032 488 ASP A CG  
3627 O OD1 . ASP A 488 ? 0.6869 0.3247 0.2147 0.0796  -0.0110 -0.0030 488 ASP A OD1 
3628 O OD2 . ASP A 488 ? 0.7821 0.4467 0.3119 0.0741  -0.0247 -0.0049 488 ASP A OD2 
3629 N N   . TYR A 489 ? 0.5863 0.2523 0.1537 0.0899  0.0006  0.0015  489 TYR A N   
3630 C CA  . TYR A 489 ? 0.5889 0.2519 0.1533 0.0807  -0.0006 0.0005  489 TYR A CA  
3631 C C   . TYR A 489 ? 0.6175 0.2638 0.1589 0.0645  -0.0085 -0.0029 489 TYR A C   
3632 O O   . TYR A 489 ? 0.6435 0.2644 0.1652 0.0644  -0.0072 -0.0036 489 TYR A O   
3633 C CB  . TYR A 489 ? 0.6139 0.2603 0.1780 0.0906  0.0112  0.0034  489 TYR A CB  
3634 C CG  . TYR A 489 ? 0.5581 0.2292 0.1527 0.1010  0.0176  0.0072  489 TYR A CG  
3635 C CD1 . TYR A 489 ? 0.5287 0.2306 0.1521 0.0954  0.0131  0.0069  489 TYR A CD1 
3636 C CD2 . TYR A 489 ? 0.6344 0.3001 0.2300 0.1150  0.0280  0.0112  489 TYR A CD2 
3637 C CE1 . TYR A 489 ? 0.5280 0.2508 0.1783 0.1030  0.0183  0.0103  489 TYR A CE1 
3638 C CE2 . TYR A 489 ? 0.6451 0.3347 0.2686 0.1212  0.0331  0.0150  489 TYR A CE2 
3639 C CZ  . TYR A 489 ? 0.6311 0.3473 0.2809 0.1148  0.0281  0.0144  489 TYR A CZ  
3640 O OH  . TYR A 489 ? 0.6461 0.3829 0.3204 0.1196  0.0327  0.0181  489 TYR A OH  
3641 N N   . THR A 490 ? 0.6137 0.2752 0.1575 0.0497  -0.0168 -0.0048 490 THR A N   
3642 C CA  . THR A 490 ? 0.6391 0.2920 0.1638 0.0302  -0.0257 -0.0075 490 THR A CA  
3643 C C   . THR A 490 ? 0.6743 0.3027 0.1840 0.0209  -0.0237 -0.0080 490 THR A C   
3644 O O   . THR A 490 ? 0.7906 0.4109 0.2843 0.0022  -0.0309 -0.0097 490 THR A O   
3645 C CB  . THR A 490 ? 0.6681 0.3611 0.2063 0.0175  -0.0380 -0.0088 490 THR A CB  
3646 O OG1 . THR A 490 ? 0.6484 0.3685 0.2110 0.0174  -0.0385 -0.0081 490 THR A OG1 
3647 C CG2 . THR A 490 ? 0.6350 0.3483 0.1835 0.0275  -0.0407 -0.0083 490 THR A CG2 
3648 N N   . GLY A 491 ? 0.6509 0.2685 0.1656 0.0332  -0.0141 -0.0060 491 GLY A N   
3649 C CA  . GLY A 491 ? 0.7238 0.3156 0.2233 0.0279  -0.0112 -0.0061 491 GLY A CA  
3650 C C   . GLY A 491 ? 0.6858 0.2691 0.1932 0.0474  0.0012  -0.0030 491 GLY A C   
3651 O O   . GLY A 491 ? 0.6875 0.2897 0.2152 0.0624  0.0070  -0.0006 491 GLY A O   
3652 N N   . PRO A 492 ? 0.7407 0.2966 0.2322 0.0472  0.0053  -0.0025 492 PRO A N   
3653 C CA  . PRO A 492 ? 0.7684 0.3193 0.2678 0.0661  0.0169  0.0010  492 PRO A CA  
3654 C C   . PRO A 492 ? 0.6640 0.2500 0.1923 0.0669  0.0175  0.0024  492 PRO A C   
3655 O O   . PRO A 492 ? 0.6692 0.2765 0.2068 0.0514  0.0085  0.0003  492 PRO A O   
3656 C CB  . PRO A 492 ? 0.7379 0.2486 0.2086 0.0630  0.0185  0.0006  492 PRO A CB  
3657 C CG  . PRO A 492 ? 0.7799 0.2886 0.2387 0.0374  0.0066  -0.0028 492 PRO A CG  
3658 C CD  . PRO A 492 ? 0.7934 0.3241 0.2596 0.0286  -0.0012 -0.0047 492 PRO A CD  
3659 N N   . PRO A 493 ? 0.6679 0.2635 0.2129 0.0843  0.0279  0.0066  493 PRO A N   
3660 C CA  . PRO A 493 ? 0.6165 0.2453 0.1953 0.0840  0.0287  0.0086  493 PRO A CA  
3661 C C   . PRO A 493 ? 0.6621 0.2812 0.2321 0.0722  0.0250  0.0069  493 PRO A C   
3662 O O   . PRO A 493 ? 0.6786 0.2593 0.2142 0.0718  0.0268  0.0061  493 PRO A O   
3663 C CB  . PRO A 493 ? 0.5916 0.2264 0.1828 0.1042  0.0412  0.0140  493 PRO A CB  
3664 C CG  . PRO A 493 ? 0.7534 0.3638 0.3234 0.1154  0.0465  0.0144  493 PRO A CG  
3665 C CD  . PRO A 493 ? 0.7954 0.3753 0.3355 0.1034  0.0387  0.0097  493 PRO A CD  
3666 N N   . ILE A 494 ? 0.5865 0.2403 0.1883 0.0623  0.0195  0.0064  494 ILE A N   
3667 C CA  . ILE A 494 ? 0.5992 0.2517 0.1991 0.0493  0.0153  0.0050  494 ILE A CA  
3668 C C   . ILE A 494 ? 0.5570 0.2309 0.1867 0.0593  0.0223  0.0087  494 ILE A C   
3669 O O   . ILE A 494 ? 0.5360 0.2442 0.2005 0.0651  0.0239  0.0106  494 ILE A O   
3670 C CB  . ILE A 494 ? 0.6095 0.2890 0.2221 0.0290  0.0029  0.0016  494 ILE A CB  
3671 C CG1 . ILE A 494 ? 0.7162 0.3758 0.2974 0.0179  -0.0043 -0.0015 494 ILE A CG1 
3672 C CG2 . ILE A 494 ? 0.6567 0.3401 0.2711 0.0148  -0.0012 0.0006  494 ILE A CG2 
3673 C CD1 . ILE A 494 ? 0.7793 0.4707 0.3724 -0.0011 -0.0166 -0.0041 494 ILE A CD1 
3674 N N   . GLU A 495 ? 0.5716 0.2234 0.1853 0.0612  0.0264  0.0098  495 GLU A N   
3675 C CA  . GLU A 495 ? 0.5232 0.1948 0.1632 0.0708  0.0331  0.0137  495 GLU A CA  
3676 C C   . GLU A 495 ? 0.5035 0.2136 0.1786 0.0577  0.0262  0.0124  495 GLU A C   
3677 O O   . GLU A 495 ? 0.5101 0.2260 0.1825 0.0404  0.0164  0.0086  495 GLU A O   
3678 C CB  . GLU A 495 ? 0.6433 0.2825 0.2563 0.0743  0.0374  0.0148  495 GLU A CB  
3679 C CG  . GLU A 495 ? 0.7798 0.3903 0.3608 0.0549  0.0288  0.0103  495 GLU A CG  
3680 C CD  . GLU A 495 ? 0.9666 0.5363 0.5128 0.0598  0.0334  0.0114  495 GLU A CD  
3681 O OE1 . GLU A 495 ? 0.9751 0.5180 0.4920 0.0423  0.0264  0.0082  495 GLU A OE1 
3682 O OE2 . GLU A 495 ? 0.9357 0.5025 0.4851 0.0807  0.0437  0.0152  495 GLU A OE2 
3683 N N   . PRO A 496 ? 0.4604 0.1980 0.1674 0.0653  0.0311  0.0158  496 PRO A N   
3684 C CA  . PRO A 496 ? 0.4262 0.1957 0.1624 0.0537  0.0252  0.0147  496 PRO A CA  
3685 C C   . PRO A 496 ? 0.4560 0.2095 0.1748 0.0397  0.0203  0.0122  496 PRO A C   
3686 O O   . PRO A 496 ? 0.4882 0.2073 0.1777 0.0433  0.0243  0.0130  496 PRO A O   
3687 C CB  . PRO A 496 ? 0.4246 0.2161 0.1892 0.0657  0.0331  0.0195  496 PRO A CB  
3688 C CG  . PRO A 496 ? 0.5216 0.2898 0.2672 0.0820  0.0432  0.0235  496 PRO A CG  
3689 C CD  . PRO A 496 ? 0.5144 0.2561 0.2308 0.0839  0.0422  0.0214  496 PRO A CD  
3690 N N   . ALA A 497 ? 0.4464 0.2246 0.1810 0.0238  0.0115  0.0095  497 ALA A N   
