data_8ZK6
# 
_entry.id   8ZK6 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   8ZK6         pdb_00008zk6 10.2210/pdb8zk6/pdb 
WWPDB D_1300047933 ?            ?                   
# 
_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       2025-05-21 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8ZK6 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-15 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              zhanghb@qibebt.ac.cn 
_pdbx_contact_author.name_first         Haibo 
_pdbx_contact_author.name_last          Zhang 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-3728-9840 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Dong, S.'  1 0000-0002-0452-5221 
'Liu, L.'   2 0000-0002-9684-4325 
'Zhang, H.' 3 0000-0003-3728-9840 
# 
_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                     'Crystal structure of the Decarboxylase KDC4427 from Enterobacter sp. CGMCC 5087' 
_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 'Dong, S.'  1 0000-0002-0452-5221 
primary 'Liu, L.'   2 0000-0002-9684-4325 
primary 'Zhang, H.' 3 0000-0003-3728-9840 
# 
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 'Indolepyruvate decarboxylase' 61957.320 2   ? ? ? ? 
2 non-polymer syn 'THIAMINE DIPHOSPHATE'         425.314   2   ? ? ? ? 
3 non-polymer syn 'MAGNESIUM ION'                24.305    2   ? ? ? ? 
4 water       nat water                          18.015    898 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        KDC4427 
# 
_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       
;MGSSHHHHHHSQDPMRTPYCVADYLLDRLTDCGADHLFGVPGDYNLQFLDHVIDSPDICWVGCANELNASYAADGYARCK
GFAALLTTFGVGELSAMNGIAGSYAEHVPVLHIVGAPGTASQQRGELLHHTLGDGEFRHFYHMSEPITVAQAILTEQNAC
YEIDRVLTTMLRERRPGYLMLPADVAKKAATPPVNALTLRHAHADSACLKAFRDAAENRLAMSKRTALLADFLVLRHGLK
HALQKWVKDVPMAHATMLMGKGIFDERHVGFYGTYSGSASAGAVKEAIEGADTVLCIGTRFTDTLTAGFTHQLTPSQTIE
VQPHASRVGDVWFTGIPMLQAIETLVELCKQHVHDTPVPSSQSAMVYPQPDGSLTQDNFWKTLQTFIRPGDIILADQGTS
AFGAIDLRLPADVNFIVQPLWGSIGYTLAAAFGAQTACPNRRVIVLTGDGAAQLTIQELGSMLRDKQHPIILVLNNEGYT
VERAIHGPEQRYNDIALWNWTQIPQALSLDPQAQCWRVSEAEQLADVLEKVAHHERLSLIEVMLPKADIPPLLGAITKAL
EARNSA
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGSSHHHHHHSQDPMRTPYCVADYLLDRLTDCGADHLFGVPGDYNLQFLDHVIDSPDICWVGCANELNASYAADGYARCK
GFAALLTTFGVGELSAMNGIAGSYAEHVPVLHIVGAPGTASQQRGELLHHTLGDGEFRHFYHMSEPITVAQAILTEQNAC
YEIDRVLTTMLRERRPGYLMLPADVAKKAATPPVNALTLRHAHADSACLKAFRDAAENRLAMSKRTALLADFLVLRHGLK
HALQKWVKDVPMAHATMLMGKGIFDERHVGFYGTYSGSASAGAVKEAIEGADTVLCIGTRFTDTLTAGFTHQLTPSQTIE
VQPHASRVGDVWFTGIPMLQAIETLVELCKQHVHDTPVPSSQSAMVYPQPDGSLTQDNFWKTLQTFIRPGDIILADQGTS
AFGAIDLRLPADVNFIVQPLWGSIGYTLAAAFGAQTACPNRRVIVLTGDGAAQLTIQELGSMLRDKQHPIILVLNNEGYT
VERAIHGPEQRYNDIALWNWTQIPQALSLDPQAQCWRVSEAEQLADVLEKVAHHERLSLIEVMLPKADIPPLLGAITKAL
EARNSA
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'THIAMINE DIPHOSPHATE' TPP 
3 'MAGNESIUM ION'        MG  
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  GLN n 
1 13  ASP n 
1 14  PRO n 
1 15  MET n 
1 16  ARG n 
1 17  THR n 
1 18  PRO n 
1 19  TYR n 
1 20  CYS n 
1 21  VAL n 
1 22  ALA n 
1 23  ASP n 
1 24  TYR n 
1 25  LEU n 
1 26  LEU n 
1 27  ASP n 
1 28  ARG n 
1 29  LEU n 
1 30  THR n 
1 31  ASP n 
1 32  CYS n 
1 33  GLY n 
1 34  ALA n 
1 35  ASP n 
1 36  HIS n 
1 37  LEU n 
1 38  PHE n 
1 39  GLY n 
1 40  VAL n 
1 41  PRO n 
1 42  GLY n 
1 43  ASP n 
1 44  TYR n 
1 45  ASN n 
1 46  LEU n 
1 47  GLN n 
1 48  PHE n 
1 49  LEU n 
1 50  ASP n 
1 51  HIS n 
1 52  VAL n 
1 53  ILE n 
1 54  ASP n 
1 55  SER n 
1 56  PRO n 
1 57  ASP n 
1 58  ILE n 
1 59  CYS n 
1 60  TRP n 
1 61  VAL n 
1 62  GLY n 
1 63  CYS n 
1 64  ALA n 
1 65  ASN n 
1 66  GLU n 
1 67  LEU n 
1 68  ASN n 
1 69  ALA n 
1 70  SER n 
1 71  TYR n 
1 72  ALA n 
1 73  ALA n 
1 74  ASP n 
1 75  GLY n 
1 76  TYR n 
1 77  ALA n 
1 78  ARG n 
1 79  CYS n 
1 80  LYS n 
1 81  GLY n 
1 82  PHE n 
1 83  ALA n 
1 84  ALA n 
1 85  LEU n 
1 86  LEU n 
1 87  THR n 
1 88  THR n 
1 89  PHE n 
1 90  GLY n 
1 91  VAL n 
1 92  GLY n 
1 93  GLU n 
1 94  LEU n 
1 95  SER n 
1 96  ALA n 
1 97  MET n 
1 98  ASN n 
1 99  GLY n 
1 100 ILE n 
1 101 ALA n 
1 102 GLY n 
1 103 SER n 
1 104 TYR n 
1 105 ALA n 
1 106 GLU n 
1 107 HIS n 
1 108 VAL n 
1 109 PRO n 
1 110 VAL n 
1 111 LEU n 
1 112 HIS n 
1 113 ILE n 
1 114 VAL n 
1 115 GLY n 
1 116 ALA n 
1 117 PRO n 
1 118 GLY n 
1 119 THR n 
1 120 ALA n 
1 121 SER n 
1 122 GLN n 
1 123 GLN n 
1 124 ARG n 
1 125 GLY n 
1 126 GLU n 
1 127 LEU n 
1 128 LEU n 
1 129 HIS n 
1 130 HIS n 
1 131 THR n 
1 132 LEU n 
1 133 GLY n 
1 134 ASP n 
1 135 GLY n 
1 136 GLU n 
1 137 PHE n 
1 138 ARG n 
1 139 HIS n 
1 140 PHE n 
1 141 TYR n 
1 142 HIS n 
1 143 MET n 
1 144 SER n 
1 145 GLU n 
1 146 PRO n 
1 147 ILE n 
1 148 THR n 
1 149 VAL n 
1 150 ALA n 
1 151 GLN n 
1 152 ALA n 
1 153 ILE n 
1 154 LEU n 
1 155 THR n 
1 156 GLU n 
1 157 GLN n 
1 158 ASN n 
1 159 ALA n 
1 160 CYS n 
1 161 TYR n 
1 162 GLU n 
1 163 ILE n 
1 164 ASP n 
1 165 ARG n 
1 166 VAL n 
1 167 LEU n 
1 168 THR n 
1 169 THR n 
1 170 MET n 
1 171 LEU n 
1 172 ARG n 
1 173 GLU n 
1 174 ARG n 
1 175 ARG n 
1 176 PRO n 
1 177 GLY n 
1 178 TYR n 
1 179 LEU n 
1 180 MET n 
1 181 LEU n 
1 182 PRO n 
1 183 ALA n 
1 184 ASP n 
1 185 VAL n 
1 186 ALA n 
1 187 LYS n 
1 188 LYS n 
1 189 ALA n 
1 190 ALA n 
1 191 THR n 
1 192 PRO n 
1 193 PRO n 
1 194 VAL n 
1 195 ASN n 
1 196 ALA n 
1 197 LEU n 
1 198 THR n 
1 199 LEU n 
1 200 ARG n 
1 201 HIS n 
1 202 ALA n 
1 203 HIS n 
1 204 ALA n 
1 205 ASP n 
1 206 SER n 
1 207 ALA n 
1 208 CYS n 
1 209 LEU n 
1 210 LYS n 
1 211 ALA n 
1 212 PHE n 
1 213 ARG n 
1 214 ASP n 
1 215 ALA n 
1 216 ALA n 
1 217 GLU n 
1 218 ASN n 
1 219 ARG n 
1 220 LEU n 
1 221 ALA n 
1 222 MET n 
1 223 SER n 
1 224 LYS n 
1 225 ARG n 
1 226 THR n 
1 227 ALA n 
1 228 LEU n 
1 229 LEU n 
1 230 ALA n 
1 231 ASP n 
1 232 PHE n 
1 233 LEU n 
1 234 VAL n 
1 235 LEU n 
1 236 ARG n 
1 237 HIS n 
1 238 GLY n 
1 239 LEU n 
1 240 LYS n 
1 241 HIS n 
1 242 ALA n 
1 243 LEU n 
1 244 GLN n 
1 245 LYS n 
1 246 TRP n 
1 247 VAL n 
1 248 LYS n 
1 249 ASP n 
1 250 VAL n 
1 251 PRO n 
1 252 MET n 
1 253 ALA n 
1 254 HIS n 
1 255 ALA n 
1 256 THR n 
1 257 MET n 
1 258 LEU n 
1 259 MET n 
1 260 GLY n 
1 261 LYS n 
1 262 GLY n 
1 263 ILE n 
1 264 PHE n 
1 265 ASP n 
1 266 GLU n 
1 267 ARG n 
1 268 HIS n 
1 269 VAL n 
1 270 GLY n 
1 271 PHE n 
1 272 TYR n 
1 273 GLY n 
1 274 THR n 
1 275 TYR n 
1 276 SER n 
1 277 GLY n 
1 278 SER n 
1 279 ALA n 
1 280 SER n 
1 281 ALA n 
1 282 GLY n 
1 283 ALA n 
1 284 VAL n 
1 285 LYS n 
1 286 GLU n 
1 287 ALA n 
1 288 ILE n 
1 289 GLU n 
1 290 GLY n 
1 291 ALA n 
1 292 ASP n 
1 293 THR n 
1 294 VAL n 
1 295 LEU n 
1 296 CYS n 
1 297 ILE n 
1 298 GLY n 
1 299 THR n 
1 300 ARG n 
1 301 PHE n 
1 302 THR n 
1 303 ASP n 
1 304 THR n 
1 305 LEU n 
1 306 THR n 
1 307 ALA n 
1 308 GLY n 
1 309 PHE n 
1 310 THR n 
1 311 HIS n 
1 312 GLN n 
1 313 LEU n 
1 314 THR n 
1 315 PRO n 
1 316 SER n 
1 317 GLN n 
1 318 THR n 
1 319 ILE n 
1 320 GLU n 
1 321 VAL n 
1 322 GLN n 
1 323 PRO n 
1 324 HIS n 
1 325 ALA n 
1 326 SER n 
1 327 ARG n 
1 328 VAL n 
1 329 GLY n 
1 330 ASP n 
1 331 VAL n 
1 332 TRP n 
1 333 PHE n 
1 334 THR n 
1 335 GLY n 
1 336 ILE n 
1 337 PRO n 
1 338 MET n 
1 339 LEU n 
1 340 GLN n 
1 341 ALA n 
1 342 ILE n 
1 343 GLU n 
1 344 THR n 
1 345 LEU n 
1 346 VAL n 
1 347 GLU n 
1 348 LEU n 
1 349 CYS n 
1 350 LYS n 
1 351 GLN n 
1 352 HIS n 
1 353 VAL n 
1 354 HIS n 
1 355 ASP n 
1 356 THR n 
1 357 PRO n 
1 358 VAL n 
1 359 PRO n 
1 360 SER n 
1 361 SER n 
1 362 GLN n 
1 363 SER n 
1 364 ALA n 
1 365 MET n 
1 366 VAL n 
1 367 TYR n 
1 368 PRO n 
1 369 GLN n 
1 370 PRO n 
1 371 ASP n 
1 372 GLY n 
1 373 SER n 
1 374 LEU n 
1 375 THR n 
1 376 GLN n 
1 377 ASP n 
1 378 ASN n 
1 379 PHE n 
1 380 TRP n 
1 381 LYS n 
1 382 THR n 
1 383 LEU n 
1 384 GLN n 
1 385 THR n 
1 386 PHE n 
1 387 ILE n 
1 388 ARG n 
1 389 PRO n 
1 390 GLY n 
1 391 ASP n 
1 392 ILE n 
1 393 ILE n 
1 394 LEU n 
1 395 ALA n 
1 396 ASP n 
1 397 GLN n 
1 398 GLY n 
1 399 THR n 
1 400 SER n 
1 401 ALA n 
1 402 PHE n 
1 403 GLY n 
1 404 ALA n 
1 405 ILE n 
1 406 ASP n 
1 407 LEU n 
1 408 ARG n 
1 409 LEU n 
1 410 PRO n 
1 411 ALA n 
1 412 ASP n 
1 413 VAL n 
1 414 ASN n 
1 415 PHE n 
1 416 ILE n 
1 417 VAL n 
1 418 GLN n 
1 419 PRO n 
1 420 LEU n 
1 421 TRP n 
1 422 GLY n 
1 423 SER n 
1 424 ILE n 
1 425 GLY n 
1 426 TYR n 
1 427 THR n 
1 428 LEU n 
1 429 ALA n 
1 430 ALA n 
1 431 ALA n 
1 432 PHE n 
1 433 GLY n 
1 434 ALA n 
1 435 GLN n 
1 436 THR n 
1 437 ALA n 
1 438 CYS n 
1 439 PRO n 
1 440 ASN n 
1 441 ARG n 
1 442 ARG n 
1 443 VAL n 
1 444 ILE n 
1 445 VAL n 
1 446 LEU n 
1 447 THR n 
1 448 GLY n 
1 449 ASP n 
1 450 GLY n 
1 451 ALA n 
1 452 ALA n 
1 453 GLN n 
1 454 LEU n 
1 455 THR n 
1 456 ILE n 
1 457 GLN n 
1 458 GLU n 
1 459 LEU n 
1 460 GLY n 
1 461 SER n 
1 462 MET n 
1 463 LEU n 
1 464 ARG n 
1 465 ASP n 
1 466 LYS n 
1 467 GLN n 
1 468 HIS n 
1 469 PRO n 
1 470 ILE n 
1 471 ILE n 
1 472 LEU n 
1 473 VAL n 
1 474 LEU n 
1 475 ASN n 
1 476 ASN n 
1 477 GLU n 
1 478 GLY n 
1 479 TYR n 
1 480 THR n 
1 481 VAL n 
1 482 GLU n 
1 483 ARG n 
1 484 ALA n 
1 485 ILE n 
1 486 HIS n 
1 487 GLY n 
1 488 PRO n 
1 489 GLU n 
1 490 GLN n 
1 491 ARG n 
1 492 TYR n 
1 493 ASN n 
1 494 ASP n 
1 495 ILE n 
1 496 ALA n 
1 497 LEU n 
1 498 TRP n 
1 499 ASN n 
1 500 TRP n 
1 501 THR n 
1 502 GLN n 
1 503 ILE n 
1 504 PRO n 
1 505 GLN n 
1 506 ALA n 
1 507 LEU n 
1 508 SER n 
1 509 LEU n 
1 510 ASP n 
1 511 PRO n 
1 512 GLN n 
1 513 ALA n 
1 514 GLN n 
1 515 CYS n 
1 516 TRP n 
1 517 ARG n 
1 518 VAL n 
1 519 SER n 
1 520 GLU n 
1 521 ALA n 
1 522 GLU n 
1 523 GLN n 
1 524 LEU n 
1 525 ALA n 
1 526 ASP n 
1 527 VAL n 
1 528 LEU n 
1 529 GLU n 
1 530 LYS n 
1 531 VAL n 
1 532 ALA n 
1 533 HIS n 
1 534 HIS n 
1 535 GLU n 
1 536 ARG n 
1 537 LEU n 
1 538 SER n 
1 539 LEU n 
1 540 ILE n 
1 541 GLU n 
1 542 VAL n 
1 543 MET n 
1 544 LEU n 
1 545 PRO n 
1 546 LYS n 
1 547 ALA n 
1 548 ASP n 
1 549 ILE n 
1 550 PRO n 
1 551 PRO n 
1 552 LEU n 
1 553 LEU n 
1 554 GLY n 
1 555 ALA n 
1 556 ILE n 
1 557 THR n 
1 558 LYS n 
1 559 ALA n 
1 560 LEU n 
1 561 GLU n 
1 562 ALA n 
1 563 ARG n 
1 564 ASN n 
1 565 SER n 
1 566 ALA 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                   566 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'ipdC, DEO48_12930' 
_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      'Enterobacter sp. CGMCC 5087' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2183878 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                ? 'C3 H7 N O2'           89.093  
ARG 'L-peptide linking' y ARGININE               ? 'C6 H15 N4 O2 1'       175.209 
ASN 'L-peptide linking' y ASPARAGINE             ? 'C4 H8 N2 O3'          132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'        ? 'C4 H7 N O4'           133.103 
CYS 'L-peptide linking' y CYSTEINE               ? 'C3 H7 N O2 S'         121.158 
GLN 'L-peptide linking' y GLUTAMINE              ? 'C5 H10 N2 O3'         146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'        ? 'C5 H9 N O4'           147.129 
GLY 'peptide linking'   y GLYCINE                ? 'C2 H5 N O2'           75.067  
HIS 'L-peptide linking' y HISTIDINE              ? 'C6 H10 N3 O2 1'       156.162 
HOH non-polymer         . WATER                  ? 'H2 O'                 18.015  
ILE 'L-peptide linking' y ISOLEUCINE             ? 'C6 H13 N O2'          131.173 
LEU 'L-peptide linking' y LEUCINE                ? 'C6 H13 N O2'          131.173 
LYS 'L-peptide linking' y LYSINE                 ? 'C6 H15 N2 O2 1'       147.195 
MET 'L-peptide linking' y METHIONINE             ? 'C5 H11 N O2 S'        149.211 
MG  non-polymer         . 'MAGNESIUM ION'        ? 'Mg 2'                 24.305  
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 
TPP non-polymer         . 'THIAMINE DIPHOSPHATE' ? 'C12 H19 N4 O7 P2 S 1' 425.314 
TRP 'L-peptide linking' y TRYPTOPHAN             ? 'C11 H12 N2 O2'        204.225 
TYR 'L-peptide linking' y TYROSINE               ? 'C9 H11 N O3'          181.189 
VAL 'L-peptide linking' y VALINE                 ? 'C5 H11 N O2'          117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   -13 ?   ?   ?   A . n 
A 1 2   GLY 2   -12 ?   ?   ?   A . n 
A 1 3   SER 3   -11 ?   ?   ?   A . n 
A 1 4   SER 4   -10 ?   ?   ?   A . n 
A 1 5   HIS 5   -9  ?   ?   ?   A . n 
A 1 6   HIS 6   -8  ?   ?   ?   A . n 
A 1 7   HIS 7   -7  ?   ?   ?   A . n 
A 1 8   HIS 8   -6  ?   ?   ?   A . n 
A 1 9   HIS 9   -5  ?   ?   ?   A . n 
A 1 10  HIS 10  -4  ?   ?   ?   A . n 
A 1 11  SER 11  -3  ?   ?   ?   A . n 
A 1 12  GLN 12  -2  ?   ?   ?   A . n 
A 1 13  ASP 13  -1  ?   ?   ?   A . n 
A 1 14  PRO 14  0   ?   ?   ?   A . n 
A 1 15  MET 15  1   ?   ?   ?   A . n 
A 1 16  ARG 16  2   ?   ?   ?   A . n 
A 1 17  THR 17  3   3   THR THR A . n 
A 1 18  PRO 18  4   4   PRO PRO A . n 
A 1 19  TYR 19  5   5   TYR TYR A . n 
A 1 20  CYS 20  6   6   CYS CYS A . n 
A 1 21  VAL 21  7   7   VAL VAL A . n 
A 1 22  ALA 22  8   8   ALA ALA A . n 
A 1 23  ASP 23  9   9   ASP ASP A . n 
A 1 24  TYR 24  10  10  TYR TYR A . n 
A 1 25  LEU 25  11  11  LEU LEU A . n 
A 1 26  LEU 26  12  12  LEU LEU A . n 
A 1 27  ASP 27  13  13  ASP ASP A . n 
A 1 28  ARG 28  14  14  ARG ARG A . n 
A 1 29  LEU 29  15  15  LEU LEU A . n 
A 1 30  THR 30  16  16  THR THR A . n 
A 1 31  ASP 31  17  17  ASP ASP A . n 
A 1 32  CYS 32  18  18  CYS CYS A . n 
A 1 33  GLY 33  19  19  GLY GLY A . n 
A 1 34  ALA 34  20  20  ALA ALA A . n 
A 1 35  ASP 35  21  21  ASP ASP A . n 
A 1 36  HIS 36  22  22  HIS HIS A . n 
A 1 37  LEU 37  23  23  LEU LEU A . n 
A 1 38  PHE 38  24  24  PHE PHE A . n 
A 1 39  GLY 39  25  25  GLY GLY A . n 
A 1 40  VAL 40  26  26  VAL VAL A . n 
A 1 41  PRO 41  27  27  PRO PRO A . n 
A 1 42  GLY 42  28  28  GLY GLY A . n 
A 1 43  ASP 43  29  29  ASP ASP A . n 
A 1 44  TYR 44  30  30  TYR TYR A . n 
A 1 45  ASN 45  31  31  ASN ASN A . n 
A 1 46  LEU 46  32  32  LEU LEU A . n 
A 1 47  GLN 47  33  33  GLN GLN A . n 
A 1 48  PHE 48  34  34  PHE PHE A . n 
A 1 49  LEU 49  35  35  LEU LEU A . n 
A 1 50  ASP 50  36  36  ASP ASP A . n 
A 1 51  HIS 51  37  37  HIS HIS A . n 
A 1 52  VAL 52  38  38  VAL VAL A . n 
A 1 53  ILE 53  39  39  ILE ILE A . n 
A 1 54  ASP 54  40  40  ASP ASP A . n 
A 1 55  SER 55  41  41  SER SER A . n 
A 1 56  PRO 56  42  42  PRO PRO A . n 
A 1 57  ASP 57  43  43  ASP ASP A . n 
A 1 58  ILE 58  44  44  ILE ILE A . n 
A 1 59  CYS 59  45  45  CYS CYS A . n 
A 1 60  TRP 60  46  46  TRP TRP A . n 
A 1 61  VAL 61  47  47  VAL VAL A . n 
A 1 62  GLY 62  48  48  GLY GLY A . n 
A 1 63  CYS 63  49  49  CYS CYS A . n 
A 1 64  ALA 64  50  50  ALA ALA A . n 
A 1 65  ASN 65  51  51  ASN ASN A . n 
A 1 66  GLU 66  52  52  GLU GLU A . n 
A 1 67  LEU 67  53  53  LEU LEU A . n 
A 1 68  ASN 68  54  54  ASN ASN A . n 
A 1 69  ALA 69  55  55  ALA ALA A . n 
A 1 70  SER 70  56  56  SER SER A . n 
A 1 71  TYR 71  57  57  TYR TYR A . n 
A 1 72  ALA 72  58  58  ALA ALA A . n 
A 1 73  ALA 73  59  59  ALA ALA A . n 
A 1 74  ASP 74  60  60  ASP ASP A . n 
A 1 75  GLY 75  61  61  GLY GLY A . n 
A 1 76  TYR 76  62  62  TYR TYR A . n 
A 1 77  ALA 77  63  63  ALA ALA A . n 
A 1 78  ARG 78  64  64  ARG ARG A . n 
A 1 79  CYS 79  65  65  CYS CYS A . n 
A 1 80  LYS 80  66  66  LYS LYS A . n 
A 1 81  GLY 81  67  67  GLY GLY A . n 
A 1 82  PHE 82  68  68  PHE PHE A . n 
A 1 83  ALA 83  69  69  ALA ALA A . n 
A 1 84  ALA 84  70  70  ALA ALA A . n 
A 1 85  LEU 85  71  71  LEU LEU A . n 
A 1 86  LEU 86  72  72  LEU LEU A . n 
A 1 87  THR 87  73  73  THR THR A . n 
A 1 88  THR 88  74  74  THR THR A . n 
A 1 89  PHE 89  75  75  PHE PHE A . n 
A 1 90  GLY 90  76  76  GLY GLY A . n 
A 1 91  VAL 91  77  77  VAL VAL A . n 
A 1 92  GLY 92  78  78  GLY GLY A . n 
A 1 93  GLU 93  79  79  GLU GLU A . n 
A 1 94  LEU 94  80  80  LEU LEU A . n 
A 1 95  SER 95  81  81  SER SER A . n 
A 1 96  ALA 96  82  82  ALA ALA A . n 
A 1 97  MET 97  83  83  MET MET A . n 
A 1 98  ASN 98  84  84  ASN ASN A . n 
A 1 99  GLY 99  85  85  GLY GLY A . n 
A 1 100 ILE 100 86  86  ILE ILE A . n 
A 1 101 ALA 101 87  87  ALA ALA A . n 
A 1 102 GLY 102 88  88  GLY GLY A . n 
A 1 103 SER 103 89  89  SER SER A . n 
A 1 104 TYR 104 90  90  TYR TYR A . n 
A 1 105 ALA 105 91  91  ALA ALA A . n 
A 1 106 GLU 106 92  92  GLU GLU A . n 
A 1 107 HIS 107 93  93  HIS HIS A . n 
A 1 108 VAL 108 94  94  VAL VAL A . n 
A 1 109 PRO 109 95  95  PRO PRO A . n 
A 1 110 VAL 110 96  96  VAL VAL A . n 
A 1 111 LEU 111 97  97  LEU LEU A . n 
A 1 112 HIS 112 98  98  HIS HIS A . n 
A 1 113 ILE 113 99  99  ILE ILE A . n 
A 1 114 VAL 114 100 100 VAL VAL A . n 
A 1 115 GLY 115 101 101 GLY GLY A . n 
A 1 116 ALA 116 102 102 ALA ALA A . n 
A 1 117 PRO 117 103 103 PRO PRO A . n 
A 1 118 GLY 118 104 104 GLY GLY A . n 
A 1 119 THR 119 105 105 THR THR A . n 
A 1 120 ALA 120 106 106 ALA ALA A . n 
A 1 121 SER 121 107 107 SER SER A . n 
A 1 122 GLN 122 108 108 GLN GLN A . n 
A 1 123 GLN 123 109 109 GLN GLN A . n 
A 1 124 ARG 124 110 110 ARG ARG A . n 
A 1 125 GLY 125 111 111 GLY GLY A . n 
A 1 126 GLU 126 112 112 GLU GLU A . n 
A 1 127 LEU 127 113 113 LEU LEU A . n 
A 1 128 LEU 128 114 114 LEU LEU A . n 
A 1 129 HIS 129 115 115 HIS HIS A . n 
A 1 130 HIS 130 116 116 HIS HIS A . n 
A 1 131 THR 131 117 117 THR THR A . n 
A 1 132 LEU 132 118 118 LEU LEU A . n 
A 1 133 GLY 133 119 119 GLY GLY A . n 
A 1 134 ASP 134 120 120 ASP ASP A . n 
A 1 135 GLY 135 121 121 GLY GLY A . n 
A 1 136 GLU 136 122 122 GLU GLU A . n 
A 1 137 PHE 137 123 123 PHE PHE A . n 
A 1 138 ARG 138 124 124 ARG ARG A . n 
A 1 139 HIS 139 125 125 HIS HIS A . n 
A 1 140 PHE 140 126 126 PHE PHE A . n 
A 1 141 TYR 141 127 127 TYR TYR A . n 
A 1 142 HIS 142 128 128 HIS HIS A . n 
A 1 143 MET 143 129 129 MET MET A . n 
A 1 144 SER 144 130 130 SER SER A . n 
A 1 145 GLU 145 131 131 GLU GLU A . n 
A 1 146 PRO 146 132 132 PRO PRO A . n 
A 1 147 ILE 147 133 133 ILE ILE A . n 
A 1 148 THR 148 134 134 THR THR A . n 
A 1 149 VAL 149 135 135 VAL VAL A . n 
A 1 150 ALA 150 136 136 ALA ALA A . n 
A 1 151 GLN 151 137 137 GLN GLN A . n 
A 1 152 ALA 152 138 138 ALA ALA A . n 
A 1 153 ILE 153 139 139 ILE ILE A . n 
A 1 154 LEU 154 140 140 LEU LEU A . n 
A 1 155 THR 155 141 141 THR THR A . n 
A 1 156 GLU 156 142 142 GLU GLU A . n 
A 1 157 GLN 157 143 143 GLN GLN A . n 
A 1 158 ASN 158 144 144 ASN ASN A . n 
A 1 159 ALA 159 145 145 ALA ALA A . n 
A 1 160 CYS 160 146 146 CYS CYS A . n 
A 1 161 TYR 161 147 147 TYR TYR A . n 
A 1 162 GLU 162 148 148 GLU GLU A . n 
A 1 163 ILE 163 149 149 ILE ILE A . n 
A 1 164 ASP 164 150 150 ASP ASP A . n 
A 1 165 ARG 165 151 151 ARG ARG A . n 
A 1 166 VAL 166 152 152 VAL VAL A . n 
A 1 167 LEU 167 153 153 LEU LEU A . n 
A 1 168 THR 168 154 154 THR THR A . n 
A 1 169 THR 169 155 155 THR THR A . n 
A 1 170 MET 170 156 156 MET MET A . n 
A 1 171 LEU 171 157 157 LEU LEU A . n 
A 1 172 ARG 172 158 158 ARG ARG A . n 
A 1 173 GLU 173 159 159 GLU GLU A . n 
A 1 174 ARG 174 160 160 ARG ARG A . n 
A 1 175 ARG 175 161 161 ARG ARG A . n 
A 1 176 PRO 176 162 162 PRO PRO A . n 
A 1 177 GLY 177 163 163 GLY GLY A . n 
A 1 178 TYR 178 164 164 TYR TYR A . n 
A 1 179 LEU 179 165 165 LEU LEU A . n 
A 1 180 MET 180 166 166 MET MET A . n 
A 1 181 LEU 181 167 167 LEU LEU A . n 
A 1 182 PRO 182 168 168 PRO PRO A . n 
A 1 183 ALA 183 169 169 ALA ALA A . n 
A 1 184 ASP 184 170 170 ASP ASP A . n 
A 1 185 VAL 185 171 171 VAL VAL A . n 
A 1 186 ALA 186 172 172 ALA ALA A . n 
A 1 187 LYS 187 173 173 LYS LYS A . n 
A 1 188 LYS 188 174 174 LYS LYS A . n 
A 1 189 ALA 189 175 175 ALA ALA A . n 
A 1 190 ALA 190 176 176 ALA ALA A . n 
A 1 191 THR 191 177 177 THR THR A . n 
A 1 192 PRO 192 178 178 PRO PRO A . n 
A 1 193 PRO 193 179 179 PRO PRO A . n 
A 1 194 VAL 194 180 180 VAL VAL A . n 
A 1 195 ASN 195 181 181 ASN ASN A . n 
A 1 196 ALA 196 182 182 ALA ALA A . n 
A 1 197 LEU 197 183 183 LEU LEU A . n 
A 1 198 THR 198 184 184 THR THR A . n 
A 1 199 LEU 199 185 185 LEU LEU A . n 
A 1 200 ARG 200 186 186 ARG ARG A . n 
A 1 201 HIS 201 187 187 HIS HIS A . n 
A 1 202 ALA 202 188 188 ALA ALA A . n 
A 1 203 HIS 203 189 189 HIS HIS A . n 
A 1 204 ALA 204 190 190 ALA ALA A . n 
A 1 205 ASP 205 191 191 ASP ASP A . n 
A 1 206 SER 206 192 192 SER SER A . n 
A 1 207 ALA 207 193 193 ALA ALA A . n 
A 1 208 CYS 208 194 194 CYS CYS A . n 
A 1 209 LEU 209 195 195 LEU LEU A . n 
A 1 210 LYS 210 196 196 LYS LYS A . n 
A 1 211 ALA 211 197 197 ALA ALA A . n 
A 1 212 PHE 212 198 198 PHE PHE A . n 
A 1 213 ARG 213 199 199 ARG ARG A . n 
A 1 214 ASP 214 200 200 ASP ASP A . n 
A 1 215 ALA 215 201 201 ALA ALA A . n 
A 1 216 ALA 216 202 202 ALA ALA A . n 
A 1 217 GLU 217 203 203 GLU GLU A . n 
A 1 218 ASN 218 204 204 ASN ASN A . n 
A 1 219 ARG 219 205 205 ARG ARG A . n 
A 1 220 LEU 220 206 206 LEU LEU A . n 
A 1 221 ALA 221 207 207 ALA ALA A . n 
A 1 222 MET 222 208 208 MET MET A . n 
A 1 223 SER 223 209 209 SER SER A . n 
A 1 224 LYS 224 210 210 LYS LYS A . n 
A 1 225 ARG 225 211 211 ARG ARG A . n 
A 1 226 THR 226 212 212 THR THR A . n 
A 1 227 ALA 227 213 213 ALA ALA A . n 
A 1 228 LEU 228 214 214 LEU LEU A . n 
A 1 229 LEU 229 215 215 LEU LEU A . n 
A 1 230 ALA 230 216 216 ALA ALA A . n 
A 1 231 ASP 231 217 217 ASP ASP A . n 
A 1 232 PHE 232 218 218 PHE PHE A . n 
A 1 233 LEU 233 219 219 LEU LEU A . n 
A 1 234 VAL 234 220 220 VAL VAL A . n 
A 1 235 LEU 235 221 221 LEU LEU A . n 
A 1 236 ARG 236 222 222 ARG ARG A . n 
A 1 237 HIS 237 223 223 HIS HIS A . n 
A 1 238 GLY 238 224 224 GLY GLY A . n 
A 1 239 LEU 239 225 225 LEU LEU A . n 
A 1 240 LYS 240 226 226 LYS LYS A . n 
A 1 241 HIS 241 227 227 HIS HIS A . n 
A 1 242 ALA 242 228 228 ALA ALA A . n 
A 1 243 LEU 243 229 229 LEU LEU A . n 
A 1 244 GLN 244 230 230 GLN GLN A . n 
A 1 245 LYS 245 231 231 LYS LYS A . n 
A 1 246 TRP 246 232 232 TRP TRP A . n 
A 1 247 VAL 247 233 233 VAL VAL A . n 
A 1 248 LYS 248 234 234 LYS LYS A . n 
A 1 249 ASP 249 235 235 ASP ASP A . n 
A 1 250 VAL 250 236 236 VAL VAL A . n 
A 1 251 PRO 251 237 237 PRO PRO A . n 
A 1 252 MET 252 238 238 MET MET A . n 
A 1 253 ALA 253 239 239 ALA ALA A . n 
A 1 254 HIS 254 240 240 HIS HIS A . n 
A 1 255 ALA 255 241 241 ALA ALA A . n 
A 1 256 THR 256 242 242 THR THR A . n 
A 1 257 MET 257 243 243 MET MET A . n 
A 1 258 LEU 258 244 244 LEU LEU A . n 
A 1 259 MET 259 245 245 MET MET A . n 
A 1 260 GLY 260 246 246 GLY GLY A . n 
A 1 261 LYS 261 247 247 LYS LYS A . n 
A 1 262 GLY 262 248 248 GLY GLY A . n 
A 1 263 ILE 263 249 249 ILE ILE A . n 
A 1 264 PHE 264 250 250 PHE PHE A . n 
A 1 265 ASP 265 251 251 ASP ASP A . n 
A 1 266 GLU 266 252 252 GLU GLU A . n 
A 1 267 ARG 267 253 253 ARG ARG A . n 
A 1 268 HIS 268 254 254 HIS HIS A . n 
A 1 269 VAL 269 255 255 VAL VAL A . n 
A 1 270 GLY 270 256 256 GLY GLY A . n 
A 1 271 PHE 271 257 257 PHE PHE A . n 
A 1 272 TYR 272 258 258 TYR TYR A . n 
A 1 273 GLY 273 259 259 GLY GLY A . n 
A 1 274 THR 274 260 260 THR THR A . n 
A 1 275 TYR 275 261 261 TYR TYR A . n 
A 1 276 SER 276 262 262 SER SER A . n 
A 1 277 GLY 277 263 263 GLY GLY A . n 
A 1 278 SER 278 264 264 SER SER A . n 
A 1 279 ALA 279 265 265 ALA ALA A . n 
A 1 280 SER 280 266 266 SER SER A . n 
A 1 281 ALA 281 267 267 ALA ALA A . n 
A 1 282 GLY 282 268 268 GLY GLY A . n 
A 1 283 ALA 283 269 269 ALA ALA A . n 
A 1 284 VAL 284 270 270 VAL VAL A . n 
A 1 285 LYS 285 271 271 LYS LYS A . n 
A 1 286 GLU 286 272 272 GLU GLU A . n 
A 1 287 ALA 287 273 273 ALA ALA A . n 
A 1 288 ILE 288 274 274 ILE ILE A . n 
A 1 289 GLU 289 275 275 GLU GLU A . n 
A 1 290 GLY 290 276 276 GLY GLY A . n 
A 1 291 ALA 291 277 277 ALA ALA A . n 
A 1 292 ASP 292 278 278 ASP ASP A . n 
A 1 293 THR 293 279 279 THR THR A . n 
A 1 294 VAL 294 280 280 VAL VAL A . n 
A 1 295 LEU 295 281 281 LEU LEU A . n 
A 1 296 CYS 296 282 282 CYS CYS A . n 
A 1 297 ILE 297 283 283 ILE ILE A . n 
A 1 298 GLY 298 284 284 GLY GLY A . n 
A 1 299 THR 299 285 285 THR THR A . n 
A 1 300 ARG 300 286 286 ARG ARG A . n 
A 1 301 PHE 301 287 287 PHE PHE A . n 
A 1 302 THR 302 288 288 THR THR A . n 
A 1 303 ASP 303 289 289 ASP ASP A . n 
A 1 304 THR 304 290 290 THR THR A . n 
A 1 305 LEU 305 291 291 LEU LEU A . n 
A 1 306 THR 306 292 292 THR THR A . n 
A 1 307 ALA 307 293 293 ALA ALA A . n 
A 1 308 GLY 308 294 294 GLY GLY A . n 
A 1 309 PHE 309 295 295 PHE PHE A . n 
A 1 310 THR 310 296 296 THR THR A . n 
A 1 311 HIS 311 297 297 HIS HIS A . n 
A 1 312 GLN 312 298 298 GLN GLN A . n 
A 1 313 LEU 313 299 299 LEU LEU A . n 
A 1 314 THR 314 300 300 THR THR A . n 
A 1 315 PRO 315 301 301 PRO PRO A . n 
A 1 316 SER 316 302 302 SER SER A . n 
A 1 317 GLN 317 303 303 GLN GLN A . n 
A 1 318 THR 318 304 304 THR THR A . n 
A 1 319 ILE 319 305 305 ILE ILE A . n 
A 1 320 GLU 320 306 306 GLU GLU A . n 
A 1 321 VAL 321 307 307 VAL VAL A . n 
A 1 322 GLN 322 308 308 GLN GLN A . n 
A 1 323 PRO 323 309 309 PRO PRO A . n 
A 1 324 HIS 324 310 310 HIS HIS A . n 
A 1 325 ALA 325 311 311 ALA ALA A . n 
A 1 326 SER 326 312 312 SER SER A . n 
A 1 327 ARG 327 313 313 ARG ARG A . n 
A 1 328 VAL 328 314 314 VAL VAL A . n 
A 1 329 GLY 329 315 315 GLY GLY A . n 
A 1 330 ASP 330 316 316 ASP ASP A . n 
A 1 331 VAL 331 317 317 VAL VAL A . n 
A 1 332 TRP 332 318 318 TRP TRP A . n 
A 1 333 PHE 333 319 319 PHE PHE A . n 
A 1 334 THR 334 320 320 THR THR A . n 
A 1 335 GLY 335 321 321 GLY GLY A . n 
A 1 336 ILE 336 322 322 ILE ILE A . n 
A 1 337 PRO 337 323 323 PRO PRO A . n 
A 1 338 MET 338 324 324 MET MET A . n 
A 1 339 LEU 339 325 325 LEU LEU A . n 
A 1 340 GLN 340 326 326 GLN GLN A . n 
A 1 341 ALA 341 327 327 ALA ALA A . n 
A 1 342 ILE 342 328 328 ILE ILE A . n 
A 1 343 GLU 343 329 329 GLU GLU A . n 
A 1 344 THR 344 330 330 THR THR A . n 
A 1 345 LEU 345 331 331 LEU LEU A . n 
A 1 346 VAL 346 332 332 VAL VAL A . n 
A 1 347 GLU 347 333 333 GLU GLU A . n 
A 1 348 LEU 348 334 334 LEU LEU A . n 
A 1 349 CYS 349 335 335 CYS CYS A . n 
A 1 350 LYS 350 336 336 LYS LYS A . n 
A 1 351 GLN 351 337 337 GLN GLN A . n 
A 1 352 HIS 352 338 338 HIS HIS A . n 
A 1 353 VAL 353 339 339 VAL VAL A . n 
A 1 354 HIS 354 340 340 HIS HIS A . n 
A 1 355 ASP 355 341 341 ASP ASP A . n 
A 1 356 THR 356 342 342 THR THR A . n 
A 1 357 PRO 357 343 343 PRO PRO A . n 
A 1 358 VAL 358 344 344 VAL VAL A . n 
A 1 359 PRO 359 345 345 PRO PRO A . n 
A 1 360 SER 360 346 ?   ?   ?   A . n 
A 1 361 SER 361 347 ?   ?   ?   A . n 
A 1 362 GLN 362 348 ?   ?   ?   A . n 
A 1 363 SER 363 349 ?   ?   ?   A . n 
A 1 364 ALA 364 350 ?   ?   ?   A . n 
A 1 365 MET 365 351 ?   ?   ?   A . n 
A 1 366 VAL 366 352 ?   ?   ?   A . n 
A 1 367 TYR 367 353 ?   ?   ?   A . n 
A 1 368 PRO 368 354 ?   ?   ?   A . n 
A 1 369 GLN 369 355 ?   ?   ?   A . n 
A 1 370 PRO 370 356 356 PRO PRO A . n 
A 1 371 ASP 371 357 357 ASP ASP A . n 
A 1 372 GLY 372 358 358 GLY GLY A . n 
A 1 373 SER 373 359 359 SER SER A . n 
A 1 374 LEU 374 360 360 LEU LEU A . n 
A 1 375 THR 375 361 361 THR THR A . n 
A 1 376 GLN 376 362 362 GLN GLN A . n 
A 1 377 ASP 377 363 363 ASP ASP A . n 
A 1 378 ASN 378 364 364 ASN ASN A . n 
A 1 379 PHE 379 365 365 PHE PHE A . n 
A 1 380 TRP 380 366 366 TRP TRP A . n 
A 1 381 LYS 381 367 367 LYS LYS A . n 
A 1 382 THR 382 368 368 THR THR A . n 
A 1 383 LEU 383 369 369 LEU LEU A . n 
A 1 384 GLN 384 370 370 GLN GLN A . n 
A 1 385 THR 385 371 371 THR THR A . n 
A 1 386 PHE 386 372 372 PHE PHE A . n 
A 1 387 ILE 387 373 373 ILE ILE A . n 
A 1 388 ARG 388 374 374 ARG ARG A . n 
A 1 389 PRO 389 375 375 PRO PRO A . n 
A 1 390 GLY 390 376 376 GLY GLY A . n 
A 1 391 ASP 391 377 377 ASP ASP A . n 
A 1 392 ILE 392 378 378 ILE ILE A . n 
A 1 393 ILE 393 379 379 ILE ILE A . n 
A 1 394 LEU 394 380 380 LEU LEU A . n 
A 1 395 ALA 395 381 381 ALA ALA A . n 
A 1 396 ASP 396 382 382 ASP ASP A . n 
A 1 397 GLN 397 383 383 GLN GLN A . n 
A 1 398 GLY 398 384 384 GLY GLY A . n 
A 1 399 THR 399 385 385 THR THR A . n 
A 1 400 SER 400 386 386 SER SER A . n 
A 1 401 ALA 401 387 387 ALA ALA A . n 
A 1 402 PHE 402 388 388 PHE PHE A . n 
A 1 403 GLY 403 389 389 GLY GLY A . n 
A 1 404 ALA 404 390 390 ALA ALA A . n 
A 1 405 ILE 405 391 391 ILE ILE A . n 
A 1 406 ASP 406 392 392 ASP ASP A . n 
A 1 407 LEU 407 393 393 LEU LEU A . n 
A 1 408 ARG 408 394 394 ARG ARG A . n 
A 1 409 LEU 409 395 395 LEU LEU A . n 
A 1 410 PRO 410 396 396 PRO PRO A . n 
A 1 411 ALA 411 397 397 ALA ALA A . n 
A 1 412 ASP 412 398 398 ASP ASP A . n 
A 1 413 VAL 413 399 399 VAL VAL A . n 
A 1 414 ASN 414 400 400 ASN ASN A . n 
A 1 415 PHE 415 401 401 PHE PHE A . n 
A 1 416 ILE 416 402 402 ILE ILE A . n 
A 1 417 VAL 417 403 403 VAL VAL A . n 
A 1 418 GLN 418 404 404 GLN GLN A . n 
A 1 419 PRO 419 405 405 PRO PRO A . n 
A 1 420 LEU 420 406 406 LEU LEU A . n 
A 1 421 TRP 421 407 407 TRP TRP A . n 
A 1 422 GLY 422 408 408 GLY GLY A . n 
A 1 423 SER 423 409 409 SER SER A . n 
A 1 424 ILE 424 410 410 ILE ILE A . n 
A 1 425 GLY 425 411 411 GLY GLY A . n 
A 1 426 TYR 426 412 412 TYR TYR A . n 
A 1 427 THR 427 413 413 THR THR A . n 
A 1 428 LEU 428 414 414 LEU LEU A . n 
A 1 429 ALA 429 415 415 ALA ALA A . n 
A 1 430 ALA 430 416 416 ALA ALA A . n 
A 1 431 ALA 431 417 417 ALA ALA A . n 
A 1 432 PHE 432 418 418 PHE PHE A . n 
A 1 433 GLY 433 419 419 GLY GLY A . n 
A 1 434 ALA 434 420 420 ALA ALA A . n 
A 1 435 GLN 435 421 421 GLN GLN A . n 
A 1 436 THR 436 422 422 THR THR A . n 
A 1 437 ALA 437 423 423 ALA ALA A . n 
A 1 438 CYS 438 424 424 CYS CYS A . n 
A 1 439 PRO 439 425 425 PRO PRO A . n 
A 1 440 ASN 440 426 426 ASN ASN A . n 
A 1 441 ARG 441 427 427 ARG ARG A . n 
A 1 442 ARG 442 428 428 ARG ARG A . n 
A 1 443 VAL 443 429 429 VAL VAL A . n 
A 1 444 ILE 444 430 430 ILE ILE A . n 
A 1 445 VAL 445 431 431 VAL VAL A . n 
A 1 446 LEU 446 432 432 LEU LEU A . n 
A 1 447 THR 447 433 433 THR THR A . n 
A 1 448 GLY 448 434 434 GLY GLY A . n 
A 1 449 ASP 449 435 435 ASP ASP A . n 
A 1 450 GLY 450 436 436 GLY GLY A . n 
A 1 451 ALA 451 437 437 ALA ALA A . n 
A 1 452 ALA 452 438 438 ALA ALA A . n 
A 1 453 GLN 453 439 439 GLN GLN A . n 
A 1 454 LEU 454 440 440 LEU LEU A . n 
A 1 455 THR 455 441 441 THR THR A . n 
A 1 456 ILE 456 442 442 ILE ILE A . n 
A 1 457 GLN 457 443 443 GLN GLN A . n 
A 1 458 GLU 458 444 444 GLU GLU A . n 
A 1 459 LEU 459 445 445 LEU LEU A . n 
A 1 460 GLY 460 446 446 GLY GLY A . n 
A 1 461 SER 461 447 447 SER SER A . n 
A 1 462 MET 462 448 448 MET MET A . n 
A 1 463 LEU 463 449 449 LEU LEU A . n 
A 1 464 ARG 464 450 450 ARG ARG A . n 
A 1 465 ASP 465 451 451 ASP ASP A . n 
A 1 466 LYS 466 452 452 LYS LYS A . n 
A 1 467 GLN 467 453 453 GLN GLN A . n 
A 1 468 HIS 468 454 454 HIS HIS A . n 
A 1 469 PRO 469 455 455 PRO PRO A . n 
A 1 470 ILE 470 456 456 ILE ILE A . n 
A 1 471 ILE 471 457 457 ILE ILE A . n 
A 1 472 LEU 472 458 458 LEU LEU A . n 
A 1 473 VAL 473 459 459 VAL VAL A . n 
A 1 474 LEU 474 460 460 LEU LEU A . n 
A 1 475 ASN 475 461 461 ASN ASN A . n 
A 1 476 ASN 476 462 462 ASN ASN A . n 
A 1 477 GLU 477 463 463 GLU GLU A . n 
A 1 478 GLY 478 464 464 GLY GLY A . n 
A 1 479 TYR 479 465 465 TYR TYR A . n 
A 1 480 THR 480 466 466 THR THR A . n 
A 1 481 VAL 481 467 467 VAL VAL A . n 
A 1 482 GLU 482 468 468 GLU GLU A . n 
A 1 483 ARG 483 469 469 ARG ARG A . n 
A 1 484 ALA 484 470 470 ALA ALA A . n 
A 1 485 ILE 485 471 471 ILE ILE A . n 
A 1 486 HIS 486 472 472 HIS HIS A . n 
A 1 487 GLY 487 473 473 GLY GLY A . n 
A 1 488 PRO 488 474 474 PRO PRO A . n 
A 1 489 GLU 489 475 475 GLU GLU A . n 
A 1 490 GLN 490 476 476 GLN GLN A . n 
A 1 491 ARG 491 477 477 ARG ARG A . n 
A 1 492 TYR 492 478 478 TYR TYR A . n 
A 1 493 ASN 493 479 479 ASN ASN A . n 
A 1 494 ASP 494 480 480 ASP ASP A . n 
A 1 495 ILE 495 481 481 ILE ILE A . n 
A 1 496 ALA 496 482 482 ALA ALA A . n 
A 1 497 LEU 497 483 483 LEU LEU A . n 
A 1 498 TRP 498 484 484 TRP TRP A . n 
A 1 499 ASN 499 485 485 ASN ASN A . n 
A 1 500 TRP 500 486 486 TRP TRP A . n 
A 1 501 THR 501 487 487 THR THR A . n 
A 1 502 GLN 502 488 488 GLN GLN A . n 
A 1 503 ILE 503 489 489 ILE ILE A . n 
A 1 504 PRO 504 490 490 PRO PRO A . n 
A 1 505 GLN 505 491 491 GLN GLN A . n 
A 1 506 ALA 506 492 492 ALA ALA A . n 
A 1 507 LEU 507 493 493 LEU LEU A . n 
A 1 508 SER 508 494 494 SER SER A . n 
A 1 509 LEU 509 495 495 LEU LEU A . n 
A 1 510 ASP 510 496 496 ASP ASP A . n 
A 1 511 PRO 511 497 497 PRO PRO A . n 
A 1 512 GLN 512 498 498 GLN GLN A . n 
A 1 513 ALA 513 499 499 ALA ALA A . n 
A 1 514 GLN 514 500 500 GLN GLN A . n 
A 1 515 CYS 515 501 501 CYS CYS A . n 
A 1 516 TRP 516 502 502 TRP TRP A . n 
A 1 517 ARG 517 503 503 ARG ARG A . n 
A 1 518 VAL 518 504 504 VAL VAL A . n 
A 1 519 SER 519 505 505 SER SER A . n 
A 1 520 GLU 520 506 506 GLU GLU A . n 
A 1 521 ALA 521 507 507 ALA ALA A . n 
A 1 522 GLU 522 508 508 GLU GLU A . n 
A 1 523 GLN 523 509 509 GLN GLN A . n 
A 1 524 LEU 524 510 510 LEU LEU A . n 
A 1 525 ALA 525 511 511 ALA ALA A . n 
A 1 526 ASP 526 512 512 ASP ASP A . n 
A 1 527 VAL 527 513 513 VAL VAL A . n 
A 1 528 LEU 528 514 514 LEU LEU A . n 
A 1 529 GLU 529 515 515 GLU GLU A . n 
A 1 530 LYS 530 516 516 LYS LYS A . n 
A 1 531 VAL 531 517 517 VAL VAL A . n 
A 1 532 ALA 532 518 518 ALA ALA A . n 
A 1 533 HIS 533 519 519 HIS HIS A . n 
A 1 534 HIS 534 520 520 HIS HIS A . n 
A 1 535 GLU 535 521 521 GLU GLU A . n 
A 1 536 ARG 536 522 522 ARG ARG A . n 
A 1 537 LEU 537 523 523 LEU LEU A . n 
A 1 538 SER 538 524 524 SER SER A . n 
A 1 539 LEU 539 525 525 LEU LEU A . n 
A 1 540 ILE 540 526 526 ILE ILE A . n 
A 1 541 GLU 541 527 527 GLU GLU A . n 
A 1 542 VAL 542 528 528 VAL VAL A . n 
A 1 543 MET 543 529 529 MET MET A . n 
A 1 544 LEU 544 530 530 LEU LEU A . n 
A 1 545 PRO 545 531 531 PRO PRO A . n 
A 1 546 LYS 546 532 532 LYS LYS A . n 
A 1 547 ALA 547 533 533 ALA ALA A . n 
A 1 548 ASP 548 534 534 ASP ASP A . n 
A 1 549 ILE 549 535 535 ILE ILE A . n 
A 1 550 PRO 550 536 536 PRO PRO A . n 
A 1 551 PRO 551 537 537 PRO PRO A . n 
A 1 552 LEU 552 538 538 LEU LEU A . n 
A 1 553 LEU 553 539 539 LEU LEU A . n 
A 1 554 GLY 554 540 540 GLY GLY A . n 
A 1 555 ALA 555 541 541 ALA ALA A . n 
A 1 556 ILE 556 542 542 ILE ILE A . n 
A 1 557 THR 557 543 543 THR THR A . n 
A 1 558 LYS 558 544 544 LYS LYS A . n 
A 1 559 ALA 559 545 545 ALA ALA A . n 
A 1 560 LEU 560 546 546 LEU LEU A . n 
A 1 561 GLU 561 547 547 GLU GLU A . n 
A 1 562 ALA 562 548 548 ALA ALA A . n 
A 1 563 ARG 563 549 549 ARG ARG A . n 
A 1 564 ASN 564 550 550 ASN ASN A . n 
A 1 565 SER 565 551 551 SER SER A . n 
A 1 566 ALA 566 552 ?   ?   ?   A . n 
B 1 1   MET 1   -13 ?   ?   ?   B . n 
B 1 2   GLY 2   -12 ?   ?   ?   B . n 
B 1 3   SER 3   -11 ?   ?   ?   B . n 
B 1 4   SER 4   -10 ?   ?   ?   B . n 
B 1 5   HIS 5   -9  ?   ?   ?   B . n 
B 1 6   HIS 6   -8  ?   ?   ?   B . n 
B 1 7   HIS 7   -7  ?   ?   ?   B . n 
B 1 8   HIS 8   -6  ?   ?   ?   B . n 
B 1 9   HIS 9   -5  ?   ?   ?   B . n 
B 1 10  HIS 10  -4  ?   ?   ?   B . n 
B 1 11  SER 11  -3  ?   ?   ?   B . n 
B 1 12  GLN 12  -2  ?   ?   ?   B . n 
B 1 13  ASP 13  -1  ?   ?   ?   B . n 
B 1 14  PRO 14  0   ?   ?   ?   B . n 
B 1 15  MET 15  1   ?   ?   ?   B . n 
B 1 16  ARG 16  2   ?   ?   ?   B . n 
B 1 17  THR 17  3   3   THR THR B . n 
B 1 18  PRO 18  4   4   PRO PRO B . n 
B 1 19  TYR 19  5   5   TYR TYR B . n 
B 1 20  CYS 20  6   6   CYS CYS B . n 
B 1 21  VAL 21  7   7   VAL VAL B . n 
B 1 22  ALA 22  8   8   ALA ALA B . n 
B 1 23  ASP 23  9   9   ASP ASP B . n 
B 1 24  TYR 24  10  10  TYR TYR B . n 
B 1 25  LEU 25  11  11  LEU LEU B . n 
B 1 26  LEU 26  12  12  LEU LEU B . n 
B 1 27  ASP 27  13  13  ASP ASP B . n 
B 1 28  ARG 28  14  14  ARG ARG B . n 
B 1 29  LEU 29  15  15  LEU LEU B . n 
B 1 30  THR 30  16  16  THR THR B . n 
B 1 31  ASP 31  17  17  ASP ASP B . n 
B 1 32  CYS 32  18  18  CYS CYS B . n 
B 1 33  GLY 33  19  19  GLY GLY B . n 
B 1 34  ALA 34  20  20  ALA ALA B . n 
B 1 35  ASP 35  21  21  ASP ASP B . n 
B 1 36  HIS 36  22  22  HIS HIS B . n 
B 1 37  LEU 37  23  23  LEU LEU B . n 
B 1 38  PHE 38  24  24  PHE PHE B . n 
B 1 39  GLY 39  25  25  GLY GLY B . n 
B 1 40  VAL 40  26  26  VAL VAL B . n 
B 1 41  PRO 41  27  27  PRO PRO B . n 
B 1 42  GLY 42  28  28  GLY GLY B . n 
B 1 43  ASP 43  29  29  ASP ASP B . n 
B 1 44  TYR 44  30  30  TYR TYR B . n 
B 1 45  ASN 45  31  31  ASN ASN B . n 
B 1 46  LEU 46  32  32  LEU LEU B . n 
B 1 47  GLN 47  33  33  GLN GLN B . n 
B 1 48  PHE 48  34  34  PHE PHE B . n 
B 1 49  LEU 49  35  35  LEU LEU B . n 
B 1 50  ASP 50  36  36  ASP ASP B . n 
B 1 51  HIS 51  37  37  HIS HIS B . n 
B 1 52  VAL 52  38  38  VAL VAL B . n 
B 1 53  ILE 53  39  39  ILE ILE B . n 
B 1 54  ASP 54  40  40  ASP ASP B . n 
B 1 55  SER 55  41  41  SER SER B . n 
B 1 56  PRO 56  42  42  PRO PRO B . n 
B 1 57  ASP 57  43  43  ASP ASP B . n 
B 1 58  ILE 58  44  44  ILE ILE B . n 
B 1 59  CYS 59  45  45  CYS CYS B . n 
B 1 60  TRP 60  46  46  TRP TRP B . n 
B 1 61  VAL 61  47  47  VAL VAL B . n 
B 1 62  GLY 62  48  48  GLY GLY B . n 
B 1 63  CYS 63  49  49  CYS CYS B . n 
B 1 64  ALA 64  50  50  ALA ALA B . n 
B 1 65  ASN 65  51  51  ASN ASN B . n 
B 1 66  GLU 66  52  52  GLU GLU B . n 
B 1 67  LEU 67  53  53  LEU LEU B . n 
B 1 68  ASN 68  54  54  ASN ASN B . n 
B 1 69  ALA 69  55  55  ALA ALA B . n 
B 1 70  SER 70  56  56  SER SER B . n 
B 1 71  TYR 71  57  57  TYR TYR B . n 
B 1 72  ALA 72  58  58  ALA ALA B . n 
B 1 73  ALA 73  59  59  ALA ALA B . n 
B 1 74  ASP 74  60  60  ASP ASP B . n 
B 1 75  GLY 75  61  61  GLY GLY B . n 
B 1 76  TYR 76  62  62  TYR TYR B . n 
B 1 77  ALA 77  63  63  ALA ALA B . n 
B 1 78  ARG 78  64  64  ARG ARG B . n 
B 1 79  CYS 79  65  65  CYS CYS B . n 
B 1 80  LYS 80  66  66  LYS LYS B . n 
B 1 81  GLY 81  67  67  GLY GLY B . n 
B 1 82  PHE 82  68  68  PHE PHE B . n 
B 1 83  ALA 83  69  69  ALA ALA B . n 
B 1 84  ALA 84  70  70  ALA ALA B . n 
B 1 85  LEU 85  71  71  LEU LEU B . n 
B 1 86  LEU 86  72  72  LEU LEU B . n 
B 1 87  THR 87  73  73  THR THR B . n 
B 1 88  THR 88  74  74  THR THR B . n 
B 1 89  PHE 89  75  75  PHE PHE B . n 
B 1 90  GLY 90  76  76  GLY GLY B . n 
B 1 91  VAL 91  77  77  VAL VAL B . n 
B 1 92  GLY 92  78  78  GLY GLY B . n 
B 1 93  GLU 93  79  79  GLU GLU B . n 
B 1 94  LEU 94  80  80  LEU LEU B . n 
B 1 95  SER 95  81  81  SER SER B . n 
B 1 96  ALA 96  82  82  ALA ALA B . n 
B 1 97  MET 97  83  83  MET MET B . n 
B 1 98  ASN 98  84  84  ASN ASN B . n 
B 1 99  GLY 99  85  85  GLY GLY B . n 
B 1 100 ILE 100 86  86  ILE ILE B . n 
B 1 101 ALA 101 87  87  ALA ALA B . n 
B 1 102 GLY 102 88  88  GLY GLY B . n 
B 1 103 SER 103 89  89  SER SER B . n 
B 1 104 TYR 104 90  90  TYR TYR B . n 
B 1 105 ALA 105 91  91  ALA ALA B . n 
B 1 106 GLU 106 92  92  GLU GLU B . n 
B 1 107 HIS 107 93  93  HIS HIS B . n 
B 1 108 VAL 108 94  94  VAL VAL B . n 
B 1 109 PRO 109 95  95  PRO PRO B . n 
B 1 110 VAL 110 96  96  VAL VAL B . n 
B 1 111 LEU 111 97  97  LEU LEU B . n 
B 1 112 HIS 112 98  98  HIS HIS B . n 
B 1 113 ILE 113 99  99  ILE ILE B . n 
B 1 114 VAL 114 100 100 VAL VAL B . n 
B 1 115 GLY 115 101 101 GLY GLY B . n 
B 1 116 ALA 116 102 102 ALA ALA B . n 
B 1 117 PRO 117 103 103 PRO PRO B . n 
B 1 118 GLY 118 104 104 GLY GLY B . n 
B 1 119 THR 119 105 105 THR THR B . n 
B 1 120 ALA 120 106 106 ALA ALA B . n 
B 1 121 SER 121 107 107 SER SER B . n 
B 1 122 GLN 122 108 108 GLN GLN B . n 
B 1 123 GLN 123 109 109 GLN GLN B . n 
B 1 124 ARG 124 110 110 ARG ARG B . n 
B 1 125 GLY 125 111 111 GLY GLY B . n 
B 1 126 GLU 126 112 112 GLU GLU B . n 
B 1 127 LEU 127 113 113 LEU LEU B . n 
B 1 128 LEU 128 114 114 LEU LEU B . n 
B 1 129 HIS 129 115 115 HIS HIS B . n 
B 1 130 HIS 130 116 116 HIS HIS B . n 
B 1 131 THR 131 117 117 THR THR B . n 
B 1 132 LEU 132 118 118 LEU LEU B . n 
B 1 133 GLY 133 119 119 GLY GLY B . n 
B 1 134 ASP 134 120 120 ASP ASP B . n 
B 1 135 GLY 135 121 121 GLY GLY B . n 
B 1 136 GLU 136 122 122 GLU GLU B . n 
B 1 137 PHE 137 123 123 PHE PHE B . n 
B 1 138 ARG 138 124 124 ARG ARG B . n 
B 1 139 HIS 139 125 125 HIS HIS B . n 
B 1 140 PHE 140 126 126 PHE PHE B . n 
B 1 141 TYR 141 127 127 TYR TYR B . n 
B 1 142 HIS 142 128 128 HIS HIS B . n 
B 1 143 MET 143 129 129 MET MET B . n 
B 1 144 SER 144 130 130 SER SER B . n 
B 1 145 GLU 145 131 131 GLU GLU B . n 
B 1 146 PRO 146 132 132 PRO PRO B . n 
B 1 147 ILE 147 133 133 ILE ILE B . n 
B 1 148 THR 148 134 134 THR THR B . n 
B 1 149 VAL 149 135 135 VAL VAL B . n 
B 1 150 ALA 150 136 136 ALA ALA B . n 
B 1 151 GLN 151 137 137 GLN GLN B . n 
B 1 152 ALA 152 138 138 ALA ALA B . n 
B 1 153 ILE 153 139 139 ILE ILE B . n 
B 1 154 LEU 154 140 140 LEU LEU B . n 
B 1 155 THR 155 141 141 THR THR B . n 
B 1 156 GLU 156 142 142 GLU GLU B . n 
B 1 157 GLN 157 143 143 GLN GLN B . n 
B 1 158 ASN 158 144 144 ASN ASN B . n 
B 1 159 ALA 159 145 145 ALA ALA B . n 
B 1 160 CYS 160 146 146 CYS CYS B . n 
B 1 161 TYR 161 147 147 TYR TYR B . n 
B 1 162 GLU 162 148 148 GLU GLU B . n 
B 1 163 ILE 163 149 149 ILE ILE B . n 
B 1 164 ASP 164 150 150 ASP ASP B . n 
B 1 165 ARG 165 151 151 ARG ARG B . n 
B 1 166 VAL 166 152 152 VAL VAL B . n 
B 1 167 LEU 167 153 153 LEU LEU B . n 
B 1 168 THR 168 154 154 THR THR B . n 
B 1 169 THR 169 155 155 THR THR B . n 
B 1 170 MET 170 156 156 MET MET B . n 
B 1 171 LEU 171 157 157 LEU LEU B . n 
B 1 172 ARG 172 158 158 ARG ARG B . n 
B 1 173 GLU 173 159 159 GLU GLU B . n 
B 1 174 ARG 174 160 160 ARG ARG B . n 
B 1 175 ARG 175 161 161 ARG ARG B . n 
B 1 176 PRO 176 162 162 PRO PRO B . n 
B 1 177 GLY 177 163 163 GLY GLY B . n 
B 1 178 TYR 178 164 164 TYR TYR B . n 
B 1 179 LEU 179 165 165 LEU LEU B . n 
B 1 180 MET 180 166 166 MET MET B . n 
B 1 181 LEU 181 167 167 LEU LEU B . n 
B 1 182 PRO 182 168 168 PRO PRO B . n 
B 1 183 ALA 183 169 169 ALA ALA B . n 
B 1 184 ASP 184 170 170 ASP ASP B . n 
B 1 185 VAL 185 171 171 VAL VAL B . n 
B 1 186 ALA 186 172 172 ALA ALA B . n 
B 1 187 LYS 187 173 173 LYS LYS B . n 
B 1 188 LYS 188 174 174 LYS LYS B . n 
B 1 189 ALA 189 175 175 ALA ALA B . n 
B 1 190 ALA 190 176 176 ALA ALA B . n 
B 1 191 THR 191 177 177 THR THR B . n 
B 1 192 PRO 192 178 178 PRO PRO B . n 
B 1 193 PRO 193 179 179 PRO PRO B . n 
B 1 194 VAL 194 180 180 VAL VAL B . n 
B 1 195 ASN 195 181 181 ASN ASN B . n 
B 1 196 ALA 196 182 182 ALA ALA B . n 
B 1 197 LEU 197 183 183 LEU LEU B . n 
B 1 198 THR 198 184 184 THR THR B . n 
B 1 199 LEU 199 185 185 LEU LEU B . n 
B 1 200 ARG 200 186 186 ARG ARG B . n 
B 1 201 HIS 201 187 187 HIS HIS B . n 
B 1 202 ALA 202 188 188 ALA ALA B . n 
B 1 203 HIS 203 189 189 HIS HIS B . n 
B 1 204 ALA 204 190 190 ALA ALA B . n 
B 1 205 ASP 205 191 191 ASP ASP B . n 
B 1 206 SER 206 192 192 SER SER B . n 
B 1 207 ALA 207 193 193 ALA ALA B . n 
B 1 208 CYS 208 194 194 CYS CYS B . n 
B 1 209 LEU 209 195 195 LEU LEU B . n 
B 1 210 LYS 210 196 196 LYS LYS B . n 
B 1 211 ALA 211 197 197 ALA ALA B . n 
B 1 212 PHE 212 198 198 PHE PHE B . n 
B 1 213 ARG 213 199 199 ARG ARG B . n 
B 1 214 ASP 214 200 200 ASP ASP B . n 
B 1 215 ALA 215 201 201 ALA ALA B . n 
B 1 216 ALA 216 202 202 ALA ALA B . n 
B 1 217 GLU 217 203 203 GLU GLU B . n 
B 1 218 ASN 218 204 204 ASN ASN B . n 
B 1 219 ARG 219 205 205 ARG ARG B . n 
B 1 220 LEU 220 206 206 LEU LEU B . n 
B 1 221 ALA 221 207 207 ALA ALA B . n 
B 1 222 MET 222 208 208 MET MET B . n 
B 1 223 SER 223 209 209 SER SER B . n 
B 1 224 LYS 224 210 210 LYS LYS B . n 
B 1 225 ARG 225 211 211 ARG ARG B . n 
B 1 226 THR 226 212 212 THR THR B . n 
B 1 227 ALA 227 213 213 ALA ALA B . n 
B 1 228 LEU 228 214 214 LEU LEU B . n 
B 1 229 LEU 229 215 215 LEU LEU B . n 
B 1 230 ALA 230 216 216 ALA ALA B . n 
B 1 231 ASP 231 217 217 ASP ASP B . n 
B 1 232 PHE 232 218 218 PHE PHE B . n 
B 1 233 LEU 233 219 219 LEU LEU B . n 
B 1 234 VAL 234 220 220 VAL VAL B . n 
B 1 235 LEU 235 221 221 LEU LEU B . n 
B 1 236 ARG 236 222 222 ARG ARG B . n 
B 1 237 HIS 237 223 223 HIS HIS B . n 
B 1 238 GLY 238 224 224 GLY GLY B . n 
B 1 239 LEU 239 225 225 LEU LEU B . n 
B 1 240 LYS 240 226 226 LYS LYS B . n 
B 1 241 HIS 241 227 227 HIS HIS B . n 
B 1 242 ALA 242 228 228 ALA ALA B . n 
B 1 243 LEU 243 229 229 LEU LEU B . n 
B 1 244 GLN 244 230 230 GLN GLN B . n 
B 1 245 LYS 245 231 231 LYS LYS B . n 
B 1 246 TRP 246 232 232 TRP TRP B . n 
B 1 247 VAL 247 233 233 VAL VAL B . n 
B 1 248 LYS 248 234 234 LYS LYS B . n 
B 1 249 ASP 249 235 235 ASP ASP B . n 
B 1 250 VAL 250 236 236 VAL VAL B . n 
B 1 251 PRO 251 237 237 PRO PRO B . n 
B 1 252 MET 252 238 238 MET MET B . n 
B 1 253 ALA 253 239 239 ALA ALA B . n 
B 1 254 HIS 254 240 240 HIS HIS B . n 
B 1 255 ALA 255 241 241 ALA ALA B . n 
B 1 256 THR 256 242 242 THR THR B . n 
B 1 257 MET 257 243 243 MET MET B . n 
B 1 258 LEU 258 244 244 LEU LEU B . n 
B 1 259 MET 259 245 245 MET MET B . n 
B 1 260 GLY 260 246 246 GLY GLY B . n 
B 1 261 LYS 261 247 247 LYS LYS B . n 
B 1 262 GLY 262 248 248 GLY GLY B . n 
B 1 263 ILE 263 249 249 ILE ILE B . n 
B 1 264 PHE 264 250 250 PHE PHE B . n 
B 1 265 ASP 265 251 251 ASP ASP B . n 
B 1 266 GLU 266 252 252 GLU GLU B . n 
B 1 267 ARG 267 253 253 ARG ARG B . n 
B 1 268 HIS 268 254 254 HIS HIS B . n 
B 1 269 VAL 269 255 255 VAL VAL B . n 
B 1 270 GLY 270 256 256 GLY GLY B . n 
B 1 271 PHE 271 257 257 PHE PHE B . n 
B 1 272 TYR 272 258 258 TYR TYR B . n 
B 1 273 GLY 273 259 259 GLY GLY B . n 
B 1 274 THR 274 260 260 THR THR B . n 
B 1 275 TYR 275 261 261 TYR TYR B . n 
B 1 276 SER 276 262 262 SER SER B . n 
B 1 277 GLY 277 263 263 GLY GLY B . n 
B 1 278 SER 278 264 264 SER SER B . n 
B 1 279 ALA 279 265 265 ALA ALA B . n 
B 1 280 SER 280 266 266 SER SER B . n 
B 1 281 ALA 281 267 267 ALA ALA B . n 
B 1 282 GLY 282 268 268 GLY GLY B . n 
B 1 283 ALA 283 269 269 ALA ALA B . n 
B 1 284 VAL 284 270 270 VAL VAL B . n 
B 1 285 LYS 285 271 271 LYS LYS B . n 
B 1 286 GLU 286 272 272 GLU GLU B . n 
B 1 287 ALA 287 273 273 ALA ALA B . n 
B 1 288 ILE 288 274 274 ILE ILE B . n 
B 1 289 GLU 289 275 275 GLU GLU B . n 
B 1 290 GLY 290 276 276 GLY GLY B . n 
B 1 291 ALA 291 277 277 ALA ALA B . n 
B 1 292 ASP 292 278 278 ASP ASP B . n 
B 1 293 THR 293 279 279 THR THR B . n 
B 1 294 VAL 294 280 280 VAL VAL B . n 
B 1 295 LEU 295 281 281 LEU LEU B . n 
B 1 296 CYS 296 282 282 CYS CYS B . n 
B 1 297 ILE 297 283 283 ILE ILE B . n 
B 1 298 GLY 298 284 284 GLY GLY B . n 
B 1 299 THR 299 285 285 THR THR B . n 
B 1 300 ARG 300 286 286 ARG ARG B . n 
B 1 301 PHE 301 287 287 PHE PHE B . n 
B 1 302 THR 302 288 288 THR THR B . n 
B 1 303 ASP 303 289 289 ASP ASP B . n 
B 1 304 THR 304 290 290 THR THR B . n 
B 1 305 LEU 305 291 291 LEU LEU B . n 
B 1 306 THR 306 292 292 THR THR B . n 
B 1 307 ALA 307 293 293 ALA ALA B . n 
B 1 308 GLY 308 294 294 GLY GLY B . n 
B 1 309 PHE 309 295 295 PHE PHE B . n 
B 1 310 THR 310 296 296 THR THR B . n 
B 1 311 HIS 311 297 297 HIS HIS B . n 
B 1 312 GLN 312 298 298 GLN GLN B . n 
B 1 313 LEU 313 299 299 LEU LEU B . n 
B 1 314 THR 314 300 300 THR THR B . n 
B 1 315 PRO 315 301 301 PRO PRO B . n 
B 1 316 SER 316 302 302 SER SER B . n 
B 1 317 GLN 317 303 303 GLN GLN B . n 
B 1 318 THR 318 304 304 THR THR B . n 
B 1 319 ILE 319 305 305 ILE ILE B . n 
B 1 320 GLU 320 306 306 GLU GLU B . n 
B 1 321 VAL 321 307 307 VAL VAL B . n 
B 1 322 GLN 322 308 308 GLN GLN B . n 
B 1 323 PRO 323 309 309 PRO PRO B . n 
B 1 324 HIS 324 310 310 HIS HIS B . n 
B 1 325 ALA 325 311 311 ALA ALA B . n 
B 1 326 SER 326 312 312 SER SER B . n 
B 1 327 ARG 327 313 313 ARG ARG B . n 
B 1 328 VAL 328 314 314 VAL VAL B . n 
B 1 329 GLY 329 315 315 GLY GLY B . n 
B 1 330 ASP 330 316 316 ASP ASP B . n 
B 1 331 VAL 331 317 317 VAL VAL B . n 
B 1 332 TRP 332 318 318 TRP TRP B . n 
B 1 333 PHE 333 319 319 PHE PHE B . n 
B 1 334 THR 334 320 320 THR THR B . n 
B 1 335 GLY 335 321 321 GLY GLY B . n 
B 1 336 ILE 336 322 322 ILE ILE B . n 
B 1 337 PRO 337 323 323 PRO PRO B . n 
B 1 338 MET 338 324 324 MET MET B . n 
B 1 339 LEU 339 325 325 LEU LEU B . n 
B 1 340 GLN 340 326 326 GLN GLN B . n 
B 1 341 ALA 341 327 327 ALA ALA B . n 
B 1 342 ILE 342 328 328 ILE ILE B . n 
B 1 343 GLU 343 329 329 GLU GLU B . n 
B 1 344 THR 344 330 330 THR THR B . n 
B 1 345 LEU 345 331 331 LEU LEU B . n 
B 1 346 VAL 346 332 332 VAL VAL B . n 
B 1 347 GLU 347 333 333 GLU GLU B . n 
B 1 348 LEU 348 334 334 LEU LEU B . n 
B 1 349 CYS 349 335 335 CYS CYS B . n 
B 1 350 LYS 350 336 336 LYS LYS B . n 
B 1 351 GLN 351 337 337 GLN GLN B . n 
B 1 352 HIS 352 338 338 HIS HIS B . n 
B 1 353 VAL 353 339 339 VAL VAL B . n 
B 1 354 HIS 354 340 340 HIS HIS B . n 
B 1 355 ASP 355 341 341 ASP ASP B . n 
B 1 356 THR 356 342 342 THR THR B . n 
B 1 357 PRO 357 343 343 PRO PRO B . n 
B 1 358 VAL 358 344 ?   ?   ?   B . n 
B 1 359 PRO 359 345 ?   ?   ?   B . n 
B 1 360 SER 360 346 ?   ?   ?   B . n 
B 1 361 SER 361 347 ?   ?   ?   B . n 
B 1 362 GLN 362 348 ?   ?   ?   B . n 
B 1 363 SER 363 349 ?   ?   ?   B . n 
B 1 364 ALA 364 350 ?   ?   ?   B . n 
B 1 365 MET 365 351 ?   ?   ?   B . n 
B 1 366 VAL 366 352 ?   ?   ?   B . n 
B 1 367 TYR 367 353 ?   ?   ?   B . n 
B 1 368 PRO 368 354 ?   ?   ?   B . n 
B 1 369 GLN 369 355 ?   ?   ?   B . n 
B 1 370 PRO 370 356 356 PRO PRO B . n 
B 1 371 ASP 371 357 357 ASP ASP B . n 
B 1 372 GLY 372 358 358 GLY GLY B . n 
B 1 373 SER 373 359 359 SER SER B . n 
B 1 374 LEU 374 360 360 LEU LEU B . n 
B 1 375 THR 375 361 361 THR THR B . n 
B 1 376 GLN 376 362 362 GLN GLN B . n 
B 1 377 ASP 377 363 363 ASP ASP B . n 
B 1 378 ASN 378 364 364 ASN ASN B . n 
B 1 379 PHE 379 365 365 PHE PHE B . n 
B 1 380 TRP 380 366 366 TRP TRP B . n 
B 1 381 LYS 381 367 367 LYS LYS B . n 
B 1 382 THR 382 368 368 THR THR B . n 
B 1 383 LEU 383 369 369 LEU LEU B . n 
B 1 384 GLN 384 370 370 GLN GLN B . n 
B 1 385 THR 385 371 371 THR THR B . n 
B 1 386 PHE 386 372 372 PHE PHE B . n 
B 1 387 ILE 387 373 373 ILE ILE B . n 
B 1 388 ARG 388 374 374 ARG ARG B . n 
B 1 389 PRO 389 375 375 PRO PRO B . n 
B 1 390 GLY 390 376 376 GLY GLY B . n 
B 1 391 ASP 391 377 377 ASP ASP B . n 
B 1 392 ILE 392 378 378 ILE ILE B . n 
B 1 393 ILE 393 379 379 ILE ILE B . n 
B 1 394 LEU 394 380 380 LEU LEU B . n 
B 1 395 ALA 395 381 381 ALA ALA B . n 
B 1 396 ASP 396 382 382 ASP ASP B . n 
B 1 397 GLN 397 383 383 GLN GLN B . n 
B 1 398 GLY 398 384 384 GLY GLY B . n 
B 1 399 THR 399 385 385 THR THR B . n 
B 1 400 SER 400 386 386 SER SER B . n 
B 1 401 ALA 401 387 387 ALA ALA B . n 
B 1 402 PHE 402 388 388 PHE PHE B . n 
B 1 403 GLY 403 389 389 GLY GLY B . n 
B 1 404 ALA 404 390 390 ALA ALA B . n 
B 1 405 ILE 405 391 391 ILE ILE B . n 
B 1 406 ASP 406 392 392 ASP ASP B . n 
B 1 407 LEU 407 393 393 LEU LEU B . n 
B 1 408 ARG 408 394 394 ARG ARG B . n 
B 1 409 LEU 409 395 395 LEU LEU B . n 
B 1 410 PRO 410 396 396 PRO PRO B . n 
B 1 411 ALA 411 397 397 ALA ALA B . n 
B 1 412 ASP 412 398 398 ASP ASP B . n 
B 1 413 VAL 413 399 399 VAL VAL B . n 
B 1 414 ASN 414 400 400 ASN ASN B . n 
B 1 415 PHE 415 401 401 PHE PHE B . n 
B 1 416 ILE 416 402 402 ILE ILE B . n 
B 1 417 VAL 417 403 403 VAL VAL B . n 
B 1 418 GLN 418 404 404 GLN GLN B . n 
B 1 419 PRO 419 405 405 PRO PRO B . n 
B 1 420 LEU 420 406 406 LEU LEU B . n 
B 1 421 TRP 421 407 407 TRP TRP B . n 
B 1 422 GLY 422 408 408 GLY GLY B . n 
B 1 423 SER 423 409 409 SER SER B . n 
B 1 424 ILE 424 410 410 ILE ILE B . n 
B 1 425 GLY 425 411 411 GLY GLY B . n 
B 1 426 TYR 426 412 412 TYR TYR B . n 
B 1 427 THR 427 413 413 THR THR B . n 
B 1 428 LEU 428 414 414 LEU LEU B . n 
B 1 429 ALA 429 415 415 ALA ALA B . n 
B 1 430 ALA 430 416 416 ALA ALA B . n 
B 1 431 ALA 431 417 417 ALA ALA B . n 
B 1 432 PHE 432 418 418 PHE PHE B . n 
B 1 433 GLY 433 419 419 GLY GLY B . n 
B 1 434 ALA 434 420 420 ALA ALA B . n 
B 1 435 GLN 435 421 421 GLN GLN B . n 
B 1 436 THR 436 422 422 THR THR B . n 
B 1 437 ALA 437 423 423 ALA ALA B . n 
B 1 438 CYS 438 424 424 CYS CYS B . n 
B 1 439 PRO 439 425 425 PRO PRO B . n 
B 1 440 ASN 440 426 426 ASN ASN B . n 
B 1 441 ARG 441 427 427 ARG ARG B . n 
B 1 442 ARG 442 428 428 ARG ARG B . n 
B 1 443 VAL 443 429 429 VAL VAL B . n 
B 1 444 ILE 444 430 430 ILE ILE B . n 
B 1 445 VAL 445 431 431 VAL VAL B . n 
B 1 446 LEU 446 432 432 LEU LEU B . n 
B 1 447 THR 447 433 433 THR THR B . n 
B 1 448 GLY 448 434 434 GLY GLY B . n 
B 1 449 ASP 449 435 435 ASP ASP B . n 
B 1 450 GLY 450 436 436 GLY GLY B . n 
B 1 451 ALA 451 437 437 ALA ALA B . n 
B 1 452 ALA 452 438 438 ALA ALA B . n 
B 1 453 GLN 453 439 439 GLN GLN B . n 
B 1 454 LEU 454 440 440 LEU LEU B . n 
B 1 455 THR 455 441 441 THR THR B . n 
B 1 456 ILE 456 442 442 ILE ILE B . n 
B 1 457 GLN 457 443 443 GLN GLN B . n 
B 1 458 GLU 458 444 444 GLU GLU B . n 
B 1 459 LEU 459 445 445 LEU LEU B . n 
B 1 460 GLY 460 446 446 GLY GLY B . n 
B 1 461 SER 461 447 447 SER SER B . n 
B 1 462 MET 462 448 448 MET MET B . n 
B 1 463 LEU 463 449 449 LEU LEU B . n 
B 1 464 ARG 464 450 450 ARG ARG B . n 
B 1 465 ASP 465 451 451 ASP ASP B . n 
B 1 466 LYS 466 452 452 LYS LYS B . n 
B 1 467 GLN 467 453 453 GLN GLN B . n 
B 1 468 HIS 468 454 454 HIS HIS B . n 
B 1 469 PRO 469 455 455 PRO PRO B . n 
B 1 470 ILE 470 456 456 ILE ILE B . n 
B 1 471 ILE 471 457 457 ILE ILE B . n 
B 1 472 LEU 472 458 458 LEU LEU B . n 
B 1 473 VAL 473 459 459 VAL VAL B . n 
B 1 474 LEU 474 460 460 LEU LEU B . n 
B 1 475 ASN 475 461 461 ASN ASN B . n 
B 1 476 ASN 476 462 462 ASN ASN B . n 
B 1 477 GLU 477 463 463 GLU GLU B . n 
B 1 478 GLY 478 464 464 GLY GLY B . n 
B 1 479 TYR 479 465 465 TYR TYR B . n 
B 1 480 THR 480 466 466 THR THR B . n 
B 1 481 VAL 481 467 467 VAL VAL B . n 
B 1 482 GLU 482 468 468 GLU GLU B . n 
B 1 483 ARG 483 469 469 ARG ARG B . n 
B 1 484 ALA 484 470 470 ALA ALA B . n 
B 1 485 ILE 485 471 471 ILE ILE B . n 
B 1 486 HIS 486 472 472 HIS HIS B . n 
B 1 487 GLY 487 473 473 GLY GLY B . n 
B 1 488 PRO 488 474 474 PRO PRO B . n 
B 1 489 GLU 489 475 475 GLU GLU B . n 
B 1 490 GLN 490 476 476 GLN GLN B . n 
B 1 491 ARG 491 477 477 ARG ARG B . n 
B 1 492 TYR 492 478 478 TYR TYR B . n 
B 1 493 ASN 493 479 479 ASN ASN B . n 
B 1 494 ASP 494 480 480 ASP ASP B . n 
B 1 495 ILE 495 481 481 ILE ILE B . n 
B 1 496 ALA 496 482 482 ALA ALA B . n 
B 1 497 LEU 497 483 483 LEU LEU B . n 
B 1 498 TRP 498 484 484 TRP TRP B . n 
B 1 499 ASN 499 485 485 ASN ASN B . n 
B 1 500 TRP 500 486 486 TRP TRP B . n 
B 1 501 THR 501 487 487 THR THR B . n 
B 1 502 GLN 502 488 488 GLN GLN B . n 
B 1 503 ILE 503 489 489 ILE ILE B . n 
B 1 504 PRO 504 490 490 PRO PRO B . n 
B 1 505 GLN 505 491 491 GLN GLN B . n 
B 1 506 ALA 506 492 492 ALA ALA B . n 
B 1 507 LEU 507 493 493 LEU LEU B . n 
B 1 508 SER 508 494 494 SER SER B . n 
B 1 509 LEU 509 495 495 LEU LEU B . n 
B 1 510 ASP 510 496 496 ASP ASP B . n 
B 1 511 PRO 511 497 497 PRO PRO B . n 
B 1 512 GLN 512 498 498 GLN GLN B . n 
B 1 513 ALA 513 499 499 ALA ALA B . n 
B 1 514 GLN 514 500 500 GLN GLN B . n 
B 1 515 CYS 515 501 501 CYS CYS B . n 
B 1 516 TRP 516 502 502 TRP TRP B . n 
B 1 517 ARG 517 503 503 ARG ARG B . n 
B 1 518 VAL 518 504 504 VAL VAL B . n 
B 1 519 SER 519 505 505 SER SER B . n 
B 1 520 GLU 520 506 506 GLU GLU B . n 
B 1 521 ALA 521 507 507 ALA ALA B . n 
B 1 522 GLU 522 508 508 GLU GLU B . n 
B 1 523 GLN 523 509 509 GLN GLN B . n 
B 1 524 LEU 524 510 510 LEU LEU B . n 
B 1 525 ALA 525 511 511 ALA ALA B . n 
B 1 526 ASP 526 512 512 ASP ASP B . n 
B 1 527 VAL 527 513 513 VAL VAL B . n 
B 1 528 LEU 528 514 514 LEU LEU B . n 
B 1 529 GLU 529 515 515 GLU GLU B . n 
B 1 530 LYS 530 516 516 LYS LYS B . n 
B 1 531 VAL 531 517 517 VAL VAL B . n 
B 1 532 ALA 532 518 518 ALA ALA B . n 
B 1 533 HIS 533 519 519 HIS HIS B . n 
B 1 534 HIS 534 520 520 HIS HIS B . n 
B 1 535 GLU 535 521 521 GLU GLU B . n 
B 1 536 ARG 536 522 522 ARG ARG B . n 
B 1 537 LEU 537 523 523 LEU LEU B . n 
B 1 538 SER 538 524 524 SER SER B . n 
B 1 539 LEU 539 525 525 LEU LEU B . n 
B 1 540 ILE 540 526 526 ILE ILE B . n 
B 1 541 GLU 541 527 527 GLU GLU B . n 
B 1 542 VAL 542 528 528 VAL VAL B . n 
B 1 543 MET 543 529 529 MET MET B . n 
B 1 544 LEU 544 530 530 LEU LEU B . n 
B 1 545 PRO 545 531 531 PRO PRO B . n 
B 1 546 LYS 546 532 532 LYS LYS B . n 
B 1 547 ALA 547 533 533 ALA ALA B . n 
B 1 548 ASP 548 534 534 ASP ASP B . n 
B 1 549 ILE 549 535 535 ILE ILE B . n 
B 1 550 PRO 550 536 536 PRO PRO B . n 
B 1 551 PRO 551 537 537 PRO PRO B . n 
B 1 552 LEU 552 538 538 LEU LEU B . n 
B 1 553 LEU 553 539 539 LEU LEU B . n 
B 1 554 GLY 554 540 540 GLY GLY B . n 
B 1 555 ALA 555 541 541 ALA ALA B . n 
B 1 556 ILE 556 542 542 ILE ILE B . n 
B 1 557 THR 557 543 543 THR THR B . n 
B 1 558 LYS 558 544 544 LYS LYS B . n 
B 1 559 ALA 559 545 545 ALA ALA B . n 
B 1 560 LEU 560 546 546 LEU LEU B . n 
B 1 561 GLU 561 547 547 GLU GLU B . n 
B 1 562 ALA 562 548 548 ALA ALA B . n 
B 1 563 ARG 563 549 549 ARG ARG B . n 
B 1 564 ASN 564 550 550 ASN ASN B . n 
B 1 565 SER 565 551 551 SER SER B . n 
B 1 566 ALA 566 552 ?   ?   ?   B . 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 MG  ? ? MG  ? ? 'SUBJECT OF INVESTIGATION' ? 
2 TPP ? ? TPP ? ? '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 
C 2 TPP 1   601  2   TPP TPP A . 
D 3 MG  1   602  2   MG  MG  A . 
E 2 TPP 1   601  1   TPP TPP B . 
F 3 MG  1   602  1   MG  MG  B . 
G 4 HOH 1   701  767 HOH HOH A . 
G 4 HOH 2   702  847 HOH HOH A . 
G 4 HOH 3   703  771 HOH HOH A . 
G 4 HOH 4   704  309 HOH HOH A . 
G 4 HOH 5   705  769 HOH HOH A . 
G 4 HOH 6   706  516 HOH HOH A . 
G 4 HOH 7   707  596 HOH HOH A . 
G 4 HOH 8   708  773 HOH HOH A . 
G 4 HOH 9   709  781 HOH HOH A . 
G 4 HOH 10  710  753 HOH HOH A . 
G 4 HOH 11  711  505 HOH HOH A . 
G 4 HOH 12  712  666 HOH HOH A . 
G 4 HOH 13  713  377 HOH HOH A . 
G 4 HOH 14  714  229 HOH HOH A . 
G 4 HOH 15  715  848 HOH HOH A . 
G 4 HOH 16  716  387 HOH HOH A . 
G 4 HOH 17  717  792 HOH HOH A . 
G 4 HOH 18  718  119 HOH HOH A . 
G 4 HOH 19  719  843 HOH HOH A . 
G 4 HOH 20  720  533 HOH HOH A . 
G 4 HOH 21  721  624 HOH HOH A . 
G 4 HOH 22  722  2   HOH HOH A . 
G 4 HOH 23  723  742 HOH HOH A . 
G 4 HOH 24  724  578 HOH HOH A . 
G 4 HOH 25  725  844 HOH HOH A . 
G 4 HOH 26  726  183 HOH HOH A . 
G 4 HOH 27  727  33  HOH HOH A . 
G 4 HOH 28  728  232 HOH HOH A . 
G 4 HOH 29  729  317 HOH HOH A . 
G 4 HOH 30  730  669 HOH HOH A . 
G 4 HOH 31  731  240 HOH HOH A . 
G 4 HOH 32  732  526 HOH HOH A . 
G 4 HOH 33  733  290 HOH HOH A . 
G 4 HOH 34  734  746 HOH HOH A . 
G 4 HOH 35  735  111 HOH HOH A . 
G 4 HOH 36  736  614 HOH HOH A . 
G 4 HOH 37  737  891 HOH HOH A . 
G 4 HOH 38  738  213 HOH HOH A . 
G 4 HOH 39  739  276 HOH HOH A . 
G 4 HOH 40  740  306 HOH HOH A . 
G 4 HOH 41  741  284 HOH HOH A . 
G 4 HOH 42  742  260 HOH HOH A . 
G 4 HOH 43  743  215 HOH HOH A . 
G 4 HOH 44  744  875 HOH HOH A . 
G 4 HOH 45  745  118 HOH HOH A . 
G 4 HOH 46  746  859 HOH HOH A . 
G 4 HOH 47  747  380 HOH HOH A . 
G 4 HOH 48  748  535 HOH HOH A . 
G 4 HOH 49  749  651 HOH HOH A . 
G 4 HOH 50  750  136 HOH HOH A . 
G 4 HOH 51  751  849 HOH HOH A . 
G 4 HOH 52  752  1   HOH HOH A . 
G 4 HOH 53  753  299 HOH HOH A . 
G 4 HOH 54  754  152 HOH HOH A . 
G 4 HOH 55  755  132 HOH HOH A . 
G 4 HOH 56  756  86  HOH HOH A . 
G 4 HOH 57  757  631 HOH HOH A . 
G 4 HOH 58  758  188 HOH HOH A . 
G 4 HOH 59  759  206 HOH HOH A . 
G 4 HOH 60  760  340 HOH HOH A . 
G 4 HOH 61  761  85  HOH HOH A . 
G 4 HOH 62  762  93  HOH HOH A . 
G 4 HOH 63  763  54  HOH HOH A . 
G 4 HOH 64  764  222 HOH HOH A . 
G 4 HOH 65  765  107 HOH HOH A . 
G 4 HOH 66  766  698 HOH HOH A . 
G 4 HOH 67  767  348 HOH HOH A . 
G 4 HOH 68  768  692 HOH HOH A . 
G 4 HOH 69  769  274 HOH HOH A . 
G 4 HOH 70  770  216 HOH HOH A . 
G 4 HOH 71  771  156 HOH HOH A . 
G 4 HOH 72  772  305 HOH HOH A . 
G 4 HOH 73  773  96  HOH HOH A . 
G 4 HOH 74  774  369 HOH HOH A . 
G 4 HOH 75  775  89  HOH HOH A . 
G 4 HOH 76  776  9   HOH HOH A . 
G 4 HOH 77  777  17  HOH HOH A . 
G 4 HOH 78  778  199 HOH HOH A . 
G 4 HOH 79  779  34  HOH HOH A . 
G 4 HOH 80  780  98  HOH HOH A . 
G 4 HOH 81  781  32  HOH HOH A . 
G 4 HOH 82  782  172 HOH HOH A . 
G 4 HOH 83  783  373 HOH HOH A . 
G 4 HOH 84  784  83  HOH HOH A . 
G 4 HOH 85  785  641 HOH HOH A . 
G 4 HOH 86  786  45  HOH HOH A . 
G 4 HOH 87  787  74  HOH HOH A . 
G 4 HOH 88  788  529 HOH HOH A . 
G 4 HOH 89  789  226 HOH HOH A . 
G 4 HOH 90  790  14  HOH HOH A . 
G 4 HOH 91  791  803 HOH HOH A . 
G 4 HOH 92  792  364 HOH HOH A . 
G 4 HOH 93  793  530 HOH HOH A . 
G 4 HOH 94  794  177 HOH HOH A . 
G 4 HOH 95  795  43  HOH HOH A . 
G 4 HOH 96  796  52  HOH HOH A . 
G 4 HOH 97  797  842 HOH HOH A . 
G 4 HOH 98  798  733 HOH HOH A . 
G 4 HOH 99  799  27  HOH HOH A . 
G 4 HOH 100 800  88  HOH HOH A . 
G 4 HOH 101 801  55  HOH HOH A . 
G 4 HOH 102 802  147 HOH HOH A . 
G 4 HOH 103 803  304 HOH HOH A . 
G 4 HOH 104 804  180 HOH HOH A . 
G 4 HOH 105 805  518 HOH HOH A . 
G 4 HOH 106 806  259 HOH HOH A . 
G 4 HOH 107 807  268 HOH HOH A . 
G 4 HOH 108 808  38  HOH HOH A . 
G 4 HOH 109 809  310 HOH HOH A . 
G 4 HOH 110 810  322 HOH HOH A . 
G 4 HOH 111 811  126 HOH HOH A . 
G 4 HOH 112 812  280 HOH HOH A . 
G 4 HOH 113 813  670 HOH HOH A . 
G 4 HOH 114 814  133 HOH HOH A . 
G 4 HOH 115 815  7   HOH HOH A . 
G 4 HOH 116 816  296 HOH HOH A . 
G 4 HOH 117 817  168 HOH HOH A . 
G 4 HOH 118 818  414 HOH HOH A . 
G 4 HOH 119 819  506 HOH HOH A . 
G 4 HOH 120 820  422 HOH HOH A . 
G 4 HOH 121 821  302 HOH HOH A . 
G 4 HOH 122 822  362 HOH HOH A . 
G 4 HOH 123 823  687 HOH HOH A . 
G 4 HOH 124 824  182 HOH HOH A . 
G 4 HOH 125 825  61  HOH HOH A . 
G 4 HOH 126 826  384 HOH HOH A . 
G 4 HOH 127 827  248 HOH HOH A . 
G 4 HOH 128 828  191 HOH HOH A . 
G 4 HOH 129 829  549 HOH HOH A . 
G 4 HOH 130 830  28  HOH HOH A . 
G 4 HOH 131 831  10  HOH HOH A . 
G 4 HOH 132 832  247 HOH HOH A . 
G 4 HOH 133 833  97  HOH HOH A . 
G 4 HOH 134 834  145 HOH HOH A . 
G 4 HOH 135 835  92  HOH HOH A . 
G 4 HOH 136 836  234 HOH HOH A . 
G 4 HOH 137 837  84  HOH HOH A . 
G 4 HOH 138 838  564 HOH HOH A . 
G 4 HOH 139 839  46  HOH HOH A . 
G 4 HOH 140 840  477 HOH HOH A . 
G 4 HOH 141 841  65  HOH HOH A . 
G 4 HOH 142 842  60  HOH HOH A . 
G 4 HOH 143 843  372 HOH HOH A . 
G 4 HOH 144 844  607 HOH HOH A . 
G 4 HOH 145 845  82  HOH HOH A . 
G 4 HOH 146 846  612 HOH HOH A . 
G 4 HOH 147 847  400 HOH HOH A . 
G 4 HOH 148 848  325 HOH HOH A . 
G 4 HOH 149 849  39  HOH HOH A . 
G 4 HOH 150 850  507 HOH HOH A . 
G 4 HOH 151 851  283 HOH HOH A . 
G 4 HOH 152 852  565 HOH HOH A . 
G 4 HOH 153 853  63  HOH HOH A . 
G 4 HOH 154 854  509 HOH HOH A . 
G 4 HOH 155 855  243 HOH HOH A . 
G 4 HOH 156 856  127 HOH HOH A . 
G 4 HOH 157 857  311 HOH HOH A . 
G 4 HOH 158 858  312 HOH HOH A . 
G 4 HOH 159 859  113 HOH HOH A . 
G 4 HOH 160 860  901 HOH HOH A . 
G 4 HOH 161 861  12  HOH HOH A . 
G 4 HOH 162 862  68  HOH HOH A . 
G 4 HOH 163 863  613 HOH HOH A . 
G 4 HOH 164 864  205 HOH HOH A . 
G 4 HOH 165 865  115 HOH HOH A . 
G 4 HOH 166 866  37  HOH HOH A . 
G 4 HOH 167 867  356 HOH HOH A . 
G 4 HOH 168 868  618 HOH HOH A . 
G 4 HOH 169 869  603 HOH HOH A . 
G 4 HOH 170 870  376 HOH HOH A . 
G 4 HOH 171 871  35  HOH HOH A . 
G 4 HOH 172 872  51  HOH HOH A . 
G 4 HOH 173 873  264 HOH HOH A . 
G 4 HOH 174 874  371 HOH HOH A . 
G 4 HOH 175 875  450 HOH HOH A . 
G 4 HOH 176 876  443 HOH HOH A . 
G 4 HOH 177 877  326 HOH HOH A . 
G 4 HOH 178 878  665 HOH HOH A . 
G 4 HOH 179 879  163 HOH HOH A . 
G 4 HOH 180 880  320 HOH HOH A . 
G 4 HOH 181 881  301 HOH HOH A . 
G 4 HOH 182 882  198 HOH HOH A . 
G 4 HOH 183 883  319 HOH HOH A . 
G 4 HOH 184 884  444 HOH HOH A . 
G 4 HOH 185 885  708 HOH HOH A . 
G 4 HOH 186 886  15  HOH HOH A . 
G 4 HOH 187 887  57  HOH HOH A . 
G 4 HOH 188 888  342 HOH HOH A . 
G 4 HOH 189 889  823 HOH HOH A . 
G 4 HOH 190 890  511 HOH HOH A . 
G 4 HOH 191 891  798 HOH HOH A . 
G 4 HOH 192 892  527 HOH HOH A . 
G 4 HOH 193 893  101 HOH HOH A . 
G 4 HOH 194 894  160 HOH HOH A . 
G 4 HOH 195 895  524 HOH HOH A . 
G 4 HOH 196 896  455 HOH HOH A . 
G 4 HOH 197 897  244 HOH HOH A . 
G 4 HOH 198 898  750 HOH HOH A . 
G 4 HOH 199 899  30  HOH HOH A . 
G 4 HOH 200 900  154 HOH HOH A . 
G 4 HOH 201 901  170 HOH HOH A . 
G 4 HOH 202 902  713 HOH HOH A . 
G 4 HOH 203 903  150 HOH HOH A . 
G 4 HOH 204 904  313 HOH HOH A . 
G 4 HOH 205 905  291 HOH HOH A . 
G 4 HOH 206 906  298 HOH HOH A . 
G 4 HOH 207 907  502 HOH HOH A . 
G 4 HOH 208 908  646 HOH HOH A . 
G 4 HOH 209 909  694 HOH HOH A . 
G 4 HOH 210 910  149 HOH HOH A . 
G 4 HOH 211 911  538 HOH HOH A . 
G 4 HOH 212 912  292 HOH HOH A . 
G 4 HOH 213 913  347 HOH HOH A . 
G 4 HOH 214 914  765 HOH HOH A . 
G 4 HOH 215 915  550 HOH HOH A . 
G 4 HOH 216 916  423 HOH HOH A . 
G 4 HOH 217 917  600 HOH HOH A . 
G 4 HOH 218 918  122 HOH HOH A . 
G 4 HOH 219 919  720 HOH HOH A . 
G 4 HOH 220 920  370 HOH HOH A . 
G 4 HOH 221 921  263 HOH HOH A . 
G 4 HOH 222 922  375 HOH HOH A . 
G 4 HOH 223 923  378 HOH HOH A . 
G 4 HOH 224 924  860 HOH HOH A . 
G 4 HOH 225 925  328 HOH HOH A . 
G 4 HOH 226 926  142 HOH HOH A . 
G 4 HOH 227 927  62  HOH HOH A . 
G 4 HOH 228 928  357 HOH HOH A . 
G 4 HOH 229 929  576 HOH HOH A . 
G 4 HOH 230 930  664 HOH HOH A . 
G 4 HOH 231 931  536 HOH HOH A . 
G 4 HOH 232 932  501 HOH HOH A . 
G 4 HOH 233 933  434 HOH HOH A . 
G 4 HOH 234 934  334 HOH HOH A . 
G 4 HOH 235 935  795 HOH HOH A . 
G 4 HOH 236 936  749 HOH HOH A . 
G 4 HOH 237 937  841 HOH HOH A . 
G 4 HOH 238 938  429 HOH HOH A . 
G 4 HOH 239 939  231 HOH HOH A . 
G 4 HOH 240 940  316 HOH HOH A . 
G 4 HOH 241 941  262 HOH HOH A . 
G 4 HOH 242 942  245 HOH HOH A . 
G 4 HOH 243 943  597 HOH HOH A . 
G 4 HOH 244 944  889 HOH HOH A . 
G 4 HOH 245 945  315 HOH HOH A . 
G 4 HOH 246 946  314 HOH HOH A . 
G 4 HOH 247 947  289 HOH HOH A . 
G 4 HOH 248 948  732 HOH HOH A . 
G 4 HOH 249 949  452 HOH HOH A . 
G 4 HOH 250 950  13  HOH HOH A . 
G 4 HOH 251 951  534 HOH HOH A . 
G 4 HOH 252 952  466 HOH HOH A . 
G 4 HOH 253 953  589 HOH HOH A . 
G 4 HOH 254 954  553 HOH HOH A . 
G 4 HOH 255 955  774 HOH HOH A . 
G 4 HOH 256 956  462 HOH HOH A . 
G 4 HOH 257 957  388 HOH HOH A . 
G 4 HOH 258 958  679 HOH HOH A . 
G 4 HOH 259 959  108 HOH HOH A . 
G 4 HOH 260 960  110 HOH HOH A . 
G 4 HOH 261 961  190 HOH HOH A . 
G 4 HOH 262 962  219 HOH HOH A . 
G 4 HOH 263 963  73  HOH HOH A . 
G 4 HOH 264 964  421 HOH HOH A . 
G 4 HOH 265 965  813 HOH HOH A . 
G 4 HOH 266 966  571 HOH HOH A . 
G 4 HOH 267 967  90  HOH HOH A . 
G 4 HOH 268 968  106 HOH HOH A . 
G 4 HOH 269 969  608 HOH HOH A . 
G 4 HOH 270 970  878 HOH HOH A . 
G 4 HOH 271 971  482 HOH HOH A . 
G 4 HOH 272 972  458 HOH HOH A . 
G 4 HOH 273 973  336 HOH HOH A . 
G 4 HOH 274 974  390 HOH HOH A . 
G 4 HOH 275 975  495 HOH HOH A . 
G 4 HOH 276 976  620 HOH HOH A . 
G 4 HOH 277 977  691 HOH HOH A . 
G 4 HOH 278 978  606 HOH HOH A . 
G 4 HOH 279 979  546 HOH HOH A . 
G 4 HOH 280 980  281 HOH HOH A . 
G 4 HOH 281 981  777 HOH HOH A . 
G 4 HOH 282 982  712 HOH HOH A . 
G 4 HOH 283 983  660 HOH HOH A . 
G 4 HOH 284 984  424 HOH HOH A . 
G 4 HOH 285 985  632 HOH HOH A . 
G 4 HOH 286 986  391 HOH HOH A . 
G 4 HOH 287 987  239 HOH HOH A . 
G 4 HOH 288 988  609 HOH HOH A . 
G 4 HOH 289 989  755 HOH HOH A . 
G 4 HOH 290 990  658 HOH HOH A . 
G 4 HOH 291 991  602 HOH HOH A . 
G 4 HOH 292 992  405 HOH HOH A . 
G 4 HOH 293 993  904 HOH HOH A . 
G 4 HOH 294 994  830 HOH HOH A . 
G 4 HOH 295 995  432 HOH HOH A . 
G 4 HOH 296 996  440 HOH HOH A . 
G 4 HOH 297 997  366 HOH HOH A . 
G 4 HOH 298 998  762 HOH HOH A . 
G 4 HOH 299 999  386 HOH HOH A . 
G 4 HOH 300 1000 555 HOH HOH A . 
G 4 HOH 301 1001 448 HOH HOH A . 
G 4 HOH 302 1002 76  HOH HOH A . 
G 4 HOH 303 1003 673 HOH HOH A . 
G 4 HOH 304 1004 343 HOH HOH A . 
G 4 HOH 305 1005 617 HOH HOH A . 
G 4 HOH 306 1006 605 HOH HOH A . 
G 4 HOH 307 1007 451 HOH HOH A . 
G 4 HOH 308 1008 476 HOH HOH A . 
G 4 HOH 309 1009 368 HOH HOH A . 
G 4 HOH 310 1010 520 HOH HOH A . 
G 4 HOH 311 1011 806 HOH HOH A . 
G 4 HOH 312 1012 532 HOH HOH A . 
G 4 HOH 313 1013 837 HOH HOH A . 
G 4 HOH 314 1014 840 HOH HOH A . 
G 4 HOH 315 1015 831 HOH HOH A . 
G 4 HOH 316 1016 785 HOH HOH A . 
G 4 HOH 317 1017 887 HOH HOH A . 
G 4 HOH 318 1018 491 HOH HOH A . 
G 4 HOH 319 1019 894 HOH HOH A . 
G 4 HOH 320 1020 788 HOH HOH A . 
G 4 HOH 321 1021 896 HOH HOH A . 
G 4 HOH 322 1022 801 HOH HOH A . 
G 4 HOH 323 1023 705 HOH HOH A . 
G 4 HOH 324 1024 871 HOH HOH A . 
G 4 HOH 325 1025 321 HOH HOH A . 
G 4 HOH 326 1026 438 HOH HOH A . 
G 4 HOH 327 1027 561 HOH HOH A . 
G 4 HOH 328 1028 595 HOH HOH A . 
G 4 HOH 329 1029 689 HOH HOH A . 
G 4 HOH 330 1030 521 HOH HOH A . 
G 4 HOH 331 1031 683 HOH HOH A . 
G 4 HOH 332 1032 461 HOH HOH A . 
G 4 HOH 333 1033 579 HOH HOH A . 
G 4 HOH 334 1034 854 HOH HOH A . 
G 4 HOH 335 1035 711 HOH HOH A . 
G 4 HOH 336 1036 637 HOH HOH A . 
G 4 HOH 337 1037 726 HOH HOH A . 
G 4 HOH 338 1038 500 HOH HOH A . 
G 4 HOH 339 1039 721 HOH HOH A . 
G 4 HOH 340 1040 449 HOH HOH A . 
G 4 HOH 341 1041 303 HOH HOH A . 
G 4 HOH 342 1042 230 HOH HOH A . 
G 4 HOH 343 1043 583 HOH HOH A . 
G 4 HOH 344 1044 189 HOH HOH A . 
G 4 HOH 345 1045 655 HOH HOH A . 
G 4 HOH 346 1046 846 HOH HOH A . 
G 4 HOH 347 1047 467 HOH HOH A . 
G 4 HOH 348 1048 667 HOH HOH A . 
G 4 HOH 349 1049 397 HOH HOH A . 
G 4 HOH 350 1050 661 HOH HOH A . 
G 4 HOH 351 1051 426 HOH HOH A . 
G 4 HOH 352 1052 129 HOH HOH A . 
G 4 HOH 353 1053 437 HOH HOH A . 
G 4 HOH 354 1054 425 HOH HOH A . 
G 4 HOH 355 1055 586 HOH HOH A . 
G 4 HOH 356 1056 717 HOH HOH A . 
G 4 HOH 357 1057 799 HOH HOH A . 
G 4 HOH 358 1058 454 HOH HOH A . 
G 4 HOH 359 1059 270 HOH HOH A . 
G 4 HOH 360 1060 261 HOH HOH A . 
G 4 HOH 361 1061 890 HOH HOH A . 
G 4 HOH 362 1062 590 HOH HOH A . 
G 4 HOH 363 1063 330 HOH HOH A . 
G 4 HOH 364 1064 528 HOH HOH A . 
G 4 HOH 365 1065 353 HOH HOH A . 
G 4 HOH 366 1066 821 HOH HOH A . 
G 4 HOH 367 1067 445 HOH HOH A . 
G 4 HOH 368 1068 351 HOH HOH A . 
G 4 HOH 369 1069 402 HOH HOH A . 
G 4 HOH 370 1070 427 HOH HOH A . 
G 4 HOH 371 1071 493 HOH HOH A . 
G 4 HOH 372 1072 832 HOH HOH A . 
G 4 HOH 373 1073 704 HOH HOH A . 
G 4 HOH 374 1074 881 HOH HOH A . 
G 4 HOH 375 1075 838 HOH HOH A . 
G 4 HOH 376 1076 584 HOH HOH A . 
G 4 HOH 377 1077 288 HOH HOH A . 
G 4 HOH 378 1078 628 HOH HOH A . 
G 4 HOH 379 1079 886 HOH HOH A . 
G 4 HOH 380 1080 643 HOH HOH A . 
G 4 HOH 381 1081 819 HOH HOH A . 
G 4 HOH 382 1082 898 HOH HOH A . 
G 4 HOH 383 1083 611 HOH HOH A . 
G 4 HOH 384 1084 475 HOH HOH A . 
G 4 HOH 385 1085 885 HOH HOH A . 
G 4 HOH 386 1086 282 HOH HOH A . 
G 4 HOH 387 1087 790 HOH HOH A . 
G 4 HOH 388 1088 492 HOH HOH A . 
G 4 HOH 389 1089 805 HOH HOH A . 
G 4 HOH 390 1090 862 HOH HOH A . 
G 4 HOH 391 1091 684 HOH HOH A . 
G 4 HOH 392 1092 178 HOH HOH A . 
G 4 HOH 393 1093 778 HOH HOH A . 
G 4 HOH 394 1094 787 HOH HOH A . 
G 4 HOH 395 1095 905 HOH HOH A . 
G 4 HOH 396 1096 591 HOH HOH A . 
G 4 HOH 397 1097 574 HOH HOH A . 
G 4 HOH 398 1098 484 HOH HOH A . 
G 4 HOH 399 1099 780 HOH HOH A . 
G 4 HOH 400 1100 699 HOH HOH A . 
G 4 HOH 401 1101 693 HOH HOH A . 
G 4 HOH 402 1102 899 HOH HOH A . 
G 4 HOH 403 1103 411 HOH HOH A . 
G 4 HOH 404 1104 131 HOH HOH A . 
G 4 HOH 405 1105 796 HOH HOH A . 
G 4 HOH 406 1106 741 HOH HOH A . 
G 4 HOH 407 1107 810 HOH HOH A . 
G 4 HOH 408 1108 745 HOH HOH A . 
G 4 HOH 409 1109 481 HOH HOH A . 
G 4 HOH 410 1110 469 HOH HOH A . 
G 4 HOH 411 1111 695 HOH HOH A . 
G 4 HOH 412 1112 874 HOH HOH A . 
G 4 HOH 413 1113 541 HOH HOH A . 
G 4 HOH 414 1114 826 HOH HOH A . 
G 4 HOH 415 1115 893 HOH HOH A . 
G 4 HOH 416 1116 497 HOH HOH A . 
G 4 HOH 417 1117 818 HOH HOH A . 
G 4 HOH 418 1118 804 HOH HOH A . 
H 4 HOH 1   701  598 HOH HOH B . 
H 4 HOH 2   702  525 HOH HOH B . 
H 4 HOH 3   703  861 HOH HOH B . 
H 4 HOH 4   704  470 HOH HOH B . 
H 4 HOH 5   705  399 HOH HOH B . 
H 4 HOH 6   706  766 HOH HOH B . 
H 4 HOH 7   707  852 HOH HOH B . 
H 4 HOH 8   708  839 HOH HOH B . 
H 4 HOH 9   709  895 HOH HOH B . 
H 4 HOH 10  710  822 HOH HOH B . 
H 4 HOH 11  711  355 HOH HOH B . 
H 4 HOH 12  712  212 HOH HOH B . 
H 4 HOH 13  713  627 HOH HOH B . 
H 4 HOH 14  714  902 HOH HOH B . 
H 4 HOH 15  715  625 HOH HOH B . 
H 4 HOH 16  716  41  HOH HOH B . 
H 4 HOH 17  717  345 HOH HOH B . 
H 4 HOH 18  718  439 HOH HOH B . 
H 4 HOH 19  719  407 HOH HOH B . 
H 4 HOH 20  720  577 HOH HOH B . 
H 4 HOH 21  721  707 HOH HOH B . 
H 4 HOH 22  722  112 HOH HOH B . 
H 4 HOH 23  723  757 HOH HOH B . 
H 4 HOH 24  724  642 HOH HOH B . 
H 4 HOH 25  725  381 HOH HOH B . 
H 4 HOH 26  726  412 HOH HOH B . 
H 4 HOH 27  727  70  HOH HOH B . 
H 4 HOH 28  728  203 HOH HOH B . 
H 4 HOH 29  729  81  HOH HOH B . 
H 4 HOH 30  730  763 HOH HOH B . 
H 4 HOH 31  731  563 HOH HOH B . 
H 4 HOH 32  732  250 HOH HOH B . 
H 4 HOH 33  733  877 HOH HOH B . 
H 4 HOH 34  734  537 HOH HOH B . 
H 4 HOH 35  735  144 HOH HOH B . 
H 4 HOH 36  736  157 HOH HOH B . 
H 4 HOH 37  737  254 HOH HOH B . 
H 4 HOH 38  738  338 HOH HOH B . 
H 4 HOH 39  739  460 HOH HOH B . 
H 4 HOH 40  740  836 HOH HOH B . 
H 4 HOH 41  741  639 HOH HOH B . 
H 4 HOH 42  742  24  HOH HOH B . 
H 4 HOH 43  743  633 HOH HOH B . 
H 4 HOH 44  744  341 HOH HOH B . 
H 4 HOH 45  745  513 HOH HOH B . 
H 4 HOH 46  746  42  HOH HOH B . 
H 4 HOH 47  747  164 HOH HOH B . 
H 4 HOH 48  748  114 HOH HOH B . 
H 4 HOH 49  749  94  HOH HOH B . 
H 4 HOH 50  750  729 HOH HOH B . 
H 4 HOH 51  751  238 HOH HOH B . 
H 4 HOH 52  752  623 HOH HOH B . 
H 4 HOH 53  753  870 HOH HOH B . 
H 4 HOH 54  754  671 HOH HOH B . 
H 4 HOH 55  755  285 HOH HOH B . 
H 4 HOH 56  756  696 HOH HOH B . 
H 4 HOH 57  757  99  HOH HOH B . 
H 4 HOH 58  758  308 HOH HOH B . 
H 4 HOH 59  759  25  HOH HOH B . 
H 4 HOH 60  760  395 HOH HOH B . 
H 4 HOH 61  761  100 HOH HOH B . 
H 4 HOH 62  762  130 HOH HOH B . 
H 4 HOH 63  763  11  HOH HOH B . 
H 4 HOH 64  764  271 HOH HOH B . 
H 4 HOH 65  765  75  HOH HOH B . 
H 4 HOH 66  766  728 HOH HOH B . 
H 4 HOH 67  767  324 HOH HOH B . 
H 4 HOH 68  768  235 HOH HOH B . 
H 4 HOH 69  769  207 HOH HOH B . 
H 4 HOH 70  770  406 HOH HOH B . 
H 4 HOH 71  771  36  HOH HOH B . 
H 4 HOH 72  772  676 HOH HOH B . 
H 4 HOH 73  773  218 HOH HOH B . 
H 4 HOH 74  774  146 HOH HOH B . 
H 4 HOH 75  775  66  HOH HOH B . 
H 4 HOH 76  776  233 HOH HOH B . 
H 4 HOH 77  777  754 HOH HOH B . 
H 4 HOH 78  778  363 HOH HOH B . 
H 4 HOH 79  779  249 HOH HOH B . 
H 4 HOH 80  780  428 HOH HOH B . 
H 4 HOH 81  781  50  HOH HOH B . 
H 4 HOH 82  782  193 HOH HOH B . 
H 4 HOH 83  783  350 HOH HOH B . 
H 4 HOH 84  784  416 HOH HOH B . 
H 4 HOH 85  785  601 HOH HOH B . 
H 4 HOH 86  786  47  HOH HOH B . 
H 4 HOH 87  787  225 HOH HOH B . 
H 4 HOH 88  788  339 HOH HOH B . 
H 4 HOH 89  789  49  HOH HOH B . 
H 4 HOH 90  790  155 HOH HOH B . 
H 4 HOH 91  791  4   HOH HOH B . 
H 4 HOH 92  792  256 HOH HOH B . 
H 4 HOH 93  793  834 HOH HOH B . 
H 4 HOH 94  794  143 HOH HOH B . 
H 4 HOH 95  795  273 HOH HOH B . 
H 4 HOH 96  796  21  HOH HOH B . 
H 4 HOH 97  797  23  HOH HOH B . 
H 4 HOH 98  798  19  HOH HOH B . 
H 4 HOH 99  799  294 HOH HOH B . 
H 4 HOH 100 800  615 HOH HOH B . 
H 4 HOH 101 801  714 HOH HOH B . 
H 4 HOH 102 802  413 HOH HOH B . 
H 4 HOH 103 803  179 HOH HOH B . 
H 4 HOH 104 804  588 HOH HOH B . 
H 4 HOH 105 805  167 HOH HOH B . 
H 4 HOH 106 806  566 HOH HOH B . 
H 4 HOH 107 807  158 HOH HOH B . 
H 4 HOH 108 808  228 HOH HOH B . 
H 4 HOH 109 809  128 HOH HOH B . 
H 4 HOH 110 810  120 HOH HOH B . 
H 4 HOH 111 811  26  HOH HOH B . 
H 4 HOH 112 812  252 HOH HOH B . 
H 4 HOH 113 813  159 HOH HOH B . 
H 4 HOH 114 814  354 HOH HOH B . 
H 4 HOH 115 815  872 HOH HOH B . 
H 4 HOH 116 816  278 HOH HOH B . 
H 4 HOH 117 817  221 HOH HOH B . 
H 4 HOH 118 818  195 HOH HOH B . 
H 4 HOH 119 819  91  HOH HOH B . 
H 4 HOH 120 820  69  HOH HOH B . 
H 4 HOH 121 821  544 HOH HOH B . 
H 4 HOH 122 822  556 HOH HOH B . 
H 4 HOH 123 823  187 HOH HOH B . 
H 4 HOH 124 824  109 HOH HOH B . 
H 4 HOH 125 825  123 HOH HOH B . 
H 4 HOH 126 826  8   HOH HOH B . 
H 4 HOH 127 827  358 HOH HOH B . 
H 4 HOH 128 828  499 HOH HOH B . 
H 4 HOH 129 829  496 HOH HOH B . 
H 4 HOH 130 830  329 HOH HOH B . 
H 4 HOH 131 831  227 HOH HOH B . 
H 4 HOH 132 832  77  HOH HOH B . 
H 4 HOH 133 833  18  HOH HOH B . 
H 4 HOH 134 834  5   HOH HOH B . 
H 4 HOH 135 835  209 HOH HOH B . 
H 4 HOH 136 836  490 HOH HOH B . 
H 4 HOH 137 837  656 HOH HOH B . 
H 4 HOH 138 838  332 HOH HOH B . 
H 4 HOH 139 839  44  HOH HOH B . 
H 4 HOH 140 840  567 HOH HOH B . 
H 4 HOH 141 841  105 HOH HOH B . 
H 4 HOH 142 842  200 HOH HOH B . 
H 4 HOH 143 843  224 HOH HOH B . 
H 4 HOH 144 844  295 HOH HOH B . 
H 4 HOH 145 845  659 HOH HOH B . 
H 4 HOH 146 846  141 HOH HOH B . 
H 4 HOH 147 847  241 HOH HOH B . 
H 4 HOH 148 848  258 HOH HOH B . 
H 4 HOH 149 849  868 HOH HOH B . 
H 4 HOH 150 850  652 HOH HOH B . 
H 4 HOH 151 851  166 HOH HOH B . 
H 4 HOH 152 852  318 HOH HOH B . 
H 4 HOH 153 853  165 HOH HOH B . 
H 4 HOH 154 854  236 HOH HOH B . 
H 4 HOH 155 855  171 HOH HOH B . 
H 4 HOH 156 856  253 HOH HOH B . 
H 4 HOH 157 857  31  HOH HOH B . 
H 4 HOH 158 858  385 HOH HOH B . 
H 4 HOH 159 859  367 HOH HOH B . 
H 4 HOH 160 860  138 HOH HOH B . 
H 4 HOH 161 861  456 HOH HOH B . 
H 4 HOH 162 862  616 HOH HOH B . 
H 4 HOH 163 863  418 HOH HOH B . 
H 4 HOH 164 864  237 HOH HOH B . 
H 4 HOH 165 865  29  HOH HOH B . 
H 4 HOH 166 866  201 HOH HOH B . 
H 4 HOH 167 867  104 HOH HOH B . 
H 4 HOH 168 868  504 HOH HOH B . 
H 4 HOH 169 869  124 HOH HOH B . 
H 4 HOH 170 870  286 HOH HOH B . 
H 4 HOH 171 871  56  HOH HOH B . 
H 4 HOH 172 872  78  HOH HOH B . 
H 4 HOH 173 873  293 HOH HOH B . 
H 4 HOH 174 874  277 HOH HOH B . 
H 4 HOH 175 875  95  HOH HOH B . 
H 4 HOH 176 876  6   HOH HOH B . 
H 4 HOH 177 877  197 HOH HOH B . 
H 4 HOH 178 878  825 HOH HOH B . 
H 4 HOH 179 879  20  HOH HOH B . 
H 4 HOH 180 880  116 HOH HOH B . 
H 4 HOH 181 881  459 HOH HOH B . 
H 4 HOH 182 882  568 HOH HOH B . 
H 4 HOH 183 883  137 HOH HOH B . 
H 4 HOH 184 884  446 HOH HOH B . 
H 4 HOH 185 885  161 HOH HOH B . 
H 4 HOH 186 886  503 HOH HOH B . 
H 4 HOH 187 887  791 HOH HOH B . 
H 4 HOH 188 888  153 HOH HOH B . 
H 4 HOH 189 889  551 HOH HOH B . 
H 4 HOH 190 890  22  HOH HOH B . 
H 4 HOH 191 891  463 HOH HOH B . 
H 4 HOH 192 892  117 HOH HOH B . 
H 4 HOH 193 893  184 HOH HOH B . 
H 4 HOH 194 894  48  HOH HOH B . 
H 4 HOH 195 895  779 HOH HOH B . 
H 4 HOH 196 896  359 HOH HOH B . 
H 4 HOH 197 897  383 HOH HOH B . 
H 4 HOH 198 898  760 HOH HOH B . 
H 4 HOH 199 899  570 HOH HOH B . 
H 4 HOH 200 900  650 HOH HOH B . 
H 4 HOH 201 901  697 HOH HOH B . 
H 4 HOH 202 902  102 HOH HOH B . 
H 4 HOH 203 903  647 HOH HOH B . 
H 4 HOH 204 904  169 HOH HOH B . 
H 4 HOH 205 905  572 HOH HOH B . 
H 4 HOH 206 906  389 HOH HOH B . 
H 4 HOH 207 907  220 HOH HOH B . 
H 4 HOH 208 908  323 HOH HOH B . 
H 4 HOH 209 909  457 HOH HOH B . 
H 4 HOH 210 910  674 HOH HOH B . 
H 4 HOH 211 911  211 HOH HOH B . 
H 4 HOH 212 912  403 HOH HOH B . 
H 4 HOH 213 913  121 HOH HOH B . 
H 4 HOH 214 914  410 HOH HOH B . 
H 4 HOH 215 915  587 HOH HOH B . 
H 4 HOH 216 916  802 HOH HOH B . 
H 4 HOH 217 917  483 HOH HOH B . 
H 4 HOH 218 918  349 HOH HOH B . 
H 4 HOH 219 919  176 HOH HOH B . 
H 4 HOH 220 920  58  HOH HOH B . 
H 4 HOH 221 921  151 HOH HOH B . 
H 4 HOH 222 922  175 HOH HOH B . 
H 4 HOH 223 923  139 HOH HOH B . 
H 4 HOH 224 924  419 HOH HOH B . 
H 4 HOH 225 925  494 HOH HOH B . 
H 4 HOH 226 926  125 HOH HOH B . 
H 4 HOH 227 927  441 HOH HOH B . 
H 4 HOH 228 928  208 HOH HOH B . 
H 4 HOH 229 929  680 HOH HOH B . 
H 4 HOH 230 930  690 HOH HOH B . 
H 4 HOH 231 931  379 HOH HOH B . 
H 4 HOH 232 932  59  HOH HOH B . 
H 4 HOH 233 933  417 HOH HOH B . 
H 4 HOH 234 934  87  HOH HOH B . 
H 4 HOH 235 935  599 HOH HOH B . 
H 4 HOH 236 936  135 HOH HOH B . 
H 4 HOH 237 937  72  HOH HOH B . 
H 4 HOH 238 938  465 HOH HOH B . 
H 4 HOH 239 939  517 HOH HOH B . 
H 4 HOH 240 940  134 HOH HOH B . 
H 4 HOH 241 941  67  HOH HOH B . 
H 4 HOH 242 942  214 HOH HOH B . 
H 4 HOH 243 943  735 HOH HOH B . 
H 4 HOH 244 944  855 HOH HOH B . 
H 4 HOH 245 945  40  HOH HOH B . 
H 4 HOH 246 946  217 HOH HOH B . 
H 4 HOH 247 947  181 HOH HOH B . 
H 4 HOH 248 948  393 HOH HOH B . 
H 4 HOH 249 949  16  HOH HOH B . 
H 4 HOH 250 950  487 HOH HOH B . 
H 4 HOH 251 951  824 HOH HOH B . 
H 4 HOH 252 952  815 HOH HOH B . 
H 4 HOH 253 953  242 HOH HOH B . 
H 4 HOH 254 954  279 HOH HOH B . 
H 4 HOH 255 955  79  HOH HOH B . 
H 4 HOH 256 956  657 HOH HOH B . 
H 4 HOH 257 957  851 HOH HOH B . 
H 4 HOH 258 958  797 HOH HOH B . 
H 4 HOH 259 959  433 HOH HOH B . 
H 4 HOH 260 960  756 HOH HOH B . 
H 4 HOH 261 961  365 HOH HOH B . 
H 4 HOH 262 962  71  HOH HOH B . 
H 4 HOH 263 963  723 HOH HOH B . 
H 4 HOH 264 964  53  HOH HOH B . 
H 4 HOH 265 965  700 HOH HOH B . 
H 4 HOH 266 966  888 HOH HOH B . 
H 4 HOH 267 967  739 HOH HOH B . 
H 4 HOH 268 968  174 HOH HOH B . 
H 4 HOH 269 969  604 HOH HOH B . 
H 4 HOH 270 970  431 HOH HOH B . 
H 4 HOH 271 971  409 HOH HOH B . 
H 4 HOH 272 972  352 HOH HOH B . 
H 4 HOH 273 973  223 HOH HOH B . 
H 4 HOH 274 974  360 HOH HOH B . 
H 4 HOH 275 975  335 HOH HOH B . 
H 4 HOH 276 976  435 HOH HOH B . 
H 4 HOH 277 977  768 HOH HOH B . 
H 4 HOH 278 978  265 HOH HOH B . 
H 4 HOH 279 979  382 HOH HOH B . 
H 4 HOH 280 980  593 HOH HOH B . 
H 4 HOH 281 981  204 HOH HOH B . 
H 4 HOH 282 982  186 HOH HOH B . 
H 4 HOH 283 983  740 HOH HOH B . 
H 4 HOH 284 984  194 HOH HOH B . 
H 4 HOH 285 985  478 HOH HOH B . 
H 4 HOH 286 986  192 HOH HOH B . 
H 4 HOH 287 987  814 HOH HOH B . 
H 4 HOH 288 988  275 HOH HOH B . 
H 4 HOH 289 989  634 HOH HOH B . 
H 4 HOH 290 990  202 HOH HOH B . 
H 4 HOH 291 991  480 HOH HOH B . 
H 4 HOH 292 992  622 HOH HOH B . 
H 4 HOH 293 993  554 HOH HOH B . 
H 4 HOH 294 994  148 HOH HOH B . 
H 4 HOH 295 995  685 HOH HOH B . 
H 4 HOH 296 996  635 HOH HOH B . 
H 4 HOH 297 997  709 HOH HOH B . 
H 4 HOH 298 998  672 HOH HOH B . 
H 4 HOH 299 999  867 HOH HOH B . 
H 4 HOH 300 1000 266 HOH HOH B . 
H 4 HOH 301 1001 543 HOH HOH B . 
H 4 HOH 302 1002 103 HOH HOH B . 
H 4 HOH 303 1003 858 HOH HOH B . 
H 4 HOH 304 1004 257 HOH HOH B . 
H 4 HOH 305 1005 361 HOH HOH B . 
H 4 HOH 306 1006 736 HOH HOH B . 
H 4 HOH 307 1007 300 HOH HOH B . 
H 4 HOH 308 1008 644 HOH HOH B . 
H 4 HOH 309 1009 594 HOH HOH B . 
H 4 HOH 310 1010 710 HOH HOH B . 
H 4 HOH 311 1011 267 HOH HOH B . 
H 4 HOH 312 1012 686 HOH HOH B . 
H 4 HOH 313 1013 64  HOH HOH B . 
H 4 HOH 314 1014 307 HOH HOH B . 
H 4 HOH 315 1015 196 HOH HOH B . 
H 4 HOH 316 1016 770 HOH HOH B . 
H 4 HOH 317 1017 80  HOH HOH B . 
H 4 HOH 318 1018 522 HOH HOH B . 
H 4 HOH 319 1019 793 HOH HOH B . 
H 4 HOH 320 1020 626 HOH HOH B . 
H 4 HOH 321 1021 882 HOH HOH B . 
H 4 HOH 322 1022 630 HOH HOH B . 
H 4 HOH 323 1023 523 HOH HOH B . 
H 4 HOH 324 1024 764 HOH HOH B . 
H 4 HOH 325 1025 654 HOH HOH B . 
H 4 HOH 326 1026 430 HOH HOH B . 
H 4 HOH 327 1027 471 HOH HOH B . 
H 4 HOH 328 1028 835 HOH HOH B . 
H 4 HOH 329 1029 531 HOH HOH B . 
H 4 HOH 330 1030 722 HOH HOH B . 
H 4 HOH 331 1031 140 HOH HOH B . 
H 4 HOH 332 1032 761 HOH HOH B . 
H 4 HOH 333 1033 619 HOH HOH B . 
H 4 HOH 334 1034 474 HOH HOH B . 
H 4 HOH 335 1035 498 HOH HOH B . 
H 4 HOH 336 1036 716 HOH HOH B . 
H 4 HOH 337 1037 869 HOH HOH B . 
H 4 HOH 338 1038 731 HOH HOH B . 
H 4 HOH 339 1039 751 HOH HOH B . 
H 4 HOH 340 1040 621 HOH HOH B . 
H 4 HOH 341 1041 678 HOH HOH B . 
H 4 HOH 342 1042 718 HOH HOH B . 
H 4 HOH 343 1043 629 HOH HOH B . 
H 4 HOH 344 1044 734 HOH HOH B . 
H 4 HOH 345 1045 585 HOH HOH B . 
H 4 HOH 346 1046 706 HOH HOH B . 
H 4 HOH 347 1047 702 HOH HOH B . 
H 4 HOH 348 1048 829 HOH HOH B . 
H 4 HOH 349 1049 552 HOH HOH B . 
H 4 HOH 350 1050 864 HOH HOH B . 
H 4 HOH 351 1051 581 HOH HOH B . 
H 4 HOH 352 1052 547 HOH HOH B . 
H 4 HOH 353 1053 681 HOH HOH B . 
H 4 HOH 354 1054 515 HOH HOH B . 
H 4 HOH 355 1055 715 HOH HOH B . 
H 4 HOH 356 1056 558 HOH HOH B . 
H 4 HOH 357 1057 653 HOH HOH B . 
H 4 HOH 358 1058 580 HOH HOH B . 
H 4 HOH 359 1059 744 HOH HOH B . 
H 4 HOH 360 1060 682 HOH HOH B . 
H 4 HOH 361 1061 610 HOH HOH B . 
H 4 HOH 362 1062 548 HOH HOH B . 
H 4 HOH 363 1063 648 HOH HOH B . 
H 4 HOH 364 1064 331 HOH HOH B . 
H 4 HOH 365 1065 401 HOH HOH B . 
H 4 HOH 366 1066 488 HOH HOH B . 
H 4 HOH 367 1067 519 HOH HOH B . 
H 4 HOH 368 1068 827 HOH HOH B . 
H 4 HOH 369 1069 337 HOH HOH B . 
H 4 HOH 370 1070 562 HOH HOH B . 
H 4 HOH 371 1071 472 HOH HOH B . 
H 4 HOH 372 1072 853 HOH HOH B . 
H 4 HOH 373 1073 727 HOH HOH B . 
H 4 HOH 374 1074 442 HOH HOH B . 
H 4 HOH 375 1075 645 HOH HOH B . 
H 4 HOH 376 1076 269 HOH HOH B . 
H 4 HOH 377 1077 539 HOH HOH B . 
H 4 HOH 378 1078 675 HOH HOH B . 
H 4 HOH 379 1079 545 HOH HOH B . 
H 4 HOH 380 1080 856 HOH HOH B . 
H 4 HOH 381 1081 640 HOH HOH B . 
H 4 HOH 382 1082 346 HOH HOH B . 
H 4 HOH 383 1083 327 HOH HOH B . 
H 4 HOH 384 1084 738 HOH HOH B . 
H 4 HOH 385 1085 636 HOH HOH B . 
H 4 HOH 386 1086 820 HOH HOH B . 
H 4 HOH 387 1087 812 HOH HOH B . 
H 4 HOH 388 1088 3   HOH HOH B . 
H 4 HOH 389 1089 479 HOH HOH B . 
H 4 HOH 390 1090 758 HOH HOH B . 
H 4 HOH 391 1091 344 HOH HOH B . 
H 4 HOH 392 1092 786 HOH HOH B . 
H 4 HOH 393 1093 730 HOH HOH B . 
H 4 HOH 394 1094 404 HOH HOH B . 
H 4 HOH 395 1095 800 HOH HOH B . 
H 4 HOH 396 1096 638 HOH HOH B . 
H 4 HOH 397 1097 392 HOH HOH B . 
H 4 HOH 398 1098 789 HOH HOH B . 
H 4 HOH 399 1099 512 HOH HOH B . 
H 4 HOH 400 1100 559 HOH HOH B . 
H 4 HOH 401 1101 776 HOH HOH B . 
H 4 HOH 402 1102 783 HOH HOH B . 
H 4 HOH 403 1103 828 HOH HOH B . 
H 4 HOH 404 1104 333 HOH HOH B . 
H 4 HOH 405 1105 662 HOH HOH B . 
H 4 HOH 406 1106 473 HOH HOH B . 
H 4 HOH 407 1107 408 HOH HOH B . 
H 4 HOH 408 1108 582 HOH HOH B . 
H 4 HOH 409 1109 508 HOH HOH B . 
H 4 HOH 410 1110 447 HOH HOH B . 
H 4 HOH 411 1111 782 HOH HOH B . 
H 4 HOH 412 1112 246 HOH HOH B . 
H 4 HOH 413 1113 557 HOH HOH B . 
H 4 HOH 414 1114 808 HOH HOH B . 
H 4 HOH 415 1115 396 HOH HOH B . 
H 4 HOH 416 1116 688 HOH HOH B . 
H 4 HOH 417 1117 811 HOH HOH B . 
H 4 HOH 418 1118 510 HOH HOH B . 
H 4 HOH 419 1119 374 HOH HOH B . 
H 4 HOH 420 1120 485 HOH HOH B . 
H 4 HOH 421 1121 573 HOH HOH B . 
H 4 HOH 422 1122 903 HOH HOH B . 
H 4 HOH 423 1123 884 HOH HOH B . 
H 4 HOH 424 1124 866 HOH HOH B . 
H 4 HOH 425 1125 677 HOH HOH B . 
H 4 HOH 426 1126 724 HOH HOH B . 
H 4 HOH 427 1127 668 HOH HOH B . 
H 4 HOH 428 1128 703 HOH HOH B . 
H 4 HOH 429 1129 287 HOH HOH B . 
H 4 HOH 430 1130 210 HOH HOH B . 
H 4 HOH 431 1131 752 HOH HOH B . 
H 4 HOH 432 1132 394 HOH HOH B . 
H 4 HOH 433 1133 592 HOH HOH B . 
H 4 HOH 434 1134 173 HOH HOH B . 
H 4 HOH 435 1135 845 HOH HOH B . 
H 4 HOH 436 1136 759 HOH HOH B . 
H 4 HOH 437 1137 865 HOH HOH B . 
H 4 HOH 438 1138 833 HOH HOH B . 
H 4 HOH 439 1139 415 HOH HOH B . 
H 4 HOH 440 1140 575 HOH HOH B . 
H 4 HOH 441 1141 468 HOH HOH B . 
H 4 HOH 442 1142 850 HOH HOH B . 
H 4 HOH 443 1143 649 HOH HOH B . 
H 4 HOH 444 1144 255 HOH HOH B . 
H 4 HOH 445 1145 900 HOH HOH B . 
H 4 HOH 446 1146 883 HOH HOH B . 
H 4 HOH 447 1147 560 HOH HOH B . 
H 4 HOH 448 1148 784 HOH HOH B . 
H 4 HOH 449 1149 879 HOH HOH B . 
H 4 HOH 450 1150 297 HOH HOH B . 
H 4 HOH 451 1151 748 HOH HOH B . 
H 4 HOH 452 1152 816 HOH HOH B . 
H 4 HOH 453 1153 542 HOH HOH B . 
H 4 HOH 454 1154 398 HOH HOH B . 
H 4 HOH 455 1155 807 HOH HOH B . 
H 4 HOH 456 1156 464 HOH HOH B . 
H 4 HOH 457 1157 272 HOH HOH B . 
H 4 HOH 458 1158 453 HOH HOH B . 
H 4 HOH 459 1159 880 HOH HOH B . 
H 4 HOH 460 1160 514 HOH HOH B . 
H 4 HOH 461 1161 725 HOH HOH B . 
H 4 HOH 462 1162 540 HOH HOH B . 
H 4 HOH 463 1163 794 HOH HOH B . 
H 4 HOH 464 1164 743 HOH HOH B . 
H 4 HOH 465 1165 569 HOH HOH B . 
H 4 HOH 466 1166 251 HOH HOH B . 
H 4 HOH 467 1167 876 HOH HOH B . 
H 4 HOH 468 1168 817 HOH HOH B . 
H 4 HOH 469 1169 436 HOH HOH B . 
H 4 HOH 470 1170 897 HOH HOH B . 
H 4 HOH 471 1171 701 HOH HOH B . 
H 4 HOH 472 1172 486 HOH HOH B . 
H 4 HOH 473 1173 737 HOH HOH B . 
H 4 HOH 474 1174 489 HOH HOH B . 
H 4 HOH 475 1175 863 HOH HOH B . 
H 4 HOH 476 1176 185 HOH HOH B . 
H 4 HOH 477 1177 747 HOH HOH B . 
H 4 HOH 478 1178 892 HOH HOH B . 
H 4 HOH 479 1179 809 HOH HOH B . 
H 4 HOH 480 1180 873 HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A ARG 186 ? CG  ? A ARG 200 CG  
2  1 Y 1 A ARG 186 ? CD  ? A ARG 200 CD  
3  1 Y 1 A ARG 186 ? NE  ? A ARG 200 NE  
4  1 Y 1 A ARG 186 ? CZ  ? A ARG 200 CZ  
5  1 Y 1 A ARG 186 ? NH1 ? A ARG 200 NH1 
6  1 Y 1 A ARG 186 ? NH2 ? A ARG 200 NH2 
7  1 Y 1 A HIS 187 ? CG  ? A HIS 201 CG  
8  1 Y 1 A HIS 187 ? ND1 ? A HIS 201 ND1 
9  1 Y 1 A HIS 187 ? CD2 ? A HIS 201 CD2 
10 1 Y 1 A HIS 187 ? CE1 ? A HIS 201 CE1 
11 1 Y 1 A HIS 187 ? NE2 ? A HIS 201 NE2 
12 1 Y 1 B ARG 186 ? CG  ? B ARG 200 CG  
13 1 Y 1 B ARG 186 ? CD  ? B ARG 200 CD  
14 1 Y 1 B ARG 186 ? NE  ? B ARG 200 NE  
15 1 Y 1 B ARG 186 ? CZ  ? B ARG 200 CZ  
16 1 Y 1 B ARG 186 ? NH1 ? B ARG 200 NH1 
17 1 Y 1 B ARG 186 ? NH2 ? B ARG 200 NH2 
18 1 Y 1 B HIS 187 ? CG  ? B HIS 201 CG  
19 1 Y 1 B HIS 187 ? ND1 ? B HIS 201 ND1 
20 1 Y 1 B HIS 187 ? CD2 ? B HIS 201 CD2 
21 1 Y 1 B HIS 187 ? CE1 ? B HIS 201 CE1 
22 1 Y 1 B HIS 187 ? NE2 ? B HIS 201 NE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? '(1.20.1_4487: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8ZK6 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     138.230 
_cell.length_a_esd                 ? 
_cell.length_b                     170.290 
_cell.length_b_esd                 ? 
_cell.length_c                     115.700 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        16 
_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                         8ZK6 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                20 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 2 2 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8ZK6 
_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             2.75 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          55.23 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_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    '0.1M calcium acetate, 0.1M sodium MES, pH 6.0, 13% PEG 400' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-12-30 
_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   0.979 
_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 BL19U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL19U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8ZK6 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.94 
_reflns.d_resolution_low                               78.68 
_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                                     100159 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.4 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.8 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.00 
_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                                0.179 
_reflns.pdbx_Rpim_I_all                                0.070 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       652693 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.995 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.164 
_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                                    1.94 
_reflns_shell.d_res_low                                     1.99 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           50727 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             7413 
_reflns_shell.percent_possible_obs                          100.0 
_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                               6.8 
_reflns_shell.pdbx_chi_squared                              0.86 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.6 
_reflns_shell.pdbx_Rrim_I_all                               1.361 
_reflns_shell.pdbx_Rpim_I_all                               0.517 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.658 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.258 
_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                                 8ZK6 
_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                            1.94 
_refine.ls_d_res_low                             78.68 
_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                     92221 
_refine.ls_number_reflns_R_free                  3832 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.41 
_refine.ls_percent_reflns_R_free                 1.99 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2086 
_refine.ls_R_factor_R_free                       0.2238 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2083 
_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                 23.86 
_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                            0.21 
_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                       1.94 
_refine_hist.d_res_low                        78.68 
_refine_hist.number_atoms_solvent             898 
_refine_hist.number_atoms_total               9196 
_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        8244 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         54 
_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 ? 8487 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.346 ? 1157 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 6.760 ? 1162 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.061 ? 1313 ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.009 ? 1499 ? 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' 1.94 1.96  . . 145 7028 99.00  . . . . 0.3078 . . . . . . . . . . . 0.2861 
'X-RAY DIFFRACTION' 1.96 1.99  . . 146 7059 99.00  . . . . 0.2973 . . . . . . . . . . . 0.3124 
'X-RAY DIFFRACTION' 1.99 2.02  . . 143 6978 99.00  . . . . 0.2994 . . . . . . . . . . . 0.3198 
'X-RAY DIFFRACTION' 2.02 2.05  . . 134 6173 88.00  . . . . 0.3816 . . . . . . . . . . . 0.3775 
'X-RAY DIFFRACTION' 2.05 2.08  . . 137 6771 95.00  . . . . 0.3676 . . . . . . . . . . . 0.4052 
'X-RAY DIFFRACTION' 2.08 2.11  . . 140 7015 99.00  . . . . 0.2744 . . . . . . . . . . . 0.2902 
'X-RAY DIFFRACTION' 2.11 2.14  . . 142 7011 99.00  . . . . 0.2629 . . . . . . . . . . . 0.2690 
'X-RAY DIFFRACTION' 2.14 2.18  . . 144 7058 99.00  . . . . 0.2594 . . . . . . . . . . . 0.2610 
'X-RAY DIFFRACTION' 2.18 2.22  . . 136 6794 96.00  . . . . 0.3677 . . . . . . . . . . . 0.3139 
'X-RAY DIFFRACTION' 2.22 2.26  . . 138 6742 95.00  . . . . 0.3668 . . . . . . . . . . . 0.4415 
'X-RAY DIFFRACTION' 2.26 2.31  . . 144 7099 99.00  . . . . 0.2242 . . . . . . . . . . . 0.2650 
'X-RAY DIFFRACTION' 2.31 2.36  . . 142 7021 99.00  . . . . 0.2212 . . . . . . . . . . . 0.2305 
'X-RAY DIFFRACTION' 2.36 2.41  . . 144 7044 99.00  . . . . 0.2111 . . . . . . . . . . . 0.2339 
'X-RAY DIFFRACTION' 2.41 2.48  . . 139 7054 100.00 . . . . 0.2070 . . . . . . . . . . . 0.2450 
'X-RAY DIFFRACTION' 2.48 2.54  . . 144 7047 99.00  . . . . 0.2057 . . . . . . . . . . . 0.2223 
'X-RAY DIFFRACTION' 2.54 2.62  . . 141 7098 99.00  . . . . 0.2088 . . . . . . . . . . . 0.2278 
'X-RAY DIFFRACTION' 2.62 2.70  . . 140 6933 98.00  . . . . 0.2384 . . . . . . . . . . . 0.2890 
'X-RAY DIFFRACTION' 2.70 2.80  . . 143 7024 100.00 . . . . 0.2016 . . . . . . . . . . . 0.2503 
'X-RAY DIFFRACTION' 2.80 2.91  . . 145 7087 100.00 . . . . 0.1890 . . . . . . . . . . . 0.2081 
'X-RAY DIFFRACTION' 2.91 3.04  . . 144 7070 100.00 . . . . 0.1815 . . . . . . . . . . . 0.1814 
'X-RAY DIFFRACTION' 3.04 3.20  . . 139 7068 100.00 . . . . 0.1735 . . . . . . . . . . . 0.1911 
'X-RAY DIFFRACTION' 3.20 3.40  . . 145 7016 99.00  . . . . 0.1758 . . . . . . . . . . . 0.2145 
'X-RAY DIFFRACTION' 3.40 3.67  . . 146 6992 99.00  . . . . 0.1639 . . . . . . . . . . . 0.1852 
'X-RAY DIFFRACTION' 3.67 4.04  . . 143 6967 99.00  . . . . 0.1646 . . . . . . . . . . . 0.1711 
'X-RAY DIFFRACTION' 4.04 4.62  . . 147 7090 100.00 . . . . 0.1367 . . . . . . . . . . . 0.1488 
'X-RAY DIFFRACTION' 4.62 5.82  . . 141 7081 100.00 . . . . 0.1626 . . . . . . . . . . . 0.1643 
'X-RAY DIFFRACTION' 5.82 78.68 . . 140 7069 100.00 . . . . 0.1774 . . . . . . . . . . . 0.1835 
# 
_struct.entry_id                     8ZK6 
_struct.title                        'Crystal structure of the Decarboxylase KDC4427 from Enterobacter sp. CGMCC 5087' 
_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        8ZK6 
_struct_keywords.text            'Decarboxylase, LYASE' 
_struct_keywords.pdbx_keywords   LYASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 2 ? 
F N N 3 ? 
G N N 4 ? 
H N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A2U3EYQ2_9ENTR 
_struct_ref.pdbx_db_accession          A0A2U3EYQ2 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MRTPYCVADYLLDRLTDCGADHLFGVPGDYNLQFLDHVIDSPDICWVGCANELNASYAADGYARCKGFAALLTTFGVGEL
SAMNGIAGSYAEHVPVLHIVGAPGTASQQRGELLHHTLGDGEFRHFYHMSEPITVAQAILTEQNACYEIDRVLTTMLRER
RPGYLMLPADVAKKAATPPVNALTLRHAHADSACLKAFRDAAENRLAMSKRTALLADFLVLRHGLKHALQKWVKDVPMAH
ATMLMGKGIFDERHVGFYGTYSGSASAGAVKEAIEGADTVLCIGTRFTDTLTAGFTHQLTPSQTIEVQPHASRVGDVWFT
GIPMLQAIETLVELCKQHVHDTPVPSSQSAMVYPQPDGSLTQDNFWKTLQTFIRPGDIILADQGTSAFGAIDLRLPADVN
FIVQPLWGSIGYTLAAAFGAQTACPNRRVIVLTGDGAAQLTIQELGSMLRDKQHPIILVLNNEGYTVERAIHGPEQRYND
IALWNWTQIPQALSLDPQAQCWRVSEAEQLADVLEKVAHHERLSLIEVMLPKADIPPLLGAITKALEARNSA
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8ZK6 A 15 ? 566 ? A0A2U3EYQ2 1 ? 552 ? 1 552 
2 1 8ZK6 B 15 ? 566 ? A0A2U3EYQ2 1 ? 552 ? 1 552 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8ZK6 MET A 1  ? UNP A0A2U3EYQ2 ? ? 'initiating methionine' -13 1  
1 8ZK6 GLY A 2  ? UNP A0A2U3EYQ2 ? ? 'expression tag'        -12 2  
1 8ZK6 SER A 3  ? UNP A0A2U3EYQ2 ? ? 'expression tag'        -11 3  
1 8ZK6 SER A 4  ? UNP A0A2U3EYQ2 ? ? 'expression tag'        -10 4  
1 8ZK6 HIS A 5  ? UNP A0A2U3EYQ2 ? ? 'expression tag'        -9  5  
1 8ZK6 HIS A 6  ? UNP A0A2U3EYQ2 ? ? 'expression tag'        -8  6  
1 8ZK6 HIS A 7  ? UNP A0A2U3EYQ2 ? ? 'expression tag'        -7  7  
1 8ZK6 HIS A 8  ? UNP A0A2U3EYQ2 ? ? 'expression tag'        -6  8  
1 8ZK6 HIS A 9  ? UNP A0A2U3EYQ2 ? ? 'expression tag'        -5  9  
1 8ZK6 HIS A 10 ? UNP A0A2U3EYQ2 ? ? 'expression tag'        -4  10 
1 8ZK6 SER A 11 ? UNP A0A2U3EYQ2 ? ? 'expression tag'        -3  11 
1 8ZK6 GLN A 12 ? UNP A0A2U3EYQ2 ? ? 'expression tag'        -2  12 
1 8ZK6 ASP A 13 ? UNP A0A2U3EYQ2 ? ? 'expression tag'        -1  13 
1 8ZK6 PRO A 14 ? UNP A0A2U3EYQ2 ? ? 'expression tag'        0   14 
2 8ZK6 MET B 1  ? UNP A0A2U3EYQ2 ? ? 'initiating methionine' -13 15 
2 8ZK6 GLY B 2  ? UNP A0A2U3EYQ2 ? ? 'expression tag'        -12 16 
2 8ZK6 SER B 3  ? UNP A0A2U3EYQ2 ? ? 'expression tag'        -11 17 
2 8ZK6 SER B 4  ? UNP A0A2U3EYQ2 ? ? 'expression tag'        -10 18 
2 8ZK6 HIS B 5  ? UNP A0A2U3EYQ2 ? ? 'expression tag'        -9  19 
2 8ZK6 HIS B 6  ? UNP A0A2U3EYQ2 ? ? 'expression tag'        -8  20 
2 8ZK6 HIS B 7  ? UNP A0A2U3EYQ2 ? ? 'expression tag'        -7  21 
2 8ZK6 HIS B 8  ? UNP A0A2U3EYQ2 ? ? 'expression tag'        -6  22 
2 8ZK6 HIS B 9  ? UNP A0A2U3EYQ2 ? ? 'expression tag'        -5  23 
2 8ZK6 HIS B 10 ? UNP A0A2U3EYQ2 ? ? 'expression tag'        -4  24 
2 8ZK6 SER B 11 ? UNP A0A2U3EYQ2 ? ? 'expression tag'        -3  25 
2 8ZK6 GLN B 12 ? UNP A0A2U3EYQ2 ? ? 'expression tag'        -2  26 
2 8ZK6 ASP B 13 ? UNP A0A2U3EYQ2 ? ? 'expression tag'        -1  27 
2 8ZK6 PRO B 14 ? UNP A0A2U3EYQ2 ? ? 'expression tag'        0   28 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 9430  ? 
1 MORE         -75   ? 
1 'SSA (A^2)'  34750 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H 
# 
_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 CYS A 20  ? CYS A 32  ? CYS A 6   CYS A 18  1 ? 13 
HELX_P HELX_P2  AA2 GLY A 42  ? TYR A 44  ? GLY A 28  TYR A 30  5 ? 3  
HELX_P HELX_P3  AA3 ASN A 45  ? SER A 55  ? ASN A 31  SER A 41  1 ? 11 
HELX_P HELX_P4  AA4 ASN A 65  ? GLY A 81  ? ASN A 51  GLY A 67  1 ? 17 
HELX_P HELX_P5  AA5 GLY A 90  ? ALA A 96  ? GLY A 76  ALA A 82  1 ? 7  
HELX_P HELX_P6  AA6 ALA A 96  ? GLU A 106 ? ALA A 82  GLU A 92  1 ? 11 
HELX_P HELX_P7  AA7 GLY A 118 ? ARG A 124 ? GLY A 104 ARG A 110 1 ? 7  
HELX_P HELX_P8  AA8 ARG A 138 ? SER A 144 ? ARG A 124 SER A 130 1 ? 7  
HELX_P HELX_P9  AA9 GLU A 145 ? THR A 148 ? GLU A 131 THR A 134 5 ? 4  
HELX_P HELX_P10 AB1 ASN A 158 ? ARG A 174 ? ASN A 144 ARG A 160 1 ? 17 
HELX_P HELX_P11 AB2 ALA A 183 ? LYS A 187 ? ALA A 169 LYS A 173 1 ? 5  
HELX_P HELX_P12 AB3 ASP A 205 ? MET A 222 ? ASP A 191 MET A 208 1 ? 18 
HELX_P HELX_P13 AB4 ASP A 231 ? HIS A 237 ? ASP A 217 HIS A 223 1 ? 7  
HELX_P HELX_P14 AB5 LEU A 239 ? VAL A 250 ? LEU A 225 VAL A 236 1 ? 12 
HELX_P HELX_P15 AB6 MET A 257 ? LYS A 261 ? MET A 243 LYS A 247 5 ? 5  
HELX_P HELX_P16 AB7 SER A 276 ? SER A 280 ? SER A 262 SER A 266 5 ? 5  
HELX_P HELX_P17 AB8 ALA A 281 ? GLY A 290 ? ALA A 267 GLY A 276 1 ? 10 
HELX_P HELX_P18 AB9 ASP A 303 ? ALA A 307 ? ASP A 289 ALA A 293 5 ? 5  
HELX_P HELX_P19 AC1 PRO A 337 ? VAL A 353 ? PRO A 323 VAL A 339 1 ? 17 
HELX_P HELX_P20 AC2 THR A 375 ? ILE A 387 ? THR A 361 ILE A 373 1 ? 13 
HELX_P HELX_P21 AC3 SER A 400 ? ILE A 405 ? SER A 386 ILE A 391 1 ? 6  
HELX_P HELX_P22 AC4 GLY A 425 ? CYS A 438 ? GLY A 411 CYS A 424 1 ? 14 
HELX_P HELX_P23 AC5 ASP A 449 ? LEU A 454 ? ASP A 435 LEU A 440 1 ? 6  
HELX_P HELX_P24 AC6 ILE A 456 ? ASP A 465 ? ILE A 442 ASP A 451 1 ? 10 
HELX_P HELX_P25 AC7 TYR A 479 ? HIS A 486 ? TYR A 465 HIS A 472 1 ? 8  
HELX_P HELX_P26 AC8 GLN A 490 ? ASP A 494 ? GLN A 476 ASP A 480 5 ? 5  
HELX_P HELX_P27 AC9 ASN A 499 ? THR A 501 ? ASN A 485 THR A 487 5 ? 3  
HELX_P HELX_P28 AD1 GLN A 502 ? LEU A 507 ? GLN A 488 LEU A 493 1 ? 6  
HELX_P HELX_P29 AD2 GLU A 520 ? VAL A 531 ? GLU A 506 VAL A 517 1 ? 12 
HELX_P HELX_P30 AD3 PRO A 550 ? THR A 557 ? PRO A 536 THR A 543 1 ? 8  
HELX_P HELX_P31 AD4 CYS B 20  ? CYS B 32  ? CYS B 6   CYS B 18  1 ? 13 
HELX_P HELX_P32 AD5 GLY B 42  ? TYR B 44  ? GLY B 28  TYR B 30  5 ? 3  
HELX_P HELX_P33 AD6 ASN B 45  ? SER B 55  ? ASN B 31  SER B 41  1 ? 11 
HELX_P HELX_P34 AD7 ASN B 65  ? GLY B 81  ? ASN B 51  GLY B 67  1 ? 17 
HELX_P HELX_P35 AD8 GLY B 90  ? ALA B 96  ? GLY B 76  ALA B 82  1 ? 7  
HELX_P HELX_P36 AD9 ALA B 96  ? GLU B 106 ? ALA B 82  GLU B 92  1 ? 11 
HELX_P HELX_P37 AE1 GLY B 118 ? ARG B 124 ? GLY B 104 ARG B 110 1 ? 7  
HELX_P HELX_P38 AE2 ARG B 138 ? SER B 144 ? ARG B 124 SER B 130 1 ? 7  
HELX_P HELX_P39 AE3 GLU B 145 ? THR B 148 ? GLU B 131 THR B 134 5 ? 4  
HELX_P HELX_P40 AE4 ASN B 158 ? ARG B 174 ? ASN B 144 ARG B 160 1 ? 17 
HELX_P HELX_P41 AE5 ALA B 183 ? LYS B 187 ? ALA B 169 LYS B 173 1 ? 5  
HELX_P HELX_P42 AE6 ASP B 205 ? ALA B 221 ? ASP B 191 ALA B 207 1 ? 17 
HELX_P HELX_P43 AE7 ASP B 231 ? HIS B 237 ? ASP B 217 HIS B 223 1 ? 7  
HELX_P HELX_P44 AE8 LEU B 239 ? VAL B 250 ? LEU B 225 VAL B 236 1 ? 12 
HELX_P HELX_P45 AE9 SER B 276 ? SER B 280 ? SER B 262 SER B 266 5 ? 5  
HELX_P HELX_P46 AF1 ALA B 281 ? GLU B 289 ? ALA B 267 GLU B 275 1 ? 9  
HELX_P HELX_P47 AF2 PRO B 337 ? GLN B 351 ? PRO B 323 GLN B 337 1 ? 15 
HELX_P HELX_P48 AF3 THR B 375 ? ILE B 387 ? THR B 361 ILE B 373 1 ? 13 
HELX_P HELX_P49 AF4 GLY B 398 ? ILE B 405 ? GLY B 384 ILE B 391 1 ? 8  
HELX_P HELX_P50 AF5 GLY B 425 ? CYS B 438 ? GLY B 411 CYS B 424 1 ? 14 
HELX_P HELX_P51 AF6 ASP B 449 ? LEU B 454 ? ASP B 435 LEU B 440 1 ? 6  
HELX_P HELX_P52 AF7 ILE B 456 ? ASP B 465 ? ILE B 442 ASP B 451 1 ? 10 
HELX_P HELX_P53 AF8 TYR B 479 ? HIS B 486 ? TYR B 465 HIS B 472 1 ? 8  
HELX_P HELX_P54 AF9 GLN B 490 ? ASP B 494 ? GLN B 476 ASP B 480 5 ? 5  
HELX_P HELX_P55 AG1 ASN B 499 ? THR B 501 ? ASN B 485 THR B 487 5 ? 3  
HELX_P HELX_P56 AG2 GLN B 502 ? LEU B 507 ? GLN B 488 LEU B 493 1 ? 6  
HELX_P HELX_P57 AG3 GLU B 520 ? ALA B 532 ? GLU B 506 ALA B 518 1 ? 13 
HELX_P HELX_P58 AG4 PRO B 550 ? THR B 557 ? PRO B 536 THR B 543 1 ? 8  
# 
_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 ASP 449 OD1 ? ? ? 1_555 D MG  . MG ? ? A ASP 435 A MG  602 1_555 ? ? ? ? ? ? ? 2.202 ? ? 
metalc2  metalc ? ? A ASN 476 OD1 ? ? ? 1_555 D MG  . MG ? ? A ASN 462 A MG  602 1_555 ? ? ? ? ? ? ? 2.337 ? ? 
metalc3  metalc ? ? A GLY 478 O   ? ? ? 1_555 D MG  . MG ? ? A GLY 464 A MG  602 1_555 ? ? ? ? ? ? ? 2.126 ? ? 
metalc4  metalc ? ? C TPP .   O2A ? ? ? 1_555 D MG  . MG ? ? A TPP 601 A MG  602 1_555 ? ? ? ? ? ? ? 2.282 ? ? 
metalc5  metalc ? ? C TPP .   O2B ? ? ? 1_555 D MG  . MG ? ? A TPP 601 A MG  602 1_555 ? ? ? ? ? ? ? 2.229 ? ? 
metalc6  metalc ? ? D MG  .   MG  ? ? ? 1_555 G HOH . O  ? ? A MG  602 A HOH 722 1_555 ? ? ? ? ? ? ? 1.873 ? ? 
metalc7  metalc ? ? B ASP 449 OD1 ? ? ? 1_555 F MG  . MG ? ? B ASP 435 B MG  602 1_555 ? ? ? ? ? ? ? 2.205 ? ? 
metalc8  metalc ? ? B ASN 476 OD1 ? ? ? 1_555 F MG  . MG ? ? B ASN 462 B MG  602 1_555 ? ? ? ? ? ? ? 1.984 ? ? 
metalc9  metalc ? ? B GLY 478 O   ? ? ? 1_555 F MG  . MG ? ? B GLY 464 B MG  602 1_555 ? ? ? ? ? ? ? 1.974 ? ? 
metalc10 metalc ? ? E TPP .   O2A ? ? ? 1_555 F MG  . MG ? ? B TPP 601 B MG  602 1_555 ? ? ? ? ? ? ? 2.299 ? ? 
metalc11 metalc ? ? E TPP .   O1B ? ? ? 1_555 F MG  . MG ? ? B TPP 601 B MG  602 1_555 ? ? ? ? ? ? ? 2.292 ? ? 
metalc12 metalc ? ? F MG  .   MG  ? ? ? 1_555 H HOH . O  ? ? B MG  602 B HOH 763 1_555 ? ? ? ? ? ? ? 2.530 ? ? 
# 
_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  OD1 ? A ASP 449 ? A ASP 435 ? 1_555 MG ? D MG . ? A MG 602 ? 1_555 OD1 ? A ASN 476 ? A ASN 462 ? 1_555 108.2 ? 
2  OD1 ? A ASP 449 ? A ASP 435 ? 1_555 MG ? D MG . ? A MG 602 ? 1_555 O   ? A GLY 478 ? A GLY 464 ? 1_555 104.0 ? 
3  OD1 ? A ASN 476 ? A ASN 462 ? 1_555 MG ? D MG . ? A MG 602 ? 1_555 O   ? A GLY 478 ? A GLY 464 ? 1_555 97.2  ? 
4  OD1 ? A ASP 449 ? A ASP 435 ? 1_555 MG ? D MG . ? A MG 602 ? 1_555 O2A ? C TPP .   ? A TPP 601 ? 1_555 78.2  ? 
5  OD1 ? A ASN 476 ? A ASN 462 ? 1_555 MG ? D MG . ? A MG 602 ? 1_555 O2A ? C TPP .   ? A TPP 601 ? 1_555 168.9 ? 
6  O   ? A GLY 478 ? A GLY 464 ? 1_555 MG ? D MG . ? A MG 602 ? 1_555 O2A ? C TPP .   ? A TPP 601 ? 1_555 89.8  ? 
7  OD1 ? A ASP 449 ? A ASP 435 ? 1_555 MG ? D MG . ? A MG 602 ? 1_555 O2B ? C TPP .   ? A TPP 601 ? 1_555 153.8 ? 
8  OD1 ? A ASN 476 ? A ASN 462 ? 1_555 MG ? D MG . ? A MG 602 ? 1_555 O2B ? C TPP .   ? A TPP 601 ? 1_555 91.1  ? 
9  O   ? A GLY 478 ? A GLY 464 ? 1_555 MG ? D MG . ? A MG 602 ? 1_555 O2B ? C TPP .   ? A TPP 601 ? 1_555 90.4  ? 
10 O2A ? C TPP .   ? A TPP 601 ? 1_555 MG ? D MG . ? A MG 602 ? 1_555 O2B ? C TPP .   ? A TPP 601 ? 1_555 80.1  ? 
11 OD1 ? A ASP 449 ? A ASP 435 ? 1_555 MG ? D MG . ? A MG 602 ? 1_555 O   ? G HOH .   ? A HOH 722 ? 1_555 72.3  ? 
12 OD1 ? A ASN 476 ? A ASN 462 ? 1_555 MG ? D MG . ? A MG 602 ? 1_555 O   ? G HOH .   ? A HOH 722 ? 1_555 95.8  ? 
13 O   ? A GLY 478 ? A GLY 464 ? 1_555 MG ? D MG . ? A MG 602 ? 1_555 O   ? G HOH .   ? A HOH 722 ? 1_555 167.0 ? 
14 O2A ? C TPP .   ? A TPP 601 ? 1_555 MG ? D MG . ? A MG 602 ? 1_555 O   ? G HOH .   ? A HOH 722 ? 1_555 77.3  ? 
15 O2B ? C TPP .   ? A TPP 601 ? 1_555 MG ? D MG . ? A MG 602 ? 1_555 O   ? G HOH .   ? A HOH 722 ? 1_555 88.7  ? 
16 OD1 ? B ASP 449 ? B ASP 435 ? 1_555 MG ? F MG . ? B MG 602 ? 1_555 OD1 ? B ASN 476 ? B ASN 462 ? 1_555 104.9 ? 
17 OD1 ? B ASP 449 ? B ASP 435 ? 1_555 MG ? F MG . ? B MG 602 ? 1_555 O   ? B GLY 478 ? B GLY 464 ? 1_555 111.0 ? 
18 OD1 ? B ASN 476 ? B ASN 462 ? 1_555 MG ? F MG . ? B MG 602 ? 1_555 O   ? B GLY 478 ? B GLY 464 ? 1_555 95.6  ? 
19 OD1 ? B ASP 449 ? B ASP 435 ? 1_555 MG ? F MG . ? B MG 602 ? 1_555 O2A ? E TPP .   ? B TPP 601 ? 1_555 79.2  ? 
20 OD1 ? B ASN 476 ? B ASN 462 ? 1_555 MG ? F MG . ? B MG 602 ? 1_555 O2A ? E TPP .   ? B TPP 601 ? 1_555 170.0 ? 
21 O   ? B GLY 478 ? B GLY 464 ? 1_555 MG ? F MG . ? B MG 602 ? 1_555 O2A ? E TPP .   ? B TPP 601 ? 1_555 91.3  ? 
22 OD1 ? B ASP 449 ? B ASP 435 ? 1_555 MG ? F MG . ? B MG 602 ? 1_555 O1B ? E TPP .   ? B TPP 601 ? 1_555 145.9 ? 
23 OD1 ? B ASN 476 ? B ASN 462 ? 1_555 MG ? F MG . ? B MG 602 ? 1_555 O1B ? E TPP .   ? B TPP 601 ? 1_555 92.0  ? 
24 O   ? B GLY 478 ? B GLY 464 ? 1_555 MG ? F MG . ? B MG 602 ? 1_555 O1B ? E TPP .   ? B TPP 601 ? 1_555 96.2  ? 
25 O2A ? E TPP .   ? B TPP 601 ? 1_555 MG ? F MG . ? B MG 602 ? 1_555 O1B ? E TPP .   ? B TPP 601 ? 1_555 80.0  ? 
26 OD1 ? B ASP 449 ? B ASP 435 ? 1_555 MG ? F MG . ? B MG 602 ? 1_555 O   ? H HOH .   ? B HOH 763 ? 1_555 74.2  ? 
27 OD1 ? B ASN 476 ? B ASN 462 ? 1_555 MG ? F MG . ? B MG 602 ? 1_555 O   ? H HOH .   ? B HOH 763 ? 1_555 92.8  ? 
28 O   ? B GLY 478 ? B GLY 464 ? 1_555 MG ? F MG . ? B MG 602 ? 1_555 O   ? H HOH .   ? B HOH 763 ? 1_555 168.5 ? 
29 O2A ? E TPP .   ? B TPP 601 ? 1_555 MG ? F MG . ? B MG 602 ? 1_555 O   ? H HOH .   ? B HOH 763 ? 1_555 79.4  ? 
30 O1B ? E TPP .   ? B TPP 601 ? 1_555 MG ? F MG . ? B MG 602 ? 1_555 O   ? H HOH .   ? B HOH 763 ? 1_555 75.6  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 6 ? 
AA3 ? 6 ? 
AA4 ? 6 ? 
AA5 ? 6 ? 
AA6 ? 6 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA3 4 5 ? parallel      
AA3 5 6 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? parallel      
AA4 3 4 ? parallel      
AA4 4 5 ? parallel      
AA4 5 6 ? parallel      
AA5 1 2 ? parallel      
AA5 2 3 ? parallel      
AA5 3 4 ? parallel      
AA5 4 5 ? anti-parallel 
AA5 5 6 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 2 3 ? parallel      
AA6 3 4 ? parallel      
AA6 4 5 ? parallel      
AA6 5 6 ? 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 CYS A 59  ? GLY A 62  ? CYS A 45  GLY A 48  
AA1 2 HIS A 36  ? GLY A 39  ? HIS A 22  GLY A 25  
AA1 3 ALA A 83  ? THR A 88  ? ALA A 69  THR A 74  
AA1 4 VAL A 110 ? ALA A 116 ? VAL A 96  ALA A 102 
AA1 5 GLY A 177 ? PRO A 182 ? GLY A 163 PRO A 168 
AA1 6 ALA A 150 ? ILE A 153 ? ALA A 136 ILE A 139 
AA2 1 ALA A 253 ? ALA A 255 ? ALA A 239 ALA A 241 
AA2 2 THR A 226 ? ALA A 230 ? THR A 212 ALA A 216 
AA2 3 THR A 293 ? ILE A 297 ? THR A 279 ILE A 283 
AA2 4 THR A 318 ? VAL A 321 ? THR A 304 VAL A 307 
AA2 5 ALA A 325 ? VAL A 328 ? ALA A 311 VAL A 314 
AA2 6 VAL A 331 ? THR A 334 ? VAL A 317 THR A 320 
AA3 1 ASN A 414 ? ILE A 416 ? ASN A 400 ILE A 402 
AA3 2 ILE A 392 ? ALA A 395 ? ILE A 378 ALA A 381 
AA3 3 VAL A 443 ? GLY A 448 ? VAL A 429 GLY A 434 
AA3 4 ILE A 470 ? ASN A 475 ? ILE A 456 ASN A 461 
AA3 5 LEU A 537 ? MET A 543 ? LEU A 523 MET A 529 
AA3 6 ALA A 513 ? VAL A 518 ? ALA A 499 VAL A 504 
AA4 1 CYS B 59  ? GLY B 62  ? CYS B 45  GLY B 48  
AA4 2 HIS B 36  ? GLY B 39  ? HIS B 22  GLY B 25  
AA4 3 ALA B 83  ? THR B 88  ? ALA B 69  THR B 74  
AA4 4 VAL B 110 ? ALA B 116 ? VAL B 96  ALA B 102 
AA4 5 GLY B 177 ? PRO B 182 ? GLY B 163 PRO B 168 
AA4 6 ALA B 150 ? ILE B 153 ? ALA B 136 ILE B 139 
AA5 1 HIS B 254 ? THR B 256 ? HIS B 240 THR B 242 
AA5 2 THR B 226 ? ALA B 230 ? THR B 212 ALA B 216 
AA5 3 THR B 293 ? ILE B 297 ? THR B 279 ILE B 283 
AA5 4 THR B 318 ? VAL B 321 ? THR B 304 VAL B 307 
AA5 5 ALA B 325 ? VAL B 328 ? ALA B 311 VAL B 314 
AA5 6 VAL B 331 ? THR B 334 ? VAL B 317 THR B 320 
AA6 1 ASN B 414 ? ILE B 416 ? ASN B 400 ILE B 402 
AA6 2 ILE B 392 ? ALA B 395 ? ILE B 378 ALA B 381 
AA6 3 VAL B 443 ? GLY B 448 ? VAL B 429 GLY B 434 
AA6 4 ILE B 470 ? ASN B 475 ? ILE B 456 ASN B 461 
AA6 5 LEU B 537 ? MET B 543 ? LEU B 523 MET B 529 
AA6 6 ALA B 513 ? VAL B 518 ? ALA B 499 VAL B 504 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O VAL A 61  ? O VAL A 47  N LEU A 37  ? N LEU A 23  
AA1 2 3 N PHE A 38  ? N PHE A 24  O LEU A 86  ? O LEU A 72  
AA1 3 4 N LEU A 85  ? N LEU A 71  O LEU A 111 ? O LEU A 97  
AA1 4 5 N VAL A 114 ? N VAL A 100 O LEU A 181 ? O LEU A 167 
AA1 5 6 O MET A 180 ? O MET A 166 N ALA A 152 ? N ALA A 138 
AA2 1 2 O ALA A 253 ? O ALA A 239 N LEU A 228 ? N LEU A 214 
AA2 2 3 N LEU A 229 ? N LEU A 215 O LEU A 295 ? O LEU A 281 
AA2 3 4 N CYS A 296 ? N CYS A 282 O ILE A 319 ? O ILE A 305 
AA2 4 5 N GLU A 320 ? N GLU A 306 O ARG A 327 ? O ARG A 313 
AA2 5 6 N SER A 326 ? N SER A 312 O PHE A 333 ? O PHE A 319 
AA3 1 2 O ILE A 416 ? O ILE A 402 N ILE A 393 ? N ILE A 379 
AA3 2 3 N LEU A 394 ? N LEU A 380 O LEU A 446 ? O LEU A 432 
AA3 3 4 N VAL A 445 ? N VAL A 431 O LEU A 472 ? O LEU A 458 
AA3 4 5 N ILE A 471 ? N ILE A 457 O ILE A 540 ? O ILE A 526 
AA3 5 6 O GLU A 541 ? O GLU A 527 N TRP A 516 ? N TRP A 502 
AA4 1 2 O VAL B 61  ? O VAL B 47  N LEU B 37  ? N LEU B 23  
AA4 2 3 N PHE B 38  ? N PHE B 24  O LEU B 86  ? O LEU B 72  
AA4 3 4 N LEU B 85  ? N LEU B 71  O LEU B 111 ? O LEU B 97  
AA4 4 5 N VAL B 114 ? N VAL B 100 O LEU B 181 ? O LEU B 167 
AA4 5 6 O MET B 180 ? O MET B 166 N ALA B 152 ? N ALA B 138 
AA5 1 2 O ALA B 255 ? O ALA B 241 N ALA B 230 ? N ALA B 216 
AA5 2 3 N LEU B 229 ? N LEU B 215 O LEU B 295 ? O LEU B 281 
AA5 3 4 N CYS B 296 ? N CYS B 282 O ILE B 319 ? O ILE B 305 
AA5 4 5 N GLU B 320 ? N GLU B 306 O ARG B 327 ? O ARG B 313 
AA5 5 6 N SER B 326 ? N SER B 312 O PHE B 333 ? O PHE B 319 
AA6 1 2 O ILE B 416 ? O ILE B 402 N ILE B 393 ? N ILE B 379 
AA6 2 3 N ILE B 392 ? N ILE B 378 O ILE B 444 ? O ILE B 430 
AA6 3 4 N VAL B 445 ? N VAL B 431 O LEU B 472 ? O LEU B 458 
AA6 4 5 N ILE B 471 ? N ILE B 457 O ILE B 540 ? O ILE B 526 
AA6 5 6 O GLU B 541 ? O GLU B 527 N TRP B 516 ? N TRP B 502 
# 
_pdbx_entry_details.entry_id                   8ZK6 
_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 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O   B HOH 785  ? ? O B HOH 851  ? ? 2.03 
2  1 CD  A ARG 549  ? ? O B HOH 712  ? ? 2.11 
3  1 OG1 A THR 371  ? ? O A HOH 701  ? ? 2.12 
4  1 OE1 B GLU 275  ? ? O B HOH 701  ? ? 2.12 
5  1 O   B HOH 1163 ? ? O B HOH 1179 ? ? 2.12 
6  1 OG1 B THR 371  ? ? O B HOH 702  ? ? 2.13 
7  1 O   B HOH 706  ? ? O B HOH 884  ? ? 2.13 
8  1 OD1 B ASP 512  ? ? O B HOH 703  ? ? 2.14 
9  1 O   B HOH 1081 ? ? O B HOH 1127 ? ? 2.14 
10 1 O   B HOH 1009 ? ? O B HOH 1108 ? ? 2.15 
11 1 O   B HOH 1058 ? ? O B HOH 1096 ? ? 2.15 
12 1 O   B HOH 708  ? ? O B HOH 1091 ? ? 2.15 
13 1 O   A HOH 724  ? ? O A HOH 885  ? ? 2.15 
14 1 O   B HOH 1099 ? ? O B HOH 1108 ? ? 2.16 
15 1 O   A PRO 345  ? ? O A HOH 702  ? ? 2.16 
16 1 O   A HOH 923  ? ? O A HOH 1042 ? ? 2.16 
17 1 O   B HOH 1057 ? ? O B HOH 1121 ? ? 2.17 
18 1 O   A HOH 1000 ? ? O A HOH 1066 ? ? 2.17 
19 1 O   A HOH 992  ? ? O A HOH 1086 ? ? 2.17 
20 1 O   A HOH 739  ? ? O A HOH 1090 ? ? 2.18 
21 1 O   A HOH 746  ? ? O A HOH 1077 ? ? 2.18 
22 1 NH1 A ARG 160  ? ? O A HOH 703  ? ? 2.19 
23 1 NZ  A LYS 516  ? ? O A HOH 704  ? ? 2.19 
24 1 O   B HOH 1021 ? ? O B HOH 1051 ? ? 2.19 
25 1 OE2 B GLU 329  ? ? O B HOH 704  ? ? 2.19 
26 1 OE2 A GLU 131  ? ? O A HOH 705  ? ? 2.19 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O A HOH 820 ? ? 1_555 O B HOH 738 ? ? 8_455 2.18 
2 1 O A HOH 724 ? ? 1_555 O B HOH 785 ? ? 6_555 2.18 
# 
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 SER A 262 ? ? -142.56 47.56   
2  1 ILE A 274 ? ? -96.82  -62.49  
3  1 ASP A 357 ? ? -89.49  -152.02 
4  1 THR A 385 ? ? -67.33  2.33    
5  1 ASP A 496 ? ? -152.83 71.24   
6  1 ALA A 545 ? ? -108.53 43.77   
7  1 LEU A 546 ? ? -131.66 -44.89  
8  1 ARG A 549 ? ? -97.57  -95.78  
9  1 ASN A 550 ? ? -78.88  39.31   
10 1 SER B 262 ? ? -141.70 45.91   
11 1 ILE B 274 ? ? -97.30  -62.66  
12 1 HIS B 338 ? ? -135.00 -100.53 
13 1 VAL B 339 ? ? 7.08    86.15   
14 1 ASP B 341 ? ? 110.29  96.74   
15 1 ASP B 357 ? ? -89.93  -156.72 
16 1 THR B 543 ? ? -97.58  47.34   
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 1110 ? G HOH . 
2 1 B HOH 715  ? H HOH . 
# 
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 27.8675 40.1357 -1.2872  0.2659 ? -0.0173 ? -0.0816 ? 0.2740 ? -0.0140 ? 0.2694 ? 1.8574 ? -0.9815 
? -0.8050 ? 1.4731 ? -0.7265 ? 2.0647 ? 0.0357  ? 0.2917  ? -0.3944 ? -0.1591 ? -0.1641 ? -0.0097 ? 0.3252  ? -0.1233 ? 0.2149  ? 
2 'X-RAY DIFFRACTION' ? refined 22.2244 61.0772 -34.9846 0.1476 ? 0.0064  ? 0.0129  ? 0.1827 ? 0.0227  ? 0.1652 ? 0.3233 ? 0.0432  
? 0.0953  ? 0.7006 ? -0.2754 ? 0.5228 ? -0.0186 ? 0.1027  ? 0.0679  ? -0.0332 ? -0.0331 ? -0.0832 ? -0.0601 ? 0.0717  ? 0.0561  ? 
3 'X-RAY DIFFRACTION' ? refined 33.9469 69.0220 -13.9040 0.1855 ? -0.0022 ? -0.0532 ? 0.1806 ? 0.0330  ? 0.2432 ? 1.3880 ? 0.4359  
? 0.1815  ? 0.8791 ? -0.1948 ? 1.5810 ? -0.0542 ? -0.0094 ? 0.2706  ? 0.0708  ? -0.0321 ? -0.0276 ? -0.2898 ? -0.0166 ? 0.0971  ? 
4 'X-RAY DIFFRACTION' ? refined 2.7401  62.4413 -9.2617  0.1946 ? 0.0168  ? 0.0060  ? 0.2043 ? -0.0080 ? 0.1580 ? 0.8420 ? -0.2071 
? 0.1858  ? 0.5175 ? 0.1862  ? 0.3390 ? 0.0037  ? -0.0935 ? 0.0581  ? 0.0762  ? -0.0458 ? 0.0655  ? -0.0425 ? -0.1071 ? 0.0365  ? 
5 'X-RAY DIFFRACTION' ? refined 3.6985  33.3807 0.1637   0.1871 ? -0.0128 ? 0.0124  ? 0.2077 ? 0.0413  ? 0.1526 ? 0.9951 ? 0.2765  
? 0.2896  ? 0.4996 ? -0.0478 ? 0.1706 ? 0.0269  ? -0.2282 ? -0.1978 ? 0.1156  ? -0.0145 ? -0.0448 ? 0.0500  ? -0.0464 ? -0.0133 ? 
# 
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 451 through 551 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 3 through 338 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 339 through 551 )
;
4 'X-RAY DIFFRACTION' 4 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 3 through 191 )
;
5 'X-RAY DIFFRACTION' 5 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 192 through 450 )
;
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1  1 O ? A HOH 1110 ? 5.82 . 
2  1 O ? A HOH 1111 ? 5.91 . 
3  1 O ? A HOH 1112 ? 5.95 . 
4  1 O ? A HOH 1113 ? 6.22 . 
5  1 O ? A HOH 1114 ? 6.31 . 
6  1 O ? A HOH 1115 ? 6.42 . 
7  1 O ? A HOH 1116 ? 7.08 . 
8  1 O ? A HOH 1117 ? 7.44 . 
9  1 O ? A HOH 1118 ? 8.50 . 
10 1 O ? B HOH 1177 ? 6.27 . 
11 1 O ? B HOH 1178 ? 6.51 . 
12 1 O ? B HOH 1179 ? 6.82 . 
13 1 O ? B HOH 1180 ? 7.41 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET -13 ? A MET 1   
2  1 Y 1 A GLY -12 ? A GLY 2   
3  1 Y 1 A SER -11 ? A SER 3   
4  1 Y 1 A SER -10 ? A SER 4   
5  1 Y 1 A HIS -9  ? A HIS 5   
6  1 Y 1 A HIS -8  ? A HIS 6   
7  1 Y 1 A HIS -7  ? A HIS 7   
8  1 Y 1 A HIS -6  ? A HIS 8   
9  1 Y 1 A HIS -5  ? A HIS 9   
10 1 Y 1 A HIS -4  ? A HIS 10  
11 1 Y 1 A SER -3  ? A SER 11  
12 1 Y 1 A GLN -2  ? A GLN 12  
13 1 Y 1 A ASP -1  ? A ASP 13  
14 1 Y 1 A PRO 0   ? A PRO 14  
15 1 Y 1 A MET 1   ? A MET 15  
16 1 Y 1 A ARG 2   ? A ARG 16  
17 1 Y 1 A SER 346 ? A SER 360 
18 1 Y 1 A SER 347 ? A SER 361 
19 1 Y 1 A GLN 348 ? A GLN 362 
20 1 Y 1 A SER 349 ? A SER 363 
21 1 Y 1 A ALA 350 ? A ALA 364 
22 1 Y 1 A MET 351 ? A MET 365 
23 1 Y 1 A VAL 352 ? A VAL 366 
24 1 Y 1 A TYR 353 ? A TYR 367 
25 1 Y 1 A PRO 354 ? A PRO 368 
26 1 Y 1 A GLN 355 ? A GLN 369 
27 1 Y 1 A ALA 552 ? A ALA 566 
28 1 Y 1 B MET -13 ? B MET 1   
29 1 Y 1 B GLY -12 ? B GLY 2   
30 1 Y 1 B SER -11 ? B SER 3   
31 1 Y 1 B SER -10 ? B SER 4   
32 1 Y 1 B HIS -9  ? B HIS 5   
33 1 Y 1 B HIS -8  ? B HIS 6   
34 1 Y 1 B HIS -7  ? B HIS 7   
35 1 Y 1 B HIS -6  ? B HIS 8   
36 1 Y 1 B HIS -5  ? B HIS 9   
37 1 Y 1 B HIS -4  ? B HIS 10  
38 1 Y 1 B SER -3  ? B SER 11  
39 1 Y 1 B GLN -2  ? B GLN 12  
40 1 Y 1 B ASP -1  ? B ASP 13  
41 1 Y 1 B PRO 0   ? B PRO 14  
42 1 Y 1 B MET 1   ? B MET 15  
43 1 Y 1 B ARG 2   ? B ARG 16  
44 1 Y 1 B VAL 344 ? B VAL 358 
45 1 Y 1 B PRO 345 ? B PRO 359 
46 1 Y 1 B SER 346 ? B SER 360 
47 1 Y 1 B SER 347 ? B SER 361 
48 1 Y 1 B GLN 348 ? B GLN 362 
49 1 Y 1 B SER 349 ? B SER 363 
50 1 Y 1 B ALA 350 ? B ALA 364 
51 1 Y 1 B MET 351 ? B MET 365 
52 1 Y 1 B VAL 352 ? B VAL 366 
53 1 Y 1 B TYR 353 ? B TYR 367 
54 1 Y 1 B PRO 354 ? B PRO 368 
55 1 Y 1 B GLN 355 ? B GLN 369 
56 1 Y 1 B ALA 552 ? B ALA 566 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N  N N 1   
ALA CA     C  N S 2   
ALA C      C  N N 3   
ALA O      O  N N 4   
ALA CB     C  N N 5   
ALA OXT    O  N N 6   
ALA H      H  N N 7   
ALA H2     H  N N 8   
ALA HA     H  N N 9   
ALA HB1    H  N N 10  
ALA HB2    H  N N 11  
ALA HB3    H  N N 12  
ALA HXT    H  N N 13  
ARG N      N  N N 14  
ARG CA     C  N S 15  
ARG C      C  N N 16  
ARG O      O  N N 17  
ARG CB     C  N N 18  
ARG CG     C  N N 19  
ARG CD     C  N N 20  
ARG NE     N  N N 21  
ARG CZ     C  N N 22  
ARG NH1    N  N N 23  
ARG NH2    N  N N 24  
ARG OXT    O  N N 25  
ARG H      H  N N 26  
ARG H2     H  N N 27  
ARG HA     H  N N 28  
ARG HB2    H  N N 29  
ARG HB3    H  N N 30  
ARG HG2    H  N N 31  
ARG HG3    H  N N 32  
ARG HD2    H  N N 33  
ARG HD3    H  N N 34  
ARG HE     H  N N 35  
ARG HH11   H  N N 36  
ARG HH12   H  N N 37  
ARG HH21   H  N N 38  
ARG HH22   H  N N 39  
ARG HXT    H  N N 40  
ASN N      N  N N 41  
ASN CA     C  N S 42  
ASN C      C  N N 43  
ASN O      O  N N 44  
ASN CB     C  N N 45  
ASN CG     C  N N 46  
ASN OD1    O  N N 47  
ASN ND2    N  N N 48  
ASN OXT    O  N N 49  
ASN H      H  N N 50  
ASN H2     H  N N 51  
ASN HA     H  N N 52  
ASN HB2    H  N N 53  
ASN HB3    H  N N 54  
ASN HD21   H  N N 55  
ASN HD22   H  N N 56  
ASN HXT    H  N N 57  
ASP N      N  N N 58  
ASP CA     C  N S 59  
ASP C      C  N N 60  
ASP O      O  N N 61  
ASP CB     C  N N 62  
ASP CG     C  N N 63  
ASP OD1    O  N N 64  
ASP OD2    O  N N 65  
ASP OXT    O  N N 66  
ASP H      H  N N 67  
ASP H2     H  N N 68  
ASP HA     H  N N 69  
ASP HB2    H  N N 70  
ASP HB3    H  N N 71  
ASP HD2    H  N N 72  
ASP HXT    H  N N 73  
CYS N      N  N N 74  
CYS CA     C  N R 75  
CYS C      C  N N 76  
CYS O      O  N N 77  
CYS CB     C  N N 78  
CYS SG     S  N N 79  
CYS OXT    O  N N 80  
CYS H      H  N N 81  
CYS H2     H  N N 82  
CYS HA     H  N N 83  
CYS HB2    H  N N 84  
CYS HB3    H  N N 85  
CYS HG     H  N N 86  
CYS HXT    H  N N 87  
GLN N      N  N N 88  
GLN CA     C  N S 89  
GLN C      C  N N 90  
GLN O      O  N N 91  
GLN CB     C  N N 92  
GLN CG     C  N N 93  
GLN CD     C  N N 94  
GLN OE1    O  N N 95  
GLN NE2    N  N N 96  
GLN OXT    O  N N 97  
GLN H      H  N N 98  
GLN H2     H  N N 99  
GLN HA     H  N N 100 
GLN HB2    H  N N 101 
GLN HB3    H  N N 102 
GLN HG2    H  N N 103 
GLN HG3    H  N N 104 
GLN HE21   H  N N 105 
GLN HE22   H  N N 106 
GLN HXT    H  N N 107 
GLU N      N  N N 108 
GLU CA     C  N S 109 
GLU C      C  N N 110 
GLU O      O  N N 111 
GLU CB     C  N N 112 
GLU CG     C  N N 113 
GLU CD     C  N N 114 
GLU OE1    O  N N 115 
GLU OE2    O  N N 116 
GLU OXT    O  N N 117 
GLU H      H  N N 118 
GLU H2     H  N N 119 
GLU HA     H  N N 120 
GLU HB2    H  N N 121 
GLU HB3    H  N N 122 
GLU HG2    H  N N 123 
GLU HG3    H  N N 124 
GLU HE2    H  N N 125 
GLU HXT    H  N N 126 
GLY N      N  N N 127 
GLY CA     C  N N 128 
GLY C      C  N N 129 
GLY O      O  N N 130 
GLY OXT    O  N N 131 
GLY H      H  N N 132 
GLY H2     H  N N 133 
GLY HA2    H  N N 134 
GLY HA3    H  N N 135 
GLY HXT    H  N N 136 
HIS N      N  N N 137 
HIS CA     C  N S 138 
HIS C      C  N N 139 
HIS O      O  N N 140 
HIS CB     C  N N 141 
HIS CG     C  Y N 142 
HIS ND1    N  Y N 143 
HIS CD2    C  Y N 144 
HIS CE1    C  Y N 145 
HIS NE2    N  Y N 146 
HIS OXT    O  N N 147 
HIS H      H  N N 148 
HIS H2     H  N N 149 
HIS HA     H  N N 150 
HIS HB2    H  N N 151 
HIS HB3    H  N N 152 
HIS HD1    H  N N 153 
HIS HD2    H  N N 154 
HIS HE1    H  N N 155 
HIS HE2    H  N N 156 
HIS HXT    H  N N 157 
HOH O      O  N N 158 
HOH H1     H  N N 159 
HOH H2     H  N N 160 
ILE N      N  N N 161 
ILE CA     C  N S 162 
ILE C      C  N N 163 
ILE O      O  N N 164 
ILE CB     C  N S 165 
ILE CG1    C  N N 166 
ILE CG2    C  N N 167 
ILE CD1    C  N N 168 
ILE OXT    O  N N 169 
ILE H      H  N N 170 
ILE H2     H  N N 171 
ILE HA     H  N N 172 
ILE HB     H  N N 173 
ILE HG12   H  N N 174 
ILE HG13   H  N N 175 
ILE HG21   H  N N 176 
ILE HG22   H  N N 177 
ILE HG23   H  N N 178 
ILE HD11   H  N N 179 
ILE HD12   H  N N 180 
ILE HD13   H  N N 181 
ILE HXT    H  N N 182 
LEU N      N  N N 183 
LEU CA     C  N S 184 
LEU C      C  N N 185 
LEU O      O  N N 186 
LEU CB     C  N N 187 
LEU CG     C  N N 188 
LEU CD1    C  N N 189 
LEU CD2    C  N N 190 
LEU OXT    O  N N 191 
LEU H      H  N N 192 
LEU H2     H  N N 193 
LEU HA     H  N N 194 
LEU HB2    H  N N 195 
LEU HB3    H  N N 196 
LEU HG     H  N N 197 
LEU HD11   H  N N 198 
LEU HD12   H  N N 199 
LEU HD13   H  N N 200 
LEU HD21   H  N N 201 
LEU HD22   H  N N 202 
LEU HD23   H  N N 203 
LEU HXT    H  N N 204 
LYS N      N  N N 205 
LYS CA     C  N S 206 
LYS C      C  N N 207 
LYS O      O  N N 208 
LYS CB     C  N N 209 
LYS CG     C  N N 210 
LYS CD     C  N N 211 
LYS CE     C  N N 212 
LYS NZ     N  N N 213 
LYS OXT    O  N N 214 
LYS H      H  N N 215 
LYS H2     H  N N 216 
LYS HA     H  N N 217 
LYS HB2    H  N N 218 
LYS HB3    H  N N 219 
LYS HG2    H  N N 220 
LYS HG3    H  N N 221 
LYS HD2    H  N N 222 
LYS HD3    H  N N 223 
LYS HE2    H  N N 224 
LYS HE3    H  N N 225 
LYS HZ1    H  N N 226 
LYS HZ2    H  N N 227 
LYS HZ3    H  N N 228 
LYS HXT    H  N N 229 
MET N      N  N N 230 
MET CA     C  N S 231 
MET C      C  N N 232 
MET O      O  N N 233 
MET CB     C  N N 234 
MET CG     C  N N 235 
MET SD     S  N N 236 
MET CE     C  N N 237 
MET OXT    O  N N 238 
MET H      H  N N 239 
MET H2     H  N N 240 
MET HA     H  N N 241 
MET HB2    H  N N 242 
MET HB3    H  N N 243 
MET HG2    H  N N 244 
MET HG3    H  N N 245 
MET HE1    H  N N 246 
MET HE2    H  N N 247 
MET HE3    H  N N 248 
MET HXT    H  N N 249 
MG  MG     MG N N 250 
PHE N      N  N N 251 
PHE CA     C  N S 252 
PHE C      C  N N 253 
PHE O      O  N N 254 
PHE CB     C  N N 255 
PHE CG     C  Y N 256 
PHE CD1    C  Y N 257 
PHE CD2    C  Y N 258 
PHE CE1    C  Y N 259 
PHE CE2    C  Y N 260 
PHE CZ     C  Y N 261 
PHE OXT    O  N N 262 
PHE H      H  N N 263 
PHE H2     H  N N 264 
PHE HA     H  N N 265 
PHE HB2    H  N N 266 
PHE HB3    H  N N 267 
PHE HD1    H  N N 268 
PHE HD2    H  N N 269 
PHE HE1    H  N N 270 
PHE HE2    H  N N 271 
PHE HZ     H  N N 272 
PHE HXT    H  N N 273 
PRO N      N  N N 274 
PRO CA     C  N S 275 
PRO C      C  N N 276 
PRO O      O  N N 277 
PRO CB     C  N N 278 
PRO CG     C  N N 279 
PRO CD     C  N N 280 
PRO OXT    O  N N 281 
PRO H      H  N N 282 
PRO HA     H  N N 283 
PRO HB2    H  N N 284 
PRO HB3    H  N N 285 
PRO HG2    H  N N 286 
PRO HG3    H  N N 287 
PRO HD2    H  N N 288 
PRO HD3    H  N N 289 
PRO HXT    H  N N 290 
SER N      N  N N 291 
SER CA     C  N S 292 
SER C      C  N N 293 
SER O      O  N N 294 
SER CB     C  N N 295 
SER OG     O  N N 296 
SER OXT    O  N N 297 
SER H      H  N N 298 
SER H2     H  N N 299 
SER HA     H  N N 300 
SER HB2    H  N N 301 
SER HB3    H  N N 302 
SER HG     H  N N 303 
SER HXT    H  N N 304 
THR N      N  N N 305 
THR CA     C  N S 306 
THR C      C  N N 307 
THR O      O  N N 308 
THR CB     C  N R 309 
THR OG1    O  N N 310 
THR CG2    C  N N 311 
THR OXT    O  N N 312 
THR H      H  N N 313 
THR H2     H  N N 314 
THR HA     H  N N 315 
THR HB     H  N N 316 
THR HG1    H  N N 317 
THR HG21   H  N N 318 
THR HG22   H  N N 319 
THR HG23   H  N N 320 
THR HXT    H  N N 321 
TPP "N1'"  N  Y N 322 
TPP "C2'"  C  Y N 323 
TPP CM2    C  N N 324 
TPP "N3'"  N  Y N 325 
TPP "C4'"  C  Y N 326 
TPP "N4'"  N  N N 327 
TPP "C5'"  C  Y N 328 
TPP "C6'"  C  Y N 329 
TPP "C7'"  C  N N 330 
TPP N3     N  Y N 331 
TPP C2     C  Y N 332 
TPP S1     S  Y N 333 
TPP C5     C  Y N 334 
TPP C4     C  Y N 335 
TPP CM4    C  N N 336 
TPP C6     C  N N 337 
TPP C7     C  N N 338 
TPP O7     O  N N 339 
TPP PA     P  N S 340 
TPP O1A    O  N N 341 
TPP O2A    O  N N 342 
TPP O3A    O  N N 343 
TPP PB     P  N N 344 
TPP O1B    O  N N 345 
TPP O2B    O  N N 346 
TPP O3B    O  N N 347 
TPP HM21   H  N N 348 
TPP HM22   H  N N 349 
TPP HM23   H  N N 350 
TPP HN41   H  N N 351 
TPP HN42   H  N N 352 
TPP "H6'"  H  N N 353 
TPP "H7'1" H  N N 354 
TPP "H7'2" H  N N 355 
TPP H2     H  N N 356 
TPP HM41   H  N N 357 
TPP HM42   H  N N 358 
TPP HM43   H  N N 359 
TPP H61    H  N N 360 
TPP H62    H  N N 361 
TPP H71    H  N N 362 
TPP H72    H  N N 363 
TPP HOA2   H  N N 364 
TPP HOB2   H  N N 365 
TPP HOB3   H  N N 366 
TRP N      N  N N 367 
TRP CA     C  N S 368 
TRP C      C  N N 369 
TRP O      O  N N 370 
TRP CB     C  N N 371 
TRP CG     C  Y N 372 
TRP CD1    C  Y N 373 
TRP CD2    C  Y N 374 
TRP NE1    N  Y N 375 
TRP CE2    C  Y N 376 
TRP CE3    C  Y N 377 
TRP CZ2    C  Y N 378 
TRP CZ3    C  Y N 379 
TRP CH2    C  Y N 380 
TRP OXT    O  N N 381 
TRP H      H  N N 382 
TRP H2     H  N N 383 
TRP HA     H  N N 384 
TRP HB2    H  N N 385 
TRP HB3    H  N N 386 
TRP HD1    H  N N 387 
TRP HE1    H  N N 388 
TRP HE3    H  N N 389 
TRP HZ2    H  N N 390 
TRP HZ3    H  N N 391 
TRP HH2    H  N N 392 
TRP HXT    H  N N 393 
TYR N      N  N N 394 
TYR CA     C  N S 395 
TYR C      C  N N 396 
TYR O      O  N N 397 
TYR CB     C  N N 398 
TYR CG     C  Y N 399 
TYR CD1    C  Y N 400 
TYR CD2    C  Y N 401 
TYR CE1    C  Y N 402 
TYR CE2    C  Y N 403 
TYR CZ     C  Y N 404 
TYR OH     O  N N 405 
TYR OXT    O  N N 406 
TYR H      H  N N 407 
TYR H2     H  N N 408 
TYR HA     H  N N 409 
TYR HB2    H  N N 410 
TYR HB3    H  N N 411 
TYR HD1    H  N N 412 
TYR HD2    H  N N 413 
TYR HE1    H  N N 414 
TYR HE2    H  N N 415 
TYR HH     H  N N 416 
TYR HXT    H  N N 417 
VAL N      N  N N 418 
VAL CA     C  N S 419 
VAL C      C  N N 420 
VAL O      O  N N 421 
VAL CB     C  N N 422 
VAL CG1    C  N N 423 
VAL CG2    C  N N 424 
VAL OXT    O  N N 425 
VAL H      H  N N 426 
VAL H2     H  N N 427 
VAL HA     H  N N 428 
VAL HB     H  N N 429 
VAL HG11   H  N N 430 
VAL HG12   H  N N 431 
VAL HG13   H  N N 432 
VAL HG21   H  N N 433 
VAL HG22   H  N N 434 
VAL HG23   H  N N 435 
VAL HXT    H  N N 436 
# 
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 
TPP "N1'" "C2'"  doub Y N 306 
TPP "N1'" "C6'"  sing Y N 307 
TPP "C2'" CM2    sing N N 308 
TPP "C2'" "N3'"  sing Y N 309 
TPP CM2   HM21   sing N N 310 
TPP CM2   HM22   sing N N 311 
TPP CM2   HM23   sing N N 312 
TPP "N3'" "C4'"  doub Y N 313 
TPP "C4'" "N4'"  sing N N 314 
TPP "C4'" "C5'"  sing Y N 315 
TPP "N4'" HN41   sing N N 316 
TPP "N4'" HN42   sing N N 317 
TPP "C5'" "C6'"  doub Y N 318 
TPP "C5'" "C7'"  sing N N 319 
TPP "C6'" "H6'"  sing N N 320 
TPP "C7'" N3     sing N N 321 
TPP "C7'" "H7'1" sing N N 322 
TPP "C7'" "H7'2" sing N N 323 
TPP N3    C2     doub Y N 324 
TPP N3    C4     sing Y N 325 
TPP C2    S1     sing Y N 326 
TPP C2    H2     sing N N 327 
TPP S1    C5     sing Y N 328 
TPP C5    C4     doub Y N 329 
TPP C5    C6     sing N N 330 
TPP C4    CM4    sing N N 331 
TPP CM4   HM41   sing N N 332 
TPP CM4   HM42   sing N N 333 
TPP CM4   HM43   sing N N 334 
TPP C6    C7     sing N N 335 
TPP C6    H61    sing N N 336 
TPP C6    H62    sing N N 337 
TPP C7    O7     sing N N 338 
TPP C7    H71    sing N N 339 
TPP C7    H72    sing N N 340 
TPP O7    PA     sing N N 341 
TPP PA    O1A    doub N N 342 
TPP PA    O2A    sing N N 343 
TPP PA    O3A    sing N N 344 
TPP O2A   HOA2   sing N N 345 
TPP O3A   PB     sing N N 346 
TPP PB    O1B    doub N N 347 
TPP PB    O2B    sing N N 348 
TPP PB    O3B    sing N N 349 
TPP O2B   HOB2   sing N N 350 
TPP O3B   HOB3   sing N N 351 
TRP N     CA     sing N N 352 
TRP N     H      sing N N 353 
TRP N     H2     sing N N 354 
TRP CA    C      sing N N 355 
TRP CA    CB     sing N N 356 
TRP CA    HA     sing N N 357 
TRP C     O      doub N N 358 
TRP C     OXT    sing N N 359 
TRP CB    CG     sing N N 360 
TRP CB    HB2    sing N N 361 
TRP CB    HB3    sing N N 362 
TRP CG    CD1    doub Y N 363 
TRP CG    CD2    sing Y N 364 
TRP CD1   NE1    sing Y N 365 
TRP CD1   HD1    sing N N 366 
TRP CD2   CE2    doub Y N 367 
TRP CD2   CE3    sing Y N 368 
TRP NE1   CE2    sing Y N 369 
TRP NE1   HE1    sing N N 370 
TRP CE2   CZ2    sing Y N 371 
TRP CE3   CZ3    doub Y N 372 
TRP CE3   HE3    sing N N 373 
TRP CZ2   CH2    doub Y N 374 
TRP CZ2   HZ2    sing N N 375 
TRP CZ3   CH2    sing Y N 376 
TRP CZ3   HZ3    sing N N 377 
TRP CH2   HH2    sing N N 378 
TRP OXT   HXT    sing N N 379 
TYR N     CA     sing N N 380 
TYR N     H      sing N N 381 
TYR N     H2     sing N N 382 
TYR CA    C      sing N N 383 
TYR CA    CB     sing N N 384 
TYR CA    HA     sing N N 385 
TYR C     O      doub N N 386 
TYR C     OXT    sing N N 387 
TYR CB    CG     sing N N 388 
TYR CB    HB2    sing N N 389 
TYR CB    HB3    sing N N 390 
TYR CG    CD1    doub Y N 391 
TYR CG    CD2    sing Y N 392 
TYR CD1   CE1    sing Y N 393 
TYR CD1   HD1    sing N N 394 
TYR CD2   CE2    doub Y N 395 
TYR CD2   HD2    sing N N 396 
TYR CE1   CZ     doub Y N 397 
TYR CE1   HE1    sing N N 398 
TYR CE2   CZ     sing Y N 399 
TYR CE2   HE2    sing N N 400 
TYR CZ    OH     sing N N 401 
TYR OH    HH     sing N N 402 
TYR OXT   HXT    sing N N 403 
VAL N     CA     sing N N 404 
VAL N     H      sing N N 405 
VAL N     H2     sing N N 406 
VAL CA    C      sing N N 407 
VAL CA    CB     sing N N 408 
VAL CA    HA     sing N N 409 
VAL C     O      doub N N 410 
VAL C     OXT    sing N N 411 
VAL CB    CG1    sing N N 412 
VAL CB    CG2    sing N N 413 
VAL CB    HB     sing N N 414 
VAL CG1   HG11   sing N N 415 
VAL CG1   HG12   sing N N 416 
VAL CG1   HG13   sing N N 417 
VAL CG2   HG21   sing N N 418 
VAL CG2   HG22   sing N N 419 
VAL CG2   HG23   sing N N 420 
VAL OXT   HXT    sing N N 421 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           32171203 
_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   1VOM 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8ZK6 
_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]   0.007234 
_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]   0.005872 
_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]   0.008643 
_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  
MG 
N  
O  
P  
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     . THR A 1 17  ? 0.990   82.296 1.328   1.00 77.03  ? 3    THR A N     1 
ATOM   2    C  CA    . THR A 1 17  ? 0.901   80.861 1.074   1.00 66.23  ? 3    THR A CA    1 
ATOM   3    C  C     . THR A 1 17  ? -0.535  80.324 1.075   1.00 57.43  ? 3    THR A C     1 
ATOM   4    O  O     . THR A 1 17  ? -0.871  79.452 1.881   1.00 56.03  ? 3    THR A O     1 
ATOM   5    C  CB    . THR A 1 17  ? 1.711   80.077 2.122   1.00 69.72  ? 3    THR A CB    1 
ATOM   6    O  OG1   . THR A 1 17  ? 1.441   80.612 3.428   1.00 73.57  ? 3    THR A OG1   1 
ATOM   7    C  CG2   . THR A 1 17  ? 3.205   80.159 1.824   1.00 68.81  ? 3    THR A CG2   1 
ATOM   8    N  N     . PRO A 1 18  ? -1.382  80.831 0.178   1.00 52.94  ? 4    PRO A N     1 
ATOM   9    C  CA    . PRO A 1 18  ? -2.741  80.283 0.078   1.00 48.44  ? 4    PRO A CA    1 
ATOM   10   C  C     . PRO A 1 18  ? -2.707  78.822 -0.352  1.00 39.83  ? 4    PRO A C     1 
ATOM   11   O  O     . PRO A 1 18  ? -1.838  78.394 -1.112  1.00 40.00  ? 4    PRO A O     1 
ATOM   12   C  CB    . PRO A 1 18  ? -3.423  81.170 -0.976  1.00 45.59  ? 4    PRO A CB    1 
ATOM   13   C  CG    . PRO A 1 18  ? -2.417  82.199 -1.391  1.00 48.73  ? 4    PRO A CG    1 
ATOM   14   C  CD    . PRO A 1 18  ? -1.072  81.763 -0.920  1.00 50.16  ? 4    PRO A CD    1 
ATOM   15   N  N     . TYR A 1 19  ? -3.662  78.055 0.165   1.00 38.03  ? 5    TYR A N     1 
ATOM   16   C  CA    . TYR A 1 19  ? -3.752  76.633 -0.138  1.00 31.69  ? 5    TYR A CA    1 
ATOM   17   C  C     . TYR A 1 19  ? -3.994  76.423 -1.630  1.00 30.65  ? 5    TYR A C     1 
ATOM   18   O  O     . TYR A 1 19  ? -4.886  77.042 -2.218  1.00 29.14  ? 5    TYR A O     1 
ATOM   19   C  CB    . TYR A 1 19  ? -4.878  76.022 0.691   1.00 30.29  ? 5    TYR A CB    1 
ATOM   20   C  CG    . TYR A 1 19  ? -4.948  74.518 0.689   1.00 30.26  ? 5    TYR A CG    1 
ATOM   21   C  CD1   . TYR A 1 19  ? -5.648  73.834 -0.311  1.00 27.41  ? 5    TYR A CD1   1 
ATOM   22   C  CD2   . TYR A 1 19  ? -4.332  73.776 1.698   1.00 26.94  ? 5    TYR A CD2   1 
ATOM   23   C  CE1   . TYR A 1 19  ? -5.733  72.456 -0.304  1.00 26.49  ? 5    TYR A CE1   1 
ATOM   24   C  CE2   . TYR A 1 19  ? -4.402  72.400 1.704   1.00 27.67  ? 5    TYR A CE2   1 
ATOM   25   C  CZ    . TYR A 1 19  ? -5.104  71.746 0.704   1.00 26.72  ? 5    TYR A CZ    1 
ATOM   26   O  OH    . TYR A 1 19  ? -5.177  70.373 0.724   1.00 26.91  ? 5    TYR A OH    1 
ATOM   27   N  N     . CYS A 1 20  ? -3.211  75.531 -2.241  1.00 28.55  ? 6    CYS A N     1 
ATOM   28   C  CA    . CYS A 1 20  ? -3.229  75.374 -3.691  1.00 28.51  ? 6    CYS A CA    1 
ATOM   29   C  C     . CYS A 1 20  ? -3.131  73.901 -4.053  1.00 24.65  ? 6    CYS A C     1 
ATOM   30   O  O     . CYS A 1 20  ? -2.998  73.031 -3.190  1.00 25.32  ? 6    CYS A O     1 
ATOM   31   C  CB    . CYS A 1 20  ? -2.088  76.159 -4.354  1.00 27.34  ? 6    CYS A CB    1 
ATOM   32   S  SG    . CYS A 1 20  ? -0.425  75.691 -3.805  1.00 30.55  ? 6    CYS A SG    1 
ATOM   33   N  N     . VAL A 1 21  ? -3.151  73.644 -5.363  1.00 24.94  ? 7    VAL A N     1 
ATOM   34   C  CA    . VAL A 1 21  ? -3.157  72.280 -5.884  1.00 24.21  ? 7    VAL A CA    1 
ATOM   35   C  C     . VAL A 1 21  ? -2.004  71.474 -5.307  1.00 21.89  ? 7    VAL A C     1 
ATOM   36   O  O     . VAL A 1 21  ? -2.169  70.306 -4.938  1.00 22.15  ? 7    VAL A O     1 
ATOM   37   C  CB    . VAL A 1 21  ? -3.107  72.308 -7.424  1.00 22.61  ? 7    VAL A CB    1 
ATOM   38   C  CG1   . VAL A 1 21  ? -2.824  70.925 -7.981  1.00 21.36  ? 7    VAL A CG1   1 
ATOM   39   C  CG2   . VAL A 1 21  ? -4.396  72.874 -7.985  1.00 22.87  ? 7    VAL A CG2   1 
ATOM   40   N  N     . ALA A 1 22  ? -0.822  72.086 -5.210  1.00 23.04  ? 8    ALA A N     1 
ATOM   41   C  CA    . ALA A 1 22  ? 0.318   71.408 -4.596  1.00 24.59  ? 8    ALA A CA    1 
ATOM   42   C  C     . ALA A 1 22  ? -0.033  70.898 -3.197  1.00 24.63  ? 8    ALA A C     1 
ATOM   43   O  O     . ALA A 1 22  ? 0.248   69.744 -2.852  1.00 23.75  ? 8    ALA A O     1 
ATOM   44   C  CB    . ALA A 1 22  ? 1.519   72.353 -4.541  1.00 23.66  ? 8    ALA A CB    1 
ATOM   45   N  N     . ASP A 1 23  ? -0.693  71.737 -2.396  1.00 24.70  ? 9    ASP A N     1 
ATOM   46   C  CA    . ASP A 1 23  ? -1.063  71.345 -1.034  1.00 26.20  ? 9    ASP A CA    1 
ATOM   47   C  C     . ASP A 1 23  ? -2.129  70.256 -1.022  1.00 25.85  ? 9    ASP A C     1 
ATOM   48   O  O     . ASP A 1 23  ? -2.078  69.340 -0.191  1.00 25.59  ? 9    ASP A O     1 
ATOM   49   C  CB    . ASP A 1 23  ? -1.558  72.563 -0.267  1.00 26.61  ? 9    ASP A CB    1 
ATOM   50   C  CG    . ASP A 1 23  ? -0.584  73.701 -0.316  1.00 26.97  ? 9    ASP A CG    1 
ATOM   51   O  OD1   . ASP A 1 23  ? 0.616   73.467 -0.035  1.00 29.46  ? 9    ASP A OD1   1 
ATOM   52   O  OD2   . ASP A 1 23  ? -1.017  74.815 -0.658  1.00 27.28  ? 9    ASP A OD2   1 
ATOM   53   N  N     . TYR A 1 24  ? -3.117  70.358 -1.914  1.00 24.90  ? 10   TYR A N     1 
ATOM   54   C  CA    . TYR A 1 24  ? -4.153  69.331 -2.008  1.00 24.48  ? 10   TYR A CA    1 
ATOM   55   C  C     . TYR A 1 24  ? -3.552  67.973 -2.341  1.00 25.17  ? 10   TYR A C     1 
ATOM   56   O  O     . TYR A 1 24  ? -3.932  66.954 -1.746  1.00 25.21  ? 10   TYR A O     1 
ATOM   57   C  CB    . TYR A 1 24  ? -5.188  69.741 -3.057  1.00 23.04  ? 10   TYR A CB    1 
ATOM   58   C  CG    . TYR A 1 24  ? -6.394  68.835 -3.173  1.00 24.71  ? 10   TYR A CG    1 
ATOM   59   C  CD1   . TYR A 1 24  ? -6.360  67.700 -3.989  1.00 25.77  ? 10   TYR A CD1   1 
ATOM   60   C  CD2   . TYR A 1 24  ? -7.576  69.119 -2.493  1.00 25.33  ? 10   TYR A CD2   1 
ATOM   61   C  CE1   . TYR A 1 24  ? -7.463  66.871 -4.100  1.00 23.73  ? 10   TYR A CE1   1 
ATOM   62   C  CE2   . TYR A 1 24  ? -8.690  68.299 -2.613  1.00 25.54  ? 10   TYR A CE2   1 
ATOM   63   C  CZ    . TYR A 1 24  ? -8.621  67.176 -3.416  1.00 26.11  ? 10   TYR A CZ    1 
ATOM   64   O  OH    . TYR A 1 24  ? -9.719  66.354 -3.545  1.00 26.46  ? 10   TYR A OH    1 
ATOM   65   N  N     . LEU A 1 25  ? -2.603  67.937 -3.284  1.00 22.83  ? 11   LEU A N     1 
ATOM   66   C  CA    . LEU A 1 25  ? -1.959  66.675 -3.627  1.00 22.43  ? 11   LEU A CA    1 
ATOM   67   C  C     . LEU A 1 25  ? -1.238  66.091 -2.424  1.00 23.79  ? 11   LEU A C     1 
ATOM   68   O  O     . LEU A 1 25  ? -1.359  64.893 -2.139  1.00 22.59  ? 11   LEU A O     1 
ATOM   69   C  CB    . LEU A 1 25  ? -0.990  66.884 -4.798  1.00 21.50  ? 11   LEU A CB    1 
ATOM   70   C  CG    . LEU A 1 25  ? -0.101  65.721 -5.253  1.00 20.99  ? 11   LEU A CG    1 
ATOM   71   C  CD1   . LEU A 1 25  ? -0.903  64.446 -5.485  1.00 19.45  ? 11   LEU A CD1   1 
ATOM   72   C  CD2   . LEU A 1 25  ? 0.719   66.092 -6.501  1.00 20.09  ? 11   LEU A CD2   1 
ATOM   73   N  N     . LEU A 1 26  ? -0.518  66.933 -1.675  1.00 24.34  ? 12   LEU A N     1 
ATOM   74   C  CA    . LEU A 1 26  ? 0.197   66.447 -0.498  1.00 25.13  ? 12   LEU A CA    1 
ATOM   75   C  C     . LEU A 1 26  ? -0.765  65.944 0.576   1.00 27.24  ? 12   LEU A C     1 
ATOM   76   O  O     . LEU A 1 26  ? -0.483  64.944 1.252   1.00 26.73  ? 12   LEU A O     1 
ATOM   77   C  CB    . LEU A 1 26  ? 1.108   67.545 0.053   1.00 23.85  ? 12   LEU A CB    1 
ATOM   78   C  CG    . LEU A 1 26  ? 2.250   67.963 -0.891  1.00 27.39  ? 12   LEU A CG    1 
ATOM   79   C  CD1   . LEU A 1 26  ? 2.983   69.192 -0.355  1.00 27.84  ? 12   LEU A CD1   1 
ATOM   80   C  CD2   . LEU A 1 26  ? 3.227   66.812 -1.137  1.00 23.14  ? 12   LEU A CD2   1 
ATOM   81   N  N     . ASP A 1 27  ? -1.889  66.636 0.770   1.00 25.74  ? 13   ASP A N     1 
ATOM   82   C  CA    . ASP A 1 27  ? -2.894  66.155 1.712   1.00 27.61  ? 13   ASP A CA    1 
ATOM   83   C  C     . ASP A 1 27  ? -3.426  64.786 1.295   1.00 28.30  ? 13   ASP A C     1 
ATOM   84   O  O     . ASP A 1 27  ? -3.627  63.900 2.138   1.00 27.02  ? 13   ASP A O     1 
ATOM   85   C  CB    . ASP A 1 27  ? -4.019  67.182 1.842   1.00 27.77  ? 13   ASP A CB    1 
ATOM   86   C  CG    . ASP A 1 27  ? -3.716  68.245 2.901   1.00 30.76  ? 13   ASP A CG    1 
ATOM   87   O  OD1   . ASP A 1 27  ? -2.921  67.973 3.813   1.00 32.75  ? 13   ASP A OD1   1 
ATOM   88   O  OD2   . ASP A 1 27  ? -4.256  69.362 2.820   1.00 32.13  ? 13   ASP A OD2   1 
ATOM   89   N  N     . ARG A 1 28  ? -3.662  64.591 -0.004  1.00 25.93  ? 14   ARG A N     1 
ATOM   90   C  CA    . ARG A 1 28  ? -4.165  63.304 -0.470  1.00 26.46  ? 14   ARG A CA    1 
ATOM   91   C  C     . ARG A 1 28  ? -3.106  62.217 -0.327  1.00 26.77  ? 14   ARG A C     1 
ATOM   92   O  O     . ARG A 1 28  ? -3.440  61.054 -0.070  1.00 28.58  ? 14   ARG A O     1 
ATOM   93   C  CB    . ARG A 1 28  ? -4.621  63.422 -1.923  1.00 24.54  ? 14   ARG A CB    1 
ATOM   94   C  CG    . ARG A 1 28  ? -5.850  64.253 -2.114  1.00 25.05  ? 14   ARG A CG    1 
ATOM   95   C  CD    . ARG A 1 28  ? -6.869  63.958 -1.039  1.00 26.72  ? 14   ARG A CD    1 
ATOM   96   N  NE    . ARG A 1 28  ? -8.227  64.035 -1.561  1.00 28.09  ? 14   ARG A NE    1 
ATOM   97   C  CZ    . ARG A 1 28  ? -9.317  64.063 -0.810  1.00 29.27  ? 14   ARG A CZ    1 
ATOM   98   N  NH1   . ARG A 1 28  ? -9.247  64.058 0.512   1.00 29.73  ? 14   ARG A NH1   1 
ATOM   99   N  NH2   . ARG A 1 28  ? -10.508 64.105 -1.401  1.00 29.55  ? 14   ARG A NH2   1 
ATOM   100  N  N     . LEU A 1 29  ? -1.832  62.584 -0.479  1.00 26.22  ? 15   LEU A N     1 
ATOM   101  C  CA    . LEU A 1 29  ? -0.735  61.652 -0.230  1.00 27.23  ? 15   LEU A CA    1 
ATOM   102  C  C     . LEU A 1 29  ? -0.777  61.111 1.194   1.00 28.87  ? 15   LEU A C     1 
ATOM   103  O  O     . LEU A 1 29  ? -0.625  59.903 1.412   1.00 27.80  ? 15   LEU A O     1 
ATOM   104  C  CB    . LEU A 1 29  ? 0.601   62.352 -0.470  1.00 29.44  ? 15   LEU A CB    1 
ATOM   105  C  CG    . LEU A 1 29  ? 1.361   62.026 -1.744  1.00 27.39  ? 15   LEU A CG    1 
ATOM   106  C  CD1   . LEU A 1 29  ? 0.416   62.162 -2.909  1.00 26.83  ? 15   LEU A CD1   1 
ATOM   107  C  CD2   . LEU A 1 29  ? 2.542   62.972 -1.877  1.00 26.07  ? 15   LEU A CD2   1 
ATOM   108  N  N     . THR A 1 30  ? -0.956  61.998 2.186   1.00 28.84  ? 16   THR A N     1 
ATOM   109  C  CA    . THR A 1 30  ? -1.029  61.537 3.571   1.00 29.06  ? 16   THR A CA    1 
ATOM   110  C  C     . THR A 1 30  ? -2.227  60.626 3.789   1.00 30.51  ? 16   THR A C     1 
ATOM   111  O  O     . THR A 1 30  ? -2.120  59.602 4.478   1.00 31.38  ? 16   THR A O     1 
ATOM   112  C  CB    . THR A 1 30  ? -1.147  62.718 4.537   1.00 32.09  ? 16   THR A CB    1 
ATOM   113  O  OG1   . THR A 1 30  ? -2.399  63.374 4.321   1.00 43.21  ? 16   THR A OG1   1 
ATOM   114  C  CG2   . THR A 1 30  ? -0.079  63.725 4.292   1.00 30.23  ? 16   THR A CG2   1 
ATOM   115  N  N     . ASP A 1 31  ? -3.375  60.980 3.196   1.00 30.62  ? 17   ASP A N     1 
ATOM   116  C  CA    . ASP A 1 31  ? -4.575  60.159 3.317   1.00 30.10  ? 17   ASP A CA    1 
ATOM   117  C  C     . ASP A 1 31  ? -4.326  58.736 2.852   1.00 28.15  ? 17   ASP A C     1 
ATOM   118  O  O     . ASP A 1 31  ? -4.878  57.789 3.422   1.00 27.88  ? 17   ASP A O     1 
ATOM   119  C  CB    . ASP A 1 31  ? -5.711  60.769 2.498   1.00 31.51  ? 17   ASP A CB    1 
ATOM   120  C  CG    . ASP A 1 31  ? -6.206  62.091 3.053   1.00 32.60  ? 17   ASP A CG    1 
ATOM   121  O  OD1   . ASP A 1 31  ? -5.786  62.493 4.169   1.00 31.94  ? 17   ASP A OD1   1 
ATOM   122  O  OD2   . ASP A 1 31  ? -6.985  62.753 2.331   1.00 30.83  ? 17   ASP A OD2   1 
ATOM   123  N  N     . CYS A 1 32  ? -3.475  58.567 1.843   1.00 29.15  ? 18   CYS A N     1 
ATOM   124  C  CA    . CYS A 1 32  ? -3.240  57.269 1.230   1.00 28.29  ? 18   CYS A CA    1 
ATOM   125  C  C     . CYS A 1 32  ? -2.207  56.432 1.976   1.00 29.28  ? 18   CYS A C     1 
ATOM   126  O  O     . CYS A 1 32  ? -2.008  55.267 1.615   1.00 28.79  ? 18   CYS A O     1 
ATOM   127  C  CB    . CYS A 1 32  ? -2.808  57.473 -0.225  1.00 26.70  ? 18   CYS A CB    1 
ATOM   128  S  SG    . CYS A 1 32  ? -4.161  58.003 -1.320  1.00 24.17  ? 18   CYS A SG    1 
ATOM   129  N  N     . GLY A 1 33  ? -1.554  56.987 3.000   1.00 27.12  ? 19   GLY A N     1 
ATOM   130  C  CA    . GLY A 1 33  ? -0.645  56.233 3.840   1.00 29.09  ? 19   GLY A CA    1 
ATOM   131  C  C     . GLY A 1 33  ? 0.808   56.635 3.728   1.00 30.02  ? 19   GLY A C     1 
ATOM   132  O  O     . GLY A 1 33  ? 1.652   56.053 4.424   1.00 29.12  ? 19   GLY A O     1 
ATOM   133  N  N     . ALA A 1 34  ? 1.125   57.598 2.870   1.00 28.01  ? 20   ALA A N     1 
ATOM   134  C  CA    . ALA A 1 34  ? 2.491   58.057 2.658   1.00 28.27  ? 20   ALA A CA    1 
ATOM   135  C  C     . ALA A 1 34  ? 2.822   59.208 3.596   1.00 28.74  ? 20   ALA A C     1 
ATOM   136  O  O     . ALA A 1 34  ? 2.100   60.211 3.643   1.00 31.73  ? 20   ALA A O     1 
ATOM   137  C  CB    . ALA A 1 34  ? 2.691   58.498 1.207   1.00 25.43  ? 20   ALA A CB    1 
ATOM   138  N  N     . ASP A 1 35  ? 3.904   59.056 4.351   1.00 26.46  ? 21   ASP A N     1 
ATOM   139  C  CA    . ASP A 1 35  ? 4.418   60.134 5.183   1.00 27.96  ? 21   ASP A CA    1 
ATOM   140  C  C     . ASP A 1 35  ? 5.716   60.703 4.644   1.00 26.72  ? 21   ASP A C     1 
ATOM   141  O  O     . ASP A 1 35  ? 6.301   61.589 5.279   1.00 24.81  ? 21   ASP A O     1 
ATOM   142  C  CB    . ASP A 1 35  ? 4.618   59.647 6.619   1.00 30.23  ? 21   ASP A CB    1 
ATOM   143  C  CG    . ASP A 1 35  ? 3.334   59.120 7.225   1.00 32.39  ? 21   ASP A CG    1 
ATOM   144  O  OD1   . ASP A 1 35  ? 2.291   59.786 7.079   1.00 31.87  ? 21   ASP A OD1   1 
ATOM   145  O  OD2   . ASP A 1 35  ? 3.364   58.034 7.830   1.00 33.86  ? 21   ASP A OD2   1 
ATOM   146  N  N     . HIS A 1 36  ? 6.176   60.213 3.494   1.00 23.58  ? 22   HIS A N     1 
ATOM   147  C  CA    . HIS A 1 36  ? 7.419   60.655 2.887   1.00 22.33  ? 22   HIS A CA    1 
ATOM   148  C  C     . HIS A 1 36  ? 7.232   60.763 1.384   1.00 22.14  ? 22   HIS A C     1 
ATOM   149  O  O     . HIS A 1 36  ? 6.348   60.133 0.797   1.00 20.91  ? 22   HIS A O     1 
ATOM   150  C  CB    . HIS A 1 36  ? 8.577   59.696 3.182   1.00 23.08  ? 22   HIS A CB    1 
ATOM   151  C  CG    . HIS A 1 36  ? 8.906   59.590 4.637   1.00 23.86  ? 22   HIS A CG    1 
ATOM   152  N  ND1   . HIS A 1 36  ? 8.139   58.861 5.518   1.00 24.68  ? 22   HIS A ND1   1 
ATOM   153  C  CD2   . HIS A 1 36  ? 9.906   60.135 5.368   1.00 23.40  ? 22   HIS A CD2   1 
ATOM   154  C  CE1   . HIS A 1 36  ? 8.659   58.953 6.730   1.00 24.75  ? 22   HIS A CE1   1 
ATOM   155  N  NE2   . HIS A 1 36  ? 9.734   59.715 6.663   1.00 25.90  ? 22   HIS A NE2   1 
ATOM   156  N  N     . LEU A 1 37  ? 8.076   61.586 0.769   1.00 19.44  ? 23   LEU A N     1 
ATOM   157  C  CA    . LEU A 1 37  ? 8.134   61.735 -0.681  1.00 20.16  ? 23   LEU A CA    1 
ATOM   158  C  C     . LEU A 1 37  ? 9.584   61.540 -1.093  1.00 19.57  ? 23   LEU A C     1 
ATOM   159  O  O     . LEU A 1 37  ? 10.468  62.199 -0.539  1.00 19.86  ? 23   LEU A O     1 
ATOM   160  C  CB    . LEU A 1 37  ? 7.624   63.113 -1.103  1.00 18.05  ? 23   LEU A CB    1 
ATOM   161  C  CG    . LEU A 1 37  ? 7.658   63.421 -2.599  1.00 19.86  ? 23   LEU A CG    1 
ATOM   162  C  CD1   . LEU A 1 37  ? 6.776   62.457 -3.387  1.00 18.30  ? 23   LEU A CD1   1 
ATOM   163  C  CD2   . LEU A 1 37  ? 7.247   64.864 -2.847  1.00 18.93  ? 23   LEU A CD2   1 
ATOM   164  N  N     . PHE A 1 38  ? 9.843   60.586 -1.994  1.00 19.72  ? 24   PHE A N     1 
ATOM   165  C  CA    . PHE A 1 38  ? 11.187  60.332 -2.503  1.00 19.00  ? 24   PHE A CA    1 
ATOM   166  C  C     . PHE A 1 38  ? 11.387  61.014 -3.858  1.00 19.31  ? 24   PHE A C     1 
ATOM   167  O  O     . PHE A 1 38  ? 10.441  61.175 -4.627  1.00 18.83  ? 24   PHE A O     1 
ATOM   168  C  CB    . PHE A 1 38  ? 11.452  58.826 -2.652  1.00 18.67  ? 24   PHE A CB    1 
ATOM   169  C  CG    . PHE A 1 38  ? 11.360  58.053 -1.362  1.00 18.86  ? 24   PHE A CG    1 
ATOM   170  C  CD1   . PHE A 1 38  ? 10.130  57.547 -0.926  1.00 19.70  ? 24   PHE A CD1   1 
ATOM   171  C  CD2   . PHE A 1 38  ? 12.495  57.827 -0.578  1.00 16.88  ? 24   PHE A CD2   1 
ATOM   172  C  CE1   . PHE A 1 38  ? 10.030  56.837 0.286   1.00 19.66  ? 24   PHE A CE1   1 
ATOM   173  C  CE2   . PHE A 1 38  ? 12.415  57.106 0.623   1.00 18.54  ? 24   PHE A CE2   1 
ATOM   174  C  CZ    . PHE A 1 38  ? 11.192  56.619 1.063   1.00 19.62  ? 24   PHE A CZ    1 
ATOM   175  N  N     . GLY A 1 39  ? 12.624  61.399 -4.164  1.00 20.25  ? 25   GLY A N     1 
ATOM   176  C  CA    . GLY A 1 39  ? 12.895  61.828 -5.532  1.00 18.49  ? 25   GLY A CA    1 
ATOM   177  C  C     . GLY A 1 39  ? 14.158  62.674 -5.651  1.00 20.73  ? 25   GLY A C     1 
ATOM   178  O  O     . GLY A 1 39  ? 15.033  62.643 -4.785  1.00 19.12  ? 25   GLY A O     1 
ATOM   179  N  N     . VAL A 1 40  ? 14.231  63.396 -6.773  1.00 20.67  ? 26   VAL A N     1 
ATOM   180  C  CA    . VAL A 1 40  ? 15.372  64.238 -7.131  1.00 20.30  ? 26   VAL A CA    1 
ATOM   181  C  C     . VAL A 1 40  ? 14.810  65.569 -7.617  1.00 21.02  ? 26   VAL A C     1 
ATOM   182  O  O     . VAL A 1 40  ? 13.856  65.591 -8.412  1.00 19.86  ? 26   VAL A O     1 
ATOM   183  C  CB    . VAL A 1 40  ? 16.261  63.588 -8.212  1.00 20.04  ? 26   VAL A CB    1 
ATOM   184  C  CG1   . VAL A 1 40  ? 17.305  64.584 -8.766  1.00 19.31  ? 26   VAL A CG1   1 
ATOM   185  C  CG2   . VAL A 1 40  ? 16.954  62.332 -7.691  1.00 17.46  ? 26   VAL A CG2   1 
ATOM   186  N  N     . PRO A 1 41  ? 15.339  66.693 -7.151  1.00 21.32  ? 27   PRO A N     1 
ATOM   187  C  CA    . PRO A 1 41  ? 14.782  67.988 -7.550  1.00 23.40  ? 27   PRO A CA    1 
ATOM   188  C  C     . PRO A 1 41  ? 15.150  68.360 -8.980  1.00 22.91  ? 27   PRO A C     1 
ATOM   189  O  O     . PRO A 1 41  ? 16.113  67.861 -9.561  1.00 22.85  ? 27   PRO A O     1 
ATOM   190  C  CB    . PRO A 1 41  ? 15.404  68.957 -6.539  1.00 24.44  ? 27   PRO A CB    1 
ATOM   191  C  CG    . PRO A 1 41  ? 16.665  68.303 -6.136  1.00 27.47  ? 27   PRO A CG    1 
ATOM   192  C  CD    . PRO A 1 41  ? 16.348  66.832 -6.090  1.00 23.61  ? 27   PRO A CD    1 
ATOM   193  N  N     . GLY A 1 42  ? 14.356  69.268 -9.539  1.00 23.75  ? 28   GLY A N     1 
ATOM   194  C  CA    . GLY A 1 42  ? 14.639  69.865 -10.831 1.00 23.99  ? 28   GLY A CA    1 
ATOM   195  C  C     . GLY A 1 42  ? 13.865  71.156 -10.948 1.00 24.91  ? 28   GLY A C     1 
ATOM   196  O  O     . GLY A 1 42  ? 12.862  71.358 -10.262 1.00 23.32  ? 28   GLY A O     1 
ATOM   197  N  N     . ASP A 1 43  ? 14.326  72.033 -11.841 1.00 24.79  ? 29   ASP A N     1 
ATOM   198  C  CA    . ASP A 1 43  ? 13.718  73.360 -11.919 1.00 28.43  ? 29   ASP A CA    1 
ATOM   199  C  C     . ASP A 1 43  ? 12.203  73.297 -12.157 1.00 29.31  ? 29   ASP A C     1 
ATOM   200  O  O     . ASP A 1 43  ? 11.454  74.135 -11.630 1.00 30.92  ? 29   ASP A O     1 
ATOM   201  C  CB    . ASP A 1 43  ? 14.460  74.187 -12.979 1.00 29.88  ? 29   ASP A CB    1 
ATOM   202  C  CG    . ASP A 1 43  ? 14.067  73.828 -14.399 1.00 29.48  ? 29   ASP A CG    1 
ATOM   203  O  OD1   . ASP A 1 43  ? 13.966  72.619 -14.706 1.00 26.66  ? 29   ASP A OD1   1 
ATOM   204  O  OD2   . ASP A 1 43  ? 13.901  74.753 -15.222 1.00 32.91  ? 29   ASP A OD2   1 
ATOM   205  N  N     . TYR A 1 44  ? 11.720  72.267 -12.852 1.00 24.90  ? 30   TYR A N     1 
ATOM   206  C  CA    . TYR A 1 44  ? 10.293  72.131 -13.102 1.00 25.52  ? 30   TYR A CA    1 
ATOM   207  C  C     . TYR A 1 44  ? 9.483   71.675 -11.888 1.00 25.09  ? 30   TYR A C     1 
ATOM   208  O  O     . TYR A 1 44  ? 8.254   71.765 -11.940 1.00 26.23  ? 30   TYR A O     1 
ATOM   209  C  CB    . TYR A 1 44  ? 10.046  71.162 -14.253 1.00 23.90  ? 30   TYR A CB    1 
ATOM   210  C  CG    . TYR A 1 44  ? 10.615  71.611 -15.575 1.00 24.56  ? 30   TYR A CG    1 
ATOM   211  C  CD1   . TYR A 1 44  ? 10.453  72.917 -16.023 1.00 26.08  ? 30   TYR A CD1   1 
ATOM   212  C  CD2   . TYR A 1 44  ? 11.297  70.717 -16.391 1.00 23.11  ? 30   TYR A CD2   1 
ATOM   213  C  CE1   . TYR A 1 44  ? 10.975  73.315 -17.244 1.00 25.76  ? 30   TYR A CE1   1 
ATOM   214  C  CE2   . TYR A 1 44  ? 11.813  71.104 -17.613 1.00 23.58  ? 30   TYR A CE2   1 
ATOM   215  C  CZ    . TYR A 1 44  ? 11.648  72.404 -18.038 1.00 25.28  ? 30   TYR A CZ    1 
ATOM   216  O  OH    . TYR A 1 44  ? 12.166  72.782 -19.273 1.00 25.06  ? 30   TYR A OH    1 
ATOM   217  N  N     . ASN A 1 45  ? 10.104  71.175 -10.811 1.00 24.60  ? 31   ASN A N     1 
ATOM   218  C  CA    . ASN A 1 45  ? 9.338   70.785 -9.626  1.00 24.92  ? 31   ASN A CA    1 
ATOM   219  C  C     . ASN A 1 45  ? 9.741   71.541 -8.361  1.00 27.40  ? 31   ASN A C     1 
ATOM   220  O  O     . ASN A 1 45  ? 9.299   71.165 -7.268  1.00 25.04  ? 31   ASN A O     1 
ATOM   221  C  CB    . ASN A 1 45  ? 9.417   69.265 -9.370  1.00 22.35  ? 31   ASN A CB    1 
ATOM   222  C  CG    . ASN A 1 45  ? 10.834  68.757 -9.070  1.00 23.23  ? 31   ASN A CG    1 
ATOM   223  O  OD1   . ASN A 1 45  ? 11.622  69.407 -8.375  1.00 22.96  ? 31   ASN A OD1   1 
ATOM   224  N  ND2   . ASN A 1 45  ? 11.136  67.556 -9.557  1.00 20.11  ? 31   ASN A ND2   1 
ATOM   225  N  N     . LEU A 1 46  ? 10.578  72.579 -8.468  1.00 27.43  ? 32   LEU A N     1 
ATOM   226  C  CA    . LEU A 1 46  ? 11.129  73.204 -7.268  1.00 29.10  ? 32   LEU A CA    1 
ATOM   227  C  C     . LEU A 1 46  ? 10.056  73.894 -6.440  1.00 30.52  ? 32   LEU A C     1 
ATOM   228  O  O     . LEU A 1 46  ? 10.063  73.798 -5.206  1.00 31.78  ? 32   LEU A O     1 
ATOM   229  C  CB    . LEU A 1 46  ? 12.224  74.210 -7.629  1.00 33.67  ? 32   LEU A CB    1 
ATOM   230  C  CG    . LEU A 1 46  ? 13.569  73.651 -8.097  1.00 32.54  ? 32   LEU A CG    1 
ATOM   231  C  CD1   . LEU A 1 46  ? 14.605  74.766 -8.180  1.00 39.64  ? 32   LEU A CD1   1 
ATOM   232  C  CD2   . LEU A 1 46  ? 14.032  72.551 -7.170  1.00 30.59  ? 32   LEU A CD2   1 
ATOM   233  N  N     . GLN A 1 47  ? 9.150   74.624 -7.090  1.00 31.08  ? 33   GLN A N     1 
ATOM   234  C  CA    . GLN A 1 47  ? 8.137   75.341 -6.330  1.00 33.71  ? 33   GLN A CA    1 
ATOM   235  C  C     . GLN A 1 47  ? 7.204   74.372 -5.625  1.00 30.15  ? 33   GLN A C     1 
ATOM   236  O  O     . GLN A 1 47  ? 6.845   74.591 -4.465  1.00 28.58  ? 33   GLN A O     1 
ATOM   237  C  CB    . GLN A 1 47  ? 7.385   76.309 -7.237  1.00 38.14  ? 33   GLN A CB    1 
ATOM   238  C  CG    . GLN A 1 47  ? 8.302   77.427 -7.734  1.00 49.71  ? 33   GLN A CG    1 
ATOM   239  C  CD    . GLN A 1 47  ? 7.738   78.211 -8.901  1.00 69.43  ? 33   GLN A CD    1 
ATOM   240  O  OE1   . GLN A 1 47  ? 6.894   77.718 -9.652  1.00 66.81  ? 33   GLN A OE1   1 
ATOM   241  N  NE2   . GLN A 1 47  ? 8.219   79.440 -9.071  1.00 70.88  ? 33   GLN A NE2   1 
ATOM   242  N  N     . PHE A 1 48  ? 6.850   73.268 -6.286  1.00 27.63  ? 34   PHE A N     1 
ATOM   243  C  CA    . PHE A 1 48  ? 6.121   72.203 -5.603  1.00 27.10  ? 34   PHE A CA    1 
ATOM   244  C  C     . PHE A 1 48  ? 6.912   71.680 -4.406  1.00 27.03  ? 34   PHE A C     1 
ATOM   245  O  O     . PHE A 1 48  ? 6.343   71.436 -3.336  1.00 25.16  ? 34   PHE A O     1 
ATOM   246  C  CB    . PHE A 1 48  ? 5.829   71.075 -6.591  1.00 22.80  ? 34   PHE A CB    1 
ATOM   247  C  CG    . PHE A 1 48  ? 5.249   69.844 -5.966  1.00 21.92  ? 34   PHE A CG    1 
ATOM   248  C  CD1   . PHE A 1 48  ? 3.919   69.812 -5.556  1.00 21.40  ? 34   PHE A CD1   1 
ATOM   249  C  CD2   . PHE A 1 48  ? 6.033   68.706 -5.804  1.00 22.30  ? 34   PHE A CD2   1 
ATOM   250  C  CE1   . PHE A 1 48  ? 3.386   68.675 -4.994  1.00 21.82  ? 34   PHE A CE1   1 
ATOM   251  C  CE2   . PHE A 1 48  ? 5.513   67.562 -5.240  1.00 20.85  ? 34   PHE A CE2   1 
ATOM   252  C  CZ    . PHE A 1 48  ? 4.183   67.542 -4.824  1.00 21.65  ? 34   PHE A CZ    1 
ATOM   253  N  N     . LEU A 1 49  ? 8.230   71.516 -4.568  1.00 26.12  ? 35   LEU A N     1 
ATOM   254  C  CA    . LEU A 1 49  ? 9.073   71.032 -3.478  1.00 27.89  ? 35   LEU A CA    1 
ATOM   255  C  C     . LEU A 1 49  ? 9.007   71.944 -2.265  1.00 28.44  ? 35   LEU A C     1 
ATOM   256  O  O     . LEU A 1 49  ? 9.148   71.473 -1.132  1.00 30.17  ? 35   LEU A O     1 
ATOM   257  C  CB    . LEU A 1 49  ? 10.521  70.897 -3.943  1.00 29.42  ? 35   LEU A CB    1 
ATOM   258  C  CG    . LEU A 1 49  ? 10.960  69.458 -4.164  1.00 30.44  ? 35   LEU A CG    1 
ATOM   259  C  CD1   . LEU A 1 49  ? 12.327  69.408 -4.852  1.00 28.37  ? 35   LEU A CD1   1 
ATOM   260  C  CD2   . LEU A 1 49  ? 10.978  68.729 -2.832  1.00 25.64  ? 35   LEU A CD2   1 
ATOM   261  N  N     . ASP A 1 50  ? 8.842   73.253 -2.482  1.00 29.87  ? 36   ASP A N     1 
ATOM   262  C  CA    . ASP A 1 50  ? 8.657   74.173 -1.364  1.00 31.39  ? 36   ASP A CA    1 
ATOM   263  C  C     . ASP A 1 50  ? 7.436   73.808 -0.531  1.00 32.49  ? 36   ASP A C     1 
ATOM   264  O  O     . ASP A 1 50  ? 7.416   74.045 0.680   1.00 32.06  ? 36   ASP A O     1 
ATOM   265  C  CB    . ASP A 1 50  ? 8.499   75.611 -1.860  1.00 34.03  ? 36   ASP A CB    1 
ATOM   266  C  CG    . ASP A 1 50  ? 9.766   76.179 -2.452  1.00 37.30  ? 36   ASP A CG    1 
ATOM   267  O  OD1   . ASP A 1 50  ? 10.868  75.651 -2.175  1.00 38.20  ? 36   ASP A OD1   1 
ATOM   268  O  OD2   . ASP A 1 50  ? 9.643   77.181 -3.183  1.00 38.81  ? 36   ASP A OD2   1 
ATOM   269  N  N     . HIS A 1 51  ? 6.383   73.294 -1.165  1.00 31.20  ? 37   HIS A N     1 
ATOM   270  C  CA    . HIS A 1 51  ? 5.215   72.885 -0.394  1.00 30.92  ? 37   HIS A CA    1 
ATOM   271  C  C     . HIS A 1 51  ? 5.464   71.585 0.350   1.00 30.81  ? 37   HIS A C     1 
ATOM   272  O  O     . HIS A 1 51  ? 4.930   71.388 1.446   1.00 31.49  ? 37   HIS A O     1 
ATOM   273  C  CB    . HIS A 1 51  ? 4.006   72.765 -1.308  1.00 28.16  ? 37   HIS A CB    1 
ATOM   274  C  CG    . HIS A 1 51  ? 3.521   74.086 -1.797  1.00 28.53  ? 37   HIS A CG    1 
ATOM   275  N  ND1   . HIS A 1 51  ? 2.484   74.759 -1.196  1.00 27.89  ? 37   HIS A ND1   1 
ATOM   276  C  CD2   . HIS A 1 51  ? 3.953   74.876 -2.809  1.00 28.63  ? 37   HIS A CD2   1 
ATOM   277  C  CE1   . HIS A 1 51  ? 2.289   75.906 -1.822  1.00 30.15  ? 37   HIS A CE1   1 
ATOM   278  N  NE2   . HIS A 1 51  ? 3.167   76.002 -2.805  1.00 30.35  ? 37   HIS A NE2   1 
ATOM   279  N  N     . VAL A 1 52  ? 6.263   70.692 -0.232  1.00 29.01  ? 38   VAL A N     1 
ATOM   280  C  CA    . VAL A 1 52  ? 6.623   69.460 0.456   1.00 29.18  ? 38   VAL A CA    1 
ATOM   281  C  C     . VAL A 1 52  ? 7.444   69.776 1.698   1.00 30.87  ? 38   VAL A C     1 
ATOM   282  O  O     . VAL A 1 52  ? 7.236   69.192 2.765   1.00 28.18  ? 38   VAL A O     1 
ATOM   283  C  CB    . VAL A 1 52  ? 7.382   68.520 -0.499  1.00 27.20  ? 38   VAL A CB    1 
ATOM   284  C  CG1   . VAL A 1 52  ? 7.847   67.265 0.236   1.00 24.63  ? 38   VAL A CG1   1 
ATOM   285  C  CG2   . VAL A 1 52  ? 6.530   68.185 -1.724  1.00 24.54  ? 38   VAL A CG2   1 
ATOM   286  N  N     . ILE A 1 53  ? 8.399   70.695 1.572   1.00 31.90  ? 39   ILE A N     1 
ATOM   287  C  CA    . ILE A 1 53  ? 9.244   71.054 2.709   1.00 34.09  ? 39   ILE A CA    1 
ATOM   288  C  C     . ILE A 1 53  ? 8.400   71.673 3.814   1.00 35.31  ? 39   ILE A C     1 
ATOM   289  O  O     . ILE A 1 53  ? 8.548   71.341 4.996   1.00 34.86  ? 39   ILE A O     1 
ATOM   290  C  CB    . ILE A 1 53  ? 10.377  71.997 2.259   1.00 36.90  ? 39   ILE A CB    1 
ATOM   291  C  CG1   . ILE A 1 53  ? 11.382  71.223 1.399   1.00 34.82  ? 39   ILE A CG1   1 
ATOM   292  C  CG2   . ILE A 1 53  ? 11.067  72.636 3.468   1.00 36.58  ? 39   ILE A CG2   1 
ATOM   293  C  CD1   . ILE A 1 53  ? 12.376  70.417 2.183   1.00 38.58  ? 39   ILE A CD1   1 
ATOM   294  N  N     . ASP A 1 54  ? 7.511   72.595 3.445   1.00 36.06  ? 40   ASP A N     1 
ATOM   295  C  CA    . ASP A 1 54  ? 6.707   73.298 4.433   1.00 35.04  ? 40   ASP A CA    1 
ATOM   296  C  C     . ASP A 1 54  ? 5.662   72.400 5.077   1.00 36.50  ? 40   ASP A C     1 
ATOM   297  O  O     . ASP A 1 54  ? 5.198   72.704 6.178   1.00 38.44  ? 40   ASP A O     1 
ATOM   298  C  CB    . ASP A 1 54  ? 6.027   74.502 3.785   1.00 37.25  ? 40   ASP A CB    1 
ATOM   299  C  CG    . ASP A 1 54  ? 7.018   75.592 3.400   1.00 42.18  ? 40   ASP A CG    1 
ATOM   300  O  OD1   . ASP A 1 54  ? 8.200   75.501 3.804   1.00 41.55  ? 40   ASP A OD1   1 
ATOM   301  O  OD2   . ASP A 1 54  ? 6.621   76.532 2.678   1.00 43.92  ? 40   ASP A OD2   1 
ATOM   302  N  N     . SER A 1 55  ? 5.284   71.311 4.428   1.00 35.14  ? 41   SER A N     1 
ATOM   303  C  CA    . SER A 1 55  ? 4.229   70.456 4.958   1.00 34.47  ? 41   SER A CA    1 
ATOM   304  C  C     . SER A 1 55  ? 4.676   69.822 6.272   1.00 35.29  ? 41   SER A C     1 
ATOM   305  O  O     . SER A 1 55  ? 5.780   69.278 6.345   1.00 36.48  ? 41   SER A O     1 
ATOM   306  C  CB    . SER A 1 55  ? 3.875   69.375 3.933   1.00 33.73  ? 41   SER A CB    1 
ATOM   307  O  OG    . SER A 1 55  ? 3.134   68.316 4.518   1.00 33.54  ? 41   SER A OG    1 
ATOM   308  N  N     . PRO A 1 56  ? 3.858   69.868 7.329   1.00 38.07  ? 42   PRO A N     1 
ATOM   309  C  CA    . PRO A 1 56  ? 4.198   69.124 8.551   1.00 37.29  ? 42   PRO A CA    1 
ATOM   310  C  C     . PRO A 1 56  ? 3.951   67.632 8.427   1.00 36.46  ? 42   PRO A C     1 
ATOM   311  O  O     . PRO A 1 56  ? 4.381   66.875 9.308   1.00 38.68  ? 42   PRO A O     1 
ATOM   312  C  CB    . PRO A 1 56  ? 3.276   69.747 9.616   1.00 36.48  ? 42   PRO A CB    1 
ATOM   313  C  CG    . PRO A 1 56  ? 2.158   70.436 8.833   1.00 38.37  ? 42   PRO A CG    1 
ATOM   314  C  CD    . PRO A 1 56  ? 2.468   70.352 7.352   1.00 35.21  ? 42   PRO A CD    1 
ATOM   315  N  N     . ASP A 1 57  ? 3.266   67.197 7.369   1.00 36.03  ? 43   ASP A N     1 
ATOM   316  C  CA    . ASP A 1 57  ? 2.802   65.826 7.225   1.00 34.54  ? 43   ASP A CA    1 
ATOM   317  C  C     . ASP A 1 57  ? 3.639   64.982 6.278   1.00 33.58  ? 43   ASP A C     1 
ATOM   318  O  O     . ASP A 1 57  ? 3.586   63.751 6.362   1.00 33.43  ? 43   ASP A O     1 
ATOM   319  C  CB    . ASP A 1 57  ? 1.362   65.832 6.712   1.00 36.94  ? 43   ASP A CB    1 
ATOM   320  C  CG    . ASP A 1 57  ? 0.374   66.310 7.753   1.00 38.51  ? 43   ASP A CG    1 
ATOM   321  O  OD1   . ASP A 1 57  ? 0.807   66.744 8.840   1.00 40.48  ? 43   ASP A OD1   1 
ATOM   322  O  OD2   . ASP A 1 57  ? -0.838  66.266 7.470   1.00 46.82  ? 43   ASP A OD2   1 
ATOM   323  N  N     . ILE A 1 58  ? 4.421   65.600 5.399   1.00 32.14  ? 44   ILE A N     1 
ATOM   324  C  CA    . ILE A 1 58  ? 5.182   64.881 4.386   1.00 29.33  ? 44   ILE A CA    1 
ATOM   325  C  C     . ILE A 1 58  ? 6.629   65.305 4.516   1.00 29.02  ? 44   ILE A C     1 
ATOM   326  O  O     . ILE A 1 58  ? 6.935   66.502 4.524   1.00 30.46  ? 44   ILE A O     1 
ATOM   327  C  CB    . ILE A 1 58  ? 4.674   65.164 2.959   1.00 28.58  ? 44   ILE A CB    1 
ATOM   328  C  CG1   . ILE A 1 58  ? 3.175   64.923 2.853   1.00 30.09  ? 44   ILE A CG1   1 
ATOM   329  C  CG2   . ILE A 1 58  ? 5.383   64.261 1.939   1.00 26.70  ? 44   ILE A CG2   1 
ATOM   330  C  CD1   . ILE A 1 58  ? 2.856   63.449 2.804   1.00 27.97  ? 44   ILE A CD1   1 
ATOM   331  N  N     . CYS A 1 59  ? 7.512   64.325 4.591   1.00 26.68  ? 45   CYS A N     1 
ATOM   332  C  CA    . CYS A 1 59  ? 8.935   64.560 4.743   1.00 27.57  ? 45   CYS A CA    1 
ATOM   333  C  C     . CYS A 1 59  ? 9.615   64.274 3.409   1.00 26.04  ? 45   CYS A C     1 
ATOM   334  O  O     . CYS A 1 59  ? 9.519   63.159 2.881   1.00 22.76  ? 45   CYS A O     1 
ATOM   335  C  CB    . CYS A 1 59  ? 9.499   63.684 5.857   1.00 26.25  ? 45   CYS A CB    1 
ATOM   336  S  SG    . CYS A 1 59  ? 11.269  63.565 5.834   1.00 31.71  ? 45   CYS A SG    1 
ATOM   337  N  N     . TRP A 1 60  ? 10.289  65.282 2.866   1.00 23.05  ? 46   TRP A N     1 
ATOM   338  C  CA    . TRP A 1 60  ? 11.042  65.097 1.637   1.00 23.73  ? 46   TRP A CA    1 
ATOM   339  C  C     . TRP A 1 60  ? 12.246  64.201 1.880   1.00 24.48  ? 46   TRP A C     1 
ATOM   340  O  O     . TRP A 1 60  ? 12.968  64.364 2.865   1.00 23.40  ? 46   TRP A O     1 
ATOM   341  C  CB    . TRP A 1 60  ? 11.502  66.440 1.098   1.00 23.64  ? 46   TRP A CB    1 
ATOM   342  C  CG    . TRP A 1 60  ? 12.470  66.335 -0.018  1.00 24.44  ? 46   TRP A CG    1 
ATOM   343  C  CD1   . TRP A 1 60  ? 13.794  66.674 -0.001  1.00 25.40  ? 46   TRP A CD1   1 
ATOM   344  C  CD2   . TRP A 1 60  ? 12.186  65.870 -1.338  1.00 22.67  ? 46   TRP A CD2   1 
ATOM   345  N  NE1   . TRP A 1 60  ? 14.351  66.441 -1.235  1.00 26.35  ? 46   TRP A NE1   1 
ATOM   346  C  CE2   . TRP A 1 60  ? 13.381  65.952 -2.074  1.00 24.07  ? 46   TRP A CE2   1 
ATOM   347  C  CE3   . TRP A 1 60  ? 11.028  65.403 -1.972  1.00 21.69  ? 46   TRP A CE3   1 
ATOM   348  C  CZ2   . TRP A 1 60  ? 13.456  65.586 -3.413  1.00 22.77  ? 46   TRP A CZ2   1 
ATOM   349  C  CZ3   . TRP A 1 60  ? 11.108  65.030 -3.313  1.00 21.01  ? 46   TRP A CZ3   1 
ATOM   350  C  CH2   . TRP A 1 60  ? 12.315  65.124 -4.010  1.00 20.96  ? 46   TRP A CH2   1 
ATOM   351  N  N     . VAL A 1 61  ? 12.457  63.243 0.992   1.00 21.84  ? 47   VAL A N     1 
ATOM   352  C  CA    . VAL A 1 61  ? 13.634  62.385 1.039   1.00 22.31  ? 47   VAL A CA    1 
ATOM   353  C  C     . VAL A 1 61  ? 14.346  62.528 -0.300  1.00 21.74  ? 47   VAL A C     1 
ATOM   354  O  O     . VAL A 1 61  ? 13.966  61.889 -1.286  1.00 19.70  ? 47   VAL A O     1 
ATOM   355  C  CB    . VAL A 1 61  ? 13.280  60.925 1.340   1.00 21.95  ? 47   VAL A CB    1 
ATOM   356  C  CG1   . VAL A 1 61  ? 14.551  60.093 1.526   1.00 22.55  ? 47   VAL A CG1   1 
ATOM   357  C  CG2   . VAL A 1 61  ? 12.429  60.849 2.593   1.00 21.66  ? 47   VAL A CG2   1 
ATOM   358  N  N     . GLY A 1 62  ? 15.378  63.366 -0.346  1.00 22.36  ? 48   GLY A N     1 
ATOM   359  C  CA    . GLY A 1 62  ? 16.166  63.490 -1.567  1.00 22.74  ? 48   GLY A CA    1 
ATOM   360  C  C     . GLY A 1 62  ? 17.008  62.247 -1.794  1.00 20.61  ? 48   GLY A C     1 
ATOM   361  O  O     . GLY A 1 62  ? 17.674  61.754 -0.876  1.00 22.79  ? 48   GLY A O     1 
ATOM   362  N  N     . CYS A 1 63  ? 16.982  61.725 -3.015  1.00 21.40  ? 49   CYS A N     1 
ATOM   363  C  CA    . CYS A 1 63  ? 17.720  60.516 -3.334  1.00 18.54  ? 49   CYS A CA    1 
ATOM   364  C  C     . CYS A 1 63  ? 18.873  60.817 -4.286  1.00 19.76  ? 49   CYS A C     1 
ATOM   365  O  O     . CYS A 1 63  ? 18.907  61.851 -4.963  1.00 18.97  ? 49   CYS A O     1 
ATOM   366  C  CB    . CYS A 1 63  ? 16.791  59.459 -3.937  1.00 19.01  ? 49   CYS A CB    1 
ATOM   367  S  SG    . CYS A 1 63  ? 15.489  58.872 -2.803  1.00 23.21  ? 49   CYS A SG    1 
ATOM   368  N  N     . ALA A 1 64  ? 19.815  59.881 -4.350  1.00 19.38  ? 50   ALA A N     1 
ATOM   369  C  CA    . ALA A 1 64  ? 21.023  60.098 -5.136  1.00 18.36  ? 50   ALA A CA    1 
ATOM   370  C  C     . ALA A 1 64  ? 20.803  59.946 -6.639  1.00 18.23  ? 50   ALA A C     1 
ATOM   371  O  O     . ALA A 1 64  ? 21.595  60.493 -7.410  1.00 20.87  ? 50   ALA A O     1 
ATOM   372  C  CB    . ALA A 1 64  ? 22.143  59.158 -4.663  1.00 19.23  ? 50   ALA A CB    1 
ATOM   373  N  N     . ASN A 1 65  ? 19.795  59.189 -7.082  1.00 19.52  ? 51   ASN A N     1 
ATOM   374  C  CA    . ASN A 1 65  ? 19.301  59.326 -8.451  1.00 18.62  ? 51   ASN A CA    1 
ATOM   375  C  C     . ASN A 1 65  ? 17.860  58.835 -8.506  1.00 17.88  ? 51   ASN A C     1 
ATOM   376  O  O     . ASN A 1 65  ? 17.337  58.257 -7.550  1.00 17.42  ? 51   ASN A O     1 
ATOM   377  C  CB    . ASN A 1 65  ? 20.201  58.624 -9.502  1.00 16.21  ? 51   ASN A CB    1 
ATOM   378  C  CG    . ASN A 1 65  ? 20.312  57.097 -9.325  1.00 18.31  ? 51   ASN A CG    1 
ATOM   379  O  OD1   . ASN A 1 65  ? 19.375  56.418 -8.900  1.00 17.23  ? 51   ASN A OD1   1 
ATOM   380  N  ND2   . ASN A 1 65  ? 21.479  56.554 -9.680  1.00 15.67  ? 51   ASN A ND2   1 
ATOM   381  N  N     . GLU A 1 66  ? 17.229  59.067 -9.660  1.00 16.26  ? 52   GLU A N     1 
ATOM   382  C  CA    . GLU A 1 66  ? 15.800  58.818 -9.802  1.00 16.54  ? 52   GLU A CA    1 
ATOM   383  C  C     . GLU A 1 66  ? 15.485  57.334 -9.869  1.00 16.58  ? 52   GLU A C     1 
ATOM   384  O  O     . GLU A 1 66  ? 14.430  56.903 -9.392  1.00 16.34  ? 52   GLU A O     1 
ATOM   385  C  CB    . GLU A 1 66  ? 15.265  59.509 -11.058 1.00 16.32  ? 52   GLU A CB    1 
ATOM   386  C  CG    . GLU A 1 66  ? 15.129  61.009 -10.937 1.00 17.44  ? 52   GLU A CG    1 
ATOM   387  C  CD    . GLU A 1 66  ? 16.373  61.745 -11.368 1.00 18.16  ? 52   GLU A CD    1 
ATOM   388  O  OE1   . GLU A 1 66  ? 17.384  61.086 -11.718 1.00 14.85  ? 52   GLU A OE1   1 
ATOM   389  O  OE2   . GLU A 1 66  ? 16.318  62.990 -11.375 1.00 16.13  ? 52   GLU A OE2   1 
ATOM   390  N  N     . LEU A 1 67  ? 16.355  56.535 -10.483 1.00 17.18  ? 53   LEU A N     1 
ATOM   391  C  CA    . LEU A 1 67  ? 16.098  55.104 -10.462 1.00 16.96  ? 53   LEU A CA    1 
ATOM   392  C  C     . LEU A 1 67  ? 16.044  54.604 -9.027  1.00 15.91  ? 53   LEU A C     1 
ATOM   393  O  O     . LEU A 1 67  ? 15.092  53.927 -8.628  1.00 15.76  ? 53   LEU A O     1 
ATOM   394  C  CB    . LEU A 1 67  ? 17.160  54.354 -11.258 1.00 14.45  ? 53   LEU A CB    1 
ATOM   395  C  CG    . LEU A 1 67  ? 16.968  52.828 -11.285 1.00 16.35  ? 53   LEU A CG    1 
ATOM   396  C  CD1   . LEU A 1 67  ? 15.618  52.446 -11.857 1.00 16.00  ? 53   LEU A CD1   1 
ATOM   397  C  CD2   . LEU A 1 67  ? 18.115  52.126 -12.040 1.00 14.90  ? 53   LEU A CD2   1 
ATOM   398  N  N     . ASN A 1 68  ? 17.061  54.951 -8.230  1.00 16.36  ? 54   ASN A N     1 
ATOM   399  C  CA    . ASN A 1 68  ? 17.093  54.531 -6.836  1.00 15.92  ? 54   ASN A CA    1 
ATOM   400  C  C     . ASN A 1 68  ? 15.910  55.083 -6.062  1.00 14.78  ? 54   ASN A C     1 
ATOM   401  O  O     . ASN A 1 68  ? 15.402  54.429 -5.144  1.00 16.50  ? 54   ASN A O     1 
ATOM   402  C  CB    . ASN A 1 68  ? 18.395  54.979 -6.165  1.00 16.95  ? 54   ASN A CB    1 
ATOM   403  C  CG    . ASN A 1 68  ? 19.621  54.363 -6.790  1.00 16.29  ? 54   ASN A CG    1 
ATOM   404  O  OD1   . ASN A 1 68  ? 19.528  53.494 -7.667  1.00 16.69  ? 54   ASN A OD1   1 
ATOM   405  N  ND2   . ASN A 1 68  ? 20.792  54.795 -6.325  1.00 16.96  ? 54   ASN A ND2   1 
ATOM   406  N  N     . ALA A 1 69  ? 15.521  56.324 -6.351  1.00 14.24  ? 55   ALA A N     1 
ATOM   407  C  CA    . ALA A 1 69  ? 14.370  56.895 -5.676  1.00 15.24  ? 55   ALA A CA    1 
ATOM   408  C  C     . ALA A 1 69  ? 13.129  56.051 -5.933  1.00 15.29  ? 55   ALA A C     1 
ATOM   409  O  O     . ALA A 1 69  ? 12.343  55.801 -5.016  1.00 17.72  ? 55   ALA A O     1 
ATOM   410  C  CB    . ALA A 1 69  ? 14.155  58.343 -6.128  1.00 13.98  ? 55   ALA A CB    1 
ATOM   411  N  N     . SER A 1 70  ? 12.960  55.567 -7.163  1.00 15.00  ? 56   SER A N     1 
ATOM   412  C  CA    . SER A 1 70  ? 11.769  54.786 -7.481  1.00 16.61  ? 56   SER A CA    1 
ATOM   413  C  C     . SER A 1 70  ? 11.829  53.410 -6.826  1.00 17.26  ? 56   SER A C     1 
ATOM   414  O  O     . SER A 1 70  ? 10.800  52.886 -6.381  1.00 17.52  ? 56   SER A O     1 
ATOM   415  C  CB    . SER A 1 70  ? 11.579  54.704 -9.009  1.00 16.58  ? 56   SER A CB    1 
ATOM   416  O  OG    . SER A 1 70  ? 12.559  53.916 -9.674  1.00 15.07  ? 56   SER A OG    1 
ATOM   417  N  N     . TYR A 1 71  ? 13.028  52.818 -6.743  1.00 17.19  ? 57   TYR A N     1 
ATOM   418  C  CA    . TYR A 1 71  ? 13.207  51.595 -5.958  1.00 16.24  ? 57   TYR A CA    1 
ATOM   419  C  C     . TYR A 1 71  ? 12.904  51.840 -4.477  1.00 17.23  ? 57   TYR A C     1 
ATOM   420  O  O     . TYR A 1 71  ? 12.249  51.019 -3.824  1.00 16.41  ? 57   TYR A O     1 
ATOM   421  C  CB    . TYR A 1 71  ? 14.646  51.072 -6.096  1.00 16.59  ? 57   TYR A CB    1 
ATOM   422  C  CG    . TYR A 1 71  ? 15.087  50.464 -7.441  1.00 15.82  ? 57   TYR A CG    1 
ATOM   423  C  CD1   . TYR A 1 71  ? 14.177  49.874 -8.330  1.00 14.98  ? 57   TYR A CD1   1 
ATOM   424  C  CD2   . TYR A 1 71  ? 16.436  50.472 -7.797  1.00 13.72  ? 57   TYR A CD2   1 
ATOM   425  C  CE1   . TYR A 1 71  ? 14.625  49.322 -9.563  1.00 15.33  ? 57   TYR A CE1   1 
ATOM   426  C  CE2   . TYR A 1 71  ? 16.889  49.914 -9.009  1.00 15.66  ? 57   TYR A CE2   1 
ATOM   427  C  CZ    . TYR A 1 71  ? 15.985  49.341 -9.875  1.00 13.65  ? 57   TYR A CZ    1 
ATOM   428  O  OH    . TYR A 1 71  ? 16.460  48.794 -11.053 1.00 15.71  ? 57   TYR A OH    1 
ATOM   429  N  N     . ALA A 1 72  ? 13.392  52.959 -3.928  1.00 17.90  ? 58   ALA A N     1 
ATOM   430  C  CA    . ALA A 1 72  ? 13.150  53.267 -2.522  1.00 18.27  ? 58   ALA A CA    1 
ATOM   431  C  C     . ALA A 1 72  ? 11.661  53.454 -2.244  1.00 18.18  ? 58   ALA A C     1 
ATOM   432  O  O     . ALA A 1 72  ? 11.145  52.942 -1.244  1.00 17.32  ? 58   ALA A O     1 
ATOM   433  C  CB    . ALA A 1 72  ? 13.947  54.509 -2.107  1.00 16.45  ? 58   ALA A CB    1 
ATOM   434  N  N     . ALA A 1 73  ? 10.944  54.162 -3.126  1.00 18.38  ? 59   ALA A N     1 
ATOM   435  C  CA    . ALA A 1 73  ? 9.501   54.301 -2.945  1.00 17.60  ? 59   ALA A CA    1 
ATOM   436  C  C     . ALA A 1 73  ? 8.815   52.942 -2.979  1.00 17.26  ? 59   ALA A C     1 
ATOM   437  O  O     . ALA A 1 73  ? 7.893   52.683 -2.203  1.00 16.80  ? 59   ALA A O     1 
ATOM   438  C  CB    . ALA A 1 73  ? 8.910   55.210 -4.023  1.00 17.35  ? 59   ALA A CB    1 
ATOM   439  N  N     . ASP A 1 74  ? 9.270   52.053 -3.857  1.00 15.75  ? 60   ASP A N     1 
ATOM   440  C  CA    . ASP A 1 74  ? 8.698   50.712 -3.917  1.00 16.49  ? 60   ASP A CA    1 
ATOM   441  C  C     . ASP A 1 74  ? 8.847   49.992 -2.578  1.00 17.76  ? 60   ASP A C     1 
ATOM   442  O  O     . ASP A 1 74  ? 7.864   49.481 -2.023  1.00 16.80  ? 60   ASP A O     1 
ATOM   443  C  CB    . ASP A 1 74  ? 9.369   49.941 -5.060  1.00 17.81  ? 60   ASP A CB    1 
ATOM   444  C  CG    . ASP A 1 74  ? 8.726   48.592 -5.333  1.00 15.92  ? 60   ASP A CG    1 
ATOM   445  O  OD1   . ASP A 1 74  ? 8.735   47.740 -4.431  1.00 16.54  ? 60   ASP A OD1   1 
ATOM   446  O  OD2   . ASP A 1 74  ? 8.244   48.363 -6.464  1.00 18.58  ? 60   ASP A OD2   1 
ATOM   447  N  N     . GLY A 1 75  ? 10.066  49.970 -2.027  1.00 17.45  ? 61   GLY A N     1 
ATOM   448  C  CA    . GLY A 1 75  ? 10.270  49.351 -0.723  1.00 16.98  ? 61   GLY A CA    1 
ATOM   449  C  C     . GLY A 1 75  ? 9.449   49.993 0.379   1.00 18.93  ? 61   GLY A C     1 
ATOM   450  O  O     . GLY A 1 75  ? 8.921   49.306 1.258   1.00 17.16  ? 61   GLY A O     1 
ATOM   451  N  N     . TYR A 1 76  ? 9.360   51.325 0.367   1.00 17.62  ? 62   TYR A N     1 
ATOM   452  C  CA    . TYR A 1 76  ? 8.504   52.029 1.318   1.00 18.99  ? 62   TYR A CA    1 
ATOM   453  C  C     . TYR A 1 76  ? 7.052   51.573 1.183   1.00 19.40  ? 62   TYR A C     1 
ATOM   454  O  O     . TYR A 1 76  ? 6.393   51.233 2.180   1.00 17.70  ? 62   TYR A O     1 
ATOM   455  C  CB    . TYR A 1 76  ? 8.666   53.532 1.076   1.00 18.86  ? 62   TYR A CB    1 
ATOM   456  C  CG    . TYR A 1 76  ? 7.939   54.486 1.986   1.00 20.88  ? 62   TYR A CG    1 
ATOM   457  C  CD1   . TYR A 1 76  ? 6.607   54.829 1.747   1.00 19.81  ? 62   TYR A CD1   1 
ATOM   458  C  CD2   . TYR A 1 76  ? 8.594   55.088 3.057   1.00 21.47  ? 62   TYR A CD2   1 
ATOM   459  C  CE1   . TYR A 1 76  ? 5.948   55.723 2.557   1.00 20.94  ? 62   TYR A CE1   1 
ATOM   460  C  CE2   . TYR A 1 76  ? 7.943   55.990 3.882   1.00 22.21  ? 62   TYR A CE2   1 
ATOM   461  C  CZ    . TYR A 1 76  ? 6.616   56.300 3.629   1.00 24.44  ? 62   TYR A CZ    1 
ATOM   462  O  OH    . TYR A 1 76  ? 5.961   57.202 4.433   1.00 23.17  ? 62   TYR A OH    1 
ATOM   463  N  N     . ALA A 1 77  ? 6.549   51.511 -0.058  1.00 17.56  ? 63   ALA A N     1 
ATOM   464  C  CA    . ALA A 1 77  ? 5.162   51.096 -0.270  1.00 18.59  ? 63   ALA A CA    1 
ATOM   465  C  C     . ALA A 1 77  ? 4.918   49.668 0.196   1.00 18.03  ? 63   ALA A C     1 
ATOM   466  O  O     . ALA A 1 77  ? 3.811   49.344 0.633   1.00 19.33  ? 63   ALA A O     1 
ATOM   467  C  CB    . ALA A 1 77  ? 4.777   51.229 -1.748  1.00 18.11  ? 63   ALA A CB    1 
ATOM   468  N  N     . ARG A 1 78  ? 5.924   48.794 0.107   1.00 19.18  ? 64   ARG A N     1 
ATOM   469  C  CA    . ARG A 1 78  ? 5.767   47.446 0.645   1.00 17.94  ? 64   ARG A CA    1 
ATOM   470  C  C     . ARG A 1 78  ? 5.794   47.417 2.167   1.00 19.64  ? 64   ARG A C     1 
ATOM   471  O  O     . ARG A 1 78  ? 5.512   46.369 2.762   1.00 20.09  ? 64   ARG A O     1 
ATOM   472  C  CB    . ARG A 1 78  ? 6.846   46.520 0.086   1.00 17.57  ? 64   ARG A CB    1 
ATOM   473  C  CG    . ARG A 1 78  ? 6.753   46.314 -1.437  1.00 18.48  ? 64   ARG A CG    1 
ATOM   474  C  CD    . ARG A 1 78  ? 7.816   45.314 -1.887  1.00 18.30  ? 64   ARG A CD    1 
ATOM   475  N  NE    . ARG A 1 78  ? 7.997   45.234 -3.334  1.00 17.43  ? 64   ARG A NE    1 
ATOM   476  C  CZ    . ARG A 1 78  ? 8.306   44.105 -3.959  1.00 17.64  ? 64   ARG A CZ    1 
ATOM   477  N  NH1   . ARG A 1 78  ? 8.370   42.957 -3.309  1.00 16.97  ? 64   ARG A NH1   1 
ATOM   478  N  NH2   . ARG A 1 78  ? 8.554   44.126 -5.265  1.00 16.29  ? 64   ARG A NH2   1 
ATOM   479  N  N     . CYS A 1 79  ? 6.143   48.522 2.810   1.00 18.44  ? 65   CYS A N     1 
ATOM   480  C  CA    . CYS A 1 79  ? 6.047   48.609 4.255   1.00 22.89  ? 65   CYS A CA    1 
ATOM   481  C  C     . CYS A 1 79  ? 4.820   49.379 4.696   1.00 22.56  ? 65   CYS A C     1 
ATOM   482  O  O     . CYS A 1 79  ? 4.204   49.024 5.700   1.00 23.89  ? 65   CYS A O     1 
ATOM   483  C  CB    . CYS A 1 79  ? 7.295   49.279 4.839   1.00 21.03  ? 65   CYS A CB    1 
ATOM   484  S  SG    . CYS A 1 79  ? 8.772   48.301 4.646   1.00 25.34  ? 65   CYS A SG    1 
ATOM   485  N  N     . LYS A 1 80  ? 4.443   50.417 3.953   1.00 23.68  ? 66   LYS A N     1 
ATOM   486  C  CA    . LYS A 1 80  ? 3.363   51.295 4.367   1.00 25.73  ? 66   LYS A CA    1 
ATOM   487  C  C     . LYS A 1 80  ? 2.098   51.167 3.531   1.00 27.16  ? 66   LYS A C     1 
ATOM   488  O  O     . LYS A 1 80  ? 1.084   51.778 3.887   1.00 28.51  ? 66   LYS A O     1 
ATOM   489  C  CB    . LYS A 1 80  ? 3.852   52.751 4.364   1.00 24.99  ? 66   LYS A CB    1 
ATOM   490  C  CG    . LYS A 1 80  ? 5.014   52.923 5.348   1.00 26.82  ? 66   LYS A CG    1 
ATOM   491  C  CD    . LYS A 1 80  ? 5.065   54.301 5.950   1.00 27.57  ? 66   LYS A CD    1 
ATOM   492  C  CE    . LYS A 1 80  ? 3.990   54.444 6.991   1.00 32.03  ? 66   LYS A CE    1 
ATOM   493  N  NZ    . LYS A 1 80  ? 4.111   55.726 7.721   1.00 35.85  ? 66   LYS A NZ    1 
ATOM   494  N  N     . GLY A 1 81  ? 2.113   50.373 2.461   1.00 25.17  ? 67   GLY A N     1 
ATOM   495  C  CA    . GLY A 1 81  ? 0.943   50.193 1.623   1.00 24.93  ? 67   GLY A CA    1 
ATOM   496  C  C     . GLY A 1 81  ? 0.761   51.233 0.548   1.00 25.11  ? 67   GLY A C     1 
ATOM   497  O  O     . GLY A 1 81  ? -0.191  51.131 -0.232  1.00 24.42  ? 67   GLY A O     1 
ATOM   498  N  N     . PHE A 1 82  ? 1.635   52.232 0.483   1.00 23.74  ? 68   PHE A N     1 
ATOM   499  C  CA    . PHE A 1 82  ? 1.548   53.317 -0.484  1.00 23.63  ? 68   PHE A CA    1 
ATOM   500  C  C     . PHE A 1 82  ? 2.866   54.077 -0.460  1.00 22.44  ? 68   PHE A C     1 
ATOM   501  O  O     . PHE A 1 82  ? 3.566   54.075 0.557   1.00 21.35  ? 68   PHE A O     1 
ATOM   502  C  CB    . PHE A 1 82  ? 0.385   54.263 -0.152  1.00 24.65  ? 68   PHE A CB    1 
ATOM   503  C  CG    . PHE A 1 82  ? 0.127   55.303 -1.203  1.00 23.06  ? 68   PHE A CG    1 
ATOM   504  C  CD1   . PHE A 1 82  ? -0.717  55.030 -2.268  1.00 24.17  ? 68   PHE A CD1   1 
ATOM   505  C  CD2   . PHE A 1 82  ? 0.729   56.549 -1.129  1.00 23.41  ? 68   PHE A CD2   1 
ATOM   506  C  CE1   . PHE A 1 82  ? -0.971  55.984 -3.247  1.00 23.58  ? 68   PHE A CE1   1 
ATOM   507  C  CE2   . PHE A 1 82  ? 0.489   57.511 -2.110  1.00 26.21  ? 68   PHE A CE2   1 
ATOM   508  C  CZ    . PHE A 1 82  ? -0.360  57.222 -3.173  1.00 24.03  ? 68   PHE A CZ    1 
ATOM   509  N  N     . ALA A 1 83  ? 3.206   54.705 -1.586  1.00 19.19  ? 69   ALA A N     1 
ATOM   510  C  CA    . ALA A 1 83  ? 4.405   55.529 -1.662  1.00 20.22  ? 69   ALA A CA    1 
ATOM   511  C  C     . ALA A 1 83  ? 4.254   56.518 -2.807  1.00 20.03  ? 69   ALA A C     1 
ATOM   512  O  O     . ALA A 1 83  ? 3.411   56.353 -3.690  1.00 17.17  ? 69   ALA A O     1 
ATOM   513  C  CB    . ALA A 1 83  ? 5.675   54.691 -1.849  1.00 16.97  ? 69   ALA A CB    1 
ATOM   514  N  N     . ALA A 1 84  ? 5.132   57.523 -2.805  1.00 19.59  ? 70   ALA A N     1 
ATOM   515  C  CA    . ALA A 1 84  ? 5.112   58.589 -3.790  1.00 17.70  ? 70   ALA A CA    1 
ATOM   516  C  C     . ALA A 1 84  ? 6.529   58.937 -4.227  1.00 18.32  ? 70   ALA A C     1 
ATOM   517  O  O     . ALA A 1 84  ? 7.466   58.984 -3.418  1.00 16.09  ? 70   ALA A O     1 
ATOM   518  C  CB    . ALA A 1 84  ? 4.426   59.841 -3.239  1.00 20.23  ? 70   ALA A CB    1 
ATOM   519  N  N     . LEU A 1 85  ? 6.662   59.207 -5.509  1.00 17.67  ? 71   LEU A N     1 
ATOM   520  C  CA    . LEU A 1 85  ? 7.925   59.568 -6.134  1.00 17.90  ? 71   LEU A CA    1 
ATOM   521  C  C     . LEU A 1 85  ? 7.749   60.902 -6.844  1.00 16.89  ? 71   LEU A C     1 
ATOM   522  O  O     . LEU A 1 85  ? 6.716   61.134 -7.480  1.00 17.94  ? 71   LEU A O     1 
ATOM   523  C  CB    . LEU A 1 85  ? 8.346   58.477 -7.113  1.00 15.80  ? 71   LEU A CB    1 
ATOM   524  C  CG    . LEU A 1 85  ? 9.431   58.753 -8.140  1.00 17.98  ? 71   LEU A CG    1 
ATOM   525  C  CD1   . LEU A 1 85  ? 10.770  58.815 -7.435  1.00 14.63  ? 71   LEU A CD1   1 
ATOM   526  C  CD2   . LEU A 1 85  ? 9.426   57.672 -9.215  1.00 16.77  ? 71   LEU A CD2   1 
ATOM   527  N  N     . LEU A 1 86  ? 8.737   61.789 -6.711  1.00 17.42  ? 72   LEU A N     1 
ATOM   528  C  CA    . LEU A 1 86  ? 8.764   63.063 -7.429  1.00 17.92  ? 72   LEU A CA    1 
ATOM   529  C  C     . LEU A 1 86  ? 9.992   63.112 -8.332  1.00 18.34  ? 72   LEU A C     1 
ATOM   530  O  O     . LEU A 1 86  ? 11.116  62.951 -7.851  1.00 17.47  ? 72   LEU A O     1 
ATOM   531  C  CB    . LEU A 1 86  ? 8.795   64.242 -6.446  1.00 19.16  ? 72   LEU A CB    1 
ATOM   532  C  CG    . LEU A 1 86  ? 8.940   65.634 -7.087  1.00 19.99  ? 72   LEU A CG    1 
ATOM   533  C  CD1   . LEU A 1 86  ? 7.745   65.964 -7.980  1.00 19.70  ? 72   LEU A CD1   1 
ATOM   534  C  CD2   . LEU A 1 86  ? 9.168   66.727 -6.027  1.00 21.11  ? 72   LEU A CD2   1 
ATOM   535  N  N     . THR A 1 87  ? 9.786   63.350 -9.631  1.00 15.98  ? 73   THR A N     1 
ATOM   536  C  CA    . THR A 1 87  ? 10.890  63.519 -10.571 1.00 16.75  ? 73   THR A CA    1 
ATOM   537  C  C     . THR A 1 87  ? 10.676  64.805 -11.358 1.00 18.02  ? 73   THR A C     1 
ATOM   538  O  O     . THR A 1 87  ? 9.613   65.438 -11.284 1.00 16.76  ? 73   THR A O     1 
ATOM   539  C  CB    . THR A 1 87  ? 11.020  62.319 -11.535 1.00 15.50  ? 73   THR A CB    1 
ATOM   540  O  OG1   . THR A 1 87  ? 9.868   62.242 -12.402 1.00 15.60  ? 73   THR A OG1   1 
ATOM   541  C  CG2   . THR A 1 87  ? 11.171  61.021 -10.761 1.00 15.51  ? 73   THR A CG2   1 
ATOM   542  N  N     . THR A 1 88  ? 11.695  65.205 -12.113 1.00 18.17  ? 74   THR A N     1 
ATOM   543  C  CA    . THR A 1 88  ? 11.538  66.329 -13.023 1.00 18.26  ? 74   THR A CA    1 
ATOM   544  C  C     . THR A 1 88  ? 11.253  65.821 -14.435 1.00 19.50  ? 74   THR A C     1 
ATOM   545  O  O     . THR A 1 88  ? 11.563  64.677 -14.791 1.00 17.54  ? 74   THR A O     1 
ATOM   546  C  CB    . THR A 1 88  ? 12.765  67.255 -13.003 1.00 21.58  ? 74   THR A CB    1 
ATOM   547  O  OG1   . THR A 1 88  ? 12.435  68.479 -13.669 1.00 18.99  ? 74   THR A OG1   1 
ATOM   548  C  CG2   . THR A 1 88  ? 13.971  66.623 -13.709 1.00 20.06  ? 74   THR A CG2   1 
ATOM   549  N  N     . PHE A 1 89  ? 10.589  66.675 -15.209 1.00 20.25  ? 75   PHE A N     1 
ATOM   550  C  CA    . PHE A 1 89  ? 10.165  66.357 -16.567 1.00 18.17  ? 75   PHE A CA    1 
ATOM   551  C  C     . PHE A 1 89  ? 11.311  65.791 -17.400 1.00 18.59  ? 75   PHE A C     1 
ATOM   552  O  O     . PHE A 1 89  ? 12.436  66.315 -17.398 1.00 17.13  ? 75   PHE A O     1 
ATOM   553  C  CB    . PHE A 1 89  ? 9.597   67.623 -17.207 1.00 19.14  ? 75   PHE A CB    1 
ATOM   554  C  CG    . PHE A 1 89  ? 9.038   67.432 -18.589 1.00 21.27  ? 75   PHE A CG    1 
ATOM   555  C  CD1   . PHE A 1 89  ? 7.714   67.063 -18.774 1.00 19.64  ? 75   PHE A CD1   1 
ATOM   556  C  CD2   . PHE A 1 89  ? 9.826   67.667 -19.708 1.00 18.59  ? 75   PHE A CD2   1 
ATOM   557  C  CE1   . PHE A 1 89  ? 7.184   66.920 -20.045 1.00 20.55  ? 75   PHE A CE1   1 
ATOM   558  C  CE2   . PHE A 1 89  ? 9.307   67.512 -20.980 1.00 19.43  ? 75   PHE A CE2   1 
ATOM   559  C  CZ    . PHE A 1 89  ? 7.978   67.142 -21.151 1.00 19.18  ? 75   PHE A CZ    1 
ATOM   560  N  N     . GLY A 1 90  ? 11.030  64.678 -18.061 1.00 15.51  ? 76   GLY A N     1 
ATOM   561  C  CA    . GLY A 1 90  ? 11.938  64.107 -19.036 1.00 18.54  ? 76   GLY A CA    1 
ATOM   562  C  C     . GLY A 1 90  ? 13.098  63.341 -18.438 1.00 16.57  ? 76   GLY A C     1 
ATOM   563  O  O     . GLY A 1 90  ? 13.053  62.111 -18.332 1.00 16.49  ? 76   GLY A O     1 
ATOM   564  N  N     . VAL A 1 91  ? 14.130  64.062 -18.003 1.00 16.22  ? 77   VAL A N     1 
ATOM   565  C  CA    . VAL A 1 91  ? 15.337  63.397 -17.530 1.00 17.19  ? 77   VAL A CA    1 
ATOM   566  C  C     . VAL A 1 91  ? 15.053  62.646 -16.235 1.00 16.44  ? 77   VAL A C     1 
ATOM   567  O  O     . VAL A 1 91  ? 15.619  61.578 -15.985 1.00 16.86  ? 77   VAL A O     1 
ATOM   568  C  CB    . VAL A 1 91  ? 16.491  64.407 -17.379 1.00 16.99  ? 77   VAL A CB    1 
ATOM   569  C  CG1   . VAL A 1 91  ? 16.802  65.046 -18.725 1.00 17.84  ? 77   VAL A CG1   1 
ATOM   570  C  CG2   . VAL A 1 91  ? 16.184  65.481 -16.321 1.00 18.27  ? 77   VAL A CG2   1 
ATOM   571  N  N     . GLY A 1 92  ? 14.197  63.196 -15.385 1.00 17.29  ? 78   GLY A N     1 
ATOM   572  C  CA    . GLY A 1 92  ? 13.894  62.535 -14.127 1.00 16.12  ? 78   GLY A CA    1 
ATOM   573  C  C     . GLY A 1 92  ? 12.952  61.360 -14.298 1.00 16.35  ? 78   GLY A C     1 
ATOM   574  O  O     . GLY A 1 92  ? 13.262  60.242 -13.883 1.00 15.42  ? 78   GLY A O     1 
ATOM   575  N  N     . GLU A 1 93  ? 11.793  61.593 -14.918 1.00 15.81  ? 79   GLU A N     1 
ATOM   576  C  CA    . GLU A 1 93  ? 10.798  60.529 -15.028 1.00 15.80  ? 79   GLU A CA    1 
ATOM   577  C  C     . GLU A 1 93  ? 11.325  59.340 -15.837 1.00 15.97  ? 79   GLU A C     1 
ATOM   578  O  O     . GLU A 1 93  ? 11.028  58.189 -15.513 1.00 16.37  ? 79   GLU A O     1 
ATOM   579  C  CB    . GLU A 1 93  ? 9.512   61.076 -15.664 1.00 16.12  ? 79   GLU A CB    1 
ATOM   580  C  CG    . GLU A 1 93  ? 9.680   61.599 -17.112 1.00 16.85  ? 79   GLU A CG    1 
ATOM   581  C  CD    . GLU A 1 93  ? 8.415   62.276 -17.599 1.00 16.54  ? 79   GLU A CD    1 
ATOM   582  O  OE1   . GLU A 1 93  ? 7.331   61.649 -17.524 1.00 16.54  ? 79   GLU A OE1   1 
ATOM   583  O  OE2   . GLU A 1 93  ? 8.490   63.457 -17.984 1.00 16.46  ? 79   GLU A OE2   1 
ATOM   584  N  N     . LEU A 1 94  ? 12.108  59.591 -16.891 1.00 14.86  ? 80   LEU A N     1 
ATOM   585  C  CA    . LEU A 1 94  ? 12.620  58.471 -17.687 1.00 15.21  ? 80   LEU A CA    1 
ATOM   586  C  C     . LEU A 1 94  ? 13.712  57.695 -16.951 1.00 15.84  ? 80   LEU A C     1 
ATOM   587  O  O     . LEU A 1 94  ? 13.886  56.496 -17.201 1.00 14.81  ? 80   LEU A O     1 
ATOM   588  C  CB    . LEU A 1 94  ? 13.132  58.970 -19.045 1.00 17.18  ? 80   LEU A CB    1 
ATOM   589  C  CG    . LEU A 1 94  ? 12.012  59.415 -20.004 1.00 19.24  ? 80   LEU A CG    1 
ATOM   590  C  CD1   . LEU A 1 94  ? 12.512  59.654 -21.431 1.00 17.71  ? 80   LEU A CD1   1 
ATOM   591  C  CD2   . LEU A 1 94  ? 10.814  58.452 -20.007 1.00 18.78  ? 80   LEU A CD2   1 
ATOM   592  N  N     . SER A 1 95  ? 14.460  58.347 -16.051 1.00 15.03  ? 81   SER A N     1 
ATOM   593  C  CA    . SER A 1 95  ? 15.402  57.609 -15.218 1.00 15.16  ? 81   SER A CA    1 
ATOM   594  C  C     . SER A 1 95  ? 14.681  56.652 -14.274 1.00 15.63  ? 81   SER A C     1 
ATOM   595  O  O     . SER A 1 95  ? 15.247  55.623 -13.894 1.00 14.27  ? 81   SER A O     1 
ATOM   596  C  CB    . SER A 1 95  ? 16.287  58.573 -14.419 1.00 16.71  ? 81   SER A CB    1 
ATOM   597  O  OG    . SER A 1 95  ? 17.190  59.292 -15.268 1.00 16.71  ? 81   SER A OG    1 
ATOM   598  N  N     . ALA A 1 96  ? 13.436  56.958 -13.896 1.00 15.45  ? 82   ALA A N     1 
ATOM   599  C  CA    . ALA A 1 96  ? 12.690  56.149 -12.932 1.00 15.88  ? 82   ALA A CA    1 
ATOM   600  C  C     . ALA A 1 96  ? 11.788  55.102 -13.582 1.00 15.12  ? 82   ALA A C     1 
ATOM   601  O  O     . ALA A 1 96  ? 11.070  54.386 -12.875 1.00 14.20  ? 82   ALA A O     1 
ATOM   602  C  CB    . ALA A 1 96  ? 11.849  57.058 -12.025 1.00 16.25  ? 82   ALA A CB    1 
ATOM   603  N  N     . MET A 1 97  ? 11.797  54.990 -14.903 1.00 15.45  ? 83   MET A N     1 
ATOM   604  C  CA    . MET A 1 97  ? 10.794  54.161 -15.558 1.00 16.34  ? 83   MET A CA    1 
ATOM   605  C  C     . MET A 1 97  ? 10.902  52.700 -15.151 1.00 15.26  ? 83   MET A C     1 
ATOM   606  O  O     . MET A 1 97  ? 9.878   52.025 -14.985 1.00 15.20  ? 83   MET A O     1 
ATOM   607  C  CB    . MET A 1 97  ? 10.906  54.320 -17.068 1.00 17.08  ? 83   MET A CB    1 
ATOM   608  C  CG    . MET A 1 97  ? 10.070  53.340 -17.811 1.00 20.70  ? 83   MET A CG    1 
ATOM   609  S  SD    . MET A 1 97  ? 9.599   54.077 -19.367 1.00 43.02  ? 83   MET A SD    1 
ATOM   610  C  CE    . MET A 1 97  ? 8.549   55.458 -18.881 1.00 22.82  ? 83   MET A CE    1 
ATOM   611  N  N     . ASN A 1 98  ? 12.133  52.182 -15.021 1.00 14.71  ? 84   ASN A N     1 
ATOM   612  C  CA    . ASN A 1 98  ? 12.325  50.786 -14.624 1.00 15.20  ? 84   ASN A CA    1 
ATOM   613  C  C     . ASN A 1 98  ? 11.790  50.516 -13.217 1.00 14.76  ? 84   ASN A C     1 
ATOM   614  O  O     . ASN A 1 98  ? 11.304  49.415 -12.931 1.00 15.77  ? 84   ASN A O     1 
ATOM   615  C  CB    . ASN A 1 98  ? 13.809  50.418 -14.704 1.00 13.82  ? 84   ASN A CB    1 
ATOM   616  C  CG    . ASN A 1 98  ? 14.049  48.932 -14.471 1.00 15.09  ? 84   ASN A CG    1 
ATOM   617  O  OD1   . ASN A 1 98  ? 13.342  48.081 -15.022 1.00 16.40  ? 84   ASN A OD1   1 
ATOM   618  N  ND2   . ASN A 1 98  ? 15.020  48.614 -13.622 1.00 15.33  ? 84   ASN A ND2   1 
ATOM   619  N  N     . GLY A 1 99  ? 11.904  51.489 -12.313 1.00 14.24  ? 85   GLY A N     1 
ATOM   620  C  CA    . GLY A 1 99  ? 11.290  51.331 -11.003 1.00 15.38  ? 85   GLY A CA    1 
ATOM   621  C  C     . GLY A 1 99  ? 9.775   51.251 -11.087 1.00 14.79  ? 85   GLY A C     1 
ATOM   622  O  O     . GLY A 1 99  ? 9.155   50.329 -10.555 1.00 16.25  ? 85   GLY A O     1 
ATOM   623  N  N     . ILE A 1 100 ? 9.163   52.187 -11.804 1.00 15.57  ? 86   ILE A N     1 
ATOM   624  C  CA    . ILE A 1 100 ? 7.704   52.181 -11.907 1.00 16.69  ? 86   ILE A CA    1 
ATOM   625  C  C     . ILE A 1 100 ? 7.228   50.904 -12.588 1.00 15.97  ? 86   ILE A C     1 
ATOM   626  O  O     . ILE A 1 100 ? 6.213   50.319 -12.195 1.00 15.91  ? 86   ILE A O     1 
ATOM   627  C  CB    . ILE A 1 100 ? 7.211   53.446 -12.636 1.00 16.61  ? 86   ILE A CB    1 
ATOM   628  C  CG1   . ILE A 1 100 ? 7.571   54.680 -11.815 1.00 16.13  ? 86   ILE A CG1   1 
ATOM   629  C  CG2   . ILE A 1 100 ? 5.682   53.384 -12.891 1.00 17.13  ? 86   ILE A CG2   1 
ATOM   630  C  CD1   . ILE A 1 100 ? 6.965   54.644 -10.351 1.00 18.98  ? 86   ILE A CD1   1 
ATOM   631  N  N     . ALA A 1 101 ? 7.971   50.441 -13.601 1.00 15.16  ? 87   ALA A N     1 
ATOM   632  C  CA    . ALA A 1 101 ? 7.657   49.182 -14.275 1.00 16.86  ? 87   ALA A CA    1 
ATOM   633  C  C     . ALA A 1 101 ? 7.659   48.000 -13.313 1.00 16.54  ? 87   ALA A C     1 
ATOM   634  O  O     . ALA A 1 101 ? 6.797   47.112 -13.403 1.00 16.32  ? 87   ALA A O     1 
ATOM   635  C  CB    . ALA A 1 101 ? 8.670   48.930 -15.393 1.00 14.45  ? 87   ALA A CB    1 
ATOM   636  N  N     . GLY A 1 102 ? 8.661   47.932 -12.436 1.00 14.55  ? 88   GLY A N     1 
ATOM   637  C  CA    . GLY A 1 102 ? 8.702   46.873 -11.442 1.00 14.92  ? 88   GLY A CA    1 
ATOM   638  C  C     . GLY A 1 102 ? 7.608   46.996 -10.404 1.00 16.11  ? 88   GLY A C     1 
ATOM   639  O  O     . GLY A 1 102 ? 7.053   45.990 -9.948  1.00 16.16  ? 88   GLY A O     1 
ATOM   640  N  N     . SER A 1 103 ? 7.262   48.226 -10.029 1.00 16.01  ? 89   SER A N     1 
ATOM   641  C  CA    . SER A 1 103 ? 6.118   48.399 -9.145  1.00 16.67  ? 89   SER A CA    1 
ATOM   642  C  C     . SER A 1 103 ? 4.835   47.928 -9.827  1.00 15.76  ? 89   SER A C     1 
ATOM   643  O  O     . SER A 1 103 ? 3.983   47.305 -9.189  1.00 17.54  ? 89   SER A O     1 
ATOM   644  C  CB    . SER A 1 103 ? 6.017   49.855 -8.698  1.00 15.42  ? 89   SER A CB    1 
ATOM   645  O  OG    . SER A 1 103 ? 7.203   50.249 -7.991  1.00 17.72  ? 89   SER A OG    1 
ATOM   646  N  N     . TYR A 1 104 ? 4.679   48.203 -11.130 1.00 17.73  ? 90   TYR A N     1 
ATOM   647  C  CA    . TYR A 1 104 ? 3.498   47.701 -11.833 1.00 16.39  ? 90   TYR A CA    1 
ATOM   648  C  C     . TYR A 1 104 ? 3.504   46.177 -11.896 1.00 16.58  ? 90   TYR A C     1 
ATOM   649  O  O     . TYR A 1 104 ? 2.495   45.527 -11.597 1.00 17.22  ? 90   TYR A O     1 
ATOM   650  C  CB    . TYR A 1 104 ? 3.415   48.314 -13.234 1.00 17.15  ? 90   TYR A CB    1 
ATOM   651  C  CG    . TYR A 1 104 ? 2.168   47.940 -14.013 1.00 19.09  ? 90   TYR A CG    1 
ATOM   652  C  CD1   . TYR A 1 104 ? 2.125   46.783 -14.785 1.00 20.43  ? 90   TYR A CD1   1 
ATOM   653  C  CD2   . TYR A 1 104 ? 1.027   48.735 -13.960 1.00 18.80  ? 90   TYR A CD2   1 
ATOM   654  C  CE1   . TYR A 1 104 ? 0.988   46.433 -15.489 1.00 18.74  ? 90   TYR A CE1   1 
ATOM   655  C  CE2   . TYR A 1 104 ? -0.107  48.405 -14.678 1.00 19.81  ? 90   TYR A CE2   1 
ATOM   656  C  CZ    . TYR A 1 104 ? -0.124  47.240 -15.433 1.00 21.01  ? 90   TYR A CZ    1 
ATOM   657  O  OH    . TYR A 1 104 ? -1.251  46.885 -16.150 1.00 23.58  ? 90   TYR A OH    1 
ATOM   658  N  N     . ALA A 1 105 ? 4.646   45.587 -12.260 1.00 16.98  ? 91   ALA A N     1 
ATOM   659  C  CA    . ALA A 1 105 ? 4.723   44.135 -12.401 1.00 17.29  ? 91   ALA A CA    1 
ATOM   660  C  C     . ALA A 1 105 ? 4.378   43.430 -11.096 1.00 18.42  ? 91   ALA A C     1 
ATOM   661  O  O     . ALA A 1 105 ? 3.729   42.384 -11.105 1.00 16.35  ? 91   ALA A O     1 
ATOM   662  C  CB    . ALA A 1 105 ? 6.120   43.708 -12.870 1.00 15.00  ? 91   ALA A CB    1 
ATOM   663  N  N     . GLU A 1 106 ? 4.810   43.977 -9.965  1.00 17.57  ? 92   GLU A N     1 
ATOM   664  C  CA    . GLU A 1 106 ? 4.640   43.298 -8.691  1.00 17.53  ? 92   GLU A CA    1 
ATOM   665  C  C     . GLU A 1 106 ? 3.530   43.915 -7.841  1.00 18.48  ? 92   GLU A C     1 
ATOM   666  O  O     . GLU A 1 106 ? 3.432   43.612 -6.649  1.00 17.31  ? 92   GLU A O     1 
ATOM   667  C  CB    . GLU A 1 106 ? 5.966   43.286 -7.934  1.00 16.87  ? 92   GLU A CB    1 
ATOM   668  C  CG    . GLU A 1 106 ? 7.156   42.801 -8.763  1.00 16.58  ? 92   GLU A CG    1 
ATOM   669  C  CD    . GLU A 1 106 ? 8.033   41.770 -8.051  1.00 17.62  ? 92   GLU A CD    1 
ATOM   670  O  OE1   . GLU A 1 106 ? 8.031   41.713 -6.797  1.00 16.49  ? 92   GLU A OE1   1 
ATOM   671  O  OE2   . GLU A 1 106 ? 8.763   41.029 -8.751  1.00 18.38  ? 92   GLU A OE2   1 
ATOM   672  N  N     . HIS A 1 107 ? 2.696   44.768 -8.437  1.00 18.17  ? 93   HIS A N     1 
ATOM   673  C  CA    . HIS A 1 107 ? 1.505   45.320 -7.797  1.00 19.81  ? 93   HIS A CA    1 
ATOM   674  C  C     . HIS A 1 107 ? 1.869   46.121 -6.547  1.00 19.31  ? 93   HIS A C     1 
ATOM   675  O  O     . HIS A 1 107 ? 1.398   45.850 -5.443  1.00 20.48  ? 93   HIS A O     1 
ATOM   676  C  CB    . HIS A 1 107 ? 0.500   44.220 -7.464  1.00 18.40  ? 93   HIS A CB    1 
ATOM   677  C  CG    . HIS A 1 107 ? -0.195  43.653 -8.661  1.00 21.06  ? 93   HIS A CG    1 
ATOM   678  N  ND1   . HIS A 1 107 ? 0.448   42.869 -9.597  1.00 21.75  ? 93   HIS A ND1   1 
ATOM   679  C  CD2   . HIS A 1 107 ? -1.477  43.768 -9.081  1.00 20.34  ? 93   HIS A CD2   1 
ATOM   680  C  CE1   . HIS A 1 107 ? -0.416  42.508 -10.532 1.00 21.97  ? 93   HIS A CE1   1 
ATOM   681  N  NE2   . HIS A 1 107 ? -1.593  43.036 -10.238 1.00 23.35  ? 93   HIS A NE2   1 
ATOM   682  N  N     . VAL A 1 108 ? 2.713   47.123 -6.743  1.00 19.58  ? 94   VAL A N     1 
ATOM   683  C  CA    . VAL A 1 108 ? 3.150   48.019 -5.676  1.00 16.46  ? 94   VAL A CA    1 
ATOM   684  C  C     . VAL A 1 108 ? 2.614   49.408 -6.001  1.00 18.28  ? 94   VAL A C     1 
ATOM   685  O  O     . VAL A 1 108 ? 2.933   49.954 -7.071  1.00 17.51  ? 94   VAL A O     1 
ATOM   686  C  CB    . VAL A 1 108 ? 4.679   48.041 -5.538  1.00 19.36  ? 94   VAL A CB    1 
ATOM   687  C  CG1   . VAL A 1 108 ? 5.079   48.905 -4.336  1.00 18.24  ? 94   VAL A CG1   1 
ATOM   688  C  CG2   . VAL A 1 108 ? 5.247   46.626 -5.407  1.00 16.17  ? 94   VAL A CG2   1 
ATOM   689  N  N     . PRO A 1 109 ? 1.783   49.998 -5.148  1.00 20.93  ? 95   PRO A N     1 
ATOM   690  C  CA    . PRO A 1 109 ? 1.195   51.306 -5.472  1.00 20.46  ? 95   PRO A CA    1 
ATOM   691  C  C     . PRO A 1 109 ? 2.117   52.472 -5.163  1.00 19.19  ? 95   PRO A C     1 
ATOM   692  O  O     . PRO A 1 109 ? 2.096   53.022 -4.054  1.00 19.47  ? 95   PRO A O     1 
ATOM   693  C  CB    . PRO A 1 109 ? -0.080  51.338 -4.614  1.00 19.80  ? 95   PRO A CB    1 
ATOM   694  C  CG    . PRO A 1 109 ? 0.256   50.515 -3.452  1.00 20.27  ? 95   PRO A CG    1 
ATOM   695  C  CD    . PRO A 1 109 ? 1.186   49.418 -3.935  1.00 19.36  ? 95   PRO A CD    1 
ATOM   696  N  N     . VAL A 1 110 ? 2.958   52.818 -6.139  1.00 21.04  ? 96   VAL A N     1 
ATOM   697  C  CA    . VAL A 1 110 ? 3.830   53.985 -6.083  1.00 16.12  ? 96   VAL A CA    1 
ATOM   698  C  C     . VAL A 1 110 ? 3.244   55.057 -6.989  1.00 18.36  ? 96   VAL A C     1 
ATOM   699  O  O     . VAL A 1 110 ? 2.938   54.791 -8.158  1.00 18.69  ? 96   VAL A O     1 
ATOM   700  C  CB    . VAL A 1 110 ? 5.264   53.635 -6.522  1.00 18.03  ? 96   VAL A CB    1 
ATOM   701  C  CG1   . VAL A 1 110 ? 6.067   54.906 -6.775  1.00 16.00  ? 96   VAL A CG1   1 
ATOM   702  C  CG2   . VAL A 1 110 ? 5.962   52.745 -5.474  1.00 16.78  ? 96   VAL A CG2   1 
ATOM   703  N  N     . LEU A 1 111 ? 3.102   56.269 -6.466  1.00 16.84  ? 97   LEU A N     1 
ATOM   704  C  CA    . LEU A 1 111 ? 2.608   57.397 -7.245  1.00 18.68  ? 97   LEU A CA    1 
ATOM   705  C  C     . LEU A 1 111 ? 3.782   58.178 -7.818  1.00 18.04  ? 97   LEU A C     1 
ATOM   706  O  O     . LEU A 1 111 ? 4.607   58.704 -7.064  1.00 16.71  ? 97   LEU A O     1 
ATOM   707  C  CB    . LEU A 1 111 ? 1.750   58.325 -6.387  1.00 17.79  ? 97   LEU A CB    1 
ATOM   708  C  CG    . LEU A 1 111 ? 1.372   59.637 -7.104  1.00 19.66  ? 97   LEU A CG    1 
ATOM   709  C  CD1   . LEU A 1 111 ? 0.345   59.403 -8.220  1.00 19.72  ? 97   LEU A CD1   1 
ATOM   710  C  CD2   . LEU A 1 111 ? 0.841   60.646 -6.105  1.00 20.63  ? 97   LEU A CD2   1 
ATOM   711  N  N     . HIS A 1 112 ? 3.829   58.288 -9.144  1.00 17.22  ? 98   HIS A N     1 
ATOM   712  C  CA    . HIS A 1 112 ? 4.865   59.052 -9.831  1.00 17.91  ? 98   HIS A CA    1 
ATOM   713  C  C     . HIS A 1 112 ? 4.338   60.454 -10.128 1.00 18.60  ? 98   HIS A C     1 
ATOM   714  O  O     . HIS A 1 112 ? 3.481   60.635 -11.003 1.00 18.53  ? 98   HIS A O     1 
ATOM   715  C  CB    . HIS A 1 112 ? 5.303   58.353 -11.117 1.00 16.32  ? 98   HIS A CB    1 
ATOM   716  C  CG    . HIS A 1 112 ? 6.573   58.905 -11.692 1.00 17.79  ? 98   HIS A CG    1 
ATOM   717  N  ND1   . HIS A 1 112 ? 7.144   58.412 -12.847 1.00 16.36  ? 98   HIS A ND1   1 
ATOM   718  C  CD2   . HIS A 1 112 ? 7.404   59.884 -11.248 1.00 15.54  ? 98   HIS A CD2   1 
ATOM   719  C  CE1   . HIS A 1 112 ? 8.257   59.076 -13.106 1.00 16.29  ? 98   HIS A CE1   1 
ATOM   720  N  NE2   . HIS A 1 112 ? 8.441   59.971 -12.149 1.00 18.72  ? 98   HIS A NE2   1 
ATOM   721  N  N     . ILE A 1 113 ? 4.863   61.445 -9.413  1.00 17.35  ? 99   ILE A N     1 
ATOM   722  C  CA    . ILE A 1 113 ? 4.573   62.851 -9.675  1.00 18.18  ? 99   ILE A CA    1 
ATOM   723  C  C     . ILE A 1 113 ? 5.706   63.417 -10.521 1.00 18.82  ? 99   ILE A C     1 
ATOM   724  O  O     . ILE A 1 113 ? 6.876   63.346 -10.129 1.00 16.57  ? 99   ILE A O     1 
ATOM   725  C  CB    . ILE A 1 113 ? 4.417   63.646 -8.369  1.00 17.90  ? 99   ILE A CB    1 
ATOM   726  C  CG1   . ILE A 1 113 ? 3.327   63.009 -7.479  1.00 19.06  ? 99   ILE A CG1   1 
ATOM   727  C  CG2   . ILE A 1 113 ? 4.087   65.117 -8.677  1.00 17.21  ? 99   ILE A CG2   1 
ATOM   728  C  CD1   . ILE A 1 113 ? 3.401   63.421 -6.000  1.00 19.50  ? 99   ILE A CD1   1 
ATOM   729  N  N     . VAL A 1 114 ? 5.371   64.000 -11.663 1.00 18.85  ? 100  VAL A N     1 
ATOM   730  C  CA    . VAL A 1 114 ? 6.369   64.551 -12.571 1.00 16.72  ? 100  VAL A CA    1 
ATOM   731  C  C     . VAL A 1 114 ? 6.148   66.053 -12.645 1.00 18.84  ? 100  VAL A C     1 
ATOM   732  O  O     . VAL A 1 114 ? 5.131   66.506 -13.178 1.00 17.46  ? 100  VAL A O     1 
ATOM   733  C  CB    . VAL A 1 114 ? 6.300   63.912 -13.964 1.00 17.84  ? 100  VAL A CB    1 
ATOM   734  C  CG1   . VAL A 1 114 ? 7.399   64.478 -14.869 1.00 17.30  ? 100  VAL A CG1   1 
ATOM   735  C  CG2   . VAL A 1 114 ? 6.430   62.395 -13.851 1.00 16.04  ? 100  VAL A CG2   1 
ATOM   736  N  N     . GLY A 1 115 ? 7.090   66.826 -12.106 1.00 18.37  ? 101  GLY A N     1 
ATOM   737  C  CA    . GLY A 1 115 ? 7.053   68.270 -12.289 1.00 18.95  ? 101  GLY A CA    1 
ATOM   738  C  C     . GLY A 1 115 ? 7.407   68.628 -13.725 1.00 21.23  ? 101  GLY A C     1 
ATOM   739  O  O     . GLY A 1 115 ? 8.374   68.099 -14.286 1.00 21.67  ? 101  GLY A O     1 
ATOM   740  N  N     . ALA A 1 116 ? 6.619   69.516 -14.330 1.00 21.32  ? 102  ALA A N     1 
ATOM   741  C  CA    . ALA A 1 116 ? 6.662   69.782 -15.760 1.00 21.78  ? 102  ALA A CA    1 
ATOM   742  C  C     . ALA A 1 116 ? 6.687   71.278 -16.030 1.00 23.58  ? 102  ALA A C     1 
ATOM   743  O  O     . ALA A 1 116 ? 6.323   72.079 -15.163 1.00 22.71  ? 102  ALA A O     1 
ATOM   744  C  CB    . ALA A 1 116 ? 5.453   69.150 -16.470 1.00 21.08  ? 102  ALA A CB    1 
ATOM   745  N  N     . PRO A 1 117 ? 7.120   71.687 -17.225 1.00 24.14  ? 103  PRO A N     1 
ATOM   746  C  CA    . PRO A 1 117 ? 7.026   73.104 -17.606 1.00 25.34  ? 103  PRO A CA    1 
ATOM   747  C  C     . PRO A 1 117 ? 5.595   73.617 -17.545 1.00 24.63  ? 103  PRO A C     1 
ATOM   748  O  O     . PRO A 1 117 ? 4.633   72.869 -17.734 1.00 23.85  ? 103  PRO A O     1 
ATOM   749  C  CB    . PRO A 1 117 ? 7.543   73.118 -19.050 1.00 26.70  ? 103  PRO A CB    1 
ATOM   750  C  CG    . PRO A 1 117 ? 8.348   71.893 -19.188 1.00 25.42  ? 103  PRO A CG    1 
ATOM   751  C  CD    . PRO A 1 117 ? 7.769   70.874 -18.270 1.00 23.48  ? 103  PRO A CD    1 
ATOM   752  N  N     . GLY A 1 118 ? 5.464   74.923 -17.329 1.00 25.72  ? 104  GLY A N     1 
ATOM   753  C  CA    . GLY A 1 118 ? 4.146   75.514 -17.223 1.00 28.13  ? 104  GLY A CA    1 
ATOM   754  C  C     . GLY A 1 118 ? 3.364   75.360 -18.513 1.00 27.73  ? 104  GLY A C     1 
ATOM   755  O  O     . GLY A 1 118 ? 3.927   75.171 -19.589 1.00 26.93  ? 104  GLY A O     1 
ATOM   756  N  N     . THR A 1 119 ? 2.036   75.414 -18.389 1.00 26.37  ? 105  THR A N     1 
ATOM   757  C  CA    . THR A 1 119 ? 1.180   75.044 -19.514 1.00 28.09  ? 105  THR A CA    1 
ATOM   758  C  C     . THR A 1 119 ? 1.402   75.957 -20.716 1.00 30.37  ? 105  THR A C     1 
ATOM   759  O  O     . THR A 1 119 ? 1.440   75.484 -21.857 1.00 31.35  ? 105  THR A O     1 
ATOM   760  C  CB    . THR A 1 119 ? -0.295  75.065 -19.102 1.00 28.07  ? 105  THR A CB    1 
ATOM   761  O  OG1   . THR A 1 119 ? -0.647  76.370 -18.632 1.00 27.42  ? 105  THR A OG1   1 
ATOM   762  C  CG2   . THR A 1 119 ? -0.555  74.045 -17.990 1.00 25.38  ? 105  THR A CG2   1 
ATOM   763  N  N     . ALA A 1 120 ? 1.554   77.265 -20.485 1.00 30.28  ? 106  ALA A N     1 
ATOM   764  C  CA    . ALA A 1 120 ? 1.763   78.182 -21.603 1.00 28.99  ? 106  ALA A CA    1 
ATOM   765  C  C     . ALA A 1 120 ? 3.019   77.816 -22.379 1.00 31.02  ? 106  ALA A C     1 
ATOM   766  O  O     . ALA A 1 120 ? 3.005   77.801 -23.616 1.00 31.34  ? 106  ALA A O     1 
ATOM   767  C  CB    . ALA A 1 120 ? 1.842   79.626 -21.109 1.00 28.10  ? 106  ALA A CB    1 
ATOM   768  N  N     . SER A 1 121 ? 4.112   77.508 -21.665 1.00 30.15  ? 107  SER A N     1 
ATOM   769  C  CA    . SER A 1 121 ? 5.342   77.060 -22.316 1.00 29.68  ? 107  SER A CA    1 
ATOM   770  C  C     . SER A 1 121 ? 5.094   75.833 -23.172 1.00 29.83  ? 107  SER A C     1 
ATOM   771  O  O     . SER A 1 121 ? 5.624   75.723 -24.284 1.00 29.33  ? 107  SER A O     1 
ATOM   772  C  CB    . SER A 1 121 ? 6.411   76.737 -21.271 1.00 31.27  ? 107  SER A CB    1 
ATOM   773  O  OG    . SER A 1 121 ? 7.235   77.850 -21.029 1.00 39.80  ? 107  SER A OG    1 
ATOM   774  N  N     . GLN A 1 122 ? 4.319   74.882 -22.646 1.00 30.10  ? 108  GLN A N     1 
ATOM   775  C  CA    . GLN A 1 122 ? 4.009   73.675 -23.399 1.00 27.24  ? 108  GLN A CA    1 
ATOM   776  C  C     . GLN A 1 122 ? 3.187   74.002 -24.636 1.00 28.74  ? 108  GLN A C     1 
ATOM   777  O  O     . GLN A 1 122 ? 3.475   73.502 -25.734 1.00 27.78  ? 108  GLN A O     1 
ATOM   778  C  CB    . GLN A 1 122 ? 3.274   72.682 -22.503 1.00 27.67  ? 108  GLN A CB    1 
ATOM   779  C  CG    . GLN A 1 122 ? 4.117   72.098 -21.410 1.00 24.86  ? 108  GLN A CG    1 
ATOM   780  C  CD    . GLN A 1 122 ? 3.370   71.045 -20.632 1.00 26.75  ? 108  GLN A CD    1 
ATOM   781  O  OE1   . GLN A 1 122 ? 2.566   70.304 -21.199 1.00 26.44  ? 108  GLN A OE1   1 
ATOM   782  N  NE2   . GLN A 1 122 ? 3.680   70.919 -19.343 1.00 23.57  ? 108  GLN A NE2   1 
ATOM   783  N  N     . GLN A 1 123 ? 2.173   74.860 -24.481 1.00 30.08  ? 109  GLN A N     1 
ATOM   784  C  CA    . GLN A 1 123 ? 1.302   75.208 -25.599 1.00 31.24  ? 109  GLN A CA    1 
ATOM   785  C  C     . GLN A 1 123 ? 2.066   75.913 -26.709 1.00 28.63  ? 109  GLN A C     1 
ATOM   786  O  O     . GLN A 1 123 ? 1.756   75.722 -27.889 1.00 28.85  ? 109  GLN A O     1 
ATOM   787  C  CB    . GLN A 1 123 ? 0.139   76.084 -25.110 1.00 33.22  ? 109  GLN A CB    1 
ATOM   788  C  CG    . GLN A 1 123 ? -1.121  75.301 -24.762 1.00 40.20  ? 109  GLN A CG    1 
ATOM   789  C  CD    . GLN A 1 123 ? -1.957  75.932 -23.648 1.00 47.72  ? 109  GLN A CD    1 
ATOM   790  O  OE1   . GLN A 1 123 ? -2.225  77.136 -23.656 1.00 44.25  ? 109  GLN A OE1   1 
ATOM   791  N  NE2   . GLN A 1 123 ? -2.418  75.101 -22.711 1.00 41.87  ? 109  GLN A NE2   1 
ATOM   792  N  N     . ARG A 1 124 ? 3.069   76.718 -26.356 1.00 28.86  ? 110  ARG A N     1 
ATOM   793  C  CA    . ARG A 1 124 ? 3.901   77.385 -27.351 1.00 28.86  ? 110  ARG A CA    1 
ATOM   794  C  C     . ARG A 1 124 ? 4.905   76.454 -28.031 1.00 29.67  ? 110  ARG A C     1 
ATOM   795  O  O     . ARG A 1 124 ? 5.564   76.886 -28.984 1.00 28.67  ? 110  ARG A O     1 
ATOM   796  C  CB    . ARG A 1 124 ? 4.657   78.542 -26.701 1.00 31.66  ? 110  ARG A CB    1 
ATOM   797  C  CG    . ARG A 1 124 ? 3.789   79.644 -26.129 1.00 32.16  ? 110  ARG A CG    1 
ATOM   798  C  CD    . ARG A 1 124 ? 4.657   80.825 -25.724 1.00 37.28  ? 110  ARG A CD    1 
ATOM   799  N  NE    . ARG A 1 124 ? 4.337   81.326 -24.391 1.00 42.21  ? 110  ARG A NE    1 
ATOM   800  C  CZ    . ARG A 1 124 ? 5.098   81.151 -23.316 1.00 39.24  ? 110  ARG A CZ    1 
ATOM   801  N  NH1   . ARG A 1 124 ? 6.224   80.461 -23.368 1.00 38.72  ? 110  ARG A NH1   1 
ATOM   802  N  NH2   . ARG A 1 124 ? 4.717   81.679 -22.156 1.00 40.17  ? 110  ARG A NH2   1 
ATOM   803  N  N     . GLY A 1 125 ? 5.060   75.219 -27.563 1.00 27.81  ? 111  GLY A N     1 
ATOM   804  C  CA    . GLY A 1 125 ? 6.019   74.305 -28.167 1.00 26.54  ? 111  GLY A CA    1 
ATOM   805  C  C     . GLY A 1 125 ? 7.450   74.796 -28.098 1.00 26.07  ? 111  GLY A C     1 
ATOM   806  O  O     . GLY A 1 125 ? 8.214   74.610 -29.053 1.00 23.53  ? 111  GLY A O     1 
ATOM   807  N  N     . GLU A 1 126 ? 7.841   75.401 -26.978 1.00 27.63  ? 112  GLU A N     1 
ATOM   808  C  CA    . GLU A 1 126 ? 9.173   75.984 -26.885 1.00 27.45  ? 112  GLU A CA    1 
ATOM   809  C  C     . GLU A 1 126 ? 10.235  74.894 -26.870 1.00 26.13  ? 112  GLU A C     1 
ATOM   810  O  O     . GLU A 1 126 ? 9.979   73.759 -26.452 1.00 22.46  ? 112  GLU A O     1 
ATOM   811  C  CB    . GLU A 1 126 ? 9.302   76.841 -25.631 1.00 30.40  ? 112  GLU A CB    1 
ATOM   812  C  CG    . GLU A 1 126 ? 8.186   77.841 -25.445 1.00 31.41  ? 112  GLU A CG    1 
ATOM   813  C  CD    . GLU A 1 126 ? 8.470   78.794 -24.310 1.00 34.95  ? 112  GLU A CD    1 
ATOM   814  O  OE1   . GLU A 1 126 ? 8.848   78.329 -23.213 1.00 35.16  ? 112  GLU A OE1   1 
ATOM   815  O  OE2   . GLU A 1 126 ? 8.306   80.013 -24.508 1.00 38.13  ? 112  GLU A OE2   1 
ATOM   816  N  N     . LEU A 1 127 ? 11.442  75.257 -27.326 1.00 25.49  ? 113  LEU A N     1 
ATOM   817  C  CA    . LEU A 1 127 ? 12.598  74.354 -27.336 1.00 25.73  ? 113  LEU A CA    1 
ATOM   818  C  C     . LEU A 1 127 ? 13.255  74.383 -25.961 1.00 25.17  ? 113  LEU A C     1 
ATOM   819  O  O     . LEU A 1 127 ? 14.329  74.963 -25.751 1.00 24.73  ? 113  LEU A O     1 
ATOM   820  C  CB    . LEU A 1 127 ? 13.595  74.740 -28.421 1.00 24.61  ? 113  LEU A CB    1 
ATOM   821  C  CG    . LEU A 1 127 ? 13.093  74.715 -29.858 1.00 29.18  ? 113  LEU A CG    1 
ATOM   822  C  CD1   . LEU A 1 127 ? 14.276  74.849 -30.783 1.00 26.87  ? 113  LEU A CD1   1 
ATOM   823  C  CD2   . LEU A 1 127 ? 12.304  73.428 -30.138 1.00 25.65  ? 113  LEU A CD2   1 
ATOM   824  N  N     . LEU A 1 128 ? 12.614  73.690 -25.027 1.00 23.23  ? 114  LEU A N     1 
ATOM   825  C  CA    . LEU A 1 128 ? 12.991  73.705 -23.621 1.00 23.16  ? 114  LEU A CA    1 
ATOM   826  C  C     . LEU A 1 128 ? 13.923  72.542 -23.277 1.00 22.53  ? 114  LEU A C     1 
ATOM   827  O  O     . LEU A 1 128 ? 13.912  71.494 -23.927 1.00 21.44  ? 114  LEU A O     1 
ATOM   828  C  CB    . LEU A 1 128 ? 11.733  73.637 -22.757 1.00 23.68  ? 114  LEU A CB    1 
ATOM   829  C  CG    . LEU A 1 128 ? 10.790  74.843 -22.719 1.00 27.45  ? 114  LEU A CG    1 
ATOM   830  C  CD1   . LEU A 1 128 ? 9.787   74.679 -21.588 1.00 28.06  ? 114  LEU A CD1   1 
ATOM   831  C  CD2   . LEU A 1 128 ? 11.535  76.177 -22.601 1.00 27.61  ? 114  LEU A CD2   1 
ATOM   832  N  N     . HIS A 1 129 ? 14.738  72.739 -22.238 1.00 22.13  ? 115  HIS A N     1 
ATOM   833  C  CA    . HIS A 1 129 ? 15.558  71.657 -21.712 1.00 21.55  ? 115  HIS A CA    1 
ATOM   834  C  C     . HIS A 1 129 ? 14.681  70.519 -21.198 1.00 21.07  ? 115  HIS A C     1 
ATOM   835  O  O     . HIS A 1 129 ? 13.560  70.735 -20.731 1.00 19.05  ? 115  HIS A O     1 
ATOM   836  C  CB    . HIS A 1 129 ? 16.466  72.178 -20.599 1.00 22.54  ? 115  HIS A CB    1 
ATOM   837  C  CG    . HIS A 1 129 ? 15.730  72.639 -19.379 1.00 23.52  ? 115  HIS A CG    1 
ATOM   838  N  ND1   . HIS A 1 129 ? 15.192  73.904 -19.270 1.00 24.74  ? 115  HIS A ND1   1 
ATOM   839  C  CD2   . HIS A 1 129 ? 15.488  72.023 -18.197 1.00 24.97  ? 115  HIS A CD2   1 
ATOM   840  C  CE1   . HIS A 1 129 ? 14.625  74.036 -18.083 1.00 29.11  ? 115  HIS A CE1   1 
ATOM   841  N  NE2   . HIS A 1 129 ? 14.794  72.910 -17.411 1.00 24.55  ? 115  HIS A NE2   1 
ATOM   842  N  N     . HIS A 1 130 ? 15.219  69.297 -21.272 1.00 19.29  ? 116  HIS A N     1 
ATOM   843  C  CA    . HIS A 1 130 ? 14.519  68.047 -20.959 1.00 19.91  ? 116  HIS A CA    1 
ATOM   844  C  C     . HIS A 1 130 ? 13.396  67.736 -21.944 1.00 20.07  ? 116  HIS A C     1 
ATOM   845  O  O     . HIS A 1 130 ? 12.449  67.001 -21.609 1.00 16.97  ? 116  HIS A O     1 
ATOM   846  C  CB    . HIS A 1 130 ? 13.953  68.030 -19.523 1.00 18.34  ? 116  HIS A CB    1 
ATOM   847  C  CG    . HIS A 1 130 ? 14.941  68.410 -18.459 1.00 19.87  ? 116  HIS A CG    1 
