data_9UCE
# 
_entry.id   9UCE 
# 
_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   9UCE         pdb_00009uce 10.2210/pdb9uce/pdb 
WWPDB D_1300058010 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-04-23 
_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                        9UCE 
_pdbx_database_status.recvd_initial_deposition_date   2025-04-04 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              yzhang2011@sjtu.edu.cn 
_pdbx_contact_author.name_first         Yong 
_pdbx_contact_author.name_last          Zhang 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-1497-5979 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Zhu, J.S.' 1 ? 
'Zhang, Y.' 2 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Crystal structure of glycosyltransferase UGT73K1 in complex with UDP' 
_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 'Zhu, J.S.' 1 ? 
primary 'Zhang, Y.' 2 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man Glycosyltransferase      57548.594 1   2.4.1.- ? ? ? 
2 non-polymer syn 'CHLORIDE ION'           35.453    3   ?       ? ? ? 
3 non-polymer syn 'SULFATE ION'            96.063    4   ?       ? ? ? 
4 non-polymer syn "URIDINE-5'-DIPHOSPHATE" 404.161   1   ?       ? ? ? 
5 water       nat water                    18.015    150 ?       ? ? ? 
# 
_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       
;MGSSHHHHHHSSGLVPRGSHMASMTGGQQMGRGSMGTESKPLKIYMLPFFAQGHLIPLVNLARLVASKNQHVTIITTPSN
AQLFDKTIEEEKAAGHHIRVHIIKFPSAQLGLPTGVENLFAASDNQTAGKIHMAAHFVKADIEEFMKENPPDVFISDIIF
TWSESTAKNLQIPRLVFNPISIFDVCMIQAIQSHPESFVSDSGPYQIHGLPHPLTLPIKPSPGFARLTESLIEAENDSHG
VIVNSFAELDEGYTEYYENLTGRKVWHVGPTSLMVEIPKKKKVVSTENDSSITKHQSLTWLDTKEPSSVLYISFGSLCRL
SNEQLKEMANGIEASKHQFLWVVHGKEGEDEDNWLPKGFVERMKEEKKGMLIKGWVPQALILDHPSIGGFLTHCGWNATV
EAISSGVPMVTMPGFGDQYYNEKLVTEVHRIGVEVGAAEWSMSPYDAKKTVVRAERIEKAVKKLMDSNGEGGEIRKRAKE
MKEKAWKAVQEGGSSQNCLTKLVDYLHSVVVTKSVELN
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGSSHHHHHHSSGLVPRGSHMASMTGGQQMGRGSMGTESKPLKIYMLPFFAQGHLIPLVNLARLVASKNQHVTIITTPSN
AQLFDKTIEEEKAAGHHIRVHIIKFPSAQLGLPTGVENLFAASDNQTAGKIHMAAHFVKADIEEFMKENPPDVFISDIIF
TWSESTAKNLQIPRLVFNPISIFDVCMIQAIQSHPESFVSDSGPYQIHGLPHPLTLPIKPSPGFARLTESLIEAENDSHG
VIVNSFAELDEGYTEYYENLTGRKVWHVGPTSLMVEIPKKKKVVSTENDSSITKHQSLTWLDTKEPSSVLYISFGSLCRL
SNEQLKEMANGIEASKHQFLWVVHGKEGEDEDNWLPKGFVERMKEEKKGMLIKGWVPQALILDHPSIGGFLTHCGWNATV
EAISSGVPMVTMPGFGDQYYNEKLVTEVHRIGVEVGAAEWSMSPYDAKKTVVRAERIEKAVKKLMDSNGEGGEIRKRAKE
MKEKAWKAVQEGGSSQNCLTKLVDYLHSVVVTKSVELN
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'CHLORIDE ION'           CL  
3 'SULFATE ION'            SO4 
4 "URIDINE-5'-DIPHOSPHATE" UDP 
5 water                    HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLY n 
1 3   SER n 
1 4   SER n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   HIS n 
1 10  HIS n 
1 11  SER n 
1 12  SER n 
1 13  GLY n 
1 14  LEU n 
1 15  VAL n 
1 16  PRO n 
1 17  ARG n 
1 18  GLY n 
1 19  SER n 
1 20  HIS n 
1 21  MET n 
1 22  ALA n 
1 23  SER n 
1 24  MET n 
1 25  THR n 
1 26  GLY n 
1 27  GLY n 
1 28  GLN n 
1 29  GLN n 
1 30  MET n 
1 31  GLY n 
1 32  ARG n 
1 33  GLY n 
1 34  SER n 
1 35  MET n 
1 36  GLY n 
1 37  THR n 
1 38  GLU n 
1 39  SER n 
1 40  LYS n 
1 41  PRO n 
1 42  LEU n 
1 43  LYS n 
1 44  ILE n 
1 45  TYR n 
1 46  MET n 
1 47  LEU n 
1 48  PRO n 
1 49  PHE n 
1 50  PHE n 
1 51  ALA n 
1 52  GLN n 
1 53  GLY n 
1 54  HIS n 
1 55  LEU n 
1 56  ILE n 
1 57  PRO n 
1 58  LEU n 
1 59  VAL n 
1 60  ASN n 
1 61  LEU n 
1 62  ALA n 
1 63  ARG n 
1 64  LEU n 
1 65  VAL n 
1 66  ALA n 
1 67  SER n 
1 68  LYS n 
1 69  ASN n 
1 70  GLN n 
1 71  HIS n 
1 72  VAL n 
1 73  THR n 
1 74  ILE n 
1 75  ILE n 
1 76  THR n 
1 77  THR n 
1 78  PRO n 
1 79  SER n 
1 80  ASN n 
1 81  ALA n 
1 82  GLN n 
1 83  LEU n 
1 84  PHE n 
1 85  ASP n 
1 86  LYS n 
1 87  THR n 
1 88  ILE n 
1 89  GLU n 
1 90  GLU n 
1 91  GLU n 
1 92  LYS n 
1 93  ALA n 
1 94  ALA n 
1 95  GLY n 
1 96  HIS n 
1 97  HIS n 
1 98  ILE n 
1 99  ARG n 
1 100 VAL n 
1 101 HIS n 
1 102 ILE n 
1 103 ILE n 
1 104 LYS n 
1 105 PHE n 
1 106 PRO n 
1 107 SER n 
1 108 ALA n 
1 109 GLN n 
1 110 LEU n 
1 111 GLY n 
1 112 LEU n 
1 113 PRO n 
1 114 THR n 
1 115 GLY n 
1 116 VAL n 
1 117 GLU n 
1 118 ASN n 
1 119 LEU n 
1 120 PHE n 
1 121 ALA n 
1 122 ALA n 
1 123 SER n 
1 124 ASP n 
1 125 ASN n 
1 126 GLN n 
1 127 THR n 
1 128 ALA n 
1 129 GLY n 
1 130 LYS n 
1 131 ILE n 
1 132 HIS n 
1 133 MET n 
1 134 ALA n 
1 135 ALA n 
1 136 HIS n 
1 137 PHE n 
1 138 VAL n 
1 139 LYS n 
1 140 ALA n 
1 141 ASP n 
1 142 ILE n 
1 143 GLU n 
1 144 GLU n 
1 145 PHE n 
1 146 MET n 
1 147 LYS n 
1 148 GLU n 
1 149 ASN n 
1 150 PRO n 
1 151 PRO n 
1 152 ASP n 
1 153 VAL n 
1 154 PHE n 
1 155 ILE n 
1 156 SER n 
1 157 ASP n 
1 158 ILE n 
1 159 ILE n 
1 160 PHE n 
1 161 THR n 
1 162 TRP n 
1 163 SER n 
1 164 GLU n 
1 165 SER n 
1 166 THR n 
1 167 ALA n 
1 168 LYS n 
1 169 ASN n 
1 170 LEU n 
1 171 GLN n 
1 172 ILE n 
1 173 PRO n 
1 174 ARG n 
1 175 LEU n 
1 176 VAL n 
1 177 PHE n 
1 178 ASN n 
1 179 PRO n 
1 180 ILE n 
1 181 SER n 
1 182 ILE n 
1 183 PHE n 
1 184 ASP n 
1 185 VAL n 
1 186 CYS n 
1 187 MET n 
1 188 ILE n 
1 189 GLN n 
1 190 ALA n 
1 191 ILE n 
1 192 GLN n 
1 193 SER n 
1 194 HIS n 
1 195 PRO n 
1 196 GLU n 
1 197 SER n 
1 198 PHE n 
1 199 VAL n 
1 200 SER n 
1 201 ASP n 
1 202 SER n 
1 203 GLY n 
1 204 PRO n 
1 205 TYR n 
1 206 GLN n 
1 207 ILE n 
1 208 HIS n 
1 209 GLY n 
1 210 LEU n 
1 211 PRO n 
1 212 HIS n 
1 213 PRO n 
1 214 LEU n 
1 215 THR n 
1 216 LEU n 
1 217 PRO n 
1 218 ILE n 
1 219 LYS n 
1 220 PRO n 
1 221 SER n 
1 222 PRO n 
1 223 GLY n 
1 224 PHE n 
1 225 ALA n 
1 226 ARG n 
1 227 LEU n 
1 228 THR n 
1 229 GLU n 
1 230 SER n 
1 231 LEU n 
1 232 ILE n 
1 233 GLU n 
1 234 ALA n 
1 235 GLU n 
1 236 ASN n 
1 237 ASP n 
1 238 SER n 
1 239 HIS n 
1 240 GLY n 
1 241 VAL n 
1 242 ILE n 
1 243 VAL n 
1 244 ASN n 
1 245 SER n 
1 246 PHE n 
1 247 ALA n 
1 248 GLU n 
1 249 LEU n 
1 250 ASP n 
1 251 GLU n 
1 252 GLY n 
1 253 TYR n 
1 254 THR n 
1 255 GLU n 
1 256 TYR n 
1 257 TYR n 
1 258 GLU n 
1 259 ASN n 
1 260 LEU n 
1 261 THR n 
1 262 GLY n 
1 263 ARG n 
1 264 LYS n 
1 265 VAL n 
1 266 TRP n 
1 267 HIS n 
1 268 VAL n 
1 269 GLY n 
1 270 PRO n 
1 271 THR n 
1 272 SER n 
1 273 LEU n 
1 274 MET n 
1 275 VAL n 
1 276 GLU n 
1 277 ILE n 
1 278 PRO n 
1 279 LYS n 
1 280 LYS n 
1 281 LYS n 
1 282 LYS n 
1 283 VAL n 
1 284 VAL n 
1 285 SER n 
1 286 THR n 
1 287 GLU n 
1 288 ASN n 
1 289 ASP n 
1 290 SER n 
1 291 SER n 
1 292 ILE n 
1 293 THR n 
1 294 LYS n 
1 295 HIS n 
1 296 GLN n 
1 297 SER n 
1 298 LEU n 
1 299 THR n 
1 300 TRP n 
1 301 LEU n 
1 302 ASP n 
1 303 THR n 
1 304 LYS n 
1 305 GLU n 
1 306 PRO n 
1 307 SER n 
1 308 SER n 
1 309 VAL n 
1 310 LEU n 
1 311 TYR n 
1 312 ILE n 
1 313 SER n 
1 314 PHE n 
1 315 GLY n 
1 316 SER n 
1 317 LEU n 
1 318 CYS n 
1 319 ARG n 
1 320 LEU n 
1 321 SER n 
1 322 ASN n 
1 323 GLU n 
1 324 GLN n 
1 325 LEU n 
1 326 LYS n 
1 327 GLU n 
1 328 MET n 
1 329 ALA n 
1 330 ASN n 
1 331 GLY n 
1 332 ILE n 
1 333 GLU n 
1 334 ALA n 
1 335 SER n 
1 336 LYS n 
1 337 HIS n 
1 338 GLN n 
1 339 PHE n 
1 340 LEU n 
1 341 TRP n 
1 342 VAL n 
1 343 VAL n 
1 344 HIS n 
1 345 GLY n 
1 346 LYS n 
1 347 GLU n 
1 348 GLY n 
1 349 GLU n 
1 350 ASP n 
1 351 GLU n 
1 352 ASP n 
1 353 ASN n 
1 354 TRP n 
1 355 LEU n 
1 356 PRO n 
1 357 LYS n 
1 358 GLY n 
1 359 PHE n 
1 360 VAL n 
1 361 GLU n 
1 362 ARG n 
1 363 MET n 
1 364 LYS n 
1 365 GLU n 
1 366 GLU n 
1 367 LYS n 
1 368 LYS n 
1 369 GLY n 
1 370 MET n 
1 371 LEU n 
1 372 ILE n 
1 373 LYS n 
1 374 GLY n 
1 375 TRP n 
1 376 VAL n 
1 377 PRO n 
1 378 GLN n 
1 379 ALA n 
1 380 LEU n 
1 381 ILE n 
1 382 LEU n 
1 383 ASP n 
1 384 HIS n 
1 385 PRO n 
1 386 SER n 
1 387 ILE n 
1 388 GLY n 
1 389 GLY n 
1 390 PHE n 
1 391 LEU n 
1 392 THR n 
1 393 HIS n 
1 394 CYS n 
1 395 GLY n 
1 396 TRP n 
1 397 ASN n 
1 398 ALA n 
1 399 THR n 
1 400 VAL n 
1 401 GLU n 
1 402 ALA n 
1 403 ILE n 
1 404 SER n 
1 405 SER n 
1 406 GLY n 
1 407 VAL n 
1 408 PRO n 
1 409 MET n 
1 410 VAL n 
1 411 THR n 
1 412 MET n 
1 413 PRO n 
1 414 GLY n 
1 415 PHE n 
1 416 GLY n 
1 417 ASP n 
1 418 GLN n 
1 419 TYR n 
1 420 TYR n 
1 421 ASN n 
1 422 GLU n 
1 423 LYS n 
1 424 LEU n 
1 425 VAL n 
1 426 THR n 
1 427 GLU n 
1 428 VAL n 
1 429 HIS n 
1 430 ARG n 
1 431 ILE n 
1 432 GLY n 
1 433 VAL n 
1 434 GLU n 
1 435 VAL n 
1 436 GLY n 
1 437 ALA n 
1 438 ALA n 
1 439 GLU n 
1 440 TRP n 
1 441 SER n 
1 442 MET n 
1 443 SER n 
1 444 PRO n 
1 445 TYR n 
1 446 ASP n 
1 447 ALA n 
1 448 LYS n 
1 449 LYS n 
1 450 THR n 
1 451 VAL n 
1 452 VAL n 
1 453 ARG n 
1 454 ALA n 
1 455 GLU n 
1 456 ARG n 
1 457 ILE n 
1 458 GLU n 
1 459 LYS n 
1 460 ALA n 
1 461 VAL n 
1 462 LYS n 
1 463 LYS n 
1 464 LEU n 
1 465 MET n 
1 466 ASP n 
1 467 SER n 
1 468 ASN n 
1 469 GLY n 
1 470 GLU n 
1 471 GLY n 
1 472 GLY n 
1 473 GLU n 
1 474 ILE n 
1 475 ARG n 
1 476 LYS n 
1 477 ARG n 
1 478 ALA n 
1 479 LYS n 
1 480 GLU n 
1 481 MET n 
1 482 LYS n 
1 483 GLU n 
1 484 LYS n 
1 485 ALA n 
1 486 TRP n 
1 487 LYS n 
1 488 ALA n 
1 489 VAL n 
1 490 GLN n 
1 491 GLU n 
1 492 GLY n 
1 493 GLY n 
1 494 SER n 
1 495 SER n 
1 496 GLN n 
1 497 ASN n 
1 498 CYS n 
1 499 LEU n 
1 500 THR n 
1 501 LYS n 
1 502 LEU n 
1 503 VAL n 
1 504 ASP n 
1 505 TYR n 
1 506 LEU n 
1 507 HIS n 
1 508 SER n 
1 509 VAL n 
1 510 VAL n 
1 511 VAL n 
1 512 THR n 
1 513 LYS n 
1 514 SER n 
1 515 VAL n 
1 516 GLU n 
1 517 LEU n 
1 518 ASN 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                   518 
_entity_src_gen.gene_src_common_name               'barrel medic' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 '11431381, MTR_4g031800, MtrunA17_Chr4g0014061' 
_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      'Medicago truncatula' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     3880 
_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 
CL  non-polymer         . 'CHLORIDE ION'           ? 'Cl -1'            35.453  
CYS 'L-peptide linking' y CYSTEINE                 ? 'C3 H7 N O2 S'     121.158 
GLN 'L-peptide linking' y GLUTAMINE                ? 'C5 H10 N2 O3'     146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'          ? 'C5 H9 N O4'       147.129 
GLY 'peptide linking'   y GLYCINE                  ? 'C2 H5 N O2'       75.067  
HIS 'L-peptide linking' y HISTIDINE                ? 'C6 H10 N3 O2 1'   156.162 
HOH non-polymer         . WATER                    ? 'H2 O'             18.015  
ILE 'L-peptide linking' y ISOLEUCINE               ? 'C6 H13 N O2'      131.173 
LEU 'L-peptide linking' y LEUCINE                  ? 'C6 H13 N O2'      131.173 
LYS 'L-peptide linking' y LYSINE                   ? 'C6 H15 N2 O2 1'   147.195 
MET 'L-peptide linking' y METHIONINE               ? 'C5 H11 N O2 S'    149.211 
PHE 'L-peptide linking' y PHENYLALANINE            ? 'C9 H11 N O2'      165.189 
PRO 'L-peptide linking' y PROLINE                  ? 'C5 H9 N O2'       115.130 
SER 'L-peptide linking' y SERINE                   ? 'C3 H7 N O3'       105.093 
SO4 non-polymer         . 'SULFATE ION'            ? 'O4 S -2'          96.063  
THR 'L-peptide linking' y THREONINE                ? 'C4 H9 N O3'       119.119 
TRP 'L-peptide linking' y TRYPTOPHAN               ? 'C11 H12 N2 O2'    204.225 
TYR 'L-peptide linking' y TYROSINE                 ? 'C9 H11 N O3'      181.189 
UDP 'RNA linking'       . "URIDINE-5'-DIPHOSPHATE" ? 'C9 H14 N2 O12 P2' 404.161 
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   -33 ?   ?   ?   A . n 
A 1 2   GLY 2   -32 ?   ?   ?   A . n 
A 1 3   SER 3   -31 ?   ?   ?   A . n 
A 1 4   SER 4   -30 ?   ?   ?   A . n 
A 1 5   HIS 5   -29 ?   ?   ?   A . n 
A 1 6   HIS 6   -28 ?   ?   ?   A . n 
A 1 7   HIS 7   -27 ?   ?   ?   A . n 
A 1 8   HIS 8   -26 ?   ?   ?   A . n 
A 1 9   HIS 9   -25 ?   ?   ?   A . n 
A 1 10  HIS 10  -24 ?   ?   ?   A . n 
A 1 11  SER 11  -23 ?   ?   ?   A . n 
A 1 12  SER 12  -22 ?   ?   ?   A . n 
A 1 13  GLY 13  -21 ?   ?   ?   A . n 
A 1 14  LEU 14  -20 ?   ?   ?   A . n 
A 1 15  VAL 15  -19 ?   ?   ?   A . n 
A 1 16  PRO 16  -18 ?   ?   ?   A . n 
A 1 17  ARG 17  -17 ?   ?   ?   A . n 
A 1 18  GLY 18  -16 ?   ?   ?   A . n 
A 1 19  SER 19  -15 ?   ?   ?   A . n 
A 1 20  HIS 20  -14 ?   ?   ?   A . n 
A 1 21  MET 21  -13 ?   ?   ?   A . n 
A 1 22  ALA 22  -12 ?   ?   ?   A . n 
A 1 23  SER 23  -11 ?   ?   ?   A . n 
A 1 24  MET 24  -10 ?   ?   ?   A . n 
A 1 25  THR 25  -9  ?   ?   ?   A . n 
A 1 26  GLY 26  -8  ?   ?   ?   A . n 
A 1 27  GLY 27  -7  ?   ?   ?   A . n 
A 1 28  GLN 28  -6  ?   ?   ?   A . n 
A 1 29  GLN 29  -5  ?   ?   ?   A . n 
A 1 30  MET 30  -4  ?   ?   ?   A . n 
A 1 31  GLY 31  -3  ?   ?   ?   A . n 
A 1 32  ARG 32  -2  ?   ?   ?   A . n 
A 1 33  GLY 33  -1  ?   ?   ?   A . n 
A 1 34  SER 34  0   ?   ?   ?   A . n 
A 1 35  MET 35  1   ?   ?   ?   A . n 
A 1 36  GLY 36  2   ?   ?   ?   A . n 
A 1 37  THR 37  3   ?   ?   ?   A . n 
A 1 38  GLU 38  4   ?   ?   ?   A . n 
A 1 39  SER 39  5   ?   ?   ?   A . n 
A 1 40  LYS 40  6   ?   ?   ?   A . n 
A 1 41  PRO 41  7   7   PRO PRO A . n 
A 1 42  LEU 42  8   8   LEU LEU A . n 
A 1 43  LYS 43  9   9   LYS LYS A . n 
A 1 44  ILE 44  10  10  ILE ILE A . n 
A 1 45  TYR 45  11  11  TYR TYR A . n 
A 1 46  MET 46  12  12  MET MET A . n 
A 1 47  LEU 47  13  13  LEU LEU A . n 
A 1 48  PRO 48  14  14  PRO PRO A . n 
A 1 49  PHE 49  15  15  PHE PHE A . n 
A 1 50  PHE 50  16  16  PHE PHE A . n 
A 1 51  ALA 51  17  17  ALA ALA A . n 
A 1 52  GLN 52  18  18  GLN GLN A . n 
A 1 53  GLY 53  19  19  GLY GLY A . n 
A 1 54  HIS 54  20  20  HIS HIS A . n 
A 1 55  LEU 55  21  21  LEU LEU A . n 
A 1 56  ILE 56  22  22  ILE ILE A . n 
A 1 57  PRO 57  23  23  PRO PRO A . n 
A 1 58  LEU 58  24  24  LEU LEU A . n 
A 1 59  VAL 59  25  25  VAL VAL A . n 
A 1 60  ASN 60  26  26  ASN ASN A . n 
A 1 61  LEU 61  27  27  LEU LEU A . n 
A 1 62  ALA 62  28  28  ALA ALA A . n 
A 1 63  ARG 63  29  29  ARG ARG A . n 
A 1 64  LEU 64  30  30  LEU LEU A . n 
A 1 65  VAL 65  31  31  VAL VAL A . n 
A 1 66  ALA 66  32  32  ALA ALA A . n 
A 1 67  SER 67  33  33  SER SER A . n 
A 1 68  LYS 68  34  34  LYS LYS A . n 
A 1 69  ASN 69  35  35  ASN ASN A . n 
A 1 70  GLN 70  36  36  GLN GLN A . n 
A 1 71  HIS 71  37  37  HIS HIS A . n 
A 1 72  VAL 72  38  38  VAL VAL A . n 
A 1 73  THR 73  39  39  THR THR A . n 
A 1 74  ILE 74  40  40  ILE ILE A . n 
A 1 75  ILE 75  41  41  ILE ILE A . n 
A 1 76  THR 76  42  42  THR THR A . n 
A 1 77  THR 77  43  43  THR THR A . n 
A 1 78  PRO 78  44  44  PRO PRO A . n 
A 1 79  SER 79  45  45  SER SER A . n 
A 1 80  ASN 80  46  46  ASN ASN A . n 
A 1 81  ALA 81  47  47  ALA ALA A . n 
A 1 82  GLN 82  48  48  GLN GLN A . n 
A 1 83  LEU 83  49  49  LEU LEU A . n 
A 1 84  PHE 84  50  50  PHE PHE A . n 
A 1 85  ASP 85  51  51  ASP ASP A . n 
A 1 86  LYS 86  52  52  LYS LYS A . n 
A 1 87  THR 87  53  53  THR THR A . n 
A 1 88  ILE 88  54  54  ILE ILE A . n 
A 1 89  GLU 89  55  55  GLU GLU A . n 
A 1 90  GLU 90  56  56  GLU GLU A . n 
A 1 91  GLU 91  57  57  GLU GLU A . n 
A 1 92  LYS 92  58  58  LYS LYS A . n 
A 1 93  ALA 93  59  59  ALA ALA A . n 
A 1 94  ALA 94  60  60  ALA ALA A . n 
A 1 95  GLY 95  61  61  GLY GLY A . n 
A 1 96  HIS 96  62  62  HIS HIS A . n 
A 1 97  HIS 97  63  63  HIS HIS A . n 
A 1 98  ILE 98  64  64  ILE ILE A . n 
A 1 99  ARG 99  65  65  ARG ARG A . n 
A 1 100 VAL 100 66  66  VAL VAL A . n 
A 1 101 HIS 101 67  67  HIS HIS A . n 
A 1 102 ILE 102 68  68  ILE ILE A . n 
A 1 103 ILE 103 69  69  ILE ILE A . n 
A 1 104 LYS 104 70  70  LYS LYS A . n 
A 1 105 PHE 105 71  71  PHE PHE A . n 
A 1 106 PRO 106 72  72  PRO PRO A . n 
A 1 107 SER 107 73  73  SER SER A . n 
A 1 108 ALA 108 74  74  ALA ALA A . n 
A 1 109 GLN 109 75  75  GLN GLN A . n 
A 1 110 LEU 110 76  76  LEU LEU A . n 
A 1 111 GLY 111 77  77  GLY GLY A . n 
A 1 112 LEU 112 78  78  LEU LEU A . n 
A 1 113 PRO 113 79  79  PRO PRO A . n 
A 1 114 THR 114 80  80  THR THR A . n 
A 1 115 GLY 115 81  81  GLY GLY A . n 
A 1 116 VAL 116 82  82  VAL VAL A . n 
A 1 117 GLU 117 83  83  GLU GLU A . n 
A 1 118 ASN 118 84  84  ASN ASN A . n 
A 1 119 LEU 119 85  85  LEU LEU A . n 
A 1 120 PHE 120 86  86  PHE PHE A . n 
A 1 121 ALA 121 87  87  ALA ALA A . n 
A 1 122 ALA 122 88  88  ALA ALA A . n 
A 1 123 SER 123 89  89  SER SER A . n 
A 1 124 ASP 124 90  90  ASP ASP A . n 
A 1 125 ASN 125 91  91  ASN ASN A . n 
A 1 126 GLN 126 92  92  GLN GLN A . n 
A 1 127 THR 127 93  93  THR THR A . n 
A 1 128 ALA 128 94  94  ALA ALA A . n 
A 1 129 GLY 129 95  95  GLY GLY A . n 
A 1 130 LYS 130 96  96  LYS LYS A . n 
A 1 131 ILE 131 97  97  ILE ILE A . n 
A 1 132 HIS 132 98  98  HIS HIS A . n 
A 1 133 MET 133 99  99  MET MET A . n 
A 1 134 ALA 134 100 100 ALA ALA A . n 
A 1 135 ALA 135 101 101 ALA ALA A . n 
A 1 136 HIS 136 102 102 HIS HIS A . n 
A 1 137 PHE 137 103 103 PHE PHE A . n 
A 1 138 VAL 138 104 104 VAL VAL A . n 
A 1 139 LYS 139 105 105 LYS LYS A . n 
A 1 140 ALA 140 106 106 ALA ALA A . n 
A 1 141 ASP 141 107 107 ASP ASP A . n 
A 1 142 ILE 142 108 108 ILE ILE A . n 
A 1 143 GLU 143 109 109 GLU GLU A . n 
A 1 144 GLU 144 110 110 GLU GLU A . n 
A 1 145 PHE 145 111 111 PHE PHE A . n 
A 1 146 MET 146 112 112 MET MET A . n 
A 1 147 LYS 147 113 113 LYS LYS A . n 
A 1 148 GLU 148 114 114 GLU GLU A . n 
A 1 149 ASN 149 115 115 ASN ASN A . n 
A 1 150 PRO 150 116 116 PRO PRO A . n 
A 1 151 PRO 151 117 117 PRO PRO A . n 
A 1 152 ASP 152 118 118 ASP ASP A . n 
A 1 153 VAL 153 119 119 VAL VAL A . n 
A 1 154 PHE 154 120 120 PHE PHE A . n 
A 1 155 ILE 155 121 121 ILE ILE A . n 
A 1 156 SER 156 122 122 SER SER A . n 
A 1 157 ASP 157 123 123 ASP ASP A . n 
A 1 158 ILE 158 124 124 ILE ILE A . n 
A 1 159 ILE 159 125 125 ILE ILE A . n 
A 1 160 PHE 160 126 126 PHE PHE A . n 
A 1 161 THR 161 127 127 THR THR A . n 
A 1 162 TRP 162 128 128 TRP TRP A . n 
A 1 163 SER 163 129 129 SER SER A . n 
A 1 164 GLU 164 130 130 GLU GLU A . n 
A 1 165 SER 165 131 131 SER SER A . n 
A 1 166 THR 166 132 132 THR THR A . n 
A 1 167 ALA 167 133 133 ALA ALA A . n 
A 1 168 LYS 168 134 134 LYS LYS A . n 
A 1 169 ASN 169 135 135 ASN ASN A . n 
A 1 170 LEU 170 136 136 LEU LEU A . n 
A 1 171 GLN 171 137 137 GLN GLN A . n 
A 1 172 ILE 172 138 138 ILE ILE A . n 
A 1 173 PRO 173 139 139 PRO PRO A . n 
A 1 174 ARG 174 140 140 ARG ARG A . n 
A 1 175 LEU 175 141 141 LEU LEU A . n 
A 1 176 VAL 176 142 142 VAL VAL A . n 
A 1 177 PHE 177 143 143 PHE PHE A . n 
A 1 178 ASN 178 144 144 ASN ASN A . n 
A 1 179 PRO 179 145 145 PRO PRO A . n 
A 1 180 ILE 180 146 146 ILE ILE A . n 
A 1 181 SER 181 147 147 SER SER A . n 
A 1 182 ILE 182 148 148 ILE ILE A . n 
A 1 183 PHE 183 149 149 PHE PHE A . n 
A 1 184 ASP 184 150 150 ASP ASP A . n 
A 1 185 VAL 185 151 151 VAL VAL A . n 
A 1 186 CYS 186 152 152 CYS CYS A . n 
A 1 187 MET 187 153 153 MET MET A . n 
A 1 188 ILE 188 154 154 ILE ILE A . n 
A 1 189 GLN 189 155 155 GLN GLN A . n 
A 1 190 ALA 190 156 156 ALA ALA A . n 
A 1 191 ILE 191 157 157 ILE ILE A . n 
A 1 192 GLN 192 158 158 GLN GLN A . n 
A 1 193 SER 193 159 159 SER SER A . n 
A 1 194 HIS 194 160 160 HIS HIS A . n 
A 1 195 PRO 195 161 161 PRO PRO A . n 
A 1 196 GLU 196 162 162 GLU GLU A . n 
A 1 197 SER 197 163 163 SER SER A . n 
A 1 198 PHE 198 164 164 PHE PHE A . n 
A 1 199 VAL 199 165 165 VAL VAL A . n 
A 1 200 SER 200 166 166 SER SER A . n 
A 1 201 ASP 201 167 167 ASP ASP A . n 
A 1 202 SER 202 168 168 SER SER A . n 
A 1 203 GLY 203 169 169 GLY GLY A . n 
A 1 204 PRO 204 170 170 PRO PRO A . n 
A 1 205 TYR 205 171 171 TYR TYR A . n 
A 1 206 GLN 206 172 172 GLN GLN A . n 
A 1 207 ILE 207 173 173 ILE ILE A . n 
A 1 208 HIS 208 174 174 HIS HIS A . n 
A 1 209 GLY 209 175 175 GLY GLY A . n 
A 1 210 LEU 210 176 176 LEU LEU A . n 
A 1 211 PRO 211 177 177 PRO PRO A . n 
A 1 212 HIS 212 178 178 HIS HIS A . n 
A 1 213 PRO 213 179 179 PRO PRO A . n 
A 1 214 LEU 214 180 180 LEU LEU A . n 
A 1 215 THR 215 181 181 THR THR A . n 
A 1 216 LEU 216 182 182 LEU LEU A . n 
A 1 217 PRO 217 183 183 PRO PRO A . n 
A 1 218 ILE 218 184 184 ILE ILE A . n 
A 1 219 LYS 219 185 185 LYS LYS A . n 
A 1 220 PRO 220 186 186 PRO PRO A . n 
A 1 221 SER 221 187 187 SER SER A . n 
A 1 222 PRO 222 188 188 PRO PRO A . n 
A 1 223 GLY 223 189 189 GLY GLY A . n 
A 1 224 PHE 224 190 190 PHE PHE A . n 
A 1 225 ALA 225 191 191 ALA ALA A . n 
A 1 226 ARG 226 192 192 ARG ARG A . n 
A 1 227 LEU 227 193 193 LEU LEU A . n 
A 1 228 THR 228 194 194 THR THR A . n 
A 1 229 GLU 229 195 195 GLU GLU A . n 
A 1 230 SER 230 196 196 SER SER A . n 
A 1 231 LEU 231 197 197 LEU LEU A . n 
A 1 232 ILE 232 198 198 ILE ILE A . n 
A 1 233 GLU 233 199 199 GLU GLU A . n 
A 1 234 ALA 234 200 200 ALA ALA A . n 
A 1 235 GLU 235 201 201 GLU GLU A . n 
A 1 236 ASN 236 202 202 ASN ASN A . n 
A 1 237 ASP 237 203 203 ASP ASP A . n 
A 1 238 SER 238 204 204 SER SER A . n 
A 1 239 HIS 239 205 205 HIS HIS A . n 
A 1 240 GLY 240 206 206 GLY GLY A . n 
A 1 241 VAL 241 207 207 VAL VAL A . n 
A 1 242 ILE 242 208 208 ILE ILE A . n 
A 1 243 VAL 243 209 209 VAL VAL A . n 
A 1 244 ASN 244 210 210 ASN ASN A . n 
A 1 245 SER 245 211 211 SER SER A . n 
A 1 246 PHE 246 212 212 PHE PHE A . n 
A 1 247 ALA 247 213 213 ALA ALA A . n 
A 1 248 GLU 248 214 214 GLU GLU A . n 
A 1 249 LEU 249 215 215 LEU LEU A . n 
A 1 250 ASP 250 216 216 ASP ASP A . n 
A 1 251 GLU 251 217 217 GLU GLU A . n 
A 1 252 GLY 252 218 218 GLY GLY A . n 
A 1 253 TYR 253 219 219 TYR TYR A . n 
A 1 254 THR 254 220 220 THR THR A . n 
A 1 255 GLU 255 221 221 GLU GLU A . n 
A 1 256 TYR 256 222 222 TYR TYR A . n 
A 1 257 TYR 257 223 223 TYR TYR A . n 
A 1 258 GLU 258 224 224 GLU GLU A . n 
A 1 259 ASN 259 225 225 ASN ASN A . n 
A 1 260 LEU 260 226 226 LEU LEU A . n 
A 1 261 THR 261 227 227 THR THR A . n 
A 1 262 GLY 262 228 228 GLY GLY A . n 
A 1 263 ARG 263 229 229 ARG ARG A . n 
A 1 264 LYS 264 230 230 LYS LYS A . n 
A 1 265 VAL 265 231 231 VAL VAL A . n 
A 1 266 TRP 266 232 232 TRP TRP A . n 
A 1 267 HIS 267 233 233 HIS HIS A . n 
A 1 268 VAL 268 234 234 VAL VAL A . n 
A 1 269 GLY 269 235 235 GLY GLY A . n 
A 1 270 PRO 270 236 236 PRO PRO A . n 
A 1 271 THR 271 237 237 THR THR A . n 
A 1 272 SER 272 238 238 SER SER A . n 
A 1 273 LEU 273 239 239 LEU LEU A . n 
A 1 274 MET 274 240 240 MET MET A . n 
A 1 275 VAL 275 241 241 VAL VAL A . n 
A 1 276 GLU 276 242 242 GLU GLU A . n 
A 1 277 ILE 277 243 ?   ?   ?   A . n 
A 1 278 PRO 278 244 ?   ?   ?   A . n 
A 1 279 LYS 279 245 ?   ?   ?   A . n 
A 1 280 LYS 280 246 ?   ?   ?   A . n 
A 1 281 LYS 281 247 ?   ?   ?   A . n 
A 1 282 LYS 282 248 ?   ?   ?   A . n 
A 1 283 VAL 283 249 ?   ?   ?   A . n 
A 1 284 VAL 284 250 ?   ?   ?   A . n 
A 1 285 SER 285 251 ?   ?   ?   A . n 
A 1 286 THR 286 252 ?   ?   ?   A . n 
A 1 287 GLU 287 253 ?   ?   ?   A . n 
A 1 288 ASN 288 254 ?   ?   ?   A . n 
A 1 289 ASP 289 255 ?   ?   ?   A . n 
A 1 290 SER 290 256 ?   ?   ?   A . n 
A 1 291 SER 291 257 ?   ?   ?   A . n 
A 1 292 ILE 292 258 ?   ?   ?   A . n 
A 1 293 THR 293 259 ?   ?   ?   A . n 
A 1 294 LYS 294 260 260 LYS LYS A . n 
A 1 295 HIS 295 261 261 HIS HIS A . n 
A 1 296 GLN 296 262 262 GLN GLN A . n 
A 1 297 SER 297 263 263 SER SER A . n 
A 1 298 LEU 298 264 264 LEU LEU A . n 
A 1 299 THR 299 265 265 THR THR A . n 
A 1 300 TRP 300 266 266 TRP TRP A . n 
A 1 301 LEU 301 267 267 LEU LEU A . n 
A 1 302 ASP 302 268 268 ASP ASP A . n 
A 1 303 THR 303 269 269 THR THR A . n 
A 1 304 LYS 304 270 270 LYS LYS A . n 
A 1 305 GLU 305 271 271 GLU GLU A . n 
A 1 306 PRO 306 272 272 PRO PRO A . n 
A 1 307 SER 307 273 273 SER SER A . n 
A 1 308 SER 308 274 274 SER SER A . n 
A 1 309 VAL 309 275 275 VAL VAL A . n 
A 1 310 LEU 310 276 276 LEU LEU A . n 
A 1 311 TYR 311 277 277 TYR TYR A . n 
A 1 312 ILE 312 278 278 ILE ILE A . n 
A 1 313 SER 313 279 279 SER SER A . n 
A 1 314 PHE 314 280 280 PHE PHE A . n 
A 1 315 GLY 315 281 281 GLY GLY A . n 
A 1 316 SER 316 282 282 SER SER A . n 
A 1 317 LEU 317 283 283 LEU LEU A . n 
A 1 318 CYS 318 284 284 CYS CYS A . n 
A 1 319 ARG 319 285 285 ARG ARG A . n 
A 1 320 LEU 320 286 286 LEU LEU A . n 
A 1 321 SER 321 287 287 SER SER A . n 
A 1 322 ASN 322 288 288 ASN ASN A . n 
A 1 323 GLU 323 289 289 GLU GLU A . n 
A 1 324 GLN 324 290 290 GLN GLN A . n 
A 1 325 LEU 325 291 291 LEU LEU A . n 
A 1 326 LYS 326 292 292 LYS LYS A . n 
A 1 327 GLU 327 293 293 GLU GLU A . n 
A 1 328 MET 328 294 294 MET MET A . n 
A 1 329 ALA 329 295 295 ALA ALA A . n 
A 1 330 ASN 330 296 296 ASN ASN A . n 
A 1 331 GLY 331 297 297 GLY GLY A . n 
A 1 332 ILE 332 298 298 ILE ILE A . n 
A 1 333 GLU 333 299 299 GLU GLU A . n 
A 1 334 ALA 334 300 300 ALA ALA A . n 
A 1 335 SER 335 301 301 SER SER A . n 
A 1 336 LYS 336 302 302 LYS LYS A . n 
A 1 337 HIS 337 303 303 HIS HIS A . n 
A 1 338 GLN 338 304 304 GLN GLN A . n 
A 1 339 PHE 339 305 305 PHE PHE A . n 
A 1 340 LEU 340 306 306 LEU LEU A . n 
A 1 341 TRP 341 307 307 TRP TRP A . n 
A 1 342 VAL 342 308 308 VAL VAL A . n 
A 1 343 VAL 343 309 309 VAL VAL A . n 
A 1 344 HIS 344 310 310 HIS HIS A . n 
A 1 345 GLY 345 311 311 GLY GLY A . n 
A 1 346 LYS 346 312 312 LYS LYS A . n 
A 1 347 GLU 347 313 313 GLU GLU A . n 
A 1 348 GLY 348 314 314 GLY GLY A . n 
A 1 349 GLU 349 315 315 GLU GLU A . n 
A 1 350 ASP 350 316 316 ASP ASP A . n 
A 1 351 GLU 351 317 317 GLU GLU A . n 
A 1 352 ASP 352 318 318 ASP ASP A . n 
A 1 353 ASN 353 319 319 ASN ASN A . n 
A 1 354 TRP 354 320 320 TRP TRP A . n 
A 1 355 LEU 355 321 321 LEU LEU A . n 
A 1 356 PRO 356 322 322 PRO PRO A . n 
A 1 357 LYS 357 323 323 LYS LYS A . n 
A 1 358 GLY 358 324 324 GLY GLY A . n 
A 1 359 PHE 359 325 325 PHE PHE A . n 
A 1 360 VAL 360 326 326 VAL VAL A . n 
A 1 361 GLU 361 327 327 GLU GLU A . n 
A 1 362 ARG 362 328 328 ARG ARG A . n 
A 1 363 MET 363 329 329 MET MET A . n 
A 1 364 LYS 364 330 330 LYS LYS A . n 
A 1 365 GLU 365 331 331 GLU GLU A . n 
A 1 366 GLU 366 332 332 GLU GLU A . n 
A 1 367 LYS 367 333 333 LYS LYS A . n 
A 1 368 LYS 368 334 334 LYS LYS A . n 
A 1 369 GLY 369 335 335 GLY GLY A . n 
A 1 370 MET 370 336 336 MET MET A . n 
A 1 371 LEU 371 337 337 LEU LEU A . n 
A 1 372 ILE 372 338 338 ILE ILE A . n 
A 1 373 LYS 373 339 339 LYS LYS A . n 
A 1 374 GLY 374 340 340 GLY GLY A . n 
A 1 375 TRP 375 341 341 TRP TRP A . n 
A 1 376 VAL 376 342 342 VAL VAL A . n 
A 1 377 PRO 377 343 343 PRO PRO A . n 
A 1 378 GLN 378 344 344 GLN GLN A . n 
A 1 379 ALA 379 345 345 ALA ALA A . n 
A 1 380 LEU 380 346 346 LEU LEU A . n 
A 1 381 ILE 381 347 347 ILE ILE A . n 
A 1 382 LEU 382 348 348 LEU LEU A . n 
A 1 383 ASP 383 349 349 ASP ASP A . n 
A 1 384 HIS 384 350 350 HIS HIS A . n 
A 1 385 PRO 385 351 351 PRO PRO A . n 
A 1 386 SER 386 352 352 SER SER A . n 
A 1 387 ILE 387 353 353 ILE ILE A . n 
A 1 388 GLY 388 354 354 GLY GLY A . n 
A 1 389 GLY 389 355 355 GLY GLY A . n 
A 1 390 PHE 390 356 356 PHE PHE A . n 
A 1 391 LEU 391 357 357 LEU LEU A . n 
A 1 392 THR 392 358 358 THR THR A . n 
A 1 393 HIS 393 359 359 HIS HIS A . n 
A 1 394 CYS 394 360 360 CYS CYS A . n 
A 1 395 GLY 395 361 361 GLY GLY A . n 
A 1 396 TRP 396 362 362 TRP TRP A . n 
A 1 397 ASN 397 363 363 ASN ASN A . n 
A 1 398 ALA 398 364 364 ALA ALA A . n 
A 1 399 THR 399 365 365 THR THR A . n 
A 1 400 VAL 400 366 366 VAL VAL A . n 
A 1 401 GLU 401 367 367 GLU GLU A . n 
A 1 402 ALA 402 368 368 ALA ALA A . n 
A 1 403 ILE 403 369 369 ILE ILE A . n 
A 1 404 SER 404 370 370 SER SER A . n 
A 1 405 SER 405 371 371 SER SER A . n 
A 1 406 GLY 406 372 372 GLY GLY A . n 
A 1 407 VAL 407 373 373 VAL VAL A . n 
A 1 408 PRO 408 374 374 PRO PRO A . n 
A 1 409 MET 409 375 375 MET MET A . n 
A 1 410 VAL 410 376 376 VAL VAL A . n 
A 1 411 THR 411 377 377 THR THR A . n 
A 1 412 MET 412 378 378 MET MET A . n 
A 1 413 PRO 413 379 379 PRO PRO A . n 
A 1 414 GLY 414 380 380 GLY GLY A . n 
A 1 415 PHE 415 381 381 PHE PHE A . n 
A 1 416 GLY 416 382 382 GLY GLY A . n 
A 1 417 ASP 417 383 383 ASP ASP A . n 
A 1 418 GLN 418 384 384 GLN GLN A . n 
A 1 419 TYR 419 385 385 TYR TYR A . n 
A 1 420 TYR 420 386 386 TYR TYR A . n 
A 1 421 ASN 421 387 387 ASN ASN A . n 
A 1 422 GLU 422 388 388 GLU GLU A . n 
A 1 423 LYS 423 389 389 LYS LYS A . n 
A 1 424 LEU 424 390 390 LEU LEU A . n 
A 1 425 VAL 425 391 391 VAL VAL A . n 
A 1 426 THR 426 392 392 THR THR A . n 
A 1 427 GLU 427 393 393 GLU GLU A . n 
A 1 428 VAL 428 394 394 VAL VAL A . n 
A 1 429 HIS 429 395 395 HIS HIS A . n 
A 1 430 ARG 430 396 396 ARG ARG A . n 
A 1 431 ILE 431 397 397 ILE ILE A . n 
A 1 432 GLY 432 398 398 GLY GLY A . n 
A 1 433 VAL 433 399 399 VAL VAL A . n 
A 1 434 GLU 434 400 400 GLU GLU A . n 
A 1 435 VAL 435 401 401 VAL VAL A . n 
A 1 436 GLY 436 402 402 GLY GLY A . n 
A 1 437 ALA 437 403 403 ALA ALA A . n 
A 1 438 ALA 438 404 404 ALA ALA A . n 
A 1 439 GLU 439 405 405 GLU GLU A . n 
A 1 440 TRP 440 406 406 TRP TRP A . n 
A 1 441 SER 441 407 407 SER SER A . n 
A 1 442 MET 442 408 408 MET MET A . n 
A 1 443 SER 443 409 409 SER SER A . n 
A 1 444 PRO 444 410 410 PRO PRO A . n 
A 1 445 TYR 445 411 411 TYR TYR A . n 
A 1 446 ASP 446 412 412 ASP ASP A . n 
A 1 447 ALA 447 413 413 ALA ALA A . n 
A 1 448 LYS 448 414 414 LYS LYS A . n 
A 1 449 LYS 449 415 415 LYS LYS A . n 
A 1 450 THR 450 416 416 THR THR A . n 
A 1 451 VAL 451 417 417 VAL VAL A . n 
A 1 452 VAL 452 418 418 VAL VAL A . n 
A 1 453 ARG 453 419 419 ARG ARG A . n 
A 1 454 ALA 454 420 420 ALA ALA A . n 
A 1 455 GLU 455 421 421 GLU GLU A . n 
A 1 456 ARG 456 422 422 ARG ARG A . n 
A 1 457 ILE 457 423 423 ILE ILE A . n 
A 1 458 GLU 458 424 424 GLU GLU A . n 
A 1 459 LYS 459 425 425 LYS LYS A . n 
A 1 460 ALA 460 426 426 ALA ALA A . n 
A 1 461 VAL 461 427 427 VAL VAL A . n 
A 1 462 LYS 462 428 428 LYS LYS A . n 
A 1 463 LYS 463 429 429 LYS LYS A . n 
A 1 464 LEU 464 430 430 LEU LEU A . n 
A 1 465 MET 465 431 431 MET MET A . n 
A 1 466 ASP 466 432 432 ASP ASP A . n 
A 1 467 SER 467 433 433 SER SER A . n 
A 1 468 ASN 468 434 434 ASN ASN A . n 
A 1 469 GLY 469 435 435 GLY GLY A . n 
A 1 470 GLU 470 436 436 GLU GLU A . n 
A 1 471 GLY 471 437 437 GLY GLY A . n 
A 1 472 GLY 472 438 438 GLY GLY A . n 
A 1 473 GLU 473 439 439 GLU GLU A . n 
A 1 474 ILE 474 440 440 ILE ILE A . n 
A 1 475 ARG 475 441 441 ARG ARG A . n 
A 1 476 LYS 476 442 442 LYS LYS A . n 
A 1 477 ARG 477 443 443 ARG ARG A . n 
A 1 478 ALA 478 444 444 ALA ALA A . n 
A 1 479 LYS 479 445 445 LYS LYS A . n 
A 1 480 GLU 480 446 446 GLU GLU A . n 
A 1 481 MET 481 447 447 MET MET A . n 
A 1 482 LYS 482 448 448 LYS LYS A . n 
A 1 483 GLU 483 449 449 GLU GLU A . n 
A 1 484 LYS 484 450 450 LYS LYS A . n 
A 1 485 ALA 485 451 451 ALA ALA A . n 
A 1 486 TRP 486 452 452 TRP TRP A . n 
A 1 487 LYS 487 453 453 LYS LYS A . n 
A 1 488 ALA 488 454 454 ALA ALA A . n 
A 1 489 VAL 489 455 455 VAL VAL A . n 
A 1 490 GLN 490 456 456 GLN GLN A . n 
A 1 491 GLU 491 457 457 GLU GLU A . n 
A 1 492 GLY 492 458 458 GLY GLY A . n 
A 1 493 GLY 493 459 459 GLY GLY A . n 
A 1 494 SER 494 460 460 SER SER A . n 
A 1 495 SER 495 461 461 SER SER A . n 
A 1 496 GLN 496 462 462 GLN GLN A . n 
A 1 497 ASN 497 463 463 ASN ASN A . n 
A 1 498 CYS 498 464 464 CYS CYS A . n 
A 1 499 LEU 499 465 465 LEU LEU A . n 
A 1 500 THR 500 466 466 THR THR A . n 
A 1 501 LYS 501 467 467 LYS LYS A . n 
A 1 502 LEU 502 468 468 LEU LEU A . n 
A 1 503 VAL 503 469 469 VAL VAL A . n 
A 1 504 ASP 504 470 470 ASP ASP A . n 
A 1 505 TYR 505 471 471 TYR TYR A . n 
A 1 506 LEU 506 472 472 LEU LEU A . n 
A 1 507 HIS 507 473 473 HIS HIS A . n 
A 1 508 SER 508 474 474 SER SER A . n 
A 1 509 VAL 509 475 475 VAL VAL A . n 
A 1 510 VAL 510 476 476 VAL VAL A . n 
A 1 511 VAL 511 477 ?   ?   ?   A . n 
A 1 512 THR 512 478 ?   ?   ?   A . n 
A 1 513 LYS 513 479 ?   ?   ?   A . n 
A 1 514 SER 514 480 ?   ?   ?   A . n 
A 1 515 VAL 515 481 ?   ?   ?   A . n 
A 1 516 GLU 516 482 ?   ?   ?   A . n 
A 1 517 LEU 517 483 ?   ?   ?   A . n 
A 1 518 ASN 518 484 ?   ?   ?   A . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 CL  ? ? CL  ? ? 'SUBJECT OF INVESTIGATION' ? 
2 SO4 ? ? SO4 ? ? 'SUBJECT OF INVESTIGATION' ? 
3 UDP ? ? UDP ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 CL  1   501 503 CL  CL  A . 
C 3 SO4 1   502 504 SO4 SO4 A . 
D 3 SO4 1   503 505 SO4 SO4 A . 
E 3 SO4 1   504 508 SO4 SO4 A . 
F 2 CL  1   505 510 CL  CL  A . 
G 2 CL  1   506 512 CL  CL  A . 
H 3 SO4 1   507 513 SO4 SO4 A . 
I 4 UDP 1   508 514 UDP UDP A . 
J 5 HOH 1   601 62  HOH HOH A . 
J 5 HOH 2   602 131 HOH HOH A . 
J 5 HOH 3   603 75  HOH HOH A . 
J 5 HOH 4   604 99  HOH HOH A . 
J 5 HOH 5   605 138 HOH HOH A . 
J 5 HOH 6   606 17  HOH HOH A . 
J 5 HOH 7   607 21  HOH HOH A . 
J 5 HOH 8   608 8   HOH HOH A . 
J 5 HOH 9   609 4   HOH HOH A . 
J 5 HOH 10  610 9   HOH HOH A . 
J 5 HOH 11  611 83  HOH HOH A . 
J 5 HOH 12  612 116 HOH HOH A . 
J 5 HOH 13  613 5   HOH HOH A . 
J 5 HOH 14  614 2   HOH HOH A . 
J 5 HOH 15  615 11  HOH HOH A . 
J 5 HOH 16  616 27  HOH HOH A . 
J 5 HOH 17  617 89  HOH HOH A . 
J 5 HOH 18  618 55  HOH HOH A . 
J 5 HOH 19  619 56  HOH HOH A . 
J 5 HOH 20  620 95  HOH HOH A . 
J 5 HOH 21  621 70  HOH HOH A . 
J 5 HOH 22  622 10  HOH HOH A . 
J 5 HOH 23  623 28  HOH HOH A . 
J 5 HOH 24  624 120 HOH HOH A . 
J 5 HOH 25  625 37  HOH HOH A . 
J 5 HOH 26  626 98  HOH HOH A . 
J 5 HOH 27  627 96  HOH HOH A . 
J 5 HOH 28  628 15  HOH HOH A . 
J 5 HOH 29  629 26  HOH HOH A . 
J 5 HOH 30  630 77  HOH HOH A . 
J 5 HOH 31  631 71  HOH HOH A . 
J 5 HOH 32  632 134 HOH HOH A . 
J 5 HOH 33  633 61  HOH HOH A . 
J 5 HOH 34  634 39  HOH HOH A . 
J 5 HOH 35  635 33  HOH HOH A . 
J 5 HOH 36  636 143 HOH HOH A . 
J 5 HOH 37  637 43  HOH HOH A . 
J 5 HOH 38  638 19  HOH HOH A . 
J 5 HOH 39  639 90  HOH HOH A . 
J 5 HOH 40  640 24  HOH HOH A . 
J 5 HOH 41  641 20  HOH HOH A . 
J 5 HOH 42  642 67  HOH HOH A . 
J 5 HOH 43  643 141 HOH HOH A . 
J 5 HOH 44  644 13  HOH HOH A . 
J 5 HOH 45  645 88  HOH HOH A . 
J 5 HOH 46  646 36  HOH HOH A . 
J 5 HOH 47  647 45  HOH HOH A . 
J 5 HOH 48  648 137 HOH HOH A . 
J 5 HOH 49  649 35  HOH HOH A . 
J 5 HOH 50  650 14  HOH HOH A . 
J 5 HOH 51  651 1   HOH HOH A . 
J 5 HOH 52  652 108 HOH HOH A . 
J 5 HOH 53  653 86  HOH HOH A . 
J 5 HOH 54  654 93  HOH HOH A . 
J 5 HOH 55  655 32  HOH HOH A . 
J 5 HOH 56  656 38  HOH HOH A . 
J 5 HOH 57  657 106 HOH HOH A . 
J 5 HOH 58  658 82  HOH HOH A . 
J 5 HOH 59  659 7   HOH HOH A . 
J 5 HOH 60  660 44  HOH HOH A . 
J 5 HOH 61  661 22  HOH HOH A . 
J 5 HOH 62  662 3   HOH HOH A . 
J 5 HOH 63  663 40  HOH HOH A . 
J 5 HOH 64  664 97  HOH HOH A . 
J 5 HOH 65  665 112 HOH HOH A . 
J 5 HOH 66  666 34  HOH HOH A . 
J 5 HOH 67  667 6   HOH HOH A . 
J 5 HOH 68  668 73  HOH HOH A . 
J 5 HOH 69  669 114 HOH HOH A . 
J 5 HOH 70  670 91  HOH HOH A . 
J 5 HOH 71  671 48  HOH HOH A . 
J 5 HOH 72  672 146 HOH HOH A . 
J 5 HOH 73  673 74  HOH HOH A . 
J 5 HOH 74  674 100 HOH HOH A . 
J 5 HOH 75  675 16  HOH HOH A . 
J 5 HOH 76  676 142 HOH HOH A . 
J 5 HOH 77  677 54  HOH HOH A . 
J 5 HOH 78  678 76  HOH HOH A . 
J 5 HOH 79  679 115 HOH HOH A . 
J 5 HOH 80  680 66  HOH HOH A . 
J 5 HOH 81  681 49  HOH HOH A . 
J 5 HOH 82  682 52  HOH HOH A . 
J 5 HOH 83  683 133 HOH HOH A . 
J 5 HOH 84  684 84  HOH HOH A . 
J 5 HOH 85  685 69  HOH HOH A . 
J 5 HOH 86  686 105 HOH HOH A . 
J 5 HOH 87  687 118 HOH HOH A . 
J 5 HOH 88  688 42  HOH HOH A . 
J 5 HOH 89  689 111 HOH HOH A . 
J 5 HOH 90  690 50  HOH HOH A . 
J 5 HOH 91  691 25  HOH HOH A . 
J 5 HOH 92  692 18  HOH HOH A . 
J 5 HOH 93  693 79  HOH HOH A . 
J 5 HOH 94  694 125 HOH HOH A . 
J 5 HOH 95  695 29  HOH HOH A . 
J 5 HOH 96  696 109 HOH HOH A . 
J 5 HOH 97  697 102 HOH HOH A . 
J 5 HOH 98  698 78  HOH HOH A . 
J 5 HOH 99  699 122 HOH HOH A . 
J 5 HOH 100 700 58  HOH HOH A . 
J 5 HOH 101 701 107 HOH HOH A . 
J 5 HOH 102 702 139 HOH HOH A . 
J 5 HOH 103 703 85  HOH HOH A . 
J 5 HOH 104 704 59  HOH HOH A . 
J 5 HOH 105 705 80  HOH HOH A . 
J 5 HOH 106 706 103 HOH HOH A . 
J 5 HOH 107 707 68  HOH HOH A . 
J 5 HOH 108 708 53  HOH HOH A . 
J 5 HOH 109 709 51  HOH HOH A . 
J 5 HOH 110 710 12  HOH HOH A . 
J 5 HOH 111 711 60  HOH HOH A . 
J 5 HOH 112 712 72  HOH HOH A . 
J 5 HOH 113 713 124 HOH HOH A . 
J 5 HOH 114 714 57  HOH HOH A . 
J 5 HOH 115 715 63  HOH HOH A . 
J 5 HOH 116 716 147 HOH HOH A . 
J 5 HOH 117 717 119 HOH HOH A . 
J 5 HOH 118 718 23  HOH HOH A . 
J 5 HOH 119 719 140 HOH HOH A . 
J 5 HOH 120 720 150 HOH HOH A . 
J 5 HOH 121 721 144 HOH HOH A . 
J 5 HOH 122 722 47  HOH HOH A . 
J 5 HOH 123 723 30  HOH HOH A . 
J 5 HOH 124 724 46  HOH HOH A . 
J 5 HOH 125 725 92  HOH HOH A . 
J 5 HOH 126 726 41  HOH HOH A . 
J 5 HOH 127 727 126 HOH HOH A . 
J 5 HOH 128 728 149 HOH HOH A . 
J 5 HOH 129 729 65  HOH HOH A . 
J 5 HOH 130 730 148 HOH HOH A . 
J 5 HOH 131 731 117 HOH HOH A . 
J 5 HOH 132 732 87  HOH HOH A . 
J 5 HOH 133 733 128 HOH HOH A . 
J 5 HOH 134 734 123 HOH HOH A . 
J 5 HOH 135 735 64  HOH HOH A . 
J 5 HOH 136 736 113 HOH HOH A . 
J 5 HOH 137 737 104 HOH HOH A . 
J 5 HOH 138 738 145 HOH HOH A . 
J 5 HOH 139 739 127 HOH HOH A . 
J 5 HOH 140 740 129 HOH HOH A . 
J 5 HOH 141 741 135 HOH HOH A . 
J 5 HOH 142 742 31  HOH HOH A . 
J 5 HOH 143 743 130 HOH HOH A . 
J 5 HOH 144 744 132 HOH HOH A . 
J 5 HOH 145 745 121 HOH HOH A . 
J 5 HOH 146 746 110 HOH HOH A . 
J 5 HOH 147 747 101 HOH HOH A . 
J 5 HOH 148 748 94  HOH HOH A . 
J 5 HOH 149 749 136 HOH HOH A . 
J 5 HOH 150 750 81  HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A PHE 86  ? CG  ? A PHE 120 CG  
2  1 Y 1 A PHE 86  ? CD1 ? A PHE 120 CD1 
3  1 Y 1 A PHE 86  ? CD2 ? A PHE 120 CD2 
4  1 Y 1 A PHE 86  ? CE1 ? A PHE 120 CE1 
5  1 Y 1 A PHE 86  ? CE2 ? A PHE 120 CE2 
6  1 Y 1 A PHE 86  ? CZ  ? A PHE 120 CZ  
7  1 Y 1 A GLU 195 ? CB  ? A GLU 229 CB  
8  1 Y 1 A GLU 195 ? CG  ? A GLU 229 CG  
9  1 Y 1 A GLU 195 ? CD  ? A GLU 229 CD  
10 1 Y 1 A GLU 195 ? OE1 ? A GLU 229 OE1 
11 1 Y 1 A GLU 195 ? OE2 ? A GLU 229 OE2 
12 1 Y 1 A LYS 323 ? CG  ? A LYS 357 CG  
13 1 Y 1 A LYS 323 ? CD  ? A LYS 357 CD  
14 1 Y 1 A LYS 323 ? CE  ? A LYS 357 CE  
15 1 Y 1 A LYS 323 ? NZ  ? A LYS 357 NZ  
# 
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_reference_DOI 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.20.1_4487    ? 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? 'Jun 30, 2024' ? 2 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.20.1-4487    ? 3 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? 'Jun 30, 2024' ? 4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9UCE 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     91.500 
_cell.length_a_esd                 ? 
_cell.length_b                     91.500 
_cell.length_b_esd                 ? 
_cell.length_c                     167.000 
_cell.length_c_esd                 ? 
_cell.volume                       1398165.750 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9UCE 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                96 
_symmetry.space_group_name_Hall            'P 4nw 2abw' 
_symmetry.space_group_name_H-M             'P 43 21 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9UCE 
_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             3.04 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          59.54 
_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    'sodium citrate, K/Na tartrate, ammonium sulfate' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS 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         2025-03-22 
_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   0.97946 
_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 BL18U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97946 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL18U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9UCE 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.2 
_reflns.d_resolution_low                               50 
_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                                     36792 
_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                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                24.67 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          15.51 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.2 
_reflns_shell.d_res_low                                     2.33 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           3.95 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             5809 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               24.41 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               0.753 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.962 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.9 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               47.46 
_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                                 9UCE 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.20 
_refine.ls_d_res_low                             44.12 
_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                     36769 
_refine.ls_number_reflns_R_free                  1838 
_refine.ls_number_reflns_R_work                  34931 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.96 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1846 
_refine.ls_R_factor_R_free                       0.2077 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1834 
_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.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_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                          1.35 
_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       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 19.2380 
_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                            0.1718 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.20 
_refine_hist.d_res_low                        44.12 
_refine_hist.number_atoms_solvent             150 
_refine_hist.number_atoms_total               3745 
_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        3547 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         48 
_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_Zscore 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0037  ? 3677 ? f_bond_d           ? ? ? 
'X-RAY DIFFRACTION' ? 0.5863  ? 4990 ? f_angle_d          ? ? ? 
'X-RAY DIFFRACTION' ? 0.0442  ? 547  ? f_chiral_restr     ? ? ? 
'X-RAY DIFFRACTION' ? 0.0044  ? 633  ? f_plane_restr      ? ? ? 
'X-RAY DIFFRACTION' ? 14.9047 ? 1335 ? f_dihedral_angle_d ? ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.correlation_coeff_Fo_to_Fc 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.20 2.26  . . 137 2608 99.89  . . . . 0.2047 . . . . . . . . . . . . . . . 0.2365 
'X-RAY DIFFRACTION' 2.26 2.33  . . 139 2650 100.00 . . . . 0.2021 . . . . . . . . . . . . . . . 0.2304 
'X-RAY DIFFRACTION' 2.33 2.40  . . 140 2658 99.96  . . . . 0.1965 . . . . . . . . . . . . . . . 0.2454 
'X-RAY DIFFRACTION' 2.40 2.49  . . 138 2625 99.96  . . . . 0.2070 . . . . . . . . . . . . . . . 0.2426 
'X-RAY DIFFRACTION' 2.49 2.59  . . 140 2653 100.00 . . . . 0.2006 . . . . . . . . . . . . . . . 0.2431 
'X-RAY DIFFRACTION' 2.59 2.70  . . 140 2649 99.96  . . . . 0.1963 . . . . . . . . . . . . . . . 0.2490 
'X-RAY DIFFRACTION' 2.70 2.85  . . 140 2661 100.00 . . . . 0.1920 . . . . . . . . . . . . . . . 0.2137 
'X-RAY DIFFRACTION' 2.85 3.02  . . 140 2668 100.00 . . . . 0.1984 . . . . . . . . . . . . . . . 0.2349 
'X-RAY DIFFRACTION' 3.03 3.26  . . 141 2680 100.00 . . . . 0.1969 . . . . . . . . . . . . . . . 0.2242 
'X-RAY DIFFRACTION' 3.26 3.59  . . 142 2702 100.00 . . . . 0.1784 . . . . . . . . . . . . . . . 0.2264 
'X-RAY DIFFRACTION' 3.59 4.10  . . 142 2699 100.00 . . . . 0.1615 . . . . . . . . . . . . . . . 0.1783 
'X-RAY DIFFRACTION' 4.11 5.17  . . 146 2769 100.00 . . . . 0.1573 . . . . . . . . . . . . . . . 0.1769 
'X-RAY DIFFRACTION' 5.17 44.12 . . 153 2909 99.80  . . . . 0.1954 . . . . . . . . . . . . . . . 0.1927 
# 
_struct.entry_id                     9UCE 
_struct.title                        'Crystal structure of glycosyltransferase UGT73K1 in complex with UDP' 
_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        9UCE 
_struct_keywords.text            'Glycosyltransferase, UDP, TRANSFERASE' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 3 ? 
F N N 2 ? 
G N N 2 ? 
H N N 3 ? 
I N N 4 ? 
J N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q5IFH8_MEDTR 
_struct_ref.pdbx_db_accession          Q5IFH8 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MGTESKPLKIYMLPFFAQGHLIPLVNLARLVASKNQHVTIITTPSNAQLFDKTIEEEKAAGHHIRVHIIKFPSAQLGLPT
GVENLFAASDNQTAGKIHMAAHFVKADIEEFMKENPPDVFISDIIFTWSESTAKNLQIPRLVFNPISIFDVCMIQAIQSH
PESFVSDSGPYQIHGLPHPLTLPIKPSPGFARLTESLIEAENDSHGVIVNSFAELDEGYTEYYENLTGRKVWHVGPTSLM
VEIPKKKKVVSTENDSSITKHQSLTWLDTKEPSSVLYISFGSLCRLSNEQLKEMANGIEASKHQFLWVVHGKEGEDEDNW
LPKGFVERMKEEKKGMLIKGWVPQALILDHPSIGGFLTHCGWNATVEAISSGVPMVTMPGFGDQYYNEKLVTEVHRIGVE
VGAAEWSMSPYDAKKTVVRAERIEKAVKKLMDSNGEGGEIRKRAKEMKEKAWKAVQEGGSSQNCLTKLVDYLHSVVVTKS
VELN
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9UCE 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 35 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 518 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q5IFH8 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  484 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       484 
# 
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 9UCE MET A 1  ? UNP Q5IFH8 ? ? 'initiating methionine' -33 1  
1 9UCE GLY A 2  ? UNP Q5IFH8 ? ? 'expression tag'        -32 2  
1 9UCE SER A 3  ? UNP Q5IFH8 ? ? 'expression tag'        -31 3  
1 9UCE SER A 4  ? UNP Q5IFH8 ? ? 'expression tag'        -30 4  
1 9UCE HIS A 5  ? UNP Q5IFH8 ? ? 'expression tag'        -29 5  
1 9UCE HIS A 6  ? UNP Q5IFH8 ? ? 'expression tag'        -28 6  
1 9UCE HIS A 7  ? UNP Q5IFH8 ? ? 'expression tag'        -27 7  
1 9UCE HIS A 8  ? UNP Q5IFH8 ? ? 'expression tag'        -26 8  
1 9UCE HIS A 9  ? UNP Q5IFH8 ? ? 'expression tag'        -25 9  
1 9UCE HIS A 10 ? UNP Q5IFH8 ? ? 'expression tag'        -24 10 
1 9UCE SER A 11 ? UNP Q5IFH8 ? ? 'expression tag'        -23 11 
1 9UCE SER A 12 ? UNP Q5IFH8 ? ? 'expression tag'        -22 12 
1 9UCE GLY A 13 ? UNP Q5IFH8 ? ? 'expression tag'        -21 13 
1 9UCE LEU A 14 ? UNP Q5IFH8 ? ? 'expression tag'        -20 14 
1 9UCE VAL A 15 ? UNP Q5IFH8 ? ? 'expression tag'        -19 15 
1 9UCE PRO A 16 ? UNP Q5IFH8 ? ? 'expression tag'        -18 16 
1 9UCE ARG A 17 ? UNP Q5IFH8 ? ? 'expression tag'        -17 17 
1 9UCE GLY A 18 ? UNP Q5IFH8 ? ? 'expression tag'        -16 18 
1 9UCE SER A 19 ? UNP Q5IFH8 ? ? 'expression tag'        -15 19 
1 9UCE HIS A 20 ? UNP Q5IFH8 ? ? 'expression tag'        -14 20 
1 9UCE MET A 21 ? UNP Q5IFH8 ? ? 'expression tag'        -13 21 
1 9UCE ALA A 22 ? UNP Q5IFH8 ? ? 'expression tag'        -12 22 
1 9UCE SER A 23 ? UNP Q5IFH8 ? ? 'expression tag'        -11 23 
1 9UCE MET A 24 ? UNP Q5IFH8 ? ? 'expression tag'        -10 24 
1 9UCE THR A 25 ? UNP Q5IFH8 ? ? 'expression tag'        -9  25 
1 9UCE GLY A 26 ? UNP Q5IFH8 ? ? 'expression tag'        -8  26 
1 9UCE GLY A 27 ? UNP Q5IFH8 ? ? 'expression tag'        -7  27 
1 9UCE GLN A 28 ? UNP Q5IFH8 ? ? 'expression tag'        -6  28 
1 9UCE GLN A 29 ? UNP Q5IFH8 ? ? 'expression tag'        -5  29 
1 9UCE MET A 30 ? UNP Q5IFH8 ? ? 'expression tag'        -4  30 
1 9UCE GLY A 31 ? UNP Q5IFH8 ? ? 'expression tag'        -3  31 
1 9UCE ARG A 32 ? UNP Q5IFH8 ? ? 'expression tag'        -2  32 
1 9UCE GLY A 33 ? UNP Q5IFH8 ? ? 'expression tag'        -1  33 
1 9UCE SER A 34 ? UNP Q5IFH8 ? ? 'expression tag'        0   34 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 260   ? 
1 MORE         -19   ? 
1 'SSA (A^2)'  19530 ? 
# 
_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,I,J 
# 
_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 ALA A 51  ? SER A 67  ? ALA A 17  SER A 33  1 ? 17 
HELX_P HELX_P2  AA2 THR A 77  ? GLN A 82  ? THR A 43  GLN A 48  1 ? 6  
HELX_P HELX_P3  AA3 PHE A 84  ? ALA A 94  ? PHE A 50  ALA A 60  1 ? 11 
HELX_P HELX_P4  AA4 PRO A 106 ? GLY A 111 ? PRO A 72  GLY A 77  1 ? 6  
HELX_P HELX_P5  AA5 ASN A 118 ? ALA A 122 ? ASN A 84  ALA A 88  5 ? 5  
HELX_P HELX_P6  AA6 ASP A 124 ? VAL A 138 ? ASP A 90  VAL A 104 1 ? 15 
HELX_P HELX_P7  AA7 VAL A 138 ? ASN A 149 ? VAL A 104 ASN A 115 1 ? 12 
HELX_P HELX_P8  AA8 TRP A 162 ? LEU A 170 ? TRP A 128 LEU A 136 1 ? 9  
HELX_P HELX_P9  AA9 ILE A 182 ? SER A 193 ? ILE A 148 SER A 159 1 ? 12 
HELX_P HELX_P10 AB1 HIS A 194 ? VAL A 199 ? HIS A 160 VAL A 165 5 ? 6  
HELX_P HELX_P11 AB2 THR A 228 ? GLU A 233 ? THR A 194 GLU A 199 1 ? 6  
HELX_P HELX_P12 AB3 PHE A 246 ? GLU A 251 ? PHE A 212 GLU A 217 1 ? 6  
HELX_P HELX_P13 AB4 GLY A 252 ? GLY A 262 ? GLY A 218 GLY A 228 1 ? 11 
HELX_P HELX_P14 AB5 PRO A 270 ? VAL A 275 ? PRO A 236 VAL A 241 1 ? 6  
HELX_P HELX_P15 AB6 HIS A 295 ? ASP A 302 ? HIS A 261 ASP A 268 1 ? 8  
HELX_P HELX_P16 AB7 SER A 321 ? LYS A 336 ? SER A 287 LYS A 302 1 ? 16 
HELX_P HELX_P17 AB8 ASP A 350 ? TRP A 354 ? ASP A 316 TRP A 320 5 ? 5  
HELX_P HELX_P18 AB9 GLY A 358 ? GLU A 366 ? GLY A 324 GLU A 332 1 ? 9  
HELX_P HELX_P19 AC1 PRO A 377 ? HIS A 384 ? PRO A 343 HIS A 350 1 ? 8  
HELX_P HELX_P20 AC2 GLY A 395 ? GLY A 406 ? GLY A 361 GLY A 372 1 ? 12 
HELX_P HELX_P21 AC3 ASP A 417 ? GLU A 427 ? ASP A 383 GLU A 393 1 ? 11 
HELX_P HELX_P22 AC4 ARG A 453 ? ASP A 466 ? ARG A 419 ASP A 432 1 ? 14 
HELX_P HELX_P23 AC5 GLU A 470 ? GLN A 490 ? GLU A 436 GLN A 456 1 ? 21 
HELX_P HELX_P24 AC6 GLY A 493 ? VAL A 510 ? GLY A 459 VAL A 476 1 ? 18 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 GLY 203 A . ? GLY 169 A PRO 204 A ? PRO 170 A 1 0.63  
2 GLY 269 A . ? GLY 235 A PRO 270 A ? PRO 236 A 1 -4.86 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 2 ? 
AA3 ? 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      
AA1 6 7 ? parallel      
AA2 1 2 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA3 4 5 ? parallel      
AA3 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 ILE A 98  ? ILE A 102 ? ILE A 64  ILE A 68  
AA1 2 HIS A 71  ? THR A 76  ? HIS A 37  THR A 42  
AA1 3 LYS A 43  ? LEU A 47  ? LYS A 9   LEU A 13  
AA1 4 VAL A 153 ? ASP A 157 ? VAL A 119 ASP A 123 
AA1 5 ARG A 174 ? ASN A 178 ? ARG A 140 ASN A 144 
AA1 6 VAL A 241 ? VAL A 243 ? VAL A 207 VAL A 209 
AA1 7 VAL A 265 ? HIS A 267 ? VAL A 231 HIS A 233 
AA2 1 TYR A 205 ? ILE A 207 ? TYR A 171 ILE A 173 
AA2 2 LEU A 214 ? LEU A 216 ? LEU A 180 LEU A 182 
AA3 1 GLY A 369 ? LYS A 373 ? GLY A 335 LYS A 339 
AA3 2 GLN A 338 ? VAL A 343 ? GLN A 304 VAL A 309 
AA3 3 VAL A 309 ? SER A 313 ? VAL A 275 SER A 279 
AA3 4 ILE A 387 ? THR A 392 ? ILE A 353 THR A 358 
AA3 5 MET A 409 ? THR A 411 ? MET A 375 THR A 377 
AA3 6 GLY A 432 ? GLU A 434 ? GLY A 398 GLU A 400 
# 
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 ARG A 99  ? O ARG A 65  N ILE A 74  ? N ILE A 40  
AA1 2 3 O HIS A 71  ? O HIS A 37  N ILE A 44  ? N ILE A 10  
AA1 3 4 N TYR A 45  ? N TYR A 11  O ILE A 155 ? O ILE A 121 
AA1 4 5 N SER A 156 ? N SER A 122 O PHE A 177 ? O PHE A 143 
AA1 5 6 N ASN A 178 ? N ASN A 144 O ILE A 242 ? O ILE A 208 
AA1 6 7 N VAL A 243 ? N VAL A 209 O TRP A 266 ? O TRP A 232 
AA2 1 2 N ILE A 207 ? N ILE A 173 O LEU A 214 ? O LEU A 180 
AA3 1 2 O ILE A 372 ? O ILE A 338 N TRP A 341 ? N TRP A 307 
AA3 2 3 O LEU A 340 ? O LEU A 306 N ILE A 312 ? N ILE A 278 
AA3 3 4 N TYR A 311 ? N TYR A 277 O GLY A 389 ? O GLY A 355 
AA3 4 5 N PHE A 390 ? N PHE A 356 O VAL A 410 ? O VAL A 376 
AA3 5 6 N THR A 411 ? N THR A 377 O VAL A 433 ? O VAL A 399 
# 
_pdbx_entry_details.entry_id                   9UCE 
_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_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 LYS A 34  ? ? -99.84  32.42 
2 1 PHE A 50  ? ? -149.21 11.46 
3 1 PHE A 126 ? ? -69.93  80.79 
4 1 CYS A 284 ? ? -91.45  41.72 
# 
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 -35.516808067  10.9489975791 -36.3737992055 0.264416416946 ? -0.0166358618251 ? -0.0384218984454  
? 0.27537291985  ? 0.0572082562133  ? 0.26665948804  ? 0.795053520745 ? -0.170719574451  ? -0.00915014035115 ? 0.500489064743 ? 
0.0852550156834 ? 0.234869647282 ? 0.00957825280499 ? 0.0862555293299  ? 0.0439796695664  ? -0.250749123883  ? 0.0771153904062 ? 
0.105355711604   ? -0.0842490860425 ? -0.0784402697291  ? 3.00439758956e-09 ? 
2 'X-RAY DIFFRACTION' ? refined -16.4599697789 23.5945952221 -10.8610750412 0.412978301927 ? 0.00275260505097 ? -0.0211028571842  
? 0.386836769909 ? -0.0281132129054 ? 0.26579521367  ? 0.337133563747 ? -0.266500329424  ? 0.247277110456    ? 1.46972106955  ? 
0.501057924709  ? 1.0320164782   ? -0.0509789978176 ? -0.346897247726  ? 0.0482279982762  ? 0.656480298941   ? 0.199752341278  ? 
-0.0570523576366 ? 0.170476824874   ? -0.00154232783627 ? 0.00648977951799  ? 
3 'X-RAY DIFFRACTION' ? refined -23.6562358801 17.5372106899 -28.5124217515 0.241225506701 ? 0.00248225342882 ? 0.0121147360408   
? 0.227759327405 ? 0.0192797495547  ? 0.216787482532 ? 0.933159384451 ? 0.441662198004   ? 0.189553048133    ? 1.40841662516  ? 
0.322445516603  ? 1.0490873537   ? -0.0201413720472 ? -0.136975708736  ? 0.124147670467   ? -0.0999836470493 ? 0.0888523678205 ? 
-0.0992285923455 ? -0.0493653539314 ? 0.00768160968797  ? 0.000243527309008 ? 
4 'X-RAY DIFFRACTION' ? refined -39.4049522864 4.66569444317 -24.6859717222 0.222751148484 ? 0.00671182129669 ? -0.00527579484798 
? 0.256483028839 ? 0.0700785141389  ? 0.268636561151 ? 0.86530102427  ? -0.0760820554208 ? -0.0158901032852  ? 1.53400551357  ? 
-0.207196536898 ? 1.3688059681   ? -0.125412176674  ? -0.0928596857296 ? -0.0894125243042 ? 0.0193239720395  ? 0.20970468647   ? 
0.234470449907   ? 0.113277069564   ? -0.190938125694   ? 1.53266390196e-07 ? 
# 
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 A 189 A 195 ? A 238 A 261 ? ? 
;chain 'A' and (resid 195 through 261 )
;
2 'X-RAY DIFFRACTION' 2 A 239 A 262 ? A 338 A 361 ? ? 
;chain 'A' and (resid 262 through 361 )
;
3 'X-RAY DIFFRACTION' 3 A 339 A 362 ? A 453 A 476 ? ? 
;chain 'A' and (resid 362 through 476 )
;
4 'X-RAY DIFFRACTION' 4 A 1   A 7   ? A 188 A 194 ? ? 