3691 C CA  . ALA A 497 ? 0.4524 0.2202 0.1725 0.0075  0.0061  0.0074  497 ALA A CA  
3692 C C   . ALA A 497 ? 0.4317 0.1988 0.1615 0.0135  0.0122  0.0103  497 ALA A C   
3693 O O   . ALA A 497 ? 0.4054 0.1910 0.1608 0.0274  0.0190  0.0138  497 ALA A O   
3694 C CB  . ALA A 497 ? 0.4256 0.2283 0.1643 -0.0098 -0.0043 0.0045  497 ALA A CB  
3695 N N   . VAL A 498 ? 0.4553 0.2011 0.1631 0.0015  0.0093  0.0090  498 VAL A N   
3696 C CA  . VAL A 498 ? 0.4568 0.1919 0.1642 0.0093  0.0157  0.0120  498 VAL A CA  
3697 C C   . VAL A 498 ? 0.4276 0.2052 0.1789 0.0108  0.0167  0.0139  498 VAL A C   
3698 O O   . VAL A 498 ? 0.4151 0.1925 0.1746 0.0222  0.0238  0.0175  498 VAL A O   
3699 C CB  . VAL A 498 ? 0.5298 0.2293 0.2006 -0.0050 0.0119  0.0101  498 VAL A CB  
3700 C CG1 . VAL A 498 ? 0.6235 0.2692 0.2430 -0.0009 0.0139  0.0093  498 VAL A CG1 
3701 C CG2 . VAL A 498 ? 0.5153 0.2353 0.1922 -0.0306 0.0006  0.0065  498 VAL A CG2 
3702 N N   . HIS A 499 ? 0.3830 0.1972 0.1613 0.0006  0.0099  0.0118  499 HIS A N   
3703 C CA  . HIS A 499 ? 0.3439 0.1954 0.1602 0.0012  0.0103  0.0132  499 HIS A CA  
3704 C C   . HIS A 499 ? 0.3154 0.1895 0.1586 0.0164  0.0156  0.0160  499 HIS A C   
3705 O O   . HIS A 499 ? 0.2917 0.1954 0.1645 0.0170  0.0156  0.0170  499 HIS A O   
3706 C CB  . HIS A 499 ? 0.3283 0.2103 0.1596 -0.0157 0.0005  0.0098  499 HIS A CB  
3707 C CG  . HIS A 499 ? 0.3244 0.2212 0.1588 -0.0165 -0.0044 0.0077  499 HIS A CG  
3708 N ND1 . HIS A 499 ? 0.4149 0.2921 0.2208 -0.0250 -0.0093 0.0053  499 HIS A ND1 
3709 C CD2 . HIS A 499 ? 0.3237 0.2493 0.1834 -0.0084 -0.0047 0.0081  499 HIS A CD2 
3710 C CE1 . HIS A 499 ? 0.3859 0.2832 0.2022 -0.0219 -0.0126 0.0043  499 HIS A CE1 
3711 N NE2 . HIS A 499 ? 0.3532 0.2783 0.2009 -0.0111 -0.0097 0.0059  499 HIS A NE2 
3712 N N   . GLU A 500 ? 0.3265 0.1866 0.1585 0.0276  0.0197  0.0171  500 GLU A N   
3713 C CA  . GLU A 500 ? 0.3099 0.1903 0.1640 0.0390  0.0237  0.0197  500 GLU A CA  
3714 C C   . GLU A 500 ? 0.3327 0.1955 0.1758 0.0548  0.0333  0.0240  500 GLU A C   
3715 O O   . GLU A 500 ? 0.3410 0.2069 0.1862 0.0628  0.0360  0.0254  500 GLU A O   
3716 C CB  . GLU A 500 ? 0.2981 0.1910 0.1556 0.0356  0.0174  0.0166  500 GLU A CB  
3717 C CG  . GLU A 500 ? 0.3301 0.1970 0.1564 0.0311  0.0138  0.0137  500 GLU A CG  
3718 C CD  . GLU A 500 ? 0.3474 0.2261 0.1754 0.0299  0.0082  0.0114  500 GLU A CD  
3719 O OE1 . GLU A 500 ? 0.3109 0.2173 0.1626 0.0327  0.0064  0.0115  500 GLU A OE1 
3720 O OE2 . GLU A 500 ? 0.3748 0.2320 0.1771 0.0267  0.0058  0.0095  500 GLU A OE2 
3721 N N   . ARG A 501 ? 0.3490 0.1942 0.1792 0.0602  0.0389  0.0266  501 ARG A N   
3722 C CA  . ARG A 501 ? 0.3579 0.1886 0.1755 0.0770  0.0485  0.0314  501 ARG A CA  
3723 C C   . ARG A 501 ? 0.3609 0.2158 0.2028 0.0865  0.0559  0.0375  501 ARG A C   
3724 O O   . ARG A 501 ? 0.3924 0.2442 0.2282 0.1010  0.0642  0.0425  501 ARG A O   
3725 C CB  . ARG A 501 ? 0.4350 0.2254 0.2141 0.0808  0.0505  0.0307  501 ARG A CB  
3726 C CG  . ARG A 501 ? 0.4377 0.2019 0.1884 0.0724  0.0443  0.0256  501 ARG A CG  
3727 C CD  . ARG A 501 ? 0.5127 0.2320 0.2204 0.0715  0.0444  0.0241  501 ARG A CD  
3728 N NE  . ARG A 501 ? 0.5419 0.2374 0.2219 0.0601  0.0375  0.0193  501 ARG A NE  
3729 C CZ  . ARG A 501 ? 0.5901 0.2401 0.2253 0.0574  0.0366  0.0174  501 ARG A CZ  
3730 N NH1 . ARG A 501 ? 0.6786 0.2992 0.2893 0.0668  0.0423  0.0196  501 ARG A NH1 
3731 N NH2 . ARG A 501 ? 0.6745 0.3069 0.2865 0.0446  0.0295  0.0133  501 ARG A NH2 
3732 N N   . GLY A 502 ? 0.3085 0.1896 0.1778 0.0786  0.0530  0.0376  502 GLY A N   
3733 C CA  . GLY A 502 ? 0.2997 0.2053 0.1920 0.0849  0.0591  0.0435  502 GLY A CA  
3734 C C   . GLY A 502 ? 0.2649 0.1923 0.1757 0.0859  0.0600  0.0456  502 GLY A C   
3735 O O   . GLY A 502 ? 0.2938 0.2164 0.1991 0.0842  0.0566  0.0426  502 GLY A O   
3736 N N   . TRP A 503 ? 0.2560 0.2070 0.1873 0.0879  0.0644  0.0510  503 TRP A N   
3737 C CA  . TRP A 503 ? 0.2323 0.2014 0.1782 0.0864  0.0650  0.0533  503 TRP A CA  
3738 C C   . TRP A 503 ? 0.2323 0.2085 0.1896 0.0754  0.0564  0.0479  503 TRP A C   
3739 O O   . TRP A 503 ? 0.2229 0.2060 0.1903 0.0682  0.0522  0.0454  503 TRP A O   
3740 C CB  . TRP A 503 ? 0.2504 0.2430 0.2130 0.0885  0.0712  0.0608  503 TRP A CB  
3741 C CG  . TRP A 503 ? 0.2714 0.2640 0.2240 0.1012  0.0800  0.0671  503 TRP A CG  
3742 C CD1 . TRP A 503 ? 0.2770 0.2683 0.2244 0.1097  0.0849  0.0705  503 TRP A CD1 
3743 C CD2 . TRP A 503 ? 0.2548 0.2486 0.1991 0.1087  0.0852  0.0710  503 TRP A CD2 
3744 N NE1 . TRP A 503 ? 0.3048 0.2970 0.2415 0.1207  0.0904  0.0763  503 TRP A NE1 
3745 C CE2 . TRP A 503 ? 0.2873 0.2822 0.2232 0.1200  0.0907  0.0766  503 TRP A CE2 
3746 C CE3 . TRP A 503 ? 0.2920 0.2853 0.2345 0.1056  0.0838  0.0702  503 TRP A CE3 
3747 C CZ2 . TRP A 503 ? 0.3054 0.3027 0.2340 0.1272  0.0932  0.0812  503 TRP A CZ2 
3748 C CZ3 . TRP A 503 ? 0.2785 0.2743 0.2114 0.1145  0.0906  0.0753  503 TRP A CZ3 
3749 C CH2 . TRP A 503 ? 0.2813 0.2798 0.2099 0.1239  0.0931  0.0802  503 TRP A CH2 
3750 N N   . LYS A 504 ? 0.2293 0.2042 0.1838 0.0752  0.0541  0.0464  504 LYS A N   
3751 C CA  . LYS A 504 ? 0.2138 0.1935 0.1743 0.0685  0.0461  0.0412  504 LYS A CA  
3752 C C   . LYS A 504 ? 0.2084 0.1942 0.1728 0.0694  0.0464  0.0431  504 LYS A C   
3753 O O   . LYS A 504 ? 0.2319 0.2151 0.1907 0.0739  0.0519  0.0476  504 LYS A O   