ATOM   848  N  ND1   . HIS A 1 130 ? 16.308  68.383 -18.652 1.00 20.32  ? 116  HIS A ND1   1 
ATOM   849  C  CD2   . HIS A 1 130 ? 14.751  68.803 -17.178 1.00 20.63  ? 116  HIS A CD2   1 
ATOM   850  C  CE1   . HIS A 1 130 ? 16.913  68.764 -17.542 1.00 19.63  ? 116  HIS A CE1   1 
ATOM   851  N  NE2   . HIS A 1 130 ? 15.992  69.013 -16.630 1.00 21.61  ? 116  HIS A NE2   1 
ATOM   852  N  N     . THR A 1 131 ? 13.455  68.274 -23.155 1.00 18.74  ? 117  THR A N     1 
ATOM   853  C  CA    . THR A 1 131 ? 12.564  67.818 -24.205 1.00 19.38  ? 117  THR A CA    1 
ATOM   854  C  C     . THR A 1 131 ? 13.393  67.179 -25.302 1.00 18.53  ? 117  THR A C     1 
ATOM   855  O  O     . THR A 1 131 ? 14.622  67.276 -25.321 1.00 20.05  ? 117  THR A O     1 
ATOM   856  C  CB    . THR A 1 131 ? 11.702  68.955 -24.781 1.00 20.14  ? 117  THR A CB    1 
ATOM   857  O  OG1   . THR A 1 131 ? 12.477  69.794 -25.656 1.00 18.13  ? 117  THR A OG1   1 
ATOM   858  C  CG2   . THR A 1 131 ? 11.075  69.783 -23.671 1.00 20.06  ? 117  THR A CG2   1 
ATOM   859  N  N     . LEU A 1 132 ? 12.703  66.539 -26.238 1.00 19.51  ? 118  LEU A N     1 
ATOM   860  C  CA    . LEU A 1 132 ? 13.373  65.988 -27.410 1.00 19.60  ? 118  LEU A CA    1 
ATOM   861  C  C     . LEU A 1 132 ? 13.694  67.052 -28.452 1.00 20.69  ? 118  LEU A C     1 
ATOM   862  O  O     . LEU A 1 132 ? 14.210  66.718 -29.530 1.00 19.67  ? 118  LEU A O     1 
ATOM   863  C  CB    . LEU A 1 132 ? 12.520  64.879 -28.022 1.00 19.69  ? 118  LEU A CB    1 
ATOM   864  C  CG    . LEU A 1 132 ? 12.181  63.711 -27.093 1.00 19.41  ? 118  LEU A CG    1 
ATOM   865  C  CD1   . LEU A 1 132 ? 11.431  62.614 -27.861 1.00 20.32  ? 118  LEU A CD1   1 
ATOM   866  C  CD2   . LEU A 1 132 ? 13.420  63.170 -26.381 1.00 17.54  ? 118  LEU A CD2   1 
ATOM   867  N  N     . GLY A 1 133 ? 13.431  68.324 -28.155 1.00 20.42  ? 119  GLY A N     1 
ATOM   868  C  CA    . GLY A 1 133 ? 13.716  69.389 -29.102 1.00 21.21  ? 119  GLY A CA    1 
ATOM   869  C  C     . GLY A 1 133 ? 12.715  69.512 -30.225 1.00 22.49  ? 119  GLY A C     1 
ATOM   870  O  O     . GLY A 1 133 ? 13.010  70.142 -31.248 1.00 22.55  ? 119  GLY A O     1 
ATOM   871  N  N     . ASP A 1 134 ? 11.525  68.944 -30.054 1.00 22.35  ? 120  ASP A N     1 
ATOM   872  C  CA    . ASP A 1 134 ? 10.484  68.963 -31.073 1.00 22.88  ? 120  ASP A CA    1 
ATOM   873  C  C     . ASP A 1 134 ? 9.257   69.757 -30.641 1.00 23.14  ? 120  ASP A C     1 
ATOM   874  O  O     . ASP A 1 134 ? 8.256   69.775 -31.364 1.00 22.00  ? 120  ASP A O     1 
ATOM   875  C  CB    . ASP A 1 134 ? 10.100  67.524 -31.431 1.00 22.46  ? 120  ASP A CB    1 
ATOM   876  C  CG    . ASP A 1 134 ? 9.699   66.706 -30.213 1.00 23.25  ? 120  ASP A CG    1 
ATOM   877  O  OD1   . ASP A 1 134 ? 9.652   67.261 -29.101 1.00 23.39  ? 120  ASP A OD1   1 
ATOM   878  O  OD2   . ASP A 1 134 ? 9.455   65.489 -30.353 1.00 24.20  ? 120  ASP A OD2   1 
ATOM   879  N  N     . GLY A 1 135 ? 9.308   70.428 -29.493 1.00 22.24  ? 121  GLY A N     1 
ATOM   880  C  CA    . GLY A 1 135 ? 8.131   71.137 -29.025 1.00 22.46  ? 121  GLY A CA    1 
ATOM   881  C  C     . GLY A 1 135 ? 7.021   70.253 -28.503 1.00 23.12  ? 121  GLY A C     1 
ATOM   882  O  O     . GLY A 1 135 ? 5.909   70.744 -28.288 1.00 23.08  ? 121  GLY A O     1 
ATOM   883  N  N     . GLU A 1 136 ? 7.285   68.967 -28.272 1.00 23.16  ? 122  GLU A N     1 
ATOM   884  C  CA    . GLU A 1 136 ? 6.256   68.018 -27.863 1.00 23.16  ? 122  GLU A CA    1 
ATOM   885  C  C     . GLU A 1 136 ? 6.418   67.733 -26.375 1.00 22.40  ? 122  GLU A C     1 
ATOM   886  O  O     . GLU A 1 136 ? 7.521   67.418 -25.921 1.00 20.38  ? 122  GLU A O     1 
ATOM   887  C  CB    . GLU A 1 136 ? 6.377   66.712 -28.643 1.00 24.23  ? 122  GLU A CB    1 
ATOM   888  C  CG    . GLU A 1 136 ? 5.759   66.744 -30.027 1.00 29.98  ? 122  GLU A CG    1 
ATOM   889  C  CD    . GLU A 1 136 ? 4.261   66.960 -29.986 1.00 39.19  ? 122  GLU A CD    1 
ATOM   890  O  OE1   . GLU A 1 136 ? 3.584   66.377 -29.105 1.00 37.32  ? 122  GLU A OE1   1 
ATOM   891  O  OE2   . GLU A 1 136 ? 3.766   67.715 -30.848 1.00 38.42  ? 122  GLU A OE2   1 
ATOM   892  N  N     . PHE A 1 137 ? 5.325   67.824 -25.614 1.00 21.53  ? 123  PHE A N     1 
ATOM   893  C  CA    . PHE A 1 137 ? 5.418   67.680 -24.163 1.00 20.77  ? 123  PHE A CA    1 
ATOM   894  C  C     . PHE A 1 137 ? 4.631   66.500 -23.607 1.00 23.61  ? 123  PHE A C     1 
ATOM   895  O  O     . PHE A 1 137 ? 4.559   66.344 -22.381 1.00 22.86  ? 123  PHE A O     1 
ATOM   896  C  CB    . PHE A 1 137 ? 4.980   68.974 -23.477 1.00 21.18  ? 123  PHE A CB    1 
ATOM   897  C  CG    . PHE A 1 137 ? 5.930   70.106 -23.694 1.00 21.87  ? 123  PHE A CG    1 
ATOM   898  C  CD1   . PHE A 1 137 ? 5.801   70.939 -24.802 1.00 22.47  ? 123  PHE A CD1   1 
ATOM   899  C  CD2   . PHE A 1 137 ? 6.990   70.310 -22.818 1.00 21.78  ? 123  PHE A CD2   1 
ATOM   900  C  CE1   . PHE A 1 137 ? 6.712   71.987 -25.024 1.00 24.48  ? 123  PHE A CE1   1 
ATOM   901  C  CE2   . PHE A 1 137 ? 7.899   71.345 -23.022 1.00 20.91  ? 123  PHE A CE2   1 
ATOM   902  C  CZ    . PHE A 1 137 ? 7.763   72.191 -24.135 1.00 23.94  ? 123  PHE A CZ    1 
ATOM   903  N  N     . ARG A 1 138 ? 4.071   65.643 -24.457 1.00 20.19  ? 124  ARG A N     1 
ATOM   904  C  CA    . ARG A 1 138 ? 3.294   64.510 -23.979 1.00 22.93  ? 124  ARG A CA    1 
ATOM   905  C  C     . ARG A 1 138 ? 3.914   63.161 -24.318 1.00 23.81  ? 124  ARG A C     1 
ATOM   906  O  O     . ARG A 1 138 ? 3.304   62.128 -24.010 1.00 23.12  ? 124  ARG A O     1 
ATOM   907  C  CB    . ARG A 1 138 ? 1.870   64.585 -24.546 1.00 26.31  ? 124  ARG A CB    1 
ATOM   908  C  CG    . ARG A 1 138 ? 1.254   65.967 -24.391 1.00 28.67  ? 124  ARG A CG    1 
ATOM   909  C  CD    . ARG A 1 138 ? -0.199  65.918 -23.950 1.00 35.80  ? 124  ARG A CD    1 
ATOM   910  N  NE    . ARG A 1 138 ? -0.570  67.131 -23.233 1.00 41.16  ? 124  ARG A NE    1 
ATOM   911  C  CZ    . ARG A 1 138 ? -1.739  67.744 -23.347 1.00 54.33  ? 124  ARG A CZ    1 
ATOM   912  N  NH1   . ARG A 1 138 ? -2.690  67.274 -24.136 1.00 50.04  ? 124  ARG A NH1   1 
ATOM   913  N  NH2   . ARG A 1 138 ? -1.961  68.852 -22.643 1.00 46.98  ? 124  ARG A NH2   1 
ATOM   914  N  N     . HIS A 1 139 ? 5.098   63.137 -24.947 1.00 21.89  ? 125  HIS A N     1 
ATOM   915  C  CA    . HIS A 1 139 ? 5.758   61.872 -25.263 1.00 22.95  ? 125  HIS A CA    1 
ATOM   916  C  C     . HIS A 1 139 ? 5.895   61.001 -24.024 1.00 20.99  ? 125  HIS A C     1 
ATOM   917  O  O     . HIS A 1 139 ? 5.522   59.821 -24.024 1.00 21.34  ? 125  HIS A O     1 
ATOM   918  C  CB    . HIS A 1 139 ? 7.172   62.122 -25.813 1.00 20.77  ? 125  HIS A CB    1 
ATOM   919  C  CG    . HIS A 1 139 ? 7.230   62.702 -27.190 1.00 21.51  ? 125  HIS A CG    1 
ATOM   920  N  ND1   . HIS A 1 139 ? 6.466   62.230 -28.236 1.00 23.36  ? 125  HIS A ND1   1 
ATOM   921  C  CD2   . HIS A 1 139 ? 8.002   63.690 -27.702 1.00 21.54  ? 125  HIS A CD2   1 
ATOM   922  C  CE1   . HIS A 1 139 ? 6.760   62.910 -29.332 1.00 25.74  ? 125  HIS A CE1   1 
ATOM   923  N  NE2   . HIS A 1 139 ? 7.693   63.798 -29.037 1.00 23.43  ? 125  HIS A NE2   1 
ATOM   924  N  N     . PHE A 1 140 ? 6.457   61.570 -22.957 1.00 20.39  ? 126  PHE A N     1 
ATOM   925  C  CA    . PHE A 1 140 ? 6.844   60.762 -21.810 1.00 19.03  ? 126  PHE A CA    1 
ATOM   926  C  C     . PHE A 1 140 ? 5.633   60.338 -21.008 1.00 20.52  ? 126  PHE A C     1 
ATOM   927  O  O     . PHE A 1 140 ? 5.601   59.219 -20.471 1.00 19.18  ? 126  PHE A O     1 
ATOM   928  C  CB    . PHE A 1 140 ? 7.841   61.536 -20.950 1.00 18.45  ? 126  PHE A CB    1 
ATOM   929  C  CG    . PHE A 1 140 ? 8.868   62.288 -21.762 1.00 18.61  ? 126  PHE A CG    1 
ATOM   930  C  CD1   . PHE A 1 140 ? 9.562   61.646 -22.792 1.00 18.74  ? 126  PHE A CD1   1 
ATOM   931  C  CD2   . PHE A 1 140 ? 9.126   63.629 -21.514 1.00 17.74  ? 126  PHE A CD2   1 
ATOM   932  C  CE1   . PHE A 1 140 ? 10.494  62.327 -23.557 1.00 17.27  ? 126  PHE A CE1   1 
ATOM   933  C  CE2   . PHE A 1 140 ? 10.061  64.318 -22.263 1.00 18.12  ? 126  PHE A CE2   1 
ATOM   934  C  CZ    . PHE A 1 140 ? 10.743  63.670 -23.296 1.00 18.81  ? 126  PHE A CZ    1 
ATOM   935  N  N     . TYR A 1 141 ? 4.623   61.204 -20.948 1.00 19.68  ? 127  TYR A N     1 
ATOM   936  C  CA    . TYR A 1 141 ? 3.330   60.814 -20.400 1.00 22.71  ? 127  TYR A CA    1 
ATOM   937  C  C     . TYR A 1 141 ? 2.813   59.558 -21.096 1.00 20.81  ? 127  TYR A C     1 
ATOM   938  O  O     . TYR A 1 141 ? 2.396   58.598 -20.441 1.00 19.03  ? 127  TYR A O     1 
ATOM   939  C  CB    . TYR A 1 141 ? 2.343   61.974 -20.565 1.00 21.76  ? 127  TYR A CB    1 
ATOM   940  C  CG    . TYR A 1 141 ? 0.910   61.687 -20.140 1.00 23.95  ? 127  TYR A CG    1 
ATOM   941  C  CD1   . TYR A 1 141 ? 0.550   61.699 -18.795 1.00 22.89  ? 127  TYR A CD1   1 
ATOM   942  C  CD2   . TYR A 1 141 ? -0.076  61.428 -21.086 1.00 24.04  ? 127  TYR A CD2   1 
ATOM   943  C  CE1   . TYR A 1 141 ? -0.757  61.452 -18.401 1.00 23.32  ? 127  TYR A CE1   1 
ATOM   944  C  CE2   . TYR A 1 141 ? -1.384  61.178 -20.715 1.00 25.05  ? 127  TYR A CE2   1 
ATOM   945  C  CZ    . TYR A 1 141 ? -1.719  61.190 -19.368 1.00 26.51  ? 127  TYR A CZ    1 
ATOM   946  O  OH    . TYR A 1 141 ? -3.018  60.944 -18.984 1.00 26.28  ? 127  TYR A OH    1 
ATOM   947  N  N     . HIS A 1 142 ? 2.888   59.529 -22.428 1.00 22.96  ? 128  HIS A N     1 
ATOM   948  C  CA    . HIS A 1 142 ? 2.400   58.370 -23.169 1.00 22.63  ? 128  HIS A CA    1 
ATOM   949  C  C     . HIS A 1 142 ? 3.258   57.141 -22.908 1.00 21.03  ? 128  HIS A C     1 
ATOM   950  O  O     . HIS A 1 142 ? 2.736   56.022 -22.791 1.00 19.11  ? 128  HIS A O     1 
ATOM   951  C  CB    . HIS A 1 142 ? 2.319   58.693 -24.664 1.00 24.26  ? 128  HIS A CB    1 
ATOM   952  C  CG    . HIS A 1 142 ? 1.269   59.708 -24.991 1.00 28.53  ? 128  HIS A CG    1 
ATOM   953  N  ND1   . HIS A 1 142 ? 1.456   60.715 -25.917 1.00 34.11  ? 128  HIS A ND1   1 
ATOM   954  C  CD2   . HIS A 1 142 ? 0.017   59.880 -24.497 1.00 28.96  ? 128  HIS A CD2   1 
ATOM   955  C  CE1   . HIS A 1 142 ? 0.369   61.465 -25.973 1.00 32.18  ? 128  HIS A CE1   1 
ATOM   956  N  NE2   . HIS A 1 142 ? -0.519  60.980 -25.121 1.00 28.11  ? 128  HIS A NE2   1 
ATOM   957  N  N     . MET A 1 143 ? 4.572   57.324 -22.786 1.00 19.43  ? 129  MET A N     1 
ATOM   958  C  CA    . MET A 1 143 ? 5.430   56.174 -22.530 1.00 19.94  ? 129  MET A CA    1 
ATOM   959  C  C     . MET A 1 143 ? 5.181   55.568 -21.164 1.00 20.53  ? 129  MET A C     1 
ATOM   960  O  O     . MET A 1 143 ? 5.435   54.375 -20.975 1.00 17.92  ? 129  MET A O     1 
ATOM   961  C  CB    . MET A 1 143 ? 6.890   56.573 -22.699 1.00 20.87  ? 129  MET A CB    1 
ATOM   962  C  CG    . MET A 1 143 ? 7.125   57.173 -24.068 1.00 19.24  ? 129  MET A CG    1 
ATOM   963  S  SD    . MET A 1 143 ? 8.604   58.170 -24.247 1.00 24.29  ? 129  MET A SD    1 
ATOM   964  C  CE    . MET A 1 143 ? 9.950   57.161 -23.639 1.00 18.86  ? 129  MET A CE    1 
ATOM   965  N  N     . SER A 1 144 ? 4.618   56.330 -20.239 1.00 19.06  ? 130  SER A N     1 
ATOM   966  C  CA    . SER A 1 144 ? 4.329   55.766 -18.933 1.00 22.26  ? 130  SER A CA    1 
ATOM   967  C  C     . SER A 1 144 ? 2.995   55.025 -18.886 1.00 21.61  ? 130  SER A C     1 
ATOM   968  O  O     . SER A 1 144 ? 2.731   54.335 -17.893 1.00 21.51  ? 130  SER A O     1 
ATOM   969  C  CB    . SER A 1 144 ? 4.367   56.870 -17.879 1.00 19.89  ? 130  SER A CB    1 
ATOM   970  O  OG    . SER A 1 144 ? 4.485   56.294 -16.589 1.00 24.89  ? 130  SER A OG    1 
ATOM   971  N  N     . GLU A 1 145 ? 2.180   55.113 -19.940 1.00 21.96  ? 131  GLU A N     1 
ATOM   972  C  CA    . GLU A 1 145 ? 0.839   54.522 -19.913 1.00 23.58  ? 131  GLU A CA    1 
ATOM   973  C  C     . GLU A 1 145 ? 0.854   53.011 -19.680 1.00 23.70  ? 131  GLU A C     1 
ATOM   974  O  O     . GLU A 1 145 ? 0.026   52.534 -18.884 1.00 23.37  ? 131  GLU A O     1 
ATOM   975  C  CB    . GLU A 1 145 ? 0.106   54.922 -21.213 1.00 25.58  ? 131  GLU A CB    1 
ATOM   976  C  CG    . GLU A 1 145 ? -1.347  54.433 -21.521 1.00 33.54  ? 131  GLU A CG    1 
ATOM   977  C  CD    . GLU A 1 145 ? -1.595  52.925 -21.436 1.00 47.50  ? 131  GLU A CD    1 
ATOM   978  O  OE1   . GLU A 1 145 ? -0.877  52.151 -22.117 1.00 34.51  ? 131  GLU A OE1   1 
ATOM   979  O  OE2   . GLU A 1 145 ? -2.556  52.524 -20.733 1.00 43.45  ? 131  GLU A OE2   1 
ATOM   980  N  N     . PRO A 1 146 ? 1.726   52.213 -20.309 1.00 22.59  ? 132  PRO A N     1 
ATOM   981  C  CA    . PRO A 1 146 ? 1.706   50.766 -20.045 1.00 22.60  ? 132  PRO A CA    1 
ATOM   982  C  C     . PRO A 1 146 ? 2.074   50.370 -18.617 1.00 21.78  ? 132  PRO A C     1 
ATOM   983  O  O     . PRO A 1 146 ? 1.720   49.263 -18.205 1.00 20.65  ? 132  PRO A O     1 
ATOM   984  C  CB    . PRO A 1 146 ? 2.734   50.212 -21.044 1.00 23.19  ? 132  PRO A CB    1 
ATOM   985  C  CG    . PRO A 1 146 ? 2.803   51.231 -22.121 1.00 24.40  ? 132  PRO A CG    1 
ATOM   986  C  CD    . PRO A 1 146 ? 2.638   52.540 -21.425 1.00 23.11  ? 132  PRO A CD    1 
ATOM   987  N  N     . ILE A 1 147 ? 2.750   51.216 -17.841 1.00 19.21  ? 133  ILE A N     1 
ATOM   988  C  CA    . ILE A 1 147 ? 3.247   50.790 -16.533 1.00 19.56  ? 133  ILE A CA    1 
ATOM   989  C  C     . ILE A 1 147 ? 2.495   51.478 -15.390 1.00 19.99  ? 133  ILE A C     1 
ATOM   990  O  O     . ILE A 1 147 ? 2.991   51.529 -14.259 1.00 16.61  ? 133  ILE A O     1 
ATOM   991  C  CB    . ILE A 1 147 ? 4.768   50.989 -16.425 1.00 18.23  ? 133  ILE A CB    1 
ATOM   992  C  CG1   . ILE A 1 147 ? 5.153   52.439 -16.729 1.00 18.50  ? 133  ILE A CG1   1 
ATOM   993  C  CG2   . ILE A 1 147 ? 5.486   50.044 -17.396 1.00 18.04  ? 133  ILE A CG2   1 
ATOM   994  C  CD1   . ILE A 1 147 ? 6.621   52.723 -16.570 1.00 16.11  ? 133  ILE A CD1   1 
ATOM   995  N  N     . THR A 1 148 ? 1.296   52.001 -15.660 1.00 18.31  ? 134  THR A N     1 
ATOM   996  C  CA    . THR A 1 148 ? 0.466   52.584 -14.616 1.00 19.66  ? 134  THR A CA    1 
ATOM   997  C  C     . THR A 1 148 ? -0.977  52.140 -14.824 1.00 21.61  ? 134  THR A C     1 
ATOM   998  O  O     . THR A 1 148 ? -1.375  51.756 -15.924 1.00 18.38  ? 134  THR A O     1 
ATOM   999  C  CB    . THR A 1 148 ? 0.551   54.116 -14.601 1.00 19.70  ? 134  THR A CB    1 
ATOM   1000 O  OG1   . THR A 1 148 ? 0.193   54.613 -15.889 1.00 21.06  ? 134  THR A OG1   1 
ATOM   1001 C  CG2   . THR A 1 148 ? 1.976   54.580 -14.253 1.00 18.97  ? 134  THR A CG2   1 
ATOM   1002 N  N     . VAL A 1 149 ? -1.754  52.146 -13.740 1.00 22.29  ? 135  VAL A N     1 
ATOM   1003 C  CA    . VAL A 1 149 ? -3.171  51.827 -13.875 1.00 22.62  ? 135  VAL A CA    1 
ATOM   1004 C  C     . VAL A 1 149 ? -3.992  53.078 -14.120 1.00 23.82  ? 135  VAL A C     1 
ATOM   1005 O  O     . VAL A 1 149 ? -5.142  52.976 -14.563 1.00 24.57  ? 135  VAL A O     1 
ATOM   1006 C  CB    . VAL A 1 149 ? -3.761  51.099 -12.651 1.00 22.86  ? 135  VAL A CB    1 
ATOM   1007 C  CG1   . VAL A 1 149 ? -3.378  49.629 -12.665 1.00 21.79  ? 135  VAL A CG1   1 
ATOM   1008 C  CG2   . VAL A 1 149 ? -3.392  51.805 -11.327 1.00 21.89  ? 135  VAL A CG2   1 
ATOM   1009 N  N     . ALA A 1 150 ? -3.460  54.247 -13.787 1.00 21.04  ? 136  ALA A N     1 
ATOM   1010 C  CA    . ALA A 1 150 ? -4.148  55.497 -14.023 1.00 24.51  ? 136  ALA A CA    1 
ATOM   1011 C  C     . ALA A 1 150 ? -3.089  56.568 -14.190 1.00 23.33  ? 136  ALA A C     1 
ATOM   1012 O  O     . ALA A 1 150 ? -2.034  56.521 -13.552 1.00 22.03  ? 136  ALA A O     1 
ATOM   1013 C  CB    . ALA A 1 150 ? -5.112  55.871 -12.881 1.00 22.83  ? 136  ALA A CB    1 
ATOM   1014 N  N     . GLN A 1 151 ? -3.379  57.529 -15.059 1.00 21.43  ? 137  GLN A N     1 
ATOM   1015 C  CA    . GLN A 1 151 ? -2.536  58.701 -15.166 1.00 20.89  ? 137  GLN A CA    1 
ATOM   1016 C  C     . GLN A 1 151 ? -3.407  59.874 -15.578 1.00 22.74  ? 137  GLN A C     1 
ATOM   1017 O  O     . GLN A 1 151 ? -4.513  59.703 -16.099 1.00 22.45  ? 137  GLN A O     1 
ATOM   1018 C  CB    . GLN A 1 151 ? -1.374  58.476 -16.141 1.00 21.57  ? 137  GLN A CB    1 
ATOM   1019 C  CG    . GLN A 1 151 ? -1.831  57.948 -17.441 1.00 25.96  ? 137  GLN A CG    1 
ATOM   1020 C  CD    . GLN A 1 151 ? -0.770  57.985 -18.531 1.00 28.72  ? 137  GLN A CD    1 
ATOM   1021 O  OE1   . GLN A 1 151 ? 0.426   58.219 -18.280 1.00 24.75  ? 137  GLN A OE1   1 
ATOM   1022 N  NE2   . GLN A 1 151 ? -1.212  57.742 -19.762 1.00 27.18  ? 137  GLN A NE2   1 
ATOM   1023 N  N     . ALA A 1 152 ? -2.897  61.073 -15.316 1.00 21.66  ? 138  ALA A N     1 
ATOM   1024 C  CA    . ALA A 1 152 ? -3.604  62.301 -15.631 1.00 22.71  ? 138  ALA A CA    1 
ATOM   1025 C  C     . ALA A 1 152 ? -2.575  63.379 -15.920 1.00 22.12  ? 138  ALA A C     1 
ATOM   1026 O  O     . ALA A 1 152 ? -1.488  63.390 -15.331 1.00 19.41  ? 138  ALA A O     1 
ATOM   1027 C  CB    . ALA A 1 152 ? -4.514  62.746 -14.468 1.00 22.23  ? 138  ALA A CB    1 
ATOM   1028 N  N     . ILE A 1 153 ? -2.931  64.290 -16.818 1.00 21.98  ? 139  ILE A N     1 
ATOM   1029 C  CA    . ILE A 1 153 ? -2.219  65.554 -16.971 1.00 22.89  ? 139  ILE A CA    1 
ATOM   1030 C  C     . ILE A 1 153 ? -3.057  66.596 -16.247 1.00 22.40  ? 139  ILE A C     1 
ATOM   1031 O  O     . ILE A 1 153 ? -4.195  66.873 -16.639 1.00 23.66  ? 139  ILE A O     1 
ATOM   1032 C  CB    . ILE A 1 153 ? -2.009  65.931 -18.443 1.00 23.97  ? 139  ILE A CB    1 
ATOM   1033 C  CG1   . ILE A 1 153 ? -1.100  64.931 -19.144 1.00 23.51  ? 139  ILE A CG1   1 
ATOM   1034 C  CG2   . ILE A 1 153 ? -1.434  67.337 -18.564 1.00 24.19  ? 139  ILE A CG2   1 
ATOM   1035 C  CD1   . ILE A 1 153 ? -1.077  65.132 -20.674 1.00 26.92  ? 139  ILE A CD1   1 
ATOM   1036 N  N     . LEU A 1 154 ? -2.505  67.153 -15.181 1.00 21.66  ? 140  LEU A N     1 
ATOM   1037 C  CA    . LEU A 1 154 ? -3.261  68.048 -14.321 1.00 22.16  ? 140  LEU A CA    1 
ATOM   1038 C  C     . LEU A 1 154 ? -3.373  69.413 -14.980 1.00 22.49  ? 140  LEU A C     1 
ATOM   1039 O  O     . LEU A 1 154 ? -2.381  69.974 -15.459 1.00 21.04  ? 140  LEU A O     1 
ATOM   1040 C  CB    . LEU A 1 154 ? -2.591  68.158 -12.946 1.00 21.61  ? 140  LEU A CB    1 
ATOM   1041 C  CG    . LEU A 1 154 ? -2.559  66.843 -12.147 1.00 19.47  ? 140  LEU A CG    1 
ATOM   1042 C  CD1   . LEU A 1 154 ? -2.016  67.048 -10.739 1.00 19.51  ? 140  LEU A CD1   1 
ATOM   1043 C  CD2   . LEU A 1 154 ? -3.946  66.205 -12.097 1.00 18.91  ? 140  LEU A CD2   1 
ATOM   1044 N  N     . THR A 1 155 ? -4.588  69.941 -15.009 1.00 21.85  ? 141  THR A N     1 
ATOM   1045 C  CA    . THR A 1 155 ? -4.851  71.282 -15.485 1.00 22.39  ? 141  THR A CA    1 
ATOM   1046 C  C     . THR A 1 155 ? -5.556  72.048 -14.379 1.00 21.97  ? 141  THR A C     1 
ATOM   1047 O  O     . THR A 1 155 ? -6.035  71.473 -13.398 1.00 20.94  ? 141  THR A O     1 
ATOM   1048 C  CB    . THR A 1 155 ? -5.724  71.278 -16.744 1.00 22.83  ? 141  THR A CB    1 
ATOM   1049 O  OG1   . THR A 1 155 ? -7.070  70.956 -16.374 1.00 22.04  ? 141  THR A OG1   1 
ATOM   1050 C  CG2   . THR A 1 155 ? -5.220  70.243 -17.748 1.00 22.35  ? 141  THR A CG2   1 
ATOM   1051 N  N     . GLU A 1 156 ? -5.636  73.361 -14.574 1.00 22.90  ? 142  GLU A N     1 
ATOM   1052 C  CA    . GLU A 1 156 ? -6.408  74.210 -13.674 1.00 23.31  ? 142  GLU A CA    1 
ATOM   1053 C  C     . GLU A 1 156 ? -7.867  73.763 -13.575 1.00 24.03  ? 142  GLU A C     1 
ATOM   1054 O  O     . GLU A 1 156 ? -8.502  73.937 -12.527 1.00 19.11  ? 142  GLU A O     1 
ATOM   1055 C  CB    . GLU A 1 156 ? -6.332  75.649 -14.170 1.00 24.20  ? 142  GLU A CB    1 
ATOM   1056 C  CG    . GLU A 1 156 ? -7.229  76.609 -13.437 1.00 27.45  ? 142  GLU A CG    1 
ATOM   1057 C  CD    . GLU A 1 156 ? -7.035  78.026 -13.909 1.00 28.58  ? 142  GLU A CD    1 
ATOM   1058 O  OE1   . GLU A 1 156 ? -6.772  78.202 -15.119 1.00 29.92  ? 142  GLU A OE1   1 
ATOM   1059 O  OE2   . GLU A 1 156 ? -7.120  78.948 -13.068 1.00 28.41  ? 142  GLU A OE2   1 
ATOM   1060 N  N     . GLN A 1 157 ? -8.406  73.176 -14.650 1.00 22.01  ? 143  GLN A N     1 
ATOM   1061 C  CA    . GLN A 1 157 ? -9.811  72.798 -14.753 1.00 23.31  ? 143  GLN A CA    1 
ATOM   1062 C  C     . GLN A 1 157 ? -10.124 71.382 -14.275 1.00 22.59  ? 143  GLN A C     1 
ATOM   1063 O  O     . GLN A 1 157 ? -11.307 71.066 -14.082 1.00 22.11  ? 143  GLN A O     1 
ATOM   1064 C  CB    . GLN A 1 157 ? -10.272 72.962 -16.213 1.00 24.52  ? 143  GLN A CB    1 
ATOM   1065 C  CG    . GLN A 1 157 ? -10.076 74.369 -16.739 1.00 26.28  ? 143  GLN A CG    1 
ATOM   1066 C  CD    . GLN A 1 157 ? -10.875 74.688 -18.004 1.00 29.98  ? 143  GLN A CD    1 
ATOM   1067 O  OE1   . GLN A 1 157 ? -11.837 73.997 -18.357 1.00 31.22  ? 143  GLN A OE1   1 
ATOM   1068 N  NE2   . GLN A 1 157 ? -10.467 75.754 -18.695 1.00 33.84  ? 143  GLN A NE2   1 
ATOM   1069 N  N     . ASN A 1 158 ? -9.117  70.528 -14.050 1.00 20.16  ? 144  ASN A N     1 
ATOM   1070 C  CA    . ASN A 1 158 ? -9.369  69.157 -13.628 1.00 22.73  ? 144  ASN A CA    1 
ATOM   1071 C  C     . ASN A 1 158 ? -8.605  68.717 -12.379 1.00 23.82  ? 144  ASN A C     1 
ATOM   1072 O  O     . ASN A 1 158 ? -8.830  67.597 -11.909 1.00 22.31  ? 144  ASN A O     1 
ATOM   1073 C  CB    . ASN A 1 158 ? -9.080  68.180 -14.791 1.00 24.33  ? 144  ASN A CB    1 
ATOM   1074 C  CG    . ASN A 1 158 ? -7.585  68.030 -15.106 1.00 25.46  ? 144  ASN A CG    1 
ATOM   1075 O  OD1   . ASN A 1 158 ? -6.721  68.520 -14.378 1.00 21.32  ? 144  ASN A OD1   1 
ATOM   1076 N  ND2   . ASN A 1 158 ? -7.284  67.326 -16.205 1.00 25.45  ? 144  ASN A ND2   1 
ATOM   1077 N  N     . ALA A 1 159 ? -7.735  69.570 -11.827 1.00 22.63  ? 145  ALA A N     1 
ATOM   1078 C  CA    . ALA A 1 159 ? -6.683  69.147 -10.898 1.00 23.12  ? 145  ALA A CA    1 
ATOM   1079 C  C     . ALA A 1 159 ? -7.187  68.232 -9.785  1.00 22.92  ? 145  ALA A C     1 
ATOM   1080 O  O     . ALA A 1 159 ? -6.759  67.079 -9.665  1.00 23.22  ? 145  ALA A O     1 
ATOM   1081 C  CB    . ALA A 1 159 ? -6.011  70.383 -10.289 1.00 23.56  ? 145  ALA A CB    1 
ATOM   1082 N  N     . CYS A 1 160 ? -8.089  68.731 -8.946  1.00 23.70  ? 146  CYS A N     1 
ATOM   1083 C  CA    . CYS A 1 160 ? -8.396  67.996 -7.723  1.00 24.87  ? 146  CYS A CA    1 
ATOM   1084 C  C     . CYS A 1 160 ? -9.154  66.709 -8.006  1.00 23.83  ? 146  CYS A C     1 
ATOM   1085 O  O     . CYS A 1 160 ? -8.961  65.719 -7.293  1.00 21.30  ? 146  CYS A O     1 
ATOM   1086 C  CB    . CYS A 1 160 ? -9.148  68.886 -6.727  1.00 24.84  ? 146  CYS A CB    1 
ATOM   1087 S  SG    . CYS A 1 160 ? -8.040  70.160 -6.061  1.00 25.96  ? 146  CYS A SG    1 
ATOM   1088 N  N     . TYR A 1 161 ? -10.016 66.681 -9.022  1.00 22.57  ? 147  TYR A N     1 
ATOM   1089 C  CA    . TYR A 1 161 ? -10.692 65.414 -9.249  1.00 24.73  ? 147  TYR A CA    1 
ATOM   1090 C  C     . TYR A 1 161 ? -9.856  64.432 -10.058 1.00 24.45  ? 147  TYR A C     1 
ATOM   1091 O  O     . TYR A 1 161 ? -10.090 63.228 -9.938  1.00 24.97  ? 147  TYR A O     1 
ATOM   1092 C  CB    . TYR A 1 161 ? -12.074 65.604 -9.892  1.00 25.34  ? 147  TYR A CB    1 
ATOM   1093 C  CG    . TYR A 1 161 ? -12.130 66.099 -11.314 1.00 25.40  ? 147  TYR A CG    1 
ATOM   1094 C  CD1   . TYR A 1 161 ? -11.947 65.229 -12.388 1.00 24.95  ? 147  TYR A CD1   1 
ATOM   1095 C  CD2   . TYR A 1 161 ? -12.438 67.435 -11.588 1.00 25.62  ? 147  TYR A CD2   1 
ATOM   1096 C  CE1   . TYR A 1 161 ? -12.019 65.686 -13.708 1.00 27.43  ? 147  TYR A CE1   1 
ATOM   1097 C  CE2   . TYR A 1 161 ? -12.515 67.903 -12.902 1.00 25.98  ? 147  TYR A CE2   1 
ATOM   1098 C  CZ    . TYR A 1 161 ? -12.306 67.021 -13.959 1.00 28.55  ? 147  TYR A CZ    1 
ATOM   1099 O  OH    . TYR A 1 161 ? -12.394 67.474 -15.262 1.00 29.00  ? 147  TYR A OH    1 
ATOM   1100 N  N     . GLU A 1 162 ? -8.886  64.900 -10.858 1.00 21.99  ? 148  GLU A N     1 
ATOM   1101 C  CA    . GLU A 1 162 ? -7.956  63.967 -11.483 1.00 22.03  ? 148  GLU A CA    1 
ATOM   1102 C  C     . GLU A 1 162 ? -7.000  63.377 -10.453 1.00 22.09  ? 148  GLU A C     1 
ATOM   1103 O  O     . GLU A 1 162 ? -6.606  62.208 -10.561 1.00 22.94  ? 148  GLU A O     1 
ATOM   1104 C  CB    . GLU A 1 162 ? -7.179  64.650 -12.614 1.00 22.71  ? 148  GLU A CB    1 
ATOM   1105 C  CG    . GLU A 1 162 ? -7.974  64.773 -13.909 1.00 26.20  ? 148  GLU A CG    1 
ATOM   1106 C  CD    . GLU A 1 162 ? -8.395  63.428 -14.484 1.00 26.63  ? 148  GLU A CD    1 
ATOM   1107 O  OE1   . GLU A 1 162 ? -9.338  62.800 -13.960 1.00 28.59  ? 148  GLU A OE1   1 
ATOM   1108 O  OE2   . GLU A 1 162 ? -7.777  62.983 -15.458 1.00 28.71  ? 148  GLU A OE2   1 
ATOM   1109 N  N     . ILE A 1 163 ? -6.580  64.183 -9.477  1.00 19.85  ? 149  ILE A N     1 
ATOM   1110 C  CA    . ILE A 1 163 ? -5.762  63.668 -8.384  1.00 21.61  ? 149  ILE A CA    1 
ATOM   1111 C  C     . ILE A 1 163 ? -6.520  62.585 -7.634  1.00 20.67  ? 149  ILE A C     1 
ATOM   1112 O  O     . ILE A 1 163 ? -6.004  61.488 -7.397  1.00 19.38  ? 149  ILE A O     1 
ATOM   1113 C  CB    . ILE A 1 163 ? -5.342  64.812 -7.441  1.00 21.86  ? 149  ILE A CB    1 
ATOM   1114 C  CG1   . ILE A 1 163 ? -4.321  65.733 -8.112  1.00 21.21  ? 149  ILE A CG1   1 
ATOM   1115 C  CG2   . ILE A 1 163 ? -4.796  64.256 -6.113  1.00 21.59  ? 149  ILE A CG2   1 
ATOM   1116 C  CD1   . ILE A 1 163 ? -4.121  67.029 -7.347  1.00 21.72  ? 149  ILE A CD1   1 
ATOM   1117 N  N     . ASP A 1 164 ? -7.770  62.868 -7.270  1.00 20.36  ? 150  ASP A N     1 
ATOM   1118 C  CA    . ASP A 1 164 ? -8.529  61.873 -6.527  1.00 21.54  ? 150  ASP A CA    1 
ATOM   1119 C  C     . ASP A 1 164 ? -8.785  60.632 -7.370  1.00 22.06  ? 150  ASP A C     1 
ATOM   1120 O  O     . ASP A 1 164 ? -8.773  59.515 -6.845  1.00 23.07  ? 150  ASP A O     1 
ATOM   1121 C  CB    . ASP A 1 164 ? -9.841  62.472 -6.020  1.00 22.61  ? 150  ASP A CB    1 
ATOM   1122 C  CG    . ASP A 1 164 ? -9.623  63.520 -4.944  1.00 23.08  ? 150  ASP A CG    1 
ATOM   1123 O  OD1   . ASP A 1 164 ? -8.513  63.588 -4.390  1.00 21.70  ? 150  ASP A OD1   1 
ATOM   1124 O  OD2   . ASP A 1 164 ? -10.561 64.275 -4.645  1.00 25.18  ? 150  ASP A OD2   1 
ATOM   1125 N  N     . ARG A 1 165 ? -9.051  60.800 -8.670  1.00 21.54  ? 151  ARG A N     1 
ATOM   1126 C  CA    . ARG A 1 165 ? -9.301  59.626 -9.508  1.00 22.65  ? 151  ARG A CA    1 
ATOM   1127 C  C     . ARG A 1 165 ? -8.074  58.720 -9.585  1.00 21.86  ? 151  ARG A C     1 
ATOM   1128 O  O     . ARG A 1 165 ? -8.190  57.492 -9.468  1.00 22.22  ? 151  ARG A O     1 
ATOM   1129 C  CB    . ARG A 1 165 ? -9.749  60.044 -10.914 1.00 21.18  ? 151  ARG A CB    1 
ATOM   1130 C  CG    . ARG A 1 165 ? -9.977  58.845 -11.857 1.00 21.81  ? 151  ARG A CG    1 
ATOM   1131 C  CD    . ARG A 1 165 ? -10.265 59.245 -13.307 1.00 21.96  ? 151  ARG A CD    1 
ATOM   1132 N  NE    . ARG A 1 165 ? -9.168  59.964 -13.951 1.00 23.72  ? 151  ARG A NE    1 
ATOM   1133 C  CZ    . ARG A 1 165 ? -8.085  59.382 -14.460 1.00 24.74  ? 151  ARG A CZ    1 
ATOM   1134 N  NH1   . ARG A 1 165 ? -7.871  58.081 -14.333 1.00 23.12  ? 151  ARG A NH1   1 
ATOM   1135 N  NH2   . ARG A 1 165 ? -7.191  60.126 -15.109 1.00 24.11  ? 151  ARG A NH2   1 
ATOM   1136 N  N     . VAL A 1 166 ? -6.889  59.298 -9.785  1.00 19.43  ? 152  VAL A N     1 
ATOM   1137 C  CA    . VAL A 1 166 ? -5.699  58.473 -10.009 1.00 19.98  ? 152  VAL A CA    1 
ATOM   1138 C  C     . VAL A 1 166 ? -5.317  57.724 -8.736  1.00 21.79  ? 152  VAL A C     1 
ATOM   1139 O  O     . VAL A 1 166 ? -5.097  56.505 -8.758  1.00 19.42  ? 152  VAL A O     1 
ATOM   1140 C  CB    . VAL A 1 166 ? -4.542  59.334 -10.550 1.00 21.01  ? 152  VAL A CB    1 
ATOM   1141 C  CG1   . VAL A 1 166 ? -3.194  58.580 -10.474 1.00 19.77  ? 152  VAL A CG1   1 
ATOM   1142 C  CG2   . VAL A 1 166 ? -4.836  59.764 -12.010 1.00 19.64  ? 152  VAL A CG2   1 
ATOM   1143 N  N     . LEU A 1 167 ? -5.305  58.432 -7.599  1.00 20.29  ? 153  LEU A N     1 
ATOM   1144 C  CA    . LEU A 1 167 ? -5.020  57.817 -6.306  1.00 20.72  ? 153  LEU A CA    1 
ATOM   1145 C  C     . LEU A 1 167 ? -6.047  56.748 -5.954  1.00 23.78  ? 153  LEU A C     1 
ATOM   1146 O  O     . LEU A 1 167 ? -5.683  55.662 -5.479  1.00 23.14  ? 153  LEU A O     1 
ATOM   1147 C  CB    . LEU A 1 167 ? -5.000  58.897 -5.223  1.00 19.78  ? 153  LEU A CB    1 
ATOM   1148 C  CG    . LEU A 1 167 ? -3.948  59.992 -5.374  1.00 21.92  ? 153  LEU A CG    1 
ATOM   1149 C  CD1   . LEU A 1 167 ? -4.114  61.035 -4.289  1.00 21.94  ? 153  LEU A CD1   1 
ATOM   1150 C  CD2   . LEU A 1 167 ? -2.553  59.415 -5.335  1.00 20.68  ? 153  LEU A CD2   1 
ATOM   1151 N  N     . THR A 1 168 ? -7.337  57.028 -6.191  1.00 22.78  ? 154  THR A N     1 
ATOM   1152 C  CA    . THR A 1 168 ? -8.361  56.024 -5.906  1.00 24.92  ? 154  THR A CA    1 
ATOM   1153 C  C     . THR A 1 168 ? -8.140  54.777 -6.743  1.00 24.41  ? 154  THR A C     1 
ATOM   1154 O  O     . THR A 1 168 ? -8.275  53.650 -6.247  1.00 26.33  ? 154  THR A O     1 
ATOM   1155 C  CB    . THR A 1 168 ? -9.771  56.579 -6.159  1.00 26.01  ? 154  THR A CB    1 
ATOM   1156 O  OG1   . THR A 1 168 ? -10.043 57.670 -5.270  1.00 26.59  ? 154  THR A OG1   1 
ATOM   1157 C  CG2   . THR A 1 168 ? -10.818 55.498 -5.952  1.00 27.97  ? 154  THR A CG2   1 
ATOM   1158 N  N     . THR A 1 169 ? -7.821  54.953 -8.025  1.00 23.00  ? 155  THR A N     1 
ATOM   1159 C  CA    . THR A 1 169 ? -7.576  53.792 -8.868  1.00 25.83  ? 155  THR A CA    1 
ATOM   1160 C  C     . THR A 1 169 ? -6.325  53.042 -8.414  1.00 24.20  ? 155  THR A C     1 
ATOM   1161 O  O     . THR A 1 169 ? -6.276  51.806 -8.477  1.00 23.36  ? 155  THR A O     1 
ATOM   1162 C  CB    . THR A 1 169 ? -7.453  54.216 -10.336 1.00 23.81  ? 155  THR A CB    1 
ATOM   1163 O  OG1   . THR A 1 169 ? -8.645  54.900 -10.741 1.00 27.10  ? 155  THR A OG1   1 
ATOM   1164 C  CG2   . THR A 1 169 ? -7.235  53.006 -11.235 1.00 24.09  ? 155  THR A CG2   1 
ATOM   1165 N  N     . MET A 1 170 ? -5.327  53.712 -7.918  1.00 22.78  ? 156  MET A N     1 
ATOM   1166 C  CA    . MET A 1 170 ? -4.122  53.072 -7.429  1.00 22.67  ? 156  MET A CA    1 
ATOM   1167 C  C     . MET A 1 170 ? -4.463  52.234 -6.209  1.00 24.33  ? 156  MET A C     1 
ATOM   1168 O  O     . MET A 1 170 ? -3.970  51.172 -6.063  1.00 24.49  ? 156  MET A O     1 
ATOM   1169 C  CB    . MET A 1 170 ? -3.090  54.105 -7.020  1.00 20.30  ? 156  MET A CB    1 
ATOM   1170 C  CG    . MET A 1 170 ? -2.298  54.764 -8.114  1.00 23.12  ? 156  MET A CG    1 
ATOM   1171 S  SD    . MET A 1 170 ? -1.284  56.104 -7.539  1.00 27.86  ? 156  MET A SD    1 
ATOM   1172 C  CE    . MET A 1 170 ? -0.202  55.274 -6.472  1.00 18.38  ? 156  MET A CE    1 
ATOM   1173 N  N     . LEU A 1 171 ? -5.327  52.728 -5.344  1.00 24.97  ? 157  LEU A N     1 
ATOM   1174 C  CA    . LEU A 1 171 ? -5.695  51.980 -4.143  1.00 28.54  ? 157  LEU A CA    1 
ATOM   1175 C  C     . LEU A 1 171 ? -6.500  50.741 -4.489  1.00 29.58  ? 157  LEU A C     1 
ATOM   1176 O  O     . LEU A 1 171 ? -6.348  49.693 -3.851  1.00 30.86  ? 157  LEU A O     1 
ATOM   1177 C  CB    . LEU A 1 171 ? -6.501  52.859 -3.193  1.00 29.59  ? 157  LEU A CB    1 
ATOM   1178 C  CG    . LEU A 1 171 ? -5.786  53.995 -2.462  1.00 30.38  ? 157  LEU A CG    1 
ATOM   1179 C  CD1   . LEU A 1 171 ? -6.816  54.987 -1.942  1.00 31.31  ? 157  LEU A CD1   1 
ATOM   1180 C  CD2   . LEU A 1 171 ? -4.921  53.462 -1.323  1.00 34.52  ? 157  LEU A CD2   1 
ATOM   1181 N  N     . ARG A 1 172 ? -7.372  50.847 -5.484  1.00 27.08  ? 158  ARG A N     1 
ATOM   1182 C  CA    . ARG A 1 172 ? -8.184  49.701 -5.855  1.00 30.33  ? 158  ARG A CA    1 
ATOM   1183 C  C     . ARG A 1 172 ? -7.322  48.618 -6.486  1.00 27.79  ? 158  ARG A C     1 
ATOM   1184 O  O     . ARG A 1 172 ? -7.474  47.433 -6.173  1.00 29.70  ? 158  ARG A O     1 
ATOM   1185 C  CB    . ARG A 1 172 ? -9.308  50.146 -6.796  1.00 33.06  ? 158  ARG A CB    1 
ATOM   1186 C  CG    . ARG A 1 172 ? -9.894  49.045 -7.670  1.00 35.23  ? 158  ARG A CG    1 
ATOM   1187 C  CD    . ARG A 1 172 ? -11.007 49.571 -8.580  1.00 39.08  ? 158  ARG A CD    1 
ATOM   1188 N  NE    . ARG A 1 172 ? -10.567 49.618 -9.971  1.00 53.03  ? 158  ARG A NE    1 
ATOM   1189 C  CZ    . ARG A 1 172 ? -10.341 50.734 -10.658 1.00 59.24  ? 158  ARG A CZ    1 
ATOM   1190 N  NH1   . ARG A 1 172 ? -10.568 51.931 -10.132 1.00 43.71  ? 158  ARG A NH1   1 
ATOM   1191 N  NH2   . ARG A 1 172 ? -9.874  50.646 -11.904 1.00 44.69  ? 158  ARG A NH2   1 
ATOM   1192 N  N     . GLU A 1 173 ? -6.383  49.006 -7.343  1.00 25.65  ? 159  GLU A N     1 
ATOM   1193 C  CA    . GLU A 1 173 ? -5.576  48.043 -8.079  1.00 25.26  ? 159  GLU A CA    1 
ATOM   1194 C  C     . GLU A 1 173 ? -4.237  47.729 -7.424  1.00 23.87  ? 159  GLU A C     1 
ATOM   1195 O  O     . GLU A 1 173 ? -3.596  46.744 -7.816  1.00 23.29  ? 159  GLU A O     1 
ATOM   1196 C  CB    . GLU A 1 173 ? -5.330  48.552 -9.506  1.00 25.19  ? 159  GLU A CB    1 
ATOM   1197 C  CG    . GLU A 1 173 ? -6.584  48.751 -10.321 1.00 28.05  ? 159  GLU A CG    1 
ATOM   1198 C  CD    . GLU A 1 173 ? -7.489  47.536 -10.315 1.00 33.27  ? 159  GLU A CD    1 
ATOM   1199 O  OE1   . GLU A 1 173 ? -6.969  46.401 -10.303 1.00 32.99  ? 159  GLU A OE1   1 
ATOM   1200 O  OE2   . GLU A 1 173 ? -8.721  47.716 -10.352 1.00 35.11  ? 159  GLU A OE2   1 
ATOM   1201 N  N     . ARG A 1 174 ? -3.802  48.528 -6.449  1.00 21.91  ? 160  ARG A N     1 
ATOM   1202 C  CA    . ARG A 1 174 ? -2.486  48.367 -5.812  1.00 23.19  ? 160  ARG A CA    1 
ATOM   1203 C  C     . ARG A 1 174 ? -1.372  48.388 -6.849  1.00 21.06  ? 160  ARG A C     1 
ATOM   1204 O  O     . ARG A 1 174 ? -0.535  47.490 -6.907  1.00 21.67  ? 160  ARG A O     1 
ATOM   1205 C  CB    . ARG A 1 174 ? -2.406  47.082 -4.980  1.00 23.12  ? 160  ARG A CB    1 
ATOM   1206 C  CG    . ARG A 1 174 ? -3.504  46.891 -3.982  1.00 26.08  ? 160  ARG A CG    1 
ATOM   1207 C  CD    . ARG A 1 174 ? -3.759  48.124 -3.149  1.00 28.42  ? 160  ARG A CD    1 
ATOM   1208 N  NE    . ARG A 1 174 ? -4.745  47.793 -2.130  1.00 34.98  ? 160  ARG A NE    1 
ATOM   1209 C  CZ    . ARG A 1 174 ? -5.099  48.580 -1.124  1.00 49.48  ? 160  ARG A CZ    1 
ATOM   1210 N  NH1   . ARG A 1 174 ? -4.565  49.782 -0.959  1.00 38.11  ? 160  ARG A NH1   1 
ATOM   1211 N  NH2   . ARG A 1 174 ? -6.017  48.150 -0.263  1.00 45.78  ? 160  ARG A NH2   1 
ATOM   1212 N  N     . ARG A 1 175 ? -1.358  49.430 -7.665  1.00 19.43  ? 161  ARG A N     1 
ATOM   1213 C  CA    . ARG A 1 175 ? -0.409  49.536 -8.762  1.00 20.76  ? 161  ARG A CA    1 
ATOM   1214 C  C     . ARG A 1 175 ? -0.074  51.005 -8.936  1.00 18.76  ? 161  ARG A C     1 
ATOM   1215 O  O     . ARG A 1 175 ? -0.757  51.873 -8.381  1.00 17.61  ? 161  ARG A O     1 
ATOM   1216 C  CB    . ARG A 1 175 ? -0.983  48.917 -10.053 1.00 18.64  ? 161  ARG A CB    1 
ATOM   1217 C  CG    . ARG A 1 175 ? -0.654  47.424 -10.179 1.00 19.29  ? 161  ARG A CG    1 
ATOM   1218 C  CD    . ARG A 1 175 ? -1.136  46.818 -11.496 1.00 20.92  ? 161  ARG A CD    1 
ATOM   1219 N  NE    . ARG A 1 175 ? -0.255  45.748 -11.958 1.00 20.23  ? 161  ARG A NE    1 
ATOM   1220 C  CZ    . ARG A 1 175 ? -0.609  44.821 -12.840 1.00 22.22  ? 161  ARG A CZ    1 
ATOM   1221 N  NH1   . ARG A 1 175 ? -1.837  44.778 -13.346 1.00 20.42  ? 161  ARG A NH1   1 
ATOM   1222 N  NH2   . ARG A 1 175 ? 0.296   43.934 -13.246 1.00 22.31  ? 161  ARG A NH2   1 
ATOM   1223 N  N     . PRO A 1 176 ? 0.991   51.320 -9.675  1.00 17.82  ? 162  PRO A N     1 
ATOM   1224 C  CA    . PRO A 1 176 ? 1.412   52.724 -9.828  1.00 17.72  ? 162  PRO A CA    1 
ATOM   1225 C  C     . PRO A 1 176 ? 0.430   53.622 -10.572 1.00 17.59  ? 162  PRO A C     1 
ATOM   1226 O  O     . PRO A 1 176 ? -0.330  53.192 -11.447 1.00 18.48  ? 162  PRO A O     1 
ATOM   1227 C  CB    . PRO A 1 176 ? 2.722   52.609 -10.626 1.00 16.90  ? 162  PRO A CB    1 
ATOM   1228 C  CG    . PRO A 1 176 ? 3.219   51.265 -10.313 1.00 17.27  ? 162  PRO A CG    1 
ATOM   1229 C  CD    . PRO A 1 176 ? 2.000   50.403 -10.233 1.00 19.63  ? 162  PRO A CD    1 
ATOM   1230 N  N     . GLY A 1 177 ? 0.489   54.908 -10.229 1.00 17.98  ? 163  GLY A N     1 
ATOM   1231 C  CA    . GLY A 1 177 ? -0.214  55.931 -10.968 1.00 17.93  ? 163  GLY A CA    1 
ATOM   1232 C  C     . GLY A 1 177 ? 0.760   57.031 -11.348 1.00 18.43  ? 163  GLY A C     1 
ATOM   1233 O  O     . GLY A 1 177 ? 1.882   57.078 -10.854 1.00 16.26  ? 163  GLY A O     1 
ATOM   1234 N  N     . TYR A 1 178 ? 0.301   57.928 -12.222 1.00 18.62  ? 164  TYR A N     1 
ATOM   1235 C  CA    . TYR A 1 178 ? 1.154   58.965 -12.783 1.00 18.41  ? 164  TYR A CA    1 
ATOM   1236 C  C     . TYR A 1 178 ? 0.381   60.268 -12.855 1.00 19.48  ? 164  TYR A C     1 
ATOM   1237 O  O     . TYR A 1 178 ? -0.775  60.287 -13.285 1.00 18.35  ? 164  TYR A O     1 
ATOM   1238 C  CB    . TYR A 1 178 ? 1.630   58.550 -14.184 1.00 19.77  ? 164  TYR A CB    1 
ATOM   1239 C  CG    . TYR A 1 178 ? 2.498   59.532 -14.941 1.00 19.67  ? 164  TYR A CG    1 
ATOM   1240 C  CD1   . TYR A 1 178 ? 1.981   60.719 -15.451 1.00 19.48  ? 164  TYR A CD1   1 
ATOM   1241 C  CD2   . TYR A 1 178 ? 3.816   59.228 -15.215 1.00 18.30  ? 164  TYR A CD2   1 
ATOM   1242 C  CE1   . TYR A 1 178 ? 2.776   61.596 -16.175 1.00 19.62  ? 164  TYR A CE1   1 
ATOM   1243 C  CE2   . TYR A 1 178 ? 4.617   60.091 -15.958 1.00 19.45  ? 164  TYR A CE2   1 
ATOM   1244 C  CZ    . TYR A 1 178 ? 4.090   61.273 -16.430 1.00 19.10  ? 164  TYR A CZ    1 
ATOM   1245 O  OH    . TYR A 1 178 ? 4.883   62.134 -17.158 1.00 17.52  ? 164  TYR A OH    1 
ATOM   1246 N  N     . LEU A 1 179 ? 1.029   61.359 -12.462 1.00 17.74  ? 165  LEU A N     1 
ATOM   1247 C  CA    . LEU A 1 179 ? 0.433   62.686 -12.539 1.00 18.77  ? 165  LEU A CA    1 
ATOM   1248 C  C     . LEU A 1 179 ? 1.472   63.633 -13.110 1.00 19.44  ? 165  LEU A C     1 
ATOM   1249 O  O     . LEU A 1 179 ? 2.559   63.770 -12.544 1.00 19.31  ? 165  LEU A O     1 
ATOM   1250 C  CB    . LEU A 1 179 ? -0.026  63.175 -11.160 1.00 17.61  ? 165  LEU A CB    1 
ATOM   1251 C  CG    . LEU A 1 179 ? -1.155  62.403 -10.480 1.00 18.26  ? 165  LEU A CG    1 
ATOM   1252 C  CD1   . LEU A 1 179 ? -1.347  62.945 -9.057  1.00 18.87  ? 165  LEU A CD1   1 
ATOM   1253 C  CD2   . LEU A 1 179 ? -2.446  62.486 -11.293 1.00 18.04  ? 165  LEU A CD2   1 
ATOM   1254 N  N     . MET A 1 180 ? 1.160   64.281 -14.227 1.00 19.38  ? 166  MET A N     1 
ATOM   1255 C  CA    . MET A 1 180 ? 2.043   65.334 -14.691 1.00 20.50  ? 166  MET A CA    1 
ATOM   1256 C  C     . MET A 1 180 ? 1.554   66.625 -14.051 1.00 20.89  ? 166  MET A C     1 
ATOM   1257 O  O     . MET A 1 180 ? 0.379   66.978 -14.176 1.00 19.10  ? 166  MET A O     1 
ATOM   1258 C  CB    . MET A 1 180 ? 2.073   65.474 -16.214 1.00 19.24  ? 166  MET A CB    1 
ATOM   1259 C  CG    . MET A 1 180 ? 2.788   66.767 -16.643 1.00 22.10  ? 166  MET A CG    1 
ATOM   1260 S  SD    . MET A 1 180 ? 2.470   67.460 -18.288 1.00 24.03  ? 166  MET A SD    1 
ATOM   1261 C  CE    . MET A 1 180 ? 2.916   66.082 -19.354 1.00 23.39  ? 166  MET A CE    1 
ATOM   1262 N  N     . LEU A 1 181 ? 2.457   67.331 -13.375 1.00 19.29  ? 167  LEU A N     1 
ATOM   1263 C  CA    . LEU A 1 181 ? 2.111   68.554 -12.661 1.00 20.98  ? 167  LEU A CA    1 
ATOM   1264 C  C     . LEU A 1 181 ? 2.848   69.737 -13.274 1.00 21.29  ? 167  LEU A C     1 
ATOM   1265 O  O     . LEU A 1 181 ? 3.975   70.064 -12.856 1.00 18.31  ? 167  LEU A O     1 
ATOM   1266 C  CB    . LEU A 1 181 ? 2.442   68.418 -11.175 1.00 19.27  ? 167  LEU A CB    1 
ATOM   1267 C  CG    . LEU A 1 181 ? 2.071   69.620 -10.308 1.00 22.43  ? 167  LEU A CG    1 
ATOM   1268 C  CD1   . LEU A 1 181 ? 0.573   69.934 -10.401 1.00 22.13  ? 167  LEU A CD1   1 
ATOM   1269 C  CD2   . LEU A 1 181 ? 2.482   69.353 -8.877  1.00 19.80  ? 167  LEU A CD2   1 
ATOM   1270 N  N     . PRO A 1 182 ? 2.233   70.437 -14.233 1.00 22.12  ? 168  PRO A N     1 
ATOM   1271 C  CA    . PRO A 1 182 ? 2.828   71.686 -14.724 1.00 23.36  ? 168  PRO A CA    1 
ATOM   1272 C  C     . PRO A 1 182 ? 2.982   72.675 -13.576 1.00 24.55  ? 168  PRO A C     1 
ATOM   1273 O  O     . PRO A 1 182 ? 2.155   72.728 -12.661 1.00 22.74  ? 168  PRO A O     1 
ATOM   1274 C  CB    . PRO A 1 182 ? 1.818   72.181 -15.772 1.00 24.09  ? 168  PRO A CB    1 
ATOM   1275 C  CG    . PRO A 1 182 ? 0.966   70.943 -16.119 1.00 23.19  ? 168  PRO A CG    1 
ATOM   1276 C  CD    . PRO A 1 182 ? 0.889   70.210 -14.798 1.00 22.40  ? 168  PRO A CD    1 
ATOM   1277 N  N     . ALA A 1 183 ? 4.063   73.453 -13.625 1.00 24.13  ? 169  ALA A N     1 
ATOM   1278 C  CA    . ALA A 1 183 ? 4.428   74.294 -12.487 1.00 26.25  ? 169  ALA A CA    1 
ATOM   1279 C  C     . ALA A 1 183 ? 3.347   75.325 -12.176 1.00 27.16  ? 169  ALA A C     1 
ATOM   1280 O  O     . ALA A 1 183 ? 3.103   75.647 -11.004 1.00 26.81  ? 169  ALA A O     1 
ATOM   1281 C  CB    . ALA A 1 183 ? 5.773   74.976 -12.748 1.00 29.65  ? 169  ALA A CB    1 
ATOM   1282 N  N     . ASP A 1 184 ? 2.687   75.855 -13.208 1.00 27.45  ? 170  ASP A N     1 
ATOM   1283 C  CA    . ASP A 1 184 ? 1.647   76.851 -12.964 1.00 27.94  ? 170  ASP A CA    1 
ATOM   1284 C  C     . ASP A 1 184 ? 0.401   76.219 -12.341 1.00 26.77  ? 170  ASP A C     1 
ATOM   1285 O  O     . ASP A 1 184 ? -0.237  76.821 -11.465 1.00 27.31  ? 170  ASP A O     1 
ATOM   1286 C  CB    . ASP A 1 184 ? 1.318   77.584 -14.272 1.00 28.87  ? 170  ASP A CB    1 
ATOM   1287 C  CG    . ASP A 1 184 ? 0.783   76.652 -15.363 1.00 28.21  ? 170  ASP A CG    1 
ATOM   1288 O  OD1   . ASP A 1 184 ? 1.333   75.538 -15.526 1.00 26.53  ? 170  ASP A OD1   1 
ATOM   1289 O  OD2   . ASP A 1 184 ? -0.167  77.046 -16.082 1.00 27.36  ? 170  ASP A OD2   1 
ATOM   1290 N  N     . VAL A 1 185 ? 0.043   75.003 -12.769 1.00 25.10  ? 171  VAL A N     1 
ATOM   1291 C  CA    . VAL A 1 185 ? -1.127  74.317 -12.214 1.00 23.21  ? 171  VAL A CA    1 
ATOM   1292 C  C     . VAL A 1 185 ? -0.963  74.084 -10.711 1.00 24.86  ? 171  VAL A C     1 
ATOM   1293 O  O     . VAL A 1 185 ? -1.934  74.158 -9.944  1.00 24.15  ? 171  VAL A O     1 
ATOM   1294 C  CB    . VAL A 1 185 ? -1.366  72.997 -12.969 1.00 22.96  ? 171  VAL A CB    1 
ATOM   1295 C  CG1   . VAL A 1 185 ? -2.557  72.237 -12.376 1.00 22.80  ? 171  VAL A CG1   1 
ATOM   1296 C  CG2   . VAL A 1 185 ? -1.562  73.265 -14.471 1.00 23.91  ? 171  VAL A CG2   1 
ATOM   1297 N  N     . ALA A 1 186 ? 0.263   73.777 -10.272 1.00 22.97  ? 172  ALA A N     1 
ATOM   1298 C  CA    . ALA A 1 186 ? 0.527   73.504 -8.861  1.00 23.54  ? 172  ALA A CA    1 
ATOM   1299 C  C     . ALA A 1 186 ? 0.209   74.697 -7.967  1.00 23.80  ? 172  ALA A C     1 
ATOM   1300 O  O     . ALA A 1 186 ? -0.108  74.517 -6.785  1.00 24.69  ? 172  ALA A O     1 
ATOM   1301 C  CB    . ALA A 1 186 ? 1.990   73.088 -8.673  1.00 22.47  ? 172  ALA A CB    1 
ATOM   1302 N  N     . LYS A 1 187 ? 0.294   75.914 -8.495  1.00 25.06  ? 173  LYS A N     1 
ATOM   1303 C  CA    . LYS A 1 187 ? -0.006  77.101 -7.705  1.00 29.89  ? 173  LYS A CA    1 
ATOM   1304 C  C     . LYS A 1 187 ? -1.457  77.535 -7.786  1.00 28.09  ? 173  LYS A C     1 
ATOM   1305 O  O     . LYS A 1 187 ? -1.826  78.523 -7.139  1.00 26.87  ? 173  LYS A O     1 
ATOM   1306 C  CB    . LYS A 1 187 ? 0.860   78.276 -8.128  1.00 31.57  ? 173  LYS A CB    1 
ATOM   1307 C  CG    . LYS A 1 187 ? 2.327   78.019 -8.022  1.00 34.15  ? 173  LYS A CG    1 
ATOM   1308 C  CD    . LYS A 1 187 ? 2.945   78.336 -9.338  1.00 39.19  ? 173  LYS A CD    1 
ATOM   1309 C  CE    . LYS A 1 187 ? 3.732   79.602 -9.185  1.00 52.99  ? 173  LYS A CE    1 
ATOM   1310 N  NZ    . LYS A 1 187 ? 4.831   79.660 -10.138 1.00 62.60  ? 173  LYS A NZ    1 
ATOM   1311 N  N     . LYS A 1 188 ? -2.283  76.839 -8.560  1.00 26.18  ? 174  LYS A N     1 
ATOM   1312 C  CA    . LYS A 1 188 ? -3.664  77.263 -8.694  1.00 26.86  ? 174  LYS A CA    1 
ATOM   1313 C  C     . LYS A 1 188 ? -4.406  77.028 -7.386  1.00 27.20  ? 174  LYS A C     1 
ATOM   1314 O  O     . LYS A 1 188 ? -4.130  76.073 -6.656  1.00 26.91  ? 174  LYS A O     1 
ATOM   1315 C  CB    . LYS A 1 188 ? -4.328  76.523 -9.848  1.00 26.28  ? 174  LYS A CB    1 
ATOM   1316 C  CG    . LYS A 1 188 ? -4.746  77.481 -10.931 1.00 28.32  ? 174  LYS A CG    1 
ATOM   1317 C  CD    . LYS A 1 188 ? -3.552  77.890 -11.714 1.00 26.13  ? 174  LYS A CD    1 
ATOM   1318 C  CE    . LYS A 1 188 ? -3.858  79.050 -12.618 1.00 27.99  ? 174  LYS A CE    1 
ATOM   1319 N  NZ    . LYS A 1 188 ? -2.798  79.190 -13.621 1.00 29.91  ? 174  LYS A NZ    1 
ATOM   1320 N  N     . ALA A 1 189 ? -5.344  77.925 -7.089  1.00 26.98  ? 175  ALA A N     1 
ATOM   1321 C  CA    . ALA A 1 189 ? -6.040  77.890 -5.805  1.00 29.64  ? 175  ALA A CA    1 
ATOM   1322 C  C     . ALA A 1 189 ? -6.815  76.588 -5.650  1.00 28.27  ? 175  ALA A C     1 
ATOM   1323 O  O     . ALA A 1 189 ? -7.375  76.061 -6.614  1.00 28.49  ? 175  ALA A O     1 
ATOM   1324 C  CB    . ALA A 1 189 ? -6.983  79.085 -5.675  1.00 28.16  ? 175  ALA A CB    1 
ATOM   1325 N  N     . ALA A 1 190 ? -6.833  76.058 -4.430  1.00 27.62  ? 176  ALA A N     1 
ATOM   1326 C  CA    . ALA A 1 190 ? -7.597  74.856 -4.132  1.00 28.09  ? 176  ALA A CA    1 
ATOM   1327 C  C     . ALA A 1 190 ? -8.183  74.977 -2.730  1.00 29.34  ? 176  ALA A C     1 
ATOM   1328 O  O     . ALA A 1 190 ? -7.955  75.961 -2.017  1.00 30.01  ? 176  ALA A O     1 
ATOM   1329 C  CB    . ALA A 1 190 ? -6.732  73.601 -4.278  1.00 25.45  ? 176  ALA A CB    1 
ATOM   1330 N  N     . THR A 1 191 ? -8.973  73.979 -2.342  1.00 29.02  ? 177  THR A N     1 
ATOM   1331 C  CA    . THR A 1 191 ? -9.589  73.967 -1.030  1.00 28.96  ? 177  THR A CA    1 
ATOM   1332 C  C     . THR A 1 191 ? -9.231  72.685 -0.288  1.00 28.54  ? 177  THR A C     1 
ATOM   1333 O  O     . THR A 1 191 ? -9.329  71.590 -0.864  1.00 24.00  ? 177  THR A O     1 
ATOM   1334 C  CB    . THR A 1 191 ? -11.106 74.096 -1.153  1.00 29.26  ? 177  THR A CB    1 
ATOM   1335 O  OG1   . THR A 1 191 ? -11.414 75.382 -1.700  1.00 31.10  ? 177  THR A OG1   1 
ATOM   1336 C  CG2   . THR A 1 191 ? -11.766 73.978 0.203   1.00 29.50  ? 177  THR A CG2   1 
ATOM   1337 N  N     . PRO A 1 192 ? -8.814  72.774 0.973   1.00 29.81  ? 178  PRO A N     1 
ATOM   1338 C  CA    . PRO A 1 192 ? -8.544  71.563 1.763   1.00 28.52  ? 178  PRO A CA    1 
ATOM   1339 C  C     . PRO A 1 192 ? -9.801  70.724 1.898   1.00 29.88  ? 178  PRO A C     1 
ATOM   1340 O  O     . PRO A 1 192 ? -10.858 71.240 2.297   1.00 30.41  ? 178  PRO A O     1 
ATOM   1341 C  CB    . PRO A 1 192 ? -8.117  72.125 3.129   1.00 28.90  ? 178  PRO A CB    1 
ATOM   1342 C  CG    . PRO A 1 192 ? -7.552  73.472 2.808   1.00 29.21  ? 178  PRO A CG    1 
ATOM   1343 C  CD    . PRO A 1 192 ? -8.460  74.001 1.715   1.00 28.18  ? 178  PRO A CD    1 
ATOM   1344 N  N     . PRO A 1 193 ? -9.725  69.427 1.611   1.00 28.62  ? 179  PRO A N     1 
ATOM   1345 C  CA    . PRO A 1 193 ? -10.911 68.571 1.759   1.00 28.80  ? 179  PRO A CA    1 
ATOM   1346 C  C     . PRO A 1 193 ? -11.188 68.288 3.227   1.00 32.79  ? 179  PRO A C     1 
ATOM   1347 O  O     . PRO A 1 193 ? -10.264 68.178 4.036   1.00 33.19  ? 179  PRO A O     1 
ATOM   1348 C  CB    . PRO A 1 193 ? -10.529 67.287 1.013   1.00 27.80  ? 179  PRO A CB    1 
ATOM   1349 C  CG    . PRO A 1 193 ? -9.012  67.295 0.933   1.00 30.99  ? 179  PRO A CG    1 
ATOM   1350 C  CD    . PRO A 1 193 ? -8.537  68.714 1.095   1.00 27.36  ? 179  PRO A CD    1 
ATOM   1351 N  N     . VAL A 1 194 ? -12.482 68.192 3.570   1.00 33.00  ? 180  VAL A N     1 
ATOM   1352 C  CA    . VAL A 1 194 ? -12.870 67.870 4.945   1.00 35.07  ? 180  VAL A CA    1 
ATOM   1353 C  C     . VAL A 1 194 ? -12.595 66.408 5.260   1.00 34.90  ? 180  VAL A C     1 
ATOM   1354 O  O     . VAL A 1 194 ? -12.139 66.069 6.359   1.00 32.78  ? 180  VAL A O     1 
ATOM   1355 C  CB    . VAL A 1 194 ? -14.355 68.196 5.196   1.00 35.14  ? 180  VAL A CB    1 
ATOM   1356 C  CG1   . VAL A 1 194 ? -14.594 68.374 6.681   1.00 39.00  ? 180  VAL A CG1   1 
ATOM   1357 C  CG2   . VAL A 1 194 ? -14.783 69.422 4.445   1.00 36.36  ? 180  VAL A CG2   1 
ATOM   1358 N  N     . ASN A 1 195 ? -12.889 65.523 4.314   1.00 34.57  ? 181  ASN A N     1 
ATOM   1359 C  CA    . ASN A 1 195 ? -12.825 64.082 4.510   1.00 35.56  ? 181  ASN A CA    1 
ATOM   1360 C  C     . ASN A 1 195 ? -11.596 63.517 3.822   1.00 34.60  ? 181  ASN A C     1 
ATOM   1361 O  O     . ASN A 1 195 ? -11.247 63.938 2.714   1.00 36.04  ? 181  ASN A O     1 
ATOM   1362 C  CB    . ASN A 1 195 ? -14.077 63.404 3.947   1.00 35.92  ? 181  ASN A CB    1 
ATOM   1363 C  CG    . ASN A 1 195 ? -15.336 63.763 4.711   1.00 34.83  ? 181  ASN A CG    1 
ATOM   1364 O  OD1   . ASN A 1 195 ? -15.297 64.023 5.905   1.00 38.28  ? 181  ASN A OD1   1 
ATOM   1365 N  ND2   . ASN A 1 195 ? -16.449 63.843 4.000   1.00 36.33  ? 181  ASN A ND2   1 
ATOM   1366 N  N     . ALA A 1 196 ? -10.970 62.531 4.456   1.00 34.92  ? 182  ALA A N     1 
ATOM   1367 C  CA    . ALA A 1 196 ? -9.865  61.834 3.817   1.00 34.60  ? 182  ALA A CA    1 
ATOM   1368 C  C     . ALA A 1 196 ? -10.336 61.104 2.563   1.00 37.97  ? 182  ALA A C     1 
ATOM   1369 O  O     . ALA A 1 196 ? -11.514 60.780 2.402   1.00 37.85  ? 182  ALA A O     1 
ATOM   1370 C  CB    . ALA A 1 196 ? -9.232  60.840 4.788   1.00 34.53  ? 182  ALA A CB    1 
ATOM   1371 N  N     . LEU A 1 197 ? -9.410  60.902 1.638   1.00 37.24  ? 183  LEU A N     1 
ATOM   1372 C  CA    . LEU A 1 197 ? -9.688  60.044 0.500   1.00 38.14  ? 183  LEU A CA    1 
ATOM   1373 C  C     . LEU A 1 197 ? -9.726  58.602 0.975   1.00 42.75  ? 183  LEU A C     1 
ATOM   1374 O  O     . LEU A 1 197 ? -8.778  58.125 1.606   1.00 43.37  ? 183  LEU A O     1 
ATOM   1375 C  CB    . LEU A 1 197 ? -8.627  60.233 -0.572  1.00 36.04  ? 183  LEU A CB    1 
ATOM   1376 C  CG    . LEU A 1 197 ? -8.894  59.577 -1.916  1.00 34.80  ? 183  LEU A CG    1 
ATOM   1377 C  CD1   . LEU A 1 197 ? -9.951  60.371 -2.662  1.00 31.53  ? 183  LEU A CD1   1 
ATOM   1378 C  CD2   . LEU A 1 197 ? -7.592  59.539 -2.709  1.00 28.56  ? 183  LEU A CD2   1 
ATOM   1379 N  N     . THR A 1 198 ? -10.810 57.901 0.665   1.00 46.16  ? 184  THR A N     1 
ATOM   1380 C  CA    . THR A 1 198 ? -10.969 56.516 1.076   1.00 51.28  ? 184  THR A CA    1 
ATOM   1381 C  C     . THR A 1 198 ? -11.335 55.653 -0.122  1.00 53.42  ? 184  THR A C     1 
ATOM   1382 O  O     . THR A 1 198 ? -12.018 56.098 -1.049  1.00 51.60  ? 184  THR A O     1 
ATOM   1383 C  CB    . THR A 1 198 ? -12.051 56.379 2.176   1.00 54.78  ? 184  THR A CB    1 
ATOM   1384 O  OG1   . THR A 1 198 ? -11.785 55.221 2.977   1.00 59.80  ? 184  THR A OG1   1 
ATOM   1385 C  CG2   . THR A 1 198 ? -13.459 56.275 1.575   1.00 55.68  ? 184  THR A CG2   1 
ATOM   1386 N  N     . LEU A 1 199 ? -10.859 54.410 -0.094  1.00 55.16  ? 185  LEU A N     1 
ATOM   1387 C  CA    . LEU A 1 199 ? -11.265 53.407 -1.073  1.00 55.60  ? 185  LEU A CA    1 
ATOM   1388 C  C     . LEU A 1 199 ? -12.443 52.662 -0.464  1.00 58.62  ? 185  LEU A C     1 
ATOM   1389 O  O     . LEU A 1 199 ? -12.263 51.781 0.383   1.00 57.81  ? 185  LEU A O     1 
ATOM   1390 C  CB    . LEU A 1 199 ? -10.116 52.455 -1.384  1.00 58.74  ? 185  LEU A CB    1 
ATOM   1391 C  CG    . LEU A 1 199 ? -10.345 51.416 -2.487  1.00 55.16  ? 185  LEU A CG    1 
ATOM   1392 C  CD1   . LEU A 1 199 ? -10.372 52.070 -3.864  1.00 42.66  ? 185  LEU A CD1   1 
ATOM   1393 C  CD2   . LEU A 1 199 ? -9.318  50.290 -2.421  1.00 45.27  ? 185  LEU A CD2   1 
ATOM   1394 N  N     . ARG A 1 200 ? -13.653 53.019 -0.889  1.00 54.95  ? 186  ARG A N     1 
ATOM   1395 C  CA    . ARG A 1 200 ? -14.834 52.303 -0.434  1.00 56.77  ? 186  ARG A CA    1 
ATOM   1396 C  C     . ARG A 1 200 ? -14.747 50.844 -0.861  1.00 55.60  ? 186  ARG A C     1 
ATOM   1397 O  O     . ARG A 1 200 ? -14.437 50.543 -2.019  1.00 54.58  ? 186  ARG A O     1 
ATOM   1398 C  CB    . ARG A 1 200 ? -16.096 52.957 -0.987  1.00 53.14  ? 186  ARG A CB    1 
ATOM   1399 N  N     . HIS A 1 201 ? -15.013 49.939 0.078   1.00 56.95  ? 187  HIS A N     1 
ATOM   1400 C  CA    . HIS A 1 201 ? -14.928 48.512 -0.208  1.00 53.28  ? 187  HIS A CA    1 
ATOM   1401 C  C     . HIS A 1 201 ? -15.989 48.126 -1.234  1.00 51.76  ? 187  HIS A C     1 
ATOM   1402 O  O     . HIS A 1 201 ? -17.180 48.389 -1.035  1.00 51.33  ? 187  HIS A O     1 
ATOM   1403 C  CB    . HIS A 1 201 ? -15.098 47.702 1.076   1.00 51.17  ? 187  HIS A CB    1 
ATOM   1404 N  N     . ALA A 1 202 ? -15.558 47.522 -2.339  1.00 49.03  ? 188  ALA A N     1 
ATOM   1405 C  CA    . ALA A 1 202 ? -16.511 47.049 -3.327  1.00 46.60  ? 188  ALA A CA    1 
ATOM   1406 C  C     . ALA A 1 202 ? -17.234 45.817 -2.796  1.00 44.84  ? 188  ALA A C     1 
ATOM   1407 O  O     . ALA A 1 202 ? -16.740 45.094 -1.928  1.00 43.60  ? 188  ALA A O     1 
ATOM   1408 C  CB    . ALA A 1 202 ? -15.815 46.722 -4.649  1.00 44.04  ? 188  ALA A CB    1 
ATOM   1409 N  N     . HIS A 1 203 ? -18.421 45.576 -3.328  1.00 43.78  ? 189  HIS A N     1 
ATOM   1410 C  CA    . HIS A 1 203 ? -19.205 44.424 -2.923  1.00 42.36  ? 189  HIS A CA    1 
ATOM   1411 C  C     . HIS A 1 203 ? -19.709 43.731 -4.170  1.00 38.83  ? 189  HIS A C     1 
ATOM   1412 O  O     . HIS A 1 203 ? -20.246 44.384 -5.070  1.00 39.31  ? 189  HIS A O     1 
ATOM   1413 C  CB    . HIS A 1 203 ? -20.385 44.833 -2.036  1.00 46.16  ? 189  HIS A CB    1 
ATOM   1414 C  CG    . HIS A 1 203 ? -19.975 45.410 -0.719  1.00 55.44  ? 189  HIS A CG    1 
ATOM   1415 N  ND1   . HIS A 1 203 ? -20.471 46.604 -0.243  1.00 61.53  ? 189  HIS A ND1   1 
ATOM   1416 C  CD2   . HIS A 1 203 ? -19.100 44.966 0.215   1.00 55.00  ? 189  HIS A CD2   1 
ATOM   1417 C  CE1   . HIS A 1 203 ? -19.931 46.864 0.934   1.00 69.82  ? 189  HIS A CE1   1 
ATOM   1418 N  NE2   . HIS A 1 203 ? -19.094 45.886 1.234   1.00 61.10  ? 189  HIS A NE2   1 
ATOM   1419 N  N     . ALA A 1 204 ? -19.524 42.417 -4.229  1.00 36.90  ? 190  ALA A N     1 
ATOM   1420 C  CA    . ALA A 1 204 ? -20.085 41.644 -5.324  1.00 33.86  ? 190  ALA A CA    1 
ATOM   1421 C  C     . ALA A 1 204 ? -21.602 41.644 -5.223  1.00 33.99  ? 190  ALA A C     1 
ATOM   1422 O  O     . ALA A 1 204 ? -22.167 41.740 -4.129  1.00 34.65  ? 190  ALA A O     1 
ATOM   1423 C  CB    . ALA A 1 204 ? -19.553 40.213 -5.297  1.00 29.88  ? 190  ALA A CB    1 
ATOM   1424 N  N     . ASP A 1 205 ? -22.268 41.558 -6.377  1.00 31.93  ? 191  ASP A N     1 
ATOM   1425 C  CA    . ASP A 1 205 ? -23.685 41.245 -6.350  1.00 33.39  ? 191  ASP A CA    1 
ATOM   1426 C  C     . ASP A 1 205 ? -23.859 39.949 -5.576  1.00 32.42  ? 191  ASP A C     1 
ATOM   1427 O  O     . ASP A 1 205 ? -23.049 39.024 -5.700  1.00 31.65  ? 191  ASP A O     1 
ATOM   1428 C  CB    . ASP A 1 205 ? -24.259 41.118 -7.765  1.00 32.05  ? 191  ASP A CB    1 
ATOM   1429 C  CG    . ASP A 1 205 ? -25.767 40.933 -7.768  1.00 35.50  ? 191  ASP A CG    1 
ATOM   1430 O  OD1   . ASP A 1 205 ? -26.501 41.948 -7.729  1.00 35.13  ? 191  ASP A OD1   1 
ATOM   1431 O  OD2   . ASP A 1 205 ? -26.236 39.775 -7.818  1.00 36.20  ? 191  ASP A OD2   1 
ATOM   1432 N  N     . SER A 1 206 ? -24.872 39.915 -4.714  1.00 31.56  ? 192  SER A N     1 
ATOM   1433 C  CA    . SER A 1 206 ? -25.002 38.792 -3.796  1.00 32.55  ? 192  SER A CA    1 
ATOM   1434 C  C     . SER A 1 206 ? -25.290 37.486 -4.530  1.00 31.27  ? 192  SER A C     1 
ATOM   1435 O  O     . SER A 1 206 ? -24.893 36.410 -4.059  1.00 29.81  ? 192  SER A O     1 
ATOM   1436 C  CB    . SER A 1 206 ? -26.092 39.092 -2.767  1.00 34.79  ? 192  SER A CB    1 
ATOM   1437 O  OG    . SER A 1 206 ? -27.316 39.415 -3.408  1.00 36.83  ? 192  SER A OG    1 
ATOM   1438 N  N     . ALA A 1 207 ? -25.980 37.546 -5.672  1.00 30.27  ? 193  ALA A N     1 
ATOM   1439 C  CA    . ALA A 1 207 ? -26.190 36.324 -6.438  1.00 28.63  ? 193  ALA A CA    1 
ATOM   1440 C  C     . ALA A 1 207 ? -24.887 35.850 -7.062  1.00 27.80  ? 193  ALA A C     1 
ATOM   1441 O  O     . ALA A 1 207 ? -24.628 34.643 -7.128  1.00 27.68  ? 193  ALA A O     1 
ATOM   1442 C  CB    . ALA A 1 207 ? -27.260 36.531 -7.509  1.00 29.13  ? 193  ALA A CB    1 
ATOM   1443 N  N     . CYS A 1 208 ? -24.057 36.783 -7.533  1.00 28.52  ? 194  CYS A N     1 
ATOM   1444 C  CA    . CYS A 1 208 ? -22.728 36.422 -8.024  1.00 26.80  ? 194  CYS A CA    1 
ATOM   1445 C  C     . CYS A 1 208 ? -21.855 35.812 -6.925  1.00 25.00  ? 194  CYS A C     1 
ATOM   1446 O  O     . CYS A 1 208 ? -21.196 34.790 -7.140  1.00 22.17  ? 194  CYS A O     1 
ATOM   1447 C  CB    . CYS A 1 208 ? -22.064 37.648 -8.648  1.00 29.65  ? 194  CYS A CB    1 
ATOM   1448 S  SG    . CYS A 1 208 ? -22.996 38.302 -10.102 1.00 39.30  ? 194  CYS A SG    1 
ATOM   1449 N  N     . LEU A 1 209 ? -21.832 36.413 -5.734  1.00 25.58  ? 195  LEU A N     1 
ATOM   1450 C  CA    . LEU A 1 209 ? -21.060 35.798 -4.657  1.00 25.31  ? 195  LEU A CA    1 
ATOM   1451 C  C     . LEU A 1 209 ? -21.597 34.403 -4.345  1.00 24.93  ? 195  LEU A C     1 
ATOM   1452 O  O     . LEU A 1 209 ? -20.823 33.457 -4.130  1.00 23.15  ? 195  LEU A O     1 
ATOM   1453 C  CB    . LEU A 1 209 ? -21.065 36.685 -3.411  1.00 26.42  ? 195  LEU A CB    1 
ATOM   1454 C  CG    . LEU A 1 209 ? -20.081 36.301 -2.310  1.00 24.88  ? 195  LEU A CG    1 
ATOM   1455 C  CD1   . LEU A 1 209 ? -18.646 36.353 -2.826  1.00 24.22  ? 195  LEU A CD1   1 
ATOM   1456 C  CD2   . LEU A 1 209 ? -20.248 37.215 -1.101  1.00 25.93  ? 195  LEU A CD2   1 
ATOM   1457 N  N     . LYS A 1 210 ? -22.929 34.252 -4.359  1.00 26.24  ? 196  LYS A N     1 
ATOM   1458 C  CA    . LYS A 1 210 ? -23.560 32.969 -4.062  1.00 26.18  ? 196  LYS A CA    1 
ATOM   1459 C  C     . LYS A 1 210 ? -23.112 31.884 -5.040  1.00 25.62  ? 196  LYS A C     1 
ATOM   1460 O  O     . LYS A 1 210 ? -22.846 30.745 -4.634  1.00 26.13  ? 196  LYS A O     1 
ATOM   1461 C  CB    . LYS A 1 210 ? -25.083 33.142 -4.090  1.00 29.84  ? 196  LYS A CB    1 
ATOM   1462 C  CG    . LYS A 1 210 ? -25.915 31.867 -4.069  1.00 33.96  ? 196  LYS A CG    1 
ATOM   1463 C  CD    . LYS A 1 210 ? -26.721 31.737 -2.803  1.00 37.77  ? 196  LYS A CD    1 
ATOM   1464 C  CE    . LYS A 1 210 ? -27.864 30.728 -2.943  1.00 36.42  ? 196  LYS A CE    1 
ATOM   1465 N  NZ    . LYS A 1 210 ? -27.522 29.440 -3.613  1.00 36.83  ? 196  LYS A NZ    1 
ATOM   1466 N  N     . ALA A 1 211 ? -23.025 32.210 -6.336  1.00 24.67  ? 197  ALA A N     1 
ATOM   1467 C  CA    . ALA A 1 211 ? -22.625 31.205 -7.319  1.00 24.89  ? 197  ALA A CA    1 
ATOM   1468 C  C     . ALA A 1 211 ? -21.235 30.658 -7.009  1.00 23.23  ? 197  ALA A C     1 
ATOM   1469 O  O     . ALA A 1 211 ? -21.005 29.444 -7.049  1.00 23.56  ? 197  ALA A O     1 
ATOM   1470 C  CB    . ALA A 1 211 ? -22.669 31.795 -8.736  1.00 22.91  ? 197  ALA A CB    1 
ATOM   1471 N  N     . PHE A 1 212 ? -20.293 31.546 -6.701  1.00 20.84  ? 198  PHE A N     1 
ATOM   1472 C  CA    . PHE A 1 212 ? -18.946 31.106 -6.340  1.00 23.68  ? 198  PHE A CA    1 
ATOM   1473 C  C     . PHE A 1 212 ? -18.969 30.298 -5.046  1.00 23.04  ? 198  PHE A C     1 
ATOM   1474 O  O     . PHE A 1 212 ? -18.315 29.250 -4.938  1.00 22.41  ? 198  PHE A O     1 
ATOM   1475 C  CB    . PHE A 1 212 ? -18.013 32.308 -6.186  1.00 20.53  ? 198  PHE A CB    1 
ATOM   1476 C  CG    . PHE A 1 212 ? -16.695 31.965 -5.525  1.00 21.41  ? 198  PHE A CG    1 
ATOM   1477 C  CD1   . PHE A 1 212 ? -15.704 31.296 -6.237  1.00 19.36  ? 198  PHE A CD1   1 
ATOM   1478 C  CD2   . PHE A 1 212 ? -16.480 32.246 -4.178  1.00 20.16  ? 198  PHE A CD2   1 
ATOM   1479 C  CE1   . PHE A 1 212 ? -14.512 30.946 -5.637  1.00 19.09  ? 198  PHE A CE1   1 
ATOM   1480 C  CE2   . PHE A 1 212 ? -15.276 31.905 -3.559  1.00 20.23  ? 198  PHE A CE2   1 
ATOM   1481 C  CZ    . PHE A 1 212 ? -14.288 31.245 -4.290  1.00 18.82  ? 198  PHE A CZ    1 
ATOM   1482 N  N     . ARG A 1 213 ? -19.714 30.777 -4.052  1.00 24.50  ? 199  ARG A N     1 
ATOM   1483 C  CA    . ARG A 1 213 ? -19.801 30.064 -2.782  1.00 25.03  ? 199  ARG A CA    1 
ATOM   1484 C  C     . ARG A 1 213 ? -20.314 28.643 -2.972  1.00 25.08  ? 199  ARG A C     1 
ATOM   1485 O  O     . ARG A 1 213 ? -19.774 27.693 -2.390  1.00 27.07  ? 199  ARG A O     1 
ATOM   1486 C  CB    . ARG A 1 213 ? -20.716 30.810 -1.816  1.00 27.86  ? 199  ARG A CB    1 
ATOM   1487 C  CG    . ARG A 1 213 ? -20.888 30.043 -0.510  1.00 31.20  ? 199  ARG A CG    1 
ATOM   1488 C  CD    . ARG A 1 213 ? -22.103 30.507 0.253   1.00 32.36  ? 199  ARG A CD    1 
ATOM   1489 N  NE    . ARG A 1 213 ? -22.337 29.666 1.422   1.00 38.11  ? 199  ARG A NE    1 
ATOM   1490 C  CZ    . ARG A 1 213 ? -22.775 28.410 1.389   1.00 44.29  ? 199  ARG A CZ    1 
ATOM   1491 N  NH1   . ARG A 1 213 ? -23.038 27.791 0.244   1.00 36.30  ? 199  ARG A NH1   1 
ATOM   1492 N  NH2   . ARG A 1 213 ? -22.937 27.752 2.534   1.00 36.58  ? 199  ARG A NH2   1 
ATOM   1493 N  N     . ASP A 1 214 ? -21.371 28.472 -3.772  1.00 26.06  ? 200  ASP A N     1 
ATOM   1494 C  CA    . ASP A 1 214 ? -21.924 27.132 -3.948  1.00 26.49  ? 200  ASP A CA    1 
ATOM   1495 C  C     . ASP A 1 214 ? -20.932 26.210 -4.639  1.00 26.37  ? 200  ASP A C     1 
ATOM   1496 O  O     . ASP A 1 214 ? -20.730 25.069 -4.200  1.00 27.34  ? 200  ASP A O     1 
ATOM   1497 C  CB    . ASP A 1 214 ? -23.249 27.191 -4.711  1.00 27.17  ? 200  ASP A CB    1 
ATOM   1498 C  CG    . ASP A 1 214 ? -24.343 27.896 -3.913  1.00 30.73  ? 200  ASP A CG    1 
ATOM   1499 O  OD1   . ASP A 1 214 ? -24.170 28.081 -2.692  1.00 30.31  ? 200  ASP A OD1   1 
ATOM   1500 O  OD2   . ASP A 1 214 ? -25.382 28.246 -4.494  1.00 33.87  ? 200  ASP A OD2   1 
ATOM   1501 N  N     . ALA A 1 215 ? -20.285 26.692 -5.700  1.00 25.08  ? 201  ALA A N     1 
ATOM   1502 C  CA    . ALA A 1 215 ? -19.328 25.853 -6.414  1.00 26.36  ? 201  ALA A CA    1 
ATOM   1503 C  C     . ALA A 1 215 ? -18.125 25.526 -5.539  1.00 26.15  ? 201  ALA A C     1 
ATOM   1504 O  O     . ALA A 1 215 ? -17.674 24.375 -5.501  1.00 26.32  ? 201  ALA A O     1 
ATOM   1505 C  CB    . ALA A 1 215 ? -18.880 26.542 -7.701  1.00 24.81  ? 201  ALA A CB    1 
ATOM   1506 N  N     . ALA A 1 216 ? -17.600 26.524 -4.820  1.00 25.36  ? 202  ALA A N     1 
ATOM   1507 C  CA    . ALA A 1 216 ? -16.483 26.264 -3.915  1.00 24.79  ? 202  ALA A CA    1 
ATOM   1508 C  C     . ALA A 1 216 ? -16.885 25.264 -2.840  1.00 26.16  ? 202  ALA A C     1 
ATOM   1509 O  O     . ALA A 1 216 ? -16.120 24.351 -2.514  1.00 24.75  ? 202  ALA A O     1 
ATOM   1510 C  CB    . ALA A 1 216 ? -16.003 27.568 -3.275  1.00 23.71  ? 202  ALA A CB    1 
ATOM   1511 N  N     . GLU A 1 217 ? -18.092 25.409 -2.293  1.00 25.81  ? 203  GLU A N     1 
ATOM   1512 C  CA    . GLU A 1 217 ? -18.551 24.479 -1.270  1.00 27.48  ? 203  GLU A CA    1 
ATOM   1513 C  C     . GLU A 1 217 ? -18.630 23.056 -1.801  1.00 29.94  ? 203  GLU A C     1 
ATOM   1514 O  O     . GLU A 1 217 ? -18.200 22.106 -1.133  1.00 30.50  ? 203  GLU A O     1 
ATOM   1515 C  CB    . GLU A 1 217 ? -19.909 24.895 -0.740  1.00 28.13  ? 203  GLU A CB    1 
ATOM   1516 C  CG    . GLU A 1 217 ? -20.363 23.848 0.197   1.00 33.39  ? 203  GLU A CG    1 
ATOM   1517 C  CD    . GLU A 1 217 ? -21.539 24.229 0.980   1.00 34.05  ? 203  GLU A CD    1 
ATOM   1518 O  OE1   . GLU A 1 217 ? -22.285 25.158 0.581   1.00 43.90  ? 203  GLU A OE1   1 
ATOM   1519 O  OE2   . GLU A 1 217 ? -21.651 23.617 2.053   1.00 37.98  ? 203  GLU A OE2   1 
ATOM   1520 N  N     . ASN A 1 218 ? -19.205 22.886 -2.995  1.00 29.14  ? 204  ASN A N     1 
ATOM   1521 C  CA    . ASN A 1 218 ? -19.342 21.551 -3.558  1.00 30.42  ? 204  ASN A CA    1 
ATOM   1522 C  C     . ASN A 1 218 ? -17.980 20.905 -3.759  1.00 32.70  ? 204  ASN A C     1 
ATOM   1523 O  O     . ASN A 1 218 ? -17.815 19.703 -3.536  1.00 34.62  ? 204  ASN A O     1 
ATOM   1524 C  CB    . ASN A 1 218 ? -20.103 21.628 -4.879  1.00 34.11  ? 204  ASN A CB    1 
ATOM   1525 C  CG    . ASN A 1 218 ? -20.616 20.282 -5.332  1.00 41.84  ? 204  ASN A CG    1 
ATOM   1526 O  OD1   . ASN A 1 218 ? -20.142 19.731 -6.327  1.00 45.70  ? 204  ASN A OD1   1 
ATOM   1527 N  ND2   . ASN A 1 218 ? -21.581 19.733 -4.594  1.00 42.90  ? 204  ASN A ND2   1 
ATOM   1528 N  N     . ARG A 1 219 ? -16.978 21.695 -4.145  1.00 31.40  ? 205  ARG A N     1 
ATOM   1529 C  CA    . ARG A 1 219 ? -15.630 21.158 -4.256  1.00 31.11  ? 205  ARG A CA    1 
ATOM   1530 C  C     . ARG A 1 219 ? -15.056 20.834 -2.881  1.00 29.87  ? 205  ARG A C     1 
ATOM   1531 O  O     . ARG A 1 219 ? -14.559 19.726 -2.647  1.00 31.76  ? 205  ARG A O     1 
ATOM   1532 C  CB    . ARG A 1 219 ? -14.749 22.157 -5.013  1.00 30.85  ? 205  ARG A CB    1 
ATOM   1533 C  CG    . ARG A 1 219 ? -13.328 21.720 -5.196  1.00 30.20  ? 205  ARG A CG    1 
ATOM   1534 C  CD    . ARG A 1 219 ? -13.285 20.331 -5.795  1.00 33.78  ? 205  ARG A CD    1 
ATOM   1535 N  NE    . ARG A 1 219 ? -11.921 19.830 -5.872  1.00 33.98  ? 205  ARG A NE    1 
ATOM   1536 C  CZ    . ARG A 1 219 ? -11.532 18.833 -6.654  1.00 36.78  ? 205  ARG A CZ    1 
ATOM   1537 N  NH1   . ARG A 1 219 ? -12.384 18.207 -7.454  1.00 33.53  ? 205  ARG A NH1   1 
ATOM   1538 N  NH2   . ARG A 1 219 ? -10.256 18.454 -6.636  1.00 34.90  ? 205  ARG A NH2   1 
ATOM   1539 N  N     . LEU A 1 220 ? -15.160 21.771 -1.938  1.00 29.11  ? 206  LEU A N     1 
ATOM   1540 C  CA    . LEU A 1 220 ? -14.562 21.550 -0.624  1.00 29.28  ? 206  LEU A CA    1 
ATOM   1541 C  C     . LEU A 1 220 ? -15.252 20.432 0.146   1.00 29.28  ? 206  LEU A C     1 
ATOM   1542 O  O     . LEU A 1 220 ? -14.589 19.694 0.889   1.00 29.88  ? 206  LEU A O     1 
ATOM   1543 C  CB    . LEU A 1 220 ? -14.579 22.845 0.181   1.00 27.36  ? 206  LEU A CB    1 
ATOM   1544 C  CG    . LEU A 1 220 ? -13.499 23.817 -0.290  1.00 26.15  ? 206  LEU A CG    1 
ATOM   1545 C  CD1   . LEU A 1 220 ? -13.718 25.200 0.292   1.00 24.96  ? 206  LEU A CD1   1 
ATOM   1546 C  CD2   . LEU A 1 220 ? -12.136 23.273 0.099   1.00 24.99  ? 206  LEU A CD2   1 
ATOM   1547 N  N     . ALA A 1 221 ? -16.565 20.280 -0.020  1.00 29.55  ? 207  ALA A N     1 
ATOM   1548 C  CA    . ALA A 1 221 ? -17.277 19.215 0.684   1.00 30.68  ? 207  ALA A CA    1 
ATOM   1549 C  C     . ALA A 1 221 ? -16.807 17.823 0.278   1.00 31.79  ? 207  ALA A C     1 
ATOM   1550 O  O     . ALA A 1 221 ? -16.995 16.878 1.045   1.00 29.70  ? 207  ALA A O     1 
ATOM   1551 C  CB    . ALA A 1 221 ? -18.782 19.331 0.454   1.00 27.92  ? 207  ALA A CB    1 
ATOM   1552 N  N     . MET A 1 222 ? -16.227 17.655 -0.912  1.00 33.94  ? 208  MET A N     1 
ATOM   1553 C  CA    . MET A 1 222 ? -15.744 16.344 -1.333  1.00 34.10  ? 208  MET A CA    1 
ATOM   1554 C  C     . MET A 1 222 ? -14.224 16.219 -1.279  1.00 34.96  ? 208  MET A C     1 
ATOM   1555 O  O     . MET A 1 222 ? -13.687 15.189 -1.693  1.00 37.03  ? 208  MET A O     1 
ATOM   1556 C  CB    . MET A 1 222 ? -16.261 16.011 -2.738  1.00 36.09  ? 208  MET A CB    1 
ATOM   1557 C  CG    . MET A 1 222 ? -15.693 16.854 -3.870  1.00 44.40  ? 208  MET A CG    1 
ATOM   1558 S  SD    . MET A 1 222 ? -16.834 16.987 -5.285  1.00 62.39  ? 208  MET A SD    1 
ATOM   1559 C  CE    . MET A 1 222 ? -17.778 15.465 -5.142  1.00 49.45  ? 208  MET A CE    1 
ATOM   1560 N  N     . SER A 1 223 ? -13.525 17.204 -0.725  1.00 32.71  ? 209  SER A N     1 
ATOM   1561 C  CA    . SER A 1 223 ? -12.068 17.191 -0.684  1.00 33.85  ? 209  SER A CA    1 
ATOM   1562 C  C     . SER A 1 223 ? -11.595 16.428 0.553   1.00 35.77  ? 209  SER A C     1 
ATOM   1563 O  O     . SER A 1 223 ? -11.932 16.791 1.684   1.00 34.55  ? 209  SER A O     1 
ATOM   1564 C  CB    . SER A 1 223 ? -11.537 18.623 -0.697  1.00 32.52  ? 209  SER A CB    1 
ATOM   1565 O  OG    . SER A 1 223 ? -10.124 18.654 -0.738  1.00 34.87  ? 209  SER A OG    1 
ATOM   1566 N  N     . LYS A 1 224 ? -10.792 15.388 0.340   1.00 36.49  ? 210  LYS A N     1 
ATOM   1567 C  CA    . LYS A 1 224 ? -10.222 14.644 1.461   1.00 38.34  ? 210  LYS A CA    1 
ATOM   1568 C  C     . LYS A 1 224 ? -9.171  15.466 2.206   1.00 37.92  ? 210  LYS A C     1 
ATOM   1569 O  O     . LYS A 1 224 ? -9.215  15.578 3.435   1.00 39.29  ? 210  LYS A O     1 
ATOM   1570 C  CB    . LYS A 1 224 ? -9.623  13.333 0.954   1.00 41.56  ? 210  LYS A CB    1 
ATOM   1571 C  CG    . LYS A 1 224 ? -10.611 12.174 0.827   1.00 49.37  ? 210  LYS A CG    1 
ATOM   1572 C  CD    . LYS A 1 224 ? -10.417 11.129 1.918   1.00 58.31  ? 210  LYS A CD    1 
ATOM   1573 C  CE    . LYS A 1 224 ? -11.740 10.659 2.496   1.00 64.33  ? 210  LYS A CE    1 
ATOM   1574 N  NZ    . LYS A 1 224 ? -11.532 9.515  3.434   1.00 63.87  ? 210  LYS A NZ    1 
ATOM   1575 N  N     . ARG A 1 225 ? -8.217  16.058 1.487   1.00 36.65  ? 211  ARG A N     1 
ATOM   1576 C  CA    . ARG A 1 225 ? -7.263  16.947 2.136   1.00 37.15  ? 211  ARG A CA    1 
ATOM   1577 C  C     . ARG A 1 225 ? -7.103  18.209 1.304   1.00 35.78  ? 211  ARG A C     1 
ATOM   1578 O  O     . ARG A 1 225 ? -6.879  18.154 0.092   1.00 32.29  ? 211  ARG A O     1 
ATOM   1579 C  CB    . ARG A 1 225 ? -5.912  16.258 2.420   1.00 39.41  ? 211  ARG A CB    1 
ATOM   1580 C  CG    . ARG A 1 225 ? -5.209  15.503 1.299   1.00 40.52  ? 211  ARG A CG    1 
ATOM   1581 C  CD    . ARG A 1 225 ? -3.770  15.142 1.775   1.00 43.46  ? 211  ARG A CD    1 
ATOM   1582 N  NE    . ARG A 1 225 ? -3.197  16.174 2.641   1.00 57.16  ? 211  ARG A NE    1 
ATOM   1583 C  CZ    . ARG A 1 225 ? -2.331  17.107 2.254   1.00 50.19  ? 211  ARG A CZ    1 
ATOM   1584 N  NH1   . ARG A 1 225 ? -1.818  17.118 1.035   1.00 38.40  ? 211  ARG A NH1   1 
ATOM   1585 N  NH2   . ARG A 1 225 ? -1.990  18.069 3.106   1.00 46.51  ? 211  ARG A NH2   1 
ATOM   1586 N  N     . THR A 1 226 ? -7.240  19.344 1.973   1.00 34.66  ? 212  THR A N     1 
ATOM   1587 C  CA    . THR A 1 226 ? -7.219  20.650 1.344   1.00 29.70  ? 212  THR A CA    1 
ATOM   1588 C  C     . THR A 1 226 ? -5.991  21.404 1.826   1.00 27.45  ? 212  THR A C     1 
ATOM   1589 O  O     . THR A 1 226 ? -5.658  21.367 3.012   1.00 27.99  ? 212  THR A O     1 
ATOM   1590 C  CB    . THR A 1 226 ? -8.500  21.407 1.706   1.00 30.17  ? 212  THR A CB    1 
ATOM   1591 O  OG1   . THR A 1 226 ? -9.618  20.730 1.125   1.00 31.05  ? 212  THR A OG1   1 
ATOM   1592 C  CG2   . THR A 1 226 ? -8.458  22.846 1.201   1.00 27.52  ? 212  THR A CG2   1 
ATOM   1593 N  N     . ALA A 1 227 ? -5.319  22.087 0.908   1.00 27.63  ? 213  ALA A N     1 
ATOM   1594 C  CA    . ALA A 1 227 ? -4.146  22.872 1.244   1.00 27.38  ? 213  ALA A CA    1 
ATOM   1595 C  C     . ALA A 1 227 ? -4.369  24.314 0.822   1.00 27.39  ? 213  ALA A C     1 
ATOM   1596 O  O     . ALA A 1 227 ? -5.192  24.615 -0.049  1.00 24.75  ? 213  ALA A O     1 
ATOM   1597 C  CB    . ALA A 1 227 ? -2.868  22.319 0.579   1.00 26.92  ? 213  ALA A CB    1 
ATOM   1598 N  N     . LEU A 1 228 ? -3.617  25.211 1.450   1.00 25.59  ? 214  LEU A N     1 
ATOM   1599 C  CA    . LEU A 1 228 ? -3.747  26.638 1.201   1.00 26.16  ? 214  LEU A CA    1 
ATOM   1600 C  C     . LEU A 1 228 ? -2.417  27.172 0.686   1.00 26.56  ? 214  LEU A C     1 
ATOM   1601 O  O     . LEU A 1 228 ? -1.385  26.998 1.341   1.00 24.71  ? 214  LEU A O     1 
ATOM   1602 C  CB    . LEU A 1 228 ? -4.184  27.355 2.478   1.00 25.22  ? 214  LEU A CB    1 
ATOM   1603 C  CG    . LEU A 1 228 ? -4.250  28.873 2.459   1.00 25.44  ? 214  LEU A CG    1 
ATOM   1604 C  CD1   . LEU A 1 228 ? -5.193  29.343 1.384   1.00 24.28  ? 214  LEU A CD1   1 
ATOM   1605 C  CD2   . LEU A 1 228 ? -4.723  29.335 3.835   1.00 27.41  ? 214  LEU A CD2   1 
ATOM   1606 N  N     . LEU A 1 229 ? -2.437  27.789 -0.494  1.00 23.35  ? 215  LEU A N     1 
ATOM   1607 C  CA    . LEU A 1 229 ? -1.262  28.424 -1.083  1.00 24.25  ? 215  LEU A CA    1 
ATOM   1608 C  C     . LEU A 1 229 ? -1.574  29.897 -1.297  1.00 23.94  ? 215  LEU A C     1 
ATOM   1609 O  O     . LEU A 1 229 ? -2.372  30.243 -2.175  1.00 23.78  ? 215  LEU A O     1 
ATOM   1610 C  CB    . LEU A 1 229 ? -0.874  27.757 -2.400  1.00 22.31  ? 215  LEU A CB    1 
ATOM   1611 C  CG    . LEU A 1 229 ? 0.424   28.242 -3.057  1.00 23.71  ? 215  LEU A CG    1 
ATOM   1612 C  CD1   . LEU A 1 229 ? 1.665   27.897 -2.224  1.00 20.73  ? 215  LEU A CD1   1 
ATOM   1613 C  CD2   . LEU A 1 229 ? 0.524   27.682 -4.475  1.00 22.28  ? 215  LEU A CD2   1 
ATOM   1614 N  N     . ALA A 1 230 ? -0.940  30.765 -0.517  1.00 22.43  ? 216  ALA A N     1 
ATOM   1615 C  CA    . ALA A 1 230 ? -1.181  32.197 -0.622  1.00 23.41  ? 216  ALA A CA    1 
ATOM   1616 C  C     . ALA A 1 230 ? 0.088   32.888 -1.092  1.00 22.62  ? 216  ALA A C     1 
ATOM   1617 O  O     . ALA A 1 230 ? 1.192   32.459 -0.760  1.00 23.40  ? 216  ALA A O     1 
ATOM   1618 C  CB    . ALA A 1 230 ? -1.617  32.794 0.717   1.00 22.37  ? 216  ALA A CB    1 
ATOM   1619 N  N     . ASP A 1 231 ? -0.064  33.960 -1.861  1.00 21.26  ? 217  ASP A N     1 
ATOM   1620 C  CA    . ASP A 1 231 ? 1.106   34.688 -2.340  1.00 19.72  ? 217  ASP A CA    1 
ATOM   1621 C  C     . ASP A 1 231 ? 0.829   36.184 -2.406  1.00 19.55  ? 217  ASP A C     1 
ATOM   1622 O  O     . ASP A 1 231 ? -0.080  36.710 -1.757  1.00 20.16  ? 217  ASP A O     1 
ATOM   1623 C  CB    . ASP A 1 231 ? 1.653   34.118 -3.662  1.00 20.61  ? 217  ASP A CB    1 
ATOM   1624 C  CG    . ASP A 1 231 ? 3.165   34.274 -3.748  1.00 20.52  ? 217  ASP A CG    1 
ATOM   1625 O  OD1   . ASP A 1 231 ? 3.924   33.615 -3.003  1.00 20.76  ? 217  ASP A OD1   1 
ATOM   1626 O  OD2   . ASP A 1 231 ? 3.596   35.106 -4.565  1.00 19.53  ? 217  ASP A OD2   1 
ATOM   1627 N  N     . PHE A 1 232 ? 1.694   36.879 -3.158  1.00 18.88  ? 218  PHE A N     1 
ATOM   1628 C  CA    . PHE A 1 232 ? 1.953   38.297 -2.934  1.00 19.54  ? 218  PHE A CA    1 
ATOM   1629 C  C     . PHE A 1 232 ? 0.727   39.194 -3.034  1.00 20.21  ? 218  PHE A C     1 
ATOM   1630 O  O     . PHE A 1 232 ? 0.702   40.249 -2.393  1.00 20.05  ? 218  PHE A O     1 
ATOM   1631 C  CB    . PHE A 1 232 ? 3.078   38.762 -3.857  1.00 18.63  ? 218  PHE A CB    1 
ATOM   1632 C  CG    . PHE A 1 232 ? 2.641   39.038 -5.251  1.00 18.84  ? 218  PHE A CG    1 
ATOM   1633 C  CD1   . PHE A 1 232 ? 2.409   37.979 -6.117  1.00 18.55  ? 218  PHE A CD1   1 
ATOM   1634 C  CD2   . PHE A 1 232 ? 2.433   40.327 -5.696  1.00 20.22  ? 218  PHE A CD2   1 
ATOM   1635 C  CE1   . PHE A 1 232 ? 2.010   38.197 -7.401  1.00 20.42  ? 218  PHE A CE1   1 
ATOM   1636 C  CE2   . PHE A 1 232 ? 2.021   40.554 -7.005  1.00 20.88  ? 218  PHE A CE2   1 
ATOM   1637 C  CZ    . PHE A 1 232 ? 1.807   39.488 -7.848  1.00 20.50  ? 218  PHE A CZ    1 
ATOM   1638 N  N     . LEU A 1 233 ? -0.278  38.842 -3.836  1.00 20.08  ? 219  LEU A N     1 
ATOM   1639 C  CA    . LEU A 1 233 ? -1.434  39.733 -3.904  1.00 20.28  ? 219  LEU A CA    1 
ATOM   1640 C  C     . LEU A 1 233 ? -2.111  39.864 -2.554  1.00 20.81  ? 219  LEU A C     1 
ATOM   1641 O  O     . LEU A 1 233 ? -2.759  40.882 -2.293  1.00 20.59  ? 219  LEU A O     1 
ATOM   1642 C  CB    . LEU A 1 233 ? -2.428  39.285 -4.980  1.00 19.64  ? 219  LEU A CB    1 
ATOM   1643 C  CG    . LEU A 1 233 ? -1.823  39.536 -6.370  1.00 22.26  ? 219  LEU A CG    1 
ATOM   1644 C  CD1   . LEU A 1 233 ? -2.563  38.789 -7.477  1.00 22.87  ? 219  LEU A CD1   1 
ATOM   1645 C  CD2   . LEU A 1 233 ? -1.811  41.030 -6.656  1.00 21.82  ? 219  LEU A CD2   1 
ATOM   1646 N  N     . VAL A 1 234 ? -1.989  38.840 -1.700  1.00 18.80  ? 220  VAL A N     1 
ATOM   1647 C  CA    . VAL A 1 234 ? -2.465  38.941 -0.324  1.00 20.89  ? 220  VAL A CA    1 
ATOM   1648 C  C     . VAL A 1 234 ? -1.790  40.105 0.388   1.00 22.24  ? 220  VAL A C     1 
ATOM   1649 O  O     . VAL A 1 234 ? -2.448  40.905 1.063   1.00 22.66  ? 220  VAL A O     1 
ATOM   1650 C  CB    . VAL A 1 234 ? -2.224  37.616 0.419   1.00 21.21  ? 220  VAL A CB    1 
ATOM   1651 C  CG1   . VAL A 1 234 ? -2.346  37.809 1.938   1.00 19.90  ? 220  VAL A CG1   1 
ATOM   1652 C  CG2   . VAL A 1 234 ? -3.173  36.550 -0.105  1.00 20.33  ? 220  VAL A CG2   1 
ATOM   1653 N  N     . LEU A 1 235 ? -0.469  40.235 0.228   1.00 20.38  ? 221  LEU A N     1 
ATOM   1654 C  CA    . LEU A 1 235 ? 0.247   41.325 0.891   1.00 20.17  ? 221  LEU A CA    1 
ATOM   1655 C  C     . LEU A 1 235 ? -0.195  42.685 0.368   1.00 20.67  ? 221  LEU A C     1 
ATOM   1656 O  O     . LEU A 1 235 ? -0.420  43.614 1.150   1.00 19.85  ? 221  LEU A O     1 
ATOM   1657 C  CB    . LEU A 1 235 ? 1.756   41.160 0.707   1.00 19.89  ? 221  LEU A CB    1 
ATOM   1658 C  CG    . LEU A 1 235 ? 2.410   39.961 1.381   1.00 20.33  ? 221  LEU A CG    1 
ATOM   1659 C  CD1   . LEU A 1 235 ? 3.810   39.792 0.823   1.00 19.65  ? 221  LEU A CD1   1 
ATOM   1660 C  CD2   . LEU A 1 235 ? 2.419   40.109 2.890   1.00 19.26  ? 221  LEU A CD2   1 
ATOM   1661 N  N     . ARG A 1 236 ? -0.322  42.821 -0.957  1.00 20.35  ? 222  ARG A N     1 
ATOM   1662 C  CA    . ARG A 1 236 ? -0.565  44.134 -1.556  1.00 22.38  ? 222  ARG A CA    1 
ATOM   1663 C  C     . ARG A 1 236 ? -1.934  44.692 -1.186  1.00 23.01  ? 222  ARG A C     1 
ATOM   1664 O  O     . ARG A 1 236 ? -2.093  45.911 -1.026  1.00 22.08  ? 222  ARG A O     1 
ATOM   1665 C  CB    . ARG A 1 236 ? -0.422  44.048 -3.077  1.00 20.89  ? 222  ARG A CB    1 
ATOM   1666 C  CG    . ARG A 1 236 ? 0.860   43.313 -3.496  1.00 19.59  ? 222  ARG A CG    1 
ATOM   1667 C  CD    . ARG A 1 236 ? 2.090   44.137 -3.093  1.00 19.18  ? 222  ARG A CD    1 
ATOM   1668 N  NE    . ARG A 1 236 ? 3.260   43.770 -3.885  1.00 19.76  ? 222  ARG A NE    1 
ATOM   1669 C  CZ    . ARG A 1 236 ? 4.335   43.178 -3.386  1.00 19.62  ? 222  ARG A CZ    1 
ATOM   1670 N  NH1   . ARG A 1 236 ? 4.458   42.955 -2.090  1.00 15.37  ? 222  ARG A NH1   1 
ATOM   1671 N  NH2   . ARG A 1 236 ? 5.309   42.796 -4.210  1.00 19.96  ? 222  ARG A NH2   1 
ATOM   1672 N  N     . HIS A 1 237 ? -2.932  43.825 -1.071  1.00 21.92  ? 223  HIS A N     1 
ATOM   1673 C  CA    . HIS A 1 237 ? -4.296  44.246 -0.793  1.00 24.86  ? 223  HIS A CA    1 
ATOM   1674 C  C     . HIS A 1 237 ? -4.619  44.214 0.692   1.00 25.16  ? 223  HIS A C     1 
ATOM   1675 O  O     . HIS A 1 237 ? -5.793  44.252 1.061   1.00 26.69  ? 223  HIS A O     1 
ATOM   1676 C  CB    . HIS A 1 237 ? -5.271  43.362 -1.567  1.00 24.99  ? 223  HIS A CB    1 
ATOM   1677 C  CG    . HIS A 1 237 ? -5.269  43.607 -3.045  1.00 25.82  ? 223  HIS A CG    1 
ATOM   1678 N  ND1   . HIS A 1 237 ? -6.236  44.355 -3.683  1.00 27.88  ? 223  HIS A ND1   1 
ATOM   1679 C  CD2   . HIS A 1 237 ? -4.409  43.202 -4.013  1.00 25.88  ? 223  HIS A CD2   1 
ATOM   1680 C  CE1   . HIS A 1 237 ? -5.980  44.388 -4.980  1.00 25.31  ? 223  HIS A CE1   1 
ATOM   1681 N  NE2   . HIS A 1 237 ? -4.877  43.695 -5.205  1.00 24.05  ? 223  HIS A NE2   1 
ATOM   1682 N  N     . GLY A 1 238 ? -3.601  44.151 1.547   1.00 24.85  ? 224  GLY A N     1 
ATOM   1683 C  CA    . GLY A 1 238 ? -3.795  44.307 2.976   1.00 24.33  ? 224  GLY A CA    1 
ATOM   1684 C  C     . GLY A 1 238 ? -4.441  43.134 3.669   1.00 24.65  ? 224  GLY A C     1 
ATOM   1685 O  O     . GLY A 1 238 ? -5.078  43.323 4.708   1.00 26.59  ? 224  GLY A O     1 
ATOM   1686 N  N     . LEU A 1 239 ? -4.277  41.918 3.143   1.00 24.67  ? 225  LEU A N     1 
ATOM   1687 C  CA    . LEU A 1 239 ? -4.994  40.752 3.653   1.00 24.62  ? 225  LEU A CA    1 
ATOM   1688 C  C     . LEU A 1 239 ? -4.091  39.770 4.391   1.00 24.76  ? 225  LEU A C     1 
ATOM   1689 O  O     . LEU A 1 239 ? -4.509  38.638 4.651   1.00 22.76  ? 225  LEU A O     1 
ATOM   1690 C  CB    . LEU A 1 239 ? -5.729  40.050 2.505   1.00 24.13  ? 225  LEU A CB    1 
ATOM   1691 C  CG    . LEU A 1 239 ? -6.842  40.912 1.898   1.00 25.39  ? 225  LEU A CG    1 
ATOM   1692 C  CD1   . LEU A 1 239 ? -7.284  40.435 0.508   1.00 27.11  ? 225  LEU A CD1   1 
ATOM   1693 C  CD2   . LEU A 1 239 ? -8.027  40.944 2.847   1.00 28.98  ? 225  LEU A CD2   1 
ATOM   1694 N  N     . LYS A 1 240 ? -2.863  40.177 4.733   1.00 25.67  ? 226  LYS A N     1 
ATOM   1695 C  CA    . LYS A 1 240 ? -1.972  39.327 5.520   1.00 27.05  ? 226  LYS A CA    1 
ATOM   1696 C  C     . LYS A 1 240 ? -2.640  38.827 6.805   1.00 28.57  ? 226  LYS A C     1 
ATOM   1697 O  O     . LYS A 1 240 ? -2.636  37.623 7.091   1.00 26.91  ? 226  LYS A O     1 
ATOM   1698 C  CB    . LYS A 1 240 ? -0.683  40.093 5.839   1.00 28.01  ? 226  LYS A CB    1 
ATOM   1699 C  CG    . LYS A 1 240 ? 0.339   39.305 6.644   1.00 28.50  ? 226  LYS A CG    1 
ATOM   1700 C  CD    . LYS A 1 240 ? 1.593   40.123 6.930   1.00 30.44  ? 226  LYS A CD    1 
ATOM   1701 C  CE    . LYS A 1 240 ? 2.524   39.353 7.891   1.00 34.63  ? 226  LYS A CE    1 
ATOM   1702 N  NZ    . LYS A 1 240 ? 3.893   39.959 8.092   1.00 33.77  ? 226  LYS A NZ    1 
ATOM   1703 N  N     . HIS A 1 241 ? -3.232  39.732 7.592   1.00 31.28  ? 227  HIS A N     1 
ATOM   1704 C  CA    . HIS A 1 241 ? -3.809  39.309 8.868   1.00 32.49  ? 227  HIS A CA    1 
ATOM   1705 C  C     . HIS A 1 241 ? -4.964  38.330 8.647   1.00 30.06  ? 227  HIS A C     1 
ATOM   1706 O  O     . HIS A 1 241 ? -5.156  37.395 9.433   1.00 27.52  ? 227  HIS A O     1 
ATOM   1707 C  CB    . HIS A 1 241 ? -4.289  40.520 9.672   1.00 39.05  ? 227  HIS A CB    1 
ATOM   1708 C  CG    . HIS A 1 241 ? -3.209  41.503 10.014  1.00 55.48  ? 227  HIS A CG    1 
ATOM   1709 N  ND1   . HIS A 1 241 ? -1.917  41.133 10.327  1.00 55.04  ? 227  HIS A ND1   1 
ATOM   1710 C  CD2   . HIS A 1 241 ? -3.243  42.855 10.108  1.00 69.26  ? 227  HIS A CD2   1 
ATOM   1711 C  CE1   . HIS A 1 241 ? -1.200  42.214 10.580  1.00 58.02  ? 227  HIS A CE1   1 
ATOM   1712 N  NE2   . HIS A 1 241 ? -1.981  43.272 10.457  1.00 65.19  ? 227  HIS A NE2   1 
ATOM   1713 N  N     . ALA A 1 242 ? -5.738  38.528 7.574   1.00 28.97  ? 228  ALA A N     1 
ATOM   1714 C  CA    . ALA A 1 242 ? -6.821  37.603 7.259   1.00 26.73  ? 228  ALA A CA    1 
ATOM   1715 C  C     . ALA A 1 242 ? -6.297  36.196 6.986   1.00 25.88  ? 228  ALA A C     1 
ATOM   1716 O  O     . ALA A 1 242 ? -6.863  35.209 7.474   1.00 26.57  ? 228  ALA A O     1 
ATOM   1717 C  CB    . ALA A 1 242 ? -7.613  38.124 6.058   1.00 26.60  ? 228  ALA A CB    1 
ATOM   1718 N  N     . LEU A 1 243 ? -5.197  36.082 6.234   1.00 24.89  ? 229  LEU A N     1 
ATOM   1719 C  CA    . LEU A 1 243 ? -4.643  34.766 5.918   1.00 24.48  ? 229  LEU A CA    1 
ATOM   1720 C  C     . LEU A 1 243 ? -4.033  34.095 7.144   1.00 25.57  ? 229  LEU A C     1 
ATOM   1721 O  O     . LEU A 1 243 ? -4.101  32.867 7.280   1.00 25.17  ? 229  LEU A O     1 
ATOM   1722 C  CB    . LEU A 1 243 ? -3.607  34.883 4.795   1.00 20.96  ? 229  LEU A CB    1 
ATOM   1723 C  CG    . LEU A 1 243 ? -4.173  34.653 3.378   1.00 23.44  ? 229  LEU A CG    1 
ATOM   1724 C  CD1   . LEU A 1 243 ? -4.373  33.159 3.136   1.00 20.06  ? 229  LEU A CD1   1 
ATOM   1725 C  CD2   . LEU A 1 243 ? -5.481  35.405 3.146   1.00 19.14  ? 229  LEU A CD2   1 
ATOM   1726 N  N     . GLN A 1 244 ? -3.376  34.869 8.015   1.00 25.62  ? 230  GLN A N     1 
ATOM   1727 C  CA    . GLN A 1 244 ? -2.856  34.296 9.252   1.00 27.55  ? 230  GLN A CA    1 
ATOM   1728 C  C     . GLN A 1 244 ? -3.986  33.820 10.145  1.00 27.01  ? 230  GLN A C     1 
ATOM   1729 O  O     . GLN A 1 244 ? -3.896  32.746 10.748  1.00 27.18  ? 230  GLN A O     1 
ATOM   1730 C  CB    . GLN A 1 244 ? -1.974  35.306 9.998   1.00 28.79  ? 230  GLN A CB    1 
ATOM   1731 C  CG    . GLN A 1 244 ? -0.899  35.923 9.131   1.00 30.93  ? 230  GLN A CG    1 
ATOM   1732 C  CD    . GLN A 1 244 ? -0.041  36.922 9.880   1.00 38.64  ? 230  GLN A CD    1 
ATOM   1733 O  OE1   . GLN A 1 244 ? -0.560  37.762 10.614  1.00 38.48  ? 230  GLN A OE1   1 
ATOM   1734 N  NE2   . GLN A 1 244 ? 1.282   36.845 9.688   1.00 32.92  ? 230  GLN A NE2   1 
ATOM   1735 N  N     . LYS A 1 245 ? -5.045  34.624 10.264  1.00 28.44  ? 231  LYS A N     1 
ATOM   1736 C  CA    . LYS A 1 245 ? -6.185  34.230 11.081  1.00 28.77  ? 231  LYS A CA    1 
ATOM   1737 C  C     . LYS A 1 245 ? -6.892  33.015 10.490  1.00 29.94  ? 231  LYS A C     1 
ATOM   1738 O  O     . LYS A 1 245 ? -7.360  32.139 11.226  1.00 28.77  ? 231  LYS A O     1 
ATOM   1739 C  CB    . LYS A 1 245 ? -7.147  35.405 11.217  1.00 29.66  ? 231  LYS A CB    1 
ATOM   1740 C  CG    . LYS A 1 245 ? -8.197  35.197 12.279  1.00 35.21  ? 231  LYS A CG    1 
ATOM   1741 C  CD    . LYS A 1 245 ? -9.273  36.268 12.243  1.00 35.47  ? 231  LYS A CD    1 
ATOM   1742 C  CE    . LYS A 1 245 ? -10.600 35.674 12.679  1.00 38.77  ? 231  LYS A CE    1 
ATOM   1743 N  NZ    . LYS A 1 245 ? -10.577 35.437 14.137  1.00 39.26  ? 231  LYS A NZ    1 
ATOM   1744 N  N     . TRP A 1 246 ? -6.945  32.933 9.161   1.00 27.73  ? 232  TRP A N     1 
ATOM   1745 C  CA    . TRP A 1 246 ? -7.532  31.774 8.494   1.00 26.65  ? 232  TRP A CA    1 
ATOM   1746 C  C     . TRP A 1 246 ? -6.858  30.494 8.963   1.00 27.23  ? 232  TRP A C     1 
ATOM   1747 O  O     . TRP A 1 246 ? -7.515  29.551 9.416   1.00 29.99  ? 232  TRP A O     1 
ATOM   1748 C  CB    . TRP A 1 246 ? -7.373  31.959 6.981   1.00 25.91  ? 232  TRP A CB    1 
ATOM   1749 C  CG    . TRP A 1 246 ? -7.934  30.914 6.067   1.00 25.26  ? 232  TRP A CG    1 
ATOM   1750 C  CD1   . TRP A 1 246 ? -8.345  29.647 6.382   1.00 26.63  ? 232  TRP A CD1   1 
ATOM   1751 C  CD2   . TRP A 1 246 ? -8.123  31.056 4.654   1.00 23.78  ? 232  TRP A CD2   1 
ATOM   1752 N  NE1   . TRP A 1 246 ? -8.803  29.007 5.244   1.00 23.71  ? 232  TRP A NE1   1 
ATOM   1753 C  CE2   . TRP A 1 246 ? -8.663  29.847 4.174   1.00 23.99  ? 232  TRP A CE2   1 
ATOM   1754 C  CE3   . TRP A 1 246 ? -7.885  32.094 3.746   1.00 23.32  ? 232  TRP A CE3   1 
ATOM   1755 C  CZ2   . TRP A 1 246 ? -8.961  29.645 2.826   1.00 23.36  ? 232  TRP A CZ2   1 
ATOM   1756 C  CZ3   . TRP A 1 246 ? -8.182  31.889 2.411   1.00 23.04  ? 232  TRP A CZ3   1 
ATOM   1757 C  CH2   . TRP A 1 246 ? -8.720  30.678 1.968   1.00 22.67  ? 232  TRP A CH2   1 
ATOM   1758 N  N     . VAL A 1 247 ? -5.530  30.462 8.902   1.00 28.38  ? 233  VAL A N     1 
ATOM   1759 C  CA    . VAL A 1 247 ? -4.817  29.236 9.207   1.00 29.16  ? 233  VAL A CA    1 
ATOM   1760 C  C     . VAL A 1 247 ? -4.704  28.999 10.715  1.00 31.67  ? 233  VAL A C     1 
ATOM   1761 O  O     . VAL A 1 247 ? -4.499  27.855 11.148  1.00 30.85  ? 233  VAL A O     1 
ATOM   1762 C  CB    . VAL A 1 247 ? -3.487  29.298 8.425   1.00 30.95  ? 233  VAL A CB    1 
ATOM   1763 C  CG1   . VAL A 1 247 ? -2.409  30.155 9.124   1.00 29.16  ? 233  VAL A CG1   1 
ATOM   1764 C  CG2   . VAL A 1 247 ? -3.023  27.923 8.070   1.00 33.21  ? 233  VAL A CG2   1 
ATOM   1765 N  N     . LYS A 1 248 ? -4.862  30.043 11.532  1.00 30.43  ? 234  LYS A N     1 
ATOM   1766 C  CA    . LYS A 1 248 ? -4.953  29.851 12.976  1.00 31.05  ? 234  LYS A CA    1 
ATOM   1767 C  C     . LYS A 1 248 ? -6.306  29.264 13.363  1.00 31.07  ? 234  LYS A C     1 
ATOM   1768 O  O     . LYS A 1 248 ? -6.382  28.308 14.142  1.00 31.49  ? 234  LYS A O     1 
ATOM   1769 C  CB    . LYS A 1 248 ? -4.702  31.184 13.683  1.00 32.52  ? 234  LYS A CB    1 
ATOM   1770 C  CG    . LYS A 1 248 ? -4.797  31.140 15.189  1.00 35.66  ? 234  LYS A CG    1 
ATOM   1771 C  CD    . LYS A 1 248 ? -5.707  32.241 15.702  1.00 39.01  ? 234  LYS A CD    1 
ATOM   1772 C  CE    . LYS A 1 248 ? -6.261  31.875 17.064  1.00 40.94  ? 234  LYS A CE    1 
ATOM   1773 N  NZ    . LYS A 1 248 ? -5.196  32.183 18.060  1.00 40.40  ? 234  LYS A NZ    1 
ATOM   1774 N  N     . ASP A 1 249 ? -7.391  29.812 12.807  1.00 31.32  ? 235  ASP A N     1 
ATOM   1775 C  CA    . ASP A 1 249 ? -8.724  29.299 13.121  1.00 31.75  ? 235  ASP A CA    1 
ATOM   1776 C  C     . ASP A 1 249 ? -9.001  27.960 12.453  1.00 30.87  ? 235  ASP A C     1 
ATOM   1777 O  O     . ASP A 1 249 ? -9.782  27.160 12.980  1.00 29.98  ? 235  ASP A O     1 
ATOM   1778 C  CB    . ASP A 1 249 ? -9.784  30.322 12.729  1.00 31.49  ? 235  ASP A CB    1 
ATOM   1779 C  CG    . ASP A 1 249 ? -9.646  31.608 13.502  1.00 33.22  ? 235  ASP A CG    1 
ATOM   1780 O  OD1   . ASP A 1 249 ? -8.854  31.623 14.465  1.00 35.65  ? 235  ASP A OD1   1 
ATOM   1781 O  OD2   . ASP A 1 249 ? -10.321 32.600 13.159  1.00 35.84  ? 235  ASP A OD2   1 
ATOM   1782 N  N     . VAL A 1 250 ? -8.391  27.700 11.303  1.00 28.30  ? 236  VAL A N     1 
ATOM   1783 C  CA    . VAL A 1 250 ? -8.620  26.461 10.560  1.00 29.89  ? 236  VAL A CA    1 
ATOM   1784 C  C     . VAL A 1 250 ? -7.280  25.803 10.243  1.00 30.39  ? 236  VAL A C     1 
ATOM   1785 O  O     . VAL A 1 250 ? -6.749  25.995 9.139   1.00 29.16  ? 236  VAL A O     1 
ATOM   1786 C  CB    . VAL A 1 250 ? -9.422  26.721 9.272   1.00 28.31  ? 236  VAL A CB    1 
ATOM   1787 C  CG1   . VAL A 1 250 ? -9.886  25.415 8.664   1.00 29.98  ? 236  VAL A CG1   1 
ATOM   1788 C  CG2   . VAL A 1 250 ? -10.629 27.604 9.562   1.00 29.97  ? 236  VAL A CG2   1 
ATOM   1789 N  N     . PRO A 1 251 ? -6.700  25.029 11.160  1.00 31.94  ? 237  PRO A N     1 
ATOM   1790 C  CA    . PRO A 1 251 ? -5.404  24.399 10.877  1.00 32.37  ? 237  PRO A CA    1 
ATOM   1791 C  C     . PRO A 1 251 ? -5.478  23.521 9.634   1.00 32.01  ? 237  PRO A C     1 
ATOM   1792 O  O     . PRO A 1 251 ? -6.408  22.730 9.467   1.00 32.96  ? 237  PRO A O     1 
ATOM   1793 C  CB    . PRO A 1 251 ? -5.137  23.567 12.140  1.00 33.20  ? 237  PRO A CB    1 
ATOM   1794 C  CG    . PRO A 1 251 ? -5.949  24.227 13.213  1.00 32.51  ? 237  PRO A CG    1 
ATOM   1795 C  CD    . PRO A 1 251 ? -7.203  24.659 12.498  1.00 34.19  ? 237  PRO A CD    1 
ATOM   1796 N  N     . MET A 1 252 ? -4.489  23.673 8.756   1.00 32.32  ? 238  MET A N     1 
ATOM   1797 C  CA    . MET A 1 252 ? -4.372  22.868 7.544   1.00 31.14  ? 238  MET A CA    1 
ATOM   1798 C  C     . MET A 1 252 ? -3.029  23.185 6.903   1.00 30.92  ? 238  MET A C     1 
ATOM   1799 O  O     . MET A 1 252 ? -2.367  24.165 7.257   1.00 30.27  ? 238  MET A O     1 
ATOM   1800 C  CB    . MET A 1 252 ? -5.531  23.125 6.578   1.00 32.75  ? 238  MET A CB    1 
ATOM   1801 C  CG    . MET A 1 252 ? -5.761  24.574 6.342   1.00 31.79  ? 238  MET A CG    1 
ATOM   1802 S  SD    . MET A 1 252 ? -6.747  24.986 4.895   1.00 38.75  ? 238  MET A SD    1 
ATOM   1803 C  CE    . MET A 1 252 ? -7.235  26.542 5.525   1.00 30.90  ? 238  MET A CE    1 
ATOM   1804 N  N     . ALA A 1 253 ? -2.630  22.333 5.961   1.00 31.20  ? 239  ALA A N     1 
ATOM   1805 C  CA    . ALA A 1 253 ? -1.394  22.566 5.230   1.00 30.14  ? 239  ALA A CA    1 
ATOM   1806 C  C     . ALA A 1 253 ? -1.464  23.887 4.486   1.00 29.57  ? 239  ALA A C     1 
ATOM   1807 O  O     . ALA A 1 253 ? -2.455  24.185 3.804   1.00 28.28  ? 239  ALA A O     1 
ATOM   1808 C  CB    . ALA A 1 253 ? -1.114  21.418 4.255   1.00 29.94  ? 239  ALA A CB    1 
ATOM   1809 N  N     . HIS A 1 254 ? -0.404  24.679 4.617   1.00 27.54  ? 240  HIS A N     1 
ATOM   1810 C  CA    . HIS A 1 254 ? -0.348  25.954 3.926   1.00 28.68  ? 240  HIS A CA    1 
ATOM   1811 C  C     . HIS A 1 254 ? 1.098   26.286 3.579   1.00 28.67  ? 240  HIS A C     1 
ATOM   1812 O  O     . HIS A 1 254 ? 2.045   25.772 4.182   1.00 29.21  ? 240  HIS A O     1 
ATOM   1813 C  CB    . HIS A 1 254 ? -0.991  27.084 4.744   1.00 26.10  ? 240  HIS A CB    1 
ATOM   1814 C  CG    . HIS A 1 254 ? -0.379  27.284 6.095   1.00 29.16  ? 240  HIS A CG    1 
ATOM   1815 N  ND1   . HIS A 1 254 ? -0.515  26.369 7.121   1.00 28.51  ? 240  HIS A ND1   1 
ATOM   1816 C  CD2   . HIS A 1 254 ? 0.373   28.296 6.590   1.00 27.58  ? 240  HIS A CD2   1 
ATOM   1817 C  CE1   . HIS A 1 254 ? 0.123   26.814 8.189   1.00 31.11  ? 240  HIS A CE1   1 
ATOM   1818 N  NE2   . HIS A 1 254 ? 0.673   27.979 7.892   1.00 30.77  ? 240  HIS A NE2   1 
ATOM   1819 N  N     . ALA A 1 255 ? 1.245   27.158 2.586   1.00 25.81  ? 241  ALA A N     1 
ATOM   1820 C  CA    . ALA A 1 255 ? 2.543   27.596 2.101   1.00 25.52  ? 241  ALA A CA    1 
ATOM   1821 C  C     . ALA A 1 255 ? 2.353   28.916 1.377   1.00 22.96  ? 241  ALA A C     1 
ATOM   1822 O  O     . ALA A 1 255 ? 1.230   29.342 1.108   1.00 24.64  ? 241  ALA A O     1 
ATOM   1823 C  CB    . ALA A 1 255 ? 3.177   26.564 1.160   1.00 25.52  ? 241  ALA A CB    1 
ATOM   1824 N  N     . THR A 1 256 ? 3.466   29.565 1.073   1.00 22.74  ? 242  THR A N     1 
ATOM   1825 C  CA    . THR A 1 256 ? 3.501   30.604 0.054   1.00 20.71  ? 242  THR A CA    1 
ATOM   1826 C  C     . THR A 1 256 ? 4.519   30.204 -1.004  1.00 22.30  ? 242  THR A C     1 
ATOM   1827 O  O     . THR A 1 256 ? 5.172   29.162 -0.903  1.00 21.94  ? 242  THR A O     1 
ATOM   1828 C  CB    . THR A 1 256 ? 3.859   31.978 0.627   1.00 21.24  ? 242  THR A CB    1 
ATOM   1829 O  OG1   . THR A 1 256 ? 5.283   32.152 0.612   1.00 22.89  ? 242  THR A OG1   1 
ATOM   1830 C  CG2   . THR A 1 256 ? 3.318   32.147 2.047   1.00 22.08  ? 242  THR A CG2   1 
ATOM   1831 N  N     . MET A 1 257 ? 4.644   31.047 -2.025  1.00 22.43  ? 243  MET A N     1 
ATOM   1832 C  CA    . MET A 1 257 ? 5.745   30.987 -2.973  1.00 19.64  ? 243  MET A CA    1 
ATOM   1833 C  C     . MET A 1 257 ? 6.745   32.083 -2.602  1.00 21.59  ? 243  MET A C     1 
ATOM   1834 O  O     . MET A 1 257 ? 6.558   32.800 -1.617  1.00 20.65  ? 243  MET A O     1 
ATOM   1835 C  CB    . MET A 1 257 ? 5.216   31.121 -4.407  1.00 20.20  ? 243  MET A CB    1 
ATOM   1836 C  CG    . MET A 1 257 ? 4.640   29.800 -4.937  1.00 20.54  ? 243  MET A CG    1 
ATOM   1837 S  SD    . MET A 1 257 ? 3.874   29.855 -6.586  1.00 23.73  ? 243  MET A SD    1 
ATOM   1838 C  CE    . MET A 1 257 ? 2.568   31.070 -6.368  1.00 22.34  ? 243  MET A CE    1 
ATOM   1839 N  N     . LEU A 1 258 ? 7.818   32.216 -3.392  1.00 21.80  ? 244  LEU A N     1 
ATOM   1840 C  CA    . LEU A 1 258 ? 8.879   33.156 -3.034  1.00 22.52  ? 244  LEU A CA    1 
ATOM   1841 C  C     . LEU A 1 258 ? 8.344   34.570 -2.843  1.00 22.11  ? 244  LEU A C     1 
ATOM   1842 O  O     . LEU A 1 258 ? 8.741   35.258 -1.893  1.00 20.94  ? 244  LEU A O     1 
ATOM   1843 C  CB    . LEU A 1 258 ? 9.979   33.153 -4.097  1.00 21.50  ? 244  LEU A CB    1 
ATOM   1844 C  CG    . LEU A 1 258 ? 11.192  34.089 -3.919  1.00 24.55  ? 244  LEU A CG    1 
ATOM   1845 C  CD1   . LEU A 1 258 ? 11.835  33.988 -2.529  1.00 24.32  ? 244  LEU A CD1   1 
ATOM   1846 C  CD2   . LEU A 1 258 ? 12.250  33.859 -5.016  1.00 27.22  ? 244  LEU A CD2   1 
ATOM   1847 N  N     . MET A 1 259 ? 7.449   35.024 -3.736  1.00 20.99  ? 245  MET A N     1 
ATOM   1848 C  CA    . MET A 1 259 ? 7.013   36.424 -3.726  1.00 20.49  ? 245  MET A CA    1 
ATOM   1849 C  C     . MET A 1 259 ? 6.233   36.771 -2.470  1.00 21.81  ? 245  MET A C     1 
ATOM   1850 O  O     . MET A 1 259 ? 6.271   37.919 -2.008  1.00 21.40  ? 245  MET A O     1 
ATOM   1851 C  CB    . MET A 1 259 ? 6.131   36.761 -4.933  1.00 21.39  ? 245  MET A CB    1 
ATOM   1852 C  CG    . MET A 1 259 ? 6.875   37.382 -6.067  1.00 20.28  ? 245  MET A CG    1 
ATOM   1853 S  SD    . MET A 1 259 ? 6.043   37.384 -7.643  1.00 24.08  ? 245  MET A SD    1 
ATOM   1854 C  CE    . MET A 1 259 ? 5.342   39.026 -7.633  1.00 17.59  ? 245  MET A CE    1 
ATOM   1855 N  N     . GLY A 1 260 ? 5.440   35.833 -1.968  1.00 20.61  ? 246  GLY A N     1 
ATOM   1856 C  CA    . GLY A 1 260 ? 4.573   36.081 -0.837  1.00 21.99  ? 246  GLY A CA    1 
ATOM   1857 C  C     . GLY A 1 260 ? 5.163   35.690 0.493   1.00 21.81  ? 246  GLY A C     1 
ATOM   1858 O  O     . GLY A 1 260 ? 4.469   35.770 1.514   1.00 22.66  ? 246  GLY A O     1 
ATOM   1859 N  N     . LYS A 1 261 ? 6.420   35.267 0.517   1.00 22.07  ? 247  LYS A N     1 
ATOM   1860 C  CA    . LYS A 1 261 ? 7.070   34.926 1.767   1.00 21.85  ? 247  LYS A CA    1 
ATOM   1861 C  C     . LYS A 1 261 ? 6.902   36.066 2.762   1.00 21.94  ? 247  LYS A C     1 
ATOM   1862 O  O     . LYS A 1 261 ? 7.017   37.243 2.407   1.00 20.64  ? 247  LYS A O     1 
ATOM   1863 C  CB    . LYS A 1 261 ? 8.547   34.650 1.488   1.00 24.03  ? 247  LYS A CB    1 
ATOM   1864 C  CG    . LYS A 1 261 ? 9.174   33.534 2.269   1.00 24.88  ? 247  LYS A CG    1 
ATOM   1865 C  CD    . LYS A 1 261 ? 10.658  33.438 1.923   1.00 24.99  ? 247  LYS A CD    1 
ATOM   1866 C  CE    . LYS A 1 261 ? 11.416  32.477 2.828   1.00 23.91  ? 247  LYS A CE    1 
ATOM   1867 N  NZ    . LYS A 1 261 ? 10.574  31.452 3.472   1.00 25.94  ? 247  LYS A NZ    1 
ATOM   1868 N  N     . GLY A 1 262 ? 6.590   35.708 4.010   1.00 22.55  ? 248  GLY A N     1 
ATOM   1869 C  CA    . GLY A 1 262 ? 6.243   36.667 5.036   1.00 23.13  ? 248  GLY A CA    1 
ATOM   1870 C  C     . GLY A 1 262 ? 4.761   36.754 5.353   1.00 24.82  ? 248  GLY A C     1 
ATOM   1871 O  O     . GLY A 1 262 ? 4.403   37.298 6.405   1.00 22.77  ? 248  GLY A O     1 
ATOM   1872 N  N     . ILE A 1 263 ? 3.891   36.196 4.508   1.00 22.25  ? 249  ILE A N     1 
ATOM   1873 C  CA    . ILE A 1 263 ? 2.471   36.146 4.854   1.00 23.35  ? 249  ILE A CA    1 
ATOM   1874 C  C     . ILE A 1 263 ? 2.266   35.346 6.137   1.00 25.74  ? 249  ILE A C     1 
ATOM   1875 O  O     . ILE A 1 263 ? 1.494   35.746 7.022   1.00 24.75  ? 249  ILE A O     1 
ATOM   1876 C  CB    . ILE A 1 263 ? 1.653   35.551 3.693   1.00 22.86  ? 249  ILE A CB    1 
ATOM   1877 C  CG1   . ILE A 1 263 ? 1.462   36.587 2.590   1.00 20.68  ? 249  ILE A CG1   1 
ATOM   1878 C  CG2   . ILE A 1 263 ? 0.306   35.013 4.206   1.00 21.95  ? 249  ILE A CG2   1 
ATOM   1879 C  CD1   . ILE A 1 263 ? 1.255   35.978 1.178   1.00 22.40  ? 249  ILE A CD1   1 
ATOM   1880 N  N     . PHE A 1 264 ? 2.971   34.227 6.275   1.00 22.90  ? 250  PHE A N     1 
ATOM   1881 C  CA    . PHE A 1 264 ? 2.762   33.311 7.387   1.00 25.68  ? 250  PHE A CA    1 
ATOM   1882 C  C     . PHE A 1 264 ? 3.952   33.288 8.329   1.00 25.86  ? 250  PHE A C     1 
ATOM   1883 O  O     . PHE A 1 264 ? 5.104   33.447 7.914   1.00 25.17  ? 250  PHE A O     1 
ATOM   1884 C  CB    . PHE A 1 264 ? 2.517   31.883 6.893   1.00 24.99  ? 250  PHE A CB    1 
ATOM   1885 C  CG    . PHE A 1 264 ? 1.248   31.720 6.116   1.00 25.12  ? 250  PHE A CG    1 
ATOM   1886 C  CD1   . PHE A 1 264 ? 0.023   32.038 6.692   1.00 23.73  ? 250  PHE A CD1   1 
ATOM   1887 C  CD2   . PHE A 1 264 ? 1.279   31.289 4.795   1.00 24.13  ? 250  PHE A CD2   1 
ATOM   1888 C  CE1   . PHE A 1 264 ? -1.159  31.889 5.966   1.00 25.85  ? 250  PHE A CE1   1 
ATOM   1889 C  CE2   . PHE A 1 264 ? 0.109   31.138 4.064   1.00 24.39  ? 250  PHE A CE2   1 
ATOM   1890 C  CZ    . PHE A 1 264 ? -1.115  31.434 4.646   1.00 23.15  ? 250  PHE A CZ    1 
ATOM   1891 N  N     . ASP A 1 265 ? 3.652   33.045 9.605   1.00 27.56  ? 251  ASP A N     1 
ATOM   1892 C  CA    . ASP A 1 265 ? 4.660   32.609 10.558  1.00 28.51  ? 251  ASP A CA    1 
ATOM   1893 C  C     . ASP A 1 265 ? 5.031   31.185 10.174  1.00 30.21  ? 251  ASP A C     1 
ATOM   1894 O  O     . ASP A 1 265 ? 4.207   30.272 10.286  1.00 29.43  ? 251  ASP A O     1 
ATOM   1895 C  CB    . ASP A 1 265 ? 4.094   32.667 11.972  1.00 29.64  ? 251  ASP A CB    1 
ATOM   1896 C  CG    . ASP A 1 265 ? 5.092   32.256 13.033  1.00 32.51  ? 251  ASP A CG    1 
ATOM   1897 O  OD1   . ASP A 1 265 ? 6.066   31.523 12.744  1.00 30.59  ? 251  ASP A OD1   1 
ATOM   1898 O  OD2   . ASP A 1 265 ? 4.859   32.639 14.198  1.00 36.70  ? 251  ASP A OD2   1 
ATOM   1899 N  N     . GLU A 1 266 ? 6.269   30.982 9.740   1.00 28.88  ? 252  GLU A N     1 
ATOM   1900 C  CA    . GLU A 1 266 ? 6.647   29.698 9.163   1.00 29.84  ? 252  GLU A CA    1 
ATOM   1901 C  C     . GLU A 1 266 ? 7.054   28.654 10.201  1.00 34.68  ? 252  GLU A C     1 
ATOM   1902 O  O     . GLU A 1 266 ? 7.472   27.558 9.816   1.00 36.39  ? 252  GLU A O     1 
ATOM   1903 C  CB    . GLU A 1 266 ? 7.768   29.921 8.144   1.00 27.15  ? 252  GLU A CB    1 
ATOM   1904 C  CG    . GLU A 1 266 ? 7.418   30.988 7.096   1.00 27.16  ? 252  GLU A CG    1 
ATOM   1905 C  CD    . GLU A 1 266 ? 8.351   30.990 5.879   1.00 27.20  ? 252  GLU A CD    1 
ATOM   1906 O  OE1   . GLU A 1 266 ? 9.519   30.574 6.028   1.00 28.36  ? 252  GLU A OE1   1 
ATOM   1907 O  OE2   . GLU A 1 266 ? 7.921   31.414 4.772   1.00 26.06  ? 252  GLU A OE2   1 
ATOM   1908 N  N     . ARG A 1 267 ? 6.941   28.959 11.497  1.00 36.13  ? 253  ARG A N     1 
ATOM   1909 C  CA    . ARG A 1 267 ? 7.070   27.950 12.546  1.00 37.46  ? 253  ARG A CA    1 
ATOM   1910 C  C     . ARG A 1 267 ? 5.736   27.307 12.916  1.00 38.38  ? 253  ARG A C     1 
ATOM   1911 O  O     . ARG A 1 267 ? 5.727   26.250 13.555  1.00 38.14  ? 253  ARG A O     1 
ATOM   1912 C  CB    . ARG A 1 267 ? 7.711   28.565 13.796  1.00 36.17  ? 253  ARG A CB    1 
ATOM   1913 C  CG    . ARG A 1 267 ? 9.011   29.330 13.518  1.00 35.77  ? 253  ARG A CG    1 
ATOM   1914 C  CD    . ARG A 1 267 ? 9.326   30.389 14.586  1.00 35.14  ? 253  ARG A CD    1 
ATOM   1915 N  NE    . ARG A 1 267 ? 8.196   31.258 14.890  1.00 33.62  ? 253  ARG A NE    1 
ATOM   1916 C  CZ    . ARG A 1 267 ? 8.235   32.263 15.758  1.00 36.16  ? 253  ARG A CZ    1 
ATOM   1917 N  NH1   . ARG A 1 267 ? 9.328   32.535 16.461  1.00 34.89  ? 253  ARG A NH1   1 
ATOM   1918 N  NH2   . ARG A 1 267 ? 7.154   33.019 15.921  1.00 35.65  ? 253  ARG A NH2   1 
ATOM   1919 N  N     . HIS A 1 268 ? 4.621   27.909 12.509  1.00 37.61  ? 254  HIS A N     1 
ATOM   1920 C  CA    . HIS A 1 268 ? 3.288   27.483 12.922  1.00 40.65  ? 254  HIS A CA    1 
ATOM   1921 C  C     . HIS A 1 268 ? 2.943   26.112 12.327  1.00 39.65  ? 254  HIS A C     1 
ATOM   1922 O  O     . HIS A 1 268 ? 3.458   25.718 11.276  1.00 39.11  ? 254  HIS A O     1 
ATOM   1923 C  CB    . HIS A 1 268 ? 2.287   28.570 12.509  1.00 40.67  ? 254  HIS A CB    1 
ATOM   1924 C  CG    . HIS A 1 268 ? 0.933   28.455 13.137  1.00 48.31  ? 254  HIS A CG    1 
ATOM   1925 N  ND1   . HIS A 1 268 ? 0.046   27.444 12.836  1.00 52.72  ? 254  HIS A ND1   1 
ATOM   1926 C  CD2   . HIS A 1 268 ? 0.323   29.224 14.070  1.00 58.80  ? 254  HIS A CD2   1 
ATOM   1927 C  CE1   . HIS A 1 268 ? -1.059  27.604 13.544  1.00 51.38  ? 254  HIS A CE1   1 
ATOM   1928 N  NE2   . HIS A 1 268 ? -0.915  28.675 14.303  1.00 71.76  ? 254  HIS A NE2   1 
ATOM   1929 N  N     . VAL A 1 269 ? 2.066   25.375 13.019  1.00 40.88  ? 255  VAL A N     1 
ATOM   1930 C  CA    . VAL A 1 269 ? 1.683   24.044 12.554  1.00 38.88  ? 255  VAL A CA    1 
ATOM   1931 C  C     . VAL A 1 269 ? 1.045   24.144 11.176  1.00 35.78  ? 255  VAL A C     1 
ATOM   1932 O  O     . VAL A 1 269 ? 0.282   25.076 10.886  1.00 33.43  ? 255  VAL A O     1 
ATOM   1933 C  CB    . VAL A 1 269 ? 0.726   23.365 13.551  1.00 42.09  ? 255  VAL A CB    1 
ATOM   1934 C  CG1   . VAL A 1 269 ? -0.403  24.309 13.950  1.00 44.29  ? 255  VAL A CG1   1 
ATOM   1935 C  CG2   . VAL A 1 269 ? 0.154   22.070 12.981  1.00 39.26  ? 255  VAL A CG2   1 
ATOM   1936 N  N     . GLY A 1 270 ? 1.358   23.170 10.317  1.00 34.54  ? 256  GLY A N     1 
ATOM   1937 C  CA    . GLY A 1 270 ? 0.859   23.131 8.962   1.00 34.73  ? 256  GLY A CA    1 
ATOM   1938 C  C     . GLY A 1 270 ? 1.748   23.769 7.916   1.00 33.29  ? 256  GLY A C     1 
ATOM   1939 O  O     . GLY A 1 270 ? 1.448   23.656 6.716   1.00 30.18  ? 256  GLY A O     1 
ATOM   1940 N  N     . PHE A 1 271 ? 2.811   24.460 8.315   1.00 32.46  ? 257  PHE A N     1 
ATOM   1941 C  CA    . PHE A 1 271 ? 3.743   25.037 7.358   1.00 30.70  ? 257  PHE A CA    1 
ATOM   1942 C  C     . PHE A 1 271 ? 4.975   24.153 7.261   1.00 31.09  ? 257  PHE A C     1 
ATOM   1943 O  O     . PHE A 1 271 ? 5.578   23.806 8.283   1.00 34.36  ? 257  PHE A O     1 
ATOM   1944 C  CB    . PHE A 1 271 ? 4.139   26.462 7.739   1.00 32.58  ? 257  PHE A CB    1 
ATOM   1945 C  CG    . PHE A 1 271 ? 4.993   27.134 6.705   1.00 29.03  ? 257  PHE A CG    1 
ATOM   1946 C  CD1   . PHE A 1 271 ? 4.411   27.826 5.659   1.00 28.09  ? 257  PHE A CD1   1 
ATOM   1947 C  CD2   . PHE A 1 271 ? 6.371   27.047 6.756   1.00 30.35  ? 257  PHE A CD2   1 
ATOM   1948 C  CE1   . PHE A 1 271 ? 5.181   28.426 4.694   1.00 26.43  ? 257  PHE A CE1   1 
ATOM   1949 C  CE2   . PHE A 1 271 ? 7.143   27.649 5.797   1.00 28.79  ? 257  PHE A CE2   1 
ATOM   1950 C  CZ    . PHE A 1 271 ? 6.547   28.345 4.767   1.00 27.82  ? 257  PHE A CZ    1 
ATOM   1951 N  N     . TYR A 1 272 ? 5.339   23.786 6.032   1.00 30.28  ? 258  TYR A N     1 
ATOM   1952 C  CA    . TYR A 1 272 ? 6.433   22.859 5.785   1.00 32.98  ? 258  TYR A CA    1 
ATOM   1953 C  C     . TYR A 1 272 ? 7.578   23.448 4.967   1.00 31.88  ? 258  TYR A C     1 
ATOM   1954 O  O     . TYR A 1 272 ? 8.592   22.769 4.781   1.00 31.73  ? 258  TYR A O     1 
ATOM   1955 C  CB    . TYR A 1 272 ? 5.888   21.601 5.089   1.00 31.86  ? 258  TYR A CB    1 
ATOM   1956 C  CG    . TYR A 1 272 ? 4.787   20.947 5.891   1.00 32.13  ? 258  TYR A CG    1 
ATOM   1957 C  CD1   . TYR A 1 272 ? 5.089   20.116 6.967   1.00 36.00  ? 258  TYR A CD1   1 
ATOM   1958 C  CD2   . TYR A 1 272 ? 3.448   21.167 5.586   1.00 32.31  ? 258  TYR A CD2   1 
ATOM   1959 C  CE1   . TYR A 1 272 ? 4.096   19.520 7.714   1.00 36.56  ? 258  TYR A CE1   1 
ATOM   1960 C  CE2   . TYR A 1 272 ? 2.442   20.576 6.331   1.00 33.62  ? 258  TYR A CE2   1 
ATOM   1961 C  CZ    . TYR A 1 272 ? 2.775   19.745 7.393   1.00 35.75  ? 258  TYR A CZ    1 
ATOM   1962 O  OH    . TYR A 1 272 ? 1.785   19.150 8.150   1.00 39.71  ? 258  TYR A OH    1 
ATOM   1963 N  N     . GLY A 1 273 ? 7.457   24.683 4.491   1.00 30.24  ? 259  GLY A N     1 
ATOM   1964 C  CA    . GLY A 1 273 ? 8.466   25.294 3.643   1.00 29.70  ? 259  GLY A CA    1 
ATOM   1965 C  C     . GLY A 1 273 ? 7.844   26.052 2.484   1.00 28.36  ? 259  GLY A C     1 
ATOM   1966 O  O     . GLY A 1 273 ? 6.638   25.932 2.232   1.00 26.78  ? 259  GLY A O     1 
ATOM   1967 N  N     . THR A 1 274 ? 8.651   26.833 1.767   1.00 26.85  ? 260  THR A N     1 
ATOM   1968 C  CA    . THR A 1 274 ? 8.142   27.622 0.656   1.00 26.42  ? 260  THR A CA    1 
ATOM   1969 C  C     . THR A 1 274 ? 7.979   26.746 -0.582  1.00 25.69  ? 260  THR A C     1 
ATOM   1970 O  O     . THR A 1 274 ? 8.830   25.906 -0.881  1.00 26.18  ? 260  THR A O     1 
ATOM   1971 C  CB    . THR A 1 274 ? 9.069   28.806 0.370   1.00 26.40  ? 260  THR A CB    1 
ATOM   1972 O  OG1   . THR A 1 274 ? 9.162   29.626 1.543   1.00 25.16  ? 260  THR A OG1   1 
ATOM   1973 C  CG2   . THR A 1 274 ? 8.517   29.661 -0.790  1.00 24.23  ? 260  THR A CG2   1 
ATOM   1974 N  N     . TYR A 1 275 ? 6.849   26.912 -1.270  1.00 25.27  ? 261  TYR A N     1 
ATOM   1975 C  CA    . TYR A 1 275 ? 6.560   26.148 -2.481  1.00 25.85  ? 261  TYR A CA    1 
ATOM   1976 C  C     . TYR A 1 275 ? 7.247   26.781 -3.686  1.00 26.22  ? 261  TYR A C     1 
ATOM   1977 O  O     . TYR A 1 275 ? 7.123   27.990 -3.919  1.00 25.88  ? 261  TYR A O     1 
ATOM   1978 C  CB    . TYR A 1 275 ? 5.048   26.086 -2.710  1.00 23.48  ? 261  TYR A CB    1 
ATOM   1979 C  CG    . TYR A 1 275 ? 4.609   25.313 -3.945  1.00 24.74  ? 261  TYR A CG    1 
ATOM   1980 C  CD1   . TYR A 1 275 ? 4.886   23.959 -4.081  1.00 24.29  ? 261  TYR A CD1   1 
ATOM   1981 C  CD2   . TYR A 1 275 ? 3.899   25.940 -4.958  1.00 23.10  ? 261  TYR A CD2   1 
ATOM   1982 C  CE1   . TYR A 1 275 ? 4.479   23.262 -5.195  1.00 25.12  ? 261  TYR A CE1   1 
ATOM   1983 C  CE2   . TYR A 1 275 ? 3.481   25.248 -6.082  1.00 24.24  ? 261  TYR A CE2   1 
ATOM   1984 C  CZ    . TYR A 1 275 ? 3.763   23.912 -6.192  1.00 25.93  ? 261  TYR A CZ    1 
ATOM   1985 O  OH    . TYR A 1 275 ? 3.337   23.226 -7.305  1.00 27.15  ? 261  TYR A OH    1 
ATOM   1986 N  N     . SER A 1 276 ? 8.001   25.979 -4.430  1.00 26.87  ? 262  SER A N     1 
ATOM   1987 C  CA    . SER A 1 276 ? 8.639   26.446 -5.661  1.00 27.65  ? 262  SER A CA    1 
ATOM   1988 C  C     . SER A 1 276 ? 8.628   25.357 -6.730  1.00 28.16  ? 262  SER A C     1 
ATOM   1989 O  O     . SER A 1 276 ? 9.650   25.059 -7.349  1.00 28.90  ? 262  SER A O     1 
ATOM   1990 C  CB    . SER A 1 276 ? 10.063  26.947 -5.410  1.00 31.35  ? 262  SER A CB    1 
ATOM   1991 O  OG    . SER A 1 276 ? 10.835  25.971 -4.752  1.00 33.28  ? 262  SER A OG    1 
ATOM   1992 N  N     . GLY A 1 277 ? 7.476   24.724 -6.938  1.00 27.69  ? 263  GLY A N     1 
ATOM   1993 C  CA    . GLY A 1 277 ? 7.376   23.735 -8.001  1.00 27.03  ? 263  GLY A CA    1 
ATOM   1994 C  C     . GLY A 1 277 ? 8.212   22.507 -7.701  1.00 29.52  ? 263  GLY A C     1 
ATOM   1995 O  O     . GLY A 1 277 ? 8.308   22.053 -6.550  1.00 29.36  ? 263  GLY A O     1 
ATOM   1996 N  N     . SER A 1 278 ? 8.854   21.967 -8.748  1.00 29.70  ? 264  SER A N     1 
ATOM   1997 C  CA    . SER A 1 278 ? 9.627   20.736 -8.581  1.00 31.58  ? 264  SER A CA    1 
ATOM   1998 C  C     . SER A 1 278 ? 10.837  20.920 -7.677  1.00 31.51  ? 264  SER A C     1 
ATOM   1999 O  O     . SER A 1 278 ? 11.396  19.925 -7.196  1.00 30.83  ? 264  SER A O     1 
ATOM   2000 C  CB    . SER A 1 278 ? 10.079  20.199 -9.942  1.00 30.68  ? 264  SER A CB    1 
ATOM   2001 O  OG    . SER A 1 278 ? 10.983  21.093 -10.574 1.00 32.21  ? 264  SER A OG    1 
ATOM   2002 N  N     . ALA A 1 279 ? 11.247  22.158 -7.425  1.00 30.47  ? 265  ALA A N     1 
ATOM   2003 C  CA    . ALA A 1 279 ? 12.373  22.418 -6.542  1.00 31.70  ? 265  ALA A CA    1 
ATOM   2004 C  C     . ALA A 1 279 ? 11.984  22.434 -5.071  1.00 33.71  ? 265  ALA A C     1 
ATOM   2005 O  O     . ALA A 1 279 ? 12.872  22.531 -4.211  1.00 36.23  ? 265  ALA A O     1 
ATOM   2006 C  CB    . ALA A 1 279 ? 13.011  23.751 -6.918  1.00 34.31  ? 265  ALA A CB    1 
ATOM   2007 N  N     . SER A 1 280 ? 10.691  22.327 -4.763  1.00 31.62  ? 266  SER A N     1 
ATOM   2008 C  CA    . SER A 1 280 ? 10.240  22.343 -3.380  1.00 31.36  ? 266  SER A CA    1 
ATOM   2009 C  C     . SER A 1 280 ? 10.829  21.155 -2.627  1.00 32.93  ? 266  SER A C     1 
ATOM   2010 O  O     . SER A 1 280 ? 11.104  20.102 -3.207  1.00 31.01  ? 266  SER A O     1 
ATOM   2011 C  CB    . SER A 1 280 ? 8.710   22.272 -3.314  1.00 30.34  ? 266  SER A CB    1 
ATOM   2012 O  OG    . SER A 1 280 ? 8.084   23.244 -4.147  1.00 28.36  ? 266  SER A OG    1 
ATOM   2013 N  N     . ALA A 1 281 ? 11.017  21.332 -1.321  1.00 33.05  ? 267  ALA A N     1 
ATOM   2014 C  CA    . ALA A 1 281 ? 11.258  20.198 -0.438  1.00 32.96  ? 267  ALA A CA    1 
ATOM   2015 C  C     . ALA A 1 281 ? 10.128  19.176 -0.549  1.00 32.75  ? 267  ALA A C     1 
ATOM   2016 O  O     . ALA A 1 281 ? 8.971   19.519 -0.808  1.00 32.78  ? 267  ALA A O     1 
ATOM   2017 C  CB    . ALA A 1 281 ? 11.392  20.671 1.009   1.00 34.40  ? 267  ALA A CB    1 
ATOM   2018 N  N     . GLY A 1 282 ? 10.480  17.901 -0.355  1.00 33.17  ? 268  GLY A N     1 
ATOM   2019 C  CA    . GLY A 1 282 ? 9.517   16.826 -0.543  1.00 32.94  ? 268  GLY A CA    1 
ATOM   2020 C  C     . GLY A 1 282 ? 8.295   16.938 0.349   1.00 32.96  ? 268  GLY A C     1 
ATOM   2021 O  O     . GLY A 1 282 ? 7.188   16.568 -0.058  1.00 34.02  ? 268  GLY A O     1 
ATOM   2022 N  N     . ALA A 1 283 ? 8.475   17.429 1.577   1.00 34.33  ? 269  ALA A N     1 
ATOM   2023 C  CA    . ALA A 1 283 ? 7.334   17.626 2.465   1.00 33.41  ? 269  ALA A CA    1 
ATOM   2024 C  C     . ALA A 1 283 ? 6.387   18.682 1.916   1.00 32.82  ? 269  ALA A C     1 
ATOM   2025 O  O     . ALA A 1 283 ? 5.165   18.573 2.071   1.00 32.83  ? 269  ALA A O     1 
ATOM   2026 C  CB    . ALA A 1 283 ? 7.816   18.022 3.859   1.00 33.58  ? 269  ALA A CB    1 
ATOM   2027 N  N     . VAL A 1 284 ? 6.935   19.716 1.279   1.00 33.40  ? 270  VAL A N     1 
ATOM   2028 C  CA    . VAL A 1 284 ? 6.094   20.753 0.691   1.00 32.32  ? 270  VAL A CA    1 
ATOM   2029 C  C     . VAL A 1 284 ? 5.363   20.215 -0.527  1.00 30.63  ? 270  VAL A C     1 
ATOM   2030 O  O     . VAL A 1 284 ? 4.161   20.442 -0.696  1.00 30.34  ? 270  VAL A O     1 
ATOM   2031 C  CB    . VAL A 1 284 ? 6.939   21.988 0.344   1.00 30.00  ? 270  VAL A CB    1 
ATOM   2032 C  CG1   . VAL A 1 284 ? 6.100   23.017 -0.394  1.00 28.70  ? 270  VAL A CG1   1 
ATOM   2033 C  CG2   . VAL A 1 284 ? 7.541   22.563 1.608   1.00 31.59  ? 270  VAL A CG2   1 
ATOM   2034 N  N     . LYS A 1 285 ? 6.076   19.492 -1.395  1.00 31.93  ? 271  LYS A N     1 
ATOM   2035 C  CA    . LYS A 1 285 ? 5.427   18.920 -2.569  1.00 32.40  ? 271  LYS A CA    1 
ATOM   2036 C  C     . LYS A 1 285 ? 4.251   18.044 -2.160  1.00 32.72  ? 271  LYS A C     1 
ATOM   2037 O  O     . LYS A 1 285 ? 3.167   18.134 -2.747  1.00 30.55  ? 271  LYS A O     1 
ATOM   2038 C  CB    . LYS A 1 285 ? 6.437   18.134 -3.404  1.00 32.20  ? 271  LYS A CB    1 
ATOM   2039 C  CG    . LYS A 1 285 ? 7.278   19.035 -4.309  1.00 36.12  ? 271  LYS A CG    1 
ATOM   2040 C  CD    . LYS A 1 285 ? 7.815   18.320 -5.547  1.00 35.19  ? 271  LYS A CD    1 
ATOM   2041 C  CE    . LYS A 1 285 ? 9.282   17.975 -5.403  1.00 34.46  ? 271  LYS A CE    1 
ATOM   2042 N  NZ    . LYS A 1 285 ? 9.878   17.604 -6.720  1.00 33.07  ? 271  LYS A NZ    1 
ATOM   2043 N  N     . GLU A 1 286 ? 4.442   17.203 -1.142  1.00 33.37  ? 272  GLU A N     1 
ATOM   2044 C  CA    . GLU A 1 286 ? 3.360   16.346 -0.687  1.00 34.36  ? 272  GLU A CA    1 
ATOM   2045 C  C     . GLU A 1 286 ? 2.240   17.167 -0.057  1.00 34.46  ? 272  GLU A C     1 
ATOM   2046 O  O     . GLU A 1 286 ? 1.057   16.911 -0.311  1.00 31.63  ? 272  GLU A O     1 
ATOM   2047 C  CB    . GLU A 1 286 ? 3.899   15.308 0.304   1.00 37.42  ? 272  GLU A CB    1 
ATOM   2048 C  CG    . GLU A 1 286 ? 2.824   14.428 0.916   1.00 43.44  ? 272  GLU A CG    1 
ATOM   2049 C  CD    . GLU A 1 286 ? 2.171   13.517 -0.115  1.00 47.48  ? 272  GLU A CD    1 
ATOM   2050 O  OE1   . GLU A 1 286 ? 2.863   13.131 -1.080  1.00 49.91  ? 272  GLU A OE1   1 
ATOM   2051 O  OE2   . GLU A 1 286 ? 0.965   13.212 0.024   1.00 47.34  ? 272  GLU A OE2   1 
ATOM   2052 N  N     . ALA A 1 287 ? 2.591   18.177 0.746   1.00 32.47  ? 273  ALA A N     1 
ATOM   2053 C  CA    . ALA A 1 287 ? 1.561   18.946 1.435   1.00 34.17  ? 273  ALA A CA    1 
ATOM   2054 C  C     . ALA A 1 287 ? 0.719   19.746 0.452   1.00 33.38  ? 273  ALA A C     1 
ATOM   2055 O  O     . ALA A 1 287 ? -0.505  19.833 0.606   1.00 35.71  ? 273  ALA A O     1 
ATOM   2056 C  CB    . ALA A 1 287 ? 2.192   19.867 2.478   1.00 32.19  ? 273  ALA A CB    1 
ATOM   2057 N  N     . ILE A 1 288 ? 1.344   20.300 -0.587  1.00 29.65  ? 274  ILE A N     1 
ATOM   2058 C  CA    . ILE A 1 288 ? 0.628   21.156 -1.523  1.00 30.11  ? 274  ILE A CA    1 
ATOM   2059 C  C     . ILE A 1 288 ? 0.195   20.355 -2.746  1.00 30.11  ? 274  ILE A C     1 
ATOM   2060 O  O     . ILE A 1 288 ? -1.002  20.208 -3.009  1.00 28.51  ? 274  ILE A O     1 
ATOM   2061 C  CB    . ILE A 1 288 ? 1.483   22.376 -1.922  1.00 26.55  ? 274  ILE A CB    1 
ATOM   2062 C  CG1   . ILE A 1 288 ? 1.873   23.179 -0.678  1.00 27.12  ? 274  ILE A CG1   1 
ATOM   2063 C  CG2   . ILE A 1 288 ? 0.753   23.251 -2.951  1.00 25.69  ? 274  ILE A CG2   1 
ATOM   2064 C  CD1   . ILE A 1 288 ? 0.715   23.500 0.244   1.00 27.39  ? 274  ILE A CD1   1 
ATOM   2065 N  N     . GLU A 1 289 ? 1.155   19.822 -3.500  1.00 30.73  ? 275  GLU A N     1 
ATOM   2066 C  CA    . GLU A 1 289 ? 0.796   19.110 -4.722  1.00 29.15  ? 275  GLU A CA    1 
ATOM   2067 C  C     . GLU A 1 289 ? 0.040   17.815 -4.433  1.00 30.04  ? 275  GLU A C     1 
ATOM   2068 O  O     . GLU A 1 289 ? -0.720  17.351 -5.291  1.00 28.60  ? 275  GLU A O     1 
ATOM   2069 C  CB    . GLU A 1 289 ? 2.055   18.831 -5.546  1.00 28.21  ? 275  GLU A CB    1 
ATOM   2070 C  CG    . GLU A 1 289 ? 2.408   19.983 -6.476  1.00 31.11  ? 275  GLU A CG    1 
ATOM   2071 C  CD    . GLU A 1 289 ? 3.755   19.837 -7.156  1.00 31.84  ? 275  GLU A CD    1 
ATOM   2072 O  OE1   . GLU A 1 289 ? 4.328   18.732 -7.115  1.00 32.59  ? 275  GLU A OE1   1 
ATOM   2073 O  OE2   . GLU A 1 289 ? 4.226   20.832 -7.749  1.00 29.48  ? 275  GLU A OE2   1 
ATOM   2074 N  N     . GLY A 1 290 ? 0.216   17.229 -3.244  1.00 30.30  ? 276  GLY A N     1 
ATOM   2075 C  CA    . GLY A 1 290 ? -0.470  15.995 -2.885  1.00 30.01  ? 276  GLY A CA    1 
ATOM   2076 C  C     . GLY A 1 290 ? -1.896  16.169 -2.406  1.00 31.36  ? 276  GLY A C     1 
ATOM   2077 O  O     . GLY A 1 290 ? -2.638  15.184 -2.318  1.00 31.87  ? 276  GLY A O     1 
ATOM   2078 N  N     . ALA A 1 291 ? -2.302  17.396 -2.098  1.00 31.48  ? 277  ALA A N     1 
ATOM   2079 C  CA    . ALA A 1 291 ? -3.675  17.648 -1.692  1.00 31.78  ? 277  ALA A CA    1 
ATOM   2080 C  C     . ALA A 1 291 ? -4.625  17.501 -2.879  1.00 31.51  ? 277  ALA A C     1 
ATOM   2081 O  O     . ALA A 1 291 ? -4.273  17.774 -4.032  1.00 29.38  ? 277  ALA A O     1 
ATOM   2082 C  CB    . ALA A 1 291 ? -3.807  19.049 -1.089  1.00 29.49  ? 277  ALA A CB    1 
ATOM   2083 N  N     . ASP A 1 292 ? -5.845  17.052 -2.597  1.00 30.84  ? 278  ASP A N     1 
ATOM   2084 C  CA    . ASP A 1 292 ? -6.783  16.956 -3.706  1.00 30.84  ? 278  ASP A CA    1 
ATOM   2085 C  C     . ASP A 1 292 ? -7.449  18.289 -4.022  1.00 30.00  ? 278  ASP A C     1 
ATOM   2086 O  O     . ASP A 1 292 ? -8.014  18.437 -5.110  1.00 30.39  ? 278  ASP A O     1 
ATOM   2087 C  CB    . ASP A 1 292 ? -7.801  15.838 -3.438  1.00 35.37  ? 278  ASP A CB    1 
ATOM   2088 C  CG    . ASP A 1 292 ? -8.220  15.754 -1.993  1.00 36.88  ? 278  ASP A CG    1 
ATOM   2089 O  OD1   . ASP A 1 292 ? -8.643  16.786 -1.428  1.00 37.80  ? 278  ASP A OD1   1 
ATOM   2090 O  OD2   . ASP A 1 292 ? -8.078  14.657 -1.407  1.00 36.45  ? 278  ASP A OD2   1 
ATOM   2091 N  N     . THR A 1 293 ? -7.339  19.280 -3.137  1.00 29.00  ? 279  THR A N     1 
ATOM   2092 C  CA    . THR A 1 293 ? -7.780  20.637 -3.433  1.00 27.57  ? 279  THR A CA    1 
ATOM   2093 C  C     . THR A 1 293 ? -6.786  21.626 -2.856  1.00 26.27  ? 279  THR A C     1 
ATOM   2094 O  O     . THR A 1 293 ? -6.432  21.539 -1.677  1.00 26.13  ? 279  THR A O     1 
ATOM   2095 C  CB    . THR A 1 293 ? -9.180  20.916 -2.876  1.00 27.96  ? 279  THR A CB    1 
ATOM   2096 O  OG1   . THR A 1 293 ? -10.068 19.893 -3.317  1.00 31.12  ? 279  THR A OG1   1 
ATOM   2097 C  CG2   . THR A 1 293 ? -9.701  22.251 -3.370  1.00 27.42  ? 279  THR A CG2   1 
ATOM   2098 N  N     . VAL A 1 294 ? -6.346  22.565 -3.685  1.00 26.27  ? 280  VAL A N     1 
ATOM   2099 C  CA    . VAL A 1 294 ? -5.390  23.587 -3.290  1.00 24.43  ? 280  VAL A CA    1 
ATOM   2100 C  C     . VAL A 1 294 ? -6.058  24.926 -3.540  1.00 24.68  ? 280  VAL A C     1 
ATOM   2101 O  O     . VAL A 1 294 ? -6.435  25.231 -4.679  1.00 23.00  ? 280  VAL A O     1 
ATOM   2102 C  CB    . VAL A 1 294 ? -4.063  23.480 -4.070  1.00 27.37  ? 280  VAL A CB    1 
ATOM   2103 C  CG1   . VAL A 1 294 ? -3.109  24.599 -3.674  1.00 23.44  ? 280  VAL A CG1   1 
ATOM   2104 C  CG2   . VAL A 1 294 ? -3.409  22.102 -3.869  1.00 25.37  ? 280  VAL A CG2   1 
ATOM   2105 N  N     . LEU A 1 295 ? -6.244  25.700 -2.471  1.00 22.27  ? 281  LEU A N     1 
ATOM   2106 C  CA    . LEU A 1 295 ? -6.786  27.050 -2.558  1.00 21.47  ? 281  LEU A CA    1 
ATOM   2107 C  C     . LEU A 1 295 ? -5.627  27.981 -2.879  1.00 24.22  ? 281  LEU A C     1 
ATOM   2108 O  O     . LEU A 1 295 ? -4.706  28.132 -2.069  1.00 24.37  ? 281  LEU A O     1 
ATOM   2109 C  CB    . LEU A 1 295 ? -7.469  27.428 -1.242  1.00 22.46  ? 281  LEU A CB    1 
ATOM   2110 C  CG    . LEU A 1 295 ? -8.504  26.394 -0.782  1.00 22.60  ? 281  LEU A CG    1 
ATOM   2111 C  CD1   . LEU A 1 295 ? -9.254  26.792 0.513   1.00 22.48  ? 281  LEU A CD1   1 
ATOM   2112 C  CD2   . LEU A 1 295 ? -9.495  26.108 -1.889  1.00 20.29  ? 281  LEU A CD2   1 
ATOM   2113 N  N     . CYS A 1 296 ? -5.640  28.563 -4.079  1.00 22.99  ? 282  CYS A N     1 
ATOM   2114 C  CA    . CYS A 1 296 ? -4.574  29.437 -4.552  1.00 22.49  ? 282  CYS A CA    1 
ATOM   2115 C  C     . CYS A 1 296 ? -5.040  30.883 -4.402  1.00 22.00  ? 282  CYS A C     1 
ATOM   2116 O  O     . CYS A 1 296 ? -5.904  31.341 -5.152  1.00 20.60  ? 282  CYS A O     1 
ATOM   2117 C  CB    . CYS A 1 296 ? -4.216  29.111 -6.002  1.00 20.52  ? 282  CYS A CB    1 
ATOM   2118 S  SG    . CYS A 1 296 ? -3.606  27.435 -6.272  1.00 24.44  ? 282  CYS A SG    1 
ATOM   2119 N  N     . ILE A 1 297 ? -4.480  31.596 -3.426  1.00 22.07  ? 283  ILE A N     1 
ATOM   2120 C  CA    . ILE A 1 297 ? -4.960  32.919 -3.038  1.00 21.55  ? 283  ILE A CA    1 
ATOM   2121 C  C     . ILE A 1 297 ? -3.927  33.945 -3.482  1.00 20.64  ? 283  ILE A C     1 
ATOM   2122 O  O     . ILE A 1 297 ? -2.804  33.964 -2.964  1.00 21.36  ? 283  ILE A O     1 
ATOM   2123 C  CB    . ILE A 1 297 ? -5.197  33.032 -1.523  1.00 22.18  ? 283  ILE A CB    1 
ATOM   2124 C  CG1   . ILE A 1 297 ? -5.934  31.818 -0.946  1.00 21.74  ? 283  ILE A CG1   1 
ATOM   2125 C  CG2   . ILE A 1 297 ? -5.911  34.349 -1.181  1.00 21.90  ? 283  ILE A CG2   1 
ATOM   2126 C  CD1   . ILE A 1 297 ? -7.287  31.532 -1.515  1.00 21.05  ? 283  ILE A CD1   1 
ATOM   2127 N  N     . GLY A 1 298 ? -4.307  34.814 -4.415  1.00 21.19  ? 284  GLY A N     1 
ATOM   2128 C  CA    . GLY A 1 298 ? -3.420  35.891 -4.841  1.00 20.90  ? 284  GLY A CA    1 
ATOM   2129 C  C     . GLY A 1 298 ? -2.114  35.417 -5.443  1.00 21.47  ? 284  GLY A C     1 
ATOM   2130 O  O     . GLY A 1 298 ? -1.065  36.042 -5.238  1.00 19.97  ? 284  GLY A O     1 
ATOM   2131 N  N     . THR A 1 299 ? -2.170  34.362 -6.243  1.00 22.85  ? 285  THR A N     1 
ATOM   2132 C  CA    . THR A 1 299 ? -0.999  33.648 -6.724  1.00 23.12  ? 285  THR A CA    1 
ATOM   2133 C  C     . THR A 1 299 ? -0.735  34.001 -8.184  1.00 25.32  ? 285  THR A C     1 
ATOM   2134 O  O     . THR A 1 299 ? -1.664  34.292 -8.948  1.00 22.08  ? 285  THR A O     1 
ATOM   2135 C  CB    . THR A 1 299 ? -1.206  32.138 -6.581  1.00 22.86  ? 285  THR A CB    1 
ATOM   2136 O  OG1   . THR A 1 299 ? -2.509  31.804 -7.076  1.00 25.12  ? 285  THR A OG1   1 
ATOM   2137 C  CG2   . THR A 1 299 ? -1.111  31.713 -5.111  1.00 22.93  ? 285  THR A CG2   1 
ATOM   2138 N  N     . ARG A 1 300 ? 0.552   34.052 -8.539  1.00 22.18  ? 286  ARG A N     1 
ATOM   2139 C  CA    . ARG A 1 300 ? 0.989   34.217 -9.923  1.00 23.09  ? 286  ARG A CA    1 
ATOM   2140 C  C     . ARG A 1 300 ? 2.119   33.223 -10.131 1.00 23.32  ? 286  ARG A C     1 
ATOM   2141 O  O     . ARG A 1 300 ? 3.194   33.356 -9.531  1.00 19.81  ? 286  ARG A O     1 
ATOM   2142 C  CB    . ARG A 1 300 ? 1.441   35.647 -10.216 1.00 23.41  ? 286  ARG A CB    1 
ATOM   2143 C  CG    . ARG A 1 300 ? 0.294   36.665 -10.110 1.00 25.09  ? 286  ARG A CG    1 
ATOM   2144 C  CD    . ARG A 1 300 ? -0.797  36.377 -11.121 1.00 27.02  ? 286  ARG A CD    1 
ATOM   2145 N  NE    . ARG A 1 300 ? -2.058  37.025 -10.781 1.00 27.67  ? 286  ARG A NE    1 
ATOM   2146 C  CZ    . ARG A 1 300 ? -2.398  38.251 -11.155 1.00 29.77  ? 286  ARG A CZ    1 
ATOM   2147 N  NH1   . ARG A 1 300 ? -1.585  39.001 -11.879 1.00 27.95  ? 286  ARG A NH1   1 
ATOM   2148 N  NH2   . ARG A 1 300 ? -3.594  38.729 -10.808 1.00 29.29  ? 286  ARG A NH2   1 
ATOM   2149 N  N     . PHE A 1 301 ? 1.865   32.204 -10.947 1.00 21.98  ? 287  PHE A N     1 
ATOM   2150 C  CA    . PHE A 1 301 ? 2.809   31.105 -11.099 1.00 22.82  ? 287  PHE A CA    1 
ATOM   2151 C  C     . PHE A 1 301 ? 3.843   31.509 -12.150 1.00 23.44  ? 287  PHE A C     1 
ATOM   2152 O  O     . PHE A 1 301 ? 3.799   31.091 -13.310 1.00 21.60  ? 287  PHE A O     1 
ATOM   2153 C  CB    . PHE A 1 301 ? 2.066   29.828 -11.469 1.00 22.69  ? 287  PHE A CB    1 
ATOM   2154 C  CG    . PHE A 1 301 ? 1.250   29.256 -10.331 1.00 24.09  ? 287  PHE A CG    1 
ATOM   2155 C  CD1   . PHE A 1 301 ? 1.864   28.536 -9.314  1.00 25.11  ? 287  PHE A CD1   1 
ATOM   2156 C  CD2   . PHE A 1 301 ? -0.119  29.451 -10.271 1.00 25.33  ? 287  PHE A CD2   1 
ATOM   2157 C  CE1   . PHE A 1 301 ? 1.115   28.008 -8.248  1.00 23.61  ? 287  PHE A CE1   1 
ATOM   2158 C  CE2   . PHE A 1 301 ? -0.872  28.931 -9.210  1.00 26.14  ? 287  PHE A CE2   1 
ATOM   2159 C  CZ    . PHE A 1 301 ? -0.248  28.204 -8.207  1.00 24.26  ? 287  PHE A CZ    1 
ATOM   2160 N  N     . THR A 1 302 ? 4.801   32.335 -11.722 1.00 21.96  ? 288  THR A N     1 
ATOM   2161 C  CA    . THR A 1 302 ? 5.825   32.802 -12.646 1.00 22.20  ? 288  THR A CA    1 
ATOM   2162 C  C     . THR A 1 302 ? 6.905   31.738 -12.808 1.00 23.85  ? 288  THR A C     1 
ATOM   2163 O  O     . THR A 1 302 ? 6.974   30.758 -12.051 1.00 20.32  ? 288  THR A O     1 
ATOM   2164 C  CB    . THR A 1 302 ? 6.457   34.111 -12.166 1.00 21.66  ? 288  THR A CB    1 
ATOM   2165 O  OG1   . THR A 1 302 ? 7.449   33.824 -11.173 1.00 21.90  ? 288  THR A OG1   1 
ATOM   2166 C  CG2   . THR A 1 302 ? 5.414   35.050 -11.578 1.00 23.09  ? 288  THR A CG2   1 
ATOM   2167 N  N     . ASP A 1 303 ? 7.780   31.955 -13.801 1.00 22.74  ? 289  ASP A N     1 
ATOM   2168 C  CA    . ASP A 1 303 ? 8.806   30.957 -14.091 1.00 23.30  ? 289  ASP A CA    1 
ATOM   2169 C  C     . ASP A 1 303 ? 9.729   30.773 -12.900 1.00 24.39  ? 289  ASP A C     1 
ATOM   2170 O  O     . ASP A 1 303 ? 10.008  29.643 -12.488 1.00 26.20  ? 289  ASP A O     1 
ATOM   2171 C  CB    . ASP A 1 303 ? 9.608   31.340 -15.348 1.00 23.47  ? 289  ASP A CB    1 
ATOM   2172 C  CG    . ASP A 1 303 ? 10.308  32.693 -15.247 1.00 21.81  ? 289  ASP A CG    1 
ATOM   2173 O  OD1   . ASP A 1 303 ? 10.033  33.498 -14.335 1.00 23.22  ? 289  ASP A OD1   1 
ATOM   2174 O  OD2   . ASP A 1 303 ? 11.145  32.976 -16.122 1.00 25.15  ? 289  ASP A OD2   1 
ATOM   2175 N  N     . THR A 1 304 ? 10.158  31.877 -12.298 1.00 23.06  ? 290  THR A N     1 
ATOM   2176 C  CA    . THR A 1 304 ? 11.020  31.802 -11.128 1.00 27.61  ? 290  THR A CA    1 
ATOM   2177 C  C     . THR A 1 304 ? 10.309  31.135 -9.954  1.00 27.13  ? 290  THR A C     1 
ATOM   2178 O  O     . THR A 1 304 ? 10.912  30.346 -9.219  1.00 31.13  ? 290  THR A O     1 
ATOM   2179 C  CB    . THR A 1 304 ? 11.462  33.212 -10.754 1.00 29.08  ? 290  THR A CB    1 
ATOM   2180 O  OG1   . THR A 1 304 ? 12.338  33.743 -11.760 1.00 30.97  ? 290  THR A OG1   1 
ATOM   2181 C  CG2   . THR A 1 304 ? 12.089  33.243 -9.404  1.00 32.67  ? 290  THR A CG2   1 
ATOM   2182 N  N     . LEU A 1 305 ? 9.019   31.418 -9.782  1.00 25.10  ? 291  LEU A N     1 
ATOM   2183 C  CA    . LEU A 1 305 ? 8.287   30.907 -8.627  1.00 25.89  ? 291  LEU A CA    1 
ATOM   2184 C  C     . LEU A 1 305 ? 7.971   29.422 -8.737  1.00 25.59  ? 291  LEU A C     1 
ATOM   2185 O  O     . LEU A 1 305 ? 7.628   28.803 -7.724  1.00 25.46  ? 291  LEU A O     1 
ATOM   2186 C  CB    . LEU A 1 305 ? 6.996   31.703 -8.445  1.00 22.28  ? 291  LEU A CB    1 
ATOM   2187 C  CG    . LEU A 1 305 ? 7.075   32.795 -7.380  1.00 23.49  ? 291  LEU A CG    1 
ATOM   2188 C  CD1   . LEU A 1 305 ? 8.249   33.737 -7.620  1.00 24.16  ? 291  LEU A CD1   1 
ATOM   2189 C  CD2   . LEU A 1 305 ? 5.771   33.563 -7.344  1.00 21.16  ? 291  LEU A CD2   1 
ATOM   2190 N  N     . THR A 1 306 ? 8.083   28.829 -9.927  1.00 25.46  ? 292  THR A N     1 
ATOM   2191 C  CA    . THR A 1 306 ? 7.696   27.437 -10.130 1.00 25.17  ? 292  THR A CA    1 
ATOM   2192 C  C     . THR A 1 306 ? 8.849   26.591 -10.674 1.00 28.21  ? 292  THR A C     1 
ATOM   2193 O  O     . THR A 1 306 ? 8.621   25.499 -11.207 1.00 26.97  ? 292  THR A O     1 
ATOM   2194 C  CB    . THR A 1 306 ? 6.492   27.374 -11.066 1.00 25.85  ? 292  THR A CB    1 
ATOM   2195 O  OG1   . THR A 1 306 ? 6.832   28.010 -12.305 1.00 26.13  ? 292  THR A OG1   1 
ATOM   2196 C  CG2   . THR A 1 306 ? 5.295   28.108 -10.447 1.00 23.54  ? 292  THR A CG2   1 
ATOM   2197 N  N     . ALA A 1 307 ? 10.084  27.067 -10.537 1.00 28.26  ? 293  ALA A N     1 
ATOM   2198 C  CA    . ALA A 1 307 ? 11.260  26.376 -11.070 1.00 32.13  ? 293  ALA A CA    1 
ATOM   2199 C  C     . ALA A 1 307 ? 11.049  26.012 -12.538 1.00 30.61  ? 293  ALA A C     1 
ATOM   2200 O  O     . ALA A 1 307 ? 11.134  24.849 -12.936 1.00 31.97  ? 293  ALA A O     1 
ATOM   2201 C  CB    . ALA A 1 307 ? 11.605  25.137 -10.242 1.00 32.90  ? 293  ALA A CB    1 
ATOM   2202 N  N     . GLY A 1 308 ? 10.732  27.021 -13.343 1.00 30.22  ? 294  GLY A N     1 
ATOM   2203 C  CA    . GLY A 1 308 ? 10.485  26.794 -14.757 1.00 29.00  ? 294  GLY A CA    1 
ATOM   2204 C  C     . GLY A 1 308 ? 9.182   26.098 -15.088 1.00 27.96  ? 294  GLY A C     1 
ATOM   2205 O  O     . GLY A 1 308 ? 9.167   25.207 -15.943 1.00 27.46  ? 294  GLY A O     1 
ATOM   2206 N  N     . PHE A 1 309 ? 8.088   26.471 -14.414 1.00 28.01  ? 295  PHE A N     1 
ATOM   2207 C  CA    . PHE A 1 309 ? 6.753   25.930 -14.691 1.00 27.33  ? 295  PHE A CA    1 
ATOM   2208 C  C     . PHE A 1 309 ? 6.705   24.414 -14.505 1.00 28.30  ? 295  PHE A C     1 
ATOM   2209 O  O     . PHE A 1 309 ? 6.046   23.699 -15.262 1.00 27.41  ? 295  PHE A O     1 
ATOM   2210 C  CB    . PHE A 1 309 ? 6.273   26.315 -16.092 1.00 26.11  ? 295  PHE A CB    1 
ATOM   2211 C  CG    . PHE A 1 309 ? 6.407   27.781 -16.403 1.00 26.53  ? 295  PHE A CG    1 
ATOM   2212 C  CD1   . PHE A 1 309 ? 5.725   28.730 -15.648 1.00 24.84  ? 295  PHE A CD1   1 
ATOM   2213 C  CD2   . PHE A 1 309 ? 7.207   28.210 -17.461 1.00 25.53  ? 295  PHE A CD2   1 
ATOM   2214 C  CE1   . PHE A 1 309 ? 5.846   30.077 -15.919 1.00 22.24  ? 295  PHE A CE1   1 
ATOM   2215 C  CE2   . PHE A 1 309 ? 7.319   29.564 -17.757 1.00 25.64  ? 295  PHE A CE2   1 
ATOM   2216 C  CZ    . PHE A 1 309 ? 6.624   30.500 -16.985 1.00 22.94  ? 295  PHE A CZ    1 
ATOM   2217 N  N     . THR A 1 310 ? 7.409   23.910 -13.490 1.00 28.47  ? 296  THR A N     1 
ATOM   2218 C  CA    . THR A 1 310 ? 7.357   22.491 -13.162 1.00 28.26  ? 296  THR A CA    1 
ATOM   2219 C  C     . THR A 1 310 ? 6.448   22.213 -11.973 1.00 28.56  ? 296  THR A C     1 
ATOM   2220 O  O     . THR A 1 310 ? 6.523   21.130 -11.385 1.00 29.21  ? 296  THR A O     1 
ATOM   2221 C  CB    . THR A 1 310 ? 8.752   21.950 -12.876 1.00 28.13  ? 296  THR A CB    1 
ATOM   2222 O  OG1   . THR A 1 310 ? 9.420   22.819 -11.952 1.00 30.56  ? 296  THR A OG1   1 
ATOM   2223 C  CG2   . THR A 1 310 ? 9.555   21.862 -14.167 1.00 29.47  ? 296  THR A CG2   1 
ATOM   2224 N  N     . HIS A 1 311 ? 5.607   23.176 -11.607 1.00 27.67  ? 297  HIS A N     1 
ATOM   2225 C  CA    . HIS A 1 311 ? 4.555   22.935 -10.629 1.00 28.25  ? 297  HIS A CA    1 
ATOM   2226 C  C     . HIS A 1 311 ? 3.526   21.962 -11.185 1.00 28.14  ? 297  HIS A C     1 
ATOM   2227 O  O     . HIS A 1 311 ? 3.247   21.938 -12.387 1.00 28.80  ? 297  HIS A O     1 
ATOM   2228 C  CB    . HIS A 1 311 ? 3.880   24.247 -10.219 1.00 26.15  ? 297  HIS A CB    1 
ATOM   2229 C  CG    . HIS A 1 311 ? 3.310   25.037 -11.361 1.00 27.51  ? 297  HIS A CG    1 
ATOM   2230 N  ND1   . HIS A 1 311 ? 4.039   25.361 -12.488 1.00 26.79  ? 297  HIS A ND1   1 
ATOM   2231 C  CD2   . HIS A 1 311 ? 2.078   25.579 -11.542 1.00 26.92  ? 297  HIS A CD2   1 
ATOM   2232 C  CE1   . HIS A 1 311 ? 3.284   26.073 -13.307 1.00 25.91  ? 297  HIS A CE1   1 
ATOM   2233 N  NE2   . HIS A 1 311 ? 2.091   26.219 -12.757 1.00 26.62  ? 297  HIS A NE2   1 
ATOM   2234 N  N     . GLN A 1 312 ? 2.984   21.129 -10.305 1.00 30.06  ? 298  GLN A N     1 
ATOM   2235 C  CA    . GLN A 1 312 ? 2.002   20.113 -10.676 1.00 30.51  ? 298  GLN A CA    1 
ATOM   2236 C  C     . GLN A 1 312 ? 0.698   20.438 -9.950  1.00 30.77  ? 298  GLN A C     1 
ATOM   2237 O  O     . GLN A 1 312 ? 0.426   19.918 -8.863  1.00 31.09  ? 298  GLN A O     1 
ATOM   2238 C  CB    . GLN A 1 312 ? 2.531   18.728 -10.340 1.00 31.90  ? 298  GLN A CB    1 
ATOM   2239 C  CG    . GLN A 1 312 ? 3.834   18.416 -11.079 1.00 36.73  ? 298  GLN A CG    1 
ATOM   2240 C  CD    . GLN A 1 312 ? 4.199   16.945 -11.054 1.00 43.80  ? 298  GLN A CD    1 
ATOM   2241 O  OE1   . GLN A 1 312 ? 5.282   16.572 -10.606 1.00 50.83  ? 298  GLN A OE1   1 
ATOM   2242 N  NE2   . GLN A 1 312 ? 3.291   16.099 -11.532 1.00 47.40  ? 298  GLN A NE2   1 
ATOM   2243 N  N     . LEU A 1 313 ? -0.110  21.297 -10.571 1.00 29.60  ? 299  LEU A N     1 
ATOM   2244 C  CA    . LEU A 1 313 ? -1.398  21.728 -10.037 1.00 29.06  ? 299  LEU A CA    1 
ATOM   2245 C  C     . LEU A 1 313 ? -2.357  21.851 -11.206 1.00 31.03  ? 299  LEU A C     1 
ATOM   2246 O  O     . LEU A 1 313 ? -2.119  22.646 -12.117 1.00 33.29  ? 299  LEU A O     1 
ATOM   2247 C  CB    . LEU A 1 313 ? -1.277  23.070 -9.310  1.00 26.80  ? 299  LEU A CB    1 
ATOM   2248 C  CG    . LEU A 1 313 ? -0.497  23.099 -7.996  1.00 28.88  ? 299  LEU A CG    1 
ATOM   2249 C  CD1   . LEU A 1 313 ? -0.408  24.520 -7.461  1.00 27.47  ? 299  LEU A CD1   1 
ATOM   2250 C  CD2   . LEU A 1 313 ? -1.128  22.163 -6.961  1.00 28.71  ? 299  LEU A CD2   1 
ATOM   2251 N  N     . THR A 1 314 ? -3.425  21.068 -11.188 1.00 30.55  ? 300  THR A N     1 
ATOM   2252 C  CA    . THR A 1 314 ? -4.367  21.038 -12.292 1.00 29.92  ? 300  THR A CA    1 
ATOM   2253 C  C     . THR A 1 314 ? -5.550  21.943 -12.001 1.00 31.31  ? 300  THR A C     1 
ATOM   2254 O  O     . THR A 1 314 ? -5.760  22.361 -10.858 1.00 29.42  ? 300  THR A O     1 
ATOM   2255 C  CB    . THR A 1 314 ? -4.856  19.611 -12.547 1.00 31.10  ? 300  THR A CB    1 
ATOM   2256 O  OG1   . THR A 1 314 ? -5.791  19.242 -11.529 1.00 34.17  ? 300  THR A OG1   1 
ATOM   2257 C  CG2   . THR A 1 314 ? -3.690  18.634 -12.544 1.00 31.43  ? 300  THR A CG2   1 
ATOM   2258 N  N     . PRO A 1 315 ? -6.325  22.310 -13.030 1.00 32.33  ? 301  PRO A N     1 
ATOM   2259 C  CA    . PRO A 1 315 ? -7.507  23.147 -12.772 1.00 30.24  ? 301  PRO A CA    1 
ATOM   2260 C  C     . PRO A 1 315 ? -8.530  22.511 -11.847 1.00 29.83  ? 301  PRO A C     1 
ATOM   2261 O  O     . PRO A 1 315 ? -9.031  23.187 -10.935 1.00 30.10  ? 301  PRO A O     1 
ATOM   2262 C  CB    . PRO A 1 315 ? -8.085  23.373 -14.178 1.00 33.13  ? 301  PRO A CB    1 
ATOM   2263 C  CG    . PRO A 1 315 ? -6.941  23.196 -15.105 1.00 33.47  ? 301  PRO A CG    1 
ATOM   2264 C  CD    . PRO A 1 315 ? -6.015  22.203 -14.469 1.00 34.78  ? 301  PRO A CD    1 
ATOM   2265 N  N     . SER A 1 316 ? -8.838  21.222 -12.022 1.00 28.40  ? 302  SER A N     1 
ATOM   2266 C  CA    . SER A 1 316 ? -9.864  20.615 -11.178 1.00 31.06  ? 302  SER A CA    1 
ATOM   2267 C  C     . SER A 1 316 ? -9.376  20.428 -9.751  1.00 31.95  ? 302  SER A C     1 
ATOM   2268 O  O     . SER A 1 316 ? -10.200 20.310 -8.834  1.00 31.97  ? 302  SER A O     1 
ATOM   2269 C  CB    . SER A 1 316 ? -10.330 19.275 -11.755 1.00 32.53  ? 302  SER A CB    1 
ATOM   2270 O  OG    . SER A 1 316 ? -9.291  18.312 -11.717 1.00 37.80  ? 302  SER A OG    1 
ATOM   2271 N  N     . GLN A 1 317 ? -8.058  20.404 -9.554  1.00 30.71  ? 303  GLN A N     1 
ATOM   2272 C  CA    . GLN A 1 317 ? -7.438  20.347 -8.240  1.00 28.95  ? 303  GLN A CA    1 
ATOM   2273 C  C     . GLN A 1 317 ? -7.463  21.689 -7.512  1.00 28.52  ? 303  GLN A C     1 
ATOM   2274 O  O     . GLN A 1 317 ? -7.198  21.720 -6.310  1.00 27.94  ? 303  GLN A O     1 
ATOM   2275 C  CB    . GLN A 1 317 ? -5.988  19.838 -8.377  1.00 29.18  ? 303  GLN A CB    1 
ATOM   2276 C  CG    . GLN A 1 317 ? -5.267  19.550 -7.067  1.00 29.18  ? 303  GLN A CG    1 
ATOM   2277 C  CD    . GLN A 1 317 ? -3.801  19.166 -7.269  1.00 29.85  ? 303  GLN A CD    1 
ATOM   2278 O  OE1   . GLN A 1 317 ? -3.265  19.280 -8.369  1.00 28.41  ? 303  GLN A OE1   1 
ATOM   2279 N  NE2   . GLN A 1 317 ? -3.159  18.687 -6.205  1.00 27.93  ? 303  GLN A NE2   1 
ATOM   2280 N  N     . THR A 1 318 ? -7.776  22.797 -8.184  1.00 26.25  ? 304  THR A N     1 
ATOM   2281 C  CA    . THR A 1 318 ? -7.535  24.106 -7.598  1.00 25.74  ? 304  THR A CA    1 
ATOM   2282 C  C     . THR A 1 318 ? -8.794  24.968 -7.539  1.00 25.30  ? 304  THR A C     1 
ATOM   2283 O  O     . THR A 1 318 ? -9.758  24.786 -8.292  1.00 25.04  ? 304  THR A O     1 
ATOM   2284 C  CB    . THR A 1 318 ? -6.452  24.886 -8.362  1.00 27.14  ? 304  THR A CB    1 
ATOM   2285 O  OG1   . THR A 1 318 ? -6.667  24.779 -9.778  1.00 27.46  ? 304  THR A OG1   1 
ATOM   2286 C  CG2   . THR A 1 318 ? -5.063  24.363 -7.993  1.00 24.76  ? 304  THR A CG2   1 
ATOM   2287 N  N     . ILE A 1 319 ? -8.753  25.897 -6.590  1.00 22.90  ? 305  ILE A N     1 
ATOM   2288 C  CA    . ILE A 1 319 ? -9.616  27.069 -6.515  1.00 22.62  ? 305  ILE A CA    1 
ATOM   2289 C  C     . ILE A 1 319 ? -8.681  28.268 -6.423  1.00 22.18  ? 305  ILE A C     1 
ATOM   2290 O  O     . ILE A 1 319 ? -7.726  28.243 -5.637  1.00 22.37  ? 305  ILE A O     1 
ATOM   2291 C  CB    . ILE A 1 319 ? -10.546 26.997 -5.286  1.00 22.59  ? 305  ILE A CB    1 
ATOM   2292 C  CG1   . ILE A 1 319 ? -11.551 25.858 -5.425  1.00 24.66  ? 305  ILE A CG1   1 
ATOM   2293 C  CG2   . ILE A 1 319 ? -11.235 28.323 -5.027  1.00 22.40  ? 305  ILE A CG2   1 
ATOM   2294 C  CD1   . ILE A 1 319 ? -12.490 25.724 -4.235  1.00 25.86  ? 305  ILE A CD1   1 
ATOM   2295 N  N     . GLU A 1 320 ? -8.901  29.295 -7.245  1.00 22.17  ? 306  GLU A N     1 
ATOM   2296 C  CA    . GLU A 1 320 ? -8.011  30.449 -7.165  1.00 22.83  ? 306  GLU A CA    1 
ATOM   2297 C  C     . GLU A 1 320 ? -8.814  31.730 -7.004  1.00 22.40  ? 306  GLU A C     1 
ATOM   2298 O  O     . GLU A 1 320 ? -9.968  31.822 -7.433  1.00 22.04  ? 306  GLU A O     1 
ATOM   2299 C  CB    . GLU A 1 320 ? -7.037  30.576 -8.368  1.00 23.48  ? 306  GLU A CB    1 
ATOM   2300 C  CG    . GLU A 1 320 ? -7.517  31.291 -9.568  1.00 23.02  ? 306  GLU A CG    1 
ATOM   2301 C  CD    . GLU A 1 320 ? -6.476  31.282 -10.696 1.00 23.78  ? 306  GLU A CD    1 
ATOM   2302 O  OE1   . GLU A 1 320 ? -5.596  32.180 -10.783 1.00 25.60  ? 306  GLU A OE1   1 
ATOM   2303 O  OE2   . GLU A 1 320 ? -6.521  30.322 -11.476 1.00 20.37  ? 306  GLU A OE2   1 
ATOM   2304 N  N     . VAL A 1 321 ? -8.177  32.687 -6.364  1.00 20.38  ? 307  VAL A N     1 
ATOM   2305 C  CA    . VAL A 1 321 ? -8.762  33.949 -6.037  1.00 19.94  ? 307  VAL A CA    1 
ATOM   2306 C  C     . VAL A 1 321 ? -7.869  35.101 -6.505  1.00 22.87  ? 307  VAL A C     1 
ATOM   2307 O  O     . VAL A 1 321 ? -6.773  35.226 -6.065  1.00 22.02  ? 307  VAL A O     1 
ATOM   2308 C  CB    . VAL A 1 321 ? -8.953  34.028 -4.510  1.00 21.28  ? 307  VAL A CB    1 
ATOM   2309 C  CG1   . VAL A 1 321 ? -9.473  35.354 -4.101  1.00 22.34  ? 307  VAL A CG1   1 
ATOM   2310 C  CG2   . VAL A 1 321 ? -9.837  32.905 -4.043  1.00 24.85  ? 307  VAL A CG2   1 
ATOM   2311 N  N     . GLN A 1 322 ? -8.359  35.893 -7.445  1.00 22.98  ? 308  GLN A N     1 
ATOM   2312 C  CA    . GLN A 1 322 ? -7.633  37.039 -7.939  1.00 22.53  ? 308  GLN A CA    1 
ATOM   2313 C  C     . GLN A 1 322 ? -8.351  38.287 -7.451  1.00 21.93  ? 308  GLN A C     1 
ATOM   2314 O  O     . GLN A 1 322 ? -9.422  38.196 -6.843  1.00 21.93  ? 308  GLN A O     1 
ATOM   2315 C  CB    . GLN A 1 322 ? -7.529  36.976 -9.475  1.00 21.28  ? 308  GLN A CB    1 
ATOM   2316 C  CG    . GLN A 1 322 ? -6.673  35.789 -9.984  1.00 22.49  ? 308  GLN A CG    1 
ATOM   2317 C  CD    . GLN A 1 322 ? -5.216  35.792 -9.461  1.00 24.37  ? 308  GLN A CD    1 
ATOM   2318 O  OE1   . GLN A 1 322 ? -4.667  36.841 -9.109  1.00 23.94  ? 308  GLN A OE1   1 
ATOM   2319 N  NE2   . GLN A 1 322 ? -4.595  34.613 -9.417  1.00 20.38  ? 308  GLN A NE2   1 
ATOM   2320 N  N     . PRO A 1 323 ? -7.766  39.474 -7.640  1.00 22.94  ? 309  PRO A N     1 
ATOM   2321 C  CA    . PRO A 1 323 ? -8.382  40.682 -7.061  1.00 24.11  ? 309  PRO A CA    1 
ATOM   2322 C  C     . PRO A 1 323 ? -9.850  40.913 -7.416  1.00 22.91  ? 309  PRO A C     1 
ATOM   2323 O  O     . PRO A 1 323 ? -10.599 41.419 -6.576  1.00 23.42  ? 309  PRO A O     1 
ATOM   2324 C  CB    . PRO A 1 323 ? -7.491  41.797 -7.614  1.00 22.44  ? 309  PRO A CB    1 
ATOM   2325 C  CG    . PRO A 1 323 ? -6.129  41.137 -7.670  1.00 23.89  ? 309  PRO A CG    1 
ATOM   2326 C  CD    . PRO A 1 323 ? -6.423  39.759 -8.182  1.00 23.35  ? 309  PRO A CD    1 
ATOM   2327 N  N     . HIS A 1 324 ? -10.297 40.544 -8.611  1.00 24.28  ? 310  HIS A N     1 
ATOM   2328 C  CA    . HIS A 1 324 ? -11.667 40.827 -9.007  1.00 22.83  ? 310  HIS A CA    1 
ATOM   2329 C  C     . HIS A 1 324 ? -12.423 39.593 -9.467  1.00 22.82  ? 310  HIS A C     1 
ATOM   2330 O  O     . HIS A 1 324 ? -13.572 39.721 -9.912  1.00 22.58  ? 310  HIS A O     1 
ATOM   2331 C  CB    . HIS A 1 324 ? -11.691 41.859 -10.144 1.00 25.96  ? 310  HIS A CB    1 
ATOM   2332 C  CG    . HIS A 1 324 ? -10.965 43.132 -9.838  1.00 25.84  ? 310  HIS A CG    1 
ATOM   2333 N  ND1   . HIS A 1 324 ? -11.384 44.016 -8.867  1.00 28.12  ? 310  HIS A ND1   1 
ATOM   2334 C  CD2   . HIS A 1 324 ? -9.856  43.680 -10.391 1.00 26.04  ? 310  HIS A CD2   1 
ATOM   2335 C  CE1   . HIS A 1 324 ? -10.559 45.048 -8.828  1.00 28.97  ? 310  HIS A CE1   1 
ATOM   2336 N  NE2   . HIS A 1 324 ? -9.627  44.872 -9.746  1.00 27.99  ? 310  HIS A NE2   1 
ATOM   2337 N  N     . ALA A 1 325 ? -11.814 38.415 -9.412  1.00 20.41  ? 311  ALA A N     1 
ATOM   2338 C  CA    . ALA A 1 325 ? -12.490 37.241 -9.940  1.00 22.41  ? 311  ALA A CA    1 
ATOM   2339 C  C     . ALA A 1 325 ? -11.904 36.004 -9.290  1.00 21.14  ? 311  ALA A C     1 
ATOM   2340 O  O     . ALA A 1 325 ? -10.736 35.988 -8.899  1.00 20.79  ? 311  ALA A O     1 
ATOM   2341 C  CB    . ALA A 1 325 ? -12.359 37.149 -11.469 1.00 22.15  ? 311  ALA A CB    1 
ATOM   2342 N  N     . SER A 1 326 ? -12.724 34.960 -9.192  1.00 21.25  ? 312  SER A N     1 
ATOM   2343 C  CA    . SER A 1 326 ? -12.277 33.707 -8.615  1.00 21.45  ? 312  SER A CA    1 
ATOM   2344 C  C     . SER A 1 326 ? -12.711 32.567 -9.523  1.00 21.08  ? 312  SER A C     1 
ATOM   2345 O  O     . SER A 1 326 ? -13.642 32.700 -10.323 1.00 22.32  ? 312  SER A O     1 
ATOM   2346 C  CB    . SER A 1 326 ? -12.827 33.524 -7.189  1.00 19.66  ? 312  SER A CB    1 
ATOM   2347 O  OG    . SER A 1 326 ? -12.031 34.253 -6.261  1.00 20.20  ? 312  SER A OG    1 
ATOM   2348 N  N     . ARG A 1 327 ? -12.036 31.432 -9.369  1.00 20.49  ? 313  ARG A N     1 
ATOM   2349 C  CA    . ARG A 1 327 ? -12.224 30.276 -10.229 1.00 23.38  ? 313  ARG A CA    1 
ATOM   2350 C  C     . ARG A 1 327 ? -12.371 29.022 -9.380  1.00 23.78  ? 313  ARG A C     1 
ATOM   2351 O  O     . ARG A 1 327 ? -11.611 28.824 -8.426  1.00 21.94  ? 313  ARG A O     1 
ATOM   2352 C  CB    . ARG A 1 327 ? -11.035 30.114 -11.192 1.00 22.45  ? 313  ARG A CB    1 
ATOM   2353 C  CG    . ARG A 1 327 ? -10.960 28.763 -11.876 1.00 23.04  ? 313  ARG A CG    1 
ATOM   2354 C  CD    . ARG A 1 327 ? -9.717  28.633 -12.772 1.00 22.92  ? 313  ARG A CD    1 
ATOM   2355 N  NE    . ARG A 1 327 ? -8.487  28.569 -11.984 1.00 24.62  ? 313  ARG A NE    1 
ATOM   2356 C  CZ    . ARG A 1 327 ? -8.076  27.486 -11.343 1.00 26.14  ? 313  ARG A CZ    1 
ATOM   2357 N  NH1   . ARG A 1 327 ? -8.802  26.377 -11.327 1.00 24.82  ? 313  ARG A NH1   1 
ATOM   2358 N  NH2   . ARG A 1 327 ? -6.916  27.516 -10.691 1.00 25.31  ? 313  ARG A NH2   1 
ATOM   2359 N  N     . VAL A 1 328 ? -13.336 28.171 -9.735  1.00 22.35  ? 314  VAL A N     1 
ATOM   2360 C  CA    . VAL A 1 328 ? -13.465 26.839 -9.146  1.00 24.58  ? 314  VAL A CA    1 
ATOM   2361 C  C     . VAL A 1 328 ? -13.368 25.844 -10.296 1.00 25.25  ? 314  VAL A C     1 
ATOM   2362 O  O     . VAL A 1 328 ? -14.272 25.770 -11.137 1.00 23.94  ? 314  VAL A O     1 
ATOM   2363 C  CB    . VAL A 1 328 ? -14.777 26.659 -8.369  1.00 24.75  ? 314  VAL A CB    1 
ATOM   2364 C  CG1   . VAL A 1 328 ? -14.829 25.277 -7.750  1.00 24.80  ? 314  VAL A CG1   1 
ATOM   2365 C  CG2   . VAL A 1 328 ? -14.945 27.729 -7.307  1.00 21.85  ? 314  VAL A CG2   1 
ATOM   2366 N  N     . GLY A 1 329 ? -12.280 25.083 -10.341 1.00 26.00  ? 315  GLY A N     1 
ATOM   2367 C  CA    . GLY A 1 329 ? -12.091 24.152 -11.441 1.00 27.00  ? 315  GLY A CA    1 
ATOM   2368 C  C     . GLY A 1 329 ? -11.944 24.911 -12.748 1.00 27.86  ? 315  GLY A C     1 
ATOM   2369 O  O     . GLY A 1 329 ? -11.040 25.738 -12.916 1.00 28.21  ? 315  GLY A O     1 
ATOM   2370 N  N     . ASP A 1 330 ? -12.840 24.649 -13.692 1.00 28.17  ? 316  ASP A N     1 
ATOM   2371 C  CA    . ASP A 1 330 ? -12.789 25.307 -14.990 1.00 29.32  ? 316  ASP A CA    1 
ATOM   2372 C  C     . ASP A 1 330 ? -13.654 26.563 -15.069 1.00 27.07  ? 316  ASP A C     1 
ATOM   2373 O  O     . ASP A 1 330 ? -13.632 27.243 -16.099 1.00 25.02  ? 316  ASP A O     1 
ATOM   2374 C  CB    . ASP A 1 330 ? -13.211 24.333 -16.097 1.00 33.54  ? 316  ASP A CB    1 
ATOM   2375 C  CG    . ASP A 1 330 ? -12.231 23.190 -16.276 1.00 36.82  ? 316  ASP A CG    1 
ATOM   2376 O  OD1   . ASP A 1 330 ? -11.009 23.441 -16.299 1.00 36.10  ? 316  ASP A OD1   1 
ATOM   2377 O  OD2   . ASP A 1 330 ? -12.693 22.035 -16.402 1.00 44.13  ? 316  ASP A OD2   1 
ATOM   2378 N  N     . VAL A 1 331 ? -14.411 26.901 -14.027 1.00 25.25  ? 317  VAL A N     1 
ATOM   2379 C  CA    . VAL A 1 331 ? -15.416 27.957 -14.109 1.00 23.68  ? 317  VAL A CA    1 
ATOM   2380 C  C     . VAL A 1 331 ? -14.899 29.192 -13.376 1.00 23.93  ? 317  VAL A C     1 
ATOM   2381 O  O     . VAL A 1 331 ? -14.464 29.102 -12.221 1.00 22.42  ? 317  VAL A O     1 
ATOM   2382 C  CB    . VAL A 1 331 ? -16.771 27.501 -13.540 1.00 25.92  ? 317  VAL A CB    1 
ATOM   2383 C  CG1   . VAL A 1 331 ? -17.823 28.587 -13.751 1.00 26.45  ? 317  VAL A CG1   1 
ATOM   2384 C  CG2   . VAL A 1 331 ? -17.216 26.199 -14.199 1.00 27.71  ? 317  VAL A CG2   1 
ATOM   2385 N  N     . TRP A 1 332 ? -14.958 30.341 -14.050 1.00 20.74  ? 318  TRP A N     1 
ATOM   2386 C  CA    . TRP A 1 332 ? -14.572 31.631 -13.496 1.00 21.35  ? 318  TRP A CA    1 
ATOM   2387 C  C     . TRP A 1 332 ? -15.797 32.407 -13.032 1.00 23.38  ? 318  TRP A C     1 
ATOM   2388 O  O     . TRP A 1 332 ? -16.843 32.387 -13.689 1.00 22.38  ? 318  TRP A O     1 
ATOM   2389 C  CB    . TRP A 1 332 ? -13.807 32.444 -14.541 1.00 21.49  ? 318  TRP A CB    1 
ATOM   2390 C  CG    . TRP A 1 332 ? -12.370 32.091 -14.594 1.00 22.79  ? 318  TRP A CG    1 
ATOM   2391 C  CD1   . TRP A 1 332 ? -11.764 31.212 -15.456 1.00 24.25  ? 318  TRP A CD1   1 
ATOM   2392 C  CD2   . TRP A 1 332 ? -11.340 32.605 -13.747 1.00 22.91  ? 318  TRP A CD2   1 
ATOM   2393 N  NE1   . TRP A 1 332 ? -10.415 31.147 -15.186 1.00 23.75  ? 318  TRP A NE1   1 
ATOM   2394 C  CE2   . TRP A 1 332 ? -10.129 31.987 -14.139 1.00 23.56  ? 318  TRP A CE2   1 
ATOM   2395 C  CE3   . TRP A 1 332 ? -11.324 33.525 -12.688 1.00 23.28  ? 318  TRP A CE3   1 
ATOM   2396 C  CZ2   . TRP A 1 332 ? -8.902  32.271 -13.518 1.00 24.42  ? 318  TRP A CZ2   1 
ATOM   2397 C  CZ3   . TRP A 1 332 ? -10.109 33.792 -12.057 1.00 23.36  ? 318  TRP A CZ3   1 
ATOM   2398 C  CH2   . TRP A 1 332 ? -8.910  33.170 -12.486 1.00 24.44  ? 318  TRP A CH2   1 
ATOM   2399 N  N     . PHE A 1 333 ? -15.656 33.095 -11.897 1.00 23.44  ? 319  PHE A N     1 
ATOM   2400 C  CA    . PHE A 1 333 ? -16.704 33.931 -11.306 1.00 23.16  ? 319  PHE A CA    1 
ATOM   2401 C  C     . PHE A 1 333 ? -16.142 35.344 -11.199 1.00 22.62  ? 319  PHE A C     1 
ATOM   2402 O  O     . PHE A 1 333 ? -15.338 35.631 -10.306 1.00 22.15  ? 319  PHE A O     1 
ATOM   2403 C  CB    . PHE A 1 333 ? -17.137 33.391 -9.932  1.00 21.31  ? 319  PHE A CB    1 
ATOM   2404 C  CG    . PHE A 1 333 ? -17.525 31.935 -9.945  1.00 21.40  ? 319  PHE A CG    1 
ATOM   2405 C  CD1   . PHE A 1 333 ? -16.556 30.941 -9.877  1.00 22.24  ? 319  PHE A CD1   1 
ATOM   2406 C  CD2   . PHE A 1 333 ? -18.873 31.559 -10.026 1.00 21.73  ? 319  PHE A CD2   1 
ATOM   2407 C  CE1   . PHE A 1 333 ? -16.913 29.611 -9.916  1.00 22.30  ? 319  PHE A CE1   1 
ATOM   2408 C  CE2   . PHE A 1 333 ? -19.234 30.238 -10.055 1.00 22.82  ? 319  PHE A CE2   1 
ATOM   2409 C  CZ    . PHE A 1 333 ? -18.261 29.255 -10.001 1.00 23.17  ? 319  PHE A CZ    1 
ATOM   2410 N  N     . THR A 1 334 ? -16.573 36.234 -12.087 1.00 22.56  ? 320  THR A N     1 
ATOM   2411 C  CA    . THR A 1 334 ? -15.955 37.546 -12.203 1.00 22.05  ? 320  THR A CA    1 
ATOM   2412 C  C     . THR A 1 334 ? -16.803 38.627 -11.541 1.00 22.90  ? 320  THR A C     1 
ATOM   2413 O  O     . THR A 1 334 ? -18.019 38.488 -11.373 1.00 23.60  ? 320  THR A O     1 
ATOM   2414 C  CB    . THR A 1 334 ? -15.687 37.882 -13.670 1.00 22.16  ? 320  THR A CB    1 
ATOM   2415 O  OG1   . THR A 1 334 ? -16.924 38.076 -14.366 1.00 21.86  ? 320  THR A OG1   1 
ATOM   2416 C  CG2   . THR A 1 334 ? -14.936 36.730 -14.311 1.00 22.53  ? 320  THR A CG2   1 
ATOM   2417 N  N     . GLY A 1 335 ? -16.140 39.718 -11.167 1.00 23.01  ? 321  GLY A N     1 
ATOM   2418 C  CA    . GLY A 1 335 ? -16.794 40.729 -10.347 1.00 22.54  ? 321  GLY A CA    1 
ATOM   2419 C  C     . GLY A 1 335 ? -16.943 40.320 -8.897  1.00 25.24  ? 321  GLY A C     1 
ATOM   2420 O  O     . GLY A 1 335 ? -17.940 40.664 -8.255  1.00 25.51  ? 321  GLY A O     1 
ATOM   2421 N  N     . ILE A 1 336 ? -15.983 39.574 -8.364  1.00 22.80  ? 322  ILE A N     1 
ATOM   2422 C  CA    . ILE A 1 336 ? -15.965 39.216 -6.953  1.00 23.45  ? 322  ILE A CA    1 
ATOM   2423 C  C     . ILE A 1 336 ? -14.691 39.765 -6.324  1.00 24.19  ? 322  ILE A C     1 
ATOM   2424 O  O     . ILE A 1 336 ? -13.589 39.346 -6.698  1.00 23.35  ? 322  ILE A O     1 
ATOM   2425 C  CB    . ILE A 1 336 ? -16.070 37.697 -6.740  1.00 23.92  ? 322  ILE A CB    1 
ATOM   2426 C  CG1   . ILE A 1 336 ? -17.439 37.216 -7.221  1.00 25.62  ? 322  ILE A CG1   1 
ATOM   2427 C  CG2   . ILE A 1 336 ? -15.861 37.359 -5.263  1.00 24.50  ? 322  ILE A CG2   1 
ATOM   2428 C  CD1   . ILE A 1 336 ? -17.663 35.740 -7.099  1.00 23.55  ? 322  ILE A CD1   1 
ATOM   2429 N  N     . PRO A 1 337 ? -14.790 40.701 -5.376  1.00 24.35  ? 323  PRO A N     1 
ATOM   2430 C  CA    . PRO A 1 337 ? -13.592 41.184 -4.678  1.00 24.19  ? 323  PRO A CA    1 
ATOM   2431 C  C     . PRO A 1 337 ? -12.870 40.067 -3.944  1.00 24.23  ? 323  PRO A C     1 
ATOM   2432 O  O     . PRO A 1 337 ? -13.488 39.255 -3.257  1.00 23.79  ? 323  PRO A O     1 
ATOM   2433 C  CB    . PRO A 1 337 ? -14.150 42.219 -3.694  1.00 25.51  ? 323  PRO A CB    1 
ATOM   2434 C  CG    . PRO A 1 337 ? -15.415 42.689 -4.350  1.00 28.88  ? 323  PRO A CG    1 
ATOM   2435 C  CD    . PRO A 1 337 ? -15.993 41.466 -4.999  1.00 25.54  ? 323  PRO A CD    1 
ATOM   2436 N  N     . MET A 1 338 ? -11.537 40.091 -4.033  1.00 22.21  ? 324  MET A N     1 
ATOM   2437 C  CA    . MET A 1 338 ? -10.708 39.086 -3.378  1.00 22.39  ? 324  MET A CA    1 
ATOM   2438 C  C     . MET A 1 338 ? -11.013 38.966 -1.887  1.00 21.78  ? 324  MET A C     1 
ATOM   2439 O  O     . MET A 1 338 ? -11.007 37.862 -1.330  1.00 19.67  ? 324  MET A O     1 
ATOM   2440 C  CB    . MET A 1 338 ? -9.241  39.454 -3.590  1.00 21.46  ? 324  MET A CB    1 
ATOM   2441 C  CG    . MET A 1 338 ? -8.232  38.606 -2.854  1.00 24.34  ? 324  MET A CG    1 
ATOM   2442 S  SD    . MET A 1 338 ? -6.548  39.148 -3.278  1.00 27.20  ? 324  MET A SD    1 
ATOM   2443 C  CE    . MET A 1 338 ? -6.870  40.866 -3.482  1.00 24.09  ? 324  MET A CE    1 
ATOM   2444 N  N     . LEU A 1 339 ? -11.313 40.087 -1.231  1.00 25.43  ? 325  LEU A N     1 
ATOM   2445 C  CA    . LEU A 1 339 ? -11.655 40.042 0.189   1.00 25.16  ? 325  LEU A CA    1 
ATOM   2446 C  C     . LEU A 1 339 ? -12.866 39.150 0.443   1.00 23.53  ? 325  LEU A C     1 
ATOM   2447 O  O     . LEU A 1 339 ? -12.833 38.283 1.326   1.00 24.81  ? 325  LEU A O     1 
ATOM   2448 C  CB    . LEU A 1 339 ? -11.905 41.455 0.724   1.00 26.10  ? 325  LEU A CB    1 
ATOM   2449 C  CG    . LEU A 1 339 ? -12.484 41.465 2.146   1.00 29.92  ? 325  LEU A CG    1 
ATOM   2450 C  CD1   . LEU A 1 339 ? -11.490 40.879 3.153   1.00 29.58  ? 325  LEU A CD1   1 
ATOM   2451 C  CD2   . LEU A 1 339 ? -12.941 42.856 2.586   1.00 32.45  ? 325  LEU A CD2   1 
ATOM   2452 N  N     . GLN A 1 340 ? -13.956 39.362 -0.304  1.00 23.45  ? 326  GLN A N     1 
ATOM   2453 C  CA    . GLN A 1 340 ? -15.155 38.553 -0.081  1.00 25.16  ? 326  GLN A CA    1 
ATOM   2454 C  C     . GLN A 1 340 ? -14.946 37.113 -0.519  1.00 23.08  ? 326  GLN A C     1 
ATOM   2455 O  O     . GLN A 1 340 ? -15.503 36.193 0.086   1.00 23.87  ? 326  GLN A O     1 
ATOM   2456 C  CB    . GLN A 1 340 ? -16.384 39.140 -0.773  1.00 26.51  ? 326  GLN A CB    1 
ATOM   2457 C  CG    . GLN A 1 340 ? -16.684 40.605 -0.509  1.00 29.74  ? 326  GLN A CG    1 
ATOM   2458 C  CD    . GLN A 1 340 ? -18.031 41.009 -1.097  1.00 35.48  ? 326  GLN A CD    1 
ATOM   2459 O  OE1   . GLN A 1 340 ? -18.113 41.456 -2.245  1.00 36.41  ? 326  GLN A OE1   1 
ATOM   2460 N  NE2   . GLN A 1 340 ? -19.097 40.849 -0.314  1.00 36.14  ? 326  GLN A NE2   1 
ATOM   2461 N  N     . ALA A 1 341 ? -14.180 36.890 -1.589  1.00 23.70  ? 327  ALA A N     1 
ATOM   2462 C  CA    . ALA A 1 341 ? -13.847 35.515 -1.946  1.00 21.52  ? 327  ALA A CA    1 
ATOM   2463 C  C     . ALA A 1 341 ? -13.134 34.817 -0.795  1.00 22.12  ? 327  ALA A C     1 
ATOM   2464 O  O     . ALA A 1 341 ? -13.423 33.653 -0.496  1.00 21.24  ? 327  ALA A O     1 
ATOM   2465 C  CB    . ALA A 1 341 ? -12.994 35.476 -3.211  1.00 19.73  ? 327  ALA A CB    1 
ATOM   2466 N  N     . ILE A 1 342 ? -12.187 35.509 -0.150  1.00 23.17  ? 328  ILE A N     1 
ATOM   2467 C  CA    . ILE A 1 342 ? -11.463 34.937 0.988   1.00 22.71  ? 328  ILE A CA    1 
ATOM   2468 C  C     . ILE A 1 342 ? -12.402 34.689 2.172   1.00 24.29  ? 328  ILE A C     1 
ATOM   2469 O  O     . ILE A 1 342 ? -12.344 33.636 2.823   1.00 21.07  ? 328  ILE A O     1 
ATOM   2470 C  CB    . ILE A 1 342 ? -10.283 35.844 1.383   1.00 23.88  ? 328  ILE A CB    1 
ATOM   2471 C  CG1   . ILE A 1 342 ? -9.184  35.773 0.322   1.00 23.20  ? 328  ILE A CG1   1 
ATOM   2472 C  CG2   . ILE A 1 342 ? -9.737  35.445 2.754   1.00 21.05  ? 328  ILE A CG2   1 
ATOM   2473 C  CD1   . ILE A 1 342 ? -8.127  36.848 0.448   1.00 22.99  ? 328  ILE A CD1   1 
ATOM   2474 N  N     . GLU A 1 343 ? -13.256 35.665 2.494   1.00 24.44  ? 329  GLU A N     1 
ATOM   2475 C  CA    . GLU A 1 343 ? -14.200 35.475 3.594   1.00 23.67  ? 329  GLU A CA    1 
ATOM   2476 C  C     . GLU A 1 343 ? -15.056 34.239 3.362   1.00 24.68  ? 329  GLU A C     1 
ATOM   2477 O  O     . GLU A 1 343 ? -15.301 33.460 4.290   1.00 24.48  ? 329  GLU A O     1 
ATOM   2478 C  CB    . GLU A 1 343 ? -15.097 36.706 3.758   1.00 23.88  ? 329  GLU A CB    1 
ATOM   2479 C  CG    . GLU A 1 343 ? -14.374 37.983 4.134   1.00 27.41  ? 329  GLU A CG    1 
ATOM   2480 C  CD    . GLU A 1 343 ? -15.325 39.159 4.347   1.00 30.79  ? 329  GLU A CD    1 
ATOM   2481 O  OE1   . GLU A 1 343 ? -16.300 39.309 3.577   1.00 32.31  ? 329  GLU A OE1   1 
ATOM   2482 O  OE2   . GLU A 1 343 ? -15.097 39.938 5.299   1.00 33.79  ? 329  GLU A OE2   1 
ATOM   2483 N  N     . THR A 1 344 ? -15.535 34.060 2.130   1.00 23.18  ? 330  THR A N     1 
ATOM   2484 C  CA    . THR A 1 344 ? -16.327 32.886 1.779   1.00 22.16  ? 330  THR A CA    1 
ATOM   2485 C  C     . THR A 1 344 ? -15.548 31.595 2.016   1.00 23.08  ? 330  THR A C     1 
ATOM   2486 O  O     . THR A 1 344 ? -16.076 30.633 2.585   1.00 24.35  ? 330  THR A O     1 
ATOM   2487 C  CB    . THR A 1 344 ? -16.754 32.976 0.314   1.00 23.56  ? 330  THR A CB    1 
ATOM   2488 O  OG1   . THR A 1 344 ? -17.606 34.114 0.138   1.00 24.04  ? 330  THR A OG1   1 
ATOM   2489 C  CG2   . THR A 1 344 ? -17.492 31.722 -0.082  1.00 24.28  ? 330  THR A CG2   1 
ATOM   2490 N  N     . LEU A 1 345 ? -14.303 31.537 1.531   1.00 23.48  ? 331  LEU A N     1 
ATOM   2491 C  CA    . LEU A 1 345 ? -13.516 30.315 1.663   1.00 23.74  ? 331  LEU A CA    1 
ATOM   2492 C  C     . LEU A 1 345 ? -13.128 30.042 3.111   1.00 22.91  ? 331  LEU A C     1 
ATOM   2493 O  O     . LEU A 1 345 ? -13.030 28.877 3.509   1.00 22.18  ? 331  LEU A O     1 
ATOM   2494 C  CB    . LEU A 1 345 ? -12.269 30.397 0.792   1.00 20.05  ? 331  LEU A CB    1 
ATOM   2495 C  CG    . LEU A 1 345 ? -12.492 30.318 -0.719  1.00 22.90  ? 331  LEU A CG    1 
ATOM   2496 C  CD1   . LEU A 1 345 ? -11.165 30.582 -1.451  1.00 20.27  ? 331  LEU A CD1   1 
ATOM   2497 C  CD2   . LEU A 1 345 ? -13.095 28.984 -1.138  1.00 20.92  ? 331  LEU A CD2   1 
ATOM   2498 N  N     . VAL A 1 346 ? -12.908 31.087 3.914   1.00 23.69  ? 332  VAL A N     1 
ATOM   2499 C  CA    . VAL A 1 346 ? -12.625 30.872 5.336   1.00 25.72  ? 332  VAL A CA    1 
ATOM   2500 C  C     . VAL A 1 346 ? -13.801 30.168 5.995   1.00 26.14  ? 332  VAL A C     1 
ATOM   2501 O  O     . VAL A 1 346 ? -13.634 29.184 6.728   1.00 26.11  ? 332  VAL A O     1 
ATOM   2502 C  CB    . VAL A 1 346 ? -12.299 32.204 6.040   1.00 26.93  ? 332  VAL A CB    1 
ATOM   2503 C  CG1   . VAL A 1 346 ? -12.225 32.002 7.541   1.00 27.81  ? 332  VAL A CG1   1 
ATOM   2504 C  CG2   . VAL A 1 346 ? -10.978 32.756 5.545   1.00 24.50  ? 332  VAL A CG2   1 
ATOM   2505 N  N     . GLU A 1 347 ? -15.016 30.644 5.714   1.00 28.20  ? 333  GLU A N     1 
ATOM   2506 C  CA    . GLU A 1 347 ? -16.209 30.006 6.267   1.00 30.51  ? 333  GLU A CA    1 
ATOM   2507 C  C     . GLU A 1 347 ? -16.315 28.547 5.834   1.00 28.13  ? 333  GLU A C     1 
ATOM   2508 O  O     . GLU A 1 347 ? -16.503 27.650 6.667   1.00 27.11  ? 333  GLU A O     1 
ATOM   2509 C  CB    . GLU A 1 347 ? -17.449 30.790 5.827   1.00 34.70  ? 333  GLU A CB    1 
ATOM   2510 C  CG    . GLU A 1 347 ? -18.596 30.774 6.785   1.00 42.44  ? 333  GLU A CG    1 
ATOM   2511 C  CD    . GLU A 1 347 ? -18.141 30.750 8.242   1.00 65.64  ? 333  GLU A CD    1 
ATOM   2512 O  OE1   . GLU A 1 347 ? -18.649 29.896 9.011   1.00 56.03  ? 333  GLU A OE1   1 
ATOM   2513 O  OE2   . GLU A 1 347 ? -17.290 31.594 8.625   1.00 50.37  ? 333  GLU A OE2   1 
ATOM   2514 N  N     . LEU A 1 348 ? -16.166 28.289 4.532   1.00 23.82  ? 334  LEU A N     1 
ATOM   2515 C  CA    . LEU A 1 348 ? -16.291 26.924 4.028   1.00 24.97  ? 334  LEU A CA    1 
ATOM   2516 C  C     . LEU A 1 348 ? -15.196 26.018 4.587   1.00 24.95  ? 334  LEU A C     1 
ATOM   2517 O  O     . LEU A 1 348 ? -15.421 24.823 4.804   1.00 24.79  ? 334  LEU A O     1 
ATOM   2518 C  CB    . LEU A 1 348 ? -16.275 26.925 2.498   1.00 22.25  ? 334  LEU A CB    1 
ATOM   2519 C  CG    . LEU A 1 348 ? -17.454 27.615 1.818   1.00 22.47  ? 334  LEU A CG    1 
ATOM   2520 C  CD1   . LEU A 1 348 ? -17.197 27.764 0.311   1.00 24.14  ? 334  LEU A CD1   1 
ATOM   2521 C  CD2   . LEU A 1 348 ? -18.758 26.866 2.071   1.00 28.55  ? 334  LEU A CD2   1 
ATOM   2522 N  N     . CYS A 1 349 ? -13.980 26.545 4.754   1.00 23.58  ? 335  CYS A N     1 
ATOM   2523 C  CA    . CYS A 1 349 ? -12.921 25.732 5.338   1.00 24.66  ? 335  CYS A CA    1 
ATOM   2524 C  C     . CYS A 1 349 ? -13.231 25.394 6.790   1.00 26.04  ? 335  CYS A C     1 
ATOM   2525 O  O     . CYS A 1 349 ? -13.024 24.253 7.228   1.00 25.03  ? 335  CYS A O     1 
ATOM   2526 C  CB    . CYS A 1 349 ? -11.587 26.465 5.218   1.00 23.90  ? 335  CYS A CB    1 
ATOM   2527 S  SG    . CYS A 1 349 ? -10.901 26.336 3.566   1.00 23.53  ? 335  CYS A SG    1 
ATOM   2528 N  N     . LYS A 1 350 ? -13.759 26.366 7.545   1.00 24.93  ? 336  LYS A N     1 
ATOM   2529 C  CA    . LYS A 1 350 ? -14.145 26.096 8.929   1.00 27.65  ? 336  LYS A CA    1 
ATOM   2530 C  C     . LYS A 1 350 ? -15.184 24.983 8.996   1.00 26.66  ? 336  LYS A C     1 
ATOM   2531 O  O     . LYS A 1 350 ? -15.213 24.212 9.966   1.00 26.98  ? 336  LYS A O     1 
ATOM   2532 C  CB    . LYS A 1 350 ? -14.673 27.379 9.576   1.00 28.38  ? 336  LYS A CB    1 
ATOM   2533 C  CG    . LYS A 1 350 ? -15.250 27.269 10.995  1.00 32.61  ? 336  LYS A CG    1 
ATOM   2534 C  CD    . LYS A 1 350 ? -14.226 27.655 12.076  1.00 36.28  ? 336  LYS A CD    1 
ATOM   2535 C  CE    . LYS A 1 350 ? -14.647 27.195 13.489  1.00 38.30  ? 336  LYS A CE    1 
ATOM   2536 N  NZ    . LYS A 1 350 ? -13.924 26.001 14.013  1.00 37.30  ? 336  LYS A NZ    1 
ATOM   2537 N  N     . GLN A 1 351 ? -15.972 24.816 7.929   1.00 26.11  ? 337  GLN A N     1 
ATOM   2538 C  CA    . GLN A 1 351 ? -16.984 23.768 7.903   1.00 26.95  ? 337  GLN A CA    1 
ATOM   2539 C  C     . GLN A 1 351 ? -16.454 22.408 7.482   1.00 27.53  ? 337  GLN A C     1 
ATOM   2540 O  O     . GLN A 1 351 ? -16.812 21.392 8.091   1.00 26.54  ? 337  GLN A O     1 
ATOM   2541 C  CB    . GLN A 1 351 ? -18.082 24.134 6.911   1.00 26.80  ? 337  GLN A CB    1 
ATOM   2542 C  CG    . GLN A 1 351 ? -19.347 23.397 7.151   1.00 24.59  ? 337  GLN A CG    1 
ATOM   2543 C  CD    . GLN A 1 351 ? -20.344 23.574 6.031   1.00 25.09  ? 337  GLN A CD    1 
ATOM   2544 O  OE1   . GLN A 1 351 ? -20.522 24.676 5.530   1.00 26.12  ? 337  GLN A OE1   1 
ATOM   2545 N  NE2   . GLN A 1 351 ? -21.055 22.512 5.693   1.00 22.83  ? 337  GLN A NE2   1 
ATOM   2546 N  N     . HIS A 1 352 ? -15.544 22.362 6.512   1.00 27.28  ? 338  HIS A N     1 
ATOM   2547 C  CA    . HIS A 1 352 ? -15.212 21.089 5.898   1.00 29.06  ? 338  HIS A CA    1 
ATOM   2548 C  C     . HIS A 1 352 ? -13.785 20.646 6.154   1.00 31.05  ? 338  HIS A C     1 
ATOM   2549 O  O     . HIS A 1 352 ? -13.497 19.454 6.003   1.00 32.35  ? 338  HIS A O     1 
ATOM   2550 C  CB    . HIS A 1 352 ? -15.449 21.151 4.377   1.00 28.82  ? 338  HIS A CB    1 
ATOM   2551 C  CG    . HIS A 1 352 ? -16.877 21.408 3.991   1.00 27.76  ? 338  HIS A CG    1 
ATOM   2552 N  ND1   . HIS A 1 352 ? -17.861 20.448 4.106   1.00 27.16  ? 338  HIS A ND1   1 
ATOM   2553 C  CD2   . HIS A 1 352 ? -17.484 22.507 3.484   1.00 26.45  ? 338  HIS A CD2   1 
ATOM   2554 C  CE1   . HIS A 1 352 ? -19.014 20.946 3.697   1.00 25.95  ? 338  HIS A CE1   1 
ATOM   2555 N  NE2   . HIS A 1 352 ? -18.815 22.194 3.320   1.00 27.40  ? 338  HIS A NE2   1 
ATOM   2556 N  N     . VAL A 1 353 ? -12.907 21.553 6.570   1.00 29.06  ? 339  VAL A N     1 
ATOM   2557 C  CA    . VAL A 1 353 ? -11.483 21.259 6.747   1.00 30.79  ? 339  VAL A CA    1 
ATOM   2558 C  C     . VAL A 1 353 ? -11.252 21.011 8.235   1.00 31.93  ? 339  VAL A C     1 
ATOM   2559 O  O     . VAL A 1 353 ? -11.019 21.935 9.016   1.00 31.72  ? 339  VAL A O     1 
ATOM   2560 C  CB    . VAL A 1 353 ? -10.598 22.377 6.219   1.00 30.14  ? 339  VAL A CB    1 
ATOM   2561 C  CG1   . VAL A 1 353 ? -9.141  22.072 6.554   1.00 30.91  ? 339  VAL A CG1   1 
ATOM   2562 C  CG2   . VAL A 1 353 ? -10.799 22.527 4.723   1.00 27.62  ? 339  VAL A CG2   1 
ATOM   2563 N  N     . HIS A 1 354 ? -11.443 19.777 8.659   1.00 30.88  ? 340  HIS A N     1 
ATOM   2564 C  CA    . HIS A 1 354 ? -11.231 19.418 10.055  1.00 34.44  ? 340  HIS A CA    1 
ATOM   2565 C  C     . HIS A 1 354 ? -9.949  18.581 10.083  1.00 36.40  ? 340  HIS A C     1 
ATOM   2566 O  O     . HIS A 1 354 ? -9.999  17.350 10.087  1.00 36.85  ? 340  HIS A O     1 
ATOM   2567 C  CB    . HIS A 1 354 ? -12.448 18.700 10.576  1.00 33.11  ? 340  HIS A CB    1 
ATOM   2568 C  CG    . HIS A 1 354 ? -13.619 19.609 10.787  1.00 33.68  ? 340  HIS A CG    1 
ATOM   2569 N  ND1   . HIS A 1 354 ? -13.982 20.086 12.029  1.00 33.97  ? 340  HIS A ND1   1 
ATOM   2570 C  CD2   . HIS A 1 354 ? -14.464 20.188 9.901   1.00 31.52  ? 340  HIS A CD2   1 
ATOM   2571 C  CE1   . HIS A 1 354 ? -15.028 20.882 11.905  1.00 34.41  ? 340  HIS A CE1   1 
ATOM   2572 N  NE2   . HIS A 1 354 ? -15.338 20.965 10.624  1.00 32.73  ? 340  HIS A NE2   1 
ATOM   2573 N  N     . ASP A 1 355 ? -8.799  19.251 10.166  1.00 36.88  ? 341  ASP A N     1 
ATOM   2574 C  CA    . ASP A 1 355 ? -7.523  18.550 10.209  1.00 37.66  ? 341  ASP A CA    1 
ATOM   2575 C  C     . ASP A 1 355 ? -6.696  18.968 11.408  1.00 40.66  ? 341  ASP A C     1 
ATOM   2576 O  O     . ASP A 1 355 ? -6.919  20.010 12.033  1.00 40.06  ? 341  ASP A O     1 
ATOM   2577 C  CB    . ASP A 1 355 ? -6.639  18.810 8.974   1.00 37.27  ? 341  ASP A CB    1 
ATOM   2578 C  CG    . ASP A 1 355 ? -7.372  18.670 7.667   1.00 37.62  ? 341  ASP A CG    1 
ATOM   2579 O  OD1   . ASP A 1 355 ? -8.152  17.701 7.515   1.00 36.90  ? 341  ASP A OD1   1 
ATOM   2580 O  OD2   . ASP A 1 355 ? -7.120  19.521 6.777   1.00 34.30  ? 341  ASP A OD2   1 
ATOM   2581 N  N     . THR A 1 356 ? -5.661  18.165 11.628  1.00 40.15  ? 342  THR A N     1 
ATOM   2582 C  CA    . THR A 1 356 ? -4.570  18.478 12.544  1.00 45.97  ? 342  THR A CA    1 
ATOM   2583 C  C     . THR A 1 356 ? -3.345  18.138 11.714  1.00 46.32  ? 342  THR A C     1 
ATOM   2584 O  O     . THR A 1 356 ? -3.011  16.952 11.537  1.00 47.98  ? 342  THR A O     1 
ATOM   2585 C  CB    . THR A 1 356 ? -4.610  17.683 13.848  1.00 45.35  ? 342  THR A CB    1 
ATOM   2586 O  OG1   . THR A 1 356 ? -4.657  16.279 13.559  1.00 55.27  ? 342  THR A OG1   1 
ATOM   2587 C  CG2   . THR A 1 356 ? -5.787  18.088 14.713  1.00 41.58  ? 342  THR A CG2   1 
ATOM   2588 N  N     . PRO A 1 357 ? -2.659  19.145 11.189  1.00 45.69  ? 343  PRO A N     1 
ATOM   2589 C  CA    . PRO A 1 357 ? -1.547  18.885 10.274  1.00 47.66  ? 343  PRO A CA    1 
ATOM   2590 C  C     . PRO A 1 357 ? -0.425  18.131 10.965  1.00 48.44  ? 343  PRO A C     1 
ATOM   2591 O  O     . PRO A 1 357 ? 0.039   18.514 12.044  1.00 46.97  ? 343  PRO A O     1 
ATOM   2592 C  CB    . PRO A 1 357 ? -1.126  20.294 9.848   1.00 43.27  ? 343  PRO A CB    1 
ATOM   2593 C  CG    . PRO A 1 357 ? -2.461  21.023 9.833   1.00 39.16  ? 343  PRO A CG    1 
ATOM   2594 C  CD    . PRO A 1 357 ? -3.101  20.549 11.115  1.00 41.31  ? 343  PRO A CD    1 
ATOM   2595 N  N     . VAL A 1 358 ? -0.015  17.033 10.339  1.00 50.09  ? 344  VAL A N     1 
ATOM   2596 C  CA    . VAL A 1 358 ? 1.118   16.261 10.851  1.00 55.58  ? 344  VAL A CA    1 
ATOM   2597 C  C     . VAL A 1 358 ? 2.336   17.170 10.908  1.00 53.08  ? 344  VAL A C     1 
ATOM   2598 O  O     . VAL A 1 358 ? 2.683   17.803 9.893   1.00 50.89  ? 344  VAL A O     1 
ATOM   2599 C  CB    . VAL A 1 358 ? 1.381   15.034 9.958   1.00 61.46  ? 344  VAL A CB    1 
ATOM   2600 C  CG1   . VAL A 1 358 ? 2.626   14.292 10.418  1.00 65.96  ? 344  VAL A CG1   1 
ATOM   2601 C  CG2   . VAL A 1 358 ? 0.169   14.104 9.963   1.00 59.55  ? 344  VAL A CG2   1 
ATOM   2602 N  N     . PRO A 1 359 ? 3.009   17.299 12.058  1.00 55.03  ? 345  PRO A N     1 
ATOM   2603 C  CA    . PRO A 1 359 ? 4.084   18.283 12.170  1.00 55.08  ? 345  PRO A CA    1 
ATOM   2604 C  C     . PRO A 1 359 ? 5.415   17.755 11.655  1.00 53.36  ? 345  PRO A C     1 
ATOM   2605 O  O     . PRO A 1 359 ? 6.113   18.531 11.008  1.00 52.11  ? 345  PRO A O     1 
ATOM   2606 C  CB    . PRO A 1 359 ? 4.135   18.551 13.669  1.00 57.53  ? 345  PRO A CB    1 
ATOM   2607 C  CG    . PRO A 1 359 ? 3.812   17.213 14.271  1.00 56.92  ? 345  PRO A CG    1 
ATOM   2608 C  CD    . PRO A 1 359 ? 2.863   16.512 13.296  1.00 56.17  ? 345  PRO A CD    1 
ATOM   2609 N  N     . PRO A 1 370 ? 27.929  24.964 12.867  1.00 83.29  ? 356  PRO A N     1 
ATOM   2610 C  CA    . PRO A 1 370 ? 28.973  25.910 12.459  1.00 83.41  ? 356  PRO A CA    1 
ATOM   2611 C  C     . PRO A 1 370 ? 30.316  25.264 12.097  1.00 84.98  ? 356  PRO A C     1 
ATOM   2612 O  O     . PRO A 1 370 ? 30.990  24.634 12.916  1.00 84.93  ? 356  PRO A O     1 
ATOM   2613 C  CB    . PRO A 1 370 ? 29.104  26.833 13.682  1.00 86.75  ? 356  PRO A CB    1 
ATOM   2614 C  CG    . PRO A 1 370 ? 28.339  26.145 14.796  1.00 87.18  ? 356  PRO A CG    1 
ATOM   2615 C  CD    . PRO A 1 370 ? 27.255  25.403 14.098  1.00 81.22  ? 356  PRO A CD    1 
ATOM   2616 N  N     . ASP A 1 371 ? 30.671  25.444 10.826  1.00 83.52  ? 357  ASP A N     1 
ATOM   2617 C  CA    . ASP A 1 371 ? 31.814  24.836 10.150  1.00 78.45  ? 357  ASP A CA    1 
ATOM   2618 C  C     . ASP A 1 371 ? 33.047  25.710 10.297  1.00 70.07  ? 357  ASP A C     1 
ATOM   2619 O  O     . ASP A 1 371 ? 33.259  26.333 11.342  1.00 68.27  ? 357  ASP A O     1 
ATOM   2620 C  CB    . ASP A 1 371 ? 31.535  24.573 8.665   1.00 76.74  ? 357  ASP A CB    1 
ATOM   2621 C  CG    . ASP A 1 371 ? 30.284  23.747 8.435   1.00 82.06  ? 357  ASP A CG    1 
ATOM   2622 O  OD1   . ASP A 1 371 ? 29.217  24.103 8.984   1.00 83.84  ? 357  ASP A OD1   1 
ATOM   2623 O  OD2   . ASP A 1 371 ? 30.385  22.729 7.709   1.00 76.77  ? 357  ASP A OD2   1 
ATOM   2624 N  N     . GLY A 1 372 ? 33.942  25.613 9.316   1.00 64.28  ? 358  GLY A N     1 
ATOM   2625 C  CA    . GLY A 1 372 ? 34.989  26.565 9.068   1.00 51.64  ? 358  GLY A CA    1 
ATOM   2626 C  C     . GLY A 1 372 ? 34.612  27.457 7.862   1.00 47.89  ? 358  GLY A C     1 
ATOM   2627 O  O     . GLY A 1 372 ? 33.905  28.456 8.033   1.00 46.09  ? 358  GLY A O     1 
ATOM   2628 N  N     . SER A 1 373 ? 35.098  27.097 6.686   1.00 44.60  ? 359  SER A N     1 
ATOM   2629 C  CA    . SER A 1 373 ? 35.005  27.978 5.519   1.00 43.33  ? 359  SER A CA    1 
ATOM   2630 C  C     . SER A 1 373 ? 33.562  28.234 5.073   1.00 42.41  ? 359  SER A C     1 
ATOM   2631 O  O     . SER A 1 373 ? 32.702  27.348 5.131   1.00 41.92  ? 359  SER A O     1 
ATOM   2632 C  CB    . SER A 1 373 ? 35.826  27.364 4.381   1.00 45.26  ? 359  SER A CB    1 
ATOM   2633 O  OG    . SER A 1 373 ? 35.540  27.967 3.139   1.00 53.07  ? 359  SER A OG    1 
ATOM   2634 N  N     . LEU A 1 374 ? 33.300  29.465 4.619   1.00 38.63  ? 360  LEU A N     1 
ATOM   2635 C  CA    . LEU A 1 374 ? 31.941  29.867 4.270   1.00 37.88  ? 360  LEU A CA    1 
ATOM   2636 C  C     . LEU A 1 374 ? 31.486  29.206 2.977   1.00 38.66  ? 360  LEU A C     1 
ATOM   2637 O  O     . LEU A 1 374 ? 32.158  29.293 1.943   1.00 39.14  ? 360  LEU A O     1 
ATOM   2638 C  CB    . LEU A 1 374 ? 31.847  31.389 4.133   1.00 38.02  ? 360  LEU A CB    1 
ATOM   2639 C  CG    . LEU A 1 374 ? 31.477  32.188 5.385   1.00 34.64  ? 360  LEU A CG    1 
ATOM   2640 C  CD1   . LEU A 1 374 ? 31.684  33.692 5.176   1.00 31.13  ? 360  LEU A CD1   1 
ATOM   2641 C  CD2   . LEU A 1 374 ? 30.039  31.896 5.778   1.00 33.29  ? 360  LEU A CD2   1 
ATOM   2642 N  N     . THR A 1 375 ? 30.327  28.563 3.035   1.00 35.78  ? 361  THR A N     1 
ATOM   2643 C  CA    . THR A 1 375 ? 29.643  28.026 1.874   1.00 37.72  ? 361  THR A CA    1 
ATOM   2644 C  C     . THR A 1 375 ? 28.250  28.626 1.819   1.00 37.54  ? 361  THR A C     1 
ATOM   2645 O  O     . THR A 1 375 ? 27.780  29.247 2.774   1.00 35.11  ? 361  THR A O     1 
ATOM   2646 C  CB    . THR A 1 375 ? 29.515  26.503 1.941   1.00 36.68  ? 361  THR A CB    1 
ATOM   2647 O  OG1   . THR A 1 375 ? 28.764  26.154 3.108   1.00 34.75  ? 361  THR A OG1   1 
ATOM   2648 C  CG2   . THR A 1 375 ? 30.888  25.860 2.019   1.00 37.85  ? 361  THR A CG2   1 
ATOM   2649 N  N     . GLN A 1 376 ? 27.575  28.404 0.693   1.00 41.20  ? 362  GLN A N     1 
ATOM   2650 C  CA    . GLN A 1 376 ? 26.168  28.768 0.609   1.00 41.26  ? 362  GLN A CA    1 
ATOM   2651 C  C     . GLN A 1 376 ? 25.367  28.121 1.731   1.00 38.23  ? 362  GLN A C     1 
ATOM   2652 O  O     . GLN A 1 376 ? 24.558  28.775 2.400   1.00 35.22  ? 362  GLN A O     1 
ATOM   2653 C  CB    . GLN A 1 376 ? 25.599  28.348 -0.739  1.00 46.89  ? 362  GLN A CB    1 
ATOM   2654 C  CG    . GLN A 1 376 ? 25.974  29.266 -1.855  1.00 54.18  ? 362  GLN A CG    1 
ATOM   2655 C  CD    . GLN A 1 376 ? 25.102  30.479 -1.856  1.00 54.26  ? 362  GLN A CD    1 
ATOM   2656 O  OE1   . GLN A 1 376 ? 23.883  30.370 -1.812  1.00 53.39  ? 362  GLN A OE1   1 
ATOM   2657 N  NE2   . GLN A 1 376 ? 25.716  31.653 -1.942  1.00 51.81  ? 362  GLN A NE2   1 
ATOM   2658 N  N     . ASP A 1 377 ? 25.599  26.834 1.966   1.00 36.81  ? 363  ASP A N     1 
ATOM   2659 C  CA    . ASP A 1 377 ? 24.813  26.117 2.961   1.00 37.31  ? 363  ASP A CA    1 
ATOM   2660 C  C     . ASP A 1 377 ? 25.010  26.702 4.356   1.00 35.44  ? 363  ASP A C     1 
ATOM   2661 O  O     . ASP A 1 377 ? 24.036  27.040 5.040   1.00 35.77  ? 363  ASP A O     1 
ATOM   2662 C  CB    . ASP A 1 377 ? 25.173  24.633 2.928   1.00 39.42  ? 363  ASP A CB    1 
ATOM   2663 C  CG    . ASP A 1 377 ? 23.993  23.751 3.239   1.00 42.69  ? 363  ASP A CG    1 
ATOM   2664 O  OD1   . ASP A 1 377 ? 23.033  23.746 2.436   1.00 44.81  ? 363  ASP A OD1   1 
ATOM   2665 O  OD2   . ASP A 1 377 ? 24.028  23.059 4.274   1.00 46.12  ? 363  ASP A OD2   1 
ATOM   2666 N  N     . ASN A 1 378 ? 26.261  26.838 4.802   1.00 34.90  ? 364  ASN A N     1 
ATOM   2667 C  CA    . ASN A 1 378 ? 26.441  27.313 6.172   1.00 35.36  ? 364  ASN A CA    1 
ATOM   2668 C  C     . ASN A 1 378 ? 26.192  28.811 6.299   1.00 32.85  ? 364  ASN A C     1 
ATOM   2669 O  O     . ASN A 1 378 ? 25.965  29.287 7.414   1.00 30.60  ? 364  ASN A O     1 
ATOM   2670 C  CB    . ASN A 1 378 ? 27.823  26.916 6.739   1.00 36.14  ? 364  ASN A CB    1 
ATOM   2671 C  CG    . ASN A 1 378 ? 29.003  27.554 6.011   1.00 38.18  ? 364  ASN A CG    1 
ATOM   2672 O  OD1   . ASN A 1 378 ? 28.890  28.604 5.384   1.00 35.86  ? 364  ASN A OD1   1 
ATOM   2673 N  ND2   . ASN A 1 378 ? 30.164  26.909 6.118   1.00 42.79  ? 364  ASN A ND2   1 
ATOM   2674 N  N     . PHE A 1 379 ? 26.189  29.560 5.187   1.00 32.71  ? 365  PHE A N     1 
ATOM   2675 C  CA    . PHE A 1 379 ? 25.784  30.960 5.271   1.00 31.33  ? 365  PHE A CA    1 
ATOM   2676 C  C     . PHE A 1 379 ? 24.317  31.085 5.665   1.00 30.18  ? 365  PHE A C     1 
ATOM   2677 O  O     . PHE A 1 379 ? 23.975  31.815 6.604   1.00 29.21  ? 365  PHE A O     1 
ATOM   2678 C  CB    . PHE A 1 379 ? 26.024  31.690 3.951   1.00 30.57  ? 365  PHE A CB    1 
ATOM   2679 C  CG    . PHE A 1 379 ? 25.384  33.051 3.912   1.00 30.00  ? 365  PHE A CG    1 
ATOM   2680 C  CD1   . PHE A 1 379 ? 26.031  34.149 4.460   1.00 27.70  ? 365  PHE A CD1   1 
ATOM   2681 C  CD2   . PHE A 1 379 ? 24.114  33.226 3.369   1.00 28.83  ? 365  PHE A CD2   1 
ATOM   2682 C  CE1   . PHE A 1 379 ? 25.435  35.403 4.440   1.00 25.83  ? 365  PHE A CE1   1 
ATOM   2683 C  CE2   . PHE A 1 379 ? 23.509  34.471 3.356   1.00 27.39  ? 365  PHE A CE2   1 
ATOM   2684 C  CZ    . PHE A 1 379 ? 24.170  35.565 3.896   1.00 25.91  ? 365  PHE A CZ    1 
ATOM   2685 N  N     . TRP A 1 380 ? 23.428  30.392 4.944   1.00 28.77  ? 366  TRP A N     1 
ATOM   2686 C  CA    . TRP A 1 380 ? 22.004  30.496 5.250   1.00 30.01  ? 366  TRP A CA    1 
ATOM   2687 C  C     . TRP A 1 380 ? 21.669  29.887 6.600   1.00 30.04  ? 366  TRP A C     1 
ATOM   2688 O  O     . TRP A 1 380 ? 20.787  30.396 7.300   1.00 29.02  ? 366  TRP A O     1 
ATOM   2689 C  CB    . TRP A 1 380 ? 21.171  29.862 4.132   1.00 29.05  ? 366  TRP A CB    1 
ATOM   2690 C  CG    . TRP A 1 380 ? 21.368  30.621 2.866   1.00 29.57  ? 366  TRP A CG    1 
ATOM   2691 C  CD1   . TRP A 1 380 ? 22.053  30.215 1.757   1.00 30.86  ? 366  TRP A CD1   1 
ATOM   2692 C  CD2   . TRP A 1 380 ? 20.931  31.959 2.600   1.00 29.48  ? 366  TRP A CD2   1 
ATOM   2693 N  NE1   . TRP A 1 380 ? 22.059  31.212 0.813   1.00 31.58  ? 366  TRP A NE1   1 
ATOM   2694 C  CE2   . TRP A 1 380 ? 21.371  32.291 1.302   1.00 30.93  ? 366  TRP A CE2   1 
ATOM   2695 C  CE3   . TRP A 1 380 ? 20.201  32.904 3.329   1.00 26.45  ? 366  TRP A CE3   1 
ATOM   2696 C  CZ2   . TRP A 1 380 ? 21.105  33.525 0.719   1.00 29.63  ? 366  TRP A CZ2   1 
ATOM   2697 C  CZ3   . TRP A 1 380 ? 19.941  34.126 2.753   1.00 26.34  ? 366  TRP A CZ3   1 
ATOM   2698 C  CH2   . TRP A 1 380 ? 20.393  34.429 1.459   1.00 27.72  ? 366  TRP A CH2   1 
ATOM   2699 N  N     . LYS A 1 381 ? 22.372  28.822 6.992   1.00 30.58  ? 367  LYS A N     1 
ATOM   2700 C  CA    . LYS A 1 381 ? 22.170  28.263 8.322   1.00 32.83  ? 367  LYS A CA    1 
ATOM   2701 C  C     . LYS A 1 381 ? 22.564  29.270 9.391   1.00 31.64  ? 367  LYS A C     1 
ATOM   2702 O  O     . LYS A 1 381 ? 21.904  29.370 10.430  1.00 32.25  ? 367  LYS A O     1 
ATOM   2703 C  CB    . LYS A 1 381 ? 22.975  26.975 8.475   1.00 34.67  ? 367  LYS A CB    1 
ATOM   2704 C  CG    . LYS A 1 381 ? 22.168  25.712 8.290   1.00 38.45  ? 367  LYS A CG    1 
ATOM   2705 C  CD    . LYS A 1 381 ? 23.088  24.597 7.819   1.00 41.11  ? 367  LYS A CD    1 
ATOM   2706 C  CE    . LYS A 1 381 ? 22.372  23.629 6.889   1.00 42.74  ? 367  LYS A CE    1 
ATOM   2707 N  NZ    . LYS A 1 381 ? 23.143  22.355 6.810   1.00 42.44  ? 367  LYS A NZ    1 
ATOM   2708 N  N     . THR A 1 382 ? 23.640  30.024 9.157   1.00 29.47  ? 368  THR A N     1 
ATOM   2709 C  CA    . THR A 1 382 ? 24.034  31.043 10.124  1.00 32.78  ? 368  THR A CA    1 
ATOM   2710 C  C     . THR A 1 382 ? 22.988  32.143 10.202  1.00 30.10  ? 368  THR A C     1 
ATOM   2711 O  O     . THR A 1 382 ? 22.609  32.571 11.298  1.00 31.15  ? 368  THR A O     1 
ATOM   2712 C  CB    . THR A 1 382 ? 25.404  31.637 9.761   1.00 33.37  ? 368  THR A CB    1 
ATOM   2713 O  OG1   . THR A 1 382 ? 26.378  30.593 9.627   1.00 34.26  ? 368  THR A OG1   1 
ATOM   2714 C  CG2   . THR A 1 382 ? 25.875  32.625 10.820  1.00 29.18  ? 368  THR A CG2   1 
ATOM   2715 N  N     . LEU A 1 383 ? 22.485  32.591 9.051   1.00 27.63  ? 369  LEU A N     1 
ATOM   2716 C  CA    . LEU A 1 383 ? 21.488  33.655 9.050   1.00 27.69  ? 369  LEU A CA    1 
ATOM   2717 C  C     . LEU A 1 383 ? 20.165  33.180 9.654   1.00 28.85  ? 369  LEU A C     1 
ATOM   2718 O  O     . LEU A 1 383 ? 19.479  33.942 10.345  1.00 28.10  ? 369  LEU A O     1 
ATOM   2719 C  CB    . LEU A 1 383 ? 21.303  34.169 7.625   1.00 27.52  ? 369  LEU A CB    1 
ATOM   2720 C  CG    . LEU A 1 383 ? 20.621  35.529 7.490   1.00 28.35  ? 369  LEU A CG    1 
ATOM   2721 C  CD1   . LEU A 1 383 ? 21.479  36.597 8.126   1.00 28.70  ? 369  LEU A CD1   1 
ATOM   2722 C  CD2   . LEU A 1 383 ? 20.376  35.863 6.027   1.00 29.25  ? 369  LEU A CD2   1 
ATOM   2723 N  N     . GLN A 1 384 ? 19.804  31.917 9.423   1.00 26.97  ? 370  GLN A N     1 
ATOM   2724 C  CA    . GLN A 1 384 ? 18.582  31.372 10.004  1.00 27.45  ? 370  GLN A CA    1 
ATOM   2725 C  C     . GLN A 1 384 ? 18.548  31.554 11.520  1.00 29.07  ? 370  GLN A C     1 
ATOM   2726 O  O     . GLN A 1 384 ? 17.506  31.902 12.087  1.00 28.70  ? 370  GLN A O     1 
ATOM   2727 C  CB    . GLN A 1 384 ? 18.460  29.890 9.643   1.00 27.29  ? 370  GLN A CB    1 
ATOM   2728 C  CG    . GLN A 1 384 ? 17.258  29.194 10.241  1.00 26.07  ? 370  GLN A CG    1 
ATOM   2729 C  CD    . GLN A 1 384 ? 15.955  29.824 9.794   1.00 28.13  ? 370  GLN A CD    1 
ATOM   2730 O  OE1   . GLN A 1 384 ? 15.679  29.913 8.593   1.00 28.25  ? 370  GLN A OE1   1 
ATOM   2731 N  NE2   . GLN A 1 384 ? 15.155  30.279 10.749  1.00 26.80  ? 370  GLN A NE2   1 
ATOM   2732 N  N     . THR A 1 385 ? 19.675  31.315 12.198  1.00 27.93  ? 371  THR A N     1 
ATOM   2733 C  CA    . THR A 1 385 ? 19.680  31.455 13.654  1.00 30.90  ? 371  THR A CA    1 
ATOM   2734 C  C     . THR A 1 385 ? 19.614  32.909 14.113  1.00 30.65  ? 371  THR A C     1 
ATOM   2735 O  O     . THR A 1 385 ? 19.244  33.162 15.265  1.00 31.01  ? 371  THR A O     1 
ATOM   2736 C  CB    . THR A 1 385 ? 20.916  30.780 14.256  1.00 31.31  ? 371  THR A CB    1 
ATOM   2737 O  OG1   . THR A 1 385 ? 22.047  31.636 14.090  1.00 34.51  ? 371  THR A OG1   1 
ATOM   2738 C  CG2   . THR A 1 385 ? 21.191  29.446 13.587  1.00 28.70  ? 371  THR A CG2   1 
ATOM   2739 N  N     . PHE A 1 386 ? 19.915  33.861 13.228  1.00 30.20  ? 372  PHE A N     1 
ATOM   2740 C  CA    . PHE A 1 386 ? 20.057  35.283 13.533  1.00 29.87  ? 372  PHE A CA    1 
ATOM   2741 C  C     . PHE A 1 386 ? 18.752  36.068 13.382  1.00 29.11  ? 372  PHE A C     1 
ATOM   2742 O  O     . PHE A 1 386 ? 18.505  37.011 14.146  1.00 28.20  ? 372  PHE A O     1 
ATOM   2743 C  CB    . PHE A 1 386 ? 21.133  35.888 12.618  1.00 30.41  ? 372  PHE A CB    1 
ATOM   2744 C  CG    . PHE A 1 386 ? 21.179  37.397 12.624  1.00 29.12  ? 372  PHE A CG    1 
ATOM   2745 C  CD1   . PHE A 1 386 ? 21.739  38.083 13.694  1.00 29.75  ? 372  PHE A CD1   1 
ATOM   2746 C  CD2   . PHE A 1 386 ? 20.673  38.126 11.554  1.00 27.64  ? 372  PHE A CD2   1 
ATOM   2747 C  CE1   . PHE A 1 386 ? 21.785  39.474 13.696  1.00 28.99  ? 372  PHE A CE1   1 
ATOM   2748 C  CE2   . PHE A 1 386 ? 20.719  39.507 11.551  1.00 26.04  ? 372  PHE A CE2   1 
ATOM   2749 C  CZ    . PHE A 1 386 ? 21.273  40.181 12.622  1.00 27.03  ? 372  PHE A CZ    1 
ATOM   2750 N  N     . ILE A 1 387 ? 17.925  35.728 12.389  1.00 26.23  ? 373  ILE A N     1 
ATOM   2751 C  CA    . ILE A 1 387 ? 16.710  36.516 12.147  1.00 27.19  ? 373  ILE A CA    1 
ATOM   2752 C  C     . ILE A 1 387 ? 15.755  36.409 13.336  1.00 26.48  ? 373  ILE A C     1 
ATOM   2753 O  O     . ILE A 1 387 ? 15.803  35.463 14.137  1.00 26.88  ? 373  ILE A O     1 
ATOM   2754 C  CB    . ILE A 1 387 ? 16.013  36.110 10.838  1.00 26.53  ? 373  ILE A CB    1 
ATOM   2755 C  CG1   . ILE A 1 387 ? 15.325  34.747 10.980  1.00 28.07  ? 373  ILE A CG1   1 
ATOM   2756 C  CG2   . ILE A 1 387 ? 16.994  36.143 9.673   1.00 23.46  ? 373  ILE A CG2   1 
ATOM   2757 C  CD1   . ILE A 1 387 ? 14.657  34.245 9.665   1.00 25.21  ? 373  ILE A CD1   1 
ATOM   2758 N  N     . ARG A 1 388 ? 14.914  37.427 13.475  1.00 26.28  ? 374  ARG A N     1 
ATOM   2759 C  CA    . ARG A 1 388 ? 14.053  37.585 14.637  1.00 26.26  ? 374  ARG A CA    1 
ATOM   2760 C  C     . ARG A 1 388 ? 12.734  38.198 14.196  1.00 26.68  ? 374  ARG A C     1 
ATOM   2761 O  O     . ARG A 1 388 ? 12.660  38.829 13.137  1.00 25.83  ? 374  ARG A O     1 
ATOM   2762 C  CB    . ARG A 1 388 ? 14.700  38.473 15.711  1.00 27.35  ? 374  ARG A CB    1 
ATOM   2763 C  CG    . ARG A 1 388 ? 15.956  37.874 16.385  1.00 28.14  ? 374  ARG A CG    1 
ATOM   2764 C  CD    . ARG A 1 388 ? 15.565  36.766 17.355  1.00 30.65  ? 374  ARG A CD    1 
ATOM   2765 N  NE    . ARG A 1 388 ? 16.697  36.291 18.151  1.00 27.60  ? 374  ARG A NE    1 
ATOM   2766 C  CZ    . ARG A 1 388 ? 17.664  35.519 17.673  1.00 31.48  ? 374  ARG A CZ    1 
ATOM   2767 N  NH1   . ARG A 1 388 ? 17.636  35.072 16.424  1.00 28.82  ? 374  ARG A NH1   1 
ATOM   2768 N  NH2   . ARG A 1 388 ? 18.673  35.172 18.467  1.00 31.25  ? 374  ARG A NH2   1 
ATOM   2769 N  N     . PRO A 1 389 ? 11.685  38.061 15.006  1.00 28.63  ? 375  PRO A N     1 
ATOM   2770 C  CA    . PRO A 1 389 ? 10.449  38.799 14.742  1.00 27.71  ? 375  PRO A CA    1 
ATOM   2771 C  C     . PRO A 1 389 ? 10.728  40.297 14.656  1.00 27.98  ? 375  PRO A C     1 
ATOM   2772 O  O     . PRO A 1 389 ? 11.613  40.829 15.330  1.00 26.92  ? 375  PRO A O     1 
ATOM   2773 C  CB    . PRO A 1 389 ? 9.575   38.458 15.959  1.00 31.45  ? 375  PRO A CB    1 
ATOM   2774 C  CG    . PRO A 1 389 ? 10.029  37.096 16.356  1.00 29.17  ? 375  PRO A CG    1 
ATOM   2775 C  CD    . PRO A 1 389 ? 11.535  37.109 16.127  1.00 29.09  ? 375  PRO A CD    1 
ATOM   2776 N  N     . GLY A 1 390 ? 9.984   40.974 13.778  1.00 27.07  ? 376  GLY A N     1 
ATOM   2777 C  CA    . GLY A 1 390 ? 10.201  42.380 13.512  1.00 25.59  ? 376  GLY A CA    1 
ATOM   2778 C  C     . GLY A 1 390 ? 11.169  42.672 12.381  1.00 24.55  ? 376  GLY A C     1 
ATOM   2779 O  O     . GLY A 1 390 ? 11.241  43.822 11.930  1.00 24.08  ? 376  GLY A O     1 
ATOM   2780 N  N     . ASP A 1 391 ? 11.920  41.678 11.913  1.00 23.71  ? 377  ASP A N     1 
ATOM   2781 C  CA    . ASP A 1 391 ? 12.910  41.911 10.871  1.00 23.70  ? 377  ASP A CA    1 
ATOM   2782 C  C     . ASP A 1 391 ? 12.238  42.315 9.563   1.00 23.08  ? 377  ASP A C     1 
ATOM   2783 O  O     . ASP A 1 391 ? 11.170  41.804 9.213   1.00 21.23  ? 377  ASP A O     1 
ATOM   2784 C  CB    . ASP A 1 391 ? 13.746  40.652 10.647  1.00 23.60  ? 377  ASP A CB    1 
ATOM   2785 C  CG    . ASP A 1 391 ? 14.892  40.514 11.666  1.00 25.22  ? 377  ASP A CG    1 
ATOM   2786 O  OD1   . ASP A 1 391 ? 15.158  41.482 12.409  1.00 23.68  ? 377  ASP A OD1   1 
ATOM   2787 O  OD2   . ASP A 1 391 ? 15.513  39.431 11.725  1.00 24.31  ? 377  ASP A OD2   1 
ATOM   2788 N  N     . ILE A 1 392 ? 12.882  43.227 8.839   1.00 21.65  ? 378  ILE A N     1 
ATOM   2789 C  CA    . ILE A 1 392 ? 12.608  43.470 7.426   1.00 21.45  ? 378  ILE A CA    1 
ATOM   2790 C  C     . ILE A 1 392 ? 13.774  42.890 6.639   1.00 21.03  ? 378  ILE A C     1 
ATOM   2791 O  O     . ILE A 1 392 ? 14.919  43.347 6.781   1.00 23.11  ? 378  ILE A O     1 
ATOM   2792 C  CB    . ILE A 1 392 ? 12.436  44.962 7.112   1.00 20.86  ? 378  ILE A CB    1 
ATOM   2793 C  CG1   . ILE A 1 392 ? 11.283  45.574 7.911   1.00 20.66  ? 378  ILE A CG1   1 
ATOM   2794 C  CG2   . ILE A 1 392 ? 12.252  45.172 5.575   1.00 20.39  ? 378  ILE A CG2   1 
ATOM   2795 C  CD1   . ILE A 1 392 ? 11.163  47.049 7.695   1.00 20.56  ? 378  ILE A CD1   1 
ATOM   2796 N  N     . ILE A 1 393 ? 13.492  41.892 5.809   1.00 21.47  ? 379  ILE A N     1 
ATOM   2797 C  CA    . ILE A 1 393 ? 14.528  41.153 5.097   1.00 20.74  ? 379  ILE A CA    1 
ATOM   2798 C  C     . ILE A 1 393 ? 14.329  41.378 3.609   1.00 21.21  ? 379  ILE A C     1 
ATOM   2799 O  O     . ILE A 1 393 ? 13.271  41.041 3.066   1.00 20.37  ? 379  ILE A O     1 
ATOM   2800 C  CB    . ILE A 1 393 ? 14.505  39.654 5.443   1.00 20.33  ? 379  ILE A CB    1 
ATOM   2801 C  CG1   . ILE A 1 393 ? 14.744  39.449 6.949   1.00 21.45  ? 379  ILE A CG1   1 
ATOM   2802 C  CG2   . ILE A 1 393 ? 15.545  38.886 4.608   1.00 18.21  ? 379  ILE A CG2   1 
ATOM   2803 C  CD1   . ILE A 1 393 ? 14.468  38.003 7.423   1.00 20.84  ? 379  ILE A CD1   1 
ATOM   2804 N  N     . LEU A 1 394 ? 15.349  41.940 2.947   1.00 19.48  ? 380  LEU A N     1 
ATOM   2805 C  CA    . LEU A 1 394 ? 15.306  42.171 1.508   1.00 18.97  ? 380  LEU A CA    1 
ATOM   2806 C  C     . LEU A 1 394 ? 16.409  41.373 0.835   1.00 19.90  ? 380  LEU A C     1 
ATOM   2807 O  O     . LEU A 1 394 ? 17.555  41.357 1.308   1.00 21.09  ? 380  LEU A O     1 
ATOM   2808 C  CB    . LEU A 1 394 ? 15.468  43.659 1.162   1.00 18.67  ? 380  LEU A CB    1 
ATOM   2809 C  CG    . LEU A 1 394 ? 14.485  44.627 1.824   1.00 20.57  ? 380  LEU A CG    1 
ATOM   2810 C  CD1   . LEU A 1 394 ? 15.017  45.117 3.173   1.00 18.61  ? 380  LEU A CD1   1 
ATOM   2811 C  CD2   . LEU A 1 394 ? 14.175  45.805 0.902   1.00 18.72  ? 380  LEU A CD2   1 
ATOM   2812 N  N     . ALA A 1 395 ? 16.070  40.730 -0.279  1.00 16.99  ? 381  ALA A N     1 
ATOM   2813 C  CA    . ALA A 1 395 ? 17.025  39.915 -1.018  1.00 21.94  ? 381  ALA A CA    1 
ATOM   2814 C  C     . ALA A 1 395 ? 16.921  40.218 -2.504  1.00 21.67  ? 381  ALA A C     1 
ATOM   2815 O  O     . ALA A 1 395 ? 15.815  40.366 -3.037  1.00 19.39  ? 381  ALA A O     1 
ATOM   2816 C  CB    . ALA A 1 395 ? 16.792  38.419 -0.779  1.00 23.56  ? 381  ALA A CB    1 
ATOM   2817 N  N     . ASP A 1 396 ? 18.073  40.322 -3.165  1.00 22.46  ? 382  ASP A N     1 
ATOM   2818 C  CA    . ASP A 1 396 ? 18.105  40.597 -4.595  1.00 21.84  ? 382  ASP A CA    1 
ATOM   2819 C  C     . ASP A 1 396 ? 18.154  39.304 -5.407  1.00 24.17  ? 382  ASP A C     1 
ATOM   2820 O  O     . ASP A 1 396 ? 18.324  38.205 -4.872  1.00 25.42  ? 382  ASP A O     1 
ATOM   2821 C  CB    . ASP A 1 396 ? 19.292  41.491 -4.963  1.00 19.92  ? 382  ASP A CB    1 
ATOM   2822 C  CG    . ASP A 1 396 ? 18.923  42.523 -6.012  1.00 19.85  ? 382  ASP A CG    1 
ATOM   2823 O  OD1   . ASP A 1 396 ? 18.232  42.136 -6.981  1.00 20.40  ? 382  ASP A OD1   1 
ATOM   2824 O  OD2   . ASP A 1 396 ? 19.316  43.705 -5.891  1.00 17.44  ? 382  ASP A OD2   1 
ATOM   2825 N  N     . GLN A 1 397 ? 17.966  39.451 -6.720  1.00 21.29  ? 383  GLN A N     1 
ATOM   2826 C  CA    . GLN A 1 397 ? 18.049  38.325 -7.638  1.00 24.38  ? 383  GLN A CA    1 
ATOM   2827 C  C     . GLN A 1 397 ? 19.502  37.887 -7.775  1.00 25.60  ? 383  GLN A C     1 
ATOM   2828 O  O     . GLN A 1 397 ? 20.418  38.696 -7.648  1.00 25.65  ? 383  GLN A O     1 
ATOM   2829 C  CB    . GLN A 1 397 ? 17.460  38.710 -8.998  1.00 24.97  ? 383  GLN A CB    1 
ATOM   2830 C  CG    . GLN A 1 397 ? 15.987  39.050 -8.911  1.00 22.18  ? 383  GLN A CG    1 
ATOM   2831 C  CD    . GLN A 1 397 ? 15.192  37.933 -8.263  1.00 25.47  ? 383  GLN A CD    1 
ATOM   2832 O  OE1   . GLN A 1 397 ? 15.061  36.850 -8.836  1.00 29.45  ? 383  GLN A OE1   1 
ATOM   2833 N  NE2   . GLN A 1 397 ? 14.685  38.177 -7.049  1.00 24.61  ? 383  GLN A NE2   1 
ATOM   2834 N  N     . GLY A 1 398 ? 19.695  36.597 -8.031  1.00 29.66  ? 384  GLY A N     1 
ATOM   2835 C  CA    . GLY A 1 398 ? 20.963  35.908 -7.896  1.00 35.11  ? 384  GLY A CA    1 
ATOM   2836 C  C     . GLY A 1 398 ? 20.892  34.863 -6.797  1.00 41.24  ? 384  GLY A C     1 
ATOM   2837 O  O     . GLY A 1 398 ? 19.817  34.431 -6.376  1.00 42.52  ? 384  GLY A O     1 
ATOM   2838 N  N     . THR A 1 399 ? 22.071  34.462 -6.312  1.00 44.86  ? 385  THR A N     1 
ATOM   2839 C  CA    . THR A 1 399 ? 22.220  33.524 -5.176  1.00 47.91  ? 385  THR A CA    1 
ATOM   2840 C  C     . THR A 1 399 ? 21.733  34.111 -3.804  1.00 43.88  ? 385  THR A C     1 
ATOM   2841 O  O     . THR A 1 399 ? 21.990  33.481 -2.767  1.00 45.55  ? 385  THR A O     1 
ATOM   2842 C  CB    . THR A 1 399 ? 23.666  33.068 -5.053  1.00 46.12  ? 385  THR A CB    1 
ATOM   2843 O  OG1   . THR A 1 399 ? 24.396  34.007 -4.248  1.00 41.05  ? 385  THR A OG1   1 
ATOM   2844 C  CG2   . THR A 1 399 ? 24.280  32.944 -6.431  1.00 54.35  ? 385  THR A CG2   1 
ATOM   2845 N  N     . SER A 1 400 ? 21.199  35.331 -3.752  1.00 40.98  ? 386  SER A N     1 
ATOM   2846 C  CA    . SER A 1 400 ? 20.604  35.886 -2.539  1.00 37.50  ? 386  SER A CA    1 
ATOM   2847 C  C     . SER A 1 400 ? 19.151  35.449 -2.339  1.00 39.14  ? 386  SER A C     1 
ATOM   2848 O  O     . SER A 1 400 ? 18.825  34.786 -1.353  1.00 36.65  ? 386  SER A O     1 
ATOM   2849 C  CB    . SER A 1 400 ? 20.680  37.412 -2.588  1.00 32.12  ? 386  SER A CB    1 
ATOM   2850 O  OG    . SER A 1 400 ? 21.841  37.878 -1.930  1.00 40.38  ? 386  SER A OG    1 
ATOM   2851 N  N     . ALA A 1 401 ? 18.265  35.823 -3.269  1.00 47.56  ? 387  ALA A N     1 
ATOM   2852 C  CA    . ALA A 1 401 ? 16.843  35.525 -3.105  1.00 40.22  ? 387  ALA A CA    1 
ATOM   2853 C  C     . ALA A 1 401 ? 16.602  34.022 -3.071  1.00 52.85  ? 387  ALA A C     1 
ATOM   2854 O  O     . ALA A 1 401 ? 15.785  33.530 -2.282  1.00 43.17  ? 387  ALA A O     1 
ATOM   2855 C  CB    . ALA A 1 401 ? 16.033  36.175 -4.228  1.00 36.50  ? 387  ALA A CB    1 
ATOM   2856 N  N     . PHE A 1 402 ? 17.305  33.277 -3.923  1.00 60.69  ? 388  PHE A N     1 
ATOM   2857 C  CA    . PHE A 1 402 ? 17.117  31.838 -3.996  1.00 59.41  ? 388  PHE A CA    1 
ATOM   2858 C  C     . PHE A 1 402 ? 17.816  31.086 -2.878  1.00 51.30  ? 388  PHE A C     1 
ATOM   2859 O  O     . PHE A 1 402 ? 17.580  29.884 -2.723  1.00 65.84  ? 388  PHE A O     1 
ATOM   2860 C  CB    . PHE A 1 402 ? 17.558  31.344 -5.364  1.00 67.13  ? 388  PHE A CB    1 
ATOM   2861 C  CG    . PHE A 1 402 ? 16.708  31.886 -6.459  1.00 78.30  ? 388  PHE A CG    1 
ATOM   2862 C  CD1   . PHE A 1 402 ? 15.333  31.814 -6.351  1.00 70.11  ? 388  PHE A CD1   1 
ATOM   2863 C  CD2   . PHE A 1 402 ? 17.260  32.495 -7.570  1.00 87.50  ? 388  PHE A CD2   1 
ATOM   2864 C  CE1   . PHE A 1 402 ? 14.526  32.301 -7.324  1.00 73.88  ? 388  PHE A CE1   1 
ATOM   2865 C  CE2   . PHE A 1 402 ? 16.446  32.996 -8.562  1.00 83.62  ? 388  PHE A CE2   1 
ATOM   2866 C  CZ    . PHE A 1 402 ? 15.083  32.898 -8.434  1.00 70.13  ? 388  PHE A CZ    1 
ATOM   2867 N  N     . GLY A 1 403 ? 18.671  31.748 -2.114  1.00 41.77  ? 389  GLY A N     1 
ATOM   2868 C  CA    . GLY A 1 403 ? 19.077  31.179 -0.853  1.00 37.08  ? 389  GLY A CA    1 
ATOM   2869 C  C     . GLY A 1 403 ? 18.090  31.572 0.228   1.00 33.59  ? 389  GLY A C     1 
ATOM   2870 O  O     . GLY A 1 403 ? 17.673  30.741 1.038   1.00 31.15  ? 389  GLY A O     1 
ATOM   2871 N  N     . ALA A 1 404 ? 17.669  32.840 0.218   1.00 33.47  ? 390  ALA A N     1 
ATOM   2872 C  CA    . ALA A 1 404 ? 16.760  33.341 1.243   1.00 30.60  ? 390  ALA A CA    1 
ATOM   2873 C  C     . ALA A 1 404 ? 15.417  32.622 1.235   1.00 30.59  ? 390  ALA A C     1 
ATOM   2874 O  O     . ALA A 1 404 ? 14.735  32.586 2.271   1.00 26.67  ? 390  ALA A O     1 
ATOM   2875 C  CB    . ALA A 1 404 ? 16.559  34.847 1.049   1.00 28.73  ? 390  ALA A CB    1 
ATOM   2876 N  N     . ILE A 1 405 ? 15.045  32.011 0.105   1.00 32.02  ? 391  ILE A N     1 
ATOM   2877 C  CA    . ILE A 1 405 ? 13.780  31.286 0.010   1.00 29.45  ? 391  ILE A CA    1 
ATOM   2878 C  C     . ILE A 1 405 ? 13.689  30.183 1.054   1.00 28.54  ? 391  ILE A C     1 
ATOM   2879 O  O     . ILE A 1 405 ? 12.587  29.800 1.468   1.00 25.09  ? 391  ILE A O     1 
ATOM   2880 C  CB    . ILE A 1 405 ? 13.608  30.713 -1.407  1.00 30.40  ? 391  ILE A CB    1 
ATOM   2881 C  CG1   . ILE A 1 405 ? 12.175  30.233 -1.604  1.00 29.37  ? 391  ILE A CG1   1 
ATOM   2882 C  CG2   . ILE A 1 405 ? 14.593  29.575 -1.633  1.00 33.33  ? 391  ILE A CG2   1 
ATOM   2883 C  CD1   . ILE A 1 405 ? 11.845  29.848 -3.019  1.00 29.96  ? 391  ILE A CD1   1 
ATOM   2884 N  N     . ASP A 1 406 ? 14.829  29.631 1.475   1.00 26.83  ? 392  ASP A N     1 
ATOM   2885 C  CA    . ASP A 1 406 ? 14.848  28.548 2.444   1.00 28.38  ? 392  ASP A CA    1 
ATOM   2886 C  C     . ASP A 1 406 ? 14.880  29.040 3.885   1.00 28.89  ? 392  ASP A C     1 
ATOM   2887 O  O     . ASP A 1 406 ? 14.966  28.214 4.798   1.00 28.28  ? 392  ASP A O     1 
ATOM   2888 C  CB    . ASP A 1 406 ? 16.046  27.624 2.200   1.00 29.43  ? 392  ASP A CB    1 
ATOM   2889 C  CG    . ASP A 1 406 ? 15.950  26.879 0.882   1.00 32.93  ? 392  ASP A CG    1 
ATOM   2890 O  OD1   . ASP A 1 406 ? 14.857  26.355 0.568   1.00 33.79  ? 392  ASP A OD1   1 
ATOM   2891 O  OD2   . ASP A 1 406 ? 16.976  26.817 0.166   1.00 36.97  ? 392  ASP A OD2   1 
ATOM   2892 N  N     . LEU A 1 407 ? 14.893  30.350 4.113   1.00 26.86  ? 393  LEU A N     1 
ATOM   2893 C  CA    . LEU A 1 407 ? 14.811  30.856 5.474   1.00 26.81  ? 393  LEU A CA    1 
ATOM   2894 C  C     . LEU A 1 407 ? 13.436  30.552 6.050   1.00 26.97  ? 393  LEU A C     1 
ATOM   2895 O  O     . LEU A 1 407 ? 12.413  30.760 5.391   1.00 24.99  ? 393  LEU A O     1 
ATOM   2896 C  CB    . LEU A 1 407 ? 15.070  32.363 5.506   1.00 25.33  ? 393  LEU A CB    1 
ATOM   2897 C  CG    . LEU A 1 407 ? 16.520  32.816 5.353   1.00 26.82  ? 393  LEU A CG    1 
ATOM   2898 C  CD1   . LEU A 1 407 ? 16.583  34.328 5.141   1.00 25.20  ? 393  LEU A CD1   1 
ATOM   2899 C  CD2   . LEU A 1 407 ? 17.355  32.377 6.567   1.00 27.71  ? 393  LEU A CD2   1 
ATOM   2900 N  N     . ARG A 1 408 ? 13.416  30.075 7.295   1.00 26.32  ? 394  ARG A N     1 
ATOM   2901 C  CA    . ARG A 1 408 ? 12.174  29.794 8.012   1.00 26.98  ? 394  ARG A CA    1 
ATOM   2902 C  C     . ARG A 1 408 ? 11.828  31.022 8.841   1.00 27.79  ? 394  ARG A C     1 
ATOM   2903 O  O     . ARG A 1 408 ? 12.410  31.255 9.906   1.00 25.34  ? 394  ARG A O     1 
ATOM   2904 C  CB    . ARG A 1 408 ? 12.319  28.556 8.889   1.00 32.44  ? 394  ARG A CB    1 
ATOM   2905 C  CG    . ARG A 1 408 ? 11.006  27.831 9.165   1.00 37.91  ? 394  ARG A CG    1 
ATOM   2906 C  CD    . ARG A 1 408 ? 11.105  26.948 10.417  1.00 45.92  ? 394  ARG A CD    1 
ATOM   2907 N  NE    . ARG A 1 408 ? 10.086  25.904 10.435  1.00 61.07  ? 394  ARG A NE    1 
ATOM   2908 C  CZ    . ARG A 1 408 ? 9.875   25.075 11.449  1.00 63.63  ? 394  ARG A CZ    1 
ATOM   2909 N  NH1   . ARG A 1 408 ? 10.595  25.143 12.557  1.00 58.83  ? 394  ARG A NH1   1 
ATOM   2910 N  NH2   . ARG A 1 408 ? 8.917   24.158 11.349  1.00 68.69  ? 394  ARG A NH2   1 
ATOM   2911 N  N     . LEU A 1 409 ? 10.868  31.794 8.363   1.00 25.75  ? 395  LEU A N     1 
ATOM   2912 C  CA    . LEU A 1 409 ? 10.643  33.136 8.894   1.00 27.20  ? 395  LEU A CA    1 
ATOM   2913 C  C     . LEU A 1 409 ? 9.827   33.082 10.180  1.00 30.14  ? 395  LEU A C     1 
ATOM   2914 O  O     . LEU A 1 409 ? 8.744   32.483 10.196  1.00 29.61  ? 395  LEU A O     1 
ATOM   2915 C  CB    . LEU A 1 409 ? 9.917   34.006 7.867   1.00 25.19  ? 395  LEU A CB    1 
ATOM   2916 C  CG    . LEU A 1 409 ? 10.607  34.298 6.532   1.00 24.71  ? 395  LEU A CG    1 
ATOM   2917 C  CD1   . LEU A 1 409 ? 9.790   35.328 5.757   1.00 25.19  ? 395  LEU A CD1   1 
ATOM   2918 C  CD2   . LEU A 1 409 ? 12.052  34.762 6.709   1.00 23.20  ? 395  LEU A CD2   1 
ATOM   2919 N  N     . PRO A 1 410 ? 10.261  33.780 11.243  1.00 28.57  ? 396  PRO A N     1 
ATOM   2920 C  CA    . PRO A 1 410 ? 9.438   33.884 12.454  1.00 30.82  ? 396  PRO A CA    1 
ATOM   2921 C  C     . PRO A 1 410 ? 8.239   34.779 12.208  1.00 31.21  ? 396  PRO A C     1 
ATOM   2922 O  O     . PRO A 1 410 ? 7.995   35.206 11.075  1.00 28.61  ? 396  PRO A O     1 
ATOM   2923 C  CB    . PRO A 1 410 ? 10.386  34.535 13.472  1.00 29.16  ? 396  PRO A CB    1 
ATOM   2924 C  CG    . PRO A 1 410 ? 11.763  34.324 12.902  1.00 31.17  ? 396  PRO A CG    1 
ATOM   2925 C  CD    . PRO A 1 410 ? 11.577  34.413 11.425  1.00 27.21  ? 396  PRO A CD    1 
ATOM   2926 N  N     . ALA A 1 411 ? 7.486   35.067 13.261  1.00 30.60  ? 397  ALA A N     1 
ATOM   2927 C  CA    . ALA A 1 411 ? 6.340   35.950 13.135  1.00 32.44  ? 397  ALA A CA    1 
ATOM   2928 C  C     . ALA A 1 411 ? 6.784   37.382 12.840  1.00 31.83  ? 397  ALA A C     1 
ATOM   2929 O  O     . ALA A 1 411 ? 7.872   37.812 13.235  1.00 30.04  ? 397  ALA A O     1 
ATOM   2930 C  CB    . ALA A 1 411 ? 5.506   35.912 14.417  1.00 34.45  ? 397  ALA A CB    1 
ATOM   2931 N  N     . ASP A 1 412 ? 5.907   38.125 12.152  1.00 31.79  ? 398  ASP A N     1 
ATOM   2932 C  CA    . ASP A 1 412 ? 6.052   39.567 11.923  1.00 30.02  ? 398  ASP A CA    1 
ATOM   2933 C  C     . ASP A 1 412 ? 7.360   39.912 11.215  1.00 28.57  ? 398  ASP A C     1 
ATOM   2934 O  O     . ASP A 1 412 ? 8.128   40.768 11.657  1.00 28.83  ? 398  ASP A O     1 
ATOM   2935 C  CB    . ASP A 1 412 ? 5.927   40.350 13.235  1.00 32.67  ? 398  ASP A CB    1 
ATOM   2936 C  CG    . ASP A 1 412 ? 4.749   39.899 14.076  1.00 42.43  ? 398  ASP A CG    1 
ATOM   2937 O  OD1   . ASP A 1 412 ? 3.649   39.719 13.508  1.00 50.74  ? 398  ASP A OD1   1 
ATOM   2938 O  OD2   . ASP A 1 412 ? 4.921   39.725 15.306  1.00 50.60  ? 398  ASP A OD2   1 
ATOM   2939 N  N     . VAL A 1 413 ? 7.613   39.246 10.094  1.00 27.26  ? 399  VAL A N     1 
ATOM   2940 C  CA    . VAL A 1 413 ? 8.764   39.545 9.247   1.00 26.03  ? 399  VAL A CA    1 
ATOM   2941 C  C     . VAL A 1 413 ? 8.233   40.104 7.938   1.00 23.23  ? 399  VAL A C     1 
ATOM   2942 O  O     . VAL A 1 413 ? 7.234   39.605 7.404   1.00 23.27  ? 399  VAL A O     1 
ATOM   2943 C  CB    . VAL A 1 413 ? 9.652   38.309 9.014   1.00 24.59  ? 399  VAL A CB    1 
ATOM   2944 C  CG1   . VAL A 1 413 ? 10.735  38.604 7.953   1.00 24.61  ? 399  VAL A CG1   1 
ATOM   2945 C  CG2   . VAL A 1 413 ? 10.297  37.883 10.307  1.00 27.11  ? 399  VAL A CG2   1 
ATOM   2946 N  N     . ASN A 1 414 ? 8.831   41.190 7.472   1.00 22.80  ? 400  ASN A N     1 
ATOM   2947 C  CA    . ASN A 1 414 ? 8.531   41.718 6.151   1.00 22.17  ? 400  ASN A CA    1 
ATOM   2948 C  C     . ASN A 1 414 ? 9.653   41.244 5.232   1.00 20.23  ? 400  ASN A C     1 
ATOM   2949 O  O     . ASN A 1 414 ? 10.813  41.658 5.383   1.00 20.88  ? 400  ASN A O     1 
ATOM   2950 C  CB    . ASN A 1 414 ? 8.387   43.240 6.166   1.00 21.14  ? 400  ASN A CB    1 
ATOM   2951 C  CG    . ASN A 1 414 ? 7.837   43.783 4.845   1.00 23.21  ? 400  ASN A CG    1 
ATOM   2952 O  OD1   . ASN A 1 414 ? 7.953   43.138 3.806   1.00 22.00  ? 400  ASN A OD1   1 
ATOM   2953 N  ND2   . ASN A 1 414 ? 7.194   44.944 4.893   1.00 20.77  ? 400  ASN A ND2   1 
ATOM   2954 N  N     . PHE A 1 415 ? 9.309   40.347 4.309   1.00 20.61  ? 401  PHE A N     1 
ATOM   2955 C  CA    . PHE A 1 415 ? 10.266  39.691 3.424   1.00 20.69  ? 401  PHE A CA    1 
ATOM   2956 C  C     . PHE A 1 415 ? 10.076  40.268 2.027   1.00 19.42  ? 401  PHE A C     1 
ATOM   2957 O  O     . PHE A 1 415 ? 9.069   39.999 1.363   1.00 19.13  ? 401  PHE A O     1 
ATOM   2958 C  CB    . PHE A 1 415 ? 10.076  38.176 3.427   1.00 20.31  ? 401  PHE A CB    1 
ATOM   2959 C  CG    . PHE A 1 415 ? 11.108  37.433 2.621   1.00 20.84  ? 401  PHE A CG    1 
ATOM   2960 C  CD1   . PHE A 1 415 ? 10.929  37.221 1.259   1.00 21.19  ? 401  PHE A CD1   1 
ATOM   2961 C  CD2   . PHE A 1 415 ? 12.267  36.956 3.229   1.00 21.18  ? 401  PHE A CD2   1 
ATOM   2962 C  CE1   . PHE A 1 415 ? 11.885  36.530 0.516   1.00 21.69  ? 401  PHE A CE1   1 
ATOM   2963 C  CE2   . PHE A 1 415 ? 13.234  36.272 2.500   1.00 21.09  ? 401  PHE A CE2   1 
ATOM   2964 C  CZ    . PHE A 1 415 ? 13.042  36.057 1.141   1.00 22.10  ? 401  PHE A CZ    1 
ATOM   2965 N  N     . ILE A 1 416 ? 11.053  41.040 1.573   1.00 19.51  ? 402  ILE A N     1 
ATOM   2966 C  CA    . ILE A 1 416 ? 10.911  41.812 0.349   1.00 19.54  ? 402  ILE A CA    1 
ATOM   2967 C  C     . ILE A 1 416 ? 11.834  41.224 -0.705  1.00 18.49  ? 402  ILE A C     1 
ATOM   2968 O  O     . ILE A 1 416 ? 13.063  41.314 -0.596  1.00 17.87  ? 402  ILE A O     1 
ATOM   2969 C  CB    . ILE A 1 416 ? 11.199  43.296 0.577   1.00 17.93  ? 402  ILE A CB    1 
ATOM   2970 C  CG1   . ILE A 1 416 ? 10.128  43.873 1.492   1.00 19.43  ? 402  ILE A CG1   1 
ATOM   2971 C  CG2   . ILE A 1 416 ? 11.188  44.029 -0.780  1.00 17.52  ? 402  ILE A CG2   1 
ATOM   2972 C  CD1   . ILE A 1 416 ? 10.377  45.322 1.867   1.00 20.64  ? 402  ILE A CD1   1 
ATOM   2973 N  N     . VAL A 1 417 ? 11.230  40.644 -1.738  1.00 16.96  ? 403  VAL A N     1 
ATOM   2974 C  CA    . VAL A 1 417 ? 11.935  40.081 -2.883  1.00 18.21  ? 403  VAL A CA    1 
ATOM   2975 C  C     . VAL A 1 417 ? 11.154  40.440 -4.139  1.00 18.61  ? 403  VAL A C     1 
ATOM   2976 O  O     . VAL A 1 417 ? 9.930   40.611 -4.102  1.00 15.48  ? 403  VAL A O     1 
ATOM   2977 C  CB    . VAL A 1 417 ? 12.109  38.555 -2.732  1.00 21.14  ? 403  VAL A CB    1 
ATOM   2978 C  CG1   . VAL A 1 417 ? 10.755  37.855 -2.767  1.00 20.55  ? 403  VAL A CG1   1 
ATOM   2979 C  CG2   . VAL A 1 417 ? 13.032  38.006 -3.796  1.00 22.28  ? 403  VAL A CG2   1 
ATOM   2980 N  N     . GLN A 1 418 ? 11.866  40.564 -5.261  1.00 19.11  ? 404  GLN A N     1 
ATOM   2981 C  CA    . GLN A 1 418 ? 11.287  41.051 -6.515  1.00 18.94  ? 404  GLN A CA    1 
ATOM   2982 C  C     . GLN A 1 418 ? 11.577  40.054 -7.632  1.00 19.56  ? 404  GLN A C     1 
ATOM   2983 O  O     . GLN A 1 418 ? 12.328  40.352 -8.567  1.00 19.64  ? 404  GLN A O     1 
ATOM   2984 C  CB    . GLN A 1 418 ? 11.840  42.437 -6.857  1.00 17.63  ? 404  GLN A CB    1 
ATOM   2985 C  CG    . GLN A 1 418 ? 11.099  43.131 -7.995  1.00 19.41  ? 404  GLN A CG    1 
ATOM   2986 C  CD    . GLN A 1 418 ? 11.907  44.261 -8.609  1.00 17.49  ? 404  GLN A CD    1 
ATOM   2987 O  OE1   . GLN A 1 418 ? 13.032  44.057 -9.056  1.00 17.91  ? 404  GLN A OE1   1 
ATOM   2988 N  NE2   . GLN A 1 418 ? 11.330  45.457 -8.637  1.00 17.11  ? 404  GLN A NE2   1 
ATOM   2989 N  N     . PRO A 1 419 ? 10.988  38.854 -7.566  1.00 20.19  ? 405  PRO A N     1 
ATOM   2990 C  CA    . PRO A 1 419 ? 11.357  37.792 -8.518  1.00 21.55  ? 405  PRO A CA    1 
ATOM   2991 C  C     . PRO A 1 419 ? 10.645  37.842 -9.866  1.00 21.33  ? 405  PRO A C     1 
ATOM   2992 O  O     . PRO A 1 419 ? 11.150  37.234 -10.823 1.00 19.61  ? 405  PRO A O     1 
ATOM   2993 C  CB    . PRO A 1 419 ? 10.972  36.500 -7.774  1.00 21.53  ? 405  PRO A CB    1 
ATOM   2994 C  CG    . PRO A 1 419 ? 10.448  36.941 -6.418  1.00 22.14  ? 405  PRO A CG    1 
ATOM   2995 C  CD    . PRO A 1 419 ? 10.037  38.362 -6.560  1.00 19.35  ? 405  PRO A CD    1 
ATOM   2996 N  N     . LEU A 1 420 ? 9.502   38.527 -9.982  1.00 18.19  ? 406  LEU A N     1 
ATOM   2997 C  CA    . LEU A 1 420 ? 8.835   38.632 -11.280 1.00 18.38  ? 406  LEU A CA    1 
ATOM   2998 C  C     . LEU A 1 420 ? 9.483   39.701 -12.154 1.00 17.90  ? 406  LEU A C     1 
ATOM   2999 O  O     . LEU A 1 420 ? 9.879   39.426 -13.292 1.00 19.27  ? 406  LEU A O     1 
ATOM   3000 C  CB    . LEU A 1 420 ? 7.343   38.928 -11.092 1.00 17.47  ? 406  LEU A CB    1 
ATOM   3001 C  CG    . LEU A 1 420 ? 6.538   39.253 -12.367 1.00 18.76  ? 406  LEU A CG    1 
ATOM   3002 C  CD1   . LEU A 1 420 ? 6.719   38.219 -13.484 1.00 18.17  ? 406  LEU A CD1   1 
ATOM   3003 C  CD2   . LEU A 1 420 ? 5.061   39.396 -12.027 1.00 19.06  ? 406  LEU A CD2   1 
ATOM   3004 N  N     . TRP A 1 421 ? 9.603   40.929 -11.652 1.00 18.08  ? 407  TRP A N     1 
ATOM   3005 C  CA    . TRP A 1 421 ? 10.326  41.940 -12.411 1.00 17.10  ? 407  TRP A CA    1 
ATOM   3006 C  C     . TRP A 1 421 ? 11.811  41.596 -12.496 1.00 17.78  ? 407  TRP A C     1 
ATOM   3007 O  O     . TRP A 1 421 ? 12.379  41.502 -13.597 1.00 16.55  ? 407  TRP A O     1 
ATOM   3008 C  CB    . TRP A 1 421 ? 10.115  43.326 -11.793 1.00 17.55  ? 407  TRP A CB    1 
ATOM   3009 C  CG    . TRP A 1 421 ? 10.587  44.443 -12.705 1.00 17.40  ? 407  TRP A CG    1 
ATOM   3010 C  CD1   . TRP A 1 421 ? 11.455  45.457 -12.387 1.00 17.36  ? 407  TRP A CD1   1 
ATOM   3011 C  CD2   . TRP A 1 421 ? 10.249  44.625 -14.091 1.00 16.94  ? 407  TRP A CD2   1 
ATOM   3012 N  NE1   . TRP A 1 421 ? 11.640  46.274 -13.472 1.00 16.31  ? 407  TRP A NE1   1 
ATOM   3013 C  CE2   . TRP A 1 421 ? 10.922  45.779 -14.534 1.00 16.44  ? 407  TRP A CE2   1 
ATOM   3014 C  CE3   . TRP A 1 421 ? 9.434   43.923 -15.000 1.00 16.40  ? 407  TRP A CE3   1 
ATOM   3015 C  CZ2   . TRP A 1 421 ? 10.813  46.251 -15.847 1.00 16.99  ? 407  TRP A CZ2   1 
ATOM   3016 C  CZ3   . TRP A 1 421 ? 9.324   44.395 -16.305 1.00 15.93  ? 407  TRP A CZ3   1 
ATOM   3017 C  CH2   . TRP A 1 421 ? 10.013  45.548 -16.717 1.00 15.85  ? 407  TRP A CH2   1 
ATOM   3018 N  N     . GLY A 1 422 ? 12.443  41.360 -11.349 1.00 18.13  ? 408  GLY A N     1 
ATOM   3019 C  CA    . GLY A 1 422 ? 13.780  40.799 -11.330 1.00 18.49  ? 408  GLY A CA    1 
ATOM   3020 C  C     . GLY A 1 422 ? 14.913  41.750 -11.662 1.00 17.66  ? 408  GLY A C     1 
ATOM   3021 O  O     . GLY A 1 422 ? 15.856  41.361 -12.363 1.00 15.69  ? 408  GLY A O     1 
ATOM   3022 N  N     . SER A 1 423 ? 14.854  42.988 -11.178 1.00 16.70  ? 409  SER A N     1 
ATOM   3023 C  CA    . SER A 1 423 ? 15.859  44.001 -11.501 1.00 18.90  ? 409  SER A CA    1 
ATOM   3024 C  C     . SER A 1 423 ? 16.927  44.011 -10.401 1.00 17.16  ? 409  SER A C     1 
ATOM   3025 O  O     . SER A 1 423 ? 16.636  44.375 -9.257  1.00 17.27  ? 409  SER A O     1 
ATOM   3026 C  CB    . SER A 1 423 ? 15.203  45.374 -11.637 1.00 15.88  ? 409  SER A CB    1 
ATOM   3027 O  OG    . SER A 1 423 ? 16.081  46.296 -12.269 1.00 17.92  ? 409  SER A OG    1 
ATOM   3028 N  N     . ILE A 1 424 ? 18.153  43.578 -10.728 1.00 16.69  ? 410  ILE A N     1 
ATOM   3029 C  CA    . ILE A 1 424 ? 19.215  43.608 -9.725  1.00 17.41  ? 410  ILE A CA    1 
ATOM   3030 C  C     . ILE A 1 424 ? 19.604  45.059 -9.453  1.00 17.84  ? 410  ILE A C     1 
ATOM   3031 O  O     . ILE A 1 424 ? 19.542  45.931 -10.338 1.00 16.19  ? 410  ILE A O     1 
ATOM   3032 C  CB    . ILE A 1 424 ? 20.438  42.759 -10.134 1.00 19.06  ? 410  ILE A CB    1 
ATOM   3033 C  CG1   . ILE A 1 424 ? 21.066  43.251 -11.442 1.00 19.32  ? 410  ILE A CG1   1 
ATOM   3034 C  CG2   . ILE A 1 424 ? 20.061  41.281 -10.263 1.00 20.20  ? 410  ILE A CG2   1 
ATOM   3035 C  CD1   . ILE A 1 424 ? 22.540  42.803 -11.620 1.00 21.31  ? 410  ILE A CD1   1 
ATOM   3036 N  N     . GLY A 1 425 ? 19.995  45.326 -8.207  1.00 17.67  ? 411  GLY A N     1 
ATOM   3037 C  CA    . GLY A 1 425 ? 20.144  46.675 -7.700  1.00 18.12  ? 411  GLY A CA    1 
ATOM   3038 C  C     . GLY A 1 425 ? 18.919  47.183 -6.957  1.00 17.33  ? 411  GLY A C     1 
ATOM   3039 O  O     . GLY A 1 425 ? 19.042  48.063 -6.087  1.00 17.63  ? 411  GLY A O     1 
ATOM   3040 N  N     . TYR A 1 426 ? 17.741  46.632 -7.269  1.00 17.24  ? 412  TYR A N     1 
ATOM   3041 C  CA    . TYR A 1 426 ? 16.518  47.022 -6.575  1.00 16.55  ? 412  TYR A CA    1 
ATOM   3042 C  C     . TYR A 1 426 ? 16.696  46.943 -5.054  1.00 17.59  ? 412  TYR A C     1 
ATOM   3043 O  O     . TYR A 1 426 ? 16.272  47.839 -4.313  1.00 18.60  ? 412  TYR A O     1 
ATOM   3044 C  CB    . TYR A 1 426 ? 15.362  46.127 -7.036  1.00 16.99  ? 412  TYR A CB    1 
ATOM   3045 C  CG    . TYR A 1 426 ? 14.160  46.197 -6.123  1.00 17.26  ? 412  TYR A CG    1 
ATOM   3046 C  CD1   . TYR A 1 426 ? 13.237  47.220 -6.246  1.00 15.20  ? 412  TYR A CD1   1 
ATOM   3047 C  CD2   . TYR A 1 426 ? 13.961  45.242 -5.127  1.00 16.34  ? 412  TYR A CD2   1 
ATOM   3048 C  CE1   . TYR A 1 426 ? 12.136  47.299 -5.375  1.00 17.68  ? 412  TYR A CE1   1 
ATOM   3049 C  CE2   . TYR A 1 426 ? 12.878  45.308 -4.268  1.00 17.89  ? 412  TYR A CE2   1 
ATOM   3050 C  CZ    . TYR A 1 426 ? 11.973  46.335 -4.389  1.00 17.03  ? 412  TYR A CZ    1 
ATOM   3051 O  OH    . TYR A 1 426 ? 10.889  46.389 -3.521  1.00 18.20  ? 412  TYR A OH    1 
ATOM   3052 N  N     . THR A 1 427 ? 17.341  45.886 -4.576  1.00 16.82  ? 413  THR A N     1 
ATOM   3053 C  CA    . THR A 1 427 ? 17.302  45.569 -3.150  1.00 17.75  ? 413  THR A CA    1 
ATOM   3054 C  C     . THR A 1 427 ? 17.995  46.620 -2.289  1.00 15.25  ? 413  THR A C     1 
ATOM   3055 O  O     . THR A 1 427 ? 17.438  47.056 -1.277  1.00 17.94  ? 413  THR A O     1 
ATOM   3056 C  CB    . THR A 1 427 ? 17.910  44.200 -2.929  1.00 18.87  ? 413  THR A CB    1 
ATOM   3057 O  OG1   . THR A 1 427 ? 17.078  43.253 -3.599  1.00 17.49  ? 413  THR A OG1   1 
ATOM   3058 C  CG2   . THR A 1 427 ? 18.001  43.873 -1.431  1.00 17.18  ? 413  THR A CG2   1 
ATOM   3059 N  N     . LEU A 1 428 ? 19.208  47.043 -2.656  1.00 16.28  ? 414  LEU A N     1 
ATOM   3060 C  CA    . LEU A 1 428 ? 19.895  48.030 -1.816  1.00 18.33  ? 414  LEU A CA    1 
ATOM   3061 C  C     . LEU A 1 428 ? 19.094  49.326 -1.730  1.00 18.65  ? 414  LEU A C     1 
ATOM   3062 O  O     . LEU A 1 428 ? 19.026  49.957 -0.668  1.00 18.25  ? 414  LEU A O     1 
ATOM   3063 C  CB    . LEU A 1 428 ? 21.311  48.313 -2.338  1.00 16.40  ? 414  LEU A CB    1 
ATOM   3064 C  CG    . LEU A 1 428 ? 22.095  49.406 -1.599  1.00 16.08  ? 414  LEU A CG    1 
ATOM   3065 C  CD1   . LEU A 1 428 ? 22.459  48.989 -0.161  1.00 16.97  ? 414  LEU A CD1   1 
ATOM   3066 C  CD2   . LEU A 1 428 ? 23.365  49.781 -2.391  1.00 16.55  ? 414  LEU A CD2   1 
ATOM   3067 N  N     . ALA A 1 429 ? 18.511  49.762 -2.851  1.00 16.72  ? 415  ALA A N     1 
ATOM   3068 C  CA    . ALA A 1 429 ? 17.749  51.009 -2.840  1.00 18.63  ? 415  ALA A CA    1 
ATOM   3069 C  C     . ALA A 1 429 ? 16.389  50.834 -2.167  1.00 18.48  ? 415  ALA A C     1 
ATOM   3070 O  O     . ALA A 1 429 ? 15.924  51.730 -1.449  1.00 16.96  ? 415  ALA A O     1 
ATOM   3071 C  CB    . ALA A 1 429 ? 17.573  51.525 -4.271  1.00 16.49  ? 415  ALA A CB    1 
ATOM   3072 N  N     . ALA A 1 430 ? 15.744  49.686 -2.382  1.00 17.03  ? 416  ALA A N     1 
ATOM   3073 C  CA    . ALA A 1 430 ? 14.492  49.408 -1.679  1.00 18.32  ? 416  ALA A CA    1 
ATOM   3074 C  C     . ALA A 1 430 ? 14.706  49.392 -0.171  1.00 18.79  ? 416  ALA A C     1 
ATOM   3075 O  O     . ALA A 1 430 ? 13.830  49.810 0.599   1.00 17.18  ? 416  ALA A O     1 
ATOM   3076 C  CB    . ALA A 1 430 ? 13.911  48.075 -2.156  1.00 17.58  ? 416  ALA A CB    1 
ATOM   3077 N  N     . ALA A 1 431 ? 15.862  48.895 0.268   1.00 17.85  ? 417  ALA A N     1 
ATOM   3078 C  CA    . ALA A 1 431 ? 16.161  48.864 1.694   1.00 18.76  ? 417  ALA A CA    1 
ATOM   3079 C  C     . ALA A 1 431 ? 16.198  50.269 2.279   1.00 18.93  ? 417  ALA A C     1 
ATOM   3080 O  O     . ALA A 1 431 ? 15.758  50.493 3.413   1.00 19.81  ? 417  ALA A O     1 
ATOM   3081 C  CB    . ALA A 1 431 ? 17.486  48.144 1.924   1.00 19.13  ? 417  ALA A CB    1 
ATOM   3082 N  N     . PHE A 1 432 ? 16.724  51.229 1.519   1.00 18.17  ? 418  PHE A N     1 
ATOM   3083 C  CA    . PHE A 1 432 ? 16.733  52.606 1.992   1.00 18.58  ? 418  PHE A CA    1 
ATOM   3084 C  C     . PHE A 1 432 ? 15.311  53.124 2.149   1.00 19.69  ? 418  PHE A C     1 
ATOM   3085 O  O     . PHE A 1 432 ? 15.011  53.865 3.095   1.00 19.86  ? 418  PHE A O     1 
ATOM   3086 C  CB    . PHE A 1 432 ? 17.537  53.481 1.038   1.00 20.04  ? 418  PHE A CB    1 
ATOM   3087 C  CG    . PHE A 1 432 ? 17.394  54.949 1.293   1.00 20.28  ? 418  PHE A CG    1 
ATOM   3088 C  CD1   . PHE A 1 432 ? 17.885  55.517 2.461   1.00 19.69  ? 418  PHE A CD1   1 
ATOM   3089 C  CD2   . PHE A 1 432 ? 16.737  55.756 0.379   1.00 18.55  ? 418  PHE A CD2   1 
ATOM   3090 C  CE1   . PHE A 1 432 ? 17.744  56.868 2.699   1.00 20.06  ? 418  PHE A CE1   1 
ATOM   3091 C  CE2   . PHE A 1 432 ? 16.596  57.111 0.609   1.00 18.98  ? 418  PHE A CE2   1 
ATOM   3092 C  CZ    . PHE A 1 432 ? 17.091  57.666 1.775   1.00 20.72  ? 418  PHE A CZ    1 
ATOM   3093 N  N     . GLY A 1 433 ? 14.426  52.762 1.215   1.00 17.60  ? 419  GLY A N     1 
ATOM   3094 C  CA    . GLY A 1 433 ? 13.021  53.101 1.373   1.00 20.44  ? 419  GLY A CA    1 
ATOM   3095 C  C     . GLY A 1 433 ? 12.362  52.385 2.538   1.00 19.39  ? 419  GLY A C     1 
ATOM   3096 O  O     . GLY A 1 433 ? 11.562  52.975 3.268   1.00 21.31  ? 419  GLY A O     1 
ATOM   3097 N  N     . ALA A 1 434 ? 12.678  51.101 2.723   1.00 20.13  ? 420  ALA A N     1 
ATOM   3098 C  CA    . ALA A 1 434 ? 12.053  50.336 3.794   1.00 20.69  ? 420  ALA A CA    1 
ATOM   3099 C  C     . ALA A 1 434 ? 12.468  50.862 5.165   1.00 22.09  ? 420  ALA A C     1 
ATOM   3100 O  O     . ALA A 1 434 ? 11.629  50.986 6.064   1.00 22.45  ? 420  ALA A O     1 
ATOM   3101 C  CB    . ALA A 1 434 ? 12.395  48.850 3.652   1.00 20.69  ? 420  ALA A CB    1 
ATOM   3102 N  N     . GLN A 1 435 ? 13.756  51.190 5.339   1.00 19.33  ? 421  GLN A N     1 
ATOM   3103 C  CA    . GLN A 1 435 ? 14.210  51.760 6.602   1.00 22.74  ? 421  GLN A CA    1 