;chain 'A' and (resid 7 through 194 )
;
# 
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 -33 ? A MET 1   
2  1 Y 1 A GLY -32 ? A GLY 2   
3  1 Y 1 A SER -31 ? A SER 3   
4  1 Y 1 A SER -30 ? A SER 4   
5  1 Y 1 A HIS -29 ? A HIS 5   
6  1 Y 1 A HIS -28 ? A HIS 6   
7  1 Y 1 A HIS -27 ? A HIS 7   
8  1 Y 1 A HIS -26 ? A HIS 8   
9  1 Y 1 A HIS -25 ? A HIS 9   
10 1 Y 1 A HIS -24 ? A HIS 10  
11 1 Y 1 A SER -23 ? A SER 11  
12 1 Y 1 A SER -22 ? A SER 12  
13 1 Y 1 A GLY -21 ? A GLY 13  
14 1 Y 1 A LEU -20 ? A LEU 14  
15 1 Y 1 A VAL -19 ? A VAL 15  
16 1 Y 1 A PRO -18 ? A PRO 16  
17 1 Y 1 A ARG -17 ? A ARG 17  
18 1 Y 1 A GLY -16 ? A GLY 18  
19 1 Y 1 A SER -15 ? A SER 19  
20 1 Y 1 A HIS -14 ? A HIS 20  
21 1 Y 1 A MET -13 ? A MET 21  
22 1 Y 1 A ALA -12 ? A ALA 22  
23 1 Y 1 A SER -11 ? A SER 23  
24 1 Y 1 A MET -10 ? A MET 24  
25 1 Y 1 A THR -9  ? A THR 25  
26 1 Y 1 A GLY -8  ? A GLY 26  
27 1 Y 1 A GLY -7  ? A GLY 27  
28 1 Y 1 A GLN -6  ? A GLN 28  
29 1 Y 1 A GLN -5  ? A GLN 29  
30 1 Y 1 A MET -4  ? A MET 30  
31 1 Y 1 A GLY -3  ? A GLY 31  
32 1 Y 1 A ARG -2  ? A ARG 32  
33 1 Y 1 A GLY -1  ? A GLY 33  
34 1 Y 1 A SER 0   ? A SER 34  
35 1 Y 1 A MET 1   ? A MET 35  
36 1 Y 1 A GLY 2   ? A GLY 36  
37 1 Y 1 A THR 3   ? A THR 37  
38 1 Y 1 A GLU 4   ? A GLU 38  
39 1 Y 1 A SER 5   ? A SER 39  
40 1 Y 1 A LYS 6   ? A LYS 40  
41 1 Y 1 A ILE 243 ? A ILE 277 
42 1 Y 1 A PRO 244 ? A PRO 278 
43 1 Y 1 A LYS 245 ? A LYS 279 
44 1 Y 1 A LYS 246 ? A LYS 280 
45 1 Y 1 A LYS 247 ? A LYS 281 
46 1 Y 1 A LYS 248 ? A LYS 282 
47 1 Y 1 A VAL 249 ? A VAL 283 
48 1 Y 1 A VAL 250 ? A VAL 284 
49 1 Y 1 A SER 251 ? A SER 285 
50 1 Y 1 A THR 252 ? A THR 286 
51 1 Y 1 A GLU 253 ? A GLU 287 
52 1 Y 1 A ASN 254 ? A ASN 288 
53 1 Y 1 A ASP 255 ? A ASP 289 
54 1 Y 1 A SER 256 ? A SER 290 
55 1 Y 1 A SER 257 ? A SER 291 
56 1 Y 1 A ILE 258 ? A ILE 292 
57 1 Y 1 A THR 259 ? A THR 293 
58 1 Y 1 A VAL 477 ? A VAL 511 
59 1 Y 1 A THR 478 ? A THR 512 
60 1 Y 1 A LYS 479 ? A LYS 513 
61 1 Y 1 A SER 480 ? A SER 514 
62 1 Y 1 A VAL 481 ? A VAL 515 
63 1 Y 1 A GLU 482 ? A GLU 516 
64 1 Y 1 A LEU 483 ? A LEU 517 
65 1 Y 1 A ASN 484 ? A ASN 518 
# 
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  
CL  CL     CL N N 74  
CYS N      N  N N 75  
CYS CA     C  N R 76  
CYS C      C  N N 77  
CYS O      O  N N 78  
CYS CB     C  N N 79  
CYS SG     S  N N 80  
CYS OXT    O  N N 81  
CYS H      H  N N 82  
CYS H2     H  N N 83  
CYS HA     H  N N 84  
CYS HB2    H  N N 85  
CYS HB3    H  N N 86  
CYS HG     H  N N 87  
CYS HXT    H  N N 88  
GLN N      N  N N 89  
GLN CA     C  N S 90  
GLN C      C  N N 91  
GLN O      O  N N 92  
GLN CB     C  N N 93  
GLN CG     C  N N 94  
GLN CD     C  N N 95  
GLN OE1    O  N N 96  
GLN NE2    N  N N 97  
GLN OXT    O  N N 98  
GLN H      H  N N 99  
GLN H2     H  N N 100 
GLN HA     H  N N 101 
GLN HB2    H  N N 102 
GLN HB3    H  N N 103 
GLN HG2    H  N N 104 
GLN HG3    H  N N 105 
GLN HE21   H  N N 106 
GLN HE22   H  N N 107 
GLN HXT    H  N N 108 
GLU N      N  N N 109 
GLU CA     C  N S 110 
GLU C      C  N N 111 
GLU O      O  N N 112 
GLU CB     C  N N 113 
GLU CG     C  N N 114 
GLU CD     C  N N 115 
GLU OE1    O  N N 116 
GLU OE2    O  N N 117 
GLU OXT    O  N N 118 
GLU H      H  N N 119 
GLU H2     H  N N 120 
GLU HA     H  N N 121 
GLU HB2    H  N N 122 
GLU HB3    H  N N 123 
GLU HG2    H  N N 124 
GLU HG3    H  N N 125 
GLU HE2    H  N N 126 
GLU HXT    H  N N 127 
GLY N      N  N N 128 
GLY CA     C  N N 129 
GLY C      C  N N 130 
GLY O      O  N N 131 
GLY OXT    O  N N 132 
GLY H      H  N N 133 
GLY H2     H  N N 134 
GLY HA2    H  N N 135 
GLY HA3    H  N N 136 
GLY HXT    H  N N 137 
HIS N      N  N N 138 
HIS CA     C  N S 139 
HIS C      C  N N 140 
HIS O      O  N N 141 
HIS CB     C  N N 142 
HIS CG     C  Y N 143 
HIS ND1    N  Y N 144 
HIS CD2    C  Y N 145 
HIS CE1    C  Y N 146 
HIS NE2    N  Y N 147 
HIS OXT    O  N N 148 
HIS H      H  N N 149 
HIS H2     H  N N 150 
HIS HA     H  N N 151 
HIS HB2    H  N N 152 
HIS HB3    H  N N 153 
HIS HD1    H  N N 154 
HIS HD2    H  N N 155 
HIS HE1    H  N N 156 
HIS HE2    H  N N 157 
HIS HXT    H  N N 158 
HOH O      O  N N 159 
HOH H1     H  N N 160 
HOH H2     H  N N 161 
ILE N      N  N N 162 
ILE CA     C  N S 163 
ILE C      C  N N 164 
ILE O      O  N N 165 
ILE CB     C  N S 166 
ILE CG1    C  N N 167 
ILE CG2    C  N N 168 
ILE CD1    C  N N 169 
ILE OXT    O  N N 170 
ILE H      H  N N 171 
ILE H2     H  N N 172 
ILE HA     H  N N 173 
ILE HB     H  N N 174 
ILE HG12   H  N N 175 
ILE HG13   H  N N 176 
ILE HG21   H  N N 177 
ILE HG22   H  N N 178 
ILE HG23   H  N N 179 
ILE HD11   H  N N 180 
ILE HD12   H  N N 181 
ILE HD13   H  N N 182 
ILE HXT    H  N N 183 
LEU N      N  N N 184 
LEU CA     C  N S 185 
LEU C      C  N N 186 
LEU O      O  N N 187 
LEU CB     C  N N 188 
LEU CG     C  N N 189 
LEU CD1    C  N N 190 
LEU CD2    C  N N 191 
LEU OXT    O  N N 192 
LEU H      H  N N 193 
LEU H2     H  N N 194 
LEU HA     H  N N 195 
LEU HB2    H  N N 196 
LEU HB3    H  N N 197 
LEU HG     H  N N 198 
LEU HD11   H  N N 199 
LEU HD12   H  N N 200 
LEU HD13   H  N N 201 
LEU HD21   H  N N 202 
LEU HD22   H  N N 203 
LEU HD23   H  N N 204 
LEU HXT    H  N N 205 
LYS N      N  N N 206 
LYS CA     C  N S 207 
LYS C      C  N N 208 
LYS O      O  N N 209 
LYS CB     C  N N 210 
LYS CG     C  N N 211 
LYS CD     C  N N 212 
LYS CE     C  N N 213 
LYS NZ     N  N N 214 
LYS OXT    O  N N 215 
LYS H      H  N N 216 
LYS H2     H  N N 217 
LYS HA     H  N N 218 
LYS HB2    H  N N 219 
LYS HB3    H  N N 220 
LYS HG2    H  N N 221 
LYS HG3    H  N N 222 
LYS HD2    H  N N 223 
LYS HD3    H  N N 224 
LYS HE2    H  N N 225 
LYS HE3    H  N N 226 
LYS HZ1    H  N N 227 
LYS HZ2    H  N N 228 
LYS HZ3    H  N N 229 
LYS HXT    H  N N 230 
MET N      N  N N 231 
MET CA     C  N S 232 
MET C      C  N N 233 
MET O      O  N N 234 
MET CB     C  N N 235 
MET CG     C  N N 236 
MET SD     S  N N 237 
MET CE     C  N N 238 
MET OXT    O  N N 239 
MET H      H  N N 240 
MET H2     H  N N 241 
MET HA     H  N N 242 
MET HB2    H  N N 243 
MET HB3    H  N N 244 
MET HG2    H  N N 245 
MET HG3    H  N N 246 
MET HE1    H  N N 247 
MET HE2    H  N N 248 
MET HE3    H  N N 249 
MET HXT    H  N N 250 
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 
SO4 S      S  N N 305 
SO4 O1     O  N N 306 
SO4 O2     O  N N 307 
SO4 O3     O  N N 308 
SO4 O4     O  N N 309 
THR N      N  N N 310 
THR CA     C  N S 311 
THR C      C  N N 312 
THR O      O  N N 313 
THR CB     C  N R 314 
THR OG1    O  N N 315 
THR CG2    C  N N 316 
THR OXT    O  N N 317 
THR H      H  N N 318 
THR H2     H  N N 319 
THR HA     H  N N 320 
THR HB     H  N N 321 
THR HG1    H  N N 322 
THR HG21   H  N N 323 
THR HG22   H  N N 324 
THR HG23   H  N N 325 
THR HXT    H  N N 326 
TRP N      N  N N 327 
TRP CA     C  N S 328 
TRP C      C  N N 329 
TRP O      O  N N 330 
TRP CB     C  N N 331 
TRP CG     C  Y N 332 
TRP CD1    C  Y N 333 
TRP CD2    C  Y N 334 
TRP NE1    N  Y N 335 
TRP CE2    C  Y N 336 
TRP CE3    C  Y N 337 
TRP CZ2    C  Y N 338 
TRP CZ3    C  Y N 339 
TRP CH2    C  Y N 340 
TRP OXT    O  N N 341 
TRP H      H  N N 342 
TRP H2     H  N N 343 
TRP HA     H  N N 344 
TRP HB2    H  N N 345 
TRP HB3    H  N N 346 
TRP HD1    H  N N 347 
TRP HE1    H  N N 348 
TRP HE3    H  N N 349 
TRP HZ2    H  N N 350 
TRP HZ3    H  N N 351 
TRP HH2    H  N N 352 
TRP HXT    H  N N 353 
TYR N      N  N N 354 
TYR CA     C  N S 355 
TYR C      C  N N 356 
TYR O      O  N N 357 
TYR CB     C  N N 358 
TYR CG     C  Y N 359 
TYR CD1    C  Y N 360 
TYR CD2    C  Y N 361 
TYR CE1    C  Y N 362 
TYR CE2    C  Y N 363 
TYR CZ     C  Y N 364 
TYR OH     O  N N 365 
TYR OXT    O  N N 366 
TYR H      H  N N 367 
TYR H2     H  N N 368 
TYR HA     H  N N 369 
TYR HB2    H  N N 370 
TYR HB3    H  N N 371 
TYR HD1    H  N N 372 
TYR HD2    H  N N 373 
TYR HE1    H  N N 374 
TYR HE2    H  N N 375 
TYR HH     H  N N 376 
TYR HXT    H  N N 377 
UDP N1     N  N N 378 
UDP C2     C  N N 379 
UDP N3     N  N N 380 
UDP C4     C  N N 381 
UDP C5     C  N N 382 
UDP C6     C  N N 383 
UDP O2     O  N N 384 
UDP O4     O  N N 385 
UDP "C1'"  C  N R 386 
UDP "C2'"  C  N R 387 
UDP "O2'"  O  N N 388 
UDP "C3'"  C  N S 389 
UDP "C4'"  C  N R 390 
UDP "O4'"  O  N N 391 
UDP "O3'"  O  N N 392 
UDP "C5'"  C  N N 393 
UDP "O5'"  O  N N 394 
UDP PA     P  N N 395 
UDP O1A    O  N N 396 
UDP O2A    O  N N 397 
UDP O3A    O  N N 398 
UDP PB     P  N N 399 
UDP O1B    O  N N 400 
UDP O2B    O  N N 401 
UDP O3B    O  N N 402 
UDP HN3    H  N N 403 
UDP H5     H  N N 404 
UDP H6     H  N N 405 
UDP "H1'"  H  N N 406 
UDP "H2'"  H  N N 407 
UDP "HO2'" H  N N 408 
UDP "H3'"  H  N N 409 
UDP "H4'"  H  N N 410 
UDP "HO3'" H  N N 411 
UDP "H5'1" H  N N 412 
UDP "H5'2" H  N N 413 
UDP HOA2   H  N N 414 
UDP HOB2   H  N N 415 
UDP HOB3   H  N N 416 
VAL N      N  N N 417 
VAL CA     C  N S 418 
VAL C      C  N N 419 
VAL O      O  N N 420 
VAL CB     C  N N 421 
VAL CG1    C  N N 422 
VAL CG2    C  N N 423 
VAL OXT    O  N N 424 
VAL H      H  N N 425 
VAL H2     H  N N 426 
VAL HA     H  N N 427 
VAL HB     H  N N 428 
VAL HG11   H  N N 429 
VAL HG12   H  N N 430 
VAL HG13   H  N N 431 
VAL HG21   H  N N 432 
VAL HG22   H  N N 433 
VAL HG23   H  N N 434 
VAL HXT    H  N N 435 
# 
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 
SO4 S     O1     doub N N 290 
SO4 S     O2     doub N N 291 
SO4 S     O3     sing N N 292 
SO4 S     O4     sing N N 293 
THR N     CA     sing N N 294 
THR N     H      sing N N 295 
THR N     H2     sing N N 296 
THR CA    C      sing N N 297 
THR CA    CB     sing N N 298 
THR CA    HA     sing N N 299 
THR C     O      doub N N 300 
THR C     OXT    sing N N 301 
THR CB    OG1    sing N N 302 
THR CB    CG2    sing N N 303 
THR CB    HB     sing N N 304 
THR OG1   HG1    sing N N 305 
THR CG2   HG21   sing N N 306 
THR CG2   HG22   sing N N 307 
THR CG2   HG23   sing N N 308 
THR OXT   HXT    sing N N 309 
TRP N     CA     sing N N 310 
TRP N     H      sing N N 311 
TRP N     H2     sing N N 312 
TRP CA    C      sing N N 313 
TRP CA    CB     sing N N 314 
TRP CA    HA     sing N N 315 
TRP C     O      doub N N 316 
TRP C     OXT    sing N N 317 
TRP CB    CG     sing N N 318 
TRP CB    HB2    sing N N 319 
TRP CB    HB3    sing N N 320 
TRP CG    CD1    doub Y N 321 
TRP CG    CD2    sing Y N 322 
TRP CD1   NE1    sing Y N 323 
TRP CD1   HD1    sing N N 324 
TRP CD2   CE2    doub Y N 325 
TRP CD2   CE3    sing Y N 326 
TRP NE1   CE2    sing Y N 327 
TRP NE1   HE1    sing N N 328 
TRP CE2   CZ2    sing Y N 329 
TRP CE3   CZ3    doub Y N 330 
TRP CE3   HE3    sing N N 331 
TRP CZ2   CH2    doub Y N 332 
TRP CZ2   HZ2    sing N N 333 
TRP CZ3   CH2    sing Y N 334 
TRP CZ3   HZ3    sing N N 335 
TRP CH2   HH2    sing N N 336 
TRP OXT   HXT    sing N N 337 
TYR N     CA     sing N N 338 
TYR N     H      sing N N 339 
TYR N     H2     sing N N 340 
TYR CA    C      sing N N 341 
TYR CA    CB     sing N N 342 
TYR CA    HA     sing N N 343 
TYR C     O      doub N N 344 
TYR C     OXT    sing N N 345 
TYR CB    CG     sing N N 346 
TYR CB    HB2    sing N N 347 
TYR CB    HB3    sing N N 348 
TYR CG    CD1    doub Y N 349 
TYR CG    CD2    sing Y N 350 
TYR CD1   CE1    sing Y N 351 
TYR CD1   HD1    sing N N 352 
TYR CD2   CE2    doub Y N 353 
TYR CD2   HD2    sing N N 354 
TYR CE1   CZ     doub Y N 355 
TYR CE1   HE1    sing N N 356 
TYR CE2   CZ     sing Y N 357 
TYR CE2   HE2    sing N N 358 
TYR CZ    OH     sing N N 359 
TYR OH    HH     sing N N 360 
TYR OXT   HXT    sing N N 361 
UDP N1    C2     sing N N 362 
UDP N1    C6     sing N N 363 
UDP N1    "C1'"  sing N N 364 
UDP C2    N3     sing N N 365 
UDP C2    O2     doub N N 366 
UDP N3    C4     sing N N 367 
UDP N3    HN3    sing N N 368 
UDP C4    C5     sing N N 369 
UDP C4    O4     doub N N 370 
UDP C5    C6     doub N N 371 
UDP C5    H5     sing N N 372 
UDP C6    H6     sing N N 373 
UDP "C1'" "C2'"  sing N N 374 
UDP "C1'" "O4'"  sing N N 375 
UDP "C1'" "H1'"  sing N N 376 
UDP "C2'" "O2'"  sing N N 377 
UDP "C2'" "C3'"  sing N N 378 
UDP "C2'" "H2'"  sing N N 379 
UDP "O2'" "HO2'" sing N N 380 
UDP "C3'" "C4'"  sing N N 381 
UDP "C3'" "O3'"  sing N N 382 
UDP "C3'" "H3'"  sing N N 383 
UDP "C4'" "O4'"  sing N N 384 
UDP "C4'" "C5'"  sing N N 385 
UDP "C4'" "H4'"  sing N N 386 
UDP "O3'" "HO3'" sing N N 387 
UDP "C5'" "O5'"  sing N N 388 
UDP "C5'" "H5'1" sing N N 389 
UDP "C5'" "H5'2" sing N N 390 
UDP "O5'" PA     sing N N 391 
UDP PA    O1A    doub N N 392 
UDP PA    O2A    sing N N 393 
UDP PA    O3A    sing N N 394 
UDP O2A   HOA2   sing N N 395 
UDP O3A   PB     sing N N 396 
UDP PB    O1B    doub N N 397 
UDP PB    O2B    sing N N 398 
UDP PB    O3B    sing N N 399 
UDP O2B   HOB2   sing N N 400 
UDP O3B   HOB3   sing N N 401 
VAL N     CA     sing N N 402 
VAL N     H      sing N N 403 
VAL N     H2     sing N N 404 
VAL CA    C      sing N N 405 
VAL CA    CB     sing N N 406 
VAL CA    HA     sing N N 407 
VAL C     O      doub N N 408 
VAL C     OXT    sing N N 409 
VAL CB    CG1    sing N N 410 
VAL CB    CG2    sing N N 411 
VAL CB    HB     sing N N 412 
VAL CG1   HG11   sing N N 413 
VAL CG1   HG12   sing N N 414 
VAL CG1   HG13   sing N N 415 
VAL CG2   HG21   sing N N 416 
VAL CG2   HG22   sing N N 417 
VAL CG2   HG23   sing N N 418 
VAL OXT   HXT    sing N N 419 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9UCE 
_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]   0.010929 
_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]   0.010929 
_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]   0.005988 
_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  
CL 
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     . PRO A 1 41  ? -60.49000 15.14100  -34.64400 1.000 56.19355  ? 7   PRO A N     1 
ATOM   2    C  CA    . PRO A 1 41  ? -59.43600 14.94900  -33.64200 1.000 63.83181  ? 7   PRO A CA    1 
ATOM   3    C  C     . PRO A 1 41  ? -59.13900 13.47500  -33.41500 1.000 57.89787  ? 7   PRO A C     1 
ATOM   4    O  O     . PRO A 1 41  ? -60.06600 12.67600  -33.29900 1.000 59.98834  ? 7   PRO A O     1 
ATOM   5    C  CB    . PRO A 1 41  ? -60.02500 15.58500  -32.37400 1.000 65.05394  ? 7   PRO A CB    1 
ATOM   6    C  CG    . PRO A 1 41  ? -61.13600 16.46100  -32.85100 1.000 62.11335  ? 7   PRO A CG    1 
ATOM   7    C  CD    . PRO A 1 41  ? -61.68100 15.78800  -34.07000 1.000 67.80747  ? 7   PRO A CD    1 
ATOM   8    N  N     . LEU A 1 42  ? -57.86200 13.11700  -33.34800 1.000 54.07436  ? 8   LEU A N     1 
ATOM   9    C  CA    . LEU A 1 42  ? -57.47300 11.72300  -33.20600 1.000 59.29149  ? 8   LEU A CA    1 
ATOM   10   C  C     . LEU A 1 42  ? -57.32100 11.34500  -31.73600 1.000 48.20606  ? 8   LEU A C     1 
ATOM   11   O  O     . LEU A 1 42  ? -57.04000 12.18700  -30.87900 1.000 49.43337  ? 8   LEU A O     1 
ATOM   12   C  CB    . LEU A 1 42  ? -56.16900 11.45000  -33.95500 1.000 50.34792  ? 8   LEU A CB    1 
ATOM   13   C  CG    . LEU A 1 42  ? -56.24900 11.52100  -35.48100 1.000 60.41273  ? 8   LEU A CG    1 
ATOM   14   C  CD1   . LEU A 1 42  ? -54.92700 11.11100  -36.10700 1.000 49.75864  ? 8   LEU A CD1   1 
ATOM   15   C  CD2   . LEU A 1 42  ? -57.38800 10.65500  -36.01000 1.000 53.64173  ? 8   LEU A CD2   1 
ATOM   16   N  N     . LYS A 1 43  ? -57.52900 10.06100  -31.45400 1.000 53.59536  ? 9   LYS A N     1 
ATOM   17   C  CA    . LYS A 1 43  ? -57.27300 9.48000   -30.14000 1.000 50.07466  ? 9   LYS A CA    1 
ATOM   18   C  C     . LYS A 1 43  ? -55.88400 8.85500   -30.18400 1.000 43.99314  ? 9   LYS A C     1 
ATOM   19   O  O     . LYS A 1 43  ? -55.68600 7.81200   -30.81600 1.000 49.91482  ? 9   LYS A O     1 
ATOM   20   C  CB    . LYS A 1 43  ? -58.33400 8.44100   -29.78700 1.000 53.81542  ? 9   LYS A CB    1 
ATOM   21   C  CG    . LYS A 1 43  ? -58.51800 8.20600   -28.30200 1.000 55.65500  ? 9   LYS A CG    1 
ATOM   22   C  CD    . LYS A 1 43  ? -59.51500 9.18100   -27.71100 1.000 70.43160  ? 9   LYS A CD    1 
ATOM   23   C  CE    . LYS A 1 43  ? -59.52400 9.10700   -26.19000 1.000 84.33826  ? 9   LYS A CE    1 
ATOM   24   N  NZ    . LYS A 1 43  ? -59.46200 10.46700  -25.57700 1.000 70.04520  ? 9   LYS A NZ    1 
ATOM   25   N  N     . ILE A 1 44  ? -54.92100 9.50000   -29.53400 1.000 43.36042  ? 10  ILE A N     1 
ATOM   26   C  CA    . ILE A 1 44  ? -53.51600 9.11900   -29.63300 1.000 41.80147  ? 10  ILE A CA    1 
ATOM   27   C  C     . ILE A 1 44  ? -53.01500 8.76200   -28.23900 1.000 41.39375  ? 10  ILE A C     1 
ATOM   28   O  O     . ILE A 1 44  ? -53.02300 9.60600   -27.33400 1.000 41.47388  ? 10  ILE A O     1 
ATOM   29   C  CB    . ILE A 1 44  ? -52.66800 10.23700  -30.26200 1.000 41.58909  ? 10  ILE A CB    1 
ATOM   30   C  CG1   . ILE A 1 44  ? -53.22300 10.60600  -31.64200 1.000 41.77015  ? 10  ILE A CG1   1 
ATOM   31   C  CG2   . ILE A 1 44  ? -51.20700 9.80300   -30.38100 1.000 39.66262  ? 10  ILE A CG2   1 
ATOM   32   C  CD1   . ILE A 1 44  ? -52.50500 11.76700  -32.31000 1.000 38.53493  ? 10  ILE A CD1   1 
ATOM   33   N  N     . TYR A 1 45  ? -52.59600 7.50900   -28.06400 1.000 38.17525  ? 11  TYR A N     1 
ATOM   34   C  CA    . TYR A 1 45  ? -51.98500 7.04200   -26.82500 1.000 44.56791  ? 11  TYR A CA    1 
ATOM   35   C  C     . TYR A 1 45  ? -50.47000 7.04300   -26.97100 1.000 43.35636  ? 11  TYR A C     1 
ATOM   36   O  O     . TYR A 1 45  ? -49.92900 6.57000   -27.97700 1.000 40.39354  ? 11  TYR A O     1 
ATOM   37   C  CB    . TYR A 1 45  ? -52.44700 5.63100   -26.45100 1.000 40.86223  ? 11  TYR A CB    1 
ATOM   38   C  CG    . TYR A 1 45  ? -53.89700 5.49800   -26.04900 1.000 43.45193  ? 11  TYR A CG    1 
ATOM   39   C  CD1   . TYR A 1 45  ? -54.73300 6.60600   -25.97100 1.000 47.82319  ? 11  TYR A CD1   1 
ATOM   40   C  CD2   . TYR A 1 45  ? -54.43100 4.25200   -25.75300 1.000 46.07275  ? 11  TYR A CD2   1 
ATOM   41   C  CE1   . TYR A 1 45  ? -56.06100 6.47200   -25.61000 1.000 50.26546  ? 11  TYR A CE1   1 
ATOM   42   C  CE2   . TYR A 1 45  ? -55.75300 4.10700   -25.39900 1.000 51.78287  ? 11  TYR A CE2   1 
ATOM   43   C  CZ    . TYR A 1 45  ? -56.56500 5.21600   -25.32500 1.000 53.30366  ? 11  TYR A CZ    1 
ATOM   44   O  OH    . TYR A 1 45  ? -57.88500 5.06300   -24.96600 1.000 62.77711  ? 11  TYR A OH    1 
ATOM   45   N  N     . MET A 1 46  ? -49.79400 7.54900   -25.94600 1.000 38.28906  ? 12  MET A N     1 
ATOM   46   C  CA    . MET A 1 46  ? -48.35100 7.74400   -25.95200 1.000 38.19538  ? 12  MET A CA    1 
ATOM   47   C  C     . MET A 1 46  ? -47.75200 7.02600   -24.75000 1.000 42.39313  ? 12  MET A C     1 
ATOM   48   O  O     . MET A 1 46  ? -48.15700 7.27600   -23.60900 1.000 35.50488  ? 12  MET A O     1 
ATOM   49   C  CB    . MET A 1 46  ? -48.02900 9.24000   -25.93800 1.000 37.38625  ? 12  MET A CB    1 
ATOM   50   C  CG    . MET A 1 46  ? -48.35300 9.92200   -27.26500 1.000 43.52065  ? 12  MET A CG    1 
ATOM   51   S  SD    . MET A 1 46  ? -47.44700 11.45500  -27.50200 1.000 40.51091  ? 12  MET A SD    1 
ATOM   52   C  CE    . MET A 1 46  ? -48.43300 12.22100  -28.79400 1.000 37.06002  ? 12  MET A CE    1 
ATOM   53   N  N     . LEU A 1 47  ? -46.80300 6.12800   -25.01000 1.000 34.40667  ? 13  LEU A N     1 
ATOM   54   C  CA    . LEU A 1 47  ? -46.24700 5.24000   -23.98600 1.000 38.82425  ? 13  LEU A CA    1 
ATOM   55   C  C     . LEU A 1 47  ? -44.76600 5.52300   -23.77300 1.000 35.61973  ? 13  LEU A C     1 
ATOM   56   O  O     . LEU A 1 47  ? -43.92000 5.01200   -24.52700 1.000 33.60622  ? 13  LEU A O     1 
ATOM   57   C  CB    . LEU A 1 47  ? -46.45400 3.77800   -24.38100 1.000 36.49403  ? 13  LEU A CB    1 
ATOM   58   C  CG    . LEU A 1 47  ? -45.84700 2.72000   -23.45700 1.000 40.22532  ? 13  LEU A CG    1 
ATOM   59   C  CD1   . LEU A 1 47  ? -46.31800 2.90300   -22.00500 1.000 37.01131  ? 13  LEU A CD1   1 
ATOM   60   C  CD2   . LEU A 1 47  ? -46.16800 1.32800   -23.97700 1.000 35.44297  ? 13  LEU A CD2   1 
ATOM   61   N  N     . PRO A 1 48  ? -44.40300 6.30700   -22.76200 1.000 37.90432  ? 14  PRO A N     1 
ATOM   62   C  CA    . PRO A 1 48  ? -42.98900 6.57300   -22.48200 1.000 32.58774  ? 14  PRO A CA    1 
ATOM   63   C  C     . PRO A 1 48  ? -42.33000 5.48300   -21.64600 1.000 40.51360  ? 14  PRO A C     1 
ATOM   64   O  O     . PRO A 1 48  ? -42.97400 4.76500   -20.87700 1.000 36.68550  ? 14  PRO A O     1 
ATOM   65   C  CB    . PRO A 1 48  ? -43.03900 7.89400   -21.70100 1.000 29.11549  ? 14  PRO A CB    1 
ATOM   66   C  CG    . PRO A 1 48  ? -44.36200 7.84300   -21.00100 1.000 37.97473  ? 14  PRO A CG    1 
ATOM   67   C  CD    . PRO A 1 48  ? -45.30400 7.08700   -21.89400 1.000 36.23711  ? 14  PRO A CD    1 
ATOM   68   N  N     . PHE A 1 49  ? -41.01400 5.37500   -21.81300 1.000 36.34756  ? 15  PHE A N     1 
ATOM   69   C  CA    . PHE A 1 49  ? -40.23400 4.49400   -20.96000 1.000 36.76410  ? 15  PHE A CA    1 
ATOM   70   C  C     . PHE A 1 49  ? -39.90500 5.19000   -19.63700 1.000 35.20074  ? 15  PHE A C     1 
ATOM   71   O  O     . PHE A 1 49  ? -39.87500 6.42100   -19.53900 1.000 31.10828  ? 15  PHE A O     1 
ATOM   72   C  CB    . PHE A 1 49  ? -38.95600 4.03700   -21.67200 1.000 30.84646  ? 15  PHE A CB    1 
ATOM   73   C  CG    . PHE A 1 49  ? -38.04600 3.20300   -20.80600 1.000 36.04819  ? 15  PHE A CG    1 
ATOM   74   C  CD1   . PHE A 1 49  ? -38.45800 1.96500   -20.33700 1.000 36.28297  ? 15  PHE A CD1   1 
ATOM   75   C  CD2   . PHE A 1 49  ? -36.78700 3.66300   -20.45000 1.000 36.82814  ? 15  PHE A CD2   1 
ATOM   76   C  CE1   . PHE A 1 49  ? -37.63000 1.19800   -19.53600 1.000 39.10457  ? 15  PHE A CE1   1 
ATOM   77   C  CE2   . PHE A 1 49  ? -35.95100 2.89700   -19.65000 1.000 36.32032  ? 15  PHE A CE2   1 
ATOM   78   C  CZ    . PHE A 1 49  ? -36.37400 1.66400   -19.19500 1.000 34.75331  ? 15  PHE A CZ    1 
ATOM   79   N  N     . PHE A 1 50  ? -39.65900 4.37200   -18.60900 1.000 32.75134  ? 16  PHE A N     1 
ATOM   80   C  CA    . PHE A 1 50  ? -39.46500 4.84600   -17.23700 1.000 39.60865  ? 16  PHE A CA    1 
ATOM   81   C  C     . PHE A 1 50  ? -38.03100 5.32600   -17.00100 1.000 41.06334  ? 16  PHE A C     1 
ATOM   82   O  O     . PHE A 1 50  ? -37.29400 4.80800   -16.16300 1.000 43.32899  ? 16  PHE A O     1 
ATOM   83   C  CB    . PHE A 1 50  ? -39.82300 3.74900   -16.24200 1.000 38.20178  ? 16  PHE A CB    1 
ATOM   84   C  CG    . PHE A 1 50  ? -40.85700 2.78800   -16.73900 1.000 42.18086  ? 16  PHE A CG    1 
ATOM   85   C  CD1   . PHE A 1 50  ? -42.16600 3.20300   -16.93600 1.000 39.16049  ? 16  PHE A CD1   1 
ATOM   86   C  CD2   . PHE A 1 50  ? -40.52900 1.46700   -16.99000 1.000 34.89840  ? 16  PHE A CD2   1 
ATOM   87   C  CE1   . PHE A 1 50  ? -43.12900 2.32100   -17.38700 1.000 38.70680  ? 16  PHE A CE1   1 
ATOM   88   C  CE2   . PHE A 1 50  ? -41.48700 0.57900   -17.44500 1.000 37.38462  ? 16  PHE A CE2   1 
ATOM   89   C  CZ    . PHE A 1 50  ? -42.79000 1.00700   -17.64100 1.000 35.21634  ? 16  PHE A CZ    1 
ATOM   90   N  N     . ALA A 1 51  ? -37.64700 6.35300   -17.74900 1.000 36.52000  ? 17  ALA A N     1 
ATOM   91   C  CA    . ALA A 1 51  ? -36.34200 6.97700   -17.59000 1.000 36.50531  ? 17  ALA A CA    1 
ATOM   92   C  C     . ALA A 1 51  ? -36.47700 8.42500   -18.02600 1.000 34.40896  ? 17  ALA A C     1 
ATOM   93   O  O     . ALA A 1 51  ? -37.19600 8.71900   -18.98400 1.000 32.97342  ? 17  ALA A O     1 
ATOM   94   C  CB    . ALA A 1 51  ? -35.26100 6.25700   -18.40400 1.000 31.60055  ? 17  ALA A CB    1 
ATOM   95   N  N     . GLN A 1 52  ? -35.79200 9.32300   -17.31400 1.000 31.58531  ? 18  GLN A N     1 
ATOM   96   C  CA    . GLN A 1 52  ? -36.02400 10.75400  -17.50200 1.000 41.97947  ? 18  GLN A CA    1 
ATOM   97   C  C     . GLN A 1 52  ? -35.71200 11.19800  -18.92500 1.000 36.84158  ? 18  GLN A C     1 
ATOM   98   O  O     . GLN A 1 52  ? -36.43000 12.03000  -19.49200 1.000 39.77944  ? 18  GLN A O     1 
ATOM   99   C  CB    . GLN A 1 52  ? -35.19700 11.55400  -16.49600 1.000 42.03519  ? 18  GLN A CB    1 
ATOM   100  C  CG    . GLN A 1 52  ? -35.52700 11.24500  -15.03900 1.000 64.29196  ? 18  GLN A CG    1 
ATOM   101  C  CD    . GLN A 1 52  ? -36.92000 11.70000  -14.63800 1.000 77.61240  ? 18  GLN A CD    1 
ATOM   102  O  OE1   . GLN A 1 52  ? -37.92900 11.18800  -15.13100 1.000 67.12990  ? 18  GLN A OE1   1 
ATOM   103  N  NE2   . GLN A 1 52  ? -36.98100 12.66700  -13.72700 1.000 79.36234  ? 18  GLN A NE2   1 
ATOM   104  N  N     . GLY A 1 53  ? -34.64200 10.66200  -19.51800 1.000 26.50276  ? 19  GLY A N     1 
ATOM   105  C  CA    . GLY A 1 53  ? -34.30300 11.00400  -20.88700 1.000 32.13328  ? 19  GLY A CA    1 
ATOM   106  C  C     . GLY A 1 53  ? -35.27900 10.46700  -21.91100 1.000 38.35072  ? 19  GLY A C     1 
ATOM   107  O  O     . GLY A 1 53  ? -35.25100 10.89900  -23.06600 1.000 34.72025  ? 19  GLY A O     1 
ATOM   108  N  N     . HIS A 1 54  ? -36.13000 9.52200   -21.51900 1.000 34.67465  ? 20  HIS A N     1 
ATOM   109  C  CA    . HIS A 1 54  ? -37.19100 9.01700   -22.37800 1.000 34.83901  ? 20  HIS A CA    1 
ATOM   110  C  C     . HIS A 1 54  ? -38.53900 9.64000   -22.06300 1.000 36.41453  ? 20  HIS A C     1 
ATOM   111  O  O     . HIS A 1 54  ? -39.31400 9.92900   -22.98300 1.000 35.57624  ? 20  HIS A O     1 
ATOM   112  C  CB    . HIS A 1 54  ? -37.30300 7.49500   -22.25100 1.000 30.36319  ? 20  HIS A CB    1 
ATOM   113  C  CG    . HIS A 1 54  ? -36.11000 6.75700   -22.77000 1.000 36.29486  ? 20  HIS A CG    1 
ATOM   114  N  ND1   . HIS A 1 54  ? -36.18600 5.86900   -23.82200 1.000 32.79494  ? 20  HIS A ND1   1 
ATOM   115  C  CD2   . HIS A 1 54  ? -34.81400 6.76700   -22.37900 1.000 29.27032  ? 20  HIS A CD2   1 
ATOM   116  C  CE1   . HIS A 1 54  ? -34.98700 5.36700   -24.05900 1.000 34.19343  ? 20  HIS A CE1   1 
ATOM   117  N  NE2   . HIS A 1 54  ? -34.13600 5.89700   -23.19900 1.000 30.11868  ? 20  HIS A NE2   1 
ATOM   118  N  N     . LEU A 1 55  ? -38.80300 9.88400   -20.77800 1.000 29.10731  ? 21  LEU A N     1 
ATOM   119  C  CA    . LEU A 1 55  ? -40.12900 10.28900  -20.32600 1.000 37.81434  ? 21  LEU A CA    1 
ATOM   120  C  C     . LEU A 1 55  ? -40.44300 11.72600  -20.72100 1.000 32.32305  ? 21  LEU A C     1 
ATOM   121  O  O     . LEU A 1 55  ? -41.49300 12.00300  -21.31000 1.000 32.21548  ? 21  LEU A O     1 
ATOM   122  C  CB    . LEU A 1 55  ? -40.22700 10.11700  -18.80600 1.000 30.24252  ? 21  LEU A CB    1 
ATOM   123  C  CG    . LEU A 1 55  ? -41.47500 10.66800  -18.11200 1.000 39.61085  ? 21  LEU A CG    1 
ATOM   124  C  CD1   . LEU A 1 55  ? -42.70700 9.93300   -18.58500 1.000 35.49116  ? 21  LEU A CD1   1 
ATOM   125  C  CD2   . LEU A 1 55  ? -41.34900 10.57200  -16.59200 1.000 41.02133  ? 21  LEU A CD2   1 
ATOM   126  N  N     . ILE A 1 56  ? -39.55500 12.65600  -20.39100 1.000 32.27789  ? 22  ILE A N     1 
ATOM   127  C  CA    . ILE A 1 56  ? -39.83600 14.07600  -20.58000 1.000 33.80212  ? 22  ILE A CA    1 
ATOM   128  C  C     . ILE A 1 56  ? -39.88800 14.42900  -22.06500 1.000 35.06375  ? 22  ILE A C     1 
ATOM   129  O  O     . ILE A 1 56  ? -40.77000 15.20400  -22.46500 1.000 35.00055  ? 22  ILE A O     1 
ATOM   130  C  CB    . ILE A 1 56  ? -38.81900 14.94300  -19.82300 1.000 31.65266  ? 22  ILE A CB    1 
ATOM   131  C  CG1   . ILE A 1 56  ? -38.85600 14.59700  -18.33100 1.000 35.28727  ? 22  ILE A CG1   1 
ATOM   132  C  CG2   . ILE A 1 56  ? -39.10400 16.42500  -20.04400 1.000 30.40349  ? 22  ILE A CG2   1 
ATOM   133  C  CD1   . ILE A 1 56  ? -40.19300 14.88800  -17.67000 1.000 39.82855  ? 22  ILE A CD1   1 
ATOM   134  N  N     . PRO A 1 57  ? -38.99500 13.91300  -22.92500 1.000 36.57681  ? 23  PRO A N     1 
ATOM   135  C  CA    . PRO A 1 57  ? -39.18000 14.17500  -24.36500 1.000 32.51027  ? 23  PRO A CA    1 
ATOM   136  C  C     . PRO A 1 57  ? -40.51200 13.68300  -24.90500 1.000 33.42565  ? 23  PRO A C     1 
ATOM   137  O  O     . PRO A 1 57  ? -41.12100 14.37000  -25.73500 1.000 33.10491  ? 23  PRO A O     1 
ATOM   138  C  CB    . PRO A 1 57  ? -37.99000 13.45100  -25.00800 1.000 29.36670  ? 23  PRO A CB    1 
ATOM   139  C  CG    . PRO A 1 57  ? -36.93300 13.50300  -23.95100 1.000 36.04238  ? 23  PRO A CG    1 
ATOM   140  C  CD    . PRO A 1 57  ? -37.67500 13.30200  -22.65900 1.000 32.44411  ? 23  PRO A CD    1 
ATOM   141  N  N     . LEU A 1 58  ? -40.99700 12.52100  -24.45700 1.000 30.51650  ? 24  LEU A N     1 
ATOM   142  C  CA    . LEU A 1 58  ? -42.28300 12.04200  -24.95500 1.000 30.09989  ? 24  LEU A CA    1 
ATOM   143  C  C     . LEU A 1 58  ? -43.43700 12.84400  -24.37000 1.000 31.40970  ? 24  LEU A C     1 
ATOM   144  O  O     . LEU A 1 58  ? -44.43800 13.08500  -25.05400 1.000 33.82570  ? 24  LEU A O     1 
ATOM   145  C  CB    . LEU A 1 58  ? -42.46300 10.55400  -24.65800 1.000 27.05077  ? 24  LEU A CB    1 
ATOM   146  C  CG    . LEU A 1 58  ? -43.68900 9.95700   -25.36200 1.000 33.08194  ? 24  LEU A CG    1 
ATOM   147  C  CD1   . LEU A 1 58  ? -43.72600 10.37600  -26.81500 1.000 39.87815  ? 24  LEU A CD1   1 
ATOM   148  C  CD2   . LEU A 1 58  ? -43.67800 8.45900   -25.28900 1.000 39.50956  ? 24  LEU A CD2   1 
ATOM   149  N  N     . VAL A 1 59  ? -43.32700 13.25600  -23.10500 1.000 35.24746  ? 25  VAL A N     1 
ATOM   150  C  CA    . VAL A 1 59  ? -44.35900 14.11300  -22.52900 1.000 42.13756  ? 25  VAL A CA    1 
ATOM   151  C  C     . VAL A 1 59  ? -44.45700 15.41300  -23.31500 1.000 34.06180  ? 25  VAL A C     1 
ATOM   152  O  O     . VAL A 1 59  ? -45.55500 15.88000  -23.64000 1.000 31.25390  ? 25  VAL A O     1 
ATOM   153  C  CB    . VAL A 1 59  ? -44.08400 14.37200  -21.03600 1.000 31.48226  ? 25  VAL A CB    1 
ATOM   154  C  CG1   . VAL A 1 59  ? -44.94700 15.52000  -20.53000 1.000 34.73137  ? 25  VAL A CG1   1 
ATOM   155  C  CG2   . VAL A 1 59  ? -44.35300 13.11700  -20.22300 1.000 36.36977  ? 25  VAL A CG2   1 
ATOM   156  N  N     . ASN A 1 60  ? -43.31200 16.00700  -23.65300 1.000 31.71430  ? 26  ASN A N     1 
ATOM   157  C  CA    . ASN A 1 60  ? -43.33200 17.24800  -24.41500 1.000 34.32450  ? 26  ASN A CA    1 
ATOM   158  C  C     . ASN A 1 60  ? -43.94000 17.03600  -25.79500 1.000 40.10382  ? 26  ASN A C     1 
ATOM   159  O  O     . ASN A 1 60  ? -44.68900 17.88800  -26.28600 1.000 39.38778  ? 26  ASN A O     1 
ATOM   160  C  CB    . ASN A 1 60  ? -41.92200 17.81800  -24.51000 1.000 35.16416  ? 26  ASN A CB    1 
ATOM   161  C  CG    . ASN A 1 60  ? -41.48000 18.44300  -23.21100 1.000 39.71360  ? 26  ASN A CG    1 
ATOM   162  O  OD1   . ASN A 1 60  ? -42.31000 18.90300  -22.42800 1.000 41.45777  ? 26  ASN A OD1   1 
ATOM   163  N  ND2   . ASN A 1 60  ? -40.17800 18.45300  -22.96300 1.000 36.51577  ? 26  ASN A ND2   1 
ATOM   164  N  N     . LEU A 1 61  ? -43.65000 15.89800  -26.43100 1.000 30.75360  ? 27  LEU A N     1 
ATOM   165  C  CA    . LEU A 1 61  ? -44.34100 15.57000  -27.67200 1.000 36.61629  ? 27  LEU A CA    1 
ATOM   166  C  C     . LEU A 1 61  ? -45.84700 15.49000  -27.45200 1.000 36.36891  ? 27  LEU A C     1 
ATOM   167  O  O     . LEU A 1 61  ? -46.63200 15.90700  -28.31100 1.000 33.28891  ? 27  LEU A O     1 
ATOM   168  C  CB    . LEU A 1 61  ? -43.81800 14.25300  -28.24000 1.000 32.24262  ? 27  LEU A CB    1 
ATOM   169  C  CG    . LEU A 1 61  ? -44.53800 13.82900  -29.52000 1.000 37.03681  ? 27  LEU A CG    1 
ATOM   170  C  CD1   . LEU A 1 61  ? -44.26400 14.85000  -30.61700 1.000 29.89337  ? 27  LEU A CD1   1 
ATOM   171  C  CD2   . LEU A 1 61  ? -44.11800 12.43500  -29.96000 1.000 37.62830  ? 27  LEU A CD2   1 
ATOM   172  N  N     . ALA A 1 62  ? -46.26900 14.95800  -26.30200 1.000 39.46011  ? 28  ALA A N     1 
ATOM   173  C  CA    . ALA A 1 62  ? -47.69600 14.86600  -26.00800 1.000 39.11449  ? 28  ALA A CA    1 
ATOM   174  C  C     . ALA A 1 62  ? -48.32800 16.24900  -25.91800 1.000 38.86003  ? 28  ALA A C     1 
ATOM   175  O  O     . ALA A 1 62  ? -49.44200 16.46400  -26.41000 1.000 37.56864  ? 28  ALA A O     1 
ATOM   176  C  CB    . ALA A 1 62  ? -47.91600 14.09000  -24.71100 1.000 34.63422  ? 28  ALA A CB    1 
ATOM   177  N  N     . ARG A 1 63  ? -47.62800 17.19900  -25.29400 1.000 36.56420  ? 29  ARG A N     1 
ATOM   178  C  CA    . ARG A 1 63  ? -48.13100 18.56500  -25.21100 1.000 38.74160  ? 29  ARG A CA    1 
ATOM   179  C  C     . ARG A 1 63  ? -48.21800 19.21200  -26.58900 1.000 44.87130  ? 29  ARG A C     1 
ATOM   180  O  O     . ARG A 1 63  ? -49.15100 19.97600  -26.86400 1.000 44.57789  ? 29  ARG A O     1 
ATOM   181  C  CB    . ARG A 1 63  ? -47.24100 19.39000  -24.28300 1.000 37.02567  ? 29  ARG A CB    1 
ATOM   182  C  CG    . ARG A 1 63  ? -47.15500 18.84300  -22.86200 1.000 38.59733  ? 29  ARG A CG    1 
ATOM   183  C  CD    . ARG A 1 63  ? -45.98900 19.46400  -22.11600 1.000 34.80947  ? 29  ARG A CD    1 
ATOM   184  N  NE    . ARG A 1 63  ? -46.11800 20.91200  -22.01500 1.000 43.25828  ? 29  ARG A NE    1 
ATOM   185  C  CZ    . ARG A 1 63  ? -45.15900 21.72200  -21.58700 1.000 41.30095  ? 29  ARG A CZ    1 
ATOM   186  N  NH1   . ARG A 1 63  ? -43.97000 21.26200  -21.23800 1.000 45.83090  ? 29  ARG A NH1   1 
ATOM   187  N  NH2   . ARG A 1 63  ? -45.40000 23.02700  -21.50700 1.000 47.92011  ? 29  ARG A NH2   1 
ATOM   188  N  N     . LEU A 1 64  ? -47.25800 18.91500  -27.47100 1.000 36.03410  ? 30  LEU A N     1 
ATOM   189  C  CA    . LEU A 1 64  ? -47.27700 19.49900  -28.80900 1.000 40.12862  ? 30  LEU A CA    1 
ATOM   190  C  C     . LEU A 1 64  ? -48.43600 18.95700  -29.63500 1.000 38.87076  ? 30  LEU A C     1 
ATOM   191  O  O     . LEU A 1 64  ? -49.13200 19.72100  -30.31300 1.000 44.31069  ? 30  LEU A O     1 
ATOM   192  C  CB    . LEU A 1 64  ? -45.94800 19.23500  -29.51900 1.000 37.73546  ? 30  LEU A CB    1 
ATOM   193  C  CG    . LEU A 1 64  ? -44.70300 19.80100  -28.83500 1.000 36.61435  ? 30  LEU A CG    1 
ATOM   194  C  CD1   . LEU A 1 64  ? -43.43500 19.16400  -29.39400 1.000 28.57925  ? 30  LEU A CD1   1 
ATOM   195  C  CD2   . LEU A 1 64  ? -44.66300 21.31500  -28.98000 1.000 33.71912  ? 30  LEU A CD2   1 
ATOM   196  N  N     . VAL A 1 65  ? -48.66200 17.64400  -29.58600 1.000 36.66589  ? 31  VAL A N     1 
ATOM   197  C  CA    . VAL A 1 65  ? -49.73500 17.04000  -30.36700 1.000 46.17910  ? 31  VAL A CA    1 
ATOM   198  C  C     . VAL A 1 65  ? -51.09900 17.45000  -29.81900 1.000 43.63878  ? 31  VAL A C     1 
ATOM   199  O  O     . VAL A 1 65  ? -52.04500 17.67700  -30.58100 1.000 46.01326  ? 31  VAL A O     1 
ATOM   200  C  CB    . VAL A 1 65  ? -49.55400 15.51200  -30.40300 1.000 39.71896  ? 31  VAL A CB    1 
ATOM   201  C  CG1   . VAL A 1 65  ? -50.71300 14.84500  -31.12800 1.000 39.14387  ? 31  VAL A CG1   1 
ATOM   202  C  CG2   . VAL A 1 65  ? -48.23500 15.17000  -31.08000 1.000 35.22776  ? 31  VAL A CG2   1 
ATOM   203  N  N     . ALA A 1 66  ? -51.22000 17.57200  -28.49500 1.000 43.17939  ? 32  ALA A N     1 
ATOM   204  C  CA    . ALA A 1 66  ? -52.46300 18.07600  -27.91700 1.000 47.89226  ? 32  ALA A CA    1 
ATOM   205  C  C     . ALA A 1 66  ? -52.72200 19.51500  -28.34600 1.000 51.52986  ? 32  ALA A C     1 
ATOM   206  O  O     . ALA A 1 66  ? -53.87400 19.90600  -28.57000 1.000 47.35335  ? 32  ALA A O     1 
ATOM   207  C  CB    . ALA A 1 66  ? -52.42400 17.96800  -26.39200 1.000 47.35510  ? 32  ALA A CB    1 
ATOM   208  N  N     . SER A 1 67  ? -51.66100 20.31700  -28.47600 1.000 46.30871  ? 33  SER A N     1 
ATOM   209  C  CA    . SER A 1 67  ? -51.80100 21.69300  -28.93700 1.000 52.38697  ? 33  SER A CA    1 
ATOM   210  C  C     . SER A 1 67  ? -52.25500 21.78900  -30.38800 1.000 55.70660  ? 33  SER A C     1 
ATOM   211  O  O     . SER A 1 67  ? -52.62500 22.88100  -30.83100 1.000 55.49829  ? 33  SER A O     1 
ATOM   212  C  CB    . SER A 1 67  ? -50.48300 22.44800  -28.76200 1.000 52.04346  ? 33  SER A CB    1 
ATOM   213  O  OG    . SER A 1 67  ? -50.28800 22.81700  -27.40700 1.000 56.75570  ? 33  SER A OG    1 
ATOM   214  N  N     . LYS A 1 68  ? -52.22700 20.68800  -31.13700 1.000 45.99738  ? 34  LYS A N     1 
ATOM   215  C  CA    . LYS A 1 68  ? -52.80400 20.63200  -32.47300 1.000 52.12278  ? 34  LYS A CA    1 
ATOM   216  C  C     . LYS A 1 68  ? -54.18300 19.97700  -32.46900 1.000 56.49361  ? 34  LYS A C     1 
ATOM   217  O  O     . LYS A 1 68  ? -54.55000 19.29200  -33.43000 1.000 53.26487  ? 34  LYS A O     1 
ATOM   218  C  CB    . LYS A 1 68  ? -51.85600 19.90500  -33.42700 1.000 48.32853  ? 34  LYS A CB    1 
ATOM   219  C  CG    . LYS A 1 68  ? -50.42300 20.42300  -33.35400 1.000 50.78253  ? 34  LYS A CG    1 
ATOM   220  C  CD    . LYS A 1 68  ? -49.56300 19.89100  -34.49000 1.000 50.80398  ? 34  LYS A CD    1 
ATOM   221  C  CE    . LYS A 1 68  ? -49.53900 20.85500  -35.66200 1.000 59.19485  ? 34  LYS A CE    1 
ATOM   222  N  NZ    . LYS A 1 68  ? -48.88300 22.14300  -35.30300 1.000 60.37673  ? 34  LYS A NZ    1 
ATOM   223  N  N     . ASN A 1 69  ? -54.93700 20.15700  -31.37800 1.000 54.95291  ? 35  ASN A N     1 
ATOM   224  C  CA    . ASN A 1 69  ? -56.34400 19.75700  -31.28700 1.000 61.34013  ? 35  ASN A CA    1 
ATOM   225  C  C     . ASN A 1 69  ? -56.51500 18.24700  -31.45100 1.000 58.52502  ? 35  ASN A C     1 
ATOM   226  O  O     . ASN A 1 69  ? -57.40300 17.77500  -32.16300 1.000 68.92559  ? 35  ASN A O     1 
ATOM   227  C  CB    . ASN A 1 69  ? -57.20000 20.51500  -32.30900 1.000 64.14486  ? 35  ASN A CB    1 
ATOM   228  C  CG    . ASN A 1 69  ? -56.82300 21.98300  -32.42000 1.000 78.41014  ? 35  ASN A CG    1 
ATOM   229  O  OD1   . ASN A 1 69  ? -56.43600 22.61500  -31.43600 1.000 79.22295  ? 35  ASN A OD1   1 
ATOM   230  N  ND2   . ASN A 1 69  ? -56.93100 22.53000  -33.62700 1.000 84.73238  ? 35  ASN A ND2   1 
ATOM   231  N  N     . GLN A 1 70  ? -55.65100 17.48400  -30.79000 1.000 51.88276  ? 36  GLN A N     1 
ATOM   232  C  CA    . GLN A 1 70  ? -55.76300 16.03300  -30.77900 1.000 52.86801  ? 36  GLN A CA    1 
ATOM   233  C  C     . GLN A 1 70  ? -55.97000 15.55200  -29.34900 1.000 42.88854  ? 36  GLN A C     1 
ATOM   234  O  O     . GLN A 1 70  ? -55.62000 16.23700  -28.38500 1.000 48.38759  ? 36  GLN A O     1 
ATOM   235  C  CB    . GLN A 1 70  ? -54.52400 15.36600  -31.39300 1.000 43.58113  ? 36  GLN A CB    1 
ATOM   236  C  CG    . GLN A 1 70  ? -54.11400 15.94600  -32.73600 1.000 47.12019  ? 36  GLN A CG    1 
ATOM   237  C  CD    . GLN A 1 70  ? -55.19300 15.80400  -33.79400 1.000 52.50929  ? 36  GLN A CD    1 
ATOM   238  O  OE1   . GLN A 1 70  ? -55.79300 14.74100  -33.95000 1.000 51.13867  ? 36  GLN A OE1   1 
ATOM   239  N  NE2   . GLN A 1 70  ? -55.45700 16.88700  -34.51500 1.000 51.26632  ? 36  GLN A NE2   1 
ATOM   240  N  N     . HIS A 1 71  ? -56.55800 14.36600  -29.22100 1.000 44.39621  ? 37  HIS A N     1 
ATOM   241  C  CA    . HIS A 1 71  ? -56.87500 13.77800  -27.92000 1.000 50.82357  ? 37  HIS A CA    1 
ATOM   242  C  C     . HIS A 1 71  ? -55.74600 12.82200  -27.55000 1.000 40.85666  ? 37  HIS A C     1 
ATOM   243  O  O     . HIS A 1 71  ? -55.65900 11.70800  -28.07700 1.000 46.47590  ? 37  HIS A O     1 
ATOM   244  C  CB    . HIS A 1 71  ? -58.22800 13.07600  -27.96200 1.000 52.79530  ? 37  HIS A CB    1 
ATOM   245  C  CG    . HIS A 1 71  ? -59.38800 14.01300  -28.09300 1.000 61.87876  ? 37  HIS A CG    1 
ATOM   246  N  ND1   . HIS A 1 71  ? -60.63700 13.72600  -27.58800 1.000 66.39915  ? 37  HIS A ND1   1 
ATOM   247  C  CD2   . HIS A 1 71  ? -59.48700 15.23600  -28.66800 1.000 55.90915  ? 37  HIS A CD2   1 
ATOM   248  C  CE1   . HIS A 1 71  ? -61.45600 14.73000  -27.84600 1.000 60.70564  ? 37  HIS A CE1   1 
ATOM   249  N  NE2   . HIS A 1 71  ? -60.78300 15.65800  -28.50100 1.000 64.82465  ? 37  HIS A NE2   1 
ATOM   250  N  N     . VAL A 1 72  ? -54.87800 13.26700  -26.64600 1.000 44.16878  ? 38  VAL A N     1 
ATOM   251  C  CA    . VAL A 1 72  ? -53.65600 12.55200  -26.29100 1.000 44.07917  ? 38  VAL A CA    1 
ATOM   252  C  C     . VAL A 1 72  ? -53.80100 11.98800  -24.88400 1.000 43.07557  ? 38  VAL A C     1 
ATOM   253  O  O     . VAL A 1 72  ? -54.18900 12.70700  -23.95500 1.000 44.41977  ? 38  VAL A O     1 
ATOM   254  C  CB    . VAL A 1 72  ? -52.42000 13.46600  -26.39100 1.000 46.36434  ? 38  VAL A CB    1 
ATOM   255  C  CG1   . VAL A 1 72  ? -51.17700 12.73800  -25.90100 1.000 36.19103  ? 38  VAL A CG1   1 
ATOM   256  C  CG2   . VAL A 1 72  ? -52.22200 13.94400  -27.82400 1.000 38.26779  ? 38  VAL A CG2   1 
ATOM   257  N  N     . THR A 1 73  ? -53.48500 10.70400  -24.72900 1.000 42.35627  ? 39  THR A N     1 
ATOM   258  C  CA    . THR A 1 73  ? -53.38500 10.06000  -23.42700 1.000 43.18521  ? 39  THR A CA    1 
ATOM   259  C  C     . THR A 1 73  ? -51.96400 9.54500   -23.22800 1.000 44.47793  ? 39  THR A C     1 
ATOM   260  O  O     . THR A 1 73  ? -51.44300 8.80600   -24.07000 1.000 44.04187  ? 39  THR A O     1 
ATOM   261  C  CB    . THR A 1 73  ? -54.38000 8.90200   -23.29100 1.000 44.25590  ? 39  THR A CB    1 
ATOM   262  O  OG1   . THR A 1 73  ? -55.71600 9.38400   -23.48900 1.000 48.50055  ? 39  THR A OG1   1 
ATOM   263  C  CG2   . THR A 1 73  ? -54.27100 8.27300   -21.90500 1.000 41.18496  ? 39  THR A CG2   1 
ATOM   264  N  N     . ILE A 1 74  ? -51.34400 9.94400   -22.12000 1.000 40.04875  ? 40  ILE A N     1 
ATOM   265  C  CA    . ILE A 1 74  ? -50.03600 9.44300   -21.70600 1.000 39.84526  ? 40  ILE A CA    1 
ATOM   266  C  C     . ILE A 1 74  ? -50.25600 8.29000   -20.73600 1.000 43.08168  ? 40  ILE A C     1 
ATOM   267  O  O     . ILE A 1 74  ? -50.90500 8.46300   -19.69900 1.000 39.73466  ? 40  ILE A O     1 
ATOM   268  C  CB    . ILE A 1 74  ? -49.19700 10.54500  -21.04200 1.000 40.14030  ? 40  ILE A CB    1 
ATOM   269  C  CG1   . ILE A 1 74  ? -49.04800 11.75600  -21.96600 1.000 38.75494  ? 40  ILE A CG1   1 
ATOM   270  C  CG2   . ILE A 1 74  ? -47.84100 9.99200   -20.61500 1.000 36.69947  ? 40  ILE A CG2   1 
ATOM   271  C  CD1   . ILE A 1 74  ? -48.38400 12.94200  -21.29300 1.000 32.63186  ? 40  ILE A CD1   1 
ATOM   272  N  N     . ILE A 1 75  ? -49.71000 7.12100   -21.05900 1.000 40.78902  ? 41  ILE A N     1 
ATOM   273  C  CA    . ILE A 1 75  ? -49.83000 5.93000   -20.22200 1.000 42.71997  ? 41  ILE A CA    1 
ATOM   274  C  C     . ILE A 1 75  ? -48.54800 5.78000   -19.41200 1.000 45.50940  ? 41  ILE A C     1 
ATOM   275  O  O     . ILE A 1 75  ? -47.46800 5.58100   -19.98300 1.000 35.21990  ? 41  ILE A O     1 
ATOM   276  C  CB    . ILE A 1 75  ? -50.09400 4.68000   -21.07400 1.000 39.46610  ? 41  ILE A CB    1 
ATOM   277  C  CG1   . ILE A 1 75  ? -51.37500 4.85700   -21.89400 1.000 46.20544  ? 41  ILE A CG1   1 
ATOM   278  C  CG2   . ILE A 1 75  ? -50.16700 3.44300   -20.19800 1.000 43.64290  ? 41  ILE A CG2   1 
ATOM   279  C  CD1   . ILE A 1 75  ? -51.58900 3.77500   -22.92600 1.000 39.09940  ? 41  ILE A CD1   1 
ATOM   280  N  N     . THR A 1 76  ? -48.65400 5.86500   -18.08700 1.000 36.39533  ? 42  THR A N     1 
ATOM   281  C  CA    . THR A 1 76  ? -47.46300 5.79100   -17.24600 1.000 38.68136  ? 42  THR A CA    1 
ATOM   282  C  C     . THR A 1 76  ? -47.86800 5.37100   -15.83400 1.000 44.71673  ? 42  THR A C     1 
ATOM   283  O  O     . THR A 1 76  ? -49.04700 5.15100   -15.54300 1.000 43.39090  ? 42  THR A O     1 
ATOM   284  C  CB    . THR A 1 76  ? -46.70200 7.12300   -17.26200 1.000 40.99095  ? 42  THR A CB    1 
ATOM   285  O  OG1   . THR A 1 76  ? -45.37500 6.92800   -16.75800 1.000 41.14106  ? 42  THR A OG1   1 
ATOM   286  C  CG2   . THR A 1 76  ? -47.41200 8.17200   -16.42300 1.000 43.46502  ? 42  THR A CG2   1 
ATOM   287  N  N     . THR A 1 77  ? -46.86000 5.24600   -14.95400 1.000 43.17631  ? 43  THR A N     1 
ATOM   288  C  CA    . THR A 1 77  ? -46.99400 4.75200   -13.59100 1.000 42.18639  ? 43  THR A CA    1 
ATOM   289  C  C     . THR A 1 77  ? -47.06000 5.91000   -12.60100 1.000 47.90897  ? 43  THR A C     1 
ATOM   290  O  O     . THR A 1 77  ? -46.65600 7.03400   -12.91900 1.000 45.74460  ? 43  THR A O     1 
ATOM   291  C  CB    . THR A 1 77  ? -45.81800 3.82400   -13.24100 1.000 41.22552  ? 43  THR A CB    1 
ATOM   292  O  OG1   . THR A 1 77  ? -44.58900 4.55800   -13.27900 1.000 43.68965  ? 43  THR A OG1   1 
ATOM   293  C  CG2   . THR A 1 77  ? -45.74500 2.65300   -14.21000 1.000 43.27178  ? 43  THR A CG2   1 
ATOM   294  N  N     . PRO A 1 78  ? -47.57200 5.66800   -11.38100 1.000 50.43018  ? 44  PRO A N     1 
ATOM   295  C  CA    . PRO A 1 78  ? -47.84600 6.79400   -10.46600 1.000 43.59832  ? 44  PRO A CA    1 
ATOM   296  C  C     . PRO A 1 78  ? -46.64200 7.66500   -10.14400 1.000 43.85045  ? 44  PRO A C     1 
ATOM   297  O  O     . PRO A 1 78  ? -46.77100 8.89500   -10.13700 1.000 43.44838  ? 44  PRO A O     1 
ATOM   298  C  CB    . PRO A 1 78  ? -48.37800 6.09200   -9.20600  1.000 49.16390  ? 44  PRO A CB    1 
ATOM   299  C  CG    . PRO A 1 78  ? -48.95700 4.82000   -9.69700  1.000 52.09996  ? 44  PRO A CG    1 
ATOM   300  C  CD    . PRO A 1 78  ? -48.08300 4.39200   -10.84200 1.000 49.84827  ? 44  PRO A CD    1 
ATOM   301  N  N     . SER A 1 79  ? -45.47900 7.07400   -9.85600  1.000 42.75410  ? 45  SER A N     1 
ATOM   302  C  CA    . SER A 1 79  ? -44.32100 7.89000   -9.50200  1.000 43.87630  ? 45  SER A CA    1 
ATOM   303  C  C     . SER A 1 79  ? -43.82900 8.71700   -10.68300 1.000 49.45812  ? 45  SER A C     1 
ATOM   304  O  O     . SER A 1 79  ? -43.26100 9.79900   -10.48800 1.000 43.24836  ? 45  SER A O     1 
ATOM   305  C  CB    . SER A 1 79  ? -43.18700 7.01100   -8.97300  1.000 44.37391  ? 45  SER A CB    1 
ATOM   306  O  OG    . SER A 1 79  ? -43.53200 6.41400   -7.73700  1.000 60.14174  ? 45  SER A OG    1 
ATOM   307  N  N     . ASN A 1 80  ? -44.02700 8.23200   -11.90700 1.000 43.22768  ? 46  ASN A N     1 
ATOM   308  C  CA    . ASN A 1 80  ? -43.58900 9.00000   -13.06600 1.000 49.55711  ? 46  ASN A CA    1 
ATOM   309  C  C     . ASN A 1 80  ? -44.58400 10.09500  -13.42600 1.000 45.48609  ? 46  ASN A C     1 
ATOM   310  O  O     . ASN A 1 80  ? -44.17200 11.19000  -13.83000 1.000 41.57876  ? 46  ASN A O     1 
ATOM   311  C  CB    . ASN A 1 80  ? -43.35300 8.07000   -14.25900 1.000 38.13904  ? 46  ASN A CB    1 
ATOM   312  C  CG    . ASN A 1 80  ? -42.15100 7.16300   -14.05400 1.000 45.53122  ? 46  ASN A CG    1 
ATOM   313  O  OD1   . ASN A 1 80  ? -41.02100 7.63400   -13.90200 1.000 42.41432  ? 46  ASN A OD1   1 
ATOM   314  N  ND2   . ASN A 1 80  ? -42.38800 5.85700   -14.05800 1.000 44.88862  ? 46  ASN A ND2   1 
ATOM   315  N  N     . ALA A 1 81  ? -45.88500 9.83100   -13.26700 1.000 42.98585  ? 47  ALA A N     1 
ATOM   316  C  CA    . ALA A 1 81  ? -46.89100 10.83800  -13.58800 1.000 46.89656  ? 47  ALA A CA    1 
ATOM   317  C  C     . ALA A 1 81  ? -46.76800 12.06600  -12.69700 1.000 54.64209  ? 47  ALA A C     1 
ATOM   318  O  O     . ALA A 1 81  ? -47.04900 13.18400  -13.14400 1.000 50.32551  ? 47  ALA A O     1 
ATOM   319  C  CB    . ALA A 1 81  ? -48.29200 10.24100  -13.47100 1.000 43.23489  ? 47  ALA A CB    1 
ATOM   320  N  N     . GLN A 1 82  ? -46.34800 11.89000  -11.44300 1.000 51.23917  ? 48  GLN A N     1 
ATOM   321  C  CA    . GLN A 1 82  ? -46.20400 13.03900  -10.55800 1.000 60.15639  ? 48  GLN A CA    1 
ATOM   322  C  C     . GLN A 1 82  ? -44.99900 13.90400  -10.90900 1.000 58.17227  ? 48  GLN A C     1 
ATOM   323  O  O     . GLN A 1 82  ? -44.84400 14.98300  -10.32700 1.000 65.08224  ? 48  GLN A O     1 
ATOM   324  C  CB    . GLN A 1 82  ? -46.12700 12.57800  -9.09800  1.000 61.58914  ? 48  GLN A CB    1 
ATOM   325  C  CG    . GLN A 1 82  ? -44.75300 12.12700  -8.63000  1.000 71.82355  ? 48  GLN A CG    1 
ATOM   326  C  CD    . GLN A 1 82  ? -44.78800 11.51200  -7.23300  1.000 87.11582  ? 48  GLN A CD    1 
ATOM   327  O  OE1   . GLN A 1 82  ? -45.74300 10.82300  -6.86700  1.000 80.68005  ? 48  GLN A OE1   1 
ATOM   328  N  NE2   . GLN A 1 82  ? -43.74300 11.76000  -6.44900  1.000 67.78772  ? 48  GLN A NE2   1 
ATOM   329  N  N     . LEU A 1 83  ? -44.15400 13.47200  -11.84600 1.000 55.30296  ? 49  LEU A N     1 
ATOM   330  C  CA    . LEU A 1 83  ? -43.08100 14.32600  -12.34000 1.000 55.52315  ? 49  LEU A CA    1 
ATOM   331  C  C     . LEU A 1 83  ? -43.56700 15.36800  -13.33900 1.000 48.10496  ? 49  LEU A C     1 
ATOM   332  O  O     . LEU A 1 83  ? -42.80300 16.27800  -13.67600 1.000 52.25138  ? 49  LEU A O     1 
ATOM   333  C  CB    . LEU A 1 83  ? -41.98000 13.48500  -12.99300 1.000 51.93246  ? 49  LEU A CB    1 
ATOM   334  C  CG    . LEU A 1 83  ? -41.25400 12.46500  -12.11700 1.000 57.26046  ? 49  LEU A CG    1 
ATOM   335  C  CD1   . LEU A 1 83  ? -40.34800 11.60900  -12.97400 1.000 46.43839  ? 49  LEU A CD1   1 
ATOM   336  C  CD2   . LEU A 1 83  ? -40.46500 13.15100  -11.01200 1.000 53.96101  ? 49  LEU A CD2   1 
ATOM   337  N  N     . PHE A 1 84  ? -44.80800 15.26000  -13.82100 1.000 49.32576  ? 50  PHE A N     1 
ATOM   338  C  CA    . PHE A 1 84  ? -45.29400 16.21700  -14.80800 1.000 53.81874  ? 50  PHE A CA    1 
ATOM   339  C  C     . PHE A 1 84  ? -46.79700 16.46500  -14.71900 1.000 54.58432  ? 50  PHE A C     1 
ATOM   340  O  O     . PHE A 1 84  ? -47.34800 17.09900  -15.62900 1.000 53.58324  ? 50  PHE A O     1 
ATOM   341  C  CB    . PHE A 1 84  ? -44.92000 15.74700  -16.22800 1.000 43.82917  ? 50  PHE A CB    1 
ATOM   342  C  CG    . PHE A 1 84  ? -45.52100 14.42000  -16.61800 1.000 47.18829  ? 50  PHE A CG    1 
ATOM   343  C  CD1   . PHE A 1 84  ? -44.86600 13.23500  -16.32500 1.000 46.45943  ? 50  PHE A CD1   1 
ATOM   344  C  CD2   . PHE A 1 84  ? -46.72900 14.36000  -17.29600 1.000 43.34115  ? 50  PHE A CD2   1 
ATOM   345  C  CE1   . PHE A 1 84  ? -45.41100 12.01500  -16.68800 1.000 42.60298  ? 50  PHE A CE1   1 
ATOM   346  C  CE2   . PHE A 1 84  ? -47.28000 13.14200  -17.66600 1.000 42.02702  ? 50  PHE A CE2   1 
ATOM   347  C  CZ    . PHE A 1 84  ? -46.62000 11.96800  -17.36000 1.000 40.36126  ? 50  PHE A CZ    1 
ATOM   348  N  N     . ASP A 1 85  ? -47.47800 16.01000  -13.66300 1.000 55.72510  ? 51  ASP A N     1 
ATOM   349  C  CA    . ASP A 1 85  ? -48.92200 16.20600  -13.56500 1.000 58.95169  ? 51  ASP A CA    1 
ATOM   350  C  C     . ASP A 1 85  ? -49.29100 17.68100  -13.43600 1.000 57.42861  ? 51  ASP A C     1 
ATOM   351  O  O     . ASP A 1 85  ? -50.35500 18.09300  -13.90900 1.000 60.03148  ? 51  ASP A O     1 
ATOM   352  C  CB    . ASP A 1 85  ? -49.48000 15.41200  -12.38200 1.000 64.63919  ? 51  ASP A CB    1 
ATOM   353  C  CG    . ASP A 1 85  ? -48.95500 15.90700  -11.04600 1.000 76.68859  ? 51  ASP A CG    1 
ATOM   354  O  OD1   . ASP A 1 85  ? -47.75200 16.24100  -10.96400 1.000 75.17140  ? 51  ASP A OD1   1 
ATOM   355  O  OD2   . ASP A 1 85  ? -49.74300 15.96300  -10.07700 1.000 90.79087  ? 51  ASP A OD2   1 
ATOM   356  N  N     . LYS A 1 86  ? -48.43800 18.48600  -12.79700 1.000 58.61653  ? 52  LYS A N     1 
ATOM   357  C  CA    . LYS A 1 86  ? -48.71400 19.91600  -12.69900 1.000 61.85640  ? 52  LYS A CA    1 
ATOM   358  C  C     . LYS A 1 86  ? -48.69400 20.57800  -14.07100 1.000 63.96640  ? 52  LYS A C     1 
ATOM   359  O  O     . LYS A 1 86  ? -49.48900 21.49000  -14.32900 1.000 57.11092  ? 52  LYS A O     1 
ATOM   360  C  CB    . LYS A 1 86  ? -47.71800 20.59600  -11.75000 1.000 63.32167  ? 52  LYS A CB    1 
ATOM   361  C  CG    . LYS A 1 86  ? -47.81600 20.20800  -10.27300 1.000 86.89772  ? 52  LYS A CG    1 
ATOM   362  C  CD    . LYS A 1 86  ? -46.77300 20.91500  -9.41400  1.000 92.04020  ? 52  LYS A CD    1 
ATOM   363  C  CE    . LYS A 1 86  ? -46.92000 20.52100  -7.95000  1.000 101.85092 ? 52  LYS A CE    1 
ATOM   364  N  NZ    . LYS A 1 86  ? -45.90000 21.17600  -7.09100  1.000 104.22956 ? 52  LYS A NZ    1 
ATOM   365  N  N     . THR A 1 87  ? -47.81000 20.12400  -14.96500 1.000 55.61988  ? 53  THR A N     1 
ATOM   366  C  CA    . THR A 1 87  ? -47.82300 20.62100  -16.33700 1.000 57.39095  ? 53  THR A CA    1 
ATOM   367  C  C     . THR A 1 87  ? -49.09200 20.19100  -17.06200 1.000 51.46621  ? 53  THR A C     1 
ATOM   368  O  O     . THR A 1 87  ? -49.66600 20.97000  -17.83200 1.000 49.04104  ? 53  THR A O     1 
ATOM   369  C  CB    . THR A 1 87  ? -46.58000 20.12900  -17.08200 1.000 56.89275  ? 53  THR A CB    1 
ATOM   370  O  OG1   . THR A 1 87  ? -45.40300 20.61700  -16.42800 1.000 57.39836  ? 53  THR A OG1   1 
ATOM   371  C  CG2   . THR A 1 87  ? -46.58800 20.61100  -18.52800 1.000 50.47798  ? 53  THR A CG2   1 
ATOM   372  N  N     . ILE A 1 88  ? -49.54900 18.96000  -16.81700 1.000 48.91096  ? 54  ILE A N     1 
ATOM   373  C  CA    . ILE A 1 88  ? -50.77200 18.47100  -17.45000 1.000 57.52462  ? 54  ILE A CA    1 
ATOM   374  C  C     . ILE A 1 88  ? -51.96900 19.30400  -17.01200 1.000 63.58281  ? 54  ILE A C     1 
ATOM   375  O  O     . ILE A 1 88  ? -52.84700 19.63200  -17.82200 1.000 59.92142  ? 54  ILE A O     1 
ATOM   376  C  CB    . ILE A 1 88  ? -50.98100 16.97800  -17.13100 1.000 58.97754  ? 54  ILE A CB    1 
ATOM   377  C  CG1   . ILE A 1 88  ? -49.76500 16.15800  -17.56500 1.000 53.55440  ? 54  ILE A CG1   1 
ATOM   378  C  CG2   . ILE A 1 88  ? -52.24400 16.45900  -17.80500 1.000 54.98270  ? 54  ILE A CG2   1 
ATOM   379  C  CD1   . ILE A 1 88  ? -49.44600 16.27200  -19.03900 1.000 56.06394  ? 54  ILE A CD1   1 
ATOM   380  N  N     . GLU A 1 89  ? -52.02700 19.65500  -15.72400 1.000 59.71793  ? 55  GLU A N     1 
ATOM   381  C  CA    . GLU A 1 89  ? -53.12400 20.48100  -15.23100 1.000 67.34153  ? 55  GLU A CA    1 
ATOM   382  C  C     . GLU A 1 89  ? -53.14400 21.83400  -15.92900 1.000 64.50399  ? 55  GLU A C     1 
ATOM   383  O  O     . GLU A 1 89  ? -54.21500 22.34900  -16.27300 1.000 64.91121  ? 55  GLU A O     1 
ATOM   384  C  CB    . GLU A 1 89  ? -53.00700 20.65500  -13.71600 1.000 68.27240  ? 55  GLU A CB    1 
ATOM   385  C  CG    . GLU A 1 89  ? -53.51800 19.46900  -12.90400 1.000 81.78974  ? 55  GLU A CG    1 
ATOM   386  C  CD    . GLU A 1 89  ? -54.72200 18.79000  -13.53600 1.000 89.64045  ? 55  GLU A CD    1 
ATOM   387  O  OE1   . GLU A 1 89  ? -55.82600 19.37400  -13.49300 1.000 88.60768  ? 55  GLU A OE1   1 
ATOM   388  O  OE2   . GLU A 1 89  ? -54.56700 17.67000  -14.07100 1.000 79.85533  ? 55  GLU A OE2   1 
ATOM   389  N  N     . GLU A 1 90  ? -51.96700 22.41900  -16.16000 1.000 62.07223  ? 56  GLU A N     1 