3754 C CB  . LYS A 504 ? 0.2321 0.1976 0.1773 0.0668  0.0400  0.0353  504 LYS A CB  
3755 C CG  . LYS A 504 ? 0.2412 0.2017 0.1825 0.0607  0.0369  0.0323  504 LYS A CG  
3756 C CD  . LYS A 504 ? 0.2671 0.2129 0.1896 0.0564  0.0309  0.0272  504 LYS A CD  
3757 C CE  . LYS A 504 ? 0.2314 0.1917 0.1605 0.0517  0.0229  0.0231  504 LYS A CE  
3758 N NZ  . LYS A 504 ? 0.2265 0.2107 0.1771 0.0474  0.0197  0.0225  504 LYS A NZ  
3759 N N   . ASP A 505 ? 0.1957 0.1894 0.1680 0.0651  0.0405  0.0400  505 ASP A N   
3760 C CA  . ASP A 505 ? 0.1929 0.1862 0.1630 0.0662  0.0397  0.0410  505 ASP A CA  
3761 C C   . ASP A 505 ? 0.2256 0.2149 0.1885 0.0681  0.0324  0.0354  505 ASP A C   
3762 O O   . ASP A 505 ? 0.2084 0.1927 0.1646 0.0709  0.0313  0.0358  505 ASP A O   
3763 C CB  . ASP A 505 ? 0.2194 0.2237 0.2014 0.0616  0.0409  0.0443  505 ASP A CB  
3764 C CG  . ASP A 505 ? 0.2043 0.2196 0.1987 0.0575  0.0362  0.0408  505 ASP A CG  
3765 O OD1 . ASP A 505 ? 0.1913 0.2079 0.1841 0.0585  0.0298  0.0354  505 ASP A OD1 
3766 O OD2 . ASP A 505 ? 0.2084 0.2334 0.2143 0.0530  0.0388  0.0440  505 ASP A OD2 
3767 N N   . THR A 506 ? 0.2457 0.1877 0.1427 0.0591  0.0342  0.0568  506 THR A N   
3768 C CA  . THR A 506 ? 0.2565 0.1915 0.1452 0.0529  0.0310  0.0515  506 THR A CA  
3769 C C   . THR A 506 ? 0.2583 0.1714 0.1285 0.0554  0.0316  0.0493  506 THR A C   
3770 O O   . THR A 506 ? 0.2845 0.1884 0.1493 0.0559  0.0306  0.0506  506 THR A O   
3771 C CB  . THR A 506 ? 0.2418 0.1853 0.1357 0.0442  0.0249  0.0495  506 THR A CB  
3772 O OG1 . THR A 506 ? 0.2607 0.2226 0.1700 0.0428  0.0241  0.0507  506 THR A OG1 
3773 C CG2 . THR A 506 ? 0.2592 0.1991 0.1480 0.0383  0.0215  0.0445  506 THR A CG2 
3774 N N   . VAL A 507 ? 0.2716 0.1752 0.1313 0.0569  0.0328  0.0461  507 VAL A N   
3775 C CA  . VAL A 507 ? 0.2993 0.1804 0.1393 0.0601  0.0331  0.0429  507 VAL A CA  
3776 C C   . VAL A 507 ? 0.3083 0.1828 0.1391 0.0532  0.0271  0.0372  507 VAL A C   
3777 O O   . VAL A 507 ? 0.2928 0.1763 0.1273 0.0517  0.0263  0.0364  507 VAL A O   
3778 C CB  . VAL A 507 ? 0.3053 0.1786 0.1368 0.0715  0.0412  0.0445  507 VAL A CB  
3779 C CG1 . VAL A 507 ? 0.3386 0.2221 0.1740 0.0732  0.0446  0.0455  507 VAL A CG1 
3780 C CG2 . VAL A 507 ? 0.3601 0.2077 0.1685 0.0750  0.0410  0.0396  507 VAL A CG2 
3781 N N   . LYS A 508 ? 0.3042 0.1627 0.1235 0.0491  0.0225  0.0336  508 LYS A N   
3782 C CA  . LYS A 508 ? 0.3069 0.1589 0.1174 0.0426  0.0157  0.0280  508 LYS A CA  
3783 C C   . LYS A 508 ? 0.3478 0.1862 0.1404 0.0499  0.0180  0.0248  508 LYS A C   
3784 O O   . LYS A 508 ? 0.3701 0.1886 0.1466 0.0553  0.0201  0.0225  508 LYS A O   
3785 C CB  . LYS A 508 ? 0.3398 0.1785 0.1447 0.0351  0.0100  0.0254  508 LYS A CB  
3786 C CG  . LYS A 508 ? 0.3432 0.1789 0.1432 0.0267  0.0017  0.0199  508 LYS A CG  
3787 C CD  . LYS A 508 ? 0.3801 0.1985 0.1727 0.0195  -0.0036 0.0171  508 LYS A CD  
3788 C CE  . LYS A 508 ? 0.4190 0.2405 0.2128 0.0091  -0.0130 0.0126  508 LYS A CE  
3789 N NZ  . LYS A 508 ? 0.5413 0.3420 0.3258 0.0018  -0.0187 0.0089  508 LYS A NZ  
3790 N N   . ALA A 509 ? 0.3165 0.1643 0.1104 0.0506  0.0177  0.0247  509 ALA A N   
3791 C CA  . ALA A 509 ? 0.3351 0.1711 0.1101 0.0572  0.0193  0.0221  509 ALA A CA  
3792 C C   . ALA A 509 ? 0.3701 0.1968 0.1331 0.0503  0.0092  0.0155  509 ALA A C   
3793 O O   . ALA A 509 ? 0.3728 0.2123 0.1449 0.0440  0.0032  0.0153  509 ALA A O   
3794 C CB  . ALA A 509 ? 0.3466 0.1974 0.1295 0.0616  0.0246  0.0268  509 ALA A CB  
3795 N N   . GLU A 510 ? 0.3834 0.1874 0.1266 0.0515  0.0068  0.0100  510 GLU A N   
3796 C CA  . GLU A 510 ? 0.4087 0.2024 0.1413 0.0435  -0.0043 0.0031  510 GLU A CA  
3797 C C   . GLU A 510 ? 0.4011 0.1951 0.1204 0.0463  -0.0080 0.0005  510 GLU A C   
3798 O O   . GLU A 510 ? 0.4420 0.2314 0.1483 0.0567  -0.0011 0.0019  510 GLU A O   
3799 C CB  . GLU A 510 ? 0.4369 0.2032 0.1502 0.0447  -0.0056 -0.0027 510 GLU A CB  
3800 C CG  . GLU A 510 ? 0.4347 0.1965 0.1582 0.0412  -0.0036 -0.0002 510 GLU A CG  
3801 C CD  . GLU A 510 ? 0.5025 0.2703 0.2393 0.0269  -0.0127 -0.0009 510 GLU A CD  
3802 O OE1 . GLU A 510 ? 0.5208 0.3021 0.2644 0.0200  -0.0197 -0.0023 510 GLU A OE1 
3803 O OE2 . GLU A 510 ? 0.5188 0.2769 0.2587 0.0229  -0.0126 0.0002  510 GLU A OE2 
3804 N N   . PRO A 511 ? 0.4466 0.2455 0.1680 0.0375  -0.0191 -0.0030 511 PRO A N   
3805 C CA  . PRO A 511 ? 0.4531 0.2522 0.1608 0.0403  -0.0243 -0.0052 511 PRO A CA  
3806 C C   . PRO A 511 ? 0.4859 0.2594 0.1619 0.0465  -0.0255 -0.0120 511 PRO A C   
3807 O O   . PRO A 511 ? 0.5205 0.2749 0.1860 0.0434  -0.0288 -0.0181 511 PRO A O   
3808 C CB  . PRO A 511 ? 0.4792 0.2889 0.1982 0.0285  -0.0372 -0.0079 511 PRO A CB  
3809 C CG  . PRO A 511 ? 0.4733 0.2847 0.2079 0.0193  -0.0384 -0.0079 511 PRO A CG  
3810 C CD  . PRO A 511 ? 0.4325 0.2364 0.1680 0.0248  -0.0275 -0.0048 511 PRO A CD  
3811 N N   . GLY A 512 ? 0.4740 0.2495 0.1408 0.0546  -0.0226 -0.0108 512 GLY A N   
3812 C CA  . GLY A 512 ? 0.5231 0.2798 0.1677 0.0603  -0.0231 -0.0168 512 GLY A CA  
3813 C C   . GLY A 512 ? 0.5153 0.2554 0.1499 0.0690  -0.0122 -0.0172 512 GLY A C   
3814 O O   . GLY A 512 ? 0.5412 0.2610 0.1560 0.0726  -0.0136 -0.0236 512 GLY A O   
3815 N N   . MET A 513 ? 0.5016 0.2508 0.1505 0.0729  -0.0016 -0.0102 513 MET A N   
3816 C CA  . MET A 513 ? 0.4880 0.2252 0.1312 0.0821  0.0095  -0.0090 513 MET A CA  
3817 C C   . MET A 513 ? 0.4671 0.2234 0.1276 0.0898  0.0221  0.0006  513 MET A C   