ATOM   3104 C  C     . GLN A 1 435 ? 13.571  53.121 6.860   1.00 23.40  ? 421  GLN A C     1 
ATOM   3105 O  O     . GLN A 1 435 ? 13.202  53.433 8.000   1.00 21.91  ? 421  GLN A O     1 
ATOM   3106 C  CB    . GLN A 1 435 ? 15.737  51.876 6.624   1.00 20.42  ? 421  GLN A CB    1 
ATOM   3107 C  CG    . GLN A 1 435 ? 16.324  52.191 8.009   1.00 22.62  ? 421  GLN A CG    1 
ATOM   3108 C  CD    . GLN A 1 435 ? 16.345  50.996 8.947   1.00 25.20  ? 421  GLN A CD    1 
ATOM   3109 O  OE1   . GLN A 1 435 ? 17.359  50.288 9.027   1.00 24.71  ? 421  GLN A OE1   1 
ATOM   3110 N  NE2   . GLN A 1 435 ? 15.252  50.776 9.684   1.00 23.61  ? 421  GLN A NE2   1 
ATOM   3111 N  N     . THR A 1 436 ? 13.412  53.939 5.814   1.00 21.38  ? 422  THR A N     1 
ATOM   3112 C  CA    . THR A 1 436 ? 12.719  55.215 5.990   1.00 23.46  ? 422  THR A CA    1 
ATOM   3113 C  C     . THR A 1 436 ? 11.311  55.005 6.534   1.00 23.35  ? 422  THR A C     1 
ATOM   3114 O  O     . THR A 1 436 ? 10.886  55.701 7.465   1.00 24.79  ? 422  THR A O     1 
ATOM   3115 C  CB    . THR A 1 436 ? 12.670  55.990 4.666   1.00 22.32  ? 422  THR A CB    1 
ATOM   3116 O  OG1   . THR A 1 436 ? 14.002  56.127 4.142   1.00 21.04  ? 422  THR A OG1   1 
ATOM   3117 C  CG2   . THR A 1 436 ? 12.088  57.371 4.907   1.00 21.62  ? 422  THR A CG2   1 
ATOM   3118 N  N     . ALA A 1 437 ? 10.584  54.029 5.982   1.00 21.45  ? 423  ALA A N     1 
ATOM   3119 C  CA    . ALA A 1 437 ? 9.236   53.739 6.458   1.00 23.63  ? 423  ALA A CA    1 
ATOM   3120 C  C     . ALA A 1 437 ? 9.237   53.271 7.910   1.00 24.33  ? 423  ALA A C     1 
ATOM   3121 O  O     . ALA A 1 437 ? 8.347   53.642 8.684   1.00 24.16  ? 423  ALA A O     1 
ATOM   3122 C  CB    . ALA A 1 437 ? 8.577   52.686 5.571   1.00 20.32  ? 423  ALA A CB    1 
ATOM   3123 N  N     . CYS A 1 438 ? 10.205  52.441 8.292   1.00 23.40  ? 424  CYS A N     1 
ATOM   3124 C  CA    . CYS A 1 438 ? 10.215  51.784 9.605   1.00 25.87  ? 424  CYS A CA    1 
ATOM   3125 C  C     . CYS A 1 438 ? 11.561  52.003 10.285  1.00 25.22  ? 424  CYS A C     1 
ATOM   3126 O  O     . CYS A 1 438 ? 12.387  51.082 10.378  1.00 24.64  ? 424  CYS A O     1 
ATOM   3127 C  CB    . CYS A 1 438 ? 9.900   50.292 9.473   1.00 24.89  ? 424  CYS A CB    1 
ATOM   3128 S  SG    . CYS A 1 438 ? 8.420   49.917 8.482   1.00 26.29  ? 424  CYS A SG    1 
ATOM   3129 N  N     . PRO A 1 439 ? 11.811  53.219 10.784  1.00 25.06  ? 425  PRO A N     1 
ATOM   3130 C  CA    . PRO A 1 439 ? 13.101  53.500 11.443  1.00 26.50  ? 425  PRO A CA    1 
ATOM   3131 C  C     . PRO A 1 439 ? 13.396  52.603 12.631  1.00 28.59  ? 425  PRO A C     1 
ATOM   3132 O  O     . PRO A 1 439 ? 14.574  52.403 12.960  1.00 27.76  ? 425  PRO A O     1 
ATOM   3133 C  CB    . PRO A 1 439 ? 12.961  54.964 11.886  1.00 25.41  ? 425  PRO A CB    1 
ATOM   3134 C  CG    . PRO A 1 439 ? 11.479  55.234 11.864  1.00 25.83  ? 425  PRO A CG    1 
ATOM   3135 C  CD    . PRO A 1 439 ? 10.925  54.392 10.772  1.00 25.63  ? 425  PRO A CD    1 
ATOM   3136 N  N     . ASN A 1 440 ? 12.373  52.078 13.309  1.00 29.91  ? 426  ASN A N     1 
ATOM   3137 C  CA    . ASN A 1 440 ? 12.606  51.287 14.513  1.00 30.04  ? 426  ASN A CA    1 
ATOM   3138 C  C     . ASN A 1 440 ? 12.681  49.789 14.251  1.00 30.10  ? 426  ASN A C     1 
ATOM   3139 O  O     . ASN A 1 440 ? 12.858  49.023 15.204  1.00 32.58  ? 426  ASN A O     1 
ATOM   3140 C  CB    . ASN A 1 440 ? 11.512  51.544 15.560  1.00 33.06  ? 426  ASN A CB    1 
ATOM   3141 C  CG    . ASN A 1 440 ? 11.368  53.011 15.924  1.00 33.24  ? 426  ASN A CG    1 
ATOM   3142 O  OD1   . ASN A 1 440 ? 12.348  53.705 16.174  1.00 32.72  ? 426  ASN A OD1   1 
ATOM   3143 N  ND2   . ASN A 1 440 ? 10.133  53.475 15.994  1.00 36.87  ? 426  ASN A ND2   1 
ATOM   3144 N  N     . ARG A 1 441 ? 12.569  49.348 13.003  1.00 29.20  ? 427  ARG A N     1 
ATOM   3145 C  CA    . ARG A 1 441 ? 12.681  47.933 12.679  1.00 28.62  ? 427  ARG A CA    1 
ATOM   3146 C  C     . ARG A 1 441 ? 14.066  47.619 12.126  1.00 27.13  ? 427  ARG A C     1 
ATOM   3147 O  O     . ARG A 1 441 ? 14.716  48.464 11.502  1.00 26.54  ? 427  ARG A O     1 
ATOM   3148 C  CB    . ARG A 1 441 ? 11.594  47.515 11.685  1.00 24.30  ? 427  ARG A CB    1 
ATOM   3149 C  CG    . ARG A 1 441 ? 10.199  47.557 12.295  1.00 26.30  ? 427  ARG A CG    1 
ATOM   3150 C  CD    . ARG A 1 441 ? 9.122   47.049 11.347  1.00 26.27  ? 427  ARG A CD    1 
ATOM   3151 N  NE    . ARG A 1 441 ? 9.276   45.644 10.997  1.00 23.93  ? 427  ARG A NE    1 
ATOM   3152 C  CZ    . ARG A 1 441 ? 8.355   44.928 10.364  1.00 26.95  ? 427  ARG A CZ    1 
ATOM   3153 N  NH1   . ARG A 1 441 ? 7.198   45.462 9.990   1.00 26.53  ? 427  ARG A NH1   1 
ATOM   3154 N  NH2   . ARG A 1 441 ? 8.614   43.654 10.066  1.00 24.43  ? 427  ARG A NH2   1 
ATOM   3155 N  N     . ARG A 1 442 ? 14.525  46.399 12.394  1.00 26.37  ? 428  ARG A N     1 
ATOM   3156 C  CA    . ARG A 1 442 ? 15.835  45.956 11.926  1.00 26.40  ? 428  ARG A CA    1 
ATOM   3157 C  C     . ARG A 1 442 ? 15.740  45.554 10.459  1.00 23.39  ? 428  ARG A C     1 
ATOM   3158 O  O     . ARG A 1 442 ? 14.914  44.712 10.092  1.00 23.39  ? 428  ARG A O     1 
ATOM   3159 C  CB    . ARG A 1 442 ? 16.332  44.777 12.764  1.00 24.54  ? 428  ARG A CB    1 
ATOM   3160 C  CG    . ARG A 1 442 ? 17.790  44.412 12.546  1.00 24.35  ? 428  ARG A CG    1 
ATOM   3161 C  CD    . ARG A 1 442 ? 18.269  43.429 13.597  1.00 23.30  ? 428  ARG A CD    1 
ATOM   3162 N  NE    . ARG A 1 442 ? 17.726  42.093 13.376  1.00 23.59  ? 428  ARG A NE    1 
ATOM   3163 C  CZ    . ARG A 1 442 ? 18.127  41.004 14.020  1.00 27.03  ? 428  ARG A CZ    1 
ATOM   3164 N  NH1   . ARG A 1 442 ? 19.061  41.055 14.959  1.00 23.09  ? 428  ARG A NH1   1 
ATOM   3165 N  NH2   . ARG A 1 442 ? 17.571  39.835 13.722  1.00 27.46  ? 428  ARG A NH2   1 
ATOM   3166 N  N     . VAL A 1 443 ? 16.590  46.148 9.624   1.00 24.32  ? 429  VAL A N     1 
ATOM   3167 C  CA    . VAL A 1 443 ? 16.596  45.914 8.180   1.00 20.67  ? 429  VAL A CA    1 
ATOM   3168 C  C     . VAL A 1 443 ? 17.835  45.103 7.824   1.00 21.87  ? 429  VAL A C     1 
ATOM   3169 O  O     . VAL A 1 443 ? 18.971  45.524 8.100   1.00 24.28  ? 429  VAL A O     1 
ATOM   3170 C  CB    . VAL A 1 443 ? 16.561  47.233 7.397   1.00 20.33  ? 429  VAL A CB    1 
ATOM   3171 C  CG1   . VAL A 1 443 ? 16.933  47.005 5.909   1.00 20.12  ? 429  VAL A CG1   1 
ATOM   3172 C  CG2   . VAL A 1 443 ? 15.190  47.867 7.515   1.00 20.39  ? 429  VAL A CG2   1 
ATOM   3173 N  N     . ILE A 1 444 ? 17.617  43.935 7.228   1.00 20.47  ? 430  ILE A N     1 
ATOM   3174 C  CA    . ILE A 1 444 ? 18.690  43.074 6.753   1.00 20.55  ? 430  ILE A CA    1 
ATOM   3175 C  C     . ILE A 1 444 ? 18.656  43.067 5.228   1.00 21.41  ? 430  ILE A C     1 
ATOM   3176 O  O     . ILE A 1 444 ? 17.638  42.706 4.623   1.00 20.99  ? 430  ILE A O     1 
ATOM   3177 C  CB    . ILE A 1 444 ? 18.566  41.654 7.329   1.00 21.84  ? 430  ILE A CB    1 
ATOM   3178 C  CG1   . ILE A 1 444 ? 18.684  41.693 8.863   1.00 21.92  ? 430  ILE A CG1   1 
ATOM   3179 C  CG2   . ILE A 1 444 ? 19.643  40.760 6.743   1.00 21.28  ? 430  ILE A CG2   1 
ATOM   3180 C  CD1   . ILE A 1 444 ? 17.738  40.751 9.568   1.00 23.36  ? 430  ILE A CD1   1 
ATOM   3181 N  N     . VAL A 1 445 ? 19.780  43.429 4.609   1.00 21.62  ? 431  VAL A N     1 
ATOM   3182 C  CA    . VAL A 1 445 ? 19.892  43.542 3.155   1.00 22.06  ? 431  VAL A CA    1 
ATOM   3183 C  C     . VAL A 1 445 ? 20.800  42.426 2.660   1.00 21.35  ? 431  VAL A C     1 
ATOM   3184 O  O     . VAL A 1 445 ? 21.988  42.376 3.017   1.00 21.73  ? 431  VAL A O     1 
ATOM   3185 C  CB    . VAL A 1 445 ? 20.454  44.910 2.742   1.00 22.37  ? 431  VAL A CB    1 
ATOM   3186 C  CG1   . VAL A 1 445 ? 20.372  45.101 1.227   1.00 21.32  ? 431  VAL A CG1   1 
ATOM   3187 C  CG2   . VAL A 1 445 ? 19.773  46.034 3.508   1.00 21.37  ? 431  VAL A CG2   1 
ATOM   3188 N  N     . LEU A 1 446 ? 20.251  41.543 1.835   1.00 19.46  ? 432  LEU A N     1 
ATOM   3189 C  CA    . LEU A 1 446 ? 21.005  40.465 1.197   1.00 22.83  ? 432  LEU A CA    1 
ATOM   3190 C  C     . LEU A 1 446 ? 21.195  40.814 -0.277  1.00 20.73  ? 432  LEU A C     1 
ATOM   3191 O  O     . LEU A 1 446 ? 20.268  40.675 -1.079  1.00 20.34  ? 432  LEU A O     1 
ATOM   3192 C  CB    . LEU A 1 446 ? 20.271  39.138 1.357   1.00 21.35  ? 432  LEU A CB    1 
ATOM   3193 C  CG    . LEU A 1 446 ? 20.018  38.783 2.819   1.00 22.36  ? 432  LEU A CG    1 
ATOM   3194 C  CD1   . LEU A 1 446 ? 18.797  37.904 2.961   1.00 22.54  ? 432  LEU A CD1   1 
ATOM   3195 C  CD2   . LEU A 1 446 ? 21.260  38.078 3.366   1.00 25.21  ? 432  LEU A CD2   1 
ATOM   3196 N  N     . THR A 1 447 ? 22.394  41.266 -0.640  1.00 21.74  ? 433  THR A N     1 
ATOM   3197 C  CA    . THR A 1 447 ? 22.662  41.628 -2.023  1.00 20.58  ? 433  THR A CA    1 
ATOM   3198 C  C     . THR A 1 447 ? 23.958  40.997 -2.501  1.00 23.97  ? 433  THR A C     1 
ATOM   3199 O  O     . THR A 1 447 ? 24.930  40.882 -1.739  1.00 22.09  ? 433  THR A O     1 
ATOM   3200 C  CB    . THR A 1 447 ? 22.723  43.149 -2.213  1.00 19.73  ? 433  THR A CB    1 
ATOM   3201 O  OG1   . THR A 1 447 ? 23.064  43.433 -3.575  1.00 19.04  ? 433  THR A OG1   1 
ATOM   3202 C  CG2   . THR A 1 447 ? 23.767  43.784 -1.304  1.00 20.86  ? 433  THR A CG2   1 
ATOM   3203 N  N     . GLY A 1 448 ? 23.956  40.572 -3.769  1.00 23.49  ? 434  GLY A N     1 
ATOM   3204 C  CA    . GLY A 1 448 ? 25.184  40.158 -4.411  1.00 22.34  ? 434  GLY A CA    1 
ATOM   3205 C  C     . GLY A 1 448 ? 26.099  41.336 -4.668  1.00 23.17  ? 434  GLY A C     1 
ATOM   3206 O  O     . GLY A 1 448 ? 25.685  42.498 -4.638  1.00 21.66  ? 434  GLY A O     1 
ATOM   3207 N  N     . ASP A 1 449 ? 27.379  41.031 -4.920  1.00 23.23  ? 435  ASP A N     1 
ATOM   3208 C  CA    . ASP A 1 449 ? 28.308  42.103 -5.257  1.00 23.49  ? 435  ASP A CA    1 
ATOM   3209 C  C     . ASP A 1 449 ? 27.924  42.755 -6.580  1.00 22.96  ? 435  ASP A C     1 
ATOM   3210 O  O     . ASP A 1 449 ? 28.031  43.979 -6.730  1.00 22.12  ? 435  ASP A O     1 
ATOM   3211 C  CB    . ASP A 1 449 ? 29.762  41.599 -5.283  1.00 24.61  ? 435  ASP A CB    1 
ATOM   3212 C  CG    . ASP A 1 449 ? 29.966  40.328 -6.121  1.00 28.72  ? 435  ASP A CG    1 
ATOM   3213 O  OD1   . ASP A 1 449 ? 29.062  39.490 -6.262  1.00 27.33  ? 435  ASP A OD1   1 
ATOM   3214 O  OD2   . ASP A 1 449 ? 31.075  40.166 -6.662  1.00 32.12  ? 435  ASP A OD2   1 
ATOM   3215 N  N     . GLY A 1 450 ? 27.466  41.962 -7.550  1.00 22.65  ? 436  GLY A N     1 
ATOM   3216 C  CA    . GLY A 1 450 ? 27.033  42.550 -8.809  1.00 22.12  ? 436  GLY A CA    1 
ATOM   3217 C  C     . GLY A 1 450 ? 25.833  43.465 -8.639  1.00 21.21  ? 436  GLY A C     1 
ATOM   3218 O  O     . GLY A 1 450 ? 25.842  44.605 -9.104  1.00 18.49  ? 436  GLY A O     1 
ATOM   3219 N  N     . ALA A 1 451 ? 24.807  42.992 -7.919  1.00 20.07  ? 437  ALA A N     1 
ATOM   3220 C  CA    . ALA A 1 451 ? 23.577  43.766 -7.748  1.00 20.50  ? 437  ALA A CA    1 
ATOM   3221 C  C     . ALA A 1 451 ? 23.837  45.110 -7.077  1.00 19.88  ? 437  ALA A C     1 
ATOM   3222 O  O     . ALA A 1 451 ? 23.321  46.145 -7.517  1.00 17.41  ? 437  ALA A O     1 
ATOM   3223 C  CB    . ALA A 1 451 ? 22.556  42.966 -6.934  1.00 18.78  ? 437  ALA A CB    1 
ATOM   3224 N  N     . ALA A 1 452 ? 24.624  45.111 -5.997  1.00 18.37  ? 438  ALA A N     1 
ATOM   3225 C  CA    . ALA A 1 452 ? 24.880  46.340 -5.248  1.00 18.96  ? 438  ALA A CA    1 
ATOM   3226 C  C     . ALA A 1 452 ? 25.572  47.414 -6.081  1.00 18.57  ? 438  ALA A C     1 
ATOM   3227 O  O     . ALA A 1 452 ? 25.390  48.605 -5.801  1.00 19.62  ? 438  ALA A O     1 
ATOM   3228 C  CB    . ALA A 1 452 ? 25.731  46.034 -4.010  1.00 18.91  ? 438  ALA A CB    1 
ATOM   3229 N  N     . GLN A 1 453 ? 26.297  47.036 -7.137  1.00 18.53  ? 439  GLN A N     1 
ATOM   3230 C  CA    . GLN A 1 453 ? 26.979  48.044 -7.954  1.00 20.03  ? 439  GLN A CA    1 
ATOM   3231 C  C     . GLN A 1 453 ? 26.009  48.962 -8.680  1.00 19.25  ? 439  GLN A C     1 
ATOM   3232 O  O     . GLN A 1 453 ? 26.329  50.139 -8.899  1.00 18.93  ? 439  GLN A O     1 
ATOM   3233 C  CB    . GLN A 1 453 ? 27.886  47.375 -8.976  1.00 19.26  ? 439  GLN A CB    1 
ATOM   3234 C  CG    . GLN A 1 453 ? 28.959  46.491 -8.366  1.00 21.70  ? 439  GLN A CG    1 
ATOM   3235 C  CD    . GLN A 1 453 ? 30.003  46.099 -9.385  1.00 22.79  ? 439  GLN A CD    1 
ATOM   3236 O  OE1   . GLN A 1 453 ? 29.679  45.868 -10.553 1.00 25.65  ? 439  GLN A OE1   1 
ATOM   3237 N  NE2   . GLN A 1 453 ? 31.249  45.991 -8.956  1.00 22.70  ? 439  GLN A NE2   1 
ATOM   3238 N  N     . LEU A 1 454 ? 24.826  48.452 -9.060  1.00 16.58  ? 440  LEU A N     1 
ATOM   3239 C  CA    . LEU A 1 454 ? 23.920  49.227 -9.904  1.00 19.00  ? 440  LEU A CA    1 
ATOM   3240 C  C     . LEU A 1 454 ? 23.280  50.389 -9.163  1.00 17.84  ? 440  LEU A C     1 
ATOM   3241 O  O     . LEU A 1 454 ? 22.834  51.345 -9.806  1.00 16.67  ? 440  LEU A O     1 
ATOM   3242 C  CB    . LEU A 1 454 ? 22.819  48.328 -10.483 1.00 16.66  ? 440  LEU A CB    1 
ATOM   3243 C  CG    . LEU A 1 454 ? 23.234  47.420 -11.655 1.00 18.36  ? 440  LEU A CG    1 
ATOM   3244 C  CD1   . LEU A 1 454 ? 23.923  46.106 -11.197 1.00 17.65  ? 440  LEU A CD1   1 
ATOM   3245 C  CD2   . LEU A 1 454 ? 22.030  47.116 -12.557 1.00 16.26  ? 440  LEU A CD2   1 
ATOM   3246 N  N     . THR A 1 455 ? 23.216  50.323 -7.829  1.00 18.29  ? 441  THR A N     1 
ATOM   3247 C  CA    . THR A 1 455 ? 22.512  51.317 -7.027  1.00 16.70  ? 441  THR A CA    1 
ATOM   3248 C  C     . THR A 1 455 ? 23.334  51.762 -5.814  1.00 18.10  ? 441  THR A C     1 
ATOM   3249 O  O     . THR A 1 455 ? 22.766  52.251 -4.831  1.00 17.86  ? 441  THR A O     1 
ATOM   3250 C  CB    . THR A 1 455 ? 21.161  50.756 -6.579  1.00 17.10  ? 441  THR A CB    1 
ATOM   3251 O  OG1   . THR A 1 455 ? 21.371  49.547 -5.831  1.00 17.13  ? 441  THR A OG1   1 
ATOM   3252 C  CG2   . THR A 1 455 ? 20.283  50.437 -7.792  1.00 16.94  ? 441  THR A CG2   1 
ATOM   3253 N  N     . ILE A 1 456 ? 24.663  51.633 -5.883  1.00 19.40  ? 442  ILE A N     1 
ATOM   3254 C  CA    . ILE A 1 456 ? 25.520  51.817 -4.715  1.00 17.99  ? 442  ILE A CA    1 
ATOM   3255 C  C     . ILE A 1 456 ? 25.373  53.207 -4.111  1.00 19.02  ? 442  ILE A C     1 
ATOM   3256 O  O     . ILE A 1 456 ? 25.505  53.372 -2.896  1.00 20.12  ? 442  ILE A O     1 
ATOM   3257 C  CB    . ILE A 1 456 ? 26.995  51.517 -5.068  1.00 18.16  ? 442  ILE A CB    1 
ATOM   3258 C  CG1   . ILE A 1 456 ? 27.856  51.502 -3.792  1.00 20.38  ? 442  ILE A CG1   1 
ATOM   3259 C  CG2   . ILE A 1 456 ? 27.566  52.564 -5.992  1.00 18.06  ? 442  ILE A CG2   1 
ATOM   3260 C  CD1   . ILE A 1 456 ? 27.334  50.562 -2.717  1.00 19.49  ? 442  ILE A CD1   1 
ATOM   3261 N  N     . GLN A 1 457 ? 25.085  54.228 -4.925  1.00 19.58  ? 443  GLN A N     1 
ATOM   3262 C  CA    . GLN A 1 457 ? 25.096  55.584 -4.384  1.00 18.24  ? 443  GLN A CA    1 
ATOM   3263 C  C     . GLN A 1 457 ? 24.011  55.806 -3.334  1.00 20.05  ? 443  GLN A C     1 
ATOM   3264 O  O     . GLN A 1 457 ? 24.126  56.749 -2.538  1.00 18.99  ? 443  GLN A O     1 
ATOM   3265 C  CB    . GLN A 1 457 ? 24.965  56.614 -5.514  1.00 18.62  ? 443  GLN A CB    1 
ATOM   3266 C  CG    . GLN A 1 457 ? 23.782  56.413 -6.434  1.00 16.92  ? 443  GLN A CG    1 
ATOM   3267 C  CD    . GLN A 1 457 ? 24.135  55.525 -7.603  1.00 17.50  ? 443  GLN A CD    1 
ATOM   3268 O  OE1   . GLN A 1 457 ? 23.890  54.322 -7.568  1.00 16.08  ? 443  GLN A OE1   1 
ATOM   3269 N  NE2   . GLN A 1 457 ? 24.740  56.112 -8.639  1.00 16.57  ? 443  GLN A NE2   1 
ATOM   3270 N  N     . GLU A 1 458 ? 22.987  54.947 -3.278  1.00 18.08  ? 444  GLU A N     1 
ATOM   3271 C  CA    . GLU A 1 458 ? 21.984  55.103 -2.228  1.00 18.73  ? 444  GLU A CA    1 
ATOM   3272 C  C     . GLU A 1 458 ? 22.472  54.657 -0.861  1.00 20.42  ? 444  GLU A C     1 
ATOM   3273 O  O     . GLU A 1 458 ? 21.809  54.967 0.139   1.00 19.85  ? 444  GLU A O     1 
ATOM   3274 C  CB    . GLU A 1 458 ? 20.696  54.349 -2.574  1.00 18.60  ? 444  GLU A CB    1 
ATOM   3275 C  CG    . GLU A 1 458 ? 19.463  55.204 -2.386  1.00 16.86  ? 444  GLU A CG    1 
ATOM   3276 C  CD    . GLU A 1 458 ? 19.580  56.526 -3.137  1.00 18.06  ? 444  GLU A CD    1 
ATOM   3277 O  OE1   . GLU A 1 458 ? 20.075  56.509 -4.278  1.00 17.67  ? 444  GLU A OE1   1 
ATOM   3278 O  OE2   . GLU A 1 458 ? 19.176  57.585 -2.602  1.00 19.80  ? 444  GLU A OE2   1 
ATOM   3279 N  N     . LEU A 1 459 ? 23.592  53.928 -0.782  1.00 20.60  ? 445  LEU A N     1 
ATOM   3280 C  CA    . LEU A 1 459 ? 24.232  53.731 0.517   1.00 21.19  ? 445  LEU A CA    1 
ATOM   3281 C  C     . LEU A 1 459 ? 24.581  55.074 1.142   1.00 21.88  ? 445  LEU A C     1 
ATOM   3282 O  O     . LEU A 1 459 ? 24.490  55.247 2.367   1.00 21.07  ? 445  LEU A O     1 
ATOM   3283 C  CB    . LEU A 1 459 ? 25.483  52.854 0.374   1.00 22.43  ? 445  LEU A CB    1 
ATOM   3284 C  CG    . LEU A 1 459 ? 26.359  52.688 1.631   1.00 23.45  ? 445  LEU A CG    1 
ATOM   3285 C  CD1   . LEU A 1 459 ? 25.590  52.115 2.798   1.00 24.39  ? 445  LEU A CD1   1 
ATOM   3286 C  CD2   . LEU A 1 459 ? 27.585  51.842 1.343   1.00 25.85  ? 445  LEU A CD2   1 
ATOM   3287 N  N     . GLY A 1 460 ? 24.963  56.042 0.305   1.00 21.81  ? 446  GLY A N     1 
ATOM   3288 C  CA    . GLY A 1 460 ? 25.247  57.375 0.795   1.00 21.40  ? 446  GLY A CA    1 
ATOM   3289 C  C     . GLY A 1 460 ? 24.035  58.048 1.409   1.00 21.89  ? 446  GLY A C     1 
ATOM   3290 O  O     . GLY A 1 460 ? 24.158  58.796 2.379   1.00 20.40  ? 446  GLY A O     1 
ATOM   3291 N  N     . SER A 1 461 ? 22.851  57.816 0.833   1.00 19.44  ? 447  SER A N     1 
ATOM   3292 C  CA    . SER A 1 461 ? 21.623  58.335 1.429   1.00 22.08  ? 447  SER A CA    1 
ATOM   3293 C  C     . SER A 1 461 ? 21.346  57.681 2.775   1.00 19.90  ? 447  SER A C     1 
ATOM   3294 O  O     . SER A 1 461 ? 20.917  58.355 3.719   1.00 19.97  ? 447  SER A O     1 
ATOM   3295 C  CB    . SER A 1 461 ? 20.437  58.126 0.483   1.00 18.85  ? 447  SER A CB    1 
ATOM   3296 O  OG    . SER A 1 461 ? 20.702  58.677 -0.797  1.00 18.47  ? 447  SER A OG    1 
ATOM   3297 N  N     . MET A 1 462 ? 21.578  56.366 2.879   1.00 20.36  ? 448  MET A N     1 
ATOM   3298 C  CA    . MET A 1 462 ? 21.422  55.694 4.163   1.00 21.39  ? 448  MET A CA    1 
ATOM   3299 C  C     . MET A 1 462 ? 22.302  56.339 5.222   1.00 22.77  ? 448  MET A C     1 
ATOM   3300 O  O     . MET A 1 462 ? 21.841  56.641 6.332   1.00 23.43  ? 448  MET A O     1 
ATOM   3301 C  CB    . MET A 1 462 ? 21.775  54.208 4.037   1.00 20.78  ? 448  MET A CB    1 
ATOM   3302 C  CG    . MET A 1 462 ? 21.084  53.434 2.940   1.00 20.34  ? 448  MET A CG    1 
ATOM   3303 S  SD    . MET A 1 462 ? 21.718  51.743 2.945   1.00 24.86  ? 448  MET A SD    1 
ATOM   3304 C  CE    . MET A 1 462 ? 20.246  50.833 2.469   1.00 17.97  ? 448  MET A CE    1 
ATOM   3305 N  N     . LEU A 1 463 ? 23.571  56.588 4.878   1.00 20.94  ? 449  LEU A N     1 
ATOM   3306 C  CA    . LEU A 1 463 ? 24.506  57.164 5.836   1.00 22.30  ? 449  LEU A CA    1 
ATOM   3307 C  C     . LEU A 1 463 ? 24.141  58.604 6.161   1.00 22.97  ? 449  LEU A C     1 
ATOM   3308 O  O     . LEU A 1 463 ? 24.212  59.015 7.325   1.00 21.69  ? 449  LEU A O     1 
ATOM   3309 C  CB    . LEU A 1 463 ? 25.939  57.082 5.293   1.00 21.15  ? 449  LEU A CB    1 
ATOM   3310 C  CG    . LEU A 1 463 ? 26.523  55.690 5.038   1.00 21.56  ? 449  LEU A CG    1 
ATOM   3311 C  CD1   . LEU A 1 463 ? 27.784  55.805 4.165   1.00 21.81  ? 449  LEU A CD1   1 
ATOM   3312 C  CD2   . LEU A 1 463 ? 26.850  54.984 6.355   1.00 24.46  ? 449  LEU A CD2   1 
ATOM   3313 N  N     . ARG A 1 464 ? 23.771  59.392 5.144   1.00 22.66  ? 450  ARG A N     1 
ATOM   3314 C  CA    . ARG A 1 464 ? 23.322  60.761 5.397   1.00 25.14  ? 450  ARG A CA    1 
ATOM   3315 C  C     . ARG A 1 464 ? 22.189  60.797 6.421   1.00 25.58  ? 450  ARG A C     1 
ATOM   3316 O  O     . ARG A 1 464 ? 22.208  61.606 7.363   1.00 24.49  ? 450  ARG A O     1 
ATOM   3317 C  CB    . ARG A 1 464 ? 22.877  61.427 4.088   1.00 23.74  ? 450  ARG A CB    1 
ATOM   3318 C  CG    . ARG A 1 464 ? 22.191  62.778 4.300   1.00 24.19  ? 450  ARG A CG    1 
ATOM   3319 C  CD    . ARG A 1 464 ? 21.257  63.121 3.148   1.00 24.28  ? 450  ARG A CD    1 
ATOM   3320 N  NE    . ARG A 1 464 ? 20.064  62.276 3.067   1.00 24.33  ? 450  ARG A NE    1 
ATOM   3321 C  CZ    . ARG A 1 464 ? 19.337  62.148 1.960   1.00 25.64  ? 450  ARG A CZ    1 
ATOM   3322 N  NH1   . ARG A 1 464 ? 19.671  62.777 0.846   1.00 26.50  ? 450  ARG A NH1   1 
ATOM   3323 N  NH2   . ARG A 1 464 ? 18.255  61.360 1.967   1.00 22.85  ? 450  ARG A NH2   1 
ATOM   3324 N  N     . ASP A 1 465 ? 21.213  59.904 6.279   1.00 25.20  ? 451  ASP A N     1 
ATOM   3325 C  CA    . ASP A 1 465 ? 20.050  59.892 7.151   1.00 24.18  ? 451  ASP A CA    1 
ATOM   3326 C  C     . ASP A 1 465 ? 20.266  59.083 8.427   1.00 26.58  ? 451  ASP A C     1 
ATOM   3327 O  O     . ASP A 1 465 ? 19.332  58.941 9.219   1.00 25.25  ? 451  ASP A O     1 
ATOM   3328 C  CB    . ASP A 1 465 ? 18.830  59.381 6.371   1.00 25.78  ? 451  ASP A CB    1 
ATOM   3329 C  CG    . ASP A 1 465 ? 18.406  60.339 5.267   1.00 24.81  ? 451  ASP A CG    1 
ATOM   3330 O  OD1   . ASP A 1 465 ? 18.941  61.469 5.223   1.00 24.90  ? 451  ASP A OD1   1 
ATOM   3331 O  OD2   . ASP A 1 465 ? 17.526  59.976 4.450   1.00 24.60  ? 451  ASP A OD2   1 
ATOM   3332 N  N     . LYS A 1 466 ? 21.486  58.579 8.651   1.00 25.75  ? 452  LYS A N     1 
ATOM   3333 C  CA    . LYS A 1 466 ? 21.881  57.900 9.887   1.00 28.33  ? 452  LYS A CA    1 
ATOM   3334 C  C     . LYS A 1 466 ? 21.045  56.651 10.148  1.00 28.06  ? 452  LYS A C     1 
ATOM   3335 O  O     . LYS A 1 466 ? 20.689  56.345 11.295  1.00 26.26  ? 452  LYS A O     1 
ATOM   3336 C  CB    . LYS A 1 466 ? 21.851  58.850 11.086  1.00 30.44  ? 452  LYS A CB    1 
ATOM   3337 C  CG    . LYS A 1 466 ? 22.748  60.053 10.868  1.00 34.70  ? 452  LYS A CG    1 
ATOM   3338 C  CD    . LYS A 1 466 ? 23.486  60.455 12.127  1.00 39.50  ? 452  LYS A CD    1 
ATOM   3339 C  CE    . LYS A 1 466 ? 24.002  61.879 12.005  1.00 44.27  ? 452  LYS A CE    1 
ATOM   3340 N  NZ    . LYS A 1 466 ? 25.309  61.944 11.284  1.00 50.04  ? 452  LYS A NZ    1 
ATOM   3341 N  N     . GLN A 1 467 ? 20.751  55.917 9.077   1.00 23.93  ? 453  GLN A N     1 
ATOM   3342 C  CA    . GLN A 1 467 ? 20.094  54.625 9.175   1.00 23.65  ? 453  GLN A CA    1 
ATOM   3343 C  C     . GLN A 1 467 ? 21.091  53.542 9.566   1.00 24.71  ? 453  GLN A C     1 
ATOM   3344 O  O     . GLN A 1 467 ? 22.300  53.658 9.352   1.00 23.42  ? 453  GLN A O     1 
ATOM   3345 C  CB    . GLN A 1 467 ? 19.441  54.219 7.857   1.00 24.66  ? 453  GLN A CB    1 
ATOM   3346 C  CG    . GLN A 1 467 ? 18.553  55.253 7.198   1.00 23.91  ? 453  GLN A CG    1 
ATOM   3347 C  CD    . GLN A 1 467 ? 17.888  54.670 5.973   1.00 23.32  ? 453  GLN A CD    1 
ATOM   3348 O  OE1   . GLN A 1 467 ? 18.489  53.859 5.262   1.00 23.39  ? 453  GLN A OE1   1 
ATOM   3349 N  NE2   . GLN A 1 467 ? 16.636  55.047 5.733   1.00 22.27  ? 453  GLN A NE2   1 
ATOM   3350 N  N     . HIS A 1 468 ? 20.559  52.455 10.114  1.00 22.77  ? 454  HIS A N     1 
ATOM   3351 C  CA    . HIS A 1 468 ? 21.390  51.381 10.650  1.00 24.50  ? 454  HIS A CA    1 
ATOM   3352 C  C     . HIS A 1 468 ? 20.987  50.012 10.106  1.00 24.71  ? 454  HIS A C     1 
ATOM   3353 O  O     . HIS A 1 468 ? 20.793  49.069 10.874  1.00 25.08  ? 454  HIS A O     1 
ATOM   3354 C  CB    . HIS A 1 468 ? 21.332  51.383 12.176  1.00 26.11  ? 454  HIS A CB    1 
ATOM   3355 C  CG    . HIS A 1 468 ? 21.648  52.709 12.809  1.00 29.18  ? 454  HIS A CG    1 
ATOM   3356 N  ND1   . HIS A 1 468 ? 21.062  53.133 13.983  1.00 29.34  ? 454  HIS A ND1   1 
ATOM   3357 C  CD2   . HIS A 1 468 ? 22.487  53.704 12.432  1.00 30.67  ? 454  HIS A CD2   1 
ATOM   3358 C  CE1   . HIS A 1 468 ? 21.532  54.324 14.307  1.00 30.13  ? 454  HIS A CE1   1 
ATOM   3359 N  NE2   . HIS A 1 468 ? 22.396  54.695 13.379  1.00 31.70  ? 454  HIS A NE2   1 
ATOM   3360 N  N     . PRO A 1 469 ? 20.894  49.849 8.778   1.00 24.35  ? 455  PRO A N     1 
ATOM   3361 C  CA    . PRO A 1 469 ? 20.632  48.514 8.230   1.00 23.85  ? 455  PRO A CA    1 
ATOM   3362 C  C     . PRO A 1 469 ? 21.837  47.615 8.454   1.00 23.21  ? 455  PRO A C     1 
ATOM   3363 O  O     . PRO A 1 469 ? 22.922  48.062 8.839   1.00 24.39  ? 455  PRO A O     1 
ATOM   3364 C  CB    . PRO A 1 469 ? 20.390  48.765 6.737   1.00 23.68  ? 455  PRO A CB    1 
ATOM   3365 C  CG    . PRO A 1 469 ? 21.163  50.002 6.440   1.00 23.25  ? 455  PRO A CG    1 
ATOM   3366 C  CD    . PRO A 1 469 ? 21.310  50.789 7.720   1.00 22.94  ? 455  PRO A CD    1 
ATOM   3367 N  N     . ILE A 1 470 ? 21.611  46.318 8.270   1.00 22.67  ? 456  ILE A N     1 
ATOM   3368 C  CA    . ILE A 1 470 ? 22.670  45.314 8.228   1.00 24.29  ? 456  ILE A CA    1 
ATOM   3369 C  C     . ILE A 1 470 ? 22.787  44.859 6.774   1.00 23.17  ? 456  ILE A C     1 
ATOM   3370 O  O     . ILE A 1 470 ? 21.937  44.114 6.271   1.00 23.34  ? 456  ILE A O     1 
ATOM   3371 C  CB    . ILE A 1 470 ? 22.387  44.135 9.168   1.00 24.21  ? 456  ILE A CB    1 
ATOM   3372 C  CG1   . ILE A 1 470 ? 22.330  44.602 10.634  1.00 25.95  ? 456  ILE A CG1   1 
ATOM   3373 C  CG2   . ILE A 1 470 ? 23.451  43.055 8.993   1.00 22.69  ? 456  ILE A CG2   1 
ATOM   3374 C  CD1   . ILE A 1 470 ? 21.494  43.718 11.529  1.00 24.46  ? 456  ILE A CD1   1 
ATOM   3375 N  N     . ILE A 1 471 ? 23.832  45.310 6.088   1.00 22.49  ? 457  ILE A N     1 
ATOM   3376 C  CA    . ILE A 1 471 ? 24.028  45.031 4.670   1.00 21.21  ? 457  ILE A CA    1 
ATOM   3377 C  C     . ILE A 1 471 ? 25.032  43.901 4.535   1.00 21.42  ? 457  ILE A C     1 
ATOM   3378 O  O     . ILE A 1 471 ? 26.199  44.053 4.917   1.00 24.04  ? 457  ILE A O     1 
ATOM   3379 C  CB    . ILE A 1 471 ? 24.510  46.275 3.907   1.00 22.04  ? 457  ILE A CB    1 
ATOM   3380 C  CG1   . ILE A 1 471 ? 23.570  47.444 4.177   1.00 22.40  ? 457  ILE A CG1   1 
ATOM   3381 C  CG2   . ILE A 1 471 ? 24.564  45.982 2.385   1.00 20.24  ? 457  ILE A CG2   1 
ATOM   3382 C  CD1   . ILE A 1 471 ? 24.033  48.747 3.594   1.00 20.98  ? 457  ILE A CD1   1 
ATOM   3383 N  N     . LEU A 1 472 ? 24.578  42.771 3.996   1.00 18.78  ? 458  LEU A N     1 
ATOM   3384 C  CA    . LEU A 1 472 ? 25.439  41.631 3.700   1.00 21.71  ? 458  LEU A CA    1 
ATOM   3385 C  C     . LEU A 1 472 ? 25.671  41.587 2.196   1.00 21.86  ? 458  LEU A C     1 
ATOM   3386 O  O     . LEU A 1 472 ? 24.766  41.244 1.437   1.00 20.14  ? 458  LEU A O     1 
ATOM   3387 C  CB    . LEU A 1 472 ? 24.820  40.320 4.188   1.00 21.76  ? 458  LEU A CB    1 
ATOM   3388 C  CG    . LEU A 1 472 ? 24.619  40.174 5.700   1.00 22.69  ? 458  LEU A CG    1 
ATOM   3389 C  CD1   . LEU A 1 472 ? 23.173  40.187 6.055   1.00 23.10  ? 458  LEU A CD1   1 
ATOM   3390 C  CD2   . LEU A 1 472 ? 25.290  38.908 6.215   1.00 24.42  ? 458  LEU A CD2   1 
ATOM   3391 N  N     . VAL A 1 473 ? 26.882  41.921 1.766   1.00 20.95  ? 459  VAL A N     1 
ATOM   3392 C  CA    . VAL A 1 473 ? 27.232  41.845 0.355   1.00 22.09  ? 459  VAL A CA    1 
ATOM   3393 C  C     . VAL A 1 473 ? 27.812  40.456 0.145   1.00 22.92  ? 459  VAL A C     1 
ATOM   3394 O  O     . VAL A 1 473 ? 28.855  40.121 0.712   1.00 24.05  ? 459  VAL A O     1 
ATOM   3395 C  CB    . VAL A 1 473 ? 28.224  42.943 -0.046  1.00 23.81  ? 459  VAL A CB    1 
ATOM   3396 C  CG1   . VAL A 1 473 ? 28.547  42.868 -1.549  1.00 24.02  ? 459  VAL A CG1   1 
ATOM   3397 C  CG2   . VAL A 1 473 ? 27.666  44.321 0.331   1.00 21.06  ? 459  VAL A CG2   1 
ATOM   3398 N  N     . LEU A 1 474 ? 27.099  39.622 -0.607  1.00 21.47  ? 460  LEU A N     1 
ATOM   3399 C  CA    . LEU A 1 474 ? 27.555  38.266 -0.886  1.00 24.51  ? 460  LEU A CA    1 
ATOM   3400 C  C     . LEU A 1 474 ? 28.547  38.348 -2.035  1.00 25.86  ? 460  LEU A C     1 
ATOM   3401 O  O     . LEU A 1 474 ? 28.160  38.418 -3.203  1.00 25.99  ? 460  LEU A O     1 
ATOM   3402 C  CB    . LEU A 1 474 ? 26.378  37.357 -1.209  1.00 25.76  ? 460  LEU A CB    1 
ATOM   3403 C  CG    . LEU A 1 474 ? 25.213  37.394 -0.217  1.00 24.94  ? 460  LEU A CG    1 
ATOM   3404 C  CD1   . LEU A 1 474 ? 24.240  36.274 -0.532  1.00 29.81  ? 460  LEU A CD1   1 
ATOM   3405 C  CD2   . LEU A 1 474 ? 25.718  37.303 1.233   1.00 25.90  ? 460  LEU A CD2   1 
ATOM   3406 N  N     . ASN A 1 475 ? 29.832  38.340 -1.698  1.00 27.51  ? 461  ASN A N     1 
ATOM   3407 C  CA    . ASN A 1 475 ? 30.908  38.595 -2.651  1.00 29.01  ? 461  ASN A CA    1 
ATOM   3408 C  C     . ASN A 1 475 ? 31.529  37.278 -3.094  1.00 31.17  ? 461  ASN A C     1 
ATOM   3409 O  O     . ASN A 1 475 ? 32.352  36.692 -2.389  1.00 31.44  ? 461  ASN A O     1 
ATOM   3410 C  CB    . ASN A 1 475 ? 31.974  39.499 -2.044  1.00 28.38  ? 461  ASN A CB    1 
ATOM   3411 C  CG    . ASN A 1 475 ? 33.070  39.849 -3.039  1.00 32.78  ? 461  ASN A CG    1 
ATOM   3412 O  OD1   . ASN A 1 475 ? 33.021  39.441 -4.207  1.00 34.58  ? 461  ASN A OD1   1 
ATOM   3413 N  ND2   . ASN A 1 475 ? 34.074  40.584 -2.581  1.00 30.07  ? 461  ASN A ND2   1 
ATOM   3414 N  N     . ASN A 1 476 ? 31.150  36.830 -4.280  1.00 32.05  ? 462  ASN A N     1 
ATOM   3415 C  CA    . ASN A 1 476 ? 31.843  35.741 -4.947  1.00 36.93  ? 462  ASN A CA    1 
ATOM   3416 C  C     . ASN A 1 476 ? 32.512  36.192 -6.247  1.00 40.84  ? 462  ASN A C     1 
ATOM   3417 O  O     . ASN A 1 476 ? 32.778  35.369 -7.129  1.00 43.72  ? 462  ASN A O     1 
ATOM   3418 C  CB    . ASN A 1 476 ? 30.897  34.553 -5.107  1.00 38.49  ? 462  ASN A CB    1 
ATOM   3419 C  CG    . ASN A 1 476 ? 29.780  34.807 -6.076  1.00 40.00  ? 462  ASN A CG    1 
ATOM   3420 O  OD1   . ASN A 1 476 ? 29.646  35.881 -6.666  1.00 34.59  ? 462  ASN A OD1   1 
ATOM   3421 N  ND2   . ASN A 1 476 ? 28.941  33.795 -6.241  1.00 45.13  ? 462  ASN A ND2   1 
ATOM   3422 N  N     . GLU A 1 477 ? 32.752  37.506 -6.379  1.00 40.16  ? 463  GLU A N     1 
ATOM   3423 C  CA    . GLU A 1 477 ? 33.673  38.079 -7.365  1.00 43.26  ? 463  GLU A CA    1 
ATOM   3424 C  C     . GLU A 1 477 ? 33.165  37.916 -8.800  1.00 45.29  ? 463  GLU A C     1 
ATOM   3425 O  O     . GLU A 1 477 ? 33.900  37.493 -9.692  1.00 49.03  ? 463  GLU A O     1 
ATOM   3426 C  CB    . GLU A 1 477 ? 35.068  37.471 -7.202  1.00 49.66  ? 463  GLU A CB    1 
ATOM   3427 C  CG    . GLU A 1 477 ? 35.751  37.787 -5.881  1.00 49.95  ? 463  GLU A CG    1 
ATOM   3428 C  CD    . GLU A 1 477 ? 37.263  37.855 -6.004  1.00 68.58  ? 463  GLU A CD    1 
ATOM   3429 O  OE1   . GLU A 1 477 ? 37.803  37.356 -7.019  1.00 63.72  ? 463  GLU A OE1   1 
ATOM   3430 O  OE2   . GLU A 1 477 ? 37.907  38.413 -5.089  1.00 66.16  ? 463  GLU A OE2   1 
ATOM   3431 N  N     . GLY A 1 478 ? 31.909  38.265 -9.020  1.00 42.28  ? 464  GLY A N     1 
ATOM   3432 C  CA    . GLY A 1 478 ? 31.348  38.256 -10.357 1.00 46.98  ? 464  GLY A CA    1 
ATOM   3433 C  C     . GLY A 1 478 ? 29.869  37.923 -10.336 1.00 44.30  ? 464  GLY A C     1 
ATOM   3434 O  O     . GLY A 1 478 ? 29.232  37.925 -9.287  1.00 39.47  ? 464  GLY A O     1 
ATOM   3435 N  N     . TYR A 1 479 ? 29.339  37.676 -11.545 1.00 48.46  ? 465  TYR A N     1 
ATOM   3436 C  CA    . TYR A 1 479 ? 27.927  37.345 -11.790 1.00 48.90  ? 465  TYR A CA    1 
ATOM   3437 C  C     . TYR A 1 479 ? 27.716  35.826 -11.744 1.00 57.65  ? 465  TYR A C     1 
ATOM   3438 O  O     . TYR A 1 479 ? 27.695  35.142 -12.767 1.00 64.68  ? 465  TYR A O     1 
ATOM   3439 C  CB    . TYR A 1 479 ? 27.470  37.886 -13.147 1.00 51.87  ? 465  TYR A CB    1 
ATOM   3440 C  CG    . TYR A 1 479 ? 27.412  39.396 -13.384 1.00 46.31  ? 465  TYR A CG    1 
ATOM   3441 C  CD1   . TYR A 1 479 ? 27.118  40.301 -12.358 1.00 40.90  ? 465  TYR A CD1   1 
ATOM   3442 C  CD2   . TYR A 1 479 ? 27.585  39.903 -14.672 1.00 45.52  ? 465  TYR A CD2   1 
ATOM   3443 C  CE1   . TYR A 1 479 ? 27.031  41.679 -12.612 1.00 37.12  ? 465  TYR A CE1   1 
ATOM   3444 C  CE2   . TYR A 1 479 ? 27.505  41.261 -14.936 1.00 41.99  ? 465  TYR A CE2   1 
ATOM   3445 C  CZ    . TYR A 1 479 ? 27.231  42.148 -13.909 1.00 40.68  ? 465  TYR A CZ    1 
ATOM   3446 O  OH    . TYR A 1 479 ? 27.162  43.499 -14.194 1.00 36.18  ? 465  TYR A OH    1 
ATOM   3447 N  N     . THR A 1 480 ? 27.563  35.280 -10.534 1.00 54.45  ? 466  THR A N     1 
ATOM   3448 C  CA    . THR A 1 480 ? 27.474  33.822 -10.389 1.00 60.57  ? 466  THR A CA    1 
ATOM   3449 C  C     . THR A 1 480 ? 26.177  33.234 -10.939 1.00 69.45  ? 466  THR A C     1 
ATOM   3450 O  O     . THR A 1 480 ? 26.196  32.154 -11.545 1.00 73.18  ? 466  THR A O     1 
ATOM   3451 C  CB    . THR A 1 480 ? 27.637  33.428 -8.930  1.00 56.41  ? 466  THR A CB    1 
ATOM   3452 O  OG1   . THR A 1 480 ? 28.930  33.847 -8.490  1.00 55.87  ? 466  THR A OG1   1 
ATOM   3453 C  CG2   . THR A 1 480 ? 27.502  31.917 -8.740  1.00 61.05  ? 466  THR A CG2   1 
ATOM   3454 N  N     . VAL A 1 481 ? 25.039  33.900 -10.717 1.00 77.53  ? 467  VAL A N     1 
ATOM   3455 C  CA    . VAL A 1 481 ? 23.755  33.337 -11.142 1.00 75.89  ? 467  VAL A CA    1 
ATOM   3456 C  C     . VAL A 1 481 ? 23.791  33.049 -12.635 1.00 82.02  ? 467  VAL A C     1 
ATOM   3457 O  O     . VAL A 1 481 ? 23.408  31.967 -13.098 1.00 84.04  ? 467  VAL A O     1 
ATOM   3458 C  CB    . VAL A 1 481 ? 22.615  34.315 -10.814 1.00 61.95  ? 467  VAL A CB    1 
ATOM   3459 C  CG1   . VAL A 1 481 ? 23.130  35.723 -10.955 1.00 51.31  ? 467  VAL A CG1   1 
ATOM   3460 C  CG2   . VAL A 1 481 ? 21.406  34.086 -11.705 1.00 60.05  ? 467  VAL A CG2   1 
ATOM   3461 N  N     . GLU A 1 482 ? 24.267  33.979 -13.463 1.00 78.91  ? 468  GLU A N     1 
ATOM   3462 C  CA    . GLU A 1 482 ? 24.343  33.696 -14.912 1.00 76.61  ? 468  GLU A CA    1 
ATOM   3463 C  C     . GLU A 1 482 ? 25.534  32.814 -15.170 1.00 80.42  ? 468  GLU A C     1 
ATOM   3464 O  O     . GLU A 1 482 ? 25.595  32.162 -16.158 1.00 82.17  ? 468  GLU A O     1 
ATOM   3465 C  CB    . GLU A 1 482 ? 24.418  34.907 -15.826 1.00 70.61  ? 468  GLU A CB    1 
ATOM   3466 C  CG    . GLU A 1 482 ? 24.204  36.263 -15.243 1.00 61.81  ? 468  GLU A CG    1 
ATOM   3467 C  CD    . GLU A 1 482 ? 23.045  36.975 -15.898 1.00 57.49  ? 468  GLU A CD    1 
ATOM   3468 O  OE1   . GLU A 1 482 ? 23.250  37.830 -16.715 1.00 51.70  ? 468  GLU A OE1   1 
ATOM   3469 O  OE2   . GLU A 1 482 ? 21.924  36.702 -15.554 1.00 57.19  ? 468  GLU A OE2   1 
ATOM   3470 N  N     . ARG A 1 483 ? 26.560  32.910 -14.356 1.00 79.83  ? 469  ARG A N     1 
ATOM   3471 C  CA    . ARG A 1 483 ? 27.631  31.939 -14.542 1.00 82.04  ? 469  ARG A CA    1 
ATOM   3472 C  C     . ARG A 1 483 ? 27.053  30.533 -14.577 1.00 85.87  ? 469  ARG A C     1 
ATOM   3473 O  O     . ARG A 1 483 ? 27.397  29.724 -15.448 1.00 87.62  ? 469  ARG A O     1 
ATOM   3474 C  CB    . ARG A 1 483 ? 28.644  32.075 -13.399 1.00 77.37  ? 469  ARG A CB    1 
ATOM   3475 C  CG    . ARG A 1 483 ? 29.764  33.079 -13.624 1.00 75.31  ? 469  ARG A CG    1 
ATOM   3476 C  CD    . ARG A 1 483 ? 31.086  32.627 -13.021 1.00 74.57  ? 469  ARG A CD    1 
ATOM   3477 N  NE    . ARG A 1 483 ? 31.698  33.702 -12.244 1.00 74.37  ? 469  ARG A NE    1 
ATOM   3478 C  CZ    . ARG A 1 483 ? 32.209  34.817 -12.754 1.00 67.47  ? 469  ARG A CZ    1 
ATOM   3479 N  NH1   . ARG A 1 483 ? 32.237  35.035 -14.059 1.00 68.65  ? 469  ARG A NH1   1 
ATOM   3480 N  NH2   . ARG A 1 483 ? 32.697  35.741 -11.931 1.00 60.86  ? 469  ARG A NH2   1 
ATOM   3481 N  N     . ALA A 1 484 ? 26.146  30.237 -13.643 1.00 85.08  ? 470  ALA A N     1 
ATOM   3482 C  CA    . ALA A 1 484 ? 25.508  28.926 -13.600 1.00 88.19  ? 470  ALA A CA    1 
ATOM   3483 C  C     . ALA A 1 484 ? 24.707  28.639 -14.869 1.00 91.77  ? 470  ALA A C     1 
ATOM   3484 O  O     . ALA A 1 484 ? 24.803  27.546 -15.439 1.00 92.62  ? 470  ALA A O     1 
ATOM   3485 C  CB    . ALA A 1 484 ? 24.621  28.822 -12.357 1.00 84.62  ? 470  ALA A CB    1 
ATOM   3486 N  N     . ILE A 1 485 ? 23.909  29.607 -15.333 1.00 91.36  ? 471  ILE A N     1 
ATOM   3487 C  CA    . ILE A 1 485 ? 23.027  29.346 -16.472 1.00 92.28  ? 471  ILE A CA    1 
ATOM   3488 C  C     . ILE A 1 485 ? 23.814  29.314 -17.788 1.00 91.05  ? 471  ILE A C     1 
ATOM   3489 O  O     . ILE A 1 485 ? 23.645  28.388 -18.593 1.00 90.39  ? 471  ILE A O     1 
ATOM   3490 C  CB    . ILE A 1 485 ? 21.816  30.314 -16.459 1.00 90.90  ? 471  ILE A CB    1 
ATOM   3491 C  CG1   . ILE A 1 485 ? 21.960  31.584 -17.315 1.00 82.97  ? 471  ILE A CG1   1 
ATOM   3492 C  CG2   . ILE A 1 485 ? 21.368  30.610 -15.019 1.00 88.59  ? 471  ILE A CG2   1 
ATOM   3493 C  CD1   . ILE A 1 485 ? 21.579  31.402 -18.761 1.00 72.77  ? 471  ILE A CD1   1 
ATOM   3494 N  N     . HIS A 1 486 ? 24.690  30.297 -18.034 1.00 88.02  ? 472  HIS A N     1 
ATOM   3495 C  CA    . HIS A 1 486 ? 25.411  30.277 -19.306 1.00 85.84  ? 472  HIS A CA    1 
ATOM   3496 C  C     . HIS A 1 486 ? 26.731  31.034 -19.253 1.00 84.17  ? 472  HIS A C     1 
ATOM   3497 O  O     . HIS A 1 486 ? 26.791  32.171 -18.773 1.00 80.25  ? 472  HIS A O     1 
ATOM   3498 C  CB    . HIS A 1 486 ? 24.567  30.845 -20.447 1.00 78.11  ? 472  HIS A CB    1 
ATOM   3499 C  CG    . HIS A 1 486 ? 25.179  30.607 -21.787 1.00 74.90  ? 472  HIS A CG    1 
ATOM   3500 N  ND1   . HIS A 1 486 ? 25.761  29.402 -22.110 1.00 80.63  ? 472  HIS A ND1   1 
ATOM   3501 C  CD2   . HIS A 1 486 ? 25.305  31.394 -22.881 1.00 60.29  ? 472  HIS A CD2   1 
ATOM   3502 C  CE1   . HIS A 1 486 ? 26.224  29.456 -23.345 1.00 74.43  ? 472  HIS A CE1   1 
ATOM   3503 N  NE2   . HIS A 1 486 ? 25.959  30.654 -23.836 1.00 62.74  ? 472  HIS A NE2   1 
ATOM   3504 N  N     . GLY A 1 487 ? 27.767  30.404 -19.819 1.00 84.55  ? 473  GLY A N     1 
ATOM   3505 C  CA    . GLY A 1 487 ? 29.082  30.980 -19.974 1.00 83.62  ? 473  GLY A CA    1 
ATOM   3506 C  C     . GLY A 1 487 ? 29.755  31.269 -18.648 1.00 87.89  ? 473  GLY A C     1 
ATOM   3507 O  O     . GLY A 1 487 ? 30.063  32.422 -18.330 1.00 84.12  ? 473  GLY A O     1 
ATOM   3508 N  N     . PRO A 1 488 ? 30.010  30.224 -17.850 1.00 94.56  ? 474  PRO A N     1 
ATOM   3509 C  CA    . PRO A 1 488 ? 30.635  30.455 -16.534 1.00 95.66  ? 474  PRO A CA    1 
ATOM   3510 C  C     . PRO A 1 488 ? 32.046  31.012 -16.625 1.00 87.52  ? 474  PRO A C     1 
ATOM   3511 O  O     . PRO A 1 488 ? 32.471  31.755 -15.732 1.00 83.54  ? 474  PRO A O     1 
ATOM   3512 C  CB    . PRO A 1 488 ? 30.601  29.068 -15.867 1.00 90.50  ? 474  PRO A CB    1 
ATOM   3513 C  CG    . PRO A 1 488 ? 30.124  28.089 -16.926 1.00 88.67  ? 474  PRO A CG    1 
ATOM   3514 C  CD    . PRO A 1 488 ? 30.049  28.803 -18.240 1.00 90.04  ? 474  PRO A CD    1 
ATOM   3515 N  N     . GLU A 1 489 ? 32.781  30.680 -17.684 1.00 88.40  ? 475  GLU A N     1 
ATOM   3516 C  CA    . GLU A 1 489 ? 34.132  31.178 -17.899 1.00 88.90  ? 475  GLU A CA    1 
ATOM   3517 C  C     . GLU A 1 489 ? 34.167  32.420 -18.783 1.00 91.47  ? 475  GLU A C     1 
ATOM   3518 O  O     . GLU A 1 489 ? 35.259  32.901 -19.109 1.00 83.82  ? 475  GLU A O     1 
ATOM   3519 C  CB    . GLU A 1 489 ? 35.001  30.081 -18.522 1.00 87.71  ? 475  GLU A CB    1 
ATOM   3520 C  CG    . GLU A 1 489 ? 35.804  29.250 -17.526 1.00 88.92  ? 475  GLU A CG    1 
ATOM   3521 C  CD    . GLU A 1 489 ? 36.310  27.950 -18.137 1.00 95.21  ? 475  GLU A CD    1 
ATOM   3522 O  OE1   . GLU A 1 489 ? 35.758  27.522 -19.175 1.00 97.74  ? 475  GLU A OE1   1 
ATOM   3523 O  OE2   . GLU A 1 489 ? 37.261  27.356 -17.585 1.00 96.80  ? 475  GLU A OE2   1 
ATOM   3524 N  N     . GLN A 1 490 ? 33.008  32.940 -19.186 1.00 89.64  ? 476  GLN A N     1 
ATOM   3525 C  CA    . GLN A 1 490 ? 32.958  34.084 -20.086 1.00 76.52  ? 476  GLN A CA    1 
ATOM   3526 C  C     . GLN A 1 490 ? 33.187  35.388 -19.333 1.00 70.41  ? 476  GLN A C     1 
ATOM   3527 O  O     . GLN A 1 490 ? 32.712  35.573 -18.208 1.00 68.32  ? 476  GLN A O     1 
ATOM   3528 C  CB    . GLN A 1 490 ? 31.629  34.128 -20.841 1.00 68.60  ? 476  GLN A CB    1 
ATOM   3529 C  CG    . GLN A 1 490 ? 31.501  33.060 -21.928 1.00 65.70  ? 476  GLN A CG    1 
ATOM   3530 C  CD    . GLN A 1 490 ? 32.412  33.312 -23.132 1.00 62.81  ? 476  GLN A CD    1 
ATOM   3531 O  OE1   . GLN A 1 490 ? 33.608  33.571 -22.981 1.00 65.51  ? 476  GLN A OE1   1 
ATOM   3532 N  NE2   . GLN A 1 490 ? 31.844  33.228 -24.337 1.00 53.10  ? 476  GLN A NE2   1 
ATOM   3533 N  N     . ARG A 1 491 ? 33.935  36.293 -19.969 1.00 67.60  ? 477  ARG A N     1 
ATOM   3534 C  CA    . ARG A 1 491 ? 34.342  37.530 -19.317 1.00 65.32  ? 477  ARG A CA    1 
ATOM   3535 C  C     . ARG A 1 491 ? 33.170  38.458 -19.013 1.00 63.28  ? 477  ARG A C     1 
ATOM   3536 O  O     . ARG A 1 491 ? 33.261  39.258 -18.071 1.00 62.05  ? 477  ARG A O     1 
ATOM   3537 C  CB    . ARG A 1 491 ? 35.374  38.242 -20.201 1.00 62.59  ? 477  ARG A CB    1 
ATOM   3538 C  CG    . ARG A 1 491 ? 35.289  39.758 -20.191 1.00 60.34  ? 477  ARG A CG    1 
ATOM   3539 C  CD    . ARG A 1 491 ? 36.432  40.412 -20.952 1.00 59.07  ? 477  ARG A CD    1 
ATOM   3540 N  NE    . ARG A 1 491 ? 36.086  40.661 -22.347 1.00 59.43  ? 477  ARG A NE    1 
ATOM   3541 C  CZ    . ARG A 1 491 ? 35.497  41.767 -22.784 1.00 42.74  ? 477  ARG A CZ    1 
ATOM   3542 N  NH1   . ARG A 1 491 ? 35.078  42.706 -21.946 1.00 38.23  ? 477  ARG A NH1   1 
ATOM   3543 N  NH2   . ARG A 1 491 ? 35.314  41.933 -24.090 1.00 41.88  ? 477  ARG A NH2   1 
ATOM   3544 N  N     . TYR A 1 492 ? 32.046  38.322 -19.725 1.00 59.94  ? 478  TYR A N     1 
ATOM   3545 C  CA    . TYR A 1 492 ? 30.911  39.200 -19.457 1.00 57.67  ? 478  TYR A CA    1 
ATOM   3546 C  C     . TYR A 1 492 ? 30.269  38.943 -18.102 1.00 58.30  ? 478  TYR A C     1 
ATOM   3547 O  O     . TYR A 1 492 ? 29.519  39.796 -17.618 1.00 53.85  ? 478  TYR A O     1 
ATOM   3548 C  CB    . TYR A 1 492 ? 29.867  39.097 -20.575 1.00 50.86  ? 478  TYR A CB    1 
ATOM   3549 C  CG    . TYR A 1 492 ? 29.316  37.716 -20.913 1.00 60.57  ? 478  TYR A CG    1 
ATOM   3550 C  CD1   . TYR A 1 492 ? 28.595  36.962 -19.987 1.00 57.91  ? 478  TYR A CD1   1 
ATOM   3551 C  CD2   . TYR A 1 492 ? 29.492  37.189 -22.189 1.00 54.18  ? 478  TYR A CD2   1 
ATOM   3552 C  CE1   . TYR A 1 492 ? 28.083  35.712 -20.326 1.00 56.99  ? 478  TYR A CE1   1 
ATOM   3553 C  CE2   . TYR A 1 492 ? 28.988  35.951 -22.535 1.00 49.00  ? 478  TYR A CE2   1 
ATOM   3554 C  CZ    . TYR A 1 492 ? 28.285  35.215 -21.606 1.00 52.13  ? 478  TYR A CZ    1 
ATOM   3555 O  OH    . TYR A 1 492 ? 27.788  33.984 -21.984 1.00 52.67  ? 478  TYR A OH    1 
ATOM   3556 N  N     . ASN A 1 493 ? 30.554  37.809 -17.473 1.00 61.29  ? 479  ASN A N     1 
ATOM   3557 C  CA    . ASN A 1 493 ? 30.087  37.554 -16.119 1.00 60.74  ? 479  ASN A CA    1 
ATOM   3558 C  C     . ASN A 1 493 ? 31.056  38.072 -15.061 1.00 61.13  ? 479  ASN A C     1 
ATOM   3559 O  O     . ASN A 1 493 ? 30.758  37.970 -13.866 1.00 58.16  ? 479  ASN A O     1 
ATOM   3560 C  CB    . ASN A 1 493 ? 29.825  36.055 -15.930 1.00 64.55  ? 479  ASN A CB    1 
ATOM   3561 C  CG    . ASN A 1 493 ? 28.507  35.607 -16.562 1.00 69.26  ? 479  ASN A CG    1 
ATOM   3562 O  OD1   . ASN A 1 493 ? 27.631  36.425 -16.847 1.00 63.46  ? 479  ASN A OD1   1 
ATOM   3563 N  ND2   . ASN A 1 493 ? 28.379  34.306 -16.811 1.00 74.68  ? 479  ASN A ND2   1 
ATOM   3564 N  N     . ASP A 1 494 ? 32.193  38.638 -15.467 1.00 61.11  ? 480  ASP A N     1 
ATOM   3565 C  CA    . ASP A 1 494 ? 33.077  39.320 -14.532 1.00 58.21  ? 480  ASP A CA    1 
ATOM   3566 C  C     . ASP A 1 494 ? 32.616  40.759 -14.316 1.00 54.71  ? 480  ASP A C     1 
ATOM   3567 O  O     . ASP A 1 494 ? 31.918  41.351 -15.145 1.00 63.16  ? 480  ASP A O     1 
ATOM   3568 C  CB    . ASP A 1 494 ? 34.525  39.330 -15.028 1.00 59.05  ? 480  ASP A CB    1 
ATOM   3569 C  CG    . ASP A 1 494 ? 35.040  37.952 -15.366 1.00 62.83  ? 480  ASP A CG    1 
ATOM   3570 O  OD1   . ASP A 1 494 ? 34.861  37.036 -14.537 1.00 64.06  ? 480  ASP A OD1   1 
ATOM   3571 O  OD2   . ASP A 1 494 ? 35.667  37.797 -16.436 1.00 62.79  ? 480  ASP A OD2   1 
ATOM   3572 N  N     . ILE A 1 495 ? 33.029  41.325 -13.184 1.00 46.85  ? 481  ILE A N     1 
ATOM   3573 C  CA    . ILE A 1 495 ? 32.727  42.705 -12.831 1.00 41.80  ? 481  ILE A CA    1 
ATOM   3574 C  C     . ILE A 1 495 ? 34.005  43.375 -12.346 1.00 37.21  ? 481  ILE A C     1 
ATOM   3575 O  O     . ILE A 1 495 ? 35.010  42.724 -12.073 1.00 35.66  ? 481  ILE A O     1 
ATOM   3576 C  CB    . ILE A 1 495 ? 31.646  42.814 -11.735 1.00 39.27  ? 481  ILE A CB    1 
ATOM   3577 C  CG1   . ILE A 1 495 ? 32.102  42.059 -10.481 1.00 37.93  ? 481  ILE A CG1   1 
ATOM   3578 C  CG2   . ILE A 1 495 ? 30.315  42.304 -12.243 1.00 42.00  ? 481  ILE A CG2   1 
ATOM   3579 C  CD1   . ILE A 1 495 ? 31.001  41.767 -9.498  1.00 34.55  ? 481  ILE A CD1   1 
ATOM   3580 N  N     . ALA A 1 496 ? 33.950  44.699 -12.242 1.00 33.04  ? 482  ALA A N     1 
ATOM   3581 C  CA    . ALA A 1 496 ? 34.946  45.419 -11.464 1.00 27.51  ? 482  ALA A CA    1 
ATOM   3582 C  C     . ALA A 1 496 ? 34.895  44.953 -10.013 1.00 29.10  ? 482  ALA A C     1 
ATOM   3583 O  O     . ALA A 1 496 ? 33.813  44.779 -9.436  1.00 26.61  ? 482  ALA A O     1 
ATOM   3584 C  CB    . ALA A 1 496 ? 34.696  46.924 -11.547 1.00 24.94  ? 482  ALA A CB    1 
ATOM   3585 N  N     . LEU A 1 497 ? 36.070  44.742 -9.424  1.00 25.67  ? 483  LEU A N     1 
ATOM   3586 C  CA    . LEU A 1 497 ? 36.184  44.268 -8.043  1.00 28.00  ? 483  LEU A CA    1 
ATOM   3587 C  C     . LEU A 1 497 ? 36.357  45.463 -7.107  1.00 25.31  ? 483  LEU A C     1 
ATOM   3588 O  O     . LEU A 1 497 ? 37.373  46.169 -7.159  1.00 24.78  ? 483  LEU A O     1 
ATOM   3589 C  CB    . LEU A 1 497 ? 37.330  43.269 -7.902  1.00 27.28  ? 483  LEU A CB    1 
ATOM   3590 C  CG    . LEU A 1 497 ? 37.210  42.111 -8.906  1.00 30.39  ? 483  LEU A CG    1 
ATOM   3591 C  CD1   . LEU A 1 497 ? 38.389  41.121 -8.833  1.00 29.53  ? 483  LEU A CD1   1 
ATOM   3592 C  CD2   . LEU A 1 497 ? 35.864  41.394 -8.771  1.00 32.11  ? 483  LEU A CD2   1 
ATOM   3593 N  N     . TRP A 1 498 ? 35.366  45.679 -6.252  1.00 22.27  ? 484  TRP A N     1 
ATOM   3594 C  CA    . TRP A 1 498 ? 35.288  46.825 -5.361  1.00 22.82  ? 484  TRP A CA    1 
ATOM   3595 C  C     . TRP A 1 498 ? 35.850  46.510 -3.976  1.00 25.13  ? 484  TRP A C     1 
ATOM   3596 O  O     . TRP A 1 498 ? 35.950  45.354 -3.561  1.00 24.59  ? 484  TRP A O     1 
ATOM   3597 C  CB    . TRP A 1 498 ? 33.836  47.273 -5.227  1.00 22.12  ? 484  TRP A CB    1 
ATOM   3598 C  CG    . TRP A 1 498 ? 33.327  47.976 -6.436  1.00 22.35  ? 484  TRP A CG    1 
ATOM   3599 C  CD1   . TRP A 1 498 ? 33.964  48.121 -7.637  1.00 21.83  ? 484  TRP A CD1   1 
ATOM   3600 C  CD2   . TRP A 1 498 ? 32.069  48.640 -6.563  1.00 21.28  ? 484  TRP A CD2   1 
ATOM   3601 N  NE1   . TRP A 1 498 ? 33.176  48.837 -8.505  1.00 23.18  ? 484  TRP A NE1   1 
ATOM   3602 C  CE2   . TRP A 1 498 ? 32.005  49.167 -7.872  1.00 21.38  ? 484  TRP A CE2   1 
ATOM   3603 C  CE3   . TRP A 1 498 ? 30.987  48.835 -5.698  1.00 22.71  ? 484  TRP A CE3   1 
ATOM   3604 C  CZ2   . TRP A 1 498 ? 30.908  49.891 -8.335  1.00 21.42  ? 484  TRP A CZ2   1 
ATOM   3605 C  CZ3   . TRP A 1 498 ? 29.896  49.551 -6.160  1.00 21.10  ? 484  TRP A CZ3   1 
ATOM   3606 C  CH2   . TRP A 1 498 ? 29.866  50.064 -7.474  1.00 20.76  ? 484  TRP A CH2   1 
ATOM   3607 N  N     . ASN A 1 499 ? 36.193  47.576 -3.251  1.00 24.21  ? 485  ASN A N     1 
ATOM   3608 C  CA    . ASN A 1 499 ? 36.676  47.480 -1.879  1.00 26.45  ? 485  ASN A CA    1 
ATOM   3609 C  C     . ASN A 1 499 ? 35.500  47.777 -0.950  1.00 25.23  ? 485  ASN A C     1 
ATOM   3610 O  O     . ASN A 1 499 ? 35.370  48.862 -0.397  1.00 23.92  ? 485  ASN A O     1 
ATOM   3611 C  CB    . ASN A 1 499 ? 37.832  48.446 -1.664  1.00 27.18  ? 485  ASN A CB    1 
ATOM   3612 C  CG    . ASN A 1 499 ? 38.670  48.082 -0.471  1.00 29.44  ? 485  ASN A CG    1 
ATOM   3613 O  OD1   . ASN A 1 499 ? 38.414  47.073 0.189   1.00 32.24  ? 485  ASN A OD1   1 
ATOM   3614 N  ND2   . ASN A 1 499 ? 39.671  48.913 -0.166  1.00 31.57  ? 485  ASN A ND2   1 
ATOM   3615 N  N     . TRP A 1 500 ? 34.632  46.774 -0.782  1.00 23.30  ? 486  TRP A N     1 
ATOM   3616 C  CA    . TRP A 1 500 ? 33.338  47.002 -0.151  1.00 23.83  ? 486  TRP A CA    1 
ATOM   3617 C  C     . TRP A 1 500 ? 33.475  47.655 1.219   1.00 23.46  ? 486  TRP A C     1 
ATOM   3618 O  O     . TRP A 1 500 ? 32.758  48.614 1.526   1.00 23.62  ? 486  TRP A O     1 
ATOM   3619 C  CB    . TRP A 1 500 ? 32.572  45.679 -0.068  1.00 24.01  ? 486  TRP A CB    1 
ATOM   3620 C  CG    . TRP A 1 500 ? 32.231  45.170 -1.426  1.00 24.80  ? 486  TRP A CG    1 
ATOM   3621 C  CD1   . TRP A 1 500 ? 32.913  44.234 -2.141  1.00 25.75  ? 486  TRP A CD1   1 
ATOM   3622 C  CD2   . TRP A 1 500 ? 31.154  45.614 -2.269  1.00 23.29  ? 486  TRP A CD2   1 
ATOM   3623 N  NE1   . TRP A 1 500 ? 32.309  44.038 -3.359  1.00 24.85  ? 486  TRP A NE1   1 
ATOM   3624 C  CE2   . TRP A 1 500 ? 31.229  44.876 -3.464  1.00 23.99  ? 486  TRP A CE2   1 
ATOM   3625 C  CE3   . TRP A 1 500 ? 30.121  46.543 -2.115  1.00 22.13  ? 486  TRP A CE3   1 
ATOM   3626 C  CZ2   . TRP A 1 500 ? 30.320  45.048 -4.511  1.00 22.74  ? 486  TRP A CZ2   1 
ATOM   3627 C  CZ3   . TRP A 1 500 ? 29.217  46.715 -3.153  1.00 21.70  ? 486  TRP A CZ3   1 
ATOM   3628 C  CH2   . TRP A 1 500 ? 29.317  45.970 -4.335  1.00 21.62  ? 486  TRP A CH2   1 
ATOM   3629 N  N     . THR A 1 501 ? 34.433  47.204 2.036   1.00 25.99  ? 487  THR A N     1 
ATOM   3630 C  CA    . THR A 1 501 ? 34.515  47.737 3.394   1.00 26.39  ? 487  THR A CA    1 
ATOM   3631 C  C     . THR A 1 501 ? 34.996  49.182 3.435   1.00 27.58  ? 487  THR A C     1 
ATOM   3632 O  O     . THR A 1 501 ? 35.058  49.757 4.525   1.00 27.28  ? 487  THR A O     1 
ATOM   3633 C  CB    . THR A 1 501 ? 35.407  46.863 4.286   1.00 27.23  ? 487  THR A CB    1 
ATOM   3634 O  OG1   . THR A 1 501 ? 36.741  46.820 3.773   1.00 28.76  ? 487  THR A OG1   1 
ATOM   3635 C  CG2   . THR A 1 501 ? 34.850  45.445 4.338   1.00 28.38  ? 487  THR A CG2   1 
ATOM   3636 N  N     . GLN A 1 502 ? 35.390  49.766 2.299   1.00 25.21  ? 488  GLN A N     1 
ATOM   3637 C  CA    . GLN A 1 502 ? 35.774  51.170 2.252   1.00 27.15  ? 488  GLN A CA    1 
ATOM   3638 C  C     . GLN A 1 502 ? 34.699  52.077 1.669   1.00 26.37  ? 488  GLN A C     1 
ATOM   3639 O  O     . GLN A 1 502 ? 34.864  53.298 1.684   1.00 25.62  ? 488  GLN A O     1 
ATOM   3640 C  CB    . GLN A 1 502 ? 37.079  51.340 1.467   1.00 27.10  ? 488  GLN A CB    1 
ATOM   3641 C  CG    . GLN A 1 502 ? 38.270  50.897 2.254   1.00 31.14  ? 488  GLN A CG    1 
ATOM   3642 C  CD    . GLN A 1 502 ? 38.443  51.726 3.522   1.00 33.48  ? 488  GLN A CD    1 
ATOM   3643 O  OE1   . GLN A 1 502 ? 38.383  52.959 3.489   1.00 35.66  ? 488  GLN A OE1   1 
ATOM   3644 N  NE2   . GLN A 1 502 ? 38.576  51.049 4.651   1.00 31.23  ? 488  GLN A NE2   1 
ATOM   3645 N  N     . ILE A 1 503 ? 33.599  51.523 1.177   1.00 25.24  ? 489  ILE A N     1 
ATOM   3646 C  CA    . ILE A 1 503 ? 32.583  52.338 0.526   1.00 24.69  ? 489  ILE A CA    1 
ATOM   3647 C  C     . ILE A 1 503 ? 31.909  53.294 1.510   1.00 25.03  ? 489  ILE A C     1 
ATOM   3648 O  O     . ILE A 1 503 ? 31.762  54.476 1.174   1.00 26.87  ? 489  ILE A O     1 
ATOM   3649 C  CB    . ILE A 1 503 ? 31.563  51.457 -0.206  1.00 25.13  ? 489  ILE A CB    1 
ATOM   3650 C  CG1   . ILE A 1 503 ? 32.281  50.733 -1.346  1.00 24.09  ? 489  ILE A CG1   1 
ATOM   3651 C  CG2   . ILE A 1 503 ? 30.456  52.325 -0.797  1.00 23.11  ? 489  ILE A CG2   1 
ATOM   3652 C  CD1   . ILE A 1 503 ? 31.412  49.783 -2.143  1.00 25.35  ? 489  ILE A CD1   1 
ATOM   3653 N  N     . PRO A 1 504 ? 31.501  52.877 2.720   1.00 26.24  ? 490  PRO A N     1 
ATOM   3654 C  CA    . PRO A 1 504 ? 30.879  53.863 3.628   1.00 26.46  ? 490  PRO A CA    1 
ATOM   3655 C  C     . PRO A 1 504 ? 31.742  55.091 3.886   1.00 27.25  ? 490  PRO A C     1 
ATOM   3656 O  O     . PRO A 1 504 ? 31.222  56.218 3.905   1.00 27.14  ? 490  PRO A O     1 
ATOM   3657 C  CB    . PRO A 1 504 ? 30.634  53.042 4.900   1.00 26.68  ? 490  PRO A CB    1 
ATOM   3658 C  CG    . PRO A 1 504 ? 30.369  51.645 4.343   1.00 24.68  ? 490  PRO A CG    1 
ATOM   3659 C  CD    . PRO A 1 504 ? 31.419  51.511 3.284   1.00 24.03  ? 490  PRO A CD    1 
ATOM   3660 N  N     . GLN A 1 505 ? 33.054  54.911 4.034   1.00 25.52  ? 491  GLN A N     1 
ATOM   3661 C  CA    . GLN A 1 505 ? 33.988  56.015 4.229   1.00 28.47  ? 491  GLN A CA    1 
ATOM   3662 C  C     . GLN A 1 505 ? 34.264  56.811 2.956   1.00 27.39  ? 491  GLN A C     1 
ATOM   3663 O  O     . GLN A 1 505 ? 34.821  57.911 3.043   1.00 24.82  ? 491  GLN A O     1 
ATOM   3664 C  CB    . GLN A 1 505 ? 35.306  55.487 4.831   1.00 29.97  ? 491  GLN A CB    1 
ATOM   3665 C  CG    . GLN A 1 505 ? 35.181  54.604 6.124   1.00 33.20  ? 491  GLN A CG    1 
ATOM   3666 C  CD    . GLN A 1 505 ? 34.460  53.242 5.955   1.00 40.15  ? 491  GLN A CD    1 
ATOM   3667 O  OE1   . GLN A 1 505 ? 34.480  52.625 4.886   1.00 30.75  ? 491  GLN A OE1   1 
ATOM   3668 N  NE2   . GLN A 1 505 ? 33.859  52.756 7.051   1.00 36.16  ? 491  GLN A NE2   1 
ATOM   3669 N  N     . ALA A 1 506 ? 33.890  56.304 1.784   1.00 24.99  ? 492  ALA A N     1 
ATOM   3670 C  CA    . ALA A 1 506 ? 33.959  57.137 0.589   1.00 25.03  ? 492  ALA A CA    1 
ATOM   3671 C  C     . ALA A 1 506 ? 32.695  57.959 0.390   1.00 25.19  ? 492  ALA A C     1 
ATOM   3672 O  O     . ALA A 1 506 ? 32.766  59.095 -0.092  1.00 22.61  ? 492  ALA A O     1 
ATOM   3673 C  CB    . ALA A 1 506 ? 34.212  56.276 -0.653  1.00 25.57  ? 492  ALA A CB    1 
ATOM   3674 N  N     . LEU A 1 507 ? 31.535  57.404 0.751   1.00 26.40  ? 493  LEU A N     1 
ATOM   3675 C  CA    . LEU A 1 507 ? 30.250  58.058 0.530   1.00 24.97  ? 493  LEU A CA    1 
ATOM   3676 C  C     . LEU A 1 507 ? 29.780  58.850 1.732   1.00 25.51  ? 493  LEU A C     1 
ATOM   3677 O  O     . LEU A 1 507 ? 28.597  59.215 1.802   1.00 27.22  ? 493  LEU A O     1 
ATOM   3678 C  CB    . LEU A 1 507 ? 29.187  57.038 0.125   1.00 24.55  ? 493  LEU A CB    1 
ATOM   3679 C  CG    . LEU A 1 507 ? 29.605  56.167 -1.067  1.00 25.15  ? 493  LEU A CG    1 
ATOM   3680 C  CD1   . LEU A 1 507 ? 28.465  55.252 -1.464  1.00 21.58  ? 493  LEU A CD1   1 
ATOM   3681 C  CD2   . LEU A 1 507 ? 30.096  57.014 -2.252  1.00 22.62  ? 493  LEU A CD2   1 
ATOM   3682 N  N     . SER A 1 508 ? 30.680  59.140 2.667   1.00 26.02  ? 494  SER A N     1 
ATOM   3683 C  CA    . SER A 1 508 ? 30.324  59.927 3.836   1.00 27.81  ? 494  SER A CA    1 
ATOM   3684 C  C     . SER A 1 508 ? 31.577  60.552 4.419   1.00 28.64  ? 494  SER A C     1 
ATOM   3685 O  O     . SER A 1 508 ? 32.637  59.922 4.444   1.00 27.76  ? 494  SER A O     1 
ATOM   3686 C  CB    . SER A 1 508 ? 29.638  59.080 4.910   1.00 27.59  ? 494  SER A CB    1 
ATOM   3687 O  OG    . SER A 1 508 ? 29.357  59.885 6.040   1.00 29.37  ? 494  SER A OG    1 
ATOM   3688 N  N     . LEU A 1 509 ? 31.425  61.770 4.941   1.00 29.78  ? 495  LEU A N     1 
ATOM   3689 C  CA    . LEU A 1 509 ? 32.523  62.413 5.641   1.00 31.54  ? 495  LEU A CA    1 
ATOM   3690 C  C     . LEU A 1 509 ? 32.692  61.886 7.061   1.00 32.57  ? 495  LEU A C     1 
ATOM   3691 O  O     . LEU A 1 509 ? 33.779  62.014 7.629   1.00 35.63  ? 495  LEU A O     1 
ATOM   3692 C  CB    . LEU A 1 509 ? 32.298  63.924 5.674   1.00 30.24  ? 495  LEU A CB    1 
ATOM   3693 C  CG    . LEU A 1 509 ? 32.320  64.691 4.352   1.00 30.28  ? 495  LEU A CG    1 
ATOM   3694 C  CD1   . LEU A 1 509 ? 32.133  66.200 4.598   1.00 31.15  ? 495  LEU A CD1   1 
ATOM   3695 C  CD2   . LEU A 1 509 ? 33.599  64.416 3.565   1.00 26.66  ? 495  LEU A CD2   1 
ATOM   3696 N  N     . ASP A 1 510 ? 31.647  61.302 7.646   1.00 32.93  ? 496  ASP A N     1 
ATOM   3697 C  CA    . ASP A 1 510 ? 31.700  60.791 9.016   1.00 33.66  ? 496  ASP A CA    1 
ATOM   3698 C  C     . ASP A 1 510 ? 30.702  59.654 9.164   1.00 33.39  ? 496  ASP A C     1 
ATOM   3699 O  O     . ASP A 1 510 ? 29.670  59.794 9.826   1.00 35.08  ? 496  ASP A O     1 
ATOM   3700 C  CB    . ASP A 1 510 ? 31.418  61.907 10.016  1.00 38.09  ? 496  ASP A CB    1 
ATOM   3701 C  CG    . ASP A 1 510 ? 31.703  61.493 11.445  1.00 42.35  ? 496  ASP A CG    1 
ATOM   3702 O  OD1   . ASP A 1 510 ? 32.593  60.638 11.663  1.00 43.63  ? 496  ASP A OD1   1 
ATOM   3703 O  OD2   . ASP A 1 510 ? 31.025  62.024 12.351  1.00 47.03  ? 496  ASP A OD2   1 
ATOM   3704 N  N     . PRO A 1 511 ? 30.983  58.500 8.557   1.00 34.92  ? 497  PRO A N     1 
ATOM   3705 C  CA    . PRO A 1 511 ? 29.990  57.414 8.531   1.00 32.51  ? 497  PRO A CA    1 
ATOM   3706 C  C     . PRO A 1 511 ? 29.698  56.869 9.921   1.00 33.15  ? 497  PRO A C     1 
ATOM   3707 O  O     . PRO A 1 511 ? 30.613  56.591 10.699  1.00 30.84  ? 497  PRO A O     1 
ATOM   3708 C  CB    . PRO A 1 511 ? 30.663  56.337 7.666   1.00 29.40  ? 497  PRO A CB    1 
ATOM   3709 C  CG    . PRO A 1 511 ? 31.871  56.996 7.055   1.00 31.66  ? 497  PRO A CG    1 
ATOM   3710 C  CD    . PRO A 1 511 ? 32.281  58.058 8.018   1.00 32.08  ? 497  PRO A CD    1 
ATOM   3711 N  N     . GLN A 1 512 ? 28.412  56.708 10.233  1.00 32.43  ? 498  GLN A N     1 
ATOM   3712 C  CA    . GLN A 1 512 ? 28.017  56.025 11.472  1.00 35.52  ? 498  GLN A CA    1 
ATOM   3713 C  C     . GLN A 1 512 ? 27.887  54.548 11.081  1.00 34.05  ? 498  GLN A C     1 
ATOM   3714 O  O     . GLN A 1 512 ? 26.796  54.001 10.876  1.00 32.81  ? 498  GLN A O     1 
ATOM   3715 C  CB    . GLN A 1 512 ? 26.739  56.630 12.063  1.00 38.17  ? 498  GLN A CB    1 
ATOM   3716 C  CG    . GLN A 1 512 ? 25.882  55.682 12.933  1.00 44.81  ? 498  GLN A CG    1 
ATOM   3717 C  CD    . GLN A 1 512 ? 25.037  56.376 13.998  1.00 57.09  ? 498  GLN A CD    1 
ATOM   3718 O  OE1   . GLN A 1 512 ? 23.980  56.949 13.705  1.00 40.24  ? 498  GLN A OE1   1 
ATOM   3719 N  NE2   . GLN A 1 512 ? 25.492  56.307 15.249  1.00 67.80  ? 498  GLN A NE2   1 
ATOM   3720 N  N     . ALA A 1 513 ? 29.050  53.972 10.757  1.00 32.77  ? 499  ALA A N     1 
ATOM   3721 C  CA    . ALA A 1 513 ? 29.117  52.641 10.168  1.00 31.57  ? 499  ALA A CA    1 
ATOM   3722 C  C     . ALA A 1 513 ? 30.274  51.832 10.735  1.00 32.31  ? 499  ALA A C     1 
ATOM   3723 O  O     . ALA A 1 513 ? 31.263  52.382 11.225  1.00 30.06  ? 499  ALA A O     1 
ATOM   3724 C  CB    . ALA A 1 513 ? 29.249  52.722 8.633   1.00 26.96  ? 499  ALA A CB    1 
ATOM   3725 N  N     . GLN A 1 514 ? 30.105  50.513 10.723  1.00 31.17  ? 500  GLN A N     1 
ATOM   3726 C  CA    . GLN A 1 514 ? 31.188  49.567 10.948  1.00 30.64  ? 500  GLN A CA    1 
ATOM   3727 C  C     . GLN A 1 514 ? 31.169  48.509 9.851   1.00 30.41  ? 500  GLN A C     1 
ATOM   3728 O  O     . GLN A 1 514 ? 30.097  48.028 9.474   1.00 30.55  ? 500  GLN A O     1 
ATOM   3729 C  CB    . GLN A 1 514 ? 31.113  48.913 12.318  1.00 35.63  ? 500  GLN A CB    1 
ATOM   3730 C  CG    . GLN A 1 514 ? 32.454  48.294 12.690  1.00 34.68  ? 500  GLN A CG    1 
ATOM   3731 C  CD    . GLN A 1 514 ? 32.722  48.313 14.173  1.00 40.48  ? 500  GLN A CD    1 
ATOM   3732 O  OE1   . GLN A 1 514 ? 32.176  49.138 14.907  1.00 49.97  ? 500  GLN A OE1   1 
ATOM   3733 N  NE2   . GLN A 1 514 ? 33.589  47.416 14.624  1.00 40.58  ? 500  GLN A NE2   1 
ATOM   3734 N  N     . CYS A 1 515 ? 32.333  48.186 9.298   1.00 30.87  ? 501  CYS A N     1 
ATOM   3735 C  CA    . CYS A 1 515 ? 32.432  47.217 8.218   1.00 30.10  ? 501  CYS A CA    1 
ATOM   3736 C  C     . CYS A 1 515 ? 33.320  46.044 8.618   1.00 29.83  ? 501  CYS A C     1 
ATOM   3737 O  O     . CYS A 1 515 ? 34.315  46.214 9.320   1.00 32.98  ? 501  CYS A O     1 
ATOM   3738 C  CB    . CYS A 1 515 ? 32.971  47.879 6.954   1.00 28.44  ? 501  CYS A CB    1 
ATOM   3739 S  SG    . CYS A 1 515 ? 31.995  49.329 6.525   1.00 29.17  ? 501  CYS A SG    1 
ATOM   3740 N  N     . TRP A 1 516 ? 32.957  44.851 8.141   1.00 29.82  ? 502  TRP A N     1 
ATOM   3741 C  CA    . TRP A 1 516 ? 33.740  43.637 8.340   1.00 27.99  ? 502  TRP A CA    1 
ATOM   3742 C  C     . TRP A 1 516 ? 33.807  42.848 7.043   1.00 28.92  ? 502  TRP A C     1 
ATOM   3743 O  O     . TRP A 1 516 ? 32.878  42.872 6.223   1.00 26.67  ? 502  TRP A O     1 
ATOM   3744 C  CB    . TRP A 1 516 ? 33.149  42.700 9.394   1.00 27.70  ? 502  TRP A CB    1 
ATOM   3745 C  CG    . TRP A 1 516 ? 33.107  43.215 10.788  1.00 31.33  ? 502  TRP A CG    1 
ATOM   3746 C  CD1   . TRP A 1 516 ? 34.005  42.969 11.778  1.00 31.84  ? 502  TRP A CD1   1 
ATOM   3747 C  CD2   . TRP A 1 516 ? 32.078  44.029 11.368  1.00 34.25  ? 502  TRP A CD2   1 
ATOM   3748 N  NE1   . TRP A 1 516 ? 33.613  43.589 12.939  1.00 34.95  ? 502  TRP A NE1   1 
ATOM   3749 C  CE2   . TRP A 1 516 ? 32.433  44.248 12.717  1.00 35.08  ? 502  TRP A CE2   1 
ATOM   3750 C  CE3   . TRP A 1 516 ? 30.894  44.596 10.878  1.00 30.33  ? 502  TRP A CE3   1 
ATOM   3751 C  CZ2   . TRP A 1 516 ? 31.648  45.012 13.584  1.00 34.41  ? 502  TRP A CZ2   1 
ATOM   3752 C  CZ3   . TRP A 1 516 ? 30.115  45.362 11.744  1.00 31.40  ? 502  TRP A CZ3   1 
ATOM   3753 C  CH2   . TRP A 1 516 ? 30.495  45.559 13.079  1.00 30.78  ? 502  TRP A CH2   1 
ATOM   3754 N  N     . ARG A 1 517 ? 34.902  42.117 6.885   1.00 26.78  ? 503  ARG A N     1 
ATOM   3755 C  CA    . ARG A 1 517 ? 35.045  41.103 5.852   1.00 29.40  ? 503  ARG A CA    1 
ATOM   3756 C  C     . ARG A 1 517 ? 35.163  39.749 6.535   1.00 29.59  ? 503  ARG A C     1 
ATOM   3757 O  O     . ARG A 1 517 ? 36.029  39.564 7.392   1.00 30.94  ? 503  ARG A O     1 
ATOM   3758 C  CB    . ARG A 1 517 ? 36.274  41.394 4.991   1.00 33.23  ? 503  ARG A CB    1 
ATOM   3759 C  CG    . ARG A 1 517 ? 36.588  40.345 3.937   1.00 34.84  ? 503  ARG A CG    1 
ATOM   3760 C  CD    . ARG A 1 517 ? 37.062  41.023 2.647   1.00 38.43  ? 503  ARG A CD    1 
ATOM   3761 N  NE    . ARG A 1 517 ? 38.484  40.818 2.415   1.00 44.36  ? 503  ARG A NE    1 
ATOM   3762 C  CZ    . ARG A 1 517 ? 39.414  41.748 2.586   1.00 54.49  ? 503  ARG A CZ    1 
ATOM   3763 N  NH1   . ARG A 1 517 ? 39.102  42.977 2.967   1.00 47.34  ? 503  ARG A NH1   1 
ATOM   3764 N  NH2   . ARG A 1 517 ? 40.691  41.435 2.379   1.00 47.63  ? 503  ARG A NH2   1 
ATOM   3765 N  N     . VAL A 1 518 ? 34.296  38.810 6.171   1.00 27.17  ? 504  VAL A N     1 
ATOM   3766 C  CA    . VAL A 1 518 ? 34.271  37.494 6.796   1.00 30.11  ? 504  VAL A CA    1 
ATOM   3767 C  C     . VAL A 1 518 ? 34.409  36.429 5.719   1.00 31.29  ? 504  VAL A C     1 
ATOM   3768 O  O     . VAL A 1 518 ? 33.875  36.570 4.610   1.00 28.52  ? 504  VAL A O     1 
ATOM   3769 C  CB    . VAL A 1 518 ? 32.990  37.252 7.633   1.00 29.25  ? 504  VAL A CB    1 
ATOM   3770 C  CG1   . VAL A 1 518 ? 32.838  38.319 8.697   1.00 30.73  ? 504  VAL A CG1   1 
ATOM   3771 C  CG2   . VAL A 1 518 ? 31.744  37.193 6.736   1.00 28.25  ? 504  VAL A CG2   1 
ATOM   3772 N  N     . SER A 1 519 ? 35.152  35.371 6.052   1.00 30.92  ? 505  SER A N     1 
ATOM   3773 C  CA    . SER A 1 519 ? 35.318  34.209 5.191   1.00 32.54  ? 505  SER A CA    1 
ATOM   3774 C  C     . SER A 1 519 ? 34.991  32.897 5.890   1.00 33.07  ? 505  SER A C     1 
ATOM   3775 O  O     . SER A 1 519 ? 35.030  31.846 5.242   1.00 34.71  ? 505  SER A O     1 
ATOM   3776 C  CB    . SER A 1 519 ? 36.756  34.135 4.663   1.00 33.05  ? 505  SER A CB    1 
ATOM   3777 O  OG    . SER A 1 519 ? 37.659  34.032 5.748   1.00 40.97  ? 505  SER A OG    1 
ATOM   3778 N  N     . GLU A 1 520 ? 34.697  32.919 7.184   1.00 35.02  ? 506  GLU A N     1 
ATOM   3779 C  CA    . GLU A 1 520 ? 34.445  31.717 7.963   1.00 38.07  ? 506  GLU A CA    1 
ATOM   3780 C  C     . GLU A 1 520 ? 33.061  31.814 8.593   1.00 34.61  ? 506  GLU A C     1 
ATOM   3781 O  O     . GLU A 1 520 ? 32.610  32.898 8.964   1.00 34.37  ? 506  GLU A O     1 
ATOM   3782 C  CB    . GLU A 1 520 ? 35.522  31.527 9.057   1.00 37.71  ? 506  GLU A CB    1 
ATOM   3783 C  CG    . GLU A 1 520 ? 36.979  31.589 8.562   1.00 38.49  ? 506  GLU A CG    1 
ATOM   3784 C  CD    . GLU A 1 520 ? 37.329  30.536 7.521   1.00 39.56  ? 506  GLU A CD    1 
ATOM   3785 O  OE1   . GLU A 1 520 ? 37.054  29.344 7.764   1.00 42.21  ? 506  GLU A OE1   1 
ATOM   3786 O  OE2   . GLU A 1 520 ? 37.883  30.895 6.454   1.00 37.89  ? 506  GLU A OE2   1 
ATOM   3787 N  N     . ALA A 1 521 ? 32.390  30.668 8.729   1.00 37.10  ? 507  ALA A N     1 
ATOM   3788 C  CA    . ALA A 1 521 ? 31.052  30.665 9.320   1.00 36.69  ? 507  ALA A CA    1 
ATOM   3789 C  C     . ALA A 1 521 ? 31.046  31.262 10.725  1.00 36.90  ? 507  ALA A C     1 
ATOM   3790 O  O     . ALA A 1 521 ? 30.123  32.006 11.087  1.00 33.41  ? 507  ALA A O     1 
ATOM   3791 C  CB    . ALA A 1 521 ? 30.491  29.244 9.340   1.00 42.35  ? 507  ALA A CB    1 
ATOM   3792 N  N     . GLU A 1 522 ? 32.060  30.942 11.538  1.00 37.33  ? 508  GLU A N     1 
ATOM   3793 C  CA    . GLU A 1 522 ? 32.087  31.416 12.922  1.00 36.19  ? 508  GLU A CA    1 
ATOM   3794 C  C     . GLU A 1 522 ? 32.315  32.919 12.988  1.00 35.87  ? 508  GLU A C     1 
ATOM   3795 O  O     . GLU A 1 522 ? 31.802  33.591 13.889  1.00 35.20  ? 508  GLU A O     1 
ATOM   3796 C  CB    . GLU A 1 522 ? 33.163  30.685 13.723  1.00 40.37  ? 508  GLU A CB    1 
ATOM   3797 C  CG    . GLU A 1 522 ? 33.377  29.284 13.256  1.00 45.48  ? 508  GLU A CG    1 
ATOM   3798 C  CD    . GLU A 1 522 ? 34.362  29.264 12.106  1.00 47.23  ? 508  GLU A CD    1 
ATOM   3799 O  OE1   . GLU A 1 522 ? 35.439  29.882 12.246  1.00 44.91  ? 508  GLU A OE1   1 
ATOM   3800 O  OE2   . GLU A 1 522 ? 34.038  28.714 11.038  1.00 59.72  ? 508  GLU A OE2   1 
ATOM   3801 N  N     . GLN A 1 523 ? 33.143  33.453 12.086  1.00 36.76  ? 509  GLN A N     1 
ATOM   3802 C  CA    . GLN A 1 523 ? 33.314  34.899 12.027  1.00 36.01  ? 509  GLN A CA    1 
ATOM   3803 C  C     . GLN A 1 523 ? 31.993  35.580 11.722  1.00 34.72  ? 509  GLN A C     1 
ATOM   3804 O  O     . GLN A 1 523 ? 31.637  36.577 12.362  1.00 35.57  ? 509  GLN A O     1 
ATOM   3805 C  CB    . GLN A 1 523 ? 34.331  35.281 10.956  1.00 35.67  ? 509  GLN A CB    1 
ATOM   3806 C  CG    . GLN A 1 523 ? 35.659  34.607 11.062  1.00 37.20  ? 509  GLN A CG    1 
ATOM   3807 C  CD    . GLN A 1 523 ? 36.503  34.884 9.839   1.00 37.03  ? 509  GLN A CD    1 
ATOM   3808 O  OE1   . GLN A 1 523 ? 35.987  35.022 8.724   1.00 35.00  ? 509  GLN A OE1   1 
ATOM   3809 N  NE2   . GLN A 1 523 ? 37.806  34.977 10.039  1.00 38.09  ? 509  GLN A NE2   1 
ATOM   3810 N  N     . LEU A 1 524 ? 31.245  35.042 10.755  1.00 33.33  ? 510  LEU A N     1 
ATOM   3811 C  CA    . LEU A 1 524 ? 29.949  35.610 10.416  1.00 32.37  ? 510  LEU A CA    1 
ATOM   3812 C  C     . LEU A 1 524 ? 29.017  35.543 11.613  1.00 30.97  ? 510  LEU A C     1 
ATOM   3813 O  O     . LEU A 1 524 ? 28.369  36.534 11.962  1.00 30.46  ? 510  LEU A O     1 
ATOM   3814 C  CB    . LEU A 1 524 ? 29.346  34.871 9.216   1.00 32.33  ? 510  LEU A CB    1 
ATOM   3815 C  CG    . LEU A 1 524 ? 27.877  35.163 8.876   1.00 29.59  ? 510  LEU A CG    1 
ATOM   3816 C  CD1   . LEU A 1 524 ? 27.649  36.633 8.543   1.00 28.99  ? 510  LEU A CD1   1 
ATOM   3817 C  CD2   . LEU A 1 524 ? 27.364  34.260 7.751   1.00 31.25  ? 510  LEU A CD2   1 
ATOM   3818 N  N     . ALA A 1 525 ? 28.983  34.394 12.293  1.00 32.72  ? 511  ALA A N     1 
ATOM   3819 C  CA    . ALA A 1 525 ? 28.154  34.281 13.488  1.00 33.16  ? 511  ALA A CA    1 
ATOM   3820 C  C     . ALA A 1 525 ? 28.543  35.330 14.522  1.00 34.41  ? 511  ALA A C     1 
ATOM   3821 O  O     . ALA A 1 525 ? 27.675  35.997 15.102  1.00 34.29  ? 511  ALA A O     1 
ATOM   3822 C  CB    . ALA A 1 525 ? 28.263  32.874 14.076  1.00 33.05  ? 511  ALA A CB    1 
ATOM   3823 N  N     . ASP A 1 526 ? 29.848  35.517 14.738  1.00 37.04  ? 512  ASP A N     1 
ATOM   3824 C  CA    . ASP A 1 526 ? 30.304  36.484 15.732  1.00 38.16  ? 512  ASP A CA    1 
ATOM   3825 C  C     . ASP A 1 526 ? 29.918  37.903 15.340  1.00 34.14  ? 512  ASP A C     1 
ATOM   3826 O  O     . ASP A 1 526 ? 29.408  38.663 16.168  1.00 36.54  ? 512  ASP A O     1 
ATOM   3827 C  CB    . ASP A 1 526 ? 31.814  36.365 15.932  1.00 42.37  ? 512  ASP A CB    1 
ATOM   3828 C  CG    . ASP A 1 526 ? 32.192  35.156 16.767  1.00 60.26  ? 512  ASP A CG    1 
ATOM   3829 O  OD1   . ASP A 1 526 ? 31.281  34.519 17.349  1.00 63.94  ? 512  ASP A OD1   1 
ATOM   3830 O  OD2   . ASP A 1 526 ? 33.402  34.847 16.848  1.00 75.07  ? 512  ASP A OD2   1 
ATOM   3831 N  N     . VAL A 1 527 ? 30.144  38.275 14.075  1.00 33.28  ? 513  VAL A N     1 
ATOM   3832 C  CA    . VAL A 1 527 ? 29.784  39.618 13.618  1.00 32.78  ? 513  VAL A CA    1 
ATOM   3833 C  C     . VAL A 1 527 ? 28.286  39.850 13.768  1.00 30.11  ? 513  VAL A C     1 
ATOM   3834 O  O     . VAL A 1 527 ? 27.850  40.891 14.280  1.00 31.58  ? 513  VAL A O     1 
ATOM   3835 C  CB    . VAL A 1 527 ? 30.244  39.839 12.161  1.00 31.84  ? 513  VAL A CB    1 
ATOM   3836 C  CG1   . VAL A 1 527 ? 29.693  41.149 11.614  1.00 28.66  ? 513  VAL A CG1   1 
ATOM   3837 C  CG2   . VAL A 1 527 ? 31.765  39.845 12.068  1.00 33.50  ? 513  VAL A CG2   1 
ATOM   3838 N  N     . LEU A 1 528 ? 27.474  38.873 13.354  1.00 28.74  ? 514  LEU A N     1 
ATOM   3839 C  CA    . LEU A 1 528 ? 26.024  39.053 13.420  1.00 30.45  ? 514  LEU A CA    1 
ATOM   3840 C  C     . LEU A 1 528 ? 25.562  39.280 14.854  1.00 32.67  ? 514  LEU A C     1 
ATOM   3841 O  O     . LEU A 1 528 ? 24.716  40.145 15.114  1.00 32.11  ? 514  LEU A O     1 
ATOM   3842 C  CB    . LEU A 1 528 ? 25.309  37.846 12.812  1.00 28.30  ? 514  LEU A CB    1 
ATOM   3843 C  CG    . LEU A 1 528 ? 25.335  37.799 11.278  1.00 30.30  ? 514  LEU A CG    1 
ATOM   3844 C  CD1   . LEU A 1 528 ? 24.741  36.495 10.767  1.00 29.25  ? 514  LEU A CD1   1 
ATOM   3845 C  CD2   . LEU A 1 528 ? 24.630  39.015 10.662  1.00 27.56  ? 514  LEU A CD2   1 
ATOM   3846 N  N     . GLU A 1 529 ? 26.126  38.525 15.798  1.00 34.22  ? 515  GLU A N     1 
ATOM   3847 C  CA    . GLU A 1 529 ? 25.849  38.747 17.214  1.00 33.38  ? 515  GLU A CA    1 
ATOM   3848 C  C     . GLU A 1 529 ? 26.191  40.172 17.641  1.00 32.68  ? 515  GLU A C     1 
ATOM   3849 O  O     . GLU A 1 529 ? 25.432  40.797 18.389  1.00 33.70  ? 515  GLU A O     1 
ATOM   3850 C  CB    . GLU A 1 529 ? 26.629  37.735 18.046  1.00 39.22  ? 515  GLU A CB    1 
ATOM   3851 C  CG    . GLU A 1 529 ? 25.983  37.386 19.369  1.00 46.84  ? 515  GLU A CG    1 
ATOM   3852 C  CD    . GLU A 1 529 ? 26.961  36.719 20.318  1.00 56.48  ? 515  GLU A CD    1 
ATOM   3853 O  OE1   . GLU A 1 529 ? 27.836  35.967 19.835  1.00 62.02  ? 515  GLU A OE1   1 
ATOM   3854 O  OE2   . GLU A 1 529 ? 26.863  36.961 21.542  1.00 63.80  ? 515  GLU A OE2   1 
ATOM   3855 N  N     . LYS A 1 530 ? 27.326  40.706 17.176  1.00 34.38  ? 516  LYS A N     1 
ATOM   3856 C  CA    . LYS A 1 530 ? 27.724  42.062 17.556  1.00 34.70  ? 516  LYS A CA    1 
ATOM   3857 C  C     . LYS A 1 530 ? 26.735  43.112 17.062  1.00 33.23  ? 516  LYS A C     1 
ATOM   3858 O  O     . LYS A 1 530 ? 26.484  44.105 17.750  1.00 33.04  ? 516  LYS A O     1 
ATOM   3859 C  CB    . LYS A 1 530 ? 29.098  42.409 16.987  1.00 35.60  ? 516  LYS A CB    1 
ATOM   3860 C  CG    . LYS A 1 530 ? 30.165  41.367 17.102  1.00 41.00  ? 516  LYS A CG    1 
ATOM   3861 C  CD    . LYS A 1 530 ? 31.442  42.001 17.595  1.00 47.26  ? 516  LYS A CD    1 
ATOM   3862 C  CE    . LYS A 1 530 ? 32.652  41.135 17.314  1.00 52.85  ? 516  LYS A CE    1 
ATOM   3863 N  NZ    . LYS A 1 530 ? 33.371  41.568 16.076  1.00 45.88  ? 516  LYS A NZ    1 
ATOM   3864 N  N     . VAL A 1 531 ? 26.208  42.947 15.847  1.00 31.67  ? 517  VAL A N     1 
ATOM   3865 C  CA    . VAL A 1 531 ? 25.383  43.986 15.235  1.00 30.08  ? 517  VAL A CA    1 
ATOM   3866 C  C     . VAL A 1 531 ? 23.895  43.741 15.455  1.00 29.39  ? 517  VAL A C     1 
ATOM   3867 O  O     . VAL A 1 531 ? 23.064  44.391 14.815  1.00 30.32  ? 517  VAL A O     1 
ATOM   3868 C  CB    . VAL A 1 531 ? 25.714  44.161 13.742  1.00 30.92  ? 517  VAL A CB    1 
ATOM   3869 C  CG1   . VAL A 1 531 ? 27.218  44.359 13.560  1.00 28.52  ? 517  VAL A CG1   1 
ATOM   3870 C  CG2   . VAL A 1 531 ? 25.204  42.982 12.906  1.00 27.12  ? 517  VAL A CG2   1 
ATOM   3871 N  N     . ALA A 1 532 ? 23.545  42.827 16.367  1.00 30.58  ? 518  ALA A N     1 
ATOM   3872 C  CA    . ALA A 1 532 ? 22.158  42.412 16.559  1.00 29.70  ? 518  ALA A CA    1 
ATOM   3873 C  C     . ALA A 1 532 ? 21.231  43.587 16.839  1.00 30.22  ? 518  ALA A C     1 
ATOM   3874 O  O     . ALA A 1 532 ? 20.081  43.592 16.385  1.00 27.74  ? 518  ALA A O     1 
ATOM   3875 C  CB    . ALA A 1 532 ? 22.069  41.397 17.700  1.00 29.71  ? 518  ALA A CB    1 
ATOM   3876 N  N     . HIS A 1 533 ? 21.694  44.586 17.587  1.00 31.45  ? 519  HIS A N     1 
ATOM   3877 C  CA    . HIS A 1 533 ? 20.834  45.713 17.934  1.00 30.01  ? 519  HIS A CA    1 
ATOM   3878 C  C     . HIS A 1 533 ? 21.077  46.933 17.063  1.00 29.75  ? 519  HIS A C     1 
ATOM   3879 O  O     . HIS A 1 533 ? 20.530  48.004 17.347  1.00 29.56  ? 519  HIS A O     1 
ATOM   3880 C  CB    . HIS A 1 533 ? 20.966  46.045 19.419  1.00 30.96  ? 519  HIS A CB    1 
ATOM   3881 C  CG    . HIS A 1 533 ? 20.884  44.835 20.292  1.00 32.18  ? 519  HIS A CG    1 
ATOM   3882 N  ND1   . HIS A 1 533 ? 19.680  44.289 20.682  1.00 35.34  ? 519  HIS A ND1   1 
ATOM   3883 C  CD2   . HIS A 1 533 ? 21.847  44.056 20.838  1.00 33.72  ? 519  HIS A CD2   1 
ATOM   3884 C  CE1   . HIS A 1 533 ? 19.905  43.224 21.433  1.00 34.79  ? 519  HIS A CE1   1 
ATOM   3885 N  NE2   . HIS A 1 533 ? 21.211  43.060 21.541  1.00 36.69  ? 519  HIS A NE2   1 
ATOM   3886 N  N     . HIS A 1 534 ? 21.843  46.769 15.989  1.00 29.41  ? 520  HIS A N     1 
ATOM   3887 C  CA    . HIS A 1 534 ? 21.959  47.717 14.877  1.00 28.65  ? 520  HIS A CA    1 
ATOM   3888 C  C     . HIS A 1 534 ? 22.097  49.163 15.353  1.00 29.76  ? 520  HIS A C     1 
ATOM   3889 O  O     . HIS A 1 534 ? 21.336  50.053 14.981  1.00 28.19  ? 520  HIS A O     1 
ATOM   3890 C  CB    . HIS A 1 534 ? 20.769  47.558 13.920  1.00 29.67  ? 520  HIS A CB    1 
ATOM   3891 C  CG    . HIS A 1 534 ? 19.417  47.663 14.567  1.00 29.06  ? 520  HIS A CG    1 
ATOM   3892 N  ND1   . HIS A 1 534 ? 18.809  48.873 14.837  1.00 29.95  ? 520  HIS A ND1   1 
ATOM   3893 C  CD2   . HIS A 1 534 ? 18.572  46.710 15.027  1.00 29.06  ? 520  HIS A CD2   1 
ATOM   3894 C  CE1   . HIS A 1 534 ? 17.629  48.659 15.394  1.00 29.87  ? 520  HIS A CE1   1 
ATOM   3895 N  NE2   . HIS A 1 534 ? 17.464  47.355 15.528  1.00 30.54  ? 520  HIS A NE2   1 
ATOM   3896 N  N     . GLU A 1 535 ? 23.121  49.390 16.176  1.00 31.20  ? 521  GLU A N     1 
ATOM   3897 C  CA    . GLU A 1 535 ? 23.394  50.724 16.692  1.00 33.04  ? 521  GLU A CA    1 
ATOM   3898 C  C     . GLU A 1 535 ? 24.075  51.609 15.664  1.00 33.14  ? 521  GLU A C     1 
ATOM   3899 O  O     . GLU A 1 535 ? 24.084  52.835 15.818  1.00 31.96  ? 521  GLU A O     1 
ATOM   3900 C  CB    . GLU A 1 535 ? 24.283  50.613 17.934  1.00 38.12  ? 521  GLU A CB    1 
ATOM   3901 C  CG    . GLU A 1 535 ? 23.525  50.387 19.223  1.00 43.75  ? 521  GLU A CG    1 
ATOM   3902 C  CD    . GLU A 1 535 ? 24.329  50.814 20.438  1.00 76.67  ? 521  GLU A CD    1 
ATOM   3903 O  OE1   . GLU A 1 535 ? 25.323  50.123 20.755  1.00 70.08  ? 521  GLU A OE1   1 
ATOM   3904 O  OE2   . GLU A 1 535 ? 23.978  51.842 21.063  1.00 74.99  ? 521  GLU A OE2   1 
ATOM   3905 N  N     . ARG A 1 536 ? 24.621  51.003 14.616  1.00 32.40  ? 522  ARG A N     1 
ATOM   3906 C  CA    . ARG A 1 536 ? 25.283  51.680 13.520  1.00 31.52  ? 522  ARG A CA    1 
ATOM   3907 C  C     . ARG A 1 536 ? 24.875  50.971 12.237  1.00 28.49  ? 522  ARG A C     1 
ATOM   3908 O  O     . ARG A 1 536 ? 24.344  49.857 12.267  1.00 26.55  ? 522  ARG A O     1 
ATOM   3909 C  CB    . ARG A 1 536 ? 26.813  51.648 13.714  1.00 34.41  ? 522  ARG A CB    1 
ATOM   3910 C  CG    . ARG A 1 536 ? 27.341  52.731 14.637  1.00 38.91  ? 522  ARG A CG    1 
ATOM   3911 C  CD    . ARG A 1 536 ? 28.804  52.519 15.033  1.00 40.72  ? 522  ARG A CD    1 
ATOM   3912 N  NE    . ARG A 1 536 ? 28.883  51.764 16.280  1.00 47.77  ? 522  ARG A NE    1 
ATOM   3913 C  CZ    . ARG A 1 536 ? 28.883  50.439 16.365  1.00 58.20  ? 522  ARG A CZ    1 
ATOM   3914 N  NH1   . ARG A 1 536 ? 28.876  49.670 15.283  1.00 44.41  ? 522  ARG A NH1   1 
ATOM   3915 N  NH2   . ARG A 1 536 ? 28.871  49.867 17.566  1.00 51.08  ? 522  ARG A NH2   1 
ATOM   3916 N  N     . LEU A 1 537 ? 25.091  51.626 11.104  1.00 27.75  ? 523  LEU A N     1 
ATOM   3917 C  CA    . LEU A 1 537 ? 25.024  50.886 9.852   1.00 26.32  ? 523  LEU A CA    1 
ATOM   3918 C  C     . LEU A 1 537 ? 26.122  49.837 9.882   1.00 26.09  ? 523  LEU A C     1 
ATOM   3919 O  O     . LEU A 1 537 ? 27.222  50.094 10.370  1.00 28.03  ? 523  LEU A O     1 
ATOM   3920 C  CB    . LEU A 1 537 ? 25.205  51.818 8.647   1.00 24.66  ? 523  LEU A CB    1 
ATOM   3921 C  CG    . LEU A 1 537 ? 25.088  51.214 7.231   1.00 23.76  ? 523  LEU A CG    1 
ATOM   3922 C  CD1   . LEU A 1 537 ? 24.272  52.105 6.259   1.00 21.13  ? 523  LEU A CD1   1 
ATOM   3923 C  CD2   . LEU A 1 537 ? 26.459  50.858 6.635   1.00 22.39  ? 523  LEU A CD2   1 
ATOM   3924 N  N     . SER A 1 538 ? 25.819  48.626 9.445   1.00 25.39  ? 524  SER A N     1 
ATOM   3925 C  CA    . SER A 1 538 ? 26.866  47.624 9.368   1.00 26.63  ? 524  SER A CA    1 
ATOM   3926 C  C     . SER A 1 538 ? 26.914  47.087 7.947   1.00 26.08  ? 524  SER A C     1 
ATOM   3927 O  O     . SER A 1 538 ? 25.873  46.805 7.335   1.00 25.97  ? 524  SER A O     1 
ATOM   3928 C  CB    . SER A 1 538 ? 26.672  46.501 10.411  1.00 25.22  ? 524  SER A CB    1 
ATOM   3929 O  OG    . SER A 1 538 ? 25.571  45.692 10.114  1.00 31.05  ? 524  SER A OG    1 
ATOM   3930 N  N     . LEU A 1 539 ? 28.128  46.964 7.418   1.00 25.05  ? 525  LEU A N     1 
ATOM   3931 C  CA    . LEU A 1 539 ? 28.334  46.384 6.101   1.00 24.94  ? 525  LEU A CA    1 
ATOM   3932 C  C     . LEU A 1 539 ? 29.269  45.197 6.262   1.00 25.69  ? 525  LEU A C     1 
ATOM   3933 O  O     . LEU A 1 539 ? 30.404  45.351 6.720   1.00 27.60  ? 525  LEU A O     1 
ATOM   3934 C  CB    . LEU A 1 539 ? 28.886  47.418 5.118   1.00 25.47  ? 525  LEU A CB    1 
ATOM   3935 C  CG    . LEU A 1 539 ? 28.771  47.004 3.644   1.00 26.36  ? 525  LEU A CG    1 
ATOM   3936 C  CD1   . LEU A 1 539 ? 28.694  48.233 2.738   1.00 26.18  ? 525  LEU A CD1   1 
ATOM   3937 C  CD2   . LEU A 1 539 ? 29.930  46.105 3.220   1.00 25.25  ? 525  LEU A CD2   1 
ATOM   3938 N  N     . ILE A 1 540 ? 28.776  44.013 5.919   1.00 24.50  ? 526  ILE A N     1 
ATOM   3939 C  CA    . ILE A 1 540 ? 29.519  42.770 6.066   1.00 23.94  ? 526  ILE A CA    1 
ATOM   3940 C  C     . ILE A 1 540 ? 29.795  42.215 4.678   1.00 23.95  ? 526  ILE A C     1 
ATOM   3941 O  O     . ILE A 1 540 ? 28.887  41.689 4.023   1.00 21.11  ? 526  ILE A O     1 
ATOM   3942 C  CB    . ILE A 1 540 ? 28.736  41.758 6.904   1.00 23.21  ? 526  ILE A CB    1 
ATOM   3943 C  CG1   . ILE A 1 540 ? 28.203  42.425 8.173   1.00 25.94  ? 526  ILE A CG1   1 
ATOM   3944 C  CG2   . ILE A 1 540 ? 29.604  40.545 7.227   1.00 24.64  ? 526  ILE A CG2   1 
ATOM   3945 C  CD1   . ILE A 1 540 ? 27.198  41.571 8.914   1.00 23.74  ? 526  ILE A CD1   1 
ATOM   3946 N  N     . GLU A 1 541 ? 31.057  42.254 4.262   1.00 23.98  ? 527  GLU A N     1 
ATOM   3947 C  CA    . GLU A 1 541 ? 31.456  41.652 3.000   1.00 24.15  ? 527  GLU A CA    1 
ATOM   3948 C  C     . GLU A 1 541 ? 31.640  40.160 3.240   1.00 26.17  ? 527  GLU A C     1 
ATOM   3949 O  O     . GLU A 1 541 ? 32.575  39.743 3.931   1.00 25.99  ? 527  GLU A O     1 
ATOM   3950 C  CB    . GLU A 1 541 ? 32.732  42.301 2.471   1.00 26.30  ? 527  GLU A CB    1 
ATOM   3951 C  CG    . GLU A 1 541 ? 33.305  41.600 1.244   1.00 27.61  ? 527  GLU A CG    1 
ATOM   3952 C  CD    . GLU A 1 541 ? 34.525  42.298 0.678   1.00 30.53  ? 527  GLU A CD    1 
ATOM   3953 O  OE1   . GLU A 1 541 ? 35.121  43.133 1.399   1.00 29.74  ? 527  GLU A OE1   1 
ATOM   3954 O  OE2   . GLU A 1 541 ? 34.913  41.979 -0.470  1.00 27.39  ? 527  GLU A OE2   1 
ATOM   3955 N  N     . VAL A 1 542 ? 30.732  39.360 2.695   1.00 23.44  ? 528  VAL A N     1 
ATOM   3956 C  CA    . VAL A 1 542 ? 30.700  37.923 2.929   1.00 26.50  ? 528  VAL A CA    1 
ATOM   3957 C  C     . VAL A 1 542 ? 31.397  37.246 1.755   1.00 27.32  ? 528  VAL A C     1 
ATOM   3958 O  O     . VAL A 1 542 ? 30.918  37.303 0.617   1.00 26.55  ? 528  VAL A O     1 
ATOM   3959 C  CB    . VAL A 1 542 ? 29.262  37.412 3.097   1.00 27.23  ? 528  VAL A CB    1 
ATOM   3960 C  CG1   . VAL A 1 542 ? 29.263  35.914 3.405   1.00 27.51  ? 528  VAL A CG1   1 
ATOM   3961 C  CG2   . VAL A 1 542 ? 28.520  38.218 4.182   1.00 23.88  ? 528  VAL A CG2   1 
ATOM   3962 N  N     . MET A 1 543 ? 32.534  36.605 2.023   1.00 29.21  ? 529  MET A N     1 
ATOM   3963 C  CA    . MET A 1 543 ? 33.328  35.978 0.973   1.00 31.62  ? 529  MET A CA    1 
ATOM   3964 C  C     . MET A 1 543 ? 32.842  34.548 0.756   1.00 34.96  ? 529  MET A C     1 
ATOM   3965 O  O     . MET A 1 543 ? 32.950  33.705 1.658   1.00 34.16  ? 529  MET A O     1 
ATOM   3966 C  CB    . MET A 1 543 ? 34.824  35.998 1.304   1.00 31.42  ? 529  MET A CB    1 
ATOM   3967 C  CG    . MET A 1 543 ? 35.411  37.368 1.695   1.00 32.07  ? 529  MET A CG    1 
ATOM   3968 S  SD    . MET A 1 543 ? 35.243  38.664 0.442   1.00 36.34  ? 529  MET A SD    1 
ATOM   3969 C  CE    . MET A 1 543 ? 36.053  37.926 -0.961  1.00 34.84  ? 529  MET A CE    1 
ATOM   3970 N  N     . LEU A 1 544 ? 32.320  34.278 -0.439  1.00 35.89  ? 530  LEU A N     1 
ATOM   3971 C  CA    . LEU A 1 544 ? 31.722  33.012 -0.836  1.00 38.49  ? 530  LEU A CA    1 
ATOM   3972 C  C     . LEU A 1 544 ? 32.407  32.463 -2.084  1.00 40.96  ? 530  LEU A C     1 
ATOM   3973 O  O     . LEU A 1 544 ? 33.015  33.221 -2.849  1.00 40.24  ? 530  LEU A O     1 
ATOM   3974 C  CB    . LEU A 1 544 ? 30.221  33.184 -1.116  1.00 36.20  ? 530  LEU A CB    1 
ATOM   3975 C  CG    . LEU A 1 544 ? 29.343  33.532 0.082   1.00 35.46  ? 530  LEU A CG    1 
ATOM   3976 C  CD1   . LEU A 1 544 ? 28.006  34.080 -0.377  1.00 33.33  ? 530  LEU A CD1   1 
ATOM   3977 C  CD2   . LEU A 1 544 ? 29.144  32.324 0.981   1.00 35.65  ? 530  LEU A CD2   1 
ATOM   3978 N  N     . PRO A 1 545 ? 32.343  31.146 -2.312  1.00 44.27  ? 531  PRO A N     1 
ATOM   3979 C  CA    . PRO A 1 545 ? 33.006  30.563 -3.489  1.00 45.96  ? 531  PRO A CA    1 
ATOM   3980 C  C     . PRO A 1 545 ? 32.367  31.022 -4.795  1.00 52.00  ? 531  PRO A C     1 
ATOM   3981 O  O     . PRO A 1 545 ? 31.163  31.286 -4.867  1.00 51.39  ? 531  PRO A O     1 
ATOM   3982 C  CB    . PRO A 1 545 ? 32.822  29.055 -3.287  1.00 47.47  ? 531  PRO A CB    1 
ATOM   3983 C  CG    . PRO A 1 545 ? 32.557  28.894 -1.804  1.00 44.60  ? 531  PRO A CG    1 
ATOM   3984 C  CD    . PRO A 1 545 ? 31.765  30.105 -1.439  1.00 43.41  ? 531  PRO A CD    1 
ATOM   3985 N  N     . LYS A 1 546 ? 33.198  31.095 -5.844  1.00 53.81  ? 532  LYS A N     1 
ATOM   3986 C  CA    . LYS A 1 546 ? 32.754  31.664 -7.118  1.00 54.86  ? 532  LYS A CA    1 
ATOM   3987 C  C     . LYS A 1 546 ? 31.648  30.840 -7.768  1.00 57.87  ? 532  LYS A C     1 
ATOM   3988 O  O     . LYS A 1 546 ? 30.692  31.399 -8.319  1.00 57.35  ? 532  LYS A O     1 
ATOM   3989 C  CB    . LYS A 1 546 ? 33.934  31.805 -8.084  1.00 58.12  ? 532  LYS A CB    1 
ATOM   3990 C  CG    . LYS A 1 546 ? 33.703  32.867 -9.162  1.00 60.67  ? 532  LYS A CG    1 
ATOM   3991 C  CD    . LYS A 1 546 ? 34.987  33.533 -9.640  1.00 61.79  ? 532  LYS A CD    1 
ATOM   3992 C  CE    . LYS A 1 546 ? 35.553  34.441 -8.563  1.00 63.28  ? 532  LYS A CE    1 
ATOM   3993 N  NZ    . LYS A 1 546 ? 36.893  35.014 -8.887  1.00 67.80  ? 532  LYS A NZ    1 
ATOM   3994 N  N     . ALA A 1 547 ? 31.768  29.515 -7.747  1.00 60.38  ? 533  ALA A N     1 
ATOM   3995 C  CA    . ALA A 1 547 ? 30.814  28.650 -8.427  1.00 63.03  ? 533  ALA A CA    1 
ATOM   3996 C  C     . ALA A 1 547 ? 29.765  28.070 -7.486  1.00 66.25  ? 533  ALA A C     1 
ATOM   3997 O  O     . ALA A 1 547 ? 29.127  27.068 -7.826  1.00 69.69  ? 533  ALA A O     1 
ATOM   3998 C  CB    . ALA A 1 547 ? 31.547  27.524 -9.161  1.00 60.23  ? 533  ALA A CB    1 
ATOM   3999 N  N     . ASP A 1 548 ? 29.575  28.663 -6.311  1.00 66.41  ? 534  ASP A N     1 
ATOM   4000 C  CA    . ASP A 1 548 ? 28.664  28.102 -5.322  1.00 69.04  ? 534  ASP A CA    1 
ATOM   4001 C  C     . ASP A 1 548 ? 27.267  28.684 -5.516  1.00 76.86  ? 534  ASP A C     1 
ATOM   4002 O  O     . ASP A 1 548 ? 27.086  29.909 -5.491  1.00 75.97  ? 534  ASP A O     1 
ATOM   4003 C  CB    . ASP A 1 548 ? 29.169  28.358 -3.903  1.00 61.52  ? 534  ASP A CB    1 
ATOM   4004 C  CG    . ASP A 1 548 ? 28.614  27.360 -2.912  1.00 60.44  ? 534  ASP A CG    1 
ATOM   4005 O  OD1   . ASP A 1 548 ? 27.868  26.455 -3.347  1.00 68.30  ? 534  ASP A OD1   1 
ATOM   4006 O  OD2   . ASP A 1 548 ? 28.933  27.460 -1.710  1.00 53.48  ? 534  ASP A OD2   1 
ATOM   4007 N  N     . ILE A 1 549 ? 26.284  27.800 -5.685  1.00 75.53  ? 535  ILE A N     1 
ATOM   4008 C  CA    . ILE A 1 549 ? 24.896  28.172 -5.963  1.00 78.10  ? 535  ILE A CA    1 
ATOM   4009 C  C     . ILE A 1 549 ? 23.994  27.486 -4.940  1.00 81.32  ? 535  ILE A C     1 
ATOM   4010 O  O     . ILE A 1 549 ? 24.295  26.364 -4.502  1.00 77.98  ? 535  ILE A O     1 
ATOM   4011 C  CB    . ILE A 1 549 ? 24.486  27.808 -7.405  1.00 82.25  ? 535  ILE A CB    1 
ATOM   4012 C  CG1   . ILE A 1 549 ? 24.528  26.290 -7.633  1.00 77.97  ? 535  ILE A CG1   1 
ATOM   4013 C  CG2   . ILE A 1 549 ? 25.367  28.534 -8.420  1.00 78.25  ? 535  ILE A CG2   1 
ATOM   4014 C  CD1   . ILE A 1 549 ? 23.954  25.852 -8.963  1.00 75.04  ? 535  ILE A CD1   1 
ATOM   4015 N  N     . PRO A 1 550 ? 22.909  28.130 -4.507  1.00 82.65  ? 536  PRO A N     1 
ATOM   4016 C  CA    . PRO A 1 550 ? 22.017  27.518 -3.499  1.00 77.69  ? 536  PRO A CA    1 
ATOM   4017 C  C     . PRO A 1 550 ? 21.243  26.353 -4.091  1.00 81.53  ? 536  PRO A C     1 
ATOM   4018 O  O     . PRO A 1 550 ? 21.211  26.184 -5.320  1.00 83.59  ? 536  PRO A O     1 
ATOM   4019 C  CB    . PRO A 1 550 ? 21.062  28.662 -3.117  1.00 70.96  ? 536  PRO A CB    1 
ATOM   4020 C  CG    . PRO A 1 550 ? 21.656  29.910 -3.661  1.00 67.35  ? 536  PRO A CG    1 
ATOM   4021 C  CD    . PRO A 1 550 ? 22.582  29.540 -4.779  1.00 72.81  ? 536  PRO A CD    1 
ATOM   4022 N  N     . PRO A 1 551 ? 20.612  25.523 -3.247  1.00 81.12  ? 537  PRO A N     1 
ATOM   4023 C  CA    . PRO A 1 551 ? 19.851  24.374 -3.777  1.00 82.94  ? 537  PRO A CA    1 
ATOM   4024 C  C     . PRO A 1 551 ? 18.809  24.726 -4.831  1.00 84.45  ? 537  PRO A C     1 
ATOM   4025 O  O     . PRO A 1 551 ? 18.798  24.126 -5.915  1.00 85.69  ? 537  PRO A O     1 
ATOM   4026 C  CB    . PRO A 1 551 ? 19.194  23.802 -2.515  1.00 75.71  ? 537  PRO A CB    1 
ATOM   4027 C  CG    . PRO A 1 551 ? 20.179  24.068 -1.438  1.00 71.59  ? 537  PRO A CG    1 
ATOM   4028 C  CD    . PRO A 1 551 ? 20.869  25.381 -1.800  1.00 77.35  ? 537  PRO A CD    1 
ATOM   4029 N  N     . LEU A 1 552 ? 17.934  25.694 -4.541  1.00 83.09  ? 538  LEU A N     1 
ATOM   4030 C  CA    . LEU A 1 552 ? 16.825  25.987 -5.445  1.00 88.08  ? 538  LEU A CA    1 
ATOM   4031 C  C     . LEU A 1 552 ? 17.316  26.475 -6.802  1.00 87.87  ? 538  LEU A C     1 
ATOM   4032 O  O     . LEU A 1 552 ? 16.729  26.131 -7.835  1.00 86.41  ? 538  LEU A O     1 
ATOM   4033 C  CB    . LEU A 1 552 ? 15.878  27.002 -4.804  1.00 89.06  ? 538  LEU A CB    1 
ATOM   4034 C  CG    . LEU A 1 552 ? 14.888  27.737 -5.711  1.00 74.00  ? 538  LEU A CG    1 
ATOM   4035 C  CD1   . LEU A 1 552 ? 13.620  26.951 -5.938  1.00 59.75  ? 538  LEU A CD1   1 
ATOM   4036 C  CD2   . LEU A 1 552 ? 14.537  29.018 -5.048  1.00 66.41  ? 538  LEU A CD2   1 
ATOM   4037 N  N     . LEU A 1 553 ? 18.403  27.254 -6.827  1.00 87.25  ? 539  LEU A N     1 
ATOM   4038 C  CA    . LEU A 1 553 ? 18.928  27.729 -8.104  1.00 90.65  ? 539  LEU A CA    1 
ATOM   4039 C  C     . LEU A 1 553 ? 19.328  26.566 -9.002  1.00 93.14  ? 539  LEU A C     1 
ATOM   4040 O  O     . LEU A 1 553 ? 19.045  26.585 -10.204 1.00 94.86  ? 539  LEU A O     1 
ATOM   4041 C  CB    . LEU A 1 553 ? 20.110  28.675 -7.892  1.00 86.87  ? 539  LEU A CB    1 
ATOM   4042 C  CG    . LEU A 1 553 ? 20.367  29.598 -9.090  1.00 91.12  ? 539  LEU A CG    1 
ATOM   4043 C  CD1   . LEU A 1 553 ? 19.072  30.240 -9.573  1.00 89.79  ? 539  LEU A CD1   1 
ATOM   4044 C  CD2   . LEU A 1 553 ? 21.418  30.660 -8.778  1.00 86.02  ? 539  LEU A CD2   1 
ATOM   4045 N  N     . GLY A 1 554 ? 19.923  25.516 -8.425  1.00 91.29  ? 540  GLY A N     1 
ATOM   4046 C  CA    . GLY A 1 554 ? 20.298  24.356 -9.223  1.00 91.46  ? 540  GLY A CA    1 
ATOM   4047 C  C     . GLY A 1 554 ? 19.142  23.796 -10.028 1.00 94.50  ? 540  GLY A C     1 
ATOM   4048 O  O     . GLY A 1 554 ? 19.328  23.312 -11.148 1.00 95.51  ? 540  GLY A O     1 
ATOM   4049 N  N     . ALA A 1 555 ? 17.932  23.841 -9.466  1.00 93.60  ? 541  ALA A N     1 
ATOM   4050 C  CA    . ALA A 1 555 ? 16.756  23.443 -10.227 1.00 91.28  ? 541  ALA A CA    1 
ATOM   4051 C  C     . ALA A 1 555 ? 16.346  24.518 -11.227 1.00 92.58  ? 541  ALA A C     1 
ATOM   4052 O  O     . ALA A 1 555 ? 15.841  24.187 -12.303 1.00 90.07  ? 541  ALA A O     1 
ATOM   4053 C  CB    . ALA A 1 555 ? 15.596  23.118 -9.286  1.00 80.27  ? 541  ALA A CB    1 
ATOM   4054 N  N     . ILE A 1 556 ? 16.517  25.801 -10.882 1.00 93.65  ? 542  ILE A N     1 
ATOM   4055 C  CA    . ILE A 1 556 ? 16.156  26.892 -11.793 1.00 96.65  ? 542  ILE A CA    1 
ATOM   4056 C  C     . ILE A 1 556 ? 17.215  27.141 -12.884 1.00 100.31 ? 542  ILE A C     1 
ATOM   4057 O  O     . ILE A 1 556 ? 16.889  27.759 -13.907 1.00 100.53 ? 542  ILE A O     1 
ATOM   4058 C  CB    . ILE A 1 556 ? 15.762  28.171 -11.031 1.00 96.27  ? 542  ILE A CB    1 
ATOM   4059 C  CG1   . ILE A 1 556 ? 15.084  27.809 -9.704  1.00 86.84  ? 542  ILE A CG1   1 
ATOM   4060 C  CG2   . ILE A 1 556 ? 14.784  28.997 -11.864 1.00 83.08  ? 542  ILE A CG2   1 
ATOM   4061 C  CD1   . ILE A 1 556 ? 14.023  28.811 -9.218  1.00 66.47  ? 542  ILE A CD1   1 
ATOM   4062 N  N     . THR A 1 557 ? 18.469  26.695 -12.709 1.00 99.85  ? 543  THR A N     1 
ATOM   4063 C  CA    . THR A 1 557 ? 19.484  26.897 -13.746 1.00 100.45 ? 543  THR A CA    1 
ATOM   4064 C  C     . THR A 1 557 ? 19.407  25.883 -14.885 1.00 104.00 ? 543  THR A C     1 
ATOM   4065 O  O     . THR A 1 557 ? 20.095  26.069 -15.896 1.00 105.86 ? 543  THR A O     1 
ATOM   4066 C  CB    . THR A 1 557 ? 20.909  26.789 -13.183 1.00 96.81  ? 543  THR A CB    1 
ATOM   4067 O  OG1   . THR A 1 557 ? 21.206  25.411 -12.905 1.00 96.16  ? 543  THR A OG1   1 
ATOM   4068 C  CG2   . THR A 1 557 ? 21.118  27.643 -11.961 1.00 94.12  ? 543  THR A CG2   1 
ATOM   4069 N  N     . LYS A 1 558 ? 18.730  24.778 -14.685 1.00 103.03 ? 544  LYS A N     1 
ATOM   4070 C  CA    . LYS A 1 558 ? 18.681  23.774 -15.718 1.00 103.14 ? 544  LYS A CA    1 
ATOM   4071 C  C     . LYS A 1 558 ? 17.488  23.960 -16.613 1.00 107.38 ? 544  LYS A C     1 
ATOM   4072 O  O     . LYS A 1 558 ? 17.540  23.607 -17.803 1.00 105.53 ? 544  LYS A O     1 
ATOM   4073 C  CB    . LYS A 1 558 ? 18.661  22.423 -15.059 1.00 99.78  ? 544  LYS A CB    1 
ATOM   4074 C  CG    . LYS A 1 558 ? 19.804  22.279 -14.069 1.00 99.07  ? 544  LYS A CG    1 
ATOM   4075 C  CD    . LYS A 1 558 ? 20.989  23.112 -14.495 1.00 99.81  ? 544  LYS A CD    1 
ATOM   4076 C  CE    . LYS A 1 558 ? 22.258  22.256 -14.573 1.00 97.38  ? 544  LYS A CE    1 
ATOM   4077 N  NZ    . LYS A 1 558 ? 22.049  21.059 -15.447 1.00 86.42  ? 544  LYS A NZ    1 
ATOM   4078 N  N     . ALA A 1 559 ? 16.434  24.540 -16.038 1.00 107.14 ? 545  ALA A N     1 
ATOM   4079 C  CA    . ALA A 1 559 ? 15.209  24.790 -16.778 1.00 106.30 ? 545  ALA A CA    1 
ATOM   4080 C  C     . ALA A 1 559 ? 15.049  26.290 -17.042 1.00 107.91 ? 545  ALA A C     1 
ATOM   4081 O  O     . ALA A 1 559 ? 13.959  26.805 -16.840 1.00 99.95  ? 545  ALA A O     1 
ATOM   4082 C  CB    . ALA A 1 559 ? 14.003  24.235 -16.031 1.00 83.58  ? 545  ALA A CB    1 
ATOM   4083 N  N     . LEU A 1 560 ? 16.163  26.946 -17.448 1.00 116.04 ? 546  LEU A N     1 
ATOM   4084 C  CA    . LEU A 1 560 ? 16.298  28.400 -17.820 1.00 113.32 ? 546  LEU A CA    1 
ATOM   4085 C  C     . LEU A 1 560 ? 17.053  28.425 -19.157 1.00 116.43 ? 546  LEU A C     1 
ATOM   4086 O  O     . LEU A 1 560 ? 16.656  29.098 -20.113 1.00 116.45 ? 546  LEU A O     1 
ATOM   4087 C  CB    . LEU A 1 560 ? 17.084  29.229 -16.801 1.00 102.36 ? 546  LEU A CB    1 
ATOM   4088 C  CG    . LEU A 1 560 ? 16.280  30.195 -15.923 1.00 91.73  ? 546  LEU A CG    1 
ATOM   4089 C  CD1   . LEU A 1 560 ? 16.351  31.602 -16.515 1.00 68.77  ? 546  LEU A CD1   1 
ATOM   4090 C  CD2   . LEU A 1 560 ? 14.864  29.692 -15.848 1.00 100.52 ? 546  LEU A CD2   1 
ATOM   4091 N  N     . GLU A 1 561 ? 18.129  27.612 -19.238 1.00 118.40 ? 547  GLU A N     1 
ATOM   4092 C  CA    . GLU A 1 561 ? 18.840  27.335 -20.512 1.00 119.61 ? 547  GLU A CA    1 
ATOM   4093 C  C     . GLU A 1 561 ? 18.185  26.108 -21.277 1.00 118.28 ? 547  GLU A C     1 
ATOM   4094 O  O     . GLU A 1 561 ? 18.746  25.540 -22.201 1.00 116.67 ? 547  GLU A O     1 
ATOM   4095 C  CB    . GLU A 1 561 ? 20.372  27.205 -20.391 1.00 117.84 ? 547  GLU A CB    1 
ATOM   4096 C  CG    . GLU A 1 561 ? 21.153  28.060 -21.408 1.00 112.22 ? 547  GLU A CG    1 
ATOM   4097 C  CD    . GLU A 1 561 ? 22.275  27.312 -22.138 1.00 114.63 ? 547  GLU A CD    1 
ATOM   4098 O  OE1   . GLU A 1 561 ? 23.059  26.622 -21.459 1.00 115.73 ? 547  GLU A OE1   1 
ATOM   4099 O  OE2   . GLU A 1 561 ? 22.378  27.399 -23.380 1.00 108.32 ? 547  GLU A OE2   1 
ATOM   4100 N  N     . ALA A 1 562 ? 17.024  25.695 -20.775 1.00 116.69 ? 548  ALA A N     1 
ATOM   4101 C  CA    . ALA A 1 562 ? 16.066  24.762 -21.332 1.00 117.22 ? 548  ALA A CA    1 
ATOM   4102 C  C     . ALA A 1 562 ? 15.080  25.567 -22.226 1.00 118.84 ? 548  ALA A C     1 
ATOM   4103 O  O     . ALA A 1 562 ? 14.240  24.983 -22.888 1.00 118.26 ? 548  ALA A O     1 
ATOM   4104 C  CB    . ALA A 1 562 ? 15.295  24.143 -20.203 1.00 111.79 ? 548  ALA A CB    1 
ATOM   4105 N  N     . ARG A 1 563 ? 15.263  26.885 -22.271 1.00 119.07 ? 549  ARG A N     1 
ATOM   4106 C  CA    . ARG A 1 563 ? 14.397  27.764 -23.054 1.00 109.32 ? 549  ARG A CA    1 
ATOM   4107 C  C     . ARG A 1 563 ? 14.922  28.160 -24.442 1.00 104.47 ? 549  ARG A C     1 
ATOM   4108 O  O     . ARG A 1 563 ? 14.751  27.423 -25.413 1.00 99.31  ? 549  ARG A O     1 
ATOM   4109 C  CB    . ARG A 1 563 ? 14.062  29.025 -22.252 1.00 94.70  ? 549  ARG A CB    1 
ATOM   4110 C  CG    . ARG A 1 563 ? 13.059  28.801 -21.133 1.00 94.44  ? 549  ARG A CG    1 
ATOM   4111 C  CD    . ARG A 1 563 ? 11.711  29.419 -21.468 1.00 84.66  ? 549  ARG A CD    1 
ATOM   4112 N  NE    . ARG A 1 563 ? 11.847  30.610 -22.300 1.00 68.58  ? 549  ARG A NE    1 
ATOM   4113 C  CZ    . ARG A 1 563 ? 12.428  31.737 -21.903 1.00 64.79  ? 549  ARG A CZ    1 
ATOM   4114 N  NH1   . ARG A 1 563 ? 12.931  31.831 -20.679 1.00 61.43  ? 549  ARG A NH1   1 
ATOM   4115 N  NH2   . ARG A 1 563 ? 12.507  32.772 -22.728 1.00 65.29  ? 549  ARG A NH2   1 
ATOM   4116 N  N     . ASN A 1 564 ? 15.560  29.326 -24.523 1.00 105.01 ? 550  ASN A N     1 
ATOM   4117 C  CA    . ASN A 1 564 ? 16.056  29.858 -25.785 1.00 99.50  ? 550  ASN A CA    1 
ATOM   4118 C  C     . ASN A 1 564 ? 17.379  29.283 -26.341 1.00 100.70 ? 550  ASN A C     1 
ATOM   4119 O  O     . ASN A 1 564 ? 18.202  30.041 -26.863 1.00 93.60  ? 550  ASN A O     1 
ATOM   4120 C  CB    . ASN A 1 564 ? 16.178  31.401 -25.727 1.00 30.00  ? 550  ASN A CB    1 
ATOM   4121 C  CG    . ASN A 1 564 ? 15.392  32.077 -24.561 1.00 30.00  ? 550  ASN A CG    1 
ATOM   4122 O  OD1   . ASN A 1 564 ? 14.159  32.105 -24.559 1.00 30.00  ? 550  ASN A OD1   1 
ATOM   4123 N  ND2   . ASN A 1 564 ? 16.150  32.677 -23.599 1.00 30.00  ? 550  ASN A ND2   1 
ATOM   4124 N  N     . SER A 1 565 ? 17.582  27.970 -26.211 1.00 104.86 ? 551  SER A N     1 
ATOM   4125 C  CA    . SER A 1 565 ? 18.758  27.321 -26.748 1.00 105.35 ? 551  SER A CA    1 
ATOM   4126 C  C     . SER A 1 565 ? 18.346  25.973 -27.377 1.00 101.09 ? 551  SER A C     1 
ATOM   4127 O  O     . SER A 1 565 ? 18.761  25.634 -28.487 1.00 103.64 ? 551  SER A O     1 
ATOM   4128 C  CB    . SER A 1 565 ? 19.807  27.103 -25.657 1.00 30.00  ? 551  SER A CB    1 
ATOM   4129 O  OG    . SER A 1 565 ? 20.852  26.279 -26.118 1.00 30.00  ? 551  SER A OG    1 
ATOM   4130 N  N     . THR B 1 17  ? 29.980  26.860 -34.746 1.00 64.97  ? 3    THR B N     1 
ATOM   4131 C  CA    . THR B 1 17  ? 29.483  28.232 -34.717 1.00 58.28  ? 3    THR B CA    1 
ATOM   4132 C  C     . THR B 1 17  ? 29.135  28.742 -36.117 1.00 50.76  ? 3    THR B C     1 
ATOM   4133 O  O     . THR B 1 17  ? 29.738  29.703 -36.598 1.00 48.93  ? 3    THR B O     1 
ATOM   4134 C  CB    . THR B 1 17  ? 30.507  29.189 -34.064 1.00 65.44  ? 3    THR B CB    1 
ATOM   4135 O  OG1   . THR B 1 17  ? 31.811  28.963 -34.621 1.00 75.96  ? 3    THR B OG1   1 
ATOM   4136 C  CG2   . THR B 1 17  ? 30.547  28.978 -32.560 1.00 63.23  ? 3    THR B CG2   1 
ATOM   4137 N  N     . PRO B 1 18  ? 28.153  28.114 -36.765 1.00 47.56  ? 4    PRO B N     1 
ATOM   4138 C  CA    . PRO B 1 18  ? 27.749  28.577 -38.098 1.00 43.67  ? 4    PRO B CA    1 
ATOM   4139 C  C     . PRO B 1 18  ? 27.230  30.008 -38.055 1.00 37.10  ? 4    PRO B C     1 
ATOM   4140 O  O     . PRO B 1 18  ? 26.634  30.454 -37.072 1.00 36.83  ? 4    PRO B O     1 
ATOM   4141 C  CB    . PRO B 1 18  ? 26.648  27.592 -38.514 1.00 42.30  ? 4    PRO B CB    1 
ATOM   4142 C  CG    . PRO B 1 18  ? 26.217  26.903 -37.267 1.00 45.23  ? 4    PRO B CG    1 
ATOM   4143 C  CD    . PRO B 1 18  ? 27.192  27.170 -36.169 1.00 46.09  ? 4    PRO B CD    1 
ATOM   4144 N  N     . TYR B 1 19  ? 27.482  30.728 -39.141 1.00 32.82  ? 5    TYR B N     1 
ATOM   4145 C  CA    . TYR B 1 19  ? 27.104  32.129 -39.228 1.00 29.72  ? 5    TYR B CA    1 
ATOM   4146 C  C     . TYR B 1 19  ? 25.596  32.287 -39.089 1.00 26.95  ? 5    TYR B C     1 
ATOM   4147 O  O     . TYR B 1 19  ? 24.821  31.564 -39.722 1.00 27.60  ? 5    TYR B O     1 
ATOM   4148 C  CB    . TYR B 1 19  ? 27.580  32.695 -40.560 1.00 26.19  ? 5    TYR B CB    1 
ATOM   4149 C  CG    . TYR B 1 19  ? 27.510  34.188 -40.693 1.00 26.18  ? 5    TYR B CG    1 
ATOM   4150 C  CD1   . TYR B 1 19  ? 26.350  34.807 -41.162 1.00 24.07  ? 5    TYR B CD1   1 
ATOM   4151 C  CD2   . TYR B 1 19  ? 28.616  34.983 -40.410 1.00 25.74  ? 5    TYR B CD2   1 
ATOM   4152 C  CE1   . TYR B 1 19  ? 26.291  36.172 -41.321 1.00 24.12  ? 5    TYR B CE1   1 
ATOM   4153 C  CE2   . TYR B 1 19  ? 28.562  36.351 -40.560 1.00 24.21  ? 5    TYR B CE2   1 
ATOM   4154 C  CZ    . TYR B 1 19  ? 27.400  36.937 -41.017 1.00 24.23  ? 5    TYR B CZ    1 
ATOM   4155 O  OH    . TYR B 1 19  ? 27.345  38.295 -41.181 1.00 25.73  ? 5    TYR B OH    1 
ATOM   4156 N  N     . CYS B 1 20  ? 25.180  33.225 -38.241 1.00 25.21  ? 6    CYS B N     1 
ATOM   4157 C  CA    . CYS B 1 20  ? 23.775  33.377 -37.899 1.00 23.98  ? 6    CYS B CA    1 
ATOM   4158 C  C     . CYS B 1 20  ? 23.444  34.862 -37.778 1.00 22.66  ? 6    CYS B C     1 
ATOM   4159 O  O     . CYS B 1 20  ? 24.306  35.728 -37.977 1.00 22.73  ? 6    CYS B O     1 
ATOM   4160 C  CB    . CYS B 1 20  ? 23.451  32.619 -36.602 1.00 24.03  ? 6    CYS B CB    1 
ATOM   4161 S  SG    . CYS B 1 20  ? 24.318  33.265 -35.169 1.00 28.48  ? 6    CYS B SG    1 
ATOM   4162 N  N     . VAL B 1 21  ? 22.171  35.143 -37.445 1.00 20.65  ? 7    VAL B N     1 
ATOM   4163 C  CA    . VAL B 1 21  ? 21.672  36.517 -37.347 1.00 20.13  ? 7    VAL B CA    1 
ATOM   4164 C  C     . VAL B 1 21  ? 22.513  37.344 -36.382 1.00 19.79  ? 7    VAL B C     1 
ATOM   4165 O  O     . VAL B 1 21  ? 22.807  38.520 -36.642 1.00 17.55  ? 7    VAL B O     1 
ATOM   4166 C  CB    . VAL B 1 21  ? 20.185  36.521 -36.928 1.00 18.29  ? 7    VAL B CB    1 
ATOM   4167 C  CG1   . VAL B 1 21  ? 19.760  37.914 -36.515 1.00 17.80  ? 7    VAL B CG1   1 
ATOM   4168 C  CG2   . VAL B 1 21  ? 19.311  36.017 -38.063 1.00 19.08  ? 7    VAL B CG2   1 
ATOM   4169 N  N     . ALA B 1 22  ? 22.892  36.762 -35.241 1.00 18.90  ? 8    ALA B N     1 
ATOM   4170 C  CA    . ALA B 1 22  ? 23.747  37.491 -34.312 1.00 20.20  ? 8    ALA B CA    1 
ATOM   4171 C  C     . ALA B 1 22  ? 25.003  38.002 -35.015 1.00 21.31  ? 8    ALA B C     1 
ATOM   4172 O  O     . ALA B 1 22  ? 25.400  39.157 -34.831 1.00 19.54  ? 8    ALA B O     1 
ATOM   4173 C  CB    . ALA B 1 22  ? 24.116  36.613 -33.113 1.00 20.18  ? 8    ALA B CB    1 
ATOM   4174 N  N     . ASP B 1 23  ? 25.632  37.158 -35.836 1.00 23.67  ? 9    ASP B N     1 
ATOM   4175 C  CA    . ASP B 1 23  ? 26.842  37.571 -36.543 1.00 23.98  ? 9    ASP B CA    1 
ATOM   4176 C  C     . ASP B 1 23  ? 26.547  38.643 -37.588 1.00 22.58  ? 9    ASP B C     1 
ATOM   4177 O  O     . ASP B 1 23  ? 27.332  39.585 -37.752 1.00 21.51  ? 9    ASP B O     1 
ATOM   4178 C  CB    . ASP B 1 23  ? 27.507  36.356 -37.190 1.00 26.33  ? 9    ASP B CB    1 
ATOM   4179 C  CG    . ASP B 1 23  ? 27.827  35.268 -36.186 1.00 27.55  ? 9    ASP B CG    1 
ATOM   4180 O  OD1   . ASP B 1 23  ? 28.501  35.571 -35.179 1.00 27.56  ? 9    ASP B OD1   1 
ATOM   4181 O  OD2   . ASP B 1 23  ? 27.407  34.109 -36.408 1.00 28.00  ? 9    ASP B OD2   1 
ATOM   4182 N  N     . TYR B 1 24  ? 25.430  38.511 -38.316 1.00 21.38  ? 10   TYR B N     1 
ATOM   4183 C  CA    . TYR B 1 24  ? 25.057  39.522 -39.301 1.00 21.70  ? 10   TYR B CA    1 
ATOM   4184 C  C     . TYR B 1 24  ? 24.867  40.887 -38.655 1.00 21.30  ? 10   TYR B C     1 
ATOM   4185 O  O     . TYR B 1 24  ? 25.332  41.908 -39.185 1.00 20.35  ? 10   TYR B O     1 
ATOM   4186 C  CB    . TYR B 1 24  ? 23.779  39.094 -40.022 1.00 20.09  ? 10   TYR B CB    1 
ATOM   4187 C  CG    . TYR B 1 24  ? 23.426  39.943 -41.223 1.00 21.17  ? 10   TYR B CG    1 
ATOM   4188 C  CD1   . TYR B 1 24  ? 22.637  41.076 -41.082 1.00 21.21  ? 10   TYR B CD1   1 
ATOM   4189 C  CD2   . TYR B 1 24  ? 23.869  39.603 -42.500 1.00 21.92  ? 10   TYR B CD2   1 
ATOM   4190 C  CE1   . TYR B 1 24  ? 22.304  41.851 -42.177 1.00 23.66  ? 10   TYR B CE1   1 
ATOM   4191 C  CE2   . TYR B 1 24  ? 23.531  40.377 -43.612 1.00 23.27  ? 10   TYR B CE2   1 
ATOM   4192 C  CZ    . TYR B 1 24  ? 22.746  41.497 -43.435 1.00 22.36  ? 10   TYR B CZ    1 
ATOM   4193 O  OH    . TYR B 1 24  ? 22.401  42.296 -44.492 1.00 22.40  ? 10   TYR B OH    1 
ATOM   4194 N  N     . LEU B 1 25  ? 24.192  40.924 -37.504 1.00 20.78  ? 11   LEU B N     1 
ATOM   4195 C  CA    . LEU B 1 25  ? 24.007  42.185 -36.791 1.00 20.84  ? 11   LEU B CA    1 
ATOM   4196 C  C     . LEU B 1 25  ? 25.351  42.794 -36.403 1.00 21.10  ? 11   LEU B C     1 
ATOM   4197 O  O     . LEU B 1 25  ? 25.561  44.005 -36.538 1.00 20.82  ? 11   LEU B O     1 
ATOM   4198 C  CB    . LEU B 1 25  ? 23.146  41.945 -35.548 1.00 19.64  ? 11   LEU B CB    1 
ATOM   4199 C  CG    . LEU B 1 25  ? 22.858  43.093 -34.583 1.00 17.61  ? 11   LEU B CG    1 
ATOM   4200 C  CD1   . LEU B 1 25  ? 22.326  44.328 -35.333 1.00 17.11  ? 11   LEU B CD1   1 
ATOM   4201 C  CD2   . LEU B 1 25  ? 21.875  42.650 -33.490 1.00 18.61  ? 11   LEU B CD2   1 
ATOM   4202 N  N     . LEU B 1 26  ? 26.274  41.966 -35.920 1.00 19.73  ? 12   LEU B N     1 
ATOM   4203 C  CA    . LEU B 1 26  ? 27.581  42.482 -35.519 1.00 22.15  ? 12   LEU B CA    1 
ATOM   4204 C  C     . LEU B 1 26  ? 28.373  42.993 -36.718 1.00 23.95  ? 12   LEU B C     1 
ATOM   4205 O  O     . LEU B 1 26  ? 29.029  44.036 -36.632 1.00 22.89  ? 12   LEU B O     1 
ATOM   4206 C  CB    . LEU B 1 26  ? 28.349  41.405 -34.763 1.00 22.53  ? 12   LEU B CB    1 
ATOM   4207 C  CG    . LEU B 1 26  ? 27.689  41.106 -33.407 1.00 20.74  ? 12   LEU B CG    1 
ATOM   4208 C  CD1   . LEU B 1 26  ? 28.275  39.882 -32.730 1.00 23.38  ? 12   LEU B CD1   1 
ATOM   4209 C  CD2   . LEU B 1 26  ? 27.668  42.328 -32.462 1.00 21.63  ? 12   LEU B CD2   1 
ATOM   4210 N  N     . ASP B 1 27  ? 28.306  42.279 -37.848 1.00 23.78  ? 13   ASP B N     1 
ATOM   4211 C  CA    . ASP B 1 27  ? 28.957  42.743 -39.067 1.00 24.65  ? 13   ASP B CA    1 
ATOM   4212 C  C     . ASP B 1 27  ? 28.425  44.107 -39.490 1.00 23.69  ? 13   ASP B C     1 
ATOM   4213 O  O     . ASP B 1 27  ? 29.201  45.007 -39.825 1.00 23.24  ? 13   ASP B O     1 
ATOM   4214 C  CB    . ASP B 1 27  ? 28.738  41.719 -40.187 1.00 24.43  ? 13   ASP B CB    1 
ATOM   4215 C  CG    . ASP B 1 27  ? 29.770  40.593 -40.178 1.00 29.40  ? 13   ASP B CG    1 
ATOM   4216 O  OD1   . ASP B 1 27  ? 30.894  40.820 -39.699 1.00 33.10  ? 13   ASP B OD1   1 
ATOM   4217 O  OD2   . ASP B 1 27  ? 29.452  39.472 -40.648 1.00 31.14  ? 13   ASP B OD2   1 
ATOM   4218 N  N     . ARG B 1 28  ? 27.104  44.293 -39.443 1.00 22.16  ? 14   ARG B N     1 
ATOM   4219 C  CA    . ARG B 1 28  ? 26.511  45.557 -39.873 1.00 21.89  ? 14   ARG B CA    1 
ATOM   4220 C  C     . ARG B 1 28  ? 26.792  46.693 -38.895 1.00 23.78  ? 14   ARG B C     1 
ATOM   4221 O  O     . ARG B 1 28  ? 26.916  47.850 -39.311 1.00 23.55  ? 14   ARG B O     1 
ATOM   4222 C  CB    . ARG B 1 28  ? 24.997  45.390 -40.029 1.00 22.77  ? 14   ARG B CB    1 
ATOM   4223 C  CG    . ARG B 1 28  ? 24.534  44.461 -41.131 1.00 21.59  ? 14   ARG B CG    1 
ATOM   4224 C  CD    . ARG B 1 28  ? 25.382  44.604 -42.384 1.00 24.00  ? 14   ARG B CD    1 
ATOM   4225 N  NE    . ARG B 1 28  ? 24.541  44.611 -43.571 1.00 22.41  ? 14   ARG B NE    1 
ATOM   4226 C  CZ    . ARG B 1 28  ? 24.980  44.613 -44.821 1.00 25.06  ? 14   ARG B CZ    1 
ATOM   4227 N  NH1   . ARG B 1 28  ? 26.273  44.545 -45.101 1.00 24.58  ? 14   ARG B NH1   1 
ATOM   4228 N  NH2   . ARG B 1 28  ? 24.098  44.707 -45.817 1.00 23.62  ? 14   ARG B NH2   1 
ATOM   4229 N  N     . LEU B 1 29  ? 26.839  46.387 -37.596 1.00 21.82  ? 15   LEU B N     1 
ATOM   4230 C  CA    . LEU B 1 29  ? 27.187  47.379 -36.580 1.00 24.35  ? 15   LEU B CA    1 
ATOM   4231 C  C     . LEU B 1 29  ? 28.577  47.958 -36.809 1.00 24.92  ? 15   LEU B C     1 
ATOM   4232 O  O     . LEU B 1 29  ? 28.766  49.182 -36.800 1.00 22.95  ? 15   LEU B O     1 
ATOM   4233 C  CB    . LEU B 1 29  ? 27.111  46.726 -35.200 1.00 24.73  ? 15   LEU B CB    1 
ATOM   4234 C  CG    . LEU B 1 29  ? 27.178  47.548 -33.918 1.00 25.20  ? 15   LEU B CG    1 
ATOM   4235 C  CD1   . LEU B 1 29  ? 26.410  48.883 -34.024 1.00 23.84  ? 15   LEU B CD1   1 
ATOM   4236 C  CD2   . LEU B 1 29  ? 26.680  46.664 -32.766 1.00 23.59  ? 15   LEU B CD2   1 
ATOM   4237 N  N     . THR B 1 30  ? 29.571  47.086 -36.993 1.00 25.28  ? 16   THR B N     1 
ATOM   4238 C  CA    . THR B 1 30  ? 30.922  47.556 -37.279 1.00 26.88  ? 16   THR B CA    1 
ATOM   4239 C  C     . THR B 1 30  ? 30.984  48.326 -38.595 1.00 26.77  ? 16   THR B C     1 
ATOM   4240 O  O     . THR B 1 30  ? 31.765  49.276 -38.708 1.00 28.58  ? 16   THR B O     1 
ATOM   4241 C  CB    . THR B 1 30  ? 31.906  46.385 -37.243 1.00 27.19  ? 16   THR B CB    1 
ATOM   4242 O  OG1   . THR B 1 30  ? 31.651  45.490 -38.328 1.00 29.51  ? 16   THR B OG1   1 
ATOM   4243 C  CG2   . THR B 1 30  ? 31.761  45.639 -35.936 1.00 27.55  ? 16   THR B CG2   1 
ATOM   4244 N  N     . ASP B 1 31  ? 30.178  47.941 -39.599 1.00 27.10  ? 17   ASP B N     1 
ATOM   4245 C  CA    . ASP B 1 31  ? 30.109  48.731 -40.832 1.00 26.89  ? 17   ASP B CA    1 
ATOM   4246 C  C     . ASP B 1 31  ? 29.753  50.188 -40.543 1.00 26.52  ? 17   ASP B C     1 
ATOM   4247 O  O     . ASP B 1 31  ? 30.232  51.097 -41.236 1.00 24.95  ? 17   ASP B O     1 
ATOM   4248 C  CB    . ASP B 1 31  ? 29.068  48.150 -41.801 1.00 26.19  ? 17   ASP B CB    1 
ATOM   4249 C  CG    . ASP B 1 31  ? 29.514  46.861 -42.478 1.00 27.35  ? 17   ASP B CG    1 
ATOM   4250 O  OD1   . ASP B 1 31  ? 30.726  46.534 -42.443 1.00 26.37  ? 17   ASP B OD1   1 
ATOM   4251 O  OD2   . ASP B 1 31  ? 28.625  46.191 -43.076 1.00 25.24  ? 17   ASP B OD2   1 
ATOM   4252 N  N     . CYS B 1 32  ? 28.926  50.432 -39.522 1.00 22.97  ? 18   CYS B N     1 
ATOM   4253 C  CA    . CYS B 1 32  ? 28.456  51.777 -39.215 1.00 21.97  ? 18   CYS B CA    1 
ATOM   4254 C  C     . CYS B 1 32  ? 29.444  52.577 -38.374 1.00 22.65  ? 18   CYS B C     1 
ATOM   4255 O  O     . CYS B 1 32  ? 29.217  53.771 -38.152 1.00 24.40  ? 18   CYS B O     1 
ATOM   4256 C  CB    . CYS B 1 32  ? 27.108  51.708 -38.491 1.00 23.29  ? 18   CYS B CB    1 
ATOM   4257 S  SG    . CYS B 1 32  ? 25.743  51.081 -39.509 1.00 18.21  ? 18   CYS B SG    1 
ATOM   4258 N  N     . GLY B 1 33  ? 30.532  51.963 -37.920 1.00 23.18  ? 19   GLY B N     1 
ATOM   4259 C  CA    . GLY B 1 33  ? 31.588  52.666 -37.216 1.00 25.44  ? 19   GLY B CA    1 
ATOM   4260 C  C     . GLY B 1 33  ? 31.764  52.293 -35.756 1.00 25.28  ? 19   GLY B C     1 
ATOM   4261 O  O     . GLY B 1 33  ? 32.682  52.810 -35.113 1.00 25.20  ? 19   GLY B O     1 
ATOM   4262 N  N     . ALA B 1 34  ? 30.941  51.406 -35.217 1.00 23.94  ? 20   ALA B N     1 
ATOM   4263 C  CA    . ALA B 1 34  ? 31.049  51.002 -33.822 1.00 22.39  ? 20   ALA B CA    1 
ATOM   4264 C  C     . ALA B 1 34  ? 32.014  49.826 -33.718 1.00 25.97  ? 20   ALA B C     1 
ATOM   4265 O  O     . ALA B 1 34  ? 31.788  48.782 -34.335 1.00 27.62  ? 20   ALA B O     1 
ATOM   4266 C  CB    . ALA B 1 34  ? 29.675  50.617 -33.279 1.00 21.53  ? 20   ALA B CB    1 
ATOM   4267 N  N     . ASP B 1 35  ? 33.068  49.985 -32.913 1.00 22.30  ? 21   ASP B N     1 
ATOM   4268 C  CA    . ASP B 1 35  ? 34.020  48.919 -32.642 1.00 23.43  ? 21   ASP B CA    1 
ATOM   4269 C  C     . ASP B 1 35  ? 33.867  48.360 -31.239 1.00 23.83  ? 21   ASP B C     1 
ATOM   4270 O  O     . ASP B 1 35  ? 34.634  47.470 -30.846 1.00 23.11  ? 21   ASP B O     1 
ATOM   4271 C  CB    . ASP B 1 35  ? 35.458  49.426 -32.849 1.00 22.79  ? 21   ASP B CB    1 
ATOM   4272 C  CG    . ASP B 1 35  ? 35.683  49.967 -34.253 1.00 26.95  ? 21   ASP B CG    1 
ATOM   4273 O  OD1   . ASP B 1 35  ? 35.225  49.309 -35.214 1.00 26.04  ? 21   ASP B OD1   1 
ATOM   4274 O  OD2   . ASP B 1 35  ? 36.288  51.054 -34.398 1.00 27.07  ? 21   ASP B OD2   1 
ATOM   4275 N  N     . HIS B 1 36  ? 32.885  48.852 -30.486 1.00 22.97  ? 22   HIS B N     1 
ATOM   4276 C  CA    . HIS B 1 36  ? 32.619  48.423 -29.125 1.00 21.74  ? 22   HIS B CA    1 
ATOM   4277 C  C     . HIS B 1 36  ? 31.118  48.315 -28.926 1.00 20.97  ? 22   HIS B C     1 
ATOM   4278 O  O     . HIS B 1 36  ? 30.333  49.007 -29.583 1.00 18.04  ? 22   HIS B O     1 
ATOM   4279 C  CB    . HIS B 1 36  ? 33.195  49.396 -28.082 1.00 21.65  ? 22   HIS B CB    1 
ATOM   4280 C  CG    . HIS B 1 36  ? 34.686  49.505 -28.114 1.00 22.57  ? 22   HIS B CG    1 
ATOM   4281 N  ND1   . HIS B 1 36  ? 35.361  50.239 -29.067 1.00 24.09  ? 22   HIS B ND1   1 
ATOM   4282 C  CD2   . HIS B 1 36  ? 35.634  48.970 -27.310 1.00 23.35  ? 22   HIS B CD2   1 
ATOM   4283 C  CE1   . HIS B 1 36  ? 36.662  50.143 -28.853 1.00 24.38  ? 22   HIS B CE1   1 
ATOM   4284 N  NE2   . HIS B 1 36  ? 36.854  49.377 -27.794 1.00 24.91  ? 22   HIS B NE2   1 
ATOM   4285 N  N     . LEU B 1 37  ? 30.728  47.458 -27.986 1.00 21.63  ? 23   LEU B N     1 
ATOM   4286 C  CA    . LEU B 1 37  ? 29.337  47.319 -27.573 1.00 20.36  ? 23   LEU B CA    1 
ATOM   4287 C  C     . LEU B 1 37  ? 29.286  47.446 -26.059 1.00 19.72  ? 23   LEU B C     1 
ATOM   4288 O  O     . LEU B 1 37  ? 29.895  46.643 -25.344 1.00 20.21  ? 23   LEU B O     1 
ATOM   4289 C  CB    . LEU B 1 37  ? 28.756  45.972 -28.034 1.00 19.33  ? 23   LEU B CB    1 
ATOM   4290 C  CG    . LEU B 1 37  ? 27.335  45.597 -27.599 1.00 21.26  ? 23   LEU B CG    1 
ATOM   4291 C  CD1   . LEU B 1 37  ? 26.314  46.469 -28.286 1.00 19.55  ? 23   LEU B CD1   1 
ATOM   4292 C  CD2   . LEU B 1 37  ? 27.025  44.108 -27.840 1.00 19.37  ? 23   LEU B CD2   1 
ATOM   4293 N  N     . PHE B 1 38  ? 28.534  48.426 -25.576 1.00 17.47  ? 24   PHE B N     1 
ATOM   4294 C  CA    . PHE B 1 38  ? 28.327  48.652 -24.161 1.00 18.11  ? 24   PHE B CA    1 
ATOM   4295 C  C     . PHE B 1 38  ? 27.042  47.972 -23.712 1.00 18.48  ? 24   PHE B C     1 
ATOM   4296 O  O     . PHE B 1 38  ? 26.100  47.816 -24.495 1.00 19.33  ? 24   PHE B O     1 
ATOM   4297 C  CB    . PHE B 1 38  ? 28.225  50.153 -23.876 1.00 17.79  ? 24   PHE B CB    1 
ATOM   4298 C  CG    . PHE B 1 38  ? 29.441  50.926 -24.277 1.00 19.10  ? 24   PHE B CG    1 
ATOM   4299 C  CD1   . PHE B 1 38  ? 29.595  51.392 -25.577 1.00 18.49  ? 24   PHE B CD1   1 
ATOM   4300 C  CD2   . PHE B 1 38  ? 30.440  51.195 -23.348 1.00 19.11  ? 24   PHE B CD2   1 
ATOM   4301 C  CE1   . PHE B 1 38  ? 30.754  52.109 -25.943 1.00 17.40  ? 24   PHE B CE1   1 
ATOM   4302 C  CE2   . PHE B 1 38  ? 31.568  51.911 -23.713 1.00 19.05  ? 24   PHE B CE2   1 
ATOM   4303 C  CZ    . PHE B 1 38  ? 31.718  52.372 -25.012 1.00 16.69  ? 24   PHE B CZ    1 
ATOM   4304 N  N     . GLY B 1 39  ? 27.008  47.565 -22.449 1.00 19.04  ? 25   GLY B N     1 
ATOM   4305 C  CA    . GLY B 1 39  ? 25.745  47.138 -21.872 1.00 17.36  ? 25   GLY B CA    1 
ATOM   4306 C  C     . GLY B 1 39  ? 25.954  46.274 -20.636 1.00 18.87  ? 25   GLY B C     1 
ATOM   4307 O  O     . GLY B 1 39  ? 27.008  46.306 -20.007 1.00 16.97  ? 25   GLY B O     1 
ATOM   4308 N  N     . VAL B 1 40  ? 24.901  45.541 -20.285 1.00 17.97  ? 26   VAL B N     1 
ATOM   4309 C  CA    . VAL B 1 40  ? 24.899  44.708 -19.081 1.00 19.33  ? 26   VAL B CA    1 
ATOM   4310 C  C     . VAL B 1 40  ? 24.270  43.377 -19.469 1.00 19.14  ? 26   VAL B C     1 
ATOM   4311 O  O     . VAL B 1 40  ? 23.206  43.354 -20.108 1.00 16.51  ? 26   VAL B O     1 
ATOM   4312 C  CB    . VAL B 1 40  ? 24.138  45.382 -17.921 1.00 18.71  ? 26   VAL B CB    1 
ATOM   4313 C  CG1   . VAL B 1 40  ? 23.974  44.431 -16.714 1.00 19.69  ? 26   VAL B CG1   1 
ATOM   4314 C  CG2   . VAL B 1 40  ? 24.819  46.675 -17.496 1.00 17.13  ? 26   VAL B CG2   1 
ATOM   4315 N  N     . PRO B 1 41  ? 24.876  42.254 -19.110 1.00 21.59  ? 27   PRO B N     1 
ATOM   4316 C  CA    . PRO B 1 41  ? 24.327  40.965 -19.522 1.00 23.25  ? 27   PRO B CA    1 
ATOM   4317 C  C     . PRO B 1 41  ? 23.053  40.630 -18.765 1.00 22.40  ? 27   PRO B C     1 
ATOM   4318 O  O     . PRO B 1 41  ? 22.755  41.185 -17.707 1.00 19.86  ? 27   PRO B O     1 
ATOM   4319 C  CB    . PRO B 1 41  ? 25.446  39.983 -19.174 1.00 28.25  ? 27   PRO B CB    1 
ATOM   4320 C  CG    . PRO B 1 41  ? 26.086  40.615 -17.988 1.00 29.80  ? 27   PRO B CG    1 
ATOM   4321 C  CD    . PRO B 1 41  ? 26.084  42.090 -18.285 1.00 24.69  ? 27   PRO B CD    1 
ATOM   4322 N  N     . GLY B 1 42  ? 22.303  39.708 -19.353 1.00 22.89  ? 28   GLY B N     1 
ATOM   4323 C  CA    . GLY B 1 42  ? 21.119  39.116 -18.760 1.00 23.54  ? 28   GLY B CA    1 
ATOM   4324 C  C     . GLY B 1 42  ? 20.859  37.832 -19.509 1.00 25.80  ? 28   GLY B C     1 
ATOM   4325 O  O     . GLY B 1 42  ? 21.365  37.632 -20.619 1.00 23.45  ? 28   GLY B O     1 
ATOM   4326 N  N     . ASP B 1 43  ? 20.086  36.945 -18.886 1.00 25.35  ? 29   ASP B N     1 
ATOM   4327 C  CA    . ASP B 1 43  ? 19.889  35.621 -19.473 1.00 28.36  ? 29   ASP B CA    1 
ATOM   4328 C  C     . ASP B 1 43  ? 19.284  35.693 -20.883 1.00 26.11  ? 29   ASP B C     1 
ATOM   4329 O  O     . ASP B 1 43  ? 19.618  34.865 -21.744 1.00 25.36  ? 29   ASP B O     1 
ATOM   4330 C  CB    . ASP B 1 43  ? 19.074  34.750 -18.503 1.00 28.11  ? 29   ASP B CB    1 
ATOM   4331 C  CG    . ASP B 1 43  ? 17.603  35.098 -18.474 1.00 27.55  ? 29   ASP B CG    1 
ATOM   4332 O  OD1   . ASP B 1 43  ? 17.274  36.286 -18.271 1.00 23.78  ? 29   ASP B OD1   1 
ATOM   4333 O  OD2   . ASP B 1 43  ? 16.776  34.163 -18.573 1.00 29.01  ? 29   ASP B OD2   1 
ATOM   4334 N  N     . TYR B 1 44  ? 18.481  36.718 -21.173 1.00 23.56  ? 30   TYR B N     1 
ATOM   4335 C  CA    . TYR B 1 44  ? 17.881  36.815 -22.498 1.00 22.74  ? 30   TYR B CA    1 
ATOM   4336 C  C     . TYR B 1 44  ? 18.862  37.249 -23.579 1.00 23.51  ? 30   TYR B C     1 
ATOM   4337 O  O     . TYR B 1 44  ? 18.527  37.117 -24.761 1.00 22.28  ? 30   TYR B O     1 
ATOM   4338 C  CB    . TYR B 1 44  ? 16.691  37.796 -22.498 1.00 20.87  ? 30   TYR B CB    1 
ATOM   4339 C  CG    . TYR B 1 44  ? 15.532  37.377 -21.608 1.00 21.69  ? 30   TYR B CG    1 
ATOM   4340 C  CD1   . TYR B 1 44  ? 14.992  36.100 -21.696 1.00 22.92  ? 30   TYR B CD1   1 
ATOM   4341 C  CD2   . TYR B 1 44  ? 14.963  38.276 -20.699 1.00 18.52  ? 30   TYR B CD2   1 
ATOM   4342 C  CE1   . TYR B 1 44  ? 13.941  35.716 -20.884 1.00 23.76  ? 30   TYR B CE1   1 
ATOM   4343 C  CE2   . TYR B 1 44  ? 13.913  37.896 -19.881 1.00 20.26  ? 30   TYR B CE2   1 
ATOM   4344 C  CZ    . TYR B 1 44  ? 13.401  36.619 -19.989 1.00 21.02  ? 30   TYR B CZ    1 
ATOM   4345 O  OH    . TYR B 1 44  ? 12.348  36.239 -19.199 1.00 21.89  ? 30   TYR B OH    1 
ATOM   4346 N  N     . ASN B 1 45  ? 20.040  37.778 -23.224 1.00 22.19  ? 31   ASN B N     1 
ATOM   4347 C  CA    . ASN B 1 45  ? 21.014  38.197 -24.228 1.00 22.72  ? 31   ASN B CA    1 
ATOM   4348 C  C     . ASN B 1 45  ? 22.347  37.455 -24.146 1.00 25.73  ? 31   ASN B C     1 
ATOM   4349 O  O     . ASN B 1 45  ? 23.277  37.822 -24.873 1.00 25.65  ? 31   ASN B O     1 
ATOM   4350 C  CB    . ASN B 1 45  ? 21.276  39.717 -24.161 1.00 20.78  ? 31   ASN B CB    1 
ATOM   4351 C  CG    . ASN B 1 45  ? 22.008  40.177 -22.869 1.00 21.75  ? 31   ASN B CG    1 
ATOM   4352 O  OD1   . ASN B 1 45  ? 22.842  39.475 -22.298 1.00 20.74  ? 31   ASN B OD1   1 
ATOM   4353 N  ND2   . ASN B 1 45  ? 21.759  41.411 -22.486 1.00 18.42  ? 31   ASN B ND2   1 
ATOM   4354 N  N     . LEU B 1 46  ? 22.464  36.421 -23.304 1.00 25.58  ? 32   LEU B N     1 
ATOM   4355 C  CA    . LEU B 1 46  ? 23.766  35.800 -23.062 1.00 28.02  ? 32   LEU B CA    1 
ATOM   4356 C  C     . LEU B 1 46  ? 24.297  35.111 -24.307 1.00 30.90  ? 32   LEU B C     1 
ATOM   4357 O  O     . LEU B 1 46  ? 25.494  35.191 -24.613 1.00 30.09  ? 32   LEU B O     1 
ATOM   4358 C  CB    . LEU B 1 46  ? 23.669  34.786 -21.927 1.00 31.82  ? 32   LEU B CB    1 
ATOM   4359 C  CG    . LEU B 1 46  ? 23.512  35.327 -20.516 1.00 35.99  ? 32   LEU B CG    1 
ATOM   4360 C  CD1   . LEU B 1 46  ? 23.840  34.223 -19.542 1.00 46.59  ? 32   LEU B CD1   1 
ATOM   4361 C  CD2   . LEU B 1 46  ? 24.399  36.545 -20.309 1.00 34.87  ? 32   LEU B CD2   1 
ATOM   4362 N  N     . GLN B 1 47  ? 23.432  34.388 -25.012 1.00 30.43  ? 33   GLN B N     1 
ATOM   4363 C  CA    . GLN B 1 47  ? 23.882  33.684 -26.202 1.00 30.93  ? 33   GLN B CA    1 
ATOM   4364 C  C     . GLN B 1 47  ? 24.314  34.665 -27.284 1.00 29.80  ? 33   GLN B C     1 
ATOM   4365 O  O     . GLN B 1 47  ? 25.300  34.420 -27.980 1.00 28.62  ? 33   GLN B O     1 
ATOM   4366 C  CB    . GLN B 1 47  ? 22.784  32.755 -26.700 1.00 35.55  ? 33   GLN B CB    1 
ATOM   4367 C  CG    . GLN B 1 47  ? 22.341  31.747 -25.659 1.00 45.37  ? 33   GLN B CG    1 
ATOM   4368 C  CD    . GLN B 1 47  ? 22.217  30.345 -26.218 1.00 59.08  ? 33   GLN B CD    1 
ATOM   4369 O  OE1   . GLN B 1 47  ? 21.194  29.683 -26.051 1.00 68.59  ? 33   GLN B OE1   1 
ATOM   4370 N  NE2   . GLN B 1 47  ? 23.269  29.882 -26.882 1.00 57.35  ? 33   GLN B NE2   1 
ATOM   4371 N  N     . PHE B 1 48  ? 23.589  35.782 -27.447 1.00 25.07  ? 34   PHE B N     1 
ATOM   4372 C  CA    . PHE B 1 48  ? 24.079  36.831 -28.335 1.00 24.11  ? 34   PHE B CA    1 
ATOM   4373 C  C     . PHE B 1 48  ? 25.430  37.354 -27.868 1.00 25.56  ? 34   PHE B C     1 
ATOM   4374 O  O     . PHE B 1 48  ? 26.326  37.611 -28.685 1.00 23.50  ? 34   PHE B O     1 
ATOM   4375 C  CB    . PHE B 1 48  ? 23.070  37.974 -28.428 1.00 21.52  ? 34   PHE B CB    1 
ATOM   4376 C  CG    . PHE B 1 48  ? 23.567  39.156 -29.215 1.00 21.02  ? 34   PHE B CG    1 
ATOM   4377 C  CD1   . PHE B 1 48  ? 23.737  39.063 -30.591 1.00 20.22  ? 34   PHE B CD1   1 
ATOM   4378 C  CD2   . PHE B 1 48  ? 23.847  40.362 -28.588 1.00 21.41  ? 34   PHE B CD2   1 
ATOM   4379 C  CE1   . PHE B 1 48  ? 24.191  40.139 -31.329 1.00 21.31  ? 34   PHE B CE1   1 
ATOM   4380 C  CE2   . PHE B 1 48  ? 24.295  41.458 -29.325 1.00 18.27  ? 34   PHE B CE2   1 
ATOM   4381 C  CZ    . PHE B 1 48  ? 24.462  41.344 -30.695 1.00 21.55  ? 34   PHE B CZ    1 
ATOM   4382 N  N     . LEU B 1 49  ? 25.593  37.518 -26.550 1.00 24.44  ? 35   LEU B N     1 
ATOM   4383 C  CA    . LEU B 1 49  ? 26.850  38.020 -26.009 1.00 27.80  ? 35   LEU B CA    1 
ATOM   4384 C  C     . LEU B 1 49  ? 28.027  37.126 -26.368 1.00 28.33  ? 35   LEU B C     1 
ATOM   4385 O  O     . LEU B 1 49  ? 29.137  37.626 -26.575 1.00 29.38  ? 35   LEU B O     1 
ATOM   4386 C  CB    . LEU B 1 49  ? 26.743  38.158 -24.490 1.00 29.10  ? 35   LEU B CB    1 
ATOM   4387 C  CG    . LEU B 1 49  ? 26.808  39.580 -23.945 1.00 30.09  ? 35   LEU B CG    1 
ATOM   4388 C  CD1   . LEU B 1 49  ? 26.708  39.558 -22.427 1.00 31.87  ? 35   LEU B CD1   1 
ATOM   4389 C  CD2   . LEU B 1 49  ? 28.071  40.282 -24.390 1.00 28.00  ? 35   LEU B CD2   1 
ATOM   4390 N  N     . ASP B 1 50  ? 27.820  35.808 -26.435 1.00 28.59  ? 36   ASP B N     1 
ATOM   4391 C  CA    . ASP B 1 50  ? 28.912  34.933 -26.848 1.00 31.66  ? 36   ASP B CA    1 
ATOM   4392 C  C     . ASP B 1 50  ? 29.420  35.301 -28.235 1.00 32.27  ? 36   ASP B C     1 
ATOM   4393 O  O     . ASP B 1 50  ? 30.624  35.189 -28.516 1.00 32.19  ? 36   ASP B O     1 
ATOM   4394 C  CB    . ASP B 1 50  ? 28.470  33.471 -26.822 1.00 33.98  ? 36   ASP B CB    1 
ATOM   4395 C  CG    . ASP B 1 50  ? 28.271  32.940 -25.407 1.00 39.32  ? 36   ASP B CG    1 
ATOM   4396 O  OD1   . ASP B 1 50  ? 28.820  33.535 -24.451 1.00 38.25  ? 36   ASP B OD1   1 
ATOM   4397 O  OD2   . ASP B 1 50  ? 27.582  31.909 -25.264 1.00 39.24  ? 36   ASP B OD2   1 
ATOM   4398 N  N     . HIS B 1 51  ? 28.528  35.759 -29.111 1.00 28.50  ? 37   HIS B N     1 
ATOM   4399 C  CA    . HIS B 1 51  ? 28.984  36.160 -30.431 1.00 28.41  ? 37   HIS B CA    1 
ATOM   4400 C  C     . HIS B 1 51  ? 29.750  37.468 -30.360 1.00 29.66  ? 37   HIS B C     1 
ATOM   4401 O  O     . HIS B 1 51  ? 30.704  37.662 -31.120 1.00 30.71  ? 37   HIS B O     1 
ATOM   4402 C  CB    . HIS B 1 51  ? 27.800  36.253 -31.392 1.00 27.02  ? 37   HIS B CB    1 
ATOM   4403 C  CG    . HIS B 1 51  ? 27.211  34.920 -31.728 1.00 27.75  ? 37   HIS B CG    1 
ATOM   4404 N  ND1   . HIS B 1 51  ? 27.419  34.294 -32.937 1.00 27.21  ? 37   HIS B ND1   1 
ATOM   4405 C  CD2   . HIS B 1 51  ? 26.436  34.083 -30.998 1.00 27.76  ? 37   HIS B CD2   1 
ATOM   4406 C  CE1   . HIS B 1 51  ? 26.802  33.126 -32.937 1.00 29.17  ? 37   HIS B CE1   1 
ATOM   4407 N  NE2   . HIS B 1 51  ? 26.195  32.975 -31.773 1.00 28.13  ? 37   HIS B NE2   1 
ATOM   4408 N  N     . VAL B 1 52  ? 29.368  38.364 -29.444 1.00 26.62  ? 38   VAL B N     1 
ATOM   4409 C  CA    . VAL B 1 52  ? 30.124  39.594 -29.264 1.00 26.46  ? 38   VAL B CA    1 
ATOM   4410 C  C     . VAL B 1 52  ? 31.523  39.274 -28.756 1.00 29.46  ? 38   VAL B C     1 
ATOM   4411 O  O     . VAL B 1 52  ? 32.521  39.799 -29.265 1.00 27.92  ? 38   VAL B O     1 
ATOM   4412 C  CB    . VAL B 1 52  ? 29.397  40.548 -28.300 1.00 27.71  ? 38   VAL B CB    1 
ATOM   4413 C  CG1   . VAL B 1 52  ? 30.210  41.836 -28.118 1.00 26.54  ? 38   VAL B CG1   1 
ATOM   4414 C  CG2   . VAL B 1 52  ? 27.972  40.829 -28.760 1.00 24.16  ? 38   VAL B CG2   1 
ATOM   4415 N  N     . ILE B 1 53  ? 31.619  38.385 -27.759 1.00 29.44  ? 39   ILE B N     1 
ATOM   4416 C  CA    . ILE B 1 53  ? 32.928  38.036 -27.206 1.00 31.71  ? 39   ILE B CA    1 
ATOM   4417 C  C     . ILE B 1 53  ? 33.804  37.386 -28.273 1.00 33.12  ? 39   ILE B C     1 
ATOM   4418 O  O     . ILE B 1 53  ? 34.949  37.797 -28.492 1.00 34.12  ? 39   ILE B O     1 
ATOM   4419 C  CB    . ILE B 1 53  ? 32.774  37.125 -25.971 1.00 34.85  ? 39   ILE B CB    1 
ATOM   4420 C  CG1   . ILE B 1 53  ? 32.655  37.943 -24.686 1.00 35.11  ? 39   ILE B CG1   1 
ATOM   4421 C  CG2   . ILE B 1 53  ? 33.965  36.168 -25.838 1.00 37.59  ? 39   ILE B CG2   1 
ATOM   4422 C  CD1   . ILE B 1 53  ? 31.431  38.785 -24.582 1.00 33.28  ? 39   ILE B CD1   1 
ATOM   4423 N  N     . ASP B 1 54  ? 33.263  36.400 -28.992 1.00 31.95  ? 40   ASP B N     1 
ATOM   4424 C  CA    . ASP B 1 54  ? 34.091  35.659 -29.934 1.00 35.15  ? 40   ASP B CA    1 
ATOM   4425 C  C     . ASP B 1 54  ? 34.494  36.491 -31.139 1.00 34.13  ? 40   ASP B C     1 
ATOM   4426 O  O     . ASP B 1 54  ? 35.468  36.145 -31.811 1.00 34.46  ? 40   ASP B O     1 
ATOM   4427 C  CB    . ASP B 1 54  ? 33.372  34.394 -30.410 1.00 37.96  ? 40   ASP B CB    1 
ATOM   4428 C  CG    . ASP B 1 54  ? 33.329  33.308 -29.347 1.00 41.88  ? 40   ASP B CG    1 
ATOM   4429 O  OD1   . ASP B 1 54  ? 34.260  33.245 -28.515 1.00 51.44  ? 40   ASP B OD1   1 
ATOM   4430 O  OD2   . ASP B 1 54  ? 32.380  32.499 -29.363 1.00 41.48  ? 40   ASP B OD2   1 
ATOM   4431 N  N     . SER B 1 55  ? 33.753  37.541 -31.449 1.00 33.62  ? 41   SER B N     1 
ATOM   4432 C  CA    . SER B 1 55  ? 34.049  38.329 -32.639 1.00 35.03  ? 41   SER B CA    1 
ATOM   4433 C  C     . SER B 1 55  ? 35.377  39.066 -32.489 1.00 34.43  ? 41   SER B C     1 
ATOM   4434 O  O     . SER B 1 55  ? 35.617  39.698 -31.455 1.00 32.06  ? 41   SER B O     1 
ATOM   4435 C  CB    . SER B 1 55  ? 32.934  39.325 -32.913 1.00 32.25  ? 41   SER B CB    1 
ATOM   4436 O  OG    . SER B 1 55  ? 33.393  40.348 -33.775 1.00 33.68  ? 41   SER B OG    1 
ATOM   4437 N  N     . PRO B 1 56  ? 36.260  39.015 -33.492 1.00 36.38  ? 42   PRO B N     1 
ATOM   4438 C  CA    . PRO B 1 56  ? 37.466  39.852 -33.457 1.00 34.16  ? 42   PRO B CA    1 
ATOM   4439 C  C     . PRO B 1 56  ? 37.193  41.316 -33.770 1.00 33.57  ? 42   PRO B C     1 
ATOM   4440 O  O     . PRO B 1 56  ? 38.078  42.155 -33.557 1.00 33.77  ? 42   PRO B O     1 
ATOM   4441 C  CB    . PRO B 1 56  ? 38.362  39.236 -34.548 1.00 37.93  ? 42   PRO B CB    1 
ATOM   4442 C  CG    . PRO B 1 56  ? 37.607  38.072 -35.131 1.00 36.95  ? 42   PRO B CG    1 
ATOM   4443 C  CD    . PRO B 1 56  ? 36.173  38.202 -34.715 1.00 36.40  ? 42   PRO B CD    1 
ATOM   4444 N  N     . ASP B 1 57  ? 36.005  41.652 -34.266 1.00 32.70  ? 43   ASP B N     1 
ATOM   4445 C  CA    . ASP B 1 57  ? 35.730  42.990 -34.768 1.00 30.97  ? 43   ASP B CA    1 
ATOM   4446 C  C     . ASP B 1 57  ? 35.003  43.881 -33.771 1.00 30.83  ? 43   ASP B C     1 
ATOM   4447 O  O     . ASP B 1 57  ? 34.911  45.091 -34.001 1.00 27.78  ? 43   ASP B O     1 
ATOM   4448 C  CB    . ASP B 1 57  ? 34.890  42.912 -36.047 1.00 36.40  ? 43   ASP B CB    1 
ATOM   4449 C  CG    . ASP B 1 57  ? 35.537  42.067 -37.128 1.00 39.45  ? 43   ASP B CG    1 
ATOM   4450 O  OD1   . ASP B 1 57  ? 36.701  41.639 -36.966 1.00 38.13  ? 43   ASP B OD1   1 
ATOM   4451 O  OD2   . ASP B 1 57  ? 34.853  41.804 -38.135 1.00 43.40  ? 43   ASP B OD2   1 
ATOM   4452 N  N     . ILE B 1 58  ? 34.424  43.319 -32.717 1.00 29.18  ? 44   ILE B N     1 
ATOM   4453 C  CA    . ILE B 1 58  ? 33.643  44.095 -31.767 1.00 26.01  ? 44   ILE B CA    1 
ATOM   4454 C  C     . ILE B 1 58  ? 34.093  43.727 -30.360 1.00 26.39  ? 44   ILE B C     1 
ATOM   4455 O  O     . ILE B 1 58  ? 34.313  42.549 -30.056 1.00 27.98  ? 44   ILE B O     1 
ATOM   4456 C  CB    . ILE B 1 58  ? 32.129  43.867 -31.971 1.00 25.18  ? 44   ILE B CB    1 
ATOM   4457 C  CG1   . ILE B 1 58  ? 31.309  44.749 -31.041 1.00 25.75  ? 44   ILE B CG1   1 
ATOM   4458 C  CG2   . ILE B 1 58  ? 31.763  42.406 -31.783 1.00 28.81  ? 44   ILE B CG2   1 
ATOM   4459 C  CD1   . ILE B 1 58  ? 31.134  46.138 -31.569 1.00 24.77  ? 44   ILE B CD1   1 
ATOM   4460 N  N     . CYS B 1 59  ? 34.285  44.737 -29.517 1.00 25.62  ? 45   CYS B N     1 
ATOM   4461 C  CA    . CYS B 1 59  ? 34.745  44.535 -28.151 1.00 26.09  ? 45   CYS B CA    1 
ATOM   4462 C  C     . CYS B 1 59  ? 33.599  44.797 -27.177 1.00 22.85  ? 45   CYS B C     1 
ATOM   4463 O  O     . CYS B 1 59  ? 33.030  45.895 -27.164 1.00 22.42  ? 45   CYS B O     1 
ATOM   4464 C  CB    . CYS B 1 59  ? 35.938  45.443 -27.855 1.00 28.02  ? 45   CYS B CB    1 
ATOM   4465 S  SG    . CYS B 1 59  ? 36.482  45.449 -26.148 1.00 30.32  ? 45   CYS B SG    1 
ATOM   4466 N  N     . TRP B 1 60  ? 33.274  43.791 -26.368 1.00 25.03  ? 46   TRP B N     1 
ATOM   4467 C  CA    . TRP B 1 60  ? 32.288  43.945 -25.298 1.00 24.08  ? 46   TRP B CA    1 
ATOM   4468 C  C     . TRP B 1 60  ? 32.818  44.822 -24.166 1.00 24.45  ? 46   TRP B C     1 
ATOM   4469 O  O     . TRP B 1 60  ? 33.917  44.595 -23.643 1.00 24.01  ? 46   TRP B O     1 
ATOM   4470 C  CB    . TRP B 1 60  ? 31.907  42.577 -24.742 1.00 24.28  ? 46   TRP B CB    1 
ATOM   4471 C  CG    . TRP B 1 60  ? 31.029  42.647 -23.520 1.00 25.93  ? 46   TRP B CG    1 
ATOM   4472 C  CD1   . TRP B 1 60  ? 31.341  42.237 -22.259 1.00 27.23  ? 46   TRP B CD1   1 
ATOM   4473 C  CD2   . TRP B 1 60  ? 29.693  43.161 -23.456 1.00 24.22  ? 46   TRP B CD2   1 
ATOM   4474 N  NE1   . TRP B 1 60  ? 30.276  42.460 -21.409 1.00 27.90  ? 46   TRP B NE1   1 
ATOM   4475 C  CE2   . TRP B 1 60  ? 29.252  43.022 -22.123 1.00 24.88  ? 46   TRP B CE2   1 
ATOM   4476 C  CE3   . TRP B 1 60  ? 28.823  43.718 -24.399 1.00 21.61  ? 46   TRP B CE3   1 
ATOM   4477 C  CZ2   . TRP B 1 60  ? 27.977  43.431 -21.708 1.00 24.49  ? 46   TRP B CZ2   1 
ATOM   4478 C  CZ3   . TRP B 1 60  ? 27.559  44.115 -23.985 1.00 21.22  ? 46   TRP B CZ3   1 
ATOM   4479 C  CH2   . TRP B 1 60  ? 27.158  43.984 -22.651 1.00 21.23  ? 46   TRP B CH2   1 
ATOM   4480 N  N     . VAL B 1 61  ? 32.006  45.779 -23.732 1.00 20.02  ? 47   VAL B N     1 
ATOM   4481 C  CA    . VAL B 1 61  ? 32.352  46.653 -22.612 1.00 21.62  ? 47   VAL B CA    1 
ATOM   4482 C  C     . VAL B 1 61  ? 31.249  46.524 -21.568 1.00 20.28  ? 47   VAL B C     1 
ATOM   4483 O  O     . VAL B 1 61  ? 30.186  47.144 -21.692 1.00 19.22  ? 47   VAL B O     1 
ATOM   4484 C  CB    . VAL B 1 61  ? 32.536  48.108 -23.058 1.00 20.74  ? 47   VAL B CB    1 
ATOM   4485 C  CG1   . VAL B 1 61  ? 32.992  48.985 -21.890 1.00 20.09  ? 47   VAL B CG1   1 
ATOM   4486 C  CG2   . VAL B 1 61  ? 33.536  48.177 -24.222 1.00 19.42  ? 47   VAL B CG2   1 
ATOM   4487 N  N     . GLY B 1 62  ? 31.482  45.705 -20.545 1.00 19.21  ? 48   GLY B N     1 
ATOM   4488 C  CA    . GLY B 1 62  ? 30.506  45.578 -19.474 1.00 21.44  ? 48   GLY B CA    1 
ATOM   4489 C  C     . GLY B 1 62  ? 30.489  46.832 -18.628 1.00 20.28  ? 48   GLY B C     1 
ATOM   4490 O  O     . GLY B 1 62  ? 31.545  47.353 -18.250 1.00 20.30  ? 48   GLY B O     1 
ATOM   4491 N  N     . CYS B 1 63  ? 29.293  47.341 -18.351 1.00 16.80  ? 49   CYS B N     1 
ATOM   4492 C  CA    . CYS B 1 63  ? 29.117  48.556 -17.576 1.00 17.01  ? 49   CYS B CA    1 
ATOM   4493 C  C     . CYS B 1 63  ? 28.472  48.227 -16.235 1.00 18.16  ? 49   CYS B C     1 
ATOM   4494 O  O     . CYS B 1 63  ? 27.919  47.141 -16.031 1.00 16.70  ? 49   CYS B O     1 
ATOM   4495 C  CB    . CYS B 1 63  ? 28.285  49.579 -18.354 1.00 18.61  ? 49   CYS B CB    1 
ATOM   4496 S  SG    . CYS B 1 63  ? 29.118  50.163 -19.871 1.00 13.40  ? 49   CYS B SG    1 
ATOM   4497 N  N     . ALA B 1 64  ? 28.576  49.180 -15.308 1.00 19.05  ? 50   ALA B N     1 
ATOM   4498 C  CA    . ALA B 1 64  ? 28.112  48.951 -13.940 1.00 18.87  ? 50   ALA B CA    1 
ATOM   4499 C  C     . ALA B 1 64  ? 26.590  49.025 -13.790 1.00 18.91  ? 50   ALA B C     1 
ATOM   4500 O  O     . ALA B 1 64  ? 26.051  48.443 -12.843 1.00 21.33  ? 50   ALA B O     1 
ATOM   4501 C  CB    . ALA B 1 64  ? 28.779  49.947 -12.991 1.00 18.88  ? 50   ALA B CB    1 
ATOM   4502 N  N     . ASN B 1 65  ? 25.887  49.762 -14.647 1.00 16.48  ? 51   ASN B N     1 
ATOM   4503 C  CA    . ASN B 1 65  ? 24.436  49.605 -14.784 1.00 16.19  ? 51   ASN B CA    1 
ATOM   4504 C  C     . ASN B 1 65  ? 24.037  50.091 -16.173 1.00 16.27  ? 51   ASN B C     1 
ATOM   4505 O  O     . ASN B 1 65  ? 24.860  50.622 -16.915 1.00 15.92  ? 51   ASN B O     1 
ATOM   4506 C  CB    . ASN B 1 65  ? 23.645  50.323 -13.664 1.00 17.39  ? 51   ASN B CB    1 
ATOM   4507 C  CG    . ASN B 1 65  ? 23.817  51.834 -13.660 1.00 16.21  ? 51   ASN B CG    1 
ATOM   4508 O  OD1   . ASN B 1 65  ? 23.982  52.465 -14.701 1.00 17.36  ? 51   ASN B OD1   1 
ATOM   4509 N  ND2   . ASN B 1 65  ? 23.734  52.431 -12.464 1.00 16.65  ? 51   ASN B ND2   1 
ATOM   4510 N  N     . GLU B 1 66  ? 22.761  49.881 -16.530 1.00 15.28  ? 52   GLU B N     1 
ATOM   4511 C  CA    . GLU B 1 66  ? 22.336  50.139 -17.905 1.00 15.90  ? 52   GLU B CA    1 
ATOM   4512 C  C     . GLU B 1 66  ? 22.206  51.621 -18.217 1.00 16.22  ? 52   GLU B C     1 
ATOM   4513 O  O     . GLU B 1 66  ? 22.415  52.017 -19.368 1.00 16.59  ? 52   GLU B O     1 
ATOM   4514 C  CB    . GLU B 1 66  ? 21.006  49.438 -18.224 1.00 14.79  ? 52   GLU B CB    1 
ATOM   4515 C  CG    . GLU B 1 66  ? 21.090  47.921 -18.269 1.00 15.01  ? 52   GLU B CG    1 
ATOM   4516 C  CD    . GLU B 1 66  ? 20.930  47.252 -16.919 1.00 15.96  ? 52   GLU B CD    1 
ATOM   4517 O  OE1   . GLU B 1 66  ? 20.934  47.942 -15.876 1.00 15.27  ? 52   GLU B OE1   1 
ATOM   4518 O  OE2   . GLU B 1 66  ? 20.800  46.011 -16.906 1.00 13.73  ? 52   GLU B OE2   1 
ATOM   4519 N  N     . LEU B 1 67  ? 21.790  52.448 -17.252 1.00 15.59  ? 53   LEU B N     1 
ATOM   4520 C  CA    . LEU B 1 67  ? 21.740  53.884 -17.525 1.00 15.80  ? 53   LEU B CA    1 
ATOM   4521 C  C     . LEU B 1 67  ? 23.117  54.399 -17.909 1.00 16.35  ? 53   LEU B C     1 
ATOM   4522 O  O     . LEU B 1 67  ? 23.281  55.090 -18.922 1.00 16.71  ? 53   LEU B O     1 
ATOM   4523 C  CB    . LEU B 1 67  ? 21.207  54.660 -16.313 1.00 16.23  ? 53   LEU B CB    1 
ATOM   4524 C  CG    . LEU B 1 67  ? 21.074  56.173 -16.534 1.00 17.97  ? 53   LEU B CG    1 
ATOM   4525 C  CD1   . LEU B 1 67  ? 20.197  56.433 -17.764 1.00 16.22  ? 53   LEU B CD1   1 
ATOM   4526 C  CD2   . LEU B 1 67  ? 20.512  56.937 -15.303 1.00 15.42  ? 53   LEU B CD2   1 
ATOM   4527 N  N     . ASN B 1 68  ? 24.121  54.057 -17.102 1.00 17.16  ? 54   ASN B N     1 
ATOM   4528 C  CA    . ASN B 1 68  ? 25.486  54.464 -17.392 1.00 18.15  ? 54   ASN B CA    1 
ATOM   4529 C  C     . ASN B 1 68  ? 25.935  53.938 -18.744 1.00 16.74  ? 54   ASN B C     1 
ATOM   4530 O  O     . ASN B 1 68  ? 26.615  54.644 -19.495 1.00 17.38  ? 54   ASN B O     1 
ATOM   4531 C  CB    . ASN B 1 68  ? 26.419  53.951 -16.292 1.00 17.85  ? 54   ASN B CB    1 
ATOM   4532 C  CG    . ASN B 1 68  ? 26.128  54.573 -14.948 1.00 16.65  ? 54   ASN B CG    1 
ATOM   4533 O  OD1   . ASN B 1 68  ? 25.274  55.447 -14.839 1.00 19.21  ? 54   ASN B OD1   1 
ATOM   4534 N  ND2   . ASN B 1 68  ? 26.865  54.158 -13.922 1.00 19.02  ? 54   ASN B ND2   1 
ATOM   4535 N  N     . ALA B 1 69  ? 25.575  52.691 -19.065 1.00 16.80  ? 55   ALA B N     1 
ATOM   4536 C  CA    . ALA B 1 69  ? 25.963  52.116 -20.349 1.00 17.11  ? 55   ALA B CA    1 
ATOM   4537 C  C     . ALA B 1 69  ? 25.404  52.934 -21.500 1.00 17.48  ? 55   ALA B C     1 
ATOM   4538 O  O     . ALA B 1 69  ? 26.089  53.155 -22.507 1.00 16.71  ? 55   ALA B O     1 
ATOM   4539 C  CB    . ALA B 1 69  ? 25.492  50.660 -20.441 1.00 16.21  ? 55   ALA B CB    1 
ATOM   4540 N  N     . SER B 1 70  ? 24.154  53.395 -21.371 1.00 17.85  ? 56   SER B N     1 
ATOM   4541 C  CA    . SER B 1 70  ? 23.557  54.195 -22.432 1.00 16.17  ? 56   SER B CA    1 
ATOM   4542 C  C     . SER B 1 70  ? 24.207  55.574 -22.518 1.00 16.56  ? 56   SER B C     1 
ATOM   4543 O  O     . SER B 1 70  ? 24.397  56.105 -23.618 1.00 17.66  ? 56   SER B O     1 
ATOM   4544 C  CB    . SER B 1 70  ? 22.038  54.299 -22.224 1.00 17.17  ? 56   SER B CB    1 
ATOM   4545 O  OG    . SER B 1 70  ? 21.702  55.043 -21.062 1.00 16.82  ? 56   SER B OG    1 
ATOM   4546 N  N     . TYR B 1 71  ? 24.587  56.154 -21.375 1.00 17.17  ? 57   TYR B N     1 
ATOM   4547 C  CA    . TYR B 1 71  ? 25.376  57.383 -21.394 1.00 17.34  ? 57   TYR B CA    1 
ATOM   4548 C  C     . TYR B 1 71  ? 26.740  57.150 -22.052 1.00 16.60  ? 57   TYR B C     1 
ATOM   4549 O  O     . TYR B 1 71  ? 27.216  57.983 -22.841 1.00 15.64  ? 57   TYR B O     1 
ATOM   4550 C  CB    . TYR B 1 71  ? 25.581  57.888 -19.969 1.00 17.70  ? 57   TYR B CB    1 
ATOM   4551 C  CG    . TYR B 1 71  ? 24.396  58.498 -19.227 1.00 17.09  ? 57   TYR B CG    1 
ATOM   4552 C  CD1   . TYR B 1 71  ? 23.346  59.128 -19.895 1.00 17.54  ? 57   TYR B CD1   1 
ATOM   4553 C  CD2   . TYR B 1 71  ? 24.352  58.450 -17.833 1.00 17.67  ? 57   TYR B CD2   1 
ATOM   4554 C  CE1   . TYR B 1 71  ? 22.277  59.689 -19.183 1.00 16.63  ? 57   TYR B CE1   1 
ATOM   4555 C  CE2   . TYR B 1 71  ? 23.296  59.006 -17.112 1.00 15.54  ? 57   TYR B CE2   1 
ATOM   4556 C  CZ    . TYR B 1 71  ? 22.266  59.633 -17.788 1.00 16.71  ? 57   TYR B CZ    1 
ATOM   4557 O  OH    . TYR B 1 71  ? 21.232  60.204 -17.056 1.00 13.50  ? 57   TYR B OH    1 
ATOM   4558 N  N     . ALA B 1 72  ? 27.392  56.030 -21.709 1.00 16.42  ? 58   ALA B N     1 
ATOM   4559 C  CA    . ALA B 1 72  ? 28.716  55.713 -22.253 1.00 17.35  ? 58   ALA B CA    1 
ATOM   4560 C  C     . ALA B 1 72  ? 28.662  55.524 -23.759 1.00 17.28  ? 58   ALA B C     1 
ATOM   4561 O  O     . ALA B 1 72  ? 29.535  56.017 -24.488 1.00 16.84  ? 58   ALA B O     1 
ATOM   4562 C  CB    . ALA B 1 72  ? 29.273  54.452 -21.592 1.00 14.66  ? 58   ALA B CB    1 
ATOM   4563 N  N     . ALA B 1 73  ? 27.639  54.816 -24.248 1.00 16.48  ? 59   ALA B N     1 
ATOM   4564 C  CA    . ALA B 1 73  ? 27.502  54.645 -25.689 1.00 18.10  ? 59   ALA B CA    1 
ATOM   4565 C  C     . ALA B 1 73  ? 27.328  55.991 -26.374 1.00 16.31  ? 59   ALA B C     1 
ATOM   4566 O  O     . ALA B 1 73  ? 27.874  56.232 -27.456 1.00 18.62  ? 59   ALA B O     1 
ATOM   4567 C  CB    . ALA B 1 73  ? 26.327  53.724 -25.993 1.00 14.15  ? 59   ALA B CB    1 
ATOM   4568 N  N     . ASP B 1 74  ? 26.579  56.885 -25.744 1.00 17.70  ? 60   ASP B N     1 
ATOM   4569 C  CA    . ASP B 1 74  ? 26.367  58.219 -26.283 1.00 17.13  ? 60   ASP B CA    1 
ATOM   4570 C  C     . ASP B 1 74  ? 27.685  58.974 -26.435 1.00 17.52  ? 60   ASP B C     1 
ATOM   4571 O  O     . ASP B 1 74  ? 27.981  59.523 -27.506 1.00 16.68  ? 60   ASP B O     1 
ATOM   4572 C  CB    . ASP B 1 74  ? 25.402  58.960 -25.355 1.00 16.02  ? 60   ASP B CB    1 
ATOM   4573 C  CG    . ASP B 1 74  ? 25.003  60.323 -25.880 1.00 16.78  ? 60   ASP B CG    1 
ATOM   4574 O  OD1   . ASP B 1 74  ? 25.887  61.194 -26.056 1.00 17.01  ? 60   ASP B OD1   1 
ATOM   4575 O  OD2   . ASP B 1 74  ? 23.786  60.540 -26.065 1.00 18.45  ? 60   ASP B OD2   1 
ATOM   4576 N  N     . GLY B 1 75  ? 28.482  59.036 -25.362 1.00 17.34  ? 61   GLY B N     1 
ATOM   4577 C  CA    . GLY B 1 75  ? 29.796  59.656 -25.473 1.00 18.32  ? 61   GLY B CA    1 
ATOM   4578 C  C     . GLY B 1 75  ? 30.659  58.981 -26.525 1.00 18.74  ? 61   GLY B C     1 
ATOM   4579 O  O     . GLY B 1 75  ? 31.314  59.648 -27.331 1.00 17.95  ? 61   GLY B O     1 
ATOM   4580 N  N     . TYR B 1 76  ? 30.627  57.649 -26.570 1.00 16.44  ? 62   TYR B N     1 
ATOM   4581 C  CA    . TYR B 1 76  ? 31.361  56.932 -27.607 1.00 17.98  ? 62   TYR B CA    1 
ATOM   4582 C  C     . TYR B 1 76  ? 30.946  57.409 -29.000 1.00 19.12  ? 62   TYR B C     1 
ATOM   4583 O  O     . TYR B 1 76  ? 31.796  57.777 -29.819 1.00 20.73  ? 62   TYR B O     1 
ATOM   4584 C  CB    . TYR B 1 76  ? 31.102  55.438 -27.434 1.00 17.10  ? 62   TYR B CB    1 
ATOM   4585 C  CG    . TYR B 1 76  ? 31.857  54.516 -28.348 1.00 18.40  ? 62   TYR B CG    1 
ATOM   4586 C  CD1   . TYR B 1 76  ? 31.370  54.208 -29.616 1.00 18.44  ? 62   TYR B CD1   1 
ATOM   4587 C  CD2   . TYR B 1 76  ? 33.041  53.913 -27.929 1.00 19.31  ? 62   TYR B CD2   1 
ATOM   4588 C  CE1   . TYR B 1 76  ? 32.037  53.346 -30.437 1.00 18.66  ? 62   TYR B CE1   1 
ATOM   4589 C  CE2   . TYR B 1 76  ? 33.722  53.050 -28.752 1.00 19.41  ? 62   TYR B CE2   1 
ATOM   4590 C  CZ    . TYR B 1 76  ? 33.215  52.761 -29.997 1.00 20.86  ? 62   TYR B CZ    1 
ATOM   4591 O  OH    . TYR B 1 76  ? 33.894  51.895 -30.813 1.00 19.62  ? 62   TYR B OH    1 
ATOM   4592 N  N     . ALA B 1 77  ? 29.635  57.475 -29.255 1.00 17.48  ? 63   ALA B N     1 
ATOM   4593 C  CA    . ALA B 1 77  ? 29.136  57.882 -30.570 1.00 18.77  ? 63   ALA B CA    1 
ATOM   4594 C  C     . ALA B 1 77  ? 29.523  59.311 -30.903 1.00 20.12  ? 63   ALA B C     1 
ATOM   4595 O  O     . ALA B 1 77  ? 29.736  59.643 -32.079 1.00 19.18  ? 63   ALA B O     1 
ATOM   4596 C  CB    . ALA B 1 77  ? 27.618  57.725 -30.638 1.00 18.23  ? 63   ALA B CB    1 
ATOM   4597 N  N     . ARG B 1 78  ? 29.640  60.170 -29.889 1.00 17.12  ? 64   ARG B N     1 
ATOM   4598 C  CA    . ARG B 1 78  ? 30.122  61.519 -30.156 1.00 19.64  ? 64   ARG B CA    1 
ATOM   4599 C  C     . ARG B 1 78  ? 31.607  61.549 -30.510 1.00 20.63  ? 64   ARG B C     1 
ATOM   4600 O  O     . ARG B 1 78  ? 32.108  62.594 -30.951 1.00 19.90  ? 64   ARG B O     1 
ATOM   4601 C  CB    . ARG B 1 78  ? 29.826  62.404 -28.949 1.00 18.79  ? 64   ARG B CB    1 
ATOM   4602 C  CG    . ARG B 1 78  ? 28.330  62.567 -28.695 1.00 20.43  ? 64   ARG B CG    1 
ATOM   4603 C  CD    . ARG B 1 78  ? 28.127  63.579 -27.586 1.00 21.66  ? 64   ARG B CD    1 
ATOM   4604 N  NE    . ARG B 1 78  ? 26.740  63.721 -27.162 1.00 20.63  ? 64   ARG B NE    1 
ATOM   4605 C  CZ    . ARG B 1 78  ? 26.237  64.854 -26.690 1.00 21.23  ? 64   ARG B CZ    1 
ATOM   4606 N  NH1   . ARG B 1 78  ? 26.950  65.970 -26.676 1.00 18.92  ? 64   ARG B NH1   1 
ATOM   4607 N  NH2   . ARG B 1 78  ? 25.001  64.863 -26.197 1.00 17.69  ? 64   ARG B NH2   1 
ATOM   4608 N  N     . CYS B 1 79  ? 32.314  60.433 -30.344 1.00 18.83  ? 65   CYS B N     1 
ATOM   4609 C  CA    . CYS B 1 79  ? 33.707  60.320 -30.756 1.00 20.96  ? 65   CYS B CA    1 
ATOM   4610 C  C     . CYS B 1 79  ? 33.880  59.522 -32.038 1.00 22.16  ? 65   CYS B C     1 
ATOM   4611 O  O     . CYS B 1 79  ? 34.751  59.852 -32.847 1.00 24.10  ? 65   CYS B O     1 
ATOM   4612 C  CB    . CYS B 1 79  ? 34.532  59.676 -29.643 1.00 20.23  ? 65   CYS B CB    1 
ATOM   4613 S  SG    . CYS B 1 79  ? 34.563  60.706 -28.181 1.00 23.47  ? 65   CYS B SG    1 
ATOM   4614 N  N     . LYS B 1 80  ? 33.073  58.476 -32.245 1.00 20.64  ? 66   LYS B N     1 
ATOM   4615 C  CA    . LYS B 1 80  ? 33.245  57.583 -33.382 1.00 21.57  ? 66   LYS B CA    1 
ATOM   4616 C  C     . LYS B 1 80  ? 32.151  57.708 -34.432 1.00 23.44  ? 66   LYS B C     1 
ATOM   4617 O  O     . LYS B 1 80  ? 32.267  57.099 -35.502 1.00 24.43  ? 66   LYS B O     1 
ATOM   4618 C  CB    . LYS B 1 80  ? 33.331  56.126 -32.896 1.00 22.57  ? 66   LYS B CB    1 
ATOM   4619 C  CG    . LYS B 1 80  ? 34.543  55.903 -31.978 1.00 25.48  ? 66   LYS B CG    1 
ATOM   4620 C  CD    . LYS B 1 80  ? 35.146  54.517 -32.119 1.00 25.84  ? 66   LYS B CD    1 
ATOM   4621 C  CE    . LYS B 1 80  ? 35.907  54.394 -33.406 1.00 28.64  ? 66   LYS B CE    1 
ATOM   4622 N  NZ    . LYS B 1 80  ? 36.882  53.247 -33.431 1.00 32.16  ? 66   LYS B NZ    1 
ATOM   4623 N  N     . GLY B 1 81  ? 31.119  58.499 -34.173 1.00 21.36  ? 67   GLY B N     1 
ATOM   4624 C  CA    . GLY B 1 81  ? 30.024  58.668 -35.097 1.00 23.49  ? 67   GLY B CA    1 
ATOM   4625 C  C     . GLY B 1 81  ? 28.931  57.628 -34.998 1.00 22.56  ? 67   GLY B C     1 
ATOM   4626 O  O     . GLY B 1 81  ? 27.926  57.754 -35.701 1.00 24.39  ? 67   GLY B O     1 
ATOM   4627 N  N     . PHE B 1 82  ? 29.082  56.612 -34.147 1.00 20.81  ? 68   PHE B N     1 
ATOM   4628 C  CA    . PHE B 1 82  ? 28.081  55.555 -34.016 1.00 21.04  ? 68   PHE B CA    1 
ATOM   4629 C  C     . PHE B 1 82  ? 28.403  54.752 -32.765 1.00 17.98  ? 68   PHE B C     1 
ATOM   4630 O  O     . PHE B 1 82  ? 29.568  54.653 -32.385 1.00 20.40  ? 68   PHE B O     1 
ATOM   4631 C  CB    . PHE B 1 82  ? 28.082  54.642 -35.253 1.00 21.72  ? 68   PHE B CB    1 
ATOM   4632 C  CG    . PHE B 1 82  ? 26.740  54.060 -35.585 1.00 21.80  ? 68   PHE B CG    1 
ATOM   4633 C  CD1   . PHE B 1 82  ? 25.859  54.752 -36.404 1.00 22.84  ? 68   PHE B CD1   1 
ATOM   4634 C  CD2   . PHE B 1 82  ? 26.377  52.809 -35.124 1.00 21.51  ? 68   PHE B CD2   1 
ATOM   4635 C  CE1   . PHE B 1 82  ? 24.617  54.214 -36.733 1.00 23.97  ? 68   PHE B CE1   1 
ATOM   4636 C  CE2   . PHE B 1 82  ? 25.145  52.262 -35.444 1.00 21.21  ? 68   PHE B CE2   1 
ATOM   4637 C  CZ    . PHE B 1 82  ? 24.262  52.958 -36.240 1.00 23.83  ? 68   PHE B CZ    1 
ATOM   4638 N  N     . ALA B 1 83  ? 27.380  54.144 -32.157 1.00 18.39  ? 69   ALA B N     1 
ATOM   4639 C  CA    . ALA B 1 83  ? 27.593  53.332 -30.963 1.00 17.57  ? 69   ALA B CA    1 
ATOM   4640 C  C     . ALA B 1 83  ? 26.455  52.333 -30.795 1.00 19.11  ? 69   ALA B C     1 
ATOM   4641 O  O     . ALA B 1 83  ? 25.405  52.430 -31.434 1.00 18.58  ? 69   ALA B O     1 
ATOM   4642 C  CB    . ALA B 1 83  ? 27.704  54.192 -29.704 1.00 17.34  ? 69   ALA B CB    1 
ATOM   4643 N  N     . ALA B 1 84  ? 26.674  51.372 -29.905 1.00 15.36  ? 70   ALA B N     1 
ATOM   4644 C  CA    . ALA B 1 84  ? 25.676  50.349 -29.674 1.00 17.81  ? 70   ALA B CA    1 
ATOM   4645 C  C     . ALA B 1 84  ? 25.611  50.008 -28.195 1.00 18.42  ? 70   ALA B C     1 
ATOM   4646 O  O     . ALA B 1 84  ? 26.641  49.947 -27.505 1.00 17.67  ? 70   ALA B O     1 
ATOM   4647 C  CB    . ALA B 1 84  ? 25.972  49.101 -30.497 1.00 17.42  ? 70   ALA B CB    1 
ATOM   4648 N  N     . LEU B 1 85  ? 24.390  49.779 -27.733 1.00 17.08  ? 71   LEU B N     1 
ATOM   4649 C  CA    . LEU B 1 85  ? 24.075  49.422 -26.364 1.00 16.23  ? 71   LEU B CA    1 
ATOM   4650 C  C     . LEU B 1 85  ? 23.330  48.092 -26.375 1.00 17.50  ? 71   LEU B C     1 
ATOM   4651 O  O     . LEU B 1 85  ? 22.427  47.897 -27.184 1.00 16.61  ? 71   LEU B O     1 
ATOM   4652 C  CB    . LEU B 1 85  ? 23.197  50.516 -25.723 1.00 17.57  ? 71   LEU B CB    1 
ATOM   4653 C  CG    . LEU B 1 85  ? 22.435  50.181 -24.435 1.00 16.16  ? 71   LEU B CG    1 
ATOM   4654 C  CD1   . LEU B 1 85  ? 23.352  50.284 -23.246 1.00 16.43  ? 71   LEU B CD1   1 
ATOM   4655 C  CD2   . LEU B 1 85  ? 21.253  51.123 -24.267 1.00 16.34  ? 71   LEU B CD2   1 
ATOM   4656 N  N     . LEU B 1 86  ? 23.694  47.177 -25.475 1.00 18.29  ? 72   LEU B N     1 
ATOM   4657 C  CA    . LEU B 1 86  ? 22.969  45.921 -25.308 1.00 17.71  ? 72   LEU B CA    1 
ATOM   4658 C  C     . LEU B 1 86  ? 22.410  45.828 -23.892 1.00 17.28  ? 72   LEU B C     1 
ATOM   4659 O  O     . LEU B 1 86  ? 23.152  45.947 -22.911 1.00 17.44  ? 72   LEU B O     1 
ATOM   4660 C  CB    . LEU B 1 86  ? 23.866  44.707 -25.610 1.00 17.99  ? 72   LEU B CB    1 
ATOM   4661 C  CG    . LEU B 1 86  ? 23.268  43.355 -25.195 1.00 18.82  ? 72   LEU B CG    1 
ATOM   4662 C  CD1   . LEU B 1 86  ? 22.160  42.932 -26.178 1.00 17.92  ? 72   LEU B CD1   1 
ATOM   4663 C  CD2   . LEU B 1 86  ? 24.341  42.264 -25.114 1.00 19.90  ? 72   LEU B CD2   1 
ATOM   4664 N  N     . THR B 1 87  ? 21.107  45.615 -23.783 1.00 15.81  ? 73   THR B N     1 
ATOM   4665 C  CA    . THR B 1 87  ? 20.462  45.415 -22.495 1.00 15.89  ? 73   THR B CA    1 
ATOM   4666 C  C     . THR B 1 87  ? 19.636  44.145 -22.569 1.00 16.91  ? 73   THR B C     1 
ATOM   4667 O  O     . THR B 1 87  ? 19.462  43.558 -23.640 1.00 16.87  ? 73   THR B O     1 
ATOM   4668 C  CB    . THR B 1 87  ? 19.572  46.603 -22.109 1.00 16.04  ? 73   THR B CB    1 
ATOM   4669 O  OG1   . THR B 1 87  ? 18.458  46.680 -23.010 1.00 15.68  ? 73   THR B OG1   1 
ATOM   4670 C  CG2   . THR B 1 87  ? 20.373  47.906 -22.188 1.00 15.19  ? 73   THR B CG2   1 
ATOM   4671 N  N     . THR B 1 88  ? 19.128  43.716 -21.416 1.00 16.13  ? 74   THR B N     1 
ATOM   4672 C  CA    . THR B 1 88  ? 18.195  42.602 -21.374 1.00 15.89  ? 74   THR B CA    1 
ATOM   4673 C  C     . THR B 1 88  ? 16.758  43.118 -21.309 1.00 17.28  ? 74   THR B C     1 
ATOM   4674 O  O     . THR B 1 88  ? 16.490  44.237 -20.849 1.00 17.34  ? 74   THR B O     1 
ATOM   4675 C  CB    . THR B 1 88  ? 18.502  41.682 -20.188 1.00 17.95  ? 74   THR B CB    1 
ATOM   4676 O  OG1   . THR B 1 88  ? 17.824  40.433 -20.360 1.00 19.71  ? 74   THR B OG1   1 
ATOM   4677 C  CG2   . THR B 1 88  ? 18.031  42.307 -18.884 1.00 15.97  ? 74   THR B CG2   1 
ATOM   4678 N  N     . PHE B 1 89  ? 15.836  42.274 -21.785 1.00 17.58  ? 75   PHE B N     1 
ATOM   4679 C  CA    . PHE B 1 89  ? 14.406  42.586 -21.862 1.00 17.34  ? 75   PHE B CA    1 
ATOM   4680 C  C     . PHE B 1 89  ? 13.878  43.174 -20.555 1.00 15.07  ? 75   PHE B C     1 
ATOM   4681 O  O     . PHE B 1 89  ? 14.151  42.657 -19.474 1.00 15.20  ? 75   PHE B O     1 
ATOM   4682 C  CB    . PHE B 1 89  ? 13.642  41.301 -22.194 1.00 17.77  ? 75   PHE B CB    1 
ATOM   4683 C  CG    . PHE B 1 89  ? 12.173  41.500 -22.492 1.00 17.14  ? 75   PHE B CG    1 
ATOM   4684 C  CD1   . PHE B 1 89  ? 11.750  41.842 -23.771 1.00 17.30  ? 75   PHE B CD1   1 
ATOM   4685 C  CD2   . PHE B 1 89  ? 11.219  41.309 -21.501 1.00 16.34  ? 75   PHE B CD2   1 
ATOM   4686 C  CE1   . PHE B 1 89  ? 10.390  41.998 -24.070 1.00 17.54  ? 75   PHE B CE1   1 
ATOM   4687 C  CE2   . PHE B 1 89  ? 9.851   41.472 -21.776 1.00 18.54  ? 75   PHE B CE2   1 
ATOM   4688 C  CZ    . PHE B 1 89  ? 9.436   41.829 -23.066 1.00 16.74  ? 75   PHE B CZ    1 
ATOM   4689 N  N     . GLY B 1 90  ? 13.155  44.285 -20.664 1.00 16.66  ? 76   GLY B N     1 
ATOM   4690 C  CA    . GLY B 1 90  ? 12.438  44.866 -19.536 1.00 15.12  ? 76   GLY B CA    1 
ATOM   4691 C  C     . GLY B 1 90  ? 13.306  45.630 -18.551 1.00 14.60  ? 76   GLY B C     1 
ATOM   4692 O  O     . GLY B 1 90  ? 13.418  46.856 -18.639 1.00 15.54  ? 76   GLY B O     1 
ATOM   4693 N  N     . VAL B 1 91  ? 13.977  44.912 -17.641 1.00 15.03  ? 77   VAL B N     1 
ATOM   4694 C  CA    . VAL B 1 91  ? 14.733  45.581 -16.583 1.00 15.97  ? 77   VAL B CA    1 
ATOM   4695 C  C     . VAL B 1 91  ? 15.929  46.326 -17.162 1.00 16.60  ? 77   VAL B C     1 
ATOM   4696 O  O     . VAL B 1 91  ? 16.259  47.435 -16.719 1.00 15.53  ? 77   VAL B O     1 
ATOM   4697 C  CB    . VAL B 1 91  ? 15.164  44.574 -15.499 1.00 15.84  ? 77   VAL B CB    1 
ATOM   4698 C  CG1   . VAL B 1 91  ? 13.931  43.980 -14.817 1.00 15.62  ? 77   VAL B CG1   1 
ATOM   4699 C  CG2   . VAL B 1 91  ? 16.058  43.471 -16.075 1.00 15.07  ? 77   VAL B CG2   1 
ATOM   4700 N  N     . GLY B 1 92  ? 16.574  45.749 -18.178 1.00 15.77  ? 78   GLY B N     1 
ATOM   4701 C  CA    . GLY B 1 92  ? 17.746  46.365 -18.772 1.00 15.87  ? 78   GLY B CA    1 
ATOM   4702 C  C     . GLY B 1 92  ? 17.372  47.544 -19.645 1.00 14.37  ? 78   GLY B C     1 
ATOM   4703 O  O     . GLY B 1 92  ? 17.853  48.667 -19.423 1.00 14.30  ? 78   GLY B O     1 
ATOM   4704 N  N     . GLU B 1 93  ? 16.482  47.294 -20.619 1.00 14.69  ? 79   GLU B N     1 
ATOM   4705 C  CA    . GLU B 1 93  ? 16.117  48.317 -21.597 1.00 13.91  ? 79   GLU B CA    1 
ATOM   4706 C  C     . GLU B 1 93  ? 15.423  49.502 -20.943 1.00 15.60  ? 79   GLU B C     1 
ATOM   4707 O  O     . GLU B 1 93  ? 15.643  50.653 -21.342 1.00 15.91  ? 79   GLU B O     1 
ATOM   4708 C  CB    . GLU B 1 93  ? 15.232  47.712 -22.698 1.00 15.54  ? 79   GLU B CB    1 
ATOM   4709 C  CG    . GLU B 1 93  ? 13.824  47.330 -22.276 1.00 15.31  ? 79   GLU B CG    1 
ATOM   4710 C  CD    . GLU B 1 93  ? 13.056  46.713 -23.424 1.00 16.70  ? 79   GLU B CD    1 
ATOM   4711 O  OE1   . GLU B 1 93  ? 12.864  47.417 -24.457 1.00 16.08  ? 79   GLU B OE1   1 
ATOM   4712 O  OE2   . GLU B 1 93  ? 12.687  45.520 -23.305 1.00 15.19  ? 79   GLU B OE2   1 
ATOM   4713 N  N     . LEU B 1 94  ? 14.584  49.254 -19.928 1.00 16.17  ? 80   LEU B N     1 
ATOM   4714 C  CA    . LEU B 1 94  ? 13.920  50.383 -19.289 1.00 14.37  ? 80   LEU B CA    1 
ATOM   4715 C  C     . LEU B 1 94  ? 14.881  51.161 -18.413 1.00 15.25  ? 80   LEU B C     1 
ATOM   4716 O  O     . LEU B 1 94  ? 14.703  52.369 -18.219 1.00 14.87  ? 80   LEU B O     1 
ATOM   4717 C  CB    . LEU B 1 94  ? 12.713  49.911 -18.469 1.00 14.60  ? 80   LEU B CB    1 
ATOM   4718 C  CG    . LEU B 1 94  ? 11.509  49.412 -19.286 1.00 16.80  ? 80   LEU B CG    1 
ATOM   4719 C  CD1   . LEU B 1 94  ? 10.284  49.258 -18.376 1.00 14.79  ? 80   LEU B CD1   1 
ATOM   4720 C  CD2   . LEU B 1 94  ? 11.176  50.354 -20.453 1.00 16.93  ? 80   LEU B CD2   1 
ATOM   4721 N  N     . SER B 1 95  ? 15.906  50.497 -17.872 1.00 15.28  ? 81   SER B N     1 
ATOM   4722 C  CA    . SER B 1 95  ? 16.911  51.241 -17.119 1.00 15.11  ? 81   SER B CA    1 
ATOM   4723 C  C     . SER B 1 95  ? 17.667  52.224 -18.012 1.00 15.57  ? 81   SER B C     1 
ATOM   4724 O  O     . SER B 1 95  ? 18.164  53.246 -17.526 1.00 14.36  ? 81   SER B O     1 
ATOM   4725 C  CB    . SER B 1 95  ? 17.880  50.277 -16.434 1.00 14.33  ? 81   SER B CB    1 
ATOM   4726 O  OG    . SER B 1 95  ? 17.302  49.692 -15.275 1.00 13.91  ? 81   SER B OG    1 
ATOM   4727 N  N     . ALA B 1 96  ? 17.755  51.942 -19.314 1.00 15.95  ? 82   ALA B N     1 
ATOM   4728 C  CA    . ALA B 1 96  ? 18.522  52.756 -20.254 1.00 15.48  ? 82   ALA B CA    1 
ATOM   4729 C  C     . ALA B 1 96  ? 17.686  53.805 -20.981 1.00 15.05  ? 82   ALA B C     1 
ATOM   4730 O  O     . ALA B 1 96  ? 18.235  54.580 -21.770 1.00 14.77  ? 82   ALA B O     1 
ATOM   4731 C  CB    . ALA B 1 96  ? 19.203  51.855 -21.282 1.00 16.20  ? 82   ALA B CB    1 
ATOM   4732 N  N     . MET B 1 97  ? 16.390  53.886 -20.696 1.00 16.42  ? 83   MET B N     1 
ATOM   4733 C  CA    . MET B 1 97  ? 15.495  54.702 -21.506 1.00 16.70  ? 83   MET B CA    1 
ATOM   4734 C  C     . MET B 1 97  ? 15.889  56.173 -21.485 1.00 17.66  ? 83   MET B C     1 
ATOM   4735 O  O     . MET B 1 97  ? 15.821  56.850 -22.516 1.00 17.80  ? 83   MET B O     1 
ATOM   4736 C  CB    . MET B 1 97  ? 14.062  54.496 -21.020 1.00 17.31  ? 83   MET B CB    1 
ATOM   4737 C  CG    . MET B 1 97  ? 13.120  55.561 -21.434 1.00 24.31  ? 83   MET B CG    1 
ATOM   4738 S  SD    . MET B 1 97  ? 11.492  54.834 -21.621 1.00 36.53  ? 83   MET B SD    1 
ATOM   4739 C  CE    . MET B 1 97  ? 11.802  53.489 -22.785 1.00 23.43  ? 83   MET B CE    1 
ATOM   4740 N  N     . ASN B 1 98  ? 16.299  56.693 -20.324 1.00 14.78  ? 84   ASN B N     1 
ATOM   4741 C  CA    . ASN B 1 98  ? 16.732  58.091 -20.268 1.00 16.13  ? 84   ASN B CA    1 
ATOM   4742 C  C     . ASN B 1 98  ? 17.978  58.332 -21.116 1.00 15.07  ? 84   ASN B C     1 
ATOM   4743 O  O     . ASN B 1 98  ? 18.154  59.423 -21.671 1.00 15.65  ? 84   ASN B O     1 
ATOM   4744 C  CB    . ASN B 1 98  ? 16.984  58.507 -18.813 1.00 15.95  ? 84   ASN B CB    1 
ATOM   4745 C  CG    . ASN B 1 98  ? 17.243  59.998 -18.663 1.00 18.30  ? 84   ASN B CG    1 
ATOM   4746 O  OD1   . ASN B 1 98  ? 16.450  60.839 -19.113 1.00 18.01  ? 84   ASN B OD1   1 
ATOM   4747 N  ND2   . ASN B 1 98  ? 18.362  60.336 -18.021 1.00 14.93  ? 84   ASN B ND2   1 
ATOM   4748 N  N     . GLY B 1 99  ? 18.872  57.349 -21.203 1.00 15.10  ? 85   GLY B N     1 
ATOM   4749 C  CA    . GLY B 1 99  ? 20.023  57.509 -22.080 1.00 15.81  ? 85   GLY B CA    1 
ATOM   4750 C  C     . GLY B 1 99  ? 19.626  57.634 -23.540 1.00 16.95  ? 85   GLY B C     1 
ATOM   4751 O  O     . GLY B 1 99  ? 20.047  58.560 -24.238 1.00 17.11  ? 85   GLY B O     1 
ATOM   4752 N  N     . ILE B 1 100 ? 18.789  56.712 -24.013 1.00 17.21  ? 86   ILE B N     1 
ATOM   4753 C  CA    . ILE B 1 100 ? 18.388  56.718 -25.413 1.00 15.70  ? 86   ILE B CA    1 
ATOM   4754 C  C     . ILE B 1 100 ? 17.608  57.981 -25.734 1.00 16.85  ? 86   ILE B C     1 
ATOM   4755 O  O     . ILE B 1 100 ? 17.796  58.589 -26.793 1.00 16.22  ? 86   ILE B O     1 
ATOM   4756 C  CB    . ILE B 1 100 ? 17.574  55.453 -25.730 1.00 14.46  ? 86   ILE B CB    1 
ATOM   4757 C  CG1   . ILE B 1 100 ? 18.479  54.214 -25.657 1.00 14.59  ? 86   ILE B CG1   1 
ATOM   4758 C  CG2   . ILE B 1 100 ? 16.908  55.585 -27.117 1.00 18.25  ? 86   ILE B CG2   1 
ATOM   4759 C  CD1   . ILE B 1 100 ? 19.649  54.238 -26.638 1.00 15.74  ? 86   ILE B CD1   1 
ATOM   4760 N  N     . ALA B 1 101 ? 16.736  58.412 -24.813 1.00 16.66  ? 87   ALA B N     1 
ATOM   4761 C  CA    . ALA B 1 101 ? 15.999  59.652 -25.016 1.00 16.71  ? 87   ALA B CA    1 
ATOM   4762 C  C     . ALA B 1 101 ? 16.941  60.831 -25.188 1.00 17.51  ? 87   ALA B C     1 
ATOM   4763 O  O     . ALA B 1 101 ? 16.738  61.670 -26.071 1.00 15.79  ? 87   ALA B O     1 
ATOM   4764 C  CB    . ALA B 1 101 ? 15.058  59.909 -23.840 1.00 17.38  ? 87   ALA B CB    1 
ATOM   4765 N  N     . GLY B 1 102 ? 17.985  60.917 -24.359 1.00 17.44  ? 88   GLY B N     1 
ATOM   4766 C  CA    . GLY B 1 102 ? 18.933  62.005 -24.529 1.00 16.80  ? 88   GLY B CA    1 
ATOM   4767 C  C     . GLY B 1 102 ? 19.692  61.922 -25.838 1.00 16.82  ? 88   GLY B C     1 
ATOM   4768 O  O     . GLY B 1 102 ? 20.060  62.952 -26.420 1.00 17.64  ? 88   GLY B O     1 
ATOM   4769 N  N     . SER B 1 103 ? 19.971  60.707 -26.303 1.00 16.60  ? 89   SER B N     1 
ATOM   4770 C  CA    . SER B 1 103 ? 20.595  60.555 -27.609 1.00 17.54  ? 89   SER B CA    1 
ATOM   4771 C  C     . SER B 1 103 ? 19.658  61.024 -28.707 1.00 17.72  ? 89   SER B C     1 
ATOM   4772 O  O     . SER B 1 103 ? 20.089  61.683 -29.661 1.00 17.18  ? 89   SER B O     1 
ATOM   4773 C  CB    . SER B 1 103 ? 21.015  59.096 -27.817 1.00 17.25  ? 89   SER B CB    1 
ATOM   4774 O  OG    . SER B 1 103 ? 21.937  58.710 -26.800 1.00 17.21  ? 89   SER B OG    1 
ATOM   4775 N  N     . TYR B 1 104 ? 18.364  60.715 -28.577 1.00 17.89  ? 90   TYR B N     1 
ATOM   4776 C  CA    . TYR B 1 104 ? 17.392  61.197 -29.552 1.00 17.03  ? 90   TYR B CA    1 
ATOM   4777 C  C     . TYR B 1 104 ? 17.304  62.722 -29.524 1.00 17.47  ? 90   TYR B C     1 
ATOM   4778 O  O     . TYR B 1 104 ? 17.356  63.378 -30.569 1.00 17.19  ? 90   TYR B O     1 
ATOM   4779 C  CB    . TYR B 1 104 ? 16.025  60.556 -29.294 1.00 17.12  ? 90   TYR B CB    1 
ATOM   4780 C  CG    . TYR B 1 104 ? 15.006  60.877 -30.364 1.00 17.84  ? 90   TYR B CG    1 
ATOM   4781 C  CD1   . TYR B 1 104 ? 14.235  62.022 -30.277 1.00 18.96  ? 90   TYR B CD1   1 
ATOM   4782 C  CD2   . TYR B 1 104 ? 14.810  60.034 -31.455 1.00 19.29  ? 90   TYR B CD2   1 
ATOM   4783 C  CE1   . TYR B 1 104 ? 13.311  62.333 -31.237 1.00 18.49  ? 90   TYR B CE1   1 
ATOM   4784 C  CE2   . TYR B 1 104 ? 13.886  60.345 -32.436 1.00 19.00  ? 90   TYR B CE2   1 
ATOM   4785 C  CZ    . TYR B 1 104 ? 13.137  61.501 -32.313 1.00 20.71  ? 90   TYR B CZ    1 
ATOM   4786 O  OH    . TYR B 1 104 ? 12.191  61.845 -33.247 1.00 22.58  ? 90   TYR B OH    1 
ATOM   4787 N  N     . ALA B 1 105 ? 17.233  63.304 -28.327 1.00 18.40  ? 91   ALA B N     1 
ATOM   4788 C  CA    . ALA B 1 105 ? 17.118  64.756 -28.203 1.00 18.55  ? 91   ALA B CA    1 
ATOM   4789 C  C     . ALA B 1 105 ? 18.296  65.474 -28.855 1.00 17.88  ? 91   ALA B C     1 
ATOM   4790 O  O     . ALA B 1 105 ? 18.128  66.530 -29.481 1.00 20.71  ? 91   ALA B O     1 
ATOM   4791 C  CB    . ALA B 1 105 ? 17.019  65.135 -26.722 1.00 17.24  ? 91   ALA B CB    1 
ATOM   4792 N  N     . GLU B 1 106 ? 19.497  64.930 -28.709 1.00 18.34  ? 92   GLU B N     1 
ATOM   4793 C  CA    . GLU B 1 106 ? 20.705  65.595 -29.172 1.00 19.40  ? 92   GLU B CA    1 
ATOM   4794 C  C     . GLU B 1 106 ? 21.293  64.949 -30.419 1.00 17.96  ? 92   GLU B C     1 
ATOM   4795 O  O     . GLU B 1 106 ? 22.453  65.212 -30.755 1.00 18.43  ? 92   GLU B O     1 
ATOM   4796 C  CB    . GLU B 1 106 ? 21.735  65.650 -28.038 1.00 17.94  ? 92   GLU B CB    1 
ATOM   4797 C  CG    . GLU B 1 106 ? 21.185  66.167 -26.726 1.00 18.74  ? 92   GLU B CG    1 
ATOM   4798 C  CD    . GLU B 1 106 ? 22.129  67.147 -26.017 1.00 21.60  ? 92   GLU B CD    1 
ATOM   4799 O  OE1   . GLU B 1 106 ? 23.359  67.093 -26.260 1.00 20.31  ? 92   GLU B OE1   1 
ATOM   4800 O  OE2   . GLU B 1 106 ? 21.645  67.950 -25.192 1.00 20.51  ? 92   GLU B OE2   1 
ATOM   4801 N  N     . HIS B 1 107 ? 20.532  64.086 -31.089 1.00 17.17  ? 93   HIS B N     1 
ATOM   4802 C  CA    . HIS B 1 107 ? 20.897  63.536 -32.393 1.00 18.56  ? 93   HIS B CA    1 
ATOM   4803 C  C     . HIS B 1 107 ? 22.216  62.754 -32.328 1.00 19.23  ? 93   HIS B C     1 
ATOM   4804 O  O     . HIS B 1 107 ? 23.162  63.001 -33.085 1.00 17.84  ? 93   HIS B O     1 
ATOM   4805 C  CB    . HIS B 1 107 ? 20.967  64.652 -33.444 1.00 17.82  ? 93   HIS B CB    1 
ATOM   4806 C  CG    . HIS B 1 107 ? 19.643  65.278 -33.753 1.00 20.46  ? 93   HIS B CG    1 
ATOM   4807 N  ND1   . HIS B 1 107 ? 19.024  65.151 -34.980 1.00 18.54  ? 93   HIS B ND1   1 
ATOM   4808 C  CD2   . HIS B 1 107 ? 18.815  66.033 -32.989 1.00 19.91  ? 93   HIS B CD2   1 
ATOM   4809 C  CE1   . HIS B 1 107 ? 17.884  65.822 -34.964 1.00 21.26  ? 93   HIS B CE1   1 
ATOM   4810 N  NE2   . HIS B 1 107 ? 17.732  66.365 -33.767 1.00 20.10  ? 93   HIS B NE2   1 
ATOM   4811 N  N     . VAL B 1 108 ? 22.241  61.768 -31.443 1.00 18.85  ? 94   VAL B N     1 
ATOM   4812 C  CA    . VAL B 1 108 ? 23.383  60.880 -31.259 1.00 16.29  ? 94   VAL B CA    1 
ATOM   4813 C  C     . VAL B 1 108 ? 22.964  59.487 -31.716 1.00 17.25  ? 94   VAL B C     1 
ATOM   4814 O  O     . VAL B 1 108 ? 22.034  58.904 -31.138 1.00 16.47  ? 94   VAL B O     1 
ATOM   4815 C  CB    . VAL B 1 108 ? 23.867  60.864 -29.801 1.00 16.58  ? 94   VAL B CB    1 
ATOM   4816 C  CG1   . VAL B 1 108 ? 25.078  59.987 -29.680 1.00 16.30  ? 94   VAL B CG1   1 
ATOM   4817 C  CG2   . VAL B 1 108 ? 24.217  62.272 -29.348 1.00 16.18  ? 94   VAL B CG2   1 
ATOM   4818 N  N     . PRO B 1 109 ? 23.618  58.914 -32.720 1.00 16.27  ? 95   PRO B N     1 
ATOM   4819 C  CA    . PRO B 1 109 ? 23.179  57.616 -33.246 1.00 18.44  ? 95   PRO B CA    1 
ATOM   4820 C  C     . PRO B 1 109 ? 23.651  56.445 -32.396 1.00 18.30  ? 95   PRO B C     1 
ATOM   4821 O  O     . PRO B 1 109 ? 24.728  55.884 -32.632 1.00 18.73  ? 95   PRO B O     1 
ATOM   4822 C  CB    . PRO B 1 109 ? 23.790  57.589 -34.657 1.00 20.37  ? 95   PRO B CB    1 
ATOM   4823 C  CG    . PRO B 1 109 ? 25.024  58.400 -34.532 1.00 19.36  ? 95   PRO B CG    1 
ATOM   4824 C  CD    . PRO B 1 109 ? 24.711  59.494 -33.524 1.00 18.30  ? 95   PRO B CD    1 
ATOM   4825 N  N     . VAL B 1 110 ? 22.856  56.089 -31.387 1.00 17.91  ? 96   VAL B N     1 
ATOM   4826 C  CA    . VAL B 1 110 ? 23.095  54.929 -30.536 1.00 17.75  ? 96   VAL B CA    1 
ATOM   4827 C  C     . VAL B 1 110 ? 22.097  53.836 -30.894 1.00 17.17  ? 96   VAL B C     1 
ATOM   4828 O  O     . VAL B 1 110 ? 20.885  54.079 -30.943 1.00 18.78  ? 96   VAL B O     1 
ATOM   4829 C  CB    . VAL B 1 110 ? 22.978  55.291 -29.042 1.00 17.93  ? 96   VAL B CB    1 
ATOM   4830 C  CG1   . VAL B 1 110 ? 22.996  54.015 -28.208 1.00 14.23  ? 96   VAL B CG1   1 
ATOM   4831 C  CG2   . VAL B 1 110 ? 24.135  56.217 -28.634 1.00 16.45  ? 96   VAL B CG2   1 
ATOM   4832 N  N     . LEU B 1 111 ? 22.596  52.631 -31.134 1.00 17.57  ? 97   LEU B N     1 
ATOM   4833 C  CA    . LEU B 1 111 ? 21.732  51.493 -31.420 1.00 17.64  ? 97   LEU B CA    1 
ATOM   4834 C  C     . LEU B 1 111 ? 21.473  50.738 -30.127 1.00 17.41  ? 97   LEU B C     1 
ATOM   4835 O  O     . LEU B 1 111 ? 22.421  50.288 -29.470 1.00 17.45  ? 97   LEU B O     1 
ATOM   4836 C  CB    . LEU B 1 111 ? 22.372  50.570 -32.452 1.00 14.96  ? 97   LEU B CB    1 
ATOM   4837 C  CG    . LEU B 1 111 ? 21.579  49.297 -32.738 1.00 15.72  ? 97   LEU B CG    1 
ATOM   4838 C  CD1   . LEU B 1 111 ? 20.342  49.568 -33.642 1.00 16.54  ? 97   LEU B CD1   1 
ATOM   4839 C  CD2   . LEU B 1 111 ? 22.483  48.224 -33.322 1.00 18.17  ? 97   LEU B CD2   1 
ATOM   4840 N  N     . HIS B 1 112 ? 20.199  50.621 -29.750 1.00 16.12  ? 98   HIS B N     1 
ATOM   4841 C  CA    . HIS B 1 112 ? 19.788  49.873 -28.567 1.00 15.18  ? 98   HIS B CA    1 
ATOM   4842 C  C     . HIS B 1 112 ? 19.381  48.478 -29.025 1.00 16.70  ? 98   HIS B C     1 
ATOM   4843 O  O     . HIS B 1 112 ? 18.351  48.318 -29.686 1.00 16.94  ? 98   HIS B O     1 
ATOM   4844 C  CB    . HIS B 1 112 ? 18.634  50.575 -27.855 1.00 15.58  ? 98   HIS B CB    1 
ATOM   4845 C  CG    . HIS B 1 112 ? 18.369  50.057 -26.479 1.00 15.39  ? 98   HIS B CG    1 
ATOM   4846 N  ND1   . HIS B 1 112 ? 17.374  50.570 -25.676 1.00 13.10  ? 98   HIS B ND1   1 
ATOM   4847 C  CD2   . HIS B 1 112 ? 18.981  49.089 -25.752 1.00 16.97  ? 98   HIS B CD2   1 
ATOM   4848 C  CE1   . HIS B 1 112 ? 17.388  49.948 -24.510 1.00 16.85  ? 98   HIS B CE1   1 
ATOM   4849 N  NE2   . HIS B 1 112 ? 18.350  49.040 -24.531 1.00 16.65  ? 98   HIS B NE2   1 
ATOM   4850 N  N     . ILE B 1 113 ? 20.200  47.474 -28.698 1.00 14.95  ? 99   ILE B N     1 
ATOM   4851 C  CA    . ILE B 1 113 ? 19.861  46.070 -28.911 1.00 16.33  ? 99   ILE B CA    1 
ATOM   4852 C  C     . ILE B 1 113 ? 19.287  45.505 -27.613 1.00 16.10  ? 99   ILE B C     1 
ATOM   4853 O  O     . ILE B 1 113 ? 19.890  45.650 -26.544 1.00 16.26  ? 99   ILE B O     1 
ATOM   4854 C  CB    . ILE B 1 113 ? 21.085  45.260 -29.371 1.00 15.99  ? 99   ILE B CB    1 
ATOM   4855 C  CG1   . ILE B 1 113 ? 21.712  45.888 -30.630 1.00 15.41  ? 99   ILE B CG1   1 
ATOM   4856 C  CG2   . ILE B 1 113 ? 20.691  43.817 -29.669 1.00 15.43  ? 99   ILE B CG2   1 
ATOM   4857 C  CD1   . ILE B 1 113 ? 23.143  45.407 -30.895 1.00 17.42  ? 99   ILE B CD1   1 
ATOM   4858 N  N     . VAL B 1 114 ? 18.106  44.902 -27.693 1.00 16.02  ? 100  VAL B N     1 
ATOM   4859 C  CA    . VAL B 1 114 ? 17.428  44.343 -26.520 1.00 14.53  ? 100  VAL B CA    1 
ATOM   4860 C  C     . VAL B 1 114 ? 17.295  42.843 -26.730 1.00 14.79  ? 100  VAL B C     1 
ATOM   4861 O  O     . VAL B 1 114 ? 16.530  42.403 -27.593 1.00 17.01  ? 100  VAL B O     1 
ATOM   4862 C  CB    . VAL B 1 114 ? 16.048  44.970 -26.278 1.00 15.94  ? 100  VAL B CB    1 
ATOM   4863 C  CG1   . VAL B 1 114 ? 15.407  44.322 -25.048 1.00 15.21  ? 100  VAL B CG1   1 
ATOM   4864 C  CG2   . VAL B 1 114 ? 16.163  46.465 -26.081 1.00 15.22  ? 100  VAL B CG2   1 
ATOM   4865 N  N     . GLY B 1 115 ? 18.042  42.060 -25.957 1.00 15.71  ? 101  GLY B N     1 
ATOM   4866 C  CA    . GLY B 1 115 ? 17.878  40.614 -25.998 1.00 17.34  ? 101  GLY B CA    1 
ATOM   4867 C  C     . GLY B 1 115 ? 16.597  40.213 -25.287 1.00 17.92  ? 101  GLY B C     1 
ATOM   4868 O  O     . GLY B 1 115 ? 16.331  40.665 -24.166 1.00 15.76  ? 101  GLY B O     1 
ATOM   4869 N  N     . ALA B 1 116 ? 15.814  39.339 -25.916 1.00 17.03  ? 102  ALA B N     1 
ATOM   4870 C  CA    . ALA B 1 116 ? 14.458  39.057 -25.477 1.00 17.86  ? 102  ALA B CA    1 
ATOM   4871 C  C     . ALA B 1 116 ? 14.209  37.562 -25.371 1.00 19.51  ? 102  ALA B C     1 
ATOM   4872 O  O     . ALA B 1 116 ? 14.963  36.755 -25.928 1.00 18.00  ? 102  ALA B O     1 
ATOM   4873 C  CB    . ALA B 1 116 ? 13.427  39.684 -26.431 1.00 16.47  ? 102  ALA B CB    1 
ATOM   4874 N  N     . PRO B 1 117 ? 13.172  37.159 -24.623 1.00 20.48  ? 103  PRO B N     1 
ATOM   4875 C  CA    . PRO B 1 117 ? 12.772  35.746 -24.605 1.00 22.69  ? 103  PRO B CA    1 
ATOM   4876 C  C     . PRO B 1 117 ? 12.464  35.254 -26.007 1.00 19.72  ? 103  PRO B C     1 
ATOM   4877 O  O     . PRO B 1 117 ? 12.050  36.026 -26.875 1.00 18.73  ? 103  PRO B O     1 
ATOM   4878 C  CB    . PRO B 1 117 ? 11.491  35.750 -23.762 1.00 19.76  ? 103  PRO B CB    1 
ATOM   4879 C  CG    . PRO B 1 117 ? 11.521  37.016 -23.021 1.00 21.65  ? 103  PRO B CG    1 
ATOM   4880 C  CD    . PRO B 1 117 ? 12.232  37.996 -23.856 1.00 19.08  ? 103  PRO B CD    1 
ATOM   4881 N  N     . GLY B 1 118 ? 12.615  33.947 -26.196 1.00 21.93  ? 104  GLY B N     1 
ATOM   4882 C  CA    . GLY B 1 118 ? 12.392  33.369 -27.505 1.00 23.14  ? 104  GLY B CA    1 
ATOM   4883 C  C     . GLY B 1 118 ? 10.951  33.516 -27.950 1.00 24.92  ? 104  GLY B C     1 
ATOM   4884 O  O     . GLY B 1 118 ? 10.024  33.593 -27.133 1.00 24.13  ? 104  GLY B O     1 
ATOM   4885 N  N     . THR B 1 119 ? 10.772  33.519 -29.275 1.00 25.17  ? 105  THR B N     1 
ATOM   4886 C  CA    . THR B 1 119 ? 9.483   33.874 -29.856 1.00 26.14  ? 105  THR B CA    1 
ATOM   4887 C  C     . THR B 1 119 ? 8.396   32.927 -29.381 1.00 28.25  ? 105  THR B C     1 
ATOM   4888 O  O     . THR B 1 119 ? 7.288   33.365 -29.068 1.00 29.66  ? 105  THR B O     1 
ATOM   4889 C  CB    . THR B 1 119 ? 9.563   33.872 -31.381 1.00 27.43  ? 105  THR B CB    1 
ATOM   4890 O  OG1   . THR B 1 119 ? 9.982   32.585 -31.822 1.00 27.51  ? 105  THR B OG1   1 
ATOM   4891 C  CG2   . THR B 1 119 ? 10.557  34.894 -31.876 1.00 27.12  ? 105  THR B CG2   1 
ATOM   4892 N  N     . ALA B 1 120 ? 8.704   31.635 -29.277 1.00 29.72  ? 106  ALA B N     1 
ATOM   4893 C  CA    . ALA B 1 120 ? 7.710   30.673 -28.808 1.00 31.28  ? 106  ALA B CA    1 
ATOM   4894 C  C     . ALA B 1 120 ? 7.211   31.032 -27.412 1.00 29.82  ? 106  ALA B C     1 
ATOM   4895 O  O     . ALA B 1 120 ? 6.002   31.008 -27.143 1.00 31.08  ? 106  ALA B O     1 
ATOM   4896 C  CB    . ALA B 1 120 ? 8.308   29.266 -28.816 1.00 30.56  ? 106  ALA B CB    1 
ATOM   4897 N  N     . SER B 1 121 ? 8.132   31.374 -26.513 1.00 29.47  ? 107  SER B N     1 
ATOM   4898 C  CA    . SER B 1 121 ? 7.752   31.813 -25.172 1.00 30.17  ? 107  SER B CA    1 
ATOM   4899 C  C     . SER B 1 121 ? 6.834   33.023 -25.228 1.00 27.57  ? 107  SER B C     1 
ATOM   4900 O  O     . SER B 1 121 ? 5.852   33.113 -24.472 1.00 26.13  ? 107  SER B O     1 
ATOM   4901 C  CB    . SER B 1 121 ? 9.003   32.140 -24.354 1.00 30.36  ? 107  SER B CB    1 
ATOM   4902 O  OG    . SER B 1 121 ? 9.400   31.023 -23.596 1.00 37.46  ? 107  SER B OG    1 
ATOM   4903 N  N     . GLN B 1 122 ? 7.151   33.976 -26.105 1.00 26.37  ? 108  GLN B N     1 
ATOM   4904 C  CA    . GLN B 1 122 ? 6.328   35.170 -26.233 1.00 26.16  ? 108  GLN B CA    1 
ATOM   4905 C  C     . GLN B 1 122 ? 4.931   34.826 -26.733 1.00 26.61  ? 108  GLN B C     1 
ATOM   4906 O  O     . GLN B 1 122 ? 3.936   35.309 -26.181 1.00 26.11  ? 108  GLN B O     1 
ATOM   4907 C  CB    . GLN B 1 122 ? 7.009   36.167 -27.164 1.00 25.07  ? 108  GLN B CB    1 
ATOM   4908 C  CG    . GLN B 1 122 ? 8.313   36.717 -26.602 1.00 23.23  ? 108  GLN B CG    1 
ATOM   4909 C  CD    . GLN B 1 122 ? 8.876   37.791 -27.482 1.00 23.52  ? 108  GLN B CD    1 
ATOM   4910 O  OE1   . GLN B 1 122 ? 8.123   38.565 -28.075 1.00 24.47  ? 108  GLN B OE1   1 
ATOM   4911 N  NE2   . GLN B 1 122 ? 10.207  37.874 -27.559 1.00 22.24  ? 108  GLN B NE2   1 
ATOM   4912 N  N     . GLN B 1 123 ? 4.832   33.971 -27.765 1.00 28.07  ? 109  GLN B N     1 
ATOM   4913 C  CA    . GLN B 1 123 ? 3.516   33.635 -28.320 1.00 30.09  ? 109  GLN B CA    1 
ATOM   4914 C  C     . GLN B 1 123 ? 2.639   32.903 -27.311 1.00 27.76  ? 109  GLN B C     1 
ATOM   4915 O  O     . GLN B 1 123 ? 1.415   33.072 -27.326 1.00 28.69  ? 109  GLN B O     1 
ATOM   4916 C  CB    . GLN B 1 123 ? 3.639   32.799 -29.607 1.00 32.23  ? 109  GLN B CB    1 
ATOM   4917 C  CG    . GLN B 1 123 ? 4.880   33.078 -30.446 1.00 36.41  ? 109  GLN B CG    1 
ATOM   4918 C  CD    . GLN B 1 123 ? 4.749   32.712 -31.921 1.00 45.86  ? 109  GLN B CD    1 
ATOM   4919 O  OE1   . GLN B 1 123 ? 4.207   31.667 -32.267 1.00 56.54  ? 109  GLN B OE1   1 
ATOM   4920 N  NE2   . GLN B 1 123 ? 5.265   33.573 -32.793 1.00 46.52  ? 109  GLN B NE2   1 
ATOM   4921 N  N     . ARG B 1 124 ? 3.234   32.082 -26.442 1.00 25.99  ? 110  ARG B N     1 
ATOM   4922 C  CA    . ARG B 1 124 ? 2.480   31.397 -25.396 1.00 27.36  ? 110  ARG B CA    1 
ATOM   4923 C  C     . ARG B 1 124 ? 2.073   32.316 -24.247 1.00 27.30  ? 110  ARG B C     1 
ATOM   4924 O  O     . ARG B 1 124 ? 1.349   31.865 -23.352 1.00 27.21  ? 110  ARG B O     1 
ATOM   4925 C  CB    . ARG B 1 124 ? 3.293   30.231 -24.846 1.00 27.99  ? 110  ARG B CB    1 
ATOM   4926 C  CG    . ARG B 1 124 ? 3.718   29.236 -25.886 1.00 29.41  ? 110  ARG B CG    1 
ATOM   4927 C  CD    . ARG B 1 124 ? 4.035   27.909 -25.244 1.00 33.88  ? 110  ARG B CD    1 
ATOM   4928 N  NE    . ARG B 1 124 ? 5.362   27.963 -24.646 1.00 38.95  ? 110  ARG B NE    1 
ATOM   4929 C  CZ    . ARG B 1 124 ? 6.468   27.547 -25.249 1.00 50.63  ? 110  ARG B CZ    1 
ATOM   4930 N  NH1   . ARG B 1 124 ? 6.434   27.008 -26.459 1.00 44.17  ? 110  ARG B NH1   1 
ATOM   4931 N  NH2   . ARG B 1 124 ? 7.638   27.682 -24.628 1.00 47.55  ? 110  ARG B NH2   1 
ATOM   4932 N  N     . GLY B 1 125 ? 2.545   33.559 -24.228 1.00 24.78  ? 111  GLY B N     1 
ATOM   4933 C  CA    . GLY B 1 125 ? 2.183   34.486 -23.169 1.00 24.05  ? 111  GLY B CA    1 
ATOM   4934 C  C     . GLY B 1 125 ? 2.620   34.038 -21.794 1.00 25.24  ? 111  GLY B C     1 
ATOM   4935 O  O     . GLY B 1 125 ? 1.864   34.194 -20.827 1.00 24.31  ? 111  GLY B O     1 
ATOM   4936 N  N     . GLU B 1 126 ? 3.825   33.481 -21.682 1.00 23.00  ? 112  GLU B N     1 
ATOM   4937 C  CA    . GLU B 1 126 ? 4.278   32.933 -20.410 1.00 24.99  ? 112  GLU B CA    1 
ATOM   4938 C  C     . GLU B 1 126 ? 4.531   34.036 -19.384 1.00 22.51  ? 112  GLU B C     1 
ATOM   4939 O  O     . GLU B 1 126 ? 4.847   35.176 -19.730 1.00 20.11  ? 112  GLU B O     1 
ATOM   4940 C  CB    . GLU B 1 126 ? 5.552   32.103 -20.612 1.00 23.53  ? 112  GLU B CB    1 
ATOM   4941 C  CG    . GLU B 1 126 ? 5.428   31.075 -21.733 1.00 28.60  ? 112  GLU B CG    1 
ATOM   4942 C  CD    . GLU B 1 126 ? 6.570   30.063 -21.771 1.00 30.85  ? 112  GLU B CD    1 
ATOM   4943 O  OE1   . GLU B 1 126 ? 7.743   30.455 -21.616 1.00 31.27  ? 112  GLU B OE1   1 
ATOM   4944 O  OE2   . GLU B 1 126 ? 6.288   28.866 -21.971 1.00 35.29  ? 112  GLU B OE2   1 
ATOM   4945 N  N     . LEU B 1 127 ? 4.397   33.674 -18.101 1.00 21.10  ? 113  LEU B N     1 
ATOM   4946 C  CA    . LEU B 1 127 ? 4.654   34.584 -16.981 1.00 21.72  ? 113  LEU B CA    1 
ATOM   4947 C  C     . LEU B 1 127 ? 6.144   34.553 -16.643 1.00 20.68  ? 113  LEU B C     1 
ATOM   4948 O  O     . LEU B 1 127 ? 6.583   33.976 -15.645 1.00 20.67  ? 113  LEU B O     1 
ATOM   4949 C  CB    . LEU B 1 127 ? 3.793   34.209 -15.777 1.00 21.17  ? 113  LEU B CB    1 
ATOM   4950 C  CG    . LEU B 1 127 ? 2.287   34.200 -16.050 1.00 23.54  ? 113  LEU B CG    1 
ATOM   4951 C  CD1   . LEU B 1 127 ? 1.463   33.781 -14.820 1.00 24.63  ? 113  LEU B CD1   1 
ATOM   4952 C  CD2   . LEU B 1 127 ? 1.864   35.580 -16.497 1.00 25.16  ? 113  LEU B CD2   1 
ATOM   4953 N  N     . LEU B 1 128 ? 6.925   35.230 -17.474 1.00 18.68  ? 114  LEU B N     1 
ATOM   4954 C  CA    . LEU B 1 128 ? 8.377   35.203 -17.395 1.00 20.96  ? 114  LEU B CA    1 
ATOM   4955 C  C     . LEU B 1 128 ? 8.929   36.357 -16.554 1.00 19.32  ? 114  LEU B C     1 
ATOM   4956 O  O     . LEU B 1 128 ? 8.322   37.427 -16.452 1.00 19.00  ? 114  LEU B O     1 
ATOM   4957 C  CB    . LEU B 1 128 ? 8.969   35.271 -18.805 1.00 20.40  ? 114  LEU B CB    1 
ATOM   4958 C  CG    . LEU B 1 128 ? 8.758   34.121 -19.789 1.00 24.84  ? 114  LEU B CG    1 
ATOM   4959 C  CD1   . LEU B 1 128 ? 9.678   34.319 -21.013 1.00 24.70  ? 114  LEU B CD1   1 
ATOM   4960 C  CD2   . LEU B 1 128 ? 8.996   32.747 -19.144 1.00 25.60  ? 114  LEU B CD2   1 
ATOM   4961 N  N     . HIS B 1 129 ? 10.112  36.142 -15.977 1.00 19.48  ? 115  HIS B N     1 
ATOM   4962 C  CA    . HIS B 1 129 ? 10.807  37.236 -15.305 1.00 19.11  ? 115  HIS B CA    1 
ATOM   4963 C  C     . HIS B 1 129 ? 11.088  38.363 -16.300 1.00 19.20  ? 115  HIS B C     1 
ATOM   4964 O  O     . HIS B 1 129 ? 11.231  38.136 -17.507 1.00 17.77  ? 115  HIS B O     1 
ATOM   4965 C  CB    . HIS B 1 129 ? 12.112  36.741 -14.673 1.00 20.24  ? 115  HIS B CB    1 
ATOM   4966 C  CG    . HIS B 1 129 ? 13.114  36.248 -15.670 1.00 21.42  ? 115  HIS B CG    1 
ATOM   4967 N  ND1   . HIS B 1 129 ? 13.083  34.970 -16.187 1.00 23.39  ? 115  HIS B ND1   1 
ATOM   4968 C  CD2   . HIS B 1 129 ? 14.180  36.860 -16.245 1.00 21.07  ? 115  HIS B CD2   1 
ATOM   4969 C  CE1   . HIS B 1 129 ? 14.076  34.820 -17.047 1.00 24.20  ? 115  HIS B CE1   1 
ATOM   4970 N  NE2   . HIS B 1 129 ? 14.757  35.950 -17.098 1.00 19.85  ? 115  HIS B NE2   1 
ATOM   4971 N  N     . HIS B 1 130 ? 11.143  39.589 -15.780 1.00 18.37  ? 116  HIS B N     1 
ATOM   4972 C  CA    . HIS B 1 130 ? 11.258  40.820 -16.554 1.00 17.50  ? 116  HIS B CA    1 
ATOM   4973 C  C     . HIS B 1 130 ? 10.014  41.101 -17.412 1.00 18.82  ? 116  HIS B C     1 
ATOM   4974 O  O     . HIS B 1 130 ? 10.106  41.785 -18.433 1.00 15.53  ? 116  HIS B O     1 
ATOM   4975 C  CB    . HIS B 1 130 ? 12.518  40.839 -17.443 1.00 15.71  ? 116  HIS B CB    1 
ATOM   4976 C  CG    . HIS B 1 130 ? 13.801  40.478 -16.744 1.00 18.12  ? 116  HIS B CG    1 
ATOM   4977 N  ND1   . HIS B 1 130 ? 13.952  40.479 -15.370 1.00 17.20  ? 116  HIS B ND1   1 
ATOM   4978 C  CD2   . HIS B 1 130 ? 15.011  40.127 -17.251 1.00 18.62  ? 116  HIS B CD2   1 
ATOM   4979 C  CE1   . HIS B 1 130 ? 15.189  40.130 -15.065 1.00 16.78  ? 116  HIS B CE1   1 
ATOM   4980 N  NE2   . HIS B 1 130 ? 15.853  39.910 -16.188 1.00 19.34  ? 116  HIS B NE2   1 
ATOM   4981 N  N     . THR B 1 131 ? 8.841   40.588 -17.049 1.00 18.95  ? 117  THR B N     1 
ATOM   4982 C  CA    . THR B 1 131 ? 7.606   41.037 -17.678 1.00 18.73  ? 117  THR B CA    1 
ATOM   4983 C  C     . THR B 1 131 ? 6.713   41.691 -16.638 1.00 19.38  ? 117  THR B C     1 
ATOM   4984 O  O     . THR B 1 131 ? 6.999   41.674 -15.437 1.00 17.30  ? 117  THR B O     1 
ATOM   4985 C  CB    . THR B 1 131 ? 6.854   39.887 -18.371 1.00 19.86  ? 117  THR B CB    1 
ATOM   4986 O  OG1   . THR B 1 131 ? 6.352   38.965 -17.391 1.00 21.72  ? 117  THR B OG1   1 
ATOM   4987 C  CG2   . THR B 1 131 ? 7.760   39.158 -19.373 1.00 17.63  ? 117  THR B CG2   1 
ATOM   4988 N  N     . LEU B 1 132 ? 5.621   42.301 -17.112 1.00 19.49  ? 118  LEU B N     1 
ATOM   4989 C  CA    . LEU B 1 132 ? 4.638   42.834 -16.182 1.00 19.69  ? 118  LEU B CA    1 
ATOM   4990 C  C     . LEU B 1 132 ? 3.734   41.746 -15.625 1.00 21.19  ? 118  LEU B C     1 
ATOM   4991 O  O     . LEU B 1 132 ? 2.807   42.050 -14.861 1.00 19.23  ? 118  LEU B O     1 
ATOM   4992 C  CB    . LEU B 1 132 ? 3.803   43.926 -16.854 1.00 19.39  ? 118  LEU B CB    1 
ATOM   4993 C  CG    . LEU B 1 132 ? 4.619   45.087 -17.443 1.00 20.51  ? 118  LEU B CG    1 
ATOM   4994 C  CD1   . LEU B 1 132 ? 3.661   46.166 -17.983 1.00 20.33  ? 118  LEU B CD1   1 
ATOM   4995 C  CD2   . LEU B 1 132 ? 5.619   45.667 -16.420 1.00 16.31  ? 118  LEU B CD2   1 
ATOM   4996 N  N     . GLY B 1 133 ? 3.984   40.489 -15.978 1.00 21.49  ? 119  GLY B N     1 
ATOM   4997 C  CA    . GLY B 1 133 ? 3.166   39.409 -15.470 1.00 22.21  ? 119  GLY B CA    1 
ATOM   4998 C  C     . GLY B 1 133 ? 1.820   39.287 -16.143 1.00 23.47  ? 119  GLY B C     1 
ATOM   4999 O  O     . GLY B 1 133 ? 0.898   38.701 -15.564 1.00 22.88  ? 119  GLY B O     1 
ATOM   5000 N  N     . ASP B 1 134 ? 1.674   39.844 -17.341 1.00 23.90  ? 120  ASP B N     1 
ATOM   5001 C  CA    . ASP B 1 134 ? 0.418   39.810 -18.076 1.00 24.33  ? 120  ASP B CA    1 
ATOM   5002 C  C     . ASP B 1 134 ? 0.519   39.013 -19.375 1.00 26.46  ? 120  ASP B C     1 
ATOM   5003 O  O     . ASP B 1 134 ? -0.451  38.975 -20.144 1.00 28.01  ? 120  ASP B O     1 
ATOM   5004 C  CB    . ASP B 1 134 ? -0.034  41.237 -18.376 1.00 26.05  ? 120  ASP B CB    1 
ATOM   5005 C  CG    . ASP B 1 134 ? 0.999   42.022 -19.177 1.00 24.71  ? 120  ASP B CG    1 
ATOM   5006 O  OD1   . ASP B 1 134 ? 2.082   41.471 -19.522 1.00 22.64  ? 120  ASP B OD1   1 
ATOM   5007 O  OD2   . ASP B 1 134 ? 0.728   43.207 -19.450 1.00 23.58  ? 120  ASP B OD2   1 
ATOM   5008 N  N     . GLY B 1 135 ? 1.655   38.368 -19.634 1.00 22.37  ? 121  GLY B N     1 
ATOM   5009 C  CA    . GLY B 1 135 ? 1.873   37.655 -20.886 1.00 22.81  ? 121  GLY B CA    1 
ATOM   5010 C  C     . GLY B 1 135 ? 2.144   38.516 -22.103 1.00 24.14  ? 121  GLY B C     1 
ATOM   5011 O  O     . GLY B 1 135 ? 2.088   38.006 -23.229 1.00 22.65  ? 121  GLY B O     1 
ATOM   5012 N  N     . GLU B 1 136 ? 2.431   39.805 -21.931 1.00 22.38  ? 122  GLU B N     1 
ATOM   5013 C  CA    . GLU B 1 136 ? 2.591   40.722 -23.053 1.00 23.05  ? 122  GLU B CA    1 
ATOM   5014 C  C     . GLU B 1 136 ? 4.067   41.053 -23.234 1.00 22.80  ? 122  GLU B C     1 
ATOM   5015 O  O     . GLU B 1 136 ? 4.759   41.343 -22.257 1.00 22.43  ? 122  GLU B O     1 
ATOM   5016 C  CB    . GLU B 1 136 ? 1.785   42.004 -22.839 1.00 23.29  ? 122  GLU B CB    1 
ATOM   5017 C  CG    . GLU B 1 136 ? 2.289   43.103 -23.737 1.00 26.32  ? 122  GLU B CG    1 
ATOM   5018 C  CD    . GLU B 1 136 ? 1.825   42.934 -25.169 1.00 28.35  ? 122  GLU B CD    1 
ATOM   5019 O  OE1   . GLU B 1 136 ? 0.926   42.084 -25.420 1.00 30.58  ? 122  GLU B OE1   1 
ATOM   5020 O  OE2   . GLU B 1 136 ? 2.398   43.618 -26.037 1.00 25.75  ? 122  GLU B OE2   1 
ATOM   5021 N  N     . PHE B 1 137 ? 4.560   40.991 -24.473 1.00 21.26  ? 123  PHE B N     1 
ATOM   5022 C  CA    . PHE B 1 137 ? 5.992   41.160 -24.717 1.00 22.45  ? 123  PHE B CA    1 
ATOM   5023 C  C     . PHE B 1 137 ? 6.341   42.359 -25.600 1.00 21.81  ? 123  PHE B C     1 
ATOM   5024 O  O     . PHE B 1 137 ? 7.521   42.547 -25.932 1.00 21.44  ? 123  PHE B O     1 
ATOM   5025 C  CB    . PHE B 1 137 ? 6.556   39.847 -25.280 1.00 21.78  ? 123  PHE B CB    1 
ATOM   5026 C  CG    . PHE B 1 137 ? 6.578   38.728 -24.253 1.00 22.54  ? 123  PHE B CG    1 
ATOM   5027 C  CD1   . PHE B 1 137 ? 5.446   37.942 -24.031 1.00 23.00  ? 123  PHE B CD1   1 
ATOM   5028 C  CD2   . PHE B 1 137 ? 7.704   38.508 -23.467 1.00 20.80  ? 123  PHE B CD2   1 
ATOM   5029 C  CE1   . PHE B 1 137 ? 5.452   36.930 -23.069 1.00 22.80  ? 123  PHE B CE1   1 
ATOM   5030 C  CE2   . PHE B 1 137 ? 7.722   37.501 -22.504 1.00 20.55  ? 123  PHE B CE2   1 
ATOM   5031 C  CZ    . PHE B 1 137 ? 6.600   36.705 -22.307 1.00 22.30  ? 123  PHE B CZ    1 
ATOM   5032 N  N     . ARG B 1 138 ? 5.374   43.220 -25.935 1.00 22.06  ? 124  ARG B N     1 
ATOM   5033 C  CA    . ARG B 1 138 ? 5.637   44.363 -26.804 1.00 23.52  ? 124  ARG B CA    1 
ATOM   5034 C  C     . ARG B 1 138 ? 5.479   45.716 -26.123 1.00 22.89  ? 124  ARG B C     1 
ATOM   5035 O  O     . ARG B 1 138 ? 5.654   46.746 -26.793 1.00 22.11  ? 124  ARG B O     1 
ATOM   5036 C  CB    . ARG B 1 138 ? 4.707   44.341 -28.017 1.00 27.18  ? 124  ARG B CB    1 
ATOM   5037 C  CG    . ARG B 1 138 ? 4.729   43.073 -28.821 1.00 32.69  ? 124  ARG B CG    1 
ATOM   5038 C  CD    . ARG B 1 138 ? 4.201   43.381 -30.225 1.00 50.68  ? 124  ARG B CD    1 
ATOM   5039 N  NE    . ARG B 1 138 ? 3.899   42.253 -31.107 1.00 60.44  ? 124  ARG B NE    1 
ATOM   5040 C  CZ    . ARG B 1 138 ? 4.601   41.131 -31.231 1.00 55.19  ? 124  ARG B CZ    1 
ATOM   5041 N  NH1   . ARG B 1 138 ? 5.689   40.899 -30.512 1.00 47.40  ? 124  ARG B NH1   1 
ATOM   5042 N  NH2   . ARG B 1 138 ? 4.201   40.216 -32.110 1.00 51.60  ? 124  ARG B NH2   1 
ATOM   5043 N  N     . HIS B 1 139 ? 5.146   45.747 -24.826 1.00 20.88  ? 125  HIS B N     1 
ATOM   5044 C  CA    . HIS B 1 139 ? 4.977   47.014 -24.119 1.00 20.34  ? 125  HIS B CA    1 
ATOM   5045 C  C     . HIS B 1 139 ? 6.219   47.884 -24.277 1.00 19.78  ? 125  HIS B C     1 
ATOM   5046 O  O     . HIS B 1 139 ? 6.139   49.068 -24.627 1.00 20.98  ? 125  HIS B O     1 
ATOM   5047 C  CB    . HIS B 1 139 ? 4.738   46.770 -22.619 1.00 21.08  ? 125  HIS B CB    1 
ATOM   5048 C  CG    . HIS B 1 139 ? 3.395   46.209 -22.254 1.00 21.87  ? 125  HIS B CG    1 
ATOM   5049 N  ND1   . HIS B 1 139 ? 2.206   46.683 -22.763 1.00 24.00  ? 125  HIS B ND1   1 
ATOM   5050 C  CD2   . HIS B 1 139 ? 3.061   45.251 -21.354 1.00 21.23  ? 125  HIS B CD2   1 
ATOM   5051 C  CE1   . HIS B 1 139 ? 1.200   46.017 -22.223 1.00 23.53  ? 125  HIS B CE1   1 
ATOM   5052 N  NE2   . HIS B 1 139 ? 1.692   45.142 -21.363 1.00 24.13  ? 125  HIS B NE2   1 
ATOM   5053 N  N     . PHE B 1 140 ? 7.382   47.313 -23.987 1.00 19.09  ? 126  PHE B N     1 
ATOM   5054 C  CA    . PHE B 1 140 ? 8.598   48.113 -23.904 1.00 18.21  ? 126  PHE B CA    1 
ATOM   5055 C  C     . PHE B 1 140 ? 9.098   48.505 -25.283 1.00 18.74  ? 126  PHE B C     1 
ATOM   5056 O  O     . PHE B 1 140 ? 9.707   49.570 -25.445 1.00 17.01  ? 126  PHE B O     1 
ATOM   5057 C  CB    . PHE B 1 140 ? 9.659   47.356 -23.109 1.00 16.31  ? 126  PHE B CB    1 
ATOM   5058 C  CG    . PHE B 1 140 ? 9.092   46.622 -21.925 1.00 17.13  ? 126  PHE B CG    1 
ATOM   5059 C  CD1   . PHE B 1 140 ? 8.181   47.256 -21.083 1.00 17.02  ? 126  PHE B CD1   1 
ATOM   5060 C  CD2   . PHE B 1 140 ? 9.454   45.305 -21.650 1.00 16.64  ? 126  PHE B CD2   1 
ATOM   5061 C  CE1   . PHE B 1 140 ? 7.612   46.590 -19.989 1.00 16.17  ? 126  PHE B CE1   1 
ATOM   5062 C  CE2   . PHE B 1 140 ? 8.908   44.636 -20.538 1.00 17.46  ? 126  PHE B CE2   1 
ATOM   5063 C  CZ    . PHE B 1 140 ? 7.986   45.287 -19.714 1.00 16.66  ? 126  PHE B CZ    1 
ATOM   5064 N  N     . TYR B 1 141 ? 8.870   47.652 -26.274 1.00 19.10  ? 127  TYR B N     1 
ATOM   5065 C  CA    . TYR B 1 141 ? 9.107   48.047 -27.659 1.00 20.00  ? 127  TYR B CA    1 
ATOM   5066 C  C     . TYR B 1 141 ? 8.294   49.291 -28.023 1.00 20.50  ? 127  TYR B C     1 
ATOM   5067 O  O     . TYR B 1 141 ? 8.828   50.252 -28.592 1.00 19.76  ? 127  TYR B O     1 
ATOM   5068 C  CB    . TYR B 1 141 ? 8.791   46.861 -28.566 1.00 19.90  ? 127  TYR B CB    1 
ATOM   5069 C  CG    . TYR B 1 141 ? 8.783   47.146 -30.051 1.00 22.09  ? 127  TYR B CG    1 
ATOM   5070 C  CD1   . TYR B 1 141 ? 9.965   47.146 -30.775 1.00 22.49  ? 127  TYR B CD1   1 
ATOM   5071 C  CD2   . TYR B 1 141 ? 7.592   47.376 -30.732 1.00 22.69  ? 127  TYR B CD2   1 
ATOM   5072 C  CE1   . TYR B 1 141 ? 9.972   47.391 -32.135 1.00 23.11  ? 127  TYR B CE1   1 
ATOM   5073 C  CE2   . TYR B 1 141 ? 7.590   47.619 -32.094 1.00 23.66  ? 127  TYR B CE2   1 
ATOM   5074 C  CZ    . TYR B 1 141 ? 8.787   47.626 -32.787 1.00 24.72  ? 127  TYR B CZ    1 
ATOM   5075 O  OH    . TYR B 1 141 ? 8.806   47.863 -34.140 1.00 26.33  ? 127  TYR B OH    1 
ATOM   5076 N  N     . HIS B 1 142 ? 7.007   49.314 -27.663 1.00 20.62  ? 128  HIS B N     1 
ATOM   5077 C  CA    . HIS B 1 142 ? 6.189   50.473 -28.005 1.00 21.73  ? 128  HIS B CA    1 
ATOM   5078 C  C     . HIS B 1 142 ? 6.630   51.708 -27.233 1.00 19.75  ? 128  HIS B C     1 
ATOM   5079 O  O     . HIS B 1 142 ? 6.671   52.805 -27.802 1.00 16.20  ? 128  HIS B O     1 
ATOM   5080 C  CB    . HIS B 1 142 ? 4.696   50.192 -27.765 1.00 22.77  ? 128  HIS B CB    1 
ATOM   5081 C  CG    . HIS B 1 142 ? 4.131   49.161 -28.690 1.00 26.94  ? 128  HIS B CG    1 
ATOM   5082 N  ND1   . HIS B 1 142 ? 4.343   49.189 -30.055 1.00 26.57  ? 128  HIS B ND1   1 
ATOM   5083 C  CD2   . HIS B 1 142 ? 3.365   48.070 -28.450 1.00 26.29  ? 128  HIS B CD2   1 
ATOM   5084 C  CE1   . HIS B 1 142 ? 3.742   48.155 -30.613 1.00 28.66  ? 128  HIS B CE1   1 
ATOM   5085 N  NE2   . HIS B 1 142 ? 3.139   47.462 -29.662 1.00 30.92  ? 128  HIS B NE2   1 
ATOM   5086 N  N     . MET B 1 143 ? 6.989   51.557 -25.950 1.00 18.00  ? 129  MET B N     1 
ATOM   5087 C  CA    . MET B 1 143 ? 7.442   52.731 -25.206 1.00 18.70  ? 129  MET B CA    1 
ATOM   5088 C  C     . MET B 1 143 ? 8.744   53.302 -25.740 1.00 19.38  ? 129  MET B C     1 
ATOM   5089 O  O     . MET B 1 143 ? 9.030   54.479 -25.501 1.00 17.21  ? 129  MET B O     1 
ATOM   5090 C  CB    . MET B 1 143 ? 7.582   52.488 -23.689 1.00 19.23  ? 129  MET B CB    1 
ATOM   5091 C  CG    . MET B 1 143 ? 6.355   51.894 -22.966 1.00 19.66  ? 129  MET B CG    1 
ATOM   5092 S  SD    . MET B 1 143 ? 6.652   50.695 -21.631 1.00 14.42  ? 129  MET B SD    1 
ATOM   5093 C  CE    . MET B 1 143 ? 7.212   51.842 -20.375 1.00 17.63  ? 129  MET B CE    1 
ATOM   5094 N  N     . SER B 1 144 ? 9.525   52.524 -26.483 1.00 18.29  ? 130  SER B N     1 
ATOM   5095 C  CA    . SER B 1 144 ? 10.725  53.089 -27.076 1.00 20.09  ? 130  SER B CA    1 
ATOM   5096 C  C     . SER B 1 144 ? 10.460  53.830 -28.383 1.00 20.92  ? 130  SER B C     1 
ATOM   5097 O  O     . SER B 1 144 ? 11.376  54.485 -28.895 1.00 21.93  ? 130  SER B O     1 
ATOM   5098 C  CB    . SER B 1 144 ? 11.744  51.981 -27.318 1.00 19.78  ? 130  SER B CB    1 
ATOM   5099 O  OG    . SER B 1 144 ? 13.035  52.528 -27.300 1.00 25.64  ? 130  SER B OG    1 
ATOM   5100 N  N     . GLU B 1 145 ? 9.247   53.738 -28.932 1.00 20.14  ? 131  GLU B N     1 
ATOM   5101 C  CA    . GLU B 1 145 ? 8.976   54.324 -30.244 1.00 21.59  ? 131  GLU B CA    1 
ATOM   5102 C  C     . GLU B 1 145 ? 9.192   55.837 -30.282 1.00 21.36  ? 131  GLU B C     1 
ATOM   5103 O  O     . GLU B 1 145 ? 9.780   56.319 -31.263 1.00 20.20  ? 131  GLU B O     1 
ATOM   5104 C  CB    . GLU B 1 145 ? 7.556   53.910 -30.689 1.00 23.04  ? 131  GLU B CB    1 
ATOM   5105 C  CG    . GLU B 1 145 ? 7.040   54.370 -32.076 1.00 26.46  ? 131  GLU B CG    1 
ATOM   5106 C  CD    . GLU B 1 145 ? 6.922   55.876 -32.290 1.00 34.02  ? 131  GLU B CD    1 
ATOM   5107 O  OE1   . GLU B 1 145 ? 6.591   56.611 -31.335 1.00 41.57  ? 131  GLU B OE1   1 
ATOM   5108 O  OE2   . GLU B 1 145 ? 7.173   56.326 -33.432 1.00 37.77  ? 131  GLU B OE2   1 
ATOM   5109 N  N     . PRO B 1 146 ? 8.765   56.632 -29.294 1.00 21.84  ? 132  PRO B N     1 
ATOM   5110 C  CA    . PRO B 1 146 ? 8.990   58.083 -29.382 1.00 21.90  ? 132  PRO B CA    1 
ATOM   5111 C  C     . PRO B 1 146 ? 10.448  58.511 -29.347 1.00 20.71  ? 132  PRO B C     1 
ATOM   5112 O  O     . PRO B 1 146 ? 10.727  59.665 -29.696 1.00 20.13  ? 132  PRO B O     1 
ATOM   5113 C  CB    . PRO B 1 146 ? 8.238   58.631 -28.160 1.00 20.76  ? 132  PRO B CB    1 
ATOM   5114 C  CG    . PRO B 1 146 ? 7.246   57.586 -27.818 1.00 22.29  ? 132  PRO B CG    1 
ATOM   5115 C  CD    . PRO B 1 146 ? 7.953   56.297 -28.111 1.00 21.52  ? 132  PRO B CD    1 
ATOM   5116 N  N     . ILE B 1 147 ? 11.378  57.672 -28.887 1.00 18.96  ? 133  ILE B N     1 
ATOM   5117 C  CA    . ILE B 1 147 ? 12.752  58.122 -28.675 1.00 19.08  ? 133  ILE B CA    1 
ATOM   5118 C  C     . ILE B 1 147 ? 13.725  57.444 -29.638 1.00 19.64  ? 133  ILE B C     1 
ATOM   5119 O  O     . ILE B 1 147 ? 14.941  57.418 -29.388 1.00 18.91  ? 133  ILE B O     1 
ATOM   5120 C  CB    . ILE B 1 147 ? 13.176  57.944 -27.206 1.00 17.75  ? 133  ILE B CB    1 
ATOM   5121 C  CG1   . ILE B 1 147 ? 13.066  56.487 -26.769 1.00 18.07  ? 133  ILE B CG1   1 
ATOM   5122 C  CG2   . ILE B 1 147 ? 12.297  58.817 -26.308 1.00 18.08  ? 133  ILE B CG2   1 
ATOM   5123 C  CD1   . ILE B 1 147 ? 13.468  56.284 -25.279 1.00 19.43  ? 133  ILE B CD1   1 
ATOM   5124 N  N     . THR B 1 148 ? 13.213  56.907 -30.749 1.00 18.12  ? 134  THR B N     1 
ATOM   5125 C  CA    . THR B 1 148 ? 14.052  56.331 -31.794 1.00 18.20  ? 134  THR B CA    1 
ATOM   5126 C  C     . THR B 1 148 ? 13.508  56.759 -33.152 1.00 20.22  ? 134  THR B C     1 
ATOM   5127 O  O     . THR B 1 148 ? 12.333  57.107 -33.278 1.00 16.25  ? 134  THR B O     1 
ATOM   5128 C  CB    . THR B 1 148 ? 14.118  54.799 -31.675 1.00 17.92  ? 134  THR B CB    1 
ATOM   5129 O  OG1   . THR B 1 148 ? 12.789  54.266 -31.623 1.00 19.21  ? 134  THR B OG1   1 
ATOM   5130 C  CG2   . THR B 1 148 ? 14.885  54.380 -30.387 1.00 17.86  ? 134  THR B CG2   1 
ATOM   5131 N  N     . VAL B 1 149 ? 14.380  56.785 -34.165 1.00 17.63  ? 135  VAL B N     1 
ATOM   5132 C  CA    . VAL B 1 149 ? 13.912  57.105 -35.511 1.00 18.77  ? 135  VAL B CA    1 
ATOM   5133 C  C     . VAL B 1 149 ? 13.471  55.856 -36.249 1.00 18.80  ? 135  VAL B C     1 
ATOM   5134 O  O     . VAL B 1 149 ? 12.757  55.954 -37.255 1.00 19.94  ? 135  VAL B O     1 
ATOM   5135 C  CB    . VAL B 1 149 ? 14.979  57.830 -36.351 1.00 20.31  ? 135  VAL B CB    1 
ATOM   5136 C  CG1   . VAL B 1 149 ? 15.108  59.257 -35.877 1.00 22.67  ? 135  VAL B CG1   1 
ATOM   5137 C  CG2   . VAL B 1 149 ? 16.326  57.099 -36.267 1.00 19.50  ? 135  VAL B CG2   1 
ATOM   5138 N  N     . ALA B 1 150 ? 13.899  54.690 -35.800 1.00 19.13  ? 136  ALA B N     1 
ATOM   5139 C  CA    . ALA B 1 150 ? 13.528  53.439 -36.433 1.00 19.66  ? 136  ALA B CA    1 
ATOM   5140 C  C     . ALA B 1 150 ? 13.603  52.359 -35.374 1.00 19.17  ? 136  ALA B C     1 
ATOM   5141 O  O     . ALA B 1 150 ? 14.468  52.397 -34.498 1.00 17.83  ? 136  ALA B O     1 
ATOM   5142 C  CB    . ALA B 1 150 ? 14.451  53.102 -37.605 1.00 17.76  ? 136  ALA B CB    1 
ATOM   5143 N  N     . GLN B 1 151 ? 12.705  51.390 -35.467 1.00 18.93  ? 137  GLN B N     1 
ATOM   5144 C  CA    . GLN B 1 151 ? 12.796  50.237 -34.588 1.00 20.56  ? 137  GLN B CA    1 
ATOM   5145 C  C     . GLN B 1 151 ? 12.242  49.035 -35.328 1.00 21.40  ? 137  GLN B C     1 
ATOM   5146 O  O     . GLN B 1 151 ? 11.509  49.170 -36.310 1.00 22.05  ? 137  GLN B O     1 
ATOM   5147 C  CB    . GLN B 1 151 ? 12.031  50.445 -33.266 1.00 20.10  ? 137  GLN B CB    1 
ATOM   5148 C  CG    . GLN B 1 151 ? 10.542  50.629 -33.476 1.00 22.32  ? 137  GLN B CG    1 
ATOM   5149 C  CD    . GLN B 1 151 ? 9.783   51.058 -32.218 1.00 26.90  ? 137  GLN B CD    1 
ATOM   5150 O  OE1   . GLN B 1 151 ? 8.584   51.354 -32.289 1.00 27.83  ? 137  GLN B OE1   1 
ATOM   5151 N  NE2   . GLN B 1 151 ? 10.461  51.042 -31.058 1.00 22.65  ? 137  GLN B NE2   1 
ATOM   5152 N  N     . ALA B 1 152 ? 12.601  47.851 -34.847 1.00 20.37  ? 138  ALA B N     1 
ATOM   5153 C  CA    . ALA B 1 152 ? 12.086  46.624 -35.432 1.00 21.43  ? 138  ALA B CA    1 
ATOM   5154 C  C     . ALA B 1 152 ? 12.024  45.548 -34.357 1.00 21.21  ? 138  ALA B C     1 
ATOM   5155 O  O     . ALA B 1 152 ? 12.844  45.521 -33.440 1.00 19.05  ? 138  ALA B O     1 
ATOM   5156 C  CB    . ALA B 1 152 ? 12.957  46.129 -36.602 1.00 21.35  ? 138  ALA B CB    1 
ATOM   5157 N  N     . ILE B 1 153 ? 11.067  44.642 -34.493 1.00 21.79  ? 139  ILE B N     1 
ATOM   5158 C  CA    . ILE B 1 153 ? 11.115  43.369 -33.788 1.00 22.06  ? 139  ILE B CA    1 
ATOM   5159 C  C     . ILE B 1 153 ? 11.622  42.340 -34.786 1.00 22.56  ? 139  ILE B C     1 
ATOM   5160 O  O     . ILE B 1 153 ? 10.962  42.073 -35.796 1.00 22.70  ? 139  ILE B O     1 
ATOM   5161 C  CB    . ILE B 1 153 ? 9.746   42.958 -33.228 1.00 24.11  ? 139  ILE B CB    1 
ATOM   5162 C  CG1   . ILE B 1 153 ? 9.293   43.923 -32.136 1.00 22.94  ? 139  ILE B CG1   1 
ATOM   5163 C  CG2   . ILE B 1 153 ? 9.812   41.537 -32.707 1.00 23.96  ? 139  ILE B CG2   1 
ATOM   5164 C  CD1   . ILE B 1 153 ? 7.858   43.646 -31.620 1.00 26.58  ? 139  ILE B CD1   1 
ATOM   5165 N  N     . LEU B 1 154 ? 12.789  41.774 -34.509 1.00 17.56  ? 140  LEU B N     1 
ATOM   5166 C  CA    . LEU B 1 154 ? 13.442  40.883 -35.452 1.00 21.43  ? 140  LEU B CA    1 
ATOM   5167 C  C     . LEU B 1 154 ? 12.770  39.524 -35.402 1.00 21.08  ? 140  LEU B C     1 
ATOM   5168 O  O     . LEU B 1 154 ? 12.514  38.992 -34.320 1.00 18.89  ? 140  LEU B O     1 
ATOM   5169 C  CB    . LEU B 1 154 ? 14.936  40.769 -35.131 1.00 17.98  ? 140  LEU B CB    1 
ATOM   5170 C  CG    . LEU B 1 154 ? 15.723  42.064 -35.362 1.00 19.35  ? 140  LEU B CG    1 
ATOM   5171 C  CD1   . LEU B 1 154 ? 17.224  41.871 -35.085 1.00 15.66  ? 140  LEU B CD1   1 
ATOM   5172 C  CD2   . LEU B 1 154 ? 15.509  42.540 -36.809 1.00 18.25  ? 140  LEU B CD2   1 
ATOM   5173 N  N     . THR B 1 155 ? 12.462  38.974 -36.571 1.00 19.49  ? 141  THR B N     1 
ATOM   5174 C  CA    . THR B 1 155 ? 11.928  37.628 -36.685 1.00 20.99  ? 141  THR B CA    1 
ATOM   5175 C  C     . THR B 1 155 ? 12.814  36.819 -37.618 1.00 21.07  ? 141  THR B C     1 
ATOM   5176 O  O     . THR B 1 155 ? 13.640  37.365 -38.346 1.00 19.93  ? 141  THR B O     1 
ATOM   5177 C  CB    . THR B 1 155 ? 10.498  37.632 -37.225 1.00 22.46  ? 141  THR B CB    1 
ATOM   5178 O  OG1   . THR B 1 155 ? 10.516  38.039 -38.603 1.00 20.34  ? 141  THR B OG1   1 
ATOM   5179 C  CG2   . THR B 1 155 ? 9.587   38.572 -36.394 1.00 23.39  ? 141  THR B CG2   1 
ATOM   5180 N  N     . GLU B 1 156 ? 12.599  35.505 -37.626 1.00 22.38  ? 142  GLU B N     1 
ATOM   5181 C  CA    . GLU B 1 156 ? 13.288  34.649 -38.589 1.00 22.69  ? 142  GLU B CA    1 
ATOM   5182 C  C     . GLU B 1 156 ? 13.017  35.088 -40.025 1.00 22.75  ? 142  GLU B C     1 
ATOM   5183 O  O     . GLU B 1 156 ? 13.868  34.909 -40.906 1.00 22.00  ? 142  GLU B O     1 
ATOM   5184 C  CB    . GLU B 1 156 ? 12.854  33.200 -38.373 1.00 24.40  ? 142  GLU B CB    1 
ATOM   5185 C  CG    . GLU B 1 156 ? 13.434  32.206 -39.357 1.00 25.78  ? 142  GLU B CG    1 
ATOM   5186 C  CD    . GLU B 1 156 ? 12.929  30.802 -39.110 1.00 28.13  ? 142  GLU B CD    1 
ATOM   5187 O  OE1   . GLU B 1 156 ? 11.754  30.669 -38.689 1.00 27.01  ? 142  GLU B OE1   1 
ATOM   5188 O  OE2   . GLU B 1 156 ? 13.695  29.842 -39.358 1.00 26.07  ? 142  GLU B OE2   1 
ATOM   5189 N  N     . GLN B 1 157 ? 11.854  35.680 -40.280 1.00 22.18  ? 143  GLN B N     1 
ATOM   5190 C  CA    . GLN B 1 157 ? 11.465  36.042 -41.634 1.00 22.91  ? 143  GLN B CA    1 
ATOM   5191 C  C     . GLN B 1 157 ? 11.871  37.448 -42.050 1.00 22.17  ? 143  GLN B C     1 
ATOM   5192 O  O     . GLN B 1 157 ? 11.787  37.758 -43.243 1.00 23.07  ? 143  GLN B O     1 
ATOM   5193 C  CB    . GLN B 1 157 ? 9.952   35.889 -41.820 1.00 23.16  ? 143  GLN B CB    1 
ATOM   5194 C  CG    . GLN B 1 157 ? 9.483   34.483 -41.650 1.00 26.28  ? 143  GLN B CG    1 
ATOM   5195 C  CD    . GLN B 1 157 ? 8.006   34.340 -41.875 1.00 29.44  ? 143  GLN B CD    1 
ATOM   5196 O  OE1   . GLN B 1 157 ? 7.384   35.190 -42.513 1.00 31.84  ? 143  GLN B OE1   1 
ATOM   5197 N  NE2   . GLN B 1 157 ? 7.430   33.255 -41.365 1.00 31.02  ? 143  GLN B NE2   1 
ATOM   5198 N  N     . ASN B 1 158 ? 12.312  38.309 -41.129 1.00 21.33  ? 144  ASN B N     1 
ATOM   5199 C  CA    . ASN B 1 158 ? 12.647  39.666 -41.531 1.00 21.74  ? 144  ASN B CA    1 
ATOM   5200 C  C     . ASN B 1 158 ? 14.038  40.123 -41.120 1.00 20.23  ? 144  ASN B C     1 
ATOM   5201 O  O     . ASN B 1 158 ? 14.434  41.234 -41.490 1.00 19.44  ? 144  ASN B O     1 
ATOM   5202 C  CB    . ASN B 1 158 ? 11.596  40.654 -40.990 1.00 21.94  ? 144  ASN B CB    1 
ATOM   5203 C  CG    . ASN B 1 158 ? 11.743  40.943 -39.480 1.00 23.88  ? 144  ASN B CG    1 
ATOM   5204 O  OD1   . ASN B 1 158 ? 12.718  40.548 -38.834 1.00 19.83  ? 144  ASN B OD1   1 
ATOM   5205 N  ND2   . ASN B 1 158 ? 10.738  41.615 -38.914 1.00 22.62  ? 144  ASN B ND2   1 
ATOM   5206 N  N     . ALA B 1 159 ? 14.782  39.291 -40.386 1.00 20.10  ? 145  ALA B N     1 
ATOM   5207 C  CA    . ALA B 1 159 ? 15.929  39.731 -39.590 1.00 21.44  ? 145  ALA B CA    1 
ATOM   5208 C  C     . ALA B 1 159 ? 16.880  40.648 -40.357 1.00 21.23  ? 145  ALA B C     1 
ATOM   5209 O  O     . ALA B 1 159 ? 17.125  41.789 -39.948 1.00 20.98  ? 145  ALA B O     1 
ATOM   5210 C  CB    . ALA B 1 159 ? 16.679  38.509 -39.054 1.00 20.41  ? 145  ALA B CB    1 
ATOM   5211 N  N     . CYS B 1 160 ? 17.451  40.157 -41.461 1.00 20.31  ? 146  CYS B N     1 
ATOM   5212 C  CA    . CYS B 1 160 ? 18.587  40.863 -42.051 1.00 23.09  ? 146  CYS B CA    1 
ATOM   5213 C  C     . CYS B 1 160 ? 18.175  42.169 -42.709 1.00 22.48  ? 146  CYS B C     1 
ATOM   5214 O  O     . CYS B 1 160 ? 18.923  43.152 -42.651 1.00 20.79  ? 146  CYS B O     1 
ATOM   5215 C  CB    . CYS B 1 160 ? 19.338  39.971 -43.036 1.00 22.40  ? 146  CYS B CB    1 
ATOM   5216 S  SG    . CYS B 1 160 ? 20.143  38.595 -42.209 1.00 27.05  ? 146  CYS B SG    1 
ATOM   5217 N  N     . TYR B 1 161 ? 16.999  42.221 -43.335 1.00 21.89  ? 147  TYR B N     1 
ATOM   5218 C  CA    . TYR B 1 161 ? 16.641  43.509 -43.913 1.00 24.00  ? 147  TYR B CA    1 
ATOM   5219 C  C     . TYR B 1 161 ? 16.065  44.475 -42.898 1.00 22.59  ? 147  TYR B C     1 
ATOM   5220 O  O     . TYR B 1 161 ? 16.139  45.686 -43.128 1.00 21.50  ? 147  TYR B O     1 
ATOM   5221 C  CB    . TYR B 1 161 ? 15.680  43.396 -45.098 1.00 23.86  ? 147  TYR B CB    1 
ATOM   5222 C  CG    . TYR B 1 161 ? 14.277  42.930 -44.818 1.00 26.54  ? 147  TYR B CG    1 
ATOM   5223 C  CD1   . TYR B 1 161 ? 13.983  41.566 -44.752 1.00 27.52  ? 147  TYR B CD1   1 
ATOM   5224 C  CD2   . TYR B 1 161 ? 13.247  43.844 -44.564 1.00 26.86  ? 147  TYR B CD2   1 
ATOM   5225 C  CE1   . TYR B 1 161 ? 12.693  41.115 -44.524 1.00 25.18  ? 147  TYR B CE1   1 
ATOM   5226 C  CE2   . TYR B 1 161 ? 11.949  43.404 -44.303 1.00 28.45  ? 147  TYR B CE2   1 
ATOM   5227 C  CZ    . TYR B 1 161 ? 11.679  42.030 -44.281 1.00 28.01  ? 147  TYR B CZ    1 
ATOM   5228 O  OH    . TYR B 1 161 ? 10.407  41.548 -44.034 1.00 27.65  ? 147  TYR B OH    1 
ATOM   5229 N  N     . GLU B 1 162 ? 15.524  43.989 -41.776 1.00 22.42  ? 148  GLU B N     1 
ATOM   5230 C  CA    . GLU B 1 162 ? 15.126  44.922 -40.727 1.00 20.04  ? 148  GLU B CA    1 
ATOM   5231 C  C     . GLU B 1 162 ? 16.347  45.521 -40.037 1.00 21.89  ? 148  GLU B C     1 
ATOM   5232 O  O     . GLU B 1 162 ? 16.357  46.712 -39.690 1.00 20.55  ? 148  GLU B O     1 
ATOM   5233 C  CB    . GLU B 1 162 ? 14.210  44.224 -39.725 1.00 22.26  ? 148  GLU B CB    1 
ATOM   5234 C  CG    . GLU B 1 162 ? 12.751  44.135 -40.180 1.00 24.62  ? 148  GLU B CG    1 
ATOM   5235 C  CD    . GLU B 1 162 ? 12.123  45.493 -40.463 1.00 27.24  ? 148  GLU B CD    1 
ATOM   5236 O  OE1   . GLU B 1 162 ? 12.417  46.097 -41.514 1.00 26.18  ? 148  GLU B OE1   1 
ATOM   5237 O  OE2   . GLU B 1 162 ? 11.327  45.963 -39.628 1.00 29.69  ? 148  GLU B OE2   1 
ATOM   5238 N  N     . ILE B 1 163 ? 17.388  44.714 -39.834 1.00 19.62  ? 149  ILE B N     1 
ATOM   5239 C  CA    . ILE B 1 163 ? 18.635  45.249 -39.294 1.00 19.97  ? 149  ILE B CA    1 
ATOM   5240 C  C     . ILE B 1 163 ? 19.158  46.349 -40.204 1.00 21.12  ? 149  ILE B C     1 
ATOM   5241 O  O     . ILE B 1 163 ? 19.488  47.453 -39.753 1.00 17.88  ? 149  ILE B O     1 
ATOM   5242 C  CB    . ILE B 1 163 ? 19.671  44.121 -39.117 1.00 19.38  ? 149  ILE B CB    1 
ATOM   5243 C  CG1   . ILE B 1 163 ? 19.307  43.229 -37.915 1.00 18.11  ? 149  ILE B CG1   1 
ATOM   5244 C  CG2   . ILE B 1 163 ? 21.092  44.687 -38.964 1.00 20.08  ? 149  ILE B CG2   1 
ATOM   5245 C  CD1   . ILE B 1 163 ? 20.117  41.918 -37.878 1.00 18.58  ? 149  ILE B CD1   1 
ATOM   5246 N  N     . ASP B 1 164 ? 19.187  46.079 -41.509 1.00 18.71  ? 150  ASP B N     1 
ATOM   5247 C  CA    . ASP B 1 164 ? 19.729  47.054 -42.438 1.00 21.64  ? 150  ASP B CA    1 
ATOM   5248 C  C     . ASP B 1 164 ? 18.868  48.309 -42.490 1.00 22.12  ? 150  ASP B C     1 
ATOM   5249 O  O     . ASP B 1 164 ? 19.401  49.420 -42.600 1.00 20.26  ? 150  ASP B O     1 
ATOM   5250 C  CB    . ASP B 1 164 ? 19.873  46.435 -43.830 1.00 21.60  ? 150  ASP B CB    1 
ATOM   5251 C  CG    . ASP B 1 164 ? 20.992  45.393 -43.898 1.00 22.82  ? 150  ASP B CG    1 
ATOM   5252 O  OD1   . ASP B 1 164 ? 21.853  45.349 -42.994 1.00 21.88  ? 150  ASP B OD1   1 
ATOM   5253 O  OD2   . ASP B 1 164 ? 21.017  44.608 -44.865 1.00 24.66  ? 150  ASP B OD2   1 
ATOM   5254 N  N     . ARG B 1 165 ? 17.539  48.156 -42.434 1.00 20.23  ? 151  ARG B N     1 
ATOM   5255 C  CA    . ARG B 1 165 ? 16.664  49.324 -42.481 1.00 20.76  ? 151  ARG B CA    1 
ATOM   5256 C  C     . ARG B 1 165 ? 16.900  50.228 -41.284 1.00 20.31  ? 151  ARG B C     1 
ATOM   5257 O  O     . ARG B 1 165 ? 17.055  51.448 -41.428 1.00 18.53  ? 151  ARG B O     1 
ATOM   5258 C  CB    . ARG B 1 165 ? 15.195  48.894 -42.540 1.00 21.34  ? 151  ARG B CB    1 
ATOM   5259 C  CG    . ARG B 1 165 ? 14.218  50.069 -42.497 1.00 20.99  ? 151  ARG B CG    1 
ATOM   5260 C  CD    . ARG B 1 165 ? 12.745  49.621 -42.446 1.00 21.98  ? 151  ARG B CD    1 
ATOM   5261 N  NE    . ARG B 1 165 ? 12.384  48.882 -41.240 1.00 23.19  ? 151  ARG B NE    1 
ATOM   5262 C  CZ    . ARG B 1 165 ? 12.116  49.447 -40.069 1.00 22.38  ? 151  ARG B CZ    1 
ATOM   5263 N  NH1   . ARG B 1 165 ? 12.275  50.744 -39.878 1.00 21.32  ? 151  ARG B NH1   1 
ATOM   5264 N  NH2   . ARG B 1 165 ? 11.678  48.689 -39.063 1.00 23.23  ? 151  ARG B NH2   1 
ATOM   5265 N  N     . VAL B 1 166 ? 16.957  49.641 -40.090 1.00 19.76  ? 152  VAL B N     1 
ATOM   5266 C  CA    . VAL B 1 166 ? 17.056  50.457 -38.891 1.00 19.63  ? 152  VAL B CA    1 
ATOM   5267 C  C     . VAL B 1 166 ? 18.416  51.135 -38.834 1.00 18.25  ? 152  VAL B C     1 
ATOM   5268 O  O     . VAL B 1 166 ? 18.516  52.331 -38.550 1.00 19.91  ? 152  VAL B O     1 
ATOM   5269 C  CB    . VAL B 1 166 ? 16.774  49.597 -37.645 1.00 18.53  ? 152  VAL B CB    1 
ATOM   5270 C  CG1   . VAL B 1 166 ? 17.281  50.279 -36.368 1.00 17.45  ? 152  VAL B CG1   1 
ATOM   5271 C  CG2   . VAL B 1 166 ? 15.296  49.265 -37.548 1.00 17.87  ? 152  VAL B CG2   1 
ATOM   5272 N  N     . LEU B 1 167 ? 19.486  50.388 -39.120 1.00 17.01  ? 153  LEU B N     1 
ATOM   5273 C  CA    . LEU B 1 167 ? 20.810  51.003 -39.155 1.00 20.65  ? 153  LEU B CA    1 
ATOM   5274 C  C     . LEU B 1 167 ? 20.895  52.086 -40.227 1.00 20.81  ? 153  LEU B C     1 
ATOM   5275 O  O     . LEU B 1 167 ? 21.513  53.139 -40.014 1.00 21.43  ? 153  LEU B O     1 
ATOM   5276 C  CB    . LEU B 1 167 ? 21.880  49.937 -39.377 1.00 19.89  ? 153  LEU B CB    1 
ATOM   5277 C  CG    . LEU B 1 167 ? 22.172  49.061 -38.158 1.00 19.88  ? 153  LEU B CG    1 
ATOM   5278 C  CD1   . LEU B 1 167 ? 23.143  47.945 -38.524 1.00 18.39  ? 153  LEU B CD1   1 
ATOM   5279 C  CD2   . LEU B 1 167 ? 22.713  49.897 -37.004 1.00 18.66  ? 153  LEU B CD2   1 
ATOM   5280 N  N     . THR B 1 168 ? 20.296  51.842 -41.392 1.00 20.84  ? 154  THR B N     1 
ATOM   5281 C  CA    . THR B 1 168 ? 20.321  52.848 -42.449 1.00 22.19  ? 154  THR B CA    1 
ATOM   5282 C  C     . THR B 1 168 ? 19.629  54.132 -42.011 1.00 22.47  ? 154  THR B C     1 
ATOM   5283 O  O     . THR B 1 168 ? 20.164  55.230 -42.217 1.00 22.82  ? 154  THR B O     1 
ATOM   5284 C  CB    . THR B 1 168 ? 19.676  52.287 -43.713 1.00 22.49  ? 154  THR B CB    1 
ATOM   5285 O  OG1   . THR B 1 168 ? 20.495  51.215 -44.207 1.00 23.50  ? 154  THR B OG1   1 
ATOM   5286 C  CG2   . THR B 1 168 ? 19.541  53.380 -44.770 1.00 25.55  ? 154  THR B CG2   1 
ATOM   5287 N  N     . THR B 1 169 ? 18.456  54.017 -41.373 1.00 20.64  ? 155  THR B N     1 
ATOM   5288 C  CA    . THR B 1 169 ? 17.752  55.210 -40.914 1.00 21.55  ? 155  THR B CA    1 
ATOM   5289 C  C     . THR B 1 169 ? 18.547  55.927 -39.834 1.00 20.85  ? 155  THR B C     1 
ATOM   5290 O  O     . THR B 1 169 ? 18.543  57.160 -39.771 1.00 21.47  ? 155  THR B O     1 
ATOM   5291 C  CB    . THR B 1 169 ? 16.362  54.848 -40.371 1.00 20.64  ? 155  THR B CB    1 
ATOM   5292 O  OG1   . THR B 1 169 ? 15.630  54.092 -41.339 1.00 21.26  ? 155  THR B OG1   1 
ATOM   5293 C  CG2   . THR B 1 169 ? 15.576  56.104 -40.019 1.00 19.40  ? 155  THR B CG2   1 
ATOM   5294 N  N     . MET B 1 170 ? 19.201  55.157 -38.958 1.00 18.74  ? 156  MET B N     1 
ATOM   5295 C  CA    . MET B 1 170 ? 20.109  55.710 -37.955 1.00 21.96  ? 156  MET B CA    1 
ATOM   5296 C  C     . MET B 1 170 ? 21.204  56.543 -38.608 1.00 23.43  ? 156  MET B C     1 
ATOM   5297 O  O     . MET B 1 170 ? 21.530  57.642 -38.136 1.00 22.53  ? 156  MET B O     1 
ATOM   5298 C  CB    . MET B 1 170 ? 20.736  54.555 -37.172 1.00 21.09  ? 156  MET B CB    1 
ATOM   5299 C  CG    . MET B 1 170 ? 19.862  53.968 -36.079 1.00 18.50  ? 156  MET B CG    1 
ATOM   5300 S  SD    . MET B 1 170 ? 20.796  52.896 -34.970 1.00 17.17  ? 156  MET B SD    1 
ATOM   5301 C  CE    . MET B 1 170 ? 21.798  54.079 -34.077 1.00 17.91  ? 156  MET B CE    1 
ATOM   5302 N  N     . LEU B 1 171 ? 21.792  56.025 -39.692 1.00 21.95  ? 157  LEU B N     1 
ATOM   5303 C  CA    . LEU B 1 171 ? 22.860  56.742 -40.385 1.00 23.63  ? 157  LEU B CA    1 
ATOM   5304 C  C     . LEU B 1 171 ? 22.335  58.006 -41.054 1.00 24.77  ? 157  LEU B C     1 
ATOM   5305 O  O     . LEU B 1 171 ? 23.032  59.024 -41.098 1.00 27.15  ? 157  LEU B O     1 
ATOM   5306 C  CB    . LEU B 1 171 ? 23.526  55.833 -41.420 1.00 24.54  ? 157  LEU B CB    1 
ATOM   5307 C  CG    . LEU B 1 171 ? 24.452  54.693 -40.970 1.00 26.26  ? 157  LEU B CG    1 
ATOM   5308 C  CD1   . LEU B 1 171 ? 24.816  53.825 -42.171 1.00 26.64  ? 157  LEU B CD1   1 
ATOM   5309 C  CD2   . LEU B 1 171 ? 25.712  55.177 -40.255 1.00 25.07  ? 157  LEU B CD2   1 
ATOM   5310 N  N     . ARG B 1 172 ? 21.120  57.948 -41.604 1.00 23.69  ? 158  ARG B N     1 
ATOM   5311 C  CA    . ARG B 1 172 ? 20.541  59.100 -42.291 1.00 25.90  ? 158  ARG B CA    1 
ATOM   5312 C  C     . ARG B 1 172 ? 20.147  60.199 -41.315 1.00 24.98  ? 158  ARG B C     1 
ATOM   5313 O  O     . ARG B 1 172 ? 20.429  61.381 -41.555 1.00 23.29  ? 158  ARG B O     1 
ATOM   5314 C  CB    . ARG B 1 172 ? 19.327  58.654 -43.108 1.00 28.30  ? 158  ARG B CB    1 
ATOM   5315 C  CG    . ARG B 1 172 ? 18.620  59.772 -43.851 1.00 32.13  ? 158  ARG B CG    1 
ATOM   5316 C  CD    . ARG B 1 172 ? 17.301  59.267 -44.439 1.00 33.85  ? 158  ARG B CD    1 
ATOM   5317 N  NE    . ARG B 1 172 ? 17.500  58.051 -45.224 1.00 36.30  ? 158  ARG B NE    1 
ATOM   5318 C  CZ    . ARG B 1 172 ? 16.930  56.883 -44.948 1.00 40.93  ? 158  ARG B CZ    1 
ATOM   5319 N  NH1   . ARG B 1 172 ? 16.153  56.728 -43.888 1.00 31.56  ? 158  ARG B NH1   1 
ATOM   5320 N  NH2   . ARG B 1 172 ? 17.174  55.836 -45.735 1.00 37.72  ? 158  ARG B NH2   1 
ATOM   5321 N  N     . GLU B 1 173 ? 19.523  59.826 -40.196 1.00 22.52  ? 159  GLU B N     1 
ATOM   5322 C  CA    . GLU B 1 173 ? 18.999  60.800 -39.246 1.00 25.30  ? 159  GLU B CA    1 
ATOM   5323 C  C     . GLU B 1 173 ? 19.961  61.117 -38.122 1.00 23.88  ? 159  GLU B C     1 
ATOM   5324 O  O     . GLU B 1 173 ? 19.728  62.096 -37.393 1.00 22.79  ? 159  GLU B O     1 
ATOM   5325 C  CB    . GLU B 1 173 ? 17.690  60.308 -38.619 1.00 22.64  ? 159  GLU B CB    1 
ATOM   5326 C  CG    . GLU B 1 173 ? 16.568  60.029 -39.584 1.00 26.41  ? 159  GLU B CG    1 
ATOM   5327 C  CD    . GLU B 1 173 ? 16.345  61.127 -40.607 1.00 28.37  ? 159  GLU B CD    1 
ATOM   5328 O  OE1   . GLU B 1 173 ? 16.562  62.313 -40.289 1.00 28.09  ? 159  GLU B OE1   1 
ATOM   5329 O  OE2   . GLU B 1 173 ? 15.890  60.799 -41.717 1.00 28.56  ? 159  GLU B OE2   1 
ATOM   5330 N  N     . ARG B 1 174 ? 21.011  60.309 -37.952 1.00 19.69  ? 160  ARG B N     1 
ATOM   5331 C  CA    . ARG B 1 174 ? 21.940  60.468 -36.844 1.00 19.94  ? 160  ARG B CA    1 
ATOM   5332 C  C     . ARG B 1 174 ? 21.194  60.472 -35.500 1.00 21.06  ? 160  ARG B C     1 
ATOM   5333 O  O     . ARG B 1 174 ? 21.333  61.376 -34.671 1.00 18.03  ? 160  ARG B O     1 
ATOM   5334 C  CB    . ARG B 1 174 ? 22.779  61.724 -37.055 1.00 21.64  ? 160  ARG B CB    1 
ATOM   5335 C  CG    . ARG B 1 174 ? 23.699  61.612 -38.299 1.00 22.90  ? 160  ARG B CG    1 
ATOM   5336 C  CD    . ARG B 1 174 ? 24.799  60.579 -38.059 1.00 27.51  ? 160  ARG B CD    1 
ATOM   5337 N  NE    . ARG B 1 174 ? 25.329  59.984 -39.286 1.00 31.04  ? 160  ARG B NE    1 
ATOM   5338 C  CZ    . ARG B 1 174 ? 26.305  59.083 -39.319 1.00 33.03  ? 160  ARG B CZ    1 
ATOM   5339 N  NH1   . ARG B 1 174 ? 26.885  58.646 -38.207 1.00 29.82  ? 160  ARG B NH1   1 
ATOM   5340 N  NH2   . ARG B 1 174 ? 26.721  58.618 -40.497 1.00 35.17  ? 160  ARG B NH2   1 
ATOM   5341 N  N     . ARG B 1 175 ? 20.402  59.428 -35.285 1.00 18.87  ? 161  ARG B N     1 
ATOM   5342 C  CA    . ARG B 1 175 ? 19.560  59.324 -34.099 1.00 18.96  ? 161  ARG B CA    1 
ATOM   5343 C  C     . ARG B 1 175 ? 19.475  57.855 -33.715 1.00 18.28  ? 161  ARG B C     1 
ATOM   5344 O  O     . ARG B 1 175 ? 19.850  56.975 -34.501 1.00 16.69  ? 161  ARG B O     1 
ATOM   5345 C  CB    . ARG B 1 175 ? 18.164  59.920 -34.360 1.00 19.09  ? 161  ARG B CB    1 
ATOM   5346 C  CG    . ARG B 1 175 ? 18.105  61.427 -34.110 1.00 18.81  ? 161  ARG B CG    1 
ATOM   5347 C  CD    . ARG B 1 175 ? 16.714  62.004 -34.291 1.00 19.74  ? 161  ARG B CD    1 
ATOM   5348 N  NE    . ARG B 1 175 ? 16.439  63.020 -33.282 1.00 19.50  ? 161  ARG B NE    1 
ATOM   5349 C  CZ    . ARG B 1 175 ? 15.511  63.959 -33.397 1.00 21.90  ? 161  ARG B CZ    1 
ATOM   5350 N  NH1   . ARG B 1 175 ? 14.767  64.071 -34.494 1.00 20.19  ? 161  ARG B NH1   1 
ATOM   5351 N  NH2   . ARG B 1 175 ? 15.325  64.806 -32.391 1.00 20.28  ? 161  ARG B NH2   1 
ATOM   5352 N  N     . PRO B 1 176 ? 19.008  57.564 -32.499 1.00 16.36  ? 162  PRO B N     1 
ATOM   5353 C  CA    . PRO B 1 176 ? 18.965  56.171 -32.028 1.00 17.55  ? 162  PRO B CA    1 
ATOM   5354 C  C     . PRO B 1 176 ? 18.010  55.275 -32.794 1.00 18.01  ? 162  PRO B C     1 
ATOM   5355 O  O     . PRO B 1 176 ? 16.974  55.705 -33.308 1.00 17.45  ? 162  PRO B O     1 
ATOM   5356 C  CB    . PRO B 1 176 ? 18.483  56.310 -30.572 1.00 16.79  ? 162  PRO B CB    1 
ATOM   5357 C  CG    . PRO B 1 176 ? 18.844  57.684 -30.191 1.00 18.05  ? 162  PRO B CG    1 
ATOM   5358 C  CD    . PRO B 1 176 ? 18.615  58.493 -31.424 1.00 17.60  ? 162  PRO B CD    1 
ATOM   5359 N  N     . GLY B 1 177 ? 18.354  53.982 -32.793 1.00 17.93  ? 163  GLY B N     1 