ATOM   390  C  CA    . GLU A 1 90  ? -51.89900 23.69400  -16.86300 1.000 61.32349  ? 56  GLU A CA    1 
ATOM   391  C  C     . GLU A 1 90  ? -52.32800 23.54800  -18.31800 1.000 64.97831  ? 56  GLU A C     1 
ATOM   392  O  O     . GLU A 1 90  ? -52.95800 24.45300  -18.87800 1.000 64.42194  ? 56  GLU A O     1 
ATOM   393  C  CB    . GLU A 1 90  ? -50.48500 24.26100  -16.77000 1.000 63.43035  ? 56  GLU A CB    1 
ATOM   394  C  CG    . GLU A 1 90  ? -50.18800 24.92900  -15.44000 1.000 70.31467  ? 56  GLU A CG    1 
ATOM   395  C  CD    . GLU A 1 90  ? -48.71800 25.24600  -15.26400 1.000 83.49638  ? 56  GLU A CD    1 
ATOM   396  O  OE1   . GLU A 1 90  ? -47.92100 24.87300  -16.15100 1.000 82.30183  ? 56  GLU A OE1   1 
ATOM   397  O  OE2   . GLU A 1 90  ? -48.35800 25.86700  -14.24100 1.000 85.24443  ? 56  GLU A OE2   1 
ATOM   398  N  N     . GLU A 1 91  ? -51.99800 22.41900  -18.95100 1.000 58.44270  ? 57  GLU A N     1 
ATOM   399  C  CA    . GLU A 1 91  ? -52.43300 22.20100  -20.32800 1.000 67.87771  ? 57  GLU A CA    1 
ATOM   400  C  C     . GLU A 1 91  ? -53.93800 21.98000  -20.39800 1.000 63.10116  ? 57  GLU A C     1 
ATOM   401  O  O     . GLU A 1 91  ? -54.60500 22.48900  -21.30600 1.000 69.21776  ? 57  GLU A O     1 
ATOM   402  C  CB    . GLU A 1 91  ? -51.68800 21.01600  -20.94300 1.000 60.20008  ? 57  GLU A CB    1 
ATOM   403  C  CG    . GLU A 1 91  ? -50.17600 21.18100  -21.00100 1.000 53.01596  ? 57  GLU A CG    1 
ATOM   404  C  CD    . GLU A 1 91  ? -49.72000 22.02800  -22.17200 1.000 58.39646  ? 57  GLU A CD    1 
ATOM   405  O  OE1   . GLU A 1 91  ? -50.58000 22.46600  -22.96500 1.000 72.78079  ? 57  GLU A OE1   1 
ATOM   406  O  OE2   . GLU A 1 91  ? -48.49900 22.25500  -22.30100 1.000 49.96686  ? 57  GLU A OE2   1 
ATOM   407  N  N     . LYS A 1 92  ? -54.48900 21.21600  -19.45200 1.000 60.50067  ? 58  LYS A N     1 
ATOM   408  C  CA    . LYS A 1 92  ? -55.93400 21.02200  -19.41000 1.000 70.03147  ? 58  LYS A CA    1 
ATOM   409  C  C     . LYS A 1 92  ? -56.65500 22.34100  -19.15700 1.000 71.41313  ? 58  LYS A C     1 
ATOM   410  O  O     . LYS A 1 92  ? -57.71200 22.60200  -19.74400 1.000 62.42665  ? 58  LYS A O     1 
ATOM   411  C  CB    . LYS A 1 92  ? -56.29400 19.99300  -18.33700 1.000 69.38551  ? 58  LYS A CB    1 
ATOM   412  C  CG    . LYS A 1 92  ? -55.95900 18.56300  -18.72700 1.000 66.38203  ? 58  LYS A CG    1 
ATOM   413  C  CD    . LYS A 1 92  ? -56.87700 17.56000  -18.04600 1.000 74.07484  ? 58  LYS A CD    1 
ATOM   414  C  CE    . LYS A 1 92  ? -56.09100 16.59400  -17.17700 1.000 65.23019  ? 58  LYS A CE    1 
ATOM   415  N  NZ    . LYS A 1 92  ? -56.96900 15.87500  -16.21400 1.000 81.56139  ? 58  LYS A NZ    1 
ATOM   416  N  N     . ALA A 1 93  ? -56.08800 23.19100  -18.29600 1.000 70.68517  ? 59  ALA A N     1 
ATOM   417  C  CA    . ALA A 1 93  ? -56.67900 24.49500  -18.01900 1.000 72.19719  ? 59  ALA A CA    1 
ATOM   418  C  C     . ALA A 1 93  ? -56.63700 25.42300  -19.22600 1.000 66.56788  ? 59  ALA A C     1 
ATOM   419  O  O     . ALA A 1 93  ? -57.40100 26.39300  -19.27100 1.000 76.03676  ? 59  ALA A O     1 
ATOM   420  C  CB    . ALA A 1 93  ? -55.97100 25.15300  -16.83300 1.000 69.78043  ? 59  ALA A CB    1 
ATOM   421  N  N     . ALA A 1 94  ? -55.76500 25.15700  -20.19600 1.000 64.61768  ? 60  ALA A N     1 
ATOM   422  C  CA    . ALA A 1 94  ? -55.70900 25.93200  -21.42800 1.000 67.92048  ? 60  ALA A CA    1 
ATOM   423  C  C     . ALA A 1 94  ? -56.61400 25.37300  -22.52000 1.000 71.05144  ? 60  ALA A C     1 
ATOM   424  O  O     . ALA A 1 94  ? -56.59500 25.88600  -23.64500 1.000 71.64870  ? 60  ALA A O     1 
ATOM   425  C  CB    . ALA A 1 94  ? -54.26700 26.00700  -21.94100 1.000 66.84663  ? 60  ALA A CB    1 
ATOM   426  N  N     . GLY A 1 95  ? -57.40000 24.34000  -22.22000 1.000 64.74873  ? 61  GLY A N     1 
ATOM   427  C  CA    . GLY A 1 95  ? -58.30900 23.75900  -23.18300 1.000 64.96993  ? 61  GLY A CA    1 
ATOM   428  C  C     . GLY A 1 95  ? -57.75400 22.59700  -23.97500 1.000 74.18139  ? 61  GLY A C     1 
ATOM   429  O  O     . GLY A 1 95  ? -58.47800 22.03400  -24.80800 1.000 71.33484  ? 61  GLY A O     1 
ATOM   430  N  N     . HIS A 1 96  ? -56.50100 22.21300  -23.74200 1.000 71.42136  ? 62  HIS A N     1 
ATOM   431  C  CA    . HIS A 1 96  ? -55.88800 21.12600  -24.49100 1.000 70.27875  ? 62  HIS A CA    1 
ATOM   432  C  C     . HIS A 1 96  ? -56.35000 19.78300  -23.94100 1.000 63.26425  ? 62  HIS A C     1 
ATOM   433  O  O     . HIS A 1 96  ? -56.38000 19.57500  -22.72400 1.000 60.76297  ? 62  HIS A O     1 
ATOM   434  C  CB    . HIS A 1 96  ? -54.36600 21.23500  -24.43600 1.000 59.88033  ? 62  HIS A CB    1 
ATOM   435  C  CG    . HIS A 1 96  ? -53.83100 22.46600  -25.10000 1.000 69.19933  ? 62  HIS A CG    1 
ATOM   436  N  ND1   . HIS A 1 96  ? -52.70300 23.12300  -24.65700 1.000 76.00487  ? 62  HIS A ND1   1 
ATOM   437  C  CD2   . HIS A 1 96  ? -54.27400 23.16100  -26.17400 1.000 60.33257  ? 62  HIS A CD2   1 
ATOM   438  C  CE1   . HIS A 1 96  ? -52.47300 24.16900  -25.43100 1.000 69.61486  ? 62  HIS A CE1   1 
ATOM   439  N  NE2   . HIS A 1 96  ? -53.41200 24.21500  -26.35800 1.000 67.19035  ? 62  HIS A NE2   1 
ATOM   440  N  N     . HIS A 1 97  ? -56.71100 18.87300  -24.84500 1.000 56.42457  ? 63  HIS A N     1 
ATOM   441  C  CA    . HIS A 1 97  ? -57.22400 17.55800  -24.46600 1.000 60.69502  ? 63  HIS A CA    1 
ATOM   442  C  C     . HIS A 1 97  ? -56.04200 16.61300  -24.27500 1.000 60.46310  ? 63  HIS A C     1 
ATOM   443  O  O     . HIS A 1 97  ? -55.65100 15.87000  -25.17800 1.000 58.31782  ? 63  HIS A O     1 
ATOM   444  C  CB    . HIS A 1 97  ? -58.20900 17.04900  -25.51400 1.000 53.78637  ? 63  HIS A CB    1 
ATOM   445  C  CG    . HIS A 1 97  ? -59.37400 17.96800  -25.74200 1.000 76.71369  ? 63  HIS A CG    1 
ATOM   446  N  ND1   . HIS A 1 97  ? -60.06500 18.56300  -24.70900 1.000 80.12950  ? 63  HIS A ND1   1 
ATOM   447  C  CD2   . HIS A 1 97  ? -59.97000 18.39000  -26.88400 1.000 78.48955  ? 63  HIS A CD2   1 
ATOM   448  C  CE1   . HIS A 1 97  ? -61.03200 19.31600  -25.20200 1.000 72.48091  ? 63  HIS A CE1   1 
ATOM   449  N  NE2   . HIS A 1 97  ? -60.99700 19.22800  -26.51900 1.000 79.22969  ? 63  HIS A NE2   1 
ATOM   450  N  N     . ILE A 1 98  ? -55.46200 16.64700  -23.07700 1.000 49.84646  ? 64  ILE A N     1 
ATOM   451  C  CA    . ILE A 1 98  ? -54.34600 15.78300  -22.70700 1.000 56.75231  ? 64  ILE A CA    1 
ATOM   452  C  C     . ILE A 1 98  ? -54.59900 15.23900  -21.30800 1.000 50.64681  ? 64  ILE A C     1 
ATOM   453  O  O     . ILE A 1 98  ? -54.98100 15.98600  -20.40200 1.000 58.45109  ? 64  ILE A O     1 
ATOM   454  C  CB    . ILE A 1 98  ? -52.99300 16.52200  -22.76900 1.000 50.12127  ? 64  ILE A CB    1 
ATOM   455  C  CG1   . ILE A 1 98  ? -51.85300 15.59000  -22.35900 1.000 53.42203  ? 64  ILE A CG1   1 
ATOM   456  C  CG2   . ILE A 1 98  ? -53.01000 17.78000  -21.90800 1.000 56.97430  ? 64  ILE A CG2   1 
ATOM   457  C  CD1   . ILE A 1 98  ? -50.48900 16.05900  -22.83300 1.000 48.16189  ? 64  ILE A CD1   1 
ATOM   458  N  N     . ARG A 1 99  ? -54.39400 13.93600  -21.13300 1.000 48.18216  ? 65  ARG A N     1 
ATOM   459  C  CA    . ARG A 1 99  ? -54.63200 13.30200  -19.84700 1.000 46.46866  ? 65  ARG A CA    1 
ATOM   460  C  C     . ARG A 1 99  ? -53.61800 12.18500  -19.64700 1.000 53.43517  ? 65  ARG A C     1 
ATOM   461  O  O     . ARG A 1 99  ? -52.93900 11.75400  -20.58200 1.000 46.85083  ? 65  ARG A O     1 
ATOM   462  C  CB    . ARG A 1 99  ? -56.06500 12.76400  -19.74900 1.000 59.61050  ? 65  ARG A CB    1 
ATOM   463  C  CG    . ARG A 1 99  ? -56.42000 11.74200  -20.81600 1.000 65.87485  ? 65  ARG A CG    1 
ATOM   464  C  CD    . ARG A 1 99  ? -57.82100 11.17900  -20.60000 1.000 74.26539  ? 65  ARG A CD    1 
ATOM   465  N  NE    . ARG A 1 99  ? -58.15900 10.16200  -21.58900 1.000 105.91505 ? 65  ARG A NE    1 
ATOM   466  C  CZ    . ARG A 1 99  ? -59.33400 9.55100   -21.66800 1.000 117.41162 ? 65  ARG A CZ    1 
ATOM   467  N  NH1   . ARG A 1 99  ? -60.31300 9.82000   -20.81800 1.000 117.67121 ? 65  ARG A NH1   1 
ATOM   468  N  NH2   . ARG A 1 99  ? -59.53300 8.64900   -22.62600 1.000 111.82362 ? 65  ARG A NH2   1 
ATOM   469  N  N     . VAL A 1 100 ? -53.52700 11.71900  -18.40500 1.000 49.24141  ? 66  VAL A N     1 
ATOM   470  C  CA    . VAL A 1 100 ? -52.63000 10.63800  -18.02300 1.000 47.39893  ? 66  VAL A CA    1 
ATOM   471  C  C     . VAL A 1 100 ? -53.47200 9.45800   -17.56300 1.000 49.61857  ? 66  VAL A C     1 
ATOM   472  O  O     . VAL A 1 100 ? -54.34000 9.61200   -16.69600 1.000 58.39706  ? 66  VAL A O     1 
ATOM   473  C  CB    . VAL A 1 100 ? -51.65700 11.07400  -16.91300 1.000 49.17685  ? 66  VAL A CB    1 
ATOM   474  C  CG1   . VAL A 1 100 ? -50.67900 9.95300   -16.59800 1.000 53.44986  ? 66  VAL A CG1   1 
ATOM   475  C  CG2   . VAL A 1 100 ? -50.92500 12.34400  -17.31400 1.000 46.48992  ? 66  VAL A CG2   1 
ATOM   476  N  N     . HIS A 1 101 ? -53.22200 8.28700   -18.14100 1.000 48.30527  ? 67  HIS A N     1 
ATOM   477  C  CA    . HIS A 1 101 ? -53.82100 7.04300   -17.67500 1.000 50.34537  ? 67  HIS A CA    1 
ATOM   478  C  C     . HIS A 1 101 ? -52.79600 6.29200   -16.83200 1.000 55.26790  ? 67  HIS A C     1 
ATOM   479  O  O     . HIS A 1 101 ? -51.75900 5.86000   -17.34700 1.000 47.94219  ? 67  HIS A O     1 
ATOM   480  C  CB    . HIS A 1 101 ? -54.29400 6.17300   -18.83800 1.000 48.82898  ? 67  HIS A CB    1 
ATOM   481  C  CG    . HIS A 1 101 ? -54.77600 4.82300   -18.41100 1.000 56.61770  ? 67  HIS A CG    1 
ATOM   482  N  ND1   . HIS A 1 101 ? -55.92900 4.64300   -17.67700 1.000 57.97451  ? 67  HIS A ND1   1 
ATOM   483  C  CD2   . HIS A 1 101 ? -54.25000 3.58900   -18.59300 1.000 58.07310  ? 67  HIS A CD2   1 
ATOM   484  C  CE1   . HIS A 1 101 ? -56.09800 3.35500   -17.43500 1.000 60.21780  ? 67  HIS A CE1   1 
ATOM   485  N  NE2   . HIS A 1 101 ? -55.09100 2.69400   -17.97800 1.000 52.81279  ? 67  HIS A NE2   1 
ATOM   486  N  N     . ILE A 1 102 ? -53.09100 6.13800   -15.54500 1.000 52.64511  ? 68  ILE A N     1 
ATOM   487  C  CA    . ILE A 1 102 ? -52.17700 5.48700   -14.61300 1.000 50.39468  ? 68  ILE A CA    1 
ATOM   488  C  C     . ILE A 1 102 ? -52.25800 3.97700   -14.78800 1.000 56.75392  ? 68  ILE A C     1 
ATOM   489  O  O     . ILE A 1 102 ? -53.35200 3.40500   -14.87000 1.000 56.88162  ? 68  ILE A O     1 
ATOM   490  C  CB    . ILE A 1 102 ? -52.50200 5.89000   -13.16700 1.000 53.02586  ? 68  ILE A CB    1 
ATOM   491  C  CG1   . ILE A 1 102 ? -52.34400 7.39900   -12.98500 1.000 49.30221  ? 68  ILE A CG1   1 
ATOM   492  C  CG2   . ILE A 1 102 ? -51.62600 5.12200   -12.18200 1.000 50.43039  ? 68  ILE A CG2   1 
ATOM   493  C  CD1   . ILE A 1 102 ? -50.99700 7.91700   -13.39600 1.000 49.16821  ? 68  ILE A CD1   1 
ATOM   494  N  N     . ILE A 1 103 ? -51.09700 3.33000   -14.85500 1.000 50.17548  ? 69  ILE A N     1 
ATOM   495  C  CA    . ILE A 1 103 ? -50.99500 1.88000   -14.75200 1.000 48.78833  ? 69  ILE A CA    1 
ATOM   496  C  C     . ILE A 1 103 ? -50.06700 1.55600   -13.59200 1.000 54.58553  ? 69  ILE A C     1 
ATOM   497  O  O     . ILE A 1 103 ? -49.19800 2.35400   -13.22300 1.000 52.57578  ? 69  ILE A O     1 
ATOM   498  C  CB    . ILE A 1 103 ? -50.49500 1.21700   -16.05400 1.000 59.55956  ? 69  ILE A CB    1 
ATOM   499  C  CG1   . ILE A 1 103 ? -49.03700 1.60500   -16.32200 1.000 55.12744  ? 69  ILE A CG1   1 
ATOM   500  C  CG2   . ILE A 1 103 ? -51.40700 1.56800   -17.22100 1.000 50.60711  ? 69  ILE A CG2   1 
ATOM   501  C  CD1   . ILE A 1 103 ? -48.48500 1.05600   -17.60500 1.000 58.32281  ? 69  ILE A CD1   1 
ATOM   502  N  N     . LYS A 1 104 ? -50.26300 0.37500   -13.01100 1.000 51.19761  ? 70  LYS A N     1 
ATOM   503  C  CA    . LYS A 1 104 ? -49.50100 -0.04800  -11.84200 1.000 52.58815  ? 70  LYS A CA    1 
ATOM   504  C  C     . LYS A 1 104 ? -48.08900 -0.45300  -12.25600 1.000 52.51834  ? 70  LYS A C     1 
ATOM   505  O  O     . LYS A 1 104 ? -47.91400 -1.32700  -13.11200 1.000 54.30222  ? 70  LYS A O     1 
ATOM   506  C  CB    . LYS A 1 104 ? -50.21300 -1.21000  -11.15100 1.000 53.10775  ? 70  LYS A CB    1 
ATOM   507  C  CG    . LYS A 1 104 ? -49.77100 -1.47200  -9.71900  1.000 67.89586  ? 70  LYS A CG    1 
ATOM   508  C  CD    . LYS A 1 104 ? -50.32800 -2.79900  -9.20400  1.000 74.26758  ? 70  LYS A CD    1 
ATOM   509  C  CE    . LYS A 1 104 ? -50.93000 -2.65200  -7.81100  1.000 76.37856  ? 70  LYS A CE    1 
ATOM   510  N  NZ    . LYS A 1 104 ? -52.42100 -2.62100  -7.84700  1.000 89.64060  ? 70  LYS A NZ    1 
ATOM   511  N  N     . PHE A 1 105 ? -47.08700 0.17300   -11.64900 1.000 44.85333  ? 71  PHE A N     1 
ATOM   512  C  CA    . PHE A 1 105 ? -45.71100 -0.26000  -11.86600 1.000 44.32135  ? 71  PHE A CA    1 
ATOM   513  C  C     . PHE A 1 105 ? -45.51500 -1.65000  -11.27000 1.000 49.17004  ? 71  PHE A C     1 
ATOM   514  O  O     . PHE A 1 105 ? -45.89300 -1.88300  -10.11500 1.000 47.90020  ? 71  PHE A O     1 
ATOM   515  C  CB    . PHE A 1 105 ? -44.72100 0.72200   -11.24600 1.000 44.35018  ? 71  PHE A CB    1 
ATOM   516  C  CG    . PHE A 1 105 ? -43.29000 0.45700   -11.63100 1.000 44.17469  ? 71  PHE A CG    1 
ATOM   517  C  CD1   . PHE A 1 105 ? -42.76900 0.98400   -12.80100 1.000 40.80847  ? 71  PHE A CD1   1 
ATOM   518  C  CD2   . PHE A 1 105 ? -42.46900 -0.32000  -10.82800 1.000 43.14832  ? 71  PHE A CD2   1 
ATOM   519  C  CE1   . PHE A 1 105 ? -41.45600 0.74100   -13.16700 1.000 43.28154  ? 71  PHE A CE1   1 
ATOM   520  C  CE2   . PHE A 1 105 ? -41.15700 -0.56600  -11.18600 1.000 43.99324  ? 71  PHE A CE2   1 
ATOM   521  C  CZ    . PHE A 1 105 ? -40.65100 -0.03600  -12.36200 1.000 49.77702  ? 71  PHE A CZ    1 
ATOM   522  N  N     . PRO A 1 106 ? -44.92000 -2.58800  -12.00700 1.000 45.38230  ? 72  PRO A N     1 
ATOM   523  C  CA    . PRO A 1 106 ? -44.85300 -3.97500  -11.52700 1.000 47.95070  ? 72  PRO A CA    1 
ATOM   524  C  C     . PRO A 1 106 ? -43.81500 -4.17700  -10.43400 1.000 47.23267  ? 72  PRO A C     1 
ATOM   525  O  O     . PRO A 1 106 ? -42.88900 -4.97800  -10.59600 1.000 37.62907  ? 72  PRO A O     1 
ATOM   526  C  CB    . PRO A 1 106 ? -44.48400 -4.75800  -12.79200 1.000 47.61313  ? 72  PRO A CB    1 
ATOM   527  C  CG    . PRO A 1 106 ? -43.68100 -3.78500  -13.58900 1.000 44.68731  ? 72  PRO A CG    1 
ATOM   528  C  CD    . PRO A 1 106 ? -44.28900 -2.42900  -13.32900 1.000 44.53595  ? 72  PRO A CD    1 
ATOM   529  N  N     . SER A 1 107 ? -43.96000 -3.45500  -9.32000  1.000 42.40116  ? 73  SER A N     1 
ATOM   530  C  CA    . SER A 1 107 ? -42.98300 -3.55900  -8.24300  1.000 42.21538  ? 73  SER A CA    1 
ATOM   531  C  C     . SER A 1 107 ? -42.95500 -4.96600  -7.65500  1.000 39.69042  ? 73  SER A C     1 
ATOM   532  O  O     . SER A 1 107 ? -41.87900 -5.49900  -7.35900  1.000 44.66418  ? 73  SER A O     1 
ATOM   533  C  CB    . SER A 1 107 ? -43.29300 -2.52700  -7.16000  1.000 48.57009  ? 73  SER A CB    1 
ATOM   534  O  OG    . SER A 1 107 ? -43.33100 -1.22000  -7.70700  1.000 43.01006  ? 73  SER A OG    1 
ATOM   535  N  N     . ALA A 1 108 ? -44.12700 -5.59000  -7.50300  1.000 37.01078  ? 74  ALA A N     1 
ATOM   536  C  CA    . ALA A 1 108 ? -44.20800 -6.88900  -6.84100  1.000 38.34757  ? 74  ALA A CA    1 
ATOM   537  C  C     . ALA A 1 108 ? -43.55300 -7.98000  -7.67400  1.000 45.27146  ? 74  ALA A C     1 
ATOM   538  O  O     . ALA A 1 108 ? -42.82300 -8.82500  -7.14200  1.000 45.69959  ? 74  ALA A O     1 
ATOM   539  C  CB    . ALA A 1 108 ? -45.66800 -7.23900  -6.56000  1.000 49.71265  ? 74  ALA A CB    1 
ATOM   540  N  N     . GLN A 1 109 ? -43.80900 -7.97800  -8.98200  1.000 45.66044  ? 75  GLN A N     1 
ATOM   541  C  CA    . GLN A 1 109 ? -43.21300 -8.96100  -9.87700  1.000 48.70681  ? 75  GLN A CA    1 
ATOM   542  C  C     . GLN A 1 109 ? -41.69900 -8.84000  -9.94900  1.000 44.43961  ? 75  GLN A C     1 
ATOM   543  O  O     . GLN A 1 109 ? -41.02900 -9.81700  -10.29500 1.000 53.23717  ? 75  GLN A O     1 
ATOM   544  C  CB    . GLN A 1 109 ? -43.80800 -8.83200  -11.28900 1.000 54.83797  ? 75  GLN A CB    1 
ATOM   545  C  CG    . GLN A 1 109 ? -45.35200 -8.69800  -11.39600 1.000 58.46283  ? 75  GLN A CG    1 
ATOM   546  C  CD    . GLN A 1 109 ? -45.92600 -7.35100  -10.92900 1.000 70.35464  ? 75  GLN A CD    1 
ATOM   547  O  OE1   . GLN A 1 109 ? -45.45900 -6.75500  -9.95900  1.000 61.59149  ? 75  GLN A OE1   1 
ATOM   548  N  NE2   . GLN A 1 109 ? -46.95600 -6.87600  -11.63100 1.000 79.26499  ? 75  GLN A NE2   1 
ATOM   549  N  N     . LEU A 1 110 ? -41.14900 -7.67000  -9.64600  1.000 46.06359  ? 76  LEU A N     1 
ATOM   550  C  CA    . LEU A 1 110 ? -39.71500 -7.44300  -9.73700  1.000 43.68605  ? 76  LEU A CA    1 
ATOM   551  C  C     . LEU A 1 110 ? -39.02600 -7.44100  -8.38300  1.000 45.28391  ? 76  LEU A C     1 
ATOM   552  O  O     . LEU A 1 110 ? -37.79400 -7.33800  -8.33000  1.000 46.92519  ? 76  LEU A O     1 
ATOM   553  C  CB    . LEU A 1 110 ? -39.43300 -6.11900  -10.45500 1.000 40.93556  ? 76  LEU A CB    1 
ATOM   554  C  CG    . LEU A 1 110 ? -39.93300 -6.05900  -11.89800 1.000 51.67527  ? 76  LEU A CG    1 
ATOM   555  C  CD1   . LEU A 1 110 ? -40.03600 -4.61800  -12.36900 1.000 45.69157  ? 76  LEU A CD1   1 
ATOM   556  C  CD2   . LEU A 1 110 ? -39.01600 -6.86700  -12.80500 1.000 45.79354  ? 76  LEU A CD2   1 
ATOM   557  N  N     . GLY A 1 111 ? -39.78100 -7.55500  -7.29400  1.000 39.06030  ? 77  GLY A N     1 
ATOM   558  C  CA    . GLY A 1 111 ? -39.18900 -7.46100  -5.97800  1.000 47.12855  ? 77  GLY A CA    1 
ATOM   559  C  C     . GLY A 1 111 ? -38.64700 -6.09400  -5.64300  1.000 48.99157  ? 77  GLY A C     1 
ATOM   560  O  O     . GLY A 1 111 ? -37.75900 -5.98100  -4.79500  1.000 46.78057  ? 77  GLY A O     1 
ATOM   561  N  N     . LEU A 1 112 ? -39.15700 -5.04500  -6.28900  1.000 37.80956  ? 78  LEU A N     1 
ATOM   562  C  CA    . LEU A 1 112 ? -38.67800 -3.69100  -6.03600  1.000 39.01893  ? 78  LEU A CA    1 
ATOM   563  C  C     . LEU A 1 112 ? -39.53300 -3.00900  -4.97100  1.000 42.95887  ? 78  LEU A C     1 
ATOM   564  O  O     . LEU A 1 112 ? -40.75600 -3.17900  -4.95000  1.000 45.43728  ? 78  LEU A O     1 
ATOM   565  C  CB    . LEU A 1 112 ? -38.70700 -2.86000  -7.31600  1.000 32.07963  ? 78  LEU A CB    1 
ATOM   566  C  CG    . LEU A 1 112 ? -37.71900 -3.24000  -8.42000  1.000 41.10826  ? 78  LEU A CG    1 
ATOM   567  C  CD1   . LEU A 1 112 ? -38.08000 -2.53000  -9.72500  1.000 39.36807  ? 78  LEU A CD1   1 
ATOM   568  C  CD2   . LEU A 1 112 ? -36.30000 -2.89900  -7.99400  1.000 38.26004  ? 78  LEU A CD2   1 
ATOM   569  N  N     . PRO A 1 113 ? -38.92300 -2.22800  -4.08800  1.000 48.71156  ? 79  PRO A N     1 
ATOM   570  C  CA    . PRO A 1 113 ? -39.71600 -1.47600  -3.11300  1.000 41.13623  ? 79  PRO A CA    1 
ATOM   571  C  C     . PRO A 1 113 ? -40.48200 -0.36200  -3.80700  1.000 48.89611  ? 79  PRO A C     1 
ATOM   572  O  O     . PRO A 1 113 ? -40.06200 0.15500   -4.84600  1.000 44.19544  ? 79  PRO A O     1 
ATOM   573  C  CB    . PRO A 1 113 ? -38.66300 -0.92000  -2.14800  1.000 46.31954  ? 79  PRO A CB    1 
ATOM   574  C  CG    . PRO A 1 113 ? -37.42100 -0.81700  -2.97900  1.000 40.05269  ? 79  PRO A CG    1 
ATOM   575  C  CD    . PRO A 1 113 ? -37.47900 -1.95500  -3.96900  1.000 35.30808  ? 79  PRO A CD    1 
ATOM   576  N  N     . THR A 1 114 ? -41.62000 0.00200   -3.22000  1.000 43.87219  ? 80  THR A N     1 
ATOM   577  C  CA    . THR A 1 114 ? -42.50600 0.97400   -3.84700  1.000 46.70337  ? 80  THR A CA    1 
ATOM   578  C  C     . THR A 1 114 ? -41.79300 2.31100   -4.03800  1.000 38.38081  ? 80  THR A C     1 
ATOM   579  O  O     . THR A 1 114 ? -40.88500 2.67500   -3.28500  1.000 46.94907  ? 80  THR A O     1 
ATOM   580  C  CB    . THR A 1 114 ? -43.77300 1.15800   -3.00800  1.000 46.47727  ? 80  THR A CB    1 
ATOM   581  O  OG1   . THR A 1 114 ? -44.69600 2.00300   -3.70800  1.000 50.13405  ? 80  THR A OG1   1 
ATOM   582  C  CG2   . THR A 1 114 ? -43.43900 1.78200   -1.66500  1.000 34.66138  ? 80  THR A CG2   1 
ATOM   583  N  N     . GLY A 1 115 ? -42.19900 3.04000   -5.07200  1.000 39.49473  ? 81  GLY A N     1 
ATOM   584  C  CA    . GLY A 1 115 ? -41.55900 4.30100   -5.38100  1.000 50.64148  ? 81  GLY A CA    1 
ATOM   585  C  C     . GLY A 1 115 ? -40.28200 4.20200   -6.18900  1.000 43.40931  ? 81  GLY A C     1 
ATOM   586  O  O     . GLY A 1 115 ? -39.67600 5.24000   -6.48400  1.000 45.51198  ? 81  GLY A O     1 
ATOM   587  N  N     . VAL A 1 116 ? -39.84300 2.99900   -6.54600  1.000 39.42736  ? 82  VAL A N     1 
ATOM   588  C  CA    . VAL A 1 116 ? -38.70600 2.81800   -7.44700  1.000 33.81895  ? 82  VAL A CA    1 
ATOM   589  C  C     . VAL A 1 116 ? -39.30900 2.46800   -8.80100  1.000 45.94049  ? 82  VAL A C     1 
ATOM   590  O  O     . VAL A 1 116 ? -39.52500 1.29900   -9.12800  1.000 42.68795  ? 82  VAL A O     1 
ATOM   591  C  CB    . VAL A 1 116 ? -37.73700 1.75000   -6.94800  1.000 36.69351  ? 82  VAL A CB    1 
ATOM   592  C  CG1   . VAL A 1 116 ? -36.58000 1.59000   -7.93200  1.000 36.25543  ? 82  VAL A CG1   1 
ATOM   593  C  CG2   . VAL A 1 116 ? -37.21100 2.11900   -5.57100  1.000 42.54293  ? 82  VAL A CG2   1 
ATOM   594  N  N     . GLU A 1 117 ? -39.59700 3.50200   -9.60000  1.000 41.16228  ? 83  GLU A N     1 
ATOM   595  C  CA    . GLU A 1 117 ? -40.32900 3.32900   -10.84800 1.000 46.07602  ? 83  GLU A CA    1 
ATOM   596  C  C     . GLU A 1 117 ? -39.62200 3.94800   -12.05100 1.000 50.71979  ? 83  GLU A C     1 
ATOM   597  O  O     . GLU A 1 117 ? -40.22300 4.03600   -13.12800 1.000 43.19347  ? 83  GLU A O     1 
ATOM   598  C  CB    . GLU A 1 117 ? -41.74600 3.90700   -10.71700 1.000 42.77197  ? 83  GLU A CB    1 
ATOM   599  C  CG    . GLU A 1 117 ? -42.54100 3.32800   -9.54700  1.000 44.02274  ? 83  GLU A CG    1 
ATOM   600  C  CD    . GLU A 1 117 ? -44.00600 3.74300   -9.55200  1.000 47.42256  ? 83  GLU A CD    1 
ATOM   601  O  OE1   . GLU A 1 117 ? -44.43800 4.42800   -10.50500 1.000 45.27881  ? 83  GLU A OE1   1 
ATOM   602  O  OE2   . GLU A 1 117 ? -44.73400 3.36900   -8.60600  1.000 46.19235  ? 83  GLU A OE2   1 
ATOM   603  N  N     . ASN A 1 118 ? -38.37100 4.37300   -11.90600 1.000 41.61597  ? 84  ASN A N     1 
ATOM   604  C  CA    . ASN A 1 118 ? -37.62100 4.91900   -13.02800 1.000 44.82941  ? 84  ASN A CA    1 
ATOM   605  C  C     . ASN A 1 118 ? -36.13500 4.75200   -12.74800 1.000 46.09712  ? 84  ASN A C     1 
ATOM   606  O  O     . ASN A 1 118 ? -35.72000 4.49900   -11.61400 1.000 47.67183  ? 84  ASN A O     1 
ATOM   607  C  CB    . ASN A 1 118 ? -37.98800 6.38900   -13.28900 1.000 45.51156  ? 84  ASN A CB    1 
ATOM   608  C  CG    . ASN A 1 118 ? -37.81400 7.26700   -12.06000 1.000 50.49570  ? 84  ASN A CG    1 
ATOM   609  O  OD1   . ASN A 1 118 ? -36.80900 7.18000   -11.35300 1.000 60.05496  ? 84  ASN A OD1   1 
ATOM   610  N  ND2   . ASN A 1 118 ? -38.80400 8.11000   -11.79100 1.000 46.82362  ? 84  ASN A ND2   1 
ATOM   611  N  N     . LEU A 1 119 ? -35.33500 4.91600   -13.80700 1.000 41.73679  ? 85  LEU A N     1 
ATOM   612  C  CA    . LEU A 1 119 ? -33.89200 4.72200   -13.70000 1.000 42.88007  ? 85  LEU A CA    1 
ATOM   613  C  C     . LEU A 1 119 ? -33.25200 5.70200   -12.72800 1.000 39.28389  ? 85  LEU A C     1 
ATOM   614  O  O     . LEU A 1 119 ? -32.20600 5.39600   -12.14400 1.000 51.10424  ? 85  LEU A O     1 
ATOM   615  C  CB    . LEU A 1 119 ? -33.23500 4.85100   -15.07700 1.000 43.14185  ? 85  LEU A CB    1 
ATOM   616  C  CG    . LEU A 1 119 ? -33.28300 3.61700   -15.98000 1.000 53.33867  ? 85  LEU A CG    1 
ATOM   617  C  CD1   . LEU A 1 119 ? -32.51300 3.86100   -17.27900 1.000 38.79109  ? 85  LEU A CD1   1 
ATOM   618  C  CD2   . LEU A 1 119 ? -32.74800 2.39200   -15.24500 1.000 42.26374  ? 85  LEU A CD2   1 
ATOM   619  N  N     . PHE A 1 120 ? -33.85100 6.87900   -12.54300 1.000 42.84614  ? 86  PHE A N     1 
ATOM   620  C  CA    . PHE A 1 120 ? -33.30100 7.83800   -11.59100 1.000 51.27360  ? 86  PHE A CA    1 
ATOM   621  C  C     . PHE A 1 120 ? -33.36100 7.32200   -10.15900 1.000 49.18626  ? 86  PHE A C     1 
ATOM   622  O  O     . PHE A 1 120 ? -32.56900 7.76200   -9.31800  1.000 53.37296  ? 86  PHE A O     1 
ATOM   623  C  CB    . PHE A 1 120 ? -34.04000 9.17300   -11.70000 1.000 52.67293  ? 86  PHE A CB    1 
ATOM   624  N  N     . ALA A 1 121 ? -34.28000 6.40400   -9.86200  1.000 50.77958  ? 87  ALA A N     1 
ATOM   625  C  CA    . ALA A 1 121 ? -34.39200 5.81600   -8.53400  1.000 48.97661  ? 87  ALA A CA    1 
ATOM   626  C  C     . ALA A 1 121 ? -33.50400 4.59200   -8.34700  1.000 53.93568  ? 87  ALA A C     1 
ATOM   627  O  O     . ALA A 1 121 ? -33.40100 4.08300   -7.22600  1.000 47.94259  ? 87  ALA A O     1 
ATOM   628  C  CB    . ALA A 1 121 ? -35.84800 5.43800   -8.25000  1.000 40.58924  ? 87  ALA A CB    1 
ATOM   629  N  N     . ALA A 1 122 ? -32.86900 4.10800   -9.40700  1.000 48.23672  ? 88  ALA A N     1 
ATOM   630  C  CA    . ALA A 1 122 ? -31.97600 2.96600   -9.31700  1.000 46.60910  ? 88  ALA A CA    1 
ATOM   631  C  C     . ALA A 1 122 ? -30.57600 3.42100   -8.93100  1.000 47.20343  ? 88  ALA A C     1 
ATOM   632  O  O     . ALA A 1 122 ? -30.16800 4.55200   -9.20700  1.000 58.32631  ? 88  ALA A O     1 
ATOM   633  C  CB    . ALA A 1 122 ? -31.93200 2.20600   -10.64300 1.000 44.39473  ? 88  ALA A CB    1 
ATOM   634  N  N     . SER A 1 123 ? -29.83700 2.51900   -8.29100  1.000 43.43134  ? 89  SER A N     1 
ATOM   635  C  CA    . SER A 1 123 ? -28.49800 2.82300   -7.80900  1.000 47.34431  ? 89  SER A CA    1 
ATOM   636  C  C     . SER A 1 123 ? -27.49900 1.73000   -8.16000  1.000 43.14616  ? 89  SER A C     1 
ATOM   637  O  O     . SER A 1 123 ? -26.34900 1.79000   -7.71000  1.000 49.73050  ? 89  SER A O     1 
ATOM   638  C  CB    . SER A 1 123 ? -28.51700 3.04800   -6.29300  1.000 46.33178  ? 89  SER A CB    1 
ATOM   639  O  OG    . SER A 1 123 ? -29.14000 1.95300   -5.64100  1.000 57.40003  ? 89  SER A OG    1 
ATOM   640  N  N     . ASP A 1 124 ? -27.90600 0.74200   -8.95000  1.000 44.18287  ? 90  ASP A N     1 
ATOM   641  C  CA    . ASP A 1 124 ? -27.04500 -0.37500  -9.30800  1.000 47.51493  ? 90  ASP A CA    1 
ATOM   642  C  C     . ASP A 1 124 ? -27.60400 -1.01100  -10.56800 1.000 33.58167  ? 90  ASP A C     1 
ATOM   643  O  O     . ASP A 1 124 ? -28.74800 -0.76100  -10.95600 1.000 37.32080  ? 90  ASP A O     1 
ATOM   644  C  CB    . ASP A 1 124 ? -26.95600 -1.39900  -8.17400  1.000 42.10234  ? 90  ASP A CB    1 
ATOM   645  C  CG    . ASP A 1 124 ? -28.31600 -1.72500  -7.58200  1.000 48.27087  ? 90  ASP A CG    1 
ATOM   646  O  OD1   . ASP A 1 124 ? -29.13200 -2.36200  -8.28300  1.000 45.15338  ? 90  ASP A OD1   1 
ATOM   647  O  OD2   . ASP A 1 124 ? -28.56900 -1.34400  -6.41900  1.000 60.40737  ? 90  ASP A OD2   1 
ATOM   648  N  N     . ASN A 1 125 ? -26.78800 -1.86400  -11.19300 1.000 31.78358  ? 91  ASN A N     1 
ATOM   649  C  CA    . ASN A 1 125 ? -27.19500 -2.47800  -12.45300 1.000 45.64251  ? 91  ASN A CA    1 
ATOM   650  C  C     . ASN A 1 125 ? -28.37200 -3.42200  -12.26600 1.000 41.07931  ? 91  ASN A C     1 
ATOM   651  O  O     . ASN A 1 125 ? -29.21000 -3.55200  -13.16700 1.000 38.66610  ? 91  ASN A O     1 
ATOM   652  C  CB    . ASN A 1 125 ? -26.02600 -3.23300  -13.08600 1.000 46.18429  ? 91  ASN A CB    1 
ATOM   653  C  CG    . ASN A 1 125 ? -24.89100 -2.32000  -13.48200 1.000 42.61643  ? 91  ASN A CG    1 
ATOM   654  O  OD1   . ASN A 1 125 ? -25.10000 -1.14700  -13.78100 1.000 41.89052  ? 91  ASN A OD1   1 
ATOM   655  N  ND2   . ASN A 1 125 ? -23.67300 -2.85300  -13.47600 1.000 50.80462  ? 91  ASN A ND2   1 
ATOM   656  N  N     . GLN A 1 126 ? -28.44300 -4.10900  -11.12400 1.000 39.93407  ? 92  GLN A N     1 
ATOM   657  C  CA    . GLN A 1 126 ? -29.54300 -5.04300  -10.91300 1.000 41.23711  ? 92  GLN A CA    1 
ATOM   658  C  C     . GLN A 1 126 ? -30.87800 -4.31400  -10.89800 1.000 35.64176  ? 92  GLN A C     1 
ATOM   659  O  O     . GLN A 1 126 ? -31.84000 -4.75500  -11.53500 1.000 41.82304  ? 92  GLN A O     1 
ATOM   660  C  CB    . GLN A 1 126 ? -29.33500 -5.82700  -9.61600  1.000 46.03973  ? 92  GLN A CB    1 
ATOM   661  C  CG    . GLN A 1 126 ? -29.66600 -7.31100  -9.74200  1.000 54.82687  ? 92  GLN A CG    1 
ATOM   662  C  CD    . GLN A 1 126 ? -30.05200 -7.94600  -8.41100  1.000 74.98420  ? 92  GLN A CD    1 
ATOM   663  O  OE1   . GLN A 1 126 ? -29.49400 -7.61400  -7.36400  1.000 62.60925  ? 92  GLN A OE1   1 
ATOM   664  N  NE2   . GLN A 1 126 ? -31.01500 -8.86400  -8.45000  1.000 64.35274  ? 92  GLN A NE2   1 
ATOM   665  N  N     . THR A 1 127 ? -30.95500 -3.19100  -10.17800 1.000 35.48821  ? 93  THR A N     1 
ATOM   666  C  CA    . THR A 1 127 ? -32.18400 -2.40400  -10.17200 1.000 42.04570  ? 93  THR A CA    1 
ATOM   667  C  C     . THR A 1 127 ? -32.45900 -1.80800  -11.54600 1.000 41.61042  ? 93  THR A C     1 
ATOM   668  O  O     . THR A 1 127 ? -33.59800 -1.84200  -12.02800 1.000 40.38326  ? 93  THR A O     1 
ATOM   669  C  CB    . THR A 1 127 ? -32.10000 -1.29800  -9.12100  1.000 47.29755  ? 93  THR A CB    1 
ATOM   670  O  OG1   . THR A 1 127 ? -31.67700 -1.85400  -7.87200  1.000 41.49694  ? 93  THR A OG1   1 
ATOM   671  C  CG2   . THR A 1 127 ? -33.45600 -0.63100  -8.94400  1.000 41.60264  ? 93  THR A CG2   1 
ATOM   672  N  N     . ALA A 1 128 ? -31.42700 -1.26400  -12.19500 1.000 40.70049  ? 94  ALA A N     1 
ATOM   673  C  CA    . ALA A 1 128 ? -31.61200 -0.68700  -13.52100 1.000 39.49252  ? 94  ALA A CA    1 
ATOM   674  C  C     . ALA A 1 128 ? -32.11800 -1.73200  -14.50700 1.000 42.00522  ? 94  ALA A C     1 
ATOM   675  O  O     . ALA A 1 128 ? -33.00200 -1.45000  -15.32300 1.000 40.41935  ? 94  ALA A O     1 
ATOM   676  C  CB    . ALA A 1 128 ? -30.30400 -0.06600  -14.01000 1.000 40.18102  ? 94  ALA A CB    1 
ATOM   677  N  N     . GLY A 1 129 ? -31.58000 -2.95000  -14.43500 1.000 40.41763  ? 95  GLY A N     1 
ATOM   678  C  CA    . GLY A 1 129 ? -32.07800 -4.01400  -15.28600 1.000 40.60648  ? 95  GLY A CA    1 
ATOM   679  C  C     . GLY A 1 129 ? -33.51200 -4.38800  -14.98300 1.000 43.09164  ? 95  GLY A C     1 
ATOM   680  O  O     . GLY A 1 129 ? -34.25500 -4.79300  -15.88300 1.000 40.15925  ? 95  GLY A O     1 
ATOM   681  N  N     . LYS A 1 130 ? -33.92600 -4.25600  -13.71900 1.000 41.65802  ? 96  LYS A N     1 
ATOM   682  C  CA    . LYS A 1 130 ? -35.30400 -4.57700  -13.36200 1.000 42.53768  ? 96  LYS A CA    1 
ATOM   683  C  C     . LYS A 1 130 ? -36.27200 -3.54800  -13.93200 1.000 34.91933  ? 96  LYS A C     1 
ATOM   684  O  O     . LYS A 1 130 ? -37.36600 -3.90300  -14.38800 1.000 34.97528  ? 96  LYS A O     1 
ATOM   685  C  CB    . LYS A 1 130 ? -35.44500 -4.67200  -11.84100 1.000 36.87673  ? 96  LYS A CB    1 
ATOM   686  C  CG    . LYS A 1 130 ? -34.81300 -5.92300  -11.25400 1.000 37.10419  ? 96  LYS A CG    1 
ATOM   687  C  CD    . LYS A 1 130 ? -35.12900 -6.08200  -9.78000  1.000 40.92150  ? 96  LYS A CD    1 
ATOM   688  C  CE    . LYS A 1 130 ? -34.61500 -7.42200  -9.26000  1.000 41.95833  ? 96  LYS A CE    1 
ATOM   689  N  NZ    . LYS A 1 130 ? -35.09800 -7.67900  -7.88000  1.000 49.80648  ? 96  LYS A NZ    1 
ATOM   690  N  N     . ILE A 1 131 ? -35.88400 -2.27100  -13.91200 1.000 35.02948  ? 97  ILE A N     1 
ATOM   691  C  CA    . ILE A 1 131 ? -36.71600 -1.22500  -14.50300 1.000 38.48077  ? 97  ILE A CA    1 
ATOM   692  C  C     . ILE A 1 131 ? -36.84800 -1.43900  -16.00600 1.000 41.51440  ? 97  ILE A C     1 
ATOM   693  O  O     . ILE A 1 131 ? -37.92000 -1.22800  -16.58600 1.000 37.94309  ? 97  ILE A O     1 
ATOM   694  C  CB    . ILE A 1 131 ? -36.14400 0.16500   -14.16300 1.000 41.13599  ? 97  ILE A CB    1 
ATOM   695  C  CG1   . ILE A 1 131 ? -36.36200 0.47000   -12.67500 1.000 41.84567  ? 97  ILE A CG1   1 
ATOM   696  C  CG2   . ILE A 1 131 ? -36.80600 1.24300   -15.01100 1.000 31.76073  ? 97  ILE A CG2   1 
ATOM   697  C  CD1   . ILE A 1 131 ? -35.25000 1.26000   -12.04500 1.000 49.86983  ? 97  ILE A CD1   1 
ATOM   698  N  N     . HIS A 1 132 ? -35.77200 -1.89100  -16.65800 1.000 38.70205  ? 98  HIS A N     1 
ATOM   699  C  CA    . HIS A 1 132 ? -35.88900 -2.27200  -18.06400 1.000 43.61016  ? 98  HIS A CA    1 
ATOM   700  C  C     . HIS A 1 132 ? -36.85300 -3.44100  -18.23400 1.000 37.59133  ? 98  HIS A C     1 
ATOM   701  O  O     . HIS A 1 132 ? -37.67700 -3.44800  -19.15500 1.000 41.09011  ? 98  HIS A O     1 
ATOM   702  C  CB    . HIS A 1 132 ? -34.51100 -2.61200  -18.64300 1.000 36.14612  ? 98  HIS A CB    1 
ATOM   703  C  CG    . HIS A 1 132 ? -33.70300 -1.40500  -19.01500 1.000 51.94313  ? 98  HIS A CG    1 
ATOM   704  N  ND1   . HIS A 1 132 ? -33.54800 -0.98500  -20.32000 1.000 48.77052  ? 98  HIS A ND1   1 
ATOM   705  C  CD2   . HIS A 1 132 ? -33.00900 -0.52500  -18.25300 1.000 49.08891  ? 98  HIS A CD2   1 
ATOM   706  C  CE1   . HIS A 1 132 ? -32.79700 0.10200   -20.34500 1.000 48.49330  ? 98  HIS A CE1   1 
ATOM   707  N  NE2   . HIS A 1 132 ? -32.45400 0.40000   -19.10500 1.000 56.69164  ? 98  HIS A NE2   1 
ATOM   708  N  N     . MET A 1 133 ? -36.78100 -4.42400  -17.33300 1.000 37.33154  ? 99  MET A N     1 
ATOM   709  C  CA    . MET A 1 133 ? -37.69800 -5.56000  -17.37600 1.000 36.31463  ? 99  MET A CA    1 
ATOM   710  C  C     . MET A 1 133 ? -39.13900 -5.13600  -17.12400 1.000 44.82365  ? 99  MET A C     1 
ATOM   711  O  O     . MET A 1 133 ? -40.07100 -5.81800  -17.56500 1.000 43.13951  ? 99  MET A O     1 
ATOM   712  C  CB    . MET A 1 133 ? -37.27200 -6.60700  -16.34100 1.000 43.65552  ? 99  MET A CB    1 
ATOM   713  C  CG    . MET A 1 133 ? -37.68200 -8.04300  -16.65300 1.000 64.83502  ? 99  MET A CG    1 
ATOM   714  S  SD    . MET A 1 133 ? -37.10300 -8.67000  -18.24100 1.000 78.33605  ? 99  MET A SD    1 
ATOM   715  C  CE    . MET A 1 133 ? -38.52400 -9.62600  -18.76500 1.000 68.72308  ? 99  MET A CE    1 
ATOM   716  N  N     . ALA A 1 134 ? -39.34100 -4.02600  -16.40400 1.000 41.04398  ? 100 ALA A N     1 
ATOM   717  C  CA    . ALA A 1 134 ? -40.69400 -3.54800  -16.13600 1.000 37.70582  ? 100 ALA A CA    1 
ATOM   718  C  C     . ALA A 1 134 ? -41.42500 -3.17800  -17.41900 1.000 38.84112  ? 100 ALA A C     1 
ATOM   719  O  O     . ALA A 1 134 ? -42.65800 -3.25500  -17.47400 1.000 43.92634  ? 100 ALA A O     1 
ATOM   720  C  CB    . ALA A 1 134 ? -40.65100 -2.34800  -15.18900 1.000 33.67788  ? 100 ALA A CB    1 
ATOM   721  N  N     . ALA A 1 135 ? -40.68900 -2.78200  -18.46100 1.000 35.82911  ? 101 ALA A N     1 
ATOM   722  C  CA    . ALA A 1 135 ? -41.33000 -2.44600  -19.72800 1.000 47.74133  ? 101 ALA A CA    1 
ATOM   723  C  C     . ALA A 1 135 ? -42.07500 -3.63800  -20.31200 1.000 44.67721  ? 101 ALA A C     1 
ATOM   724  O  O     . ALA A 1 135 ? -43.09100 -3.46600  -20.99500 1.000 40.66103  ? 101 ALA A O     1 
ATOM   725  C  CB    . ALA A 1 135 ? -40.29000 -1.92700  -20.72300 1.000 37.61115  ? 101 ALA A CB    1 
ATOM   726  N  N     . HIS A 1 136 ? -41.59400 -4.85400  -20.05600 1.000 48.82282  ? 102 HIS A N     1 
ATOM   727  C  CA    . HIS A 1 136 ? -42.31100 -6.02500  -20.54200 1.000 49.84862  ? 102 HIS A CA    1 
ATOM   728  C  C     . HIS A 1 136 ? -43.51400 -6.34900  -19.66800 1.000 54.94649  ? 102 HIS A C     1 
ATOM   729  O  O     . HIS A 1 136 ? -44.54200 -6.81200  -20.17600 1.000 58.07467  ? 102 HIS A O     1 
ATOM   730  C  CB    . HIS A 1 136 ? -41.37600 -7.23100  -20.61700 1.000 63.73361  ? 102 HIS A CB    1 
ATOM   731  C  CG    . HIS A 1 136 ? -42.01300 -8.44600  -21.21500 1.000 84.83717  ? 102 HIS A CG    1 
ATOM   732  N  ND1   . HIS A 1 136 ? -42.11800 -8.63800  -22.57700 1.000 91.73479  ? 102 HIS A ND1   1 
ATOM   733  C  CD2   . HIS A 1 136 ? -42.58800 -9.52800  -20.63700 1.000 81.37274  ? 102 HIS A CD2   1 
ATOM   734  C  CE1   . HIS A 1 136 ? -42.72400 -9.78700  -22.81200 1.000 89.18522  ? 102 HIS A CE1   1 
ATOM   735  N  NE2   . HIS A 1 136 ? -43.01900 -10.34800 -21.65300 1.000 93.04613  ? 102 HIS A NE2   1 
ATOM   736  N  N     . PHE A 1 137 ? -43.41100 -6.10200  -18.35700 1.000 48.34967  ? 103 PHE A N     1 
ATOM   737  C  CA    . PHE A 1 137 ? -44.46300 -6.53600  -17.44400 1.000 45.99310  ? 103 PHE A CA    1 
ATOM   738  C  C     . PHE A 1 137 ? -45.71200 -5.67200  -17.55100 1.000 53.78189  ? 103 PHE A C     1 
ATOM   739  O  O     . PHE A 1 137 ? -46.80900 -6.12900  -17.21400 1.000 53.51904  ? 103 PHE A O     1 
ATOM   740  C  CB    . PHE A 1 137 ? -43.94400 -6.53800  -16.00800 1.000 52.26526  ? 103 PHE A CB    1 
ATOM   741  C  CG    . PHE A 1 137 ? -43.06400 -7.71100  -15.68600 1.000 58.61634  ? 103 PHE A CG    1 
ATOM   742  C  CD1   . PHE A 1 137 ? -43.58000 -8.99500  -15.66700 1.000 67.53158  ? 103 PHE A CD1   1 
ATOM   743  C  CD2   . PHE A 1 137 ? -41.71900 -7.53000  -15.41300 1.000 51.63865  ? 103 PHE A CD2   1 
ATOM   744  C  CE1   . PHE A 1 137 ? -42.77100 -10.07700 -15.37500 1.000 75.40264  ? 103 PHE A CE1   1 
ATOM   745  C  CE2   . PHE A 1 137 ? -40.90600 -8.60800  -15.12500 1.000 57.32383  ? 103 PHE A CE2   1 
ATOM   746  C  CZ    . PHE A 1 137 ? -41.43200 -9.88200  -15.10600 1.000 63.49617  ? 103 PHE A CZ    1 
ATOM   747  N  N     . VAL A 1 138 ? -45.58200 -4.43800  -18.02800 1.000 44.62530  ? 104 VAL A N     1 
ATOM   748  C  CA    . VAL A 1 138 ? -46.72900 -3.53800  -18.08300 1.000 48.12618  ? 104 VAL A CA    1 
ATOM   749  C  C     . VAL A 1 138 ? -47.59100 -3.87600  -19.29100 1.000 48.06554  ? 104 VAL A C     1 
ATOM   750  O  O     . VAL A 1 138 ? -48.65100 -3.27400  -19.49800 1.000 54.05137  ? 104 VAL A O     1 
ATOM   751  C  CB    . VAL A 1 138 ? -46.27700 -2.06900  -18.12300 1.000 50.29481  ? 104 VAL A CB    1 
ATOM   752  C  CG1   . VAL A 1 138 ? -45.74600 -1.64900  -16.75700 1.000 42.44825  ? 104 VAL A CG1   1 
ATOM   753  C  CG2   . VAL A 1 138 ? -45.20800 -1.86300  -19.19300 1.000 40.13793  ? 104 VAL A CG2   1 
ATOM   754  N  N     . LYS A 1 139 ? -47.14700 -4.85200  -20.08600 1.000 47.34737  ? 105 LYS A N     1 
ATOM   755  C  CA    . LYS A 1 139 ? -47.83800 -5.18500  -21.33000 1.000 53.44071  ? 105 LYS A CA    1 
ATOM   756  C  C     . LYS A 1 139 ? -49.29600 -5.56200  -21.08900 1.000 60.56419  ? 105 LYS A C     1 
ATOM   757  O  O     . LYS A 1 139 ? -50.18500 -5.15200  -21.84600 1.000 57.95592  ? 105 LYS A O     1 
ATOM   758  C  CB    . LYS A 1 139 ? -47.11700 -6.33100  -22.03500 1.000 54.65528  ? 105 LYS A CB    1 
ATOM   759  C  CG    . LYS A 1 139 ? -47.71900 -6.70200  -23.38000 1.000 60.46161  ? 105 LYS A CG    1 
ATOM   760  C  CD    . LYS A 1 139 ? -46.93400 -7.80600  -24.05800 1.000 64.04690  ? 105 LYS A CD    1 
ATOM   761  C  CE    . LYS A 1 139 ? -47.85500 -8.93000  -24.49300 1.000 66.55914  ? 105 LYS A CE    1 
ATOM   762  N  NZ    . LYS A 1 139 ? -48.31000 -8.78200  -25.90900 1.000 87.93535  ? 105 LYS A NZ    1 
ATOM   763  N  N     . ALA A 1 140 ? -49.56200 -6.35600  -20.05000 1.000 49.88008  ? 106 ALA A N     1 
ATOM   764  C  CA    . ALA A 1 140 ? -50.92000 -6.83400  -19.80400 1.000 57.69417  ? 106 ALA A CA    1 
ATOM   765  C  C     . ALA A 1 140 ? -51.86300 -5.68400  -19.46600 1.000 59.17611  ? 106 ALA A C     1 
ATOM   766  O  O     . ALA A 1 140 ? -52.94300 -5.56100  -20.05600 1.000 60.57033  ? 106 ALA A O     1 
ATOM   767  C  CB    . ALA A 1 140 ? -50.90900 -7.87500  -18.68300 1.000 62.31726  ? 106 ALA A CB    1 
ATOM   768  N  N     . ASP A 1 141 ? -51.47100 -4.83000  -18.51500 1.000 53.06781  ? 107 ASP A N     1 
ATOM   769  C  CA    . ASP A 1 141 ? -52.32300 -3.70600  -18.13800 1.000 53.90576  ? 107 ASP A CA    1 
ATOM   770  C  C     . ASP A 1 141 ? -52.54300 -2.75400  -19.31000 1.000 55.41081  ? 107 ASP A C     1 
ATOM   771  O  O     . ASP A 1 141 ? -53.63200 -2.18700  -19.46100 1.000 59.55453  ? 107 ASP A O     1 
ATOM   772  C  CB    . ASP A 1 141 ? -51.72000 -2.95900  -16.95000 1.000 46.87451  ? 107 ASP A CB    1 
ATOM   773  C  CG    . ASP A 1 141 ? -51.88000 -3.71300  -15.64300 1.000 65.14489  ? 107 ASP A CG    1 
ATOM   774  O  OD1   . ASP A 1 141 ? -52.42900 -4.83500  -15.66500 1.000 63.08753  ? 107 ASP A OD1   1 
ATOM   775  O  OD2   . ASP A 1 141 ? -51.45800 -3.18300  -14.59200 1.000 62.10049  ? 107 ASP A OD2   1 
ATOM   776  N  N     . ILE A 1 142 ? -51.52500 -2.56900  -20.15200 1.000 49.66411  ? 108 ILE A N     1 
ATOM   777  C  CA    . ILE A 1 142 ? -51.65700 -1.65100  -21.27900 1.000 56.46403  ? 108 ILE A CA    1 
ATOM   778  C  C     . ILE A 1 142 ? -52.50800 -2.26500  -22.38100 1.000 59.17393  ? 108 ILE A C     1 
ATOM   779  O  O     . ILE A 1 142 ? -53.39400 -1.60300  -22.93400 1.000 54.08539  ? 108 ILE A O     1 
ATOM   780  C  CB    . ILE A 1 142 ? -50.26800 -1.23700  -21.79500 1.000 47.87706  ? 108 ILE A CB    1 
ATOM   781  C  CG1   . ILE A 1 142 ? -49.53100 -0.44000  -20.71700 1.000 42.63217  ? 108 ILE A CG1   1 
ATOM   782  C  CG2   . ILE A 1 142 ? -50.39400 -0.42000  -23.07300 1.000 41.59275  ? 108 ILE A CG2   1 
ATOM   783  C  CD1   . ILE A 1 142 ? -48.06900 -0.20600  -21.01800 1.000 39.26080  ? 108 ILE A CD1   1 
ATOM   784  N  N     . GLU A 1 143 ? -52.26200 -3.53400  -22.71600 1.000 56.73131  ? 109 GLU A N     1 
ATOM   785  C  CA    . GLU A 1 143 ? -53.08200 -4.19800  -23.72300 1.000 60.72355  ? 109 GLU A CA    1 
ATOM   786  C  C     . GLU A 1 143 ? -54.54200 -4.24700  -23.29400 1.000 62.37034  ? 109 GLU A C     1 
ATOM   787  O  O     . GLU A 1 143 ? -55.44000 -3.98100  -24.10000 1.000 62.76375  ? 109 GLU A O     1 
ATOM   788  C  CB    . GLU A 1 143 ? -52.55100 -5.60300  -23.99000 1.000 56.14009  ? 109 GLU A CB    1 
ATOM   789  C  CG    . GLU A 1 143 ? -51.48100 -5.64500  -25.05600 1.000 58.78183  ? 109 GLU A CG    1 
ATOM   790  C  CD    . GLU A 1 143 ? -51.14800 -7.05500  -25.49200 1.000 75.72031  ? 109 GLU A CD    1 
ATOM   791  O  OE1   . GLU A 1 143 ? -51.37200 -7.99100  -24.69500 1.000 78.22046  ? 109 GLU A OE1   1 
ATOM   792  O  OE2   . GLU A 1 143 ? -50.66400 -7.22700  -26.63100 1.000 77.03448  ? 109 GLU A OE2   1 
ATOM   793  N  N     . GLU A 1 144 ? -54.79700 -4.57700  -22.02500 1.000 60.98706  ? 110 GLU A N     1 
ATOM   794  C  CA    . GLU A 1 144 ? -56.16400 -4.56500  -21.51600 1.000 64.94978  ? 110 GLU A CA    1 
ATOM   795  C  C     . GLU A 1 144 ? -56.79400 -3.18500  -21.65900 1.000 63.99558  ? 110 GLU A C     1 
ATOM   796  O  O     . GLU A 1 144 ? -57.95700 -3.06400  -22.06200 1.000 68.14317  ? 110 GLU A O     1 
ATOM   797  C  CB    . GLU A 1 144 ? -56.18300 -5.01200  -20.05400 1.000 66.44212  ? 110 GLU A CB    1 
ATOM   798  C  CG    . GLU A 1 144 ? -57.58000 -5.19700  -19.48000 1.000 78.38512  ? 110 GLU A CG    1 
ATOM   799  C  CD    . GLU A 1 144 ? -58.20500 -6.52200  -19.88200 1.000 99.09133  ? 110 GLU A CD    1 
ATOM   800  O  OE1   . GLU A 1 144 ? -57.96200 -7.53000  -19.18200 1.000 98.60949  ? 110 GLU A OE1   1 
ATOM   801  O  OE2   . GLU A 1 144 ? -58.94000 -6.55400  -20.89300 1.000 93.48555  ? 110 GLU A OE2   1 
ATOM   802  N  N     . PHE A 1 145 ? -56.03900 -2.13200  -21.33600 1.000 62.93425  ? 111 PHE A N     1 
ATOM   803  C  CA    . PHE A 1 145 ? -56.56400 -0.77500  -21.44900 1.000 60.88718  ? 111 PHE A CA    1 
ATOM   804  C  C     . PHE A 1 145 ? -56.83200 -0.39000  -22.89700 1.000 62.20582  ? 111 PHE A C     1 
ATOM   805  O  O     . PHE A 1 145 ? -57.75200 0.38900   -23.16600 1.000 65.44427  ? 111 PHE A O     1 
ATOM   806  C  CB    . PHE A 1 145 ? -55.59400 0.21600   -20.80500 1.000 56.93081  ? 111 PHE A CB    1 
ATOM   807  C  CG    . PHE A 1 145 ? -55.94300 1.65800   -21.05000 1.000 62.43172  ? 111 PHE A CG    1 
ATOM   808  C  CD1   . PHE A 1 145 ? -57.03900 2.23500   -20.42800 1.000 63.83599  ? 111 PHE A CD1   1 
ATOM   809  C  CD2   . PHE A 1 145 ? -55.16700 2.44300   -21.88800 1.000 57.01391  ? 111 PHE A CD2   1 
ATOM   810  C  CE1   . PHE A 1 145 ? -57.36000 3.56700   -20.64300 1.000 63.54591  ? 111 PHE A CE1   1 
ATOM   811  C  CE2   . PHE A 1 145 ? -55.48100 3.77300   -22.10500 1.000 57.86941  ? 111 PHE A CE2   1 
ATOM   812  C  CZ    . PHE A 1 145 ? -56.57900 4.33600   -21.48300 1.000 57.04173  ? 111 PHE A CZ    1 
ATOM   813  N  N     . MET A 1 146 ? -56.05600 -0.92600  -23.83700 1.000 58.82078  ? 112 MET A N     1 
ATOM   814  C  CA    . MET A 1 146 ? -56.24000 -0.59400  -25.24500 1.000 65.46791  ? 112 MET A CA    1 
ATOM   815  C  C     . MET A 1 146 ? -57.26300 -1.47600  -25.94300 1.000 64.51598  ? 112 MET A C     1 
ATOM   816  O  O     . MET A 1 146 ? -57.86700 -1.04200  -26.92900 1.000 59.82386  ? 112 MET A O     1 
ATOM   817  C  CB    . MET A 1 146 ? -54.90600 -0.67000  -25.99000 1.000 53.68464  ? 112 MET A CB    1 
ATOM   818  C  CG    . MET A 1 146 ? -54.21100 0.67100   -26.10500 1.000 62.77851  ? 112 MET A CG    1 
ATOM   819  S  SD    . MET A 1 146 ? -52.42700 0.51900   -26.18100 1.000 56.29567  ? 112 MET A SD    1 
ATOM   820  C  CE    . MET A 1 146 ? -52.21600 -0.07300  -27.85300 1.000 61.29758  ? 112 MET A CE    1 
ATOM   821  N  N     . LYS A 1 147 ? -57.47100 -2.70500  -25.47100 1.000 63.12641  ? 113 LYS A N     1 
ATOM   822  C  CA    . LYS A 1 147 ? -58.58100 -3.48900  -26.00000 1.000 65.30294  ? 113 LYS A CA    1 
ATOM   823  C  C     . LYS A 1 147 ? -59.92000 -2.92400  -25.55000 1.000 65.35288  ? 113 LYS A C     1 
ATOM   824  O  O     . LYS A 1 147 ? -60.90700 -3.01400  -26.28800 1.000 69.52544  ? 113 LYS A O     1 
ATOM   825  C  CB    . LYS A 1 147 ? -58.45200 -4.95600  -25.58700 1.000 74.11509  ? 113 LYS A CB    1 
ATOM   826  C  CG    . LYS A 1 147 ? -57.19600 -5.64200  -26.10700 1.000 83.79881  ? 113 LYS A CG    1 
ATOM   827  C  CD    . LYS A 1 147 ? -57.09200 -7.07200  -25.59200 1.000 88.25611  ? 113 LYS A CD    1 
ATOM   828  C  CE    . LYS A 1 147 ? -56.42100 -7.11800  -24.22600 1.000 79.54675  ? 113 LYS A CE    1 
ATOM   829  N  NZ    . LYS A 1 147 ? -55.90500 -8.47400  -23.89900 1.000 73.66549  ? 113 LYS A NZ    1 
ATOM   830  N  N     . GLU A 1 148 ? -59.96900 -2.32500  -24.35900 1.000 64.62778  ? 114 GLU A N     1 
ATOM   831  C  CA    . GLU A 1 148 ? -61.21100 -1.73800  -23.86500 1.000 69.60791  ? 114 GLU A CA    1 
ATOM   832  C  C     . GLU A 1 148 ? -61.46000 -0.35500  -24.45400 1.000 70.82303  ? 114 GLU A C     1 
ATOM   833  O  O     . GLU A 1 148 ? -62.59800 -0.02700  -24.80600 1.000 71.81184  ? 114 GLU A O     1 
ATOM   834  C  CB    . GLU A 1 148 ? -61.18700 -1.65500  -22.34000 1.000 67.75356  ? 114 GLU A CB    1 
ATOM   835  C  CG    . GLU A 1 148 ? -61.51500 -2.95400  -21.63900 1.000 86.85318  ? 114 GLU A CG    1 
ATOM   836  C  CD    . GLU A 1 148 ? -61.49900 -2.80600  -20.13300 1.000 99.34342  ? 114 GLU A CD    1 
ATOM   837  O  OE1   . GLU A 1 148 ? -61.99300 -1.77000  -19.63600 1.000 101.19651 ? 114 GLU A OE1   1 
ATOM   838  O  OE2   . GLU A 1 148 ? -60.99300 -3.72000  -19.44800 1.000 100.36915 ? 114 GLU A OE2   1 
ATOM   839  N  N     . ASN A 1 149 ? -60.41600 0.47300   -24.55100 1.000 64.40501  ? 115 ASN A N     1 
ATOM   840  C  CA    . ASN A 1 149 ? -60.51100 1.82800   -25.09200 1.000 66.11083  ? 115 ASN A CA    1 
ATOM   841  C  C     . ASN A 1 149 ? -59.51900 1.96100   -26.24400 1.000 62.71121  ? 115 ASN A C     1 
ATOM   842  O  O     . ASN A 1 149 ? -58.46400 2.59600   -26.09600 1.000 55.62952  ? 115 ASN A O     1 
ATOM   843  C  CB    . ASN A 1 149 ? -60.24200 2.87700   -24.01600 1.000 62.18361  ? 115 ASN A CB    1 
ATOM   844  C  CG    . ASN A 1 149 ? -61.01600 2.61300   -22.74200 1.000 70.62366  ? 115 ASN A CG    1 
ATOM   845  O  OD1   . ASN A 1 149 ? -60.49600 2.01500   -21.80000 1.000 71.26817  ? 115 ASN A OD1   1 
ATOM   846  N  ND2   . ASN A 1 149 ? -62.26300 3.06500   -22.70400 1.000 75.27156  ? 115 ASN A ND2   1 
ATOM   847  N  N     . PRO A 1 150 ? -59.82700 1.38500   -27.40200 1.000 62.34110  ? 116 PRO A N     1 
ATOM   848  C  CA    . PRO A 1 150 ? -58.88800 1.42200   -28.52400 1.000 54.06658  ? 116 PRO A CA    1 
ATOM   849  C  C     . PRO A 1 150 ? -58.69200 2.84400   -29.02300 1.000 57.41489  ? 116 PRO A C     1 
ATOM   850  O  O     . PRO A 1 150 ? -59.66700 3.57200   -29.25200 1.000 59.38353  ? 116 PRO A O     1 
ATOM   851  C  CB    . PRO A 1 150 ? -59.56700 0.54500   -29.58600 1.000 61.25109  ? 116 PRO A CB    1 
ATOM   852  C  CG    . PRO A 1 150 ? -61.01400 0.58000   -29.23600 1.000 59.92351  ? 116 PRO A CG    1 
ATOM   853  C  CD    . PRO A 1 150 ? -61.07100 0.67300   -27.74100 1.000 59.91010  ? 116 PRO A CD    1 
ATOM   854  N  N     . PRO A 1 151 ? -57.44400 3.27400   -29.18700 1.000 53.49930  ? 117 PRO A N     1 
ATOM   855  C  CA    . PRO A 1 151 ? -57.19700 4.61400   -29.72600 1.000 53.76066  ? 117 PRO A CA    1 
ATOM   856  C  C     . PRO A 1 151 ? -57.06400 4.58800   -31.23600 1.000 49.22300  ? 117 PRO A C     1 
ATOM   857  O  O     . PRO A 1 151 ? -57.12700 3.52200   -31.85600 1.000 48.58919  ? 117 PRO A O     1 
ATOM   858  C  CB    . PRO A 1 151 ? -55.87900 5.01000   -29.05500 1.000 52.75749  ? 117 PRO A CB    1 
ATOM   859  C  CG    . PRO A 1 151 ? -55.14400 3.71100   -28.97600 1.000 45.87029  ? 117 PRO A CG    1 
ATOM   860  C  CD    . PRO A 1 151 ? -56.19200 2.62400   -28.76200 1.000 55.86724  ? 117 PRO A CD    1 
ATOM   861  N  N     . ASP A 1 152 ? -56.86500 5.75800   -31.84000 1.000 48.06873  ? 118 ASP A N     1 
ATOM   862  C  CA    . ASP A 1 152 ? -56.61500 5.79900   -33.27500 1.000 54.32569  ? 118 ASP A CA    1 
ATOM   863  C  C     . ASP A 1 152 ? -55.15300 5.49900   -33.59000 1.000 47.75350  ? 118 ASP A C     1 
ATOM   864  O  O     . ASP A 1 152 ? -54.86000 4.77700   -34.54800 1.000 50.58927  ? 118 ASP A O     1 
ATOM   865  C  CB    . ASP A 1 152 ? -57.02900 7.16000   -33.83800 1.000 48.16644  ? 118 ASP A CB    1 
ATOM   866  C  CG    . ASP A 1 152 ? -58.52200 7.41000   -33.70900 1.000 53.83855  ? 118 ASP A CG    1 
ATOM   867  O  OD1   . ASP A 1 152 ? -59.30500 6.57200   -34.20300 1.000 53.76772  ? 118 ASP A OD1   1 
ATOM   868  O  OD2   . ASP A 1 152 ? -58.91100 8.42700   -33.09200 1.000 53.03995  ? 118 ASP A OD2   1 
ATOM   869  N  N     . VAL A 1 153 ? -54.22600 6.03500   -32.79200 1.000 50.39142  ? 119 VAL A N     1 
ATOM   870  C  CA    . VAL A 1 153 ? -52.79500 5.86400   -33.01200 1.000 49.05273  ? 119 VAL A CA    1 
ATOM   871  C  C     . VAL A 1 153 ? -52.12800 5.49100   -31.69300 1.000 47.96594  ? 119 VAL A C     1 
ATOM   872  O  O     . VAL A 1 153 ? -52.55500 5.91800   -30.61500 1.000 38.04667  ? 119 VAL A O     1 
ATOM   873  C  CB    . VAL A 1 153 ? -52.15100 7.13800   -33.61100 1.000 43.86855  ? 119 VAL A CB    1 
ATOM   874  C  CG1   . VAL A 1 153 ? -50.69000 6.89800   -33.96000 1.000 43.34363  ? 119 VAL A CG1   1 
ATOM   875  C  CG2   . VAL A 1 153 ? -52.91800 7.59600   -34.85100 1.000 44.89835  ? 119 VAL A CG2   1 
ATOM   876  N  N     . PHE A 1 154 ? -51.07100 4.68500   -31.78600 1.000 39.74138  ? 120 PHE A N     1 
ATOM   877  C  CA    . PHE A 1 154 ? -50.28000 4.27400   -30.63300 1.000 44.84773  ? 120 PHE A CA    1 
ATOM   878  C  C     . PHE A 1 154 ? -48.82500 4.66400   -30.86000 1.000 36.59257  ? 120 PHE A C     1 
ATOM   879  O  O     . PHE A 1 154 ? -48.18600 4.17000   -31.79100 1.000 38.35422  ? 120 PHE A O     1 
ATOM   880  C  CB    . PHE A 1 154 ? -50.40600 2.76800   -30.39800 1.000 43.38410  ? 120 PHE A CB    1 
ATOM   881  C  CG    . PHE A 1 154 ? -49.67000 2.28000   -29.18600 1.000 45.03097  ? 120 PHE A CG    1 
ATOM   882  C  CD1   . PHE A 1 154 ? -49.73600 2.98400   -27.99600 1.000 51.14494  ? 120 PHE A CD1   1 
ATOM   883  C  CD2   . PHE A 1 154 ? -48.94100 1.10500   -29.22600 1.000 52.96654  ? 120 PHE A CD2   1 
ATOM   884  C  CE1   . PHE A 1 154 ? -49.06600 2.53900   -26.87000 1.000 50.96182  ? 120 PHE A CE1   1 
ATOM   885  C  CE2   . PHE A 1 154 ? -48.27100 0.65100   -28.10300 1.000 56.05132  ? 120 PHE A CE2   1 
ATOM   886  C  CZ    . PHE A 1 154 ? -48.33300 1.37200   -26.92400 1.000 54.95147  ? 120 PHE A CZ    1 
ATOM   887  N  N     . ILE A 1 155 ? -48.30000 5.53100   -30.00100 1.000 39.92092  ? 121 ILE A N     1 
ATOM   888  C  CA    . ILE A 1 155 ? -46.90700 5.96000   -30.06000 1.000 35.60854  ? 121 ILE A CA    1 
ATOM   889  C  C     . ILE A 1 155 ? -46.19700 5.40200   -28.83400 1.000 39.72852  ? 121 ILE A C     1 
ATOM   890  O  O     . ILE A 1 155 ? -46.60200 5.67200   -27.69700 1.000 39.04893  ? 121 ILE A O     1 
ATOM   891  C  CB    . ILE A 1 155 ? -46.79600 7.49100   -30.12900 1.000 35.66684  ? 121 ILE A CB    1 
ATOM   892  C  CG1   . ILE A 1 155 ? -47.32700 7.99600   -31.47900 1.000 33.63749  ? 121 ILE A CG1   1 
ATOM   893  C  CG2   . ILE A 1 155 ? -45.36100 7.94000   -29.88300 1.000 29.16133  ? 121 ILE A CG2   1 
ATOM   894  C  CD1   . ILE A 1 155 ? -47.52300 9.50300   -31.54300 1.000 33.86177  ? 121 ILE A CD1   1 
ATOM   895  N  N     . SER A 1 156 ? -45.14200 4.61900   -29.05600 1.000 33.63085  ? 122 SER A N     1 
ATOM   896  C  CA    . SER A 1 156 ? -44.45600 3.94100   -27.96800 1.000 33.76807  ? 122 SER A CA    1 
ATOM   897  C  C     . SER A 1 156 ? -42.94900 4.10700   -28.08700 1.000 35.96307  ? 122 SER A C     1 
ATOM   898  O  O     . SER A 1 156 ? -42.38500 4.11500   -29.18500 1.000 34.29725  ? 122 SER A O     1 
ATOM   899  C  CB    . SER A 1 156 ? -44.79300 2.44800   -27.93200 1.000 41.70783  ? 122 SER A CB    1 
ATOM   900  O  OG    . SER A 1 156 ? -44.30700 1.80000   -29.08900 1.000 45.58753  ? 122 SER A OG    1 
ATOM   901  N  N     . ASP A 1 157 ? -42.30500 4.22400   -26.93000 1.000 31.56627  ? 123 ASP A N     1 
ATOM   902  C  CA    . ASP A 1 157 ? -40.85300 4.26600   -26.86500 1.000 31.89401  ? 123 ASP A CA    1 
ATOM   903  C  C     . ASP A 1 157 ? -40.25000 3.01300   -27.49200 1.000 38.11648  ? 123 ASP A C     1 
ATOM   904  O  O     . ASP A 1 157 ? -40.83000 1.92400   -27.43400 1.000 35.59621  ? 123 ASP A O     1 
ATOM   905  C  CB    . ASP A 1 157 ? -40.40300 4.39400   -25.40800 1.000 31.05156  ? 123 ASP A CB    1 
ATOM   906  C  CG    . ASP A 1 157 ? -38.90800 4.57700   -25.27200 1.000 35.36359  ? 123 ASP A CG    1 
ATOM   907  O  OD1   . ASP A 1 157 ? -38.17400 3.57000   -25.35900 1.000 36.89633  ? 123 ASP A OD1   1 
ATOM   908  O  OD2   . ASP A 1 157 ? -38.46900 5.73100   -25.08100 1.000 34.82593  ? 123 ASP A OD2   1 
ATOM   909  N  N     . ILE A 1 158 ? -39.06300 3.18300   -28.09000 1.000 41.71762  ? 124 ILE A N     1 
ATOM   910  C  CA    . ILE A 1 158 ? -38.33400 2.08800   -28.73900 1.000 44.38135  ? 124 ILE A CA    1 
ATOM   911  C  C     . ILE A 1 158 ? -38.28600 0.84400   -27.86700 1.000 44.83452  ? 124 ILE A C     1 