3818 O O   . MET A 513 ? 0.4626 0.2402 0.1424 0.0858  0.0220  0.0062  513 MET A O   
3819 C CB  . MET A 513 ? 0.5266 0.2547 0.1717 0.0770  0.0083  -0.0104 513 MET A CB  
3820 C CG  . MET A 513 ? 0.5041 0.2170 0.1422 0.0657  -0.0049 -0.0189 513 MET A CG  
3821 S SD  . MET A 513 ? 0.5355 0.2324 0.1798 0.0624  -0.0034 -0.0198 513 MET A SD  
3822 C CE  . MET A 513 ? 0.5539 0.2176 0.1659 0.0771  0.0043  -0.0260 513 MET A CE  
3823 N N   . VAL A 514 ? 0.4949 0.2432 0.1492 0.1009  0.0326  0.0023  514 VAL A N   
3824 C CA  . VAL A 514 ? 0.4629 0.2276 0.1353 0.1079  0.0450  0.0113  514 VAL A CA  
3825 C C   . VAL A 514 ? 0.4563 0.2180 0.1352 0.1087  0.0490  0.0131  514 VAL A C   
3826 O O   . VAL A 514 ? 0.4824 0.2232 0.1454 0.1136  0.0505  0.0088  514 VAL A O   
3827 C CB  . VAL A 514 ? 0.4825 0.2427 0.1454 0.1200  0.0545  0.0135  514 VAL A CB  
3828 C CG1 . VAL A 514 ? 0.4771 0.2558 0.1615 0.1264  0.0670  0.0233  514 VAL A CG1 
3829 C CG2 . VAL A 514 ? 0.4927 0.2544 0.1460 0.1194  0.0500  0.0119  514 VAL A CG2 
3830 N N   . THR A 515 ? 0.4268 0.2085 0.1288 0.1036  0.0500  0.0193  515 THR A N   
3831 C CA  . THR A 515 ? 0.4173 0.2009 0.1303 0.1037  0.0531  0.0227  515 THR A CA  
3832 C C   . THR A 515 ? 0.4261 0.2253 0.1545 0.1129  0.0654  0.0313  515 THR A C   
3833 O O   . THR A 515 ? 0.4029 0.2237 0.1514 0.1102  0.0671  0.0366  515 THR A O   
3834 C CB  . THR A 515 ? 0.4137 0.2131 0.1487 0.0904  0.0443  0.0240  515 THR A CB  
3835 O OG1 . THR A 515 ? 0.4236 0.2105 0.1480 0.0813  0.0331  0.0166  515 THR A OG1 
3836 C CG2 . THR A 515 ? 0.3850 0.1918 0.1382 0.0901  0.0469  0.0285  515 THR A CG2 
3837 N N   . SER A 516 ? 0.4516 0.2406 0.1735 0.1233  0.0734  0.0324  516 SER A N   
3838 C CA  . SER A 516 ? 0.4602 0.2644 0.1976 0.1330  0.0852  0.0404  516 SER A CA  
3839 C C   . SER A 516 ? 0.4285 0.2439 0.1866 0.1325  0.0861  0.0457  516 SER A C   
3840 O O   . SER A 516 ? 0.4314 0.2321 0.1838 0.1320  0.0821  0.0423  516 SER A O   
3841 C CB  . SER A 516 ? 0.4563 0.2447 0.1773 0.1457  0.0925  0.0390  516 SER A CB  
3842 O OG  . SER A 516 ? 0.4905 0.2739 0.1991 0.1451  0.0901  0.0357  516 SER A OG  
3843 N N   . VAL A 517 ? 0.3930 0.2343 0.1766 0.1318  0.0903  0.0539  517 VAL A N   
3844 C CA  . VAL A 517 ? 0.3878 0.2454 0.1956 0.1312  0.0903  0.0597  517 VAL A CA  
3845 C C   . VAL A 517 ? 0.3588 0.2338 0.1822 0.1412  0.1021  0.0682  517 VAL A C   
3846 O O   . VAL A 517 ? 0.3701 0.2506 0.1918 0.1450  0.1096  0.0710  517 VAL A O   
3847 C CB  . VAL A 517 ? 0.3561 0.2311 0.1837 0.1174  0.0807  0.0605  517 VAL A CB  
3848 C CG1 . VAL A 517 ? 0.3906 0.2512 0.2053 0.1074  0.0699  0.0529  517 VAL A CG1 
3849 C CG2 . VAL A 517 ? 0.3668 0.2610 0.2088 0.1135  0.0828  0.0644  517 VAL A CG2 
3850 N N   . ILE A 518 ? 0.3674 0.2516 0.2064 0.1459  0.1039  0.0731  518 ILE A N   
3851 C CA  . ILE A 518 ? 0.3521 0.2550 0.2092 0.1557  0.1146  0.0818  518 ILE A CA  
3852 C C   . ILE A 518 ? 0.3265 0.2550 0.2140 0.1498  0.1096  0.0877  518 ILE A C   
3853 O O   . ILE A 518 ? 0.3272 0.2535 0.2172 0.1445  0.1006  0.0859  518 ILE A O   
3854 C CB  . ILE A 518 ? 0.3776 0.2664 0.2212 0.1692  0.1225  0.0821  518 ILE A CB  
3855 C CG1 . ILE A 518 ? 0.3772 0.2876 0.2395 0.1752  0.1317  0.0916  518 ILE A CG1 
3856 C CG2 . ILE A 518 ? 0.3907 0.2706 0.2339 0.1692  0.1162  0.0801  518 ILE A CG2 
3857 C CD1 . ILE A 518 ? 0.4071 0.3034 0.2531 0.1862  0.1391  0.0920  518 ILE A CD1 
3858 N N   . MET A 519 ? 0.3347 0.2874 0.2451 0.1513  0.1158  0.0953  519 MET A N   
3859 C CA  . MET A 519 ? 0.3140 0.2934 0.2544 0.1437  0.1102  0.1004  519 MET A CA  
3860 C C   . MET A 519 ? 0.2937 0.2967 0.2581 0.1510  0.1203  0.1100  519 MET A C   
3861 O O   . MET A 519 ? 0.3036 0.3029 0.2608 0.1568  0.1300  0.1125  519 MET A O   
3862 C CB  . MET A 519 ? 0.3466 0.3271 0.2871 0.1293  0.1020  0.0959  519 MET A CB  
3863 C CG  . MET A 519 ? 0.2729 0.2674 0.2264 0.1268  0.1083  0.1005  519 MET A CG  
3864 S SD  . MET A 519 ? 0.3018 0.2880 0.2459 0.1129  0.0990  0.0935  519 MET A SD  
3865 C CE  . MET A 519 ? 0.3279 0.2824 0.2344 0.1178  0.0986  0.0855  519 MET A CE  
3866 N N   . LYS A 520 ? 0.2785 0.3052 0.2702 0.1478  0.1155  0.1151  520 LYS A N   
3867 C CA  . LYS A 520 ? 0.2872 0.3393 0.3055 0.1495  0.1216  0.1239  520 LYS A CA  
3868 C C   . LYS A 520 ? 0.3197 0.3971 0.3672 0.1381  0.1134  0.1263  520 LYS A C   
3869 O O   . LYS A 520 ? 0.3114 0.3931 0.3639 0.1328  0.1019  0.1239  520 LYS A O   
3870 C CB  . LYS A 520 ? 0.3029 0.3593 0.3255 0.1584  0.1241  0.1283  520 LYS A CB  
3871 C CG  . LYS A 520 ? 0.3127 0.3963 0.3643 0.1584  0.1281  0.1374  520 LYS A CG  
3872 C CD  . LYS A 520 ? 0.3833 0.4644 0.4309 0.1704  0.1348  0.1412  520 LYS A CD  
3873 C CE  . LYS A 520 ? 0.3869 0.4958 0.4643 0.1706  0.1385  0.1505  520 LYS A CE  
3874 N NZ  . LYS A 520 ? 0.4227 0.5373 0.5052 0.1807  0.1404  0.1545  520 LYS A NZ  
3875 N N   . PHE A 521 ? 0.2795 0.3708 0.3433 0.1324  0.1179  0.1304  521 PHE A N   
3876 C CA  . PHE A 521 ? 0.2595 0.3721 0.3500 0.1192  0.1093  0.1316  521 PHE A CA  
3877 C C   . PHE A 521 ? 0.2601 0.3991 0.3800 0.1211  0.1090  0.1394  521 PHE A C   
3878 O O   . PHE A 521 ? 0.2760 0.4180 0.3992 0.1270  0.1176  0.1452  521 PHE A O   
3879 C CB  . PHE A 521 ? 0.2479 0.3604 0.3420 0.1116  0.1142  0.1329  521 PHE A CB  
3880 C CG  . PHE A 521 ? 0.2288 0.3160 0.2947 0.1070  0.1109  0.1246  521 PHE A CG  
3881 C CD1 . PHE A 521 ? 0.2813 0.3471 0.3191 0.1160  0.1191  0.1228  521 PHE A CD1 