ATOM   5360 C  CA    . GLY B 1 177 ? 17.468  52.947 -33.272 1.00 17.87  ? 163  GLY B CA    1 
ATOM   5361 C  C     . GLY B 1 177 ? 17.317  51.870 -32.209 1.00 16.54  ? 163  GLY B C     1 
ATOM   5362 O  O     . GLY B 1 177 ? 18.029  51.859 -31.201 1.00 15.87  ? 163  GLY B O     1 
ATOM   5363 N  N     . TYR B 1 178 ? 16.362  50.971 -32.437 1.00 16.02  ? 164  TYR B N     1 
ATOM   5364 C  CA    . TYR B 1 178 ? 16.030  49.951 -31.446 1.00 17.32  ? 164  TYR B CA    1 
ATOM   5365 C  C     . TYR B 1 178 ? 15.801  48.631 -32.167 1.00 16.40  ? 164  TYR B C     1 
ATOM   5366 O  O     . TYR B 1 178 ? 15.116  48.599 -33.185 1.00 15.82  ? 164  TYR B O     1 
ATOM   5367 C  CB    . TYR B 1 178 ? 14.770  50.357 -30.650 1.00 17.01  ? 164  TYR B CB    1 
ATOM   5368 C  CG    . TYR B 1 178 ? 14.230  49.350 -29.645 1.00 17.20  ? 164  TYR B CG    1 
ATOM   5369 C  CD1   . TYR B 1 178 ? 13.619  48.159 -30.047 1.00 16.38  ? 164  TYR B CD1   1 
ATOM   5370 C  CD2   . TYR B 1 178 ? 14.294  49.621 -28.283 1.00 17.55  ? 164  TYR B CD2   1 
ATOM   5371 C  CE1   . TYR B 1 178 ? 13.110  47.262 -29.107 1.00 17.73  ? 164  TYR B CE1   1 
ATOM   5372 C  CE2   . TYR B 1 178 ? 13.786  48.737 -27.344 1.00 18.61  ? 164  TYR B CE2   1 
ATOM   5373 C  CZ    . TYR B 1 178 ? 13.197  47.561 -27.757 1.00 17.27  ? 164  TYR B CZ    1 
ATOM   5374 O  OH    . TYR B 1 178 ? 12.700  46.684 -26.809 1.00 17.98  ? 164  TYR B OH    1 
ATOM   5375 N  N     . LEU B 1 179 ? 16.339  47.538 -31.621 1.00 16.13  ? 165  LEU B N     1 
ATOM   5376 C  CA    . LEU B 1 179 ? 16.107  46.213 -32.190 1.00 16.38  ? 165  LEU B CA    1 
ATOM   5377 C  C     . LEU B 1 179 ? 15.783  45.241 -31.071 1.00 17.16  ? 165  LEU B C     1 
ATOM   5378 O  O     . LEU B 1 179 ? 16.607  45.039 -30.177 1.00 15.03  ? 165  LEU B O     1 
ATOM   5379 C  CB    . LEU B 1 179 ? 17.333  45.706 -32.951 1.00 13.79  ? 165  LEU B CB    1 
ATOM   5380 C  CG    . LEU B 1 179 ? 17.755  46.471 -34.216 1.00 17.27  ? 165  LEU B CG    1 
ATOM   5381 C  CD1   . LEU B 1 179 ? 19.107  45.943 -34.703 1.00 15.17  ? 165  LEU B CD1   1 
ATOM   5382 C  CD2   . LEU B 1 179 ? 16.704  46.338 -35.281 1.00 15.40  ? 165  LEU B CD2   1 
ATOM   5383 N  N     . MET B 1 180 ? 14.621  44.603 -31.134 1.00 16.99  ? 166  MET B N     1 
ATOM   5384 C  CA    . MET B 1 180 ? 14.348  43.527 -30.194 1.00 16.26  ? 166  MET B CA    1 
ATOM   5385 C  C     . MET B 1 180 ? 14.870  42.271 -30.869 1.00 17.74  ? 166  MET B C     1 
ATOM   5386 O  O     . MET B 1 180 ? 14.519  41.992 -32.021 1.00 17.39  ? 166  MET B O     1 
ATOM   5387 C  CB    . MET B 1 180 ? 12.863  43.383 -29.868 1.00 17.76  ? 166  MET B CB    1 
ATOM   5388 C  CG    . MET B 1 180 ? 12.595  42.251 -28.855 1.00 19.35  ? 166  MET B CG    1 
ATOM   5389 S  SD    . MET B 1 180 ? 10.954  41.527 -28.891 1.00 23.14  ? 166  MET B SD    1 
ATOM   5390 C  CE    . MET B 1 180 ? 10.063  42.805 -28.035 1.00 17.48  ? 166  MET B CE    1 
ATOM   5391 N  N     . LEU B 1 181 ? 15.746  41.552 -30.175 1.00 17.41  ? 167  LEU B N     1 
ATOM   5392 C  CA    . LEU B 1 181 ? 16.386  40.352 -30.697 1.00 18.54  ? 167  LEU B CA    1 
ATOM   5393 C  C     . LEU B 1 181 ? 15.975  39.187 -29.811 1.00 17.07  ? 167  LEU B C     1 
ATOM   5394 O  O     . LEU B 1 181 ? 16.647  38.891 -28.816 1.00 16.30  ? 167  LEU B O     1 
ATOM   5395 C  CB    . LEU B 1 181 ? 17.905  40.521 -30.727 1.00 17.98  ? 167  LEU B CB    1 
ATOM   5396 C  CG    . LEU B 1 181 ? 18.711  39.354 -31.280 1.00 17.74  ? 167  LEU B CG    1 
ATOM   5397 C  CD1   . LEU B 1 181 ? 18.272  39.019 -32.696 1.00 17.82  ? 167  LEU B CD1   1 
ATOM   5398 C  CD2   . LEU B 1 181 ? 20.183  39.731 -31.239 1.00 19.49  ? 167  LEU B CD2   1 
ATOM   5399 N  N     . PRO B 1 182 ? 14.890  38.488 -30.141 1.00 19.57  ? 168  PRO B N     1 
ATOM   5400 C  CA    . PRO B 1 182 ? 14.552  37.268 -29.401 1.00 19.60  ? 168  PRO B CA    1 
ATOM   5401 C  C     . PRO B 1 182 ? 15.693  36.268 -29.485 1.00 19.91  ? 168  PRO B C     1 
ATOM   5402 O  O     . PRO B 1 182 ? 16.385  36.169 -30.501 1.00 18.91  ? 168  PRO B O     1 
ATOM   5403 C  CB    . PRO B 1 182 ? 13.304  36.754 -30.126 1.00 20.09  ? 168  PRO B CB    1 
ATOM   5404 C  CG    . PRO B 1 182 ? 12.706  38.012 -30.735 1.00 19.43  ? 168  PRO B CG    1 
ATOM   5405 C  CD    . PRO B 1 182 ? 13.891  38.791 -31.185 1.00 19.23  ? 168  PRO B CD    1 
ATOM   5406 N  N     . ALA B 1 183 ? 15.884  35.521 -28.397 1.00 20.29  ? 169  ALA B N     1 
ATOM   5407 C  CA    . ALA B 1 183 ? 17.064  34.669 -28.288 1.00 20.23  ? 169  ALA B CA    1 
ATOM   5408 C  C     . ALA B 1 183 ? 17.116  33.633 -29.403 1.00 24.22  ? 169  ALA B C     1 
ATOM   5409 O  O     . ALA B 1 183 ? 18.201  33.307 -29.901 1.00 24.94  ? 169  ALA B O     1 
ATOM   5410 C  CB    . ALA B 1 183 ? 17.100  33.989 -26.919 1.00 22.70  ? 169  ALA B CB    1 
ATOM   5411 N  N     . ASP B 1 184 ? 15.957  33.103 -29.820 1.00 23.18  ? 170  ASP B N     1 
ATOM   5412 C  CA    . ASP B 1 184 ? 15.966  32.096 -30.880 1.00 23.96  ? 170  ASP B CA    1 
ATOM   5413 C  C     . ASP B 1 184 ? 16.273  32.713 -32.245 1.00 23.38  ? 170  ASP B C     1 
ATOM   5414 O  O     . ASP B 1 184 ? 16.976  32.107 -33.058 1.00 24.48  ? 170  ASP B O     1 
ATOM   5415 C  CB    . ASP B 1 184 ? 14.637  31.333 -30.915 1.00 25.51  ? 170  ASP B CB    1 
ATOM   5416 C  CG    . ASP B 1 184 ? 13.442  32.221 -31.256 1.00 25.46  ? 170  ASP B CG    1 
ATOM   5417 O  OD1   . ASP B 1 184 ? 13.325  33.317 -30.668 1.00 21.98  ? 170  ASP B OD1   1 
ATOM   5418 O  OD2   . ASP B 1 184 ? 12.609  31.811 -32.102 1.00 25.65  ? 170  ASP B OD2   1 
ATOM   5419 N  N     . VAL B 1 185 ? 15.757  33.910 -32.513 1.00 21.39  ? 171  VAL B N     1 
ATOM   5420 C  CA    . VAL B 1 185 ? 16.020  34.570 -33.787 1.00 22.18  ? 171  VAL B CA    1 
ATOM   5421 C  C     . VAL B 1 185 ? 17.517  34.785 -33.973 1.00 22.16  ? 171  VAL B C     1 
ATOM   5422 O  O     . VAL B 1 185 ? 18.045  34.659 -35.084 1.00 19.38  ? 171  VAL B O     1 
ATOM   5423 C  CB    . VAL B 1 185 ? 15.250  35.900 -33.856 1.00 19.78  ? 171  VAL B CB    1 
ATOM   5424 C  CG1   . VAL B 1 185 ? 15.654  36.681 -35.109 1.00 20.00  ? 171  VAL B CG1   1 
ATOM   5425 C  CG2   . VAL B 1 185 ? 13.739  35.659 -33.802 1.00 21.30  ? 171  VAL B CG2   1 
ATOM   5426 N  N     . ALA B 1 186 ? 18.224  35.109 -32.885 1.00 19.16  ? 172  ALA B N     1 
ATOM   5427 C  CA    . ALA B 1 186 ? 19.659  35.372 -32.971 1.00 22.08  ? 172  ALA B CA    1 
ATOM   5428 C  C     . ALA B 1 186 ? 20.430  34.171 -33.496 1.00 21.82  ? 172  ALA B C     1 
ATOM   5429 O  O     . ALA B 1 186 ? 21.488  34.336 -34.117 1.00 22.14  ? 172  ALA B O     1 
ATOM   5430 C  CB    . ALA B 1 186 ? 20.211  35.765 -31.596 1.00 20.79  ? 172  ALA B CB    1 
ATOM   5431 N  N     . LYS B 1 187 ? 19.923  32.967 -33.272 1.00 22.03  ? 173  LYS B N     1 
ATOM   5432 C  CA    . LYS B 1 187 ? 20.611  31.764 -33.715 1.00 23.01  ? 173  LYS B CA    1 
ATOM   5433 C  C     . LYS B 1 187 ? 20.218  31.306 -35.111 1.00 23.80  ? 173  LYS B C     1 
ATOM   5434 O  O     . LYS B 1 187 ? 20.771  30.309 -35.582 1.00 24.70  ? 173  LYS B O     1 
ATOM   5435 C  CB    . LYS B 1 187 ? 20.355  30.616 -32.745 1.00 25.62  ? 173  LYS B CB    1 
ATOM   5436 C  CG    . LYS B 1 187 ? 20.564  30.952 -31.282 1.00 31.54  ? 173  LYS B CG    1 
ATOM   5437 C  CD    . LYS B 1 187 ? 20.781  29.663 -30.516 1.00 42.66  ? 173  LYS B CD    1 
ATOM   5438 C  CE    . LYS B 1 187 ? 19.689  29.449 -29.500 1.00 55.10  ? 173  LYS B CE    1 
ATOM   5439 N  NZ    . LYS B 1 187 ? 19.904  30.302 -28.305 1.00 60.45  ? 173  LYS B NZ    1 
ATOM   5440 N  N     . LYS B 1 188 ? 19.284  31.982 -35.778 1.00 22.21  ? 174  LYS B N     1 
ATOM   5441 C  CA    . LYS B 1 188 ? 18.863  31.539 -37.106 1.00 23.41  ? 174  LYS B CA    1 
ATOM   5442 C  C     . LYS B 1 188 ? 19.962  31.782 -38.141 1.00 23.57  ? 174  LYS B C     1 
ATOM   5443 O  O     . LYS B 1 188 ? 20.751  32.724 -38.039 1.00 21.93  ? 174  LYS B O     1 
ATOM   5444 C  CB    . LYS B 1 188 ? 17.569  32.235 -37.528 1.00 21.46  ? 174  LYS B CB    1 
ATOM   5445 C  CG    . LYS B 1 188 ? 16.426  31.991 -36.541 1.00 24.53  ? 174  LYS B CG    1 
ATOM   5446 C  CD    . LYS B 1 188 ? 15.989  30.524 -36.579 1.00 25.24  ? 174  LYS B CD    1 
ATOM   5447 C  CE    . LYS B 1 188 ? 14.749  30.302 -35.728 1.00 27.64  ? 174  LYS B CE    1 
ATOM   5448 N  NZ    . LYS B 1 188 ? 14.532  28.855 -35.462 1.00 29.29  ? 174  LYS B NZ    1 
ATOM   5449 N  N     . ALA B 1 189 ? 20.006  30.907 -39.144 1.00 23.76  ? 175  ALA B N     1 
ATOM   5450 C  CA    . ALA B 1 189 ? 21.055  30.954 -40.152 1.00 24.35  ? 175  ALA B CA    1 
ATOM   5451 C  C     . ALA B 1 189 ? 21.041  32.274 -40.910 1.00 24.21  ? 175  ALA B C     1 
ATOM   5452 O  O     . ALA B 1 189 ? 19.981  32.854 -41.166 1.00 24.16  ? 175  ALA B O     1 
ATOM   5453 C  CB    . ALA B 1 189 ? 20.883  29.798 -41.139 1.00 26.53  ? 175  ALA B CB    1 
ATOM   5454 N  N     . ALA B 1 190 ? 22.235  32.759 -41.255 1.00 24.79  ? 176  ALA B N     1 
ATOM   5455 C  CA    . ALA B 1 190 ? 22.372  33.946 -42.086 1.00 24.55  ? 176  ALA B CA    1 
ATOM   5456 C  C     . ALA B 1 190 ? 23.589  33.779 -42.992 1.00 26.16  ? 176  ALA B C     1 
ATOM   5457 O  O     . ALA B 1 190 ? 24.357  32.819 -42.871 1.00 26.29  ? 176  ALA B O     1 
ATOM   5458 C  CB    . ALA B 1 190 ? 22.478  35.217 -41.229 1.00 23.35  ? 176  ALA B CB    1 
ATOM   5459 N  N     . THR B 1 191 ? 23.773  34.741 -43.895 1.00 24.88  ? 177  THR B N     1 
ATOM   5460 C  CA    . THR B 1 191 ? 24.886  34.738 -44.838 1.00 25.74  ? 177  THR B CA    1 
ATOM   5461 C  C     . THR B 1 191 ? 25.690  36.023 -44.711 1.00 25.06  ? 177  THR B C     1 
ATOM   5462 O  O     . THR B 1 191 ? 25.106  37.116 -44.668 1.00 22.12  ? 177  THR B O     1 
ATOM   5463 C  CB    . THR B 1 191 ? 24.402  34.575 -46.297 1.00 26.59  ? 177  THR B CB    1 
ATOM   5464 O  OG1   . THR B 1 191 ? 23.564  33.418 -46.408 1.00 28.21  ? 177  THR B OG1   1 
ATOM   5465 C  CG2   . THR B 1 191 ? 25.582  34.445 -47.272 1.00 27.37  ? 177  THR B CG2   1 
ATOM   5466 N  N     . PRO B 1 192 ? 27.015  35.937 -44.640 1.00 27.08  ? 178  PRO B N     1 
ATOM   5467 C  CA    . PRO B 1 192 ? 27.846  37.150 -44.635 1.00 28.29  ? 178  PRO B CA    1 
ATOM   5468 C  C     . PRO B 1 192 ? 27.650  37.939 -45.915 1.00 27.50  ? 178  PRO B C     1 
ATOM   5469 O  O     . PRO B 1 192 ? 27.679  37.366 -47.011 1.00 27.84  ? 178  PRO B O     1 
ATOM   5470 C  CB    . PRO B 1 192 ? 29.279  36.593 -44.543 1.00 28.83  ? 178  PRO B CB    1 
ATOM   5471 C  CG    . PRO B 1 192 ? 29.124  35.223 -44.002 1.00 27.59  ? 178  PRO B CG    1 
ATOM   5472 C  CD    . PRO B 1 192 ? 27.829  34.712 -44.550 1.00 26.76  ? 178  PRO B CD    1 
ATOM   5473 N  N     . PRO B 1 193 ? 27.413  39.242 -45.820 1.00 29.82  ? 179  PRO B N     1 
ATOM   5474 C  CA    . PRO B 1 193 ? 27.293  40.062 -47.029 1.00 31.14  ? 179  PRO B CA    1 
ATOM   5475 C  C     . PRO B 1 193 ? 28.651  40.378 -47.643 1.00 31.84  ? 179  PRO B C     1 
ATOM   5476 O  O     . PRO B 1 193 ? 29.659  40.516 -46.948 1.00 32.70  ? 179  PRO B O     1 
ATOM   5477 C  CB    . PRO B 1 193 ? 26.606  41.342 -46.531 1.00 28.75  ? 179  PRO B CB    1 
ATOM   5478 C  CG    . PRO B 1 193 ? 26.577  41.250 -45.014 1.00 28.32  ? 179  PRO B CG    1 
ATOM   5479 C  CD    . PRO B 1 193 ? 27.325  40.036 -44.582 1.00 27.55  ? 179  PRO B CD    1 
ATOM   5480 N  N     . VAL B 1 194 ? 28.667  40.480 -48.975 1.00 33.27  ? 180  VAL B N     1 
ATOM   5481 C  CA    . VAL B 1 194 ? 29.894  40.857 -49.681 1.00 37.22  ? 180  VAL B CA    1 
ATOM   5482 C  C     . VAL B 1 194 ? 30.215  42.329 -49.449 1.00 35.13  ? 180  VAL B C     1 
ATOM   5483 O  O     . VAL B 1 194 ? 31.386  42.710 -49.327 1.00 31.93  ? 180  VAL B O     1 
ATOM   5484 C  CB    . VAL B 1 194 ? 29.783  40.558 -51.189 1.00 37.31  ? 180  VAL B CB    1 
ATOM   5485 C  CG1   . VAL B 1 194 ? 31.161  40.436 -51.797 1.00 37.68  ? 180  VAL B CG1   1 
ATOM   5486 C  CG2   . VAL B 1 194 ? 28.997  39.310 -51.435 1.00 39.45  ? 180  VAL B CG2   1 
ATOM   5487 N  N     . ASN B 1 195 ? 29.187  43.178 -49.438 1.00 32.26  ? 181  ASN B N     1 
ATOM   5488 C  CA    . ASN B 1 195 ? 29.341  44.621 -49.324 1.00 33.49  ? 181  ASN B CA    1 
ATOM   5489 C  C     . ASN B 1 195 ? 28.987  45.094 -47.922 1.00 31.15  ? 181  ASN B C     1 
ATOM   5490 O  O     . ASN B 1 195 ? 28.023  44.619 -47.316 1.00 31.48  ? 181  ASN B O     1 
ATOM   5491 C  CB    . ASN B 1 195 ? 28.449  45.352 -50.334 1.00 32.07  ? 181  ASN B CB    1 
ATOM   5492 C  CG    . ASN B 1 195 ? 28.744  44.964 -51.776 1.00 39.74  ? 181  ASN B CG    1 
ATOM   5493 O  OD1   . ASN B 1 195 ? 29.716  45.440 -52.368 1.00 35.67  ? 181  ASN B OD1   1 
ATOM   5494 N  ND2   . ASN B 1 195 ? 27.909  44.096 -52.346 1.00 43.35  ? 181  ASN B ND2   1 
ATOM   5495 N  N     . ALA B 1 196 ? 29.763  46.048 -47.420 1.00 30.26  ? 182  ALA B N     1 
ATOM   5496 C  CA    . ALA B 1 196 ? 29.414  46.718 -46.180 1.00 28.81  ? 182  ALA B CA    1 
ATOM   5497 C  C     . ALA B 1 196 ? 28.131  47.529 -46.349 1.00 29.23  ? 182  ALA B C     1 
ATOM   5498 O  O     . ALA B 1 196 ? 27.784  47.970 -47.448 1.00 25.97  ? 182  ALA B O     1 
ATOM   5499 C  CB    . ALA B 1 196 ? 30.553  47.628 -45.730 1.00 29.92  ? 182  ALA B CB    1 
ATOM   5500 N  N     . LEU B 1 197 ? 27.433  47.735 -45.239 1.00 25.75  ? 183  LEU B N     1 
ATOM   5501 C  CA    . LEU B 1 197 ? 26.285  48.631 -45.230 1.00 26.57  ? 183  LEU B CA    1 
ATOM   5502 C  C     . LEU B 1 197 ? 26.750  50.067 -45.418 1.00 28.19  ? 183  LEU B C     1 
ATOM   5503 O  O     . LEU B 1 197 ? 27.650  50.531 -44.710 1.00 28.55  ? 183  LEU B O     1 
ATOM   5504 C  CB    . LEU B 1 197 ? 25.530  48.497 -43.907 1.00 24.23  ? 183  LEU B CB    1 
ATOM   5505 C  CG    . LEU B 1 197 ? 24.126  49.115 -43.773 1.00 26.02  ? 183  LEU B CG    1 
ATOM   5506 C  CD1   . LEU B 1 197 ? 23.109  48.475 -44.703 1.00 26.24  ? 183  LEU B CD1   1 
ATOM   5507 C  CD2   . LEU B 1 197 ? 23.669  49.012 -42.327 1.00 25.18  ? 183  LEU B CD2   1 
ATOM   5508 N  N     . THR B 1 198 ? 26.183  50.746 -46.419 1.00 29.76  ? 184  THR B N     1 
ATOM   5509 C  CA    . THR B 1 198 ? 26.447  52.152 -46.687 1.00 32.61  ? 184  THR B CA    1 
ATOM   5510 C  C     . THR B 1 198 ? 25.128  52.883 -46.902 1.00 34.03  ? 184  THR B C     1 
ATOM   5511 O  O     . THR B 1 198 ? 24.157  52.310 -47.395 1.00 34.20  ? 184  THR B O     1 
ATOM   5512 C  CB    . THR B 1 198 ? 27.329  52.369 -47.921 1.00 33.21  ? 184  THR B CB    1 
ATOM   5513 O  OG1   . THR B 1 198 ? 26.590  52.017 -49.095 1.00 38.10  ? 184  THR B OG1   1 
ATOM   5514 C  CG2   . THR B 1 198 ? 28.568  51.520 -47.847 1.00 32.60  ? 184  THR B CG2   1 
ATOM   5515 N  N     . LEU B 1 199 ? 25.106  54.153 -46.520 1.00 34.49  ? 185  LEU B N     1 
ATOM   5516 C  CA    . LEU B 1 199 ? 23.995  55.045 -46.832 1.00 39.01  ? 185  LEU B CA    1 
ATOM   5517 C  C     . LEU B 1 199 ? 24.342  55.785 -48.118 1.00 41.96  ? 185  LEU B C     1 
ATOM   5518 O  O     . LEU B 1 199 ? 25.281  56.587 -48.143 1.00 41.68  ? 185  LEU B O     1 
ATOM   5519 C  CB    . LEU B 1 199 ? 23.725  56.016 -45.685 1.00 38.14  ? 185  LEU B CB    1 
ATOM   5520 C  CG    . LEU B 1 199 ? 22.834  57.231 -45.976 1.00 38.14  ? 185  LEU B CG    1 
ATOM   5521 C  CD1   . LEU B 1 199 ? 21.364  56.839 -46.009 1.00 37.87  ? 185  LEU B CD1   1 
ATOM   5522 C  CD2   . LEU B 1 199 ? 23.069  58.322 -44.928 1.00 35.74  ? 185  LEU B CD2   1 
ATOM   5523 N  N     . ARG B 1 200 ? 23.630  55.475 -49.198 1.00 44.57  ? 186  ARG B N     1 
ATOM   5524 C  CA    . ARG B 1 200 ? 23.846  56.197 -50.445 1.00 52.35  ? 186  ARG B CA    1 
ATOM   5525 C  C     . ARG B 1 200 ? 23.659  57.693 -50.217 1.00 54.07  ? 186  ARG B C     1 
ATOM   5526 O  O     . ARG B 1 200 ? 22.713  58.121 -49.546 1.00 46.66  ? 186  ARG B O     1 
ATOM   5527 C  CB    . ARG B 1 200 ? 22.887  55.698 -51.527 1.00 51.24  ? 186  ARG B CB    1 
ATOM   5528 N  N     . HIS B 1 201 ? 24.599  58.481 -50.738 1.00 55.19  ? 187  HIS B N     1 
ATOM   5529 C  CA    . HIS B 1 201 ? 24.573  59.930 -50.570 1.00 54.61  ? 187  HIS B CA    1 
ATOM   5530 C  C     . HIS B 1 201 ? 23.357  60.519 -51.281 1.00 50.07  ? 187  HIS B C     1 
ATOM   5531 O  O     . HIS B 1 201 ? 23.186  60.332 -52.490 1.00 50.83  ? 187  HIS B O     1 
ATOM   5532 C  CB    . HIS B 1 201 ? 25.865  60.529 -51.119 1.00 54.16  ? 187  HIS B CB    1 
ATOM   5533 N  N     . ALA B 1 202 ? 22.508  61.222 -50.537 1.00 47.04  ? 188  ALA B N     1 
ATOM   5534 C  CA    . ALA B 1 202 ? 21.347  61.862 -51.138 1.00 45.18  ? 188  ALA B CA    1 
ATOM   5535 C  C     . ALA B 1 202 ? 21.744  63.116 -51.914 1.00 43.39  ? 188  ALA B C     1 
ATOM   5536 O  O     . ALA B 1 202 ? 22.763  63.758 -51.636 1.00 41.64  ? 188  ALA B O     1 
ATOM   5537 C  CB    . ALA B 1 202 ? 20.307  62.218 -50.074 1.00 40.15  ? 188  ALA B CB    1 
ATOM   5538 N  N     . HIS B 1 203 ? 20.918  63.456 -52.899 1.00 41.70  ? 189  HIS B N     1 
ATOM   5539 C  CA    . HIS B 1 203 ? 21.086  64.645 -53.725 1.00 40.28  ? 189  HIS B CA    1 
ATOM   5540 C  C     . HIS B 1 203 ? 19.727  65.299 -53.914 1.00 36.40  ? 189  HIS B C     1 
ATOM   5541 O  O     . HIS B 1 203 ? 18.741  64.609 -54.188 1.00 34.60  ? 189  HIS B O     1 
ATOM   5542 C  CB    . HIS B 1 203 ? 21.706  64.306 -55.088 1.00 43.19  ? 189  HIS B CB    1 
ATOM   5543 C  CG    . HIS B 1 203 ? 22.938  63.461 -54.999 1.00 55.97  ? 189  HIS B CG    1 
ATOM   5544 N  ND1   . HIS B 1 203 ? 24.115  63.918 -54.442 1.00 57.67  ? 189  HIS B ND1   1 
ATOM   5545 C  CD2   . HIS B 1 203 ? 23.174  62.184 -55.380 1.00 61.12  ? 189  HIS B CD2   1 
ATOM   5546 C  CE1   . HIS B 1 203 ? 25.025  62.961 -54.494 1.00 58.93  ? 189  HIS B CE1   1 
ATOM   5547 N  NE2   . HIS B 1 203 ? 24.479  61.898 -55.058 1.00 65.70  ? 189  HIS B NE2   1 
ATOM   5548 N  N     . ALA B 1 204 ? 19.665  66.615 -53.756 1.00 35.22  ? 190  ALA B N     1 
ATOM   5549 C  CA    . ALA B 1 204 ? 18.431  67.323 -54.058 1.00 31.95  ? 190  ALA B CA    1 
ATOM   5550 C  C     . ALA B 1 204 ? 18.127  67.270 -55.553 1.00 31.17  ? 190  ALA B C     1 
ATOM   5551 O  O     . ALA B 1 204 ? 19.026  67.190 -56.393 1.00 32.21  ? 190  ALA B O     1 
ATOM   5552 C  CB    . ALA B 1 204 ? 18.520  68.777 -53.603 1.00 30.46  ? 190  ALA B CB    1 
ATOM   5553 N  N     . ASP B 1 205 ? 16.835  67.299 -55.873 1.00 31.07  ? 191  ASP B N     1 
ATOM   5554 C  CA    . ASP B 1 205 ? 16.401  67.588 -57.228 1.00 31.10  ? 191  ASP B CA    1 
ATOM   5555 C  C     . ASP B 1 205 ? 17.044  68.891 -57.692 1.00 32.42  ? 191  ASP B C     1 
ATOM   5556 O  O     . ASP B 1 205 ? 17.150  69.851 -56.922 1.00 30.44  ? 191  ASP B O     1 
ATOM   5557 C  CB    . ASP B 1 205 ? 14.880  67.702 -57.264 1.00 31.12  ? 191  ASP B CB    1 
ATOM   5558 C  CG    . ASP B 1 205 ? 14.360  67.996 -58.633 1.00 33.03  ? 191  ASP B CG    1 
ATOM   5559 O  OD1   . ASP B 1 205 ? 14.146  67.036 -59.404 1.00 34.23  ? 191  ASP B OD1   1 
ATOM   5560 O  OD2   . ASP B 1 205 ? 14.182  69.194 -58.942 1.00 35.05  ? 191  ASP B OD2   1 
ATOM   5561 N  N     . SER B 1 206 ? 17.520  68.909 -58.942 1.00 32.35  ? 192  SER B N     1 
ATOM   5562 C  CA    . SER B 1 206 ? 18.339  70.035 -59.392 1.00 32.02  ? 192  SER B CA    1 
ATOM   5563 C  C     . SER B 1 206 ? 17.551  71.343 -59.448 1.00 31.34  ? 192  SER B C     1 
ATOM   5564 O  O     . SER B 1 206 ? 18.136  72.418 -59.253 1.00 28.40  ? 192  SER B O     1 
ATOM   5565 C  CB    . SER B 1 206 ? 18.965  69.726 -60.752 1.00 33.09  ? 192  SER B CB    1 
ATOM   5566 O  OG    . SER B 1 206 ? 17.988  69.358 -61.706 1.00 36.97  ? 192  SER B OG    1 
ATOM   5567 N  N     . ALA B 1 207 ? 16.239  71.279 -59.714 1.00 30.47  ? 193  ALA B N     1 
ATOM   5568 C  CA    . ALA B 1 207 ? 15.417  72.488 -59.685 1.00 28.57  ? 193  ALA B CA    1 
ATOM   5569 C  C     . ALA B 1 207 ? 15.243  72.998 -58.259 1.00 27.62  ? 193  ALA B C     1 
ATOM   5570 O  O     . ALA B 1 207 ? 15.280  74.211 -58.016 1.00 25.89  ? 193  ALA B O     1 
ATOM   5571 C  CB    . ALA B 1 207 ? 14.055  72.218 -60.329 1.00 29.14  ? 193  ALA B CB    1 
ATOM   5572 N  N     . CYS B 1 208 ? 15.059  72.083 -57.306 1.00 28.63  ? 194  CYS B N     1 
ATOM   5573 C  CA    . CYS B 1 208 ? 15.058  72.449 -55.892 1.00 29.48  ? 194  CYS B CA    1 
ATOM   5574 C  C     . CYS B 1 208 ? 16.384  73.057 -55.474 1.00 27.80  ? 194  CYS B C     1 
ATOM   5575 O  O     . CYS B 1 208 ? 16.422  74.065 -54.757 1.00 26.69  ? 194  CYS B O     1 
ATOM   5576 C  CB    . CYS B 1 208 ? 14.771  71.224 -55.025 1.00 30.90  ? 194  CYS B CB    1 
ATOM   5577 S  SG    . CYS B 1 208 ? 14.806  71.611 -53.246 1.00 38.69  ? 194  CYS B SG    1 
ATOM   5578 N  N     . LEU B 1 209 ? 17.488  72.442 -55.897 1.00 26.85  ? 195  LEU B N     1 
ATOM   5579 C  CA    . LEU B 1 209 ? 18.799  72.986 -55.576 1.00 27.95  ? 195  LEU B CA    1 
ATOM   5580 C  C     . LEU B 1 209 ? 18.960  74.401 -56.118 1.00 25.27  ? 195  LEU B C     1 
ATOM   5581 O  O     . LEU B 1 209 ? 19.437  75.294 -55.405 1.00 24.31  ? 195  LEU B O     1 
ATOM   5582 C  CB    . LEU B 1 209 ? 19.880  72.075 -56.150 1.00 29.38  ? 195  LEU B CB    1 
ATOM   5583 C  CG    . LEU B 1 209 ? 21.295  72.439 -55.724 1.00 29.60  ? 195  LEU B CG    1 
ATOM   5584 C  CD1   . LEU B 1 209 ? 21.430  72.099 -54.271 1.00 27.90  ? 195  LEU B CD1   1 
ATOM   5585 C  CD2   . LEU B 1 209 ? 22.317  71.681 -56.565 1.00 32.05  ? 195  LEU B CD2   1 
ATOM   5586 N  N     . LYS B 1 210 ? 18.542  74.631 -57.365 1.00 25.95  ? 196  LYS B N     1 
ATOM   5587 C  CA    . LYS B 1 210 ? 18.674  75.953 -57.966 1.00 24.19  ? 196  LYS B CA    1 
ATOM   5588 C  C     . LYS B 1 210 ? 17.852  76.988 -57.207 1.00 23.68  ? 196  LYS B C     1 
ATOM   5589 O  O     . LYS B 1 210 ? 18.324  78.100 -56.954 1.00 22.26  ? 196  LYS B O     1 
ATOM   5590 C  CB    . LYS B 1 210 ? 18.250  75.896 -59.434 1.00 26.25  ? 196  LYS B CB    1 
ATOM   5591 C  CG    . LYS B 1 210 ? 17.732  77.200 -60.022 1.00 26.97  ? 196  LYS B CG    1 
ATOM   5592 C  CD    . LYS B 1 210 ? 17.957  77.237 -61.529 1.00 25.05  ? 196  LYS B CD    1 
ATOM   5593 C  CE    . LYS B 1 210 ? 17.155  78.349 -62.184 1.00 26.29  ? 196  LYS B CE    1 
ATOM   5594 N  NZ    . LYS B 1 210 ? 17.825  79.665 -61.948 1.00 27.23  ? 196  LYS B NZ    1 
ATOM   5595 N  N     . ALA B 1 211 ? 16.621  76.637 -56.820 1.00 23.73  ? 197  ALA B N     1 
ATOM   5596 C  CA    . ALA B 1 211 ? 15.771  77.595 -56.120 1.00 23.75  ? 197  ALA B CA    1 
ATOM   5597 C  C     . ALA B 1 211 ? 16.437  78.081 -54.835 1.00 23.48  ? 197  ALA B C     1 
ATOM   5598 O  O     . ALA B 1 211 ? 16.477  79.289 -54.559 1.00 23.04  ? 197  ALA B O     1 
ATOM   5599 C  CB    . ALA B 1 211 ? 14.404  76.967 -55.819 1.00 23.48  ? 197  ALA B CB    1 
ATOM   5600 N  N     . PHE B 1 212 ? 16.983  77.155 -54.045 1.00 21.26  ? 198  PHE B N     1 
ATOM   5601 C  CA    . PHE B 1 212 ? 17.695  77.545 -52.830 1.00 22.75  ? 198  PHE B CA    1 
ATOM   5602 C  C     . PHE B 1 212 ? 18.965  78.317 -53.161 1.00 23.33  ? 198  PHE B C     1 
ATOM   5603 O  O     . PHE B 1 212 ? 19.251  79.355 -52.551 1.00 22.09  ? 198  PHE B O     1 
ATOM   5604 C  CB    . PHE B 1 212 ? 18.047  76.313 -52.005 1.00 21.94  ? 198  PHE B CB    1 
ATOM   5605 C  CG    . PHE B 1 212 ? 19.049  76.581 -50.916 1.00 22.89  ? 198  PHE B CG    1 
ATOM   5606 C  CD1   . PHE B 1 212 ? 18.674  77.250 -49.755 1.00 23.38  ? 198  PHE B CD1   1 
ATOM   5607 C  CD2   . PHE B 1 212 ? 20.364  76.176 -51.054 1.00 22.87  ? 198  PHE B CD2   1 
ATOM   5608 C  CE1   . PHE B 1 212 ? 19.593  77.509 -48.756 1.00 20.55  ? 198  PHE B CE1   1 
ATOM   5609 C  CE2   . PHE B 1 212 ? 21.289  76.443 -50.057 1.00 23.49  ? 198  PHE B CE2   1 
ATOM   5610 C  CZ    . PHE B 1 212 ? 20.896  77.099 -48.901 1.00 21.83  ? 198  PHE B CZ    1 
ATOM   5611 N  N     . ARG B 1 213 ? 19.744  77.814 -54.122 1.00 24.13  ? 199  ARG B N     1 
ATOM   5612 C  CA    . ARG B 1 213 ? 20.981  78.488 -54.502 1.00 23.91  ? 199  ARG B CA    1 
ATOM   5613 C  C     . ARG B 1 213 ? 20.707  79.916 -54.948 1.00 24.19  ? 199  ARG B C     1 
ATOM   5614 O  O     . ARG B 1 213 ? 21.422  80.847 -54.558 1.00 24.88  ? 199  ARG B O     1 
ATOM   5615 C  CB    . ARG B 1 213 ? 21.694  77.712 -55.609 1.00 24.76  ? 199  ARG B CB    1 
ATOM   5616 C  CG    . ARG B 1 213 ? 23.055  78.313 -55.978 1.00 25.67  ? 199  ARG B CG    1 
ATOM   5617 C  CD    . ARG B 1 213 ? 23.207  78.524 -57.463 1.00 27.45  ? 199  ARG B CD    1 
ATOM   5618 N  NE    . ARG B 1 213 ? 22.686  79.825 -57.853 1.00 27.88  ? 199  ARG B NE    1 
ATOM   5619 C  CZ    . ARG B 1 213 ? 23.410  80.909 -58.108 1.00 27.11  ? 199  ARG B CZ    1 
ATOM   5620 N  NH1   . ARG B 1 213 ? 24.735  80.891 -58.072 1.00 28.68  ? 199  ARG B NH1   1 
ATOM   5621 N  NH2   . ARG B 1 213 ? 22.785  82.042 -58.405 1.00 26.03  ? 199  ARG B NH2   1 
ATOM   5622 N  N     . ASP B 1 214 ? 19.679  80.110 -55.782 1.00 24.65  ? 200  ASP B N     1 
ATOM   5623 C  CA    . ASP B 1 214 ? 19.386  81.459 -56.248 1.00 23.92  ? 200  ASP B CA    1 
ATOM   5624 C  C     . ASP B 1 214 ? 18.979  82.374 -55.097 1.00 24.48  ? 200  ASP B C     1 
ATOM   5625 O  O     . ASP B 1 214 ? 19.423  83.526 -55.030 1.00 26.80  ? 200  ASP B O     1 
ATOM   5626 C  CB    . ASP B 1 214 ? 18.300  81.444 -57.326 1.00 25.69  ? 200  ASP B CB    1 
ATOM   5627 C  CG    . ASP B 1 214 ? 18.778  80.818 -58.635 1.00 25.87  ? 200  ASP B CG    1 
ATOM   5628 O  OD1   . ASP B 1 214 ? 19.995  80.555 -58.775 1.00 27.29  ? 200  ASP B OD1   1 
ATOM   5629 O  OD2   . ASP B 1 214 ? 17.944  80.627 -59.538 1.00 23.97  ? 200  ASP B OD2   1 
ATOM   5630 N  N     . ALA B 1 215 ? 18.118  81.897 -54.197 1.00 23.99  ? 201  ALA B N     1 
ATOM   5631 C  CA    . ALA B 1 215 ? 17.663  82.757 -53.105 1.00 25.66  ? 201  ALA B CA    1 
ATOM   5632 C  C     . ALA B 1 215 ? 18.799  83.089 -52.154 1.00 24.84  ? 201  ALA B C     1 
ATOM   5633 O  O     . ALA B 1 215 ? 18.917  84.231 -51.694 1.00 24.03  ? 201  ALA B O     1 
ATOM   5634 C  CB    . ALA B 1 215 ? 16.511  82.105 -52.343 1.00 20.98  ? 201  ALA B CB    1 
ATOM   5635 N  N     . ALA B 1 216 ? 19.621  82.096 -51.812 1.00 23.20  ? 202  ALA B N     1 
ATOM   5636 C  CA    . ALA B 1 216 ? 20.775  82.387 -50.972 1.00 24.38  ? 202  ALA B CA    1 
ATOM   5637 C  C     . ALA B 1 216 ? 21.724  83.354 -51.675 1.00 24.81  ? 202  ALA B C     1 
ATOM   5638 O  O     . ALA B 1 216 ? 22.190  84.330 -51.070 1.00 23.62  ? 202  ALA B O     1 
ATOM   5639 C  CB    . ALA B 1 216 ? 21.490  81.086 -50.607 1.00 24.05  ? 202  ALA B CB    1 
ATOM   5640 N  N     . GLU B 1 217 ? 21.977  83.137 -52.971 1.00 25.74  ? 203  GLU B N     1 
ATOM   5641 C  CA    . GLU B 1 217 ? 22.931  83.991 -53.666 1.00 25.09  ? 203  GLU B CA    1 
ATOM   5642 C  C     . GLU B 1 217 ? 22.462  85.434 -53.674 1.00 25.94  ? 203  GLU B C     1 
ATOM   5643 O  O     . GLU B 1 217 ? 23.241  86.348 -53.379 1.00 26.32  ? 203  GLU B O     1 
ATOM   5644 C  CB    . GLU B 1 217 ? 23.173  83.501 -55.092 1.00 26.59  ? 203  GLU B CB    1 
ATOM   5645 C  CG    . GLU B 1 217 ? 23.418  84.649 -56.069 1.00 29.25  ? 203  GLU B CG    1 
ATOM   5646 C  CD    . GLU B 1 217 ? 24.800  85.218 -55.907 1.00 30.34  ? 203  GLU B CD    1 
ATOM   5647 O  OE1   . GLU B 1 217 ? 25.620  84.561 -55.233 1.00 34.51  ? 203  GLU B OE1   1 
ATOM   5648 O  OE2   . GLU B 1 217 ? 25.054  86.334 -56.398 1.00 31.52  ? 203  GLU B OE2   1 
ATOM   5649 N  N     . ASN B 1 218 ? 21.188  85.657 -54.021 1.00 26.23  ? 204  ASN B N     1 
ATOM   5650 C  CA    . ASN B 1 218 ? 20.667  87.015 -54.098 1.00 26.36  ? 204  ASN B CA    1 
ATOM   5651 C  C     . ASN B 1 218 ? 20.674  87.677 -52.734 1.00 26.89  ? 204  ASN B C     1 
ATOM   5652 O  O     . ASN B 1 218 ? 20.864  88.894 -52.634 1.00 27.95  ? 204  ASN B O     1 
ATOM   5653 C  CB    . ASN B 1 218 ? 19.268  87.012 -54.716 1.00 24.95  ? 204  ASN B CB    1 
ATOM   5654 C  CG    . ASN B 1 218 ? 19.243  86.335 -56.091 1.00 27.17  ? 204  ASN B CG    1 
ATOM   5655 O  OD1   . ASN B 1 218 ? 20.293  86.141 -56.723 1.00 26.00  ? 204  ASN B OD1   1 
ATOM   5656 N  ND2   . ASN B 1 218 ? 18.050  85.964 -56.554 1.00 24.88  ? 204  ASN B ND2   1 
ATOM   5657 N  N     . ARG B 1 219 ? 20.451  86.896 -51.678 1.00 25.84  ? 205  ARG B N     1 
ATOM   5658 C  CA    . ARG B 1 219 ? 20.507  87.448 -50.332 1.00 26.94  ? 205  ARG B CA    1 
ATOM   5659 C  C     . ARG B 1 219 ? 21.935  87.808 -49.950 1.00 28.03  ? 205  ARG B C     1 
ATOM   5660 O  O     . ARG B 1 219 ? 22.196  88.914 -49.458 1.00 28.70  ? 205  ARG B O     1 
ATOM   5661 C  CB    . ARG B 1 219 ? 19.916  86.460 -49.332 1.00 26.30  ? 205  ARG B CB    1 
ATOM   5662 C  CG    . ARG B 1 219 ? 19.984  86.981 -47.913 1.00 26.41  ? 205  ARG B CG    1 
ATOM   5663 C  CD    . ARG B 1 219 ? 19.071  88.198 -47.813 1.00 28.51  ? 205  ARG B CD    1 
ATOM   5664 N  NE    . ARG B 1 219 ? 19.093  88.816 -46.497 1.00 28.61  ? 205  ARG B NE    1 
ATOM   5665 C  CZ    . ARG B 1 219 ? 20.143  89.436 -45.989 1.00 29.16  ? 205  ARG B CZ    1 
ATOM   5666 N  NH1   . ARG B 1 219 ? 21.272  89.546 -46.673 1.00 30.34  ? 205  ARG B NH1   1 
ATOM   5667 N  NH2   . ARG B 1 219 ? 20.063  89.954 -44.765 1.00 29.02  ? 205  ARG B NH2   1 
ATOM   5668 N  N     . LEU B 1 220 ? 22.876  86.879 -50.170 1.00 26.75  ? 206  LEU B N     1 
ATOM   5669 C  CA    . LEU B 1 220 ? 24.266  87.130 -49.801 1.00 27.92  ? 206  LEU B CA    1 
ATOM   5670 C  C     . LEU B 1 220 ? 24.882  88.233 -50.643 1.00 30.25  ? 206  LEU B C     1 
ATOM   5671 O  O     . LEU B 1 220 ? 25.750  88.961 -50.157 1.00 31.40  ? 206  LEU B O     1 
ATOM   5672 C  CB    . LEU B 1 220 ? 25.112  85.860 -49.924 1.00 28.06  ? 206  LEU B CB    1 
ATOM   5673 C  CG    . LEU B 1 220 ? 24.729  84.691 -49.017 1.00 28.05  ? 206  LEU B CG    1 
ATOM   5674 C  CD1   . LEU B 1 220 ? 25.151  83.357 -49.622 1.00 26.70  ? 206  LEU B CD1   1 
ATOM   5675 C  CD2   . LEU B 1 220 ? 25.356  84.903 -47.644 1.00 26.85  ? 206  LEU B CD2   1 
ATOM   5676 N  N     . ALA B 1 221 ? 24.452  88.370 -51.902 1.00 30.39  ? 207  ALA B N     1 
ATOM   5677 C  CA    . ALA B 1 221 ? 25.002  89.411 -52.762 1.00 31.66  ? 207  ALA B CA    1 
ATOM   5678 C  C     . ALA B 1 221 ? 24.750  90.810 -52.221 1.00 29.63  ? 207  ALA B C     1 
ATOM   5679 O  O     . ALA B 1 221 ? 25.473  91.738 -52.597 1.00 33.70  ? 207  ALA B O     1 
ATOM   5680 C  CB    . ALA B 1 221 ? 24.436  89.298 -54.182 1.00 29.60  ? 207  ALA B CB    1 
ATOM   5681 N  N     . MET B 1 222 ? 23.749  91.000 -51.361 1.00 30.35  ? 208  MET B N     1 
ATOM   5682 C  CA    . MET B 1 222 ? 23.494  92.326 -50.813 1.00 32.86  ? 208  MET B CA    1 
ATOM   5683 C  C     . MET B 1 222 ? 24.028  92.487 -49.394 1.00 30.99  ? 208  MET B C     1 
ATOM   5684 O  O     . MET B 1 222 ? 23.735  93.494 -48.746 1.00 34.14  ? 208  MET B O     1 
ATOM   5685 C  CB    . MET B 1 222 ? 21.998  92.683 -50.857 1.00 31.72  ? 208  MET B CB    1 
ATOM   5686 C  CG    . MET B 1 222 ? 20.991  91.577 -50.602 1.00 31.10  ? 208  MET B CG    1 
ATOM   5687 S  SD    . MET B 1 222 ? 19.309  92.276 -50.615 1.00 38.54  ? 208  MET B SD    1 
ATOM   5688 C  CE    . MET B 1 222 ? 18.395  91.051 -49.703 1.00 30.01  ? 208  MET B CE    1 
ATOM   5689 N  N     . SER B 1 223 ? 24.832  91.545 -48.913 1.00 31.81  ? 209  SER B N     1 
ATOM   5690 C  CA    . SER B 1 223 ? 25.352  91.598 -47.549 1.00 32.85  ? 209  SER B CA    1 
ATOM   5691 C  C     . SER B 1 223 ? 26.600  92.473 -47.475 1.00 33.44  ? 209  SER B C     1 
ATOM   5692 O  O     . SER B 1 223 ? 27.540  92.289 -48.253 1.00 34.33  ? 209  SER B O     1 
ATOM   5693 C  CB    . SER B 1 223 ? 25.688  90.197 -47.049 1.00 31.52  ? 209  SER B CB    1 
ATOM   5694 O  OG    . SER B 1 223 ? 26.146  90.258 -45.707 1.00 29.39  ? 209  SER B OG    1 
ATOM   5695 N  N     . LYS B 1 224 ? 26.585  93.471 -46.589 1.00 34.12  ? 210  LYS B N     1 
ATOM   5696 C  CA    . LYS B 1 224 ? 27.818  94.201 -46.299 1.00 35.58  ? 210  LYS B CA    1 
ATOM   5697 C  C     . LYS B 1 224 ? 28.772  93.334 -45.481 1.00 34.94  ? 210  LYS B C     1 
ATOM   5698 O  O     . LYS B 1 224 ? 29.967  93.237 -45.788 1.00 35.53  ? 210  LYS B O     1 
ATOM   5699 C  CB    . LYS B 1 224 ? 27.515  95.501 -45.553 1.00 39.61  ? 210  LYS B CB    1 
ATOM   5700 C  CG    . LYS B 1 224 ? 26.452  96.388 -46.184 1.00 49.64  ? 210  LYS B CG    1 
ATOM   5701 C  CD    . LYS B 1 224 ? 27.023  97.238 -47.309 1.00 52.82  ? 210  LYS B CD    1 
ATOM   5702 C  CE    . LYS B 1 224 ? 26.019  98.293 -47.760 1.00 55.91  ? 210  LYS B CE    1 
ATOM   5703 N  NZ    . LYS B 1 224 ? 25.875  99.392 -46.759 1.00 58.37  ? 210  LYS B NZ    1 
ATOM   5704 N  N     . ARG B 1 225 ? 28.261  92.719 -44.415 1.00 32.63  ? 211  ARG B N     1 
ATOM   5705 C  CA    . ARG B 1 225 ? 29.028  91.790 -43.595 1.00 31.98  ? 211  ARG B CA    1 
ATOM   5706 C  C     . ARG B 1 225 ? 28.168  90.582 -43.251 1.00 30.47  ? 211  ARG B C     1 
ATOM   5707 O  O     . ARG B 1 225 ? 27.029  90.732 -42.804 1.00 30.14  ? 211  ARG B O     1 
ATOM   5708 C  CB    . ARG B 1 225 ? 29.521  92.467 -42.311 1.00 31.90  ? 211  ARG B CB    1 
ATOM   5709 C  CG    . ARG B 1 225 ? 30.477  91.623 -41.482 1.00 31.31  ? 211  ARG B CG    1 
ATOM   5710 C  CD    . ARG B 1 225 ? 31.124  92.462 -40.380 1.00 31.58  ? 211  ARG B CD    1 
ATOM   5711 N  NE    . ARG B 1 225 ? 30.210  92.778 -39.284 1.00 31.60  ? 211  ARG B NE    1 
ATOM   5712 C  CZ    . ARG B 1 225 ? 29.820  91.920 -38.345 1.00 32.62  ? 211  ARG B CZ    1 
ATOM   5713 N  NH1   . ARG B 1 225 ? 30.206  90.651 -38.359 1.00 31.39  ? 211  ARG B NH1   1 
ATOM   5714 N  NH2   . ARG B 1 225 ? 29.034  92.348 -37.358 1.00 31.01  ? 211  ARG B NH2   1 
ATOM   5715 N  N     . THR B 1 226 ? 28.721  89.392 -43.460 1.00 29.48  ? 212  THR B N     1 
ATOM   5716 C  CA    . THR B 1 226 ? 28.052  88.132 -43.183 1.00 28.95  ? 212  THR B CA    1 
ATOM   5717 C  C     . THR B 1 226 ? 28.788  87.410 -42.067 1.00 28.26  ? 212  THR B C     1 
ATOM   5718 O  O     . THR B 1 226 ? 30.016  87.480 -41.982 1.00 29.38  ? 212  THR B O     1 
ATOM   5719 C  CB    . THR B 1 226 ? 27.986  87.264 -44.436 1.00 28.02  ? 212  THR B CB    1 
ATOM   5720 O  OG1   . THR B 1 226 ? 27.153  87.928 -45.389 1.00 29.01  ? 212  THR B OG1   1 
ATOM   5721 C  CG2   . THR B 1 226 ? 27.398  85.887 -44.124 1.00 26.31  ? 212  THR B CG2   1 
ATOM   5722 N  N     . ALA B 1 227 ? 28.033  86.768 -41.176 1.00 27.56  ? 213  ALA B N     1 
ATOM   5723 C  CA    . ALA B 1 227 ? 28.617  85.994 -40.094 1.00 26.25  ? 213  ALA B CA    1 
ATOM   5724 C  C     . ALA B 1 227 ? 28.119  84.556 -40.150 1.00 25.54  ? 213  ALA B C     1 
ATOM   5725 O  O     . ALA B 1 227 ? 27.040  84.259 -40.671 1.00 24.15  ? 213  ALA B O     1 
ATOM   5726 C  CB    . ALA B 1 227 ? 28.297  86.612 -38.725 1.00 26.50  ? 213  ALA B CB    1 
ATOM   5727 N  N     . LEU B 1 228 ? 28.902  83.660 -39.566 1.00 26.93  ? 214  LEU B N     1 
ATOM   5728 C  CA    . LEU B 1 228 ? 28.611  82.233 -39.606 1.00 25.37  ? 214  LEU B CA    1 
ATOM   5729 C  C     . LEU B 1 228 ? 28.388  81.729 -38.190 1.00 25.41  ? 214  LEU B C     1 
ATOM   5730 O  O     . LEU B 1 228 ? 29.269  81.853 -37.340 1.00 25.48  ? 214  LEU B O     1 
ATOM   5731 C  CB    . LEU B 1 228 ? 29.759  81.480 -40.277 1.00 25.10  ? 214  LEU B CB    1 
ATOM   5732 C  CG    . LEU B 1 228 ? 29.724  79.960 -40.278 1.00 28.06  ? 214  LEU B CG    1 
ATOM   5733 C  CD1   . LEU B 1 228 ? 28.483  79.500 -40.956 1.00 26.07  ? 214  LEU B CD1   1 
ATOM   5734 C  CD2   . LEU B 1 228 ? 30.938  79.448 -41.024 1.00 26.78  ? 214  LEU B CD2   1 
ATOM   5735 N  N     . LEU B 1 229 ? 27.212  81.163 -37.938 1.00 24.40  ? 215  LEU B N     1 
ATOM   5736 C  CA    . LEU B 1 229 ? 26.877  80.561 -36.653 1.00 23.06  ? 215  LEU B CA    1 
ATOM   5737 C  C     . LEU B 1 229 ? 26.561  79.090 -36.903 1.00 24.80  ? 215  LEU B C     1 
ATOM   5738 O  O     . LEU B 1 229 ? 25.564  78.774 -37.562 1.00 21.57  ? 215  LEU B O     1 
ATOM   5739 C  CB    . LEU B 1 229 ? 25.699  81.283 -35.995 1.00 22.77  ? 215  LEU B CB    1 
ATOM   5740 C  CG    . LEU B 1 229 ? 25.277  80.765 -34.610 1.00 24.13  ? 215  LEU B CG    1 
ATOM   5741 C  CD1   . LEU B 1 229 ? 26.367  80.989 -33.569 1.00 23.24  ? 215  LEU B CD1   1 
ATOM   5742 C  CD2   . LEU B 1 229 ? 23.935  81.362 -34.166 1.00 25.11  ? 215  LEU B CD2   1 
ATOM   5743 N  N     . ALA B 1 230 ? 27.425  78.194 -36.414 1.00 21.03  ? 216  ALA B N     1 
ATOM   5744 C  CA    . ALA B 1 230 ? 27.261  76.762 -36.613 1.00 20.54  ? 216  ALA B CA    1 
ATOM   5745 C  C     . ALA B 1 230 ? 27.112  76.061 -35.267 1.00 24.01  ? 216  ALA B C     1 
ATOM   5746 O  O     . ALA B 1 230 ? 27.681  76.496 -34.261 1.00 19.06  ? 216  ALA B O     1 
ATOM   5747 C  CB    . ALA B 1 230 ? 28.447  76.169 -37.386 1.00 21.43  ? 216  ALA B CB    1 
ATOM   5748 N  N     . ASP B 1 231 ? 26.350  74.973 -35.247 1.00 22.18  ? 217  ASP B N     1 
ATOM   5749 C  CA    . ASP B 1 231 ? 26.145  74.232 -34.004 1.00 20.79  ? 217  ASP B CA    1 
ATOM   5750 C  C     . ASP B 1 231 ? 26.054  72.738 -34.273 1.00 19.92  ? 217  ASP B C     1 
ATOM   5751 O  O     . ASP B 1 231 ? 26.490  72.242 -35.316 1.00 18.21  ? 217  ASP B O     1 
ATOM   5752 C  CB    . ASP B 1 231 ? 24.946  74.755 -33.210 1.00 20.47  ? 217  ASP B CB    1 
ATOM   5753 C  CG    . ASP B 1 231 ? 25.168  74.624 -31.704 1.00 22.49  ? 217  ASP B CG    1 
ATOM   5754 O  OD1   . ASP B 1 231 ? 26.080  75.289 -31.152 1.00 21.27  ? 217  ASP B OD1   1 
ATOM   5755 O  OD2   . ASP B 1 231 ? 24.404  73.859 -31.077 1.00 22.31  ? 217  ASP B OD2   1 
ATOM   5756 N  N     . PHE B 1 232 ? 25.526  72.027 -33.266 1.00 19.85  ? 218  PHE B N     1 
ATOM   5757 C  CA    . PHE B 1 232 ? 25.783  70.601 -33.061 1.00 20.09  ? 218  PHE B CA    1 
ATOM   5758 C  C     . PHE B 1 232 ? 25.384  69.703 -34.229 1.00 20.79  ? 218  PHE B C     1 
ATOM   5759 O  O     . PHE B 1 232 ? 25.954  68.615 -34.381 1.00 20.42  ? 218  PHE B O     1 
ATOM   5760 C  CB    . PHE B 1 232 ? 25.120  70.173 -31.752 1.00 19.74  ? 218  PHE B CB    1 
ATOM   5761 C  CG    . PHE B 1 232 ? 23.646  69.897 -31.876 1.00 20.98  ? 218  PHE B CG    1 
ATOM   5762 C  CD1   . PHE B 1 232 ? 22.747  70.952 -31.745 1.00 19.13  ? 218  PHE B CD1   1 
ATOM   5763 C  CD2   . PHE B 1 232 ? 23.156  68.624 -32.101 1.00 19.26  ? 218  PHE B CD2   1 
ATOM   5764 C  CE1   . PHE B 1 232 ? 21.384  70.751 -31.833 1.00 20.79  ? 218  PHE B CE1   1 
ATOM   5765 C  CE2   . PHE B 1 232 ? 21.783  68.407 -32.179 1.00 19.08  ? 218  PHE B CE2   1 
ATOM   5766 C  CZ    . PHE B 1 232 ? 20.900  69.470 -32.053 1.00 20.29  ? 218  PHE B CZ    1 
ATOM   5767 N  N     . LEU B 1 233 ? 24.378  70.075 -35.021 1.00 19.68  ? 219  LEU B N     1 
ATOM   5768 C  CA    . LEU B 1 233 ? 24.035  69.197 -36.133 1.00 20.41  ? 219  LEU B CA    1 
ATOM   5769 C  C     . LEU B 1 233 ? 25.207  69.070 -37.112 1.00 21.20  ? 219  LEU B C     1 
ATOM   5770 O  O     . LEU B 1 233 ? 25.393  68.014 -37.726 1.00 21.75  ? 219  LEU B O     1 
ATOM   5771 C  CB    . LEU B 1 233 ? 22.751  69.697 -36.804 1.00 19.31  ? 219  LEU B CB    1 
ATOM   5772 C  CG    . LEU B 1 233 ? 21.538  69.398 -35.900 1.00 22.59  ? 219  LEU B CG    1 
ATOM   5773 C  CD1   . LEU B 1 233 ? 20.235  70.106 -36.329 1.00 20.99  ? 219  LEU B CD1   1 
ATOM   5774 C  CD2   . LEU B 1 233 ? 21.310  67.898 -35.771 1.00 20.90  ? 219  LEU B CD2   1 
ATOM   5775 N  N     . VAL B 1 234 ? 26.047  70.108 -37.216 1.00 20.19  ? 220  VAL B N     1 
ATOM   5776 C  CA    . VAL B 1 234 ? 27.287  70.003 -37.986 1.00 20.87  ? 220  VAL B CA    1 
ATOM   5777 C  C     . VAL B 1 234 ? 28.144  68.858 -37.458 1.00 22.09  ? 220  VAL B C     1 
ATOM   5778 O  O     . VAL B 1 234 ? 28.744  68.095 -38.228 1.00 21.16  ? 220  VAL B O     1 
ATOM   5779 C  CB    . VAL B 1 234 ? 28.042  71.346 -37.945 1.00 21.10  ? 220  VAL B CB    1 
ATOM   5780 C  CG1   . VAL B 1 234 ? 29.497  71.174 -38.357 1.00 20.89  ? 220  VAL B CG1   1 
ATOM   5781 C  CG2   . VAL B 1 234 ? 27.333  72.387 -38.815 1.00 20.77  ? 220  VAL B CG2   1 
ATOM   5782 N  N     . LEU B 1 235 ? 28.238  68.736 -36.135 1.00 20.52  ? 221  LEU B N     1 
ATOM   5783 C  CA    . LEU B 1 235 ? 29.034  67.664 -35.550 1.00 22.57  ? 221  LEU B CA    1 
ATOM   5784 C  C     . LEU B 1 235 ? 28.438  66.302 -35.879 1.00 22.61  ? 221  LEU B C     1 
ATOM   5785 O  O     . LEU B 1 235 ? 29.148  65.385 -36.306 1.00 20.03  ? 221  LEU B O     1 
ATOM   5786 C  CB    . LEU B 1 235 ? 29.119  67.855 -34.038 1.00 20.07  ? 221  LEU B CB    1 
ATOM   5787 C  CG    . LEU B 1 235 ? 29.963  69.023 -33.532 1.00 19.84  ? 221  LEU B CG    1 
ATOM   5788 C  CD1   . LEU B 1 235 ? 29.785  69.142 -32.029 1.00 19.53  ? 221  LEU B CD1   1 
ATOM   5789 C  CD2   . LEU B 1 235 ? 31.448  68.905 -33.944 1.00 22.97  ? 221  LEU B CD2   1 
ATOM   5790 N  N     . ARG B 1 236 ? 27.119  66.160 -35.701 1.00 20.76  ? 222  ARG B N     1 
ATOM   5791 C  CA    . ARG B 1 236 ? 26.500  64.848 -35.831 1.00 23.06  ? 222  ARG B CA    1 
ATOM   5792 C  C     . ARG B 1 236 ? 26.576  64.321 -37.255 1.00 22.52  ? 222  ARG B C     1 
ATOM   5793 O  O     . ARG B 1 236 ? 26.721  63.108 -37.455 1.00 23.65  ? 222  ARG B O     1 
ATOM   5794 C  CB    . ARG B 1 236 ? 25.046  64.893 -35.355 1.00 20.79  ? 222  ARG B CB    1 
ATOM   5795 C  CG    . ARG B 1 236 ? 24.902  65.550 -34.012 1.00 20.28  ? 222  ARG B CG    1 
ATOM   5796 C  CD    . ARG B 1 236 ? 25.612  64.737 -32.926 1.00 20.11  ? 222  ARG B CD    1 
ATOM   5797 N  NE    . ARG B 1 236 ? 25.120  65.134 -31.615 1.00 21.38  ? 222  ARG B NE    1 
ATOM   5798 C  CZ    . ARG B 1 236 ? 25.841  65.809 -30.734 1.00 21.55  ? 222  ARG B CZ    1 
ATOM   5799 N  NH1   . ARG B 1 236 ? 27.121  66.080 -30.955 1.00 20.25  ? 222  ARG B NH1   1 
ATOM   5800 N  NH2   . ARG B 1 236 ? 25.260  66.242 -29.617 1.00 19.19  ? 222  ARG B NH2   1 
ATOM   5801 N  N     . HIS B 1 237 ? 26.487  65.202 -38.246 1.00 22.05  ? 223  HIS B N     1 
ATOM   5802 C  CA    . HIS B 1 237 ? 26.490  64.805 -39.647 1.00 23.75  ? 223  HIS B CA    1 
ATOM   5803 C  C     . HIS B 1 237 ? 27.876  64.876 -40.278 1.00 24.83  ? 223  HIS B C     1 
ATOM   5804 O  O     . HIS B 1 237 ? 27.988  64.882 -41.509 1.00 25.14  ? 223  HIS B O     1 
ATOM   5805 C  CB    . HIS B 1 237 ? 25.487  65.656 -40.420 1.00 22.73  ? 223  HIS B CB    1 
ATOM   5806 C  CG    . HIS B 1 237 ? 24.073  65.374 -40.040 1.00 24.99  ? 223  HIS B CG    1 
ATOM   5807 N  ND1   . HIS B 1 237 ? 23.268  64.518 -40.757 1.00 25.77  ? 223  HIS B ND1   1 
ATOM   5808 C  CD2   . HIS B 1 237 ? 23.340  65.776 -38.973 1.00 23.51  ? 223  HIS B CD2   1 
ATOM   5809 C  CE1   . HIS B 1 237 ? 22.086  64.435 -40.171 1.00 27.22  ? 223  HIS B CE1   1 
ATOM   5810 N  NE2   . HIS B 1 237 ? 22.102  65.190 -39.089 1.00 23.35  ? 223  HIS B NE2   1 
ATOM   5811 N  N     . GLY B 1 238 ? 28.927  64.942 -39.463 1.00 24.18  ? 224  GLY B N     1 
ATOM   5812 C  CA    . GLY B 1 238 ? 30.278  64.801 -39.970 1.00 24.39  ? 224  GLY B CA    1 
ATOM   5813 C  C     . GLY B 1 238 ? 30.786  65.978 -40.768 1.00 24.46  ? 224  GLY B C     1 
ATOM   5814 O  O     . GLY B 1 238 ? 31.588  65.788 -41.683 1.00 23.76  ? 224  GLY B O     1 
ATOM   5815 N  N     . LEU B 1 239 ? 30.314  67.188 -40.477 1.00 24.31  ? 225  LEU B N     1 
ATOM   5816 C  CA    . LEU B 1 239 ? 30.615  68.349 -41.307 1.00 23.85  ? 225  LEU B CA    1 
ATOM   5817 C  C     . LEU B 1 239 ? 31.546  69.334 -40.615 1.00 27.27  ? 225  LEU B C     1 
ATOM   5818 O  O     . LEU B 1 239 ? 31.712  70.464 -41.101 1.00 26.45  ? 225  LEU B O     1 
ATOM   5819 C  CB    . LEU B 1 239 ? 29.306  69.030 -41.718 1.00 23.40  ? 225  LEU B CB    1 
ATOM   5820 C  CG    . LEU B 1 239 ? 28.453  68.158 -42.657 1.00 23.63  ? 225  LEU B CG    1 
ATOM   5821 C  CD1   . LEU B 1 239 ? 26.988  68.589 -42.649 1.00 26.21  ? 225  LEU B CD1   1 
ATOM   5822 C  CD2   . LEU B 1 239 ? 28.992  68.202 -44.081 1.00 25.39  ? 225  LEU B CD2   1 
ATOM   5823 N  N     . LYS B 1 240 ? 32.175  68.920 -39.507 1.00 26.46  ? 226  LYS B N     1 
ATOM   5824 C  CA    . LYS B 1 240 ? 33.139  69.767 -38.802 1.00 27.86  ? 226  LYS B CA    1 
ATOM   5825 C  C     . LYS B 1 240 ? 34.227  70.291 -39.734 1.00 27.97  ? 226  LYS B C     1 
ATOM   5826 O  O     . LYS B 1 240 ? 34.507  71.494 -39.766 1.00 28.53  ? 226  LYS B O     1 
ATOM   5827 C  CB    . LYS B 1 240 ? 33.758  68.981 -37.634 1.00 25.24  ? 226  LYS B CB    1 
ATOM   5828 C  CG    . LYS B 1 240 ? 34.520  69.820 -36.611 1.00 29.54  ? 226  LYS B CG    1 
ATOM   5829 C  CD    . LYS B 1 240 ? 35.331  68.951 -35.616 1.00 28.80  ? 226  LYS B CD    1 
ATOM   5830 C  CE    . LYS B 1 240 ? 36.282  69.810 -34.761 1.00 35.43  ? 226  LYS B CE    1 
ATOM   5831 N  NZ    . LYS B 1 240 ? 37.136  69.061 -33.740 1.00 33.58  ? 226  LYS B NZ    1 
ATOM   5832 N  N     . HIS B 1 241 ? 34.870  69.399 -40.487 1.00 30.42  ? 227  HIS B N     1 
ATOM   5833 C  CA    . HIS B 1 241 ? 35.963  69.833 -41.350 1.00 33.43  ? 227  HIS B CA    1 
ATOM   5834 C  C     . HIS B 1 241 ? 35.462  70.768 -42.442 1.00 33.40  ? 227  HIS B C     1 
ATOM   5835 O  O     . HIS B 1 241 ? 36.154  71.725 -42.816 1.00 34.72  ? 227  HIS B O     1 
ATOM   5836 C  CB    . HIS B 1 241 ? 36.680  68.628 -41.961 1.00 39.21  ? 227  HIS B CB    1 
ATOM   5837 C  CG    . HIS B 1 241 ? 37.647  68.989 -43.052 1.00 55.94  ? 227  HIS B CG    1 
ATOM   5838 N  ND1   . HIS B 1 241 ? 38.495  70.075 -42.975 1.00 61.26  ? 227  HIS B ND1   1 
ATOM   5839 C  CD2   . HIS B 1 241 ? 37.876  68.423 -44.263 1.00 59.58  ? 227  HIS B CD2   1 
ATOM   5840 C  CE1   . HIS B 1 241 ? 39.215  70.151 -44.081 1.00 53.14  ? 227  HIS B CE1   1 
ATOM   5841 N  NE2   . HIS B 1 241 ? 38.857  69.162 -44.880 1.00 54.28  ? 227  HIS B NE2   1 
ATOM   5842 N  N     . ALA B 1 242 ? 34.257  70.517 -42.960 1.00 30.52  ? 228  ALA B N     1 
ATOM   5843 C  CA    . ALA B 1 242 ? 33.697  71.412 -43.971 1.00 30.00  ? 228  ALA B CA    1 
ATOM   5844 C  C     . ALA B 1 242 ? 33.489  72.814 -43.409 1.00 27.85  ? 228  ALA B C     1 
ATOM   5845 O  O     . ALA B 1 242 ? 33.749  73.812 -44.094 1.00 29.20  ? 228  ALA B O     1 
ATOM   5846 C  CB    . ALA B 1 242 ? 32.388  70.842 -44.521 1.00 27.53  ? 228  ALA B CB    1 
ATOM   5847 N  N     . LEU B 1 243 ? 33.012  72.912 -42.165 1.00 27.51  ? 229  LEU B N     1 
ATOM   5848 C  CA    . LEU B 1 243 ? 32.813  74.227 -41.561 1.00 27.37  ? 229  LEU B CA    1 
ATOM   5849 C  C     . LEU B 1 243 ? 34.141  74.924 -41.269 1.00 28.72  ? 229  LEU B C     1 
ATOM   5850 O  O     . LEU B 1 243 ? 34.255  76.143 -41.443 1.00 28.09  ? 229  LEU B O     1 
ATOM   5851 C  CB    . LEU B 1 243 ? 31.985  74.112 -40.279 1.00 24.03  ? 229  LEU B CB    1 
ATOM   5852 C  CG    . LEU B 1 243 ? 30.476  74.235 -40.481 1.00 23.45  ? 229  LEU B CG    1 
ATOM   5853 C  CD1   . LEU B 1 243 ? 30.130  75.706 -40.738 1.00 23.62  ? 229  LEU B CD1   1 
ATOM   5854 C  CD2   . LEU B 1 243 ? 29.935  73.325 -41.594 1.00 23.28  ? 229  LEU B CD2   1 
ATOM   5855 N  N     . GLN B 1 244 ? 35.152  74.178 -40.817 1.00 26.87  ? 230  GLN B N     1 
ATOM   5856 C  CA    . GLN B 1 244 ? 36.461  74.781 -40.582 1.00 28.95  ? 230  GLN B CA    1 
ATOM   5857 C  C     . GLN B 1 244 ? 37.077  75.291 -41.880 1.00 30.15  ? 230  GLN B C     1 
ATOM   5858 O  O     . GLN B 1 244 ? 37.577  76.421 -41.939 1.00 30.32  ? 230  GLN B O     1 
ATOM   5859 C  CB    . GLN B 1 244 ? 37.397  73.771 -39.913 1.00 31.11  ? 230  GLN B CB    1 
ATOM   5860 C  CG    . GLN B 1 244 ? 36.948  73.323 -38.545 1.00 31.21  ? 230  GLN B CG    1 
ATOM   5861 C  CD    . GLN B 1 244 ? 37.848  72.255 -37.958 1.00 33.64  ? 230  GLN B CD    1 
ATOM   5862 O  OE1   . GLN B 1 244 ? 38.449  71.462 -38.687 1.00 34.43  ? 230  GLN B OE1   1 
ATOM   5863 N  NE2   . GLN B 1 244 ? 37.935  72.218 -36.629 1.00 33.11  ? 230  GLN B NE2   1 
ATOM   5864 N  N     . LYS B 1 245 ? 37.030  74.482 -42.944 1.00 32.53  ? 231  LYS B N     1 
ATOM   5865 C  CA    . LYS B 1 245 ? 37.626  74.911 -44.210 1.00 32.97  ? 231  LYS B CA    1 
ATOM   5866 C  C     . LYS B 1 245 ? 36.891  76.116 -44.790 1.00 33.16  ? 231  LYS B C     1 
ATOM   5867 O  O     . LYS B 1 245 ? 37.513  76.987 -45.413 1.00 33.83  ? 231  LYS B O     1 
ATOM   5868 C  CB    . LYS B 1 245 ? 37.648  73.750 -45.206 1.00 33.80  ? 231  LYS B CB    1 
ATOM   5869 C  CG    . LYS B 1 245 ? 38.341  74.109 -46.520 1.00 37.26  ? 231  LYS B CG    1 
ATOM   5870 C  CD    . LYS B 1 245 ? 38.757  72.879 -47.316 1.00 38.93  ? 231  LYS B CD    1 
ATOM   5871 C  CE    . LYS B 1 245 ? 38.592  73.106 -48.810 1.00 40.79  ? 231  LYS B CE    1 
ATOM   5872 N  NZ    . LYS B 1 245 ? 39.575  74.087 -49.312 1.00 39.31  ? 231  LYS B NZ    1 
ATOM   5873 N  N     . TRP B 1 246 ? 35.575  76.183 -44.571 1.00 31.70  ? 232  TRP B N     1 
ATOM   5874 C  CA    . TRP B 1 246 ? 34.765  77.310 -45.024 1.00 29.60  ? 232  TRP B CA    1 
ATOM   5875 C  C     . TRP B 1 246 ? 35.301  78.632 -44.479 1.00 31.33  ? 232  TRP B C     1 
ATOM   5876 O  O     . TRP B 1 246 ? 35.582  79.561 -45.247 1.00 31.02  ? 232  TRP B O     1 
ATOM   5877 C  CB    . TRP B 1 246 ? 33.315  77.064 -44.590 1.00 27.85  ? 232  TRP B CB    1 
ATOM   5878 C  CG    . TRP B 1 246 ? 32.277  78.037 -45.056 1.00 25.44  ? 232  TRP B CG    1 
ATOM   5879 C  CD1   . TRP B 1 246 ? 32.469  79.198 -45.749 1.00 27.30  ? 232  TRP B CD1   1 
ATOM   5880 C  CD2   . TRP B 1 246 ? 30.863  77.920 -44.853 1.00 25.00  ? 232  TRP B CD2   1 
ATOM   5881 N  NE1   . TRP B 1 246 ? 31.256  79.811 -45.995 1.00 26.76  ? 232  TRP B NE1   1 
ATOM   5882 C  CE2   . TRP B 1 246 ? 30.256  79.040 -45.457 1.00 26.78  ? 232  TRP B CE2   1 
ATOM   5883 C  CE3   . TRP B 1 246 ? 30.049  76.964 -44.237 1.00 24.78  ? 232  TRP B CE3   1 
ATOM   5884 C  CZ2   . TRP B 1 246 ? 28.875  79.237 -45.443 1.00 25.30  ? 232  TRP B CZ2   1 
ATOM   5885 C  CZ3   . TRP B 1 246 ? 28.682  77.158 -44.224 1.00 23.20  ? 232  TRP B CZ3   1 
ATOM   5886 C  CH2   . TRP B 1 246 ? 28.106  78.286 -44.825 1.00 24.52  ? 232  TRP B CH2   1 
ATOM   5887 N  N     . VAL B 1 247 ? 35.493  78.725 -43.157 1.00 30.28  ? 233  VAL B N     1 
ATOM   5888 C  CA    . VAL B 1 247 ? 35.932  79.994 -42.582 1.00 29.96  ? 233  VAL B CA    1 
ATOM   5889 C  C     . VAL B 1 247 ? 37.408  80.227 -42.853 1.00 32.95  ? 233  VAL B C     1 
ATOM   5890 O  O     . VAL B 1 247 ? 37.871  81.372 -42.824 1.00 32.41  ? 233  VAL B O     1 
ATOM   5891 C  CB    . VAL B 1 247 ? 35.706  80.086 -41.063 1.00 30.12  ? 233  VAL B CB    1 
ATOM   5892 C  CG1   . VAL B 1 247 ? 34.291  79.716 -40.705 1.00 29.48  ? 233  VAL B CG1   1 
ATOM   5893 C  CG2   . VAL B 1 247 ? 36.692  79.208 -40.316 1.00 30.64  ? 233  VAL B CG2   1 
ATOM   5894 N  N     . LYS B 1 248 ? 38.154  79.171 -43.149 1.00 32.95  ? 234  LYS B N     1 
ATOM   5895 C  CA    . LYS B 1 248 ? 39.524  79.358 -43.598 1.00 35.72  ? 234  LYS B CA    1 
ATOM   5896 C  C     . LYS B 1 248 ? 39.547  79.963 -44.997 1.00 35.33  ? 234  LYS B C     1 
ATOM   5897 O  O     . LYS B 1 248 ? 40.259  80.939 -45.251 1.00 35.77  ? 234  LYS B O     1 
ATOM   5898 C  CB    . LYS B 1 248 ? 40.255  78.019 -43.562 1.00 37.32  ? 234  LYS B CB    1 
ATOM   5899 C  CG    . LYS B 1 248 ? 41.744  78.115 -43.788 1.00 39.10  ? 234  LYS B CG    1 
ATOM   5900 C  CD    . LYS B 1 248 ? 42.047  77.825 -45.246 1.00 53.09  ? 234  LYS B CD    1 
ATOM   5901 C  CE    . LYS B 1 248 ? 42.467  76.382 -45.481 1.00 51.99  ? 234  LYS B CE    1 
ATOM   5902 N  NZ    . LYS B 1 248 ? 42.338  76.032 -46.934 1.00 50.56  ? 234  LYS B NZ    1 
ATOM   5903 N  N     . ASP B 1 249 ? 38.739  79.421 -45.911 1.00 36.28  ? 235  ASP B N     1 
ATOM   5904 C  CA    . ASP B 1 249 ? 38.710  79.954 -47.268 1.00 35.11  ? 235  ASP B CA    1 
ATOM   5905 C  C     . ASP B 1 249 ? 37.985  81.292 -47.330 1.00 36.64  ? 235  ASP B C     1 
ATOM   5906 O  O     . ASP B 1 249 ? 38.310  82.138 -48.174 1.00 35.63  ? 235  ASP B O     1 
ATOM   5907 C  CB    . ASP B 1 249 ? 38.049  78.946 -48.208 1.00 36.13  ? 235  ASP B CB    1 
ATOM   5908 C  CG    . ASP B 1 249 ? 38.876  77.697 -48.387 1.00 37.89  ? 235  ASP B CG    1 
ATOM   5909 O  OD1   . ASP B 1 249 ? 40.047  77.713 -47.954 1.00 38.84  ? 235  ASP B OD1   1 
ATOM   5910 O  OD2   . ASP B 1 249 ? 38.358  76.701 -48.942 1.00 37.79  ? 235  ASP B OD2   1 
ATOM   5911 N  N     . VAL B 1 250 ? 37.007  81.501 -46.455 1.00 34.61  ? 236  VAL B N     1 
ATOM   5912 C  CA    . VAL B 1 250 ? 36.218  82.730 -46.447 1.00 35.32  ? 236  VAL B CA    1 
ATOM   5913 C  C     . VAL B 1 250 ? 36.226  83.319 -45.040 1.00 35.20  ? 236  VAL B C     1 
ATOM   5914 O  O     . VAL B 1 250 ? 35.274  83.093 -44.272 1.00 33.72  ? 236  VAL B O     1 
ATOM   5915 C  CB    . VAL B 1 250 ? 34.780  82.465 -46.926 1.00 35.16  ? 236  VAL B CB    1 
ATOM   5916 C  CG1   . VAL B 1 250 ? 34.036  83.744 -47.014 1.00 40.06  ? 236  VAL B CG1   1 
ATOM   5917 C  CG2   . VAL B 1 250 ? 34.774  81.779 -48.285 1.00 34.88  ? 236  VAL B CG2   1 
ATOM   5918 N  N     . PRO B 1 251 ? 37.259  84.072 -44.658 1.00 34.89  ? 237  PRO B N     1 
ATOM   5919 C  CA    . PRO B 1 251 ? 37.302  84.641 -43.304 1.00 36.74  ? 237  PRO B CA    1 
ATOM   5920 C  C     . PRO B 1 251 ? 36.095  85.523 -43.012 1.00 37.75  ? 237  PRO B C     1 
ATOM   5921 O  O     . PRO B 1 251 ? 35.736  86.394 -43.804 1.00 40.15  ? 237  PRO B O     1 
ATOM   5922 C  CB    . PRO B 1 251 ? 38.598  85.461 -43.313 1.00 40.95  ? 237  PRO B CB    1 
ATOM   5923 C  CG    . PRO B 1 251 ? 39.445  84.808 -44.353 1.00 36.37  ? 237  PRO B CG    1 
ATOM   5924 C  CD    . PRO B 1 251 ? 38.475  84.401 -45.425 1.00 37.74  ? 237  PRO B CD    1 
ATOM   5925 N  N     . MET B 1 252 ? 35.503  85.325 -41.838 1.00 33.98  ? 238  MET B N     1 
ATOM   5926 C  CA    . MET B 1 252 ? 34.379  86.136 -41.382 1.00 34.13  ? 238  MET B CA    1 
ATOM   5927 C  C     . MET B 1 252 ? 34.172  85.858 -39.905 1.00 32.87  ? 238  MET B C     1 
ATOM   5928 O  O     . MET B 1 252 ? 34.667  84.862 -39.366 1.00 31.39  ? 238  MET B O     1 
ATOM   5929 C  CB    . MET B 1 252 ? 33.059  85.836 -42.119 1.00 33.60  ? 238  MET B CB    1 
ATOM   5930 C  CG    . MET B 1 252 ? 32.770  84.355 -42.368 1.00 33.86  ? 238  MET B CG    1 
ATOM   5931 S  SD    . MET B 1 252 ? 31.269  84.045 -43.355 1.00 30.90  ? 238  MET B SD    1 
ATOM   5932 C  CE    . MET B 1 252 ? 31.237  82.263 -43.290 1.00 29.50  ? 238  MET B CE    1 
ATOM   5933 N  N     . ALA B 1 253 ? 33.415  86.744 -39.265 1.00 29.93  ? 239  ALA B N     1 
ATOM   5934 C  CA    . ALA B 1 253 ? 33.009  86.507 -37.889 1.00 28.49  ? 239  ALA B CA    1 
ATOM   5935 C  C     . ALA B 1 253 ? 32.222  85.208 -37.822 1.00 29.69  ? 239  ALA B C     1 
ATOM   5936 O  O     . ALA B 1 253 ? 31.362  84.941 -38.671 1.00 27.29  ? 239  ALA B O     1 
ATOM   5937 C  CB    . ALA B 1 253 ? 32.163  87.669 -37.372 1.00 28.33  ? 239  ALA B CB    1 
ATOM   5938 N  N     . HIS B 1 254 ? 32.540  84.379 -36.832 1.00 28.74  ? 240  HIS B N     1 
ATOM   5939 C  CA    . HIS B 1 254 ? 31.849  83.110 -36.691 1.00 27.49  ? 240  HIS B CA    1 
ATOM   5940 C  C     . HIS B 1 254 ? 31.804  82.707 -35.225 1.00 25.76  ? 240  HIS B C     1 
ATOM   5941 O  O     . HIS B 1 254 ? 32.611  83.158 -34.407 1.00 26.66  ? 240  HIS B O     1 
ATOM   5942 C  CB    . HIS B 1 254 ? 32.507  82.016 -37.548 1.00 26.59  ? 240  HIS B CB    1 
ATOM   5943 C  CG    . HIS B 1 254 ? 33.976  81.853 -37.306 1.00 27.65  ? 240  HIS B CG    1 
ATOM   5944 N  ND1   . HIS B 1 254 ? 34.907  82.800 -37.680 1.00 29.78  ? 240  HIS B ND1   1 
ATOM   5945 C  CD2   . HIS B 1 254 ? 34.676  80.837 -36.748 1.00 27.50  ? 240  HIS B CD2   1 
ATOM   5946 C  CE1   . HIS B 1 254 ? 36.115  82.377 -37.349 1.00 30.55  ? 240  HIS B CE1   1 
ATOM   5947 N  NE2   . HIS B 1 254 ? 36.001  81.189 -36.783 1.00 26.56  ? 240  HIS B NE2   1 
ATOM   5948 N  N     . ALA B 1 255 ? 30.861  81.824 -34.910 1.00 26.08  ? 241  ALA B N     1 
ATOM   5949 C  CA    . ALA B 1 255 ? 30.678  81.353 -33.545 1.00 23.49  ? 241  ALA B CA    1 
ATOM   5950 C  C     . ALA B 1 255 ? 29.972  80.011 -33.567 1.00 23.89  ? 241  ALA B C     1 
ATOM   5951 O  O     . ALA B 1 255 ? 29.450  79.570 -34.593 1.00 23.52  ? 241  ALA B O     1 
ATOM   5952 C  CB    . ALA B 1 255 ? 29.872  82.351 -32.709 1.00 23.63  ? 241  ALA B CB    1 
ATOM   5953 N  N     . THR B 1 256 ? 29.968  79.361 -32.411 1.00 23.91  ? 242  THR B N     1 
ATOM   5954 C  CA    . THR B 1 256 ? 29.040  78.284 -32.146 1.00 22.56  ? 242  THR B CA    1 
ATOM   5955 C  C     . THR B 1 256 ? 28.187  78.688 -30.956 1.00 22.98  ? 242  THR B C     1 
ATOM   5956 O  O     . THR B 1 256 ? 28.368  79.756 -30.365 1.00 22.91  ? 242  THR B O     1 
ATOM   5957 C  CB    . THR B 1 256 ? 29.748  76.947 -31.860 1.00 24.00  ? 242  THR B CB    1 
ATOM   5958 O  OG1   . THR B 1 256 ? 30.173  76.898 -30.485 1.00 22.65  ? 242  THR B OG1   1 
ATOM   5959 C  CG2   . THR B 1 256 ? 30.946  76.740 -32.785 1.00 23.07  ? 242  THR B CG2   1 
ATOM   5960 N  N     . MET B 1 257 ? 27.234  77.834 -30.630 1.00 21.94  ? 243  MET B N     1 
ATOM   5961 C  CA    . MET B 1 257 ? 26.528  77.907 -29.368 1.00 22.56  ? 243  MET B CA    1 
ATOM   5962 C  C     . MET B 1 257 ? 27.103  76.811 -28.471 1.00 21.22  ? 243  MET B C     1 
ATOM   5963 O  O     . MET B 1 257 ? 28.004  76.070 -28.870 1.00 17.31  ? 243  MET B O     1 
ATOM   5964 C  CB    . MET B 1 257 ? 25.019  77.766 -29.613 1.00 22.87  ? 243  MET B CB    1 
ATOM   5965 C  CG    . MET B 1 257 ? 24.381  79.054 -30.148 1.00 22.87  ? 243  MET B CG    1 
ATOM   5966 S  SD    . MET B 1 257 ? 22.584  78.956 -30.384 1.00 24.94  ? 243  MET B SD    1 
ATOM   5967 C  CE    . MET B 1 257 ? 22.493  78.038 -31.920 1.00 22.57  ? 243  MET B CE    1 
ATOM   5968 N  N     . LEU B 1 258 ? 26.566  76.681 -27.254 1.00 21.74  ? 244  LEU B N     1 
ATOM   5969 C  CA    . LEU B 1 258 ? 27.150  75.738 -26.301 1.00 22.51  ? 244  LEU B CA    1 
ATOM   5970 C  C     . LEU B 1 258 ? 27.202  74.317 -26.858 1.00 21.99  ? 244  LEU B C     1 
ATOM   5971 O  O     . LEU B 1 258 ? 28.220  73.626 -26.708 1.00 21.47  ? 244  LEU B O     1 
ATOM   5972 C  CB    . LEU B 1 258 ? 26.374  75.769 -24.983 1.00 22.17  ? 244  LEU B CB    1 
ATOM   5973 C  CG    . LEU B 1 258 ? 26.838  74.826 -23.872 1.00 23.12  ? 244  LEU B CG    1 
ATOM   5974 C  CD1   . LEU B 1 258 ? 28.357  74.869 -23.657 1.00 22.70  ? 244  LEU B CD1   1 
ATOM   5975 C  CD2   . LEU B 1 258 ? 26.089  75.118 -22.571 1.00 24.78  ? 244  LEU B CD2   1 
ATOM   5976 N  N     . MET B 1 259 ? 26.129  73.864 -27.517 1.00 20.75  ? 245  MET B N     1 
ATOM   5977 C  CA    . MET B 1 259 ? 26.059  72.461 -27.934 1.00 22.58  ? 245  MET B CA    1 
ATOM   5978 C  C     . MET B 1 259 ? 27.126  72.109 -28.959 1.00 22.84  ? 245  MET B C     1 
ATOM   5979 O  O     . MET B 1 259 ? 27.702  71.014 -28.916 1.00 24.30  ? 245  MET B O     1 
ATOM   5980 C  CB    . MET B 1 259 ? 24.690  72.143 -28.530 1.00 23.74  ? 245  MET B CB    1 
ATOM   5981 C  CG    . MET B 1 259 ? 23.649  71.779 -27.548 1.00 22.95  ? 245  MET B CG    1 
ATOM   5982 S  SD    . MET B 1 259 ? 22.075  71.425 -28.303 1.00 25.83  ? 245  MET B SD    1 
ATOM   5983 C  CE    . MET B 1 259 ? 22.081  69.638 -28.468 1.00 20.56  ? 245  MET B CE    1 
ATOM   5984 N  N     . GLY B 1 260 ? 27.391  73.005 -29.897 1.00 21.82  ? 246  GLY B N     1 
ATOM   5985 C  CA    . GLY B 1 260 ? 28.309  72.725 -30.978 1.00 22.15  ? 246  GLY B CA    1 
ATOM   5986 C  C     . GLY B 1 260 ? 29.711  73.206 -30.738 1.00 21.73  ? 246  GLY B C     1 
ATOM   5987 O  O     . GLY B 1 260 ? 30.549  73.102 -31.642 1.00 21.55  ? 246  GLY B O     1 
ATOM   5988 N  N     . LYS B 1 261 ? 29.995  73.733 -29.546 1.00 23.38  ? 247  LYS B N     1 
ATOM   5989 C  CA    . LYS B 1 261 ? 31.335  74.179 -29.214 1.00 23.82  ? 247  LYS B CA    1 
ATOM   5990 C  C     . LYS B 1 261 ? 32.338  73.061 -29.509 1.00 23.63  ? 247  LYS B C     1 
ATOM   5991 O  O     . LYS B 1 261 ? 32.059  71.879 -29.300 1.00 23.52  ? 247  LYS B O     1 
ATOM   5992 C  CB    . LYS B 1 261 ? 31.357  74.618 -27.740 1.00 23.73  ? 247  LYS B CB    1 
ATOM   5993 C  CG    . LYS B 1 261 ? 32.691  74.767 -27.138 1.00 25.44  ? 247  LYS B CG    1 
ATOM   5994 C  CD    . LYS B 1 261 ? 32.609  75.411 -25.754 1.00 26.52  ? 247  LYS B CD    1 
ATOM   5995 C  CE    . LYS B 1 261 ? 32.560  76.895 -25.888 1.00 29.02  ? 247  LYS B CE    1 
ATOM   5996 N  NZ    . LYS B 1 261 ? 33.920  77.495 -25.864 1.00 25.64  ? 247  LYS B NZ    1 
ATOM   5997 N  N     . GLY B 1 262 ? 33.486  73.429 -30.062 1.00 26.28  ? 248  GLY B N     1 
ATOM   5998 C  CA    . GLY B 1 262 ? 34.425  72.455 -30.576 1.00 24.03  ? 248  GLY B CA    1 
ATOM   5999 C  C     . GLY B 1 262 ? 34.442  72.332 -32.091 1.00 25.64  ? 248  GLY B C     1 
ATOM   6000 O  O     . GLY B 1 262 ? 35.400  71.772 -32.639 1.00 26.08  ? 248  GLY B O     1 
ATOM   6001 N  N     . ILE B 1 263 ? 33.443  72.879 -32.787 1.00 24.23  ? 249  ILE B N     1 
ATOM   6002 C  CA    . ILE B 1 263 ? 33.471  72.883 -34.249 1.00 23.64  ? 249  ILE B CA    1 
ATOM   6003 C  C     . ILE B 1 263 ? 34.681  73.659 -34.752 1.00 26.40  ? 249  ILE B C     1 
ATOM   6004 O  O     . ILE B 1 263 ? 35.359  73.249 -35.707 1.00 25.77  ? 249  ILE B O     1 
ATOM   6005 C  CB    . ILE B 1 263 ? 32.160  73.469 -34.801 1.00 23.23  ? 249  ILE B CB    1 
ATOM   6006 C  CG1   . ILE B 1 263 ? 31.044  72.425 -34.755 1.00 24.17  ? 249  ILE B CG1   1 
ATOM   6007 C  CG2   . ILE B 1 263 ? 32.338  73.963 -36.232 1.00 22.45  ? 249  ILE B CG2   1 
ATOM   6008 C  CD1   . ILE B 1 263 ? 29.653  73.014 -34.989 1.00 20.00  ? 249  ILE B CD1   1 
ATOM   6009 N  N     . PHE B 1 264 ? 34.987  74.776 -34.102 1.00 24.44  ? 250  PHE B N     1 
ATOM   6010 C  CA    . PHE B 1 264 ? 36.024  75.685 -34.551 1.00 24.96  ? 250  PHE B CA    1 
ATOM   6011 C  C     . PHE B 1 264 ? 37.202  75.716 -33.592 1.00 26.83  ? 250  PHE B C     1 
ATOM   6012 O  O     . PHE B 1 264 ? 37.057  75.495 -32.380 1.00 26.60  ? 250  PHE B O     1 
ATOM   6013 C  CB    . PHE B 1 264 ? 35.485  77.107 -34.698 1.00 25.07  ? 250  PHE B CB    1 
ATOM   6014 C  CG    . PHE B 1 264 ? 34.427  77.264 -35.755 1.00 24.26  ? 250  PHE B CG    1 
ATOM   6015 C  CD1   . PHE B 1 264 ? 34.745  77.137 -37.107 1.00 25.10  ? 250  PHE B CD1   1 
ATOM   6016 C  CD2   . PHE B 1 264 ? 33.115  77.567 -35.402 1.00 24.45  ? 250  PHE B CD2   1 
ATOM   6017 C  CE1   . PHE B 1 264 ? 33.757  77.298 -38.092 1.00 25.25  ? 250  PHE B CE1   1 
ATOM   6018 C  CE2   . PHE B 1 264 ? 32.125  77.733 -36.373 1.00 22.27  ? 250  PHE B CE2   1 
ATOM   6019 C  CZ    . PHE B 1 264 ? 32.448  77.600 -37.719 1.00 24.01  ? 250  PHE B CZ    1 
ATOM   6020 N  N     . ASP B 1 265 ? 38.373  75.989 -34.166 1.00 28.09  ? 251  ASP B N     1 
ATOM   6021 C  CA    . ASP B 1 265 ? 39.517  76.490 -33.413 1.00 29.39  ? 251  ASP B CA    1 
ATOM   6022 C  C     . ASP B 1 265 ? 39.179  77.908 -32.984 1.00 29.71  ? 251  ASP B C     1 
ATOM   6023 O  O     . ASP B 1 265 ? 39.062  78.801 -33.831 1.00 29.05  ? 251  ASP B O     1 
ATOM   6024 C  CB    . ASP B 1 265 ? 40.767  76.516 -34.287 1.00 31.01  ? 251  ASP B CB    1 
ATOM   6025 C  CG    . ASP B 1 265 ? 42.037  76.822 -33.502 1.00 34.78  ? 251  ASP B CG    1 
ATOM   6026 O  OD1   . ASP B 1 265 ? 41.966  77.600 -32.516 1.00 33.03  ? 251  ASP B OD1   1 
ATOM   6027 O  OD2   . ASP B 1 265 ? 43.092  76.226 -33.835 1.00 32.76  ? 251  ASP B OD2   1 
ATOM   6028 N  N     . GLU B 1 266 ? 39.022  78.129 -31.684 1.00 27.38  ? 252  GLU B N     1 
ATOM   6029 C  CA    . GLU B 1 266 ? 38.575  79.423 -31.189 1.00 29.49  ? 252  GLU B CA    1 
ATOM   6030 C  C     . GLU B 1 266 ? 39.714  80.413 -30.973 1.00 32.07  ? 252  GLU B C     1 
ATOM   6031 O  O     . GLU B 1 266 ? 39.480  81.501 -30.440 1.00 32.75  ? 252  GLU B O     1 
ATOM   6032 C  CB    . GLU B 1 266 ? 37.734  79.236 -29.921 1.00 27.46  ? 252  GLU B CB    1 
ATOM   6033 C  CG    . GLU B 1 266 ? 36.763  78.069 -30.070 1.00 27.32  ? 252  GLU B CG    1 
ATOM   6034 C  CD    . GLU B 1 266 ? 35.785  77.926 -28.909 1.00 28.61  ? 252  GLU B CD    1 
ATOM   6035 O  OE1   . GLU B 1 266 ? 36.151  78.230 -27.750 1.00 28.40  ? 252  GLU B OE1   1 
ATOM   6036 O  OE2   . GLU B 1 266 ? 34.640  77.504 -29.167 1.00 26.96  ? 252  GLU B OE2   1 
ATOM   6037 N  N     . ARG B 1 267 ? 40.934  80.063 -31.384 1.00 32.55  ? 253  ARG B N     1 
ATOM   6038 C  CA    . ARG B 1 267 ? 42.035  81.017 -31.446 1.00 35.55  ? 253  ARG B CA    1 
ATOM   6039 C  C     . ARG B 1 267 ? 42.083  81.740 -32.782 1.00 36.80  ? 253  ARG B C     1 
ATOM   6040 O  O     . ARG B 1 267 ? 42.766  82.764 -32.897 1.00 38.04  ? 253  ARG B O     1 
ATOM   6041 C  CB    . ARG B 1 267 ? 43.368  80.290 -31.235 1.00 34.65  ? 253  ARG B CB    1 
ATOM   6042 C  CG    . ARG B 1 267 ? 43.435  79.483 -29.954 1.00 34.76  ? 253  ARG B CG    1 
ATOM   6043 C  CD    . ARG B 1 267 ? 44.637  78.546 -29.983 1.00 35.30  ? 253  ARG B CD    1 
ATOM   6044 N  NE    . ARG B 1 267 ? 44.487  77.573 -31.062 1.00 34.88  ? 253  ARG B NE    1 
ATOM   6045 C  CZ    . ARG B 1 267 ? 45.272  76.520 -31.251 1.00 34.03  ? 253  ARG B CZ    1 
ATOM   6046 N  NH1   . ARG B 1 267 ? 46.295  76.266 -30.449 1.00 34.46  ? 253  ARG B NH1   1 
ATOM   6047 N  NH2   . ARG B 1 267 ? 45.020  75.699 -32.268 1.00 33.94  ? 253  ARG B NH2   1 
ATOM   6048 N  N     . HIS B 1 268 ? 41.370  81.225 -33.781 1.00 36.53  ? 254  HIS B N     1 
ATOM   6049 C  CA    . HIS B 1 268 ? 41.446  81.726 -35.143 1.00 38.95  ? 254  HIS B CA    1 
ATOM   6050 C  C     . HIS B 1 268 ? 40.850  83.122 -35.253 1.00 39.11  ? 254  HIS B C     1 
ATOM   6051 O  O     . HIS B 1 268 ? 39.997  83.526 -34.460 1.00 37.01  ? 254  HIS B O     1 
ATOM   6052 C  CB    . HIS B 1 268 ? 40.723  80.769 -36.093 1.00 41.82  ? 254  HIS B CB    1 
ATOM   6053 C  CG    . HIS B 1 268 ? 41.302  80.723 -37.472 1.00 57.12  ? 254  HIS B CG    1 
ATOM   6054 N  ND1   . HIS B 1 268 ? 42.399  79.952 -37.794 1.00 65.79  ? 254  HIS B ND1   1 
ATOM   6055 C  CD2   . HIS B 1 268 ? 40.922  81.336 -38.621 1.00 56.37  ? 254  HIS B CD2   1 
ATOM   6056 C  CE1   . HIS B 1 268 ? 42.681  80.106 -39.077 1.00 66.45  ? 254  HIS B CE1   1 
ATOM   6057 N  NE2   . HIS B 1 268 ? 41.800  80.940 -39.601 1.00 62.52  ? 254  HIS B NE2   1 
ATOM   6058 N  N     . VAL B 1 269 ? 41.335  83.874 -36.242 1.00 39.65  ? 255  VAL B N     1 
ATOM   6059 C  CA    . VAL B 1 269 ? 40.798  85.202 -36.490 1.00 39.00  ? 255  VAL B CA    1 
ATOM   6060 C  C     . VAL B 1 269 ? 39.323  85.077 -36.868 1.00 38.69  ? 255  VAL B C     1 
ATOM   6061 O  O     . VAL B 1 269 ? 38.901  84.101 -37.502 1.00 36.43  ? 255  VAL B O     1 
ATOM   6062 C  CB    . VAL B 1 269 ? 41.632  85.918 -37.568 1.00 39.57  ? 255  VAL B CB    1 
ATOM   6063 C  CG1   . VAL B 1 269 ? 41.302  85.398 -38.954 1.00 41.58  ? 255  VAL B CG1   1 
ATOM   6064 C  CG2   . VAL B 1 269 ? 41.427  87.427 -37.490 1.00 44.23  ? 255  VAL B CG2   1 
ATOM   6065 N  N     . GLY B 1 270 ? 38.518  86.034 -36.410 1.00 35.81  ? 256  GLY B N     1 
ATOM   6066 C  CA    . GLY B 1 270 ? 37.092  86.023 -36.654 1.00 34.75  ? 256  GLY B CA    1 
ATOM   6067 C  C     . GLY B 1 270 ? 36.256  85.355 -35.582 1.00 33.41  ? 256  GLY B C     1 
ATOM   6068 O  O     . GLY B 1 270 ? 35.023  85.497 -35.603 1.00 29.99  ? 256  GLY B O     1 
ATOM   6069 N  N     . PHE B 1 271 ? 36.874  84.650 -34.637 1.00 31.82  ? 257  PHE B N     1 
ATOM   6070 C  CA    . PHE B 1 271 ? 36.147  84.059 -33.521 1.00 31.32  ? 257  PHE B CA    1 
ATOM   6071 C  C     . PHE B 1 271 ? 36.328  84.919 -32.278 1.00 32.65  ? 257  PHE B C     1 
ATOM   6072 O  O     . PHE B 1 271 ? 37.461  85.152 -31.844 1.00 32.67  ? 257  PHE B O     1 
ATOM   6073 C  CB    . PHE B 1 271 ? 36.622  82.634 -33.234 1.00 28.04  ? 257  PHE B CB    1 
ATOM   6074 C  CG    . PHE B 1 271 ? 35.764  81.916 -32.238 1.00 28.52  ? 257  PHE B CG    1 
ATOM   6075 C  CD1   . PHE B 1 271 ? 35.982  82.065 -30.878 1.00 28.48  ? 257  PHE B CD1   1 
ATOM   6076 C  CD2   . PHE B 1 271 ? 34.715  81.112 -32.660 1.00 27.20  ? 257  PHE B CD2   1 
ATOM   6077 C  CE1   . PHE B 1 271 ? 35.186  81.412 -29.959 1.00 27.16  ? 257  PHE B CE1   1 
ATOM   6078 C  CE2   . PHE B 1 271 ? 33.915  80.458 -31.745 1.00 26.18  ? 257  PHE B CE2   1 
ATOM   6079 C  CZ    . PHE B 1 271 ? 34.149  80.617 -30.391 1.00 27.28  ? 257  PHE B CZ    1 
ATOM   6080 N  N     . TYR B 1 272 ? 35.212  85.337 -31.675 1.00 30.06  ? 258  TYR B N     1 
ATOM   6081 C  CA    . TYR B 1 272 ? 35.242  86.218 -30.514 1.00 30.58  ? 258  TYR B CA    1 
ATOM   6082 C  C     . TYR B 1 272 ? 34.646  85.588 -29.264 1.00 29.26  ? 258  TYR B C     1 
ATOM   6083 O  O     . TYR B 1 272 ? 34.683  86.210 -28.196 1.00 32.72  ? 258  TYR B O     1 
ATOM   6084 C  CB    . TYR B 1 272 ? 34.515  87.535 -30.818 1.00 30.31  ? 258  TYR B CB    1 
ATOM   6085 C  CG    . TYR B 1 272 ? 34.951  88.195 -32.102 1.00 33.99  ? 258  TYR B CG    1 
ATOM   6086 C  CD1   . TYR B 1 272 ? 34.367  87.864 -33.314 1.00 32.28  ? 258  TYR B CD1   1 
ATOM   6087 C  CD2   . TYR B 1 272 ? 35.973  89.145 -32.099 1.00 35.78  ? 258  TYR B CD2   1 
ATOM   6088 C  CE1   . TYR B 1 272 ? 34.770  88.473 -34.491 1.00 34.04  ? 258  TYR B CE1   1 
ATOM   6089 C  CE2   . TYR B 1 272 ? 36.389  89.751 -33.263 1.00 37.54  ? 258  TYR B CE2   1 
ATOM   6090 C  CZ    . TYR B 1 272 ? 35.786  89.414 -34.460 1.00 37.28  ? 258  TYR B CZ    1 
ATOM   6091 O  OH    . TYR B 1 272 ? 36.207  90.025 -35.619 1.00 39.52  ? 258  TYR B OH    1 
ATOM   6092 N  N     . GLY B 1 273 ? 34.116  84.376 -29.352 1.00 29.48  ? 259  GLY B N     1 
ATOM   6093 C  CA    . GLY B 1 273 ? 33.479  83.762 -28.202 1.00 29.35  ? 259  GLY B CA    1 
ATOM   6094 C  C     . GLY B 1 273 ? 32.224  83.000 -28.575 1.00 28.04  ? 259  GLY B C     1 
ATOM   6095 O  O     . GLY B 1 273 ? 31.737  83.103 -29.704 1.00 27.07  ? 259  GLY B O     1 
ATOM   6096 N  N     . THR B 1 274 ? 31.701  82.225 -27.634 1.00 25.78  ? 260  THR B N     1 
ATOM   6097 C  CA    . THR B 1 274 ? 30.517  81.423 -27.887 1.00 26.95  ? 260  THR B CA    1 
ATOM   6098 C  C     . THR B 1 274 ? 29.274  82.286 -27.783 1.00 28.18  ? 260  THR B C     1 
ATOM   6099 O  O     . THR B 1 274 ? 29.144  83.108 -26.873 1.00 27.81  ? 260  THR B O     1 
ATOM   6100 C  CB    . THR B 1 274 ? 30.434  80.254 -26.906 1.00 26.55  ? 260  THR B CB    1 
ATOM   6101 O  OG1   . THR B 1 274 ? 31.587  79.427 -27.085 1.00 26.32  ? 260  THR B OG1   1 
ATOM   6102 C  CG2   . THR B 1 274 ? 29.155  79.422 -27.146 1.00 24.60  ? 260  THR B CG2   1 
ATOM   6103 N  N     . TYR B 1 275 ? 28.369  82.103 -28.737 1.00 26.79  ? 261  TYR B N     1 
ATOM   6104 C  CA    . TYR B 1 275 ? 27.130  82.860 -28.771 1.00 27.36  ? 261  TYR B CA    1 
ATOM   6105 C  C     . TYR B 1 275 ? 26.130  82.242 -27.805 1.00 26.48  ? 261  TYR B C     1 
ATOM   6106 O  O     . TYR B 1 275 ? 25.893  81.033 -27.832 1.00 26.67  ? 261  TYR B O     1 
ATOM   6107 C  CB    . TYR B 1 275 ? 26.577  82.867 -30.196 1.00 26.98  ? 261  TYR B CB    1 
ATOM   6108 C  CG    . TYR B 1 275 ? 25.265  83.586 -30.366 1.00 26.73  ? 261  TYR B CG    1 
ATOM   6109 C  CD1   . TYR B 1 275 ? 25.168  84.944 -30.132 1.00 27.86  ? 261  TYR B CD1   1 
ATOM   6110 C  CD2   . TYR B 1 275 ? 24.124  82.901 -30.768 1.00 27.24  ? 261  TYR B CD2   1 
ATOM   6111 C  CE1   . TYR B 1 275 ? 23.984  85.613 -30.300 1.00 29.24  ? 261  TYR B CE1   1 
ATOM   6112 C  CE2   . TYR B 1 275 ? 22.928  83.559 -30.931 1.00 28.54  ? 261  TYR B CE2   1 
ATOM   6113 C  CZ    . TYR B 1 275 ? 22.864  84.916 -30.691 1.00 28.86  ? 261  TYR B CZ    1 
ATOM   6114 O  OH    . TYR B 1 275 ? 21.679  85.581 -30.855 1.00 30.04  ? 261  TYR B OH    1 
ATOM   6115 N  N     . SER B 1 276 ? 25.572  83.060 -26.923 1.00 28.24  ? 262  SER B N     1 
ATOM   6116 C  CA    . SER B 1 276 ? 24.533  82.594 -26.013 1.00 29.31  ? 262  SER B CA    1 
ATOM   6117 C  C     . SER B 1 276 ? 23.468  83.671 -25.829 1.00 32.13  ? 262  SER B C     1 
ATOM   6118 O  O     . SER B 1 276 ? 23.026  83.963 -24.716 1.00 32.35  ? 262  SER B O     1 
ATOM   6119 C  CB    . SER B 1 276 ? 25.152  82.137 -24.691 1.00 31.45  ? 262  SER B CB    1 
ATOM   6120 O  OG    . SER B 1 276 ? 25.215  83.201 -23.763 1.00 34.47  ? 262  SER B OG    1 
ATOM   6121 N  N     . GLY B 1 277 ? 23.031  84.272 -26.939 1.00 31.35  ? 263  GLY B N     1 
ATOM   6122 C  CA    . GLY B 1 277 ? 21.951  85.248 -26.855 1.00 31.22  ? 263  GLY B CA    1 
ATOM   6123 C  C     . GLY B 1 277 ? 22.388  86.495 -26.112 1.00 33.35  ? 263  GLY B C     1 
ATOM   6124 O  O     . GLY B 1 277 ? 23.517  86.981 -26.271 1.00 32.72  ? 263  GLY B O     1 
ATOM   6125 N  N     . SER B 1 278 ? 21.485  87.024 -25.279 1.00 33.73  ? 264  SER B N     1 
ATOM   6126 C  CA    . SER B 1 278 ? 21.795  88.247 -24.543 1.00 34.41  ? 264  SER B CA    1 
ATOM   6127 C  C     . SER B 1 278 ? 22.903  88.047 -23.518 1.00 34.59  ? 264  SER B C     1 
ATOM   6128 O  O     . SER B 1 278 ? 23.460  89.036 -23.032 1.00 38.12  ? 264  SER B O     1 
ATOM   6129 C  CB    . SER B 1 278 ? 20.538  88.805 -23.856 1.00 36.96  ? 264  SER B CB    1 
ATOM   6130 O  OG    . SER B 1 278 ? 20.090  87.976 -22.790 1.00 37.38  ? 264  SER B OG    1 
ATOM   6131 N  N     . ALA B 1 279 ? 23.238  86.806 -23.172 1.00 33.14  ? 265  ALA B N     1 
ATOM   6132 C  CA    . ALA B 1 279 ? 24.324  86.556 -22.232 1.00 36.02  ? 265  ALA B CA    1 
ATOM   6133 C  C     . ALA B 1 279 ? 25.697  86.554 -22.896 1.00 35.11  ? 265  ALA B C     1 
ATOM   6134 O  O     . ALA B 1 279 ? 26.707  86.419 -22.195 1.00 36.04  ? 265  ALA B O     1 
ATOM   6135 C  CB    . ALA B 1 279 ? 24.099  85.227 -21.504 1.00 38.76  ? 265  ALA B CB    1 
ATOM   6136 N  N     . SER B 1 280 ? 25.752  86.700 -24.219 1.00 35.45  ? 266  SER B N     1 
ATOM   6137 C  CA    . SER B 1 280 ? 27.014  86.694 -24.947 1.00 34.29  ? 266  SER B CA    1 
ATOM   6138 C  C     . SER B 1 280 ? 27.886  87.865 -24.524 1.00 36.10  ? 266  SER B C     1 
ATOM   6139 O  O     . SER B 1 280 ? 27.393  88.932 -24.146 1.00 35.57  ? 266  SER B O     1 
ATOM   6140 C  CB    . SER B 1 280 ? 26.761  86.796 -26.457 1.00 32.36  ? 266  SER B CB    1 
ATOM   6141 O  OG    . SER B 1 280 ? 25.835  85.823 -26.897 1.00 30.24  ? 266  SER B OG    1 
ATOM   6142 N  N     . ALA B 1 281 ? 29.199  87.671 -24.624 1.00 35.03  ? 267  ALA B N     1 
ATOM   6143 C  CA    . ALA B 1 281 ? 30.109  88.803 -24.563 1.00 36.63  ? 267  ALA B CA    1 
ATOM   6144 C  C     . ALA B 1 281 ? 29.737  89.816 -25.640 1.00 36.22  ? 267  ALA B C     1 
ATOM   6145 O  O     . ALA B 1 281 ? 29.246  89.459 -26.716 1.00 36.55  ? 267  ALA B O     1 
ATOM   6146 C  CB    . ALA B 1 281 ? 31.555  88.342 -24.744 1.00 36.33  ? 267  ALA B CB    1 
ATOM   6147 N  N     . GLY B 1 282 ? 29.960  91.098 -25.337 1.00 36.36  ? 268  GLY B N     1 
ATOM   6148 C  CA    . GLY B 1 282 ? 29.535  92.143 -26.255 1.00 33.84  ? 268  GLY B CA    1 
ATOM   6149 C  C     . GLY B 1 282 ? 30.167  92.015 -27.628 1.00 35.71  ? 268  GLY B C     1 
ATOM   6150 O  O     . GLY B 1 282 ? 29.524  92.289 -28.646 1.00 35.97  ? 268  GLY B O     1 
ATOM   6151 N  N     . ALA B 1 283 ? 31.433  91.585 -27.678 1.00 35.67  ? 269  ALA B N     1 
ATOM   6152 C  CA    . ALA B 1 283 ? 32.085  91.380 -28.969 1.00 34.95  ? 269  ALA B CA    1 
ATOM   6153 C  C     . ALA B 1 283 ? 31.400  90.280 -29.770 1.00 34.15  ? 269  ALA B C     1 
ATOM   6154 O  O     . ALA B 1 283 ? 31.338  90.358 -31.002 1.00 33.01  ? 269  ALA B O     1 
ATOM   6155 C  CB    . ALA B 1 283 ? 33.565  91.046 -28.772 1.00 31.33  ? 269  ALA B CB    1 
ATOM   6156 N  N     . VAL B 1 284 ? 30.902  89.242 -29.095 1.00 33.05  ? 270  VAL B N     1 
ATOM   6157 C  CA    . VAL B 1 284 ? 30.190  88.179 -29.797 1.00 32.54  ? 270  VAL B CA    1 
ATOM   6158 C  C     . VAL B 1 284 ? 28.845  88.687 -30.296 1.00 32.77  ? 270  VAL B C     1 
ATOM   6159 O  O     . VAL B 1 284 ? 28.448  88.435 -31.440 1.00 29.43  ? 270  VAL B O     1 
ATOM   6160 C  CB    . VAL B 1 284 ? 30.017  86.961 -28.874 1.00 33.05  ? 270  VAL B CB    1 
ATOM   6161 C  CG1   . VAL B 1 284 ? 29.311  85.835 -29.606 1.00 30.01  ? 270  VAL B CG1   1 
ATOM   6162 C  CG2   . VAL B 1 284 ? 31.362  86.527 -28.301 1.00 29.97  ? 270  VAL B CG2   1 
ATOM   6163 N  N     . LYS B 1 285 ? 28.125  89.409 -29.441 1.00 33.62  ? 271  LYS B N     1 
ATOM   6164 C  CA    . LYS B 1 285 ? 26.844  89.969 -29.844 1.00 34.93  ? 271  LYS B CA    1 
ATOM   6165 C  C     . LYS B 1 285 ? 27.003  90.828 -31.090 1.00 33.66  ? 271  LYS B C     1 
ATOM   6166 O  O     . LYS B 1 285 ? 26.259  90.674 -32.065 1.00 32.97  ? 271  LYS B O     1 
ATOM   6167 C  CB    . LYS B 1 285 ? 26.260  90.785 -28.691 1.00 34.09  ? 271  LYS B CB    1 
ATOM   6168 C  CG    . LYS B 1 285 ? 24.789  90.565 -28.443 1.00 34.87  ? 271  LYS B CG    1 
ATOM   6169 C  CD    . LYS B 1 285 ? 24.340  91.319 -27.216 1.00 36.89  ? 271  LYS B CD    1 
ATOM   6170 C  CE    . LYS B 1 285 ? 24.877  90.672 -25.964 1.00 34.34  ? 271  LYS B CE    1 
ATOM   6171 N  NZ    . LYS B 1 285 ? 23.911  90.840 -24.839 1.00 37.61  ? 271  LYS B NZ    1 
ATOM   6172 N  N     . GLU B 1 286 ? 28.015  91.697 -31.095 1.00 32.96  ? 272  GLU B N     1 
ATOM   6173 C  CA    . GLU B 1 286 ? 28.239  92.578 -32.235 1.00 35.68  ? 272  GLU B CA    1 
ATOM   6174 C  C     . GLU B 1 286 ? 28.683  91.797 -33.469 1.00 33.04  ? 272  GLU B C     1 
ATOM   6175 O  O     . GLU B 1 286 ? 28.266  92.111 -34.588 1.00 33.57  ? 272  GLU B O     1 
ATOM   6176 C  CB    . GLU B 1 286 ? 29.265  93.653 -31.871 1.00 34.52  ? 272  GLU B CB    1 
ATOM   6177 C  CG    . GLU B 1 286 ? 29.511  94.665 -32.975 1.00 38.11  ? 272  GLU B CG    1 
ATOM   6178 C  CD    . GLU B 1 286 ? 28.211  95.316 -33.469 1.00 48.16  ? 272  GLU B CD    1 
ATOM   6179 O  OE1   . GLU B 1 286 ? 27.299  95.546 -32.640 1.00 45.98  ? 272  GLU B OE1   1 
ATOM   6180 O  OE2   . GLU B 1 286 ? 28.099  95.605 -34.683 1.00 43.69  ? 272  GLU B OE2   1 
ATOM   6181 N  N     . ALA B 1 287 ? 29.542  90.788 -33.290 1.00 34.50  ? 273  ALA B N     1 
ATOM   6182 C  CA    . ALA B 1 287 ? 30.062  90.045 -34.435 1.00 31.26  ? 273  ALA B CA    1 
ATOM   6183 C  C     . ALA B 1 287 ? 28.970  89.242 -35.127 1.00 30.85  ? 273  ALA B C     1 
ATOM   6184 O  O     . ALA B 1 287 ? 28.957  89.144 -36.359 1.00 31.59  ? 273  ALA B O     1 
ATOM   6185 C  CB    . ALA B 1 287 ? 31.195  89.123 -33.998 1.00 30.79  ? 273  ALA B CB    1 
ATOM   6186 N  N     . ILE B 1 288 ? 28.045  88.666 -34.353 1.00 28.95  ? 274  ILE B N     1 
ATOM   6187 C  CA    . ILE B 1 288 ? 27.013  87.792 -34.889 1.00 27.89  ? 274  ILE B CA    1 
ATOM   6188 C  C     . ILE B 1 288 ? 25.727  88.579 -35.097 1.00 28.91  ? 274  ILE B C     1 
ATOM   6189 O  O     . ILE B 1 288 ? 25.248  88.722 -36.227 1.00 31.18  ? 274  ILE B O     1 
ATOM   6190 C  CB    . ILE B 1 288 ? 26.770  86.591 -33.953 1.00 28.14  ? 274  ILE B CB    1 
ATOM   6191 C  CG1   . ILE B 1 288 ? 28.056  85.768 -33.747 1.00 27.83  ? 274  ILE B CG1   1 
ATOM   6192 C  CG2   . ILE B 1 288 ? 25.596  85.748 -34.446 1.00 26.60  ? 274  ILE B CG2   1 
ATOM   6193 C  CD1   . ILE B 1 288 ? 28.764  85.303 -35.026 1.00 29.58  ? 274  ILE B CD1   1 
ATOM   6194 N  N     . GLU B 1 289 ? 25.158  89.100 -34.010 1.00 30.16  ? 275  GLU B N     1 
ATOM   6195 C  CA    . GLU B 1 289 ? 23.883  89.801 -34.108 1.00 30.59  ? 275  GLU B CA    1 
ATOM   6196 C  C     . GLU B 1 289 ? 24.005  91.098 -34.893 1.00 30.72  ? 275  GLU B C     1 
ATOM   6197 O  O     . GLU B 1 289 ? 23.019  91.553 -35.484 1.00 32.05  ? 275  GLU B O     1 
ATOM   6198 C  CB    . GLU B 1 289 ? 23.324  90.049 -32.702 1.00 31.98  ? 275  GLU B CB    1 
ATOM   6199 C  CG    . GLU B 1 289 ? 22.522  88.875 -32.196 1.00 31.40  ? 275  GLU B CG    1 
ATOM   6200 C  CD    . GLU B 1 289 ? 22.092  88.986 -30.745 1.00 33.25  ? 275  GLU B CD    1 
ATOM   6201 O  OE1   . GLU B 1 289 ? 22.173  90.080 -30.161 1.00 33.21  ? 275  GLU B OE1   1 
ATOM   6202 O  OE2   . GLU B 1 289 ? 21.631  87.963 -30.200 1.00 31.41  ? 275  GLU B OE2   1 
ATOM   6203 N  N     . GLY B 1 290 ? 25.195  91.683 -34.947 1.00 30.95  ? 276  GLY B N     1 
ATOM   6204 C  CA    . GLY B 1 290 ? 25.370  92.912 -35.685 1.00 33.28  ? 276  GLY B CA    1 
ATOM   6205 C  C     . GLY B 1 290 ? 25.560  92.743 -37.175 1.00 32.04  ? 276  GLY B C     1 
ATOM   6206 O  O     . GLY B 1 290 ? 25.490  93.735 -37.902 1.00 32.56  ? 276  GLY B O     1 
ATOM   6207 N  N     . ALA B 1 291 ? 25.818  91.524 -37.644 1.00 29.99  ? 277  ALA B N     1 
ATOM   6208 C  CA    . ALA B 1 291 ? 25.972  91.295 -39.070 1.00 29.52  ? 277  ALA B CA    1 
ATOM   6209 C  C     . ALA B 1 291 ? 24.628  91.424 -39.769 1.00 30.09  ? 277  ALA B C     1 
ATOM   6210 O  O     . ALA B 1 291 ? 23.587  91.042 -39.230 1.00 28.69  ? 277  ALA B O     1 
ATOM   6211 C  CB    . ALA B 1 291 ? 26.559  89.907 -39.329 1.00 29.86  ? 277  ALA B CB    1 
ATOM   6212 N  N     . ASP B 1 292 ? 24.652  91.923 -41.004 1.00 29.64  ? 278  ASP B N     1 
ATOM   6213 C  CA    . ASP B 1 292 ? 23.376  92.062 -41.686 1.00 29.65  ? 278  ASP B CA    1 
ATOM   6214 C  C     . ASP B 1 292 ? 22.886  90.750 -42.281 1.00 28.80  ? 278  ASP B C     1 
ATOM   6215 O  O     . ASP B 1 292 ? 21.704  90.655 -42.626 1.00 29.32  ? 278  ASP B O     1 
ATOM   6216 C  CB    . ASP B 1 292 ? 23.449  93.126 -42.785 1.00 32.54  ? 278  ASP B CB    1 
ATOM   6217 C  CG    . ASP B 1 292 ? 24.595  92.904 -43.717 1.00 33.93  ? 278  ASP B CG    1 
ATOM   6218 O  OD1   . ASP B 1 292 ? 24.558  91.865 -44.414 1.00 32.18  ? 278  ASP B OD1   1 
ATOM   6219 O  OD2   . ASP B 1 292 ? 25.502  93.776 -43.789 1.00 35.94  ? 278  ASP B OD2   1 
ATOM   6220 N  N     . THR B 1 293 ? 23.742  89.733 -42.369 1.00 28.18  ? 279  THR B N     1 
ATOM   6221 C  CA    . THR B 1 293 ? 23.341  88.391 -42.775 1.00 28.21  ? 279  THR B CA    1 
ATOM   6222 C  C     . THR B 1 293 ? 24.045  87.386 -41.879 1.00 26.68  ? 279  THR B C     1 
ATOM   6223 O  O     . THR B 1 293 ? 25.269  87.452 -41.723 1.00 26.16  ? 279  THR B O     1 
ATOM   6224 C  CB    . THR B 1 293 ? 23.711  88.106 -44.236 1.00 28.21  ? 279  THR B CB    1 
ATOM   6225 O  OG1   . THR B 1 293 ? 23.441  89.263 -45.042 1.00 31.44  ? 279  THR B OG1   1 
ATOM   6226 C  CG2   . THR B 1 293 ? 22.913  86.934 -44.758 1.00 25.22  ? 279  THR B CG2   1 
ATOM   6227 N  N     . VAL B 1 294 ? 23.293  86.453 -41.300 1.00 24.42  ? 280  VAL B N     1 
ATOM   6228 C  CA    . VAL B 1 294 ? 23.872  85.450 -40.412 1.00 23.60  ? 280  VAL B CA    1 
ATOM   6229 C  C     . VAL B 1 294 ? 23.488  84.068 -40.926 1.00 23.91  ? 280  VAL B C     1 
ATOM   6230 O  O     . VAL B 1 294 ? 22.299  83.724 -40.966 1.00 21.72  ? 280  VAL B O     1 
ATOM   6231 C  CB    . VAL B 1 294 ? 23.422  85.647 -38.956 1.00 24.77  ? 280  VAL B CB    1 
ATOM   6232 C  CG1   . VAL B 1 294 ? 23.998  84.546 -38.073 1.00 22.03  ? 280  VAL B CG1   1 
ATOM   6233 C  CG2   . VAL B 1 294 ? 23.846  87.037 -38.454 1.00 24.72  ? 280  VAL B CG2   1 
ATOM   6234 N  N     . LEU B 1 295 ? 24.496  83.274 -41.288 1.00 22.03  ? 281  LEU B N     1 
ATOM   6235 C  CA    . LEU B 1 295 ? 24.309  81.899 -41.744 1.00 23.08  ? 281  LEU B CA    1 
ATOM   6236 C  C     . LEU B 1 295 ? 24.221  80.980 -40.530 1.00 24.60  ? 281  LEU B C     1 
ATOM   6237 O  O     . LEU B 1 295 ? 25.199  80.827 -39.786 1.00 24.34  ? 281  LEU B O     1 
ATOM   6238 C  CB    . LEU B 1 295 ? 25.457  81.482 -42.657 1.00 24.19  ? 281  LEU B CB    1 
ATOM   6239 C  CG    . LEU B 1 295 ? 25.672  82.315 -43.920 1.00 23.37  ? 281  LEU B CG    1 
ATOM   6240 C  CD1   . LEU B 1 295 ? 27.007  81.988 -44.553 1.00 25.48  ? 281  LEU B CD1   1 
ATOM   6241 C  CD2   . LEU B 1 295 ? 24.554  82.037 -44.903 1.00 24.84  ? 281  LEU B CD2   1 
ATOM   6242 N  N     . CYS B 1 296 ? 23.046  80.375 -40.322 1.00 21.63  ? 282  CYS B N     1 
ATOM   6243 C  CA    . CYS B 1 296 ? 22.783  79.509 -39.177 1.00 23.70  ? 282  CYS B CA    1 
ATOM   6244 C  C     . CYS B 1 296 ? 22.836  78.060 -39.654 1.00 23.30  ? 282  CYS B C     1 
ATOM   6245 O  O     . CYS B 1 296 ? 21.918  77.593 -40.333 1.00 23.53  ? 282  CYS B O     1 
ATOM   6246 C  CB    . CYS B 1 296 ? 21.425  79.847 -38.566 1.00 21.84  ? 282  CYS B CB    1 
ATOM   6247 S  SG    . CYS B 1 296 ? 21.312  81.545 -37.984 1.00 25.46  ? 282  CYS B SG    1 
ATOM   6248 N  N     . ILE B 1 297 ? 23.902  77.347 -39.301 1.00 21.57  ? 283  ILE B N     1 
ATOM   6249 C  CA    . ILE B 1 297 ? 24.172  76.030 -39.866 1.00 20.73  ? 283  ILE B CA    1 
ATOM   6250 C  C     . ILE B 1 297 ? 23.977  74.986 -38.772 1.00 21.60  ? 283  ILE B C     1 
ATOM   6251 O  O     . ILE B 1 297 ? 24.774  74.914 -37.828 1.00 20.08  ? 283  ILE B O     1 
ATOM   6252 C  CB    . ILE B 1 297 ? 25.590  75.946 -40.453 1.00 21.97  ? 283  ILE B CB    1 
ATOM   6253 C  CG1   . ILE B 1 297 ? 25.940  77.201 -41.288 1.00 22.61  ? 283  ILE B CG1   1 
ATOM   6254 C  CG2   . ILE B 1 297 ? 25.795  74.637 -41.193 1.00 19.87  ? 283  ILE B CG2   1 
ATOM   6255 C  CD1   . ILE B 1 297 ? 24.987  77.553 -42.456 1.00 21.67  ? 283  ILE B CD1   1 
ATOM   6256 N  N     . GLY B 1 298 ? 22.970  74.130 -38.934 1.00 21.92  ? 284  GLY B N     1 
ATOM   6257 C  CA    . GLY B 1 298 ? 22.741  73.051 -37.977 1.00 20.59  ? 284  GLY B CA    1 
ATOM   6258 C  C     . GLY B 1 298 ? 22.449  73.547 -36.577 1.00 21.30  ? 284  GLY B C     1 
ATOM   6259 O  O     . GLY B 1 298 ? 22.939  72.976 -35.592 1.00 19.93  ? 284  GLY B O     1 
ATOM   6260 N  N     . THR B 1 299 ? 21.653  74.606 -36.471 1.00 21.93  ? 285  THR B N     1 
ATOM   6261 C  CA    . THR B 1 299 ? 21.445  75.352 -35.242 1.00 23.34  ? 285  THR B CA    1 
ATOM   6262 C  C     . THR B 1 299 ? 20.074  75.063 -34.646 1.00 24.05  ? 285  THR B C     1 
ATOM   6263 O  O     . THR B 1 299 ? 19.083  74.921 -35.371 1.00 22.03  ? 285  THR B O     1 
ATOM   6264 C  CB    . THR B 1 299 ? 21.593  76.853 -35.508 1.00 26.06  ? 285  THR B CB    1 
ATOM   6265 O  OG1   . THR B 1 299 ? 20.630  77.266 -36.486 1.00 40.34  ? 285  THR B OG1   1 
ATOM   6266 C  CG2   . THR B 1 299 ? 23.002  77.173 -35.974 1.00 24.21  ? 285  THR B CG2   1 
ATOM   6267 N  N     . ARG B 1 300 ? 20.022  74.990 -33.320 1.00 24.23  ? 286  ARG B N     1 
ATOM   6268 C  CA    . ARG B 1 300 ? 18.765  74.806 -32.599 1.00 23.74  ? 286  ARG B CA    1 
ATOM   6269 C  C     . ARG B 1 300 ? 18.766  75.770 -31.419 1.00 25.44  ? 286  ARG B C     1 
ATOM   6270 O  O     . ARG B 1 300 ? 19.562  75.614 -30.484 1.00 23.95  ? 286  ARG B O     1 
ATOM   6271 C  CB    . ARG B 1 300 ? 18.594  73.355 -32.148 1.00 23.16  ? 286  ARG B CB    1 
ATOM   6272 C  CG    . ARG B 1 300 ? 18.403  72.341 -33.295 1.00 21.65  ? 286  ARG B CG    1 
ATOM   6273 C  CD    . ARG B 1 300 ? 17.144  72.590 -34.146 1.00 25.10  ? 286  ARG B CD    1 
ATOM   6274 N  NE    . ARG B 1 300 ? 17.178  71.831 -35.395 1.00 22.82  ? 286  ARG B NE    1 
ATOM   6275 C  CZ    . ARG B 1 300 ? 16.703  70.601 -35.546 1.00 23.18  ? 286  ARG B CZ    1 
ATOM   6276 N  NH1   . ARG B 1 300 ? 16.135  69.951 -34.543 1.00 23.81  ? 286  ARG B NH1   1 
ATOM   6277 N  NH2   . ARG B 1 300 ? 16.800  70.008 -36.733 1.00 22.14  ? 286  ARG B NH2   1 
ATOM   6278 N  N     . PHE B 1 301 ? 17.888  76.778 -31.470 1.00 24.50  ? 287  PHE B N     1 
ATOM   6279 C  CA    . PHE B 1 301 ? 17.907  77.865 -30.492 1.00 25.04  ? 287  PHE B CA    1 
ATOM   6280 C  C     . PHE B 1 301 ? 17.127  77.423 -29.254 1.00 25.85  ? 287  PHE B C     1 
ATOM   6281 O  O     . PHE B 1 301 ? 15.957  77.757 -29.060 1.00 27.16  ? 287  PHE B O     1 
ATOM   6282 C  CB    . PHE B 1 301 ? 17.344  79.152 -31.088 1.00 25.14  ? 287  PHE B CB    1 
ATOM   6283 C  CG    . PHE B 1 301 ? 18.215  79.759 -32.157 1.00 28.91  ? 287  PHE B CG    1 
ATOM   6284 C  CD1   . PHE B 1 301 ? 19.401  80.405 -31.821 1.00 28.39  ? 287  PHE B CD1   1 
ATOM   6285 C  CD2   . PHE B 1 301 ? 17.848  79.701 -33.501 1.00 30.45  ? 287  PHE B CD2   1 
ATOM   6286 C  CE1   . PHE B 1 301 ? 20.208  80.968 -32.802 1.00 26.58  ? 287  PHE B CE1   1 
ATOM   6287 C  CE2   . PHE B 1 301 ? 18.661  80.264 -34.481 1.00 29.85  ? 287  PHE B CE2   1 
ATOM   6288 C  CZ    . PHE B 1 301 ? 19.848  80.887 -34.121 1.00 27.64  ? 287  PHE B CZ    1 
ATOM   6289 N  N     . THR B 1 302 ? 17.794  76.643 -28.403 1.00 23.84  ? 288  THR B N     1 
ATOM   6290 C  CA    . THR B 1 302 ? 17.146  76.152 -27.197 1.00 24.90  ? 288  THR B CA    1 
ATOM   6291 C  C     . THR B 1 302 ? 17.171  77.225 -26.108 1.00 26.41  ? 288  THR B C     1 
ATOM   6292 O  O     . THR B 1 302 ? 17.822  78.263 -26.239 1.00 26.19  ? 288  THR B O     1 
ATOM   6293 C  CB    . THR B 1 302 ? 17.816  74.868 -26.711 1.00 24.84  ? 288  THR B CB    1 
ATOM   6294 O  OG1   . THR B 1 302 ? 19.074  75.179 -26.095 1.00 25.89  ? 288  THR B OG1   1 
ATOM   6295 C  CG2   . THR B 1 302 ? 18.047  73.925 -27.870 1.00 23.70  ? 288  THR B CG2   1 
ATOM   6296 N  N     . ASP B 1 303 ? 16.425  76.977 -25.024 1.00 26.03  ? 289  ASP B N     1 
ATOM   6297 C  CA    . ASP B 1 303 ? 16.351  77.968 -23.950 1.00 28.17  ? 289  ASP B CA    1 
ATOM   6298 C  C     . ASP B 1 303 ? 17.719  78.203 -23.305 1.00 26.95  ? 289  ASP B C     1 
ATOM   6299 O  O     . ASP B 1 303 ? 18.109  79.351 -23.064 1.00 28.14  ? 289  ASP B O     1 
ATOM   6300 C  CB    . ASP B 1 303 ? 15.300  77.549 -22.916 1.00 26.15  ? 289  ASP B CB    1 
ATOM   6301 C  CG    . ASP B 1 303 ? 15.541  76.160 -22.337 1.00 26.75  ? 289  ASP B CG    1 
ATOM   6302 O  OD1   . ASP B 1 303 ? 16.324  75.367 -22.907 1.00 26.74  ? 289  ASP B OD1   1 
ATOM   6303 O  OD2   . ASP B 1 303 ? 14.908  75.847 -21.313 1.00 26.36  ? 289  ASP B OD2   1 
ATOM   6304 N  N     . THR B 1 304 ? 18.468  77.134 -23.039 1.00 25.82  ? 290  THR B N     1 
ATOM   6305 C  CA    . THR B 1 304 ? 19.794  77.282 -22.443 1.00 27.80  ? 290  THR B CA    1 
ATOM   6306 C  C     . THR B 1 304 ? 20.781  77.948 -23.401 1.00 29.04  ? 290  THR B C     1 
ATOM   6307 O  O     . THR B 1 304 ? 21.587  78.792 -22.986 1.00 30.44  ? 290  THR B O     1 
ATOM   6308 C  CB    . THR B 1 304 ? 20.312  75.916 -22.011 1.00 29.28  ? 290  THR B CB    1 
ATOM   6309 O  OG1   . THR B 1 304 ? 19.465  75.400 -20.977 1.00 28.31  ? 290  THR B OG1   1 
ATOM   6310 C  CG2   . THR B 1 304 ? 21.735  76.038 -21.475 1.00 33.05  ? 290  THR B CG2   1 
ATOM   6311 N  N     . LEU B 1 305 ? 20.707  77.613 -24.692 1.00 26.47  ? 291  LEU B N     1 
ATOM   6312 C  CA    . LEU B 1 305 ? 21.682  78.116 -25.656 1.00 26.55  ? 291  LEU B CA    1 
ATOM   6313 C  C     . LEU B 1 305 ? 21.485  79.592 -25.957 1.00 26.57  ? 291  LEU B C     1 
ATOM   6314 O  O     . LEU B 1 305 ? 22.388  80.221 -26.519 1.00 28.53  ? 291  LEU B O     1 
ATOM   6315 C  CB    . LEU B 1 305 ? 21.588  77.314 -26.965 1.00 25.31  ? 291  LEU B CB    1 
ATOM   6316 C  CG    . LEU B 1 305 ? 22.556  76.154 -27.206 1.00 24.39  ? 291  LEU B CG    1 
ATOM   6317 C  CD1   . LEU B 1 305 ? 22.726  75.299 -25.969 1.00 24.16  ? 291  LEU B CD1   1 
ATOM   6318 C  CD2   . LEU B 1 305 ? 22.080  75.305 -28.386 1.00 22.67  ? 291  LEU B CD2   1 
ATOM   6319 N  N     . THR B 1 306 ? 20.326  80.157 -25.599 1.00 27.47  ? 292  THR B N     1 
ATOM   6320 C  CA    . THR B 1 306 ? 19.970  81.526 -25.959 1.00 30.14  ? 292  THR B CA    1 
ATOM   6321 C  C     . THR B 1 306 ? 19.617  82.384 -24.745 1.00 29.99  ? 292  THR B C     1 
ATOM   6322 O  O     . THR B 1 306 ? 19.003  83.439 -24.908 1.00 30.75  ? 292  THR B O     1 
ATOM   6323 C  CB    . THR B 1 306 ? 18.796  81.527 -26.944 1.00 29.14  ? 292  THR B CB    1 
ATOM   6324 O  OG1   . THR B 1 306 ? 17.624  81.029 -26.279 1.00 27.98  ? 292  THR B OG1   1 
ATOM   6325 C  CG2   . THR B 1 306 ? 19.107  80.639 -28.149 1.00 26.20  ? 292  THR B CG2   1 
ATOM   6326 N  N     . ALA B 1 307 ? 20.006  81.972 -23.542 1.00 30.11  ? 293  ALA B N     1 
ATOM   6327 C  CA    . ALA B 1 307 ? 19.689  82.709 -22.316 1.00 32.84  ? 293  ALA B CA    1 
ATOM   6328 C  C     . ALA B 1 307 ? 18.196  83.007 -22.211 1.00 33.50  ? 293  ALA B C     1 
ATOM   6329 O  O     . ALA B 1 307 ? 17.773  84.150 -22.020 1.00 35.34  ? 293  ALA B O     1 
ATOM   6330 C  CB    . ALA B 1 307 ? 20.506  83.998 -22.216 1.00 35.45  ? 293  ALA B CB    1 
ATOM   6331 N  N     . GLY B 1 308 ? 17.391  81.956 -22.323 1.00 30.90  ? 294  GLY B N     1 
ATOM   6332 C  CA    . GLY B 1 308 ? 15.949  82.129 -22.273 1.00 29.75  ? 294  GLY B CA    1 
ATOM   6333 C  C     . GLY B 1 308 ? 15.347  82.776 -23.502 1.00 29.81  ? 294  GLY B C     1 
ATOM   6334 O  O     . GLY B 1 308 ? 14.448  83.618 -23.376 1.00 30.14  ? 294  GLY B O     1 
ATOM   6335 N  N     . PHE B 1 309 ? 15.815  82.397 -24.693 1.00 31.84  ? 295  PHE B N     1 
ATOM   6336 C  CA    . PHE B 1 309 ? 15.261  82.890 -25.961 1.00 29.48  ? 295  PHE B CA    1 
ATOM   6337 C  C     . PHE B 1 309 ? 15.392  84.406 -26.108 1.00 31.70  ? 295  PHE B C     1 
ATOM   6338 O  O     . PHE B 1 309 ? 14.496  85.073 -26.634 1.00 31.21  ? 295  PHE B O     1 
ATOM   6339 C  CB    . PHE B 1 309 ? 13.801  82.453 -26.119 1.00 30.84  ? 295  PHE B CB    1 
ATOM   6340 C  CG    . PHE B 1 309 ? 13.594  80.981 -25.935 1.00 31.78  ? 295  PHE B CG    1 
ATOM   6341 C  CD1   . PHE B 1 309 ? 14.197  80.074 -26.795 1.00 30.10  ? 295  PHE B CD1   1 
ATOM   6342 C  CD2   . PHE B 1 309 ? 12.790  80.499 -24.912 1.00 30.46  ? 295  PHE B CD2   1 
ATOM   6343 C  CE1   . PHE B 1 309 ? 14.007  78.712 -26.633 1.00 27.02  ? 295  PHE B CE1   1 
ATOM   6344 C  CE2   . PHE B 1 309 ? 12.597  79.134 -24.741 1.00 29.16  ? 295  PHE B CE2   1 
ATOM   6345 C  CZ    . PHE B 1 309 ? 13.203  78.243 -25.609 1.00 28.69  ? 295  PHE B CZ    1 
ATOM   6346 N  N     . THR B 1 310 ? 16.521  84.960 -25.654 1.00 31.43  ? 296  THR B N     1 
ATOM   6347 C  CA    . THR B 1 310 ? 16.811  86.381 -25.812 1.00 30.81  ? 296  THR B CA    1 
ATOM   6348 C  C     . THR B 1 310 ? 17.807  86.650 -26.938 1.00 32.50  ? 296  THR B C     1 
ATOM   6349 O  O     . THR B 1 310 ? 18.422  87.722 -26.974 1.00 33.32  ? 296  THR B O     1 
ATOM   6350 C  CB    . THR B 1 310 ? 17.315  86.979 -24.497 1.00 32.72  ? 296  THR B CB    1 
ATOM   6351 O  OG1   . THR B 1 310 ? 18.440  86.230 -24.026 1.00 34.77  ? 296  THR B OG1   1 
ATOM   6352 C  CG2   . THR B 1 310 ? 16.223  86.914 -23.448 1.00 31.87  ? 296  THR B CG2   1 
ATOM   6353 N  N     . HIS B 1 311 ? 18.006  85.683 -27.828 1.00 31.16  ? 297  HIS B N     1 
ATOM   6354 C  CA    . HIS B 1 311 ? 18.752  85.918 -29.055 1.00 29.87  ? 297  HIS B CA    1 
ATOM   6355 C  C     . HIS B 1 311 ? 17.987  86.872 -29.962 1.00 32.50  ? 297  HIS B C     1 
ATOM   6356 O  O     . HIS B 1 311 ? 16.759  86.810 -30.051 1.00 34.97  ? 297  HIS B O     1 
ATOM   6357 C  CB    . HIS B 1 311 ? 18.996  84.596 -29.783 1.00 28.21  ? 297  HIS B CB    1 
ATOM   6358 C  CG    . HIS B 1 311 ? 17.745  83.829 -30.092 1.00 29.96  ? 297  HIS B CG    1 
ATOM   6359 N  ND1   . HIS B 1 311 ? 16.800  83.518 -29.134 1.00 31.03  ? 297  HIS B ND1   1 
ATOM   6360 C  CD2   . HIS B 1 311 ? 17.292  83.293 -31.251 1.00 30.96  ? 297  HIS B CD2   1 
ATOM   6361 C  CE1   . HIS B 1 311 ? 15.821  82.828 -29.690 1.00 31.27  ? 297  HIS B CE1   1 
ATOM   6362 N  NE2   . HIS B 1 311 ? 16.096  82.675 -30.974 1.00 31.57  ? 297  HIS B NE2   1 
ATOM   6363 N  N     . GLN B 1 312 ? 18.726  87.735 -30.662 1.00 32.04  ? 298  GLN B N     1 
ATOM   6364 C  CA    . GLN B 1 312 ? 18.179  88.756 -31.554 1.00 33.47  ? 298  GLN B CA    1 
ATOM   6365 C  C     . GLN B 1 312 ? 18.658  88.463 -32.975 1.00 33.83  ? 298  GLN B C     1 
ATOM   6366 O  O     . GLN B 1 312 ? 19.690  88.979 -33.409 1.00 33.61  ? 298  GLN B O     1 
ATOM   6367 C  CB    . GLN B 1 312 ? 18.605  90.143 -31.115 1.00 35.49  ? 298  GLN B CB    1 
ATOM   6368 C  CG    . GLN B 1 312 ? 17.703  90.794 -30.083 1.00 41.42  ? 298  GLN B CG    1 
ATOM   6369 C  CD    . GLN B 1 312 ? 18.273  92.106 -29.584 1.00 47.39  ? 298  GLN B CD    1 
ATOM   6370 O  OE1   . GLN B 1 312 ? 18.731  92.200 -28.447 1.00 52.06  ? 298  GLN B OE1   1 
ATOM   6371 N  NE2   . GLN B 1 312 ? 18.274  93.123 -30.445 1.00 50.64  ? 298  GLN B NE2   1 
ATOM   6372 N  N     . LEU B 1 313 ? 17.903  87.630 -33.688 1.00 33.03  ? 299  LEU B N     1 
ATOM   6373 C  CA    . LEU B 1 313 ? 18.187  87.262 -35.071 1.00 32.10  ? 299  LEU B CA    1 
ATOM   6374 C  C     . LEU B 1 313 ? 16.849  87.141 -35.783 1.00 32.48  ? 299  LEU B C     1 
ATOM   6375 O  O     . LEU B 1 313 ? 15.995  86.352 -35.368 1.00 35.42  ? 299  LEU B O     1 
ATOM   6376 C  CB    . LEU B 1 313 ? 18.974  85.948 -35.163 1.00 29.52  ? 299  LEU B CB    1 
ATOM   6377 C  CG    . LEU B 1 313 ? 20.412  85.890 -34.644 1.00 30.73  ? 299  LEU B CG    1 
ATOM   6378 C  CD1   . LEU B 1 313 ? 20.958  84.482 -34.820 1.00 29.95  ? 299  LEU B CD1   1 
ATOM   6379 C  CD2   . LEU B 1 313 ? 21.327  86.905 -35.336 1.00 29.48  ? 299  LEU B CD2   1 
ATOM   6380 N  N     . THR B 1 314 ? 16.654  87.920 -36.809 1.00 30.75  ? 300  THR B N     1 
ATOM   6381 C  CA    . THR B 1 314 ? 15.366  87.917 -37.479 1.00 29.90  ? 300  THR B CA    1 
ATOM   6382 C  C     . THR B 1 314 ? 15.388  86.974 -38.672 1.00 29.52  ? 300  THR B C     1 
ATOM   6383 O  O     . THR B 1 314 ? 16.458  86.590 -39.156 1.00 29.17  ? 300  THR B O     1 
ATOM   6384 C  CB    . THR B 1 314 ? 15.024  89.324 -37.948 1.00 30.27  ? 300  THR B CB    1 
ATOM   6385 O  OG1   . THR B 1 314 ? 15.821  89.639 -39.092 1.00 30.09  ? 300  THR B OG1   1 
ATOM   6386 C  CG2   . THR B 1 314 ? 15.318  90.340 -36.847 1.00 29.88  ? 300  THR B CG2   1 
ATOM   6387 N  N     . PRO B 1 315 ? 14.216  86.550 -39.158 1.00 31.86  ? 301  PRO B N     1 
ATOM   6388 C  CA    . PRO B 1 315 ? 14.209  85.717 -40.369 1.00 30.09  ? 301  PRO B CA    1 
ATOM   6389 C  C     . PRO B 1 315 ? 14.840  86.393 -41.577 1.00 27.69  ? 301  PRO B C     1 
ATOM   6390 O  O     . PRO B 1 315 ? 15.561  85.730 -42.330 1.00 26.84  ? 301  PRO B O     1 
ATOM   6391 C  CB    . PRO B 1 315 ? 12.711  85.407 -40.553 1.00 30.36  ? 301  PRO B CB    1 
ATOM   6392 C  CG    . PRO B 1 315 ? 12.022  86.524 -39.839 1.00 32.74  ? 301  PRO B CG    1 
ATOM   6393 C  CD    . PRO B 1 315 ? 12.855  86.630 -38.594 1.00 30.61  ? 301  PRO B CD    1 
ATOM   6394 N  N     . SER B 1 316 ? 14.617  87.694 -41.782 1.00 28.27  ? 302  SER B N     1 
ATOM   6395 C  CA    . SER B 1 316 ? 15.208  88.347 -42.948 1.00 29.19  ? 302  SER B CA    1 
ATOM   6396 C  C     . SER B 1 316 ? 16.720  88.501 -42.799 1.00 29.49  ? 302  SER B C     1 
ATOM   6397 O  O     . SER B 1 316 ? 17.435  88.602 -43.804 1.00 27.75  ? 302  SER B O     1 
ATOM   6398 C  CB    . SER B 1 316 ? 14.547  89.710 -43.180 1.00 29.68  ? 302  SER B CB    1 
ATOM   6399 O  OG    . SER B 1 316 ? 15.381  90.569 -43.930 1.00 35.09  ? 302  SER B OG    1 
ATOM   6400 N  N     . GLN B 1 317 ? 17.218  88.480 -41.566 1.00 27.55  ? 303  GLN B N     1 
ATOM   6401 C  CA    . GLN B 1 317 ? 18.646  88.530 -41.307 1.00 27.07  ? 303  GLN B CA    1 
ATOM   6402 C  C     . GLN B 1 317 ? 19.358  87.206 -41.553 1.00 26.29  ? 303  GLN B C     1 
ATOM   6403 O  O     . GLN B 1 317 ? 20.586  87.196 -41.704 1.00 25.44  ? 303  GLN B O     1 
ATOM   6404 C  CB    . GLN B 1 317 ? 18.861  88.953 -39.852 1.00 28.31  ? 303  GLN B CB    1 
ATOM   6405 C  CG    . GLN B 1 317 ? 20.287  89.109 -39.405 1.00 26.71  ? 303  GLN B CG    1 
ATOM   6406 C  CD    . GLN B 1 317 ? 20.348  89.541 -37.972 1.00 29.42  ? 303  GLN B CD    1 
ATOM   6407 O  OE1   . GLN B 1 317 ? 19.341  89.489 -37.264 1.00 31.16  ? 303  GLN B OE1   1 
ATOM   6408 N  NE2   . GLN B 1 317 ? 21.508  90.018 -37.540 1.00 28.60  ? 303  GLN B NE2   1 
ATOM   6409 N  N     . THR B 1 318 ? 18.633  86.097 -41.650 1.00 25.21  ? 304  THR B N     1 
ATOM   6410 C  CA    . THR B 1 318 ? 19.270  84.801 -41.505 1.00 23.84  ? 304  THR B CA    1 
ATOM   6411 C  C     . THR B 1 318 ? 19.051  83.894 -42.710 1.00 22.96  ? 304  THR B C     1 
ATOM   6412 O  O     . THR B 1 318 ? 18.109  84.058 -43.494 1.00 24.59  ? 304  THR B O     1 
ATOM   6413 C  CB    . THR B 1 318 ? 18.778  84.110 -40.231 1.00 25.61  ? 304  THR B CB    1 
ATOM   6414 O  OG1   . THR B 1 318 ? 17.357  84.246 -40.143 1.00 26.93  ? 304  THR B OG1   1 
ATOM   6415 C  CG2   . THR B 1 318 ? 19.421  84.768 -38.992 1.00 25.01  ? 304  THR B CG2   1 
ATOM   6416 N  N     . ILE B 1 319 ? 19.990  82.971 -42.869 1.00 21.95  ? 305  ILE B N     1 
ATOM   6417 C  CA    . ILE B 1 319 ? 19.873  81.806 -43.735 1.00 21.79  ? 305  ILE B CA    1 
ATOM   6418 C  C     . ILE B 1 319 ? 20.166  80.608 -42.855 1.00 21.60  ? 305  ILE B C     1 
ATOM   6419 O  O     . ILE B 1 319 ? 21.173  80.608 -42.142 1.00 21.72  ? 305  ILE B O     1 
ATOM   6420 C  CB    . ILE B 1 319 ? 20.872  81.868 -44.904 1.00 21.87  ? 305  ILE B CB    1 
ATOM   6421 C  CG1   . ILE B 1 319 ? 20.595  83.089 -45.785 1.00 21.49  ? 305  ILE B CG1   1 
ATOM   6422 C  CG2   . ILE B 1 319 ? 20.878  80.535 -45.683 1.00 20.99  ? 305  ILE B CG2   1 
ATOM   6423 C  CD1   . ILE B 1 319 ? 21.573  83.251 -46.953 1.00 22.29  ? 305  ILE B CD1   1 
ATOM   6424 N  N     . GLU B 1 320 ? 19.300  79.595 -42.879 1.00 20.30  ? 306  GLU B N     1 
ATOM   6425 C  CA    . GLU B 1 320 ? 19.534  78.465 -41.992 1.00 22.80  ? 306  GLU B CA    1 
ATOM   6426 C  C     . GLU B 1 320 ? 19.465  77.149 -42.748 1.00 23.31  ? 306  GLU B C     1 
ATOM   6427 O  O     . GLU B 1 320 ? 18.694  76.993 -43.702 1.00 20.98  ? 306  GLU B O     1 
ATOM   6428 C  CB    . GLU B 1 320 ? 18.559  78.466 -40.778 1.00 23.81  ? 306  GLU B CB    1 
ATOM   6429 C  CG    . GLU B 1 320 ? 17.213  77.890 -40.989 1.00 25.62  ? 306  GLU B CG    1 
ATOM   6430 C  CD    . GLU B 1 320 ? 16.394  77.831 -39.699 1.00 26.53  ? 306  GLU B CD    1 
ATOM   6431 O  OE1   . GLU B 1 320 ? 16.587  76.936 -38.842 1.00 26.71  ? 306  GLU B OE1   1 
ATOM   6432 O  OE2   . GLU B 1 320 ? 15.553  78.730 -39.540 1.00 27.80  ? 306  GLU B OE2   1 
ATOM   6433 N  N     . VAL B 1 321 ? 20.289  76.193 -42.305 1.00 22.99  ? 307  VAL B N     1 
ATOM   6434 C  CA    . VAL B 1 321 ? 20.373  74.889 -42.951 1.00 22.59  ? 307  VAL B CA    1 
ATOM   6435 C  C     . VAL B 1 321 ? 20.179  73.804 -41.902 1.00 21.40  ? 307  VAL B C     1 
ATOM   6436 O  O     . VAL B 1 321 ? 20.926  73.721 -40.917 1.00 21.64  ? 307  VAL B O     1 
ATOM   6437 C  CB    . VAL B 1 321 ? 21.688  74.695 -43.727 1.00 21.84  ? 307  VAL B CB    1 
ATOM   6438 C  CG1   . VAL B 1 321 ? 22.798  75.107 -42.915 1.00 25.98  ? 307  VAL B CG1   1 
ATOM   6439 C  CG2   . VAL B 1 321 ? 21.892  73.238 -44.044 1.00 23.13  ? 307  VAL B CG2   1 
ATOM   6440 N  N     . GLN B 1 322 ? 19.173  72.990 -42.114 1.00 22.21  ? 308  GLN B N     1 
ATOM   6441 C  CA    . GLN B 1 322 ? 18.805  71.857 -41.296 1.00 20.95  ? 308  GLN B CA    1 
ATOM   6442 C  C     . GLN B 1 322 ? 19.108  70.584 -42.081 1.00 22.25  ? 308  GLN B C     1 
ATOM   6443 O  O     . GLN B 1 322 ? 19.434  70.647 -43.271 1.00 21.58  ? 308  GLN B O     1 
ATOM   6444 C  CB    . GLN B 1 322 ? 17.315  71.979 -40.924 1.00 21.75  ? 308  GLN B CB    1 
ATOM   6445 C  CG    . GLN B 1 322 ? 16.997  73.192 -40.028 1.00 21.44  ? 308  GLN B CG    1 
ATOM   6446 C  CD    . GLN B 1 322 ? 17.780  73.163 -38.705 1.00 22.76  ? 308  GLN B CD    1 
ATOM   6447 O  OE1   . GLN B 1 322 ? 18.270  72.120 -38.301 1.00 20.88  ? 308  GLN B OE1   1 
ATOM   6448 N  NE2   . GLN B 1 322 ? 17.886  74.312 -38.032 1.00 22.94  ? 308  GLN B NE2   1 
ATOM   6449 N  N     . PRO B 1 323 ? 19.045  69.404 -41.448 1.00 21.68  ? 309  PRO B N     1 
ATOM   6450 C  CA    . PRO B 1 323 ? 19.455  68.182 -42.169 1.00 22.38  ? 309  PRO B CA    1 
ATOM   6451 C  C     . PRO B 1 323 ? 18.754  67.917 -43.506 1.00 24.02  ? 309  PRO B C     1 
ATOM   6452 O  O     . PRO B 1 323 ? 19.388  67.337 -44.403 1.00 24.70  ? 309  PRO B O     1 
ATOM   6453 C  CB    . PRO B 1 323 ? 19.173  67.069 -41.148 1.00 23.42  ? 309  PRO B CB    1 
ATOM   6454 C  CG    . PRO B 1 323 ? 19.326  67.754 -39.817 1.00 24.07  ? 309  PRO B CG    1 
ATOM   6455 C  CD    . PRO B 1 323 ? 18.713  69.118 -40.038 1.00 22.86  ? 309  PRO B CD    1 
ATOM   6456 N  N     . HIS B 1 324 ? 17.479  68.288 -43.683 1.00 22.21  ? 310  HIS B N     1 
ATOM   6457 C  CA    . HIS B 1 324 ? 16.779  67.972 -44.927 1.00 24.51  ? 310  HIS B CA    1 
ATOM   6458 C  C     . HIS B 1 324 ? 16.134  69.175 -45.592 1.00 25.58  ? 310  HIS B C     1 
ATOM   6459 O  O     . HIS B 1 324 ? 15.448  69.007 -46.610 1.00 22.96  ? 310  HIS B O     1 
ATOM   6460 C  CB    . HIS B 1 324 ? 15.691  66.912 -44.697 1.00 24.81  ? 310  HIS B CB    1 
ATOM   6461 C  CG    . HIS B 1 324 ? 16.202  65.653 -44.078 1.00 27.78  ? 310  HIS B CG    1 
ATOM   6462 N  ND1   . HIS B 1 324 ? 17.124  64.841 -44.704 1.00 28.53  ? 310  HIS B ND1   1 
ATOM   6463 C  CD2   . HIS B 1 324 ? 15.932  65.072 -42.886 1.00 26.84  ? 310  HIS B CD2   1 
ATOM   6464 C  CE1   . HIS B 1 324 ? 17.401  63.813 -43.923 1.00 29.32  ? 310  HIS B CE1   1 
ATOM   6465 N  NE2   . HIS B 1 324 ? 16.694  63.932 -42.812 1.00 30.65  ? 310  HIS B NE2   1 
ATOM   6466 N  N     . ALA B 1 325 ? 16.316  70.371 -45.045 1.00 22.63  ? 311  ALA B N     1 
ATOM   6467 C  CA    . ALA B 1 325 ? 15.675  71.560 -45.573 1.00 22.79  ? 311  ALA B CA    1 
ATOM   6468 C  C     . ALA B 1 325 ? 16.494  72.760 -45.134 1.00 21.50  ? 311  ALA B C     1 
ATOM   6469 O  O     . ALA B 1 325 ? 17.149  72.733 -44.085 1.00 19.96  ? 311  ALA B O     1 
ATOM   6470 C  CB    . ALA B 1 325 ? 14.217  71.689 -45.091 1.00 21.97  ? 311  ALA B CB    1 
ATOM   6471 N  N     . SER B 1 326 ? 16.427  73.814 -45.938 1.00 18.60  ? 312  SER B N     1 
ATOM   6472 C  CA    . SER B 1 326 ? 17.120  75.065 -45.673 1.00 20.20  ? 312  SER B CA    1 
ATOM   6473 C  C     . SER B 1 326 ? 16.148  76.216 -45.894 1.00 22.07  ? 312  SER B C     1 
ATOM   6474 O  O     . SER B 1 326 ? 15.122  76.074 -46.573 1.00 20.28  ? 312  SER B O     1 
ATOM   6475 C  CB    . SER B 1 326 ? 18.347  75.228 -46.578 1.00 21.69  ? 312  SER B CB    1 
ATOM   6476 O  OG    . SER B 1 326 ? 19.443  74.483 -46.080 1.00 21.03  ? 312  SER B OG    1 
ATOM   6477 N  N     . ARG B 1 327 ? 16.483  77.363 -45.308 1.00 21.48  ? 313  ARG B N     1 
ATOM   6478 C  CA    . ARG B 1 327 ? 15.614  78.529 -45.308 1.00 21.37  ? 313  ARG B CA    1 
ATOM   6479 C  C     . ARG B 1 327 ? 16.396  79.775 -45.696 1.00 22.57  ? 313  ARG B C     1 
ATOM   6480 O  O     . ARG B 1 327 ? 17.538  79.962 -45.264 1.00 21.56  ? 313  ARG B O     1 
ATOM   6481 C  CB    . ARG B 1 327 ? 14.956  78.727 -43.930 1.00 22.23  ? 313  ARG B CB    1 
ATOM   6482 C  CG    . ARG B 1 327 ? 14.162  80.027 -43.779 1.00 22.18  ? 313  ARG B CG    1 
ATOM   6483 C  CD    . ARG B 1 327 ? 13.663  80.191 -42.348 1.00 24.27  ? 313  ARG B CD    1 
ATOM   6484 N  NE    . ARG B 1 327 ? 14.730  80.363 -41.360 1.00 24.37  ? 313  ARG B NE    1 
ATOM   6485 C  CZ    . ARG B 1 327 ? 15.404  81.488 -41.151 1.00 25.41  ? 313  ARG B CZ    1 
ATOM   6486 N  NH1   . ARG B 1 327 ? 15.194  82.570 -41.884 1.00 23.42  ? 313  ARG B NH1   1 
ATOM   6487 N  NH2   . ARG B 1 327 ? 16.307  81.531 -40.171 1.00 26.00  ? 313  ARG B NH2   1 
ATOM   6488 N  N     . VAL B 1 328 ? 15.794  80.608 -46.544 1.00 20.81  ? 314  VAL B N     1 
ATOM   6489 C  CA    . VAL B 1 328 ? 16.326  81.934 -46.845 1.00 22.32  ? 314  VAL B CA    1 
ATOM   6490 C  C     . VAL B 1 328 ? 15.247  82.941 -46.501 1.00 23.08  ? 314  VAL B C     1 
ATOM   6491 O  O     . VAL B 1 328 ? 14.221  83.022 -47.187 1.00 23.60  ? 314  VAL B O     1 
ATOM   6492 C  CB    . VAL B 1 328 ? 16.765  82.081 -48.307 1.00 23.93  ? 314  VAL B CB    1 
ATOM   6493 C  CG1   . VAL B 1 328 ? 17.209  83.504 -48.572 1.00 24.31  ? 314  VAL B CG1   1 
ATOM   6494 C  CG2   . VAL B 1 328 ? 17.899  81.123 -48.633 1.00 22.95  ? 314  VAL B CG2   1 
ATOM   6495 N  N     . GLY B 1 329 ? 15.479  83.721 -45.466 1.00 23.96  ? 315  GLY B N     1 
ATOM   6496 C  CA    . GLY B 1 329 ? 14.477  84.689 -45.074 1.00 26.63  ? 315  GLY B CA    1 
ATOM   6497 C  C     . GLY B 1 329 ? 13.235  83.949 -44.643 1.00 27.55  ? 315  GLY B C     1 
ATOM   6498 O  O     . GLY B 1 329 ? 13.274  83.116 -43.743 1.00 25.81  ? 315  GLY B O     1 
ATOM   6499 N  N     . ASP B 1 330 ? 12.129  84.197 -45.334 1.00 27.12  ? 316  ASP B N     1 
ATOM   6500 C  CA    . ASP B 1 330 ? 10.845  83.616 -44.973 1.00 27.98  ? 316  ASP B CA    1 
ATOM   6501 C  C     . ASP B 1 330 ? 10.536  82.314 -45.692 1.00 26.36  ? 316  ASP B C     1 
ATOM   6502 O  O     . ASP B 1 330 ? 9.504   81.696 -45.406 1.00 26.68  ? 316  ASP B O     1 
ATOM   6503 C  CB    . ASP B 1 330 ? 9.745   84.620 -45.286 1.00 32.03  ? 316  ASP B CB    1 
ATOM   6504 C  CG    . ASP B 1 330 ? 9.674   85.725 -44.277 1.00 32.84  ? 316  ASP B CG    1 
ATOM   6505 O  OD1   . ASP B 1 330 ? 10.271  85.571 -43.196 1.00 32.08  ? 316  ASP B OD1   1 
ATOM   6506 O  OD2   . ASP B 1 330 ? 9.076   86.773 -44.593 1.00 39.03  ? 316  ASP B OD2   1 
ATOM   6507 N  N     . VAL B 1 331 ? 11.374  81.886 -46.624 1.00 24.09  ? 317  VAL B N     1 
ATOM   6508 C  CA    . VAL B 1 331 ? 11.027  80.798 -47.529 1.00 24.32  ? 317  VAL B CA    1 
ATOM   6509 C  C     . VAL B 1 331 ? 11.841  79.565 -47.184 1.00 23.47  ? 317  VAL B C     1 
ATOM   6510 O  O     . VAL B 1 331 ? 13.072  79.636 -47.075 1.00 20.79  ? 317  VAL B O     1 
ATOM   6511 C  CB    . VAL B 1 331 ? 11.244  81.208 -48.994 1.00 24.27  ? 317  VAL B CB    1 
ATOM   6512 C  CG1   . VAL B 1 331 ? 10.881  80.054 -49.920 1.00 24.03  ? 317  VAL B CG1   1 
ATOM   6513 C  CG2   . VAL B 1 331 ? 10.423  82.451 -49.306 1.00 25.80  ? 317  VAL B CG2   1 
ATOM   6514 N  N     . TRP B 1 332 ? 11.157  78.433 -47.034 1.00 22.28  ? 318  TRP B N     1 
ATOM   6515 C  CA    . TRP B 1 332 ? 11.802  77.151 -46.807 1.00 22.43  ? 318  TRP B CA    1 
ATOM   6516 C  C     . TRP B 1 332 ? 11.907  76.393 -48.124 1.00 23.50  ? 318  TRP B C     1 
ATOM   6517 O  O     . TRP B 1 332 ? 11.018  76.479 -48.981 1.00 22.14  ? 318  TRP B O     1 
ATOM   6518 C  CB    . TRP B 1 332 ? 11.039  76.316 -45.778 1.00 22.64  ? 318  TRP B CB    1 
ATOM   6519 C  CG    . TRP B 1 332 ? 11.290  76.733 -44.366 1.00 23.49  ? 318  TRP B CG    1 
ATOM   6520 C  CD1   . TRP B 1 332 ? 10.556  77.618 -43.637 1.00 24.06  ? 318  TRP B CD1   1 
ATOM   6521 C  CD2   . TRP B 1 332 ? 12.355  76.291 -43.513 1.00 23.35  ? 318  TRP B CD2   1 
ATOM   6522 N  NE1   . TRP B 1 332 ? 11.093  77.757 -42.382 1.00 25.61  ? 318  TRP B NE1   1 
ATOM   6523 C  CE2   . TRP B 1 332 ? 12.193  76.947 -42.274 1.00 24.84  ? 318  TRP B CE2   1 
ATOM   6524 C  CE3   . TRP B 1 332 ? 13.419  75.401 -43.670 1.00 22.68  ? 318  TRP B CE3   1 
ATOM   6525 C  CZ2   . TRP B 1 332 ? 13.061  76.748 -41.201 1.00 25.43  ? 318  TRP B CZ2   1 
ATOM   6526 C  CZ3   . TRP B 1 332 ? 14.284  75.188 -42.586 1.00 23.04  ? 318  TRP B CZ3   1 
ATOM   6527 C  CH2   . TRP B 1 332 ? 14.096  75.865 -41.371 1.00 24.58  ? 318  TRP B CH2   1 
ATOM   6528 N  N     . PHE B 1 333 ? 13.029  75.698 -48.290 1.00 21.67  ? 319  PHE B N     1 
ATOM   6529 C  CA    . PHE B 1 333 ? 13.318  74.841 -49.437 1.00 22.27  ? 319  PHE B CA    1 
ATOM   6530 C  C     . PHE B 1 333 ? 13.559  73.445 -48.878 1.00 23.81  ? 319  PHE B C     1 
ATOM   6531 O  O     . PHE B 1 333 ? 14.609  73.190 -48.283 1.00 22.50  ? 319  PHE B O     1 
ATOM   6532 C  CB    . PHE B 1 333 ? 14.539  75.337 -50.215 1.00 22.17  ? 319  PHE B CB    1 
ATOM   6533 C  CG    . PHE B 1 333 ? 14.431  76.774 -50.672 1.00 22.38  ? 319  PHE B CG    1 
ATOM   6534 C  CD1   . PHE B 1 333 ? 14.720  77.822 -49.806 1.00 22.71  ? 319  PHE B CD1   1 
ATOM   6535 C  CD2   . PHE B 1 333 ? 14.034  77.073 -51.960 1.00 20.76  ? 319  PHE B CD2   1 
ATOM   6536 C  CE1   . PHE B 1 333 ? 14.596  79.129 -50.210 1.00 21.29  ? 319  PHE B CE1   1 
ATOM   6537 C  CE2   . PHE B 1 333 ? 13.915  78.383 -52.375 1.00 21.26  ? 319  PHE B CE2   1 
ATOM   6538 C  CZ    . PHE B 1 333 ? 14.200  79.413 -51.502 1.00 22.64  ? 319  PHE B CZ    1 
ATOM   6539 N  N     . THR B 1 334 ? 12.602  72.544 -49.051 1.00 23.82  ? 320  THR B N     1 
ATOM   6540 C  CA    . THR B 1 334 ? 12.671  71.251 -48.386 1.00 24.89  ? 320  THR B CA    1 
ATOM   6541 C  C     . THR B 1 334 ? 13.181  70.170 -49.336 1.00 26.57  ? 320  THR B C     1 
ATOM   6542 O  O     . THR B 1 334 ? 13.052  70.273 -50.559 1.00 26.15  ? 320  THR B O     1 
ATOM   6543 C  CB    . THR B 1 334 ? 11.298  70.873 -47.811 1.00 24.65  ? 320  THR B CB    1 
ATOM   6544 O  OG1   . THR B 1 334 ? 10.350  70.683 -48.870 1.00 26.18  ? 320  THR B OG1   1 
ATOM   6545 C  CG2   . THR B 1 334 ? 10.787  71.978 -46.892 1.00 23.44  ? 320  THR B CG2   1 
ATOM   6546 N  N     . GLY B 1 335 ? 13.776  69.129 -48.761 1.00 26.85  ? 321  GLY B N     1 
ATOM   6547 C  CA    . GLY B 1 335 ? 14.429  68.116 -49.572 1.00 26.08  ? 321  GLY B CA    1 
ATOM   6548 C  C     . GLY B 1 335 ? 15.785  68.492 -50.135 1.00 27.44  ? 321  GLY B C     1 
ATOM   6549 O  O     . GLY B 1 335 ? 16.111  68.109 -51.267 1.00 27.35  ? 321  GLY B O     1 
ATOM   6550 N  N     . ILE B 1 336 ? 16.578  69.249 -49.385 1.00 25.61  ? 322  ILE B N     1 
ATOM   6551 C  CA    . ILE B 1 336 ? 17.962  69.544 -49.726 1.00 27.86  ? 322  ILE B CA    1 
ATOM   6552 C  C     . ILE B 1 336 ? 18.828  68.979 -48.607 1.00 27.74  ? 322  ILE B C     1 
ATOM   6553 O  O     . ILE B 1 336 ? 18.719  69.426 -47.463 1.00 26.35  ? 322  ILE B O     1 
ATOM   6554 C  CB    . ILE B 1 336 ? 18.225  71.050 -49.882 1.00 26.19  ? 322  ILE B CB    1 
ATOM   6555 C  CG1   . ILE B 1 336 ? 17.318  71.630 -50.944 1.00 27.62  ? 322  ILE B CG1   1 
ATOM   6556 C  CG2   . ILE B 1 336 ? 19.683  71.299 -50.242 1.00 25.49  ? 322  ILE B CG2   1 
ATOM   6557 C  CD1   . ILE B 1 336 ? 17.364  73.105 -50.970 1.00 27.59  ? 322  ILE B CD1   1 
ATOM   6558 N  N     . PRO B 1 337 ? 19.693  68.006 -48.886 1.00 28.38  ? 323  PRO B N     1 
ATOM   6559 C  CA    . PRO B 1 337 ? 20.600  67.506 -47.852 1.00 25.53  ? 323  PRO B CA    1 
ATOM   6560 C  C     . PRO B 1 337 ? 21.479  68.624 -47.324 1.00 26.86  ? 323  PRO B C     1 
ATOM   6561 O  O     . PRO B 1 337 ? 21.949  69.482 -48.072 1.00 25.38  ? 323  PRO B O     1 
ATOM   6562 C  CB    . PRO B 1 337 ? 21.427  66.445 -48.587 1.00 28.50  ? 323  PRO B CB    1 
ATOM   6563 C  CG    . PRO B 1 337 ? 20.553  66.003 -49.706 1.00 32.54  ? 323  PRO B CG    1 
ATOM   6564 C  CD    . PRO B 1 337 ? 19.832  67.255 -50.146 1.00 31.08  ? 323  PRO B CD    1 
ATOM   6565 N  N     . MET B 1 338 ? 21.686  68.610 -46.010 1.00 25.46  ? 324  MET B N     1 
ATOM   6566 C  CA    . MET B 1 338 ? 22.517  69.625 -45.383 1.00 25.16  ? 324  MET B CA    1 
ATOM   6567 C  C     . MET B 1 338 ? 23.924  69.663 -45.984 1.00 25.12  ? 324  MET B C     1 
ATOM   6568 O  O     . MET B 1 338 ? 24.499  70.748 -46.127 1.00 26.47  ? 324  MET B O     1 
ATOM   6569 C  CB    . MET B 1 338 ? 22.467  69.409 -43.869 1.00 23.82  ? 324  MET B CB    1 
ATOM   6570 C  CG    . MET B 1 338 ? 23.529  70.011 -43.033 1.00 25.52  ? 324  MET B CG    1 
ATOM   6571 S  SD    . MET B 1 338 ? 23.451  69.260 -41.372 1.00 26.16  ? 324  MET B SD    1 
ATOM   6572 C  CE    . MET B 1 338 ? 23.927  70.699 -40.431 1.00 22.70  ? 324  MET B CE    1 
ATOM   6573 N  N     . LEU B 1 339 ? 24.467  68.519 -46.412 1.00 28.45  ? 325  LEU B N     1 
ATOM   6574 C  CA    . LEU B 1 339 ? 25.758  68.542 -47.097 1.00 28.32  ? 325  LEU B CA    1 
ATOM   6575 C  C     . LEU B 1 339 ? 25.703  69.444 -48.327 1.00 25.81  ? 325  LEU B C     1 
ATOM   6576 O  O     . LEU B 1 339 ? 26.561  70.318 -48.504 1.00 25.24  ? 325  LEU B O     1 
ATOM   6577 C  CB    . LEU B 1 339 ? 26.185  67.129 -47.512 1.00 31.15  ? 325  LEU B CB    1 
ATOM   6578 C  CG    . LEU B 1 339 ? 27.554  67.007 -48.221 1.00 32.63  ? 325  LEU B CG    1 
ATOM   6579 C  CD1   . LEU B 1 339 ? 28.606  67.998 -47.704 1.00 31.50  ? 325  LEU B CD1   1 
ATOM   6580 C  CD2   . LEU B 1 339 ? 28.099  65.590 -48.207 1.00 35.00  ? 325  LEU B CD2   1 
ATOM   6581 N  N     . GLN B 1 340 ? 24.692  69.254 -49.185 1.00 25.69  ? 326  GLN B N     1 
ATOM   6582 C  CA    . GLN B 1 340 ? 24.599  70.067 -50.401 1.00 28.72  ? 326  GLN B CA    1 
ATOM   6583 C  C     . GLN B 1 340 ? 24.304  71.525 -50.103 1.00 25.78  ? 326  GLN B C     1 
ATOM   6584 O  O     . GLN B 1 340 ? 24.807  72.413 -50.797 1.00 25.44  ? 326  GLN B O     1 
ATOM   6585 C  CB    . GLN B 1 340 ? 23.506  69.573 -51.338 1.00 29.95  ? 326  GLN B CB    1 
ATOM   6586 C  CG    . GLN B 1 340 ? 23.580  68.184 -51.844 1.00 34.25  ? 326  GLN B CG    1 
ATOM   6587 C  CD    . GLN B 1 340 ? 22.684  68.043 -53.065 1.00 33.70  ? 326  GLN B CD    1 
ATOM   6588 O  OE1   . GLN B 1 340 ? 21.470  67.923 -52.946 1.00 34.77  ? 326  GLN B OE1   1 
ATOM   6589 N  NE2   . GLN B 1 340 ? 23.277  68.131 -54.242 1.00 35.62  ? 326  GLN B NE2   1 
ATOM   6590 N  N     . ALA B 1 341 ? 23.443  71.790 -49.117 1.00 25.38  ? 327  ALA B N     1 
ATOM   6591 C  CA    . ALA B 1 341 ? 23.172  73.170 -48.737 1.00 23.11  ? 327  ALA B CA    1 
ATOM   6592 C  C     . ALA B 1 341 ? 24.454  73.871 -48.320 1.00 24.09  ? 327  ALA B C     1 
ATOM   6593 O  O     . ALA B 1 341 ? 24.731  74.993 -48.761 1.00 22.03  ? 327  ALA B O     1 
ATOM   6594 C  CB    . ALA B 1 341 ? 22.137  73.219 -47.617 1.00 22.61  ? 327  ALA B CB    1 
ATOM   6595 N  N     . ILE B 1 342 ? 25.274  73.205 -47.500 1.00 23.79  ? 328  ILE B N     1 
ATOM   6596 C  CA    . ILE B 1 342 ? 26.534  73.806 -47.066 1.00 22.76  ? 328  ILE B CA    1 
ATOM   6597 C  C     . ILE B 1 342 ? 27.459  74.021 -48.256 1.00 23.31  ? 328  ILE B C     1 
ATOM   6598 O  O     . ILE B 1 342 ? 28.030  75.104 -48.436 1.00 22.43  ? 328  ILE B O     1 
ATOM   6599 C  CB    . ILE B 1 342 ? 27.195  72.933 -45.985 1.00 23.71  ? 328  ILE B CB    1 
ATOM   6600 C  CG1   . ILE B 1 342 ? 26.447  73.101 -44.662 1.00 21.48  ? 328  ILE B CG1   1 
ATOM   6601 C  CG2   . ILE B 1 342 ? 28.670  73.287 -45.823 1.00 21.95  ? 328  ILE B CG2   1 
ATOM   6602 C  CD1   . ILE B 1 342 ? 26.730  72.008 -43.663 1.00 24.67  ? 328  ILE B CD1   1 
ATOM   6603 N  N     . GLU B 1 343 ? 27.604  72.998 -49.101 1.00 23.49  ? 329  GLU B N     1 
ATOM   6604 C  CA    . GLU B 1 343 ? 28.454  73.140 -50.279 1.00 25.78  ? 329  GLU B CA    1 
ATOM   6605 C  C     . GLU B 1 343 ? 27.997  74.303 -51.138 1.00 25.38  ? 329  GLU B C     1 
ATOM   6606 O  O     . GLU B 1 343 ? 28.821  75.097 -51.607 1.00 24.92  ? 329  GLU B O     1 
ATOM   6607 C  CB    . GLU B 1 343 ? 28.464  71.849 -51.095 1.00 28.65  ? 329  GLU B CB    1 
ATOM   6608 C  CG    . GLU B 1 343 ? 29.045  70.656 -50.358 1.00 30.65  ? 329  GLU B CG    1 
ATOM   6609 C  CD    . GLU B 1 343 ? 28.909  69.385 -51.158 1.00 35.88  ? 329  GLU B CD    1 
ATOM   6610 O  OE1   . GLU B 1 343 ? 27.877  69.242 -51.850 1.00 35.32  ? 329  GLU B OE1   1 
ATOM   6611 O  OE2   . GLU B 1 343 ? 29.827  68.537 -51.104 1.00 39.91  ? 329  GLU B OE2   1 
ATOM   6612 N  N     . THR B 1 344 ? 26.685  74.433 -51.339 1.00 23.07  ? 330  THR B N     1 
ATOM   6613 C  CA    . THR B 1 344 ? 26.168  75.568 -52.100 1.00 23.34  ? 330  THR B CA    1 
ATOM   6614 C  C     . THR B 1 344 ? 26.595  76.880 -51.460 1.00 24.34  ? 330  THR B C     1 
ATOM   6615 O  O     . THR B 1 344 ? 27.169  77.751 -52.122 1.00 25.53  ? 330  THR B O     1 
ATOM   6616 C  CB    . THR B 1 344 ? 24.639  75.490 -52.173 1.00 23.66  ? 330  THR B CB    1 
ATOM   6617 O  OG1   . THR B 1 344 ? 24.258  74.277 -52.828 1.00 25.61  ? 330  THR B OG1   1 
ATOM   6618 C  CG2   . THR B 1 344 ? 24.069  76.681 -52.949 1.00 20.51  ? 330  THR B CG2   1 
ATOM   6619 N  N     . LEU B 1 345 ? 26.380  77.010 -50.147 1.00 23.13  ? 331  LEU B N     1 
ATOM   6620 C  CA    . LEU B 1 345 ? 26.684  78.264 -49.462 1.00 23.65  ? 331  LEU B CA    1 
ATOM   6621 C  C     . LEU B 1 345 ? 28.186  78.561 -49.441 1.00 25.10  ? 331  LEU B C     1 
ATOM   6622 O  O     . LEU B 1 345 ? 28.582  79.730 -49.503 1.00 24.57  ? 331  LEU B O     1 
ATOM   6623 C  CB    . LEU B 1 345 ? 26.123  78.210 -48.044 1.00 22.54  ? 331  LEU B CB    1 
ATOM   6624 C  CG    . LEU B 1 345 ? 24.604  78.296 -47.858 1.00 23.48  ? 331  LEU B CG    1 
ATOM   6625 C  CD1   . LEU B 1 345 ? 24.241  78.111 -46.391 1.00 20.53  ? 331  LEU B CD1   1 
ATOM   6626 C  CD2   . LEU B 1 345 ? 24.049  79.624 -48.376 1.00 20.71  ? 331  LEU B CD2   1 
ATOM   6627 N  N     . VAL B 1 346 ? 29.030  77.527 -49.371 1.00 24.72  ? 332  VAL B N     1 
ATOM   6628 C  CA    . VAL B 1 346 ? 30.478  77.735 -49.418 1.00 26.08  ? 332  VAL B CA    1 
ATOM   6629 C  C     . VAL B 1 346 ? 30.886  78.343 -50.755 1.00 29.16  ? 332  VAL B C     1 
ATOM   6630 O  O     . VAL B 1 346 ? 31.625  79.336 -50.807 1.00 29.29  ? 332  VAL B O     1 
ATOM   6631 C  CB    . VAL B 1 346 ? 31.221  76.413 -49.141 1.00 26.74  ? 332  VAL B CB    1 
ATOM   6632 C  CG1   . VAL B 1 346 ? 32.688  76.493 -49.594 1.00 27.43  ? 332  VAL B CG1   1 
ATOM   6633 C  CG2   . VAL B 1 346 ? 31.126  76.039 -47.661 1.00 24.63  ? 332  VAL B CG2   1 
ATOM   6634 N  N     . GLU B 1 347 ? 30.396  77.766 -51.856 1.00 28.88  ? 333  GLU B N     1 
ATOM   6635 C  CA    . GLU B 1 347 ? 30.711  78.299 -53.181 1.00 32.99  ? 333  GLU B CA    1 
ATOM   6636 C  C     . GLU B 1 347 ? 30.204  79.730 -53.330 1.00 34.02  ? 333  GLU B C     1 
ATOM   6637 O  O     . GLU B 1 347 ? 30.918  80.607 -53.832 1.00 33.07  ? 333  GLU B O     1 
ATOM   6638 C  CB    . GLU B 1 347 ? 30.130  77.386 -54.263 1.00 35.42  ? 333  GLU B CB    1 
ATOM   6639 C  CG    . GLU B 1 347 ? 30.533  77.727 -55.709 1.00 41.75  ? 333  GLU B CG    1 
ATOM   6640 C  CD    . GLU B 1 347 ? 32.024  78.064 -55.862 1.00 63.31  ? 333  GLU B CD    1 
ATOM   6641 O  OE1   . GLU B 1 347 ? 32.370  79.268 -55.938 1.00 57.93  ? 333  GLU B OE1   1 
ATOM   6642 O  OE2   . GLU B 1 347 ? 32.853  77.124 -55.879 1.00 49.86  ? 333  GLU B OE2   1 
ATOM   6643 N  N     . LEU B 1 348 ? 28.964  79.986 -52.892 1.00 30.97  ? 334  LEU B N     1 
ATOM   6644 C  CA    . LEU B 1 348 ? 28.405  81.332 -52.989 1.00 30.33  ? 334  LEU B CA    1 
ATOM   6645 C  C     . LEU B 1 348 ? 29.216  82.330 -52.167 1.00 34.05  ? 334  LEU B C     1 
ATOM   6646 O  O     . LEU B 1 348 ? 29.482  83.451 -52.618 1.00 35.55  ? 334  LEU B O     1 
ATOM   6647 C  CB    . LEU B 1 348 ? 26.948  81.311 -52.522 1.00 27.63  ? 334  LEU B CB    1 
ATOM   6648 C  CG    . LEU B 1 348 ? 25.987  80.570 -53.455 1.00 27.06  ? 334  LEU B CG    1 
ATOM   6649 C  CD1   . LEU B 1 348 ? 24.544  80.632 -52.946 1.00 23.57  ? 334  LEU B CD1   1 
ATOM   6650 C  CD2   . LEU B 1 348 ? 26.104  81.164 -54.858 1.00 26.90  ? 334  LEU B CD2   1 
ATOM   6651 N  N     . CYS B 1 349 ? 29.651  81.925 -50.970 1.00 32.90  ? 335  CYS B N     1 
ATOM   6652 C  CA    . CYS B 1 349 ? 30.441  82.810 -50.119 1.00 35.04  ? 335  CYS B CA    1 
ATOM   6653 C  C     . CYS B 1 349 ? 31.781  83.132 -50.762 1.00 40.01  ? 335  CYS B C     1 
ATOM   6654 O  O     . CYS B 1 349 ? 32.287  84.254 -50.639 1.00 43.70  ? 335  CYS B O     1 
ATOM   6655 C  CB    . CYS B 1 349 ? 30.644  82.171 -48.747 1.00 31.60  ? 335  CYS B CB    1 
ATOM   6656 S  SG    . CYS B 1 349 ? 29.236  82.427 -47.627 1.00 29.20  ? 335  CYS B SG    1 
ATOM   6657 N  N     . LYS B 1 350 ? 32.362  82.134 -51.407 1.00 36.71  ? 336  LYS B N     1 
ATOM   6658 C  CA    . LYS B 1 350 ? 33.612  82.274 -52.108 1.00 40.33  ? 336  LYS B CA    1 
ATOM   6659 C  C     . LYS B 1 350 ? 33.502  83.372 -53.156 1.00 43.82  ? 336  LYS B C     1 
ATOM   6660 O  O     . LYS B 1 350 ? 34.424  84.111 -53.388 1.00 46.05  ? 336  LYS B O     1 
ATOM   6661 C  CB    . LYS B 1 350 ? 34.014  80.921 -52.709 1.00 40.52  ? 336  LYS B CB    1 
ATOM   6662 C  CG    . LYS B 1 350 ? 34.790  80.065 -51.731 1.00 37.48  ? 336  LYS B CG    1 
ATOM   6663 C  CD    . LYS B 1 350 ? 35.254  78.775 -52.341 1.00 39.40  ? 336  LYS B CD    1 
ATOM   6664 C  CE    . LYS B 1 350 ? 35.719  77.816 -51.277 1.00 37.54  ? 336  LYS B CE    1 
ATOM   6665 N  NZ    . LYS B 1 350 ? 35.698  76.447 -51.842 1.00 40.69  ? 336  LYS B NZ    1 
ATOM   6666 N  N     . GLN B 1 351 ? 32.317  83.503 -53.713 1.00 44.06  ? 337  GLN B N     1 
ATOM   6667 C  CA    . GLN B 1 351 ? 31.944  84.490 -54.706 1.00 46.08  ? 337  GLN B CA    1 
ATOM   6668 C  C     . GLN B 1 351 ? 31.705  85.906 -54.159 1.00 49.38  ? 337  GLN B C     1 
ATOM   6669 O  O     . GLN B 1 351 ? 31.514  86.806 -54.907 1.00 53.29  ? 337  GLN B O     1 
ATOM   6670 C  CB    . GLN B 1 351 ? 30.694  83.998 -55.435 1.00 45.07  ? 337  GLN B CB    1 
ATOM   6671 C  CG    . GLN B 1 351 ? 30.983  83.405 -56.780 1.00 42.51  ? 337  GLN B CG    1 
ATOM   6672 C  CD    . GLN B 1 351 ? 29.908  82.516 -57.328 1.00 44.34  ? 337  GLN B CD    1 
ATOM   6673 O  OE1   . GLN B 1 351 ? 30.158  81.326 -57.534 1.00 41.64  ? 337  GLN B OE1   1 
ATOM   6674 N  NE2   . GLN B 1 351 ? 28.749  83.056 -57.613 1.00 47.04  ? 337  GLN B NE2   1 
ATOM   6675 N  N     . HIS B 1 352 ? 31.631  86.104 -52.864 1.00 51.72  ? 338  HIS B N     1 
ATOM   6676 C  CA    . HIS B 1 352 ? 31.439  87.433 -52.288 1.00 57.26  ? 338  HIS B CA    1 
ATOM   6677 C  C     . HIS B 1 352 ? 32.399  87.638 -51.104 1.00 76.96  ? 338  HIS B C     1 
ATOM   6678 O  O     . HIS B 1 352 ? 33.595  87.897 -51.251 1.00 87.23  ? 338  HIS B O     1 
ATOM   6679 C  CB    . HIS B 1 352 ? 29.999  87.650 -51.819 1.00 56.39  ? 338  HIS B CB    1 
ATOM   6680 C  CG    . HIS B 1 352 ? 28.965  87.421 -52.884 1.00 45.68  ? 338  HIS B CG    1 
ATOM   6681 N  ND1   . HIS B 1 352 ? 28.798  88.269 -53.949 1.00 44.56  ? 338  HIS B ND1   1 
ATOM   6682 C  CD2   . HIS B 1 352 ? 28.106  86.398 -53.085 1.00 41.44  ? 338  HIS B CD2   1 
ATOM   6683 C  CE1   . HIS B 1 352 ? 27.856  87.796 -54.739 1.00 42.85  ? 338  HIS B CE1   1 
ATOM   6684 N  NE2   . HIS B 1 352 ? 27.429  86.656 -54.247 1.00 40.16  ? 338  HIS B NE2   1 
ATOM   6685 N  N     . VAL B 1 353 ? 31.822  87.471 -49.931 1.00 67.49  ? 339  VAL B N     1 
ATOM   6686 C  CA    . VAL B 1 353 ? 32.482  87.559 -48.621 1.00 74.25  ? 339  VAL B CA    1 
ATOM   6687 C  C     . VAL B 1 353 ? 33.925  88.039 -48.670 1.00 76.83  ? 339  VAL B C     1 
ATOM   6688 O  O     . VAL B 1 353 ? 34.885  87.295 -48.802 1.00 77.80  ? 339  VAL B O     1 
ATOM   6689 C  CB    . VAL B 1 353 ? 32.274  86.282 -47.778 1.00 63.68  ? 339  VAL B CB    1 
ATOM   6690 C  CG1   . VAL B 1 353 ? 32.757  86.491 -46.364 1.00 52.99  ? 339  VAL B CG1   1 
ATOM   6691 C  CG2   . VAL B 1 353 ? 30.793  85.892 -47.740 1.00 54.44  ? 339  VAL B CG2   1 
ATOM   6692 N  N     . HIS B 1 354 ? 34.013  89.349 -48.654 1.00 78.63  ? 340  HIS B N     1 
ATOM   6693 C  CA    . HIS B 1 354 ? 35.258  89.961 -48.827 1.00 83.75  ? 340  HIS B CA    1 
ATOM   6694 C  C     . HIS B 1 354 ? 35.440  91.123 -47.817 1.00 92.26  ? 340  HIS B C     1 
ATOM   6695 O  O     . HIS B 1 354 ? 34.550  91.930 -47.669 1.00 114.56 ? 340  HIS B O     1 
ATOM   6696 C  CB    . HIS B 1 354 ? 35.350  90.297 -50.325 1.00 80.46  ? 340  HIS B CB    1 
ATOM   6697 C  CG    . HIS B 1 354 ? 34.151  91.015 -50.873 1.00 77.03  ? 340  HIS B CG    1 
ATOM   6698 N  ND1   . HIS B 1 354 ? 33.351  91.830 -50.105 1.00 72.85  ? 340  HIS B ND1   1 
ATOM   6699 C  CD2   . HIS B 1 354 ? 33.651  91.089 -52.134 1.00 78.78  ? 340  HIS B CD2   1 
ATOM   6700 C  CE1   . HIS B 1 354 ? 32.388  92.337 -50.851 1.00 68.32  ? 340  HIS B CE1   1 
ATOM   6701 N  NE2   . HIS B 1 354 ? 32.567  91.933 -52.092 1.00 70.88  ? 340  HIS B NE2   1 
ATOM   6702 N  N     . ASP B 1 355 ? 36.561  91.035 -47.089 1.00 88.00  ? 341  ASP B N     1 
ATOM   6703 C  CA    . ASP B 1 355 ? 37.150  91.876 -46.016 1.00 88.97  ? 341  ASP B CA    1 
ATOM   6704 C  C     . ASP B 1 355 ? 37.157  91.269 -44.613 1.00 84.99  ? 341  ASP B C     1 
ATOM   6705 O  O     . ASP B 1 355 ? 36.232  91.365 -43.845 1.00 79.34  ? 341  ASP B O     1 
ATOM   6706 C  CB    . ASP B 1 355 ? 36.841  93.375 -46.003 1.00 96.09  ? 341  ASP B CB    1 
ATOM   6707 C  CG    . ASP B 1 355 ? 38.065  94.206 -46.201 1.00 101.63 ? 341  ASP B CG    1 
ATOM   6708 O  OD1   . ASP B 1 355 ? 39.154  93.681 -45.985 1.00 106.84 ? 341  ASP B OD1   1 
ATOM   6709 O  OD2   . ASP B 1 355 ? 37.919  95.399 -46.564 1.00 97.06  ? 341  ASP B OD2   1 
ATOM   6710 N  N     . THR B 1 356 ? 38.296  90.706 -44.316 1.00 81.14  ? 342  THR B N     1 
ATOM   6711 C  CA    . THR B 1 356 ? 38.551  89.977 -43.108 1.00 74.25  ? 342  THR B CA    1 
ATOM   6712 C  C     . THR B 1 356 ? 38.320  90.683 -41.785 1.00 71.13  ? 342  THR B C     1 
ATOM   6713 O  O     . THR B 1 356 ? 38.558  91.864 -41.643 1.00 70.81  ? 342  THR B O     1 
ATOM   6714 C  CB    . THR B 1 356 ? 39.940  89.325 -43.127 1.00 76.77  ? 342  THR B CB    1 
ATOM   6715 O  OG1   . THR B 1 356 ? 40.878  90.136 -42.414 1.00 74.33  ? 342  THR B OG1   1 
ATOM   6716 C  CG2   . THR B 1 356 ? 40.427  89.088 -44.517 1.00 73.61  ? 342  THR B CG2   1 
ATOM   6717 N  N     . PRO B 1 357 ? 37.872  89.875 -40.834 1.00 64.95  ? 343  PRO B N     1 
ATOM   6718 C  CA    . PRO B 1 357 ? 37.538  90.268 -39.483 1.00 61.38  ? 343  PRO B CA    1 
ATOM   6719 C  C     . PRO B 1 357 ? 38.738  90.802 -38.751 1.00 60.68  ? 343  PRO B C     1 
ATOM   6720 O  O     . PRO B 1 357 ? 38.455  91.548 -37.861 1.00 61.00  ? 343  PRO B O     1 
ATOM   6721 C  CB    . PRO B 1 357 ? 37.098  88.945 -38.837 1.00 50.33  ? 343  PRO B CB    1 
ATOM   6722 C  CG    . PRO B 1 357 ? 37.503  87.874 -39.782 1.00 48.04  ? 343  PRO B CG    1 
ATOM   6723 C  CD    . PRO B 1 357 ? 38.287  88.477 -40.892 1.00 58.17  ? 343  PRO B CD    1 
ATOM   6724 N  N     . PRO B 1 370 ? 47.441  84.681 -11.410 1.00 76.79  ? 356  PRO B N     1 
ATOM   6725 C  CA    . PRO B 1 370 ? 47.406  83.633 -10.385 1.00 77.82  ? 356  PRO B CA    1 
ATOM   6726 C  C     . PRO B 1 370 ? 47.124  84.169 -8.971  1.00 76.79  ? 356  PRO B C     1 
ATOM   6727 O  O     . PRO B 1 370 ? 47.932  84.873 -8.361  1.00 76.95  ? 356  PRO B O     1 
ATOM   6728 C  CB    . PRO B 1 370 ? 48.801  83.034 -10.489 1.00 89.75  ? 356  PRO B CB    1 
ATOM   6729 C  CG    . PRO B 1 370 ? 49.061  83.073 -11.973 1.00 77.64  ? 356  PRO B CG    1 
ATOM   6730 C  CD    . PRO B 1 370 ? 48.464  84.397 -12.436 1.00 76.34  ? 356  PRO B CD    1 
ATOM   6731 N  N     . ASP B 1 371 ? 45.972  83.753 -8.459  1.00 71.20  ? 357  ASP B N     1 
ATOM   6732 C  CA    . ASP B 1 371 ? 45.309  84.278 -7.271  1.00 69.65  ? 357  ASP B CA    1 
ATOM   6733 C  C     . ASP B 1 371 ? 45.739  83.553 -5.993  1.00 63.31  ? 357  ASP B C     1 
ATOM   6734 O  O     . ASP B 1 371 ? 46.865  83.056 -5.875  1.00 61.87  ? 357  ASP B O     1 
ATOM   6735 C  CB    . ASP B 1 371 ? 43.792  84.163 -7.456  1.00 63.55  ? 357  ASP B CB    1 
ATOM   6736 C  CG    . ASP B 1 371 ? 43.109  85.504 -7.592  1.00 68.52  ? 357  ASP B CG    1 
ATOM   6737 O  OD1   . ASP B 1 371 ? 43.759  86.548 -7.355  1.00 76.68  ? 357  ASP B OD1   1 
ATOM   6738 O  OD2   . ASP B 1 371 ? 41.902  85.501 -7.920  1.00 58.65  ? 357  ASP B OD2   1 
ATOM   6739 N  N     . GLY B 1 372 ? 44.869  83.618 -4.979  1.00 57.64  ? 358  GLY B N     1 
ATOM   6740 C  CA    . GLY B 1 372 ? 44.833  82.702 -3.853  1.00 48.30  ? 358  GLY B CA    1 
ATOM   6741 C  C     . GLY B 1 372 ? 43.630  81.761 -3.893  1.00 44.63  ? 358  GLY B C     1 
ATOM   6742 O  O     . GLY B 1 372 ? 43.649  80.755 -4.610  1.00 42.99  ? 358  GLY B O     1 
ATOM   6743 N  N     . SER B 1 373 ? 42.574  82.085 -3.143  1.00 41.17  ? 359  SER B N     1 
ATOM   6744 C  CA    . SER B 1 373 ? 41.441  81.181 -2.946  1.00 38.87  ? 359  SER B CA    1 
ATOM   6745 C  C     . SER B 1 373 ? 40.642  80.944 -4.233  1.00 37.79  ? 359  SER B C     1 
ATOM   6746 O  O     . SER B 1 373 ? 40.416  81.866 -5.024  1.00 35.45  ? 359  SER B O     1 
ATOM   6747 C  CB    . SER B 1 373 ? 40.520  81.742 -1.860  1.00 41.41  ? 359  SER B CB    1 
ATOM   6748 O  OG    . SER B 1 373 ? 39.802  80.712 -1.201  1.00 43.63  ? 359  SER B OG    1 
ATOM   6749 N  N     . LEU B 1 374 ? 40.169  79.707 -4.412  1.00 34.61  ? 360  LEU B N     1 
ATOM   6750 C  CA    . LEU B 1 374 ? 39.500  79.322 -5.653  1.00 35.45  ? 360  LEU B CA    1 
ATOM   6751 C  C     . LEU B 1 374 ? 38.112  79.945 -5.769  1.00 35.93  ? 360  LEU B C     1 
ATOM   6752 O  O     . LEU B 1 374 ? 37.278  79.828 -4.864  1.00 35.93  ? 360  LEU B O     1 
ATOM   6753 C  CB    . LEU B 1 374 ? 39.379  77.801 -5.749  1.00 33.07  ? 360  LEU B CB    1 
ATOM   6754 C  CG    . LEU B 1 374 ? 40.561  76.999 -6.295  1.00 33.69  ? 360  LEU B CG    1 
ATOM   6755 C  CD1   . LEU B 1 374 ? 40.318  75.514 -6.056  1.00 30.62  ? 360  LEU B CD1   1 
ATOM   6756 C  CD2   . LEU B 1 374 ? 40.785  77.274 -7.763  1.00 32.05  ? 360  LEU B CD2   1 
ATOM   6757 N  N     . THR B 1 375 ? 37.860  80.589 -6.899  1.00 36.02  ? 361  THR B N     1 
ATOM   6758 C  CA    . THR B 1 375 ? 36.534  81.046 -7.280  1.00 36.45  ? 361  THR B CA    1 
ATOM   6759 C  C     . THR B 1 375 ? 36.199  80.422 -8.624  1.00 36.55  ? 361  THR B C     1 
ATOM   6760 O  O     . THR B 1 375 ? 37.061  79.846 -9.292  1.00 35.23  ? 361  THR B O     1 
ATOM   6761 C  CB    . THR B 1 375 ? 36.465  82.573 -7.392  1.00 36.72  ? 361  THR B CB    1 
ATOM   6762 O  OG1   . THR B 1 375 ? 37.396  83.006 -8.391  1.00 36.89  ? 361  THR B OG1   1 
ATOM   6763 C  CG2   . THR B 1 375 ? 36.821  83.233 -6.062  1.00 35.63  ? 361  THR B CG2   1 
ATOM   6764 N  N     . GLN B 1 376 ? 34.932  80.549 -9.028  1.00 37.56  ? 362  GLN B N     1 
ATOM   6765 C  CA    . GLN B 1 376 ? 34.570  80.183 -10.394 1.00 38.46  ? 362  GLN B CA    1 
ATOM   6766 C  C     . GLN B 1 376 ? 35.463  80.914 -11.387 1.00 36.02  ? 362  GLN B C     1 
ATOM   6767 O  O     . GLN B 1 376 ? 35.965  80.321 -12.346 1.00 33.35  ? 362  GLN B O     1 
ATOM   6768 C  CB    . GLN B 1 376 ? 33.098  80.499 -10.654 1.00 41.79  ? 362  GLN B CB    1 
ATOM   6769 C  CG    . GLN B 1 376 ? 32.138  79.558 -9.952  1.00 44.60  ? 362  GLN B CG    1 
ATOM   6770 C  CD    . GLN B 1 376 ? 31.960  78.248 -10.692 1.00 45.60  ? 362  GLN B CD    1 
ATOM   6771 O  OE1   . GLN B 1 376 ? 32.122  78.186 -11.915 1.00 43.93  ? 362  GLN B OE1   1 
ATOM   6772 N  NE2   . GLN B 1 376 ? 31.617  77.191 -9.957  1.00 41.34  ? 362  GLN B NE2   1 
ATOM   6773 N  N     . ASP B 1 377 ? 35.714  82.196 -11.133 1.00 37.27  ? 363  ASP B N     1 
ATOM   6774 C  CA    . ASP B 1 377 ? 36.488  83.017 -12.053 1.00 38.13  ? 363  ASP B CA    1 
ATOM   6775 C  C     . ASP B 1 377 ? 37.902  82.481 -12.251 1.00 37.16  ? 363  ASP B C     1 
ATOM   6776 O  O     . ASP B 1 377 ? 38.333  82.243 -13.386 1.00 37.03  ? 363  ASP B O     1 
ATOM   6777 C  CB    . ASP B 1 377 ? 36.529  84.445 -11.521 1.00 41.83  ? 363  ASP B CB    1 
ATOM   6778 C  CG    . ASP B 1 377 ? 36.937  85.437 -12.568 1.00 46.78  ? 363  ASP B CG    1 
ATOM   6779 O  OD1   . ASP B 1 377 ? 38.151  85.537 -12.850 1.00 46.42  ? 363  ASP B OD1   1 
ATOM   6780 O  OD2   . ASP B 1 377 ? 36.042  86.106 -13.123 1.00 58.63  ? 363  ASP B OD2   1 
ATOM   6781 N  N     . ASN B 1 378 ? 38.653  82.295 -11.158 1.00 35.19  ? 364  ASN B N     1 
ATOM   6782 C  CA    . ASN B 1 378 ? 40.042  81.877 -11.326 1.00 33.50  ? 364  ASN B CA    1 
ATOM   6783 C  C     . ASN B 1 378 ? 40.166  80.392 -11.645 1.00 30.80  ? 364  ASN B C     1 
ATOM   6784 O  O     . ASN B 1 378 ? 41.193  79.971 -12.183 1.00 31.11  ? 364  ASN B O     1 
ATOM   6785 C  CB    . ASN B 1 378 ? 40.883  82.252 -10.090 1.00 34.24  ? 364  ASN B CB    1 
ATOM   6786 C  CG    . ASN B 1 378 ? 40.399  81.597 -8.793  1.00 35.81  ? 364  ASN B CG    1 
ATOM   6787 O  OD1   . ASN B 1 378 ? 39.777  80.537 -8.795  1.00 35.28  ? 364  ASN B OD1   1 
ATOM   6788 N  ND2   . ASN B 1 378 ? 40.688  82.249 -7.673  1.00 37.60  ? 364  ASN B ND2   1 
ATOM   6789 N  N     . PHE B 1 379 ? 39.135  79.602 -11.360 1.00 31.39  ? 365  PHE B N     1 
ATOM   6790 C  CA    . PHE B 1 379 ? 39.147  78.200 -11.762 1.00 30.25  ? 365  PHE B CA    1 
ATOM   6791 C  C     . PHE B 1 379 ? 39.120  78.058 -13.279 1.00 29.09  ? 365  PHE B C     1 
ATOM   6792 O  O     . PHE B 1 379 ? 39.922  77.316 -13.856 1.00 27.90  ? 365  PHE B O     1 
ATOM   6793 C  CB    . PHE B 1 379 ? 37.962  77.458 -11.154 1.00 28.80  ? 365  PHE B CB    1 
ATOM   6794 C  CG    . PHE B 1 379 ? 37.715  76.117 -11.791 1.00 28.78  ? 365  PHE B CG    1 
ATOM   6795 C  CD1   . PHE B 1 379 ? 38.442  75.011 -11.393 1.00 26.28  ? 365  PHE B CD1   1 
ATOM   6796 C  CD2   . PHE B 1 379 ? 36.798  75.979 -12.829 1.00 27.22  ? 365  PHE B CD2   1 
ATOM   6797 C  CE1   . PHE B 1 379 ? 38.238  73.784 -11.990 1.00 26.46  ? 365  PHE B CE1   1 
ATOM   6798 C  CE2   . PHE B 1 379 ? 36.595  74.756 -13.433 1.00 26.10  ? 365  PHE B CE2   1 
ATOM   6799 C  CZ    . PHE B 1 379 ? 37.309  73.661 -13.017 1.00 24.72  ? 365  PHE B CZ    1 
ATOM   6800 N  N     . TRP B 1 380 ? 38.169  78.727 -13.939 1.00 29.44  ? 366  TRP B N     1 
ATOM   6801 C  CA    . TRP B 1 380 ? 38.089  78.629 -15.394 1.00 29.46  ? 366  TRP B CA    1 
ATOM   6802 C  C     . TRP B 1 380 ? 39.306  79.259 -16.058 1.00 29.56  ? 366  TRP B C     1 
ATOM   6803 O  O     . TRP B 1 380 ? 39.763  78.771 -17.096 1.00 29.93  ? 366  TRP B O     1 
ATOM   6804 C  CB    . TRP B 1 380 ? 36.774  79.249 -15.893 1.00 28.33  ? 366  TRP B CB    1 
ATOM   6805 C  CG    . TRP B 1 380 ? 35.595  78.400 -15.461 1.00 28.42  ? 366  TRP B CG    1 
ATOM   6806 C  CD1   . TRP B 1 380 ? 34.646  78.713 -14.537 1.00 28.54  ? 366  TRP B CD1   1 
ATOM   6807 C  CD2   . TRP B 1 380 ? 35.306  77.062 -15.896 1.00 29.21  ? 366  TRP B CD2   1 
ATOM   6808 N  NE1   . TRP B 1 380 ? 33.766  77.662 -14.385 1.00 29.23  ? 366  TRP B NE1   1 
ATOM   6809 C  CE2   . TRP B 1 380 ? 34.158  76.634 -15.202 1.00 29.65  ? 366  TRP B CE2   1 
ATOM   6810 C  CE3   . TRP B 1 380 ? 35.906  76.188 -16.809 1.00 27.33  ? 366  TRP B CE3   1 
ATOM   6811 C  CZ2   . TRP B 1 380 ? 33.592  75.379 -15.405 1.00 29.23  ? 366  TRP B CZ2   1 
ATOM   6812 C  CZ3   . TRP B 1 380 ? 35.352  74.942 -16.997 1.00 26.01  ? 366  TRP B CZ3   1 
ATOM   6813 C  CH2   . TRP B 1 380 ? 34.203  74.549 -16.303 1.00 27.25  ? 366  TRP B CH2   1 
ATOM   6814 N  N     . LYS B 1 381 ? 39.850  80.328 -15.474 1.00 31.61  ? 367  LYS B N     1 
ATOM   6815 C  CA    . LYS B 1 381 ? 41.096  80.888 -15.988 1.00 31.18  ? 367  LYS B CA    1 
ATOM   6816 C  C     . LYS B 1 381 ? 42.255  79.914 -15.816 1.00 29.09  ? 367  LYS B C     1 
ATOM   6817 O  O     . LYS B 1 381 ? 43.097  79.783 -16.710 1.00 29.78  ? 367  LYS B O     1 
ATOM   6818 C  CB    . LYS B 1 381 ? 41.399  82.209 -15.295 1.00 32.04  ? 367  LYS B CB    1 
ATOM   6819 C  CG    . LYS B 1 381 ? 40.737  83.378 -15.970 1.00 35.68  ? 367  LYS B CG    1 
ATOM   6820 C  CD    . LYS B 1 381 ? 40.732  84.598 -15.083 1.00 38.97  ? 367  LYS B CD    1 
ATOM   6821 C  CE    . LYS B 1 381 ? 40.022  85.741 -15.779 1.00 41.62  ? 367  LYS B CE    1 
ATOM   6822 N  NZ    . LYS B 1 381 ? 39.088  86.407 -14.844 1.00 44.97  ? 367  LYS B NZ    1 
ATOM   6823 N  N     . THR B 1 382 ? 42.319  79.217 -14.678 1.00 28.61  ? 368  THR B N     1 
ATOM   6824 C  CA    . THR B 1 382 ? 43.383  78.233 -14.495 1.00 30.46  ? 368  THR B CA    1 
ATOM   6825 C  C     . THR B 1 382 ? 43.226  77.090 -15.485 1.00 29.55  ? 368  THR B C     1 
ATOM   6826 O  O     . THR B 1 382 ? 44.210  76.619 -16.069 1.00 28.93  ? 368  THR B O     1 
ATOM   6827 C  CB    . THR B 1 382 ? 43.392  77.698 -13.055 1.00 29.40  ? 368  THR B CB    1 
ATOM   6828 O  OG1   . THR B 1 382 ? 43.430  78.792 -12.122 1.00 27.74  ? 368  THR B OG1   1 
ATOM   6829 C  CG2   . THR B 1 382 ? 44.589  76.777 -12.832 1.00 29.46  ? 368  THR B CG2   1 
ATOM   6830 N  N     . LEU B 1 383 ? 41.992  76.636 -15.691 1.00 28.64  ? 369  LEU B N     1 
ATOM   6831 C  CA    . LEU B 1 383 ? 41.762  75.539 -16.620 1.00 28.45  ? 369  LEU B CA    1 
ATOM   6832 C  C     . LEU B 1 383 ? 42.084  75.958 -18.047 1.00 27.12  ? 369  LEU B C     1 
ATOM   6833 O  O     . LEU B 1 383 ? 42.581  75.148 -18.835 1.00 25.91  ? 369  LEU B O     1 
ATOM   6834 C  CB    . LEU B 1 383 ? 40.312  75.059 -16.506 1.00 26.75  ? 369  LEU B CB    1 
ATOM   6835 C  CG    . LEU B 1 383 ? 40.007  73.706 -17.148 1.00 25.47  ? 369  LEU B CG    1 
ATOM   6836 C  CD1   . LEU B 1 383 ? 40.751  72.611 -16.422 1.00 26.05  ? 369  LEU B CD1   1 
ATOM   6837 C  CD2   . LEU B 1 383 ? 38.523  73.421 -17.165 1.00 26.52  ? 369  LEU B CD2   1 
ATOM   6838 N  N     . GLN B 1 384 ? 41.823  77.223 -18.380 1.00 27.27  ? 370  GLN B N     1 
ATOM   6839 C  CA    . GLN B 1 384 ? 42.123  77.757 -19.707 1.00 27.22  ? 370  GLN B CA    1 
ATOM   6840 C  C     . GLN B 1 384 ? 43.591  77.566 -20.086 1.00 28.56  ? 370  GLN B C     1 
ATOM   6841 O  O     . GLN B 1 384 ? 43.906  77.214 -21.230 1.00 26.84  ? 370  GLN B O     1 
ATOM   6842 C  CB    . GLN B 1 384 ? 41.743  79.238 -19.735 1.00 27.60  ? 370  GLN B CB    1 
ATOM   6843 C  CG    . GLN B 1 384 ? 42.020  79.954 -21.035 1.00 30.05  ? 370  GLN B CG    1 
ATOM   6844 C  CD    . GLN B 1 384 ? 41.299  79.330 -22.219 1.00 28.93  ? 370  GLN B CD    1 
ATOM   6845 O  OE1   . GLN B 1 384 ? 40.077  79.173 -22.206 1.00 29.51  ? 370  GLN B OE1   1 
ATOM   6846 N  NE2   . GLN B 1 384 ? 42.052  79.001 -23.263 1.00 28.78  ? 370  GLN B NE2   1 
ATOM   6847 N  N     . THR B 1 385 ? 44.508  77.810 -19.149 1.00 29.34  ? 371  THR B N     1 
ATOM   6848 C  CA    . THR B 1 385 ? 45.925  77.640 -19.461 1.00 30.70  ? 371  THR B CA    1 
ATOM   6849 C  C     . THR B 1 385 ? 46.302  76.171 -19.628 1.00 31.24  ? 371  THR B C     1 
ATOM   6850 O  O     . THR B 1 385 ? 47.377  75.881 -20.160 1.00 32.47  ? 371  THR B O     1 
ATOM   6851 C  CB    . THR B 1 385 ? 46.798  78.301 -18.383 1.00 31.70  ? 371  THR B CB    1 
ATOM   6852 O  OG1   . THR B 1 385 ? 46.742  77.532 -17.179 1.00 32.67  ? 371  THR B OG1   1 
ATOM   6853 C  CG2   . THR B 1 385 ? 46.335  79.713 -18.080 1.00 30.82  ? 371  THR B CG2   1 
ATOM   6854 N  N     . PHE B 1 386 ? 45.439  75.243 -19.198 1.00 30.44  ? 372  PHE B N     1 
ATOM   6855 C  CA    . PHE B 1 386 ? 45.747  73.814 -19.134 1.00 29.36  ? 372  PHE B CA    1 
ATOM   6856 C  C     . PHE B 1 386 ? 45.347  73.033 -20.388 1.00 27.94  ? 372  PHE B C     1 
ATOM   6857 O  O     . PHE B 1 386 ? 46.069  72.116 -20.804 1.00 26.51  ? 372  PHE B O     1 
ATOM   6858 C  CB    . PHE B 1 386 ? 45.044  73.203 -17.915 1.00 28.56  ? 372  PHE B CB    1 
ATOM   6859 C  CG    . PHE B 1 386 ? 45.081  71.694 -17.869 1.00 25.87  ? 372  PHE B CG    1 
ATOM   6860 C  CD1   . PHE B 1 386 ? 46.263  71.031 -17.551 1.00 26.99  ? 372  PHE B CD1   1 
ATOM   6861 C  CD2   . PHE B 1 386 ? 43.933  70.945 -18.090 1.00 26.25  ? 372  PHE B CD2   1 
ATOM   6862 C  CE1   . PHE B 1 386 ? 46.315  69.650 -17.482 1.00 26.50  ? 372  PHE B CE1   1 
ATOM   6863 C  CE2   . PHE B 1 386 ? 43.972  69.547 -18.022 1.00 25.63  ? 372  PHE B CE2   1 
ATOM   6864 C  CZ    . PHE B 1 386 ? 45.166  68.905 -17.723 1.00 25.38  ? 372  PHE B CZ    1 
ATOM   6865 N  N     . ILE B 1 387 ? 44.195  73.343 -20.985 1.00 26.16  ? 373  ILE B N     1 
ATOM   6866 C  CA    . ILE B 1 387 ? 43.721  72.561 -22.121 1.00 26.24  ? 373  ILE B CA    1 
ATOM   6867 C  C     . ILE B 1 387 ? 44.668  72.697 -23.312 1.00 27.65  ? 373  ILE B C     1 
ATOM   6868 O  O     . ILE B 1 387 ? 45.399  73.689 -23.452 1.00 26.91  ? 373  ILE B O     1 
ATOM   6869 C  CB    . ILE B 1 387 ? 42.286  72.971 -22.488 1.00 24.26  ? 373  ILE B CB    1 
ATOM   6870 C  CG1   . ILE B 1 387 ? 42.297  74.388 -23.060 1.00 23.69  ? 373  ILE B CG1   1 
ATOM   6871 C  CG2   . ILE B 1 387 ? 41.345  72.777 -21.281 1.00 21.35  ? 373  ILE B CG2   1 
ATOM   6872 C  CD1   . ILE B 1 387 ? 40.984  74.847 -23.679 1.00 26.17  ? 373  ILE B CD1   1 
ATOM   6873 N  N     . ARG B 1 388 ? 44.653  71.684 -24.174 1.00 27.14  ? 374  ARG B N     1 
ATOM   6874 C  CA    . ARG B 1 388 ? 45.618  71.553 -25.258 1.00 28.42  ? 374  ARG B CA    1 
ATOM   6875 C  C     . ARG B 1 388 ? 44.915  70.931 -26.456 1.00 28.37  ? 374  ARG B C     1 
ATOM   6876 O  O     . ARG B 1 388 ? 43.838  70.341 -26.309 1.00 26.25  ? 374  ARG B O     1 
ATOM   6877 C  CB    . ARG B 1 388 ? 46.830  70.718 -24.806 1.00 29.27  ? 374  ARG B CB    1 
ATOM   6878 C  CG    . ARG B 1 388 ? 48.199  71.253 -25.276 1.00 34.24  ? 374  ARG B CG    1 
ATOM   6879 C  CD    . ARG B 1 388 ? 49.069  71.891 -24.195 1.00 34.24  ? 374  ARG B CD    1 
ATOM   6880 N  NE    . ARG B 1 388 ? 48.340  72.874 -23.406 1.00 33.62  ? 374  ARG B NE    1 
ATOM   6881 C  CZ    . ARG B 1 388 ? 48.897  73.686 -22.518 1.00 32.26  ? 374  ARG B CZ    1 
ATOM   6882 N  NH1   . ARG B 1 388 ? 50.186  73.630 -22.244 1.00 33.18  ? 374  ARG B NH1   1 
ATOM   6883 N  NH2   . ARG B 1 388 ? 48.138  74.586 -21.899 1.00 33.19  ? 374  ARG B NH2   1 
ATOM   6884 N  N     . PRO B 1 389 ? 45.477  71.064 -27.662 1.00 28.37  ? 375  PRO B N     1 
ATOM   6885 C  CA    . PRO B 1 389 ? 44.901  70.348 -28.803 1.00 26.64  ? 375  PRO B CA    1 
ATOM   6886 C  C     . PRO B 1 389 ? 44.840  68.851 -28.530 1.00 27.64  ? 375  PRO B C     1 
ATOM   6887 O  O     . PRO B 1 389 ? 45.671  68.282 -27.814 1.00 27.25  ? 375  PRO B O     1 
ATOM   6888 C  CB    . PRO B 1 389 ? 45.863  70.671 -29.951 1.00 28.00  ? 375  PRO B CB    1 
ATOM   6889 C  CG    . PRO B 1 389 ? 46.380  72.027 -29.620 1.00 29.00  ? 375  PRO B CG    1 
ATOM   6890 C  CD    . PRO B 1 389 ? 46.445  72.091 -28.097 1.00 30.31  ? 375  PRO B CD    1 
ATOM   6891 N  N     . GLY B 1 390 ? 43.799  68.223 -29.060 1.00 28.80  ? 376  GLY B N     1 
ATOM   6892 C  CA    . GLY B 1 390 ? 43.561  66.817 -28.839 1.00 26.47  ? 376  GLY B CA    1 
ATOM   6893 C  C     . GLY B 1 390 ? 42.699  66.495 -27.644 1.00 25.36  ? 376  GLY B C     1 
ATOM   6894 O  O     . GLY B 1 390 ? 42.207  65.360 -27.547 1.00 25.84  ? 376  GLY B O     1 
ATOM   6895 N  N     . ASP B 1 391 ? 42.460  67.456 -26.753 1.00 23.73  ? 377  ASP B N     1 
ATOM   6896 C  CA    . ASP B 1 391 ? 41.679  67.175 -25.557 1.00 23.99  ? 377  ASP B CA    1 
ATOM   6897 C  C     . ASP B 1 391 ? 40.259  66.767 -25.924 1.00 23.43  ? 377  ASP B C     1 
ATOM   6898 O  O     . ASP B 1 391 ? 39.683  67.262 -26.900 1.00 23.59  ? 377  ASP B O     1 
ATOM   6899 C  CB    . ASP B 1 391 ? 41.638  68.405 -24.645 1.00 24.54  ? 377  ASP B CB    1 
ATOM   6900 C  CG    . ASP B 1 391 ? 42.917  68.579 -23.828 1.00 24.99  ? 377  ASP B CG    1 
ATOM   6901 O  OD1   . ASP B 1 391 ? 43.745  67.640 -23.785 1.00 23.20  ? 377  ASP B OD1   1 
ATOM   6902 O  OD2   . ASP B 1 391 ? 43.097  69.668 -23.243 1.00 24.29  ? 377  ASP B OD2   1 
ATOM   6903 N  N     . ILE B 1 392 ? 39.720  65.827 -25.157 1.00 21.09  ? 378  ILE B N     1 
ATOM   6904 C  CA    . ILE B 1 392 ? 38.288  65.555 -25.098 1.00 22.67  ? 378  ILE B CA    1 
ATOM   6905 C  C     . ILE B 1 392 ? 37.790  66.110 -23.770 1.00 22.55  ? 378  ILE B C     1 
ATOM   6906 O  O     . ILE B 1 392 ? 38.236  65.676 -22.699 1.00 21.73  ? 378  ILE B O     1 
ATOM   6907 C  CB    . ILE B 1 392 ? 37.965  64.061 -25.209 1.00 20.29  ? 378  ILE B CB    1 
ATOM   6908 C  CG1   . ILE B 1 392 ? 38.527  63.462 -26.497 1.00 22.20  ? 378  ILE B CG1   1 
ATOM   6909 C  CG2   . ILE B 1 392 ? 36.432  63.865 -25.155 1.00 21.37  ? 378  ILE B CG2   1 
ATOM   6910 C  CD1   . ILE B 1 392 ? 38.222  61.958 -26.627 1.00 21.29  ? 378  ILE B CD1   1 
ATOM   6911 N  N     . ILE B 1 393 ? 36.897  67.090 -23.840 1.00 21.60  ? 379  ILE B N     1 
ATOM   6912 C  CA    . ILE B 1 393 ? 36.430  67.826 -22.676 1.00 21.10  ? 379  ILE B CA    1 
ATOM   6913 C  C     . ILE B 1 393 ? 34.934  67.606 -22.566 1.00 20.79  ? 379  ILE B C     1 
ATOM   6914 O  O     . ILE B 1 393 ? 34.185  67.918 -23.499 1.00 21.38  ? 379  ILE B O     1 
ATOM   6915 C  CB    . ILE B 1 393 ? 36.756  69.324 -22.783 1.00 20.60  ? 379  ILE B CB    1 
ATOM   6916 C  CG1   . ILE B 1 393 ? 38.263  69.545 -22.931 1.00 23.69  ? 379  ILE B CG1   1 
ATOM   6917 C  CG2   . ILE B 1 393 ? 36.205  70.084 -21.575 1.00 20.90  ? 379  ILE B CG2   1 
ATOM   6918 C  CD1   . ILE B 1 393 ? 38.639  71.026 -23.156 1.00 22.01  ? 379  ILE B CD1   1 
ATOM   6919 N  N     . LEU B 1 394 ? 34.502  67.052 -21.442 1.00 21.37  ? 380  LEU B N     1 
ATOM   6920 C  CA    . LEU B 1 394 ? 33.096  66.832 -21.158 1.00 18.97  ? 380  LEU B CA    1 
ATOM   6921 C  C     . LEU B 1 394 ? 32.707  67.657 -19.941 1.00 20.54  ? 380  LEU B C     1 
ATOM   6922 O  O     . LEU B 1 394 ? 33.459  67.723 -18.962 1.00 18.54  ? 380  LEU B O     1 
ATOM   6923 C  CB    . LEU B 1 394 ? 32.798  65.345 -20.903 1.00 19.01  ? 380  LEU B CB    1 
ATOM   6924 C  CG    . LEU B 1 394 ? 33.245  64.338 -21.970 1.00 20.99  ? 380  LEU B CG    1 
ATOM   6925 C  CD1   . LEU B 1 394 ? 34.667  63.837 -21.717 1.00 19.18  ? 380  LEU B CD1   1 
ATOM   6926 C  CD2   . LEU B 1 394 ? 32.266  63.166 -22.074 1.00 18.01  ? 380  LEU B CD2   1 
ATOM   6927 N  N     . ALA B 1 395 ? 31.539  68.297 -20.007 1.00 20.02  ? 381  ALA B N     1 
ATOM   6928 C  CA    . ALA B 1 395 ? 31.058  69.101 -18.889 1.00 21.96  ? 381  ALA B CA    1 
ATOM   6929 C  C     . ALA B 1 395 ? 29.588  68.799 -18.631 1.00 21.95  ? 381  ALA B C     1 
ATOM   6930 O  O     . ALA B 1 395 ? 28.798  68.672 -19.573 1.00 17.94  ? 381  ALA B O     1 
ATOM   6931 C  CB    . ALA B 1 395 ? 31.252  70.596 -19.148 1.00 21.30  ? 381  ALA B CB    1 
ATOM   6932 N  N     . ASP B 1 396 ? 29.221  68.679 -17.353 1.00 19.79  ? 382  ASP B N     1 
ATOM   6933 C  CA    . ASP B 1 396 ? 27.834  68.384 -17.005 1.00 21.46  ? 382  ASP B CA    1 
ATOM   6934 C  C     . ASP B 1 396 ? 27.024  69.656 -16.789 1.00 22.06  ? 382  ASP B C     1 
ATOM   6935 O  O     . ASP B 1 396 ? 27.558  70.756 -16.694 1.00 22.15  ? 382  ASP B O     1 
ATOM   6936 C  CB    . ASP B 1 396 ? 27.746  67.507 -15.745 1.00 20.74  ? 382  ASP B CB    1 
ATOM   6937 C  CG    . ASP B 1 396 ? 26.697  66.402 -15.877 1.00 20.08  ? 382  ASP B CG    1 
ATOM   6938 O  OD1   . ASP B 1 396 ? 25.589  66.686 -16.392 1.00 20.55  ? 382  ASP B OD1   1 
ATOM   6939 O  OD2   . ASP B 1 396 ? 26.970  65.257 -15.464 1.00 20.23  ? 382  ASP B OD2   1 
ATOM   6940 N  N     . GLN B 1 397 ? 25.705  69.487 -16.685 1.00 22.86  ? 383  GLN B N     1 
ATOM   6941 C  CA    . GLN B 1 397 ? 24.829  70.621 -16.425 1.00 22.33  ? 383  GLN B CA    1 
ATOM   6942 C  C     . GLN B 1 397 ? 25.044  71.132 -15.000 1.00 26.58  ? 383  GLN B C     1 
ATOM   6943 O  O     . GLN B 1 397 ? 25.433  70.382 -14.101 1.00 26.24  ? 383  GLN B O     1 
ATOM   6944 C  CB    . GLN B 1 397 ? 23.371  70.213 -16.659 1.00 24.23  ? 383  GLN B CB    1 
ATOM   6945 C  CG    . GLN B 1 397 ? 23.101  69.884 -18.113 1.00 23.87  ? 383  GLN B CG    1 
ATOM   6946 C  CD    . GLN B 1 397 ? 23.518  71.014 -19.020 1.00 26.65  ? 383  GLN B CD    1 
ATOM   6947 O  OE1   . GLN B 1 397 ? 22.912  72.087 -19.010 1.00 30.34  ? 383  GLN B OE1   1 
ATOM   6948 N  NE2   . GLN B 1 397 ? 24.580  70.800 -19.784 1.00 24.43  ? 383  GLN B NE2   1 
ATOM   6949 N  N     . GLY B 1 398 ? 24.842  72.433 -14.806 1.00 31.93  ? 384  GLY B N     1 
ATOM   6950 C  CA    . GLY B 1 398 ? 25.279  73.095 -13.582 1.00 33.09  ? 384  GLY B CA    1 
ATOM   6951 C  C     . GLY B 1 398 ? 26.357  74.128 -13.853 1.00 37.83  ? 384  GLY B C     1 
ATOM   6952 O  O     . GLY B 1 398 ? 26.549  74.523 -15.002 1.00 37.03  ? 384  GLY B O     1 
ATOM   6953 N  N     . THR B 1 399 ? 27.111  74.549 -12.834 1.00 40.92  ? 385  THR B N     1 
ATOM   6954 C  CA    . THR B 1 399 ? 28.155  75.541 -13.094 1.00 40.45  ? 385  THR B CA    1 
ATOM   6955 C  C     . THR B 1 399 ? 29.266  75.000 -13.999 1.00 39.39  ? 385  THR B C     1 
ATOM   6956 O  O     . THR B 1 399 ? 29.891  75.776 -14.735 1.00 40.96  ? 385  THR B O     1 
ATOM   6957 C  CB    . THR B 1 399 ? 28.765  75.993 -11.773 1.00 40.04  ? 385  THR B CB    1 
ATOM   6958 O  OG1   . THR B 1 399 ? 29.613  74.951 -11.274 1.00 34.36  ? 385  THR B OG1   1 
ATOM   6959 C  CG2   . THR B 1 399 ? 27.673  76.240 -10.772 1.00 43.16  ? 385  THR B CG2   1 
ATOM   6960 N  N     . SER B 1 400 ? 29.428  73.677 -14.075 1.00 34.15  ? 386  SER B N     1 
ATOM   6961 C  CA    . SER B 1 400 ? 30.444  73.111 -14.956 1.00 33.61  ? 386  SER B CA    1 
ATOM   6962 C  C     . SER B 1 400 ? 30.230  73.553 -16.402 1.00 33.32  ? 386  SER B C     1 
ATOM   6963 O  O     . SER B 1 400 ? 31.089  74.208 -16.996 1.00 32.71  ? 386  SER B O     1 
ATOM   6964 C  CB    . SER B 1 400 ? 30.439  71.582 -14.855 1.00 27.75  ? 386  SER B CB    1 
ATOM   6965 O  OG    . SER B 1 400 ? 31.035  71.136 -13.646 1.00 28.24  ? 386  SER B OG    1 
ATOM   6966 N  N     . ALA B 1 401 ? 29.076  73.215 -16.983 1.00 40.98  ? 387  ALA B N     1 
ATOM   6967 C  CA    . ALA B 1 401 ? 28.837  73.550 -18.387 1.00 36.34  ? 387  ALA B CA    1 
ATOM   6968 C  C     . ALA B 1 401 ? 28.821  75.060 -18.608 1.00 39.30  ? 387  ALA B C     1 
ATOM   6969 O  O     . ALA B 1 401 ? 29.360  75.556 -19.605 1.00 38.74  ? 387  ALA B O     1 
ATOM   6970 C  CB    . ALA B 1 401 ? 27.518  72.929 -18.865 1.00 33.36  ? 387  ALA B CB    1 
ATOM   6971 N  N     . PHE B 1 402 ? 28.205  75.813 -17.698 1.00 43.58  ? 388  PHE B N     1 
ATOM   6972 C  CA    . PHE B 1 402 ? 28.085  77.248 -17.923 1.00 45.78  ? 388  PHE B CA    1 
ATOM   6973 C  C     . PHE B 1 402 ? 29.350  78.030 -17.595 1.00 43.22  ? 388  PHE B C     1 
ATOM   6974 O  O     . PHE B 1 402 ? 29.430  79.212 -17.948 1.00 52.15  ? 388  PHE B O     1 
ATOM   6975 C  CB    . PHE B 1 402 ? 26.882  77.787 -17.148 1.00 51.30  ? 388  PHE B CB    1 
ATOM   6976 C  CG    . PHE B 1 402 ? 25.639  76.981 -17.371 1.00 56.71  ? 388  PHE B CG    1 
ATOM   6977 C  CD1   . PHE B 1 402 ? 25.267  76.622 -18.660 1.00 56.17  ? 388  PHE B CD1   1 
ATOM   6978 C  CD2   . PHE B 1 402 ? 24.837  76.586 -16.307 1.00 65.61  ? 388  PHE B CD2   1 
ATOM   6979 C  CE1   . PHE B 1 402 ? 24.125  75.871 -18.885 1.00 69.20  ? 388  PHE B CE1   1 
ATOM   6980 C  CE2   . PHE B 1 402 ? 23.689  75.833 -16.522 1.00 59.60  ? 388  PHE B CE2   1 
ATOM   6981 C  CZ    . PHE B 1 402 ? 23.332  75.477 -17.814 1.00 63.84  ? 388  PHE B CZ    1 
ATOM   6982 N  N     . GLY B 1 403 ? 30.332  77.417 -16.940 1.00 36.23  ? 389  GLY B N     1 
ATOM   6983 C  CA    . GLY B 1 403 ? 31.646  78.014 -16.888 1.00 32.97  ? 389  GLY B CA    1 
ATOM   6984 C  C     . GLY B 1 403 ? 32.484  77.613 -18.087 1.00 30.86  ? 389  GLY B C     1 
ATOM   6985 O  O     . GLY B 1 403 ? 33.190  78.441 -18.669 1.00 30.49  ? 389  GLY B O     1 
ATOM   6986 N  N     . ALA B 1 404 ? 32.410  76.334 -18.462 1.00 29.69  ? 390  ALA B N     1 
ATOM   6987 C  CA    . ALA B 1 404 ? 33.188  75.816 -19.583 1.00 28.54  ? 390  ALA B CA    1 
ATOM   6988 C  C     . ALA B 1 404 ? 32.825  76.470 -20.915 1.00 28.64  ? 390  ALA B C     1 
ATOM   6989 O  O     . ALA B 1 404 ? 33.624  76.416 -21.858 1.00 26.54  ? 390  ALA B O     1 
ATOM   6990 C  CB    . ALA B 1 404 ? 33.014  74.303 -19.677 1.00 26.60  ? 390  ALA B CB    1 
ATOM   6991 N  N     . ILE B 1 405 ? 31.635  77.069 -21.024 1.00 30.12  ? 391  ILE B N     1 
ATOM   6992 C  CA    . ILE B 1 405 ? 31.262  77.764 -22.252 1.00 27.42  ? 391  ILE B CA    1 
ATOM   6993 C  C     . ILE B 1 405 ? 32.256  78.876 -22.567 1.00 28.11  ? 391  ILE B C     1 
ATOM   6994 O  O     . ILE B 1 405 ? 32.476  79.210 -23.739 1.00 27.49  ? 391  ILE B O     1 
ATOM   6995 C  CB    . ILE B 1 405 ? 29.829  78.317 -22.127 1.00 28.90  ? 391  ILE B CB    1 
ATOM   6996 C  CG1   . ILE B 1 405 ? 29.289  78.713 -23.494 1.00 27.69  ? 391  ILE B CG1   1 
ATOM   6997 C  CG2   . ILE B 1 405 ? 29.785  79.516 -21.188 1.00 31.86  ? 391  ILE B CG2   1 
ATOM   6998 C  CD1   . ILE B 1 405 ? 27.842  79.185 -23.448 1.00 28.63  ? 391  ILE B CD1   1 
ATOM   6999 N  N     . ASP B 1 406 ? 32.882  79.456 -21.539 1.00 27.86  ? 392  ASP B N     1 
ATOM   7000 C  CA    . ASP B 1 406 ? 33.821  80.559 -21.714 1.00 29.03  ? 392  ASP B CA    1 
ATOM   7001 C  C     . ASP B 1 406 ? 35.237  80.081 -22.021 1.00 29.40  ? 392  ASP B C     1 
ATOM   7002 O  O     . ASP B 1 406 ? 36.129  80.913 -22.206 1.00 28.81  ? 392  ASP B O     1 
ATOM   7003 C  CB    . ASP B 1 406 ? 33.870  81.452 -20.457 1.00 31.21  ? 392  ASP B CB    1 
ATOM   7004 C  CG    . ASP B 1 406 ? 32.562  82.186 -20.177 1.00 35.56  ? 392  ASP B CG    1 
ATOM   7005 O  OD1   . ASP B 1 406 ? 31.932  82.695 -21.118 1.00 37.62  ? 392  ASP B OD1   1 
ATOM   7006 O  OD2   . ASP B 1 406 ? 32.185  82.293 -18.990 1.00 40.15  ? 392  ASP B OD2   1 
ATOM   7007 N  N     . LEU B 1 407 ? 35.480  78.775 -22.062 1.00 27.34  ? 393  LEU B N     1 
ATOM   7008 C  CA    . LEU B 1 407 ? 36.791  78.297 -22.479 1.00 27.59  ? 393  LEU B CA    1 
ATOM   7009 C  C     . LEU B 1 407 ? 37.005  78.619 -23.955 1.00 28.32  ? 393  LEU B C     1 
ATOM   7010 O  O     . LEU B 1 407 ? 36.099  78.458 -24.776 1.00 26.64  ? 393  LEU B O     1 
ATOM   7011 C  CB    . LEU B 1 407 ? 36.919  76.790 -22.258 1.00 26.29  ? 393  LEU B CB    1 
ATOM   7012 C  CG    . LEU B 1 407 ? 37.070  76.240 -20.844 1.00 27.31  ? 393  LEU B CG    1 
ATOM   7013 C  CD1   . LEU B 1 407 ? 36.942  74.719 -20.851 1.00 24.32  ? 393  LEU B CD1   1 
ATOM   7014 C  CD2   . LEU B 1 407 ? 38.390  76.686 -20.212 1.00 26.41  ? 393  LEU B CD2   1 
ATOM   7015 N  N     . ARG B 1 408 ? 38.204  79.106 -24.273 1.00 28.80  ? 394  ARG B N     1 
ATOM   7016 C  CA    . ARG B 1 408 ? 38.642  79.402 -25.637 1.00 29.09  ? 394  ARG B CA    1 
ATOM   7017 C  C     . ARG B 1 408 ? 39.426  78.192 -26.141 1.00 30.23  ? 394  ARG B C     1 
ATOM   7018 O  O     . ARG B 1 408 ? 40.616  78.041 -25.843 1.00 31.06  ? 394  ARG B O     1 
ATOM   7019 C  CB    . ARG B 1 408 ? 39.502  80.662 -25.641 1.00 31.20  ? 394  ARG B CB    1 
ATOM   7020 C  CG    . ARG B 1 408 ? 39.917  81.174 -27.015 1.00 37.62  ? 394  ARG B CG    1 
ATOM   7021 C  CD    . ARG B 1 408 ? 40.354  82.640 -26.936 1.00 40.72  ? 394  ARG B CD    1 
ATOM   7022 N  NE    . ARG B 1 408 ? 40.526  83.248 -28.250 1.00 54.17  ? 394  ARG B NE    1 
ATOM   7023 C  CZ    . ARG B 1 408 ? 41.667  83.754 -28.703 1.00 61.13  ? 394  ARG B CZ    1 
ATOM   7024 N  NH1   . ARG B 1 408 ? 42.772  83.736 -27.971 1.00 58.06  ? 394  ARG B NH1   1 
ATOM   7025 N  NH2   . ARG B 1 408 ? 41.699  84.294 -29.919 1.00 50.39  ? 394  ARG B NH2   1 
ATOM   7026 N  N     . LEU B 1 409 ? 38.774  77.365 -26.943 1.00 27.81  ? 395  LEU B N     1 
ATOM   7027 C  CA    . LEU B 1 409 ? 39.273  76.031 -27.280 1.00 27.95  ? 395  LEU B CA    1 
ATOM   7028 C  C     . LEU B 1 409 ? 40.315  76.082 -28.401 1.00 29.20  ? 395  LEU B C     1 
ATOM   7029 O  O     . LEU B 1 409 ? 40.111  76.777 -29.404 1.00 29.60  ? 395  LEU B O     1 
ATOM   7030 C  CB    . LEU B 1 409 ? 38.117  75.145 -27.703 1.00 26.70  ? 395  LEU B CB    1 
ATOM   7031 C  CG    . LEU B 1 409 ? 37.038  74.789 -26.682 1.00 26.53  ? 395  LEU B CG    1 
ATOM   7032 C  CD1   . LEU B 1 409 ? 36.115  73.793 -27.326 1.00 24.32  ? 395  LEU B CD1   1 
ATOM   7033 C  CD2   . LEU B 1 409 ? 37.650  74.216 -25.374 1.00 24.13  ? 395  LEU B CD2   1 
ATOM   7034 N  N     . PRO B 1 410 ? 41.440  75.370 -28.266 1.00 28.87  ? 396  PRO B N     1 
ATOM   7035 C  CA    . PRO B 1 410 ? 42.365  75.215 -29.400 1.00 29.96  ? 396  PRO B CA    1 
ATOM   7036 C  C     . PRO B 1 410 ? 41.864  74.224 -30.440 1.00 30.33  ? 396  PRO B C     1 
ATOM   7037 O  O     . PRO B 1 410 ? 40.755  73.696 -30.320 1.00 29.73  ? 396  PRO B O     1 
ATOM   7038 C  CB    . PRO B 1 410 ? 43.655  74.708 -28.745 1.00 31.44  ? 396  PRO B CB    1 
ATOM   7039 C  CG    . PRO B 1 410 ? 43.297  74.411 -27.293 1.00 30.42  ? 396  PRO B CG    1 
ATOM   7040 C  CD    . PRO B 1 410 ? 41.827  74.528 -27.128 1.00 27.73  ? 396  PRO B CD    1 
ATOM   7041 N  N     . ALA B 1 411 ? 42.705  73.928 -31.433 1.00 31.19  ? 397  ALA B N     1 
ATOM   7042 C  CA    . ALA B 1 411 ? 42.353  73.002 -32.503 1.00 31.45  ? 397  ALA B CA    1 
ATOM   7043 C  C     . ALA B 1 411 ? 42.185  71.580 -31.980 1.00 33.69  ? 397  ALA B C     1 
ATOM   7044 O  O     . ALA B 1 411 ? 42.777  71.192 -30.968 1.00 31.43  ? 397  ALA B O     1 
ATOM   7045 C  CB    . ALA B 1 411 ? 43.423  73.022 -33.596 1.00 32.84  ? 397  ALA B CB    1 
ATOM   7046 N  N     . ASP B 1 412 ? 41.345  70.806 -32.686 1.00 32.64  ? 398  ASP B N     1 
ATOM   7047 C  CA    . ASP B 1 412 ? 41.152  69.370 -32.445 1.00 32.71  ? 398  ASP B CA    1 
ATOM   7048 C  C     . ASP B 1 412 ? 40.743  69.081 -31.005 1.00 30.61  ? 398  ASP B C     1 
ATOM   7049 O  O     . ASP B 1 412 ? 41.315  68.221 -30.330 1.00 29.24  ? 398  ASP B O     1 
ATOM   7050 C  CB    . ASP B 1 412 ? 42.392  68.556 -32.824 1.00 37.72  ? 398  ASP B CB    1 
ATOM   7051 C  CG    . ASP B 1 412 ? 42.959  68.946 -34.181 1.00 56.48  ? 398  ASP B CG    1 
ATOM   7052 O  OD1   . ASP B 1 412 ? 42.229  69.578 -34.974 1.00 52.77  ? 398  ASP B OD1   1 
ATOM   7053 O  OD2   . ASP B 1 412 ? 44.134  68.613 -34.458 1.00 71.60  ? 398  ASP B OD2   1 
ATOM   7054 N  N     . VAL B 1 413 ? 39.715  69.783 -30.545 1.00 28.40  ? 399  VAL B N     1 
ATOM   7055 C  CA    . VAL B 1 413 ? 39.111  69.535 -29.244 1.00 26.66  ? 399  VAL B CA    1 
ATOM   7056 C  C     . VAL B 1 413 ? 37.722  68.961 -29.473 1.00 25.04  ? 399  VAL B C     1 
ATOM   7057 O  O     . VAL B 1 413 ? 36.937  69.506 -30.257 1.00 24.65  ? 399  VAL B O     1 
ATOM   7058 C  CB    . VAL B 1 413 ? 39.045  70.815 -28.393 1.00 26.38  ? 399  VAL B CB    1 
ATOM   7059 C  CG1   . VAL B 1 413 ? 38.136  70.595 -27.168 1.00 24.68  ? 399  VAL B CG1   1 
ATOM   7060 C  CG2   . VAL B 1 413 ? 40.443  71.233 -27.952 1.00 26.19  ? 399  VAL B CG2   1 
ATOM   7061 N  N     . ASN B 1 414 ? 37.421  67.860 -28.800 1.00 23.85  ? 400  ASN B N     1 
ATOM   7062 C  CA    . ASN B 1 414 ? 36.072  67.314 -28.788 1.00 24.44  ? 400  ASN B CA    1 
ATOM   7063 C  C     . ASN B 1 414 ? 35.422  67.765 -27.482 1.00 23.07  ? 400  ASN B C     1 
ATOM   7064 O  O     . ASN B 1 414 ? 35.825  67.338 -26.399 1.00 22.32  ? 400  ASN B O     1 
ATOM   7065 C  CB    . ASN B 1 414 ? 36.091  65.794 -28.930 1.00 23.34  ? 400  ASN B CB    1 
ATOM   7066 C  CG    . ASN B 1 414 ? 34.707  65.208 -29.160 1.00 24.41  ? 400  ASN B CG    1 
ATOM   7067 O  OD1   . ASN B 1 414 ? 33.691  65.753 -28.711 1.00 22.88  ? 400  ASN B OD1   1 
ATOM   7068 N  ND2   . ASN B 1 414 ? 34.658  64.109 -29.893 1.00 21.35  ? 400  ASN B ND2   1 
ATOM   7069 N  N     . PHE B 1 415 ? 34.440  68.656 -27.590 1.00 22.42  ? 401  PHE B N     1 
ATOM   7070 C  CA    . PHE B 1 415 ? 33.780  69.259 -26.438 1.00 21.97  ? 401  PHE B CA    1 
ATOM   7071 C  C     . PHE B 1 415 ? 32.375  68.672 -26.357 1.00 19.90  ? 401  PHE B C     1 
ATOM   7072 O  O     . PHE B 1 415 ? 31.533  68.947 -27.215 1.00 20.84  ? 401  PHE B O     1 
ATOM   7073 C  CB    . PHE B 1 415 ? 33.745  70.779 -26.582 1.00 22.38  ? 401  PHE B CB    1 
ATOM   7074 C  CG    . PHE B 1 415 ? 33.254  71.500 -25.359 1.00 22.27  ? 401  PHE B CG    1 
ATOM   7075 C  CD1   . PHE B 1 415 ? 31.893  71.705 -25.154 1.00 22.42  ? 401  PHE B CD1   1 
ATOM   7076 C  CD2   . PHE B 1 415 ? 34.155  72.019 -24.441 1.00 22.83  ? 401  PHE B CD2   1 
ATOM   7077 C  CE1   . PHE B 1 415 ? 31.437  72.387 -24.040 1.00 23.19  ? 401  PHE B CE1   1 
ATOM   7078 C  CE2   . PHE B 1 415 ? 33.709  72.704 -23.330 1.00 25.26  ? 401  PHE B CE2   1 
ATOM   7079 C  CZ    . PHE B 1 415 ? 32.338  72.891 -23.129 1.00 23.89  ? 401  PHE B CZ    1 
ATOM   7080 N  N     . ILE B 1 416 ? 32.125  67.867 -25.332 1.00 20.32  ? 402  ILE B N     1 
ATOM   7081 C  CA    . ILE B 1 416 ? 30.891  67.102 -25.206 1.00 21.00  ? 402  ILE B CA    1 
ATOM   7082 C  C     . ILE B 1 416 ? 30.082  67.682 -24.054 1.00 22.07  ? 402  ILE B C     1 
ATOM   7083 O  O     . ILE B 1 416 ? 30.471  67.565 -22.879 1.00 19.24  ? 402  ILE B O     1 
ATOM   7084 C  CB    . ILE B 1 416 ? 31.174  65.616 -24.975 1.00 22.28  ? 402  ILE B CB    1 
ATOM   7085 C  CG1   . ILE B 1 416 ? 31.835  65.020 -26.216 1.00 21.88  ? 402  ILE B CG1   1 
ATOM   7086 C  CG2   . ILE B 1 416 ? 29.869  64.884 -24.581 1.00 19.07  ? 402  ILE B CG2   1 
ATOM   7087 C  CD1   . ILE B 1 416 ? 32.387  63.613 -26.017 1.00 21.96  ? 402  ILE B CD1   1 
ATOM   7088 N  N     . VAL B 1 417 ? 28.939  68.278 -24.395 1.00 20.75  ? 403  VAL B N     1 
ATOM   7089 C  CA    . VAL B 1 417 ? 28.008  68.841 -23.428 1.00 21.55  ? 403  VAL B CA    1 
ATOM   7090 C  C     . VAL B 1 417 ? 26.593  68.519 -23.889 1.00 21.73  ? 403  VAL B C     1 
ATOM   7091 O  O     . VAL B 1 417 ? 26.319  68.415 -25.089 1.00 22.81  ? 403  VAL B O     1 
ATOM   7092 C  CB    . VAL B 1 417 ? 28.241  70.364 -23.268 1.00 22.39  ? 403  VAL B CB    1 
ATOM   7093 C  CG1   . VAL B 1 417 ? 27.975  71.099 -24.577 1.00 21.54  ? 403  VAL B CG1   1 
ATOM   7094 C  CG2   . VAL B 1 417 ? 27.413  70.925 -22.148 1.00 23.28  ? 403  VAL B CG2   1 
ATOM   7095 N  N     . GLN B 1 418 ? 25.679  68.391 -22.930 1.00 21.82  ? 404  GLN B N     1 
ATOM   7096 C  CA    . GLN B 1 418 ? 24.319  67.908 -23.185 1.00 20.62  ? 404  GLN B CA    1 
ATOM   7097 C  C     . GLN B 1 418 ? 23.313  68.920 -22.648 1.00 22.17  ? 404  GLN B C     1 
ATOM   7098 O  O     . GLN B 1 418 ? 22.554  68.634 -21.715 1.00 23.35  ? 404  GLN B O     1 
ATOM   7099 C  CB    . GLN B 1 418 ? 24.115  66.528 -22.550 1.00 20.47  ? 404  GLN B CB    1 
ATOM   7100 C  CG    . GLN B 1 418 ? 22.830  65.794 -22.980 1.00 19.88  ? 404  GLN B CG    1 
ATOM   7101 C  CD    . GLN B 1 418 ? 22.480  64.646 -22.030 1.00 19.69  ? 404  GLN B CD    1 
ATOM   7102 O  OE1   . GLN B 1 418 ? 22.363  64.846 -20.827 1.00 19.47  ? 404  GLN B OE1   1 
ATOM   7103 N  NE2   . GLN B 1 418 ? 22.335  63.442 -22.570 1.00 18.16  ? 404  GLN B NE2   1 
ATOM   7104 N  N     . PRO B 1 419 ? 23.251  70.110 -23.254 1.00 21.83  ? 405  PRO B N     1 
ATOM   7105 C  CA    . PRO B 1 419 ? 22.398  71.177 -22.711 1.00 23.44  ? 405  PRO B CA    1 
ATOM   7106 C  C     . PRO B 1 419 ? 20.940  71.086 -23.104 1.00 21.65  ? 405  PRO B C     1 
ATOM   7107 O  O     . PRO B 1 419 ? 20.124  71.766 -22.468 1.00 22.04  ? 405  PRO B O     1 
ATOM   7108 C  CB    . PRO B 1 419 ? 23.005  72.465 -23.311 1.00 22.24  ? 405  PRO B CB    1 
ATOM   7109 C  CG    . PRO B 1 419 ? 24.173  72.001 -24.169 1.00 25.18  ? 405  PRO B CG    1 
ATOM   7110 C  CD    . PRO B 1 419 ? 23.945  70.558 -24.467 1.00 23.08  ? 405  PRO B CD    1 
ATOM   7111 N  N     . LEU B 1 420 ? 20.581  70.339 -24.160 1.00 20.98  ? 406  LEU B N     1 
ATOM   7112 C  CA    . LEU B 1 420 ? 19.165  70.233 -24.521 1.00 21.75  ? 406  LEU B CA    1 
ATOM   7113 C  C     . LEU B 1 420 ? 18.452  69.178 -23.682 1.00 21.28  ? 406  LEU B C     1 
ATOM   7114 O  O     . LEU B 1 420 ? 17.420  69.465 -23.061 1.00 21.94  ? 406  LEU B O     1 
ATOM   7115 C  CB    . LEU B 1 420 ? 19.008  69.934 -26.012 1.00 22.08  ? 406  LEU B CB    1 
ATOM   7116 C  CG    . LEU B 1 420 ? 17.587  69.604 -26.475 1.00 22.85  ? 406  LEU B CG    1 
ATOM   7117 C  CD1   . LEU B 1 420 ? 16.557  70.674 -26.082 1.00 24.06  ? 406  LEU B CD1   1 
ATOM   7118 C  CD2   . LEU B 1 420 ? 17.564  69.361 -27.970 1.00 23.25  ? 406  LEU B CD2   1 
ATOM   7119 N  N     . TRP B 1 421 ? 18.971  67.948 -23.659 1.00 20.48  ? 407  TRP B N     1 
ATOM   7120 C  CA    . TRP B 1 421 ? 18.390  66.942 -22.779 1.00 21.39  ? 407  TRP B CA    1 
ATOM   7121 C  C     . TRP B 1 421 ? 18.628  67.302 -21.313 1.00 20.06  ? 407  TRP B C     1 
ATOM   7122 O  O     . TRP B 1 421 ? 17.676  67.378 -20.526 1.00 20.22  ? 407  TRP B O     1 
ATOM   7123 C  CB    . TRP B 1 421 ? 18.939  65.546 -23.105 1.00 19.58  ? 407  TRP B CB    1 
ATOM   7124 C  CG    . TRP B 1 421 ? 18.181  64.436 -22.378 1.00 18.83  ? 407  TRP B CG    1 
ATOM   7125 C  CD1   . TRP B 1 421 ? 18.699  63.507 -21.540 1.00 18.73  ? 407  TRP B CD1   1 
ATOM   7126 C  CD2   . TRP B 1 421 ? 16.769  64.191 -22.426 1.00 19.56  ? 407  TRP B CD2   1 
ATOM   7127 N  NE1   . TRP B 1 421 ? 17.705  62.675 -21.079 1.00 18.69  ? 407  TRP B NE1   1 
ATOM   7128 C  CE2   . TRP B 1 421 ? 16.510  63.078 -21.609 1.00 19.18  ? 407  TRP B CE2   1 
ATOM   7129 C  CE3   . TRP B 1 421 ? 15.702  64.794 -23.101 1.00 20.62  ? 407  TRP B CE3   1 
ATOM   7130 C  CZ2   . TRP B 1 421 ? 15.221  62.572 -21.422 1.00 19.80  ? 407  TRP B CZ2   1 
ATOM   7131 C  CZ3   . TRP B 1 421 ? 14.437  64.285 -22.930 1.00 21.23  ? 407  TRP B CZ3   1 
ATOM   7132 C  CH2   . TRP B 1 421 ? 14.204  63.184 -22.094 1.00 20.82  ? 407  TRP B CH2   1 
ATOM   7133 N  N     . GLY B 1 422 ? 19.881  67.562 -20.945 1.00 21.10  ? 408  GLY B N     1 
ATOM   7134 C  CA    . GLY B 1 422 ? 20.214  68.140 -19.652 1.00 19.07  ? 408  GLY B CA    1 
ATOM   7135 C  C     . GLY B 1 422 ? 20.189  67.205 -18.464 1.00 20.13  ? 408  GLY B C     1 
ATOM   7136 O  O     . GLY B 1 422 ? 19.754  67.604 -17.376 1.00 20.35  ? 408  GLY B O     1 
ATOM   7137 N  N     . SER B 1 423 ? 20.675  65.975 -18.623 1.00 19.07  ? 409  SER B N     1 
ATOM   7138 C  CA    . SER B 1 423 ? 20.592  64.957 -17.579 1.00 19.97  ? 409  SER B CA    1 
ATOM   7139 C  C     . SER B 1 423 ? 21.887  64.915 -16.760 1.00 18.86  ? 409  SER B C     1 
ATOM   7140 O  O     . SER B 1 423 ? 22.913  64.419 -17.237 1.00 18.74  ? 409  SER B O     1 
ATOM   7141 C  CB    . SER B 1 423 ? 20.296  63.608 -18.232 1.00 18.25  ? 409  SER B CB    1 
ATOM   7142 O  OG    . SER B 1 423 ? 19.992  62.602 -17.289 1.00 16.91  ? 409  SER B OG    1 
ATOM   7143 N  N     . ILE B 1 424 ? 21.842  65.375 -15.505 1.00 19.10  ? 410  ILE B N     1 
ATOM   7144 C  CA    . ILE B 1 424 ? 23.066  65.328 -14.719 1.00 16.90  ? 410  ILE B CA    1 
ATOM   7145 C  C     . ILE B 1 424 ? 23.394  63.875 -14.410 1.00 18.10  ? 410  ILE B C     1 
ATOM   7146 O  O     . ILE B 1 424 ? 22.503  63.019 -14.255 1.00 18.90  ? 410  ILE B O     1 
ATOM   7147 C  CB    . ILE B 1 424 ? 22.996  66.189 -13.438 1.00 18.95  ? 410  ILE B CB    1 
ATOM   7148 C  CG1   . ILE B 1 424 ? 21.931  65.688 -12.449 1.00 18.10  ? 410  ILE B CG1   1 
ATOM   7149 C  CG2   . ILE B 1 424 ? 22.705  67.648 -13.794 1.00 20.47  ? 410  ILE B CG2   1 
ATOM   7150 C  CD1   . ILE B 1 424 ? 22.135  66.252 -11.042 1.00 19.80  ? 410  ILE B CD1   1 
ATOM   7151 N  N     . GLY B 1 425 ? 24.687  63.597 -14.333 1.00 17.91  ? 411  GLY B N     1 
ATOM   7152 C  CA    . GLY B 1 425 ? 25.225  62.257 -14.323 1.00 18.25  ? 411  GLY B CA    1 
ATOM   7153 C  C     . GLY B 1 425 ? 25.698  61.787 -15.682 1.00 16.40  ? 411  GLY B C     1 
ATOM   7154 O  O     . GLY B 1 425 ? 26.588  60.931 -15.754 1.00 15.91  ? 411  GLY B O     1 
ATOM   7155 N  N     . TYR B 1 426 ? 25.150  62.358 -16.757 1.00 18.06  ? 412  TYR B N     1 
ATOM   7156 C  CA    . TYR B 1 426 ? 25.576  61.996 -18.106 1.00 18.43  ? 412  TYR B CA    1 
ATOM   7157 C  C     . TYR B 1 426 ? 27.095  62.067 -18.267 1.00 17.23  ? 412  TYR B C     1 
ATOM   7158 O  O     . TYR B 1 426 ? 27.717  61.153 -18.824 1.00 17.19  ? 412  TYR B O     1 
ATOM   7159 C  CB    . TYR B 1 426 ? 24.894  62.919 -19.125 1.00 17.90  ? 412  TYR B CB    1 
ATOM   7160 C  CG    . TYR B 1 426 ? 25.485  62.797 -20.514 1.00 18.84  ? 412  TYR B CG    1 
ATOM   7161 C  CD1   . TYR B 1 426 ? 25.118  61.758 -21.362 1.00 18.73  ? 412  TYR B CD1   1 
ATOM   7162 C  CD2   . TYR B 1 426 ? 26.432  63.708 -20.961 1.00 17.44  ? 412  TYR B CD2   1 
ATOM   7163 C  CE1   . TYR B 1 426 ? 25.673  61.644 -22.635 1.00 16.71  ? 412  TYR B CE1   1 
ATOM   7164 C  CE2   . TYR B 1 426 ? 26.993  63.599 -22.208 1.00 19.04  ? 412  TYR B CE2   1 
ATOM   7165 C  CZ    . TYR B 1 426 ? 26.619  62.569 -23.038 1.00 19.10  ? 412  TYR B CZ    1 
ATOM   7166 O  OH    . TYR B 1 426 ? 27.197  62.485 -24.279 1.00 18.24  ? 412  TYR B OH    1 
ATOM   7167 N  N     . THR B 1 427 ? 27.713  63.129 -17.752 1.00 18.31  ? 413  THR B N     1 
ATOM   7168 C  CA    . THR B 1 427 ? 29.090  63.439 -18.112 1.00 17.29  ? 413  THR B CA    1 
ATOM   7169 C  C     . THR B 1 427 ? 30.077  62.376 -17.624 1.00 16.17  ? 413  THR B C     1 
ATOM   7170 O  O     . THR B 1 427 ? 30.930  61.922 -18.389 1.00 17.28  ? 413  THR B O     1 
ATOM   7171 C  CB    . THR B 1 427 ? 29.439  64.822 -17.577 1.00 19.49  ? 413  THR B CB    1 
ATOM   7172 O  OG1   . THR B 1 427 ? 28.605  65.791 -18.234 1.00 19.15  ? 413  THR B OG1   1 
ATOM   7173 C  CG2   . THR B 1 427 ? 30.910  65.142 -17.800 1.00 16.89  ? 413  THR B CG2   1 
ATOM   7174 N  N     . LEU B 1 428 ? 29.976  61.944 -16.366 1.00 16.05  ? 414  LEU B N     1 
ATOM   7175 C  CA    . LEU B 1 428 ? 30.958  60.974 -15.874 1.00 17.90  ? 414  LEU B CA    1 
ATOM   7176 C  C     . LEU B 1 428 ? 30.907  59.672 -16.674 1.00 16.16  ? 414  LEU B C     1 
ATOM   7177 O  O     . LEU B 1 428 ? 31.948  59.117 -17.042 1.00 15.74  ? 414  LEU B O     1 
ATOM   7178 C  CB    . LEU B 1 428 ? 30.731  60.699 -14.386 1.00 15.95  ? 414  LEU B CB    1 
ATOM   7179 C  CG    . LEU B 1 428 ? 31.664  59.693 -13.713 1.00 18.11  ? 414  LEU B CG    1 
ATOM   7180 C  CD1   . LEU B 1 428 ? 33.090  60.232 -13.691 1.00 14.95  ? 414  LEU B CD1   1 
ATOM   7181 C  CD2   . LEU B 1 428 ? 31.173  59.388 -12.293 1.00 16.68  ? 414  LEU B CD2   1 
ATOM   7182 N  N     . ALA B 1 429 ? 29.705  59.179 -16.965 1.00 17.58  ? 415  ALA B N     1 
ATOM   7183 C  CA    . ALA B 1 429 ? 29.574  57.929 -17.706 1.00 16.80  ? 415  ALA B CA    1 
ATOM   7184 C  C     . ALA B 1 429 ? 29.884  58.127 -19.185 1.00 15.98  ? 415  ALA B C     1 
ATOM   7185 O  O     . ALA B 1 429 ? 30.452  57.238 -19.823 1.00 18.15  ? 415  ALA B O     1 
ATOM   7186 C  CB    . ALA B 1 429 ? 28.170  57.356 -17.517 1.00 15.89  ? 415  ALA B CB    1 
ATOM   7187 N  N     . ALA B 1 430 ? 29.503  59.279 -19.748 1.00 16.94  ? 416  ALA B N     1 
ATOM   7188 C  CA    . ALA B 1 430 ? 29.874  59.599 -21.124 1.00 17.07  ? 416  ALA B CA    1 
ATOM   7189 C  C     . ALA B 1 430 ? 31.388  59.652 -21.291 1.00 17.33  ? 416  ALA B C     1 
ATOM   7190 O  O     . ALA B 1 430 ? 31.917  59.261 -22.341 1.00 17.47  ? 416  ALA B O     1 
ATOM   7191 C  CB    . ALA B 1 430 ? 29.248  60.932 -21.546 1.00 15.94  ? 416  ALA B CB    1 
ATOM   7192 N  N     . ALA B 1 431 ? 32.097  60.161 -20.276 1.00 18.17  ? 417  ALA B N     1 
ATOM   7193 C  CA    . ALA B 1 431 ? 33.556  60.192 -20.322 1.00 17.52  ? 417  ALA B CA    1 
ATOM   7194 C  C     . ALA B 1 431 ? 34.121  58.789 -20.426 1.00 16.72  ? 417  ALA B C     1 
ATOM   7195 O  O     . ALA B 1 431 ? 35.122  58.569 -21.114 1.00 17.69  ? 417  ALA B O     1 
ATOM   7196 C  CB    . ALA B 1 431 ? 34.120  60.883 -19.081 1.00 16.22  ? 417  ALA B CB    1 
ATOM   7197 N  N     . PHE B 1 432 ? 33.500  57.826 -19.741 1.00 17.06  ? 418  PHE B N     1 
ATOM   7198 C  CA    . PHE B 1 432 ? 33.968  56.448 -19.854 1.00 18.26  ? 418  PHE B CA    1 
ATOM   7199 C  C     . PHE B 1 432 ? 33.801  55.921 -21.276 1.00 17.68  ? 418  PHE B C     1 
ATOM   7200 O  O     . PHE B 1 432 ? 34.695  55.250 -21.806 1.00 19.30  ? 418  PHE B O     1 
ATOM   7201 C  CB    . PHE B 1 432 ? 33.216  55.557 -18.868 1.00 17.73  ? 418  PHE B CB    1 
ATOM   7202 C  CG    . PHE B 1 432 ? 33.472  54.083 -19.059 1.00 19.81  ? 418  PHE B CG    1 
ATOM   7203 C  CD1   . PHE B 1 432 ? 34.732  53.541 -18.818 1.00 18.71  ? 418  PHE B CD1   1 
ATOM   7204 C  CD2   . PHE B 1 432 ? 32.449  53.238 -19.489 1.00 17.99  ? 418  PHE B CD2   1 
ATOM   7205 C  CE1   . PHE B 1 432 ? 34.971  52.183 -18.995 1.00 18.51  ? 418  PHE B CE1   1 
ATOM   7206 C  CE2   . PHE B 1 432 ? 32.672  51.875 -19.659 1.00 18.30  ? 418  PHE B CE2   1 
ATOM   7207 C  CZ    . PHE B 1 432 ? 33.947  51.352 -19.422 1.00 19.24  ? 418  PHE B CZ    1 
ATOM   7208 N  N     . GLY B 1 433 ? 32.668  56.219 -21.914 1.00 17.49  ? 419  GLY B N     1 
ATOM   7209 C  CA    . GLY B 1 433 ? 32.494  55.827 -23.304 1.00 17.27  ? 419  GLY B CA    1 
ATOM   7210 C  C     . GLY B 1 433 ? 33.457  56.540 -24.235 1.00 17.59  ? 419  GLY B C     1 
ATOM   7211 O  O     . GLY B 1 433 ? 33.980  55.941 -25.177 1.00 18.48  ? 419  GLY B O     1 
ATOM   7212 N  N     . ALA B 1 434 ? 33.690  57.833 -24.000 1.00 17.13  ? 420  ALA B N     1 
ATOM   7213 C  CA    . ALA B 1 434 ? 34.587  58.587 -24.869 1.00 18.92  ? 420  ALA B CA    1 
ATOM   7214 C  C     . ALA B 1 434 ? 36.024  58.089 -24.765 1.00 20.88  ? 420  ALA B C     1 
ATOM   7215 O  O     . ALA B 1 434 ? 36.716  57.954 -25.785 1.00 21.11  ? 420  ALA B O     1 
ATOM   7216 C  CB    . ALA B 1 434 ? 34.520  60.075 -24.527 1.00 18.92  ? 420  ALA B CB    1 
ATOM   7217 N  N     . GLN B 1 435 ? 36.499  57.822 -23.539 1.00 20.72  ? 421  GLN B N     1 
ATOM   7218 C  CA    . GLN B 1 435 ? 37.851  57.294 -23.371 1.00 19.07  ? 421  GLN B CA    1 
ATOM   7219 C  C     . GLN B 1 435 ? 37.989  55.910 -24.004 1.00 20.97  ? 421  GLN B C     1 
ATOM   7220 O  O     . GLN B 1 435 ? 39.051  55.564 -24.536 1.00 23.42  ? 421  GLN B O     1 
ATOM   7221 C  CB    . GLN B 1 435 ? 38.220  57.253 -21.885 1.00 20.31  ? 421  GLN B CB    1 
ATOM   7222 C  CG    . GLN B 1 435 ? 39.686  56.920 -21.616 1.00 20.87  ? 421  GLN B CG    1 
ATOM   7223 C  CD    . GLN B 1 435 ? 40.631  58.086 -21.885 1.00 23.06  ? 421  GLN B CD    1 
ATOM   7224 O  OE1   . GLN B 1 435 ? 41.005  58.355 -23.026 1.00 23.60  ? 421  GLN B OE1   1 
ATOM   7225 N  NE2   . GLN B 1 435 ? 41.006  58.791 -20.831 1.00 21.01  ? 421  GLN B NE2   1 
ATOM   7226 N  N     . THR B 1 436 ? 36.939  55.087 -23.919 1.00 19.61  ? 422  THR B N     1 
ATOM   7227 C  CA    . THR B 1 436 ? 36.946  53.809 -24.620 1.00 20.31  ? 422  THR B CA    1 
ATOM   7228 C  C     . THR B 1 436 ? 37.156  54.023 -26.117 1.00 22.29  ? 422  THR B C     1 
ATOM   7229 O  O     . THR B 1 436 ? 38.006  53.370 -26.737 1.00 23.20  ? 422  THR B O     1 
ATOM   7230 C  CB    . THR B 1 436 ? 35.630  53.067 -24.344 1.00 19.60  ? 422  THR B CB    1 
ATOM   7231 O  OG1   . THR B 1 436 ? 35.427  52.959 -22.928 1.00 18.39  ? 422  THR B OG1   1 
ATOM   7232 C  CG2   . THR B 1 436 ? 35.622  51.681 -24.951 1.00 19.55  ? 422  THR B CG2   1 
ATOM   7233 N  N     . ALA B 1 437 ? 36.433  54.991 -26.698 1.00 19.89  ? 423  ALA B N     1 
ATOM   7234 C  CA    . ALA B 1 437 ? 36.585  55.289 -28.123 1.00 22.68  ? 423  ALA B CA    1 
ATOM   7235 C  C     . ALA B 1 437 ? 37.989  55.770 -28.462 1.00 23.62  ? 423  ALA B C     1 
ATOM   7236 O  O     . ALA B 1 437 ? 38.521  55.424 -29.522 1.00 24.21  ? 423  ALA B O     1 
ATOM   7237 C  CB    . ALA B 1 437 ? 35.568  56.344 -28.563 1.00 19.91  ? 423  ALA B CB    1 
ATOM   7238 N  N     . CYS B 1 438 ? 38.586  56.604 -27.602 1.00 23.05  ? 424  CYS B N     1 
ATOM   7239 C  CA    . CYS B 1 438 ? 39.842  57.302 -27.897 1.00 23.80  ? 424  CYS B CA    1 
ATOM   7240 C  C     . CYS B 1 438 ? 40.834  57.103 -26.748 1.00 26.19  ? 424  CYS B C     1 
ATOM   7241 O  O     . CYS B 1 438 ? 41.120  58.038 -25.988 1.00 23.53  ? 424  CYS B O     1 
ATOM   7242 C  CB    . CYS B 1 438 ? 39.579  58.796 -28.122 1.00 23.72  ? 424  CYS B CB    1 
ATOM   7243 S  SG    . CYS B 1 438 ? 38.290  59.197 -29.357 1.00 24.81  ? 424  CYS B SG    1 
ATOM   7244 N  N     . PRO B 1 439 ? 41.393  55.895 -26.605 1.00 24.55  ? 425  PRO B N     1 
ATOM   7245 C  CA    . PRO B 1 439 ? 42.310  55.636 -25.478 1.00 28.37  ? 425  PRO B CA    1 
ATOM   7246 C  C     . PRO B 1 439 ? 43.536  56.543 -25.450 1.00 29.25  ? 425  PRO B C     1 
ATOM   7247 O  O     . PRO B 1 439 ? 44.088  56.777 -24.368 1.00 29.97  ? 425  PRO B O     1 
ATOM   7248 C  CB    . PRO B 1 439 ? 42.707  54.165 -25.676 1.00 26.55  ? 425  PRO B CB    1 
ATOM   7249 C  CG    . PRO B 1 439 ? 42.375  53.858 -27.100 1.00 26.15  ? 425  PRO B CG    1 
ATOM   7250 C  CD    . PRO B 1 439 ? 41.212  54.711 -27.458 1.00 26.35  ? 425  PRO B CD    1 
ATOM   7251 N  N     . ASN B 1 440 ? 43.988  57.053 -26.597 1.00 28.01  ? 426  ASN B N     1 
ATOM   7252 C  CA    . ASN B 1 440 ? 45.208  57.848 -26.652 1.00 29.27  ? 426  ASN B CA    1 
ATOM   7253 C  C     . ASN B 1 440 ? 44.968  59.347 -26.586 1.00 27.35  ? 426  ASN B C     1 
ATOM   7254 O  O     . ASN B 1 440 ? 45.923  60.123 -26.713 1.00 30.92  ? 426  ASN B O     1 
ATOM   7255 C  CB    . ASN B 1 440 ? 46.012  57.490 -27.911 1.00 31.24  ? 426  ASN B CB    1 
ATOM   7256 C  CG    . ASN B 1 440 ? 46.365  56.019 -27.949 1.00 33.35  ? 426  ASN B CG    1 
ATOM   7257 O  OD1   . ASN B 1 440 ? 46.526  55.395 -26.903 1.00 32.43  ? 426  ASN B OD1   1 
ATOM   7258 N  ND2   . ASN B 1 440 ? 46.481  55.455 -29.142 1.00 36.68  ? 426  ASN B ND2   1 
ATOM   7259 N  N     . ARG B 1 441 ? 43.735  59.782 -26.417 1.00 24.71  ? 427  ARG B N     1 
ATOM   7260 C  CA    . ARG B 1 441 ? 43.455  61.195 -26.239 1.00 25.60  ? 427  ARG B CA    1 
ATOM   7261 C  C     . ARG B 1 441 ? 43.224  61.488 -24.765 1.00 25.88  ? 427  ARG B C     1 
ATOM   7262 O  O     . ARG B 1 441 ? 42.770  60.623 -24.006 1.00 21.98  ? 427  ARG B O     1 
ATOM   7263 C  CB    . ARG B 1 441 ? 42.252  61.626 -27.068 1.00 25.31  ? 427  ARG B CB    1 
ATOM   7264 C  CG    . ARG B 1 441 ? 42.543  61.579 -28.552 1.00 26.77  ? 427  ARG B CG    1 
ATOM   7265 C  CD    . ARG B 1 441 ? 41.352  62.021 -29.366 1.00 26.12  ? 427  ARG B CD    1 
ATOM   7266 N  NE    . ARG B 1 441 ? 40.997  63.412 -29.123 1.00 25.66  ? 427  ARG B NE    1 
ATOM   7267 C  CZ    . ARG B 1 441 ? 40.145  64.094 -29.877 1.00 27.25  ? 427  ARG B CZ    1 
ATOM   7268 N  NH1   . ARG B 1 441 ? 39.548  63.538 -30.916 1.00 27.44  ? 427  ARG B NH1   1 
ATOM   7269 N  NH2   . ARG B 1 441 ? 39.889  65.366 -29.582 1.00 26.47  ? 427  ARG B NH2   1 
ATOM   7270 N  N     . ARG B 1 442 ? 43.582  62.709 -24.365 1.00 24.07  ? 428  ARG B N     1 
ATOM   7271 C  CA    . ARG B 1 442 ? 43.433  63.156 -22.991 1.00 23.02  ? 428  ARG B CA    1 
ATOM   7272 C  C     . ARG B 1 442 ? 41.987  63.559 -22.748 1.00 22.16  ? 428  ARG B C     1 
ATOM   7273 O  O     . ARG B 1 442 ? 41.431  64.382 -23.479 1.00 23.34  ? 428  ARG B O     1 
ATOM   7274 C  CB    . ARG B 1 442 ? 44.368  64.336 -22.708 1.00 22.95  ? 428  ARG B CB    1 
ATOM   7275 C  CG    . ARG B 1 442 ? 44.358  64.793 -21.266 1.00 22.44  ? 428  ARG B CG    1 
ATOM   7276 C  CD    . ARG B 1 442 ? 45.480  65.790 -20.979 1.00 25.53  ? 428  ARG B CD    1 
ATOM   7277 N  NE    . ARG B 1 442 ? 45.230  67.103 -21.562 1.00 23.36  ? 428  ARG B NE    1 
ATOM   7278 C  CZ    . ARG B 1 442 ? 45.862  68.217 -21.211 1.00 26.38  ? 428  ARG B CZ    1 
ATOM   7279 N  NH1   . ARG B 1 442 ? 46.835  68.213 -20.299 1.00 25.46  ? 428  ARG B NH1   1 
ATOM   7280 N  NH2   . ARG B 1 442 ? 45.502  69.368 -21.772 1.00 26.25  ? 428  ARG B NH2   1 
ATOM   7281 N  N     . VAL B 1 443 ? 41.377  62.976 -21.727 1.00 21.26  ? 429  VAL B N     1 
ATOM   7282 C  CA    . VAL B 1 443 ? 39.975  63.207 -21.391 1.00 22.65  ? 429  VAL B CA    1 
ATOM   7283 C  C     . VAL B 1 443 ? 39.922  64.031 -20.109 1.00 24.02  ? 429  VAL B C     1 
ATOM   7284 O  O     . VAL B 1 443 ? 40.454  63.604 -19.072 1.00 22.10  ? 429  VAL B O     1 
ATOM   7285 C  CB    . VAL B 1 443 ? 39.222  61.876 -21.234 1.00 23.87  ? 429  VAL B CB    1 
ATOM   7286 C  CG1   . VAL B 1 443 ? 37.877  62.067 -20.530 1.00 20.15  ? 429  VAL B CG1   1 
ATOM   7287 C  CG2   . VAL B 1 443 ? 39.037  61.216 -22.598 1.00 22.19  ? 429  VAL B CG2   1 
ATOM   7288 N  N     . ILE B 1 444 ? 39.297  65.212 -20.186 1.00 22.26  ? 430  ILE B N     1 
ATOM   7289 C  CA    . ILE B 1 444 ? 39.065  66.080 -19.033 1.00 22.74  ? 430  ILE B CA    1 
ATOM   7290 C  C     . ILE B 1 444 ? 37.571  66.039 -18.714 1.00 22.81  ? 430  ILE B C     1 
ATOM   7291 O  O     . ILE B 1 444 ? 36.732  66.342 -19.572 1.00 21.54  ? 430  ILE B O     1 
ATOM   7292 C  CB    . ILE B 1 444 ? 39.523  67.533 -19.274 1.00 23.18  ? 430  ILE B CB    1 
ATOM   7293 C  CG1   . ILE B 1 444 ? 41.044  67.655 -19.447 1.00 23.62  ? 430  ILE B CG1   1 
ATOM   7294 C  CG2   . ILE B 1 444 ? 39.109  68.433 -18.117 1.00 21.34  ? 430  ILE B CG2   1 
ATOM   7295 C  CD1   . ILE B 1 444 ? 41.476  67.953 -20.847 1.00 25.60  ? 430  ILE B CD1   1 
ATOM   7296 N  N     . VAL B 1 445 ? 37.236  65.673 -17.479 1.00 21.68  ? 431  VAL B N     1 
ATOM   7297 C  CA    . VAL B 1 445 ? 35.845  65.538 -17.044 1.00 22.27  ? 431  VAL B CA    1 
ATOM   7298 C  C     . VAL B 1 445 ? 35.551  66.660 -16.059 1.00 20.85  ? 431  VAL B C     1 
ATOM   7299 O  O     . VAL B 1 445 ? 36.174  66.734 -14.992 1.00 20.34  ? 431  VAL B O     1 
ATOM   7300 C  CB    . VAL B 1 445 ? 35.583  64.166 -16.398 1.00 21.13  ? 431  VAL B CB    1 
ATOM   7301 C  CG1   . VAL B 1 445 ? 34.086  63.969 -16.133 1.00 21.01  ? 431  VAL B CG1   1 
ATOM   7302 C  CG2   . VAL B 1 445 ? 36.137  63.052 -17.273 1.00 21.23  ? 431  VAL B CG2   1 
ATOM   7303 N  N     . LEU B 1 446 ? 34.598  67.531 -16.408 1.00 19.80  ? 432  LEU B N     1 
ATOM   7304 C  CA    . LEU B 1 446 ? 34.149  68.611 -15.524 1.00 20.30  ? 432  LEU B CA    1 
ATOM   7305 C  C     . LEU B 1 446 ? 32.751  68.287 -14.991 1.00 22.41  ? 432  LEU B C     1 
ATOM   7306 O  O     . LEU B 1 446 ? 31.743  68.491 -15.678 1.00 18.64  ? 432  LEU B O     1 
ATOM   7307 C  CB    . LEU B 1 446 ? 34.176  69.942 -16.266 1.00 20.43  ? 432  LEU B CB    1 
ATOM   7308 C  CG    . LEU B 1 446 ? 35.585  70.329 -16.718 1.00 22.12  ? 432  LEU B CG    1 
ATOM   7309 C  CD1   . LEU B 1 446 ? 35.551  71.205 -18.001 1.00 21.85  ? 432  LEU B CD1   1 
ATOM   7310 C  CD2   . LEU B 1 446 ? 36.299  71.034 -15.588 1.00 20.80  ? 432  LEU B CD2   1 
ATOM   7311 N  N     . THR B 1 447 ? 32.669  67.831 -13.743 1.00 20.48  ? 433  THR B N     1 
ATOM   7312 C  CA    . THR B 1 447 ? 31.361  67.469 -13.221 1.00 20.21  ? 433  THR B CA    1 
ATOM   7313 C  C     . THR B 1 447 ? 31.121  68.101 -11.857 1.00 21.31  ? 433  THR B C     1 
ATOM   7314 O  O     . THR B 1 447 ? 32.036  68.208 -11.044 1.00 21.41  ? 433  THR B O     1 
ATOM   7315 C  CB    . THR B 1 447 ? 31.210  65.949 -13.138 1.00 20.08  ? 433  THR B CB    1 
ATOM   7316 O  OG1   . THR B 1 447 ? 29.939  65.640 -12.548 1.00 18.73  ? 433  THR B OG1   1 
ATOM   7317 C  CG2   . THR B 1 447 ? 32.336  65.328 -12.302 1.00 17.70  ? 433  THR B CG2   1 
ATOM   7318 N  N     . GLY B 1 448 ? 29.877  68.511 -11.604 1.00 23.68  ? 434  GLY B N     1 
ATOM   7319 C  CA    . GLY B 1 448 ? 29.518  68.939 -10.268 1.00 22.59  ? 434  GLY B CA    1 
ATOM   7320 C  C     . GLY B 1 448 ? 29.534  67.775 -9.299  1.00 21.95  ? 434  GLY B C     1 
ATOM   7321 O  O     . GLY B 1 448 ? 29.516  66.605 -9.684  1.00 21.17  ? 434  GLY B O     1 
ATOM   7322 N  N     . ASP B 1 449 ? 29.594  68.095 -8.009  1.00 23.99  ? 435  ASP B N     1 
ATOM   7323 C  CA    . ASP B 1 449 ? 29.535  67.024 -7.023  1.00 23.84  ? 435  ASP B CA    1 
ATOM   7324 C  C     . ASP B 1 449 ? 28.179  66.334 -7.066  1.00 22.64  ? 435  ASP B C     1 
ATOM   7325 O  O     . ASP B 1 449 ? 28.102  65.106 -6.977  1.00 21.15  ? 435  ASP B O     1 
ATOM   7326 C  CB    . ASP B 1 449 ? 29.846  67.563 -5.629  1.00 24.42  ? 435  ASP B CB    1 
ATOM   7327 C  CG    . ASP B 1 449 ? 28.990  68.761 -5.257  1.00 28.88  ? 435  ASP B CG    1 
ATOM   7328 O  OD1   . ASP B 1 449 ? 28.682  69.579 -6.145  1.00 28.70  ? 435  ASP B OD1   1 
ATOM   7329 O  OD2   . ASP B 1 449 ? 28.646  68.897 -4.070  1.00 29.79  ? 435  ASP B OD2   1 
ATOM   7330 N  N     . GLY B 1 450 ? 27.106  67.103 -7.251  1.00 22.80  ? 436  GLY B N     1 
ATOM   7331 C  CA    . GLY B 1 450 ? 25.788  66.501 -7.334  1.00 22.16  ? 436  GLY B CA    1 
ATOM   7332 C  C     . GLY B 1 450 ? 25.637  65.595 -8.541  1.00 22.02  ? 436  GLY B C     1 
ATOM   7333 O  O     . GLY B 1 450 ? 25.132  64.474 -8.434  1.00 21.14  ? 436  GLY B O     1 
ATOM   7334 N  N     . ALA B 1 451 ? 26.074  66.071 -9.709  1.00 21.34  ? 437  ALA B N     1 
ATOM   7335 C  CA    . ALA B 1 451 ? 25.935  65.280 -10.928 1.00 20.73  ? 437  ALA B CA    1 
ATOM   7336 C  C     . ALA B 1 451 ? 26.655  63.943 -10.805 1.00 19.73  ? 437  ALA B C     1 
ATOM   7337 O  O     . ALA B 1 451 ? 26.082  62.895 -11.122 1.00 17.22  ? 437  ALA B O     1 
ATOM   7338 C  CB    . ALA B 1 451 ? 26.466  66.063 -12.133 1.00 20.34  ? 437  ALA B CB    1 
ATOM   7339 N  N     . ALA B 1 452 ? 27.907  63.950 -10.311 1.00 19.05  ? 438  ALA B N     1 
ATOM   7340 C  CA    . ALA B 1 452 ? 28.688  62.714 -10.262 1.00 18.91  ? 438  ALA B CA    1 
ATOM   7341 C  C     . ALA B 1 452 ? 28.061  61.647 -9.375  1.00 19.43  ? 438  ALA B C     1 
ATOM   7342 O  O     . ALA B 1 452 ? 28.380  60.461 -9.545  1.00 17.37  ? 438  ALA B O     1 
ATOM   7343 C  CB    . ALA B 1 452 ? 30.136  62.968 -9.799  1.00 17.28  ? 438  ALA B CB    1 
ATOM   7344 N  N     . GLN B 1 453 ? 27.190  62.028 -8.429  1.00 19.36  ? 439  GLN B N     1 
ATOM   7345 C  CA    . GLN B 1 453 ? 26.571  61.020 -7.565  1.00 20.24  ? 439  GLN B CA    1 
ATOM   7346 C  C     . GLN B 1 453 ? 25.658  60.081 -8.351  1.00 19.14  ? 439  GLN B C     1 
ATOM   7347 O  O     . GLN B 1 453 ? 25.480  58.913 -7.967  1.00 16.52  ? 439  GLN B O     1 
ATOM   7348 C  CB    . GLN B 1 453 ? 25.779  61.691 -6.443  1.00 19.53  ? 439  GLN B CB    1 
ATOM   7349 C  CG    . GLN B 1 453 ? 26.629  62.512 -5.481  1.00 19.89  ? 439  GLN B CG    1 
ATOM   7350 C  CD    . GLN B 1 453 ? 25.858  62.925 -4.247  1.00 24.00  ? 439  GLN B CD    1 
ATOM   7351 O  OE1   . GLN B 1 453 ? 24.632  63.104 -4.290  1.00 28.40  ? 439  GLN B OE1   1 
ATOM   7352 N  NE2   . GLN B 1 453 ? 26.559  63.094 -3.150  1.00 23.49  ? 439  GLN B NE2   1 
ATOM   7353 N  N     . LEU B 1 454 ? 25.049  60.576 -9.431  1.00 16.76  ? 440  LEU B N     1 
ATOM   7354 C  CA    . LEU B 1 454 ? 24.033  59.789 -10.115 1.00 17.96  ? 440  LEU B CA    1 
ATOM   7355 C  C     . LEU B 1 454 ? 24.631  58.614 -10.872 1.00 15.32  ? 440  LEU B C     1 
ATOM   7356 O  O     . LEU B 1 454 ? 23.922  57.643 -11.150 1.00 16.90  ? 440  LEU B O     1 
ATOM   7357 C  CB    . LEU B 1 454 ? 23.216  60.683 -11.067 1.00 17.27  ? 440  LEU B CB    1 
ATOM   7358 C  CG    . LEU B 1 454 ? 22.131  61.550 -10.413 1.00 17.69  ? 440  LEU B CG    1 
ATOM   7359 C  CD1   . LEU B 1 454 ? 22.708  62.839 -9.854  1.00 17.31  ? 440  LEU B CD1   1 
ATOM   7360 C  CD2   . LEU B 1 454 ? 20.965  61.854 -11.406 1.00 16.45  ? 440  LEU B CD2   1 
ATOM   7361 N  N     . THR B 1 455 ? 25.916  58.681 -11.220 1.00 18.02  ? 441  THR B N     1 
ATOM   7362 C  CA    . THR B 1 455 ? 26.521  57.667 -12.077 1.00 16.36  ? 441  THR B CA    1 
ATOM   7363 C  C     . THR B 1 455 ? 27.887  57.236 -11.546 1.00 18.18  ? 441  THR B C     1 
ATOM   7364 O  O     . THR B 1 455 ? 28.725  56.753 -12.317 1.00 17.29  ? 441  THR B O     1 
ATOM   7365 C  CB    . THR B 1 455 ? 26.636  58.197 -13.510 1.00 16.97  ? 441  THR B CB    1 
ATOM   7366 O  OG1   . THR B 1 455 ? 27.397  59.417 -13.525 1.00 15.48  ? 441  THR B OG1   1 
ATOM   7367 C  CG2   . THR B 1 455 ? 25.247  58.497 -14.077 1.00 16.49  ? 441  THR B CG2   1 
ATOM   7368 N  N     . ILE B 1 456 ? 28.126  57.378 -10.238 1.00 17.88  ? 442  ILE B N     1 
ATOM   7369 C  CA    . ILE B 1 456 ? 29.473  57.204 -9.699  1.00 17.91  ? 442  ILE B CA    1 
ATOM   7370 C  C     . ILE B 1 456 ? 30.048  55.823 -10.001 1.00 16.92  ? 442  ILE B C     1 
ATOM   7371 O  O     . ILE B 1 456 ? 31.269  55.673 -10.142 1.00 16.89  ? 442  ILE B O     1 
ATOM   7372 C  CB    . ILE B 1 456 ? 29.470  57.485 -8.182  1.00 18.40  ? 442  ILE B CB    1 
ATOM   7373 C  CG1   . ILE B 1 456 ? 30.907  57.620 -7.671  1.00 18.33  ? 442  ILE B CG1   1 
ATOM   7374 C  CG2   . ILE B 1 456 ? 28.769  56.370 -7.425  1.00 17.07  ? 442  ILE B CG2   1 
ATOM   7375 C  CD1   . ILE B 1 456 ? 31.700  58.710 -8.374  1.00 16.75  ? 442  ILE B CD1   1 
ATOM   7376 N  N     . GLN B 1 457 ? 29.206  54.795 -10.094 1.00 17.76  ? 443  GLN B N     1 
ATOM   7377 C  CA    . GLN B 1 457 ? 29.738  53.438 -10.207 1.00 17.05  ? 443  GLN B CA    1 
ATOM   7378 C  C     . GLN B 1 457 ? 30.496  53.201 -11.510 1.00 19.06  ? 443  GLN B C     1 
ATOM   7379 O  O     . GLN B 1 457 ? 31.288  52.248 -11.583 1.00 16.98  ? 443  GLN B O     1 
ATOM   7380 C  CB    . GLN B 1 457 ? 28.614  52.413 -10.048 1.00 18.61  ? 443  GLN B CB    1 
ATOM   7381 C  CG    . GLN B 1 457 ? 27.423  52.610 -10.975 1.00 18.26  ? 443  GLN B CG    1 
ATOM   7382 C  CD    . GLN B 1 457 ? 26.351  53.475 -10.358 1.00 17.20  ? 443  GLN B CD    1 
ATOM   7383 O  OE1   . GLN B 1 457 ? 26.207  54.666 -10.683 1.00 16.01  ? 443  GLN B OE1   1 
ATOM   7384 N  NE2   . GLN B 1 457 ? 25.597  52.889 -9.445  1.00 16.04  ? 443  GLN B NE2   1 
ATOM   7385 N  N     . GLU B 1 458 ? 30.301  54.055 -12.524 1.00 15.23  ? 444  GLU B N     1 
ATOM   7386 C  CA    . GLU B 1 458 ? 31.095  53.933 -13.740 1.00 17.94  ? 444  GLU B CA    1 
ATOM   7387 C  C     . GLU B 1 458 ? 32.526  54.418 -13.546 1.00 18.20  ? 444  GLU B C     1 
ATOM   7388 O  O     . GLU B 1 458 ? 33.387  54.117 -14.380 1.00 18.41  ? 444  GLU B O     1 
ATOM   7389 C  CB    . GLU B 1 458 ? 30.454  54.685 -14.908 1.00 17.99  ? 444  GLU B CB    1 
ATOM   7390 C  CG    . GLU B 1 458 ? 30.398  53.823 -16.167 1.00 17.93  ? 444  GLU B CG    1 
ATOM   7391 C  CD    . GLU B 1 458 ? 29.742  52.479 -15.876 1.00 19.08  ? 444  GLU B CD    1 
ATOM   7392 O  OE1   . GLU B 1 458 ? 28.780  52.450 -15.097 1.00 18.00  ? 444  GLU B OE1   1 
ATOM   7393 O  OE2   . GLU B 1 458 ? 30.182  51.439 -16.393 1.00 20.92  ? 444  GLU B OE2   1 
ATOM   7394 N  N     . LEU B 1 459 ? 32.812  55.150 -12.468 1.00 17.68  ? 445  LEU B N     1 
ATOM   7395 C  CA    . LEU B 1 459 ? 34.214  55.369 -12.125 1.00 18.70  ? 445  LEU B CA    1 
ATOM   7396 C  C     . LEU B 1 459 ? 34.928  54.032 -11.945 1.00 19.73  ? 445  LEU B C     1 
ATOM   7397 O  O     . LEU B 1 459 ? 36.092  53.875 -12.341 1.00 20.85  ? 445  LEU B O     1 
ATOM   7398 C  CB    . LEU B 1 459 ? 34.312  56.227 -10.863 1.00 17.67  ? 445  LEU B CB    1 
ATOM   7399 C  CG    . LEU B 1 459 ? 35.680  56.419 -10.201 1.00 21.76  ? 445  LEU B CG    1 
ATOM   7400 C  CD1   . LEU B 1 459 ? 36.751  56.880 -11.197 1.00 18.34  ? 445  LEU B CD1   1 
ATOM   7401 C  CD2   . LEU B 1 459 ? 35.552  57.402 -9.058  1.00 20.17  ? 445  LEU B CD2   1 
ATOM   7402 N  N     . GLY B 1 460 ? 34.221  53.046 -11.385 1.00 19.24  ? 446  GLY B N     1 
ATOM   7403 C  CA    . GLY B 1 460 ? 34.790  51.719 -11.229 1.00 19.27  ? 446  GLY B CA    1 
ATOM   7404 C  C     . GLY B 1 460 ? 35.124  51.061 -12.553 1.00 20.81  ? 446  GLY B C     1 
ATOM   7405 O  O     . GLY B 1 460 ? 36.109  50.319 -12.657 1.00 19.66  ? 446  GLY B O     1 
ATOM   7406 N  N     . SER B 1 461 ? 34.299  51.305 -13.578 1.00 19.10  ? 447  SER B N     1 
ATOM   7407 C  CA    . SER B 1 461 ? 34.603  50.796 -14.918 1.00 20.36  ? 447  SER B CA    1 
ATOM   7408 C  C     . SER B 1 461 ? 35.864  51.433 -15.496 1.00 20.14  ? 447  SER B C     1 
ATOM   7409 O  O     . SER B 1 461 ? 36.679  50.739 -16.123 1.00 21.59  ? 447  SER B O     1 
ATOM   7410 C  CB    . SER B 1 461 ? 33.425  51.032 -15.873 1.00 18.48  ? 447  SER B CB    1 
ATOM   7411 O  OG    . SER B 1 461 ? 32.258  50.368 -15.416 1.00 20.96  ? 447  SER B OG    1 
ATOM   7412 N  N     . MET B 1 462 ? 36.035  52.754 -15.331 1.00 20.41  ? 448  MET B N     1 
ATOM   7413 C  CA    . MET B 1 462 ? 37.274  53.364 -15.807 1.00 20.12  ? 448  MET B CA    1 
ATOM   7414 C  C     . MET B 1 462 ? 38.497  52.761 -15.137 1.00 21.13  ? 448  MET B C     1 
ATOM   7415 O  O     . MET B 1 462 ? 39.523  52.550 -15.798 1.00 21.57  ? 448  MET B O     1 
ATOM   7416 C  CB    . MET B 1 462 ? 37.295  54.902 -15.702 1.00 19.57  ? 448  MET B CB    1 
ATOM   7417 C  CG    . MET B 1 462 ? 36.026  55.719 -15.994 1.00 18.02  ? 448  MET B CG    1 
ATOM   7418 S  SD    . MET B 1 462 ? 36.035  57.344 -15.174 1.00 25.44  ? 448  MET B SD    1 
ATOM   7419 C  CE    . MET B 1 462 ? 35.190  58.394 -16.370 1.00 17.88  ? 448  MET B CE    1 
ATOM   7420 N  N     . LEU B 1 463 ? 38.430  52.514 -13.822 1.00 20.61  ? 449  LEU B N     1 
ATOM   7421 C  CA    . LEU B 1 463 ? 39.576  51.944 -13.121 1.00 20.45  ? 449  LEU B CA    1 
ATOM   7422 C  C     . LEU B 1 463 ? 39.825  50.504 -13.556 1.00 21.16  ? 449  LEU B C     1 
ATOM   7423 O  O     . LEU B 1 463 ? 40.973  50.116 -13.808 1.00 19.54  ? 449  LEU B O     1 
ATOM   7424 C  CB    . LEU B 1 463 ? 39.357  52.034 -11.613 1.00 20.72  ? 449  LEU B CB    1 
ATOM   7425 C  CG    . LEU B 1 463 ? 39.287  53.470 -11.091 1.00 20.33  ? 449  LEU B CG    1 
ATOM   7426 C  CD1   . LEU B 1 463 ? 38.653  53.525 -9.702  1.00 20.54  ? 449  LEU B CD1   1 
ATOM   7427 C  CD2   . LEU B 1 463 ? 40.684  54.107 -11.076 1.00 23.10  ? 449  LEU B CD2   1 
ATOM   7428 N  N     . ARG B 1 464 ? 38.757  49.707 -13.686 1.00 20.59  ? 450  ARG B N     1 
ATOM   7429 C  CA    . ARG B 1 464 ? 38.900  48.340 -14.191 1.00 22.94  ? 450  ARG B CA    1 
ATOM   7430 C  C     . ARG B 1 464 ? 39.617  48.305 -15.541 1.00 22.44  ? 450  ARG B C     1 
ATOM   7431 O  O     . ARG B 1 464 ? 40.485  47.458 -15.770 1.00 22.41  ? 450  ARG B O     1 
ATOM   7432 C  CB    . ARG B 1 464 ? 37.524  47.673 -14.301 1.00 22.36  ? 450  ARG B CB    1 
ATOM   7433 C  CG    . ARG B 1 464 ? 37.540  46.259 -14.877 1.00 23.21  ? 450  ARG B CG    1 
ATOM   7434 C  CD    . ARG B 1 464 ? 36.167  45.870 -15.417 1.00 24.09  ? 450  ARG B CD    1 
ATOM   7435 N  NE    . ARG B 1 464 ? 35.838  46.613 -16.624 1.00 20.85  ? 450  ARG B NE    1 
ATOM   7436 C  CZ    . ARG B 1 464 ? 34.601  46.842 -17.057 1.00 20.90  ? 450  ARG B CZ    1 
ATOM   7437 N  NH1   . ARG B 1 464 ? 33.540  46.394 -16.401 1.00 18.50  ? 450  ARG B NH1   1 
ATOM   7438 N  NH2   . ARG B 1 464 ? 34.424  47.563 -18.159 1.00 20.96  ? 450  ARG B NH2   1 
ATOM   7439 N  N     . ASP B 1 465 ? 39.256  49.206 -16.448 1.00 20.65  ? 451  ASP B N     1 
ATOM   7440 C  CA    . ASP B 1 465 ? 39.796  49.231 -17.802 1.00 23.08  ? 451  ASP B CA    1 
ATOM   7441 C  C     . ASP B 1 465 ? 41.083  50.044 -17.916 1.00 22.79  ? 451  ASP B C     1 
ATOM   7442 O  O     . ASP B 1 465 ? 41.561  50.260 -19.032 1.00 23.32  ? 451  ASP B O     1 
ATOM   7443 C  CB    . ASP B 1 465 ? 38.739  49.772 -18.787 1.00 22.52  ? 451  ASP B CB    1 
ATOM   7444 C  CG    . ASP B 1 465 ? 37.565  48.818 -18.967 1.00 23.87  ? 451  ASP B CG    1 
ATOM   7445 O  OD1   . ASP B 1 465 ? 37.702  47.639 -18.574 1.00 17.21  ? 451  ASP B OD1   1 
ATOM   7446 O  OD2   . ASP B 1 465 ? 36.509  49.247 -19.517 1.00 24.35  ? 451  ASP B OD2   1 
ATOM   7447 N  N     . LYS B 1 466 ? 41.636  50.506 -16.791 1.00 23.35  ? 452  LYS B N     1 
ATOM   7448 C  CA    . LYS B 1 466 ? 42.932  51.192 -16.739 1.00 24.66  ? 452  LYS B CA    1 
ATOM   7449 C  C     . LYS B 1 466 ? 42.914  52.489 -17.550 1.00 26.53  ? 452  LYS B C     1 
ATOM   7450 O  O     . LYS B 1 466 ? 43.902  52.845 -18.204 1.00 25.55  ? 452  LYS B O     1 
ATOM   7451 C  CB    . LYS B 1 466 ? 44.074  50.284 -17.224 1.00 25.73  ? 452  LYS B CB    1 
ATOM   7452 C  CG    . LYS B 1 466 ? 44.252  48.928 -16.531 1.00 25.03  ? 452  LYS B CG    1 
ATOM   7453 C  CD    . LYS B 1 466 ? 44.520  48.945 -15.016 1.00 31.11  ? 452  LYS B CD    1 
ATOM   7454 C  CE    . LYS B 1 466 ? 45.212  50.222 -14.504 1.00 36.71  ? 452  LYS B CE    1 
ATOM   7455 N  NZ    . LYS B 1 466 ? 45.518  50.169 -13.042 1.00 32.90  ? 452  LYS B NZ    1 
ATOM   7456 N  N     . GLN B 1 467 ? 41.789  53.203 -17.505 1.00 23.24  ? 453  GLN B N     1 
ATOM   7457 C  CA    . GLN B 1 467 ? 41.712  54.502 -18.152 1.00 23.23  ? 453  GLN B CA    1 
ATOM   7458 C  C     . GLN B 1 467 ? 42.335  55.582 -17.276 1.00 25.06  ? 453  GLN B C     1 
ATOM   7459 O  O     . GLN B 1 467 ? 42.409  55.469 -16.045 1.00 25.47  ? 453  GLN B O     1 
ATOM   7460 C  CB    . GLN B 1 467 ? 40.263  54.879 -18.470 1.00 22.23  ? 453  GLN B CB    1 
ATOM   7461 C  CG    . GLN B 1 467 ? 39.489  53.856 -19.258 1.00 22.19  ? 453  GLN B CG    1 
ATOM   7462 C  CD    . GLN B 1 467 ? 38.138  54.389 -19.724 1.00 20.96  ? 453  GLN B CD    1 
ATOM   7463 O  OE1   . GLN B 1 467 ? 37.509  55.211 -19.046 1.00 19.95  ? 453  GLN B OE1   1 
ATOM   7464 N  NE2   . GLN B 1 467 ? 37.680  53.912 -20.872 1.00 20.54  ? 453  GLN B NE2   1 
ATOM   7465 N  N     . HIS B 1 468 ? 42.761  56.665 -17.930 1.00 24.71  ? 454  HIS B N     1 
ATOM   7466 C  CA    . HIS B 1 468 ? 43.469  57.753 -17.251 1.00 24.29  ? 454  HIS B CA    1 
ATOM   7467 C  C     . HIS B 1 468 ? 42.825  59.108 -17.531 1.00 24.51  ? 454  HIS B C     1 
ATOM   7468 O  O     . HIS B 1 468 ? 43.513  60.056 -17.910 1.00 24.04  ? 454  HIS B O     1 
ATOM   7469 C  CB    . HIS B 1 468 ? 44.937  57.801 -17.671 1.00 24.15  ? 454  HIS B CB    1 
ATOM   7470 C  CG    . HIS B 1 468 ? 45.672  56.510 -17.524 1.00 26.25  ? 454  HIS B CG    1 
ATOM   7471 N  ND1   . HIS B 1 468 ? 46.674  56.122 -18.389 1.00 26.72  ? 454  HIS B ND1   1 
ATOM   7472 C  CD2   . HIS B 1 468 ? 45.581  55.534 -16.592 1.00 26.11  ? 454  HIS B CD2   1 
ATOM   7473 C  CE1   . HIS B 1 468 ? 47.153  54.954 -18.007 1.00 27.27  ? 454  HIS B CE1   1 
ATOM   7474 N  NE2   . HIS B 1 468 ? 46.512  54.580 -16.914 1.00 26.35  ? 454  HIS B NE2   1 
ATOM   7475 N  N     . PRO B 1 469 ? 41.508  59.247 -17.340 1.00 22.70  ? 455  PRO B N     1 
ATOM   7476 C  CA    . PRO B 1 469 ? 40.917  60.576 -17.459 1.00 21.37  ? 455  PRO B CA    1 
ATOM   7477 C  C     . PRO B 1 469 ? 41.389  61.460 -16.322 1.00 23.22  ? 455  PRO B C     1 
ATOM   7478 O  O     . PRO B 1 469 ? 41.917  60.998 -15.303 1.00 22.70  ? 455  PRO B O     1 
ATOM   7479 C  CB    . PRO B 1 469 ? 39.412  60.328 -17.355 1.00 22.47  ? 455  PRO B CB    1 
ATOM   7480 C  CG    . PRO B 1 469 ? 39.294  59.061 -16.619 1.00 21.43  ? 455  PRO B CG    1 
ATOM   7481 C  CD    . PRO B 1 469 ? 40.548  58.280 -16.783 1.00 21.15  ? 455  PRO B CD    1 
ATOM   7482 N  N     . ILE B 1 470 ? 41.190  62.755 -16.519 1.00 21.59  ? 456  ILE B N     1 
ATOM   7483 C  CA    . ILE B 1 470 ? 41.373  63.753 -15.480 1.00 21.68  ? 456  ILE B CA    1 
ATOM   7484 C  C     . ILE B 1 470 ? 39.974  64.215 -15.080 1.00 22.11  ? 456  ILE B C     1 
ATOM   7485 O  O     . ILE B 1 470 ? 39.317  64.960 -15.818 1.00 21.94  ? 456  ILE B O     1 
ATOM   7486 C  CB    . ILE B 1 470 ? 42.254  64.914 -15.961 1.00 22.49  ? 456  ILE B CB    1 
ATOM   7487 C  CG1   . ILE B 1 470 ? 43.630  64.381 -16.396 1.00 22.25  ? 456  ILE B CG1   1 
ATOM   7488 C  CG2   . ILE B 1 470 ? 42.416  65.960 -14.866 1.00 21.62  ? 456  ILE B CG2   1 
ATOM   7489 C  CD1   . ILE B 1 470 ? 44.316  65.238 -17.431 1.00 23.50  ? 456  ILE B CD1   1 
ATOM   7490 N  N     . ILE B 1 471 ? 39.512  63.762 -13.918 1.00 22.06  ? 457  ILE B N     1 
ATOM   7491 C  CA    . ILE B 1 471 ? 38.163  64.036 -13.427 1.00 21.95  ? 457  ILE B CA    1 
ATOM   7492 C  C     . ILE B 1 471 ? 38.241  65.180 -12.426 1.00 21.94  ? 457  ILE B C     1 
ATOM   7493 O  O     . ILE B 1 471 ? 38.866  65.048 -11.364 1.00 19.96  ? 457  ILE B O     1 
ATOM   7494 C  CB    . ILE B 1 471 ? 37.537  62.785 -12.790 1.00 21.40  ? 457  ILE B CB    1 
ATOM   7495 C  CG1   . ILE B 1 471 ? 37.568  61.601 -13.764 1.00 21.24  ? 457  ILE B CG1   1 
ATOM   7496 C  CG2   . ILE B 1 471 ? 36.118  63.067 -12.283 1.00 19.71  ? 457  ILE B CG2   1 
ATOM   7497 C  CD1   . ILE B 1 471 ? 37.160  60.248 -13.106 1.00 21.44  ? 457  ILE B CD1   1 
ATOM   7498 N  N     . LEU B 1 472 ? 37.619  66.308 -12.769 1.00 21.15  ? 458  LEU B N     1 
ATOM   7499 C  CA    . LEU B 1 472 ? 37.539  67.471 -11.890 1.00 22.43  ? 458  LEU B CA    1 
ATOM   7500 C  C     . LEU B 1 472 ? 36.126  67.538 -11.316 1.00 22.31  ? 458  LEU B C     1 
ATOM   7501 O  O     . LEU B 1 472 ? 35.158  67.780 -12.047 1.00 21.30  ? 458  LEU B O     1 
ATOM   7502 C  CB    . LEU B 1 472 ? 37.906  68.757 -12.630 1.00 19.60  ? 458  LEU B CB    1 
ATOM   7503 C  CG    . LEU B 1 472 ? 39.370  68.909 -13.069 1.00 23.26  ? 458  LEU B CG    1 
ATOM   7504 C  CD1   . LEU B 1 472 ? 39.500  68.789 -14.561 1.00 23.60  ? 458  LEU B CD1   1 
ATOM   7505 C  CD2   . LEU B 1 472 ? 39.962  70.241 -12.593 1.00 23.66  ? 458  LEU B CD2   1 
ATOM   7506 N  N     . VAL B 1 473 ? 36.003  67.279 -10.015 1.00 21.60  ? 459  VAL B N     1 
ATOM   7507 C  CA    . VAL B 1 473 ? 34.722  67.330 -9.323  1.00 21.45  ? 459  VAL B CA    1 
ATOM   7508 C  C     . VAL B 1 473 ? 34.590  68.703 -8.684  1.00 24.77  ? 459  VAL B C     1 
ATOM   7509 O  O     . VAL B 1 473 ? 35.303  69.026 -7.723  1.00 22.32  ? 459  VAL B O     1 
ATOM   7510 C  CB    . VAL B 1 473 ? 34.600  66.222 -8.271  1.00 22.08  ? 459  VAL B CB    1 
ATOM   7511 C  CG1   . VAL B 1 473 ? 33.299  66.381 -7.498  1.00 22.18  ? 459  VAL B CG1   1 
ATOM   7512 C  CG2   . VAL B 1 473 ? 34.676  64.862 -8.927  1.00 21.67  ? 459  VAL B CG2   1 
ATOM   7513 N  N     . LEU B 1 474 ? 33.655  69.503 -9.190  1.00 23.12  ? 460  LEU B N     1 
ATOM   7514 C  CA    . LEU B 1 474 ? 33.447  70.844 -8.657  1.00 23.85  ? 460  LEU B CA    1 
ATOM   7515 C  C     . LEU B 1 474 ? 32.604  70.705 -7.400  1.00 25.54  ? 460  LEU B C     1 
ATOM   7516 O  O     . LEU B 1 474 ? 31.390  70.497 -7.467  1.00 25.20  ? 460  LEU B O     1 
ATOM   7517 C  CB    . LEU B 1 474 ? 32.800  71.745 -9.702  1.00 22.89  ? 460  LEU B CB    1 
ATOM   7518 C  CG    . LEU B 1 474 ? 33.530  71.739 -11.053 1.00 22.68  ? 460  LEU B CG    1 
ATOM   7519 C  CD1   . LEU B 1 474 ? 33.057  72.885 -11.943 1.00 27.82  ? 460  LEU B CD1   1 
ATOM   7520 C  CD2   . LEU B 1 474 ? 35.039  71.813 -10.875 1.00 24.77  ? 460  LEU B CD2   1 
ATOM   7521 N  N     . ASN B 1 475 ? 33.258  70.766 -6.244  1.00 26.52  ? 461  ASN B N     1 
ATOM   7522 C  CA    . ASN B 1 475 ? 32.601  70.522 -4.966  1.00 27.94  ? 461  ASN B CA    1 
ATOM   7523 C  C     . ASN B 1 475 ? 32.259  71.867 -4.338  1.00 31.62  ? 461  ASN B C     1 
ATOM   7524 O  O     . ASN B 1 475 ? 33.112  72.524 -3.736  1.00 30.79  ? 461  ASN B O     1 
ATOM   7525 C  CB    . ASN B 1 475 ? 33.478  69.687 -4.042  1.00 27.48  ? 461  ASN B CB    1 
ATOM   7526 C  CG    . ASN B 1 475 ? 32.775  69.339 -2.736  1.00 30.23  ? 461  ASN B CG    1 
ATOM   7527 O  OD1   . ASN B 1 475 ? 31.646  69.777 -2.491  1.00 33.24  ? 461  ASN B OD1   1 
ATOM   7528 N  ND2   . ASN B 1 475 ? 33.442  68.567 -1.885  1.00 26.05  ? 461  ASN B ND2   1 
ATOM   7529 N  N     . ASN B 1 476 ? 30.994  72.255 -4.467  1.00 30.76  ? 462  ASN B N     1 
ATOM   7530 C  CA    . ASN B 1 476 ? 30.418  73.383 -3.749  1.00 35.68  ? 462  ASN B CA    1 
ATOM   7531 C  C     . ASN B 1 476 ? 29.349  72.936 -2.758  1.00 36.46  ? 462  ASN B C     1 
ATOM   7532 O  O     . ASN B 1 476 ? 28.561  73.765 -2.292  1.00 37.94  ? 462  ASN B O     1 
ATOM   7533 C  CB    . ASN B 1 476 ? 29.839  74.375 -4.760  1.00 36.14  ? 462  ASN B CB    1 
ATOM   7534 C  CG    . ASN B 1 476 ? 28.876  73.709 -5.737  1.00 36.54  ? 462  ASN B CG    1 
ATOM   7535 O  OD1   . ASN B 1 476 ? 28.159  72.772 -5.383  1.00 35.70  ? 462  ASN B OD1   1 
ATOM   7536 N  ND2   . ASN B 1 476 ? 28.877  74.175 -6.983  1.00 37.05  ? 462  ASN B ND2   1 
ATOM   7537 N  N     . GLU B 1 477 ? 29.299  71.632 -2.454  1.00 35.66  ? 463  GLU B N     1 
ATOM   7538 C  CA    . GLU B 1 477 ? 28.526  71.050 -1.350  1.00 39.47  ? 463  GLU B CA    1 
ATOM   7539 C  C     . GLU B 1 477 ? 27.005  71.143 -1.566  1.00 38.20  ? 463  GLU B C     1 
ATOM   7540 O  O     . GLU B 1 477 ? 26.252  71.500 -0.658  1.00 39.14  ? 463  GLU B O     1 
ATOM   7541 C  CB    . GLU B 1 477 ? 28.936  71.691 -0.023  1.00 40.61  ? 463  GLU B CB    1 
ATOM   7542 C  CG    . GLU B 1 477 ? 30.335  71.286 0.400   1.00 41.99  ? 463  GLU B CG    1 
ATOM   7543 C  CD    . GLU B 1 477 ? 30.527  71.287 1.897   1.00 51.64  ? 463  GLU B CD    1 
ATOM   7544 O  OE1   . GLU B 1 477 ? 29.794  72.023 2.600   1.00 50.32  ? 463  GLU B OE1   1 
ATOM   7545 O  OE2   . GLU B 1 477 ? 31.431  70.561 2.365   1.00 51.07  ? 463  GLU B OE2   1 
ATOM   7546 N  N     . GLY B 1 478 ? 26.553  70.768 -2.760  1.00 39.13  ? 464  GLY B N     1 
ATOM   7547 C  CA    . GLY B 1 478 ? 25.130  70.702 -3.047  1.00 39.11  ? 464  GLY B CA    1 
ATOM   7548 C  C     . GLY B 1 478 ? 24.826  71.040 -4.498  1.00 40.47  ? 464  GLY B C     1 
ATOM   7549 O  O     . GLY B 1 478 ? 25.721  71.144 -5.335  1.00 38.05  ? 464  GLY B O     1 
ATOM   7550 N  N     . TYR B 1 479 ? 23.525  71.220 -4.767  1.00 43.15  ? 465  TYR B N     1 
ATOM   7551 C  CA    . TYR B 1 479 ? 22.988  71.542 -6.098  1.00 44.35  ? 465  TYR B CA    1 
ATOM   7552 C  C     . TYR B 1 479 ? 23.002  73.062 -6.281  1.00 48.21  ? 465  TYR B C     1 
ATOM   7553 O  O     . TYR B 1 479 ? 21.978  73.739 -6.159  1.00 51.87  ? 465  TYR B O     1 
ATOM   7554 C  CB    . TYR B 1 479 ? 21.562  71.012 -6.232  1.00 43.35  ? 465  TYR B CB    1 
ATOM   7555 C  CG    . TYR B 1 479 ? 21.351  69.506 -6.177  1.00 41.71  ? 465  TYR B CG    1 
ATOM   7556 C  CD1   . TYR B 1 479 ? 22.339  68.616 -6.595  1.00 35.46  ? 465  TYR B CD1   1 
ATOM   7557 C  CD2   . TYR B 1 479 ? 20.143  68.977 -5.713  1.00 39.48  ? 465  TYR B CD2   1 
ATOM   7558 C  CE1   . TYR B 1 479 ? 22.124  67.243 -6.566  1.00 33.94  ? 465  TYR B CE1   1 
ATOM   7559 C  CE2   . TYR B 1 479 ? 19.926  67.606 -5.668  1.00 35.26  ? 465  TYR B CE2   1 
ATOM   7560 C  CZ    . TYR B 1 479 ? 20.916  66.745 -6.090  1.00 34.50  ? 465  TYR B CZ    1 
ATOM   7561 O  OH    . TYR B 1 479 ? 20.688  65.385 -6.041  1.00 32.10  ? 465  TYR B OH    1 
ATOM   7562 N  N     . THR B 1 480 ? 24.181  73.611 -6.599  1.00 46.39  ? 466  THR B N     1 
ATOM   7563 C  CA    . THR B 1 480 ? 24.323  75.071 -6.638  1.00 49.34  ? 466  THR B CA    1 
ATOM   7564 C  C     . THR B 1 480 ? 23.455  75.695 -7.722  1.00 54.99  ? 466  THR B C     1 
ATOM   7565 O  O     . THR B 1 480 ? 22.869  76.766 -7.521  1.00 55.48  ? 466  THR B O     1 
ATOM   7566 C  CB    . THR B 1 480 ? 25.788  75.460 -6.837  1.00 47.33  ? 466  THR B CB    1 
ATOM   7567 O  OG1   . THR B 1 480 ? 26.506  75.237 -5.619  1.00 53.72  ? 466  THR B OG1   1 
ATOM   7568 C  CG2   . THR B 1 480 ? 25.930  76.919 -7.265  1.00 54.21  ? 466  THR B CG2   1 
ATOM   7569 N  N     . VAL B 1 481 ? 23.382  75.050 -8.885  1.00 58.08  ? 467  VAL B N     1 
ATOM   7570 C  CA    . VAL B 1 481 ? 22.557  75.548 -9.981  1.00 54.94  ? 467  VAL B CA    1 
ATOM   7571 C  C     . VAL B 1 481 ? 21.100  75.675 -9.545  1.00 55.78  ? 467  VAL B C     1 
ATOM   7572 O  O     . VAL B 1 481 ? 20.430  76.664 -9.863  1.00 55.94  ? 467  VAL B O     1 
ATOM   7573 C  CB    . VAL B 1 481 ? 22.724  74.633 -11.202 1.00 48.51  ? 467  VAL B CB    1 
ATOM   7574 C  CG1   . VAL B 1 481 ? 22.612  73.219 -10.743 1.00 42.43  ? 467  VAL B CG1   1 
ATOM   7575 C  CG2   . VAL B 1 481 ? 21.681  74.943 -12.257 1.00 50.07  ? 467  VAL B CG2   1 
ATOM   7576 N  N     . GLU B 1 482 ? 20.585  74.678 -8.811  1.00 58.59  ? 468  GLU B N     1 
ATOM   7577 C  CA    . GLU B 1 482 ? 19.202  74.745 -8.344  1.00 55.61  ? 468  GLU B CA    1 
ATOM   7578 C  C     . GLU B 1 482 ? 19.038  75.829 -7.285  1.00 57.08  ? 468  GLU B C     1 
ATOM   7579 O  O     . GLU B 1 482 ? 17.957  76.419 -7.164  1.00 56.90  ? 468  GLU B O     1 
ATOM   7580 C  CB    . GLU B 1 482 ? 18.770  73.399 -7.759  1.00 50.26  ? 468  GLU B CB    1 
ATOM   7581 C  CG    . GLU B 1 482 ? 18.982  72.196 -8.658  1.00 43.31  ? 468  GLU B CG    1 
ATOM   7582 C  CD    . GLU B 1 482 ? 17.985  72.114 -9.787  1.00 39.01  ? 468  GLU B CD    1 
ATOM   7583 O  OE1   . GLU B 1 482 ? 18.135  72.854 -10.794 1.00 38.23  ? 468  GLU B OE1   1 
ATOM   7584 O  OE2   . GLU B 1 482 ? 17.039  71.310 -9.653  1.00 35.62  ? 468  GLU B OE2   1 
ATOM   7585 N  N     . ARG B 1 483 ? 20.099  76.098 -6.513  1.00 57.36  ? 469  ARG B N     1 
ATOM   7586 C  CA    . ARG B 1 483 ? 20.093  77.230 -5.590  1.00 59.98  ? 469  ARG B CA    1 
ATOM   7587 C  C     . ARG B 1 483 ? 19.892  78.535 -6.349  1.00 59.67  ? 469  ARG B C     1 
ATOM   7588 O  O     . ARG B 1 483 ? 19.149  79.416 -5.903  1.00 59.89  ? 469  ARG B O     1 
ATOM   7589 C  CB    . ARG B 1 483 ? 21.398  77.277 -4.785  1.00 57.72  ? 469  ARG B CB    1 
ATOM   7590 C  CG    . ARG B 1 483 ? 21.695  76.057 -3.905  1.00 55.84  ? 469  ARG B CG    1 
ATOM   7591 C  CD    . ARG B 1 483 ? 22.938  76.313 -3.046  1.00 56.46  ? 469  ARG B CD    1 
ATOM   7592 N  NE    . ARG B 1 483 ? 23.446  75.138 -2.337  1.00 51.76  ? 469  ARG B NE    1 
ATOM   7593 C  CZ    . ARG B 1 483 ? 22.843  74.514 -1.331  1.00 51.95  ? 469  ARG B CZ    1 
ATOM   7594 N  NH1   . ARG B 1 483 ? 21.686  74.935 -0.845  1.00 53.25  ? 469  ARG B NH1   1 
ATOM   7595 N  NH2   . ARG B 1 483 ? 23.419  73.436 -0.802  1.00 47.87  ? 469  ARG B NH2   1 
ATOM   7596 N  N     . ALA B 1 484 ? 20.578  78.683 -7.487  1.00 60.04  ? 470  ALA B N     1 
ATOM   7597 C  CA    . ALA B 1 484 ? 20.420  79.871 -8.320  1.00 62.76  ? 470  ALA B CA    1 
ATOM   7598 C  C     . ALA B 1 484 ? 18.981  80.034 -8.796  1.00 63.00  ? 470  ALA B C     1 
ATOM   7599 O  O     . ALA B 1 484 ? 18.446  81.149 -8.802  1.00 63.12  ? 470  ALA B O     1 
ATOM   7600 C  CB    . ALA B 1 484 ? 21.380  79.811 -9.510  1.00 64.03  ? 470  ALA B CB    1 
ATOM   7601 N  N     . ILE B 1 485 ? 18.338  78.939 -9.215  1.00 61.66  ? 471  ILE B N     1 
ATOM   7602 C  CA    . ILE B 1 485 ? 16.985  79.046 -9.759  1.00 61.84  ? 471  ILE B CA    1 
ATOM   7603 C  C     . ILE B 1 485 ? 15.981  79.335 -8.646  1.00 61.54  ? 471  ILE B C     1 
ATOM   7604 O  O     . ILE B 1 485 ? 15.205  80.296 -8.724  1.00 62.31  ? 471  ILE B O     1 
ATOM   7605 C  CB    . ILE B 1 485 ? 16.588  77.767 -10.532 1.00 60.03  ? 471  ILE B CB    1 
ATOM   7606 C  CG1   . ILE B 1 485 ? 17.242  77.637 -11.920 1.00 61.23  ? 471  ILE B CG1   1 
ATOM   7607 C  CG2   . ILE B 1 485 ? 15.082  77.697 -10.712 1.00 60.66  ? 471  ILE B CG2   1 
ATOM   7608 C  CD1   . ILE B 1 485 ? 18.711  77.856 -12.019 1.00 60.25  ? 471  ILE B CD1   1 
ATOM   7609 N  N     . HIS B 1 486 ? 15.993  78.531 -7.582  1.00 61.40  ? 472  HIS B N     1 
ATOM   7610 C  CA    . HIS B 1 486 ? 14.972  78.673 -6.552  1.00 60.85  ? 472  HIS B CA    1 
ATOM   7611 C  C     . HIS B 1 486 ? 15.427  78.043 -5.241  1.00 59.68  ? 472  HIS B C     1 
ATOM   7612 O  O     . HIS B 1 486 ? 15.997  76.946 -5.237  1.00 58.45  ? 472  HIS B O     1 
ATOM   7613 C  CB    . HIS B 1 486 ? 13.661  78.029 -7.010  1.00 58.09  ? 472  HIS B CB    1 
ATOM   7614 C  CG    . HIS B 1 486 ? 12.475  78.426 -6.193  1.00 57.60  ? 472  HIS B CG    1 
ATOM   7615 N  ND1   . HIS B 1 486 ? 11.982  79.713 -6.172  1.00 58.31  ? 472  HIS B ND1   1 
ATOM   7616 C  CD2   . HIS B 1 486 ? 11.690  77.707 -5.356  1.00 50.57  ? 472  HIS B CD2   1 