ATOM   912  O  O     . ILE A 1 158 ? -38.28500 -0.28400  -28.37600 1.000 44.60695  ? 124 ILE A O     1 
ATOM   913  C  CB    . ILE A 1 158 ? -36.89900 2.53700   -29.10100 1.000 53.00811  ? 124 ILE A CB    1 
ATOM   914  C  CG1   . ILE A 1 158 ? -36.34300 3.50100   -28.05000 1.000 50.47430  ? 124 ILE A CG1   1 
ATOM   915  C  CG2   . ILE A 1 158 ? -36.83900 3.17300   -30.46500 1.000 56.63328  ? 124 ILE A CG2   1 
ATOM   916  C  CD1   . ILE A 1 158 ? -34.84200 3.67700   -28.13700 1.000 65.61500  ? 124 ILE A CD1   1 
ATOM   917  N  N     . ILE A 1 159 ? -38.24400 1.02100   -26.54500 1.000 43.39615  ? 125 ILE A N     1 
ATOM   918  C  CA    . ILE A 1 159 ? -37.94800 -0.09800  -25.65600 1.000 40.51163  ? 125 ILE A CA    1 
ATOM   919  C  C     . ILE A 1 159 ? -39.09500 -1.10100  -25.63400 1.000 41.32853  ? 125 ILE A C     1 
ATOM   920  O  O     . ILE A 1 159 ? -38.86900 -2.31700  -25.59700 1.000 42.64853  ? 125 ILE A O     1 
ATOM   921  C  CB    . ILE A 1 159 ? -37.60500 0.43200   -24.25200 1.000 42.57614  ? 125 ILE A CB    1 
ATOM   922  C  CG1   . ILE A 1 159 ? -36.21000 1.06000   -24.28600 1.000 40.15360  ? 125 ILE A CG1   1 
ATOM   923  C  CG2   . ILE A 1 159 ? -37.67800 -0.68200  -23.21000 1.000 39.36152  ? 125 ILE A CG2   1 
ATOM   924  C  CD1   . ILE A 1 159 ? -35.80700 1.74500   -23.02300 1.000 51.21631  ? 125 ILE A CD1   1 
ATOM   925  N  N     . PHE A 1 160 ? -40.34000 -0.62100  -25.67300 1.000 42.23911  ? 126 PHE A N     1 
ATOM   926  C  CA    . PHE A 1 160 ? -41.50800 -1.50200  -25.61600 1.000 43.44756  ? 126 PHE A CA    1 
ATOM   927  C  C     . PHE A 1 160 ? -41.60500 -2.29400  -26.92000 1.000 55.98439  ? 126 PHE A C     1 
ATOM   928  O  O     . PHE A 1 160 ? -42.38000 -1.97700  -27.82600 1.000 49.58236  ? 126 PHE A O     1 
ATOM   929  C  CB    . PHE A 1 160 ? -42.77800 -0.69600  -25.36300 1.000 42.90468  ? 126 PHE A CB    1 
ATOM   930  C  CG    . PHE A 1 160 ? -42.75800 0.09300   -24.08500 1.000 42.98936  ? 126 PHE A CG    1 
ATOM   931  C  CD1   . PHE A 1 160 ? -43.13000 -0.49800  -22.88500 1.000 45.34676  ? 126 PHE A CD1   1 
ATOM   932  C  CD2   . PHE A 1 160 ? -42.37100 1.42500   -24.08200 1.000 36.09808  ? 126 PHE A CD2   1 
ATOM   933  C  CE1   . PHE A 1 160 ? -43.11700 0.22300   -21.71100 1.000 39.20961  ? 126 PHE A CE1   1 
ATOM   934  C  CE2   . PHE A 1 160 ? -42.35200 2.15200   -22.91100 1.000 35.97016  ? 126 PHE A CE2   1 
ATOM   935  C  CZ    . PHE A 1 160 ? -42.72500 1.55400   -21.72100 1.000 43.51813  ? 126 PHE A CZ    1 
ATOM   936  N  N     . THR A 1 161 ? -40.80900 -3.36700  -27.00400 1.000 55.66576  ? 127 THR A N     1 
ATOM   937  C  CA    . THR A 1 161 ? -40.75200 -4.15800  -28.23300 1.000 51.86046  ? 127 THR A CA    1 
ATOM   938  C  C     . THR A 1 161 ? -42.05900 -4.88800  -28.50900 1.000 52.61273  ? 127 THR A C     1 
ATOM   939  O  O     . THR A 1 161 ? -42.35300 -5.21100  -29.66500 1.000 67.20446  ? 127 THR A O     1 
ATOM   940  C  CB    . THR A 1 161 ? -39.60700 -5.16900  -28.17000 1.000 49.62326  ? 127 THR A CB    1 
ATOM   941  O  OG1   . THR A 1 161 ? -39.84500 -6.09400  -27.10100 1.000 67.87941  ? 127 THR A OG1   1 
ATOM   942  C  CG2   . THR A 1 161 ? -38.27800 -4.46100  -27.94900 1.000 55.04704  ? 127 THR A CG2   1 
ATOM   943  N  N     . TRP A 1 162 ? -42.85300 -5.15800  -27.47400 1.000 54.63660  ? 128 TRP A N     1 
ATOM   944  C  CA    . TRP A 1 162 ? -44.12500 -5.84000  -27.66900 1.000 53.99441  ? 128 TRP A CA    1 
ATOM   945  C  C     . TRP A 1 162 ? -45.17600 -4.95700  -28.32700 1.000 54.03427  ? 128 TRP A C     1 
ATOM   946  O  O     . TRP A 1 162 ? -46.23600 -5.46900  -28.70100 1.000 57.66254  ? 128 TRP A O     1 
ATOM   947  C  CB    . TRP A 1 162 ? -44.65500 -6.35300  -26.32800 1.000 52.36085  ? 128 TRP A CB    1 
ATOM   948  C  CG    . TRP A 1 162 ? -44.67700 -5.31200  -25.24700 1.000 60.08908  ? 128 TRP A CG    1 
ATOM   949  C  CD1   . TRP A 1 162 ? -43.75100 -5.13900  -24.26000 1.000 51.87346  ? 128 TRP A CD1   1 
ATOM   950  C  CD2   . TRP A 1 162 ? -45.68200 -4.30800  -25.03400 1.000 58.47841  ? 128 TRP A CD2   1 
ATOM   951  N  NE1   . TRP A 1 162 ? -44.11100 -4.08500  -23.45300 1.000 47.37671  ? 128 TRP A NE1   1 
ATOM   952  C  CE2   . TRP A 1 162 ? -45.29300 -3.56100  -23.90400 1.000 51.00274  ? 128 TRP A CE2   1 
ATOM   953  C  CE3   . TRP A 1 162 ? -46.87000 -3.96900  -25.69000 1.000 55.60644  ? 128 TRP A CE3   1 
ATOM   954  C  CZ2   . TRP A 1 162 ? -46.04800 -2.49400  -23.41800 1.000 46.93557  ? 128 TRP A CZ2   1 
ATOM   955  C  CZ3   . TRP A 1 162 ? -47.61900 -2.91100  -25.20400 1.000 54.58069  ? 128 TRP A CZ3   1 
ATOM   956  C  CH2   . TRP A 1 162 ? -47.20500 -2.18700  -24.08000 1.000 51.83854  ? 128 TRP A CH2   1 
ATOM   957  N  N     . SER A 1 163 ? -44.91600 -3.65300  -28.46900 1.000 50.77257  ? 129 SER A N     1 
ATOM   958  C  CA    . SER A 1 163 ? -45.92700 -2.74800  -29.00600 1.000 46.55974  ? 129 SER A CA    1 
ATOM   959  C  C     . SER A 1 163 ? -46.26000 -3.07300  -30.45600 1.000 54.29226  ? 129 SER A C     1 
ATOM   960  O  O     . SER A 1 163 ? -47.38600 -2.82300  -30.90200 1.000 49.13777  ? 129 SER A O     1 
ATOM   961  C  CB    . SER A 1 163 ? -45.45900 -1.29500  -28.88300 1.000 51.17204  ? 129 SER A CB    1 
ATOM   962  O  OG    . SER A 1 163 ? -44.32500 -1.04700  -29.70400 1.000 55.81987  ? 129 SER A OG    1 
ATOM   963  N  N     . GLU A 1 164 ? -45.30000 -3.62500  -31.20200 1.000 41.68582  ? 130 GLU A N     1 
ATOM   964  C  CA    . GLU A 1 164 ? -45.55200 -3.99000  -32.59100 1.000 51.54897  ? 130 GLU A CA    1 
ATOM   965  C  C     . GLU A 1 164 ? -46.63600 -5.05800  -32.68300 1.000 60.42040  ? 130 GLU A C     1 
ATOM   966  O  O     . GLU A 1 164 ? -47.61700 -4.90500  -33.42100 1.000 52.90086  ? 130 GLU A O     1 
ATOM   967  C  CB    . GLU A 1 164 ? -44.25200 -4.46400  -33.24100 1.000 54.62812  ? 130 GLU A CB    1 
ATOM   968  C  CG    . GLU A 1 164 ? -44.41800 -5.08600  -34.61800 1.000 60.61045  ? 130 GLU A CG    1 
ATOM   969  C  CD    . GLU A 1 164 ? -43.11700 -5.11300  -35.40000 1.000 70.23497  ? 130 GLU A CD    1 
ATOM   970  O  OE1   . GLU A 1 164 ? -42.04200 -5.11000  -34.76200 1.000 80.08228  ? 130 GLU A OE1   1 
ATOM   971  O  OE2   . GLU A 1 164 ? -43.16800 -5.13400  -36.64900 1.000 80.66059  ? 130 GLU A OE2   1 
ATOM   972  N  N     . SER A 1 165 ? -46.48400 -6.14600  -31.92100 1.000 60.67224  ? 131 SER A N     1 
ATOM   973  C  CA    . SER A 1 165 ? -47.49800 -7.19500  -31.92600 1.000 54.22844  ? 131 SER A CA    1 
ATOM   974  C  C     . SER A 1 165 ? -48.81600 -6.70900  -31.33600 1.000 58.91458  ? 131 SER A C     1 
ATOM   975  O  O     . SER A 1 165 ? -49.88600 -7.16100  -31.75900 1.000 64.17177  ? 131 SER A O     1 
ATOM   976  C  CB    . SER A 1 165 ? -46.98700 -8.42200  -31.16600 1.000 62.33044  ? 131 SER A CB    1 
ATOM   977  O  OG    . SER A 1 165 ? -46.61700 -8.08900  -29.83700 1.000 72.02684  ? 131 SER A OG    1 
ATOM   978  N  N     . THR A 1 166 ? -48.76300 -5.78700  -30.37100 1.000 60.23535  ? 132 THR A N     1 
ATOM   979  C  CA    . THR A 1 166 ? -49.99000 -5.24200  -29.79500 1.000 60.42917  ? 132 THR A CA    1 
ATOM   980  C  C     . THR A 1 166 ? -50.75700 -4.41100  -30.81600 1.000 59.93616  ? 132 THR A C     1 
ATOM   981  O  O     . THR A 1 166 ? -51.99200 -4.47100  -30.87400 1.000 65.96939  ? 132 THR A O     1 
ATOM   982  C  CB    . THR A 1 166 ? -49.65900 -4.40500  -28.55700 1.000 54.96278  ? 132 THR A CB    1 
ATOM   983  O  OG1   . THR A 1 166 ? -49.11200 -5.25100  -27.53800 1.000 62.56001  ? 132 THR A OG1   1 
ATOM   984  C  CG2   . THR A 1 166 ? -50.90100 -3.71000  -28.02100 1.000 53.15791  ? 132 THR A CG2   1 
ATOM   985  N  N     . ALA A 1 167 ? -50.04400 -3.63300  -31.63300 1.000 58.16098  ? 133 ALA A N     1 
ATOM   986  C  CA    . ALA A 1 167 ? -50.70800 -2.81400  -32.63900 1.000 58.52459  ? 133 ALA A CA    1 
ATOM   987  C  C     . ALA A 1 167 ? -51.28900 -3.66000  -33.76600 1.000 59.74073  ? 133 ALA A C     1 
ATOM   988  O  O     . ALA A 1 167 ? -52.34400 -3.31700  -34.31200 1.000 64.12230  ? 133 ALA A O     1 
ATOM   989  C  CB    . ALA A 1 167 ? -49.73200 -1.78100  -33.19900 1.000 54.97552  ? 133 ALA A CB    1 
ATOM   990  N  N     . LYS A 1 168 ? -50.61800 -4.75500  -34.13200 1.000 55.33637  ? 134 LYS A N     1 
ATOM   991  C  CA    . LYS A 1 168 ? -51.14300 -5.62700  -35.17800 1.000 62.50236  ? 134 LYS A CA    1 
ATOM   992  C  C     . LYS A 1 168 ? -52.42600 -6.31300  -34.72400 1.000 68.12819  ? 134 LYS A C     1 
ATOM   993  O  O     . LYS A 1 168 ? -53.44300 -6.27700  -35.42700 1.000 64.23920  ? 134 LYS A O     1 
ATOM   994  C  CB    . LYS A 1 168 ? -50.09300 -6.66400  -35.58000 1.000 67.39415  ? 134 LYS A CB    1 
ATOM   995  C  CG    . LYS A 1 168 ? -50.60100 -7.70500  -36.56800 1.000 74.62577  ? 134 LYS A CG    1 
ATOM   996  C  CD    . LYS A 1 168 ? -49.57600 -8.80900  -36.79300 1.000 88.79512  ? 134 LYS A CD    1 
ATOM   997  C  CE    . LYS A 1 168 ? -50.10000 -9.87100  -37.75100 1.000 90.20367  ? 134 LYS A CE    1 
ATOM   998  N  NZ    . LYS A 1 168 ? -49.11300 -10.96700 -37.96000 1.000 94.35794  ? 134 LYS A NZ    1 
ATOM   999  N  N     . ASN A 1 169 ? -52.39900 -6.93100  -33.53900 1.000 73.50038  ? 135 ASN A N     1 
ATOM   1000 C  CA    . ASN A 1 169 ? -53.56200 -7.65000  -33.03100 1.000 76.92397  ? 135 ASN A CA    1 
ATOM   1001 C  C     . ASN A 1 169 ? -54.74400 -6.73000  -32.75900 1.000 74.14467  ? 135 ASN A C     1 
ATOM   1002 O  O     . ASN A 1 169 ? -55.88300 -7.20500  -32.71200 1.000 88.05290  ? 135 ASN A O     1 
ATOM   1003 C  CB    . ASN A 1 169 ? -53.19600 -8.41300  -31.75700 1.000 78.64102  ? 135 ASN A CB    1 
ATOM   1004 C  CG    . ASN A 1 169 ? -52.10700 -9.44600  -31.98700 1.000 95.32034  ? 135 ASN A CG    1 
ATOM   1005 O  OD1   . ASN A 1 169 ? -51.89100 -9.90100  -33.11100 1.000 101.91507 ? 135 ASN A OD1   1 
ATOM   1006 N  ND2   . ASN A 1 169 ? -51.41700 -9.82400  -30.91800 1.000 96.63483  ? 135 ASN A ND2   1 
ATOM   1007 N  N     . LEU A 1 170 ? -54.50300 -5.43600  -32.57600 1.000 68.48814  ? 136 LEU A N     1 
ATOM   1008 C  CA    . LEU A 1 170 ? -55.56900 -4.46000  -32.41200 1.000 63.09468  ? 136 LEU A CA    1 
ATOM   1009 C  C     . LEU A 1 170 ? -55.83300 -3.66100  -33.67800 1.000 67.62220  ? 136 LEU A C     1 
ATOM   1010 O  O     . LEU A 1 170 ? -56.70500 -2.78500  -33.66600 1.000 69.58218  ? 136 LEU A O     1 
ATOM   1011 C  CB    . LEU A 1 170 ? -55.24100 -3.50800  -31.26000 1.000 74.49003  ? 136 LEU A CB    1 
ATOM   1012 C  CG    . LEU A 1 170 ? -55.82500 -3.86800  -29.89500 1.000 80.71915  ? 136 LEU A CG    1 
ATOM   1013 C  CD1   . LEU A 1 170 ? -54.91100 -4.83400  -29.15200 1.000 68.22023  ? 136 LEU A CD1   1 
ATOM   1014 C  CD2   . LEU A 1 170 ? -56.05400 -2.60800  -29.08100 1.000 73.83779  ? 136 LEU A CD2   1 
ATOM   1015 N  N     . GLN A 1 171 ? -55.10300 -3.94000  -34.75800 1.000 66.37171  ? 137 GLN A N     1 
ATOM   1016 C  CA    . GLN A 1 171 ? -55.26300 -3.27000  -36.04900 1.000 65.71760  ? 137 GLN A CA    1 
ATOM   1017 C  C     . GLN A 1 171 ? -55.27300 -1.75000  -35.88400 1.000 63.20026  ? 137 GLN A C     1 
ATOM   1018 O  O     . GLN A 1 171 ? -56.22900 -1.05600  -36.23200 1.000 64.89346  ? 137 GLN A O     1 
ATOM   1019 C  CB    . GLN A 1 171 ? -56.52300 -3.76200  -36.76600 1.000 68.39634  ? 137 GLN A CB    1 
ATOM   1020 C  CG    . GLN A 1 171 ? -56.35300 -5.11600  -37.43600 1.000 72.31171  ? 137 GLN A CG    1 
ATOM   1021 C  CD    . GLN A 1 171 ? -57.58600 -5.55000  -38.20600 1.000 84.96277  ? 137 GLN A CD    1 
ATOM   1022 O  OE1   . GLN A 1 171 ? -58.69300 -5.07200  -37.95300 1.000 78.74876  ? 137 GLN A OE1   1 
ATOM   1023 N  NE2   . GLN A 1 171 ? -57.39800 -6.45800  -39.15800 1.000 88.47282  ? 137 GLN A NE2   1 
ATOM   1024 N  N     . ILE A 1 172 ? -54.17400 -1.24400  -35.33700 1.000 74.22395  ? 138 ILE A N     1 
ATOM   1025 C  CA    . ILE A 1 172 ? -54.02100 0.17900   -35.05000 1.000 76.32054  ? 138 ILE A CA    1 
ATOM   1026 C  C     . ILE A 1 172 ? -52.62500 0.62200   -35.47500 1.000 69.73296  ? 138 ILE A C     1 
ATOM   1027 O  O     . ILE A 1 172 ? -51.64200 -0.07400  -35.18000 1.000 62.43531  ? 138 ILE A O     1 
ATOM   1028 C  CB    . ILE A 1 172 ? -54.27500 0.46800   -33.56300 1.000 68.29563  ? 138 ILE A CB    1 
ATOM   1029 C  CG1   . ILE A 1 172 ? -54.26000 1.97000   -33.29500 1.000 73.96496  ? 138 ILE A CG1   1 
ATOM   1030 C  CG2   . ILE A 1 172 ? -53.24700 -0.23600  -32.69800 1.000 62.01934  ? 138 ILE A CG2   1 
ATOM   1031 C  CD1   . ILE A 1 172 ? -54.79900 2.33000   -31.95200 1.000 72.04586  ? 138 ILE A CD1   1 
ATOM   1032 N  N     . PRO A 1 173 ? -52.48800 1.75100   -36.17200 1.000 59.85667  ? 139 PRO A N     1 
ATOM   1033 C  CA    . PRO A 1 173 ? -51.15100 2.21500   -36.56100 1.000 48.09263  ? 139 PRO A CA    1 
ATOM   1034 C  C     . PRO A 1 173 ? -50.29000 2.52200   -35.34400 1.000 51.04003  ? 139 PRO A C     1 
ATOM   1035 O  O     . PRO A 1 173 ? -50.75400 3.08800   -34.35300 1.000 43.23236  ? 139 PRO A O     1 
ATOM   1036 C  CB    . PRO A 1 173 ? -51.43800 3.47600   -37.38600 1.000 53.82540  ? 139 PRO A CB    1 
ATOM   1037 C  CG    . PRO A 1 173 ? -52.80400 3.91400   -36.96300 1.000 56.04755  ? 139 PRO A CG    1 
ATOM   1038 C  CD    . PRO A 1 173 ? -53.54900 2.64800   -36.66100 1.000 65.80672  ? 139 PRO A CD    1 
ATOM   1039 N  N     . ARG A 1 174 ? -49.02100 2.13300   -35.42700 1.000 42.56026  ? 140 ARG A N     1 
ATOM   1040 C  CA    . ARG A 1 174 ? -48.06700 2.36700   -34.35600 1.000 50.06387  ? 140 ARG A CA    1 
ATOM   1041 C  C     . ARG A 1 174 ? -46.83800 3.05800   -34.91700 1.000 47.79124  ? 140 ARG A C     1 
ATOM   1042 O  O     . ARG A 1 174 ? -46.30000 2.63900   -35.94600 1.000 45.06505  ? 140 ARG A O     1 
ATOM   1043 C  CB    . ARG A 1 174 ? -47.66100 1.06000   -33.67300 1.000 42.16338  ? 140 ARG A CB    1 
ATOM   1044 C  CG    . ARG A 1 174 ? -46.58700 1.21500   -32.62000 1.000 46.67648  ? 140 ARG A CG    1 
ATOM   1045 C  CD    . ARG A 1 174 ? -45.93800 -0.12200  -32.34500 1.000 54.55520  ? 140 ARG A CD    1 
ATOM   1046 N  NE    . ARG A 1 174 ? -45.18500 -0.59300  -33.50000 1.000 59.17793  ? 140 ARG A NE    1 
ATOM   1047 C  CZ    . ARG A 1 174 ? -43.88700 -0.86400  -33.48700 1.000 60.44237  ? 140 ARG A CZ    1 
ATOM   1048 N  NH1   . ARG A 1 174 ? -43.17000 -0.76200  -32.37800 1.000 52.75825  ? 140 ARG A NH1   1 
ATOM   1049 N  NH2   . ARG A 1 174 ? -43.29800 -1.26800  -34.60900 1.000 51.64609  ? 140 ARG A NH2   1 
ATOM   1050 N  N     . LEU A 1 175 ? -46.40200 4.11100   -34.23900 1.000 44.29951  ? 141 LEU A N     1 
ATOM   1051 C  CA    . LEU A 1 175 ? -45.14500 4.77500   -34.53500 1.000 38.92845  ? 141 LEU A CA    1 
ATOM   1052 C  C     . LEU A 1 175 ? -44.22700 4.64700   -33.33100 1.000 39.39738  ? 141 LEU A C     1 
ATOM   1053 O  O     . LEU A 1 175 ? -44.67200 4.73700   -32.18300 1.000 39.07405  ? 141 LEU A O     1 
ATOM   1054 C  CB    . LEU A 1 175 ? -45.35500 6.25200   -34.88400 1.000 43.74416  ? 141 LEU A CB    1 
ATOM   1055 C  CG    . LEU A 1 175 ? -45.83900 6.55100   -36.30700 1.000 39.32014  ? 141 LEU A CG    1 
ATOM   1056 C  CD1   . LEU A 1 175 ? -47.34900 6.40300   -36.40400 1.000 38.47343  ? 141 LEU A CD1   1 
ATOM   1057 C  CD2   . LEU A 1 175 ? -45.40500 7.94300   -36.72500 1.000 35.91076  ? 141 LEU A CD2   1 
ATOM   1058 N  N     . VAL A 1 176 ? -42.96100 4.43100   -33.60500 1.000 35.15384  ? 142 VAL A N     1 
ATOM   1059 C  CA    . VAL A 1 176 ? -41.92800 4.30500   -32.58900 1.000 38.60687  ? 142 VAL A CA    1 
ATOM   1060 C  C     . VAL A 1 176 ? -41.39300 5.69700   -32.26100 1.000 34.14602  ? 142 VAL A C     1 
ATOM   1061 O  O     . VAL A 1 176 ? -41.25700 6.54400   -33.15200 1.000 31.35185  ? 142 VAL A O     1 
ATOM   1062 C  CB    . VAL A 1 176 ? -40.81900 3.36400   -33.09700 1.000 45.86110  ? 142 VAL A CB    1 
ATOM   1063 C  CG1   . VAL A 1 176 ? -39.50500 3.68800   -32.46300 1.000 48.56398  ? 142 VAL A CG1   1 
ATOM   1064 C  CG2   . VAL A 1 176 ? -41.19800 1.90600   -32.85500 1.000 46.24880  ? 142 VAL A CG2   1 
ATOM   1065 N  N     . PHE A 1 177 ? -41.10900 5.95900   -30.98400 1.000 31.79299  ? 143 PHE A N     1 
ATOM   1066 C  CA    . PHE A 1 177 ? -40.54500 7.24000   -30.57200 1.000 28.55362  ? 143 PHE A CA    1 
ATOM   1067 C  C     . PHE A 1 177 ? -39.09200 7.05500   -30.14900 1.000 32.28606  ? 143 PHE A C     1 
ATOM   1068 O  O     . PHE A 1 177 ? -38.80000 6.28800   -29.22400 1.000 30.73687  ? 143 PHE A O     1 
ATOM   1069 C  CB    . PHE A 1 177 ? -41.35900 7.86900   -29.44500 1.000 24.30046  ? 143 PHE A CB    1 
ATOM   1070 C  CG    . PHE A 1 177 ? -40.75800 9.13600   -28.90000 1.000 34.48264  ? 143 PHE A CG    1 
ATOM   1071 C  CD1   . PHE A 1 177 ? -40.72700 10.29100  -29.66900 1.000 29.85250  ? 143 PHE A CD1   1 
ATOM   1072 C  CD2   . PHE A 1 177 ? -40.21400 9.16800   -27.62100 1.000 31.33068  ? 143 PHE A CD2   1 
ATOM   1073 C  CE1   . PHE A 1 177 ? -40.17700 11.45800  -29.17300 1.000 38.18067  ? 143 PHE A CE1   1 
ATOM   1074 C  CE2   . PHE A 1 177 ? -39.65700 10.33100  -27.11700 1.000 36.86715  ? 143 PHE A CE2   1 
ATOM   1075 C  CZ    . PHE A 1 177 ? -39.63700 11.48100  -27.89500 1.000 32.97522  ? 143 PHE A CZ    1 
ATOM   1076 N  N     . ASN A 1 178 ? -38.18900 7.76600   -30.82800 1.000 31.03317  ? 144 ASN A N     1 
ATOM   1077 C  CA    . ASN A 1 178 ? -36.76700 7.74600   -30.51400 1.000 25.35909  ? 144 ASN A CA    1 
ATOM   1078 C  C     . ASN A 1 178 ? -36.41900 9.04100   -29.80100 1.000 35.53164  ? 144 ASN A C     1 
ATOM   1079 O  O     . ASN A 1 178 ? -36.47300 10.11100  -30.42700 1.000 34.14604  ? 144 ASN A O     1 
ATOM   1080 C  CB    . ASN A 1 178 ? -35.93500 7.59400   -31.78800 1.000 32.27001  ? 144 ASN A CB    1 
ATOM   1081 C  CG    . ASN A 1 178 ? -34.43800 7.46900   -31.51500 1.000 36.01409  ? 144 ASN A CG    1 
ATOM   1082 O  OD1   . ASN A 1 178 ? -34.00000 7.39700   -30.36800 1.000 37.84063  ? 144 ASN A OD1   1 
ATOM   1083 N  ND2   . ASN A 1 178 ? -33.64900 7.42600   -32.58400 1.000 39.44086  ? 144 ASN A ND2   1 
ATOM   1084 N  N     . PRO A 1 179 ? -36.05300 9.00900   -28.51800 1.000 27.32896  ? 145 PRO A N     1 
ATOM   1085 C  CA    . PRO A 1 179 ? -35.90700 10.25300  -27.75400 1.000 24.69786  ? 145 PRO A CA    1 
ATOM   1086 C  C     . PRO A 1 179 ? -34.59900 10.99500  -27.98600 1.000 27.86825  ? 145 PRO A C     1 
ATOM   1087 O  O     . PRO A 1 179 ? -34.37300 12.02000  -27.33000 1.000 28.04505  ? 145 PRO A O     1 
ATOM   1088 C  CB    . PRO A 1 179 ? -36.01200 9.76800   -26.30000 1.000 30.62335  ? 145 PRO A CB    1 
ATOM   1089 C  CG    . PRO A 1 179 ? -35.45600 8.37600   -26.34000 1.000 30.35775  ? 145 PRO A CG    1 
ATOM   1090 C  CD    . PRO A 1 179 ? -35.85400 7.81000   -27.68200 1.000 28.46236  ? 145 PRO A CD    1 
ATOM   1091 N  N     . ILE A 1 180 ? -33.73700 10.52400  -28.88900 1.000 25.50087  ? 146 ILE A N     1 
ATOM   1092 C  CA    . ILE A 1 180 ? -32.47700 11.18000  -29.20500 1.000 25.73397  ? 146 ILE A CA    1 
ATOM   1093 C  C     . ILE A 1 180 ? -32.32400 11.26600  -30.72400 1.000 32.34073  ? 146 ILE A C     1 
ATOM   1094 O  O     . ILE A 1 180 ? -33.20500 10.86700  -31.48500 1.000 26.72895  ? 146 ILE A O     1 
ATOM   1095 C  CB    . ILE A 1 180 ? -31.26500 10.46200  -28.57300 1.000 25.68264  ? 146 ILE A CB    1 
ATOM   1096 C  CG1   . ILE A 1 180 ? -31.11600 9.05500   -29.14200 1.000 30.55459  ? 146 ILE A CG1   1 
ATOM   1097 C  CG2   . ILE A 1 180 ? -31.39600 10.40400  -27.05000 1.000 26.43670  ? 146 ILE A CG2   1 
ATOM   1098 C  CD1   . ILE A 1 180 ? -29.84100 8.35700   -28.68600 1.000 36.63445  ? 146 ILE A CD1   1 
ATOM   1099 N  N     . SER A 1 181 ? -31.18200 11.79800  -31.15400 1.000 26.54298  ? 147 SER A N     1 
ATOM   1100 C  CA    . SER A 1 181 ? -30.88100 11.93200  -32.57300 1.000 26.95899  ? 147 SER A CA    1 
ATOM   1101 C  C     . SER A 1 181 ? -30.78200 10.56700  -33.24300 1.000 30.55152  ? 147 SER A C     1 
ATOM   1102 O  O     . SER A 1 181 ? -30.40500 9.57200   -32.62000 1.000 30.48235  ? 147 SER A O     1 
ATOM   1103 C  CB    . SER A 1 181 ? -29.56900 12.69900  -32.75500 1.000 28.01014  ? 147 SER A CB    1 
ATOM   1104 O  OG    . SER A 1 181 ? -29.08300 12.59900  -34.07600 1.000 35.72688  ? 147 SER A OG    1 
ATOM   1105 N  N     . ILE A 1 182 ? -31.12200 10.52600  -34.53500 1.000 26.75296  ? 148 ILE A N     1 
ATOM   1106 C  CA    . ILE A 1 182 ? -30.98300 9.30200   -35.31900 1.000 27.04766  ? 148 ILE A CA    1 
ATOM   1107 C  C     . ILE A 1 182 ? -29.52900 8.97200   -35.62100 1.000 25.62254  ? 148 ILE A C     1 
ATOM   1108 O  O     . ILE A 1 182 ? -29.22800 7.84000   -36.02200 1.000 26.81564  ? 148 ILE A O     1 
ATOM   1109 C  CB    . ILE A 1 182 ? -31.79700 9.40500   -36.62900 1.000 26.67386  ? 148 ILE A CB    1 
ATOM   1110 C  CG1   . ILE A 1 182 ? -32.15200 8.01400   -37.15800 1.000 32.07637  ? 148 ILE A CG1   1 
ATOM   1111 C  CG2   . ILE A 1 182 ? -31.03900 10.22400  -37.69300 1.000 22.20157  ? 148 ILE A CG2   1 
ATOM   1112 C  CD1   . ILE A 1 182 ? -33.06100 7.21300   -36.24300 1.000 29.07039  ? 148 ILE A CD1   1 
ATOM   1113 N  N     . PHE A 1 183 ? -28.60300 9.89900   -35.40500 1.000 26.20467  ? 149 PHE A N     1 
ATOM   1114 C  CA    . PHE A 1 183 ? -27.15700 9.64900   -35.64800 1.000 29.99079  ? 149 PHE A CA    1 
ATOM   1115 C  C     . PHE A 1 183 ? -26.64500 8.45200   -34.84400 1.000 26.91177  ? 149 PHE A C     1 
ATOM   1116 O  O     . PHE A 1 183 ? -25.86500 7.67600   -35.38200 1.000 29.43137  ? 149 PHE A O     1 
ATOM   1117 C  CB    . PHE A 1 183 ? -26.33300 10.87400  -35.25200 1.000 25.76417  ? 149 PHE A CB    1 
ATOM   1118 C  CG    . PHE A 1 183 ? -24.83800 10.65500  -35.08800 1.000 28.69879  ? 149 PHE A CG    1 
ATOM   1119 C  CD1   . PHE A 1 183 ? -23.99700 10.66800  -36.19100 1.000 24.61731  ? 149 PHE A CD1   1 
ATOM   1120 C  CD2   . PHE A 1 183 ? -24.27700 10.44700  -33.83600 1.000 21.64068  ? 149 PHE A CD2   1 
ATOM   1121 C  CE1   . PHE A 1 183 ? -22.63800 10.46700  -36.04600 1.000 25.85269  ? 149 PHE A CE1   1 
ATOM   1122 C  CE2   . PHE A 1 183 ? -22.91700 10.24100  -33.70000 1.000 24.61192  ? 149 PHE A CE2   1 
ATOM   1123 C  CZ    . PHE A 1 183 ? -22.10200 10.25900  -34.80100 1.000 30.36676  ? 149 PHE A CZ    1 
ATOM   1124 N  N     . ASP A 1 184 ? -27.06100 8.32600   -33.59100 1.000 22.82432  ? 150 ASP A N     1 
ATOM   1125 C  CA    . ASP A 1 184 ? -26.51800 7.26800   -32.69700 1.000 29.35873  ? 150 ASP A CA    1 
ATOM   1126 C  C     . ASP A 1 184 ? -26.70700 5.86800   -33.29300 1.000 25.27370  ? 150 ASP A C     1 
ATOM   1127 O  O     . ASP A 1 184 ? -25.72500 5.13000   -33.36400 1.000 30.25706  ? 150 ASP A O     1 
ATOM   1128 C  CB    . ASP A 1 184 ? -27.10000 7.40800   -31.30300 1.000 26.02660  ? 150 ASP A CB    1 
ATOM   1129 C  CG    . ASP A 1 184 ? -26.79800 8.70700   -30.57400 1.000 38.25582  ? 150 ASP A CG    1 
ATOM   1130 O  OD1   . ASP A 1 184 ? -26.94000 9.77500   -31.19400 1.000 31.07343  ? 150 ASP A OD1   1 
ATOM   1131 O  OD2   . ASP A 1 184 ? -26.43100 8.62800   -29.38900 1.000 28.74234  ? 150 ASP A OD2   1 
ATOM   1132 N  N     . VAL A 1 185 ? -27.93200 5.53600   -33.68300 1.000 25.40451  ? 151 VAL A N     1 
ATOM   1133 C  CA    . VAL A 1 185 ? -28.22400 4.20300   -34.28000 1.000 27.44011  ? 151 VAL A CA    1 
ATOM   1134 C  C     . VAL A 1 185 ? -27.38900 4.04600   -35.56200 1.000 32.46477  ? 151 VAL A C     1 
ATOM   1135 O  O     . VAL A 1 185 ? -26.91900 2.93400   -35.82100 1.000 26.01308  ? 151 VAL A O     1 
ATOM   1136 C  CB    . VAL A 1 185 ? -29.72600 3.96700   -34.52800 1.000 31.18081  ? 151 VAL A CB    1 
ATOM   1137 C  CG1   . VAL A 1 185 ? -30.28400 4.77600   -35.68800 1.000 24.29447  ? 151 VAL A CG1   1 
ATOM   1138 C  CG2   . VAL A 1 185 ? -30.04800 2.48900   -34.68800 1.000 41.41230  ? 151 VAL A CG2   1 
ATOM   1139 N  N     . CYS A 1 186 ? -27.17800 5.14400   -36.28700 1.000 24.20727  ? 152 CYS A N     1 
ATOM   1140 C  CA    . CYS A 1 186 ? -26.36700 5.04200   -37.49800 1.000 27.85296  ? 152 CYS A CA    1 
ATOM   1141 C  C     . CYS A 1 186 ? -24.92400 4.71000   -37.15500 1.000 29.27252  ? 152 CYS A C     1 
ATOM   1142 O  O     . CYS A 1 186 ? -24.30600 3.84400   -37.78500 1.000 28.84880  ? 152 CYS A O     1 
ATOM   1143 C  CB    . CYS A 1 186 ? -26.42900 6.34400   -38.30400 1.000 33.15739  ? 152 CYS A CB    1 
ATOM   1144 S  SG    . CYS A 1 186 ? -28.06800 6.79000   -38.92600 1.000 30.57042  ? 152 CYS A SG    1 
ATOM   1145 N  N     . MET A 1 187 ? -24.36400 5.41200   -36.17100 1.000 23.96252  ? 153 MET A N     1 
ATOM   1146 C  CA    . MET A 1 187 ? -23.00500 5.11600   -35.73300 1.000 30.21538  ? 153 MET A CA    1 
ATOM   1147 C  C     . MET A 1 187 ? -22.89100 3.67900   -35.24600 1.000 31.01562  ? 153 MET A C     1 
ATOM   1148 O  O     . MET A 1 187 ? -21.92900 2.97600   -35.57600 1.000 26.99688  ? 153 MET A O     1 
ATOM   1149 C  CB    . MET A 1 187 ? -22.59700 6.08600   -34.62600 1.000 28.32777  ? 153 MET A CB    1 
ATOM   1150 C  CG    . MET A 1 187 ? -21.13400 6.01600   -34.26600 1.000 30.53490  ? 153 MET A CG    1 
ATOM   1151 S  SD    . MET A 1 187 ? -20.63400 7.36800   -33.19100 1.000 31.91074  ? 153 MET A SD    1 
ATOM   1152 C  CE    . MET A 1 187 ? -19.21500 6.61200   -32.40200 1.000 35.13817  ? 153 MET A CE    1 
ATOM   1153 N  N     . ILE A 1 188 ? -23.87200 3.23100   -34.45600 1.000 28.41263  ? 154 ILE A N     1 
ATOM   1154 C  CA    . ILE A 1 188 ? -23.89700 1.85200   -33.97100 1.000 31.86252  ? 154 ILE A CA    1 
ATOM   1155 C  C     . ILE A 1 188 ? -23.90900 0.87800   -35.14200 1.000 30.71317  ? 154 ILE A C     1 
ATOM   1156 O  O     . ILE A 1 188 ? -23.11600 -0.07100  -35.19700 1.000 31.28973  ? 154 ILE A O     1 
ATOM   1157 C  CB    . ILE A 1 188 ? -25.11600 1.63700   -33.05600 1.000 28.92082  ? 154 ILE A CB    1 
ATOM   1158 C  CG1   . ILE A 1 188 ? -24.90700 2.32900   -31.70700 1.000 29.57574  ? 154 ILE A CG1   1 
ATOM   1159 C  CG2   . ILE A 1 188 ? -25.40300 0.15300   -32.89300 1.000 28.31136  ? 154 ILE A CG2   1 
ATOM   1160 C  CD1   . ILE A 1 188 ? -26.09100 2.20000   -30.75900 1.000 25.75976  ? 154 ILE A CD1   1 
ATOM   1161 N  N     . GLN A 1 189 ? -24.81300 1.10000   -36.09700 1.000 31.82750  ? 155 GLN A N     1 
ATOM   1162 C  CA    . GLN A 1 189 ? -24.90300 0.19800   -37.23900 1.000 33.34955  ? 155 GLN A CA    1 
ATOM   1163 C  C     . GLN A 1 189 ? -23.61200 0.19200   -38.05000 1.000 27.72329  ? 155 GLN A C     1 
ATOM   1164 O  O     . GLN A 1 189 ? -23.17900 -0.86300  -38.52600 1.000 33.35008  ? 155 GLN A O     1 
ATOM   1165 C  CB    . GLN A 1 189 ? -26.09200 0.57800   -38.12100 1.000 35.90198  ? 155 GLN A CB    1 
ATOM   1166 C  CG    . GLN A 1 189 ? -26.40300 -0.45800  -39.18500 1.000 34.95695  ? 155 GLN A CG    1 
ATOM   1167 C  CD    . GLN A 1 189 ? -25.64600 -0.19200  -40.46800 1.000 39.82438  ? 155 GLN A CD    1 
ATOM   1168 O  OE1   . GLN A 1 189 ? -25.13700 0.91100   -40.67800 1.000 42.55987  ? 155 GLN A OE1   1 
ATOM   1169 N  NE2   . GLN A 1 189 ? -25.55100 -1.20300  -41.32600 1.000 39.42432  ? 155 GLN A NE2   1 
ATOM   1170 N  N     . ALA A 1 190 ? -22.97700 1.35600   -38.21700 1.000 27.39287  ? 156 ALA A N     1 
ATOM   1171 C  CA    . ALA A 1 190 ? -21.72200 1.39300   -38.96500 1.000 33.11565  ? 156 ALA A CA    1 
ATOM   1172 C  C     . ALA A 1 190 ? -20.62800 0.61500   -38.24200 1.000 36.65114  ? 156 ALA A C     1 
ATOM   1173 O  O     . ALA A 1 190 ? -19.80800 -0.05400  -38.88300 1.000 34.62516  ? 156 ALA A O     1 
ATOM   1174 C  CB    . ALA A 1 190 ? -21.28600 2.83800   -39.20700 1.000 26.52626  ? 156 ALA A CB    1 
ATOM   1175 N  N     . ILE A 1 191 ? -20.60200 0.68700   -36.90900 1.000 33.50618  ? 157 ILE A N     1 
ATOM   1176 C  CA    . ILE A 1 191 ? -19.65000 -0.11000  -36.13600 1.000 34.40149  ? 157 ILE A CA    1 
ATOM   1177 C  C     . ILE A 1 191 ? -19.94400 -1.59400  -36.31400 1.000 32.44455  ? 157 ILE A C     1 
ATOM   1178 O  O     . ILE A 1 191 ? -19.04600 -2.39700  -36.59200 1.000 36.08147  ? 157 ILE A O     1 
ATOM   1179 C  CB    . ILE A 1 191 ? -19.69600 0.29000   -34.64900 1.000 31.53847  ? 157 ILE A CB    1 
ATOM   1180 C  CG1   . ILE A 1 191 ? -19.16800 1.71100   -34.44600 1.000 26.36930  ? 157 ILE A CG1   1 
ATOM   1181 C  CG2   . ILE A 1 191 ? -18.91900 -0.71000  -33.80300 1.000 35.09433  ? 157 ILE A CG2   1 
ATOM   1182 C  CD1   . ILE A 1 191 ? -19.47900 2.27900   -33.06600 1.000 27.66476  ? 157 ILE A CD1   1 
ATOM   1183 N  N     . GLN A 1 192 ? -21.21500 -1.97400  -36.15200 1.000 33.38930  ? 158 GLN A N     1 
ATOM   1184 C  CA    . GLN A 1 192 ? -21.60100 -3.37700  -36.25800 1.000 35.99699  ? 158 GLN A CA    1 
ATOM   1185 C  C     . GLN A 1 192 ? -21.25700 -3.94500  -37.62400 1.000 38.16707  ? 158 GLN A C     1 
ATOM   1186 O  O     . GLN A 1 192 ? -20.83000 -5.10000  -37.73200 1.000 46.28201  ? 158 GLN A O     1 
ATOM   1187 C  CB    . GLN A 1 192 ? -23.09700 -3.53400  -35.99000 1.000 36.34173  ? 158 GLN A CB    1 
ATOM   1188 C  CG    . GLN A 1 192 ? -23.47800 -3.39000  -34.53600 1.000 39.75336  ? 158 GLN A CG    1 
ATOM   1189 C  CD    . GLN A 1 192 ? -24.64500 -4.27700  -34.15600 1.000 56.92449  ? 158 GLN A CD    1 
ATOM   1190 O  OE1   . GLN A 1 192 ? -25.78000 -4.05300  -34.58500 1.000 50.49581  ? 158 GLN A OE1   1 
ATOM   1191 N  NE2   . GLN A 1 192 ? -24.36900 -5.30100  -33.34900 1.000 48.79880  ? 158 GLN A NE2   1 
ATOM   1192 N  N     . SER A 1 193 ? -21.43100 -3.14800  -38.68100 1.000 37.05437  ? 159 SER A N     1 
ATOM   1193 C  CA    . SER A 1 193 ? -21.23400 -3.63600  -40.03800 1.000 39.22167  ? 159 SER A CA    1 
ATOM   1194 C  C     . SER A 1 193 ? -19.77800 -3.59700  -40.48600 1.000 43.47465  ? 159 SER A C     1 
ATOM   1195 O  O     . SER A 1 193 ? -19.49400 -3.98700  -41.62300 1.000 42.10987  ? 159 SER A O     1 
ATOM   1196 C  CB    . SER A 1 193 ? -22.10000 -2.83500  -41.01700 1.000 37.71905  ? 159 SER A CB    1 
ATOM   1197 O  OG    . SER A 1 193 ? -21.81400 -1.44800  -40.95100 1.000 42.20157  ? 159 SER A OG    1 
ATOM   1198 N  N     . HIS A 1 194 ? -18.85200 -3.15000  -39.63800 1.000 42.32337  ? 160 HIS A N     1 
ATOM   1199 C  CA    . HIS A 1 194 ? -17.42500 -3.12400  -39.97200 1.000 38.99312  ? 160 HIS A CA    1 
ATOM   1200 C  C     . HIS A 1 194 ? -16.59800 -3.75000  -38.85800 1.000 42.60835  ? 160 HIS A C     1 
ATOM   1201 O  O     . HIS A 1 194 ? -15.73600 -3.09400  -38.26600 1.000 49.71002  ? 160 HIS A O     1 
ATOM   1202 C  CB    . HIS A 1 194 ? -16.95700 -1.69600  -40.24400 1.000 42.53236  ? 160 HIS A CB    1 
ATOM   1203 C  CG    . HIS A 1 194 ? -17.61200 -1.06200  -41.42800 1.000 47.92462  ? 160 HIS A CG    1 
ATOM   1204 N  ND1   . HIS A 1 194 ? -18.82100 -0.40600  -41.34600 1.000 47.65388  ? 160 HIS A ND1   1 
ATOM   1205 C  CD2   . HIS A 1 194 ? -17.22200 -0.97500  -42.72200 1.000 42.40847  ? 160 HIS A CD2   1 
ATOM   1206 C  CE1   . HIS A 1 194 ? -19.15000 0.05500   -42.53900 1.000 44.24788  ? 160 HIS A CE1   1 
ATOM   1207 N  NE2   . HIS A 1 194 ? -18.19800 -0.27700  -43.39200 1.000 49.22206  ? 160 HIS A NE2   1 
ATOM   1208 N  N     . PRO A 1 195 ? -16.81300 -5.03500  -38.56000 1.000 44.80341  ? 161 PRO A N     1 
ATOM   1209 C  CA    . PRO A 1 195 ? -16.03400 -5.66600  -37.48300 1.000 53.13560  ? 161 PRO A CA    1 
ATOM   1210 C  C     . PRO A 1 195 ? -14.54600 -5.72300  -37.77500 1.000 50.25435  ? 161 PRO A C     1 
ATOM   1211 O  O     . PRO A 1 195 ? -13.74400 -5.80400  -36.83600 1.000 55.60589  ? 161 PRO A O     1 
ATOM   1212 C  CB    . PRO A 1 195 ? -16.64700 -7.06900  -37.38600 1.000 54.25964  ? 161 PRO A CB    1 
ATOM   1213 C  CG    . PRO A 1 195 ? -17.16000 -7.33800  -38.75200 1.000 47.28855  ? 161 PRO A CG    1 
ATOM   1214 C  CD    . PRO A 1 195 ? -17.65500 -6.01500  -39.27000 1.000 53.00328  ? 161 PRO A CD    1 
ATOM   1215 N  N     . GLU A 1 196 ? -14.14900 -5.66800  -39.04700 1.000 46.52547  ? 162 GLU A N     1 
ATOM   1216 C  CA    . GLU A 1 196 ? -12.73200 -5.67900  -39.38500 1.000 51.38990  ? 162 GLU A CA    1 
ATOM   1217 C  C     . GLU A 1 196 ? -12.02300 -4.40500  -38.94300 1.000 55.23033  ? 162 GLU A C     1 
ATOM   1218 O  O     . GLU A 1 196 ? -10.79100 -4.39700  -38.85300 1.000 59.78791  ? 162 GLU A O     1 
ATOM   1219 C  CB    . GLU A 1 196 ? -12.55400 -5.89200  -40.89500 1.000 50.86041  ? 162 GLU A CB    1 
ATOM   1220 C  CG    . GLU A 1 196 ? -13.06400 -4.75100  -41.77400 1.000 57.84538  ? 162 GLU A CG    1 
ATOM   1221 C  CD    . GLU A 1 196 ? -14.56700 -4.80200  -42.01200 1.000 58.25359  ? 162 GLU A CD    1 
ATOM   1222 O  OE1   . GLU A 1 196 ? -15.22500 -5.74700  -41.52900 1.000 54.62189  ? 162 GLU A OE1   1 
ATOM   1223 O  OE2   . GLU A 1 196 ? -15.09000 -3.89600  -42.69300 1.000 60.29877  ? 162 GLU A OE2   1 
ATOM   1224 N  N     . SER A 1 197 ? -12.76900 -3.33400  -38.65600 1.000 48.28478  ? 163 SER A N     1 
ATOM   1225 C  CA    . SER A 1 197 ? -12.16700 -2.08100  -38.21500 1.000 56.22110  ? 163 SER A CA    1 
ATOM   1226 C  C     . SER A 1 197 ? -11.82400 -2.06700  -36.73100 1.000 51.07519  ? 163 SER A C     1 
ATOM   1227 O  O     . SER A 1 197 ? -11.12600 -1.14700  -36.28700 1.000 50.20647  ? 163 SER A O     1 
ATOM   1228 C  CB    . SER A 1 197 ? -13.10200 -0.90900  -38.52500 1.000 45.44476  ? 163 SER A CB    1 
ATOM   1229 O  OG    . SER A 1 197 ? -13.50900 -0.93500  -39.88200 1.000 52.71599  ? 163 SER A OG    1 
ATOM   1230 N  N     . PHE A 1 198 ? -12.28300 -3.05500  -35.96100 1.000 48.71936  ? 164 PHE A N     1 
ATOM   1231 C  CA    . PHE A 1 198 ? -12.12200 -3.06800  -34.51100 1.000 51.94631  ? 164 PHE A CA    1 
ATOM   1232 C  C     . PHE A 1 198 ? -11.43600 -4.34000  -34.02200 1.000 60.93739  ? 164 PHE A C     1 
ATOM   1233 O  O     . PHE A 1 198 ? -11.69700 -4.80500  -32.91000 1.000 66.17608  ? 164 PHE A O     1 
ATOM   1234 C  CB    . PHE A 1 198 ? -13.47400 -2.89900  -33.81800 1.000 47.53696  ? 164 PHE A CB    1 
ATOM   1235 C  CG    . PHE A 1 198 ? -14.20700 -1.65800  -34.22200 1.000 51.53116  ? 164 PHE A CG    1 
ATOM   1236 C  CD1   . PHE A 1 198 ? -14.99900 -1.64400  -35.36000 1.000 43.70443  ? 164 PHE A CD1   1 
ATOM   1237 C  CD2   . PHE A 1 198 ? -14.09800 -0.50100  -33.46900 1.000 39.75019  ? 164 PHE A CD2   1 
ATOM   1238 C  CE1   . PHE A 1 198 ? -15.66900 -0.49900  -35.74000 1.000 41.81006  ? 164 PHE A CE1   1 
ATOM   1239 C  CE2   . PHE A 1 198 ? -14.76700 0.64700   -33.84300 1.000 44.87445  ? 164 PHE A CE2   1 
ATOM   1240 C  CZ    . PHE A 1 198 ? -15.55300 0.64800   -34.98200 1.000 48.92056  ? 164 PHE A CZ    1 
ATOM   1241 N  N     . VAL A 1 199 ? -10.55100 -4.91200  -34.83900 1.000 62.91792  ? 165 VAL A N     1 
ATOM   1242 C  CA    . VAL A 1 199 ? -9.87100  -6.13800  -34.43900 1.000 69.81698  ? 165 VAL A CA    1 
ATOM   1243 C  C     . VAL A 1 199 ? -8.62900  -5.85600  -33.60600 1.000 74.78701  ? 165 VAL A C     1 
ATOM   1244 O  O     . VAL A 1 199 ? -8.21100  -6.71700  -32.82300 1.000 76.72013  ? 165 VAL A O     1 
ATOM   1245 C  CB    . VAL A 1 199 ? -9.51100  -6.98200  -35.67500 1.000 58.54437  ? 165 VAL A CB    1 
ATOM   1246 C  CG1   . VAL A 1 199 ? -10.75700 -7.26900  -36.49800 1.000 58.70582  ? 165 VAL A CG1   1 
ATOM   1247 C  CG2   . VAL A 1 199 ? -8.46900  -6.26500  -36.52600 1.000 62.31988  ? 165 VAL A CG2   1 
ATOM   1248 N  N     . SER A 1 200 ? -8.03400  -4.67400  -33.74000 1.000 77.38461  ? 166 SER A N     1 
ATOM   1249 C  CA    . SER A 1 200 ? -6.81200  -4.36300  -33.01100 1.000 73.47240  ? 166 SER A CA    1 
ATOM   1250 C  C     . SER A 1 200 ? -7.08700  -4.22400  -31.51600 1.000 79.77419  ? 166 SER A C     1 
ATOM   1251 O  O     . SER A 1 200 ? -8.18600  -3.86100  -31.09100 1.000 71.28659  ? 166 SER A O     1 
ATOM   1252 C  CB    . SER A 1 200 ? -6.18000  -3.07700  -33.54800 1.000 68.89101  ? 166 SER A CB    1 
ATOM   1253 O  OG    . SER A 1 200 ? -5.06800  -2.69100  -32.75600 1.000 82.63609  ? 166 SER A OG    1 
ATOM   1254 N  N     . ASP A 1 201 ? -6.06200  -4.52300  -30.71300 1.000 89.02642  ? 167 ASP A N     1 
ATOM   1255 C  CA    . ASP A 1 201 ? -6.20600  -4.39900  -29.26500 1.000 93.92477  ? 167 ASP A CA    1 
ATOM   1256 C  C     . ASP A 1 201 ? -6.20800  -2.94100  -28.82200 1.000 80.16064  ? 167 ASP A C     1 
ATOM   1257 O  O     . ASP A 1 201 ? -6.87100  -2.59300  -27.83800 1.000 64.64760  ? 167 ASP A O     1 
ATOM   1258 C  CB    . ASP A 1 201 ? -5.09000  -5.16800  -28.55800 1.000 96.64051  ? 167 ASP A CB    1 
ATOM   1259 C  CG    . ASP A 1 201 ? -5.18600  -6.66500  -28.77600 1.000 109.66772 ? 167 ASP A CG    1 
ATOM   1260 O  OD1   . ASP A 1 201 ? -6.31700  -7.19700  -28.75800 1.000 111.41130 ? 167 ASP A OD1   1 
ATOM   1261 O  OD2   . ASP A 1 201 ? -4.13200  -7.30700  -28.96700 1.000 116.54108 ? 167 ASP A OD2   1 
ATOM   1262 N  N     . SER A 1 202 ? -5.48500  -2.08100  -29.53500 1.000 79.88282  ? 168 SER A N     1 
ATOM   1263 C  CA    . SER A 1 202 ? -5.38100  -0.66800  -29.20800 1.000 75.43162  ? 168 SER A CA    1 
ATOM   1264 C  C     . SER A 1 202 ? -5.94300  0.17600   -30.34500 1.000 71.00556  ? 168 SER A C     1 
ATOM   1265 O  O     . SER A 1 202 ? -5.91000  -0.22200  -31.51400 1.000 69.67315  ? 168 SER A O     1 
ATOM   1266 C  CB    . SER A 1 202 ? -3.92400  -0.26900  -28.93600 1.000 70.33883  ? 168 SER A CB    1 
ATOM   1267 O  OG    . SER A 1 202 ? -3.85500  0.93600   -28.19500 1.000 77.25763  ? 168 SER A OG    1 
ATOM   1268 N  N     . GLY A 1 203 ? -6.46000  1.34900   -29.98900 1.000 61.99920  ? 169 GLY A N     1 
ATOM   1269 C  CA    . GLY A 1 203 ? -6.97600  2.28200   -30.95800 1.000 52.89696  ? 169 GLY A CA    1 
ATOM   1270 C  C     . GLY A 1 203 ? -5.86500  3.05400   -31.63700 1.000 55.00814  ? 169 GLY A C     1 
ATOM   1271 O  O     . GLY A 1 203 ? -4.67900  2.76900   -31.44500 1.000 61.96854  ? 169 GLY A O     1 
ATOM   1272 N  N     . PRO A 1 204 ? -6.22400  4.06400   -32.44300 1.000 58.90377  ? 170 PRO A N     1 
ATOM   1273 C  CA    . PRO A 1 204 ? -7.58200  4.54200   -32.75400 1.000 47.98042  ? 170 PRO A CA    1 
ATOM   1274 C  C     . PRO A 1 204 ? -8.32400  3.60300   -33.69300 1.000 49.17047  ? 170 PRO A C     1 
ATOM   1275 O  O     . PRO A 1 204 ? -7.71700  2.75100   -34.33300 1.000 48.77892  ? 170 PRO A O     1 
ATOM   1276 C  CB    . PRO A 1 204 ? -7.33600  5.90800   -33.42700 1.000 44.48584  ? 170 PRO A CB    1 
ATOM   1277 C  CG    . PRO A 1 204 ? -5.88500  6.24300   -33.17000 1.000 58.35169  ? 170 PRO A CG    1 
ATOM   1278 C  CD    . PRO A 1 204 ? -5.20200  4.91500   -33.06900 1.000 55.95608  ? 170 PRO A CD    1 
ATOM   1279 N  N     . TYR A 1 205 ? -9.64100  3.74900   -33.79600 1.000 42.38634  ? 171 TYR A N     1 
ATOM   1280 C  CA    . TYR A 1 205 ? -10.45400 2.94100   -34.68900 1.000 45.53611  ? 171 TYR A CA    1 
ATOM   1281 C  C     . TYR A 1 205 ? -11.22200 3.84600   -35.63900 1.000 47.61533  ? 171 TYR A C     1 
ATOM   1282 O  O     . TYR A 1 205 ? -11.74700 4.88500   -35.22900 1.000 43.74392  ? 171 TYR A O     1 
ATOM   1283 C  CB    . TYR A 1 205 ? -11.42500 2.06800   -33.90400 1.000 40.50346  ? 171 TYR A CB    1 
ATOM   1284 C  CG    . TYR A 1 205 ? -10.75800 1.16800   -32.89600 1.000 48.29870  ? 171 TYR A CG    1 
ATOM   1285 C  CD1   . TYR A 1 205 ? -10.23800 -0.06300  -33.27900 1.000 43.96725  ? 171 TYR A CD1   1 
ATOM   1286 C  CD2   . TYR A 1 205 ? -10.66100 1.53800   -31.55700 1.000 43.39204  ? 171 TYR A CD2   1 
ATOM   1287 C  CE1   . TYR A 1 205 ? -9.63400  -0.89700  -32.36300 1.000 54.25650  ? 171 TYR A CE1   1 
ATOM   1288 C  CE2   . TYR A 1 205 ? -10.06000 0.70800   -30.63000 1.000 47.82577  ? 171 TYR A CE2   1 
ATOM   1289 C  CZ    . TYR A 1 205 ? -9.54700  -0.50800  -31.04100 1.000 57.84609  ? 171 TYR A CZ    1 
ATOM   1290 O  OH    . TYR A 1 205 ? -8.94400  -1.34700  -30.13200 1.000 57.12343  ? 171 TYR A OH    1 
ATOM   1291 N  N     . GLN A 1 206 ? -11.28900 3.44200   -36.90600 1.000 35.39866  ? 172 GLN A N     1 
ATOM   1292 C  CA    . GLN A 1 206 ? -11.97800 4.19900   -37.94400 1.000 39.27919  ? 172 GLN A CA    1 
ATOM   1293 C  C     . GLN A 1 206 ? -13.38600 3.65300   -38.14200 1.000 42.12053  ? 172 GLN A C     1 
ATOM   1294 O  O     . GLN A 1 206 ? -13.57500 2.43700   -38.24700 1.000 38.34933  ? 172 GLN A O     1 
ATOM   1295 C  CB    . GLN A 1 206 ? -11.21500 4.13200   -39.26800 1.000 41.20307  ? 172 GLN A CB    1 
ATOM   1296 C  CG    . GLN A 1 206 ? -9.89500  4.87400   -39.28100 1.000 42.37931  ? 172 GLN A CG    1 
ATOM   1297 C  CD    . GLN A 1 206 ? -10.03200 6.29800   -38.79200 1.000 56.75418  ? 172 GLN A CD    1 
ATOM   1298 O  OE1   . GLN A 1 206 ? -9.63100  6.61600   -37.67600 1.000 64.22407  ? 172 GLN A OE1   1 
ATOM   1299 N  NE2   . GLN A 1 206 ? -10.61000 7.16500   -39.62300 1.000 64.95951  ? 172 GLN A NE2   1 
ATOM   1300 N  N     . ILE A 1 207 ? -14.36600 4.54700   -38.21000 1.000 36.57689  ? 173 ILE A N     1 
ATOM   1301 C  CA    . ILE A 1 207 ? -15.74200 4.17700   -38.51900 1.000 37.03405  ? 173 ILE A CA    1 
ATOM   1302 C  C     . ILE A 1 207 ? -16.03400 4.59800   -39.95000 1.000 41.87762  ? 173 ILE A C     1 
ATOM   1303 O  O     . ILE A 1 207 ? -16.01200 5.79400   -40.27100 1.000 38.26545  ? 173 ILE A O     1 
ATOM   1304 C  CB    . ILE A 1 207 ? -16.73600 4.81100   -37.53700 1.000 39.52587  ? 173 ILE A CB    1 
ATOM   1305 C  CG1   . ILE A 1 207 ? -16.33900 4.46100   -36.09800 1.000 42.37506  ? 173 ILE A CG1   1 
ATOM   1306 C  CG2   . ILE A 1 207 ? -18.14400 4.32900   -37.84200 1.000 34.25404  ? 173 ILE A CG2   1 
ATOM   1307 C  CD1   . ILE A 1 207 ? -17.21300 5.10500   -35.05100 1.000 35.51046  ? 173 ILE A CD1   1 
ATOM   1308 N  N     . HIS A 1 208 ? -16.31400 3.62100   -40.80700 1.000 42.10773  ? 174 HIS A N     1 
ATOM   1309 C  CA    . HIS A 1 208 ? -16.48400 3.84800   -42.23300 1.000 44.38475  ? 174 HIS A CA    1 
ATOM   1310 C  C     . HIS A 1 208 ? -17.95300 3.78000   -42.62900 1.000 43.33873  ? 174 HIS A C     1 
ATOM   1311 O  O     . HIS A 1 208 ? -18.78900 3.21600   -41.91800 1.000 38.91283  ? 174 HIS A O     1 
ATOM   1312 C  CB    . HIS A 1 208 ? -15.68600 2.82300   -43.05100 1.000 40.62922  ? 174 HIS A CB    1 
ATOM   1313 C  CG    . HIS A 1 208 ? -14.20900 2.87600   -42.81500 1.000 47.57022  ? 174 HIS A CG    1 
ATOM   1314 N  ND1   . HIS A 1 208 ? -13.43000 3.93600   -43.22700 1.000 54.48511  ? 174 HIS A ND1   1 
ATOM   1315 C  CD2   . HIS A 1 208 ? -13.36400 1.99400   -42.23100 1.000 45.24981  ? 174 HIS A CD2   1 
ATOM   1316 C  CE1   . HIS A 1 208 ? -12.17200 3.71400   -42.89100 1.000 46.08702  ? 174 HIS A CE1   1 
ATOM   1317 N  NE2   . HIS A 1 208 ? -12.10400 2.54100   -42.28600 1.000 53.48433  ? 174 HIS A NE2   1 
ATOM   1318 N  N     . GLY A 1 209 ? -18.25400 4.36500   -43.79200 1.000 41.15838  ? 175 GLY A N     1 
ATOM   1319 C  CA    . GLY A 1 209 ? -19.55900 4.25100   -44.40600 1.000 29.93571  ? 175 GLY A CA    1 
ATOM   1320 C  C     . GLY A 1 209 ? -20.54400 5.35200   -44.08200 1.000 33.08443  ? 175 GLY A C     1 
ATOM   1321 O  O     . GLY A 1 209 ? -21.66600 5.32100   -44.60300 1.000 38.21606  ? 175 GLY A O     1 
ATOM   1322 N  N     . LEU A 1 210 ? -20.16900 6.32500   -43.23600 1.000 31.44128  ? 176 LEU A N     1 
ATOM   1323 C  CA    . LEU A 1 210 ? -21.08900 7.37100   -42.81000 1.000 34.06401  ? 176 LEU A CA    1 
ATOM   1324 C  C     . LEU A 1 210 ? -20.80200 8.67100   -43.54700 1.000 30.01443  ? 176 LEU A C     1 
ATOM   1325 O  O     . LEU A 1 210 ? -19.75100 8.81800   -44.17400 1.000 33.86904  ? 176 LEU A O     1 
ATOM   1326 C  CB    . LEU A 1 210 ? -20.97800 7.58900   -41.29300 1.000 32.12076  ? 176 LEU A CB    1 
ATOM   1327 C  CG    . LEU A 1 210 ? -21.48300 6.41800   -40.44500 1.000 34.05531  ? 176 LEU A CG    1 
ATOM   1328 C  CD1   . LEU A 1 210 ? -21.16300 6.63400   -38.97000 1.000 29.71704  ? 176 LEU A CD1   1 
ATOM   1329 C  CD2   . LEU A 1 210 ? -22.98100 6.23300   -40.65300 1.000 25.98024  ? 176 LEU A CD2   1 
ATOM   1330 N  N     . PRO A 1 211 ? -21.72900 9.63800   -43.51400 1.000 32.86808  ? 177 PRO A N     1 
ATOM   1331 C  CA    . PRO A 1 211 ? -21.44200 10.94400  -44.13100 1.000 33.86190  ? 177 PRO A CA    1 
ATOM   1332 C  C     . PRO A 1 211 ? -20.15000 11.58200  -43.65800 1.000 33.75459  ? 177 PRO A C     1 
ATOM   1333 O  O     . PRO A 1 211 ? -19.52500 12.33200  -44.41800 1.000 38.74213  ? 177 PRO A O     1 
ATOM   1334 C  CB    . PRO A 1 211 ? -22.66300 11.78400  -43.73600 1.000 30.13230  ? 177 PRO A CB    1 
ATOM   1335 C  CG    . PRO A 1 211 ? -23.76800 10.78700  -43.66700 1.000 35.17367  ? 177 PRO A CG    1 
ATOM   1336 C  CD    . PRO A 1 211 ? -23.14600 9.52700   -43.11100 1.000 32.43019  ? 177 PRO A CD    1 
ATOM   1337 N  N     . HIS A 1 212 ? -19.71800 11.29700  -42.43600 1.000 33.54402  ? 178 HIS A N     1 
ATOM   1338 C  CA    . HIS A 1 212 ? -18.50700 11.89100  -41.90400 1.000 35.06661  ? 178 HIS A CA    1 
ATOM   1339 C  C     . HIS A 1 212 ? -17.54000 10.80300  -41.46100 1.000 31.90098  ? 178 HIS A C     1 
ATOM   1340 O  O     . HIS A 1 212 ? -17.96400 9.74300   -40.98700 1.000 36.91333  ? 178 HIS A O     1 
ATOM   1341 C  CB    . HIS A 1 212 ? -18.81900 12.81000  -40.71400 1.000 28.15057  ? 178 HIS A CB    1 
ATOM   1342 C  CG    . HIS A 1 212 ? -19.76700 13.92200  -41.04300 1.000 32.86682  ? 178 HIS A CG    1 
ATOM   1343 N  ND1   . HIS A 1 212 ? -21.13500 13.75300  -41.04700 1.000 27.94237  ? 178 HIS A ND1   1 
ATOM   1344 C  CD2   . HIS A 1 212 ? -19.54600 15.21600  -41.37300 1.000 29.70328  ? 178 HIS A CD2   1 
ATOM   1345 C  CE1   . HIS A 1 212 ? -21.71700 14.89500  -41.36900 1.000 34.61734  ? 178 HIS A CE1   1 
ATOM   1346 N  NE2   . HIS A 1 212 ? -20.77500 15.79900  -41.57100 1.000 39.76422  ? 178 HIS A NE2   1 
ATOM   1347 N  N     . PRO A 1 213 ? -16.23800 11.02800  -41.61500 1.000 29.48684  ? 179 PRO A N     1 
ATOM   1348 C  CA    . PRO A 1 213 ? -15.26100 10.10300  -41.02800 1.000 35.15498  ? 179 PRO A CA    1 
ATOM   1349 C  C     . PRO A 1 213 ? -15.26900 10.24600  -39.51200 1.000 38.58816  ? 179 PRO A C     1 
ATOM   1350 O  O     . PRO A 1 213 ? -15.17500 11.35300  -38.97900 1.000 39.75975  ? 179 PRO A O     1 
ATOM   1351 C  CB    . PRO A 1 213 ? -13.92400 10.55900  -41.62800 1.000 34.67423  ? 179 PRO A CB    1 
ATOM   1352 C  CG    . PRO A 1 213 ? -14.27100 11.56700  -42.69000 1.000 44.71864  ? 179 PRO A CG    1 
ATOM   1353 C  CD    . PRO A 1 213 ? -15.58600 12.15400  -42.29900 1.000 32.82685  ? 179 PRO A CD    1 
ATOM   1354 N  N     . LEU A 1 214 ? -15.40100 9.12500   -38.81900 1.000 34.06393  ? 180 LEU A N     1 
ATOM   1355 C  CA    . LEU A 1 214 ? -15.43300 9.12900   -37.36700 1.000 44.91089  ? 180 LEU A CA    1 
ATOM   1356 C  C     . LEU A 1 214 ? -14.32200 8.24100   -36.83400 1.000 40.85191  ? 180 LEU A C     1 
ATOM   1357 O  O     . LEU A 1 214 ? -13.91400 7.27400   -37.48300 1.000 37.05466  ? 180 LEU A O     1 
ATOM   1358 C  CB    . LEU A 1 214 ? -16.79100 8.65500   -36.83300 1.000 37.05964  ? 180 LEU A CB    1 
ATOM   1359 C  CG    . LEU A 1 214 ? -18.02400 9.43500   -37.30000 1.000 34.89734  ? 180 LEU A CG    1 
ATOM   1360 C  CD1   . LEU A 1 214 ? -19.28200 8.84000   -36.69100 1.000 40.93758  ? 180 LEU A CD1   1 
ATOM   1361 C  CD2   . LEU A 1 214 ? -17.90800 10.90700  -36.93400 1.000 33.96668  ? 180 LEU A CD2   1 
ATOM   1362 N  N     . THR A 1 215 ? -13.82900 8.58900   -35.64900 1.000 39.86832  ? 181 THR A N     1 
ATOM   1363 C  CA    . THR A 1 215 ? -12.75700 7.85800   -34.99300 1.000 41.92779  ? 181 THR A CA    1 
ATOM   1364 C  C     . THR A 1 215 ? -13.15400 7.55400   -33.55600 1.000 42.39806  ? 181 THR A C     1 
ATOM   1365 O  O     . THR A 1 215 ? -13.93500 8.28200   -32.93800 1.000 44.30064  ? 181 THR A O     1 
ATOM   1366 C  CB    . THR A 1 215 ? -11.43600 8.64500   -35.00800 1.000 44.28948  ? 181 THR A CB    1 
ATOM   1367 O  OG1   . THR A 1 215 ? -11.58200 9.83200   -34.21900 1.000 54.67529  ? 181 THR A OG1   1 
ATOM   1368 C  CG2   . THR A 1 215 ? -11.06500 9.04200   -36.42400 1.000 41.94838  ? 181 THR A CG2   1 
ATOM   1369 N  N     . LEU A 1 216 ? -12.60700 6.46400   -33.03400 1.000 41.11458  ? 182 LEU A N     1 
ATOM   1370 C  CA    . LEU A 1 216 ? -12.84000 6.05900   -31.66300 1.000 40.30773  ? 182 LEU A CA    1 
ATOM   1371 C  C     . LEU A 1 216 ? -11.50000 5.68600   -31.04500 1.000 41.11012  ? 182 LEU A C     1 
ATOM   1372 O  O     . LEU A 1 216 ? -10.72800 4.92700   -31.65500 1.000 38.51301  ? 182 LEU A O     1 
ATOM   1373 C  CB    . LEU A 1 216 ? -13.80600 4.87600   -31.58600 1.000 41.25340  ? 182 LEU A CB    1 
ATOM   1374 C  CG    . LEU A 1 216 ? -15.28200 5.15600   -31.85100 1.000 42.17352  ? 182 LEU A CG    1 
ATOM   1375 C  CD1   . LEU A 1 216 ? -16.08400 3.87000   -31.72000 1.000 43.63857  ? 182 LEU A CD1   1 
ATOM   1376 C  CD2   . LEU A 1 216 ? -15.80900 6.23000   -30.90900 1.000 39.11792  ? 182 LEU A CD2   1 
ATOM   1377 N  N     . PRO A 1 217 ? -11.18100 6.19400   -29.85500 1.000 39.09306  ? 183 PRO A N     1 
ATOM   1378 C  CA    . PRO A 1 217 ? -9.93000  5.79900   -29.19200 1.000 41.96599  ? 183 PRO A CA    1 
ATOM   1379 C  C     . PRO A 1 217 ? -10.03100 4.44600   -28.50600 1.000 42.59681  ? 183 PRO A C     1 
ATOM   1380 O  O     . PRO A 1 217 ? -9.02400  3.75300   -28.32500 1.000 44.80797  ? 183 PRO A O     1 
ATOM   1381 C  CB    . PRO A 1 217 ? -9.70500  6.92800   -28.17800 1.000 43.52431  ? 183 PRO A CB    1 
ATOM   1382 C  CG    . PRO A 1 217 ? -11.08400 7.41800   -27.85900 1.000 45.42639  ? 183 PRO A CG    1 
ATOM   1383 C  CD    . PRO A 1 217 ? -11.88100 7.27500   -29.13800 1.000 35.68279  ? 183 PRO A CD    1 
ATOM   1384 N  N     . ILE A 1 218 ? -11.24400 4.06500   -28.10900 1.000 41.70718  ? 184 ILE A N     1 
ATOM   1385 C  CA    . ILE A 1 218 ? -11.50700 2.79900   -27.43200 1.000 46.65106  ? 184 ILE A CA    1 
ATOM   1386 C  C     . ILE A 1 218 ? -12.60600 2.06300   -28.17800 1.000 44.03415  ? 184 ILE A C     1 
ATOM   1387 O  O     . ILE A 1 218 ? -13.57200 2.67900   -28.64200 1.000 39.56322  ? 184 ILE A O     1 
ATOM   1388 C  CB    . ILE A 1 218 ? -11.91400 3.00700   -25.95800 1.000 47.08648  ? 184 ILE A CB    1 
ATOM   1389 C  CG1   . ILE A 1 218 ? -11.02000 4.06300   -25.31100 1.000 48.76853  ? 184 ILE A CG1   1 
ATOM   1390 C  CG2   . ILE A 1 218 ? -11.86600 1.68900   -25.19400 1.000 53.68881  ? 184 ILE A CG2   1 
ATOM   1391 C  CD1   . ILE A 1 218 ? -9.70100  3.51500   -24.84000 1.000 48.15055  ? 184 ILE A CD1   1 
ATOM   1392 N  N     . LYS A 1 219 ? -12.47300 0.74400   -28.27900 1.000 44.05660  ? 185 LYS A N     1 
ATOM   1393 C  CA    . LYS A 1 219 ? -13.48300 -0.02600  -28.98200 1.000 51.36937  ? 185 LYS A CA    1 
ATOM   1394 C  C     . LYS A 1 219 ? -14.72000 -0.19000  -28.10000 1.000 41.86067  ? 185 LYS A C     1 
ATOM   1395 O  O     . LYS A 1 219 ? -14.61700 -0.22200  -26.87100 1.000 41.96916  ? 185 LYS A O     1 
ATOM   1396 C  CB    . LYS A 1 219 ? -12.94200 -1.39400  -29.39900 1.000 49.12809  ? 185 LYS A CB    1 
ATOM   1397 C  CG    . LYS A 1 219 ? -12.61000 -2.32000  -28.25200 1.000 53.24104  ? 185 LYS A CG    1 
ATOM   1398 C  CD    . LYS A 1 219 ? -12.38300 -3.73900  -28.74700 1.000 56.59669  ? 185 LYS A CD    1 
ATOM   1399 C  CE    . LYS A 1 219 ? -11.23400 -3.81000  -29.73700 1.000 55.00286  ? 185 LYS A CE    1 
ATOM   1400 N  NZ    . LYS A 1 219 ? -11.02400 -5.20500  -30.22500 1.000 66.43913  ? 185 LYS A NZ    1 
ATOM   1401 N  N     . PRO A 1 220 ? -15.90400 -0.26000  -28.70700 1.000 40.12436  ? 186 PRO A N     1 
ATOM   1402 C  CA    . PRO A 1 220 ? -17.12600 -0.43700  -27.91500 1.000 37.47522  ? 186 PRO A CA    1 
ATOM   1403 C  C     . PRO A 1 220 ? -17.09700 -1.74000  -27.13000 1.000 42.95083  ? 186 PRO A C     1 
ATOM   1404 O  O     . PRO A 1 220 ? -16.63300 -2.77400  -27.61600 1.000 48.19551  ? 186 PRO A O     1 
ATOM   1405 C  CB    . PRO A 1 220 ? -18.23600 -0.44100  -28.97400 1.000 35.63208  ? 186 PRO A CB    1 
ATOM   1406 C  CG    . PRO A 1 220 ? -17.64800 0.29000   -30.14200 1.000 37.25491  ? 186 PRO A CG    1 
ATOM   1407 C  CD    . PRO A 1 220 ? -16.18900 -0.04900  -30.13700 1.000 37.60879  ? 186 PRO A CD    1 
ATOM   1408 N  N     . SER A 1 221 ? -17.59400 -1.67600  -25.90200 1.000 35.39183  ? 187 SER A N     1 
ATOM   1409 C  CA    . SER A 1 221 ? -17.62400 -2.82600  -25.02200 1.000 38.72458  ? 187 SER A CA    1 
ATOM   1410 C  C     . SER A 1 221 ? -18.78800 -3.74000  -25.39200 1.000 37.23480  ? 187 SER A C     1 
ATOM   1411 O  O     . SER A 1 221 ? -19.76000 -3.29700  -26.01100 1.000 33.16488  ? 187 SER A O     1 
ATOM   1412 C  CB    . SER A 1 221 ? -17.73900 -2.36200  -23.57100 1.000 38.49015  ? 187 SER A CB    1 
ATOM   1413 O  OG    . SER A 1 221 ? -19.08400 -2.41000  -23.13500 1.000 47.03173  ? 187 SER A OG    1 
ATOM   1414 N  N     . PRO A 1 222 ? -18.71000 -5.02600  -25.03700 1.000 44.92260  ? 188 PRO A N     1 
ATOM   1415 C  CA    . PRO A 1 222 ? -19.78600 -5.95700  -25.40400 1.000 33.79998  ? 188 PRO A CA    1 
ATOM   1416 C  C     . PRO A 1 222 ? -21.15000 -5.44600  -24.96000 1.000 34.30614  ? 188 PRO A C     1 
ATOM   1417 O  O     . PRO A 1 222 ? -21.31000 -4.91000  -23.86000 1.000 39.52492  ? 188 PRO A O     1 
ATOM   1418 C  CB    . PRO A 1 222 ? -19.40100 -7.24900  -24.67500 1.000 39.29507  ? 188 PRO A CB    1 
ATOM   1419 C  CG    . PRO A 1 222 ? -17.91800 -7.15700  -24.49800 1.000 41.96470  ? 188 PRO A CG    1 
ATOM   1420 C  CD    . PRO A 1 222 ? -17.63200 -5.69600  -24.28300 1.000 43.05146  ? 188 PRO A CD    1 
ATOM   1421 N  N     . GLY A 1 223 ? -22.13400 -5.59600  -25.84000 1.000 35.36643  ? 189 GLY A N     1 
ATOM   1422 C  CA    . GLY A 1 223 ? -23.46200 -5.07800  -25.58100 1.000 34.21775  ? 189 GLY A CA    1 
ATOM   1423 C  C     . GLY A 1 223 ? -23.67900 -3.62200  -25.93500 1.000 35.34571  ? 189 GLY A C     1 
ATOM   1424 O  O     . GLY A 1 223 ? -24.68600 -3.04700  -25.51700 1.000 36.92730  ? 189 GLY A O     1 
ATOM   1425 N  N     . PHE A 1 224 ? -22.77600 -3.00300  -26.69900 1.000 38.23468  ? 190 PHE A N     1 
ATOM   1426 C  CA    . PHE A 1 224 ? -22.93400 -1.58800  -27.02600 1.000 33.81699  ? 190 PHE A CA    1 
ATOM   1427 C  C     . PHE A 1 224 ? -24.14500 -1.31800  -27.91100 1.000 30.49617  ? 190 PHE A C     1 
ATOM   1428 O  O     . PHE A 1 224 ? -24.59400 -0.16800  -27.98500 1.000 40.50087  ? 190 PHE A O     1 
ATOM   1429 C  CB    . PHE A 1 224 ? -21.67600 -1.05500  -27.71400 1.000 35.14508  ? 190 PHE A CB    1 
ATOM   1430 C  CG    . PHE A 1 224 ? -21.47500 -1.58900  -29.10800 1.000 34.99655  ? 190 PHE A CG    1 
ATOM   1431 C  CD1   . PHE A 1 224 ? -20.93400 -2.84900  -29.30600 1.000 34.74006  ? 190 PHE A CD1   1 
ATOM   1432 C  CD2   . PHE A 1 224 ? -21.81800 -0.82900  -30.21700 1.000 32.11408  ? 190 PHE A CD2   1 
ATOM   1433 C  CE1   . PHE A 1 224 ? -20.74600 -3.34600  -30.58200 1.000 36.11494  ? 190 PHE A CE1   1 