3882 C CD2 . PHE A 521 ? 0.2542 0.3388 0.3206 0.0943  0.0988  0.1179  521 PHE A CD2 
3883 C CE1 . PHE A 521 ? 0.2698 0.3139 0.2827 0.1115  0.1144  0.1151  521 PHE A CE1 
3884 C CE2 . PHE A 521 ? 0.2720 0.3354 0.3142 0.0906  0.0953  0.1105  521 PHE A CE2 
3885 C CZ  . PHE A 521 ? 0.2766 0.3206 0.2930 0.0989  0.1028  0.1094  521 PHE A CZ  
3886 N N   . THR A 522 ? 0.2675 0.4236 0.4059 0.1153  0.0972  0.1388  522 THR A N   
3887 C CA  . THR A 522 ? 0.2251 0.4031 0.3864 0.1164  0.0940  0.1446  522 THR A CA  
3888 C C   . THR A 522 ? 0.2042 0.4078 0.3969 0.1034  0.0847  0.1460  522 THR A C   
3889 O O   . THR A 522 ? 0.2288 0.4519 0.4440 0.1024  0.0844  0.1517  522 THR A O   
3890 C CB  . THR A 522 ? 0.2923 0.4674 0.4450 0.1239  0.0873  0.1435  522 THR A CB  
3891 O OG1 . THR A 522 ? 0.2918 0.4632 0.4382 0.1174  0.0751  0.1374  522 THR A OG1 
3892 C CG2 . THR A 522 ? 0.3446 0.4944 0.4686 0.1367  0.0965  0.1424  522 THR A CG2 
3893 N N   . GLU A 523 ? 0.2057 0.4073 0.3980 0.0924  0.0757  0.1398  523 GLU A N   
3894 C CA  . GLU A 523 ? 0.2010 0.4234 0.4204 0.0789  0.0654  0.1393  523 GLU A CA  
3895 C C   . GLU A 523 ? 0.1702 0.3757 0.3763 0.0660  0.0589  0.1299  523 GLU A C   
3896 O O   . GLU A 523 ? 0.1974 0.3782 0.3756 0.0679  0.0622  0.1246  523 GLU A O   
3897 C CB  . GLU A 523 ? 0.2306 0.4700 0.4611 0.0787  0.0520  0.1389  523 GLU A CB  
3898 C CG  . GLU A 523 ? 0.1994 0.4197 0.4007 0.0811  0.0440  0.1314  523 GLU A CG  
3899 C CD  . GLU A 523 ? 0.2873 0.5254 0.4990 0.0817  0.0311  0.1324  523 GLU A CD  
3900 O OE1 . GLU A 523 ? 0.3550 0.6190 0.5952 0.0811  0.0285  0.1384  523 GLU A OE1 
3901 O OE2 . GLU A 523 ? 0.2411 0.4667 0.4316 0.0823  0.0235  0.1272  523 GLU A OE2 
3902 N N   . ASN A 524 ? 0.1681 0.3875 0.3951 0.0531  0.0491  0.1275  524 ASN A N   
3903 C CA  . ASN A 524 ? 0.1565 0.3625 0.3750 0.0406  0.0415  0.1181  524 ASN A CA  
3904 C C   . ASN A 524 ? 0.1592 0.3493 0.3704 0.0383  0.0518  0.1190  524 ASN A C   
3905 O O   . ASN A 524 ? 0.1600 0.3275 0.3456 0.0380  0.0518  0.1124  524 ASN A O   
3906 C CB  . ASN A 524 ? 0.1554 0.3453 0.3465 0.0410  0.0322  0.1085  524 ASN A CB  
3907 C CG  . ASN A 524 ? 0.1635 0.3695 0.3628 0.0396  0.0192  0.1066  524 ASN A CG  
3908 O OD1 . ASN A 524 ? 0.1521 0.3776 0.3760 0.0316  0.0113  0.1070  524 ASN A OD1 
3909 N ND2 . ASN A 524 ? 0.1565 0.3547 0.3355 0.0474  0.0165  0.1051  524 ASN A ND2 
3910 N N   . PRO A 525 ? 0.1672 0.3692 0.4010 0.0363  0.0606  0.1277  525 PRO A N   
3911 C CA  . PRO A 525 ? 0.1828 0.3697 0.4103 0.0327  0.0691  0.1289  525 PRO A CA  
3912 C C   . PRO A 525 ? 0.1758 0.3522 0.4016 0.0196  0.0584  0.1198  525 PRO A C   
3913 O O   . PRO A 525 ? 0.2155 0.4026 0.4562 0.0106  0.0461  0.1148  525 PRO A O   
3914 C CB  . PRO A 525 ? 0.1717 0.3784 0.4293 0.0317  0.0793  0.1412  525 PRO A CB  
3915 C CG  . PRO A 525 ? 0.2040 0.4381 0.4909 0.0278  0.0701  0.1430  525 PRO A CG  
3916 C CD  . PRO A 525 ? 0.1733 0.4046 0.4421 0.0351  0.0613  0.1365  525 PRO A CD  
3917 N N   . GLY A 526 ? 0.1747 0.3292 0.3808 0.0193  0.0629  0.1171  526 GLY A N   
3918 C CA  . GLY A 526 ? 0.1883 0.3303 0.3906 0.0089  0.0542  0.1085  526 GLY A CA  
3919 C C   . GLY A 526 ? 0.1805 0.2980 0.3539 0.0130  0.0583  0.1048  526 GLY A C   
3920 O O   . GLY A 526 ? 0.2141 0.3237 0.3712 0.0227  0.0681  0.1094  526 GLY A O   
3921 N N   . GLU A 527 ? 0.1771 0.2828 0.3442 0.0057  0.0499  0.0959  527 GLU A N   
3922 C CA  . GLU A 527 ? 0.2071 0.2913 0.3507 0.0081  0.0519  0.0921  527 GLU A CA  
3923 C C   . GLU A 527 ? 0.2019 0.2785 0.3219 0.0127  0.0457  0.0834  527 GLU A C   
3924 O O   . GLU A 527 ? 0.2036 0.2819 0.3236 0.0077  0.0354  0.0749  527 GLU A O   
3925 C CB  . GLU A 527 ? 0.2318 0.3078 0.3837 -0.0018 0.0470  0.0877  527 GLU A CB  
3926 C CG  . GLU A 527 ? 0.3156 0.3918 0.4851 -0.0059 0.0551  0.0973  527 GLU A CG  
3927 C CD  . GLU A 527 ? 0.3823 0.4483 0.5362 0.0029  0.0676  0.1058  527 GLU A CD  
3928 O OE1 . GLU A 527 ? 0.3843 0.4343 0.5138 0.0078  0.0670  0.1014  527 GLU A OE1 
3929 O OE2 . GLU A 527 ? 0.4987 0.5733 0.6648 0.0048  0.0779  0.1169  527 GLU A OE2 
3930 N N   . TYR A 528 ? 0.1792 0.2467 0.2787 0.0218  0.0519  0.0855  528 TYR A N   
3931 C CA  . TYR A 528 ? 0.1706 0.2296 0.2482 0.0256  0.0470  0.0784  528 TYR A CA  
3932 C C   . TYR A 528 ? 0.1714 0.2125 0.2279 0.0290  0.0504  0.0771  528 TYR A C   
3933 O O   . TYR A 528 ? 0.1973 0.2322 0.2559 0.0278  0.0550  0.0806  528 TYR A O   
3934 C CB  . TYR A 528 ? 0.1666 0.2316 0.2394 0.0333  0.0495  0.0816  528 TYR A CB  
3935 C CG  . TYR A 528 ? 0.1623 0.2465 0.2555 0.0311  0.0451  0.0835  528 TYR A CG  
3936 C CD1 . TYR A 528 ? 0.1639 0.2628 0.2788 0.0319  0.0510  0.0920  528 TYR A CD1 
3937 C CD2 . TYR A 528 ? 0.1707 0.2597 0.2621 0.0284  0.0350  0.0772  528 TYR A CD2 
3938 C CE1 . TYR A 528 ? 0.1602 0.2790 0.2955 0.0299  0.0459  0.0940  528 TYR A CE1 
3939 C CE2 . TYR A 528 ? 0.1560 0.2634 0.2650 0.0267  0.0296  0.0790  528 TYR A CE2 
3940 C CZ  . TYR A 528 ? 0.1561 0.2788 0.2878 0.0274  0.0345  0.0872  528 TYR A CZ  
3941 O OH  . TYR A 528 ? 0.1583 0.3014 0.3092 0.0258  0.0283  0.0893  528 TYR A OH  
3942 N N   . VAL A 529 ? 0.1781 0.2110 0.2147 0.0329  0.0478  0.0723  529 VAL A N   
3943 C CA  . VAL A 529 ? 0.2057 0.2232 0.2225 0.0357  0.0490  0.0702  529 VAL A CA  
3944 C C   . VAL A 529 ? 0.1871 0.1979 0.1850 0.0424  0.0503  0.0694  529 VAL A C   
3945 O O   . VAL A 529 ? 0.1939 0.2106 0.1935 0.0443  0.0490  0.0694  529 VAL A O   