ATOM   7617 C  CE1   . HIS B 1 486 ? 10.937  79.769 -5.365  1.00 56.79  ? 472  HIS B CE1   1 
ATOM   7618 N  NE2   . HIS B 1 486 ? 10.738  78.565 -4.859  1.00 52.46  ? 472  HIS B NE2   1 
ATOM   7619 N  N     . GLY B 1 487 ? 15.168  78.743 -4.134  1.00 60.40  ? 473  GLY B N     1 
ATOM   7620 C  CA    . GLY B 1 487 ? 15.391  78.203 -2.812  1.00 59.43  ? 473  GLY B CA    1 
ATOM   7621 C  C     . GLY B 1 487 ? 16.843  77.891 -2.506  1.00 60.81  ? 473  GLY B C     1 
ATOM   7622 O  O     . GLY B 1 487 ? 17.221  76.729 -2.319  1.00 58.25  ? 473  GLY B O     1 
ATOM   7623 N  N     . PRO B 1 488 ? 17.690  78.922 -2.446  1.00 63.10  ? 474  PRO B N     1 
ATOM   7624 C  CA    . PRO B 1 488 ? 19.118  78.665 -2.192  1.00 63.21  ? 474  PRO B CA    1 
ATOM   7625 C  C     . PRO B 1 488 ? 19.386  78.047 -0.827  1.00 62.92  ? 474  PRO B C     1 
ATOM   7626 O  O     . PRO B 1 488 ? 20.340  77.270 -0.685  1.00 60.71  ? 474  PRO B O     1 
ATOM   7627 C  CB    . PRO B 1 488 ? 19.761  80.056 -2.327  1.00 64.40  ? 474  PRO B CB    1 
ATOM   7628 C  CG    . PRO B 1 488 ? 18.621  81.046 -2.499  1.00 63.45  ? 474  PRO B CG    1 
ATOM   7629 C  CD    . PRO B 1 488 ? 17.337  80.333 -2.223  1.00 63.49  ? 474  PRO B CD    1 
ATOM   7630 N  N     . GLU B 1 489 ? 18.565  78.357 0.176   1.00 66.02  ? 475  GLU B N     1 
ATOM   7631 C  CA    . GLU B 1 489 ? 18.712  77.810 1.518   1.00 66.62  ? 475  GLU B CA    1 
ATOM   7632 C  C     . GLU B 1 489 ? 17.853  76.575 1.755   1.00 62.62  ? 475  GLU B C     1 
ATOM   7633 O  O     . GLU B 1 489 ? 17.832  76.058 2.879   1.00 65.76  ? 475  GLU B O     1 
ATOM   7634 C  CB    . GLU B 1 489 ? 18.370  78.873 2.569   1.00 70.45  ? 475  GLU B CB    1 
ATOM   7635 C  CG    . GLU B 1 489 ? 19.289  80.084 2.563   1.00 76.50  ? 475  GLU B CG    1 
ATOM   7636 C  CD    . GLU B 1 489 ? 18.751  81.227 3.406   1.00 88.64  ? 475  GLU B CD    1 
ATOM   7637 O  OE1   . GLU B 1 489 ? 19.046  81.265 4.621   1.00 87.32  ? 475  GLU B OE1   1 
ATOM   7638 O  OE2   . GLU B 1 489 ? 18.024  82.082 2.857   1.00 97.87  ? 475  GLU B OE2   1 
ATOM   7639 N  N     . GLN B 1 490 ? 17.147  76.090 0.738   1.00 58.33  ? 476  GLN B N     1 
ATOM   7640 C  CA    . GLN B 1 490 ? 16.242  74.968 0.925   1.00 54.47  ? 476  GLN B CA    1 
ATOM   7641 C  C     . GLN B 1 490 ? 17.018  73.658 0.953   1.00 51.75  ? 476  GLN B C     1 
ATOM   7642 O  O     . GLN B 1 490 ? 17.921  73.432 0.140   1.00 48.90  ? 476  GLN B O     1 
ATOM   7643 C  CB    . GLN B 1 490 ? 15.200  74.937 -0.192  1.00 49.84  ? 476  GLN B CB    1 
ATOM   7644 C  CG    . GLN B 1 490 ? 14.067  75.951 -0.058  1.00 50.12  ? 476  GLN B CG    1 
ATOM   7645 C  CD    . GLN B 1 490 ? 13.139  75.708 1.131   1.00 48.35  ? 476  GLN B CD    1 
ATOM   7646 O  OE1   . GLN B 1 490 ? 13.554  75.231 2.186   1.00 51.75  ? 476  GLN B OE1   1 
ATOM   7647 N  NE2   . GLN B 1 490 ? 11.865  76.032 0.948   1.00 43.24  ? 476  GLN B NE2   1 
ATOM   7648 N  N     . ARG B 1 491 ? 16.645  72.782 1.889   1.00 50.11  ? 477  ARG B N     1 
ATOM   7649 C  CA    . ARG B 1 491 ? 17.396  71.548 2.092   1.00 51.68  ? 477  ARG B CA    1 
ATOM   7650 C  C     . ARG B 1 491 ? 17.277  70.573 0.919   1.00 49.17  ? 477  ARG B C     1 
ATOM   7651 O  O     . ARG B 1 491 ? 18.097  69.652 0.820   1.00 48.37  ? 477  ARG B O     1 
ATOM   7652 C  CB    . ARG B 1 491 ? 16.990  70.903 3.424   1.00 52.48  ? 477  ARG B CB    1 
ATOM   7653 C  CG    . ARG B 1 491 ? 15.559  70.431 3.529   1.00 57.26  ? 477  ARG B CG    1 
ATOM   7654 C  CD    . ARG B 1 491 ? 15.397  69.382 4.629   1.00 54.07  ? 477  ARG B CD    1 
ATOM   7655 N  NE    . ARG B 1 491 ? 15.619  68.047 4.091   1.00 55.96  ? 477  ARG B NE    1 
ATOM   7656 C  CZ    . ARG B 1 491 ? 14.711  67.081 4.054   1.00 41.48  ? 477  ARG B CZ    1 
ATOM   7657 N  NH1   . ARG B 1 491 ? 13.515  67.228 4.609   1.00 37.69  ? 477  ARG B NH1   1 
ATOM   7658 N  NH2   . ARG B 1 491 ? 15.011  65.939 3.443   1.00 35.89  ? 477  ARG B NH2   1 
ATOM   7659 N  N     . TYR B 1 492 ? 16.285  70.734 0.034   1.00 45.67  ? 478  TYR B N     1 
ATOM   7660 C  CA    . TYR B 1 492 ? 16.219  69.845 -1.127  1.00 44.10  ? 478  TYR B CA    1 
ATOM   7661 C  C     . TYR B 1 492 ? 17.364  70.076 -2.106  1.00 43.99  ? 478  TYR B C     1 
ATOM   7662 O  O     . TYR B 1 492 ? 17.618  69.216 -2.958  1.00 41.09  ? 478  TYR B O     1 
ATOM   7663 C  CB    . TYR B 1 492 ? 14.884  69.982 -1.865  1.00 38.02  ? 478  TYR B CB    1 
ATOM   7664 C  CG    . TYR B 1 492 ? 14.457  71.384 -2.277  1.00 41.79  ? 478  TYR B CG    1 
ATOM   7665 C  CD1   . TYR B 1 492 ? 15.115  72.084 -3.291  1.00 40.13  ? 478  TYR B CD1   1 
ATOM   7666 C  CD2   . TYR B 1 492 ? 13.348  71.979 -1.687  1.00 39.24  ? 478  TYR B CD2   1 
ATOM   7667 C  CE1   . TYR B 1 492 ? 14.693  73.358 -3.678  1.00 41.95  ? 478  TYR B CE1   1 
ATOM   7668 C  CE2   . TYR B 1 492 ? 12.917  73.239 -2.069  1.00 40.07  ? 478  TYR B CE2   1 
ATOM   7669 C  CZ    . TYR B 1 492 ? 13.589  73.927 -3.061  1.00 42.23  ? 478  TYR B CZ    1 
ATOM   7670 O  OH    . TYR B 1 492 ? 13.136  75.185 -3.414  1.00 41.79  ? 478  TYR B OH    1 
ATOM   7671 N  N     . ASN B 1 493 ? 18.067  71.201 -1.994  1.00 45.21  ? 479  ASN B N     1 
ATOM   7672 C  CA    . ASN B 1 493 ? 19.256  71.462 -2.793  1.00 48.90  ? 479  ASN B CA    1 
ATOM   7673 C  C     . ASN B 1 493 ? 20.524  70.922 -2.139  1.00 48.00  ? 479  ASN B C     1 
ATOM   7674 O  O     . ASN B 1 493 ? 21.607  71.024 -2.727  1.00 46.65  ? 479  ASN B O     1 
ATOM   7675 C  CB    . ASN B 1 493 ? 19.378  72.968 -3.047  1.00 49.58  ? 479  ASN B CB    1 
ATOM   7676 C  CG    . ASN B 1 493 ? 18.420  73.441 -4.123  1.00 52.36  ? 479  ASN B CG    1 
ATOM   7677 O  OD1   . ASN B 1 493 ? 17.926  72.635 -4.911  1.00 48.47  ? 479  ASN B OD1   1 
ATOM   7678 N  ND2   . ASN B 1 493 ? 18.114  74.736 -4.131  1.00 54.03  ? 479  ASN B ND2   1 
ATOM   7679 N  N     . ASP B 1 494 ? 20.409  70.337 -0.950  1.00 47.25  ? 480  ASP B N     1 
ATOM   7680 C  CA    . ASP B 1 494 ? 21.530  69.666 -0.313  1.00 45.86  ? 480  ASP B CA    1 
ATOM   7681 C  C     . ASP B 1 494 ? 21.657  68.228 -0.815  1.00 42.42  ? 480  ASP B C     1 
ATOM   7682 O  O     . ASP B 1 494 ? 20.710  67.634 -1.342  1.00 42.95  ? 480  ASP B O     1 
ATOM   7683 C  CB    . ASP B 1 494 ? 21.362  69.683 1.205   1.00 46.98  ? 480  ASP B CB    1 
ATOM   7684 C  CG    . ASP B 1 494 ? 21.325  71.086 1.764   1.00 48.43  ? 480  ASP B CG    1 
ATOM   7685 O  OD1   . ASP B 1 494 ? 21.924  71.987 1.133   1.00 49.03  ? 480  ASP B OD1   1 
ATOM   7686 O  OD2   . ASP B 1 494 ? 20.681  71.290 2.815   1.00 49.16  ? 480  ASP B OD2   1 
ATOM   7687 N  N     . ILE B 1 495 ? 22.863  67.678 -0.668  1.00 41.22  ? 481  ILE B N     1 
ATOM   7688 C  CA    . ILE B 1 495 ? 23.155  66.297 -1.024  1.00 35.33  ? 481  ILE B CA    1 
ATOM   7689 C  C     . ILE B 1 495 ? 23.927  65.659 0.124   1.00 31.54  ? 481  ILE B C     1 
ATOM   7690 O  O     . ILE B 1 495 ? 24.406  66.337 1.032   1.00 31.11  ? 481  ILE B O     1 
ATOM   7691 C  CB    . ILE B 1 495 ? 23.966  66.167 -2.326  1.00 32.35  ? 481  ILE B CB    1 
ATOM   7692 C  CG1   . ILE B 1 495 ? 25.285  66.924 -2.220  1.00 33.59  ? 481  ILE B CG1   1 
ATOM   7693 C  CG2   . ILE B 1 495 ? 23.173  66.710 -3.480  1.00 36.79  ? 481  ILE B CG2   1 
ATOM   7694 C  CD1   . ILE B 1 495 ? 25.986  67.128 -3.560  1.00 31.30  ? 481  ILE B CD1   1 
ATOM   7695 N  N     . ALA B 1 496 ? 24.044  64.335 0.070   1.00 27.67  ? 482  ALA B N     1 
ATOM   7696 C  CA    . ALA B 1 496 ? 25.031  63.666 0.905   1.00 27.57  ? 482  ALA B CA    1 
ATOM   7697 C  C     . ALA B 1 496 ? 26.417  64.178 0.545   1.00 27.65  ? 482  ALA B C     1 
ATOM   7698 O  O     . ALA B 1 496 ? 26.751  64.336 -0.639  1.00 26.06  ? 482  ALA B O     1 
ATOM   7699 C  CB    . ALA B 1 496 ? 24.969  62.154 0.726   1.00 24.48  ? 482  ALA B CB    1 
ATOM   7700 N  N     . LEU B 1 497 ? 27.224  64.438 1.570   1.00 24.60  ? 483  LEU B N     1 
ATOM   7701 C  CA    . LEU B 1 497 ? 28.576  64.948 1.378   1.00 26.18  ? 483  LEU B CA    1 
ATOM   7702 C  C     . LEU B 1 497 ? 29.531  63.767 1.311   1.00 26.12  ? 483  LEU B C     1 
ATOM   7703 O  O     . LEU B 1 497 ? 29.756  63.075 2.311   1.00 26.60  ? 483  LEU B O     1 
ATOM   7704 C  CB    . LEU B 1 497 ? 28.964  65.907 2.501   1.00 26.98  ? 483  LEU B CB    1 
ATOM   7705 C  CG    . LEU B 1 497 ? 28.052  67.127 2.591   1.00 31.45  ? 483  LEU B CG    1 
ATOM   7706 C  CD1   . LEU B 1 497 ? 28.384  67.971 3.815   1.00 36.34  ? 483  LEU B CD1   1 
ATOM   7707 C  CD2   . LEU B 1 497 ? 28.140  67.940 1.308   1.00 33.10  ? 483  LEU B CD2   1 
ATOM   7708 N  N     . TRP B 1 498 ? 30.109  63.552 0.139   1.00 24.50  ? 484  TRP B N     1 
ATOM   7709 C  CA    . TRP B 1 498 ? 30.974  62.410 -0.096  1.00 23.90  ? 484  TRP B CA    1 
ATOM   7710 C  C     . TRP B 1 498 ? 32.428  62.790 0.132   1.00 26.09  ? 484  TRP B C     1 
ATOM   7711 O  O     . TRP B 1 498 ? 32.790  63.969 0.145   1.00 24.31  ? 484  TRP B O     1 
ATOM   7712 C  CB    . TRP B 1 498 ? 30.808  61.892 -1.522  1.00 23.67  ? 484  TRP B CB    1 
ATOM   7713 C  CG    . TRP B 1 498 ? 29.530  61.159 -1.756  1.00 24.18  ? 484  TRP B CG    1 
ATOM   7714 C  CD1   . TRP B 1 498 ? 28.500  60.962 -0.866  1.00 24.93  ? 484  TRP B CD1   1 
ATOM   7715 C  CD2   . TRP B 1 498 ? 29.132  60.531 -2.977  1.00 23.42  ? 484  TRP B CD2   1 
ATOM   7716 N  NE1   . TRP B 1 498 ? 27.489  60.234 -1.470  1.00 22.74  ? 484  TRP B NE1   1 
ATOM   7717 C  CE2   . TRP B 1 498 ? 27.855  59.962 -2.764  1.00 20.27  ? 484  TRP B CE2   1 
ATOM   7718 C  CE3   . TRP B 1 498 ? 29.735  60.390 -4.231  1.00 22.52  ? 484  TRP B CE3   1 
ATOM   7719 C  CZ2   . TRP B 1 498 ? 27.175  59.262 -3.762  1.00 22.90  ? 484  TRP B CZ2   1 
ATOM   7720 C  CZ3   . TRP B 1 498 ? 29.047  59.690 -5.232  1.00 20.29  ? 484  TRP B CZ3   1 
ATOM   7721 C  CH2   . TRP B 1 498 ? 27.788  59.139 -4.986  1.00 20.15  ? 484  TRP B CH2   1 
ATOM   7722 N  N     . ASN B 1 499 ? 33.253  61.759 0.345   1.00 22.98  ? 485  ASN B N     1 
ATOM   7723 C  CA    . ASN B 1 499 ? 34.702  61.893 0.487   1.00 25.10  ? 485  ASN B CA    1 
ATOM   7724 C  C     . ASN B 1 499 ? 35.326  61.521 -0.857  1.00 23.73  ? 485  ASN B C     1 
ATOM   7725 O  O     . ASN B 1 499 ? 35.824  60.415 -1.063  1.00 22.67  ? 485  ASN B O     1 
ATOM   7726 C  CB    . ASN B 1 499 ? 35.203  61.017 1.632   1.00 24.55  ? 485  ASN B CB    1 
ATOM   7727 C  CG    . ASN B 1 499 ? 36.567  61.439 2.136   1.00 24.17  ? 485  ASN B CG    1 
ATOM   7728 O  OD1   . ASN B 1 499 ? 37.201  62.327 1.572   1.00 25.07  ? 485  ASN B OD1   1 
ATOM   7729 N  ND2   . ASN B 1 499 ? 37.016  60.817 3.217   1.00 26.62  ? 485  ASN B ND2   1 
ATOM   7730 N  N     . TRP B 1 500 ? 35.285  62.484 -1.781  1.00 23.17  ? 486  TRP B N     1 
ATOM   7731 C  CA    . TRP B 1 500 ? 35.575  62.223 -3.191  1.00 23.66  ? 486  TRP B CA    1 
ATOM   7732 C  C     . TRP B 1 500 ? 36.938  61.568 -3.404  1.00 24.55  ? 486  TRP B C     1 
ATOM   7733 O  O     . TRP B 1 500 ? 37.057  60.620 -4.192  1.00 21.46  ? 486  TRP B O     1 
ATOM   7734 C  CB    . TRP B 1 500 ? 35.471  63.532 -3.979  1.00 23.12  ? 486  TRP B CB    1 
ATOM   7735 C  CG    . TRP B 1 500 ? 34.066  64.025 -4.027  1.00 23.20  ? 486  TRP B CG    1 
ATOM   7736 C  CD1   . TRP B 1 500 ? 33.512  64.981 -3.236  1.00 23.68  ? 486  TRP B CD1   1 
ATOM   7737 C  CD2   . TRP B 1 500 ? 33.015  63.546 -4.877  1.00 24.70  ? 486  TRP B CD2   1 
ATOM   7738 N  NE1   . TRP B 1 500 ? 32.184  65.146 -3.545  1.00 24.06  ? 486  TRP B NE1   1 
ATOM   7739 C  CE2   . TRP B 1 500 ? 31.850  64.273 -4.548  1.00 24.24  ? 486  TRP B CE2   1 
ATOM   7740 C  CE3   . TRP B 1 500 ? 32.947  62.585 -5.891  1.00 22.35  ? 486  TRP B CE3   1 
ATOM   7741 C  CZ2   . TRP B 1 500 ? 30.635  64.074 -5.203  1.00 22.60  ? 486  TRP B CZ2   1 
ATOM   7742 C  CZ3   . TRP B 1 500 ? 31.734  62.389 -6.540  1.00 23.07  ? 486  TRP B CZ3   1 
ATOM   7743 C  CH2   . TRP B 1 500 ? 30.595  63.126 -6.188  1.00 22.24  ? 486  TRP B CH2   1 
ATOM   7744 N  N     . THR B 1 501 ? 37.975  62.042 -2.706  1.00 24.27  ? 487  THR B N     1 
ATOM   7745 C  CA    . THR B 1 501 ? 39.316  61.527 -2.974  1.00 25.59  ? 487  THR B CA    1 
ATOM   7746 C  C     . THR B 1 501 ? 39.500  60.088 -2.517  1.00 25.34  ? 487  THR B C     1 
ATOM   7747 O  O     . THR B 1 501 ? 40.508  59.469 -2.873  1.00 27.08  ? 487  THR B O     1 
ATOM   7748 C  CB    . THR B 1 501 ? 40.377  62.411 -2.300  1.00 26.18  ? 487  THR B CB    1 
ATOM   7749 O  OG1   . THR B 1 501 ? 40.181  62.384 -0.883  1.00 24.69  ? 487  THR B OG1   1 
ATOM   7750 C  CG2   . THR B 1 501 ? 40.282  63.854 -2.785  1.00 25.20  ? 487  THR B CG2   1 
ATOM   7751 N  N     . GLN B 1 502 ? 38.543  59.528 -1.779  1.00 24.61  ? 488  GLN B N     1 
ATOM   7752 C  CA    . GLN B 1 502 ? 38.609  58.144 -1.331  1.00 25.52  ? 488  GLN B CA    1 
ATOM   7753 C  C     . GLN B 1 502 ? 37.780  57.199 -2.186  1.00 25.20  ? 488  GLN B C     1 
ATOM   7754 O  O     . GLN B 1 502 ? 37.796  55.991 -1.944  1.00 25.34  ? 488  GLN B O     1 
ATOM   7755 C  CB    . GLN B 1 502 ? 38.152  58.042 0.129   1.00 25.74  ? 488  GLN B CB    1 
ATOM   7756 C  CG    . GLN B 1 502 ? 38.891  58.996 1.073   1.00 27.65  ? 488  GLN B CG    1 
ATOM   7757 C  CD    . GLN B 1 502 ? 40.400  58.832 1.014   1.00 32.20  ? 488  GLN B CD    1 
ATOM   7758 O  OE1   . GLN B 1 502 ? 40.906  57.711 1.041   1.00 34.17  ? 488  GLN B OE1   1 
ATOM   7759 N  NE2   . GLN B 1 502 ? 41.132  59.955 0.923   1.00 29.99  ? 488  GLN B NE2   1 
ATOM   7760 N  N     . ILE B 1 503 ? 37.043  57.709 -3.166  1.00 23.94  ? 489  ILE B N     1 
ATOM   7761 C  CA    . ILE B 1 503 ? 36.164  56.847 -3.949  1.00 22.86  ? 489  ILE B CA    1 
ATOM   7762 C  C     . ILE B 1 503 ? 36.950  55.866 -4.818  1.00 22.43  ? 489  ILE B C     1 
ATOM   7763 O  O     . ILE B 1 503 ? 36.616  54.675 -4.814  1.00 23.44  ? 489  ILE B O     1 
ATOM   7764 C  CB    . ILE B 1 503 ? 35.186  57.692 -4.772  1.00 22.38  ? 489  ILE B CB    1 
ATOM   7765 C  CG1   . ILE B 1 503 ? 34.331  58.511 -3.790  1.00 22.33  ? 489  ILE B CG1   1 
ATOM   7766 C  CG2   . ILE B 1 503 ? 34.356  56.791 -5.652  1.00 21.40  ? 489  ILE B CG2   1 
ATOM   7767 C  CD1   . ILE B 1 503 ? 33.294  59.427 -4.414  1.00 21.48  ? 489  ILE B CD1   1 
ATOM   7768 N  N     . PRO B 1 504 ? 38.002  56.273 -5.555  1.00 25.67  ? 490  PRO B N     1 
ATOM   7769 C  CA    . PRO B 1 504 ? 38.720  55.267 -6.361  1.00 23.94  ? 490  PRO B CA    1 
ATOM   7770 C  C     . PRO B 1 504 ? 39.219  54.078 -5.553  1.00 25.22  ? 490  PRO B C     1 
ATOM   7771 O  O     . PRO B 1 504 ? 39.120  52.937 -6.023  1.00 26.10  ? 490  PRO B O     1 
ATOM   7772 C  CB    . PRO B 1 504 ? 39.877  56.074 -6.970  1.00 23.93  ? 490  PRO B CB    1 
ATOM   7773 C  CG    . PRO B 1 504 ? 39.348  57.472 -7.024  1.00 23.41  ? 490  PRO B CG    1 
ATOM   7774 C  CD    . PRO B 1 504 ? 38.598  57.614 -5.738  1.00 23.25  ? 490  PRO B CD    1 
ATOM   7775 N  N     . GLN B 1 505 ? 39.719  54.292 -4.333  1.00 25.62  ? 491  GLN B N     1 
ATOM   7776 C  CA    . GLN B 1 505 ? 40.172  53.152 -3.544  1.00 26.12  ? 491  GLN B CA    1 
ATOM   7777 C  C     . GLN B 1 505 ? 39.022  52.330 -2.972  1.00 26.79  ? 491  GLN B C     1 
ATOM   7778 O  O     . GLN B 1 505 ? 39.261  51.217 -2.491  1.00 28.51  ? 491  GLN B O     1 
ATOM   7779 C  CB    . GLN B 1 505 ? 41.132  53.618 -2.429  1.00 31.50  ? 491  GLN B CB    1 
ATOM   7780 C  CG    . GLN B 1 505 ? 40.527  54.555 -1.398  1.00 31.49  ? 491  GLN B CG    1 
ATOM   7781 C  CD    . GLN B 1 505 ? 39.986  53.839 -0.174  1.00 38.75  ? 491  GLN B CD    1 
ATOM   7782 O  OE1   . GLN B 1 505 ? 40.489  52.786 0.231   1.00 40.85  ? 491  GLN B OE1   1 
ATOM   7783 N  NE2   . GLN B 1 505 ? 38.917  54.388 0.397   1.00 34.64  ? 491  GLN B NE2   1 
ATOM   7784 N  N     . ALA B 1 506 ? 37.790  52.831 -3.011  1.00 25.51  ? 492  ALA B N     1 
ATOM   7785 C  CA    . ALA B 1 506 ? 36.650  51.987 -2.675  1.00 26.56  ? 492  ALA B CA    1 
ATOM   7786 C  C     . ALA B 1 506 ? 36.146  51.180 -3.870  1.00 24.68  ? 492  ALA B C     1 
ATOM   7787 O  O     . ALA B 1 506 ? 35.661  50.054 -3.687  1.00 22.99  ? 492  ALA B O     1 
ATOM   7788 C  CB    . ALA B 1 506 ? 35.510  52.834 -2.097  1.00 24.12  ? 492  ALA B CB    1 
ATOM   7789 N  N     . LEU B 1 507 ? 36.238  51.729 -5.084  1.00 24.81  ? 493  LEU B N     1 
ATOM   7790 C  CA    . LEU B 1 507 ? 35.711  51.088 -6.285  1.00 23.81  ? 493  LEU B CA    1 
ATOM   7791 C  C     . LEU B 1 507 ? 36.776  50.295 -7.041  1.00 24.80  ? 493  LEU B C     1 
ATOM   7792 O  O     . LEU B 1 507 ? 36.559  49.914 -8.199  1.00 23.73  ? 493  LEU B O     1 
ATOM   7793 C  CB    . LEU B 1 507 ? 35.055  52.130 -7.194  1.00 21.53  ? 493  LEU B CB    1 
ATOM   7794 C  CG    . LEU B 1 507 ? 33.938  52.949 -6.515  1.00 23.17  ? 493  LEU B CG    1 
ATOM   7795 C  CD1   . LEU B 1 507 ? 33.225  53.884 -7.483  1.00 22.11  ? 493  LEU B CD1   1 
ATOM   7796 C  CD2   . LEU B 1 507 ? 32.935  52.058 -5.808  1.00 21.10  ? 493  LEU B CD2   1 
ATOM   7797 N  N     . SER B 1 508 ? 37.910  50.018 -6.395  1.00 26.42  ? 494  SER B N     1 
ATOM   7798 C  CA    . SER B 1 508 ? 38.975  49.227 -6.988  1.00 25.57  ? 494  SER B CA    1 
ATOM   7799 C  C     . SER B 1 508 ? 39.832  48.653 -5.871  1.00 28.07  ? 494  SER B C     1 
ATOM   7800 O  O     . SER B 1 508 ? 40.011  49.283 -4.829  1.00 28.40  ? 494  SER B O     1 
ATOM   7801 C  CB    . SER B 1 508 ? 39.836  50.066 -7.936  1.00 28.11  ? 494  SER B CB    1 
ATOM   7802 O  OG    . SER B 1 508 ? 40.749  49.253 -8.662  1.00 29.87  ? 494  SER B OG    1 
ATOM   7803 N  N     . LEU B 1 509 ? 40.337  47.441 -6.088  1.00 27.08  ? 495  LEU B N     1 
ATOM   7804 C  CA    . LEU B 1 509 ? 41.310  46.857 -5.178  1.00 29.34  ? 495  LEU B CA    1 
ATOM   7805 C  C     . LEU B 1 509 ? 42.717  47.392 -5.434  1.00 29.84  ? 495  LEU B C     1 
ATOM   7806 O  O     . LEU B 1 509 ? 43.564  47.344 -4.539  1.00 28.75  ? 495  LEU B O     1 
ATOM   7807 C  CB    . LEU B 1 509 ? 41.273  45.334 -5.306  1.00 29.10  ? 495  LEU B CB    1 
ATOM   7808 C  CG    . LEU B 1 509 ? 39.926  44.731 -4.888  1.00 30.88  ? 495  LEU B CG    1 
ATOM   7809 C  CD1   . LEU B 1 509 ? 39.909  43.206 -5.059  1.00 28.90  ? 495  LEU B CD1   1 
ATOM   7810 C  CD2   . LEU B 1 509 ? 39.636  45.098 -3.433  1.00 31.35  ? 495  LEU B CD2   1 
ATOM   7811 N  N     . ASP B 1 510 ? 42.960  47.937 -6.626  1.00 29.34  ? 496  ASP B N     1 
ATOM   7812 C  CA    . ASP B 1 510 ? 44.274  48.450 -7.018  1.00 30.80  ? 496  ASP B CA    1 
ATOM   7813 C  C     . ASP B 1 510 ? 44.038  49.616 -7.968  1.00 29.33  ? 496  ASP B C     1 
ATOM   7814 O  O     . ASP B 1 510 ? 44.297  49.528 -9.171  1.00 30.22  ? 496  ASP B O     1 
ATOM   7815 C  CB    . ASP B 1 510 ? 45.104  47.343 -7.677  1.00 30.88  ? 496  ASP B CB    1 
ATOM   7816 C  CG    . ASP B 1 510 ? 46.554  47.735 -7.891  1.00 35.05  ? 496  ASP B CG    1 
ATOM   7817 O  OD1   . ASP B 1 510 ? 47.028  48.682 -7.222  1.00 33.72  ? 496  ASP B OD1   1 
ATOM   7818 O  OD2   . ASP B 1 510 ? 47.205  47.109 -8.756  1.00 33.76  ? 496  ASP B OD2   1 
ATOM   7819 N  N     . PRO B 1 511 ? 43.517  50.734 -7.450  1.00 29.37  ? 497  PRO B N     1 
ATOM   7820 C  CA    . PRO B 1 511 ? 43.093  51.828 -8.341  1.00 27.49  ? 497  PRO B CA    1 
ATOM   7821 C  C     . PRO B 1 511 ? 44.217  52.489 -9.112  1.00 29.71  ? 497  PRO B C     1 
ATOM   7822 O  O     . PRO B 1 511 ? 44.054  52.782 -10.303 1.00 29.44  ? 497  PRO B O     1 
ATOM   7823 C  CB    . PRO B 1 511 ? 42.435  52.839 -7.387  1.00 27.00  ? 497  PRO B CB    1 
ATOM   7824 C  CG    . PRO B 1 511 ? 42.548  52.294 -6.023  1.00 29.59  ? 497  PRO B CG    1 
ATOM   7825 C  CD    . PRO B 1 511 ? 43.405  51.078 -6.022  1.00 30.38  ? 497  PRO B CD    1 
ATOM   7826 N  N     . GLN B 1 512 ? 45.351  52.747 -8.468  1.00 32.98  ? 498  GLN B N     1 
ATOM   7827 C  CA    . GLN B 1 512 ? 46.437  53.464 -9.115  1.00 35.07  ? 498  GLN B CA    1 
ATOM   7828 C  C     . GLN B 1 512 ? 45.924  54.810 -9.619  1.00 30.60  ? 498  GLN B C     1 
ATOM   7829 O  O     . GLN B 1 512 ? 46.109  55.209 -10.769 1.00 31.64  ? 498  GLN B O     1 
ATOM   7830 C  CB    . GLN B 1 512 ? 47.033  52.596 -10.230 1.00 37.67  ? 498  GLN B CB    1 
ATOM   7831 C  CG    . GLN B 1 512 ? 47.663  51.323 -9.677  1.00 40.16  ? 498  GLN B CG    1 
ATOM   7832 C  CD    . GLN B 1 512 ? 48.958  51.653 -8.972  1.00 51.35  ? 498  GLN B CD    1 
ATOM   7833 O  OE1   . GLN B 1 512 ? 49.183  51.323 -7.802  1.00 70.64  ? 498  GLN B OE1   1 
ATOM   7834 N  NE2   . GLN B 1 512 ? 49.840  52.295 -9.715  1.00 58.90  ? 498  GLN B NE2   1 
ATOM   7835 N  N     . ALA B 1 513 ? 45.384  55.566 -8.678  1.00 28.30  ? 499  ALA B N     1 
ATOM   7836 C  CA    . ALA B 1 513 ? 44.738  56.821 -8.995  1.00 28.11  ? 499  ALA B CA    1 
ATOM   7837 C  C     . ALA B 1 513 ? 45.488  57.894 -8.235  1.00 27.32  ? 499  ALA B C     1 
ATOM   7838 O  O     . ALA B 1 513 ? 46.027  57.653 -7.154  1.00 29.99  ? 499  ALA B O     1 
ATOM   7839 C  CB    . ALA B 1 513 ? 43.233  56.821 -8.625  1.00 25.33  ? 499  ALA B CB    1 
ATOM   7840 N  N     . GLN B 1 514 ? 45.513  59.084 -8.796  1.00 25.59  ? 500  GLN B N     1 
ATOM   7841 C  CA    . GLN B 1 514 ? 46.124  60.208 -8.121  1.00 24.97  ? 500  GLN B CA    1 
ATOM   7842 C  C     . GLN B 1 514 ? 45.002  61.162 -7.770  1.00 26.02  ? 500  GLN B C     1 
ATOM   7843 O  O     . GLN B 1 514 ? 44.304  61.662 -8.657  1.00 22.32  ? 500  GLN B O     1 
ATOM   7844 C  CB    . GLN B 1 514 ? 47.167  60.854 -9.033  1.00 24.47  ? 500  GLN B CB    1 
ATOM   7845 C  CG    . GLN B 1 514 ? 48.162  59.843 -9.629  1.00 26.45  ? 500  GLN B CG    1 
ATOM   7846 C  CD    . GLN B 1 514 ? 49.282  60.498 -10.447 1.00 24.67  ? 500  GLN B CD    1 
ATOM   7847 O  OE1   . GLN B 1 514 ? 49.122  61.606 -10.964 1.00 27.05  ? 500  GLN B OE1   1 
ATOM   7848 N  NE2   . GLN B 1 514 ? 50.423  59.814 -10.556 1.00 27.92  ? 500  GLN B NE2   1 
ATOM   7849 N  N     . CYS B 1 515 ? 44.841  61.423 -6.481  1.00 24.77  ? 501  CYS B N     1 
ATOM   7850 C  CA    . CYS B 1 515 ? 43.732  62.228 -6.011  1.00 24.59  ? 501  CYS B CA    1 
ATOM   7851 C  C     . CYS B 1 515 ? 44.275  63.430 -5.266  1.00 25.33  ? 501  CYS B C     1 
ATOM   7852 O  O     . CYS B 1 515 ? 45.290  63.341 -4.575  1.00 23.57  ? 501  CYS B O     1 
ATOM   7853 C  CB    . CYS B 1 515 ? 42.785  61.404 -5.111  1.00 25.86  ? 501  CYS B CB    1 
ATOM   7854 S  SG    . CYS B 1 515 ? 41.998  59.989 -5.934  1.00 28.14  ? 501  CYS B SG    1 
ATOM   7855 N  N     . TRP B 1 516 ? 43.619  64.562 -5.448  1.00 23.71  ? 502  TRP B N     1 
ATOM   7856 C  CA    . TRP B 1 516 ? 43.954  65.760 -4.705  1.00 24.92  ? 502  TRP B CA    1 
ATOM   7857 C  C     . TRP B 1 516 ? 42.654  66.447 -4.335  1.00 27.20  ? 502  TRP B C     1 
ATOM   7858 O  O     . TRP B 1 516 ? 41.658  66.363 -5.062  1.00 24.71  ? 502  TRP B O     1 
ATOM   7859 C  CB    . TRP B 1 516 ? 44.780  66.772 -5.507  1.00 23.53  ? 502  TRP B CB    1 
ATOM   7860 C  CG    . TRP B 1 516 ? 46.202  66.432 -5.886  1.00 24.47  ? 502  TRP B CG    1 
ATOM   7861 C  CD1   . TRP B 1 516 ? 47.353  66.876 -5.288  1.00 26.56  ? 502  TRP B CD1   1 
ATOM   7862 C  CD2   . TRP B 1 516 ? 46.609  65.644 -7.006  1.00 25.09  ? 502  TRP B CD2   1 
ATOM   7863 N  NE1   . TRP B 1 516 ? 48.455  66.392 -5.963  1.00 25.18  ? 502  TRP B NE1   1 
ATOM   7864 C  CE2   . TRP B 1 516 ? 48.019  65.633 -7.022  1.00 26.27  ? 502  TRP B CE2   1 
ATOM   7865 C  CE3   . TRP B 1 516 ? 45.910  64.946 -8.002  1.00 24.05  ? 502  TRP B CE3   1 
ATOM   7866 C  CZ2   . TRP B 1 516 ? 48.748  64.941 -7.990  1.00 27.01  ? 502  TRP B CZ2   1 
ATOM   7867 C  CZ3   . TRP B 1 516 ? 46.625  64.262 -8.952  1.00 23.35  ? 502  TRP B CZ3   1 
ATOM   7868 C  CH2   . TRP B 1 516 ? 48.035  64.267 -8.945  1.00 24.46  ? 502  TRP B CH2   1 
ATOM   7869 N  N     . ARG B 1 517 ? 42.694  67.155 -3.220  1.00 27.38  ? 503  ARG B N     1 
ATOM   7870 C  CA    . ARG B 1 517 ? 41.693  68.144 -2.864  1.00 28.00  ? 503  ARG B CA    1 
ATOM   7871 C  C     . ARG B 1 517 ? 42.395  69.494 -2.887  1.00 26.46  ? 503  ARG B C     1 
ATOM   7872 O  O     . ARG B 1 517 ? 43.419  69.669 -2.228  1.00 24.93  ? 503  ARG B O     1 
ATOM   7873 C  CB    . ARG B 1 517 ? 41.108  67.842 -1.488  1.00 31.20  ? 503  ARG B CB    1 
ATOM   7874 C  CG    . ARG B 1 517 ? 39.971  68.740 -1.080  1.00 34.59  ? 503  ARG B CG    1 
ATOM   7875 C  CD    . ARG B 1 517 ? 39.188  68.081 0.036   1.00 39.42  ? 503  ARG B CD    1 
ATOM   7876 N  NE    . ARG B 1 517 ? 39.541  68.612 1.343   1.00 47.97  ? 503  ARG B NE    1 
ATOM   7877 C  CZ    . ARG B 1 517 ? 38.655  69.057 2.222   1.00 58.61  ? 503  ARG B CZ    1 
ATOM   7878 N  NH1   . ARG B 1 517 ? 37.359  69.067 1.948   1.00 58.93  ? 503  ARG B NH1   1 
ATOM   7879 N  NH2   . ARG B 1 517 ? 39.078  69.511 3.400   1.00 57.02  ? 503  ARG B NH2   1 
ATOM   7880 N  N     . VAL B 1 518 ? 41.874  70.436 -3.661  1.00 28.24  ? 504  VAL B N     1 
ATOM   7881 C  CA    . VAL B 1 518 ? 42.523  71.734 -3.814  1.00 29.22  ? 504  VAL B CA    1 
ATOM   7882 C  C     . VAL B 1 518 ? 41.516  72.819 -3.470  1.00 30.05  ? 504  VAL B C     1 
ATOM   7883 O  O     . VAL B 1 518 ? 40.322  72.689 -3.765  1.00 29.63  ? 504  VAL B O     1 
ATOM   7884 C  CB    . VAL B 1 518 ? 43.099  71.927 -5.237  1.00 29.25  ? 504  VAL B CB    1 
ATOM   7885 C  CG1   . VAL B 1 518 ? 44.204  70.901 -5.500  1.00 27.07  ? 504  VAL B CG1   1 
ATOM   7886 C  CG2   . VAL B 1 518 ? 42.003  71.810 -6.301  1.00 26.15  ? 504  VAL B CG2   1 
ATOM   7887 N  N     . SER B 1 519 ? 41.999  73.876 -2.817  1.00 30.75  ? 505  SER B N     1 
ATOM   7888 C  CA    . SER B 1 519 ? 41.185  75.033 -2.480  1.00 31.64  ? 505  SER B CA    1 
ATOM   7889 C  C     . SER B 1 519 ? 41.780  76.339 -2.973  1.00 34.12  ? 505  SER B C     1 
ATOM   7890 O  O     . SER B 1 519 ? 41.128  77.381 -2.850  1.00 33.27  ? 505  SER B O     1 
ATOM   7891 C  CB    . SER B 1 519 ? 40.998  75.133 -0.960  1.00 33.00  ? 505  SER B CB    1 
ATOM   7892 O  OG    . SER B 1 519 ? 42.261  75.164 -0.314  1.00 35.63  ? 505  SER B OG    1 
ATOM   7893 N  N     . GLU B 1 520 ? 42.983  76.315 -3.531  1.00 34.91  ? 506  GLU B N     1 
ATOM   7894 C  CA    . GLU B 1 520 ? 43.686  77.508 -3.961  1.00 35.11  ? 506  GLU B CA    1 
ATOM   7895 C  C     . GLU B 1 520 ? 44.012  77.380 -5.438  1.00 35.89  ? 506  GLU B C     1 
ATOM   7896 O  O     . GLU B 1 520 ? 44.278  76.280 -5.934  1.00 34.00  ? 506  GLU B O     1 
ATOM   7897 C  CB    . GLU B 1 520 ? 44.990  77.707 -3.169  1.00 36.50  ? 506  GLU B CB    1 
ATOM   7898 C  CG    . GLU B 1 520 ? 44.880  77.498 -1.667  1.00 36.03  ? 506  GLU B CG    1 
ATOM   7899 C  CD    . GLU B 1 520 ? 43.857  78.398 -1.015  1.00 38.49  ? 506  GLU B CD    1 
ATOM   7900 O  OE1   . GLU B 1 520 ? 43.916  79.624 -1.236  1.00 41.27  ? 506  GLU B OE1   1 
ATOM   7901 O  OE2   . GLU B 1 520 ? 42.989  77.880 -0.280  1.00 39.88  ? 506  GLU B OE2   1 
ATOM   7902 N  N     . ALA B 1 521 ? 43.991  78.519 -6.131  1.00 36.04  ? 507  ALA B N     1 
ATOM   7903 C  CA    . ALA B 1 521 ? 44.339  78.537 -7.544  1.00 36.09  ? 507  ALA B CA    1 
ATOM   7904 C  C     . ALA B 1 521 ? 45.741  77.977 -7.780  1.00 36.23  ? 507  ALA B C     1 
ATOM   7905 O  O     . ALA B 1 521 ? 45.968  77.247 -8.755  1.00 33.97  ? 507  ALA B O     1 
ATOM   7906 C  CB    . ALA B 1 521 ? 44.222  79.960 -8.086  1.00 38.74  ? 507  ALA B CB    1 
ATOM   7907 N  N     . GLU B 1 522 ? 46.692  78.297 -6.896  1.00 36.49  ? 508  GLU B N     1 
ATOM   7908 C  CA    . GLU B 1 522 ? 48.065  77.834 -7.096  1.00 37.38  ? 508  GLU B CA    1 
ATOM   7909 C  C     . GLU B 1 522 ? 48.158  76.324 -6.965  1.00 35.38  ? 508  GLU B C     1 
ATOM   7910 O  O     . GLU B 1 522 ? 48.863  75.676 -7.749  1.00 34.10  ? 508  GLU B O     1 
ATOM   7911 C  CB    . GLU B 1 522 ? 49.022  78.484 -6.091  1.00 36.85  ? 508  GLU B CB    1 
ATOM   7912 C  CG    . GLU B 1 522 ? 48.656  79.886 -5.742  1.00 45.57  ? 508  GLU B CG    1 
ATOM   7913 C  CD    . GLU B 1 522 ? 47.650  79.937 -4.615  1.00 44.37  ? 508  GLU B CD    1 
ATOM   7914 O  OE1   . GLU B 1 522 ? 46.561  80.493 -4.852  1.00 44.99  ? 508  GLU B OE1   1 
ATOM   7915 O  OE2   . GLU B 1 522 ? 47.960  79.465 -3.495  1.00 42.76  ? 508  GLU B OE2   1 
ATOM   7916 N  N     . GLN B 1 523 ? 47.451  75.743 -5.988  1.00 31.99  ? 509  GLN B N     1 
ATOM   7917 C  CA    . GLN B 1 523 ? 47.431  74.290 -5.872  1.00 31.94  ? 509  GLN B CA    1 
ATOM   7918 C  C     . GLN B 1 523 ? 46.862  73.654 -7.131  1.00 30.84  ? 509  GLN B C     1 
ATOM   7919 O  O     . GLN B 1 523 ? 47.368  72.624 -7.588  1.00 28.71  ? 509  GLN B O     1 
ATOM   7920 C  CB    . GLN B 1 523 ? 46.607  73.836 -4.669  1.00 31.91  ? 509  GLN B CB    1 
ATOM   7921 C  CG    . GLN B 1 523 ? 46.889  74.523 -3.365  1.00 36.55  ? 509  GLN B CG    1 
ATOM   7922 C  CD    . GLN B 1 523 ? 45.865  74.130 -2.319  1.00 35.75  ? 509  GLN B CD    1 
ATOM   7923 O  OE1   . GLN B 1 523 ? 44.665  74.084 -2.602  1.00 33.93  ? 509  GLN B OE1   1 
ATOM   7924 N  NE2   . GLN B 1 523 ? 46.325  73.882 -1.097  1.00 34.66  ? 509  GLN B NE2   1 
ATOM   7925 N  N     . LEU B 1 524 ? 45.772  74.223 -7.671  1.00 29.25  ? 510  LEU B N     1 
ATOM   7926 C  CA    . LEU B 1 524 ? 45.164  73.674 -8.880  1.00 28.80  ? 510  LEU B CA    1 
ATOM   7927 C  C     . LEU B 1 524 ? 46.119  73.759 -10.067 1.00 29.26  ? 510  LEU B C     1 
ATOM   7928 O  O     . LEU B 1 524 ? 46.259  72.801 -10.838 1.00 26.95  ? 510  LEU B O     1 
ATOM   7929 C  CB    . LEU B 1 524 ? 43.846  74.397 -9.193  1.00 27.81  ? 510  LEU B CB    1 
ATOM   7930 C  CG    . LEU B 1 524 ? 43.153  73.953 -10.490 1.00 29.20  ? 510  LEU B CG    1 
ATOM   7931 C  CD1   . LEU B 1 524 ? 42.838  72.453 -10.474 1.00 24.74  ? 510  LEU B CD1   1 
ATOM   7932 C  CD2   . LEU B 1 524 ? 41.888  74.753 -10.791 1.00 26.67  ? 510  LEU B CD2   1 
ATOM   7933 N  N     . ALA B 1 525 ? 46.780  74.910 -10.239 1.00 30.94  ? 511  ALA B N     1 
ATOM   7934 C  CA    . ALA B 1 525 ? 47.745  75.046 -11.325 1.00 30.73  ? 511  ALA B CA    1 
ATOM   7935 C  C     . ALA B 1 525 ? 48.843  73.997 -11.209 1.00 31.04  ? 511  ALA B C     1 
ATOM   7936 O  O     . ALA B 1 525 ? 49.193  73.339 -12.198 1.00 29.62  ? 511  ALA B O     1 
ATOM   7937 C  CB    . ALA B 1 525 ? 48.339  76.454 -11.324 1.00 31.29  ? 511  ALA B CB    1 
ATOM   7938 N  N     . ASP B 1 526 ? 49.359  73.799 -9.993  1.00 30.38  ? 512  ASP B N     1 
ATOM   7939 C  CA    . ASP B 1 526 ? 50.422  72.826 -9.762  1.00 32.14  ? 512  ASP B CA    1 
ATOM   7940 C  C     . ASP B 1 526 ? 49.938  71.412 -10.057 1.00 30.39  ? 512  ASP B C     1 
ATOM   7941 O  O     . ASP B 1 526 ? 50.595  70.662 -10.783 1.00 30.91  ? 512  ASP B O     1 
ATOM   7942 C  CB    . ASP B 1 526 ? 50.910  72.950 -8.314  1.00 33.55  ? 512  ASP B CB    1 
ATOM   7943 C  CG    . ASP B 1 526 ? 51.864  71.839 -7.911  1.00 35.69  ? 512  ASP B CG    1 
ATOM   7944 O  OD1   . ASP B 1 526 ? 52.969  71.762 -8.498  1.00 36.68  ? 512  ASP B OD1   1 
ATOM   7945 O  OD2   . ASP B 1 526 ? 51.508  71.051 -7.000  1.00 37.61  ? 512  ASP B OD2   1 
ATOM   7946 N  N     . VAL B 1 527 ? 48.764  71.047 -9.536  1.00 27.29  ? 513  VAL B N     1 
ATOM   7947 C  CA    . VAL B 1 527 ? 48.200  69.723 -9.789  1.00 27.68  ? 513  VAL B CA    1 
ATOM   7948 C  C     . VAL B 1 527 ? 47.980  69.507 -11.280 1.00 27.62  ? 513  VAL B C     1 
ATOM   7949 O  O     . VAL B 1 527 ? 48.244  68.422 -11.814 1.00 26.00  ? 513  VAL B O     1 
ATOM   7950 C  CB    . VAL B 1 527 ? 46.887  69.546 -9.007  1.00 26.86  ? 513  VAL B CB    1 
ATOM   7951 C  CG1   . VAL B 1 527 ? 46.153  68.303 -9.490  1.00 24.43  ? 513  VAL B CG1   1 
ATOM   7952 C  CG2   . VAL B 1 527 ? 47.166  69.473 -7.522  1.00 28.15  ? 513  VAL B CG2   1 
ATOM   7953 N  N     . LEU B 1 528 ? 47.452  70.519 -11.968 1.00 26.16  ? 514  LEU B N     1 
ATOM   7954 C  CA    . LEU B 1 528 ? 47.208  70.384 -13.398 1.00 27.49  ? 514  LEU B CA    1 
ATOM   7955 C  C     . LEU B 1 528 ? 48.508  70.115 -14.155 1.00 28.55  ? 514  LEU B C     1 
ATOM   7956 O  O     . LEU B 1 528 ? 48.536  69.284 -15.070 1.00 26.94  ? 514  LEU B O     1 
ATOM   7957 C  CB    . LEU B 1 528 ? 46.495  71.629 -13.917 1.00 25.92  ? 514  LEU B CB    1 
ATOM   7958 C  CG    . LEU B 1 528 ? 45.014  71.622 -13.498 1.00 26.35  ? 514  LEU B CG    1 
ATOM   7959 C  CD1   . LEU B 1 528 ? 44.302  72.934 -13.841 1.00 26.71  ? 514  LEU B CD1   1 
ATOM   7960 C  CD2   . LEU B 1 528 ? 44.308  70.442 -14.143 1.00 25.84  ? 514  LEU B CD2   1 
ATOM   7961 N  N     . GLU B 1 529 ? 49.600  70.792 -13.777 1.00 29.20  ? 515  GLU B N     1 
ATOM   7962 C  CA    . GLU B 1 529 ? 50.902  70.463 -14.359 1.00 30.47  ? 515  GLU B CA    1 
ATOM   7963 C  C     . GLU B 1 529 ? 51.275  69.000 -14.118 1.00 28.33  ? 515  GLU B C     1 
ATOM   7964 O  O     . GLU B 1 529 ? 51.755  68.324 -15.034 1.00 27.68  ? 515  GLU B O     1 
ATOM   7965 C  CB    . GLU B 1 529 ? 51.988  71.380 -13.803 1.00 36.00  ? 515  GLU B CB    1 
ATOM   7966 C  CG    . GLU B 1 529 ? 51.822  72.847 -14.145 1.00 43.65  ? 515  GLU B CG    1 
ATOM   7967 C  CD    . GLU B 1 529 ? 52.890  73.718 -13.496 1.00 59.45  ? 515  GLU B CD    1 
ATOM   7968 O  OE1   . GLU B 1 529 ? 52.783  74.963 -13.579 1.00 56.50  ? 515  GLU B OE1   1 
ATOM   7969 O  OE2   . GLU B 1 529 ? 53.840  73.155 -12.907 1.00 56.87  ? 515  GLU B OE2   1 
ATOM   7970 N  N     . LYS B 1 530 ? 51.041  68.490 -12.898 1.00 29.06  ? 516  LYS B N     1 
ATOM   7971 C  CA    . LYS B 1 530 ? 51.398  67.104 -12.566 1.00 28.65  ? 516  LYS B CA    1 
ATOM   7972 C  C     . LYS B 1 530 ? 50.604  66.073 -13.366 1.00 27.81  ? 516  LYS B C     1 
ATOM   7973 O  O     . LYS B 1 530 ? 51.121  64.988 -13.652 1.00 28.38  ? 516  LYS B O     1 
ATOM   7974 C  CB    . LYS B 1 530 ? 51.232  66.841 -11.072 1.00 28.43  ? 516  LYS B CB    1 
ATOM   7975 C  CG    . LYS B 1 530 ? 51.684  67.977 -10.180 1.00 31.88  ? 516  LYS B CG    1 
ATOM   7976 C  CD    . LYS B 1 530 ? 52.577  67.485 -9.084  1.00 33.24  ? 516  LYS B CD    1 
ATOM   7977 C  CE    . LYS B 1 530 ? 53.233  68.633 -8.341  1.00 33.83  ? 516  LYS B CE    1 
ATOM   7978 N  NZ    . LYS B 1 530 ? 53.374  68.340 -6.897  1.00 32.54  ? 516  LYS B NZ    1 
ATOM   7979 N  N     . VAL B 1 531 ? 49.324  66.326 -13.644 1.00 27.12  ? 517  VAL B N     1 
ATOM   7980 C  CA    . VAL B 1 531 ? 48.516  65.332 -14.346 1.00 25.23  ? 517  VAL B CA    1 
ATOM   7981 C  C     . VAL B 1 531 ? 48.454  65.601 -15.849 1.00 26.16  ? 517  VAL B C     1 
ATOM   7982 O  O     . VAL B 1 531 ? 47.745  64.899 -16.568 1.00 25.27  ? 517  VAL B O     1 
ATOM   7983 C  CB    . VAL B 1 531 ? 47.097  65.231 -13.759 1.00 27.24  ? 517  VAL B CB    1 
ATOM   7984 C  CG1   . VAL B 1 531 ? 47.144  64.939 -12.263 1.00 25.25  ? 517  VAL B CG1   1 
ATOM   7985 C  CG2   . VAL B 1 531 ? 46.305  66.512 -14.038 1.00 23.58  ? 517  VAL B CG2   1 
ATOM   7986 N  N     . ALA B 1 532 ? 49.238  66.557 -16.345 1.00 27.59  ? 518  ALA B N     1 
ATOM   7987 C  CA    . ALA B 1 532 ? 49.116  66.981 -17.737 1.00 27.77  ? 518  ALA B CA    1 
ATOM   7988 C  C     . ALA B 1 532 ? 49.251  65.824 -18.721 1.00 27.13  ? 518  ALA B C     1 
ATOM   7989 O  O     . ALA B 1 532 ? 48.626  65.848 -19.788 1.00 28.34  ? 518  ALA B O     1 
ATOM   7990 C  CB    . ALA B 1 532 ? 50.155  68.062 -18.048 1.00 26.21  ? 518  ALA B CB    1 
ATOM   7991 N  N     . HIS B 1 533 ? 50.074  64.821 -18.406 1.00 28.59  ? 519  HIS B N     1 
ATOM   7992 C  CA    . HIS B 1 533 ? 50.319  63.709 -19.318 1.00 28.80  ? 519  HIS B CA    1 
ATOM   7993 C  C     . HIS B 1 533 ? 49.514  62.466 -18.966 1.00 28.32  ? 519  HIS B C     1 
ATOM   7994 O  O     . HIS B 1 533 ? 49.736  61.406 -19.568 1.00 26.63  ? 519  HIS B O     1 
ATOM   7995 C  CB    . HIS B 1 533 ? 51.815  63.377 -19.350 1.00 31.30  ? 519  HIS B CB    1 
ATOM   7996 C  CG    . HIS B 1 533 ? 52.673  64.539 -19.740 1.00 32.76  ? 519  HIS B CG    1 
ATOM   7997 N  ND1   . HIS B 1 533 ? 52.894  64.895 -21.054 1.00 35.84  ? 519  HIS B ND1   1 
ATOM   7998 C  CD2   . HIS B 1 533 ? 53.375  65.420 -18.988 1.00 32.67  ? 519  HIS B CD2   1 
ATOM   7999 C  CE1   . HIS B 1 533 ? 53.679  65.957 -21.093 1.00 35.05  ? 519  HIS B CE1   1 
ATOM   8000 N  NE2   . HIS B 1 533 ? 53.989  66.292 -19.853 1.00 32.56  ? 519  HIS B NE2   1 
ATOM   8001 N  N     . HIS B 1 534 ? 48.584  62.583 -18.011 1.00 26.60  ? 520  HIS B N     1 
ATOM   8002 C  CA    . HIS B 1 534 ? 47.548  61.593 -17.724 1.00 26.64  ? 520  HIS B CA    1 
ATOM   8003 C  C     . HIS B 1 534 ? 48.075  60.155 -17.776 1.00 26.77  ? 520  HIS B C     1 
ATOM   8004 O  O     . HIS B 1 534 ? 47.541  59.283 -18.460 1.00 26.40  ? 520  HIS B O     1 
ATOM   8005 C  CB    . HIS B 1 534 ? 46.348  61.796 -18.663 1.00 25.63  ? 520  HIS B CB    1 
ATOM   8006 C  CG    . HIS B 1 534 ? 46.688  61.690 -20.116 1.00 26.25  ? 520  HIS B CG    1 
ATOM   8007 N  ND1   . HIS B 1 534 ? 46.676  60.493 -20.798 1.00 27.41  ? 520  HIS B ND1   1 
ATOM   8008 C  CD2   . HIS B 1 534 ? 47.095  62.625 -21.007 1.00 25.86  ? 520  HIS B CD2   1 
ATOM   8009 C  CE1   . HIS B 1 534 ? 47.035  60.698 -22.054 1.00 26.17  ? 520  HIS B CE1   1 
ATOM   8010 N  NE2   . HIS B 1 534 ? 47.297  61.983 -22.205 1.00 27.03  ? 520  HIS B NE2   1 
ATOM   8011 N  N     . GLU B 1 535 ? 49.130  59.901 -17.004 1.00 27.34  ? 521  GLU B N     1 
ATOM   8012 C  CA    . GLU B 1 535 ? 49.693  58.560 -16.900 1.00 29.45  ? 521  GLU B CA    1 
ATOM   8013 C  C     . GLU B 1 535 ? 48.902  57.672 -15.954 1.00 26.85  ? 521  GLU B C     1 
ATOM   8014 O  O     . GLU B 1 535 ? 49.113  56.452 -15.941 1.00 25.03  ? 521  GLU B O     1 
ATOM   8015 C  CB    . GLU B 1 535 ? 51.158  58.640 -16.453 1.00 29.80  ? 521  GLU B CB    1 
ATOM   8016 C  CG    . GLU B 1 535 ? 51.990  59.591 -17.314 1.00 30.97  ? 521  GLU B CG    1 
ATOM   8017 C  CD    . GLU B 1 535 ? 53.475  59.409 -17.102 1.00 39.08  ? 521  GLU B CD    1 
ATOM   8018 O  OE1   . GLU B 1 535 ? 53.882  58.298 -16.697 1.00 38.82  ? 521  GLU B OE1   1 
ATOM   8019 O  OE2   . GLU B 1 535 ? 54.228  60.382 -17.331 1.00 48.69  ? 521  GLU B OE2   1 
ATOM   8020 N  N     . ARG B 1 536 ? 48.027  58.263 -15.146 1.00 27.81  ? 522  ARG B N     1 
ATOM   8021 C  CA    . ARG B 1 536 ? 47.143  57.531 -14.259 1.00 25.78  ? 522  ARG B CA    1 
ATOM   8022 C  C     . ARG B 1 536 ? 45.794  58.220 -14.311 1.00 26.26  ? 522  ARG B C     1 
ATOM   8023 O  O     . ARG B 1 536 ? 45.685  59.356 -14.782 1.00 26.16  ? 522  ARG B O     1 
ATOM   8024 C  CB    . ARG B 1 536 ? 47.660  57.503 -12.815 1.00 26.03  ? 522  ARG B CB    1 
ATOM   8025 C  CG    . ARG B 1 536 ? 49.068  56.982 -12.709 1.00 28.28  ? 522  ARG B CG    1 
ATOM   8026 C  CD    . ARG B 1 536 ? 49.147  55.456 -12.674 1.00 32.79  ? 522  ARG B CD    1 
ATOM   8027 N  NE    . ARG B 1 536 ? 50.534  55.019 -12.525 1.00 35.28  ? 522  ARG B NE    1 
ATOM   8028 C  CZ    . ARG B 1 536 ? 51.427  55.026 -13.507 1.00 37.40  ? 522  ARG B CZ    1 
ATOM   8029 N  NH1   . ARG B 1 536 ? 51.115  55.455 -14.721 1.00 34.99  ? 522  ARG B NH1   1 
ATOM   8030 N  NH2   . ARG B 1 536 ? 52.683  54.663 -13.248 1.00 38.31  ? 522  ARG B NH2   1 
ATOM   8031 N  N     . LEU B 1 537 ? 44.757  57.526 -13.845 1.00 24.69  ? 523  LEU B N     1 
ATOM   8032 C  CA    . LEU B 1 537 ? 43.502  58.213 -13.579 1.00 23.05  ? 523  LEU B CA    1 
ATOM   8033 C  C     . LEU B 1 537 ? 43.737  59.228 -12.467 1.00 25.45  ? 523  LEU B C     1 
ATOM   8034 O  O     . LEU B 1 537 ? 44.433  58.949 -11.488 1.00 21.51  ? 523  LEU B O     1 
ATOM   8035 C  CB    . LEU B 1 537 ? 42.407  57.219 -13.175 1.00 23.10  ? 523  LEU B CB    1 
ATOM   8036 C  CG    . LEU B 1 537 ? 41.008  57.803 -12.920 1.00 21.34  ? 523  LEU B CG    1 
ATOM   8037 C  CD1   . LEU B 1 537 ? 39.912  56.850 -13.410 1.00 20.25  ? 523  LEU B CD1   1 
ATOM   8038 C  CD2   . LEU B 1 537 ? 40.787  58.157 -11.444 1.00 20.65  ? 523  LEU B CD2   1 
ATOM   8039 N  N     . SER B 1 538 ? 43.193  60.425 -12.632 1.00 23.49  ? 524  SER B N     1 
ATOM   8040 C  CA    . SER B 1 538 ? 43.308  61.440 -11.598 1.00 23.54  ? 524  SER B CA    1 
ATOM   8041 C  C     . SER B 1 538 ? 41.919  61.944 -11.231 1.00 23.52  ? 524  SER B C     1 
ATOM   8042 O  O     . SER B 1 538 ? 41.016  61.981 -12.078 1.00 21.94  ? 524  SER B O     1 
ATOM   8043 C  CB    . SER B 1 538 ? 44.237  62.596 -12.022 1.00 22.54  ? 524  SER B CB    1 
ATOM   8044 O  OG    . SER B 1 538 ? 43.767  63.234 -13.185 1.00 26.40  ? 524  SER B OG    1 
ATOM   8045 N  N     . LEU B 1 539 ? 41.715  62.204 -9.937  1.00 22.00  ? 525  LEU B N     1 
ATOM   8046 C  CA    . LEU B 1 539 ? 40.486  62.831 -9.459  1.00 22.56  ? 525  LEU B CA    1 
ATOM   8047 C  C     . LEU B 1 539 ? 40.862  64.055 -8.637  1.00 22.68  ? 525  LEU B C     1 
ATOM   8048 O  O     . LEU B 1 539 ? 41.565  63.934 -7.630  1.00 22.32  ? 525  LEU B O     1 
ATOM   8049 C  CB    . LEU B 1 539 ? 39.632  61.849 -8.644  1.00 21.30  ? 525  LEU B CB    1 
ATOM   8050 C  CG    . LEU B 1 539 ? 38.197  62.294 -8.312  1.00 21.06  ? 525  LEU B CG    1 
ATOM   8051 C  CD1   . LEU B 1 539 ? 37.308  61.069 -8.106  1.00 20.24  ? 525  LEU B CD1   1 
ATOM   8052 C  CD2   . LEU B 1 539 ? 38.137  63.188 -7.059  1.00 19.73  ? 525  LEU B CD2   1 
ATOM   8053 N  N     . ILE B 1 540 ? 40.415  65.228 -9.076  1.00 20.12  ? 526  ILE B N     1 
ATOM   8054 C  CA    . ILE B 1 540 ? 40.718  66.493 -8.414  1.00 21.45  ? 526  ILE B CA    1 
ATOM   8055 C  C     . ILE B 1 540 ? 39.423  67.028 -7.825  1.00 22.74  ? 526  ILE B C     1 
ATOM   8056 O  O     . ILE B 1 540 ? 38.492  67.389 -8.562  1.00 21.83  ? 526  ILE B O     1 
ATOM   8057 C  CB    . ILE B 1 540 ? 41.348  67.511 -9.372  1.00 22.16  ? 526  ILE B CB    1 
ATOM   8058 C  CG1   . ILE B 1 540 ? 42.533  66.884 -10.100 1.00 22.49  ? 526  ILE B CG1   1 
ATOM   8059 C  CG2   . ILE B 1 540 ? 41.747  68.782 -8.631  1.00 23.41  ? 526  ILE B CG2   1 
ATOM   8060 C  CD1   . ILE B 1 540 ? 43.064  67.752 -11.219 1.00 24.89  ? 526  ILE B CD1   1 
ATOM   8061 N  N     . GLU B 1 541 ? 39.347  67.053 -6.502  1.00 21.88  ? 527  GLU B N     1 
ATOM   8062 C  CA    . GLU B 1 541 ? 38.195  67.618 -5.814  1.00 23.36  ? 527  GLU B CA    1 
ATOM   8063 C  C     . GLU B 1 541 ? 38.442  69.112 -5.666  1.00 26.12  ? 527  GLU B C     1 
ATOM   8064 O  O     . GLU B 1 541 ? 39.324  69.533 -4.902  1.00 25.33  ? 527  GLU B O     1 
ATOM   8065 C  CB    . GLU B 1 541 ? 37.970  66.943 -4.464  1.00 24.62  ? 527  GLU B CB    1 
ATOM   8066 C  CG    . GLU B 1 541 ? 36.872  67.598 -3.640  1.00 26.22  ? 527  GLU B CG    1 
ATOM   8067 C  CD    . GLU B 1 541 ? 36.663  66.915 -2.295  1.00 28.64  ? 527  GLU B CD    1 
ATOM   8068 O  OE1   . GLU B 1 541 ? 37.581  66.205 -1.826  1.00 25.99  ? 527  GLU B OE1   1 
ATOM   8069 O  OE2   . GLU B 1 541 ? 35.583  67.096 -1.701  1.00 26.58  ? 527  GLU B OE2   1 
ATOM   8070 N  N     . VAL B 1 542 ? 37.684  69.911 -6.405  1.00 24.82  ? 528  VAL B N     1 
ATOM   8071 C  CA    . VAL B 1 542 ? 37.887  71.351 -6.459  1.00 24.69  ? 528  VAL B CA    1 
ATOM   8072 C  C     . VAL B 1 542 ? 36.918  71.997 -5.494  1.00 26.86  ? 528  VAL B C     1 
ATOM   8073 O  O     . VAL B 1 542 ? 35.703  71.960 -5.718  1.00 26.52  ? 528  VAL B O     1 
ATOM   8074 C  CB    . VAL B 1 542 ? 37.681  71.898 -7.880  1.00 24.94  ? 528  VAL B CB    1 
ATOM   8075 C  CG1   . VAL B 1 542 ? 37.966  73.395 -7.900  1.00 25.30  ? 528  VAL B CG1   1 
ATOM   8076 C  CG2   . VAL B 1 542 ? 38.549  71.146 -8.882  1.00 24.38  ? 528  VAL B CG2   1 
ATOM   8077 N  N     . MET B 1 543 ? 37.454  72.634 -4.449  1.00 27.77  ? 529  MET B N     1 
ATOM   8078 C  CA    . MET B 1 543 ? 36.634  73.227 -3.395  1.00 28.93  ? 529  MET B CA    1 
ATOM   8079 C  C     . MET B 1 543 ? 36.193  74.614 -3.845  1.00 31.26  ? 529  MET B C     1 
ATOM   8080 O  O     . MET B 1 543 ? 37.018  75.523 -3.969  1.00 31.20  ? 529  MET B O     1 
ATOM   8081 C  CB    . MET B 1 543 ? 37.438  73.326 -2.103  1.00 31.04  ? 529  MET B CB    1 
ATOM   8082 C  CG    . MET B 1 543 ? 37.662  72.037 -1.312  1.00 32.39  ? 529  MET B CG    1 
ATOM   8083 S  SD    . MET B 1 543 ? 36.470  70.705 -1.440  1.00 35.97  ? 529  MET B SD    1 
ATOM   8084 C  CE    . MET B 1 543 ? 34.955  71.513 -0.914  1.00 36.83  ? 529  MET B CE    1 
ATOM   8085 N  N     . LEU B 1 544 ? 34.894  74.794 -4.066  1.00 35.59  ? 530  LEU B N     1 
ATOM   8086 C  CA    . LEU B 1 544 ? 34.387  76.057 -4.577  1.00 35.79  ? 530  LEU B CA    1 
ATOM   8087 C  C     . LEU B 1 544 ? 33.316  76.607 -3.646  1.00 39.36  ? 530  LEU B C     1 
ATOM   8088 O  O     . LEU B 1 544 ? 32.678  75.847 -2.909  1.00 38.82  ? 530  LEU B O     1 
ATOM   8089 C  CB    . LEU B 1 544 ? 33.820  75.879 -5.992  1.00 34.07  ? 530  LEU B CB    1 
ATOM   8090 C  CG    . LEU B 1 544 ? 34.902  75.691 -7.061  1.00 32.53  ? 530  LEU B CG    1 
ATOM   8091 C  CD1   . LEU B 1 544 ? 34.344  75.074 -8.348  1.00 30.39  ? 530  LEU B CD1   1 
ATOM   8092 C  CD2   . LEU B 1 544 ? 35.599  77.009 -7.362  1.00 34.62  ? 530  LEU B CD2   1 
ATOM   8093 N  N     . PRO B 1 545 ? 33.119  77.926 -3.635  1.00 39.86  ? 531  PRO B N     1 
ATOM   8094 C  CA    . PRO B 1 545 ? 32.124  78.514 -2.730  1.00 43.00  ? 531  PRO B CA    1 
ATOM   8095 C  C     . PRO B 1 545 ? 30.707  78.112 -3.109  1.00 46.59  ? 531  PRO B C     1 
ATOM   8096 O  O     . PRO B 1 545 ? 30.383  77.898 -4.282  1.00 46.90  ? 531  PRO B O     1 
ATOM   8097 C  CB    . PRO B 1 545 ? 32.333  80.025 -2.883  1.00 43.13  ? 531  PRO B CB    1 
ATOM   8098 C  CG    . PRO B 1 545 ? 33.635  80.204 -3.553  1.00 42.20  ? 531  PRO B CG    1 
ATOM   8099 C  CD    . PRO B 1 545 ? 33.974  78.938 -4.278  1.00 40.40  ? 531  PRO B CD    1 
ATOM   8100 N  N     . LYS B 1 546 ? 29.854  78.030 -2.086  1.00 48.36  ? 532  LYS B N     1 
ATOM   8101 C  CA    . LYS B 1 546 ? 28.509  77.495 -2.277  1.00 49.22  ? 532  LYS B CA    1 
ATOM   8102 C  C     . LYS B 1 546 ? 27.670  78.374 -3.199  1.00 52.76  ? 532  LYS B C     1 
ATOM   8103 O  O     . LYS B 1 546 ? 26.941  77.862 -4.058  1.00 53.03  ? 532  LYS B O     1 
ATOM   8104 C  CB    . LYS B 1 546 ? 27.825  77.315 -0.923  1.00 52.19  ? 532  LYS B CB    1 
ATOM   8105 C  CG    . LYS B 1 546 ? 26.372  76.910 -1.019  1.00 55.11  ? 532  LYS B CG    1 
ATOM   8106 C  CD    . LYS B 1 546 ? 25.821  76.510 0.341   1.00 57.16  ? 532  LYS B CD    1 
ATOM   8107 C  CE    . LYS B 1 546 ? 26.407  75.176 0.782   1.00 54.73  ? 532  LYS B CE    1 
ATOM   8108 N  NZ    . LYS B 1 546 ? 25.783  74.667 2.031   1.00 60.17  ? 532  LYS B NZ    1 
ATOM   8109 N  N     . ALA B 1 547 ? 27.764  79.696 -3.054  1.00 52.93  ? 533  ALA B N     1 
ATOM   8110 C  CA    . ALA B 1 547 ? 26.922  80.605 -3.820  1.00 55.42  ? 533  ALA B CA    1 
ATOM   8111 C  C     . ALA B 1 547 ? 27.609  81.146 -5.069  1.00 56.44  ? 533  ALA B C     1 
ATOM   8112 O  O     . ALA B 1 547 ? 27.099  82.091 -5.683  1.00 57.42  ? 533  ALA B O     1 
ATOM   8113 C  CB    . ALA B 1 547 ? 26.469  81.769 -2.934  1.00 52.49  ? 533  ALA B CB    1 
ATOM   8114 N  N     . ASP B 1 548 ? 28.715  80.536 -5.493  1.00 53.42  ? 534  ASP B N     1 
ATOM   8115 C  CA    . ASP B 1 548 ? 29.490  81.045 -6.616  1.00 53.17  ? 534  ASP B CA    1 
ATOM   8116 C  C     . ASP B 1 548 ? 28.995  80.437 -7.921  1.00 54.12  ? 534  ASP B C     1 
ATOM   8117 O  O     . ASP B 1 548 ? 28.882  79.213 -8.046  1.00 52.62  ? 534  ASP B O     1 
ATOM   8118 C  CB    . ASP B 1 548 ? 30.983  80.766 -6.442  1.00 48.56  ? 534  ASP B CB    1 
ATOM   8119 C  CG    . ASP B 1 548 ? 31.851  81.768 -7.193  1.00 47.51  ? 534  ASP B CG    1 
ATOM   8120 O  OD1   . ASP B 1 548 ? 31.301  82.538 -8.018  1.00 50.41  ? 534  ASP B OD1   1 
ATOM   8121 O  OD2   . ASP B 1 548 ? 33.081  81.786 -6.966  1.00 42.41  ? 534  ASP B OD2   1 
ATOM   8122 N  N     . ILE B 1 549 ? 28.667  81.305 -8.872  1.00 55.25  ? 535  ILE B N     1 
ATOM   8123 C  CA    . ILE B 1 549 ? 28.117  80.902 -10.161 1.00 59.22  ? 535  ILE B CA    1 
ATOM   8124 C  C     . ILE B 1 549 ? 28.882  81.589 -11.291 1.00 59.69  ? 535  ILE B C     1 
ATOM   8125 O  O     . ILE B 1 549 ? 29.294  82.751 -11.145 1.00 59.36  ? 535  ILE B O     1 
ATOM   8126 C  CB    . ILE B 1 549 ? 26.605  81.184 -10.202 1.00 62.33  ? 535  ILE B CB    1 
ATOM   8127 C  CG1   . ILE B 1 549 ? 26.322  82.658 -9.910  1.00 62.98  ? 535  ILE B CG1   1 
ATOM   8128 C  CG2   . ILE B 1 549 ? 25.871  80.299 -9.209  1.00 60.61  ? 535  ILE B CG2   1 
ATOM   8129 C  CD1   . ILE B 1 549 ? 25.067  83.162 -10.526 1.00 66.91  ? 535  ILE B CD1   1 
ATOM   8130 N  N     . PRO B 1 550 ? 29.104  80.916 -12.420 1.00 61.97  ? 536  PRO B N     1 
ATOM   8131 C  CA    . PRO B 1 550 ? 29.849  81.532 -13.526 1.00 59.05  ? 536  PRO B CA    1 
ATOM   8132 C  C     . PRO B 1 550 ? 29.029  82.641 -14.159 1.00 64.03  ? 536  PRO B C     1 
ATOM   8133 O  O     . PRO B 1 550 ? 27.822  82.746 -13.889 1.00 65.76  ? 536  PRO B O     1 
ATOM   8134 C  CB    . PRO B 1 550 ? 30.064  80.364 -14.506 1.00 55.48  ? 536  PRO B CB    1 
ATOM   8135 C  CG    . PRO B 1 550 ? 29.793  79.130 -13.720 1.00 53.00  ? 536  PRO B CG    1 
ATOM   8136 C  CD    . PRO B 1 550 ? 28.744  79.522 -12.724 1.00 57.18  ? 536  PRO B CD    1 
ATOM   8137 N  N     . PRO B 1 551 ? 29.650  83.502 -14.983 1.00 67.87  ? 537  PRO B N     1 
ATOM   8138 C  CA    . PRO B 1 551 ? 28.899  84.633 -15.580 1.00 64.31  ? 537  PRO B CA    1 
ATOM   8139 C  C     . PRO B 1 551 ? 27.625  84.245 -16.316 1.00 66.06  ? 537  PRO B C     1 
ATOM   8140 O  O     . PRO B 1 551 ? 26.595  84.906 -16.124 1.00 67.81  ? 537  PRO B O     1 
ATOM   8141 C  CB    . PRO B 1 551 ? 29.942  85.294 -16.495 1.00 61.24  ? 537  PRO B CB    1 
ATOM   8142 C  CG    . PRO B 1 551 ? 31.247  84.980 -15.819 1.00 58.98  ? 537  PRO B CG    1 
ATOM   8143 C  CD    . PRO B 1 551 ? 31.090  83.579 -15.290 1.00 58.71  ? 537  PRO B CD    1 
ATOM   8144 N  N     . LEU B 1 552 ? 27.671  83.236 -17.194 1.00 64.34  ? 538  LEU B N     1 
ATOM   8145 C  CA    . LEU B 1 552 ? 26.472  82.880 -17.954 1.00 65.62  ? 538  LEU B CA    1 
ATOM   8146 C  C     . LEU B 1 552 ? 25.363  82.380 -17.037 1.00 69.91  ? 538  LEU B C     1 
ATOM   8147 O  O     . LEU B 1 552 ? 24.179  82.643 -17.285 1.00 71.17  ? 538  LEU B O     1 
ATOM   8148 C  CB    . LEU B 1 552 ? 26.781  81.827 -19.026 1.00 60.20  ? 538  LEU B CB    1 
ATOM   8149 C  CG    . LEU B 1 552 ? 25.551  81.103 -19.619 1.00 63.41  ? 538  LEU B CG    1 
ATOM   8150 C  CD1   . LEU B 1 552 ? 24.908  81.869 -20.773 1.00 50.95  ? 538  LEU B CD1   1 
ATOM   8151 C  CD2   . LEU B 1 552 ? 25.880  79.679 -20.070 1.00 52.00  ? 538  LEU B CD2   1 
ATOM   8152 N  N     . LEU B 1 553 ? 25.725  81.653 -15.974 1.00 68.48  ? 539  LEU B N     1 
ATOM   8153 C  CA    . LEU B 1 553 ? 24.716  81.143 -15.051 1.00 71.90  ? 539  LEU B CA    1 
ATOM   8154 C  C     . LEU B 1 553 ? 23.937  82.285 -14.411 1.00 76.69  ? 539  LEU B C     1 
ATOM   8155 O  O     . LEU B 1 553 ? 22.711  82.209 -14.273 1.00 79.42  ? 539  LEU B O     1 
ATOM   8156 C  CB    . LEU B 1 553 ? 25.377  80.275 -13.979 1.00 67.80  ? 539  LEU B CB    1 
ATOM   8157 C  CG    . LEU B 1 553 ? 24.460  79.477 -13.049 1.00 68.74  ? 539  LEU B CG    1 
ATOM   8158 C  CD1   . LEU B 1 553 ? 23.299  78.885 -13.821 1.00 70.26  ? 539  LEU B CD1   1 
ATOM   8159 C  CD2   . LEU B 1 553 ? 25.224  78.376 -12.321 1.00 63.80  ? 539  LEU B CD2   1 
ATOM   8160 N  N     . GLY B 1 554 ? 24.632  83.351 -14.010 1.00 75.01  ? 540  GLY B N     1 
ATOM   8161 C  CA    . GLY B 1 554 ? 23.941  84.521 -13.492 1.00 76.27  ? 540  GLY B CA    1 
ATOM   8162 C  C     . GLY B 1 554 ? 22.983  85.135 -14.495 1.00 80.09  ? 540  GLY B C     1 
ATOM   8163 O  O     . GLY B 1 554 ? 21.913  85.626 -14.126 1.00 81.04  ? 540  GLY B O     1 
ATOM   8164 N  N     . ALA B 1 555 ? 23.358  85.120 -15.778 1.00 79.66  ? 541  ALA B N     1 
ATOM   8165 C  CA    . ALA B 1 555 ? 22.506  85.684 -16.823 1.00 78.59  ? 541  ALA B CA    1 
ATOM   8166 C  C     . ALA B 1 555 ? 21.324  84.774 -17.151 1.00 79.39  ? 541  ALA B C     1 
ATOM   8167 O  O     . ALA B 1 555 ? 20.228  85.266 -17.452 1.00 80.13  ? 541  ALA B O     1 
ATOM   8168 C  CB    . ALA B 1 555 ? 23.335  85.973 -18.074 1.00 70.45  ? 541  ALA B CB    1 
ATOM   8169 N  N     . ILE B 1 556 ? 21.547  83.465 -17.102 1.00 79.15  ? 542  ILE B N     1 
ATOM   8170 C  CA    . ILE B 1 556 ? 20.497  82.497 -17.402 1.00 79.42  ? 542  ILE B CA    1 
ATOM   8171 C  C     . ILE B 1 556 ? 19.551  82.312 -16.220 1.00 83.29  ? 542  ILE B C     1 
ATOM   8172 O  O     . ILE B 1 556 ? 18.454  81.774 -16.369 1.00 85.14  ? 542  ILE B O     1 
ATOM   8173 C  CB    . ILE B 1 556 ? 21.087  81.131 -17.801 1.00 77.98  ? 542  ILE B CB    1 
ATOM   8174 C  CG1   . ILE B 1 556 ? 21.709  81.206 -19.196 1.00 70.25  ? 542  ILE B CG1   1 
ATOM   8175 C  CG2   . ILE B 1 556 ? 20.017  80.051 -17.749 1.00 77.64  ? 542  ILE B CG2   1 
ATOM   8176 C  CD1   . ILE B 1 556 ? 20.957  80.414 -20.244 1.00 56.11  ? 542  ILE B CD1   1 
ATOM   8177 N  N     . THR B 1 557 ? 19.981  82.763 -15.046 1.00 82.88  ? 543  THR B N     1 
ATOM   8178 C  CA    . THR B 1 557 ? 19.171  82.647 -13.839 1.00 84.09  ? 543  THR B CA    1 
ATOM   8179 C  C     . THR B 1 557 ? 18.418  83.943 -13.552 1.00 85.76  ? 543  THR B C     1 
ATOM   8180 O  O     . THR B 1 557 ? 18.416  84.435 -12.424 1.00 87.03  ? 543  THR B O     1 
ATOM   8181 C  CB    . THR B 1 557 ? 20.031  82.278 -12.615 1.00 79.91  ? 543  THR B CB    1 
ATOM   8182 O  OG1   . THR B 1 557 ? 21.082  83.239 -12.458 1.00 82.54  ? 543  THR B OG1   1 
ATOM   8183 C  CG2   . THR B 1 557 ? 20.637  80.894 -12.789 1.00 78.38  ? 543  THR B CG2   1 
ATOM   8184 N  N     . LYS B 1 558 ? 17.780  84.490 -14.582 1.00 85.28  ? 544  LYS B N     1 
ATOM   8185 C  CA    . LYS B 1 558 ? 17.021  85.727 -14.446 1.00 86.90  ? 544  LYS B CA    1 
ATOM   8186 C  C     . LYS B 1 558 ? 15.658  85.613 -15.120 1.00 93.68  ? 544  LYS B C     1 
ATOM   8187 O  O     . LYS B 1 558 ? 14.759  86.413 -14.864 1.00 89.02  ? 544  LYS B O     1 
ATOM   8188 C  CB    . LYS B 1 558 ? 17.802  86.902 -15.037 1.00 82.70  ? 544  LYS B CB    1 
ATOM   8189 C  CG    . LYS B 1 558 ? 17.283  87.377 -16.384 1.00 78.18  ? 544  LYS B CG    1 
ATOM   8190 C  CD    . LYS B 1 558 ? 18.345  87.246 -17.462 1.00 79.90  ? 544  LYS B CD    1 
ATOM   8191 C  CE    . LYS B 1 558 ? 17.762  87.494 -18.844 1.00 74.74  ? 544  LYS B CE    1 
ATOM   8192 N  NZ    . LYS B 1 558 ? 18.238  86.489 -19.834 1.00 63.93  ? 544  LYS B NZ    1 
ATOM   8193 N  N     . ALA B 1 559 ? 15.513  84.612 -15.982 1.00 96.95  ? 545  ALA B N     1 
ATOM   8194 C  CA    . ALA B 1 559 ? 14.260  84.390 -16.695 1.00 92.40  ? 545  ALA B CA    1 
ATOM   8195 C  C     . ALA B 1 559 ? 13.906  82.907 -16.736 1.00 97.40  ? 545  ALA B C     1 
ATOM   8196 O  O     . ALA B 1 559 ? 12.935  82.509 -17.380 1.00 98.57  ? 545  ALA B O     1 
ATOM   8197 C  CB    . ALA B 1 559 ? 14.344  84.957 -18.104 1.00 82.08  ? 545  ALA B CB    1 
ATOM   8198 N  N     . LEU B 1 560 ? 14.699  82.096 -16.044 1.00 95.53  ? 546  LEU B N     1 
ATOM   8199 C  CA    . LEU B 1 560 ? 14.472  80.656 -16.000 1.00 92.33  ? 546  LEU B CA    1 
ATOM   8200 C  C     . LEU B 1 560 ? 13.118  80.331 -15.378 1.00 96.61  ? 546  LEU B C     1 
ATOM   8201 O  O     . LEU B 1 560 ? 12.302  79.629 -15.975 1.00 91.40  ? 546  LEU B O     1 
ATOM   8202 C  CB    . LEU B 1 560 ? 15.590  79.962 -15.219 1.00 85.41  ? 546  LEU B CB    1 
ATOM   8203 C  CG    . LEU B 1 560 ? 16.087  78.628 -15.780 1.00 72.83  ? 546  LEU B CG    1 
ATOM   8204 C  CD1   . LEU B 1 560 ? 15.560  77.467 -14.951 1.00 61.74  ? 546  LEU B CD1   1 
ATOM   8205 C  CD2   . LEU B 1 560 ? 15.691  78.474 -17.240 1.00 64.95  ? 546  LEU B CD2   1 
ATOM   8206 N  N     . GLU B 1 561 ? 12.886  80.846 -14.175 1.00 99.26  ? 547  GLU B N     1 
ATOM   8207 C  CA    . GLU B 1 561 ? 11.630  80.612 -13.471 1.00 104.36 ? 547  GLU B CA    1 
ATOM   8208 C  C     . GLU B 1 561 ? 10.694  81.809 -13.603 1.00 103.31 ? 547  GLU B C     1 
ATOM   8209 O  O     . GLU B 1 561 ? 9.872   82.067 -12.724 1.00 102.06 ? 547  GLU B O     1 
ATOM   8210 C  CB    . GLU B 1 561 ? 11.891  80.308 -11.995 1.00 92.08  ? 547  GLU B CB    1 
ATOM   8211 C  CG    . GLU B 1 561 ? 11.020  79.200 -11.426 1.00 83.79  ? 547  GLU B CG    1 
ATOM   8212 C  CD    . GLU B 1 561 ? 11.713  78.420 -10.325 1.00 77.33  ? 547  GLU B CD    1 
ATOM   8213 O  OE1   . GLU B 1 561 ? 11.896  78.979 -9.223  1.00 76.24  ? 547  GLU B OE1   1 
ATOM   8214 O  OE2   . GLU B 1 561 ? 12.075  77.248 -10.562 1.00 58.53  ? 547  GLU B OE2   1 
ATOM   8215 N  N     . ALA B 1 562 ? 10.825  82.535 -14.708 1.00 102.19 ? 548  ALA B N     1 
ATOM   8216 C  CA    . ALA B 1 562 ? 9.994   83.707 -14.959 1.00 102.25 ? 548  ALA B CA    1 
ATOM   8217 C  C     . ALA B 1 562 ? 8.563   83.306 -15.303 1.00 104.05 ? 548  ALA B C     1 
ATOM   8218 O  O     . ALA B 1 562 ? 7.618   84.047 -15.029 1.00 101.95 ? 548  ALA B O     1 
ATOM   8219 C  CB    . ALA B 1 562 ? 10.592  84.552 -16.073 1.00 99.43  ? 548  ALA B CB    1 
ATOM   8220 N  N     . ARG B 1 563 ? 8.410   82.131 -15.903 1.00 104.19 ? 549  ARG B N     1 
ATOM   8221 C  CA    . ARG B 1 563 ? 7.094   81.631 -16.285 1.00 101.68 ? 549  ARG B CA    1 
ATOM   8222 C  C     . ARG B 1 563 ? 6.148   81.594 -15.089 1.00 105.88 ? 549  ARG B C     1 
ATOM   8223 O  O     . ARG B 1 563 ? 5.006   82.045 -15.175 1.00 98.05  ? 549  ARG B O     1 
ATOM   8224 C  CB    . ARG B 1 563 ? 7.210   80.239 -16.909 1.00 88.70  ? 549  ARG B CB    1 
ATOM   8225 C  CG    . ARG B 1 563 ? 7.812   80.234 -18.304 1.00 86.97  ? 549  ARG B CG    1 
ATOM   8226 C  CD    . ARG B 1 563 ? 9.314   80.464 -18.257 1.00 78.92  ? 549  ARG B CD    1 
ATOM   8227 N  NE    . ARG B 1 563 ? 10.041  79.253 -17.891 1.00 67.86  ? 549  ARG B NE    1 
ATOM   8228 C  CZ    . ARG B 1 563 ? 9.919   78.089 -18.520 1.00 51.78  ? 549  ARG B CZ    1 
ATOM   8229 N  NH1   . ARG B 1 563 ? 9.095   77.975 -19.553 1.00 48.43  ? 549  ARG B NH1   1 
ATOM   8230 N  NH2   . ARG B 1 563 ? 10.620  77.038 -18.117 1.00 44.54  ? 549  ARG B NH2   1 
ATOM   8231 N  N     . ASN B 1 564 ? 6.630   81.053 -13.975 1.00 112.83 ? 550  ASN B N     1 
ATOM   8232 C  CA    . ASN B 1 564 ? 5.828   80.956 -12.762 1.00 101.62 ? 550  ASN B CA    1 
ATOM   8233 C  C     . ASN B 1 564 ? 6.292   81.961 -11.713 1.00 95.58  ? 550  ASN B C     1 
ATOM   8234 O  O     . ASN B 1 564 ? 7.131   81.645 -10.868 1.00 92.99  ? 550  ASN B O     1 
ATOM   8235 C  CB    . ASN B 1 564 ? 5.885   79.537 -12.193 1.00 30.00  ? 550  ASN B CB    1 
ATOM   8236 C  CG    . ASN B 1 564 ? 4.932   78.589 -12.895 1.00 30.00  ? 550  ASN B CG    1 
ATOM   8237 O  OD1   . ASN B 1 564 ? 3.833   78.324 -12.409 1.00 30.00  ? 550  ASN B OD1   1 
ATOM   8238 N  ND2   . ASN B 1 564 ? 5.351   78.074 -14.045 1.00 30.00  ? 550  ASN B ND2   1 
ATOM   8239 N  N     . SER B 1 565 ? 5.738   83.170 -11.778 1.00 99.60  ? 551  SER B N     1 
ATOM   8240 C  CA    . SER B 1 565 ? 6.074   84.246 -10.848 1.00 101.42 ? 551  SER B CA    1 
ATOM   8241 C  C     . SER B 1 565 ? 7.581   84.441 -10.706 1.00 95.42  ? 551  SER B C     1 
ATOM   8242 O  O     . SER B 1 565 ? 8.135   85.435 -11.176 1.00 92.54  ? 551  SER B O     1 
ATOM   8243 C  CB    . SER B 1 565 ? 5.436   83.999 -9.477  1.00 30.00  ? 551  SER B CB    1 
ATOM   8244 O  OG    . SER B 1 565 ? 4.504   85.017 -9.157  1.00 30.00  ? 551  SER B OG    1 
HETATM 8245 N  "N1'" . TPP C 2 .   ? 20.293  44.032 -15.356 1.00 17.97  ? 601  TPP A "N1'" 1 
HETATM 8246 C  "C2'" . TPP C 2 .   ? 19.289  44.184 -14.467 1.00 17.68  ? 601  TPP A "C2'" 1 
HETATM 8247 C  CM2   . TPP C 2 .   ? 18.876  45.581 -14.125 1.00 14.80  ? 601  TPP A CM2   1 
HETATM 8248 N  "N3'" . TPP C 2 .   ? 18.643  43.195 -13.850 1.00 17.20  ? 601  TPP A "N3'" 1 
HETATM 8249 C  "C4'" . TPP C 2 .   ? 18.997  41.935 -14.144 1.00 19.24  ? 601  TPP A "C4'" 1 
HETATM 8250 N  "N4'" . TPP C 2 .   ? 18.325  40.957 -13.524 1.00 17.69  ? 601  TPP A "N4'" 1 
HETATM 8251 C  "C5'" . TPP C 2 .   ? 20.036  41.663 -15.083 1.00 20.97  ? 601  TPP A "C5'" 1 
HETATM 8252 C  "C6'" . TPP C 2 .   ? 20.646  42.771 -15.628 1.00 20.55  ? 601  TPP A "C6'" 1 
HETATM 8253 C  "C7'" . TPP C 2 .   ? 20.505  40.276 -15.405 1.00 24.48  ? 601  TPP A "C7'" 1 
HETATM 8254 N  N3    . TPP C 2 .   ? 21.125  39.606 -14.235 1.00 26.46  ? 601  TPP A N3    1 
HETATM 8255 C  C2    . TPP C 2 .   ? 20.493  38.728 -13.477 1.00 29.49  ? 601  TPP A C2    1 
HETATM 8256 S  S1    . TPP C 2 .   ? 21.446  38.166 -12.217 1.00 28.82  ? 601  TPP A S1    1 
HETATM 8257 C  C5    . TPP C 2 .   ? 22.764  39.147 -12.731 1.00 30.49  ? 601  TPP A C5    1 
HETATM 8258 C  C4    . TPP C 2 .   ? 22.431  39.879 -13.821 1.00 28.08  ? 601  TPP A C4    1 
HETATM 8259 C  CM4   . TPP C 2 .   ? 23.293  40.842 -14.566 1.00 26.33  ? 601  TPP A CM4   1 
HETATM 8260 C  C6    . TPP C 2 .   ? 24.051  39.128 -11.965 1.00 31.59  ? 601  TPP A C6    1 
HETATM 8261 C  C7    . TPP C 2 .   ? 23.823  39.164 -10.474 1.00 31.35  ? 601  TPP A C7    1 
HETATM 8262 O  O7    . TPP C 2 .   ? 25.093  39.345 -9.806  1.00 31.73  ? 601  TPP A O7    1 
HETATM 8263 P  PA    . TPP C 2 .   ? 25.275  39.221 -8.254  1.00 26.11  ? 601  TPP A PA    1 
HETATM 8264 O  O1A   . TPP C 2 .   ? 24.403  40.215 -7.591  1.00 23.16  ? 601  TPP A O1A   1 
HETATM 8265 O  O2A   . TPP C 2 .   ? 26.774  39.249 -7.910  1.00 26.67  ? 601  TPP A O2A   1 
HETATM 8266 O  O3A   . TPP C 2 .   ? 24.754  37.741 -8.013  1.00 30.80  ? 601  TPP A O3A   1 
HETATM 8267 P  PB    . TPP C 2 .   ? 25.328  36.300 -7.696  1.00 34.59  ? 601  TPP A PB    1 
HETATM 8268 O  O1B   . TPP C 2 .   ? 25.159  35.976 -6.250  1.00 36.64  ? 601  TPP A O1B   1 
HETATM 8269 O  O2B   . TPP C 2 .   ? 26.802  36.360 -8.189  1.00 37.39  ? 601  TPP A O2B   1 
HETATM 8270 O  O3B   . TPP C 2 .   ? 24.583  35.364 -8.586  1.00 39.37  ? 601  TPP A O3B   1 
HETATM 8271 MG MG    . MG  D 3 .   ? 28.367  37.711 -7.357  1.00 23.33  ? 602  MG  A MG    1 
HETATM 8272 N  "N1'" . TPP E 2 .   ? 17.847  64.845 -12.521 1.00 17.24  ? 601  TPP B "N1'" 1 
HETATM 8273 C  "C2'" . TPP E 2 .   ? 18.500  64.733 -13.691 1.00 18.43  ? 601  TPP B "C2'" 1 
HETATM 8274 C  CM2   . TPP E 2 .   ? 18.753  63.353 -14.204 1.00 17.04  ? 601  TPP B CM2   1 
HETATM 8275 N  "N3'" . TPP E 2 .   ? 18.938  65.751 -14.436 1.00 17.81  ? 601  TPP B "N3'" 1 
HETATM 8276 C  "C4'" . TPP E 2 .   ? 18.711  66.999 -13.987 1.00 20.58  ? 601  TPP B "C4'" 1 
HETATM 8277 N  "N4'" . TPP E 2 .   ? 19.155  68.006 -14.744 1.00 19.38  ? 601  TPP B "N4'" 1 
HETATM 8278 C  "C5'" . TPP E 2 .   ? 18.032  67.225 -12.752 1.00 20.98  ? 601  TPP B "C5'" 1 
HETATM 8279 C  "C6'" . TPP E 2 .   ? 17.643  66.090 -12.079 1.00 19.10  ? 601  TPP B "C6'" 1 
HETATM 8280 C  "C7'" . TPP E 2 .   ? 17.772  68.596 -12.191 1.00 23.53  ? 601  TPP B "C7'" 1 
HETATM 8281 N  N3    . TPP E 2 .   ? 19.024  69.338 -11.915 1.00 26.78  ? 601  TPP B N3    1 
HETATM 8282 C  C2    . TPP E 2 .   ? 19.555  70.213 -12.746 1.00 29.12  ? 601  TPP B C2    1 
HETATM 8283 S  S1    . TPP E 2 .   ? 20.997  70.837 -12.170 1.00 32.67  ? 601  TPP B S1    1 
HETATM 8284 C  C5    . TPP E 2 .   ? 20.888  69.873 -10.742 1.00 28.43  ? 601  TPP B C5    1 
HETATM 8285 C  C4    . TPP E 2 .   ? 19.783  69.110 -10.766 1.00 27.03  ? 601  TPP B C4    1 
HETATM 8286 C  CM4   . TPP E 2 .   ? 19.326  68.143 -9.726  1.00 26.68  ? 601  TPP B CM4   1 
HETATM 8287 C  C6    . TPP E 2 .   ? 21.953  69.937 -9.688  1.00 32.22  ? 601  TPP B C6    1 
HETATM 8288 C  C7    . TPP E 2 .   ? 23.344  69.772 -10.256 1.00 31.33  ? 601  TPP B C7    1 
HETATM 8289 O  O7    . TPP E 2 .   ? 24.298  69.828 -9.169  1.00 29.40  ? 601  TPP B O7    1 
HETATM 8290 P  PA    . TPP E 2 .   ? 25.857  69.861 -9.372  1.00 25.96  ? 601  TPP B PA    1 
HETATM 8291 O  O1A   . TPP E 2 .   ? 26.277  68.769 -10.275 1.00 23.30  ? 601  TPP B O1A   1 
HETATM 8292 O  O2A   . TPP E 2 .   ? 26.496  69.834 -7.993  1.00 28.90  ? 601  TPP B O2A   1 
HETATM 8293 O  O3A   . TPP E 2 .   ? 26.098  71.301 -9.958  1.00 29.66  ? 601  TPP B O3A   1 
HETATM 8294 P  PB    . TPP E 2 .   ? 26.477  72.752 -9.448  1.00 35.08  ? 601  TPP B PB    1 
HETATM 8295 O  O1B   . TPP E 2 .   ? 26.464  72.785 -7.959  1.00 35.79  ? 601  TPP B O1B   1 
HETATM 8296 O  O2B   . TPP E 2 .   ? 27.838  73.030 -10.085 1.00 34.45  ? 601  TPP B O2B   1 
HETATM 8297 O  O3B   . TPP E 2 .   ? 25.466  73.669 -10.094 1.00 37.57  ? 601  TPP B O3B   1 
HETATM 8298 MG MG    . MG  F 3 .   ? 27.345  71.307 -6.445  1.00 23.37  ? 602  MG  B MG    1 
HETATM 8299 O  O     . HOH G 4 .   ? 23.503  33.122 13.704  1.00 45.50  ? 701  HOH A O     1 
HETATM 8300 O  O     . HOH G 4 .   ? 7.099   20.386 10.507  1.00 53.79  ? 702  HOH A O     1 
HETATM 8301 O  O     . HOH G 4 .   ? -2.525  50.511 -0.643  1.00 41.60  ? 703  HOH A O     1 
HETATM 8302 O  O     . HOH G 4 .   ? 34.013  39.771 15.000  1.00 43.35  ? 704  HOH A O     1 
HETATM 8303 O  O     . HOH G 4 .   ? -2.690  50.363 -20.380 1.00 47.63  ? 705  HOH A O     1 
HETATM 8304 O  O     . HOH G 4 .   ? -18.532 27.714 8.747   1.00 32.44  ? 706  HOH A O     1 
HETATM 8305 O  O     . HOH G 4 .   ? -13.423 72.398 -18.343 1.00 35.44  ? 707  HOH A O     1 
HETATM 8306 O  O     . HOH G 4 .   ? 37.233  28.859 11.332  1.00 44.81  ? 708  HOH A O     1 
HETATM 8307 O  O     . HOH G 4 .   ? 38.838  38.739 1.573   1.00 47.01  ? 709  HOH A O     1 
HETATM 8308 O  O     . HOH G 4 .   ? 19.681  36.656 -15.933 1.00 33.49  ? 710  HOH A O     1 
HETATM 8309 O  O     . HOH G 4 .   ? 1.226   72.199 1.771   1.00 32.12  ? 711  HOH A O     1 
HETATM 8310 O  O     . HOH G 4 .   ? -9.349  24.795 -17.147 1.00 42.25  ? 712  HOH A O     1 
HETATM 8311 O  O     . HOH G 4 .   ? 1.132   21.917 -13.324 1.00 36.53  ? 713  HOH A O     1 
HETATM 8312 O  O     . HOH G 4 .   ? 8.030   68.367 5.384   1.00 38.07  ? 714  HOH A O     1 
HETATM 8313 O  O     . HOH G 4 .   ? -7.876  63.502 -17.737 1.00 44.17  ? 715  HOH A O     1 
HETATM 8314 O  O     . HOH G 4 .   ? -29.140 37.956 -3.629  1.00 35.58  ? 716  HOH A O     1 
HETATM 8315 O  O     . HOH G 4 .   ? 1.451   61.974 6.860   1.00 43.43  ? 717  HOH A O     1 
HETATM 8316 O  O     . HOH G 4 .   ? -5.432  29.843 -13.533 1.00 27.53  ? 718  HOH A O     1 
HETATM 8317 O  O     . HOH G 4 .   ? -14.042 23.624 13.802  1.00 58.63  ? 719  HOH A O     1 
HETATM 8318 O  O     . HOH G 4 .   ? -6.361  16.966 -11.991 1.00 44.69  ? 720  HOH A O     1 
HETATM 8319 O  O     . HOH G 4 .   ? 24.397  45.188 18.191  1.00 30.94  ? 721  HOH A O     1 
HETATM 8320 O  O     . HOH G 4 .   ? 27.358  37.842 -5.785  1.00 28.56  ? 722  HOH A O     1 
HETATM 8321 O  O     . HOH G 4 .   ? 37.390  37.967 8.602   1.00 37.04  ? 723  HOH A O     1 
HETATM 8322 O  O     . HOH G 4 .   ? 33.659  33.842 19.055  1.00 38.05  ? 724  HOH A O     1 
HETATM 8323 O  O     . HOH G 4 .   ? 35.260  35.747 15.541  1.00 46.28  ? 725  HOH A O     1 
HETATM 8324 O  O     . HOH G 4 .   ? -10.842 55.509 -9.857  1.00 28.76  ? 726  HOH A O     1 
HETATM 8325 O  O     . HOH G 4 .   ? -8.247  78.730 -10.903 1.00 25.87  ? 727  HOH A O     1 
HETATM 8326 O  O     . HOH G 4 .   ? 6.441   42.450 1.948   1.00 19.69  ? 728  HOH A O     1 
HETATM 8327 O  O     . HOH G 4 .   ? -1.660  17.671 -9.407  1.00 30.80  ? 729  HOH A O     1 
HETATM 8328 O  O     . HOH G 4 .   ? 36.512  42.009 -13.946 1.00 46.91  ? 730  HOH A O     1 
HETATM 8329 O  O     . HOH G 4 .   ? -8.053  18.611 4.634   1.00 34.76  ? 731  HOH A O     1 
HETATM 8330 O  O     . HOH G 4 .   ? -21.102 31.147 3.041   1.00 38.64  ? 732  HOH A O     1 
HETATM 8331 O  O     . HOH G 4 .   ? 0.793   38.486 -12.542 1.00 27.18  ? 733  HOH A O     1 
HETATM 8332 O  O     . HOH G 4 .   ? -8.705  29.679 -16.331 1.00 46.93  ? 734  HOH A O     1 
HETATM 8333 O  O     . HOH G 4 .   ? 16.103  32.679 14.044  1.00 29.21  ? 735  HOH A O     1 
HETATM 8334 O  O     . HOH G 4 .   ? -2.305  51.540 -18.282 1.00 25.90  ? 736  HOH A O     1 
HETATM 8335 O  O     . HOH G 4 .   ? 11.355  26.399 -2.294  1.00 46.02  ? 737  HOH A O     1 
HETATM 8336 O  O     . HOH G 4 .   ? 11.844  60.021 8.061   1.00 28.52  ? 738  HOH A O     1 
HETATM 8337 O  O     . HOH G 4 .   ? 7.224   34.860 17.690  1.00 40.99  ? 739  HOH A O     1 
HETATM 8338 O  O     . HOH G 4 .   ? 38.622  48.503 4.865   1.00 32.46  ? 740  HOH A O     1 
HETATM 8339 O  O     . HOH G 4 .   ? 12.360  31.412 -17.737 1.00 41.13  ? 741  HOH A O     1 
HETATM 8340 O  O     . HOH G 4 .   ? 32.777  58.144 11.125  1.00 36.38  ? 742  HOH A O     1 
HETATM 8341 O  O     . HOH G 4 .   ? 23.148  36.930 -4.987  1.00 35.10  ? 743  HOH A O     1 
HETATM 8342 O  O     . HOH G 4 .   ? -9.298  21.819 -17.296 1.00 47.73  ? 744  HOH A O     1 
HETATM 8343 O  O     . HOH G 4 .   ? -7.337  74.133 -10.251 1.00 23.13  ? 745  HOH A O     1 
HETATM 8344 O  O     . HOH G 4 .   ? 1.160   56.716 7.964   1.00 54.78  ? 746  HOH A O     1 
HETATM 8345 O  O     . HOH G 4 .   ? 4.368   16.173 -6.850  1.00 45.30  ? 747  HOH A O     1 
HETATM 8346 O  O     . HOH G 4 .   ? -20.263 41.401 -9.089  1.00 42.63  ? 748  HOH A O     1 
HETATM 8347 O  O     . HOH G 4 .   ? 31.059  34.992 -9.390  1.00 53.88  ? 749  HOH A O     1 
HETATM 8348 O  O     . HOH G 4 .   ? 35.075  59.474 5.171   1.00 27.44  ? 750  HOH A O     1 
HETATM 8349 O  O     . HOH G 4 .   ? 35.121  33.046 17.542  1.00 43.72  ? 751  HOH A O     1 
HETATM 8350 O  O     . HOH G 4 .   ? 8.544   45.980 -7.424  1.00 14.74  ? 752  HOH A O     1 
HETATM 8351 O  O     . HOH G 4 .   ? -2.047  54.470 -17.178 1.00 26.20  ? 753  HOH A O     1 
HETATM 8352 O  O     . HOH G 4 .   ? 23.919  47.370 11.653  1.00 25.94  ? 754  HOH A O     1 
HETATM 8353 O  O     . HOH G 4 .   ? -8.030  76.438 -9.101  1.00 24.97  ? 755  HOH A O     1 
HETATM 8354 O  O     . HOH G 4 .   ? 36.583  45.286 1.534   1.00 30.27  ? 756  HOH A O     1 
HETATM 8355 O  O     . HOH G 4 .   ? -10.612 14.831 9.796   1.00 37.52  ? 757  HOH A O     1 
HETATM 8356 O  O     . HOH G 4 .   ? 5.663   71.059 -11.133 1.00 21.56  ? 758  HOH A O     1 
HETATM 8357 O  O     . HOH G 4 .   ? 0.191   47.464 -19.316 1.00 24.17  ? 759  HOH A O     1 
HETATM 8358 O  O     . HOH G 4 .   ? 16.751  58.686 9.513   1.00 29.06  ? 760  HOH A O     1 
HETATM 8359 O  O     . HOH G 4 .   ? 19.157  48.412 -11.087 1.00 14.80  ? 761  HOH A O     1 
HETATM 8360 O  O     . HOH G 4 .   ? 9.890   66.409 -26.632 1.00 20.23  ? 762  HOH A O     1 
HETATM 8361 O  O     . HOH G 4 .   ? 5.811   64.153 -18.552 1.00 18.28  ? 763  HOH A O     1 
HETATM 8362 O  O     . HOH G 4 .   ? 5.641   24.274 11.083  1.00 39.21  ? 764  HOH A O     1 
HETATM 8363 O  O     . HOH G 4 .   ? 22.295  39.750 -6.083  1.00 24.48  ? 765  HOH A O     1 
HETATM 8364 O  O     . HOH G 4 .   ? -15.048 43.769 -0.402  1.00 38.36  ? 766  HOH A O     1 
HETATM 8365 O  O     . HOH G 4 .   ? 4.928   76.127 0.695   1.00 34.85  ? 767  HOH A O     1 
HETATM 8366 O  O     . HOH G 4 .   ? -14.765 18.508 -8.554  1.00 42.74  ? 768  HOH A O     1 
HETATM 8367 O  O     . HOH G 4 .   ? 36.699  43.714 -1.351  1.00 30.58  ? 769  HOH A O     1 
HETATM 8368 O  O     . HOH G 4 .   ? -21.659 41.032 -1.635  1.00 33.81  ? 770  HOH A O     1 
HETATM 8369 O  O     . HOH G 4 .   ? 14.533  70.089 -14.190 1.00 23.61  ? 771  HOH A O     1 
HETATM 8370 O  O     . HOH G 4 .   ? 32.946  44.399 -6.965  1.00 24.69  ? 772  HOH A O     1 
HETATM 8371 O  O     . HOH G 4 .   ? 18.260  64.381 -4.534  1.00 23.78  ? 773  HOH A O     1 
HETATM 8372 O  O     . HOH G 4 .   ? -16.772 24.903 -11.073 1.00 29.74  ? 774  HOH A O     1 
HETATM 8373 O  O     . HOH G 4 .   ? -22.317 27.965 -8.809  1.00 25.16  ? 775  HOH A O     1 
HETATM 8374 O  O     . HOH G 4 .   ? 2.622   34.269 -6.898  1.00 19.82  ? 776  HOH A O     1 
HETATM 8375 O  O     . HOH G 4 .   ? 14.159  64.490 -11.036 1.00 17.05  ? 777  HOH A O     1 
HETATM 8376 O  O     . HOH G 4 .   ? 4.713   75.299 -8.922  1.00 33.47  ? 778  HOH A O     1 
HETATM 8377 O  O     . HOH G 4 .   ? 16.254  55.470 -17.855 1.00 16.21  ? 779  HOH A O     1 
HETATM 8378 O  O     . HOH G 4 .   ? 10.884  70.993 -27.421 1.00 21.00  ? 780  HOH A O     1 
HETATM 8379 O  O     . HOH G 4 .   ? 8.075   39.723 -1.244  1.00 18.60  ? 781  HOH A O     1 
HETATM 8380 O  O     . HOH G 4 .   ? 13.589  36.234 -11.208 1.00 29.18  ? 782  HOH A O     1 
HETATM 8381 O  O     . HOH G 4 .   ? 1.471   67.969 -29.428 1.00 39.77  ? 783  HOH A O     1 
HETATM 8382 O  O     . HOH G 4 .   ? 9.447   35.312 -12.121 1.00 22.37  ? 784  HOH A O     1 
HETATM 8383 O  O     . HOH G 4 .   ? -12.075 57.184 -3.483  1.00 40.29  ? 785  HOH A O     1 
HETATM 8384 O  O     . HOH G 4 .   ? 13.886  42.160 14.652  1.00 25.50  ? 786  HOH A O     1 
HETATM 8385 O  O     . HOH G 4 .   ? 1.464   29.762 9.710   1.00 30.89  ? 787  HOH A O     1 
HETATM 8386 O  O     . HOH G 4 .   ? 19.146  51.572 15.103  1.00 29.82  ? 788  HOH A O     1 
HETATM 8387 O  O     . HOH G 4 .   ? -8.724  22.020 10.586  1.00 33.15  ? 789  HOH A O     1 
HETATM 8388 O  O     . HOH G 4 .   ? 14.593  53.623 -15.539 1.00 15.63  ? 790  HOH A O     1 
HETATM 8389 O  O     . HOH G 4 .   ? 6.547   56.391 8.599   1.00 39.92  ? 791  HOH A O     1 
HETATM 8390 O  O     . HOH G 4 .   ? -10.842 17.908 6.838   1.00 35.69  ? 792  HOH A O     1 
HETATM 8391 O  O     . HOH G 4 .   ? 8.664   77.031 -11.553 1.00 58.57  ? 793  HOH A O     1 
HETATM 8392 O  O     . HOH G 4 .   ? 6.486   35.577 8.799   1.00 27.37  ? 794  HOH A O     1 
HETATM 8393 O  O     . HOH G 4 .   ? 19.074  59.693 -13.390 1.00 16.24  ? 795  HOH A O     1 
HETATM 8394 O  O     . HOH G 4 .   ? 6.812   30.628 2.392   1.00 24.45  ? 796  HOH A O     1 
HETATM 8395 O  O     . HOH G 4 .   ? -1.470  79.432 -15.953 1.00 43.26  ? 797  HOH A O     1 
HETATM 8396 O  O     . HOH G 4 .   ? -7.307  78.577 -1.967  1.00 34.69  ? 798  HOH A O     1 
HETATM 8397 O  O     . HOH G 4 .   ? 20.839  45.357 -4.399  1.00 16.67  ? 799  HOH A O     1 
HETATM 8398 O  O     . HOH G 4 .   ? 24.357  59.292 -1.667  1.00 20.04  ? 800  HOH A O     1 
HETATM 8399 O  O     . HOH G 4 .   ? 14.676  40.675 -5.465  1.00 21.46  ? 801  HOH A O     1 
HETATM 8400 O  O     . HOH G 4 .   ? 4.227   24.408 3.357   1.00 28.99  ? 802  HOH A O     1 
HETATM 8401 O  O     . HOH G 4 .   ? -11.445 22.696 -7.992  1.00 28.44  ? 803  HOH A O     1 
HETATM 8402 O  O     . HOH G 4 .   ? 35.019  41.301 -26.702 1.00 28.96  ? 804  HOH A O     1 
HETATM 8403 O  O     . HOH G 4 .   ? -8.216  76.620 -17.472 1.00 31.05  ? 805  HOH A O     1 
HETATM 8404 O  O     . HOH G 4 .   ? 15.258  58.630 5.058   1.00 24.40  ? 806  HOH A O     1 
HETATM 8405 O  O     . HOH G 4 .   ? 22.193  60.916 -1.105  1.00 22.16  ? 807  HOH A O     1 
HETATM 8406 O  O     . HOH G 4 .   ? 8.804   52.736 -8.209  1.00 16.24  ? 808  HOH A O     1 
HETATM 8407 O  O     . HOH G 4 .   ? -18.017 36.270 -16.068 1.00 29.59  ? 809  HOH A O     1 
HETATM 8408 O  O     . HOH G 4 .   ? -13.328 69.939 -15.904 1.00 28.79  ? 810  HOH A O     1 
HETATM 8409 O  O     . HOH G 4 .   ? -22.923 25.281 4.418   1.00 29.29  ? 811  HOH A O     1 
HETATM 8410 O  O     . HOH G 4 .   ? -0.065  53.266 -24.457 1.00 33.81  ? 812  HOH A O     1 
HETATM 8411 O  O     . HOH G 4 .   ? 33.195  24.676 5.138   1.00 46.73  ? 813  HOH A O     1 
HETATM 8412 O  O     . HOH G 4 .   ? -0.017  47.680 -1.134  1.00 25.51  ? 814  HOH A O     1 
HETATM 8413 O  O     . HOH G 4 .   ? 6.501   57.586 -0.185  1.00 19.61  ? 815  HOH A O     1 
HETATM 8414 O  O     . HOH G 4 .   ? -1.840  70.675 -18.046 1.00 27.66  ? 816  HOH A O     1 
HETATM 8415 O  O     . HOH G 4 .   ? 2.085   30.107 -15.206 1.00 25.81  ? 817  HOH A O     1 
HETATM 8416 O  O     . HOH G 4 .   ? 4.592   60.274 -28.640 1.00 35.34  ? 818  HOH A O     1 
HETATM 8417 O  O     . HOH G 4 .   ? -13.007 51.595 -11.332 1.00 40.19  ? 819  HOH A O     1 
HETATM 8418 O  O     . HOH G 4 .   ? -14.207 17.330 3.113   1.00 44.97  ? 820  HOH A O     1 
HETATM 8419 O  O     . HOH G 4 .   ? -0.241  58.897 6.499   1.00 35.22  ? 821  HOH A O     1 
HETATM 8420 O  O     . HOH G 4 .   ? 2.371   33.623 14.824  1.00 37.54  ? 822  HOH A O     1 
HETATM 8421 O  O     . HOH G 4 .   ? 2.750   21.142 11.544  1.00 44.56  ? 823  HOH A O     1 
HETATM 8422 O  O     . HOH G 4 .   ? 24.356  55.473 9.541   1.00 27.52  ? 824  HOH A O     1 
HETATM 8423 O  O     . HOH G 4 .   ? 4.221   43.963 2.413   1.00 20.15  ? 825  HOH A O     1 
HETATM 8424 O  O     . HOH G 4 .   ? -24.549 35.866 -1.382  1.00 30.90  ? 826  HOH A O     1 
HETATM 8425 O  O     . HOH G 4 .   ? 5.835   47.766 10.652  1.00 39.56  ? 827  HOH A O     1 
HETATM 8426 O  O     . HOH G 4 .   ? 11.535  77.623 -28.740 1.00 29.86  ? 828  HOH A O     1 
HETATM 8427 O  O     . HOH G 4 .   ? 3.196   72.887 2.982   1.00 39.53  ? 829  HOH A O     1 
HETATM 8428 O  O     . HOH G 4 .   ? 21.133  53.509 -10.008 1.00 14.66  ? 830  HOH A O     1 
HETATM 8429 O  O     . HOH G 4 .   ? 6.435   56.213 -14.636 1.00 19.12  ? 831  HOH A O     1 
HETATM 8430 O  O     . HOH G 4 .   ? 12.107  30.701 12.594  1.00 32.84  ? 832  HOH A O     1 
HETATM 8431 O  O     . HOH G 4 .   ? 7.401   58.963 -18.173 1.00 17.18  ? 833  HOH A O     1 
HETATM 8432 O  O     . HOH G 4 .   ? 10.533  23.855 -0.136  1.00 32.82  ? 834  HOH A O     1 
HETATM 8433 O  O     . HOH G 4 .   ? -9.235  55.646 -13.343 1.00 24.75  ? 835  HOH A O     1 
HETATM 8434 O  O     . HOH G 4 .   ? -12.055 20.122 2.300   1.00 31.62  ? 836  HOH A O     1 
HETATM 8435 O  O     . HOH G 4 .   ? -17.306 32.150 -16.415 1.00 23.63  ? 837  HOH A O     1 
HETATM 8436 O  O     . HOH G 4 .   ? -25.828 42.205 -3.464  1.00 38.66  ? 838  HOH A O     1 
HETATM 8437 O  O     . HOH G 4 .   ? -8.742  70.103 -18.428 1.00 24.42  ? 839  HOH A O     1 
HETATM 8438 O  O     . HOH G 4 .   ? -25.981 29.435 -6.939  1.00 32.99  ? 840  HOH A O     1 
HETATM 8439 O  O     . HOH G 4 .   ? 5.441   63.846 -21.524 1.00 20.77  ? 841  HOH A O     1 
HETATM 8440 O  O     . HOH G 4 .   ? 33.985  44.502 -20.119 1.00 24.85  ? 842  HOH A O     1 
HETATM 8441 O  O     . HOH G 4 .   ? 12.052  76.841 -15.300 1.00 49.32  ? 843  HOH A O     1 
HETATM 8442 O  O     . HOH G 4 .   ? -18.168 37.917 2.033   1.00 31.71  ? 844  HOH A O     1 
HETATM 8443 O  O     . HOH G 4 .   ? 11.648  48.134 -10.470 1.00 16.53  ? 845  HOH A O     1 
HETATM 8444 O  O     . HOH G 4 .   ? 16.832  71.815 -13.063 1.00 29.45  ? 846  HOH A O     1 
HETATM 8445 O  O     . HOH G 4 .   ? 11.255  27.239 2.713   1.00 28.70  ? 847  HOH A O     1 
HETATM 8446 O  O     . HOH G 4 .   ? 19.701  38.522 16.182  1.00 30.75  ? 848  HOH A O     1 
HETATM 8447 O  O     . HOH G 4 .   ? -12.004 37.102 -6.131  1.00 20.59  ? 849  HOH A O     1 
HETATM 8448 O  O     . HOH G 4 .   ? -0.454  70.279 -20.754 1.00 35.43  ? 850  HOH A O     1 
HETATM 8449 O  O     . HOH G 4 .   ? 39.768  45.725 -8.553  1.00 29.15  ? 851  HOH A O     1 
HETATM 8450 O  O     . HOH G 4 .   ? -20.310 34.168 0.896   1.00 32.66  ? 852  HOH A O     1 
HETATM 8451 O  O     . HOH G 4 .   ? 26.353  60.330 3.228   1.00 25.65  ? 853  HOH A O     1 
HETATM 8452 O  O     . HOH G 4 .   ? -22.230 47.660 -2.165  1.00 51.17  ? 854  HOH A O     1 
HETATM 8453 O  O     . HOH G 4 .   ? -9.573  35.511 8.162   1.00 30.21  ? 855  HOH A O     1 
HETATM 8454 O  O     . HOH G 4 .   ? 26.226  58.054 9.038   1.00 29.74  ? 856  HOH A O     1 
HETATM 8455 O  O     . HOH G 4 .   ? -9.618  46.112 -4.916  1.00 32.38  ? 857  HOH A O     1 
HETATM 8456 O  O     . HOH G 4 .   ? 11.331  22.763 4.132   1.00 36.06  ? 858  HOH A O     1 
HETATM 8457 O  O     . HOH G 4 .   ? 2.382   47.177 -0.468  1.00 21.50  ? 859  HOH A O     1 
HETATM 8458 O  O     . HOH G 4 .   ? -2.130  38.992 12.610  1.00 49.32  ? 860  HOH A O     1 
HETATM 8459 O  O     . HOH G 4 .   ? 6.835   42.136 -0.806  1.00 15.50  ? 861  HOH A O     1 
HETATM 8460 O  O     . HOH G 4 .   ? 5.771   33.223 5.176   1.00 23.78  ? 862  HOH A O     1 
HETATM 8461 O  O     . HOH G 4 .   ? 10.384  49.157 -8.292  1.00 16.99  ? 863  HOH A O     1 
HETATM 8462 O  O     . HOH G 4 .   ? -5.725  43.877 -9.998  1.00 28.12  ? 864  HOH A O     1 
HETATM 8463 O  O     . HOH G 4 .   ? 4.922   40.415 5.495   1.00 22.47  ? 865  HOH A O     1 
HETATM 8464 O  O     . HOH G 4 .   ? 17.982  48.371 11.014  1.00 24.50  ? 866  HOH A O     1 
HETATM 8465 O  O     . HOH G 4 .   ? -26.314 32.377 -7.325  1.00 32.24  ? 867  HOH A O     1 
HETATM 8466 O  O     . HOH G 4 .   ? 14.411  42.799 -2.665  1.00 21.52  ? 868  HOH A O     1 
HETATM 8467 O  O     . HOH G 4 .   ? -5.882  61.110 6.641   1.00 36.62  ? 869  HOH A O     1 
HETATM 8468 O  O     . HOH G 4 .   ? -10.841 32.931 10.391  1.00 37.37  ? 870  HOH A O     1 
HETATM 8469 O  O     . HOH G 4 .   ? 15.461  42.455 -7.529  1.00 16.38  ? 871  HOH A O     1 
HETATM 8470 O  O     . HOH G 4 .   ? -8.740  39.966 -10.915 1.00 23.84  ? 872  HOH A O     1 
HETATM 8471 O  O     . HOH G 4 .   ? -7.563  54.243 -15.338 1.00 36.53  ? 873  HOH A O     1 
HETATM 8472 O  O     . HOH G 4 .   ? 10.156  27.996 5.015   1.00 29.58  ? 874  HOH A O     1 
HETATM 8473 O  O     . HOH G 4 .   ? -4.523  68.704 -21.416 1.00 36.78  ? 875  HOH A O     1 
HETATM 8474 O  O     . HOH G 4 .   ? 19.551  57.515 13.627  1.00 35.31  ? 876  HOH A O     1 
HETATM 8475 O  O     . HOH G 4 .   ? 8.011   17.136 -8.818  1.00 42.17  ? 877  HOH A O     1 
HETATM 8476 O  O     . HOH G 4 .   ? 3.143   25.745 15.631  1.00 43.02  ? 878  HOH A O     1 
HETATM 8477 O  O     . HOH G 4 .   ? 10.923  29.944 -6.397  1.00 32.33  ? 879  HOH A O     1 
HETATM 8478 O  O     . HOH G 4 .   ? 5.109   37.424 9.165   1.00 28.84  ? 880  HOH A O     1 
HETATM 8479 O  O     . HOH G 4 .   ? 35.495  42.090 -4.542  1.00 31.80  ? 881  HOH A O     1 
HETATM 8480 O  O     . HOH G 4 .   ? 14.535  63.101 4.889   1.00 26.06  ? 882  HOH A O     1 
HETATM 8481 O  O     . HOH G 4 .   ? 6.488   19.505 -9.031  1.00 33.95  ? 883  HOH A O     1 
HETATM 8482 O  O     . HOH G 4 .   ? 41.647  49.714 1.742   1.00 39.28  ? 884  HOH A O     1 
HETATM 8483 O  O     . HOH G 4 .   ? 32.289  32.218 18.722  1.00 50.24  ? 885  HOH A O     1 
HETATM 8484 O  O     . HOH G 4 .   ? 7.324   65.065 -24.302 1.00 20.93  ? 886  HOH A O     1 
HETATM 8485 O  O     . HOH G 4 .   ? 8.665   30.221 -5.264  1.00 22.30  ? 887  HOH A O     1 
HETATM 8486 O  O     . HOH G 4 .   ? -0.645  49.373 -22.778 1.00 37.03  ? 888  HOH A O     1 
HETATM 8487 O  O     . HOH G 4 .   ? 11.467  30.817 17.287  1.00 44.58  ? 889  HOH A O     1 
HETATM 8488 O  O     . HOH G 4 .   ? 38.538  34.196 12.698  1.00 37.71  ? 890  HOH A O     1 
HETATM 8489 O  O     . HOH G 4 .   ? 3.554   36.600 11.545  1.00 38.67  ? 891  HOH A O     1 
HETATM 8490 O  O     . HOH G 4 .   ? -2.700  31.208 -9.876  1.00 36.59  ? 892  HOH A O     1 
HETATM 8491 O  O     . HOH G 4 .   ? 7.071   40.441 -4.288  1.00 17.72  ? 893  HOH A O     1 
HETATM 8492 O  O     . HOH G 4 .   ? 9.134   74.621 -10.010 1.00 35.75  ? 894  HOH A O     1 
HETATM 8493 O  O     . HOH G 4 .   ? -1.286  57.473 -22.621 1.00 28.00  ? 895  HOH A O     1 
HETATM 8494 O  O     . HOH G 4 .   ? 1.105   69.628 -23.579 1.00 34.88  ? 896  HOH A O     1 
HETATM 8495 O  O     . HOH G 4 .   ? 12.070  40.369 18.147  1.00 31.18  ? 897  HOH A O     1 
HETATM 8496 O  O     . HOH G 4 .   ? 24.964  35.028 15.387  1.00 36.12  ? 898  HOH A O     1 
HETATM 8497 O  O     . HOH G 4 .   ? 6.597   39.966 3.290   1.00 19.96  ? 899  HOH A O     1 
HETATM 8498 O  O     . HOH G 4 .   ? -12.519 23.383 11.023  1.00 32.11  ? 900  HOH A O     1 
HETATM 8499 O  O     . HOH G 4 .   ? -15.258 34.677 6.918   1.00 27.43  ? 901  HOH A O     1 
HETATM 8500 O  O     . HOH G 4 .   ? 35.219  45.588 16.171  1.00 42.07  ? 902  HOH A O     1 
HETATM 8501 O  O     . HOH G 4 .   ? -6.001  41.286 6.719   1.00 30.83  ? 903  HOH A O     1 
HETATM 8502 O  O     . HOH G 4 .   ? 17.011  63.478 4.419   1.00 30.62  ? 904  HOH A O     1 
HETATM 8503 O  O     . HOH G 4 .   ? 1.706   78.503 -17.751 1.00 29.71  ? 905  HOH A O     1 
HETATM 8504 O  O     . HOH G 4 .   ? 16.848  50.627 12.648  1.00 27.42  ? 906  HOH A O     1 
HETATM 8505 O  O     . HOH G 4 .   ? 18.934  32.282 18.375  1.00 41.89  ? 907  HOH A O     1 
HETATM 8506 O  O     . HOH G 4 .   ? 7.618   76.662 -16.449 1.00 44.61  ? 908  HOH A O     1 
HETATM 8507 O  O     . HOH G 4 .   ? -5.402  69.921 5.435   1.00 37.42  ? 909  HOH A O     1 
HETATM 8508 O  O     . HOH G 4 .   ? 17.841  53.020 10.997  1.00 26.24  ? 910  HOH A O     1 
HETATM 8509 O  O     . HOH G 4 .   ? -12.477 65.546 -6.435  1.00 36.18  ? 911  HOH A O     1 
HETATM 8510 O  O     . HOH G 4 .   ? 19.324  28.183 1.222   1.00 35.86  ? 912  HOH A O     1 
HETATM 8511 O  O     . HOH G 4 .   ? -6.362  80.063 -8.789  1.00 34.96  ? 913  HOH A O     1 
HETATM 8512 O  O     . HOH G 4 .   ? -5.603  63.892 -17.916 1.00 35.39  ? 914  HOH A O     1 
HETATM 8513 O  O     . HOH G 4 .   ? -7.286  16.732 -7.365  1.00 53.26  ? 915  HOH A O     1 
HETATM 8514 O  O     . HOH G 4 .   ? 14.488  46.871 16.320  1.00 32.08  ? 916  HOH A O     1 
HETATM 8515 O  O     . HOH G 4 .   ? -20.022 17.972 -2.719  1.00 37.59  ? 917  HOH A O     1 
HETATM 8516 O  O     . HOH G 4 .   ? 13.246  44.893 14.546  1.00 27.03  ? 918  HOH A O     1 
HETATM 8517 O  O     . HOH G 4 .   ? 8.583   19.195 12.424  1.00 46.12  ? 919  HOH A O     1 
HETATM 8518 O  O     . HOH G 4 .   ? -12.451 61.983 -8.743  1.00 26.65  ? 920  HOH A O     1 
HETATM 8519 O  O     . HOH G 4 .   ? -11.920 28.571 14.391  1.00 35.99  ? 921  HOH A O     1 
HETATM 8520 O  O     . HOH G 4 .   ? 27.114  45.361 -11.938 1.00 25.73  ? 922  HOH A O     1 
HETATM 8521 O  O     . HOH G 4 .   ? 35.712  46.639 11.857  1.00 47.24  ? 923  HOH A O     1 
HETATM 8522 O  O     . HOH G 4 .   ? 26.359  26.862 11.281  1.00 58.95  ? 924  HOH A O     1 
HETATM 8523 O  O     . HOH G 4 .   ? 29.736  42.626 -18.348 1.00 34.58  ? 925  HOH A O     1 
HETATM 8524 O  O     . HOH G 4 .   ? -4.290  74.419 -16.955 1.00 26.44  ? 926  HOH A O     1 
HETATM 8525 O  O     . HOH G 4 .   ? -6.021  57.163 -16.419 1.00 25.49  ? 927  HOH A O     1 
HETATM 8526 O  O     . HOH G 4 .   ? 33.157  42.109 -5.433  1.00 27.80  ? 928  HOH A O     1 
HETATM 8527 O  O     . HOH G 4 .   ? 28.663  33.537 18.279  1.00 47.76  ? 929  HOH A O     1 
HETATM 8528 O  O     . HOH G 4 .   ? 39.374  35.810 7.686   1.00 36.45  ? 930  HOH A O     1 
HETATM 8529 O  O     . HOH G 4 .   ? -9.398  66.925 -18.220 1.00 36.65  ? 931  HOH A O     1 
HETATM 8530 O  O     . HOH G 4 .   ? 3.328   54.069 -24.924 1.00 40.72  ? 932  HOH A O     1 
HETATM 8531 O  O     . HOH G 4 .   ? -3.179  52.558 1.470   1.00 35.42  ? 933  HOH A O     1 
HETATM 8532 O  O     . HOH G 4 .   ? -2.517  25.798 10.268  1.00 34.33  ? 934  HOH A O     1 
HETATM 8533 O  O     . HOH G 4 .   ? -17.992 41.733 3.462   1.00 50.52  ? 935  HOH A O     1 
HETATM 8534 O  O     . HOH G 4 .   ? 9.042   24.143 8.298   1.00 43.85  ? 936  HOH A O     1 
HETATM 8535 O  O     . HOH G 4 .   ? -1.081  72.495 -22.274 1.00 42.00  ? 937  HOH A O     1 
HETATM 8536 O  O     . HOH G 4 .   ? 3.015   71.134 -27.792 1.00 44.77  ? 938  HOH A O     1 
HETATM 8537 O  O     . HOH G 4 .   ? 34.169  43.137 -15.874 1.00 38.45  ? 939  HOH A O     1 
HETATM 8538 O  O     . HOH G 4 .   ? -18.846 35.436 -13.819 1.00 23.97  ? 940  HOH A O     1 
HETATM 8539 O  O     . HOH G 4 .   ? -8.203  45.849 -2.038  1.00 42.42  ? 941  HOH A O     1 
HETATM 8540 O  O     . HOH G 4 .   ? 38.368  45.129 -11.266 1.00 29.92  ? 942  HOH A O     1 
HETATM 8541 O  O     . HOH G 4 .   ? -1.863  52.036 3.593   1.00 45.47  ? 943  HOH A O     1 
HETATM 8542 O  O     . HOH G 4 .   ? 13.565  25.519 -1.980  1.00 44.95  ? 944  HOH A O     1 
HETATM 8543 O  O     . HOH G 4 .   ? -1.051  42.644 3.901   1.00 28.37  ? 945  HOH A O     1 
HETATM 8544 O  O     . HOH G 4 .   ? 36.029  49.916 7.345   1.00 32.49  ? 946  HOH A O     1 
HETATM 8545 O  O     . HOH G 4 .   ? 39.002  27.383 6.623   1.00 42.31  ? 947  HOH A O     1 
HETATM 8546 O  O     . HOH G 4 .   ? 0.977   26.366 15.622  1.00 44.10  ? 948  HOH A O     1 
HETATM 8547 O  O     . HOH G 4 .   ? -9.061  21.564 13.428  1.00 35.29  ? 949  HOH A O     1 
HETATM 8548 O  O     . HOH G 4 .   ? 18.774  56.991 -12.186 1.00 13.23  ? 950  HOH A O     1 
HETATM 8549 O  O     . HOH G 4 .   ? -15.120 22.781 -13.169 1.00 35.04  ? 951  HOH A O     1 
HETATM 8550 O  O     . HOH G 4 .   ? -24.961 24.680 1.840   1.00 33.26  ? 952  HOH A O     1 
HETATM 8551 O  O     . HOH G 4 .   ? -3.277  24.799 -13.851 1.00 37.71  ? 953  HOH A O     1 
HETATM 8552 O  O     . HOH G 4 .   ? -6.790  15.883 5.555   1.00 44.15  ? 954  HOH A O     1 
HETATM 8553 O  O     . HOH G 4 .   ? 0.802   58.456 9.350   1.00 42.00  ? 955  HOH A O     1 
HETATM 8554 O  O     . HOH G 4 .   ? 11.226  17.680 2.779   1.00 36.03  ? 956  HOH A O     1 
HETATM 8555 O  O     . HOH G 4 .   ? 34.846  49.830 9.539   1.00 34.24  ? 957  HOH A O     1 
HETATM 8556 O  O     . HOH G 4 .   ? -0.960  43.992 7.713   1.00 45.78  ? 958  HOH A O     1 
HETATM 8557 O  O     . HOH G 4 .   ? -0.778  32.255 -12.407 1.00 25.98  ? 959  HOH A O     1 
HETATM 8558 O  O     . HOH G 4 .   ? 0.790   33.186 10.563  1.00 28.98  ? 960  HOH A O     1 
HETATM 8559 O  O     . HOH G 4 .   ? 3.101   44.744 -0.068  1.00 19.67  ? 961  HOH A O     1 
HETATM 8560 O  O     . HOH G 4 .   ? -11.353 24.576 12.994  1.00 33.88  ? 962  HOH A O     1 
HETATM 8561 O  O     . HOH G 4 .   ? -10.717 42.889 -2.226  1.00 26.56  ? 963  HOH A O     1 
HETATM 8562 O  O     . HOH G 4 .   ? -0.156  79.822 -11.940 1.00 31.33  ? 964  HOH A O     1 
HETATM 8563 O  O     . HOH G 4 .   ? 3.828   77.977 -5.024  1.00 55.30  ? 965  HOH A O     1 
HETATM 8564 O  O     . HOH G 4 .   ? -21.184 29.391 4.414   1.00 43.14  ? 966  HOH A O     1 
HETATM 8565 O  O     . HOH G 4 .   ? 15.538  57.366 7.387   1.00 24.00  ? 967  HOH A O     1 
HETATM 8566 O  O     . HOH G 4 .   ? 6.746   73.167 -9.342  1.00 28.36  ? 968  HOH A O     1 
HETATM 8567 O  O     . HOH G 4 .   ? 6.564   63.009 7.979   1.00 31.06  ? 969  HOH A O     1 
HETATM 8568 O  O     . HOH G 4 .   ? -2.683  62.974 -24.267 1.00 49.96  ? 970  HOH A O     1 
HETATM 8569 O  O     . HOH G 4 .   ? -4.633  79.030 -23.747 1.00 43.49  ? 971  HOH A O     1 
HETATM 8570 O  O     . HOH G 4 .   ? -4.182  57.325 -20.394 1.00 31.71  ? 972  HOH A O     1 
HETATM 8571 O  O     . HOH G 4 .   ? -10.169 71.610 -3.886  1.00 30.67  ? 973  HOH A O     1 
HETATM 8572 O  O     . HOH G 4 .   ? 13.197  17.920 -3.759  1.00 37.60  ? 974  HOH A O     1 
HETATM 8573 O  O     . HOH G 4 .   ? -5.976  59.079 -18.748 1.00 40.35  ? 975  HOH A O     1 
HETATM 8574 O  O     . HOH G 4 .   ? 5.803   42.492 9.497   1.00 26.77  ? 976  HOH A O     1 
HETATM 8575 O  O     . HOH G 4 .   ? -9.893  61.577 -17.225 1.00 35.18  ? 977  HOH A O     1 
HETATM 8576 O  O     . HOH G 4 .   ? 8.560   78.415 1.168   1.00 39.39  ? 978  HOH A O     1 
HETATM 8577 O  O     . HOH G 4 .   ? -11.101 65.678 -17.429 1.00 34.88  ? 979  HOH A O     1 
HETATM 8578 O  O     . HOH G 4 .   ? -4.480  46.202 -12.547 1.00 25.94  ? 980  HOH A O     1 
HETATM 8579 O  O     . HOH G 4 .   ? 9.006   19.226 10.114  1.00 42.94  ? 981  HOH A O     1 
HETATM 8580 O  O     . HOH G 4 .   ? 12.659  24.938 2.252   1.00 39.62  ? 982  HOH A O     1 
HETATM 8581 O  O     . HOH G 4 .   ? 4.534   78.376 -18.708 1.00 37.05  ? 983  HOH A O     1 
HETATM 8582 O  O     . HOH G 4 .   ? 31.257  45.737 -13.418 1.00 34.51  ? 984  HOH A O     1 
HETATM 8583 O  O     . HOH G 4 .   ? -1.444  49.405 -17.978 1.00 29.83  ? 985  HOH A O     1 
HETATM 8584 O  O     . HOH G 4 .   ? -10.641 18.479 3.974   1.00 35.31  ? 986  HOH A O     1 
HETATM 8585 O  O     . HOH G 4 .   ? -5.999  66.480 -19.162 1.00 28.80  ? 987  HOH A O     1 
HETATM 8586 O  O     . HOH G 4 .   ? 24.963  30.569 14.493  1.00 35.42  ? 988  HOH A O     1 
HETATM 8587 O  O     . HOH G 4 .   ? 17.429  45.932 19.254  1.00 29.55  ? 989  HOH A O     1 
HETATM 8588 O  O     . HOH G 4 .   ? 0.764   53.780 6.390   1.00 35.08  ? 990  HOH A O     1 
HETATM 8589 O  O     . HOH G 4 .   ? -12.635 53.487 -8.338  1.00 38.52  ? 991  HOH A O     1 
HETATM 8590 O  O     . HOH G 4 .   ? -4.325  41.686 -11.648 1.00 36.68  ? 992  HOH A O     1 
HETATM 8591 O  O     . HOH G 4 .   ? -3.286  79.298 3.916   1.00 56.05  ? 993  HOH A O     1 
HETATM 8592 O  O     . HOH G 4 .   ? 4.310   16.630 4.428   1.00 45.94  ? 994  HOH A O     1 
HETATM 8593 O  O     . HOH G 4 .   ? -20.590 40.375 -11.400 1.00 33.11  ? 995  HOH A O     1 
HETATM 8594 O  O     . HOH G 4 .   ? -8.897  16.565 -9.073  1.00 37.92  ? 996  HOH A O     1 
HETATM 8595 O  O     . HOH G 4 .   ? -17.517 18.982 -7.990  1.00 42.15  ? 997  HOH A O     1 
HETATM 8596 O  O     . HOH G 4 .   ? -0.287  69.496 2.833   1.00 38.87  ? 998  HOH A O     1 
HETATM 8597 O  O     . HOH G 4 .   ? -14.061 75.276 -20.302 1.00 32.61  ? 999  HOH A O     1 
HETATM 8598 O  O     . HOH G 4 .   ? 23.082  39.129 19.828  1.00 42.53  ? 1000 HOH A O     1 
HETATM 8599 O  O     . HOH G 4 .   ? 7.247   41.489 16.668  1.00 37.55  ? 1001 HOH A O     1 
HETATM 8600 O  O     . HOH G 4 .   ? 9.191   51.758 12.869  1.00 28.67  ? 1002 HOH A O     1 
HETATM 8601 O  O     . HOH G 4 .   ? -8.838  14.783 11.663  1.00 39.40  ? 1003 HOH A O     1 
HETATM 8602 O  O     . HOH G 4 .   ? -1.994  70.974 4.567   1.00 38.10  ? 1004 HOH A O     1 
HETATM 8603 O  O     . HOH G 4 .   ? -2.664  42.840 6.884   1.00 36.69  ? 1005 HOH A O     1 
HETATM 8604 O  O     . HOH G 4 .   ? 2.120   36.901 13.971  1.00 43.77  ? 1006 HOH A O     1 
HETATM 8605 O  O     . HOH G 4 .   ? -3.348  57.881 6.935   1.00 39.61  ? 1007 HOH A O     1 
HETATM 8606 O  O     . HOH G 4 .   ? -12.504 77.107 -20.838 1.00 48.55  ? 1008 HOH A O     1 
HETATM 8607 O  O     . HOH G 4 .   ? -19.944 31.411 -13.415 1.00 35.43  ? 1009 HOH A O     1 
HETATM 8608 O  O     . HOH G 4 .   ? -4.276  33.752 -13.359 1.00 31.41  ? 1010 HOH A O     1 
HETATM 8609 O  O     . HOH G 4 .   ? 35.867  62.866 10.053  1.00 43.37  ? 1011 HOH A O     1 
HETATM 8610 O  O     . HOH G 4 .   ? -8.857  43.980 -0.238  1.00 36.81  ? 1012 HOH A O     1 
HETATM 8611 O  O     . HOH G 4 .   ? -2.169  41.500 -14.053 1.00 43.78  ? 1013 HOH A O     1 
HETATM 8612 O  O     . HOH G 4 .   ? -4.330  25.727 -12.029 1.00 36.56  ? 1014 HOH A O     1 
HETATM 8613 O  O     . HOH G 4 .   ? -5.139  38.800 12.509  1.00 38.07  ? 1015 HOH A O     1 
HETATM 8614 O  O     . HOH G 4 .   ? 27.280  29.559 12.735  1.00 50.44  ? 1016 HOH A O     1 
HETATM 8615 O  O     . HOH G 4 .   ? -4.891  54.757 -17.459 1.00 56.68  ? 1017 HOH A O     1 
HETATM 8616 O  O     . HOH G 4 .   ? -1.760  47.279 2.101   1.00 32.26  ? 1018 HOH A O     1 
HETATM 8617 O  O     . HOH G 4 .   ? 38.198  41.552 -1.368  1.00 53.58  ? 1019 HOH A O     1 
HETATM 8618 O  O     . HOH G 4 .   ? 12.209  28.114 13.285  1.00 42.44  ? 1020 HOH A O     1 
HETATM 8619 O  O     . HOH G 4 .   ? -28.961 29.753 -6.747  1.00 51.85  ? 1021 HOH A O     1 
HETATM 8620 O  O     . HOH G 4 .   ? -9.207  18.214 14.012  1.00 43.44  ? 1022 HOH A O     1 
HETATM 8621 O  O     . HOH G 4 .   ? 5.652   78.109 -1.449  1.00 36.18  ? 1023 HOH A O     1 
HETATM 8622 O  O     . HOH G 4 .   ? 14.977  22.965 -1.412  1.00 51.34  ? 1024 HOH A O     1 
HETATM 8623 O  O     . HOH G 4 .   ? -22.768 33.958 -0.832  1.00 31.01  ? 1025 HOH A O     1 
HETATM 8624 O  O     . HOH G 4 .   ? -22.493 25.047 -7.936  1.00 33.77  ? 1026 HOH A O     1 
HETATM 8625 O  O     . HOH G 4 .   ? 34.758  38.254 12.538  1.00 39.01  ? 1027 HOH A O     1 
HETATM 8626 O  O     . HOH G 4 .   ? -12.391 59.118 -7.533  1.00 29.64  ? 1028 HOH A O     1 
HETATM 8627 O  O     . HOH G 4 .   ? 18.578  39.305 18.585  1.00 39.66  ? 1029 HOH A O     1 
HETATM 8628 O  O     . HOH G 4 .   ? 32.890  42.820 -18.293 1.00 35.84  ? 1030 HOH A O     1 
HETATM 8629 O  O     . HOH G 4 .   ? -14.063 54.956 -3.894  1.00 47.30  ? 1031 HOH A O     1 
HETATM 8630 O  O     . HOH G 4 .   ? 17.360  55.328 12.213  1.00 42.53  ? 1032 HOH A O     1 
HETATM 8631 O  O     . HOH G 4 .   ? 10.749  25.386 6.912   1.00 40.30  ? 1033 HOH A O     1 
HETATM 8632 O  O     . HOH G 4 .   ? 8.701   57.370 9.853   1.00 38.14  ? 1034 HOH A O     1 
HETATM 8633 O  O     . HOH G 4 .   ? -7.392  27.021 -15.096 1.00 35.09  ? 1035 HOH A O     1 
HETATM 8634 O  O     . HOH G 4 .   ? 18.158  74.875 -17.342 1.00 41.53  ? 1036 HOH A O     1 
HETATM 8635 O  O     . HOH G 4 .   ? 17.882  73.381 -15.445 1.00 45.47  ? 1037 HOH A O     1 
HETATM 8636 O  O     . HOH G 4 .   ? -4.039  73.348 -19.895 1.00 34.84  ? 1038 HOH A O     1 
HETATM 8637 O  O     . HOH G 4 .   ? -4.353  71.887 5.516   1.00 37.17  ? 1039 HOH A O     1 
HETATM 8638 O  O     . HOH G 4 .   ? -1.925  34.349 -13.339 1.00 32.19  ? 1040 HOH A O     1 
HETATM 8639 O  O     . HOH G 4 .   ? 2.565   27.412 -16.271 1.00 28.54  ? 1041 HOH A O     1 
HETATM 8640 O  O     . HOH G 4 .   ? 36.735  48.416 11.169  1.00 37.19  ? 1042 HOH A O     1 
HETATM 8641 O  O     . HOH G 4 .   ? 0.106   48.065 4.655   1.00 39.34  ? 1043 HOH A O     1 
HETATM 8642 O  O     . HOH G 4 .   ? -7.812  67.931 -19.883 1.00 28.93  ? 1044 HOH A O     1 
HETATM 8643 O  O     . HOH G 4 .   ? 38.313  44.130 -23.414 1.00 40.41  ? 1045 HOH A O     1 
HETATM 8644 O  O     . HOH G 4 .   ? 8.897   66.771 7.759   1.00 45.55  ? 1046 HOH A O     1 
HETATM 8645 O  O     . HOH G 4 .   ? 1.697   46.403 4.559   1.00 45.62  ? 1047 HOH A O     1 
HETATM 8646 O  O     . HOH G 4 .   ? -3.974  60.042 7.769   1.00 49.27  ? 1048 HOH A O     1 
HETATM 8647 O  O     . HOH G 4 .   ? 0.483   46.938 2.780   1.00 30.14  ? 1049 HOH A O     1 
HETATM 8648 O  O     . HOH G 4 .   ? 9.231   75.680 -14.381 1.00 37.02  ? 1050 HOH A O     1 
HETATM 8649 O  O     . HOH G 4 .   ? -12.026 57.420 -9.024  1.00 27.87  ? 1051 HOH A O     1 
HETATM 8650 O  O     . HOH G 4 .   ? 15.766  42.720 16.664  1.00 25.87  ? 1052 HOH A O     1 
HETATM 8651 O  O     . HOH G 4 .   ? 12.879  34.086 16.659  1.00 33.70  ? 1053 HOH A O     1 
HETATM 8652 O  O     . HOH G 4 .   ? -13.822 21.519 -9.554  1.00 32.56  ? 1054 HOH A O     1 
HETATM 8653 O  O     . HOH G 4 .   ? -0.133  71.662 -24.663 1.00 45.01  ? 1055 HOH A O     1 
HETATM 8654 O  O     . HOH G 4 .   ? -15.808 44.100 2.405   1.00 43.52  ? 1056 HOH A O     1 
HETATM 8655 O  O     . HOH G 4 .   ? 35.234  65.518 8.688   1.00 47.33  ? 1057 HOH A O     1 
HETATM 8656 O  O     . HOH G 4 .   ? 35.099  47.239 18.290  1.00 44.29  ? 1058 HOH A O     1 
HETATM 8657 O  O     . HOH G 4 .   ? 13.972  60.954 6.093   1.00 27.12  ? 1059 HOH A O     1 
HETATM 8658 O  O     . HOH G 4 .   ? -8.067  72.634 -19.909 1.00 36.10  ? 1060 HOH A O     1 
HETATM 8659 O  O     . HOH G 4 .   ? 36.812  49.648 15.607  1.00 39.68  ? 1061 HOH A O     1 
HETATM 8660 O  O     . HOH G 4 .   ? 12.250  23.929 6.065   1.00 43.00  ? 1062 HOH A O     1 
HETATM 8661 O  O     . HOH G 4 .   ? 10.718  18.166 -13.387 1.00 39.05  ? 1063 HOH A O     1 
HETATM 8662 O  O     . HOH G 4 .   ? -14.164 49.509 -11.919 1.00 35.20  ? 1064 HOH A O     1 
HETATM 8663 O  O     . HOH G 4 .   ? 13.106  32.164 14.842  1.00 35.89  ? 1065 HOH A O     1 
HETATM 8664 O  O     . HOH G 4 .   ? 21.934  37.288 19.863  1.00 48.22  ? 1066 HOH A O     1 
HETATM 8665 O  O     . HOH G 4 .   ? 15.945  61.182 8.442   1.00 31.64  ? 1067 HOH A O     1 
HETATM 8666 O  O     . HOH G 4 .   ? 9.346   17.187 -11.061 1.00 40.18  ? 1068 HOH A O     1 
HETATM 8667 O  O     . HOH G 4 .   ? 10.522  45.484 15.652  1.00 29.50  ? 1069 HOH A O     1 
HETATM 8668 O  O     . HOH G 4 .   ? 21.817  37.738 17.512  1.00 35.37  ? 1070 HOH A O     1 
HETATM 8669 O  O     . HOH G 4 .   ? -11.325 36.632 6.062   1.00 28.63  ? 1071 HOH A O     1 
HETATM 8670 O  O     . HOH G 4 .   ? 32.593  39.217 19.470  1.00 43.33  ? 1072 HOH A O     1 
HETATM 8671 O  O     . HOH G 4 .   ? 0.945   13.611 4.209   1.00 42.44  ? 1073 HOH A O     1 
HETATM 8672 O  O     . HOH G 4 .   ? 18.979  36.175 -12.155 1.00 50.08  ? 1074 HOH A O     1 
HETATM 8673 O  O     . HOH G 4 .   ? -3.123  28.739 -13.429 1.00 37.97  ? 1075 HOH A O     1 
HETATM 8674 O  O     . HOH G 4 .   ? -20.396 33.219 3.205   1.00 42.52  ? 1076 HOH A O     1 
HETATM 8675 O  O     . HOH G 4 .   ? -0.971  57.193 7.901   1.00 40.21  ? 1077 HOH A O     1 
HETATM 8676 O  O     . HOH G 4 .   ? -12.599 44.643 -0.983  1.00 35.38  ? 1078 HOH A O     1 
HETATM 8677 O  O     . HOH G 4 .   ? 26.869  42.646 22.002  1.00 48.17  ? 1079 HOH A O     1 
HETATM 8678 O  O     . HOH G 4 .   ? -11.631 55.781 -13.770 1.00 39.02  ? 1080 HOH A O     1 
HETATM 8679 O  O     . HOH G 4 .   ? 31.721  30.194 17.602  1.00 50.81  ? 1081 HOH A O     1 
HETATM 8680 O  O     . HOH G 4 .   ? -4.268  81.724 3.401   1.00 49.70  ? 1082 HOH A O     1 
HETATM 8681 O  O     . HOH G 4 .   ? -16.821 23.191 -15.583 1.00 37.54  ? 1083 HOH A O     1 
HETATM 8682 O  O     . HOH G 4 .   ? 1.157   56.553 -27.209 1.00 32.61  ? 1084 HOH A O     1 
HETATM 8683 O  O     . HOH G 4 .   ? 11.725  38.047 19.420  1.00 47.60  ? 1085 HOH A O     1 
HETATM 8684 O  O     . HOH G 4 .   ? -6.472  42.003 -11.577 1.00 28.97  ? 1086 HOH A O     1 
HETATM 8685 O  O     . HOH G 4 .   ? 12.011  27.828 15.814  1.00 39.74  ? 1087 HOH A O     1 
HETATM 8686 O  O     . HOH G 4 .   ? 6.647   50.165 10.886  1.00 33.48  ? 1088 HOH A O     1 
HETATM 8687 O  O     . HOH G 4 .   ? 17.470  63.985 8.598   1.00 47.77  ? 1089 HOH A O     1 
HETATM 8688 O  O     . HOH G 4 .   ? 6.812   36.924 18.268  1.00 47.94  ? 1090 HOH A O     1 
HETATM 8689 O  O     . HOH G 4 .   ? 36.331  50.626 12.982  1.00 38.66  ? 1091 HOH A O     1 
HETATM 8690 O  O     . HOH G 4 .   ? -0.558  30.686 -14.602 1.00 26.25  ? 1092 HOH A O     1 
HETATM 8691 O  O     . HOH G 4 .   ? -20.560 23.582 -9.041  1.00 33.95  ? 1093 HOH A O     1 
HETATM 8692 O  O     . HOH G 4 .   ? 8.668   42.944 18.155  1.00 38.05  ? 1094 HOH A O     1 
HETATM 8693 O  O     . HOH G 4 .   ? 2.930   35.909 16.942  1.00 49.59  ? 1095 HOH A O     1 
HETATM 8694 O  O     . HOH G 4 .   ? -13.568 36.421 7.849   1.00 39.85  ? 1096 HOH A O     1 
HETATM 8695 O  O     . HOH G 4 .   ? -12.039 35.036 9.633   1.00 35.02  ? 1097 HOH A O     1 
HETATM 8696 O  O     . HOH G 4 .   ? -6.908  82.315 -7.470  1.00 35.92  ? 1098 HOH A O     1 
HETATM 8697 O  O     . HOH G 4 .   ? -18.308 53.158 -2.785  1.00 45.83  ? 1099 HOH A O     1 
HETATM 8698 O  O     . HOH G 4 .   ? 9.818   39.392 19.514  1.00 49.13  ? 1100 HOH A O     1 
HETATM 8699 O  O     . HOH G 4 .   ? -3.301  24.140 -16.612 1.00 42.77  ? 1101 HOH A O     1 
HETATM 8700 O  O     . HOH G 4 .   ? -4.599  22.611 -17.716 1.00 47.36  ? 1102 HOH A O     1 
HETATM 8701 O  O     . HOH G 4 .   ? -21.085 27.083 -11.554 1.00 41.53  ? 1103 HOH A O     1 
HETATM 8702 O  O     . HOH G 4 .   ? -19.347 25.072 -11.194 1.00 30.17  ? 1104 HOH A O     1 
HETATM 8703 O  O     . HOH G 4 .   ? -14.144 55.613 -7.622  1.00 39.77  ? 1105 HOH A O     1 
HETATM 8704 O  O     . HOH G 4 .   ? 19.345  59.922 14.832  1.00 51.08  ? 1106 HOH A O     1 
HETATM 8705 O  O     . HOH G 4 .   ? -17.249 53.971 -4.768  1.00 43.70  ? 1107 HOH A O     1 
HETATM 8706 O  O     . HOH G 4 .   ? 40.707  44.079 -22.382 1.00 46.15  ? 1108 HOH A O     1 
HETATM 8707 O  O     . HOH G 4 .   ? -8.597  82.226 -5.007  1.00 38.07  ? 1109 HOH A O     1 
HETATM 8708 O  O     . HOH G 4 .   ? 0.000   55.949 -28.925 0.50 35.90  ? 1110 HOH A O     1 
HETATM 8709 O  O     . HOH G 4 .   ? -5.625  26.190 -17.426 1.00 45.10  ? 1111 HOH A O     1 
HETATM 8710 O  O     . HOH G 4 .   ? 11.791  76.397 -33.461 1.00 47.95  ? 1112 HOH A O     1 
HETATM 8711 O  O     . HOH G 4 .   ? -18.909 22.612 -14.202 1.00 40.71  ? 1113 HOH A O     1 
HETATM 8712 O  O     . HOH G 4 .   ? 0.862   11.295 6.034   1.00 53.20  ? 1114 HOH A O     1 
HETATM 8713 O  O     . HOH G 4 .   ? 1.463   11.076 8.447   1.00 53.73  ? 1115 HOH A O     1 
HETATM 8714 O  O     . HOH G 4 .   ? -20.865 24.018 -13.715 1.00 33.53  ? 1116 HOH A O     1 
HETATM 8715 O  O     . HOH G 4 .   ? -5.488  27.344 -19.396 1.00 50.63  ? 1117 HOH A O     1 
HETATM 8716 O  O     . HOH G 4 .   ? 14.345  64.819 12.807  1.00 47.11  ? 1118 HOH A O     1 
HETATM 8717 O  O     . HOH H 4 .   ? 22.131  92.172 -30.486 1.00 36.71  ? 701  HOH B O     1 
HETATM 8718 O  O     . HOH H 4 .   ? 46.922  76.007 -15.709 1.00 39.69  ? 702  HOH B O     1 
HETATM 8719 O  O     . HOH H 4 .   ? 53.592  71.980 -10.531 1.00 48.83  ? 703  HOH B O     1 
HETATM 8720 O  O     . HOH H 4 .   ? 29.146  66.852 -52.332 1.00 39.85  ? 704  HOH B O     1 
HETATM 8721 O  O     . HOH H 4 .   ? 31.606  45.158 -40.520 1.00 29.51  ? 705  HOH B O     1 
HETATM 8722 O  O     . HOH H 4 .   ? 32.149  41.671 -38.056 1.00 37.12  ? 706  HOH B O     1 
HETATM 8723 O  O     . HOH H 4 .   ? 22.790  73.149 -3.889  1.00 48.28  ? 707  HOH B O     1 
HETATM 8724 O  O     . HOH H 4 .   ? 30.397  36.770 -35.185 1.00 41.37  ? 708  HOH B O     1 
HETATM 8725 O  O     . HOH H 4 .   ? 39.302  71.793 -41.761 1.00 46.07  ? 709  HOH B O     1 
HETATM 8726 O  O     . HOH H 4 .   ? 39.790  88.359 -13.932 1.00 48.52  ? 710  HOH B O     1 
HETATM 8727 O  O     . HOH H 4 .   ? 9.638   75.785 1.347   1.00 44.39  ? 711  HOH B O     1 
HETATM 8728 O  O     . HOH H 4 .   ? 9.631   29.227 -21.148 1.00 45.18  ? 712  HOH B O     1 
HETATM 8729 O  O     . HOH H 4 .   ? 28.335  80.025 -58.087 1.00 40.07  ? 713  HOH B O     1 
HETATM 8730 O  O     . HOH H 4 .   ? 27.195  70.499 -53.676 1.00 53.56  ? 714  HOH B O     1 
HETATM 8731 O  O     . HOH H 4 .   ? 27.764  85.145 -57.850 0.50 38.86  ? 715  HOH B O     1 
HETATM 8732 O  O     . HOH H 4 .   ? 34.785  40.324 -29.293 1.00 30.24  ? 716  HOH B O     1 
HETATM 8733 O  O     . HOH H 4 .   ? 43.596  78.655 -36.260 1.00 44.11  ? 717  HOH B O     1 
HETATM 8734 O  O     . HOH H 4 .   ? 5.431   39.150 -28.958 1.00 36.10  ? 718  HOH B O     1 
HETATM 8735 O  O     . HOH H 4 .   ? 32.616  68.635 1.630   1.00 36.71  ? 719  HOH B O     1 
HETATM 8736 O  O     . HOH H 4 .   ? 33.563  83.370 -5.252  1.00 42.42  ? 720  HOH B O     1 
HETATM 8737 O  O     . HOH H 4 .   ? 14.860  58.253 -42.483 1.00 32.71  ? 721  HOH B O     1 
HETATM 8738 O  O     . HOH H 4 .   ? 28.500  71.752 -12.065 1.00 31.80  ? 722  HOH B O     1 
HETATM 8739 O  O     . HOH H 4 .   ? 45.342  54.824 -13.066 1.00 28.51  ? 723  HOH B O     1 
HETATM 8740 O  O     . HOH H 4 .   ? 37.355  78.080 -3.119  1.00 35.01  ? 724  HOH B O     1 
HETATM 8741 O  O     . HOH H 4 .   ? 43.514  81.672 -18.274 1.00 34.46  ? 725  HOH B O     1 
HETATM 8742 O  O     . HOH H 4 .   ? 20.498  73.078 -59.674 1.00 29.74  ? 726  HOH B O     1 
HETATM 8743 O  O     . HOH H 4 .   ? 17.076  85.895 -51.880 1.00 24.29  ? 727  HOH B O     1 
HETATM 8744 O  O     . HOH H 4 .   ? 14.083  27.781 -37.663 1.00 29.13  ? 728  HOH B O     1 
HETATM 8745 O  O     . HOH H 4 .   ? 43.042  51.746 -12.345 1.00 27.44  ? 729  HOH B O     1 
HETATM 8746 O  O     . HOH H 4 .   ? 28.726  95.133 -37.062 1.00 38.93  ? 730  HOH B O     1 
HETATM 8747 O  O     . HOH H 4 .   ? 7.401   36.954 -44.305 1.00 40.35  ? 731  HOH B O     1 
HETATM 8748 O  O     . HOH H 4 .   ? 41.651  50.916 -21.463 1.00 30.40  ? 732  HOH B O     1 
HETATM 8749 O  O     . HOH H 4 .   ? 25.704  61.308 -41.400 1.00 54.64  ? 733  HOH B O     1 
HETATM 8750 O  O     . HOH H 4 .   ? 39.831  69.065 -35.595 1.00 38.90  ? 734  HOH B O     1 
HETATM 8751 O  O     . HOH H 4 .   ? 17.146  66.747 -2.607  1.00 33.52  ? 735  HOH B O     1 
HETATM 8752 O  O     . HOH H 4 .   ? 38.079  73.552 -31.096 1.00 28.82  ? 736  HOH B O     1 
HETATM 8753 O  O     . HOH H 4 .   ? 45.842  52.269 -19.745 1.00 32.79  ? 737  HOH B O     1 
HETATM 8754 O  O     . HOH H 4 .   ? 55.271  68.324 -5.198  1.00 55.39  ? 738  HOH B O     1 
HETATM 8755 O  O     . HOH H 4 .   ? 18.881  90.983 -34.758 1.00 39.09  ? 739  HOH B O     1 
HETATM 8756 O  O     . HOH H 4 .   ? 18.263  78.181 -36.718 1.00 29.90  ? 740  HOH B O     1 
HETATM 8757 O  O     . HOH H 4 .   ? 25.450  73.854 -3.251  1.00 46.80  ? 741  HOH B O     1 
HETATM 8758 O  O     . HOH H 4 .   ? 27.250  69.342 -12.570 1.00 22.17  ? 742  HOH B O     1 
HETATM 8759 O  O     . HOH H 4 .   ? 12.605  71.912 -52.473 1.00 38.61  ? 743  HOH B O     1 
HETATM 8760 O  O     . HOH H 4 .   ? 13.814  79.585 -37.862 1.00 31.33  ? 744  HOH B O     1 
HETATM 8761 O  O     . HOH H 4 .   ? 22.901  64.135 -6.404  1.00 25.70  ? 745  HOH B O     1 
HETATM 8762 O  O     . HOH H 4 .   ? 28.532  63.581 -14.295 1.00 17.54  ? 746  HOH B O     1 
HETATM 8763 O  O     . HOH H 4 .   ? 20.440  72.893 -20.175 1.00 29.23  ? 747  HOH B O     1 
HETATM 8764 O  O     . HOH H 4 .   ? 21.646  60.595 -14.472 1.00 16.08  ? 748  HOH B O     1 
HETATM 8765 O  O     . HOH H 4 .   ? 31.409  64.836 -32.027 1.00 21.22  ? 749  HOH B O     1 
HETATM 8766 O  O     . HOH H 4 .   ? 8.427   81.696 -43.057 1.00 32.82  ? 750  HOH B O     1 
HETATM 8767 O  O     . HOH H 4 .   ? 33.955  49.970 -37.366 1.00 31.46  ? 751  HOH B O     1 
HETATM 8768 O  O     . HOH H 4 .   ? 29.928  81.743 -17.749 1.00 51.81  ? 752  HOH B O     1 
HETATM 8769 O  O     . HOH H 4 .   ? 37.577  40.242 -38.960 1.00 47.49  ? 753  HOH B O     1 
HETATM 8770 O  O     . HOH H 4 .   ? 25.960  57.277 -52.582 1.00 50.40  ? 754  HOH B O     1 
HETATM 8771 O  O     . HOH H 4 .   ? 21.479  67.827 -56.927 1.00 34.22  ? 755  HOH B O     1 
HETATM 8772 O  O     . HOH H 4 .   ? 30.191  77.168 -7.121  1.00 45.98  ? 756  HOH B O     1 
HETATM 8773 O  O     . HOH H 4 .   ? 34.121  73.877 -46.666 1.00 30.40  ? 757  HOH B O     1 
HETATM 8774 O  O     . HOH H 4 .   ? 51.121  76.646 -8.615  1.00 36.21  ? 758  HOH B O     1 
HETATM 8775 O  O     . HOH H 4 .   ? 38.080  64.045 -0.454  1.00 25.64  ? 759  HOH B O     1 
HETATM 8776 O  O     . HOH H 4 .   ? 19.684  64.828 -37.482 1.00 23.08  ? 760  HOH B O     1 
HETATM 8777 O  O     . HOH H 4 .   ? 29.541  51.433 -29.044 1.00 19.10  ? 761  HOH B O     1 
HETATM 8778 O  O     . HOH H 4 .   ? 45.407  66.700 -25.563 1.00 25.93  ? 762  HOH B O     1 
HETATM 8779 O  O     . HOH H 4 .   ? 29.103  71.474 -8.257  1.00 27.53  ? 763  HOH B O     1 
HETATM 8780 O  O     . HOH H 4 .   ? 20.658  88.958 -27.512 1.00 34.50  ? 764  HOH B O     1 
HETATM 8781 O  O     . HOH H 4 .   ? 17.828  38.830 -18.046 1.00 22.33  ? 765  HOH B O     1 
HETATM 8782 O  O     . HOH H 4 .   ? 34.670  56.108 -35.776 1.00 38.96  ? 766  HOH B O     1 
HETATM 8783 O  O     . HOH H 4 .   ? 19.916  92.288 -41.634 1.00 31.53  ? 767  HOH B O     1 
HETATM 8784 O  O     . HOH H 4 .   ? 35.369  46.853 -36.108 1.00 29.42  ? 768  HOH B O     1 
HETATM 8785 O  O     . HOH H 4 .   ? 28.953  64.871 -1.950  1.00 26.58  ? 769  HOH B O     1 
HETATM 8786 O  O     . HOH H 4 .   ? 21.108  33.282 -45.506 1.00 26.49  ? 770  HOH B O     1 
HETATM 8787 O  O     . HOH H 4 .   ? 22.870  62.969 -25.689 1.00 17.82  ? 771  HOH B O     1 
HETATM 8788 O  O     . HOH H 4 .   ? 34.751  53.739 -36.439 1.00 38.36  ? 772  HOH B O     1 
HETATM 8789 O  O     . HOH H 4 .   ? 45.642  76.298 -23.196 1.00 30.58  ? 773  HOH B O     1 
HETATM 8790 O  O     . HOH H 4 .   ? 12.041  50.027 -24.308 1.00 18.43  ? 774  HOH B O     1 
HETATM 8791 O  O     . HOH H 4 .   ? 1.475   48.316 -24.700 1.00 27.92  ? 775  HOH B O     1 
HETATM 8792 O  O     . HOH H 4 .   ? 39.033  52.080 -22.201 1.00 24.66  ? 776  HOH B O     1 
HETATM 8793 O  O     . HOH H 4 .   ? 51.315  62.974 -11.492 1.00 28.50  ? 777  HOH B O     1 
HETATM 8794 O  O     . HOH H 4 .   ? 25.004  29.762 -41.643 1.00 30.46  ? 778  HOH B O     1 
HETATM 8795 O  O     . HOH H 4 .   ? 45.254  61.918 -15.258 1.00 24.65  ? 779  HOH B O     1 
HETATM 8796 O  O     . HOH H 4 .   ? 35.568  41.104 -40.580 1.00 43.92  ? 780  HOH B O     1 
HETATM 8797 O  O     . HOH H 4 .   ? 15.287  52.609 -25.919 1.00 17.20  ? 781  HOH B O     1 
HETATM 8798 O  O     . HOH H 4 .   ? 9.260   61.208 -31.262 1.00 23.96  ? 782  HOH B O     1 
HETATM 8799 O  O     . HOH H 4 .   ? 43.076  78.402 -26.743 1.00 33.95  ? 783  HOH B O     1 
HETATM 8800 O  O     . HOH H 4 .   ? -0.795  44.963 -18.189 1.00 25.62  ? 784  HOH B O     1 
HETATM 8801 O  O     . HOH H 4 .   ? 36.128  52.033 -36.851 1.00 56.63  ? 785  HOH B O     1 
HETATM 8802 O  O     . HOH H 4 .   ? 21.797  74.245 -31.502 1.00 21.94  ? 786  HOH B O     1 
HETATM 8803 O  O     . HOH H 4 .   ? 51.619  64.236 -16.144 1.00 30.03  ? 787  HOH B O     1 
HETATM 8804 O  O     . HOH H 4 .   ? 46.841  51.107 -6.156  1.00 37.42  ? 788  HOH B O     1 
HETATM 8805 O  O     . HOH H 4 .   ? 28.830  69.120 -27.430 1.00 21.95  ? 789  HOH B O     1 
HETATM 8806 O  O     . HOH H 4 .   ? 26.988  61.209 -35.613 1.00 24.19  ? 790  HOH B O     1 
HETATM 8807 O  O     . HOH H 4 .   ? 19.550  49.197 -13.939 1.00 13.46  ? 791  HOH B O     1 
HETATM 8808 O  O     . HOH H 4 .   ? 31.498  38.642 -38.290 1.00 35.30  ? 792  HOH B O     1 
HETATM 8809 O  O     . HOH H 4 .   ? 49.128  74.617 -14.537 1.00 34.35  ? 793  HOH B O     1 
HETATM 8810 O  O     . HOH H 4 .   ? 13.091  53.280 -41.263 1.00 22.77  ? 794  HOH B O     1 
HETATM 8811 O  O     . HOH H 4 .   ? 11.579  54.626 -39.251 1.00 28.12  ? 795  HOH B O     1 
HETATM 8812 O  O     . HOH H 4 .   ? 4.010   37.725 -18.545 1.00 19.16  ? 796  HOH B O     1 
HETATM 8813 O  O     . HOH H 4 .   ? 4.589   42.398 -19.659 1.00 18.54  ? 797  HOH B O     1 
HETATM 8814 O  O     . HOH H 4 .   ? 32.058  78.576 -29.588 1.00 25.28  ? 798  HOH B O     1 
HETATM 8815 O  O     . HOH H 4 .   ? 41.567  49.869 -2.696  1.00 30.82  ? 799  HOH B O     1 
HETATM 8816 O  O     . HOH H 4 .   ? 42.824  60.745 -20.598 1.00 24.11  ? 800  HOH B O     1 
HETATM 8817 O  O     . HOH H 4 .   ? 9.159   44.717 -36.375 1.00 39.49  ? 801  HOH B O     1 
HETATM 8818 O  O     . HOH H 4 .   ? 13.709  83.815 -49.701 1.00 26.16  ? 802  HOH B O     1 
HETATM 8819 O  O     . HOH H 4 .   ? 16.467  34.522 -40.344 1.00 23.02  ? 803  HOH B O     1 
HETATM 8820 O  O     . HOH H 4 .   ? 24.689  30.981 -46.257 1.00 30.91  ? 804  HOH B O     1 
HETATM 8821 O  O     . HOH H 4 .   ? 33.354  75.895 -53.540 1.00 36.46  ? 805  HOH B O     1 
HETATM 8822 O  O     . HOH H 4 .   ? 32.156  68.793 -49.782 1.00 39.94  ? 806  HOH B O     1 
HETATM 8823 O  O     . HOH H 4 .   ? 30.158  85.182 -25.490 1.00 32.46  ? 807  HOH B O     1 
HETATM 8824 O  O     . HOH H 4 .   ? -1.025  41.270 -23.747 1.00 36.19  ? 808  HOH B O     1 
HETATM 8825 O  O     . HOH H 4 .   ? 13.607  78.605 -30.079 1.00 31.21  ? 809  HOH B O     1 
HETATM 8826 O  O     . HOH H 4 .   ? 34.534  75.791 -31.250 1.00 24.92  ? 810  HOH B O     1 
HETATM 8827 O  O     . HOH H 4 .   ? 16.597  64.361 1.933   1.00 28.68  ? 811  HOH B O     1 
HETATM 8828 O  O     . HOH H 4 .   ? 37.695  79.135 -36.339 1.00 30.67  ? 812  HOH B O     1 
HETATM 8829 O  O     . HOH H 4 .   ? 15.857  70.532 -31.921 1.00 21.39  ? 813  HOH B O     1 
HETATM 8830 O  O     . HOH H 4 .   ? 39.804  82.593 -41.385 1.00 39.61  ? 814  HOH B O     1 
HETATM 8831 O  O     . HOH H 4 .   ? 8.964   26.201 -26.967 1.00 53.14  ? 815  HOH B O     1 
HETATM 8832 O  O     . HOH H 4 .   ? 17.741  81.544 -63.894 1.00 27.48  ? 816  HOH B O     1 
HETATM 8833 O  O     . HOH H 4 .   ? 21.340  62.521 -43.837 1.00 32.47  ? 817  HOH B O     1 
HETATM 8834 O  O     . HOH H 4 .   ? 19.304  42.961 -46.170 1.00 26.53  ? 818  HOH B O     1 
HETATM 8835 O  O     . HOH H 4 .   ? 31.355  66.476 -29.884 1.00 21.06  ? 819  HOH B O     1 
HETATM 8836 O  O     . HOH H 4 .   ? 26.202  68.181 -20.196 1.00 20.69  ? 820  HOH B O     1 
HETATM 8837 O  O     . HOH H 4 .   ? 2.264   80.532 -12.215 1.00 46.36  ? 821  HOH B O     1 
HETATM 8838 O  O     . HOH H 4 .   ? 28.894  32.168 -35.223 1.00 37.98  ? 822  HOH B O     1 
HETATM 8839 O  O     . HOH H 4 .   ? 5.936   50.973 -31.795 1.00 24.22  ? 823  HOH B O     1 
HETATM 8840 O  O     . HOH H 4 .   ? 16.688  46.486 -45.671 1.00 23.33  ? 824  HOH B O     1 
HETATM 8841 O  O     . HOH H 4 .   ? 15.866  30.121 -40.981 1.00 23.90  ? 825  HOH B O     1 
HETATM 8842 O  O     . HOH H 4 .   ? 19.440  71.542 -45.903 1.00 22.28  ? 826  HOH B O     1 
HETATM 8843 O  O     . HOH H 4 .   ? 14.815  73.614 4.003   1.00 49.70  ? 827  HOH B O     1 
HETATM 8844 O  O     . HOH H 4 .   ? 38.530  52.944 -30.689 1.00 37.36  ? 828  HOH B O     1 
HETATM 8845 O  O     . HOH H 4 .   ? 40.733  41.506 -33.349 1.00 38.44  ? 829  HOH B O     1 
HETATM 8846 O  O     . HOH H 4 .   ? 17.287  64.550 -38.879 1.00 36.34  ? 830  HOH B O     1 
HETATM 8847 O  O     . HOH H 4 .   ? 8.505   72.589 -49.566 1.00 31.24  ? 831  HOH B O     1 
HETATM 8848 O  O     . HOH H 4 .   ? 36.647  50.406 -21.999 1.00 21.99  ? 832  HOH B O     1 
HETATM 8849 O  O     . HOH H 4 .   ? 11.427  44.575 -25.565 1.00 17.47  ? 833  HOH B O     1 
HETATM 8850 O  O     . HOH H 4 .   ? 20.702  44.481 -19.288 1.00 14.26  ? 834  HOH B O     1 
HETATM 8851 O  O     . HOH H 4 .   ? 28.000  44.466 -16.690 1.00 24.64  ? 835  HOH B O     1 
HETATM 8852 O  O     . HOH H 4 .   ? 16.108  32.461 -20.637 1.00 47.07  ? 836  HOH B O     1 
HETATM 8853 O  O     . HOH H 4 .   ? 36.405  83.642 -22.498 1.00 38.34  ? 837  HOH B O     1 
HETATM 8854 O  O     . HOH H 4 .   ? 50.364  61.580 -15.195 1.00 29.17  ? 838  HOH B O     1 
HETATM 8855 O  O     . HOH H 4 .   ? 18.833  37.720 -27.438 1.00 19.67  ? 839  HOH B O     1 
HETATM 8856 O  O     . HOH H 4 .   ? 15.236  80.614 -58.991 1.00 30.26  ? 840  HOH B O     1 
HETATM 8857 O  O     . HOH H 4 .   ? 8.665   45.009 -25.419 1.00 20.36  ? 841  HOH B O     1 
HETATM 8858 O  O     . HOH H 4 .   ? 14.445  75.907 -60.031 1.00 26.65  ? 842  HOH B O     1 
HETATM 8859 O  O     . HOH H 4 .   ? 55.346  54.354 -13.926 1.00 38.15  ? 843  HOH B O     1 
HETATM 8860 O  O     . HOH H 4 .   ? 32.549  84.581 -31.897 1.00 27.59  ? 844  HOH B O     1 
HETATM 8861 O  O     . HOH H 4 .   ? 14.737  67.433 -53.571 1.00 32.92  ? 845  HOH B O     1 
HETATM 8862 O  O     . HOH H 4 .   ? 20.834  79.364 -61.127 1.00 28.65  ? 846  HOH B O     1 
HETATM 8863 O  O     . HOH H 4 .   ? 40.903  56.730 -3.762  1.00 26.36  ? 847  HOH B O     1 
HETATM 8864 O  O     . HOH H 4 .   ? 48.380  68.851 -27.940 1.00 36.61  ? 848  HOH B O     1 
HETATM 8865 O  O     . HOH H 4 .   ? 21.117  87.693 -20.229 1.00 49.09  ? 849  HOH B O     1 
HETATM 8866 O  O     . HOH H 4 .   ? 46.451  69.967 -33.756 1.00 41.72  ? 850  HOH B O     1 
HETATM 8867 O  O     . HOH H 4 .   ? 37.117  50.271 -37.010 1.00 39.25  ? 851  HOH B O     1 
HETATM 8868 O  O     . HOH H 4 .   ? 24.572  69.915 0.890   1.00 40.84  ? 852  HOH B O     1 
HETATM 8869 O  O     . HOH H 4 .   ? 24.996  78.725 -26.209 1.00 24.97  ? 853  HOH B O     1 
HETATM 8870 O  O     . HOH H 4 .   ? 31.362  74.156 -52.234 1.00 30.18  ? 854  HOH B O     1 
HETATM 8871 O  O     . HOH H 4 .   ? 13.552  77.456 -19.492 1.00 38.52  ? 855  HOH B O     1 
HETATM 8872 O  O     . HOH H 4 .   ? 14.453  81.989 -33.114 1.00 35.36  ? 856  HOH B O     1 
HETATM 8873 O  O     . HOH H 4 .   ? 22.102  56.277 -25.186 1.00 17.59  ? 857  HOH B O     1 
HETATM 8874 O  O     . HOH H 4 .   ? 48.317  61.804 -13.624 1.00 28.65  ? 858  HOH B O     1 
HETATM 8875 O  O     . HOH H 4 .   ? 12.457  29.266 -33.235 1.00 30.12  ? 859  HOH B O     1 
HETATM 8876 O  O     . HOH H 4 .   ? 35.298  65.192 0.320   1.00 26.88  ? 860  HOH B O     1 
HETATM 8877 O  O     . HOH H 4 .   ? 37.006  83.051 -53.347 1.00 42.03  ? 861  HOH B O     1 
HETATM 8878 O  O     . HOH H 4 .   ? 29.066  66.050 -21.001 1.00 20.59  ? 862  HOH B O     1 
HETATM 8879 O  O     . HOH H 4 .   ? 32.095  50.970 -43.313 1.00 35.58  ? 863  HOH B O     1 
HETATM 8880 O  O     . HOH H 4 .   ? 43.249  75.252 -36.448 1.00 35.97  ? 864  HOH B O     1 
HETATM 8881 O  O     . HOH H 4 .   ? 36.270  45.803 -22.745 1.00 25.82  ? 865  HOH B O     1 
HETATM 8882 O  O     . HOH H 4 .   ? 46.746  64.402 -2.433  1.00 27.09  ? 866  HOH B O     1 
HETATM 8883 O  O     . HOH H 4 .   ? 38.830  48.822 -25.890 1.00 28.26  ? 867  HOH B O     1 
HETATM 8884 O  O     . HOH H 4 .   ? 8.871   47.128 -40.309 1.00 45.18  ? 868  HOH B O     1 
HETATM 8885 O  O     . HOH H 4 .   ? 42.878  53.554 -14.053 1.00 25.68  ? 869  HOH B O     1 
HETATM 8886 O  O     . HOH H 4 .   ? 9.254   31.781 -39.301 1.00 29.84  ? 870  HOH B O     1 
HETATM 8887 O  O     . HOH H 4 .   ? 1.637   40.962 -12.556 1.00 21.67  ? 871  HOH B O     1 
HETATM 8888 O  O     . HOH H 4 .   ? 48.380  70.625 -20.246 1.00 28.28  ? 872  HOH B O     1 
HETATM 8889 O  O     . HOH H 4 .   ? 10.355  63.897 -32.696 1.00 29.29  ? 873  HOH B O     1 
HETATM 8890 O  O     . HOH H 4 .   ? 33.828  81.102 -17.049 1.00 34.28  ? 874  HOH B O     1 
HETATM 8891 O  O     . HOH H 4 .   ? 16.322  67.989 -31.063 1.00 20.47  ? 875  HOH B O     1 
HETATM 8892 O  O     . HOH H 4 .   ? 32.226  49.606 -11.397 1.00 16.80  ? 876  HOH B O     1 
HETATM 8893 O  O     . HOH H 4 .   ? 31.859  88.900 -40.399 1.00 29.11  ? 877  HOH B O     1 
HETATM 8894 O  O     . HOH H 4 .   ? 32.948  74.079 -0.735  1.00 43.14  ? 878  HOH B O     1 
HETATM 8895 O  O     . HOH H 4 .   ? 37.423  48.784 -10.630 1.00 24.62  ? 879  HOH B O     1 
HETATM 8896 O  O     . HOH H 4 .   ? 16.047  76.763 -33.603 1.00 29.45  ? 880  HOH B O     1 
HETATM 8897 O  O     . HOH H 4 .   ? 33.128  91.817 -25.439 1.00 36.34  ? 881  HOH B O     1 
HETATM 8898 O  O     . HOH H 4 .   ? 14.511  87.470 -28.116 1.00 40.15  ? 882  HOH B O     1 
HETATM 8899 O  O     . HOH H 4 .   ? 17.757  86.270 -45.354 1.00 25.77  ? 883  HOH B O     1 
HETATM 8900 O  O     . HOH H 4 .   ? 31.913  40.775 -36.137 1.00 38.30  ? 884  HOH B O     1 
HETATM 8901 O  O     . HOH H 4 .   ? 45.234  64.138 -26.149 1.00 26.43  ? 885  HOH B O     1 
HETATM 8902 O  O     . HOH H 4 .   ? 24.823  93.657 -54.562 1.00 35.71  ? 886  HOH B O     1 
HETATM 8903 O  O     . HOH H 4 .   ? 17.969  67.333 2.699   1.00 59.51  ? 887  HOH B O     1 
HETATM 8904 O  O     . HOH H 4 .   ? 25.630  68.493 -27.953 1.00 23.47  ? 888  HOH B O     1 
HETATM 8905 O  O     . HOH H 4 .   ? 40.338  71.740 -35.154 1.00 36.50  ? 889  HOH B O     1 
HETATM 8906 O  O     . HOH H 4 .   ? 22.462  59.833 -23.512 1.00 16.60  ? 890  HOH B O     1 
HETATM 8907 O  O     . HOH H 4 .   ? 17.809  66.533 -60.444 1.00 34.22  ? 891  HOH B O     1 
HETATM 8908 O  O     . HOH H 4 .   ? 14.733  81.171 -55.749 1.00 24.38  ? 892  HOH B O     1 
HETATM 8909 O  O     . HOH H 4 .   ? 18.454  73.694 -23.723 1.00 25.22  ? 893  HOH B O     1 
HETATM 8910 O  O     . HOH H 4 .   ? 10.895  34.480 -35.614 1.00 23.57  ? 894  HOH B O     1 
HETATM 8911 O  O     . HOH H 4 .   ? 31.361  90.821 -54.400 1.00 51.52  ? 895  HOH B O     1 
HETATM 8912 O  O     . HOH H 4 .   ? 16.756  29.307 -33.422 1.00 29.71  ? 896  HOH B O     1 
HETATM 8913 O  O     . HOH H 4 .   ? 7.191   51.072 -34.741 1.00 27.22  ? 897  HOH B O     1 
HETATM 8914 O  O     . HOH H 4 .   ? 10.731  54.192 -33.574 1.00 26.05  ? 898  HOH B O     1 
HETATM 8915 O  O     . HOH H 4 .   ? 10.431  27.909 -25.075 1.00 54.18  ? 899  HOH B O     1 
HETATM 8916 O  O     . HOH H 4 .   ? 27.512  55.129 -45.374 1.00 35.24  ? 900  HOH B O     1 
HETATM 8917 O  O     . HOH H 4 .   ? 39.113  91.934 -35.121 1.00 46.14  ? 901  HOH B O     1 
HETATM 8918 O  O     . HOH H 4 .   ? 33.338  67.703 -42.851 1.00 27.87  ? 902  HOH B O     1 
HETATM 8919 O  O     . HOH H 4 .   ? 28.290  90.937 -54.797 1.00 39.97  ? 903  HOH B O     1 
HETATM 8920 O  O     . HOH H 4 .   ? 51.299  67.371 -5.207  1.00 30.47  ? 904  HOH B O     1 
HETATM 8921 O  O     . HOH H 4 .   ? -1.483  37.144 -15.653 1.00 34.48  ? 905  HOH B O     1 
HETATM 8922 O  O     . HOH H 4 .   ? 38.938  84.603 -49.453 1.00 44.46  ? 906  HOH B O     1 
HETATM 8923 O  O     . HOH H 4 .   ? 32.378  48.064 -13.741 1.00 22.66  ? 907  HOH B O     1 
HETATM 8924 O  O     . HOH H 4 .   ? 28.590  56.406 -39.044 1.00 29.36  ? 908  HOH B O     1 
HETATM 8925 O  O     . HOH H 4 .   ? 28.731  63.213 4.972   1.00 29.41  ? 909  HOH B O     1 
HETATM 8926 O  O     . HOH H 4 .   ? 39.617  45.697 -19.420 1.00 42.81  ? 910  HOH B O     1 
HETATM 8927 O  O     . HOH H 4 .   ? 7.979   38.657 -39.765 1.00 25.82  ? 911  HOH B O     1 
HETATM 8928 O  O     . HOH H 4 .   ? 10.725  67.853 4.619   1.00 33.80  ? 912  HOH B O     1 
HETATM 8929 O  O     . HOH H 4 .   ? 20.737  33.873 -28.705 1.00 27.29  ? 913  HOH B O     1 
HETATM 8930 O  O     . HOH H 4 .   ? 20.549  65.807 0.860   1.00 36.72  ? 914  HOH B O     1 
HETATM 8931 O  O     . HOH H 4 .   ? 22.564  41.745 -47.307 1.00 33.02  ? 915  HOH B O     1 
HETATM 8932 O  O     . HOH H 4 .   ? 49.916  77.104 -20.730 1.00 45.58  ? 916  HOH B O     1 
HETATM 8933 O  O     . HOH H 4 .   ? 19.042  89.627 -20.682 1.00 43.10  ? 917  HOH B O     1 
HETATM 8934 O  O     . HOH H 4 .   ? 11.660  32.066 -34.807 1.00 30.94  ? 918  HOH B O     1 
HETATM 8935 O  O     . HOH H 4 .   ? 36.552  45.450 -20.049 1.00 26.53  ? 919  HOH B O     1 
HETATM 8936 O  O     . HOH H 4 .   ? 23.198  55.403 -12.808 1.00 16.11  ? 920  HOH B O     1 
HETATM 8937 O  O     . HOH H 4 .   ? 22.212  37.077 -44.536 1.00 24.60  ? 921  HOH B O     1 
HETATM 8938 O  O     . HOH H 4 .   ? 22.562  63.094 -2.069  1.00 27.12  ? 922  HOH B O     1 
HETATM 8939 O  O     . HOH H 4 .   ? 20.612  60.927 -21.785 1.00 17.71  ? 923  HOH B O     1 
HETATM 8940 O  O     . HOH H 4 .   ? 43.538  82.663 -37.657 1.00 45.95  ? 924  HOH B O     1 
HETATM 8941 O  O     . HOH H 4 .   ? 39.605  51.253 -25.601 1.00 35.04  ? 925  HOH B O     1 
HETATM 8942 O  O     . HOH H 4 .   ? 15.558  69.185 -41.724 1.00 24.50  ? 926  HOH B O     1 
HETATM 8943 O  O     . HOH H 4 .   ? 35.787  75.765 -48.004 1.00 34.46  ? 927  HOH B O     1 
HETATM 8944 O  O     . HOH H 4 .   ? 21.484  51.289 -46.971 1.00 33.00  ? 928  HOH B O     1 
HETATM 8945 O  O     . HOH H 4 .   ? 28.170  82.623 -24.191 1.00 36.39  ? 929  HOH B O     1 
HETATM 8946 O  O     . HOH H 4 .   ? 36.700  81.488 -2.564  1.00 37.81  ? 930  HOH B O     1 
HETATM 8947 O  O     . HOH H 4 .   ? 5.932   59.412 -31.652 1.00 30.94  ? 931  HOH B O     1 
HETATM 8948 O  O     . HOH H 4 .   ? 20.840  52.014 -14.552 1.00 16.08  ? 932  HOH B O     1 
HETATM 8949 O  O     . HOH H 4 .   ? 8.162   42.096 -36.533 1.00 29.65  ? 933  HOH B O     1 
HETATM 8950 O  O     . HOH H 4 .   ? 28.852  66.763 -28.712 1.00 19.03  ? 934  HOH B O     1 
HETATM 8951 O  O     . HOH H 4 .   ? 10.584  79.251 -39.952 1.00 37.19  ? 935  HOH B O     1 
HETATM 8952 O  O     . HOH H 4 .   ? 33.159  81.849 -25.157 1.00 28.73  ? 936  HOH B O     1 
HETATM 8953 O  O     . HOH H 4 .   ? 15.319  62.902 -37.089 1.00 26.91  ? 937  HOH B O     1 
HETATM 8954 O  O     . HOH H 4 .   ? 0.926   32.141 -19.007 1.00 30.45  ? 938  HOH B O     1 
HETATM 8955 O  O     . HOH H 4 .   ? 9.374   38.546 -44.646 1.00 24.73  ? 939  HOH B O     1 
HETATM 8956 O  O     . HOH H 4 .   ? 47.265  57.302 -20.973 1.00 33.41  ? 940  HOH B O     1 
HETATM 8957 O  O     . HOH H 4 .   ? 24.396  66.493 -19.030 1.00 19.18  ? 941  HOH B O     1 
HETATM 8958 O  O     . HOH H 4 .   ? 24.394  65.364 -49.840 1.00 33.53  ? 942  HOH B O     1 
HETATM 8959 O  O     . HOH H 4 .   ? 8.794   44.924 -38.643 1.00 44.98  ? 943  HOH B O     1 
HETATM 8960 O  O     . HOH H 4 .   ? 8.033   37.892 -30.907 1.00 42.27  ? 944  HOH B O     1 
HETATM 8961 O  O     . HOH H 4 .   ? 32.766  69.156 -30.055 1.00 20.94  ? 945  HOH B O     1 
HETATM 8962 O  O     . HOH H 4 .   ? 18.174  28.652 -39.383 1.00 25.37  ? 946  HOH B O     1 
HETATM 8963 O  O     . HOH H 4 .   ? 26.514  78.603 -57.686 1.00 31.95  ? 947  HOH B O     1 
HETATM 8964 O  O     . HOH H 4 .   ? 23.836  30.093 -43.794 1.00 34.70  ? 948  HOH B O     1 
HETATM 8965 O  O     . HOH H 4 .   ? 10.759  51.829 -37.612 1.00 20.36  ? 949  HOH B O     1 
HETATM 8966 O  O     . HOH H 4 .   ? 28.902  57.031 -41.645 1.00 37.16  ? 950  HOH B O     1 
HETATM 8967 O  O     . HOH H 4 .   ? 14.930  86.220 -32.266 1.00 37.10  ? 951  HOH B O     1 
HETATM 8968 O  O     . HOH H 4 .   ? 47.340  62.523 -25.088 1.00 39.99  ? 952  HOH B O     1 
HETATM 8969 O  O     . HOH H 4 .   ? 28.700  64.283 -32.656 1.00 20.89  ? 953  HOH B O     1 
HETATM 8970 O  O     . HOH H 4 .   ? 2.021   37.553 -26.134 1.00 25.20  ? 954  HOH B O     1 
HETATM 8971 O  O     . HOH H 4 .   ? 6.330   43.751 -22.877 1.00 19.08  ? 955  HOH B O     1 
HETATM 8972 O  O     . HOH H 4 .   ? 9.007   88.625 -46.878 1.00 43.12  ? 956  HOH B O     1 
HETATM 8973 O  O     . HOH H 4 .   ? 49.699  71.165 -4.678  1.00 39.96  ? 957  HOH B O     1 
HETATM 8974 O  O     . HOH H 4 .   ? 8.472   30.364 -33.038 1.00 39.08  ? 958  HOH B O     1 
HETATM 8975 O  O     . HOH H 4 .   ? 31.402  57.005 -38.319 1.00 32.13  ? 959  HOH B O     1 
HETATM 8976 O  O     . HOH H 4 .   ? 23.544  65.889 -45.443 1.00 30.10  ? 960  HOH B O     1 
HETATM 8977 O  O     . HOH H 4 .   ? 21.280  65.073 -44.347 1.00 34.67  ? 961  HOH B O     1 
HETATM 8978 O  O     . HOH H 4 .   ? 20.524  34.196 -24.540 1.00 28.65  ? 962  HOH B O     1 
HETATM 8979 O  O     . HOH H 4 .   ? 36.273  88.661 -27.770 1.00 37.21  ? 963  HOH B O     1 
HETATM 8980 O  O     . HOH H 4 .   ? 20.689  35.760 -26.879 1.00 23.60  ? 964  HOH B O     1 
HETATM 8981 O  O     . HOH H 4 .   ? 0.593   45.734 -27.041 1.00 42.75  ? 965  HOH B O     1 
HETATM 8982 O  O     . HOH H 4 .   ? 53.937  60.623 -20.266 1.00 49.20  ? 966  HOH B O     1 
HETATM 8983 O  O     . HOH H 4 .   ? 20.440  32.021 -21.652 1.00 50.51  ? 967  HOH B O     1 
HETATM 8984 O  O     . HOH H 4 .   ? 9.369   34.895 -38.868 1.00 27.60  ? 968  HOH B O     1 
HETATM 8985 O  O     . HOH H 4 .   ? 12.187  68.878 -53.028 1.00 38.96  ? 969  HOH B O     1 
HETATM 8986 O  O     . HOH H 4 .   ? 30.152  66.880 -2.258  1.00 27.59  ? 970  HOH B O     1 
HETATM 8987 O  O     . HOH H 4 .   ? 38.361  71.629 -32.713 1.00 30.55  ? 971  HOH B O     1 
HETATM 8988 O  O     . HOH H 4 .   ? 37.634  83.762 -40.162 1.00 36.40  ? 972  HOH B O     1 
HETATM 8989 O  O     . HOH H 4 .   ? 12.577  89.597 -40.757 1.00 31.40  ? 973  HOH B O     1 
HETATM 8990 O  O     . HOH H 4 .   ? 15.840  85.845 -54.569 1.00 27.08  ? 974  HOH B O     1 
HETATM 8991 O  O     . HOH H 4 .   ? 28.811  43.315 -43.810 1.00 32.83  ? 975  HOH B O     1 
HETATM 8992 O  O     . HOH H 4 .   ? 18.184  81.017 -37.916 1.00 29.71  ? 976  HOH B O     1 
HETATM 8993 O  O     . HOH H 4 .   ? 47.247  52.611 -14.803 1.00 36.14  ? 977  HOH B O     1 
HETATM 8994 O  O     . HOH H 4 .   ? 10.069  37.874 -33.036 1.00 26.37  ? 978  HOH B O     1 
HETATM 8995 O  O     . HOH H 4 .   ? 46.196  79.766 -11.583 1.00 39.93  ? 979  HOH B O     1 
HETATM 8996 O  O     . HOH H 4 .   ? 25.873  30.868 -27.963 1.00 43.52  ? 980  HOH B O     1 
HETATM 8997 O  O     . HOH H 4 .   ? 38.351  65.960 -32.193 1.00 28.85  ? 981  HOH B O     1 
HETATM 8998 O  O     . HOH H 4 .   ? 34.453  66.465 -40.097 1.00 28.94  ? 982  HOH B O     1 
HETATM 8999 O  O     . HOH H 4 .   ? 34.922  69.504 3.626   1.00 50.54  ? 983  HOH B O     1 
HETATM 9000 O  O     . HOH H 4 .   ? 44.400  58.503 -21.945 1.00 27.34  ? 984  HOH B O     1 
HETATM 9001 O  O     . HOH H 4 .   ? 27.057  94.255 -40.403 1.00 32.98  ? 985  HOH B O     1 
HETATM 9002 O  O     . HOH H 4 .   ? 38.390  76.132 -37.162 1.00 28.38  ? 986  HOH B O     1 
HETATM 9003 O  O     . HOH H 4 .   ? 22.509  62.179 -47.694 1.00 41.36  ? 987  HOH B O     1 
HETATM 9004 O  O     . HOH H 4 .   ? 28.294  61.924 -33.390 1.00 23.71  ? 988  HOH B O     1 
HETATM 9005 O  O     . HOH H 4 .   ? 39.162  88.590 -34.975 1.00 42.17  ? 989  HOH B O     1 
HETATM 9006 O  O     . HOH H 4 .   ? 16.353  53.305 -44.145 1.00 26.76  ? 990  HOH B O     1 
HETATM 9007 O  O     . HOH H 4 .   ? 29.828  32.901 -30.899 1.00 36.16  ? 991  HOH B O     1 
HETATM 9008 O  O     . HOH H 4 .   ? 10.395  76.656 -51.916 1.00 28.54  ? 992  HOH B O     1 
HETATM 9009 O  O     . HOH H 4 .   ? 40.585  73.688 -52.120 1.00 47.33  ? 993  HOH B O     1 
HETATM 9010 O  O     . HOH H 4 .   ? 2.942   31.062 -17.742 1.00 23.63  ? 994  HOH B O     1 
HETATM 9011 O  O     . HOH H 4 .   ? 11.547  61.092 -36.093 1.00 41.09  ? 995  HOH B O     1 
HETATM 9012 O  O     . HOH H 4 .   ? 19.448  64.410 -46.574 1.00 33.01  ? 996  HOH B O     1 
HETATM 9013 O  O     . HOH H 4 .   ? 6.280   36.120 -31.532 1.00 38.22  ? 997  HOH B O     1 
HETATM 9014 O  O     . HOH H 4 .   ? 19.017  59.659 -47.280 1.00 45.66  ? 998  HOH B O     1 
HETATM 9015 O  O     . HOH H 4 .   ? 46.736  55.798 -23.288 1.00 56.18  ? 999  HOH B O     1 
HETATM 9016 O  O     . HOH H 4 .   ? 17.350  92.082 -42.205 1.00 33.17  ? 1000 HOH B O     1 
HETATM 9017 O  O     . HOH H 4 .   ? 43.375  85.658 -33.555 1.00 42.54  ? 1001 HOH B O     1 
HETATM 9018 O  O     . HOH H 4 .   ? 3.317   39.721 -26.928 1.00 25.28  ? 1002 HOH B O     1 
HETATM 9019 O  O     . HOH H 4 .   ? 30.486  85.156 -22.216 1.00 66.58  ? 1003 HOH B O     1 
HETATM 9020 O  O     . HOH H 4 .   ? 31.699  66.833 0.088   1.00 29.72  ? 1004 HOH B O     1 
HETATM 9021 O  O     . HOH H 4 .   ? 54.006  66.269 -15.406 1.00 54.18  ? 1005 HOH B O     1 
HETATM 9022 O  O     . HOH H 4 .   ? 43.306  81.614 1.022   1.00 43.23  ? 1006 HOH B O     1 
HETATM 9023 O  O     . HOH H 4 .   ? 21.104  46.447 -47.324 1.00 33.00  ? 1007 HOH B O     1 
HETATM 9024 O  O     . HOH H 4 .   ? 33.910  83.792 -9.141  1.00 42.23  ? 1008 HOH B O     1 
HETATM 9025 O  O     . HOH H 4 .   ? 32.181  65.080 -35.915 1.00 37.99  ? 1009 HOH B O     1 
HETATM 9026 O  O     . HOH H 4 .   ? 33.287  46.799 -40.762 1.00 39.48  ? 1010 HOH B O     1 
HETATM 9027 O  O     . HOH H 4 .   ? 24.635  78.732 -23.390 1.00 29.32  ? 1011 HOH B O     1 
HETATM 9028 O  O     . HOH H 4 .   ? 30.883  32.024 -38.266 1.00 38.82  ? 1012 HOH B O     1 
HETATM 9029 O  O     . HOH H 4 .   ? 34.568  68.616 -32.011 1.00 24.10  ? 1013 HOH B O     1 
HETATM 9030 O  O     . HOH H 4 .   ? 39.796  47.421 -10.948 1.00 37.72  ? 1014 HOH B O     1 
HETATM 9031 O  O     . HOH H 4 .   ? 10.287  73.303 -50.938 1.00 26.96  ? 1015 HOH B O     1 
HETATM 9032 O  O     . HOH H 4 .   ? 11.990  85.952 -47.876 1.00 31.22  ? 1016 HOH B O     1 
HETATM 9033 O  O     . HOH H 4 .   ? 42.975  56.156 -20.978 1.00 28.71  ? 1017 HOH B O     1 
HETATM 9034 O  O     . HOH H 4 .   ? 29.705  35.313 -48.150 1.00 28.72  ? 1018 HOH B O     1 
HETATM 9035 O  O     . HOH H 4 .   ? 28.750  84.938 -20.386 1.00 52.78  ? 1019 HOH B O     1 
HETATM 9036 O  O     . HOH H 4 .   ? 52.228  60.788 -12.892 1.00 32.82  ? 1020 HOH B O     1 
HETATM 9037 O  O     . HOH H 4 .   ? 36.690  62.029 -31.760 1.00 47.98  ? 1021 HOH B O     1 
HETATM 9038 O  O     . HOH H 4 .   ? 8.665   43.089 -40.709 1.00 32.28  ? 1022 HOH B O     1 
HETATM 9039 O  O     . HOH H 4 .   ? 18.404  49.249 -45.548 1.00 26.45  ? 1023 HOH B O     1 
HETATM 9040 O  O     . HOH H 4 .   ? 37.665  46.762 -31.040 1.00 28.60  ? 1024 HOH B O     1 
HETATM 9041 O  O     . HOH H 4 .   ? 26.654  31.088 -44.079 1.00 30.93  ? 1025 HOH B O     1 
HETATM 9042 O  O     . HOH H 4 .   ? 11.054  30.250 -26.647 1.00 35.95  ? 1026 HOH B O     1 
HETATM 9043 O  O     . HOH H 4 .   ? 39.939  60.823 -32.435 1.00 33.20  ? 1027 HOH B O     1 
HETATM 9044 O  O     . HOH H 4 .   ? 14.621  83.729 -37.847 1.00 30.92  ? 1028 HOH B O     1 
HETATM 9045 O  O     . HOH H 4 .   ? 31.956  66.247 -37.876 1.00 34.36  ? 1029 HOH B O     1 
HETATM 9046 O  O     . HOH H 4 .   ? 20.022  64.667 -2.109  1.00 38.58  ? 1030 HOH B O     1 
HETATM 9047 O  O     . HOH H 4 .   ? 24.412  49.085 -48.415 1.00 29.41  ? 1031 HOH B O     1 
HETATM 9048 O  O     . HOH H 4 .   ? 29.016  83.471 -22.001 1.00 44.01  ? 1032 HOH B O     1 
HETATM 9049 O  O     . HOH H 4 .   ? 17.687  37.921 -14.576 1.00 26.05  ? 1033 HOH B O     1 
HETATM 9050 O  O     . HOH H 4 .   ? 35.657  81.125 -26.427 1.00 32.92  ? 1034 HOH B O     1 
HETATM 9051 O  O     . HOH H 4 .   ? 8.458   49.896 -36.840 1.00 36.76  ? 1035 HOH B O     1 
HETATM 9052 O  O     . HOH H 4 .   ? 26.182  62.790 4.101   1.00 35.24  ? 1036 HOH B O     1 
HETATM 9053 O  O     . HOH H 4 .   ? 6.455   32.994 -35.709 1.00 47.47  ? 1037 HOH B O     1 
HETATM 9054 O  O     . HOH H 4 .   ? 46.668  61.330 -29.599 1.00 45.17  ? 1038 HOH B O     1 
HETATM 9055 O  O     . HOH H 4 .   ? 32.086  84.295 -11.601 1.00 48.02  ? 1039 HOH B O     1 
HETATM 9056 O  O     . HOH H 4 .   ? 18.238  71.072 -15.233 1.00 37.58  ? 1040 HOH B O     1 
HETATM 9057 O  O     . HOH H 4 .   ? 28.188  31.153 -29.953 1.00 43.14  ? 1041 HOH B O     1 
HETATM 9058 O  O     . HOH H 4 .   ? 24.474  30.563 -30.415 1.00 41.19  ? 1042 HOH B O     1 
HETATM 9059 O  O     . HOH H 4 .   ? 33.400  92.354 -32.609 1.00 36.57  ? 1043 HOH B O     1 
HETATM 9060 O  O     . HOH H 4 .   ? 8.883   46.778 -37.286 1.00 42.94  ? 1044 HOH B O     1 
HETATM 9061 O  O     . HOH H 4 .   ? 33.574  61.447 -35.522 1.00 36.22  ? 1045 HOH B O     1 
HETATM 9062 O  O     . HOH H 4 .   ? 13.195  81.250 -30.139 1.00 36.38  ? 1046 HOH B O     1 
HETATM 9063 O  O     . HOH H 4 .   ? 34.220  72.129 3.361   1.00 40.83  ? 1047 HOH B O     1 
HETATM 9064 O  O     . HOH H 4 .   ? 32.894  44.673 -47.049 1.00 33.40  ? 1048 HOH B O     1 
HETATM 9065 O  O     . HOH H 4 .   ? 2.782   39.796 -35.145 1.00 45.72  ? 1049 HOH B O     1 
HETATM 9066 O  O     . HOH H 4 .   ? 7.359   38.958 -32.725 1.00 56.78  ? 1050 HOH B O     1 
HETATM 9067 O  O     . HOH H 4 .   ? 36.697  64.019 -32.676 1.00 30.97  ? 1051 HOH B O     1 
HETATM 9068 O  O     . HOH H 4 .   ? 29.311  96.023 -39.666 1.00 37.68  ? 1052 HOH B O     1 
HETATM 9069 O  O     . HOH H 4 .   ? 34.744  81.640 -56.455 1.00 42.89  ? 1053 HOH B O     1 
HETATM 9070 O  O     . HOH H 4 .   ? 42.766  57.490 -29.742 1.00 30.59  ? 1054 HOH B O     1 
HETATM 9071 O  O     . HOH H 4 .   ? 47.319  78.045 -27.730 1.00 38.63  ? 1055 HOH B O     1 
HETATM 9072 O  O     . HOH H 4 .   ? 43.813  80.561 -25.746 1.00 42.40  ? 1056 HOH B O     1 
HETATM 9073 O  O     . HOH H 4 .   ? 44.313  53.330 -30.785 1.00 41.18  ? 1057 HOH B O     1 
HETATM 9074 O  O     . HOH H 4 .   ? 13.224  81.803 -38.601 1.00 32.26  ? 1058 HOH B O     1 
HETATM 9075 O  O     . HOH H 4 .   ? 39.707  87.573 -32.924 1.00 53.62  ? 1059 HOH B O     1 
HETATM 9076 O  O     . HOH H 4 .   ? 31.194  94.804 -36.184 1.00 38.55  ? 1060 HOH B O     1 
HETATM 9077 O  O     . HOH H 4 .   ? 20.950  52.988 -48.552 1.00 40.38  ? 1061 HOH B O     1 
HETATM 9078 O  O     . HOH H 4 .   ? 29.663  60.731 -38.530 1.00 43.02  ? 1062 HOH B O     1 
HETATM 9079 O  O     . HOH H 4 .   ? 13.485  70.356 -37.773 1.00 36.69  ? 1063 HOH B O     1 
HETATM 9080 O  O     . HOH H 4 .   ? 48.558  74.228 -17.303 1.00 45.60  ? 1064 HOH B O     1 
HETATM 9081 O  O     . HOH H 4 .   ? 11.756  29.924 -28.822 1.00 30.97  ? 1065 HOH B O     1 
HETATM 9082 O  O     . HOH H 4 .   ? 7.242   41.201 -38.617 1.00 32.44  ? 1066 HOH B O     1 
HETATM 9083 O  O     . HOH H 4 .   ? 37.539  41.749 -28.857 1.00 33.39  ? 1067 HOH B O     1 
HETATM 9084 O  O     . HOH H 4 .   ? -3.362  38.902 -18.107 1.00 38.60  ? 1068 HOH B O     1 
HETATM 9085 O  O     . HOH H 4 .   ? 16.261  82.289 -36.690 1.00 32.78  ? 1069 HOH B O     1 
HETATM 9086 O  O     . HOH H 4 .   ? 47.491  78.985 -14.012 1.00 36.89  ? 1070 HOH B O     1 
HETATM 9087 O  O     . HOH H 4 .   ? 17.452  66.101 0.851   1.00 39.30  ? 1071 HOH B O     1 
HETATM 9088 O  O     . HOH H 4 .   ? 40.495  73.650 -42.852 1.00 39.44  ? 1072 HOH B O     1 
HETATM 9089 O  O     . HOH H 4 .   ? 48.730  78.085 -22.655 1.00 40.62  ? 1073 HOH B O     1 
HETATM 9090 O  O     . HOH H 4 .   ? 4.955   35.325 -39.766 1.00 41.48  ? 1074 HOH B O     1 
HETATM 9091 O  O     . HOH H 4 .   ? 41.335  73.410 -36.900 1.00 36.99  ? 1075 HOH B O     1 
HETATM 9092 O  O     . HOH H 4 .   ? 21.882  75.331 -58.562 1.00 29.07  ? 1076 HOH B O     1 
HETATM 9093 O  O     . HOH H 4 .   ? 30.868  33.272 -33.353 1.00 37.68  ? 1077 HOH B O     1 
HETATM 9094 O  O     . HOH H 4 .   ? 22.637  89.914 -19.600 1.00 44.72  ? 1078 HOH B O     1 
HETATM 9095 O  O     . HOH H 4 .   ? 13.934  88.554 -33.325 1.00 36.43  ? 1079 HOH B O     1 
HETATM 9096 O  O     . HOH H 4 .   ? -2.572  39.941 -15.731 1.00 39.16  ? 1080 HOH B O     1 
HETATM 9097 O  O     . HOH H 4 .   ? 4.417   37.095 -30.148 1.00 37.99  ? 1081 HOH B O     1 
HETATM 9098 O  O     . HOH H 4 .   ? 7.181   36.394 -39.020 1.00 31.23  ? 1082 HOH B O     1 
HETATM 9099 O  O     . HOH H 4 .   ? 15.935  87.030 -47.229 1.00 28.08  ? 1083 HOH B O     1 
HETATM 9100 O  O     . HOH H 4 .   ? 13.255  63.913 -40.757 1.00 33.43  ? 1084 HOH B O     1 
HETATM 9101 O  O     . HOH H 4 .   ? 5.255   38.013 -43.667 1.00 36.83  ? 1085 HOH B O     1 
HETATM 9102 O  O     . HOH H 4 .   ? 22.561  95.566 -39.306 1.00 52.64  ? 1086 HOH B O     1 
HETATM 9103 O  O     . HOH H 4 .   ? 47.508  75.444 -26.998 1.00 41.29  ? 1087 HOH B O     1 
HETATM 9104 O  O     . HOH H 4 .   ? 20.576  54.454 -12.674 1.00 13.71  ? 1088 HOH B O     1 
HETATM 9105 O  O     . HOH H 4 .   ? 40.179  51.349 -29.057 1.00 33.41  ? 1089 HOH B O     1 
HETATM 9106 O  O     . HOH H 4 .   ? 21.117  93.731 -38.093 1.00 35.44  ? 1090 HOH B O     1 
HETATM 9107 O  O     . HOH H 4 .   ? 30.649  38.652 -36.189 1.00 36.92  ? 1091 HOH B O     1 
HETATM 9108 O  O     . HOH H 4 .   ? 46.369  53.848 -21.445 1.00 45.28  ? 1092 HOH B O     1 
HETATM 9109 O  O     . HOH H 4 .   ? 6.708   39.904 -35.027 1.00 40.79  ? 1093 HOH B O     1 
HETATM 9110 O  O     . HOH H 4 .   ? 16.993  50.918 -45.809 1.00 27.06  ? 1094 HOH B O     1 
HETATM 9111 O  O     . HOH H 4 .   ? 33.045  94.947 -37.768 1.00 40.90  ? 1095 HOH B O     1 
HETATM 9112 O  O     . HOH H 4 .   ? 11.585  82.151 -39.942 1.00 38.38  ? 1096 HOH B O     1 
HETATM 9113 O  O     . HOH H 4 .   ? 45.027  76.620 -25.992 1.00 43.76  ? 1097 HOH B O     1 
HETATM 9114 O  O     . HOH H 4 .   ? 18.073  65.622 5.908   1.00 39.34  ? 1098 HOH B O     1 
HETATM 9115 O  O     . HOH H 4 .   ? 31.176  61.836 -36.203 1.00 29.13  ? 1099 HOH B O     1 
HETATM 9116 O  O     . HOH H 4 .   ? 12.433  87.966 -35.382 1.00 35.70  ? 1100 HOH B O     1 
HETATM 9117 O  O     . HOH H 4 .   ? 12.886  84.902 -30.775 1.00 40.12  ? 1101 HOH B O     1 
HETATM 9118 O  O     . HOH H 4 .   ? 55.783  53.914 -10.953 1.00 40.48  ? 1102 HOH B O     1 
HETATM 9119 O  O     . HOH H 4 .   ? 46.150  84.558 -26.134 1.00 45.59  ? 1103 HOH B O     1 
HETATM 9120 O  O     . HOH H 4 .   ? 14.522  83.491 -54.639 1.00 28.95  ? 1104 HOH B O     1 
HETATM 9121 O  O     . HOH H 4 .   ? 32.684  91.982 -35.556 1.00 45.44  ? 1105 HOH B O     1 
HETATM 9122 O  O     . HOH H 4 .   ? 13.963  78.132 -59.368 1.00 27.88  ? 1106 HOH B O     1 
HETATM 9123 O  O     . HOH H 4 .   ? 31.622  36.469 -37.487 1.00 46.79  ? 1107 HOH B O     1 
HETATM 9124 O  O     . HOH H 4 .   ? 32.234  63.191 -34.898 1.00 34.72  ? 1108 HOH B O     1 
HETATM 9125 O  O     . HOH H 4 .   ? 41.104  74.392 3.444   1.00 46.36  ? 1109 HOH B O     1 
HETATM 9126 O  O     . HOH H 4 .   ? 49.997  71.492 -18.093 1.00 31.56  ? 1110 HOH B O     1 
HETATM 9127 O  O     . HOH H 4 .   ? 1.925   52.032 -28.546 1.00 41.96  ? 1111 HOH B O     1 
HETATM 9128 O  O     . HOH H 4 .   ? 14.503  74.818 -34.911 1.00 36.70  ? 1112 HOH B O     1 
HETATM 9129 O  O     . HOH H 4 .   ? 16.648  92.299 -34.054 1.00 39.69  ? 1113 HOH B O     1 
HETATM 9130 O  O     . HOH H 4 .   ? 30.300  86.735 -20.331 1.00 50.65  ? 1114 HOH B O     1 
HETATM 9131 O  O     . HOH H 4 .   ? 24.432  64.056 -47.938 1.00 37.39  ? 1115 HOH B O     1 
HETATM 9132 O  O     . HOH H 4 .   ? 50.753  69.609 -21.880 1.00 34.88  ? 1116 HOH B O     1 
HETATM 9133 O  O     . HOH H 4 .   ? 39.431  66.898 -36.324 1.00 41.11  ? 1117 HOH B O     1 
HETATM 9134 O  O     . HOH H 4 .   ? 13.242  62.097 -37.924 1.00 42.82  ? 1118 HOH B O     1 
HETATM 9135 O  O     . HOH H 4 .   ? 3.557   28.217 -19.006 1.00 32.53  ? 1119 HOH B O     1 
HETATM 9136 O  O     . HOH H 4 .   ? 50.115  57.118 -20.825 1.00 47.55  ? 1120 HOH B O     1 
HETATM 9137 O  O     . HOH H 4 .   ? 42.924  54.952 -31.153 1.00 39.76  ? 1121 HOH B O     1 
HETATM 9138 O  O     . HOH H 4 .   ? 12.959  87.983 -46.762 1.00 52.75  ? 1122 HOH B O     1 
HETATM 9139 O  O     . HOH H 4 .   ? 35.322  95.394 -50.835 1.00 56.02  ? 1123 HOH B O     1 
HETATM 9140 O  O     . HOH H 4 .   ? 7.948   31.164 -35.139 1.00 45.78  ? 1124 HOH B O     1 
HETATM 9141 O  O     . HOH H 4 .   ? 45.580  63.577 -29.163 1.00 33.31  ? 1125 HOH B O     1 
HETATM 9142 O  O     . HOH H 4 .   ? 31.544  88.343 -21.269 1.00 45.27  ? 1126 HOH B O     1 
HETATM 9143 O  O     . HOH H 4 .   ? 2.339   36.906 -29.680 1.00 38.46  ? 1127 HOH B O     1 
HETATM 9144 O  O     . HOH H 4 .   ? 33.068  86.361 -19.130 1.00 43.17  ? 1128 HOH B O     1 
HETATM 9145 O  O     . HOH H 4 .   ? 15.042  86.144 -49.878 1.00 28.56  ? 1129 HOH B O     1 
HETATM 9146 O  O     . HOH H 4 .   ? 37.257  48.136 -23.512 1.00 26.20  ? 1130 HOH B O     1 
HETATM 9147 O  O     . HOH H 4 .   ? 7.202   83.064 -41.732 1.00 38.81  ? 1131 HOH B O     1 
HETATM 9148 O  O     . HOH H 4 .   ? 31.762  33.846 -37.268 1.00 34.93  ? 1132 HOH B O     1 
HETATM 9149 O  O     . HOH H 4 .   ? 42.461  53.009 -22.194 1.00 38.60  ? 1133 HOH B O     1 
HETATM 9150 O  O     . HOH H 4 .   ? 21.919  76.909 -60.857 1.00 29.67  ? 1134 HOH B O     1 
HETATM 9151 O  O     . HOH H 4 .   ? 48.354  67.079 -24.520 1.00 37.16  ? 1135 HOH B O     1 
HETATM 9152 O  O     . HOH H 4 .   ? 33.669  65.633 -33.806 1.00 33.05  ? 1136 HOH B O     1 
HETATM 9153 O  O     . HOH H 4 .   ? 17.615  93.724 -45.856 1.00 54.27  ? 1137 HOH B O     1 
HETATM 9154 O  O     . HOH H 4 .   ? 15.609  66.498 -39.014 1.00 32.41  ? 1138 HOH B O     1 
HETATM 9155 O  O     . HOH H 4 .   ? 21.861  68.714 -59.471 1.00 37.37  ? 1139 HOH B O     1 
HETATM 9156 O  O     . HOH H 4 .   ? 34.826  71.221 -47.473 1.00 35.82  ? 1140 HOH B O     1 
HETATM 9157 O  O     . HOH H 4 .   ? -3.048  42.354 -21.591 1.00 42.21  ? 1141 HOH B O     1 
HETATM 9158 O  O     . HOH H 4 .   ? 20.497  62.177 -46.714 1.00 53.25  ? 1142 HOH B O     1 
HETATM 9159 O  O     . HOH H 4 .   ? 34.832  83.880 -57.814 1.00 44.87  ? 1143 HOH B O     1 
HETATM 9160 O  O     . HOH H 4 .   ? 32.448  69.548 -47.643 1.00 32.24  ? 1144 HOH B O     1 
HETATM 9161 O  O     . HOH H 4 .   ? 39.792  88.911 -31.020 1.00 52.35  ? 1145 HOH B O     1 
HETATM 9162 O  O     . HOH H 4 .   ? 49.705  73.561 -27.727 1.00 47.58  ? 1146 HOH B O     1 
HETATM 9163 O  O     . HOH H 4 .   ? 13.665  77.818 -33.032 1.00 35.72  ? 1147 HOH B O     1 
HETATM 9164 O  O     . HOH H 4 .   ? 25.902  93.806 -56.682 1.00 48.03  ? 1148 HOH B O     1 
HETATM 9165 O  O     . HOH H 4 .   ? 30.925  72.718 -54.943 1.00 45.73  ? 1149 HOH B O     1 
HETATM 9166 O  O     . HOH H 4 .   ? 32.084  72.338 -48.232 1.00 30.07  ? 1150 HOH B O     1 
HETATM 9167 O  O     . HOH H 4 .   ? 22.552  26.982 -32.927 1.00 46.23  ? 1151 HOH B O     1 
HETATM 9168 O  O     . HOH H 4 .   ? 32.356  96.821 -40.109 1.00 51.09  ? 1152 HOH B O     1 
HETATM 9169 O  O     . HOH H 4 .   ? 2.380   52.300 -25.969 1.00 44.53  ? 1153 HOH B O     1 
HETATM 9170 O  O     . HOH H 4 .   ? 19.508  26.443 -40.627 1.00 30.03  ? 1154 HOH B O     1 
HETATM 9171 O  O     . HOH H 4 .   ? 44.041  51.449 -22.980 1.00 42.90  ? 1155 HOH B O     1 
HETATM 9172 O  O     . HOH H 4 .   ? 24.366  74.825 -57.647 1.00 35.31  ? 1156 HOH B O     1 
HETATM 9173 O  O     . HOH H 4 .   ? 32.853  72.559 -50.634 1.00 30.30  ? 1157 HOH B O     1 
HETATM 9174 O  O     . HOH H 4 .   ? 14.268  72.462 6.161   1.00 44.98  ? 1158 HOH B O     1 
HETATM 9175 O  O     . HOH H 4 .   ? 7.099   84.810 -48.636 1.00 49.76  ? 1159 HOH B O     1 
HETATM 9176 O  O     . HOH H 4 .   ? 21.675  28.936 -44.434 1.00 32.57  ? 1160 HOH B O     1 
HETATM 9177 O  O     . HOH H 4 .   ? 29.064  31.412 -44.299 1.00 37.22  ? 1161 HOH B O     1 
HETATM 9178 O  O     . HOH H 4 .   ? 34.556  83.471 -2.513  1.00 39.63  ? 1162 HOH B O     1 
HETATM 9179 O  O     . HOH H 4 .   ? 36.028  93.627 -26.982 1.00 42.92  ? 1163 HOH B O     1 
HETATM 9180 O  O     . HOH H 4 .   ? 35.506  56.886 -39.503 1.00 44.38  ? 1164 HOH B O     1 
HETATM 9181 O  O     . HOH H 4 .   ? -1.274  32.152 -17.287 1.00 40.14  ? 1165 HOH B O     1 
HETATM 9182 O  O     . HOH H 4 .   ? 12.827  83.426 -52.154 1.00 28.94  ? 1166 HOH B O     1 
HETATM 9183 O  O     . HOH H 4 .   ? 38.917  44.328 -27.241 1.00 54.45  ? 1167 HOH B O     1 
HETATM 9184 O  O     . HOH H 4 .   ? 41.461  43.533 -9.296  1.00 39.51  ? 1168 HOH B O     1 
HETATM 9185 O  O     . HOH H 4 .   ? 20.938  75.096 -62.707 1.00 38.57  ? 1169 HOH B O     1 
HETATM 9186 O  O     . HOH H 4 .   ? 4.848   89.058 -46.654 1.00 59.16  ? 1170 HOH B O     1 
HETATM 9187 O  O     . HOH H 4 .   ? 22.052  92.532 -19.017 1.00 48.61  ? 1171 HOH B O     1 
HETATM 9188 O  O     . HOH H 4 .   ? 42.180  73.427 5.842   1.00 49.56  ? 1172 HOH B O     1 
HETATM 9189 O  O     . HOH H 4 .   ? 24.666  25.309 -33.394 1.00 44.94  ? 1173 HOH B O     1 
HETATM 9190 O  O     . HOH H 4 .   ? 42.594  50.171 -25.935 1.00 40.60  ? 1174 HOH B O     1 
HETATM 9191 O  O     . HOH H 4 .   ? 16.919  96.023 -44.238 1.00 41.83  ? 1175 HOH B O     1 
HETATM 9192 O  O     . HOH H 4 .   ? 20.982  26.655 -42.794 1.00 30.37  ? 1176 HOH B O     1 
HETATM 9193 O  O     . HOH H 4 .   ? 43.403  44.994 -21.892 1.00 44.54  ? 1177 HOH B O     1 
HETATM 9194 O  O     . HOH H 4 .   ? 36.934  96.845 -52.834 1.00 59.01  ? 1178 HOH B O     1 
HETATM 9195 O  O     . HOH H 4 .   ? 37.910  93.091 -26.163 1.00 43.40  ? 1179 HOH B O     1 
HETATM 9196 O  O     . HOH H 4 .   ? 3.722   89.558 -48.898 1.00 54.74  ? 1180 HOH B 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   . THR A 17  ? 0.9748 0.9646 0.9875 0.0676  -0.0274 -0.1087 3   THR A N   
2    C CA  . THR A 17  ? 0.8394 0.8346 0.8425 0.0636  -0.0222 -0.1011 3   THR A CA  
3    C C   . THR A 17  ? 0.7255 0.7306 0.7260 0.0650  -0.0175 -0.1018 3   THR A C   
4    O O   . THR A 17  ? 0.7075 0.7220 0.6993 0.0642  -0.0133 -0.1028 3   THR A O   
5    C CB  . THR A 17  ? 0.8857 0.8849 0.8786 0.0614  -0.0208 -0.1017 3   THR A CB  
6    O OG1 . THR A 17  ? 0.9330 0.9383 0.9241 0.0655  -0.0219 -0.1120 3   THR A OG1 
7    C CG2 . THR A 17  ? 0.8767 0.8665 0.8713 0.0583  -0.0243 -0.0977 3   THR A CG2 
8    N N   . PRO A 18  ? 0.6666 0.6699 0.6749 0.0671  -0.0183 -0.1012 4   PRO A N   
9    C CA  . PRO A 18  ? 0.6068 0.6197 0.6139 0.0683  -0.0140 -0.1017 4   PRO A CA  
10   C C   . PRO A 18  ? 0.4991 0.5155 0.4987 0.0635  -0.0093 -0.0932 4   PRO A C   
11   O O   . PRO A 18  ? 0.5040 0.5135 0.5022 0.0599  -0.0101 -0.0856 4   PRO A O   
12   C CB  . PRO A 18  ? 0.5689 0.5768 0.5865 0.0713  -0.0170 -0.1016 4   PRO A CB  
13   C CG  . PRO A 18  ? 0.6107 0.6059 0.6347 0.0717  -0.0226 -0.1007 4   PRO A CG  
14   C CD  . PRO A 18  ? 0.6320 0.6240 0.6499 0.0678  -0.0228 -0.0981 4   PRO A CD  
15   N N   . TYR A 19  ? 0.4740 0.5016 0.4693 0.0634  -0.0044 -0.0947 5   TYR A N   
16   C CA  . TYR A 19  ? 0.3944 0.4260 0.3835 0.0590  0.0001  -0.0874 5   TYR A CA  
17   C C   . TYR A 19  ? 0.3812 0.4081 0.3754 0.0578  -0.0007 -0.0809 5   TYR A C   
18   O O   . TYR A 19  ? 0.3594 0.3869 0.3611 0.0610  -0.0020 -0.0832 5   TYR A O   
19   C CB  . TYR A 19  ? 0.3735 0.4182 0.3593 0.0595  0.0056  -0.0909 5   TYR A CB  
20   C CG  . TYR A 19  ? 0.3736 0.4233 0.3527 0.0547  0.0105  -0.0841 5   TYR A CG  
21   C CD1 . TYR A 19  ? 0.3357 0.3872 0.3185 0.0530  0.0124  -0.0793 5   TYR A CD1 
22   C CD2 . TYR A 19  ? 0.3340 0.3866 0.3032 0.0522  0.0129  -0.0828 5   TYR A CD2 
23   C CE1 . TYR A 19  ? 0.3243 0.3800 0.3022 0.0486  0.0166  -0.0735 5   TYR A CE1 
24   C CE2 . TYR A 19  ? 0.3437 0.4002 0.3074 0.0479  0.0172  -0.0763 5   TYR A CE2 
25   C CZ  . TYR A 19  ? 0.3296 0.3874 0.2981 0.0460  0.0190  -0.0717 5   TYR A CZ  
26   O OH  . TYR A 19  ? 0.3324 0.3937 0.2965 0.0416  0.0230  -0.0656 5   TYR A OH  
27   N N   . CYS A 20  ? 0.3573 0.3801 0.3474 0.0536  -0.0001 -0.0729 6   CYS A N   
28   C CA  . CYS A 20  ? 0.3571 0.3748 0.3512 0.0527  -0.0015 -0.0666 6   CYS A CA  
29   C C   . CYS A 20  ? 0.3090 0.3298 0.2978 0.0483  0.0019  -0.0601 6   CYS A C   
30   O O   . CYS A 20  ? 0.3179 0.3438 0.3002 0.0458  0.0051  -0.0598 6   CYS A O   
31   C CB  . CYS A 20  ? 0.3453 0.3514 0.3421 0.0526  -0.0060 -0.0636 6   CYS A CB  
32   S SG  . CYS A 20  ? 0.3898 0.3910 0.3798 0.0485  -0.0065 -0.0604 6   CYS A SG  
33   N N   . VAL A 21  ? 0.3130 0.3302 0.3045 0.0477  0.0008  -0.0547 7   VAL A N   
34   C CA  . VAL A 21  ? 0.3039 0.3239 0.2921 0.0441  0.0034  -0.0490 7   VAL A CA  
35   C C   . VAL A 21  ? 0.2775 0.2956 0.2584 0.0401  0.0045  -0.0457 7   VAL A C   
36   O O   . VAL A 21  ? 0.2805 0.3037 0.2572 0.0373  0.0077  -0.0436 7   VAL A O   
37   C CB  . VAL A 21  ? 0.2840 0.2992 0.2758 0.0445  0.0011  -0.0441 7   VAL A CB  
38   C CG1 . VAL A 21  ? 0.2689 0.2856 0.2571 0.0408  0.0029  -0.0384 7   VAL A CG1 
39   C CG2 . VAL A 21  ? 0.2840 0.3024 0.2826 0.0485  0.0002  -0.0472 7   VAL A CG2 
40   N N   . ALA A 22  ? 0.2951 0.3057 0.2749 0.0399  0.0015  -0.0450 8   ALA A N   
41   C CA  . ALA A 22  ? 0.3175 0.3262 0.2907 0.0366  0.0019  -0.0426 8   ALA A CA  
42   C C   . ALA A 22  ? 0.3175 0.3335 0.2850 0.0361  0.0050  -0.0460 8   ALA A C   
43   O O   . ALA A 22  ? 0.3074 0.3258 0.2691 0.0329  0.0073  -0.0426 8   ALA A O   
44   C CB  . ALA A 22  ? 0.3080 0.3086 0.2826 0.0371  -0.0019 -0.0432 8   ALA A CB  
45   N N   . ASP A 23  ? 0.3165 0.3363 0.2855 0.0393  0.0052  -0.0527 9   ASP A N   
46   C CA  . ASP A 23  ? 0.3350 0.3626 0.2979 0.0393  0.0084  -0.0562 9   ASP A CA  
47   C C   . ASP A 23  ? 0.3281 0.3641 0.2898 0.0374  0.0133  -0.0540 9   ASP A C   
48   O O   . ASP A 23  ? 0.3255 0.3662 0.2805 0.0351  0.0165  -0.0523 9   ASP A O   
49   C CB  . ASP A 23  ? 0.3384 0.3687 0.3039 0.0437  0.0073  -0.0646 9   ASP A CB  
50   C CG  . ASP A 23  ? 0.3449 0.3665 0.3135 0.0455  0.0022  -0.0672 9   ASP A CG  
51   O OD1 . ASP A 23  ? 0.3794 0.3963 0.3436 0.0434  0.0005  -0.0650 9   ASP A OD1 
52   O OD2 . ASP A 23  ? 0.3471 0.3664 0.3231 0.0489  -0.0003 -0.0713 9   ASP A OD2 
53   N N   . TYR A 24  ? 0.3131 0.3513 0.2819 0.0386  0.0138  -0.0541 10  TYR A N   
54   C CA  . TYR A 24  ? 0.3047 0.3509 0.2744 0.0367  0.0182  -0.0522 10  TYR A CA  
55   C C   . TYR A 24  ? 0.3155 0.3597 0.2812 0.0321  0.0193  -0.0449 10  TYR A C   
56   O O   . TYR A 24  ? 0.3151 0.3652 0.2775 0.0294  0.0234  -0.0429 10  TYR A O   
57   C CB  . TYR A 24  ? 0.2829 0.3307 0.2618 0.0391  0.0174  -0.0537 10  TYR A CB  
58   C CG  . TYR A 24  ? 0.2999 0.3568 0.2821 0.0377  0.0215  -0.0531 10  TYR A CG  
59   C CD1 . TYR A 24  ? 0.3133 0.3695 0.2964 0.0343  0.0222  -0.0473 10  TYR A CD1 
60   C CD2 . TYR A 24  ? 0.3035 0.3700 0.2890 0.0397  0.0247  -0.0587 10  TYR A CD2 
61   C CE1 . TYR A 24  ? 0.2833 0.3476 0.2708 0.0328  0.0257  -0.0471 10  TYR A CE1 
62   C CE2 . TYR A 24  ? 0.3018 0.3769 0.2917 0.0380  0.0287  -0.0582 10  TYR A CE2 
63   C CZ  . TYR A 24  ? 0.3090 0.3828 0.3002 0.0345  0.0290  -0.0523 10  TYR A CZ  
64   O OH  . TYR A 24  ? 0.3087 0.3910 0.3056 0.0327  0.0327  -0.0520 10  TYR A OH  
65   N N   . LEU A 25  ? 0.2884 0.3243 0.2547 0.0312  0.0159  -0.0409 11  LEU A N   
66   C CA  . LEU A 25  ? 0.2852 0.3189 0.2481 0.0272  0.0164  -0.0346 11  LEU A CA  
67   C C   . LEU A 25  ? 0.3051 0.3392 0.2596 0.0249  0.0178  -0.0334 11  LEU A C   
68   O O   . LEU A 25  ? 0.2899 0.3270 0.2413 0.0218  0.0206  -0.0296 11  LEU A O   
69   C CB  . LEU A 25  ? 0.2757 0.3010 0.2404 0.0271  0.0124  -0.0312 11  LEU A CB  
70   C CG  . LEU A 25  ? 0.2712 0.2932 0.2330 0.0236  0.0120  -0.0254 11  LEU A CG  
71   C CD1 . LEU A 25  ? 0.2494 0.2769 0.2126 0.0212  0.0149  -0.0229 11  LEU A CD1 
72   C CD2 . LEU A 25  ? 0.2612 0.2763 0.2256 0.0242  0.0085  -0.0227 11  LEU A CD2 
73   N N   . LEU A 26  ? 0.3142 0.3454 0.2650 0.0267  0.0158  -0.0366 12  LEU A N   
74   C CA  . LEU A 26  ? 0.3270 0.3587 0.2692 0.0252  0.0165  -0.0358 12  LEU A CA  
75   C C   . LEU A 26  ? 0.3519 0.3929 0.2900 0.0248  0.0214  -0.0371 12  LEU A C   
76   O O   . LEU A 26  ? 0.3473 0.3899 0.2786 0.0221  0.0235  -0.0333 12  LEU A O   
77   C CB  . LEU A 26  ? 0.3129 0.3401 0.2531 0.0276  0.0129  -0.0401 12  LEU A CB  
78   C CG  . LEU A 26  ? 0.3597 0.3776 0.3035 0.0273  0.0084  -0.0380 12  LEU A CG  
79   C CD1 . LEU A 26  ? 0.3666 0.3805 0.3109 0.0299  0.0047  -0.0431 12  LEU A CD1 
80   C CD2 . LEU A 26  ? 0.3083 0.3227 0.2482 0.0237  0.0079  -0.0318 12  LEU A CD2 
81   N N   . ASP A 27  ? 0.3295 0.3767 0.2716 0.0275  0.0234  -0.0422 13  ASP A N   
82   C CA  . ASP A 27  ? 0.3508 0.4081 0.2900 0.0270  0.0288  -0.0433 13  ASP A CA  
83   C C   . ASP A 27  ? 0.3581 0.4183 0.2990 0.0228  0.0323  -0.0372 13  ASP A C   
84   O O   . ASP A 27  ? 0.3420 0.4071 0.2774 0.0203  0.0363  -0.0342 13  ASP A O   
85   C CB  . ASP A 27  ? 0.3488 0.4125 0.2938 0.0309  0.0299  -0.0505 13  ASP A CB  
86   C CG  . ASP A 27  ? 0.3877 0.4526 0.3284 0.0346  0.0285  -0.0573 13  ASP A CG  
87   O OD1 . ASP A 27  ? 0.4162 0.4804 0.3478 0.0339  0.0284  -0.0564 13  ASP A OD1 
88   O OD2 . ASP A 27  ? 0.4026 0.4691 0.3491 0.0386  0.0271  -0.0639 13  ASP A OD2 
89   N N   . ARG A 28  ? 0.3264 0.3837 0.2752 0.0221  0.0307  -0.0351 14  ARG A N   
90   C CA  . ARG A 28  ? 0.3312 0.3910 0.2831 0.0184  0.0334  -0.0300 14  ARG A CA  
91   C C   . ARG A 28  ? 0.3390 0.3934 0.2846 0.0148  0.0326  -0.0237 14  ARG A C   
92   O O   . ARG A 28  ? 0.3611 0.4187 0.3061 0.0113  0.0358  -0.0193 14  ARG A O   
93   C CB  . ARG A 28  ? 0.3044 0.3624 0.2657 0.0192  0.0311  -0.0302 14  ARG A CB  
94   C CG  . ARG A 28  ? 0.3063 0.3705 0.2749 0.0224  0.0322  -0.0358 14  ARG A CG  
95   C CD  . ARG A 28  ? 0.3241 0.3989 0.2923 0.0216  0.0379  -0.0378 14  ARG A CD  
96   N NE  . ARG A 28  ? 0.3357 0.4177 0.3137 0.0227  0.0397  -0.0408 14  ARG A NE  
97   C CZ  . ARG A 28  ? 0.3464 0.4388 0.3269 0.0230  0.0446  -0.0441 14  ARG A CZ  
98   N NH1 . ARG A 28  ? 0.3532 0.4503 0.3262 0.0225  0.0483  -0.0448 14  ARG A NH1 
99   N NH2 . ARG A 28  ? 0.3444 0.4432 0.3352 0.0239  0.0457  -0.0469 14  ARG A NH2 
100  N N   . LEU A 29  ? 0.3360 0.3824 0.2778 0.0156  0.0282  -0.0231 15  LEU A N   
101  C CA  . LEU A 29  ? 0.3526 0.3939 0.2882 0.0127  0.0270  -0.0179 15  LEU A CA  
102  C C   . LEU A 29  ? 0.3748 0.4204 0.3017 0.0114  0.0304  -0.0163 15  LEU A C   
103  O O   . LEU A 29  ? 0.3623 0.4076 0.2864 0.0080  0.0319  -0.0107 15  LEU A O   
104  C CB  . LEU A 29  ? 0.3839 0.4173 0.3173 0.0143  0.0220  -0.0189 15  LEU A CB  
105  C CG  . LEU A 29  ? 0.3589 0.3855 0.2964 0.0132  0.0186  -0.0156 15  LEU A CG  
106  C CD1 . LEU A 29  ? 0.3482 0.3769 0.2943 0.0140  0.0190  -0.0164 15  LEU A CD1 
107  C CD2 . LEU A 29  ? 0.3447 0.3648 0.2811 0.0151  0.0143  -0.0175 15  LEU A CD2 
108  N N   . THR A 30  ? 0.3746 0.4243 0.2969 0.0142  0.0314  -0.0212 16  THR A N   
109  C CA  . THR A 30  ? 0.3788 0.4336 0.2918 0.0134  0.0348  -0.0199 16  THR A CA  
110  C C   . THR A 30  ? 0.3938 0.4564 0.3089 0.0106  0.0408  -0.0166 16  THR A C   
111  O O   . THR A 30  ? 0.4066 0.4704 0.3155 0.0077  0.0434  -0.0110 16  THR A O   
112  C CB  . THR A 30  ? 0.4173 0.4763 0.3257 0.0175  0.0349  -0.0269 16  THR A CB  
113  O OG1 . THR A 30  ? 0.5535 0.6194 0.4691 0.0195  0.0376  -0.0317 16  THR A OG1 
114  C CG2 . THR A 30  ? 0.3961 0.4477 0.3046 0.0203  0.0290  -0.0308 16  THR A CG2 
115  N N   . ASP A 31  ? 0.3905 0.4583 0.3148 0.0113  0.0429  -0.0197 17  ASP A N   
116  C CA  . ASP A 31  ? 0.3797 0.4556 0.3083 0.0085  0.0486  -0.0171 17  ASP A CA  
117  C C   . ASP A 31  ? 0.3558 0.4276 0.2862 0.0038  0.0488  -0.0095 17  ASP A C   
118  O O   . ASP A 31  ? 0.3510 0.4277 0.2805 0.0004  0.0535  -0.0050 17  ASP A O   
119  C CB  . ASP A 31  ? 0.3922 0.4729 0.3322 0.0103  0.0494  -0.0220 17  ASP A CB  
120  C CG  . ASP A 31  ? 0.4043 0.4906 0.3438 0.0149  0.0500  -0.0299 17  ASP A CG  
121  O OD1 . ASP A 31  ? 0.3985 0.4865 0.3287 0.0165  0.0506  -0.0318 17  ASP A OD1 
122  O OD2 . ASP A 31  ? 0.3780 0.4668 0.3267 0.0171  0.0494  -0.0345 17  ASP A OD2 
123  N N   . CYS A 32  ? 0.3704 0.4334 0.3035 0.0035  0.0437  -0.0079 18  CYS A N   
124  C CA  . CYS A 32  ? 0.3599 0.4187 0.2964 -0.0004 0.0430  -0.0017 18  CYS A CA  
125  C C   . CYS A 32  ? 0.3772 0.4310 0.3043 -0.0026 0.0421  0.0040  18  CYS A C   
126  O O   . CYS A 32  ? 0.3712 0.4216 0.3009 -0.0059 0.0416  0.0094  18  CYS A O   
127  C CB  . CYS A 32  ? 0.3395 0.3921 0.2830 0.0007  0.0379  -0.0030 18  CYS A CB  
128  S SG  . CYS A 32  ? 0.3013 0.3596 0.2574 0.0024  0.0387  -0.0078 18  CYS A SG  
129  N N   . GLY A 33  ? 0.3534 0.4068 0.2702 -0.0006 0.0415  0.0027  19  GLY A N   
130  C CA  . GLY A 33  ? 0.3830 0.4324 0.2900 -0.0021 0.0408  0.0079  19  GLY A CA  
131  C C   . GLY A 33  ? 0.3991 0.4404 0.3012 -0.0001 0.0348  0.0067  19  GLY A C   
132  O O   . GLY A 33  ? 0.3916 0.4294 0.2856 -0.0009 0.0333  0.0106  19  GLY A O   
133  N N   . ALA A 34  ? 0.3729 0.4111 0.2802 0.0025  0.0312  0.0018  20  ALA A N   
134  C CA  . ALA A 34  ? 0.3795 0.4104 0.2842 0.0042  0.0256  0.0004  20  ALA A CA  
135  C C   . ALA A 34  ? 0.3871 0.4196 0.2852 0.0077  0.0246  -0.0050 20  ALA A C   
136  O O   . ALA A 34  ? 0.4226 0.4595 0.3235 0.0102  0.0260  -0.0104 20  ALA A O   
137  C CB  . ALA A 34  ? 0.3418 0.3685 0.2558 0.0049  0.0225  -0.0016 20  ALA A CB  
138  N N   . ASP A 35  ? 0.3622 0.3911 0.2520 0.0082  0.0218  -0.0039 21  ASP A N   
139  C CA  . ASP A 35  ? 0.3829 0.4124 0.2669 0.0118  0.0196  -0.0096 21  ASP A CA  
140  C C   . ASP A 35  ? 0.3689 0.3907 0.2555 0.0130  0.0137  -0.0119 21  ASP A C   
141  O O   . ASP A 35  ? 0.3461 0.3674 0.2292 0.0158  0.0109  -0.0168 21  ASP A O   
142  C CB  . ASP A 35  ? 0.4148 0.4474 0.2865 0.0121  0.0209  -0.0076 21  ASP A CB  
143  C CG  . ASP A 35  ? 0.4404 0.4812 0.3092 0.0107  0.0275  -0.0051 21  ASP A CG  
144  O OD1 . ASP A 35  ? 0.4301 0.4769 0.3039 0.0119  0.0306  -0.0092 21  ASP A OD1 
145  O OD2 . ASP A 35  ? 0.4609 0.5023 0.3232 0.0083  0.0295  0.0013  21  ASP A OD2 
146  N N   . HIS A 36  ? 0.3287 0.3452 0.2220 0.0110  0.0117  -0.0086 22  HIS A N   
147  C CA  . HIS A 36  ? 0.3140 0.3238 0.2106 0.0116  0.0066  -0.0099 22  HIS A CA  
148  C C   . HIS A 36  ? 0.3091 0.3165 0.2158 0.0107  0.0063  -0.0091 22  HIS A C   
149  O O   . HIS A 36  ? 0.2915 0.3013 0.2019 0.0091  0.0092  -0.0064 22  HIS A O   
150  C CB  . HIS A 36  ? 0.3265 0.3320 0.2183 0.0102  0.0037  -0.0058 22  HIS A CB  
151  C CG  . HIS A 36  ? 0.3395 0.3468 0.2204 0.0115  0.0031  -0.0064 22  HIS A CG  
152  N ND1 . HIS A 36  ? 0.3507 0.3627 0.2242 0.0106  0.0071  -0.0030 22  HIS A ND1 
153  C CD2 . HIS A 36  ? 0.3358 0.3412 0.2119 0.0137  -0.0009 -0.0099 22  HIS A CD2 
154  C CE1 . HIS A 36  ? 0.3546 0.3677 0.2183 0.0125  0.0055  -0.0042 22  HIS A CE1 
155  N NE2 . HIS A 36  ? 0.3700 0.3790 0.2351 0.0145  0.0004  -0.0087 22  HIS A NE2 
156  N N   . LEU A 37  ? 0.2748 0.2776 0.1860 0.0119  0.0028  -0.0116 23  LEU A N   
157  C CA  . LEU A 37  ? 0.2820 0.2821 0.2018 0.0113  0.0020  -0.0105 23  LEU A CA  
158  C C   . LEU A 37  ? 0.2760 0.2706 0.1969 0.0105  -0.0019 -0.0089 23  LEU A C   
159  O O   . LEU A 37  ? 0.2810 0.2733 0.2004 0.0117  -0.0047 -0.0118 23  LEU A O   
160  C CB  . LEU A 37  ? 0.2534 0.2539 0.1787 0.0138  0.0019  -0.0149 23  LEU A CB  
161  C CG  . LEU A 37  ? 0.2746 0.2723 0.2079 0.0137  0.0011  -0.0136 23  LEU A CG  
162  C CD1 . LEU A 37  ? 0.2530 0.2536 0.1888 0.0122  0.0036  -0.0102 23  LEU A CD1 
163  C CD2 . LEU A 37  ? 0.2613 0.2585 0.1995 0.0164  0.0005  -0.0179 23  LEU A CD2 
164  N N   . PHE A 38  ? 0.2775 0.2705 0.2013 0.0086  -0.0021 -0.0048 24  PHE A N   
165  C CA  . PHE A 38  ? 0.2692 0.2579 0.1950 0.0079  -0.0054 -0.0034 24  PHE A CA  
166  C C   . PHE A 38  ? 0.2710 0.2580 0.2046 0.0083  -0.0060 -0.0038 24  PHE A C   
167  O O   . PHE A 38  ? 0.2631 0.2520 0.2002 0.0087  -0.0040 -0.0035 24  PHE A O   
168  C CB  . PHE A 38  ? 0.2656 0.2537 0.1899 0.0057  -0.0057 0.0010  24  PHE A CB  
169  C CG  . PHE A 38  ? 0.2704 0.2594 0.1868 0.0051  -0.0053 0.0026  24  PHE A CG  
170  C CD1 . PHE A 38  ? 0.2807 0.2735 0.1945 0.0042  -0.0016 0.0043  24  PHE A CD1 
171  C CD2 . PHE A 38  ? 0.2478 0.2341 0.1595 0.0053  -0.0085 0.0027  24  PHE A CD2 
172  C CE1 . PHE A 38  ? 0.2824 0.2763 0.1883 0.0035  -0.0007 0.0067  24  PHE A CE1 
173  C CE2 . PHE A 38  ? 0.2714 0.2584 0.1748 0.0050  -0.0083 0.0048  24  PHE A CE2 
174  C CZ  . PHE A 38  ? 0.2849 0.2756 0.1850 0.0040  -0.0042 0.0071  24  PHE A CZ  
175  N N   . GLY A 39  ? 0.2832 0.2668 0.2195 0.0083  -0.0089 -0.0042 25  GLY A N   
176  C CA  . GLY A 39  ? 0.2591 0.2414 0.2021 0.0084  -0.0090 -0.0032 25  GLY A CA  
177  C C   . GLY A 39  ? 0.2873 0.2663 0.2341 0.0085  -0.0116 -0.0046 25  GLY A C   
178  O O   . GLY A 39  ? 0.2681 0.2457 0.2127 0.0083  -0.0139 -0.0061 25  GLY A O   
179  N N   . VAL A 40  ? 0.2849 0.2629 0.2376 0.0089  -0.0111 -0.0037 26  VAL A N   
180  C CA  . VAL A 40  ? 0.2794 0.2545 0.2375 0.0086  -0.0129 -0.0042 26  VAL A CA  
181  C C   . VAL A 40  ? 0.2876 0.2611 0.2501 0.0099  -0.0121 -0.0049 26  VAL A C   
182  O O   . VAL A 40  ? 0.2721 0.2472 0.2352 0.0108  -0.0101 -0.0032 26  VAL A O   
183  C CB  . VAL A 40  ? 0.2749 0.2503 0.2361 0.0073  -0.0130 -0.0009 26  VAL A CB  
184  C CG1 . VAL A 40  ? 0.2642 0.2373 0.2323 0.0068  -0.0139 -0.0006 26  VAL A CG1 
185  C CG2 . VAL A 40  ? 0.2431 0.2193 0.2010 0.0062  -0.0146 -0.0005 26  VAL A CG2 
186  N N   . PRO A 41  ? 0.2911 0.2616 0.2572 0.0103  -0.0139 -0.0077 27  PRO A N   
187  C CA  . PRO A 41  ? 0.3166 0.2849 0.2876 0.0117  -0.0135 -0.0085 27  PRO A CA  
188  C C   . PRO A 41  ? 0.3090 0.2758 0.2856 0.0111  -0.0126 -0.0041 27  PRO A C   
189  O O   . PRO A 41  ? 0.3075 0.2747 0.2858 0.0094  -0.0125 -0.0014 27  PRO A O   
190  C CB  . PRO A 41  ? 0.3298 0.2951 0.3036 0.0121  -0.0163 -0.0131 27  PRO A CB  
191  C CG  . PRO A 41  ? 0.3684 0.3338 0.3415 0.0104  -0.0182 -0.0132 27  PRO A CG  
192  C CD  . PRO A 41  ? 0.3208 0.2898 0.2867 0.0098  -0.0168 -0.0109 27  PRO A CD  
193  N N   . GLY A 42  ? 0.3192 0.2845 0.2987 0.0127  -0.0118 -0.0035 28  GLY A N   
194  C CA  . GLY A 42  ? 0.3213 0.2845 0.3059 0.0125  -0.0110 0.0009  28  GLY A CA  
195  C C   . GLY A 42  ? 0.3327 0.2925 0.3211 0.0145  -0.0114 0.0000  28  GLY A C   
196  O O   . GLY A 42  ? 0.3131 0.2737 0.2994 0.0165  -0.0118 -0.0038 28  GLY A O   
197  N N   . ASP A 43  ? 0.3304 0.2866 0.3248 0.0142  -0.0114 0.0037  29  ASP A N   
198  C CA  . ASP A 43  ? 0.3764 0.3281 0.3757 0.0161  -0.0124 0.0030  29  ASP A CA  
199  C C   . ASP A 43  ? 0.3881 0.3420 0.3837 0.0191  -0.0117 0.0023  29  ASP A C   
200  O O   . ASP A 43  ? 0.4084 0.3602 0.4063 0.0213  -0.0130 -0.0014 29  ASP A O   
201  C CB  . ASP A 43  ? 0.3939 0.3414 0.3998 0.0150  -0.0120 0.0085  29  ASP A CB  
202  C CG  . ASP A 43  ? 0.3891 0.3389 0.3921 0.0158  -0.0097 0.0147  29  ASP A CG  
203  O OD1 . ASP A 43  ? 0.3535 0.3088 0.3505 0.0156  -0.0082 0.0155  29  ASP A OD1 
204  O OD2 . ASP A 43  ? 0.4325 0.3786 0.4392 0.0168  -0.0095 0.0188  29  ASP A OD2 
205  N N   . TYR A 44  ? 0.3323 0.2910 0.3227 0.0194  -0.0097 0.0049  30  TYR A N   
206  C CA  . TYR A 44  ? 0.3402 0.3017 0.3278 0.0222  -0.0091 0.0040  30  TYR A CA  
207  C C   . TYR A 44  ? 0.3346 0.2997 0.3189 0.0229  -0.0091 -0.0018 30  TYR A C   
208  O O   . TYR A 44  ? 0.3485 0.3159 0.3322 0.0253  -0.0087 -0.0035 30  TYR A O   
209  C CB  . TYR A 44  ? 0.3195 0.2852 0.3034 0.0224  -0.0074 0.0081  30  TYR A CB  
210  C CG  . TYR A 44  ? 0.3278 0.2914 0.3139 0.0225  -0.0070 0.0141  30  TYR A CG  
211  C CD1 . TYR A 44  ? 0.3473 0.3057 0.3379 0.0240  -0.0079 0.0163  30  TYR A CD1 
212  C CD2 . TYR A 44  ? 0.3092 0.2761 0.2928 0.0211  -0.0056 0.0177  30  TYR A CD2 
213  C CE1 . TYR A 44  ? 0.3434 0.3001 0.3353 0.0240  -0.0071 0.0226  30  TYR A CE1 
214  C CE2 . TYR A 44  ? 0.3151 0.2810 0.2999 0.0213  -0.0047 0.0234  30  TYR A CE2 
215  C CZ  . TYR A 44  ? 0.3371 0.2979 0.3257 0.0227  -0.0053 0.0262  30  TYR A CZ  
216  O OH  . TYR A 44  ? 0.3343 0.2944 0.3236 0.0228  -0.0040 0.0327  30  TYR A OH  
217  N N   . ASN A 45  ? 0.3290 0.2950 0.3108 0.0211  -0.0094 -0.0046 31  ASN A N   
218  C CA  . ASN A 45  ? 0.3330 0.3027 0.3110 0.0218  -0.0090 -0.0095 31  ASN A CA  
219  C C   . ASN A 45  ? 0.3648 0.3322 0.3441 0.0221  -0.0109 -0.0147 31  ASN A C   
220  O O   . ASN A 45  ? 0.3352 0.3062 0.3101 0.0226  -0.0105 -0.0187 31  ASN A O   
221  C CB  . ASN A 45  ? 0.3009 0.2753 0.2729 0.0199  -0.0074 -0.0085 31  ASN A CB  
222  C CG  . ASN A 45  ? 0.3129 0.2858 0.2838 0.0173  -0.0084 -0.0073 31  ASN A CG  
223  O OD1 . ASN A 45  ? 0.3099 0.2796 0.2827 0.0169  -0.0103 -0.0097 31  ASN A OD1 
224  N ND2 . ASN A 45  ? 0.2736 0.2488 0.2417 0.0157  -0.0075 -0.0042 31  ASN A ND2 
225  N N   . LEU A 46  ? 0.3650 0.3269 0.3502 0.0219  -0.0131 -0.0147 32  LEU A N   
226  C CA  . LEU A 46  ? 0.3864 0.3462 0.3732 0.0220  -0.0155 -0.0201 32  LEU A CA  
227  C C   . LEU A 46  ? 0.4038 0.3650 0.3908 0.0252  -0.0161 -0.0262 32  LEU A C   
228  O O   . LEU A 46  ? 0.4202 0.3838 0.4036 0.0258  -0.0168 -0.0314 32  LEU A O   
229  C CB  . LEU A 46  ? 0.4436 0.3971 0.4387 0.0209  -0.0178 -0.0190 32  LEU A CB  
230  C CG  . LEU A 46  ? 0.4292 0.3818 0.4252 0.0177  -0.0176 -0.0148 32  LEU A CG  
231  C CD1 . LEU A 46  ? 0.5180 0.4647 0.5233 0.0165  -0.0199 -0.0149 32  LEU A CD1 
232  C CD2 . LEU A 46  ? 0.4054 0.3620 0.3948 0.0165  -0.0177 -0.0170 32  LEU A CD2 
233  N N   . GLN A 47  ? 0.4101 0.3699 0.4010 0.0274  -0.0160 -0.0258 33  GLN A N   
234  C CA  . GLN A 47  ? 0.4425 0.4038 0.4346 0.0307  -0.0168 -0.0321 33  GLN A CA  
235  C C   . GLN A 47  ? 0.3973 0.3665 0.3818 0.0313  -0.0141 -0.0346 33  GLN A C   
236  O O   . GLN A 47  ? 0.3770 0.3494 0.3594 0.0330  -0.0144 -0.0407 33  GLN A O   
237  C CB  . GLN A 47  ? 0.4976 0.4555 0.4960 0.0332  -0.0176 -0.0309 33  GLN A CB  
238  C CG  . GLN A 47  ? 0.6441 0.5936 0.6509 0.0327  -0.0204 -0.0289 33  GLN A CG  
239  C CD  . GLN A 47  ? 0.8935 0.8387 0.9057 0.0345  -0.0210 -0.0249 33  GLN A CD  
240  O OE1 . GLN A 47  ? 0.8604 0.8089 0.8694 0.0356  -0.0191 -0.0219 33  GLN A OE1 
241  N NE2 . GLN A 47  ? 0.9115 0.8492 0.9323 0.0349  -0.0238 -0.0248 33  GLN A NE2 
242  N N   . PHE A 48  ? 0.3654 0.3383 0.3459 0.0299  -0.0114 -0.0298 34  PHE A N   
243  C CA  . PHE A 48  ? 0.3585 0.3387 0.3323 0.0295  -0.0085 -0.0311 34  PHE A CA  
244  C C   . PHE A 48  ? 0.3592 0.3406 0.3272 0.0279  -0.0088 -0.0332 34  PHE A C   
245  O O   . PHE A 48  ? 0.3354 0.3220 0.2987 0.0289  -0.0075 -0.0371 34  PHE A O   
246  C CB  . PHE A 48  ? 0.3039 0.2866 0.2756 0.0278  -0.0063 -0.0255 34  PHE A CB  
247  C CG  . PHE A 48  ? 0.2927 0.2819 0.2584 0.0265  -0.0034 -0.0256 34  PHE A CG  
248  C CD1 . PHE A 48  ? 0.2842 0.2793 0.2497 0.0282  -0.0012 -0.0288 34  PHE A CD1 
249  C CD2 . PHE A 48  ? 0.2989 0.2885 0.2599 0.0235  -0.0028 -0.0224 34  PHE A CD2 
250  C CE1 . PHE A 48  ? 0.2891 0.2903 0.2498 0.0266  0.0018  -0.0283 34  PHE A CE1 
251  C CE2 . PHE A 48  ? 0.2804 0.2754 0.2364 0.0222  -0.0002 -0.0218 34  PHE A CE2 
252  C CZ  . PHE A 48  ? 0.2887 0.2895 0.2445 0.0235  0.0023  -0.0245 34  PHE A CZ  
253  N N   . LEU A 49  ? 0.3490 0.3262 0.3173 0.0257  -0.0106 -0.0306 35  LEU A N   
254  C CA  . LEU A 49  ? 0.3729 0.3510 0.3359 0.0245  -0.0115 -0.0324 35  LEU A CA  
255  C C   . LEU A 49  ? 0.3797 0.3582 0.3427 0.0270  -0.0135 -0.0396 35  LEU A C   
256  O O   . LEU A 49  ? 0.4026 0.3847 0.3589 0.0272  -0.0134 -0.0423 35  LEU A O   
257  C CB  . LEU A 49  ? 0.3930 0.3664 0.3585 0.0221  -0.0136 -0.0291 35  LEU A CB  
258  C CG  . LEU A 49  ? 0.4070 0.3824 0.3673 0.0195  -0.0122 -0.0244 35  LEU A CG  
259  C CD1 . LEU A 49  ? 0.3807 0.3520 0.3451 0.0173  -0.0139 -0.0211 35  LEU A CD1 
260  C CD2 . LEU A 49  ? 0.3477 0.3267 0.2999 0.0194  -0.0120 -0.0268 35  LEU A CD2 
261  N N   . ASP A 50  ? 0.3965 0.3715 0.3670 0.0292  -0.0156 -0.0429 36  ASP A N   
262  C CA  . ASP A 50  ? 0.4152 0.3910 0.3865 0.0321  -0.0177 -0.0508 36  ASP A CA  
263  C C   . ASP A 50  ? 0.4286 0.4122 0.3935 0.0342  -0.0149 -0.0544 36  ASP A C   
264  O O   . ASP A 50  ? 0.4234 0.4103 0.3844 0.0362  -0.0157 -0.0605 36  ASP A O   
265  C CB  . ASP A 50  ? 0.4470 0.4173 0.4285 0.0343  -0.0204 -0.0534 36  ASP A CB  
266  C CG  . ASP A 50  ? 0.4885 0.4511 0.4774 0.0323  -0.0234 -0.0509 36  ASP A CG  
267  O OD1 . ASP A 50  ? 0.5010 0.4628 0.4875 0.0300  -0.0243 -0.0496 36  ASP A OD1 
268  O OD2 . ASP A 50  ? 0.5066 0.4639 0.5041 0.0332  -0.0249 -0.0502 36  ASP A OD2 
269  N N   . HIS A 51  ? 0.4113 0.3985 0.3755 0.0341  -0.0114 -0.0512 37  HIS A N   
270  C CA  . HIS A 51  ? 0.4069 0.4023 0.3657 0.0356  -0.0081 -0.0542 37  HIS A CA  
271  C C   . HIS A 51  ? 0.4072 0.4072 0.3563 0.0332  -0.0057 -0.0517 37  HIS A C   
272  O O   . HIS A 51  ? 0.4157 0.4222 0.3588 0.0346  -0.0038 -0.0553 37  HIS A O   
273  C CB  . HIS A 51  ? 0.3698 0.3679 0.3323 0.0361  -0.0055 -0.0520 37  HIS A CB  
274  C CG  . HIS A 51  ? 0.3726 0.3674 0.3438 0.0393  -0.0078 -0.0555 37  HIS A CG  
275  N ND1 . HIS A 51  ? 0.3623 0.3619 0.3355 0.0430  -0.0074 -0.0622 37  HIS A ND1 
276  C CD2 . HIS A 51  ? 0.3740 0.3612 0.3526 0.0396  -0.0107 -0.0532 37  HIS A CD2 
277  C CE1 . HIS A 51  ? 0.3898 0.3842 0.3715 0.0454  -0.0103 -0.0640 37  HIS A CE1 
278  N NE2 . HIS A 51  ? 0.3939 0.3806 0.3788 0.0434  -0.0123 -0.0583 37  HIS A NE2 
279  N N   . VAL A 52  ? 0.3860 0.3829 0.3335 0.0299  -0.0058 -0.0454 38  VAL A N   
280  C CA  . VAL A 52  ? 0.3900 0.3900 0.3288 0.0278  -0.0042 -0.0425 38  VAL A CA  
281  C C   . VAL A 52  ? 0.4131 0.4128 0.3468 0.0290  -0.0069 -0.0470 38  VAL A C   
282  O O   . VAL A 52  ? 0.3802 0.3852 0.3054 0.0293  -0.0052 -0.0479 38  VAL A O   
283  C CB  . VAL A 52  ? 0.3660 0.3621 0.3053 0.0244  -0.0045 -0.0355 38  VAL A CB  
284  C CG1 . VAL A 52  ? 0.3356 0.3337 0.2665 0.0223  -0.0036 -0.0325 38  VAL A CG1 
285  C CG2 . VAL A 52  ? 0.3306 0.3275 0.2744 0.0236  -0.0021 -0.0317 38  VAL A CG2 
286  N N   . ILE A 53  ? 0.4263 0.4203 0.3655 0.0298  -0.0112 -0.0497 39  ILE A N   
287  C CA  . ILE A 53  ? 0.4553 0.4489 0.3909 0.0312  -0.0145 -0.0548 39  ILE A CA  
288  C C   . ILE A 53  ? 0.4700 0.4695 0.4022 0.0349  -0.0139 -0.0621 39  ILE A C   
289  O O   . ILE A 53  ? 0.4657 0.4695 0.3891 0.0361  -0.0140 -0.0648 39  ILE A O   
290  C CB  . ILE A 53  ? 0.4904 0.4766 0.4349 0.0311  -0.0192 -0.0565 39  ILE A CB  
291  C CG1 . ILE A 53  ? 0.4650 0.4470 0.4110 0.0274  -0.0196 -0.0496 39  ILE A CG1 
292  C CG2 . ILE A 53  ? 0.4869 0.4733 0.4298 0.0335  -0.0233 -0.0638 39  ILE A CG2 
293  C CD1 . ILE A 53  ? 0.5148 0.4974 0.4538 0.0264  -0.0214 -0.0491 39  ILE A CD1 
294  N N   . ASP A 54  ? 0.4771 0.4770 0.4160 0.0372  -0.0134 -0.0656 40  ASP A N   
295  C CA  . ASP A 54  ? 0.4629 0.4687 0.4000 0.0412  -0.0130 -0.0735 40  ASP A CA  
296  C C   . ASP A 54  ? 0.4812 0.4963 0.4092 0.0412  -0.0077 -0.0724 40  ASP A C   
297  O O   . ASP A 54  ? 0.5052 0.5269 0.4282 0.0443  -0.0070 -0.0785 40  ASP A O   
298  C CB  . ASP A 54  ? 0.4881 0.4914 0.4358 0.0436  -0.0142 -0.0773 40  ASP A CB  
299  C CG  . ASP A 54  ? 0.5503 0.5448 0.5075 0.0440  -0.0196 -0.0797 40  ASP A CG  
300  O OD1 . ASP A 54  ? 0.5439 0.5353 0.4994 0.0430  -0.0227 -0.0801 40  ASP A OD1 
301  O OD2 . ASP A 54  ? 0.5705 0.5610 0.5372 0.0454  -0.0210 -0.0809 40  ASP A OD2 
302  N N   . SER A 55  ? 0.4642 0.4805 0.3904 0.0380  -0.0040 -0.0648 41  SER A N   
303  C CA  . SER A 55  ? 0.4552 0.4802 0.3745 0.0375  0.0014  -0.0632 41  SER A CA  
304  C C   . SER A 55  ? 0.4682 0.4973 0.3756 0.0376  0.0020  -0.0635 41  SER A C   
305  O O   . SER A 55  ? 0.4859 0.5105 0.3895 0.0358  -0.0004 -0.0600 41  SER A O   
306  C CB  . SER A 55  ? 0.4454 0.4697 0.3664 0.0337  0.0045  -0.0550 41  SER A CB  
307  O OG  . SER A 55  ? 0.4429 0.4746 0.3569 0.0322  0.0095  -0.0519 41  SER A OG  
308  N N   . PRO A 56  ? 0.5024 0.5405 0.4035 0.0400  0.0052  -0.0676 42  PRO A N   
309  C CA  . PRO A 56  ? 0.4953 0.5379 0.3835 0.0400  0.0064  -0.0664 42  PRO A CA  
310  C C   . PRO A 56  ? 0.4860 0.5305 0.3687 0.0358  0.0108  -0.0571 42  PRO A C   
311  O O   . PRO A 56  ? 0.5171 0.5635 0.3891 0.0352  0.0114  -0.0543 42  PRO A O   
312  C CB  . PRO A 56  ? 0.4832 0.5357 0.3673 0.0442  0.0089  -0.0740 42  PRO A CB  
313  C CG  . PRO A 56  ? 0.5029 0.5573 0.3979 0.0452  0.0108  -0.0770 42  PRO A CG  
314  C CD  . PRO A 56  ? 0.4626 0.5079 0.3675 0.0422  0.0088  -0.0717 42  PRO A CD  
315  N N   . ASP A 57  ? 0.4784 0.5222 0.3682 0.0331  0.0136  -0.0525 43  ASP A N   
316  C CA  . ASP A 57  ? 0.4599 0.5062 0.3464 0.0291  0.0182  -0.0445 43  ASP A CA  
317  C C   . ASP A 57  ? 0.4495 0.4877 0.3388 0.0254  0.0160  -0.0374 43  ASP A C   
318  O O   . ASP A 57  ? 0.4487 0.4876 0.3337 0.0223  0.0185  -0.0307 43  ASP A O   
319  C CB  . ASP A 57  ? 0.4860 0.5384 0.3793 0.0287  0.0230  -0.0447 43  ASP A CB  
320  C CG  . ASP A 57  ? 0.5037 0.5665 0.3932 0.0317  0.0268  -0.0503 43  ASP A CG  
321  O OD1 . ASP A 57  ? 0.5304 0.5956 0.4120 0.0346  0.0255  -0.0547 43  ASP A OD1 
322  O OD2 . ASP A 57  ? 0.6050 0.6740 0.4998 0.0314  0.0311  -0.0508 43  ASP A OD2 
323  N N   . ILE A 58  ? 0.4314 0.4620 0.3277 0.0258  0.0114  -0.0387 44  ILE A N   
324  C CA  . ILE A 58  ? 0.3969 0.4205 0.2968 0.0226  0.0094  -0.0327 44  ILE A CA  
325  C C   . ILE A 58  ? 0.3955 0.4127 0.2946 0.0234  0.0039  -0.0344 44  ILE A C   
326  O O   . ILE A 58  ? 0.4130 0.4280 0.3162 0.0260  0.0009  -0.0402 44  ILE A O   
327  C CB  . ILE A 58  ? 0.3846 0.4060 0.2952 0.0220  0.0096  -0.0318 44  ILE A CB  
328  C CG1 . ILE A 58  ? 0.4007 0.4291 0.3136 0.0218  0.0146  -0.0316 44  ILE A CG1 
329  C CG2 . ILE A 58  ? 0.3618 0.3775 0.2752 0.0188  0.0082  -0.0255 44  ILE A CG2 
330  C CD1 . ILE A 58  ? 0.3739 0.4045 0.2842 0.0181  0.0179  -0.0249 44  ILE A CD1 
331  N N   . CYS A 59  ? 0.3684 0.3823 0.2631 0.0212  0.0025  -0.0294 45  CYS A N   
332  C CA  . CYS A 59  ? 0.3817 0.3900 0.2757 0.0216  -0.0027 -0.0306 45  CYS A CA  
333  C C   . CYS A 59  ? 0.3617 0.3639 0.2636 0.0192  -0.0045 -0.0267 45  CYS A C   
334  O O   . CYS A 59  ? 0.3205 0.3220 0.2222 0.0165  -0.0029 -0.0208 45  CYS A O   
335  C CB  . CYS A 59  ? 0.3683 0.3778 0.2514 0.0214  -0.0034 -0.0283 45  CYS A CB  
336  S SG  . CYS A 59  ? 0.4396 0.4422 0.3229 0.0211  -0.0097 -0.0281 45  CYS A SG  
337  N N   . TRP A 60  ? 0.3230 0.3208 0.2321 0.0202  -0.0079 -0.0300 46  TRP A N   
338  C CA  . TRP A 60  ? 0.3310 0.3235 0.2472 0.0181  -0.0096 -0.0264 46  TRP A CA  
339  C C   . TRP A 60  ? 0.3426 0.3324 0.2551 0.0166  -0.0122 -0.0235 46  TRP A C   
340  O O   . TRP A 60  ? 0.3305 0.3200 0.2384 0.0179  -0.0151 -0.0264 46  TRP A O   
341  C CB  . TRP A 60  ? 0.3282 0.3168 0.2530 0.0194  -0.0123 -0.0303 46  TRP A CB  
342  C CG  . TRP A 60  ? 0.3379 0.3216 0.2692 0.0175  -0.0141 -0.0269 46  TRP A CG  
343  C CD1 . TRP A 60  ? 0.3502 0.3300 0.2849 0.0171  -0.0179 -0.0281 46  TRP A CD1 
344  C CD2 . TRP A 60  ? 0.3142 0.2971 0.2499 0.0157  -0.0121 -0.0220 46  TRP A CD2 
345  N NE1 . TRP A 60  ? 0.3611 0.3381 0.3019 0.0151  -0.0179 -0.0240 46  TRP A NE1 
346  C CE2 . TRP A 60  ? 0.3316 0.3104 0.2727 0.0144  -0.0145 -0.0203 46  TRP A CE2 
347  C CE3 . TRP A 60  ? 0.3008 0.2866 0.2369 0.0153  -0.0086 -0.0193 46  TRP A CE3 
348  C CZ2 . TRP A 60  ? 0.3140 0.2917 0.2596 0.0129  -0.0133 -0.0159 46  TRP A CZ2 
349  C CZ3 . TRP A 60  ? 0.2910 0.2753 0.2318 0.0139  -0.0080 -0.0152 46  TRP A CZ3 
350  C CH2 . TRP A 60  ? 0.2902 0.2707 0.2353 0.0129  -0.0103 -0.0135 46  TRP A CH2 
351  N N   . VAL A 61  ? 0.3090 0.2972 0.2237 0.0141  -0.0115 -0.0181 47  VAL A N   
352  C CA  . VAL A 61  ? 0.3166 0.3018 0.2295 0.0128  -0.0143 -0.0153 47  VAL A CA  
353  C C   . VAL A 61  ? 0.3075 0.2893 0.2294 0.0115  -0.0156 -0.0138 47  VAL A C   
354  O O   . VAL A 61  ? 0.2805 0.2626 0.2054 0.0100  -0.0136 -0.0100 47  VAL A O   
355  C CB  . VAL A 61  ? 0.3135 0.3003 0.2201 0.0111  -0.0125 -0.0102 47  VAL A CB  
356  C CG1 . VAL A 61  ? 0.3229 0.3065 0.2274 0.0103  -0.0162 -0.0080 47  VAL A CG1 
357  C CG2 . VAL A 61  ? 0.3113 0.3025 0.2091 0.0123  -0.0102 -0.0111 47  VAL A CG2 
358  N N   . GLY A 62  ? 0.3148 0.2937 0.2413 0.0121  -0.0189 -0.0168 48  GLY A N   
359  C CA  . GLY A 62  ? 0.3177 0.2939 0.2525 0.0107  -0.0198 -0.0149 48  GLY A CA  
360  C C   . GLY A 62  ? 0.2913 0.2668 0.2250 0.0091  -0.0212 -0.0114 48  GLY A C   
361  O O   . GLY A 62  ? 0.3207 0.2958 0.2495 0.0094  -0.0238 -0.0121 48  GLY A O   
362  N N   . CYS A 63  ? 0.2999 0.2753 0.2378 0.0078  -0.0197 -0.0079 49  CYS A N   
363  C CA  . CYS A 63  ? 0.2638 0.2389 0.2017 0.0065  -0.0210 -0.0049 49  CYS A CA  
364  C C   . CYS A 63  ? 0.2770 0.2509 0.2228 0.0058  -0.0224 -0.0049 49  CYS A C   
365  O O   . CYS A 63  ? 0.2653 0.2386 0.2168 0.0059  -0.0215 -0.0057 49  CYS A O   
366  C CB  . CYS A 63  ? 0.2697 0.2465 0.2061 0.0056  -0.0183 -0.0012 49  CYS A CB  
367  S SG  . CYS A 63  ? 0.3251 0.3040 0.2529 0.0057  -0.0160 -0.0002 49  CYS A SG  
368  N N   . ALA A 64  ? 0.2722 0.2457 0.2183 0.0051  -0.0246 -0.0037 50  ALA A N   
369  C CA  . ALA A 64  ? 0.2568 0.2301 0.2106 0.0045  -0.0260 -0.0040 50  ALA A CA  
370  C C   . ALA A 64  ? 0.2530 0.2280 0.2116 0.0038  -0.0233 -0.0012 50  ALA A C   
371  O O   . ALA A 64  ? 0.2840 0.2595 0.2494 0.0033  -0.0232 -0.0013 50  ALA A O   
372  C CB  . ALA A 64  ? 0.2683 0.2412 0.2213 0.0044  -0.0297 -0.0043 50  ALA A CB  
373  N N   . ASN A 65  ? 0.2698 0.2463 0.2256 0.0039  -0.0212 0.0011  51  ASN A N   
374  C CA  . ASN A 65  ? 0.2565 0.2350 0.2160 0.0039  -0.0184 0.0030  51  ASN A CA  
375  C C   . ASN A 65  ? 0.2480 0.2277 0.2037 0.0043  -0.0163 0.0042  51  ASN A C   
376  O O   . ASN A 65  ? 0.2441 0.2233 0.1946 0.0041  -0.0166 0.0042  51  ASN A O   
377  C CB  . ASN A 65  ? 0.2238 0.2043 0.1879 0.0036  -0.0189 0.0042  51  ASN A CB  
378  C CG  . ASN A 65  ? 0.2509 0.2319 0.2127 0.0034  -0.0206 0.0049  51  ASN A CG  
379  O OD1 . ASN A 65  ? 0.2388 0.2194 0.1963 0.0034  -0.0202 0.0058  51  ASN A OD1 
380  N ND2 . ASN A 65  ? 0.2159 0.1979 0.1814 0.0033  -0.0226 0.0045  51  ASN A ND2 
381  N N   . GLU A 66  ? 0.2259 0.2076 0.1843 0.0049  -0.0140 0.0055  52  GLU A N   
382  C CA  . GLU A 66  ? 0.2297 0.2130 0.1859 0.0054  -0.0120 0.0061  52  GLU A CA  
383  C C   . GLU A 66  ? 0.2302 0.2148 0.1850 0.0048  -0.0124 0.0073  52  GLU A C   
384  O O   . GLU A 66  ? 0.2278 0.2131 0.1800 0.0045  -0.0112 0.0076  52  GLU A O   
385  C CB  . GLU A 66  ? 0.2253 0.2102 0.1848 0.0066  -0.0101 0.0069  52  GLU A CB  
386  C CG  . GLU A 66  ? 0.2395 0.2226 0.2004 0.0073  -0.0094 0.0060  52  GLU A CG  
387  C CD  . GLU A 66  ? 0.2478 0.2293 0.2129 0.0069  -0.0102 0.0065  52  GLU A CD  
388  O OE1 . GLU A 66  ? 0.2050 0.1874 0.1717 0.0061  -0.0111 0.0073  52  GLU A OE1 
389  O OE2 . GLU A 66  ? 0.2219 0.2014 0.1894 0.0074  -0.0098 0.0061  52  GLU A OE2 
390  N N   . LEU A 67  ? 0.2368 0.2220 0.1941 0.0045  -0.0139 0.0079  53  LEU A N   
391  C CA  . LEU A 67  ? 0.2339 0.2196 0.1907 0.0040  -0.0148 0.0088  53  LEU A CA  
392  C C   . LEU A 67  ? 0.2231 0.2062 0.1752 0.0029  -0.0159 0.0093  53  LEU A C   
393  O O   . LEU A 67  ? 0.2218 0.2052 0.1719 0.0021  -0.0150 0.0105  53  LEU A O   
394  C CB  . LEU A 67  ? 0.2006 0.1874 0.1612 0.0042  -0.0168 0.0086  53  LEU A CB  
395  C CG  . LEU A 67  ? 0.2243 0.2111 0.1857 0.0038  -0.0185 0.0092  53  LEU A CG  
396  C CD1 . LEU A 67  ? 0.2187 0.2078 0.1813 0.0040  -0.0167 0.0095  53  LEU A CD1 
397  C CD2 . LEU A 67  ? 0.2041 0.1922 0.1698 0.0045  -0.0208 0.0082  53  LEU A CD2 
398  N N   . ASN A 68  ? 0.2302 0.2110 0.1804 0.0028  -0.0179 0.0085  54  ASN A N   
399  C CA  . ASN A 68  ? 0.2273 0.2058 0.1718 0.0022  -0.0193 0.0091  54  ASN A CA  
400  C C   . ASN A 68  ? 0.2141 0.1933 0.1540 0.0022  -0.0166 0.0090  54  ASN A C   
401  O O   . ASN A 68  ? 0.2377 0.2164 0.1727 0.0015  -0.0163 0.0107  54  ASN A O   
402  C CB  . ASN A 68  ? 0.2412 0.2177 0.1849 0.0026  -0.0222 0.0074  54  ASN A CB  
403  C CG  . ASN A 68  ? 0.2314 0.2078 0.1798 0.0027  -0.0250 0.0072  54  ASN A CG  
404  O OD1 . ASN A 68  ? 0.2349 0.2125 0.1866 0.0026  -0.0249 0.0082  54  ASN A OD1 
405  N ND2 . ASN A 68  ? 0.2399 0.2152 0.1891 0.0031  -0.0276 0.0053  54  ASN A ND2 
406  N N   . ALA A 69  ? 0.2065 0.1869 0.1479 0.0030  -0.0149 0.0072  55  ALA A N   
407  C CA  . ALA A 69  ? 0.2198 0.2015 0.1577 0.0034  -0.0124 0.0064  55  ALA A CA  
408  C C   . ALA A 69  ? 0.2196 0.2037 0.1577 0.0025  -0.0099 0.0084  55  ALA A C   
409  O O   . ALA A 69  ? 0.2514 0.2366 0.1852 0.0020  -0.0082 0.0091  55  ALA A O   
410  C CB  . ALA A 69  ? 0.2027 0.1849 0.1437 0.0047  -0.0113 0.0040  55  ALA A CB  
411  N N   . SER A 70  ? 0.2138 0.1990 0.1570 0.0024  -0.0097 0.0092  56  SER A N   
412  C CA  . SER A 70  ? 0.2329 0.2206 0.1778 0.0017  -0.0077 0.0105  56  SER A CA  
413  C C   . SER A 70  ? 0.2422 0.2285 0.1852 -0.0001 -0.0086 0.0131  56  SER A C   
414  O O   . SER A 70  ? 0.2453 0.2331 0.1875 -0.0013 -0.0065 0.0146  56  SER A O   
415  C CB  . SER A 70  ? 0.2297 0.2195 0.1807 0.0026  -0.0078 0.0100  56  SER A CB  
416  O OG  . SER A 70  ? 0.2101 0.1988 0.1637 0.0025  -0.0103 0.0105  56  SER A OG  
417  N N   . TYR A 71  ? 0.2424 0.2258 0.1850 -0.0003 -0.0118 0.0139  57  TYR A N   
418  C CA  . TYR A 71  ? 0.2320 0.2129 0.1720 -0.0018 -0.0132 0.0168  57  TYR A CA  
419  C C   . TYR A 71  ? 0.2473 0.2277 0.1796 -0.0023 -0.0119 0.0180  57  TYR A C   
420  O O   . TYR A 71  ? 0.2378 0.2181 0.1677 -0.0039 -0.0106 0.0211  57  TYR A O   
421  C CB  . TYR A 71  ? 0.2371 0.2150 0.1781 -0.0014 -0.0173 0.0168  57  TYR A CB  
422  C CG  . TYR A 71  ? 0.2247 0.2034 0.1729 -0.0009 -0.0190 0.0158  57  TYR A CG  
423  C CD1 . TYR A 71  ? 0.2117 0.1926 0.1649 -0.0012 -0.0178 0.0159  57  TYR A CD1 
424  C CD2 . TYR A 71  ? 0.1979 0.1755 0.1481 0.0002  -0.0220 0.0144  57  TYR A CD2 
425  C CE1 . TYR A 71  ? 0.2137 0.1959 0.1730 -0.0002 -0.0196 0.0143  57  TYR A CE1 
426  C CE2 . TYR A 71  ? 0.2198 0.1990 0.1762 0.0009  -0.0234 0.0131  57  TYR A CE2 
427  C CZ  . TYR A 71  ? 0.1922 0.1737 0.1528 0.0009  -0.0223 0.0130  57  TYR A CZ  
428  O OH  . TYR A 71  ? 0.2156 0.1993 0.1819 0.0021  -0.0240 0.0111  57  TYR A OH  
429  N N   . ALA A 72  ? 0.2571 0.2374 0.1855 -0.0009 -0.0123 0.0156  58  ALA A N   
430  C CA  . ALA A 72  ? 0.2644 0.2449 0.1848 -0.0007 -0.0113 0.0160  58  ALA A CA  
431  C C   . ALA A 72  ? 0.2624 0.2468 0.1817 -0.0014 -0.0068 0.0164  58  ALA A C   
432  O O   . ALA A 72  ? 0.2530 0.2383 0.1668 -0.0024 -0.0051 0.0190  58  ALA A O   
433  C CB  . ALA A 72  ? 0.2424 0.2223 0.1606 0.0012  -0.0131 0.0122  58  ALA A CB  
434  N N   . ALA A 73  ? 0.2621 0.2493 0.1868 -0.0007 -0.0048 0.0141  59  ALA A N   
435  C CA  . ALA A 73  ? 0.2507 0.2422 0.1758 -0.0012 -0.0007 0.0141  59  ALA A CA  
436  C C   . ALA A 73  ? 0.2456 0.2378 0.1726 -0.0037 0.0008  0.0180  59  ALA A C   
437  O O   . ALA A 73  ? 0.2397 0.2348 0.1640 -0.0049 0.0041  0.0197  59  ALA A O   
438  C CB  . ALA A 73  ? 0.2447 0.2385 0.1759 0.0002  0.0004  0.0110  59  ALA A CB  
439  N N   . ASP A 74  ? 0.2255 0.2153 0.1578 -0.0045 -0.0015 0.0194  60  ASP A N   
440  C CA  . ASP A 74  ? 0.2338 0.2234 0.1693 -0.0069 -0.0008 0.0230  60  ASP A CA  
441  C C   . ASP A 74  ? 0.2529 0.2405 0.1814 -0.0086 -0.0004 0.0273  60  ASP A C   
442  O O   . ASP A 74  ? 0.2401 0.2300 0.1681 -0.0106 0.0029  0.0302  60  ASP A O   
443  C CB  . ASP A 74  ? 0.2492 0.2362 0.1912 -0.0069 -0.0043 0.0229  60  ASP A CB  
444  C CG  . ASP A 74  ? 0.2235 0.2103 0.1712 -0.0092 -0.0040 0.0256  60  ASP A CG  
445  O OD1 . ASP A 74  ? 0.2331 0.2175 0.1779 -0.0112 -0.0039 0.0297  60  ASP A OD1 
446  O OD2 . ASP A 74  ? 0.2538 0.2428 0.2092 -0.0089 -0.0043 0.0236  60  ASP A OD2 
447  N N   . GLY A 75  ? 0.2521 0.2357 0.1750 -0.0076 -0.0038 0.0278  61  GLY A N   
448  C CA  . GLY A 75  ? 0.2495 0.2311 0.1645 -0.0086 -0.0039 0.0321  61  GLY A CA  
449  C C   . GLY A 75  ? 0.2752 0.2610 0.1829 -0.0085 0.0003  0.0323  61  GLY A C   
450  O O   . GLY A 75  ? 0.2540 0.2405 0.1573 -0.0103 0.0027  0.0368  61  GLY A O   
451  N N   . TYR A 76  ? 0.2580 0.2469 0.1645 -0.0063 0.0012  0.0273  62  TYR A N   
452  C CA  . TYR A 76  ? 0.2757 0.2696 0.1763 -0.0056 0.0052  0.0262  62  TYR A CA  
453  C C   . TYR A 76  ? 0.2779 0.2764 0.1828 -0.0079 0.0102  0.0283  62  TYR A C   
454  O O   . TYR A 76  ? 0.2571 0.2587 0.1566 -0.0092 0.0138  0.0315  62  TYR A O   
455  C CB  . TYR A 76  ? 0.2732 0.2689 0.1745 -0.0028 0.0046  0.0199  62  TYR A CB  
456  C CG  . TYR A 76  ? 0.2988 0.2997 0.1948 -0.0012 0.0078  0.0170  62  TYR A CG  
457  C CD1 . TYR A 76  ? 0.2821 0.2885 0.1822 -0.0015 0.0122  0.0155  62  TYR A CD1 
458  C CD2 . TYR A 76  ? 0.3092 0.3100 0.1966 0.0010  0.0061  0.0148  62  TYR A CD2 
459  C CE1 . TYR A 76  ? 0.2960 0.3078 0.1918 0.0003  0.0150  0.0121  62  TYR A CE1 
460  C CE2 . TYR A 76  ? 0.3184 0.3244 0.2010 0.0029  0.0087  0.0112  62  TYR A CE2 
461  C CZ  . TYR A 76  ? 0.3434 0.3550 0.2303 0.0026  0.0133  0.0099  62  TYR A CZ  
462  O OH  . TYR A 76  ? 0.3268 0.3441 0.2096 0.0048  0.0159  0.0057  62  TYR A OH  
463  N N   . ALA A 77  ? 0.2510 0.2504 0.1659 -0.0085 0.0105  0.0268  63  ALA A N   
464  C CA  . ALA A 77  ? 0.2605 0.2647 0.1811 -0.0106 0.0148  0.0280  63  ALA A CA  
465  C C   . ALA A 77  ? 0.2538 0.2565 0.1746 -0.0141 0.0160  0.0345  63  ALA A C   
466  O O   . ALA A 77  ? 0.2684 0.2757 0.1905 -0.0162 0.0206  0.0367  63  ALA A O   
467  C CB  . ALA A 77  ? 0.2506 0.2556 0.1818 -0.0102 0.0139  0.0249  63  ALA A CB  
468  N N   . ARG A 78  ? 0.2707 0.2670 0.1908 -0.0147 0.0120  0.0376  64  ARG A N   
469  C CA  . ARG A 78  ? 0.2560 0.2498 0.1759 -0.0179 0.0127  0.0442  64  ARG A CA  
470  C C   . ARG A 78  ? 0.2812 0.2759 0.1893 -0.0182 0.0150  0.0484  64  ARG A C   
471  O O   . ARG A 78  ? 0.2878 0.2810 0.1947 -0.0211 0.0166  0.0548  64  ARG A O   
472  C CB  . ARG A 78  ? 0.2527 0.2393 0.1758 -0.0181 0.0072  0.0459  64  ARG A CB  
473  C CG  . ARG A 78  ? 0.2603 0.2467 0.1953 -0.0180 0.0050  0.0424  64  ARG A CG  
474  C CD  . ARG A 78  ? 0.2592 0.2390 0.1973 -0.0180 -0.0003 0.0439  64  ARG A CD  
475  N NE  . ARG A 78  ? 0.2450 0.2248 0.1925 -0.0169 -0.0031 0.0397  64  ARG A NE  
476  C CZ  . ARG A 78  ? 0.2464 0.2226 0.2011 -0.0178 -0.0064 0.0406  64  ARG A CZ  
477  N NH1 . ARG A 78  ? 0.2395 0.2113 0.1942 -0.0201 -0.0073 0.0460  64  ARG A NH1 
478  N NH2 . ARG A 78  ? 0.2266 0.2037 0.1886 -0.0161 -0.0090 0.0361  64  ARG A NH2 
479  N N   . CYS A 79  ? 0.2681 0.2649 0.1676 -0.0153 0.0151  0.0449  65  CYS A N   
480  C CA  . CYS A 79  ? 0.3276 0.3268 0.2153 -0.0150 0.0176  0.0479  65  CYS A CA  
481  C C   . CYS A 79  ? 0.3210 0.3288 0.2074 -0.0149 0.0237  0.0455  65  CYS A C   
482  O O   . CYS A 79  ? 0.3386 0.3503 0.2190 -0.0163 0.0280  0.0499  65  CYS A O   
483  C CB  . CYS A 79  ? 0.3081 0.3045 0.1864 -0.0115 0.0132  0.0452  65  CYS A CB  
484  S SG  . CYS A 79  ? 0.3660 0.3530 0.2438 -0.0115 0.0064  0.0485  65  CYS A SG  
485  N N   . LYS A 80  ? 0.3320 0.3432 0.2243 -0.0130 0.0240  0.0389  66  LYS A N   
486  C CA  . LYS A 80  ? 0.3555 0.3751 0.2469 -0.0120 0.0290  0.0354  66  LYS A CA  
487  C C   . LYS A 80  ? 0.3682 0.3924 0.2712 -0.0140 0.0326  0.0344  66  LYS A C   
488  O O   . LYS A 80  ? 0.3827 0.4146 0.2861 -0.0134 0.0372  0.0317  66  LYS A O   
489  C CB  . LYS A 80  ? 0.3470 0.3673 0.2353 -0.0078 0.0266  0.0280  66  LYS A CB  
490  C CG  . LYS A 80  ? 0.3751 0.3921 0.2519 -0.0056 0.0232  0.0283  66  LYS A CG  
491  C CD  . LYS A 80  ? 0.3851 0.4060 0.2565 -0.0018 0.0232  0.0216  66  LYS A CD  
492  C CE  . LYS A 80  ? 0.4407 0.4701 0.3061 -0.0017 0.0291  0.0219  66  LYS A CE  
493  N NZ  . LYS A 80  ? 0.4899 0.5232 0.3490 0.0025  0.0285  0.0150  66  LYS A NZ  
494  N N   . GLY A 81  ? 0.3410 0.3614 0.2537 -0.0160 0.0306  0.0360  67  GLY A N   
495  C CA  . GLY A 81  ? 0.3326 0.3574 0.2570 -0.0177 0.0333  0.0347  67  GLY A CA  
496  C C   . GLY A 81  ? 0.3324 0.3587 0.2632 -0.0148 0.0315  0.0278  67  GLY A C   
497  O O   . GLY A 81  ? 0.3190 0.3491 0.2597 -0.0156 0.0330  0.0261  67  GLY A O   
498  N N   . PHE A 82  ? 0.3175 0.3411 0.2434 -0.0113 0.0282  0.0239  68  PHE A N   
499  C CA  . PHE A 82  ? 0.3141 0.3384 0.2451 -0.0084 0.0263  0.0179  68  PHE A CA  
500  C C   . PHE A 82  ? 0.3028 0.3218 0.2280 -0.0057 0.0219  0.0157  68  PHE A C   
501  O O   . PHE A 82  ? 0.2925 0.3097 0.2089 -0.0054 0.0213  0.0171  68  PHE A O   
502  C CB  . PHE A 82  ? 0.3242 0.3562 0.2563 -0.0068 0.0304  0.0138  68  PHE A CB  
503  C CG  . PHE A 82  ? 0.3017 0.3344 0.2402 -0.0039 0.0286  0.0083  68  PHE A CG  
504  C CD1 . PHE A 82  ? 0.3115 0.3466 0.2601 -0.0044 0.0290  0.0073  68  PHE A CD1 
505  C CD2 . PHE A 82  ? 0.3079 0.3386 0.2427 -0.0005 0.0262  0.0041  68  PHE A CD2 
506  C CE1 . PHE A 82  ? 0.3022 0.3378 0.2561 -0.0014 0.0271  0.0027  68  PHE A CE1 
507  C CE2 . PHE A 82  ? 0.3415 0.3722 0.2822 0.0022  0.0245  -0.0002 68  PHE A CE2 
508  C CZ  . PHE A 82  ? 0.3100 0.3431 0.2598 0.0018  0.0249  -0.0007 68  PHE A CZ  
509  N N   . ALA A 83  ? 0.2607 0.2773 0.1912 -0.0038 0.0189  0.0124  69  ALA A N   
510  C CA  . ALA A 83  ? 0.2765 0.2885 0.2033 -0.0014 0.0151  0.0100  69  ALA A CA  
511  C C   . ALA A 83  ? 0.2719 0.2840 0.2052 0.0009  0.0137  0.0060  69  ALA A C   
512  O O   . ALA A 83  ? 0.2324 0.2471 0.1727 0.0007  0.0148  0.0055  69  ALA A O   
513  C CB  . ALA A 83  ? 0.2379 0.2438 0.1632 -0.0025 0.0113  0.0132  69  ALA A CB  
514  N N   . ALA A 84  ? 0.2682 0.2770 0.1992 0.0031  0.0110  0.0034  70  ALA A N   
515  C CA  . ALA A 84  ? 0.2428 0.2508 0.1790 0.0054  0.0096  0.0002  70  ALA A CA  
516  C C   . ALA A 84  ? 0.2526 0.2550 0.1886 0.0061  0.0057  0.0002  70  ALA A C   
517  O O   . ALA A 84  ? 0.2269 0.2267 0.1577 0.0060  0.0040  0.0002  70  ALA A O   
518  C CB  . ALA A 84  ? 0.2740 0.2851 0.2095 0.0079  0.0111  -0.0043 70  ALA A CB  
519  N N   . LEU A 85  ? 0.2430 0.2439 0.1845 0.0069  0.0044  0.0001  71  LEU A N   
520  C CA  . LEU A 85  ? 0.2469 0.2434 0.1896 0.0074  0.0013  0.0004  71  LEU A CA  
521  C C   . LEU A 85  ? 0.2330 0.2289 0.1797 0.0097  0.0009  -0.0019 71  LEU A C   
522  O O   . LEU A 85  ? 0.2442 0.2428 0.1945 0.0108  0.0023  -0.0026 71  LEU A O   
523  C CB  . LEU A 85  ? 0.2197 0.2154 0.1653 0.0061  0.0002  0.0033  71  LEU A CB  
524  C CG  . LEU A 85  ? 0.2473 0.2402 0.1958 0.0067  -0.0022 0.0038  71  LEU A CG  
525  C CD1 . LEU A 85  ? 0.2071 0.1965 0.1525 0.0061  -0.0044 0.0039  71  LEU A CD1 
526  C CD2 . LEU A 85  ? 0.2304 0.2245 0.1823 0.0061  -0.0028 0.0057  71  LEU A CD2 
527  N N   . LEU A 86  ? 0.2410 0.2332 0.1876 0.0105  -0.0012 -0.0031 72  LEU A N   
528  C CA  . LEU A 86  ? 0.2465 0.2368 0.1975 0.0124  -0.0019 -0.0044 72  LEU A CA  
529  C C   . LEU A 86  ? 0.2521 0.2390 0.2057 0.0118  -0.0039 -0.0022 72  LEU A C   
530  O O   . LEU A 86  ? 0.2423 0.2270 0.1945 0.0107  -0.0055 -0.0021 72  LEU A O   
531  C CB  . LEU A 86  ? 0.2630 0.2520 0.2130 0.0138  -0.0026 -0.0083 72  LEU A CB  
532  C CG  . LEU A 86  ? 0.2728 0.2586 0.2282 0.0157  -0.0039 -0.0096 72  LEU A CG  
533  C CD1 . LEU A 86  ? 0.2673 0.2551 0.2261 0.0174  -0.0025 -0.0093 72  LEU A CD1 
534  C CD2 . LEU A 86  ? 0.2877 0.2716 0.2429 0.0170  -0.0053 -0.0140 72  LEU A CD2 
535  N N   . THR A 87  ? 0.2209 0.2080 0.1784 0.0127  -0.0036 -0.0005 73  THR A N   
536  C CA  . THR A 87  ? 0.2304 0.2153 0.1906 0.0124  -0.0048 0.0018  73  THR A CA  
537  C C   . THR A 87  ? 0.2459 0.2288 0.2099 0.0142  -0.0048 0.0023  73  THR A C   
538  O O   . THR A 87  ? 0.2294 0.2130 0.1942 0.0160  -0.0042 0.0006  73  THR A O   
539  C CB  . THR A 87  ? 0.2138 0.2011 0.1742 0.0117  -0.0046 0.0044  73  THR A CB  
540  O OG1 . THR A 87  ? 0.2136 0.2039 0.1753 0.0133  -0.0035 0.0047  73  THR A OG1 
541  C CG2 . THR A 87  ? 0.2145 0.2030 0.1718 0.0099  -0.0049 0.0043  73  THR A CG2 
542  N N   . THR A 88  ? 0.2476 0.2283 0.2144 0.0138  -0.0055 0.0046  74  THR A N   
543  C CA  . THR A 88  ? 0.2482 0.2269 0.2186 0.0154  -0.0054 0.0064  74  THR A CA  
544  C C   . THR A 88  ? 0.2630 0.2447 0.2331 0.0165  -0.0044 0.0096  74  THR A C   
545  O O   . THR A 88  ? 0.2378 0.2225 0.2063 0.0156  -0.0042 0.0105  74  THR A O   
546  C CB  . THR A 88  ? 0.2904 0.2648 0.2647 0.0143  -0.0063 0.0073  74  THR A CB  
547  O OG1 . THR A 88  ? 0.2574 0.2289 0.2354 0.0159  -0.0063 0.0090  74  THR A OG1 
548  C CG2 . THR A 88  ? 0.2705 0.2461 0.2456 0.0126  -0.0061 0.0103  74  THR A CG2 
549  N N   . PHE A 89  ? 0.2722 0.2531 0.2440 0.0187  -0.0042 0.0110  75  PHE A N   
550  C CA  . PHE A 89  ? 0.2452 0.2292 0.2162 0.0206  -0.0037 0.0137  75  PHE A CA  
551  C C   . PHE A 89  ? 0.2501 0.2357 0.2208 0.0194  -0.0032 0.0168  75  PHE A C   
552  O O   . PHE A 89  ? 0.2317 0.2145 0.2045 0.0179  -0.0031 0.0187  75  PHE A O   
553  C CB  . PHE A 89  ? 0.2576 0.2390 0.2307 0.0231  -0.0040 0.0155  75  PHE A CB  
554  C CG  . PHE A 89  ? 0.2840 0.2686 0.2555 0.0258  -0.0038 0.0182  75  PHE A CG  
555  C CD1 . PHE A 89  ? 0.2624 0.2506 0.2331 0.0281  -0.0042 0.0159  75  PHE A CD1 
556  C CD2 . PHE A 89  ? 0.2503 0.2348 0.2215 0.0261  -0.0032 0.0229  75  PHE A CD2 
557  C CE1 . PHE A 89  ? 0.2734 0.2648 0.2427 0.0310  -0.0046 0.0179  75  PHE A CE1 
558  C CE2 . PHE A 89  ? 0.2606 0.2485 0.2294 0.0290  -0.0032 0.0252  75  PHE A CE2 
559  C CZ  . PHE A 89  ? 0.2566 0.2478 0.2244 0.0316  -0.0042 0.0225  75  PHE A CZ  
560  N N   . GLY A 90  ? 0.2101 0.2004 0.1787 0.0201  -0.0030 0.0168  76  GLY A N   
561  C CA  . GLY A 90  ? 0.2477 0.2409 0.2158 0.0199  -0.0026 0.0192  76  GLY A CA  
562  C C   . GLY A 90  ? 0.2225 0.2158 0.1912 0.0172  -0.0029 0.0183  76  GLY A C   
563  O O   . GLY A 90  ? 0.2210 0.2172 0.1885 0.0167  -0.0035 0.0165  76  GLY A O   
564  N N   . VAL A 91  ? 0.2185 0.2083 0.1895 0.0154  -0.0027 0.0193  77  VAL A N   
565  C CA  . VAL A 91  ? 0.2302 0.2204 0.2024 0.0131  -0.0033 0.0184  77  VAL A CA  
566  C C   . VAL A 91  ? 0.2218 0.2109 0.1921 0.0119  -0.0047 0.0150  77  VAL A C   
567  O O   . VAL A 91  ? 0.2267 0.2174 0.1965 0.0108  -0.0056 0.0139  77  VAL A O   
568  C CB  . VAL A 91  ? 0.2274 0.2143 0.2036 0.0114  -0.0029 0.0201  77  VAL A CB  
569  C CG1 . VAL A 91  ? 0.2373 0.2257 0.2151 0.0123  -0.0010 0.0245  77  VAL A CG1 
570  C CG2 . VAL A 91  ? 0.2449 0.2265 0.2228 0.0109  -0.0038 0.0184  77  VAL A CG2 
571  N N   . GLY A 92  ? 0.2336 0.2203 0.2030 0.0122  -0.0049 0.0132  78  GLY A N   
572  C CA  . GLY A 92  ? 0.2198 0.2060 0.1867 0.0111  -0.0058 0.0104  78  GLY A CA  
573  C C   . GLY A 92  ? 0.2223 0.2120 0.1870 0.0116  -0.0055 0.0098  78  GLY A C   
574  O O   . GLY A 92  ? 0.2107 0.2012 0.1742 0.0104  -0.0063 0.0093  78  GLY A O   
575  N N   . GLU A 93  ? 0.2147 0.2064 0.1796 0.0135  -0.0046 0.0099  79  GLU A N   
576  C CA  . GLU A 93  ? 0.2137 0.2088 0.1779 0.0139  -0.0045 0.0089  79  GLU A CA  
577  C C   . GLU A 93  ? 0.2147 0.2126 0.1795 0.0137  -0.0053 0.0095  79  GLU A C   
578  O O   . GLU A 93  ? 0.2193 0.2185 0.1841 0.0127  -0.0058 0.0086  79  GLU A O   
579  C CB  . GLU A 93  ? 0.2168 0.2138 0.1819 0.0163  -0.0037 0.0085  79  GLU A CB  
580  C CG  . GLU A 93  ? 0.2253 0.2235 0.1913 0.0186  -0.0038 0.0107  79  GLU A CG  
581  C CD  . GLU A 93  ? 0.2207 0.2202 0.1874 0.0213  -0.0036 0.0102  79  GLU A CD  
582  O OE1 . GLU A 93  ? 0.2195 0.2221 0.1869 0.0219  -0.0037 0.0080  79  GLU A OE1 
583  O OE2 . GLU A 93  ? 0.2204 0.2173 0.1875 0.0228  -0.0035 0.0119  79  GLU A OE2 
584  N N   . LEU A 94  ? 0.2000 0.1989 0.1658 0.0147  -0.0053 0.0112  80  LEU A N   
585  C CA  . LEU A 94  ? 0.2030 0.2053 0.1695 0.0150  -0.0062 0.0111  80  LEU A CA  
586  C C   . LEU A 94  ? 0.2114 0.2121 0.1783 0.0128  -0.0074 0.0106  80  LEU A C   
587  O O   . LEU A 94  ? 0.1974 0.2002 0.1652 0.0127  -0.0087 0.0095  80  LEU A O   
588  C CB  . LEU A 94  ? 0.2270 0.2318 0.1938 0.0169  -0.0055 0.0131  80  LEU A CB  
589  C CG  . LEU A 94  ? 0.2525 0.2599 0.2186 0.0199  -0.0050 0.0135  80  LEU A CG  
590  C CD1 . LEU A 94  ? 0.2322 0.2432 0.1975 0.0221  -0.0044 0.0157  80  LEU A CD1 
591  C CD2 . LEU A 94  ? 0.2456 0.2557 0.2123 0.0207  -0.0061 0.0108  80  LEU A CD2 
592  N N   . SER A 95  ? 0.2025 0.1995 0.1690 0.0112  -0.0075 0.0109  81  SER A N   
593  C CA  . SER A 95  ? 0.2047 0.2001 0.1712 0.0094  -0.0091 0.0102  81  SER A CA  
594  C C   . SER A 95  ? 0.2116 0.2060 0.1761 0.0084  -0.0099 0.0092  81  SER A C   
595  O O   . SER A 95  ? 0.1946 0.1885 0.1592 0.0074  -0.0117 0.0089  81  SER A O   
596  C CB  . SER A 95  ? 0.2254 0.2173 0.1922 0.0082  -0.0094 0.0102  81  SER A CB  
597  O OG  . SER A 95  ? 0.2241 0.2169 0.1939 0.0085  -0.0086 0.0116  81  SER A OG  
598  N N   . ALA A 96  ? 0.2099 0.2043 0.1730 0.0086  -0.0087 0.0089  82  ALA A N   
599  C CA  . ALA A 96  ? 0.2161 0.2100 0.1774 0.0073  -0.0087 0.0085  82  ALA A CA  
600  C C   . ALA A 96  ? 0.2047 0.2016 0.1684 0.0077  -0.0087 0.0082  82  ALA A C   
601  O O   . ALA A 96  ? 0.1932 0.1900 0.1564 0.0063  -0.0084 0.0083  82  ALA A O   
602  C CB  . ALA A 96  ? 0.2219 0.2148 0.1808 0.0073  -0.0070 0.0079  82  ALA A CB  
603  N N   . MET A 97  ? 0.2070 0.2069 0.1733 0.0094  -0.0091 0.0077  83  MET A N   
604  C CA  . MET A 97  ? 0.2162 0.2194 0.1854 0.0102  -0.0093 0.0066  83  MET A CA  
605  C C   . MET A 97  ? 0.2020 0.2046 0.1732 0.0085  -0.0110 0.0064  83  MET A C   
606  O O   . MET A 97  ? 0.2001 0.2038 0.1736 0.0077  -0.0107 0.0059  83  MET A O   
607  C CB  . MET A 97  ? 0.2237 0.2307 0.1946 0.0129  -0.0098 0.0059  83  MET A CB  
608  C CG  . MET A 97  ? 0.2670 0.2778 0.2415 0.0140  -0.0109 0.0039  83  MET A CG  
609  S SD  . MET A 97  ? 0.5481 0.5637 0.5226 0.0180  -0.0107 0.0032  83  MET A SD  
610  C CE  . MET A 97  ? 0.2934 0.3075 0.2661 0.0184  -0.0085 0.0042  83  MET A CE  
611  N N   . ASN A 98  ? 0.1957 0.1964 0.1667 0.0079  -0.0128 0.0068  84  ASN A N   
612  C CA  . ASN A 98  ? 0.2017 0.2009 0.1749 0.0065  -0.0149 0.0068  84  ASN A CA  
613  C C   . ASN A 98  ? 0.1980 0.1939 0.1687 0.0039  -0.0141 0.0088  84  ASN A C   
614  O O   . ASN A 98  ? 0.2103 0.2054 0.1836 0.0025  -0.0149 0.0094  84  ASN A O   
615  C CB  . ASN A 98  ? 0.1846 0.1824 0.1581 0.0067  -0.0172 0.0067  84  ASN A CB  
616  C CG  . ASN A 98  ? 0.2002 0.1962 0.1768 0.0057  -0.0201 0.0064  84  ASN A CG  
617  O OD1 . ASN A 98  ? 0.2148 0.2126 0.1958 0.0060  -0.0210 0.0052  84  ASN A OD1 
618  N ND2 . ASN A 98  ? 0.2051 0.1974 0.1800 0.0047  -0.0219 0.0076  84  ASN A ND2 
619  N N   . GLY A 99  ? 0.1937 0.1877 0.1596 0.0034  -0.0125 0.0098  85  GLY A N   
620  C CA  . GLY A 99  ? 0.2099 0.2020 0.1725 0.0014  -0.0112 0.0115  85  GLY A CA  
621  C C   . GLY A 99  ? 0.2006 0.1958 0.1656 0.0010  -0.0088 0.0112  85  GLY A C   
622  O O   . GLY A 99  ? 0.2188 0.2137 0.1851 -0.0010 -0.0083 0.0127  85  GLY A O   
623  N N   . ILE A 100 ? 0.2091 0.2073 0.1753 0.0028  -0.0073 0.0095  86  ILE A N   
624  C CA  . ILE A 100 ? 0.2211 0.2228 0.1902 0.0027  -0.0052 0.0086  86  ILE A CA  
625  C C   . ILE A 100 ? 0.2093 0.2129 0.1847 0.0021  -0.0066 0.0081  86  ILE A C   
626  O O   . ILE A 100 ? 0.2070 0.2120 0.1854 0.0004  -0.0052 0.0086  86  ILE A O   
627  C CB  . ILE A 100 ? 0.2191 0.2234 0.1885 0.0053  -0.0042 0.0067  86  ILE A CB  
628  C CG1 . ILE A 100 ? 0.2154 0.2175 0.1798 0.0056  -0.0030 0.0069  86  ILE A CG1 
629  C CG2 . ILE A 100 ? 0.2229 0.2315 0.1965 0.0056  -0.0025 0.0052  86  ILE A CG2 
630  C CD1 . ILE A 100 ? 0.2526 0.2546 0.2138 0.0037  -0.0008 0.0076  86  ILE A CD1 
631  N N   . ALA A 101 ? 0.1982 0.2018 0.1761 0.0035  -0.0093 0.0070  87  ALA A N   
632  C CA  . ALA A 101 ? 0.2170 0.2222 0.2014 0.0033  -0.0114 0.0057  87  ALA A CA  
633  C C   . ALA A 101 ? 0.2136 0.2154 0.1996 0.0002  -0.0119 0.0081  87  ALA A C   
634  O O   . ALA A 101 ? 0.2084 0.2114 0.2005 -0.0012 -0.0121 0.0078  87  ALA A O   
635  C CB  . ALA A 101 ? 0.1858 0.1917 0.1715 0.0057  -0.0142 0.0039  87  ALA A CB  
636  N N   . GLY A 102 ? 0.1915 0.1889 0.1725 -0.0010 -0.0125 0.0105  88  GLY A N   
637  C CA  . GLY A 102 ? 0.1974 0.1910 0.1786 -0.0038 -0.0131 0.0136  88  GLY A CA  
638  C C   . GLY A 102 ? 0.2128 0.2071 0.1923 -0.0062 -0.0094 0.0161  88  GLY A C   
639  O O   . GLY A 102 ? 0.2126 0.2058 0.1957 -0.0088 -0.0091 0.0184  88  GLY A O   
640  N N   . SER A 103 ? 0.2124 0.2088 0.1871 -0.0054 -0.0066 0.0155  89  SER A N   
641  C CA  . SER A 103 ? 0.2204 0.2189 0.1940 -0.0073 -0.0028 0.0171  89  SER A CA  
642  C C   . SER A 103 ? 0.2046 0.2075 0.1869 -0.0079 -0.0017 0.0155  89  SER A C   
643  O O   . SER A 103 ? 0.2258 0.2298 0.2108 -0.0106 0.0006  0.0177  89  SER A O   
644  C CB  . SER A 103 ? 0.2060 0.2063 0.1735 -0.0057 -0.0004 0.0158  89  SER A CB  
645  O OG  . SER A 103 ? 0.2389 0.2353 0.1992 -0.0053 -0.0017 0.0169  89  SER A OG  
646  N N   . TYR A 104 ? 0.2270 0.2327 0.2139 -0.0053 -0.0033 0.0118  90  TYR A N   
647  C CA  . TYR A 104 ? 0.2057 0.2157 0.2014 -0.0055 -0.0031 0.0096  90  TYR A CA  
648  C C   . TYR A 104 ? 0.2064 0.2144 0.2091 -0.0079 -0.0052 0.0108  90  TYR A C   
649  O O   . TYR A 104 ? 0.2119 0.2216 0.2209 -0.0105 -0.0036 0.0117  90  TYR A O   
650  C CB  . TYR A 104 ? 0.2133 0.2268 0.2114 -0.0017 -0.0049 0.0053  90  TYR A CB  
651  C CG  . TYR A 104 ? 0.2332 0.2518 0.2403 -0.0012 -0.0052 0.0022  90  TYR A CG  
652  C CD1 . TYR A 104 ? 0.2475 0.2666 0.2623 -0.0013 -0.0083 0.0004  90  TYR A CD1 
653  C CD2 . TYR A 104 ? 0.2276 0.2507 0.2360 -0.0005 -0.0026 0.0007  90  TYR A CD2 
654  C CE1 . TYR A 104 ? 0.2214 0.2455 0.2452 -0.0007 -0.0090 -0.0031 90  TYR A CE1 
655  C CE2 . TYR A 104 ? 0.2357 0.2639 0.2529 0.0002  -0.0031 -0.0026 90  TYR A CE2 
656  C CZ  . TYR A 104 ? 0.2482 0.2769 0.2732 0.0000  -0.0064 -0.0045 90  TYR A CZ  
657  O OH  . TYR A 104 ? 0.2759 0.3098 0.3104 0.0008  -0.0074 -0.0083 90  TYR A OH  
658  N N   . ALA A 105 ? 0.2129 0.2170 0.2152 -0.0072 -0.0089 0.0109  91  ALA A N   
659  C CA  . ALA A 105 ? 0.2153 0.2169 0.2249 -0.0090 -0.0117 0.0115  91  ALA A CA  
660  C C   . ALA A 105 ? 0.2307 0.2290 0.2402 -0.0132 -0.0095 0.0167  91  ALA A C   
661  O O   . ALA A 105 ? 0.2017 0.1997 0.2199 -0.0156 -0.0100 0.0176  91  ALA A O   
662  C CB  . ALA A 105 ? 0.1878 0.1858 0.1961 -0.0072 -0.0159 0.0106  91  ALA A CB  
663  N N   . GLU A 106 ? 0.2239 0.2198 0.2239 -0.0141 -0.0073 0.0204  92  GLU A N   
664  C CA  . GLU A 106 ? 0.2252 0.2178 0.2232 -0.0177 -0.0054 0.0261  92  GLU A CA  
665  C C   . GLU A 106 ? 0.2367 0.2335 0.2320 -0.0195 0.0002  0.0278  92  GLU A C   
666  O O   . GLU A 106 ? 0.2240 0.2190 0.2148 -0.0221 0.0027  0.0329  92  GLU A O   
667  C CB  . GLU A 106 ? 0.2217 0.2086 0.2107 -0.0173 -0.0073 0.0290  92  GLU A CB  
668  C CG  . GLU A 106 ? 0.2184 0.2019 0.2098 -0.0151 -0.0126 0.0267  92  GLU A CG  
669  C CD  . GLU A 106 ? 0.2343 0.2109 0.2241 -0.0165 -0.0157 0.0309  92  GLU A CD  
670  O OE1 . GLU A 106 ? 0.2231 0.1972 0.2063 -0.0185 -0.0137 0.0359  92  GLU A OE1 
671  O OE2 . GLU A 106 ? 0.2431 0.2172 0.2382 -0.0153 -0.0202 0.0289  92  GLU A OE2 
672  N N   . HIS A 107 ? 0.2299 0.2327 0.2279 -0.0178 0.0021  0.0237  93  HIS A N   
673  C CA  . HIS A 107 ? 0.2490 0.2571 0.2467 -0.0192 0.0072  0.0242  93  HIS A CA  
674  C C   . HIS A 107 ? 0.2468 0.2542 0.2327 -0.0191 0.0101  0.0268  93  HIS A C   
675  O O   . HIS A 107 ? 0.2622 0.2705 0.2453 -0.0218 0.0137  0.0309  93  HIS A O   
676  C CB  . HIS A 107 ? 0.2278 0.2373 0.2342 -0.0233 0.0094  0.0272  93  HIS A CB  
677  C CG  . HIS A 107 ? 0.2562 0.2685 0.2756 -0.0231 0.0073  0.0232  93  HIS A CG  
678  N ND1 . HIS A 107 ? 0.2643 0.2731 0.2891 -0.0221 0.0021  0.0213  93  HIS A ND1 
679  C CD2 . HIS A 107 ? 0.2419 0.2607 0.2701 -0.0236 0.0094  0.0202  93  HIS A CD2 
680  C CE1 . HIS A 107 ? 0.2619 0.2749 0.2981 -0.0218 0.0009  0.0172  93  HIS A CE1 
681  N NE2 . HIS A 107 ? 0.2765 0.2954 0.3151 -0.0228 0.0052  0.0166  93  HIS A NE2 
682  N N   . VAL A 108 ? 0.2529 0.2590 0.2320 -0.0159 0.0083  0.0243  94  VAL A N   
683  C CA  . VAL A 108 ? 0.2171 0.2227 0.1855 -0.0150 0.0101  0.0254  94  VAL A CA  
684  C C   . VAL A 108 ? 0.2389 0.2492 0.2066 -0.0123 0.0118  0.0208  94  VAL A C   
685  O O   . VAL A 108 ? 0.2283 0.2384 0.1985 -0.0096 0.0093  0.0173  94  VAL A O   
686  C CB  . VAL A 108 ? 0.2581 0.2577 0.2200 -0.0137 0.0062  0.0262  94  VAL A CB  
687  C CG1 . VAL A 108 ? 0.2475 0.2468 0.1987 -0.0129 0.0078  0.0270  94  VAL A CG1 
688  C CG2 . VAL A 108 ? 0.2186 0.2131 0.1826 -0.0159 0.0036  0.0302  94  VAL A CG2 
689  N N   . PRO A 109 ? 0.2719 0.2866 0.2367 -0.0126 0.0161  0.0207  95  PRO A N   
690  C CA  . PRO A 109 ? 0.2643 0.2834 0.2296 -0.0098 0.0174  0.0160  95  PRO A CA  
691  C C   . PRO A 109 ? 0.2518 0.2682 0.2091 -0.0070 0.0159  0.0142  95  PRO A C   
692  O O   . PRO A 109 ? 0.2572 0.2749 0.2077 -0.0068 0.0181  0.0142  95  PRO A O   
693  C CB  . PRO A 109 ? 0.2535 0.2790 0.2199 -0.0115 0.0226  0.0165  95  PRO A CB  
694  C CG  . PRO A 109 ? 0.2621 0.2854 0.2226 -0.0144 0.0242  0.0218  95  PRO A CG  
695  C CD  . PRO A 109 ? 0.2522 0.2689 0.2145 -0.0157 0.0201  0.0248  95  PRO A CD  
696  N N   . VAL A 110 ? 0.2761 0.2891 0.2344 -0.0049 0.0121  0.0124  96  VAL A N   
697  C CA  . VAL A 110 ? 0.2163 0.2267 0.1695 -0.0023 0.0104  0.0104  96  VAL A CA  
698  C C   . VAL A 110 ? 0.2423 0.2554 0.1997 0.0004  0.0105  0.0066  96  VAL A C   
699  O O   . VAL A 110 ? 0.2442 0.2583 0.2077 0.0011  0.0092  0.0058  96  VAL A O   
700  C CB  . VAL A 110 ? 0.2428 0.2477 0.1946 -0.0022 0.0065  0.0116  96  VAL A CB  
701  C CG1 . VAL A 110 ? 0.2187 0.2215 0.1679 0.0004  0.0047  0.0091  96  VAL A CG1 
702  C CG2 . VAL A 110 ? 0.2299 0.2315 0.1763 -0.0043 0.0058  0.0152  96  VAL A CG2 
703  N N   . LEU A 111 ? 0.2239 0.2379 0.1781 0.0023  0.0115  0.0040  97  LEU A N   
704  C CA  . LEU A 111 ? 0.2454 0.2610 0.2032 0.0053  0.0111  0.0007  97  LEU A CA  
705  C C   . LEU A 111 ? 0.2396 0.2502 0.1958 0.0071  0.0080  0.0003  97  LEU A C   
706  O O   . LEU A 111 ? 0.2253 0.2330 0.1767 0.0073  0.0072  0.0000  97  LEU A O   
707  C CB  . LEU A 111 ? 0.2333 0.2528 0.1898 0.0066  0.0138  -0.0023 97  LEU A CB  
708  C CG  . LEU A 111 ? 0.2557 0.2755 0.2156 0.0101  0.0128  -0.0058 97  LEU A CG  
709  C CD1 . LEU A 111 ? 0.2529 0.2764 0.2201 0.0110  0.0129  -0.0067 97  LEU A CD1 
710  C CD2 . LEU A 111 ? 0.2679 0.2904 0.2256 0.0117  0.0147  -0.0093 97  LEU A CD2 
711  N N   . HIS A 112 ? 0.2279 0.2380 0.1884 0.0085  0.0063  0.0001  98  HIS A N   
712  C CA  . HIS A 112 ? 0.2381 0.2442 0.1981 0.0101  0.0038  0.0003  98  HIS A CA  
713  C C   . HIS A 112 ? 0.2462 0.2527 0.2079 0.0130  0.0039  -0.0021 98  HIS A C   
714  O O   . HIS A 112 ? 0.2430 0.2521 0.2087 0.0148  0.0040  -0.0030 98  HIS A O   
715  C CB  . HIS A 112 ? 0.2172 0.2229 0.1800 0.0103  0.0019  0.0019  98  HIS A CB  
716  C CG  . HIS A 112 ? 0.2373 0.2393 0.1991 0.0111  0.0000  0.0029  98  HIS A CG  
717  N ND1 . HIS A 112 ? 0.2187 0.2208 0.1823 0.0116  -0.0016 0.0042  98  HIS A ND1 
718  C CD2 . HIS A 112 ? 0.2109 0.2093 0.1704 0.0115  -0.0007 0.0027  98  HIS A CD2 
719  C CE1 . HIS A 112 ? 0.2191 0.2182 0.1816 0.0121  -0.0026 0.0051  98  HIS A CE1 
720  N NE2 . HIS A 112 ? 0.2515 0.2480 0.2120 0.0119  -0.0022 0.0043  98  HIS A NE2 
721  N N   . ILE A 113 ? 0.2322 0.2358 0.1913 0.0137  0.0036  -0.0033 99  ILE A N   
722  C CA  . ILE A 113 ? 0.2424 0.2448 0.2035 0.0164  0.0030  -0.0055 99  ILE A CA  
723  C C   . ILE A 113 ? 0.2518 0.2495 0.2138 0.0170  0.0008  -0.0035 99  ILE A C   
724  O O   . ILE A 113 ? 0.2251 0.2196 0.1850 0.0155  -0.0003 -0.0026 99  ILE A O   
725  C CB  . ILE A 113 ? 0.2397 0.2420 0.1984 0.0170  0.0037  -0.0087 99  ILE A CB  
726  C CG1 . ILE A 113 ? 0.2529 0.2610 0.2103 0.0161  0.0067  -0.0101 99  ILE A CG1 
727  C CG2 . ILE A 113 ? 0.2304 0.2310 0.1926 0.0200  0.0027  -0.0112 99  ILE A CG2 
728  C CD1 . ILE A 113 ? 0.2598 0.2687 0.2126 0.0162  0.0077  -0.0128 99  ILE A CD1 
729  N N   . VAL A 114 ? 0.2511 0.2486 0.2164 0.0192  0.0001  -0.0029 100 VAL A N   
730  C CA  . VAL A 114 ? 0.2252 0.2187 0.1914 0.0197  -0.0015 -0.0003 100 VAL A CA  
731  C C   . VAL A 114 ? 0.2522 0.2427 0.2210 0.0220  -0.0022 -0.0013 100 VAL A C   
732  O O   . VAL A 114 ? 0.2334 0.2255 0.2044 0.0245  -0.0023 -0.0021 100 VAL A O   
733  C CB  . VAL A 114 ? 0.2383 0.2341 0.2056 0.0204  -0.0018 0.0023  100 VAL A CB  
734  C CG1 . VAL A 114 ? 0.2323 0.2248 0.2001 0.0208  -0.0028 0.0054  100 VAL A CG1 
735  C CG2 . VAL A 114 ? 0.2149 0.2136 0.1809 0.0183  -0.0015 0.0026  100 VAL A CG2 
736  N N   . GLY A 115 ? 0.2476 0.2336 0.2167 0.0213  -0.0032 -0.0016 101 GLY A N   
737  C CA  . GLY A 115 ? 0.2552 0.2371 0.2278 0.0233  -0.0044 -0.0021 101 GLY A CA  
738  C C   . GLY A 115 ? 0.2841 0.2640 0.2587 0.0243  -0.0049 0.0024  101 GLY A C   
739  O O   . GLY A 115 ? 0.2900 0.2697 0.2637 0.0226  -0.0047 0.0056  101 GLY A O   
740  N N   . ALA A 116 ? 0.2847 0.2635 0.2620 0.0271  -0.0056 0.0027  102 ALA A N   
741  C CA  . ALA A 116 ? 0.2905 0.2684 0.2685 0.0287  -0.0059 0.0072  102 ALA A CA  
742  C C   . ALA A 116 ? 0.3140 0.2861 0.2960 0.0306  -0.0073 0.0086  102 ALA A C   
743  O O   . ALA A 116 ? 0.3028 0.2724 0.2877 0.0314  -0.0083 0.0049  102 ALA A O   
744  C CB  . ALA A 116 ? 0.2803 0.2636 0.2570 0.0311  -0.0057 0.0068  102 ALA A CB  
745  N N   . PRO A 117 ? 0.3216 0.2914 0.3041 0.0314  -0.0075 0.0140  103 PRO A N   
746  C CA  . PRO A 117 ? 0.3374 0.3013 0.3241 0.0333  -0.0089 0.0163  103 PRO A CA  
747  C C   . PRO A 117 ? 0.3278 0.2922 0.3159 0.0372  -0.0104 0.0131  103 PRO A C   