ATOM   1434 C  CE2   . PHE A 1 224 ? -21.63200 -1.32100  -31.49600 1.000 35.92011  ? 190 PHE A CE2   1 
ATOM   1435 C  CZ    . PHE A 1 224 ? -21.09600 -2.58100  -31.67800 1.000 31.06709  ? 190 PHE A CZ    1 
ATOM   1436 N  N     . ALA A 1 225 ? -24.68500 -2.33600  -28.58200 1.000 33.41375  ? 191 ALA A N     1 
ATOM   1437 C  CA    . ALA A 1 225 ? -25.76500 -2.14500  -29.54400 1.000 39.52778  ? 191 ALA A CA    1 
ATOM   1438 C  C     . ALA A 1 225 ? -27.13000 -2.54200  -28.98800 1.000 37.76667  ? 191 ALA A C     1 
ATOM   1439 O  O     . ALA A 1 225 ? -28.03900 -2.87300  -29.76100 1.000 36.83896  ? 191 ALA A O     1 
ATOM   1440 C  CB    . ALA A 1 225 ? -25.47100 -2.91300  -30.83200 1.000 32.13358  ? 191 ALA A CB    1 
ATOM   1441 N  N     . ARG A 1 226 ? -27.29400 -2.50700  -27.66800 1.000 43.01201  ? 192 ARG A N     1 
ATOM   1442 C  CA    . ARG A 1 226 ? -28.58700 -2.79300  -27.06100 1.000 40.87245  ? 192 ARG A CA    1 
ATOM   1443 C  C     . ARG A 1 226 ? -29.61400 -1.73700  -27.43900 1.000 33.67022  ? 192 ARG A C     1 
ATOM   1444 O  O     . ARG A 1 226 ? -29.28000 -0.57700  -27.69800 1.000 36.31363  ? 192 ARG A O     1 
ATOM   1445 C  CB    . ARG A 1 226 ? -28.48700 -2.83600  -25.53700 1.000 40.07171  ? 192 ARG A CB    1 
ATOM   1446 C  CG    . ARG A 1 226 ? -27.52300 -3.83300  -24.97800 1.000 47.06220  ? 192 ARG A CG    1 
ATOM   1447 C  CD    . ARG A 1 226 ? -27.15500 -3.45800  -23.55200 1.000 47.26518  ? 192 ARG A CD    1 
ATOM   1448 N  NE    . ARG A 1 226 ? -26.10200 -4.32400  -23.03700 1.000 57.22806  ? 192 ARG A NE    1 
ATOM   1449 C  CZ    . ARG A 1 226 ? -25.43400 -4.10200  -21.91400 1.000 56.16109  ? 192 ARG A CZ    1 
ATOM   1450 N  NH1   . ARG A 1 226 ? -25.72300 -3.07400  -21.13000 1.000 49.45174  ? 192 ARG A NH1   1 
ATOM   1451 N  NH2   . ARG A 1 226 ? -24.44800 -4.92800  -21.57400 1.000 52.64218  ? 192 ARG A NH2   1 
ATOM   1452 N  N     . LEU A 1 227 ? -30.88300 -2.15200  -27.43000 1.000 44.56996  ? 193 LEU A N     1 
ATOM   1453 C  CA    . LEU A 1 227 ? -32.02200 -1.26000  -27.66300 1.000 56.66946  ? 193 LEU A CA    1 
ATOM   1454 C  C     . LEU A 1 227 ? -31.94000 -0.58700  -29.03400 1.000 43.20547  ? 193 LEU A C     1 
ATOM   1455 O  O     . LEU A 1 227 ? -32.31500 0.57600   -29.19900 1.000 64.17116  ? 193 LEU A O     1 
ATOM   1456 C  CB    . LEU A 1 227 ? -32.14600 -0.21700  -26.54700 1.000 55.77371  ? 193 LEU A CB    1 
ATOM   1457 C  CG    . LEU A 1 227 ? -32.19600 -0.77100  -25.11700 1.000 61.41213  ? 193 LEU A CG    1 
ATOM   1458 C  CD1   . LEU A 1 227 ? -32.28300 0.35100   -24.08900 1.000 57.46855  ? 193 LEU A CD1   1 
ATOM   1459 C  CD2   . LEU A 1 227 ? -33.35200 -1.74700  -24.95000 1.000 55.57282  ? 193 LEU A CD2   1 
ATOM   1460 N  N     . THR A 1 228 ? -31.43300 -1.32100  -30.02900 1.000 42.37615  ? 194 THR A N     1 
ATOM   1461 C  CA    . THR A 1 228 ? -31.40800 -0.83400  -31.40400 1.000 44.01009  ? 194 THR A CA    1 
ATOM   1462 C  C     . THR A 1 228 ? -32.03300 -1.78900  -32.40700 1.000 50.76485  ? 194 THR A C     1 
ATOM   1463 O  O     . THR A 1 228 ? -32.19700 -1.40000  -33.56900 1.000 54.04018  ? 194 THR A O     1 
ATOM   1464 C  CB    . THR A 1 228 ? -29.97000 -0.54200  -31.86900 1.000 41.36419  ? 194 THR A CB    1 
ATOM   1465 O  OG1   . THR A 1 228 ? -29.29500 -1.77600  -32.14800 1.000 44.24343  ? 194 THR A OG1   1 
ATOM   1466 C  CG2   . THR A 1 228 ? -29.19800 0.23000   -30.81400 1.000 47.58643  ? 194 THR A CG2   1 
ATOM   1467 N  N     . GLU A 1 229 ? -32.37400 -3.01900  -32.01200 1.000 52.84014  ? 195 GLU A N     1 
ATOM   1468 C  CA    . GLU A 1 229 ? -32.92800 -3.97400  -32.96600 1.000 57.54972  ? 195 GLU A CA    1 
ATOM   1469 C  C     . GLU A 1 229 ? -34.23700 -3.46600  -33.55800 1.000 52.57128  ? 195 GLU A C     1 
ATOM   1470 O  O     . GLU A 1 229 ? -34.50700 -3.66000  -34.75000 1.000 55.05274  ? 195 GLU A O     1 
ATOM   1471 N  N     . SER A 1 230 ? -35.05700 -2.80100  -32.74500 1.000 44.83226  ? 196 SER A N     1 
ATOM   1472 C  CA    . SER A 1 230 ? -36.32200 -2.27700  -33.24200 1.000 55.36843  ? 196 SER A CA    1 
ATOM   1473 C  C     . SER A 1 230 ? -36.11200 -1.12300  -34.21900 1.000 55.73215  ? 196 SER A C     1 
ATOM   1474 O  O     . SER A 1 230 ? -36.95300 -0.89900  -35.09500 1.000 52.05423  ? 196 SER A O     1 
ATOM   1475 C  CB    . SER A 1 230 ? -37.20200 -1.84800  -32.06600 1.000 49.54855  ? 196 SER A CB    1 
ATOM   1476 O  OG    . SER A 1 230 ? -37.11500 -0.45400  -31.81900 1.000 71.32616  ? 196 SER A OG    1 
ATOM   1477 N  N     . LEU A 1 231 ? -34.99900 -0.39400  -34.09800 1.000 45.88502  ? 197 LEU A N     1 
ATOM   1478 C  CA    . LEU A 1 231 ? -34.70500 0.72700   -34.98700 1.000 46.89183  ? 197 LEU A CA    1 
ATOM   1479 C  C     . LEU A 1 231 ? -33.96800 0.30200   -36.25100 1.000 43.96298  ? 197 LEU A C     1 
ATOM   1480 O  O     . LEU A 1 231 ? -34.21400 0.86300   -37.32500 1.000 53.26521  ? 197 LEU A O     1 
ATOM   1481 C  CB    . LEU A 1 231 ? -33.87300 1.78000   -34.25400 1.000 46.16317  ? 197 LEU A CB    1 
ATOM   1482 C  CG    . LEU A 1 231 ? -34.61900 2.84700   -33.46100 1.000 48.58053  ? 197 LEU A CG    1 
ATOM   1483 C  CD1   . LEU A 1 231 ? -33.63500 3.61000   -32.58500 1.000 50.44475  ? 197 LEU A CD1   1 
ATOM   1484 C  CD2   . LEU A 1 231 ? -35.36200 3.78800   -34.38800 1.000 42.73458  ? 197 LEU A CD2   1 
ATOM   1485 N  N     . ILE A 1 232 ? -33.06500 -0.67600  -36.14400 1.000 47.30392  ? 198 ILE A N     1 
ATOM   1486 C  CA    . ILE A 1 232 ? -32.23000 -1.05600  -37.28100 1.000 38.32751  ? 198 ILE A CA    1 
ATOM   1487 C  C     . ILE A 1 232 ? -32.97400 -1.97500  -38.25000 1.000 44.82896  ? 198 ILE A C     1 
ATOM   1488 O  O     . ILE A 1 232 ? -32.68300 -1.97700  -39.45400 1.000 51.02608  ? 198 ILE A O     1 
ATOM   1489 C  CB    . ILE A 1 232 ? -30.92100 -1.69200  -36.77100 1.000 53.88574  ? 198 ILE A CB    1 
ATOM   1490 C  CG1   . ILE A 1 232 ? -29.85000 -0.62100  -36.57500 1.000 53.62982  ? 198 ILE A CG1   1 
ATOM   1491 C  CG2   . ILE A 1 232 ? -30.40500 -2.77400  -37.71100 1.000 51.60046  ? 198 ILE A CG2   1 
ATOM   1492 C  CD1   . ILE A 1 232 ? -28.55300 -1.15400  -35.98700 1.000 62.10525  ? 198 ILE A CD1   1 
ATOM   1493 N  N     . GLU A 1 233 ? -33.94500 -2.74700  -37.76600 1.000 49.68353  ? 199 GLU A N     1 
ATOM   1494 C  CA    . GLU A 1 233 ? -34.65600 -3.67900  -38.63200 1.000 60.74833  ? 199 GLU A CA    1 
ATOM   1495 C  C     . GLU A 1 233 ? -35.38600 -2.94100  -39.75400 1.000 55.47756  ? 199 GLU A C     1 
ATOM   1496 O  O     . GLU A 1 233 ? -35.80400 -1.78900  -39.61000 1.000 49.07945  ? 199 GLU A O     1 
ATOM   1497 C  CB    . GLU A 1 233 ? -35.63900 -4.51900  -37.81400 1.000 57.44199  ? 199 GLU A CB    1 
ATOM   1498 C  CG    . GLU A 1 233 ? -36.94100 -3.81500  -37.47200 1.000 64.90955  ? 199 GLU A CG    1 
ATOM   1499 C  CD    . GLU A 1 233 ? -37.84300 -4.65100  -36.58300 1.000 76.72169  ? 199 GLU A CD    1 
ATOM   1500 O  OE1   . GLU A 1 233 ? -37.57800 -5.86600  -36.44200 1.000 82.08401  ? 199 GLU A OE1   1 
ATOM   1501 O  OE2   . GLU A 1 233 ? -38.81600 -4.09400  -36.02800 1.000 78.44142  ? 199 GLU A OE2   1 
ATOM   1502 N  N     . ALA A 1 234 ? -35.52700 -3.62300  -40.88800 1.000 58.01739  ? 200 ALA A N     1 
ATOM   1503 C  CA    . ALA A 1 234 ? -36.14100 -3.03200  -42.06500 1.000 57.88198  ? 200 ALA A CA    1 
ATOM   1504 C  C     . ALA A 1 234 ? -37.62700 -2.75800  -41.82600 1.000 65.25963  ? 200 ALA A C     1 
ATOM   1505 O  O     . ALA A 1 234 ? -38.22000 -3.17800  -40.82800 1.000 68.20872  ? 200 ALA A O     1 
ATOM   1506 C  CB    . ALA A 1 234 ? -35.96000 -3.94500  -43.27600 1.000 54.70999  ? 200 ALA A CB    1 
ATOM   1507 N  N     . GLU A 1 235 ? -38.22800 -2.03600  -42.76800 1.000 71.15712  ? 201 GLU A N     1 
ATOM   1508 C  CA    . GLU A 1 235 ? -39.62700 -1.65500  -42.65600 1.000 73.86521  ? 201 GLU A CA    1 
ATOM   1509 C  C     . GLU A 1 235 ? -40.53400 -2.83300  -42.98000 1.000 81.20251  ? 201 GLU A C     1 
ATOM   1510 O  O     . GLU A 1 235 ? -40.24100 -3.64300  -43.86500 1.000 83.72152  ? 201 GLU A O     1 
ATOM   1511 C  CB    . GLU A 1 235 ? -39.94900 -0.48400  -43.59000 1.000 62.29429  ? 201 GLU A CB    1 
ATOM   1512 C  CG    . GLU A 1 235 ? -39.87100 -0.81900  -45.07400 1.000 68.84624  ? 201 GLU A CG    1 
ATOM   1513 C  CD    . GLU A 1 235 ? -41.19800 -1.30500  -45.64900 1.000 81.75504  ? 201 GLU A CD    1 
ATOM   1514 O  OE1   . GLU A 1 235 ? -42.25800 -0.77300  -45.25300 1.000 77.86719  ? 201 GLU A OE1   1 
ATOM   1515 O  OE2   . GLU A 1 235 ? -41.17700 -2.22900  -46.49100 1.000 77.34480  ? 201 GLU A OE2   1 
ATOM   1516 N  N     . ASN A 1 236 ? -41.64400 -2.92200  -42.25200 1.000 77.06224  ? 202 ASN A N     1 
ATOM   1517 C  CA    . ASN A 1 236 ? -42.74000 -3.83600  -42.57200 1.000 78.96300  ? 202 ASN A CA    1 
ATOM   1518 C  C     . ASN A 1 236 ? -44.00100 -2.97700  -42.57800 1.000 76.64774  ? 202 ASN A C     1 
ATOM   1519 O  O     . ASN A 1 236 ? -44.78100 -2.99100  -41.62000 1.000 74.58463  ? 202 ASN A O     1 
ATOM   1520 C  CB    . ASN A 1 236 ? -42.82200 -4.99100  -41.57900 1.000 90.99957  ? 202 ASN A CB    1 
ATOM   1521 C  CG    . ASN A 1 236 ? -43.32000 -6.27200  -42.21900 1.000 95.07281  ? 202 ASN A CG    1 
ATOM   1522 O  OD1   . ASN A 1 236 ? -43.41500 -6.36900  -43.44400 1.000 93.23865  ? 202 ASN A OD1   1 
ATOM   1523 N  ND2   . ASN A 1 236 ? -43.63800 -7.26300  -41.39400 1.000 94.71817  ? 202 ASN A ND2   1 
ATOM   1524 N  N     . ASP A 1 237 ? -44.18200 -2.22000  -43.66000 1.000 68.88133  ? 203 ASP A N     1 
ATOM   1525 C  CA    . ASP A 1 237 ? -45.24400 -1.22400  -43.76800 1.000 58.96205  ? 203 ASP A CA    1 
ATOM   1526 C  C     . ASP A 1 237 ? -45.20500 -0.27600  -42.56900 1.000 51.24127  ? 203 ASP A C     1 
ATOM   1527 O  O     . ASP A 1 237 ? -46.15400 -0.15500  -41.79300 1.000 51.03325  ? 203 ASP A O     1 
ATOM   1528 C  CB    . ASP A 1 237 ? -46.61200 -1.89500  -43.91400 1.000 66.44996  ? 203 ASP A CB    1 
ATOM   1529 C  CG    . ASP A 1 237 ? -46.64800 -2.89300  -45.05600 1.000 74.60822  ? 203 ASP A CG    1 
ATOM   1530 O  OD1   . ASP A 1 237 ? -46.21300 -2.53500  -46.17200 1.000 60.23754  ? 203 ASP A OD1   1 
ATOM   1531 O  OD2   . ASP A 1 237 ? -47.11200 -4.03300  -44.83600 1.000 82.21392  ? 203 ASP A OD2   1 
ATOM   1532 N  N     . SER A 1 238 ? -44.06700 0.39500   -42.43000 1.000 47.49831  ? 204 SER A N     1 
ATOM   1533 C  CA    . SER A 1 238 ? -43.83100 1.25900   -41.28400 1.000 39.67328  ? 204 SER A CA    1 
ATOM   1534 C  C     . SER A 1 238 ? -44.43900 2.63600   -41.50800 1.000 35.54882  ? 204 SER A C     1 
ATOM   1535 O  O     . SER A 1 238 ? -44.32000 3.21800   -42.58900 1.000 41.36527  ? 204 SER A O     1 
ATOM   1536 C  CB    . SER A 1 238 ? -42.33000 1.39200   -41.01800 1.000 44.97596  ? 204 SER A CB    1 
ATOM   1537 O  OG    . SER A 1 238 ? -42.07900 2.42400   -40.08000 1.000 45.37731  ? 204 SER A OG    1 
ATOM   1538 N  N     . HIS A 1 239 ? -45.09500 3.15200   -40.47300 1.000 31.81821  ? 205 HIS A N     1 
ATOM   1539 C  CA    . HIS A 1 239 ? -45.58100 4.52400   -40.46100 1.000 37.30105  ? 205 HIS A CA    1 
ATOM   1540 C  C     . HIS A 1 239 ? -44.49100 5.52800   -40.10200 1.000 35.59092  ? 205 HIS A C     1 
ATOM   1541 O  O     . HIS A 1 239 ? -44.78000 6.72600   -39.99300 1.000 32.54778  ? 205 HIS A O     1 
ATOM   1542 C  CB    . HIS A 1 239 ? -46.74900 4.65100   -39.47900 1.000 34.90158  ? 205 HIS A CB    1 
ATOM   1543 C  CG    . HIS A 1 239 ? -47.87600 3.70400   -39.75300 1.000 41.63380  ? 205 HIS A CG    1 
ATOM   1544 N  ND1   . HIS A 1 239 ? -48.84900 3.95300   -40.69800 1.000 42.81343  ? 205 HIS A ND1   1 
ATOM   1545 C  CD2   . HIS A 1 239 ? -48.18200 2.50300   -39.20800 1.000 45.19569  ? 205 HIS A CD2   1 
ATOM   1546 C  CE1   . HIS A 1 239 ? -49.70800 2.95000   -40.71700 1.000 47.63351  ? 205 HIS A CE1   1 
ATOM   1547 N  NE2   . HIS A 1 239 ? -49.32500 2.05500   -39.82500 1.000 44.99861  ? 205 HIS A NE2   1 
ATOM   1548 N  N     . GLY A 1 240 ? -43.26300 5.07400   -39.90600 1.000 34.47562  ? 206 GLY A N     1 
ATOM   1549 C  CA    . GLY A 1 240 ? -42.14200 5.94900   -39.63200 1.000 33.39732  ? 206 GLY A CA    1 
ATOM   1550 C  C     . GLY A 1 240 ? -41.71900 5.91000   -38.17200 1.000 37.70329  ? 206 GLY A C     1 
ATOM   1551 O  O     . GLY A 1 240 ? -42.35500 5.29700   -37.31300 1.000 35.89087  ? 206 GLY A O     1 
ATOM   1552 N  N     . VAL A 1 241 ? -40.60700 6.59700   -37.91300 1.000 30.39971  ? 207 VAL A N     1 
ATOM   1553 C  CA    . VAL A 1 241 ? -40.02100 6.73100   -36.58400 1.000 28.03908  ? 207 VAL A CA    1 
ATOM   1554 C  C     . VAL A 1 241 ? -40.02200 8.20700   -36.21400 1.000 30.31003  ? 207 VAL A C     1 
ATOM   1555 O  O     . VAL A 1 241 ? -39.52100 9.04000   -36.97600 1.000 31.30432  ? 207 VAL A O     1 
ATOM   1556 C  CB    . VAL A 1 241 ? -38.59100 6.16000   -36.53500 1.000 32.84892  ? 207 VAL A CB    1 
ATOM   1557 C  CG1   . VAL A 1 241 ? -38.01000 6.28400   -35.11900 1.000 27.41564  ? 207 VAL A CG1   1 
ATOM   1558 C  CG2   . VAL A 1 241 ? -38.58300 4.71500   -36.99200 1.000 41.49074  ? 207 VAL A CG2   1 
ATOM   1559 N  N     . ILE A 1 242 ? -40.58800 8.53100   -35.05500 1.000 29.17330  ? 208 ILE A N     1 
ATOM   1560 C  CA    . ILE A 1 242 ? -40.58000 9.89800   -34.54500 1.000 29.15782  ? 208 ILE A CA    1 
ATOM   1561 C  C     . ILE A 1 242 ? -39.27300 10.11700  -33.79600 1.000 30.55147  ? 208 ILE A C     1 
ATOM   1562 O  O     . ILE A 1 242 ? -38.96700 9.39200   -32.84100 1.000 30.26409  ? 208 ILE A O     1 
ATOM   1563 C  CB    . ILE A 1 242 ? -41.78800 10.15900  -33.63800 1.000 40.09117  ? 208 ILE A CB    1 
ATOM   1564 C  CG1   . ILE A 1 242 ? -43.09100 9.89700   -34.39700 1.000 37.42047  ? 208 ILE A CG1   1 
ATOM   1565 C  CG2   . ILE A 1 242 ? -41.75900 11.58800  -33.10700 1.000 29.64918  ? 208 ILE A CG2   1 
ATOM   1566 C  CD1   . ILE A 1 242 ? -44.32000 9.92500   -33.50000 1.000 31.36044  ? 208 ILE A CD1   1 
ATOM   1567 N  N     . VAL A 1 243 ? -38.50400 11.11900  -34.22000 1.000 25.52715  ? 209 VAL A N     1 
ATOM   1568 C  CA    . VAL A 1 243 ? -37.15200 11.34400  -33.71800 1.000 29.90671  ? 209 VAL A CA    1 
ATOM   1569 C  C     . VAL A 1 243 ? -37.11500 12.68400  -33.00000 1.000 35.62395  ? 209 VAL A C     1 
ATOM   1570 O  O     . VAL A 1 243 ? -37.49200 13.71200  -33.57400 1.000 30.90344  ? 209 VAL A O     1 
ATOM   1571 C  CB    . VAL A 1 243 ? -36.11000 11.29200  -34.85200 1.000 32.56628  ? 209 VAL A CB    1 
ATOM   1572 C  CG1   . VAL A 1 243 ? -34.75900 11.79900  -34.37800 1.000 26.97676  ? 209 VAL A CG1   1 
ATOM   1573 C  CG2   . VAL A 1 243 ? -35.97900 9.86600   -35.38900 1.000 23.93757  ? 209 VAL A CG2   1 
ATOM   1574 N  N     . ASN A 1 244 ? -36.66300 12.66900  -31.74200 1.000 28.48532  ? 210 ASN A N     1 
ATOM   1575 C  CA    . ASN A 1 244 ? -36.52600 13.88900  -30.94600 1.000 28.10543  ? 210 ASN A CA    1 
ATOM   1576 C  C     . ASN A 1 244 ? -35.21200 14.59700  -31.29100 1.000 30.71954  ? 210 ASN A C     1 
ATOM   1577 O  O     . ASN A 1 244 ? -34.24800 14.62100  -30.52300 1.000 29.41463  ? 210 ASN A O     1 
ATOM   1578 C  CB    . ASN A 1 244 ? -36.60300 13.57300  -29.46000 1.000 27.01181  ? 210 ASN A CB    1 
ATOM   1579 C  CG    . ASN A 1 244 ? -36.55000 14.81700  -28.61200 1.000 31.07560  ? 210 ASN A CG    1 
ATOM   1580 O  OD1   . ASN A 1 244 ? -37.04400 15.86800  -29.02200 1.000 28.84012  ? 210 ASN A OD1   1 
ATOM   1581 N  ND2   . ASN A 1 244 ? -35.91500 14.72400  -27.44000 1.000 29.07641  ? 210 ASN A ND2   1 
ATOM   1582 N  N     . SER A 1 245 ? -35.20200 15.20100  -32.47500 1.000 26.91622  ? 211 SER A N     1 
ATOM   1583 C  CA    . SER A 1 245 ? -34.07800 15.98900  -32.96900 1.000 29.90649  ? 211 SER A CA    1 
ATOM   1584 C  C     . SER A 1 245 ? -34.60300 16.87200  -34.09700 1.000 26.32127  ? 211 SER A C     1 
ATOM   1585 O  O     . SER A 1 245 ? -35.80000 16.87300  -34.39300 1.000 27.06000  ? 211 SER A O     1 
ATOM   1586 C  CB    . SER A 1 245 ? -32.92800 15.09200  -33.44200 1.000 28.09698  ? 211 SER A CB    1 
ATOM   1587 O  OG    . SER A 1 245 ? -31.76500 15.85600  -33.71100 1.000 29.39934  ? 211 SER A OG    1 
ATOM   1588 N  N     . PHE A 1 246 ? -33.70600 17.63400  -34.72200 1.000 27.80176  ? 212 PHE A N     1 
ATOM   1589 C  CA    . PHE A 1 246 ? -34.08300 18.46600  -35.85700 1.000 28.19611  ? 212 PHE A CA    1 
ATOM   1590 C  C     . PHE A 1 246 ? -33.20500 18.14800  -37.06300 1.000 31.87139  ? 212 PHE A C     1 
ATOM   1591 O  O     . PHE A 1 246 ? -32.09100 17.62900  -36.93600 1.000 27.93518  ? 212 PHE A O     1 
ATOM   1592 C  CB    . PHE A 1 246 ? -34.04100 19.97400  -35.51500 1.000 26.75822  ? 212 PHE A CB    1 
ATOM   1593 C  CG    . PHE A 1 246 ? -32.72100 20.46900  -34.96500 1.000 27.45734  ? 212 PHE A CG    1 
ATOM   1594 C  CD1   . PHE A 1 246 ? -32.33500 20.17400  -33.66300 1.000 27.35479  ? 212 PHE A CD1   1 
ATOM   1595 C  CD2   . PHE A 1 246 ? -31.89800 21.28800  -35.73700 1.000 28.82694  ? 212 PHE A CD2   1 
ATOM   1596 C  CE1   . PHE A 1 246 ? -31.13600 20.65100  -33.14500 1.000 25.70024  ? 212 PHE A CE1   1 
ATOM   1597 C  CE2   . PHE A 1 246 ? -30.69700 21.77000  -35.22800 1.000 36.70219  ? 212 PHE A CE2   1 
ATOM   1598 C  CZ    . PHE A 1 246 ? -30.31600 21.45100  -33.92100 1.000 29.06989  ? 212 PHE A CZ    1 
ATOM   1599 N  N     . ALA A 1 247 ? -33.74900 18.45500  -38.24800 1.000 27.55258  ? 213 ALA A N     1 
ATOM   1600 C  CA    . ALA A 1 247 ? -33.17800 17.96900  -39.50500 1.000 32.05775  ? 213 ALA A CA    1 
ATOM   1601 C  C     . ALA A 1 247 ? -31.73100 18.40600  -39.68500 1.000 29.43609  ? 213 ALA A C     1 
ATOM   1602 O  O     . ALA A 1 247 ? -30.88900 17.62000  -40.14000 1.000 27.92867  ? 213 ALA A O     1 
ATOM   1603 C  CB    . ALA A 1 247 ? -34.01900 18.46000  -40.68600 1.000 30.77691  ? 213 ALA A CB    1 
ATOM   1604 N  N     . GLU A 1 248 ? -31.42800 19.66300  -39.35200 1.000 34.31779  ? 214 GLU A N     1 
ATOM   1605 C  CA    . GLU A 1 248 ? -30.08100 20.19200  -39.54300 1.000 32.82878  ? 214 GLU A CA    1 
ATOM   1606 C  C     . GLU A 1 248 ? -29.04600 19.42200  -38.72500 1.000 36.02686  ? 214 GLU A C     1 
ATOM   1607 O  O     . GLU A 1 248 ? -27.92500 19.18700  -39.19200 1.000 34.19074  ? 214 GLU A O     1 
ATOM   1608 C  CB    . GLU A 1 248 ? -30.05800 21.67400  -39.17100 1.000 42.82597  ? 214 GLU A CB    1 
ATOM   1609 C  CG    . GLU A 1 248 ? -28.67200 22.28900  -39.15100 1.000 53.08722  ? 214 GLU A CG    1 
ATOM   1610 C  CD    . GLU A 1 248 ? -28.05600 22.38000  -40.53500 1.000 66.72120  ? 214 GLU A CD    1 
ATOM   1611 O  OE1   . GLU A 1 248 ? -28.73500 22.88700  -41.45600 1.000 64.41779  ? 214 GLU A OE1   1 
ATOM   1612 O  OE2   . GLU A 1 248 ? -26.89700 21.93900  -40.70000 1.000 71.66891  ? 214 GLU A OE2   1 
ATOM   1613 N  N     . LEU A 1 249 ? -29.39300 19.03600  -37.49400 1.000 28.16540  ? 215 LEU A N     1 
ATOM   1614 C  CA    . LEU A 1 249 ? -28.45400 18.28000  -36.66700 1.000 30.32526  ? 215 LEU A CA    1 
ATOM   1615 C  C     . LEU A 1 249 ? -28.24700 16.86800  -37.21000 1.000 26.60166  ? 215 LEU A C     1 
ATOM   1616 O  O     . LEU A 1 249 ? -27.11900 16.36100  -37.22800 1.000 25.85886  ? 215 LEU A O     1 
ATOM   1617 C  CB    . LEU A 1 249 ? -28.94800 18.24100  -35.21500 1.000 24.66087  ? 215 LEU A CB    1 
ATOM   1618 C  CG    . LEU A 1 249 ? -27.92100 17.93500  -34.11800 1.000 28.56141  ? 215 LEU A CG    1 
ATOM   1619 C  CD1   . LEU A 1 249 ? -26.91600 19.06600  -33.96700 1.000 27.80825  ? 215 LEU A CD1   1 
ATOM   1620 C  CD2   . LEU A 1 249 ? -28.61300 17.63600  -32.78600 1.000 29.61588  ? 215 LEU A CD2   1 
ATOM   1621 N  N     . ASP A 1 250 ? -29.31600 16.22300  -37.67200 1.000 25.48748  ? 216 ASP A N     1 
ATOM   1622 C  CA    . ASP A 1 250 ? -29.25700 14.85100  -38.16000 1.000 24.24525  ? 216 ASP A CA    1 
ATOM   1623 C  C     . ASP A 1 250 ? -28.94000 14.74800  -39.64900 1.000 28.11074  ? 216 ASP A C     1 
ATOM   1624 O  O     . ASP A 1 250 ? -28.94800 13.63600  -40.18900 1.000 29.04367  ? 216 ASP A O     1 
ATOM   1625 C  CB    . ASP A 1 250 ? -30.58300 14.13800  -37.88000 1.000 26.84829  ? 216 ASP A CB    1 
ATOM   1626 C  CG    . ASP A 1 250 ? -30.81600 13.88000  -36.39600 1.000 30.59980  ? 216 ASP A CG    1 
ATOM   1627 O  OD1   . ASP A 1 250 ? -30.05500 14.41100  -35.55700 1.000 27.09873  ? 216 ASP A OD1   1 
ATOM   1628 O  OD2   . ASP A 1 250 ? -31.76000 13.12400  -36.07700 1.000 27.31826  ? 216 ASP A OD2   1 
ATOM   1629 N  N     . GLU A 1 251 ? -28.66600 15.87200  -40.31700 1.000 28.99595  ? 217 GLU A N     1 
ATOM   1630 C  CA    . GLU A 1 251 ? -28.53500 15.88600  -41.77300 1.000 26.26584  ? 217 GLU A CA    1 
ATOM   1631 C  C     . GLU A 1 251 ? -27.49400 14.87700  -42.23700 1.000 30.93057  ? 217 GLU A C     1 
ATOM   1632 O  O     . GLU A 1 251 ? -26.40200 14.79000  -41.67000 1.000 30.58373  ? 217 GLU A O     1 
ATOM   1633 C  CB    . GLU A 1 251 ? -28.16200 17.29200  -42.25600 1.000 25.16602  ? 217 GLU A CB    1 
ATOM   1634 C  CG    . GLU A 1 251 ? -27.94500 17.39700  -43.76800 1.000 36.13157  ? 217 GLU A CG    1 
ATOM   1635 C  CD    . GLU A 1 251 ? -28.13300 18.81100  -44.29100 1.000 51.92190  ? 217 GLU A CD    1 
ATOM   1636 O  OE1   . GLU A 1 251 ? -27.45300 19.73400  -43.78700 1.000 48.34822  ? 217 GLU A OE1   1 
ATOM   1637 O  OE2   . GLU A 1 251 ? -28.97200 19.00100  -45.19800 1.000 50.04414  ? 217 GLU A OE2   1 
ATOM   1638 N  N     . GLY A 1 252 ? -27.83900 14.11000  -43.26700 1.000 30.06175  ? 218 GLY A N     1 
ATOM   1639 C  CA    . GLY A 1 252 ? -26.99900 13.02300  -43.75000 1.000 27.11255  ? 218 GLY A CA    1 
ATOM   1640 C  C     . GLY A 1 252 ? -27.27400 11.70000  -43.05900 1.000 34.94338  ? 218 GLY A C     1 
ATOM   1641 O  O     . GLY A 1 252 ? -27.31200 10.65200  -43.70600 1.000 33.05456  ? 218 GLY A O     1 
ATOM   1642 N  N     . TYR A 1 253 ? -27.47000 11.73400  -41.74200 1.000 25.88798  ? 219 TYR A N     1 
ATOM   1643 C  CA    . TYR A 1 253 ? -27.78400 10.51000  -41.01900 1.000 27.65146  ? 219 TYR A CA    1 
ATOM   1644 C  C     . TYR A 1 253 ? -29.25200 10.14300  -41.16500 1.000 26.18081  ? 219 TYR A C     1 
ATOM   1645 O  O     . TYR A 1 253 ? -29.59000 8.95300   -41.18600 1.000 26.40836  ? 219 TYR A O     1 
ATOM   1646 C  CB    . TYR A 1 253 ? -27.34300 10.66300  -39.55100 1.000 27.38228  ? 219 TYR A CB    1 
ATOM   1647 C  CG    . TYR A 1 253 ? -25.84500 10.86800  -39.52100 1.000 27.98649  ? 219 TYR A CG    1 
ATOM   1648 C  CD1   . TYR A 1 253 ? -24.98300 9.78000   -39.50700 1.000 21.00250  ? 219 TYR A CD1   1 
ATOM   1649 C  CD2   . TYR A 1 253 ? -25.29300 12.14400  -39.62400 1.000 23.58160  ? 219 TYR A CD2   1 
ATOM   1650 C  CE1   . TYR A 1 253 ? -23.61300 9.95200   -39.54400 1.000 20.98467  ? 219 TYR A CE1   1 
ATOM   1651 C  CE2   . TYR A 1 253 ? -23.92500 12.32700  -39.66900 1.000 29.38490  ? 219 TYR A CE2   1 
ATOM   1652 C  CZ    . TYR A 1 253 ? -23.09100 11.22800  -39.62800 1.000 22.87994  ? 219 TYR A CZ    1 
ATOM   1653 O  OH    . TYR A 1 253 ? -21.73200 11.41600  -39.66900 1.000 28.98579  ? 219 TYR A OH    1 
ATOM   1654 N  N     . THR A 1 254 ? -30.12500 11.14500  -41.30100 1.000 23.91201  ? 220 THR A N     1 
ATOM   1655 C  CA    . THR A 1 254 ? -31.51200 10.88600  -41.67800 1.000 27.89422  ? 220 THR A CA    1 
ATOM   1656 C  C     . THR A 1 254 ? -31.58300 10.02300  -42.93000 1.000 30.34434  ? 220 THR A C     1 
ATOM   1657 O  O     . THR A 1 254 ? -32.27100 8.99500   -42.96000 1.000 29.31914  ? 220 THR A O     1 
ATOM   1658 C  CB    . THR A 1 254 ? -32.24500 12.20700  -41.90800 1.000 29.68658  ? 220 THR A CB    1 
ATOM   1659 O  OG1   . THR A 1 254 ? -32.07500 13.05100  -40.76500 1.000 36.98171  ? 220 THR A OG1   1 
ATOM   1660 C  CG2   . THR A 1 254 ? -33.73000 11.96700  -42.14800 1.000 29.92569  ? 220 THR A CG2   1 
ATOM   1661 N  N     . GLU A 1 255 ? -30.85700 10.42900  -43.97600 1.000 32.89322  ? 221 GLU A N     1 
ATOM   1662 C  CA    . GLU A 1 255 ? -30.91100 9.72400   -45.25200 1.000 30.16926  ? 221 GLU A CA    1 
ATOM   1663 C  C     . GLU A 1 255 ? -30.21700 8.37200   -45.16500 1.000 32.04077  ? 221 GLU A C     1 
ATOM   1664 O  O     . GLU A 1 255 ? -30.69800 7.38100   -45.72900 1.000 27.18558  ? 221 GLU A O     1 
ATOM   1665 C  CB    . GLU A 1 255 ? -30.28000 10.58900  -46.34700 1.000 29.84723  ? 221 GLU A CB    1 
ATOM   1666 C  CG    . GLU A 1 255 ? -31.05900 11.85900  -46.64900 1.000 25.76035  ? 221 GLU A CG    1 
ATOM   1667 C  CD    . GLU A 1 255 ? -30.63200 13.03300  -45.78500 1.000 31.49203  ? 221 GLU A CD    1 
ATOM   1668 O  OE1   . GLU A 1 255 ? -29.87700 12.82400  -44.81800 1.000 38.02489  ? 221 GLU A OE1   1 
ATOM   1669 O  OE2   . GLU A 1 255 ? -31.06300 14.16900  -46.06300 1.000 35.87982  ? 221 GLU A OE2   1 
ATOM   1670 N  N     . TYR A 1 256 ? -29.08000 8.31400   -44.46900 1.000 24.78772  ? 222 TYR A N     1 
ATOM   1671 C  CA    . TYR A 1 256 ? -28.43000 7.03400   -44.21000 1.000 31.43912  ? 222 TYR A CA    1 
ATOM   1672 C  C     . TYR A 1 256 ? -29.40500 6.04900   -43.57600 1.000 34.72506  ? 222 TYR A C     1 
ATOM   1673 O  O     . TYR A 1 256 ? -29.48600 4.88300   -43.98100 1.000 31.33021  ? 222 TYR A O     1 
ATOM   1674 C  CB    . TYR A 1 256 ? -27.21600 7.24200   -43.30100 1.000 34.09984  ? 222 TYR A CB    1 
ATOM   1675 C  CG    . TYR A 1 256 ? -26.41400 5.98500   -43.05100 1.000 32.99371  ? 222 TYR A CG    1 
ATOM   1676 C  CD1   . TYR A 1 256 ? -26.75200 5.10800   -42.02400 1.000 29.68515  ? 222 TYR A CD1   1 
ATOM   1677 C  CD2   . TYR A 1 256 ? -25.31600 5.67600   -43.84300 1.000 31.08653  ? 222 TYR A CD2   1 
ATOM   1678 C  CE1   . TYR A 1 256 ? -26.01800 3.96000   -41.79600 1.000 32.97796  ? 222 TYR A CE1   1 
ATOM   1679 C  CE2   . TYR A 1 256 ? -24.57400 4.53100   -43.62500 1.000 31.11013  ? 222 TYR A CE2   1 
ATOM   1680 C  CZ    . TYR A 1 256 ? -24.92700 3.67800   -42.60500 1.000 38.52901  ? 222 TYR A CZ    1 
ATOM   1681 O  OH    . TYR A 1 256 ? -24.18300 2.54400   -42.39200 1.000 40.09332  ? 222 TYR A OH    1 
ATOM   1682 N  N     . TYR A 1 257 ? -30.16400 6.51300   -42.57900 1.000 30.76236  ? 223 TYR A N     1 
ATOM   1683 C  CA    . TYR A 1 257 ? -31.07800 5.63200   -41.85800 1.000 31.32693  ? 223 TYR A CA    1 
ATOM   1684 C  C     . TYR A 1 257 ? -32.25400 5.22000   -42.73100 1.000 26.46734  ? 223 TYR A C     1 
ATOM   1685 O  O     . TYR A 1 257 ? -32.64100 4.04700   -42.75300 1.000 31.18035  ? 223 TYR A O     1 
ATOM   1686 C  CB    . TYR A 1 257 ? -31.58400 6.32000   -40.59000 1.000 28.06820  ? 223 TYR A CB    1 
ATOM   1687 C  CG    . TYR A 1 257 ? -32.62800 5.51000   -39.85800 1.000 28.80272  ? 223 TYR A CG    1 
ATOM   1688 C  CD1   . TYR A 1 257 ? -32.25600 4.51700   -38.95300 1.000 29.52973  ? 223 TYR A CD1   1 
ATOM   1689 C  CD2   . TYR A 1 257 ? -33.98600 5.72900   -40.07400 1.000 26.73697  ? 223 TYR A CD2   1 
ATOM   1690 C  CE1   . TYR A 1 257 ? -33.20900 3.76800   -38.27700 1.000 34.44074  ? 223 TYR A CE1   1 
ATOM   1691 C  CE2   . TYR A 1 257 ? -34.94500 4.98200   -39.41200 1.000 32.76670  ? 223 TYR A CE2   1 
ATOM   1692 C  CZ    . TYR A 1 257 ? -34.54900 4.00300   -38.51200 1.000 36.34797  ? 223 TYR A CZ    1 
ATOM   1693 O  OH    . TYR A 1 257 ? -35.49900 3.26100   -37.84900 1.000 35.68231  ? 223 TYR A OH    1 
ATOM   1694 N  N     . GLU A 1 258 ? -32.86600 6.18300   -43.42000 1.000 26.54983  ? 224 GLU A N     1 
ATOM   1695 C  CA    . GLU A 1 258 ? -33.98400 5.86100   -44.30100 1.000 38.13653  ? 224 GLU A CA    1 
ATOM   1696 C  C     . GLU A 1 258 ? -33.55400 4.91400   -45.41300 1.000 37.03330  ? 224 GLU A C     1 
ATOM   1697 O  O     . GLU A 1 258 ? -34.27900 3.97300   -45.75100 1.000 31.69442  ? 224 GLU A O     1 
ATOM   1698 C  CB    . GLU A 1 258 ? -34.57800 7.14400   -44.87500 1.000 33.77722  ? 224 GLU A CB    1 
ATOM   1699 C  CG    . GLU A 1 258 ? -35.28000 7.97100   -43.80600 1.000 32.05083  ? 224 GLU A CG    1 
ATOM   1700 C  CD    . GLU A 1 258 ? -35.89600 9.24400   -44.34500 1.000 35.73623  ? 224 GLU A CD    1 
ATOM   1701 O  OE1   . GLU A 1 258 ? -35.66100 9.57100   -45.52800 1.000 45.08564  ? 224 GLU A OE1   1 
ATOM   1702 O  OE2   . GLU A 1 258 ? -36.62000 9.91900   -43.58400 1.000 35.50769  ? 224 GLU A OE2   1 
ATOM   1703 N  N     . ASN A 1 259 ? -32.36700 5.13000   -45.97900 1.000 31.79434  ? 225 ASN A N     1 
ATOM   1704 C  CA    . ASN A 1 259 ? -31.87000 4.20900   -46.99600 1.000 31.20925  ? 225 ASN A CA    1 
ATOM   1705 C  C     . ASN A 1 259 ? -31.62400 2.82100   -46.41400 1.000 36.72942  ? 225 ASN A C     1 
ATOM   1706 O  O     . ASN A 1 259 ? -31.89000 1.81000   -47.07200 1.000 40.96456  ? 225 ASN A O     1 
ATOM   1707 C  CB    . ASN A 1 259 ? -30.59400 4.76800   -47.62600 1.000 39.10173  ? 225 ASN A CB    1 
ATOM   1708 C  CG    . ASN A 1 259 ? -29.89400 3.76400   -48.51900 1.000 56.68449  ? 225 ASN A CG    1 
ATOM   1709 O  OD1   . ASN A 1 259 ? -28.98900 3.05100   -48.08400 1.000 57.99732  ? 225 ASN A OD1   1 
ATOM   1710 N  ND2   . ASN A 1 259 ? -30.31200 3.70200   -49.78000 1.000 64.83335  ? 225 ASN A ND2   1 
ATOM   1711 N  N     . LEU A 1 260 ? -31.13100 2.75200   -45.17600 1.000 35.26533  ? 226 LEU A N     1 
ATOM   1712 C  CA    . LEU A 1 260 ? -30.79400 1.46300   -44.58100 1.000 35.83533  ? 226 LEU A CA    1 
ATOM   1713 C  C     . LEU A 1 260 ? -32.04300 0.68200   -44.18900 1.000 38.36743  ? 226 LEU A C     1 
ATOM   1714 O  O     . LEU A 1 260 ? -32.14300 -0.52200  -44.45200 1.000 39.66200  ? 226 LEU A O     1 
ATOM   1715 C  CB    . LEU A 1 260 ? -29.89800 1.66700   -43.35900 1.000 34.73046  ? 226 LEU A CB    1 
ATOM   1716 C  CG    . LEU A 1 260 ? -29.74600 0.41200   -42.49800 1.000 44.85642  ? 226 LEU A CG    1 
ATOM   1717 C  CD1   . LEU A 1 260 ? -28.89400 -0.62400  -43.22000 1.000 41.65073  ? 226 LEU A CD1   1 
ATOM   1718 C  CD2   . LEU A 1 260 ? -29.16300 0.74900   -41.14000 1.000 37.95945  ? 226 LEU A CD2   1 
ATOM   1719 N  N     . THR A 1 261 ? -33.00100 1.34400   -43.53900 1.000 37.85485  ? 227 THR A N     1 
ATOM   1720 C  CA    . THR A 1 261 ? -34.16100 0.65200   -42.99500 1.000 38.95143  ? 227 THR A CA    1 
ATOM   1721 C  C     . THR A 1 261 ? -35.41000 0.77400   -43.85300 1.000 38.80128  ? 227 THR A C     1 
ATOM   1722 O  O     . THR A 1 261 ? -36.34600 -0.01000  -43.66600 1.000 36.32832  ? 227 THR A O     1 
ATOM   1723 C  CB    . THR A 1 261 ? -34.48800 1.17800   -41.59300 1.000 30.63921  ? 227 THR A CB    1 
ATOM   1724 O  OG1   . THR A 1 261 ? -34.99800 2.51600   -41.69000 1.000 33.91218  ? 227 THR A OG1   1 
ATOM   1725 C  CG2   . THR A 1 261 ? -33.24600 1.16200   -40.71200 1.000 36.60878  ? 227 THR A CG2   1 
ATOM   1726 N  N     . GLY A 1 262 ? -35.45800 1.73700   -44.76700 1.000 36.40216  ? 228 GLY A N     1 
ATOM   1727 C  CA    . GLY A 1 262 ? -36.67600 1.98800   -45.50500 1.000 34.57757  ? 228 GLY A CA    1 
ATOM   1728 C  C     . GLY A 1 262 ? -37.74200 2.71600   -44.72700 1.000 42.12690  ? 228 GLY A C     1 
ATOM   1729 O  O     . GLY A 1 262 ? -38.85000 2.88600   -45.24400 1.000 45.67240  ? 228 GLY A O     1 
ATOM   1730 N  N     . ARG A 1 263 ? -37.43900 3.16700   -43.50800 1.000 29.36383  ? 229 ARG A N     1 
ATOM   1731 C  CA    . ARG A 1 263 ? -38.43200 3.75100   -42.61700 1.000 27.88729  ? 229 ARG A CA    1 
ATOM   1732 C  C     . ARG A 1 263 ? -38.31400 5.27100   -42.59200 1.000 32.08055  ? 229 ARG A C     1 
ATOM   1733 O  O     . ARG A 1 263 ? -37.21400 5.81300   -42.45000 1.000 37.13156  ? 229 ARG A O     1 
ATOM   1734 C  CB    . ARG A 1 263 ? -38.27700 3.18100   -41.20400 1.000 37.52922  ? 229 ARG A CB    1 
ATOM   1735 C  CG    . ARG A 1 263 ? -38.16600 1.65900   -41.19300 1.000 50.83887  ? 229 ARG A CG    1 
ATOM   1736 C  CD    . ARG A 1 263 ? -37.71800 1.10200   -39.84800 1.000 56.70339  ? 229 ARG A CD    1 
ATOM   1737 N  NE    . ARG A 1 263 ? -38.61200 1.48000   -38.76200 1.000 44.47191  ? 229 ARG A NE    1 
ATOM   1738 C  CZ    . ARG A 1 263 ? -38.55500 0.96000   -37.54600 1.000 60.52543  ? 229 ARG A CZ    1 
ATOM   1739 N  NH1   . ARG A 1 263 ? -37.66200 0.03500   -37.23300 1.000 59.85040  ? 229 ARG A NH1   1 
ATOM   1740 N  NH2   . ARG A 1 263 ? -39.41700 1.37600   -36.62100 1.000 62.41317  ? 229 ARG A NH2   1 
ATOM   1741 N  N     . LYS A 1 264 ? -39.45600 5.94800   -42.71100 1.000 37.01763  ? 230 LYS A N     1 
ATOM   1742 C  CA    . LYS A 1 264 ? -39.51000 7.40400   -42.67400 1.000 36.88067  ? 230 LYS A CA    1 
ATOM   1743 C  C     . LYS A 1 264 ? -39.10900 7.93900   -41.30200 1.000 38.45062  ? 230 LYS A C     1 
ATOM   1744 O  O     . LYS A 1 264 ? -39.50100 7.39500   -40.26700 1.000 28.34114  ? 230 LYS A O     1 
ATOM   1745 C  CB    . LYS A 1 264 ? -40.92700 7.87300   -43.01500 1.000 36.13915  ? 230 LYS A CB    1 
ATOM   1746 C  CG    . LYS A 1 264 ? -41.22800 9.33300   -42.68100 1.000 36.33068  ? 230 LYS A CG    1 
ATOM   1747 C  CD    . LYS A 1 264 ? -40.61500 10.25800  -43.72200 1.000 34.31193  ? 230 LYS A CD    1 
ATOM   1748 C  CE    . LYS A 1 264 ? -41.08700 11.69400  -43.56100 1.000 36.32481  ? 230 LYS A CE    1 
ATOM   1749 N  NZ    . LYS A 1 264 ? -40.24900 12.62600  -44.36500 1.000 37.27485  ? 230 LYS A NZ    1 
ATOM   1750 N  N     . VAL A 1 265 ? -38.34200 9.02800   -41.29900 1.000 30.38158  ? 231 VAL A N     1 
ATOM   1751 C  CA    . VAL A 1 265 ? -37.96700 9.74100   -40.08300 1.000 34.76583  ? 231 VAL A CA    1 
ATOM   1752 C  C     . VAL A 1 265 ? -38.82100 11.00100  -39.96700 1.000 32.20803  ? 231 VAL A C     1 
ATOM   1753 O  O     . VAL A 1 265 ? -38.87100 11.80900  -40.90300 1.000 33.04919  ? 231 VAL A O     1 
ATOM   1754 C  CB    . VAL A 1 265 ? -36.46900 10.09500  -40.08700 1.000 37.75546  ? 231 VAL A CB    1 
ATOM   1755 C  CG1   . VAL A 1 265 ? -36.13500 11.00300  -38.90800 1.000 36.02398  ? 231 VAL A CG1   1 
ATOM   1756 C  CG2   . VAL A 1 265 ? -35.62400 8.83000   -40.05400 1.000 29.39282  ? 231 VAL A CG2   1 
ATOM   1757 N  N     . TRP A 1 266 ? -39.49500 11.16500  -38.82200 1.000 29.07532  ? 232 TRP A N     1 
ATOM   1758 C  CA    . TRP A 1 266 ? -40.23500 12.38800  -38.49200 1.000 31.26126  ? 232 TRP A CA    1 
ATOM   1759 C  C     . TRP A 1 266 ? -39.44300 13.14200  -37.42600 1.000 35.36730  ? 232 TRP A C     1 
ATOM   1760 O  O     . TRP A 1 266 ? -39.44400 12.74900  -36.25400 1.000 29.50864  ? 232 TRP A O     1 
ATOM   1761 C  CB    . TRP A 1 266 ? -41.64800 12.08900  -37.98300 1.000 28.16972  ? 232 TRP A CB    1 
ATOM   1762 C  CG    . TRP A 1 266 ? -42.50300 11.20100  -38.85700 1.000 33.44393  ? 232 TRP A CG    1 
ATOM   1763 C  CD1   . TRP A 1 266 ? -42.67500 9.85000   -38.73600 1.000 31.17587  ? 232 TRP A CD1   1 
ATOM   1764 C  CD2   . TRP A 1 266 ? -43.32800 11.61200  -39.96100 1.000 28.57767  ? 232 TRP A CD2   1 
ATOM   1765 N  NE1   . TRP A 1 266 ? -43.54300 9.39300   -39.70600 1.000 32.53383  ? 232 TRP A NE1   1 
ATOM   1766 C  CE2   . TRP A 1 266 ? -43.96300 10.45500  -40.46400 1.000 30.59569  ? 232 TRP A CE2   1 
ATOM   1767 C  CE3   . TRP A 1 266 ? -43.58800 12.84500  -40.57200 1.000 31.12530  ? 232 TRP A CE3   1 
ATOM   1768 C  CZ2   . TRP A 1 266 ? -44.83600 10.49300  -41.55600 1.000 37.70568  ? 232 TRP A CZ2   1 
ATOM   1769 C  CZ3   . TRP A 1 266 ? -44.45800 12.88200  -41.66100 1.000 32.84377  ? 232 TRP A CZ3   1 
ATOM   1770 C  CH2   . TRP A 1 266 ? -45.07200 11.71300  -42.13800 1.000 35.89933  ? 232 TRP A CH2   1 
ATOM   1771 N  N     . HIS A 1 267 ? -38.78200 14.23100  -37.82600 1.000 30.30653  ? 233 HIS A N     1 
ATOM   1772 C  CA    . HIS A 1 267 ? -38.03300 15.08200  -36.90000 1.000 33.42935  ? 233 HIS A CA    1 
ATOM   1773 C  C     . HIS A 1 267 ? -38.98100 16.12000  -36.31200 1.000 39.30561  ? 233 HIS A C     1 
ATOM   1774 O  O     . HIS A 1 267 ? -39.47700 16.99300  -37.03000 1.000 39.16637  ? 233 HIS A O     1 
ATOM   1775 C  CB    . HIS A 1 267 ? -36.86100 15.76400  -37.60400 1.000 23.29162  ? 233 HIS A CB    1 
ATOM   1776 C  CG    . HIS A 1 267 ? -35.64800 14.90000  -37.72500 1.000 32.59921  ? 233 HIS A CG    1 
ATOM   1777 N  ND1   . HIS A 1 267 ? -35.17300 14.45100  -38.93700 1.000 30.63559  ? 233 HIS A ND1   1 
ATOM   1778 C  CD2   . HIS A 1 267 ? -34.81800 14.39100  -36.78300 1.000 28.79198  ? 233 HIS A CD2   1 
ATOM   1779 C  CE1   . HIS A 1 267 ? -34.10100 13.70400  -38.73800 1.000 33.94366  ? 233 HIS A CE1   1 
ATOM   1780 N  NE2   . HIS A 1 267 ? -33.86600 13.65000  -37.43800 1.000 32.24747  ? 233 HIS A NE2   1 
ATOM   1781 N  N     . VAL A 1 268 ? -39.22300 16.03700  -35.00400 1.000 33.23773  ? 234 VAL A N     1 
ATOM   1782 C  CA    . VAL A 1 268 ? -40.18900 16.91300  -34.35000 1.000 37.07770  ? 234 VAL A CA    1 
ATOM   1783 C  C     . VAL A 1 268 ? -39.55900 17.57900  -33.13600 1.000 33.21736  ? 234 VAL A C     1 
ATOM   1784 O  O     . VAL A 1 268 ? -40.26300 18.14700  -32.29200 1.000 34.64852  ? 234 VAL A O     1 
ATOM   1785 C  CB    . VAL A 1 268 ? -41.45200 16.13400  -33.93600 1.000 33.92172  ? 234 VAL A CB    1 
ATOM   1786 C  CG1   . VAL A 1 268 ? -42.11400 15.49700  -35.15500 1.000 35.92289  ? 234 VAL A CG1   1 
ATOM   1787 C  CG2   . VAL A 1 268 ? -41.09800 15.09100  -32.90300 1.000 31.35683  ? 234 VAL A CG2   1 
ATOM   1788 N  N     . GLY A 1 269 ? -38.23300 17.53300  -33.04400 1.000 31.03957  ? 235 GLY A N     1 
ATOM   1789 C  CA    . GLY A 1 269 ? -37.55300 17.96900  -31.84700 1.000 29.27635  ? 235 GLY A CA    1 
ATOM   1790 C  C     . GLY A 1 269 ? -36.62600 19.15200  -32.04500 1.000 28.16692  ? 235 GLY A C     1 
ATOM   1791 O  O     . GLY A 1 269 ? -36.58800 19.77100  -33.11300 1.000 26.24154  ? 235 GLY A O     1 
ATOM   1792 N  N     . PRO A 1 270 ? -35.86900 19.50700  -30.99100 1.000 29.00455  ? 236 PRO A N     1 
ATOM   1793 C  CA    . PRO A 1 270 ? -35.90700 18.94000  -29.63200 1.000 26.17690  ? 236 PRO A CA    1 
ATOM   1794 C  C     . PRO A 1 270 ? -37.21300 19.33500  -28.96300 1.000 27.04146  ? 236 PRO A C     1 
ATOM   1795 O  O     . PRO A 1 270 ? -37.50900 20.52200  -28.88400 1.000 33.51611  ? 236 PRO A O     1 
ATOM   1796 C  CB    . PRO A 1 270 ? -34.68800 19.58000  -28.93800 1.000 28.28482  ? 236 PRO A CB    1 
ATOM   1797 C  CG    . PRO A 1 270 ? -33.85100 20.17700  -30.04500 1.000 29.81204  ? 236 PRO A CG    1 
ATOM   1798 C  CD    . PRO A 1 270 ? -34.84600 20.55800  -31.10500 1.000 28.27873  ? 236 PRO A CD    1 
ATOM   1799 N  N     . THR A 1 271 ? -38.02200 18.38600  -28.48900 1.000 29.89504  ? 237 THR A N     1 
ATOM   1800 C  CA    . THR A 1 271 ? -39.34000 18.74600  -27.97500 1.000 33.88921  ? 237 THR A CA    1 
ATOM   1801 C  C     . THR A 1 271 ? -39.26500 19.63400  -26.74100 1.000 37.22825  ? 237 THR A C     1 
ATOM   1802 O  O     . THR A 1 271 ? -40.23600 20.33700  -26.44300 1.000 38.87846  ? 237 THR A O     1 
ATOM   1803 C  CB    . THR A 1 271 ? -40.15400 17.49300  -27.66200 1.000 31.08801  ? 237 THR A CB    1 
ATOM   1804 O  OG1   . THR A 1 271 ? -39.47900 16.71900  -26.66200 1.000 34.23217  ? 237 THR A OG1   1 
ATOM   1805 C  CG2   . THR A 1 271 ? -40.33900 16.65800  -28.91600 1.000 29.10084  ? 237 THR A CG2   1 
ATOM   1806 N  N     . SER A 1 272 ? -38.13700 19.63200  -26.02000 1.000 34.63745  ? 238 SER A N     1 
ATOM   1807 C  CA    . SER A 1 272 ? -38.00500 20.53800  -24.88100 1.000 33.89315  ? 238 SER A CA    1 
ATOM   1808 C  C     . SER A 1 272 ? -37.94100 21.99100  -25.33400 1.000 34.40872  ? 238 SER A C     1 
ATOM   1809 O  O     . SER A 1 272 ? -38.35900 22.89100  -24.60000 1.000 39.56276  ? 238 SER A O     1 
ATOM   1810 C  CB    . SER A 1 272 ? -36.76500 20.18700  -24.05900 1.000 33.38551  ? 238 SER A CB    1 
ATOM   1811 O  OG    . SER A 1 272 ? -35.57800 20.39300  -24.80900 1.000 33.61210  ? 238 SER A OG    1 
ATOM   1812 N  N     . LEU A 1 273 ? -37.42200 22.24300  -26.53100 1.000 40.14604  ? 239 LEU A N     1 
ATOM   1813 C  CA    . LEU A 1 273 ? -37.45100 23.58800  -27.09000 1.000 40.69148  ? 239 LEU A CA    1 
ATOM   1814 C  C     . LEU A 1 273 ? -38.76900 23.89500  -27.78600 1.000 41.59900  ? 239 LEU A C     1 
ATOM   1815 O  O     . LEU A 1 273 ? -39.21600 25.04800  -27.76100 1.000 40.40065  ? 239 LEU A O     1 
ATOM   1816 C  CB    . LEU A 1 273 ? -36.29000 23.78200  -28.07000 1.000 24.12964  ? 239 LEU A CB    1 
ATOM   1817 C  CG    . LEU A 1 273 ? -34.89500 23.43000  -27.53000 1.000 37.80793  ? 239 LEU A CG    1 
ATOM   1818 C  CD1   . LEU A 1 273 ? -33.81800 23.77200  -28.54900 1.000 35.18125  ? 239 LEU A CD1   1 
ATOM   1819 C  CD2   . LEU A 1 273 ? -34.62900 24.12100  -26.20000 1.000 33.53383  ? 239 LEU A CD2   1 
ATOM   1820 N  N     . MET A 1 274 ? -39.40900 22.88400  -28.38500 1.000 32.49538  ? 240 MET A N     1 
ATOM   1821 C  CA    . MET A 1 274 ? -40.67300 23.10800  -29.08300 1.000 31.86551  ? 240 MET A CA    1 
ATOM   1822 C  C     . MET A 1 274 ? -41.76300 23.60500  -28.13900 1.000 43.71930  ? 240 MET A C     1 
ATOM   1823 O  O     . MET A 1 274 ? -42.58600 24.44300  -28.52400 1.000 41.82369  ? 240 MET A O     1 
ATOM   1824 C  CB    . MET A 1 274 ? -41.13000 21.82800  -29.78000 1.000 35.52386  ? 240 MET A CB    1 
ATOM   1825 C  CG    . MET A 1 274 ? -40.22800 21.34700  -30.89700 1.000 37.44818  ? 240 MET A CG    1 
ATOM   1826 S  SD    . MET A 1 274 ? -40.77000 21.88200  -32.53800 1.000 40.87332  ? 240 MET A SD    1 
ATOM   1827 C  CE    . MET A 1 274 ? -42.46000 21.28600  -32.59100 1.000 38.75218  ? 240 MET A CE    1 
ATOM   1828 N  N     . VAL A 1 275 ? -41.78300 23.11100  -26.90000 1.000 35.87245  ? 241 VAL A N     1 
ATOM   1829 C  CA    . VAL A 1 275 ? -42.84100 23.46200  -25.95700 1.000 36.82717  ? 241 VAL A CA    1 
ATOM   1830 C  C     . VAL A 1 275 ? -42.57000 24.83800  -25.36400 1.000 44.83834  ? 241 VAL A C     1 
ATOM   1831 O  O     . VAL A 1 275 ? -43.25800 25.27100  -24.43300 1.000 55.31516  ? 241 VAL A O     1 
ATOM   1832 C  CB    . VAL A 1 275 ? -42.98900 22.41300  -24.83700 1.000 41.08428  ? 241 VAL A CB    1 
ATOM   1833 C  CG1   . VAL A 1 275 ? -43.46700 21.08100  -25.40200 1.000 39.25836  ? 241 VAL A CG1   1 
ATOM   1834 C  CG2   . VAL A 1 275 ? -41.68600 22.25300  -24.06800 1.000 34.88892  ? 241 VAL A CG2   1 
ATOM   1835 N  N     . GLU A 1 276 ? -41.57000 25.53200  -25.89100 1.000 49.29149  ? 242 GLU A N     1 
ATOM   1836 C  CA    . GLU A 1 276 ? -41.31000 26.90400  -25.48600 1.000 58.48271  ? 242 GLU A CA    1 
ATOM   1837 C  C     . GLU A 1 276 ? -41.55600 27.86500  -26.64400 1.000 47.32940  ? 242 GLU A C     1 
ATOM   1838 O  O     . GLU A 1 276 ? -41.55100 29.08100  -26.46100 1.000 61.75411  ? 242 GLU A O     1 
ATOM   1839 C  CB    . GLU A 1 276 ? -39.88100 27.04500  -24.97300 1.000 53.13016  ? 242 GLU A CB    1 
ATOM   1840 C  CG    . GLU A 1 276 ? -39.66100 26.40400  -23.62000 1.000 69.72720  ? 242 GLU A CG    1 
ATOM   1841 C  CD    . GLU A 1 276 ? -38.28000 26.67600  -23.07600 1.000 75.32564  ? 242 GLU A CD    1 
ATOM   1842 O  OE1   . GLU A 1 276 ? -37.29600 26.39900  -23.79300 1.000 71.36631  ? 242 GLU A OE1   1 
ATOM   1843 O  OE2   . GLU A 1 276 ? -38.18000 27.17400  -21.93500 1.000 88.39429  ? 242 GLU A OE2   1 
ATOM   1844 N  N     . LYS A 1 294 ? -31.34200 35.20400  -5.87300  1.000 81.19880  ? 260 LYS A N     1 
ATOM   1845 C  CA    . LYS A 1 294 ? -30.28200 34.95900  -6.84500  1.000 74.36481  ? 260 LYS A CA    1 
ATOM   1846 C  C     . LYS A 1 294 ? -29.17400 34.08600  -6.26000  1.000 74.33521  ? 260 LYS A C     1 
ATOM   1847 O  O     . LYS A 1 294 ? -28.53100 34.45200  -5.27400  1.000 77.94292  ? 260 LYS A O     1 
ATOM   1848 C  CB    . LYS A 1 294 ? -29.69900 36.27900  -7.34400  1.000 79.03917  ? 260 LYS A CB    1 
ATOM   1849 C  CG    . LYS A 1 294 ? -28.76700 36.13400  -8.53600  1.000 75.02574  ? 260 LYS A CG    1 
ATOM   1850 C  CD    . LYS A 1 294 ? -28.48600 37.48400  -9.16900  1.000 73.66471  ? 260 LYS A CD    1 
ATOM   1851 C  CE    . LYS A 1 294 ? -27.76700 37.33500  -10.49800 1.000 70.03417  ? 260 LYS A CE    1 
ATOM   1852 N  NZ    . LYS A 1 294 ? -27.68100 38.63600  -11.22400 1.000 80.58618  ? 260 LYS A NZ    1 
ATOM   1853 N  N     . HIS A 1 295 ? -28.96000 32.93100  -6.88700  1.000 61.08162  ? 261 HIS A N     1 
ATOM   1854 C  CA    . HIS A 1 295 ? -27.94700 31.99000  -6.43100  1.000 63.27788  ? 261 HIS A CA    1 
ATOM   1855 C  C     . HIS A 1 295 ? -26.55600 32.61400  -6.50700  1.000 63.16194  ? 261 HIS A C     1 
ATOM   1856 O  O     . HIS A 1 295 ? -26.27600 33.46900  -7.35400  1.000 60.95543  ? 261 HIS A O     1 
ATOM   1857 C  CB    . HIS A 1 295 ? -28.01200 30.70900  -7.27300  1.000 61.40425  ? 261 HIS A CB    1 
ATOM   1858 C  CG    . HIS A 1 295 ? -27.27100 29.54900  -6.68200  1.000 71.02462  ? 261 HIS A CG    1 
ATOM   1859 N  ND1   . HIS A 1 295 ? -25.91100 29.37800  -6.82800  1.000 65.42650  ? 261 HIS A ND1   1 
ATOM   1860 C  CD2   . HIS A 1 295 ? -27.70200 28.50500  -5.93400  1.000 73.65341  ? 261 HIS A CD2   1 
ATOM   1861 C  CE1   . HIS A 1 295 ? -25.53600 28.27900  -6.19800  1.000 74.13959  ? 261 HIS A CE1   1 
ATOM   1862 N  NE2   . HIS A 1 295 ? -26.60400 27.73000  -5.64800  1.000 81.95448  ? 261 HIS A NE2   1 
ATOM   1863 N  N     . GLN A 1 296 ? -25.67600 32.17400  -5.60200  1.000 58.82549  ? 262 GLN A N     1 
ATOM   1864 C  CA    . GLN A 1 296 ? -24.32100 32.71300  -5.54400  1.000 54.64681  ? 262 GLN A CA    1 
ATOM   1865 C  C     . GLN A 1 296 ? -23.51600 32.42300  -6.80700  1.000 53.88491  ? 262 GLN A C     1 
ATOM   1866 O  O     . GLN A 1 296 ? -22.57400 33.16400  -7.10900  1.000 47.78538  ? 262 GLN A O     1 
ATOM   1867 C  CB    . GLN A 1 296 ? -23.58700 32.15400  -4.32500  1.000 65.46204  ? 262 GLN A CB    1 
ATOM   1868 C  CG    . GLN A 1 296 ? -23.59400 30.63800  -4.24500  1.000 71.32159  ? 262 GLN A CG    1 
ATOM   1869 C  CD    . GLN A 1 296 ? -22.47400 30.09800  -3.38000  1.000 84.71950  ? 262 GLN A CD    1 
ATOM   1870 O  OE1   . GLN A 1 296 ? -21.48100 30.78400  -3.12800  1.000 85.49518  ? 262 GLN A OE1   1 
ATOM   1871 N  NE2   . GLN A 1 296 ? -22.63100 28.86300  -2.91200  1.000 83.98620  ? 262 GLN A NE2   1 
ATOM   1872 N  N     . SER A 1 297 ? -23.85700 31.36500  -7.54600  1.000 42.87173  ? 263 SER A N     1 
ATOM   1873 C  CA    . SER A 1 297 ? -23.13900 31.06800  -8.78200  1.000 50.48576  ? 263 SER A CA    1 
ATOM   1874 C  C     . SER A 1 297 ? -23.32100 32.19000  -9.79900  1.000 37.73204  ? 263 SER A C     1 
ATOM   1875 O  O     . SER A 1 297 ? -22.34800 32.67200  -10.38900 1.000 42.20204  ? 263 SER A O     1 
ATOM   1876 C  CB    . SER A 1 297 ? -23.60200 29.72500  -9.35300  1.000 38.46458  ? 263 SER A CB    1 
ATOM   1877 O  OG    . SER A 1 297 ? -25.00300 29.70300  -9.55500  1.000 49.02272  ? 263 SER A OG    1 
ATOM   1878 N  N     . LEU A 1 298 ? -24.56100 32.64500  -9.98800  1.000 37.43476  ? 264 LEU A N     1 
ATOM   1879 C  CA    . LEU A 1 298 ? -24.82400 33.72600  -10.93500 1.000 41.23601  ? 264 LEU A CA    1 
ATOM   1880 C  C     . LEU A 1 298 ? -24.17100 35.02900  -10.48700 1.000 44.02243  ? 264 LEU A C     1 
ATOM   1881 O  O     . LEU A 1 298 ? -23.69500 35.81100  -11.32000 1.000 41.41457  ? 264 LEU A O     1 
ATOM   1882 C  CB    . LEU A 1 298 ? -26.33200 33.90400  -11.10900 1.000 42.36644  ? 264 LEU A CB    1 
ATOM   1883 C  CG    . LEU A 1 298 ? -27.05900 32.70400  -11.72500 1.000 40.16449  ? 264 LEU A CG    1 
ATOM   1884 C  CD1   . LEU A 1 298 ? -28.57100 32.88700  -11.67500 1.000 44.82888  ? 264 LEU A CD1   1 
ATOM   1885 C  CD2   . LEU A 1 298 ? -26.59100 32.48600  -13.16500 1.000 42.73642  ? 264 LEU A CD2   1 
ATOM   1886 N  N     . THR A 1 299 ? -24.13600 35.27500  -9.17500  1.000 41.67206  ? 265 THR A N     1 
ATOM   1887 C  CA    . THR A 1 299 ? -23.48700 36.47300  -8.65400  1.000 40.84763  ? 265 THR A CA    1 
ATOM   1888 C  C     . THR A 1 299 ? -21.99400 36.45600  -8.94500  1.000 36.52236  ? 265 THR A C     1 
ATOM   1889 O  O     . THR A 1 299 ? -21.40700 37.48800  -9.29000  1.000 41.78155  ? 265 THR A O     1 
ATOM   1890 C  CB    . THR A 1 299 ? -23.74400 36.58700  -7.14900  1.000 43.40012  ? 265 THR A CB    1 
ATOM   1891 O  OG1   . THR A 1 299 ? -25.15100 36.73500  -6.92000  1.000 47.09106  ? 265 THR A OG1   1 
ATOM   1892 C  CG2   . THR A 1 299 ? -22.99500 37.77700  -6.54900  1.000 44.89927  ? 265 THR A CG2   1 
ATOM   1893 N  N     . TRP A 1 300 ? -21.36500 35.28800  -8.81100  1.000 39.50348  ? 266 TRP A N     1 
ATOM   1894 C  CA    . TRP A 1 300 ? -19.95700 35.16000  -9.16300  1.000 35.61136  ? 266 TRP A CA    1 
ATOM   1895 C  C     . TRP A 1 300 ? -19.75100 35.35100  -10.66300 1.000 34.06996  ? 266 TRP A C     1 
ATOM   1896 O  O     . TRP A 1 300 ? -18.79500 36.01400  -11.08500 1.000 36.10063  ? 266 TRP A O     1 
ATOM   1897 C  CB    . TRP A 1 300 ? -19.43500 33.79700  -8.70100  1.000 38.71690  ? 266 TRP A CB    1 
ATOM   1898 C  CG    . TRP A 1 300 ? -17.97000 33.58500  -8.91300  1.000 43.10014  ? 266 TRP A CG    1 
ATOM   1899 C  CD1   . TRP A 1 300 ? -16.94800 34.11400  -8.17800  1.000 47.67012  ? 266 TRP A CD1   1 
ATOM   1900 C  CD2   . TRP A 1 300 ? -17.35800 32.78300  -9.93100  1.000 42.19029  ? 266 TRP A CD2   1 
ATOM   1901 N  NE1   . TRP A 1 300 ? -15.73800 33.69000  -8.67400  1.000 44.45429  ? 266 TRP A NE1   1 
ATOM   1902 C  CE2   . TRP A 1 300 ? -15.96200 32.87200  -9.75000  1.000 49.28386  ? 266 TRP A CE2   1 
ATOM   1903 C  CE3   . TRP A 1 300 ? -17.85400 31.99900  -10.97700 1.000 45.16970  ? 266 TRP A CE3   1 
ATOM   1904 C  CZ2   . TRP A 1 300 ? -15.05800 32.20700  -10.57800 1.000 40.87181  ? 266 TRP A CZ2   1 
ATOM   1905 C  CZ3   . TRP A 1 300 ? -16.95500 31.33800  -11.79500 1.000 38.94101  ? 266 TRP A CZ3   1 
ATOM   1906 C  CH2   . TRP A 1 300 ? -15.57400 31.44800  -11.59200 1.000 43.46781  ? 266 TRP A CH2   1 
ATOM   1907 N  N     . LEU A 1 301 ? -20.65200 34.80400  -11.48400 1.000 34.20065  ? 267 LEU A N     1 
ATOM   1908 C  CA    . LEU A 1 301 ? -20.51800 34.95400  -12.93300 1.000 34.84380  ? 267 LEU A CA    1 
ATOM   1909 C  C     . LEU A 1 301 ? -20.70500 36.40100  -13.37000 1.000 31.98968  ? 267 LEU A C     1 
ATOM   1910 O  O     . LEU A 1 301 ? -20.13500 36.82100  -14.38500 1.000 33.32989  ? 267 LEU A O     1 
ATOM   1911 C  CB    . LEU A 1 301 ? -21.52000 34.04400  -13.65600 1.000 34.84169  ? 267 LEU A CB    1 
ATOM   1912 C  CG    . LEU A 1 301 ? -21.32200 32.52600  -13.52700 1.000 33.46528  ? 267 LEU A CG    1 
ATOM   1913 C  CD1   . LEU A 1 301 ? -22.46100 31.78500  -14.19600 1.000 34.73374  ? 267 LEU A CD1   1 
ATOM   1914 C  CD2   . LEU A 1 301 ? -19.98200 32.08300  -14.11600 1.000 28.46793  ? 267 LEU A CD2   1 
ATOM   1915 N  N     . ASP A 1 302 ? -21.48100 37.18300  -12.61800 1.000 34.51614  ? 268 ASP A N     1 
ATOM   1916 C  CA    . ASP A 1 302 ? -21.67100 38.58900  -12.95700 1.000 34.91457  ? 268 ASP A CA    1 
ATOM   1917 C  C     . ASP A 1 302 ? -20.38200 39.40100  -12.87500 1.000 33.83093  ? 268 ASP A C     1 
ATOM   1918 O  O     . ASP A 1 302 ? -20.35800 40.53700  -13.36100 1.000 36.01018  ? 268 ASP A O     1 
ATOM   1919 C  CB    . ASP A 1 302 ? -22.73400 39.20200  -12.04300 1.000 34.44331  ? 268 ASP A CB    1 
ATOM   1920 C  CG    . ASP A 1 302 ? -24.14600 38.90500  -12.51100 1.000 37.54252  ? 268 ASP A CG    1 
ATOM   1921 O  OD1   . ASP A 1 302 ? -24.34700 38.72600  -13.73300 1.000 37.39614  ? 268 ASP A OD1   1 
ATOM   1922 O  OD2   . ASP A 1 302 ? -25.05400 38.85400  -11.65800 1.000 36.52982  ? 268 ASP A OD2   1 
ATOM   1923 N  N     . THR A 1 303 ? -19.32300 38.86100  -12.27300 1.000 35.08777  ? 269 THR A N     1 
ATOM   1924 C  CA    . THR A 1 303 ? -18.04000 39.54600  -12.16800 1.000 36.88174  ? 269 THR A CA    1 
ATOM   1925 C  C     . THR A 1 303 ? -17.05600 39.14400  -13.25400 1.000 36.57758  ? 269 THR A C     1 
ATOM   1926 O  O     . THR A 1 303 ? -15.94700 39.68300  -13.29100 1.000 37.84313  ? 269 THR A O     1 
ATOM   1927 C  CB    . THR A 1 303 ? -17.39600 39.28100  -10.79900 1.000 40.57039  ? 269 THR A CB    1 
ATOM   1928 O  OG1   . THR A 1 303 ? -16.98000 37.91100  -10.72000 1.000 36.88287  ? 269 THR A OG1   1 
ATOM   1929 C  CG2   . THR A 1 303 ? -18.36300 39.58700  -9.66700  1.000 32.23493  ? 269 THR A CG2   1 
ATOM   1930 N  N     . LYS A 1 304 ? -17.42700 38.22100  -14.13700 1.000 35.24498  ? 270 LYS A N     1 
ATOM   1931 C  CA    . LYS A 1 304 ? -16.50100 37.63100  -15.09100 1.000 36.32746  ? 270 LYS A CA    1 
ATOM   1932 C  C     . LYS A 1 304 ? -16.74800 38.16100  -16.49900 1.000 33.59485  ? 270 LYS A C     1 
ATOM   1933 O  O     . LYS A 1 304 ? -17.85400 38.59000  -16.83800 1.000 35.96053  ? 270 LYS A O     1 
ATOM   1934 C  CB    . LYS A 1 304 ? -16.61500 36.10300  -15.07100 1.000 34.30881  ? 270 LYS A CB    1 
ATOM   1935 C  CG    . LYS A 1 304 ? -16.24100 35.49500  -13.72600 1.000 35.37257  ? 270 LYS A CG    1 
ATOM   1936 C  CD    . LYS A 1 304 ? -14.85400 35.95900  -13.31400 1.000 37.65855  ? 270 LYS A CD    1 
ATOM   1937 C  CE    . LYS A 1 304 ? -14.45500 35.41800  -11.95600 1.000 41.76678  ? 270 LYS A CE    1 
ATOM   1938 N  NZ    . LYS A 1 304 ? -13.04900 35.79400  -11.63200 1.000 47.38963  ? 270 LYS A NZ    1 
ATOM   1939 N  N     . GLU A 1 305 ? -15.70100 38.12300  -17.31900 1.000 38.80310  ? 271 GLU A N     1 
ATOM   1940 C  CA    . GLU A 1 305 ? -15.78100 38.60900  -18.68700 1.000 33.66280  ? 271 GLU A CA    1 
ATOM   1941 C  C     . GLU A 1 305 ? -16.63500 37.66200  -19.53400 1.000 40.30999  ? 271 GLU A C     1 
ATOM   1942 O  O     . GLU A 1 305 ? -16.76300 36.47800  -19.21400 1.000 36.67967  ? 271 GLU A O     1 
ATOM   1943 C  CB    . GLU A 1 305 ? -14.37600 38.72300  -19.27600 1.000 45.75348  ? 271 GLU A CB    1 
ATOM   1944 C  CG    . GLU A 1 305 ? -13.65200 40.06000  -19.02800 1.000 48.10092  ? 271 GLU A CG    1 
ATOM   1945 C  CD    . GLU A 1 305 ? -14.55400 41.27500  -19.18300 1.000 57.54489  ? 271 GLU A CD    1 
ATOM   1946 O  OE1   . GLU A 1 305 ? -14.69200 41.78400  -20.31700 1.000 54.64192  ? 271 GLU A OE1   1 
ATOM   1947 O  OE2   . GLU A 1 305 ? -15.11200 41.73600  -18.16700 1.000 55.84674  ? 271 GLU A OE2   1 
ATOM   1948 N  N     . PRO A 1 306 ? -17.23400 38.16100  -20.61600 1.000 44.11538  ? 272 PRO A N     1 
ATOM   1949 C  CA    . PRO A 1 306 ? -18.03700 37.28300  -21.48000 1.000 42.61552  ? 272 PRO A CA    1 
ATOM   1950 C  C     . PRO A 1 306 ? -17.22500 36.09300  -21.96800 1.000 36.96228  ? 272 PRO A C     1 
ATOM   1951 O  O     . PRO A 1 306 ? -16.03900 36.21800  -22.28300 1.000 29.87647  ? 272 PRO A O     1 
ATOM   1952 C  CB    . PRO A 1 306 ? -18.44000 38.19700  -22.64400 1.000 37.64153  ? 272 PRO A CB    1 
ATOM   1953 C  CG    . PRO A 1 306 ? -18.37600 39.58200  -22.07300 1.000 46.13643  ? 272 PRO A CG    1 
ATOM   1954 C  CD    . PRO A 1 306 ? -17.25700 39.56300  -21.07300 1.000 38.87500  ? 272 PRO A CD    1 
ATOM   1955 N  N     . SER A 1 307 ? -17.87800 34.92500  -22.00100 1.000 29.64133  ? 273 SER A N     1 