3946 C CB  . VAL A 529 ? 0.2048 0.2174 0.2184 0.0303  0.0413  0.0623  529 VAL A CB  
3947 C CG1 . VAL A 529 ? 0.2167 0.2324 0.2475 0.0238  0.0396  0.0620  529 VAL A CG1 
3948 C CG2 . VAL A 529 ? 0.2374 0.2541 0.2469 0.0284  0.0341  0.0558  529 VAL A CG2 
3949 N N   . TRP A 530 ? 0.2069 0.2044 0.1865 0.0458  0.0521  0.0686  530 TRP A N   
3950 C CA  . TRP A 530 ? 0.2253 0.2129 0.1851 0.0499  0.0507  0.0653  530 TRP A CA  
3951 C C   . TRP A 530 ? 0.2088 0.1866 0.1559 0.0479  0.0462  0.0607  530 TRP A C   
3952 O O   . TRP A 530 ? 0.2187 0.1948 0.1683 0.0467  0.0470  0.0621  530 TRP A O   
3953 C CB  . TRP A 530 ? 0.2196 0.2012 0.1687 0.0587  0.0590  0.0702  530 TRP A CB  
3954 C CG  . TRP A 530 ? 0.2471 0.2204 0.1861 0.0630  0.0655  0.0742  530 TRP A CG  
3955 C CD1 . TRP A 530 ? 0.2755 0.2544 0.2258 0.0634  0.0721  0.0811  530 TRP A CD1 
3956 C CD2 . TRP A 530 ? 0.2465 0.2045 0.1612 0.0677  0.0659  0.0719  530 TRP A CD2 
3957 N NE1 . TRP A 530 ? 0.2692 0.2369 0.2021 0.0688  0.0773  0.0839  530 TRP A NE1 
3958 C CE2 . TRP A 530 ? 0.2534 0.2084 0.1638 0.0717  0.0730  0.0779  530 TRP A CE2 
3959 C CE3 . TRP A 530 ? 0.2957 0.2420 0.1919 0.0685  0.0606  0.0657  530 TRP A CE3 
3960 C CZ2 . TRP A 530 ? 0.2991 0.2415 0.1888 0.0760  0.0729  0.0750  530 TRP A CZ2 
3961 C CZ3 . TRP A 530 ? 0.2960 0.2285 0.1702 0.0728  0.0612  0.0643  530 TRP A CZ3 
3962 C CH2 . TRP A 530 ? 0.2952 0.2268 0.1677 0.0763  0.0664  0.0675  530 TRP A CH2 
3963 N N   . HIS A 531 ? 0.2153 0.1875 0.1504 0.0470  0.0410  0.0555  531 HIS A N   
3964 C CA  . HIS A 531 ? 0.2234 0.1910 0.1517 0.0439  0.0355  0.0510  531 HIS A CA  
3965 C C   . HIS A 531 ? 0.2250 0.1861 0.1400 0.0431  0.0310  0.0467  531 HIS A C   
3966 O O   . HIS A 531 ? 0.2287 0.1896 0.1421 0.0436  0.0311  0.0465  531 HIS A O   
3967 C CB  . HIS A 531 ? 0.2117 0.1886 0.1548 0.0379  0.0311  0.0479  531 HIS A CB  
3968 C CG  . HIS A 531 ? 0.2022 0.1880 0.1533 0.0343  0.0277  0.0451  531 HIS A CG  
3969 N ND1 . HIS A 531 ? 0.2184 0.2050 0.1644 0.0314  0.0227  0.0405  531 HIS A ND1 
3970 C CD2 . HIS A 531 ? 0.2316 0.2265 0.1951 0.0334  0.0286  0.0470  531 HIS A CD2 
3971 C CE1 . HIS A 531 ? 0.2332 0.2282 0.1863 0.0293  0.0210  0.0397  531 HIS A CE1 
3972 N NE2 . HIS A 531 ? 0.2436 0.2439 0.2073 0.0305  0.0238  0.0433  531 HIS A NE2 
3973 N N   . CYS A 532 ? 0.2308 0.1868 0.1374 0.0416  0.0267  0.0436  532 CYS A N   
3974 C CA  . CYS A 532 ? 0.2160 0.1686 0.1148 0.0382  0.0212  0.0392  532 CYS A CA  
3975 C C   . CYS A 532 ? 0.2087 0.1726 0.1199 0.0327  0.0178  0.0367  532 CYS A C   
3976 O O   . CYS A 532 ? 0.2251 0.1976 0.1480 0.0309  0.0173  0.0360  532 CYS A O   
3977 C CB  . CYS A 532 ? 0.2291 0.1766 0.1187 0.0376  0.0167  0.0369  532 CYS A CB  
3978 S SG  . CYS A 532 ? 0.2509 0.1948 0.1331 0.0321  0.0098  0.0321  532 CYS A SG  
3979 N N   . HIS A 533 ? 0.2096 0.1723 0.1170 0.0302  0.0157  0.0353  533 HIS A N   
3980 C CA  . HIS A 533 ? 0.1848 0.1578 0.1009 0.0254  0.0131  0.0334  533 HIS A CA  
3981 C C   . HIS A 533 ? 0.1984 0.1737 0.1132 0.0207  0.0086  0.0302  533 HIS A C   
3982 O O   . HIS A 533 ? 0.2012 0.1846 0.1210 0.0169  0.0072  0.0289  533 HIS A O   
3983 C CB  . HIS A 533 ? 0.1954 0.1683 0.1105 0.0257  0.0142  0.0356  533 HIS A CB  
3984 C CG  . HIS A 533 ? 0.1927 0.1785 0.1190 0.0240  0.0136  0.0355  533 HIS A CG  
3985 N ND1 . HIS A 533 ? 0.1824 0.1763 0.1119 0.0195  0.0106  0.0325  533 HIS A ND1 
3986 C CD2 . HIS A 533 ? 0.2090 0.2012 0.1434 0.0261  0.0151  0.0377  533 HIS A CD2 
3987 C CE1 . HIS A 533 ? 0.1814 0.1850 0.1184 0.0192  0.0101  0.0322  533 HIS A CE1 
3988 N NE2 . HIS A 533 ? 0.2303 0.2334 0.1712 0.0227  0.0122  0.0353  533 HIS A NE2 
3989 N N   . ILE A 534 ? 0.1869 0.1565 0.0955 0.0209  0.0063  0.0290  534 ILE A N   
3990 C CA  . ILE A 534 ? 0.2030 0.1798 0.1162 0.0171  0.0021  0.0263  534 ILE A CA  
3991 C C   . ILE A 534 ? 0.1999 0.1855 0.1239 0.0190  0.0033  0.0255  534 ILE A C   
3992 O O   . ILE A 534 ? 0.1911 0.1726 0.1145 0.0229  0.0047  0.0270  534 ILE A O   
3993 C CB  . ILE A 534 ? 0.2214 0.1907 0.1253 0.0168  -0.0020 0.0254  534 ILE A CB  
3994 C CG1 . ILE A 534 ? 0.2256 0.1851 0.1197 0.0134  -0.0039 0.0250  534 ILE A CG1 
3995 C CG2 . ILE A 534 ? 0.2211 0.2011 0.1332 0.0144  -0.0063 0.0234  534 ILE A CG2 
3996 C CD1 . ILE A 534 ? 0.2426 0.1901 0.1234 0.0136  -0.0084 0.0232  534 ILE A CD1 
3997 N N   . LEU A 535 ? 0.1931 0.1894 0.1262 0.0166  0.0032  0.0234  535 LEU A N   
3998 C CA  . LEU A 535 ? 0.1667 0.1682 0.1091 0.0187  0.0046  0.0219  535 LEU A CA  
3999 C C   . LEU A 535 ? 0.1883 0.1897 0.1335 0.0212  0.0030  0.0213  535 LEU A C   
4000 O O   . LEU A 535 ? 0.1867 0.1859 0.1368 0.0241  0.0046  0.0217  535 LEU A O   
4001 C CB  . LEU A 535 ? 0.1890 0.2008 0.1377 0.0163  0.0047  0.0187  535 LEU A CB  
4002 C CG  . LEU A 535 ? 0.1557 0.1688 0.1012 0.0142  0.0056  0.0200  535 LEU A CG  
4003 C CD1 . LEU A 535 ? 0.1745 0.1979 0.1240 0.0127  0.0056  0.0166  535 LEU A CD1 
4004 C CD2 . LEU A 535 ? 0.1842 0.1919 0.1296 0.0166  0.0074  0.0229  535 LEU A CD2 
4005 N N   . GLU A 536 ? 0.1715 0.1752 0.1146 0.0200  -0.0004 0.0207  536 GLU A N   
4006 C CA  . GLU A 536 ? 0.1837 0.1880 0.1288 0.0231  -0.0029 0.0210  536 GLU A CA  
4007 C C   . GLU A 536 ? 0.1944 0.1872 0.1309 0.0271  -0.0024 0.0246  536 GLU A C   
4008 O O   . GLU A 536 ? 0.2415 0.2331 0.1797 0.0311  -0.0034 0.0261  536 GLU A O   