748  O O   . PRO A 117 ? 0.3168 0.2869 0.3024 0.0388  -0.0101 0.0111  103 PRO A O   
749  C CB  . PRO A 117 ? 0.3554 0.3189 0.3403 0.0338  -0.0082 0.0232  103 PRO A CB  
750  C CG  . PRO A 117 ? 0.3388 0.3070 0.3201 0.0311  -0.0065 0.0240  103 PRO A CG  
751  C CD  . PRO A 117 ? 0.3134 0.2862 0.2927 0.0305  -0.0063 0.0184  103 PRO A CD  
752  N N   . GLY A 118 ? 0.3419 0.3002 0.3350 0.0387  -0.0122 0.0127  104 GLY A N   
753  C CA  . GLY A 118 ? 0.3715 0.3301 0.3670 0.0426  -0.0140 0.0092  104 GLY A CA  
754  C C   . GLY A 118 ? 0.3665 0.3275 0.3597 0.0459  -0.0146 0.0127  104 GLY A C   
755  O O   . GLY A 118 ? 0.3575 0.3181 0.3478 0.0456  -0.0140 0.0188  104 GLY A O   
756  N N   . THR A 119 ? 0.3477 0.3120 0.3421 0.0493  -0.0157 0.0085  105 THR A N   
757  C CA  . THR A 119 ? 0.3689 0.3374 0.3610 0.0526  -0.0165 0.0103  105 THR A CA  
758  C C   . THR A 119 ? 0.3997 0.3625 0.3918 0.0552  -0.0183 0.0171  105 THR A C   
759  O O   . THR A 119 ? 0.4127 0.3781 0.4002 0.0564  -0.0182 0.0216  105 THR A O   
760  C CB  . THR A 119 ? 0.3662 0.3392 0.3612 0.0558  -0.0177 0.0040  105 THR A CB  
761  O OG1 . THR A 119 ? 0.3579 0.3254 0.3585 0.0582  -0.0199 0.0018  105 THR A OG1 
762  C CG2 . THR A 119 ? 0.3301 0.3096 0.3245 0.0531  -0.0153 -0.0017 105 THR A CG2 
763  N N   . ALA A 120 ? 0.3995 0.3544 0.3965 0.0562  -0.0202 0.0182  106 ALA A N   
764  C CA  . ALA A 120 ? 0.3852 0.3339 0.3823 0.0585  -0.0218 0.0255  106 ALA A CA  
765  C C   . ALA A 120 ? 0.4125 0.3606 0.4053 0.0554  -0.0195 0.0329  106 ALA A C   
766  O O   . ALA A 120 ? 0.4179 0.3666 0.4064 0.0576  -0.0196 0.0389  106 ALA A O   
767  C CB  . ALA A 120 ? 0.3745 0.3141 0.3790 0.0593  -0.0242 0.0252  106 ALA A CB  
768  N N   . SER A 121 ? 0.4014 0.3489 0.3951 0.0507  -0.0173 0.0322  107 SER A N   
769  C CA  . SER A 121 ? 0.3964 0.3445 0.3867 0.0475  -0.0147 0.0382  107 SER A CA  
770  C C   . SER A 121 ? 0.3980 0.3545 0.3810 0.0486  -0.0134 0.0392  107 SER A C   
771  O O   . SER A 121 ? 0.3927 0.3501 0.3716 0.0490  -0.0123 0.0456  107 SER A O   
772  C CB  . SER A 121 ? 0.4159 0.3635 0.4085 0.0426  -0.0129 0.0355  107 SER A CB  
773  O OG  . SER A 121 ? 0.5246 0.4643 0.5233 0.0407  -0.0134 0.0383  107 SER A OG  
774  N N   . GLN A 122 ? 0.3997 0.3625 0.3813 0.0491  -0.0135 0.0327  108 GLN A N   
775  C CA  . GLN A 122 ? 0.3628 0.3335 0.3388 0.0502  -0.0128 0.0325  108 GLN A CA  
776  C C   . GLN A 122 ? 0.3822 0.3541 0.3555 0.0553  -0.0148 0.0357  108 GLN A C   
777  O O   . GLN A 122 ? 0.3707 0.3463 0.3387 0.0564  -0.0142 0.0397  108 GLN A O   
778  C CB  . GLN A 122 ? 0.3660 0.3425 0.3427 0.0494  -0.0126 0.0251  108 GLN A CB  
779  C CG  . GLN A 122 ? 0.3301 0.3068 0.3077 0.0446  -0.0106 0.0225  108 GLN A CG  
780  C CD  . GLN A 122 ? 0.3521 0.3347 0.3296 0.0439  -0.0101 0.0163  108 GLN A CD  
781  O OE1 . GLN A 122 ? 0.3468 0.3351 0.3228 0.0458  -0.0106 0.0149  108 GLN A OE1 
782  N NE2 . GLN A 122 ? 0.3116 0.2933 0.2907 0.0408  -0.0091 0.0128  108 GLN A NE2 
783  N N   . GLN A 123 ? 0.3991 0.3679 0.3759 0.0587  -0.0175 0.0338  109 GLN A N   
784  C CA  . GLN A 123 ? 0.4143 0.3840 0.3886 0.0641  -0.0201 0.0364  109 GLN A CA  
785  C C   . GLN A 123 ? 0.3840 0.3491 0.3547 0.0650  -0.0198 0.0457  109 GLN A C   
786  O O   . GLN A 123 ? 0.3874 0.3559 0.3526 0.0687  -0.0208 0.0492  109 GLN A O   
787  C CB  . GLN A 123 ? 0.4385 0.4053 0.4184 0.0675  -0.0232 0.0323  109 GLN A CB  
788  C CG  . GLN A 123 ? 0.5239 0.4984 0.5053 0.0695  -0.0242 0.0245  109 GLN A CG  
789  C CD  . GLN A 123 ? 0.6173 0.5901 0.6057 0.0704  -0.0255 0.0181  109 GLN A CD  
790  O OE1 . GLN A 123 ? 0.5742 0.5407 0.5664 0.0730  -0.0279 0.0192  109 GLN A OE1 
791  N NE2 . GLN A 123 ? 0.5405 0.5195 0.5310 0.0683  -0.0239 0.0112  109 GLN A NE2 
792  N N   . ARG A 124 ? 0.3883 0.3461 0.3623 0.0618  -0.0185 0.0498  110 ARG A N   
793  C CA  . ARG A 124 ? 0.3906 0.3440 0.3620 0.0618  -0.0175 0.0593  110 ARG A CA  
794  C C   . ARG A 124 ? 0.4009 0.3602 0.3662 0.0595  -0.0141 0.0630  110 ARG A C   
795  O O   . ARG A 124 ? 0.3899 0.3474 0.3519 0.0598  -0.0127 0.0712  110 ARG A O   
796  C CB  . ARG A 124 ? 0.4269 0.3706 0.4054 0.0587  -0.0172 0.0620  110 ARG A CB  
797  C CG  . ARG A 124 ? 0.4333 0.3702 0.4186 0.0614  -0.0208 0.0592  110 ARG A CG  
798  C CD  . ARG A 124 ? 0.4990 0.4258 0.4915 0.0585  -0.0207 0.0631  110 ARG A CD  
799  N NE  . ARG A 124 ? 0.5600 0.4830 0.5607 0.0577  -0.0227 0.0554  110 ARG A NE  
800  C CZ  . ARG A 124 ? 0.5212 0.4437 0.5259 0.0533  -0.0212 0.0511  110 ARG A CZ  
801  N NH1 . ARG A 124 ? 0.5145 0.4401 0.5166 0.0490  -0.0178 0.0534  110 ARG A NH1 
802  N NH2 . ARG A 124 ? 0.5319 0.4513 0.5433 0.0535  -0.0233 0.0439  110 ARG A NH2 
803  N N   . GLY A 125 ? 0.3755 0.3416 0.3395 0.0572  -0.0126 0.0573  111 GLY A N   
804  C CA  . GLY A 125 ? 0.3591 0.3310 0.3181 0.0552  -0.0097 0.0599  111 GLY A CA  
805  C C   . GLY A 125 ? 0.3538 0.3215 0.3152 0.0508  -0.0067 0.0655  111 GLY A C   
806  O O   . GLY A 125 ? 0.3221 0.2929 0.2790 0.0506  -0.0043 0.0713  111 GLY A O   
807  N N   . GLU A 126 ? 0.3734 0.3346 0.3419 0.0474  -0.0067 0.0635  112 GLU A N   
808  C CA  . GLU A 126 ? 0.3713 0.3280 0.3438 0.0432  -0.0042 0.0686  112 GLU A CA  
809  C C   . GLU A 126 ? 0.3530 0.3161 0.3235 0.0397  -0.0012 0.0677  112 GLU A C   
810  O O   . GLU A 126 ? 0.3054 0.2743 0.2737 0.0395  -0.0015 0.0615  112 GLU A O   
811  C CB  . GLU A 126 ? 0.4083 0.3572 0.3896 0.0407  -0.0056 0.0653  112 GLU A CB  
812  C CG  . GLU A 126 ? 0.4220 0.3649 0.4064 0.0443  -0.0091 0.0642  112 GLU A CG  
813  C CD  . GLU A 126 ? 0.4665 0.4014 0.4601 0.0419  -0.0104 0.0614  112 GLU A CD  
814  O OE1 . GLU A 126 ? 0.4678 0.4043 0.4640 0.0389  -0.0100 0.0552  112 GLU A OE1 
815  O OE2 . GLU A 126 ? 0.5077 0.4349 0.5060 0.0433  -0.0122 0.0652  112 GLU A OE2 
816  N N   . LEU A 127 ? 0.3449 0.3068 0.3169 0.0369  0.0017  0.0741  113 LEU A N   
817  C CA  . LEU A 127 ? 0.3461 0.3138 0.3175 0.0335  0.0046  0.0736  113 LEU A CA  
818  C C   . LEU A 127 ? 0.3378 0.3019 0.3166 0.0291  0.0043  0.0686  113 LEU A C   
819  O O   . LEU A 127 ? 0.3314 0.2920 0.3162 0.0255  0.0059  0.0717  113 LEU A O   
820  C CB  . LEU A 127 ? 0.3319 0.3009 0.3021 0.0325  0.0081  0.0824  113 LEU A CB  
821  C CG  . LEU A 127 ? 0.3912 0.3645 0.3529 0.0371  0.0088  0.0881  113 LEU A CG  
822  C CD1 . LEU A 127 ? 0.3613 0.3380 0.3217 0.0352  0.0132  0.0960  113 LEU A CD1 
823  C CD2 . LEU A 127 ? 0.3461 0.3278 0.3006 0.0406  0.0072  0.0821  113 LEU A CD2 
824  N N   . LEU A 128 ? 0.3129 0.2786 0.2913 0.0294  0.0022  0.0608  114 LEU A N   
825  C CA  . LEU A 128 ? 0.3111 0.2736 0.2952 0.0262  0.0012  0.0553  114 LEU A CA  
826  C C   . LEU A 128 ? 0.3017 0.2696 0.2849 0.0233  0.0027  0.0524  114 LEU A C   
827  O O   . LEU A 128 ? 0.2873 0.2621 0.2651 0.0244  0.0037  0.0523  114 LEU A O   
828  C CB  . LEU A 128 ? 0.3182 0.2795 0.3018 0.0283  -0.0016 0.0487  114 LEU A CB  
829  C CG  . LEU A 128 ? 0.3671 0.3223 0.3535 0.0311  -0.0038 0.0494  114 LEU A CG  
830  C CD1 . LEU A 128 ? 0.3746 0.3298 0.3619 0.0323  -0.0060 0.0416  114 LEU A CD1 
831  C CD2 . LEU A 128 ? 0.3695 0.3165 0.3632 0.0292  -0.0039 0.0535  114 LEU A CD2 
832  N N   . HIS A 129 ? 0.2957 0.2605 0.2846 0.0198  0.0023  0.0497  115 HIS A N   
833  C CA  . HIS A 129 ? 0.2871 0.2562 0.2757 0.0173  0.0029  0.0461  115 HIS A CA  
834  C C   . HIS A 129 ? 0.2813 0.2544 0.2648 0.0188  0.0014  0.0403  115 HIS A C   
835  O O   . HIS A 129 ? 0.2567 0.2280 0.2392 0.0208  -0.0003 0.0374  115 HIS A O   
836  C CB  . HIS A 129 ? 0.2987 0.2632 0.2945 0.0138  0.0020  0.0437  115 HIS A CB  
837  C CG  . HIS A 129 ? 0.3121 0.2720 0.3097 0.0144  -0.0008 0.0382  115 HIS A CG  
838  N ND1 . HIS A 129 ? 0.3283 0.2819 0.3299 0.0156  -0.0021 0.0391  115 HIS A ND1 
839  C CD2 . HIS A 129 ? 0.3306 0.2914 0.3267 0.0141  -0.0025 0.0318  115 HIS A CD2 
840  C CE1 . HIS A 129 ? 0.3841 0.3355 0.3865 0.0162  -0.0044 0.0329  115 HIS A CE1 
841  N NE2 . HIS A 129 ? 0.3261 0.2820 0.3248 0.0152  -0.0045 0.0287  115 HIS A NE2 
842  N N   . HIS A 130 ? 0.2577 0.2364 0.2387 0.0178  0.0021  0.0387  116 HIS A N   
843  C CA  . HIS A 130 ? 0.2655 0.2486 0.2422 0.0189  0.0011  0.0342  116 HIS A CA  
844  C C   . HIS A 130 ? 0.2679 0.2547 0.2399 0.0226  0.0010  0.0351  116 HIS A C   
845  O O   . HIS A 130 ? 0.2287 0.2177 0.1984 0.0238  -0.0003 0.0311  116 HIS A O   
846  C CB  . HIS A 130 ? 0.2465 0.2264 0.2240 0.0182  -0.0008 0.0289  116 HIS A CB  
847  C CG  . HIS A 130 ? 0.2657 0.2419 0.2474 0.0152  -0.0014 0.0271  116 HIS A CG  
848  N ND1 . HIS A 130 ? 0.2701 0.2468 0.2551 0.0128  -0.0005 0.0291  116 HIS A ND1 
849  C CD2 . HIS A 130 ? 0.2760 0.2485 0.2594 0.0144  -0.0030 0.0231  116 HIS A CD2 
850  C CE1 . HIS A 130 ? 0.2614 0.2344 0.2502 0.0107  -0.0019 0.0263  116 HIS A CE1 
851  N NE2 . HIS A 130 ? 0.2876 0.2582 0.2752 0.0117  -0.0035 0.0226  116 HIS A NE2 
852  N N   . THR A 131 ? 0.2513 0.2389 0.2219 0.0244  0.0022  0.0402  117 THR A N   
853  C CA  . THR A 131 ? 0.2593 0.2519 0.2250 0.0282  0.0019  0.0408  117 THR A CA  
854  C C   . THR A 131 ? 0.2475 0.2462 0.2103 0.0286  0.0037  0.0436  117 THR A C   
855  O O   . THR A 131 ? 0.2659 0.2647 0.2311 0.0260  0.0056  0.0458  117 THR A O   
856  C CB  . THR A 131 ? 0.2704 0.2596 0.2352 0.0313  0.0012  0.0443  117 THR A CB  
857  O OG1 . THR A 131 ? 0.2455 0.2331 0.2104 0.0311  0.0032  0.0512  117 THR A OG1 
858  C CG2 . THR A 131 ? 0.2703 0.2529 0.2391 0.0307  -0.0004 0.0417  117 THR A CG2 
859  N N   . LEU A 132 ? 0.2597 0.2641 0.2177 0.0321  0.0030  0.0430  118 LEU A N   
860  C CA  . LEU A 132 ? 0.2596 0.2709 0.2142 0.0335  0.0047  0.0453  118 LEU A CA  
861  C C   . LEU A 132 ? 0.2744 0.2851 0.2268 0.0349  0.0068  0.0527  118 LEU A C   
862  O O   . LEU A 132 ? 0.2605 0.2776 0.2091 0.0365  0.0086  0.0554  118 LEU A O   
863  C CB  . LEU A 132 ? 0.2600 0.2778 0.2106 0.0370  0.0028  0.0413  118 LEU A CB  
864  C CG  . LEU A 132 ? 0.2553 0.2740 0.2083 0.0355  0.0008  0.0345  118 LEU A CG  
865  C CD1 . LEU A 132 ? 0.2653 0.2910 0.2156 0.0390  -0.0011 0.0307  118 LEU A CD1 
866  C CD2 . LEU A 132 ? 0.2306 0.2489 0.1869 0.0316  0.0018  0.0333  118 LEU A CD2 
867  N N   . GLY A 133 ? 0.2726 0.2759 0.2274 0.0344  0.0067  0.0563  119 GLY A N   
868  C CA  . GLY A 133 ? 0.2836 0.2853 0.2368 0.0356  0.0087  0.0642  119 GLY A CA  
869  C C   . GLY A 133 ? 0.3012 0.3059 0.2475 0.0409  0.0076  0.0666  119 GLY A C   
870  O O   . GLY A 133 ? 0.3028 0.3083 0.2456 0.0425  0.0095  0.0736  119 GLY A O   
871  N N   . ASP A 134 ? 0.2994 0.3058 0.2439 0.0437  0.0044  0.0610  120 ASP A N   
872  C CA  . ASP A 134 ? 0.3070 0.3167 0.2455 0.0492  0.0025  0.0620  120 ASP A CA  
873  C C   . ASP A 134 ? 0.3117 0.3154 0.2522 0.0512  -0.0005 0.0609  120 ASP A C   
874  O O   . ASP A 134 ? 0.2978 0.3039 0.2341 0.0560  -0.0028 0.0607  120 ASP A O   
875  C CB  . ASP A 134 ? 0.2999 0.3184 0.2352 0.0515  0.0010  0.0557  120 ASP A CB  
876  C CG  . ASP A 134 ? 0.3085 0.3261 0.2488 0.0490  -0.0008 0.0480  120 ASP A CG  
877  O OD1 . ASP A 134 ? 0.3109 0.3217 0.2563 0.0460  -0.0008 0.0472  120 ASP A OD1 
878  O OD2 . ASP A 134 ? 0.3188 0.3425 0.2583 0.0500  -0.0020 0.0427  120 ASP A OD2 
879  N N   . GLY A 135 ? 0.3007 0.2968 0.2476 0.0480  -0.0007 0.0599  121 GLY A N   
880  C CA  . GLY A 135 ? 0.3043 0.2954 0.2537 0.0501  -0.0035 0.0579  121 GLY A CA  
881  C C   . GLY A 135 ? 0.3112 0.3061 0.2612 0.0515  -0.0060 0.0499  121 GLY A C   
882  O O   . GLY A 135 ? 0.3108 0.3034 0.2625 0.0541  -0.0084 0.0479  121 GLY A O   
883  N N   . GLU A 136 ? 0.3099 0.3106 0.2595 0.0498  -0.0054 0.0454  122 GLU A N   
884  C CA  . GLU A 136 ? 0.3081 0.3131 0.2589 0.0509  -0.0074 0.0383  122 GLU A CA  
885  C C   . GLU A 136 ? 0.2977 0.2998 0.2535 0.0465  -0.0068 0.0339  122 GLU A C   
886  O O   . GLU A 136 ? 0.2722 0.2734 0.2289 0.0428  -0.0050 0.0345  122 GLU A O   
887  C CB  . GLU A 136 ? 0.3201 0.3333 0.2672 0.0522  -0.0076 0.0361  122 GLU A CB  
888  C CG  . GLU A 136 ? 0.3930 0.4112 0.3349 0.0578  -0.0094 0.0378  122 GLU A CG  
889  C CD  . GLU A 136 ? 0.5091 0.5274 0.4526 0.0613  -0.0126 0.0342  122 GLU A CD  
890  O OE1 . GLU A 136 ? 0.4834 0.5026 0.4318 0.0598  -0.0135 0.0282  122 GLU A OE1 
891  O OE2 . GLU A 136 ? 0.5006 0.5185 0.4407 0.0657  -0.0141 0.0377  122 GLU A OE2 
892  N N   . PHE A 137 ? 0.2860 0.2871 0.2450 0.0471  -0.0083 0.0294  123 PHE A N   
893  C CA  . PHE A 137 ? 0.2759 0.2744 0.2389 0.0433  -0.0076 0.0256  123 PHE A CA  
894  C C   . PHE A 137 ? 0.3098 0.3132 0.2742 0.0427  -0.0081 0.0197  123 PHE A C   
895  O O   . PHE A 137 ? 0.2998 0.3017 0.2669 0.0399  -0.0075 0.0166  123 PHE A O   
896  C CB  . PHE A 137 ? 0.2820 0.2743 0.2485 0.0438  -0.0083 0.0256  123 PHE A CB  
897  C CG  . PHE A 137 ? 0.2927 0.2787 0.2597 0.0429  -0.0075 0.0311  123 PHE A CG  
898  C CD1 . PHE A 137 ? 0.3016 0.2856 0.2667 0.0462  -0.0083 0.0364  123 PHE A CD1 
899  C CD2 . PHE A 137 ? 0.2920 0.2740 0.2615 0.0389  -0.0062 0.0313  123 PHE A CD2 
900  C CE1 . PHE A 137 ? 0.3285 0.3065 0.2950 0.0450  -0.0073 0.0423  123 PHE A CE1 
901  C CE2 . PHE A 137 ? 0.2823 0.2586 0.2537 0.0377  -0.0055 0.0363  123 PHE A CE2 
902  C CZ  . PHE A 137 ? 0.3218 0.2959 0.2919 0.0406  -0.0058 0.0421  123 PHE A CZ  
903  N N   . ARG A 138 ? 0.2649 0.2744 0.2279 0.0451  -0.0093 0.0181  124 ARG A N   
904  C CA  . ARG A 138 ? 0.2971 0.3113 0.2628 0.0443  -0.0099 0.0128  124 ARG A CA  
905  C C   . ARG A 138 ? 0.3073 0.3257 0.2719 0.0428  -0.0097 0.0118  124 ARG A C   
906  O O   . ARG A 138 ? 0.2963 0.3184 0.2637 0.0420  -0.0104 0.0077  124 ARG A O   
907  C CB  . ARG A 138 ? 0.3381 0.3562 0.3054 0.0485  -0.0121 0.0101  124 ARG A CB  
908  C CG  . ARG A 138 ? 0.3690 0.3829 0.3374 0.0508  -0.0128 0.0112  124 ARG A CG  
909  C CD  . ARG A 138 ? 0.4568 0.4737 0.4299 0.0524  -0.0140 0.0060  124 ARG A CD  
910  N NE  . ARG A 138 ? 0.5254 0.5376 0.5010 0.0529  -0.0140 0.0058  124 ARG A NE  
911  C CZ  . ARG A 138 ? 0.6908 0.7041 0.6695 0.0565  -0.0158 0.0035  124 ARG A CZ  
912  N NH1 . ARG A 138 ? 0.6341 0.6531 0.6139 0.0599  -0.0180 0.0011  124 ARG A NH1 
913  N NH2 . ARG A 138 ? 0.5984 0.6070 0.5796 0.0569  -0.0158 0.0030  124 ARG A NH2 
914  N N   . HIS A 139 ? 0.2841 0.3023 0.2453 0.0425  -0.0089 0.0153  125 HIS A N   
915  C CA  . HIS A 139 ? 0.2964 0.3187 0.2570 0.0414  -0.0090 0.0139  125 HIS A CA  
916  C C   . HIS A 139 ? 0.2708 0.2920 0.2348 0.0373  -0.0085 0.0108  125 HIS A C   
917  O O   . HIS A 139 ? 0.2732 0.2982 0.2395 0.0369  -0.0096 0.0073  125 HIS A O   
918  C CB  . HIS A 139 ? 0.2700 0.2916 0.2275 0.0407  -0.0074 0.0182  125 HIS A CB  
919  C CG  . HIS A 139 ? 0.2800 0.3041 0.2331 0.0447  -0.0076 0.0218  125 HIS A CG  
920  N ND1 . HIS A 139 ? 0.3021 0.3323 0.2532 0.0490  -0.0096 0.0199  125 HIS A ND1 
921  C CD2 . HIS A 139 ? 0.2821 0.3038 0.2324 0.0451  -0.0059 0.0276  125 HIS A CD2 
922  C CE1 . HIS A 139 ? 0.3335 0.3649 0.2796 0.0521  -0.0092 0.0245  125 HIS A CE1 
923  N NE2 . HIS A 139 ? 0.3061 0.3324 0.2518 0.0496  -0.0067 0.0295  125 HIS A NE2 
924  N N   . PHE A 140 ? 0.2648 0.2806 0.2293 0.0342  -0.0069 0.0122  126 PHE A N   
925  C CA  . PHE A 140 ? 0.2474 0.2619 0.2136 0.0303  -0.0064 0.0103  126 PHE A CA  
926  C C   . PHE A 140 ? 0.2650 0.2806 0.2342 0.0296  -0.0066 0.0068  126 PHE A C   
927  O O   . PHE A 140 ? 0.2470 0.2639 0.2179 0.0274  -0.0068 0.0048  126 PHE A O   
928  C CB  . PHE A 140 ? 0.2421 0.2511 0.2078 0.0277  -0.0051 0.0125  126 PHE A CB  
929  C CG  . PHE A 140 ? 0.2452 0.2529 0.2091 0.0284  -0.0044 0.0165  126 PHE A CG  
930  C CD1 . PHE A 140 ? 0.2459 0.2576 0.2084 0.0294  -0.0045 0.0176  126 PHE A CD1 
931  C CD2 . PHE A 140 ? 0.2356 0.2384 0.2000 0.0283  -0.0037 0.0191  126 PHE A CD2 
932  C CE1 . PHE A 140 ? 0.2280 0.2394 0.1889 0.0299  -0.0032 0.0217  126 PHE A CE1 
933  C CE2 . PHE A 140 ? 0.2411 0.2427 0.2047 0.0285  -0.0027 0.0234  126 PHE A CE2 
934  C CZ  . PHE A 140 ? 0.2490 0.2552 0.2107 0.0293  -0.0022 0.0249  126 PHE A CZ  
935  N N   . TYR A 141 ? 0.2541 0.2694 0.2243 0.0316  -0.0067 0.0061  127 TYR A N   
936  C CA  . TYR A 141 ? 0.2905 0.3085 0.2641 0.0315  -0.0067 0.0026  127 TYR A CA  
937  C C   . TYR A 141 ? 0.2637 0.2872 0.2398 0.0323  -0.0082 0.0001  127 TYR A C   
938  O O   . TYR A 141 ? 0.2394 0.2647 0.2189 0.0299  -0.0078 -0.0021 127 TYR A O   
939  C CB  . TYR A 141 ? 0.2781 0.2959 0.2528 0.0345  -0.0071 0.0020  127 TYR A CB  
940  C CG  . TYR A 141 ? 0.3031 0.3248 0.2822 0.0350  -0.0071 -0.0020 127 TYR A CG  
941  C CD1 . TYR A 141 ? 0.2892 0.3103 0.2701 0.0324  -0.0051 -0.0038 127 TYR A CD1 
942  C CD2 . TYR A 141 ? 0.3016 0.3284 0.2834 0.0383  -0.0090 -0.0041 127 TYR A CD2 
943  C CE1 . TYR A 141 ? 0.2917 0.3172 0.2772 0.0326  -0.0046 -0.0073 127 TYR A CE1 
944  C CE2 . TYR A 141 ? 0.3113 0.3422 0.2984 0.0386  -0.0089 -0.0080 127 TYR A CE2 
945  C CZ  . TYR A 141 ? 0.3291 0.3596 0.3184 0.0356  -0.0064 -0.0094 127 TYR A CZ  
946  O OH  . TYR A 141 ? 0.3227 0.3582 0.3177 0.0357  -0.0058 -0.0132 127 TYR A OH  
947  N N   . HIS A 142 ? 0.2904 0.3167 0.2651 0.0356  -0.0099 0.0006  128 HIS A N   
948  C CA  . HIS A 142 ? 0.2835 0.3154 0.2611 0.0369  -0.0119 -0.0025 128 HIS A CA  
949  C C   . HIS A 142 ? 0.2629 0.2949 0.2414 0.0340  -0.0119 -0.0030 128 HIS A C   
950  O O   . HIS A 142 ? 0.2361 0.2709 0.2193 0.0329  -0.0130 -0.0061 128 HIS A O   
951  C CB  . HIS A 142 ? 0.3039 0.3392 0.2787 0.0418  -0.0139 -0.0020 128 HIS A CB  
952  C CG  . HIS A 142 ? 0.3576 0.3936 0.3326 0.0453  -0.0147 -0.0022 128 HIS A CG  
953  N ND1 . HIS A 142 ? 0.4303 0.4654 0.4005 0.0490  -0.0154 0.0011  128 HIS A ND1 
954  C CD2 . HIS A 142 ? 0.3611 0.3984 0.3408 0.0456  -0.0150 -0.0052 128 HIS A CD2 
955  C CE1 . HIS A 142 ? 0.4051 0.4405 0.3770 0.0517  -0.0165 0.0000  128 HIS A CE1 
956  N NE2 . HIS A 142 ? 0.3511 0.3881 0.3290 0.0498  -0.0163 -0.0040 128 HIS A NE2 
957  N N   . MET A 143 ? 0.2450 0.2736 0.2198 0.0325  -0.0109 0.0000  129 MET A N   
958  C CA  . MET A 143 ? 0.2511 0.2796 0.2269 0.0300  -0.0113 -0.0006 129 MET A CA  
959  C C   . MET A 143 ? 0.2585 0.2844 0.2373 0.0260  -0.0104 -0.0014 129 MET A C   
960  O O   . MET A 143 ? 0.2244 0.2508 0.2058 0.0243  -0.0115 -0.0027 129 MET A O   
961  C CB  . MET A 143 ? 0.2649 0.2911 0.2368 0.0295  -0.0105 0.0025  129 MET A CB  
962  C CG  . MET A 143 ? 0.2444 0.2736 0.2130 0.0334  -0.0108 0.0040  129 MET A CG  
963  S SD  . MET A 143 ? 0.3108 0.3370 0.2753 0.0328  -0.0087 0.0089  129 MET A SD  
964  C CE  . MET A 143 ? 0.2418 0.2670 0.2078 0.0294  -0.0087 0.0082  129 MET A CE  
965  N N   . SER A 144 ? 0.2407 0.2642 0.2192 0.0248  -0.0087 -0.0008 130 SER A N   
966  C CA  . SER A 144 ? 0.2812 0.3030 0.2615 0.0212  -0.0075 -0.0012 130 SER A CA  
967  C C   . SER A 144 ? 0.2697 0.2956 0.2558 0.0210  -0.0077 -0.0040 130 SER A C   
968  O O   . SER A 144 ? 0.2680 0.2931 0.2562 0.0177  -0.0066 -0.0040 130 SER A O   
969  C CB  . SER A 144 ? 0.2534 0.2715 0.2307 0.0201  -0.0054 0.0002  130 SER A CB  
970  O OG  . SER A 144 ? 0.3175 0.3337 0.2946 0.0166  -0.0041 0.0006  130 SER A OG  
971  N N   . GLU A 145 ? 0.2718 0.3020 0.2606 0.0242  -0.0092 -0.0063 131 GLU A N   
972  C CA  . GLU A 145 ? 0.2886 0.3231 0.2841 0.0241  -0.0095 -0.0094 131 GLU A CA  
973  C C   . GLU A 145 ? 0.2882 0.3235 0.2889 0.0212  -0.0104 -0.0106 131 GLU A C   
974  O O   . GLU A 145 ? 0.2820 0.3184 0.2876 0.0185  -0.0089 -0.0112 131 GLU A O   
975  C CB  . GLU A 145 ? 0.3119 0.3510 0.3089 0.0288  -0.0118 -0.0119 131 GLU A CB  
976  C CG  . GLU A 145 ? 0.4081 0.4531 0.4132 0.0299  -0.0131 -0.0162 131 GLU A CG  
977  C CD  . GLU A 145 ? 0.5818 0.6289 0.5942 0.0273  -0.0142 -0.0185 131 GLU A CD  
978  O OE1 . GLU A 145 ? 0.4172 0.4645 0.4294 0.0280  -0.0166 -0.0192 131 GLU A OE1 
979  O OE2 . GLU A 145 ? 0.5276 0.5767 0.5465 0.0248  -0.0128 -0.0199 131 GLU A OE2 
980  N N   . PRO A 146 ? 0.2743 0.3092 0.2749 0.0216  -0.0127 -0.0108 132 PRO A N   
981  C CA  . PRO A 146 ? 0.2724 0.3073 0.2790 0.0189  -0.0139 -0.0120 132 PRO A CA  
982  C C   . PRO A 146 ? 0.2638 0.2941 0.2695 0.0142  -0.0116 -0.0087 132 PRO A C   
983  O O   . PRO A 146 ? 0.2476 0.2777 0.2592 0.0114  -0.0120 -0.0091 132 PRO A O   
984  C CB  . PRO A 146 ? 0.2800 0.3154 0.2855 0.0210  -0.0168 -0.0130 132 PRO A CB  
985  C CG  . PRO A 146 ? 0.2961 0.3342 0.2969 0.0255  -0.0174 -0.0135 132 PRO A CG  
986  C CD  . PRO A 146 ? 0.2822 0.3177 0.2783 0.0249  -0.0144 -0.0106 132 PRO A CD  
987  N N   . ILE A 147 ? 0.2349 0.2613 0.2336 0.0133  -0.0095 -0.0057 133 ILE A N   
988  C CA  . ILE A 147 ? 0.2415 0.2635 0.2381 0.0094  -0.0080 -0.0027 133 ILE A CA  
989  C C   . ILE A 147 ? 0.2477 0.2696 0.2424 0.0077  -0.0045 -0.0014 133 ILE A C   
990  O O   . ILE A 147 ? 0.2074 0.2259 0.1978 0.0054  -0.0029 0.0012  133 ILE A O   
991  C CB  . ILE A 147 ? 0.2281 0.2458 0.2188 0.0095  -0.0088 -0.0006 133 ILE A CB  
992  C CG1 . ILE A 147 ? 0.2335 0.2508 0.2187 0.0119  -0.0079 -0.0001 133 ILE A CG1 
993  C CG2 . ILE A 147 ? 0.2245 0.2429 0.2180 0.0107  -0.0121 -0.0021 133 ILE A CG2 
994  C CD1 . ILE A 147 ? 0.2060 0.2196 0.1864 0.0117  -0.0085 0.0018  133 ILE A CD1 
995  N N   . THR A 148 ? 0.2237 0.2500 0.2219 0.0092  -0.0034 -0.0036 134 THR A N   
996  C CA  . THR A 148 ? 0.2406 0.2682 0.2381 0.0078  0.0000  -0.0033 134 THR A CA  
997  C C   . THR A 148 ? 0.2607 0.2939 0.2667 0.0075  0.0008  -0.0058 134 THR A C   
998  O O   . THR A 148 ? 0.2169 0.2531 0.2284 0.0094  -0.0018 -0.0086 134 THR A O   
999  C CB  . THR A 148 ? 0.2431 0.2700 0.2354 0.0105  0.0008  -0.0037 134 THR A CB  
1000 O OG1 . THR A 148 ? 0.2587 0.2882 0.2532 0.0143  -0.0012 -0.0060 134 THR A OG1 
1001 C CG2 . THR A 148 ? 0.2381 0.2595 0.2231 0.0103  0.0003  -0.0013 134 THR A CG2 
1002 N N   . VAL A 149 ? 0.2681 0.3033 0.2754 0.0049  0.0043  -0.0051 135 VAL A N   
1003 C CA  . VAL A 149 ? 0.2673 0.3086 0.2836 0.0045  0.0055  -0.0077 135 VAL A CA  
1004 C C   . VAL A 149 ? 0.2811 0.3263 0.2977 0.0079  0.0063  -0.0108 135 VAL A C   
1005 O O   . VAL A 149 ? 0.2860 0.3369 0.3106 0.0088  0.0062  -0.0140 135 VAL A O   
1006 C CB  . VAL A 149 ? 0.2687 0.3116 0.2881 -0.0002 0.0094  -0.0055 135 VAL A CB  
1007 C CG1 . VAL A 149 ? 0.2547 0.2950 0.2783 -0.0034 0.0079  -0.0032 135 VAL A CG1 
1008 C CG2 . VAL A 149 ? 0.2602 0.3011 0.2706 -0.0013 0.0128  -0.0028 135 VAL A CG2 
1009 N N   . ALA A 150 ? 0.2494 0.2918 0.2583 0.0097  0.0069  -0.0101 136 ALA A N   
1010 C CA  . ALA A 150 ? 0.2924 0.3375 0.3015 0.0132  0.0071  -0.0129 136 ALA A CA  
1011 C C   . ALA A 150 ? 0.2819 0.3216 0.2830 0.0156  0.0057  -0.0116 136 ALA A C   
1012 O O   . ALA A 150 ? 0.2691 0.3040 0.2641 0.0138  0.0062  -0.0088 136 ALA A O   
1013 C CB  . ALA A 150 ? 0.2690 0.3184 0.2799 0.0119  0.0112  -0.0141 136 ALA A CB  
1014 N N   . GLN A 151 ? 0.2575 0.2978 0.2590 0.0198  0.0038  -0.0134 137 GLN A N   
1015 C CA  . GLN A 151 ? 0.2545 0.2898 0.2496 0.0220  0.0028  -0.0121 137 GLN A CA  
1016 C C   . GLN A 151 ? 0.2765 0.3138 0.2739 0.0260  0.0021  -0.0147 137 GLN A C   
1017 O O   . GLN A 151 ? 0.2690 0.3116 0.2724 0.0277  0.0014  -0.0175 137 GLN A O   
1018 C CB  . GLN A 151 ? 0.2655 0.2970 0.2572 0.0228  0.0001  -0.0097 137 GLN A CB  
1019 C CG  . GLN A 151 ? 0.3184 0.3536 0.3142 0.0251  -0.0024 -0.0112 137 GLN A CG  
1020 C CD  . GLN A 151 ? 0.3556 0.3882 0.3473 0.0270  -0.0049 -0.0091 137 GLN A CD  
1021 O OE1 . GLN A 151 ? 0.3086 0.3366 0.2953 0.0258  -0.0045 -0.0063 137 GLN A OE1 
1022 N NE2 . GLN A 151 ? 0.3341 0.3704 0.3284 0.0302  -0.0074 -0.0108 137 GLN A NE2 
1023 N N   . ALA A 152 ? 0.2656 0.2986 0.2587 0.0275  0.0019  -0.0139 138 ALA A N   
1024 C CA  . ALA A 152 ? 0.2781 0.3116 0.2731 0.0315  0.0009  -0.0160 138 ALA A CA  
1025 C C   . ALA A 152 ? 0.2745 0.3012 0.2646 0.0332  -0.0007 -0.0134 138 ALA A C   
1026 O O   . ALA A 152 ? 0.2432 0.2655 0.2289 0.0308  0.0001  -0.0112 138 ALA A O   
1027 C CB  . ALA A 152 ? 0.2701 0.3070 0.2677 0.0312  0.0035  -0.0194 138 ALA A CB  
1028 N N   . ILE A 153 ? 0.2727 0.2985 0.2639 0.0373  -0.0030 -0.0136 139 ILE A N   
1029 C CA  . ILE A 153 ? 0.2873 0.3067 0.2756 0.0391  -0.0042 -0.0114 139 ILE A CA  
1030 C C   . ILE A 153 ? 0.2800 0.2997 0.2714 0.0411  -0.0039 -0.0149 139 ILE A C   
1031 O O   . ILE A 153 ? 0.2933 0.3167 0.2890 0.0442  -0.0050 -0.0177 139 ILE A O   
1032 C CB  . ILE A 153 ? 0.3021 0.3197 0.2891 0.0424  -0.0070 -0.0084 139 ILE A CB  
1033 C CG1 . ILE A 153 ? 0.2972 0.3151 0.2809 0.0407  -0.0072 -0.0054 139 ILE A CG1 
1034 C CG2 . ILE A 153 ? 0.3077 0.3184 0.2930 0.0442  -0.0081 -0.0058 139 ILE A CG2 
1035 C CD1 . ILE A 153 ? 0.3408 0.3591 0.3229 0.0445  -0.0097 -0.0029 139 ILE A CD1 
1036 N N   . LEU A 154 ? 0.2724 0.2885 0.2620 0.0395  -0.0027 -0.0155 140 LEU A N   
1037 C CA  . LEU A 154 ? 0.2774 0.2946 0.2701 0.0413  -0.0022 -0.0198 140 LEU A CA  
1038 C C   . LEU A 154 ? 0.2825 0.2948 0.2771 0.0455  -0.0052 -0.0194 140 LEU A C   
1039 O O   . LEU A 154 ? 0.2672 0.2729 0.2595 0.0456  -0.0067 -0.0155 140 LEU A O   
1040 C CB  . LEU A 154 ? 0.2720 0.2873 0.2616 0.0385  -0.0003 -0.0209 140 LEU A CB  
1041 C CG  . LEU A 154 ? 0.2442 0.2640 0.2315 0.0345  0.0028  -0.0210 140 LEU A CG  
1042 C CD1 . LEU A 154 ? 0.2463 0.2649 0.2300 0.0326  0.0045  -0.0225 140 LEU A CD1 
1043 C CD2 . LEU A 154 ? 0.2329 0.2610 0.2248 0.0348  0.0046  -0.0239 140 LEU A CD2 
1044 N N   . THR A 155 ? 0.2716 0.2875 0.2712 0.0489  -0.0060 -0.0234 141 THR A N   
1045 C CA  . THR A 155 ? 0.2790 0.2904 0.2814 0.0532  -0.0091 -0.0237 141 THR A CA  
1046 C C   . THR A 155 ? 0.2717 0.2849 0.2781 0.0548  -0.0086 -0.0297 141 THR A C   
1047 O O   . THR A 155 ? 0.2564 0.2759 0.2634 0.0529  -0.0056 -0.0335 141 THR A O   
1048 C CB  . THR A 155 ? 0.2828 0.2967 0.2877 0.0571  -0.0117 -0.0231 141 THR A CB  
1049 O OG1 . THR A 155 ? 0.2684 0.2905 0.2786 0.0585  -0.0108 -0.0287 141 THR A OG1 
1050 C CG2 . THR A 155 ? 0.2777 0.2928 0.2788 0.0556  -0.0118 -0.0187 141 THR A CG2 
1051 N N   . GLU A 156 ? 0.2844 0.2921 0.2937 0.0584  -0.0115 -0.0303 142 GLU A N   
1052 C CA  . GLU A 156 ? 0.2873 0.2969 0.3016 0.0611  -0.0118 -0.0368 142 GLU A CA  
1053 C C   . GLU A 156 ? 0.2915 0.3110 0.3105 0.0629  -0.0106 -0.0419 142 GLU A C   
1054 O O   . GLU A 156 ? 0.2264 0.2512 0.2484 0.0634  -0.0087 -0.0478 142 GLU A O   
1055 C CB  . GLU A 156 ? 0.3000 0.3016 0.3178 0.0652  -0.0160 -0.0361 142 GLU A CB  
1056 C CG  . GLU A 156 ? 0.3385 0.3418 0.3626 0.0690  -0.0172 -0.0432 142 GLU A CG  
1057 C CD  . GLU A 156 ? 0.3547 0.3486 0.3827 0.0727  -0.0217 -0.0420 142 GLU A CD  
1058 O OE1 . GLU A 156 ? 0.3738 0.3625 0.4006 0.0739  -0.0241 -0.0358 142 GLU A OE1 
1059 O OE2 . GLU A 156 ? 0.3519 0.3437 0.3840 0.0745  -0.0229 -0.0471 142 GLU A OE2 
1060 N N   . GLN A 157 ? 0.2645 0.2872 0.2846 0.0641  -0.0116 -0.0399 143 GLN A N   
1061 C CA  . GLN A 157 ? 0.2759 0.3079 0.3019 0.0662  -0.0112 -0.0446 143 GLN A CA  
1062 C C   . GLN A 157 ? 0.2641 0.3046 0.2899 0.0619  -0.0070 -0.0457 143 GLN A C   
1063 O O   . GLN A 157 ? 0.2530 0.3022 0.2849 0.0629  -0.0057 -0.0503 143 GLN A O   
1064 C CB  . GLN A 157 ? 0.2910 0.3219 0.3188 0.0703  -0.0153 -0.0423 143 GLN A CB  
1065 C CG  . GLN A 157 ? 0.3159 0.3381 0.3444 0.0747  -0.0197 -0.0406 143 GLN A CG  
1066 C CD  . GLN A 157 ? 0.3617 0.3844 0.3931 0.0800  -0.0240 -0.0400 143 GLN A CD  
1067 O OE1 . GLN A 157 ? 0.3734 0.4044 0.4083 0.0812  -0.0241 -0.0429 143 GLN A OE1 
1068 N NE2 . GLN A 157 ? 0.4139 0.4277 0.4440 0.0833  -0.0278 -0.0359 143 GLN A NE2 
1069 N N   . ASN A 158 ? 0.2360 0.2744 0.2557 0.0572  -0.0047 -0.0415 144 ASN A N   
1070 C CA  . ASN A 158 ? 0.2661 0.3116 0.2859 0.0530  -0.0010 -0.0418 144 ASN A CA  
1071 C C   . ASN A 158 ? 0.2818 0.3267 0.2964 0.0485  0.0027  -0.0410 144 ASN A C   
1072 O O   . ASN A 158 ? 0.2608 0.3113 0.2755 0.0448  0.0061  -0.0408 144 ASN A O   
1073 C CB  . ASN A 158 ? 0.2870 0.3322 0.3054 0.0519  -0.0024 -0.0376 144 ASN A CB  
1074 C CG  . ASN A 158 ? 0.3065 0.3436 0.3173 0.0496  -0.0032 -0.0317 144 ASN A CG  
1075 O OD1 . ASN A 158 ? 0.2571 0.2891 0.2639 0.0481  -0.0023 -0.0306 144 ASN A OD1 
1076 N ND2 . ASN A 158 ? 0.3070 0.3437 0.3163 0.0495  -0.0048 -0.0284 144 ASN A ND2 
1077 N N   . ALA A 159 ? 0.2703 0.3087 0.2809 0.0487  0.0021  -0.0405 145 ALA A N   
1078 C CA  . ALA A 159 ? 0.2794 0.3152 0.2836 0.0447  0.0043  -0.0385 145 ALA A CA  
1079 C C   . ALA A 159 ? 0.2745 0.3183 0.2782 0.0415  0.0090  -0.0405 145 ALA A C   
1080 O O   . ALA A 159 ? 0.2790 0.3236 0.2795 0.0375  0.0109  -0.0371 145 ALA A O   
1081 C CB  . ALA A 159 ? 0.2877 0.3173 0.2900 0.0463  0.0028  -0.0400 145 ALA A CB  
1082 N N   . CYS A 160 ? 0.2812 0.3310 0.2881 0.0432  0.0109  -0.0459 146 CYS A N   
1083 C CA  . CYS A 160 ? 0.2944 0.3512 0.2992 0.0401  0.0158  -0.0473 146 CYS A CA  
1084 C C   . CYS A 160 ? 0.2776 0.3415 0.2863 0.0373  0.0185  -0.0458 146 CYS A C   
1085 O O   . CYS A 160 ? 0.2459 0.3125 0.2511 0.0331  0.0221  -0.0434 146 CYS A O   
1086 C CB  . CYS A 160 ? 0.2915 0.3538 0.2986 0.0430  0.0174  -0.0539 146 CYS A CB  
1087 S SG  . CYS A 160 ? 0.3101 0.3642 0.3120 0.0451  0.0146  -0.0558 146 CYS A SG  
1088 N N   . TYR A 161 ? 0.2583 0.3250 0.2742 0.0394  0.0167  -0.0470 147 TYR A N   
1089 C CA  . TYR A 161 ? 0.2820 0.3553 0.3025 0.0364  0.0192  -0.0459 147 TYR A CA  
1090 C C   . TYR A 161 ? 0.2811 0.3492 0.2987 0.0336  0.0174  -0.0404 147 TYR A C   
1091 O O   . TYR A 161 ? 0.2857 0.3578 0.3053 0.0299  0.0198  -0.0385 147 TYR A O   
1092 C CB  . TYR A 161 ? 0.2839 0.3644 0.3145 0.0395  0.0183  -0.0504 147 TYR A CB  
1093 C CG  . TYR A 161 ? 0.2851 0.3613 0.3185 0.0436  0.0128  -0.0503 147 TYR A CG  
1094 C CD1 . TYR A 161 ? 0.2796 0.3545 0.3139 0.0425  0.0107  -0.0471 147 TYR A CD1 
1095 C CD2 . TYR A 161 ? 0.2880 0.3621 0.3234 0.0489  0.0097  -0.0536 147 TYR A CD2 
1096 C CE1 . TYR A 161 ? 0.3116 0.3833 0.3475 0.0467  0.0056  -0.0469 147 TYR A CE1 
1097 C CE2 . TYR A 161 ? 0.2932 0.3634 0.3305 0.0529  0.0046  -0.0529 147 TYR A CE2 
1098 C CZ  . TYR A 161 ? 0.3261 0.3954 0.3632 0.0518  0.0027  -0.0494 147 TYR A CZ  
1099 O OH  . TYR A 161 ? 0.3326 0.3988 0.3706 0.0562  -0.0022 -0.0486 147 TYR A OH  
1100 N N   . GLU A 162 ? 0.2542 0.3138 0.2675 0.0353  0.0134  -0.0376 148 GLU A N   
1101 C CA  . GLU A 162 ? 0.2574 0.3125 0.2672 0.0326  0.0121  -0.0326 148 GLU A CA  
1102 C C   . GLU A 162 ? 0.2613 0.3137 0.2642 0.0284  0.0147  -0.0296 148 GLU A C   
1103 O O   . GLU A 162 ? 0.2726 0.3247 0.2745 0.0250  0.0153  -0.0263 148 GLU A O   
1104 C CB  . GLU A 162 ? 0.2693 0.3170 0.2764 0.0356  0.0076  -0.0304 148 GLU A CB  
1105 C CG  . GLU A 162 ? 0.3109 0.3610 0.3235 0.0392  0.0045  -0.0318 148 GLU A CG  
1106 C CD  . GLU A 162 ? 0.3133 0.3683 0.3300 0.0372  0.0047  -0.0314 148 GLU A CD  
1107 O OE1 . GLU A 162 ? 0.3339 0.3960 0.3564 0.0354  0.0074  -0.0340 148 GLU A OE1 
1108 O OE2 . GLU A 162 ? 0.3414 0.3934 0.3560 0.0374  0.0022  -0.0285 148 GLU A OE2 
1109 N N   . ILE A 163 ? 0.2352 0.2855 0.2335 0.0289  0.0156  -0.0308 149 ILE A N   
1110 C CA  . ILE A 163 ? 0.2604 0.3090 0.2519 0.0254  0.0179  -0.0284 149 ILE A CA  
1111 C C   . ILE A 163 ? 0.2453 0.3013 0.2386 0.0220  0.0224  -0.0281 149 ILE A C   
1112 O O   . ILE A 163 ? 0.2303 0.2851 0.2208 0.0182  0.0235  -0.0241 149 ILE A O   
1113 C CB  . ILE A 163 ? 0.2657 0.3119 0.2528 0.0272  0.0179  -0.0310 149 ILE A CB  
1114 C CG1 . ILE A 163 ? 0.2612 0.2986 0.2463 0.0294  0.0136  -0.0299 149 ILE A CG1 
1115 C CG2 . ILE A 163 ? 0.2644 0.3113 0.2444 0.0240  0.0208  -0.0296 149 ILE A CG2 
1116 C CD1 . ILE A 163 ? 0.2688 0.3040 0.2524 0.0320  0.0128  -0.0338 149 ILE A CD1 
1117 N N   . ASP A 164 ? 0.2370 0.3009 0.2358 0.0232  0.0250  -0.0322 150 ASP A N   
1118 C CA  . ASP A 164 ? 0.2486 0.3201 0.2497 0.0197  0.0298  -0.0316 150 ASP A CA  
1119 C C   . ASP A 164 ? 0.2530 0.3255 0.2599 0.0169  0.0294  -0.0287 150 ASP A C   
1120 O O   . ASP A 164 ? 0.2653 0.3396 0.2718 0.0126  0.0323  -0.0253 150 ASP A O   
1121 C CB  . ASP A 164 ? 0.2571 0.3378 0.2640 0.0217  0.0328  -0.0370 150 ASP A CB  
1122 C CG  . ASP A 164 ? 0.2649 0.3460 0.2659 0.0240  0.0340  -0.0403 150 ASP A CG  
1123 O OD1 . ASP A 164 ? 0.2523 0.3275 0.2445 0.0231  0.0333  -0.0379 150 ASP A OD1 
1124 O OD2 . ASP A 164 ? 0.2880 0.3755 0.2934 0.0269  0.0353  -0.0457 150 ASP A OD2 
1125 N N   . ARG A 165 ? 0.2449 0.3163 0.2574 0.0195  0.0256  -0.0301 151 ARG A N   
1126 C CA  . ARG A 165 ? 0.2564 0.3291 0.2749 0.0174  0.0246  -0.0282 151 ARG A CA  
1127 C C   . ARG A 165 ? 0.2507 0.3166 0.2634 0.0142  0.0234  -0.0230 151 ARG A C   
1128 O O   . ARG A 165 ? 0.2537 0.3212 0.2695 0.0104  0.0249  -0.0206 151 ARG A O   
1129 C CB  . ARG A 165 ? 0.2358 0.3087 0.2601 0.0214  0.0202  -0.0310 151 ARG A CB  
1130 C CG  . ARG A 165 ? 0.2412 0.3156 0.2718 0.0198  0.0184  -0.0300 151 ARG A CG  
1131 C CD  . ARG A 165 ? 0.2419 0.3161 0.2764 0.0244  0.0135  -0.0325 151 ARG A CD  
1132 N NE  . ARG A 165 ? 0.2694 0.3357 0.2960 0.0272  0.0099  -0.0303 151 ARG A NE  
1133 C CZ  . ARG A 165 ? 0.2857 0.3466 0.3077 0.0259  0.0080  -0.0267 151 ARG A CZ  
1134 N NH1 . ARG A 165 ? 0.2644 0.3258 0.2881 0.0220  0.0089  -0.0248 151 ARG A NH1 
1135 N NH2 . ARG A 165 ? 0.2819 0.3366 0.2977 0.0287  0.0051  -0.0249 151 ARG A NH2 
1136 N N   . VAL A 166 ? 0.2249 0.2832 0.2301 0.0157  0.0206  -0.0214 152 VAL A N   
1137 C CA  . VAL A 166 ? 0.2355 0.2876 0.2361 0.0133  0.0189  -0.0170 152 VAL A CA  
1138 C C   . VAL A 166 ? 0.2601 0.3119 0.2561 0.0092  0.0222  -0.0138 152 VAL A C   
1139 O O   . VAL A 166 ? 0.2299 0.2808 0.2272 0.0059  0.0224  -0.0106 152 VAL A O   
1140 C CB  . VAL A 166 ? 0.2529 0.2977 0.2476 0.0160  0.0153  -0.0161 152 VAL A CB  
1141 C CG1 . VAL A 166 ? 0.2410 0.2799 0.2302 0.0134  0.0141  -0.0119 152 VAL A CG1 
1142 C CG2 . VAL A 166 ? 0.2342 0.2789 0.2331 0.0197  0.0117  -0.0177 152 VAL A CG2 
1143 N N   . LEU A 167 ? 0.2425 0.2953 0.2332 0.0095  0.0247  -0.0147 153 LEU A N   
1144 C CA  . LEU A 167 ? 0.2496 0.3029 0.2347 0.0061  0.0281  -0.0117 153 LEU A CA  
1145 C C   . LEU A 167 ? 0.2842 0.3441 0.2754 0.0026  0.0321  -0.0104 153 LEU A C   
1146 O O   . LEU A 167 ? 0.2773 0.3356 0.2665 -0.0012 0.0333  -0.0059 153 LEU A O   
1147 C CB  . LEU A 167 ? 0.2392 0.2940 0.2183 0.0080  0.0300  -0.0143 153 LEU A CB  
1148 C CG  . LEU A 167 ? 0.2703 0.3184 0.2440 0.0110  0.0263  -0.0157 153 LEU A CG  
1149 C CD1 . LEU A 167 ? 0.2712 0.3218 0.2406 0.0132  0.0280  -0.0194 153 LEU A CD1 
1150 C CD2 . LEU A 167 ? 0.2591 0.3000 0.2266 0.0091  0.0240  -0.0114 153 LEU A CD2 
1151 N N   . THR A 168 ? 0.2663 0.3336 0.2656 0.0037  0.0339  -0.0141 154 THR A N   
1152 C CA  . THR A 168 ? 0.2886 0.3628 0.2955 0.0001  0.0378  -0.0130 154 THR A CA  
1153 C C   . THR A 168 ? 0.2814 0.3524 0.2938 -0.0025 0.0354  -0.0100 154 THR A C   
1154 O O   . THR A 168 ? 0.3047 0.3767 0.3192 -0.0069 0.0380  -0.0061 154 THR A O   
1155 C CB  . THR A 168 ? 0.2964 0.3794 0.3126 0.0022  0.0396  -0.0183 154 THR A CB  
1156 O OG1 . THR A 168 ? 0.3039 0.3907 0.3156 0.0046  0.0422  -0.0215 154 THR A OG1 
1157 C CG2 . THR A 168 ? 0.3156 0.4059 0.3413 -0.0019 0.0436  -0.0171 154 THR A CG2 
1158 N N   . THR A 169 ? 0.2639 0.3313 0.2789 0.0002  0.0304  -0.0118 155 THR A N   
1159 C CA  . THR A 169 ? 0.2987 0.3635 0.3191 -0.0017 0.0276  -0.0099 155 THR A CA  
1160 C C   . THR A 169 ? 0.2830 0.3405 0.2960 -0.0045 0.0269  -0.0047 155 THR A C   
1161 O O   . THR A 169 ? 0.2712 0.3276 0.2886 -0.0079 0.0267  -0.0018 155 THR A O   
1162 C CB  . THR A 169 ? 0.2728 0.3358 0.2960 0.0024  0.0225  -0.0132 155 THR A CB  
1163 O OG1 . THR A 169 ? 0.3099 0.3796 0.3401 0.0052  0.0228  -0.0180 155 THR A OG1 
1164 C CG2 . THR A 169 ? 0.2750 0.3362 0.3040 0.0009  0.0193  -0.0122 155 THR A CG2 
1165 N N   . MET A 170 ? 0.2702 0.3226 0.2728 -0.0029 0.0260  -0.0036 156 MET A N   
1166 C CA  . MET A 170 ? 0.2732 0.3192 0.2688 -0.0053 0.0252  0.0011  156 MET A CA  
1167 C C   . MET A 170 ? 0.2937 0.3419 0.2887 -0.0097 0.0295  0.0051  156 MET A C   
1168 O O   . MET A 170 ? 0.2972 0.3414 0.2920 -0.0127 0.0287  0.0094  156 MET A O   
1169 C CB  . MET A 170 ? 0.2484 0.2895 0.2335 -0.0032 0.0240  0.0013  156 MET A CB  
1170 C CG  . MET A 170 ? 0.2868 0.3220 0.2695 -0.0005 0.0193  0.0005  156 MET A CG  
1171 S SD  . MET A 170 ? 0.3502 0.3830 0.3254 0.0030  0.0185  -0.0019 156 MET A SD  
1172 C CE  . MET A 170 ? 0.2346 0.2625 0.2013 0.0003  0.0186  0.0023  156 MET A CE  
1173 N N   . LEU A 171 ? 0.3001 0.3545 0.2941 -0.0099 0.0342  0.0040  157 LEU A N   
1174 C CA  . LEU A 171 ? 0.3448 0.4022 0.3372 -0.0139 0.0391  0.0084  157 LEU A CA  
1175 C C   . LEU A 171 ? 0.3534 0.4136 0.3571 -0.0178 0.0404  0.0105  157 LEU A C   
1176 O O   . LEU A 171 ? 0.3704 0.4287 0.3734 -0.0218 0.0423  0.0161  157 LEU A O   
1177 C CB  . LEU A 171 ? 0.3566 0.4215 0.3461 -0.0128 0.0440  0.0060  157 LEU A CB  
1178 C CG  . LEU A 171 ? 0.3712 0.4342 0.3491 -0.0096 0.0436  0.0042  157 LEU A CG  
1179 C CD1 . LEU A 171 ? 0.3796 0.4513 0.3586 -0.0074 0.0474  -0.0006 157 LEU A CD1 
1180 C CD2 . LEU A 171 ? 0.4284 0.4877 0.3956 -0.0118 0.0447  0.0096  157 LEU A CD2 
1181 N N   . ARG A 172 ? 0.3166 0.3811 0.3311 -0.0165 0.0393  0.0061  158 ARG A N   
1182 C CA  . ARG A 172 ? 0.3527 0.4202 0.3796 -0.0201 0.0403  0.0072  158 ARG A CA  
1183 C C   . ARG A 172 ? 0.3224 0.3823 0.3512 -0.0217 0.0357  0.0101  158 ARG A C   
1184 O O   . ARG A 172 ? 0.3453 0.4041 0.3792 -0.0260 0.0370  0.0144  158 ARG A O   
1185 C CB  . ARG A 172 ? 0.3812 0.4556 0.4192 -0.0177 0.0395  0.0009  158 ARG A CB  
1186 C CG  . ARG A 172 ? 0.4036 0.4795 0.4556 -0.0200 0.0375  0.0002  158 ARG A CG  
1187 C CD  . ARG A 172 ? 0.4464 0.5295 0.5088 -0.0170 0.0364  -0.0066 158 ARG A CD  
1188 N NE  . ARG A 172 ? 0.6237 0.7031 0.6881 -0.0133 0.0298  -0.0100 158 ARG A NE  
1189 C CZ  . ARG A 172 ? 0.7042 0.7828 0.7637 -0.0080 0.0266  -0.0139 158 ARG A CZ  
1190 N NH1 . ARG A 172 ? 0.5086 0.5898 0.5624 -0.0055 0.0290  -0.0155 158 ARG A NH1 
1191 N NH2 . ARG A 172 ? 0.5207 0.5960 0.5812 -0.0049 0.0210  -0.0161 158 ARG A NH2 
1192 N N   . GLU A 173 ? 0.2985 0.3529 0.3232 -0.0181 0.0304  0.0080  159 GLU A N   
1193 C CA  . GLU A 173 ? 0.2949 0.3428 0.3220 -0.0188 0.0257  0.0094  159 GLU A CA  
1194 C C   . GLU A 173 ? 0.2834 0.3236 0.3001 -0.0198 0.0245  0.0143  159 GLU A C   
1195 O O   . GLU A 173 ? 0.2769 0.3118 0.2961 -0.0211 0.0211  0.0162  159 GLU A O   
1196 C CB  . GLU A 173 ? 0.2935 0.3408 0.3228 -0.0143 0.0207  0.0042  159 GLU A CB  
1197 C CG  . GLU A 173 ? 0.3237 0.3782 0.3638 -0.0127 0.0205  -0.0009 159 GLU A CG  
1198 C CD  . GLU A 173 ? 0.3844 0.4424 0.4373 -0.0168 0.0217  -0.0003 159 GLU A CD  
1199 O OE1 . GLU A 173 ? 0.3816 0.4349 0.4369 -0.0196 0.0201  0.0029  159 GLU A OE1 
1200 O OE2 . GLU A 173 ? 0.4024 0.4679 0.4638 -0.0171 0.0242  -0.0032 159 GLU A OE2 
1201 N N   . ARG A 174 ? 0.2626 0.3020 0.2681 -0.0190 0.0268  0.0158  160 ARG A N   
1202 C CA  . ARG A 174 ? 0.2845 0.3168 0.2796 -0.0193 0.0252  0.0197  160 ARG A CA  
1203 C C   . ARG A 174 ? 0.2598 0.2864 0.2540 -0.0166 0.0194  0.0178  160 ARG A C   
1204 O O   . ARG A 174 ? 0.2696 0.2906 0.2634 -0.0179 0.0166  0.0207  160 ARG A O   
1205 C CB  . ARG A 174 ? 0.2845 0.3141 0.2799 -0.0238 0.0268  0.0261  160 ARG A CB  
1206 C CG  . ARG A 174 ? 0.3195 0.3551 0.3165 -0.0270 0.0329  0.0289  160 ARG A CG  
1207 C CD  . ARG A 174 ? 0.3503 0.3908 0.3386 -0.0249 0.0367  0.0271  160 ARG A CD  
1208 N NE  . ARG A 174 ? 0.4310 0.4776 0.4203 -0.0283 0.0430  0.0304  160 ARG A NE  
1209 C CZ  . ARG A 174 ? 0.6154 0.6675 0.5972 -0.0274 0.0475  0.0300  160 ARG A CZ  
1210 N NH1 . ARG A 174 ? 0.4745 0.5261 0.4475 -0.0233 0.0460  0.0261  160 ARG A NH1 
1211 N NH2 . ARG A 174 ? 0.5659 0.6242 0.5494 -0.0308 0.0536  0.0335  160 ARG A NH2 
1212 N N   . ARG A 175 ? 0.2386 0.2669 0.2327 -0.0128 0.0178  0.0132  161 ARG A N   
1213 C CA  . ARG A 175 ? 0.2569 0.2812 0.2507 -0.0101 0.0129  0.0112  161 ARG A CA  
1214 C C   . ARG A 175 ? 0.2335 0.2579 0.2212 -0.0064 0.0126  0.0084  161 ARG A C   
1215 O O   . ARG A 175 ? 0.2183 0.2465 0.2042 -0.0056 0.0156  0.0070  161 ARG A O   
1216 C CB  . ARG A 175 ? 0.2258 0.2525 0.2301 -0.0095 0.0105  0.0083  161 ARG A CB  
1217 C CG  . ARG A 175 ? 0.2333 0.2567 0.2430 -0.0123 0.0083  0.0108  161 ARG A CG  
1218 C CD  . ARG A 175 ? 0.2496 0.2755 0.2699 -0.0111 0.0051  0.0069  161 ARG A CD  
1219 N NE  . ARG A 175 ? 0.2416 0.2627 0.2643 -0.0116 0.0010  0.0077  161 ARG A NE  
1220 C CZ  . ARG A 175 ? 0.2630 0.2854 0.2959 -0.0117 -0.0019 0.0050  161 ARG A CZ  
1221 N NH1 . ARG A 175 ? 0.2352 0.2635 0.2772 -0.0115 -0.0013 0.0017  161 ARG A NH1 
1222 N NH2 . ARG A 175 ? 0.2651 0.2831 0.2996 -0.0115 -0.0059 0.0052  161 ARG A NH2 
1223 N N   . PRO A 176 ? 0.2239 0.2445 0.2088 -0.0041 0.0090  0.0076  162 PRO A N   
1224 C CA  . PRO A 176 ? 0.2247 0.2444 0.2043 -0.0009 0.0085  0.0056  162 PRO A CA  
1225 C C   . PRO A 176 ? 0.2200 0.2444 0.2038 0.0019  0.0090  0.0019  162 PRO A C   
1226 O O   . PRO A 176 ? 0.2279 0.2556 0.2188 0.0025  0.0082  0.0001  162 PRO A O   
1227 C CB  . PRO A 176 ? 0.2163 0.2316 0.1941 0.0004  0.0047  0.0060  162 PRO A CB  
1228 C CG  . PRO A 176 ? 0.2217 0.2342 0.2004 -0.0023 0.0036  0.0088  162 PRO A CG  
1229 C CD  . PRO A 176 ? 0.2480 0.2642 0.2337 -0.0045 0.0054  0.0089  162 PRO A CD  
1230 N N   . GLY A 177 ? 0.2266 0.2506 0.2059 0.0040  0.0099  0.0005  163 GLY A N   
1231 C CA  . GLY A 177 ? 0.2241 0.2510 0.2063 0.0074  0.0095  -0.0027 163 GLY A CA  
1232 C C   . GLY A 177 ? 0.2333 0.2559 0.2109 0.0100  0.0075  -0.0028 163 GLY A C   
1233 O O   . GLY A 177 ? 0.2091 0.2272 0.1815 0.0090  0.0068  -0.0010 163 GLY A O   
1234 N N   . TYR A 178 ? 0.2345 0.2583 0.2145 0.0133  0.0064  -0.0049 164 TYR A N   
1235 C CA  . TYR A 178 ? 0.2343 0.2540 0.2112 0.0157  0.0044  -0.0045 164 TYR A CA  
1236 C C   . TYR A 178 ? 0.2470 0.2679 0.2253 0.0188  0.0047  -0.0070 164 TYR A C   
1237 O O   . TYR A 178 ? 0.2296 0.2550 0.2126 0.0203  0.0049  -0.0092 164 TYR A O   
1238 C CB  . TYR A 178 ? 0.2512 0.2704 0.2295 0.0170  0.0018  -0.0034 164 TYR A CB  
1239 C CG  . TYR A 178 ? 0.2520 0.2676 0.2277 0.0194  0.0001  -0.0021 164 TYR A CG  
1240 C CD1 . TYR A 178 ? 0.2493 0.2649 0.2259 0.0226  -0.0004 -0.0030 164 TYR A CD1 
1241 C CD2 . TYR A 178 ? 0.2367 0.2490 0.2096 0.0184  -0.0010 0.0002  164 TYR A CD2 
1242 C CE1 . TYR A 178 ? 0.2530 0.2650 0.2275 0.0245  -0.0017 -0.0010 164 TYR A CE1 
1243 C CE2 . TYR A 178 ? 0.2528 0.2623 0.2240 0.0202  -0.0021 0.0018  164 TYR A CE2 
1244 C CZ  . TYR A 178 ? 0.2481 0.2574 0.2200 0.0231  -0.0024 0.0015  164 TYR A CZ  
1245 O OH  . TYR A 178 ? 0.2297 0.2359 0.2002 0.0246  -0.0032 0.0040  164 TYR A OH  
1246 N N   . LEU A 179 ? 0.2275 0.2442 0.2024 0.0197  0.0043  -0.0069 165 LEU A N   
1247 C CA  . LEU A 179 ? 0.2400 0.2566 0.2165 0.0229  0.0040  -0.0092 165 LEU A CA  
1248 C C   . LEU A 179 ? 0.2511 0.2619 0.2257 0.0244  0.0019  -0.0073 165 LEU A C   
1249 O O   . LEU A 179 ? 0.2519 0.2586 0.2232 0.0227  0.0017  -0.0060 165 LEU A O   
1250 C CB  . LEU A 179 ? 0.2251 0.2433 0.2006 0.0225  0.0061  -0.0120 165 LEU A CB  
1251 C CG  . LEU A 179 ? 0.2305 0.2553 0.2082 0.0210  0.0091  -0.0138 165 LEU A CG  
1252 C CD1 . LEU A 179 ? 0.2386 0.2648 0.2135 0.0207  0.0113  -0.0163 165 LEU A CD1 
1253 C CD2 . LEU A 179 ? 0.2237 0.2536 0.2080 0.0233  0.0089  -0.0161 165 LEU A CD2 
1254 N N   . MET A 180 ? 0.2497 0.2601 0.2266 0.0274  0.0002  -0.0068 166 MET A N   
1255 C CA  . MET A 180 ? 0.2662 0.2708 0.2419 0.0288  -0.0014 -0.0046 166 MET A CA  
1256 C C   . MET A 180 ? 0.2712 0.2739 0.2487 0.0307  -0.0016 -0.0073 166 MET A C   
1257 O O   . MET A 180 ? 0.2465 0.2523 0.2271 0.0333  -0.0017 -0.0099 166 MET A O   
1258 C CB  . MET A 180 ? 0.2500 0.2545 0.2263 0.0313  -0.0031 -0.0019 166 MET A CB  
1259 C CG  . MET A 180 ? 0.2883 0.2869 0.2643 0.0328  -0.0043 0.0007  166 MET A CG  
1260 S SD  . MET A 180 ? 0.3128 0.3107 0.2893 0.0370  -0.0063 0.0040  166 MET A SD  
1261 C CE  . MET A 180 ? 0.3042 0.3065 0.2779 0.0363  -0.0063 0.0062  166 MET A CE  
1262 N N   . LEU A 181 ? 0.2529 0.2508 0.2291 0.0298  -0.0019 -0.0072 167 LEU A N   
1263 C CA  . LEU A 181 ? 0.2744 0.2701 0.2528 0.0317  -0.0025 -0.0105 167 LEU A CA  
1264 C C   . LEU A 181 ? 0.2799 0.2688 0.2601 0.0330  -0.0046 -0.0081 167 LEU A C   
1265 O O   . LEU A 181 ? 0.2439 0.2284 0.2234 0.0312  -0.0052 -0.0071 167 LEU A O   
1266 C CB  . LEU A 181 ? 0.2534 0.2496 0.2293 0.0296  -0.0013 -0.0134 167 LEU A CB  
1267 C CG  . LEU A 181 ? 0.2931 0.2879 0.2711 0.0318  -0.0019 -0.0181 167 LEU A CG  
1268 C CD1 . LEU A 181 ? 0.2865 0.2861 0.2681 0.0348  -0.0014 -0.0215 167 LEU A CD1 
1269 C CD2 . LEU A 181 ? 0.2606 0.2567 0.2348 0.0299  -0.0008 -0.0208 167 LEU A CD2 
1270 N N   . PRO A 182 ? 0.2899 0.2777 0.2729 0.0363  -0.0061 -0.0070 168 PRO A N   
1271 C CA  . PRO A 182 ? 0.3071 0.2879 0.2926 0.0376  -0.0080 -0.0044 168 PRO A CA  
1272 C C   . PRO A 182 ? 0.3224 0.2996 0.3107 0.0378  -0.0089 -0.0084 168 PRO A C   
1273 O O   . PRO A 182 ? 0.2981 0.2788 0.2872 0.0389  -0.0084 -0.0137 168 PRO A O   
1274 C CB  . PRO A 182 ? 0.3154 0.2968 0.3032 0.0416  -0.0095 -0.0034 168 PRO A CB  
1275 C CG  . PRO A 182 ? 0.3020 0.2912 0.2880 0.0418  -0.0083 -0.0045 168 PRO A CG  
1276 C CD  . PRO A 182 ? 0.2912 0.2841 0.2760 0.0390  -0.0062 -0.0085 168 PRO A CD  
1277 N N   . ALA A 183 ? 0.3188 0.2893 0.3090 0.0368  -0.0102 -0.0061 169 ALA A N   
1278 C CA  . ALA A 183 ? 0.3457 0.3127 0.3388 0.0366  -0.0114 -0.0103 169 ALA A CA  
1279 C C   . ALA A 183 ? 0.3560 0.3223 0.3537 0.0404  -0.0130 -0.0149 169 ALA A C   
1280 O O   . ALA A 183 ? 0.3508 0.3183 0.3495 0.0410  -0.0133 -0.0210 169 ALA A O   
1281 C CB  . ALA A 183 ? 0.3902 0.3500 0.3862 0.0347  -0.0127 -0.0067 169 ALA A CB  
1282 N N   . ASP A 184 ? 0.3593 0.3239 0.3597 0.0434  -0.0143 -0.0124 170 ASP A N   
1283 C CA  . ASP A 184 ? 0.3642 0.3279 0.3695 0.0474  -0.0163 -0.0169 170 ASP A CA  
1284 C C   . ASP A 184 ? 0.3469 0.3193 0.3509 0.0489  -0.0146 -0.0226 170 ASP A C   
1285 O O   . ASP A 184 ? 0.3522 0.3261 0.3594 0.0511  -0.0153 -0.0290 170 ASP A O   
1286 C CB  . ASP A 184 ? 0.3764 0.3356 0.3848 0.0504  -0.0185 -0.0121 170 ASP A CB  
1287 C CG  . ASP A 184 ? 0.3678 0.3321 0.3719 0.0510  -0.0173 -0.0083 170 ASP A CG  
1288 O OD1 . ASP A 184 ? 0.3471 0.3149 0.3462 0.0479  -0.0150 -0.0058 170 ASP A OD1 
1289 O OD2 . ASP A 184 ? 0.3563 0.3210 0.3624 0.0549  -0.0190 -0.0079 170 ASP A OD2 
1290 N N   . VAL A 185 ? 0.3251 0.3037 0.3249 0.0476  -0.0124 -0.0207 171 VAL A N   
1291 C CA  . VAL A 185 ? 0.2984 0.2857 0.2978 0.0483  -0.0103 -0.0255 171 VAL A CA  
1292 C C   . VAL A 185 ? 0.3189 0.3094 0.3162 0.0465  -0.0084 -0.0304 171 VAL A C   
1293 O O   . VAL A 185 ? 0.3075 0.3037 0.3063 0.0481  -0.0073 -0.0361 171 VAL A O   
1294 C CB  . VAL A 185 ? 0.2946 0.2872 0.2906 0.0467  -0.0085 -0.0221 171 VAL A CB  
1295 C CG1 . VAL A 185 ? 0.2893 0.2910 0.2860 0.0469  -0.0061 -0.0267 171 VAL A CG1 
1296 C CG2 . VAL A 185 ? 0.3070 0.2972 0.3043 0.0493  -0.0107 -0.0176 171 VAL A CG2 
1297 N N   . ALA A 186 ? 0.2972 0.2846 0.2908 0.0431  -0.0080 -0.0284 172 ALA A N   
1298 C CA  . ALA A 186 ? 0.3046 0.2949 0.2949 0.0415  -0.0064 -0.0326 172 ALA A CA  
1299 C C   . ALA A 186 ? 0.3070 0.2963 0.3011 0.0445  -0.0081 -0.0391 172 ALA A C   
1300 O O   . ALA A 186 ? 0.3173 0.3119 0.3089 0.0445  -0.0064 -0.0442 172 ALA A O   
1301 C CB  . ALA A 186 ? 0.2937 0.2800 0.2802 0.0379  -0.0066 -0.0292 172 ALA A CB  
1302 N N   . LYS A 187 ? 0.3232 0.3058 0.3231 0.0470  -0.0114 -0.0392 173 LYS A N   
1303 C CA  . LYS A 187 ? 0.3833 0.3643 0.3880 0.0502  -0.0136 -0.0460 173 LYS A CA  
1304 C C   . LYS A 187 ? 0.3575 0.3431 0.3666 0.0544  -0.0137 -0.0504 173 LYS A C   
1305 O O   . LYS A 187 ? 0.3407 0.3258 0.3545 0.0576  -0.0157 -0.0568 173 LYS A O   
1306 C CB  . LYS A 187 ? 0.4061 0.3769 0.4164 0.0508  -0.0174 -0.0442 173 LYS A CB  
1307 C CG  . LYS A 187 ? 0.4411 0.4074 0.4490 0.0470  -0.0177 -0.0406 173 LYS A CG  
1308 C CD  . LYS A 187 ? 0.5064 0.4655 0.5172 0.0460  -0.0190 -0.0330 173 LYS A CD  
1309 C CE  . LYS A 187 ? 0.6817 0.6322 0.6996 0.0464  -0.0225 -0.0340 173 LYS A CE  
1310 N NZ  . LYS A 187 ? 0.8051 0.7493 0.8242 0.0435  -0.0228 -0.0262 173 LYS A NZ  
1311 N N   . LYS A 188 ? 0.3319 0.3223 0.3405 0.0547  -0.0120 -0.0478 174 LYS A N   
1312 C CA  . LYS A 188 ? 0.3373 0.3323 0.3510 0.0588  -0.0125 -0.0522 174 LYS A CA  
1313 C C   . LYS A 188 ? 0.3388 0.3430 0.3515 0.0595  -0.0097 -0.0596 174 LYS A C   
1314 O O   . LYS A 188 ? 0.3355 0.3447 0.3421 0.0562  -0.0062 -0.0593 174 LYS A O   
1315 C CB  . LYS A 188 ? 0.3289 0.3272 0.3424 0.0589  -0.0117 -0.0478 174 LYS A CB  
1316 C CG  . LYS A 188 ? 0.3547 0.3476 0.3738 0.0630  -0.0156 -0.0462 174 LYS A CG  
1317 C CD  . LYS A 188 ? 0.3306 0.3135 0.3486 0.0616  -0.0178 -0.0393 174 LYS A CD  
1318 C CE  . LYS A 188 ? 0.3546 0.3306 0.3782 0.0657  -0.0219 -0.0375 174 LYS A CE  
1319 N NZ  . LYS A 188 ? 0.3823 0.3504 0.4039 0.0640  -0.0231 -0.0292 174 LYS A NZ  
1320 N N   . ALA A 189 ? 0.3333 0.3398 0.3521 0.0640  -0.0111 -0.0661 175 ALA A N   
1321 C CA  . ALA A 189 ? 0.3640 0.3797 0.3824 0.0652  -0.0085 -0.0740 175 ALA A CA  
1322 C C   . ALA A 189 ? 0.3442 0.3706 0.3593 0.0629  -0.0034 -0.0731 175 ALA A C   
1323 O O   . ALA A 189 ? 0.3458 0.3739 0.3628 0.0626  -0.0030 -0.0695 175 ALA A O   
1324 C CB  . ALA A 189 ? 0.3421 0.3589 0.3689 0.0709  -0.0112 -0.0813 175 ALA A CB  
1325 N N   . ALA A 190 ? 0.3353 0.3689 0.3453 0.0612  0.0004  -0.0763 176 ALA A N   
1326 C CA  . ALA A 190 ? 0.3386 0.3826 0.3461 0.0587  0.0057  -0.0756 176 ALA A CA  
1327 C C   . ALA A 190 ? 0.3517 0.4053 0.3577 0.0601  0.0090  -0.0828 176 ALA A C   
1328 O O   . ALA A 190 ? 0.3605 0.4126 0.3671 0.0631  0.0070  -0.0887 176 ALA A O   
1329 C CB  . ALA A 190 ? 0.3082 0.3503 0.3084 0.0533  0.0077  -0.0681 176 ALA A CB  
1330 N N   . THR A 191 ? 0.3447 0.4087 0.3493 0.0579  0.0143  -0.0825 177 THR A N   
1331 C CA  . THR A 191 ? 0.3411 0.4157 0.3435 0.0589  0.0185  -0.0886 177 THR A CA  
1332 C C   . THR A 191 ? 0.3373 0.4165 0.3307 0.0539  0.0236  -0.0840 177 THR A C   
1333 O O   . THR A 191 ? 0.2796 0.3596 0.2727 0.0500  0.0257  -0.0777 177 THR A O   
1334 C CB  . THR A 191 ? 0.3387 0.4235 0.3495 0.0616  0.0208  -0.0936 177 THR A CB  
1335 O OG1 . THR A 191 ? 0.3608 0.4411 0.3797 0.0669  0.0157  -0.0985 177 THR A OG1 
1336 C CG2 . THR A 191 ? 0.3384 0.4358 0.3468 0.0622  0.0261  -0.0994 177 THR A CG2 
1337 N N   . PRO A 192 ? 0.3547 0.4370 0.3408 0.0540  0.0253  -0.0869 178 PRO A N   
1338 C CA  . PRO A 192 ? 0.3398 0.4270 0.3168 0.0496  0.0302  -0.0823 178 PRO A CA  
1339 C C   . PRO A 192 ? 0.3521 0.4510 0.3321 0.0478  0.0364  -0.0817 178 PRO A C   
1340 O O   . PRO A 192 ? 0.3542 0.4623 0.3391 0.0509  0.0386  -0.0883 178 PRO A O   
1341 C CB  . PRO A 192 ? 0.3462 0.4362 0.3158 0.0519  0.0305  -0.0879 178 PRO A CB  
1342 C CG  . PRO A 192 ? 0.3516 0.4327 0.3256 0.0560  0.0240  -0.0927 178 PRO A CG  
1343 C CD  . PRO A 192 ? 0.3350 0.4155 0.3204 0.0584  0.0222  -0.0943 178 PRO A CD  
1344 N N   . PRO A 193 ? 0.3369 0.4361 0.3146 0.0427  0.0392  -0.0742 179 PRO A N   
1345 C CA  . PRO A 193 ? 0.3341 0.4445 0.3158 0.0404  0.0452  -0.0732 179 PRO A CA  
1346 C C   . PRO A 193 ? 0.3837 0.5042 0.3581 0.0398  0.0512  -0.0749 179 PRO A C   
1347 O O   . PRO A 193 ? 0.3931 0.5108 0.3571 0.0390  0.0510  -0.0732 179 PRO A O   
1348 C CB  . PRO A 193 ? 0.3232 0.4288 0.3044 0.0352  0.0455  -0.0644 179 PRO A CB  
1349 C CG  . PRO A 193 ? 0.3701 0.4640 0.3433 0.0342  0.0412  -0.0604 179 PRO A CG  
1350 C CD  . PRO A 193 ? 0.3260 0.4151 0.2986 0.0390  0.0367  -0.0665 179 PRO A CD  
1351 N N   . VAL A 194 ? 0.3801 0.5133 0.3603 0.0402  0.0564  -0.0784 180 VAL A N   
1352 C CA  . VAL A 194 ? 0.4048 0.5494 0.3783 0.0395  0.0630  -0.0795 180 VAL A CA  
1353 C C   . VAL A 194 ? 0.4045 0.5498 0.3716 0.0332  0.0675  -0.0702 180 VAL A C   
1354 O O   . VAL A 194 ? 0.3806 0.5284 0.3365 0.0321  0.0705  -0.0680 180 VAL A O   
1355 C CB  . VAL A 194 ? 0.3981 0.5568 0.3804 0.0417  0.0677  -0.0861 180 VAL A CB  
1356 C CG1 . VAL A 194 ? 0.4459 0.6158 0.4202 0.0433  0.0731  -0.0901 180 VAL A CG1 
1357 C CG2 . VAL A 194 ? 0.4109 0.5674 0.4034 0.0472  0.0624  -0.0938 180 VAL A CG2 
1358 N N   . ASN A 195 ? 0.3987 0.5417 0.3730 0.0293  0.0678  -0.0646 181 ASN A N   
1359 C CA  . ASN A 195 ? 0.4119 0.5560 0.3832 0.0232  0.0721  -0.0559 181 ASN A CA  
1360 C C   . ASN A 195 ? 0.4056 0.5361 0.3728 0.0207  0.0670  -0.0493 181 ASN A C   
1361 O O   . ASN A 195 ? 0.4250 0.5472 0.3973 0.0223  0.0613  -0.0503 181 ASN A O   
1362 C CB  . ASN A 195 ? 0.4096 0.5617 0.3934 0.0204  0.0761  -0.0549 181 ASN A CB  
1363 C CG  . ASN A 195 ? 0.3892 0.5565 0.3775 0.0221  0.0823  -0.0607 181 ASN A CG  
1364 O OD1 . ASN A 195 ? 0.4336 0.6074 0.4133 0.0233  0.0861  -0.0625 181 ASN A OD1 
1365 N ND2 . ASN A 195 ? 0.4016 0.5752 0.4037 0.0227  0.0831  -0.0642 181 ASN A ND2 
1366 N N   . ALA A 196 ? 0.4133 0.5419 0.3716 0.0166  0.0694  -0.0422 182 ALA A N   
1367 C CA  . ALA A 196 ? 0.4141 0.5309 0.3695 0.0139  0.0650  -0.0357 182 ALA A CA  
1368 C C   . ALA A 196 ? 0.4538 0.5685 0.4205 0.0111  0.0641  -0.0327 182 ALA A C   
1369 O O   . ALA A 196 ? 0.4463 0.5697 0.4222 0.0098  0.0680  -0.0336 182 ALA A O   
1370 C CB  . ALA A 196 ? 0.4173 0.5332 0.3616 0.0102  0.0679  -0.0286 182 ALA A CB  
1371 N N   . LEU A 197 ? 0.4481 0.5519 0.4148 0.0106  0.0585  -0.0298 183 LEU A N   
1372 C CA  . LEU A 197 ? 0.4573 0.5588 0.4331 0.0078  0.0573  -0.0264 183 LEU A CA  
1373 C C   . LEU A 197 ? 0.5156 0.6187 0.4900 0.0022  0.0613  -0.0192 183 LEU A C   
1374 O O   . LEU A 197 ? 0.5284 0.6265 0.4931 0.0004  0.0611  -0.0144 183 LEU A O   
1375 C CB  . LEU A 197 ? 0.4347 0.5248 0.4100 0.0090  0.0505  -0.0253 183 LEU A CB  
1376 C CG  . LEU A 197 ? 0.4165 0.5042 0.4014 0.0076  0.0480  -0.0236 183 LEU A CG  
1377 C CD1 . LEU A 197 ? 0.3703 0.4629 0.3649 0.0111  0.0471  -0.0296 183 LEU A CD1 
1378 C CD2 . LEU A 197 ? 0.3425 0.4191 0.3235 0.0080  0.0423  -0.0209 183 LEU A CD2 
1379 N N   . THR A 198 ? 0.5531 0.6629 0.5378 -0.0006 0.0648  -0.0183 184 THR A N   
1380 C CA  . THR A 198 ? 0.6171 0.7286 0.6026 -0.0062 0.0688  -0.0112 184 THR A CA  
1381 C C   . THR A 198 ? 0.6409 0.7504 0.6386 -0.0088 0.0667  -0.0095 184 THR A C   
1382 O O   . THR A 198 ? 0.6136 0.7257 0.6212 -0.0065 0.0647  -0.0146 184 THR A O   
1383 C CB  . THR A 198 ? 0.6570 0.7810 0.6435 -0.0080 0.0768  -0.0112 184 THR A CB  
1384 O OG1 . THR A 198 ? 0.7226 0.8460 0.7036 -0.0130 0.0807  -0.0030 184 THR A OG1 
1385 C CG2 . THR A 198 ? 0.6601 0.7932 0.6621 -0.0088 0.0795  -0.0147 184 THR A CG2 
1386 N N   . LEU A 199 ? 0.6648 0.7694 0.6618 -0.0133 0.0668  -0.0026 185 LEU A N   
1387 C CA  . LEU A 199 ? 0.6667 0.7702 0.6759 -0.0163 0.0653  -0.0007 185 LEU A CA  
1388 C C   . LEU A 199 ? 0.6990 0.8123 0.7162 -0.0208 0.0723  0.0016  185 LEU A C   
1389 O O   . LEU A 199 ? 0.6902 0.8031 0.7032 -0.0251 0.0760  0.0084  185 LEU A O   
1390 C CB  . LEU A 199 ? 0.7113 0.8041 0.7166 -0.0187 0.0613  0.0051  185 LEU A CB  
1391 C CG  . LEU A 199 ? 0.6627 0.7530 0.6801 -0.0213 0.0585  0.0063  185 LEU A CG  
1392 C CD1 . LEU A 199 ? 0.5031 0.5917 0.5263 -0.0170 0.0529  0.0002  185 LEU A CD1 
1393 C CD2 . LEU A 199 ? 0.5418 0.6231 0.5552 -0.0245 0.0562  0.0130  185 LEU A CD2 
1394 N N   . ARG A 200 ? 0.6455 0.7677 0.6745 -0.0197 0.0740  -0.0038 186 ARG A N   
1395 C CA  . ARG A 200 ? 0.6619 0.7942 0.7010 -0.0241 0.0806  -0.0020 186 ARG A CA  
1396 C C   . ARG A 200 ? 0.6459 0.7736 0.6929 -0.0295 0.0798  0.0040  186 ARG A C   
1397 O O   . ARG A 200 ? 0.6332 0.7545 0.6861 -0.0287 0.0737  0.0026  186 ARG A O   
1398 C CB  . ARG A 200 ? 0.6083 0.7504 0.6602 -0.0216 0.0814  -0.0098 186 ARG A CB  
1399 N N   . HIS A 201 ? 0.6619 0.7928 0.7090 -0.0349 0.0859  0.0109  187 HIS A N   
1400 C CA  . HIS A 201 ? 0.6144 0.7405 0.6694 -0.0405 0.0853  0.0172  187 HIS A CA  
1401 C C   . HIS A 201 ? 0.5870 0.7183 0.6615 -0.0417 0.0842  0.0128  187 HIS A C   
1402 O O   . HIS A 201 ? 0.5746 0.7173 0.6584 -0.0423 0.0891  0.0094  187 HIS A O   
1403 C CB  . HIS A 201 ? 0.5879 0.7171 0.6391 -0.0460 0.0927  0.0258  187 HIS A CB  
1404 N N   . ALA A 202 ? 0.5529 0.6764 0.6337 -0.0417 0.0776  0.0123  188 ALA A N   
1405 C CA  . ALA A 202 ? 0.5144 0.6424 0.6139 -0.0429 0.0758  0.0080  188 ALA A CA  
1406 C C   . ALA A 202 ? 0.4868 0.6190 0.5980 -0.0502 0.0814  0.0139  188 ALA A C   
1407 O O   . ALA A 202 ? 0.4747 0.6026 0.5794 -0.0544 0.0846  0.0223  188 ALA A O   
1408 C CB  . ALA A 202 ? 0.4840 0.6028 0.5864 -0.0406 0.0671  0.0056  188 ALA A CB  
1409 N N   . HIS A 203 ? 0.4645 0.6052 0.5937 -0.0516 0.0824  0.0095  189 HIS A N   
1410 C CA  . HIS A 203 ? 0.4403 0.5857 0.5835 -0.0588 0.0877  0.0145  189 HIS A CA  
1411 C C   . HIS A 203 ? 0.3894 0.5345 0.5516 -0.0596 0.0822  0.0098  189 HIS A C   
1412 O O   . HIS A 203 ? 0.3915 0.5415 0.5608 -0.0551 0.0785  0.0010  189 HIS A O   
1413 C CB  . HIS A 203 ? 0.4821 0.6417 0.6301 -0.0607 0.0967  0.0139  189 HIS A CB  
1414 C CG  . HIS A 203 ? 0.6051 0.7662 0.7351 -0.0602 0.1026  0.0186  189 HIS A CG  
1415 N ND1 . HIS A 203 ? 0.6808 0.8516 0.8054 -0.0562 0.1064  0.0133  189 HIS A ND1 
1416 C CD2 . HIS A 203 ? 0.6066 0.7609 0.7224 -0.0628 0.1050  0.0276  189 HIS A CD2 
1417 C CE1 . HIS A 203 ? 0.7915 0.9617 0.8995 -0.0564 0.1110  0.0185  189 HIS A CE1 
1418 N NE2 . HIS A 203 ? 0.6864 0.8467 0.7885 -0.0603 0.1102  0.0274  189 HIS A NE2 
1419 N N   . ALA A 204 ? 0.3641 0.5034 0.5346 -0.0650 0.0813  0.0155  190 ALA A N   
1420 C CA  . ALA A 204 ? 0.3187 0.4586 0.5091 -0.0664 0.0765  0.0110  190 ALA A CA  
1421 C C   . ALA A 204 ? 0.3097 0.4635 0.5182 -0.0691 0.0819  0.0074  190 ALA A C   
1422 O O   . ALA A 204 ? 0.3158 0.4773 0.5236 -0.0728 0.0907  0.0118  190 ALA A O   
1423 C CB  . ALA A 204 ? 0.2697 0.4001 0.4656 -0.0719 0.0747  0.0182  190 ALA A CB  
1424 N N   . ASP A 205 ? 0.2769 0.4346 0.5016 -0.0671 0.0766  -0.0010 191 ASP A N   
1425 C CA  . ASP A 205 ? 0.2843 0.4543 0.5301 -0.0709 0.0810  -0.0040 191 ASP A CA  
1426 C C   . ASP A 205 ? 0.2694 0.4380 0.5246 -0.0799 0.0866  0.0054  191 ASP A C   
1427 O O   . ASP A 205 ? 0.2638 0.4211 0.5175 -0.0825 0.0830  0.0108  191 ASP A O   
1428 C CB  . ASP A 205 ? 0.2607 0.4335 0.5236 -0.0678 0.0732  -0.0141 191 ASP A CB  
1429 C CG  . ASP A 205 ? 0.2923 0.4790 0.5776 -0.0710 0.0773  -0.0185 191 ASP A CG  
1430 O OD1 . ASP A 205 ? 0.2839 0.4810 0.5698 -0.0672 0.0796  -0.0246 191 ASP A OD1 
1431 O OD2 . ASP A 205 ? 0.2948 0.4823 0.5982 -0.0773 0.0782  -0.0163 191 ASP A OD2 
1432 N N   . SER A 206 ? 0.3498 0.4290 0.4204 -0.0261 0.0534  0.0142  192 SER A N   
1433 C CA  . SER A 206 ? 0.3619 0.4471 0.4278 -0.0274 0.0577  0.0193  192 SER A CA  
1434 C C   . SER A 206 ? 0.3473 0.4262 0.4147 -0.0308 0.0553  0.0267  192 SER A C   
1435 O O   . SER A 206 ? 0.3307 0.4101 0.3920 -0.0322 0.0565  0.0319  192 SER A O   
1436 C CB  . SER A 206 ? 0.3838 0.4819 0.4562 -0.0267 0.0637  0.0176  192 SER A CB  
1437 O OG  . SER A 206 ? 0.4049 0.5034 0.4910 -0.0273 0.0628  0.0171  192 SER A OG  
1438 N N   . ALA A 207 ? 0.3336 0.4068 0.4096 -0.0322 0.0516  0.0273  193 ALA A N   
1439 C CA  . ALA A 207 ? 0.3147 0.3812 0.3919 -0.0354 0.0488  0.0334  193 ALA A CA  
1440 C C   . ALA A 207 ? 0.3106 0.3675 0.3782 -0.0359 0.0450  0.0339  193 ALA A C   
1441 O O   . ALA A 207 ? 0.3111 0.3646 0.3760 -0.0377 0.0443  0.0387  193 ALA A O   
1442 C CB  . ALA A 207 ? 0.3184 0.3815 0.4068 -0.0372 0.0454  0.0338  193 ALA A CB  
1443 N N   . CYS A 208 ? 0.3225 0.3752 0.3860 -0.0342 0.0424  0.0289  194 CYS A N   
1444 C CA  . CYS A 208 ? 0.3064 0.3514 0.3606 -0.0343 0.0396  0.0288  194 CYS A CA  
1445 C C   . CYS A 208 ? 0.2853 0.3335 0.3312 -0.0332 0.0426  0.0307  194 CYS A C   
1446 O O   . CYS A 208 ? 0.2524 0.2955 0.2942 -0.0343 0.0411  0.0339  194 CYS A O   
1447 C CB  . CYS A 208 ? 0.3444 0.3858 0.3966 -0.0329 0.0365  0.0234  194 CYS A CB  
1448 S SG  . CYS A 208 ? 0.4647 0.5016 0.5267 -0.0352 0.0315  0.0224  194 CYS A SG  
1449 N N   . LEU A 209 ? 0.2905 0.3472 0.3341 -0.0311 0.0465  0.0286  195 LEU A N   
1450 C CA  . LEU A 209 ? 0.2886 0.3489 0.3241 -0.0306 0.0490  0.0313  195 LEU A CA  
1451 C C   . LEU A 209 ? 0.2824 0.3444 0.3204 -0.0332 0.0502  0.0387  195 LEU A C   
1452 O O   . LEU A 209 ? 0.2624 0.3215 0.2956 -0.0341 0.0493  0.0428  195 LEU A O   
1453 C CB  . LEU A 209 ? 0.3003 0.3707 0.3328 -0.0283 0.0532  0.0276  195 LEU A CB  
1454 C CG  . LEU A 209 ? 0.2829 0.3570 0.3053 -0.0278 0.0550  0.0295  195 LEU A CG  
1455 C CD1 . LEU A 209 ? 0.2797 0.3452 0.2953 -0.0268 0.0512  0.0280  195 LEU A CD1 
1456 C CD2 . LEU A 209 ? 0.2934 0.3786 0.3132 -0.0259 0.0594  0.0250  195 LEU A CD2 
1457 N N   . LYS A 210 ? 0.2947 0.3610 0.3414 -0.0347 0.0519  0.0408  196 LYS A N   
1458 C CA  . LYS A 210 ? 0.2919 0.3602 0.3425 -0.0375 0.0529  0.0483  196 LYS A CA  
1459 C C   . LYS A 210 ? 0.2883 0.3458 0.3395 -0.0394 0.0482  0.0517  196 LYS A C   
1460 O O   . LYS A 210 ? 0.2952 0.3522 0.3455 -0.0410 0.0480  0.0575  196 LYS A O   
1461 C CB  . LYS A 210 ? 0.3328 0.4070 0.3939 -0.0386 0.0550  0.0491  196 LYS A CB  
1462 C CG  . LYS A 210 ? 0.3824 0.4576 0.4502 -0.0419 0.0551  0.0569  196 LYS A CG  
1463 C CD  . LYS A 210 ? 0.4256 0.5141 0.4956 -0.0428 0.0607  0.0604  196 LYS A CD  
1464 C CE  . LYS A 210 ? 0.4046 0.4948 0.4846 -0.0461 0.0607  0.0676  196 LYS A CE  
1465 N NZ  . LYS A 210 ? 0.4127 0.4929 0.4939 -0.0485 0.0558  0.0732  196 LYS A NZ  
1466 N N   . ALA A 211 ? 0.2785 0.3274 0.3317 -0.0394 0.0443  0.0480  197 ALA A N   
1467 C CA  . ALA A 211 ? 0.2843 0.3233 0.3382 -0.0413 0.0400  0.0499  197 ALA A CA  
1468 C C   . ALA A 211 ? 0.2670 0.3026 0.3132 -0.0403 0.0393  0.0506  197 ALA A C   
1469 O O   . ALA A 211 ? 0.2717 0.3036 0.3197 -0.0419 0.0377  0.0550  197 ALA A O   
1470 C CB  . ALA A 211 ? 0.2611 0.2928 0.3165 -0.0417 0.0361  0.0452  197 ALA A CB  
1471 N N   . PHE A 212 ? 0.2388 0.2755 0.2775 -0.0378 0.0400  0.0463  198 PHE A N   
1472 C CA  . PHE A 212 ? 0.2779 0.3120 0.3099 -0.0368 0.0393  0.0470  198 PHE A CA  
1473 C C   . PHE A 212 ? 0.2679 0.3084 0.2992 -0.0376 0.0416  0.0534  198 PHE A C   
1474 O O   . PHE A 212 ? 0.2612 0.2980 0.2924 -0.0384 0.0398  0.0574  198 PHE A O   
1475 C CB  . PHE A 212 ? 0.2402 0.2752 0.2648 -0.0341 0.0396  0.0413  198 PHE A CB  
1476 C CG  . PHE A 212 ? 0.2538 0.2883 0.2715 -0.0329 0.0395  0.0424  198 PHE A CG  
1477 C CD1 . PHE A 212 ? 0.2307 0.2572 0.2475 -0.0330 0.0364  0.0422  198 PHE A CD1 
1478 C CD2 . PHE A 212 ? 0.2368 0.2794 0.2496 -0.0318 0.0424  0.0439  198 PHE A CD2 
1479 C CE1 . PHE A 212 ? 0.2291 0.2551 0.2411 -0.0319 0.0360  0.0436  198 PHE A CE1 
1480 C CE2 . PHE A 212 ? 0.2399 0.2820 0.2467 -0.0311 0.0417  0.0456  198 PHE A CE2 
1481 C CZ  . PHE A 212 ? 0.2248 0.2585 0.2319 -0.0310 0.0384  0.0457  198 PHE A CZ  
1482 N N   . ARG A 213 ? 0.2830 0.3335 0.3142 -0.0374 0.0456  0.0546  199 ARG A N   
1483 C CA  . ARG A 213 ? 0.2877 0.3459 0.3176 -0.0388 0.0481  0.0612  199 ARG A CA  
1484 C C   . ARG A 213 ? 0.2866 0.3421 0.3240 -0.0419 0.0462  0.0687  199 ARG A C   
1485 O O   . ARG A 213 ? 0.3121 0.3677 0.3487 -0.0431 0.0452  0.0747  199 ARG A O   
1486 C CB  . ARG A 213 ? 0.3194 0.3899 0.3491 -0.0386 0.0530  0.0605  199 ARG A CB  
1487 C CG  . ARG A 213 ? 0.3593 0.4391 0.3872 -0.0408 0.0558  0.0681  199 ARG A CG  
1488 C CD  . ARG A 213 ? 0.3689 0.4612 0.3995 -0.0416 0.0610  0.0682  199 ARG A CD  
1489 N NE  . ARG A 213 ? 0.4390 0.5409 0.4681 -0.0446 0.0634  0.0765  199 ARG A NE  
1490 C CZ  . ARG A 213 ? 0.5155 0.6164 0.5511 -0.0479 0.0618  0.0852  199 ARG A CZ  
1491 N NH1 . ARG A 213 ? 0.4150 0.5054 0.4588 -0.0485 0.0578  0.0863  199 ARG A NH1 
1492 N NH2 . ARG A 213 ? 0.4151 0.5260 0.4487 -0.0509 0.0640  0.0932  199 ARG A NH2 
1493 N N   . ASP A 214 ? 0.2972 0.3501 0.3428 -0.0433 0.0454  0.0687  200 ASP A N   
1494 C CA  . ASP A 214 ? 0.3007 0.3511 0.3545 -0.0463 0.0434  0.0758  200 ASP A CA  
1495 C C   . ASP A 214 ? 0.3027 0.3423 0.3571 -0.0465 0.0387  0.0763  200 ASP A C   
1496 O O   . ASP A 214 ? 0.3139 0.3529 0.3718 -0.0482 0.0372  0.0830  200 ASP A O   
1497 C CB  . ASP A 214 ? 0.3067 0.3563 0.3693 -0.0478 0.0431  0.0753  200 ASP A CB  
1498 C CG  . ASP A 214 ? 0.3472 0.4086 0.4118 -0.0479 0.0480  0.0759  200 ASP A CG  
1499 O OD1 . ASP A 214 ? 0.3404 0.4113 0.4000 -0.0476 0.0518  0.0779  200 ASP A OD1 
1500 O OD2 . ASP A 214 ? 0.3846 0.4463 0.4562 -0.0484 0.0481  0.0742  200 ASP A OD2 
1501 N N   . ALA A 215 ? 0.2899 0.3214 0.3415 -0.0448 0.0364  0.0692  201 ALA A N   
1502 C CA  . ALA A 215 ? 0.3090 0.3309 0.3617 -0.0448 0.0325  0.0684  201 ALA A CA  
1503 C C   . ALA A 215 ? 0.3076 0.3307 0.3555 -0.0436 0.0324  0.0710  201 ALA A C   
1504 O O   . ALA A 215 ? 0.3096 0.3284 0.3622 -0.0446 0.0297  0.0751  201 ALA A O   
1505 C CB  . ALA A 215 ? 0.2927 0.3076 0.3424 -0.0435 0.0306  0.0602  201 ALA A CB  
1506 N N   . ALA A 216 ? 0.2985 0.3272 0.3378 -0.0416 0.0350  0.0686  202 ALA A N   
1507 C CA  . ALA A 216 ? 0.2924 0.3229 0.3267 -0.0408 0.0348  0.0715  202 ALA A CA  
1508 C C   . ALA A 216 ? 0.3066 0.3429 0.3447 -0.0434 0.0351  0.0812  202 ALA A C   
1509 O O   . ALA A 216 ? 0.2889 0.3225 0.3291 -0.0440 0.0325  0.0859  202 ALA A O   
1510 C CB  . ALA A 216 ? 0.2800 0.3165 0.3045 -0.0384 0.0376  0.0672  202 ALA A CB  
1511 N N   . GLU A 217 ? 0.2987 0.3433 0.3387 -0.0451 0.0382  0.0845  203 GLU A N   
1512 C CA  . GLU A 217 ? 0.3164 0.3678 0.3601 -0.0482 0.0387  0.0944  203 GLU A CA  
1513 C C   . GLU A 217 ? 0.3464 0.3901 0.4009 -0.0504 0.0342  0.0999  203 GLU A C   
1514 O O   . GLU A 217 ? 0.3523 0.3968 0.4097 -0.0522 0.0320  0.1076  203 GLU A O   
1515 C CB  . GLU A 217 ? 0.3207 0.3825 0.3656 -0.0498 0.0431  0.0963  203 GLU A CB  
1516 C CG  . GLU A 217 ? 0.3836 0.4521 0.4329 -0.0535 0.0431  0.1071  203 GLU A CG  
1517 C CD  . GLU A 217 ? 0.3877 0.4691 0.4369 -0.0553 0.0482  0.1098  203 GLU A CD  
1518 O OE1 . GLU A 217 ? 0.5117 0.5953 0.5612 -0.0537 0.0512  0.1033  203 GLU A OE1 
1519 O OE2 . GLU A 217 ? 0.4348 0.5248 0.4835 -0.0583 0.0491  0.1185  203 GLU A OE2 
1520 N N   . ASN A 218 ? 0.3366 0.3729 0.3977 -0.0505 0.0325  0.0962  204 ASN A N   
1521 C CA  . ASN A 218 ? 0.3517 0.3803 0.4239 -0.0525 0.0280  0.1003  204 ASN A CA  
1522 C C   . ASN A 218 ? 0.3828 0.4036 0.4560 -0.0513 0.0242  0.0996  204 ASN A C   
1523 O O   . ASN A 218 ? 0.4052 0.4231 0.4869 -0.0531 0.0207  0.1062  204 ASN A O   
1524 C CB  . ASN A 218 ? 0.3989 0.4209 0.4764 -0.0527 0.0268  0.0948  204 ASN A CB  
1525 C CG  . ASN A 218 ? 0.4945 0.5107 0.5845 -0.0554 0.0227  0.0997  204 ASN A CG  
1526 O OD1 . ASN A 218 ? 0.5452 0.5514 0.6396 -0.0549 0.0190  0.0955  204 ASN A OD1 
1527 N ND2 . ASN A 218 ? 0.5036 0.5265 0.5998 -0.0584 0.0235  0.1084  204 ASN A ND2 
1528 N N   . ARG A 219 ? 0.3701 0.3876 0.4353 -0.0482 0.0246  0.0919  205 ARG A N   
1529 C CA  . ARG A 219 ? 0.3682 0.3793 0.4345 -0.0468 0.0214  0.0911  205 ARG A CA  
1530 C C   . ARG A 219 ? 0.3511 0.3686 0.4153 -0.0476 0.0212  0.0991  205 ARG A C   
1531 O O   . ARG A 219 ? 0.3736 0.3876 0.4457 -0.0488 0.0174  0.1048  205 ARG A O   
1532 C CB  . ARG A 219 ? 0.3689 0.3761 0.4272 -0.0436 0.0222  0.0811  205 ARG A CB  
1533 C CG  . ARG A 219 ? 0.3623 0.3635 0.4217 -0.0418 0.0195  0.0790  205 ARG A CG  
1534 C CD  . ARG A 219 ? 0.4061 0.3994 0.4781 -0.0430 0.0153  0.0807  205 ARG A CD  
1535 N NE  . ARG A 219 ? 0.4093 0.3975 0.4844 -0.0413 0.0126  0.0792  205 ARG A NE  
1536 C CZ  . ARG A 219 ? 0.4440 0.4239 0.5294 -0.0412 0.0091  0.0767  205 ARG A CZ  
1537 N NH1 . ARG A 219 ? 0.4018 0.3773 0.4951 -0.0428 0.0076  0.0754  205 ARG A NH1 
1538 N NH2 . ARG A 219 ? 0.4204 0.3966 0.5091 -0.0393 0.0071  0.0751  205 ARG A NH2 
1539 N N   . LEU A 220 ? 0.3416 0.3687 0.3958 -0.0473 0.0251  0.1000  206 LEU A N   
1540 C CA  . LEU A 220 ? 0.3428 0.3765 0.3931 -0.0484 0.0249  0.1073  206 LEU A CA  
1541 C C   . LEU A 220 ? 0.3386 0.3771 0.3968 -0.0526 0.0234  0.1189  206 LEU A C   
1542 O O   . LEU A 220 ? 0.3450 0.3846 0.4057 -0.0541 0.0204  0.1264  206 LEU A O   
1543 C CB  . LEU A 220 ? 0.3195 0.3631 0.3571 -0.0473 0.0295  0.1045  206 LEU A CB  
1544 C CG  . LEU A 220 ? 0.3081 0.3473 0.3381 -0.0436 0.0296  0.0953  206 LEU A CG  
1545 C CD1 . LEU A 220 ? 0.2939 0.3416 0.3129 -0.0422 0.0341  0.0908  206 LEU A CD1 
1546 C CD2 . LEU A 220 ? 0.2945 0.3304 0.3245 -0.0431 0.0260  0.0984  206 LEU A CD2 
1547 N N   . ALA A 221 ? 0.3394 0.3809 0.4024 -0.0546 0.0251  0.1210  207 ALA A N   
1548 C CA  . ALA A 221 ? 0.3493 0.3958 0.4205 -0.0589 0.0236  0.1326  207 ALA A CA  
1549 C C   . ALA A 221 ? 0.3622 0.3990 0.4466 -0.0601 0.0172  0.1375  207 ALA A C   
1550 O O   . ALA A 221 ? 0.3323 0.3729 0.4234 -0.0637 0.0147  0.1485  207 ALA A O   
1551 C CB  . ALA A 221 ? 0.3115 0.3625 0.3867 -0.0607 0.0266  0.1333  207 ALA A CB  
1552 N N   . MET A 222 ? 0.3920 0.4168 0.4809 -0.0574 0.0145  0.1295  208 MET A N   
1553 C CA  . MET A 222 ? 0.3925 0.4080 0.4951 -0.0581 0.0084  0.1327  208 MET A CA  
1554 C C   . MET A 222 ? 0.4053 0.4157 0.5072 -0.0557 0.0056  0.1304  208 MET A C   
1555 O O   . MET A 222 ? 0.4303 0.4323 0.5443 -0.0556 0.0006  0.1314  208 MET A O   
1556 C CB  . MET A 222 ? 0.4182 0.4240 0.5291 -0.0573 0.0068  0.1257  208 MET A CB  
1557 C CG  . MET A 222 ? 0.5278 0.5271 0.6320 -0.0535 0.0083  0.1126  208 MET A CG  
1558 S SD  . MET A 222 ? 0.7562 0.7501 0.8641 -0.0538 0.0087  0.1052  208 MET A SD  
1559 C CE  . MET A 222 ? 0.5874 0.5794 0.7122 -0.0579 0.0044  0.1149  208 MET A CE  
1560 N N   . SER A 223 ? 0.3794 0.3950 0.4684 -0.0538 0.0085  0.1278  209 SER A N   
1561 C CA  . SER A 223 ? 0.3957 0.4069 0.4837 -0.0514 0.0061  0.1253  209 SER A CA  
1562 C C   . SER A 223 ? 0.4172 0.4330 0.5090 -0.0542 0.0026  0.1373  209 SER A C   
1563 O O   . SER A 223 ? 0.4009 0.4275 0.4845 -0.0566 0.0048  0.1441  209 SER A O   
1564 C CB  . SER A 223 ? 0.3828 0.3971 0.4558 -0.0483 0.0103  0.1170  209 SER A CB  
1565 O OG  . SER A 223 ? 0.4142 0.4241 0.4865 -0.0458 0.0080  0.1140  209 SER A OG  
1566 N N   . LYS A 224 ? 0.4247 0.4327 0.5291 -0.0540 -0.0031 0.1398  210 LYS A N   
1567 C CA  . LYS A 224 ? 0.4453 0.4568 0.5547 -0.0567 -0.0074 0.1515  210 LYS A CA  
1568 C C   . LYS A 224 ? 0.4425 0.4589 0.5395 -0.0552 -0.0063 0.1508  210 LYS A C   
1569 O O   . LYS A 224 ? 0.4587 0.4849 0.5490 -0.0583 -0.0061 0.1598  210 LYS A O   
1570 C CB  . LYS A 224 ? 0.4833 0.4843 0.6115 -0.0564 -0.0142 0.1534  210 LYS A CB  
1571 C CG  . LYS A 224 ? 0.5779 0.5767 0.7212 -0.0599 -0.0176 0.1607  210 LYS A CG  
1572 C CD  . LYS A 224 ? 0.6867 0.6897 0.8389 -0.0630 -0.0235 0.1732  210 LYS A CD  
1573 C CE  . LYS A 224 ? 0.7600 0.7715 0.9129 -0.0661 -0.0235 0.1797  210 LYS A CE  
1574 N NZ  . LYS A 224 ? 0.7494 0.7649 0.9123 -0.0684 -0.0302 0.1896  210 LYS A NZ  
1575 N N   . ARG A 225 ? 0.4296 0.4399 0.5231 -0.0509 -0.0055 0.1403  211 ARG A N   
1576 C CA  . ARG A 225 ? 0.4384 0.4534 0.5197 -0.0494 -0.0042 0.1388  211 ARG A CA  
1577 C C   . ARG A 225 ? 0.4253 0.4384 0.4959 -0.0453 0.0006  0.1256  211 ARG A C   
1578 O O   . ARG A 225 ? 0.3822 0.3867 0.4581 -0.0426 0.0005  0.1168  211 ARG A O   
1579 C CB  . ARG A 225 ? 0.4657 0.4761 0.5557 -0.0488 -0.0099 0.1426  211 ARG A CB  
1580 C CG  . ARG A 225 ? 0.4787 0.4770 0.5838 -0.0459 -0.0135 0.1366  211 ARG A CG  
1581 C CD  . ARG A 225 ? 0.5147 0.5109 0.6257 -0.0450 -0.0183 0.1399  211 ARG A CD  
1582 N NE  . ARG A 225 ? 0.6909 0.6947 0.7864 -0.0448 -0.0163 0.1407  211 ARG A NE  
1583 C CZ  . ARG A 225 ? 0.6058 0.6079 0.6933 -0.0411 -0.0140 0.1315  211 ARG A CZ  
1584 N NH1 . ARG A 225 ? 0.4572 0.4510 0.5508 -0.0374 -0.0134 0.1211  211 ARG A NH1 
1585 N NH2 . ARG A 225 ? 0.5615 0.5712 0.6344 -0.0413 -0.0121 0.1326  211 ARG A NH2 
1586 N N   . THR A 226 ? 0.4132 0.4348 0.4689 -0.0453 0.0047  0.1243  212 THR A N   
1587 C CA  . THR A 226 ? 0.3540 0.3754 0.3991 -0.0420 0.0092  0.1131  212 THR A CA  
1588 C C   . THR A 226 ? 0.3278 0.3510 0.3642 -0.0400 0.0089  0.1106  212 THR A C   
1589 O O   . THR A 226 ? 0.3340 0.3639 0.3657 -0.0419 0.0076  0.1179  212 THR A O   
1590 C CB  . THR A 226 ? 0.3600 0.3900 0.3963 -0.0434 0.0141  0.1129  212 THR A CB  
1591 O OG1 . THR A 226 ? 0.3690 0.3965 0.4141 -0.0451 0.0142  0.1145  212 THR A OG1 
1592 C CG2 . THR A 226 ? 0.3298 0.3604 0.3554 -0.0402 0.0182  0.1020  212 THR A CG2 
1593 N N   . ALA A 227 ? 0.3328 0.3503 0.3669 -0.0364 0.0099  0.1006  213 ALA A N   
1594 C CA  . ALA A 227 ? 0.3317 0.3503 0.3582 -0.0342 0.0096  0.0974  213 ALA A CA  
1595 C C   . ALA A 227 ? 0.3348 0.3555 0.3502 -0.0320 0.0139  0.0881  213 ALA A C   
1596 O O   . ALA A 227 ? 0.3019 0.3205 0.3178 -0.0315 0.0165  0.0827  213 ALA A O   
1597 C CB  . ALA A 227 ? 0.3257 0.3357 0.3615 -0.0320 0.0059  0.0947  213 ALA A CB  
1598 N N   . LEU A 228 ? 0.3139 0.3386 0.3198 -0.0308 0.0144  0.0864  214 LEU A N   
1599 C CA  . LEU A 228 ? 0.3236 0.3508 0.3195 -0.0287 0.0178  0.0781  214 LEU A CA  
1600 C C   . LEU A 228 ? 0.3306 0.3530 0.3256 -0.0258 0.0163  0.0722  214 LEU A C   
1601 O O   . LEU A 228 ? 0.3072 0.3302 0.3016 -0.0257 0.0136  0.0756  214 LEU A O   
1602 C CB  . LEU A 228 ? 0.3119 0.3495 0.2970 -0.0301 0.0201  0.0807  214 LEU A CB  
1603 C CG  . LEU A 228 ? 0.3168 0.3579 0.2921 -0.0280 0.0232  0.0725  214 LEU A CG  
1604 C CD1 . LEU A 228 ? 0.3023 0.3405 0.2798 -0.0270 0.0259  0.0661  214 LEU A CD1 
1605 C CD2 . LEU A 228 ? 0.3410 0.3933 0.3070 -0.0299 0.0253  0.0757  214 LEU A CD2 
1606 N N   . LEU A 229 ? 0.2914 0.3092 0.2865 -0.0238 0.0179  0.0638  215 LEU A N   
1607 C CA  . LEU A 229 ? 0.3046 0.3186 0.2983 -0.0212 0.0170  0.0577  215 LEU A CA  
1608 C C   . LEU A 229 ? 0.3026 0.3195 0.2875 -0.0200 0.0197  0.0510  215 LEU A C   
1609 O O   . LEU A 229 ? 0.3010 0.3162 0.2865 -0.0200 0.0216  0.0467  215 LEU A O   
1610 C CB  . LEU A 229 ? 0.2795 0.2855 0.2826 -0.0203 0.0160  0.0538  215 LEU A CB  
1611 C CG  . LEU A 229 ? 0.2983 0.3009 0.3016 -0.0180 0.0152  0.0480  215 LEU A CG  
1612 C CD1 . LEU A 229 ? 0.2597 0.2629 0.2650 -0.0173 0.0122  0.0523  215 LEU A CD1 
1613 C CD2 . LEU A 229 ? 0.2796 0.2759 0.2910 -0.0175 0.0154  0.0428  215 LEU A CD2 
1614 N N   . ALA A 230 ? 0.2846 0.3057 0.2619 -0.0191 0.0194  0.0503  216 ALA A N   
1615 C CA  . ALA A 230 ? 0.2985 0.3223 0.2685 -0.0178 0.0213  0.0440  216 ALA A CA  
1616 C C   . ALA A 230 ? 0.2899 0.3106 0.2589 -0.0157 0.0197  0.0393  216 ALA A C   
1617 O O   . ALA A 230 ? 0.2996 0.3190 0.2704 -0.0152 0.0172  0.0419  216 ALA A O   
1618 C CB  . ALA A 230 ? 0.2853 0.3176 0.2471 -0.0185 0.0226  0.0459  216 ALA A CB  
1619 N N   . ASP A 231 ? 0.2738 0.2935 0.2406 -0.0146 0.0207  0.0328  217 ASP A N   
1620 C CA  . ASP A 231 ? 0.2553 0.2727 0.2213 -0.0130 0.0191  0.0287  217 ASP A CA  
1621 C C   . ASP A 231 ? 0.2541 0.2740 0.2148 -0.0121 0.0198  0.0233  217 ASP A C   
1622 O O   . ASP A 231 ? 0.2615 0.2861 0.2184 -0.0124 0.0214  0.0229  217 ASP A O   
1623 C CB  . ASP A 231 ? 0.2663 0.2776 0.2392 -0.0128 0.0186  0.0265  217 ASP A CB  
1624 C CG  . ASP A 231 ? 0.2653 0.2749 0.2393 -0.0113 0.0165  0.0254  217 ASP A CG  
1625 O OD1 . ASP A 231 ? 0.2676 0.2775 0.2436 -0.0111 0.0146  0.0296  217 ASP A OD1 
1626 O OD2 . ASP A 231 ? 0.2535 0.2620 0.2267 -0.0107 0.0165  0.0206  217 ASP A OD2 
1627 N N   . PHE A 232 ? 0.2463 0.2635 0.2076 -0.0110 0.0185  0.0193  218 PHE A N   
1628 C CA  . PHE A 232 ? 0.2553 0.2749 0.2122 -0.0099 0.0176  0.0153  218 PHE A CA  
1629 C C   . PHE A 232 ? 0.2635 0.2856 0.2190 -0.0101 0.0192  0.0120  218 PHE A C   
1630 O O   . PHE A 232 ? 0.2615 0.2870 0.2134 -0.0092 0.0187  0.0093  218 PHE A O   
1631 C CB  . PHE A 232 ? 0.2441 0.2605 0.2032 -0.0092 0.0158  0.0124  218 PHE A CB  
1632 C CG  . PHE A 232 ? 0.2466 0.2602 0.2089 -0.0102 0.0165  0.0093  218 PHE A CG  
1633 C CD1 . PHE A 232 ? 0.2426 0.2529 0.2091 -0.0114 0.0176  0.0102  218 PHE A CD1 
1634 C CD2 . PHE A 232 ? 0.2642 0.2786 0.2254 -0.0102 0.0156  0.0055  218 PHE A CD2 
1635 C CE1 . PHE A 232 ? 0.2663 0.2747 0.2349 -0.0127 0.0181  0.0074  218 PHE A CE1 
1636 C CE2 . PHE A 232 ? 0.2724 0.2847 0.2363 -0.0117 0.0158  0.0035  218 PHE A CE2 
1637 C CZ  . PHE A 232 ? 0.2675 0.2770 0.2344 -0.0131 0.0171  0.0044  218 PHE A CZ  
1638 N N   . LEU A 233 ? 0.2612 0.2815 0.2202 -0.0114 0.0207  0.0118  219 LEU A N   
1639 C CA  . LEU A 233 ? 0.2629 0.2858 0.2220 -0.0115 0.0219  0.0088  219 LEU A CA  
1640 C C   . LEU A 233 ? 0.2687 0.2978 0.2242 -0.0111 0.0237  0.0097  219 LEU A C   
1641 O O   . LEU A 233 ? 0.2650 0.2974 0.2199 -0.0105 0.0243  0.0059  219 LEU A O   
1642 C CB  . LEU A 233 ? 0.2541 0.2742 0.2178 -0.0132 0.0229  0.0090  219 LEU A CB  
1643 C CG  . LEU A 233 ? 0.2881 0.3036 0.2542 -0.0138 0.0212  0.0067  219 LEU A CG  
1644 C CD1 . LEU A 233 ? 0.2956 0.3078 0.2656 -0.0159 0.0219  0.0073  219 LEU A CD1 
1645 C CD2 . LEU A 233 ? 0.2822 0.2987 0.2481 -0.0134 0.0194  0.0028  219 LEU A CD2 
1646 N N   . VAL A 234 ? 0.2433 0.2744 0.1967 -0.0118 0.0244  0.0146  220 VAL A N   
1647 C CA  . VAL A 234 ? 0.2690 0.3073 0.2175 -0.0119 0.0261  0.0158  220 VAL A CA  
1648 C C   . VAL A 234 ? 0.2867 0.3282 0.2302 -0.0103 0.0248  0.0117  220 VAL A C   
1649 O O   . VAL A 234 ? 0.2910 0.3381 0.2319 -0.0097 0.0264  0.0081  220 VAL A O   
1650 C CB  . VAL A 234 ? 0.2729 0.3127 0.2204 -0.0133 0.0262  0.0229  220 VAL A CB  
1651 C CG1 . VAL A 234 ? 0.2559 0.3040 0.1963 -0.0138 0.0272  0.0244  220 VAL A CG1 
1652 C CG2 . VAL A 234 ? 0.2605 0.2984 0.2135 -0.0150 0.0277  0.0266  220 VAL A CG2 
1653 N N   . LEU A 235 ? 0.2645 0.3026 0.2072 -0.0094 0.0218  0.0116  221 LEU A N   
1654 C CA  . LEU A 235 ? 0.2625 0.3031 0.2008 -0.0080 0.0200  0.0078  221 LEU A CA  
1655 C C   . LEU A 235 ? 0.2681 0.3084 0.2088 -0.0068 0.0197  0.0012  221 LEU A C   
1656 O O   . LEU A 235 ? 0.2571 0.3021 0.1950 -0.0058 0.0198  -0.0031 221 LEU A O   
1657 C CB  . LEU A 235 ? 0.2603 0.2969 0.1987 -0.0075 0.0166  0.0094  221 LEU A CB  
1658 C CG  . LEU A 235 ? 0.2662 0.3033 0.2030 -0.0085 0.0158  0.0159  221 LEU A CG  
1659 C CD1 . LEU A 235 ? 0.2582 0.2902 0.1982 -0.0077 0.0128  0.0168  221 LEU A CD1 
1660 C CD2 . LEU A 235 ? 0.2529 0.2969 0.1821 -0.0090 0.0157  0.0173  221 LEU A CD2 
1661 N N   . ARG A 236 ? 0.2639 0.2989 0.2103 -0.0070 0.0190  0.0001  222 ARG A N   
1662 C CA  . ARG A 236 ? 0.2887 0.3228 0.2387 -0.0062 0.0175  -0.0052 222 ARG A CA  
1663 C C   . ARG A 236 ? 0.2947 0.3332 0.2464 -0.0059 0.0198  -0.0085 222 ARG A C   
1664 O O   . ARG A 236 ? 0.2817 0.3219 0.2354 -0.0046 0.0185  -0.0138 222 ARG A O   
1665 C CB  . ARG A 236 ? 0.2701 0.2985 0.2252 -0.0073 0.0162  -0.0046 222 ARG A CB  
1666 C CG  . ARG A 236 ? 0.2551 0.2798 0.2096 -0.0076 0.0149  -0.0015 222 ARG A CG  
1667 C CD  . ARG A 236 ? 0.2505 0.2754 0.2029 -0.0063 0.0119  -0.0033 222 ARG A CD  
1668 N NE  . ARG A 236 ? 0.2584 0.2797 0.2127 -0.0067 0.0103  -0.0016 222 ARG A NE  
1669 C CZ  . ARG A 236 ? 0.2573 0.2783 0.2098 -0.0062 0.0095  0.0009  222 ARG A CZ  
1670 N NH1 . ARG A 236 ? 0.2039 0.2281 0.1521 -0.0055 0.0095  0.0024  222 ARG A NH1 
1671 N NH2 . ARG A 236 ? 0.2616 0.2797 0.2171 -0.0066 0.0086  0.0020  222 ARG A NH2 
1672 N N   . HIS A 237 ? 0.2801 0.3206 0.2323 -0.0070 0.0230  -0.0057 223 HIS A N   
1673 C CA  . HIS A 237 ? 0.3149 0.3599 0.2699 -0.0069 0.0256  -0.0085 223 HIS A CA  
1674 C C   . HIS A 237 ? 0.3178 0.3709 0.2673 -0.0065 0.0283  -0.0094 223 HIS A C   
1675 O O   . HIS A 237 ? 0.3348 0.3932 0.2862 -0.0067 0.0315  -0.0107 223 HIS A O   
1676 C CB  . HIS A 237 ? 0.3157 0.3586 0.2751 -0.0087 0.0274  -0.0050 223 HIS A CB  
1677 C CG  . HIS A 237 ? 0.3265 0.3630 0.2916 -0.0095 0.0250  -0.0054 223 HIS A CG  
1678 N ND1 . HIS A 237 ? 0.3505 0.3868 0.3220 -0.0097 0.0246  -0.0082 223 HIS A ND1 
1679 C CD2 . HIS A 237 ? 0.3291 0.3598 0.2943 -0.0104 0.0228  -0.0033 223 HIS A CD2 
1680 C CE1 . HIS A 237 ? 0.3187 0.3494 0.2934 -0.0110 0.0220  -0.0074 223 HIS A CE1 
1681 N NE2 . HIS A 237 ? 0.3052 0.3327 0.2758 -0.0115 0.0212  -0.0047 223 HIS A NE2 
1682 N N   . GLY A 238 ? 0.3154 0.3704 0.2582 -0.0061 0.0272  -0.0086 224 GLY A N   
1683 C CA  . GLY A 238 ? 0.3082 0.3718 0.2446 -0.0059 0.0293  -0.0103 224 GLY A CA  
1684 C C   . GLY A 238 ? 0.3117 0.3806 0.2445 -0.0080 0.0328  -0.0046 224 GLY A C   
1685 O O   . GLY A 238 ? 0.3345 0.4122 0.2635 -0.0084 0.0358  -0.0066 224 GLY A O   
1686 N N   . LEU A 239 ? 0.3128 0.3772 0.2472 -0.0096 0.0324  0.0025  225 LEU A N   
1687 C CA  . LEU A 239 ? 0.3111 0.3799 0.2443 -0.0120 0.0352  0.0087  225 LEU A CA  
1688 C C   . LEU A 239 ? 0.3145 0.3842 0.2422 -0.0136 0.0336  0.0157  225 LEU A C   
1689 O O   . LEU A 239 ? 0.2883 0.3599 0.2165 -0.0158 0.0349  0.0224  225 LEU A O   
1690 C CB  . LEU A 239 ? 0.3042 0.3674 0.2451 -0.0128 0.0359  0.0116  225 LEU A CB  
1691 C CG  . LEU A 239 ? 0.3180 0.3817 0.2649 -0.0119 0.0375  0.0060  225 LEU A CG  
1692 C CD1 . LEU A 239 ? 0.3397 0.3960 0.2941 -0.0127 0.0367  0.0078  225 LEU A CD1 
1693 C CD2 . LEU A 239 ? 0.3606 0.4341 0.3065 -0.0126 0.0419  0.0054  225 LEU A CD2 
1694 N N   . LYS A 240 ? 0.3278 0.3962 0.2512 -0.0126 0.0305  0.0145  226 LYS A N   
1695 C CA  . LYS A 240 ? 0.3465 0.4163 0.2651 -0.0142 0.0284  0.0212  226 LYS A CA  
1696 C C   . LYS A 240 ? 0.3644 0.4444 0.2767 -0.0169 0.0311  0.0253  226 LYS A C   
1697 O O   . LYS A 240 ? 0.3430 0.4238 0.2558 -0.0193 0.0307  0.0337  226 LYS A O   
1698 C CB  . LYS A 240 ? 0.3605 0.4290 0.2748 -0.0128 0.0249  0.0180  226 LYS A CB  
1699 C CG  . LYS A 240 ? 0.3677 0.4373 0.2777 -0.0145 0.0219  0.0249  226 LYS A CG  
1700 C CD  . LYS A 240 ? 0.3940 0.4623 0.3004 -0.0130 0.0182  0.0215  226 LYS A CD  
1701 C CE  . LYS A 240 ? 0.4478 0.5186 0.3494 -0.0151 0.0151  0.0288  226 LYS A CE  
1702 N NZ  . LYS A 240 ? 0.4384 0.5067 0.3379 -0.0139 0.0107  0.0269  226 LYS A NZ  
1703 N N   . HIS A 241 ? 0.3976 0.4861 0.3046 -0.0166 0.0338  0.0195  227 HIS A N   
1704 C CA  . HIS A 241 ? 0.4115 0.5114 0.3115 -0.0194 0.0367  0.0232  227 HIS A CA  
1705 C C   . HIS A 241 ? 0.3785 0.4803 0.2833 -0.0216 0.0398  0.0289  227 HIS A C   
1706 O O   . HIS A 241 ? 0.3454 0.4534 0.2468 -0.0249 0.0405  0.0368  227 HIS A O   
1707 C CB  . HIS A 241 ? 0.4935 0.6026 0.3877 -0.0185 0.0396  0.0143  227 HIS A CB  
1708 C CG  . HIS A 241 ? 0.7036 0.8116 0.5929 -0.0166 0.0363  0.0084  227 HIS A CG  
1709 N ND1 . HIS A 241 ? 0.7004 0.8054 0.5854 -0.0175 0.0318  0.0132  227 HIS A ND1 
1710 C CD2 . HIS A 241 ? 0.8777 0.9873 0.7665 -0.0140 0.0366  -0.0019 227 HIS A CD2 
1711 C CE1 . HIS A 241 ? 0.7393 0.8441 0.6210 -0.0155 0.0295  0.0062  227 HIS A CE1 
1712 N NE2 . HIS A 241 ? 0.8285 0.9359 0.7125 -0.0134 0.0323  -0.0031 227 HIS A NE2 
1713 N N   . ALA A 242 ? 0.3636 0.4603 0.2768 -0.0200 0.0414  0.0256  228 ALA A N   
1714 C CA  . ALA A 242 ? 0.3330 0.4306 0.2519 -0.0219 0.0440  0.0309  228 ALA A CA  
1715 C C   . ALA A 242 ? 0.3231 0.4149 0.2453 -0.0240 0.0409  0.0406  228 ALA A C   
1716 O O   . ALA A 242 ? 0.3302 0.4267 0.2528 -0.0270 0.0421  0.0482  228 ALA A O   
1717 C CB  . ALA A 242 ? 0.3304 0.4224 0.2580 -0.0198 0.0452  0.0253  228 ALA A CB  
1718 N N   . LEU A 243 ? 0.3130 0.3948 0.2380 -0.0224 0.0368  0.0406  229 LEU A N   
1719 C CA  . LEU A 243 ? 0.3082 0.3840 0.2380 -0.0239 0.0337  0.0488  229 LEU A CA  
1720 C C   . LEU A 243 ? 0.3219 0.4034 0.2461 -0.0266 0.0317  0.0566  229 LEU A C   
1721 O O   . LEU A 243 ? 0.3157 0.3966 0.2440 -0.0292 0.0303  0.0653  229 LEU A O   
1722 C CB  . LEU A 243 ? 0.2655 0.3304 0.2003 -0.0215 0.0303  0.0458  229 LEU A CB  
1723 C CG  . LEU A 243 ? 0.2966 0.3538 0.2401 -0.0206 0.0309  0.0437  229 LEU A CG  
1724 C CD1 . LEU A 243 ? 0.2527 0.3066 0.2030 -0.0227 0.0298  0.0514  229 LEU A CD1 
1725 C CD2 . LEU A 243 ? 0.2408 0.3016 0.1849 -0.0202 0.0346  0.0386  229 LEU A CD2 
1726 N N   . GLN A 244 ? 0.3238 0.4106 0.2392 -0.0263 0.0310  0.0538  230 GLN A N   
1727 C CA  . GLN A 244 ? 0.3482 0.4416 0.2570 -0.0294 0.0289  0.0613  230 GLN A CA  
1728 C C   . GLN A 244 ? 0.3388 0.4433 0.2441 -0.0331 0.0325  0.0665  230 GLN A C   
1729 O O   . GLN A 244 ? 0.3399 0.4475 0.2453 -0.0367 0.0306  0.0766  230 GLN A O   
1730 C CB  . GLN A 244 ? 0.3658 0.4629 0.2652 -0.0284 0.0274  0.0564  230 GLN A CB  
1731 C CG  . GLN A 244 ? 0.3951 0.4823 0.2980 -0.0248 0.0242  0.0508  230 GLN A CG  
1732 C CD  . GLN A 244 ? 0.4944 0.5851 0.3888 -0.0240 0.0223  0.0461  230 GLN A CD  
1733 O OE1 . GLN A 244 ? 0.4921 0.5912 0.3790 -0.0241 0.0251  0.0407  230 GLN A OE1 
1734 N NE2 . GLN A 244 ? 0.4234 0.5078 0.3194 -0.0230 0.0176  0.0477  230 GLN A NE2 
1735 N N   . LYS A 245 ? 0.3557 0.4668 0.2583 -0.0324 0.0375  0.0598  231 LYS A N   
1736 C CA  . LYS A 245 ? 0.3570 0.4797 0.2566 -0.0359 0.0417  0.0640  231 LYS A CA  
1737 C C   . LYS A 245 ? 0.3697 0.4887 0.2792 -0.0378 0.0417  0.0719  231 LYS A C   
1738 O O   . LYS A 245 ? 0.3527 0.4792 0.2612 -0.0419 0.0424  0.0808  231 LYS A O   
1739 C CB  . LYS A 245 ? 0.3667 0.4966 0.2636 -0.0341 0.0471  0.0538  231 LYS A CB  
1740 C CG  . LYS A 245 ? 0.4337 0.5785 0.3254 -0.0377 0.0520  0.0568  231 LYS A CG  
1741 C CD  . LYS A 245 ? 0.4347 0.5858 0.3271 -0.0355 0.0577  0.0464  231 LYS A CD  
1742 C CE  . LYS A 245 ? 0.4725 0.6341 0.3666 -0.0389 0.0627  0.0511  231 LYS A CE  
1743 N NZ  . LYS A 245 ? 0.4781 0.6504 0.3632 -0.0422 0.0632  0.0544  231 LYS A NZ  
1744 N N   . TRP A 246 ? 0.3423 0.4498 0.2615 -0.0350 0.0407  0.0689  232 TRP A N   
1745 C CA  . TRP A 246 ? 0.3270 0.4295 0.2563 -0.0366 0.0401  0.0756  232 TRP A CA  
1746 C C   . TRP A 246 ? 0.3340 0.4354 0.2653 -0.0397 0.0357  0.0869  232 TRP A C   
1747 O O   . TRP A 246 ? 0.3664 0.4728 0.3004 -0.0435 0.0361  0.0957  232 TRP A O   
1748 C CB  . TRP A 246 ? 0.3191 0.4087 0.2568 -0.0331 0.0387  0.0698  232 TRP A CB  
1749 C CG  . TRP A 246 ? 0.3095 0.3923 0.2581 -0.0340 0.0379  0.0742  232 TRP A CG  
1750 C CD1 . TRP A 246 ? 0.3246 0.4091 0.2782 -0.0374 0.0369  0.0840  232 TRP A CD1 
1751 C CD2 . TRP A 246 ? 0.2915 0.3645 0.2477 -0.0316 0.0375  0.0687  232 TRP A CD2 
1752 N NE1 . TRP A 246 ? 0.2870 0.3630 0.2511 -0.0370 0.0360  0.0842  232 TRP A NE1 
1753 C CE2 . TRP A 246 ? 0.2924 0.3615 0.2577 -0.0335 0.0364  0.0749  232 TRP A CE2 
1754 C CE3 . TRP A 246 ? 0.2875 0.3549 0.2436 -0.0282 0.0377  0.0595  232 TRP A CE3 
1755 C CZ2 . TRP A 246 ? 0.2847 0.3447 0.2582 -0.0323 0.0357  0.0715  232 TRP A CZ2 
1756 C CZ3 . TRP A 246 ? 0.2842 0.3430 0.2482 -0.0273 0.0369  0.0569  232 TRP A CZ3 
1757 C CH2 . TRP A 246 ? 0.2780 0.3333 0.2501 -0.0293 0.0361  0.0626  232 TRP A CH2 
1758 N N   . VAL A 247 ? 0.3508 0.4461 0.2814 -0.0385 0.0312  0.0873  233 VAL A N   
1759 C CA  . VAL A 247 ? 0.3600 0.4526 0.2952 -0.0411 0.0262  0.0977  233 VAL A CA  
1760 C C   . VAL A 247 ? 0.3909 0.4954 0.3171 -0.0454 0.0255  0.1057  233 VAL A C   
1761 O O   . VAL A 247 ? 0.3788 0.4839 0.3094 -0.0490 0.0218  0.1167  233 VAL A O   
1762 C CB  . VAL A 247 ? 0.3850 0.4661 0.3247 -0.0378 0.0220  0.0943  233 VAL A CB  
1763 C CG1 . VAL A 247 ? 0.3646 0.4486 0.2946 -0.0368 0.0202  0.0913  233 VAL A CG1 
1764 C CG2 . VAL A 247 ? 0.4122 0.4861 0.3634 -0.0390 0.0173  0.1025  233 VAL A CG2 
1765 N N   . LYS A 248 ? 0.3759 0.4902 0.2900 -0.0455 0.0287  0.1004  234 LYS A N   
1766 C CA  . LYS A 248 ? 0.3827 0.5103 0.2869 -0.0503 0.0290  0.1074  234 LYS A CA  
1767 C C   . LYS A 248 ? 0.3794 0.5161 0.2850 -0.0541 0.0328  0.1131  234 LYS A C   
1768 O O   . LYS A 248 ? 0.3829 0.5231 0.2905 -0.0578 0.0300  0.1220  234 LYS A O   
1769 C CB  . LYS A 248 ? 0.4031 0.5385 0.2942 -0.0490 0.0314  0.0985  234 LYS A CB  
1770 C CG  . LYS A 248 ? 0.4420 0.5894 0.3235 -0.0529 0.0314  0.1017  234 LYS A CG  
1771 C CD  . LYS A 248 ? 0.4838 0.6406 0.3580 -0.0517 0.0376  0.0912  234 LYS A CD  
1772 C CE  . LYS A 248 ? 0.5060 0.6741 0.3753 -0.0559 0.0385  0.0951  234 LYS A CE  
1773 N NZ  . LYS A 248 ? 0.5012 0.6725 0.3611 -0.0572 0.0347  0.0950  234 LYS A NZ  
1774 N N   . ASP A 249 ? 0.3815 0.5194 0.2893 -0.0520 0.0383  0.1059  235 ASP A N   
1775 C CA  . ASP A 249 ? 0.3834 0.5283 0.2947 -0.0547 0.0418  0.1095  235 ASP A CA  
1776 C C   . ASP A 249 ? 0.3703 0.5081 0.2943 -0.0566 0.0389  0.1192  235 ASP A C   
1777 O O   . ASP A 249 ? 0.3562 0.4990 0.2840 -0.0598 0.0390  0.1256  235 ASP A O   
1778 C CB  . ASP A 249 ? 0.3791 0.5281 0.2894 -0.0521 0.0485  0.0992  235 ASP A CB  
1779 C CG  . ASP A 249 ? 0.4021 0.5588 0.3013 -0.0504 0.0513  0.0892  235 ASP A CG  
1780 O OD1 . ASP A 249 ? 0.4343 0.5944 0.3257 -0.0519 0.0484  0.0910  235 ASP A OD1 
1781 O OD2 . ASP A 249 ? 0.4345 0.5939 0.3335 -0.0476 0.0561  0.0795  235 ASP A OD2 
1782 N N   . VAL A 250 ? 0.3395 0.4637 0.2722 -0.0537 0.0355  0.1179  236 VAL A N   
1783 C CA  . VAL A 250 ? 0.3578 0.4735 0.3042 -0.0547 0.0324  0.1250  236 VAL A CA  
1784 C C   . VAL A 250 ? 0.3657 0.4708 0.3180 -0.0538 0.0256  0.1287  236 VAL A C   
1785 O O   . VAL A 250 ? 0.3522 0.4456 0.3103 -0.0497 0.0242  0.1219  236 VAL A O   
1786 C CB  . VAL A 250 ? 0.3377 0.4457 0.2921 -0.0514 0.0351  0.1173  236 VAL A CB  
1787 C CG1 . VAL A 250 ? 0.3565 0.4581 0.3244 -0.0533 0.0324  0.1249  236 VAL A CG1 
1788 C CG2 . VAL A 250 ? 0.3573 0.4755 0.3061 -0.0514 0.0418  0.1116  236 VAL A CG2 
1789 N N   . PRO A 251 ? 0.3843 0.4934 0.3359 -0.0578 0.0213  0.1395  237 PRO A N   
1790 C CA  . PRO A 251 ? 0.3906 0.4898 0.3495 -0.0568 0.0147  0.1431  237 PRO A CA  
1791 C C   . PRO A 251 ? 0.3850 0.4714 0.3599 -0.0549 0.0122  0.1431  237 PRO A C   
1792 O O   . PRO A 251 ? 0.3942 0.4811 0.3770 -0.0573 0.0126  0.1485  237 PRO A O   
1793 C CB  . PRO A 251 ? 0.3990 0.5062 0.3563 -0.0623 0.0105  0.1562  237 PRO A CB  
1794 C CG  . PRO A 251 ? 0.3898 0.5105 0.3348 -0.0640 0.0152  0.1529  237 PRO A CG  
1795 C CD  . PRO A 251 ? 0.4105 0.5321 0.3566 -0.0625 0.0215  0.1468  237 PRO A CD  
1796 N N   . MET A 252 ? 0.3910 0.4662 0.3708 -0.0507 0.0098  0.1366  238 MET A N   
1797 C CA  . MET A 252 ? 0.3752 0.4381 0.3699 -0.0487 0.0073  0.1352  238 MET A CA  
1798 C C   . MET A 252 ? 0.3746 0.4286 0.3716 -0.0446 0.0047  0.1286  238 MET A C   
1799 O O   . MET A 252 ? 0.3689 0.4257 0.3556 -0.0430 0.0055  0.1239  238 MET A O   
1800 C CB  . MET A 252 ? 0.3956 0.4559 0.3928 -0.0472 0.0118  0.1284  238 MET A CB  
1801 C CG  . MET A 252 ? 0.3862 0.4493 0.3723 -0.0442 0.0169  0.1175  238 MET A CG  
1802 S SD  . MET A 252 ? 0.4749 0.5316 0.4656 -0.0414 0.0207  0.1078  238 MET A SD  
1803 C CE  . MET A 252 ? 0.3770 0.4439 0.3531 -0.0405 0.0262  0.1011  238 MET A CE  
1804 N N   . ALA A 253 ? 0.3770 0.4204 0.3879 -0.0431 0.0015  0.1281  239 ALA A N   
1805 C CA  . ALA A 253 ? 0.3652 0.4003 0.3798 -0.0392 -0.0005 0.1213  239 ALA A CA  
1806 C C   . ALA A 253 ? 0.3613 0.3953 0.3671 -0.0356 0.0042  0.1091  239 ALA A C   
1807 O O   . ALA A 253 ? 0.3454 0.3787 0.3505 -0.0350 0.0080  0.1040  239 ALA A O   
1808 C CB  . ALA A 253 ? 0.3603 0.3851 0.3922 -0.0381 -0.0039 0.1214  239 ALA A CB  
1809 N N   . HIS A 254 ? 0.3377 0.3715 0.3374 -0.0334 0.0036  0.1047  240 HIS A N   
1810 C CA  . HIS A 254 ? 0.3550 0.3876 0.3473 -0.0301 0.0072  0.0938  240 HIS A CA  
1811 C C   . HIS A 254 ? 0.3560 0.3836 0.3498 -0.0273 0.0047  0.0895  240 HIS A C   
1812 O O   . HIS A 254 ? 0.3617 0.3891 0.3590 -0.0280 0.0005  0.0952  240 HIS A O   
1813 C CB  . HIS A 254 ? 0.3238 0.3658 0.3020 -0.0309 0.0109  0.0918  240 HIS A CB  
1814 C CG  . HIS A 254 ? 0.3628 0.4122 0.3329 -0.0327 0.0088  0.0972  240 HIS A CG  
1815 N ND1 . HIS A 254 ? 0.3525 0.4072 0.3237 -0.0367 0.0063  0.1082  240 HIS A ND1 
1816 C CD2 . HIS A 254 ? 0.3450 0.3975 0.3056 -0.0314 0.0086  0.0933  240 HIS A CD2 
1817 C CE1 . HIS A 254 ? 0.3863 0.4475 0.3483 -0.0380 0.0046  0.1108  240 HIS A CE1 
1818 N NE2 . HIS A 254 ? 0.3846 0.4443 0.3401 -0.0347 0.0060  0.1016  240 HIS A NE2 
1819 N N   . ALA A 255 ? 0.3217 0.3456 0.3134 -0.0243 0.0072  0.0798  241 ALA A N   
1820 C CA  . ALA A 255 ? 0.3190 0.3386 0.3120 -0.0215 0.0056  0.0748  241 ALA A CA  
1821 C C   . ALA A 255 ? 0.2890 0.3085 0.2748 -0.0194 0.0091  0.0652  241 ALA A C   
1822 O O   . ALA A 255 ? 0.3109 0.3323 0.2929 -0.0198 0.0123  0.0624  241 ALA A O   
1823 C CB  . ALA A 255 ? 0.3171 0.3286 0.3241 -0.0204 0.0034  0.0742  241 ALA A CB  
1824 N N   . THR A 256 ? 0.2874 0.3047 0.2721 -0.0172 0.0080  0.0607  242 THR A N   
1825 C CA  . THR A 256 ? 0.2633 0.2785 0.2452 -0.0152 0.0103  0.0519  242 THR A CA  
1826 C C   . THR A 256 ? 0.2826 0.2915 0.2733 -0.0135 0.0091  0.0485  242 THR A C   
1827 O O   . THR A 256 ? 0.2760 0.2821 0.2754 -0.0135 0.0065  0.0524  242 THR A O   
1828 C CB  . THR A 256 ? 0.2719 0.2915 0.2436 -0.0142 0.0105  0.0486  242 THR A CB  
1829 O OG1 . THR A 256 ? 0.2928 0.3104 0.2665 -0.0127 0.0078  0.0479  242 THR A OG1 
1830 C CG2 . THR A 256 ? 0.2827 0.3098 0.2463 -0.0160 0.0106  0.0534  242 THR A CG2 
1831 N N   . MET A 257 ? 0.2854 0.2925 0.2743 -0.0121 0.0109  0.0411  243 MET A N   
1832 C CA  . MET A 257 ? 0.2494 0.2524 0.2443 -0.0105 0.0103  0.0369  243 MET A CA  
1833 C C   . MET A 257 ? 0.2751 0.2806 0.2645 -0.0092 0.0090  0.0350  243 MET A C   
1834 O O   . MET A 257 ? 0.2645 0.2742 0.2458 -0.0095 0.0085  0.0368  243 MET A O   
1835 C CB  . MET A 257 ? 0.2569 0.2570 0.2536 -0.0106 0.0129  0.0306  243 MET A CB  
1836 C CG  . MET A 257 ? 0.2595 0.2559 0.2650 -0.0116 0.0132  0.0317  243 MET A CG  
1837 S SD  . MET A 257 ? 0.3004 0.2938 0.3073 -0.0123 0.0160  0.0246  243 MET A SD  
1838 C CE  . MET A 257 ? 0.2851 0.2824 0.2814 -0.0135 0.0178  0.0242  243 MET A CE  
1839 N N   . LEU A 258 ? 0.2771 0.2802 0.2711 -0.0078 0.0086  0.0311  244 LEU A N   
1840 C CA  . LEU A 258 ? 0.2867 0.2918 0.2771 -0.0067 0.0069  0.0300  244 LEU A CA  
1841 C C   . LEU A 258 ? 0.2839 0.2922 0.2641 -0.0068 0.0078  0.0270  244 LEU A C   
1842 O O   . LEU A 258 ? 0.2699 0.2812 0.2446 -0.0065 0.0059  0.0284  244 LEU A O   
1843 C CB  . LEU A 258 ? 0.2724 0.2751 0.2696 -0.0054 0.0071  0.0256  244 LEU A CB  
1844 C CG  . LEU A 258 ? 0.3110 0.3155 0.3064 -0.0043 0.0053  0.0242  244 LEU A CG  
1845 C CD1 . LEU A 258 ? 0.3078 0.3141 0.3020 -0.0040 0.0016  0.0299  244 LEU A CD1 
1846 C CD2 . LEU A 258 ? 0.3425 0.3454 0.3463 -0.0033 0.0060  0.0203  244 LEU A CD2 
1847 N N   . MET A 259 ? 0.2706 0.2783 0.2489 -0.0074 0.0104  0.0229  245 MET A N   
1848 C CA  . MET A 259 ? 0.2657 0.2760 0.2368 -0.0073 0.0108  0.0194  245 MET A CA  
1849 C C   . MET A 259 ? 0.2833 0.2976 0.2476 -0.0077 0.0108  0.0218  245 MET A C   
1850 O O   . MET A 259 ? 0.2791 0.2962 0.2378 -0.0071 0.0101  0.0194  245 MET A O   
1851 C CB  . MET A 259 ? 0.2774 0.2863 0.2488 -0.0082 0.0131  0.0153  245 MET A CB  
1852 C CG  . MET A 259 ? 0.2632 0.2710 0.2365 -0.0081 0.0129  0.0111  245 MET A CG  
1853 S SD  . MET A 259 ? 0.3114 0.3173 0.2864 -0.0100 0.0151  0.0073  245 MET A SD  
1854 C CE  . MET A 259 ? 0.2302 0.2386 0.1996 -0.0105 0.0144  0.0051  245 MET A CE  
1855 N N   . GLY A 260 ? 0.2678 0.2828 0.2327 -0.0088 0.0118  0.0259  246 GLY A N   
1856 C CA  . GLY A 260 ? 0.2857 0.3057 0.2442 -0.0096 0.0125  0.0281  246 GLY A CA  
1857 C C   . GLY A 260 ? 0.2833 0.3066 0.2389 -0.0100 0.0103  0.0334  246 GLY A C   
1858 O O   . GLY A 260 ? 0.2942 0.3227 0.2440 -0.0112 0.0110  0.0357  246 GLY A O   
1859 N N   . LYS A 261 ? 0.2860 0.3069 0.2458 -0.0094 0.0075  0.0355  247 LYS A N   
1860 C CA  . LYS A 261 ? 0.2830 0.3069 0.2403 -0.0101 0.0045  0.0411  247 LYS A CA  
1861 C C   . LYS A 261 ? 0.2856 0.3154 0.2325 -0.0103 0.0043  0.0392  247 LYS A C   
1862 O O   . LYS A 261 ? 0.2702 0.3000 0.2142 -0.0089 0.0047  0.0330  247 LYS A O   
1863 C CB  . LYS A 261 ? 0.3097 0.3300 0.2735 -0.0089 0.0014  0.0419  247 LYS A CB  
1864 C CG  . LYS A 261 ? 0.3188 0.3392 0.2874 -0.0100 -0.0019 0.0495  247 LYS A CG  
1865 C CD  . LYS A 261 ? 0.3189 0.3360 0.2947 -0.0084 -0.0048 0.0491  247 LYS A CD  
1866 C CE  . LYS A 261 ? 0.3034 0.3209 0.2843 -0.0095 -0.0092 0.0571  247 LYS A CE  
1867 N NZ  . LYS A 261 ? 0.3282 0.3474 0.3100 -0.0119 -0.0095 0.0640  247 LYS A NZ  
1868 N N   . GLY A 262 ? 0.2934 0.3286 0.2349 -0.0122 0.0037  0.0443  248 GLY A N   
1869 C CA  . GLY A 262 ? 0.3019 0.3439 0.2330 -0.0127 0.0041  0.0421  248 GLY A CA  
1870 C C   . GLY A 262 ? 0.3230 0.3702 0.2497 -0.0139 0.0081  0.0413  248 GLY A C   
1871 O O   . GLY A 262 ? 0.2975 0.3519 0.2156 -0.0149 0.0088  0.0404  248 GLY A O   
1872 N N   . ILE A 263 ? 0.2896 0.3337 0.2220 -0.0141 0.0108  0.0415  249 ILE A N   
1873 C CA  . ILE A 263 ? 0.3028 0.3523 0.2322 -0.0155 0.0145  0.0417  249 ILE A CA  
1874 C C   . ILE A 263 ? 0.3323 0.3885 0.2573 -0.0185 0.0140  0.0495  249 ILE A C   
1875 O O   . ILE A 263 ? 0.3194 0.3839 0.2370 -0.0198 0.0164  0.0489  249 ILE A O   
1876 C CB  . ILE A 263 ? 0.2956 0.3401 0.2330 -0.0154 0.0167  0.0415  249 ILE A CB  
1877 C CG1 . ILE A 263 ? 0.2687 0.3093 0.2078 -0.0133 0.0179  0.0334  249 ILE A CG1 
1878 C CG2 . ILE A 263 ? 0.2827 0.3326 0.2189 -0.0177 0.0197  0.0451  249 ILE A CG2 
1879 C CD1 . ILE A 263 ? 0.2900 0.3235 0.2376 -0.0131 0.0184  0.0329  249 ILE A CD1 
1880 N N   . PHE A 264 ? 0.2956 0.3491 0.2255 -0.0198 0.0107  0.0570  250 PHE A N   
1881 C CA  . PHE A 264 ? 0.3295 0.3890 0.2570 -0.0233 0.0096  0.0660  250 PHE A CA  
1882 C C   . PHE A 264 ? 0.3325 0.3943 0.2558 -0.0243 0.0051  0.0702  250 PHE A C   
1883 O O   . PHE A 264 ? 0.3243 0.3804 0.2516 -0.0223 0.0019  0.0686  250 PHE A O   
1884 C CB  . PHE A 264 ? 0.3188 0.3736 0.2570 -0.0246 0.0086  0.0730  250 PHE A CB  
1885 C CG  . PHE A 264 ? 0.3196 0.3730 0.2617 -0.0245 0.0127  0.0705  250 PHE A CG  
1886 C CD1 . PHE A 264 ? 0.3014 0.3628 0.2372 -0.0261 0.0165  0.0703  250 PHE A CD1 
1887 C CD2 . PHE A 264 ? 0.3067 0.3513 0.2587 -0.0227 0.0127  0.0680  250 PHE A CD2 
1888 C CE1 . PHE A 264 ? 0.3273 0.3874 0.2676 -0.0260 0.0199  0.0683  250 PHE A CE1 
1889 C CE2 . PHE A 264 ? 0.3094 0.3526 0.2649 -0.0229 0.0159  0.0659  250 PHE A CE2 
1890 C CZ  . PHE A 264 ? 0.2929 0.3436 0.2430 -0.0245 0.0194  0.0663  250 PHE A CZ  
1891 N N   . ASP A 265 ? 0.3536 0.4244 0.2693 -0.0278 0.0047  0.0761  251 ASP A N   
1892 C CA  . ASP A 265 ? 0.3656 0.4389 0.2788 -0.0301 -0.0004 0.0835  251 ASP A CA  
1893 C C   . ASP A 265 ? 0.3849 0.4520 0.3108 -0.0311 -0.0039 0.0922  251 ASP A C   
1894 O O   . ASP A 265 ? 0.3732 0.4422 0.3027 -0.0336 -0.0029 0.0984  251 ASP A O   
1895 C CB  . ASP A 265 ? 0.3797 0.4652 0.2811 -0.0342 0.0004  0.0878  251 ASP A CB  
1896 C CG  . ASP A 265 ? 0.4161 0.5053 0.3138 -0.0372 -0.0053 0.0960  251 ASP A CG  
1897 O OD1 . ASP A 265 ? 0.3910 0.4733 0.2981 -0.0370 -0.0102 0.1015  251 ASP A OD1 
1898 O OD2 . ASP A 265 ? 0.4699 0.5696 0.3552 -0.0403 -0.0048 0.0972  251 ASP A OD2 
1899 N N   . GLU A 266 ? 0.3679 0.4279 0.3014 -0.0292 -0.0080 0.0926  252 GLU A N   
1900 C CA  . GLU A 266 ? 0.3776 0.4306 0.3256 -0.0293 -0.0110 0.0986  252 GLU A CA  
1901 C C   . GLU A 266 ? 0.4369 0.4933 0.3876 -0.0333 -0.0163 0.1108  252 GLU A C   
1902 O O   . GLU A 266 ? 0.4559 0.5064 0.4203 -0.0334 -0.0197 0.1163  252 GLU A O   
1903 C CB  . GLU A 266 ? 0.3436 0.3879 0.3002 -0.0254 -0.0125 0.0928  252 GLU A CB  
1904 C CG  . GLU A 266 ? 0.3456 0.3868 0.2995 -0.0220 -0.0079 0.0815  252 GLU A CG  
1905 C CD  . GLU A 266 ? 0.3456 0.3783 0.3097 -0.0186 -0.0086 0.0764  252 GLU A CD  
1906 O OE1 . GLU A 266 ? 0.3589 0.3892 0.3295 -0.0183 -0.0129 0.0798  252 GLU A OE1 
1907 O OE2 . GLU A 266 ? 0.3317 0.3609 0.2975 -0.0165 -0.0050 0.0691  252 GLU A OE2 
1908 N N   . ARG A 267 ? 0.4561 0.5221 0.3946 -0.0368 -0.0174 0.1153  253 ARG A N   
1909 C CA  . ARG A 267 ? 0.4708 0.5419 0.4105 -0.0418 -0.0221 0.1282  253 ARG A CA  
1910 C C   . ARG A 267 ? 0.4810 0.5583 0.4190 -0.0455 -0.0194 0.1342  253 ARG A C   
1911 O O   . ARG A 267 ? 0.4754 0.5555 0.4182 -0.0497 -0.0235 0.1460  253 ARG A O   
1912 C CB  . ARG A 267 ? 0.4561 0.5353 0.3829 -0.0443 -0.0253 0.1307  253 ARG A CB  
1913 C CG  . ARG A 267 ? 0.4526 0.5265 0.3799 -0.0408 -0.0280 0.1246  253 ARG A CG  
1914 C CD  . ARG A 267 ? 0.4472 0.5296 0.3582 -0.0424 -0.0288 0.1221  253 ARG A CD  
1915 N NE  . ARG A 267 ? 0.4298 0.5200 0.3276 -0.0428 -0.0226 0.1152  253 ARG A NE  
1916 C CZ  . ARG A 267 ? 0.4641 0.5624 0.3473 -0.0438 -0.0220 0.1108  253 ARG A CZ  
1917 N NH1 . ARG A 267 ? 0.4490 0.5489 0.3277 -0.0451 -0.0274 0.1131  253 ARG A NH1 
1918 N NH2 . ARG A 267 ? 0.4587 0.5636 0.3323 -0.0437 -0.0159 0.1036  253 ARG A NH2 
1919 N N   . HIS A 268 ? 0.4723 0.5517 0.4049 -0.0441 -0.0128 0.1267  254 HIS A N   
1920 C CA  . HIS A 268 ? 0.5093 0.5963 0.4389 -0.0476 -0.0094 0.1314  254 HIS A CA  
1921 C C   . HIS A 268 ? 0.4935 0.5742 0.4387 -0.0486 -0.0113 0.1387  254 HIS A C   
1922 O O   . HIS A 268 ? 0.4861 0.5559 0.4441 -0.0453 -0.0130 0.1359  254 HIS A O   
1923 C CB  . HIS A 268 ? 0.5113 0.6009 0.4331 -0.0451 -0.0022 0.1201  254 HIS A CB  
1924 C CG  . HIS A 268 ? 0.6067 0.7068 0.5222 -0.0486 0.0022  0.1232  254 HIS A CG  
1925 N ND1 . HIS A 268 ? 0.6598 0.7591 0.5841 -0.0506 0.0031  0.1295  254 HIS A ND1 
1926 C CD2 . HIS A 268 ? 0.7402 0.8524 0.6417 -0.0506 0.0061  0.1207  254 HIS A CD2 
1927 C CE1 . HIS A 268 ? 0.6418 0.7525 0.5579 -0.0537 0.0074  0.1311  254 HIS A CE1 
1928 N NE2 . HIS A 268 ? 0.9018 1.0207 0.8040 -0.0538 0.0095  0.1255  254 HIS A NE2 
1929 N N   . VAL A 269 ? 0.5068 0.5950 0.4514 -0.0534 -0.0112 0.1481  255 VAL A N   
1930 C CA  . VAL A 269 ? 0.4782 0.5610 0.4381 -0.0549 -0.0135 0.1558  255 VAL A CA  
1931 C C   . VAL A 269 ? 0.4393 0.5136 0.4067 -0.0506 -0.0092 0.1466  255 VAL A C   
1932 O O   . VAL A 269 ? 0.4112 0.4884 0.3704 -0.0488 -0.0032 0.1378  255 VAL A O   
1933 C CB  . VAL A 269 ? 0.5162 0.6100 0.4729 -0.0611 -0.0134 0.1673  255 VAL A CB  
1934 C CG1 . VAL A 269 ? 0.5454 0.6496 0.4877 -0.0617 -0.0061 0.1609  255 VAL A CG1 
1935 C CG2 . VAL A 269 ? 0.4769 0.5648 0.4500 -0.0624 -0.0154 0.1743  255 VAL A CG2 
1936 N N   . GLY A 270 ? 0.4214 0.4855 0.4053 -0.0492 -0.0125 0.1485  256 GLY A N   
1937 C CA  . GLY A 270 ? 0.4240 0.4795 0.4160 -0.0456 -0.0093 0.1403  256 GLY A CA  
1938 C C   . GLY A 270 ? 0.4079 0.4546 0.4023 -0.0403 -0.0087 0.1293  256 GLY A C   
1939 O O   . GLY A 270 ? 0.3685 0.4077 0.3703 -0.0376 -0.0066 0.1226  256 GLY A O   
1940 N N   . PHE A 271 ? 0.3991 0.4469 0.3872 -0.0390 -0.0104 0.1270  257 PHE A N   
1941 C CA  . PHE A 271 ? 0.3785 0.4186 0.3695 -0.0344 -0.0103 0.1175  257 PHE A CA  
1942 C C   . PHE A 271 ? 0.3810 0.4149 0.3854 -0.0339 -0.0163 0.1222  257 PHE A C   
1943 O O   . PHE A 271 ? 0.4214 0.4590 0.4253 -0.0365 -0.0210 0.1308  257 PHE A O   
1944 C CB  . PHE A 271 ? 0.4056 0.4502 0.3823 -0.0329 -0.0082 0.1109  257 PHE A CB  
1945 C CG  . PHE A 271 ? 0.3620 0.3995 0.3415 -0.0284 -0.0077 0.1012  257 PHE A CG  
1946 C CD1 . PHE A 271 ? 0.3516 0.3861 0.3295 -0.0258 -0.0030 0.0916  257 PHE A CD1 
1947 C CD2 . PHE A 271 ? 0.3783 0.4123 0.3627 -0.0271 -0.0120 0.1021  257 PHE A CD2 
1948 C CE1 . PHE A 271 ? 0.3317 0.3604 0.3121 -0.0223 -0.0025 0.0834  257 PHE A CE1 
1949 C CE2 . PHE A 271 ? 0.3594 0.3878 0.3467 -0.0233 -0.0112 0.0935  257 PHE A CE2 
1950 C CZ  . PHE A 271 ? 0.3488 0.3747 0.3336 -0.0210 -0.0064 0.0843  257 PHE A CZ  
1951 N N   . TYR A 272 ? 0.3698 0.3945 0.3863 -0.0306 -0.0162 0.1163  258 TYR A N   
1952 C CA  . TYR A 272 ? 0.4009 0.4191 0.4329 -0.0296 -0.0214 0.1195  258 TYR A CA  
1953 C C   . TYR A 272 ? 0.3878 0.4008 0.4226 -0.0254 -0.0210 0.1104  258 TYR A C   
1954 O O   . TYR A 272 ? 0.3830 0.3913 0.4312 -0.0242 -0.0251 0.1122  258 TYR A O   
1955 C CB  . TYR A 272 ? 0.3835 0.3958 0.4313 -0.0300 -0.0223 0.1215  258 TYR A CB  
1956 C CG  . TYR A 272 ? 0.3855 0.4031 0.4321 -0.0345 -0.0232 0.1315  258 TYR A CG  
1957 C CD1 . TYR A 272 ? 0.4317 0.4525 0.4836 -0.0383 -0.0291 0.1442  258 TYR A CD1 
1958 C CD2 . TYR A 272 ? 0.3891 0.4089 0.4297 -0.0353 -0.0183 0.1288  258 TYR A CD2 
1959 C CE1 . TYR A 272 ? 0.4372 0.4638 0.4880 -0.0430 -0.0299 0.1540  258 TYR A CE1 
1960 C CE2 . TYR A 272 ? 0.4039 0.4294 0.4439 -0.0397 -0.0188 0.1382  258 TYR A CE2 
1961 C CZ  . TYR A 272 ? 0.4282 0.4572 0.4731 -0.0436 -0.0246 0.1509  258 TYR A CZ  
1962 O OH  . TYR A 272 ? 0.4763 0.5118 0.5205 -0.0484 -0.0252 0.1610  258 TYR A OH  
1963 N N   . GLY A 273 ? 0.3704 0.3846 0.3941 -0.0232 -0.0164 0.1011  259 GLY A N   
1964 C CA  . GLY A 273 ? 0.3642 0.3741 0.3902 -0.0195 -0.0156 0.0925  259 GLY A CA  
1965 C C   . GLY A 273 ? 0.3494 0.3573 0.3708 -0.0173 -0.0100 0.0822  259 GLY A C   
1966 O O   . GLY A 273 ? 0.3300 0.3385 0.3489 -0.0185 -0.0070 0.0816  259 GLY A O   
1967 N N   . THR A 274 ? 0.3313 0.3371 0.3518 -0.0145 -0.0087 0.0744  260 THR A N   
1968 C CA  . THR A 274 ? 0.3279 0.3321 0.3437 -0.0129 -0.0040 0.0651  260 THR A CA  
1969 C C   . THR A 274 ? 0.3167 0.3150 0.3445 -0.0120 -0.0028 0.0613  260 THR A C   
1970 O O   . THR A 274 ? 0.3200 0.3144 0.3604 -0.0110 -0.0052 0.0618  260 THR A O   
1971 C CB  . THR A 274 ? 0.3292 0.3342 0.3397 -0.0108 -0.0035 0.0590  260 THR A CB  
1972 O OG1 . THR A 274 ? 0.3153 0.3258 0.3146 -0.0118 -0.0048 0.0620  260 THR A OG1 
1973 C CG2 . THR A 274 ? 0.3036 0.3075 0.3095 -0.0097 0.0009  0.0503  260 THR A CG2 
1974 N N   . TYR A 275 ? 0.3127 0.3104 0.3372 -0.0125 0.0008  0.0574  261 TYR A N   
1975 C CA  . TYR A 275 ? 0.3184 0.3109 0.3527 -0.0120 0.0022  0.0529  261 TYR A CA  
1976 C C   . TYR A 275 ? 0.3238 0.3143 0.3582 -0.0099 0.0044  0.0437  261 TYR A C   
1977 O O   . TYR A 275 ? 0.3220 0.3151 0.3462 -0.0096 0.0067  0.0395  261 TYR A O   
1978 C CB  . TYR A 275 ? 0.2896 0.2827 0.3200 -0.0138 0.0047  0.0529  261 TYR A CB  
1979 C CG  . TYR A 275 ? 0.3043 0.2920 0.3436 -0.0137 0.0060  0.0483  261 TYR A CG  
1980 C CD1 . TYR A 275 ? 0.2952 0.2787 0.3489 -0.0137 0.0033  0.0507  261 TYR A CD1 
1981 C CD2 . TYR A 275 ? 0.2855 0.2728 0.3195 -0.0137 0.0094  0.0415  261 TYR A CD2 
1982 C CE1 . TYR A 275 ? 0.3046 0.2834 0.3664 -0.0136 0.0044  0.0456  261 TYR A CE1 
1983 C CE2 . TYR A 275 ? 0.2989 0.2819 0.3402 -0.0140 0.0104  0.0370  261 TYR A CE2 
1984 C CZ  . TYR A 275 ? 0.3172 0.2960 0.3721 -0.0139 0.0080  0.0387  261 TYR A CZ  
1985 O OH  . TYR A 275 ? 0.3317 0.3062 0.3938 -0.0142 0.0088  0.0335  261 TYR A OH  
1986 N N   . SER A 276 ? 0.3293 0.3157 0.3760 -0.0086 0.0037  0.0405  262 SER A N   
1987 C CA  . SER A 276 ? 0.3392 0.3246 0.3870 -0.0070 0.0063  0.0316  262 SER A CA  
1988 C C   . SER A 276 ? 0.3430 0.3240 0.4032 -0.0066 0.0071  0.0268  262 SER A C   
1989 O O   . SER A 276 ? 0.3499 0.3296 0.4187 -0.0050 0.0072  0.0221  262 SER A O   
1990 C CB  . SER A 276 ? 0.3851 0.3721 0.4340 -0.0053 0.0049  0.0310  262 SER A CB  
1991 O OG  . SER A 276 ? 0.4063 0.3916 0.4667 -0.0046 0.0011  0.0362  262 SER A OG  
1992 N N   . GLY A 277 ? 0.3371 0.3160 0.3989 -0.0081 0.0075  0.0278  263 GLY A N   
1993 C CA  . GLY A 277 ? 0.3265 0.3012 0.3995 -0.0079 0.0083  0.0223  263 GLY A CA  
1994 C C   . GLY A 277 ? 0.3535 0.3249 0.4431 -0.0066 0.0049  0.0246  263 GLY A C   
1995 O O   . GLY A 277 ? 0.3502 0.3216 0.4436 -0.0070 0.0011  0.0334  263 GLY A O   
1996 N N   . SER A 278 ? 0.3531 0.3222 0.4532 -0.0051 0.0061  0.0166  264 SER A N   
1997 C CA  . SER A 278 ? 0.3719 0.3375 0.4905 -0.0036 0.0028  0.0177  264 SER A CA  
1998 C C   . SER A 278 ? 0.3692 0.3365 0.4913 -0.0021 -0.0001 0.0227  264 SER A C   
1999 O O   . SER A 278 ? 0.3563 0.3210 0.4938 -0.0013 -0.0041 0.0267  264 SER A O   
2000 C CB  . SER A 278 ? 0.3577 0.3213 0.4866 -0.0022 0.0053  0.0065  264 SER A CB  
2001 O OG  . SER A 278 ? 0.3777 0.3451 0.5010 -0.0009 0.0087  -0.0003 264 SER A OG  
2002 N N   . ALA A 279 ? 0.3590 0.3307 0.4682 -0.0019 0.0014  0.0228  265 ALA A N   
2003 C CA  . ALA A 279 ? 0.3732 0.3468 0.4845 -0.0008 -0.0016 0.0276  265 ALA A CA  
2004 C C   . ALA A 279 ? 0.4000 0.3749 0.5060 -0.0026 -0.0056 0.0391  265 ALA A C   
2005 O O   . ALA A 279 ? 0.4305 0.4070 0.5389 -0.0021 -0.0090 0.0444  265 ALA A O   
2006 C CB  . ALA A 279 ? 0.4085 0.3863 0.5088 0.0000  0.0014  0.0226  265 ALA A CB  
2007 N N   . SER A 280 ? 0.3757 0.3507 0.4750 -0.0048 -0.0053 0.0430  266 SER A N   
2008 C CA  . SER A 280 ? 0.3737 0.3512 0.4669 -0.0070 -0.0085 0.0537  266 SER A CA  
2009 C C   . SER A 280 ? 0.3891 0.3644 0.4979 -0.0073 -0.0142 0.0616  266 SER A C   
2010 O O   . SER A 280 ? 0.3607 0.3314 0.4861 -0.0062 -0.0156 0.0592  266 SER A O   
2011 C CB  . SER A 280 ? 0.3630 0.3410 0.4489 -0.0094 -0.0068 0.0560  266 SER A CB  
2012 O OG  . SER A 280 ? 0.3413 0.3207 0.4155 -0.0092 -0.0019 0.0484  266 SER A OG  
2013 N N   . ALA A 281 ? 0.3911 0.3699 0.4948 -0.0090 -0.0178 0.0711  267 ALA A N   
2014 C CA  . ALA A 281 ? 0.3860 0.3636 0.5027 -0.0106 -0.0239 0.0812  267 ALA A CA  
2015 C C   . ALA A 281 ? 0.3819 0.3567 0.5056 -0.0125 -0.0247 0.0847  267 ALA A C   
2016 O O   . ALA A 281 ? 0.3853 0.3615 0.4988 -0.0138 -0.0210 0.0828  267 ALA A O   
2017 C CB  . ALA A 281 ? 0.4059 0.3891 0.5119 -0.0130 -0.0272 0.0911  267 ALA A CB  
2018 N N   . GLY A 282 ? 0.3823 0.3532 0.5249 -0.0129 -0.0299 0.0901  268 GLY A N   
2019 C CA  . GLY A 282 ? 0.3771 0.3446 0.5298 -0.0146 -0.0313 0.0931  268 GLY A CA  
2020 C C   . GLY A 282 ? 0.3798 0.3520 0.5205 -0.0186 -0.0314 0.1022  268 GLY A C   
2021 O O   . GLY A 282 ? 0.3936 0.3643 0.5348 -0.0199 -0.0296 0.1014  268 GLY A O   
2022 N N   . ALA A 283 ? 0.3986 0.3769 0.5288 -0.0209 -0.0335 0.1109  269 ALA A N   
2023 C CA  . ALA A 283 ? 0.3892 0.3736 0.5066 -0.0249 -0.0329 0.1189  269 ALA A CA  
2024 C C   . ALA A 283 ? 0.3864 0.3734 0.4872 -0.0242 -0.0258 0.1108  269 ALA A C   
2025 O O   . ALA A 283 ? 0.3874 0.3768 0.4832 -0.0266 -0.0240 0.1138  269 ALA A O   
2026 C CB  . ALA A 283 ? 0.3921 0.3834 0.5005 -0.0274 -0.0363 0.1285  269 ALA A CB  
2027 N N   . VAL A 284 ? 0.3966 0.3833 0.4894 -0.0211 -0.0220 0.1008  270 VAL A N   
2028 C CA  . VAL A 284 ? 0.3869 0.3757 0.4654 -0.0204 -0.0159 0.0930  270 VAL A CA  
2029 C C   . VAL A 284 ? 0.3648 0.3481 0.4509 -0.0196 -0.0135 0.0866  270 VAL A C   
2030 O O   . VAL A 284 ? 0.3629 0.3479 0.4420 -0.0210 -0.0104 0.0859  270 VAL A O   
2031 C CB  . VAL A 284 ? 0.3603 0.3502 0.4294 -0.0176 -0.0133 0.0849  270 VAL A CB  
2032 C CG1 . VAL A 284 ? 0.3475 0.3387 0.4043 -0.0169 -0.0075 0.0767  270 VAL A CG1 
2033 C CG2 . VAL A 284 ? 0.3815 0.3771 0.4418 -0.0188 -0.0158 0.0912  270 VAL A CG2 
2034 N N   . LYS A 285 ? 0.3784 0.3554 0.4795 -0.0174 -0.0149 0.0816  271 LYS A N   
2035 C CA  . LYS A 285 ? 0.3835 0.3554 0.4923 -0.0168 -0.0129 0.0749  271 LYS A CA  
2036 C C   . LYS A 285 ? 0.3860 0.3575 0.4995 -0.0199 -0.0148 0.0827  271 LYS A C   
2037 O O   . LYS A 285 ? 0.3601 0.3311 0.4697 -0.0208 -0.0118 0.0793  271 LYS A O   
2038 C CB  . LYS A 285 ? 0.3772 0.3431 0.5032 -0.0142 -0.0146 0.0689  271 LYS A CB  
2039 C CG  . LYS A 285 ? 0.4285 0.3946 0.5491 -0.0112 -0.0107 0.0580  271 LYS A CG  
2040 C CD  . LYS A 285 ? 0.4136 0.3744 0.5488 -0.0089 -0.0101 0.0484  271 LYS A CD  
2041 C CE  . LYS A 285 ? 0.4006 0.3604 0.5485 -0.0065 -0.0128 0.0479  271 LYS A CE  
2042 N NZ  . LYS A 285 ? 0.3804 0.3370 0.5392 -0.0040 -0.0104 0.0360  271 LYS A NZ  
2043 N N   . GLU A 286 ? 0.3910 0.3633 0.5134 -0.0220 -0.0202 0.0937  272 GLU A N   
2044 C CA  . GLU A 286 ? 0.4018 0.3744 0.5295 -0.0254 -0.0224 0.1023  272 GLU A CA  
2045 C C   . GLU A 286 ? 0.4063 0.3864 0.5164 -0.0280 -0.0189 0.1061  272 GLU A C   
2046 O O   . GLU A 286 ? 0.3706 0.3507 0.4805 -0.0297 -0.0173 0.1068  272 GLU A O   
2047 C CB  . GLU A 286 ? 0.4360 0.4084 0.5773 -0.0274 -0.0295 0.1142  272 GLU A CB  
2048 C CG  . GLU A 286 ? 0.5100 0.4838 0.6567 -0.0316 -0.0325 0.1250  272 GLU A CG  
2049 C CD  . GLU A 286 ? 0.5588 0.5255 0.7197 -0.0312 -0.0328 0.1204  272 GLU A CD  
2050 O OE1 . GLU A 286 ? 0.5879 0.5477 0.7609 -0.0279 -0.0333 0.1115  272 GLU A OE1 
2051 O OE2 . GLU A 286 ? 0.5568 0.5251 0.7166 -0.0341 -0.0323 0.1251  272 GLU A OE2 
2052 N N   . ALA A 287 ? 0.3838 0.3704 0.4793 -0.0282 -0.0175 0.1079  273 ALA A N   
2053 C CA  . ALA A 287 ? 0.4080 0.4025 0.4877 -0.0306 -0.0141 0.1112  273 ALA A CA  
2054 C C   . ALA A 287 ? 0.4010 0.3948 0.4724 -0.0291 -0.0084 0.1013  273 ALA A C   
2055 O O   . ALA A 287 ? 0.4310 0.4284 0.4974 -0.0313 -0.0060 0.1035  273 ALA A O   
2056 C CB  . ALA A 287 ? 0.3851 0.3866 0.4515 -0.0310 -0.0141 0.1140  273 ALA A CB  
2057 N N   . ILE A 288 ? 0.3554 0.3449 0.4261 -0.0257 -0.0062 0.0906  274 ILE A N   
2058 C CA  . ILE A 288 ? 0.3643 0.3535 0.4265 -0.0246 -0.0012 0.0816  274 ILE A CA  
2059 C C   . ILE A 288 ? 0.3627 0.3450 0.4361 -0.0242 -0.0012 0.0765  274 ILE A C   
2060 O O   . ILE A 288 ? 0.3427 0.3252 0.4154 -0.0259 0.0004  0.0770  274 ILE A O   
2061 C CB  . ILE A 288 ? 0.3220 0.3119 0.3750 -0.0218 0.0012  0.0735  274 ILE A CB  
2062 C CG1 . ILE A 288 ? 0.3306 0.3274 0.3724 -0.0224 0.0008  0.0781  274 ILE A CG1 
2063 C CG2 . ILE A 288 ? 0.3137 0.3032 0.3592 -0.0211 0.0056  0.0647  274 ILE A CG2 
2064 C CD1 . ILE A 288 ? 0.3348 0.3387 0.3672 -0.0251 0.0025  0.0837  274 ILE A CD1 
2065 N N   . GLU A 289 ? 0.3690 0.3453 0.4531 -0.0221 -0.0029 0.0714  275 GLU A N   
2066 C CA  . GLU A 289 ? 0.3477 0.3178 0.4419 -0.0216 -0.0026 0.0650  275 GLU A CA  
2067 C C   . GLU A 289 ? 0.3557 0.3232 0.4624 -0.0240 -0.0060 0.0722  275 GLU A C   
2068 O O   . GLU A 289 ? 0.3370 0.3007 0.4489 -0.0245 -0.0054 0.0682  275 GLU A O   
2069 C CB  . GLU A 289 ? 0.3344 0.2999 0.4377 -0.0187 -0.0033 0.0572  275 GLU A CB  
2070 C CG  . GLU A 289 ? 0.3743 0.3408 0.4668 -0.0169 0.0011  0.0470  275 GLU A CG  
2071 C CD  . GLU A 289 ? 0.3819 0.3457 0.4821 -0.0142 0.0010  0.0398  275 GLU A CD  
2072 O OE1 . GLU A 289 ? 0.3875 0.3475 0.5034 -0.0134 -0.0023 0.0410  275 GLU A OE1 
2073 O OE2 . GLU A 289 ? 0.3543 0.3201 0.4456 -0.0129 0.0041  0.0329  275 GLU A OE2 
2074 N N   . GLY A 290 ? 0.3565 0.3263 0.4682 -0.0257 -0.0100 0.0831  276 GLY A N   
2075 C CA  . GLY A 290 ? 0.3493 0.3171 0.4737 -0.0284 -0.0139 0.0915  276 GLY A CA  
2076 C C   . GLY A 290 ? 0.3673 0.3402 0.4839 -0.0317 -0.0121 0.0975  276 GLY A C   
2077 O O   . GLY A 290 ? 0.3709 0.3419 0.4980 -0.0341 -0.0148 0.1033  276 GLY A O   
2078 N N   . ALA A 291 ? 0.3724 0.3518 0.4718 -0.0318 -0.0076 0.0961  277 ALA A N   
2079 C CA  . ALA A 291 ? 0.3768 0.3618 0.4690 -0.0346 -0.0052 0.1006  277 ALA A CA  
2080 C C   . ALA A 291 ? 0.3737 0.3541 0.4693 -0.0345 -0.0033 0.0938  277 ALA A C   
2081 O O   . ALA A 291 ? 0.3484 0.3237 0.4443 -0.0320 -0.0018 0.0835  277 ALA A O   
2082 C CB  . ALA A 291 ? 0.3511 0.3442 0.4252 -0.0344 -0.0009 0.0994  277 ALA A CB  
2083 N N   . ASP A 292 ? 0.3637 0.3464 0.4618 -0.0375 -0.0034 0.1000  278 ASP A N   
2084 C CA  . ASP A 292 ? 0.3641 0.3427 0.4649 -0.0377 -0.0018 0.0939  278 ASP A CA  
2085 C C   . ASP A 292 ? 0.3569 0.3399 0.4430 -0.0371 0.0035  0.0879  278 ASP A C   
2086 O O   . ASP A 292 ? 0.3630 0.3423 0.4495 -0.0367 0.0049  0.0809  278 ASP A O   
2087 C CB  . ASP A 292 ? 0.4178 0.3959 0.5300 -0.0411 -0.0047 0.1023  278 ASP A CB  
2088 C CG  . ASP A 292 ? 0.4352 0.4221 0.5442 -0.0443 -0.0051 0.1148  278 ASP A CG  
2089 O OD1 . ASP A 292 ? 0.4487 0.4438 0.5436 -0.0447 -0.0009 0.1153  278 ASP A OD1 
2090 O OD2 . ASP A 292 ? 0.4260 0.4121 0.5469 -0.0465 -0.0099 0.1241  278 ASP A OD2 
2091 N N   . THR A 293 ? 0.3459 0.3366 0.4195 -0.0369 0.0062  0.0901  279 THR A N   
2092 C CA  . THR A 293 ? 0.3308 0.3253 0.3915 -0.0358 0.0108  0.0836  279 THR A CA  
2093 C C   . THR A 293 ? 0.3165 0.3150 0.3667 -0.0338 0.0121  0.0816  279 THR A C   
2094 O O   . THR A 293 ? 0.3138 0.3176 0.3615 -0.0348 0.0111  0.0887  279 THR A O   
2095 C CB  . THR A 293 ? 0.3346 0.3363 0.3913 -0.0383 0.0134  0.0883  279 THR A CB  
2096 O OG1 . THR A 293 ? 0.3722 0.3702 0.4399 -0.0405 0.0116  0.0914  279 THR A OG1 
2097 C CG2 . THR A 293 ? 0.3304 0.3346 0.3769 -0.0370 0.0176  0.0807  279 THR A CG2 
2098 N N   . VAL A 294 ? 0.3192 0.3154 0.3633 -0.0314 0.0140  0.0724  280 VAL A N   
2099 C CA  . VAL A 294 ? 0.2981 0.2973 0.3328 -0.0293 0.0150  0.0694  280 VAL A CA  
2100 C C   . VAL A 294 ? 0.3034 0.3065 0.3278 -0.0287 0.0188  0.0640  280 VAL A C   
2101 O O   . VAL A 294 ? 0.2832 0.2826 0.3082 -0.0283 0.0198  0.0576  280 VAL A O   
2102 C CB  . VAL A 294 ? 0.3361 0.3291 0.3746 -0.0268 0.0134  0.0635  280 VAL A CB  
2103 C CG1 . VAL A 294 ? 0.2885 0.2847 0.3173 -0.0249 0.0143  0.0607  280 VAL A CG1 
2104 C CG2 . VAL A 294 ? 0.3081 0.2967 0.3593 -0.0272 0.0092  0.0684  280 VAL A CG2 
2105 N N   . LEU A 295 ? 0.2733 0.2841 0.2889 -0.0290 0.0207  0.0666  281 LEU A N   
2106 C CA  . LEU A 295 ? 0.2646 0.2797 0.2714 -0.0281 0.0240  0.0613  281 LEU A CA  
2107 C C   . LEU A 295 ? 0.3018 0.3151 0.3031 -0.0255 0.0237  0.0550  281 LEU A C   
2108 O O   . LEU A 295 ? 0.3042 0.3198 0.3019 -0.0248 0.0226  0.0571  281 LEU A O   
2109 C CB  . LEU A 295 ? 0.2761 0.3008 0.2767 -0.0295 0.0262  0.0662  281 LEU A CB  
2110 C CG  . LEU A 295 ? 0.2748 0.3023 0.2814 -0.0325 0.0262  0.0740  281 LEU A CG  
2111 C CD1 . LEU A 295 ? 0.2717 0.3105 0.2717 -0.0343 0.0292  0.0785  281 LEU A CD1 
2112 C CD2 . LEU A 295 ? 0.2449 0.2678 0.2581 -0.0332 0.0267  0.0714  281 LEU A CD2 
2113 N N   . CYS A 296 ? 0.2878 0.2969 0.2889 -0.0244 0.0243  0.0478  282 CYS A N   
2114 C CA  . CYS A 296 ? 0.2835 0.2908 0.2804 -0.0223 0.0239  0.0419  282 CYS A CA  
2115 C C   . CYS A 296 ? 0.2783 0.2902 0.2675 -0.0216 0.0259  0.0381  282 CYS A C   
2116 O O   . CYS A 296 ? 0.2606 0.2718 0.2503 -0.0222 0.0270  0.0348  282 CYS A O   
2117 C CB  . CYS A 296 ? 0.2591 0.2595 0.2610 -0.0221 0.0230  0.0367  282 CYS A CB  
2118 S SG  . CYS A 296 ? 0.3070 0.3015 0.3200 -0.0224 0.0204  0.0394  282 CYS A SG  
2119 N N   . ILE A 297 ? 0.2798 0.2963 0.2626 -0.0205 0.0261  0.0385  283 ILE A N   
2120 C CA  . ILE A 297 ? 0.2736 0.2953 0.2501 -0.0198 0.0279  0.0351  283 ILE A CA  
2121 C C   . ILE A 297 ? 0.2638 0.2836 0.2369 -0.0179 0.0267  0.0296  283 ILE A C   
2122 O O   . ILE A 297 ? 0.2736 0.2936 0.2443 -0.0169 0.0252  0.0305  283 ILE A O   
2123 C CB  . ILE A 297 ? 0.2806 0.3102 0.2519 -0.0202 0.0292  0.0390  283 ILE A CB  
2124 C CG1 . ILE A 297 ? 0.2730 0.3051 0.2480 -0.0226 0.0297  0.0464  283 ILE A CG1 
2125 C CG2 . ILE A 297 ? 0.2768 0.3121 0.2434 -0.0194 0.0315  0.0344  283 ILE A CG2 
2126 C CD1 . ILE A 297 ? 0.2628 0.2945 0.2427 -0.0240 0.0315  0.0466  283 ILE A CD1 
2127 N N   . GLY A 298 ? 0.2712 0.2893 0.2445 -0.0176 0.0270  0.0245  284 GLY A N   
2128 C CA  . GLY A 298 ? 0.2689 0.2859 0.2394 -0.0162 0.0256  0.0197  284 GLY A CA  
2129 C C   . GLY A 298 ? 0.2771 0.2895 0.2494 -0.0157 0.0238  0.0192  284 GLY A C   
2130 O O   . GLY A 298 ? 0.2588 0.2717 0.2284 -0.0144 0.0225  0.0176  284 GLY A O   
2131 N N   . THR A 299 ? 0.2942 0.3023 0.2718 -0.0168 0.0237  0.0201  285 THR A N   
2132 C CA  . THR A 299 ? 0.2978 0.3020 0.2788 -0.0163 0.0224  0.0197  285 THR A CA  
2133 C C   . THR A 299 ? 0.3262 0.3274 0.3084 -0.0169 0.0222  0.0145  285 THR A C   
2134 O O   . THR A 299 ? 0.2853 0.2860 0.2675 -0.0184 0.0228  0.0126  285 THR A O   
2135 C CB  . THR A 299 ? 0.2932 0.2950 0.2805 -0.0171 0.0222  0.0239  285 THR A CB  
2136 O OG1 . THR A 299 ? 0.3213 0.3222 0.3110 -0.0189 0.0233  0.0241  285 THR A OG1 
2137 C CG2 . THR A 299 ? 0.2932 0.2985 0.2795 -0.0169 0.0216  0.0300  285 THR A CG2 
2138 N N   . ARG A 300 ? 0.2867 0.2866 0.2696 -0.0159 0.0214  0.0125  286 ARG A N   
2139 C CA  . ARG A 300 ? 0.2984 0.2963 0.2825 -0.0168 0.0214  0.0078  286 ARG A CA  
2140 C C   . ARG A 300 ? 0.3003 0.2959 0.2899 -0.0159 0.0212  0.0072  286 ARG A C   
2141 O O   . ARG A 300 ? 0.2554 0.2521 0.2452 -0.0142 0.0203  0.0082  286 ARG A O   
2142 C CB  . ARG A 300 ? 0.3033 0.3035 0.2827 -0.0167 0.0207  0.0051  286 ARG A CB  
2143 C CG  . ARG A 300 ? 0.3250 0.3272 0.3010 -0.0175 0.0206  0.0050  286 ARG A CG  
2144 C CD  . ARG A 300 ? 0.3494 0.3500 0.3273 -0.0199 0.0212  0.0038  286 ARG A CD  
2145 N NE  . ARG A 300 ? 0.3573 0.3598 0.3341 -0.0204 0.0213  0.0048  286 ARG A NE  
2146 C CZ  . ARG A 300 ? 0.3840 0.3879 0.3593 -0.0211 0.0201  0.0030  286 ARG A CZ  
2147 N NH1 . ARG A 300 ? 0.3613 0.3654 0.3353 -0.0217 0.0186  0.0008  286 ARG A NH1 
2148 N NH2 . ARG A 300 ? 0.3770 0.3827 0.3531 -0.0214 0.0203  0.0037  286 ARG A NH2 
2149 N N   . PHE A 301 ? 0.2825 0.2751 0.2774 -0.0170 0.0218  0.0055  287 PHE A N   
2150 C CA  . PHE A 301 ? 0.2915 0.2818 0.2939 -0.0160 0.0216  0.0047  287 PHE A CA  
2151 C C   . PHE A 301 ? 0.2991 0.2901 0.3014 -0.0160 0.0224  -0.0009 287 PHE A C   
2152 O O   . PHE A 301 ? 0.2753 0.2653 0.2800 -0.0174 0.0235  -0.0056 287 PHE A O   
2153 C CB  . PHE A 301 ? 0.2888 0.2755 0.2978 -0.0170 0.0217  0.0048  287 PHE A CB  
2154 C CG  . PHE A 301 ? 0.3060 0.2924 0.3168 -0.0171 0.0208  0.0114  287 PHE A CG  
2155 C CD1 . PHE A 301 ? 0.3174 0.3034 0.3332 -0.0157 0.0192  0.0162  287 PHE A CD1 
2156 C CD2 . PHE A 301 ? 0.3226 0.3097 0.3303 -0.0187 0.0214  0.0132  287 PHE A CD2 
2157 C CE1 . PHE A 301 ? 0.2978 0.2845 0.3148 -0.0164 0.0183  0.0230  287 PHE A CE1 
2158 C CE2 . PHE A 301 ? 0.3320 0.3200 0.3413 -0.0190 0.0209  0.0195  287 PHE A CE2 
2159 C CZ  . PHE A 301 ? 0.3067 0.2947 0.3203 -0.0180 0.0193  0.0245  287 PHE A CZ  
2160 N N   . THR A 302 ? 0.2804 0.2740 0.2798 -0.0147 0.0217  -0.0005 288 THR A N   
2161 C CA  . THR A 302 ? 0.2829 0.2783 0.2823 -0.0149 0.0225  -0.0051 288 THR A CA  
2162 C C   . THR A 302 ? 0.3012 0.2953 0.3095 -0.0134 0.0229  -0.0071 288 THR A C   
2163 O O   . THR A 302 ? 0.2553 0.2469 0.2700 -0.0120 0.0218  -0.0040 288 THR A O   
2164 C CB  . THR A 302 ? 0.2769 0.2754 0.2708 -0.0141 0.0213  -0.0039 288 THR A CB  
2165 O OG1 . THR A 302 ? 0.2787 0.2772 0.2761 -0.0117 0.0200  -0.0012 288 THR A OG1 
2166 C CG2 . THR A 302 ? 0.2968 0.2963 0.2841 -0.0147 0.0204  -0.0013 288 THR A CG2 
2167 N N   . ASP A 303 ? 0.2862 0.2825 0.2956 -0.0139 0.0244  -0.0122 289 ASP A N   
2168 C CA  . ASP A 303 ? 0.2902 0.2859 0.3094 -0.0124 0.0252  -0.0154 289 ASP A CA  
2169 C C   . ASP A 303 ? 0.3024 0.2976 0.3265 -0.0096 0.0231  -0.0110 289 ASP A C   
2170 O O   . ASP A 303 ? 0.3232 0.3155 0.3567 -0.0081 0.0222  -0.0098 289 ASP A O   
2171 C CB  . ASP A 303 ? 0.2911 0.2908 0.3099 -0.0136 0.0276  -0.0218 289 ASP A CB  
2172 C CG  . ASP A 303 ? 0.2707 0.2746 0.2834 -0.0138 0.0271  -0.0205 289 ASP A CG  
2173 O OD1 . ASP A 303 ? 0.2905 0.2941 0.2979 -0.0133 0.0249  -0.0156 289 ASP A OD1 
2174 O OD2 . ASP A 303 ? 0.3114 0.3194 0.3249 -0.0147 0.0289  -0.0247 289 ASP A OD2 
2175 N N   . THR A 304 ? 0.2869 0.2846 0.3049 -0.0091 0.0218  -0.0082 290 THR A N   
2176 C CA  . THR A 304 ? 0.3433 0.3409 0.3649 -0.0069 0.0194  -0.0038 290 THR A CA  
2177 C C   . THR A 304 ? 0.3379 0.3327 0.3604 -0.0064 0.0173  0.0023  290 THR A C   
2178 O O   . THR A 304 ? 0.3864 0.3798 0.4164 -0.0050 0.0153  0.0057  290 THR A O   
2179 C CB  . THR A 304 ? 0.3634 0.3643 0.3772 -0.0069 0.0182  -0.0024 290 THR A CB  
2180 O OG1 . THR A 304 ? 0.3860 0.3900 0.4006 -0.0074 0.0198  -0.0070 290 THR A OG1 
2181 C CG2 . THR A 304 ? 0.4085 0.4093 0.4234 -0.0051 0.0152  0.0029  290 THR A CG2 
2182 N N   . LEU A 305 ? 0.3146 0.3090 0.3301 -0.0079 0.0176  0.0041  291 LEU A N   
2183 C CA  . LEU A 305 ? 0.3251 0.3183 0.3403 -0.0079 0.0159  0.0103  291 LEU A CA  
2184 C C   . LEU A 305 ? 0.3192 0.3088 0.3443 -0.0080 0.0156  0.0114  291 LEU A C   
2185 O O   . LEU A 305 ? 0.3170 0.3058 0.3443 -0.0081 0.0137  0.0175  291 LEU A O   
2186 C CB  . LEU A 305 ? 0.2820 0.2767 0.2877 -0.0093 0.0167  0.0113  291 LEU A CB  
2187 C CG  . LEU A 305 ? 0.2990 0.2970 0.2966 -0.0088 0.0153  0.0142  291 LEU A CG  
2188 C CD1 . LEU A 305 ? 0.3074 0.3072 0.3034 -0.0079 0.0147  0.0115  291 LEU A CD1 
2189 C CD2 . LEU A 305 ? 0.2714 0.2710 0.2616 -0.0101 0.0165  0.0139  291 LEU A CD2 
2190 N N   . THR A 306 ? 0.3161 0.3038 0.3474 -0.0082 0.0174  0.0056  292 THR A N   
2191 C CA  . THR A 306 ? 0.3104 0.2942 0.3518 -0.0084 0.0169  0.0057  292 THR A CA  
2192 C C   . THR A 306 ? 0.3453 0.3275 0.3992 -0.0068 0.0170  0.0014  292 THR A C   
2193 O O   . THR A 306 ? 0.3275 0.3065 0.3908 -0.0068 0.0171  -0.0014 292 THR A O   
2194 C CB  . THR A 306 ? 0.3205 0.3031 0.3586 -0.0105 0.0189  0.0021  292 THR A CB  
2195 O OG1 . THR A 306 ? 0.3245 0.3091 0.3590 -0.0112 0.0214  -0.0052 292 THR A OG1 
2196 C CG2 . THR A 306 ? 0.2940 0.2782 0.3221 -0.0119 0.0188  0.0066  292 THR A CG2 
2197 N N   . ALA A 307 ? 0.3447 0.3294 0.3996 -0.0052 0.0167  0.0005  293 ALA A N   
2198 C CA  . ALA A 307 ? 0.3898 0.3740 0.4571 -0.0035 0.0171  -0.0042 293 ALA A CA  
2199 C C   . ALA A 307 ? 0.3696 0.3537 0.4397 -0.0043 0.0205  -0.0132 293 ALA A C   
2200 O O   . ALA A 307 ? 0.3838 0.3649 0.4659 -0.0036 0.0205  -0.0166 293 ALA A O   
2201 C CB  . ALA A 307 ? 0.3962 0.3768 0.4772 -0.0020 0.0136  0.0007  293 ALA A CB  
2202 N N   . GLY A 308 ? 0.3673 0.3546 0.4261 -0.0061 0.0232  -0.0170 294 GLY A N   
2203 C CA  . GLY A 308 ? 0.3516 0.3398 0.4106 -0.0077 0.0264  -0.0253 294 GLY A CA  
2204 C C   . GLY A 308 ? 0.3395 0.3241 0.3988 -0.0094 0.0262  -0.0260 294 GLY A C   
2205 O O   . GLY A 308 ? 0.3311 0.3142 0.3979 -0.0097 0.0276  -0.0324 294 GLY A O   
2206 N N   . PHE A 309 ? 0.3432 0.3263 0.3949 -0.0105 0.0247  -0.0197 295 PHE A N   
2207 C CA  . PHE A 309 ? 0.3358 0.3158 0.3869 -0.0124 0.0244  -0.0195 295 PHE A CA  
2208 C C   . PHE A 309 ? 0.3449 0.3201 0.4102 -0.0113 0.0227  -0.0194 295 PHE A C   
2209 O O   . PHE A 309 ? 0.3332 0.3059 0.4023 -0.0126 0.0232  -0.0236 295 PHE A O   
2210 C CB  . PHE A 309 ? 0.3218 0.3037 0.3665 -0.0151 0.0270  -0.0265 295 PHE A CB  
2211 C CG  . PHE A 309 ? 0.3296 0.3163 0.3622 -0.0165 0.0281  -0.0266 295 PHE A CG  
2212 C CD1 . PHE A 309 ? 0.3108 0.2982 0.3348 -0.0170 0.0268  -0.0205 295 PHE A CD1 
2213 C CD2 . PHE A 309 ? 0.3161 0.3072 0.3467 -0.0175 0.0305  -0.0331 295 PHE A CD2 
2214 C CE1 . PHE A 309 ? 0.2796 0.2711 0.2942 -0.0182 0.0272  -0.0206 295 PHE A CE1 
2215 C CE2 . PHE A 309 ? 0.3194 0.3150 0.3398 -0.0191 0.0310  -0.0325 295 PHE A CE2 
2216 C CZ  . PHE A 309 ? 0.2879 0.2832 0.3007 -0.0194 0.0291  -0.0262 295 PHE A CZ  
2217 N N   . THR A 310 ? 0.3447 0.3185 0.4185 -0.0091 0.0203  -0.0144 296 THR A N   
2218 C CA  . THR A 310 ? 0.3388 0.3078 0.4273 -0.0082 0.0177  -0.0126 296 THR A CA  
2219 C C   . THR A 310 ? 0.3435 0.3106 0.4312 -0.0091 0.0146  -0.0026 296 THR A C   
2220 O O   . THR A 310 ? 0.3487 0.3124 0.4488 -0.0084 0.0115  0.0017  296 THR A O   
2221 C CB  . THR A 310 ? 0.3330 0.3017 0.4342 -0.0054 0.0164  -0.0135 296 THR A CB  
2222 O OG1 . THR A 310 ? 0.3647 0.3366 0.4597 -0.0045 0.0154  -0.0078 296 THR A OG1 
2223 C CG2 . THR A 310 ? 0.3478 0.3183 0.4536 -0.0047 0.0198  -0.0247 296 THR A CG2 
2224 N N   . HIS A 311 ? 0.3358 0.3054 0.4099 -0.0106 0.0154  0.0014  297 HIS A N   
2225 C CA  . HIS A 311 ? 0.3441 0.3130 0.4164 -0.0120 0.0134  0.0099  297 HIS A CA  
2226 C C   . HIS A 311 ? 0.3417 0.3066 0.4208 -0.0136 0.0129  0.0086  297 HIS A C   
2227 O O   . HIS A 311 ? 0.3506 0.3145 0.4291 -0.0144 0.0149  0.0009  297 HIS A O   
2228 C CB  . HIS A 311 ? 0.3212 0.2943 0.3782 -0.0132 0.0148  0.0128  297 HIS A CB  
2229 C CG  . HIS A 311 ? 0.3409 0.3151 0.3893 -0.0145 0.0177  0.0062  297 HIS A CG  
2230 N ND1 . HIS A 311 ? 0.3317 0.3067 0.3795 -0.0142 0.0197  -0.0018 297 HIS A ND1 
2231 C CD2 . HIS A 311 ? 0.3357 0.3110 0.3763 -0.0165 0.0187  0.0069  297 HIS A CD2 
2232 C CE1 . HIS A 311 ? 0.3229 0.2993 0.3624 -0.0162 0.0214  -0.0052 297 HIS A CE1 
2233 N NE2 . HIS A 311 ? 0.3332 0.3095 0.3686 -0.0175 0.0208  -0.0001 297 HIS A NE2 
2234 N N   . GLN A 312 ? 0.3645 0.3274 0.4502 -0.0143 0.0099  0.0164  298 GLN A N   
2235 C CA  . GLN A 312 ? 0.3688 0.3277 0.4627 -0.0159 0.0087  0.0166  298 GLN A CA  
2236 C C   . GLN A 312 ? 0.3740 0.3352 0.4600 -0.0181 0.0085  0.0242  298 GLN A C   
2237 O O   . GLN A 312 ? 0.3765 0.3382 0.4667 -0.0189 0.0059  0.0333  298 GLN A O   
2238 C CB  . GLN A 312 ? 0.3820 0.3366 0.4937 -0.0149 0.0048  0.0192  298 GLN A CB  
2239 C CG  . GLN A 312 ? 0.4407 0.3936 0.5615 -0.0124 0.0053  0.0108  298 GLN A CG  
2240 C CD  . GLN A 312 ? 0.5251 0.4728 0.6663 -0.0114 0.0016  0.0109  298 GLN A CD  
2241 O OE1 . GLN A 312 ? 0.6110 0.5581 0.7621 -0.0094 -0.0006 0.0125  298 GLN A OE1 
2242 N NE2 . GLN A 312 ? 0.5696 0.5132 0.7180 -0.0128 0.0004  0.0095  298 GLN A NE2 
2243 N N   . LEU A 313 ? 0.3622 0.3252 0.4372 -0.0194 0.0113  0.0206  299 LEU A N   
2244 C CA  . LEU A 313 ? 0.3568 0.3226 0.4245 -0.0215 0.0119  0.0262  299 LEU A CA  
2245 C C   . LEU A 313 ? 0.3833 0.3474 0.4484 -0.0232 0.0134  0.0205  299 LEU A C   
2246 O O   . LEU A 313 ? 0.4138 0.3789 0.4720 -0.0231 0.0155  0.0135  299 LEU A O   
2247 C CB  . LEU A 313 ? 0.3307 0.3023 0.3852 -0.0210 0.0137  0.0287  299 LEU A CB  
2248 C CG  . LEU A 313 ? 0.3562 0.3305 0.4105 -0.0199 0.0121  0.0354  299 LEU A CG  
2249 C CD1 . LEU A 313 ? 0.3409 0.3208 0.3819 -0.0194 0.0140  0.0357  299 LEU A CD1 
2250 C CD2 . LEU A 313 ? 0.3518 0.3265 0.4124 -0.0215 0.0096  0.0449  299 LEU A CD2 
2251 N N   . THR A 314 ? 0.3759 0.3378 0.4470 -0.0251 0.0120  0.0238  300 THR A N   
2252 C CA  . THR A 314 ? 0.3689 0.3288 0.4391 -0.0270 0.0127  0.0187  300 THR A CA  
2253 C C   . THR A 314 ? 0.3884 0.3523 0.4490 -0.0287 0.0142  0.0224  300 THR A C   
2254 O O   . THR A 314 ? 0.3644 0.3325 0.4210 -0.0285 0.0147  0.0292  300 THR A O   
2255 C CB  . THR A 314 ? 0.3812 0.3357 0.4649 -0.0281 0.0099  0.0195  300 THR A CB  
2256 O OG1 . THR A 314 ? 0.4186 0.3745 0.5052 -0.0296 0.0084  0.0292  300 THR A OG1 
2257 C CG2 . THR A 314 ? 0.3825 0.3333 0.4784 -0.0261 0.0079  0.0174  300 THR A CG2 
2258 N N   . PRO A 315 ? 0.4027 0.3659 0.4596 -0.0305 0.0151  0.0175  301 PRO A N   
2259 C CA  . PRO A 315 ? 0.3775 0.3444 0.4273 -0.0320 0.0163  0.0210  301 PRO A CA  
2260 C C   . PRO A 315 ? 0.3700 0.3380 0.4253 -0.0333 0.0153  0.0293  301 PRO A C   
2261 O O   . PRO A 315 ? 0.3735 0.3467 0.4234 -0.0334 0.0167  0.0345  301 PRO A O   
2262 C CB  . PRO A 315 ? 0.4154 0.3804 0.4630 -0.0341 0.0163  0.0143  301 PRO A CB  
2263 C CG  . PRO A 315 ? 0.4203 0.3829 0.4684 -0.0332 0.0165  0.0065  301 PRO A CG  
2264 C CD  . PRO A 315 ? 0.4347 0.3949 0.4919 -0.0311 0.0153  0.0083  301 PRO A CD  
2265 N N   . SER A 316 ? 0.3497 0.3132 0.4161 -0.0344 0.0129  0.0308  302 SER A N   
2266 C CA  . SER A 316 ? 0.3811 0.3460 0.4531 -0.0361 0.0118  0.0395  302 SER A CA  
2267 C C   . SER A 316 ? 0.3908 0.3594 0.4637 -0.0352 0.0115  0.0475  302 SER A C   
2268 O O   . SER A 316 ? 0.3895 0.3623 0.4630 -0.0367 0.0117  0.0555  302 SER A O   
2269 C CB  . SER A 316 ? 0.3975 0.3564 0.4821 -0.0377 0.0086  0.0392  302 SER A CB  
2270 O OG  . SER A 316 ? 0.4626 0.4171 0.5566 -0.0363 0.0063  0.0382  302 SER A OG  
2271 N N   . GLN A 317 ? 0.3755 0.3431 0.4484 -0.0330 0.0110  0.0458  303 GLN A N   
2272 C CA  . GLN A 317 ? 0.3521 0.3235 0.4245 -0.0322 0.0104  0.0530  303 GLN A CA  
2273 C C   . GLN A 317 ? 0.3487 0.3273 0.4078 -0.0316 0.0135  0.0543  303 GLN A C   
2274 O O   . GLN A 317 ? 0.3404 0.3237 0.3975 -0.0316 0.0132  0.0609  303 GLN A O   
2275 C CB  . GLN A 317 ? 0.3543 0.3218 0.4328 -0.0300 0.0084  0.0502  303 GLN A CB  
2276 C CG  . GLN A 317 ? 0.3526 0.3230 0.4332 -0.0296 0.0065  0.0583  303 GLN A CG  
2277 C CD  . GLN A 317 ? 0.3602 0.3268 0.4472 -0.0272 0.0046  0.0548  303 GLN A CD  
2278 O OE1 . GLN A 317 ? 0.3428 0.3057 0.4308 -0.0256 0.0056  0.0456  303 GLN A OE1 
2279 N NE2 . GLN A 317 ? 0.3338 0.3017 0.4256 -0.0271 0.0019  0.0624  303 GLN A NE2 
2280 N N   . THR A 318 ? 0.3223 0.3023 0.3727 -0.0312 0.0160  0.0481  304 THR A N   
2281 C CA  . THR A 318 ? 0.3176 0.3035 0.3568 -0.0299 0.0185  0.0475  304 THR A CA  
2282 C C   . THR A 318 ? 0.3125 0.3029 0.3459 -0.0311 0.0209  0.0477  304 THR A C   
2283 O O   . THR A 318 ? 0.3088 0.2972 0.3454 -0.0327 0.0209  0.0462  304 THR A O   
2284 C CB  . THR A 318 ? 0.3378 0.3217 0.3718 -0.0279 0.0190  0.0397  304 THR A CB  
2285 O OG1 . THR A 318 ? 0.3427 0.3220 0.3789 -0.0286 0.0189  0.0330  304 THR A OG1 
2286 C CG2 . THR A 318 ? 0.3069 0.2890 0.3448 -0.0261 0.0173  0.0405  304 THR A CG2 
2287 N N   . ILE A 319 ? 0.2826 0.2795 0.3081 -0.0303 0.0228  0.0495  305 ILE A N   
2288 C CA  . ILE A 319 ? 0.2795 0.2813 0.2985 -0.0304 0.0254  0.0476  305 ILE A CA  
2289 C C   . ILE A 319 ? 0.2761 0.2797 0.2869 -0.0282 0.0262  0.0429  305 ILE A C   
2290 O O   . ILE A 319 ? 0.2788 0.2841 0.2870 -0.0270 0.0257  0.0449  305 ILE A O   
2291 C CB  . ILE A 319 ? 0.2768 0.2861 0.2953 -0.0318 0.0272  0.0543  305 ILE A CB  
2292 C CG1 . ILE A 319 ? 0.3006 0.3084 0.3280 -0.0343 0.0263  0.0593  305 ILE A CG1 
2293 C CG2 . ILE A 319 ? 0.2745 0.2899 0.2865 -0.0312 0.0302  0.0514  305 ILE A CG2 
2294 C CD1 . ILE A 319 ? 0.3131 0.3292 0.3404 -0.0361 0.0283  0.0665  305 ILE A CD1 
2295 N N   . GLU A 320 ? 0.2773 0.2804 0.2846 -0.0278 0.0269  0.0370  306 GLU A N   
2296 C CA  . GLU A 320 ? 0.2874 0.2921 0.2878 -0.0258 0.0273  0.0329  306 GLU A CA  
2297 C C   . GLU A 320 ? 0.2818 0.2912 0.2781 -0.0256 0.0289  0.0307  306 GLU A C   
2298 O O   . GLU A 320 ? 0.2761 0.2859 0.2753 -0.0270 0.0295  0.0305  306 GLU A O   
2299 C CB  . GLU A 320 ? 0.2974 0.2967 0.2978 -0.0252 0.0258  0.0274  306 GLU A CB  
2300 C CG  . GLU A 320 ? 0.2926 0.2902 0.2919 -0.0263 0.0256  0.0225  306 GLU A CG  
2301 C CD  . GLU A 320 ? 0.3036 0.2972 0.3026 -0.0262 0.0244  0.0175  306 GLU A CD  
2302 O OE1 . GLU A 320 ? 0.3278 0.3226 0.3223 -0.0250 0.0242  0.0147  306 GLU A OE1 
2303 O OE2 . GLU A 320 ? 0.2603 0.2497 0.2639 -0.0274 0.0236  0.0164  306 GLU A OE2 
2304 N N   . VAL A 321 ? 0.2570 0.2701 0.2474 -0.0238 0.0295  0.0291  307 VAL A N   
2305 C CA  . VAL A 321 ? 0.2507 0.2686 0.2382 -0.0231 0.0309  0.0262  307 VAL A CA  
2306 C C   . VAL A 321 ? 0.2897 0.3060 0.2733 -0.0216 0.0295  0.0212  307 VAL A C   
2307 O O   . VAL A 321 ? 0.2801 0.2963 0.2602 -0.0202 0.0287  0.0211  307 VAL A O   
2308 C CB  . VAL A 321 ? 0.2662 0.2918 0.2508 -0.0227 0.0332  0.0292  307 VAL A CB  
2309 C CG1 . VAL A 321 ? 0.2790 0.3094 0.2605 -0.0213 0.0344  0.0247  307 VAL A CG1 
2310 C CG2 . VAL A 321 ? 0.3123 0.3389 0.2932 -0.0219 0.0326  0.0319  307 VAL A CG2 
2311 N N   . GLN A 322 ? 0.2911 0.3060 0.2761 -0.0221 0.0287  0.0175  308 GLN A N   
2312 C CA  . GLN A 322 ? 0.2866 0.3006 0.2690 -0.0212 0.0271  0.0132  308 GLN A CA  
2313 C C   . GLN A 322 ? 0.2773 0.2960 0.2598 -0.0203 0.0277  0.0109  308 GLN A C   
2314 O O   . GLN A 322 ? 0.2753 0.2979 0.2600 -0.0205 0.0297  0.0123  308 GLN A O   
2315 C CB  . GLN A 322 ? 0.2717 0.2807 0.2562 -0.0231 0.0251  0.0112  308 GLN A CB  
2316 C CG  . GLN A 322 ? 0.2883 0.2930 0.2733 -0.0236 0.0247  0.0119  308 GLN A CG  
2317 C CD  . GLN A 322 ? 0.3131 0.3179 0.2949 -0.0217 0.0244  0.0116  308 GLN A CD  
2318 O OE1 . GLN A 322 ? 0.3081 0.3151 0.2865 -0.0203 0.0238  0.0099  308 GLN A OE1 
2319 N NE2 . GLN A 322 ? 0.2628 0.2650 0.2466 -0.0215 0.0244  0.0134  308 GLN A NE2 
2320 N N   . PRO A 323 ? 0.2906 0.3094 0.2715 -0.0192 0.0260  0.0073  309 PRO A N   
2321 C CA  . PRO A 323 ? 0.3035 0.3269 0.2857 -0.0180 0.0263  0.0045  309 PRO A CA  
2322 C C   . PRO A 323 ? 0.2858 0.3105 0.2742 -0.0191 0.0269  0.0042  309 PRO A C   
2323 O O   . PRO A 323 ? 0.2898 0.3198 0.2801 -0.0179 0.0288  0.0028  309 PRO A O   
2324 C CB  . PRO A 323 ? 0.2833 0.3047 0.2648 -0.0174 0.0232  0.0012  309 PRO A CB  
2325 C CG  . PRO A 323 ? 0.3040 0.3226 0.2809 -0.0171 0.0227  0.0026  309 PRO A CG  
2326 C CD  . PRO A 323 ? 0.2978 0.3135 0.2760 -0.0189 0.0237  0.0057  309 PRO A CD  
2327 N N   . HIS A 324 ? 0.3034 0.3240 0.2953 -0.0215 0.0254  0.0053  310 HIS A N   
2328 C CA  . HIS A 324 ? 0.2824 0.3041 0.2809 -0.0228 0.0253  0.0053  310 HIS A CA  
2329 C C   . HIS A 324 ? 0.2822 0.3018 0.2831 -0.0250 0.0261  0.0088  310 HIS A C   
2330 O O   . HIS A 324 ? 0.2771 0.2970 0.2839 -0.0265 0.0257  0.0093  310 HIS A O   
2331 C CB  . HIS A 324 ? 0.3218 0.3408 0.3236 -0.0241 0.0214  0.0031  310 HIS A CB  
2332 C CG  . HIS A 324 ? 0.3201 0.3405 0.3211 -0.0222 0.0197  -0.0002 310 HIS A CG  
2333 N ND1 . HIS A 324 ? 0.3464 0.3716 0.3504 -0.0198 0.0207  -0.0031 310 HIS A ND1 
2334 C CD2 . HIS A 324 ? 0.3245 0.3424 0.3227 -0.0225 0.0168  -0.0013 310 HIS A CD2 
2335 C CE1 . HIS A 324 ? 0.3576 0.3824 0.3608 -0.0186 0.0183  -0.0059 310 HIS A CE1 
2336 N NE2 . HIS A 324 ? 0.3477 0.3682 0.3475 -0.0203 0.0158  -0.0045 310 HIS A NE2 
2337 N N   . ALA A 325 ? 0.2536 0.2707 0.2512 -0.0254 0.0269  0.0113  311 ALA A N   
2338 C CA  . ALA A 325 ? 0.2788 0.2932 0.2797 -0.0277 0.0270  0.0143  311 ALA A CA  
2339 C C   . ALA A 325 ? 0.2636 0.2774 0.2622 -0.0272 0.0285  0.0175  311 ALA A C   
2340 O O   . ALA A 325 ? 0.2609 0.2743 0.2549 -0.0257 0.0285  0.0170  311 ALA A O   
2341 C CB  . ALA A 325 ? 0.2770 0.2859 0.2786 -0.0302 0.0240  0.0129  311 ALA A CB  
2342 N N   . SER A 326 ? 0.2637 0.2773 0.2663 -0.0287 0.0295  0.0211  312 SER A N   
2343 C CA  . SER A 326 ? 0.2666 0.2794 0.2690 -0.0287 0.0302  0.0250  312 SER A CA  
2344 C C   . SER A 326 ? 0.2620 0.2695 0.2695 -0.0310 0.0288  0.0266  312 SER A C   
2345 O O   . SER A 326 ? 0.2769 0.2831 0.2881 -0.0328 0.0278  0.0257  312 SER A O   
2346 C CB  . SER A 326 ? 0.2416 0.2613 0.2440 -0.0281 0.0331  0.0290  312 SER A CB  
2347 O OG  . SER A 326 ? 0.2491 0.2729 0.2456 -0.0259 0.0341  0.0276  312 SER A OG  
2348 N N   . ARG A 327 ? 0.2551 0.2597 0.2637 -0.0310 0.0282  0.0288  313 ARG A N   
2349 C CA  . ARG A 327 ? 0.2918 0.2908 0.3058 -0.0329 0.0265  0.0294  313 ARG A CA  
2350 C C   . ARG A 327 ? 0.2952 0.2946 0.3138 -0.0333 0.0268  0.0353  313 ARG A C   
2351 O O   . ARG A 327 ? 0.2718 0.2734 0.2884 -0.0320 0.0273  0.0380  313 ARG A O   
2352 C CB  . ARG A 327 ? 0.2824 0.2761 0.2945 -0.0326 0.0248  0.0248  313 ARG A CB  
2353 C CG  . ARG A 327 ? 0.2898 0.2779 0.3078 -0.0340 0.0232  0.0247  313 ARG A CG  
2354 C CD  . ARG A 327 ? 0.2901 0.2744 0.3065 -0.0335 0.0222  0.0193  313 ARG A CD  
2355 N NE  . ARG A 327 ? 0.3118 0.2970 0.3266 -0.0310 0.0227  0.0201  313 ARG A NE  
2356 C CZ  . ARG A 327 ? 0.3299 0.3136 0.3499 -0.0303 0.0221  0.0236  313 ARG A CZ  
2357 N NH1 . ARG A 327 ? 0.3115 0.2928 0.3389 -0.0318 0.0211  0.0267  313 ARG A NH1 
2358 N NH2 . ARG A 327 ? 0.3195 0.3040 0.3380 -0.0282 0.0222  0.0243  313 ARG A NH2 
2359 N N   . VAL A 328 ? 0.2755 0.2729 0.3009 -0.0355 0.0259  0.0378  314 VAL A N   
2360 C CA  . VAL A 328 ? 0.3018 0.2984 0.3336 -0.0365 0.0252  0.0437  314 VAL A CA  
2361 C C   . VAL A 328 ? 0.3108 0.2997 0.3488 -0.0378 0.0224  0.0413  314 VAL A C   
2362 O O   . VAL A 328 ? 0.2940 0.2807 0.3350 -0.0397 0.0215  0.0397  314 VAL A O   
2363 C CB  . VAL A 328 ? 0.3009 0.3031 0.3363 -0.0380 0.0268  0.0497  314 VAL A CB  
2364 C CG1 . VAL A 328 ? 0.2995 0.3010 0.3419 -0.0394 0.0255  0.0567  314 VAL A CG1 
2365 C CG2 . VAL A 328 ? 0.2635 0.2741 0.2926 -0.0367 0.0300  0.0506  314 VAL A CG2 
2366 N N   . GLY A 329 ? 0.3209 0.3058 0.3612 -0.0368 0.0210  0.0406  315 GLY A N   
2367 C CA  . GLY A 329 ? 0.3338 0.3117 0.3803 -0.0378 0.0185  0.0368  315 GLY A CA  
2368 C C   . GLY A 329 ? 0.3472 0.3229 0.3885 -0.0382 0.0185  0.0290  315 GLY A C   
2369 O O   . GLY A 329 ? 0.3535 0.3304 0.3880 -0.0367 0.0194  0.0250  315 GLY A O   
2370 N N   . ASP A 330 ? 0.3510 0.3240 0.3954 -0.0406 0.0171  0.0269  316 ASP A N   
2371 C CA  . ASP A 330 ? 0.3678 0.3392 0.4072 -0.0419 0.0166  0.0201  316 ASP A CA  
2372 C C   . ASP A 330 ? 0.3395 0.3151 0.3738 -0.0428 0.0174  0.0208  316 ASP A C   
2373 O O   . ASP A 330 ? 0.3153 0.2903 0.3452 -0.0443 0.0165  0.0162  316 ASP A O   
2374 C CB  . ASP A 330 ? 0.4210 0.3871 0.4662 -0.0444 0.0141  0.0168  316 ASP A CB  
2375 C CG  . ASP A 330 ? 0.4622 0.4237 0.5131 -0.0433 0.0131  0.0138  316 ASP A CG  
2376 O OD1 . ASP A 330 ? 0.4541 0.4161 0.5015 -0.0413 0.0142  0.0103  316 ASP A OD1 
2377 O OD2 . ASP A 330 ? 0.5530 0.5106 0.6130 -0.0445 0.0111  0.0149  316 ASP A OD2 
2378 N N   . VAL A 331 ? 0.3146 0.2947 0.3499 -0.0423 0.0188  0.0263  317 VAL A N   
2379 C CA  . VAL A 331 ? 0.2941 0.2779 0.3276 -0.0433 0.0193  0.0269  317 VAL A CA  
2380 C C   . VAL A 331 ? 0.2978 0.2866 0.3249 -0.0408 0.0214  0.0264  317 VAL A C   
2381 O O   . VAL A 331 ? 0.2779 0.2700 0.3040 -0.0387 0.0233  0.0294  317 VAL A O   
2382 C CB  . VAL A 331 ? 0.3194 0.3056 0.3599 -0.0446 0.0197  0.0325  317 VAL A CB  
2383 C CG1 . VAL A 331 ? 0.3249 0.3147 0.3652 -0.0456 0.0199  0.0324  317 VAL A CG1 
2384 C CG2 . VAL A 331 ? 0.3415 0.3222 0.3892 -0.0470 0.0172  0.0332  317 VAL A CG2 
2385 N N   . TRP A 332 ? 0.2584 0.2481 0.2815 -0.0413 0.0207  0.0229  318 TRP A N   
2386 C CA  . TRP A 332 ? 0.2663 0.2604 0.2846 -0.0392 0.0221  0.0219  318 TRP A CA  
2387 C C   . TRP A 332 ? 0.2894 0.2882 0.3107 -0.0393 0.0230  0.0238  318 TRP A C   
2388 O O   . TRP A 332 ? 0.2755 0.2734 0.3014 -0.0417 0.0215  0.0244  318 TRP A O   
2389 C CB  . TRP A 332 ? 0.2704 0.2626 0.2835 -0.0398 0.0203  0.0170  318 TRP A CB  
2390 C CG  . TRP A 332 ? 0.2888 0.2790 0.2980 -0.0384 0.0206  0.0147  318 TRP A CG  
2391 C CD1 . TRP A 332 ? 0.3086 0.2946 0.3181 -0.0396 0.0195  0.0119  318 TRP A CD1 
2392 C CD2 . TRP A 332 ? 0.2909 0.2835 0.2959 -0.0355 0.0219  0.0144  318 TRP A CD2 
2393 N NE1 . TRP A 332 ? 0.3035 0.2892 0.3099 -0.0375 0.0204  0.0102  318 TRP A NE1 
2394 C CE2 . TRP A 332 ? 0.3006 0.2902 0.3041 -0.0350 0.0217  0.0120  318 TRP A CE2 
2395 C CE3 . TRP A 332 ? 0.2948 0.2922 0.2977 -0.0333 0.0234  0.0157  318 TRP A CE3 
2396 C CZ2 . TRP A 332 ? 0.3123 0.3032 0.3123 -0.0325 0.0225  0.0115  318 TRP A CZ2 
2397 C CZ3 . TRP A 332 ? 0.2968 0.2953 0.2954 -0.0309 0.0241  0.0149  318 TRP A CZ3 
2398 C CH2 . TRP A 332 ? 0.3121 0.3072 0.3094 -0.0305 0.0235  0.0131  318 TRP A CH2 
2399 N N   . PHE A 333 ? 0.2890 0.2932 0.3083 -0.0369 0.0254  0.0246  319 PHE A N   
2400 C CA  . PHE A 333 ? 0.2825 0.2924 0.3051 -0.0363 0.0269  0.0254  319 PHE A CA  
2401 C C   . PHE A 333 ? 0.2762 0.2884 0.2949 -0.0344 0.0267  0.0215  319 PHE A C   
2402 O O   . PHE A 333 ? 0.2709 0.2857 0.2850 -0.0320 0.0284  0.0209  319 PHE A O   
2403 C CB  . PHE A 333 ? 0.2567 0.2722 0.2810 -0.0353 0.0303  0.0296  319 PHE A CB  
2404 C CG  . PHE A 333 ? 0.2571 0.2703 0.2857 -0.0372 0.0301  0.0342  319 PHE A CG  
2405 C CD1 . PHE A 333 ? 0.2697 0.2791 0.2963 -0.0371 0.0293  0.0356  319 PHE A CD1 
2406 C CD2 . PHE A 333 ? 0.2583 0.2731 0.2942 -0.0392 0.0303  0.0373  319 PHE A CD2 
2407 C CE1 . PHE A 333 ? 0.2695 0.2763 0.3016 -0.0388 0.0285  0.0397  319 PHE A CE1 
2408 C CE2 . PHE A 333 ? 0.2713 0.2837 0.3120 -0.0411 0.0296  0.0417  319 PHE A CE2 
2409 C CZ  . PHE A 333 ? 0.2777 0.2859 0.3167 -0.0409 0.0286  0.0429  319 PHE A CZ  
2410 N N   . THR A 334 ? 0.2749 0.2860 0.2960 -0.0357 0.0242  0.0193  320 THR A N   
2411 C CA  . THR A 334 ? 0.2691 0.2811 0.2875 -0.0344 0.0229  0.0157  320 THR A CA  
2412 C C   . THR A 334 ? 0.2763 0.2939 0.3000 -0.0329 0.0240  0.0147  320 THR A C   
2413 O O   . THR A 334 ? 0.2821 0.3023 0.3125 -0.0336 0.0250  0.0163  320 THR A O   
2414 C CB  . THR A 334 ? 0.2723 0.2797 0.2899 -0.0371 0.0189  0.0141  320 THR A CB  
2415 O OG1 . THR A 334 ? 0.2664 0.2735 0.2906 -0.0396 0.0167  0.0152  320 THR A OG1 
2416 C CG2 . THR A 334 ? 0.2800 0.2827 0.2933 -0.0385 0.0184  0.0142  320 THR A CG2 
2417 N N   . GLY A 335 ? 0.2778 0.2973 0.2991 -0.0307 0.0237  0.0115  321 GLY A N   
2418 C CA  . GLY A 335 ? 0.2682 0.2935 0.2945 -0.0286 0.0252  0.0093  321 GLY A CA  
2419 C C   . GLY A 335 ? 0.3011 0.3325 0.3255 -0.0264 0.0300  0.0100  321 GLY A C   
2420 O O   . GLY A 335 ? 0.3006 0.3378 0.3309 -0.0256 0.0324  0.0092  321 GLY A O   
2421 N N   . ILE A 336 ? 0.2729 0.3037 0.2898 -0.0257 0.0314  0.0115  322 ILE A N   
2422 C CA  . ILE A 336 ? 0.2801 0.3172 0.2938 -0.0241 0.0355  0.0126  322 ILE A CA  
2423 C C   . ILE A 336 ? 0.2916 0.3296 0.2980 -0.0218 0.0354  0.0099  322 ILE A C   
2424 O O   . ILE A 336 ? 0.2843 0.3174 0.2856 -0.0221 0.0336  0.0108  322 ILE A O   
2425 C CB  . ILE A 336 ? 0.2867 0.3231 0.2991 -0.0258 0.0370  0.0182  322 ILE A CB  
2426 C CG1 . ILE A 336 ? 0.3055 0.3420 0.3259 -0.0280 0.0372  0.0208  322 ILE A CG1 
2427 C CG2 . ILE A 336 ? 0.2932 0.3365 0.3010 -0.0246 0.0406  0.0202  322 ILE A CG2 
2428 C CD1 . ILE A 336 ? 0.2795 0.3148 0.3006 -0.0299 0.0380  0.0265  322 ILE A CD1 
2429 N N   . PRO A 337 ? 0.2916 0.3359 0.2977 -0.0196 0.0373  0.0063  323 PRO A N   
2430 C CA  . PRO A 337 ? 0.2916 0.3370 0.2905 -0.0176 0.0371  0.0038  323 PRO A CA  
2431 C C   . PRO A 337 ? 0.2943 0.3405 0.2859 -0.0180 0.0386  0.0081  323 PRO A C   
2432 O O   . PRO A 337 ? 0.2872 0.3379 0.2788 -0.0190 0.0416  0.0119  323 PRO A O   
2433 C CB  . PRO A 337 ? 0.3049 0.3583 0.3059 -0.0155 0.0396  -0.0011 323 PRO A CB  
2434 C CG  . PRO A 337 ? 0.3441 0.3977 0.3554 -0.0161 0.0392  -0.0025 323 PRO A CG  
2435 C CD  . PRO A 337 ? 0.3022 0.3526 0.3155 -0.0189 0.0393  0.0033  323 PRO A CD  
2436 N N   . MET A 338 ? 0.2719 0.3143 0.2579 -0.0172 0.0365  0.0078  324 MET A N   
2437 C CA  . MET A 338 ? 0.2760 0.3185 0.2562 -0.0175 0.0370  0.0120  324 MET A CA  
2438 C C   . MET A 338 ? 0.2666 0.3179 0.2429 -0.0172 0.0404  0.0133  324 MET A C   
2439 O O   . MET A 338 ? 0.2400 0.2932 0.2144 -0.0186 0.0416  0.0189  324 MET A O   
2440 C CB  . MET A 338 ? 0.2671 0.3055 0.2428 -0.0163 0.0342  0.0102  324 MET A CB  
2441 C CG  . MET A 338 ? 0.3053 0.3439 0.2755 -0.0163 0.0341  0.0140  324 MET A CG  
2442 S SD  . MET A 338 ? 0.3444 0.3780 0.3111 -0.0148 0.0306  0.0113  324 MET A SD  
2443 C CE  . MET A 338 ? 0.3039 0.3393 0.2722 -0.0133 0.0298  0.0046  324 MET A CE  
2444 N N   . LEU A 339 ? 0.3111 0.3685 0.2867 -0.0155 0.0419  0.0082  325 LEU A N   
2445 C CA  . LEU A 339 ? 0.3059 0.3730 0.2772 -0.0155 0.0456  0.0086  325 LEU A CA  
2446 C C   . LEU A 339 ? 0.2824 0.3543 0.2573 -0.0176 0.0489  0.0133  325 LEU A C   
2447 O O   . LEU A 339 ? 0.2983 0.3752 0.2690 -0.0192 0.0507  0.0186  325 LEU A O   
2448 C CB  . LEU A 339 ? 0.3157 0.3885 0.2874 -0.0133 0.0468  0.0008  325 LEU A CB  
2449 C CG  . LEU A 339 ? 0.3615 0.4461 0.3293 -0.0135 0.0514  0.0000  325 LEU A CG  
2450 C CD1 . LEU A 339 ? 0.3595 0.4473 0.3170 -0.0144 0.0514  0.0039  325 LEU A CD1 
2451 C CD2 . LEU A 339 ? 0.3906 0.4812 0.3611 -0.0111 0.0530  -0.0090 325 LEU A CD2 
2452 N N   . GLN A 340 ? 0.2790 0.3498 0.2622 -0.0179 0.0494  0.0119  326 GLN A N   
2453 C CA  . GLN A 340 ? 0.2976 0.3731 0.2852 -0.0200 0.0525  0.0165  326 GLN A CA  
2454 C C   . GLN A 340 ? 0.2731 0.3429 0.2611 -0.0224 0.0508  0.0241  326 GLN A C   
2455 O O   . GLN A 340 ? 0.2813 0.3560 0.2698 -0.0245 0.0530  0.0299  326 GLN A O   
2456 C CB  . GLN A 340 ? 0.3114 0.3870 0.3088 -0.0198 0.0531  0.0132  326 GLN A CB  
2457 C CG  . GLN A 340 ? 0.3497 0.4300 0.3501 -0.0173 0.0541  0.0051  326 GLN A CG  
2458 C CD  . GLN A 340 ? 0.4183 0.4996 0.4301 -0.0175 0.0548  0.0032  326 GLN A CD  
2459 O OE1 . GLN A 340 ? 0.4305 0.5046 0.4482 -0.0174 0.0510  0.0017  326 GLN A OE1 
2460 N NE2 . GLN A 340 ? 0.4224 0.5134 0.4376 -0.0180 0.0595  0.0036  326 GLN A NE2 
2461 N N   . ALA A 341 ? 0.2840 0.3439 0.2726 -0.0223 0.0468  0.0242  327 ALA A N   
2462 C CA  . ALA A 341 ? 0.2579 0.3124 0.2473 -0.0242 0.0451  0.0305  327 ALA A CA  
2463 C C   . ALA A 341 ? 0.2662 0.3247 0.2495 -0.0248 0.0457  0.0354  327 ALA A C   
2464 O O   . ALA A 341 ? 0.2541 0.3136 0.2395 -0.0270 0.0460  0.0421  327 ALA A O   
2465 C CB  . ALA A 341 ? 0.2384 0.2827 0.2285 -0.0238 0.0411  0.0285  327 ALA A CB  
2466 N N   . ILE A 342 ? 0.2811 0.3420 0.2574 -0.0231 0.0455  0.0324  328 ILE A N   
2467 C CA  . ILE A 342 ? 0.2759 0.3411 0.2458 -0.0239 0.0456  0.0372  328 ILE A CA  
2468 C C   . ILE A 342 ? 0.2927 0.3692 0.2610 -0.0258 0.0495  0.0408  328 ILE A C   
2469 O O   . ILE A 342 ? 0.2514 0.3308 0.2186 -0.0282 0.0495  0.0484  328 ILE A O   
2470 C CB  . ILE A 342 ? 0.2931 0.3584 0.2559 -0.0217 0.0442  0.0326  328 ILE A CB  
2471 C CG1 . ILE A 342 ? 0.2875 0.3424 0.2518 -0.0206 0.0402  0.0312  328 ILE A CG1 
2472 C CG2 . ILE A 342 ? 0.2574 0.3296 0.2128 -0.0229 0.0447  0.0371  328 ILE A CG2 
2473 C CD1 . ILE A 342 ? 0.2867 0.3409 0.2459 -0.0183 0.0386  0.0258  328 ILE A CD1 
2474 N N   . GLU A 343 ? 0.2922 0.3757 0.2606 -0.0249 0.0529  0.0354  329 GLU A N   
2475 C CA  . GLU A 343 ? 0.2790 0.3745 0.2461 -0.0267 0.0574  0.0381  329 GLU A CA  
2476 C C   . GLU A 343 ? 0.2896 0.3849 0.2633 -0.0297 0.0579  0.0460  329 GLU A C   
2477 O O   . GLU A 343 ? 0.2853 0.3882 0.2567 -0.0325 0.0596  0.0529  329 GLU A O   
2478 C CB  . GLU A 343 ? 0.2786 0.3809 0.2479 -0.0249 0.0610  0.0300  329 GLU A CB  
2479 C CG  . GLU A 343 ? 0.3246 0.4285 0.2883 -0.0221 0.0607  0.0218  329 GLU A CG  
2480 C CD  . GLU A 343 ? 0.3637 0.4747 0.3314 -0.0202 0.0643  0.0135  329 GLU A CD  
2481 O OE1 . GLU A 343 ? 0.3805 0.4894 0.3577 -0.0200 0.0649  0.0122  329 GLU A OE1 
2482 O OE2 . GLU A 343 ? 0.4010 0.5198 0.3630 -0.0191 0.0664  0.0081  329 GLU A OE2 
2483 N N   . THR A 344 ? 0.2705 0.3576 0.2526 -0.0295 0.0562  0.0453  330 THR A N   
2484 C CA  . THR A 344 ? 0.2557 0.3412 0.2451 -0.0322 0.0559  0.0523  330 THR A CA  
2485 C C   . THR A 344 ? 0.2690 0.3509 0.2571 -0.0343 0.0530  0.0605  330 THR A C   
2486 O O   . THR A 344 ? 0.2826 0.3694 0.2732 -0.0373 0.0538  0.0683  330 THR A O   
2487 C CB  . THR A 344 ? 0.2740 0.3499 0.2714 -0.0315 0.0536  0.0492  330 THR A CB  
2488 O OG1 . THR A 344 ? 0.2777 0.3574 0.2781 -0.0300 0.0560  0.0427  330 THR A OG1 
2489 C CG2 . THR A 344 ? 0.2813 0.3547 0.2864 -0.0344 0.0527  0.0562  330 THR A CG2 
2490 N N   . LEU A 345 ? 0.2777 0.3509 0.2634 -0.0328 0.0492  0.0590  331 LEU A N   
2491 C CA  . LEU A 345 ? 0.2821 0.3511 0.2689 -0.0344 0.0458  0.0662  331 LEU A CA  
2492 C C   . LEU A 345 ? 0.2708 0.3489 0.2508 -0.0361 0.0467  0.0720  331 LEU A C   
2493 O O   . LEU A 345 ? 0.2605 0.3390 0.2434 -0.0389 0.0448  0.0807  331 LEU A O   
2494 C CB  . LEU A 345 ? 0.2391 0.2974 0.2255 -0.0322 0.0420  0.0624  331 LEU A CB  
2495 C CG  . LEU A 345 ? 0.2761 0.3247 0.2694 -0.0314 0.0402  0.0584  331 LEU A CG  
2496 C CD1 . LEU A 345 ? 0.2461 0.2867 0.2374 -0.0292 0.0372  0.0538  331 LEU A CD1 
2497 C CD2 . LEU A 345 ? 0.2493 0.2941 0.2514 -0.0339 0.0387  0.0644  331 LEU A CD2 
2498 N N   . VAL A 346 ? 0.2810 0.3666 0.2523 -0.0349 0.0492  0.0675  332 VAL A N   
2499 C CA  . VAL A 346 ? 0.3060 0.4017 0.2696 -0.0371 0.0502  0.0728  332 VAL A CA  
2500 C C   . VAL A 346 ? 0.3072 0.4125 0.2735 -0.0409 0.0532  0.0800  332 VAL A C   
2501 O O   . VAL A 346 ? 0.3057 0.4149 0.2714 -0.0443 0.0518  0.0895  332 VAL A O   
2502 C CB  . VAL A 346 ? 0.3222 0.4249 0.2761 -0.0351 0.0526  0.0652  332 VAL A CB  
2503 C CG1 . VAL A 346 ? 0.3320 0.4472 0.2773 -0.0381 0.0544  0.0704  332 VAL A CG1 
2504 C CG2 . VAL A 346 ? 0.2953 0.3893 0.2464 -0.0321 0.0490  0.0601  332 VAL A CG2 
2505 N N   . GLU A 347 ? 0.3307 0.4398 0.3010 -0.0405 0.0571  0.0761  333 GLU A N   
2506 C CA  . GLU A 347 ? 0.3556 0.4742 0.3296 -0.0440 0.0603  0.0827  333 GLU A CA  
2507 C C   . GLU A 347 ? 0.3247 0.4368 0.3075 -0.0468 0.0566  0.0925  333 GLU A C   
2508 O O   . GLU A 347 ? 0.3094 0.4284 0.2922 -0.0508 0.0564  0.1022  333 GLU A O   
2509 C CB  . GLU A 347 ? 0.4058 0.5277 0.3849 -0.0426 0.0645  0.0760  333 GLU A CB  
2510 C CG  . GLU A 347 ? 0.4990 0.6358 0.4778 -0.0453 0.0700  0.0788  333 GLU A CG  
2511 C CD  . GLU A 347 ? 0.7924 0.9415 0.7601 -0.0477 0.0720  0.0824  333 GLU A CD  
2512 O OE1 . GLU A 347 ? 0.6676 0.8259 0.6354 -0.0520 0.0735  0.0917  333 GLU A OE1 
2513 O OE2 . GLU A 347 ? 0.6016 0.7516 0.5605 -0.0454 0.0719  0.0761  333 GLU A OE2 
2514 N N   . LEU A 348 ? 0.2719 0.3709 0.2623 -0.0450 0.0532  0.0900  334 LEU A N   
2515 C CA  . LEU A 348 ? 0.2856 0.3777 0.2856 -0.0473 0.0494  0.0978  334 LEU A CA  
2516 C C   . LEU A 348 ? 0.2864 0.3765 0.2850 -0.0490 0.0452  0.1055  334 LEU A C   
2517 O O   . LEU A 348 ? 0.2821 0.3722 0.2876 -0.0523 0.0428  0.1150  334 LEU A O   
2518 C CB  . LEU A 348 ? 0.2531 0.3320 0.2604 -0.0450 0.0467  0.0921  334 LEU A CB  
2519 C CG  . LEU A 348 ? 0.2542 0.3339 0.2655 -0.0441 0.0497  0.0864  334 LEU A CG  
2520 C CD1 . LEU A 348 ? 0.2781 0.3449 0.2940 -0.0418 0.0465  0.0801  334 LEU A CD1 
2521 C CD2 . LEU A 348 ? 0.3268 0.4124 0.3457 -0.0475 0.0514  0.0934  334 LEU A CD2 
2522 N N   . CYS A 349 ? 0.2723 0.3598 0.2636 -0.0468 0.0436  0.1016  335 CYS A N   
2523 C CA  . CYS A 349 ? 0.2868 0.3730 0.2774 -0.0484 0.0394  0.1090  335 CYS A CA  
2524 C C   . CYS A 349 ? 0.3015 0.4012 0.2868 -0.0526 0.0409  0.1180  335 CYS A C   
2525 O O   . CYS A 349 ? 0.2870 0.3870 0.2771 -0.0560 0.0374  0.1285  335 CYS A O   
2526 C CB  . CYS A 349 ? 0.2810 0.3623 0.2649 -0.0450 0.0376  0.1025  335 CYS A CB  
2527 S SG  . CYS A 349 ? 0.2791 0.3441 0.2710 -0.0414 0.0341  0.0958  335 CYS A SG  
2528 N N   . LYS A 350 ? 0.2866 0.3980 0.2626 -0.0527 0.0462  0.1141  336 LYS A N   
2529 C CA  . LYS A 350 ? 0.3182 0.4443 0.2881 -0.0572 0.0484  0.1222  336 LYS A CA  
2530 C C   . LYS A 350 ? 0.3017 0.4302 0.2811 -0.0610 0.0481  0.1312  336 LYS A C   
2531 O O   . LYS A 350 ? 0.3042 0.4378 0.2831 -0.0641 0.0458  0.1385  336 LYS A O   
2532 C CB  . LYS A 350 ? 0.3269 0.4649 0.2867 -0.0562 0.0548  0.1142  336 LYS A CB  
2533 C CG  . LYS A 350 ? 0.3781 0.5293 0.3317 -0.0592 0.0571  0.1171  336 LYS A CG  
2534 C CD  . LYS A 350 ? 0.4270 0.5830 0.3685 -0.0595 0.0555  0.1162  336 LYS A CD  
2535 C CE  . LYS A 350 ? 0.4503 0.6178 0.3871 -0.0634 0.0558  0.1216  336 LYS A CE  
2536 N NZ  . LYS A 350 ? 0.4377 0.6032 0.3765 -0.0668 0.0493  0.1328  336 LYS A NZ  
2537 N N   . GLN A 351 ? 0.2935 0.4157 0.2828 -0.0600 0.0489  0.1292  337 GLN A N   
2538 C CA  . GLN A 351 ? 0.3005 0.4237 0.2999 -0.0632 0.0480  0.1368  337 GLN A CA  
2539 C C   . GLN A 351 ? 0.3078 0.4205 0.3178 -0.0647 0.0411  0.1450  337 GLN A C   
2540 O O   . GLN A 351 ? 0.2926 0.4082 0.3076 -0.0677 0.0382  0.1530  337 GLN A O   
2541 C CB  . GLN A 351 ? 0.2969 0.4179 0.3035 -0.0619 0.0514  0.1318  337 GLN A CB  
2542 C CG  . GLN A 351 ? 0.2648 0.3904 0.2790 -0.0647 0.0521  0.1372  337 GLN A CG  
2543 C CD  . GLN A 351 ? 0.2694 0.3909 0.2930 -0.0638 0.0540  0.1336  337 GLN A CD  
2544 O OE1 . GLN A 351 ? 0.2837 0.4045 0.3044 -0.0605 0.0572  0.1239  337 GLN A OE1 
2545 N NE2 . GLN A 351 ? 0.2383 0.3559 0.2730 -0.0659 0.0511  0.1395  337 GLN A NE2 
2546 N N   . HIS A 352 ? 0.3076 0.4076 0.3213 -0.0619 0.0376  0.1414  338 HIS A N   
2547 C CA  . HIS A 352 ? 0.3295 0.4187 0.3560 -0.0629 0.0315  0.1473  338 HIS A CA  
2548 C C   . HIS A 352 ? 0.3565 0.4403 0.3828 -0.0625 0.0262  0.1504  338 HIS A C   
2549 O O   . HIS A 352 ? 0.3713 0.4489 0.4088 -0.0644 0.0208  0.1579  338 HIS A O   
2550 C CB  . HIS A 352 ? 0.3280 0.4045 0.3625 -0.0595 0.0307  0.1386  338 HIS A CB  
2551 C CG  . HIS A 352 ? 0.3123 0.3923 0.3501 -0.0602 0.0346  0.1365  338 HIS A CG  
2552 N ND1 . HIS A 352 ? 0.3005 0.3832 0.3481 -0.0640 0.0338  0.1452  338 HIS A ND1 
2553 C CD2 . HIS A 352 ? 0.2967 0.3780 0.3304 -0.0576 0.0390  0.1271  338 HIS A CD2 
2554 C CE1 . HIS A 352 ? 0.2838 0.3694 0.3329 -0.0637 0.0377  0.1411  338 HIS A CE1 
2555 N NE2 . HIS A 352 ? 0.3051 0.3899 0.3461 -0.0598 0.0408  0.1302  338 HIS A NE2 
2556 N N   . VAL A 353 ? 0.3344 0.4206 0.3491 -0.0603 0.0274  0.1452  339 VAL A N   
2557 C CA  . VAL A 353 ? 0.3583 0.4390 0.3727 -0.0595 0.0224  0.1471  339 VAL A CA  
2558 C C   . VAL A 353 ? 0.3710 0.4635 0.3786 -0.0639 0.0216  0.1575  339 VAL A C   
2559 O O   . VAL A 353 ? 0.3698 0.4711 0.3642 -0.0637 0.0246  0.1544  339 VAL A O   
2560 C CB  . VAL A 353 ? 0.3543 0.4296 0.3612 -0.0545 0.0236  0.1352  339 VAL A CB  
2561 C CG1 . VAL A 353 ? 0.3655 0.4369 0.3721 -0.0540 0.0186  0.1381  339 VAL A CG1 
2562 C CG2 . VAL A 353 ? 0.3238 0.3879 0.3376 -0.0509 0.0239  0.1261  339 VAL A CG2 
2563 N N   . HIS A 354 ? 0.3545 0.4472 0.3714 -0.0669 0.0169  0.1667  340 HIS A N   
2564 C CA  . HIS A 354 ? 0.3982 0.5004 0.4100 -0.0700 0.0145  0.1735  340 HIS A CA  
2565 C C   . HIS A 354 ? 0.4230 0.5175 0.4427 -0.0703 0.0070  0.1794  340 HIS A C   
2566 O O   . HIS A 354 ? 0.4254 0.5164 0.4582 -0.0723 0.0015  0.1868  340 HIS A O   
2567 C CB  . HIS A 354 ? 0.3773 0.4868 0.3939 -0.0734 0.0148  0.1793  340 HIS A CB  
2568 C CG  . HIS A 354 ? 0.3842 0.5033 0.3921 -0.0732 0.0224  0.1735  340 HIS A CG  
2569 N ND1 . HIS A 354 ? 0.3871 0.5199 0.3837 -0.0752 0.0256  0.1737  340 HIS A ND1 
2570 C CD2 . HIS A 354 ? 0.3572 0.4740 0.3664 -0.0711 0.0273  0.1666  340 HIS A CD2 
2571 C CE1 . HIS A 354 ? 0.3922 0.5307 0.3844 -0.0742 0.0323  0.1672  340 HIS A CE1 
2572 N NE2 . HIS A 354 ? 0.3715 0.5006 0.3714 -0.0717 0.0333  0.1631  340 HIS A NE2 
2573 N N   . ASP A 355 ? 0.4322 0.5248 0.4443 -0.0684 0.0064  0.1761  341 ASP A N   
2574 C CA  . ASP A 355 ? 0.4418 0.5274 0.4616 -0.0684 -0.0007 0.1812  341 ASP A CA  
2575 C C   . ASP A 355 ? 0.4809 0.5745 0.4893 -0.0697 -0.0023 0.1833  341 ASP A C   
2576 O O   . ASP A 355 ? 0.4753 0.5781 0.4685 -0.0697 0.0025  0.1785  341 ASP A O   
2577 C CB  . ASP A 355 ? 0.4395 0.5120 0.4646 -0.0644 -0.0015 0.1754  341 ASP A CB  
2578 C CG  . ASP A 355 ? 0.4438 0.5076 0.4779 -0.0616 0.0007  0.1679  341 ASP A CG  
2579 O OD1 . ASP A 355 ? 0.4314 0.4941 0.4766 -0.0643 -0.0010 0.1747  341 ASP A OD1 
2580 O OD2 . ASP A 355 ? 0.4050 0.4629 0.4353 -0.0568 0.0036  0.1556  341 ASP A OD2 
2581 N N   . THR A 356 ? 0.4732 0.5620 0.4903 -0.0706 -0.0094 0.1897  342 THR A N   
2582 C CA  . THR A 356 ? 0.5481 0.6412 0.5572 -0.0714 -0.0125 0.1917  342 THR A CA  
2583 C C   . THR A 356 ? 0.5533 0.6333 0.5735 -0.0685 -0.0174 0.1916  342 THR A C   
2584 O O   . THR A 356 ? 0.5709 0.6447 0.6075 -0.0694 -0.0236 0.1978  342 THR A O   
2585 C CB  . THR A 356 ? 0.5368 0.6392 0.5471 -0.0763 -0.0171 0.2015  342 THR A CB  
2586 O OG1 . THR A 356 ? 0.6582 0.7546 0.6873 -0.0778 -0.0232 0.2092  342 THR A OG1 
2587 C CG2 . THR A 356 ? 0.4884 0.6044 0.4871 -0.0791 -0.0119 0.2011  342 THR A CG2 
2588 N N   . PRO A 357 ? 0.5491 0.6250 0.5618 -0.0650 -0.0149 0.1842  343 PRO A N   
2589 C CA  . PRO A 357 ? 0.5746 0.6376 0.5988 -0.0612 -0.0188 0.1808  343 PRO A CA  
2590 C C   . PRO A 357 ? 0.5823 0.6444 0.6140 -0.0634 -0.0267 0.1904  343 PRO A C   
2591 O O   . PRO A 357 ? 0.5644 0.6348 0.5856 -0.0653 -0.0281 0.1928  343 PRO A O   
2592 C CB  . PRO A 357 ? 0.5234 0.5854 0.5352 -0.0563 -0.0140 0.1670  343 PRO A CB  
2593 C CG  . PRO A 357 ? 0.4726 0.5417 0.4738 -0.0567 -0.0068 0.1621  343 PRO A CG  
2594 C CD  . PRO A 357 ? 0.4973 0.5787 0.4937 -0.0630 -0.0075 0.1746  343 PRO A CD  
2595 N N   . VAL A 358 ? 0.6000 0.6521 0.6511 -0.0625 -0.0320 0.1936  344 VAL A N   
2596 C CA  . VAL A 358 ? 0.6667 0.7165 0.7286 -0.0634 -0.0399 0.2000  344 VAL A CA  
2597 C C   . VAL A 358 ? 0.6383 0.6865 0.6920 -0.0609 -0.0403 0.1963  344 VAL A C   
2598 O O   . VAL A 358 ? 0.6130 0.6541 0.6664 -0.0554 -0.0367 0.1834  344 VAL A O   
2599 C CB  . VAL A 358 ? 0.7372 0.7751 0.8229 -0.0618 -0.0448 0.2013  344 VAL A CB  
2600 C CG1 . VAL A 358 ? 0.7908 0.8262 0.8892 -0.0621 -0.0530 0.2068  344 VAL A CG1 
2601 C CG2 . VAL A 358 ? 0.7095 0.7496 0.8035 -0.0644 -0.0451 0.2054  344 VAL A CG2 
2602 N N   . PRO A 359 ? 0.6628 0.7184 0.7098 -0.0633 -0.0439 0.2009  345 PRO A N   
2603 C CA  . PRO A 359 ? 0.6667 0.7219 0.7040 -0.0611 -0.0440 0.1969  345 PRO A CA  
2604 C C   . PRO A 359 ? 0.6429 0.6877 0.6967 -0.0582 -0.0500 0.1970  345 PRO A C   
2605 O O   . PRO A 359 ? 0.6295 0.6695 0.6808 -0.0532 -0.0476 0.1859  345 PRO A O   
2606 C CB  . PRO A 359 ? 0.6980 0.7660 0.7220 -0.0654 -0.0455 0.2015  345 PRO A CB  
2607 C CG  . PRO A 359 ? 0.6850 0.7559 0.7218 -0.0696 -0.0507 0.2112  345 PRO A CG  
2608 C CD  . PRO A 359 ? 0.6735 0.7380 0.7226 -0.0685 -0.0487 0.2103  345 PRO A CD  
2609 N N   . PRO A 370 ? 1.0108 1.0274 1.1265 -0.0246 -0.1113 0.1684  356 PRO A N   
2610 C CA  . PRO A 370 ? 1.0123 1.0281 1.1289 -0.0213 -0.1105 0.1611  356 PRO A CA  
2611 C C   . PRO A 370 ? 1.0247 1.0366 1.1675 -0.0188 -0.1154 0.1632  356 PRO A C   
2612 O O   . PRO A 370 ? 1.0206 1.0329 1.1734 -0.0216 -0.1239 0.1735  356 PRO A O   
2613 C CB  . PRO A 370 ? 1.0593 1.0813 1.1555 -0.0253 -0.1150 0.1654  356 PRO A CB  
2614 C CG  . PRO A 370 ? 1.0660 1.0921 1.1543 -0.0311 -0.1195 0.1771  356 PRO A CG  
2615 C CD  . PRO A 370 ? 0.9899 1.0132 1.0829 -0.0300 -0.1137 0.1749  356 PRO A CD  
2616 N N   . ASP A 371 ? 1.0039 1.0122 1.1573 -0.0135 -0.1091 0.1523  357 ASP A N   
2617 C CA  . ASP A 371 ? 0.9321 0.9367 1.1118 -0.0100 -0.1109 0.1506  357 ASP A CA  
2618 C C   . ASP A 371 ? 0.8252 0.8316 1.0057 -0.0089 -0.1137 0.1492  357 ASP A C   
2619 O O   . ASP A 371 ? 0.8058 0.8157 0.9726 -0.0123 -0.1191 0.1551  357 ASP A O   
2620 C CB  . ASP A 371 ? 0.9082 0.9093 1.0983 -0.0052 -0.1021 0.1390  357 ASP A CB  
2621 C CG  . ASP A 371 ? 0.9765 0.9755 1.1658 -0.0061 -0.0990 0.1396  357 ASP A CG  
2622 O OD1 . ASP A 371 ? 1.0051 1.0066 1.1739 -0.0092 -0.0977 0.1420  357 ASP A OD1 
2623 O OD2 . ASP A 371 ? 0.9039 0.8988 1.1141 -0.0037 -0.0979 0.1373  357 ASP A OD2 
2624 N N   . GLY A 372 ? 0.7463 0.7505 0.9455 -0.0045 -0.1111 0.1424  358 GLY A N   
2625 C CA  . GLY A 372 ? 0.5854 0.5914 0.7853 -0.0025 -0.1109 0.1376  358 GLY A CA  
2626 C C   . GLY A 372 ? 0.5408 0.5473 0.7315 0.0008  -0.1006 0.1242  358 GLY A C   
2627 O O   . GLY A 372 ? 0.5249 0.5335 0.6930 -0.0005 -0.0975 0.1211  358 GLY A O   
2628 N N   . SER A 373 ? 0.4937 0.4987 0.7023 0.0048  -0.0956 0.1166  359 SER A N   
2629 C CA  . SER A 373 ? 0.4792 0.4857 0.6814 0.0076  -0.0867 0.1047  359 SER A CA  
2630 C C   . SER A 373 ? 0.4737 0.4796 0.6579 0.0071  -0.0798 0.0993  359 SER A C   
2631 O O   . SER A 373 ? 0.4678 0.4714 0.6535 0.0063  -0.0793 0.1016  359 SER A O   
2632 C CB  . SER A 373 ? 0.4957 0.5016 0.7222 0.0116  -0.0830 0.0981  359 SER A CB  
2633 O OG  . SER A 373 ? 0.5959 0.6034 0.8170 0.0138  -0.0738 0.0867  359 SER A OG  
2634 N N   . LEU A 374 ? 0.4304 0.4387 0.5986 0.0075  -0.0747 0.0923  360 LEU A N   
2635 C CA  . LEU A 374 ? 0.4270 0.4351 0.5773 0.0068  -0.0687 0.0875  360 LEU A CA  
2636 C C   . LEU A 374 ? 0.4343 0.4406 0.5940 0.0092  -0.0615 0.0798  360 LEU A C   
2637 O O   . LEU A 374 ? 0.4364 0.4437 0.6071 0.0118  -0.0573 0.0728  360 LEU A O   
2638 C CB  . LEU A 374 ? 0.4336 0.4446 0.5663 0.0065  -0.0661 0.0824  360 LEU A CB  
2639 C CG  . LEU A 374 ? 0.3967 0.4094 0.5101 0.0034  -0.0708 0.0875  360 LEU A CG  
2640 C CD1 . LEU A 374 ? 0.3554 0.3706 0.4568 0.0037  -0.0691 0.0819  360 LEU A CD1 
2641 C CD2 . LEU A 374 ? 0.3842 0.3964 0.4841 0.0014  -0.0690 0.0892  360 LEU A CD2 
2642 N N   . THR A 375 ? 0.4001 0.4042 0.5550 0.0081  -0.0599 0.0810  361 THR A N   
2643 C CA  . THR A 375 ? 0.4237 0.4260 0.5834 0.0098  -0.0530 0.0735  361 THR A CA  
2644 C C   . THR A 375 ? 0.4284 0.4310 0.5670 0.0081  -0.0488 0.0711  361 THR A C   
2645 O O   . THR A 375 ? 0.4024 0.4065 0.5250 0.0057  -0.0516 0.0759  361 THR A O   
2646 C CB  . THR A 375 ? 0.4059 0.4046 0.5832 0.0101  -0.0554 0.0774  361 THR A CB  
2647 O OG1 . THR A 375 ? 0.3847 0.3825 0.5533 0.0068  -0.0604 0.0870  361 THR A OG1 
2648 C CG2 . THR A 375 ? 0.4132 0.4114 0.6136 0.0118  -0.0599 0.0798  361 THR A CG2 
2649 N N   . GLN A 376 ? 0.4749 0.4764 0.6143 0.0093  -0.0422 0.0635  362 GLN A N   
2650 C CA  . GLN A 376 ? 0.4813 0.4826 0.6036 0.0078  -0.0385 0.0617  362 GLN A CA  
2651 C C   . GLN A 376 ? 0.4449 0.4450 0.5626 0.0052  -0.0428 0.0706  362 GLN A C   
2652 O O   . GLN A 376 ? 0.4121 0.4139 0.5122 0.0030  -0.0430 0.0730  362 GLN A O   
2653 C CB  . GLN A 376 ? 0.5515 0.5514 0.6785 0.0092  -0.0318 0.0532  362 GLN A CB  
2654 C CG  . GLN A 376 ? 0.6440 0.6466 0.7681 0.0105  -0.0264 0.0444  362 GLN A CG  
2655 C CD  . GLN A 376 ? 0.6512 0.6556 0.7549 0.0090  -0.0240 0.0424  362 GLN A CD  
2656 O OE1 . GLN A 376 ? 0.6438 0.6468 0.7381 0.0077  -0.0222 0.0426  362 GLN A OE1 
2657 N NE2 . GLN A 376 ? 0.6212 0.6286 0.7188 0.0091  -0.0239 0.0404  362 GLN A NE2 
2658 N N   . ASP A 377 ? 0.4224 0.4198 0.5565 0.0052  -0.0464 0.0756  363 ASP A N   
2659 C CA  . ASP A 377 ? 0.4300 0.4265 0.5611 0.0023  -0.0505 0.0847  363 ASP A CA  
2660 C C   . ASP A 377 ? 0.4093 0.4092 0.5281 -0.0005 -0.0563 0.0932  363 ASP A C   
2661 O O   . ASP A 377 ? 0.4182 0.4203 0.5206 -0.0032 -0.0562 0.0965  363 ASP A O   
2662 C CB  . ASP A 377 ? 0.4504 0.4432 0.6041 0.0029  -0.0542 0.0889  363 ASP A CB  
2663 C CG  . ASP A 377 ? 0.4928 0.4836 0.6456 0.0007  -0.0549 0.0940  363 ASP A CG  
2664 O OD1 . ASP A 377 ? 0.5218 0.5114 0.6695 0.0013  -0.0490 0.0876  363 ASP A OD1 
2665 O OD2 . ASP A 377 ? 0.5346 0.5254 0.6923 -0.0019 -0.0616 0.1047  363 ASP A OD2 
2666 N N   . ASN A 378 ? 0.3996 0.4004 0.5262 -0.0001 -0.0614 0.0966  364 ASN A N   
2667 C CA  . ASN A 378 ? 0.4082 0.4123 0.5231 -0.0033 -0.0675 0.1049  364 ASN A CA  
2668 C C   . ASN A 378 ? 0.3821 0.3897 0.4763 -0.0037 -0.0646 0.0999  364 ASN A C   
2669 O O   . ASN A 378 ? 0.3572 0.3683 0.4373 -0.0066 -0.0682 0.1052  364 ASN A O   
2670 C CB  . ASN A 378 ? 0.4131 0.4169 0.5431 -0.0034 -0.0750 0.1116  364 ASN A CB  
2671 C CG  . ASN A 378 ? 0.4362 0.4401 0.5743 -0.0001 -0.0735 0.1047  364 ASN A CG  
2672 O OD1 . ASN A 378 ? 0.4098 0.4152 0.5375 0.0013  -0.0682 0.0965  364 ASN A OD1 
2673 N ND2 . ASN A 378 ? 0.4884 0.4911 0.6463 0.0009  -0.0785 0.1086  364 ASN A ND2 
2674 N N   . PHE A 379 ? 0.3812 0.3883 0.4731 -0.0009 -0.0584 0.0898  365 PHE A N   
2675 C CA  . PHE A 379 ? 0.3692 0.3792 0.4422 -0.0014 -0.0558 0.0850  365 PHE A CA  
2676 C C   . PHE A 379 ? 0.3593 0.3708 0.4165 -0.0035 -0.0532 0.0856  365 PHE A C   
2677 O O   . PHE A 379 ? 0.3510 0.3661 0.3928 -0.0057 -0.0551 0.0877  365 PHE A O   
2678 C CB  . PHE A 379 ? 0.3590 0.3685 0.4338 0.0015  -0.0499 0.0749  365 PHE A CB  
2679 C CG  . PHE A 379 ? 0.3571 0.3689 0.4138 0.0010  -0.0469 0.0698  365 PHE A CG  
2680 C CD1 . PHE A 379 ? 0.3296 0.3438 0.3790 0.0006  -0.0501 0.0697  365 PHE A CD1 
2681 C CD2 . PHE A 379 ? 0.3454 0.3569 0.3931 0.0008  -0.0414 0.0652  365 PHE A CD2 
2682 C CE1 . PHE A 379 ? 0.3103 0.3264 0.3446 0.0003  -0.0478 0.0648  365 PHE A CE1 
2683 C CE2 . PHE A 379 ? 0.3315 0.3450 0.3642 0.0004  -0.0391 0.0606  365 PHE A CE2 
2684 C CZ  . PHE A 379 ? 0.3142 0.3300 0.3405 0.0002  -0.0423 0.0602  365 PHE A CZ  
2685 N N   . TRP A 380 ? 0.3411 0.3502 0.4019 -0.0030 -0.0487 0.0832  366 TRP A N   
2686 C CA  . TRP A 380 ? 0.3609 0.3716 0.4079 -0.0050 -0.0459 0.0835  366 TRP A CA  
2687 C C   . TRP A 380 ? 0.3618 0.3751 0.4046 -0.0085 -0.0509 0.0938  366 TRP A C   
2688 O O   . TRP A 380 ? 0.3528 0.3700 0.3798 -0.0108 -0.0501 0.0949  366 TRP A O   
2689 C CB  . TRP A 380 ? 0.3478 0.3553 0.4007 -0.0037 -0.0403 0.0787  366 TRP A CB  
2690 C CG  . TRP A 380 ? 0.3546 0.3611 0.4079 -0.0010 -0.0351 0.0688  366 TRP A CG  
2691 C CD1 . TRP A 380 ? 0.3671 0.3710 0.4345 0.0014  -0.0330 0.0638  366 TRP A CD1 
2692 C CD2 . TRP A 380 ? 0.3574 0.3661 0.3964 -0.0009 -0.0318 0.0627  366 TRP A CD2 
2693 N NE1 . TRP A 380 ? 0.3776 0.3825 0.4396 0.0027  -0.0284 0.0557  366 TRP A NE1 
2694 C CE2 . TRP A 380 ? 0.3742 0.3816 0.4193 0.0014  -0.0279 0.0551  366 TRP A CE2 
2695 C CE3 . TRP A 380 ? 0.3236 0.3355 0.3460 -0.0024 -0.0317 0.0628  366 TRP A CE3 
2696 C CZ2 . TRP A 380 ? 0.3605 0.3694 0.3959 0.0018  -0.0246 0.0487  366 TRP A CZ2 
2697 C CZ3 . TRP A 380 ? 0.3247 0.3377 0.3385 -0.0016 -0.0283 0.0557  366 TRP A CZ3 
2698 C CH2 . TRP A 380 ? 0.3405 0.3518 0.3610 0.0004  -0.0251 0.0492  366 TRP A CH2 
2699 N N   . LYS A 381 ? 0.3643 0.3760 0.4215 -0.0093 -0.0564 0.1014  367 LYS A N   
2700 C CA  . LYS A 381 ? 0.3930 0.4079 0.4464 -0.0133 -0.0621 0.1125  367 LYS A CA  
2701 C C   . LYS A 381 ? 0.3812 0.4011 0.4197 -0.0154 -0.0657 0.1147  367 LYS A C   
2702 O O   . LYS A 381 ? 0.3918 0.4167 0.4170 -0.0191 -0.0674 0.1200  367 LYS A O   
2703 C CB  . LYS A 381 ? 0.4106 0.4223 0.4845 -0.0136 -0.0681 0.1203  367 LYS A CB  
2704 C CG  . LYS A 381 ? 0.4561 0.4652 0.5395 -0.0147 -0.0677 0.1246  367 LYS A CG  
2705 C CD  . LYS A 381 ? 0.4831 0.4872 0.5917 -0.0127 -0.0713 0.1267  367 LYS A CD  
2706 C CE  . LYS A 381 ? 0.5013 0.5007 0.6218 -0.0113 -0.0676 0.1235  367 LYS A CE  
2707 N NZ  . LYS A 381 ? 0.4905 0.4858 0.6361 -0.0105 -0.0730 0.1285  367 LYS A NZ  
2708 N N   . THR A 382 ? 0.3532 0.3725 0.3941 -0.0133 -0.0670 0.1106  368 THR A N   
2709 C CA  . THR A 382 ? 0.3982 0.4220 0.4252 -0.0151 -0.0706 0.1117  368 THR A CA  
2710 C C   . THR A 382 ? 0.3696 0.3969 0.3772 -0.0154 -0.0655 0.1050  368 THR A C   
2711 O O   . THR A 382 ? 0.3860 0.4187 0.3789 -0.0186 -0.0677 0.1080  368 THR A O   
2712 C CB  . THR A 382 ? 0.4036 0.4257 0.4387 -0.0125 -0.0729 0.1083  368 THR A CB  
2713 O OG1 . THR A 382 ? 0.4092 0.4281 0.4644 -0.0119 -0.0773 0.1139  368 THR A OG1 
2714 C CG2 . THR A 382 ? 0.3535 0.3799 0.3754 -0.0146 -0.0776 0.1099  368 THR A CG2 
2715 N N   . LEU A 383 ? 0.3392 0.3639 0.3469 -0.0124 -0.0588 0.0958  369 LEU A N   
2716 C CA  . LEU A 383 ? 0.3444 0.3719 0.3357 -0.0125 -0.0542 0.0891  369 LEU A CA  
2717 C C   . LEU A 383 ? 0.3610 0.3920 0.3432 -0.0153 -0.0523 0.0928  369 LEU A C   
2718 O O   . LEU A 383 ? 0.3549 0.3910 0.3217 -0.0170 -0.0511 0.0910  369 LEU A O   
2719 C CB  . LEU A 383 ? 0.3422 0.3661 0.3374 -0.0090 -0.0482 0.0796  369 LEU A CB  
2720 C CG  . LEU A 383 ? 0.3566 0.3827 0.3379 -0.0085 -0.0445 0.0717  369 LEU A CG  
2721 C CD1 . LEU A 383 ? 0.3623 0.3907 0.3376 -0.0086 -0.0486 0.0704  369 LEU A CD1 
2722 C CD2 . LEU A 383 ? 0.3675 0.3900 0.3539 -0.0057 -0.0389 0.0638  369 LEU A CD2 
2723 N N   . GLN A 384 ? 0.3346 0.3633 0.3268 -0.0160 -0.0520 0.0980  370 GLN A N   
2724 C CA  . GLN A 384 ? 0.3419 0.3741 0.3269 -0.0191 -0.0506 0.1027  370 GLN A CA  
2725 C C   . GLN A 384 ? 0.3642 0.4037 0.3365 -0.0233 -0.0550 0.1096  370 GLN A C   
2726 O O   . GLN A 384 ? 0.3623 0.4075 0.3208 -0.0255 -0.0522 0.1090  370 GLN A O   
2727 C CB  . GLN A 384 ? 0.3360 0.3643 0.3365 -0.0195 -0.0516 0.1089  370 GLN A CB  
2728 C CG  . GLN A 384 ? 0.3211 0.3530 0.3164 -0.0230 -0.0508 0.1152  370 GLN A CG  
2729 C CD  . GLN A 384 ? 0.3502 0.3839 0.3346 -0.0223 -0.0436 0.1078  370 GLN A CD  
2730 O OE1 . GLN A 384 ? 0.3515 0.3803 0.3416 -0.0192 -0.0390 0.1004  370 GLN A OE1 
2731 N NE2 . GLN A 384 ? 0.3361 0.3770 0.3051 -0.0253 -0.0427 0.1095  370 GLN A NE2 
2732 N N   . THR A 385 ? 0.3481 0.3881 0.3248 -0.0247 -0.0619 0.1162  371 THR A N   
2733 C CA  . THR A 385 ? 0.3875 0.4351 0.3516 -0.0294 -0.0666 0.1231  371 THR A CA  
2734 C C   . THR A 385 ? 0.3884 0.4407 0.3353 -0.0292 -0.0652 0.1156  371 THR A C   
2735 O O   . THR A 385 ? 0.3951 0.4551 0.3279 -0.0331 -0.0669 0.1188  371 THR A O   
2736 C CB  . THR A 385 ? 0.3896 0.4364 0.3638 -0.0313 -0.0751 0.1328  371 THR A CB  
2737 O OG1 . THR A 385 ? 0.4303 0.4751 0.4059 -0.0288 -0.0774 0.1279  371 THR A OG1 
2738 C CG2 . THR A 385 ? 0.3516 0.3921 0.3467 -0.0301 -0.0766 0.1381  371 THR A CG2 
2739 N N   . PHE A 386 ? 0.3836 0.4319 0.3319 -0.0251 -0.0621 0.1055  372 PHE A N   
2740 C CA  . PHE A 386 ? 0.3827 0.4340 0.3185 -0.0243 -0.0617 0.0978  372 PHE A CA  
2741 C C   . PHE A 386 ? 0.3760 0.4304 0.2997 -0.0237 -0.0550 0.0896  372 PHE A C   
2742 O O   . PHE A 386 ? 0.3672 0.4272 0.2771 -0.0249 -0.0551 0.0856  372 PHE A O   
2743 C CB  . PHE A 386 ? 0.3882 0.4335 0.3338 -0.0203 -0.0624 0.0920  372 PHE A CB  
2744 C CG  . PHE A 386 ? 0.3747 0.4215 0.3102 -0.0188 -0.0612 0.0828  372 PHE A CG  
2745 C CD1 . PHE A 386 ? 0.3844 0.4356 0.3104 -0.0208 -0.0663 0.0834  372 PHE A CD1 
2746 C CD2 . PHE A 386 ? 0.3567 0.4005 0.2930 -0.0156 -0.0555 0.0735  372 PHE A CD2 
2747 C CE1 . PHE A 386 ? 0.3771 0.4292 0.2951 -0.0193 -0.0657 0.0745  372 PHE A CE1 
2748 C CE2 . PHE A 386 ? 0.3386 0.3834 0.2673 -0.0143 -0.0551 0.0654  372 PHE A CE2 
2749 C CZ  . PHE A 386 ? 0.3527 0.4016 0.2727 -0.0160 -0.0601 0.0657  372 PHE A CZ  
2750 N N   . ILE A 387 ? 0.3389 0.3898 0.2682 -0.0217 -0.0493 0.0865  373 ILE A N   
2751 C CA  . ILE A 387 ? 0.3533 0.4067 0.2731 -0.0208 -0.0431 0.0784  373 ILE A CA  
2752 C C   . ILE A 387 ? 0.3459 0.4081 0.2522 -0.0247 -0.0423 0.0818  373 ILE A C   
2753 O O   . ILE A 387 ? 0.3499 0.4155 0.2558 -0.0283 -0.0456 0.0914  373 ILE A O   
2754 C CB  . ILE A 387 ? 0.3437 0.3917 0.2724 -0.0183 -0.0376 0.0751  373 ILE A CB  
2755 C CG1 . ILE A 387 ? 0.3616 0.4102 0.2947 -0.0206 -0.0369 0.0831  373 ILE A CG1 
2756 C CG2 . ILE A 387 ? 0.3030 0.3435 0.2447 -0.0149 -0.0382 0.0721  373 ILE A CG2 
2757 C CD1 . ILE A 387 ? 0.3240 0.3669 0.2668 -0.0183 -0.0319 0.0799  373 ILE A CD1 
2758 N N   . ARG A 388 ? 0.3456 0.4119 0.2412 -0.0241 -0.0381 0.0736  374 ARG A N   
2759 C CA  . ARG A 388 ? 0.3468 0.4229 0.2282 -0.0276 -0.0368 0.0745  374 ARG A CA  
2760 C C   . ARG A 388 ? 0.3528 0.4307 0.2300 -0.0259 -0.0298 0.0661  374 ARG A C   
2761 O O   . ARG A 388 ? 0.3422 0.4141 0.2250 -0.0222 -0.0271 0.0585  374 ARG A O   
2762 C CB  . ARG A 388 ? 0.3625 0.4441 0.2326 -0.0291 -0.0409 0.0722  374 ARG A CB  
2763 C CG  . ARG A 388 ? 0.3717 0.4533 0.2443 -0.0317 -0.0486 0.0815  374 ARG A CG  
2764 C CD  . ARG A 388 ? 0.4026 0.4910 0.2707 -0.0370 -0.0504 0.0927  374 ARG A CD  
2765 N NE  . ARG A 388 ? 0.3634 0.4530 0.2323 -0.0402 -0.0584 0.1019  374 ARG A NE  
2766 C CZ  . ARG A 388 ? 0.4101 0.4924 0.2938 -0.0392 -0.0629 0.1084  374 ARG A CZ  
2767 N NH1 . ARG A 388 ? 0.3744 0.4482 0.2726 -0.0354 -0.0600 0.1068  374 ARG A NH1 
2768 N NH2 . ARG A 388 ? 0.4064 0.4904 0.2907 -0.0423 -0.0705 0.1167  374 ARG A NH2 
2769 N N   . PRO A 389 ? 0.3779 0.4645 0.2452 -0.0289 -0.0268 0.0673  375 PRO A N   
2770 C CA  . PRO A 389 ? 0.3669 0.4565 0.2297 -0.0274 -0.0203 0.0585  375 PRO A CA  
2771 C C   . PRO A 389 ? 0.3717 0.4608 0.2305 -0.0244 -0.0203 0.0472  375 PRO A C   
2772 O O   . PRO A 389 ? 0.3594 0.4503 0.2129 -0.0251 -0.0248 0.0462  375 PRO A O   
2773 C CB  . PRO A 389 ? 0.4141 0.5154 0.2653 -0.0319 -0.0184 0.0624  375 PRO A CB  
2774 C CG  . PRO A 389 ? 0.3840 0.4855 0.2389 -0.0355 -0.0226 0.0757  375 PRO A CG  
2775 C CD  . PRO A 389 ? 0.3831 0.4773 0.2446 -0.0341 -0.0290 0.0778  375 PRO A CD  
2776 N N   . GLY A 390 ? 0.3600 0.4461 0.2225 -0.0213 -0.0158 0.0389  376 GLY A N   
2777 C CA  . GLY A 390 ? 0.3421 0.4264 0.2038 -0.0182 -0.0161 0.0284  376 GLY A CA  
2778 C C   . GLY A 390 ? 0.3288 0.4030 0.2012 -0.0151 -0.0188 0.0269  376 GLY A C   
2779 O O   . GLY A 390 ? 0.3230 0.3947 0.1971 -0.0125 -0.0188 0.0186  376 GLY A O   
2780 N N   . ASP A 391 ? 0.3173 0.3860 0.1977 -0.0154 -0.0212 0.0347  377 ASP A N   
2781 C CA  . ASP A 391 ? 0.3165 0.3770 0.2071 -0.0128 -0.0236 0.0334  377 ASP A CA  
2782 C C   . ASP A 391 ? 0.3081 0.3637 0.2053 -0.0101 -0.0193 0.0276  377 ASP A C   
2783 O O   . ASP A 391 ? 0.2841 0.3402 0.1823 -0.0105 -0.0150 0.0282  377 ASP A O   
2784 C CB  . ASP A 391 ? 0.3139 0.3703 0.2127 -0.0136 -0.0264 0.0426  377 ASP A CB  
2785 C CG  . ASP A 391 ? 0.3346 0.3933 0.2302 -0.0155 -0.0326 0.0478  377 ASP A CG  
2786 O OD1 . ASP A 391 ? 0.3166 0.3792 0.2039 -0.0159 -0.0349 0.0436  377 ASP A OD1 
2787 O OD2 . ASP A 391 ? 0.3216 0.3784 0.2238 -0.0168 -0.0355 0.0562  377 ASP A OD2 
2788 N N   . ILE A 392 ? 0.2898 0.3409 0.1919 -0.0078 -0.0209 0.0224  378 ILE A N   
2789 C CA  . ILE A 392 ? 0.2864 0.3319 0.1968 -0.0057 -0.0183 0.0188  378 ILE A CA  
2790 C C   . ILE A 392 ? 0.2797 0.3196 0.1996 -0.0051 -0.0206 0.0229  378 ILE A C   
2791 O O   . ILE A 392 ? 0.3058 0.3446 0.2275 -0.0045 -0.0247 0.0228  378 ILE A O   
2792 C CB  . ILE A 392 ? 0.2792 0.3243 0.1892 -0.0040 -0.0185 0.0102  378 ILE A CB  
2793 C CG1 . ILE A 392 ? 0.2773 0.3285 0.1791 -0.0043 -0.0160 0.0051  378 ILE A CG1 
2794 C CG2 . ILE A 392 ? 0.2721 0.3116 0.1911 -0.0025 -0.0164 0.0078  378 ILE A CG2 
2795 C CD1 . ILE A 392 ? 0.2759 0.3266 0.1788 -0.0025 -0.0170 -0.0035 378 ILE A CD1 
2796 N N   . ILE A 393 ? 0.2842 0.3208 0.2109 -0.0051 -0.0179 0.0261  379 ILE A N   
2797 C CA  . ILE A 393 ? 0.2732 0.3052 0.2096 -0.0045 -0.0194 0.0298  379 ILE A CA  
2798 C C   . ILE A 393 ? 0.2782 0.3061 0.2215 -0.0031 -0.0164 0.0256  379 ILE A C   
2799 O O   . ILE A 393 ? 0.2677 0.2950 0.2114 -0.0033 -0.0125 0.0245  379 ILE A O   
2800 C CB  . ILE A 393 ? 0.2669 0.2988 0.2066 -0.0059 -0.0196 0.0374  379 ILE A CB  
2801 C CG1 . ILE A 393 ? 0.2820 0.3188 0.2144 -0.0080 -0.0232 0.0425  379 ILE A CG1 
2802 C CG2 . ILE A 393 ? 0.2376 0.2648 0.1896 -0.0049 -0.0208 0.0399  379 ILE A CG2 
2803 C CD1 . ILE A 393 ? 0.2730 0.3108 0.2079 -0.0101 -0.0235 0.0508  379 ILE A CD1 
2804 N N   . LEU A 394 ? 0.2553 0.2808 0.2040 -0.0020 -0.0182 0.0235  380 LEU A N   
2805 C CA  . LEU A 394 ? 0.2478 0.2703 0.2028 -0.0012 -0.0157 0.0200  380 LEU A CA  
2806 C C   . LEU A 394 ? 0.2571 0.2772 0.2219 -0.0007 -0.0162 0.0226  380 LEU A C   
2807 O O   . LEU A 394 ? 0.2712 0.2915 0.2387 -0.0004 -0.0198 0.0251  380 LEU A O   
2808 C CB  . LEU A 394 ? 0.2442 0.2671 0.1979 -0.0006 -0.0171 0.0148  380 LEU A CB  
2809 C CG  . LEU A 394 ? 0.2701 0.2956 0.2159 -0.0007 -0.0170 0.0109  380 LEU A CG  
2810 C CD1 . LEU A 394 ? 0.2463 0.2747 0.1862 -0.0007 -0.0210 0.0111  380 LEU A CD1 
2811 C CD2 . LEU A 394 ? 0.2463 0.2707 0.1944 -0.0003 -0.0167 0.0057  380 LEU A CD2 
2812 N N   . ALA A 395 ? 0.2191 0.2370 0.1895 -0.0007 -0.0127 0.0217  381 ALA A N   
2813 C CA  . ALA A 395 ? 0.2791 0.2950 0.2596 -0.0001 -0.0124 0.0230  381 ALA A CA  
2814 C C   . ALA A 395 ? 0.2747 0.2898 0.2590 -0.0002 -0.0091 0.0184  381 ALA A C   
2815 O O   . ALA A 395 ? 0.2471 0.2618 0.2279 -0.0010 -0.0063 0.0160  381 ALA A O   
2816 C CB  . ALA A 395 ? 0.2986 0.3131 0.2837 -0.0004 -0.0115 0.0272  381 ALA A CB  
2817 N N   . ASP A 396 ? 0.2823 0.2976 0.2736 0.0003  -0.0096 0.0175  382 ASP A N   
2818 C CA  . ASP A 396 ? 0.2731 0.2888 0.2678 -0.0003 -0.0066 0.0135  382 ASP A CA  
2819 C C   . ASP A 396 ? 0.3004 0.3149 0.3029 -0.0002 -0.0032 0.0128  382 ASP A C   
2820 O O   . ASP A 396 ? 0.3152 0.3281 0.3224 0.0006  -0.0038 0.0157  382 ASP A O   
2821 C CB  . ASP A 396 ? 0.2470 0.2648 0.2452 -0.0002 -0.0085 0.0124  382 ASP A CB  
2822 C CG  . ASP A 396 ? 0.2464 0.2657 0.2422 -0.0017 -0.0071 0.0090  382 ASP A CG  
2823 O OD1 . ASP A 396 ? 0.2534 0.2725 0.2494 -0.0028 -0.0034 0.0068  382 ASP A OD1 
2824 O OD2 . ASP A 396 ? 0.2160 0.2366 0.2101 -0.0021 -0.0099 0.0086  382 ASP A OD2 
2825 N N   . GLN A 397 ? 0.2632 0.2786 0.2672 -0.0012 0.0001  0.0089  383 GLN A N   
2826 C CA  . GLN A 397 ? 0.3001 0.3149 0.3114 -0.0012 0.0035  0.0067  383 GLN A CA  
2827 C C   . GLN A 397 ? 0.3116 0.3279 0.3332 0.0000  0.0031  0.0067  383 GLN A C   
2828 O O   . GLN A 397 ? 0.3111 0.3298 0.3335 0.0002  0.0010  0.0073  383 GLN A O   
2829 C CB  . GLN A 397 ? 0.3079 0.3242 0.3167 -0.0032 0.0070  0.0024  383 GLN A CB  
2830 C CG  . GLN A 397 ? 0.2758 0.2905 0.2762 -0.0044 0.0074  0.0024  383 GLN A CG  
2831 C CD  . GLN A 397 ? 0.3185 0.3300 0.3193 -0.0037 0.0078  0.0045  383 GLN A CD  
2832 O OE1 . GLN A 397 ? 0.3675 0.3776 0.3738 -0.0037 0.0102  0.0030  383 GLN A OE1 
2833 N NE2 . GLN A 397 ? 0.3097 0.3204 0.3051 -0.0032 0.0055  0.0079  383 GLN A NE2 
2834 N N   . GLY A 398 ? 0.3605 0.3754 0.3909 0.0009  0.0048  0.0060  384 GLY A N   
2835 C CA  . GLY A 398 ? 0.4255 0.4409 0.4678 0.0026  0.0039  0.0067  384 GLY A CA  
2836 C C   . GLY A 398 ? 0.5026 0.5146 0.5496 0.0038  0.0009  0.0116  384 GLY A C   
2837 O O   . GLY A 398 ? 0.5213 0.5306 0.5636 0.0033  0.0008  0.0136  384 GLY A O   
2838 N N   . THR A 399 ? 0.5451 0.5574 0.6021 0.0053  -0.0017 0.0141  385 THR A N   
2839 C CA  . THR A 399 ? 0.5827 0.5921 0.6454 0.0061  -0.0058 0.0201  385 THR A CA  
2840 C C   . THR A 399 ? 0.5357 0.5448 0.5868 0.0051  -0.0100 0.0261  385 THR A C   
2841 O O   . THR A 399 ? 0.5560 0.5638 0.6108 0.0053  -0.0140 0.0320  385 THR A O   
2842 C CB  . THR A 399 ? 0.5550 0.5654 0.6320 0.0078  -0.0080 0.0212  385 THR A CB  
2843 O OG1 . THR A 399 ? 0.4916 0.5038 0.5643 0.0077  -0.0120 0.0249  385 THR A OG1 
2844 C CG2 . THR A 399 ? 0.6554 0.6684 0.7413 0.0086  -0.0033 0.0141  385 THR A CG2 
2845 N N   . SER A 400 ? 0.5027 0.5133 0.5411 0.0041  -0.0096 0.0247  386 SER A N   
2846 C CA  . SER A 400 ? 0.4624 0.4732 0.4894 0.0032  -0.0127 0.0287  386 SER A CA  
2847 C C   . SER A 400 ? 0.4858 0.4952 0.5061 0.0021  -0.0108 0.0296  386 SER A C   
2848 O O   . SER A 400 ? 0.4547 0.4635 0.4742 0.0015  -0.0131 0.0349  386 SER A O   
2849 C CB  . SER A 400 ? 0.3964 0.4096 0.4145 0.0028  -0.0132 0.0260  386 SER A CB  
2850 O OG  . SER A 400 ? 0.4998 0.5143 0.5200 0.0033  -0.0175 0.0285  386 SER A OG  
2851 N N   . ALA A 401 ? 0.5940 0.6033 0.6098 0.0015  -0.0068 0.0248  387 ALA A N   
2852 C CA  . ALA A 401 ? 0.5035 0.5118 0.5130 0.0004  -0.0050 0.0255  387 ALA A CA  
2853 C C   . ALA A 401 ? 0.6615 0.6672 0.6794 0.0004  -0.0046 0.0283  387 ALA A C   
2854 O O   . ALA A 401 ? 0.5401 0.5455 0.5547 -0.0006 -0.0055 0.0326  387 ALA A O   
2855 C CB  . ALA A 401 ? 0.4578 0.4664 0.4627 -0.0003 -0.0011 0.0199  387 ALA A CB  
2856 N N   . PHE A 402 ? 0.7573 0.7615 0.7870 0.0014  -0.0034 0.0258  388 PHE A N   
2857 C CA  . PHE A 402 ? 0.7387 0.7400 0.7786 0.0016  -0.0034 0.0277  388 PHE A CA  
2858 C C   . PHE A 402 ? 0.6337 0.6343 0.6809 0.0020  -0.0082 0.0347  388 PHE A C   
2859 O O   . PHE A 402 ? 0.8159 0.8139 0.8718 0.0018  -0.0092 0.0378  388 PHE A O   
2860 C CB  . PHE A 402 ? 0.8334 0.8338 0.8835 0.0026  0.0000  0.0213  388 PHE A CB  
2861 C CG  . PHE A 402 ? 0.9770 0.9781 1.0200 0.0015  0.0043  0.0153  388 PHE A CG  
2862 C CD1 . PHE A 402 ? 0.8762 0.8760 0.9118 0.0001  0.0054  0.0163  388 PHE A CD1 
2863 C CD2 . PHE A 402 ? 1.0925 1.0961 1.1359 0.0016  0.0071  0.0093  388 PHE A CD2 
2864 C CE1 . PHE A 402 ? 0.9258 0.9261 0.9554 -0.0011 0.0088  0.0115  388 PHE A CE1 
2865 C CE2 . PHE A 402 ? 1.0454 1.0498 1.0820 0.0001  0.0105  0.0047  388 PHE A CE2 
2866 C CZ  . PHE A 402 ? 0.8774 0.8799 0.9072 -0.0012 0.0111  0.0058  388 PHE A CZ  
2867 N N   . GLY A 403 ? 0.5133 0.5160 0.5579 0.0022  -0.0115 0.0376  389 GLY A N   
2868 C CA  . GLY A 403 ? 0.4528 0.4555 0.5005 0.0016  -0.0167 0.0456  389 GLY A CA  
2869 C C   . GLY A 403 ? 0.4126 0.4174 0.4464 -0.0005 -0.0180 0.0501  389 GLY A C   
2870 O O   . GLY A 403 ? 0.3813 0.3859 0.4164 -0.0019 -0.0204 0.0566  389 GLY A O   
2871 N N   . ALA A 404 ? 0.4145 0.4217 0.4355 -0.0007 -0.0162 0.0464  390 ALA A N   
2872 C CA  . ALA A 404 ? 0.3817 0.3918 0.3893 -0.0025 -0.0170 0.0493  390 ALA A CA  
2873 C C   . ALA A 404 ? 0.3823 0.3919 0.3882 -0.0039 -0.0145 0.0509  390 ALA A C   
2874 O O   . ALA A 404 ? 0.3343 0.3468 0.3323 -0.0058 -0.0157 0.0556  390 ALA A O   
2875 C CB  . ALA A 404 ? 0.3608 0.3731 0.3577 -0.0022 -0.0153 0.0436  390 ALA A CB  
2876 N N   . ILE A 405 ? 0.3991 0.4053 0.4123 -0.0032 -0.0112 0.0474  391 ILE A N   
2877 C CA  . ILE A 405 ? 0.3670 0.3723 0.3798 -0.0045 -0.0091 0.0488  391 ILE A CA  
2878 C C   . ILE A 405 ? 0.3539 0.3595 0.3711 -0.0061 -0.0127 0.0577  391 ILE A C   
2879 O O   . ILE A 405 ? 0.3111 0.3179 0.3242 -0.0080 -0.0118 0.0611  391 ILE A O   
2880 C CB  . ILE A 405 ? 0.3773 0.3787 0.3991 -0.0034 -0.0057 0.0434  391 ILE A CB  
2881 C CG1 . ILE A 405 ? 0.3653 0.3659 0.3848 -0.0049 -0.0032 0.0438  391 ILE A CG1 
2882 C CG2 . ILE A 405 ? 0.4102 0.4086 0.4476 -0.0023 -0.0079 0.0450  391 ILE A CG2 
2883 C CD1 . ILE A 405 ? 0.3718 0.3691 0.3973 -0.0043 0.0002  0.0375  391 ILE A CD1 
2884 N N   . ASP A 406 ? 0.3294 0.3341 0.3557 -0.0057 -0.0169 0.0620  392 ASP A N   
2885 C CA  . ASP A 406 ? 0.3471 0.3520 0.3791 -0.0076 -0.0213 0.0713  392 ASP A CA  
2886 C C   . ASP A 406 ? 0.3556 0.3659 0.3763 -0.0100 -0.0247 0.0778  392 ASP A C   
2887 O O   . ASP A 406 ? 0.3462 0.3576 0.3706 -0.0122 -0.0290 0.0866  392 ASP A O   
2888 C CB  . ASP A 406 ? 0.3558 0.3571 0.4054 -0.0062 -0.0248 0.0733  392 ASP A CB  
2889 C CG  . ASP A 406 ? 0.3975 0.3939 0.4597 -0.0044 -0.0216 0.0674  392 ASP A CG  
2890 O OD1 . ASP A 406 ? 0.4089 0.4039 0.4711 -0.0053 -0.0194 0.0672  392 ASP A OD1 
2891 O OD2 . ASP A 406 ? 0.4458 0.4404 0.5183 -0.0020 -0.0214 0.0628  392 ASP A OD2 
2892 N N   . LEU A 407 ? 0.3330 0.3466 0.3408 -0.0096 -0.0234 0.0736  393 LEU A N   
2893 C CA  . LEU A 407 ? 0.3345 0.3539 0.3303 -0.0120 -0.0262 0.0784  393 LEU A CA  
2894 C C   . LEU A 407 ? 0.3379 0.3610 0.3258 -0.0147 -0.0242 0.0820  393 LEU A C   
2895 O O   . LEU A 407 ? 0.3140 0.3365 0.2989 -0.0141 -0.0194 0.0772  393 LEU A O   
2896 C CB  . LEU A 407 ? 0.3186 0.3404 0.3033 -0.0108 -0.0250 0.0718  393 LEU A CB  
2897 C CG  . LEU A 407 ? 0.3363 0.3565 0.3262 -0.0090 -0.0282 0.0702  393 LEU A CG  
2898 C CD1 . LEU A 407 ? 0.3184 0.3402 0.2987 -0.0077 -0.0265 0.0626  393 LEU A CD1 
2899 C CD2 . LEU A 407 ? 0.3464 0.3689 0.3375 -0.0109 -0.0346 0.0787  393 LEU A CD2 
2900 N N   . ARG A 408 ? 0.3294 0.3569 0.3139 -0.0179 -0.0281 0.0909  394 ARG A N   
2901 C CA  . ARG A 408 ? 0.3387 0.3715 0.3150 -0.0211 -0.0265 0.0955  394 ARG A CA  
2902 C C   . ARG A 408 ? 0.3522 0.3922 0.3114 -0.0221 -0.0251 0.0923  394 ARG A C   
2903 O O   . ARG A 408 ? 0.3218 0.3665 0.2746 -0.0241 -0.0290 0.0966  394 ARG A O   
2904 C CB  . ARG A 408 ? 0.4052 0.4398 0.3877 -0.0246 -0.0316 0.1074  394 ARG A CB  
2905 C CG  . ARG A 408 ? 0.4739 0.5116 0.4550 -0.0275 -0.0295 0.1126  394 ARG A CG  
2906 C CD  . ARG A 408 ? 0.5735 0.6162 0.5551 -0.0323 -0.0350 0.1255  394 ARG A CD  
2907 N NE  . ARG A 408 ? 0.7633 0.8066 0.7504 -0.0349 -0.0343 0.1319  394 ARG A NE  
2908 C CZ  . ARG A 408 ? 0.7938 0.8422 0.7814 -0.0397 -0.0384 0.1438  394 ARG A CZ  
2909 N NH1 . ARG A 408 ? 0.7330 0.7868 0.7153 -0.0427 -0.0436 0.1509  394 ARG A NH1 
2910 N NH2 . ARG A 408 ? 0.8558 0.9044 0.8495 -0.0418 -0.0376 0.1491  394 ARG A NH2 
2911 N N   . LEU A 409 ? 0.3283 0.3694 0.2807 -0.0209 -0.0197 0.0848  395 LEU A N   
2912 C CA  . LEU A 409 ? 0.3495 0.3961 0.2880 -0.0207 -0.0180 0.0789  395 LEU A CA  
2913 C C   . LEU A 409 ? 0.3874 0.4432 0.3145 -0.0245 -0.0176 0.0837  395 LEU A C   
2914 O O   . LEU A 409 ? 0.3799 0.4380 0.3073 -0.0262 -0.0147 0.0866  395 LEU A O   
2915 C CB  . LEU A 409 ? 0.3253 0.3695 0.2624 -0.0179 -0.0127 0.0691  395 LEU A CB  
2916 C CG  . LEU A 409 ? 0.3187 0.3553 0.2647 -0.0145 -0.0123 0.0630  395 LEU A CG  
2917 C CD1 . LEU A 409 ? 0.3263 0.3625 0.2683 -0.0128 -0.0077 0.0542  395 LEU A CD1 
2918 C CD2 . LEU A 409 ? 0.2996 0.3349 0.2470 -0.0134 -0.0165 0.0626  395 LEU A CD2 
2919 N N   . PRO A 410 ? 0.3691 0.4311 0.2855 -0.0259 -0.0200 0.0838  396 PRO A N   
2920 C CA  . PRO A 410 ? 0.3983 0.4706 0.3021 -0.0297 -0.0187 0.0867  396 PRO A CA  
2921 C C   . PRO A 410 ? 0.4045 0.4802 0.3013 -0.0283 -0.0124 0.0778  396 PRO A C   
2922 O O   . PRO A 410 ? 0.3717 0.4413 0.2741 -0.0249 -0.0094 0.0707  396 PRO A O   
2923 C CB  . PRO A 410 ? 0.3788 0.4556 0.2735 -0.0310 -0.0232 0.0870  396 PRO A CB  
2924 C CG  . PRO A 410 ? 0.4034 0.4719 0.3090 -0.0287 -0.0280 0.0884  396 PRO A CG  
2925 C CD  . PRO A 410 ? 0.3527 0.4128 0.2684 -0.0246 -0.0243 0.0819  396 PRO A CD  
2926 N N   . ALA A 411 ? 0.3973 0.4832 0.2822 -0.0312 -0.0103 0.0782  397 ALA A N   
2927 C CA  . ALA A 411 ? 0.4211 0.5112 0.3001 -0.0299 -0.0044 0.0694  397 ALA A CA  
2928 C C   . ALA A 411 ? 0.4152 0.5031 0.2912 -0.0263 -0.0042 0.0584  397 ALA A C   
2929 O O   . ALA A 411 ? 0.3937 0.4809 0.2669 -0.0261 -0.0086 0.0578  397 ALA A O   
2930 C CB  . ALA A 411 ? 0.4462 0.5492 0.3134 -0.0341 -0.0022 0.0721  397 ALA A CB  
2931 N N   . ASP A 412 ? 0.4146 0.5014 0.2918 -0.0238 0.0005  0.0498  398 ASP A N   
2932 C CA  . ASP A 412 ? 0.3933 0.4792 0.2680 -0.0207 0.0010  0.0390  398 ASP A CA  
2933 C C   . ASP A 412 ? 0.3758 0.4529 0.2568 -0.0181 -0.0033 0.0374  398 ASP A C   
2934 O O   . ASP A 412 ? 0.3802 0.4583 0.2568 -0.0174 -0.0063 0.0334  398 ASP A O   
2935 C CB  . ASP A 412 ? 0.4278 0.5239 0.2897 -0.0223 0.0012  0.0350  398 ASP A CB  
2936 C CG  . ASP A 412 ? 0.5501 0.6568 0.4051 -0.0256 0.0055  0.0377  398 ASP A CG  
2937 O OD1 . ASP A 412 ? 0.6539 0.7605 0.5134 -0.0249 0.0101  0.0364  398 ASP A OD1 
2938 O OD2 . ASP A 412 ? 0.6540 0.7697 0.4989 -0.0291 0.0041  0.0415  398 ASP A OD2 
2939 N N   . VAL A 413 ? 0.3584 0.4272 0.2501 -0.0168 -0.0036 0.0402  399 VAL A N   
2940 C CA  . VAL A 413 ? 0.3431 0.4039 0.2421 -0.0143 -0.0068 0.0383  399 VAL A CA  
2941 C C   . VAL A 413 ? 0.3073 0.3629 0.2125 -0.0116 -0.0036 0.0316  399 VAL A C   
2942 O O   . VAL A 413 ? 0.3070 0.3619 0.2154 -0.0119 0.0001  0.0322  399 VAL A O   
2943 C CB  . VAL A 413 ? 0.3237 0.3798 0.2307 -0.0151 -0.0101 0.0467  399 VAL A CB  
2944 C CG1 . VAL A 413 ? 0.3236 0.3720 0.2396 -0.0123 -0.0121 0.0439  399 VAL A CG1 
2945 C CG2 . VAL A 413 ? 0.3559 0.4170 0.2573 -0.0179 -0.0143 0.0536  399 VAL A CG2 
2946 N N   . ASN A 414 ? 0.3024 0.3549 0.2089 -0.0094 -0.0052 0.0254  400 ASN A N   
2947 C CA  . ASN A 414 ? 0.2939 0.3412 0.2072 -0.0073 -0.0032 0.0201  400 ASN A CA  
2948 C C   . ASN A 414 ? 0.2688 0.3094 0.1906 -0.0065 -0.0055 0.0228  400 ASN A C   
2949 O O   . ASN A 414 ? 0.2771 0.3165 0.1996 -0.0058 -0.0093 0.0226  400 ASN A O   
2950 C CB  . ASN A 414 ? 0.2813 0.3299 0.1919 -0.0057 -0.0035 0.0117  400 ASN A CB  
2951 C CG  . ASN A 414 ? 0.3068 0.3509 0.2240 -0.0043 -0.0015 0.0071  400 ASN A CG  
2952 O OD1 . ASN A 414 ? 0.2910 0.3302 0.2147 -0.0042 -0.0007 0.0096  400 ASN A OD1 
2953 N ND2 . ASN A 414 ? 0.2757 0.3219 0.1916 -0.0032 -0.0007 0.0002  400 ASN A ND2 
2954 N N   . PHE A 415 ? 0.2726 0.3092 0.2011 -0.0066 -0.0033 0.0252  401 PHE A N   
2955 C CA  . PHE A 415 ? 0.2725 0.3037 0.2100 -0.0059 -0.0047 0.0275  401 PHE A CA  
2956 C C   . PHE A 415 ? 0.2561 0.2834 0.1984 -0.0047 -0.0027 0.0221  401 PHE A C   
2957 O O   . PHE A 415 ? 0.2522 0.2784 0.1961 -0.0050 0.0005  0.0209  401 PHE A O   
2958 C CB  . PHE A 415 ? 0.2665 0.2963 0.2088 -0.0072 -0.0040 0.0340  401 PHE A CB  
2959 C CG  . PHE A 415 ? 0.2716 0.2963 0.2241 -0.0063 -0.0055 0.0359  401 PHE A CG  
2960 C CD1 . PHE A 415 ? 0.2751 0.2956 0.2344 -0.0055 -0.0030 0.0326  401 PHE A CD1 
2961 C CD2 . PHE A 415 ? 0.2749 0.2995 0.2305 -0.0065 -0.0095 0.0406  401 PHE A CD2 
2962 C CE1 . PHE A 415 ? 0.2795 0.2962 0.2485 -0.0047 -0.0038 0.0334  401 PHE A CE1 
2963 C CE2 . PHE A 415 ? 0.2716 0.2919 0.2379 -0.0055 -0.0106 0.0418  401 PHE A CE2 
2964 C CZ  . PHE A 415 ? 0.2833 0.2999 0.2564 -0.0045 -0.0075 0.0378  401 PHE A CZ  
2965 N N   . ILE A 416 ? 0.2570 0.2825 0.2017 -0.0035 -0.0049 0.0193  402 ILE A N   
2966 C CA  . ILE A 416 ? 0.2571 0.2801 0.2051 -0.0029 -0.0037 0.0144  402 ILE A CA  
2967 C C   . ILE A 416 ? 0.2423 0.2617 0.1984 -0.0026 -0.0038 0.0154  402 ILE A C   
2968 O O   . ILE A 416 ? 0.2337 0.2528 0.1927 -0.0020 -0.0065 0.0165  402 ILE A O   
2969 C CB  . ILE A 416 ? 0.2373 0.2618 0.1823 -0.0021 -0.0061 0.0099  402 ILE A CB  
2970 C CG1 . ILE A 416 ? 0.2572 0.2857 0.1952 -0.0022 -0.0052 0.0074  402 ILE A CG1 
2971 C CG2 . ILE A 416 ? 0.2313 0.2533 0.1812 -0.0020 -0.0056 0.0062  402 ILE A CG2 
2972 C CD1 . ILE A 416 ? 0.2729 0.3029 0.2086 -0.0013 -0.0080 0.0023  402 ILE A CD1 
2973 N N   . VAL A 417 ? 0.2224 0.2397 0.1824 -0.0032 -0.0008 0.0147  403 VAL A N   
2974 C CA  . VAL A 417 ? 0.2365 0.2511 0.2041 -0.0031 0.0001  0.0143  403 VAL A CA  
2975 C C   . VAL A 417 ? 0.2418 0.2553 0.2101 -0.0040 0.0027  0.0105  403 VAL A C   
2976 O O   . VAL A 417 ? 0.2032 0.2172 0.1680 -0.0047 0.0043  0.0096  403 VAL A O   
2977 C CB  . VAL A 417 ? 0.2725 0.2854 0.2455 -0.0031 0.0007  0.0183  403 VAL A CB  
2978 C CG1 . VAL A 417 ? 0.2656 0.2779 0.2373 -0.0041 0.0033  0.0193  403 VAL A CG1 
2979 C CG2 . VAL A 417 ? 0.2846 0.2954 0.2664 -0.0027 0.0014  0.0170  403 VAL A CG2 
2980 N N   . GLN A 418 ? 0.2467 0.2595 0.2197 -0.0043 0.0031  0.0085  404 GLN A N   
2981 C CA  . GLN A 418 ? 0.2447 0.2572 0.2179 -0.0057 0.0049  0.0052  404 GLN A CA  
2982 C C   . GLN A 418 ? 0.2510 0.2623 0.2300 -0.0065 0.0075  0.0042  404 GLN A C   
2983 O O   . GLN A 418 ? 0.2506 0.2630 0.2325 -0.0072 0.0078  0.0022  404 GLN A O   
2984 C CB  . GLN A 418 ? 0.2277 0.2419 0.2002 -0.0061 0.0027  0.0032  404 GLN A CB  
2985 C CG  . GLN A 418 ? 0.2503 0.2648 0.2223 -0.0081 0.0036  0.0008  404 GLN A CG  
2986 C CD  . GLN A 418 ? 0.2249 0.2412 0.1986 -0.0090 0.0013  -0.0003 404 GLN A CD  
2987 O OE1 . GLN A 418 ? 0.2286 0.2460 0.2059 -0.0091 0.0014  -0.0001 404 GLN A OE1 
2988 N NE2 . GLN A 418 ? 0.2204 0.2372 0.1924 -0.0097 -0.0008 -0.0014 404 GLN A NE2 
2989 N N   . PRO A 419 ? 0.2590 0.2683 0.2399 -0.0065 0.0093  0.0054  405 PRO A N   
2990 C CA  . PRO A 419 ? 0.2744 0.2824 0.2620 -0.0068 0.0114  0.0039  405 PRO A CA  
2991 C C   . PRO A 419 ? 0.2718 0.2797 0.2588 -0.0089 0.0139  0.0003  405 PRO A C   
2992 O O   . PRO A 419 ? 0.2484 0.2565 0.2402 -0.0095 0.0158  -0.0024 405 PRO A O   
2993 C CB  . PRO A 419 ? 0.2739 0.2796 0.2646 -0.0060 0.0116  0.0071  405 PRO A CB  
2994 C CG  . PRO A 419 ? 0.2833 0.2901 0.2678 -0.0056 0.0097  0.0108  405 PRO A CG  
2995 C CD  . PRO A 419 ? 0.2495 0.2582 0.2275 -0.0062 0.0093  0.0084  405 PRO A CD  
2996 N N   . LEU A 420 ? 0.2337 0.2419 0.2154 -0.0102 0.0139  0.0000  406 LEU A N   
2997 C CA  . LEU A 420 ? 0.2364 0.2447 0.2173 -0.0127 0.0156  -0.0029 406 LEU A CA  
2998 C C   . LEU A 420 ? 0.2296 0.2409 0.2095 -0.0143 0.0149  -0.0049 406 LEU A C   
2999 O O   . LEU A 420 ? 0.2459 0.2586 0.2277 -0.0160 0.0166  -0.0075 406 LEU A O   
3000 C CB  . LEU A 420 ? 0.2265 0.2340 0.2035 -0.0136 0.0156  -0.0021 406 LEU A CB  
3001 C CG  . LEU A 420 ? 0.2431 0.2509 0.2187 -0.0166 0.0164  -0.0044 406 LEU A CG  
3002 C CD1 . LEU A 420 ? 0.2349 0.2420 0.2137 -0.0181 0.0187  -0.0070 406 LEU A CD1 
3003 C CD2 . LEU A 420 ? 0.2480 0.2547 0.2214 -0.0171 0.0164  -0.0031 406 LEU A CD2 
3004 N N   . TRP A 421 ? 0.2324 0.2451 0.2094 -0.0139 0.0123  -0.0038 407 TRP A N   
3005 C CA  . TRP A 421 ? 0.2190 0.2346 0.1961 -0.0156 0.0111  -0.0047 407 TRP A CA  
3006 C C   . TRP A 421 ? 0.2256 0.2430 0.2070 -0.0146 0.0115  -0.0051 407 TRP A C   
3007 O O   . TRP A 421 ? 0.2084 0.2285 0.1918 -0.0164 0.0131  -0.0071 407 TRP A O   
3008 C CB  . TRP A 421 ? 0.2254 0.2416 0.2000 -0.0153 0.0076  -0.0035 407 TRP A CB  
3009 C CG  . TRP A 421 ? 0.2223 0.2414 0.1976 -0.0177 0.0058  -0.0038 407 TRP A CG  
3010 C CD1 . TRP A 421 ? 0.2208 0.2415 0.1972 -0.0173 0.0027  -0.0030 407 TRP A CD1 
3011 C CD2 . TRP A 421 ? 0.2158 0.2369 0.1908 -0.0214 0.0065  -0.0046 407 TRP A CD2 
3012 N NE1 . TRP A 421 ? 0.2063 0.2299 0.1837 -0.0205 0.0014  -0.0027 407 TRP A NE1 
3013 C CE2 . TRP A 421 ? 0.2081 0.2323 0.1842 -0.0232 0.0038  -0.0036 407 TRP A CE2 
3014 C CE3 . TRP A 421 ? 0.2095 0.2303 0.1832 -0.0237 0.0090  -0.0059 407 TRP A CE3 
3015 C CZ2 . TRP A 421 ? 0.2141 0.2415 0.1899 -0.0275 0.0034  -0.0033 407 TRP A CZ2 
3016 C CZ3 . TRP A 421 ? 0.2029 0.2268 0.1757 -0.0278 0.0087  -0.0061 407 TRP A CZ3 
3017 C CH2 . TRP A 421 ? 0.2004 0.2278 0.1741 -0.0298 0.0060  -0.0046 407 TRP A CH2 
3018 N N   . GLY A 422 ? 0.2299 0.2461 0.2128 -0.0118 0.0102  -0.0033 408 GLY A N   
3019 C CA  . GLY A 422 ? 0.2322 0.2496 0.2207 -0.0106 0.0106  -0.0034 408 GLY A CA  
3020 C C   . GLY A 422 ? 0.2200 0.2409 0.2102 -0.0112 0.0091  -0.0035 408 GLY A C   
3021 O O   . GLY A 422 ? 0.1926 0.2160 0.1877 -0.0116 0.0109  -0.0051 408 GLY A O   
3022 N N   . SER A 423 ? 0.2087 0.2301 0.1956 -0.0113 0.0057  -0.0021 409 SER A N   
3023 C CA  . SER A 423 ? 0.2349 0.2595 0.2237 -0.0122 0.0036  -0.0017 409 SER A CA  
3024 C C   . SER A 423 ? 0.2121 0.2363 0.2037 -0.0096 0.0011  0.0002  409 SER A C   
3025 O O   . SER A 423 ? 0.2151 0.2373 0.2036 -0.0080 -0.0017 0.0016  409 SER A O   
3026 C CB  . SER A 423 ? 0.1976 0.2227 0.1829 -0.0139 0.0007  -0.0012 409 SER A CB  
3027 O OG  . SER A 423 ? 0.2214 0.2501 0.2093 -0.0158 -0.0011 -0.0006 409 SER A OG  
3028 N N   . ILE A 424 ? 0.2033 0.2299 0.2011 -0.0092 0.0020  0.0001  410 ILE A N   
3029 C CA  . ILE A 424 ? 0.2114 0.2377 0.2126 -0.0070 -0.0009 0.0022  410 ILE A CA  
3030 C C   . ILE A 424 ? 0.2168 0.2445 0.2164 -0.0077 -0.0051 0.0034  410 ILE A C   
3031 O O   . ILE A 424 ? 0.1952 0.2255 0.1945 -0.0101 -0.0053 0.0028  410 ILE A O   
3032 C CB  . ILE A 424 ? 0.2286 0.2572 0.2385 -0.0063 0.0012  0.0017  410 ILE A CB  
3033 C CG1 . ILE A 424 ? 0.2291 0.2630 0.2420 -0.0087 0.0031  -0.0002 410 ILE A CG1 
3034 C CG2 . ILE A 424 ? 0.2426 0.2691 0.2556 -0.0053 0.0046  0.0003  410 ILE A CG2 
3035 C CD1 . ILE A 424 ? 0.2500 0.2874 0.2724 -0.0077 0.0041  -0.0004 410 ILE A CD1 
3036 N N   . GLY A 425 ? 0.2155 0.2416 0.2144 -0.0057 -0.0088 0.0053  411 GLY A N   
3037 C CA  . GLY A 425 ? 0.2219 0.2482 0.2186 -0.0059 -0.0134 0.0058  411 GLY A CA  
3038 C C   . GLY A 425 ? 0.2150 0.2388 0.2047 -0.0055 -0.0149 0.0049  411 GLY A C   
3039 O O   . GLY A 425 ? 0.2196 0.2429 0.2074 -0.0047 -0.0190 0.0048  411 GLY A O   
3040 N N   . TYR A 426 ? 0.2153 0.2378 0.2017 -0.0060 -0.0116 0.0037  412 TYR A N   
3041 C CA  . TYR A 426 ? 0.2092 0.2300 0.1896 -0.0055 -0.0124 0.0026  412 TYR A CA  
3042 C C   . TYR A 426 ? 0.2238 0.2438 0.2009 -0.0034 -0.0149 0.0035  412 TYR A C   
3043 O O   . TYR A 426 ? 0.2377 0.2578 0.2112 -0.0029 -0.0175 0.0019  412 TYR A O   
3044 C CB  . TYR A 426 ? 0.2159 0.2355 0.1942 -0.0061 -0.0082 0.0019  412 TYR A CB  
3045 C CG  . TYR A 426 ? 0.2215 0.2398 0.1943 -0.0052 -0.0082 0.0012  412 TYR A CG  
3046 C CD1 . TYR A 426 ? 0.1960 0.2145 0.1670 -0.0059 -0.0093 -0.0009 412 TYR A CD1 
3047 C CD2 . TYR A 426 ? 0.2110 0.2286 0.1811 -0.0039 -0.0072 0.0029  412 TYR A CD2 
3048 C CE1 . TYR A 426 ? 0.2290 0.2472 0.1956 -0.0050 -0.0089 -0.0021 412 TYR A CE1 
3049 C CE2 . TYR A 426 ? 0.2324 0.2501 0.1973 -0.0034 -0.0069 0.0023  412 TYR A CE2 
3050 C CZ  . TYR A 426 ? 0.2220 0.2402 0.1851 -0.0038 -0.0074 -0.0006 412 TYR A CZ  
3051 O OH  . TYR A 426 ? 0.2379 0.2571 0.1964 -0.0032 -0.0066 -0.0017 412 TYR A OH  
3052 N N   . THR A 427 ? 0.2135 0.2333 0.1922 -0.0024 -0.0143 0.0059  413 THR A N   
3053 C CA  . THR A 427 ? 0.2269 0.2464 0.2013 -0.0011 -0.0162 0.0076  413 THR A CA  
3054 C C   . THR A 427 ? 0.1954 0.2158 0.1682 -0.0006 -0.0211 0.0072  413 THR A C   
3055 O O   . THR A 427 ? 0.2314 0.2524 0.1980 -0.0001 -0.0227 0.0060  413 THR A O   
3056 C CB  . THR A 427 ? 0.2400 0.2589 0.2182 -0.0005 -0.0151 0.0110  413 THR A CB  
3057 O OG1 . THR A 427 ? 0.2226 0.2403 0.2017 -0.0010 -0.0109 0.0108  413 THR A OG1 
3058 C CG2 . THR A 427 ? 0.2199 0.2392 0.1937 0.0001  -0.0178 0.0139  413 THR A CG2 
3059 N N   . LEU A 428 ? 0.2063 0.2274 0.1847 -0.0006 -0.0235 0.0079  414 LEU A N   
3060 C CA  . LEU A 428 ? 0.2324 0.2541 0.2098 -0.0002 -0.0286 0.0076  414 LEU A CA  
3061 C C   . LEU A 428 ? 0.2377 0.2594 0.2116 -0.0004 -0.0304 0.0036  414 LEU A C   
3062 O O   . LEU A 428 ? 0.2339 0.2560 0.2035 0.0003  -0.0337 0.0019  414 LEU A O   
3063 C CB  . LEU A 428 ? 0.2051 0.2277 0.1903 -0.0004 -0.0309 0.0092  414 LEU A CB  
3064 C CG  . LEU A 428 ? 0.2008 0.2239 0.1862 -0.0001 -0.0367 0.0088  414 LEU A CG  
3065 C CD1 . LEU A 428 ? 0.2135 0.2366 0.1948 0.0008  -0.0397 0.0107  414 LEU A CD1 
3066 C CD2 . LEU A 428 ? 0.2034 0.2279 0.1977 -0.0008 -0.0383 0.0104  414 LEU A CD2 
3067 N N   . ALA A 429 ? 0.2125 0.2339 0.1888 -0.0015 -0.0285 0.0020  415 ALA A N   
3068 C CA  . ALA A 429 ? 0.2371 0.2584 0.2124 -0.0018 -0.0306 -0.0015 415 ALA A CA  
3069 C C   . ALA A 429 ? 0.2374 0.2585 0.2062 -0.0011 -0.0284 -0.0041 415 ALA A C   
3070 O O   . ALA A 429 ? 0.2188 0.2402 0.1853 -0.0003 -0.0309 -0.0076 415 ALA A O   
3071 C CB  . ALA A 429 ? 0.2082 0.2296 0.1887 -0.0038 -0.0298 -0.0015 415 ALA A CB  
3072 N N   . ALA A 430 ? 0.2199 0.2408 0.1865 -0.0012 -0.0239 -0.0026 416 ALA A N   
3073 C CA  . ALA A 430 ? 0.2381 0.2595 0.1987 -0.0007 -0.0216 -0.0043 416 ALA A CA  
3074 C C   . ALA A 430 ? 0.2453 0.2684 0.2001 0.0004  -0.0236 -0.0046 416 ALA A C   
3075 O O   . ALA A 430 ? 0.2259 0.2508 0.1759 0.0009  -0.0234 -0.0079 416 ALA A O   
3076 C CB  . ALA A 430 ? 0.2291 0.2499 0.1892 -0.0013 -0.0168 -0.0018 416 ALA A CB  
3077 N N   . ALA A 431 ? 0.2333 0.2565 0.1885 0.0006  -0.0256 -0.0013 417 ALA A N   
3078 C CA  . ALA A 431 ? 0.2461 0.2714 0.1953 0.0011  -0.0282 -0.0009 417 ALA A CA  
3079 C C   . ALA A 431 ? 0.2485 0.2748 0.1960 0.0016  -0.0321 -0.0059 417 ALA A C   
3080 O O   . ALA A 431 ? 0.2610 0.2900 0.2017 0.0019  -0.0328 -0.0084 417 ALA A O   
3081 C CB  . ALA A 431 ? 0.2500 0.2749 0.2019 0.0010  -0.0304 0.0040  417 ALA A CB  
3082 N N   . PHE A 432 ? 0.2372 0.2619 0.1913 0.0016  -0.0348 -0.0075 418 PHE A N   
3083 C CA  . PHE A 432 ? 0.2422 0.2673 0.1965 0.0022  -0.0391 -0.0126 418 PHE A CA  
3084 C C   . PHE A 432 ? 0.2567 0.2829 0.2086 0.0027  -0.0370 -0.0178 418 PHE A C   
3085 O O   . PHE A 432 ? 0.2594 0.2874 0.2079 0.0036  -0.0390 -0.0229 418 PHE A O   
3086 C CB  . PHE A 432 ? 0.2584 0.2815 0.2215 0.0017  -0.0425 -0.0122 418 PHE A CB  
3087 C CG  . PHE A 432 ? 0.2607 0.2835 0.2265 0.0022  -0.0470 -0.0175 418 PHE A CG  
3088 C CD1 . PHE A 432 ? 0.2539 0.2777 0.2167 0.0031  -0.0513 -0.0205 418 PHE A CD1 
3089 C CD2 . PHE A 432 ? 0.2371 0.2587 0.2091 0.0017  -0.0472 -0.0196 418 PHE A CD2 
3090 C CE1 . PHE A 432 ? 0.2575 0.2808 0.2238 0.0037  -0.0557 -0.0261 418 PHE A CE1 
3091 C CE2 . PHE A 432 ? 0.2412 0.2622 0.2176 0.0022  -0.0518 -0.0245 418 PHE A CE2 
3092 C CZ  . PHE A 432 ? 0.2639 0.2856 0.2377 0.0034  -0.0560 -0.0281 418 PHE A CZ  
3093 N N   . GLY A 433 ? 0.2298 0.2550 0.1839 0.0022  -0.0329 -0.0171 419 GLY A N   
3094 C CA  . GLY A 433 ? 0.2659 0.2924 0.2184 0.0027  -0.0305 -0.0215 419 GLY A CA  
3095 C C   . GLY A 433 ? 0.2544 0.2844 0.1981 0.0031  -0.0275 -0.0222 419 GLY A C   
3096 O O   . GLY A 433 ? 0.2787 0.3115 0.2195 0.0038  -0.0271 -0.0276 419 GLY A O   
3097 N N   . ALA A 434 ? 0.2648 0.2953 0.2047 0.0023  -0.0252 -0.0167 420 ALA A N   
3098 C CA  . ALA A 434 ? 0.2734 0.3078 0.2050 0.0021  -0.0225 -0.0160 420 ALA A CA  
3099 C C   . ALA A 434 ? 0.2920 0.3301 0.2172 0.0024  -0.0257 -0.0189 420 ALA A C   
3100 O O   . ALA A 434 ? 0.2971 0.3399 0.2160 0.0024  -0.0239 -0.0225 420 ALA A O   
3101 C CB  . ALA A 434 ? 0.2740 0.3075 0.2047 0.0011  -0.0204 -0.0088 420 ALA A CB  
3102 N N   . GLN A 435 ? 0.2570 0.2936 0.1836 0.0024  -0.0305 -0.0177 421 GLN A N   
3103 C CA  . GLN A 435 ? 0.3011 0.3411 0.2217 0.0025  -0.0342 -0.0208 421 GLN A CA  
3104 C C   . GLN A 435 ? 0.3088 0.3502 0.2301 0.0037  -0.0353 -0.0297 421 GLN A C   
3105 O O   . GLN A 435 ? 0.2907 0.3370 0.2047 0.0037  -0.0355 -0.0344 421 GLN A O   
3106 C CB  . GLN A 435 ? 0.2716 0.3092 0.1951 0.0023  -0.0394 -0.0175 421 GLN A CB  
3107 C CG  . GLN A 435 ? 0.3008 0.3420 0.2168 0.0018  -0.0436 -0.0192 421 GLN A CG  
3108 C CD  . GLN A 435 ? 0.3350 0.3801 0.2425 0.0001  -0.0424 -0.0136 421 GLN A CD  
3109 O OE1 . GLN A 435 ? 0.3287 0.3725 0.2376 -0.0008 -0.0449 -0.0071 421 GLN A OE1 
3110 N NE2 . GLN A 435 ? 0.3159 0.3661 0.2151 -0.0006 -0.0388 -0.0160 421 GLN A NE2 
3111 N N   . THR A 436 ? 0.2815 0.3191 0.2120 0.0046  -0.0363 -0.0323 422 THR A N   
3112 C CA  . THR A 436 ? 0.3064 0.3449 0.2399 0.0059  -0.0376 -0.0408 422 THR A CA  
3113 C C   . THR A 436 ? 0.3051 0.3483 0.2336 0.0062  -0.0325 -0.0449 422 THR A C   
3114 O O   . THR A 436 ? 0.3231 0.3705 0.2484 0.0070  -0.0330 -0.0522 422 THR A O   
3115 C CB  . THR A 436 ? 0.2897 0.3234 0.2348 0.0062  -0.0393 -0.0413 422 THR A CB  
3116 O OG1 . THR A 436 ? 0.2730 0.3034 0.2229 0.0056  -0.0436 -0.0369 422 THR A OG1 
3117 C CG2 . THR A 436 ? 0.2789 0.3132 0.2293 0.0076  -0.0419 -0.0499 422 THR A CG2 
3118 N N   . ALA A 437 ? 0.2813 0.3244 0.2093 0.0055  -0.0275 -0.0404 423 ALA A N   
3119 C CA  . ALA A 437 ? 0.3087 0.3567 0.2325 0.0055  -0.0224 -0.0434 423 ALA A CA  
3120 C C   . ALA A 437 ? 0.3192 0.3739 0.2313 0.0047  -0.0212 -0.0439 423 ALA A C   
3121 O O   . ALA A 437 ? 0.3164 0.3770 0.2247 0.0051  -0.0188 -0.0502 423 ALA A O   
3122 C CB  . ALA A 437 ? 0.2667 0.3129 0.1924 0.0046  -0.0179 -0.0375 423 ALA A CB  
3123 N N   . CYS A 438 ? 0.3092 0.3639 0.2160 0.0033  -0.0229 -0.0373 424 CYS A N   
3124 C CA  . CYS A 438 ? 0.3420 0.4034 0.2374 0.0016  -0.0218 -0.0355 424 CYS A CA  
3125 C C   . CYS A 438 ? 0.3352 0.3964 0.2268 0.0010  -0.0276 -0.0343 424 CYS A C   
3126 O O   . CYS A 438 ? 0.3289 0.3888 0.2186 -0.0004 -0.0291 -0.0263 424 CYS A O   
3127 C CB  . CYS A 438 ? 0.3303 0.3924 0.2230 -0.0002 -0.0181 -0.0268 424 CYS A CB  
3128 S SG  . CYS A 438 ? 0.3465 0.4074 0.2450 0.0003  -0.0119 -0.0269 424 CYS A SG  
3129 N N   . PRO A 439 ? 0.3327 0.3951 0.2242 0.0021  -0.0311 -0.0422 425 PRO A N   
3130 C CA  . PRO A 439 ? 0.3522 0.4144 0.2404 0.0014  -0.0371 -0.0414 425 PRO A CA  
3131 C C   . PRO A 439 ? 0.3806 0.4488 0.2569 -0.0012 -0.0372 -0.0365 425 PRO A C   
3132 O O   . PRO A 439 ? 0.3710 0.4378 0.2458 -0.0023 -0.0421 -0.0320 425 PRO A O   
3133 C CB  . PRO A 439 ? 0.3374 0.4011 0.2269 0.0030  -0.0399 -0.0525 425 PRO A CB  
3134 C CG  . PRO A 439 ? 0.3413 0.4089 0.2313 0.0041  -0.0344 -0.0590 425 PRO A CG  
3135 C CD  . PRO A 439 ? 0.3382 0.4021 0.2335 0.0040  -0.0301 -0.0525 425 PRO A CD  
3136 N N   . ASN A 440 ? 0.3977 0.4730 0.2657 -0.0026 -0.0324 -0.0370 426 ASN A N   
3137 C CA  . ASN A 440 ? 0.4010 0.4832 0.2571 -0.0058 -0.0329 -0.0321 426 ASN A CA  
3138 C C   . ASN A 440 ? 0.4021 0.4832 0.2583 -0.0077 -0.0312 -0.0203 426 ASN A C   
3139 O O   . ASN A 440 ? 0.4346 0.5214 0.2819 -0.0108 -0.0319 -0.0146 426 ASN A O   
3140 C CB  . ASN A 440 ? 0.4392 0.5317 0.2852 -0.0069 -0.0289 -0.0388 426 ASN A CB  
3141 C CG  . ASN A 440 ? 0.4408 0.5352 0.2870 -0.0049 -0.0304 -0.0517 426 ASN A CG  
3142 O OD1 . ASN A 440 ? 0.4348 0.5269 0.2814 -0.0044 -0.0363 -0.0545 426 ASN A OD1 
3143 N ND2 . ASN A 440 ? 0.4851 0.5842 0.3316 -0.0036 -0.0254 -0.0597 426 ASN A ND2 
3144 N N   . ARG A 441 ? 0.3896 0.4638 0.2559 -0.0063 -0.0292 -0.0166 427 ARG A N   
3145 C CA  . ARG A 441 ? 0.3823 0.4545 0.2506 -0.0078 -0.0279 -0.0062 427 ARG A CA  
3146 C C   . ARG A 441 ? 0.3633 0.4287 0.2390 -0.0074 -0.0327 -0.0003 427 ARG A C   
3147 O O   . ARG A 441 ? 0.3553 0.4157 0.2375 -0.0054 -0.0354 -0.0041 427 ARG A O   
3148 C CB  . ARG A 441 ? 0.3264 0.3962 0.2008 -0.0068 -0.0222 -0.0059 427 ARG A CB  
3149 C CG  . ARG A 441 ? 0.3514 0.4289 0.2190 -0.0076 -0.0171 -0.0098 427 ARG A CG  
3150 C CD  . ARG A 441 ? 0.3498 0.4249 0.2236 -0.0069 -0.0118 -0.0086 427 ARG A CD  
3151 N NE  . ARG A 441 ? 0.3201 0.3926 0.1967 -0.0085 -0.0112 0.0013  427 ARG A NE  
3152 C CZ  . ARG A 441 ? 0.3573 0.4287 0.2379 -0.0087 -0.0069 0.0040  427 ARG A CZ  
3153 N NH1 . ARG A 441 ? 0.3510 0.4236 0.2332 -0.0075 -0.0028 -0.0020 427 ARG A NH1 
3154 N NH2 . ARG A 441 ? 0.3252 0.3936 0.2092 -0.0100 -0.0071 0.0128  427 ARG A NH2 
3155 N N   . ARG A 442 ? 0.3537 0.4193 0.2289 -0.0095 -0.0338 0.0091  428 ARG A N   
3156 C CA  . ARG A 442 ? 0.3533 0.4132 0.2365 -0.0092 -0.0381 0.0150  428 ARG A CA  
3157 C C   . ARG A 442 ? 0.3136 0.3666 0.2084 -0.0072 -0.0351 0.0163  428 ARG A C   
3158 O O   . ARG A 442 ? 0.3132 0.3662 0.2094 -0.0077 -0.0309 0.0192  428 ARG A O   
3159 C CB  . ARG A 442 ? 0.3299 0.3926 0.2098 -0.0122 -0.0408 0.0248  428 ARG A CB  
3160 C CG  . ARG A 442 ? 0.3264 0.3844 0.2143 -0.0120 -0.0462 0.0305  428 ARG A CG  
3161 C CD  . ARG A 442 ? 0.3132 0.3751 0.1971 -0.0155 -0.0501 0.0398  428 ARG A CD  
3162 N NE  . ARG A 442 ? 0.3157 0.3772 0.2034 -0.0167 -0.0472 0.0471  428 ARG A NE  
3163 C CZ  . ARG A 442 ? 0.3584 0.4218 0.2467 -0.0196 -0.0506 0.0568  428 ARG A CZ  
3164 N NH1 . ARG A 442 ? 0.3089 0.3749 0.1934 -0.0218 -0.0568 0.0609  428 ARG A NH1 
3165 N NH2 . ARG A 442 ? 0.3625 0.4250 0.2558 -0.0205 -0.0480 0.0629  428 ARG A NH2 
3166 N N   . VAL A 443 ? 0.3245 0.3722 0.2275 -0.0053 -0.0374 0.0142  429 VAL A N   
3167 C CA  . VAL A 443 ? 0.2766 0.3186 0.1901 -0.0037 -0.0348 0.0145  429 VAL A CA  
3168 C C   . VAL A 443 ? 0.2903 0.3289 0.2120 -0.0038 -0.0375 0.0210  429 VAL A C   
3169 O O   . VAL A 443 ? 0.3204 0.3583 0.2440 -0.0036 -0.0423 0.0216  429 VAL A O   
3170 C CB  . VAL A 443 ? 0.2718 0.3113 0.1893 -0.0018 -0.0349 0.0072  429 VAL A CB  
3171 C CG1 . VAL A 443 ? 0.2673 0.3016 0.1957 -0.0008 -0.0334 0.0085  429 VAL A CG1 
3172 C CG2 . VAL A 443 ? 0.2733 0.3155 0.1858 -0.0014 -0.0314 0.0008  429 VAL A CG2 
3173 N N   . ILE A 444 ? 0.2713 0.3078 0.1986 -0.0039 -0.0346 0.0256  430 ILE A N   
3174 C CA  . ILE A 444 ? 0.2701 0.3033 0.2073 -0.0037 -0.0364 0.0310  430 ILE A CA  
3175 C C   . ILE A 444 ? 0.2794 0.3083 0.2258 -0.0021 -0.0329 0.0283  430 ILE A C   
3176 O O   . ILE A 444 ? 0.2743 0.3025 0.2208 -0.0020 -0.0283 0.0270  430 ILE A O   
3177 C CB  . ILE A 444 ? 0.2859 0.3201 0.2237 -0.0054 -0.0366 0.0387  430 ILE A CB  
3178 C CG1 . ILE A 444 ? 0.2886 0.3279 0.2165 -0.0077 -0.0406 0.0421  430 ILE A CG1 
3179 C CG2 . ILE A 444 ? 0.2759 0.3063 0.2263 -0.0047 -0.0382 0.0434  430 ILE A CG2 
3180 C CD1 . ILE A 444 ? 0.3074 0.3504 0.2296 -0.0101 -0.0388 0.0470  430 ILE A CD1 
3181 N N   . VAL A 445 ? 0.2802 0.3070 0.2343 -0.0010 -0.0350 0.0277  431 VAL A N   
3182 C CA  . VAL A 445 ? 0.2840 0.3080 0.2462 0.0000  -0.0320 0.0249  431 VAL A CA  
3183 C C   . VAL A 445 ? 0.2721 0.2942 0.2450 0.0004  -0.0319 0.0292  431 VAL A C   
3184 O O   . VAL A 445 ? 0.2752 0.2975 0.2530 0.0006  -0.0359 0.0320  431 VAL A O   
3185 C CB  . VAL A 445 ? 0.2875 0.3114 0.2510 0.0007  -0.0341 0.0206  431 VAL A CB  
3186 C CG1 . VAL A 445 ? 0.2725 0.2947 0.2427 0.0010  -0.0306 0.0179  431 VAL A CG1 
3187 C CG2 . VAL A 445 ? 0.2773 0.3032 0.2316 0.0005  -0.0357 0.0164  431 VAL A CG2 
3188 N N   . LEU A 446 ? 0.2472 0.2677 0.2246 0.0006  -0.0276 0.0293  432 LEU A N   
3189 C CA  . LEU A 446 ? 0.2865 0.3052 0.2755 0.0012  -0.0268 0.0317  432 LEU A CA  
3190 C C   . LEU A 446 ? 0.2583 0.2763 0.2532 0.0018  -0.0233 0.0271  432 LEU A C   
3191 O O   . LEU A 446 ? 0.2540 0.2712 0.2476 0.0015  -0.0191 0.0242  432 LEU A O   
3192 C CB  . LEU A 446 ? 0.2677 0.2852 0.2582 0.0007  -0.0248 0.0351  432 LEU A CB  
3193 C CG  . LEU A 446 ? 0.2821 0.3014 0.2661 -0.0007 -0.0281 0.0405  432 LEU A CG  
3194 C CD1 . LEU A 446 ? 0.2853 0.3044 0.2665 -0.0017 -0.0253 0.0425  432 LEU A CD1 
3195 C CD2 . LEU A 446 ? 0.3155 0.3345 0.3079 -0.0007 -0.0328 0.0462  432 LEU A CD2 
3196 N N   . THR A 447 ? 0.2686 0.2873 0.2700 0.0024  -0.0252 0.0265  433 THR A N   
3197 C CA  . THR A 447 ? 0.2519 0.2713 0.2586 0.0025  -0.0220 0.0226  433 THR A CA  
3198 C C   . THR A 447 ? 0.2905 0.3106 0.3098 0.0033  -0.0220 0.0237  433 THR A C   
3199 O O   . THR A 447 ? 0.2651 0.2855 0.2886 0.0039  -0.0261 0.0272  433 THR A O   
3200 C CB  . THR A 447 ? 0.2422 0.2630 0.2442 0.0019  -0.0236 0.0198  433 THR A CB  
3201 O OG1 . THR A 447 ? 0.2312 0.2534 0.2388 0.0014  -0.0208 0.0170  433 THR A OG1 
3202 C CG2 . THR A 447 ? 0.2561 0.2778 0.2587 0.0022  -0.0292 0.0220  433 THR A CG2 
3203 N N   . GLY A 448 ? 0.2821 0.3028 0.3074 0.0033  -0.0174 0.0205  434 GLY A N   
3204 C CA  . GLY A 448 ? 0.2628 0.2855 0.3004 0.0041  -0.0166 0.0200  434 GLY A CA  
3205 C C   . GLY A 448 ? 0.2719 0.2976 0.3107 0.0036  -0.0185 0.0193  434 GLY A C   
3206 O O   . GLY A 448 ? 0.2554 0.2816 0.2861 0.0025  -0.0198 0.0183  434 GLY A O   
3207 N N   . ASP A 449 ? 0.2681 0.2961 0.3184 0.0044  -0.0189 0.0199  435 ASP A N   
3208 C CA  . ASP A 449 ? 0.2694 0.3009 0.3223 0.0038  -0.0206 0.0196  435 ASP A CA  
3209 C C   . ASP A 449 ? 0.2625 0.2972 0.3128 0.0019  -0.0163 0.0156  435 ASP A C   
3210 O O   . ASP A 449 ? 0.2525 0.2889 0.2990 0.0006  -0.0183 0.0156  435 ASP A O   
3211 C CB  . ASP A 449 ? 0.2781 0.3120 0.3450 0.0050  -0.0215 0.0211  435 ASP A CB  
3212 C CG  . ASP A 449 ? 0.3262 0.3613 0.4039 0.0060  -0.0164 0.0184  435 ASP A CG  
3213 O OD1 . ASP A 449 ? 0.3100 0.3426 0.3857 0.0063  -0.0136 0.0169  435 ASP A OD1 
3214 O OD2 . ASP A 449 ? 0.3639 0.4031 0.4534 0.0065  -0.0151 0.0173  435 ASP A OD2 
3215 N N   . GLY A 450 ? 0.2575 0.2931 0.3101 0.0017  -0.0108 0.0122  436 GLY A N   
3216 C CA  . GLY A 450 ? 0.2509 0.2898 0.2999 -0.0007 -0.0070 0.0088  436 GLY A CA  
3217 C C   . GLY A 450 ? 0.2441 0.2807 0.2811 -0.0021 -0.0085 0.0089  436 GLY A C   
3218 O O   . GLY A 450 ? 0.2098 0.2489 0.2439 -0.0041 -0.0096 0.0087  436 GLY A O   
3219 N N   . ALA A 451 ? 0.2333 0.2653 0.2641 -0.0012 -0.0090 0.0095  437 ALA A N   
3220 C CA  . ALA A 451 ? 0.2429 0.2729 0.2632 -0.0023 -0.0099 0.0090  437 ALA A CA  
3221 C C   . ALA A 451 ? 0.2362 0.2662 0.2529 -0.0026 -0.0151 0.0105  437 ALA A C   
3222 O O   . ALA A 451 ? 0.2061 0.2369 0.2186 -0.0043 -0.0158 0.0094  437 ALA A O   
3223 C CB  . ALA A 451 ? 0.2241 0.2499 0.2394 -0.0012 -0.0096 0.0098  437 ALA A CB  
3224 N N   . ALA A 452 ? 0.2167 0.2458 0.2355 -0.0011 -0.0191 0.0132  438 ALA A N   
3225 C CA  . ALA A 452 ? 0.2254 0.2543 0.2409 -0.0012 -0.0245 0.0141  438 ALA A CA  
3226 C C   . ALA A 452 ? 0.2178 0.2501 0.2375 -0.0028 -0.0257 0.0138  438 ALA A C   
3227 O O   . ALA A 452 ? 0.2324 0.2643 0.2489 -0.0035 -0.0295 0.0135  438 ALA A O   
3228 C CB  . ALA A 452 ? 0.2244 0.2523 0.2420 0.0004  -0.0288 0.0172  438 ALA A CB  
3229 N N   . GLN A 453 ? 0.2137 0.2497 0.2409 -0.0037 -0.0224 0.0135  439 GLN A N   
3230 C CA  . GLN A 453 ? 0.2297 0.2701 0.2612 -0.0058 -0.0234 0.0139  439 GLN A CA  
3231 C C   . GLN A 453 ? 0.2216 0.2623 0.2476 -0.0083 -0.0231 0.0126  439 GLN A C   
3232 O O   . GLN A 453 ? 0.2164 0.2590 0.2439 -0.0100 -0.0266 0.0138  439 GLN A O   
3233 C CB  . GLN A 453 ? 0.2153 0.2608 0.2556 -0.0065 -0.0190 0.0134  439 GLN A CB  
3234 C CG  . GLN A 453 ? 0.2435 0.2890 0.2920 -0.0041 -0.0195 0.0148  439 GLN A CG  
3235 C CD  . GLN A 453 ? 0.2517 0.3036 0.3106 -0.0048 -0.0156 0.0139  439 GLN A CD  
3236 O OE1 . GLN A 453 ? 0.2868 0.3423 0.3455 -0.0066 -0.0105 0.0111  439 GLN A OE1 
3237 N NE2 . GLN A 453 ? 0.2470 0.3006 0.3150 -0.0035 -0.0180 0.0160  439 GLN A NE2 
3238 N N   . LEU A 454 ? 0.1901 0.2292 0.2106 -0.0087 -0.0194 0.0105  440 LEU A N   
3239 C CA  . LEU A 454 ? 0.2218 0.2618 0.2384 -0.0114 -0.0189 0.0096  440 LEU A CA  
3240 C C   . LEU A 454 ? 0.2095 0.2463 0.2219 -0.0112 -0.0241 0.0098  440 LEU A C   
3241 O O   . LEU A 454 ? 0.1945 0.2324 0.2065 -0.0136 -0.0256 0.0099  440 LEU A O   
3242 C CB  . LEU A 454 ? 0.1940 0.2329 0.2063 -0.0118 -0.0139 0.0073  440 LEU A CB  