ATOM   1956 C  CA    . SER A 1 307 ? -17.31400 33.68400  -22.54700 1.000 36.89385  ? 273 SER A CA    1 
ATOM   1957 C  C     . SER A 1 307 ? -16.00800 33.27500  -21.87000 1.000 32.50050  ? 273 SER A C     1 
ATOM   1958 O  O     . SER A 1 307 ? -15.19800 32.55800  -22.46000 1.000 40.02971  ? 273 SER A O     1 
ATOM   1959 C  CB    . SER A 1 307 ? -17.09800 33.78300  -24.06100 1.000 29.46281  ? 273 SER A CB    1 
ATOM   1960 O  OG    . SER A 1 307 ? -18.31600 34.05100  -24.72500 1.000 39.05999  ? 273 SER A OG    1 
ATOM   1961 N  N     . SER A 1 308 ? -15.79100 33.69300  -20.62600 1.000 32.48396  ? 274 SER A N     1 
ATOM   1962 C  CA    . SER A 1 308 ? -14.50900 33.46800  -19.97400 1.000 32.39537  ? 274 SER A CA    1 
ATOM   1963 C  C     . SER A 1 308 ? -14.51500 32.32100  -18.97100 1.000 36.09177  ? 274 SER A C     1 
ATOM   1964 O  O     . SER A 1 308 ? -13.44700 31.98200  -18.44700 1.000 30.00561  ? 274 SER A O     1 
ATOM   1965 C  CB    . SER A 1 308 ? -14.05000 34.75000  -19.26600 1.000 36.15805  ? 274 SER A CB    1 
ATOM   1966 O  OG    . SER A 1 308 ? -14.92800 35.08300  -18.20200 1.000 37.19322  ? 274 SER A OG    1 
ATOM   1967 N  N     . VAL A 1 309 ? -15.66700 31.71500  -18.69100 1.000 28.24104  ? 275 VAL A N     1 
ATOM   1968 C  CA    . VAL A 1 309 ? -15.79500 30.73300  -17.61900 1.000 31.24050  ? 275 VAL A CA    1 
ATOM   1969 C  C     . VAL A 1 309 ? -16.20700 29.39100  -18.20900 1.000 29.22031  ? 275 VAL A C     1 
ATOM   1970 O  O     . VAL A 1 309 ? -17.17200 29.31100  -18.97700 1.000 29.52071  ? 275 VAL A O     1 
ATOM   1971 C  CB    . VAL A 1 309 ? -16.80800 31.18700  -16.55000 1.000 36.28680  ? 275 VAL A CB    1 
ATOM   1972 C  CG1   . VAL A 1 309 ? -16.99400 30.10000  -15.49600 1.000 29.21996  ? 275 VAL A CG1   1 
ATOM   1973 C  CG2   . VAL A 1 309 ? -16.35400 32.48900  -15.90400 1.000 31.83290  ? 275 VAL A CG2   1 
ATOM   1974 N  N     . LEU A 1 310 ? -15.47800 28.34200  -17.84100 1.000 33.07013  ? 276 LEU A N     1 
ATOM   1975 C  CA    . LEU A 1 310 ? -15.84600 26.97300  -18.17400 1.000 26.91237  ? 276 LEU A CA    1 
ATOM   1976 C  C     . LEU A 1 310 ? -16.80900 26.45100  -17.11100 1.000 35.39103  ? 276 LEU A C     1 
ATOM   1977 O  O     . LEU A 1 310 ? -16.47100 26.41600  -15.92300 1.000 35.09488  ? 276 LEU A O     1 
ATOM   1978 C  CB    . LEU A 1 310 ? -14.60400 26.08400  -18.24900 1.000 27.10983  ? 276 LEU A CB    1 
ATOM   1979 C  CG    . LEU A 1 310 ? -14.87700 24.60000  -18.50800 1.000 37.88194  ? 276 LEU A CG    1 
ATOM   1980 C  CD1   . LEU A 1 310 ? -15.21700 24.40200  -19.98300 1.000 32.05950  ? 276 LEU A CD1   1 
ATOM   1981 C  CD2   . LEU A 1 310 ? -13.69400 23.73400  -18.10700 1.000 28.97980  ? 276 LEU A CD2   1 
ATOM   1982 N  N     . TYR A 1 311 ? -18.00600 26.06200  -17.53300 1.000 31.74418  ? 277 TYR A N     1 
ATOM   1983 C  CA    . TYR A 1 311 ? -18.97700 25.43700  -16.64700 1.000 33.00906  ? 277 TYR A CA    1 
ATOM   1984 C  C     . TYR A 1 311 ? -18.75100 23.93000  -16.64700 1.000 35.12898  ? 277 TYR A C     1 
ATOM   1985 O  O     . TYR A 1 311 ? -18.65800 23.31300  -17.71400 1.000 34.43368  ? 277 TYR A O     1 
ATOM   1986 C  CB    . TYR A 1 311 ? -20.39900 25.77600  -17.10000 1.000 28.17353  ? 277 TYR A CB    1 
ATOM   1987 C  CG    . TYR A 1 311 ? -21.50300 25.12400  -16.29900 1.000 29.21831  ? 277 TYR A CG    1 
ATOM   1988 C  CD1   . TYR A 1 311 ? -21.59900 25.31300  -14.92300 1.000 36.82939  ? 277 TYR A CD1   1 
ATOM   1989 C  CD2   . TYR A 1 311 ? -22.47000 24.34600  -16.92400 1.000 28.60222  ? 277 TYR A CD2   1 
ATOM   1990 C  CE1   . TYR A 1 311 ? -22.61600 24.73000  -14.19100 1.000 33.71184  ? 277 TYR A CE1   1 
ATOM   1991 C  CE2   . TYR A 1 311 ? -23.49300 23.75800  -16.20400 1.000 31.40611  ? 277 TYR A CE2   1 
ATOM   1992 C  CZ    . TYR A 1 311 ? -23.56000 23.95300  -14.83600 1.000 38.00578  ? 277 TYR A CZ    1 
ATOM   1993 O  OH    . TYR A 1 311 ? -24.57600 23.37000  -14.11500 1.000 35.44474  ? 277 TYR A OH    1 
ATOM   1994 N  N     . ILE A 1 312 ? -18.64500 23.34600  -15.45600 1.000 32.15125  ? 278 ILE A N     1 
ATOM   1995 C  CA    . ILE A 1 312 ? -18.38900 21.91800  -15.28800 1.000 32.88662  ? 278 ILE A CA    1 
ATOM   1996 C  C     . ILE A 1 312 ? -19.51000 21.32600  -14.45000 1.000 37.56446  ? 278 ILE A C     1 
ATOM   1997 O  O     . ILE A 1 312 ? -19.73700 21.76100  -13.31300 1.000 37.57660  ? 278 ILE A O     1 
ATOM   1998 C  CB    . ILE A 1 312 ? -17.02800 21.65400  -14.62800 1.000 35.17219  ? 278 ILE A CB    1 
ATOM   1999 C  CG1   . ILE A 1 312 ? -15.93900 22.49400  -15.29900 1.000 30.60234  ? 278 ILE A CG1   1 
ATOM   2000 C  CG2   . ILE A 1 312 ? -16.70500 20.16100  -14.63700 1.000 29.58644  ? 278 ILE A CG2   1 
ATOM   2001 C  CD1   . ILE A 1 312 ? -14.61800 22.48200  -14.55000 1.000 48.85308  ? 278 ILE A CD1   1 
ATOM   2002 N  N     . SER A 1 313 ? -20.19700 20.32700  -14.99900 1.000 37.98496  ? 279 SER A N     1 
ATOM   2003 C  CA    . SER A 1 313 ? -21.28300 19.66600  -14.27700 1.000 42.95058  ? 279 SER A CA    1 
ATOM   2004 C  C     . SER A 1 313 ? -21.56100 18.31600  -14.91800 1.000 37.72067  ? 279 SER A C     1 
ATOM   2005 O  O     . SER A 1 313 ? -21.87800 18.25100  -16.11000 1.000 40.24244  ? 279 SER A O     1 
ATOM   2006 C  CB    . SER A 1 313 ? -22.54100 20.53100  -14.28100 1.000 37.99741  ? 279 SER A CB    1 
ATOM   2007 O  OG    . SER A 1 313 ? -23.60600 19.87300  -13.62500 1.000 45.87876  ? 279 SER A OG    1 
ATOM   2008 N  N     . PHE A 1 314 ? -21.45500 17.24700  -14.13200 1.000 44.13451  ? 280 PHE A N     1 
ATOM   2009 C  CA    . PHE A 1 314 ? -21.76100 15.90000  -14.59500 1.000 48.88794  ? 280 PHE A CA    1 
ATOM   2010 C  C     . PHE A 1 314 ? -23.02600 15.33400  -13.96300 1.000 52.54936  ? 280 PHE A C     1 
ATOM   2011 O  O     . PHE A 1 314 ? -23.41100 14.20300  -14.28400 1.000 46.03634  ? 280 PHE A O     1 
ATOM   2012 C  CB    . PHE A 1 314 ? -20.57800 14.96200  -14.31700 1.000 42.97926  ? 280 PHE A CB    1 
ATOM   2013 C  CG    . PHE A 1 314 ? -19.35600 15.28200  -15.12400 1.000 40.47409  ? 280 PHE A CG    1 
ATOM   2014 C  CD1   . PHE A 1 314 ? -18.53800 16.34400  -14.77100 1.000 35.26791  ? 280 PHE A CD1   1 
ATOM   2015 C  CD2   . PHE A 1 314 ? -19.03300 14.53400  -16.24500 1.000 41.06372  ? 280 PHE A CD2   1 
ATOM   2016 C  CE1   . PHE A 1 314 ? -17.41800 16.65400  -15.51600 1.000 36.67594  ? 280 PHE A CE1   1 
ATOM   2017 C  CE2   . PHE A 1 314 ? -17.91400 14.83600  -16.99100 1.000 39.30249  ? 280 PHE A CE2   1 
ATOM   2018 C  CZ    . PHE A 1 314 ? -17.10500 15.90000  -16.62700 1.000 43.45883  ? 280 PHE A CZ    1 
ATOM   2019 N  N     . GLY A 1 315 ? -23.67900 16.08100  -13.07500 1.000 51.89286  ? 281 GLY A N     1 
ATOM   2020 C  CA    . GLY A 1 315 ? -24.91500 15.62000  -12.47900 1.000 48.17983  ? 281 GLY A CA    1 
ATOM   2021 C  C     . GLY A 1 315 ? -24.68500 14.54100  -11.43500 1.000 50.53650  ? 281 GLY A C     1 
ATOM   2022 O  O     . GLY A 1 315 ? -23.57000 14.31900  -10.95100 1.000 55.85136  ? 281 GLY A O     1 
ATOM   2023 N  N     . SER A 1 316 ? -25.77500 13.85100  -11.09500 1.000 58.86645  ? 282 SER A N     1 
ATOM   2024 C  CA    . SER A 1 316 ? -25.76900 12.83700  -10.04500 1.000 65.31805  ? 282 SER A CA    1 
ATOM   2025 C  C     . SER A 1 316 ? -25.52500 11.43300  -10.59200 1.000 64.90238  ? 282 SER A C     1 
ATOM   2026 O  O     . SER A 1 316 ? -24.70800 10.68700  -10.04200 1.000 54.36397  ? 282 SER A O     1 
ATOM   2027 C  CB    . SER A 1 316 ? -27.09200 12.87900  -9.27600  1.000 58.47978  ? 282 SER A CB    1 
ATOM   2028 O  OG    . SER A 1 316 ? -28.16300 13.22300  -10.14000 1.000 80.96254  ? 282 SER A OG    1 
ATOM   2029 N  N     . LEU A 1 317 ? -26.23000 11.06100  -11.66600 1.000 65.92557  ? 283 LEU A N     1 
ATOM   2030 C  CA    . LEU A 1 317 ? -26.07100 9.72800   -12.24300 1.000 59.78524  ? 283 LEU A CA    1 
ATOM   2031 C  C     . LEU A 1 317 ? -24.63500 9.49000   -12.69800 1.000 62.86928  ? 283 LEU A C     1 
ATOM   2032 O  O     . LEU A 1 317 ? -23.99700 8.50800   -12.30000 1.000 57.07841  ? 283 LEU A O     1 
ATOM   2033 C  CB    . LEU A 1 317 ? -27.04200 9.54200   -13.41100 1.000 65.68199  ? 283 LEU A CB    1 
ATOM   2034 C  CG    . LEU A 1 317 ? -27.41200 8.10500   -13.79100 1.000 72.96543  ? 283 LEU A CG    1 
ATOM   2035 C  CD1   . LEU A 1 317 ? -27.44300 7.20600   -12.56200 1.000 55.50107  ? 283 LEU A CD1   1 
ATOM   2036 C  CD2   . LEU A 1 317 ? -28.74500 8.05800   -14.53400 1.000 60.39258  ? 283 LEU A CD2   1 
ATOM   2037 N  N     . CYS A 1 318 ? -24.10800 10.38500  -13.53000 1.000 55.27934  ? 284 CYS A N     1 
ATOM   2038 C  CA    . CYS A 1 318 ? -22.75400 10.24700  -14.06500 1.000 59.94535  ? 284 CYS A CA    1 
ATOM   2039 C  C     . CYS A 1 318 ? -21.71600 10.94200  -13.20100 1.000 60.84295  ? 284 CYS A C     1 
ATOM   2040 O  O     . CYS A 1 318 ? -20.80300 11.58900  -13.72400 1.000 56.82489  ? 284 CYS A O     1 
ATOM   2041 C  CB    . CYS A 1 318 ? -22.71300 10.77300  -15.49600 1.000 59.46576  ? 284 CYS A CB    1 
ATOM   2042 S  SG    . CYS A 1 318 ? -24.04400 10.12000  -16.53700 1.000 59.14751  ? 284 CYS A SG    1 
ATOM   2043 N  N     . ARG A 1 319 ? -21.82400 10.82600  -11.87900 1.000 60.06820  ? 285 ARG A N     1 
ATOM   2044 C  CA    . ARG A 1 319 ? -20.82800 11.41500  -10.99700 1.000 68.83210  ? 285 ARG A CA    1 
ATOM   2045 C  C     . ARG A 1 319 ? -19.52400 10.62400  -11.06500 1.000 58.84253  ? 285 ARG A C     1 
ATOM   2046 O  O     . ARG A 1 319 ? -19.51900 9.40000   -11.22500 1.000 52.07004  ? 285 ARG A O     1 
ATOM   2047 C  CB    . ARG A 1 319 ? -21.35000 11.47800  -9.55900  1.000 64.71843  ? 285 ARG A CB    1 
ATOM   2048 C  CG    . ARG A 1 319 ? -21.62100 10.13000  -8.90700  1.000 67.75498  ? 285 ARG A CG    1 
ATOM   2049 C  CD    . ARG A 1 319 ? -22.20600 10.31000  -7.51000  1.000 70.06557  ? 285 ARG A CD    1 
ATOM   2050 N  NE    . ARG A 1 319 ? -22.43400 9.03700   -6.83500  1.000 85.86133  ? 285 ARG A NE    1 
ATOM   2051 C  CZ    . ARG A 1 319 ? -21.53600 8.41600   -6.08200  1.000 104.43503 ? 285 ARG A CZ    1 
ATOM   2052 N  NH1   . ARG A 1 319 ? -20.32800 8.92200   -5.88600  1.000 95.62262  ? 285 ARG A NH1   1 
ATOM   2053 N  NH2   . ARG A 1 319 ? -21.85800 7.25900   -5.50900  1.000 105.10968 ? 285 ARG A NH2   1 
ATOM   2054 N  N     . LEU A 1 320 ? -18.41300 11.34300  -10.94500 1.000 50.75659  ? 286 LEU A N     1 
ATOM   2055 C  CA    . LEU A 1 320 ? -17.08800 10.78500  -11.16000 1.000 52.42884  ? 286 LEU A CA    1 
ATOM   2056 C  C     . LEU A 1 320 ? -16.49700 10.22800  -9.86700  1.000 52.25301  ? 286 LEU A C     1 
ATOM   2057 O  O     . LEU A 1 320 ? -16.91900 10.56700  -8.76000  1.000 49.63113  ? 286 LEU A O     1 
ATOM   2058 C  CB    . LEU A 1 320 ? -16.15400 11.84500  -11.74300 1.000 46.86106  ? 286 LEU A CB    1 
ATOM   2059 C  CG    . LEU A 1 320 ? -16.67400 12.57100  -12.98500 1.000 50.74638  ? 286 LEU A CG    1 
ATOM   2060 C  CD1   . LEU A 1 320 ? -15.72100 13.68800  -13.39600 1.000 46.89316  ? 286 LEU A CD1   1 
ATOM   2061 C  CD2   . LEU A 1 320 ? -16.87100 11.57600  -14.11700 1.000 50.41840  ? 286 LEU A CD2   1 
ATOM   2062 N  N     . SER A 1 321 ? -15.49200 9.37200   -10.02800 1.000 52.28259  ? 287 SER A N     1 
ATOM   2063 C  CA    . SER A 1 321 ? -14.80800 8.77000   -8.89800  1.000 52.92099  ? 287 SER A CA    1 
ATOM   2064 C  C     . SER A 1 321 ? -13.84700 9.76700   -8.25600  1.000 49.13921  ? 287 SER A C     1 
ATOM   2065 O  O     . SER A 1 321 ? -13.49400 10.79800  -8.83800  1.000 46.73033  ? 287 SER A O     1 
ATOM   2066 C  CB    . SER A 1 321 ? -14.03200 7.53400   -9.33700  1.000 50.95631  ? 287 SER A CB    1 
ATOM   2067 O  OG    . SER A 1 321 ? -12.90100 7.91500   -10.09400 1.000 46.62972  ? 287 SER A OG    1 
ATOM   2068 N  N     . ASN A 1 322 ? -13.41100 9.43000   -7.03700  1.000 55.49959  ? 288 ASN A N     1 
ATOM   2069 C  CA    . ASN A 1 322 ? -12.47600 10.28600  -6.30900  1.000 52.73583  ? 288 ASN A CA    1 
ATOM   2070 C  C     . ASN A 1 322 ? -11.18900 10.48500  -7.09700  1.000 50.35674  ? 288 ASN A C     1 
ATOM   2071 O  O     . ASN A 1 322 ? -10.68100 11.60800  -7.20900  1.000 50.68086  ? 288 ASN A O     1 
ATOM   2072 C  CB    . ASN A 1 322 ? -12.17000 9.68400   -4.93500  1.000 49.13985  ? 288 ASN A CB    1 
ATOM   2073 C  CG    . ASN A 1 322 ? -13.32800 9.81400   -3.96600  1.000 66.54696  ? 288 ASN A CG    1 
ATOM   2074 O  OD1   . ASN A 1 322 ? -14.15400 10.72400  -4.07600  1.000 66.66173  ? 288 ASN A OD1   1 
ATOM   2075 N  ND2   . ASN A 1 322 ? -13.39400 8.90100   -3.00500  1.000 70.47333  ? 288 ASN A ND2   1 
ATOM   2076 N  N     . GLU A 1 323 ? -10.64100 9.39800   -7.64300  1.000 52.25370  ? 289 GLU A N     1 
ATOM   2077 C  CA    . GLU A 1 323 ? -9.43600  9.50700   -8.45600  1.000 53.52218  ? 289 GLU A CA    1 
ATOM   2078 C  C     . GLU A 1 323 ? -9.68700  10.35200  -9.69900  1.000 52.47707  ? 289 GLU A C     1 
ATOM   2079 O  O     . GLU A 1 323 ? -8.81900  11.12700  -10.12000 1.000 48.51747  ? 289 GLU A O     1 
ATOM   2080 C  CB    . GLU A 1 323 ? -8.94100  8.11100   -8.84000  1.000 52.41230  ? 289 GLU A CB    1 
ATOM   2081 C  CG    . GLU A 1 323 ? -7.52900  8.08000   -9.40100  1.000 70.81112  ? 289 GLU A CG    1 
ATOM   2082 C  CD    . GLU A 1 323 ? -7.13800  6.70600   -9.91700  1.000 84.22359  ? 289 GLU A CD    1 
ATOM   2083 O  OE1   . GLU A 1 323 ? -7.95400  5.76700   -9.78200  1.000 85.83063  ? 289 GLU A OE1   1 
ATOM   2084 O  OE2   . GLU A 1 323 ? -6.02400  6.56900   -10.47000 1.000 78.72799  ? 289 GLU A OE2   1 
ATOM   2085 N  N     . GLN A 1 324 ? -10.87600 10.22500  -10.29500 1.000 50.59219  ? 290 GLN A N     1 
ATOM   2086 C  CA    . GLN A 1 324 ? -11.19500 11.01400  -11.48100 1.000 45.43927  ? 290 GLN A CA    1 
ATOM   2087 C  C     . GLN A 1 324 ? -11.36700 12.48600  -11.13300 1.000 40.84579  ? 290 GLN A C     1 
ATOM   2088 O  O     . GLN A 1 324 ? -10.93300 13.36200  -11.89100 1.000 40.92211  ? 290 GLN A O     1 
ATOM   2089 C  CB    . GLN A 1 324 ? -12.45500 10.46600  -12.15400 1.000 43.10686  ? 290 GLN A CB    1 
ATOM   2090 C  CG    . GLN A 1 324 ? -12.85300 11.20000  -13.43000 1.000 46.24102  ? 290 GLN A CG    1 
ATOM   2091 C  CD    . GLN A 1 324 ? -11.83100 11.04300  -14.53600 1.000 44.28518  ? 290 GLN A CD    1 
ATOM   2092 O  OE1   . GLN A 1 324 ? -11.83200 10.04700  -15.26100 1.000 49.57747  ? 290 GLN A OE1   1 
ATOM   2093 N  NE2   . GLN A 1 324 ? -10.94600 12.02800  -14.67000 1.000 43.36520  ? 290 GLN A NE2   1 
ATOM   2094 N  N     . LEU A 1 325 ? -11.98800 12.77800  -9.98800  1.000 44.02982  ? 291 LEU A N     1 
ATOM   2095 C  CA    . LEU A 1 325 ? -12.17800 14.16700  -9.58400  1.000 40.88066  ? 291 LEU A CA    1 
ATOM   2096 C  C     . LEU A 1 325 ? -10.84300 14.85200  -9.32100  1.000 45.99169  ? 291 LEU A C     1 
ATOM   2097 O  O     . LEU A 1 325 ? -10.67700 16.03800  -9.63100  1.000 47.67193  ? 291 LEU A O     1 
ATOM   2098 C  CB    . LEU A 1 325 ? -13.07900 14.23300  -8.35200  1.000 45.07242  ? 291 LEU A CB    1 
ATOM   2099 C  CG    . LEU A 1 325 ? -14.53500 13.83300  -8.60200  1.000 50.28250  ? 291 LEU A CG    1 
ATOM   2100 C  CD1   . LEU A 1 325 ? -15.34900 13.85900  -7.31800  1.000 51.59562  ? 291 LEU A CD1   1 
ATOM   2101 C  CD2   . LEU A 1 325 ? -15.16300 14.73700  -9.65200  1.000 45.03886  ? 291 LEU A CD2   1 
ATOM   2102 N  N     . LYS A 1 326 ? -9.87500  14.11900  -8.76200  1.000 46.47043  ? 292 LYS A N     1 
ATOM   2103 C  CA    . LYS A 1 326 ? -8.55100  14.68800  -8.53100  1.000 50.82099  ? 292 LYS A CA    1 
ATOM   2104 C  C     . LYS A 1 326 ? -7.85400  15.00100  -9.84900  1.000 46.54091  ? 292 LYS A C     1 
ATOM   2105 O  O     . LYS A 1 326 ? -7.29900  16.09200  -10.02800 1.000 44.77670  ? 292 LYS A O     1 
ATOM   2106 C  CB    . LYS A 1 326 ? -7.70600  13.73100  -7.68800  1.000 49.64953  ? 292 LYS A CB    1 
ATOM   2107 C  CG    . LYS A 1 326 ? -7.98600  13.80300  -6.19500  1.000 54.37711  ? 292 LYS A CG    1 
ATOM   2108 C  CD    . LYS A 1 326 ? -7.05000  12.89700  -5.40300  1.000 58.92853  ? 292 LYS A CD    1 
ATOM   2109 C  CE    . LYS A 1 326 ? -7.77400  12.24900  -4.23100  1.000 62.68244  ? 292 LYS A CE    1 
ATOM   2110 N  NZ    . LYS A 1 326 ? -7.07500  12.47800  -2.93700  1.000 68.21538  ? 292 LYS A NZ    1 
ATOM   2111 N  N     . GLU A 1 327 ? -7.86300  14.04700  -10.78400 1.000 42.97662  ? 293 GLU A N     1 
ATOM   2112 C  CA    . GLU A 1 327 ? -7.28800  14.30400  -12.10100 1.000 42.97470  ? 293 GLU A CA    1 
ATOM   2113 C  C     . GLU A 1 327 ? -7.96200  15.49900  -12.76200 1.000 45.01080  ? 293 GLU A C     1 
ATOM   2114 O  O     . GLU A 1 327 ? -7.30900  16.29200  -13.45100 1.000 49.08409  ? 293 GLU A O     1 
ATOM   2115 C  CB    . GLU A 1 327 ? -7.42000  13.06100  -12.98000 1.000 44.69241  ? 293 GLU A CB    1 
ATOM   2116 C  CG    . GLU A 1 327 ? -6.57400  11.87800  -12.53100 1.000 54.64452  ? 293 GLU A CG    1 
ATOM   2117 C  CD    . GLU A 1 327 ? -5.11800  11.99800  -12.94000 1.000 58.44843  ? 293 GLU A CD    1 
ATOM   2118 O  OE1   . GLU A 1 327 ? -4.77600  12.93000  -13.70100 1.000 52.04318  ? 293 GLU A OE1   1 
ATOM   2119 O  OE2   . GLU A 1 327 ? -4.31200  11.15400  -12.49900 1.000 82.60992  ? 293 GLU A OE2   1 
ATOM   2120 N  N     . MET A 1 328 ? -9.26900  15.64900  -12.54800 1.000 43.81287  ? 294 MET A N     1 
ATOM   2121 C  CA    . MET A 1 328 ? -10.00000 16.76600  -13.13300 1.000 42.55772  ? 294 MET A CA    1 
ATOM   2122 C  C     . MET A 1 328 ? -9.53100  18.09400  -12.55500 1.000 42.24400  ? 294 MET A C     1 
ATOM   2123 O  O     . MET A 1 328 ? -9.26500  19.04600  -13.29900 1.000 41.68408  ? 294 MET A O     1 
ATOM   2124 C  CB    . MET A 1 328 ? -11.49800 16.57600  -12.90800 1.000 35.89338  ? 294 MET A CB    1 
ATOM   2125 C  CG    . MET A 1 328 ? -12.33700 17.77200  -13.30800 1.000 56.30417  ? 294 MET A CG    1 
ATOM   2126 S  SD    . MET A 1 328 ? -13.93700 17.25700  -13.94200 1.000 58.33572  ? 294 MET A SD    1 
ATOM   2127 C  CE    . MET A 1 328 ? -13.42700 16.36200  -15.40500 1.000 51.62933  ? 294 MET A CE    1 
ATOM   2128 N  N     . ALA A 1 329 ? -9.41900  18.17300  -11.22600 1.000 41.34203  ? 295 ALA A N     1 
ATOM   2129 C  CA    . ALA A 1 329 ? -9.00700  19.41800  -10.58500 1.000 46.56102  ? 295 ALA A CA    1 
ATOM   2130 C  C     . ALA A 1 329 ? -7.61300  19.83900  -11.03200 1.000 49.26709  ? 295 ALA A C     1 
ATOM   2131 O  O     . ALA A 1 329 ? -7.36600  21.02600  -11.27500 1.000 46.11401  ? 295 ALA A O     1 
ATOM   2132 C  CB    . ALA A 1 329 ? -9.06300  19.26900  -9.06300  1.000 48.65025  ? 295 ALA A CB    1 
ATOM   2133 N  N     . ASN A 1 330 ? -6.69100  18.87900  -11.15400 1.000 41.75750  ? 296 ASN A N     1 
ATOM   2134 C  CA    . ASN A 1 330 ? -5.35200  19.19400  -11.64300 1.000 44.71074  ? 296 ASN A CA    1 
ATOM   2135 C  C     . ASN A 1 330 ? -5.39600  19.70400  -13.07900 1.000 45.81459  ? 296 ASN A C     1 
ATOM   2136 O  O     . ASN A 1 330 ? -4.77700  20.72300  -13.40700 1.000 44.44132  ? 296 ASN A O     1 
ATOM   2137 C  CB    . ASN A 1 330 ? -4.45100  17.96300  -11.54500 1.000 42.49054  ? 296 ASN A CB    1 
ATOM   2138 C  CG    . ASN A 1 330 ? -4.12100  17.59700  -10.11500 1.000 53.20532  ? 296 ASN A CG    1 
ATOM   2139 O  OD1   . ASN A 1 330 ? -3.92500  18.46700  -9.26800  1.000 50.97732  ? 296 ASN A OD1   1 
ATOM   2140 N  ND2   . ASN A 1 330 ? -4.05900  16.30100  -9.83600  1.000 62.04173  ? 296 ASN A ND2   1 
ATOM   2141 N  N     . GLY A 1 331 ? -6.11400  18.99900  -13.95500 1.000 45.10550  ? 297 GLY A N     1 
ATOM   2142 C  CA    . GLY A 1 331 ? -6.22300  19.45000  -15.33400 1.000 38.13675  ? 297 GLY A CA    1 
ATOM   2143 C  C     . GLY A 1 331 ? -6.89100  20.80600  -15.44100 1.000 41.21932  ? 297 GLY A C     1 
ATOM   2144 O  O     . GLY A 1 331 ? -6.44700  21.67300  -16.19800 1.000 42.32869  ? 297 GLY A O     1 
ATOM   2145 N  N     . ILE A 1 332 ? -7.95700  21.01400  -14.66700 1.000 43.11543  ? 298 ILE A N     1 
ATOM   2146 C  CA    . ILE A 1 332 ? -8.65300  22.29600  -14.67900 1.000 44.04815  ? 298 ILE A CA    1 
ATOM   2147 C  C     . ILE A 1 332 ? -7.74500  23.40500  -14.16400 1.000 47.96587  ? 298 ILE A C     1 
ATOM   2148 O  O     . ILE A 1 332 ? -7.66700  24.49000  -14.75500 1.000 42.73659  ? 298 ILE A O     1 
ATOM   2149 C  CB    . ILE A 1 332 ? -9.95500  22.20000  -13.86300 1.000 42.77806  ? 298 ILE A CB    1 
ATOM   2150 C  CG1   . ILE A 1 332 ? -10.99000 21.38000  -14.63000 1.000 47.57225  ? 298 ILE A CG1   1 
ATOM   2151 C  CG2   . ILE A 1 332 ? -10.49900 23.57700  -13.57000 1.000 46.06307  ? 298 ILE A CG2   1 
ATOM   2152 C  CD1   . ILE A 1 332 ? -11.24300 21.90700  -16.02700 1.000 41.59951  ? 298 ILE A CD1   1 
ATOM   2153 N  N     . GLU A 1 333 ? -7.04000  23.15100  -13.05800 1.000 48.81070  ? 299 GLU A N     1 
ATOM   2154 C  CA    . GLU A 1 333 ? -6.12300  24.15300  -12.52500 1.000 53.08132  ? 299 GLU A CA    1 
ATOM   2155 C  C     . GLU A 1 333 ? -4.97600  24.42200  -13.48900 1.000 49.45245  ? 299 GLU A C     1 
ATOM   2156 O  O     . GLU A 1 333 ? -4.63400  25.58100  -13.74700 1.000 48.03726  ? 299 GLU A O     1 
ATOM   2157 C  CB    . GLU A 1 333 ? -5.58400  23.71000  -11.16700 1.000 48.37876  ? 299 GLU A CB    1 
ATOM   2158 C  CG    . GLU A 1 333 ? -4.56300  24.67100  -10.58500 1.000 59.25257  ? 299 GLU A CG    1 
ATOM   2159 C  CD    . GLU A 1 333 ? -4.19000  24.33700  -9.15200  1.000 68.36882  ? 299 GLU A CD    1 
ATOM   2160 O  OE1   . GLU A 1 333 ? -4.62100  23.27400  -8.65100  1.000 67.61255  ? 299 GLU A OE1   1 
ATOM   2161 O  OE2   . GLU A 1 333 ? -3.46900  25.14400  -8.52600  1.000 65.66168  ? 299 GLU A OE2   1 
ATOM   2162 N  N     . ALA A 1 334 ? -4.37800  23.36500  -14.04300 1.000 45.38414  ? 300 ALA A N     1 
ATOM   2163 C  CA    . ALA A 1 334 ? -3.30500  23.55400  -15.01100 1.000 49.69714  ? 300 ALA A CA    1 
ATOM   2164 C  C     . ALA A 1 334 ? -3.77900  24.26400  -16.27400 1.000 48.85287  ? 300 ALA A C     1 
ATOM   2165 O  O     . ALA A 1 334 ? -2.95100  24.82500  -17.00100 1.000 51.94334  ? 300 ALA A O     1 
ATOM   2166 C  CB    . ALA A 1 334 ? -2.67700  22.20700  -15.37200 1.000 50.95972  ? 300 ALA A CB    1 
ATOM   2167 N  N     . SER A 1 335 ? -5.08500  24.25900  -16.55500 1.000 43.03297  ? 301 SER A N     1 
ATOM   2168 C  CA    . SER A 1 335 ? -5.58200  24.96000  -17.73500 1.000 47.84943  ? 301 SER A CA    1 
ATOM   2169 C  C     . SER A 1 335 ? -5.52700  26.47300  -17.57300 1.000 46.99455  ? 301 SER A C     1 
ATOM   2170 O  O     . SER A 1 335 ? -5.56100  27.19300  -18.57800 1.000 47.83766  ? 301 SER A O     1 
ATOM   2171 C  CB    . SER A 1 335 ? -7.01700  24.53400  -18.04800 1.000 40.45948  ? 301 SER A CB    1 
ATOM   2172 O  OG    . SER A 1 335 ? -7.94400  25.21100  -17.21300 1.000 40.33808  ? 301 SER A OG    1 
ATOM   2173 N  N     . LYS A 1 336 ? -5.44400  26.96500  -16.33300 1.000 45.79874  ? 302 LYS A N     1 
ATOM   2174 C  CA    . LYS A 1 336 ? -5.37600  28.39100  -16.00800 1.000 45.94249  ? 302 LYS A CA    1 
ATOM   2175 C  C     . LYS A 1 336 ? -6.62600  29.15400  -16.43200 1.000 50.75162  ? 302 LYS A C     1 
ATOM   2176 O  O     . LYS A 1 336 ? -6.60200  30.38600  -16.50700 1.000 53.94699  ? 302 LYS A O     1 
ATOM   2177 C  CB    . LYS A 1 336 ? -4.13100  29.06100  -16.61200 1.000 53.51506  ? 302 LYS A CB    1 
ATOM   2178 C  CG    . LYS A 1 336 ? -2.87500  28.19800  -16.66000 1.000 67.11349  ? 302 LYS A CG    1 
ATOM   2179 C  CD    . LYS A 1 336 ? -1.67100  29.02300  -17.10000 1.000 82.28419  ? 302 LYS A CD    1 
ATOM   2180 C  CE    . LYS A 1 336 ? -1.26700  28.69900  -18.53500 1.000 86.48838  ? 302 LYS A CE    1 
ATOM   2181 N  NZ    . LYS A 1 336 ? -0.65400  29.87300  -19.22500 1.000 87.30331  ? 302 LYS A NZ    1 
ATOM   2182 N  N     . HIS A 1 337 ? -7.72400  28.45800  -16.70900 1.000 43.36598  ? 303 HIS A N     1 
ATOM   2183 C  CA    . HIS A 1 337 ? -8.96200  29.11600  -17.09800 1.000 41.63008  ? 303 HIS A CA    1 
ATOM   2184 C  C     . HIS A 1 337 ? -9.93900  29.15400  -15.93200 1.000 36.96747  ? 303 HIS A C     1 
ATOM   2185 O  O     . HIS A 1 337 ? -9.92000  28.29300  -15.05000 1.000 39.60643  ? 303 HIS A O     1 
ATOM   2186 C  CB    . HIS A 1 337 ? -9.60500  28.42100  -18.30200 1.000 38.10664  ? 303 HIS A CB    1 
ATOM   2187 C  CG    . HIS A 1 337 ? -8.99000  28.81700  -19.60400 1.000 42.07095  ? 303 HIS A CG    1 
ATOM   2188 N  ND1   . HIS A 1 337 ? -9.25200  30.02600  -20.21000 1.000 36.99011  ? 303 HIS A ND1   1 
ATOM   2189 C  CD2   . HIS A 1 337 ? -8.09100  28.18600  -20.39500 1.000 45.53396  ? 303 HIS A CD2   1 
ATOM   2190 C  CE1   . HIS A 1 337 ? -8.55200  30.11700  -21.32700 1.000 39.08858  ? 303 HIS A CE1   1 
ATOM   2191 N  NE2   . HIS A 1 337 ? -7.84000  29.01300  -21.46300 1.000 38.32626  ? 303 HIS A NE2   1 
ATOM   2192 N  N     . GLN A 1 338 ? -10.79200 30.17400  -15.93600 1.000 40.37032  ? 304 GLN A N     1 
ATOM   2193 C  CA    . GLN A 1 338 ? -11.80600 30.30300  -14.90200 1.000 40.50552  ? 304 GLN A CA    1 
ATOM   2194 C  C     . GLN A 1 338 ? -12.86200 29.21700  -15.06900 1.000 37.36748  ? 304 GLN A C     1 
ATOM   2195 O  O     . GLN A 1 338 ? -13.15100 28.76500  -16.18000 1.000 34.82952  ? 304 GLN A O     1 
ATOM   2196 C  CB    . GLN A 1 338 ? -12.44500 31.69100  -14.95600 1.000 40.35856  ? 304 GLN A CB    1 
ATOM   2197 C  CG    . GLN A 1 338 ? -11.45200 32.81700  -14.68800 1.000 44.44355  ? 304 GLN A CG    1 
ATOM   2198 C  CD    . GLN A 1 338 ? -12.01000 34.19000  -15.00600 1.000 51.42382  ? 304 GLN A CD    1 
ATOM   2199 O  OE1   . GLN A 1 338 ? -11.73500 35.15700  -14.29600 1.000 59.92591  ? 304 GLN A OE1   1 
ATOM   2200 N  NE2   . GLN A 1 338 ? -12.79000 34.28700  -16.07900 1.000 44.47265  ? 304 GLN A NE2   1 
ATOM   2201 N  N     . PHE A 1 339 ? -13.42800 28.77900  -13.94900 1.000 35.93170  ? 305 PHE A N     1 
ATOM   2202 C  CA    . PHE A 1 339 ? -14.35800 27.66400  -14.00700 1.000 39.58319  ? 305 PHE A CA    1 
ATOM   2203 C  C     . PHE A 1 339 ? -15.43500 27.82100  -12.94900 1.000 39.47616  ? 305 PHE A C     1 
ATOM   2204 O  O     . PHE A 1 339 ? -15.21900 28.43300  -11.90100 1.000 37.50178  ? 305 PHE A O     1 
ATOM   2205 C  CB    . PHE A 1 339 ? -13.64400 26.31300  -13.83700 1.000 32.35532  ? 305 PHE A CB    1 
ATOM   2206 C  CG    . PHE A 1 339 ? -12.83900 26.19200  -12.56700 1.000 43.62758  ? 305 PHE A CG    1 
ATOM   2207 C  CD1   . PHE A 1 339 ? -11.54300 26.68300  -12.50000 1.000 44.72067  ? 305 PHE A CD1   1 
ATOM   2208 C  CD2   . PHE A 1 339 ? -13.37100 25.56700  -11.45000 1.000 41.10807  ? 305 PHE A CD2   1 
ATOM   2209 C  CE1   . PHE A 1 339 ? -10.79500 26.56100  -11.34200 1.000 41.25279  ? 305 PHE A CE1   1 
ATOM   2210 C  CE2   . PHE A 1 339 ? -12.63000 25.44400  -10.28600 1.000 46.41126  ? 305 PHE A CE2   1 
ATOM   2211 C  CZ    . PHE A 1 339 ? -11.34100 25.94200  -10.23300 1.000 42.97808  ? 305 PHE A CZ    1 
ATOM   2212 N  N     . LEU A 1 340 ? -16.60500 27.26600  -13.25300 1.000 39.99723  ? 306 LEU A N     1 
ATOM   2213 C  CA    . LEU A 1 340 ? -17.68500 27.07900  -12.29300 1.000 34.73047  ? 306 LEU A CA    1 
ATOM   2214 C  C     . LEU A 1 340 ? -17.95600 25.58200  -12.24600 1.000 38.99232  ? 306 LEU A C     1 
ATOM   2215 O  O     . LEU A 1 340 ? -18.50900 25.01600  -13.19600 1.000 37.09953  ? 306 LEU A O     1 
ATOM   2216 C  CB    . LEU A 1 340 ? -18.93100 27.86800  -12.69500 1.000 35.43362  ? 306 LEU A CB    1 
ATOM   2217 C  CG    . LEU A 1 340 ? -20.16400 27.71500  -11.80100 1.000 34.60625  ? 306 LEU A CG    1 
ATOM   2218 C  CD1   . LEU A 1 340 ? -19.85300 28.15000  -10.37600 1.000 35.99467  ? 306 LEU A CD1   1 
ATOM   2219 C  CD2   . LEU A 1 340 ? -21.34100 28.50500  -12.36100 1.000 33.35057  ? 306 LEU A CD2   1 
ATOM   2220 N  N     . TRP A 1 341 ? -17.54000 24.94300  -11.16000 1.000 38.16630  ? 307 TRP A N     1 
ATOM   2221 C  CA    . TRP A 1 341 ? -17.58100 23.49300  -11.01700 1.000 35.88128  ? 307 TRP A CA    1 
ATOM   2222 C  C     . TRP A 1 341 ? -18.69000 23.11600  -10.04400 1.000 43.35360  ? 307 TRP A C     1 
ATOM   2223 O  O     . TRP A 1 341 ? -18.64800 23.50100  -8.87000  1.000 44.69149  ? 307 TRP A O     1 
ATOM   2224 C  CB    . TRP A 1 341 ? -16.23000 22.97000  -10.53300 1.000 44.51889  ? 307 TRP A CB    1 
ATOM   2225 C  CG    . TRP A 1 341 ? -16.06900 21.48900  -10.62000 1.000 38.50782  ? 307 TRP A CG    1 
ATOM   2226 C  CD1   . TRP A 1 341 ? -17.01000 20.57900  -11.00200 1.000 38.35456  ? 307 TRP A CD1   1 
ATOM   2227 C  CD2   . TRP A 1 341 ? -14.89000 20.74200  -10.30600 1.000 44.09686  ? 307 TRP A CD2   1 
ATOM   2228 N  NE1   . TRP A 1 341 ? -16.48800 19.30900  -10.94600 1.000 38.89874  ? 307 TRP A NE1   1 
ATOM   2229 C  CE2   . TRP A 1 341 ? -15.18700 19.38200  -10.52500 1.000 39.92578  ? 307 TRP A CE2   1 
ATOM   2230 C  CE3   . TRP A 1 341 ? -13.60900 21.09000  -9.86000  1.000 45.12007  ? 307 TRP A CE3   1 
ATOM   2231 C  CZ2   . TRP A 1 341 ? -14.25100 18.36900  -10.31300 1.000 48.99591  ? 307 TRP A CZ2   1 
ATOM   2232 C  CZ3   . TRP A 1 341 ? -12.68000 20.08300  -9.65100  1.000 44.45953  ? 307 TRP A CZ3   1 
ATOM   2233 C  CH2   . TRP A 1 341 ? -13.00600 18.73900  -9.87800  1.000 47.56739  ? 307 TRP A CH2   1 
ATOM   2234 N  N     . VAL A 1 342 ? -19.67100 22.36200  -10.53100 1.000 41.04937  ? 308 VAL A N     1 
ATOM   2235 C  CA    . VAL A 1 342 ? -20.78200 21.88000  -9.71800  1.000 39.40092  ? 308 VAL A CA    1 
ATOM   2236 C  C     . VAL A 1 342 ? -20.59400 20.38400  -9.51400  1.000 48.13530  ? 308 VAL A C     1 
ATOM   2237 O  O     . VAL A 1 342 ? -20.50200 19.62400  -10.48600 1.000 49.73770  ? 308 VAL A O     1 
ATOM   2238 C  CB    . VAL A 1 342 ? -22.14000 22.18400  -10.36800 1.000 41.88071  ? 308 VAL A CB    1 
ATOM   2239 C  CG1   . VAL A 1 342 ? -23.27900 21.79400  -9.43200  1.000 44.20475  ? 308 VAL A CG1   1 
ATOM   2240 C  CG2   . VAL A 1 342 ? -22.22900 23.65800  -10.73700 1.000 45.46898  ? 308 VAL A CG2   1 
ATOM   2241 N  N     . VAL A 1 343 ? -20.52300 19.96400  -8.25300  1.000 47.85816  ? 309 VAL A N     1 
ATOM   2242 C  CA    . VAL A 1 343 ? -20.36700 18.56200  -7.88300  1.000 55.57543  ? 309 VAL A CA    1 
ATOM   2243 C  C     . VAL A 1 343 ? -21.54000 18.16900  -6.99600  1.000 54.83871  ? 309 VAL A C     1 
ATOM   2244 O  O     . VAL A 1 343 ? -21.94400 18.93500  -6.11600  1.000 51.74914  ? 309 VAL A O     1 
ATOM   2245 C  CB    . VAL A 1 343 ? -19.03000 18.30800  -7.15600  1.000 58.00874  ? 309 VAL A CB    1 
ATOM   2246 C  CG1   . VAL A 1 343 ? -18.87200 16.83300  -6.83400  1.000 65.71521  ? 309 VAL A CG1   1 
ATOM   2247 C  CG2   . VAL A 1 343 ? -17.86100 18.80200  -7.98900  1.000 50.74090  ? 309 VAL A CG2   1 
ATOM   2248 N  N     . HIS A 1 344 ? -22.09200 16.98300  -7.23700  1.000 54.53449  ? 310 HIS A N     1 
ATOM   2249 C  CA    . HIS A 1 344 ? -23.19100 16.45300  -6.44400  1.000 53.72412  ? 310 HIS A CA    1 
ATOM   2250 C  C     . HIS A 1 344 ? -22.69900 15.29800  -5.58200  1.000 65.66716  ? 310 HIS A C     1 
ATOM   2251 O  O     . HIS A 1 344 ? -21.83400 14.52300  -6.00300  1.000 60.30013  ? 310 HIS A O     1 
ATOM   2252 C  CB    . HIS A 1 344 ? -24.34300 15.98300  -7.33600  1.000 55.55461  ? 310 HIS A CB    1 
ATOM   2253 C  CG    . HIS A 1 344 ? -25.01900 17.08800  -8.08700  1.000 65.99576  ? 310 HIS A CG    1 
ATOM   2254 N  ND1   . HIS A 1 344 ? -26.09200 17.78700  -7.57700  1.000 70.54431  ? 310 HIS A ND1   1 
ATOM   2255 C  CD2   . HIS A 1 344 ? -24.78200 17.60700  -9.31500  1.000 63.91339  ? 310 HIS A CD2   1 
ATOM   2256 C  CE1   . HIS A 1 344 ? -26.48400 18.69200  -8.45600  1.000 70.08667  ? 310 HIS A CE1   1 
ATOM   2257 N  NE2   . HIS A 1 344 ? -25.70500 18.60400  -9.51900  1.000 66.44201  ? 310 HIS A NE2   1 
ATOM   2258 N  N     . GLY A 1 345 ? -23.24400 15.19700  -4.37100  1.000 61.61563  ? 311 GLY A N     1 
ATOM   2259 C  CA    . GLY A 1 345 ? -22.92300 14.08300  -3.50000  1.000 72.26383  ? 311 GLY A CA    1 
ATOM   2260 C  C     . GLY A 1 345 ? -21.58300 14.16300  -2.80700  1.000 74.05488  ? 311 GLY A C     1 
ATOM   2261 O  O     . GLY A 1 345 ? -20.95100 13.12700  -2.57200  1.000 69.28615  ? 311 GLY A O     1 
ATOM   2262 N  N     . LYS A 1 346 ? -21.12200 15.36800  -2.47100  1.000 77.82105  ? 312 LYS A N     1 
ATOM   2263 C  CA    . LYS A 1 346 ? -19.87300 15.53900  -1.74200  1.000 76.79868  ? 312 LYS A CA    1 
ATOM   2264 C  C     . LYS A 1 346 ? -20.04200 16.40600  -0.50200  1.000 77.36351  ? 312 LYS A C     1 
ATOM   2265 O  O     . LYS A 1 346 ? -19.03800 16.80100  0.10400   1.000 68.99456  ? 312 LYS A O     1 
ATOM   2266 C  CB    . LYS A 1 346 ? -18.79300 16.13500  -2.65200  1.000 68.95305  ? 312 LYS A CB    1 
ATOM   2267 C  CG    . LYS A 1 346 ? -18.30300 15.18600  -3.73300  1.000 69.76385  ? 312 LYS A CG    1 
ATOM   2268 C  CD    . LYS A 1 346 ? -17.68400 13.93500  -3.13700  1.000 75.30206  ? 312 LYS A CD    1 
ATOM   2269 C  CE    . LYS A 1 346 ? -17.22600 12.97900  -4.22400  1.000 67.33481  ? 312 LYS A CE    1 
ATOM   2270 N  NZ    . LYS A 1 346 ? -16.57000 11.77000  -3.65000  1.000 81.37813  ? 312 LYS A NZ    1 
ATOM   2271 N  N     . GLU A 1 347 ? -21.27800 16.71400  -0.11400  1.000 83.08778  ? 313 GLU A N     1 
ATOM   2272 C  CA    . GLU A 1 347 ? -21.52100 17.51300  1.08000   1.000 90.96247  ? 313 GLU A CA    1 
ATOM   2273 C  C     . GLU A 1 347 ? -21.15400 16.72000  2.32800   1.000 88.92193  ? 313 GLU A C     1 
ATOM   2274 O  O     . GLU A 1 347 ? -21.60500 15.58500  2.51200   1.000 77.37681  ? 313 GLU A O     1 
ATOM   2275 C  CB    . GLU A 1 347 ? -22.98600 17.94500  1.13600   1.000 92.86451  ? 313 GLU A CB    1 
ATOM   2276 C  CG    . GLU A 1 347 ? -23.35200 19.03300  0.14000   1.000 103.20528 ? 313 GLU A CG    1 
ATOM   2277 C  CD    . GLU A 1 347 ? -24.70000 18.79600  -0.51500  1.000 102.94307 ? 313 GLU A CD    1 
ATOM   2278 O  OE1   . GLU A 1 347 ? -24.74300 18.10900  -1.56100  1.000 84.57462  ? 313 GLU A OE1   1 
ATOM   2279 O  OE2   . GLU A 1 347 ? -25.71400 19.29600  0.01600   1.000 103.29703 ? 313 GLU A OE2   1 
ATOM   2280 N  N     . GLY A 1 348 ? -20.33100 17.31600  3.18200   1.000 87.83070  ? 314 GLY A N     1 
ATOM   2281 C  CA    . GLY A 1 348 ? -19.90100 16.63700  4.39000   1.000 96.22230  ? 314 GLY A CA    1 
ATOM   2282 C  C     . GLY A 1 348 ? -18.89100 15.53700  4.14900   1.000 97.98443  ? 314 GLY A C     1 
ATOM   2283 O  O     . GLY A 1 348 ? -18.94100 14.49600  4.81700   1.000 100.64068 ? 314 GLY A O     1 
ATOM   2284 N  N     . GLU A 1 349 ? -17.97700 15.73600  3.20200   1.000 84.98339  ? 315 GLU A N     1 
ATOM   2285 C  CA    . GLU A 1 349 ? -16.90300 14.79100  2.93900   1.000 85.99069  ? 315 GLU A CA    1 
ATOM   2286 C  C     . GLU A 1 349 ? -15.58100 15.53900  2.89900   1.000 79.08685  ? 315 GLU A C     1 
ATOM   2287 O  O     . GLU A 1 349 ? -15.51400 16.67200  2.41400   1.000 85.16507  ? 315 GLU A O     1 
ATOM   2288 C  CB    . GLU A 1 349 ? -17.12500 14.03100  1.62100   1.000 83.25338  ? 315 GLU A CB    1 
ATOM   2289 C  CG    . GLU A 1 349 ? -16.04100 13.00500  1.30300   1.000 83.33808  ? 315 GLU A CG    1 
ATOM   2290 C  CD    . GLU A 1 349 ? -16.40400 12.10900  0.13300   1.000 90.43257  ? 315 GLU A CD    1 
ATOM   2291 O  OE1   . GLU A 1 349 ? -17.56500 12.17300  -0.32500  1.000 84.85081  ? 315 GLU A OE1   1 
ATOM   2292 O  OE2   . GLU A 1 349 ? -15.53400 11.33300  -0.32100  1.000 89.69230  ? 315 GLU A OE2   1 
ATOM   2293 N  N     . ASP A 1 350 ? -14.53600 14.90300  3.42500   1.000 78.28688  ? 316 ASP A N     1 
ATOM   2294 C  CA    . ASP A 1 350 ? -13.20800 15.49800  3.40700   1.000 81.30445  ? 316 ASP A CA    1 
ATOM   2295 C  C     . ASP A 1 350 ? -12.76400 15.73700  1.97100   1.000 69.36747  ? 316 ASP A C     1 
ATOM   2296 O  O     . ASP A 1 350 ? -12.63700 14.79300  1.18300   1.000 60.22927  ? 316 ASP A O     1 
ATOM   2297 C  CB    . ASP A 1 350 ? -12.21400 14.59400  4.13400   1.000 78.82809  ? 316 ASP A CB    1 
ATOM   2298 C  CG    . ASP A 1 350 ? -10.98800 15.34500  4.61400   1.000 95.21522  ? 316 ASP A CG    1 
ATOM   2299 O  OD1   . ASP A 1 350 ? -11.14400 16.27900  5.43000   1.000 105.18213 ? 316 ASP A OD1   1 
ATOM   2300 O  OD2   . ASP A 1 350 ? -9.87000  15.00300  4.17500   1.000 99.82308  ? 316 ASP A OD2   1 
ATOM   2301 N  N     . GLU A 1 351 ? -12.53500 17.00800  1.63500   1.000 59.22864  ? 317 GLU A N     1 
ATOM   2302 C  CA    . GLU A 1 351 ? -12.14600 17.37300  0.28000   1.000 68.31928  ? 317 GLU A CA    1 
ATOM   2303 C  C     . GLU A 1 351 ? -10.83300 16.73200  -0.14000  1.000 69.60760  ? 317 GLU A C     1 
ATOM   2304 O  O     . GLU A 1 351 ? -10.59100 16.57700  -1.34100  1.000 66.05080  ? 317 GLU A O     1 
ATOM   2305 C  CB    . GLU A 1 351 ? -12.05400 18.89400  0.16200   1.000 65.47804  ? 317 GLU A CB    1 
ATOM   2306 C  CG    . GLU A 1 351 ? -13.38300 19.59400  0.38400   1.000 57.33230  ? 317 GLU A CG    1 
ATOM   2307 C  CD    . GLU A 1 351 ? -13.25900 21.10100  0.38300   1.000 69.05508  ? 317 GLU A CD    1 
ATOM   2308 O  OE1   . GLU A 1 351 ? -12.11600 21.60300  0.44100   1.000 75.28393  ? 317 GLU A OE1   1 
ATOM   2309 O  OE2   . GLU A 1 351 ? -14.30400 21.78300  0.31700   1.000 67.06520  ? 317 GLU A OE2   1 
ATOM   2310 N  N     . ASP A 1 352 ? -9.98500  16.34500  0.81600   1.000 65.77416  ? 318 ASP A N     1 
ATOM   2311 C  CA    . ASP A 1 352 ? -8.74400  15.66100  0.47000   1.000 66.09337  ? 318 ASP A CA    1 
ATOM   2312 C  C     . ASP A 1 352 ? -8.99600  14.29500  -0.15600  1.000 61.22682  ? 318 ASP A C     1 
ATOM   2313 O  O     . ASP A 1 352 ? -8.10700  13.75900  -0.82700  1.000 62.21937  ? 318 ASP A O     1 
ATOM   2314 C  CB    . ASP A 1 352 ? -7.86100  15.51600  1.70900   1.000 77.46336  ? 318 ASP A CB    1 
ATOM   2315 C  CG    . ASP A 1 352 ? -7.38500  16.85500  2.24500   1.000 92.19137  ? 318 ASP A CG    1 
ATOM   2316 O  OD1   . ASP A 1 352 ? -8.13900  17.84400  2.12800   1.000 88.07218  ? 318 ASP A OD1   1 
ATOM   2317 O  OD2   . ASP A 1 352 ? -6.25900  16.92000  2.78200   1.000 111.53571 ? 318 ASP A OD2   1 
ATOM   2318 N  N     . ASN A 1 353 ? -10.18800 13.72700  0.03800   1.000 56.60911  ? 319 ASN A N     1 
ATOM   2319 C  CA    . ASN A 1 353 ? -10.51200 12.43300  -0.54800  1.000 65.92972  ? 319 ASN A CA    1 
ATOM   2320 C  C     . ASN A 1 353 ? -10.74900 12.51900  -2.05100  1.000 64.48874  ? 319 ASN A C     1 
ATOM   2321 O  O     . ASN A 1 353 ? -10.57600 11.51500  -2.75000  1.000 60.09303  ? 319 ASN A O     1 
ATOM   2322 C  CB    . ASN A 1 353 ? -11.74400 11.84000  0.13700   1.000 63.55371  ? 319 ASN A CB    1 
ATOM   2323 C  CG    . ASN A 1 353 ? -11.41500 11.18900  1.46500   1.000 81.85157  ? 319 ASN A CG    1 
ATOM   2324 O  OD1   . ASN A 1 353 ? -12.23100 11.19500  2.38700   1.000 73.92750  ? 319 ASN A OD1   1 
ATOM   2325 N  ND2   . ASN A 1 353 ? -10.21200 10.63000  1.57500   1.000 82.96657  ? 319 ASN A ND2   1 
ATOM   2326 N  N     . TRP A 1 354 ? -11.14600 13.68800  -2.56400  1.000 64.03603  ? 320 TRP A N     1 
ATOM   2327 C  CA    . TRP A 1 354 ? -11.45100 13.81800  -3.98300  1.000 64.04090  ? 320 TRP A CA    1 
ATOM   2328 C  C     . TRP A 1 354 ? -10.87400 15.08300  -4.60900  1.000 64.90937  ? 320 TRP A C     1 
ATOM   2329 O  O     . TRP A 1 354 ? -11.16000 15.35400  -5.78200  1.000 58.35116  ? 320 TRP A O     1 
ATOM   2330 C  CB    . TRP A 1 354 ? -12.96900 13.77100  -4.21000  1.000 67.74374  ? 320 TRP A CB    1 
ATOM   2331 C  CG    . TRP A 1 354 ? -13.74200 14.78200  -3.41800  1.000 67.81421  ? 320 TRP A CG    1 
ATOM   2332 C  CD1   . TRP A 1 354 ? -14.02400 14.73500  -2.08400  1.000 65.13094  ? 320 TRP A CD1   1 
ATOM   2333 C  CD2   . TRP A 1 354 ? -14.34900 15.98400  -3.91400  1.000 62.72832  ? 320 TRP A CD2   1 
ATOM   2334 N  NE1   . TRP A 1 354 ? -14.76100 15.83400  -1.71600  1.000 66.24931  ? 320 TRP A NE1   1 
ATOM   2335 C  CE2   . TRP A 1 354 ? -14.97500 16.61500  -2.82100  1.000 63.79721  ? 320 TRP A CE2   1 
ATOM   2336 C  CE3   . TRP A 1 354 ? -14.42300 16.58600  -5.17400  1.000 59.29559  ? 320 TRP A CE3   1 
ATOM   2337 C  CZ2   . TRP A 1 354 ? -15.66300 17.82100  -2.94900  1.000 65.99791  ? 320 TRP A CZ2   1 
ATOM   2338 C  CZ3   . TRP A 1 354 ? -15.10700 17.78400  -5.29800  1.000 60.92869  ? 320 TRP A CZ3   1 
ATOM   2339 C  CH2   . TRP A 1 354 ? -15.71800 18.38800  -4.19200  1.000 58.35791  ? 320 TRP A CH2   1 
ATOM   2340 N  N     . LEU A 1 355 ? -10.07800 15.85800  -3.87900  1.000 63.43125  ? 321 LEU A N     1 
ATOM   2341 C  CA    . LEU A 1 355 ? -9.42900  17.04800  -4.41100  1.000 66.34608  ? 321 LEU A CA    1 
ATOM   2342 C  C     . LEU A 1 355 ? -7.97500  17.06900  -3.96700  1.000 65.73688  ? 321 LEU A C     1 
ATOM   2343 O  O     . LEU A 1 355 ? -7.63800  16.51100  -2.91700  1.000 67.69827  ? 321 LEU A O     1 
ATOM   2344 C  CB    . LEU A 1 355 ? -10.12000 18.34100  -3.94800  1.000 54.75919  ? 321 LEU A CB    1 
ATOM   2345 C  CG    . LEU A 1 355 ? -11.57000 18.54400  -4.38500  1.000 65.84249  ? 321 LEU A CG    1 
ATOM   2346 C  CD1   . LEU A 1 355 ? -12.19000 19.73100  -3.66500  1.000 55.82755  ? 321 LEU A CD1   1 
ATOM   2347 C  CD2   . LEU A 1 355 ? -11.64100 18.72600  -5.89700  1.000 54.68460  ? 321 LEU A CD2   1 
ATOM   2348 N  N     . PRO A 1 356 ? -7.09700  17.69900  -4.74600  1.000 68.79127  ? 322 PRO A N     1 
ATOM   2349 C  CA    . PRO A 1 356 ? -5.70100  17.84800  -4.31600  1.000 66.07768  ? 322 PRO A CA    1 
ATOM   2350 C  C     . PRO A 1 356 ? -5.60600  18.69600  -3.05700  1.000 74.53128  ? 322 PRO A C     1 
ATOM   2351 O  O     . PRO A 1 356 ? -6.55600  19.36800  -2.64400  1.000 70.84496  ? 322 PRO A O     1 
ATOM   2352 C  CB    . PRO A 1 356 ? -5.02600  18.53500  -5.50800  1.000 63.53283  ? 322 PRO A CB    1 
ATOM   2353 C  CG    . PRO A 1 356 ? -5.93500  18.27400  -6.67000  1.000 63.80645  ? 322 PRO A CG    1 
ATOM   2354 C  CD    . PRO A 1 356 ? -7.31600  18.23400  -6.10000  1.000 48.23229  ? 322 PRO A CD    1 
ATOM   2355 N  N     . LYS A 1 357 ? -4.42500  18.66000  -2.44200  1.000 79.15227  ? 323 LYS A N     1 
ATOM   2356 C  CA    . LYS A 1 357 ? -4.20000  19.36100  -1.18400  1.000 69.00859  ? 323 LYS A CA    1 
ATOM   2357 C  C     . LYS A 1 357 ? -4.41500  20.85900  -1.35500  1.000 67.96601  ? 323 LYS A C     1 
ATOM   2358 O  O     . LYS A 1 357 ? -3.71700  21.51100  -2.13900  1.000 75.06924  ? 323 LYS A O     1 
ATOM   2359 C  CB    . LYS A 1 357 ? -2.78700  19.08100  -0.67700  1.000 75.68569  ? 323 LYS A CB    1 
ATOM   2360 N  N     . GLY A 1 358 ? -5.39000  21.39600  -0.62500  1.000 65.80784  ? 324 GLY A N     1 
ATOM   2361 C  CA    . GLY A 1 358 ? -5.64800  22.82700  -0.64300  1.000 75.42393  ? 324 GLY A CA    1 
ATOM   2362 C  C     . GLY A 1 358 ? -6.11700  23.36500  -1.97600  1.000 72.90318  ? 324 GLY A C     1 
ATOM   2363 O  O     . GLY A 1 358 ? -5.83800  24.52300  -2.30100  1.000 66.20087  ? 324 GLY A O     1 
ATOM   2364 N  N     . PHE A 1 359 ? -6.83400  22.55400  -2.75800  1.000 64.19831  ? 325 PHE A N     1 
ATOM   2365 C  CA    . PHE A 1 359 ? -7.29300  23.00700  -4.06800  1.000 67.19443  ? 325 PHE A CA    1 
ATOM   2366 C  C     . PHE A 1 359 ? -8.21800  24.21000  -3.94600  1.000 70.07240  ? 325 PHE A C     1 
ATOM   2367 O  O     . PHE A 1 359 ? -8.11900  25.16100  -4.73100  1.000 64.52578  ? 325 PHE A O     1 
ATOM   2368 C  CB    . PHE A 1 359 ? -7.99400  21.86500  -4.80300  1.000 57.35708  ? 325 PHE A CB    1 
ATOM   2369 C  CG    . PHE A 1 359 ? -8.52700  22.25100  -6.15400  1.000 61.22549  ? 325 PHE A CG    1 
ATOM   2370 C  CD1   . PHE A 1 359 ? -7.67600  22.37400  -7.24100  1.000 57.64797  ? 325 PHE A CD1   1 
ATOM   2371 C  CD2   . PHE A 1 359 ? -9.88000  22.49100  -6.33800  1.000 53.93371  ? 325 PHE A CD2   1 
ATOM   2372 C  CE1   . PHE A 1 359 ? -8.16400  22.72900  -8.48800  1.000 57.81082  ? 325 PHE A CE1   1 
ATOM   2373 C  CE2   . PHE A 1 359 ? -10.37500 22.84700  -7.58100  1.000 56.38237  ? 325 PHE A CE2   1 
ATOM   2374 C  CZ    . PHE A 1 359 ? -9.51400  22.96600  -8.65800  1.000 53.99844  ? 325 PHE A CZ    1 
ATOM   2375 N  N     . VAL A 1 360 ? -9.11800  24.19300  -2.96100  1.000 70.29043  ? 326 VAL A N     1 
ATOM   2376 C  CA    . VAL A 1 360 ? -10.07900 25.28200  -2.82000  1.000 80.54242  ? 326 VAL A CA    1 
ATOM   2377 C  C     . VAL A 1 360 ? -9.40600  26.55200  -2.31400  1.000 80.64391  ? 326 VAL A C     1 
ATOM   2378 O  O     . VAL A 1 360 ? -9.85300  27.66300  -2.62800  1.000 85.35014  ? 326 VAL A O     1 
ATOM   2379 C  CB    . VAL A 1 360 ? -11.23600 24.85200  -1.90000  1.000 75.43736  ? 326 VAL A CB    1 
ATOM   2380 C  CG1   . VAL A 1 360 ? -12.44300 25.74600  -2.11400  1.000 78.70396  ? 326 VAL A CG1   1 
ATOM   2381 C  CG2   . VAL A 1 360 ? -11.59800 23.40600  -2.16400  1.000 68.56682  ? 326 VAL A CG2   1 
ATOM   2382 N  N     . GLU A 1 361 ? -8.33200  26.42200  -1.53300  1.000 79.73806  ? 327 GLU A N     1 
ATOM   2383 C  CA    . GLU A 1 361 ? -7.64000  27.60400  -1.02600  1.000 95.84598  ? 327 GLU A CA    1 
ATOM   2384 C  C     . GLU A 1 361 ? -7.09900  28.45000  -2.17100  1.000 80.31745  ? 327 GLU A C     1 
ATOM   2385 O  O     . GLU A 1 361 ? -7.46400  29.62200  -2.32300  1.000 81.11560  ? 327 GLU A O     1 
ATOM   2386 C  CB    . GLU A 1 361 ? -6.51400  27.19300  -0.07400  1.000 96.41988  ? 327 GLU A CB    1 
ATOM   2387 C  CG    . GLU A 1 361 ? -6.99600  26.59300  1.23900   1.000 106.65099 ? 327 GLU A CG    1 
ATOM   2388 C  CD    . GLU A 1 361 ? -5.86600  26.37000  2.23100   1.000 125.32388 ? 327 GLU A CD    1 
ATOM   2389 O  OE1   . GLU A 1 361 ? -4.70200  26.66500  1.88500   1.000 120.86180 ? 327 GLU A OE1   1 
ATOM   2390 O  OE2   . GLU A 1 361 ? -6.14200  25.90100  3.35600   1.000 127.69887 ? 327 GLU A OE2   1 
ATOM   2391 N  N     . ARG A 1 362 ? -6.22800  27.86700  -2.99600  1.000 77.44127  ? 328 ARG A N     1 
ATOM   2392 C  CA    . ARG A 1 362 ? -5.70400  28.59600  -4.14400  1.000 78.65107  ? 328 ARG A CA    1 
ATOM   2393 C  C     . ARG A 1 362 ? -6.79100  28.92600  -5.15400  1.000 75.44619  ? 328 ARG A C     1 
ATOM   2394 O  O     . ARG A 1 362 ? -6.64000  29.88200  -5.91800  1.000 76.55831  ? 328 ARG A O     1 
ATOM   2395 C  CB    . ARG A 1 362 ? -4.58800  27.79700  -4.81800  1.000 68.71994  ? 328 ARG A CB    1 
ATOM   2396 C  CG    . ARG A 1 362 ? -4.59900  26.33400  -4.45100  1.000 72.13053  ? 328 ARG A CG    1 
ATOM   2397 C  CD    . ARG A 1 362 ? -3.57200  25.52700  -5.22200  1.000 75.24672  ? 328 ARG A CD    1 
ATOM   2398 N  NE    . ARG A 1 362 ? -3.58300  24.13500  -4.78700  1.000 82.34241  ? 328 ARG A NE    1 
ATOM   2399 C  CZ    . ARG A 1 362 ? -3.09800  23.12000  -5.48800  1.000 85.05992  ? 328 ARG A CZ    1 
ATOM   2400 N  NH1   . ARG A 1 362 ? -2.52100  23.30600  -6.66400  1.000 81.67864  ? 328 ARG A NH1   1 
ATOM   2401 N  NH2   . ARG A 1 362 ? -3.18600  21.88800  -4.99300  1.000 88.58090  ? 328 ARG A NH2   1 
ATOM   2402 N  N     . MET A 1 363 ? -7.88800  28.16900  -5.16300  1.000 71.46135  ? 329 MET A N     1 
ATOM   2403 C  CA    . MET A 1 363 ? -8.96100  28.43500  -6.11500  1.000 74.32567  ? 329 MET A CA    1 
ATOM   2404 C  C     . MET A 1 363 ? -9.56000  29.82200  -5.90000  1.000 75.93656  ? 329 MET A C     1 
ATOM   2405 O  O     . MET A 1 363 ? -9.82300  30.54800  -6.86600  1.000 70.57591  ? 329 MET A O     1 
ATOM   2406 C  CB    . MET A 1 363 ? -10.03600 27.35200  -5.99800  1.000 76.67000  ? 329 MET A CB    1 
ATOM   2407 C  CG    . MET A 1 363 ? -11.16400 27.47800  -7.00100  1.000 63.44739  ? 329 MET A CG    1 
ATOM   2408 S  SD    . MET A 1 363 ? -12.70100 26.69800  -6.46000  1.000 76.45158  ? 329 MET A SD    1 
ATOM   2409 C  CE    . MET A 1 363 ? -13.16900 27.72900  -5.07100  1.000 56.87584  ? 329 MET A CE    1 
ATOM   2410 N  N     . LYS A 1 364 ? -9.77200  30.21200  -4.64000  1.000 76.06264  ? 330 LYS A N     1 
ATOM   2411 C  CA    . LYS A 1 364 ? -10.32300 31.52700  -4.32700  1.000 84.21835  ? 330 LYS A CA    1 
ATOM   2412 C  C     . LYS A 1 364 ? -9.26000  32.61100  -4.22100  1.000 83.63336  ? 330 LYS A C     1 
ATOM   2413 O  O     . LYS A 1 364 ? -9.56700  33.78700  -4.45100  1.000 91.35764  ? 330 LYS A O     1 
ATOM   2414 C  CB    . LYS A 1 364 ? -11.12100 31.48100  -3.02000  1.000 82.70563  ? 330 LYS A CB    1 
ATOM   2415 C  CG    . LYS A 1 364 ? -12.27200 30.50200  -3.03200  1.000 87.70150  ? 330 LYS A CG    1 
ATOM   2416 C  CD    . LYS A 1 364 ? -13.05500 30.53400  -1.72900  1.000 98.62429  ? 330 LYS A CD    1 
ATOM   2417 C  CE    . LYS A 1 364 ? -14.51800 30.18600  -1.97200  1.000 113.55402 ? 330 LYS A CE    1 
ATOM   2418 N  NZ    . LYS A 1 364 ? -15.43300 30.79700  -0.96500  1.000 116.71034 ? 330 LYS A NZ    1 
ATOM   2419 N  N     . GLU A 1 365 ? -8.02200  32.25200  -3.87400  1.000 81.10961  ? 331 GLU A N     1 
ATOM   2420 C  CA    . GLU A 1 365 ? -6.97900  33.26500  -3.75500  1.000 85.52245  ? 331 GLU A CA    1 
ATOM   2421 C  C     . GLU A 1 365 ? -6.61300  33.84500  -5.11600  1.000 78.12112  ? 331 GLU A C     1 
ATOM   2422 O  O     . GLU A 1 365 ? -6.46200  35.06400  -5.25600  1.000 85.99087  ? 331 GLU A O     1 
ATOM   2423 C  CB    . GLU A 1 365 ? -5.74900  32.67800  -3.06400  1.000 92.61977  ? 331 GLU A CB    1 
ATOM   2424 C  CG    . GLU A 1 365 ? -4.70400  33.71400  -2.68400  1.000 109.77798 ? 331 GLU A CG    1 
ATOM   2425 C  CD    . GLU A 1 365 ? -3.61000  33.14400  -1.80000  1.000 114.27233 ? 331 GLU A CD    1 
ATOM   2426 O  OE1   . GLU A 1 365 ? -3.61300  31.91700  -1.56700  1.000 103.30527 ? 331 GLU A OE1   1 
ATOM   2427 O  OE2   . GLU A 1 365 ? -2.74900  33.92500  -1.33900  1.000 119.20777 ? 331 GLU A OE2   1 
ATOM   2428 N  N     . GLU A 1 366 ? -6.47600  32.99500  -6.13300  1.000 82.37569  ? 332 GLU A N     1 
ATOM   2429 C  CA    . GLU A 1 366 ? -6.21100  33.47800  -7.48300  1.000 77.92796  ? 332 GLU A CA    1 
ATOM   2430 C  C     . GLU A 1 366 ? -7.47300  33.89900  -8.22600  1.000 58.85695  ? 332 GLU A C     1 
ATOM   2431 O  O     . GLU A 1 366 ? -7.37400  34.27800  -9.39800  1.000 74.53852  ? 332 GLU A O     1 
ATOM   2432 C  CB    . GLU A 1 366 ? -5.46700  32.41600  -8.29500  1.000 79.48021  ? 332 GLU A CB    1 
ATOM   2433 C  CG    . GLU A 1 366 ? -4.67300  31.44300  -7.45600  1.000 86.38899  ? 332 GLU A CG    1 
ATOM   2434 C  CD    . GLU A 1 366 ? -4.04200  30.34500  -8.28500  1.000 89.62489  ? 332 GLU A CD    1 
ATOM   2435 O  OE1   . GLU A 1 366 ? -2.98200  30.58600  -8.89400  1.000 97.88686  ? 332 GLU A OE1   1 
ATOM   2436 O  OE2   . GLU A 1 366 ? -4.61700  29.23400  -8.33400  1.000 90.89809  ? 332 GLU A OE2   1 
ATOM   2437 N  N     . LYS A 1 367 ? -8.63900  33.85600  -7.57700  1.000 63.92121  ? 333 LYS A N     1 
ATOM   2438 C  CA    . LYS A 1 367 ? -9.89800  34.31600  -8.16800  1.000 69.06345  ? 333 LYS A CA    1 
ATOM   2439 C  C     . LYS A 1 367 ? -10.19700 33.58500  -9.47500  1.000 69.43059  ? 333 LYS A C     1 
ATOM   2440 O  O     . LYS A 1 367 ? -10.74500 34.16000  -10.42000 1.000 69.84212  ? 333 LYS A O     1 
ATOM   2441 C  CB    . LYS A 1 367 ? -9.88700  35.83200  -8.38400  1.000 73.98161  ? 333 LYS A CB    1 
ATOM   2442 C  CG    . LYS A 1 367 ? -9.74400  36.65200  -7.10800  1.000 71.85979  ? 333 LYS A CG    1 
ATOM   2443 C  CD    . LYS A 1 367 ? -10.98100 36.53200  -6.22900  1.000 81.45387  ? 333 LYS A CD    1 
ATOM   2444 C  CE    . LYS A 1 367 ? -10.89200 37.45200  -5.01800  1.000 88.13751  ? 333 LYS A CE    1 
ATOM   2445 N  NZ    . LYS A 1 367 ? -12.10300 37.36700  -4.15700  1.000 84.96377  ? 333 LYS A NZ    1 
ATOM   2446 N  N     . LYS A 1 368 ? -9.83400  32.30500  -9.53000  1.000 63.94987  ? 334 LYS A N     1 
ATOM   2447 C  CA    . LYS A 1 368 ? -9.95600  31.54700  -10.76800 1.000 65.72238  ? 334 LYS A CA    1 
ATOM   2448 C  C     . LYS A 1 368 ? -11.28300 30.80300  -10.86100 1.000 55.96476  ? 334 LYS A C     1 
ATOM   2449 O  O     . LYS A 1 368 ? -11.98500 30.90700  -11.87100 1.000 53.64117  ? 334 LYS A O     1 
ATOM   2450 C  CB    . LYS A 1 368 ? -8.79100  30.56400  -10.89900 1.000 71.32578  ? 334 LYS A CB    1 
ATOM   2451 C  CG    . LYS A 1 368 ? -7.52700  31.17600  -11.48400 1.000 77.29714  ? 334 LYS A CG    1 
ATOM   2452 C  CD    . LYS A 1 368 ? -7.59100  31.24900  -12.99900 1.000 58.62308  ? 334 LYS A CD    1 
ATOM   2453 C  CE    . LYS A 1 368 ? -6.87900  32.48800  -13.51900 1.000 66.47418  ? 334 LYS A CE    1 
ATOM   2454 N  NZ    . LYS A 1 368 ? -6.11800  32.21000  -14.76800 1.000 67.08183  ? 334 LYS A NZ    1 
ATOM   2455 N  N     . GLY A 1 369 ? -11.65200 30.05700  -9.81900  1.000 46.47431  ? 335 GLY A N     1 
ATOM   2456 C  CA    . GLY A 1 369 ? -12.78000 29.16000  -9.90200  1.000 50.17806  ? 335 GLY A CA    1 
ATOM   2457 C  C     . GLY A 1 369 ? -13.67700 29.24300  -8.68500  1.000 56.09738  ? 335 GLY A C     1 
ATOM   2458 O  O     . GLY A 1 369 ? -13.31900 29.80100  -7.64400  1.000 48.72202  ? 335 GLY A O     1 
ATOM   2459 N  N     . MET A 1 370 ? -14.86600 28.66700  -8.84300  1.000 47.66780  ? 336 MET A N     1 
ATOM   2460 C  CA    . MET A 1 370 ? -15.84100 28.52800  -7.77500  1.000 43.94889  ? 336 MET A CA    1 
ATOM   2461 C  C     . MET A 1 370 ? -16.35900 27.09700  -7.79700  1.000 55.20988  ? 336 MET A C     1 
ATOM   2462 O  O     . MET A 1 370 ? -16.68400 26.56800  -8.86600  1.000 42.46477  ? 336 MET A O     1 
ATOM   2463 C  CB    . MET A 1 370 ? -16.99200 29.52300  -7.94400  1.000 44.92552  ? 336 MET A CB    1 
ATOM   2464 C  CG    . MET A 1 370 ? -18.29700 29.07400  -7.31100  1.000 54.84360  ? 336 MET A CG    1 
ATOM   2465 S  SD    . MET A 1 370 ? -19.40500 30.45100  -6.96600  1.000 61.58392  ? 336 MET A SD    1 
ATOM   2466 C  CE    . MET A 1 370 ? -18.33400 31.50900  -5.99100  1.000 49.33213  ? 336 MET A CE    1 
ATOM   2467 N  N     . LEU A 1 371 ? -16.40800 26.46600  -6.62800  1.000 45.04190  ? 337 LEU A N     1 
ATOM   2468 C  CA    . LEU A 1 371 ? -16.87600 25.09300  -6.49300  1.000 48.78412  ? 337 LEU A CA    1 
ATOM   2469 C  C     . LEU A 1 371 ? -18.16800 25.09800  -5.68700  1.000 49.12793  ? 337 LEU A C     1 
ATOM   2470 O  O     . LEU A 1 371 ? -18.19300 25.58900  -4.55400  1.000 44.31065  ? 337 LEU A O     1 
ATOM   2471 C  CB    . LEU A 1 371 ? -15.81400 24.21800  -5.82500  1.000 53.70337  ? 337 LEU A CB    1 
ATOM   2472 C  CG    . LEU A 1 371 ? -16.17500 22.74900  -5.59200  1.000 52.16872  ? 337 LEU A CG    1 
ATOM   2473 C  CD1   . LEU A 1 371 ? -15.70200 21.87700  -6.74500  1.000 48.18116  ? 337 LEU A CD1   1 
ATOM   2474 C  CD2   . LEU A 1 371 ? -15.58800 22.26300  -4.27700  1.000 56.79808  ? 337 LEU A CD2   1 
ATOM   2475 N  N     . ILE A 1 372 ? -19.23600 24.56400  -6.27700  1.000 47.63492  ? 338 ILE A N     1 
ATOM   2476 C  CA    . ILE A 1 372 ? -20.55000 24.50500  -5.64900  1.000 53.18062  ? 338 ILE A CA    1 
ATOM   2477 C  C     . ILE A 1 372 ? -20.90600 23.04400  -5.41100  1.000 53.59316  ? 338 ILE A C     1 