4009 C CB  . GLU A 536 ? 0.2005 0.2114 0.1458 0.0202  -0.0076 0.0201  536 GLU A CB  
4010 C CG  . GLU A 536 ? 0.1810 0.2064 0.1373 0.0176  -0.0071 0.0174  536 GLU A CG  
4011 C CD  . GLU A 536 ? 0.2067 0.2348 0.1623 0.0134  -0.0041 0.0166  536 GLU A CD  
4012 O OE1 . GLU A 536 ? 0.2090 0.2288 0.1561 0.0110  -0.0038 0.0184  536 GLU A OE1 
4013 O OE2 . GLU A 536 ? 0.1774 0.2157 0.1401 0.0133  -0.0017 0.0143  536 GLU A OE2 
4014 N N   . HIS A 537 ? 0.1908 0.1749 0.1173 0.0269  -0.0007 0.0265  537 HIS A N   
4015 C CA  . HIS A 537 ? 0.2119 0.1854 0.1290 0.0314  0.0016  0.0303  537 HIS A CA  
4016 C C   . HIS A 537 ? 0.2098 0.1823 0.1337 0.0335  0.0074  0.0330  537 HIS A C   
4017 O O   . HIS A 537 ? 0.2183 0.1866 0.1424 0.0372  0.0095  0.0366  537 HIS A O   
4018 C CB  . HIS A 537 ? 0.2345 0.1986 0.1372 0.0313  0.0017  0.0308  537 HIS A CB  
4019 C CG  . HIS A 537 ? 0.2374 0.1999 0.1322 0.0285  -0.0048 0.0281  537 HIS A CG  
4020 N ND1 . HIS A 537 ? 0.2713 0.2232 0.1524 0.0276  -0.0061 0.0271  537 HIS A ND1 
4021 C CD2 . HIS A 537 ? 0.2598 0.2302 0.1599 0.0261  -0.0108 0.0262  537 HIS A CD2 
4022 C CE1 . HIS A 537 ? 0.2745 0.2273 0.1526 0.0237  -0.0132 0.0243  537 HIS A CE1 
4023 N NE2 . HIS A 537 ? 0.2687 0.2341 0.1591 0.0227  -0.0161 0.0241  537 HIS A NE2 
4024 N N   . GLU A 538 ? 0.2001 0.1768 0.1303 0.0308  0.0097  0.0318  538 GLU A N   
4025 C CA  . GLU A 538 ? 0.2034 0.1814 0.1429 0.0312  0.0139  0.0338  538 GLU A CA  
4026 C C   . GLU A 538 ? 0.2233 0.2026 0.1726 0.0319  0.0138  0.0334  538 GLU A C   
4027 O O   . GLU A 538 ? 0.2275 0.2026 0.1809 0.0336  0.0174  0.0375  538 GLU A O   
4028 C CB  . GLU A 538 ? 0.2207 0.2057 0.1661 0.0278  0.0139  0.0315  538 GLU A CB  
4029 C CG  . GLU A 538 ? 0.2488 0.2376 0.2060 0.0269  0.0163  0.0324  538 GLU A CG  
4030 C CD  . GLU A 538 ? 0.2949 0.2915 0.2560 0.0239  0.0148  0.0301  538 GLU A CD  
4031 O OE1 . GLU A 538 ? 0.2783 0.2754 0.2318 0.0233  0.0135  0.0295  538 GLU A OE1 
4032 O OE2 . GLU A 538 ? 0.3432 0.3450 0.3147 0.0220  0.0145  0.0288  538 GLU A OE2 
4033 N N   . ASP A 539 ? 0.1814 0.1660 0.1349 0.0309  0.0101  0.0290  539 ASP A N   
4034 C CA  . ASP A 539 ? 0.1793 0.1638 0.1422 0.0322  0.0100  0.0277  539 ASP A CA  
4035 C C   . ASP A 539 ? 0.2182 0.1958 0.1774 0.0369  0.0099  0.0321  539 ASP A C   
4036 O O   . ASP A 539 ? 0.2153 0.1897 0.1820 0.0389  0.0106  0.0325  539 ASP A O   
4037 C CB  . ASP A 539 ? 0.2096 0.2027 0.1773 0.0310  0.0070  0.0215  539 ASP A CB  
4038 C CG  . ASP A 539 ? 0.1843 0.1834 0.1572 0.0273  0.0074  0.0168  539 ASP A CG  
4039 O OD1 . ASP A 539 ? 0.2175 0.2146 0.1939 0.0254  0.0091  0.0176  539 ASP A OD1 
4040 O OD2 . ASP A 539 ? 0.1873 0.1944 0.1610 0.0262  0.0060  0.0124  539 ASP A OD2 
4041 N N   . TYR A 540 ? 0.2149 0.1895 0.1621 0.0390  0.0084  0.0350  540 TYR A N   
4042 C CA  . TYR A 540 ? 0.2165 0.1845 0.1579 0.0441  0.0079  0.0399  540 TYR A CA  
4043 C C   . TYR A 540 ? 0.2475 0.2098 0.1723 0.0460  0.0075  0.0431  540 TYR A C   
4044 O O   . TYR A 540 ? 0.2612 0.2252 0.1782 0.0463  0.0019  0.0414  540 TYR A O   
4045 C CB  . TYR A 540 ? 0.2252 0.1988 0.1710 0.0462  0.0027  0.0375  540 TYR A CB  
4046 C CG  . TYR A 540 ? 0.2367 0.2042 0.1800 0.0523  0.0019  0.0429  540 TYR A CG  
4047 C CD1 . TYR A 540 ? 0.2373 0.1959 0.1845 0.0547  0.0068  0.0478  540 TYR A CD1 
4048 C CD2 . TYR A 540 ? 0.2400 0.2112 0.1782 0.0556  -0.0042 0.0435  540 TYR A CD2 
4049 C CE1 . TYR A 540 ? 0.2460 0.1979 0.1902 0.0608  0.0063  0.0540  540 TYR A CE1 
4050 C CE2 . TYR A 540 ? 0.2754 0.2415 0.2107 0.0621  -0.0056 0.0493  540 TYR A CE2 
4051 C CZ  . TYR A 540 ? 0.2551 0.2109 0.1929 0.0650  0.0000  0.0547  540 TYR A CZ  
4052 O OH  . TYR A 540 ? 0.2862 0.2357 0.2205 0.0719  -0.0011 0.0615  540 TYR A OH  
4053 N N   . ASP A 541 ? 0.2247 0.1800 0.1441 0.0477  0.0133  0.0479  541 ASP A N   
4054 C CA  . ASP A 541 ? 0.2325 0.1868 0.1624 0.0467  0.0197  0.0511  541 ASP A CA  
4055 C C   . ASP A 541 ? 0.2406 0.1933 0.1643 0.0466  0.0244  0.0530  541 ASP A C   
4056 O O   . ASP A 541 ? 0.2337 0.1820 0.1557 0.0493  0.0309  0.0594  541 ASP A O   
4057 C CB  . ASP A 541 ? 0.2476 0.1947 0.1778 0.0508  0.0231  0.0582  541 ASP A CB  
4058 C CG  . ASP A 541 ? 0.2699 0.2162 0.2147 0.0483  0.0290  0.0615  541 ASP A CG  
4059 O OD1 . ASP A 541 ? 0.3277 0.2799 0.2856 0.0435  0.0276  0.0563  541 ASP A OD1 
4060 O OD2 . ASP A 541 ? 0.3138 0.2538 0.2569 0.0510  0.0347  0.0696  541 ASP A OD2 
4061 N N   . MET A 542 ? 0.2265 0.1823 0.1459 0.0442  0.0217  0.0482  542 MET A N   
4062 C CA  . MET A 542 ? 0.2348 0.1857 0.1424 0.0464  0.0251  0.0498  542 MET A CA  
4063 C C   . MET A 542 ? 0.2133 0.1697 0.1320 0.0445  0.0297  0.0508  542 MET A C   
4064 O O   . MET A 542 ? 0.2279 0.1866 0.1458 0.0427  0.0285  0.0479  542 MET A O   
4065 C CB  . MET A 542 ? 0.2839 0.2315 0.1781 0.0455  0.0192  0.0451  542 MET A CB  
4066 C CG  . MET A 542 ? 0.2981 0.2363 0.1759 0.0488  0.0217  0.0456  542 MET A CG  
4067 S SD  . MET A 542 ? 0.2756 0.2087 0.1402 0.0455  0.0131  0.0390  542 MET A SD  
4068 C CE  . MET A 542 ? 0.3609 0.2781 0.1997 0.0521  0.0145  0.0399  542 MET A CE  
4069 N N   . MET A 543 ? 0.2230 0.1817 0.1533 0.0446  0.0345  0.0555  543 MET A N   
4070 C CA  . MET A 543 ? 0.2194 0.1856 0.1642 0.0423  0.0381  0.0571  543 MET A CA  
4071 C C   . MET A 543 ? 0.2167 0.1817 0.1676 0.0446  0.0457  0.0652  543 MET A C   
4072 O O   . MET A 543 ? 0.2330 0.1935 0.1851 0.0451  0.0466  0.0682  543 MET A O   