3243 C CG  . LEU A 454 ? 0.2127 0.2560 0.2290 -0.0132 -0.0084 0.0059  440 LEU A CG  
3244 C CD1 . LEU A 454 ? 0.2022 0.2446 0.2237 -0.0103 -0.0060 0.0053  440 LEU A CD1 
3245 C CD2 . LEU A 454 ? 0.1878 0.2310 0.1991 -0.0152 -0.0048 0.0038  440 LEU A CD2 
3246 N N   . THR A 455 ? 0.2174 0.2505 0.2269 -0.0085 -0.0269 0.0096  441 THR A N   
3247 C CA  . THR A 455 ? 0.1997 0.2299 0.2048 -0.0080 -0.0312 0.0084  441 THR A CA  
3248 C C   . THR A 455 ? 0.2176 0.2467 0.2236 -0.0062 -0.0364 0.0091  441 THR A C   
3249 O O   . THR A 455 ? 0.2168 0.2435 0.2181 -0.0050 -0.0393 0.0072  441 THR A O   
3250 C CB  . THR A 455 ? 0.2081 0.2355 0.2062 -0.0069 -0.0286 0.0063  441 THR A CB  
3251 O OG1 . THR A 455 ? 0.2094 0.2356 0.2057 -0.0049 -0.0267 0.0071  441 THR A OG1 
3252 C CG2 . THR A 455 ? 0.2061 0.2343 0.2033 -0.0089 -0.0243 0.0055  441 THR A CG2 
3253 N N   . ILE A 456 ? 0.2311 0.2625 0.2435 -0.0062 -0.0376 0.0114  442 ILE A N   
3254 C CA  . ILE A 456 ? 0.2134 0.2437 0.2267 -0.0046 -0.0424 0.0126  442 ILE A CA  
3255 C C   . ILE A 456 ? 0.2273 0.2561 0.2392 -0.0048 -0.0484 0.0110  442 ILE A C   
3256 O O   . ILE A 456 ? 0.2429 0.2700 0.2514 -0.0033 -0.0521 0.0102  442 ILE A O   
3257 C CB  . ILE A 456 ? 0.2115 0.2449 0.2336 -0.0049 -0.0427 0.0155  442 ILE A CB  
3258 C CG1 . ILE A 456 ? 0.2397 0.2718 0.2628 -0.0032 -0.0477 0.0172  442 ILE A CG1 
3259 C CG2 . ILE A 456 ? 0.2070 0.2438 0.2354 -0.0073 -0.0445 0.0166  442 ILE A CG2 
3260 C CD1 . ILE A 456 ? 0.2316 0.2610 0.2481 -0.0014 -0.0470 0.0170  442 ILE A CD1 
3261 N N   . GLN A 457 ? 0.2331 0.2628 0.2479 -0.0067 -0.0497 0.0105  443 GLN A N   
3262 C CA  . GLN A 457 ? 0.2163 0.2445 0.2323 -0.0068 -0.0561 0.0090  443 GLN A CA  
3263 C C   . GLN A 457 ? 0.2428 0.2678 0.2513 -0.0050 -0.0573 0.0046  443 GLN A C   
3264 O O   . GLN A 457 ? 0.2297 0.2533 0.2385 -0.0043 -0.0627 0.0023  443 GLN A O   
3265 C CB  . GLN A 457 ? 0.2186 0.2484 0.2405 -0.0096 -0.0577 0.0099  443 GLN A CB  
3266 C CG  . GLN A 457 ? 0.1979 0.2279 0.2171 -0.0111 -0.0533 0.0091  443 GLN A CG  
3267 C CD  . GLN A 457 ? 0.2033 0.2373 0.2242 -0.0129 -0.0478 0.0118  443 GLN A CD  
3268 O OE1 . GLN A 457 ? 0.1868 0.2205 0.2037 -0.0117 -0.0427 0.0111  443 GLN A OE1 
3269 N NE2 . GLN A 457 ? 0.1881 0.2260 0.2154 -0.0160 -0.0488 0.0149  443 GLN A NE2 
3270 N N   . GLU A 458 ? 0.2202 0.2445 0.2223 -0.0042 -0.0523 0.0033  444 GLU A N   
3271 C CA  . GLU A 458 ? 0.2315 0.2539 0.2264 -0.0026 -0.0529 -0.0008 444 GLU A CA  
3272 C C   . GLU A 458 ? 0.2546 0.2768 0.2444 -0.0010 -0.0547 -0.0009 444 GLU A C   
3273 O O   . GLU A 458 ? 0.2496 0.2713 0.2333 0.0001  -0.0561 -0.0047 444 GLU A O   
3274 C CB  . GLU A 458 ? 0.2316 0.2536 0.2215 -0.0026 -0.0471 -0.0019 444 GLU A CB  
3275 C CG  . GLU A 458 ? 0.2105 0.2315 0.1985 -0.0023 -0.0480 -0.0064 444 GLU A CG  
3276 C CD  . GLU A 458 ? 0.2232 0.2438 0.2190 -0.0038 -0.0523 -0.0068 444 GLU A CD  
3277 O OE1 . GLU A 458 ? 0.2161 0.2380 0.2172 -0.0059 -0.0516 -0.0032 444 GLU A OE1 
3278 O OE2 . GLU A 458 ? 0.2451 0.2647 0.2425 -0.0031 -0.0563 -0.0109 444 GLU A OE2 
3279 N N   . LEU A 459 ? 0.2557 0.2789 0.2480 -0.0009 -0.0549 0.0031  445 LEU A N   
3280 C CA  . LEU A 459 ? 0.2644 0.2875 0.2532 0.0001  -0.0585 0.0037  445 LEU A CA  
3281 C C   . LEU A 459 ? 0.2730 0.2955 0.2628 0.0002  -0.0650 0.0006  445 LEU A C   
3282 O O   . LEU A 459 ? 0.2649 0.2875 0.2484 0.0010  -0.0680 -0.0018 445 LEU A O   
3283 C CB  . LEU A 459 ? 0.2780 0.3021 0.2722 0.0000  -0.0583 0.0087  445 LEU A CB  
3284 C CG  . LEU A 459 ? 0.2914 0.3157 0.2838 0.0006  -0.0632 0.0106  445 LEU A CG  
3285 C CD1 . LEU A 459 ? 0.3068 0.3310 0.2888 0.0012  -0.0625 0.0096  445 LEU A CD1 
3286 C CD2 . LEU A 459 ? 0.3189 0.3442 0.3191 0.0006  -0.0630 0.0157  445 LEU A CD2 
3287 N N   . GLY A 460 ? 0.2694 0.2919 0.2673 -0.0008 -0.0676 0.0007  446 GLY A N   
3288 C CA  . GLY A 460 ? 0.2638 0.2852 0.2643 -0.0008 -0.0742 -0.0024 446 GLY A CA  
3289 C C   . GLY A 460 ? 0.2721 0.2924 0.2673 0.0001  -0.0749 -0.0088 446 GLY A C   
3290 O O   . GLY A 460 ? 0.2539 0.2737 0.2474 0.0009  -0.0799 -0.0128 446 GLY A O   
3291 N N   . SER A 461 ? 0.2418 0.2620 0.2350 0.0001  -0.0701 -0.0103 447 SER A N   
3292 C CA  . SER A 461 ? 0.2769 0.2966 0.2654 0.0012  -0.0699 -0.0166 447 SER A CA  
3293 C C   . SER A 461 ? 0.2524 0.2735 0.2302 0.0024  -0.0686 -0.0188 447 SER A C   
3294 O O   . SER A 461 ? 0.2544 0.2761 0.2284 0.0034  -0.0711 -0.0248 447 SER A O   
3295 C CB  . SER A 461 ? 0.2358 0.2553 0.2250 0.0007  -0.0648 -0.0169 447 SER A CB  
3296 O OG  . SER A 461 ? 0.2282 0.2471 0.2265 -0.0012 -0.0661 -0.0140 447 SER A OG  
3297 N N   . MET A 462 ? 0.2594 0.2816 0.2325 0.0022  -0.0648 -0.0141 448 MET A N   
3298 C CA  . MET A 462 ? 0.2751 0.2993 0.2383 0.0027  -0.0641 -0.0147 448 MET A CA  
3299 C C   . MET A 462 ? 0.2929 0.3178 0.2545 0.0029  -0.0706 -0.0166 448 MET A C   
3300 O O   . MET A 462 ? 0.3032 0.3300 0.2571 0.0033  -0.0719 -0.0214 448 MET A O   
3301 C CB  . MET A 462 ? 0.2678 0.2926 0.2291 0.0023  -0.0604 -0.0082 448 MET A CB  
3302 C CG  . MET A 462 ? 0.2617 0.2859 0.2253 0.0020  -0.0543 -0.0060 448 MET A CG  
3303 S SD  . MET A 462 ? 0.3188 0.3434 0.2823 0.0017  -0.0514 0.0011  448 MET A SD  
3304 C CE  . MET A 462 ? 0.2328 0.2574 0.1925 0.0016  -0.0443 0.0008  448 MET A CE  
3305 N N   . LEU A 463 ? 0.2677 0.2913 0.2367 0.0023  -0.0747 -0.0130 449 LEU A N   
3306 C CA  . LEU A 463 ? 0.2851 0.3090 0.2534 0.0022  -0.0814 -0.0141 449 LEU A CA  
3307 C C   . LEU A 463 ? 0.2933 0.3163 0.2631 0.0028  -0.0858 -0.0217 449 LEU A C   
3308 O O   . LEU A 463 ? 0.2786 0.3030 0.2424 0.0031  -0.0895 -0.0261 449 LEU A O   
3309 C CB  . LEU A 463 ? 0.2678 0.2907 0.2452 0.0015  -0.0846 -0.0081 449 LEU A CB  
3310 C CG  . LEU A 463 ? 0.2725 0.2961 0.2506 0.0011  -0.0813 -0.0010 449 LEU A CG  
3311 C CD1 . LEU A 463 ? 0.2719 0.2951 0.2618 0.0005  -0.0833 0.0037  449 LEU A CD1 
3312 C CD2 . LEU A 463 ? 0.3113 0.3366 0.2814 0.0009  -0.0833 0.0009  449 LEU A CD2 
3313 N N   . ARG A 464 ? 0.2872 0.3083 0.2656 0.0029  -0.0857 -0.0233 450 ARG A N   
3314 C CA  . ARG A 464 ? 0.3177 0.3377 0.2996 0.0036  -0.0900 -0.0307 450 ARG A CA  
3315 C C   . ARG A 464 ? 0.3259 0.3481 0.2981 0.0048  -0.0878 -0.0382 450 ARG A C   
3316 O O   . ARG A 464 ? 0.3124 0.3353 0.2827 0.0054  -0.0923 -0.0449 450 ARG A O   
3317 C CB  . ARG A 464 ? 0.2972 0.3151 0.2896 0.0031  -0.0895 -0.0304 450 ARG A CB  
3318 C CG  . ARG A 464 ? 0.3017 0.3183 0.2992 0.0040  -0.0935 -0.0383 450 ARG A CG  
3319 C CD  . ARG A 464 ? 0.3008 0.3162 0.3055 0.0036  -0.0911 -0.0381 450 ARG A CD  
3320 N NE  . ARG A 464 ? 0.3034 0.3202 0.3008 0.0042  -0.0838 -0.0390 450 ARG A NE  
3321 C CZ  . ARG A 464 ? 0.3188 0.3350 0.3204 0.0033  -0.0803 -0.0365 450 ARG A CZ  
3322 N NH1 . ARG A 464 ? 0.3267 0.3413 0.3390 0.0016  -0.0832 -0.0329 450 ARG A NH1 
3323 N NH2 . ARG A 464 ? 0.2852 0.3028 0.2802 0.0039  -0.0739 -0.0374 450 ARG A NH2 
3324 N N   . ASP A 465 ? 0.4044 0.3285 0.2245 0.0354  -0.0305 0.0772  451 ASP A N   
3325 C CA  . ASP A 465 ? 0.3973 0.3195 0.2020 0.0435  -0.0270 0.0816  451 ASP A CA  
3326 C C   . ASP A 465 ? 0.4309 0.3458 0.2333 0.0364  -0.0370 0.0766  451 ASP A C   
3327 O O   . ASP A 465 ? 0.4179 0.3326 0.2088 0.0434  -0.0341 0.0810  451 ASP A O   
3328 C CB  . ASP A 465 ? 0.4030 0.3592 0.2172 0.0522  -0.0228 0.0886  451 ASP A CB  
3329 C CG  . ASP A 465 ? 0.3874 0.3519 0.2033 0.0612  -0.0111 0.0932  451 ASP A CG  
3330 O OD1 . ASP A 465 ? 0.4018 0.3406 0.2037 0.0646  -0.0038 0.0951  451 ASP A OD1 
3331 O OD2 . ASP A 465 ? 0.3699 0.3647 0.2002 0.0651  -0.0090 0.0946  451 ASP A OD2 
3332 N N   . LYS A 466 ? 0.4185 0.3285 0.2314 0.0241  -0.0477 0.0689  452 LYS A N   
3333 C CA  . LYS A 466 ? 0.4551 0.3570 0.2644 0.0183  -0.0572 0.0645  452 LYS A CA  
3334 C C   . LYS A 466 ? 0.4414 0.3647 0.2602 0.0205  -0.0588 0.0684  452 LYS A C   
3335 O O   . LYS A 466 ? 0.4247 0.3407 0.2322 0.0234  -0.0601 0.0701  452 LYS A O   
3336 C CB  . LYS A 466 ? 0.5018 0.3724 0.2823 0.0219  -0.0557 0.0626  452 LYS A CB  
3337 C CG  . LYS A 466 ? 0.5662 0.4128 0.3396 0.0168  -0.0547 0.0574  452 LYS A CG  
3338 C CD  . LYS A 466 ? 0.6420 0.4616 0.3973 0.0107  -0.0631 0.0489  452 LYS A CD  
3339 C CE  . LYS A 466 ? 0.7165 0.5062 0.4593 0.0073  -0.0586 0.0442  452 LYS A CE  
3340 N NZ  . LYS A 466 ? 0.7798 0.5747 0.5468 -0.0065 -0.0647 0.0401  452 LYS A NZ  
3341 N N   . GLN A 467 ? 0.3734 0.3226 0.2132 0.0190  -0.0585 0.0696  453 GLN A N   
3342 C CA  . GLN A 467 ? 0.3583 0.3278 0.2126 0.0176  -0.0608 0.0717  453 GLN A CA  
3343 C C   . GLN A 467 ? 0.3679 0.3364 0.2347 0.0081  -0.0702 0.0665  453 GLN A C   
3344 O O   . GLN A 467 ? 0.3526 0.3140 0.2235 0.0021  -0.0757 0.0613  453 GLN A O   
3345 C CB  . GLN A 467 ? 0.3562 0.3531 0.2275 0.0184  -0.0583 0.0726  453 GLN A CB  
3346 C CG  . GLN A 467 ? 0.3473 0.3516 0.2095 0.0289  -0.0490 0.0786  453 GLN A CG  
3347 C CD  . GLN A 467 ? 0.3234 0.3596 0.2030 0.0291  -0.0492 0.0786  453 GLN A CD  
3348 O OE1 . GLN A 467 ? 0.3158 0.3618 0.2110 0.0214  -0.0556 0.0716  453 GLN A OE1 
3349 N NE2 . GLN A 467 ? 0.3053 0.3589 0.1820 0.0384  -0.0424 0.0863  453 GLN A NE2 
3350 N N   . HIS A 468 ? 0.3378 0.3149 0.2125 0.0074  -0.0712 0.0693  454 HIS A N   
3351 C CA  . HIS A 468 ? 0.3572 0.3319 0.2416 0.0011  -0.0781 0.0667  454 HIS A CA  
3352 C C   . HIS A 468 ? 0.3465 0.3390 0.2535 -0.0036 -0.0781 0.0665  454 HIS A C   
3353 O O   . HIS A 468 ? 0.3495 0.3416 0.2618 -0.0043 -0.0781 0.0699  454 HIS A O   
3354 C CB  . HIS A 468 ? 0.3880 0.3481 0.2558 0.0056  -0.0787 0.0707  454 HIS A CB  
3355 C CG  . HIS A 468 ? 0.4424 0.3815 0.2847 0.0098  -0.0792 0.0690  454 HIS A CG  
3356 N ND1 . HIS A 468 ? 0.4566 0.3823 0.2760 0.0184  -0.0758 0.0733  454 HIS A ND1 
3357 C CD2 . HIS A 468 ? 0.4672 0.3949 0.3032 0.0064  -0.0820 0.0631  454 HIS A CD2 
3358 C CE1 . HIS A 468 ? 0.4794 0.3858 0.2796 0.0196  -0.0766 0.0681  454 HIS A CE1 
3359 N NE2 . HIS A 468 ? 0.4964 0.4023 0.3057 0.0116  -0.0810 0.0625  454 HIS A NE2 
3360 N N   . PRO A 469 ? 0.3326 0.3399 0.2528 -0.0067 -0.0780 0.0622  455 PRO A N   
3361 C CA  . PRO A 469 ? 0.3151 0.3357 0.2556 -0.0127 -0.0792 0.0592  455 PRO A CA  
3362 C C   . PRO A 469 ? 0.3072 0.3189 0.2557 -0.0176 -0.0838 0.0558  455 PRO A C   
3363 O O   . PRO A 469 ? 0.3285 0.3289 0.2695 -0.0170 -0.0873 0.0554  455 PRO A O   
3364 C CB  . PRO A 469 ? 0.3052 0.3422 0.2522 -0.0131 -0.0789 0.0540  455 PRO A CB  
3365 C CG  . PRO A 469 ? 0.3070 0.3352 0.2413 -0.0089 -0.0785 0.0537  455 PRO A CG  
3366 C CD  . PRO A 469 ? 0.3150 0.3244 0.2321 -0.0053 -0.0774 0.0588  455 PRO A CD  
3367 N N   . ILE A 470 ? 0.2934 0.3102 0.2578 -0.0225 -0.0835 0.0539  456 ILE A N   
3368 C CA  . ILE A 470 ? 0.3130 0.3229 0.2869 -0.0260 -0.0860 0.0508  456 ILE A CA  
3369 C C   . ILE A 470 ? 0.2921 0.3113 0.2771 -0.0299 -0.0869 0.0419  456 ILE A C   
3370 O O   . ILE A 470 ? 0.2880 0.3154 0.2835 -0.0343 -0.0856 0.0380  456 ILE A O   
3371 C CB  . ILE A 470 ? 0.3114 0.3152 0.2933 -0.0274 -0.0831 0.0559  456 ILE A CB  
3372 C CG1 . ILE A 470 ? 0.3411 0.3361 0.3086 -0.0211 -0.0821 0.0650  456 ILE A CG1 
3373 C CG2 . ILE A 470 ? 0.2913 0.2878 0.2831 -0.0296 -0.0840 0.0532  456 ILE A CG2 
3374 C CD1 . ILE A 470 ? 0.3208 0.3140 0.2944 -0.0202 -0.0761 0.0730  456 ILE A CD1 
3375 N N   . ILE A 471 ? 0.2845 0.3029 0.2669 -0.0282 -0.0893 0.0386  457 ILE A N   
3376 C CA  . ILE A 471 ? 0.2635 0.2904 0.2520 -0.0290 -0.0896 0.0306  457 ILE A CA  
3377 C C   . ILE A 471 ? 0.2660 0.2845 0.2632 -0.0305 -0.0899 0.0277  457 ILE A C   
3378 O O   . ILE A 471 ? 0.3017 0.3136 0.2980 -0.0281 -0.0910 0.0317  457 ILE A O   
3379 C CB  . ILE A 471 ? 0.2749 0.3071 0.2554 -0.0242 -0.0896 0.0306  457 ILE A CB  
3380 C CG1 . ILE A 471 ? 0.2816 0.3182 0.2514 -0.0210 -0.0876 0.0351  457 ILE A CG1 
3381 C CG2 . ILE A 471 ? 0.2472 0.2904 0.2315 -0.0227 -0.0892 0.0228  457 ILE A CG2 
3382 C CD1 . ILE A 471 ? 0.2662 0.3036 0.2275 -0.0159 -0.0857 0.0370  457 ILE A CD1 
3383 N N   . LEU A 472 ? 0.2297 0.2485 0.2356 -0.0345 -0.0886 0.0208  458 LEU A N   
3384 C CA  . LEU A 472 ? 0.2680 0.2764 0.2806 -0.0347 -0.0870 0.0172  458 LEU A CA  
3385 C C   . LEU A 472 ? 0.2681 0.2832 0.2792 -0.0328 -0.0875 0.0074  458 LEU A C   
3386 O O   . LEU A 472 ? 0.2436 0.2658 0.2560 -0.0366 -0.0885 -0.0016 458 LEU A O   
3387 C CB  . LEU A 472 ? 0.2686 0.2673 0.2909 -0.0406 -0.0840 0.0157  458 LEU A CB  
3388 C CG  . LEU A 472 ? 0.2824 0.2737 0.3061 -0.0404 -0.0817 0.0267  458 LEU A CG  
3389 C CD1 . LEU A 472 ? 0.2839 0.2820 0.3119 -0.0457 -0.0805 0.0279  458 LEU A CD1 
3390 C CD2 . LEU A 472 ? 0.3073 0.2823 0.3382 -0.0394 -0.0769 0.0299  458 LEU A CD2 
3391 N N   . VAL A 473 ? 0.2578 0.2721 0.2662 -0.0265 -0.0868 0.0095  459 VAL A N   
3392 C CA  . VAL A 473 ? 0.2715 0.2912 0.2767 -0.0220 -0.0858 0.0018  459 VAL A CA  
3393 C C   . VAL A 473 ? 0.2853 0.2906 0.2948 -0.0214 -0.0826 -0.0030 459 VAL A C   
3394 O O   . VAL A 473 ? 0.3013 0.2978 0.3149 -0.0180 -0.0800 0.0044  459 VAL A O   
3395 C CB  . VAL A 473 ? 0.2921 0.3188 0.2938 -0.0147 -0.0849 0.0083  459 VAL A CB  
3396 C CG1 . VAL A 473 ? 0.2941 0.3274 0.2909 -0.0076 -0.0824 0.0017  459 VAL A CG1 
3397 C CG2 . VAL A 473 ? 0.2562 0.2914 0.2527 -0.0154 -0.0866 0.0139  459 VAL A CG2 
3398 N N   . LEU A 474 ? 0.2682 0.2708 0.2768 -0.0251 -0.0827 -0.0155 460 LEU A N   
3399 C CA  . LEU A 474 ? 0.3120 0.2966 0.3226 -0.0247 -0.0785 -0.0220 460 LEU A CA  
3400 C C   . LEU A 474 ? 0.3314 0.3173 0.3338 -0.0140 -0.0758 -0.0250 460 LEU A C   
3401 O O   . LEU A 474 ? 0.3336 0.3267 0.3272 -0.0120 -0.0776 -0.0360 460 LEU A O   
3402 C CB  . LEU A 474 ? 0.3287 0.3079 0.3419 -0.0346 -0.0802 -0.0356 460 LEU A CB  
3403 C CG  . LEU A 474 ? 0.3138 0.2971 0.3368 -0.0449 -0.0823 -0.0318 460 LEU A CG  
3404 C CD1 . LEU A 474 ? 0.3757 0.3510 0.4059 -0.0562 -0.0829 -0.0450 460 LEU A CD1 
3405 C CD2 . LEU A 474 ? 0.3274 0.3001 0.3566 -0.0434 -0.0782 -0.0168 460 LEU A CD2 
3406 N N   . ASN A 475 ? 0.3530 0.3339 0.3583 -0.0064 -0.0715 -0.0144 461 ASN A N   
3407 C CA  . ASN A 475 ? 0.3723 0.3577 0.3724 0.0053  -0.0676 -0.0125 461 ASN A CA  
3408 C C   . ASN A 475 ? 0.4069 0.3734 0.4040 0.0113  -0.0608 -0.0177 461 ASN A C   
3409 O O   . ASN A 475 ? 0.4115 0.3676 0.4155 0.0148  -0.0560 -0.0087 461 ASN A O   
3410 C CB  . ASN A 475 ? 0.3584 0.3538 0.3662 0.0096  -0.0671 0.0035  461 ASN A CB  
3411 C CG  . ASN A 475 ? 0.4121 0.4153 0.4180 0.0214  -0.0621 0.0078  461 ASN A CG  
3412 O OD1 . ASN A 475 ? 0.4391 0.4398 0.4349 0.0282  -0.0586 -0.0012 461 ASN A OD1 
3413 N ND2 . ASN A 475 ? 0.3712 0.3843 0.3869 0.0240  -0.0617 0.0216  461 ASN A ND2 
3414 N N   . ASN A 476 ? 0.4235 0.3856 0.4088 0.0139  -0.0601 -0.0323 462 ASN A N   
3415 C CA  . ASN A 476 ? 0.4942 0.4374 0.4716 0.0228  -0.0525 -0.0382 462 ASN A CA  
3416 C C   . ASN A 476 ? 0.5446 0.4976 0.5097 0.0370  -0.0491 -0.0394 462 ASN A C   
3417 O O   . ASN A 476 ? 0.5902 0.5286 0.5422 0.0451  -0.0440 -0.0495 462 ASN A O   
3418 C CB  . ASN A 476 ? 0.5225 0.4447 0.4954 0.0135  -0.0533 -0.0557 462 ASN A CB  
3419 C CG  . ASN A 476 ? 0.5414 0.4743 0.5040 0.0078  -0.0612 -0.0727 462 ASN A CG  
3420 O OD1 . ASN A 476 ? 0.4670 0.4232 0.4241 0.0123  -0.0653 -0.0711 462 ASN A OD1 
3421 N ND2 . ASN A 476 ? 0.6126 0.5289 0.5733 -0.0025 -0.0632 -0.0891 462 ASN A ND2 
3422 N N   . GLU A 477 ? 0.5270 0.5034 0.4953 0.0405  -0.0512 -0.0292 463 GLU A N   
3423 C CA  . GLU A 477 ? 0.5644 0.5524 0.5267 0.0557  -0.0453 -0.0228 463 GLU A CA  
3424 C C   . GLU A 477 ? 0.5967 0.5859 0.5382 0.0631  -0.0453 -0.0384 463 GLU A C   
3425 O O   . GLU A 477 ? 0.6499 0.6330 0.5800 0.0774  -0.0378 -0.0400 463 GLU A O   
3426 C CB  . GLU A 477 ? 0.6466 0.6253 0.6148 0.0665  -0.0359 -0.0115 463 GLU A CB  
3427 C CG  . GLU A 477 ? 0.6416 0.6260 0.6302 0.0617  -0.0367 0.0057  463 GLU A CG  
3428 C CD  . GLU A 477 ? 0.8721 0.8640 0.8698 0.0748  -0.0283 0.0218  463 GLU A CD  
3429 O OE1 . GLU A 477 ? 0.8157 0.8022 0.8030 0.0889  -0.0197 0.0197  463 GLU A OE1 
3430 O OE2 . GLU A 477 ? 0.8314 0.8359 0.8466 0.0712  -0.0306 0.0366  463 GLU A OE2 
3431 N N   . GLY A 478 ? 0.5573 0.5559 0.4931 0.0545  -0.0538 -0.0495 464 GLY A N   
3432 C CA  . GLY A 478 ? 0.6212 0.6270 0.5369 0.0615  -0.0560 -0.0641 464 GLY A CA  
3433 C C   . GLY A 478 ? 0.5877 0.5952 0.5002 0.0472  -0.0666 -0.0813 464 GLY A C   
3434 O O   . GLY A 478 ? 0.5221 0.5287 0.4491 0.0326  -0.0714 -0.0789 464 GLY A O   
3435 N N   . TYR A 479 ? 0.6452 0.6579 0.5382 0.0524  -0.0703 -0.0980 465 TYR A N   
3436 C CA  . TYR A 479 ? 0.6499 0.6694 0.5388 0.0396  -0.0817 -0.1166 465 TYR A CA  
3437 C C   . TYR A 479 ? 0.7714 0.7616 0.6574 0.0298  -0.0831 -0.1348 465 TYR A C   
3438 O O   . TYR A 479 ? 0.8702 0.8509 0.7364 0.0353  -0.0842 -0.1526 465 TYR A O   
3439 C CB  . TYR A 479 ? 0.6865 0.7296 0.5548 0.0508  -0.0861 -0.1258 465 TYR A CB  
3440 C CG  . TYR A 479 ? 0.6059 0.6792 0.4745 0.0608  -0.0847 -0.1101 465 TYR A CG  
3441 C CD1 . TYR A 479 ? 0.5276 0.6116 0.4150 0.0527  -0.0852 -0.0945 465 TYR A CD1 
3442 C CD2 . TYR A 479 ? 0.5972 0.6873 0.4452 0.0791  -0.0824 -0.1117 465 TYR A CD2 
3443 C CE1 . TYR A 479 ? 0.4721 0.5801 0.3582 0.0621  -0.0827 -0.0808 465 TYR A CE1 
3444 C CE2 . TYR A 479 ? 0.5439 0.6599 0.3917 0.0892  -0.0793 -0.0967 465 TYR A CE2 
3445 C CZ  . TYR A 479 ? 0.5183 0.6419 0.3855 0.0803  -0.0792 -0.0815 465 TYR A CZ  
3446 O OH  . TYR A 479 ? 0.4544 0.5999 0.3204 0.0908  -0.0746 -0.0668 465 TYR A OH  
3447 N N   . THR A 480 ? 0.7300 0.7038 0.6349 0.0157  -0.0823 -0.1305 466 THR A N   
3448 C CA  . THR A 480 ? 0.8186 0.7599 0.7231 0.0069  -0.0805 -0.1450 466 THR A CA  
3449 C C   . THR A 480 ? 0.9319 0.8749 0.8319 -0.0076 -0.0916 -0.1690 466 THR A C   
3450 O O   . THR A 480 ? 0.9917 0.9101 0.8787 -0.0090 -0.0911 -0.1879 466 THR A O   
3451 C CB  . THR A 480 ? 0.7639 0.6890 0.6903 -0.0029 -0.0755 -0.1318 466 THR A CB  
3452 O OG1 . THR A 480 ? 0.7565 0.6801 0.6862 0.0106  -0.0662 -0.1116 466 THR A OG1 
3453 C CG2 . THR A 480 ? 0.8344 0.7236 0.7618 -0.0120 -0.0717 -0.1452 466 THR A CG2 
3454 N N   . VAL A 481 ? 1.0212 0.9924 0.9322 -0.0188 -0.1017 -0.1689 467 VAL A N   
3455 C CA  . VAL A 481 ? 0.9980 0.9754 0.9099 -0.0349 -0.1134 -0.1906 467 VAL A CA  
3456 C C   . VAL A 481 ? 1.0843 1.0631 0.9688 -0.0258 -0.1184 -0.2117 467 VAL A C   
3457 O O   . VAL A 481 ? 1.1189 1.0781 0.9962 -0.0356 -0.1229 -0.2345 467 VAL A O   
3458 C CB  . VAL A 481 ? 0.8041 0.8195 0.7303 -0.0432 -0.1227 -0.1837 467 VAL A CB  
3459 C CG1 . VAL A 481 ? 0.6636 0.7031 0.5830 -0.0258 -0.1191 -0.1652 467 VAL A CG1 
3460 C CG2 . VAL A 481 ? 0.7746 0.8111 0.6959 -0.0532 -0.1367 -0.2056 467 VAL A CG2 
3461 N N   . GLU A 482 ? 1.0432 1.0441 0.9110 -0.0064 -0.1171 -0.2043 468 GLU A N   
3462 C CA  . GLU A 482 ? 1.0224 1.0278 0.8605 0.0069  -0.1206 -0.2214 468 GLU A CA  
3463 C C   . GLU A 482 ? 1.0893 1.0564 0.9098 0.0186  -0.1096 -0.2271 468 GLU A C   
3464 O O   . GLU A 482 ? 1.1234 1.0802 0.9186 0.0243  -0.1129 -0.2485 468 GLU A O   
3465 C CB  . GLU A 482 ? 0.9377 0.9790 0.7662 0.0252  -0.1200 -0.2073 468 GLU A CB  
3466 C CG  . GLU A 482 ? 0.8196 0.8943 0.6347 0.0255  -0.1335 -0.2224 468 GLU A CG  
3467 C CD  . GLU A 482 ? 0.7482 0.8617 0.5745 0.0287  -0.1356 -0.2041 468 GLU A CD  
3468 O OE1 . GLU A 482 ? 0.6736 0.8020 0.4889 0.0489  -0.1282 -0.1893 468 GLU A OE1 
3469 O OE2 . GLU A 482 ? 0.7330 0.8590 0.5811 0.0109  -0.1419 -0.2014 468 GLU A OE2 
3470 N N   . ARG A 483 ? 1.0845 1.0315 0.9171 0.0234  -0.0965 -0.2079 469 ARG A N   
3471 C CA  . ARG A 483 ? 1.1294 1.0386 0.9490 0.0339  -0.0846 -0.2110 469 ARG A CA  
3472 C C   . ARG A 483 ? 1.1902 1.0662 1.0062 0.0179  -0.0882 -0.2357 469 ARG A C   
3473 O O   . ARG A 483 ? 1.2291 1.0801 1.0199 0.0262  -0.0852 -0.2534 469 ARG A O   
3474 C CB  . ARG A 483 ? 1.0674 0.9656 0.9068 0.0379  -0.0720 -0.1852 469 ARG A CB  
3475 C CG  . ARG A 483 ? 1.0365 0.9522 0.8728 0.0590  -0.0632 -0.1633 469 ARG A CG  
3476 C CD  . ARG A 483 ? 1.0322 0.9252 0.8757 0.0688  -0.0488 -0.1469 469 ARG A CD  
3477 N NE  . ARG A 483 ? 1.0158 0.9306 0.8794 0.0721  -0.0453 -0.1207 469 ARG A NE  
3478 C CZ  . ARG A 483 ? 0.9208 0.8610 0.7818 0.0857  -0.0428 -0.1076 469 ARG A CZ  
3479 N NH1 . ARG A 483 ? 0.9404 0.8895 0.7784 0.1002  -0.0422 -0.1161 469 ARG A NH1 
3480 N NH2 . ARG A 483 ? 0.8247 0.7813 0.7063 0.0848  -0.0408 -0.0857 469 ARG A NH2 
3481 N N   . ALA A 484 ? 1.1723 1.0471 1.0132 -0.0051 -0.0941 -0.2373 470 ALA A N   
3482 C CA  . ALA A 484 ? 1.2216 1.0650 1.0643 -0.0235 -0.0973 -0.2599 470 ALA A CA  
3483 C C   . ALA A 484 ? 1.2718 1.1225 1.0925 -0.0282 -0.1111 -0.2900 470 ALA A C   
3484 O O   . ALA A 484 ? 1.3001 1.1160 1.1029 -0.0302 -0.1098 -0.3123 470 ALA A O   
3485 C CB  . ALA A 484 ? 1.1637 1.0112 1.0401 -0.0467 -0.1008 -0.2526 470 ALA A CB  
3486 N N   . ILE A 485 ? 1.2517 1.1474 1.0722 -0.0293 -0.1244 -0.2915 471 ILE A N   
3487 C CA  . ILE A 485 ? 1.2647 1.1731 1.0686 -0.0362 -0.1359 -0.3114 471 ILE A CA  
3488 C C   . ILE A 485 ? 1.2642 1.1657 1.0298 -0.0126 -0.1317 -0.3201 471 ILE A C   
3489 O O   . ILE A 485 ? 1.2698 1.1487 1.0157 -0.0171 -0.1328 -0.3387 471 ILE A O   
3490 C CB  . ILE A 485 ? 1.2250 1.1832 1.0455 -0.0460 -0.1476 -0.3013 471 ILE A CB  
3491 C CG1 . ILE A 485 ? 1.1170 1.1148 0.9209 -0.0244 -0.1496 -0.2911 471 ILE A CG1 
3492 C CG2 . ILE A 485 ? 1.1810 1.1476 1.0375 -0.0611 -0.1476 -0.2861 471 ILE A CG2 
3493 C CD1 . ILE A 485 ? 0.9934 1.0005 0.7711 -0.0190 -0.1557 -0.3049 471 ILE A CD1 
3494 N N   . HIS A 486 ? 1.2239 1.1431 0.9774 0.0130  -0.1262 -0.3062 472 HIS A N   
3495 C CA  . HIS A 486 ? 1.2098 1.1242 0.9277 0.0367  -0.1206 -0.3117 472 HIS A CA  
3496 C C   . HIS A 486 ? 1.1905 1.1075 0.9002 0.0646  -0.1070 -0.2907 472 HIS A C   
3497 O O   . HIS A 486 ? 1.1245 1.0720 0.8526 0.0681  -0.1052 -0.2667 472 HIS A O   
3498 C CB  . HIS A 486 ? 1.1031 1.0554 0.8092 0.0381  -0.1305 -0.3149 472 HIS A CB  
3499 C CG  . HIS A 486 ? 1.0776 1.0210 0.7474 0.0593  -0.1253 -0.3235 472 HIS A CG  
3500 N ND1 . HIS A 486 ? 1.1720 1.0703 0.8214 0.0616  -0.1181 -0.3398 472 HIS A ND1 
3501 C CD2 . HIS A 486 ? 0.8893 0.8616 0.5398 0.0800  -0.1250 -0.3173 472 HIS A CD2 
3502 C CE1 . HIS A 486 ? 1.1031 1.0036 0.7213 0.0827  -0.1140 -0.3435 472 HIS A CE1 
3503 N NE2 . HIS A 486 ? 0.9397 0.8854 0.5586 0.0942  -0.1183 -0.3299 472 HIS A NE2 
3504 N N   . GLY A 487 ? 1.2140 1.0996 0.8988 0.0832  -0.0948 -0.2945 473 GLY A N   
3505 C CA  . GLY A 487 ? 1.2036 1.0913 0.8822 0.1095  -0.0782 -0.2700 473 GLY A CA  
3506 C C   . GLY A 487 ? 1.2478 1.1314 0.9602 0.1050  -0.0674 -0.2414 473 GLY A C   
3507 O O   . GLY A 487 ? 1.1850 1.0980 0.9130 0.1115  -0.0643 -0.2173 473 GLY A O   
3508 N N   . PRO A 488 ? 1.3410 1.1872 1.0646 0.0942  -0.0612 -0.2436 474 PRO A N   
3509 C CA  . PRO A 488 ? 1.3452 1.1891 1.1002 0.0902  -0.0520 -0.2167 474 PRO A CA  
3510 C C   . PRO A 488 ? 1.2403 1.0907 0.9944 0.1144  -0.0369 -0.1915 474 PRO A C   
3511 O O   . PRO A 488 ? 1.1756 1.0430 0.9555 0.1128  -0.0334 -0.1671 474 PRO A O   
3512 C CB  . PRO A 488 ? 1.2926 1.0923 1.0535 0.0770  -0.0473 -0.2271 474 PRO A CB  
3513 C CG  . PRO A 488 ? 1.2883 1.0621 1.0185 0.0759  -0.0521 -0.2597 474 PRO A CG  
3514 C CD  . PRO A 488 ? 1.3058 1.1070 1.0085 0.0923  -0.0582 -0.2678 474 PRO A CD  
3515 N N   . GLU A 489 ? 1.2652 1.1030 0.9903 0.1368  -0.0279 -0.1968 475 GLU A N   
3516 C CA  . GLU A 489 ? 1.2692 1.1152 0.9935 0.1612  -0.0126 -0.1726 475 GLU A CA  
3517 C C   . GLU A 489 ? 1.2922 1.1761 1.0072 0.1762  -0.0142 -0.1643 475 GLU A C   
3518 O O   . GLU A 489 ? 1.1924 1.0860 0.9065 0.1973  -0.0011 -0.1442 475 GLU A O   
3519 C CB  . GLU A 489 ? 1.2750 1.0843 0.9731 0.1802  0.0014  -0.1798 475 GLU A CB  
3520 C CG  . GLU A 489 ? 1.2946 1.0746 1.0094 0.1793  0.0140  -0.1670 475 GLU A CG  
3521 C CD  . GLU A 489 ? 1.3990 1.1344 1.0840 0.1938  0.0260  -0.1816 475 GLU A CD  
3522 O OE1 . GLU A 489 ? 1.4468 1.1680 1.0990 0.1968  0.0207  -0.2083 475 GLU A OE1 
3523 O OE2 . GLU A 489 ? 1.4234 1.1381 1.1166 0.2030  0.0410  -0.1664 475 GLU A OE2 
3524 N N   . GLN A 490 ? 1.2634 1.1700 0.9723 0.1666  -0.0290 -0.1781 476 GLN A N   
3525 C CA  . GLN A 490 ? 1.0894 1.0312 0.7868 0.1824  -0.0298 -0.1707 476 GLN A CA  
3526 C C   . GLN A 490 ? 0.9916 0.9632 0.7203 0.1790  -0.0275 -0.1426 476 GLN A C   
3527 O O   . GLN A 490 ? 0.9553 0.9299 0.7108 0.1581  -0.0342 -0.1375 476 GLN A O   
3528 C CB  . GLN A 490 ? 0.9906 0.9477 0.6682 0.1753  -0.0464 -0.1958 476 GLN A CB  
3529 C CG  . GLN A 490 ? 0.9748 0.9078 0.6136 0.1844  -0.0486 -0.2245 476 GLN A CG  
3530 C CD  . GLN A 490 ? 0.9472 0.8843 0.5551 0.2175  -0.0360 -0.2184 476 GLN A CD  
3531 O OE1 . GLN A 490 ? 0.9797 0.9136 0.5958 0.2338  -0.0192 -0.1943 476 GLN A OE1 
3532 N NE2 . GLN A 490 ? 0.8300 0.7771 0.4105 0.2242  -0.0436 -0.2354 476 GLN A NE2 
3533 N N   . ARG A 491 ? 0.9506 0.9428 0.6749 0.2005  -0.0172 -0.1241 477 ARG A N   
3534 C CA  . ARG A 491 ? 0.9040 0.9202 0.6575 0.1988  -0.0126 -0.0966 477 ARG A CA  
3535 C C   . ARG A 491 ? 0.8663 0.9080 0.6302 0.1840  -0.0252 -0.0978 477 ARG A C   
3536 O O   . ARG A 491 ? 0.8379 0.8903 0.6293 0.1735  -0.0249 -0.0801 477 ARG A O   
3537 C CB  . ARG A 491 ? 0.8670 0.8985 0.6128 0.2257  0.0025  -0.0774 477 ARG A CB  
3538 C CG  . ARG A 491 ? 0.8225 0.8863 0.5839 0.2278  0.0043  -0.0574 477 ARG A CG  
3539 C CD  . ARG A 491 ? 0.8027 0.8793 0.5624 0.2532  0.0218  -0.0352 477 ARG A CD  
3540 N NE  . ARG A 491 ? 0.8136 0.9040 0.5404 0.2748  0.0240  -0.0425 477 ARG A NE  
3541 C CZ  . ARG A 491 ? 0.5941 0.7115 0.3184 0.2797  0.0226  -0.0360 477 ARG A CZ  
3542 N NH1 . ARG A 491 ? 0.5236 0.6544 0.2746 0.2631  0.0180  -0.0248 477 ARG A NH1 
3543 N NH2 . ARG A 491 ? 0.5894 0.7199 0.2819 0.3030  0.0263  -0.0409 477 ARG A NH2 
3544 N N   . TYR A 492 ? 0.8280 0.8790 0.5706 0.1820  -0.0369 -0.1190 478 TYR A N   
3545 C CA  . TYR A 492 ? 0.7869 0.8647 0.5395 0.1698  -0.0480 -0.1186 478 TYR A CA  
3546 C C   . TYR A 492 ? 0.7891 0.8583 0.5679 0.1427  -0.0570 -0.1209 478 TYR A C   
3547 O O   . TYR A 492 ? 0.7211 0.8110 0.5140 0.1329  -0.0631 -0.1141 478 TYR A O   
3548 C CB  . TYR A 492 ? 0.7045 0.7991 0.4288 0.1752  -0.0591 -0.1403 478 TYR A CB  
3549 C CG  . TYR A 492 ? 0.8410 0.9140 0.5464 0.1661  -0.0696 -0.1711 478 TYR A CG  
3550 C CD1 . TYR A 492 ? 0.8067 0.8642 0.5293 0.1396  -0.0799 -0.1840 478 TYR A CD1 
3551 C CD2 . TYR A 492 ? 0.7737 0.8415 0.4433 0.1845  -0.0688 -0.1875 478 TYR A CD2 
3552 C CE1 . TYR A 492 ? 0.8075 0.8435 0.5143 0.1300  -0.0890 -0.2127 478 TYR A CE1 
3553 C CE2 . TYR A 492 ? 0.7214 0.7670 0.3733 0.1750  -0.0785 -0.2169 478 TYR A CE2 
3554 C CZ  . TYR A 492 ? 0.7603 0.7895 0.4307 0.1474  -0.0887 -0.2303 478 TYR A CZ  
3555 O OH  . TYR A 492 ? 0.7791 0.7842 0.4379 0.1348  -0.0962 -0.2562 478 TYR A OH  
3556 N N   . ASN A 493 ? 0.8350 0.8738 0.6200 0.1320  -0.0567 -0.1287 479 ASN A N   
3557 C CA  . ASN A 493 ? 0.8226 0.8520 0.6334 0.1087  -0.0625 -0.1272 479 ASN A CA  
3558 C C   . ASN A 493 ? 0.8202 0.8467 0.6559 0.1079  -0.0534 -0.1021 479 ASN A C   
3559 O O   . ASN A 493 ? 0.7777 0.7980 0.6342 0.0909  -0.0572 -0.0980 479 ASN A O   
3560 C CB  . ASN A 493 ? 0.8829 0.8806 0.6889 0.0969  -0.0662 -0.1480 479 ASN A CB  
3561 C CG  . ASN A 493 ? 0.9454 0.9493 0.7370 0.0866  -0.0805 -0.1744 479 ASN A CG  
3562 O OD1 . ASN A 493 ? 0.8616 0.8966 0.6530 0.0844  -0.0894 -0.1752 479 ASN A OD1 
3563 N ND2 . ASN A 493 ? 1.0278 1.0024 0.8073 0.0806  -0.0826 -0.1960 479 ASN A ND2 
3564 N N   . ASP A 494 ? 0.8182 0.8508 0.6528 0.1260  -0.0416 -0.0851 480 ASP A N   
3565 C CA  . ASP A 494 ? 0.7719 0.8082 0.6316 0.1244  -0.0347 -0.0612 480 ASP A CA  
3566 C C   . ASP A 494 ? 0.7154 0.7775 0.5859 0.1209  -0.0376 -0.0489 480 ASP A C   
3567 O O   . ASP A 494 ? 0.8210 0.9014 0.6774 0.1275  -0.0405 -0.0538 480 ASP A O   
3568 C CB  . ASP A 494 ? 0.7838 0.8176 0.6422 0.1440  -0.0204 -0.0465 480 ASP A CB  
3569 C CG  . ASP A 494 ? 0.8455 0.8525 0.6893 0.1517  -0.0150 -0.0574 480 ASP A CG  
3570 O OD1 . ASP A 494 ? 0.8656 0.8514 0.7168 0.1384  -0.0185 -0.0647 480 ASP A OD1 
3571 O OD2 . ASP A 494 ? 0.8515 0.8576 0.6765 0.1723  -0.0058 -0.0572 480 ASP A OD2 
3572 N N   . ILE A 495 ? 0.6075 0.6706 0.5021 0.1115  -0.0364 -0.0327 481 ILE A N   
3573 C CA  . ILE A 495 ? 0.5336 0.6153 0.4394 0.1077  -0.0374 -0.0199 481 ILE A CA  
3574 C C   . ILE A 495 ? 0.4683 0.5519 0.3937 0.1109  -0.0286 0.0017  481 ILE A C   
3575 O O   . ILE A 495 ? 0.4496 0.5224 0.3831 0.1134  -0.0237 0.0070  481 ILE A O   
3576 C CB  . ILE A 495 ? 0.4985 0.5794 0.4142 0.0882  -0.0481 -0.0247 481 ILE A CB  
3577 C CG1 . ILE A 495 ? 0.4825 0.5443 0.4143 0.0760  -0.0495 -0.0223 481 ILE A CG1 
3578 C CG2 . ILE A 495 ? 0.5368 0.6219 0.4372 0.0837  -0.0573 -0.0444 481 ILE A CG2 
3579 C CD1 . ILE A 495 ? 0.4393 0.4961 0.3772 0.0585  -0.0591 -0.0300 481 ILE A CD1 
3580 N N   . ALA A 496 ? 0.4078 0.5059 0.3416 0.1106  -0.0264 0.0145  482 ALA A N   
3581 C CA  . ALA A 496 ? 0.3297 0.4290 0.2867 0.1063  -0.0218 0.0328  482 ALA A CA  
3582 C C   . ALA A 496 ? 0.3492 0.4361 0.3203 0.0887  -0.0301 0.0311  482 ALA A C   
3583 O O   . ALA A 496 ? 0.3205 0.4029 0.2875 0.0773  -0.0390 0.0208  482 ALA A O   
3584 C CB  . ALA A 496 ? 0.2912 0.4036 0.2529 0.1067  -0.0186 0.0441  482 ALA A CB  
3585 N N   . LEU A 497 ? 0.3012 0.3846 0.2895 0.0875  -0.0269 0.0421  483 LEU A N   
3586 C CA  . LEU A 497 ? 0.3298 0.4032 0.3310 0.0736  -0.0339 0.0425  483 LEU A CA  
3587 C C   . LEU A 497 ? 0.2881 0.3680 0.3054 0.0628  -0.0373 0.0536  483 LEU A C   
3588 O O   . LEU A 497 ? 0.2733 0.3625 0.3056 0.0653  -0.0321 0.0675  483 LEU A O   
3589 C CB  . LEU A 497 ? 0.3200 0.3873 0.3292 0.0795  -0.0291 0.0477  483 LEU A CB  
3590 C CG  . LEU A 497 ? 0.3693 0.4259 0.3594 0.0917  -0.0242 0.0359  483 LEU A CG  
3591 C CD1 . LEU A 497 ? 0.3589 0.4079 0.3552 0.1007  -0.0169 0.0427  483 LEU A CD1 
3592 C CD2 . LEU A 497 ? 0.4005 0.4437 0.3757 0.0828  -0.0323 0.0166  483 LEU A CD2 
3593 N N   . TRP A 498 ? 0.2524 0.3270 0.2667 0.0507  -0.0456 0.0473  484 TRP A N   
3594 C CA  . TRP A 498 ? 0.2556 0.3323 0.2791 0.0405  -0.0494 0.0544  484 TRP A CA  
3595 C C   . TRP A 498 ? 0.2824 0.3534 0.3191 0.0302  -0.0558 0.0584  484 TRP A C   
3596 O O   . TRP A 498 ? 0.2779 0.3418 0.3146 0.0297  -0.0581 0.0545  484 TRP A O   
3597 C CB  . TRP A 498 ? 0.2518 0.3267 0.2620 0.0356  -0.0539 0.0461  484 TRP A CB  
3598 C CG  . TRP A 498 ? 0.2552 0.3400 0.2541 0.0456  -0.0480 0.0457  484 TRP A CG  
3599 C CD1 . TRP A 498 ? 0.2463 0.3396 0.2434 0.0590  -0.0391 0.0506  484 TRP A CD1 
3600 C CD2 . TRP A 498 ? 0.2442 0.3330 0.2313 0.0450  -0.0496 0.0416  484 TRP A CD2 
3601 N NE1 . TRP A 498 ? 0.2647 0.3673 0.2488 0.0671  -0.0354 0.0496  484 TRP A NE1 
3602 C CE2 . TRP A 498 ? 0.2444 0.3452 0.2226 0.0586  -0.0419 0.0442  484 TRP A CE2 
3603 C CE3 . TRP A 498 ? 0.2649 0.3498 0.2480 0.0357  -0.0561 0.0372  484 TRP A CE3 
3604 C CZ2 . TRP A 498 ? 0.2460 0.3561 0.2118 0.0633  -0.0408 0.0427  484 TRP A CZ2 
3605 C CZ3 . TRP A 498 ? 0.2453 0.3392 0.2170 0.0399  -0.0547 0.0359  484 TRP A CZ3 
3606 C CH2 . TRP A 498 ? 0.2395 0.3465 0.2028 0.0537  -0.0474 0.0386  484 TRP A CH2 
3607 N N   . ASN A 499 ? 0.2665 0.3400 0.3133 0.0222  -0.0586 0.0662  485 ASN A N   
3608 C CA  . ASN A 499 ? 0.2924 0.3630 0.3497 0.0122  -0.0664 0.0696  485 ASN A CA  
3609 C C   . ASN A 499 ? 0.2841 0.3446 0.3297 0.0034  -0.0733 0.0625  485 ASN A C   
3610 O O   . ASN A 499 ? 0.2683 0.3266 0.3140 -0.0034 -0.0762 0.0649  485 ASN A O   
3611 C CB  . ASN A 499 ? 0.2923 0.3722 0.3681 0.0080  -0.0661 0.0811  485 ASN A CB  
3612 C CG  . ASN A 499 ? 0.3155 0.3988 0.4045 0.0009  -0.0740 0.0857  485 ASN A CG  
3613 O OD1 . ASN A 499 ? 0.3545 0.4322 0.4382 0.0010  -0.0782 0.0815  485 ASN A OD1 
3614 N ND2 . ASN A 499 ? 0.3330 0.4263 0.4402 -0.0055 -0.0761 0.0946  485 ASN A ND2 
3615 N N   . TRP A 500 ? 0.2655 0.3189 0.3011 0.0038  -0.0753 0.0540  486 TRP A N   
3616 C CA  . TRP A 500 ? 0.2784 0.3246 0.3023 -0.0020 -0.0796 0.0478  486 TRP A CA  
3617 C C   . TRP A 500 ? 0.2747 0.3160 0.3005 -0.0105 -0.0860 0.0519  486 TRP A C   
3618 O O   . TRP A 500 ? 0.2810 0.3183 0.2982 -0.0138 -0.0871 0.0510  486 TRP A O   
3619 C CB  . TRP A 500 ? 0.2847 0.3245 0.3031 -0.0019 -0.0805 0.0396  486 TRP A CB  
3620 C CG  . TRP A 500 ? 0.2955 0.3387 0.3080 0.0052  -0.0758 0.0324  486 TRP A CG  
3621 C CD1 . TRP A 500 ? 0.3073 0.3492 0.3218 0.0121  -0.0715 0.0306  486 TRP A CD1 
3622 C CD2 . TRP A 500 ? 0.2779 0.3275 0.2795 0.0075  -0.0747 0.0259  486 TRP A CD2 
3623 N NE1 . TRP A 500 ? 0.2984 0.3437 0.3023 0.0179  -0.0688 0.0217  486 TRP A NE1 
3624 C CE2 . TRP A 500 ? 0.2875 0.3396 0.2843 0.0151  -0.0712 0.0189  486 TRP A CE2 
3625 C CE3 . TRP A 500 ? 0.2641 0.3180 0.2586 0.0050  -0.0763 0.0256  486 TRP A CE3 
3626 C CZ2 . TRP A 500 ? 0.2725 0.3338 0.2578 0.0195  -0.0706 0.0110  486 TRP A CZ2 
3627 C CZ3 . TRP A 500 ? 0.2585 0.3227 0.2434 0.0100  -0.0747 0.0195  486 TRP A CZ3 
3628 C CH2 . TRP A 500 ? 0.2574 0.3263 0.2379 0.0169  -0.0727 0.0119  486 TRP A CH2 
3629 N N   . THR A 501 ? 0.3033 0.3454 0.3390 -0.0129 -0.0902 0.0567  487 THR A N   
3630 C CA  . THR A 501 ? 0.3103 0.3480 0.3445 -0.0204 -0.0978 0.0588  487 THR A CA  
3631 C C   . THR A 501 ? 0.3238 0.3628 0.3614 -0.0257 -0.0993 0.0621  487 THR A C   
3632 O O   . THR A 501 ? 0.3231 0.3566 0.3569 -0.0325 -0.1063 0.0620  487 THR A O   
3633 C CB  . THR A 501 ? 0.3167 0.3579 0.3599 -0.0206 -0.1027 0.0635  487 THR A CB  
3634 O OG1 . THR A 501 ? 0.3263 0.3802 0.3863 -0.0181 -0.1011 0.0705  487 THR A OG1 
3635 C CG2 . THR A 501 ? 0.3347 0.3697 0.3738 -0.0158 -0.0996 0.0605  487 THR A CG2 
3636 N N   . GLN A 502 ? 0.2894 0.3346 0.3339 -0.0226 -0.0926 0.0653  488 GLN A N   
3637 C CA  . GLN A 502 ? 0.3130 0.3567 0.3618 -0.0280 -0.0918 0.0689  488 GLN A CA  
3638 C C   . GLN A 502 ? 0.3106 0.3462 0.3452 -0.0250 -0.0851 0.0663  488 GLN A C   
3639 O O   . GLN A 502 ? 0.3028 0.3323 0.3382 -0.0291 -0.0829 0.0691  488 GLN A O   
3640 C CB  . GLN A 502 ? 0.3010 0.3580 0.3706 -0.0264 -0.0873 0.0774  488 GLN A CB  
3641 C CG  . GLN A 502 ? 0.3433 0.4104 0.4297 -0.0316 -0.0950 0.0822  488 GLN A CG  
3642 C CD  . GLN A 502 ? 0.3751 0.4359 0.4609 -0.0442 -0.1055 0.0800  488 GLN A CD  
3643 O OE1 . GLN A 502 ? 0.4057 0.4584 0.4909 -0.0508 -0.1043 0.0796  488 GLN A OE1 
3644 N NE2 . GLN A 502 ? 0.3471 0.4094 0.4302 -0.0467 -0.1151 0.0781  488 GLN A NE2 
3645 N N   . ILE A 503 ? 0.3004 0.3361 0.3225 -0.0181 -0.0819 0.0614  489 ILE A N   
3646 C CA  . ILE A 503 ? 0.2986 0.3317 0.3080 -0.0132 -0.0752 0.0604  489 ILE A CA  
3647 C C   . ILE A 503 ? 0.3118 0.3305 0.3088 -0.0185 -0.0775 0.0592  489 ILE A C   
3648 O O   . ILE A 503 ? 0.3385 0.3513 0.3312 -0.0171 -0.0712 0.0627  489 ILE A O   
3649 C CB  . ILE A 503 ? 0.3046 0.3450 0.3051 -0.0056 -0.0731 0.0546  489 ILE A CB  
3650 C CG1 . ILE A 503 ? 0.2850 0.3365 0.2940 0.0015  -0.0690 0.0553  489 ILE A CG1 
3651 C CG2 . ILE A 503 ? 0.2829 0.3248 0.2703 0.0003  -0.0671 0.0546  489 ILE A CG2 
3652 C CD1 . ILE A 503 ? 0.3017 0.3597 0.3018 0.0079  -0.0681 0.0473  489 ILE A CD1 
3653 N N   . PRO A 504 ? 0.3320 0.3432 0.3218 -0.0233 -0.0850 0.0553  490 PRO A N   
3654 C CA  . PRO A 504 ? 0.3449 0.3406 0.3197 -0.0265 -0.0860 0.0544  490 PRO A CA  
3655 C C   . PRO A 504 ? 0.3574 0.3422 0.3359 -0.0331 -0.0860 0.0569  490 PRO A C   
3656 O O   . PRO A 504 ? 0.3645 0.3359 0.3310 -0.0320 -0.0805 0.0575  490 PRO A O   
3657 C CB  . PRO A 504 ? 0.3509 0.3426 0.3203 -0.0298 -0.0944 0.0511  490 PRO A CB  
3658 C CG  . PRO A 504 ? 0.3189 0.3235 0.2955 -0.0256 -0.0938 0.0496  490 PRO A CG  
3659 C CD  . PRO A 504 ? 0.3022 0.3170 0.2940 -0.0242 -0.0909 0.0521  490 PRO A CD  
3660 N N   . GLN A 505 ? 0.3277 0.3183 0.3234 -0.0398 -0.0913 0.0588  491 GLN A N   
3661 C CA  . GLN A 505 ? 0.3648 0.3476 0.3692 -0.0486 -0.0922 0.0609  491 GLN A CA  
3662 C C   . GLN A 505 ? 0.3471 0.3324 0.3612 -0.0450 -0.0803 0.0675  491 GLN A C   
3663 O O   . GLN A 505 ? 0.3161 0.2907 0.3363 -0.0524 -0.0781 0.0696  491 GLN A O   
3664 C CB  . GLN A 505 ? 0.3740 0.3678 0.3968 -0.0572 -0.1028 0.0617  491 GLN A CB  
3665 C CG  . GLN A 505 ? 0.4177 0.4118 0.4318 -0.0590 -0.1144 0.0570  491 GLN A CG  
3666 C CD  . GLN A 505 ? 0.5049 0.5068 0.5140 -0.0495 -0.1125 0.0567  491 GLN A CD  
3667 O OE1 . GLN A 505 ? 0.3793 0.3919 0.3970 -0.0430 -0.1059 0.0594  491 GLN A OE1 
3668 N NE2 . GLN A 505 ? 0.4612 0.4567 0.4560 -0.0489 -0.1183 0.0532  491 GLN A NE2 
3669 N N   . ALA A 506 ? 0.3121 0.3102 0.3274 -0.0338 -0.0721 0.0707  492 ALA A N   
3670 C CA  . ALA A 506 ? 0.3106 0.3103 0.3302 -0.0272 -0.0592 0.0779  492 ALA A CA  
3671 C C   . ALA A 506 ? 0.3234 0.3113 0.3222 -0.0198 -0.0510 0.0776  492 ALA A C   
3672 O O   . ALA A 506 ? 0.2937 0.2725 0.2927 -0.0177 -0.0407 0.0837  492 ALA A O   
3673 C CB  . ALA A 506 ? 0.3077 0.3278 0.3360 -0.0165 -0.0538 0.0817  492 ALA A CB  
3674 N N   . LEU A 507 ? 0.3442 0.3327 0.3262 -0.0154 -0.0544 0.0720  493 LEU A N   
3675 C CA  . LEU A 507 ? 0.3343 0.3169 0.2974 -0.0064 -0.0466 0.0730  493 LEU A CA  
3676 C C   . LEU A 507 ? 0.3541 0.3134 0.3016 -0.0117 -0.0486 0.0702  493 LEU A C   
3677 O O   . LEU A 507 ? 0.3831 0.3379 0.3131 -0.0038 -0.0434 0.0708  493 LEU A O   
3678 C CB  . LEU A 507 ? 0.3258 0.3256 0.2814 0.0019  -0.0483 0.0694  493 LEU A CB  
3679 C CG  . LEU A 507 ? 0.3228 0.3433 0.2895 0.0078  -0.0471 0.0697  493 LEU A CG  
3680 C CD1 . LEU A 507 ? 0.2752 0.3109 0.2337 0.0142  -0.0495 0.0642  493 LEU A CD1 
3681 C CD2 . LEU A 507 ? 0.2876 0.3125 0.2593 0.0161  -0.0352 0.0784  493 LEU A CD2 
3682 N N   . SER A 508 ? 0.3635 0.3088 0.3164 -0.0241 -0.0559 0.0671  494 SER A N   
3683 C CA  . SER A 508 ? 0.4003 0.3206 0.3357 -0.0291 -0.0583 0.0628  494 SER A CA  
3684 C C   . SER A 508 ? 0.4118 0.3185 0.3579 -0.0434 -0.0641 0.0604  494 SER A C   
3685 O O   . SER A 508 ? 0.3893 0.3101 0.3554 -0.0511 -0.0724 0.0601  494 SER A O   
3686 C CB  . SER A 508 ? 0.4017 0.3228 0.3240 -0.0290 -0.0678 0.0569  494 SER A CB  
3687 O OG  . SER A 508 ? 0.4392 0.3349 0.3420 -0.0323 -0.0697 0.0527  494 SER A OG  
3688 N N   . LEU A 509 ? 0.4402 0.3192 0.3723 -0.0471 -0.0602 0.0582  495 LEU A N   
3689 C CA  . LEU A 509 ? 0.4648 0.3284 0.4051 -0.0630 -0.0677 0.0533  495 LEU A CA  
3690 C C   . LEU A 509 ? 0.4821 0.3425 0.4128 -0.0709 -0.0844 0.0435  495 LEU A C   
3691 O O   . LEU A 509 ? 0.5171 0.3767 0.4601 -0.0849 -0.0953 0.0388  495 LEU A O   
3692 C CB  . LEU A 509 ? 0.4637 0.2945 0.3909 -0.0645 -0.0568 0.0532  495 LEU A CB  
3693 C CG  . LEU A 509 ? 0.4611 0.2907 0.3988 -0.0577 -0.0389 0.0643  495 LEU A CG  
3694 C CD1 . LEU A 509 ? 0.4898 0.2809 0.4128 -0.0603 -0.0280 0.0634  495 LEU A CD1 
3695 C CD2 . LEU A 509 ? 0.3968 0.2476 0.3685 -0.0650 -0.0397 0.0704  495 LEU A CD2 
3696 N N   . ASP A 510 ? 0.4937 0.3539 0.4034 -0.0618 -0.0864 0.0410  496 ASP A N   
3697 C CA  . ASP A 510 ? 0.5082 0.3652 0.4055 -0.0660 -0.1003 0.0333  496 ASP A CA  
3698 C C   . ASP A 510 ? 0.5028 0.3745 0.3915 -0.0544 -0.1002 0.0357  496 ASP A C   
3699 O O   . ASP A 510 ? 0.5366 0.3953 0.4011 -0.0469 -0.0976 0.0342  496 ASP A O   
3700 C CB  . ASP A 510 ? 0.5844 0.4077 0.4550 -0.0694 -0.1013 0.0254  496 ASP A CB  
3701 C CG  . ASP A 510 ? 0.6438 0.4639 0.5014 -0.0745 -0.1171 0.0167  496 ASP A CG  
3702 O OD1 . ASP A 510 ? 0.6464 0.4888 0.5225 -0.0810 -0.1290 0.0163  496 ASP A OD1 
3703 O OD2 . ASP A 510 ? 0.7213 0.5170 0.5487 -0.0705 -0.1169 0.0109  496 ASP A OD2 
3704 N N   . PRO A 511 ? 0.5067 0.4047 0.4153 -0.0526 -0.1021 0.0398  497 PRO A N   
3705 C CA  . PRO A 511 ? 0.4734 0.3846 0.3771 -0.0428 -0.1003 0.0422  497 PRO A CA  
3706 C C   . PRO A 511 ? 0.4882 0.3944 0.3769 -0.0423 -0.1089 0.0387  497 PRO A C   
3707 O O   . PRO A 511 ? 0.4571 0.3649 0.3499 -0.0493 -0.1199 0.0355  497 PRO A O   
3708 C CB  . PRO A 511 ? 0.4174 0.3533 0.3462 -0.0435 -0.1018 0.0455  497 PRO A CB  
3709 C CG  . PRO A 511 ? 0.4396 0.3769 0.3862 -0.0510 -0.1014 0.0471  497 PRO A CG  
3710 C CD  . PRO A 511 ? 0.4553 0.3716 0.3918 -0.0600 -0.1069 0.0421  497 PRO A CD  
3711 N N   . GLN A 512 ? 0.4860 0.3882 0.3578 -0.0330 -0.1034 0.0404  498 GLN A N   
3712 C CA  . GLN A 512 ? 0.5302 0.4305 0.3889 -0.0298 -0.1091 0.0396  498 GLN A CA  
3713 C C   . GLN A 512 ? 0.4980 0.4209 0.3749 -0.0276 -0.1095 0.0436  498 GLN A C   
3714 O O   . GLN A 512 ? 0.4803 0.4103 0.3560 -0.0209 -0.1032 0.0472  498 GLN A O   
3715 C CB  . GLN A 512 ? 0.5779 0.4621 0.4101 -0.0205 -0.1019 0.0409  498 GLN A CB  
3716 C CG  . GLN A 512 ? 0.6630 0.5529 0.4867 -0.0128 -0.1020 0.0447  498 GLN A CG  
3717 C CD  . GLN A 512 ? 0.8356 0.7050 0.6286 -0.0043 -0.0983 0.0450  498 GLN A CD  
3718 O OE1 . GLN A 512 ? 0.6275 0.4918 0.4098 0.0039  -0.0875 0.0491  498 GLN A OE1 
3719 N NE2 . GLN A 512 ? 0.9799 0.8388 0.7574 -0.0047 -0.1068 0.0412  498 GLN A NE2 
3720 N N   . ALA A 513 ? 0.4710 0.4061 0.3679 -0.0338 -0.1156 0.0431  499 ALA A N   
3721 C CA  . ALA A 513 ? 0.4436 0.3970 0.3588 -0.0322 -0.1146 0.0461  499 ALA A CA  
3722 C C   . ALA A 513 ? 0.4465 0.4079 0.3730 -0.0358 -0.1236 0.0468  499 ALA A C   
3723 O O   . ALA A 513 ? 0.4188 0.3777 0.3458 -0.0417 -0.1314 0.0448  499 ALA A O   
3724 C CB  . ALA A 513 ? 0.3767 0.3404 0.3071 -0.0322 -0.1083 0.0468  499 ALA A CB  
3725 N N   . GLN A 514 ? 0.4259 0.3970 0.3613 -0.0322 -0.1222 0.0498  500 GLN A N   
3726 C CA  . GLN A 514 ? 0.4110 0.3926 0.3605 -0.0331 -0.1275 0.0525  500 GLN A CA  
3727 C C   . GLN A 514 ? 0.3992 0.3907 0.3655 -0.0307 -0.1212 0.0540  500 GLN A C   
3728 O O   . GLN A 514 ? 0.4021 0.3922 0.3663 -0.0278 -0.1148 0.0532  500 GLN A O   
3729 C CB  . GLN A 514 ? 0.4781 0.4577 0.4181 -0.0291 -0.1320 0.0555  500 GLN A CB  
3730 C CG  . GLN A 514 ? 0.4579 0.4495 0.4104 -0.0298 -0.1392 0.0590  500 GLN A CG  
3731 C CD  . GLN A 514 ? 0.5362 0.5264 0.4754 -0.0268 -0.1451 0.0593  500 GLN A CD  
3732 O OE1 . GLN A 514 ? 0.6668 0.6453 0.5864 -0.0265 -0.1464 0.0550  500 GLN A OE1 
3733 N NE2 . GLN A 514 ? 0.5300 0.5328 0.4790 -0.0231 -0.1478 0.0643  500 GLN A NE2 
3734 N N   . CYS A 515 ? 0.3962 0.3979 0.3789 -0.0321 -0.1228 0.0559  501 CYS A N   
3735 C CA  . CYS A 515 ? 0.3797 0.3883 0.3756 -0.0288 -0.1164 0.0564  501 CYS A CA  
3736 C C   . CYS A 515 ? 0.3707 0.3854 0.3772 -0.0255 -0.1180 0.0615  501 CYS A C   
3737 O O   . CYS A 515 ? 0.4070 0.4284 0.4176 -0.0266 -0.1249 0.0655  501 CYS A O   
3738 C CB  . CYS A 515 ? 0.3535 0.3685 0.3586 -0.0300 -0.1133 0.0556  501 CYS A CB  
3739 S SG  . CYS A 515 ? 0.3696 0.3770 0.3615 -0.0317 -0.1099 0.0518  501 CYS A SG  
3740 N N   . TRP A 516 ? 0.3697 0.3824 0.3809 -0.0212 -0.1114 0.0612  502 TRP A N   
3741 C CA  . TRP A 516 ? 0.3423 0.3580 0.3633 -0.0161 -0.1096 0.0667  502 TRP A CA  
3742 C C   . TRP A 516 ? 0.3516 0.3664 0.3807 -0.0127 -0.1016 0.0638  502 TRP A C   
3743 O O   . TRP A 516 ? 0.3261 0.3361 0.3510 -0.0143 -0.0976 0.0565  502 TRP A O   
3744 C CB  . TRP A 516 ? 0.3433 0.3507 0.3586 -0.0127 -0.1078 0.0700  502 TRP A CB  
3745 C CG  . TRP A 516 ? 0.3928 0.4005 0.3972 -0.0128 -0.1148 0.0737  502 TRP A CG  
3746 C CD1 . TRP A 516 ? 0.3965 0.4115 0.4016 -0.0087 -0.1203 0.0809  502 TRP A CD1 
3747 C CD2 . TRP A 516 ? 0.4373 0.4377 0.4262 -0.0155 -0.1169 0.0705  502 TRP A CD2 
3748 N NE1 . TRP A 516 ? 0.4422 0.4543 0.4317 -0.0090 -0.1265 0.0811  502 TRP A NE1 
3749 C CE2 . TRP A 516 ? 0.4507 0.4524 0.4296 -0.0129 -0.1239 0.0750  502 TRP A CE2 
3750 C CE3 . TRP A 516 ? 0.3922 0.3863 0.3740 -0.0187 -0.1133 0.0649  502 TRP A CE3 
3751 C CZ2 . TRP A 516 ? 0.4511 0.4449 0.4113 -0.0129 -0.1267 0.0733  502 TRP A CZ2 
3752 C CZ3 . TRP A 516 ? 0.4134 0.4010 0.3787 -0.0186 -0.1154 0.0647  502 TRP A CZ3 
3753 C CH2 . TRP A 516 ? 0.4099 0.3958 0.3636 -0.0156 -0.1217 0.0686  502 TRP A CH2 
3754 N N   . ARG A 517 ? 0.3193 0.3393 0.3589 -0.0071 -0.0994 0.0694  503 ARG A N   
3755 C CA  . ARG A 517 ? 0.3524 0.3675 0.3970 -0.0016 -0.0908 0.0672  503 ARG A CA  
3756 C C   . ARG A 517 ? 0.3573 0.3633 0.4037 0.0041  -0.0861 0.0722  503 ARG A C   
3757 O O   . ARG A 517 ? 0.3701 0.3840 0.4215 0.0085  -0.0887 0.0820  503 ARG A O   
3758 C CB  . ARG A 517 ? 0.3933 0.4210 0.4482 0.0027  -0.0893 0.0713  503 ARG A CB  
3759 C CG  . ARG A 517 ? 0.4149 0.4365 0.4723 0.0110  -0.0798 0.0697  503 ARG A CG  
3760 C CD  . ARG A 517 ? 0.4562 0.4873 0.5168 0.0137  -0.0770 0.0685  503 ARG A CD  
3761 N NE  . ARG A 517 ? 0.5228 0.5662 0.5964 0.0217  -0.0737 0.0791  503 ARG A NE  
3762 C CZ  . ARG A 517 ? 0.6407 0.7026 0.7270 0.0195  -0.0782 0.0879  503 ARG A CZ  
3763 N NH1 . ARG A 517 ? 0.5487 0.6156 0.6345 0.0095  -0.0859 0.0861  503 ARG A NH1 
3764 N NH2 . ARG A 517 ? 0.5445 0.6202 0.6451 0.0274  -0.0745 0.0989  503 ARG A NH2 
3765 N N   . VAL A 518 ? 0.3330 0.3232 0.3761 0.0041  -0.0791 0.0659  504 VAL A N   
3766 C CA  . VAL A 518 ? 0.3740 0.3511 0.4189 0.0091  -0.0723 0.0707  504 VAL A CA  
3767 C C   . VAL A 518 ? 0.3928 0.3563 0.4397 0.0135  -0.0627 0.0652  504 VAL A C   
3768 O O   . VAL A 518 ? 0.3601 0.3201 0.4033 0.0097  -0.0619 0.0537  504 VAL A O   
3769 C CB  . VAL A 518 ? 0.3684 0.3349 0.4082 0.0037  -0.0717 0.0692  504 VAL A CB  
3770 C CG1 . VAL A 518 ? 0.3854 0.3629 0.4192 0.0011  -0.0806 0.0740  504 VAL A CG1 
3771 C CG2 . VAL A 518 ? 0.3592 0.3174 0.3967 -0.0043 -0.0697 0.0562  504 VAL A CG2 
3772 N N   . SER A 519 ? 0.3893 0.3451 0.4404 0.0228  -0.0552 0.0735  505 SER A N   
3773 C CA  . SER A 519 ? 0.4161 0.3533 0.4669 0.0286  -0.0442 0.0689  505 SER A CA  
3774 C C   . SER A 519 ? 0.4299 0.3450 0.4816 0.0317  -0.0345 0.0729  505 SER A C   
3775 O O   . SER A 519 ? 0.4582 0.3521 0.5084 0.0357  -0.0242 0.0679  505 SER A O   
3776 C CB  . SER A 519 ? 0.4178 0.3649 0.4730 0.0406  -0.0406 0.0767  505 SER A CB  
3777 O OG  . SER A 519 ? 0.5116 0.4712 0.5740 0.0482  -0.0414 0.0929  505 SER A OG  
3778 N N   . GLU A 520 ? 0.4531 0.3711 0.5064 0.0310  -0.0364 0.0822  506 GLU A N   
3779 C CA  . GLU A 520 ? 0.4976 0.3960 0.5529 0.0357  -0.0257 0.0894  506 GLU A CA  
3780 C C   . GLU A 520 ? 0.4561 0.3481 0.5109 0.0249  -0.0273 0.0859  506 GLU A C   
3781 O O   . GLU A 520 ? 0.4487 0.3570 0.5002 0.0187  -0.0377 0.0848  506 GLU A O   
3782 C CB  . GLU A 520 ? 0.4880 0.3986 0.5460 0.0492  -0.0243 0.1083  506 GLU A CB  
3783 C CG  . GLU A 520 ? 0.4919 0.4171 0.5536 0.0604  -0.0241 0.1151  506 GLU A CG  
3784 C CD  . GLU A 520 ? 0.5128 0.4162 0.5742 0.0676  -0.0107 0.1111  506 GLU A CD  
3785 O OE1 . GLU A 520 ? 0.5551 0.4328 0.6158 0.0724  0.0022  0.1137  506 GLU A OE1 
3786 O OE2 . GLU A 520 ? 0.4893 0.3998 0.5506 0.0691  -0.0121 0.1056  506 GLU A OE2 
3787 N N   . ALA A 521 ? 0.4946 0.3619 0.5530 0.0232  -0.0159 0.0850  507 ALA A N   
3788 C CA  . ALA A 521 ? 0.4903 0.3523 0.5515 0.0131  -0.0157 0.0835  507 ALA A CA  
3789 C C   . ALA A 521 ? 0.4888 0.3666 0.5467 0.0183  -0.0202 0.0978  507 ALA A C   
3790 O O   . ALA A 521 ? 0.4423 0.3290 0.4979 0.0106  -0.0265 0.0955  507 ALA A O   
3791 C CB  . ALA A 521 ? 0.5694 0.4013 0.6382 0.0110  -0.0010 0.0828  507 ALA A CB  
3792 N N   . GLU A 522 ? 0.4933 0.3754 0.5495 0.0324  -0.0169 0.1129  508 GLU A N   
3793 C CA  . GLU A 522 ? 0.4760 0.3725 0.5264 0.0389  -0.0213 0.1261  508 GLU A CA  
3794 C C   . GLU A 522 ? 0.4664 0.3878 0.5087 0.0349  -0.0378 0.1218  508 GLU A C   
3795 O O   . GLU A 522 ? 0.4578 0.3875 0.4922 0.0342  -0.0435 0.1253  508 GLU A O   
3796 C CB  . GLU A 522 ? 0.5284 0.4267 0.5786 0.0561  -0.0144 0.1432  508 GLU A CB  
3797 C CG  . GLU A 522 ? 0.5991 0.4720 0.6569 0.0617  0.0021  0.1457  508 GLU A CG  
3798 C CD  . GLU A 522 ? 0.6199 0.4950 0.6795 0.0639  0.0009  0.1390  508 GLU A CD  
3799 O OE1 . GLU A 522 ? 0.5830 0.4826 0.6409 0.0713  -0.0078 0.1452  508 GLU A OE1 
3800 O OE2 . GLU A 522 ? 0.7841 0.6383 0.8466 0.0576  0.0075  0.1268  508 GLU A OE2 
3801 N N   . GLN A 523 ? 0.4736 0.4058 0.5172 0.0335  -0.0446 0.1153  509 GLN A N   
3802 C CA  . GLN A 523 ? 0.4594 0.4117 0.4972 0.0279  -0.0589 0.1101  509 GLN A CA  
3803 C C   . GLN A 523 ? 0.4457 0.3943 0.4793 0.0160  -0.0621 0.0993  509 GLN A C   
3804 O O   . GLN A 523 ? 0.4563 0.4142 0.4809 0.0135  -0.0702 0.0996  509 GLN A O   
3805 C CB  . GLN A 523 ? 0.4498 0.4125 0.4928 0.0278  -0.0629 0.1055  509 GLN A CB  
3806 C CG  . GLN A 523 ? 0.4650 0.4339 0.5144 0.0400  -0.0588 0.1165  509 GLN A CG  
3807 C CD  . GLN A 523 ? 0.4581 0.4350 0.5140 0.0402  -0.0599 0.1119  509 GLN A CD  
3808 O OE1 . GLN A 523 ? 0.4355 0.4036 0.4905 0.0335  -0.0580 0.0998  509 GLN A OE1 
3809 N NE2 . GLN A 523 ? 0.4630 0.4589 0.5255 0.0485  -0.0627 0.1223  509 GLN A NE2 
3810 N N   . LEU A 524 ? 0.4307 0.3657 0.4698 0.0091  -0.0558 0.0895  510 LEU A N   
3811 C CA  . LEU A 524 ? 0.4193 0.3543 0.4565 -0.0016 -0.0585 0.0801  510 LEU A CA  
3812 C C   . LEU A 524 ? 0.4035 0.3354 0.4378 -0.0014 -0.0558 0.0880  510 LEU A C   
3813 O O   . LEU A 524 ? 0.3967 0.3374 0.4232 -0.0046 -0.0618 0.0870  510 LEU A O   
3814 C CB  . LEU A 524 ? 0.4205 0.3428 0.4651 -0.0089 -0.0527 0.0681  510 LEU A CB  
3815 C CG  . LEU A 524 ? 0.3847 0.3083 0.4311 -0.0202 -0.0541 0.0593  510 LEU A CG  
3816 C CD1 . LEU A 524 ? 0.3739 0.3155 0.4119 -0.0231 -0.0641 0.0547  510 LEU A CD1 
3817 C CD2 . LEU A 524 ? 0.4073 0.3184 0.4616 -0.0278 -0.0493 0.0465  510 LEU A CD2 
3818 N N   . ALA A 525 ? 0.4283 0.3472 0.4679 0.0042  -0.0455 0.0974  511 ALA A N   
3819 C CA  . ALA A 525 ? 0.4355 0.3520 0.4725 0.0068  -0.0411 0.1075  511 ALA A CA  
3820 C C   . ALA A 525 ? 0.4515 0.3829 0.4729 0.0141  -0.0503 0.1145  511 ALA A C   
3821 O O   . ALA A 525 ? 0.4514 0.3867 0.4648 0.0126  -0.0525 0.1159  511 ALA A O   
3822 C CB  . ALA A 525 ? 0.4369 0.3368 0.4820 0.0141  -0.0272 0.1189  511 ALA A CB  
3823 N N   . ASP A 526 ? 0.4834 0.4239 0.5002 0.0217  -0.0562 0.1184  512 ASP A N   
3824 C CA  . ASP A 526 ? 0.4979 0.4524 0.4996 0.0275  -0.0666 0.1233  512 ASP A CA  
3825 C C   . ASP A 526 ? 0.4473 0.4094 0.4405 0.0186  -0.0771 0.1124  512 ASP A C   
3826 O O   . ASP A 526 ? 0.4818 0.4462 0.4605 0.0202  -0.0812 0.1141  512 ASP A O   
3827 C CB  . ASP A 526 ? 0.5470 0.5133 0.5495 0.0358  -0.0718 0.1290  512 ASP A CB  
3828 C CG  . ASP A 526 ? 0.7743 0.7362 0.7791 0.0493  -0.0619 0.1440  512 ASP A CG  
3829 O OD1 . ASP A 526 ? 0.8255 0.7746 0.8295 0.0524  -0.0515 0.1506  512 ASP A OD1 
3830 O OD2 . ASP A 526 ? 0.9573 0.9295 0.9655 0.0575  -0.0638 0.1504  512 ASP A OD2 
3831 N N   . VAL A 527 ? 0.4331 0.3978 0.4336 0.0105  -0.0802 0.1018  513 VAL A N   
3832 C CA  . VAL A 527 ? 0.4273 0.3980 0.4203 0.0031  -0.0882 0.0926  513 VAL A CA  
3833 C C   . VAL A 527 ? 0.3970 0.3620 0.3851 -0.0006 -0.0840 0.0910  513 VAL A C   
3834 O O   . VAL A 527 ? 0.4194 0.3869 0.3936 -0.0005 -0.0887 0.0904  513 VAL A O   
3835 C CB  . VAL A 527 ? 0.4109 0.3854 0.4134 -0.0030 -0.0898 0.0833  513 VAL A CB  
3836 C CG1 . VAL A 527 ? 0.3716 0.3504 0.3670 -0.0096 -0.0950 0.0751  513 VAL A CG1 
3837 C CG2 . VAL A 527 ? 0.4271 0.4110 0.4346 0.0011  -0.0945 0.0866  513 VAL A CG2 
3838 N N   . LEU A 528 ? 0.3783 0.3356 0.3783 -0.0038 -0.0747 0.0905  514 LEU A N   
3839 C CA  . LEU A 528 ? 0.4003 0.3565 0.4001 -0.0081 -0.0707 0.0897  514 LEU A CA  
3840 C C   . LEU A 528 ? 0.4331 0.3880 0.4202 -0.0003 -0.0688 0.1006  514 LEU A C   
3841 O O   . LEU A 528 ? 0.4282 0.3864 0.4053 -0.0006 -0.0700 0.1005  514 LEU A O   
3842 C CB  . LEU A 528 ? 0.3696 0.3182 0.3873 -0.0143 -0.0616 0.0874  514 LEU A CB  
3843 C CG  . LEU A 528 ? 0.3914 0.3423 0.4177 -0.0228 -0.0639 0.0738  514 LEU A CG  
3844 C CD1 . LEU A 528 ? 0.3761 0.3163 0.4188 -0.0296 -0.0557 0.0700  514 LEU A CD1 
3845 C CD2 . LEU A 528 ? 0.3545 0.3181 0.3747 -0.0276 -0.0699 0.0666  514 LEU A CD2 
3846 N N   . GLU A 529 ? 0.4546 0.4050 0.4404 0.0086  -0.0651 0.1110  515 GLU A N   
3847 C CA  . GLU A 529 ? 0.4494 0.3994 0.4195 0.0188  -0.0638 0.1219  515 GLU A CA  
3848 C C   . GLU A 529 ? 0.4459 0.4019 0.3940 0.0212  -0.0755 0.1177  515 GLU A C   
3849 O O   . GLU A 529 ? 0.4644 0.4190 0.3969 0.0258  -0.0747 0.1211  515 GLU A O   
3850 C CB  . GLU A 529 ? 0.5241 0.4707 0.4953 0.0296  -0.0590 0.1336  515 GLU A CB  
3851 C CG  . GLU A 529 ? 0.6249 0.5678 0.5870 0.0409  -0.0507 0.1479  515 GLU A CG  
3852 C CD  . GLU A 529 ? 0.7485 0.6927 0.7046 0.0549  -0.0492 0.1598  515 GLU A CD  
3853 O OE1 . GLU A 529 ? 0.8148 0.7580 0.7835 0.0549  -0.0477 0.1600  515 GLU A OE1 
3854 O OE2 . GLU A 529 ? 0.8465 0.7934 0.7841 0.0672  -0.0494 0.1692  515 GLU A OE2 
3855 N N   . LYS A 530 ? 0.4658 0.4277 0.4126 0.0182  -0.0857 0.1104  516 LYS A N   
3856 C CA  . LYS A 530 ? 0.4752 0.4405 0.4028 0.0183  -0.0970 0.1052  516 LYS A CA  
3857 C C   . LYS A 530 ? 0.4599 0.4221 0.3805 0.0126  -0.0967 0.0981  516 LYS A C   
3858 O O   . LYS A 530 ? 0.4657 0.4241 0.3654 0.0161  -0.1008 0.0971  516 LYS A O   
3859 C CB  . LYS A 530 ? 0.4818 0.4553 0.4155 0.0137  -0.1068 0.0991  516 LYS A CB  
3860 C CG  . LYS A 530 ? 0.5441 0.5239 0.4897 0.0186  -0.1063 0.1056  516 LYS A CG  
3861 C CD  . LYS A 530 ? 0.6216 0.6133 0.5606 0.0199  -0.1193 0.1048  516 LYS A CD  
3862 C CE  . LYS A 530 ? 0.6833 0.6858 0.6389 0.0233  -0.1194 0.1103  516 LYS A CE  
3863 N NZ  . LYS A 530 ? 0.5878 0.5971 0.5581 0.0144  -0.1231 0.1031  516 LYS A NZ  
3864 N N   . VAL A 531 ? 0.4344 0.3982 0.3706 0.0047  -0.0923 0.0928  517 VAL A N   
3865 C CA  . VAL A 531 ? 0.4160 0.3804 0.3466 0.0003  -0.0924 0.0867  517 VAL A CA  
3866 C C   . VAL A 531 ? 0.4070 0.3709 0.3386 0.0022  -0.0831 0.0921  517 VAL A C   
3867 O O   . VAL A 531 ? 0.4176 0.3854 0.3489 -0.0009 -0.0814 0.0885  517 VAL A O   
3868 C CB  . VAL A 531 ? 0.4202 0.3903 0.3644 -0.0080 -0.0943 0.0776  517 VAL A CB  
3869 C CG1 . VAL A 531 ? 0.3882 0.3608 0.3345 -0.0093 -0.1022 0.0746  517 VAL A CG1 
3870 C CG2 . VAL A 531 ? 0.3644 0.3372 0.3288 -0.0124 -0.0874 0.0765  517 VAL A CG2 
3871 N N   . ALA A 532 ? 0.4225 0.3833 0.3562 0.0081  -0.0766 0.1021  518 ALA A N   
3872 C CA  . ALA A 532 ? 0.4084 0.3709 0.3492 0.0089  -0.0664 0.1092  518 ALA A CA  
3873 C C   . ALA A 532 ? 0.4202 0.3842 0.3440 0.0131  -0.0654 0.1104  518 ALA A C   
3874 O O   . ALA A 532 ? 0.3828 0.3546 0.3166 0.0100  -0.0594 0.1121  518 ALA A O   
3875 C CB  . ALA A 532 ? 0.4098 0.3671 0.3519 0.0171  -0.0587 0.1222  518 ALA A CB  
3876 N N   . HIS A 533 ? 0.4468 0.4036 0.3447 0.0204  -0.0710 0.1096  519 HIS A N   
3877 C CA  . HIS A 533 ? 0.4362 0.3900 0.3141 0.0265  -0.0685 0.1112  519 HIS A CA  
3878 C C   . HIS A 533 ? 0.4357 0.3884 0.3063 0.0214  -0.0744 0.1005  519 HIS A C   
3879 O O   . HIS A 533 ? 0.4420 0.3885 0.2925 0.0274  -0.0724 0.1009  519 HIS A O   
3880 C CB  . HIS A 533 ? 0.4611 0.4042 0.3112 0.0395  -0.0687 0.1175  519 HIS A CB  
3881 C CG  . HIS A 533 ? 0.4740 0.4182 0.3306 0.0462  -0.0623 0.1294  519 HIS A CG  
3882 N ND1 . HIS A 533 ? 0.5100 0.4577 0.3749 0.0511  -0.0495 0.1406  519 HIS A ND1 
3883 C CD2 . HIS A 533 ? 0.4934 0.4363 0.3514 0.0492  -0.0656 0.1321  519 HIS A CD2 
3884 C CE1 . HIS A 533 ? 0.5016 0.4476 0.3728 0.0560  -0.0444 0.1486  519 HIS A CE1 
3885 N NE2 . HIS A 533 ? 0.5283 0.4713 0.3943 0.0558  -0.0539 0.1441  519 HIS A NE2 
3886 N N   . HIS A 534 ? 0.4244 0.3822 0.3107 0.0118  -0.0799 0.0921  520 HIS A N   
3887 C CA  . HIS A 534 ? 0.4140 0.3741 0.3007 0.0064  -0.0828 0.0837  520 HIS A CA  
3888 C C   . HIS A 534 ? 0.4413 0.3883 0.3013 0.0113  -0.0853 0.0809  520 HIS A C   
3889 O O   . HIS A 534 ? 0.4245 0.3705 0.2762 0.0140  -0.0806 0.0810  520 HIS A O   
3890 C CB  . HIS A 534 ? 0.4174 0.3912 0.3189 0.0038  -0.0760 0.0847  520 HIS A CB  
3891 C CG  . HIS A 534 ? 0.4107 0.3875 0.3061 0.0111  -0.0675 0.0943  520 HIS A CG  
3892 N ND1 . HIS A 534 ? 0.4306 0.4023 0.3051 0.0191  -0.0639 0.0968  520 HIS A ND1 
3893 C CD2 . HIS A 534 ? 0.4042 0.3880 0.3119 0.0124  -0.0607 0.1031  520 HIS A CD2 
3894 C CE1 . HIS A 534 ? 0.4274 0.4054 0.3020 0.0257  -0.0554 0.1072  520 HIS A CE1 
3895 N NE2 . HIS A 534 ? 0.4263 0.4122 0.3219 0.0212  -0.0534 0.1114  520 HIS A NE2 
3896 N N   . GLU A 535 ? 0.4675 0.4041 0.3140 0.0123  -0.0931 0.0782  521 GLU A N   
3897 C CA  . GLU A 535 ? 0.5022 0.4258 0.3273 0.0149  -0.0944 0.0717  521 GLU A CA  
3898 C C   . GLU A 535 ? 0.5039 0.4237 0.3316 0.0066  -0.0998 0.0641  521 GLU A C   
3899 O O   . GLU A 535 ? 0.4999 0.4051 0.3094 0.0076  -0.0997 0.0597  521 GLU A O   
3900 C CB  . GLU A 535 ? 0.5718 0.4907 0.3861 0.0175  -0.1007 0.0694  521 GLU A CB  
3901 C CG  . GLU A 535 ? 0.6484 0.5655 0.4486 0.0290  -0.0936 0.0760  521 GLU A CG  
3902 C CD  . GLU A 535 ? 1.0742 0.9838 0.8552 0.0322  -0.1006 0.0707  521 GLU A CD  
3903 O OE1 . GLU A 535 ? 0.9856 0.9032 0.7741 0.0303  -0.1081 0.0705  521 GLU A OE1 
3904 O OE2 . GLU A 535 ? 1.0651 0.9608 0.8232 0.0367  -0.0990 0.0666  521 GLU A OE2 
3905 N N   . ARG A 536 ? 0.4827 0.4148 0.3334 -0.0010 -0.1026 0.0629  522 ARG A N   
3906 C CA  . ARG A 536 ? 0.4681 0.4016 0.3278 -0.0079 -0.1046 0.0570  522 ARG A CA  
3907 C C   . ARG A 536 ? 0.4169 0.3669 0.2986 -0.0101 -0.0994 0.0581  522 ARG A C   
3908 O O   . ARG A 536 ? 0.3857 0.3448 0.2782 -0.0090 -0.0966 0.0617  522 ARG A O   
3909 C CB  . ARG A 536 ? 0.5026 0.4361 0.3687 -0.0148 -0.1150 0.0527  522 ARG A CB  
3910 C CG  . ARG A 536 ? 0.5722 0.4892 0.4172 -0.0161 -0.1220 0.0478  522 ARG A CG  
3911 C CD  . ARG A 536 ? 0.5904 0.5130 0.4436 -0.0229 -0.1340 0.0446  522 ARG A CD  
3912 N NE  . ARG A 536 ? 0.6808 0.6069 0.5274 -0.0167 -0.1362 0.0467  522 ARG A NE  
3913 C CZ  . ARG A 536 ? 0.8037 0.7433 0.6643 -0.0125 -0.1333 0.0531  522 ARG A CZ  
3914 N NH1 . ARG A 536 ? 0.6187 0.5685 0.5002 -0.0151 -0.1301 0.0566  522 ARG A NH1 
3915 N NH2 . ARG A 536 ? 0.7159 0.6573 0.5675 -0.0049 -0.1336 0.0562  522 ARG A NH2 
3916 N N   . LEU A 537 ? 0.4046 0.3577 0.2923 -0.0129 -0.0977 0.0549  523 LEU A N   
3917 C CA  . LEU A 537 ? 0.3743 0.3436 0.2821 -0.0152 -0.0952 0.0539  523 LEU A CA  
3918 C C   . LEU A 537 ? 0.3649 0.3388 0.2878 -0.0196 -0.1008 0.0527  523 LEU A C   
3919 O O   . LEU A 537 ? 0.3915 0.3603 0.3132 -0.0224 -0.1071 0.0519  523 LEU A O   
3920 C CB  . LEU A 537 ? 0.3516 0.3237 0.2615 -0.0155 -0.0920 0.0517  523 LEU A CB  
3921 C CG  . LEU A 537 ? 0.3292 0.3185 0.2553 -0.0158 -0.0893 0.0498  523 LEU A CG  
3922 C CD1 . LEU A 537 ? 0.2954 0.2914 0.2162 -0.0104 -0.0824 0.0510  523 LEU A CD1 
3923 C CD2 . LEU A 537 ? 0.3061 0.2986 0.2460 -0.0200 -0.0930 0.0474  523 LEU A CD2 
3924 N N   . SER A 538 ? 0.3482 0.3315 0.2850 -0.0202 -0.0987 0.0529  524 SER A N   
3925 C CA  . SER A 538 ? 0.3584 0.3447 0.3088 -0.0226 -0.1019 0.0525  524 SER A CA  
3926 C C   . SER A 538 ? 0.3435 0.3394 0.3079 -0.0241 -0.0990 0.0482  524 SER A C   
3927 O O   . SER A 538 ? 0.3394 0.3413 0.3062 -0.0241 -0.0950 0.0459  524 SER A O   
3928 C CB  . SER A 538 ? 0.3411 0.3242 0.2930 -0.0207 -0.1016 0.0571  524 SER A CB  
3929 O OG  . SER A 538 ? 0.4113 0.3979 0.3704 -0.0210 -0.0957 0.0573  524 SER A OG  
3930 N N   . LEU A 539 ? 0.3267 0.3253 0.2999 -0.0251 -0.1011 0.0473  525 LEU A N   
3931 C CA  . LEU A 539 ? 0.3191 0.3252 0.3031 -0.0246 -0.0981 0.0432  525 LEU A CA  
3932 C C   . LEU A 539 ? 0.3255 0.3303 0.3202 -0.0240 -0.0986 0.0448  525 LEU A C   
3933 O O   . LEU A 539 ? 0.3484 0.3537 0.3465 -0.0235 -0.1022 0.0491  525 LEU A O   
3934 C CB  . LEU A 539 ? 0.3240 0.3354 0.3083 -0.0235 -0.0971 0.0424  525 LEU A CB  
3935 C CG  . LEU A 539 ? 0.3305 0.3508 0.3203 -0.0206 -0.0930 0.0377  525 LEU A CG  
3936 C CD1 . LEU A 539 ? 0.3278 0.3540 0.3129 -0.0174 -0.0897 0.0382  525 LEU A CD1 
3937 C CD2 . LEU A 539 ? 0.3123 0.3338 0.3131 -0.0188 -0.0925 0.0379  525 LEU A CD2 
3938 N N   . ILE A 540 ? 0.3092 0.3121 0.3095 -0.0240 -0.0949 0.0415  526 ILE A N   
3939 C CA  . ILE A 540 ? 0.3008 0.2988 0.3099 -0.0220 -0.0930 0.0434  526 ILE A CA  
3940 C C   . ILE A 540 ? 0.2986 0.2984 0.3132 -0.0202 -0.0893 0.0369  526 ILE A C   
3941 O O   . ILE A 540 ? 0.2630 0.2613 0.2776 -0.0225 -0.0868 0.0292  526 ILE A O   
3942 C CB  . ILE A 540 ? 0.2940 0.2832 0.3044 -0.0231 -0.0900 0.0453  526 ILE A CB  
3943 C CG1 . ILE A 540 ? 0.3321 0.3202 0.3332 -0.0232 -0.0928 0.0511  526 ILE A CG1 
3944 C CG2 . ILE A 540 ? 0.3121 0.2940 0.3301 -0.0192 -0.0867 0.0497  526 ILE A CG2 
3945 C CD1 . ILE A 540 ? 0.3060 0.2874 0.3088 -0.0240 -0.0881 0.0542  526 ILE A CD1 
3946 N N   . GLU A 541 ? 0.2961 0.2995 0.3157 -0.0159 -0.0890 0.0399  527 GLU A N   
3947 C CA  . GLU A 541 ? 0.2971 0.3007 0.3198 -0.0116 -0.0843 0.0348  527 GLU A CA  
3948 C C   . GLU A 541 ? 0.3254 0.3163 0.3525 -0.0094 -0.0796 0.0345  527 GLU A C   
3949 O O   . GLU A 541 ? 0.3218 0.3111 0.3544 -0.0053 -0.0787 0.0431  527 GLU A O   
3950 C CB  . GLU A 541 ? 0.3194 0.3328 0.3469 -0.0066 -0.0840 0.0403  527 GLU A CB  
3951 C CG  . GLU A 541 ? 0.3357 0.3484 0.3649 0.0008  -0.0778 0.0370  527 GLU A CG  
3952 C CD  . GLU A 541 ? 0.3663 0.3912 0.4024 0.0064  -0.0761 0.0445  527 GLU A CD  
3953 O OE1 . GLU A 541 ? 0.3514 0.3842 0.3943 0.0031  -0.0805 0.0527  527 GLU A OE1 
3954 O OE2 . GLU A 541 ? 0.3265 0.3528 0.3613 0.0141  -0.0702 0.0422  527 GLU A OE2 
3955 N N   . VAL A 542 ? 0.2945 0.2767 0.3195 -0.0123 -0.0766 0.0248  528 VAL A N   
3956 C CA  . VAL A 542 ? 0.3376 0.3029 0.3665 -0.0118 -0.0708 0.0233  528 VAL A CA  
3957 C C   . VAL A 542 ? 0.3506 0.3095 0.3779 -0.0052 -0.0655 0.0173  528 VAL A C   
3958 O O   . VAL A 542 ? 0.3423 0.3028 0.3635 -0.0062 -0.0660 0.0058  528 VAL A O   
3959 C CB  . VAL A 542 ? 0.3489 0.3070 0.3786 -0.0209 -0.0706 0.0157  528 VAL A CB  
3960 C CG1 . VAL A 542 ? 0.3577 0.2947 0.3930 -0.0212 -0.0630 0.0151  528 VAL A CG1 
3961 C CG2 . VAL A 542 ? 0.3040 0.2701 0.3332 -0.0253 -0.0749 0.0225  528 VAL A CG2 
3962 N N   . MET A 543 ? 0.3753 0.3278 0.4067 0.0031  -0.0602 0.0255  529 MET A N   
3963 C CA  . MET A 543 ? 0.4090 0.3547 0.4376 0.0122  -0.0536 0.0221  529 MET A CA  
3964 C C   . MET A 543 ? 0.4608 0.3811 0.4865 0.0110  -0.0464 0.0127  529 MET A C   
3965 O O   . MET A 543 ? 0.4534 0.3601 0.4845 0.0119  -0.0413 0.0195  529 MET A O   
3966 C CB  . MET A 543 ? 0.4017 0.3550 0.4371 0.0229  -0.0503 0.0367  529 MET A CB  
3967 C CG  . MET A 543 ? 0.3999 0.3771 0.4415 0.0220  -0.0578 0.0466  529 MET A CG  
3968 S SD  . MET A 543 ? 0.4506 0.4428 0.4873 0.0208  -0.0611 0.0404  529 MET A SD  
3969 C CE  . MET A 543 ? 0.4347 0.4217 0.4673 0.0342  -0.0511 0.0377  529 MET A CE  
3970 N N   . LEU A 544 ? 0.4777 0.3913 0.4946 0.0094  -0.0459 -0.0028 530 LEU A N   
3971 C CA  . LEU A 544 ? 0.5205 0.4088 0.5334 0.0054  -0.0407 -0.0162 530 LEU A CA  
3972 C C   . LEU A 544 ? 0.5595 0.4363 0.5604 0.0161  -0.0345 -0.0246 530 LEU A C   
3973 O O   . LEU A 544 ? 0.5470 0.4399 0.5420 0.0247  -0.0359 -0.0228 530 LEU A O   
3974 C CB  . LEU A 544 ? 0.4903 0.3825 0.5025 -0.0090 -0.0482 -0.0304 530 LEU A CB  
3975 C CG  . LEU A 544 ? 0.4748 0.3745 0.4980 -0.0195 -0.0524 -0.0233 530 LEU A CG  
3976 C CD1 . LEU A 544 ? 0.4433 0.3574 0.4658 -0.0307 -0.0608 -0.0346 530 LEU A CD1 
3977 C CD2 . LEU A 544 ? 0.4822 0.3582 0.5140 -0.0233 -0.0446 -0.0197 530 LEU A CD2 
3978 N N   . PRO A 545 ? 0.6129 0.4600 0.6092 0.0167  -0.0264 -0.0335 531 PRO A N   
3979 C CA  . PRO A 545 ? 0.6443 0.4765 0.6256 0.0286  -0.0193 -0.0423 531 PRO A CA  
3980 C C   . PRO A 545 ? 0.7223 0.5639 0.6895 0.0259  -0.0268 -0.0604 531 PRO A C   
3981 O O   . PRO A 545 ? 0.7115 0.5608 0.6803 0.0118  -0.0360 -0.0717 531 PRO A O   
3982 C CB  . PRO A 545 ? 0.6765 0.4708 0.6562 0.0264  -0.0095 -0.0496 531 PRO A CB  
3983 C CG  . PRO A 545 ? 0.6347 0.4280 0.6318 0.0192  -0.0083 -0.0356 531 PRO A CG  
3984 C CD  . PRO A 545 ? 0.6071 0.4306 0.6117 0.0081  -0.0214 -0.0339 531 PRO A CD  
3985 N N   . LYS A 546 ? 0.7497 0.5921 0.7027 0.0411  -0.0221 -0.0621 532 LYS A N   
3986 C CA  . LYS A 546 ? 0.7636 0.6195 0.7011 0.0429  -0.0286 -0.0763 532 LYS A CA  
3987 C C   . LYS A 546 ? 0.8119 0.6491 0.7376 0.0320  -0.0330 -0.1016 532 LYS A C   
3988 O O   . LYS A 546 ? 0.8009 0.6561 0.7220 0.0240  -0.0437 -0.1135 532 LYS A O   
3989 C CB  . LYS A 546 ? 0.8086 0.6671 0.7327 0.0637  -0.0203 -0.0714 532 LYS A CB  
3990 C CG  . LYS A 546 ? 0.8360 0.7205 0.7487 0.0689  -0.0265 -0.0761 532 LYS A CG  
3991 C CD  . LYS A 546 ? 0.8453 0.7456 0.7570 0.0880  -0.0184 -0.0594 532 LYS A CD  
3992 C CE  . LYS A 546 ? 0.8492 0.7705 0.7849 0.0850  -0.0195 -0.0368 532 LYS A CE  
3993 N NZ  . LYS A 546 ? 0.8994 0.8363 0.8402 0.1013  -0.0112 -0.0185 532 LYS A NZ  
3994 N N   . ALA A 547 ? 0.8574 0.6588 0.7778 0.0317  -0.0249 -0.1104 533 ALA A N   
3995 C CA  . ALA A 547 ? 0.9020 0.6819 0.8108 0.0206  -0.0289 -0.1365 533 ALA A CA  
3996 C C   . ALA A 547 ? 0.9406 0.7086 0.8679 -0.0008 -0.0321 -0.1408 533 ALA A C   
3997 O O   . ALA A 547 ? 0.9948 0.7362 0.9171 -0.0115 -0.0322 -0.1606 533 ALA A O   
3998 C CB  . ALA A 547 ? 0.8858 0.6289 0.7738 0.0336  -0.0171 -0.1468 533 ALA A CB  
3999 N N   . ASP A 548 ? 0.9296 0.7157 0.8779 -0.0072 -0.0342 -0.1229 534 ASP A N   
4000 C CA  . ASP A 548 ? 0.9604 0.7354 0.9275 -0.0250 -0.0347 -0.1230 534 ASP A CA  
4001 C C   . ASP A 548 ? 1.0488 0.8488 1.0229 -0.0421 -0.0490 -0.1342 534 ASP A C   
4002 O O   . ASP A 548 ? 1.0255 0.8596 1.0016 -0.0402 -0.0570 -0.1261 534 ASP A O   
4003 C CB  . ASP A 548 ? 0.8578 0.6381 0.8418 -0.0213 -0.0288 -0.0976 534 ASP A CB  
4004 C CG  . ASP A 548 ? 0.8472 0.6028 0.8466 -0.0330 -0.0221 -0.0953 534 ASP A CG  
4005 O OD1 . ASP A 548 ? 0.9545 0.6872 0.9534 -0.0452 -0.0217 -0.1138 534 ASP A OD1 
4006 O OD2 . ASP A 548 ? 0.7538 0.5125 0.7658 -0.0298 -0.0171 -0.0753 534 ASP A OD2 
4007 N N   . ILE A 549 ? 1.0360 0.8189 1.0149 -0.0589 -0.0517 -0.1522 535 ILE A N   
4008 C CA  . ILE A 549 ? 1.0579 0.8648 1.0449 -0.0763 -0.0654 -0.1648 535 ILE A CA  
4009 C C   . ILE A 549 ? 1.0943 0.8893 1.1063 -0.0951 -0.0631 -0.1624 535 ILE A C   
4010 O O   . ILE A 549 ? 1.0627 0.8207 1.0794 -0.0973 -0.0515 -0.1622 535 ILE A O   
4011 C CB  . ILE A 549 ? 1.1176 0.9214 1.0861 -0.0798 -0.0738 -0.1927 535 ILE A CB  
4012 C CG1 . ILE A 549 ? 1.0803 0.8377 1.0445 -0.0872 -0.0664 -0.2101 535 ILE A CG1 
4013 C CG2 . ILE A 549 ? 1.0708 0.8884 1.0141 -0.0589 -0.0747 -0.1928 535 ILE A CG2 
4014 C CD1 . ILE A 549 ? 1.0506 0.8034 0.9971 -0.0946 -0.0767 -0.2409 535 ILE A CD1 
4015 N N   . PRO A 550 ? 1.0955 0.9204 1.1243 -0.1075 -0.0720 -0.1584 536 PRO A N   
4016 C CA  . PRO A 550 ? 1.0270 0.8433 1.0817 -0.1247 -0.0685 -0.1535 536 PRO A CA  
4017 C C   . PRO A 550 ? 1.0810 0.8752 1.1417 -0.1435 -0.0707 -0.1773 536 PRO A C   
4018 O O   . PRO A 550 ? 1.1132 0.9059 1.1567 -0.1444 -0.0785 -0.1996 536 PRO A O   
4019 C CB  . PRO A 550 ? 0.9233 0.7825 0.9904 -0.1303 -0.0785 -0.1442 536 PRO A CB  
4020 C CG  . PRO A 550 ? 0.8750 0.7605 0.9234 -0.1138 -0.0842 -0.1393 536 PRO A CG  
4021 C CD  . PRO A 550 ? 0.9579 0.8257 0.9829 -0.1027 -0.0828 -0.1530 536 PRO A CD  
4022 N N   . PRO A 551 ? 1.0738 0.8499 1.1584 -0.1589 -0.0638 -0.1737 537 PRO A N   
4023 C CA  . PRO A 551 ? 1.1017 0.8543 1.1953 -0.1797 -0.0657 -0.1972 537 PRO A CA  
4024 C C   . PRO A 551 ? 1.1113 0.8962 1.2013 -0.1923 -0.0843 -0.2162 537 PRO A C   
4025 O O   . PRO A 551 ? 1.1385 0.9087 1.2085 -0.1945 -0.0895 -0.2358 537 PRO A O   
4026 C CB  . PRO A 551 ? 1.0031 0.7449 1.1284 -0.1934 -0.0558 -0.1825 537 PRO A CB  
4027 C CG  . PRO A 551 ? 0.9547 0.6886 1.0766 -0.1736 -0.0422 -0.1550 537 PRO A CG  
4028 C CD  . PRO A 551 ? 1.0243 0.7898 1.1248 -0.1546 -0.0504 -0.1482 537 PRO A CD  
4029 N N   . LEU A 552 ? 1.0742 0.9039 1.1788 -0.1973 -0.0939 -0.2067 538 LEU A N   
4030 C CA  . LEU A 552 ? 1.1272 0.9910 1.2283 -0.2072 -0.1102 -0.2175 538 LEU A CA  
4031 C C   . LEU A 552 ? 1.1315 1.0063 1.2009 -0.1943 -0.1199 -0.2335 538 LEU A C   
4032 O O   . LEU A 552 ? 1.1153 0.9954 1.1727 -0.2012 -0.1304 -0.2492 538 LEU A O   
4033 C CB  . LEU A 552 ? 1.1174 1.0269 1.2396 -0.2112 -0.1160 -0.2010 538 LEU A CB  
4034 C CG  . LEU A 552 ? 0.9135 0.8679 1.0305 -0.2138 -0.1328 -0.2066 538 LEU A CG  
4035 C CD1 . LEU A 552 ? 0.7260 0.6849 0.8592 -0.2345 -0.1401 -0.2130 538 LEU A CD1 
4036 C CD2 . LEU A 552 ? 0.8003 0.7940 0.9289 -0.2071 -0.1343 -0.1879 538 LEU A CD2 
4037 N N   . LEU A 553 ? 1.1271 1.0050 1.1829 -0.1749 -0.1165 -0.2293 539 LEU A N   
4038 C CA  . LEU A 553 ? 1.1770 1.0655 1.2020 -0.1601 -0.1238 -0.2425 539 LEU A CA  
4039 C C   . LEU A 553 ? 1.2287 1.0782 1.2319 -0.1607 -0.1213 -0.2630 539 LEU A C   
4040 O O   . LEU A 553 ? 1.2542 1.1146 1.2356 -0.1590 -0.1312 -0.2777 539 LEU A O   
4041 C CB  . LEU A 553 ? 1.1321 1.0260 1.1427 -0.1358 -0.1166 -0.2240 539 LEU A CB  
4042 C CG  . LEU A 553 ? 1.1851 1.1070 1.1700 -0.1200 -0.1252 -0.2306 539 LEU A CG  
4043 C CD1 . LEU A 553 ? 1.1513 1.1176 1.1427 -0.1298 -0.1407 -0.2376 539 LEU A CD1 
4044 C CD2 . LEU A 553 ? 1.1204 1.0519 1.0960 -0.0980 -0.1173 -0.2071 539 LEU A CD2 
4045 N N   . GLY A 554 ? 1.2191 1.0220 1.2274 -0.1630 -0.1076 -0.2632 540 GLY A N   
4046 C CA  . GLY A 554 ? 1.2426 1.0036 1.2287 -0.1630 -0.1036 -0.2818 540 GLY A CA  
4047 C C   . GLY A 554 ? 1.2808 1.0473 1.2624 -0.1805 -0.1167 -0.2974 540 GLY A C   
4048 O O   . GLY A 554 ? 1.3086 1.0584 1.2620 -0.1771 -0.1207 -0.3164 540 GLY A O   
4049 N N   . ALA A 555 ? 1.2525 1.0421 1.2619 -0.1991 -0.1234 -0.2894 541 ALA A N   
4050 C CA  . ALA A 555 ? 1.2189 1.0210 1.2282 -0.2160 -0.1382 -0.3031 541 ALA A CA  
4051 C C   . ALA A 555 ? 1.2247 1.0743 1.2188 -0.2084 -0.1535 -0.3075 541 ALA A C   
4052 O O   . ALA A 555 ? 1.1973 1.0499 1.1751 -0.2140 -0.1653 -0.3247 541 ALA A O   
4053 C CB  . ALA A 555 ? 1.0637 0.8759 1.1101 -0.2374 -0.1396 -0.2919 541 ALA A CB  
4054 N N   . ILE A 556 ? 1.2243 1.1107 1.2234 -0.1957 -0.1535 -0.2915 542 ILE A N   
4055 C CA  . ILE A 556 ? 1.2519 1.1835 1.2368 -0.1855 -0.1657 -0.2921 542 ILE A CA  
4056 C C   . ILE A 556 ? 1.3133 1.2371 1.2609 -0.1643 -0.1642 -0.3032 542 ILE A C   
4057 O O   . ILE A 556 ? 1.3117 1.2656 1.2422 -0.1564 -0.1741 -0.3079 542 ILE A O   
4058 C CB  . ILE A 556 ? 1.2262 1.2005 1.2312 -0.1807 -0.1666 -0.2698 542 ILE A CB  
4059 C CG1 . ILE A 556 ? 1.0959 1.0667 1.1367 -0.1980 -0.1620 -0.2566 542 ILE A CG1 
4060 C CG2 . ILE A 556 ? 1.0449 1.0660 1.0459 -0.1788 -0.1807 -0.2695 542 ILE A CG2 
4061 C CD1 . ILE A 556 ? 0.8149 0.8330 0.8778 -0.2009 -0.1684 -0.2395 542 ILE A CD1 
4062 N N   . THR A 557 ? 1.3246 1.2099 1.2594 -0.1531 -0.1513 -0.3063 543 THR A N   
4063 C CA  . THR A 557 ? 1.3463 1.2242 1.2461 -0.1314 -0.1488 -0.3160 543 THR A CA  
4064 C C   . THR A 557 ? 1.4095 1.2600 1.2820 -0.1351 -0.1524 -0.3394 543 THR A C   
4065 O O   . THR A 557 ? 1.4441 1.2929 1.2851 -0.1167 -0.1513 -0.3480 543 THR A O   
4066 C CB  . THR A 557 ? 1.3121 1.1586 1.2077 -0.1152 -0.1335 -0.3105 543 THR A CB  
4067 O OG1 . THR A 557 ? 1.3215 1.1153 1.2169 -0.1239 -0.1237 -0.3201 543 THR A OG1 
4068 C CG2 . THR A 557 ? 1.2632 1.1279 1.1849 -0.1123 -0.1294 -0.2890 543 THR A CG2 
4069 N N   . LYS A 558 ? 1.4001 1.2312 1.2833 -0.1578 -0.1574 -0.3493 544 LYS A N   
4070 C CA  . LYS A 558 ? 1.4202 1.2220 1.2768 -0.1635 -0.1622 -0.3727 544 LYS A CA  
4071 C C   . LYS A 558 ? 1.4631 1.2964 1.3205 -0.1781 -0.1813 -0.3823 544 LYS A C   
4072 O O   . LYS A 558 ? 1.4538 1.2729 1.2830 -0.1789 -0.1880 -0.4024 544 LYS A O   
4073 C CB  . LYS A 558 ? 1.3943 1.1392 1.2577 -0.1768 -0.1526 -0.3793 544 LYS A CB  
4074 C CG  . LYS A 558 ? 1.3955 1.1069 1.2620 -0.1627 -0.1327 -0.3680 544 LYS A CG  
4075 C CD  . LYS A 558 ? 1.4147 1.1261 1.2513 -0.1343 -0.1247 -0.3688 544 LYS A CD  
4076 C CE  . LYS A 558 ? 1.4098 1.0623 1.2278 -0.1224 -0.1069 -0.3746 544 LYS A CE  
4077 N NZ  . LYS A 558 ? 1.2933 0.9048 1.0855 -0.1311 -0.1090 -0.3966 544 LYS A NZ  
4078 N N   . ALA A 559 ? 1.4358 1.3105 1.3245 -0.1891 -0.1899 -0.3685 545 ALA A N   
4079 C CA  . ALA A 559 ? 1.4107 1.3242 1.3038 -0.1995 -0.2080 -0.3738 545 ALA A CA  
4080 C C   . ALA A 559 ? 1.4162 1.3816 1.3024 -0.1802 -0.2122 -0.3615 545 ALA A C   
4081 O O   . ALA A 559 ? 1.2964 1.3036 1.1977 -0.1865 -0.2243 -0.3561 545 ALA A O   
4082 C CB  . ALA A 559 ? 1.1061 1.0299 1.0395 -0.2245 -0.2144 -0.3669 545 ALA A CB  
4083 N N   . LEU A 560 ? 1.5263 1.4891 1.3934 -0.1558 -0.2006 -0.3543 546 LEU A N   
4084 C CA  . LEU A 560 ? 1.4863 1.4861 1.3333 -0.1327 -0.2027 -0.3484 546 LEU A CA  
4085 C C   . LEU A 560 ? 1.5436 1.5307 1.3494 -0.1161 -0.2023 -0.3648 546 LEU A C   
4086 O O   . LEU A 560 ? 1.5363 1.5575 1.3307 -0.1090 -0.2118 -0.3666 546 LEU A O   
4087 C CB  . LEU A 560 ? 1.3367 1.3585 1.1942 -0.1151 -0.1929 -0.3244 546 LEU A CB  
4088 C CG  . LEU A 560 ? 1.1784 1.2391 1.0678 -0.1229 -0.1975 -0.3050 546 LEU A CG  
4089 C CD1 . LEU A 560 ? 0.8691 0.9722 0.7718 -0.1099 -0.1951 -0.2801 546 LEU A CD1 
4090 C CD2 . LEU A 560 ? 1.2894 1.3784 1.1514 -0.1083 -0.2059 -0.3127 546 LEU A CD2 
4091 N N   . GLU A 561 ? 1.5913 1.5344 1.3732 -0.1078 -0.1918 -0.3765 547 GLU A N   
4092 C CA  . GLU A 561 ? 1.6181 1.5622 1.3644 -0.0993 -0.1985 -0.3945 547 GLU A CA  
4093 C C   . GLU A 561 ? 1.6122 1.5290 1.3527 -0.1223 -0.2083 -0.4168 547 GLU A C   
4094 O O   . GLU A 561 ? 1.6130 1.4996 1.3202 -0.1173 -0.2066 -0.4358 547 GLU A O   
4095 C CB  . GLU A 561 ? 1.6154 1.5388 1.3231 -0.0726 -0.1871 -0.4012 547 GLU A CB  
4096 C CG  . GLU A 561 ? 1.5458 1.4805 1.2376 -0.0393 -0.1741 -0.3866 547 GLU A CG  
4097 C CD  . GLU A 561 ? 1.5920 1.4808 1.2828 -0.0319 -0.1569 -0.3844 547 GLU A CD  
4098 O OE1 . GLU A 561 ? 1.6236 1.4740 1.2994 -0.0182 -0.1423 -0.3869 547 GLU A OE1 
4099 O OE2 . GLU A 561 ? 1.5182 1.4188 1.1786 -0.0092 -0.1553 -0.3872 547 GLU A OE2 
4100 N N   . ALA A 562 ? 1.5793 1.5030 1.3513 -0.1471 -0.2175 -0.4149 548 ALA A N   
4101 C CA  . ALA A 562 ? 1.5948 1.5017 1.3574 -0.1667 -0.2305 -0.4373 548 ALA A CA  
4102 C C   . ALA A 562 ? 1.6065 1.5560 1.3530 -0.1607 -0.2459 -0.4439 548 ALA A C   
4103 O O   . ALA A 562 ? 1.6080 1.5470 1.3384 -0.1731 -0.2583 -0.4652 548 ALA A O   
4104 C CB  . ALA A 562 ? 1.5156 1.4157 1.3162 -0.1955 -0.2369 -0.4353 548 ALA A CB  
4105 N N   . ARG A 563 ? 1.5923 1.5889 1.3429 -0.1409 -0.2446 -0.4254 549 ARG A N   
4106 C CA  . ARG A 563 ? 1.4559 1.5011 1.1966 -0.1299 -0.2560 -0.4242 549 ARG A CA  
4107 C C   . ARG A 563 ? 1.3994 1.4585 1.1116 -0.0974 -0.2463 -0.4172 549 ARG A C   
4108 O O   . ARG A 563 ? 1.3347 1.4152 1.0233 -0.0866 -0.2542 -0.4258 549 ARG A O   
4109 C CB  . ARG A 563 ? 1.2428 1.3339 1.0215 -0.1373 -0.2624 -0.4045 549 ARG A CB  
4110 C CG  . ARG A 563 ? 1.2321 1.3215 1.0348 -0.1321 -0.2480 -0.3816 549 ARG A CG  
4111 C CD  . ARG A 563 ? 1.0828 1.2131 0.9209 -0.1405 -0.2539 -0.3638 549 ARG A CD  
4112 N NE  . ARG A 563 ? 0.8659 1.0441 0.6957 -0.1228 -0.2588 -0.3555 549 ARG A NE  
4113 C CZ  . ARG A 563 ? 0.8069 1.0123 0.6426 -0.1039 -0.2498 -0.3333 549 ARG A CZ  
4114 N NH1 . ARG A 563 ? 0.7637 0.9562 0.6141 -0.1011 -0.2370 -0.3173 549 ARG A NH1 
4115 N NH2 . ARG A 563 ? 0.8030 1.0488 0.6291 -0.0873 -0.2534 -0.3272 549 ARG A NH2 
4116 N N   . ASN A 564 ? 1.4089 1.4576 1.1235 -0.0811 -0.2297 -0.4013 550 ASN A N   
4117 C CA  . ASN A 564 ? 1.3416 1.4057 1.0335 -0.0496 -0.2200 -0.3916 550 ASN A CA  
4118 C C   . ASN A 564 ? 1.3815 1.4115 1.0333 -0.0364 -0.2143 -0.4098 550 ASN A C   
4119 O O   . ASN A 564 ? 1.2931 1.3425 0.9206 -0.0133 -0.2129 -0.4087 550 ASN A O   
4124 N N   . SER A 565 ? 1.4538 1.4329 1.0975 -0.0490 -0.2097 -0.4257 551 SER A N   
4125 C CA  . SER A 565 ? 1.4853 1.4288 1.0887 -0.0391 -0.2049 -0.4460 551 SER A CA  
4126 C C   . SER A 565 ? 1.4356 1.3950 1.0101 -0.0366 -0.2181 -0.4638 551 SER A C   
4127 O O   . SER A 565 ? 1.4600 1.4347 1.0430 -0.0574 -0.2353 -0.4740 551 SER A O   
4130 N N   . THR B 17  ? 0.8458 0.7959 0.8268 0.0830  0.0468  -0.0293 3   THR B N   
4131 C CA  . THR B 17  ? 0.7572 0.7167 0.7406 0.0774  0.0452  -0.0274 3   THR B CA  
4132 C C   . THR B 17  ? 0.6657 0.6239 0.6393 0.0773  0.0488  -0.0299 3   THR B C   
4133 O O   . THR B 17  ? 0.6377 0.6055 0.6160 0.0783  0.0526  -0.0278 3   THR B O   
4134 C CB  . THR B 17  ? 0.8380 0.8119 0.8365 0.0780  0.0462  -0.0222 3   THR B CB  
4135 O OG1 . THR B 17  ? 0.9682 0.9459 0.9722 0.0849  0.0524  -0.0212 3   THR B OG1 
4136 C CG2 . THR B 17  ? 0.8067 0.7822 0.8134 0.0758  0.0408  -0.0194 3   THR B CG2 
4137 N N   . PRO B 18  ? 0.6336 0.5800 0.5934 0.0756  0.0473  -0.0342 4   PRO B N   
4138 C CA  . PRO B 18  ? 0.5886 0.5328 0.5377 0.0750  0.0499  -0.0366 4   PRO B CA  
4139 C C   . PRO B 18  ? 0.5008 0.4551 0.4536 0.0696  0.0480  -0.0340 4   PRO B C   
4140 O O   . PRO B 18  ? 0.4940 0.4525 0.4526 0.0648  0.0430  -0.0319 4   PRO B O   
4141 C CB  . PRO B 18  ? 0.5812 0.5103 0.5158 0.0728  0.0465  -0.0411 4   PRO B CB  
4142 C CG  . PRO B 18  ? 0.6180 0.5437 0.5570 0.0703  0.0410  -0.0404 4   PRO B CG  
4143 C CD  . PRO B 18  ? 0.6204 0.5562 0.5746 0.0725  0.0417  -0.0362 4   PRO B CD  
4144 N N   . TYR B 19  ? 0.4467 0.4045 0.3957 0.0707  0.0522  -0.0340 5   TYR B N   
4145 C CA  . TYR B 19  ? 0.4032 0.3704 0.3556 0.0662  0.0510  -0.0314 5   TYR B CA  
4146 C C   . TYR B 19  ? 0.3718 0.3345 0.3177 0.0598  0.0448  -0.0328 5   TYR B C   
4147 O O   . TYR B 19  ? 0.3876 0.3396 0.3214 0.0589  0.0431  -0.0364 5   TYR B O   
4148 C CB  . TYR B 19  ? 0.3595 0.3290 0.3064 0.0687  0.0568  -0.0316 5   TYR B CB  
4149 C CG  . TYR B 19  ? 0.3542 0.3344 0.3062 0.0652  0.0567  -0.0282 5   TYR B CG  
4150 C CD1 . TYR B 19  ? 0.3306 0.3088 0.2750 0.0602  0.0532  -0.0290 5   TYR B CD1 
4151 C CD2 . TYR B 19  ? 0.3406 0.3326 0.3050 0.0670  0.0600  -0.0240 5   TYR B CD2 
4152 C CE1 . TYR B 19  ? 0.3269 0.3140 0.2755 0.0573  0.0531  -0.0259 5   TYR B CE1 
4153 C CE2 . TYR B 19  ? 0.3169 0.3176 0.2854 0.0637  0.0598  -0.0209 5   TYR B CE2 
4154 C CZ  . TYR B 19  ? 0.3208 0.3187 0.2811 0.0590  0.0565  -0.0219 5   TYR B CZ  
4155 O OH  . TYR B 19  ? 0.3358 0.3418 0.3001 0.0560  0.0562  -0.0187 5   TYR B OH  
4156 N N   . CYS B 20  ? 0.3443 0.3151 0.2985 0.0555  0.0412  -0.0297 6   CYS B N   
4157 C CA  . CYS B 20  ? 0.3307 0.2988 0.2815 0.0497  0.0354  -0.0303 6   CYS B CA  
4158 C C   . CYS B 20  ? 0.3090 0.2867 0.2651 0.0461  0.0343  -0.0273 6   CYS B C   
4159 O O   . CYS B 20  ? 0.3054 0.2911 0.2672 0.0478  0.0377  -0.0249 6   CYS B O   
4160 C CB  . CYS B 20  ? 0.3309 0.2960 0.2861 0.0482  0.0314  -0.0301 6   CYS B CB  
4161 S SG  . CYS B 20  ? 0.3786 0.3544 0.3490 0.0486  0.0311  -0.0257 6   CYS B SG  
4162 N N   . VAL B 21  ? 0.2845 0.2613 0.2390 0.0411  0.0295  -0.0272 7   VAL B N   
4163 C CA  . VAL B 21  ? 0.2740 0.2585 0.2326 0.0377  0.0280  -0.0247 7   VAL B CA  
4164 C C   . VAL B 21  ? 0.2627 0.2562 0.2329 0.0383  0.0290  -0.0213 7   VAL B C   
4165 O O   . VAL B 21  ? 0.2308 0.2312 0.2046 0.0377  0.0304  -0.0190 7   VAL B O   
4166 C CB  . VAL B 21  ? 0.2520 0.2341 0.2087 0.0329  0.0228  -0.0249 7   VAL B CB  
4167 C CG1 . VAL B 21  ? 0.2410 0.2313 0.2040 0.0300  0.0214  -0.0220 7   VAL B CG1 
4168 C CG2 . VAL B 21  ? 0.2682 0.2429 0.2137 0.0314  0.0212  -0.0276 7   VAL B CG2 
4169 N N   . ALA B 22  ? 0.2496 0.2429 0.2257 0.0390  0.0278  -0.0207 8   ALA B N   
4170 C CA  . ALA B 22  ? 0.2599 0.2610 0.2464 0.0394  0.0282  -0.0174 8   ALA B CA  
4171 C C   . ALA B 22  ? 0.2709 0.2777 0.2610 0.0427  0.0328  -0.0158 8   ALA B C   
4172 O O   . ALA B 22  ? 0.2440 0.2583 0.2403 0.0415  0.0332  -0.0129 8   ALA B O   
4173 C CB  . ALA B 22  ? 0.2590 0.2579 0.2500 0.0403  0.0265  -0.0171 8   ALA B CB  
4174 N N   . ASP B 23  ? 0.3033 0.3066 0.2895 0.0468  0.0366  -0.0176 9   ASP B N   
4175 C CA  . ASP B 23  ? 0.3041 0.3132 0.2940 0.0504  0.0418  -0.0158 9   ASP B CA  
4176 C C   . ASP B 23  ? 0.2867 0.2989 0.2724 0.0487  0.0434  -0.0152 9   ASP B C   
4177 O O   . ASP B 23  ? 0.2684 0.2886 0.2605 0.0490  0.0459  -0.0121 9   ASP B O   
4178 C CB  . ASP B 23  ? 0.3371 0.3407 0.3227 0.0557  0.0459  -0.0182 9   ASP B CB  
4179 C CG  . ASP B 23  ? 0.3523 0.3524 0.3422 0.0577  0.0442  -0.0186 9   ASP B CG  
4180 O OD1 . ASP B 23  ? 0.3466 0.3533 0.3474 0.0576  0.0430  -0.0154 9   ASP B OD1 
4181 O OD2 . ASP B 23  ? 0.3639 0.3542 0.3459 0.0591  0.0438  -0.0220 9   ASP B OD2 
4182 N N   . TYR B 24  ? 0.2771 0.2829 0.2521 0.0466  0.0419  -0.0179 10  TYR B N   
4183 C CA  . TYR B 24  ? 0.2820 0.2901 0.2524 0.0448  0.0428  -0.0171 10  TYR B CA  
4184 C C   . TYR B 24  ? 0.2718 0.2875 0.2501 0.0412  0.0402  -0.0137 10  TYR B C   
4185 O O   . TYR B 24  ? 0.2570 0.2785 0.2375 0.0409  0.0425  -0.0111 10  TYR B O   
4186 C CB  . TYR B 24  ? 0.2684 0.2681 0.2267 0.0426  0.0401  -0.0203 10  TYR B CB  
4187 C CG  . TYR B 24  ? 0.2842 0.2847 0.2356 0.0412  0.0411  -0.0197 10  TYR B CG  
4188 C CD1 . TYR B 24  ? 0.2825 0.2871 0.2363 0.0372  0.0378  -0.0176 10  TYR B CD1 
4189 C CD2 . TYR B 24  ? 0.2981 0.2947 0.2402 0.0441  0.0455  -0.0213 10  TYR B CD2 
4190 C CE1 . TYR B 24  ? 0.3155 0.3206 0.2630 0.0359  0.0383  -0.0168 10  TYR B CE1 
4191 C CE2 . TYR B 24  ? 0.3175 0.3144 0.2524 0.0426  0.0462  -0.0207 10  TYR B CE2 
4192 C CZ  . TYR B 24  ? 0.3035 0.3048 0.2415 0.0384  0.0424  -0.0183 10  TYR B CZ  
4193 O OH  . TYR B 24  ? 0.3060 0.3076 0.2374 0.0368  0.0426  -0.0172 10  TYR B OH  
4194 N N   . LEU B 25  ? 0.2640 0.2794 0.2462 0.0384  0.0357  -0.0135 11  LEU B N   
4195 C CA  . LEU B 25  ? 0.2605 0.2819 0.2495 0.0353  0.0334  -0.0105 11  LEU B CA  
4196 C C   . LEU B 25  ? 0.2582 0.2869 0.2567 0.0366  0.0356  -0.0072 11  LEU B C   
4197 O O   . LEU B 25  ? 0.2516 0.2856 0.2536 0.0350  0.0358  -0.0046 11  LEU B O   
4198 C CB  . LEU B 25  ? 0.2454 0.2644 0.2363 0.0327  0.0289  -0.0111 11  LEU B CB  
4199 C CG  . LEU B 25  ? 0.2163 0.2395 0.2132 0.0298  0.0262  -0.0087 11  LEU B CG  
4200 C CD1 . LEU B 25  ? 0.2099 0.2356 0.2048 0.0278  0.0261  -0.0074 11  LEU B CD1 
4201 C CD2 . LEU B 25  ? 0.2303 0.2499 0.2269 0.0277  0.0225  -0.0098 11  LEU B CD2 
4202 N N   . LEU B 26  ? 0.2392 0.2683 0.2423 0.0395  0.0370  -0.0072 12  LEU B N   
4203 C CA  . LEU B 26  ? 0.2638 0.3006 0.2772 0.0406  0.0387  -0.0036 12  LEU B CA  
4204 C C   . LEU B 26  ? 0.2849 0.3265 0.2986 0.0426  0.0437  -0.0019 12  LEU B C   
4205 O O   . LEU B 26  ? 0.2668 0.3154 0.2875 0.0413  0.0442  0.0018  12  LEU B O   
4206 C CB  . LEU B 26  ? 0.2670 0.3032 0.2856 0.0435  0.0388  -0.0037 12  LEU B CB  
4207 C CG  . LEU B 26  ? 0.2453 0.2779 0.2649 0.0410  0.0336  -0.0044 12  LEU B CG  
4208 C CD1 . LEU B 26  ? 0.2784 0.3086 0.3012 0.0439  0.0333  -0.0048 12  LEU B CD1 
4209 C CD2 . LEU B 26  ? 0.2532 0.2903 0.2786 0.0372  0.0302  -0.0015 12  LEU B CD2 
4210 N N   . ASP B 27  ? 0.2870 0.3243 0.2924 0.0455  0.0474  -0.0044 13  ASP B N   
4211 C CA  . ASP B 27  ? 0.2972 0.3384 0.3010 0.0473  0.0527  -0.0029 13  ASP B CA  
4212 C C   . ASP B 27  ? 0.2847 0.3286 0.2867 0.0434  0.0513  -0.0010 13  ASP B C   
4213 O O   . ASP B 27  ? 0.2749 0.3258 0.2823 0.0431  0.0538  0.0027  13  ASP B O   
4214 C CB  . ASP B 27  ? 0.3009 0.3345 0.2929 0.0507  0.0563  -0.0067 13  ASP B CB  
4215 C CG  . ASP B 27  ? 0.3630 0.3961 0.3580 0.0561  0.0605  -0.0074 13  ASP B CG  
4216 O OD1 . ASP B 27  ? 0.4033 0.4444 0.4100 0.0578  0.0625  -0.0039 13  ASP B OD1 
4217 O OD2 . ASP B 27  ? 0.3911 0.4155 0.3767 0.0588  0.0617  -0.0114 13  ASP B OD2 
4218 N N   . ARG B 28  ? 0.2693 0.3080 0.2646 0.0403  0.0471  -0.0029 14  ARG B N   
4219 C CA  . ARG B 28  ? 0.2660 0.3065 0.2593 0.0369  0.0456  -0.0012 14  ARG B CA  
4220 C C   . ARG B 28  ? 0.2846 0.3310 0.2879 0.0341  0.0429  0.0023  14  ARG B C   
4221 O O   . ARG B 28  ? 0.2800 0.3302 0.2847 0.0322  0.0434  0.0052  14  ARG B O   
4222 C CB  . ARG B 28  ? 0.2822 0.3161 0.2668 0.0345  0.0416  -0.0040 14  ARG B CB  
4223 C CG  . ARG B 28  ? 0.2736 0.3004 0.2463 0.0362  0.0431  -0.0073 14  ARG B CG  
4224 C CD  . ARG B 28  ? 0.3049 0.3334 0.2734 0.0387  0.0488  -0.0064 14  ARG B CD  
4225 N NE  . ARG B 28  ? 0.2908 0.3137 0.2469 0.0377  0.0484  -0.0081 14  ARG B NE  
4226 C CZ  . ARG B 28  ? 0.3274 0.3492 0.2756 0.0396  0.0529  -0.0081 14  ARG B CZ  
4227 N NH1 . ARG B 28  ? 0.3186 0.3447 0.2704 0.0431  0.0589  -0.0066 14  ARG B NH1 
4228 N NH2 . ARG B 28  ? 0.3149 0.3311 0.2513 0.0379  0.0513  -0.0094 14  ARG B NH2 
4229 N N   . LEU B 29  ? 0.2579 0.3042 0.2671 0.0335  0.0399  0.0021  15  LEU B N   
4230 C CA  . LEU B 29  ? 0.2856 0.3363 0.3034 0.0309  0.0371  0.0052  15  LEU B CA  
4231 C C   . LEU B 29  ? 0.2876 0.3458 0.3135 0.0316  0.0401  0.0092  15  LEU B C   
4232 O O   . LEU B 29  ? 0.2602 0.3220 0.2897 0.0289  0.0392  0.0122  15  LEU B O   
4233 C CB  . LEU B 29  ? 0.2899 0.3384 0.3114 0.0307  0.0338  0.0041  15  LEU B CB  
4234 C CG  . LEU B 29  ? 0.2933 0.3433 0.3208 0.0277  0.0298  0.0061  15  LEU B CG  
4235 C CD1 . LEU B 29  ? 0.2769 0.3265 0.3022 0.0245  0.0279  0.0071  15  LEU B CD1 
4236 C CD2 . LEU B 29  ? 0.2747 0.3201 0.3014 0.0277  0.0268  0.0039  15  LEU B CD2 
4237 N N   . THR B 30  ? 0.2901 0.3509 0.3196 0.0351  0.0437  0.0094  16  THR B N   
4238 C CA  . THR B 30  ? 0.3046 0.3737 0.3429 0.0361  0.0471  0.0136  16  THR B CA  
4239 C C   . THR B 30  ? 0.3038 0.3753 0.3381 0.0357  0.0509  0.0153  16  THR B C   
4240 O O   . THR B 30  ? 0.3221 0.4003 0.3634 0.0342  0.0519  0.0196  16  THR B O   
4241 C CB  . THR B 30  ? 0.3062 0.3775 0.3492 0.0406  0.0506  0.0135  16  THR B CB  
4242 O OG1 . THR B 30  ? 0.3402 0.4070 0.3740 0.0443  0.0550  0.0103  16  THR B OG1 
4243 C CG2 . THR B 30  ? 0.3109 0.3791 0.3570 0.0406  0.0463  0.0120  16  THR B CG2 
4244 N N   . ASP B 31  ? 0.3137 0.3796 0.3365 0.0369  0.0527  0.0122  17  ASP B N   
4245 C CA  . ASP B 31  ? 0.3123 0.3795 0.3298 0.0361  0.0557  0.0138  17  ASP B CA  
4246 C C   . ASP B 31  ? 0.3060 0.3752 0.3264 0.0315  0.0519  0.0167  17  ASP B C   
4247 O O   . ASP B 31  ? 0.2842 0.3578 0.3060 0.0304  0.0542  0.0203  17  ASP B O   
4248 C CB  . ASP B 31  ? 0.3107 0.3700 0.3142 0.0371  0.0563  0.0098  17  ASP B CB  
4249 C CG  . ASP B 31  ? 0.3282 0.3847 0.3263 0.0419  0.0613  0.0071  17  ASP B CG  
4250 O OD1 . ASP B 31  ? 0.3116 0.3735 0.3170 0.0451  0.0657  0.0090  17  ASP B OD1 
4251 O OD2 . ASP B 31  ? 0.3081 0.3566 0.2944 0.0426  0.0608  0.0032  17  ASP B OD2 
4252 N N   . CYS B 32  ? 0.2621 0.3277 0.2830 0.0289  0.0463  0.0154  18  CYS B N   
4253 C CA  . CYS B 32  ? 0.2489 0.3147 0.2713 0.0250  0.0426  0.0176  18  CYS B CA  
4254 C C   . CYS B 32  ? 0.2519 0.3232 0.2853 0.0229  0.0411  0.0216  18  CYS B C   
4255 O O   . CYS B 32  ? 0.2737 0.3449 0.3085 0.0196  0.0383  0.0237  18  CYS B O   
4256 C CB  . CYS B 32  ? 0.2692 0.3286 0.2871 0.0235  0.0377  0.0145  18  CYS B CB  
4257 S SG  . CYS B 32  ? 0.2112 0.2641 0.2165 0.0244  0.0378  0.0107  18  CYS B SG  
4258 N N   . GLY B 33  ? 0.2545 0.3304 0.2957 0.0247  0.0427  0.0227  19  GLY B N   
4259 C CA  . GLY B 33  ? 0.2776 0.3594 0.3297 0.0225  0.0412  0.0270  19  GLY B CA  
4260 C C   . GLY B 33  ? 0.2740 0.3548 0.3317 0.0218  0.0368  0.0264  19  GLY B C   
4261 O O   . GLY B 33  ? 0.2684 0.3538 0.3352 0.0198  0.0349  0.0300  19  GLY B O   
4262 N N   . ALA B 34  ? 0.2608 0.3355 0.3131 0.0231  0.0350  0.0222  20  ALA B N   
4263 C CA  . ALA B 34  ? 0.2405 0.3135 0.2968 0.0225  0.0309  0.0215  20  ALA B CA  
4264 C C   . ALA B 34  ? 0.2826 0.3593 0.3447 0.0260  0.0333  0.0219  20  ALA B C   
4265 O O   . ALA B 34  ? 0.3058 0.3805 0.3632 0.0296  0.0366  0.0191  20  ALA B O   
4266 C CB  . ALA B 34  ? 0.2351 0.3000 0.2830 0.0221  0.0280  0.0172  20  ALA B CB  
4267 N N   . ASP B 35  ? 0.2312 0.3129 0.3033 0.0250  0.0312  0.0253  21  ASP B N   
4268 C CA  . ASP B 35  ? 0.2417 0.3274 0.3210 0.0283  0.0327  0.0262  21  ASP B CA  
4269 C C   . ASP B 35  ? 0.2479 0.3295 0.3282 0.0276  0.0276  0.0250  21  ASP B C   
4270 O O   . ASP B 35  ? 0.2358 0.3200 0.3223 0.0301  0.0279  0.0260  21  ASP B O   
4271 C CB  . ASP B 35  ? 0.2261 0.3219 0.3178 0.0280  0.0344  0.0319  21  ASP B CB  
4272 C CG  . ASP B 35  ? 0.2776 0.3778 0.3684 0.0288  0.0400  0.0336  21  ASP B CG  
4273 O OD1 . ASP B 35  ? 0.2697 0.3671 0.3527 0.0323  0.0447  0.0305  21  ASP B OD1 
4274 O OD2 . ASP B 35  ? 0.2752 0.3811 0.3723 0.0257  0.0396  0.0380  21  ASP B OD2 
4275 N N   . HIS B 36  ? 0.2413 0.3163 0.3152 0.0243  0.0232  0.0230  22  HIS B N   
4276 C CA  . HIS B 36  ? 0.2276 0.2977 0.3006 0.0231  0.0184  0.0218  22  HIS B CA  
4277 C C   . HIS B 36  ? 0.2243 0.2861 0.2864 0.0224  0.0172  0.0174  22  HIS B C   
4278 O O   . HIS B 36  ? 0.1896 0.2495 0.2461 0.0213  0.0184  0.0163  22  HIS B O   
4279 C CB  . HIS B 36  ? 0.2243 0.2957 0.3027 0.0189  0.0131  0.0251  22  HIS B CB  
4280 C CG  . HIS B 36  ? 0.2289 0.3092 0.3196 0.0190  0.0132  0.0300  22  HIS B CG  
4281 N ND1 . HIS B 36  ? 0.2439 0.3313 0.3403 0.0186  0.0163  0.0334  22  HIS B ND1 
4282 C CD2 . HIS B 36  ? 0.2348 0.3185 0.3337 0.0194  0.0106  0.0326  22  HIS B CD2 
4283 C CE1 . HIS B 36  ? 0.2409 0.3362 0.3492 0.0187  0.0158  0.0379  22  HIS B CE1 
4284 N NE2 . HIS B 36  ? 0.2477 0.3409 0.3579 0.0192  0.0121  0.0375  22  HIS B NE2 
4285 N N   . LEU B 37  ? 0.2351 0.2920 0.2946 0.0229  0.0148  0.0154  23  LEU B N   
4286 C CA  . LEU B 37  ? 0.2247 0.2741 0.2750 0.0218  0.0133  0.0119  23  LEU B CA  
4287 C C   . LEU B 37  ? 0.2178 0.2635 0.2678 0.0193  0.0084  0.0123  23  LEU B C   
4288 O O   . LEU B 37  ? 0.2229 0.2686 0.2763 0.0202  0.0067  0.0131  23  LEU B O   
4289 C CB  . LEU B 37  ? 0.2143 0.2605 0.2599 0.0250  0.0157  0.0087  23  LEU B CB  
4290 C CG  . LEU B 37  ? 0.2437 0.2829 0.2811 0.0240  0.0143  0.0054  23  LEU B CG  
4291 C CD1 . LEU B 37  ? 0.2242 0.2623 0.2564 0.0225  0.0152  0.0043  23  LEU B CD1 
4292 C CD2 . LEU B 37  ? 0.2220 0.2577 0.2562 0.0268  0.0157  0.0028  23  LEU B CD2 
4293 N N   . PHE B 38  ? 0.1922 0.2340 0.2375 0.0164  0.0062  0.0117  24  PHE B N   
4294 C CA  . PHE B 38  ? 0.2029 0.2397 0.2455 0.0140  0.0020  0.0116  24  PHE B CA  
4295 C C   . PHE B 38  ? 0.2122 0.2429 0.2471 0.0145  0.0022  0.0083  24  PHE B C   
4296 O O   . PHE B 38  ? 0.2245 0.2544 0.2556 0.0156  0.0049  0.0062  24  PHE B O   
4297 C CB  . PHE B 38  ? 0.1999 0.2351 0.2410 0.0107  -0.0001 0.0127  24  PHE B CB  
4298 C CG  . PHE B 38  ? 0.2120 0.2530 0.2608 0.0094  -0.0008 0.0164  24  PHE B CG  
4299 C CD1 . PHE B 38  ? 0.2018 0.2476 0.2532 0.0102  0.0027  0.0174  24  PHE B CD1 
4300 C CD2 . PHE B 38  ? 0.2104 0.2520 0.2636 0.0071  -0.0051 0.0192  24  PHE B CD2 
4301 C CE1 . PHE B 38  ? 0.1833 0.2352 0.2425 0.0087  0.0023  0.0214  24  PHE B CE1 
4302 C CE2 . PHE B 38  ? 0.2049 0.2525 0.2662 0.0054  -0.0059 0.0231  24  PHE B CE2 
4303 C CZ  . PHE B 38  ? 0.1722 0.2251 0.2367 0.0063  -0.0020 0.0243  24  PHE B CZ  
4304 N N   . GLY B 39  ? 0.2214 0.2479 0.2541 0.0135  -0.0008 0.0082  25  GLY B N   
4305 C CA  . GLY B 39  ? 0.2045 0.2251 0.2298 0.0133  -0.0008 0.0056  25  GLY B CA  
4306 C C   . GLY B 39  ? 0.2254 0.2423 0.2492 0.0129  -0.0035 0.0058  25  GLY B C   
4307 O O   . GLY B 39  ? 0.1998 0.2176 0.2273 0.0120  -0.0066 0.0081  25  GLY B O   
4308 N N   . VAL B 40  ? 0.2172 0.2299 0.2355 0.0132  -0.0027 0.0037  26  VAL B N   
4309 C CA  . VAL B 40  ? 0.2370 0.2452 0.2524 0.0126  -0.0052 0.0039  26  VAL B CA  
4310 C C   . VAL B 40  ? 0.2353 0.2424 0.2495 0.0145  -0.0032 0.0023  26  VAL B C   
4311 O O   . VAL B 40  ? 0.2031 0.2098 0.2145 0.0148  -0.0006 0.0004  26  VAL B O   
4312 C CB  . VAL B 40  ? 0.2335 0.2359 0.2416 0.0102  -0.0066 0.0034  26  VAL B CB  
4313 C CG1 . VAL B 40  ? 0.2491 0.2464 0.2527 0.0096  -0.0086 0.0035  26  VAL B CG1 
4314 C CG2 . VAL B 40  ? 0.2136 0.2155 0.2218 0.0081  -0.0092 0.0048  26  VAL B CG2 
4315 N N   . PRO B 41  ? 0.2659 0.2721 0.2821 0.0156  -0.0045 0.0031  27  PRO B N   
4316 C CA  . PRO B 41  ? 0.2882 0.2923 0.3029 0.0173  -0.0029 0.0016  27  PRO B CA  
4317 C C   . PRO B 41  ? 0.2814 0.2803 0.2893 0.0156  -0.0030 0.0004  27  PRO B C   
4318 O O   . PRO B 41  ? 0.2515 0.2476 0.2554 0.0134  -0.0045 0.0010  27  PRO B O   
4319 C CB  . PRO B 41  ? 0.3500 0.3542 0.3691 0.0191  -0.0048 0.0033  27  PRO B CB  
4320 C CG  . PRO B 41  ? 0.3698 0.3733 0.3892 0.0169  -0.0085 0.0056  27  PRO B CG  
4321 C CD  . PRO B 41  ? 0.3040 0.3105 0.3238 0.0153  -0.0080 0.0057  27  PRO B CD  
4322 N N   . GLY B 42  ? 0.2887 0.2861 0.2949 0.0164  -0.0013 -0.0012 28  GLY B N   
4323 C CA  . GLY B 42  ? 0.3001 0.2931 0.3012 0.0148  -0.0012 -0.0019 28  GLY B CA  
4324 C C   . GLY B 42  ? 0.3293 0.3206 0.3305 0.0162  -0.0004 -0.0032 28  GLY B C   
4325 O O   . GLY B 42  ? 0.2979 0.2913 0.3019 0.0184  0.0009  -0.0040 28  GLY B O   
4326 N N   . ASP B 43  ? 0.3264 0.3131 0.3239 0.0148  -0.0011 -0.0032 29  ASP B N   
4327 C CA  . ASP B 43  ? 0.3657 0.3491 0.3626 0.0158  -0.0010 -0.0042 29  ASP B CA  
4328 C C   . ASP B 43  ? 0.3368 0.3219 0.3335 0.0163  0.0011  -0.0063 29  ASP B C   
4329 O O   . ASP B 43  ? 0.3278 0.3110 0.3247 0.0183  0.0015  -0.0076 29  ASP B O   
4330 C CB  . ASP B 43  ? 0.3656 0.3439 0.3586 0.0135  -0.0022 -0.0035 29  ASP B CB  
4331 C CG  . ASP B 43  ? 0.3592 0.3381 0.3495 0.0109  -0.0009 -0.0038 29  ASP B CG  
4332 O OD1 . ASP B 43  ? 0.3103 0.2927 0.3006 0.0101  0.0003  -0.0036 29  ASP B OD1 
4333 O OD2 . ASP B 43  ? 0.3794 0.3552 0.3678 0.0095  -0.0011 -0.0040 29  ASP B OD2 
4334 N N   . TYR B 44  ? 0.3034 0.2920 0.2997 0.0149  0.0023  -0.0067 30  TYR B N   
4335 C CA  . TYR B 44  ? 0.2927 0.2829 0.2885 0.0151  0.0037  -0.0083 30  TYR B CA  
4336 C C   . TYR B 44  ? 0.3007 0.2939 0.2988 0.0178  0.0051  -0.0090 30  TYR B C   
4337 O O   . TYR B 44  ? 0.2855 0.2788 0.2821 0.0183  0.0061  -0.0105 30  TYR B O   
4338 C CB  . TYR B 44  ? 0.2682 0.2614 0.2635 0.0130  0.0045  -0.0080 30  TYR B CB  
4339 C CG  . TYR B 44  ? 0.2798 0.2710 0.2732 0.0104  0.0040  -0.0072 30  TYR B CG  
4340 C CD1 . TYR B 44  ? 0.2973 0.2844 0.2889 0.0093  0.0030  -0.0075 30  TYR B CD1 
4341 C CD2 . TYR B 44  ? 0.2392 0.2322 0.2324 0.0092  0.0048  -0.0060 30  TYR B CD2 
4342 C CE1 . TYR B 44  ? 0.3088 0.2946 0.2993 0.0067  0.0027  -0.0063 30  TYR B CE1 
4343 C CE2 . TYR B 44  ? 0.2622 0.2537 0.2538 0.0070  0.0050  -0.0049 30  TYR B CE2 
4344 C CZ  . TYR B 44  ? 0.2732 0.2616 0.2639 0.0056  0.0040  -0.0049 30  TYR B CZ  
4345 O OH  . TYR B 44  ? 0.2847 0.2724 0.2746 0.0032  0.0044  -0.0033 30  TYR B OH  
4346 N N   . ASN B 45  ? 0.2818 0.2777 0.2834 0.0192  0.0050  -0.0078 31  ASN B N   
4347 C CA  . ASN B 45  ? 0.2863 0.2859 0.2910 0.0217  0.0067  -0.0079 31  ASN B CA  
4348 C C   . ASN B 45  ? 0.3234 0.3226 0.3315 0.0245  0.0066  -0.0072 31  ASN B C   
4349 O O   . ASN B 45  ? 0.3199 0.3230 0.3315 0.0267  0.0084  -0.0068 31  ASN B O   
4350 C CB  . ASN B 45  ? 0.2592 0.2639 0.2665 0.0208  0.0071  -0.0066 31  ASN B CB  
4351 C CG  . ASN B 45  ? 0.2705 0.2757 0.2803 0.0200  0.0050  -0.0045 31  ASN B CG  
4352 O OD1 . ASN B 45  ? 0.2574 0.2614 0.2693 0.0210  0.0037  -0.0035 31  ASN B OD1 
4353 N ND2 . ASN B 45  ? 0.2278 0.2347 0.2373 0.0182  0.0046  -0.0037 31  ASN B ND2 
4354 N N   . LEU B 46  ? 0.3232 0.3180 0.3307 0.0247  0.0048  -0.0068 32  LEU B N   
4355 C CA  . LEU B 46  ? 0.3526 0.3475 0.3645 0.0275  0.0044  -0.0055 32  LEU B CA  
4356 C C   . LEU B 46  ? 0.3891 0.3834 0.4015 0.0312  0.0071  -0.0071 32  LEU B C   
4357 O O   . LEU B 46  ? 0.3757 0.3739 0.3936 0.0342  0.0084  -0.0059 32  LEU B O   
4358 C CB  . LEU B 46  ? 0.4030 0.3924 0.4134 0.0268  0.0016  -0.0047 32  LEU B CB  
4359 C CG  . LEU B 46  ? 0.4561 0.4454 0.4659 0.0238  -0.0011 -0.0026 32  LEU B CG  
4360 C CD1 . LEU B 46  ? 0.5922 0.5765 0.6015 0.0241  -0.0037 -0.0013 32  LEU B CD1 
4361 C CD2 . LEU B 46  ? 0.4385 0.4336 0.4529 0.0237  -0.0016 -0.0008 32  LEU B CD2 
4362 N N   . GLN B 47  ? 0.3867 0.3760 0.3933 0.0312  0.0078  -0.0097 33  GLN B N   
4363 C CA  . GLN B 47  ? 0.3943 0.3813 0.3994 0.0348  0.0105  -0.0116 33  GLN B CA  
4364 C C   . GLN B 47  ? 0.3775 0.3706 0.3843 0.0361  0.0136  -0.0117 33  GLN B C   
4365 O O   . GLN B 47  ? 0.3612 0.3557 0.3704 0.0400  0.0164  -0.0118 33  GLN B O   
4366 C CB  . GLN B 47  ? 0.4580 0.4373 0.4555 0.0336  0.0099  -0.0144 33  GLN B CB  
4367 C CG  . GLN B 47  ? 0.5850 0.5581 0.5808 0.0321  0.0069  -0.0139 33  GLN B CG  
4368 C CD  . GLN B 47  ? 0.7633 0.7276 0.7540 0.0338  0.0069  -0.0163 33  GLN B CD  
4369 O OE1 . GLN B 47  ? 0.8873 0.8456 0.8731 0.0310  0.0048  -0.0172 33  GLN B OE1 
4370 N NE2 . GLN B 47  ? 0.7414 0.7044 0.7332 0.0386  0.0094  -0.0172 33  GLN B NE2 
4371 N N   . PHE B 48  ? 0.3168 0.3133 0.3224 0.0331  0.0134  -0.0115 34  PHE B N   
4372 C CA  . PHE B 48  ? 0.3018 0.3045 0.3096 0.0340  0.0160  -0.0109 34  PHE B CA  
4373 C C   . PHE B 48  ? 0.3154 0.3242 0.3315 0.0356  0.0165  -0.0080 34  PHE B C   
4374 O O   . PHE B 48  ? 0.2869 0.2999 0.3062 0.0383  0.0196  -0.0073 34  PHE B O   
4375 C CB  . PHE B 48  ? 0.2690 0.2740 0.2747 0.0305  0.0152  -0.0108 34  PHE B CB  
4376 C CG  . PHE B 48  ? 0.2597 0.2709 0.2679 0.0310  0.0174  -0.0096 34  PHE B CG  
4377 C CD1 . PHE B 48  ? 0.2506 0.2619 0.2557 0.0330  0.0205  -0.0109 34  PHE B CD1 
4378 C CD2 . PHE B 48  ? 0.2615 0.2776 0.2744 0.0292  0.0164  -0.0072 34  PHE B CD2 
4379 C CE1 . PHE B 48  ? 0.2619 0.2787 0.2690 0.0332  0.0226  -0.0095 34  PHE B CE1 
4380 C CE2 . PHE B 48  ? 0.2192 0.2405 0.2343 0.0292  0.0182  -0.0059 34  PHE B CE2 
4381 C CZ  . PHE B 48  ? 0.2615 0.2835 0.2740 0.0312  0.0214  -0.0069 34  PHE B CZ  
4382 N N   . LEU B 49  ? 0.2999 0.3093 0.3195 0.0338  0.0134  -0.0060 35  LEU B N   
4383 C CA  . LEU B 49  ? 0.3378 0.3529 0.3655 0.0346  0.0128  -0.0028 35  LEU B CA  
4384 C C   . LEU B 49  ? 0.3425 0.3587 0.3752 0.0391  0.0148  -0.0021 35  LEU B C   
4385 O O   . LEU B 49  ? 0.3512 0.3740 0.3912 0.0407  0.0161  0.0004  35  LEU B O   
4386 C CB  . LEU B 49  ? 0.3545 0.3681 0.3831 0.0318  0.0086  -0.0012 35  LEU B CB  
4387 C CG  . LEU B 49  ? 0.3651 0.3826 0.3957 0.0287  0.0069  0.0008  35  LEU B CG  
4388 C CD1 . LEU B 49  ? 0.3890 0.4034 0.4186 0.0262  0.0028  0.0021  35  LEU B CD1 
4389 C CD2 . LEU B 49  ? 0.3336 0.3583 0.3719 0.0300  0.0080  0.0033  35  LEU B CD2 
4390 N N   . ASP B 50  ? 0.3491 0.3589 0.3782 0.0413  0.0150  -0.0041 36  ASP B N   
4391 C CA  . ASP B 50  ? 0.3864 0.3965 0.4198 0.0463  0.0175  -0.0036 36  ASP B CA  
4392 C C   . ASP B 50  ? 0.3925 0.4069 0.4268 0.0493  0.0225  -0.0041 36  ASP B C   
4393 O O   . ASP B 50  ? 0.3873 0.4067 0.4289 0.0531  0.0252  -0.0022 36  ASP B O   
4394 C CB  . ASP B 50  ? 0.4209 0.4217 0.4486 0.0482  0.0171  -0.0061 36  ASP B CB  
4395 C CG  . ASP B 50  ? 0.4895 0.4866 0.5178 0.0461  0.0124  -0.0047 36  ASP B CG  
4396 O OD1 . ASP B 50  ? 0.4723 0.4742 0.5067 0.0446  0.0098  -0.0016 36  ASP B OD1 
4397 O OD2 . ASP B 50  ? 0.4933 0.4821 0.5156 0.0459  0.0113  -0.0067 36  ASP B OD2 
4398 N N   . HIS B 51  ? 0.3476 0.3604 0.3747 0.0476  0.0240  -0.0065 37  HIS B N   
4399 C CA  . HIS B 51  ? 0.3454 0.3619 0.3721 0.0501  0.0289  -0.0069 37  HIS B CA  
4400 C C   . HIS B 51  ? 0.3552 0.3815 0.3902 0.0489  0.0294  -0.0032 37  HIS B C   
4401 O O   . HIS B 51  ? 0.3652 0.3970 0.4047 0.0519  0.0335  -0.0017 37  HIS B O   
4402 C CB  . HIS B 51  ? 0.3330 0.3445 0.3491 0.0484  0.0297  -0.0102 37  HIS B CB  
4403 C CG  . HIS B 51  ? 0.3483 0.3499 0.3561 0.0499  0.0297  -0.0138 37  HIS B CG  
4404 N ND1 . HIS B 51  ? 0.3448 0.3423 0.3467 0.0536  0.0337  -0.0163 37  HIS B ND1 
4405 C CD2 . HIS B 51  ? 0.3520 0.3466 0.3562 0.0482  0.0261  -0.0152 37  HIS B CD2 
4406 C CE1 . HIS B 51  ? 0.3754 0.3631 0.3700 0.0540  0.0322  -0.0193 37  HIS B CE1 
4407 N NE2 . HIS B 51  ? 0.3620 0.3482 0.3584 0.0506  0.0276  -0.0185 37  HIS B NE2 
4408 N N   . VAL B 52  ? 0.3154 0.3438 0.3523 0.0445  0.0254  -0.0016 38  VAL B N   
4409 C CA  . VAL B 52  ? 0.3080 0.3447 0.3526 0.0429  0.0251  0.0021  38  VAL B CA  
4410 C C   . VAL B 52  ? 0.3407 0.3828 0.3960 0.0454  0.0251  0.0055  38  VAL B C   
4411 O O   . VAL B 52  ? 0.3162 0.3659 0.3788 0.0468  0.0278  0.0083  38  VAL B O   
4412 C CB  . VAL B 52  ? 0.3245 0.3606 0.3678 0.0378  0.0206  0.0028  38  VAL B CB  
4413 C CG1 . VAL B 52  ? 0.3047 0.3483 0.3554 0.0358  0.0199  0.0065  38  VAL B CG1 
4414 C CG2 . VAL B 52  ? 0.2842 0.3157 0.3182 0.0356  0.0206  -0.0002 38  VAL B CG2 
4415 N N   . ILE B 53  ? 0.3413 0.3796 0.3978 0.0460  0.0220  0.0056  39  ILE B N   
4416 C CA  . ILE B 53  ? 0.3648 0.4082 0.4320 0.0484  0.0213  0.0092  39  ILE B CA  
4417 C C   . ILE B 53  ? 0.3802 0.4267 0.4515 0.0542  0.0270  0.0094  39  ILE B C   
4418 O O   . ILE B 53  ? 0.3865 0.4418 0.4680 0.0559  0.0289  0.0130  39  ILE B O   
4419 C CB  . ILE B 53  ? 0.4066 0.4443 0.4732 0.0480  0.0167  0.0092  39  ILE B CB  
4420 C CG1 . ILE B 53  ? 0.4093 0.4477 0.4771 0.0430  0.0110  0.0114  39  ILE B CG1 
4421 C CG2 . ILE B 53  ? 0.4377 0.4778 0.5129 0.0529  0.0176  0.0115  39  ILE B CG2 
4422 C CD1 . ILE B 53  ? 0.3901 0.4251 0.4495 0.0386  0.0098  0.0093  39  ILE B CD1 
4423 N N   . ASP B 54  ? 0.3705 0.4098 0.4337 0.0573  0.0300  0.0054  40  ASP B N   
4424 C CA  . ASP B 54  ? 0.4097 0.4503 0.4755 0.0635  0.0357  0.0052  40  ASP B CA  
4425 C C   . ASP B 54  ? 0.3942 0.4414 0.4612 0.0645  0.0411  0.0060  40  ASP B C   
4426 O O   . ASP B 54  ? 0.3951 0.4466 0.4675 0.0696  0.0462  0.0073  40  ASP B O   
4427 C CB  . ASP B 54  ? 0.4527 0.4821 0.5077 0.0663  0.0373  0.0004  40  ASP B CB  
4428 C CG  . ASP B 54  ? 0.5041 0.5274 0.5599 0.0670  0.0333  0.0003  40  ASP B CG  
4429 O OD1 . ASP B 54  ? 0.6199 0.6484 0.6862 0.0681  0.0313  0.0041  40  ASP B OD1 
4430 O OD2 . ASP B 54  ? 0.5057 0.5189 0.5516 0.0665  0.0321  -0.0034 40  ASP B OD2 
4431 N N   . SER B 55  ? 0.3892 0.4371 0.4510 0.0601  0.0402  0.0054  41  SER B N   
4432 C CA  . SER B 55  ? 0.4053 0.4586 0.4670 0.0608  0.0452  0.0062  41  SER B CA  
4433 C C   . SER B 55  ? 0.3891 0.4543 0.4648 0.0613  0.0464  0.0117  41  SER B C   
4434 O O   . SER B 55  ? 0.3553 0.4245 0.4381 0.0576  0.0415  0.0148  41  SER B O   
4435 C CB  . SER B 55  ? 0.3735 0.4248 0.4272 0.0558  0.0433  0.0047  41  SER B CB  
4436 O OG  . SER B 55  ? 0.3883 0.4466 0.4446 0.0554  0.0468  0.0070  41  SER B OG  
4437 N N   . PRO B 56  ? 0.4105 0.4813 0.4902 0.0656  0.0529  0.0132  42  PRO B N   
4438 C CA  . PRO B 56  ? 0.3738 0.4569 0.4672 0.0653  0.0542  0.0190  42  PRO B CA  
4439 C C   . PRO B 56  ? 0.3651 0.4525 0.4578 0.0601  0.0534  0.0208  42  PRO B C   
4440 O O   . PRO B 56  ? 0.3607 0.4577 0.4647 0.0582  0.0528  0.0259  42  PRO B O   
4441 C CB  . PRO B 56  ? 0.4193 0.5062 0.5157 0.0720  0.0625  0.0196  42  PRO B CB  
4442 C CG  . PRO B 56  ? 0.4153 0.4905 0.4981 0.0758  0.0651  0.0136  42  PRO B CG  
4443 C CD  . PRO B 56  ? 0.4153 0.4811 0.4865 0.0707  0.0594  0.0097  42  PRO B CD  
4444 N N   . ASP B 57  ? 0.3607 0.4411 0.4406 0.0575  0.0529  0.0171  43  ASP B N   
4445 C CA  . ASP B 57  ? 0.3382 0.4220 0.4164 0.0534  0.0529  0.0186  43  ASP B CA  
4446 C C   . ASP B 57  ? 0.3376 0.4192 0.4148 0.0473  0.0459  0.0189  43  ASP B C   
4447 O O   . ASP B 57  ? 0.2976 0.3824 0.3754 0.0437  0.0452  0.0210  43  ASP B O   
4448 C CB  . ASP B 57  ? 0.4134 0.4914 0.4784 0.0545  0.0569  0.0148  43  ASP B CB  
4449 C CG  . ASP B 57  ? 0.4524 0.5309 0.5157 0.0607  0.0644  0.0140  43  ASP B CG  
4450 O OD1 . ASP B 57  ? 0.4300 0.5149 0.5039 0.0644  0.0673  0.0169  43  ASP B OD1 
4451 O OD2 . ASP B 57  ? 0.5087 0.5807 0.5596 0.0619  0.0674  0.0104  43  ASP B OD2 
4452 N N   . ILE B 58  ? 0.3196 0.3950 0.3943 0.0463  0.0411  0.0167  44  ILE B N   
4453 C CA  . ILE B 58  ? 0.2813 0.3535 0.3534 0.0410  0.0350  0.0165  44  ILE B CA  
4454 C C   . ILE B 58  ? 0.2838 0.3562 0.3626 0.0401  0.0301  0.0181  44  ILE B C   
4455 O O   . ILE B 58  ? 0.3045 0.3745 0.3842 0.0434  0.0304  0.0171  44  ILE B O   
4456 C CB  . ILE B 58  ? 0.2782 0.3412 0.3375 0.0399  0.0340  0.0117  44  ILE B CB  
4457 C CG1 . ILE B 58  ? 0.2871 0.3473 0.3440 0.0349  0.0287  0.0116  44  ILE B CG1 
4458 C CG2 . ILE B 58  ? 0.3278 0.3843 0.3825 0.0429  0.0342  0.0083  44  ILE B CG2 
4459 C CD1 . ILE B 58  ? 0.2740 0.3370 0.3302 0.0320  0.0290  0.0133  44  ILE B CD1 
4460 N N   . CYS B 59  ? 0.2719 0.3466 0.3550 0.0357  0.0255  0.0209  45  CYS B N   
4461 C CA  . CYS B 59  ? 0.2761 0.3507 0.3647 0.0342  0.0202  0.0229  45  CYS B CA  
4462 C C   . CYS B 59  ? 0.2407 0.3071 0.3206 0.0305  0.0154  0.0202  45  CYS B C   
4463 O O   . CYS B 59  ? 0.2370 0.3020 0.3130 0.0269  0.0139  0.0200  45  CYS B O   
4464 C CB  . CYS B 59  ? 0.2938 0.3770 0.3940 0.0319  0.0182  0.0283  45  CYS B CB  
4465 S SG  . CYS B 59  ? 0.3213 0.4038 0.4271 0.0287  0.0104  0.0311  45  CYS B SG  
4466 N N   . TRP B 60  ? 0.2710 0.3319 0.3480 0.0315  0.0131  0.0184  46  TRP B N   
4467 C CA  . TRP B 60  ? 0.2640 0.3175 0.3335 0.0281  0.0087  0.0165  46  TRP B CA  
4468 C C   . TRP B 60  ? 0.2670 0.3217 0.3404 0.0241  0.0033  0.0196  46  TRP B C   
4469 O O   . TRP B 60  ? 0.2572 0.3161 0.3390 0.0244  0.0010  0.0230  46  TRP B O   
4470 C CB  . TRP B 60  ? 0.2697 0.3174 0.3355 0.0302  0.0078  0.0143  46  TRP B CB  
4471 C CG  . TRP B 60  ? 0.2952 0.3360 0.3542 0.0269  0.0034  0.0130  46  TRP B CG  
4472 C CD1 . TRP B 60  ? 0.3121 0.3503 0.3721 0.0258  -0.0010 0.0144  46  TRP B CD1 
4473 C CD2 . TRP B 60  ? 0.2783 0.3139 0.3282 0.0245  0.0033  0.0102  46  TRP B CD2 
4474 N NE1 . TRP B 60  ? 0.3258 0.3572 0.3772 0.0228  -0.0034 0.0125  46  TRP B NE1 
4475 C CE2 . TRP B 60  ? 0.2898 0.3199 0.3355 0.0221  -0.0007 0.0100  46  TRP B CE2 
4476 C CE3 . TRP B 60  ? 0.2469 0.2821 0.2920 0.0242  0.0062  0.0081  46  TRP B CE3 
4477 C CZ2 . TRP B 60  ? 0.2895 0.3142 0.3269 0.0198  -0.0013 0.0077  46  TRP B CZ2 
4478 C CZ3 . TRP B 60  ? 0.2462 0.2763 0.2839 0.0218  0.0051  0.0060  46  TRP B CZ3 
4479 C CH2 . TRP B 60  ? 0.2492 0.2743 0.2832 0.0198  0.0017  0.0059  46  TRP B CH2 
4480 N N   . VAL B 61  ? 0.2145 0.2648 0.2813 0.0204  0.0010  0.0185  47  VAL B N   
4481 C CA  . VAL B 61  ? 0.2349 0.2839 0.3027 0.0163  -0.0044 0.0207  47  VAL B CA  
4482 C C   . VAL B 61  ? 0.2243 0.2643 0.2820 0.0145  -0.0070 0.0179  47  VAL B C   
4483 O O   . VAL B 61  ? 0.2147 0.2506 0.2650 0.0133  -0.0060 0.0154  47  VAL B O   
4484 C CB  . VAL B 61  ? 0.2223 0.2741 0.2916 0.0135  -0.0045 0.0224  47  VAL B CB  
4485 C CG1 . VAL B 61  ? 0.2146 0.2641 0.2846 0.0090  -0.0105 0.0248  47  VAL B CG1 
4486 C CG2 . VAL B 61  ? 0.1992 0.2604 0.2782 0.0155  -0.0007 0.0253  47  VAL B CG2 
4487 N N   . GLY B 62  ? 0.2118 0.2489 0.2692 0.0146  -0.0102 0.0184  48  GLY B N   
4488 C CA  . GLY B 62  ? 0.2460 0.2746 0.2938 0.0128  -0.0126 0.0161  48  GLY B CA  
4489 C C   . GLY B 62  ? 0.2338 0.2588 0.2777 0.0086  -0.0165 0.0170  48  GLY B C   
4490 O O   . GLY B 62  ? 0.2314 0.2592 0.2809 0.0066  -0.0202 0.0203  48  GLY B O   
4491 N N   . CYS B 63  ? 0.1950 0.2139 0.2296 0.0073  -0.0157 0.0142  49  CYS B N   
4492 C CA  . CYS B 63  ? 0.2011 0.2149 0.2302 0.0039  -0.0188 0.0143  49  CYS B CA  
4493 C C   . CYS B 63  ? 0.2216 0.2270 0.2413 0.0026  -0.0212 0.0129  49  CYS B C   
4494 O O   . CYS B 63  ? 0.2046 0.2083 0.2218 0.0043  -0.0197 0.0115  49  CYS B O   
4495 C CB  . CYS B 63  ? 0.2226 0.2360 0.2487 0.0037  -0.0156 0.0125  49  CYS B CB  
4496 S SG  . CYS B 63  ? 0.1502 0.1728 0.1862 0.0045  -0.0132 0.0148  49  CYS B SG  
4497 N N   . ALA B 64  ? 0.2367 0.2363 0.2509 -0.0006 -0.0249 0.0133  50  ALA B N   
4498 C CA  . ALA B 64  ? 0.2405 0.2316 0.2449 -0.0021 -0.0274 0.0123  50  ALA B CA  
4499 C C   . ALA B 64  ? 0.2459 0.2316 0.2411 -0.0011 -0.0235 0.0088  50  ALA B C   
4500 O O   . ALA B 64  ? 0.2808 0.2609 0.2687 -0.0013 -0.0239 0.0079  50  ALA B O   
4501 C CB  . ALA B 64  ? 0.2438 0.2295 0.2442 -0.0060 -0.0330 0.0138  50  ALA B CB  
4502 N N   . ASN B 65  ? 0.2146 0.2018 0.2098 -0.0001 -0.0198 0.0072  51  ASN B N   
4503 C CA  . ASN B 65  ? 0.2134 0.1984 0.2032 0.0016  -0.0153 0.0045  51  ASN B CA  
4504 C C   . ASN B 65  ? 0.2111 0.2015 0.2058 0.0032  -0.0117 0.0038  51  ASN B C   
4505 O O   . ASN B 65  ? 0.2030 0.1979 0.2039 0.0028  -0.0125 0.0054  51  ASN B O   
4506 C CB  . ASN B 65  ? 0.2353 0.2112 0.2141 0.0003  -0.0156 0.0029  51  ASN B CB  
4507 C CG  . ASN B 65  ? 0.2224 0.1948 0.1986 -0.0013 -0.0169 0.0028  51  ASN B CG  
4508 O OD1 . ASN B 65  ? 0.2335 0.2106 0.2154 -0.0008 -0.0158 0.0033  51  ASN B OD1 
4509 N ND2 . ASN B 65  ? 0.2343 0.1976 0.2008 -0.0031 -0.0192 0.0021  51  ASN B ND2 
4510 N N   . GLU B 66  ? 0.1994 0.1896 0.1914 0.0049  -0.0078 0.0018  52  GLU B N   
4511 C CA  . GLU B 66  ? 0.2040 0.1996 0.2006 0.0065  -0.0047 0.0014  52  GLU B CA  
4512 C C   . GLU B 66  ? 0.2088 0.2031 0.2043 0.0058  -0.0045 0.0014  52  GLU B C   
4513 O O   . GLU B 66  ? 0.2103 0.2095 0.2108 0.0063  -0.0033 0.0021  52  GLU B O   
4514 C CB  . GLU B 66  ? 0.1903 0.1864 0.1851 0.0081  -0.0012 -0.0004 52  GLU B CB  
4515 C CG  . GLU B 66  ? 0.1919 0.1898 0.1886 0.0090  -0.0010 -0.0005 52  GLU B CG  
4516 C CD  . GLU B 66  ? 0.2075 0.2001 0.1990 0.0081  -0.0025 -0.0005 52  GLU B CD  
4517 O OE1 . GLU B 66  ? 0.2022 0.1897 0.1882 0.0067  -0.0039 -0.0004 52  GLU B OE1 
4518 O OE2 . GLU B 66  ? 0.1787 0.1718 0.1710 0.0088  -0.0022 -0.0006 52  GLU B OE2 
4519 N N   . LEU B 67  ? 0.2055 0.1928 0.1940 0.0047  -0.0054 0.0006  53  LEU B N   
4520 C CA  . LEU B 67  ? 0.2094 0.1944 0.1967 0.0040  -0.0056 0.0007  53  LEU B CA  
4521 C C   . LEU B 67  ? 0.2136 0.2013 0.2063 0.0021  -0.0087 0.0031  53  LEU B C   
4522 O O   . LEU B 67  ? 0.2155 0.2068 0.2124 0.0022  -0.0079 0.0040  53  LEU B O   
4523 C CB  . LEU B 67  ? 0.2211 0.1966 0.1989 0.0033  -0.0062 -0.0007 53  LEU B CB  
4524 C CG  . LEU B 67  ? 0.2453 0.2168 0.2208 0.0029  -0.0064 -0.0008 53  LEU B CG  
4525 C CD1 . LEU B 67  ? 0.2199 0.1965 0.1998 0.0052  -0.0026 -0.0011 53  LEU B CD1 
4526 C CD2 . LEU B 67  ? 0.2202 0.1808 0.1849 0.0027  -0.0066 -0.0026 53  LEU B CD2 
4527 N N   . ASN B 68  ? 0.2243 0.2106 0.2172 0.0001  -0.0126 0.0044  54  ASN B N   
4528 C CA  . ASN B 68  ? 0.2335 0.2233 0.2328 -0.0020 -0.0159 0.0072  54  ASN B CA  
4529 C C   . ASN B 68  ? 0.2091 0.2089 0.2181 -0.0003 -0.0134 0.0087  54  ASN B C   
4530 O O   . ASN B 68  ? 0.2141 0.2178 0.2285 -0.0013 -0.0138 0.0108  54  ASN B O   
4531 C CB  . ASN B 68  ? 0.2306 0.2182 0.2293 -0.0040 -0.0205 0.0087  54  ASN B CB  
4532 C CG  . ASN B 68  ? 0.2227 0.1995 0.2106 -0.0062 -0.0235 0.0074  54  ASN B CG  
4533 O OD1 . ASN B 68  ? 0.2593 0.2303 0.2405 -0.0059 -0.0218 0.0055  54  ASN B OD1 
4534 N ND2 . ASN B 68  ? 0.2543 0.2281 0.2402 -0.0082 -0.0280 0.0087  54  ASN B ND2 
4535 N N   . ALA B 69  ? 0.2082 0.2114 0.2188 0.0022  -0.0108 0.0077  55  ALA B N   
4536 C CA  . ALA B 69  ? 0.2068 0.2182 0.2250 0.0042  -0.0081 0.0086  55  ALA B CA  
4537 C C   . ALA B 69  ? 0.2107 0.2243 0.2294 0.0048  -0.0052 0.0083  55  ALA B C   
4538 O O   . ALA B 69  ? 0.1969 0.2163 0.2215 0.0051  -0.0041 0.0101  55  ALA B O   
4539 C CB  . ALA B 69  ? 0.1951 0.2077 0.2130 0.0066  -0.0060 0.0070  55  ALA B CB  
4540 N N   . SER B 70  ? 0.2190 0.2280 0.2314 0.0053  -0.0038 0.0061  56  SER B N   
4541 C CA  . SER B 70  ? 0.1970 0.2077 0.2098 0.0060  -0.0014 0.0060  56  SER B CA  
4542 C C   . SER B 70  ? 0.2019 0.2113 0.2158 0.0037  -0.0034 0.0080  56  SER B C   
4543 O O   . SER B 70  ? 0.2134 0.2268 0.2308 0.0038  -0.0021 0.0095  56  SER B O   
4544 C CB  . SER B 70  ? 0.2129 0.2195 0.2198 0.0072  0.0005  0.0036  56  SER B CB  
4545 O OG  . SER B 70  ? 0.2129 0.2121 0.2139 0.0061  -0.0011 0.0028  56  SER B OG  
4546 N N   . TYR B 71  ? 0.2128 0.2162 0.2234 0.0015  -0.0069 0.0083  57  TYR B N   
4547 C CA  . TYR B 71  ? 0.2150 0.2169 0.2271 -0.0013 -0.0097 0.0106  57  TYR B CA  
4548 C C   . TYR B 71  ? 0.1998 0.2098 0.2212 -0.0024 -0.0105 0.0139  57  TYR B C   
4549 O O   . TYR B 71  ? 0.1853 0.1983 0.2106 -0.0036 -0.0105 0.0162  57  TYR B O   
4550 C CB  . TYR B 71  ? 0.2245 0.2177 0.2304 -0.0038 -0.0138 0.0101  57  TYR B CB  
4551 C CG  . TYR B 71  ? 0.2232 0.2070 0.2193 -0.0030 -0.0131 0.0072  57  TYR B CG  
4552 C CD1 . TYR B 71  ? 0.2298 0.2126 0.2240 -0.0010 -0.0099 0.0061  57  TYR B CD1 
4553 C CD2 . TYR B 71  ? 0.2358 0.2114 0.2242 -0.0042 -0.0157 0.0059  57  TYR B CD2 
4554 C CE1 . TYR B 71  ? 0.2238 0.1983 0.2098 0.0001  -0.0088 0.0037  57  TYR B CE1 
4555 C CE2 . TYR B 71  ? 0.2150 0.1817 0.1939 -0.0031 -0.0144 0.0033  57  TYR B CE2 
4556 C CZ  . TYR B 71  ? 0.2301 0.1965 0.2083 -0.0008 -0.0108 0.0022  57  TYR B CZ  
4557 O OH  . TYR B 71  ? 0.1953 0.1530 0.1647 0.0007  -0.0092 -0.0002 57  TYR B OH  
4558 N N   . ALA B 72  ? 0.1950 0.2087 0.2201 -0.0019 -0.0113 0.0145  58  ALA B N   
4559 C CA  . ALA B 72  ? 0.2009 0.2228 0.2356 -0.0024 -0.0117 0.0179  58  ALA B CA  
4560 C C   . ALA B 72  ? 0.1961 0.2252 0.2353 0.0000  -0.0070 0.0185  58  ALA B C   
4561 O O   . ALA B 72  ? 0.1864 0.2212 0.2322 -0.0011 -0.0066 0.0216  58  ALA B O   
4562 C CB  . ALA B 72  ? 0.1651 0.1890 0.2027 -0.0015 -0.0130 0.0181  58  ALA B CB  
4563 N N   . ALA B 73  ? 0.1873 0.2162 0.2228 0.0029  -0.0035 0.0156  59  ALA B N   
4564 C CA  . ALA B 73  ? 0.2052 0.2396 0.2431 0.0050  0.0007  0.0158  59  ALA B CA  
4565 C C   . ALA B 73  ? 0.1829 0.2169 0.2201 0.0035  0.0011  0.0172  59  ALA B C   
4566 O O   . ALA B 73  ? 0.2088 0.2484 0.2503 0.0037  0.0032  0.0194  59  ALA B O   
4567 C CB  . ALA B 73  ? 0.1574 0.1901 0.1902 0.0078  0.0035  0.0124  59  ALA B CB  
4568 N N   . ASP B 74  ? 0.2047 0.2317 0.2362 0.0021  -0.0009 0.0160  60  ASP B N   
4569 C CA  . ASP B 74  ? 0.1984 0.2236 0.2289 0.0006  -0.0011 0.0174  60  ASP B CA  
4570 C C   . ASP B 74  ? 0.2002 0.2286 0.2368 -0.0024 -0.0031 0.0214  60  ASP B C   
4571 O O   . ASP B 74  ? 0.1871 0.2197 0.2268 -0.0028 -0.0014 0.0238  60  ASP B O   
4572 C CB  . ASP B 74  ? 0.1898 0.2059 0.2129 0.0000  -0.0030 0.0152  60  ASP B CB  
4573 C CG  . ASP B 74  ? 0.2011 0.2140 0.2223 -0.0009 -0.0031 0.0162  60  ASP B CG  
4574 O OD1 . ASP B 74  ? 0.2030 0.2163 0.2272 -0.0036 -0.0051 0.0192  60  ASP B OD1 
4575 O OD2 . ASP B 74  ? 0.2249 0.2346 0.2416 0.0010  -0.0015 0.0143  60  ASP B OD2 
4576 N N   . GLY B 75  ? 0.1980 0.2245 0.2363 -0.0048 -0.0071 0.0225  61  GLY B N   
4577 C CA  . GLY B 75  ? 0.2067 0.2372 0.2522 -0.0080 -0.0095 0.0268  61  GLY B CA  
4578 C C   . GLY B 75  ? 0.2054 0.2467 0.2598 -0.0065 -0.0060 0.0295  61  GLY B C   
4579 O O   . GLY B 75  ? 0.1920 0.2382 0.2516 -0.0081 -0.0052 0.0330  61  GLY B O   
4580 N N   . TYR B 76  ? 0.1747 0.2196 0.2303 -0.0033 -0.0036 0.0278  62  TYR B N   
4581 C CA  . TYR B 76  ? 0.1886 0.2430 0.2515 -0.0010 0.0005  0.0298  62  TYR B CA  
4582 C C   . TYR B 76  ? 0.2029 0.2595 0.2640 0.0000  0.0046  0.0302  62  TYR B C   
4583 O O   . TYR B 76  ? 0.2190 0.2823 0.2864 -0.0007 0.0065  0.0339  62  TYR B O   
4584 C CB  . TYR B 76  ? 0.1776 0.2326 0.2394 0.0027  0.0024  0.0270  62  TYR B CB  
4585 C CG  . TYR B 76  ? 0.1892 0.2526 0.2574 0.0057  0.0067  0.0284  62  TYR B CG  
4586 C CD1 . TYR B 76  ? 0.1900 0.2553 0.2552 0.0085  0.0118  0.0270  62  TYR B CD1 
4587 C CD2 . TYR B 76  ? 0.1959 0.2648 0.2729 0.0061  0.0058  0.0310  62  TYR B CD2 
4588 C CE1 . TYR B 76  ? 0.1892 0.2608 0.2589 0.0117  0.0161  0.0279  62  TYR B CE1 
4589 C CE2 . TYR B 76  ? 0.1928 0.2690 0.2757 0.0096  0.0103  0.0322  62  TYR B CE2 
4590 C CZ  . TYR B 76  ? 0.2122 0.2893 0.2909 0.0125  0.0156  0.0304  62  TYR B CZ  
4591 O OH  . TYR B 76  ? 0.1930 0.2763 0.2762 0.0163  0.0205  0.0313  62  TYR B OH  
4592 N N   . ALA B 77  ? 0.1866 0.2379 0.2395 0.0014  0.0058  0.0268  63  ALA B N   
4593 C CA  . ALA B 77  ? 0.2033 0.2561 0.2536 0.0024  0.0093  0.0271  63  ALA B CA  
4594 C C   . ALA B 77  ? 0.2199 0.2726 0.2721 -0.0009 0.0079  0.0307  63  ALA B C   
4595 O O   . ALA B 77  ? 0.2061 0.2631 0.2595 -0.0007 0.0109  0.0329  63  ALA B O   
4596 C CB  . ALA B 77  ? 0.2014 0.2483 0.2432 0.0041  0.0098  0.0231  63  ALA B CB  
4597 N N   . ARG B 78  ? 0.1837 0.2311 0.2355 -0.0041 0.0033  0.0313  64  ARG B N   
4598 C CA  . ARG B 78  ? 0.2150 0.2619 0.2692 -0.0076 0.0015  0.0350  64  ARG B CA  
4599 C C   . ARG B 78  ? 0.2213 0.2770 0.2855 -0.0095 0.0019  0.0400  64  ARG B C   
4600 O O   . ARG B 78  ? 0.2106 0.2675 0.2778 -0.0126 0.0011  0.0438  64  ARG B O   
4601 C CB  . ARG B 78  ? 0.2088 0.2463 0.2587 -0.0104 -0.0037 0.0341  64  ARG B CB  
4602 C CG  . ARG B 78  ? 0.2355 0.2647 0.2760 -0.0083 -0.0034 0.0299  64  ARG B CG  
4603 C CD  . ARG B 78  ? 0.2559 0.2752 0.2918 -0.0109 -0.0080 0.0292  64  ARG B CD  
4604 N NE  . ARG B 78  ? 0.2483 0.2598 0.2759 -0.0086 -0.0076 0.0253  64  ARG B NE  
4605 C CZ  . ARG B 78  ? 0.2608 0.2631 0.2829 -0.0098 -0.0099 0.0247  64  ARG B CZ  
4606 N NH1 . ARG B 78  ? 0.2320 0.2313 0.2555 -0.0134 -0.0129 0.0276  64  ARG B NH1 
4607 N NH2 . ARG B 78  ? 0.2203 0.2162 0.2356 -0.0072 -0.0090 0.0211  64  ARG B NH2 
4608 N N   . CYS B 79  ? 0.1946 0.2565 0.2645 -0.0078 0.0033  0.0402  65  CYS B N   
4609 C CA  . CYS B 79  ? 0.2147 0.2864 0.2954 -0.0087 0.0046  0.0451  65  CYS B CA  
4610 C C   . CYS B 79  ? 0.2266 0.3061 0.3093 -0.0048 0.0113  0.0454  65  CYS B C   
4611 O O   . CYS B 79  ? 0.2464 0.3334 0.3358 -0.0056 0.0140  0.0498  65  CYS B O   
4612 C CB  . CYS B 79  ? 0.2026 0.2764 0.2895 -0.0094 0.0012  0.0459  65  CYS B CB  
4613 S SG  . CYS B 79  ? 0.2476 0.3123 0.3319 -0.0147 -0.0070 0.0462  65  CYS B SG  
4614 N N   . LYS B 80  ? 0.2101 0.2875 0.2867 -0.0007 0.0141  0.0410  66  LYS B N   
4615 C CA  . LYS B 80  ? 0.2197 0.3029 0.2968 0.0033  0.0203  0.0407  66  LYS B CA  
4616 C C   . LYS B 80  ? 0.2479 0.3274 0.3155 0.0049  0.0233  0.0382  66  LYS B C   
4617 O O   . LYS B 80  ? 0.2595 0.3429 0.3258 0.0079  0.0284  0.0380  66  LYS B O   
4618 C CB  . LYS B 80  ? 0.2319 0.3158 0.3099 0.0069  0.0212  0.0378  66  LYS B CB  
4619 C CG  . LYS B 80  ? 0.2636 0.3525 0.3522 0.0057  0.0185  0.0410  66  LYS B CG  
4620 C CD  . LYS B 80  ? 0.2649 0.3589 0.3582 0.0101  0.0220  0.0405  66  LYS B CD  
4621 C CE  . LYS B 80  ? 0.2958 0.3983 0.3940 0.0125  0.0284  0.0435  66  LYS B CE  
4622 N NZ  . LYS B 80  ? 0.3354 0.4448 0.4419 0.0165  0.0316  0.0447  66  LYS B NZ  
4623 N N   . GLY B 81  ? 0.2261 0.2983 0.2870 0.0031  0.0202  0.0365  67  GLY B N   
4624 C CA  . GLY B 81  ? 0.2571 0.3258 0.3096 0.0044  0.0221  0.0345  67  GLY B CA  
4625 C C   . GLY B 81  ? 0.2491 0.3135 0.2947 0.0074  0.0226  0.0295  67  GLY B C   
4626 O O   . GLY B 81  ? 0.2756 0.3369 0.3142 0.0082  0.0235  0.0279  67  GLY B O   
4627 N N   . PHE B 82  ? 0.2264 0.2905 0.2737 0.0089  0.0218  0.0273  68  PHE B N   
4628 C CA  . PHE B 82  ? 0.2327 0.2928 0.2740 0.0115  0.0222  0.0228  68  PHE B CA  
4629 C C   . PHE B 82  ? 0.1932 0.2524 0.2376 0.0119  0.0200  0.0215  68  PHE B C   
4630 O O   . PHE B 82  ? 0.2199 0.2836 0.2717 0.0115  0.0197  0.0240  68  PHE B O   
4631 C CB  . PHE B 82  ? 0.2415 0.3041 0.2795 0.0146  0.0269  0.0217  68  PHE B CB  
4632 C CG  . PHE B 82  ? 0.2472 0.3046 0.2767 0.0160  0.0269  0.0178  68  PHE B CG  
4633 C CD1 . PHE B 82  ? 0.2630 0.3182 0.2868 0.0152  0.0268  0.0179  68  PHE B CD1 
4634 C CD2 . PHE B 82  ? 0.2450 0.2999 0.2724 0.0180  0.0267  0.0145  68  PHE B CD2 
4635 C CE1 . PHE B 82  ? 0.2809 0.3320 0.2977 0.0163  0.0263  0.0147  68  PHE B CE1 
4636 C CE2 . PHE B 82  ? 0.2451 0.2955 0.2653 0.0189  0.0263  0.0113  68  PHE B CE2 
4637 C CZ  . PHE B 82  ? 0.2806 0.3293 0.2956 0.0179  0.0260  0.0114  68  PHE B CZ  
4638 N N   . ALA B 83  ? 0.2019 0.2557 0.2411 0.0128  0.0185  0.0178  69  ALA B N   
4639 C CA  . ALA B 83  ? 0.1915 0.2437 0.2326 0.0132  0.0164  0.0165  69  ALA B CA  
4640 C C   . ALA B 83  ? 0.2145 0.2622 0.2494 0.0150  0.0166  0.0126  69  ALA B C   
4641 O O   . ALA B 83  ? 0.2104 0.2558 0.2398 0.0154  0.0175  0.0109  69  ALA B O   
4642 C CB  . ALA B 83  ? 0.1892 0.2381 0.2316 0.0101  0.0120  0.0176  69  ALA B CB  
4643 N N   . ALA B 84  ? 0.1671 0.2135 0.2032 0.0159  0.0154  0.0114  70  ALA B N   
4644 C CA  . ALA B 84  ? 0.2012 0.2434 0.2321 0.0173  0.0155  0.0080  70  ALA B CA  
4645 C C   . ALA B 84  ? 0.2100 0.2487 0.2410 0.0163  0.0123  0.0074  70  ALA B C   
4646 O O   . ALA B 84  ? 0.1983 0.2387 0.2343 0.0158  0.0106  0.0092  70  ALA B O   
4647 C CB  . ALA B 84  ? 0.1958 0.2397 0.2264 0.0203  0.0186  0.0068  70  ALA B CB  
4648 N N   . LEU B 85  ? 0.1965 0.2303 0.2221 0.0160  0.0114  0.0050  71  LEU B N   
4649 C CA  . LEU B 85  ? 0.1877 0.2173 0.2115 0.0151  0.0089  0.0041  71  LEU B CA  
4650 C C   . LEU B 85  ? 0.2057 0.2330 0.2262 0.0166  0.0098  0.0016  71  LEU B C   
4651 O O   . LEU B 85  ? 0.1956 0.2225 0.2130 0.0173  0.0114  0.0002  71  LEU B O   
4652 C CB  . LEU B 85  ? 0.2073 0.2329 0.2273 0.0132  0.0074  0.0037  71  LEU B CB  
4653 C CG  . LEU B 85  ? 0.1926 0.2130 0.2084 0.0126  0.0058  0.0022  71  LEU B CG  
4654 C CD1 . LEU B 85  ? 0.1964 0.2148 0.2132 0.0111  0.0029  0.0035  71  LEU B CD1 
4655 C CD2 . LEU B 85  ? 0.1972 0.2145 0.2090 0.0119  0.0061  0.0014  71  LEU B CD2 
4656 N N   . LEU B 86  ? 0.2161 0.2415 0.2373 0.0170  0.0084  0.0014  72  LEU B N   
4657 C CA  . LEU B 86  ? 0.2109 0.2331 0.2288 0.0179  0.0087  -0.0006 72  LEU B CA  
4658 C C   . LEU B 86  ? 0.2080 0.2257 0.2228 0.0163  0.0064  -0.0009 72  LEU B C   
4659 O O   . LEU B 86  ? 0.2099 0.2267 0.2262 0.0154  0.0042  0.0004  72  LEU B O   
4660 C CB  . LEU B 86  ? 0.2132 0.2366 0.2339 0.0202  0.0095  -0.0006 72  LEU B CB  
4661 C CG  . LEU B 86  ? 0.2263 0.2451 0.2437 0.0209  0.0090  -0.0024 72  LEU B CG  
4662 C CD1 . LEU B 86  ? 0.2170 0.2342 0.2299 0.0212  0.0107  -0.0046 72  LEU B CD1 
4663 C CD2 . LEU B 86  ? 0.2388 0.2578 0.2596 0.0232  0.0091  -0.0018 72  LEU B CD2 
4664 N N   . THR B 87  ? 0.1917 0.2068 0.2023 0.0158  0.0070  -0.0025 73  THR B N   
4665 C CA  . THR B 87  ? 0.1952 0.2061 0.2024 0.0145  0.0057  -0.0028 73  THR B CA  
4666 C C   . THR B 87  ? 0.2095 0.2184 0.2145 0.0148  0.0063  -0.0041 73  THR B C   
4667 O O   . THR B 87  ? 0.2084 0.2185 0.2139 0.0159  0.0074  -0.0051 73  THR B O   
4668 C CB  . THR B 87  ? 0.1984 0.2080 0.2029 0.0132  0.0060  -0.0029 73  THR B CB  
4669 O OG1 . THR B 87  ? 0.1936 0.2047 0.1975 0.0136  0.0078  -0.0038 73  THR B OG1 
4670 C CG2 . THR B 87  ? 0.1867 0.1975 0.1930 0.0127  0.0052  -0.0016 73  THR B CG2 
4671 N N   . THR B 88  ? 0.2019 0.2071 0.2040 0.0137  0.0053  -0.0041 74  THR B N   
4672 C CA  . THR B 88  ? 0.2002 0.2033 0.2002 0.0134  0.0057  -0.0050 74  THR B CA  
4673 C C   . THR B 88  ? 0.2184 0.2218 0.2165 0.0122  0.0070  -0.0053 74  THR B C   
4674 O O   . THR B 88  ? 0.2193 0.2229 0.2165 0.0118  0.0076  -0.0048 74  THR B O   
4675 C CB  . THR B 88  ? 0.2282 0.2273 0.2264 0.0128  0.0041  -0.0044 74  THR B CB  
4676 O OG1 . THR B 88  ? 0.2517 0.2486 0.2486 0.0126  0.0042  -0.0051 74  THR B OG1 
4677 C CG2 . THR B 88  ? 0.2052 0.2017 0.1998 0.0112  0.0037  -0.0037 74  THR B CG2 
4678 N N   . PHE B 89  ? 0.2224 0.2256 0.2201 0.0118  0.0075  -0.0059 75  PHE B N   
4679 C CA  . PHE B 89  ? 0.2189 0.2235 0.2163 0.0107  0.0087  -0.0058 75  PHE B CA  
4680 C C   . PHE B 89  ? 0.1913 0.1945 0.1868 0.0100  0.0096  -0.0049 75  PHE B C   
4681 O O   . PHE B 89  ? 0.1950 0.1948 0.1880 0.0094  0.0090  -0.0044 75  PHE B O   
4682 C CB  . PHE B 89  ? 0.2248 0.2284 0.2219 0.0096  0.0081  -0.0061 75  PHE B CB  
4683 C CG  . PHE B 89  ? 0.2156 0.2218 0.2139 0.0084  0.0089  -0.0055 75  PHE B CG  
4684 C CD1 . PHE B 89  ? 0.2161 0.2252 0.2159 0.0085  0.0088  -0.0059 75  PHE B CD1 
4685 C CD2 . PHE B 89  ? 0.2056 0.2114 0.2037 0.0070  0.0098  -0.0043 75  PHE B CD2 
4686 C CE1 . PHE B 89  ? 0.2174 0.2295 0.2194 0.0072  0.0089  -0.0049 75  PHE B CE1 
4687 C CE2 . PHE B 89  ? 0.2315 0.2407 0.2322 0.0059  0.0106  -0.0032 75  PHE B CE2 
4688 C CZ  . PHE B 89  ? 0.2068 0.2194 0.2098 0.0060  0.0099  -0.0035 75  PHE B CZ  
4689 N N   . GLY B 90  ? 0.2105 0.2159 0.2067 0.0103  0.0111  -0.0046 76  GLY B N   
4690 C CA  . GLY B 90  ? 0.1922 0.1961 0.1862 0.0101  0.0127  -0.0039 76  GLY B CA  
4691 C C   . GLY B 90  ? 0.1881 0.1882 0.1784 0.0104  0.0123  -0.0040 76  GLY B C   
4692 O O   . GLY B 90  ? 0.2001 0.2002 0.1901 0.0112  0.0128  -0.0041 76  GLY B O   
4693 N N   . VAL B 91  ? 0.1958 0.1921 0.1831 0.0096  0.0108  -0.0038 77  VAL B N   
4694 C CA  . VAL B 91  ? 0.2106 0.2025 0.1934 0.0094  0.0098  -0.0037 77  VAL B CA  
4695 C C   . VAL B 91  ? 0.2176 0.2105 0.2027 0.0098  0.0079  -0.0038 77  VAL B C   
4696 O O   . VAL B 91  ? 0.2058 0.1961 0.1882 0.0097  0.0074  -0.0038 77  VAL B O   
4697 C CB  . VAL B 91  ? 0.2117 0.1994 0.1908 0.0082  0.0082  -0.0031 77  VAL B CB  
4698 C CG1 . VAL B 91  ? 0.2101 0.1967 0.1865 0.0075  0.0106  -0.0026 77  VAL B CG1 
4699 C CG2 . VAL B 91  ? 0.2003 0.1893 0.1830 0.0083  0.0059  -0.0029 77  VAL B CG2 
4700 N N   . GLY B 92  ? 0.2044 0.2007 0.1940 0.0103  0.0068  -0.0038 78  GLY B N   
4701 C CA  . GLY B 92  ? 0.2040 0.2022 0.1967 0.0107  0.0054  -0.0034 78  GLY B CA  
4702 C C   . GLY B 92  ? 0.1836 0.1845 0.1780 0.0113  0.0068  -0.0036 78  GLY B C   
4703 O O   . GLY B 92  ? 0.1835 0.1830 0.1770 0.0109  0.0060  -0.0032 78  GLY B O   
4704 N N   . GLU B 93  ? 0.1859 0.1900 0.1823 0.0119  0.0085  -0.0041 79  GLU B N   
4705 C CA  . GLU B 93  ? 0.1744 0.1813 0.1727 0.0126  0.0095  -0.0040 79  GLU B CA  
4706 C C   . GLU B 93  ? 0.1975 0.2020 0.1933 0.0127  0.0105  -0.0039 79  GLU B C   
4707 O O   . GLU B 93  ? 0.2011 0.2058 0.1975 0.0130  0.0104  -0.0035 79  GLU B O   
4708 C CB  . GLU B 93  ? 0.1933 0.2037 0.1936 0.0130  0.0106  -0.0044 79  GLU B CB  
4709 C CG  . GLU B 93  ? 0.1907 0.2009 0.1902 0.0126  0.0118  -0.0044 79  GLU B CG  
4710 C CD  . GLU B 93  ? 0.2064 0.2199 0.2081 0.0125  0.0118  -0.0046 79  GLU B CD  
4711 O OE1 . GLU B 93  ? 0.1971 0.2133 0.2004 0.0130  0.0120  -0.0043 79  GLU B OE1 
4712 O OE2 . GLU B 93  ? 0.1877 0.2004 0.1890 0.0116  0.0114  -0.0048 79  GLU B OE2 
4713 N N   . LEU B 94  ? 0.2066 0.2084 0.1993 0.0126  0.0117  -0.0042 80  LEU B N   
4714 C CA  . LEU B 94  ? 0.1858 0.1847 0.1755 0.0132  0.0133  -0.0043 80  LEU B CA  
4715 C C   . LEU B 94  ? 0.2002 0.1936 0.1855 0.0126  0.0116  -0.0044 80  LEU B C   
4716 O O   . LEU B 94  ? 0.1972 0.1875 0.1802 0.0132  0.0122  -0.0046 80  LEU B O   
4717 C CB  . LEU B 94  ? 0.1896 0.1876 0.1773 0.0135  0.0157  -0.0043 80  LEU B CB  
4718 C CG  . LEU B 94  ? 0.2141 0.2176 0.2067 0.0140  0.0173  -0.0037 80  LEU B CG  
4719 C CD1 . LEU B 94  ? 0.1892 0.1922 0.1804 0.0144  0.0202  -0.0031 80  LEU B CD1 
4720 C CD2 . LEU B 94  ? 0.2132 0.2202 0.2096 0.0151  0.0175  -0.0033 80  LEU B CD2 
4721 N N   . SER B 95  ? 0.2017 0.1933 0.1857 0.0113  0.0092  -0.0043 81  SER B N   
4722 C CA  . SER B 95  ? 0.2024 0.1890 0.1827 0.0101  0.0067  -0.0041 81  SER B CA  
4723 C C   . SER B 95  ? 0.2064 0.1950 0.1904 0.0099  0.0053  -0.0034 81  SER B C   
4724 O O   . SER B 95  ? 0.1936 0.1776 0.1744 0.0090  0.0037  -0.0033 81  SER B O   
4725 C CB  . SER B 95  ? 0.1934 0.1785 0.1727 0.0088  0.0039  -0.0035 81  SER B CB  
4726 O OG  . SER B 95  ? 0.1914 0.1721 0.1649 0.0085  0.0047  -0.0039 81  SER B OG  
4727 N N   . ALA B 96  ? 0.2071 0.2019 0.1971 0.0106  0.0060  -0.0029 82  ALA B N   
4728 C CA  . ALA B 96  ? 0.1989 0.1964 0.1927 0.0103  0.0050  -0.0018 82  ALA B CA  
4729 C C   . ALA B 96  ? 0.1932 0.1913 0.1874 0.0113  0.0068  -0.0018 82  ALA B C   
4730 O O   . ALA B 96  ? 0.1882 0.1881 0.1850 0.0109  0.0061  -0.0007 82  ALA B O   
4731 C CB  . ALA B 96  ? 0.2043 0.2079 0.2036 0.0106  0.0049  -0.0011 82  ALA B CB  
4732 N N   . MET B 97  ? 0.2118 0.2085 0.2037 0.0126  0.0090  -0.0027 83  MET B N   
4733 C CA  . MET B 97  ? 0.2142 0.2127 0.2078 0.0140  0.0107  -0.0024 83  MET B CA  
4734 C C   . MET B 97  ? 0.2281 0.2226 0.2201 0.0137  0.0097  -0.0019 83  MET B C   
4735 O O   . MET B 97  ? 0.2281 0.2251 0.2230 0.0141  0.0098  -0.0008 83  MET B O   
4736 C CB  . MET B 97  ? 0.2225 0.2205 0.2148 0.0155  0.0133  -0.0031 83  MET B CB  
4737 C CG  . MET B 97  ? 0.3108 0.3088 0.3041 0.0172  0.0150  -0.0026 83  MET B CG  
4738 S SD  . MET B 97  ? 0.4629 0.4658 0.4594 0.0187  0.0177  -0.0024 83  MET B SD  
4739 C CE  . MET B 97  ? 0.2935 0.3027 0.2942 0.0172  0.0161  -0.0020 83  MET B CE  
4740 N N   . ASN B 98  ? 0.1957 0.1833 0.1825 0.0129  0.0085  -0.0025 84  ASN B N   
4741 C CA  . ASN B 98  ? 0.2152 0.1977 0.1997 0.0123  0.0070  -0.0020 84  ASN B CA  
4742 C C   . ASN B 98  ? 0.1992 0.1852 0.1882 0.0103  0.0045  -0.0002 84  ASN B C   
4743 O O   . ASN B 98  ? 0.2067 0.1915 0.1965 0.0099  0.0039  0.0009  84  ASN B O   
4744 C CB  . ASN B 98  ? 0.2187 0.1920 0.1954 0.0114  0.0057  -0.0032 84  ASN B CB  
4745 C CG  . ASN B 98  ? 0.2521 0.2182 0.2250 0.0108  0.0043  -0.0031 84  ASN B CG  
4746 O OD1 . ASN B 98  ? 0.2487 0.2137 0.2218 0.0128  0.0062  -0.0032 84  ASN B OD1 
4747 N ND2 . ASN B 98  ? 0.2122 0.1732 0.1818 0.0080  0.0005  -0.0028 84  ASN B ND2 
4748 N N   . GLY B 99  ? 0.1972 0.1874 0.1893 0.0090  0.0032  0.0004  85  GLY B N   
4749 C CA  . GLY B 99  ? 0.2029 0.1977 0.2003 0.0076  0.0017  0.0025  85  GLY B CA  
4750 C C   . GLY B 99  ? 0.2140 0.2146 0.2155 0.0088  0.0037  0.0034  85  GLY B C   
4751 O O   . GLY B 99  ? 0.2151 0.2164 0.2185 0.0079  0.0031  0.0051  85  GLY B O   
4752 N N   . ILE B 100 ? 0.2158 0.2201 0.2182 0.0105  0.0059  0.0024  86  ILE B N   
4753 C CA  . ILE B 100 ? 0.1939 0.2033 0.1992 0.0115  0.0075  0.0031  86  ILE B CA  
4754 C C   . ILE B 100 ? 0.2097 0.2166 0.2139 0.0122  0.0078  0.0038  86  ILE B C   
4755 O O   . ILE B 100 ? 0.2002 0.2096 0.2064 0.0119  0.0079  0.0054  86  ILE B O   
4756 C CB  . ILE B 100 ? 0.1770 0.1896 0.1827 0.0128  0.0090  0.0018  86  ILE B CB  
4757 C CG1 . ILE B 100 ? 0.1773 0.1923 0.1846 0.0124  0.0087  0.0015  86  ILE B CG1 
4758 C CG2 . ILE B 100 ? 0.2232 0.2397 0.2304 0.0137  0.0102  0.0025  86  ILE B CG2 
4759 C CD1 . ILE B 100 ? 0.1894 0.2086 0.2001 0.0120  0.0087  0.0031  86  ILE B CD1 
4760 N N   . ALA B 101 ? 0.2101 0.2119 0.2109 0.0132  0.0083  0.0026  87  ALA B N   
4761 C CA  . ALA B 101 ? 0.2121 0.2109 0.2119 0.0143  0.0088  0.0031  87  ALA B CA  
4762 C C   . ALA B 101 ? 0.2235 0.2190 0.2229 0.0126  0.0068  0.0047  87  ALA B C   
4763 O O   . ALA B 101 ? 0.2011 0.1971 0.2019 0.0129  0.0068  0.0063  87  ALA B O   
4764 C CB  . ALA B 101 ? 0.2238 0.2169 0.2195 0.0160  0.0101  0.0015  87  ALA B CB  
4765 N N   . GLY B 102 ? 0.2245 0.2163 0.2220 0.0105  0.0047  0.0046  88  GLY B N   
4766 C CA  . GLY B 102 ? 0.2171 0.2061 0.2149 0.0083  0.0024  0.0064  88  GLY B CA  
4767 C C   . GLY B 102 ? 0.2133 0.2094 0.2166 0.0071  0.0023  0.0090  88  GLY B C   
4768 O O   . GLY B 102 ? 0.2236 0.2187 0.2279 0.0059  0.0013  0.0111  88  GLY B O   
4769 N N   . SER B 103 ? 0.2071 0.2101 0.2136 0.0075  0.0035  0.0089  89  SER B N   
4770 C CA  . SER B 103 ? 0.2153 0.2250 0.2261 0.0070  0.0043  0.0110  89  SER B CA  
4771 C C   . SER B 103 ? 0.2173 0.2284 0.2277 0.0084  0.0058  0.0117  89  SER B C   
4772 O O   . SER B 103 ? 0.2091 0.2223 0.2213 0.0075  0.0057  0.0141  89  SER B O   
4773 C CB  . SER B 103 ? 0.2089 0.2244 0.2222 0.0076  0.0056  0.0103  89  SER B CB  
4774 O OG  . SER B 103 ? 0.2085 0.2228 0.2227 0.0063  0.0038  0.0102  89  SER B OG  
4775 N N   . TYR B 104 ? 0.2203 0.2305 0.2288 0.0106  0.0069  0.0099  90  TYR B N   
4776 C CA  . TYR B 104 ? 0.2091 0.2205 0.2176 0.0119  0.0077  0.0108  90  TYR B CA  
4777 C C   . TYR B 104 ? 0.2168 0.2229 0.2242 0.0116  0.0065  0.0124  90  TYR B C   
4778 O O   . TYR B 104 ? 0.2124 0.2201 0.2208 0.0112  0.0063  0.0147  90  TYR B O   
4779 C CB  . TYR B 104 ? 0.2103 0.2221 0.2180 0.0141  0.0089  0.0089  90  TYR B CB  
4780 C CG  . TYR B 104 ? 0.2184 0.2326 0.2270 0.0154  0.0092  0.0102  90  TYR B CG  
4781 C CD1 . TYR B 104 ? 0.2338 0.2445 0.2422 0.0166  0.0089  0.0111  90  TYR B CD1 
4782 C CD2 . TYR B 104 ? 0.2347 0.2542 0.2440 0.0153  0.0096  0.0105  90  TYR B CD2 
4783 C CE1 . TYR B 104 ? 0.2266 0.2397 0.2364 0.0178  0.0088  0.0127  90  TYR B CE1 
4784 C CE2 . TYR B 104 ? 0.2302 0.2516 0.2399 0.0161  0.0092  0.0119  90  TYR B CE2 
4785 C CZ  . TYR B 104 ? 0.2526 0.2711 0.2630 0.0174  0.0087  0.0132  90  TYR B CZ  
4786 O OH  . TYR B 104 ? 0.2753 0.2959 0.2868 0.0183  0.0080  0.0150  90  TYR B OH  
4787 N N   . ALA B 105 ? 0.2317 0.2310 0.2365 0.0116  0.0057  0.0112  91  ALA B N   
4788 C CA  . ALA B 105 ? 0.2364 0.2291 0.2393 0.0115  0.0045  0.0124  91  ALA B CA  
4789 C C   . ALA B 105 ? 0.2272 0.2203 0.2317 0.0086  0.0027  0.0153  91  ALA B C   
4790 O O   . ALA B 105 ? 0.2639 0.2548 0.2684 0.0084  0.0020  0.0173  91  ALA B O   
4791 C CB  . ALA B 105 ? 0.2242 0.2084 0.2225 0.0118  0.0038  0.0102  91  ALA B CB  
4792 N N   . GLU B 106 ? 0.2314 0.2276 0.2379 0.0062  0.0019  0.0158  92  GLU B N   
4793 C CA  . GLU B 106 ? 0.2437 0.2408 0.2527 0.0031  0.0002  0.0189  92  GLU B CA  
4794 C C   . GLU B 106 ? 0.2210 0.2273 0.2342 0.0026  0.0020  0.0210  92  GLU B C   
4795 O O   . GLU B 106 ? 0.2249 0.2339 0.2414 0.0000  0.0012  0.0237  92  GLU B O   
4796 C CB  . GLU B 106 ? 0.2265 0.2200 0.2352 0.0004  -0.0024 0.0187  92  GLU B CB  
4797 C CG  . GLU B 106 ? 0.2420 0.2254 0.2447 0.0010  -0.0039 0.0161  92  GLU B CG  
4798 C CD  . GLU B 106 ? 0.2812 0.2574 0.2821 -0.0026 -0.0078 0.0174  92  GLU B CD  
4799 O OE1 . GLU B 106 ? 0.2619 0.2424 0.2674 -0.0059 -0.0096 0.0200  92  GLU B OE1 
4800 O OE2 . GLU B 106 ? 0.2728 0.2389 0.2675 -0.0022 -0.0091 0.0157  92  GLU B OE2 
4801 N N   . HIS B 107 ? 0.2095 0.2203 0.2225 0.0050  0.0043  0.0198  93  HIS B N   
4802 C CA  . HIS B 107 ? 0.2240 0.2421 0.2390 0.0050  0.0062  0.0214  93  HIS B CA  
4803 C C   . HIS B 107 ? 0.2296 0.2528 0.2483 0.0037  0.0069  0.0221  93  HIS B C   
4804 O O   . HIS B 107 ? 0.2096 0.2369 0.2312 0.0022  0.0077  0.0250  93  HIS B O   
4805 C CB  . HIS B 107 ? 0.2147 0.2326 0.2296 0.0039  0.0060  0.0248  93  HIS B CB  
4806 C CG  . HIS B 107 ? 0.2503 0.2646 0.2624 0.0057  0.0056  0.0246  93  HIS B CG  
4807 N ND1 . HIS B 107 ? 0.2254 0.2429 0.2363 0.0068  0.0066  0.0257  93  HIS B ND1 
4808 C CD2 . HIS B 107 ? 0.2462 0.2537 0.2565 0.0068  0.0042  0.0235  93  HIS B CD2 
4809 C CE1 . HIS B 107 ? 0.2616 0.2752 0.2710 0.0083  0.0056  0.0257  93  HIS B CE1 
4810 N NE2 . HIS B 107 ? 0.2490 0.2567 0.2582 0.0086  0.0044  0.0243  93  HIS B NE2 
4811 N N   . VAL B 108 ? 0.2247 0.2479 0.2435 0.0046  0.0069  0.0195  94  VAL B N   
4812 C CA  . VAL B 108 ? 0.1895 0.2174 0.2121 0.0040  0.0075  0.0198  94  VAL B CA  
4813 C C   . VAL B 108 ? 0.2007 0.2323 0.2224 0.0065  0.0100  0.0176  94  VAL B C   
4814 O O   . VAL B 108 ? 0.1927 0.2216 0.2116 0.0080  0.0097  0.0147  94  VAL B O   
4815 C CB  . VAL B 108 ? 0.1942 0.2183 0.2175 0.0026  0.0048  0.0190  94  VAL B CB  
4816 C CG1 . VAL B 108 ? 0.1871 0.2168 0.2155 0.0022  0.0051  0.0200  94  VAL B CG1 
4817 C CG2 . VAL B 108 ? 0.1910 0.2099 0.2140 -0.0001 0.0018  0.0209  94  VAL B CG2 
4818 N N   . PRO B 109 ? 0.1858 0.2231 0.2094 0.0071  0.0124  0.0188  95  PRO B N   
4819 C CA  . PRO B 109 ? 0.2133 0.2526 0.2346 0.0095  0.0147  0.0164  95  PRO B CA  
4820 C C   . PRO B 109 ? 0.2106 0.2507 0.2339 0.0104  0.0146  0.0146  95  PRO B C   
4821 O O   . PRO B 109 ? 0.2135 0.2578 0.2405 0.0109  0.0162  0.0157  95  PRO B O   
4822 C CB  . PRO B 109 ? 0.2360 0.2802 0.2577 0.0099  0.0176  0.0185  95  PRO B CB  
4823 C CG  . PRO B 109 ? 0.2206 0.2674 0.2477 0.0078  0.0173  0.0220  95  PRO B CG  
4824 C CD  . PRO B 109 ? 0.2088 0.2504 0.2361 0.0057  0.0136  0.0224  95  PRO B CD  
4825 N N   . VAL B 110 ? 0.2078 0.2437 0.2289 0.0107  0.0130  0.0121  96  VAL B N   
4826 C CA  . VAL B 110 ? 0.2056 0.2412 0.2276 0.0116  0.0127  0.0103  96  VAL B CA  
4827 C C   . VAL B 110 ? 0.1999 0.2346 0.2180 0.0134  0.0139  0.0076  96  VAL B C   
4828 O O   . VAL B 110 ? 0.2221 0.2544 0.2370 0.0135  0.0134  0.0065  96  VAL B O   
4829 C CB  . VAL B 110 ? 0.2096 0.2406 0.2311 0.0103  0.0098  0.0097  96  VAL B CB  
4830 C CG1 . VAL B 110 ? 0.1632 0.1932 0.1844 0.0112  0.0094  0.0078  96  VAL B CG1 
4831 C CG2 . VAL B 110 ? 0.1895 0.2208 0.2148 0.0080  0.0078  0.0125  96  VAL B CG2 
4832 N N   . LEU B 111 ? 0.2040 0.2407 0.2229 0.0149  0.0153  0.0066  97  LEU B N   
4833 C CA  . LEU B 111 ? 0.2067 0.2418 0.2217 0.0163  0.0161  0.0040  97  LEU B CA  
4834 C C   . LEU B 111 ? 0.2048 0.2370 0.2198 0.0163  0.0145  0.0024  97  LEU B C   
4835 O O   . LEU B 111 ? 0.2041 0.2369 0.2222 0.0165  0.0140  0.0029  97  LEU B O   
4836 C CB  . LEU B 111 ? 0.1721 0.2096 0.1866 0.0182  0.0187  0.0036  97  LEU B CB  
4837 C CG  . LEU B 111 ? 0.1842 0.2189 0.1941 0.0194  0.0190  0.0008  97  LEU B CG  
4838 C CD1 . LEU B 111 ? 0.1968 0.2301 0.2017 0.0188  0.0187  0.0001  97  LEU B CD1 
4839 C CD2 . LEU B 111 ? 0.2150 0.2506 0.2248 0.0217  0.0215  0.0000  97  LEU B CD2 
4840 N N   . HIS B 112 ? 0.1905 0.2197 0.2024 0.0159  0.0136  0.0009  98  HIS B N   
4841 C CA  . HIS B 112 ? 0.1798 0.2060 0.1909 0.0157  0.0124  -0.0005 98  HIS B CA  
4842 C C   . HIS B 112 ? 0.2000 0.2255 0.2090 0.0168  0.0131  -0.0023 98  HIS B C   
4843 O O   . HIS B 112 ? 0.2040 0.2291 0.2104 0.0167  0.0132  -0.0032 98  HIS B O   
4844 C CB  . HIS B 112 ? 0.1863 0.2099 0.1956 0.0149  0.0115  -0.0007 98  HIS B CB  
4845 C CG  . HIS B 112 ? 0.1854 0.2057 0.1936 0.0144  0.0105  -0.0016 98  HIS B CG  
4846 N ND1 . HIS B 112 ? 0.1579 0.1755 0.1642 0.0140  0.0103  -0.0019 98  HIS B ND1 
4847 C CD2 . HIS B 112 ? 0.2057 0.2248 0.2142 0.0145  0.0098  -0.0021 98  HIS B CD2 
4848 C CE1 . HIS B 112 ? 0.2068 0.2217 0.2117 0.0136  0.0097  -0.0025 98  HIS B CE1 
4849 N NE2 . HIS B 112 ? 0.2036 0.2191 0.2097 0.0138  0.0091  -0.0026 98  HIS B NE2 
4850 N N   . ILE B 113 ? 0.1777 0.2028 0.1878 0.0177  0.0132  -0.0028 99  ILE B N   
4851 C CA  . ILE B 113 ? 0.1967 0.2195 0.2043 0.0186  0.0135  -0.0047 99  ILE B CA  
4852 C C   . ILE B 113 ? 0.1950 0.2146 0.2019 0.0176  0.0118  -0.0053 99  ILE B C   
4853 O O   . ILE B 113 ? 0.1967 0.2156 0.2054 0.0173  0.0108  -0.0044 99  ILE B O   
4854 C CB  . ILE B 113 ? 0.1915 0.2153 0.2007 0.0207  0.0149  -0.0047 99  ILE B CB  
4855 C CG1 . ILE B 113 ? 0.1827 0.2102 0.1926 0.0217  0.0172  -0.0038 99  ILE B CG1 
4856 C CG2 . ILE B 113 ? 0.1869 0.2070 0.1925 0.0218  0.0152  -0.0070 99  ILE B CG2 
4857 C CD1 . ILE B 113 ? 0.2062 0.2362 0.2197 0.0240  0.0192  -0.0029 99  ILE B CD1 
4858 N N   . VAL B 114 ? 0.1958 0.2133 0.1998 0.0170  0.0115  -0.0065 100 VAL B N   
4859 C CA  . VAL B 114 ? 0.1781 0.1927 0.1812 0.0159  0.0103  -0.0068 100 VAL B CA  
4860 C C   . VAL B 114 ? 0.1830 0.1947 0.1841 0.0162  0.0100  -0.0082 100 VAL B C   
4861 O O   . VAL B 114 ? 0.2121 0.2232 0.2110 0.0158  0.0099  -0.0092 100 VAL B O   
4862 C CB  . VAL B 114 ? 0.1960 0.2110 0.1984 0.0145  0.0102  -0.0065 100 VAL B CB  
4863 C CG1 . VAL B 114 ? 0.1881 0.2004 0.1895 0.0134  0.0096  -0.0065 100 VAL B CG1 
4864 C CG2 . VAL B 114 ? 0.1860 0.2027 0.1897 0.0144  0.0106  -0.0053 100 VAL B CG2 
4865 N N   . GLY B 115 ? 0.1953 0.2047 0.1970 0.0168  0.0093  -0.0081 101 GLY B N   
4866 C CA  . GLY B 115 ? 0.2178 0.2234 0.2175 0.0171  0.0088  -0.0094 101 GLY B CA  
4867 C C   . GLY B 115 ? 0.2266 0.2299 0.2244 0.0148  0.0077  -0.0093 101 GLY B C   
4868 O O   . GLY B 115 ? 0.1991 0.2025 0.1975 0.0137  0.0074  -0.0082 101 GLY B O   
4869 N N   . ALA B 116 ? 0.2169 0.2178 0.2123 0.0140  0.0071  -0.0104 102 ALA B N   
4870 C CA  . ALA B 116 ? 0.2279 0.2281 0.2226 0.0114  0.0062  -0.0099 102 ALA B CA  
4871 C C   . ALA B 116 ? 0.2513 0.2463 0.2436 0.0105  0.0048  -0.0107 102 ALA B C   
4872 O O   . ALA B 116 ? 0.2340 0.2255 0.2244 0.0121  0.0046  -0.0121 102 ALA B O   
4873 C CB  . ALA B 116 ? 0.2092 0.2125 0.2041 0.0104  0.0062  -0.0099 102 ALA B CB  
4874 N N   . PRO B 117 ? 0.2639 0.2580 0.2563 0.0080  0.0040  -0.0096 103 PRO B N   
4875 C CA  . PRO B 117 ? 0.2944 0.2833 0.2845 0.0065  0.0022  -0.0100 103 PRO B CA  
4876 C C   . PRO B 117 ? 0.2584 0.2452 0.2458 0.0062  0.0011  -0.0117 103 PRO B C   
4877 O O   . PRO B 117 ? 0.2445 0.2349 0.2324 0.0060  0.0013  -0.0119 103 PRO B O   
4878 C CB  . PRO B 117 ? 0.2561 0.2467 0.2478 0.0035  0.0020  -0.0080 103 PRO B CB  
4879 C CG  . PRO B 117 ? 0.2778 0.2729 0.2718 0.0043  0.0040  -0.0068 103 PRO B CG  
4880 C CD  . PRO B 117 ? 0.2442 0.2421 0.2388 0.0065  0.0048  -0.0078 103 PRO B CD  
4881 N N   . GLY B 118 ? 0.2897 0.2699 0.2738 0.0059  -0.0005 -0.0129 104 GLY B N   
4882 C CA  . GLY B 118 ? 0.3078 0.2840 0.2875 0.0056  -0.0018 -0.0150 104 GLY B CA  
4883 C C   . GLY B 118 ? 0.3295 0.3078 0.3096 0.0019  -0.0037 -0.0141 104 GLY B C   
4884 O O   . GLY B 118 ? 0.3173 0.2985 0.3011 -0.0008 -0.0043 -0.0118 104 GLY B O   
4885 N N   . THR B 119 ? 0.3344 0.3112 0.3107 0.0017  -0.0048 -0.0157 105 THR B N   
4886 C CA  . THR B 119 ? 0.3453 0.3253 0.3227 -0.0015 -0.0070 -0.0145 105 THR B CA  
4887 C C   . THR B 119 ? 0.3725 0.3500 0.3508 -0.0057 -0.0099 -0.0131 105 THR B C   
4888 O O   . THR B 119 ? 0.3866 0.3700 0.3702 -0.0084 -0.0106 -0.0104 105 THR B O   
4889 C CB  . THR B 119 ? 0.3647 0.3417 0.3360 -0.0012 -0.0082 -0.0166 105 THR B CB  
4890 O OG1 . THR B 119 ? 0.3712 0.3385 0.3355 -0.0009 -0.0095 -0.0192 105 THR B OG1 
4891 C CG2 . THR B 119 ? 0.3597 0.3401 0.3307 0.0026  -0.0051 -0.0174 105 THR B CG2 
4892 N N   . ALA B 120 ? 0.3954 0.3646 0.3694 -0.0062 -0.0114 -0.0145 106 ALA B N   
4893 C CA  . ALA B 120 ? 0.4159 0.3821 0.3907 -0.0105 -0.0143 -0.0129 106 ALA B CA  
4894 C C   . ALA B 120 ? 0.3929 0.3653 0.3747 -0.0118 -0.0127 -0.0095 106 ALA B C   
4895 O O   . ALA B 120 ? 0.4062 0.3825 0.3923 -0.0156 -0.0141 -0.0068 106 ALA B O   
4896 C CB  . ALA B 120 ? 0.4125 0.3677 0.3811 -0.0102 -0.0158 -0.0150 106 ALA B CB  
4897 N N   . SER B 121 ? 0.3877 0.3613 0.3706 -0.0086 -0.0096 -0.0095 107 SER B N   
4898 C CA  . SER B 121 ? 0.3932 0.3719 0.3812 -0.0094 -0.0077 -0.0066 107 SER B CA  
4899 C C   . SER B 121 ? 0.3555 0.3433 0.3489 -0.0101 -0.0064 -0.0046 107 SER B C   
4900 O O   . SER B 121 ? 0.3343 0.3263 0.3322 -0.0125 -0.0058 -0.0017 107 SER B O   
4901 C CB  . SER B 121 ? 0.3959 0.3741 0.3833 -0.0057 -0.0051 -0.0072 107 SER B CB  
4902 O OG  . SER B 121 ? 0.4889 0.4606 0.4740 -0.0061 -0.0060 -0.0069 107 SER B OG  
4903 N N   . GLN B 122 ? 0.3393 0.3302 0.3326 -0.0079 -0.0056 -0.0059 108 GLN B N   
4904 C CA  . GLN B 122 ? 0.3321 0.3312 0.3305 -0.0082 -0.0045 -0.0041 108 GLN B CA  
4905 C C   . GLN B 122 ? 0.3360 0.3376 0.3375 -0.0122 -0.0074 -0.0021 108 GLN B C   
4906 O O   . GLN B 122 ? 0.3254 0.3335 0.3332 -0.0135 -0.0063 0.0009  108 GLN B O   
4907 C CB  . GLN B 122 ? 0.3182 0.3191 0.3152 -0.0052 -0.0037 -0.0058 108 GLN B CB  
4908 C CG  . GLN B 122 ? 0.2955 0.2958 0.2913 -0.0016 -0.0009 -0.0069 108 GLN B CG  
4909 C CD  . GLN B 122 ? 0.2984 0.3014 0.2937 0.0008  0.0001  -0.0079 108 GLN B CD  
4910 O OE1 . GLN B 122 ? 0.3082 0.3157 0.3058 0.0001  -0.0003 -0.0068 108 GLN B OE1 
4911 N NE2 . GLN B 122 ? 0.2838 0.2845 0.2766 0.0036  0.0014  -0.0095 108 GLN B NE2 
4912 N N   . GLN B 123 ? 0.3577 0.3539 0.3549 -0.0141 -0.0110 -0.0036 109 GLN B N   
4913 C CA  . GLN B 123 ? 0.3816 0.3799 0.3817 -0.0185 -0.0146 -0.0015 109 GLN B CA  
4914 C C   . GLN B 123 ? 0.3502 0.3497 0.3549 -0.0220 -0.0151 0.0016  109 GLN B C   
4915 O O   . GLN B 123 ? 0.3577 0.3634 0.3689 -0.0251 -0.0164 0.0048  109 GLN B O   
4916 C CB  . GLN B 123 ? 0.4138 0.4043 0.4065 -0.0201 -0.0189 -0.0040 109 GLN B CB  
4917 C CG  . GLN B 123 ? 0.4707 0.4567 0.4562 -0.0162 -0.0177 -0.0078 109 GLN B CG  
4918 C CD  . GLN B 123 ? 0.5946 0.5751 0.5730 -0.0176 -0.0215 -0.0098 109 GLN B CD  
4919 O OE1 . GLN B 123 ? 0.7330 0.7074 0.7079 -0.0212 -0.0255 -0.0101 109 GLN B OE1 
4920 N NE2 . GLN B 123 ? 0.6034 0.5854 0.5789 -0.0149 -0.0203 -0.0113 109 GLN B NE2 
4921 N N   . ARG B 124 ? 0.3307 0.3245 0.3324 -0.0217 -0.0141 0.0009  110 ARG B N   
4922 C CA  . ARG B 124 ? 0.3465 0.3411 0.3520 -0.0250 -0.0141 0.0041  110 ARG B CA  
4923 C C   . ARG B 124 ? 0.3408 0.3438 0.3527 -0.0238 -0.0096 0.0070  110 ARG B C   
4924 O O   . ARG B 124 ? 0.3377 0.3427 0.3533 -0.0264 -0.0088 0.0101  110 ARG B O   
4925 C CB  . ARG B 124 ? 0.3595 0.3447 0.3592 -0.0250 -0.0147 0.0026  110 ARG B CB  
4926 C CG  . ARG B 124 ? 0.3831 0.3586 0.3756 -0.0258 -0.0187 -0.0005 110 ARG B CG  
4927 C CD  . ARG B 124 ? 0.4439 0.4105 0.4327 -0.0273 -0.0200 -0.0005 110 ARG B CD  
4928 N NE  . ARG B 124 ? 0.5104 0.4736 0.4959 -0.0227 -0.0172 -0.0025 110 ARG B NE  
4929 C CZ  . ARG B 124 ? 0.6630 0.6186 0.6422 -0.0195 -0.0177 -0.0060 110 ARG B CZ  
4930 N NH1 . ARG B 124 ? 0.5850 0.5344 0.5590 -0.0203 -0.0207 -0.0085 110 ARG B NH1 
4931 N NH2 . ARG B 124 ? 0.6248 0.5791 0.6028 -0.0154 -0.0151 -0.0070 110 ARG B NH2 
4932 N N   . GLY B 125 ? 0.3073 0.3145 0.3199 -0.0198 -0.0065 0.0060  111 GLY B N   
4933 C CA  . GLY B 125 ? 0.2942 0.3080 0.3116 -0.0182 -0.0020 0.0083  111 GLY B CA  
4934 C C   . GLY B 125 ? 0.3112 0.3216 0.3261 -0.0179 0.0004  0.0089  111 GLY B C   
4935 O O   . GLY B 125 ? 0.2968 0.3114 0.3155 -0.0188 0.0032  0.0119  111 GLY B O   
4936 N N   . GLU B 126 ? 0.2876 0.2904 0.2960 -0.0164 -0.0005 0.0062  112 GLU B N   
4937 C CA  . GLU B 126 ? 0.3152 0.3138 0.3206 -0.0164 0.0010  0.0070  112 GLU B CA  
4938 C C   . GLU B 126 ? 0.2826 0.2846 0.2881 -0.0136 0.0052  0.0075  112 GLU B C   
4939 O O   . GLU B 126 ? 0.2510 0.2561 0.2571 -0.0107 0.0066  0.0062  112 GLU B O   
4940 C CB  . GLU B 126 ? 0.3016 0.2915 0.3009 -0.0151 -0.0013 0.0042  112 GLU B CB  
4941 C CG  . GLU B 126 ? 0.3681 0.3530 0.3655 -0.0172 -0.0054 0.0028  112 GLU B CG  
4942 C CD  . GLU B 126 ? 0.4018 0.3773 0.3933 -0.0158 -0.0072 0.0005  112 GLU B CD  
4943 O OE1 . GLU B 126 ? 0.4083 0.3824 0.3975 -0.0120 -0.0058 -0.0013 112 GLU B OE1 
4944 O OE2 . GLU B 126 ? 0.4607 0.4301 0.4501 -0.0186 -0.0101 0.0006  112 GLU B OE2 
4945 N N   . LEU B 127 ? 0.2657 0.2661 0.2697 -0.0146 0.0071  0.0096  113 LEU B N   
4946 C CA  . LEU B 127 ? 0.2739 0.2755 0.2759 -0.0122 0.0109  0.0100  113 LEU B CA  
4947 C C   . LEU B 127 ? 0.2649 0.2601 0.2608 -0.0099 0.0099  0.0076  113 LEU B C   
4948 O O   . LEU B 127 ? 0.2678 0.2582 0.2594 -0.0104 0.0098  0.0084  113 LEU B O   
4949 C CB  . LEU B 127 ? 0.2664 0.2690 0.2688 -0.0145 0.0136  0.0135  113 LEU B CB  
4950 C CG  . LEU B 127 ? 0.2915 0.3015 0.3015 -0.0170 0.0148  0.0165  113 LEU B CG  
4951 C CD1 . LEU B 127 ? 0.3047 0.3161 0.3152 -0.0192 0.0180  0.0204  113 LEU B CD1 
4952 C CD2 . LEU B 127 ? 0.3083 0.3252 0.3226 -0.0143 0.0173  0.0162  113 LEU B CD2 
4953 N N   . LEU B 128 ? 0.2395 0.2351 0.2352 -0.0073 0.0090  0.0051  114 LEU B N   
4954 C CA  . LEU B 128 ? 0.2713 0.2622 0.2631 -0.0050 0.0076  0.0030  114 LEU B CA  
4955 C C   . LEU B 128 ? 0.2511 0.2426 0.2405 -0.0028 0.0098  0.0028  114 LEU B C   
4956 O O   . LEU B 128 ? 0.2450 0.2407 0.2360 -0.0021 0.0124  0.0032  114 LEU B O   
4957 C CB  . LEU B 128 ? 0.2637 0.2548 0.2566 -0.0035 0.0057  0.0005  114 LEU B CB  
4958 C CG  . LEU B 128 ? 0.3208 0.3091 0.3139 -0.0051 0.0029  -0.0002 114 LEU B CG  
4959 C CD1 . LEU B 128 ? 0.3195 0.3070 0.3118 -0.0026 0.0017  -0.0030 114 LEU B CD1 
4960 C CD2 . LEU B 128 ? 0.3336 0.3153 0.3238 -0.0067 0.0011  0.0005  114 LEU B CD2 
4961 N N   . HIS B 129 ? 0.2560 0.2427 0.2415 -0.0018 0.0084  0.0022  115 HIS B N   
4962 C CA  . HIS B 129 ? 0.2523 0.2386 0.2352 0.0001  0.0094  0.0018  115 HIS B CA  
4963 C C   . HIS B 129 ? 0.2511 0.2414 0.2369 0.0021  0.0098  0.0001  115 HIS B C   
4964 O O   . HIS B 129 ? 0.2314 0.2235 0.2202 0.0026  0.0086  -0.0011 115 HIS B O   
4965 C CB  . HIS B 129 ? 0.2696 0.2506 0.2489 0.0006  0.0069  0.0017  115 HIS B CB  
4966 C CG  . HIS B 129 ? 0.2838 0.2642 0.2657 0.0021  0.0044  0.0002  115 HIS B CG  
4967 N ND1 . HIS B 129 ? 0.3093 0.2872 0.2920 0.0015  0.0028  0.0000  115 HIS B ND1 
4968 C CD2 . HIS B 129 ? 0.2785 0.2602 0.2620 0.0043  0.0036  -0.0011 115 HIS B CD2 
4969 C CE1 . HIS B 129 ? 0.3191 0.2967 0.3036 0.0036  0.0014  -0.0015 115 HIS B CE1 
4970 N NE2 . HIS B 129 ? 0.2627 0.2432 0.2482 0.0053  0.0020  -0.0020 115 HIS B NE2 
4971 N N   . HIS B 130 ? 0.2410 0.2321 0.2251 0.0032  0.0116  0.0000  116 HIS B N   
4972 C CA  . HIS B 130 ? 0.2279 0.2225 0.2145 0.0049  0.0123  -0.0011 116 HIS B CA  
4973 C C   . HIS B 130 ? 0.2413 0.2412 0.2325 0.0047  0.0140  -0.0007 116 HIS B C   
4974 O O   . HIS B 130 ? 0.1978 0.2007 0.1917 0.0058  0.0137  -0.0016 116 HIS B O   
4975 C CB  . HIS B 130 ? 0.2048 0.1994 0.1929 0.0062  0.0099  -0.0025 116 HIS B CB  
4976 C CG  . HIS B 130 ? 0.2376 0.2280 0.2230 0.0064  0.0078  -0.0024 116 HIS B CG  
4977 N ND1 . HIS B 130 ? 0.2289 0.2152 0.2095 0.0056  0.0076  -0.0014 116 HIS B ND1 
4978 C CD2 . HIS B 130 ? 0.2434 0.2334 0.2305 0.0075  0.0057  -0.0030 116 HIS B CD2 
4979 C CE1 . HIS B 130 ? 0.2247 0.2084 0.2045 0.0060  0.0049  -0.0013 116 HIS B CE1 
4980 N NE2 . HIS B 130 ? 0.2548 0.2410 0.2391 0.0072  0.0039  -0.0021 116 HIS B NE2 
4981 N N   . THR B 131 ? 0.2421 0.2434 0.2344 0.0032  0.0155  0.0009  117 THR B N   
4982 C CA  . THR B 131 ? 0.2358 0.2429 0.2332 0.0030  0.0171  0.0018  117 THR B CA  
4983 C C   . THR B 131 ? 0.2437 0.2521 0.2406 0.0036  0.0210  0.0034  117 THR B C   
4984 O O   . THR B 131 ? 0.2205 0.2248 0.2121 0.0036  0.0223  0.0036  117 THR B O   
4985 C CB  . THR B 131 ? 0.2482 0.2572 0.2492 0.0006  0.0154  0.0028  117 THR B CB  
4986 O OG1 . THR B 131 ? 0.2727 0.2800 0.2725 -0.0015 0.0161  0.0046  117 THR B OG1 
4987 C CG2 . THR B 131 ? 0.2211 0.2275 0.2213 0.0004  0.0119  0.0009  117 THR B CG2 
4988 N N   . LEU B 132 ? 0.2414 0.2556 0.2437 0.0041  0.0229  0.0045  118 LEU B N   
4989 C CA  . LEU B 132 ? 0.2430 0.2592 0.2458 0.0050  0.0273  0.0063  118 LEU B CA  
4990 C C   . LEU B 132 ? 0.2609 0.2787 0.2655 0.0024  0.0284  0.0089  118 LEU B C   
4991 O O   . LEU B 132 ? 0.2348 0.2551 0.2406 0.0030  0.0326  0.0108  118 LEU B O   
4992 C CB  . LEU B 132 ? 0.2354 0.2574 0.2440 0.0070  0.0291  0.0070  118 LEU B CB  
4993 C CG  . LEU B 132 ? 0.2506 0.2709 0.2576 0.0094  0.0280  0.0048  118 LEU B CG  
4994 C CD1 . LEU B 132 ? 0.2446 0.2704 0.2575 0.0115  0.0301  0.0060  118 LEU B CD1 
4995 C CD2 . LEU B 132 ? 0.2025 0.2158 0.2013 0.0107  0.0289  0.0031  118 LEU B CD2 
4996 N N   . GLY B 133 ? 0.2651 0.2814 0.2700 -0.0003 0.0250  0.0090  119 GLY B N   
4997 C CA  . GLY B 133 ? 0.2732 0.2906 0.2799 -0.0032 0.0257  0.0116  119 GLY B CA  
4998 C C   . GLY B 133 ? 0.2837 0.3088 0.2992 -0.0048 0.0260  0.0142  119 GLY B C   
4999 O O   . GLY B 133 ? 0.2744 0.3022 0.2929 -0.0069 0.0279  0.0173  119 GLY B O   
5000 N N   . ASP B 134 ? 0.2863 0.3153 0.3065 -0.0039 0.0242  0.0134  120 ASP B N   
5001 C CA  . ASP B 134 ? 0.2862 0.3229 0.3153 -0.0055 0.0237  0.0161  120 ASP B CA  
5002 C C   . ASP B 134 ? 0.3128 0.3489 0.3435 -0.0082 0.0182  0.0153  120 ASP B C   
5003 O O   . ASP B 134 ? 0.3281 0.3702 0.3659 -0.0099 0.0166  0.0174  120 ASP B O   
5004 C CB  . ASP B 134 ? 0.3048 0.3468 0.3381 -0.0021 0.0263  0.0164  120 ASP B CB  
5005 C CG  . ASP B 134 ? 0.2901 0.3289 0.3198 0.0003  0.0242  0.0131  120 ASP B CG  
5006 O OD1 . ASP B 134 ? 0.2675 0.3007 0.2918 -0.0005 0.0210  0.0106  120 ASP B OD1 
5007 O OD2 . ASP B 134 ? 0.2739 0.3159 0.3063 0.0030  0.0259  0.0132  120 ASP B OD2 
5008 N N   . GLY B 135 ? 0.2656 0.2946 0.2898 -0.0086 0.0152  0.0125  121 GLY B N   
5009 C CA  . GLY B 135 ? 0.2719 0.2988 0.2958 -0.0105 0.0104  0.0111  121 GLY B CA  
5010 C C   . GLY B 135 ? 0.2880 0.3168 0.3125 -0.0086 0.0089  0.0094  121 GLY B C   
5011 O O   . GLY B 135 ? 0.2696 0.2973 0.2939 -0.0104 0.0050  0.0086  121 GLY B O   
5012 N N   . GLU B 136 ? 0.2650 0.2958 0.2896 -0.0052 0.0116  0.0088  122 GLU B N   
5013 C CA  . GLU B 136 ? 0.2724 0.3055 0.2981 -0.0034 0.0104  0.0077  122 GLU B CA  
5014 C C   . GLU B 136 ? 0.2730 0.3008 0.2924 -0.0011 0.0102  0.0045  122 GLU B C   
5015 O O   . GLU B 136 ? 0.2704 0.2953 0.2866 0.0006  0.0124  0.0037  122 GLU B O   
5016 C CB  . GLU B 136 ? 0.2715 0.3109 0.3027 -0.0012 0.0135  0.0097  122 GLU B CB  
5017 C CG  . GLU B 136 ? 0.3099 0.3497 0.3403 0.0012  0.0128  0.0083  122 GLU B CG  
5018 C CD  . GLU B 136 ? 0.3339 0.3765 0.3670 -0.0005 0.0089  0.0088  122 GLU B CD  
5019 O OE1 . GLU B 136 ? 0.3601 0.4051 0.3968 -0.0037 0.0067  0.0107  122 GLU B OE1 
5020 O OE2 . GLU B 136 ? 0.3019 0.3437 0.3329 0.0010  0.0078  0.0074  122 GLU B OE2 
5021 N N   . PHE B 137 ? 0.2545 0.2810 0.2721 -0.0011 0.0074  0.0028  123 PHE B N   
5022 C CA  . PHE B 137 ? 0.2729 0.2949 0.2851 0.0010  0.0073  0.0002  123 PHE B CA  
5023 C C   . PHE B 137 ? 0.2639 0.2881 0.2765 0.0031  0.0074  -0.0004 123 PHE B C   
5024 O O   . PHE B 137 ? 0.2614 0.2828 0.2705 0.0046  0.0074  -0.0023 123 PHE B O   
5025 C CB  . PHE B 137 ? 0.2675 0.2843 0.2757 -0.0004 0.0045  -0.0016 123 PHE B CB  
5026 C CG  . PHE B 137 ? 0.2788 0.2918 0.2856 -0.0020 0.0045  -0.0012 123 PHE B CG  
5027 C CD1 . PHE B 137 ? 0.2835 0.2975 0.2929 -0.0051 0.0035  0.0008  123 PHE B CD1 
5028 C CD2 . PHE B 137 ? 0.2595 0.2682 0.2628 -0.0004 0.0055  -0.0024 123 PHE B CD2 
5029 C CE1 . PHE B 137 ? 0.2827 0.2931 0.2906 -0.0067 0.0035  0.0015  123 PHE B CE1 
5030 C CE2 . PHE B 137 ? 0.2581 0.2630 0.2598 -0.0019 0.0053  -0.0017 123 PHE B CE2 
5031 C CZ  . PHE B 137 ? 0.2794 0.2849 0.2831 -0.0050 0.0044  0.0001  123 PHE B CZ  
5032 N N   . ARG B 138 ? 0.2639 0.2933 0.2811 0.0033  0.0078  0.0014  124 ARG B N   
5033 C CA  . ARG B 138 ? 0.2817 0.3130 0.2991 0.0051  0.0077  0.0012  124 ARG B CA  
5034 C C   . ARG B 138 ? 0.2722 0.3056 0.2920 0.0075  0.0106  0.0022  124 ARG B C   
5035 O O   . ARG B 138 ? 0.2617 0.2964 0.2820 0.0090  0.0105  0.0024  124 ARG B O   
5036 C CB  . ARG B 138 ? 0.3259 0.3607 0.3461 0.0035  0.0050  0.0026  124 ARG B CB  
5037 C CG  . ARG B 138 ? 0.3978 0.4296 0.4146 0.0009  0.0016  0.0015  124 ARG B CG  
5038 C CD  . ARG B 138 ? 0.6249 0.6588 0.6420 0.0000  -0.0014 0.0023  124 ARG B CD  
5039 N NE  . ARG B 138 ? 0.7506 0.7816 0.7643 -0.0030 -0.0053 0.0016  124 ARG B NE  
5040 C CZ  . ARG B 138 ? 0.6882 0.7128 0.6959 -0.0038 -0.0062 -0.0009 124 ARG B CZ  
5041 N NH1 . ARG B 138 ? 0.5917 0.6127 0.5966 -0.0019 -0.0036 -0.0028 124 ARG B NH1 
5042 N NH2 . ARG B 138 ? 0.6451 0.6664 0.6492 -0.0066 -0.0100 -0.0015 124 ARG B NH2 
5043 N N   . HIS B 139 ? 0.2465 0.2797 0.2672 0.0080  0.0133  0.0029  125 HIS B N   
5044 C CA  . HIS B 139 ? 0.2391 0.2730 0.2608 0.0105  0.0163  0.0036  125 HIS B CA  
5045 C C   . HIS B 139 ? 0.2345 0.2648 0.2522 0.0122  0.0162  0.0019  125 HIS B C   
5046 O O   . HIS B 139 ? 0.2490 0.2803 0.2679 0.0139  0.0168  0.0024  125 HIS B O   
5047 C CB  . HIS B 139 ? 0.2494 0.2815 0.2699 0.0107  0.0193  0.0039  125 HIS B CB  
5048 C CG  . HIS B 139 ? 0.2562 0.2928 0.2818 0.0095  0.0205  0.0064  125 HIS B CG  
5049 N ND1 . HIS B 139 ? 0.2788 0.3218 0.3115 0.0099  0.0209  0.0088  125 HIS B ND1 
5050 C CD2 . HIS B 139 ? 0.2486 0.2845 0.2737 0.0078  0.0216  0.0071  125 HIS B CD2 
5051 C CE1 . HIS B 139 ? 0.2702 0.3167 0.3071 0.0085  0.0223  0.0110  125 HIS B CE1 
5052 N NE2 . HIS B 139 ? 0.2809 0.3230 0.3130 0.0071  0.0228  0.0101  125 HIS B NE2 
5053 N N   . PHE B 140 ? 0.2287 0.2547 0.2419 0.0116  0.0154  0.0001  126 PHE B N   
5054 C CA  . PHE B 140 ? 0.2197 0.2425 0.2296 0.0129  0.0155  -0.0011 126 PHE B CA  
5055 C C   . PHE B 140 ? 0.2258 0.2502 0.2362 0.0131  0.0138  -0.0013 126 PHE B C   
5056 O O   . PHE B 140 ? 0.2044 0.2279 0.2141 0.0143  0.0140  -0.0013 126 PHE B O   
5057 C CB  . PHE B 140 ? 0.1984 0.2170 0.2044 0.0123  0.0150  -0.0023 126 PHE B CB  
5058 C CG  . PHE B 140 ? 0.2095 0.2266 0.2145 0.0114  0.0162  -0.0019 126 PHE B CG  
5059 C CD1 . PHE B 140 ? 0.2078 0.2254 0.2133 0.0123  0.0188  -0.0009 126 PHE B CD1 
5060 C CD2 . PHE B 140 ? 0.2046 0.2196 0.2079 0.0100  0.0150  -0.0024 126 PHE B CD2 
5061 C CE1 . PHE B 140 ? 0.1979 0.2144 0.2022 0.0115  0.0205  -0.0002 126 PHE B CE1 
5062 C CE2 . PHE B 140 ? 0.2160 0.2294 0.2180 0.0090  0.0161  -0.0016 126 PHE B CE2 
5063 C CZ  . PHE B 140 ? 0.2054 0.2198 0.2078 0.0096  0.0190  -0.0004 126 PHE B CZ  
5064 N N   . TYR B 141 ? 0.2296 0.2556 0.2406 0.0119  0.0120  -0.0014 127 TYR B N   
5065 C CA  . TYR B 141 ? 0.2405 0.2681 0.2513 0.0120  0.0106  -0.0013 127 TYR B CA  
5066 C C   . TYR B 141 ? 0.2448 0.2755 0.2588 0.0130  0.0110  0.0005  127 TYR B C   
5067 O O   . TYR B 141 ? 0.2357 0.2663 0.2490 0.0140  0.0109  0.0008  127 TYR B O   
5068 C CB  . TYR B 141 ? 0.2395 0.2674 0.2493 0.0103  0.0086  -0.0018 127 TYR B CB  
5069 C CG  . TYR B 141 ? 0.2671 0.2963 0.2757 0.0102  0.0070  -0.0016 127 TYR B CG  
5070 C CD1 . TYR B 141 ? 0.2742 0.3014 0.2790 0.0109  0.0071  -0.0028 127 TYR B CD1 
5071 C CD2 . TYR B 141 ? 0.2729 0.3053 0.2841 0.0092  0.0053  0.0001  127 TYR B CD2 
5072 C CE1 . TYR B 141 ? 0.2825 0.3104 0.2851 0.0107  0.0059  -0.0026 127 TYR B CE1 
5073 C CE2 . TYR B 141 ? 0.2857 0.3186 0.2947 0.0089  0.0035  0.0004  127 TYR B CE2 
5074 C CZ  . TYR B 141 ? 0.3016 0.3320 0.3057 0.0096  0.0039  -0.0011 127 TYR B CZ  
5075 O OH  . TYR B 141 ? 0.3230 0.3535 0.3239 0.0092  0.0024  -0.0007 127 TYR B OH  
5076 N N   . HIS B 142 ? 0.2440 0.2775 0.2619 0.0129  0.0115  0.0020  128 HIS B N   
5077 C CA  . HIS B 142 ? 0.2558 0.2924 0.2776 0.0143  0.0119  0.0039  128 HIS B CA  
5078 C C   . HIS B 142 ? 0.2319 0.2658 0.2526 0.0165  0.0141  0.0038  128 HIS B C   
5079 O O   . HIS B 142 ? 0.1865 0.2208 0.2080 0.0178  0.0139  0.0047  128 HIS B O   
5080 C CB  . HIS B 142 ? 0.2655 0.3066 0.2929 0.0139  0.0121  0.0060  128 HIS B CB  
5081 C CG  . HIS B 142 ? 0.3171 0.3608 0.3458 0.0113  0.0090  0.0066  128 HIS B CG  
5082 N ND1 . HIS B 142 ? 0.3129 0.3568 0.3397 0.0104  0.0061  0.0066  128 HIS B ND1 
5083 C CD2 . HIS B 142 ? 0.3075 0.3530 0.3386 0.0091  0.0081  0.0073  128 HIS B CD2 
5084 C CE1 . HIS B 142 ? 0.3388 0.3839 0.3661 0.0077  0.0033  0.0070  128 HIS B CE1 
5085 N NE2 . HIS B 142 ? 0.3661 0.4124 0.3964 0.0068  0.0044  0.0076  128 HIS B NE2 
5086 N N   . MET B 143 ? 0.2116 0.2422 0.2300 0.0169  0.0161  0.0026  129 MET B N   
5087 C CA  . MET B 143 ? 0.2226 0.2493 0.2388 0.0188  0.0178  0.0022  129 MET B CA  
5088 C C   . MET B 143 ? 0.2330 0.2571 0.2462 0.0185  0.0163  0.0015  129 MET B C   
5089 O O   . MET B 143 ? 0.2069 0.2280 0.2189 0.0198  0.0169  0.0017  129 MET B O   
5090 C CB  . MET B 143 ? 0.2318 0.2544 0.2446 0.0190  0.0199  0.0012  129 MET B CB  
5091 C CG  . MET B 143 ? 0.2354 0.2606 0.2508 0.0192  0.0221  0.0021  129 MET B CG  
5092 S SD  . MET B 143 ? 0.1716 0.1934 0.1827 0.0177  0.0231  0.0011  129 MET B SD  
5093 C CE  . MET B 143 ? 0.2168 0.2314 0.2215 0.0196  0.0252  -0.0001 129 MET B CE  
5094 N N   . SER B 144 ? 0.2194 0.2442 0.2315 0.0170  0.0145  0.0008  130 SER B N   
5095 C CA  . SER B 144 ? 0.2432 0.2667 0.2535 0.0168  0.0136  0.0007  130 SER B CA  
5096 C C   . SER B 144 ? 0.2524 0.2784 0.2643 0.0172  0.0127  0.0022  130 SER B C   
5097 O O   . SER B 144 ? 0.2657 0.2909 0.2765 0.0170  0.0122  0.0026  130 SER B O   
5098 C CB  . SER B 144 ? 0.2399 0.2632 0.2485 0.0156  0.0127  -0.0005 130 SER B CB  
5099 O OG  . SER B 144 ? 0.3151 0.3366 0.3224 0.0156  0.0124  -0.0005 130 SER B OG  
5100 N N   . GLU B 145 ? 0.2404 0.2698 0.2551 0.0174  0.0122  0.0033  131 GLU B N   
5101 C CA  . GLU B 145 ? 0.2577 0.2894 0.2733 0.0174  0.0108  0.0049  131 GLU B CA  
5102 C C   . GLU B 145 ? 0.2553 0.2852 0.2712 0.0187  0.0112  0.0062  131 GLU B C   
5103 O O   . GLU B 145 ? 0.2409 0.2710 0.2555 0.0183  0.0101  0.0071  131 GLU B O   
5104 C CB  . GLU B 145 ? 0.2734 0.3092 0.2927 0.0171  0.0097  0.0063  131 GLU B CB  
5105 C CG  . GLU B 145 ? 0.3155 0.3540 0.3357 0.0168  0.0074  0.0083  131 GLU B CG  
5106 C CD  . GLU B 145 ? 0.4109 0.4490 0.4328 0.0186  0.0076  0.0102  131 GLU B CD  
5107 O OE1 . GLU B 145 ? 0.5062 0.5429 0.5304 0.0205  0.0095  0.0105  131 GLU B OE1 
5108 O OE2 . GLU B 145 ? 0.4588 0.4973 0.4790 0.0181  0.0060  0.0115  131 GLU B OE2 
5109 N N   . PRO B 146 ? 0.2618 0.2894 0.2788 0.0204  0.0127  0.0064  132 PRO B N   
5110 C CA  . PRO B 146 ? 0.2636 0.2882 0.2803 0.0217  0.0128  0.0075  132 PRO B CA  
5111 C C   . PRO B 146 ? 0.2509 0.2719 0.2642 0.0205  0.0123  0.0070  132 PRO B C   
5112 O O   . PRO B 146 ? 0.2444 0.2632 0.2573 0.0209  0.0117  0.0083  132 PRO B O   
5113 C CB  . PRO B 146 ? 0.2498 0.2717 0.2673 0.0239  0.0150  0.0072  132 PRO B CB  
5114 C CG  . PRO B 146 ? 0.2669 0.2927 0.2873 0.0240  0.0159  0.0071  132 PRO B CG  
5115 C CD  . PRO B 146 ? 0.2573 0.2846 0.2758 0.0214  0.0146  0.0058  132 PRO B CD  
5116 N N   . ILE B 147 ? 0.2297 0.2499 0.2409 0.0191  0.0123  0.0054  133 ILE B N   
5117 C CA  . ILE B 147 ? 0.2328 0.2501 0.2419 0.0180  0.0118  0.0052  133 ILE B CA  
5118 C C   . ILE B 147 ? 0.2388 0.2593 0.2479 0.0165  0.0111  0.0055  133 ILE B C   
5119 O O   . ILE B 147 ? 0.2302 0.2497 0.2386 0.0154  0.0108  0.0054  133 ILE B O   
5120 C CB  . ILE B 147 ? 0.2183 0.2312 0.2251 0.0178  0.0122  0.0036  133 ILE B CB  
5121 C CG1 . ILE B 147 ? 0.2217 0.2366 0.2284 0.0174  0.0127  0.0021  133 ILE B CG1 
5122 C CG2 . ILE B 147 ? 0.2243 0.2328 0.2299 0.0196  0.0134  0.0033  133 ILE B CG2 
5123 C CD1 . ILE B 147 ? 0.2415 0.2517 0.2451 0.0170  0.0129  0.0007  133 ILE B CD1 
5124 N N   . THR B 148 ? 0.2182 0.2425 0.2278 0.0165  0.0109  0.0059  134 THR B N   
5125 C CA  . THR B 148 ? 0.2188 0.2456 0.2273 0.0156  0.0108  0.0061  134 THR B CA  
5126 C C   . THR B 148 ? 0.2439 0.2728 0.2518 0.0156  0.0101  0.0079  134 THR B C   
5127 O O   . THR B 148 ? 0.1930 0.2224 0.2021 0.0163  0.0093  0.0086  134 THR B O   
5128 C CB  . THR B 148 ? 0.2151 0.2430 0.2227 0.0154  0.0111  0.0041  134 THR B CB  
5129 O OG1 . THR B 148 ? 0.2310 0.2598 0.2391 0.0156  0.0106  0.0036  134 THR B OG1 
5130 C CG2 . THR B 148 ? 0.2150 0.2408 0.2229 0.0152  0.0116  0.0029  134 THR B CG2 
5131 N N   . VAL B 149 ? 0.2112 0.2414 0.2173 0.0149  0.0104  0.0088  135 VAL B N   
5132 C CA  . VAL B 149 ? 0.2257 0.2574 0.2299 0.0147  0.0096  0.0104  135 VAL B CA  
5133 C C   . VAL B 149 ? 0.2266 0.2598 0.2279 0.0144  0.0092  0.0091  135 VAL B C   
5134 O O   . VAL B 149 ? 0.2414 0.2754 0.2407 0.0141  0.0077  0.0102  135 VAL B O   
5135 C CB  . VAL B 149 ? 0.2455 0.2778 0.2484 0.0140  0.0103  0.0125  135 VAL B CB  
5136 C CG1 . VAL B 149 ? 0.2754 0.3054 0.2806 0.0139  0.0098  0.0144  135 VAL B CG1 
5137 C CG2 . VAL B 149 ? 0.2350 0.2683 0.2375 0.0137  0.0122  0.0115  135 VAL B CG2 
5138 N N   . ALA B 150 ? 0.2312 0.2640 0.2318 0.0145  0.0101  0.0068  136 ALA B N   
5139 C CA  . ALA B 150 ? 0.2390 0.2718 0.2361 0.0142  0.0095  0.0051  136 ALA B CA  
5140 C C   . ALA B 150 ? 0.2328 0.2645 0.2312 0.0143  0.0100  0.0028  136 ALA B C   
5141 O O   . ALA B 150 ? 0.2153 0.2465 0.2157 0.0148  0.0113  0.0024  136 ALA B O   
5142 C CB  . ALA B 150 ? 0.2166 0.2494 0.2088 0.0142  0.0109  0.0050  136 ALA B CB  
5143 N N   . GLN B 151 ? 0.2303 0.2614 0.2274 0.0137  0.0086  0.0016  137 GLN B N   
5144 C CA  . GLN B 151 ? 0.2514 0.2810 0.2489 0.0137  0.0089  -0.0004 137 GLN B CA  
5145 C C   . GLN B 151 ? 0.2639 0.2920 0.2574 0.0128  0.0074  -0.0018 137 GLN B C   
5146 O O   . GLN B 151 ? 0.2727 0.3012 0.2639 0.0119  0.0056  -0.0010 137 GLN B O   
5147 C CB  . GLN B 151 ? 0.2440 0.2740 0.2459 0.0137  0.0087  -0.0001 137 GLN B CB  
5148 C CG  . GLN B 151 ? 0.2707 0.3026 0.2747 0.0129  0.0069  0.0011  137 GLN B CG  
5149 C CD  . GLN B 151 ? 0.3270 0.3597 0.3355 0.0135  0.0076  0.0019  137 GLN B CD  
5150 O OE1 . GLN B 151 ? 0.3369 0.3720 0.3486 0.0133  0.0066  0.0034  137 GLN B OE1 
5151 N NE2 . GLN B 151 ? 0.2737 0.3044 0.2825 0.0141  0.0092  0.0009  137 GLN B NE2 
5152 N N   . ALA B 152 ? 0.2520 0.2777 0.2443 0.0129  0.0079  -0.0039 138 ALA B N   
5153 C CA  . ALA B 152 ? 0.2679 0.2907 0.2558 0.0118  0.0062  -0.0054 138 ALA B CA  
5154 C C   . ALA B 152 ? 0.2652 0.2860 0.2546 0.0114  0.0061  -0.0068 138 ALA B C   
5155 O O   . ALA B 152 ? 0.2372 0.2578 0.2288 0.0126  0.0078  -0.0072 138 ALA B O   
5156 C CB  . ALA B 152 ? 0.2701 0.2901 0.2512 0.0126  0.0072  -0.0069 138 ALA B CB  
5157 N N   . ILE B 153 ? 0.2738 0.2927 0.2616 0.0096  0.0037  -0.0074 139 ILE B N   
5158 C CA  . ILE B 153 ? 0.2785 0.2939 0.2657 0.0091  0.0034  -0.0090 139 ILE B CA  
5159 C C   . ILE B 153 ? 0.2890 0.2991 0.2689 0.0094  0.0030  -0.0113 139 ILE B C   
5160 O O   . ILE B 153 ? 0.2929 0.3011 0.2684 0.0078  0.0007  -0.0117 139 ILE B O   
5161 C CB  . ILE B 153 ? 0.3031 0.3195 0.2935 0.0066  0.0011  -0.0079 139 ILE B CB  
5162 C CG1 . ILE B 153 ? 0.2845 0.3055 0.2816 0.0070  0.0024  -0.0058 139 ILE B CG1 
5163 C CG2 . ILE B 153 ? 0.3034 0.3152 0.2919 0.0057  0.0004  -0.0095 139 ILE B CG2 
5164 C CD1 . ILE B 153 ? 0.3283 0.3517 0.3297 0.0048  0.0008  -0.0041 139 ILE B CD1 
5165 N N   . LEU B 154 ? 0.2271 0.2345 0.2056 0.0115  0.0052  -0.0129 140 LEU B N   
5166 C CA  . LEU B 154 ? 0.2803 0.2824 0.2516 0.0127  0.0058  -0.0153 140 LEU B CA  
5167 C C   . LEU B 154 ? 0.2791 0.2752 0.2467 0.0109  0.0032  -0.0169 140 LEU B C   
5168 O O   . LEU B 154 ? 0.2502 0.2458 0.2215 0.0101  0.0025  -0.0166 140 LEU B O   
5169 C CB  . LEU B 154 ? 0.2363 0.2383 0.2088 0.0160  0.0093  -0.0159 140 LEU B CB  
5170 C CG  . LEU B 154 ? 0.2507 0.2581 0.2263 0.0175  0.0117  -0.0141 140 LEU B CG  
5171 C CD1 . LEU B 154 ? 0.2031 0.2111 0.1809 0.0205  0.0149  -0.0144 140 LEU B CD1 
5172 C CD2 . LEU B 154 ? 0.2387 0.2460 0.2086 0.0172  0.0118  -0.0141 140 LEU B CD2 
5173 N N   . THR B 155 ? 0.2631 0.2543 0.2230 0.0101  0.0016  -0.0185 141 THR B N   
5174 C CA  . THR B 155 ? 0.2862 0.2702 0.2411 0.0082  -0.0012 -0.0204 141 THR B CA  
5175 C C   . THR B 155 ? 0.2930 0.2693 0.2385 0.0107  0.0004  -0.0236 141 THR B C   
5176 O O   . THR B 155 ? 0.2791 0.2565 0.2218 0.0133  0.0034  -0.0240 141 THR B O   
5177 C CB  . THR B 155 ? 0.3055 0.2892 0.2588 0.0041  -0.0058 -0.0194 141 THR B CB  
5178 O OG1 . THR B 155 ? 0.2815 0.2637 0.2277 0.0042  -0.0063 -0.0200 141 THR B OG1 
5179 C CG2 . THR B 155 ? 0.3111 0.3034 0.2742 0.0023  -0.0067 -0.0160 141 THR B CG2 
5180 N N   . GLU B 156 ? 0.3140 0.2821 0.2543 0.0098  -0.0016 -0.0257 142 GLU B N   
5181 C CA  . GLU B 156 ? 0.3244 0.2835 0.2542 0.0121  -0.0003 -0.0291 142 GLU B CA  
5182 C C   . GLU B 156 ? 0.3286 0.2858 0.2498 0.0114  -0.0011 -0.0298 142 GLU B C   
5183 O O   . GLU B 156 ? 0.3233 0.2759 0.2366 0.0145  0.0021  -0.0320 142 GLU B O   
5184 C CB  . GLU B 156 ? 0.3509 0.3004 0.2760 0.0104  -0.0034 -0.0311 142 GLU B CB  
5185 C CG  . GLU B 156 ? 0.3762 0.3144 0.2891 0.0127  -0.0024 -0.0350 142 GLU B CG  
5186 C CD  . GLU B 156 ? 0.4109 0.3388 0.3191 0.0105  -0.0061 -0.0369 142 GLU B CD  
5187 O OE1 . GLU B 156 ? 0.3952 0.3243 0.3067 0.0056  -0.0108 -0.0351 142 GLU B OE1 
5188 O OE2 . GLU B 156 ? 0.3902 0.3089 0.2915 0.0138  -0.0042 -0.0399 142 GLU B OE2 
5189 N N   . GLN B 157 ? 0.3198 0.2805 0.2424 0.0074  -0.0050 -0.0278 143 GLN B N   
5190 C CA  . GLN B 157 ? 0.3328 0.2911 0.2467 0.0061  -0.0068 -0.0282 143 GLN B CA  
5191 C C   . GLN B 157 ? 0.3199 0.2860 0.2366 0.0078  -0.0040 -0.0260 143 GLN B C   
5192 O O   . GLN B 157 ? 0.3349 0.2984 0.2431 0.0074  -0.0046 -0.0264 143 GLN B O   
5193 C CB  . GLN B 157 ? 0.3362 0.2938 0.2499 0.0007  -0.0133 -0.0268 143 GLN B CB  
5194 C CG  . GLN B 157 ? 0.3803 0.3289 0.2894 -0.0017 -0.0169 -0.0289 143 GLN B CG  
5195 C CD  . GLN B 157 ? 0.4202 0.3687 0.3298 -0.0075 -0.0236 -0.0270 143 GLN B CD  
5196 O OE1 . GLN B 157 ? 0.4488 0.4020 0.3588 -0.0093 -0.0259 -0.0249 143 GLN B OE1 
5197 N NE2 . GLN B 157 ? 0.4417 0.3852 0.3517 -0.0104 -0.0270 -0.0275 143 GLN B NE2 
5198 N N   . ASN B 158 ? 0.3027 0.2774 0.2301 0.0094  -0.0011 -0.0237 144 ASN B N   
5199 C CA  . ASN B 158 ? 0.3049 0.2863 0.2349 0.0105  0.0011  -0.0215 144 ASN B CA  
5200 C C   . ASN B 158 ? 0.2829 0.2683 0.2173 0.0145  0.0066  -0.0212 144 ASN B C   
5201 O O   . ASN B 158 ? 0.2706 0.2611 0.2068 0.0154  0.0087  -0.0192 144 ASN B O   
5202 C CB  . ASN B 158 ? 0.3019 0.2909 0.2408 0.0078  -0.0018 -0.0180 144 ASN B CB  
5203 C CG  . ASN B 158 ? 0.3209 0.3155 0.2710 0.0086  -0.0003 -0.0166 144 ASN B CG  
5204 O OD1 . ASN B 158 ? 0.2692 0.2631 0.2212 0.0110  0.0028  -0.0177 144 ASN B OD1 
5205 N ND2 . ASN B 158 ? 0.3006 0.3007 0.2580 0.0065  -0.0025 -0.0140 144 ASN B ND2 
5206 N N   . ALA B 159 ? 0.2814 0.2645 0.2179 0.0167  0.0088  -0.0227 145 ALA B N   
5207 C CA  . ALA B 159 ? 0.2940 0.2824 0.2383 0.0197  0.0128  -0.0215 145 ALA B CA  
5208 C C   . ALA B 159 ? 0.2903 0.2826 0.2338 0.0220  0.0167  -0.0204 145 ALA B C   
5209 O O   . ALA B 159 ? 0.2824 0.2817 0.2331 0.0219  0.0176  -0.0176 145 ALA B O   
5210 C CB  . ALA B 159 ? 0.2827 0.2663 0.2266 0.0222  0.0144  -0.0237 145 ALA B CB  
5211 N N   . CYS B 160 ? 0.2833 0.2706 0.2177 0.0242  0.0193  -0.0224 146 CYS B N   
5212 C CA  . CYS B 160 ? 0.3171 0.3085 0.2518 0.0270  0.0242  -0.0211 146 CYS B CA  
5213 C C   . CYS B 160 ? 0.3081 0.3039 0.2423 0.0250  0.0234  -0.0184 146 CYS B C   
5214 O O   . CYS B 160 ? 0.2825 0.2849 0.2224 0.0260  0.0263  -0.0158 146 CYS B O   
5215 C CB  . CYS B 160 ? 0.3138 0.2985 0.2386 0.0304  0.0281  -0.0239 146 CYS B CB  
5216 S SG  . CYS B 160 ? 0.3732 0.3539 0.3008 0.0339  0.0301  -0.0262 146 CYS B SG  
5217 N N   . TYR B 161 ? 0.3037 0.2963 0.2316 0.0220  0.0193  -0.0188 147 TYR B N   
5218 C CA  . TYR B 161 ? 0.3289 0.3260 0.2571 0.0203  0.0184  -0.0158 147 TYR B CA  
5219 C C   . TYR B 161 ? 0.3051 0.3089 0.2443 0.0183  0.0160  -0.0130 147 TYR B C   
5220 O O   . TYR B 161 ? 0.2888 0.2973 0.2309 0.0179  0.0164  -0.0102 147 TYR B O   
5221 C CB  . TYR B 161 ? 0.3325 0.3242 0.2497 0.0179  0.0150  -0.0165 147 TYR B CB  
5222 C CG  . TYR B 161 ? 0.3673 0.3564 0.2845 0.0144  0.0089  -0.0170 147 TYR B CG  
5223 C CD1 . TYR B 161 ? 0.3841 0.3657 0.2958 0.0139  0.0071  -0.0203 147 TYR B CD1 
5224 C CD2 . TYR B 161 ? 0.3676 0.3619 0.2910 0.0116  0.0050  -0.0140 147 TYR B CD2 
5225 C CE1 . TYR B 161 ? 0.3550 0.3346 0.2672 0.0103  0.0013  -0.0203 147 TYR B CE1 
5226 C CE2 . TYR B 161 ? 0.3878 0.3807 0.3125 0.0084  -0.0004 -0.0140 147 TYR B CE2 
5227 C CZ  . TYR B 161 ? 0.3864 0.3722 0.3056 0.0075  -0.0023 -0.0171 147 TYR B CZ  
5228 O OH  . TYR B 161 ? 0.3818 0.3664 0.3026 0.0039  -0.0078 -0.0167 147 TYR B OH  
5229 N N   . GLU B 162 ? 0.3009 0.3048 0.2460 0.0173  0.0136  -0.0136 148 GLU B N   
5230 C CA  . GLU B 162 ? 0.2654 0.2753 0.2206 0.0161  0.0123  -0.0111 148 GLU B CA  
5231 C C   . GLU B 162 ? 0.2852 0.2996 0.2472 0.0183  0.0159  -0.0097 148 GLU B C   
5232 O O   . GLU B 162 ? 0.2647 0.2838 0.2323 0.0177  0.0159  -0.0072 148 GLU B O   
5233 C CB  . GLU B 162 ? 0.2927 0.3014 0.2516 0.0145  0.0092  -0.0119 148 GLU B CB  
5234 C CG  . GLU B 162 ? 0.3240 0.3313 0.2803 0.0114  0.0046  -0.0114 148 GLU B CG  
5235 C CD  . GLU B 162 ? 0.3542 0.3666 0.3140 0.0103  0.0032  -0.0083 148 GLU B CD  
5236 O OE1 . GLU B 162 ? 0.3425 0.3548 0.2974 0.0106  0.0039  -0.0074 148 GLU B OE1 
5237 O OE2 . GLU B 162 ? 0.3816 0.3977 0.3487 0.0093  0.0016  -0.0066 148 GLU B OE2 
5238 N N   . ILE B 163 ? 0.2570 0.2698 0.2187 0.0207  0.0189  -0.0113 149 ILE B N   
5239 C CA  . ILE B 163 ? 0.2577 0.2751 0.2261 0.0225  0.0221  -0.0097 149 ILE B CA  
5240 C C   . ILE B 163 ? 0.2713 0.2923 0.2388 0.0228  0.0243  -0.0074 149 ILE B C   
5241 O O   . ILE B 163 ? 0.2266 0.2524 0.2005 0.0221  0.0245  -0.0047 149 ILE B O   
5242 C CB  . ILE B 163 ? 0.2509 0.2662 0.2190 0.0254  0.0249  -0.0116 149 ILE B CB  
5243 C CG1 . ILE B 163 ? 0.2347 0.2475 0.2060 0.0250  0.0226  -0.0130 149 ILE B CG1 
5244 C CG2 . ILE B 163 ? 0.2560 0.2767 0.2303 0.0275  0.0287  -0.0094 149 ILE B CG2 
5245 C CD1 . ILE B 163 ? 0.2426 0.2513 0.2120 0.0279  0.0248  -0.0152 149 ILE B CD1 
5246 N N   . ASP B 164 ? 0.2447 0.2627 0.2034 0.0234  0.0257  -0.0083 150 ASP B N   
5247 C CA  . ASP B 164 ? 0.2814 0.3024 0.2383 0.0237  0.0283  -0.0058 150 ASP B CA  
5248 C C   . ASP B 164 ? 0.2860 0.3095 0.2449 0.0210  0.0251  -0.0032 150 ASP B C   
5249 O O   . ASP B 164 ? 0.2598 0.2876 0.2225 0.0207  0.0265  -0.0002 150 ASP B O   
5250 C CB  . ASP B 164 ? 0.2865 0.3026 0.2318 0.0250  0.0305  -0.0076 150 ASP B CB  
5251 C CG  . ASP B 164 ? 0.3030 0.3174 0.2468 0.0286  0.0351  -0.0096 150 ASP B CG  
5252 O OD1 . ASP B 164 ? 0.2866 0.3052 0.2396 0.0302  0.0370  -0.0088 150 ASP B OD1 
5253 O OD2 . ASP B 164 ? 0.3317 0.3401 0.2650 0.0301  0.0368  -0.0121 150 ASP B OD2 
5254 N N   . ARG B 165 ? 0.2637 0.2846 0.2205 0.0189  0.0208  -0.0040 151 ARG B N   
5255 C CA  . ARG B 165 ? 0.2687 0.2920 0.2279 0.0168  0.0178  -0.0014 151 ARG B CA  
5256 C C   . ARG B 165 ? 0.2583 0.2859 0.2275 0.0167  0.0178  0.0006  151 ARG B C   
5257 O O   . ARG B 165 ? 0.2339 0.2643 0.2059 0.0161  0.0179  0.0034  151 ARG B O   
5258 C CB  . ARG B 165 ? 0.2779 0.2984 0.2346 0.0148  0.0131  -0.0024 151 ARG B CB  
5259 C CG  . ARG B 165 ? 0.2712 0.2946 0.2319 0.0131  0.0100  0.0006  151 ARG B CG  
5260 C CD  . ARG B 165 ? 0.2842 0.3063 0.2446 0.0111  0.0054  0.0001  151 ARG B CD  
5261 N NE  . ARG B 165 ? 0.2977 0.3198 0.2635 0.0110  0.0047  -0.0015 151 ARG B NE  
5262 C CZ  . ARG B 165 ? 0.2836 0.3090 0.2578 0.0112  0.0047  -0.0003 151 ARG B CZ  
5263 N NH1 . ARG B 165 ? 0.2677 0.2961 0.2462 0.0118  0.0055  0.0021  151 ARG B NH1 
5264 N NH2 . ARG B 165 ? 0.2932 0.3182 0.2710 0.0109  0.0040  -0.0016 151 ARG B NH2 
5265 N N   . VAL B 166 ? 0.2497 0.2772 0.2239 0.0171  0.0175  -0.0009 152 VAL B N   
5266 C CA  . VAL B 166 ? 0.2445 0.2748 0.2268 0.0167  0.0170  0.0006  152 VAL B CA  
5267 C C   . VAL B 166 ? 0.2248 0.2581 0.2106 0.0175  0.0198  0.0025  152 VAL B C   
5268 O O   . VAL B 166 ? 0.2438 0.2792 0.2336 0.0167  0.0193  0.0049  152 VAL B O   
5269 C CB  . VAL B 166 ? 0.2298 0.2588 0.2154 0.0168  0.0159  -0.0014 152 VAL B CB  
5270 C CG1 . VAL B 166 ? 0.2132 0.2442 0.2057 0.0168  0.0162  -0.0002 152 VAL B CG1 
5271 C CG2 . VAL B 166 ? 0.2225 0.2498 0.2069 0.0154  0.0128  -0.0021 152 VAL B CG2 
5272 N N   . LEU B 167 ? 0.2093 0.2430 0.1940 0.0192  0.0228  0.0016  153 LEU B N   
5273 C CA  . LEU B 167 ? 0.2526 0.2902 0.2416 0.0198  0.0257  0.0040  153 LEU B CA  
5274 C C   . LEU B 167 ? 0.2550 0.2943 0.2415 0.0189  0.0266  0.0067  153 LEU B C   
5275 O O   . LEU B 167 ? 0.2600 0.3025 0.2516 0.0180  0.0270  0.0097  153 LEU B O   
5276 C CB  . LEU B 167 ? 0.2431 0.2811 0.2316 0.0223  0.0292  0.0027  153 LEU B CB  
5277 C CG  . LEU B 167 ? 0.2417 0.2790 0.2348 0.0232  0.0285  0.0011  153 LEU B CG  
5278 C CD1 . LEU B 167 ? 0.2232 0.2603 0.2153 0.0262  0.0320  -0.0002 153 LEU B CD1 
5279 C CD2 . LEU B 167 ? 0.2223 0.2629 0.2238 0.0220  0.0272  0.0034  153 LEU B CD2 
5280 N N   . THR B 168 ? 0.2588 0.2957 0.2373 0.0190  0.0266  0.0060  154 THR B N   
5281 C CA  . THR B 168 ? 0.2767 0.3146 0.2519 0.0180  0.0272  0.0088  154 THR B CA  
5282 C C   . THR B 168 ? 0.2786 0.3173 0.2579 0.0160  0.0240  0.0112  154 THR B C   
5283 O O   . THR B 168 ? 0.2814 0.3224 0.2633 0.0151  0.0248  0.0144  154 THR B O   
5284 C CB  . THR B 168 ? 0.2853 0.3194 0.2499 0.0181  0.0270  0.0074  154 THR B CB  
5285 O OG1 . THR B 168 ? 0.3001 0.3329 0.2601 0.0204  0.0309  0.0054  154 THR B OG1 
5286 C CG2 . THR B 168 ? 0.3251 0.3599 0.2858 0.0168  0.0269  0.0106  154 THR B CG2 
5287 N N   . THR B 169 ? 0.2557 0.2923 0.2360 0.0154  0.0204  0.0098  155 THR B N   
5288 C CA  . THR B 169 ? 0.2658 0.3027 0.2501 0.0141  0.0177  0.0119  155 THR B CA  
5289 C C   . THR B 169 ? 0.2540 0.2925 0.2455 0.0139  0.0183  0.0132  155 THR B C   
5290 O O   . THR B 169 ? 0.2611 0.2997 0.2549 0.0129  0.0174  0.0158  155 THR B O   
5291 C CB  . THR B 169 ? 0.2548 0.2899 0.2396 0.0139  0.0145  0.0102  155 THR B CB  
5292 O OG1 . THR B 169 ? 0.2654 0.2987 0.2436 0.0136  0.0132  0.0091  155 THR B OG1 
5293 C CG2 . THR B 169 ? 0.2378 0.2729 0.2263 0.0132  0.0122  0.0125  155 THR B CG2 
5294 N N   . MET B 170 ? 0.2262 0.2652 0.2208 0.0147  0.0194  0.0114  156 MET B N   
5295 C CA  . MET B 170 ? 0.2644 0.3048 0.2653 0.0141  0.0197  0.0126  156 MET B CA  
5296 C C   . MET B 170 ? 0.2815 0.3247 0.2839 0.0134  0.0216  0.0160  156 MET B C   
5297 O O   . MET B 170 ? 0.2688 0.3122 0.2752 0.0119  0.0204  0.0183  156 MET B O   
5298 C CB  . MET B 170 ? 0.2524 0.2932 0.2556 0.0153  0.0207  0.0105  156 MET B CB  
5299 C CG  . MET B 170 ? 0.2205 0.2585 0.2241 0.0154  0.0185  0.0079  156 MET B CG  
5300 S SD  . MET B 170 ? 0.2022 0.2406 0.2095 0.0163  0.0192  0.0064  156 MET B SD  
5301 C CE  . MET B 170 ? 0.2091 0.2489 0.2225 0.0148  0.0182  0.0091  156 MET B CE  
5302 N N   . LEU B 171 ? 0.2632 0.3085 0.2624 0.0143  0.0246  0.0163  157 LEU B N   
5303 C CA  . LEU B 171 ? 0.2827 0.3316 0.2836 0.0136  0.0272  0.0198  157 LEU B CA  
5304 C C   . LEU B 171 ? 0.2983 0.3460 0.2968 0.0119  0.0257  0.0227  157 LEU B C   
5305 O O   . LEU B 171 ? 0.3266 0.3762 0.3288 0.0103  0.0260  0.0261  157 LEU B O   
5306 C CB  . LEU B 171 ? 0.2949 0.3458 0.2917 0.0155  0.0314  0.0193  157 LEU B CB  
5307 C CG  . LEU B 171 ? 0.3148 0.3679 0.3150 0.0176  0.0341  0.0177  157 LEU B CG  
5308 C CD1 . LEU B 171 ? 0.3216 0.3750 0.3154 0.0200  0.0384  0.0167  157 LEU B CD1 
5309 C CD2 . LEU B 171 ? 0.2949 0.3530 0.3048 0.0169  0.0349  0.0206  157 LEU B CD2 
5310 N N   . ARG B 172 ? 0.2876 0.3323 0.2802 0.0121  0.0238  0.0215  158 ARG B N   
5311 C CA  . ARG B 172 ? 0.3169 0.3602 0.3070 0.0107  0.0221  0.0243  158 ARG B CA  
5312 C C   . ARG B 172 ? 0.3041 0.3455 0.2994 0.0096  0.0190  0.0255  158 ARG B C   
5313 O O   . ARG B 172 ? 0.2823 0.3234 0.2790 0.0081  0.0185  0.0289  158 ARG B O   
5314 C CB  . ARG B 172 ? 0.3505 0.3913 0.3335 0.0112  0.0205  0.0229  158 ARG B CB  
5315 C CG  . ARG B 172 ? 0.4004 0.4397 0.3807 0.0100  0.0182  0.0260  158 ARG B CG  
5316 C CD  . ARG B 172 ? 0.4249 0.4619 0.3995 0.0103  0.0154  0.0245  158 ARG B CD  
5317 N NE  . ARG B 172 ? 0.4584 0.4949 0.4259 0.0110  0.0174  0.0222  158 ARG B NE  
5318 C CZ  . ARG B 172 ? 0.5182 0.5532 0.4839 0.0117  0.0164  0.0187  158 ARG B CZ  
5319 N NH1 . ARG B 172 ? 0.3978 0.4325 0.3688 0.0119  0.0139  0.0172  158 ARG B NH1 
5320 N NH2 . ARG B 172 ? 0.4806 0.5139 0.4386 0.0124  0.0182  0.0166  158 ARG B NH2 
5321 N N   . GLU B 173 ? 0.2727 0.3122 0.2706 0.0103  0.0172  0.0228  159 GLU B N   
5322 C CA  . GLU B 173 ? 0.3078 0.3443 0.3091 0.0098  0.0146  0.0234  159 GLU B CA  
5323 C C   . GLU B 173 ? 0.2882 0.3244 0.2946 0.0089  0.0146  0.0236  159 GLU B C   
5324 O O   . GLU B 173 ? 0.2749 0.3077 0.2832 0.0082  0.0126  0.0244  159 GLU B O   
5325 C CB  . GLU B 173 ? 0.2750 0.3094 0.2759 0.0111  0.0127  0.0206  159 GLU B CB  
5326 C CG  . GLU B 173 ? 0.3241 0.3586 0.3209 0.0116  0.0116  0.0206  159 GLU B CG  
5327 C CD  . GLU B 173 ? 0.3498 0.3837 0.3445 0.0108  0.0105  0.0240  159 GLU B CD  
5328 O OE1 . GLU B 173 ? 0.3459 0.3781 0.3432 0.0102  0.0098  0.0263  159 GLU B OE1 
5329 O OE2 . GLU B 173 ? 0.3536 0.3881 0.3434 0.0107  0.0101  0.0245  159 GLU B OE2 
5330 N N   . ARG B 174 ? 0.2334 0.2729 0.2418 0.0089  0.0166  0.0230  160 ARG B N   
5331 C CA  . ARG B 174 ? 0.2349 0.2744 0.2484 0.0079  0.0160  0.0232  160 ARG B CA  
5332 C C   . ARG B 174 ? 0.2504 0.2855 0.2643 0.0083  0.0136  0.0207  160 ARG B C   
5333 O O   . ARG B 174 ? 0.2127 0.2443 0.2282 0.0070  0.0116  0.0215  160 ARG B O   
5334 C CB  . ARG B 174 ? 0.2553 0.2952 0.2716 0.0055  0.0156  0.0272  160 ARG B CB  
5335 C CG  . ARG B 174 ? 0.2694 0.3148 0.2860 0.0052  0.0188  0.0300  160 ARG B CG  
5336 C CD  . ARG B 174 ? 0.3248 0.3750 0.3453 0.0059  0.0213  0.0295  160 ARG B CD  
5337 N NE  . ARG B 174 ? 0.3686 0.4235 0.3873 0.0072  0.0254  0.0305  160 ARG B NE  
5338 C CZ  . ARG B 174 ? 0.3911 0.4506 0.4131 0.0085  0.0285  0.0303  160 ARG B CZ  
5339 N NH1 . ARG B 174 ? 0.3482 0.4088 0.3760 0.0086  0.0273  0.0295  160 ARG B NH1 
5340 N NH2 . ARG B 174 ? 0.4181 0.4810 0.4372 0.0100  0.0327  0.0312  160 ARG B NH2 
5341 N N   . ARG B 175 ? 0.2235 0.2582 0.2354 0.0100  0.0139  0.0177  161 ARG B N   
5342 C CA  . ARG B 175 ? 0.2259 0.2568 0.2376 0.0106  0.0122  0.0154  161 ARG B CA  
5343 C C   . ARG B 175 ? 0.2171 0.2492 0.2283 0.0118  0.0131  0.0125  161 ARG B C   
5344 O O   . ARG B 175 ? 0.1962 0.2314 0.2066 0.0124  0.0148  0.0121  161 ARG B O   
5345 C CB  . ARG B 175 ? 0.2291 0.2576 0.2386 0.0114  0.0111  0.0154  161 ARG B CB  
5346 C CG  . ARG B 175 ? 0.2266 0.2513 0.2367 0.0106  0.0097  0.0174  161 ARG B CG  
5347 C CD  . ARG B 175 ? 0.2395 0.2620 0.2485 0.0120  0.0088  0.0176  161 ARG B CD  
5348 N NE  . ARG B 175 ? 0.2383 0.2551 0.2476 0.0123  0.0077  0.0176  161 ARG B NE  
5349 C CZ  . ARG B 175 ? 0.2698 0.2836 0.2788 0.0136  0.0069  0.0186  161 ARG B CZ  
5350 N NH1 . ARG B 175 ? 0.2473 0.2636 0.2562 0.0143  0.0066  0.0202  161 ARG B NH1 
5351 N NH2 . ARG B 175 ? 0.2514 0.2591 0.2599 0.0141  0.0062  0.0181  161 ARG B NH2 
5352 N N   . PRO B 176 ? 0.1936 0.2229 0.2050 0.0121  0.0120  0.0106  162 PRO B N   
5353 C CA  . PRO B 176 ? 0.2086 0.2385 0.2197 0.0130  0.0126  0.0082  162 PRO B CA  
5354 C C   . PRO B 176 ? 0.2150 0.2460 0.2235 0.0140  0.0132  0.0067  162 PRO B C   
5355 O O   . PRO B 176 ? 0.2085 0.2391 0.2156 0.0142  0.0126  0.0072  162 PRO B O   
5356 C CB  . PRO B 176 ? 0.2004 0.2263 0.2114 0.0129  0.0113  0.0069  162 PRO B CB  
5357 C CG  . PRO B 176 ? 0.2170 0.2401 0.2286 0.0118  0.0101  0.0086  162 PRO B CG  
5358 C CD  . PRO B 176 ? 0.2109 0.2356 0.2223 0.0117  0.0104  0.0105  162 PRO B CD  
5359 N N   . GLY B 177 ? 0.2139 0.2458 0.2218 0.0147  0.0140  0.0051  163 GLY B N   
5360 C CA  . GLY B 177 ? 0.2142 0.2458 0.2192 0.0153  0.0140  0.0033  163 GLY B CA  
5361 C C   . GLY B 177 ? 0.1977 0.2276 0.2031 0.0155  0.0136  0.0013  163 GLY B C   
5362 O O   . GLY B 177 ? 0.1887 0.2179 0.1964 0.0154  0.0135  0.0013  163 GLY B O   
5363 N N   . TYR B 178 ? 0.1921 0.2212 0.1953 0.0156  0.0131  -0.0002 164 TYR B N   
5364 C CA  . TYR B 178 ? 0.2092 0.2364 0.2126 0.0155  0.0126  -0.0019 164 TYR B CA  
5365 C C   . TYR B 178 ? 0.1988 0.2251 0.1991 0.0157  0.0126  -0.0035 164 TYR B C   
5366 O O   . TYR B 178 ? 0.1923 0.2188 0.1899 0.0153  0.0120  -0.0035 164 TYR B O   
5367 C CB  . TYR B 178 ? 0.2051 0.2316 0.2097 0.0150  0.0117  -0.0016 164 TYR B CB  
5368 C CG  . TYR B 178 ? 0.2081 0.2328 0.2127 0.0146  0.0113  -0.0029 164 TYR B CG  
5369 C CD1 . TYR B 178 ? 0.1984 0.2227 0.2014 0.0141  0.0107  -0.0039 164 TYR B CD1 
5370 C CD2 . TYR B 178 ? 0.2128 0.2357 0.2183 0.0146  0.0115  -0.0028 164 TYR B CD2 
5371 C CE1 . TYR B 178 ? 0.2159 0.2385 0.2191 0.0134  0.0103  -0.0047 164 TYR B CE1 
5372 C CE2 . TYR B 178 ? 0.2269 0.2482 0.2320 0.0141  0.0114  -0.0036 164 TYR B CE2 
5373 C CZ  . TYR B 178 ? 0.2101 0.2315 0.2145 0.0135  0.0109  -0.0044 164 TYR B CZ  
5374 O OH  . TYR B 178 ? 0.2198 0.2395 0.2239 0.0128  0.0107  -0.0048 164 TYR B OH  
5375 N N   . LEU B 179 ? 0.1962 0.2206 0.1962 0.0162  0.0128  -0.0049 165 LEU B N   
5376 C CA  . LEU B 179 ? 0.2012 0.2233 0.1977 0.0164  0.0126  -0.0067 165 LEU B CA  
5377 C C   . LEU B 179 ? 0.2118 0.2312 0.2089 0.0159  0.0117  -0.0077 165 LEU B C   
5378 O O   . LEU B 179 ? 0.1843 0.2033 0.1835 0.0166  0.0121  -0.0076 165 LEU B O   
5379 C CB  . LEU B 179 ? 0.1692 0.1909 0.1638 0.0182  0.0145  -0.0074 165 LEU B CB  
5380 C CG  . LEU B 179 ? 0.2131 0.2370 0.2059 0.0188  0.0160  -0.0064 165 LEU B CG  
5381 C CD1 . LEU B 179 ? 0.1866 0.2108 0.1789 0.0210  0.0188  -0.0068 165 LEU B CD1 
5382 C CD2 . LEU B 179 ? 0.1917 0.2141 0.1793 0.0178  0.0148  -0.0071 165 LEU B CD2 
5383 N N   . MET B 180 ? 0.2107 0.2286 0.2061 0.0145  0.0102  -0.0084 166 MET B N   
5384 C CA  . MET B 180 ? 0.2023 0.2174 0.1979 0.0139  0.0093  -0.0092 166 MET B CA  
5385 C C   . MET B 180 ? 0.2238 0.2350 0.2154 0.0147  0.0093  -0.0111 166 MET B C   
5386 O O   . MET B 180 ? 0.2211 0.2310 0.2087 0.0144  0.0088  -0.0120 166 MET B O   
5387 C CB  . MET B 180 ? 0.2210 0.2364 0.2174 0.0118  0.0078  -0.0086 166 MET B CB  
5388 C CG  . MET B 180 ? 0.2422 0.2546 0.2385 0.0108  0.0071  -0.0090 166 MET B CG  
5389 S SD  . MET B 180 ? 0.2901 0.3023 0.2868 0.0079  0.0050  -0.0084 166 MET B SD  
5390 C CE  . MET B 180 ? 0.2151 0.2323 0.2168 0.0077  0.0062  -0.0061 166 MET B CE  
5391 N N   . LEU B 181 ? 0.2201 0.2291 0.2123 0.0159  0.0099  -0.0116 167 LEU B N   
5392 C CA  . LEU B 181 ? 0.2369 0.2417 0.2257 0.0174  0.0103  -0.0134 167 LEU B CA  
5393 C C   . LEU B 181 ? 0.2200 0.2205 0.2083 0.0164  0.0087  -0.0140 167 LEU B C   
5394 O O   . LEU B 181 ? 0.2096 0.2095 0.2004 0.0172  0.0088  -0.0135 167 LEU B O   
5395 C CB  . LEU B 181 ? 0.2285 0.2350 0.2196 0.0203  0.0125  -0.0131 167 LEU B CB  
5396 C CG  . LEU B 181 ? 0.2279 0.2302 0.2161 0.0228  0.0138  -0.0149 167 LEU B CG  
5397 C CD1 . LEU B 181 ? 0.2321 0.2315 0.2137 0.0230  0.0142  -0.0168 167 LEU B CD1 
5398 C CD2 . LEU B 181 ? 0.2472 0.2533 0.2398 0.0256  0.0162  -0.0137 167 LEU B CD2 
5399 N N   . PRO B 182 ? 0.2537 0.2511 0.2389 0.0143  0.0068  -0.0148 168 PRO B N   
5400 C CA  . PRO B 182 ? 0.2559 0.2485 0.2401 0.0131  0.0052  -0.0152 168 PRO B CA  
5401 C C   . PRO B 182 ? 0.2622 0.2500 0.2443 0.0158  0.0060  -0.0168 168 PRO B C   
5402 O O   . PRO B 182 ? 0.2510 0.2374 0.2302 0.0181  0.0075  -0.0182 168 PRO B O   
5403 C CB  . PRO B 182 ? 0.2642 0.2543 0.2450 0.0104  0.0029  -0.0159 168 PRO B CB  
5404 C CG  . PRO B 182 ? 0.2533 0.2491 0.2357 0.0096  0.0030  -0.0147 168 PRO B CG  
5405 C CD  . PRO B 182 ? 0.2500 0.2481 0.2325 0.0126  0.0056  -0.0150 168 PRO B CD  
5406 N N   . ALA B 183 ? 0.2675 0.2524 0.2509 0.0157  0.0052  -0.0162 169 ALA B N   
5407 C CA  . ALA B 183 ? 0.2682 0.2492 0.2511 0.0187  0.0060  -0.0171 169 ALA B CA  
5408 C C   . ALA B 183 ? 0.3231 0.2974 0.2999 0.0200  0.0060  -0.0197 169 ALA B C   
5409 O O   . ALA B 183 ? 0.3330 0.3056 0.3089 0.0236  0.0080  -0.0209 169 ALA B O   
5410 C CB  . ALA B 183 ? 0.2998 0.2782 0.2845 0.0179  0.0045  -0.0158 169 ALA B CB  
5411 N N   . ASP B 184 ? 0.3127 0.2829 0.2851 0.0170  0.0037  -0.0207 170 ASP B N   
5412 C CA  . ASP B 184 ? 0.3277 0.2900 0.2928 0.0178  0.0032  -0.0235 170 ASP B CA  
5413 C C   . ASP B 184 ? 0.3211 0.2848 0.2825 0.0196  0.0052  -0.0249 170 ASP B C   
5414 O O   . ASP B 184 ? 0.3386 0.2969 0.2947 0.0227  0.0069  -0.0272 170 ASP B O   
5415 C CB  . ASP B 184 ? 0.3503 0.3074 0.3117 0.0135  -0.0005 -0.0238 170 ASP B CB  
5416 C CG  . ASP B 184 ? 0.3473 0.3100 0.3101 0.0099  -0.0020 -0.0225 170 ASP B CG  
5417 O OD1 . ASP B 184 ? 0.2986 0.2693 0.2674 0.0096  -0.0009 -0.0203 170 ASP B OD1 
5418 O OD2 . ASP B 184 ? 0.3529 0.3114 0.3105 0.0074  -0.0046 -0.0236 170 ASP B OD2 
5419 N N   . VAL B 185 ? 0.2929 0.2634 0.2565 0.0179  0.0053  -0.0235 171 VAL B N   
5420 C CA  . VAL B 185 ? 0.3036 0.2757 0.2635 0.0193  0.0071  -0.0244 171 VAL B CA  
5421 C C   . VAL B 185 ? 0.3021 0.2762 0.2637 0.0239  0.0112  -0.0246 171 VAL B C   
5422 O O   . VAL B 185 ? 0.2696 0.2411 0.2257 0.0264  0.0135  -0.0263 171 VAL B O   
5423 C CB  . VAL B 185 ? 0.2695 0.2491 0.2329 0.0169  0.0063  -0.0223 171 VAL B CB  
5424 C CG1 . VAL B 185 ? 0.2728 0.2544 0.2327 0.0184  0.0084  -0.0227 171 VAL B CG1 
5425 C CG2 . VAL B 185 ? 0.2895 0.2678 0.2520 0.0125  0.0024  -0.0217 171 VAL B CG2 
5426 N N   . ALA B 186 ? 0.2600 0.2388 0.2292 0.0251  0.0122  -0.0227 172 ALA B N   
5427 C CA  . ALA B 186 ? 0.2948 0.2768 0.2675 0.0292  0.0158  -0.0221 172 ALA B CA  
5428 C C   . ALA B 186 ? 0.2952 0.2705 0.2636 0.0330  0.0177  -0.0244 172 ALA B C   
5429 O O   . ALA B 186 ? 0.2984 0.2757 0.2674 0.0367  0.0215  -0.0245 172 ALA B O   
5430 C CB  . ALA B 186 ? 0.2738 0.2608 0.2551 0.0292  0.0154  -0.0195 172 ALA B CB  
5431 N N   . LYS B 187 ? 0.3019 0.2690 0.2659 0.0322  0.0154  -0.0262 173 LYS B N   
5432 C CA  . LYS B 187 ? 0.3186 0.2778 0.2779 0.0361  0.0172  -0.0285 173 LYS B CA  
5433 C C   . LYS B 187 ? 0.3348 0.2864 0.2830 0.0364  0.0177  -0.0318 173 LYS B C   
5434 O O   . LYS B 187 ? 0.3506 0.2944 0.2934 0.0400  0.0195  -0.0343 173 LYS B O   
5435 C CB  . LYS B 187 ? 0.3536 0.3064 0.3132 0.0352  0.0143  -0.0288 173 LYS B CB  
5436 C CG  . LYS B 187 ? 0.4237 0.3822 0.3924 0.0341  0.0129  -0.0256 173 LYS B CG  
5437 C CD  . LYS B 187 ? 0.5670 0.5184 0.5356 0.0351  0.0112  -0.0259 173 LYS B CD  
5438 C CE  . LYS B 187 ? 0.7249 0.6748 0.6939 0.0303  0.0072  -0.0245 173 LYS B CE  
5439 N NZ  . LYS B 187 ? 0.7874 0.7454 0.7642 0.0291  0.0068  -0.0213 173 LYS B NZ  
5440 N N   . LYS B 188 ? 0.3155 0.2687 0.2598 0.0330  0.0161  -0.0319 174 LYS B N   
5441 C CA  . LYS B 188 ? 0.3372 0.2824 0.2697 0.0328  0.0160  -0.0350 174 LYS B CA  
5442 C C   . LYS B 188 ? 0.3404 0.2860 0.2692 0.0377  0.0214  -0.0361 174 LYS B C   
5443 O O   . LYS B 188 ? 0.3142 0.2689 0.2502 0.0396  0.0246  -0.0338 174 LYS B O   
5444 C CB  . LYS B 188 ? 0.3126 0.2600 0.2427 0.0278  0.0123  -0.0343 174 LYS B CB  
5445 C CG  . LYS B 188 ? 0.3501 0.2977 0.2843 0.0230  0.0075  -0.0328 174 LYS B CG  
5446 C CD  . LYS B 188 ? 0.3654 0.3013 0.2925 0.0218  0.0046  -0.0353 174 LYS B CD  
5447 C CE  . LYS B 188 ? 0.3942 0.3308 0.3252 0.0166  -0.0002 -0.0335 174 LYS B CE  
5448 N NZ  . LYS B 188 ? 0.4203 0.3461 0.3465 0.0156  -0.0028 -0.0352 174 LYS B NZ  
5449 N N   . ALA B 189 ? 0.3502 0.2853 0.2674 0.0396  0.0224  -0.0396 175 ALA B N   
5450 C CA  . ALA B 189 ? 0.3596 0.2936 0.2719 0.0447  0.0282  -0.0410 175 ALA B CA  
5451 C C   . ALA B 189 ? 0.3552 0.2972 0.2675 0.0437  0.0300  -0.0393 175 ALA B C   
5452 O O   . ALA B 189 ? 0.3551 0.2982 0.2648 0.0390  0.0261  -0.0387 175 ALA B O   
5453 C CB  . ALA B 189 ? 0.3970 0.3166 0.2944 0.0463  0.0283  -0.0456 175 ALA B CB  
5454 N N   . ALA B 190 ? 0.3595 0.3072 0.2751 0.0482  0.0359  -0.0381 176 ALA B N   
5455 C CA  . ALA B 190 ? 0.3547 0.3090 0.2693 0.0477  0.0383  -0.0364 176 ALA B CA  
5456 C C   . ALA B 190 ? 0.3767 0.3301 0.2872 0.0536  0.0455  -0.0373 176 ALA B C   
5457 O O   . ALA B 190 ? 0.3799 0.3287 0.2901 0.0582  0.0487  -0.0390 176 ALA B O   
5458 C CB  . ALA B 190 ? 0.3307 0.2979 0.2588 0.0455  0.0375  -0.0320 176 ALA B CB  
5459 N N   . THR B 191 ? 0.3599 0.3179 0.2675 0.0535  0.0484  -0.0360 177 THR B N   
5460 C CA  . THR B 191 ? 0.3720 0.3303 0.2756 0.0588  0.0559  -0.0363 177 THR B CA  
5461 C C   . THR B 191 ? 0.3550 0.3271 0.2701 0.0591  0.0593  -0.0315 177 THR B C   
5462 O O   . THR B 191 ? 0.3149 0.2928 0.2328 0.0547  0.0562  -0.0291 177 THR B O   
5463 C CB  . THR B 191 ? 0.3919 0.3408 0.2777 0.0585  0.0568  -0.0393 177 THR B CB  
5464 O OG1 . THR B 191 ? 0.4205 0.3560 0.2952 0.0572  0.0526  -0.0436 177 THR B OG1 
5465 C CG2 . THR B 191 ? 0.4038 0.3520 0.2841 0.0646  0.0654  -0.0399 177 THR B CG2 
5466 N N   . PRO B 192 ? 0.3763 0.3538 0.2988 0.0642  0.0654  -0.0299 178 PRO B N   
5467 C CA  . PRO B 192 ? 0.3839 0.3742 0.3169 0.0644  0.0688  -0.0252 178 PRO B CA  
5468 C C   . PRO B 192 ? 0.3770 0.3674 0.3004 0.0632  0.0713  -0.0247 178 PRO B C   
5469 O O   . PRO B 192 ? 0.3886 0.3708 0.2984 0.0659  0.0749  -0.0277 178 PRO B O   
5470 C CB  . PRO B 192 ? 0.3870 0.3809 0.3273 0.0709  0.0755  -0.0242 178 PRO B CB  
5471 C CG  . PRO B 192 ? 0.3753 0.3600 0.3131 0.0732  0.0737  -0.0277 178 PRO B CG  
5472 C CD  . PRO B 192 ? 0.3741 0.3463 0.2961 0.0702  0.0694  -0.0321 178 PRO B CD  
5473 N N   . PRO B 193 ? 0.4018 0.4004 0.3309 0.0592  0.0692  -0.0210 179 PRO B N   
5474 C CA  . PRO B 193 ? 0.4211 0.4203 0.3417 0.0580  0.0716  -0.0199 179 PRO B CA  
5475 C C   . PRO B 193 ? 0.4266 0.4326 0.3506 0.0623  0.0800  -0.0172 179 PRO B C   
5476 O O   . PRO B 193 ? 0.4299 0.4446 0.3678 0.0645  0.0826  -0.0142 179 PRO B O   
5477 C CB  . PRO B 193 ? 0.3863 0.3922 0.3138 0.0524  0.0662  -0.0165 179 PRO B CB  
5478 C CG  . PRO B 193 ? 0.3752 0.3851 0.3159 0.0511  0.0621  -0.0156 179 PRO B CG  
5479 C CD  . PRO B 193 ? 0.3653 0.3726 0.3088 0.0557  0.0649  -0.0176 179 PRO B CD  
5480 N N   . VAL B 194 ? 0.4505 0.4523 0.3614 0.0635  0.0841  -0.0181 180 VAL B N   
5481 C CA  . VAL B 194 ? 0.4976 0.5060 0.4107 0.0674  0.0926  -0.0151 180 VAL B CA  
5482 C C   . VAL B 194 ? 0.4630 0.4839 0.3879 0.0639  0.0922  -0.0092 180 VAL B C   
5483 O O   . VAL B 194 ? 0.4154 0.4462 0.3517 0.0662  0.0974  -0.0052 180 VAL B O   
5484 C CB  . VAL B 194 ? 0.5081 0.5076 0.4020 0.0695  0.0973  -0.0178 180 VAL B CB  
5485 C CG1 . VAL B 194 ? 0.5105 0.5149 0.4063 0.0755  0.1076  -0.0160 180 VAL B CG1 
5486 C CG2 . VAL B 194 ? 0.5450 0.5297 0.4242 0.0704  0.0946  -0.0240 180 VAL B CG2 
5487 N N   . ASN B 195 ? 0.4277 0.4480 0.3501 0.0583  0.0859  -0.0083 181 ASN B N   
5488 C CA  . ASN B 195 ? 0.4372 0.4671 0.3683 0.0546  0.0849  -0.0030 181 ASN B CA  
5489 C C   . ASN B 195 ? 0.4015 0.4362 0.3460 0.0510  0.0783  -0.0014 181 ASN B C   
5490 O O   . ASN B 195 ? 0.4084 0.4372 0.3507 0.0492  0.0725  -0.0045 181 ASN B O   
5491 C CB  . ASN B 195 ? 0.4248 0.4505 0.3434 0.0510  0.0827  -0.0027 181 ASN B CB  
5492 C CG  . ASN B 195 ? 0.5289 0.5488 0.4320 0.0541  0.0891  -0.0042 181 ASN B CG  
5493 O OD1 . ASN B 195 ? 0.4747 0.5007 0.3797 0.0561  0.0958  -0.0008 181 ASN B OD1 
5494 N ND2 . ASN B 195 ? 0.5840 0.5919 0.4714 0.0544  0.0869  -0.0092 181 ASN B ND2 
5495 N N   . ALA B 196 ? 0.3823 0.4273 0.3402 0.0498  0.0792  0.0035  182 ALA B N   
5496 C CA  . ALA B 196 ? 0.3588 0.4079 0.3278 0.0459  0.0729  0.0053  182 ALA B CA  
5497 C C   . ALA B 196 ? 0.3674 0.4128 0.3302 0.0412  0.0672  0.0052  182 ALA B C   
5498 O O   . ALA B 196 ? 0.3301 0.3732 0.2833 0.0403  0.0684  0.0057  182 ALA B O   
5499 C CB  . ALA B 196 ? 0.3644 0.4246 0.3479 0.0453  0.0750  0.0108  182 ALA B CB  
5500 N N   . LEU B 197 ? 0.3216 0.3666 0.2902 0.0384  0.0611  0.0047  183 LEU B N   
5501 C CA  . LEU B 197 ? 0.3336 0.3767 0.2993 0.0342  0.0557  0.0053  183 LEU B CA  
5502 C C   . LEU B 197 ? 0.3500 0.3997 0.3214 0.0319  0.0564  0.0103  183 LEU B C   
5503 O O   . LEU B 197 ? 0.3485 0.4049 0.3313 0.0317  0.0573  0.0133  183 LEU B O   
5504 C CB  . LEU B 197 ? 0.3025 0.3442 0.2739 0.0323  0.0499  0.0039  183 LEU B CB  
5505 C CG  . LEU B 197 ? 0.3273 0.3658 0.2955 0.0287  0.0442  0.0035  183 LEU B CG  
5506 C CD1 . LEU B 197 ? 0.3368 0.3680 0.2923 0.0286  0.0428  0.0005  183 LEU B CD1 
5507 C CD2 . LEU B 197 ? 0.3142 0.3527 0.2898 0.0274  0.0399  0.0027  183 LEU B CD2 
5508 N N   . THR B 198 ? 0.3733 0.4210 0.3365 0.0301  0.0560  0.0115  184 THR B N   
5509 C CA  . THR B 198 ? 0.4065 0.4590 0.3735 0.0275  0.0561  0.0163  184 THR B CA  
5510 C C   . THR B 198 ? 0.4277 0.4761 0.3893 0.0243  0.0507  0.0163  184 THR B C   
5511 O O   . THR B 198 ? 0.4352 0.4774 0.3870 0.0244  0.0485  0.0133  184 THR B O   
5512 C CB  . THR B 198 ? 0.4147 0.4700 0.3772 0.0290  0.0624  0.0189  184 THR B CB  
5513 O OG1 . THR B 198 ? 0.4838 0.5323 0.4314 0.0293  0.0628  0.0167  184 THR B OG1 
5514 C CG2 . THR B 198 ? 0.4041 0.4633 0.3712 0.0329  0.0685  0.0186  184 THR B CG2 
5515 N N   . LEU B 199 ? 0.4301 0.4819 0.3984 0.0216  0.0482  0.0200  185 LEU B N   
5516 C CA  . LEU B 199 ? 0.4898 0.5385 0.4539 0.0188  0.0438  0.0212  185 LEU B CA  
5517 C C   . LEU B 199 ? 0.5287 0.5785 0.4869 0.0180  0.0467  0.0247  185 LEU B C   
5518 O O   . LEU B 199 ? 0.5216 0.5765 0.4858 0.0172  0.0492  0.0288  185 LEU B O   
5519 C CB  . LEU B 199 ? 0.4750 0.5254 0.4488 0.0165  0.0396  0.0229  185 LEU B CB  
5520 C CG  . LEU B 199 ? 0.4763 0.5248 0.4482 0.0140  0.0357  0.0254  185 LEU B CG  
5521 C CD1 . LEU B 199 ? 0.4764 0.5199 0.4427 0.0138  0.0314  0.0225  185 LEU B CD1 
5522 C CD2 . LEU B 199 ? 0.4419 0.4924 0.4237 0.0121  0.0333  0.0279  185 LEU B CD2 
5523 N N   . ARG B 200 ? 0.5676 0.6123 0.5135 0.0182  0.0463  0.0234  186 ARG B N   
5524 C CA  . ARG B 200 ? 0.6685 0.7133 0.6072 0.0172  0.0486  0.0269  186 ARG B CA  
5525 C C   . ARG B 200 ? 0.6875 0.7347 0.6323 0.0141  0.0454  0.0314  186 ARG B C   
5526 O O   . ARG B 200 ? 0.5931 0.6384 0.5415 0.0126  0.0399  0.0310  186 ARG B O   
5527 C CB  . ARG B 200 ? 0.6617 0.6996 0.5856 0.0171  0.0469  0.0246  186 ARG B CB  
5528 N N   . HIS B 201 ? 0.6997 0.7510 0.6464 0.0132  0.0492  0.0360  187 HIS B N   
5529 C CA  . HIS B 201 ? 0.6898 0.7429 0.6421 0.0102  0.0465  0.0407  187 HIS B CA  
5530 C C   . HIS B 201 ? 0.6369 0.6848 0.5808 0.0085  0.0420  0.0416  187 HIS B C   
5531 O O   . HIS B 201 ? 0.6513 0.6964 0.5838 0.0087  0.0436  0.0420  187 HIS B O   
5532 C CB  . HIS B 201 ? 0.6813 0.7399 0.6365 0.0095  0.0519  0.0456  187 HIS B CB  
5533 N N   . ALA B 202 ? 0.5974 0.6434 0.5466 0.0070  0.0364  0.0419  188 ALA B N   
5534 C CA  . ALA B 202 ? 0.5772 0.6190 0.5203 0.0056  0.0317  0.0434  188 ALA B CA  
5535 C C   . ALA B 202 ? 0.5549 0.5974 0.4965 0.0034  0.0325  0.0492  188 ALA B C   
5536 O O   . ALA B 202 ? 0.5291 0.5754 0.4776 0.0023  0.0351  0.0523  188 ALA B O   
5537 C CB  . ALA B 202 ? 0.5119 0.5519 0.4618 0.0053  0.0260  0.0421  188 ALA B CB  
5538 N N   . HIS B 203 ? 0.5378 0.5763 0.4702 0.0024  0.0298  0.0508  189 HIS B N   
5539 C CA  . HIS B 203 ? 0.5210 0.5590 0.4504 0.0002  0.0296  0.0564  189 HIS B CA  
5540 C C   . HIS B 203 ? 0.4742 0.5077 0.4012 -0.0007 0.0230  0.0577  189 HIS B C   
5541 O O   . HIS B 203 ? 0.4543 0.4849 0.3753 0.0001  0.0199  0.0548  189 HIS B O   
5542 C CB  . HIS B 203 ? 0.5618 0.5998 0.4795 0.0002  0.0346  0.0580  189 HIS B CB  
5543 C CG  . HIS B 203 ? 0.7217 0.7641 0.6410 0.0021  0.0416  0.0563  189 HIS B CG  
5544 N ND1 . HIS B 203 ? 0.7376 0.7859 0.6675 0.0015  0.0452  0.0590  189 HIS B ND1 
5545 C CD2 . HIS B 203 ? 0.7895 0.8312 0.7016 0.0046  0.0454  0.0523  189 HIS B CD2 
5546 C CE1 . HIS B 203 ? 0.7525 0.8043 0.6824 0.0038  0.0512  0.0570  189 HIS B CE1 
5547 N NE2 . HIS B 203 ? 0.8433 0.8908 0.7622 0.0059  0.0516  0.0528  189 HIS B NE2 
5548 N N   . ALA B 204 ? 0.4578 0.4907 0.3899 -0.0025 0.0205  0.0620  190 ALA B N   
5549 C CA  . ALA B 204 ? 0.4184 0.4472 0.3482 -0.0031 0.0146  0.0640  190 ALA B CA  
5550 C C   . ALA B 204 ? 0.4138 0.4400 0.3304 -0.0041 0.0141  0.0664  190 ALA B C   
5551 O O   . ALA B 204 ? 0.4290 0.4562 0.3387 -0.0049 0.0188  0.0683  190 ALA B O   
5552 C CB  . ALA B 204 ? 0.3973 0.4251 0.3348 -0.0046 0.0124  0.0684  190 ALA B CB  
5553 N N   . ASP B 205 ? 0.4150 0.4378 0.3279 -0.0040 0.0084  0.0663  191 ASP B N   
5554 C CA  . ASP B 205 ? 0.4204 0.4398 0.3215 -0.0055 0.0062  0.0698  191 ASP B CA  
5555 C C   . ASP B 205 ? 0.4372 0.4562 0.3384 -0.0075 0.0074  0.0760  191 ASP B C   
5556 O O   . ASP B 205 ? 0.4085 0.4280 0.3199 -0.0078 0.0062  0.0782  191 ASP B O   
5557 C CB  . ASP B 205 ? 0.4215 0.4381 0.3227 -0.0053 -0.0012 0.0699  191 ASP B CB  
5558 C CG  . ASP B 205 ? 0.4510 0.4639 0.3401 -0.0070 -0.0045 0.0736  191 ASP B CG  
5559 O OD1 . ASP B 205 ? 0.4708 0.4815 0.3484 -0.0073 -0.0047 0.0713  191 ASP B OD1 
5560 O OD2 . ASP B 205 ? 0.4766 0.4880 0.3670 -0.0082 -0.0071 0.0789  191 ASP B OD2 
5561 N N   . SER B 206 ? 0.4408 0.4585 0.3300 -0.0089 0.0101  0.0789  192 SER B N   
5562 C CA  . SER B 206 ? 0.4364 0.4545 0.3257 -0.0111 0.0125  0.0849  192 SER B CA  
5563 C C   . SER B 206 ? 0.4279 0.4425 0.3203 -0.0124 0.0064  0.0898  192 SER B C   
5564 O O   . SER B 206 ? 0.3887 0.4036 0.2869 -0.0140 0.0072  0.0942  192 SER B O   
5565 C CB  . SER B 206 ? 0.4551 0.4723 0.3298 -0.0122 0.0171  0.0870  192 SER B CB  
5566 O OG  . SER B 206 ? 0.5102 0.5225 0.3721 -0.0124 0.0129  0.0867  192 SER B OG  
5567 N N   . ALA B 207 ? 0.4191 0.4304 0.3082 -0.0119 0.0000  0.0894  193 ALA B N   
5568 C CA  . ALA B 207 ? 0.3947 0.4028 0.2881 -0.0124 -0.0061 0.0939  193 ALA B CA  
5569 C C   . ALA B 207 ? 0.3773 0.3864 0.2858 -0.0108 -0.0075 0.0924  193 ALA B C   
5570 O O   . ALA B 207 ? 0.3543 0.3610 0.2684 -0.0115 -0.0093 0.0965  193 ALA B O   
5571 C CB  . ALA B 207 ? 0.4050 0.4101 0.2919 -0.0120 -0.0126 0.0941  193 ALA B CB  
5572 N N   . CYS B 208 ? 0.3871 0.3989 0.3016 -0.0087 -0.0066 0.0865  194 CYS B N   
5573 C CA  . CYS B 208 ? 0.3933 0.4059 0.3208 -0.0072 -0.0069 0.0845  194 CYS B CA  
5574 C C   . CYS B 208 ? 0.3702 0.3838 0.3023 -0.0088 -0.0025 0.0863  194 CYS B C   
5575 O O   . CYS B 208 ? 0.3543 0.3656 0.2942 -0.0089 -0.0042 0.0882  194 CYS B O   
5576 C CB  . CYS B 208 ? 0.4090 0.4245 0.3405 -0.0050 -0.0060 0.0780  194 CYS B CB  
5577 S SG  . CYS B 208 ? 0.5027 0.5186 0.4486 -0.0032 -0.0059 0.0753  194 CYS B SG  
5578 N N   . LEU B 209 ? 0.3585 0.3755 0.2861 -0.0099 0.0030  0.0858  195 LEU B N   
5579 C CA  . LEU B 209 ? 0.3701 0.3892 0.3028 -0.0118 0.0072  0.0882  195 LEU B CA  
5580 C C   . LEU B 209 ? 0.3376 0.3532 0.2694 -0.0144 0.0054  0.0950  195 LEU B C   
5581 O O   . LEU B 209 ? 0.3232 0.3376 0.2631 -0.0156 0.0049  0.0971  195 LEU B O   
5582 C CB  . LEU B 209 ? 0.3885 0.4123 0.3157 -0.0122 0.0137  0.0873  195 LEU B CB  
5583 C CG  . LEU B 209 ? 0.3875 0.4154 0.3219 -0.0140 0.0184  0.0895  195 LEU B CG  
5584 C CD1 . LEU B 209 ? 0.3617 0.3913 0.3069 -0.0126 0.0180  0.0850  195 LEU B CD1 
5585 C CD2 . LEU B 209 ? 0.4191 0.4516 0.3470 -0.0142 0.0253  0.0899  195 LEU B CD2 
5586 N N   . LYS B 210 ? 0.3504 0.3636 0.2721 -0.0154 0.0039  0.0987  196 LYS B N   
5587 C CA  . LYS B 210 ? 0.3299 0.3393 0.2499 -0.0179 0.0020  0.1056  196 LYS B CA  
5588 C C   . LYS B 210 ? 0.3225 0.3269 0.2505 -0.0171 -0.0038 0.1067  196 LYS B C   
5589 O O   . LYS B 210 ? 0.3039 0.3054 0.2365 -0.0190 -0.0044 0.1107  196 LYS B O   
5590 C CB  . LYS B 210 ? 0.3611 0.3685 0.2677 -0.0189 0.0009  0.1089  196 LYS B CB  
5591 C CG  . LYS B 210 ? 0.3729 0.3746 0.2772 -0.0206 -0.0040 0.1154  196 LYS B CG  
5592 C CD  . LYS B 210 ? 0.3536 0.3542 0.2439 -0.0228 -0.0025 0.1200  196 LYS B CD  
5593 C CE  . LYS B 210 ? 0.3726 0.3671 0.2592 -0.0240 -0.0087 0.1260  196 LYS B CE  
5594 N NZ  . LYS B 210 ? 0.3831 0.3753 0.2760 -0.0264 -0.0084 0.1316  196 LYS B NZ  
5595 N N   . ALA B 211 ? 0.3229 0.3259 0.2527 -0.0142 -0.0081 0.1033  197 ALA B N   
5596 C CA  . ALA B 211 ? 0.3223 0.3204 0.2596 -0.0126 -0.0131 0.1043  197 ALA B CA  
5597 C C   . ALA B 211 ? 0.3160 0.3130 0.2631 -0.0127 -0.0116 0.1028  197 ALA B C   
5598 O O   . ALA B 211 ? 0.3109 0.3026 0.2618 -0.0135 -0.0139 0.1063  197 ALA B O   
5599 C CB  . ALA B 211 ? 0.3183 0.3167 0.2572 -0.0092 -0.0170 0.1005  197 ALA B CB  
5600 N N   . PHE B 212 ? 0.2851 0.2867 0.2361 -0.0120 -0.0080 0.0976  198 PHE B N   
5601 C CA  . PHE B 212 ? 0.3014 0.3020 0.2609 -0.0125 -0.0068 0.0962  198 PHE B CA  
5602 C C   . PHE B 212 ? 0.3089 0.3093 0.2684 -0.0166 -0.0045 0.1012  198 PHE B C   
5603 O O   . PHE B 212 ? 0.2931 0.2886 0.2577 -0.0180 -0.0063 0.1033  198 PHE B O   
5604 C CB  . PHE B 212 ? 0.2883 0.2941 0.2512 -0.0111 -0.0035 0.0900  198 PHE B CB  
5605 C CG  . PHE B 212 ? 0.2979 0.3038 0.2681 -0.0125 -0.0018 0.0890  198 PHE B CG  
5606 C CD1 . PHE B 212 ? 0.3038 0.3042 0.2802 -0.0114 -0.0047 0.0875  198 PHE B CD1 
5607 C CD2 . PHE B 212 ? 0.2955 0.3068 0.2665 -0.0149 0.0028  0.0898  198 PHE B CD2 
5608 C CE1 . PHE B 212 ? 0.2663 0.2659 0.2485 -0.0131 -0.0038 0.0866  198 PHE B CE1 
5609 C CE2 . PHE B 212 ? 0.3010 0.3125 0.2792 -0.0166 0.0036  0.0893  198 PHE B CE2 
5610 C CZ  . PHE B 212 ? 0.2802 0.2856 0.2636 -0.0159 0.0001  0.0876  198 PHE B CZ  
5611 N N   . ARG B 213 ? 0.3192 0.3247 0.2730 -0.0186 -0.0003 0.1031  199 ARG B N   
5612 C CA  . ARG B 213 ? 0.3159 0.3225 0.2702 -0.0226 0.0025  0.1084  199 ARG B CA  
5613 C C   . ARG B 213 ? 0.3222 0.3218 0.2751 -0.0246 -0.0015 0.1146  199 ARG B C   
5614 O O   . ARG B 213 ? 0.3302 0.3271 0.2881 -0.0276 -0.0019 0.1180  199 ARG B O   
5615 C CB  . ARG B 213 ? 0.3270 0.3399 0.2740 -0.0237 0.0079  0.1098  199 ARG B CB  
5616 C CG  . ARG B 213 ? 0.3369 0.3527 0.2856 -0.0278 0.0118  0.1155  199 ARG B CG  
5617 C CD  . ARG B 213 ? 0.3628 0.3790 0.3012 -0.0296 0.0139  0.1209  199 ARG B CD  
5618 N NE  . ARG B 213 ? 0.3714 0.3803 0.3077 -0.0315 0.0090  0.1264  199 ARG B NE  
5619 C CZ  . ARG B 213 ? 0.3615 0.3687 0.2997 -0.0356 0.0092  0.1330  199 ARG B CZ  
5620 N NH1 . ARG B 213 ? 0.3779 0.3911 0.3207 -0.0385 0.0143  0.1355  199 ARG B NH1 
5621 N NH2 . ARG B 213 ? 0.3512 0.3507 0.2874 -0.0367 0.0041  0.1374  199 ARG B NH2 
5622 N N   . ASP B 214 ? 0.3314 0.3276 0.2775 -0.0234 -0.0047 0.1165  200 ASP B N   
5623 C CA  . ASP B 214 ? 0.3250 0.3142 0.2696 -0.0251 -0.0087 0.1227  200 ASP B CA  
5624 C C   . ASP B 214 ? 0.3317 0.3139 0.2845 -0.0240 -0.0129 0.1218  200 ASP B C   
5625 O O   . ASP B 214 ? 0.3623 0.3390 0.3171 -0.0267 -0.0145 0.1264  200 ASP B O   
5626 C CB  . ASP B 214 ? 0.3510 0.3381 0.2869 -0.0237 -0.0120 0.1248  200 ASP B CB  
5627 C CG  . ASP B 214 ? 0.3554 0.3470 0.2806 -0.0256 -0.0082 0.1270  200 ASP B CG  
5628 O OD1 . ASP B 214 ? 0.3718 0.3682 0.2968 -0.0280 -0.0026 0.1280  200 ASP B OD1 
5629 O OD2 . ASP B 214 ? 0.3346 0.3247 0.2514 -0.0247 -0.0108 0.1282  200 ASP B OD2 
5630 N N   . ALA B 215 ? 0.3244 0.3059 0.2813 -0.0199 -0.0147 0.1160  201 ALA B N   
5631 C CA  . ALA B 215 ? 0.3458 0.3198 0.3094 -0.0182 -0.0182 0.1149  201 ALA B CA  
5632 C C   . ALA B 215 ? 0.3338 0.3067 0.3031 -0.0210 -0.0165 0.1142  201 ALA B C   
5633 O O   . ALA B 215 ? 0.3254 0.2902 0.2975 -0.0222 -0.0192 0.1166  201 ALA B O   
5634 C CB  . ALA B 215 ? 0.2853 0.2597 0.2521 -0.0132 -0.0198 0.1090  201 ALA B CB  
5635 N N   . ALA B 216 ? 0.3100 0.2903 0.2812 -0.0218 -0.0123 0.1108  202 ALA B N   
5636 C CA  . ALA B 216 ? 0.3231 0.3031 0.3001 -0.0249 -0.0109 0.1108  202 ALA B CA  
5637 C C   . ALA B 216 ? 0.3294 0.3079 0.3054 -0.0301 -0.0107 0.1180  202 ALA B C   
5638 O O   . ALA B 216 ? 0.3151 0.2872 0.2950 -0.0327 -0.0130 0.1202  202 ALA B O   
5639 C CB  . ALA B 216 ? 0.3151 0.3043 0.2944 -0.0248 -0.0064 0.1065  202 ALA B CB  
5640 N N   . GLU B 217 ? 0.3414 0.3249 0.3116 -0.0316 -0.0081 0.1221  203 GLU B N   
5641 C CA  . GLU B 217 ? 0.3336 0.3166 0.3030 -0.0367 -0.0072 0.1294  203 GLU B CA  
5642 C C   . GLU B 217 ? 0.3483 0.3202 0.3172 -0.0379 -0.0125 0.1338  203 GLU B C   
5643 O O   . GLU B 217 ? 0.3531 0.3210 0.3258 -0.0421 -0.0137 0.1376  203 GLU B O   
5644 C CB  . GLU B 217 ? 0.3531 0.3427 0.3147 -0.0377 -0.0032 0.1329  203 GLU B CB  
5645 C CG  . GLU B 217 ? 0.3895 0.3748 0.3469 -0.0416 -0.0044 0.1412  203 GLU B CG  
5646 C CD  . GLU B 217 ? 0.4008 0.3883 0.3639 -0.0470 -0.0022 0.1459  203 GLU B CD  
5647 O OE1 . GLU B 217 ? 0.4491 0.4433 0.4187 -0.0475 0.0011  0.1430  203 GLU B OE1 
5648 O OE2 . GLU B 217 ? 0.4177 0.4002 0.3796 -0.0508 -0.0041 0.1527  203 GLU B OE2 
5649 N N   . ASN B 218 ? 0.3551 0.3219 0.3197 -0.0344 -0.0161 0.1334  204 ASN B N   
5650 C CA  . ASN B 218 ? 0.3606 0.3165 0.3246 -0.0348 -0.0212 0.1377  204 ASN B CA  
5651 C C   . ASN B 218 ? 0.3679 0.3155 0.3383 -0.0343 -0.0241 0.1349  204 ASN B C   
5652 O O   . ASN B 218 ? 0.3842 0.3226 0.3553 -0.0368 -0.0273 0.1391  204 ASN B O   
5653 C CB  . ASN B 218 ? 0.3453 0.2985 0.3043 -0.0306 -0.0243 0.1378  204 ASN B CB  
5654 C CG  . ASN B 218 ? 0.3737 0.3340 0.3246 -0.0313 -0.0219 0.1404  204 ASN B CG  
5655 O OD1 . ASN B 218 ? 0.3581 0.3237 0.3062 -0.0353 -0.0178 0.1436  204 ASN B OD1 
5656 N ND2 . ASN B 218 ? 0.3460 0.3063 0.2929 -0.0276 -0.0243 0.1391  204 ASN B ND2 
5657 N N   . ARG B 219 ? 0.3525 0.3025 0.3269 -0.0312 -0.0231 0.1279  205 ARG B N   
5658 C CA  . ARG B 219 ? 0.3675 0.3092 0.3467 -0.0307 -0.0256 0.1247  205 ARG B CA  
5659 C C   . ARG B 219 ? 0.3800 0.3220 0.3629 -0.0366 -0.0247 0.1271  205 ARG B C   
5660 O O   . ARG B 219 ? 0.3915 0.3234 0.3757 -0.0391 -0.0281 0.1293  205 ARG B O   
5661 C CB  . ARG B 219 ? 0.3576 0.3023 0.3395 -0.0260 -0.0245 0.1168  205 ARG B CB  
5662 C CG  . ARG B 219 ? 0.3607 0.2965 0.3462 -0.0255 -0.0267 0.1132  205 ARG B CG  
5663 C CD  . ARG B 219 ? 0.3921 0.3151 0.3760 -0.0230 -0.0310 0.1149  205 ARG B CD  
5664 N NE  . ARG B 219 ? 0.3963 0.3086 0.3820 -0.0223 -0.0333 0.1116  205 ARG B NE  
5665 C CZ  . ARG B 219 ? 0.4048 0.3117 0.3915 -0.0273 -0.0346 0.1131  205 ARG B CZ  
5666 N NH1 . ARG B 219 ? 0.4178 0.3298 0.4053 -0.0333 -0.0337 0.1183  205 ARG B NH1 
5667 N NH2 . ARG B 219 ? 0.4067 0.3026 0.3935 -0.0263 -0.0369 0.1095  205 ARG B NH2 
5668 N N   . LEU B 220 ? 0.3594 0.3127 0.3441 -0.0390 -0.0202 0.1268  206 LEU B N   
5669 C CA  . LEU B 220 ? 0.3719 0.3273 0.3616 -0.0446 -0.0192 0.1294  206 LEU B CA  
5670 C C   . LEU B 220 ? 0.4029 0.3550 0.3913 -0.0499 -0.0204 0.1378  206 LEU B C   
5671 O O   . LEU B 220 ? 0.4175 0.3655 0.4101 -0.0548 -0.0223 0.1407  206 LEU B O   
5672 C CB  . LEU B 220 ? 0.3681 0.3372 0.3607 -0.0453 -0.0137 0.1277  206 LEU B CB  
5673 C CG  . LEU B 220 ? 0.3661 0.3392 0.3606 -0.0409 -0.0123 0.1197  206 LEU B CG  
5674 C CD1 . LEU B 220 ? 0.3448 0.3309 0.3389 -0.0399 -0.0066 0.1184  206 LEU B CD1 
5675 C CD2 . LEU B 220 ? 0.3501 0.3194 0.3507 -0.0429 -0.0144 0.1172  206 LEU B CD2 
5676 N N   . ALA B 221 ? 0.4063 0.3597 0.3888 -0.0495 -0.0196 0.1421  207 ALA B N   
5677 C CA  . ALA B 221 ? 0.4241 0.3743 0.4047 -0.0546 -0.0205 0.1505  207 ALA B CA  
5678 C C   . ALA B 221 ? 0.4030 0.3385 0.3844 -0.0562 -0.0266 0.1527  207 ALA B C   
5679 O O   . ALA B 221 ? 0.4555 0.3874 0.4374 -0.0617 -0.0279 0.1595  207 ALA B O   
5680 C CB  . ALA B 221 ? 0.3996 0.3526 0.3724 -0.0533 -0.0191 0.1543  207 ALA B CB  
5681 N N   . MET B 222 ? 0.4152 0.3417 0.3963 -0.0514 -0.0302 0.1474  208 MET B N   
5682 C CA  . MET B 222 ? 0.4521 0.3633 0.4331 -0.0523 -0.0357 0.1490  208 MET B CA  
5683 C C   . MET B 222 ? 0.4287 0.3344 0.4143 -0.0538 -0.0376 0.1448  208 MET B C   
5684 O O   . MET B 222 ? 0.4736 0.3652 0.4583 -0.0537 -0.0421 0.1446  208 MET B O   
5685 C CB  . MET B 222 ? 0.4418 0.3445 0.4189 -0.0459 -0.0388 0.1470  208 MET B CB  
5686 C CG  . MET B 222 ? 0.4320 0.3408 0.4089 -0.0392 -0.0369 0.1402  208 MET B CG  
5687 S SD  . MET B 222 ? 0.5307 0.4285 0.5051 -0.0323 -0.0412 0.1395  208 MET B SD  
5688 C CE  . MET B 222 ? 0.4199 0.3234 0.3969 -0.0254 -0.0391 0.1302  208 MET B CE  
5689 N N   . SER B 223 ? 0.4342 0.3500 0.4243 -0.0554 -0.0343 0.1418  209 SER B N   
5690 C CA  . SER B 223 ? 0.4476 0.3587 0.4417 -0.0570 -0.0363 0.1377  209 SER B CA  
5691 C C   . SER B 223 ? 0.4552 0.3628 0.4527 -0.0650 -0.0387 0.1437  209 SER B C   
5692 O O   . SER B 223 ? 0.4620 0.3799 0.4626 -0.0697 -0.0357 0.1492  209 SER B O   
5693 C CB  . SER B 223 ? 0.4254 0.3488 0.4233 -0.0553 -0.0322 0.1323  209 SER B CB  
5694 O OG  . SER B 223 ? 0.3991 0.3174 0.4002 -0.0568 -0.0346 0.1283  209 SER B OG  
5695 N N   . LYS B 224 ? 0.4690 0.3617 0.4656 -0.0667 -0.0440 0.1430  210 LYS B N   
5696 C CA  . LYS B 224 ? 0.4874 0.3766 0.4879 -0.0748 -0.0470 0.1478  210 LYS B CA  
5697 C C   . LYS B 224 ? 0.4740 0.3725 0.4809 -0.0773 -0.0454 0.1448  210 LYS B C   
5698 O O   . LYS B 224 ? 0.4764 0.3842 0.4895 -0.0835 -0.0441 0.1499  210 LYS B O   
5699 C CB  . LYS B 224 ? 0.5464 0.4154 0.5430 -0.0759 -0.0535 0.1474  210 LYS B CB  
5700 C CG  . LYS B 224 ? 0.6793 0.5371 0.6696 -0.0723 -0.0556 0.1496  210 LYS B CG  
5701 C CD  . LYS B 224 ? 0.7197 0.5771 0.7101 -0.0783 -0.0566 0.1593  210 LYS B CD  
5702 C CE  . LYS B 224 ? 0.7657 0.6088 0.7498 -0.0753 -0.0601 0.1616  210 LYS B CE  
5703 N NZ  . LYS B 224 ? 0.8046 0.6276 0.7857 -0.0760 -0.0661 0.1597  210 LYS B NZ  
5704 N N   . ARG B 225 ? 0.4459 0.3421 0.4518 -0.0726 -0.0457 0.1367  211 ARG B N   
5705 C CA  . ARG B 225 ? 0.4329 0.3379 0.4443 -0.0740 -0.0443 0.1332  211 ARG B CA  
5706 C C   . ARG B 225 ? 0.4123 0.3234 0.4220 -0.0664 -0.0406 0.1256  211 ARG B C   
5707 O O   . ARG B 225 ? 0.4131 0.3147 0.4173 -0.0608 -0.0419 0.1206  211 ARG B O   
5708 C CB  . ARG B 225 ? 0.4360 0.3285 0.4475 -0.0780 -0.0503 0.1315  211 ARG B CB  
5709 C CG  . ARG B 225 ? 0.4235 0.3248 0.4414 -0.0808 -0.0498 0.1292  211 ARG B CG  
5710 C CD  . ARG B 225 ? 0.4314 0.3196 0.4491 -0.0866 -0.0567 0.1293  211 ARG B CD  
5711 N NE  . ARG B 225 ? 0.4397 0.3117 0.4491 -0.0822 -0.0601 0.1221  211 ARG B NE  
5712 C CZ  . ARG B 225 ? 0.4530 0.3258 0.4605 -0.0776 -0.0589 0.1147  211 ARG B CZ  
5713 N NH1 . ARG B 225 ? 0.4300 0.3191 0.4435 -0.0765 -0.0547 0.1131  211 ARG B NH1 
5714 N NH2 . ARG B 225 ? 0.4408 0.2975 0.4401 -0.0740 -0.0619 0.1088  211 ARG B NH2 
5715 N N   . THR B 226 ? 0.3928 0.3196 0.4076 -0.0663 -0.0360 0.1249  212 THR B N   
5716 C CA  . THR B 226 ? 0.3840 0.3180 0.3979 -0.0599 -0.0323 0.1181  212 THR B CA  
5717 C C   . THR B 226 ? 0.3723 0.3105 0.3911 -0.0613 -0.0326 0.1144  212 THR B C   
5718 O O   . THR B 226 ? 0.3826 0.3260 0.4077 -0.0672 -0.0332 0.1184  212 THR B O   
5719 C CB  . THR B 226 ? 0.3674 0.3155 0.3819 -0.0578 -0.0264 0.1201  212 THR B CB  
5720 O OG1 . THR B 226 ? 0.3835 0.3264 0.3924 -0.0560 -0.0269 0.1231  212 THR B OG1 
5721 C CG2 . THR B 226 ? 0.3433 0.2989 0.3573 -0.0519 -0.0229 0.1133  212 THR B CG2 
5722 N N   . ALA B 227 ? 0.3652 0.3007 0.3813 -0.0561 -0.0324 0.1070  213 ALA B N   
5723 C CA  . ALA B 227 ? 0.3462 0.2853 0.3659 -0.0568 -0.0327 0.1030  213 ALA B CA  
5724 C C   . ALA B 227 ? 0.3334 0.2834 0.3535 -0.0512 -0.0278 0.0981  213 ALA B C   
5725 O O   . ALA B 227 ? 0.3170 0.2675 0.3330 -0.0459 -0.0254 0.0959  213 ALA B O   
5726 C CB  . ALA B 227 ? 0.3561 0.2797 0.3712 -0.0567 -0.0379 0.0985  213 ALA B CB  
5727 N N   . LEU B 228 ? 0.3466 0.3048 0.3719 -0.0524 -0.0266 0.0964  214 LEU B N   
5728 C CA  . LEU B 228 ? 0.3229 0.2917 0.3493 -0.0477 -0.0220 0.0921  214 LEU B CA  
5729 C C   . LEU B 228 ? 0.3253 0.2895 0.3505 -0.0457 -0.0240 0.0857  214 LEU B C   
5730 O O   . LEU B 228 ? 0.3257 0.2883 0.3543 -0.0498 -0.0271 0.0861  214 LEU B O   
5731 C CB  . LEU B 228 ? 0.3119 0.2959 0.3458 -0.0503 -0.0180 0.0960  214 LEU B CB  
5732 C CG  . LEU B 228 ? 0.3451 0.3403 0.3809 -0.0462 -0.0134 0.0920  214 LEU B CG  
5733 C CD1 . LEU B 228 ? 0.3220 0.3173 0.3514 -0.0406 -0.0105 0.0890  214 LEU B CD1 
5734 C CD2 . LEU B 228 ? 0.3218 0.3307 0.3651 -0.0489 -0.0093 0.0969  214 LEU B CD2 
5735 N N   . LEU B 229 ? 0.3148 0.2770 0.3352 -0.0397 -0.0224 0.0802  215 LEU B N   
5736 C CA  . LEU B 229 ? 0.2996 0.2582 0.3182 -0.0372 -0.0233 0.0740  215 LEU B CA  
5737 C C   . LEU B 229 ? 0.3173 0.2874 0.3375 -0.0330 -0.0186 0.0708  215 LEU B C   
5738 O O   . LEU B 229 ? 0.2769 0.2488 0.2940 -0.0287 -0.0160 0.0694  215 LEU B O   
5739 C CB  . LEU B 229 ? 0.3032 0.2475 0.3144 -0.0337 -0.0257 0.0702  215 LEU B CB  
5740 C CG  . LEU B 229 ? 0.3233 0.2623 0.3312 -0.0309 -0.0265 0.0638  215 LEU B CG  
5741 C CD1 . LEU B 229 ? 0.3131 0.2477 0.3221 -0.0360 -0.0306 0.0639  215 LEU B CD1 
5742 C CD2 . LEU B 229 ? 0.3421 0.2690 0.3430 -0.0261 -0.0272 0.0602  215 LEU B CD2 
5743 N N   . ALA B 230 ? 0.2654 0.2431 0.2905 -0.0344 -0.0178 0.0699  216 ALA B N   