ATOM   2478 O  O     . ILE A 1 372 ? -20.79700 22.21600  -6.32300  1.000 56.56796  ? 338 ILE A O     1 
ATOM   2479 C  CB    . ILE A 1 372 ? -21.62700 25.19200  -6.50800  1.000 48.32470  ? 338 ILE A CB    1 
ATOM   2480 C  CG1   . ILE A 1 372 ? -21.20600 26.62100  -6.86000  1.000 48.18380  ? 338 ILE A CG1   1 
ATOM   2481 C  CG2   . ILE A 1 372 ? -22.96400 25.18600  -5.77900  1.000 58.27264  ? 338 ILE A CG2   1 
ATOM   2482 C  CD1   . ILE A 1 372 ? -21.32800 27.59800  -5.71700  1.000 65.54115  ? 338 ILE A CD1   1 
ATOM   2483 N  N     . LYS A 1 373 ? -21.33300 22.73200  -4.19100  1.000 58.55654  ? 339 LYS A N     1 
ATOM   2484 C  CA    . LYS A 1 373 ? -21.72200 21.38000  -3.79500  1.000 59.98984  ? 339 LYS A CA    1 
ATOM   2485 C  C     . LYS A 1 373 ? -23.23400 21.38200  -3.58100  1.000 61.12639  ? 339 LYS A C     1 
ATOM   2486 O  O     . LYS A 1 373 ? -23.72400 21.74500  -2.51000  1.000 78.96267  ? 339 LYS A O     1 
ATOM   2487 C  CB    . LYS A 1 373 ? -20.97600 20.93800  -2.53200  1.000 61.77783  ? 339 LYS A CB    1 
ATOM   2488 C  CG    . LYS A 1 373 ? -19.46000 20.96700  -2.65400  1.000 62.87902  ? 339 LYS A CG    1 
ATOM   2489 C  CD    . LYS A 1 373 ? -18.79000 20.38800  -1.41200  1.000 70.90207  ? 339 LYS A CD    1 
ATOM   2490 C  CE    . LYS A 1 373 ? -17.44400 21.05300  -1.15100  1.000 68.15411  ? 339 LYS A CE    1 
ATOM   2491 N  NZ    . LYS A 1 373 ? -16.81900 20.60100  0.12700   1.000 68.13745  ? 339 LYS A NZ    1 
ATOM   2492 N  N     . GLY A 1 374 ? -23.96800 20.97100  -4.59900  1.000 54.89392  ? 340 GLY A N     1 
ATOM   2493 C  CA    . GLY A 1 374 ? -25.41200 20.94800  -4.52500  1.000 58.50620  ? 340 GLY A CA    1 
ATOM   2494 C  C     . GLY A 1 374 ? -26.01500 21.34500  -5.85700  1.000 62.87947  ? 340 GLY A C     1 
ATOM   2495 O  O     . GLY A 1 374 ? -25.38100 21.22200  -6.89800  1.000 55.25169  ? 340 GLY A O     1 
ATOM   2496 N  N     . TRP A 1 375 ? -27.24900 21.83300  -5.78800  1.000 58.57641  ? 341 TRP A N     1 
ATOM   2497 C  CA    . TRP A 1 375 ? -28.02800 22.16200  -6.97300  1.000 61.41923  ? 341 TRP A CA    1 
ATOM   2498 C  C     . TRP A 1 375 ? -27.75500 23.59400  -7.42100  1.000 59.58677  ? 341 TRP A C     1 
ATOM   2499 O  O     . TRP A 1 375 ? -27.60500 24.50100  -6.59800  1.000 60.21803  ? 341 TRP A O     1 
ATOM   2500 C  CB    . TRP A 1 375 ? -29.52100 21.97600  -6.69300  1.000 62.61309  ? 341 TRP A CB    1 
ATOM   2501 C  CG    . TRP A 1 375 ? -30.41400 22.28100  -7.86100  1.000 63.70196  ? 341 TRP A CG    1 
ATOM   2502 C  CD1   . TRP A 1 375 ? -30.84800 21.40400  -8.81600  1.000 62.61669  ? 341 TRP A CD1   1 
ATOM   2503 C  CD2   . TRP A 1 375 ? -30.98900 23.55200  -8.19200  1.000 62.52437  ? 341 TRP A CD2   1 
ATOM   2504 N  NE1   . TRP A 1 375 ? -31.65800 22.05100  -9.72000  1.000 68.79609  ? 341 TRP A NE1   1 
ATOM   2505 C  CE2   . TRP A 1 375 ? -31.75900 23.37000  -9.36100  1.000 67.16464  ? 341 TRP A CE2   1 
ATOM   2506 C  CE3   . TRP A 1 375 ? -30.92500 24.82700  -7.61600  1.000 54.87735  ? 341 TRP A CE3   1 
ATOM   2507 C  CZ2   . TRP A 1 375 ? -32.45900 24.41700  -9.96600  1.000 64.92755  ? 341 TRP A CZ2   1 
ATOM   2508 C  CZ3   . TRP A 1 375 ? -31.62200 25.86300  -8.21600  1.000 57.21465  ? 341 TRP A CZ3   1 
ATOM   2509 C  CH2   . TRP A 1 375 ? -32.37800 25.65200  -9.37900  1.000 58.05799  ? 341 TRP A CH2   1 
ATOM   2510 N  N     . VAL A 1 376 ? -27.69100 23.78700  -8.73400  1.000 61.26477  ? 342 VAL A N     1 
ATOM   2511 C  CA    . VAL A 1 376 ? -27.50000 25.11200  -9.31900  1.000 50.41907  ? 342 VAL A CA    1 
ATOM   2512 C  C     . VAL A 1 376 ? -28.55500 25.31000  -10.40100 1.000 55.69951  ? 342 VAL A C     1 
ATOM   2513 O  O     . VAL A 1 376 ? -29.02900 24.32800  -10.99100 1.000 52.63563  ? 342 VAL A O     1 
ATOM   2514 C  CB    . VAL A 1 376 ? -26.08400 25.27400  -9.89500  1.000 57.07569  ? 342 VAL A CB    1 
ATOM   2515 C  CG1   . VAL A 1 376 ? -25.03900 25.19200  -8.79100  1.000 56.49514  ? 342 VAL A CG1   1 
ATOM   2516 C  CG2   . VAL A 1 376 ? -25.82300 24.23700  -10.98700 1.000 48.60396  ? 342 VAL A CG2   1 
ATOM   2517 N  N     . PRO A 1 377 ? -28.96100 26.54200  -10.68900 1.000 54.67516  ? 343 PRO A N     1 
ATOM   2518 C  CA    . PRO A 1 377 ? -29.85900 26.76500  -11.82900 1.000 49.55686  ? 343 PRO A CA    1 
ATOM   2519 C  C     . PRO A 1 377 ? -29.11100 26.62700  -13.14700 1.000 51.01458  ? 343 PRO A C     1 
ATOM   2520 O  O     . PRO A 1 377 ? -28.61500 27.61800  -13.69200 1.000 46.94048  ? 343 PRO A O     1 
ATOM   2521 C  CB    . PRO A 1 377 ? -30.36500 28.19500  -11.60100 1.000 41.98990  ? 343 PRO A CB    1 
ATOM   2522 C  CG    . PRO A 1 377 ? -29.26300 28.85400  -10.82700 1.000 44.27243  ? 343 PRO A CG    1 
ATOM   2523 C  CD    . PRO A 1 377 ? -28.66400 27.78600  -9.95500  1.000 50.53462  ? 343 PRO A CD    1 
ATOM   2524 N  N     . GLN A 1 378 ? -29.03100 25.39400  -13.66300 1.000 43.99662  ? 344 GLN A N     1 
ATOM   2525 C  CA    . GLN A 1 378 ? -28.18200 25.11400  -14.81900 1.000 51.58422  ? 344 GLN A CA    1 
ATOM   2526 C  C     . GLN A 1 378 ? -28.63400 25.88700  -16.05300 1.000 50.46610  ? 344 GLN A C     1 
ATOM   2527 O  O     . GLN A 1 378 ? -27.80100 26.36000  -16.83500 1.000 37.57023  ? 344 GLN A O     1 
ATOM   2528 C  CB    . GLN A 1 378 ? -28.16800 23.61200  -15.10900 1.000 47.65529  ? 344 GLN A CB    1 
ATOM   2529 C  CG    . GLN A 1 378 ? -27.36900 23.23400  -16.35300 1.000 42.79611  ? 344 GLN A CG    1 
ATOM   2530 C  CD    . GLN A 1 378 ? -26.86100 21.80500  -16.32000 1.000 49.15381  ? 344 GLN A CD    1 
ATOM   2531 O  OE1   . GLN A 1 378 ? -26.03300 21.44600  -15.48200 1.000 52.29640  ? 344 GLN A OE1   1 
ATOM   2532 N  NE2   . GLN A 1 378 ? -27.35100 20.98200  -17.24200 1.000 49.60264  ? 344 GLN A NE2   1 
ATOM   2533 N  N     . ALA A 1 379 ? -29.94900 26.02100  -16.24800 1.000 42.37396  ? 345 ALA A N     1 
ATOM   2534 C  CA    . ALA A 1 379 ? -30.45600 26.70900  -17.42900 1.000 42.58326  ? 345 ALA A CA    1 
ATOM   2535 C  C     . ALA A 1 379 ? -30.04600 28.17600  -17.43300 1.000 46.49491  ? 345 ALA A C     1 
ATOM   2536 O  O     . ALA A 1 379 ? -29.67100 28.72200  -18.47800 1.000 40.67044  ? 345 ALA A O     1 
ATOM   2537 C  CB    . ALA A 1 379 ? -31.97800 26.57200  -17.49900 1.000 41.15975  ? 345 ALA A CB    1 
ATOM   2538 N  N     . LEU A 1 380 ? -30.10600 28.83000  -16.26900 1.000 39.10161  ? 346 LEU A N     1 
ATOM   2539 C  CA    . LEU A 1 380 ? -29.68500 30.22400  -16.17800 1.000 41.92361  ? 346 LEU A CA    1 
ATOM   2540 C  C     . LEU A 1 380 ? -28.17500 30.35400  -16.31400 1.000 37.31434  ? 346 LEU A C     1 
ATOM   2541 O  O     . LEU A 1 380 ? -27.67800 31.33000  -16.88700 1.000 43.09703  ? 346 LEU A O     1 
ATOM   2542 C  CB    . LEU A 1 380 ? -30.15100 30.83000  -14.85300 1.000 43.07528  ? 346 LEU A CB    1 
ATOM   2543 C  CG    . LEU A 1 380 ? -31.63400 31.17700  -14.70900 1.000 52.37289  ? 346 LEU A CG    1 
ATOM   2544 C  CD1   . LEU A 1 380 ? -31.96100 31.52700  -13.26300 1.000 45.35162  ? 346 LEU A CD1   1 
ATOM   2545 C  CD2   . LEU A 1 380 ? -32.00200 32.32500  -15.63200 1.000 49.45021  ? 346 LEU A CD2   1 
ATOM   2546 N  N     . ILE A 1 381 ? -27.42800 29.38900  -15.77900 1.000 36.68524  ? 347 ILE A N     1 
ATOM   2547 C  CA    . ILE A 1 381 ? -25.97400 29.42800  -15.89800 1.000 36.93033  ? 347 ILE A CA    1 
ATOM   2548 C  C     . ILE A 1 381 ? -25.55700 29.32500  -17.36100 1.000 35.86033  ? 347 ILE A C     1 
ATOM   2549 O  O     . ILE A 1 381 ? -24.75000 30.12600  -17.84800 1.000 32.90919  ? 347 ILE A O     1 
ATOM   2550 C  CB    . ILE A 1 381 ? -25.34100 28.31800  -15.03900 1.000 34.80098  ? 347 ILE A CB    1 
ATOM   2551 C  CG1   . ILE A 1 381 ? -25.51200 28.65400  -13.55600 1.000 33.67904  ? 347 ILE A CG1   1 
ATOM   2552 C  CG2   . ILE A 1 381 ? -23.86600 28.13300  -15.38800 1.000 30.61102  ? 347 ILE A CG2   1 
ATOM   2553 C  CD1   . ILE A 1 381 ? -25.08300 27.55200  -12.61800 1.000 43.20230  ? 347 ILE A CD1   1 
ATOM   2554 N  N     . LEU A 1 382 ? -26.12200 28.36000  -18.09400 1.000 32.25283  ? 348 LEU A N     1 
ATOM   2555 C  CA    . LEU A 1 382 ? -25.76100 28.19200  -19.50000 1.000 32.09968  ? 348 LEU A CA    1 
ATOM   2556 C  C     . LEU A 1 382 ? -26.17800 29.38200  -20.35300 1.000 28.00747  ? 348 LEU A C     1 
ATOM   2557 O  O     . LEU A 1 382 ? -25.55400 29.62600  -21.39000 1.000 34.69944  ? 348 LEU A O     1 
ATOM   2558 C  CB    . LEU A 1 382 ? -26.37300 26.90500  -20.05600 1.000 33.59064  ? 348 LEU A CB    1 
ATOM   2559 C  CG    . LEU A 1 382 ? -25.78700 25.60700  -19.49000 1.000 39.74611  ? 348 LEU A CG    1 
ATOM   2560 C  CD1   . LEU A 1 382 ? -26.56900 24.40200  -19.99400 1.000 36.09305  ? 348 LEU A CD1   1 
ATOM   2561 C  CD2   . LEU A 1 382 ? -24.31600 25.48100  -19.84600 1.000 32.37711  ? 348 LEU A CD2   1 
ATOM   2562 N  N     . ASP A 1 383 ? -27.19800 30.13700  -19.93400 1.000 32.79397  ? 349 ASP A N     1 
ATOM   2563 C  CA    . ASP A 1 383 ? -27.60900 31.34700  -20.64000 1.000 33.82023  ? 349 ASP A CA    1 
ATOM   2564 C  C     . ASP A 1 383 ? -26.81400 32.58500  -20.23400 1.000 39.54595  ? 349 ASP A C     1 
ATOM   2565 O  O     . ASP A 1 383 ? -26.97200 33.63900  -20.86100 1.000 37.86004  ? 349 ASP A O     1 
ATOM   2566 C  CB    . ASP A 1 383 ? -29.09800 31.61500  -20.40200 1.000 36.46273  ? 349 ASP A CB    1 
ATOM   2567 C  CG    . ASP A 1 383 ? -29.97700 31.05600  -21.49900 1.000 42.37122  ? 349 ASP A CG    1 
ATOM   2568 O  OD1   . ASP A 1 383 ? -29.44900 30.67900  -22.56600 1.000 48.63808  ? 349 ASP A OD1   1 
ATOM   2569 O  OD2   . ASP A 1 383 ? -31.20700 30.99300  -21.29400 1.000 53.40745  ? 349 ASP A OD2   1 
ATOM   2570 N  N     . HIS A 1 384 ? -25.97900 32.48900  -19.20500 1.000 32.47811  ? 350 HIS A N     1 
ATOM   2571 C  CA    . HIS A 1 384 ? -25.22900 33.64500  -18.74200 1.000 29.05529  ? 350 HIS A CA    1 
ATOM   2572 C  C     . HIS A 1 384 ? -24.10400 33.96700  -19.72400 1.000 25.91524  ? 350 HIS A C     1 
ATOM   2573 O  O     . HIS A 1 384 ? -23.38600 33.06300  -20.16400 1.000 25.16116  ? 350 HIS A O     1 
ATOM   2574 C  CB    . HIS A 1 384 ? -24.65200 33.37800  -17.34700 1.000 31.75126  ? 350 HIS A CB    1 
ATOM   2575 C  CG    . HIS A 1 384 ? -24.17700 34.60700  -16.63600 1.000 35.53264  ? 350 HIS A CG    1 
ATOM   2576 N  ND1   . HIS A 1 384 ? -22.96800 35.20600  -16.91900 1.000 32.22599  ? 350 HIS A ND1   1 
ATOM   2577 C  CD2   . HIS A 1 384 ? -24.73500 35.33500  -15.63900 1.000 27.99381  ? 350 HIS A CD2   1 
ATOM   2578 C  CE1   . HIS A 1 384 ? -22.80500 36.25600  -16.13200 1.000 37.18826  ? 350 HIS A CE1   1 
ATOM   2579 N  NE2   . HIS A 1 384 ? -23.86200 36.35600  -15.34600 1.000 32.64677  ? 350 HIS A NE2   1 
ATOM   2580 N  N     . PRO A 1 385 ? -23.90900 35.24100  -20.06800 1.000 28.82932  ? 351 PRO A N     1 
ATOM   2581 C  CA    . PRO A 1 385 ? -22.88000 35.58700  -21.06400 1.000 31.09784  ? 351 PRO A CA    1 
ATOM   2582 C  C     . PRO A 1 385 ? -21.45600 35.23700  -20.65100 1.000 36.35454  ? 351 PRO A C     1 
ATOM   2583 O  O     . PRO A 1 385 ? -20.58500 35.14200  -21.52600 1.000 33.02619  ? 351 PRO A O     1 
ATOM   2584 C  CB    . PRO A 1 385 ? -23.05600 37.10400  -21.24100 1.000 30.52393  ? 351 PRO A CB    1 
ATOM   2585 C  CG    . PRO A 1 385 ? -23.78800 37.56500  -20.01600 1.000 35.92875  ? 351 PRO A CG    1 
ATOM   2586 C  CD    . PRO A 1 385 ? -24.67900 36.41900  -19.62700 1.000 30.59895  ? 351 PRO A CD    1 
ATOM   2587 N  N     . SER A 1 386 ? -21.18400 35.02900  -19.36300 1.000 34.30980  ? 352 SER A N     1 
ATOM   2588 C  CA    . SER A 1 386 ? -19.82200 34.73300  -18.93200 1.000 30.25035  ? 352 SER A CA    1 
ATOM   2589 C  C     . SER A 1 386 ? -19.41400 33.28400  -19.18000 1.000 27.48967  ? 352 SER A C     1 
ATOM   2590 O  O     . SER A 1 386 ? -18.21800 32.97600  -19.13800 1.000 28.16415  ? 352 SER A O     1 
ATOM   2591 C  CB    . SER A 1 386 ? -19.65800 35.06400  -17.44500 1.000 37.48985  ? 352 SER A CB    1 
ATOM   2592 O  OG    . SER A 1 386 ? -19.80200 36.46000  -17.21600 1.000 37.67006  ? 352 SER A OG    1 
ATOM   2593 N  N     . ILE A 1 387 ? -20.36000 32.39000  -19.43900 1.000 28.61316  ? 353 ILE A N     1 
ATOM   2594 C  CA    . ILE A 1 387 ? -20.02300 30.99600  -19.70800 1.000 32.76807  ? 353 ILE A CA    1 
ATOM   2595 C  C     . ILE A 1 387 ? -19.51600 30.87400  -21.14000 1.000 32.08800  ? 353 ILE A C     1 
ATOM   2596 O  O     . ILE A 1 387 ? -20.17900 31.31300  -22.08700 1.000 31.98045  ? 353 ILE A O     1 
ATOM   2597 C  CB    . ILE A 1 387 ? -21.23600 30.08600  -19.46200 1.000 34.13515  ? 353 ILE A CB    1 
ATOM   2598 C  CG1   . ILE A 1 387 ? -21.63000 30.12100  -17.98000 1.000 30.77302  ? 353 ILE A CG1   1 
ATOM   2599 C  CG2   . ILE A 1 387 ? -20.93300 28.65900  -19.90900 1.000 29.99136  ? 353 ILE A CG2   1 
ATOM   2600 C  CD1   . ILE A 1 387 ? -20.55900 29.61000  -17.04400 1.000 31.44340  ? 353 ILE A CD1   1 
ATOM   2601 N  N     . GLY A 1 388 ? -18.32900 30.29500  -21.30000 1.000 29.41775  ? 354 GLY A N     1 
ATOM   2602 C  CA    . GLY A 1 388 ? -17.75800 30.10400  -22.61800 1.000 34.89796  ? 354 GLY A CA    1 
ATOM   2603 C  C     . GLY A 1 388 ? -17.53500 28.64800  -22.96800 1.000 37.37027  ? 354 GLY A C     1 
ATOM   2604 O  O     . GLY A 1 388 ? -17.02500 28.33800  -24.04800 1.000 32.97783  ? 354 GLY A O     1 
ATOM   2605 N  N     . GLY A 1 389 ? -17.90900 27.74300  -22.06800 1.000 29.99838  ? 355 GLY A N     1 
ATOM   2606 C  CA    . GLY A 1 389 ? -17.70400 26.32700  -22.30800 1.000 26.57224  ? 355 GLY A CA    1 
ATOM   2607 C  C     . GLY A 1 389 ? -18.47000 25.48800  -21.31200 1.000 33.66781  ? 355 GLY A C     1 
ATOM   2608 O  O     . GLY A 1 389 ? -18.81600 25.94600  -20.21700 1.000 31.31326  ? 355 GLY A O     1 
ATOM   2609 N  N     . PHE A 1 390 ? -18.71800 24.23700  -21.70500 1.000 27.28140  ? 356 PHE A N     1 
ATOM   2610 C  CA    . PHE A 1 390 ? -19.51800 23.30400  -20.91100 1.000 27.34358  ? 356 PHE A CA    1 
ATOM   2611 C  C     . PHE A 1 390 ? -18.82200 21.94600  -20.93400 1.000 32.63262  ? 356 PHE A C     1 
ATOM   2612 O  O     . PHE A 1 390 ? -18.91000 21.21100  -21.92100 1.000 29.53450  ? 356 PHE A O     1 
ATOM   2613 C  CB    . PHE A 1 390 ? -20.94500 23.21800  -21.44600 1.000 24.71424  ? 356 PHE A CB    1 
ATOM   2614 C  CG    . PHE A 1 390 ? -21.88000 22.38900  -20.59200 1.000 31.02370  ? 356 PHE A CG    1 
ATOM   2615 C  CD1   . PHE A 1 390 ? -21.54700 22.03000  -19.29400 1.000 34.26959  ? 356 PHE A CD1   1 
ATOM   2616 C  CD2   . PHE A 1 390 ? -23.10400 21.97600  -21.09700 1.000 31.42439  ? 356 PHE A CD2   1 
ATOM   2617 C  CE1   . PHE A 1 390 ? -22.41800 21.27000  -18.52000 1.000 37.27022  ? 356 PHE A CE1   1 
ATOM   2618 C  CE2   . PHE A 1 390 ? -23.97800 21.22200  -20.33000 1.000 38.42389  ? 356 PHE A CE2   1 
ATOM   2619 C  CZ    . PHE A 1 390 ? -23.63600 20.86900  -19.04000 1.000 35.58949  ? 356 PHE A CZ    1 
ATOM   2620 N  N     . LEU A 1 391 ? -18.13100 21.61900  -19.84400 1.000 32.58640  ? 357 LEU A N     1 
ATOM   2621 C  CA    . LEU A 1 391 ? -17.51300 20.31000  -19.66700 1.000 29.63224  ? 357 LEU A CA    1 
ATOM   2622 C  C     . LEU A 1 391 ? -18.54000 19.38500  -19.02000 1.000 32.38345  ? 357 LEU A C     1 
ATOM   2623 O  O     . LEU A 1 391 ? -18.96600 19.62300  -17.88300 1.000 30.34222  ? 357 LEU A O     1 
ATOM   2624 C  CB    . LEU A 1 391 ? -16.24700 20.43500  -18.82100 1.000 29.27359  ? 357 LEU A CB    1 
ATOM   2625 C  CG    . LEU A 1 391 ? -15.55100 19.16400  -18.32300 1.000 32.50676  ? 357 LEU A CG    1 
ATOM   2626 C  CD1   . LEU A 1 391 ? -15.31700 18.18800  -19.46100 1.000 32.89089  ? 357 LEU A CD1   1 
ATOM   2627 C  CD2   . LEU A 1 391 ? -14.23200 19.52500  -17.67200 1.000 36.15505  ? 357 LEU A CD2   1 
ATOM   2628 N  N     . THR A 1 392 ? -18.95400 18.34100  -19.74000 1.000 34.19085  ? 358 THR A N     1 
ATOM   2629 C  CA    . THR A 1 392 ? -19.99200 17.44700  -19.23100 1.000 33.25566  ? 358 THR A CA    1 
ATOM   2630 C  C     . THR A 1 392 ? -19.92400 16.10700  -19.96000 1.000 34.75605  ? 358 THR A C     1 
ATOM   2631 O  O     . THR A 1 392 ? -19.05800 15.87500  -20.81000 1.000 31.67148  ? 358 THR A O     1 
ATOM   2632 C  CB    . THR A 1 392 ? -21.38600 18.07500  -19.36300 1.000 42.00267  ? 358 THR A CB    1 
ATOM   2633 O  OG1   . THR A 1 392 ? -22.33000 17.35800  -18.54500 1.000 37.52141  ? 358 THR A OG1   1 
ATOM   2634 C  CG2   . THR A 1 392 ? -21.84200 18.05300  -20.81700 1.000 21.04193  ? 358 THR A CG2   1 
ATOM   2635 N  N     . HIS A 1 393 ? -20.87800 15.23300  -19.62300 1.000 32.71798  ? 359 HIS A N     1 
ATOM   2636 C  CA    . HIS A 1 393 ? -20.89600 13.82500  -19.99700 1.000 34.66248  ? 359 HIS A CA    1 
ATOM   2637 C  C     . HIS A 1 393 ? -21.56500 13.54700  -21.33900 1.000 31.45969  ? 359 HIS A C     1 
ATOM   2638 O  O     . HIS A 1 393 ? -21.62200 12.38300  -21.74500 1.000 29.82014  ? 359 HIS A O     1 
ATOM   2639 C  CB    . HIS A 1 393 ? -21.61600 13.01500  -18.91500 1.000 33.00076  ? 359 HIS A CB    1 
ATOM   2640 C  CG    . HIS A 1 393 ? -22.90600 13.63000  -18.46800 1.000 43.11259  ? 359 HIS A CG    1 
ATOM   2641 N  ND1   . HIS A 1 393 ? -23.94800 13.88700  -19.33400 1.000 39.06191  ? 359 HIS A ND1   1 
ATOM   2642 C  CD2   . HIS A 1 393 ? -23.32300 14.04300  -17.24700 1.000 48.00291  ? 359 HIS A CD2   1 
ATOM   2643 C  CE1   . HIS A 1 393 ? -24.95100 14.42800  -18.66700 1.000 42.86118  ? 359 HIS A CE1   1 
ATOM   2644 N  NE2   . HIS A 1 393 ? -24.59800 14.53300  -17.39700 1.000 49.16161  ? 359 HIS A NE2   1 
ATOM   2645 N  N     . CYS A 1 394 ? -22.09900 14.56500  -22.01500 1.000 26.56223  ? 360 CYS A N     1 
ATOM   2646 C  CA    . CYS A 1 394 ? -22.72200 14.42800  -23.33000 1.000 31.98219  ? 360 CYS A CA    1 
ATOM   2647 C  C     . CYS A 1 394 ? -24.03900 13.67500  -23.29300 1.000 34.92175  ? 360 CYS A C     1 
ATOM   2648 O  O     . CYS A 1 394 ? -24.44200 13.10000  -24.31100 1.000 31.21389  ? 360 CYS A O     1 
ATOM   2649 C  CB    . CYS A 1 394 ? -21.80900 13.72100  -24.33200 1.000 34.14156  ? 360 CYS A CB    1 
ATOM   2650 S  SG    . CYS A 1 394 ? -20.21300 14.42200  -24.46200 1.000 47.33771  ? 360 CYS A SG    1 
ATOM   2651 N  N     . GLY A 1 395 ? -24.71200 13.62300  -22.14600 1.000 26.89586  ? 361 GLY A N     1 
ATOM   2652 C  CA    . GLY A 1 395 ? -26.09100 13.17600  -22.14600 1.000 28.40481  ? 361 GLY A CA    1 
ATOM   2653 C  C     . GLY A 1 395 ? -26.91800 14.01200  -23.10300 1.000 31.11647  ? 361 GLY A C     1 
ATOM   2654 O  O     . GLY A 1 395 ? -26.58200 15.15800  -23.40900 1.000 24.59019  ? 361 GLY A O     1 
ATOM   2655 N  N     . TRP A 1 396 ? -28.00200 13.42400  -23.60400 1.000 27.05766  ? 362 TRP A N     1 
ATOM   2656 C  CA    . TRP A 1 396 ? -28.77900 14.12400  -24.62000 1.000 35.04132  ? 362 TRP A CA    1 
ATOM   2657 C  C     . TRP A 1 396 ? -29.32700 15.44100  -24.09100 1.000 32.78279  ? 362 TRP A C     1 
ATOM   2658 O  O     . TRP A 1 396 ? -29.31200 16.45900  -24.79600 1.000 26.60488  ? 362 TRP A O     1 
ATOM   2659 C  CB    . TRP A 1 396 ? -29.92300 13.25200  -25.12100 1.000 32.32792  ? 362 TRP A CB    1 
ATOM   2660 C  CG    . TRP A 1 396 ? -30.64700 13.90400  -26.25000 1.000 32.92591  ? 362 TRP A CG    1 
ATOM   2661 C  CD1   . TRP A 1 396 ? -31.94600 14.33100  -26.26400 1.000 29.88784  ? 362 TRP A CD1   1 
ATOM   2662 C  CD2   . TRP A 1 396 ? -30.10200 14.23300  -27.53200 1.000 25.53258  ? 362 TRP A CD2   1 
ATOM   2663 N  NE1   . TRP A 1 396 ? -32.24300 14.89200  -27.48400 1.000 25.90305  ? 362 TRP A NE1   1 
ATOM   2664 C  CE2   . TRP A 1 396 ? -31.12800 14.84300  -28.27800 1.000 27.85431  ? 362 TRP A CE2   1 
ATOM   2665 C  CE3   . TRP A 1 396 ? -28.84700 14.06300  -28.12300 1.000 31.54951  ? 362 TRP A CE3   1 
ATOM   2666 C  CZ2   . TRP A 1 396 ? -30.93600 15.28500  -29.58600 1.000 33.10697  ? 362 TRP A CZ2   1 
ATOM   2667 C  CZ3   . TRP A 1 396 ? -28.65900 14.50200  -29.41800 1.000 40.32910  ? 362 TRP A CZ3   1 
ATOM   2668 C  CH2   . TRP A 1 396 ? -29.69800 15.10500  -30.13600 1.000 32.27427  ? 362 TRP A CH2   1 
ATOM   2669 N  N     . ASN A 1 397 ? -29.82000 15.44400  -22.85200 1.000 27.73698  ? 363 ASN A N     1 
ATOM   2670 C  CA    . ASN A 1 397 ? -30.41100 16.66500  -22.32300 1.000 30.06162  ? 363 ASN A CA    1 
ATOM   2671 C  C     . ASN A 1 397 ? -29.35500 17.74500  -22.14900 1.000 27.80095  ? 363 ASN A C     1 
ATOM   2672 O  O     . ASN A 1 397 ? -29.59300 18.91100  -22.48600 1.000 33.35234  ? 363 ASN A O     1 
ATOM   2673 C  CB    . ASN A 1 397 ? -31.12500 16.39000  -21.00000 1.000 33.89623  ? 363 ASN A CB    1 
ATOM   2674 C  CG    . ASN A 1 397 ? -31.74000 17.64200  -20.41600 1.000 54.37630  ? 363 ASN A CG    1 
ATOM   2675 O  OD1   . ASN A 1 397 ? -32.73600 18.15500  -20.92800 1.000 52.62371  ? 363 ASN A OD1   1 
ATOM   2676 N  ND2   . ASN A 1 397 ? -31.13100 18.15900  -19.35600 1.000 54.72570  ? 363 ASN A ND2   1 
ATOM   2677 N  N     . ALA A 1 398 ? -28.17800 17.37300  -21.63900 1.000 25.33118  ? 364 ALA A N     1 
ATOM   2678 C  CA    . ALA A 1 398 ? -27.08000 18.32800  -21.54300 1.000 32.88565  ? 364 ALA A CA    1 
ATOM   2679 C  C     . ALA A 1 398 ? -26.69200 18.85000  -22.91800 1.000 29.66359  ? 364 ALA A C     1 
ATOM   2680 O  O     . ALA A 1 398 ? -26.41200 20.04300  -23.08300 1.000 31.88465  ? 364 ALA A O     1 
ATOM   2681 C  CB    . ALA A 1 398 ? -25.87700 17.68000  -20.85500 1.000 28.06561  ? 364 ALA A CB    1 
ATOM   2682 N  N     . THR A 1 399 ? -26.68600 17.96900  -23.92200 1.000 30.83618  ? 365 THR A N     1 
ATOM   2683 C  CA    . THR A 1 399 ? -26.35000 18.38300  -25.28200 1.000 26.88959  ? 365 THR A CA    1 
ATOM   2684 C  C     . THR A 1 399 ? -27.37000 19.37700  -25.82800 1.000 26.93143  ? 365 THR A C     1 
ATOM   2685 O  O     . THR A 1 399 ? -26.99800 20.39200  -26.42700 1.000 28.37365  ? 365 THR A O     1 
ATOM   2686 C  CB    . THR A 1 399 ? -26.25300 17.15200  -26.18800 1.000 36.48273  ? 365 THR A CB    1 
ATOM   2687 O  OG1   . THR A 1 399 ? -25.22200 16.28100  -25.70700 1.000 29.35976  ? 365 THR A OG1   1 
ATOM   2688 C  CG2   . THR A 1 399 ? -25.94500 17.54600  -27.62500 1.000 23.37517  ? 365 THR A CG2   1 
ATOM   2689 N  N     . VAL A 1 400 ? -28.66100 19.09800  -25.63200 1.000 27.04937  ? 366 VAL A N     1 
ATOM   2690 C  CA    . VAL A 1 400 ? -29.70900 19.99100  -26.11600 1.000 26.16179  ? 366 VAL A CA    1 
ATOM   2691 C  C     . VAL A 1 400 ? -29.64300 21.33500  -25.40100 1.000 31.63359  ? 366 VAL A C     1 
ATOM   2692 O  O     . VAL A 1 400 ? -29.78700 22.39300  -26.02700 1.000 30.25410  ? 366 VAL A O     1 
ATOM   2693 C  CB    . VAL A 1 400 ? -31.08500 19.32000  -25.94900 1.000 32.40597  ? 366 VAL A CB    1 
ATOM   2694 C  CG1   . VAL A 1 400 ? -32.20500 20.34300  -26.11100 1.000 28.71477  ? 366 VAL A CG1   1 
ATOM   2695 C  CG2   . VAL A 1 400 ? -31.24500 18.18800  -26.96200 1.000 27.00761  ? 366 VAL A CG2   1 
ATOM   2696 N  N     . GLU A 1 401 ? -29.42700 21.31900  -24.08300 1.000 23.04216  ? 367 GLU A N     1 
ATOM   2697 C  CA    . GLU A 1 401 ? -29.32200 22.56800  -23.33700 1.000 32.25052  ? 367 GLU A CA    1 
ATOM   2698 C  C     . GLU A 1 401 ? -28.12600 23.38800  -23.80000 1.000 32.18603  ? 367 GLU A C     1 
ATOM   2699 O  O     . GLU A 1 401 ? -28.22700 24.61000  -23.95900 1.000 29.83769  ? 367 GLU A O     1 
ATOM   2700 C  CB    . GLU A 1 401 ? -29.23000 22.27800  -21.83800 1.000 31.64070  ? 367 GLU A CB    1 
ATOM   2701 C  CG    . GLU A 1 401 ? -30.57700 21.97200  -21.20100 1.000 33.40280  ? 367 GLU A CG    1 
ATOM   2702 C  CD    . GLU A 1 401 ? -30.48000 21.66700  -19.71200 1.000 48.27025  ? 367 GLU A CD    1 
ATOM   2703 O  OE1   . GLU A 1 401 ? -29.37000 21.74300  -19.14500 1.000 45.51031  ? 367 GLU A OE1   1 
ATOM   2704 O  OE2   . GLU A 1 401 ? -31.52400 21.34800  -19.10900 1.000 58.24720  ? 367 GLU A OE2   1 
ATOM   2705 N  N     . ALA A 1 402 ? -26.98300 22.73500  -24.02500 1.000 25.16352  ? 368 ALA A N     1 
ATOM   2706 C  CA    . ALA A 1 402 ? -25.81500 23.44900  -24.53100 1.000 27.90672  ? 368 ALA A CA    1 
ATOM   2707 C  C     . ALA A 1 402 ? -26.09600 24.05600  -25.89900 1.000 33.84703  ? 368 ALA A C     1 
ATOM   2708 O  O     . ALA A 1 402 ? -25.75800 25.21900  -26.15400 1.000 29.26912  ? 368 ALA A O     1 
ATOM   2709 C  CB    . ALA A 1 402 ? -24.61300 22.50600  -24.59000 1.000 25.79800  ? 368 ALA A CB    1 
ATOM   2710 N  N     . ILE A 1 403 ? -26.72400 23.28700  -26.79000 1.000 30.08879  ? 369 ILE A N     1 
ATOM   2711 C  CA    . ILE A 1 403 ? -27.07600 23.81200  -28.10700 1.000 30.54985  ? 369 ILE A CA    1 
ATOM   2712 C  C     . ILE A 1 403 ? -28.04100 24.98400  -27.97200 1.000 34.85870  ? 369 ILE A C     1 
ATOM   2713 O  O     . ILE A 1 403 ? -27.83800 26.04700  -28.57300 1.000 30.29964  ? 369 ILE A O     1 
ATOM   2714 C  CB    . ILE A 1 403 ? -27.65800 22.69600  -28.99000 1.000 33.16902  ? 369 ILE A CB    1 
ATOM   2715 C  CG1   . ILE A 1 403 ? -26.56400 21.69100  -29.35600 1.000 29.34642  ? 369 ILE A CG1   1 
ATOM   2716 C  CG2   . ILE A 1 403 ? -28.29100 23.28200  -30.24800 1.000 33.25822  ? 369 ILE A CG2   1 
ATOM   2717 C  CD1   . ILE A 1 403 ? -27.08300 20.47900  -30.11900 1.000 25.50492  ? 369 ILE A CD1   1 
ATOM   2718 N  N     . SER A 1 404 ? -29.09300 24.81900  -27.16200 1.000 28.37458  ? 370 SER A N     1 
ATOM   2719 C  CA    . SER A 1 404 ? -30.09100 25.87600  -27.02000 1.000 34.27992  ? 370 SER A CA    1 
ATOM   2720 C  C     . SER A 1 404 ? -29.49700 27.16400  -26.46800 1.000 31.45925  ? 370 SER A C     1 
ATOM   2721 O  O     . SER A 1 404 ? -30.04600 28.24300  -26.72100 1.000 32.51393  ? 370 SER A O     1 
ATOM   2722 C  CB    . SER A 1 404 ? -31.23700 25.41400  -26.11300 1.000 26.94576  ? 370 SER A CB    1 
ATOM   2723 O  OG    . SER A 1 404 ? -30.84700 25.43900  -24.75500 1.000 41.04348  ? 370 SER A OG    1 
ATOM   2724 N  N     . SER A 1 405 ? -28.38900 27.07700  -25.72900 1.000 31.82300  ? 371 SER A N     1 
ATOM   2725 C  CA    . SER A 1 405 ? -27.70900 28.24200  -25.17700 1.000 32.29890  ? 371 SER A CA    1 
ATOM   2726 C  C     . SER A 1 405 ? -26.49800 28.67100  -25.99200 1.000 30.44367  ? 371 SER A C     1 
ATOM   2727 O  O     . SER A 1 405 ? -25.86100 29.67100  -25.64400 1.000 30.20807  ? 371 SER A O     1 
ATOM   2728 C  CB    . SER A 1 405 ? -27.27200 27.96800  -23.73300 1.000 30.06267  ? 371 SER A CB    1 
ATOM   2729 O  OG    . SER A 1 405 ? -28.39300 27.84200  -22.88100 1.000 49.54013  ? 371 SER A OG    1 
ATOM   2730 N  N     . GLY A 1 406 ? -26.15800 27.94100  -27.05100 1.000 31.19245  ? 372 GLY A N     1 
ATOM   2731 C  CA    . GLY A 1 406 ? -25.02600 28.31300  -27.88300 1.000 26.06267  ? 372 GLY A CA    1 
ATOM   2732 C  C     . GLY A 1 406 ? -23.68000 28.16000  -27.21000 1.000 32.64701  ? 372 GLY A C     1 
ATOM   2733 O  O     . GLY A 1 406 ? -22.74300 28.88700  -27.54900 1.000 30.59453  ? 372 GLY A O     1 
ATOM   2734 N  N     . VAL A 1 407 ? -23.55500 27.23400  -26.26800 1.000 27.65404  ? 373 VAL A N     1 
ATOM   2735 C  CA    . VAL A 1 407 ? -22.34400 27.08000  -25.46400 1.000 26.36703  ? 373 VAL A CA    1 
ATOM   2736 C  C     . VAL A 1 407 ? -21.55200 25.88900  -26.01000 1.000 28.76688  ? 373 VAL A C     1 
ATOM   2737 O  O     . VAL A 1 407 ? -22.10400 24.78300  -26.08800 1.000 25.25871  ? 373 VAL A O     1 
ATOM   2738 C  CB    . VAL A 1 407 ? -22.67600 26.87700  -23.97900 1.000 31.11991  ? 373 VAL A CB    1 
ATOM   2739 C  CG1   . VAL A 1 407 ? -21.40300 26.59500  -23.19000 1.000 23.24028  ? 373 VAL A CG1   1 
ATOM   2740 C  CG2   . VAL A 1 407 ? -23.39600 28.10600  -23.43100 1.000 26.04684  ? 373 VAL A CG2   1 
ATOM   2741 N  N     . PRO A 1 408 ? -20.28800 26.07200  -26.38600 1.000 27.73113  ? 374 PRO A N     1 
ATOM   2742 C  CA    . PRO A 1 408 ? -19.48800 24.92500  -26.84100 1.000 23.57378  ? 374 PRO A CA    1 
ATOM   2743 C  C     . PRO A 1 408 ? -19.20300 23.95800  -25.70900 1.000 32.85319  ? 374 PRO A C     1 
ATOM   2744 O  O     . PRO A 1 408 ? -19.03200 24.34600  -24.55000 1.000 30.84293  ? 374 PRO A O     1 
ATOM   2745 C  CB    . PRO A 1 408 ? -18.19600 25.57200  -27.35400 1.000 27.71997  ? 374 PRO A CB    1 
ATOM   2746 C  CG    . PRO A 1 408 ? -18.13600 26.90200  -26.67300 1.000 31.70016  ? 374 PRO A CG    1 
ATOM   2747 C  CD    . PRO A 1 408 ? -19.55500 27.34400  -26.49300 1.000 24.31641  ? 374 PRO A CD    1 
ATOM   2748 N  N     . MET A 1 409 ? -19.14200 22.67800  -26.05300 1.000 26.65032  ? 375 MET A N     1 
ATOM   2749 C  CA    . MET A 1 409 ? -18.93400 21.66200  -25.03500 1.000 29.72863  ? 375 MET A CA    1 
ATOM   2750 C  C     . MET A 1 409 ? -17.49500 21.17100  -25.00600 1.000 25.68349  ? 375 MET A C     1 
ATOM   2751 O  O     . MET A 1 409 ? -16.77300 21.23100  -25.99900 1.000 28.70842  ? 375 MET A O     1 
ATOM   2752 C  CB    . MET A 1 409 ? -19.87300 20.47300  -25.23000 1.000 30.87299  ? 375 MET A CB    1 
ATOM   2753 C  CG    . MET A 1 409 ? -21.33000 20.79100  -24.96100 1.000 30.01661  ? 375 MET A CG    1 
ATOM   2754 S  SD    . MET A 1 409 ? -22.41700 19.70000  -25.88900 1.000 36.78237  ? 375 MET A SD    1 
ATOM   2755 C  CE    . MET A 1 409 ? -22.75500 18.47700  -24.60100 1.000 40.90307  ? 375 MET A CE    1 
ATOM   2756 N  N     . VAL A 1 410 ? -17.07800 20.72100  -23.82900 1.000 27.35456  ? 376 VAL A N     1 
ATOM   2757 C  CA    . VAL A 1 410 ? -15.89100 19.89700  -23.66300 1.000 24.60975  ? 376 VAL A CA    1 
ATOM   2758 C  C     . VAL A 1 410 ? -16.40800 18.53000  -23.24200 1.000 30.98805  ? 376 VAL A C     1 
ATOM   2759 O  O     . VAL A 1 410 ? -17.00800 18.38400  -22.16900 1.000 33.22221  ? 376 VAL A O     1 
ATOM   2760 C  CB    . VAL A 1 410 ? -14.92000 20.48900  -22.63400 1.000 29.71142  ? 376 VAL A CB    1 
ATOM   2761 C  CG1   . VAL A 1 410 ? -13.62000 19.72600  -22.64500 1.000 28.21401  ? 376 VAL A CG1   1 
ATOM   2762 C  CG2   . VAL A 1 410 ? -14.67000 21.96000  -22.93200 1.000 31.47608  ? 376 VAL A CG2   1 
ATOM   2763 N  N     . THR A 1 411 ? -16.21700 17.53300  -24.09700 1.000 28.39612  ? 377 THR A N     1 
ATOM   2764 C  CA    . THR A 1 411 ? -16.95300 16.28200  -23.98400 1.000 28.80501  ? 377 THR A CA    1 
ATOM   2765 C  C     . THR A 1 411 ? -16.15600 15.24700  -23.20500 1.000 27.32311  ? 377 THR A C     1 
ATOM   2766 O  O     . THR A 1 411 ? -14.98500 14.99000  -23.50500 1.000 29.06169  ? 377 THR A O     1 
ATOM   2767 C  CB    . THR A 1 411 ? -17.31000 15.74700  -25.36900 1.000 30.23980  ? 377 THR A CB    1 
ATOM   2768 O  OG1   . THR A 1 411 ? -16.11600 15.52300  -26.12400 1.000 31.23550  ? 377 THR A OG1   1 
ATOM   2769 C  CG2   . THR A 1 411 ? -18.20500 16.74000  -26.09700 1.000 34.44123  ? 377 THR A CG2   1 
ATOM   2770 N  N     . MET A 1 412 ? -16.80000 14.65400  -22.20900 1.000 28.49987  ? 378 MET A N     1 
ATOM   2771 C  CA    . MET A 1 412 ? -16.20900 13.58100  -21.41300 1.000 31.29293  ? 378 MET A CA    1 
ATOM   2772 C  C     . MET A 1 412 ? -17.30500 12.56100  -21.15900 1.000 34.08889  ? 378 MET A C     1 
ATOM   2773 O  O     . MET A 1 412 ? -17.92900 12.54300  -20.09100 1.000 31.79481  ? 378 MET A O     1 
ATOM   2774 C  CB    . MET A 1 412 ? -15.62100 14.12400  -20.10900 1.000 30.72562  ? 378 MET A CB    1 
ATOM   2775 C  CG    . MET A 1 412 ? -14.67200 13.17200  -19.41700 1.000 39.60742  ? 378 MET A CG    1 
ATOM   2776 S  SD    . MET A 1 412 ? -13.85700 13.94800  -18.00900 1.000 46.37934  ? 378 MET A SD    1 
ATOM   2777 C  CE    . MET A 1 412 ? -12.92400 15.20400  -18.85300 1.000 40.06135  ? 378 MET A CE    1 
ATOM   2778 N  N     . PRO A 1 413 ? -17.57800 11.69700  -22.13600 1.000 31.35201  ? 379 PRO A N     1 
ATOM   2779 C  CA    . PRO A 1 413 ? -18.71700 10.78200  -22.01800 1.000 29.83343  ? 379 PRO A CA    1 
ATOM   2780 C  C     . PRO A 1 413 ? -18.50400 9.74500   -20.92700 1.000 32.88824  ? 379 PRO A C     1 
ATOM   2781 O  O     . PRO A 1 413 ? -17.38500 9.29200   -20.67500 1.000 30.42987  ? 379 PRO A O     1 
ATOM   2782 C  CB    . PRO A 1 413 ? -18.78700 10.12800  -23.40400 1.000 25.83218  ? 379 PRO A CB    1 
ATOM   2783 C  CG    . PRO A 1 413 ? -17.38900 10.21500  -23.92000 1.000 30.87617  ? 379 PRO A CG    1 
ATOM   2784 C  CD    . PRO A 1 413 ? -16.86300 11.52700  -23.41100 1.000 31.09224  ? 379 PRO A CD    1 
ATOM   2785 N  N     . GLY A 1 414 ? -19.60800 9.36100   -20.29200 1.000 31.81081  ? 380 GLY A N     1 
ATOM   2786 C  CA    . GLY A 1 414 ? -19.55000 8.50700   -19.12300 1.000 37.61055  ? 380 GLY A CA    1 
ATOM   2787 C  C     . GLY A 1 414 ? -20.03100 7.09300   -19.36900 1.000 37.87788  ? 380 GLY A C     1 
ATOM   2788 O  O     . GLY A 1 414 ? -19.42000 6.13800   -18.88000 1.000 38.31867  ? 380 GLY A O     1 
ATOM   2789 N  N     . PHE A 1 415 ? -21.11800 6.93800   -20.12400 1.000 29.18561  ? 381 PHE A N     1 
ATOM   2790 C  CA    . PHE A 1 415 ? -21.67100 5.61300   -20.37100 1.000 34.34355  ? 381 PHE A CA    1 
ATOM   2791 C  C     . PHE A 1 415 ? -22.63900 5.66500   -21.54500 1.000 32.18667  ? 381 PHE A C     1 
ATOM   2792 O  O     . PHE A 1 415 ? -23.13200 6.73000   -21.92300 1.000 34.94238  ? 381 PHE A O     1 
ATOM   2793 C  CB    . PHE A 1 415 ? -22.37800 5.06200   -19.12100 1.000 35.24567  ? 381 PHE A CB    1 
ATOM   2794 C  CG    . PHE A 1 415 ? -23.76700 5.60500   -18.92000 1.000 37.50951  ? 381 PHE A CG    1 
ATOM   2795 C  CD1   . PHE A 1 415 ? -23.96200 6.82000   -18.29000 1.000 40.33403  ? 381 PHE A CD1   1 
ATOM   2796 C  CD2   . PHE A 1 415 ? -24.87800 4.89900   -19.36000 1.000 43.85552  ? 381 PHE A CD2   1 
ATOM   2797 C  CE1   . PHE A 1 415 ? -25.23600 7.32800   -18.11600 1.000 38.38608  ? 381 PHE A CE1   1 
ATOM   2798 C  CE2   . PHE A 1 415 ? -26.15200 5.40400   -19.18900 1.000 48.56237  ? 381 PHE A CE2   1 
ATOM   2799 C  CZ    . PHE A 1 415 ? -26.33000 6.61900   -18.56600 1.000 37.13741  ? 381 PHE A CZ    1 
ATOM   2800 N  N     . GLY A 1 416 ? -22.90300 4.48900   -22.11000 1.000 33.89222  ? 382 GLY A N     1 
ATOM   2801 C  CA    . GLY A 1 416 ? -24.07200 4.29900   -22.96000 1.000 33.47247  ? 382 GLY A CA    1 
ATOM   2802 C  C     . GLY A 1 416 ? -24.04900 5.13600   -24.22400 1.000 28.97447  ? 382 GLY A C     1 
ATOM   2803 O  O     . GLY A 1 416 ? -23.05500 5.18300   -24.95700 1.000 28.28403  ? 382 GLY A O     1 
ATOM   2804 N  N     . ASP A 1 417 ? -25.17200 5.80400   -24.48900 1.000 30.96455  ? 383 ASP A N     1 
ATOM   2805 C  CA    . ASP A 1 417 ? -25.30800 6.62400   -25.68600 1.000 30.04798  ? 383 ASP A CA    1 
ATOM   2806 C  C     . ASP A 1 417 ? -24.39100 7.83700   -25.68700 1.000 34.75821  ? 383 ASP A C     1 
ATOM   2807 O  O     . ASP A 1 417 ? -24.28500 8.50300   -26.72200 1.000 27.43304  ? 383 ASP A O     1 
ATOM   2808 C  CB    . ASP A 1 417 ? -26.75700 7.09100   -25.84800 1.000 32.58256  ? 383 ASP A CB    1 
ATOM   2809 C  CG    . ASP A 1 417 ? -27.70600 5.95500   -26.19400 1.000 55.52770  ? 383 ASP A CG    1 
ATOM   2810 O  OD1   . ASP A 1 417 ? -27.27600 4.99200   -26.86700 1.000 46.90012  ? 383 ASP A OD1   1 
ATOM   2811 O  OD2   . ASP A 1 417 ? -28.88700 6.02700   -25.79000 1.000 54.52484  ? 383 ASP A OD2   1 
ATOM   2812 N  N     . GLN A 1 418 ? -23.72500 8.14200   -24.57200 1.000 29.90962  ? 384 GLN A N     1 
ATOM   2813 C  CA    . GLN A 1 418 ? -22.95400 9.37800   -24.51100 1.000 33.72868  ? 384 GLN A CA    1 
ATOM   2814 C  C     . GLN A 1 418 ? -21.73400 9.34100   -25.42400 1.000 31.03956  ? 384 GLN A C     1 
ATOM   2815 O  O     . GLN A 1 418 ? -21.26800 10.39500  -25.86700 1.000 27.13325  ? 384 GLN A O     1 
ATOM   2816 C  CB    . GLN A 1 418 ? -22.55100 9.66500   -23.06600 1.000 25.18608  ? 384 GLN A CB    1 
ATOM   2817 C  CG    . GLN A 1 418 ? -23.75700 9.93300   -22.15600 1.000 29.64325  ? 384 GLN A CG    1 
ATOM   2818 C  CD    . GLN A 1 418 ? -23.40800 9.92900   -20.68200 1.000 28.02017  ? 384 GLN A CD    1 
ATOM   2819 O  OE1   . GLN A 1 418 ? -22.27800 9.63200   -20.30100 1.000 30.51258  ? 384 GLN A OE1   1 
ATOM   2820 N  NE2   . GLN A 1 418 ? -24.38100 10.26000  -19.84300 1.000 31.96388  ? 384 GLN A NE2   1 
ATOM   2821 N  N     . TYR A 1 419 ? -21.20700 8.15100   -25.71900 1.000 25.90872  ? 385 TYR A N     1 
ATOM   2822 C  CA    . TYR A 1 419 ? -20.07400 8.06500   -26.63300 1.000 25.83899  ? 385 TYR A CA    1 
ATOM   2823 C  C     . TYR A 1 419 ? -20.47900 8.41700   -28.05600 1.000 30.97946  ? 385 TYR A C     1 
ATOM   2824 O  O     . TYR A 1 419 ? -19.64600 8.89400   -28.83400 1.000 25.27716  ? 385 TYR A O     1 
ATOM   2825 C  CB    . TYR A 1 419 ? -19.45300 6.66500   -26.59000 1.000 28.30326  ? 385 TYR A CB    1 
ATOM   2826 C  CG    . TYR A 1 419 ? -19.03800 6.23500   -25.20200 1.000 32.11766  ? 385 TYR A CG    1 
ATOM   2827 C  CD1   . TYR A 1 419 ? -17.90300 6.76700   -24.60000 1.000 26.14356  ? 385 TYR A CD1   1 
ATOM   2828 C  CD2   . TYR A 1 419 ? -19.77800 5.29600   -24.49400 1.000 34.96570  ? 385 TYR A CD2   1 
ATOM   2829 C  CE1   . TYR A 1 419 ? -17.52000 6.38300   -23.32900 1.000 32.72052  ? 385 TYR A CE1   1 
ATOM   2830 C  CE2   . TYR A 1 419 ? -19.40300 4.90200   -23.22200 1.000 29.55167  ? 385 TYR A CE2   1 
ATOM   2831 C  CZ    . TYR A 1 419 ? -18.27700 5.44900   -22.64500 1.000 32.57798  ? 385 TYR A CZ    1 
ATOM   2832 O  OH    . TYR A 1 419 ? -17.90500 5.06000   -21.37900 1.000 37.22266  ? 385 TYR A OH    1 
ATOM   2833 N  N     . TYR A 1 420 ? -21.74000 8.18100   -28.42200 1.000 28.08563  ? 386 TYR A N     1 
ATOM   2834 C  CA    . TYR A 1 420 ? -22.19400 8.58100   -29.75100 1.000 26.22710  ? 386 TYR A CA    1 
ATOM   2835 C  C     . TYR A 1 420 ? -22.54700 10.06400  -29.78600 1.000 27.93167  ? 386 TYR A C     1 
ATOM   2836 O  O     . TYR A 1 420 ? -22.20600 10.76100  -30.74700 1.000 27.77010  ? 386 TYR A O     1 
ATOM   2837 C  CB    . TYR A 1 420 ? -23.38400 7.71900   -30.17800 1.000 29.10028  ? 386 TYR A CB    1 
ATOM   2838 C  CG    . TYR A 1 420 ? -23.19000 6.24200   -29.88400 1.000 33.19265  ? 386 TYR A CG    1 
ATOM   2839 C  CD1   . TYR A 1 420 ? -22.17000 5.52400   -30.49000 1.000 30.78682  ? 386 TYR A CD1   1 
ATOM   2840 C  CD2   . TYR A 1 420 ? -24.01900 5.57200   -28.98900 1.000 36.89608  ? 386 TYR A CD2   1 
ATOM   2841 C  CE1   . TYR A 1 420 ? -21.97800 4.17700   -30.22500 1.000 31.97721  ? 386 TYR A CE1   1 
ATOM   2842 C  CE2   . TYR A 1 420 ? -23.83700 4.21900   -28.71900 1.000 30.11123  ? 386 TYR A CE2   1 
ATOM   2843 C  CZ    . TYR A 1 420 ? -22.81000 3.53100   -29.34000 1.000 30.76023  ? 386 TYR A CZ    1 
ATOM   2844 O  OH    . TYR A 1 420 ? -22.61600 2.19200   -29.08600 1.000 36.67313  ? 386 TYR A OH    1 
ATOM   2845 N  N     . ASN A 1 421 ? -23.21500 10.56400  -28.74100 1.000 27.87490  ? 387 ASN A N     1 
ATOM   2846 C  CA    . ASN A 1 421 ? -23.50700 11.99300  -28.65400 1.000 30.56303  ? 387 ASN A CA    1 
ATOM   2847 C  C     . ASN A 1 421 ? -22.23500 12.82400  -28.75200 1.000 27.26167  ? 387 ASN A C     1 
ATOM   2848 O  O     . ASN A 1 421 ? -22.23700 13.91100  -29.34400 1.000 27.36499  ? 387 ASN A O     1 
ATOM   2849 C  CB    . ASN A 1 421 ? -24.23100 12.31100  -27.34500 1.000 24.15511  ? 387 ASN A CB    1 
ATOM   2850 C  CG    . ASN A 1 421 ? -25.55600 11.59800  -27.22100 1.000 30.65067  ? 387 ASN A CG    1 
ATOM   2851 O  OD1   . ASN A 1 421 ? -26.12200 11.13900  -28.21300 1.000 31.27333  ? 387 ASN A OD1   1 
ATOM   2852 N  ND2   . ASN A 1 421 ? -26.07000 11.51300  -25.99400 1.000 29.91126  ? 387 ASN A ND2   1 
ATOM   2853 N  N     . GLU A 1 422 ? -21.14000 12.33300  -28.17000 1.000 24.76592  ? 388 GLU A N     1 
ATOM   2854 C  CA    . GLU A 1 422 ? -19.87400 13.05300  -28.25600 1.000 27.44507  ? 388 GLU A CA    1 
ATOM   2855 C  C     . GLU A 1 422 ? -19.46000 13.26900  -29.70800 1.000 25.65293  ? 388 GLU A C     1 
ATOM   2856 O  O     . GLU A 1 422 ? -19.08600 14.38100  -30.10100 1.000 30.75180  ? 388 GLU A O     1 
ATOM   2857 C  CB    . GLU A 1 422 ? -18.78500 12.29600  -27.49600 1.000 23.73372  ? 388 GLU A CB    1 
ATOM   2858 C  CG    . GLU A 1 422 ? -17.39500 12.88000  -27.71700 1.000 31.57528  ? 388 GLU A CG    1 
ATOM   2859 C  CD    . GLU A 1 422 ? -16.32700 12.17500  -26.91800 1.000 36.02742  ? 388 GLU A CD    1 
ATOM   2860 O  OE1   . GLU A 1 422 ? -16.23300 10.92600  -26.99500 1.000 30.83569  ? 388 GLU A OE1   1 
ATOM   2861 O  OE2   . GLU A 1 422 ? -15.58900 12.88000  -26.20100 1.000 33.88575  ? 388 GLU A OE2   1 
ATOM   2862 N  N     . LYS A 1 423 ? -19.53100 12.21400  -30.52500 1.000 23.81786  ? 389 LYS A N     1 
ATOM   2863 C  CA    . LYS A 1 423 ? -19.06600 12.30800  -31.90700 1.000 27.77019  ? 389 LYS A CA    1 
ATOM   2864 C  C     . LYS A 1 423 ? -19.94000 13.24200  -32.72800 1.000 26.58774  ? 389 LYS A C     1 
ATOM   2865 O  O     . LYS A 1 423 ? -19.43500 13.97800  -33.58400 1.000 28.85080  ? 389 LYS A O     1 
ATOM   2866 C  CB    . LYS A 1 423 ? -19.02400 10.91700  -32.53700 1.000 32.93289  ? 389 LYS A CB    1 
ATOM   2867 C  CG    . LYS A 1 423 ? -17.95800 10.03100  -31.93100 1.000 32.31259  ? 389 LYS A CG    1 
ATOM   2868 C  CD    . LYS A 1 423 ? -16.59100 10.68300  -32.05600 1.000 33.55951  ? 389 LYS A CD    1 
ATOM   2869 C  CE    . LYS A 1 423 ? -15.63600 10.15500  -30.99600 1.000 44.16689  ? 389 LYS A CE    1 
ATOM   2870 N  NZ    . LYS A 1 423 ? -14.25400 10.64700  -31.23700 1.000 46.64895  ? 389 LYS A NZ    1 
ATOM   2871 N  N     . LEU A 1 424 ? -21.25400 13.21100  -32.49800 1.000 23.32893  ? 390 LEU A N     1 
ATOM   2872 C  CA    . LEU A 1 424 ? -22.13500 14.17700  -33.14200 1.000 28.72110  ? 390 LEU A CA    1 
ATOM   2873 C  C     . LEU A 1 424 ? -21.67400 15.60000  -32.86300 1.000 28.51941  ? 390 LEU A C     1 
ATOM   2874 O  O     . LEU A 1 424 ? -21.67000 16.44700  -33.76200 1.000 26.22886  ? 390 LEU A O     1 
ATOM   2875 C  CB    . LEU A 1 424 ? -23.57500 13.97100  -32.66100 1.000 28.83744  ? 390 LEU A CB    1 
ATOM   2876 C  CG    . LEU A 1 424 ? -24.67000 14.83900  -33.28200 1.000 31.54867  ? 390 LEU A CG    1 
ATOM   2877 C  CD1   . LEU A 1 424 ? -24.73500 14.62700  -34.79200 1.000 28.09644  ? 390 LEU A CD1   1 
ATOM   2878 C  CD2   . LEU A 1 424 ? -26.01500 14.52700  -32.64200 1.000 22.57387  ? 390 LEU A CD2   1 
ATOM   2879 N  N     . VAL A 1 425 ? -21.24900 15.86300  -31.62500 1.000 23.12503  ? 391 VAL A N     1 
ATOM   2880 C  CA    . VAL A 1 425 ? -20.86300 17.20300  -31.19600 1.000 23.09997  ? 391 VAL A CA    1 
ATOM   2881 C  C     . VAL A 1 425 ? -19.48400 17.58800  -31.73300 1.000 25.78198  ? 391 VAL A C     1 
ATOM   2882 O  O     . VAL A 1 425 ? -19.29400 18.69900  -32.23700 1.000 27.22837  ? 391 VAL A O     1 
ATOM   2883 C  CB    . VAL A 1 425 ? -20.90900 17.27900  -29.65600 1.000 30.07976  ? 391 VAL A CB    1 
ATOM   2884 C  CG1   . VAL A 1 425 ? -20.14500 18.48900  -29.15300 1.000 30.19097  ? 391 VAL A CG1   1 
ATOM   2885 C  CG2   . VAL A 1 425 ? -22.34800 17.29900  -29.16800 1.000 23.63504  ? 391 VAL A CG2   1 
ATOM   2886 N  N     . THR A 1 426 ? -18.50100 16.69000  -31.63400 1.000 24.50692  ? 392 THR A N     1 
ATOM   2887 C  CA    . THR A 1 426 ? -17.10600 17.06700  -31.84400 1.000 26.02665  ? 392 THR A CA    1 
ATOM   2888 C  C     . THR A 1 426 ? -16.58200 16.76800  -33.24000 1.000 30.56117  ? 392 THR A C     1 
ATOM   2889 O  O     . THR A 1 426 ? -15.70000 17.49000  -33.71800 1.000 30.38410  ? 392 THR A O     1 
ATOM   2890 C  CB    . THR A 1 426 ? -16.19500 16.35400  -30.84300 1.000 26.75162  ? 392 THR A CB    1 
ATOM   2891 O  OG1   . THR A 1 426 ? -16.23900 14.94000  -31.08400 1.000 22.88134  ? 392 THR A OG1   1 
ATOM   2892 C  CG2   . THR A 1 426 ? -16.62100 16.66600  -29.41400 1.000 24.85956  ? 392 THR A CG2   1 
ATOM   2893 N  N     . GLU A 1 427 ? -17.06500 15.71000  -33.89000 1.000 29.45628  ? 393 GLU A N     1 
ATOM   2894 C  CA    . GLU A 1 427 ? -16.57200 15.34300  -35.21300 1.000 35.43128  ? 393 GLU A CA    1 
ATOM   2895 C  C     . GLU A 1 427 ? -17.56500 15.64700  -36.32100 1.000 34.86877  ? 393 GLU A C     1 
ATOM   2896 O  O     . GLU A 1 427 ? -17.14600 15.96100  -37.43800 1.000 39.33294  ? 393 GLU A O     1 
ATOM   2897 C  CB    . GLU A 1 427 ? -16.19000 13.85500  -35.25200 1.000 33.89075  ? 393 GLU A CB    1 
ATOM   2898 C  CG    . GLU A 1 427 ? -14.81500 13.56000  -34.64300 1.000 34.93121  ? 393 GLU A CG    1 
ATOM   2899 C  CD    . GLU A 1 427 ? -14.36700 12.10800  -34.80600 1.000 46.42515  ? 393 GLU A CD    1 
ATOM   2900 O  OE1   . GLU A 1 427 ? -15.22400 11.21200  -34.92100 1.000 48.79684  ? 393 GLU A OE1   1 
ATOM   2901 O  OE2   . GLU A 1 427 ? -13.14500 11.85600  -34.80600 1.000 52.58742  ? 393 GLU A OE2   1 
ATOM   2902 N  N     . VAL A 1 428 ? -18.86600 15.59000  -36.04200 1.000 32.53193  ? 394 VAL A N     1 
ATOM   2903 C  CA    . VAL A 1 428 ? -19.83800 15.93600  -37.07200 1.000 35.37372  ? 394 VAL A CA    1 
ATOM   2904 C  C     . VAL A 1 428 ? -20.01700 17.44600  -37.16000 1.000 36.88411  ? 394 VAL A C     1 
ATOM   2905 O  O     . VAL A 1 428 ? -19.85700 18.04100  -38.23200 1.000 32.67228  ? 394 VAL A O     1 
ATOM   2906 C  CB    . VAL A 1 428 ? -21.17800 15.22500  -36.81800 1.000 31.80497  ? 394 VAL A CB    1 
ATOM   2907 C  CG1   . VAL A 1 428 ? -22.20200 15.64100  -37.88200 1.000 30.44218  ? 394 VAL A CG1   1 
ATOM   2908 C  CG2   . VAL A 1 428 ? -20.98100 13.72200  -36.82600 1.000 29.45628  ? 394 VAL A CG2   1 
ATOM   2909 N  N     . HIS A 1 429 ? -20.34000 18.09200  -36.03800 1.000 24.51146  ? 395 HIS A N     1 
ATOM   2910 C  CA    . HIS A 1 429 ? -20.71600 19.49500  -36.05500 1.000 30.30651  ? 395 HIS A CA    1 
ATOM   2911 C  C     . HIS A 1 429 ? -19.65400 20.43800  -35.51400 1.000 28.57633  ? 395 HIS A C     1 
ATOM   2912 O  O     . HIS A 1 429 ? -19.77800 21.65200  -35.71900 1.000 29.77797  ? 395 HIS A O     1 
ATOM   2913 C  CB    . HIS A 1 429 ? -22.02300 19.69800  -35.27700 1.000 24.20784  ? 395 HIS A CB    1 
ATOM   2914 C  CG    . HIS A 1 429 ? -23.20800 19.07800  -35.94500 1.000 31.28136  ? 395 HIS A CG    1 
ATOM   2915 N  ND1   . HIS A 1 429 ? -23.69300 19.52300  -37.15700 1.000 29.39702  ? 395 HIS A ND1   1 
ATOM   2916 C  CD2   . HIS A 1 429 ? -23.99400 18.03700  -35.58300 1.000 24.10878  ? 395 HIS A CD2   1 
ATOM   2917 C  CE1   . HIS A 1 429 ? -24.73600 18.79200  -37.50600 1.000 25.04760  ? 395 HIS A CE1   1 
ATOM   2918 N  NE2   . HIS A 1 429 ? -24.93800 17.88200  -36.56900 1.000 28.48065  ? 395 HIS A NE2   1 
ATOM   2919 N  N     . ARG A 1 430 ? -18.62300 19.92500  -34.84200 1.000 25.07069  ? 396 ARG A N     1 
ATOM   2920 C  CA    . ARG A 1 430 ? -17.53900 20.76000  -34.32200 1.000 27.80771  ? 396 ARG A CA    1 
ATOM   2921 C  C     . ARG A 1 430 ? -18.08900 21.88700  -33.44800 1.000 24.24798  ? 396 ARG A C     1 
ATOM   2922 O  O     . ARG A 1 430 ? -17.66100 23.04200  -33.52900 1.000 24.77429  ? 396 ARG A O     1 
ATOM   2923 C  CB    . ARG A 1 430 ? -16.67200 21.30700  -35.46600 1.000 22.03460  ? 396 ARG A CB    1 
ATOM   2924 C  CG    . ARG A 1 430 ? -15.88300 20.22000  -36.19400 1.000 29.00918  ? 396 ARG A CG    1 
ATOM   2925 C  CD    . ARG A 1 430 ? -15.00400 20.78000  -37.31300 1.000 33.25055  ? 396 ARG A CD    1 
ATOM   2926 N  NE    . ARG A 1 430 ? -14.04400 21.76900  -36.83500 1.000 38.68205  ? 396 ARG A NE    1 
ATOM   2927 C  CZ    . ARG A 1 430 ? -12.89300 21.47200  -36.24700 1.000 35.82099  ? 396 ARG A CZ    1 
ATOM   2928 N  NH1   . ARG A 1 430 ? -12.53700 20.21900  -36.01900 1.000 33.15414  ? 396 ARG A NH1   1 
ATOM   2929 N  NH2   . ARG A 1 430 ? -12.07800 22.45700  -35.88300 1.000 33.60525  ? 396 ARG A NH2   1 
ATOM   2930 N  N     . ILE A 1 431 ? -19.08100 21.55400  -32.63100 1.000 25.73416  ? 397 ILE A N     1 
ATOM   2931 C  CA    . ILE A 1 431 ? -19.60300 22.47500  -31.63800 1.000 25.71290  ? 397 ILE A CA    1 
ATOM   2932 C  C     . ILE A 1 431 ? -19.09300 22.11700  -30.24600 1.000 26.31059  ? 397 ILE A C     1 
ATOM   2933 O  O     . ILE A 1 431 ? -19.68600 22.51200  -29.23900 1.000 27.18195  ? 397 ILE A O     1 
ATOM   2934 C  CB    . ILE A 1 431 ? -21.13500 22.53700  -31.68200 1.000 26.66340  ? 397 ILE A CB    1 
ATOM   2935 C  CG1   . ILE A 1 431 ? -21.72800 21.14300  -31.44800 1.000 26.00464  ? 397 ILE A CG1   1 
ATOM   2936 C  CG2   . ILE A 1 431 ? -21.59400 23.13100  -33.03300 1.000 23.45184  ? 397 ILE A CG2   1 
ATOM   2937 C  CD1   . ILE A 1 431 ? -23.24400 21.11700  -31.45600 1.000 24.17511  ? 397 ILE A CD1   1 
ATOM   2938 N  N     . GLY A 1 432 ? -18.00800 21.35500  -30.18200 1.000 29.58726  ? 398 GLY A N     1 
ATOM   2939 C  CA    . GLY A 1 432 ? -17.39700 20.98600  -28.92100 1.000 27.59016  ? 398 GLY A CA    1 
ATOM   2940 C  C     . GLY A 1 432 ? -16.03500 20.38400  -29.18000 1.000 32.88752  ? 398 GLY A C     1 
ATOM   2941 O  O     . GLY A 1 432 ? -15.64500 20.13700  -30.32400 1.000 27.21154  ? 398 GLY A O     1 
ATOM   2942 N  N     . VAL A 1 433 ? -15.31700 20.14900  -28.08700 1.000 32.78687  ? 399 VAL A N     1 
ATOM   2943 C  CA    . VAL A 1 433 ? -13.95500 19.62900  -28.10400 1.000 35.26693  ? 399 VAL A CA    1 
ATOM   2944 C  C     . VAL A 1 433 ? -13.94100 18.31800  -27.33500 1.000 34.47729  ? 399 VAL A C     1 
ATOM   2945 O  O     . VAL A 1 433 ? -14.55400 18.21400  -26.26800 1.000 34.55155  ? 399 VAL A O     1 
ATOM   2946 C  CB    . VAL A 1 433 ? -12.96900 20.64200  -27.48600 1.000 37.83212  ? 399 VAL A CB    1 
ATOM   2947 C  CG1   . VAL A 1 433 ? -11.61600 20.00400  -27.25100 1.000 47.05409  ? 399 VAL A CG1   1 
ATOM   2948 C  CG2   . VAL A 1 433 ? -12.83700 21.84400  -28.39900 1.000 41.65965  ? 399 VAL A CG2   1 
ATOM   2949 N  N     . GLU A 1 434 ? -13.24500 17.32300  -27.87700 1.000 29.26803  ? 400 GLU A N     1 
ATOM   2950 C  CA    . GLU A 1 434 ? -13.21700 15.98400  -27.30200 1.000 31.91189  ? 400 GLU A CA    1 
ATOM   2951 C  C     . GLU A 1 434 ? -12.04500 15.86400  -26.33200 1.000 39.93285  ? 400 GLU A C     1 
ATOM   2952 O  O     . GLU A 1 434 ? -10.89800 16.13000  -26.70500 1.000 37.19192  ? 400 GLU A O     1 
ATOM   2953 C  CB    . GLU A 1 434 ? -13.12000 14.94400  -28.42000 1.000 37.31844  ? 400 GLU A CB    1 
ATOM   2954 C  CG    . GLU A 1 434 ? -12.67900 13.56600  -27.98200 1.000 43.05372  ? 400 GLU A CG    1 
ATOM   2955 C  CD    . GLU A 1 434 ? -12.97300 12.51100  -29.03300 1.000 50.73600  ? 400 GLU A CD    1 
ATOM   2956 O  OE1   . GLU A 1 434 ? -13.54700 12.86900  -30.08700 1.000 52.18767  ? 400 GLU A OE1   1 
ATOM   2957 O  OE2   . GLU A 1 434 ? -12.64600 11.32300  -28.79900 1.000 46.10780  ? 400 GLU A OE2   1 
ATOM   2958 N  N     . VAL A 1 435 ? -12.33600 15.48400  -25.08200 1.000 31.31088  ? 401 VAL A N     1 
ATOM   2959 C  CA    . VAL A 1 435 ? -11.26800 15.23500  -24.11500 1.000 31.21806  ? 401 VAL A CA    1 
ATOM   2960 C  C     . VAL A 1 435 ? -10.50900 13.96600  -24.48000 1.000 30.28677  ? 401 VAL A C     1 
ATOM   2961 O  O     . VAL A 1 435 ? -9.27300  13.95300  -24.52600 1.000 35.51061  ? 401 VAL A O     1 
ATOM   2962 C  CB    . VAL A 1 435 ? -11.82800 15.14500  -22.68400 1.000 32.18136  ? 401 VAL A CB    1 
ATOM   2963 C  CG1   . VAL A 1 435 ? -10.75700 14.62000  -21.75100 1.000 33.14261  ? 401 VAL A CG1   1 
ATOM   2964 C  CG2   . VAL A 1 435 ? -12.30300 16.49600  -22.20200 1.000 30.11561  ? 401 VAL A CG2   1 
ATOM   2965 N  N     . GLY A 1 436 ? -11.23800 12.88300  -24.74100 1.000 33.61712  ? 402 GLY A N     1 
ATOM   2966 C  CA    . GLY A 1 436 ? -10.63700 11.59900  -25.04100 1.000 37.58709  ? 402 GLY A CA    1 
ATOM   2967 C  C     . GLY A 1 436 ? -11.02900 10.54600  -24.02500 1.000 35.96907  ? 402 GLY A C     1 
ATOM   2968 O  O     . GLY A 1 436 ? -10.52400 10.54600  -22.89800 1.000 39.64062  ? 402 GLY A O     1 
ATOM   2969 N  N     . ALA A 1 437 ? -11.93800 9.65200   -24.40000 1.000 36.62025  ? 403 ALA A N     1 
ATOM   2970 C  CA    . ALA A 1 437 ? -12.39800 8.62900   -23.47200 1.000 40.61151  ? 403 ALA A CA    1 
ATOM   2971 C  C     . ALA A 1 437 ? -11.29100 7.62000   -23.18200 1.000 44.77843  ? 403 ALA A C     1 
ATOM   2972 O  O     . ALA A 1 437 ? -10.45200 7.31900   -24.03700 1.000 35.45044  ? 403 ALA A O     1 
ATOM   2973 C  CB    . ALA A 1 437 ? -13.62500 7.90900   -24.03500 1.000 35.05496  ? 403 ALA A CB    1 
ATOM   2974 N  N     . ALA A 1 438 ? -11.29200 7.10000   -21.94900 1.000 37.34220  ? 404 ALA A N     1 
ATOM   2975 C  CA    . ALA A 1 438 ? -10.33500 6.07900   -21.54700 1.000 42.74400  ? 404 ALA A CA    1 
ATOM   2976 C  C     . ALA A 1 438 ? -10.95400 4.70300   -21.36500 1.000 42.08419  ? 404 ALA A C     1 
ATOM   2977 O  O     . ALA A 1 438 ? -10.21700 3.71400   -21.32100 1.000 43.81025  ? 404 ALA A O     1 
ATOM   2978 C  CB    . ALA A 1 438 ? -9.62900  6.48100   -20.24300 1.000 43.51927  ? 404 ALA A CB    1 
ATOM   2979 N  N     . GLU A 1 439 ? -12.27600 4.61200   -21.27700 1.000 42.53040  ? 405 GLU A N     1 
ATOM   2980 C  CA    . GLU A 1 439 ? -12.94700 3.34500   -21.04500 1.000 39.69394  ? 405 GLU A CA    1 
ATOM   2981 C  C     . GLU A 1 439 ? -14.35000 3.43800   -21.62100 1.000 43.17389  ? 405 GLU A C     1 
ATOM   2982 O  O     . GLU A 1 439 ? -14.98200 4.49600   -21.55300 1.000 40.96848  ? 405 GLU A O     1 
ATOM   2983 C  CB    . GLU A 1 439 ? -12.99400 3.02200   -19.54700 1.000 44.24006  ? 405 GLU A CB    1 
ATOM   2984 C  CG    . GLU A 1 439 ? -13.83100 1.81800   -19.17700 1.000 53.85012  ? 405 GLU A CG    1 
ATOM   2985 C  CD    . GLU A 1 439 ? -13.77400 1.52300   -17.68900 1.000 61.83150  ? 405 GLU A CD    1 
ATOM   2986 O  OE1   . GLU A 1 439 ? -12.85300 2.04400   -17.02800 1.000 56.39030  ? 405 GLU A OE1   1 
ATOM   2987 O  OE2   . GLU A 1 439 ? -14.64300 0.77700   -17.18400 1.000 54.09789  ? 405 GLU A OE2   1 
ATOM   2988 N  N     . TRP A 1 440 ? -14.82600 2.33900   -22.19700 1.000 33.68869  ? 406 TRP A N     1 
ATOM   2989 C  CA    . TRP A 1 440 ? -16.18600 2.26400   -22.71600 1.000 39.55402  ? 406 TRP A CA    1 
ATOM   2990 C  C     . TRP A 1 440 ? -17.03000 1.51700   -21.69500 1.000 41.53576  ? 406 TRP A C     1 
ATOM   2991 O  O     . TRP A 1 440 ? -16.85800 0.30900   -21.50500 1.000 46.22657  ? 406 TRP A O     1 
ATOM   2992 C  CB    . TRP A 1 440 ? -16.23100 1.57500   -24.07700 1.000 32.44843  ? 406 TRP A CB    1 
ATOM   2993 C  CG    . TRP A 1 440 ? -17.53800 1.76600   -24.78600 1.000 35.78224  ? 406 TRP A CG    1 
ATOM   2994 C  CD1   . TRP A 1 440 ? -18.76500 1.30600   -24.39100 1.000 38.59681  ? 406 TRP A CD1   1 
ATOM   2995 C  CD2   . TRP A 1 440 ? -17.75300 2.47600   -26.01000 1.000 30.48974  ? 406 TRP A CD2   1 
ATOM   2996 N  NE1   . TRP A 1 440 ? -19.72700 1.68200   -25.30000 1.000 32.33972  ? 406 TRP A NE1   1 
ATOM   2997 C  CE2   . TRP A 1 440 ? -19.13000 2.40000   -26.30300 1.000 32.12826  ? 406 TRP A CE2   1 
ATOM   2998 C  CE3   . TRP A 1 440 ? -16.91200 3.16200   -26.89300 1.000 35.83830  ? 406 TRP A CE3   1 
ATOM   2999 C  CZ2   . TRP A 1 440 ? -19.68300 2.98800   -27.43500 1.000 25.76694  ? 406 TRP A CZ2   1 