4073 C CB  . MET A 543 ? 0.2238 0.1976 0.1840 0.0363  0.0332  0.0521  543 MET A CB  
4074 C CG  . MET A 543 ? 0.2156 0.1984 0.1916 0.0330  0.0347  0.0530  543 MET A CG  
4075 S SD  . MET A 543 ? 0.2530 0.2444 0.2399 0.0266  0.0274  0.0447  543 MET A SD  
4076 C CE  . MET A 543 ? 0.2477 0.2342 0.2435 0.0245  0.0264  0.0433  543 MET A CE  
4077 N N   . ARG A 544 ? 0.2197 0.1894 0.1758 0.0461  0.0516  0.0693  544 ARG A N   
4078 C CA  . ARG A 544 ? 0.2228 0.1936 0.1862 0.0481  0.0602  0.0782  544 ARG A CA  
4079 C C   . ARG A 544 ? 0.2155 0.1991 0.1999 0.0445  0.0624  0.0803  544 ARG A C   
4080 O O   . ARG A 544 ? 0.2159 0.2059 0.2027 0.0437  0.0590  0.0762  544 ARG A O   
4081 C CB  . ARG A 544 ? 0.2596 0.2233 0.2043 0.0565  0.0675  0.0830  544 ARG A CB  
4082 C CG  . ARG A 544 ? 0.2545 0.2059 0.1785 0.0603  0.0655  0.0825  544 ARG A CG  
4083 C CD  . ARG A 544 ? 0.2830 0.2314 0.2112 0.0606  0.0694  0.0897  544 ARG A CD  
4084 N NE  . ARG A 544 ? 0.2652 0.2160 0.1962 0.0643  0.0797  0.0973  544 ARG A NE  
4085 C CZ  . ARG A 544 ? 0.2645 0.2183 0.2108 0.0619  0.0853  0.1050  544 ARG A CZ  
4086 N NH1 . ARG A 544 ? 0.2994 0.2514 0.2578 0.0564  0.0821  0.1068  544 ARG A NH1 
4087 N NH2 . ARG A 544 ? 0.2970 0.2555 0.2475 0.0651  0.0941  0.1107  544 ARG A NH2 
4088 N N   . PRO A 545 ? 0.2157 0.2037 0.2164 0.0420  0.0675  0.0870  545 PRO A N   
4089 C CA  . PRO A 545 ? 0.2160 0.2181 0.2385 0.0384  0.0694  0.0898  545 PRO A CA  
4090 C C   . PRO A 545 ? 0.2286 0.2362 0.2472 0.0456  0.0769  0.0949  545 PRO A C   
4091 O O   . PRO A 545 ? 0.2589 0.2584 0.2604 0.0532  0.0839  0.0989  545 PRO A O   
4092 C CB  . PRO A 545 ? 0.2292 0.2326 0.2689 0.0340  0.0743  0.0971  545 PRO A CB  
4093 C CG  . PRO A 545 ? 0.3131 0.3022 0.3364 0.0381  0.0777  0.1005  545 PRO A CG  
4094 C CD  . PRO A 545 ? 0.2559 0.2359 0.2562 0.0422  0.0716  0.0929  545 PRO A CD  
4095 N N   . MET A 546 ? 0.2192 0.2403 0.2529 0.0437  0.0749  0.0943  546 MET A N   
4096 C CA  . MET A 546 ? 0.2327 0.2632 0.2710 0.0501  0.0824  0.1003  546 MET A CA  
4097 C C   . MET A 546 ? 0.2212 0.2701 0.2897 0.0444  0.0832  0.1055  546 MET A C   
4098 O O   . MET A 546 ? 0.2146 0.2734 0.2959 0.0389  0.0746  0.1008  546 MET A O   
4099 C CB  . MET A 546 ? 0.2336 0.2637 0.2612 0.0542  0.0777  0.0948  546 MET A CB  
4100 C CG  . MET A 546 ? 0.2145 0.2478 0.2384 0.0644  0.0867  0.1005  546 MET A CG  
4101 S SD  . MET A 546 ? 0.2477 0.2756 0.2565 0.0696  0.0813  0.0944  546 MET A SD  
4102 C CE  . MET A 546 ? 0.2439 0.2885 0.2745 0.0607  0.0699  0.0909  546 MET A CE  
4103 N N   . ARG A 547 ? 0.2261 0.2807 0.3062 0.0458  0.0935  0.1154  547 ARG A N   
4104 C CA  . ARG A 547 ? 0.2246 0.2984 0.3363 0.0396  0.0947  0.1213  547 ARG A CA  
4105 C C   . ARG A 547 ? 0.2362 0.3246 0.3551 0.0478  0.1017  0.1273  547 ARG A C   
4106 O O   . ARG A 547 ? 0.2573 0.3454 0.3708 0.0563  0.1143  0.1354  547 ARG A O   
4107 C CB  . ARG A 547 ? 0.2541 0.3271 0.3780 0.0352  0.1023  0.1299  547 ARG A CB  
4108 C CG  . ARG A 547 ? 0.2554 0.3477 0.4145 0.0260  0.1017  0.1351  547 ARG A CG  
4109 C CD  . ARG A 547 ? 0.3297 0.4213 0.5012 0.0227  0.1121  0.1463  547 ARG A CD  
4110 N NE  . ARG A 547 ? 0.4145 0.4880 0.5783 0.0164  0.1074  0.1425  547 ARG A NE  
4111 C CZ  . ARG A 547 ? 0.3957 0.4597 0.5582 0.0158  0.1158  0.1510  547 ARG A CZ  
4112 N NH1 . ARG A 547 ? 0.4413 0.5099 0.6050 0.0216  0.1247  0.1583  547 ARG A NH1 
4113 N NH2 . ARG A 547 ? 0.4442 0.4910 0.5992 0.0111  0.1106  0.1471  547 ARG A NH2 
4114 N N   . VAL A 548 ? 0.2089 0.3105 0.3398 0.0462  0.0938  0.1237  548 VAL A N   
4115 C CA  . VAL A 548 ? 0.2239 0.3409 0.3645 0.0546  0.0996  0.1298  548 VAL A CA  
4116 C C   . VAL A 548 ? 0.2191 0.3591 0.3949 0.0492  0.1039  0.1392  548 VAL A C   
4117 O O   . VAL A 548 ? 0.2189 0.3684 0.4156 0.0374  0.0945  0.1368  548 VAL A O   
4118 C CB  . VAL A 548 ? 0.1920 0.3129 0.3292 0.0559  0.0888  0.1229  548 VAL A CB  
4119 C CG1 . VAL A 548 ? 0.2277 0.3645 0.3759 0.0657  0.0946  0.1297  548 VAL A CG1 
4120 C CG2 . VAL A 548 ? 0.2244 0.3226 0.3288 0.0598  0.0851  0.1143  548 VAL A CG2 
4121 N N   . VAL A 549 ? 0.2375 0.3842 0.4180 0.0574  0.1169  0.1489  549 VAL A N   
4122 C CA  . VAL A 549 ? 0.2501 0.4118 0.4579 0.0517  0.1194  0.1564  549 VAL A CA  
4123 C C   . VAL A 549 ? 0.2586 0.4375 0.4791 0.0590  0.1214  0.1611  549 VAL A C   
4124 O O   . VAL A 549 ? 0.2624 0.4363 0.4654 0.0711  0.1246  0.1600  549 VAL A O   
4125 C CB  . VAL A 549 ? 0.3217 0.4709 0.5208 0.0529  0.1293  0.1621  549 VAL A CB  
4126 C CG1 . VAL A 549 ? 0.2504 0.3824 0.4380 0.0456  0.1265  0.1580  549 VAL A CG1 
4127 C CG2 . VAL A 549 ? 0.3404 0.4776 0.5129 0.0683  0.1392  0.1639  549 VAL A CG2 
4128 N N   . GLU A 550 ? 0.2896 0.4882 0.5409 0.0513  0.1193  0.1663  550 GLU A N   
4129 C CA  . GLU A 550 ? 0.3808 0.5980 0.6474 0.0573  0.1210  0.1716  550 GLU A CA  
4130 C C   . GLU A 550 ? 0.3606 0.5728 0.6181 0.0678  0.1355  0.1795  550 GLU A C   
4131 O O   . GLU A 550 ? 0.4181 0.6213 0.6721 0.0651  0.1422  0.1830  550 GLU A O   
4132 C CB  . GLU A 550 ? 0.3701 0.6108 0.6732 0.0446  0.1128  0.1739  550 GLU A CB  
4133 C CG  . GLU A 550 ? 0.3960 0.6468 0.7090 0.0375  0.0971  0.1661  550 GLU A CG  
4134 C CD  . GLU A 550 ? 0.4742 0.7382 0.7888 0.0469  0.0934  0.1664  550 GLU A CD  
4135 O OE1 . GLU A 550 ? 0.5455 0.8064 0.8487 0.0603  0.1037  0.1714  550 GLU A OE1 
4136 O OE2 . GLU A 550 ? 0.4192 0.6950 0.7446 0.0413  0.0797  0.1613  550 GLU A OE2 
# 