5744 C CA  . ALA B 230 ? 0.2552 0.2433 0.2820 -0.0307 -0.0135 0.0670  216 ALA B CA  
5745 C C   . ALA B 230 ? 0.3003 0.2858 0.3261 -0.0290 -0.0147 0.0616  216 ALA B C   
5746 O O   . ALA B 230 ? 0.2396 0.2190 0.2658 -0.0322 -0.0186 0.0614  216 ALA B O   
5747 C CB  . ALA B 230 ? 0.2598 0.2608 0.2936 -0.0332 -0.0103 0.0711  216 ALA B CB  
5748 N N   . ASP B 231 ? 0.2763 0.2659 0.3004 -0.0244 -0.0117 0.0574  217 ASP B N   
5749 C CA  . ASP B 231 ? 0.2599 0.2473 0.2827 -0.0226 -0.0124 0.0524  217 ASP B CA  
5750 C C   . ASP B 231 ? 0.2448 0.2424 0.2697 -0.0195 -0.0084 0.0501  217 ASP B C   
5751 O O   . ASP B 231 ? 0.2189 0.2258 0.2472 -0.0195 -0.0052 0.0526  217 ASP B O   
5752 C CB  . ASP B 231 ? 0.2621 0.2377 0.2779 -0.0196 -0.0142 0.0485  217 ASP B CB  
5753 C CG  . ASP B 231 ? 0.2907 0.2597 0.3042 -0.0204 -0.0170 0.0450  217 ASP B CG  
5754 O OD1 . ASP B 231 ? 0.2765 0.2408 0.2909 -0.0249 -0.0208 0.0470  217 ASP B OD1 
5755 O OD2 . ASP B 231 ? 0.2896 0.2580 0.3002 -0.0167 -0.0155 0.0406  217 ASP B OD2 
5756 N N   . PHE B 232 ? 0.2455 0.2406 0.2680 -0.0169 -0.0086 0.0453  218 PHE B N   
5757 C CA  . PHE B 232 ? 0.2450 0.2481 0.2702 -0.0152 -0.0062 0.0430  218 PHE B CA  
5758 C C   . PHE B 232 ? 0.2509 0.2624 0.2766 -0.0122 -0.0019 0.0429  218 PHE B C   
5759 O O   . PHE B 232 ? 0.2424 0.2618 0.2716 -0.0116 0.0005  0.0425  218 PHE B O   
5760 C CB  . PHE B 232 ? 0.2440 0.2409 0.2651 -0.0131 -0.0075 0.0381  218 PHE B CB  
5761 C CG  . PHE B 232 ? 0.2621 0.2567 0.2785 -0.0086 -0.0055 0.0348  218 PHE B CG  
5762 C CD1 . PHE B 232 ? 0.2430 0.2287 0.2550 -0.0075 -0.0069 0.0343  218 PHE B CD1 
5763 C CD2 . PHE B 232 ? 0.2380 0.2389 0.2548 -0.0055 -0.0026 0.0323  218 PHE B CD2 
5764 C CE1 . PHE B 232 ? 0.2657 0.2499 0.2746 -0.0033 -0.0051 0.0318  218 PHE B CE1 
5765 C CE2 . PHE B 232 ? 0.2376 0.2366 0.2509 -0.0019 -0.0012 0.0297  218 PHE B CE2 
5766 C CZ  . PHE B 232 ? 0.2566 0.2478 0.2664 -0.0007 -0.0024 0.0296  218 PHE B CZ  
5767 N N   . LEU B 233 ? 0.2387 0.2484 0.2606 -0.0102 -0.0008 0.0430  219 LEU B N   
5768 C CA  . LEU B 233 ? 0.2457 0.2627 0.2671 -0.0078 0.0028  0.0428  219 LEU B CA  
5769 C C   . LEU B 233 ? 0.2518 0.2767 0.2770 -0.0100 0.0052  0.0469  219 LEU B C   
5770 O O   . LEU B 233 ? 0.2562 0.2882 0.2820 -0.0083 0.0085  0.0463  219 LEU B O   
5771 C CB  . LEU B 233 ? 0.2345 0.2478 0.2513 -0.0056 0.0027  0.0427  219 LEU B CB  
5772 C CG  . LEU B 233 ? 0.2787 0.2870 0.2926 -0.0024 0.0018  0.0383  219 LEU B CG  
5773 C CD1 . LEU B 233 ? 0.2609 0.2647 0.2717 -0.0002 0.0010  0.0385  219 LEU B CD1 
5774 C CD2 . LEU B 233 ? 0.2553 0.2693 0.2695 -0.0002 0.0041  0.0349  219 LEU B CD2 
5775 N N   . VAL B 234 ? 0.2384 0.2623 0.2666 -0.0137 0.0035  0.0512  220 VAL B N   
5776 C CA  . VAL B 234 ? 0.2425 0.2746 0.2758 -0.0161 0.0060  0.0556  220 VAL B CA  
5777 C C   . VAL B 234 ? 0.2540 0.2929 0.2925 -0.0156 0.0076  0.0543  220 VAL B C   
5778 O O   . VAL B 234 ? 0.2385 0.2859 0.2797 -0.0147 0.0117  0.0556  220 VAL B O   
5779 C CB  . VAL B 234 ? 0.2455 0.2745 0.2818 -0.0208 0.0031  0.0605  220 VAL B CB  
5780 C CG1 . VAL B 234 ? 0.2371 0.2754 0.2811 -0.0237 0.0053  0.0651  220 VAL B CG1 
5781 C CG2 . VAL B 234 ? 0.2446 0.2685 0.2761 -0.0211 0.0026  0.0629  220 VAL B CG2 
5782 N N   . LEU B 235 ? 0.2349 0.2699 0.2748 -0.0162 0.0044  0.0518  221 LEU B N   
5783 C CA  . LEU B 235 ? 0.2571 0.2981 0.3022 -0.0157 0.0053  0.0507  221 LEU B CA  
5784 C C   . LEU B 235 ? 0.2573 0.3020 0.2997 -0.0112 0.0090  0.0469  221 LEU B C   
5785 O O   . LEU B 235 ? 0.2208 0.2734 0.2670 -0.0100 0.0124  0.0475  221 LEU B O   
5786 C CB  . LEU B 235 ? 0.2275 0.2621 0.2729 -0.0173 0.0006  0.0487  221 LEU B CB  
5787 C CG  . LEU B 235 ? 0.2247 0.2557 0.2736 -0.0224 -0.0037 0.0525  221 LEU B CG  
5788 C CD1 . LEU B 235 ? 0.2245 0.2470 0.2705 -0.0233 -0.0084 0.0493  221 LEU B CD1 
5789 C CD2 . LEU B 235 ? 0.2577 0.2988 0.3164 -0.0254 -0.0027 0.0577  221 LEU B CD2 
5790 N N   . ARG B 236 ? 0.2381 0.2770 0.2738 -0.0086 0.0084  0.0429  222 ARG B N   
5791 C CA  . ARG B 236 ? 0.2673 0.3086 0.3004 -0.0049 0.0109  0.0390  222 ARG B CA  
5792 C C   . ARG B 236 ? 0.2589 0.3062 0.2906 -0.0033 0.0152  0.0402  222 ARG B C   
5793 O O   . ARG B 236 ? 0.2718 0.3232 0.3035 -0.0009 0.0180  0.0382  222 ARG B O   
5794 C CB  . ARG B 236 ? 0.2428 0.2771 0.2699 -0.0029 0.0092  0.0352  222 ARG B CB  
5795 C CG  . ARG B 236 ? 0.2389 0.2660 0.2657 -0.0042 0.0054  0.0340  222 ARG B CG  
5796 C CD  . ARG B 236 ? 0.2352 0.2636 0.2651 -0.0046 0.0045  0.0325  222 ARG B CD  
5797 N NE  . ARG B 236 ? 0.2551 0.2754 0.2819 -0.0050 0.0013  0.0300  222 ARG B NE  
5798 C CZ  . ARG B 236 ? 0.2582 0.2744 0.2863 -0.0080 -0.0021 0.0313  222 ARG B CZ  
5799 N NH1 . ARG B 236 ? 0.2383 0.2588 0.2723 -0.0112 -0.0030 0.0351  222 ARG B NH1 
5800 N NH2 . ARG B 236 ? 0.2329 0.2401 0.2561 -0.0080 -0.0047 0.0288  222 ARG B NH2 
5801 N N   . HIS B 237 ? 0.2537 0.3007 0.2834 -0.0045 0.0158  0.0434  223 HIS B N   
5802 C CA  . HIS B 237 ? 0.2748 0.3263 0.3013 -0.0032 0.0198  0.0446  223 HIS B CA  
5803 C C   . HIS B 237 ? 0.2843 0.3431 0.3159 -0.0048 0.0231  0.0490  223 HIS B C   
5804 O O   . HIS B 237 ? 0.2882 0.3501 0.3168 -0.0043 0.0265  0.0511  223 HIS B O   
5805 C CB  . HIS B 237 ? 0.2653 0.3124 0.2858 -0.0033 0.0186  0.0457  223 HIS B CB  
5806 C CG  . HIS B 237 ? 0.2973 0.3392 0.3132 -0.0010 0.0165  0.0416  223 HIS B CG  
5807 N ND1 . HIS B 237 ? 0.3087 0.3513 0.3192 0.0014  0.0180  0.0393  223 HIS B ND1 
5808 C CD2 . HIS B 237 ? 0.2804 0.3164 0.2964 -0.0008 0.0132  0.0395  223 HIS B CD2 
5809 C CE1 . HIS B 237 ? 0.3291 0.3674 0.3377 0.0029  0.0155  0.0363  223 HIS B CE1 
5810 N NE2 . HIS B 237 ? 0.2804 0.3147 0.2922 0.0018  0.0129  0.0364  223 HIS B NE2 
5811 N N   . GLY B 238 ? 0.2724 0.3342 0.3120 -0.0067 0.0221  0.0507  224 GLY B N   
5812 C CA  . GLY B 238 ? 0.2701 0.3404 0.3164 -0.0077 0.0256  0.0548  224 GLY B CA  
5813 C C   . GLY B 238 ? 0.2699 0.3418 0.3177 -0.0110 0.0262  0.0605  224 GLY B C   
5814 O O   . GLY B 238 ? 0.2578 0.3369 0.3080 -0.0108 0.0309  0.0638  224 GLY B O   
5815 N N   . LEU B 239 ? 0.2708 0.3359 0.3168 -0.0138 0.0219  0.0618  225 LEU B N   
5816 C CA  . LEU B 239 ? 0.2650 0.3302 0.3110 -0.0170 0.0221  0.0671  225 LEU B CA  
5817 C C   . LEU B 239 ? 0.3057 0.3707 0.3596 -0.0219 0.0185  0.0714  225 LEU B C   
5818 O O   . LEU B 239 ? 0.2961 0.3591 0.3499 -0.0252 0.0173  0.0758  225 LEU B O   
5819 C CB  . LEU B 239 ? 0.2650 0.3219 0.3022 -0.0163 0.0199  0.0659  225 LEU B CB  
5820 C CG  . LEU B 239 ? 0.2702 0.3280 0.2996 -0.0124 0.0233  0.0629  225 LEU B CG  
5821 C CD1 . LEU B 239 ? 0.3080 0.3575 0.3302 -0.0111 0.0199  0.0604  225 LEU B CD1 
5822 C CD2 . LEU B 239 ? 0.2914 0.3547 0.3187 -0.0127 0.0280  0.0670  225 LEU B CD2 
5823 N N   . LYS B 240 ? 0.2927 0.3595 0.3531 -0.0226 0.0164  0.0703  226 LYS B N   
5824 C CA  . LYS B 240 ? 0.3080 0.3747 0.3760 -0.0277 0.0124  0.0744  226 LYS B CA  
5825 C C   . LYS B 240 ? 0.3044 0.3793 0.3791 -0.0309 0.0153  0.0814  226 LYS B C   
5826 O O   . LYS B 240 ? 0.3120 0.3835 0.3883 -0.0355 0.0121  0.0857  226 LYS B O   
5827 C CB  . LYS B 240 ? 0.2716 0.3412 0.3460 -0.0275 0.0105  0.0725  226 LYS B CB  
5828 C CG  . LYS B 240 ? 0.3250 0.3917 0.4055 -0.0329 0.0045  0.0754  226 LYS B CG  
5829 C CD  . LYS B 240 ? 0.3115 0.3833 0.3996 -0.0329 0.0030  0.0747  226 LYS B CD  
5830 C CE  . LYS B 240 ? 0.3936 0.4639 0.4887 -0.0390 -0.0032 0.0789  226 LYS B CE  
5831 N NZ  . LYS B 240 ? 0.3660 0.4410 0.4690 -0.0397 -0.0058 0.0790  226 LYS B NZ  
5832 N N   . HIS B 241 ? 0.3306 0.4159 0.4092 -0.0285 0.0214  0.0829  227 HIS B N   
5833 C CA  . HIS B 241 ? 0.3634 0.4576 0.4491 -0.0313 0.0250  0.0899  227 HIS B CA  
5834 C C   . HIS B 241 ? 0.3666 0.4571 0.4453 -0.0327 0.0261  0.0927  227 HIS B C   
5835 O O   . HIS B 241 ? 0.3810 0.4738 0.4644 -0.0372 0.0257  0.0990  227 HIS B O   
5836 C CB  . HIS B 241 ? 0.4313 0.5370 0.5216 -0.0275 0.0321  0.0904  227 HIS B CB  
5837 C CG  . HIS B 241 ? 0.6382 0.7532 0.7339 -0.0293 0.0375  0.0974  227 HIS B CG  
5838 N ND1 . HIS B 241 ? 0.7018 0.8197 0.8060 -0.0352 0.0350  0.1042  227 HIS B ND1 
5839 C CD2 . HIS B 241 ? 0.6829 0.8047 0.7763 -0.0260 0.0453  0.0987  227 HIS B CD2 
5840 C CE1 . HIS B 241 ? 0.5949 0.7218 0.7025 -0.0355 0.0414  0.1097  227 HIS B CE1 
5841 N NE2 . HIS B 241 ? 0.6108 0.7400 0.7115 -0.0298 0.0479  0.1063  227 HIS B NE2 
5842 N N   . ALA B 242 ? 0.3359 0.4205 0.4033 -0.0290 0.0272  0.0885  228 ALA B N   
5843 C CA  . ALA B 242 ? 0.3331 0.4133 0.3933 -0.0302 0.0276  0.0911  228 ALA B CA  
5844 C C   . ALA B 242 ? 0.3088 0.3801 0.3692 -0.0348 0.0211  0.0933  228 ALA B C   
5845 O O   . ALA B 242 ? 0.3261 0.3968 0.3865 -0.0383 0.0210  0.0988  228 ALA B O   
5846 C CB  . ALA B 242 ? 0.3073 0.3826 0.3559 -0.0256 0.0290  0.0860  228 ALA B CB  
5847 N N   . LEU B 243 ? 0.3072 0.3709 0.3672 -0.0348 0.0157  0.0892  229 LEU B N   
5848 C CA  . LEU B 243 ? 0.3089 0.3628 0.3683 -0.0389 0.0094  0.0908  229 LEU B CA  
5849 C C   . LEU B 243 ? 0.3215 0.3792 0.3907 -0.0448 0.0073  0.0969  229 LEU B C   
5850 O O   . LEU B 243 ? 0.3153 0.3676 0.3843 -0.0491 0.0042  0.1011  229 LEU B O   
5851 C CB  . LEU B 243 ? 0.2710 0.3155 0.3267 -0.0371 0.0047  0.0846  229 LEU B CB  
5852 C CG  . LEU B 243 ? 0.2698 0.3059 0.3155 -0.0333 0.0041  0.0804  229 LEU B CG  
5853 C CD1 . LEU B 243 ? 0.2760 0.3030 0.3183 -0.0362 0.0005  0.0837  229 LEU B CD1 
5854 C CD2 . LEU B 243 ? 0.2672 0.3091 0.3082 -0.0290 0.0094  0.0789  229 LEU B CD2 
5855 N N   . GLN B 244 ? 0.2920 0.3587 0.3703 -0.0453 0.0086  0.0977  230 GLN B N   
5856 C CA  . GLN B 244 ? 0.3131 0.3849 0.4022 -0.0512 0.0066  0.1041  230 GLN B CA  
5857 C C   . GLN B 244 ? 0.3248 0.4039 0.4170 -0.0537 0.0110  0.1113  230 GLN B C   
5858 O O   . GLN B 244 ? 0.3265 0.4033 0.4222 -0.0594 0.0078  0.1169  230 GLN B O   
5859 C CB  . GLN B 244 ? 0.3338 0.4153 0.4329 -0.0506 0.0075  0.1038  230 GLN B CB  
5860 C CG  . GLN B 244 ? 0.3383 0.4128 0.4349 -0.0492 0.0027  0.0977  230 GLN B CG  
5861 C CD  . GLN B 244 ? 0.3626 0.4468 0.4688 -0.0482 0.0037  0.0976  230 GLN B CD  
5862 O OE1 . GLN B 244 ? 0.3667 0.4627 0.4787 -0.0457 0.0100  0.0997  230 GLN B OE1 
5863 N NE2 . GLN B 244 ? 0.3573 0.4362 0.4647 -0.0498 -0.0023 0.0951  230 GLN B NE2 
5864 N N   . LYS B 245 ? 0.3529 0.4400 0.4430 -0.0495 0.0184  0.1112  231 LYS B N   
5865 C CA  . LYS B 245 ? 0.3555 0.4497 0.4476 -0.0515 0.0234  0.1180  231 LYS B CA  
5866 C C   . LYS B 245 ? 0.3640 0.4484 0.4475 -0.0539 0.0208  0.1200  231 LYS B C   
5867 O O   . LYS B 245 ? 0.3705 0.4574 0.4575 -0.0585 0.0214  0.1271  231 LYS B O   
5868 C CB  . LYS B 245 ? 0.3639 0.4670 0.4532 -0.0460 0.0320  0.1167  231 LYS B CB  
5869 C CG  . LYS B 245 ? 0.4045 0.5156 0.4955 -0.0478 0.0381  0.1238  231 LYS B CG  
5870 C CD  . LYS B 245 ? 0.4221 0.5439 0.5133 -0.0427 0.0471  0.1232  231 LYS B CD  
5871 C CE  . LYS B 245 ? 0.4480 0.5711 0.5307 -0.0420 0.0531  0.1264  231 LYS B CE  
5872 N NZ  . LYS B 245 ? 0.4247 0.5538 0.5151 -0.0476 0.0545  0.1356  231 LYS B NZ  
5873 N N   . TRP B 246 ? 0.3527 0.4260 0.4257 -0.0508 0.0178  0.1143  232 TRP B N   
5874 C CA  . TRP B 246 ? 0.3323 0.3953 0.3971 -0.0524 0.0148  0.1157  232 TRP B CA  
5875 C C   . TRP B 246 ? 0.3545 0.4116 0.4244 -0.0590 0.0088  0.1205  232 TRP B C   
5876 O O   . TRP B 246 ? 0.3508 0.4072 0.4206 -0.0628 0.0089  0.1268  232 TRP B O   
5877 C CB  . TRP B 246 ? 0.3166 0.3695 0.3718 -0.0477 0.0120  0.1083  232 TRP B CB  
5878 C CG  . TRP B 246 ? 0.2927 0.3350 0.3391 -0.0477 0.0092  0.1088  232 TRP B CG  
5879 C CD1 . TRP B 246 ? 0.3176 0.3567 0.3630 -0.0518 0.0080  0.1150  232 TRP B CD1 
5880 C CD2 . TRP B 246 ? 0.2928 0.3265 0.3306 -0.0433 0.0071  0.1031  232 TRP B CD2 
5881 N NE1 . TRP B 246 ? 0.3172 0.3459 0.3538 -0.0499 0.0052  0.1134  232 TRP B NE1 
5882 C CE2 . TRP B 246 ? 0.3199 0.3456 0.3521 -0.0446 0.0047  0.1062  232 TRP B CE2 
5883 C CE3 . TRP B 246 ? 0.2914 0.3239 0.3263 -0.0384 0.0071  0.0960  232 TRP B CE3 
5884 C CZ2 . TRP B 246 ? 0.3066 0.3235 0.3311 -0.0410 0.0023  0.1025  232 TRP B CZ2 
5885 C CZ3 . TRP B 246 ? 0.2767 0.3007 0.3039 -0.0351 0.0048  0.0924  232 TRP B CZ3 
5886 C CH2 . TRP B 246 ? 0.2975 0.3141 0.3199 -0.0362 0.0025  0.0956  232 TRP B CH2 
5887 N N   . VAL B 247 ? 0.3413 0.3938 0.4153 -0.0608 0.0033  0.1180  233 VAL B N   
5888 C CA  . VAL B 247 ? 0.3389 0.3836 0.4160 -0.0672 -0.0032 0.1220  233 VAL B CA  
5889 C C   . VAL B 247 ? 0.3692 0.4246 0.4583 -0.0729 -0.0019 0.1299  233 VAL B C   
5890 O O   . VAL B 247 ? 0.3629 0.4138 0.4549 -0.0791 -0.0061 0.1353  233 VAL B O   
5891 C CB  . VAL B 247 ? 0.3443 0.3793 0.4208 -0.0677 -0.0099 0.1169  233 VAL B CB  
5892 C CG1 . VAL B 247 ? 0.3426 0.3687 0.4087 -0.0616 -0.0103 0.1091  233 VAL B CG1 
5893 C CG2 . VAL B 247 ? 0.3444 0.3891 0.4308 -0.0686 -0.0096 0.1166  233 VAL B CG2 
5894 N N   . LYS B 248 ? 0.3618 0.4316 0.4584 -0.0710 0.0039  0.1309  234 LYS B N   
5895 C CA  . LYS B 248 ? 0.3889 0.4708 0.4976 -0.0758 0.0065  0.1391  234 LYS B CA  
5896 C C   . LYS B 248 ? 0.3841 0.4686 0.4897 -0.0772 0.0110  0.1451  234 LYS B C   
5897 O O   . LYS B 248 ? 0.3875 0.4728 0.4987 -0.0836 0.0092  0.1525  234 LYS B O   
5898 C CB  . LYS B 248 ? 0.4014 0.4979 0.5187 -0.0724 0.0121  0.1383  234 LYS B CB  
5899 C CG  . LYS B 248 ? 0.4143 0.5246 0.5466 -0.0770 0.0144  0.1467  234 LYS B CG  
5900 C CD  . LYS B 248 ? 0.5880 0.7090 0.7203 -0.0749 0.0239  0.1511  234 LYS B CD  
5901 C CE  . LYS B 248 ? 0.5682 0.7020 0.7051 -0.0689 0.0315  0.1489  234 LYS B CE  
5902 N NZ  . LYS B 248 ? 0.5504 0.6898 0.6810 -0.0651 0.0407  0.1505  234 LYS B NZ  
5903 N N   . ASP B 249 ? 0.3993 0.4840 0.4952 -0.0716 0.0165  0.1420  235 ASP B N   
5904 C CA  . ASP B 249 ? 0.3855 0.4719 0.4767 -0.0727 0.0208  0.1475  235 ASP B CA  
5905 C C   . ASP B 249 ? 0.4121 0.4844 0.4959 -0.0759 0.0148  0.1490  235 ASP B C   
5906 O O   . ASP B 249 ? 0.3992 0.4719 0.4828 -0.0800 0.0158  0.1560  235 ASP B O   
5907 C CB  . ASP B 249 ? 0.4002 0.4903 0.4823 -0.0658 0.0279  0.1435  235 ASP B CB  
5908 C CG  . ASP B 249 ? 0.4154 0.5197 0.5045 -0.0626 0.0350  0.1433  235 ASP B CG  
5909 O OD1 . ASP B 249 ? 0.4201 0.5332 0.5225 -0.0661 0.0352  0.1477  235 ASP B OD1 
5910 O OD2 . ASP B 249 ? 0.4159 0.5223 0.4975 -0.0566 0.0403  0.1388  235 ASP B OD2 
5911 N N   . VAL B 250 ? 0.3927 0.4522 0.4701 -0.0741 0.0087  0.1427  236 VAL B N   
5912 C CA  . VAL B 250 ? 0.4091 0.4540 0.4789 -0.0762 0.0030  0.1433  236 VAL B CA  
5913 C C   . VAL B 250 ? 0.4102 0.4447 0.4825 -0.0791 -0.0051 0.1408  236 VAL B C   
5914 O O   . VAL B 250 ? 0.3966 0.4221 0.4626 -0.0751 -0.0081 0.1336  236 VAL B O   
5915 C CB  . VAL B 250 ? 0.4135 0.4516 0.4708 -0.0699 0.0040  0.1379  236 VAL B CB  
5916 C CG1 . VAL B 250 ? 0.4825 0.5066 0.5330 -0.0718 -0.0013 0.1395  236 VAL B CG1 
5917 C CG2 . VAL B 250 ? 0.4080 0.4558 0.4615 -0.0670 0.0118  0.1398  236 VAL B CG2 
5918 N N   . PRO B 251 ? 0.4034 0.4383 0.4842 -0.0862 -0.0088 0.1466  237 PRO B N   
5919 C CA  . PRO B 251 ? 0.4302 0.4539 0.5120 -0.0894 -0.0170 0.1441  237 PRO B CA  
5920 C C   . PRO B 251 ? 0.4529 0.4584 0.5232 -0.0879 -0.0221 0.1404  237 PRO B C   
5921 O O   . PRO B 251 ? 0.4868 0.4865 0.5522 -0.0892 -0.0224 0.1442  237 PRO B O   
5922 C CB  . PRO B 251 ? 0.4788 0.5060 0.5709 -0.0981 -0.0198 0.1528  237 PRO B CB  
5923 C CG  . PRO B 251 ? 0.4121 0.4575 0.5123 -0.0981 -0.0118 0.1583  237 PRO B CG  
5924 C CD  . PRO B 251 ? 0.4327 0.4785 0.5227 -0.0918 -0.0058 0.1558  237 PRO B CD  
5925 N N   . MET B 252 ? 0.4095 0.4058 0.4756 -0.0852 -0.0261 0.1332  238 MET B N   
5926 C CA  . MET B 252 ? 0.4207 0.3995 0.4766 -0.0832 -0.0309 0.1292  238 MET B CA  
5927 C C   . MET B 252 ? 0.4079 0.3790 0.4620 -0.0819 -0.0352 0.1224  238 MET B C   
5928 O O   . MET B 252 ? 0.3843 0.3644 0.4438 -0.0811 -0.0338 0.1200  238 MET B O   
5929 C CB  . MET B 252 ? 0.4175 0.3945 0.4646 -0.0761 -0.0270 0.1256  238 MET B CB  
5930 C CG  . MET B 252 ? 0.4166 0.4058 0.4642 -0.0702 -0.0209 0.1211  238 MET B CG  
5931 S SD  . MET B 252 ? 0.3829 0.3704 0.4206 -0.0629 -0.0171 0.1180  238 MET B SD  
5932 C CE  . MET B 252 ? 0.3602 0.3610 0.3999 -0.0576 -0.0113 0.1125  238 MET B CE  
5933 N N   . ALA B 253 ? 0.3791 0.3330 0.4250 -0.0815 -0.0404 0.1193  239 ALA B N   
5934 C CA  . ALA B 253 ? 0.3655 0.3102 0.4070 -0.0793 -0.0440 0.1122  239 ALA B CA  
5935 C C   . ALA B 253 ? 0.3789 0.3308 0.4183 -0.0717 -0.0388 0.1058  239 ALA B C   
5936 O O   . ALA B 253 ? 0.3488 0.3035 0.3846 -0.0667 -0.0346 0.1049  239 ALA B O   
5937 C CB  . ALA B 253 ? 0.3734 0.2979 0.4050 -0.0787 -0.0490 0.1098  239 ALA B CB  
5938 N N   . HIS B 254 ? 0.3651 0.3200 0.4068 -0.0711 -0.0395 0.1018  240 HIS B N   
5939 C CA  . HIS B 254 ? 0.3476 0.3092 0.3877 -0.0643 -0.0350 0.0958  240 HIS B CA  
5940 C C   . HIS B 254 ? 0.3286 0.2840 0.3662 -0.0636 -0.0383 0.0901  240 HIS B C   
5941 O O   . HIS B 254 ? 0.3409 0.2914 0.3806 -0.0689 -0.0436 0.0915  240 HIS B O   
5942 C CB  . HIS B 254 ? 0.3274 0.3074 0.3756 -0.0636 -0.0290 0.0985  240 HIS B CB  
5943 C CG  . HIS B 254 ? 0.3344 0.3234 0.3929 -0.0694 -0.0303 0.1031  240 HIS B CG  
5944 N ND1 . HIS B 254 ? 0.3595 0.3488 0.4234 -0.0762 -0.0328 0.1104  240 HIS B ND1 
5945 C CD2 . HIS B 254 ? 0.3270 0.3255 0.3923 -0.0693 -0.0294 0.1019  240 HIS B CD2 
5946 C CE1 . HIS B 254 ? 0.3625 0.3616 0.4366 -0.0801 -0.0335 0.1135  240 HIS B CE1 
5947 N NE2 . HIS B 254 ? 0.3098 0.3146 0.3849 -0.0759 -0.0314 0.1084  240 HIS B NE2 
5948 N N   . ALA B 255 ? 0.3339 0.2900 0.3672 -0.0571 -0.0354 0.0839  241 ALA B N   
5949 C CA  . ALA B 255 ? 0.3041 0.2544 0.3339 -0.0557 -0.0378 0.0781  241 ALA B CA  
5950 C C   . ALA B 255 ? 0.3067 0.2652 0.3358 -0.0493 -0.0327 0.0732  241 ALA B C   
5951 O O   . ALA B 255 ? 0.2993 0.2653 0.3290 -0.0457 -0.0279 0.0736  241 ALA B O   
5952 C CB  . ALA B 255 ? 0.3154 0.2471 0.3352 -0.0548 -0.0420 0.0745  241 ALA B CB  
5953 N N   . THR B 256 ? 0.3081 0.2645 0.3357 -0.0482 -0.0341 0.0686  242 THR B N   
5954 C CA  . THR B 256 ? 0.2912 0.2504 0.3155 -0.0419 -0.0304 0.0630  242 THR B CA  
5955 C C   . THR B 256 ? 0.3045 0.2490 0.3195 -0.0398 -0.0332 0.0576  242 THR B C   
5956 O O   . THR B 256 ? 0.3093 0.2413 0.3200 -0.0430 -0.0379 0.0581  242 THR B O   
5957 C CB  . THR B 256 ? 0.3034 0.2746 0.3340 -0.0418 -0.0285 0.0622  242 THR B CB  
5958 O OG1 . THR B 256 ? 0.2890 0.2538 0.3179 -0.0441 -0.0330 0.0599  242 THR B OG1 
5959 C CG2 . THR B 256 ? 0.2838 0.2682 0.3245 -0.0453 -0.0267 0.0682  242 THR B CG2 
5960 N N   . MET B 257 ? 0.2922 0.2378 0.3038 -0.0342 -0.0300 0.0526  243 MET B N   
5961 C CA  . MET B 257 ? 0.3065 0.2405 0.3100 -0.0318 -0.0317 0.0472  243 MET B CA  
5962 C C   . MET B 257 ? 0.2873 0.2263 0.2927 -0.0325 -0.0321 0.0449  243 MET B C   
5963 O O   . MET B 257 ? 0.2311 0.1822 0.2445 -0.0345 -0.0312 0.0476  243 MET B O   
5964 C CB  . MET B 257 ? 0.3128 0.2446 0.3116 -0.0252 -0.0278 0.0437  243 MET B CB  
5965 C CG  . MET B 257 ? 0.3171 0.2396 0.3123 -0.0244 -0.0287 0.0454  243 MET B CG  
5966 S SD  . MET B 257 ? 0.3454 0.2656 0.3364 -0.0165 -0.0247 0.0419  243 MET B SD  
5967 C CE  . MET B 257 ? 0.3074 0.2445 0.3056 -0.0153 -0.0205 0.0448  243 MET B CE  
5968 N N   . LEU B 258 ? 0.2995 0.2292 0.2974 -0.0305 -0.0333 0.0400  244 LEU B N   
5969 C CA  . LEU B 258 ? 0.3079 0.2407 0.3067 -0.0317 -0.0346 0.0381  244 LEU B CA  
5970 C C   . LEU B 258 ? 0.2938 0.2420 0.2997 -0.0290 -0.0301 0.0380  244 LEU B C   
5971 O O   . LEU B 258 ? 0.2825 0.2387 0.2946 -0.0317 -0.0312 0.0398  244 LEU B O   
5972 C CB  . LEU B 258 ? 0.3113 0.2315 0.2995 -0.0291 -0.0356 0.0326  244 LEU B CB  
5973 C CG  . LEU B 258 ? 0.3234 0.2448 0.3104 -0.0300 -0.0372 0.0302  244 LEU B CG  
5974 C CD1 . LEU B 258 ? 0.3149 0.2397 0.3079 -0.0366 -0.0423 0.0342  244 LEU B CD1 
5975 C CD2 . LEU B 258 ? 0.3535 0.2600 0.3282 -0.0280 -0.0384 0.0251  244 LEU B CD2 
5976 N N   . MET B 259 ? 0.2769 0.2292 0.2821 -0.0239 -0.0253 0.0362  245 MET B N   
5977 C CA  . MET B 259 ? 0.2944 0.2591 0.3045 -0.0212 -0.0213 0.0353  245 MET B CA  
5978 C C   . MET B 259 ? 0.2905 0.2675 0.3097 -0.0237 -0.0201 0.0400  245 MET B C   
5979 O O   . MET B 259 ? 0.3043 0.2903 0.3285 -0.0235 -0.0187 0.0400  245 MET B O   
5980 C CB  . MET B 259 ? 0.3095 0.2757 0.3170 -0.0158 -0.0170 0.0330  245 MET B CB  
5981 C CG  . MET B 259 ? 0.3036 0.2636 0.3048 -0.0121 -0.0161 0.0280  245 MET B CG  
5982 S SD  . MET B 259 ? 0.3394 0.3025 0.3395 -0.0063 -0.0115 0.0262  245 MET B SD  
5983 C CE  . MET B 259 ? 0.2673 0.2424 0.2715 -0.0044 -0.0083 0.0245  245 MET B CE  
5984 N N   . GLY B 260 ? 0.2766 0.2542 0.2981 -0.0258 -0.0203 0.0440  246 GLY B N   
5985 C CA  . GLY B 260 ? 0.2742 0.2636 0.3039 -0.0277 -0.0182 0.0487  246 GLY B CA  
5986 C C   . GLY B 260 ? 0.2663 0.2573 0.3020 -0.0335 -0.0218 0.0531  246 GLY B C   
5987 O O   . GLY B 260 ? 0.2582 0.2592 0.3014 -0.0354 -0.0199 0.0577  246 GLY B O   
5988 N N   . LYS B 261 ? 0.2914 0.2730 0.3241 -0.0365 -0.0271 0.0521  247 LYS B N   
5989 C CA  . LYS B 261 ? 0.2945 0.2773 0.3332 -0.0426 -0.0315 0.0565  247 LYS B CA  
5990 C C   . LYS B 261 ? 0.2837 0.2815 0.3328 -0.0430 -0.0292 0.0590  247 LYS B C   
5991 O O   . LYS B 261 ? 0.2805 0.2833 0.3297 -0.0391 -0.0264 0.0557  247 LYS B O   
5992 C CB  . LYS B 261 ? 0.2999 0.2697 0.3319 -0.0450 -0.0375 0.0537  247 LYS B CB  
5993 C CG  . LYS B 261 ? 0.3191 0.2904 0.3570 -0.0510 -0.0428 0.0572  247 LYS B CG  
5994 C CD  . LYS B 261 ? 0.3412 0.2968 0.3698 -0.0537 -0.0493 0.0544  247 LYS B CD  
5995 C CE  . LYS B 261 ? 0.3783 0.3221 0.4023 -0.0573 -0.0529 0.0563  247 LYS B CE  
5996 N NZ  . LYS B 261 ? 0.3323 0.2781 0.3638 -0.0650 -0.0585 0.0623  247 LYS B NZ  
5997 N N   . GLY B 262 ? 0.3117 0.3169 0.3699 -0.0474 -0.0300 0.0651  248 GLY B N   
5998 C CA  . GLY B 262 ? 0.2746 0.2950 0.3435 -0.0471 -0.0267 0.0682  248 GLY B CA  
5999 C C   . GLY B 262 ? 0.2904 0.3206 0.3632 -0.0452 -0.0204 0.0713  248 GLY B C   
6000 O O   . GLY B 262 ? 0.2885 0.3313 0.3710 -0.0457 -0.0174 0.0752  248 GLY B O   
6001 N N   . ILE B 263 ? 0.2768 0.3015 0.3423 -0.0431 -0.0184 0.0700  249 ILE B N   
6002 C CA  . ILE B 263 ? 0.2660 0.2987 0.3338 -0.0419 -0.0130 0.0733  249 ILE B CA  
6003 C C   . ILE B 263 ? 0.2961 0.3343 0.3725 -0.0475 -0.0140 0.0807  249 ILE B C   
6004 O O   . ILE B 263 ? 0.2819 0.3320 0.3651 -0.0473 -0.0092 0.0846  249 ILE B O   
6005 C CB  . ILE B 263 ? 0.2667 0.2911 0.3249 -0.0392 -0.0120 0.0710  249 ILE B CB  
6006 C CG1 . ILE B 263 ? 0.2806 0.3048 0.3329 -0.0331 -0.0088 0.0650  249 ILE B CG1 
6007 C CG2 . ILE B 263 ? 0.2545 0.2841 0.3143 -0.0402 -0.0085 0.0760  249 ILE B CG2 
6008 C CD1 . ILE B 263 ? 0.2339 0.2487 0.2772 -0.0304 -0.0090 0.0623  249 ILE B CD1 
6009 N N   . PHE B 264 ? 0.2743 0.3038 0.3503 -0.0528 -0.0202 0.0828  250 PHE B N   
6010 C CA  . PHE B 264 ? 0.2773 0.3102 0.3607 -0.0588 -0.0220 0.0900  250 PHE B CA  
6011 C C   . PHE B 264 ? 0.2974 0.3327 0.3894 -0.0640 -0.0272 0.0929  250 PHE B C   
6012 O O   . PHE B 264 ? 0.2980 0.3263 0.3866 -0.0641 -0.0317 0.0889  250 PHE B O   
6013 C CB  . PHE B 264 ? 0.2853 0.3054 0.3617 -0.0616 -0.0256 0.0912  250 PHE B CB  
6014 C CG  . PHE B 264 ? 0.2781 0.2963 0.3474 -0.0575 -0.0211 0.0900  250 PHE B CG  
6015 C CD1 . PHE B 264 ? 0.2840 0.3126 0.3572 -0.0571 -0.0156 0.0945  250 PHE B CD1 
6016 C CD2 . PHE B 264 ? 0.2882 0.2940 0.3466 -0.0539 -0.0225 0.0846  250 PHE B CD2 
6017 C CE1 . PHE B 264 ? 0.2891 0.3154 0.3550 -0.0535 -0.0122 0.0936  250 PHE B CE1 
6018 C CE2 . PHE B 264 ? 0.2631 0.2674 0.3156 -0.0502 -0.0191 0.0839  250 PHE B CE2 
6019 C CZ  . PHE B 264 ? 0.2807 0.2949 0.3366 -0.0502 -0.0143 0.0884  250 PHE B CZ  
6020 N N   . ASP B 265 ? 0.3062 0.3517 0.4093 -0.0685 -0.0266 0.1002  251 ASP B N   
6021 C CA  . ASP B 265 ? 0.3196 0.3658 0.4313 -0.0754 -0.0331 0.1048  251 ASP B CA  
6022 C C   . ASP B 265 ? 0.3317 0.3617 0.4356 -0.0803 -0.0398 0.1051  251 ASP B C   
6023 O O   . ASP B 265 ? 0.3244 0.3522 0.4270 -0.0823 -0.0388 0.1087  251 ASP B O   
6024 C CB  . ASP B 265 ? 0.3302 0.3919 0.4562 -0.0789 -0.0299 0.1132  251 ASP B CB  
6025 C CG  . ASP B 265 ? 0.3730 0.4383 0.5103 -0.0859 -0.0365 0.1185  251 ASP B CG  
6026 O OD1 . ASP B 265 ? 0.3568 0.4090 0.4890 -0.0905 -0.0447 0.1174  251 ASP B OD1 
6027 O OD2 . ASP B 265 ? 0.3375 0.4187 0.4887 -0.0866 -0.0334 0.1237  251 ASP B OD2 
6028 N N   . GLU B 266 ? 0.3080 0.3262 0.4062 -0.0821 -0.0467 0.1014  252 GLU B N   
6029 C CA  . GLU B 266 ? 0.3438 0.3443 0.4323 -0.0858 -0.0530 0.1004  252 GLU B CA  
6030 C C   . GLU B 266 ? 0.3747 0.3736 0.4703 -0.0948 -0.0597 0.1072  252 GLU B C   
6031 O O   . GLU B 266 ? 0.3913 0.3743 0.4789 -0.0986 -0.0660 0.1065  252 GLU B O   
6032 C CB  . GLU B 266 ? 0.3268 0.3132 0.4033 -0.0829 -0.0565 0.0925  252 GLU B CB  
6033 C CG  . GLU B 266 ? 0.3251 0.3158 0.3972 -0.0745 -0.0500 0.0864  252 GLU B CG  
6034 C CD  . GLU B 266 ? 0.3502 0.3271 0.4097 -0.0712 -0.0524 0.0788  252 GLU B CD  
6035 O OE1 . GLU B 266 ? 0.3516 0.3194 0.4080 -0.0750 -0.0591 0.0778  252 GLU B OE1 
6036 O OE2 . GLU B 266 ? 0.3322 0.3073 0.3850 -0.0648 -0.0477 0.0740  252 GLU B OE2 
6037 N N   . ARG B 267 ? 0.3704 0.3853 0.4809 -0.0983 -0.0586 0.1140  253 ARG B N   
6038 C CA  . ARG B 267 ? 0.4050 0.4212 0.5244 -0.1071 -0.0640 0.1219  253 ARG B CA  
6039 C C   . ARG B 267 ? 0.4186 0.4388 0.5408 -0.1086 -0.0598 0.1276  253 ARG B C   
6040 O O   . ARG B 267 ? 0.4336 0.4513 0.5604 -0.1161 -0.0645 0.1339  253 ARG B O   
6041 C CB  . ARG B 267 ? 0.3827 0.4155 0.5185 -0.1102 -0.0647 0.1272  253 ARG B CB  
6042 C CG  . ARG B 267 ? 0.3853 0.4158 0.5196 -0.1089 -0.0689 0.1225  253 ARG B CG  
6043 C CD  . ARG B 267 ? 0.3799 0.4297 0.5316 -0.1097 -0.0673 0.1276  253 ARG B CD  
6044 N NE  . ARG B 267 ? 0.3680 0.4327 0.5248 -0.1027 -0.0567 0.1276  253 ARG B NE  
6045 C CZ  . ARG B 267 ? 0.3470 0.4288 0.5170 -0.1004 -0.0525 0.1304  253 ARG B CZ  
6046 N NH1 . ARG B 267 ? 0.3468 0.4347 0.5279 -0.1046 -0.0582 0.1340  253 ARG B NH1 
6047 N NH2 . ARG B 267 ? 0.3417 0.4342 0.5136 -0.0937 -0.0427 0.1296  253 ARG B NH2 
6048 N N   . HIS B 268 ? 0.4143 0.4403 0.5334 -0.1018 -0.0513 0.1256  254 HIS B N   
6049 C CA  . HIS B 268 ? 0.4419 0.4739 0.5639 -0.1026 -0.0462 0.1311  254 HIS B CA  
6050 C C   . HIS B 268 ? 0.4528 0.4681 0.5649 -0.1058 -0.0506 0.1316  254 HIS B C   
6051 O O   . HIS B 268 ? 0.4357 0.4345 0.5360 -0.1044 -0.0551 0.1256  254 HIS B O   
6052 C CB  . HIS B 268 ? 0.4766 0.5169 0.5954 -0.0943 -0.0367 0.1278  254 HIS B CB  
6053 C CG  . HIS B 268 ? 0.6631 0.7175 0.7898 -0.0947 -0.0297 0.1347  254 HIS B CG  
6054 N ND1 . HIS B 268 ? 0.7623 0.8346 0.9028 -0.0952 -0.0254 0.1394  254 HIS B ND1 
6055 C CD2 . HIS B 268 ? 0.6553 0.7087 0.7778 -0.0945 -0.0260 0.1377  254 HIS B CD2 
6056 C CE1 . HIS B 268 ? 0.7665 0.8478 0.9105 -0.0952 -0.0190 0.1449  254 HIS B CE1 
6057 N NE2 . HIS B 268 ? 0.7242 0.7942 0.8571 -0.0951 -0.0195 0.1440  254 HIS B NE2 
6058 N N   . VAL B 269 ? 0.4565 0.4761 0.5738 -0.1100 -0.0491 0.1391  255 VAL B N   
6059 C CA  . VAL B 269 ? 0.4563 0.4607 0.5648 -0.1129 -0.0528 0.1404  255 VAL B CA  
6060 C C   . VAL B 269 ? 0.4597 0.4557 0.5548 -0.1051 -0.0488 0.1337  255 VAL B C   
6061 O O   . VAL B 269 ? 0.4277 0.4338 0.5226 -0.0986 -0.0415 0.1312  255 VAL B O   
6062 C CB  . VAL B 269 ? 0.4579 0.4704 0.5752 -0.1189 -0.0511 0.1503  255 VAL B CB  
6063 C CG1 . VAL B 269 ? 0.4794 0.5035 0.5969 -0.1135 -0.0414 0.1517  255 VAL B CG1 
6064 C CG2 . VAL B 269 ? 0.5249 0.5202 0.6355 -0.1246 -0.0579 0.1528  255 VAL B CG2 
6065 N N   . GLY B 270 ? 0.4332 0.4104 0.5170 -0.1054 -0.0540 0.1305  256 GLY B N   
6066 C CA  . GLY B 270 ? 0.4267 0.3950 0.4984 -0.0982 -0.0512 0.1245  256 GLY B CA  
6067 C C   . GLY B 270 ? 0.4148 0.3760 0.4787 -0.0925 -0.0520 0.1154  256 GLY B C   
6068 O O   . GLY B 270 ? 0.3781 0.3296 0.4318 -0.0869 -0.0509 0.1103  256 GLY B O   
6069 N N   . PHE B 271 ? 0.3916 0.3571 0.4602 -0.0937 -0.0542 0.1135  257 PHE B N   
6070 C CA  . PHE B 271 ? 0.3904 0.3483 0.4512 -0.0890 -0.0555 0.1052  257 PHE B CA  
6071 C C   . PHE B 271 ? 0.4148 0.3560 0.4697 -0.0938 -0.0642 0.1037  257 PHE B C   
6072 O O   . PHE B 271 ? 0.4120 0.3553 0.4740 -0.1008 -0.0693 0.1080  257 PHE B O   
6073 C CB  . PHE B 271 ? 0.3416 0.3142 0.4098 -0.0866 -0.0522 0.1036  257 PHE B CB  
6074 C CG  . PHE B 271 ? 0.3526 0.3187 0.4125 -0.0810 -0.0523 0.0952  257 PHE B CG  
6075 C CD1 . PHE B 271 ? 0.3568 0.3127 0.4128 -0.0837 -0.0588 0.0923  257 PHE B CD1 
6076 C CD2 . PHE B 271 ? 0.3362 0.3058 0.3916 -0.0733 -0.0461 0.0905  257 PHE B CD2 
6077 C CE1 . PHE B 271 ? 0.3448 0.2946 0.3927 -0.0787 -0.0586 0.0849  257 PHE B CE1 
6078 C CE2 . PHE B 271 ? 0.3275 0.2914 0.3757 -0.0685 -0.0460 0.0832  257 PHE B CE2 
6079 C CZ  . PHE B 271 ? 0.3461 0.3001 0.3905 -0.0711 -0.0520 0.0805  257 PHE B CZ  
6080 N N   . TYR B 272 ? 0.3918 0.3165 0.4338 -0.0900 -0.0658 0.0974  258 TYR B N   
6081 C CA  . TYR B 272 ? 0.4074 0.3134 0.4410 -0.0938 -0.0737 0.0951  258 TYR B CA  
6082 C C   . TYR B 272 ? 0.3961 0.2945 0.4210 -0.0895 -0.0747 0.0871  258 TYR B C   
6083 O O   . TYR B 272 ? 0.4480 0.3305 0.4646 -0.0924 -0.0811 0.0845  258 TYR B O   
6084 C CB  . TYR B 272 ? 0.4126 0.3020 0.4369 -0.0937 -0.0756 0.0953  258 TYR B CB  
6085 C CG  . TYR B 272 ? 0.4549 0.3505 0.4862 -0.0975 -0.0744 0.1031  258 TYR B CG  
6086 C CD1 . TYR B 272 ? 0.4292 0.3348 0.4626 -0.0925 -0.0673 0.1043  258 TYR B CD1 
6087 C CD2 . TYR B 272 ? 0.4775 0.3690 0.5130 -0.1064 -0.0805 0.1095  258 TYR B CD2 
6088 C CE1 . TYR B 272 ? 0.4480 0.3587 0.4867 -0.0960 -0.0660 0.1117  258 TYR B CE1 
6089 C CE2 . TYR B 272 ? 0.4957 0.3930 0.5376 -0.1101 -0.0791 0.1171  258 TYR B CE2 
6090 C CZ  . TYR B 272 ? 0.4889 0.3957 0.5320 -0.1047 -0.0717 0.1181  258 TYR B CZ  
6091 O OH  . TYR B 272 ? 0.5136 0.4258 0.5621 -0.1085 -0.0703 0.1258  258 TYR B OH  
6092 N N   . GLY B 273 ? 0.3951 0.3040 0.4212 -0.0830 -0.0686 0.0832  259 GLY B N   
6093 C CA  . GLY B 273 ? 0.3985 0.3005 0.4163 -0.0787 -0.0689 0.0758  259 GLY B CA  
6094 C C   . GLY B 273 ? 0.3818 0.2878 0.3959 -0.0699 -0.0617 0.0709  259 GLY B C   
6095 O O   . GLY B 273 ? 0.3669 0.2784 0.3832 -0.0670 -0.0572 0.0728  259 GLY B O   
6096 N N   . THR B 274 ? 0.3558 0.2592 0.3644 -0.0658 -0.0609 0.0648  260 THR B N   
6097 C CA  . THR B 274 ? 0.3702 0.2778 0.3758 -0.0578 -0.0545 0.0602  260 THR B CA  
6098 C C   . THR B 274 ? 0.3944 0.2870 0.3893 -0.0536 -0.0540 0.0567  260 THR B C   
6099 O O   . THR B 274 ? 0.3983 0.2744 0.3841 -0.0551 -0.0585 0.0543  260 THR B O   
6100 C CB  . THR B 274 ? 0.3647 0.2754 0.3687 -0.0552 -0.0537 0.0554  260 THR B CB  
6101 O OG1 . THR B 274 ? 0.3532 0.2787 0.3683 -0.0585 -0.0538 0.0591  260 THR B OG1 
6102 C CG2 . THR B 274 ? 0.3396 0.2543 0.3407 -0.0472 -0.0472 0.0508  260 THR B CG2 
6103 N N   . TYR B 275 ? 0.3747 0.2728 0.3706 -0.0484 -0.0486 0.0565  261 TYR B N   
6104 C CA  . TYR B 275 ? 0.3887 0.2747 0.3763 -0.0437 -0.0475 0.0538  261 TYR B CA  
6105 C C   . TYR B 275 ? 0.3815 0.2627 0.3619 -0.0377 -0.0452 0.0469  261 TYR B C   
6106 O O   . TYR B 275 ? 0.3790 0.2715 0.3629 -0.0346 -0.0413 0.0449  261 TYR B O   
6107 C CB  . TYR B 275 ? 0.3794 0.2741 0.3714 -0.0407 -0.0431 0.0568  261 TYR B CB  
6108 C CG  . TYR B 275 ? 0.3820 0.2664 0.3674 -0.0354 -0.0418 0.0547  261 TYR B CG  
6109 C CD1 . TYR B 275 ? 0.4036 0.2720 0.3829 -0.0371 -0.0457 0.0556  261 TYR B CD1 
6110 C CD2 . TYR B 275 ? 0.3863 0.2769 0.3718 -0.0288 -0.0368 0.0521  261 TYR B CD2 
6111 C CE1 . TYR B 275 ? 0.4261 0.2851 0.3999 -0.0318 -0.0444 0.0540  261 TYR B CE1 
6112 C CE2 . TYR B 275 ? 0.4071 0.2893 0.3878 -0.0238 -0.0356 0.0507  261 TYR B CE2 
6113 C CZ  . TYR B 275 ? 0.4183 0.2848 0.3934 -0.0251 -0.0393 0.0517  261 TYR B CZ  
6114 O OH  . TYR B 275 ? 0.4376 0.2956 0.4084 -0.0197 -0.0380 0.0505  261 TYR B OH  
6115 N N   . SER B 276 ? 0.4129 0.2769 0.3831 -0.0363 -0.0475 0.0434  262 SER B N   
6116 C CA  . SER B 276 ? 0.4308 0.2892 0.3936 -0.0303 -0.0447 0.0371  262 SER B CA  
6117 C C   . SER B 276 ? 0.4747 0.3173 0.4287 -0.0260 -0.0443 0.0348  262 SER B C   
6118 O O   . SER B 276 ? 0.4854 0.3143 0.4294 -0.0238 -0.0451 0.0302  262 SER B O   
6119 C CB  . SER B 276 ? 0.4610 0.3148 0.4191 -0.0330 -0.0479 0.0341  262 SER B CB  
6120 O OG  . SER B 276 ? 0.5093 0.3437 0.4565 -0.0350 -0.0525 0.0321  262 SER B OG  
6121 N N   . GLY B 277 ? 0.4632 0.3075 0.4206 -0.0244 -0.0430 0.0382  263 GLY B N   
6122 C CA  . GLY B 277 ? 0.4683 0.2989 0.4188 -0.0195 -0.0421 0.0363  263 GLY B CA  
6123 C C   . GLY B 277 ? 0.5049 0.3158 0.4463 -0.0231 -0.0476 0.0359  263 GLY B C   
6124 O O   . GLY B 277 ? 0.4970 0.3061 0.4402 -0.0303 -0.0526 0.0397  263 GLY B O   
6125 N N   . SER B 278 ? 0.5183 0.3139 0.4495 -0.0180 -0.0466 0.0311  264 SER B N   
6126 C CA  . SER B 278 ? 0.5375 0.3118 0.4580 -0.0207 -0.0517 0.0300  264 SER B CA  
6127 C C   . SER B 278 ? 0.5431 0.3124 0.4589 -0.0273 -0.0568 0.0286  264 SER B C   
6128 O O   . SER B 278 ? 0.5958 0.3488 0.5038 -0.0318 -0.0625 0.0288  264 SER B O   
6129 C CB  . SER B 278 ? 0.5785 0.3374 0.4886 -0.0130 -0.0487 0.0249  264 SER B CB  
6130 O OG  . SER B 278 ? 0.5857 0.3444 0.4904 -0.0092 -0.0454 0.0193  264 SER B OG  
6131 N N   . ALA B 279 ? 0.5190 0.3011 0.4389 -0.0280 -0.0553 0.0273  265 ALA B N   
6132 C CA  . ALA B 279 ? 0.5579 0.3365 0.4742 -0.0344 -0.0605 0.0266  265 ALA B CA  
6133 C C   . ALA B 279 ? 0.5396 0.3283 0.4662 -0.0427 -0.0651 0.0329  265 ALA B C   
6134 O O   . ALA B 279 ? 0.5524 0.3391 0.4778 -0.0489 -0.0704 0.0334  265 ALA B O   
6135 C CB  . ALA B 279 ? 0.5899 0.3771 0.5059 -0.0314 -0.0571 0.0226  265 ALA B CB  
6136 N N   . SER B 280 ? 0.5368 0.3365 0.4735 -0.0431 -0.0633 0.0380  266 SER B N   
6137 C CA  . SER B 280 ? 0.5149 0.3256 0.4622 -0.0506 -0.0666 0.0445  266 SER B CA  
6138 C C   . SER B 280 ? 0.5446 0.3401 0.4870 -0.0581 -0.0745 0.0469  266 SER B C   
6139 O O   . SER B 280 ? 0.5477 0.3244 0.4796 -0.0570 -0.0767 0.0448  266 SER B O   
6140 C CB  . SER B 280 ? 0.4836 0.3060 0.4401 -0.0491 -0.0628 0.0494  266 SER B CB  
6141 O OG  . SER B 280 ? 0.4516 0.2860 0.4115 -0.0421 -0.0561 0.0471  266 SER B OG  
6142 N N   . ALA B 281 ? 0.5254 0.3295 0.4760 -0.0658 -0.0787 0.0516  267 ALA B N   
6143 C CA  . ALA B 281 ? 0.5498 0.3430 0.4991 -0.0739 -0.0861 0.0559  267 ALA B CA  
6144 C C   . ALA B 281 ? 0.5454 0.3347 0.4961 -0.0734 -0.0852 0.0597  267 ALA B C   
6145 O O   . ALA B 281 ? 0.5429 0.3450 0.5007 -0.0692 -0.0793 0.0617  267 ALA B O   
6146 C CB  . ALA B 281 ? 0.5371 0.3446 0.4987 -0.0819 -0.0897 0.0616  267 ALA B CB  
6147 N N   . GLY B 282 ? 0.5561 0.3266 0.4990 -0.0777 -0.0913 0.0607  268 GLY B N   
6148 C CA  . GLY B 282 ? 0.5265 0.2905 0.4690 -0.0770 -0.0909 0.0640  268 GLY B CA  
6149 C C   . GLY B 282 ? 0.5393 0.3214 0.4961 -0.0806 -0.0891 0.0719  268 GLY B C   
6150 O O   . GLY B 282 ? 0.5407 0.3261 0.4998 -0.0768 -0.0851 0.0741  268 GLY B O   
6151 N N   . ALA B 283 ? 0.5315 0.3259 0.4981 -0.0879 -0.0919 0.0765  269 ALA B N   
6152 C CA  . ALA B 283 ? 0.5117 0.3244 0.4920 -0.0911 -0.0894 0.0841  269 ALA B CA  
6153 C C   . ALA B 283 ? 0.4937 0.3241 0.4798 -0.0837 -0.0807 0.0829  269 ALA B C   
6154 O O   . ALA B 283 ? 0.4739 0.3140 0.4663 -0.0831 -0.0771 0.0876  269 ALA B O   
6155 C CB  . ALA B 283 ? 0.4589 0.2822 0.4493 -0.0997 -0.0936 0.0890  269 ALA B CB  
6156 N N   . VAL B 284 ? 0.4793 0.3137 0.4628 -0.0783 -0.0775 0.0767  270 VAL B N   
6157 C CA  . VAL B 284 ? 0.4662 0.3159 0.4543 -0.0713 -0.0697 0.0752  270 VAL B CA  
6158 C C   . VAL B 284 ? 0.4739 0.3159 0.4555 -0.0645 -0.0664 0.0730  270 VAL B C   
6159 O O   . VAL B 284 ? 0.4262 0.2790 0.4129 -0.0615 -0.0617 0.0756  270 VAL B O   
6160 C CB  . VAL B 284 ? 0.4713 0.3262 0.4581 -0.0677 -0.0677 0.0693  270 VAL B CB  
6161 C CG1 . VAL B 284 ? 0.4261 0.2966 0.4177 -0.0610 -0.0601 0.0678  270 VAL B CG1 
6162 C CG2 . VAL B 284 ? 0.4281 0.2895 0.4213 -0.0745 -0.0719 0.0717  270 VAL B CG2 
6163 N N   . LYS B 285 ? 0.4947 0.3177 0.4650 -0.0618 -0.0688 0.0683  271 LYS B N   
6164 C CA  . LYS B 285 ? 0.5159 0.3307 0.4806 -0.0552 -0.0660 0.0665  271 LYS B CA  
6165 C C   . LYS B 285 ? 0.4981 0.3138 0.4669 -0.0578 -0.0666 0.0733  271 LYS B C   
6166 O O   . LYS B 285 ? 0.4860 0.3090 0.4576 -0.0532 -0.0622 0.0747  271 LYS B O   
6167 C CB  . LYS B 285 ? 0.5171 0.3094 0.4687 -0.0529 -0.0691 0.0612  271 LYS B CB  
6168 C CG  . LYS B 285 ? 0.5303 0.3184 0.4761 -0.0432 -0.0640 0.0555  271 LYS B CG  
6169 C CD  . LYS B 285 ? 0.5677 0.3337 0.5002 -0.0411 -0.0667 0.0501  271 LYS B CD  
6170 C CE  . LYS B 285 ? 0.5377 0.3016 0.4656 -0.0435 -0.0687 0.0458  271 LYS B CE  
6171 N NZ  . LYS B 285 ? 0.5885 0.3367 0.5038 -0.0372 -0.0671 0.0386  271 LYS B NZ  
6172 N N   . GLU B 286 ? 0.4912 0.3002 0.4609 -0.0658 -0.0724 0.0780  272 GLU B N   
6173 C CA  . GLU B 286 ? 0.5245 0.3333 0.4977 -0.0691 -0.0734 0.0850  272 GLU B CA  
6174 C C   . GLU B 286 ? 0.4800 0.3109 0.4646 -0.0703 -0.0689 0.0903  272 GLU B C   
6175 O O   . GLU B 286 ? 0.4849 0.3193 0.4712 -0.0685 -0.0664 0.0941  272 GLU B O   
6176 C CB  . GLU B 286 ? 0.5146 0.3109 0.4861 -0.0780 -0.0810 0.0889  272 GLU B CB  
6177 C CG  . GLU B 286 ? 0.5598 0.3540 0.5343 -0.0820 -0.0826 0.0964  272 GLU B CG  
6178 C CD  . GLU B 286 ? 0.6926 0.4767 0.6605 -0.0750 -0.0804 0.0950  272 GLU B CD  
6179 O OE1 . GLU B 286 ? 0.6729 0.4428 0.6314 -0.0692 -0.0806 0.0886  272 GLU B OE1 
6180 O OE2 . GLU B 286 ? 0.6325 0.4229 0.6048 -0.0752 -0.0785 0.1007  272 GLU B OE2 
6181 N N   . ALA B 287 ? 0.4911 0.3366 0.4831 -0.0731 -0.0677 0.0907  273 ALA B N   
6182 C CA  . ALA B 287 ? 0.4399 0.3057 0.4422 -0.0742 -0.0631 0.0958  273 ALA B CA  
6183 C C   . ALA B 287 ? 0.4318 0.3067 0.4337 -0.0661 -0.0564 0.0930  273 ALA B C   
6184 O O   . ALA B 287 ? 0.4363 0.3213 0.4425 -0.0659 -0.0530 0.0975  273 ALA B O   
6185 C CB  . ALA B 287 ? 0.4270 0.3056 0.4374 -0.0783 -0.0633 0.0965  273 ALA B CB  
6186 N N   . ILE B 288 ? 0.4107 0.2820 0.4072 -0.0597 -0.0547 0.0858  274 ILE B N   
6187 C CA  . ILE B 288 ? 0.3942 0.2746 0.3909 -0.0524 -0.0488 0.0829  274 ILE B CA  
6188 C C   . ILE B 288 ? 0.4133 0.2818 0.4031 -0.0470 -0.0487 0.0814  274 ILE B C   
6189 O O   . ILE B 288 ? 0.4400 0.3133 0.4313 -0.0450 -0.0464 0.0847  274 ILE B O   
6190 C CB  . ILE B 288 ? 0.3959 0.2812 0.3920 -0.0486 -0.0466 0.0765  274 ILE B CB  
6191 C CG1 . ILE B 288 ? 0.3854 0.2830 0.3892 -0.0536 -0.0468 0.0782  274 ILE B CG1 
6192 C CG2 . ILE B 288 ? 0.3739 0.2670 0.3697 -0.0411 -0.0411 0.0733  274 ILE B CG2 
6193 C CD1 . ILE B 288 ? 0.3990 0.3133 0.4116 -0.0560 -0.0433 0.0841  274 ILE B CD1 
6194 N N   . GLU B 289 ? 0.4370 0.2898 0.4192 -0.0445 -0.0512 0.0765  275 GLU B N   
6195 C CA  . GLU B 289 ? 0.4482 0.2897 0.4243 -0.0385 -0.0507 0.0747  275 GLU B CA  
6196 C C   . GLU B 289 ? 0.4530 0.2859 0.4282 -0.0415 -0.0538 0.0805  275 GLU B C   
6197 O O   . GLU B 289 ? 0.4718 0.3009 0.4450 -0.0367 -0.0525 0.0813  275 GLU B O   
6198 C CB  . GLU B 289 ? 0.4737 0.3000 0.4413 -0.0350 -0.0521 0.0680  275 GLU B CB  
6199 C CG  . GLU B 289 ? 0.4639 0.2977 0.4314 -0.0286 -0.0474 0.0622  275 GLU B CG  
6200 C CD  . GLU B 289 ? 0.4948 0.3148 0.4537 -0.0256 -0.0483 0.0557  275 GLU B CD  
6201 O OE1 . GLU B 289 ? 0.5026 0.3050 0.4541 -0.0270 -0.0522 0.0550  275 GLU B OE1 
6202 O OE2 . GLU B 289 ? 0.4693 0.2958 0.4282 -0.0216 -0.0448 0.0511  275 GLU B OE2 
6203 N N   . GLY B 290 ? 0.4562 0.2865 0.4333 -0.0494 -0.0579 0.0851  276 GLY B N   
6204 C CA  . GLY B 290 ? 0.4888 0.3108 0.4650 -0.0529 -0.0611 0.0911  276 GLY B CA  
6205 C C   . GLY B 290 ? 0.4662 0.3022 0.4489 -0.0544 -0.0582 0.0977  276 GLY B C   
6206 O O   . GLY B 290 ? 0.4754 0.3047 0.4569 -0.0562 -0.0603 0.1027  276 GLY B O   
6207 N N   . ALA B 291 ? 0.4320 0.2865 0.4209 -0.0538 -0.0537 0.0978  277 ALA B N   
6208 C CA  . ALA B 291 ? 0.4201 0.2876 0.4138 -0.0548 -0.0505 0.1036  277 ALA B CA  
6209 C C   . ALA B 291 ? 0.4291 0.2948 0.4192 -0.0480 -0.0484 0.1030  277 ALA B C   
6210 O O   . ALA B 291 ? 0.4134 0.2763 0.4005 -0.0414 -0.0469 0.0972  277 ALA B O   
6211 C CB  . ALA B 291 ? 0.4159 0.3026 0.4162 -0.0553 -0.0460 0.1032  277 ALA B CB  
6212 N N   . ASP B 292 ? 0.4223 0.2906 0.4133 -0.0498 -0.0481 0.1094  278 ASP B N   
6213 C CA  . ASP B 292 ? 0.4240 0.2907 0.4119 -0.0435 -0.0468 0.1093  278 ASP B CA  
6214 C C   . ASP B 292 ? 0.4071 0.2897 0.3974 -0.0393 -0.0416 0.1073  278 ASP B C   
6215 O O   . ASP B 292 ? 0.4146 0.2966 0.4027 -0.0333 -0.0406 0.1058  278 ASP B O   
6216 C CB  . ASP B 292 ? 0.4626 0.3246 0.4493 -0.0465 -0.0488 0.1169  278 ASP B CB  
6217 C CG  . ASP B 292 ? 0.4747 0.3488 0.4658 -0.0530 -0.0472 0.1233  278 ASP B CG  
6218 O OD1 . ASP B 292 ? 0.4468 0.3357 0.4401 -0.0514 -0.0426 0.1233  278 ASP B OD1 
6219 O OD2 . ASP B 292 ? 0.5015 0.3701 0.4937 -0.0597 -0.0503 0.1285  278 ASP B OD2 
6220 N N   . THR B 293 ? 0.3933 0.2895 0.3879 -0.0420 -0.0386 0.1072  279 THR B N   
6221 C CA  . THR B 293 ? 0.3885 0.2987 0.3847 -0.0381 -0.0339 0.1043  279 THR B CA  
6222 C C   . THR B 293 ? 0.3656 0.2828 0.3654 -0.0391 -0.0322 0.1000  279 THR B C   
6223 O O   . THR B 293 ? 0.3567 0.2770 0.3603 -0.0449 -0.0329 0.1028  279 THR B O   
6224 C CB  . THR B 293 ? 0.3843 0.3058 0.3816 -0.0402 -0.0310 0.1101  279 THR B CB  
6225 O OG1 . THR B 293 ? 0.4288 0.3426 0.4231 -0.0416 -0.0335 0.1158  279 THR B OG1 
6226 C CG2 . THR B 293 ? 0.3433 0.2750 0.3397 -0.0350 -0.0271 0.1070  279 THR B CG2 
6227 N N   . VAL B 294 ? 0.3361 0.2564 0.3353 -0.0338 -0.0302 0.0938  280 VAL B N   
6228 C CA  . VAL B 294 ? 0.3227 0.2491 0.3248 -0.0343 -0.0287 0.0895  280 VAL B CA  
6229 C C   . VAL B 294 ? 0.3216 0.2615 0.3252 -0.0306 -0.0240 0.0871  280 VAL B C   
6230 O O   . VAL B 294 ? 0.2951 0.2343 0.2960 -0.0251 -0.0229 0.0838  280 VAL B O   
6231 C CB  . VAL B 294 ? 0.3423 0.2575 0.3414 -0.0319 -0.0311 0.0837  280 VAL B CB  
6232 C CG1 . VAL B 294 ? 0.3044 0.2264 0.3062 -0.0324 -0.0297 0.0795  280 VAL B CG1 
6233 C CG2 . VAL B 294 ? 0.3474 0.2478 0.3439 -0.0359 -0.0361 0.0859  280 VAL B CG2 
6234 N N   . LEU B 295 ? 0.2925 0.2442 0.3003 -0.0335 -0.0212 0.0888  281 LEU B N   
6235 C CA  . LEU B 295 ? 0.3014 0.2653 0.3103 -0.0305 -0.0168 0.0864  281 LEU B CA  
6236 C C   . LEU B 295 ? 0.3198 0.2849 0.3300 -0.0282 -0.0163 0.0801  281 LEU B C   
6237 O O   . LEU B 295 ? 0.3149 0.2811 0.3287 -0.0314 -0.0171 0.0797  281 LEU B O   
6238 C CB  . LEU B 295 ? 0.3104 0.2857 0.3230 -0.0343 -0.0136 0.0910  281 LEU B CB  
6239 C CG  . LEU B 295 ? 0.3004 0.2758 0.3115 -0.0371 -0.0134 0.0978  281 LEU B CG  
6240 C CD1 . LEU B 295 ? 0.3220 0.3082 0.3379 -0.0414 -0.0101 0.1025  281 LEU B CD1 
6241 C CD2 . LEU B 295 ? 0.3204 0.2973 0.3261 -0.0329 -0.0118 0.0975  281 LEU B CD2 
6242 N N   . CYS B 296 ? 0.2833 0.2480 0.2907 -0.0227 -0.0152 0.0754  282 CYS B N   
6243 C CA  . CYS B 296 ? 0.3092 0.2742 0.3170 -0.0201 -0.0146 0.0694  282 CYS B CA  
6244 C C   . CYS B 296 ? 0.2994 0.2768 0.3089 -0.0183 -0.0105 0.0676  282 CYS B C   
6245 O O   . CYS B 296 ? 0.3019 0.2826 0.3093 -0.0148 -0.0088 0.0667  282 CYS B O   
6246 C CB  . CYS B 296 ? 0.2899 0.2460 0.2939 -0.0153 -0.0159 0.0656  282 CYS B CB  
6247 S SG  . CYS B 296 ? 0.3424 0.2821 0.3430 -0.0166 -0.0204 0.0671  282 CYS B SG  
6248 N N   . ILE B 297 ? 0.2739 0.2580 0.2875 -0.0206 -0.0092 0.0673  283 ILE B N   
6249 C CA  . ILE B 297 ? 0.2589 0.2544 0.2742 -0.0194 -0.0051 0.0663  283 ILE B CA  
6250 C C   . ILE B 297 ? 0.2693 0.2660 0.2854 -0.0169 -0.0046 0.0607  283 ILE B C   
6251 O O   . ILE B 297 ? 0.2493 0.2453 0.2685 -0.0191 -0.0060 0.0599  283 ILE B O   
6252 C CB  . ILE B 297 ? 0.2704 0.2739 0.2904 -0.0235 -0.0033 0.0709  283 ILE B CB  
6253 C CG1 . ILE B 297 ? 0.2797 0.2802 0.2993 -0.0271 -0.0045 0.0771  283 ILE B CG1 
6254 C CG2 . ILE B 297 ? 0.2400 0.2544 0.2606 -0.0215 0.0015  0.0701  283 ILE B CG2 
6255 C CD1 . ILE B 297 ? 0.2700 0.2690 0.2842 -0.0250 -0.0038 0.0789  283 ILE B CD1 
6256 N N   . GLY B 298 ? 0.2734 0.2725 0.2870 -0.0127 -0.0028 0.0572  284 GLY B N   
6257 C CA  . GLY B 298 ? 0.2557 0.2566 0.2699 -0.0103 -0.0020 0.0521  284 GLY B CA  
6258 C C   . GLY B 298 ? 0.2681 0.2598 0.2812 -0.0100 -0.0049 0.0493  284 GLY B C   
6259 O O   . GLY B 298 ? 0.2501 0.2423 0.2647 -0.0106 -0.0053 0.0467  284 GLY B O   
6260 N N   . THR B 299 ? 0.2801 0.2630 0.2901 -0.0090 -0.0070 0.0496  285 THR B N   
6261 C CA  . THR B 299 ? 0.3024 0.2745 0.3100 -0.0089 -0.0098 0.0475  285 THR B CA  
6262 C C   . THR B 299 ? 0.3136 0.2820 0.3183 -0.0039 -0.0090 0.0432  285 THR B C   
6263 O O   . THR B 299 ? 0.2873 0.2583 0.2916 -0.0008 -0.0076 0.0434  285 THR B O   
6264 C CB  . THR B 299 ? 0.3402 0.3037 0.3462 -0.0112 -0.0127 0.0512  285 THR B CB  
6265 O OG1 . THR B 299 ? 0.5217 0.4849 0.5263 -0.0086 -0.0120 0.0530  285 THR B OG1 
6266 C CG2 . THR B 299 ? 0.3143 0.2815 0.3240 -0.0167 -0.0136 0.0558  285 THR B CG2 
6267 N N   . ARG B 300 ? 0.3186 0.2809 0.3211 -0.0033 -0.0099 0.0395  286 ARG B N   
6268 C CA  . ARG B 300 ? 0.3147 0.2728 0.3145 0.0014  -0.0088 0.0356  286 ARG B CA  
6269 C C   . ARG B 300 ? 0.3422 0.2872 0.3372 0.0013  -0.0110 0.0338  286 ARG B C   
6270 O O   . ARG B 300 ? 0.3249 0.2668 0.3183 -0.0013 -0.0125 0.0323  286 ARG B O   
6271 C CB  . ARG B 300 ? 0.3045 0.2698 0.3055 0.0030  -0.0064 0.0322  286 ARG B CB  
6272 C CG  . ARG B 300 ? 0.2805 0.2573 0.2847 0.0038  -0.0041 0.0332  286 ARG B CG  
6273 C CD  . ARG B 300 ? 0.3240 0.3017 0.3282 0.0071  -0.0033 0.0342  286 ARG B CD  
6274 N NE  . ARG B 300 ? 0.2913 0.2785 0.2973 0.0067  -0.0020 0.0360  286 ARG B NE  
6275 C CZ  . ARG B 300 ? 0.2934 0.2872 0.3002 0.0084  -0.0002 0.0338  286 ARG B CZ  
6276 N NH1 . ARG B 300 ? 0.3017 0.2947 0.3084 0.0106  0.0007  0.0301  286 ARG B NH1 
6277 N NH2 . ARG B 300 ? 0.2779 0.2786 0.2848 0.0078  0.0008  0.0354  286 ARG B NH2 
6278 N N   . PHE B 301 ? 0.3339 0.2706 0.3262 0.0040  -0.0115 0.0342  287 PHE B N   
6279 C CA  . PHE B 301 ? 0.3474 0.2699 0.3341 0.0039  -0.0137 0.0328  287 PHE B CA  
6280 C C   . PHE B 301 ? 0.3605 0.2785 0.3432 0.0079  -0.0118 0.0277  287 PHE B C   
6281 O O   . PHE B 301 ? 0.3791 0.2927 0.3601 0.0128  -0.0099 0.0263  287 PHE B O   
6282 C CB  . PHE B 301 ? 0.3517 0.2666 0.3371 0.0054  -0.0149 0.0354  287 PHE B CB  
6283 C CG  . PHE B 301 ? 0.3979 0.3148 0.3859 0.0009  -0.0172 0.0407  287 PHE B CG  
6284 C CD1 . PHE B 301 ? 0.3939 0.3046 0.3803 -0.0045 -0.0207 0.0423  287 PHE B CD1 
6285 C CD2 . PHE B 301 ? 0.4134 0.3382 0.4052 0.0016  -0.0162 0.0442  287 PHE B CD2 
6286 C CE1 . PHE B 301 ? 0.3691 0.2822 0.3584 -0.0089 -0.0225 0.0476  287 PHE B CE1 
6287 C CE2 . PHE B 301 ? 0.4047 0.3313 0.3982 -0.0026 -0.0179 0.0493  287 PHE B CE2 
6288 C CZ  . PHE B 301 ? 0.3788 0.2999 0.3715 -0.0079 -0.0209 0.0510  287 PHE B CZ  
6289 N N   . THR B 302 ? 0.3350 0.2545 0.3165 0.0058  -0.0121 0.0253  288 THR B N   
6290 C CA  . THR B 302 ? 0.3512 0.2666 0.3282 0.0090  -0.0101 0.0208  288 THR B CA  
6291 C C   . THR B 302 ? 0.3786 0.2777 0.3471 0.0092  -0.0120 0.0186  288 THR B C   
6292 O O   . THR B 302 ? 0.3792 0.2703 0.3455 0.0060  -0.0155 0.0207  288 THR B O   
6293 C CB  . THR B 302 ? 0.3474 0.2704 0.3260 0.0069  -0.0098 0.0192  288 THR B CB  
6294 O OG1 . THR B 302 ? 0.3635 0.2810 0.3394 0.0019  -0.0136 0.0195  288 THR B OG1 
6295 C CG2 . THR B 302 ? 0.3256 0.2631 0.3118 0.0060  -0.0084 0.0216  288 THR B CG2 
6296 N N   . ASP B 303 ? 0.3774 0.2710 0.3405 0.0129  -0.0097 0.0145  289 ASP B N   
6297 C CA  . ASP B 303 ? 0.4134 0.2902 0.3667 0.0137  -0.0110 0.0119  289 ASP B CA  
6298 C C   . ASP B 303 ? 0.4018 0.2718 0.3504 0.0075  -0.0159 0.0119  289 ASP B C   
6299 O O   . ASP B 303 ? 0.4230 0.2801 0.3659 0.0054  -0.0193 0.0123  289 ASP B O   
6300 C CB  . ASP B 303 ? 0.3907 0.2639 0.3390 0.0191  -0.0068 0.0076  289 ASP B CB  
6301 C CG  . ASP B 303 ? 0.3952 0.2767 0.3444 0.0180  -0.0055 0.0057  289 ASP B CG  
6302 O OD1 . ASP B 303 ? 0.3893 0.2819 0.3448 0.0142  -0.0070 0.0077  289 ASP B OD1 
6303 O OD2 . ASP B 303 ? 0.3937 0.2706 0.3372 0.0212  -0.0026 0.0022  289 ASP B OD2 
6304 N N   . THR B 304 ? 0.3838 0.2621 0.3350 0.0043  -0.0167 0.0116  290 THR B N   
6305 C CA  . THR B 304 ? 0.4116 0.2850 0.3598 -0.0018 -0.0218 0.0122  290 THR B CA  
6306 C C   . THR B 304 ? 0.4246 0.3004 0.3784 -0.0069 -0.0256 0.0170  290 THR B C   
6307 O O   . THR B 304 ? 0.4472 0.3128 0.3966 -0.0114 -0.0304 0.0179  290 THR B O   
6308 C CB  . THR B 304 ? 0.4261 0.3092 0.3772 -0.0034 -0.0215 0.0112  290 THR B CB  
6309 O OG1 . THR B 304 ? 0.4175 0.2963 0.3619 0.0006  -0.0184 0.0068  290 THR B OG1 
6310 C CG2 . THR B 304 ? 0.4754 0.3551 0.4252 -0.0100 -0.0272 0.0125  290 THR B CG2 
6311 N N   . LEU B 305 ? 0.3847 0.2734 0.3478 -0.0064 -0.0235 0.0203  291 LEU B N   
6312 C CA  . LEU B 305 ? 0.3823 0.2751 0.3512 -0.0113 -0.0264 0.0254  291 LEU B CA  
6313 C C   . LEU B 305 ? 0.3877 0.2688 0.3529 -0.0117 -0.0286 0.0271  291 LEU B C   
6314 O O   . LEU B 305 ? 0.4116 0.2926 0.3799 -0.0167 -0.0319 0.0313  291 LEU B O   
6315 C CB  . LEU B 305 ? 0.3580 0.2672 0.3363 -0.0102 -0.0231 0.0281  291 LEU B CB  
6316 C CG  . LEU B 305 ? 0.3397 0.2622 0.3249 -0.0131 -0.0228 0.0296  291 LEU B CG  
6317 C CD1 . LEU B 305 ? 0.3381 0.2595 0.3202 -0.0130 -0.0231 0.0258  291 LEU B CD1 
6318 C CD2 . LEU B 305 ? 0.3113 0.2473 0.3028 -0.0103 -0.0185 0.0308  291 LEU B CD2 
6319 N N   . THR B 306 ? 0.4046 0.2756 0.3635 -0.0065 -0.0267 0.0243  292 THR B N   
6320 C CA  . THR B 306 ? 0.4433 0.3031 0.3989 -0.0057 -0.0282 0.0259  292 THR B CA  
6321 C C   . THR B 306 ? 0.4516 0.2923 0.3957 -0.0040 -0.0296 0.0219  292 THR B C   
6322 O O   . THR B 306 ? 0.4659 0.2961 0.4062 -0.0013 -0.0297 0.0222  292 THR B O   
6323 C CB  . THR B 306 ? 0.4270 0.2930 0.3871 -0.0002 -0.0241 0.0271  292 THR B CB  
6324 O OG1 . THR B 306 ? 0.4136 0.2787 0.3709 0.0061  -0.0200 0.0227  292 THR B OG1 
6325 C CG2 . THR B 306 ? 0.3806 0.2644 0.3504 -0.0017 -0.0226 0.0306  292 THR B CG2 
6326 N N   . ALA B 307 ? 0.4568 0.2924 0.3947 -0.0056 -0.0309 0.0184  293 ALA B N   
6327 C CA  . ALA B 307 ? 0.5020 0.3187 0.4270 -0.0039 -0.0321 0.0142  293 ALA B CA  
6328 C C   . ALA B 307 ? 0.5134 0.3247 0.4349 0.0044  -0.0268 0.0114  293 ALA B C   
6329 O O   . ALA B 307 ? 0.5440 0.3404 0.4585 0.0066  -0.0275 0.0105  293 ALA B O   
6330 C CB  . ALA B 307 ? 0.5417 0.3438 0.4613 -0.0092 -0.0382 0.0160  293 ALA B CB  
6331 N N   . GLY B 308 ? 0.4747 0.2983 0.4012 0.0089  -0.0216 0.0101  294 GLY B N   
6332 C CA  . GLY B 308 ? 0.4612 0.2825 0.3866 0.0168  -0.0163 0.0081  294 GLY B CA  
6333 C C   . GLY B 308 ? 0.4585 0.2833 0.3909 0.0195  -0.0155 0.0118  294 GLY B C   
6334 O O   . GLY B 308 ? 0.4672 0.2821 0.3959 0.0248  -0.0135 0.0108  294 GLY B O   
6335 N N   . PHE B 309 ? 0.4764 0.3149 0.4185 0.0161  -0.0167 0.0162  295 PHE B N   
6336 C CA  . PHE B 309 ? 0.4427 0.2859 0.3915 0.0183  -0.0161 0.0202  295 PHE B CA  
6337 C C   . PHE B 309 ? 0.4774 0.3055 0.4214 0.0176  -0.0194 0.0219  295 PHE B C   
6338 O O   . PHE B 309 ? 0.4717 0.2969 0.4173 0.0222  -0.0180 0.0233  295 PHE B O   
6339 C CB  . PHE B 309 ? 0.4564 0.3061 0.4092 0.0257  -0.0109 0.0190  295 PHE B CB  
6340 C CG  . PHE B 309 ? 0.4623 0.3258 0.4194 0.0263  -0.0078 0.0173  295 PHE B CG  
6341 C CD1 . PHE B 309 ? 0.4337 0.3118 0.3981 0.0224  -0.0086 0.0199  295 PHE B CD1 
6342 C CD2 . PHE B 309 ? 0.4474 0.3089 0.4010 0.0310  -0.0038 0.0132  295 PHE B CD2 
6343 C CE1 . PHE B 309 ? 0.3896 0.2794 0.3576 0.0231  -0.0060 0.0182  295 PHE B CE1 
6344 C CE2 . PHE B 309 ? 0.4255 0.2993 0.3831 0.0313  -0.0012 0.0118  295 PHE B CE2 
6345 C CZ  . PHE B 309 ? 0.4125 0.3002 0.3773 0.0273  -0.0025 0.0143  295 PHE B CZ  
6346 N N   . THR B 310 ? 0.4792 0.2974 0.4175 0.0116  -0.0242 0.0221  296 THR B N   
6347 C CA  . THR B 310 ? 0.4779 0.2812 0.4114 0.0097  -0.0281 0.0241  296 THR B CA  
6348 C C   . THR B 310 ? 0.4950 0.3049 0.4351 0.0031  -0.0320 0.0300  296 THR B C   
6349 O O   . THR B 310 ? 0.5106 0.3087 0.4468 -0.0009 -0.0365 0.0321  296 THR B O   
6350 C CB  . THR B 310 ? 0.5123 0.2972 0.4336 0.0075  -0.0313 0.0203  296 THR B CB  
6351 O OG1 . THR B 310 ? 0.5364 0.3266 0.4579 0.0012  -0.0340 0.0199  296 THR B OG1 
6352 C CG2 . THR B 310 ? 0.5071 0.2832 0.4205 0.0149  -0.0268 0.0146  296 THR B CG2 
6353 N N   . HIS B 311 ? 0.4686 0.2970 0.4183 0.0018  -0.0303 0.0327  297 HIS B N   
6354 C CA  . HIS B 311 ? 0.4475 0.2835 0.4038 -0.0032 -0.0326 0.0387  297 HIS B CA  
6355 C C   . HIS B 311 ? 0.4820 0.3137 0.4393 -0.0001 -0.0325 0.0419  297 HIS B C   
6356 O O   . HIS B 311 ? 0.5128 0.3451 0.4706 0.0067  -0.0291 0.0404  297 HIS B O   
6357 C CB  . HIS B 311 ? 0.4169 0.2729 0.3819 -0.0042 -0.0299 0.0402  297 HIS B CB  
6358 C CG  . HIS B 311 ? 0.4351 0.3000 0.4033 0.0024  -0.0251 0.0385  297 HIS B CG  
6359 N ND1 . HIS B 311 ? 0.4514 0.3120 0.4157 0.0080  -0.0222 0.0335  297 HIS B ND1 
6360 C CD2 . HIS B 311 ? 0.4412 0.3192 0.4161 0.0041  -0.0228 0.0412  297 HIS B CD2 
6361 C CE1 . HIS B 311 ? 0.4491 0.3203 0.4185 0.0126  -0.0185 0.0335  297 HIS B CE1 
6362 N NE2 . HIS B 311 ? 0.4475 0.3290 0.4231 0.0103  -0.0191 0.0380  297 HIS B NE2 
6363 N N   . GLN B 312 ? 0.4770 0.3052 0.4353 -0.0051 -0.0362 0.0469  298 GLN B N   
6364 C CA  . GLN B 312 ? 0.4967 0.3194 0.4555 -0.0032 -0.0371 0.0508  298 GLN B CA  
6365 C C   . GLN B 312 ? 0.4939 0.3311 0.4606 -0.0069 -0.0371 0.0568  298 GLN B C   
6366 O O   . GLN B 312 ? 0.4910 0.3271 0.4588 -0.0134 -0.0404 0.0611  298 GLN B O   
6367 C CB  . GLN B 312 ? 0.5310 0.3345 0.4827 -0.0061 -0.0418 0.0516  298 GLN B CB  
6368 C CG  . GLN B 312 ? 0.6149 0.4012 0.5579 -0.0001 -0.0411 0.0466  298 GLN B CG  
6369 C CD  . GLN B 312 ? 0.7000 0.4660 0.6346 -0.0038 -0.0463 0.0470  298 GLN B CD  
6370 O OE1 . GLN B 312 ? 0.7653 0.5205 0.6922 -0.0059 -0.0483 0.0430  298 GLN B OE1 
6371 N NE2 . GLN B 312 ? 0.7427 0.5030 0.6784 -0.0051 -0.0488 0.0519  298 GLN B NE2 
6372 N N   . LEU B 313 ? 0.4775 0.3281 0.4494 -0.0029 -0.0333 0.0571  299 LEU B N   
6373 C CA  . LEU B 313 ? 0.4592 0.3233 0.4371 -0.0053 -0.0327 0.0622  299 LEU B CA  
6374 C C   . LEU B 313 ? 0.4618 0.3303 0.4419 0.0010  -0.0303 0.0628  299 LEU B C   
6375 O O   . LEU B 313 ? 0.4971 0.3704 0.4783 0.0060  -0.0272 0.0588  299 LEU B O   
6376 C CB  . LEU B 313 ? 0.4200 0.2992 0.4023 -0.0085 -0.0307 0.0616  299 LEU B CB  
6377 C CG  . LEU B 313 ? 0.4354 0.3143 0.4180 -0.0153 -0.0330 0.0622  299 LEU B CG  
6378 C CD1 . LEU B 313 ? 0.4184 0.3133 0.4061 -0.0167 -0.0302 0.0614  299 LEU B CD1 
6379 C CD2 . LEU B 313 ? 0.4206 0.2956 0.4040 -0.0215 -0.0365 0.0683  299 LEU B CD2 
6380 N N   . THR B 314 ? 0.4403 0.3070 0.4212 0.0006  -0.0319 0.0679  300 THR B N   
6381 C CA  . THR B 314 ? 0.4276 0.2976 0.4108 0.0065  -0.0305 0.0690  300 THR B CA  
6382 C C   . THR B 314 ? 0.4159 0.3022 0.4035 0.0053  -0.0288 0.0718  300 THR B C   
6383 O O   . THR B 314 ? 0.4088 0.3022 0.3974 -0.0003 -0.0288 0.0741  300 THR B O   
6384 C CB  . THR B 314 ? 0.4370 0.2950 0.4181 0.0074  -0.0335 0.0731  300 THR B CB  
6385 O OG1 . THR B 314 ? 0.4331 0.2951 0.4152 0.0017  -0.0355 0.0792  300 THR B OG1 
6386 C CG2 . THR B 314 ? 0.4399 0.2801 0.4152 0.0070  -0.0358 0.0707  300 THR B CG2 
6387 N N   . PRO B 315 ? 0.4426 0.3352 0.4328 0.0104  -0.0273 0.0717  301 PRO B N   
6388 C CA  . PRO B 315 ? 0.4146 0.3210 0.4076 0.0090  -0.0262 0.0746  301 PRO B CA  
6389 C C   . PRO B 315 ? 0.3847 0.2910 0.3765 0.0044  -0.0284 0.0811  301 PRO B C   
6390 O O   . PRO B 315 ? 0.3704 0.2866 0.3627 0.0005  -0.0273 0.0831  301 PRO B O   
6391 C CB  . PRO B 315 ? 0.4159 0.3260 0.4117 0.0154  -0.0253 0.0737  301 PRO B CB  
6392 C CG  . PRO B 315 ? 0.4509 0.3475 0.4457 0.0198  -0.0265 0.0729  301 PRO B CG  
6393 C CD  . PRO B 315 ? 0.4276 0.3165 0.4189 0.0176  -0.0260 0.0688  301 PRO B CD  
6394 N N   . SER B 316 ? 0.3963 0.2915 0.3863 0.0049  -0.0314 0.0846  302 SER B N   
6395 C CA  . SER B 316 ? 0.4084 0.3034 0.3972 0.0003  -0.0335 0.0913  302 SER B CA  
6396 C C   . SER B 316 ? 0.4128 0.3071 0.4005 -0.0067 -0.0338 0.0927  302 SER B C   
6397 O O   . SER B 316 ? 0.3893 0.2884 0.3768 -0.0114 -0.0341 0.0979  302 SER B O   
6398 C CB  . SER B 316 ? 0.4193 0.3019 0.4066 0.0028  -0.0367 0.0948  302 SER B CB  
6399 O OG  . SER B 316 ? 0.4899 0.3682 0.4750 -0.0027 -0.0392 0.1008  302 SER B OG  
6400 N N   . GLN B 317 ? 0.3903 0.2791 0.3776 -0.0077 -0.0338 0.0885  303 GLN B N   
6401 C CA  . GLN B 317 ? 0.3839 0.2731 0.3714 -0.0144 -0.0345 0.0897  303 GLN B CA  
6402 C C   . GLN B 317 ? 0.3680 0.2724 0.3586 -0.0168 -0.0312 0.0887  303 GLN B C   
6403 O O   . GLN B 317 ? 0.3554 0.2634 0.3477 -0.0226 -0.0313 0.0914  303 GLN B O   
6404 C CB  . GLN B 317 ? 0.4044 0.2816 0.3896 -0.0144 -0.0362 0.0852  303 GLN B CB  
6405 C CG  . GLN B 317 ? 0.3846 0.2603 0.3702 -0.0214 -0.0380 0.0863  303 GLN B CG  
6406 C CD  . GLN B 317 ? 0.4245 0.2870 0.4063 -0.0210 -0.0402 0.0816  303 GLN B CD  
6407 O OE1 . GLN B 317 ? 0.4495 0.3060 0.4285 -0.0150 -0.0392 0.0768  303 GLN B OE1 
6408 N NE2 . GLN B 317 ? 0.4161 0.2732 0.3974 -0.0275 -0.0433 0.0832  303 GLN B NE2 
6409 N N   . THR B 318 ? 0.3508 0.2644 0.3426 -0.0126 -0.0282 0.0853  304 THR B N   
6410 C CA  . THR B 318 ? 0.3287 0.2542 0.3230 -0.0140 -0.0251 0.0827  304 THR B CA  
6411 C C   . THR B 318 ? 0.3131 0.2512 0.3081 -0.0133 -0.0224 0.0844  304 THR B C   
6412 O O   . THR B 318 ? 0.3341 0.2724 0.3276 -0.0104 -0.0228 0.0862  304 THR B O   
6413 C CB  . THR B 318 ? 0.3513 0.2757 0.3459 -0.0102 -0.0240 0.0759  304 THR B CB  
6414 O OG1 . THR B 318 ? 0.3696 0.2903 0.3632 -0.0041 -0.0240 0.0739  304 THR B OG1 
6415 C CG2 . THR B 318 ? 0.3479 0.2614 0.3411 -0.0126 -0.0264 0.0739  304 THR B CG2 
6416 N N   . ILE B 319 ? 0.2964 0.2444 0.2933 -0.0161 -0.0197 0.0842  305 ILE B N   
6417 C CA  . ILE B 319 ? 0.2905 0.2504 0.2872 -0.0151 -0.0164 0.0839  305 ILE B CA  
6418 C C   . ILE B 319 ? 0.2853 0.2510 0.2845 -0.0141 -0.0141 0.0785  305 ILE B C   
6419 O O   . ILE B 319 ? 0.2860 0.2515 0.2878 -0.0172 -0.0141 0.0779  305 ILE B O   
6420 C CB  . ILE B 319 ? 0.2895 0.2557 0.2859 -0.0196 -0.0148 0.0895  305 ILE B CB  
6421 C CG1 . ILE B 319 ? 0.2877 0.2475 0.2811 -0.0209 -0.0174 0.0953  305 ILE B CG1 
6422 C CG2 . ILE B 319 ? 0.2748 0.2526 0.2700 -0.0184 -0.0109 0.0883  305 ILE B CG2 
6423 C CD1 . ILE B 319 ? 0.2964 0.2618 0.2888 -0.0255 -0.0156 0.1015  305 ILE B CD1 
6424 N N   . GLU B 320 ? 0.2672 0.2381 0.2659 -0.0101 -0.0124 0.0747  306 GLU B N   
6425 C CA  . GLU B 320 ? 0.2967 0.2723 0.2975 -0.0090 -0.0103 0.0696  306 GLU B CA  
6426 C C   . GLU B 320 ? 0.2997 0.2859 0.2999 -0.0080 -0.0072 0.0685  306 GLU B C   
6427 O O   . GLU B 320 ? 0.2704 0.2588 0.2678 -0.0062 -0.0071 0.0698  306 GLU B O   
6428 C CB  . GLU B 320 ? 0.3115 0.2808 0.3124 -0.0050 -0.0115 0.0647  306 GLU B CB  
6429 C CG  . GLU B 320 ? 0.3338 0.3057 0.3341 -0.0003 -0.0109 0.0625  306 GLU B CG  
6430 C CD  . GLU B 320 ? 0.3468 0.3134 0.3479 0.0034  -0.0111 0.0578  306 GLU B CD  
6431 O OE1 . GLU B 320 ? 0.3478 0.3172 0.3498 0.0039  -0.0095 0.0537  306 GLU B OE1 
6432 O OE2 . GLU B 320 ? 0.3656 0.3248 0.3661 0.0061  -0.0128 0.0584  306 GLU B OE2 
6433 N N   . VAL B 321 ? 0.2930 0.2851 0.2955 -0.0090 -0.0048 0.0661  307 VAL B N   
6434 C CA  . VAL B 321 ? 0.2851 0.2865 0.2866 -0.0081 -0.0016 0.0647  307 VAL B CA  
6435 C C   . VAL B 321 ? 0.2687 0.2721 0.2721 -0.0058 -0.0006 0.0591  307 VAL B C   
6436 O O   . VAL B 321 ? 0.2711 0.2737 0.2776 -0.0072 -0.0007 0.0576  307 VAL B O   
6437 C CB  . VAL B 321 ? 0.2733 0.2811 0.2755 -0.0115 0.0012  0.0682  307 VAL B CB  
6438 C CG1 . VAL B 321 ? 0.3244 0.3312 0.3315 -0.0147 0.0006  0.0692  307 VAL B CG1 
6439 C CG2 . VAL B 321 ? 0.2871 0.3032 0.2886 -0.0100 0.0049  0.0655  307 VAL B CG2 
6440 N N   . GLN B 322 ? 0.2788 0.2846 0.2803 -0.0026 0.0000  0.0563  308 GLN B N   
6441 C CA  . GLN B 322 ? 0.2617 0.2699 0.2644 -0.0003 0.0010  0.0513  308 GLN B CA  
6442 C C   . GLN B 322 ? 0.2762 0.2922 0.2771 -0.0001 0.0040  0.0504  308 GLN B C   
6443 O O   . GLN B 322 ? 0.2677 0.2866 0.2656 -0.0014 0.0051  0.0535  308 GLN B O   
6444 C CB  . GLN B 322 ? 0.2733 0.2777 0.2754 0.0032  -0.0008 0.0492  308 GLN B CB  
6445 C CG  . GLN B 322 ? 0.2718 0.2675 0.2751 0.0038  -0.0031 0.0494  308 GLN B CG  
6446 C CD  . GLN B 322 ? 0.2891 0.2817 0.2941 0.0026  -0.0030 0.0469  308 GLN B CD  
6447 O OE1 . GLN B 322 ? 0.2633 0.2606 0.2695 0.0023  -0.0013 0.0443  308 GLN B OE1 
6448 N NE2 . GLN B 322 ? 0.2943 0.2782 0.2990 0.0019  -0.0051 0.0476  308 GLN B NE2 
6449 N N   . PRO B 323 ? 0.2677 0.2866 0.2696 0.0014  0.0053  0.0462  309 PRO B N   
6450 C CA  . PRO B 323 ? 0.2751 0.3005 0.2749 0.0016  0.0083  0.0452  309 PRO B CA  
6451 C C   . PRO B 323 ? 0.2973 0.3242 0.2914 0.0023  0.0084  0.0463  309 PRO B C   
6452 O O   . PRO B 323 ? 0.3056 0.3365 0.2965 0.0017  0.0111  0.0472  309 PRO B O   
6453 C CB  . PRO B 323 ? 0.2873 0.3137 0.2889 0.0035  0.0087  0.0403  309 PRO B CB  
6454 C CG  . PRO B 323 ? 0.2958 0.3175 0.3012 0.0030  0.0069  0.0396  309 PRO B CG  
6455 C CD  . PRO B 323 ? 0.2825 0.2988 0.2871 0.0028  0.0045  0.0423  309 PRO B CD  
6456 N N   . HIS B 324 ? 0.2758 0.2998 0.2684 0.0038  0.0056  0.0465  310 HIS B N   
6457 C CA  . HIS B 324 ? 0.3064 0.3317 0.2933 0.0042  0.0050  0.0476  310 HIS B CA  
6458 C C   . HIS B 324 ? 0.3215 0.3433 0.3070 0.0038  0.0021  0.0517  310 HIS B C   
6459 O O   . HIS B 324 ? 0.2898 0.3122 0.2705 0.0041  0.0008  0.0530  310 HIS B O   
6460 C CB  . HIS B 324 ? 0.3100 0.3364 0.2963 0.0063  0.0040  0.0438  310 HIS B CB  
6461 C CG  . HIS B 324 ? 0.3463 0.3755 0.3336 0.0068  0.0064  0.0398  310 HIS B CG  
6462 N ND1 . HIS B 324 ? 0.3559 0.3883 0.3397 0.0061  0.0096  0.0392  310 HIS B ND1 
6463 C CD2 . HIS B 324 ? 0.3331 0.3623 0.3245 0.0081  0.0064  0.0362  310 HIS B CD2 
6464 C CE1 . HIS B 324 ? 0.3648 0.3987 0.3506 0.0071  0.0111  0.0355  310 HIS B CE1 
6465 N NE2 . HIS B 324 ? 0.3807 0.4128 0.3711 0.0081  0.0091  0.0337  310 HIS B NE2 
6466 N N   . ALA B 325 ? 0.2844 0.3020 0.2734 0.0033  0.0008  0.0538  311 ALA B N   
6467 C CA  . ALA B 325 ? 0.2881 0.3016 0.2763 0.0033  -0.0021 0.0577  311 ALA B CA  
6468 C C   . ALA B 325 ? 0.2723 0.2814 0.2631 0.0014  -0.0024 0.0604  311 ALA B C   
6469 O O   . ALA B 325 ? 0.2520 0.2601 0.2464 0.0009  -0.0014 0.0583  311 ALA B O   
6470 C CB  . ALA B 325 ? 0.2776 0.2888 0.2684 0.0064  -0.0049 0.0563  311 ALA B CB  
6471 N N   . SER B 326 ? 0.2374 0.2433 0.2261 0.0002  -0.0041 0.0651  312 SER B N   
6472 C CA  . SER B 326 ? 0.2588 0.2595 0.2493 -0.0021 -0.0050 0.0684  312 SER B CA  
6473 C C   . SER B 326 ? 0.2847 0.2789 0.2748 -0.0006 -0.0087 0.0713  312 SER B C   
6474 O O   . SER B 326 ? 0.2624 0.2576 0.2505 0.0013  -0.0103 0.0721  312 SER B O   
6475 C CB  . SER B 326 ? 0.2775 0.2813 0.2656 -0.0058 -0.0029 0.0724  312 SER B CB  
6476 O OG  . SER B 326 ? 0.2666 0.2752 0.2573 -0.0072 0.0003  0.0703  312 SER B OG  
6477 N N   . ARG B 327 ? 0.2789 0.2661 0.2712 -0.0017 -0.0102 0.0730  313 ARG B N   
6478 C CA  . ARG B 327 ? 0.2800 0.2594 0.2725 0.0002  -0.0135 0.0753  313 ARG B CA  
6479 C C   . ARG B 327 ? 0.2975 0.2713 0.2888 -0.0033 -0.0149 0.0805  313 ARG B C   
6480 O O   . ARG B 327 ? 0.2845 0.2575 0.2771 -0.0067 -0.0139 0.0808  313 ARG B O   
6481 C CB  . ARG B 327 ? 0.2916 0.2655 0.2877 0.0036  -0.0143 0.0712  313 ARG B CB  
6482 C CG  . ARG B 327 ? 0.2937 0.2584 0.2904 0.0059  -0.0172 0.0734  313 ARG B CG  
6483 C CD  . ARG B 327 ? 0.3214 0.2801 0.3206 0.0093  -0.0171 0.0690  313 ARG B CD  
6484 N NE  . ARG B 327 ? 0.3243 0.2786 0.3232 0.0067  -0.0164 0.0669  313 ARG B NE  
6485 C CZ  . ARG B 327 ? 0.3408 0.2864 0.3384 0.0041  -0.0182 0.0692  313 ARG B CZ  
6486 N NH1 . ARG B 327 ? 0.3179 0.2580 0.3141 0.0037  -0.0206 0.0739  313 ARG B NH1 
6487 N NH2 . ARG B 327 ? 0.3496 0.2914 0.3469 0.0016  -0.0181 0.0670  313 ARG B NH2 
6488 N N   . VAL B 328 ? 0.2771 0.2472 0.2663 -0.0029 -0.0174 0.0849  314 VAL B N   
6489 C CA  . VAL B 328 ? 0.2990 0.2619 0.2871 -0.0058 -0.0194 0.0900  314 VAL B CA  
6490 C C   . VAL B 328 ? 0.3113 0.2650 0.3006 -0.0022 -0.0229 0.0907  314 VAL B C   
6491 O O   . VAL B 328 ? 0.3180 0.2723 0.3064 0.0005  -0.0246 0.0925  314 VAL B O   
6492 C CB  . VAL B 328 ? 0.3197 0.2863 0.3034 -0.0091 -0.0191 0.0957  314 VAL B CB  
6493 C CG1 . VAL B 328 ? 0.3274 0.2858 0.3104 -0.0120 -0.0216 0.1013  314 VAL B CG1 
6494 C CG2 . VAL B 328 ? 0.3047 0.2801 0.2874 -0.0122 -0.0150 0.0951  314 VAL B CG2 
6495 N N   . GLY B 329 ? 0.3248 0.2696 0.3158 -0.0021 -0.0239 0.0893  315 GLY B N   
6496 C CA  . GLY B 329 ? 0.3616 0.2967 0.3534 0.0019  -0.0266 0.0897  315 GLY B CA  
6497 C C   . GLY B 329 ? 0.3711 0.3100 0.3657 0.0075  -0.0258 0.0855  315 GLY B C   
6498 O O   . GLY B 329 ? 0.3475 0.2896 0.3437 0.0087  -0.0235 0.0803  315 GLY B O   
6499 N N   . ASP B 330 ? 0.3653 0.3046 0.3606 0.0108  -0.0277 0.0881  316 ASP B N   
6500 C CA  . ASP B 330 ? 0.3737 0.3167 0.3728 0.0161  -0.0274 0.0851  316 ASP B CA  
6501 C C   . ASP B 330 ? 0.3492 0.3041 0.3482 0.0157  -0.0264 0.0844  316 ASP B C   
6502 O O   . ASP B 330 ? 0.3506 0.3099 0.3533 0.0196  -0.0262 0.0820  316 ASP B O   
6503 C CB  . ASP B 330 ? 0.4263 0.3633 0.4275 0.0202  -0.0304 0.0887  316 ASP B CB  
6504 C CG  . ASP B 330 ? 0.4404 0.3650 0.4424 0.0228  -0.0308 0.0876  316 ASP B CG  
6505 O OD1 . ASP B 330 ? 0.4322 0.3534 0.4334 0.0221  -0.0287 0.0831  316 ASP B OD1 
6506 O OD2 . ASP B 330 ? 0.5209 0.4384 0.5236 0.0253  -0.0334 0.0913  316 ASP B OD2 
6507 N N   . VAL B 331 ? 0.3201 0.2802 0.3149 0.0113  -0.0258 0.0865  317 VAL B N   
6508 C CA  . VAL B 331 ? 0.3206 0.2901 0.3134 0.0108  -0.0256 0.0866  317 VAL B CA  
6509 C C   . VAL B 331 ? 0.3080 0.2840 0.2997 0.0087  -0.0220 0.0822  317 VAL B C   
6510 O O   . VAL B 331 ? 0.2749 0.2504 0.2648 0.0052  -0.0200 0.0823  317 VAL B O   
6511 C CB  . VAL B 331 ? 0.3216 0.2915 0.3089 0.0078  -0.0276 0.0926  317 VAL B CB  
6512 C CG1 . VAL B 331 ? 0.3170 0.2953 0.3007 0.0073  -0.0276 0.0922  317 VAL B CG1 
6513 C CG2 . VAL B 331 ? 0.3428 0.3057 0.3316 0.0101  -0.0316 0.0972  317 VAL B CG2 
6514 N N   . TRP B 332 ? 0.2903 0.2727 0.2835 0.0108  -0.0212 0.0787  318 TRP B N   
6515 C CA  . TRP B 332 ? 0.2905 0.2793 0.2825 0.0092  -0.0180 0.0746  318 TRP B CA  
6516 C C   . TRP B 332 ? 0.3041 0.2988 0.2902 0.0071  -0.0180 0.0763  318 TRP B C   
6517 O O   . TRP B 332 ? 0.2872 0.2826 0.2715 0.0079  -0.0209 0.0791  318 TRP B O   
6518 C CB  . TRP B 332 ? 0.2907 0.2822 0.2873 0.0125  -0.0170 0.0695  318 TRP B CB  
6519 C CG  . TRP B 332 ? 0.3020 0.2882 0.3022 0.0139  -0.0157 0.0665  318 TRP B CG  
6520 C CD1 . TRP B 332 ? 0.3102 0.2901 0.3140 0.0173  -0.0168 0.0665  318 TRP B CD1 
6521 C CD2 . TRP B 332 ? 0.3002 0.2866 0.3003 0.0120  -0.0129 0.0631  318 TRP B CD2 
6522 N NE1 . TRP B 332 ? 0.3311 0.3063 0.3358 0.0175  -0.0150 0.0631  318 TRP B NE1 
6523 C CE2 . TRP B 332 ? 0.3205 0.2999 0.3233 0.0141  -0.0129 0.0610  318 TRP B CE2 
6524 C CE3 . TRP B 332 ? 0.2907 0.2822 0.2888 0.0090  -0.0105 0.0617  318 TRP B CE3 
6525 C CZ2 . TRP B 332 ? 0.3287 0.3059 0.3316 0.0128  -0.0112 0.0577  318 TRP B CZ2 
6526 C CZ3 . TRP B 332 ? 0.2952 0.2854 0.2947 0.0079  -0.0087 0.0586  318 TRP B CZ3 
6527 C CH2 . TRP B 332 ? 0.3163 0.2994 0.3181 0.0096  -0.0093 0.0567  318 TRP B CH2 
6528 N N   . PHE B 333 ? 0.2807 0.2790 0.2636 0.0043  -0.0147 0.0750  319 PHE B N   
6529 C CA  . PHE B 333 ? 0.2889 0.2923 0.2651 0.0024  -0.0135 0.0756  319 PHE B CA  
6530 C C   . PHE B 333 ? 0.3064 0.3148 0.2833 0.0030  -0.0106 0.0701  319 PHE B C   
6531 O O   . PHE B 333 ? 0.2889 0.2984 0.2674 0.0018  -0.0074 0.0682  319 PHE B O   
6532 C CB  . PHE B 333 ? 0.2893 0.2922 0.2609 -0.0012 -0.0115 0.0796  319 PHE B CB  
6533 C CG  . PHE B 333 ? 0.2941 0.2912 0.2652 -0.0022 -0.0144 0.0852  319 PHE B CG  
6534 C CD1 . PHE B 333 ? 0.2984 0.2898 0.2747 -0.0023 -0.0151 0.0861  319 PHE B CD1 
6535 C CD2 . PHE B 333 ? 0.2759 0.2724 0.2407 -0.0032 -0.0165 0.0897  319 PHE B CD2 
6536 C CE1 . PHE B 333 ? 0.2827 0.2679 0.2584 -0.0031 -0.0179 0.0912  319 PHE B CE1 
6537 C CE2 . PHE B 333 ? 0.2842 0.2750 0.2485 -0.0040 -0.0194 0.0951  319 PHE B CE2 
6538 C CZ  . PHE B 333 ? 0.3017 0.2868 0.2717 -0.0040 -0.0200 0.0959  319 PHE B CZ  
6539 N N   . THR B 334 ? 0.3059 0.3173 0.2819 0.0047  -0.0119 0.0678  320 THR B N   
6540 C CA  . THR B 334 ? 0.3178 0.3330 0.2952 0.0055  -0.0097 0.0626  320 THR B CA  
6541 C C   . THR B 334 ? 0.3403 0.3591 0.3101 0.0039  -0.0076 0.0616  320 THR B C   
6542 O O   . THR B 334 ? 0.3375 0.3559 0.3002 0.0026  -0.0089 0.0646  320 THR B O   
6543 C CB  . THR B 334 ? 0.3128 0.3289 0.2949 0.0084  -0.0122 0.0603  320 THR B CB  
6544 O OG1 . THR B 334 ? 0.3331 0.3504 0.3114 0.0083  -0.0157 0.0626  320 THR B OG1 
6545 C CG2 . THR B 334 ? 0.2965 0.3085 0.2856 0.0106  -0.0136 0.0613  320 THR B CG2 
6546 N N   . GLY B 335 ? 0.3427 0.3643 0.3132 0.0041  -0.0044 0.0574  321 GLY B N   
6547 C CA  . GLY B 335 ? 0.3346 0.3587 0.2977 0.0029  -0.0015 0.0561  321 GLY B CA  
6548 C C   . GLY B 335 ? 0.3525 0.3774 0.3125 0.0009  0.0022  0.0588  321 GLY B C   
6549 O O   . GLY B 335 ? 0.3540 0.3796 0.3057 -0.0001 0.0038  0.0600  321 GLY B O   
6550 N N   . ILE B 336 ? 0.3275 0.3518 0.2936 0.0002  0.0035  0.0600  322 ILE B N   
6551 C CA  . ILE B 336 ? 0.3556 0.3818 0.3211 -0.0020 0.0073  0.0626  322 ILE B CA  
6552 C C   . ILE B 336 ? 0.3511 0.3801 0.3230 -0.0016 0.0101  0.0593  322 ILE B C   
6553 O O   . ILE B 336 ? 0.3318 0.3588 0.3105 -0.0013 0.0084  0.0582  322 ILE B O   
6554 C CB  . ILE B 336 ? 0.3349 0.3578 0.3023 -0.0040 0.0057  0.0679  322 ILE B CB  
6555 C CG1 . ILE B 336 ? 0.3560 0.3760 0.3174 -0.0041 0.0024  0.0713  322 ILE B CG1 
6556 C CG2 . ILE B 336 ? 0.3251 0.3509 0.2926 -0.0065 0.0098  0.0710  322 ILE B CG2 
6557 C CD1 . ILE B 336 ? 0.3563 0.3719 0.3201 -0.0056 0.0001  0.0762  322 ILE B CD1 
6558 N N   . PRO B 337 ? 0.3584 0.3916 0.3282 -0.0016 0.0144  0.0578  323 PRO B N   
6559 C CA  . PRO B 337 ? 0.3190 0.3553 0.2956 -0.0013 0.0169  0.0554  323 PRO B CA  
6560 C C   . PRO B 337 ? 0.3338 0.3697 0.3169 -0.0037 0.0167  0.0589  323 PRO B C   
6561 O O   . PRO B 337 ? 0.3156 0.3515 0.2972 -0.0059 0.0173  0.0636  323 PRO B O   
6562 C CB  . PRO B 337 ? 0.3566 0.3973 0.3288 -0.0008 0.0218  0.0545  323 PRO B CB  
6563 C CG  . PRO B 337 ? 0.4118 0.4505 0.3741 0.0001  0.0210  0.0539  323 PRO B CG  
6564 C CD  . PRO B 337 ? 0.3951 0.4301 0.3558 -0.0014 0.0171  0.0579  323 PRO B CD  
6565 N N   . MET B 338 ? 0.3140 0.3493 0.3040 -0.0035 0.0157  0.0566  324 MET B N   
6566 C CA  . MET B 338 ? 0.3085 0.3427 0.3046 -0.0061 0.0148  0.0595  324 MET B CA  
6567 C C   . MET B 338 ? 0.3056 0.3454 0.3035 -0.0084 0.0187  0.0633  324 MET B C   
6568 O O   . MET B 338 ? 0.3223 0.3610 0.3226 -0.0114 0.0179  0.0679  324 MET B O   
6569 C CB  . MET B 338 ? 0.2905 0.3227 0.2921 -0.0053 0.0130  0.0558  324 MET B CB  
6570 C CG  . MET B 338 ? 0.3099 0.3419 0.3179 -0.0080 0.0124  0.0576  324 MET B CG  
6571 S SD  . MET B 338 ? 0.3171 0.3477 0.3291 -0.0065 0.0110  0.0522  324 MET B SD  
6572 C CE  . MET B 338 ? 0.2742 0.2982 0.2901 -0.0097 0.0072  0.0546  324 MET B CE  
6573 N N   . LEU B 339 ? 0.3462 0.3918 0.3428 -0.0070 0.0230  0.0618  325 LEU B N   
6574 C CA  . LEU B 339 ? 0.3421 0.3937 0.3404 -0.0087 0.0275  0.0658  325 LEU B CA  
6575 C C   . LEU B 339 ? 0.3125 0.3629 0.3053 -0.0106 0.0280  0.0709  325 LEU B C   
6576 O O   . LEU B 339 ? 0.3033 0.3554 0.3001 -0.0137 0.0287  0.0759  325 LEU B O   
6577 C CB  . LEU B 339 ? 0.3769 0.4338 0.3728 -0.0060 0.0325  0.0630  325 LEU B CB  
6578 C CG  . LEU B 339 ? 0.3924 0.4566 0.3906 -0.0069 0.0383  0.0670  325 LEU B CG  
6579 C CD1 . LEU B 339 ? 0.3739 0.4410 0.3820 -0.0106 0.0376  0.0719  325 LEU B CD1 
6580 C CD2 . LEU B 339 ? 0.4207 0.4898 0.4194 -0.0038 0.0429  0.0636  325 LEU B CD2 
6581 N N   . GLN B 340 ? 0.3150 0.3623 0.2987 -0.0091 0.0272  0.0699  326 GLN B N   
6582 C CA  . GLN B 340 ? 0.3561 0.4017 0.3334 -0.0109 0.0275  0.0748  326 GLN B CA  
6583 C C   . GLN B 340 ? 0.3196 0.3600 0.3000 -0.0134 0.0228  0.0785  326 GLN B C   
6584 O O   . GLN B 340 ? 0.3155 0.3560 0.2950 -0.0162 0.0236  0.0841  326 GLN B O   
6585 C CB  . GLN B 340 ? 0.3763 0.4190 0.3429 -0.0089 0.0266  0.0730  326 GLN B CB  
6586 C CG  . GLN B 340 ? 0.4318 0.4773 0.3923 -0.0064 0.0305  0.0693  326 GLN B CG  
6587 C CD  . GLN B 340 ? 0.4301 0.4720 0.3784 -0.0060 0.0293  0.0697  326 GLN B CD  
6588 O OE1 . GLN B 340 ? 0.4459 0.4837 0.3916 -0.0049 0.0247  0.0673  326 GLN B OE1 
6589 N NE2 . GLN B 340 ? 0.4564 0.4996 0.3973 -0.0069 0.0333  0.0731  326 GLN B NE2 
6590 N N   . ALA B 341 ? 0.3152 0.3506 0.2987 -0.0123 0.0182  0.0756  327 ALA B N   
6591 C CA  . ALA B 341 ? 0.2875 0.3168 0.2738 -0.0143 0.0139  0.0786  327 ALA B CA  
6592 C C   . ALA B 341 ? 0.2971 0.3280 0.2903 -0.0179 0.0148  0.0824  327 ALA B C   
6593 O O   . ALA B 341 ? 0.2719 0.3001 0.2650 -0.0208 0.0135  0.0876  327 ALA B O   
6594 C CB  . ALA B 341 ? 0.2821 0.3061 0.2709 -0.0119 0.0098  0.0743  327 ALA B CB  
6595 N N   . ILE B 342 ? 0.2897 0.3251 0.2891 -0.0179 0.0167  0.0800  328 ILE B N   
6596 C CA  . ILE B 342 ? 0.2734 0.3111 0.2803 -0.0217 0.0171  0.0838  328 ILE B CA  
6597 C C   . ILE B 342 ? 0.2787 0.3222 0.2847 -0.0242 0.0213  0.0896  328 ILE B C   
6598 O O   . ILE B 342 ? 0.2671 0.3094 0.2759 -0.0281 0.0202  0.0951  328 ILE B O   
6599 C CB  . ILE B 342 ? 0.2817 0.3238 0.2955 -0.0210 0.0181  0.0802  328 ILE B CB  
6600 C CG1 . ILE B 342 ? 0.2554 0.2903 0.2706 -0.0199 0.0133  0.0758  328 ILE B CG1 
6601 C CG2 . ILE B 342 ? 0.2549 0.3024 0.2768 -0.0249 0.0196  0.0848  328 ILE B CG2 
6602 C CD1 . ILE B 342 ? 0.2933 0.3315 0.3125 -0.0181 0.0142  0.0712  328 ILE B CD1 
6603 N N   . GLU B 343 ? 0.2805 0.3300 0.2822 -0.0219 0.0263  0.0886  329 GLU B N   
6604 C CA  . GLU B 343 ? 0.3082 0.3633 0.3080 -0.0237 0.0313  0.0940  329 GLU B CA  
6605 C C   . GLU B 343 ? 0.3069 0.3566 0.3008 -0.0260 0.0290  0.0989  329 GLU B C   
6606 O O   . GLU B 343 ? 0.2995 0.3514 0.2959 -0.0297 0.0305  0.1051  329 GLU B O   
6607 C CB  . GLU B 343 ? 0.3451 0.4052 0.3383 -0.0202 0.0368  0.0913  329 GLU B CB  
6608 C CG  . GLU B 343 ? 0.3666 0.4324 0.3657 -0.0178 0.0397  0.0871  329 GLU B CG  
6609 C CD  . GLU B 343 ? 0.4345 0.5030 0.4256 -0.0140 0.0447  0.0838  329 GLU B CD  
6610 O OE1 . GLU B 343 ? 0.4326 0.4961 0.4132 -0.0125 0.0434  0.0820  329 GLU B OE1 
6611 O OE2 . GLU B 343 ? 0.4820 0.5573 0.4772 -0.0124 0.0497  0.0831  329 GLU B OE2 
6612 N N   . THR B 344 ? 0.2824 0.3252 0.2690 -0.0240 0.0253  0.0965  330 THR B N   
6613 C CA  . THR B 344 ? 0.2895 0.3265 0.2708 -0.0260 0.0225  0.1013  330 THR B CA  
6614 C C   . THR B 344 ? 0.3012 0.3340 0.2895 -0.0298 0.0188  0.1053  330 THR B C   
6615 O O   . THR B 344 ? 0.3164 0.3492 0.3045 -0.0335 0.0195  0.1117  330 THR B O   
6616 C CB  . THR B 344 ? 0.2979 0.3284 0.2727 -0.0229 0.0182  0.0978  330 THR B CB  
6617 O OG1 . THR B 344 ? 0.3240 0.3577 0.2915 -0.0200 0.0211  0.0943  330 THR B OG1 
6618 C CG2 . THR B 344 ? 0.2618 0.2860 0.2315 -0.0247 0.0148  0.1029  330 THR B CG2 
6619 N N   . LEU B 345 ? 0.2851 0.3141 0.2796 -0.0293 0.0151  0.1017  331 LEU B N   
6620 C CA  . LEU B 345 ? 0.2920 0.3148 0.2917 -0.0329 0.0109  0.1048  331 LEU B CA  
6621 C C   . LEU B 345 ? 0.3059 0.3347 0.3129 -0.0375 0.0133  0.1097  331 LEU B C   
6622 O O   . LEU B 345 ? 0.2998 0.3246 0.3090 -0.0417 0.0108  0.1150  331 LEU B O   
6623 C CB  . LEU B 345 ? 0.2787 0.2959 0.2820 -0.0309 0.0069  0.0992  331 LEU B CB  
6624 C CG  . LEU B 345 ? 0.2946 0.3044 0.2929 -0.0269 0.0034  0.0954  331 LEU B CG  
6625 C CD1 . LEU B 345 ? 0.2575 0.2631 0.2596 -0.0250 0.0007  0.0899  331 LEU B CD1 
6626 C CD2 . LEU B 345 ? 0.2635 0.2650 0.2583 -0.0282 -0.0003 0.0999  331 LEU B CD2 
6627 N N   . VAL B 346 ? 0.2965 0.3350 0.3078 -0.0369 0.0180  0.1084  332 VAL B N   
6628 C CA  . VAL B 346 ? 0.3086 0.3544 0.3279 -0.0410 0.0208  0.1137  332 VAL B CA  
6629 C C   . VAL B 346 ? 0.3479 0.3963 0.3637 -0.0438 0.0240  0.1208  332 VAL B C   
6630 O O   . VAL B 346 ? 0.3480 0.3961 0.3687 -0.0488 0.0227  0.1270  332 VAL B O   
6631 C CB  . VAL B 346 ? 0.3118 0.3679 0.3364 -0.0388 0.0257  0.1108  332 VAL B CB  
6632 C CG1 . VAL B 346 ? 0.3147 0.3808 0.3469 -0.0423 0.0305  0.1171  332 VAL B CG1 
6633 C CG2 . VAL B 346 ? 0.2840 0.3377 0.3142 -0.0378 0.0220  0.1054  332 VAL B CG2 
6634 N N   . GLU B 347 ? 0.3468 0.3971 0.3534 -0.0408 0.0278  0.1202  333 GLU B N   
6635 C CA  . GLU B 347 ? 0.4000 0.4521 0.4013 -0.0432 0.0310  0.1268  333 GLU B CA  
6636 C C   . GLU B 347 ? 0.4171 0.4595 0.4158 -0.0464 0.0254  0.1311  333 GLU B C   
6637 O O   . GLU B 347 ? 0.4042 0.4475 0.4050 -0.0510 0.0261  0.1382  333 GLU B O   
6638 C CB  . GLU B 347 ? 0.4340 0.4879 0.4239 -0.0391 0.0353  0.1244  333 GLU B CB  
6639 C CG  . GLU B 347 ? 0.5157 0.5723 0.4984 -0.0411 0.0399  0.1309  333 GLU B CG  
6640 C CD  . GLU B 347 ? 0.7828 0.8481 0.7744 -0.0452 0.0447  0.1375  333 GLU B CD  
6641 O OE1 . GLU B 347 ? 0.7144 0.7771 0.7094 -0.0501 0.0421  0.1439  333 GLU B OE1 
6642 O OE2 . GLU B 347 ? 0.6080 0.6827 0.6037 -0.0435 0.0509  0.1365  333 GLU B OE2 
6643 N N   . LEU B 348 ? 0.3831 0.4161 0.3777 -0.0440 0.0198  0.1270  334 LEU B N   
6644 C CA  . LEU B 348 ? 0.3791 0.4020 0.3712 -0.0463 0.0143  0.1307  334 LEU B CA  
6645 C C   . LEU B 348 ? 0.4242 0.4441 0.4253 -0.0512 0.0110  0.1343  334 LEU B C   
6646 O O   . LEU B 348 ? 0.4448 0.4605 0.4455 -0.0554 0.0092  0.1407  334 LEU B O   
6647 C CB  . LEU B 348 ? 0.3492 0.3636 0.3370 -0.0420 0.0093  0.1252  334 LEU B CB  
6648 C CG  . LEU B 348 ? 0.3449 0.3603 0.3229 -0.0380 0.0108  0.1229  334 LEU B CG  
6649 C CD1 . LEU B 348 ? 0.3041 0.3118 0.2797 -0.0341 0.0056  0.1182  334 LEU B CD1 
6650 C CD2 . LEU B 348 ? 0.3454 0.3605 0.3161 -0.0405 0.0123  0.1298  334 LEU B CD2 
6651 N N   . CYS B 349 ? 0.4064 0.4281 0.4154 -0.0511 0.0101  0.1304  335 CYS B N   
6652 C CA  . CYS B 349 ? 0.4319 0.4503 0.4491 -0.0561 0.0064  0.1333  335 CYS B CA  
6653 C C   . CYS B 349 ? 0.4902 0.5169 0.5130 -0.0615 0.0100  0.1411  335 CYS B C   
6654 O O   . CYS B 349 ? 0.5373 0.5594 0.5638 -0.0668 0.0067  0.1466  335 CYS B O   
6655 C CB  . CYS B 349 ? 0.3859 0.4054 0.4095 -0.0548 0.0049  0.1274  335 CYS B CB  
6656 S SG  . CYS B 349 ? 0.3614 0.3673 0.3806 -0.0508 -0.0014 0.1202  335 CYS B SG  
6657 N N   . LYS B 350 ? 0.4442 0.4828 0.4676 -0.0601 0.0170  0.1418  336 LYS B N   
6658 C CA  . LYS B 350 ? 0.4851 0.5330 0.5143 -0.0647 0.0215  0.1495  336 LYS B CA  
6659 C C   . LYS B 350 ? 0.5327 0.5756 0.5566 -0.0684 0.0206  0.1567  336 LYS B C   
6660 O O   . LYS B 350 ? 0.5576 0.6045 0.5876 -0.0740 0.0218  0.1642  336 LYS B O   
6661 C CB  . LYS B 350 ? 0.4834 0.5439 0.5121 -0.0612 0.0299  0.1483  336 LYS B CB  
6662 C CG  . LYS B 350 ? 0.4389 0.5073 0.4777 -0.0599 0.0314  0.1446  336 LYS B CG  
6663 C CD  . LYS B 350 ? 0.4598 0.5395 0.4978 -0.0558 0.0397  0.1429  336 LYS B CD  
6664 C CE  . LYS B 350 ? 0.4314 0.5166 0.4782 -0.0535 0.0400  0.1379  336 LYS B CE  
6665 N NZ  . LYS B 350 ? 0.4696 0.5630 0.5135 -0.0481 0.0473  0.1344  336 LYS B NZ  
6666 N N   . GLN B 351 ? 0.5423 0.5766 0.5553 -0.0657 0.0184  0.1552  337 GLN B N   
6667 C CA  . GLN B 351 ? 0.5717 0.5997 0.5793 -0.0692 0.0165  0.1621  337 GLN B CA  
6668 C C   . GLN B 351 ? 0.6177 0.6321 0.6265 -0.0719 0.0083  0.1631  337 GLN B C   
6669 O O   . GLN B 351 ? 0.6700 0.6790 0.6760 -0.0757 0.0064  0.1697  337 GLN B O   
6670 C CB  . GLN B 351 ? 0.5635 0.5907 0.5583 -0.0654 0.0192  0.1617  337 GLN B CB  
6671 C CG  . GLN B 351 ? 0.5335 0.5598 0.5221 -0.0588 0.0192  0.1533  337 GLN B CG  
6672 C CD  . GLN B 351 ? 0.5600 0.5882 0.5364 -0.0562 0.0230  0.1540  337 GLN B CD  
6673 O OE1 . GLN B 351 ? 0.5312 0.5518 0.4992 -0.0538 0.0193  0.1527  337 GLN B OE1 
6674 N NE2 . GLN B 351 ? 0.5911 0.6295 0.5666 -0.0565 0.0306  0.1562  337 GLN B NE2 
6675 N N   . HIS B 352 ? 0.6485 0.6563 0.6605 -0.0700 0.0033  0.1569  338 HIS B N   
6676 C CA  . HIS B 352 ? 0.7237 0.7170 0.7350 -0.0718 -0.0042 0.1573  338 HIS B CA  
6677 C C   . HIS B 352 ? 0.9722 0.9603 0.9915 -0.0750 -0.0090 0.1558  338 HIS B C   
6678 O O   . HIS B 352 ? 1.1069 1.0824 1.1249 -0.0775 -0.0149 0.1577  338 HIS B O   
6679 C CB  . HIS B 352 ? 0.7184 0.7026 0.7217 -0.0657 -0.0074 0.1516  338 HIS B CB  
6680 C CG  . HIS B 352 ? 0.5850 0.5710 0.5794 -0.0631 -0.0048 0.1535  338 HIS B CG  
6681 N ND1 . HIS B 352 ? 0.5737 0.5557 0.5637 -0.0663 -0.0057 0.1609  338 HIS B ND1 
6682 C CD2 . HIS B 352 ? 0.5320 0.5223 0.5204 -0.0578 -0.0020 0.1490  338 HIS B CD2 
6683 C CE1 . HIS B 352 ? 0.5542 0.5383 0.5356 -0.0631 -0.0035 0.1610  338 HIS B CE1 
6684 N NE2 . HIS B 352 ? 0.5189 0.5079 0.4992 -0.0580 -0.0014 0.1538  338 HIS B NE2 
6685 N N   . VAL B 353 ? 0.8756 0.8990 0.7898 -0.1592 -0.1587 0.3606  339 VAL B N   
6686 C CA  . VAL B 353 ? 0.9653 0.9644 0.8914 -0.1493 -0.1578 0.3529  339 VAL B CA  
6687 C C   . VAL B 353 ? 1.0019 0.9908 0.9266 -0.1603 -0.1550 0.3544  339 VAL B C   
6688 O O   . VAL B 353 ? 1.0123 1.0031 0.9406 -0.1614 -0.1476 0.3434  339 VAL B O   
6689 C CB  . VAL B 353 ? 0.8263 0.8345 0.7588 -0.1398 -0.1508 0.3367  339 VAL B CB  
6690 C CG1 . VAL B 353 ? 0.6867 0.7066 0.6201 -0.1307 -0.1541 0.3363  339 VAL B CG1 
6691 C CG2 . VAL B 353 ? 0.7140 0.6956 0.6590 -0.1284 -0.1511 0.3293  339 VAL B CG2 
6692 N N   . HIS B 354 ? 1.0295 1.0095 0.9485 -0.1693 -0.1613 0.3687  340 HIS B N   
6693 C CA  . HIS B 354 ? 1.0970 1.0731 1.0120 -0.1834 -0.1593 0.3729  340 HIS B CA  
6694 C C   . HIS B 354 ? 1.2140 1.1544 1.1368 -0.1781 -0.1653 0.3760  340 HIS B C   
6695 O O   . HIS B 354 ? 1.5034 1.4253 1.4240 -0.1797 -0.1740 0.3894  340 HIS B O   
6696 C CB  . HIS B 354 ? 1.0552 1.0441 0.9579 -0.1982 -0.1625 0.3873  340 HIS B CB  
6697 C CG  . HIS B 354 ? 1.0041 1.0253 0.8973 -0.2032 -0.1585 0.3862  340 HIS B CG  
6698 N ND1 . HIS B 354 ? 0.9474 0.9781 0.8424 -0.1923 -0.1590 0.3810  340 HIS B ND1 
6699 C CD2 . HIS B 354 ? 1.0228 1.0670 0.9035 -0.2186 -0.1558 0.3923  340 HIS B CD2 
6700 C CE1 . HIS B 354 ? 0.8846 0.9430 0.7683 -0.2013 -0.1563 0.3827  340 HIS B CE1 
6701 N NE2 . HIS B 354 ? 0.9172 0.9841 0.7918 -0.2170 -0.1542 0.3894  340 HIS B NE2 
6702 N N   . ASP B 355 ? 1.1605 1.0921 1.0908 -0.1746 -0.1603 0.3642  341 ASP B N   
6703 C CA  . ASP B 355 ? 1.1761 1.1008 1.1036 -0.1882 -0.1597 0.3685  341 ASP B CA  
6704 C C   . ASP B 355 ? 1.1225 1.0480 1.0586 -0.1820 -0.1522 0.3519  341 ASP B C   
6705 O O   . ASP B 355 ? 1.0436 0.9903 0.9806 -0.1774 -0.1456 0.3422  341 ASP B O   
6706 C CB  . ASP B 355 ? 1.2772 1.1670 1.2067 -0.1894 -0.1682 0.3777  341 ASP B CB  
6707 C CG  . ASP B 355 ? 1.3483 1.2433 1.2700 -0.2090 -0.1679 0.3871  341 ASP B CG  
6708 O OD1 . ASP B 355 ? 1.4235 1.2865 1.3494 -0.2090 -0.1728 0.3888  341 ASP B OD1 
6709 O OD2 . ASP B 355 ? 1.2815 1.2100 1.1962 -0.2218 -0.1604 0.3862  341 ASP B OD2 
6710 N N   . THR B 356 ? 1.0793 0.9826 1.0210 -0.1835 -0.1528 0.3485  342 THR B N   
6711 C CA  . THR B 356 ? 0.9890 0.8933 0.9389 -0.1777 -0.1461 0.3328  342 THR B CA  
6712 C C   . THR B 356 ? 0.9561 0.8306 0.9158 -0.1662 -0.1484 0.3238  342 THR B C   
6713 O O   . THR B 356 ? 0.9609 0.8085 0.9213 -0.1687 -0.1540 0.3283  342 THR B O   
6714 C CB  . THR B 356 ? 1.0157 0.9384 0.9630 -0.1932 -0.1392 0.3310  342 THR B CB  
6715 O OG1 . THR B 356 ? 0.9748 0.9325 0.9167 -0.1980 -0.1314 0.3286  342 THR B OG1 
6716 C CG2 . THR B 356 ? 0.9757 0.8895 0.9317 -0.1903 -0.1353 0.3187  342 THR B CG2 
6717 N N   . PRO B 357 ? 0.8743 0.7525 0.8412 -0.1533 -0.1440 0.3102  343 PRO B N   
6718 C CA  . PRO B 357 ? 0.8355 0.6857 0.8110 -0.1422 -0.1461 0.3010  343 PRO B CA  
6719 C C   . PRO B 357 ? 0.8297 0.6682 0.8076 -0.1507 -0.1445 0.2958  343 PRO B C   
6720 O O   . PRO B 357 ? 0.8430 0.6515 0.8233 -0.1483 -0.1495 0.2949  343 PRO B O   
6721 C CB  . PRO B 357 ? 0.6892 0.5527 0.6706 -0.1298 -0.1407 0.2883  343 PRO B CB  
6722 C CG  . PRO B 357 ? 0.6504 0.5479 0.6271 -0.1362 -0.1343 0.2883  343 PRO B CG  
6723 C CD  . PRO B 357 ? 0.7782 0.6868 0.7454 -0.1525 -0.1352 0.3010  343 PRO B CD  
6724 N N   . PRO B 370 ? 1.0346 0.8232 1.0601 -0.1652 -0.1379 0.0564  356 PRO B N   
6725 C CA  . PRO B 370 ? 1.0410 0.8481 1.0676 -0.1610 -0.1367 0.0479  356 PRO B CA  
6726 C C   . PRO B 370 ? 1.0401 0.8248 1.0529 -0.1616 -0.1410 0.0328  356 PRO B C   
6727 O O   . PRO B 370 ? 1.0462 0.8246 1.0528 -0.1731 -0.1454 0.0297  356 PRO B O   
6728 C CB  . PRO B 370 ? 1.1773 1.0181 1.2147 -0.1729 -0.1372 0.0561  356 PRO B CB  
6729 C CG  . PRO B 370 ? 1.0175 0.8688 1.0637 -0.1743 -0.1335 0.0698  356 PRO B CG  
6730 C CD  . PRO B 370 ? 1.0160 0.8321 1.0524 -0.1736 -0.1356 0.0702  356 PRO B CD  
6731 N N   . ASP B 371 ? 0.9724 0.7529 0.9799 -0.1453 -0.1362 0.0228  357 ASP B N   
6732 C CA  . ASP B 371 ? 0.9656 0.7222 0.9587 -0.1409 -0.1377 0.0071  357 ASP B CA  
6733 C C   . ASP B 371 ? 0.8804 0.6559 0.8692 -0.1446 -0.1388 -0.0009 357 ASP B C   
6734 O O   . ASP B 371 ? 0.8520 0.6512 0.8474 -0.1562 -0.1419 0.0055  357 ASP B O   
6735 C CB  . ASP B 371 ? 0.8922 0.6388 0.8836 -0.1208 -0.1312 0.0015  357 ASP B CB  
6736 C CG  . ASP B 371 ? 0.9711 0.6778 0.9545 -0.1170 -0.1336 -0.0036 357 ASP B CG  
6737 O OD1 . ASP B 371 ? 1.0849 0.7674 1.0611 -0.1302 -0.1406 -0.0054 357 ASP B OD1 
6738 O OD2 . ASP B 371 ? 0.8482 0.5475 0.8327 -0.1006 -0.1288 -0.0059 357 ASP B OD2 
6739 N N   . GLY B 372 ? 0.8168 0.5798 0.7935 -0.1357 -0.1368 -0.0153 358 GLY B N   
6740 C CA  . GLY B 372 ? 0.6933 0.4764 0.6653 -0.1334 -0.1353 -0.0226 358 GLY B CA  
6741 C C   . GLY B 372 ? 0.6418 0.4377 0.6164 -0.1150 -0.1265 -0.0251 358 GLY B C   
6742 O O   . GLY B 372 ? 0.6086 0.4291 0.5957 -0.1099 -0.1225 -0.0151 358 GLY B O   
6743 N N   . SER B 373 ? 0.6073 0.3869 0.5703 -0.1053 -0.1234 -0.0386 359 SER B N   
6744 C CA  . SER B 373 ? 0.5730 0.3670 0.5370 -0.0897 -0.1154 -0.0424 359 SER B CA  
6745 C C   . SER B 373 ? 0.5543 0.3511 0.5304 -0.0772 -0.1100 -0.0339 359 SER B C   
6746 O O   . SER B 373 ? 0.5311 0.3066 0.5093 -0.0753 -0.1113 -0.0312 359 SER B O   
6747 C CB  . SER B 373 ? 0.6165 0.3918 0.5651 -0.0829 -0.1131 -0.0595 359 SER B CB  
6748 O OG  . SER B 373 ? 0.6384 0.4346 0.5847 -0.0741 -0.1070 -0.0639 359 SER B OG  
6749 N N   . LEU B 374 ? 0.5032 0.3255 0.4862 -0.0688 -0.1043 -0.0298 360 LEU B N   
6750 C CA  . LEU B 374 ? 0.5078 0.3370 0.5022 -0.0587 -0.0995 -0.0211 360 LEU B CA  
6751 C C   . LEU B 374 ? 0.5206 0.3323 0.5123 -0.0447 -0.0956 -0.0282 360 LEU B C   
6752 O O   . LEU B 374 ? 0.5231 0.3345 0.5076 -0.0370 -0.0919 -0.0393 360 LEU B O   
6753 C CB  . LEU B 374 ? 0.4651 0.3249 0.4665 -0.0544 -0.0948 -0.0158 360 LEU B CB  
6754 C CG  . LEU B 374 ? 0.4627 0.3437 0.4739 -0.0631 -0.0967 -0.0041 360 LEU B CG  
6755 C CD1 . LEU B 374 ? 0.4141 0.3203 0.4292 -0.0577 -0.0922 -0.0022 360 LEU B CD1 
6756 C CD2 . LEU B 374 ? 0.4390 0.3185 0.4601 -0.0639 -0.0965 0.0068  360 LEU B CD2 
6757 N N   . THR B 375 ? 0.5239 0.3227 0.5219 -0.0414 -0.0964 -0.0211 361 THR B N   
6758 C CA  . THR B 375 ? 0.5327 0.3196 0.5324 -0.0267 -0.0929 -0.0242 361 THR B CA  
6759 C C   . THR B 375 ? 0.5247 0.3276 0.5362 -0.0217 -0.0904 -0.0113 361 THR B C   
6760 O O   . THR B 375 ? 0.5012 0.3192 0.5184 -0.0302 -0.0915 -0.0009 361 THR B O   
6761 C CB  . THR B 375 ? 0.5496 0.3012 0.5446 -0.0266 -0.0975 -0.0277 361 THR B CB  
6762 O OG1 . THR B 375 ? 0.5523 0.2972 0.5520 -0.0376 -0.1029 -0.0149 361 THR B OG1 
6763 C CG2 . THR B 375 ? 0.5462 0.2797 0.5277 -0.0326 -0.1002 -0.0418 361 THR B CG2 
6764 N N   . GLN B 376 ? 0.5371 0.3376 0.5524 -0.0078 -0.0869 -0.0124 362 GLN B N   
6765 C CA  . GLN B 376 ? 0.5415 0.3531 0.5667 -0.0037 -0.0857 0.0000  362 GLN B CA  
6766 C C   . GLN B 376 ? 0.5143 0.3129 0.5416 -0.0135 -0.0914 0.0112  362 GLN B C   
6767 O O   . GLN B 376 ? 0.4731 0.2879 0.5062 -0.0190 -0.0911 0.0224  362 GLN B O   
6768 C CB  . GLN B 376 ? 0.5839 0.3909 0.6129 0.0122  -0.0829 -0.0027 362 GLN B CB  
6769 C CG  . GLN B 376 ? 0.6125 0.4401 0.6420 0.0214  -0.0763 -0.0106 362 GLN B CG  
6770 C CD  . GLN B 376 ? 0.6135 0.4693 0.6499 0.0213  -0.0729 -0.0020 362 GLN B CD  
6771 O OE1 . GLN B 376 ? 0.5892 0.4485 0.6314 0.0192  -0.0746 0.0094  362 GLN B OE1 
6772 N NE2 . GLN B 376 ? 0.5534 0.4289 0.5883 0.0229  -0.0681 -0.0074 362 GLN B NE2 
6773 N N   . ASP B 377 ? 0.5416 0.3108 0.5635 -0.0167 -0.0965 0.0081  363 ASP B N   
6774 C CA  . ASP B 377 ? 0.5573 0.3112 0.5804 -0.0267 -0.1023 0.0192  363 ASP B CA  
6775 C C   . ASP B 377 ? 0.5389 0.3094 0.5634 -0.0428 -0.1039 0.0264  363 ASP B C   
6776 O O   . ASP B 377 ? 0.5316 0.3134 0.5621 -0.0481 -0.1041 0.0392  363 ASP B O   
6777 C CB  . ASP B 377 ? 0.6189 0.3360 0.6343 -0.0281 -0.1076 0.0124  363 ASP B CB  
6778 C CG  . ASP B 377 ? 0.6881 0.3844 0.7049 -0.0350 -0.1138 0.0246  363 ASP B CG  
6779 O OD1 . ASP B 377 ? 0.6831 0.3813 0.6992 -0.0512 -0.1175 0.0321  363 ASP B OD1 
6780 O OD2 . ASP B 377 ? 0.8431 0.5225 0.8623 -0.0242 -0.1150 0.0276  363 ASP B OD2 
6781 N N   . ASN B 378 ? 0.5147 0.2882 0.5340 -0.0509 -0.1050 0.0186  364 ASN B N   
6782 C CA  . ASN B 378 ? 0.4870 0.2767 0.5093 -0.0660 -0.1071 0.0259  364 ASN B CA  
6783 C C   . ASN B 378 ? 0.4386 0.2628 0.4687 -0.0636 -0.1016 0.0305  364 ASN B C   
6784 O O   . ASN B 378 ? 0.4350 0.2759 0.4711 -0.0733 -0.1020 0.0392  364 ASN B O   
6785 C CB  . ASN B 378 ? 0.5017 0.2831 0.5162 -0.0769 -0.1116 0.0172  364 ASN B CB  
6786 C CG  . ASN B 378 ? 0.5206 0.3106 0.5293 -0.0702 -0.1083 0.0042  364 ASN B CG  
6787 O OD1 . ASN B 378 ? 0.5058 0.3165 0.5184 -0.0607 -0.1026 0.0038  364 ASN B OD1 
6788 N ND2 . ASN B 378 ? 0.5524 0.3258 0.5504 -0.0761 -0.1122 -0.0064 364 ASN B ND2 
6789 N N   . PHE B 379 ? 0.4424 0.2775 0.4729 -0.0510 -0.0962 0.0249  365 PHE B N   
6790 C CA  . PHE B 379 ? 0.4159 0.2802 0.4533 -0.0482 -0.0910 0.0295  365 PHE B CA  
6791 C C   . PHE B 379 ? 0.3963 0.2683 0.4407 -0.0479 -0.0895 0.0414  365 PHE B C   
6792 O O   . PHE B 379 ? 0.3727 0.2644 0.4229 -0.0538 -0.0877 0.0484  365 PHE B O   
6793 C CB  . PHE B 379 ? 0.3954 0.2677 0.4310 -0.0357 -0.0860 0.0214  365 PHE B CB  
6794 C CG  . PHE B 379 ? 0.3846 0.2819 0.4268 -0.0315 -0.0808 0.0266  365 PHE B CG  
6795 C CD1 . PHE B 379 ? 0.3456 0.2626 0.3902 -0.0359 -0.0793 0.0272  365 PHE B CD1 
6796 C CD2 . PHE B 379 ? 0.3626 0.2630 0.4087 -0.0236 -0.0780 0.0315  365 PHE B CD2 
6797 C CE1 . PHE B 379 ? 0.3394 0.2764 0.3895 -0.0321 -0.0746 0.0315  365 PHE B CE1 
6798 C CE2 . PHE B 379 ? 0.3397 0.2615 0.3906 -0.0210 -0.0735 0.0356  365 PHE B CE2 
6799 C CZ  . PHE B 379 ? 0.3159 0.2547 0.3686 -0.0251 -0.0715 0.0351  365 PHE B CZ  
6800 N N   . TRP B 380 ? 0.4057 0.2635 0.4495 -0.0405 -0.0898 0.0437  366 TRP B N   
6801 C CA  . TRP B 380 ? 0.4017 0.2670 0.4504 -0.0408 -0.0889 0.0554  366 TRP B CA  
6802 C C   . TRP B 380 ? 0.4041 0.2652 0.4539 -0.0547 -0.0928 0.0650  366 TRP B C   
6803 O O   . TRP B 380 ? 0.4017 0.2796 0.4558 -0.0593 -0.0905 0.0743  366 TRP B O   
6804 C CB  . TRP B 380 ? 0.3922 0.2437 0.4404 -0.0295 -0.0895 0.0564  366 TRP B CB  
6805 C CG  . TRP B 380 ? 0.3888 0.2528 0.4383 -0.0168 -0.0845 0.0490  366 TRP B CG  
6806 C CD1 . TRP B 380 ? 0.3945 0.2485 0.4415 -0.0068 -0.0838 0.0387  366 TRP B CD1 
6807 C CD2 . TRP B 380 ? 0.3889 0.2788 0.4421 -0.0140 -0.0793 0.0510  366 TRP B CD2 
6808 N NE1 . TRP B 380 ? 0.3959 0.2694 0.4454 0.0015  -0.0785 0.0351  366 TRP B NE1 
6809 C CE2 . TRP B 380 ? 0.3931 0.2875 0.4461 -0.0031 -0.0760 0.0425  366 TRP B CE2 
6810 C CE3 . TRP B 380 ? 0.3575 0.2668 0.4140 -0.0198 -0.0767 0.0586  366 TRP B CE3 
6811 C CZ2 . TRP B 380 ? 0.3795 0.2958 0.4352 0.0011  -0.0711 0.0423  366 TRP B CZ2 
6812 C CZ3 . TRP B 380 ? 0.3334 0.2627 0.3920 -0.0148 -0.0717 0.0572  366 TRP B CZ3 
6813 C CH2 . TRP B 380 ? 0.3484 0.2805 0.4065 -0.0049 -0.0693 0.0495  366 TRP B CH2 
6814 N N   . LYS B 381 ? 0.4388 0.2783 0.4841 -0.0623 -0.0984 0.0627  367 LYS B N   
6815 C CA  . LYS B 381 ? 0.4336 0.2711 0.4801 -0.0776 -0.1022 0.0718  367 LYS B CA  
6816 C C   . LYS B 381 ? 0.3960 0.2612 0.4482 -0.0861 -0.0997 0.0732  367 LYS B C   
6817 O O   . LYS B 381 ? 0.3983 0.2775 0.4556 -0.0950 -0.0989 0.0831  367 LYS B O   
6818 C CB  . LYS B 381 ? 0.4569 0.2640 0.4967 -0.0846 -0.1092 0.0679  367 LYS B CB  
6819 C CG  . LYS B 381 ? 0.5133 0.2924 0.5498 -0.0815 -0.1132 0.0732  367 LYS B CG  
6820 C CD  . LYS B 381 ? 0.5691 0.3139 0.5977 -0.0841 -0.1192 0.0653  367 LYS B CD  
6821 C CE  . LYS B 381 ? 0.6133 0.3286 0.6396 -0.0792 -0.1234 0.0712  367 LYS B CE  
6822 N NZ  . LYS B 381 ? 0.6666 0.3547 0.6873 -0.0673 -0.1246 0.0579  367 LYS B NZ  
6823 N N   . THR B 382 ? 0.3871 0.2613 0.4387 -0.0831 -0.0983 0.0636  368 THR B N   
6824 C CA  . THR B 382 ? 0.3992 0.3003 0.4577 -0.0893 -0.0962 0.0654  368 THR B CA  
6825 C C   . THR B 382 ? 0.3773 0.3025 0.4427 -0.0836 -0.0895 0.0710  368 THR B C   
6826 O O   . THR B 382 ? 0.3605 0.3056 0.4332 -0.0905 -0.0875 0.0777  368 THR B O   
6827 C CB  . THR B 382 ? 0.3854 0.2905 0.4410 -0.0867 -0.0968 0.0548  368 THR B CB  
6828 O OG1 . THR B 382 ? 0.3754 0.2563 0.4223 -0.0917 -0.1027 0.0479  368 THR B OG1 
6829 C CG2 . THR B 382 ? 0.3746 0.3064 0.4384 -0.0935 -0.0961 0.0579  368 THR B CG2 
6830 N N   . LEU B 383 ? 0.3669 0.2911 0.4301 -0.0712 -0.0858 0.0678  369 LEU B N   
6831 C CA  . LEU B 383 ? 0.3559 0.3010 0.4240 -0.0661 -0.0796 0.0720  369 LEU B CA  
6832 C C   . LEU B 383 ? 0.3376 0.2853 0.4075 -0.0720 -0.0791 0.0829  369 LEU B C   
6833 O O   . LEU B 383 ? 0.3137 0.2823 0.3886 -0.0738 -0.0743 0.0875  369 LEU B O   
6834 C CB  . LEU B 383 ? 0.3363 0.2790 0.4012 -0.0529 -0.0766 0.0664  369 LEU B CB  
6835 C CG  . LEU B 383 ? 0.3117 0.2757 0.3802 -0.0475 -0.0703 0.0676  369 LEU B CG  
6836 C CD1 . LEU B 383 ? 0.3122 0.2926 0.3849 -0.0486 -0.0680 0.0640  369 LEU B CD1 
6837 C CD2 . LEU B 383 ? 0.3272 0.2880 0.3925 -0.0363 -0.0682 0.0635  369 LEU B CD2 
6838 N N   . GLN B 384 ? 0.3482 0.2742 0.4136 -0.0751 -0.0839 0.0871  370 GLN B N   
6839 C CA  . GLN B 384 ? 0.3474 0.2738 0.4130 -0.0821 -0.0844 0.0989  370 GLN B CA  
6840 C C   . GLN B 384 ? 0.3563 0.3011 0.4277 -0.0950 -0.0831 0.1052  370 GLN B C   
6841 O O   . GLN B 384 ? 0.3284 0.2895 0.4020 -0.0984 -0.0790 0.1129  370 GLN B O   
6842 C CB  . GLN B 384 ? 0.3643 0.2605 0.4241 -0.0844 -0.0913 0.1021  370 GLN B CB  
6843 C CG  . GLN B 384 ? 0.3969 0.2894 0.4554 -0.0927 -0.0933 0.1156  370 GLN B CG  
6844 C CD  . GLN B 384 ? 0.3780 0.2850 0.4363 -0.0864 -0.0889 0.1212  370 GLN B CD  
6845 O OE1 . GLN B 384 ? 0.3878 0.2893 0.4442 -0.0742 -0.0886 0.1177  370 GLN B OE1 
6846 N NE2 . GLN B 384 ? 0.3690 0.2953 0.4289 -0.0951 -0.0856 0.1300  370 GLN B NE2 
6847 N N   . THR B 385 ? 0.3657 0.3095 0.4395 -0.1027 -0.0863 0.1020  371 THR B N   
6848 C CA  . THR B 385 ? 0.3736 0.3378 0.4550 -0.1149 -0.0852 0.1082  371 THR B CA  
6849 C C   . THR B 385 ? 0.3676 0.3622 0.4572 -0.1098 -0.0778 0.1062  371 THR B C   
6850 O O   . THR B 385 ? 0.3734 0.3895 0.4707 -0.1175 -0.0749 0.1119  371 THR B O   
6851 C CB  . THR B 385 ? 0.3889 0.3448 0.4709 -0.1252 -0.0916 0.1055  371 THR B CB  
6852 O OG1 . THR B 385 ? 0.3985 0.3608 0.4821 -0.1186 -0.0912 0.0954  371 THR B OG1 
6853 C CG2 . THR B 385 ? 0.3923 0.3137 0.4650 -0.1288 -0.0990 0.1049  371 THR B CG2 
6854 N N   . PHE B 386 ? 0.3571 0.3540 0.4454 -0.0969 -0.0746 0.0983  372 PHE B N   
6855 C CA  . PHE B 386 ? 0.3330 0.3541 0.4284 -0.0911 -0.0684 0.0950  372 PHE B CA  
6856 C C   . PHE B 386 ? 0.3105 0.3450 0.4061 -0.0858 -0.0613 0.0979  372 PHE B C   
6857 O O   . PHE B 386 ? 0.2824 0.3393 0.3854 -0.0859 -0.0556 0.0988  372 PHE B O   
6858 C CB  . PHE B 386 ? 0.3257 0.3410 0.4186 -0.0814 -0.0693 0.0852  372 PHE B CB  
6859 C CG  . PHE B 386 ? 0.2831 0.3181 0.3816 -0.0736 -0.0633 0.0819  372 PHE B CG  
6860 C CD1 . PHE B 386 ? 0.2876 0.3421 0.3960 -0.0767 -0.0622 0.0828  372 PHE B CD1 
6861 C CD2 . PHE B 386 ? 0.2899 0.3233 0.3840 -0.0633 -0.0595 0.0779  372 PHE B CD2 
6862 C CE1 . PHE B 386 ? 0.2744 0.3444 0.3883 -0.0689 -0.0572 0.0799  372 PHE B CE1 
6863 C CE2 . PHE B 386 ? 0.2757 0.3242 0.3741 -0.0568 -0.0545 0.0747  372 PHE B CE2 
6864 C CZ  . PHE B 386 ? 0.2635 0.3291 0.3717 -0.0592 -0.0533 0.0757  372 PHE B CZ  
6865 N N   . ILE B 387 ? 0.2948 0.3165 0.3826 -0.0809 -0.0613 0.0988  373 ILE B N   
6866 C CA  . ILE B 387 ? 0.2922 0.3263 0.3784 -0.0762 -0.0551 0.1006  373 ILE B CA  
6867 C C   . ILE B 387 ? 0.3041 0.3538 0.3929 -0.0856 -0.0516 0.1092  373 ILE B C   
6868 O O   . ILE B 387 ? 0.2955 0.3415 0.3853 -0.0963 -0.0552 0.1160  373 ILE B O   
6869 C CB  . ILE B 387 ? 0.2753 0.2934 0.3529 -0.0698 -0.0572 0.1009  373 ILE B CB  
6870 C CG1 . ILE B 387 ? 0.2748 0.2774 0.3481 -0.0773 -0.0626 0.1098  373 ILE B CG1 
6871 C CG2 . ILE B 387 ? 0.2432 0.2492 0.3190 -0.0603 -0.0595 0.0917  373 ILE B CG2 
6872 C CD1 . ILE B 387 ? 0.3127 0.3025 0.3791 -0.0714 -0.0649 0.1129  373 ILE B CD1 
6873 N N   . ARG B 388 ? 0.2914 0.3589 0.3808 -0.0822 -0.0443 0.1085  374 ARG B N   
6874 C CA  . ARG B 388 ? 0.2999 0.3875 0.3924 -0.0899 -0.0388 0.1145  374 ARG B CA  
6875 C C   . ARG B 388 ? 0.2993 0.3943 0.3844 -0.0861 -0.0331 0.1147  374 ARG B C   
6876 O O   . ARG B 388 ? 0.2763 0.3646 0.3567 -0.0770 -0.0329 0.1089  374 ARG B O   
6877 C CB  . ARG B 388 ? 0.2995 0.4081 0.4044 -0.0900 -0.0343 0.1110  374 ARG B CB  
6878 C CG  . ARG B 388 ? 0.3546 0.4797 0.4668 -0.1023 -0.0329 0.1188  374 ARG B CG  
6879 C CD  . ARG B 388 ? 0.3527 0.4754 0.4729 -0.1092 -0.0392 0.1201  374 ARG B CD  
6880 N NE  . ARG B 388 ? 0.3568 0.4511 0.4694 -0.1101 -0.0482 0.1196  374 ARG B NE  
6881 C CZ  . ARG B 388 ? 0.3417 0.4271 0.4570 -0.1178 -0.0551 0.1208  374 ARG B CZ  
6882 N NH1 . ARG B 388 ? 0.3435 0.4476 0.4698 -0.1256 -0.0550 0.1232  374 ARG B NH1 
6883 N NH2 . ARG B 388 ? 0.3656 0.4232 0.4724 -0.1177 -0.0624 0.1192  374 ARG B NH2 
6884 N N   . PRO B 389 ? 0.2951 0.4046 0.3784 -0.0938 -0.0287 0.1214  375 PRO B N   
6885 C CA  . PRO B 389 ? 0.2726 0.3917 0.3479 -0.0908 -0.0227 0.1203  375 PRO B CA  
6886 C C   . PRO B 389 ? 0.2805 0.4100 0.3597 -0.0809 -0.0161 0.1093  375 PRO B C   
6887 O O   . PRO B 389 ? 0.2690 0.4074 0.3590 -0.0783 -0.0136 0.1047  375 PRO B O   
6888 C CB  . PRO B 389 ? 0.2840 0.4212 0.3586 -0.1019 -0.0179 0.1284  375 PRO B CB  
6889 C CG  . PRO B 389 ? 0.2994 0.4262 0.3763 -0.1121 -0.0250 0.1376  375 PRO B CG  
6890 C CD  . PRO B 389 ? 0.3175 0.4315 0.4026 -0.1071 -0.0304 0.1316  375 PRO B CD  
6891 N N   . GLY B 390 ? 0.2989 0.4260 0.3692 -0.0753 -0.0141 0.1054  376 GLY B N   
6892 C CA  . GLY B 390 ? 0.2671 0.3997 0.3390 -0.0663 -0.0087 0.0950  376 GLY B CA  
6893 C C   . GLY B 390 ? 0.2577 0.3751 0.3309 -0.0578 -0.0134 0.0890  376 GLY B C   
6894 O O   . GLY B 390 ? 0.2639 0.3823 0.3355 -0.0510 -0.0100 0.0814  376 GLY B O   
6895 N N   . ASP B 391 ? 0.2413 0.3439 0.3163 -0.0585 -0.0211 0.0920  377 ASP B N   
6896 C CA  . ASP B 391 ? 0.2486 0.3385 0.3245 -0.0509 -0.0250 0.0860  377 ASP B CA  
6897 C C   . ASP B 391 ? 0.2462 0.3306 0.3135 -0.0457 -0.0252 0.0832  377 ASP B C   
6898 O O   . ASP B 391 ? 0.2510 0.3345 0.3109 -0.0486 -0.0263 0.0883  377 ASP B O   
6899 C CB  . ASP B 391 ? 0.2601 0.3346 0.3377 -0.0532 -0.0328 0.0892  377 ASP B CB  
6900 C CG  . ASP B 391 ? 0.2612 0.3402 0.3482 -0.0571 -0.0338 0.0893  377 ASP B CG  
6901 O OD1 . ASP B 391 ? 0.2311 0.3253 0.3251 -0.0559 -0.0287 0.0864  377 ASP B OD1 
6902 O OD2 . ASP B 391 ? 0.2562 0.3233 0.3436 -0.0616 -0.0399 0.0924  377 ASP B OD2 
6903 N N   . ILE B 392 ? 0.2170 0.2989 0.2853 -0.0387 -0.0244 0.0757  378 ILE B N   
6904 C CA  . ILE B 392 ? 0.2414 0.3166 0.3035 -0.0338 -0.0263 0.0728  378 ILE B CA  
6905 C C   . ILE B 392 ? 0.2432 0.3056 0.3080 -0.0300 -0.0319 0.0710  378 ILE B C   
6906 O O   . ILE B 392 ? 0.2315 0.2930 0.3013 -0.0277 -0.0318 0.0668  378 ILE B O   
6907 C CB  . ILE B 392 ? 0.2098 0.2911 0.2700 -0.0299 -0.0211 0.0656  378 ILE B CB  
6908 C CG1 . ILE B 392 ? 0.2311 0.3247 0.2879 -0.0333 -0.0146 0.0654  378 ILE B CG1 
6909 C CG2 . ILE B 392 ? 0.2273 0.3033 0.2814 -0.0264 -0.0237 0.0635  378 ILE B CG2 
6910 C CD1 . ILE B 392 ? 0.2195 0.3161 0.2735 -0.0295 -0.0095 0.0572  378 ILE B CD1 
6911 N N   . ILE B 393 ? 0.2355 0.2884 0.2968 -0.0291 -0.0368 0.0745  379 ILE B N   
6912 C CA  . ILE B 393 ? 0.2328 0.2728 0.2960 -0.0254 -0.0418 0.0726  379 ILE B CA  
6913 C C   . ILE B 393 ? 0.2307 0.2687 0.2907 -0.0190 -0.0429 0.0698  379 ILE B C   
6914 O O   . ILE B 393 ? 0.2387 0.2782 0.2953 -0.0188 -0.0442 0.0742  379 ILE B O   
6915 C CB  . ILE B 393 ? 0.2303 0.2589 0.2936 -0.0293 -0.0469 0.0790  379 ILE B CB  
6916 C CG1 . ILE B 393 ? 0.2667 0.2998 0.3337 -0.0372 -0.0458 0.0825  379 ILE B CG1 
6917 C CG2 . ILE B 393 ? 0.2388 0.2523 0.3029 -0.0246 -0.0516 0.0753  379 ILE B CG2 
6918 C CD1 . ILE B 393 ? 0.2496 0.2706 0.3159 -0.0432 -0.0511 0.0899  379 ILE B CD1 
6919 N N   . LEU B 394 ? 0.2380 0.2747 0.2994 -0.0144 -0.0425 0.0632  380 LEU B N   
6920 C CA  . LEU B 394 ? 0.2080 0.2450 0.2678 -0.0087 -0.0432 0.0601  380 LEU B CA  
6921 C C   . LEU B 394 ? 0.2309 0.2572 0.2924 -0.0043 -0.0465 0.0568  380 LEU B C   
6922 O O   . LEU B 394 ? 0.2067 0.2283 0.2695 -0.0055 -0.0469 0.0537  380 LEU B O   
6923 C CB  . LEU B 394 ? 0.2059 0.2516 0.2646 -0.0077 -0.0391 0.0548  380 LEU B CB  
6924 C CG  . LEU B 394 ? 0.2288 0.2836 0.2850 -0.0116 -0.0349 0.0554  380 LEU B CG  
6925 C CD1 . LEU B 394 ? 0.2042 0.2607 0.2639 -0.0141 -0.0320 0.0542  380 LEU B CD1 
6926 C CD2 . LEU B 394 ? 0.1902 0.2510 0.2430 -0.0103 -0.0326 0.0514  380 LEU B CD2 
6927 N N   . ALA B 395 ? 0.2254 0.2485 0.2870 0.0010  -0.0490 0.0575  381 ALA B N   
6928 C CA  . ALA B 395 ? 0.2528 0.2658 0.3157 0.0065  -0.0513 0.0531  381 ALA B CA  
6929 C C   . ALA B 395 ? 0.2499 0.2702 0.3140 0.0134  -0.0504 0.0498  381 ALA B C   
6930 O O   . ALA B 395 ? 0.1962 0.2242 0.2610 0.0148  -0.0509 0.0539  381 ALA B O   
6931 C CB  . ALA B 395 ? 0.2493 0.2473 0.3129 0.0070  -0.0560 0.0575  381 ALA B CB  
6932 N N   . ASP B 396 ? 0.2228 0.2421 0.2870 0.0170  -0.0492 0.0426  382 ASP B N   
6933 C CA  . ASP B 396 ? 0.2402 0.2689 0.3063 0.0232  -0.0477 0.0392  382 ASP B CA  
6934 C C   . ASP B 396 ? 0.2492 0.2703 0.3189 0.0316  -0.0502 0.0382  382 ASP B C   
6935 O O   . ASP B 396 ? 0.2557 0.2609 0.3252 0.0325  -0.0531 0.0389  382 ASP B O   
6936 C CB  . ASP B 396 ? 0.2299 0.2643 0.2937 0.0225  -0.0443 0.0322  382 ASP B CB  
6937 C CG  . ASP B 396 ? 0.2161 0.2666 0.2805 0.0227  -0.0415 0.0316  382 ASP B CG  
6938 O OD1 . ASP B 396 ? 0.2182 0.2761 0.2865 0.0273  -0.0422 0.0334  382 ASP B OD1 
6939 O OD2 . ASP B 396 ? 0.2173 0.2730 0.2785 0.0181  -0.0391 0.0298  382 ASP B OD2 
6940 N N   . GLN B 397 ? 0.2541 0.2867 0.3277 0.0379  -0.0489 0.0364  383 GLN B N   
6941 C CA  . GLN B 397 ? 0.2474 0.2748 0.3263 0.0480  -0.0506 0.0347  383 GLN B CA  
6942 C C   . GLN B 397 ? 0.3056 0.3223 0.3820 0.0512  -0.0489 0.0253  383 GLN B C   
6943 O O   . GLN B 397 ? 0.3016 0.3222 0.3731 0.0466  -0.0458 0.0201  383 GLN B O   
6944 C CB  . GLN B 397 ? 0.2630 0.3096 0.3481 0.0537  -0.0493 0.0351  383 GLN B CB  
6945 C CG  . GLN B 397 ? 0.2547 0.3108 0.3414 0.0505  -0.0521 0.0444  383 GLN B CG  
6946 C CD  . GLN B 397 ? 0.2944 0.3362 0.3820 0.0520  -0.0574 0.0520  383 GLN B CD  
6947 O OE1 . GLN B 397 ? 0.3413 0.3765 0.4348 0.0612  -0.0603 0.0532  383 GLN B OE1 
6948 N NE2 . GLN B 397 ? 0.2700 0.3064 0.3518 0.0430  -0.0585 0.0571  383 GLN B NE2 
6949 N N   . GLY B 398 ? 0.3775 0.3793 0.4564 0.0587  -0.0513 0.0235  384 GLY B N   
6950 C CA  . GLY B 398 ? 0.3988 0.3854 0.4730 0.0602  -0.0505 0.0145  384 GLY B CA  
6951 C C   . GLY B 398 ? 0.4678 0.4308 0.5388 0.0564  -0.0554 0.0173  384 GLY B C   
6952 O O   . GLY B 398 ? 0.4584 0.4163 0.5321 0.0550  -0.0593 0.0266  384 GLY B O   
6953 N N   . THR B 399 ? 0.5137 0.4627 0.5783 0.0532  -0.0555 0.0101  385 THR B N   
6954 C CA  . THR B 399 ? 0.5163 0.4428 0.5778 0.0480  -0.0606 0.0132  385 THR B CA  
6955 C C   . THR B 399 ? 0.5016 0.4326 0.5623 0.0366  -0.0625 0.0228  385 THR B C   
6956 O O   . THR B 399 ? 0.5260 0.4433 0.5868 0.0326  -0.0669 0.0297  385 THR B O   
6957 C CB  . THR B 399 ? 0.5183 0.4311 0.5721 0.0451  -0.0605 0.0029  385 THR B CB  
6958 O OG1 . THR B 399 ? 0.4439 0.3686 0.4931 0.0355  -0.0590 0.0022  385 THR B OG1 
6959 C CG2 . THR B 399 ? 0.5575 0.4714 0.6108 0.0558  -0.0566 -0.0083 385 THR B CG2 
6960 N N   . SER B 400 ? 0.4289 0.3793 0.4894 0.0320  -0.0592 0.0242  386 SER B N   
6961 C CA  . SER B 400 ? 0.4200 0.3762 0.4806 0.0226  -0.0600 0.0323  386 SER B CA  
6962 C C   . SER B 400 ? 0.4158 0.3706 0.4797 0.0231  -0.0626 0.0422  386 SER B C   
6963 O O   . SER B 400 ? 0.4118 0.3561 0.4748 0.0170  -0.0660 0.0484  386 SER B O   
6964 C CB  . SER B 400 ? 0.3393 0.3155 0.3997 0.0198  -0.0557 0.0315  386 SER B CB  
6965 O OG  . SER B 400 ? 0.3465 0.3234 0.4030 0.0163  -0.0545 0.0252  386 SER B OG  
6966 N N   . ALA B 401 ? 0.5077 0.4741 0.5753 0.0294  -0.0615 0.0445  387 ALA B N   
6967 C CA  . ALA B 401 ? 0.4478 0.4154 0.5176 0.0292  -0.0644 0.0547  387 ALA B CA  
6968 C C   . ALA B 401 ? 0.4920 0.4383 0.5629 0.0326  -0.0698 0.0587  387 ALA B C   
6969 O O   . ALA B 401 ? 0.4874 0.4274 0.5572 0.0272  -0.0733 0.0682  387 ALA B O   
6970 C CB  . ALA B 401 ? 0.4029 0.3880 0.4767 0.0354  -0.0629 0.0560  387 ALA B CB  
6971 N N   . PHE B 402 ? 0.5496 0.4841 0.6223 0.0415  -0.0704 0.0515  388 PHE B N   
6972 C CA  . PHE B 402 ? 0.5845 0.4962 0.6586 0.0461  -0.0758 0.0550  388 PHE B CA  
6973 C C   . PHE B 402 ? 0.5612 0.4511 0.6298 0.0375  -0.0788 0.0547  388 PHE B C   
6974 O O   . PHE B 402 ? 0.6814 0.5499 0.7500 0.0387  -0.0840 0.0596  388 PHE B O   
6975 C CB  . PHE B 402 ? 0.6544 0.5614 0.7333 0.0603  -0.0749 0.0469  388 PHE B CB  
6976 C CG  . PHE B 402 ? 0.7127 0.6442 0.7980 0.0678  -0.0717 0.0468  388 PHE B CG  
6977 C CD1 . PHE B 402 ? 0.7001 0.6453 0.7887 0.0664  -0.0740 0.0578  388 PHE B CD1 
6978 C CD2 . PHE B 402 ? 0.8211 0.7632 0.9087 0.0753  -0.0667 0.0360  388 PHE B CD2 
6979 C CE1 . PHE B 402 ? 0.8554 0.8240 0.9498 0.0719  -0.0717 0.0580  388 PHE B CE1 
6980 C CE2 . PHE B 402 ? 0.7347 0.7010 0.8288 0.0808  -0.0640 0.0365  388 PHE B CE2 
6981 C CZ  . PHE B 402 ? 0.7829 0.7623 0.8806 0.0790  -0.0667 0.0475  388 PHE B CZ  
6982 N N   . GLY B 403 ? 0.4727 0.3671 0.5369 0.0287  -0.0763 0.0498  389 GLY B N   
6983 C CA  . GLY B 403 ? 0.4379 0.3172 0.4977 0.0178  -0.0796 0.0523  389 GLY B CA  
6984 C C   . GLY B 403 ? 0.4075 0.2974 0.4676 0.0075  -0.0802 0.0637  389 GLY B C   
6985 O O   . GLY B 403 ? 0.4078 0.2843 0.4664 0.0003  -0.0845 0.0714  389 GLY B O   
6986 N N   . ALA B 404 ? 0.3844 0.2980 0.4459 0.0063  -0.0756 0.0647  390 ALA B N   
6987 C CA  . ALA B 404 ? 0.3656 0.2918 0.4269 -0.0028 -0.0747 0.0737  390 ALA B CA  
6988 C C   . ALA B 404 ? 0.3681 0.2905 0.4295 -0.0029 -0.0783 0.0853  390 ALA B C   
6989 O O   . ALA B 404 ? 0.3403 0.2682 0.4000 -0.0121 -0.0785 0.0937  390 ALA B O   
6990 C CB  . ALA B 404 ? 0.3330 0.2828 0.3951 -0.0022 -0.0690 0.0708  390 ALA B CB  
6991 N N   . ILE B 405 ? 0.3887 0.3033 0.4523 0.0072  -0.0811 0.0862  391 ILE B N   
6992 C CA  . ILE B 405 ? 0.3561 0.2659 0.4197 0.0074  -0.0858 0.0984  391 ILE B CA  
6993 C C   . ILE B 405 ? 0.3726 0.2624 0.4330 -0.0017 -0.0907 0.1061  391 ILE B C   
6994 O O   . ILE B 405 ? 0.3653 0.2557 0.4236 -0.0076 -0.0937 0.1183  391 ILE B O   
6995 C CB  . ILE B 405 ? 0.3754 0.2788 0.4438 0.0214  -0.0887 0.0975  391 ILE B CB  
6996 C CG1 . ILE B 405 ? 0.3590 0.2649 0.4282 0.0222  -0.0934 0.1111  391 ILE B CG1 
6997 C CG2 . ILE B 405 ? 0.4216 0.2979 0.4910 0.0271  -0.0920 0.0920  391 ILE B CG2 
6998 C CD1 . ILE B 405 ? 0.3693 0.2731 0.4455 0.0369  -0.0965 0.1113  391 ILE B CD1 
6999 N N   . ASP B 406 ? 0.3757 0.2480 0.4350 -0.0040 -0.0919 0.0993  392 ASP B N   
7000 C CA  . ASP B 406 ? 0.3985 0.2497 0.4546 -0.0137 -0.0971 0.1058  392 ASP B CA  
7001 C C   . ASP B 406 ? 0.3997 0.2636 0.4539 -0.0286 -0.0947 0.1096  392 ASP B C   
7002 O O   . ASP B 406 ? 0.3977 0.2477 0.4494 -0.0390 -0.0987 0.1158  392 ASP B O   
7003 C CB  . ASP B 406 ? 0.4352 0.2606 0.4901 -0.0105 -0.0999 0.0962  392 ASP B CB  
7004 C CG  . ASP B 406 ? 0.4950 0.3037 0.5526 0.0047  -0.1025 0.0927  392 ASP B CG  
7005 O OD1 . ASP B 406 ? 0.5221 0.3256 0.5818 0.0092  -0.1065 0.1030  392 ASP B OD1 
7006 O OD2 . ASP B 406 ? 0.5558 0.3563 0.6133 0.0122  -0.1008 0.0798  392 ASP B OD2 
7007 N N   . LEU B 407 ? 0.3646 0.2542 0.4202 -0.0300 -0.0884 0.1060  393 LEU B N   
7008 C CA  . LEU B 407 ? 0.3629 0.2670 0.4183 -0.0426 -0.0857 0.1101  393 LEU B CA  
7009 C C   . LEU B 407 ? 0.3716 0.2801 0.4244 -0.0498 -0.0871 0.1240  393 LEU B C   
7010 O O   . LEU B 407 ? 0.3489 0.2631 0.4004 -0.0443 -0.0872 0.1289  393 LEU B O   
7011 C CB  . LEU B 407 ? 0.3373 0.2665 0.3951 -0.0407 -0.0786 0.1032  393 LEU B CB  
7012 C CG  . LEU B 407 ? 0.3492 0.2798 0.4089 -0.0373 -0.0765 0.0911  393 LEU B CG  
7013 C CD1 . LEU B 407 ? 0.3028 0.2567 0.3646 -0.0339 -0.0700 0.0865  393 LEU B CD1 
7014 C CD2 . LEU B 407 ? 0.3395 0.2642 0.3998 -0.0476 -0.0786 0.0904  393 LEU B CD2 
7015 N N   . ARG B 408 ? 0.3786 0.2852 0.4304 -0.0629 -0.0884 0.1309  394 ARG B N   
7016 C CA  . ARG B 408 ? 0.3812 0.2944 0.4297 -0.0727 -0.0891 0.1445  394 ARG B CA  
7017 C C   . ARG B 408 ? 0.3850 0.3283 0.4351 -0.0783 -0.0811 0.1437  394 ARG B C   
7018 O O   . ARG B 408 ? 0.3917 0.3432 0.4451 -0.0870 -0.0788 0.1426  394 ARG B O   
7019 C CB  . ARG B 408 ? 0.4150 0.3088 0.4618 -0.0846 -0.0950 0.1525  394 ARG B CB  
7020 C CG  . ARG B 408 ? 0.4967 0.3938 0.5390 -0.0958 -0.0967 0.1683  394 ARG B CG  
7021 C CD  . ARG B 408 ? 0.5455 0.4166 0.5849 -0.1038 -0.1039 0.1743  394 ARG B CD  
7022 N NE  . ARG B 408 ? 0.7162 0.5917 0.7502 -0.1108 -0.1050 0.1856  394 ARG B NE  
7023 C CZ  . ARG B 408 ? 0.8033 0.6840 0.8354 -0.1247 -0.1049 0.1913  394 ARG B CZ  
7024 N NH1 . ARG B 408 ? 0.7621 0.6459 0.7980 -0.1333 -0.1037 0.1869  394 ARG B NH1 
7025 N NH2 . ARG B 408 ? 0.6679 0.5521 0.6944 -0.1303 -0.1062 0.2018  394 ARG B NH2 
7026 N N   . LEU B 409 ? 0.3497 0.3095 0.3975 -0.0735 -0.0772 0.1444  395 LEU B N   
7027 C CA  . LEU B 409 ? 0.3420 0.3286 0.3913 -0.0749 -0.0688 0.1399  395 LEU B CA  
7028 C C   . LEU B 409 ? 0.3537 0.3553 0.4006 -0.0877 -0.0657 0.1493  395 LEU B C   
7029 O O   . LEU B 409 ? 0.3621 0.3598 0.4027 -0.0930 -0.0689 0.1607  395 LEU B O   
7030 C CB  . LEU B 409 ? 0.3238 0.3204 0.3703 -0.0657 -0.0661 0.1363  395 LEU B CB  
7031 C CG  . LEU B 409 ? 0.3231 0.3125 0.3724 -0.0531 -0.0671 0.1262  395 LEU B CG  
7032 C CD1 . LEU B 409 ? 0.2911 0.2956 0.3375 -0.0477 -0.0637 0.1241  395 LEU B CD1 
7033 C CD2 . LEU B 409 ? 0.2904 0.2812 0.3454 -0.0513 -0.0642 0.1154  395 LEU B CD2 
7034 N N   . PRO B 410 ? 0.3418 0.3615 0.3936 -0.0927 -0.0594 0.1454  396 PRO B N   
7035 C CA  . PRO B 410 ? 0.3496 0.3892 0.3996 -0.1035 -0.0543 0.1529  396 PRO B CA  
7036 C C   . PRO B 410 ? 0.3503 0.4079 0.3943 -0.1002 -0.0481 0.1515  396 PRO B C   
7037 O O   . PRO B 410 ? 0.3447 0.3989 0.3861 -0.0903 -0.0485 0.1459  396 PRO B O   
7038 C CB  . PRO B 410 ? 0.3603 0.4140 0.4200 -0.1073 -0.0497 0.1474  396 PRO B CB  
7039 C CG  . PRO B 410 ? 0.3495 0.3918 0.4147 -0.0977 -0.0522 0.1365  396 PRO B CG  
7040 C CD  . PRO B 410 ? 0.3228 0.3486 0.3822 -0.0875 -0.0561 0.1338  396 PRO B CD  
7041 N N   . ALA B 411 ? 0.3550 0.4332 0.3969 -0.1090 -0.0418 0.1559  397 ALA B N   
7042 C CA  . ALA B 411 ? 0.3548 0.4508 0.3892 -0.1076 -0.0352 0.1541  397 ALA B CA  
7043 C C   . ALA B 411 ? 0.3786 0.4839 0.4174 -0.0973 -0.0288 0.1399  397 ALA B C   
7044 O O   . ALA B 411 ? 0.3464 0.4525 0.3953 -0.0938 -0.0272 0.1328  397 ALA B O   
7045 C CB  . ALA B 411 ? 0.3665 0.4835 0.3979 -0.1196 -0.0288 0.1608  397 ALA B CB  
7046 N N   . ASP B 412 ? 0.3659 0.4778 0.3965 -0.0931 -0.0259 0.1363  398 ASP B N   
7047 C CA  . ASP B 412 ? 0.3632 0.4842 0.3955 -0.0850 -0.0193 0.1236  398 ASP B CA  
7048 C C   . ASP B 412 ? 0.3382 0.4460 0.3788 -0.0753 -0.0225 0.1155  398 ASP B C   
7049 O O   . ASP B 412 ? 0.3163 0.4299 0.3646 -0.0711 -0.0180 0.1071  398 ASP B O   
7050 C CB  . ASP B 412 ? 0.4184 0.5602 0.4546 -0.0880 -0.0092 0.1189  398 ASP B CB  
7051 C CG  . ASP B 412 ? 0.6536 0.8106 0.6818 -0.0989 -0.0052 0.1272  398 ASP B CG  
7052 O OD1 . ASP B 412 ? 0.6119 0.7641 0.6290 -0.1035 -0.0098 0.1356  398 ASP B OD1 
7053 O OD2 . ASP B 412 ? 0.8374 1.0124 0.8708 -0.1030 0.0025  0.1257  398 ASP B OD2 
7054 N N   . VAL B 413 ? 0.3165 0.4071 0.3555 -0.0714 -0.0304 0.1182  399 VAL B N   
7055 C CA  . VAL B 413 ? 0.2966 0.3753 0.3412 -0.0623 -0.0335 0.1105  399 VAL B CA  
7056 C C   . VAL B 413 ? 0.2783 0.3560 0.3171 -0.0558 -0.0343 0.1069  399 VAL B C   
7057 O O   . VAL B 413 ? 0.2764 0.3519 0.3084 -0.0572 -0.0383 0.1138  399 VAL B O   
7058 C CB  . VAL B 413 ? 0.2979 0.3578 0.3464 -0.0624 -0.0413 0.1148  399 VAL B CB  
7059 C CG1 . VAL B 413 ? 0.2792 0.3276 0.3309 -0.0524 -0.0443 0.1068  399 VAL B CG1 
7060 C CG2 . VAL B 413 ? 0.2928 0.3543 0.3481 -0.0692 -0.0407 0.1167  399 VAL B CG2 
7061 N N   . ASN B 414 ? 0.2615 0.3415 0.3030 -0.0493 -0.0311 0.0970  400 ASN B N   
7062 C CA  . ASN B 414 ? 0.2708 0.3495 0.3082 -0.0436 -0.0326 0.0930  400 ASN B CA  
7063 C C   . ASN B 414 ? 0.2561 0.3213 0.2993 -0.0367 -0.0377 0.0905  400 ASN B C   
7064 O O   . ASN B 414 ? 0.2456 0.3081 0.2945 -0.0336 -0.0363 0.0841  400 ASN B O   
7065 C CB  . ASN B 414 ? 0.2542 0.3429 0.2895 -0.0418 -0.0258 0.0840  400 ASN B CB  
7066 C CG  . ASN B 414 ? 0.2694 0.3591 0.2990 -0.0386 -0.0272 0.0809  400 ASN B CG  
7067 O OD1 . ASN B 414 ? 0.2519 0.3347 0.2829 -0.0346 -0.0330 0.0830  400 ASN B OD1 
7068 N ND2 . ASN B 414 ? 0.2297 0.3286 0.2528 -0.0406 -0.0220 0.0759  400 ASN B ND2 
7069 N N   . PHE B 415 ? 0.2510 0.3081 0.2927 -0.0342 -0.0438 0.0957  401 PHE B N   
7070 C CA  . PHE B 415 ? 0.2480 0.2921 0.2947 -0.0272 -0.0485 0.0933  401 PHE B CA  
7071 C C   . PHE B 415 ? 0.2205 0.2692 0.2662 -0.0209 -0.0491 0.0895  401 PHE B C   
7072 O O   . PHE B 415 ? 0.2323 0.2847 0.2746 -0.0206 -0.0521 0.0950  401 PHE B O   
7073 C CB  . PHE B 415 ? 0.2575 0.2880 0.3048 -0.0281 -0.0549 0.1019  401 PHE B CB  
7074 C CG  . PHE B 415 ? 0.2596 0.2748 0.3118 -0.0210 -0.0590 0.0982  401 PHE B CG  
7075 C CD1 . PHE B 415 ? 0.2618 0.2744 0.3155 -0.0126 -0.0621 0.0972  401 PHE B CD1 
7076 C CD2 . PHE B 415 ? 0.2693 0.2735 0.3246 -0.0231 -0.0599 0.0958  401 PHE B CD2 
7077 C CE1 . PHE B 415 ? 0.2747 0.2737 0.3326 -0.0054 -0.0649 0.0928  401 PHE B CE1 
7078 C CE2 . PHE B 415 ? 0.3041 0.2935 0.3623 -0.0170 -0.0633 0.0913  401 PHE B CE2 
7079 C CZ  . PHE B 415 ? 0.2873 0.2738 0.3466 -0.0076 -0.0654 0.0894  401 PHE B CZ  
7080 N N   . ILE B 416 ? 0.2246 0.2743 0.2733 -0.0166 -0.0466 0.0809  402 ILE B N   
7081 C CA  . ILE B 416 ? 0.2311 0.2878 0.2791 -0.0123 -0.0462 0.0766  402 ILE B CA  
7082 C C   . ILE B 416 ? 0.2454 0.2945 0.2988 -0.0047 -0.0494 0.0738  402 ILE B C   
7083 O O   . ILE B 416 ? 0.2105 0.2539 0.2667 -0.0028 -0.0481 0.0680  402 ILE B O   
7084 C CB  . ILE B 416 ? 0.2453 0.3095 0.2916 -0.0140 -0.0405 0.0692  402 ILE B CB  
7085 C CG1 . ILE B 416 ? 0.2395 0.3119 0.2799 -0.0204 -0.0367 0.0708  402 ILE B CG1 
7086 C CG2 . ILE B 416 ? 0.2029 0.2725 0.2491 -0.0103 -0.0406 0.0647  402 ILE B CG2 
7087 C CD1 . ILE B 416 ? 0.2395 0.3161 0.2789 -0.0216 -0.0307 0.0633  402 ILE B CD1 
7088 N N   . VAL B 417 ? 0.2278 0.2780 0.2825 -0.0002 -0.0534 0.0777  403 VAL B N   
7089 C CA  . VAL B 417 ? 0.2377 0.2831 0.2980 0.0083  -0.0558 0.0746  403 VAL B CA  
7090 C C   . VAL B 417 ? 0.2350 0.2936 0.2969 0.0119  -0.0573 0.0761  403 VAL B C   
7091 O O   . VAL B 417 ? 0.2472 0.3138 0.3057 0.0084  -0.0591 0.0823  403 VAL B O   
7092 C CB  . VAL B 417 ? 0.2529 0.2818 0.3160 0.0116  -0.0606 0.0791  403 VAL B CB  
7093 C CG1 . VAL B 417 ? 0.2426 0.2714 0.3043 0.0103  -0.0653 0.0900  403 VAL B CG1 
7094 C CG2 . VAL B 417 ? 0.2644 0.2870 0.3331 0.0211  -0.0618 0.0737  403 VAL B CG2 
7095 N N   . GLN B 418 ? 0.2333 0.2954 0.3002 0.0185  -0.0567 0.0705  404 GLN B N   
7096 C CA  . GLN B 418 ? 0.2119 0.2900 0.2816 0.0213  -0.0574 0.0707  404 GLN B CA  
7097 C C   . GLN B 418 ? 0.2289 0.3059 0.3075 0.0320  -0.0605 0.0711  404 GLN B C   
7098 O O   . GLN B 418 ? 0.2399 0.3240 0.3231 0.0370  -0.0581 0.0649  404 GLN B O   
7099 C CB  . GLN B 418 ? 0.2074 0.2952 0.2752 0.0179  -0.0525 0.0632  404 GLN B CB  
7100 C CG  . GLN B 418 ? 0.1933 0.2996 0.2624 0.0170  -0.0530 0.0637  404 GLN B CG  
7101 C CD  . GLN B 418 ? 0.1887 0.3020 0.2573 0.0149  -0.0487 0.0563  404 GLN B CD  
7102 O OE1 . GLN B 418 ? 0.1857 0.2960 0.2580 0.0197  -0.0468 0.0515  404 GLN B OE1 
7103 N NE2 . GLN B 418 ? 0.1684 0.2900 0.2314 0.0071  -0.0471 0.0553  404 GLN B NE2 
7104 N N   . PRO B 419 ? 0.2265 0.2951 0.3078 0.0361  -0.0657 0.0786  405 PRO B N   
7105 C CA  . PRO B 419 ? 0.2453 0.3093 0.3358 0.0481  -0.0685 0.0784  405 PRO B CA  
7106 C C   . PRO B 419 ? 0.2137 0.2967 0.3120 0.0542  -0.0710 0.0817  405 PRO B C   
7107 O O   . PRO B 419 ? 0.2155 0.2987 0.3232 0.0654  -0.0717 0.0793  405 PRO B O   
7108 C CB  . PRO B 419 ? 0.2368 0.2817 0.3264 0.0490  -0.0739 0.0866  405 PRO B CB  
7109 C CG  . PRO B 419 ? 0.2778 0.3210 0.3577 0.0365  -0.0732 0.0911  405 PRO B CG  
7110 C CD  . PRO B 419 ? 0.2461 0.3087 0.3221 0.0302  -0.0692 0.0879  405 PRO B CD  
7111 N N   . LEU B 420 ? 0.2008 0.3003 0.2960 0.0475  -0.0725 0.0871  406 LEU B N   
7112 C CA  . LEU B 420 ? 0.2008 0.3212 0.3043 0.0524  -0.0755 0.0906  406 LEU B CA  
7113 C C   . LEU B 420 ? 0.1883 0.3257 0.2947 0.0518  -0.0704 0.0820  406 LEU B C   
7114 O O   . LEU B 420 ? 0.1894 0.3374 0.3066 0.0612  -0.0701 0.0796  406 LEU B O   
7115 C CB  . LEU B 420 ? 0.2031 0.3347 0.3012 0.0447  -0.0803 0.1003  406 LEU B CB  
7116 C CG  . LEU B 420 ? 0.2019 0.3589 0.3073 0.0469  -0.0839 0.1042  406 LEU B CG  
7117 C CD1 . LEU B 420 ? 0.2107 0.3716 0.3318 0.0620  -0.0877 0.1073  406 LEU B CD1 
7118 C CD2 . LEU B 420 ? 0.2066 0.3729 0.3040 0.0378  -0.0890 0.1137  406 LEU B CD2 
7119 N N   . TRP B 421 ? 0.1802 0.3206 0.2774 0.0410  -0.0661 0.0774  407 TRP B N   
7120 C CA  . TRP B 421 ? 0.1869 0.3403 0.2856 0.0393  -0.0613 0.0698  407 TRP B CA  
7121 C C   . TRP B 421 ? 0.1723 0.3156 0.2742 0.0459  -0.0569 0.0617  407 TRP B C   
7122 O O   . TRP B 421 ? 0.1677 0.3229 0.2778 0.0526  -0.0550 0.0578  407 TRP B O   
7123 C CB  . TRP B 421 ? 0.1669 0.3223 0.2546 0.0264  -0.0582 0.0671  407 TRP B CB  
7124 C CG  . TRP B 421 ? 0.1521 0.3222 0.2410 0.0228  -0.0545 0.0612  407 TRP B CG  
7125 C CD1 . TRP B 421 ? 0.1546 0.3192 0.2378 0.0176  -0.0494 0.0545  407 TRP B CD1 
7126 C CD2 . TRP B 421 ? 0.1511 0.3444 0.2479 0.0240  -0.0560 0.0627  407 TRP B CD2 
7127 N NE1 . TRP B 421 ? 0.1477 0.3291 0.2334 0.0145  -0.0476 0.0519  407 TRP B NE1 
7128 C CE2 . TRP B 421 ? 0.1447 0.3448 0.2391 0.0181  -0.0514 0.0566  407 TRP B CE2 
7129 C CE3 . TRP B 421 ? 0.1559 0.3657 0.2619 0.0291  -0.0612 0.0693  407 TRP B CE3 
7130 C CZ2 . TRP B 421 ? 0.1426 0.3662 0.2437 0.0164  -0.0514 0.0565  407 TRP B CZ2 
7131 C CZ3 . TRP B 421 ? 0.1530 0.3872 0.2665 0.0282  -0.0613 0.0691  407 TRP B CZ3 
7132 C CH2 . TRP B 421 ? 0.1462 0.3875 0.2572 0.0214  -0.0562 0.0626  407 TRP B CH2 
7133 N N   . GLY B 422 ? 0.1944 0.3173 0.2899 0.0440  -0.0554 0.0591  408 GLY B N   
7134 C CA  . GLY B 422 ? 0.1723 0.2828 0.2694 0.0502  -0.0525 0.0521  408 GLY B CA  
7135 C C   . GLY B 422 ? 0.1848 0.3010 0.2791 0.0470  -0.0469 0.0438  408 GLY B C   
7136 O O   . GLY B 422 ? 0.1860 0.3030 0.2843 0.0539  -0.0444 0.0378  408 GLY B O   
7137 N N   . SER B 423 ? 0.1730 0.2919 0.2599 0.0369  -0.0448 0.0433  409 SER B N   
7138 C CA  . SER B 423 ? 0.1834 0.3081 0.2671 0.0327  -0.0403 0.0372  409 SER B CA  
7139 C C   . SER B 423 ? 0.1772 0.2850 0.2544 0.0302  -0.0384 0.0332  409 SER B C   
7140 O O   . SER B 423 ? 0.1804 0.2799 0.2519 0.0237  -0.0387 0.0351  409 SER B O   
7141 C CB  . SER B 423 ? 0.1592 0.2955 0.2389 0.0233  -0.0397 0.0392  409 SER B CB  
7142 O OG  . SER B 423 ? 0.1406 0.2839 0.2179 0.0190  -0.0360 0.0348  409 SER B OG  
7143 N N   . ILE B 424 ? 0.1812 0.2854 0.2590 0.0349  -0.0363 0.0274  410 ILE B N   
7144 C CA  . ILE B 424 ? 0.1603 0.2500 0.2317 0.0317  -0.0354 0.0241  410 ILE B CA  
7145 C C   . ILE B 424 ? 0.1759 0.2703 0.2416 0.0231  -0.0331 0.0236  410 ILE B C   
7146 O O   . ILE B 424 ? 0.1813 0.2896 0.2473 0.0206  -0.0311 0.0232  410 ILE B O   
7147 C CB  . ILE B 424 ? 0.1882 0.2720 0.2597 0.0378  -0.0341 0.0173  410 ILE B CB  
7148 C CG1 . ILE B 424 ? 0.1720 0.2717 0.2442 0.0394  -0.0299 0.0123  410 ILE B CG1 
7149 C CG2 . ILE B 424 ? 0.2084 0.2838 0.2856 0.0469  -0.0367 0.0177  410 ILE B CG2 
7150 C CD1 . ILE B 424 ? 0.1970 0.2903 0.2651 0.0426  -0.0276 0.0045  410 ILE B CD1 
7151 N N   . GLY B 425 ? 0.1789 0.2616 0.2400 0.0186  -0.0336 0.0242  411 GLY B N   
7152 C CA  . GLY B 425 ? 0.1845 0.2679 0.2411 0.0113  -0.0323 0.0251  411 GLY B CA  
7153 C C   . GLY B 425 ? 0.1618 0.2436 0.2178 0.0074  -0.0331 0.0294  411 GLY B C   
7154 O O   . GLY B 425 ? 0.1582 0.2352 0.2110 0.0029  -0.0322 0.0298  411 GLY B O   
7155 N N   . TYR B 426 ? 0.1805 0.2663 0.2394 0.0095  -0.0348 0.0325  412 TYR B N   
7156 C CA  . TYR B 426 ? 0.1860 0.2714 0.2428 0.0054  -0.0353 0.0363  412 TYR B CA  
7157 C C   . TYR B 426 ? 0.1751 0.2493 0.2301 0.0032  -0.0351 0.0371  412 TYR B C   
7158 O O   . TYR B 426 ? 0.1759 0.2494 0.2278 -0.0014 -0.0333 0.0373  412 TYR B O   
7159 C CB  . TYR B 426 ? 0.1766 0.2667 0.2367 0.0085  -0.0383 0.0406  412 TYR B CB  
7160 C CG  . TYR B 426 ? 0.1902 0.2789 0.2466 0.0040  -0.0391 0.0449  412 TYR B CG  
7161 C CD1 . TYR B 426 ? 0.1876 0.2843 0.2396 -0.0017 -0.0381 0.0452  412 TYR B CD1 
7162 C CD2 . TYR B 426 ? 0.1756 0.2549 0.2322 0.0046  -0.0407 0.0484  412 TYR B CD2 
7163 C CE1 . TYR B 426 ? 0.1638 0.2600 0.2110 -0.0061 -0.0381 0.0481  412 TYR B CE1 
7164 C CE2 . TYR B 426 ? 0.1970 0.2769 0.2496 0.0000  -0.0407 0.0523  412 TYR B CE2 
7165 C CZ  . TYR B 426 ? 0.1966 0.2851 0.2442 -0.0051 -0.0391 0.0518  412 TYR B CZ  
7166 O OH  . TYR B 426 ? 0.1870 0.2766 0.2293 -0.0099 -0.0386 0.0549  412 TYR B OH  
7167 N N   . THR B 427 ? 0.1910 0.2566 0.2482 0.0063  -0.0367 0.0372  413 THR B N   
7168 C CA  . THR B 427 ? 0.1808 0.2383 0.2378 0.0038  -0.0372 0.0394  413 THR B CA  
7169 C C   . THR B 427 ? 0.1675 0.2237 0.2231 0.0003  -0.0349 0.0374  413 THR B C   
7170 O O   . THR B 427 ? 0.1817 0.2379 0.2370 -0.0027 -0.0334 0.0391  413 THR B O   
7171 C CB  . THR B 427 ? 0.2112 0.2590 0.2704 0.0069  -0.0401 0.0396  413 THR B CB  
7172 O OG1 . THR B 427 ? 0.2063 0.2539 0.2675 0.0108  -0.0425 0.0427  413 THR B OG1 
7173 C CG2 . THR B 427 ? 0.1804 0.2213 0.2400 0.0030  -0.0408 0.0421  413 THR B CG2 
7174 N N   . LEU B 428 ? 0.1664 0.2220 0.2213 0.0009  -0.0345 0.0340  414 LEU B N   
7175 C CA  . LEU B 428 ? 0.1906 0.2443 0.2450 -0.0017 -0.0333 0.0334  414 LEU B CA  
7176 C C   . LEU B 428 ? 0.1681 0.2251 0.2207 -0.0044 -0.0305 0.0336  414 LEU B C   
7177 O O   . LEU B 428 ? 0.1630 0.2181 0.2170 -0.0056 -0.0291 0.0343  414 LEU B O   
7178 C CB  . LEU B 428 ? 0.1667 0.2200 0.2192 -0.0013 -0.0339 0.0306  414 LEU B CB  
7179 C CG  . LEU B 428 ? 0.1949 0.2461 0.2470 -0.0036 -0.0338 0.0311  414 LEU B CG  
7180 C CD1 . LEU B 428 ? 0.1548 0.2023 0.2110 -0.0040 -0.0356 0.0329  414 LEU B CD1 
7181 C CD2 . LEU B 428 ? 0.1777 0.2302 0.2260 -0.0041 -0.0345 0.0291  414 LEU B CD2 
7182 N N   . ALA B 429 ? 0.1853 0.2475 0.2351 -0.0052 -0.0297 0.0326  415 ALA B N   
7183 C CA  . ALA B 429 ? 0.1762 0.2396 0.2227 -0.0087 -0.0273 0.0319  415 ALA B CA  
7184 C C   . ALA B 429 ? 0.1656 0.2305 0.2111 -0.0099 -0.0262 0.0333  415 ALA B C   
7185 O O   . ALA B 429 ? 0.1945 0.2574 0.2379 -0.0121 -0.0235 0.0319  415 ALA B O   
7186 C CB  . ALA B 429 ? 0.1636 0.2330 0.2070 -0.0108 -0.0272 0.0307  415 ALA B CB  
7187 N N   . ALA B 430 ? 0.1762 0.2445 0.2230 -0.0086 -0.0282 0.0359  416 ALA B N   
7188 C CA  . ALA B 430 ? 0.1778 0.2481 0.2228 -0.0105 -0.0276 0.0384  416 ALA B CA  
7189 C C   . ALA B 430 ? 0.1817 0.2479 0.2289 -0.0109 -0.0257 0.0391  416 ALA B C   
7190 O O   . ALA B 430 ? 0.1835 0.2521 0.2281 -0.0135 -0.0228 0.0390  416 ALA B O   
7191 C CB  . ALA B 430 ? 0.1620 0.2349 0.2086 -0.0085 -0.0312 0.0427  416 ALA B CB  
7192 N N   . ALA B 431 ? 0.1923 0.2539 0.2443 -0.0087 -0.0271 0.0395  417 ALA B N   
7193 C CA  . ALA B 431 ? 0.1832 0.2435 0.2391 -0.0094 -0.0256 0.0405  417 ALA B CA  
7194 C C   . ALA B 431 ? 0.1728 0.2337 0.2287 -0.0096 -0.0217 0.0373  417 ALA B C   
7195 O O   . ALA B 431 ? 0.1834 0.2472 0.2415 -0.0102 -0.0186 0.0376  417 ALA B O   
7196 C CB  . ALA B 431 ? 0.1667 0.2225 0.2272 -0.0079 -0.0287 0.0411  417 ALA B CB  
7197 N N   . PHE B 432 ? 0.1787 0.2369 0.2325 -0.0089 -0.0216 0.0345  418 PHE B N   
7198 C CA  . PHE B 432 ? 0.1950 0.2505 0.2483 -0.0086 -0.0183 0.0315  418 PHE B CA  
7199 C C   . PHE B 432 ? 0.1886 0.2464 0.2366 -0.0109 -0.0144 0.0291  418 PHE B C   
7200 O O   . PHE B 432 ? 0.2089 0.2662 0.2583 -0.0100 -0.0104 0.0268  418 PHE B O   
7201 C CB  . PHE B 432 ? 0.1907 0.2415 0.2414 -0.0088 -0.0196 0.0299  418 PHE B CB  
7202 C CG  . PHE B 432 ? 0.2196 0.2645 0.2684 -0.0089 -0.0167 0.0270  418 PHE B CG  
7203 C CD1 . PHE B 432 ? 0.2048 0.2466 0.2596 -0.0054 -0.0153 0.0270  418 PHE B CD1 
7204 C CD2 . PHE B 432 ? 0.2000 0.2421 0.2415 -0.0125 -0.0157 0.0241  418 PHE B CD2 
7205 C CE1 . PHE B 432 ? 0.2051 0.2392 0.2588 -0.0043 -0.0126 0.0241  418 PHE B CE1 
7206 C CE2 . PHE B 432 ? 0.2076 0.2411 0.2466 -0.0128 -0.0132 0.0209  418 PHE B CE2 
7207 C CZ  . PHE B 432 ? 0.2192 0.2476 0.2643 -0.0081 -0.0115 0.0207  418 PHE B CZ  
7208 N N   . GLY B 433 ? 0.1872 0.2482 0.2292 -0.0139 -0.0155 0.0293  419 GLY B N   
7209 C CA  . GLY B 433 ? 0.1856 0.2498 0.2209 -0.0172 -0.0125 0.0271  419 GLY B CA  
7210 C C   . GLY B 433 ? 0.1874 0.2569 0.2239 -0.0176 -0.0102 0.0293  419 GLY B C   
7211 O O   . GLY B 433 ? 0.1992 0.2706 0.2322 -0.0190 -0.0055 0.0260  419 GLY B O   
7212 N N   . ALA B 434 ? 0.1792 0.2512 0.2204 -0.0168 -0.0134 0.0347  420 ALA B N   
7213 C CA  . ALA B 434 ? 0.1998 0.2772 0.2420 -0.0187 -0.0117 0.0381  420 ALA B CA  
7214 C C   . ALA B 434 ? 0.2219 0.3009 0.2703 -0.0169 -0.0072 0.0361  420 ALA B C   
7215 O O   . ALA B 434 ? 0.2233 0.3088 0.2700 -0.0187 -0.0024 0.0354  420 ALA B O   
7216 C CB  . ALA B 434 ? 0.1989 0.2754 0.2447 -0.0187 -0.0167 0.0445  420 ALA B CB  
7217 N N   . GLN B 435 ? 0.2189 0.2936 0.2748 -0.0132 -0.0086 0.0355  421 GLN B N   
7218 C CA  . GLN B 435 ? 0.1944 0.2721 0.2582 -0.0105 -0.0050 0.0342  421 GLN B CA  
7219 C C   . GLN B 435 ? 0.2197 0.2965 0.2804 -0.0086 0.0010  0.0278  421 GLN B C   
7220 O O   . GLN B 435 ? 0.2472 0.3301 0.3125 -0.0068 0.0062  0.0260  421 GLN B O   
7221 C CB  . GLN B 435 ? 0.2090 0.2824 0.2804 -0.0073 -0.0089 0.0355  421 GLN B CB  
7222 C CG  . GLN B 435 ? 0.2106 0.2897 0.2927 -0.0043 -0.0066 0.0360  421 GLN B CG  
7223 C CD  . GLN B 435 ? 0.2332 0.3215 0.3213 -0.0075 -0.0072 0.0409  421 GLN B CD  
7224 O OE1 . GLN B 435 ? 0.2378 0.3339 0.3248 -0.0101 -0.0030 0.0415  421 GLN B OE1 
7225 N NE2 . GLN B 435 ? 0.2058 0.2932 0.2994 -0.0083 -0.0125 0.0445  421 GLN B NE2 
7226 N N   . THR B 436 ? 0.2077 0.2766 0.2610 -0.0090 0.0004  0.0240  422 THR B N   
7227 C CA  . THR B 436 ? 0.2195 0.2846 0.2677 -0.0082 0.0057  0.0171  422 THR B CA  
7228 C C   . THR B 436 ? 0.2439 0.3174 0.2856 -0.0116 0.0107  0.0150  422 THR B C   
7229 O O   . THR B 436 ? 0.2542 0.3302 0.2971 -0.0093 0.0172  0.0102  422 THR B O   
7230 C CB  . THR B 436 ? 0.2163 0.2721 0.2562 -0.0106 0.0032  0.0143  422 THR B CB  
7231 O OG1 . THR B 436 ? 0.2013 0.2511 0.2463 -0.0083 -0.0013 0.0170  422 THR B OG1 
7232 C CG2 . THR B 436 ? 0.2204 0.2684 0.2541 -0.0105 0.0081  0.0066  422 THR B CG2 
7233 N N   . ALA B 437 ? 0.2138 0.2926 0.2492 -0.0169 0.0078  0.0191  423 ALA B N   
7234 C CA  . ALA B 437 ? 0.2487 0.3366 0.2765 -0.0214 0.0118  0.0187  423 ALA B CA  
7235 C C   . ALA B 437 ? 0.2548 0.3526 0.2899 -0.0203 0.0161  0.0209  423 ALA B C   
7236 O O   . ALA B 437 ? 0.2614 0.3664 0.2920 -0.0217 0.0228  0.0169  423 ALA B O   
7237 C CB  . ALA B 437 ? 0.2146 0.3062 0.2357 -0.0267 0.0063  0.0249  423 ALA B CB  
7238 N N   . CYS B 438 ? 0.2435 0.3429 0.2895 -0.0185 0.0126  0.0270  424 CYS B N   
7239 C CA  . CYS B 438 ? 0.2466 0.3574 0.3001 -0.0195 0.0154  0.0311  424 CYS B CA  
7240 C C   . CYS B 438 ? 0.2721 0.3830 0.3401 -0.0141 0.0147  0.0316  424 CYS B C   
7241 O O   . CYS B 438 ? 0.2360 0.3471 0.3107 -0.0153 0.0095  0.0377  424 CYS B O   
7242 C CB  . CYS B 438 ? 0.2454 0.3590 0.2968 -0.0254 0.0101  0.0400  424 CYS B CB  
7243 S SG  . CYS B 438 ? 0.2644 0.3785 0.2999 -0.0317 0.0083  0.0422  424 CYS B SG  
7244 N N   . PRO B 439 ? 0.2499 0.3601 0.3227 -0.0081 0.0196  0.0253  425 PRO B N   
7245 C CA  . PRO B 439 ? 0.2934 0.4043 0.3804 -0.0024 0.0181  0.0267  425 PRO B CA  
7246 C C   . PRO B 439 ? 0.2958 0.4214 0.3941 -0.0043 0.0184  0.0326  425 PRO B C   
7247 O O   . PRO B 439 ? 0.3012 0.4276 0.4100 -0.0024 0.0138  0.0363  425 PRO B O   
7248 C CB  . PRO B 439 ? 0.2703 0.3786 0.3598 0.0047  0.0244  0.0188  425 PRO B CB  
7249 C CG  . PRO B 439 ? 0.2684 0.3793 0.3461 0.0018  0.0311  0.0130  425 PRO B CG  
7250 C CD  . PRO B 439 ? 0.2760 0.3839 0.3414 -0.0060 0.0264  0.0166  425 PRO B CD  
7251 N N   . ASN B 440 ? 0.2766 0.4148 0.3728 -0.0089 0.0234  0.0338  426 ASN B N   
7252 C CA  . ASN B 440 ? 0.2836 0.4376 0.3908 -0.0119 0.0243  0.0395  426 ASN B CA  
7253 C C   . ASN B 440 ? 0.2608 0.4138 0.3647 -0.0205 0.0179  0.0481  426 ASN B C   
7254 O O   . ASN B 440 ? 0.2993 0.4648 0.4108 -0.0253 0.0182  0.0537  426 ASN B O   
7255 C CB  . ASN B 440 ? 0.3027 0.4735 0.4109 -0.0120 0.0345  0.0361  426 ASN B CB  
7256 C CG  . ASN B 440 ? 0.3278 0.4984 0.4407 -0.0021 0.0413  0.0269  426 ASN B CG  
7257 O OD1 . ASN B 440 ? 0.3155 0.4791 0.4374 0.0049  0.0381  0.0259  426 ASN B OD1 
7258 N ND2 . ASN B 440 ? 0.3700 0.5474 0.4763 -0.0015 0.0504  0.0202  426 ASN B ND2 
7259 N N   . ARG B 441 ? 0.2356 0.3745 0.3289 -0.0228 0.0122  0.0493  427 ARG B N   
7260 C CA  . ARG B 441 ? 0.2491 0.3835 0.3399 -0.0294 0.0054  0.0570  427 ARG B CA  
7261 C C   . ARG B 441 ? 0.2549 0.3779 0.3504 -0.0270 -0.0021 0.0579  427 ARG B C   
7262 O O   . ARG B 441 ? 0.2078 0.3236 0.3036 -0.0210 -0.0030 0.0531  427 ARG B O   
7263 C CB  . ARG B 441 ? 0.2524 0.3800 0.3292 -0.0330 0.0038  0.0585  427 ARG B CB  
7264 C CG  . ARG B 441 ? 0.2689 0.4089 0.3393 -0.0376 0.0104  0.0592  427 ARG B CG  
7265 C CD  . ARG B 441 ? 0.2671 0.4016 0.3236 -0.0416 0.0077  0.0619  427 ARG B CD  
7266 N NE  . ARG B 441 ? 0.2642 0.3910 0.3199 -0.0460 -0.0001 0.0707  427 ARG B NE  
7267 C CZ  . ARG B 441 ? 0.2887 0.4123 0.3345 -0.0501 -0.0036 0.0762  427 ARG B CZ  
7268 N NH1 . ARG B 441 ? 0.2930 0.4217 0.3281 -0.0515 -0.0004 0.0738  427 ARG B NH1 
7269 N NH2 . ARG B 441 ? 0.2816 0.3961 0.3281 -0.0528 -0.0109 0.0842  427 ARG B NH2 
7270 N N   . ARG B 442 ? 0.2314 0.3530 0.3300 -0.0324 -0.0074 0.0641  428 ARG B N   
7271 C CA  . ARG B 442 ? 0.2205 0.3317 0.3222 -0.0315 -0.0146 0.0647  428 ARG B CA  
7272 C C   . ARG B 442 ? 0.2182 0.3139 0.3098 -0.0302 -0.0191 0.0638  428 ARG B C   
7273 O O   . ARG B 442 ? 0.2368 0.3285 0.3217 -0.0338 -0.0205 0.0675  428 ARG B O   
7274 C CB  . ARG B 442 ? 0.2167 0.3310 0.3245 -0.0387 -0.0186 0.0710  428 ARG B CB  
7275 C CG  . ARG B 442 ? 0.2127 0.3171 0.3230 -0.0386 -0.0259 0.0706  428 ARG B CG  
7276 C CD  . ARG B 442 ? 0.2478 0.3572 0.3651 -0.0468 -0.0296 0.0761  428 ARG B CD  
7277 N NE  . ARG B 442 ? 0.2253 0.3262 0.3363 -0.0542 -0.0326 0.0814  428 ARG B NE  
7278 C CZ  . ARG B 442 ? 0.2639 0.3612 0.3773 -0.0625 -0.0378 0.0861  428 ARG B CZ  
7279 N NH1 . ARG B 442 ? 0.2470 0.3511 0.3692 -0.0653 -0.0407 0.0861  428 ARG B NH1 
7280 N NH2 . ARG B 442 ? 0.2683 0.3543 0.3749 -0.0685 -0.0408 0.0912  428 ARG B NH2 
7281 N N   . VAL B 443 ? 0.2096 0.2976 0.3004 -0.0250 -0.0213 0.0593  429 VAL B N   
7282 C CA  . VAL B 443 ? 0.2338 0.3100 0.3166 -0.0227 -0.0247 0.0576  429 VAL B CA  
7283 C C   . VAL B 443 ? 0.2538 0.3209 0.3381 -0.0231 -0.0309 0.0579  429 VAL B C   
7284 O O   . VAL B 443 ? 0.2275 0.2956 0.3165 -0.0217 -0.0323 0.0560  429 VAL B O   
7285 C CB  . VAL B 443 ? 0.2507 0.3259 0.3303 -0.0175 -0.0219 0.0519  429 VAL B CB  
7286 C CG1 . VAL B 443 ? 0.2086 0.2744 0.2825 -0.0152 -0.0258 0.0500  429 VAL B CG1 
7287 C CG2 . VAL B 443 ? 0.2289 0.3104 0.3039 -0.0181 -0.0163 0.0506  429 VAL B CG2 
7288 N N   . ILE B 444 ? 0.2360 0.2939 0.3159 -0.0249 -0.0349 0.0603  430 ILE B N   
7289 C CA  . ILE B 444 ? 0.2462 0.2928 0.3252 -0.0247 -0.0404 0.0591  430 ILE B CA  
7290 C C   . ILE B 444 ? 0.2514 0.2907 0.3245 -0.0193 -0.0413 0.0555  430 ILE B C   
7291 O O   . ILE B 444 ? 0.2370 0.2750 0.3065 -0.0181 -0.0411 0.0575  430 ILE B O   
7292 C CB  . ILE B 444 ? 0.2541 0.2934 0.3333 -0.0305 -0.0444 0.0641  430 ILE B CB  
7293 C CG1 . ILE B 444 ? 0.2543 0.3026 0.3404 -0.0373 -0.0439 0.0681  430 ILE B CG1 
7294 C CG2 . ILE B 444 ? 0.2366 0.2613 0.3130 -0.0296 -0.0498 0.0611  430 ILE B CG2 
7295 C CD1 . ILE B 444 ? 0.2769 0.3325 0.3632 -0.0423 -0.0411 0.0743  430 ILE B CD1 
7296 N N   . VAL B 445 ? 0.2383 0.2748 0.3107 -0.0162 -0.0426 0.0506  431 VAL B N   
7297 C CA  . VAL B 445 ? 0.2485 0.2813 0.3162 -0.0112 -0.0427 0.0467  431 VAL B CA  
7298 C C   . VAL B 445 ? 0.2348 0.2566 0.3006 -0.0101 -0.0468 0.0442  431 VAL B C   
7299 O O   . VAL B 445 ? 0.2292 0.2485 0.2950 -0.0119 -0.0488 0.0417  431 VAL B O   
7300 C CB  . VAL B 445 ? 0.2324 0.2709 0.2995 -0.0089 -0.0403 0.0430  431 VAL B CB  
7301 C CG1 . VAL B 445 ? 0.2325 0.2706 0.2953 -0.0049 -0.0397 0.0398  431 VAL B CG1 
7302 C CG2 . VAL B 445 ? 0.2301 0.2769 0.2996 -0.0099 -0.0362 0.0445  431 VAL B CG2 
7303 N N   . LEU B 446 ? 0.2245 0.2396 0.2882 -0.0069 -0.0483 0.0446  432 LEU B N   
7304 C CA  . LEU B 446 ? 0.2356 0.2386 0.2971 -0.0042 -0.0515 0.0408  432 LEU B CA  
7305 C C   . LEU B 446 ? 0.2620 0.2680 0.3215 0.0026  -0.0497 0.0357  432 LEU B C   
7306 O O   . LEU B 446 ? 0.2134 0.2212 0.2738 0.0070  -0.0493 0.0374  432 LEU B O   
7307 C CB  . LEU B 446 ? 0.2409 0.2325 0.3028 -0.0049 -0.0548 0.0453  432 LEU B CB  
7308 C CG  . LEU B 446 ? 0.2623 0.2520 0.3261 -0.0132 -0.0566 0.0506  432 LEU B CG  
7309 C CD1 . LEU B 446 ? 0.2606 0.2448 0.3246 -0.0153 -0.0585 0.0585  432 LEU B CD1 
7310 C CD2 . LEU B 446 ? 0.2496 0.2286 0.3121 -0.0168 -0.0601 0.0469  432 LEU B CD2 
7311 N N   . THR B 447 ? 0.2379 0.2456 0.2948 0.0033  -0.0489 0.0300  433 THR B N   
7312 C CA  . THR B 447 ? 0.2331 0.2464 0.2883 0.0088  -0.0466 0.0255  433 THR B CA  
7313 C C   . THR B 447 ? 0.2507 0.2573 0.3018 0.0111  -0.0474 0.0183  433 THR B C   
7314 O O   . THR B 447 ? 0.2545 0.2565 0.3025 0.0067  -0.0492 0.0162  433 THR B O   
7315 C CB  . THR B 447 ? 0.2275 0.2533 0.2821 0.0069  -0.0434 0.0258  433 THR B CB  
7316 O OG1 . THR B 447 ? 0.2088 0.2412 0.2617 0.0109  -0.0412 0.0218  433 THR B OG1 
7317 C CG2 . THR B 447 ? 0.1978 0.2238 0.2508 0.0021  -0.0441 0.0253  433 THR B CG2 
7318 N N   . GLY B 448 ? 0.2803 0.2879 0.3314 0.0179  -0.0458 0.0141  434 GLY B N   
7319 C CA  . GLY B 448 ? 0.2693 0.2734 0.3155 0.0206  -0.0450 0.0058  434 GLY B CA  
7320 C C   . GLY B 448 ? 0.2590 0.2743 0.3006 0.0170  -0.0427 0.0035  434 GLY B C   
7321 O O   . GLY B 448 ? 0.2452 0.2710 0.2884 0.0142  -0.0412 0.0079  434 GLY B O   
7322 N N   . ASP B 449 ? 0.2882 0.3001 0.3231 0.0165  -0.0425 -0.0035 435 ASP B N   
7323 C CA  . ASP B 449 ? 0.2845 0.3074 0.3139 0.0127  -0.0406 -0.0049 435 ASP B CA  
7324 C C   . ASP B 449 ? 0.2639 0.3013 0.2951 0.0165  -0.0360 -0.0054 435 ASP B C   
7325 O O   . ASP B 449 ? 0.2419 0.2894 0.2721 0.0124  -0.0347 -0.0018 435 ASP B O   
7326 C CB  . ASP B 449 ? 0.2967 0.3141 0.3169 0.0107  -0.0416 -0.0124 435 ASP B CB  
7327 C CG  . ASP B 449 ? 0.3561 0.3667 0.3744 0.0180  -0.0395 -0.0213 435 ASP B CG  
7328 O OD1 . ASP B 449 ? 0.3545 0.3570 0.3792 0.0237  -0.0401 -0.0204 435 ASP B OD1 
7329 O OD2 . ASP B 449 ? 0.3697 0.3825 0.3797 0.0183  -0.0373 -0.0291 435 ASP B OD2 
7330 N N   . GLY B 450 ? 0.2645 0.3029 0.2990 0.0242  -0.0338 -0.0094 436 GLY B N   
7331 C CA  . GLY B 450 ? 0.2498 0.3047 0.2875 0.0275  -0.0295 -0.0095 436 GLY B CA  
7332 C C   . GLY B 450 ? 0.2437 0.3059 0.2872 0.0250  -0.0300 -0.0014 436 GLY B C   
7333 O O   . GLY B 450 ? 0.2285 0.3034 0.2712 0.0214  -0.0277 0.0006  436 GLY B O   
7334 N N   . ALA B 451 ? 0.2361 0.2902 0.2846 0.0262  -0.0329 0.0032  437 ALA B N   
7335 C CA  . ALA B 451 ? 0.2248 0.2855 0.2773 0.0236  -0.0332 0.0100  437 ALA B CA  
7336 C C   . ALA B 451 ? 0.2126 0.2757 0.2612 0.0158  -0.0329 0.0130  437 ALA B C   
7337 O O   . ALA B 451 ? 0.1774 0.2505 0.2263 0.0130  -0.0312 0.0152  437 ALA B O   
7338 C CB  . ALA B 451 ? 0.2218 0.2727 0.2783 0.0249  -0.0365 0.0146  437 ALA B CB  
7339 N N   . ALA B 452 ? 0.2082 0.2621 0.2534 0.0121  -0.0349 0.0130  438 ALA B N   
7340 C CA  . ALA B 452 ? 0.2066 0.2618 0.2499 0.0061  -0.0351 0.0166  438 ALA B CA  
7341 C C   . ALA B 452 ? 0.2117 0.2758 0.2506 0.0033  -0.0329 0.0157  438 ALA B C   
7342 O O   . ALA B 452 ? 0.1855 0.2508 0.2236 -0.0009 -0.0328 0.0193  438 ALA B O   
7343 C CB  . ALA B 452 ? 0.1893 0.2358 0.2314 0.0031  -0.0381 0.0173  438 ALA B CB  
7344 N N   . GLN B 453 ? 0.2100 0.2798 0.2458 0.0054  -0.0310 0.0109  439 GLN B N   
7345 C CA  . GLN B 453 ? 0.2196 0.2991 0.2503 0.0015  -0.0288 0.0108  439 GLN B CA  
7346 C C   . GLN B 453 ? 0.2015 0.2904 0.2352 -0.0005 -0.0268 0.0141  439 GLN B C   
7347 O O   . GLN B 453 ? 0.1682 0.2613 0.1981 -0.0062 -0.0261 0.0168  439 GLN B O   
7348 C CB  . GLN B 453 ? 0.2097 0.2958 0.2365 0.0042  -0.0262 0.0044  439 GLN B CB  
7349 C CG  . GLN B 453 ? 0.2193 0.2962 0.2403 0.0045  -0.0282 0.0000  439 GLN B CG  
7350 C CD  . GLN B 453 ? 0.2710 0.3555 0.2854 0.0059  -0.0248 -0.0072 439 GLN B CD  
7351 O OE1 . GLN B 453 ? 0.3220 0.4177 0.3395 0.0103  -0.0206 -0.0103 439 GLN B OE1 
7352 N NE2 . GLN B 453 ? 0.2690 0.3490 0.2745 0.0024  -0.0265 -0.0100 439 GLN B NE2 
7353 N N   . LEU B 454 ? 0.1684 0.2603 0.2083 0.0035  -0.0264 0.0144  440 LEU B N   
7354 C CA  . LEU B 454 ? 0.1791 0.2820 0.2214 0.0011  -0.0249 0.0168  440 LEU B CA  
7355 C C   . LEU B 454 ? 0.1481 0.2453 0.1888 -0.0049 -0.0260 0.0212  440 LEU B C   
7356 O O   . LEU B 454 ? 0.1661 0.2702 0.2057 -0.0097 -0.0250 0.0230  440 LEU B O   
7357 C CB  . LEU B 454 ? 0.1659 0.2749 0.2155 0.0071  -0.0250 0.0165  440 LEU B CB  
7358 C CG  . LEU B 454 ? 0.1662 0.2862 0.2195 0.0136  -0.0227 0.0120  440 LEU B CG  
7359 C CD1 . LEU B 454 ? 0.1655 0.2740 0.2182 0.0201  -0.0235 0.0075  440 LEU B CD1 
7360 C CD2 . LEU B 454 ? 0.1434 0.2763 0.2051 0.0177  -0.0229 0.0139  440 LEU B CD2 
7361 N N   . THR B 455 ? 0.1863 0.2713 0.2270 -0.0047 -0.0280 0.0227  441 THR B N   
7362 C CA  . THR B 455 ? 0.1674 0.2468 0.2075 -0.0086 -0.0283 0.0258  441 THR B CA  
7363 C C   . THR B 455 ? 0.1944 0.2637 0.2329 -0.0099 -0.0298 0.0272  441 THR B C   
7364 O O   . THR B 455 ? 0.1846 0.2477 0.2247 -0.0105 -0.0299 0.0290  441 THR B O   
7365 C CB  . THR B 455 ? 0.1742 0.2524 0.2181 -0.0064 -0.0288 0.0268  441 THR B CB  
7366 O OG1 . THR B 455 ? 0.1564 0.2286 0.2031 -0.0021 -0.0304 0.0265  441 THR B OG1 
7367 C CG2 . THR B 455 ? 0.1636 0.2533 0.2097 -0.0054 -0.0283 0.0265  441 THR B CG2 
7368 N N   . ILE B 456 ? 0.1916 0.2605 0.2270 -0.0102 -0.0307 0.0265  442 ILE B N   
7369 C CA  . ILE B 456 ? 0.1946 0.2560 0.2299 -0.0108 -0.0332 0.0284  442 ILE B CA  
7370 C C   . ILE B 456 ? 0.1838 0.2400 0.2192 -0.0135 -0.0334 0.0322  442 ILE B C   
7371 O O   . ILE B 456 ? 0.1841 0.2347 0.2231 -0.0123 -0.0349 0.0342  442 ILE B O   
7372 C CB  . ILE B 456 ? 0.2019 0.2654 0.2318 -0.0120 -0.0345 0.0272  442 ILE B CB  
7373 C CG1 . ILE B 456 ? 0.2028 0.2601 0.2335 -0.0124 -0.0381 0.0291  442 ILE B CG1 
7374 C CG2 . ILE B 456 ? 0.1855 0.2535 0.2096 -0.0168 -0.0336 0.0292  442 ILE B CG2 
7375 C CD1 . ILE B 456 ? 0.1824 0.2354 0.2188 -0.0093 -0.0393 0.0280  442 ILE B CD1 
7376 N N   . GLN B 457 ? 0.1951 0.2527 0.2271 -0.0172 -0.0319 0.0331  443 GLN B N   
7377 C CA  . GLN B 457 ? 0.1891 0.2386 0.2203 -0.0196 -0.0324 0.0364  443 GLN B CA  
7378 C C   . GLN B 457 ? 0.2149 0.2584 0.2509 -0.0170 -0.0312 0.0358  443 GLN B C   
7379 O O   . GLN B 457 ? 0.1908 0.2262 0.2282 -0.0167 -0.0316 0.0378  443 GLN B O   
7380 C CB  . GLN B 457 ? 0.2101 0.2611 0.2358 -0.0255 -0.0313 0.0374  443 GLN B CB  
7381 C CG  . GLN B 457 ? 0.2031 0.2617 0.2289 -0.0270 -0.0288 0.0346  443 GLN B CG  
7382 C CD  . GLN B 457 ? 0.1854 0.2575 0.2106 -0.0269 -0.0279 0.0328  443 GLN B CD  
7383 O OE1 . GLN B 457 ? 0.1673 0.2447 0.1964 -0.0219 -0.0275 0.0301  443 GLN B OE1 
7384 N NE2 . GLN B 457 ? 0.1706 0.2481 0.1909 -0.0322 -0.0275 0.0344  443 GLN B NE2 
7385 N N   . GLU B 458 ? 0.1642 0.2117 0.2029 -0.0149 -0.0297 0.0333  444 GLU B N   
7386 C CA  . GLU B 458 ? 0.1985 0.2422 0.2409 -0.0129 -0.0281 0.0326  444 GLU B CA  
7387 C C   . GLU B 458 ? 0.2004 0.2422 0.2487 -0.0093 -0.0294 0.0342  444 GLU B C   
7388 O O   . GLU B 458 ? 0.2026 0.2422 0.2549 -0.0075 -0.0277 0.0340  444 GLU B O   
7389 C CB  . GLU B 458 ? 0.1973 0.2466 0.2397 -0.0127 -0.0266 0.0307  444 GLU B CB  
7390 C CG  . GLU B 458 ? 0.1983 0.2447 0.2384 -0.0147 -0.0240 0.0291  444 GLU B CG  
7391 C CD  . GLU B 458 ? 0.2161 0.2578 0.2510 -0.0192 -0.0237 0.0285  444 GLU B CD  
7392 O OE1 . GLU B 458 ? 0.2018 0.2479 0.2342 -0.0220 -0.0249 0.0294  444 GLU B OE1 
7393 O OE2 . GLU B 458 ? 0.2429 0.2760 0.2761 -0.0200 -0.0220 0.0271  444 GLU B OE2 
7394 N N   . LEU B 459 ? 0.1929 0.2367 0.2420 -0.0088 -0.0323 0.0353  445 LEU B N   
7395 C CA  . LEU B 459 ? 0.2043 0.2471 0.2591 -0.0068 -0.0344 0.0375  445 LEU B CA  
7396 C C   . LEU B 459 ? 0.2180 0.2562 0.2754 -0.0059 -0.0346 0.0401  445 LEU B C   
7397 O O   . LEU B 459 ? 0.2297 0.2680 0.2944 -0.0030 -0.0343 0.0414  445 LEU B O   
7398 C CB  . LEU B 459 ? 0.1911 0.2361 0.2441 -0.0077 -0.0380 0.0378  445 LEU B CB  
7399 C CG  . LEU B 459 ? 0.2412 0.2868 0.2990 -0.0074 -0.0416 0.0407  445 LEU B CG  
7400 C CD1 . LEU B 459 ? 0.1944 0.2419 0.2607 -0.0057 -0.0407 0.0415  445 LEU B CD1 
7401 C CD2 . LEU B 459 ? 0.2221 0.2691 0.2753 -0.0095 -0.0450 0.0393  445 LEU B CD2 
7402 N N   . GLY B 460 ? 0.2151 0.2491 0.2668 -0.0082 -0.0350 0.0411  446 GLY B N   
7403 C CA  . GLY B 460 ? 0.2174 0.2439 0.2710 -0.0070 -0.0356 0.0440  446 GLY B CA  
7404 C C   . GLY B 460 ? 0.2373 0.2589 0.2943 -0.0043 -0.0315 0.0414  446 GLY B C   
7405 O O   . GLY B 460 ? 0.2223 0.2392 0.2854 -0.0002 -0.0314 0.0429  446 GLY B O   
7406 N N   . SER B 461 ? 0.2165 0.2396 0.2696 -0.0063 -0.0281 0.0372  447 SER B N   
7407 C CA  . SER B 461 ? 0.2332 0.2528 0.2876 -0.0045 -0.0239 0.0336  447 SER B CA  
7408 C C   . SER B 461 ? 0.2255 0.2511 0.2886 0.0001  -0.0223 0.0335  447 SER B C   
7409 O O   . SER B 461 ? 0.2434 0.2659 0.3110 0.0039  -0.0192 0.0318  447 SER B O   
7410 C CB  . SER B 461 ? 0.2108 0.2330 0.2583 -0.0086 -0.0215 0.0298  447 SER B CB  
7411 O OG  . SER B 461 ? 0.2458 0.2644 0.2862 -0.0137 -0.0227 0.0300  447 SER B OG  
7412 N N   . MET B 462 ? 0.2252 0.2593 0.2908 -0.0004 -0.0240 0.0349  448 MET B N   
7413 C CA  . MET B 462 ? 0.2166 0.2572 0.2906 0.0024  -0.0228 0.0357  448 MET B CA  
7414 C C   . MET B 462 ? 0.2264 0.2672 0.3094 0.0065  -0.0244 0.0388  448 MET B C   
7415 O O   . MET B 462 ? 0.2279 0.2728 0.3189 0.0102  -0.0214 0.0383  448 MET B O   
7416 C CB  . MET B 462 ? 0.2071 0.2545 0.2819 0.0002  -0.0251 0.0372  448 MET B CB  
7417 C CG  . MET B 462 ? 0.1899 0.2375 0.2573 -0.0028 -0.0254 0.0357  448 MET B CG  
7418 S SD  . MET B 462 ? 0.2828 0.3328 0.3510 -0.0041 -0.0300 0.0375  448 MET B SD  
7419 C CE  . MET B 462 ? 0.1876 0.2394 0.2523 -0.0053 -0.0287 0.0368  448 MET B CE  
7420 N N   . LEU B 463 ? 0.2211 0.2590 0.3032 0.0060  -0.0293 0.0423  449 LEU B N   
7421 C CA  . LEU B 463 ? 0.2157 0.2547 0.3067 0.0099  -0.0321 0.0465  449 LEU B CA  
7422 C C   . LEU B 463 ? 0.2266 0.2570 0.3203 0.0148  -0.0291 0.0455  449 LEU B C   
7423 O O   . LEU B 463 ? 0.2013 0.2352 0.3060 0.0207  -0.0279 0.0466  449 LEU B O   
7424 C CB  . LEU B 463 ? 0.2207 0.2588 0.3079 0.0071  -0.0383 0.0509  449 LEU B CB  
7425 C CG  . LEU B 463 ? 0.2141 0.2594 0.2990 0.0030  -0.0413 0.0509  449 LEU B CG  
7426 C CD1 . LEU B 463 ? 0.2202 0.2636 0.2966 -0.0008 -0.0459 0.0528  449 LEU B CD1 
7427 C CD2 . LEU B 463 ? 0.2423 0.2972 0.3382 0.0044  -0.0434 0.0535  449 LEU B CD2 
7428 N N   . ARG B 464 ? 0.2263 0.2454 0.3105 0.0124  -0.0279 0.0432  450 ARG B N   
7429 C CA  . ARG B 464 ? 0.2597 0.2671 0.3447 0.0164  -0.0249 0.0411  450 ARG B CA  
7430 C C   . ARG B 464 ? 0.2501 0.2612 0.3411 0.0212  -0.0184 0.0357  450 ARG B C   
7431 O O   . ARG B 464 ? 0.2485 0.2557 0.3474 0.0282  -0.0163 0.0349  450 ARG B O   
7432 C CB  . ARG B 464 ? 0.2606 0.2563 0.3329 0.0107  -0.0243 0.0385  450 ARG B CB  
7433 C CG  . ARG B 464 ? 0.2771 0.2571 0.3478 0.0134  -0.0213 0.0351  450 ARG B CG  
7434 C CD  . ARG B 464 ? 0.2951 0.2672 0.3530 0.0059  -0.0195 0.0307  450 ARG B CD  
7435 N NE  . ARG B 464 ? 0.2522 0.2331 0.3070 0.0038  -0.0151 0.0248  450 ARG B NE  
7436 C CZ  . ARG B 464 ? 0.2554 0.2380 0.3006 -0.0035 -0.0146 0.0222  450 ARG B CZ  
7437 N NH1 . ARG B 464 ? 0.2293 0.2065 0.2671 -0.0098 -0.0177 0.0244  450 ARG B NH1 
7438 N NH2 . ARG B 464 ? 0.2539 0.2454 0.2970 -0.0047 -0.0113 0.0181  450 ARG B NH2 
7439 N N   . ASP B 465 ? 0.2262 0.2451 0.3133 0.0177  -0.0151 0.0320  451 ASP B N   
7440 C CA  . ASP B 465 ? 0.2544 0.2783 0.3443 0.0204  -0.0085 0.0267  451 ASP B CA  
7441 C C   . ASP B 465 ? 0.2414 0.2807 0.3438 0.0237  -0.0077 0.0293  451 ASP B C   
7442 O O   . ASP B 465 ? 0.2448 0.2917 0.3495 0.0249  -0.0019 0.0257  451 ASP B O   
7443 C CB  . ASP B 465 ? 0.2506 0.2758 0.3292 0.0140  -0.0058 0.0225  451 ASP B CB  
7444 C CG  . ASP B 465 ? 0.2760 0.2878 0.3432 0.0103  -0.0054 0.0187  451 ASP B CG  
7445 O OD1 . ASP B 465 ? 0.1955 0.1949 0.2633 0.0132  -0.0057 0.0181  451 ASP B OD1 
7446 O OD2 . ASP B 465 ? 0.2845 0.2983 0.3425 0.0042  -0.0052 0.0168  451 ASP B OD2 
7447 N N   . LYS B 466 ? 0.2443 0.2892 0.3539 0.0242  -0.0134 0.0356  452 LYS B N   
7448 C CA  . LYS B 466 ? 0.2514 0.3116 0.3741 0.0265  -0.0138 0.0390  452 LYS B CA  
7449 C C   . LYS B 466 ? 0.2722 0.3428 0.3929 0.0212  -0.0116 0.0382  452 LYS B C   
7450 O O   . LYS B 466 ? 0.2527 0.3359 0.3822 0.0226  -0.0080 0.0384  452 LYS B O   
7451 C CB  . LYS B 466 ? 0.2594 0.3236 0.3945 0.0353  -0.0091 0.0375  452 LYS B CB  
7452 C CG  . LYS B 466 ? 0.2531 0.3056 0.3923 0.0422  -0.0112 0.0389  452 LYS B CG  
7453 C CD  . LYS B 466 ? 0.3284 0.3814 0.4722 0.0421  -0.0201 0.0473  452 LYS B CD  
7454 C CE  . LYS B 466 ? 0.3912 0.4617 0.5420 0.0382  -0.0244 0.0523  452 LYS B CE  
7455 N NZ  . LYS B 466 ? 0.3415 0.4130 0.4955 0.0377  -0.0332 0.0600  452 LYS B NZ  
7456 N N   . GLN B 467 ? 0.2360 0.3018 0.3453 0.0150  -0.0137 0.0377  453 GLN B N   
7457 C CA  . GLN B 467 ? 0.2341 0.3073 0.3411 0.0100  -0.0131 0.0383  453 GLN B CA  
7458 C C   . GLN B 467 ? 0.2532 0.3330 0.3661 0.0072  -0.0187 0.0435  453 GLN B C   
7459 O O   . GLN B 467 ? 0.2587 0.3359 0.3731 0.0076  -0.0240 0.0460  453 GLN B O   
7460 C CB  . GLN B 467 ? 0.2282 0.2941 0.3222 0.0056  -0.0136 0.0362  453 GLN B CB  
7461 C CG  . GLN B 467 ? 0.2327 0.2916 0.3189 0.0063  -0.0093 0.0311  453 GLN B CG  
7462 C CD  . GLN B 467 ? 0.2216 0.2780 0.2968 0.0013  -0.0101 0.0299  453 GLN B CD  
7463 O OE1 . GLN B 467 ? 0.2097 0.2655 0.2826 -0.0010 -0.0146 0.0325  453 GLN B OE1 
7464 N NE2 . GLN B 467 ? 0.2188 0.2742 0.2873 0.0000  -0.0057 0.0258  453 GLN B NE2 
7465 N N   . HIS B 468 ? 0.2452 0.3333 0.3602 0.0033  -0.0177 0.0451  454 HIS B N   
7466 C CA  . HIS B 468 ? 0.2360 0.3301 0.3566 -0.0007 -0.0228 0.0496  454 HIS B CA  
7467 C C   . HIS B 468 ? 0.2428 0.3328 0.3557 -0.0068 -0.0249 0.0504  454 HIS B C   
7468 O O   . HIS B 468 ? 0.2333 0.3300 0.3502 -0.0113 -0.0254 0.0535  454 HIS B O   
7469 C CB  . HIS B 468 ? 0.2247 0.3343 0.3587 -0.0002 -0.0204 0.0523  454 HIS B CB  
7470 C CG  . HIS B 468 ? 0.2462 0.3610 0.3903 0.0074  -0.0178 0.0516  454 HIS B CG  
7471 N ND1 . HIS B 468 ? 0.2441 0.3724 0.3988 0.0110  -0.0116 0.0511  454 HIS B ND1 
7472 C CD2 . HIS B 468 ? 0.2459 0.3544 0.3916 0.0125  -0.0208 0.0518  454 HIS B CD2 
7473 C CE1 . HIS B 468 ? 0.2480 0.3770 0.4111 0.0190  -0.0108 0.0504  454 HIS B CE1 
7474 N NE2 . HIS B 468 ? 0.2424 0.3588 0.4000 0.0198  -0.0167 0.0514  454 HIS B NE2 
7475 N N   . PRO B 469 ? 0.2270 0.3062 0.3293 -0.0071 -0.0264 0.0481  455 PRO B N   
7476 C CA  . PRO B 469 ? 0.2138 0.2881 0.3102 -0.0114 -0.0292 0.0492  455 PRO B CA  
7477 C C   . PRO B 469 ? 0.2371 0.3095 0.3358 -0.0145 -0.0353 0.0511  455 PRO B C   
7478 O O   . PRO B 469 ? 0.2284 0.3029 0.3310 -0.0135 -0.0380 0.0514  455 PRO B O   
7479 C CB  . PRO B 469 ? 0.2338 0.2994 0.3206 -0.0096 -0.0293 0.0459  455 PRO B CB  
7480 C CG  . PRO B 469 ? 0.2210 0.2852 0.3081 -0.0061 -0.0289 0.0439  455 PRO B CG  
7481 C CD  . PRO B 469 ? 0.2120 0.2833 0.3083 -0.0039 -0.0266 0.0450  455 PRO B CD  
7482 N N   . ILE B 470 ? 0.2191 0.2866 0.3145 -0.0187 -0.0378 0.0525  456 ILE B N   
7483 C CA  . ILE B 470 ? 0.2228 0.2842 0.3170 -0.0222 -0.0437 0.0527  456 ILE B CA  
7484 C C   . ILE B 470 ? 0.2353 0.2848 0.3200 -0.0200 -0.0452 0.0490  456 ILE B C   
7485 O O   . ILE B 470 ? 0.2362 0.2802 0.3172 -0.0202 -0.0448 0.0496  456 ILE B O   
7486 C CB  . ILE B 470 ? 0.2312 0.2942 0.3292 -0.0288 -0.0456 0.0569  456 ILE B CB  
7487 C CG1 . ILE B 470 ? 0.2191 0.2980 0.3282 -0.0306 -0.0431 0.0605  456 ILE B CG1 
7488 C CG2 . ILE B 470 ? 0.2240 0.2780 0.3193 -0.0333 -0.0521 0.0560  456 ILE B CG2 
7489 C CD1 . ILE B 470 ? 0.2320 0.3163 0.3445 -0.0369 -0.0419 0.0654  456 ILE B CD1 
7490 N N   . ILE B 471 ? 0.2368 0.2835 0.3179 -0.0177 -0.0469 0.0456  457 ILE B N   
7491 C CA  . ILE B 471 ? 0.2407 0.2795 0.3138 -0.0149 -0.0474 0.0414  457 ILE B CA  
7492 C C   . ILE B 471 ? 0.2445 0.2750 0.3139 -0.0175 -0.0521 0.0389  457 ILE B C   
7493 O O   . ILE B 471 ? 0.2191 0.2510 0.2882 -0.0200 -0.0552 0.0381  457 ILE B O   
7494 C CB  . ILE B 471 ? 0.2337 0.2755 0.3040 -0.0117 -0.0457 0.0391  457 ILE B CB  
7495 C CG1 . ILE B 471 ? 0.2287 0.2764 0.3021 -0.0097 -0.0413 0.0408  457 ILE B CG1 
7496 C CG2 . ILE B 471 ? 0.2163 0.2533 0.2792 -0.0091 -0.0455 0.0349  457 ILE B CG2 
7497 C CD1 . ILE B 471 ? 0.2316 0.2805 0.3028 -0.0077 -0.0403 0.0396  457 ILE B CD1 
7498 N N   . LEU B 472 ? 0.2388 0.2599 0.3049 -0.0169 -0.0530 0.0377  458 LEU B N   
7499 C CA  . LEU B 472 ? 0.2603 0.2700 0.3217 -0.0185 -0.0570 0.0339  458 LEU B CA  
7500 C C   . LEU B 472 ? 0.2623 0.2678 0.3175 -0.0125 -0.0555 0.0280  458 LEU B C   
7501 O O   . LEU B 472 ? 0.2502 0.2537 0.3054 -0.0079 -0.0535 0.0282  458 LEU B O   
7502 C CB  . LEU B 472 ? 0.2274 0.2274 0.2901 -0.0218 -0.0594 0.0369  458 LEU B CB  
7503 C CG  . LEU B 472 ? 0.2699 0.2750 0.3387 -0.0294 -0.0612 0.0426  458 LEU B CG  
7504 C CD1 . LEU B 472 ? 0.2708 0.2818 0.3442 -0.0298 -0.0581 0.0488  458 LEU B CD1 
7505 C CD2 . LEU B 472 ? 0.2800 0.2725 0.3466 -0.0359 -0.0667 0.0419  458 LEU B CD2 
7506 N N   . VAL B 473 ? 0.2549 0.2610 0.3048 -0.0127 -0.0563 0.0231  459 VAL B N   
7507 C CA  . VAL B 473 ? 0.2554 0.2601 0.2994 -0.0076 -0.0543 0.0169  459 VAL B CA  
7508 C C   . VAL B 473 ? 0.3038 0.2948 0.3426 -0.0073 -0.0569 0.0109  459 VAL B C   
7509 O O   . VAL B 473 ? 0.2756 0.2626 0.3097 -0.0122 -0.0601 0.0078  459 VAL B O   
7510 C CB  . VAL B 473 ? 0.2617 0.2755 0.3016 -0.0085 -0.0533 0.0153  459 VAL B CB  
7511 C CG1 . VAL B 473 ? 0.2650 0.2792 0.2984 -0.0042 -0.0506 0.0085  459 VAL B CG1 
7512 C CG2 . VAL B 473 ? 0.2516 0.2755 0.2963 -0.0083 -0.0508 0.0208  459 VAL B CG2 
7513 N N   . LEU B 474 ? 0.2851 0.2687 0.3245 -0.0014 -0.0556 0.0089  460 LEU B N   
7514 C CA  . LEU B 474 ? 0.3013 0.2690 0.3360 0.0004  -0.0577 0.0024  460 LEU B CA  
7515 C C   . LEU B 474 ? 0.3240 0.2947 0.3516 0.0042  -0.0550 -0.0066 460 LEU B C   
7516 O O   . LEU B 474 ? 0.3172 0.2943 0.3460 0.0115  -0.0510 -0.0090 460 LEU B O   
7517 C CB  . LEU B 474 ? 0.2908 0.2491 0.3300 0.0061  -0.0579 0.0047  460 LEU B CB  
7518 C CG  . LEU B 474 ? 0.2859 0.2447 0.3312 0.0018  -0.0597 0.0147  460 LEU B CG  
7519 C CD1 . LEU B 474 ? 0.3546 0.3000 0.4024 0.0059  -0.0617 0.0177  460 LEU B CD1 
7520 C CD2 . LEU B 474 ? 0.3131 0.2698 0.3582 -0.0081 -0.0632 0.0176  460 LEU B CD2 
7521 N N   . ASN B 475 ? 0.3397 0.3081 0.3597 -0.0014 -0.0572 -0.0113 461 ASN B N   
7522 C CA  . ASN B 475 ? 0.3590 0.3325 0.3703 0.0003  -0.0545 -0.0195 461 ASN B CA  
7523 C C   . ASN B 475 ? 0.4133 0.3703 0.4177 0.0035  -0.0549 -0.0299 461 ASN B C   
7524 O O   . ASN B 475 ? 0.4088 0.3544 0.4066 -0.0029 -0.0592 -0.0337 461 ASN B O   
7525 C CB  . ASN B 475 ? 0.3521 0.3343 0.3579 -0.0079 -0.0569 -0.0181 461 ASN B CB  
7526 C CG  . ASN B 475 ? 0.3878 0.3774 0.3832 -0.0073 -0.0539 -0.0254 461 ASN B CG  
7527 O OD1 . ASN B 475 ? 0.4272 0.4160 0.4200 -0.0003 -0.0495 -0.0327 461 ASN B OD1 
7528 N ND2 . ASN B 475 ? 0.3339 0.3320 0.3238 -0.0144 -0.0564 -0.0232 461 ASN B ND2 
7529 N N   . ASN B 476 ? 0.4021 0.3584 0.4083 0.0134  -0.0505 -0.0348 462 ASN B N   
7530 C CA  . ASN B 476 ? 0.4710 0.4139 0.4708 0.0191  -0.0491 -0.0466 462 ASN B CA  
7531 C C   . ASN B 476 ? 0.4781 0.4350 0.4724 0.0241  -0.0428 -0.0548 462 ASN B C   
7532 O O   . ASN B 476 ? 0.5001 0.4500 0.4914 0.0321  -0.0395 -0.0651 462 ASN B O   
7533 C CB  . ASN B 476 ? 0.4786 0.4080 0.4867 0.0281  -0.0494 -0.0455 462 ASN B CB  
7534 C CG  . ASN B 476 ? 0.4747 0.4200 0.4937 0.0351  -0.0460 -0.0383 462 ASN B CG  
7535 O OD1 . ASN B 476 ? 0.4576 0.4222 0.4769 0.0370  -0.0414 -0.0391 462 ASN B OD1 
7536 N ND2 . ASN B 476 ? 0.4808 0.4186 0.5083 0.0379  -0.0487 -0.0307 462 ASN B ND2 
7537 N N   . GLU B 477 ? 0.4617 0.4384 0.4549 0.0197  -0.0408 -0.0502 463 GLU B N   
7538 C CA  . GLU B 477 ? 0.5074 0.4994 0.4929 0.0205  -0.0355 -0.0565 463 GLU B CA  
7539 C C   . GLU B 477 ? 0.4857 0.4880 0.4776 0.0317  -0.0288 -0.0604 463 GLU B C   
7540 O O   . GLU B 477 ? 0.4984 0.5047 0.4841 0.0363  -0.0237 -0.0708 463 GLU B O   
7541 C CB  . GLU B 477 ? 0.5298 0.5129 0.5005 0.0163  -0.0363 -0.0675 463 GLU B CB  
7542 C CG  . GLU B 477 ? 0.5501 0.5312 0.5143 0.0039  -0.0429 -0.0626 463 GLU B CG  
7543 C CD  . GLU B 477 ? 0.6768 0.6607 0.6244 -0.0024 -0.0428 -0.0711 463 GLU B CD  
7544 O OE1 . GLU B 477 ? 0.6642 0.6440 0.6038 0.0027  -0.0382 -0.0837 463 GLU B OE1 
7545 O OE2 . GLU B 477 ? 0.6690 0.6597 0.6119 -0.0122 -0.0473 -0.0652 463 GLU B OE2 
7546 N N   . GLY B 478 ? 0.4912 0.5000 0.4955 0.0357  -0.0285 -0.0519 464 GLY B N   
7547 C CA  . GLY B 478 ? 0.4836 0.5064 0.4958 0.0452  -0.0229 -0.0534 464 GLY B CA  
7548 C C   . GLY B 478 ? 0.4978 0.5167 0.5231 0.0514  -0.0251 -0.0461 464 GLY B C   
7549 O O   . GLY B 478 ? 0.4701 0.4777 0.4980 0.0472  -0.0303 -0.0388 464 GLY B O   
7550 N N   . TYR B 479 ? 0.5251 0.5555 0.5589 0.0614  -0.0209 -0.0480 465 TYR B N   
7551 C CA  . TYR B 479 ? 0.5359 0.5666 0.5826 0.0684  -0.0228 -0.0410 465 TYR B CA  
7552 C C   . TYR B 479 ? 0.5912 0.5999 0.6405 0.0775  -0.0251 -0.0457 465 TYR B C   
7553 O O   . TYR B 479 ? 0.6346 0.6459 0.6902 0.0894  -0.0219 -0.0515 465 TYR B O   
7554 C CB  . TYR B 479 ? 0.5121 0.5676 0.5674 0.0745  -0.0178 -0.0405 465 TYR B CB  
7555 C CG  . TYR B 479 ? 0.4847 0.5616 0.5386 0.0656  -0.0157 -0.0350 465 TYR B CG  
7556 C CD1 . TYR B 479 ? 0.4081 0.4813 0.4578 0.0547  -0.0194 -0.0272 465 TYR B CD1 
7557 C CD2 . TYR B 479 ? 0.4474 0.5481 0.5045 0.0683  -0.0098 -0.0377 465 TYR B CD2 
7558 C CE1 . TYR B 479 ? 0.3840 0.4735 0.4322 0.0471  -0.0177 -0.0224 465 TYR B CE1 
7559 C CE2 . TYR B 479 ? 0.3887 0.5070 0.4440 0.0591  -0.0083 -0.0323 465 TYR B CE2 
7560 C CZ  . TYR B 479 ? 0.3831 0.4941 0.4335 0.0487  -0.0124 -0.0248 465 TYR B CZ  
7561 O OH  . TYR B 479 ? 0.3486 0.4742 0.3969 0.0400  -0.0112 -0.0196 465 TYR B OH  
7562 N N   . THR B 480 ? 0.5769 0.5636 0.6220 0.0719  -0.0309 -0.0429 466 THR B N   
7563 C CA  . THR B 480 ? 0.6226 0.5843 0.6678 0.0786  -0.0337 -0.0478 466 THR B CA  
7564 C C   . THR B 480 ? 0.6904 0.6506 0.7486 0.0900  -0.0351 -0.0424 466 THR B C   
7565 O O   . THR B 480 ? 0.6995 0.6475 0.7609 0.1014  -0.0343 -0.0491 466 THR B O   
7566 C CB  . THR B 480 ? 0.6064 0.5469 0.6451 0.0683  -0.0400 -0.0442 466 THR B CB  
7567 O OG1 . THR B 480 ? 0.6921 0.6304 0.7184 0.0601  -0.0393 -0.0518 466 THR B OG1 
7568 C CG2 . THR B 480 ? 0.7020 0.6151 0.7427 0.0739  -0.0443 -0.0452 466 THR B CG2 
7569 N N   . VAL B 481 ? 0.7231 0.6951 0.7886 0.0871  -0.0374 -0.0303 467 VAL B N   
7570 C CA  . VAL B 481 ? 0.6788 0.6524 0.7564 0.0966  -0.0396 -0.0233 467 VAL B CA  
7571 C C   . VAL B 481 ? 0.6812 0.6710 0.7671 0.1100  -0.0343 -0.0299 467 VAL B C   
7572 O O   . VAL B 481 ? 0.6830 0.6648 0.7775 0.1225  -0.0356 -0.0305 467 VAL B O   
7573 C CB  . VAL B 481 ? 0.5915 0.5788 0.6729 0.0892  -0.0423 -0.0103 467 VAL B CB  
7574 C CG1 . VAL B 481 ? 0.5081 0.5179 0.5861 0.0820  -0.0378 -0.0114 467 VAL B CG1 
7575 C CG2 . VAL B 481 ? 0.6044 0.6003 0.6979 0.0986  -0.0443 -0.0030 467 VAL B CG2 
7576 N N   . GLU B 482 ? 0.7095 0.7230 0.7937 0.1076  -0.0283 -0.0344 468 GLU B N   
7577 C CA  . GLU B 482 ? 0.6624 0.6953 0.7550 0.1193  -0.0223 -0.0408 468 GLU B CA  
7578 C C   . GLU B 482 ? 0.6872 0.7051 0.7764 0.1291  -0.0188 -0.0548 468 GLU B C   
7579 O O   . GLU B 482 ? 0.6792 0.7042 0.7785 0.1435  -0.0154 -0.0599 468 GLU B O   
7580 C CB  . GLU B 482 ? 0.5862 0.6473 0.6761 0.1122  -0.0167 -0.0419 468 GLU B CB  
7581 C CG  . GLU B 482 ? 0.4935 0.5679 0.5843 0.1012  -0.0195 -0.0300 468 GLU B CG  
7582 C CD  . GLU B 482 ? 0.4288 0.5196 0.5337 0.1071  -0.0214 -0.0217 468 GLU B CD  
7583 O OE1 . GLU B 482 ? 0.4214 0.4992 0.5319 0.1116  -0.0270 -0.0151 468 GLU B OE1 
7584 O OE2 . GLU B 482 ? 0.3753 0.4927 0.4852 0.1067  -0.0174 -0.0212 468 GLU B OE2 
7585 N N   . ARG B 483 ? 0.7023 0.6999 0.7773 0.1216  -0.0196 -0.0614 469 ARG B N   
7586 C CA  . ARG B 483 ? 0.7439 0.7216 0.8133 0.1297  -0.0173 -0.0753 469 ARG B CA  
7587 C C   . ARG B 483 ? 0.7447 0.6992 0.8232 0.1416  -0.0219 -0.0735 469 ARG B C   
7588 O O   . ARG B 483 ? 0.7483 0.6963 0.8311 0.1559  -0.0184 -0.0835 469 ARG B O   
7589 C CB  . ARG B 483 ? 0.7274 0.6864 0.7795 0.1170  -0.0193 -0.0808 469 ARG B CB  
7590 C CG  . ARG B 483 ? 0.7004 0.6793 0.7420 0.1051  -0.0156 -0.0826 469 ARG B CG  
7591 C CD  . ARG B 483 ? 0.7203 0.6797 0.7454 0.0943  -0.0184 -0.0888 469 ARG B CD  
7592 N NE  . ARG B 483 ? 0.6586 0.6341 0.6738 0.0814  -0.0172 -0.0874 469 ARG B NE  
7593 C CZ  . ARG B 483 ? 0.6563 0.6520 0.6655 0.0809  -0.0105 -0.0940 469 ARG B CZ  
7594 N NH1 . ARG B 483 ? 0.6687 0.6737 0.6810 0.0926  -0.0034 -0.1040 469 ARG B NH1 
7595 N NH2 . ARG B 483 ? 0.6036 0.6112 0.6039 0.0684  -0.0110 -0.0901 469 ARG B NH2 
7596 N N   . ALA B 484 ? 0.7531 0.6942 0.8339 0.1360  -0.0298 -0.0607 470 ALA B N   
7597 C CA  . ALA B 484 ? 0.7922 0.7109 0.8814 0.1459  -0.0353 -0.0560 470 ALA B CA  
7598 C C   . ALA B 484 ? 0.7836 0.7204 0.8899 0.1622  -0.0332 -0.0536 470 ALA B C   
7599 O O   . ALA B 484 ? 0.7880 0.7088 0.9014 0.1769  -0.0338 -0.0579 470 ALA B O   
7600 C CB  . ALA B 484 ? 0.8124 0.7198 0.9007 0.1348  -0.0436 -0.0410 470 ALA B CB  
7601 N N   . ILE B 485 ? 0.7532 0.7229 0.8668 0.1600  -0.0310 -0.0465 471 ILE B N   
7602 C CA  . ILE B 485 ? 0.7426 0.7330 0.8738 0.1742  -0.0300 -0.0425 471 ILE B CA  
7603 C C   . ILE B 485 ? 0.7332 0.7357 0.8693 0.1879  -0.0212 -0.0572 471 ILE B C   
7604 O O   . ILE B 485 ? 0.7409 0.7377 0.8889 0.2050  -0.0209 -0.0605 471 ILE B O   
7605 C CB  . ILE B 485 ? 0.7072 0.7297 0.8439 0.1661  -0.0305 -0.0310 471 ILE B CB  
7606 C CG1 . ILE B 485 ? 0.7252 0.7395 0.8617 0.1573  -0.0391 -0.0153 471 ILE B CG1 
7607 C CG2 . ILE B 485 ? 0.6997 0.7513 0.8539 0.1795  -0.0274 -0.0301 471 ILE B CG2 
7608 C CD1 . ILE B 485 ? 0.7267 0.7132 0.8495 0.1451  -0.0434 -0.0134 471 ILE B CD1 
7609 N N   . HIS B 486 ? 0.7290 0.7481 0.8560 0.1808  -0.0139 -0.0663 472 HIS B N   
7610 C CA  . HIS B 486 ? 0.7146 0.7512 0.8461 0.1926  -0.0045 -0.0798 472 HIS B CA  
7611 C C   . HIS B 486 ? 0.7036 0.7458 0.8181 0.1818  0.0021  -0.0909 472 HIS B C   
7612 O O   . HIS B 486 ? 0.6876 0.7400 0.7934 0.1658  0.0011  -0.0848 472 HIS B O   
7613 C CB  . HIS B 486 ? 0.6608 0.7364 0.8098 0.1991  -0.0015 -0.0735 472 HIS B CB  
7614 C CG  . HIS B 486 ? 0.6450 0.7393 0.8041 0.2153  0.0076  -0.0858 472 HIS B CG  
7615 N ND1 . HIS B 486 ? 0.6558 0.7345 0.8251 0.2348  0.0081  -0.0925 472 HIS B ND1 
7616 C CD2 . HIS B 486 ? 0.5445 0.6721 0.7050 0.2150  0.0170  -0.0927 472 HIS B CD2 
7617 C CE1 . HIS B 486 ? 0.6258 0.7287 0.8033 0.2467  0.0178  -0.1038 472 HIS B CE1 
7618 N NE2 . HIS B 486 ? 0.5624 0.6963 0.7346 0.2345  0.0235  -0.1039 472 HIS B NE2 
7619 N N   . GLY B 487 ? 0.7168 0.7517 0.8263 0.1907  0.0088  -0.1072 473 GLY B N   
7620 C CA  . GLY B 487 ? 0.7067 0.7509 0.8005 0.1821  0.0159  -0.1186 473 GLY B CA  
7621 C C   . GLY B 487 ? 0.7375 0.7611 0.8119 0.1642  0.0110  -0.1173 473 GLY B C   
7622 O O   . GLY B 487 ? 0.7022 0.7420 0.7691 0.1498  0.0111  -0.1116 473 GLY B O   
7623 N N   . PRO B 488 ? 0.7813 0.7687 0.8476 0.1647  0.0061  -0.1223 474 PRO B N   
7624 C CA  . PRO B 488 ? 0.7944 0.7637 0.8437 0.1473  0.0007  -0.1202 474 PRO B CA  
7625 C C   . PRO B 488 ? 0.7925 0.7732 0.8249 0.1375  0.0063  -0.1302 474 PRO B C   
7626 O O   . PRO B 488 ? 0.7677 0.7494 0.7898 0.1217  0.0025  -0.1241 474 PRO B O   
7627 C CB  . PRO B 488 ? 0.8242 0.7532 0.8695 0.1516  -0.0048 -0.1253 474 PRO B CB  
7628 C CG  . PRO B 488 ? 0.8090 0.7337 0.8680 0.1726  -0.0013 -0.1320 474 PRO B CG  
7629 C CD  . PRO B 488 ? 0.7932 0.7567 0.8625 0.1808  0.0075  -0.1340 474 PRO B CD  
7630 N N   . GLU B 489 ? 0.8294 0.8199 0.8590 0.1467  0.0153  -0.1451 475 GLU B N   
7631 C CA  . GLU B 489 ? 0.8384 0.8418 0.8509 0.1377  0.0212  -0.1549 475 GLU B CA  
7632 C C   . GLU B 489 ? 0.7728 0.8165 0.7899 0.1349  0.0279  -0.1503 475 GLU B C   
7633 O O   . GLU B 489 ? 0.8124 0.8705 0.8158 0.1276  0.0334  -0.1574 475 GLU B O   
7634 C CB  . GLU B 489 ? 0.8943 0.8848 0.8978 0.1479  0.0279  -0.1754 475 GLU B CB  
7635 C CG  . GLU B 489 ? 0.9879 0.9360 0.9826 0.1480  0.0215  -0.1822 475 GLU B CG  
7636 C CD  . GLU B 489 ? 1.1485 1.0818 1.1376 0.1617  0.0286  -0.2030 475 GLU B CD  
7637 O OE1 . GLU B 489 ? 1.1387 1.0705 1.1084 0.1551  0.0328  -0.2168 475 GLU B OE1 
7638 O OE2 . GLU B 489 ? 1.2637 1.1871 1.2678 0.1794  0.0298  -0.2057 475 GLU B OE2 
7639 N N   . GLN B 490 ? 0.7063 0.7684 0.7415 0.1395  0.0270  -0.1383 476 GLN B N   
7640 C CA  . GLN B 490 ? 0.6430 0.7430 0.6835 0.1368  0.0332  -0.1340 476 GLN B CA  
7641 C C   . GLN B 490 ? 0.6092 0.7170 0.6399 0.1177  0.0291  -0.1228 476 GLN B C   
7642 O O   . GLN B 490 ? 0.5783 0.6705 0.6092 0.1102  0.0206  -0.1119 476 GLN B O   
7643 C CB  . GLN B 490 ? 0.5710 0.6882 0.6344 0.1478  0.0331  -0.1252 476 GLN B CB  
7644 C CG  . GLN B 490 ? 0.5683 0.6911 0.6449 0.1682  0.0396  -0.1359 476 GLN B CG  
7645 C CD  . GLN B 490 ? 0.5370 0.6890 0.6109 0.1719  0.0518  -0.1482 476 GLN B CD  
7646 O OE1 . GLN B 490 ? 0.5849 0.7409 0.6406 0.1606  0.0555  -0.1543 476 GLN B OE1 
7647 N NE2 . GLN B 490 ? 0.4586 0.6331 0.5511 0.1877  0.0578  -0.1511 476 GLN B NE2 
7648 N N   . ARG B 491 ? 0.5831 0.7156 0.6054 0.1102  0.0355  -0.1252 477 ARG B N   
7649 C CA  . ARG B 491 ? 0.6048 0.7427 0.6161 0.0925  0.0317  -0.1155 477 ARG B CA  
7650 C C   . ARG B 491 ? 0.5653 0.7140 0.5889 0.0875  0.0270  -0.0992 477 ARG B C   
7651 O O   . ARG B 491 ? 0.5587 0.7042 0.5751 0.0742  0.0220  -0.0900 477 ARG B O   
7652 C CB  . ARG B 491 ? 0.6117 0.7724 0.6100 0.0855  0.0395  -0.1217 477 ARG B CB  
7653 C CG  . ARG B 491 ? 0.6570 0.8527 0.6660 0.0904  0.0482  -0.1219 477 ARG B CG  
7654 C CD  . ARG B 491 ? 0.6135 0.8322 0.6085 0.0773  0.0532  -0.1213 477 ARG B CD  
7655 N NE  . ARG B 491 ? 0.6341 0.8613 0.6309 0.0642  0.0480  -0.1052 477 ARG B NE  
7656 C CZ  . ARG B 491 ? 0.4390 0.6951 0.4418 0.0592  0.0521  -0.0984 477 ARG B CZ  
7657 N NH1 . ARG B 491 ? 0.3802 0.6641 0.3878 0.0652  0.0620  -0.1057 477 ARG B NH1 
7658 N NH2 . ARG B 491 ? 0.3672 0.6247 0.3716 0.0478  0.0462  -0.0841 477 ARG B NH2 
7659 N N   . TYR B 492 ? 0.5107 0.6723 0.5524 0.0977  0.0284  -0.0955 478 TYR B N   
7660 C CA  . TYR B 492 ? 0.4848 0.6546 0.5364 0.0920  0.0234  -0.0808 478 TYR B CA  
7661 C C   . TYR B 492 ? 0.4926 0.6350 0.5440 0.0888  0.0140  -0.0731 478 TYR B C   
7662 O O   . TYR B 492 ? 0.4536 0.5992 0.5083 0.0810  0.0095  -0.0615 478 TYR B O   
7663 C CB  . TYR B 492 ? 0.3940 0.5857 0.4649 0.1030  0.0262  -0.0782 478 TYR B CB  
7664 C CG  . TYR B 492 ? 0.4415 0.6222 0.5243 0.1207  0.0262  -0.0843 478 TYR B CG  
7665 C CD1 . TYR B 492 ? 0.4279 0.5822 0.5149 0.1245  0.0182  -0.0790 478 TYR B CD1 
7666 C CD2 . TYR B 492 ? 0.4008 0.5986 0.4916 0.1340  0.0344  -0.0946 478 TYR B CD2 
7667 C CE1 . TYR B 492 ? 0.4511 0.5938 0.5492 0.1408  0.0175  -0.0833 478 TYR B CE1 
7668 C CE2 . TYR B 492 ? 0.4109 0.5980 0.5138 0.1516  0.0343  -0.0999 478 TYR B CE2 
7669 C CZ  . TYR B 492 ? 0.4466 0.6050 0.5530 0.1549  0.0254  -0.0938 478 TYR B CZ  
7670 O OH  . TYR B 492 ? 0.4412 0.5874 0.5595 0.1726  0.0249  -0.0983 478 TYR B OH  
7671 N N   . ASN B 493 ? 0.5184 0.6341 0.5653 0.0938  0.0112  -0.0795 479 ASN B N   
7672 C CA  . ASN B 493 ? 0.5742 0.6644 0.6194 0.0892  0.0027  -0.0726 479 ASN B CA  
7673 C C   . ASN B 493 ? 0.5714 0.6512 0.6010 0.0753  -0.0004 -0.0718 479 ASN B C   
7674 O O   . ASN B 493 ? 0.5610 0.6225 0.5889 0.0699  -0.0071 -0.0657 479 ASN B O   
7675 C CB  . ASN B 493 ? 0.5898 0.6556 0.6386 0.1006  0.0005  -0.0787 479 ASN B CB  
7676 C CG  . ASN B 493 ? 0.6170 0.6887 0.6836 0.1131  -0.0002 -0.0739 479 ASN B CG  
7677 O OD1 . ASN B 493 ? 0.5585 0.6490 0.6340 0.1108  -0.0010 -0.0640 479 ASN B OD1 
7678 N ND2 . ASN B 493 ? 0.6419 0.6978 0.7134 0.1265  0.0000  -0.0811 479 ASN B ND2 
7679 N N   . ASP B 494 ? 0.5613 0.6540 0.5798 0.0693  0.0042  -0.0770 480 ASP B N   
7680 C CA  . ASP B 494 ? 0.5502 0.6372 0.5549 0.0559  0.0008  -0.0744 480 ASP B CA  
7681 C C   . ASP B 494 ? 0.5015 0.6017 0.5087 0.0463  -0.0013 -0.0616 480 ASP B C   
7682 O O   . ASP B 494 ? 0.4990 0.6173 0.5156 0.0483  0.0015  -0.0568 480 ASP B O   
7683 C CB  . ASP B 494 ? 0.5667 0.6614 0.5569 0.0530  0.0061  -0.0850 480 ASP B CB  
7684 C CG  . ASP B 494 ? 0.5921 0.6709 0.5773 0.0618  0.0083  -0.0994 480 ASP B CG  
7685 O OD1 . ASP B 494 ? 0.6064 0.6614 0.5953 0.0656  0.0031  -0.0996 480 ASP B OD1 
7686 O OD2 . ASP B 494 ? 0.6002 0.6899 0.5778 0.0646  0.0155  -0.1105 480 ASP B OD2 
7687 N N   . ILE B 495 ? 0.4921 0.5827 0.4914 0.0359  -0.0067 -0.0561 481 ILE B N   
7688 C CA  . ILE B 495 ? 0.4144 0.5135 0.4144 0.0267  -0.0090 -0.0448 481 ILE B CA  
7689 C C   . ILE B 495 ? 0.3710 0.4705 0.3569 0.0163  -0.0106 -0.0443 481 ILE B C   
7690 O O   . ILE B 495 ? 0.3717 0.4630 0.3473 0.0153  -0.0111 -0.0520 481 ILE B O   
7691 C CB  . ILE B 495 ? 0.3782 0.4648 0.3863 0.0254  -0.0151 -0.0357 481 ILE B CB  
7692 C CG1 . ILE B 495 ? 0.4024 0.4680 0.4057 0.0233  -0.0205 -0.0374 481 ILE B CG1 
7693 C CG2 . ILE B 495 ? 0.4296 0.5175 0.4507 0.0346  -0.0142 -0.0346 481 ILE B CG2 
7694 C CD1 . ILE B 495 ? 0.3745 0.4281 0.3867 0.0239  -0.0254 -0.0301 481 ILE B CD1 
7695 N N   . ALA B 496 ? 0.3193 0.4277 0.3043 0.0082  -0.0118 -0.0350 482 ALA B N   
7696 C CA  . ALA B 496 ? 0.3229 0.4281 0.2966 -0.0016 -0.0158 -0.0311 482 ALA B CA  
7697 C C   . ALA B 496 ? 0.3299 0.4162 0.3045 -0.0026 -0.0226 -0.0295 482 ALA B C   
7698 O O   . ALA B 496 ? 0.3091 0.3870 0.2942 0.0006  -0.0251 -0.0252 482 ALA B O   
7699 C CB  . ALA B 496 ? 0.2805 0.3947 0.2551 -0.0090 -0.0168 -0.0203 482 ALA B CB  
7700 N N   . LEU B 497 ? 0.2968 0.3778 0.2599 -0.0079 -0.0257 -0.0327 483 LEU B N   
7701 C CA  . LEU B 497 ? 0.3220 0.3873 0.2854 -0.0104 -0.0325 -0.0313 483 LEU B CA  
7702 C C   . LEU B 497 ? 0.3203 0.3875 0.2847 -0.0178 -0.0377 -0.0198 483 LEU B C   
7703 O O   . LEU B 497 ? 0.3272 0.4014 0.2819 -0.0247 -0.0393 -0.0171 483 LEU B O   
7704 C CB  . LEU B 497 ? 0.3388 0.3973 0.2892 -0.0127 -0.0337 -0.0412 483 LEU B CB  
7705 C CG  . LEU B 497 ? 0.3971 0.4512 0.3467 -0.0040 -0.0282 -0.0538 483 LEU B CG  
7706 C CD1 . LEU B 497 ? 0.4665 0.5137 0.4006 -0.0072 -0.0288 -0.0651 483 LEU B CD1 
7707 C CD2 . LEU B 497 ? 0.4183 0.4585 0.3809 0.0033  -0.0297 -0.0531 483 LEU B CD2 
7708 N N   . TRP B 498 ? 0.2980 0.3589 0.2739 -0.0163 -0.0405 -0.0130 484 TRP B N   
7709 C CA  . TRP B 498 ? 0.2887 0.3510 0.2682 -0.0211 -0.0447 -0.0025 484 TRP B CA  
7710 C C   . TRP B 498 ? 0.3191 0.3738 0.2983 -0.0252 -0.0514 -0.0006 484 TRP B C   
7711 O O   . TRP B 498 ? 0.2998 0.3458 0.2780 -0.0244 -0.0530 -0.0067 484 TRP B O   
7712 C CB  . TRP B 498 ? 0.2820 0.3433 0.2740 -0.0173 -0.0433 0.0032  484 TRP B CB  
7713 C CG  . TRP B 498 ? 0.2849 0.3559 0.2779 -0.0158 -0.0381 0.0041  484 TRP B CG  
7714 C CD1 . TRP B 498 ? 0.2935 0.3751 0.2786 -0.0172 -0.0341 0.0007  484 TRP B CD1 
7715 C CD2 . TRP B 498 ? 0.2719 0.3441 0.2739 -0.0136 -0.0364 0.0087  484 TRP B CD2 
7716 N NE1 . TRP B 498 ? 0.2615 0.3513 0.2513 -0.0164 -0.0303 0.0035  484 TRP B NE1 
7717 C CE2 . TRP B 498 ? 0.2289 0.3125 0.2286 -0.0143 -0.0319 0.0082  484 TRP B CE2 
7718 C CE3 . TRP B 498 ? 0.2596 0.3254 0.2708 -0.0118 -0.0380 0.0130  484 TRP B CE3 
7719 C CZ2 . TRP B 498 ? 0.2589 0.3464 0.2649 -0.0137 -0.0298 0.0118  484 TRP B CZ2 
7720 C CZ3 . TRP B 498 ? 0.2283 0.2977 0.2448 -0.0107 -0.0354 0.0160  484 TRP B CZ3 
7721 C CH2 . TRP B 498 ? 0.2240 0.3037 0.2378 -0.0119 -0.0317 0.0153  484 TRP B CH2 
7722 N N   . ASN B 499 ? 0.2782 0.3364 0.2586 -0.0298 -0.0557 0.0082  485 ASN B N   
7723 C CA  . ASN B 499 ? 0.3052 0.3601 0.2882 -0.0337 -0.0626 0.0123  485 ASN B CA  
7724 C C   . ASN B 499 ? 0.2839 0.3360 0.2818 -0.0304 -0.0631 0.0187  485 ASN B C   
7725 O O   . ASN B 499 ? 0.2675 0.3231 0.2709 -0.0309 -0.0649 0.0269  485 ASN B O   
7726 C CB  . ASN B 499 ? 0.2985 0.3605 0.2739 -0.0401 -0.0673 0.0182  485 ASN B CB  
7727 C CG  . ASN B 499 ? 0.2940 0.3553 0.2690 -0.0452 -0.0750 0.0202  485 ASN B CG  
7728 O OD1 . ASN B 499 ? 0.3053 0.3605 0.2866 -0.0446 -0.0767 0.0176  485 ASN B OD1 
7729 N ND2 . ASN B 499 ? 0.3253 0.3934 0.2927 -0.0511 -0.0801 0.0253  485 ASN B ND2 
7730 N N   . TRP B 500 ? 0.2771 0.3223 0.2809 -0.0268 -0.0614 0.0148  486 TRP B N   
7731 C CA  . TRP B 500 ? 0.2797 0.3233 0.2960 -0.0232 -0.0600 0.0195  486 TRP B CA  
7732 C C   . TRP B 500 ? 0.2872 0.3340 0.3117 -0.0255 -0.0642 0.0273  486 TRP B C   
7733 O O   . TRP B 500 ? 0.2446 0.2938 0.2769 -0.0228 -0.0624 0.0326  486 TRP B O   
7734 C CB  . TRP B 500 ? 0.2745 0.3097 0.2941 -0.0206 -0.0589 0.0149  486 TRP B CB  
7735 C CG  . TRP B 500 ? 0.2776 0.3109 0.2928 -0.0159 -0.0541 0.0084  486 TRP B CG  
7736 C CD1 . TRP B 500 ? 0.2880 0.3169 0.2949 -0.0151 -0.0534 0.0001  486 TRP B CD1 
7737 C CD2 . TRP B 500 ? 0.2939 0.3311 0.3133 -0.0111 -0.0493 0.0094  486 TRP B CD2 
7738 N NE1 . TRP B 500 ? 0.2920 0.3229 0.2993 -0.0091 -0.0482 -0.0038 486 TRP B NE1 
7739 C CE2 . TRP B 500 ? 0.2898 0.3265 0.3047 -0.0070 -0.0460 0.0022  486 TRP B CE2 
7740 C CE3 . TRP B 500 ? 0.2605 0.3017 0.2869 -0.0099 -0.0474 0.0153  486 TRP B CE3 
7741 C CZ2 . TRP B 500 ? 0.2661 0.3080 0.2844 -0.0021 -0.0415 0.0018  486 TRP B CZ2 
7742 C CZ3 . TRP B 500 ? 0.2679 0.3129 0.2959 -0.0061 -0.0432 0.0143  486 TRP B CZ3 
7743 C CH2 . TRP B 500 ? 0.2580 0.3044 0.2826 -0.0024 -0.0405 0.0081  486 TRP B CH2 
7744 N N   . THR B 501 ? 0.2838 0.3314 0.3071 -0.0304 -0.0700 0.0280  487 THR B N   
7745 C CA  . THR B 501 ? 0.2952 0.3482 0.3290 -0.0318 -0.0741 0.0356  487 THR B CA  
7746 C C   . THR B 501 ? 0.2894 0.3489 0.3244 -0.0312 -0.0756 0.0426  487 THR B C   
7747 O O   . THR B 501 ? 0.3061 0.3707 0.3521 -0.0300 -0.0779 0.0493  487 THR B O   
7748 C CB  . THR B 501 ? 0.3027 0.3567 0.3352 -0.0382 -0.0806 0.0350  487 THR B CB  
7749 O OG1 . THR B 501 ? 0.2875 0.3433 0.3072 -0.0428 -0.0841 0.0328  487 THR B OG1 
7750 C CG2 . THR B 501 ? 0.2938 0.3384 0.3253 -0.0394 -0.0798 0.0286  487 THR B CG2 
7751 N N   . GLN B 502 ? 0.2835 0.3431 0.3084 -0.0317 -0.0741 0.0417  488 GLN B N   
7752 C CA  . GLN B 502 ? 0.2938 0.3571 0.3186 -0.0317 -0.0758 0.0491  488 GLN B CA  
7753 C C   . GLN B 502 ? 0.2899 0.3499 0.3178 -0.0272 -0.0701 0.0504  488 GLN B C   
7754 O O   . GLN B 502 ? 0.2916 0.3516 0.3197 -0.0270 -0.0712 0.0567  488 GLN B O   
7755 C CB  . GLN B 502 ? 0.3005 0.3670 0.3105 -0.0371 -0.0784 0.0487  488 GLN B CB  
7756 C CG  . GLN B 502 ? 0.3258 0.3952 0.3296 -0.0429 -0.0843 0.0461  488 GLN B CG  
7757 C CD  . GLN B 502 ? 0.3780 0.4525 0.3929 -0.0440 -0.0912 0.0534  488 GLN B CD  
7758 O OE1 . GLN B 502 ? 0.3994 0.4778 0.4211 -0.0421 -0.0940 0.0624  488 GLN B OE1 
7759 N NE2 . GLN B 502 ? 0.3492 0.4236 0.3667 -0.0470 -0.0941 0.0497  488 GLN B NE2 
7760 N N   . ILE B 503 ? 0.2745 0.3309 0.3042 -0.0241 -0.0645 0.0449  489 ILE B N   
7761 C CA  . ILE B 503 ? 0.2611 0.3151 0.2922 -0.0212 -0.0595 0.0455  489 ILE B CA  
7762 C C   . ILE B 503 ? 0.2528 0.3048 0.2946 -0.0178 -0.0595 0.0509  489 ILE B C   
7763 O O   . ILE B 503 ? 0.2669 0.3161 0.3077 -0.0175 -0.0586 0.0546  489 ILE B O   
7764 C CB  . ILE B 503 ? 0.2558 0.3082 0.2864 -0.0189 -0.0544 0.0388  489 ILE B CB  
7765 C CG1 . ILE B 503 ? 0.2580 0.3124 0.2780 -0.0210 -0.0538 0.0330  489 ILE B CG1 
7766 C CG2 . ILE B 503 ? 0.2432 0.2943 0.2755 -0.0170 -0.0500 0.0397  489 ILE B CG2 
7767 C CD1 . ILE B 503 ? 0.2476 0.3011 0.2674 -0.0176 -0.0494 0.0264  489 ILE B CD1 
7768 N N   . PRO B 504 ? 0.2899 0.3431 0.3421 -0.0154 -0.0601 0.0516  490 PRO B N   
7769 C CA  . PRO B 504 ? 0.2650 0.3173 0.3274 -0.0112 -0.0590 0.0558  490 PRO B CA  
7770 C C   . PRO B 504 ? 0.2809 0.3329 0.3446 -0.0108 -0.0631 0.0628  490 PRO B C   
7771 O O   . PRO B 504 ? 0.2929 0.3393 0.3594 -0.0076 -0.0611 0.0651  490 PRO B O   
7772 C CB  . PRO B 504 ? 0.2596 0.3172 0.3323 -0.0100 -0.0598 0.0559  490 PRO B CB  
7773 C CG  . PRO B 504 ? 0.2553 0.3119 0.3223 -0.0130 -0.0591 0.0503  490 PRO B CG  
7774 C CD  . PRO B 504 ? 0.2577 0.3130 0.3128 -0.0166 -0.0615 0.0487  490 PRO B CD  
7775 N N   . GLN B 505 ? 0.2854 0.3421 0.3459 -0.0142 -0.0693 0.0663  491 GLN B N   
7776 C CA  . GLN B 505 ? 0.2916 0.3479 0.3530 -0.0138 -0.0742 0.0744  491 GLN B CA  
7777 C C   . GLN B 505 ? 0.3061 0.3560 0.3556 -0.0169 -0.0733 0.0759  491 GLN B C   
7778 O O   . GLN B 505 ? 0.3290 0.3752 0.3789 -0.0164 -0.0768 0.0834  491 GLN B O   
7779 C CB  . GLN B 505 ? 0.3567 0.4218 0.4184 -0.0174 -0.0820 0.0788  491 GLN B CB  
7780 C CG  . GLN B 505 ? 0.3606 0.4282 0.4077 -0.0246 -0.0839 0.0746  491 GLN B CG  
7781 C CD  . GLN B 505 ? 0.4568 0.5240 0.4915 -0.0291 -0.0873 0.0793  491 GLN B CD  
7782 O OE1 . GLN B 505 ? 0.4824 0.5494 0.5204 -0.0281 -0.0918 0.0884  491 GLN B OE1 
7783 N NE2 . GLN B 505 ? 0.4095 0.4766 0.4299 -0.0339 -0.0847 0.0735  491 GLN B NE2 
7784 N N   . ALA B 506 ? 0.2936 0.3425 0.3333 -0.0201 -0.0689 0.0697  492 ALA B N   
7785 C CA  . ALA B 506 ? 0.3115 0.3560 0.3416 -0.0234 -0.0670 0.0711  492 ALA B CA  
7786 C C   . ALA B 506 ? 0.2890 0.3253 0.3234 -0.0203 -0.0620 0.0698  492 ALA B C   
7787 O O   . ALA B 506 ? 0.2712 0.3007 0.3014 -0.0223 -0.0621 0.0740  492 ALA B O   
7788 C CB  . ALA B 506 ? 0.2828 0.3327 0.3011 -0.0282 -0.0645 0.0651  492 ALA B CB  
7789 N N   . LEU B 507 ? 0.2883 0.3246 0.3297 -0.0162 -0.0577 0.0642  493 LEU B N   
7790 C CA  . LEU B 507 ? 0.2771 0.3067 0.3208 -0.0142 -0.0527 0.0616  493 LEU B CA  
7791 C C   . LEU B 507 ? 0.2881 0.3117 0.3424 -0.0083 -0.0526 0.0640  493 LEU B C   
7792 O O   . LEU B 507 ? 0.2754 0.2939 0.3322 -0.0059 -0.0480 0.0603  493 LEU B O   
7793 C CB  . LEU B 507 ? 0.2469 0.2807 0.2904 -0.0137 -0.0481 0.0543  493 LEU B CB  
7794 C CG  . LEU B 507 ? 0.2686 0.3086 0.3031 -0.0178 -0.0474 0.0509  493 LEU B CG  
7795 C CD1 . LEU B 507 ? 0.2537 0.2969 0.2893 -0.0163 -0.0433 0.0448  493 LEU B CD1 
7796 C CD2 . LEU B 507 ? 0.2455 0.2848 0.2712 -0.0229 -0.0472 0.0534  493 LEU B CD2 
7797 N N   . SER B 508 ? 0.3061 0.3311 0.3666 -0.0057 -0.0575 0.0699  494 SER B N   
7798 C CA  . SER B 508 ? 0.2928 0.3137 0.3652 0.0013  -0.0575 0.0725  494 SER B CA  
7799 C C   . SER B 508 ? 0.3229 0.3446 0.3990 0.0026  -0.0646 0.0814  494 SER B C   
7800 O O   . SER B 508 ? 0.3256 0.3555 0.3980 -0.0015 -0.0696 0.0845  494 SER B O   
7801 C CB  . SER B 508 ? 0.3186 0.3480 0.4017 0.0056  -0.0546 0.0685  494 SER B CB  
7802 O OG  . SER B 508 ? 0.3378 0.3645 0.4325 0.0130  -0.0526 0.0694  494 SER B OG  
7803 N N   . LEU B 509 ? 0.3113 0.3236 0.3942 0.0083  -0.0653 0.0856  495 LEU B N   
7804 C CA  . LEU B 509 ? 0.3372 0.3508 0.4269 0.0115  -0.0725 0.0951  495 LEU B CA  
7805 C C   . LEU B 509 ? 0.3336 0.3607 0.4394 0.0178  -0.0739 0.0960  495 LEU B C   
7806 O O   . LEU B 509 ? 0.3154 0.3501 0.4269 0.0187  -0.0811 0.1039  495 LEU B O   
7807 C CB  . LEU B 509 ? 0.3393 0.3357 0.4306 0.0160  -0.0730 0.0995  495 LEU B CB  
7808 C CG  . LEU B 509 ? 0.3714 0.3552 0.4467 0.0079  -0.0729 0.1006  495 LEU B CG  
7809 C CD1 . LEU B 509 ? 0.3528 0.3163 0.4292 0.0116  -0.0737 0.1049  495 LEU B CD1 
7810 C CD2 . LEU B 509 ? 0.3782 0.3697 0.4432 -0.0002 -0.0794 0.1074  495 LEU B CD2 
7811 N N   . ASP B 510 ? 0.3234 0.3552 0.4361 0.0211  -0.0674 0.0886  496 ASP B N   
7812 C CA  . ASP B 510 ? 0.3318 0.3781 0.4605 0.0263  -0.0675 0.0891  496 ASP B CA  
7813 C C   . ASP B 510 ? 0.3114 0.3644 0.4386 0.0232  -0.0615 0.0808  496 ASP B C   
7814 O O   . ASP B 510 ? 0.3201 0.3739 0.4541 0.0279  -0.0549 0.0759  496 ASP B O   
7815 C CB  . ASP B 510 ? 0.3291 0.3717 0.4723 0.0373  -0.0650 0.0905  496 ASP B CB  
7816 C CG  . ASP B 510 ? 0.3696 0.4306 0.5316 0.0431  -0.0659 0.0929  496 ASP B CG  
7817 O OD1 . ASP B 510 ? 0.3473 0.4229 0.5112 0.0379  -0.0713 0.0963  496 ASP B OD1 
7818 O OD2 . ASP B 510 ? 0.3488 0.4103 0.5236 0.0525  -0.0609 0.0908  496 ASP B OD2 
7819 N N   . PRO B 511 ? 0.3137 0.3711 0.4312 0.0152  -0.0636 0.0791  497 PRO B N   
7820 C CA  . PRO B 511 ? 0.2900 0.3503 0.4042 0.0121  -0.0584 0.0719  497 PRO B CA  
7821 C C   . PRO B 511 ? 0.3095 0.3824 0.4370 0.0144  -0.0564 0.0712  497 PRO B C   
7822 O O   . PRO B 511 ? 0.3057 0.3787 0.4341 0.0153  -0.0500 0.0661  497 PRO B O   
7823 C CB  . PRO B 511 ? 0.2874 0.3489 0.3896 0.0041  -0.0623 0.0710  497 PRO B CB  
7824 C CG  . PRO B 511 ? 0.3216 0.3827 0.4199 0.0023  -0.0692 0.0774  497 PRO B CG  
7825 C CD  . PRO B 511 ? 0.3281 0.3886 0.4378 0.0091  -0.0712 0.0839  497 PRO B CD  
7826 N N   . GLN B 512 ? 0.3437 0.4285 0.4810 0.0144  -0.0620 0.0766  498 GLN B N   
7827 C CA  . GLN B 512 ? 0.3609 0.4603 0.5112 0.0149  -0.0606 0.0767  498 GLN B CA  
7828 C C   . GLN B 512 ? 0.3072 0.4062 0.4495 0.0079  -0.0581 0.0715  498 GLN B C   
7829 O O   . GLN B 512 ? 0.3176 0.4205 0.4641 0.0085  -0.0524 0.0684  498 GLN B O   
7830 C CB  . GLN B 512 ? 0.3886 0.4909 0.5516 0.0238  -0.0539 0.0755  498 GLN B CB  
7831 C CG  . GLN B 512 ? 0.4169 0.5191 0.5899 0.0319  -0.0572 0.0813  498 GLN B CG  
7832 C CD  . GLN B 512 ? 0.5478 0.6683 0.7349 0.0320  -0.0640 0.0886  498 GLN B CD  
7833 O OE1 . GLN B 512 ? 0.7917 0.9132 0.9791 0.0314  -0.0721 0.0954  498 GLN B OE1 
7834 N NE2 . GLN B 512 ? 0.6339 0.7707 0.8333 0.0321  -0.0607 0.0875  498 GLN B NE2 
7835 N N   . ALA B 513 ? 0.2830 0.3782 0.4142 0.0012  -0.0631 0.0711  499 ALA B N   
7836 C CA  . ALA B 513 ? 0.2849 0.3761 0.4072 -0.0046 -0.0616 0.0661  499 ALA B CA  
7837 C C   . ALA B 513 ? 0.2718 0.3705 0.3956 -0.0114 -0.0680 0.0680  499 ALA B C   
7838 O O   . ALA B 513 ? 0.3034 0.4073 0.4286 -0.0129 -0.0745 0.0723  499 ALA B O   
7839 C CB  . ALA B 513 ? 0.2592 0.3374 0.3656 -0.0062 -0.0605 0.0618  499 ALA B CB  
7840 N N   . GLN B 514 ? 0.2504 0.3489 0.3730 -0.0160 -0.0668 0.0653  500 GLN B N   
7841 C CA  . GLN B 514 ? 0.2415 0.3438 0.3633 -0.0238 -0.0730 0.0660  500 GLN B CA  
7842 C C   . GLN B 514 ? 0.2647 0.3530 0.3710 -0.0278 -0.0734 0.0600  500 GLN B C   
7843 O O   . GLN B 514 ? 0.2215 0.3023 0.3242 -0.0270 -0.0686 0.0565  500 GLN B O   
7844 C CB  . GLN B 514 ? 0.2276 0.3406 0.3615 -0.0267 -0.0717 0.0684  500 GLN B CB  
7845 C CG  . GLN B 514 ? 0.2420 0.3702 0.3927 -0.0204 -0.0687 0.0731  500 GLN B CG  
7846 C CD  . GLN B 514 ? 0.2103 0.3532 0.3738 -0.0243 -0.0673 0.0759  500 GLN B CD  
7847 O OE1 . GLN B 514 ? 0.2435 0.3820 0.4022 -0.0307 -0.0664 0.0742  500 GLN B OE1 
7848 N NE2 . GLN B 514 ? 0.2400 0.4007 0.4202 -0.0203 -0.0672 0.0808  500 GLN B NE2 
7849 N N   . CYS B 515 ? 0.2528 0.3383 0.3502 -0.0320 -0.0790 0.0587  501 CYS B N   
7850 C CA  . CYS B 515 ? 0.2597 0.3324 0.3422 -0.0344 -0.0789 0.0520  501 CYS B CA  
7851 C C   . CYS B 515 ? 0.2711 0.3421 0.3491 -0.0428 -0.0850 0.0498  501 CYS B C   
7852 O O   . CYS B 515 ? 0.2443 0.3249 0.3264 -0.0473 -0.0911 0.0538  501 CYS B O   
7853 C CB  . CYS B 515 ? 0.2804 0.3496 0.3527 -0.0318 -0.0786 0.0505  501 CYS B CB  
7854 S SG  . CYS B 515 ? 0.3086 0.3766 0.3839 -0.0236 -0.0718 0.0522  501 CYS B SG  
7855 N N   . TRP B 516 ? 0.2575 0.3161 0.3274 -0.0448 -0.0838 0.0437  502 TRP B N   
7856 C CA  . TRP B 516 ? 0.2773 0.3296 0.3399 -0.0528 -0.0893 0.0398  502 TRP B CA  
7857 C C   . TRP B 516 ? 0.3161 0.3530 0.3646 -0.0509 -0.0869 0.0309  502 TRP B C   
7858 O O   . TRP B 516 ? 0.2865 0.3178 0.3345 -0.0444 -0.0810 0.0290  502 TRP B O   
7859 C CB  . TRP B 516 ? 0.2578 0.3086 0.3277 -0.0584 -0.0908 0.0417  502 TRP B CB  
7860 C CG  . TRP B 516 ? 0.2590 0.3267 0.3440 -0.0620 -0.0934 0.0498  502 TRP B CG  
7861 C CD1 . TRP B 516 ? 0.2815 0.3574 0.3702 -0.0712 -0.1006 0.0526  502 TRP B CD1 
7862 C CD2 . TRP B 516 ? 0.2584 0.3378 0.3572 -0.0567 -0.0885 0.0557  502 TRP B CD2 
7863 N NE1 . TRP B 516 ? 0.2523 0.3463 0.3579 -0.0712 -0.1003 0.0604  502 TRP B NE1 
7864 C CE2 . TRP B 516 ? 0.2635 0.3593 0.3752 -0.0620 -0.0924 0.0619  502 TRP B CE2 
7865 C CE3 . TRP B 516 ? 0.2448 0.3230 0.3461 -0.0482 -0.0810 0.0558  502 TRP B CE3 
7866 C CZ2 . TRP B 516 ? 0.2625 0.3738 0.3899 -0.0580 -0.0883 0.0678  502 TRP B CZ2 
7867 C CZ3 . TRP B 516 ? 0.2269 0.3185 0.3419 -0.0450 -0.0772 0.0611  502 TRP B CZ3 
7868 C CH2 . TRP B 516 ? 0.2310 0.3391 0.3591 -0.0493 -0.0805 0.0668  502 TRP B CH2 
7869 N N   . ARG B 517 ? 0.3239 0.3549 0.3614 -0.0568 -0.0915 0.0254  503 ARG B N   
7870 C CA  . ARG B 517 ? 0.3413 0.3563 0.3662 -0.0559 -0.0898 0.0156  503 ARG B CA  
7871 C C   . ARG B 517 ? 0.3259 0.3300 0.3492 -0.0638 -0.0946 0.0129  503 ARG B C   
7872 O O   . ARG B 517 ? 0.3051 0.3143 0.3277 -0.0726 -0.1011 0.0144  503 ARG B O   
7873 C CB  . ARG B 517 ? 0.3861 0.4023 0.3972 -0.0564 -0.0905 0.0099  503 ARG B CB  
7874 C CG  . ARG B 517 ? 0.4379 0.4398 0.4366 -0.0536 -0.0872 -0.0013 503 ARG B CG  
7875 C CD  . ARG B 517 ? 0.5008 0.5090 0.4880 -0.0521 -0.0852 -0.0053 503 ARG B CD  
7876 N NE  . ARG B 517 ? 0.6145 0.6203 0.5877 -0.0599 -0.0900 -0.0117 503 ARG B NE  
7877 C CZ  . ARG B 517 ? 0.7560 0.7561 0.7147 -0.0588 -0.0872 -0.0223 503 ARG B CZ  
7878 N NH1 . ARG B 517 ? 0.7613 0.7586 0.7189 -0.0499 -0.0796 -0.0273 503 ARG B NH1 
7879 N NH2 . ARG B 517 ? 0.7411 0.7395 0.6860 -0.0671 -0.0919 -0.0283 503 ARG B NH2 
7880 N N   . VAL B 518 ? 0.3535 0.3427 0.3766 -0.0613 -0.0920 0.0097  504 VAL B N   
7881 C CA  . VAL B 518 ? 0.3708 0.3468 0.3926 -0.0692 -0.0966 0.0082  504 VAL B CA  
7882 C C   . VAL B 518 ? 0.3926 0.3467 0.4024 -0.0661 -0.0953 -0.0026 504 VAL B C   
7883 O O   . VAL B 518 ? 0.3891 0.3392 0.3974 -0.0561 -0.0895 -0.0058 504 VAL B O   
7884 C CB  . VAL B 518 ? 0.3661 0.3442 0.4011 -0.0704 -0.0958 0.0168  504 VAL B CB  
7885 C CG1 . VAL B 518 ? 0.3267 0.3274 0.3744 -0.0732 -0.0969 0.0262  504 VAL B CG1 
7886 C CG2 . VAL B 518 ? 0.3275 0.3007 0.3654 -0.0601 -0.0890 0.0175  504 VAL B CG2 
7887 N N   . SER B 519 ? 0.4090 0.3493 0.4102 -0.0747 -0.1008 -0.0084 505 SER B N   
7888 C CA  . SER B 519 ? 0.4320 0.3485 0.4218 -0.0720 -0.1000 -0.0196 505 SER B CA  
7889 C C   . SER B 519 ? 0.4700 0.3665 0.4600 -0.0796 -0.1048 -0.0193 505 SER B C   
7890 O O   . SER B 519 ? 0.4698 0.3429 0.4516 -0.0766 -0.1043 -0.0279 505 SER B O   
7891 C CB  . SER B 519 ? 0.4554 0.3693 0.4293 -0.0751 -0.1017 -0.0306 505 SER B CB  
7892 O OG  . SER B 519 ? 0.4872 0.4077 0.4587 -0.0884 -0.1094 -0.0284 505 SER B OG  
7893 N N   . GLU B 520 ? 0.4740 0.3790 0.4734 -0.0892 -0.1092 -0.0096 506 GLU B N   
7894 C CA  . GLU B 520 ? 0.4822 0.3702 0.4818 -0.0992 -0.1145 -0.0079 506 GLU B CA  
7895 C C   . GLU B 520 ? 0.4849 0.3800 0.4989 -0.0986 -0.1125 0.0045  506 GLU B C   
7896 O O   . GLU B 520 ? 0.4494 0.3680 0.4743 -0.0955 -0.1093 0.0124  506 GLU B O   
7897 C CB  . GLU B 520 ? 0.4987 0.3927 0.4956 -0.1148 -0.1225 -0.0075 506 GLU B CB  
7898 C CG  . GLU B 520 ? 0.4967 0.3926 0.4798 -0.1170 -0.1249 -0.0175 506 GLU B CG  
7899 C CD  . GLU B 520 ? 0.5421 0.4114 0.5090 -0.1123 -0.1232 -0.0321 506 GLU B CD  
7900 O OE1 . GLU B 520 ? 0.5874 0.4311 0.5494 -0.1169 -0.1261 -0.0363 506 GLU B OE1 
7901 O OE2 . GLU B 520 ? 0.5610 0.4345 0.5198 -0.1040 -0.1187 -0.0395 506 GLU B OE2 
7902 N N   . ALA B 521 ? 0.4941 0.3678 0.5074 -0.1017 -0.1144 0.0059  507 ALA B N   
7903 C CA  . ALA B 521 ? 0.4889 0.3684 0.5140 -0.1031 -0.1130 0.0179  507 ALA B CA  
7904 C C   . ALA B 521 ? 0.4787 0.3831 0.5147 -0.1140 -0.1154 0.0274  507 ALA B C   
7905 O O   . ALA B 521 ? 0.4400 0.3632 0.4874 -0.1111 -0.1113 0.0365  507 ALA B O   
7906 C CB  . ALA B 521 ? 0.5336 0.3840 0.5543 -0.1074 -0.1164 0.0184  507 ALA B CB  
7907 N N   . GLU B 522 ? 0.4827 0.3885 0.5154 -0.1264 -0.1221 0.0252  508 GLU B N   
7908 C CA  . GLU B 522 ? 0.4814 0.4127 0.5263 -0.1369 -0.1250 0.0346  508 GLU B CA  
7909 C C   . GLU B 522 ? 0.4433 0.4037 0.4972 -0.1287 -0.1208 0.0377  508 GLU B C   
7910 O O   . GLU B 522 ? 0.4149 0.3976 0.4830 -0.1293 -0.1184 0.0472  508 GLU B O   
7911 C CB  . GLU B 522 ? 0.4777 0.4056 0.5169 -0.1524 -0.1339 0.0314  508 GLU B CB  
7912 C CG  . GLU B 522 ? 0.6045 0.4977 0.6292 -0.1583 -0.1383 0.0231  508 GLU B CG  
7913 C CD  . GLU B 522 ? 0.5998 0.4770 0.6089 -0.1502 -0.1375 0.0091  508 GLU B CD  
7914 O OE1 . GLU B 522 ? 0.6179 0.4714 0.6200 -0.1408 -0.1339 0.0031  508 GLU B OE1 
7915 O OE2 . GLU B 522 ? 0.5773 0.4662 0.5812 -0.1535 -0.1405 0.0042  508 GLU B OE2 
7916 N N   . GLN B 523 ? 0.4032 0.3632 0.4489 -0.1209 -0.1196 0.0299  509 GLN B N   
7917 C CA  . GLN B 523 ? 0.3920 0.3761 0.4453 -0.1126 -0.1158 0.0332  509 GLN B CA  
7918 C C   . GLN B 523 ? 0.3733 0.3634 0.4352 -0.1019 -0.1078 0.0385  509 GLN B C   
7919 O O   . GLN B 523 ? 0.3349 0.3470 0.4089 -0.0989 -0.1049 0.0453  509 GLN B O   
7920 C CB  . GLN B 523 ? 0.3969 0.3774 0.4381 -0.1064 -0.1154 0.0243  509 GLN B CB  
7921 C CG  . GLN B 523 ? 0.4632 0.4340 0.4913 -0.1159 -0.1225 0.0165  509 GLN B CG  
7922 C CD  . GLN B 523 ? 0.4592 0.4253 0.4738 -0.1086 -0.1202 0.0071  509 GLN B CD  
7923 O OE1 . GLN B 523 ? 0.4408 0.3970 0.4515 -0.0977 -0.1138 0.0026  509 GLN B OE1 
7924 N NE2 . GLN B 523 ? 0.4451 0.4195 0.4523 -0.1152 -0.1257 0.0044  509 GLN B NE2 
7925 N N   . LEU B 524 ? 0.3617 0.3324 0.4172 -0.0954 -0.1042 0.0349  510 LEU B N   
7926 C CA  . LEU B 524 ? 0.3521 0.3281 0.4142 -0.0862 -0.0972 0.0396  510 LEU B CA  
7927 C C   . LEU B 524 ? 0.3501 0.3376 0.4239 -0.0924 -0.0965 0.0497  510 LEU B C   
7928 O O   . LEU B 524 ? 0.3119 0.3171 0.3949 -0.0874 -0.0913 0.0550  510 LEU B O   
7929 C CB  . LEU B 524 ? 0.3498 0.3034 0.4034 -0.0788 -0.0948 0.0345  510 LEU B CB  
7930 C CG  . LEU B 524 ? 0.3642 0.3222 0.4232 -0.0703 -0.0885 0.0396  510 LEU B CG  
7931 C CD1 . LEU B 524 ? 0.2997 0.2772 0.3631 -0.0622 -0.0833 0.0400  510 LEU B CD1 
7932 C CD2 . LEU B 524 ? 0.3414 0.2785 0.3934 -0.0632 -0.0873 0.0357  510 LEU B CD2 
7933 N N   . ALA B 525 ? 0.3751 0.3523 0.4481 -0.1037 -0.1014 0.0523  511 ALA B N   
7934 C CA  . ALA B 525 ? 0.3646 0.3547 0.4484 -0.1114 -0.1007 0.0623  511 ALA B CA  
7935 C C   . ALA B 525 ? 0.3541 0.3745 0.4509 -0.1133 -0.0998 0.0671  511 ALA B C   
7936 O O   . ALA B 525 ? 0.3264 0.3651 0.4338 -0.1106 -0.0944 0.0735  511 ALA B O   
7937 C CB  . ALA B 525 ? 0.3783 0.3523 0.4584 -0.1254 -0.1073 0.0643  511 ALA B CB  
7938 N N   . ASP B 526 ? 0.3439 0.3704 0.4401 -0.1173 -0.1051 0.0638  512 ASP B N   
7939 C CA  . ASP B 526 ? 0.3520 0.4073 0.4616 -0.1184 -0.1056 0.0688  512 ASP B CA  
7940 C C   . ASP B 526 ? 0.3238 0.3921 0.4388 -0.1044 -0.0985 0.0690  512 ASP B C   
7941 O O   . ASP B 526 ? 0.3188 0.4084 0.4474 -0.1019 -0.0943 0.0750  512 ASP B O   
7942 C CB  . ASP B 526 ? 0.3710 0.4276 0.4762 -0.1253 -0.1138 0.0650  512 ASP B CB  
7943 C CG  . ASP B 526 ? 0.3837 0.4697 0.5026 -0.1242 -0.1151 0.0702  512 ASP B CG  
7944 O OD1 . ASP B 526 ? 0.3842 0.4911 0.5182 -0.1298 -0.1151 0.0780  512 ASP B OD1 
7945 O OD2 . ASP B 526 ? 0.4086 0.4971 0.5233 -0.1177 -0.1162 0.0668  512 ASP B OD2 
7946 N N   . VAL B 527 ? 0.2924 0.3477 0.3968 -0.0952 -0.0967 0.0622  513 VAL B N   
7947 C CA  . VAL B 527 ? 0.2932 0.3576 0.4009 -0.0829 -0.0905 0.0620  513 VAL B CA  
7948 C C   . VAL B 527 ? 0.2894 0.3574 0.4028 -0.0783 -0.0831 0.0659  513 VAL B C   
7949 O O   . VAL B 527 ? 0.2602 0.3445 0.3830 -0.0721 -0.0781 0.0689  513 VAL B O   
7950 C CB  . VAL B 527 ? 0.2926 0.3414 0.3867 -0.0757 -0.0899 0.0541  513 VAL B CB  
7951 C CG1 . VAL B 527 ? 0.2589 0.3138 0.3554 -0.0641 -0.0830 0.0543  513 VAL B CG1 
7952 C CG2 . VAL B 527 ? 0.3104 0.3603 0.3988 -0.0796 -0.0963 0.0507  513 VAL B CG2 
7953 N N   . LEU B 528 ? 0.2783 0.3304 0.3853 -0.0809 -0.0824 0.0657  514 LEU B N   
7954 C CA  . LEU B 528 ? 0.2928 0.3484 0.4032 -0.0778 -0.0761 0.0698  514 LEU B CA  
7955 C C   . LEU B 528 ? 0.2941 0.3723 0.4183 -0.0831 -0.0738 0.0771  514 LEU B C   
7956 O O   . LEU B 528 ? 0.2674 0.3585 0.3975 -0.0774 -0.0670 0.0793  514 LEU B O   
7957 C CB  . LEU B 528 ? 0.2832 0.3173 0.3844 -0.0806 -0.0774 0.0697  514 LEU B CB  
7958 C CG  . LEU B 528 ? 0.2981 0.3148 0.3884 -0.0713 -0.0766 0.0625  514 LEU B CG  
7959 C CD1 . LEU B 528 ? 0.3131 0.3068 0.3951 -0.0729 -0.0790 0.0620  514 LEU B CD1 
7960 C CD2 . LEU B 528 ? 0.2878 0.3141 0.3799 -0.0612 -0.0697 0.0623  514 LEU B CD2 
7961 N N   . GLU B 529 ? 0.2986 0.3828 0.4280 -0.0942 -0.0793 0.0806  515 GLU B N   
7962 C CA  . GLU B 529 ? 0.3009 0.4111 0.4456 -0.0991 -0.0771 0.0876  515 GLU B CA  
7963 C C   . GLU B 529 ? 0.2633 0.3942 0.4189 -0.0895 -0.0734 0.0871  515 GLU B C   
7964 O O   . GLU B 529 ? 0.2455 0.3947 0.4115 -0.0858 -0.0667 0.0903  515 GLU B O   
7965 C CB  . GLU B 529 ? 0.3682 0.4827 0.5171 -0.1133 -0.0846 0.0912  515 GLU B CB  
7966 C CG  . GLU B 529 ? 0.4750 0.5690 0.6147 -0.1243 -0.0884 0.0930  515 GLU B CG  
7967 C CD  . GLU B 529 ? 0.6730 0.7700 0.8158 -0.1397 -0.0966 0.0958  515 GLU B CD  
7968 O OE1 . GLU B 529 ? 0.6453 0.7218 0.7794 -0.1498 -0.1012 0.0966  515 GLU B OE1 
7969 O OE2 . GLU B 529 ? 0.6292 0.7486 0.7831 -0.1417 -0.0989 0.0975  515 GLU B OE2 
7970 N N   . LYS B 530 ? 0.2747 0.4021 0.4273 -0.0852 -0.0777 0.0830  516 LYS B N   
7971 C CA  . LYS B 530 ? 0.2604 0.4049 0.4231 -0.0761 -0.0755 0.0834  516 LYS B CA  
7972 C C   . LYS B 530 ? 0.2508 0.3937 0.4122 -0.0641 -0.0670 0.0809  516 LYS B C   
7973 O O   . LYS B 530 ? 0.2487 0.4081 0.4217 -0.0571 -0.0627 0.0826  516 LYS B O   
7974 C CB  . LYS B 530 ? 0.2612 0.4005 0.4184 -0.0753 -0.0825 0.0804  516 LYS B CB  
7975 C CG  . LYS B 530 ? 0.3085 0.4422 0.4607 -0.0878 -0.0915 0.0803  516 LYS B CG  
7976 C CD  . LYS B 530 ? 0.3177 0.4678 0.4776 -0.0900 -0.0982 0.0830  516 LYS B CD  
7977 C CE  . LYS B 530 ? 0.3269 0.4752 0.4834 -0.1047 -0.1073 0.0834  516 LYS B CE  
7978 N NZ  . LYS B 530 ? 0.3117 0.4618 0.4630 -0.1062 -0.1150 0.0818  516 LYS B NZ  
7979 N N   . VAL B 531 ? 0.2532 0.3762 0.4010 -0.0609 -0.0648 0.0765  517 VAL B N   
7980 C CA  . VAL B 531 ? 0.2306 0.3518 0.3761 -0.0508 -0.0576 0.0738  517 VAL B CA  
7981 C C   . VAL B 531 ? 0.2413 0.3654 0.3872 -0.0518 -0.0511 0.0759  517 VAL B C   
7982 O O   . VAL B 531 ? 0.2320 0.3540 0.3743 -0.0449 -0.0451 0.0734  517 VAL B O   
7983 C CB  . VAL B 531 ? 0.2673 0.3690 0.3986 -0.0459 -0.0587 0.0681  517 VAL B CB  
7984 C CG1 . VAL B 531 ? 0.2434 0.3434 0.3726 -0.0455 -0.0647 0.0662  517 VAL B CG1 
7985 C CG2 . VAL B 531 ? 0.2303 0.3147 0.3507 -0.0504 -0.0603 0.0665  517 VAL B CG2 
7986 N N   . ALA B 532 ? 0.2559 0.3864 0.4061 -0.0613 -0.0522 0.0808  518 ALA B N   
7987 C CA  . ALA B 532 ? 0.2584 0.3902 0.4064 -0.0641 -0.0469 0.0837  518 ALA B CA  
7988 C C   . ALA B 532 ? 0.2434 0.3902 0.3971 -0.0566 -0.0378 0.0827  518 ALA B C   
7989 O O   . ALA B 532 ? 0.2624 0.4054 0.4090 -0.0556 -0.0329 0.0824  518 ALA B O   
7990 C CB  . ALA B 532 ? 0.2341 0.3742 0.3877 -0.0766 -0.0495 0.0903  518 ALA B CB  
7991 N N   . HIS B 533 ? 0.2522 0.4159 0.4184 -0.0514 -0.0357 0.0823  519 HIS B N   
7992 C CA  . HIS B 533 ? 0.2481 0.4255 0.4205 -0.0438 -0.0266 0.0804  519 HIS B CA  
7993 C C   . HIS B 533 ? 0.2466 0.4146 0.4149 -0.0325 -0.0247 0.0743  519 HIS B C   
7994 O O   . HIS B 533 ? 0.2204 0.3974 0.3940 -0.0251 -0.0177 0.0716  519 HIS B O   
7995 C CB  . HIS B 533 ? 0.2648 0.4685 0.4558 -0.0442 -0.0245 0.0840  519 HIS B CB  
7996 C CG  . HIS B 533 ? 0.2776 0.4933 0.4737 -0.0566 -0.0259 0.0905  519 HIS B CG  
7997 N ND1 . HIS B 533 ? 0.3137 0.5391 0.5089 -0.0614 -0.0192 0.0931  519 HIS B ND1 
7998 C CD2 . HIS B 533 ? 0.2735 0.4931 0.4748 -0.0663 -0.0336 0.0954  519 HIS B CD2 
7999 C CE1 . HIS B 533 ? 0.2992 0.5334 0.4991 -0.0737 -0.0226 0.0998  519 HIS B CE1 
8000 N NE2 . HIS B 533 ? 0.2676 0.4981 0.4714 -0.0770 -0.0315 0.1010  519 HIS B NE2 
8001 N N   . HIS B 534 ? 0.2340 0.3840 0.3927 -0.0315 -0.0306 0.0720  520 HIS B N   
8002 C CA  . HIS B 534 ? 0.2410 0.3788 0.3922 -0.0232 -0.0293 0.0668  520 HIS B CA  
8003 C C   . HIS B 534 ? 0.2362 0.3837 0.3971 -0.0142 -0.0248 0.0650  520 HIS B C   
8004 O O   . HIS B 534 ? 0.2341 0.3778 0.3910 -0.0084 -0.0188 0.0608  520 HIS B O   
8005 C CB  . HIS B 534 ? 0.2365 0.3627 0.3746 -0.0233 -0.0257 0.0640  520 HIS B CB  
8006 C CG  . HIS B 534 ? 0.2402 0.3771 0.3799 -0.0241 -0.0182 0.0645  520 HIS B CG  
8007 N ND1 . HIS B 534 ? 0.2528 0.3947 0.3938 -0.0172 -0.0110 0.0603  520 HIS B ND1 
8008 C CD2 . HIS B 534 ? 0.2331 0.3768 0.3727 -0.0314 -0.0166 0.0687  520 HIS B CD2 
8009 C CE1 . HIS B 534 ? 0.2336 0.3860 0.3746 -0.0202 -0.0048 0.0612  520 HIS B CE1 
8010 N NE2 . HIS B 534 ? 0.2441 0.3985 0.3844 -0.0290 -0.0082 0.0669  520 HIS B NE2 
8011 N N   . GLU B 535 ? 0.2352 0.3947 0.4090 -0.0130 -0.0281 0.0683  521 GLU B N   
8012 C CA  . GLU B 535 ? 0.2554 0.4233 0.4404 -0.0033 -0.0250 0.0675  521 GLU B CA  
8013 C C   . GLU B 535 ? 0.2297 0.3823 0.4081 0.0024  -0.0286 0.0654  521 GLU B C   
8014 O O   . GLU B 535 ? 0.2043 0.3579 0.3889 0.0112  -0.0259 0.0642  521 GLU B O   
8015 C CB  . GLU B 535 ? 0.2466 0.4357 0.4498 -0.0039 -0.0279 0.0730  521 GLU B CB  
8016 C CG  . GLU B 535 ? 0.2535 0.4596 0.4636 -0.0116 -0.0248 0.0760  521 GLU B CG  
8017 C CD  . GLU B 535 ? 0.3406 0.5725 0.5717 -0.0105 -0.0254 0.0810  521 GLU B CD  
8018 O OE1 . GLU B 535 ? 0.3317 0.5696 0.5736 -0.0003 -0.0250 0.0808  521 GLU B OE1 
8019 O OE2 . GLU B 535 ? 0.4555 0.7018 0.6928 -0.0200 -0.0266 0.0854  521 GLU B OE2 
8020 N N   . ARG B 536 ? 0.2506 0.3894 0.4167 -0.0024 -0.0346 0.0651  522 ARG B N   
8021 C CA  . ARG B 536 ? 0.2324 0.3572 0.3900 0.0011  -0.0377 0.0634  522 ARG B CA  
8022 C C   . ARG B 536 ? 0.2488 0.3587 0.3904 -0.0032 -0.0381 0.0599  522 ARG B C   
8023 O O   . ARG B 536 ? 0.2488 0.3584 0.3869 -0.0091 -0.0381 0.0599  522 ARG B O   
8024 C CB  . ARG B 536 ? 0.2331 0.3611 0.3948 -0.0001 -0.0461 0.0678  522 ARG B CB  
8025 C CG  . ARG B 536 ? 0.2496 0.3954 0.4294 0.0039  -0.0469 0.0725  522 ARG B CG  
8026 C CD  . ARG B 536 ? 0.3054 0.4491 0.4913 0.0146  -0.0445 0.0726  522 ARG B CD  
8027 N NE  . ARG B 536 ? 0.3243 0.4866 0.5296 0.0196  -0.0458 0.0777  522 ARG B NE  
8028 C CZ  . ARG B 536 ? 0.3412 0.5197 0.5601 0.0226  -0.0396 0.0774  522 ARG B CZ  
8029 N NH1 . ARG B 536 ? 0.3126 0.4904 0.5265 0.0203  -0.0319 0.0726  522 ARG B NH1 
8030 N NH2 . ARG B 536 ? 0.3398 0.5376 0.5780 0.0274  -0.0414 0.0825  522 ARG B NH2 
8031 N N   . LEU B 537 ? 0.2360 0.3337 0.3684 -0.0004 -0.0386 0.0573  523 LEU B N   
8032 C CA  . LEU B 537 ? 0.2236 0.3097 0.3424 -0.0042 -0.0403 0.0546  523 LEU B CA  
8033 C C   . LEU B 537 ? 0.2548 0.3406 0.3716 -0.0097 -0.0472 0.0562  523 LEU B C   
8034 O O   . LEU B 537 ? 0.2017 0.2926 0.3232 -0.0099 -0.0520 0.0592  523 LEU B O   
8035 C CB  . LEU B 537 ? 0.2305 0.3063 0.3409 -0.0009 -0.0396 0.0521  523 LEU B CB  
8036 C CG  . LEU B 537 ? 0.2155 0.2820 0.3132 -0.0038 -0.0405 0.0489  523 LEU B CG  
8037 C CD1 . LEU B 537 ? 0.2061 0.2661 0.2973 -0.0012 -0.0364 0.0460  523 LEU B CD1 
8038 C CD2 . LEU B 537 ? 0.2095 0.2732 0.3019 -0.0065 -0.0464 0.0495  523 LEU B CD2 
8039 N N   . SER B 538 ? 0.2343 0.3141 0.3441 -0.0142 -0.0481 0.0543  524 SER B N   
8040 C CA  . SER B 538 ? 0.2374 0.3139 0.3431 -0.0196 -0.0544 0.0542  524 SER B CA  
8041 C C   . SER B 538 ? 0.2456 0.3095 0.3386 -0.0196 -0.0546 0.0495  524 SER B C   
8042 O O   . SER B 538 ? 0.2285 0.2876 0.3176 -0.0172 -0.0505 0.0475  524 SER B O   
8043 C CB  . SER B 538 ? 0.2214 0.3025 0.3327 -0.0258 -0.0562 0.0567  524 SER B CB  
8044 O OG  . SER B 538 ? 0.2726 0.3492 0.3812 -0.0266 -0.0524 0.0561  524 SER B OG  
8045 N N   . LEU B 539 ? 0.2298 0.2898 0.3163 -0.0218 -0.0593 0.0476  525 LEU B N   
8046 C CA  . LEU B 539 ? 0.2441 0.2938 0.3193 -0.0217 -0.0594 0.0423  525 LEU B CA  
8047 C C   . LEU B 539 ? 0.2488 0.2934 0.3197 -0.0273 -0.0647 0.0400  525 LEU B C   
8048 O O   . LEU B 539 ? 0.2429 0.2917 0.3134 -0.0309 -0.0693 0.0411  525 LEU B O   
8049 C CB  . LEU B 539 ? 0.2304 0.2798 0.2990 -0.0189 -0.0586 0.0406  525 LEU B CB  
8050 C CG  . LEU B 539 ? 0.2332 0.2755 0.2916 -0.0173 -0.0568 0.0350  525 LEU B CG  
8051 C CD1 . LEU B 539 ? 0.2231 0.2679 0.2780 -0.0145 -0.0539 0.0351  525 LEU B CD1 
8052 C CD2 . LEU B 539 ? 0.2205 0.2585 0.2707 -0.0208 -0.0608 0.0306  525 LEU B CD2 
8053 N N   . ILE B 540 ? 0.2207 0.2557 0.2881 -0.0283 -0.0644 0.0372  526 ILE B N   
8054 C CA  . ILE B 540 ? 0.2421 0.2684 0.3046 -0.0338 -0.0692 0.0340  526 ILE B CA  
8055 C C   . ILE B 540 ? 0.2658 0.2810 0.3174 -0.0304 -0.0681 0.0266  526 ILE B C   
8056 O O   . ILE B 540 ? 0.2566 0.2656 0.3074 -0.0257 -0.0648 0.0251  526 ILE B O   
8057 C CB  . ILE B 540 ? 0.2508 0.2728 0.3183 -0.0380 -0.0702 0.0371  526 ILE B CB  
8058 C CG1 . ILE B 540 ? 0.2461 0.2827 0.3257 -0.0402 -0.0694 0.0442  526 ILE B CG1 
8059 C CG2 . ILE B 540 ? 0.2722 0.2831 0.3341 -0.0450 -0.0759 0.0337  526 ILE B CG2 
8060 C CD1 . ILE B 540 ? 0.2754 0.3105 0.3599 -0.0446 -0.0691 0.0483  526 ILE B CD1 
8061 N N   . GLU B 541 ? 0.2579 0.2720 0.3014 -0.0325 -0.0708 0.0221  527 GLU B N   
8062 C CA  . GLU B 541 ? 0.2832 0.2882 0.3162 -0.0294 -0.0694 0.0139  527 GLU B CA  
8063 C C   . GLU B 541 ? 0.3245 0.3146 0.3533 -0.0331 -0.0728 0.0092  527 GLU B C   
8064 O O   . GLU B 541 ? 0.3164 0.3044 0.3415 -0.0405 -0.0780 0.0078  527 GLU B O   
8065 C CB  . GLU B 541 ? 0.2999 0.3112 0.3244 -0.0306 -0.0702 0.0109  527 GLU B CB  
8066 C CG  . GLU B 541 ? 0.3265 0.3303 0.3395 -0.0280 -0.0681 0.0012  527 GLU B CG  
8067 C CD  . GLU B 541 ? 0.3578 0.3696 0.3610 -0.0304 -0.0686 -0.0012 527 GLU B CD  
8068 O OE1 . GLU B 541 ? 0.3212 0.3412 0.3252 -0.0356 -0.0727 0.0043  527 GLU B OE1 
8069 O OE2 . GLU B 541 ? 0.3348 0.3455 0.3296 -0.0270 -0.0649 -0.0084 527 GLU B OE2 
8070 N N   . VAL B 542 ? 0.3115 0.2907 0.3408 -0.0283 -0.0705 0.0070  528 VAL B N   
8071 C CA  . VAL B 542 ? 0.3168 0.2783 0.3429 -0.0311 -0.0738 0.0036  528 VAL B CA  
8072 C C   . VAL B 542 ? 0.3515 0.3020 0.3669 -0.0269 -0.0726 -0.0073 528 VAL B C   
8073 O O   . VAL B 542 ? 0.3474 0.2976 0.3628 -0.0180 -0.0680 -0.0103 528 VAL B O   
8074 C CB  . VAL B 542 ? 0.3198 0.2746 0.3530 -0.0283 -0.0726 0.0088  528 VAL B CB  
8075 C CG1 . VAL B 542 ? 0.3325 0.2666 0.3621 -0.0322 -0.0769 0.0062  528 VAL B CG1 
8076 C CG2 . VAL B 542 ? 0.3050 0.2733 0.3481 -0.0317 -0.0721 0.0188  528 VAL B CG2 
8077 N N   . MET B 543 ? 0.3688 0.3109 0.3753 -0.0333 -0.0768 -0.0136 529 MET B N   
8078 C CA  . MET B 543 ? 0.3908 0.3230 0.3854 -0.0298 -0.0752 -0.0257 529 MET B CA  
8079 C C   . MET B 543 ? 0.4281 0.3378 0.4219 -0.0258 -0.0756 -0.0306 529 MET B C   
8080 O O   . MET B 543 ? 0.4328 0.3276 0.4253 -0.0330 -0.0808 -0.0303 529 MET B O   
8081 C CB  . MET B 543 ? 0.4211 0.3533 0.4050 -0.0394 -0.0800 -0.0307 529 MET B CB  
8082 C CG  . MET B 543 ? 0.4321 0.3848 0.4136 -0.0424 -0.0799 -0.0277 529 MET B CG  
8083 S SD  . MET B 543 ? 0.4708 0.4406 0.4554 -0.0330 -0.0725 -0.0250 529 MET B SD  
8084 C CE  . MET B 543 ? 0.4881 0.4480 0.4633 -0.0242 -0.0665 -0.0384 529 MET B CE  
8085 N N   . LEU B 544 ? 0.4836 0.3903 0.4783 -0.0144 -0.0704 -0.0349 530 LEU B N   
8086 C CA  . LEU B 544 ? 0.4930 0.3782 0.4886 -0.0084 -0.0708 -0.0383 530 LEU B CA  
8087 C C   . LEU B 544 ? 0.5437 0.4208 0.5310 0.0002  -0.0668 -0.0520 530 LEU B C   
8088 O O   . LEU B 544 ? 0.5329 0.4259 0.5164 0.0035  -0.0620 -0.0567 530 LEU B O   
8089 C CB  . LEU B 544 ? 0.4657 0.3553 0.4734 -0.0013 -0.0688 -0.0289 530 LEU B CB  
8090 C CG  . LEU B 544 ? 0.4427 0.3353 0.4580 -0.0096 -0.0726 -0.0165 530 LEU B CG  
8091 C CD1 . LEU B 544 ? 0.4082 0.3130 0.4335 -0.0038 -0.0695 -0.0072 530 LEU B CD1 
8092 C CD2 . LEU B 544 ? 0.4774 0.3467 0.4911 -0.0155 -0.0782 -0.0156 530 LEU B CD2 
8093 N N   . PRO B 545 ? 0.5595 0.4117 0.5435 0.0036  -0.0685 -0.0589 531 PRO B N   
8094 C CA  . PRO B 545 ? 0.6047 0.4482 0.5810 0.0129  -0.0640 -0.0734 531 PRO B CA  
8095 C C   . PRO B 545 ? 0.6426 0.5001 0.6274 0.0272  -0.0571 -0.0733 531 PRO B C   
8096 O O   . PRO B 545 ? 0.6406 0.5037 0.6375 0.0318  -0.0572 -0.0630 531 PRO B O   
8097 C CB  . PRO B 545 ? 0.6184 0.4290 0.5914 0.0136  -0.0683 -0.0787 531 PRO B CB  
8098 C CG  . PRO B 545 ? 0.6082 0.4113 0.5838 0.0007  -0.0757 -0.0679 531 PRO B CG  
8099 C CD  . PRO B 545 ? 0.5733 0.4032 0.5587 -0.0029 -0.0750 -0.0544 531 PRO B CD  
8100 N N   . LYS B 546 ? 0.6650 0.5294 0.6430 0.0336  -0.0511 -0.0853 532 LYS B N   
8101 C CA  . LYS B 546 ? 0.6668 0.5504 0.6530 0.0457  -0.0441 -0.0854 532 LYS B CA  
8102 C C   . LYS B 546 ? 0.7119 0.5834 0.7094 0.0590  -0.0436 -0.0842 532 LYS B C   
8103 O O   . LYS B 546 ? 0.7061 0.5931 0.7156 0.0655  -0.0416 -0.0759 532 LYS B O   
8104 C CB  . LYS B 546 ? 0.7043 0.5984 0.6801 0.0489  -0.0375 -0.0990 532 LYS B CB  
8105 C CG  . LYS B 546 ? 0.7317 0.6460 0.7161 0.0615  -0.0297 -0.1007 532 LYS B CG  
8106 C CD  . LYS B 546 ? 0.7562 0.6862 0.7295 0.0617  -0.0227 -0.1122 532 LYS B CD  
8107 C CE  . LYS B 546 ? 0.7209 0.6708 0.6878 0.0487  -0.0238 -0.1051 532 LYS B CE  
8108 N NZ  . LYS B 546 ? 0.7872 0.7557 0.7435 0.0481  -0.0169 -0.1140 532 LYS B NZ  
8109 N N   . ALA B 547 ? 0.7248 0.5678 0.7185 0.0629  -0.0460 -0.0920 533 ALA B N   
8110 C CA  . ALA B 547 ? 0.7574 0.5867 0.7615 0.0769  -0.0459 -0.0914 533 ALA B CA  
8111 C C   . ALA B 547 ? 0.7742 0.5856 0.7848 0.0727  -0.0537 -0.0784 533 ALA B C   
8112 O O   . ALA B 547 ? 0.7901 0.5837 0.8077 0.0828  -0.0555 -0.0772 533 ALA B O   
8113 C CB  . ALA B 547 ? 0.7302 0.5370 0.7270 0.0861  -0.0433 -0.1083 533 ALA B CB  
8114 N N   . ASP B 548 ? 0.7344 0.5517 0.7437 0.0584  -0.0581 -0.0680 534 ASP B N   
8115 C CA  . ASP B 548 ? 0.7348 0.5367 0.7487 0.0522  -0.0652 -0.0558 534 ASP B CA  
8116 C C   . ASP B 548 ? 0.7367 0.5562 0.7635 0.0565  -0.0648 -0.0419 534 ASP B C   
8117 O O   . ASP B 548 ? 0.7077 0.5541 0.7375 0.0540  -0.0616 -0.0373 534 ASP B O   
8118 C CB  . ASP B 548 ? 0.6793 0.4799 0.6861 0.0346  -0.0699 -0.0517 534 ASP B CB  
8119 C CG  . ASP B 548 ? 0.6743 0.4496 0.6814 0.0271  -0.0774 -0.0444 534 ASP B CG  
8120 O OD1 . ASP B 548 ? 0.7138 0.4742 0.7273 0.0353  -0.0792 -0.0398 534 ASP B OD1 
8121 O OD2 . ASP B 548 ? 0.6129 0.3841 0.6143 0.0128  -0.0818 -0.0425 534 ASP B OD2 
8122 N N   . ILE B 549 ? 0.7540 0.5575 0.7877 0.0629  -0.0684 -0.0353 535 ILE B N   
8123 C CA  . ILE B 549 ? 0.7956 0.6136 0.8407 0.0674  -0.0689 -0.0222 535 ILE B CA  
8124 C C   . ILE B 549 ? 0.8070 0.6072 0.8537 0.0604  -0.0761 -0.0095 535 ILE B C   
8125 O O   . ILE B 549 ? 0.8140 0.5848 0.8564 0.0590  -0.0806 -0.0119 535 ILE B O   
8126 C CB  . ILE B 549 ? 0.8305 0.6534 0.8843 0.0852  -0.0654 -0.0261 535 ILE B CB  
8127 C CG1 . ILE B 549 ? 0.8497 0.6406 0.9026 0.0946  -0.0679 -0.0333 535 ILE B CG1 
8128 C CG2 . ILE B 549 ? 0.8010 0.6482 0.8538 0.0898  -0.0576 -0.0363 535 ILE B CG2 
8129 C CD1 . ILE B 549 ? 0.8953 0.6864 0.9606 0.1115  -0.0678 -0.0301 535 ILE B CD1 
8130 N N   . PRO B 550 ? 0.8286 0.6453 0.8806 0.0552  -0.0772 0.0038  536 PRO B N   
8131 C CA  . PRO B 550 ? 0.7961 0.5987 0.8489 0.0473  -0.0836 0.0166  536 PRO B CA  
8132 C C   . PRO B 550 ? 0.8637 0.6471 0.9220 0.0585  -0.0875 0.0211  536 PRO B C   
8133 O O   . PRO B 550 ? 0.8825 0.6697 0.9464 0.0733  -0.0847 0.0155  536 PRO B O   
8134 C CB  . PRO B 550 ? 0.7404 0.5703 0.7972 0.0411  -0.0820 0.0276  536 PRO B CB  
8135 C CG  . PRO B 550 ? 0.7013 0.5551 0.7573 0.0422  -0.0757 0.0197  536 PRO B CG  
8136 C CD  . PRO B 550 ? 0.7559 0.6047 0.8121 0.0548  -0.0727 0.0075  536 PRO B CD  
8137 N N   . PRO B 551 ? 0.9196 0.6825 0.9768 0.0520  -0.0941 0.0317  537 PRO B N   
8138 C CA  . PRO B 551 ? 0.8800 0.6213 0.9424 0.0628  -0.0990 0.0372  537 PRO B CA  
8139 C C   . PRO B 551 ? 0.8919 0.6532 0.9648 0.0759  -0.0976 0.0434  537 PRO B C   
8140 O O   . PRO B 551 ? 0.9154 0.6665 0.9944 0.0914  -0.0981 0.0395  537 PRO B O   
8141 C CB  . PRO B 551 ? 0.8482 0.5717 0.9068 0.0493  -0.1061 0.0508  537 PRO B CB  
8142 C CG  . PRO B 551 ? 0.8222 0.5461 0.8725 0.0336  -0.1050 0.0455  537 PRO B CG  
8143 C CD  . PRO B 551 ? 0.8076 0.5643 0.8589 0.0344  -0.0977 0.0385  537 PRO B CD  
8144 N N   . LEU B 552 ? 0.8602 0.6488 0.9355 0.0701  -0.0963 0.0531  538 LEU B N   
8145 C CA  . LEU B 552 ? 0.8668 0.6750 0.9515 0.0809  -0.0960 0.0597  538 LEU B CA  
8146 C C   . LEU B 552 ? 0.9138 0.7385 1.0041 0.0939  -0.0897 0.0471  538 LEU B C   
8147 O O   . LEU B 552 ? 0.9246 0.7550 1.0245 0.1079  -0.0902 0.0487  538 LEU B O   
8148 C CB  . LEU B 552 ? 0.7896 0.6239 0.8738 0.0707  -0.0954 0.0708  538 LEU B CB  
8149 C CG  . LEU B 552 ? 0.8185 0.6801 0.9108 0.0794  -0.0938 0.0748  538 LEU B CG  
8150 C CD1 . LEU B 552 ? 0.6606 0.5165 0.7589 0.0857  -0.1008 0.0886  538 LEU B CD1 
8151 C CD2 . LEU B 552 ? 0.6655 0.5556 0.7548 0.0691  -0.0896 0.0772  538 LEU B CD2 
8152 N N   . LEU B 553 ? 0.8944 0.7286 0.9791 0.0892  -0.0837 0.0353  539 LEU B N   
8153 C CA  . LEU B 553 ? 0.9306 0.7819 1.0194 0.0999  -0.0771 0.0235  539 LEU B CA  
8154 C C   . LEU B 553 ? 0.9964 0.8281 1.0893 0.1153  -0.0772 0.0146  539 LEU B C   
8155 O O   . LEU B 553 ? 1.0230 0.8692 1.1255 0.1291  -0.0741 0.0112  539 LEU B O   
8156 C CB  . LEU B 553 ? 0.8784 0.7393 0.9585 0.0907  -0.0717 0.0132  539 LEU B CB  
8157 C CG  . LEU B 553 ? 0.8820 0.7657 0.9642 0.0978  -0.0643 0.0026  539 LEU B CG  
8158 C CD1 . LEU B 553 ? 0.8892 0.7983 0.9823 0.1052  -0.0631 0.0094  539 LEU B CD1 
8159 C CD2 . LEU B 553 ? 0.8178 0.7147 0.8915 0.0858  -0.0605 -0.0022 539 LEU B CD2 
8160 N N   . GLY B 554 ? 0.9883 0.7871 1.0746 0.1132  -0.0807 0.0104  540 GLY B N   
8161 C CA  . GLY B 554 ? 1.0109 0.7864 1.1007 0.1283  -0.0812 0.0019  540 GLY B CA  
8162 C C   . GLY B 554 ? 1.0558 0.8289 1.1585 0.1418  -0.0857 0.0127  540 GLY B C   
8163 O O   . GLY B 554 ? 1.0653 0.8370 1.1769 0.1592  -0.0835 0.0059  540 GLY B O   
8164 N N   . ALA B 555 ? 1.0496 0.8232 1.1537 0.1341  -0.0922 0.0299  541 ALA B N   
8165 C CA  . ALA B 555 ? 1.0327 0.8052 1.1481 0.1452  -0.0977 0.0426  541 ALA B CA  
8166 C C   . ALA B 555 ? 1.0262 0.8367 1.1534 0.1541  -0.0944 0.0452  541 ALA B C   
8167 O O   . ALA B 555 ? 1.0303 0.8470 1.1671 0.1676  -0.0937 0.0481  541 ALA B O   
8168 C CB  . ALA B 555 ? 0.9345 0.6983 1.0439 0.1311  -0.1042 0.0599  541 ALA B CB  
8169 N N   . ILE B 556 ? 1.0146 0.8546 1.1381 0.1439  -0.0892 0.0437  542 ILE B N   
8170 C CA  . ILE B 556 ? 1.0026 0.8788 1.1361 0.1498  -0.0863 0.0466  542 ILE B CA  
8171 C C   . ILE B 556 ? 1.0450 0.9328 1.1867 0.1648  -0.0794 0.0324  542 ILE B C   
8172 O O   . ILE B 556 ? 1.0578 0.9640 1.2132 0.1779  -0.0794 0.0352  542 ILE B O   
8173 C CB  . ILE B 556 ? 0.9785 0.8797 1.1047 0.1339  -0.0828 0.0487  542 ILE B CB  
8174 C CG1 . ILE B 556 ? 0.8831 0.7821 1.0041 0.1209  -0.0888 0.0641  542 ILE B CG1 
8175 C CG2 . ILE B 556 ? 0.9593 0.8966 1.0939 0.1391  -0.0779 0.0466  542 ILE B CG2 
8176 C CD1 . ILE B 556 ? 0.6930 0.6178 0.8212 0.1224  -0.0915 0.0759  542 ILE B CD1 
8177 N N   . THR B 557 ? 1.0460 0.9234 1.1795 0.1635  -0.0736 0.0172  543 THR B N   
8178 C CA  . THR B 557 ? 1.0543 0.9473 1.1935 0.1756  -0.0656 0.0029  543 THR B CA  
8179 C C   . THR B 557 ? 1.0795 0.9521 1.2270 0.1948  -0.0658 -0.0045 543 THR B C   
8180 O O   . THR B 557 ? 1.0989 0.9650 1.2430 0.2011  -0.0594 -0.0207 543 THR B O   
8181 C CB  . THR B 557 ? 1.0053 0.9001 1.1309 0.1650  -0.0590 -0.0101 543 THR B CB  
8182 O OG1 . THR B 557 ? 1.0540 0.9133 1.1690 0.1621  -0.0610 -0.0174 543 THR B OG1 
8183 C CG2 . THR B 557 ? 0.9831 0.8939 1.1013 0.1471  -0.0596 -0.0020 543 THR B CG2 
8184 N N   . LYS B 558 ? 1.0734 0.9363 1.2308 0.2036  -0.0723 0.0073  544 LYS B N   
8185 C CA  . LYS B 558 ? 1.0933 0.9491 1.2592 0.2199  -0.0683 0.0036  544 LYS B CA  
8186 C C   . LYS B 558 ? 1.1634 1.0500 1.3458 0.2294  -0.0680 0.0148  544 LYS B C   
8187 O O   . LYS B 558 ? 1.0979 0.9927 1.2918 0.2443  -0.0623 0.0096  544 LYS B O   
8188 C CB  . LYS B 558 ? 1.0564 0.8705 1.2154 0.2196  -0.0730 0.0078  544 LYS B CB  
8189 C CG  . LYS B 558 ? 0.9985 0.8085 1.1636 0.2226  -0.0794 0.0269  544 LYS B CG  
8190 C CD  . LYS B 558 ? 1.0150 0.8429 1.1778 0.2091  -0.0861 0.0434  544 LYS B CD  
8191 C CE  . LYS B 558 ? 0.9517 0.7728 1.1152 0.2091  -0.0931 0.0619  544 LYS B CE  
8192 N NZ  . LYS B 558 ? 0.8088 0.6515 0.9688 0.1954  -0.0983 0.0754  544 LYS B NZ  
8193 N N   . ALA B 559 ? 1.1987 1.1025 1.3823 0.2206  -0.0740 0.0302  545 ALA B N   
8194 C CA  . ALA B 559 ? 1.1262 1.0614 1.3233 0.2266  -0.0750 0.0420  545 ALA B CA  
8195 C C   . ALA B 559 ? 1.1755 1.1490 1.3764 0.2197  -0.0730 0.0414  545 ALA B C   
8196 O O   . ALA B 559 ? 1.1777 1.1794 1.3880 0.2208  -0.0750 0.0522  545 ALA B O   
8197 C CB  . ALA B 559 ? 1.0005 0.9250 1.1932 0.2218  -0.0840 0.0605  545 ALA B CB  
8198 N N   . LEU B 560 ? 1.1533 1.1296 1.3467 0.2132  -0.0690 0.0286  546 LEU B N   
8199 C CA  . LEU B 560 ? 1.1002 1.1131 1.2948 0.2053  -0.0657 0.0284  546 LEU B CA  
8200 C C   . LEU B 560 ? 1.1407 1.1823 1.3476 0.2174  -0.0576 0.0181  546 LEU B C   
8201 O O   . LEU B 560 ? 1.0601 1.1344 1.2784 0.2176  -0.0570 0.0249  546 LEU B O   
8202 C CB  . LEU B 560 ? 1.0208 1.0277 1.1968 0.1869  -0.0618 0.0225  546 LEU B CB  
8203 C CG  . LEU B 560 ? 0.8497 0.8916 1.0257 0.1759  -0.0595 0.0271  546 LEU B CG  
8204 C CD1 . LEU B 560 ? 0.7124 0.7587 0.8747 0.1624  -0.0528 0.0180  546 LEU B CD1 
8205 C CD2 . LEU B 560 ? 0.7503 0.7928 0.9247 0.1669  -0.0676 0.0432  546 LEU B CD2 
8206 N N   . GLU B 561 ? 1.1790 1.2094 1.3831 0.2248  -0.0504 0.0023  547 GLU B N   
8207 C CA  . GLU B 561 ? 1.2309 1.2868 1.4474 0.2356  -0.0414 -0.0060 547 GLU B CA  
8208 C C   . GLU B 561 ? 1.2185 1.2597 1.4473 0.2506  -0.0407 -0.0049 547 GLU B C   
8209 O O   . GLU B 561 ? 1.2028 1.2404 1.4345 0.2610  -0.0328 -0.0181 547 GLU B O   
8210 C CB  . GLU B 561 ? 1.0768 1.1381 1.2837 0.2345  -0.0323 -0.0238 547 GLU B CB  
8211 C CG  . GLU B 561 ? 0.9556 1.0609 1.1671 0.2280  -0.0271 -0.0229 547 GLU B CG  
8212 C CD  . GLU B 561 ? 0.8754 0.9891 1.0737 0.2188  -0.0177 -0.0360 547 GLU B CD  
8213 O OE1 . GLU B 561 ? 0.8662 0.9692 1.0612 0.2276  -0.0112 -0.0507 547 GLU B OE1 
8214 O OE2 . GLU B 561 ? 0.6345 0.7646 0.8247 0.2023  -0.0171 -0.0315 547 GLU B OE2 
8215 N N   . ALA B 562 ? 1.2062 1.2361 1.4405 0.2513  -0.0492 0.0111  548 ALA B N   
8216 C CA  . ALA B 562 ? 1.2036 1.2278 1.4535 0.2656  -0.0496 0.0168  548 ALA B CA  
8217 C C   . ALA B 562 ? 1.2057 1.2699 1.4779 0.2701  -0.0492 0.0236  548 ALA B C   
8218 O O   . ALA B 562 ? 1.1721 1.2402 1.4612 0.2841  -0.0462 0.0224  548 ALA B O   
8219 C CB  . ALA B 562 ? 1.1796 1.1747 1.4236 0.2642  -0.0589 0.0321  548 ALA B CB  
8220 N N   . ARG B 563 ? 1.1973 1.2912 1.4704 0.2580  -0.0524 0.0296  549 ARG B N   
8221 C CA  . ARG B 563 ? 1.1467 1.2770 1.4397 0.2595  -0.0546 0.0353  549 ARG B CA  
8222 C C   . ARG B 563 ? 1.1888 1.3442 1.4898 0.2666  -0.0432 0.0213  549 ARG B C   
8223 O O   . ARG B 563 ? 1.0769 1.2508 1.3978 0.2766  -0.0421 0.0220  549 ARG B O   
8224 C CB  . ARG B 563 ? 0.9779 1.1284 1.2637 0.2427  -0.0617 0.0439  549 ARG B CB  
8225 C CG  . ARG B 563 ? 0.9675 1.0936 1.2435 0.2349  -0.0734 0.0567  549 ARG B CG  
8226 C CD  . ARG B 563 ? 0.8710 1.0005 1.1272 0.2180  -0.0746 0.0582  549 ARG B CD  
8227 N NE  . ARG B 563 ? 0.7185 0.8847 0.9750 0.2084  -0.0727 0.0587  549 ARG B NE  
8228 C CZ  . ARG B 563 ? 0.5161 0.6924 0.7590 0.1948  -0.0692 0.0574  549 ARG B CZ  
8229 N NH1 . ARG B 563 ? 0.4860 0.6406 0.7136 0.1894  -0.0680 0.0554  549 ARG B NH1 
8230 N NH2 . ARG B 563 ? 0.4130 0.6216 0.6579 0.1861  -0.0669 0.0580  549 ARG B NH2 
8231 N N   . ASN B 564 ? 1.2810 1.4392 1.5669 0.2608  -0.0350 0.0089  550 ASN B N   
8232 C CA  . ASN B 564 ? 1.1316 1.3089 1.4207 0.2667  -0.0230 -0.0059 550 ASN B CA  
8233 C C   . ASN B 564 ? 1.0685 1.2144 1.3485 0.2766  -0.0163 -0.0205 550 ASN B C   
8234 O O   . ASN B 564 ? 1.0428 1.1838 1.3067 0.2716  -0.0103 -0.0329 550 ASN B O   
8239 N N   . SER B 565 ? 1.1237 1.2470 1.4135 0.2902  -0.0179 -0.0189 551 SER B N   
8240 C CA  . SER B 565 ? 1.1599 1.2521 1.4416 0.3003  -0.0113 -0.0336 551 SER B CA  
8241 C C   . SER B 565 ? 1.0790 1.1663 1.3801 0.3182  -0.0089 -0.0332 551 SER B C   
8242 O O   . SER B 565 ? 1.0289 1.1365 1.3506 0.3227  -0.0134 -0.0209 551 SER B O   
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