ATOM   3000 C  CZ3   . TRP A 1 440 ? -17.46400 3.74500   -28.01600 1.000 29.16869  ? 406 TRP A CZ3   1 
ATOM   3001 C  CH2   . TRP A 1 440 ? -18.83700 3.65400   -28.27700 1.000 35.22778  ? 406 TRP A CH2   1 
ATOM   3002 N  N     . SER A 1 441 ? -17.93600 2.23500   -21.04100 1.000 31.31702  ? 407 SER A N     1 
ATOM   3003 C  CA    . SER A 1 441 ? -18.78200 1.67100   -20.00300 1.000 40.67261  ? 407 SER A CA    1 
ATOM   3004 C  C     . SER A 1 441 ? -20.22600 1.64900   -20.48200 1.000 33.52365  ? 407 SER A C     1 
ATOM   3005 O  O     . SER A 1 441 ? -20.72500 2.64400   -21.01500 1.000 43.28254  ? 407 SER A O     1 
ATOM   3006 C  CB    . SER A 1 441 ? -18.65900 2.47400   -18.70300 1.000 32.88164  ? 407 SER A CB    1 
ATOM   3007 O  OG    . SER A 1 441 ? -19.65800 2.07600   -17.78700 1.000 54.07632  ? 407 SER A OG    1 
ATOM   3008 N  N     . MET A 1 442 ? -20.88900 0.50900   -20.29700 1.000 37.94145  ? 408 MET A N     1 
ATOM   3009 C  CA    . MET A 1 442 ? -22.30300 0.38100   -20.62300 1.000 38.16484  ? 408 MET A CA    1 
ATOM   3010 C  C     . MET A 1 442 ? -23.21700 0.89000   -19.51600 1.000 43.04741  ? 408 MET A C     1 
ATOM   3011 O  O     . MET A 1 442 ? -24.41200 1.08300   -19.76500 1.000 54.16038  ? 408 MET A O     1 
ATOM   3012 C  CB    . MET A 1 442 ? -22.64100 -1.08500  -20.92600 1.000 41.90903  ? 408 MET A CB    1 
ATOM   3013 C  CG    . MET A 1 442 ? -22.40500 -1.52900  -22.36800 1.000 45.08747  ? 408 MET A CG    1 
ATOM   3014 S  SD    . MET A 1 442 ? -22.46700 -0.16000  -23.53600 1.000 47.16712  ? 408 MET A SD    1 
ATOM   3015 C  CE    . MET A 1 442 ? -24.22900 -0.13900  -23.88700 1.000 37.93426  ? 408 MET A CE    1 
ATOM   3016 N  N     . SER A 1 443 ? -22.69100 1.12500   -18.31300 1.000 41.22586  ? 409 SER A N     1 
ATOM   3017 C  CA    . SER A 1 443 ? -23.53500 1.42800   -17.16800 1.000 51.50433  ? 409 SER A CA    1 
ATOM   3018 C  C     . SER A 1 443 ? -22.97600 2.59000   -16.35600 1.000 37.71810  ? 409 SER A C     1 
ATOM   3019 O  O     . SER A 1 443 ? -21.76000 2.68500   -16.15000 1.000 35.03410  ? 409 SER A O     1 
ATOM   3020 C  CB    . SER A 1 443 ? -23.67900 0.19400   -16.26200 1.000 49.95288  ? 409 SER A CB    1 
ATOM   3021 O  OG    . SER A 1 443 ? -22.69100 0.18700   -15.24300 1.000 61.21100  ? 409 SER A OG    1 
ATOM   3022 N  N     . PRO A 1 444 ? -23.84500 3.47700   -15.86300 1.000 41.26970  ? 410 PRO A N     1 
ATOM   3023 C  CA    . PRO A 1 444 ? -23.37200 4.58600   -15.02100 1.000 46.61269  ? 410 PRO A CA    1 
ATOM   3024 C  C     . PRO A 1 444 ? -22.94300 4.15700   -13.62800 1.000 44.76459  ? 410 PRO A C     1 
ATOM   3025 O  O     . PRO A 1 444 ? -22.26500 4.93600   -12.94700 1.000 43.68526  ? 410 PRO A O     1 
ATOM   3026 C  CB    . PRO A 1 444 ? -24.58900 5.51300   -14.95800 1.000 46.61551  ? 410 PRO A CB    1 
ATOM   3027 C  CG    . PRO A 1 444 ? -25.75200 4.57900   -15.07700 1.000 46.08811  ? 410 PRO A CG    1 
ATOM   3028 C  CD    . PRO A 1 444 ? -25.31400 3.46300   -15.99000 1.000 46.73898  ? 410 PRO A CD    1 
ATOM   3029 N  N     . TYR A 1 445 ? -23.30900 2.95100   -13.18500 1.000 45.18027  ? 411 TYR A N     1 
ATOM   3030 C  CA    . TYR A 1 445 ? -23.06300 2.53200   -11.81000 1.000 47.74749  ? 411 TYR A CA    1 
ATOM   3031 C  C     . TYR A 1 445 ? -21.74800 1.79200   -11.62900 1.000 60.40409  ? 411 TYR A C     1 
ATOM   3032 O  O     . TYR A 1 445 ? -21.20800 1.78800   -10.51600 1.000 57.50311  ? 411 TYR A O     1 
ATOM   3033 C  CB    . TYR A 1 445 ? -24.20800 1.64500   -11.31300 1.000 43.81133  ? 411 TYR A CB    1 
ATOM   3034 C  CG    . TYR A 1 445 ? -25.56200 2.20400   -11.64400 1.000 37.47536  ? 411 TYR A CG    1 
ATOM   3035 C  CD1   . TYR A 1 445 ? -26.05800 3.31400   -10.96800 1.000 44.53675  ? 411 TYR A CD1   1 
ATOM   3036 C  CD2   . TYR A 1 445 ? -26.34200 1.63700   -12.64600 1.000 45.31980  ? 411 TYR A CD2   1 
ATOM   3037 C  CE1   . TYR A 1 445 ? -27.29600 3.84000   -11.27500 1.000 44.77059  ? 411 TYR A CE1   1 
ATOM   3038 C  CE2   . TYR A 1 445 ? -27.58000 2.15800   -12.96400 1.000 48.75984  ? 411 TYR A CE2   1 
ATOM   3039 C  CZ    . TYR A 1 445 ? -28.05200 3.25600   -12.27500 1.000 48.67336  ? 411 TYR A CZ    1 
ATOM   3040 O  OH    . TYR A 1 445 ? -29.28600 3.77400   -12.58900 1.000 58.94229  ? 411 TYR A OH    1 
ATOM   3041 N  N     . ASP A 1 446 ? -21.22500 1.17200   -12.68200 1.000 57.92747  ? 412 ASP A N     1 
ATOM   3042 C  CA    . ASP A 1 446 ? -19.96200 0.45600   -12.57600 1.000 64.09002  ? 412 ASP A CA    1 
ATOM   3043 C  C     . ASP A 1 446 ? -18.81900 1.43800   -12.37400 1.000 54.43779  ? 412 ASP A C     1 
ATOM   3044 O  O     . ASP A 1 446 ? -18.73600 2.46000   -13.06000 1.000 47.27799  ? 412 ASP A O     1 
ATOM   3045 C  CB    . ASP A 1 446 ? -19.72300 -0.38400  -13.82900 1.000 69.47183  ? 412 ASP A CB    1 
ATOM   3046 C  CG    . ASP A 1 446 ? -20.60000 -1.61600  -13.87900 1.000 68.59283  ? 412 ASP A CG    1 
ATOM   3047 O  OD1   . ASP A 1 446 ? -21.05900 -2.05800  -12.80500 1.000 74.86110  ? 412 ASP A OD1   1 
ATOM   3048 O  OD2   . ASP A 1 446 ? -20.83500 -2.13800  -14.99300 1.000 72.17604  ? 412 ASP A OD2   1 
ATOM   3049 N  N     . ALA A 1 447 ? -17.94500 1.13700   -11.41800 1.000 62.78971  ? 413 ALA A N     1 
ATOM   3050 C  CA    . ALA A 1 447 ? -16.74800 1.94400   -11.23300 1.000 64.62569  ? 413 ALA A CA    1 
ATOM   3051 C  C     . ALA A 1 447 ? -15.78800 1.71400   -12.39300 1.000 63.09790  ? 413 ALA A C     1 
ATOM   3052 O  O     . ALA A 1 447 ? -15.63300 0.59100   -12.87900 1.000 62.56713  ? 413 ALA A O     1 
ATOM   3053 C  CB    . ALA A 1 447 ? -16.07300 1.60500   -9.90600  1.000 62.05742  ? 413 ALA A CB    1 
ATOM   3054 N  N     . LYS A 1 448 ? -15.14900 2.78900   -12.84500 1.000 56.40667  ? 414 LYS A N     1 
ATOM   3055 C  CA    . LYS A 1 448 ? -14.25500 2.71600   -13.99000 1.000 51.51743  ? 414 LYS A CA    1 
ATOM   3056 C  C     . LYS A 1 448 ? -12.86500 2.27500   -13.54500 1.000 60.12767  ? 414 LYS A C     1 
ATOM   3057 O  O     . LYS A 1 448 ? -12.30800 2.82000   -12.58700 1.000 60.06020  ? 414 LYS A O     1 
ATOM   3058 C  CB    . LYS A 1 448 ? -14.19400 4.06300   -14.70900 1.000 57.51726  ? 414 LYS A CB    1 
ATOM   3059 C  CG    . LYS A 1 448 ? -15.46500 4.37600   -15.48800 1.000 55.17541  ? 414 LYS A CG    1 
ATOM   3060 C  CD    . LYS A 1 448 ? -15.28200 5.55700   -16.41400 1.000 54.04274  ? 414 LYS A CD    1 
ATOM   3061 C  CE    . LYS A 1 448 ? -16.40300 5.62000   -17.43500 1.000 42.53451  ? 414 LYS A CE    1 
ATOM   3062 N  NZ    . LYS A 1 448 ? -17.73900 5.72700   -16.79800 1.000 46.65374  ? 414 LYS A NZ    1 
ATOM   3063 N  N     . LYS A 1 449 ? -12.31400 1.27800   -14.24100 1.000 56.90693  ? 415 LYS A N     1 
ATOM   3064 C  CA    . LYS A 1 449 ? -10.98300 0.77500   -13.92300 1.000 62.42950  ? 415 LYS A CA    1 
ATOM   3065 C  C     . LYS A 1 449 ? -9.87600  1.69500   -14.41700 1.000 61.46736  ? 415 LYS A C     1 
ATOM   3066 O  O     . LYS A 1 449 ? -8.72900  1.55400   -13.97900 1.000 65.75001  ? 415 LYS A O     1 
ATOM   3067 C  CB    . LYS A 1 449 ? -10.78700 -0.62700  -14.51400 1.000 70.60644  ? 415 LYS A CB    1 
ATOM   3068 C  CG    . LYS A 1 449 ? -11.79500 -1.66700  -14.02500 1.000 72.94032  ? 415 LYS A CG    1 
ATOM   3069 C  CD    . LYS A 1 449 ? -12.00300 -1.58100  -12.51600 1.000 80.98408  ? 415 LYS A CD    1 
ATOM   3070 C  CE    . LYS A 1 449 ? -12.27900 -2.94700  -11.90000 1.000 84.83745  ? 415 LYS A CE    1 
ATOM   3071 N  NZ    . LYS A 1 449 ? -11.03300 -3.66500  -11.50600 1.000 84.08131  ? 415 LYS A NZ    1 
ATOM   3072 N  N     . THR A 1 450 ? -10.18400 2.61600   -15.32300 1.000 66.60891  ? 416 THR A N     1 
ATOM   3073 C  CA    . THR A 1 450 ? -9.23000  3.60100   -15.80600 1.000 59.92793  ? 416 THR A CA    1 
ATOM   3074 C  C     . THR A 1 450 ? -9.73000  4.99900   -15.47200 1.000 60.80421  ? 416 THR A C     1 
ATOM   3075 O  O     . THR A 1 450 ? -10.86700 5.19500   -15.03500 1.000 67.48969  ? 416 THR A O     1 
ATOM   3076 C  CB    . THR A 1 450 ? -9.00500  3.47300   -17.31500 1.000 58.73461  ? 416 THR A CB    1 
ATOM   3077 O  OG1   . THR A 1 450 ? -10.18800 3.89600   -18.00500 1.000 82.21868  ? 416 THR A OG1   1 
ATOM   3078 C  CG2   . THR A 1 450 ? -8.68200  2.03500   -17.69000 1.000 63.57846  ? 416 THR A CG2   1 
ATOM   3079 N  N     . VAL A 1 451 ? -8.85900  5.98000   -15.68200 1.000 51.49969  ? 417 VAL A N     1 
ATOM   3080 C  CA    . VAL A 1 451 ? -9.17800  7.37100   -15.40100 1.000 50.31618  ? 417 VAL A CA    1 
ATOM   3081 C  C     . VAL A 1 451 ? -8.73600  8.22200   -16.58100 1.000 48.64344  ? 417 VAL A C     1 
ATOM   3082 O  O     . VAL A 1 451 ? -7.76700  7.89900   -17.27600 1.000 50.21557  ? 417 VAL A O     1 
ATOM   3083 C  CB    . VAL A 1 451 ? -8.52000  7.84600   -14.08200 1.000 51.77460  ? 417 VAL A CB    1 
ATOM   3084 C  CG1   . VAL A 1 451 ? -7.02700  8.07000   -14.26500 1.000 49.10128  ? 417 VAL A CG1   1 
ATOM   3085 C  CG2   . VAL A 1 451 ? -9.17200  9.10800   -13.59500 1.000 54.89543  ? 417 VAL A CG2   1 
ATOM   3086 N  N     . VAL A 1 452 ? -9.47800  9.29900   -16.82600 1.000 45.62528  ? 418 VAL A N     1 
ATOM   3087 C  CA    . VAL A 1 452 ? -9.07800  10.30100  -17.80700 1.000 40.62714  ? 418 VAL A CA    1 
ATOM   3088 C  C     . VAL A 1 452 ? -8.03500  11.20100  -17.15900 1.000 47.88889  ? 418 VAL A C     1 
ATOM   3089 O  O     . VAL A 1 452 ? -8.32200  11.89000  -16.17400 1.000 40.38495  ? 418 VAL A O     1 
ATOM   3090 C  CB    . VAL A 1 452 ? -10.28200 11.11500  -18.30000 1.000 42.88190  ? 418 VAL A CB    1 
ATOM   3091 C  CG1   . VAL A 1 452 ? -9.81900  12.17100  -19.28500 1.000 40.07138  ? 418 VAL A CG1   1 
ATOM   3092 C  CG2   . VAL A 1 452 ? -11.32700 10.19900  -18.93600 1.000 36.98117  ? 418 VAL A CG2   1 
ATOM   3093 N  N     . ARG A 1 453 ? -6.82500  11.19700  -17.70900 1.000 42.80429  ? 419 ARG A N     1 
ATOM   3094 C  CA    . ARG A 1 453 ? -5.70900  11.86300  -17.05500 1.000 53.28051  ? 419 ARG A CA    1 
ATOM   3095 C  C     . ARG A 1 453 ? -5.82000  13.38000  -17.19100 1.000 49.34730  ? 419 ARG A C     1 
ATOM   3096 O  O     . ARG A 1 453 ? -6.50200  13.91100  -18.07300 1.000 44.23975  ? 419 ARG A O     1 
ATOM   3097 C  CB    . ARG A 1 453 ? -4.38300  11.36100  -17.62700 1.000 50.66591  ? 419 ARG A CB    1 
ATOM   3098 C  CG    . ARG A 1 453 ? -4.08900  9.90800   -17.26800 1.000 62.62503  ? 419 ARG A CG    1 
ATOM   3099 C  CD    . ARG A 1 453 ? -2.71500  9.73600   -16.63800 1.000 82.39747  ? 419 ARG A CD    1 
ATOM   3100 N  NE    . ARG A 1 453 ? -2.25600  8.35300   -16.71100 1.000 96.60487  ? 419 ARG A NE    1 
ATOM   3101 C  CZ    . ARG A 1 453 ? -1.54900  7.84700   -17.71300 1.000 101.64080 ? 419 ARG A CZ    1 
ATOM   3102 N  NH1   . ARG A 1 453 ? -1.21000  8.58200   -18.76000 1.000 97.81718  ? 419 ARG A NH1   1 
ATOM   3103 N  NH2   . ARG A 1 453 ? -1.17500  6.57100   -17.66400 1.000 98.00704  ? 419 ARG A NH2   1 
ATOM   3104 N  N     . ALA A 1 454 ? -5.11700  14.07900  -16.29700 1.000 46.22797  ? 420 ALA A N     1 
ATOM   3105 C  CA    . ALA A 1 454 ? -5.29300  15.52100  -16.15600 1.000 42.42417  ? 420 ALA A CA    1 
ATOM   3106 C  C     . ALA A 1 454 ? -4.82400  16.27900  -17.39200 1.000 44.10048  ? 420 ALA A C     1 
ATOM   3107 O  O     . ALA A 1 454 ? -5.42800  17.29200  -17.76300 1.000 42.36868  ? 420 ALA A O     1 
ATOM   3108 C  CB    . ALA A 1 454 ? -4.55100  16.01900  -14.91400 1.000 47.67546  ? 420 ALA A CB    1 
ATOM   3109 N  N     . GLU A 1 455 ? -3.74300  15.82200  -18.03400 1.000 39.47806  ? 421 GLU A N     1 
ATOM   3110 C  CA    . GLU A 1 455 ? -3.24600  16.52500  -19.21500 1.000 48.71610  ? 421 GLU A CA    1 
ATOM   3111 C  C     . GLU A 1 455 ? -4.29200  16.54700  -20.32100 1.000 42.05053  ? 421 GLU A C     1 
ATOM   3112 O  O     . GLU A 1 455 ? -4.44100  17.55500  -21.02400 1.000 41.64715  ? 421 GLU A O     1 
ATOM   3113 C  CB    . GLU A 1 455 ? -1.95500  15.88400  -19.73100 1.000 46.99754  ? 421 GLU A CB    1 
ATOM   3114 C  CG    . GLU A 1 455 ? -0.91500  15.57300  -18.66900 1.000 67.89531  ? 421 GLU A CG    1 
ATOM   3115 C  CD    . GLU A 1 455 ? -1.12700  14.21300  -18.02400 1.000 81.05360  ? 421 GLU A CD    1 
ATOM   3116 O  OE1   . GLU A 1 455 ? -0.90800  13.18500  -18.70500 1.000 93.76133  ? 421 GLU A OE1   1 
ATOM   3117 O  OE2   . GLU A 1 455 ? -1.52000  14.17500  -16.83700 1.000 68.72939  ? 421 GLU A OE2   1 
ATOM   3118 N  N     . ARG A 1 456 ? -5.02700  15.44500  -20.48900 1.000 36.47534  ? 422 ARG A N     1 
ATOM   3119 C  CA    . ARG A 1 456 ? -6.05500  15.39900  -21.52500 1.000 38.28650  ? 422 ARG A CA    1 
ATOM   3120 C  C     . ARG A 1 456 ? -7.17000  16.39200  -21.23000 1.000 45.64725  ? 422 ARG A C     1 
ATOM   3121 O  O     . ARG A 1 456 ? -7.66700  17.06700  -22.13900 1.000 38.00987  ? 422 ARG A O     1 
ATOM   3122 C  CB    . ARG A 1 456 ? -6.60700  13.97800  -21.65600 1.000 40.11106  ? 422 ARG A CB    1 
ATOM   3123 C  CG    . ARG A 1 456 ? -5.56200  12.95100  -22.08000 1.000 42.49083  ? 422 ARG A CG    1 
ATOM   3124 C  CD    . ARG A 1 456 ? -6.14900  11.91700  -23.03300 1.000 54.01665  ? 422 ARG A CD    1 
ATOM   3125 N  NE    . ARG A 1 456 ? -6.61200  12.51700  -24.28000 1.000 63.31743  ? 422 ARG A NE    1 
ATOM   3126 C  CZ    . ARG A 1 456 ? -6.03500  12.34100  -25.46100 1.000 63.46702  ? 422 ARG A CZ    1 
ATOM   3127 N  NH1   . ARG A 1 456 ? -4.95200  11.59200  -25.59700 1.000 60.54650  ? 422 ARG A NH1   1 
ATOM   3128 N  NH2   . ARG A 1 456 ? -6.56000  12.93100  -26.53400 1.000 51.22658  ? 422 ARG A NH2   1 
ATOM   3129 N  N     . ILE A 1 457 ? -7.56500  16.50500  -19.96000 1.000 39.81759  ? 423 ILE A N     1 
ATOM   3130 C  CA    . ILE A 1 457 ? -8.55900  17.50000  -19.57400 1.000 33.95863  ? 423 ILE A CA    1 
ATOM   3131 C  C     . ILE A 1 457 ? -8.00200  18.90400  -19.76000 1.000 37.64468  ? 423 ILE A C     1 
ATOM   3132 O  O     . ILE A 1 457 ? -8.69000  19.80100  -20.26100 1.000 35.98890  ? 423 ILE A O     1 
ATOM   3133 C  CB    . ILE A 1 457 ? -9.01700  17.25600  -18.12300 1.000 42.72703  ? 423 ILE A CB    1 
ATOM   3134 C  CG1   . ILE A 1 457 ? -9.57300  15.84000  -17.98200 1.000 41.81496  ? 423 ILE A CG1   1 
ATOM   3135 C  CG2   . ILE A 1 457 ? -10.05400 18.28400  -17.69600 1.000 36.75499  ? 423 ILE A CG2   1 
ATOM   3136 C  CD1   . ILE A 1 457 ? -9.90300  15.45000  -16.56400 1.000 45.00622  ? 423 ILE A CD1   1 
ATOM   3137 N  N     . GLU A 1 458 ? -6.74500  19.11500  -19.36700 1.000 37.13703  ? 424 GLU A N     1 
ATOM   3138 C  CA    . GLU A 1 458 ? -6.13800  20.43300  -19.50500 1.000 39.56008  ? 424 GLU A CA    1 
ATOM   3139 C  C     . GLU A 1 458 ? -5.99000  20.82400  -20.97100 1.000 37.23711  ? 424 GLU A C     1 
ATOM   3140 O  O     . GLU A 1 458 ? -6.25700  21.97200  -21.34600 1.000 37.85994  ? 424 GLU A O     1 
ATOM   3141 C  CB    . GLU A 1 458 ? -4.78200  20.45500  -18.80100 1.000 40.18374  ? 424 GLU A CB    1 
ATOM   3142 C  CG    . GLU A 1 458 ? -3.94700  21.67700  -19.11400 1.000 39.56411  ? 424 GLU A CG    1 
ATOM   3143 C  CD    . GLU A 1 458 ? -2.48900  21.48300  -18.76100 1.000 48.76293  ? 424 GLU A CD    1 
ATOM   3144 O  OE1   . GLU A 1 458 ? -2.13500  20.38600  -18.27700 1.000 46.61208  ? 424 GLU A OE1   1 
ATOM   3145 O  OE2   . GLU A 1 458 ? -1.70000  22.42800  -18.97200 1.000 51.42201  ? 424 GLU A OE2   1 
ATOM   3146 N  N     . LYS A 1 459 ? -5.57700  19.88100  -21.81900 1.000 40.40036  ? 425 LYS A N     1 
ATOM   3147 C  CA    . LYS A 1 459 ? -5.39600  20.19600  -23.23300 1.000 37.45317  ? 425 LYS A CA    1 
ATOM   3148 C  C     . LYS A 1 459 ? -6.72400  20.52900  -23.90600 1.000 34.56908  ? 425 LYS A C     1 
ATOM   3149 O  O     . LYS A 1 459 ? -6.80600  21.48200  -24.69000 1.000 33.57759  ? 425 LYS A O     1 
ATOM   3150 C  CB    . LYS A 1 459 ? -4.70800  19.03300  -23.94800 1.000 38.09002  ? 425 LYS A CB    1 
ATOM   3151 C  CG    . LYS A 1 459 ? -4.10800  19.40600  -25.29600 1.000 61.70061  ? 425 LYS A CG    1 
ATOM   3152 C  CD    . LYS A 1 459 ? -4.03300  18.20500  -26.22700 1.000 66.12531  ? 425 LYS A CD    1 
ATOM   3153 C  CE    . LYS A 1 459 ? -3.62000  18.62000  -27.63300 1.000 71.05083  ? 425 LYS A CE    1 
ATOM   3154 N  NZ    . LYS A 1 459 ? -4.57600  18.12500  -28.66500 1.000 70.43894  ? 425 LYS A NZ    1 
ATOM   3155 N  N     . ALA A 1 460 ? -7.77900  19.76400  -23.60600 1.000 32.05285  ? 426 ALA A N     1 
ATOM   3156 C  CA    . ALA A 1 460 ? -9.07600  20.01600  -24.23300 1.000 35.04448  ? 426 ALA A CA    1 
ATOM   3157 C  C     . ALA A 1 460 ? -9.65300  21.36100  -23.80700 1.000 33.67953  ? 426 ALA A C     1 
ATOM   3158 O  O     . ALA A 1 460 ? -10.19600 22.10100  -24.63700 1.000 32.21872  ? 426 ALA A O     1 
ATOM   3159 C  CB    . ALA A 1 460 ? -10.04900 18.88400  -23.90200 1.000 29.34985  ? 426 ALA A CB    1 
ATOM   3160 N  N     . VAL A 1 461 ? -9.55400  21.69600  -22.51800 1.000 30.69107  ? 427 VAL A N     1 
ATOM   3161 C  CA    . VAL A 1 461 ? -10.04100 22.99500  -22.05400 1.000 32.14109  ? 427 VAL A CA    1 
ATOM   3162 C  C     . VAL A 1 461 ? -9.26400  24.12400  -22.72700 1.000 33.67154  ? 427 VAL A C     1 
ATOM   3163 O  O     . VAL A 1 461 ? -9.85000  25.09700  -23.22000 1.000 36.38028  ? 427 VAL A O     1 
ATOM   3164 C  CB    . VAL A 1 461 ? -9.96500  23.08500  -20.51900 1.000 34.22197  ? 427 VAL A CB    1 
ATOM   3165 C  CG1   . VAL A 1 461 ? -10.32100 24.48400  -20.04500 1.000 26.40105  ? 427 VAL A CG1   1 
ATOM   3166 C  CG2   . VAL A 1 461 ? -10.89700 22.06400  -19.87900 1.000 32.18621  ? 427 VAL A CG2   1 
ATOM   3167 N  N     . LYS A 1 462 ? -7.93000  24.00800  -22.76200 1.000 33.46420  ? 428 LYS A N     1 
ATOM   3168 C  CA    . LYS A 1 462 ? -7.11500  25.01700  -23.43900 1.000 44.31899  ? 428 LYS A CA    1 
ATOM   3169 C  C     . LYS A 1 462 ? -7.47700  25.12200  -24.91300 1.000 41.55732  ? 428 LYS A C     1 
ATOM   3170 O  O     . LYS A 1 462 ? -7.51900  26.22200  -25.47400 1.000 40.07167  ? 428 LYS A O     1 
ATOM   3171 C  CB    . LYS A 1 462 ? -5.62700  24.69100  -23.29300 1.000 34.43002  ? 428 LYS A CB    1 
ATOM   3172 C  CG    . LYS A 1 462 ? -5.02000  25.03400  -21.94900 1.000 45.02486  ? 428 LYS A CG    1 
ATOM   3173 C  CD    . LYS A 1 462 ? -3.51400  24.82100  -21.98700 1.000 42.37256  ? 428 LYS A CD    1 
ATOM   3174 C  CE    . LYS A 1 462 ? -2.85300  25.25000  -20.68900 1.000 61.96159  ? 428 LYS A CE    1 
ATOM   3175 N  NZ    . LYS A 1 462 ? -1.37400  25.07400  -20.74800 1.000 62.01062  ? 428 LYS A NZ    1 
ATOM   3176 N  N     . LYS A 1 463 ? -7.73700  23.98500  -25.55800 1.000 38.69821  ? 429 LYS A N     1 
ATOM   3177 C  CA    . LYS A 1 463 ? -8.09600  23.99600  -26.97200 1.000 34.72070  ? 429 LYS A CA    1 
ATOM   3178 C  C     . LYS A 1 463 ? -9.37700  24.78900  -27.21300 1.000 35.71471  ? 429 LYS A C     1 
ATOM   3179 O  O     . LYS A 1 463 ? -9.49400  25.50800  -28.21000 1.000 40.43538  ? 429 LYS A O     1 
ATOM   3180 C  CB    . LYS A 1 463 ? -8.23900  22.55600  -27.46900 1.000 37.93732  ? 429 LYS A CB    1 
ATOM   3181 C  CG    . LYS A 1 463 ? -8.70000  22.40300  -28.91000 1.000 49.25983  ? 429 LYS A CG    1 
ATOM   3182 C  CD    . LYS A 1 463 ? -8.15800  21.10700  -29.50400 1.000 54.16838  ? 429 LYS A CD    1 
ATOM   3183 C  CE    . LYS A 1 463 ? -8.92700  20.70100  -30.74900 1.000 67.12924  ? 429 LYS A CE    1 
ATOM   3184 N  NZ    . LYS A 1 463 ? -9.23000  19.23900  -30.79100 1.000 71.83884  ? 429 LYS A NZ    1 
ATOM   3185 N  N     . LEU A 1 464 ? -10.34800 24.68200  -26.30700 1.000 35.01417  ? 430 LEU A N     1 
ATOM   3186 C  CA    . LEU A 1 464 ? -11.58400 25.43400  -26.48800 1.000 37.17203  ? 430 LEU A CA    1 
ATOM   3187 C  C     . LEU A 1 464 ? -11.44100 26.87500  -26.01200 1.000 43.80553  ? 430 LEU A C     1 
ATOM   3188 O  O     . LEU A 1 464 ? -11.80000 27.81200  -26.73500 1.000 44.29498  ? 430 LEU A O     1 
ATOM   3189 C  CB    . LEU A 1 464 ? -12.73800 24.74700  -25.75400 1.000 31.57277  ? 430 LEU A CB    1 
ATOM   3190 C  CG    . LEU A 1 464 ? -14.04200 25.55200  -25.78000 1.000 33.64468  ? 430 LEU A CG    1 
ATOM   3191 C  CD1   . LEU A 1 464 ? -14.55300 25.72200  -27.20800 1.000 29.86169  ? 430 LEU A CD1   1 
ATOM   3192 C  CD2   . LEU A 1 464 ? -15.10300 24.90300  -24.92000 1.000 31.99478  ? 430 LEU A CD2   1 
ATOM   3193 N  N     . MET A 1 465 ? -10.90500 27.07000  -24.80200 1.000 41.81266  ? 431 MET A N     1 
ATOM   3194 C  CA    . MET A 1 465 ? -11.00700 28.36000  -24.12500 1.000 40.12370  ? 431 MET A CA    1 
ATOM   3195 C  C     . MET A 1 465 ? -9.97000  29.37000  -24.60700 1.000 49.71611  ? 431 MET A C     1 
ATOM   3196 O  O     . MET A 1 465 ? -10.22200 30.57900  -24.54500 1.000 52.21905  ? 431 MET A O     1 
ATOM   3197 C  CB    . MET A 1 465 ? -10.87600 28.16600  -22.61400 1.000 38.02104  ? 431 MET A CB    1 
ATOM   3198 C  CG    . MET A 1 465 ? -11.93000 27.26900  -21.97400 1.000 43.20764  ? 431 MET A CG    1 
ATOM   3199 S  SD    . MET A 1 465 ? -13.57600 27.99400  -21.87200 1.000 61.07929  ? 431 MET A SD    1 
ATOM   3200 C  CE    . MET A 1 465 ? -13.28000 29.35700  -20.74600 1.000 41.67669  ? 431 MET A CE    1 
ATOM   3201 N  N     . ASP A 1 466 ? -8.80400  28.91400  -25.06600 1.000 48.12819  ? 432 ASP A N     1 
ATOM   3202 C  CA    . ASP A 1 466 ? -7.80200  29.83700  -25.58600 1.000 58.51892  ? 432 ASP A CA    1 
ATOM   3203 C  C     . ASP A 1 466 ? -8.32300  30.54600  -26.83000 1.000 65.38304  ? 432 ASP A C     1 
ATOM   3204 O  O     . ASP A 1 466 ? -9.07600  29.98100  -27.62800 1.000 57.96977  ? 432 ASP A O     1 
ATOM   3205 C  CB    . ASP A 1 466 ? -6.50000  29.10600  -25.91600 1.000 57.14601  ? 432 ASP A CB    1 
ATOM   3206 C  CG    . ASP A 1 466 ? -5.78500  28.59300  -24.67900 1.000 56.54118  ? 432 ASP A CG    1 
ATOM   3207 O  OD1   . ASP A 1 466 ? -6.34400  28.70900  -23.56700 1.000 46.35779  ? 432 ASP A OD1   1 
ATOM   3208 O  OD2   . ASP A 1 466 ? -4.66100  28.06900  -24.82300 1.000 53.73212  ? 432 ASP A OD2   1 
ATOM   3209 N  N     . SER A 1 467 ? -7.89900  31.80000  -26.99500 1.000 74.83737  ? 433 SER A N     1 
ATOM   3210 C  CA    . SER A 1 467 ? -8.45800  32.64700  -28.04300 1.000 93.77725  ? 433 SER A CA    1 
ATOM   3211 C  C     . SER A 1 467 ? -7.84200  32.34600  -29.40500 1.000 99.22029  ? 433 SER A C     1 
ATOM   3212 O  O     . SER A 1 467 ? -8.56300  32.09600  -30.37900 1.000 94.18974  ? 433 SER A O     1 
ATOM   3213 C  CB    . SER A 1 467 ? -8.25900  34.11900  -27.68100 1.000 91.93769  ? 433 SER A CB    1 
ATOM   3214 O  OG    . SER A 1 467 ? -6.88100  34.43000  -27.59500 1.000 88.05408  ? 433 SER A OG    1 
ATOM   3215 N  N     . ASN A 1 468 ? -6.51300  32.37400  -29.49400 1.000 99.32053  ? 434 ASN A N     1 
ATOM   3216 C  CA    . ASN A 1 468 ? -5.81900  32.20000  -30.77100 1.000 106.64468 ? 434 ASN A CA    1 
ATOM   3217 C  C     . ASN A 1 468 ? -5.67500  30.71000  -31.04700 1.000 101.49389 ? 434 ASN A C     1 
ATOM   3218 O  O     . ASN A 1 468 ? -4.68200  30.07900  -30.68300 1.000 112.44559 ? 434 ASN A O     1 
ATOM   3219 C  CB    . ASN A 1 468 ? -4.46300  32.89400  -30.74900 1.000 99.76553  ? 434 ASN A CB    1 
ATOM   3220 C  CG    . ASN A 1 468 ? -3.85500  33.03100  -32.13500 1.000 102.50762 ? 434 ASN A CG    1 
ATOM   3221 O  OD1   . ASN A 1 468 ? -4.57000  33.09000  -33.13700 1.000 97.59647  ? 434 ASN A OD1   1 
ATOM   3222 N  ND2   . ASN A 1 468 ? -2.52800  33.08400  -32.19700 1.000 104.58034 ? 434 ASN A ND2   1 
ATOM   3223 N  N     . GLY A 1 469 ? -6.68300  30.13800  -31.70300 1.000 74.12286  ? 435 GLY A N     1 
ATOM   3224 C  CA    . GLY A 1 469 ? -6.62600  28.73400  -32.05300 1.000 70.27202  ? 435 GLY A CA    1 
ATOM   3225 C  C     . GLY A 1 469 ? -7.90700  28.18700  -32.64500 1.000 74.17583  ? 435 GLY A C     1 
ATOM   3226 O  O     . GLY A 1 469 ? -8.59000  28.85900  -33.42400 1.000 59.88635  ? 435 GLY A O     1 
ATOM   3227 N  N     . GLU A 1 470 ? -8.23700  26.95200  -32.27200 1.000 63.73166  ? 436 GLU A N     1 
ATOM   3228 C  CA    . GLU A 1 470 ? -9.41100  26.27300  -32.80200 1.000 57.29651  ? 436 GLU A CA    1 
ATOM   3229 C  C     . GLU A 1 470 ? -10.69800 26.68000  -32.09800 1.000 45.72802  ? 436 GLU A C     1 
ATOM   3230 O  O     . GLU A 1 470 ? -11.78100 26.51500  -32.67200 1.000 38.45187  ? 436 GLU A O     1 
ATOM   3231 C  CB    . GLU A 1 470 ? -9.21500  24.76000  -32.69100 1.000 56.67739  ? 436 GLU A CB    1 
ATOM   3232 C  CG    . GLU A 1 470 ? -9.77000  23.96600  -33.84900 1.000 61.34766  ? 436 GLU A CG    1 
ATOM   3233 C  CD    . GLU A 1 470 ? -9.15500  22.58200  -33.93800 1.000 71.55276  ? 436 GLU A CD    1 
ATOM   3234 O  OE1   . GLU A 1 470 ? -8.12600  22.34600  -33.26700 1.000 75.06014  ? 436 GLU A OE1   1 
ATOM   3235 O  OE2   . GLU A 1 470 ? -9.70000  21.73300  -34.67500 1.000 71.77632  ? 436 GLU A OE2   1 
ATOM   3236 N  N     . GLY A 1 471 ? -10.60400 27.21300  -30.87800 1.000 42.08303  ? 437 GLY A N     1 
ATOM   3237 C  CA    . GLY A 1 471 ? -11.79600 27.46500  -30.08800 1.000 32.77487  ? 437 GLY A CA    1 
ATOM   3238 C  C     . GLY A 1 471 ? -12.68200 28.55700  -30.64900 1.000 31.29845  ? 437 GLY A C     1 
ATOM   3239 O  O     . GLY A 1 471 ? -13.89500 28.55000  -30.42400 1.000 31.89845  ? 437 GLY A O     1 
ATOM   3240 N  N     . GLY A 1 472 ? -12.10100 29.50800  -31.37900 1.000 33.84299  ? 438 GLY A N     1 
ATOM   3241 C  CA    . GLY A 1 472 ? -12.91800 30.53200  -32.00800 1.000 33.82853  ? 438 GLY A CA    1 
ATOM   3242 C  C     . GLY A 1 472 ? -13.91100 29.95800  -33.00200 1.000 31.31088  ? 438 GLY A C     1 
ATOM   3243 O  O     . GLY A 1 472 ? -15.08200 30.34400  -33.01900 1.000 31.85235  ? 438 GLY A O     1 
ATOM   3244 N  N     . GLU A 1 473 ? -13.45900 29.02700  -33.84600 1.000 31.55895  ? 439 GLU A N     1 
ATOM   3245 C  CA    . GLU A 1 473 ? -14.36700 28.38400  -34.79300 1.000 33.40051  ? 439 GLU A CA    1 
ATOM   3246 C  C     . GLU A 1 473 ? -15.45400 27.60600  -34.06000 1.000 30.89862  ? 439 GLU A C     1 
ATOM   3247 O  O     . GLU A 1 473 ? -16.64500 27.72300  -34.37500 1.000 30.55671  ? 439 GLU A O     1 
ATOM   3248 C  CB    . GLU A 1 473 ? -13.58600 27.45400  -35.72800 1.000 24.79542  ? 439 GLU A CB    1 
ATOM   3249 C  CG    . GLU A 1 473 ? -14.47000 26.45400  -36.47400 1.000 26.36518  ? 439 GLU A CG    1 
ATOM   3250 C  CD    . GLU A 1 473 ? -13.72200 25.22000  -36.95900 1.000 32.01129  ? 439 GLU A CD    1 
ATOM   3251 O  OE1   . GLU A 1 473 ? -12.51800 25.07300  -36.65100 1.000 34.38220  ? 439 GLU A OE1   1 
ATOM   3252 O  OE2   . GLU A 1 473 ? -14.34400 24.39300  -37.65800 1.000 32.83226  ? 439 GLU A OE2   1 
ATOM   3253 N  N     . ILE A 1 474 ? -15.05400 26.79900  -33.08000 1.000 35.15613  ? 440 ILE A N     1 
ATOM   3254 C  CA    . ILE A 1 474 ? -16.01300 25.97000  -32.35800 1.000 32.95892  ? 440 ILE A CA    1 
ATOM   3255 C  C     . ILE A 1 474 ? -17.01400 26.83900  -31.60900 1.000 31.26483  ? 440 ILE A C     1 
ATOM   3256 O  O     . ILE A 1 474 ? -18.22100 26.56800  -31.61500 1.000 30.33129  ? 440 ILE A O     1 
ATOM   3257 C  CB    . ILE A 1 474 ? -15.26400 25.00000  -31.42900 1.000 29.75861  ? 440 ILE A CB    1 
ATOM   3258 C  CG1   . ILE A 1 474 ? -14.45100 24.03800  -32.29700 1.000 40.61069  ? 440 ILE A CG1   1 
ATOM   3259 C  CG2   . ILE A 1 474 ? -16.23900 24.24300  -30.54900 1.000 25.57808  ? 440 ILE A CG2   1 
ATOM   3260 C  CD1   . ILE A 1 474 ? -13.52200 23.15300  -31.54500 1.000 46.59122  ? 440 ILE A CD1   1 
ATOM   3261 N  N     . ARG A 1 475 ? -16.54000 27.92200  -30.99500 1.000 27.91987  ? 441 ARG A N     1 
ATOM   3262 C  CA    . ARG A 1 475 ? -17.46200 28.83700  -30.33400 1.000 37.00319  ? 441 ARG A CA    1 
ATOM   3263 C  C     . ARG A 1 475 ? -18.44400 29.44100  -31.33100 1.000 27.80502  ? 441 ARG A C     1 
ATOM   3264 O  O     . ARG A 1 475 ? -19.64300 29.54400  -31.04800 1.000 32.04266  ? 441 ARG A O     1 
ATOM   3265 C  CB    . ARG A 1 475 ? -16.68300 29.92600  -29.59800 1.000 33.44043  ? 441 ARG A CB    1 
ATOM   3266 C  CG    . ARG A 1 475 ? -17.55700 30.90500  -28.83600 1.000 42.13518  ? 441 ARG A CG    1 
ATOM   3267 C  CD    . ARG A 1 475 ? -16.74800 31.67000  -27.80100 1.000 54.01341  ? 441 ARG A CD    1 
ATOM   3268 N  NE    . ARG A 1 475 ? -16.34400 30.82000  -26.68400 1.000 51.19899  ? 441 ARG A NE    1 
ATOM   3269 C  CZ    . ARG A 1 475 ? -15.13600 30.29000  -26.54200 1.000 58.92461  ? 441 ARG A CZ    1 
ATOM   3270 N  NH1   . ARG A 1 475 ? -14.18300 30.48200  -27.44400 1.000 48.60270  ? 441 ARG A NH1   1 
ATOM   3271 N  NH2   . ARG A 1 475 ? -14.87500 29.55100  -25.46700 1.000 51.68043  ? 441 ARG A NH2   1 
ATOM   3272 N  N     . LYS A 1 476 ? -17.96300 29.81800  -32.51900 1.000 36.32254  ? 442 LYS A N     1 
ATOM   3273 C  CA    . LYS A 1 476 ? -18.85900 30.38900  -33.52100 1.000 30.12883  ? 442 LYS A CA    1 
ATOM   3274 C  C     . LYS A 1 476 ? -19.84500 29.34700  -34.04400 1.000 30.83516  ? 442 LYS A C     1 
ATOM   3275 O  O     . LYS A 1 476 ? -21.03800 29.63800  -34.20600 1.000 29.65171  ? 442 LYS A O     1 
ATOM   3276 C  CB    . LYS A 1 476 ? -18.04400 30.99400  -34.66300 1.000 43.68369  ? 442 LYS A CB    1 
ATOM   3277 C  CG    . LYS A 1 476 ? -18.88100 31.68500  -35.72400 1.000 42.45518  ? 442 LYS A CG    1 
ATOM   3278 C  CD    . LYS A 1 476 ? -18.00700 32.33700  -36.77800 1.000 49.92090  ? 442 LYS A CD    1 
ATOM   3279 C  CE    . LYS A 1 476 ? -18.85600 32.92000  -37.89900 1.000 59.94736  ? 442 LYS A CE    1 
ATOM   3280 N  NZ    . LYS A 1 476 ? -18.02400 33.43800  -39.02100 1.000 70.00856  ? 442 LYS A NZ    1 
ATOM   3281 N  N     . ARG A 1 477 ? -19.36800 28.12600  -34.30800 1.000 30.64828  ? 443 ARG A N     1 
ATOM   3282 C  CA    . ARG A 1 477 ? -20.26300 27.05600  -34.74700 1.000 29.04413  ? 443 ARG A CA    1 
ATOM   3283 C  C     . ARG A 1 477 ? -21.33000 26.75900  -33.70100 1.000 33.03217  ? 443 ARG A C     1 
ATOM   3284 O  O     . ARG A 1 477 ? -22.48500 26.47400  -34.04300 1.000 28.44361  ? 443 ARG A O     1 
ATOM   3285 C  CB    . ARG A 1 477 ? -19.45800 25.79500  -35.05400 1.000 24.94452  ? 443 ARG A CB    1 
ATOM   3286 C  CG    . ARG A 1 477 ? -18.62700 25.87000  -36.33100 1.000 33.83346  ? 443 ARG A CG    1 
ATOM   3287 C  CD    . ARG A 1 477 ? -17.95500 24.53600  -36.58700 1.000 23.30302  ? 443 ARG A CD    1 
ATOM   3288 N  NE    . ARG A 1 477 ? -17.12200 24.54700  -37.78200 1.000 35.00852  ? 443 ARG A NE    1 
ATOM   3289 C  CZ    . ARG A 1 477 ? -17.58200 24.31700  -39.00300 1.000 34.59854  ? 443 ARG A CZ    1 
ATOM   3290 N  NH1   . ARG A 1 477 ? -18.87600 24.15500  -39.23400 1.000 27.29086  ? 443 ARG A NH1   1 
ATOM   3291 N  NH2   . ARG A 1 477 ? -16.72600 24.26000  -40.01800 1.000 31.84486  ? 443 ARG A NH2   1 
ATOM   3292 N  N     . ALA A 1 478 ? -20.96300 26.82300  -32.41800 1.000 25.85084  ? 444 ALA A N     1 
ATOM   3293 C  CA    . ALA A 1 478 ? -21.93000 26.55600  -31.35600 1.000 25.25289  ? 444 ALA A CA    1 
ATOM   3294 C  C     . ALA A 1 478 ? -23.02500 27.61300  -31.33300 1.000 29.73708  ? 444 ALA A C     1 
ATOM   3295 O  O     . ALA A 1 478 ? -24.20700 27.29000  -31.16100 1.000 32.17483  ? 444 ALA A O     1 
ATOM   3296 C  CB    . ALA A 1 478 ? -21.21700 26.49200  -30.00500 1.000 29.28577  ? 444 ALA A CB    1 
ATOM   3297 N  N     . LYS A 1 479 ? -22.64600 28.88300  -31.50400 1.000 32.78049  ? 445 LYS A N     1 
ATOM   3298 C  CA    . LYS A 1 479 ? -23.63500 29.95600  -31.56800 1.000 36.57614  ? 445 LYS A CA    1 
ATOM   3299 C  C     . LYS A 1 479 ? -24.54100 29.80300  -32.78300 1.000 32.80071  ? 445 LYS A C     1 
ATOM   3300 O  O     . LYS A 1 479 ? -25.74100 30.09400  -32.71700 1.000 34.77831  ? 445 LYS A O     1 
ATOM   3301 C  CB    . LYS A 1 479 ? -22.93200 31.31500  -31.58700 1.000 35.08225  ? 445 LYS A CB    1 
ATOM   3302 C  CG    . LYS A 1 479 ? -23.76800 32.44300  -32.17700 1.000 55.54764  ? 445 LYS A CG    1 
ATOM   3303 C  CD    . LYS A 1 479 ? -22.92500 33.66600  -32.50500 1.000 60.18276  ? 445 LYS A CD    1 
ATOM   3304 C  CE    . LYS A 1 479 ? -23.71200 34.65500  -33.35700 1.000 75.52348  ? 445 LYS A CE    1 
ATOM   3305 N  NZ    . LYS A 1 479 ? -24.95200 35.12500  -32.67300 1.000 82.79476  ? 445 LYS A NZ    1 
ATOM   3306 N  N     . GLU A 1 480 ? -23.99000 29.33400  -33.90200 1.000 33.77266  ? 446 GLU A N     1 
ATOM   3307 C  CA    . GLU A 1 480 ? -24.80900 29.16700  -35.09600 1.000 35.51981  ? 446 GLU A CA    1 
ATOM   3308 C  C     . GLU A 1 480 ? -25.75800 27.98600  -34.96600 1.000 33.12915  ? 446 GLU A C     1 
ATOM   3309 O  O     . GLU A 1 480 ? -26.88400 28.03100  -35.47800 1.000 32.65011  ? 446 GLU A O     1 
ATOM   3310 C  CB    . GLU A 1 480 ? -23.91300 29.00700  -36.31800 1.000 37.73624  ? 446 GLU A CB    1 
ATOM   3311 C  CG    . GLU A 1 480 ? -23.28200 30.30800  -36.76700 1.000 37.45642  ? 446 GLU A CG    1 
ATOM   3312 C  CD    . GLU A 1 480 ? -22.07200 30.07300  -37.62100 1.000 45.83463  ? 446 GLU A CD    1 
ATOM   3313 O  OE1   . GLU A 1 480 ? -21.67400 28.89600  -37.75100 1.000 45.66616  ? 446 GLU A OE1   1 
ATOM   3314 O  OE2   . GLU A 1 480 ? -21.52300 31.05700  -38.15700 1.000 52.72073  ? 446 GLU A OE2   1 
ATOM   3315 N  N     . MET A 1 481 ? -25.32300 26.91700  -34.29600 1.000 32.37828  ? 447 MET A N     1 
ATOM   3316 C  CA    . MET A 1 481 ? -26.22400 25.79300  -34.07200 1.000 26.11222  ? 447 MET A CA    1 
ATOM   3317 C  C     . MET A 1 481 ? -27.36800 26.19200  -33.15000 1.000 33.05844  ? 447 MET A C     1 
ATOM   3318 O  O     . MET A 1 481 ? -28.48600 25.68100  -33.29300 1.000 31.29939  ? 447 MET A O     1 
ATOM   3319 C  CB    . MET A 1 481 ? -25.46300 24.60600  -33.47500 1.000 26.28109  ? 447 MET A CB    1 
ATOM   3320 C  CG    . MET A 1 481 ? -26.23600 23.28900  -33.48700 1.000 28.59612  ? 447 MET A CG    1 
ATOM   3321 S  SD    . MET A 1 481 ? -26.82700 22.78900  -35.12400 1.000 34.26069  ? 447 MET A SD    1 
ATOM   3322 C  CE    . MET A 1 481 ? -25.28100 22.25500  -35.88100 1.000 30.54474  ? 447 MET A CE    1 
ATOM   3323 N  N     . LYS A 1 482 ? -27.10500 27.09100  -32.19500 1.000 30.42091  ? 448 LYS A N     1 
ATOM   3324 C  CA    . LYS A 1 482 ? -28.18100 27.63400  -31.37300 1.000 34.87355  ? 448 LYS A CA    1 
ATOM   3325 C  C     . LYS A 1 482 ? -29.26500 28.26000  -32.24300 1.000 32.11622  ? 448 LYS A C     1 
ATOM   3326 O  O     . LYS A 1 482 ? -30.46000 28.00600  -32.05000 1.000 32.61232  ? 448 LYS A O     1 
ATOM   3327 C  CB    . LYS A 1 482 ? -27.62200 28.66500  -30.39100 1.000 31.78961  ? 448 LYS A CB    1 
ATOM   3328 C  CG    . LYS A 1 482 ? -28.70700 29.43900  -29.66000 1.000 32.44124  ? 448 LYS A CG    1 
ATOM   3329 C  CD    . LYS A 1 482 ? -28.14000 30.54800  -28.80000 1.000 35.69094  ? 448 LYS A CD    1 
ATOM   3330 C  CE    . LYS A 1 482 ? -29.26100 31.32200  -28.11700 1.000 43.91842  ? 448 LYS A CE    1 
ATOM   3331 N  NZ    . LYS A 1 482 ? -28.74000 32.39700  -27.22600 1.000 47.88823  ? 448 LYS A NZ    1 
ATOM   3332 N  N     . GLU A 1 483 ? -28.86100 29.08400  -33.21300 1.000 32.66697  ? 449 GLU A N     1 
ATOM   3333 C  CA    . GLU A 1 483 ? -29.82700 29.70800  -34.11200 1.000 37.84453  ? 449 GLU A CA    1 
ATOM   3334 C  C     . GLU A 1 483 ? -30.55500 28.66600  -34.94600 1.000 36.68526  ? 449 GLU A C     1 
ATOM   3335 O  O     . GLU A 1 483 ? -31.76700 28.77100  -35.16900 1.000 29.99969  ? 449 GLU A O     1 
ATOM   3336 C  CB    . GLU A 1 483 ? -29.12100 30.70800  -35.02700 1.000 40.17274  ? 449 GLU A CB    1 
ATOM   3337 C  CG    . GLU A 1 483 ? -28.44800 31.85000  -34.29600 1.000 46.93199  ? 449 GLU A CG    1 
ATOM   3338 C  CD    . GLU A 1 483 ? -27.60800 32.70100  -35.22600 1.000 69.72565  ? 449 GLU A CD    1 
ATOM   3339 O  OE1   . GLU A 1 483 ? -28.08500 33.01500  -36.33800 1.000 82.54991  ? 449 GLU A OE1   1 
ATOM   3340 O  OE2   . GLU A 1 483 ? -26.46600 33.04600  -34.84900 1.000 72.07656  ? 449 GLU A OE2   1 
ATOM   3341 N  N     . LYS A 1 484 ? -29.83200 27.65300  -35.42200 1.000 28.71663  ? 450 LYS A N     1 
ATOM   3342 C  CA    . LYS A 1 484 ? -30.47300 26.62100  -36.22500 1.000 33.04667  ? 450 LYS A CA    1 
ATOM   3343 C  C     . LYS A 1 484 ? -31.45900 25.80600  -35.39900 1.000 37.25000  ? 450 LYS A C     1 
ATOM   3344 O  O     . LYS A 1 484 ? -32.51100 25.40200  -35.91000 1.000 34.70039  ? 450 LYS A O     1 
ATOM   3345 C  CB    . LYS A 1 484 ? -29.40600 25.73200  -36.86300 1.000 37.00997  ? 450 LYS A CB    1 
ATOM   3346 C  CG    . LYS A 1 484 ? -28.73100 26.41400  -38.04900 1.000 42.71849  ? 450 LYS A CG    1 
ATOM   3347 C  CD    . LYS A 1 484 ? -27.59900 25.59700  -38.65900 1.000 57.26092  ? 450 LYS A CD    1 
ATOM   3348 C  CE    . LYS A 1 484 ? -26.34100 25.65600  -37.81100 1.000 52.24468  ? 450 LYS A CE    1 
ATOM   3349 N  NZ    . LYS A 1 484 ? -25.15700 25.08300  -38.51800 1.000 56.49741  ? 450 LYS A NZ    1 
ATOM   3350 N  N     . ALA A 1 485 ? -31.15600 25.58200  -34.11800 1.000 35.45256  ? 451 ALA A N     1 
ATOM   3351 C  CA    . ALA A 1 485 ? -32.05500 24.80000  -33.27800 1.000 30.69789  ? 451 ALA A CA    1 
ATOM   3352 C  C     . ALA A 1 485 ? -33.33500 25.56900  -32.97200 1.000 34.24938  ? 451 ALA A C     1 
ATOM   3353 O  O     . ALA A 1 485 ? -34.43200 25.00000  -33.01900 1.000 28.88885  ? 451 ALA A O     1 
ATOM   3354 C  CB    . ALA A 1 485 ? -31.34100 24.39800  -31.98700 1.000 32.53786  ? 451 ALA A CB    1 
ATOM   3355 N  N     . TRP A 1 486 ? -33.22100 26.85900  -32.64600 1.000 32.14423  ? 452 TRP A N     1 
ATOM   3356 C  CA    . TRP A 1 486 ? -34.42100 27.62900  -32.33200 1.000 37.88430  ? 452 TRP A CA    1 
ATOM   3357 C  C     . TRP A 1 486 ? -35.24200 27.91000  -33.58400 1.000 34.22930  ? 452 TRP A C     1 
ATOM   3358 O  O     . TRP A 1 486 ? -36.47600 27.91700  -33.52400 1.000 37.36537  ? 452 TRP A O     1 
ATOM   3359 C  CB    . TRP A 1 486 ? -34.04800 28.93300  -31.62000 1.000 34.41372  ? 452 TRP A CB    1 
ATOM   3360 C  CG    . TRP A 1 486 ? -33.73400 28.71900  -30.16600 1.000 31.60095  ? 452 TRP A CG    1 
ATOM   3361 C  CD1   . TRP A 1 486 ? -32.50600 28.77900  -29.57300 1.000 29.66059  ? 452 TRP A CD1   1 
ATOM   3362 C  CD2   . TRP A 1 486 ? -34.66600 28.38000  -29.13000 1.000 34.09244  ? 452 TRP A CD2   1 
ATOM   3363 N  NE1   . TRP A 1 486 ? -32.61700 28.50300  -28.22700 1.000 33.28615  ? 452 TRP A NE1   1 
ATOM   3364 C  CE2   . TRP A 1 486 ? -33.93300 28.25700  -27.93200 1.000 32.55882  ? 452 TRP A CE2   1 
ATOM   3365 C  CE3   . TRP A 1 486 ? -36.04900 28.17100  -29.10100 1.000 35.06109  ? 452 TRP A CE3   1 
ATOM   3366 C  CZ2   . TRP A 1 486 ? -34.53800 27.93900  -26.71500 1.000 32.85873  ? 452 TRP A CZ2   1 
ATOM   3367 C  CZ3   . TRP A 1 486 ? -36.64800 27.85700  -27.89300 1.000 39.87637  ? 452 TRP A CZ3   1 
ATOM   3368 C  CH2   . TRP A 1 486 ? -35.89300 27.74700  -26.71600 1.000 35.45468  ? 452 TRP A CH2   1 
ATOM   3369 N  N     . LYS A 1 487 ? -34.58100 28.13300  -34.72200 1.000 33.29270  ? 453 LYS A N     1 
ATOM   3370 C  CA    . LYS A 1 487 ? -35.30500 28.28100  -35.98000 1.000 33.11575  ? 453 LYS A CA    1 
ATOM   3371 C  C     . LYS A 1 487 ? -36.12400 27.03400  -36.29700 1.000 33.89904  ? 453 LYS A C     1 
ATOM   3372 O  O     . LYS A 1 487 ? -37.27800 27.13300  -36.72700 1.000 36.59448  ? 453 LYS A O     1 
ATOM   3373 C  CB    . LYS A 1 487 ? -34.32400 28.58600  -37.11100 1.000 36.96326  ? 453 LYS A CB    1 
ATOM   3374 C  CG    . LYS A 1 487 ? -34.99500 28.95600  -38.42700 1.000 51.53142  ? 453 LYS A CG    1 
ATOM   3375 C  CD    . LYS A 1 487 ? -34.00200 28.96100  -39.57600 1.000 58.05610  ? 453 LYS A CD    1 
ATOM   3376 C  CE    . LYS A 1 487 ? -34.64500 28.48000  -40.86800 1.000 68.50740  ? 453 LYS A CE    1 
ATOM   3377 N  NZ    . LYS A 1 487 ? -33.96400 29.05600  -42.06100 1.000 76.35475  ? 453 LYS A NZ    1 
ATOM   3378 N  N     . ALA A 1 488 ? -35.54800 25.85100  -36.07500 1.000 31.51120  ? 454 ALA A N     1 
ATOM   3379 C  CA    . ALA A 1 488 ? -36.24100 24.61300  -36.41500 1.000 33.38018  ? 454 ALA A CA    1 
ATOM   3380 C  C     . ALA A 1 488 ? -37.51500 24.43100  -35.59900 1.000 37.90158  ? 454 ALA A C     1 
ATOM   3381 O  O     . ALA A 1 488 ? -38.47200 23.80800  -36.07300 1.000 37.60899  ? 454 ALA A O     1 
ATOM   3382 C  CB    . ALA A 1 488 ? -35.30400 23.41800  -36.21500 1.000 32.64733  ? 454 ALA A CB    1 
ATOM   3383 N  N     . VAL A 1 489 ? -37.55800 24.96600  -34.37800 1.000 30.64744  ? 455 VAL A N     1 
ATOM   3384 C  CA    . VAL A 1 489 ? -38.73100 24.79600  -33.52400 1.000 34.82763  ? 455 VAL A CA    1 
ATOM   3385 C  C     . VAL A 1 489 ? -39.63300 26.02100  -33.51200 1.000 38.60894  ? 455 VAL A C     1 
ATOM   3386 O  O     . VAL A 1 489 ? -40.70000 25.98100  -32.87800 1.000 35.96231  ? 455 VAL A O     1 
ATOM   3387 C  CB    . VAL A 1 489 ? -38.33000 24.43200  -32.07700 1.000 34.65283  ? 455 VAL A CB    1 
ATOM   3388 C  CG1   . VAL A 1 489 ? -37.39100 23.22600  -32.06800 1.000 31.37041  ? 455 VAL A CG1   1 
ATOM   3389 C  CG2   . VAL A 1 489 ? -37.69900 25.62600  -31.37900 1.000 32.26717  ? 455 VAL A CG2   1 
ATOM   3390 N  N     . GLN A 1 490 ? -39.24400 27.10200  -34.18000 1.000 37.88185  ? 456 GLN A N     1 
ATOM   3391 C  CA    . GLN A 1 490 ? -40.07200 28.29300  -34.25800 1.000 40.78860  ? 456 GLN A CA    1 
ATOM   3392 C  C     . GLN A 1 490 ? -41.05200 28.17000  -35.42000 1.000 43.90266  ? 456 GLN A C     1 
ATOM   3393 O  O     . GLN A 1 490 ? -41.02500 27.20900  -36.19300 1.000 41.70379  ? 456 GLN A O     1 
ATOM   3394 C  CB    . GLN A 1 490 ? -39.20000 29.54100  -34.39500 1.000 35.96752  ? 456 GLN A CB    1 
ATOM   3395 C  CG    . GLN A 1 490 ? -38.88500 30.21200  -33.06200 1.000 49.64749  ? 456 GLN A CG    1 
ATOM   3396 C  CD    . GLN A 1 490 ? -37.60800 31.03200  -33.09700 1.000 57.46764  ? 456 GLN A CD    1 
ATOM   3397 O  OE1   . GLN A 1 490 ? -37.01300 31.23300  -34.15700 1.000 59.40372  ? 456 GLN A OE1   1 
ATOM   3398 N  NE2   . GLN A 1 490 ? -37.18300 31.51600  -31.93300 1.000 57.59797  ? 456 GLN A NE2   1 
ATOM   3399 N  N     . GLU A 1 491 ? -41.93100 29.16100  -35.54400 1.000 45.58786  ? 457 GLU A N     1 
ATOM   3400 C  CA    . GLU A 1 491 ? -42.92400 29.16400  -36.60900 1.000 51.69615  ? 457 GLU A CA    1 
ATOM   3401 C  C     . GLU A 1 491 ? -42.24700 29.03600  -37.96700 1.000 43.04125  ? 457 GLU A C     1 
ATOM   3402 O  O     . GLU A 1 491 ? -41.36700 29.83000  -38.31300 1.000 46.68731  ? 457 GLU A O     1 
ATOM   3403 C  CB    . GLU A 1 491 ? -43.75500 30.44300  -36.53500 1.000 59.42723  ? 457 GLU A CB    1 
ATOM   3404 C  CG    . GLU A 1 491 ? -45.16700 30.29800  -37.07200 1.000 72.57385  ? 457 GLU A CG    1 
ATOM   3405 C  CD    . GLU A 1 491 ? -45.71800 31.60400  -37.60600 1.000 85.06810  ? 457 GLU A CD    1 
ATOM   3406 O  OE1   . GLU A 1 491 ? -45.09800 32.18100  -38.52500 1.000 81.47666  ? 457 GLU A OE1   1 
ATOM   3407 O  OE2   . GLU A 1 491 ? -46.76900 32.05700  -37.10200 1.000 96.38234  ? 457 GLU A OE2   1 
ATOM   3408 N  N     . GLY A 1 492 ? -42.63400 28.01100  -38.72200 1.000 51.40607  ? 458 GLY A N     1 
ATOM   3409 C  CA    . GLY A 1 492 ? -42.07400 27.77300  -40.03400 1.000 44.84230  ? 458 GLY A CA    1 
ATOM   3410 C  C     . GLY A 1 492 ? -40.79300 26.96800  -40.06100 1.000 41.73683  ? 458 GLY A C     1 
ATOM   3411 O  O     . GLY A 1 492 ? -40.25400 26.73800  -41.15100 1.000 38.78707  ? 458 GLY A O     1 
ATOM   3412 N  N     . GLY A 1 493 ? -40.28700 26.52900  -38.90500 1.000 36.77655  ? 459 GLY A N     1 
ATOM   3413 C  CA    . GLY A 1 493 ? -39.07800 25.73300  -38.87900 1.000 31.46300  ? 459 GLY A CA    1 
ATOM   3414 C  C     . GLY A 1 493 ? -39.31700 24.28100  -39.25800 1.000 37.72673  ? 459 GLY A C     1 
ATOM   3415 O  O     . GLY A 1 493 ? -40.44800 23.79300  -39.27900 1.000 35.88752  ? 459 GLY A O     1 
ATOM   3416 N  N     . SER A 1 494 ? -38.21000 23.59000  -39.55100 1.000 33.11770  ? 460 SER A N     1 
ATOM   3417 C  CA    . SER A 1 494 ? -38.27800 22.21300  -40.03800 1.000 30.84211  ? 460 SER A CA    1 
ATOM   3418 C  C     . SER A 1 494 ? -39.07700 21.31000  -39.10200 1.000 36.09852  ? 460 SER A C     1 
ATOM   3419 O  O     . SER A 1 494 ? -39.86600 20.47600  -39.56100 1.000 39.22302  ? 460 SER A O     1 
ATOM   3420 C  CB    . SER A 1 494 ? -36.86400 21.66100  -40.23100 1.000 29.19766  ? 460 SER A CB    1 
ATOM   3421 O  OG    . SER A 1 494 ? -36.15100 21.66100  -39.00200 1.000 31.69080  ? 460 SER A OG    1 
ATOM   3422 N  N     . SER A 1 495 ? -38.89600 21.45600  -37.78800 1.000 26.85105  ? 461 SER A N     1 
ATOM   3423 C  CA    . SER A 1 495 ? -39.56400 20.53800  -36.87100 1.000 34.27485  ? 461 SER A CA    1 
ATOM   3424 C  C     . SER A 1 495 ? -41.03300 20.88900  -36.68300 1.000 36.04712  ? 461 SER A C     1 
ATOM   3425 O  O     . SER A 1 495 ? -41.85700 19.99000  -36.47400 1.000 33.62961  ? 461 SER A O     1 
ATOM   3426 C  CB    . SER A 1 495 ? -38.84800 20.51500  -35.51900 1.000 32.50945  ? 461 SER A CB    1 
ATOM   3427 O  OG    . SER A 1 495 ? -37.57600 19.90000  -35.63700 1.000 35.06274  ? 461 SER A OG    1 
ATOM   3428 N  N     . GLN A 1 496 ? -41.37600 22.18000  -36.74400 1.000 33.90408  ? 462 GLN A N     1 
ATOM   3429 C  CA    . GLN A 1 496 ? -42.78100 22.57300  -36.70700 1.000 40.21033  ? 462 GLN A CA    1 
ATOM   3430 C  C     . GLN A 1 496 ? -43.50900 22.11700  -37.96400 1.000 36.48043  ? 462 GLN A C     1 
ATOM   3431 O  O     . GLN A 1 496 ? -44.62700 21.59600  -37.88600 1.000 41.03128  ? 462 GLN A O     1 
ATOM   3432 C  CB    . GLN A 1 496 ? -42.90700 24.08800  -36.54300 1.000 41.54678  ? 462 GLN A CB    1 
ATOM   3433 C  CG    . GLN A 1 496 ? -42.49800 24.60800  -35.18100 1.000 44.84427  ? 462 GLN A CG    1 
ATOM   3434 C  CD    . GLN A 1 496 ? -43.53100 24.32900  -34.11100 1.000 49.33919  ? 462 GLN A CD    1 
ATOM   3435 O  OE1   . GLN A 1 496 ? -44.60100 23.78700  -34.39100 1.000 43.01767  ? 462 GLN A OE1   1 
ATOM   3436 N  NE2   . GLN A 1 496 ? -43.22000 24.70500  -32.87500 1.000 42.27350  ? 462 GLN A NE2   1 
ATOM   3437 N  N     . ASN A 1 497 ? -42.89400 22.31100  -39.13300 1.000 35.26645  ? 463 ASN A N     1 
ATOM   3438 C  CA    . ASN A 1 497 ? -43.49800 21.82200  -40.36700 1.000 31.50006  ? 463 ASN A CA    1 
ATOM   3439 C  C     . ASN A 1 497 ? -43.66600 20.31100  -40.33400 1.000 37.14034  ? 463 ASN A C     1 
ATOM   3440 O  O     . ASN A 1 497 ? -44.71600 19.78700  -40.72100 1.000 37.78950  ? 463 ASN A O     1 
ATOM   3441 C  CB    . ASN A 1 497 ? -42.65900 22.24200  -41.57700 1.000 29.46702  ? 463 ASN A CB    1 
ATOM   3442 C  CG    . ASN A 1 497 ? -42.57100 23.75200  -41.73300 1.000 41.90298  ? 463 ASN A CG    1 
ATOM   3443 O  OD1   . ASN A 1 497 ? -43.33200 24.49600  -41.11400 1.000 46.62518  ? 463 ASN A OD1   1 
ATOM   3444 N  ND2   . ASN A 1 497 ? -41.65300 24.20900  -42.57400 1.000 40.11716  ? 463 ASN A ND2   1 
ATOM   3445 N  N     . CYS A 1 498 ? -42.64500 19.59300  -39.86400 1.000 34.26889  ? 464 CYS A N     1 
ATOM   3446 C  CA    . CYS A 1 498 ? -42.72000 18.13600  -39.84700 1.000 34.24938  ? 464 CYS A CA    1 
ATOM   3447 C  C     . CYS A 1 498 ? -43.77300 17.64700  -38.85900 1.000 36.21563  ? 464 CYS A C     1 
ATOM   3448 O  O     . CYS A 1 498 ? -44.46700 16.65800  -39.12300 1.000 36.98420  ? 464 CYS A O     1 
ATOM   3449 C  CB    . CYS A 1 498 ? -41.35200 17.54400  -39.51800 1.000 38.00751  ? 464 CYS A CB    1 
ATOM   3450 S  SG    . CYS A 1 498 ? -41.31400 15.75000  -39.53100 1.000 38.28158  ? 464 CYS A SG    1 
ATOM   3451 N  N     . LEU A 1 499 ? -43.91500 18.33100  -37.71900 1.000 32.40397  ? 465 LEU A N     1 
ATOM   3452 C  CA    . LEU A 1 499 ? -44.95500 17.96000  -36.76500 1.000 36.36459  ? 465 LEU A CA    1 
ATOM   3453 C  C     . LEU A 1 499 ? -46.34200 18.11400  -37.37700 1.000 40.77987  ? 465 LEU A C     1 
ATOM   3454 O  O     . LEU A 1 499 ? -47.22300 17.26900  -37.16800 1.000 35.81538  ? 465 LEU A O     1 
ATOM   3455 C  CB    . LEU A 1 499 ? -44.83400 18.80400  -35.49700 1.000 36.71339  ? 465 LEU A CB    1 
ATOM   3456 C  CG    . LEU A 1 499 ? -45.88500 18.54500  -34.41700 1.000 47.78773  ? 465 LEU A CG    1 
ATOM   3457 C  CD1   . LEU A 1 499 ? -45.85600 17.08500  -33.96900 1.000 36.70307  ? 465 LEU A CD1   1 
ATOM   3458 C  CD2   . LEU A 1 499 ? -45.68600 19.48100  -33.22900 1.000 43.33625  ? 465 LEU A CD2   1 
ATOM   3459 N  N     . THR A 1 500 ? -46.55400 19.19000  -38.13800 1.000 36.19909  ? 466 THR A N     1 
ATOM   3460 C  CA    . THR A 1 500 ? -47.83100 19.37800  -38.81900 1.000 36.17270  ? 466 THR A CA    1 
ATOM   3461 C  C     . THR A 1 500 ? -48.07100 18.28400  -39.85300 1.000 34.98773  ? 466 THR A C     1 
ATOM   3462 O  O     . THR A 1 500 ? -49.16600 17.71200  -39.91100 1.000 37.53148  ? 466 THR A O     1 
ATOM   3463 C  CB    . THR A 1 500 ? -47.87800 20.76400  -39.46500 1.000 43.95257  ? 466 THR A CB    1 
ATOM   3464 O  OG1   . THR A 1 500 ? -47.72700 21.76000  -38.44500 1.000 41.53192  ? 466 THR A OG1   1 
ATOM   3465 C  CG2   . THR A 1 500 ? -49.20400 20.98500  -40.20200 1.000 34.58860  ? 466 THR A CG2   1 
ATOM   3466 N  N     . LYS A 1 501 ? -47.05600 17.96700  -40.66300 1.000 37.92899  ? 467 LYS A N     1 
ATOM   3467 C  CA    . LYS A 1 501 ? -47.20300 16.90500  -41.65500 1.000 37.87952  ? 467 LYS A CA    1 
ATOM   3468 C  C     . LYS A 1 501 ? -47.45400 15.55300  -41.00300 1.000 40.13322  ? 467 LYS A C     1 
ATOM   3469 O  O     . LYS A 1 501 ? -48.21400 14.73800  -41.54300 1.000 40.04820  ? 467 LYS A O     1 
ATOM   3470 C  CB    . LYS A 1 501 ? -45.96200 16.83300  -42.54700 1.000 30.21599  ? 467 LYS A CB    1 
ATOM   3471 C  CG    . LYS A 1 501 ? -45.82400 18.01000  -43.50500 1.000 56.60583  ? 467 LYS A CG    1 
ATOM   3472 C  CD    . LYS A 1 501 ? -44.72100 17.78900  -44.52800 1.000 54.86765  ? 467 LYS A CD    1 
ATOM   3473 C  CE    . LYS A 1 501 ? -44.63900 18.95600  -45.51000 1.000 61.41019  ? 467 LYS A CE    1 
ATOM   3474 N  NZ    . LYS A 1 501 ? -45.93100 19.18800  -46.23400 1.000 51.05074  ? 467 LYS A NZ    1 
ATOM   3475 N  N     . LEU A 1 502 ? -46.81500 15.29100  -39.85700 1.000 35.15496  ? 468 LEU A N     1 
ATOM   3476 C  CA    . LEU A 1 502 ? -47.03000 14.02900  -39.15300 1.000 35.07145  ? 468 LEU A CA    1 
ATOM   3477 C  C     . LEU A 1 502 ? -48.49100 13.87300  -38.75100 1.000 35.98757  ? 468 LEU A C     1 
ATOM   3478 O  O     . LEU A 1 502 ? -49.11200 12.83800  -39.01600 1.000 35.76396  ? 468 LEU A O     1 
ATOM   3479 C  CB    . LEU A 1 502 ? -46.12100 13.95000  -37.92200 1.000 38.13898  ? 468 LEU A CB    1 
ATOM   3480 C  CG    . LEU A 1 502 ? -46.38000 12.81500  -36.92300 1.000 37.00311  ? 468 LEU A CG    1 
ATOM   3481 C  CD1   . LEU A 1 502 ? -46.21100 11.45600  -37.59500 1.000 33.59013  ? 468 LEU A CD1   1 
ATOM   3482 C  CD2   . LEU A 1 502 ? -45.46800 12.93700  -35.70800 1.000 30.55368  ? 468 LEU A CD2   1 
ATOM   3483 N  N     . VAL A 1 503 ? -49.05600 14.89800  -38.10900 1.000 34.54611  ? 469 VAL A N     1 
ATOM   3484 C  CA    . VAL A 1 503 ? -50.44400 14.82000  -37.66200 1.000 38.55173  ? 469 VAL A CA    1 
ATOM   3485 C  C     . VAL A 1 503 ? -51.38400 14.69600  -38.85600 1.000 38.84628  ? 469 VAL A C     1 
ATOM   3486 O  O     . VAL A 1 503 ? -52.34700 13.91800  -38.82700 1.000 44.70974  ? 469 VAL A O     1 
ATOM   3487 C  CB    . VAL A 1 503 ? -50.78600 16.03500  -36.77800 1.000 40.23400  ? 469 VAL A CB    1 
ATOM   3488 C  CG1   . VAL A 1 503 ? -52.26300 16.03800  -36.41000 1.000 42.84092  ? 469 VAL A CG1   1 
ATOM   3489 C  CG2   . VAL A 1 503 ? -49.93400 16.01300  -35.51700 1.000 34.52338  ? 469 VAL A CG2   1 
ATOM   3490 N  N     . ASP A 1 504 ? -51.10900 15.43900  -39.93200 1.000 36.58352  ? 470 ASP A N     1 
ATOM   3491 C  CA    . ASP A 1 504 ? -51.90500 15.29500  -41.14900 1.000 44.69735  ? 470 ASP A CA    1 
ATOM   3492 C  C     . ASP A 1 504 ? -51.81200 13.87900  -41.70400 1.000 48.92675  ? 470 ASP A C     1 
ATOM   3493 O  O     . ASP A 1 504 ? -52.82600 13.29300  -42.10200 1.000 43.89309  ? 470 ASP A O     1 
ATOM   3494 C  CB    . ASP A 1 504 ? -51.45300 16.30800  -42.20300 1.000 42.49143  ? 470 ASP A CB    1 
ATOM   3495 C  CG    . ASP A 1 504 ? -51.81600 17.72800  -41.83500 1.000 52.27835  ? 470 ASP A CG    1 
ATOM   3496 O  OD1   . ASP A 1 504 ? -52.65300 17.91100  -40.92300 1.000 60.67269  ? 470 ASP A OD1   1 
ATOM   3497 O  OD2   . ASP A 1 504 ? -51.26400 18.66200  -42.45400 1.000 66.47855  ? 470 ASP A OD2   1 
ATOM   3498 N  N     . TYR A 1 505 ? -50.60200 13.31200  -41.73500 1.000 39.19918  ? 471 TYR A N     1 
ATOM   3499 C  CA    . TYR A 1 505 ? -50.43600 11.94900  -42.23000 1.000 43.60323  ? 471 TYR A CA    1 
ATOM   3500 C  C     . TYR A 1 505 ? -51.19700 10.95100  -41.36500 1.000 49.24181  ? 471 TYR A C     1 
ATOM   3501 O  O     . TYR A 1 505 ? -51.80900 10.01000  -41.88400 1.000 53.29909  ? 471 TYR A O     1 
ATOM   3502 C  CB    . TYR A 1 505 ? -48.95000 11.59100  -42.29000 1.000 37.36952  ? 471 TYR A CB    1 
ATOM   3503 C  CG    . TYR A 1 505 ? -48.66600 10.10500  -42.39500 1.000 37.21874  ? 471 TYR A CG    1 
ATOM   3504 C  CD1   . TYR A 1 505 ? -48.82500 9.42900   -43.59800 1.000 42.73753  ? 471 TYR A CD1   1 
ATOM   3505 C  CD2   . TYR A 1 505 ? -48.23100 9.38000   -41.28800 1.000 39.44312  ? 471 TYR A CD2   1 
ATOM   3506 C  CE1   . TYR A 1 505 ? -48.56200 8.07300   -43.70000 1.000 39.74778  ? 471 TYR A CE1   1 
ATOM   3507 C  CE2   . TYR A 1 505 ? -47.96500 8.02500   -41.38000 1.000 41.89457  ? 471 TYR A CE2   1 
ATOM   3508 C  CZ    . TYR A 1 505 ? -48.13400 7.37800   -42.59000 1.000 39.65271  ? 471 TYR A CZ    1 
ATOM   3509 O  OH    . TYR A 1 505 ? -47.87200 6.03400   -42.68300 1.000 36.40306  ? 471 TYR A OH    1 
ATOM   3510 N  N     . LEU A 1 506 ? -51.17300 11.14100  -40.04200 1.000 36.74150  ? 472 LEU A N     1 
ATOM   3511 C  CA    . LEU A 1 506 ? -51.92400 10.25700  -39.15600 1.000 45.77708  ? 472 LEU A CA    1 
ATOM   3512 C  C     . LEU A 1 506 ? -53.41900 10.34900  -39.42500 1.000 49.13612  ? 472 LEU A C     1 
ATOM   3513 O  O     . LEU A 1 506 ? -54.13100 9.34000   -39.35800 1.000 50.38171  ? 472 LEU A O     1 
ATOM   3514 C  CB    . LEU A 1 506 ? -51.62500 10.58900  -37.69200 1.000 39.91150  ? 472 LEU A CB    1 
ATOM   3515 C  CG    . LEU A 1 506 ? -50.21400 10.26000  -37.19400 1.000 47.86259  ? 472 LEU A CG    1 
ATOM   3516 C  CD1   . LEU A 1 506 ? -50.08800 10.52400  -35.70200 1.000 37.64678  ? 472 LEU A CD1   1 
ATOM   3517 C  CD2   . LEU A 1 506 ? -49.85900 8.81800   -37.51600 1.000 44.33564  ? 472 LEU A CD2   1 
ATOM   3518 N  N     . HIS A 1 507 ? -53.91400 11.55200  -39.73000 1.000 44.07286  ? 473 HIS A N     1 
ATOM   3519 C  CA    . HIS A 1 507 ? -55.32900 11.70300  -40.05600 1.000 53.99240  ? 473 HIS A CA    1 
ATOM   3520 C  C     . HIS A 1 507 ? -55.70500 10.86800  -41.27300 1.000 58.10982  ? 473 HIS A C     1 
ATOM   3521 O  O     . HIS A 1 507 ? -56.71800 10.15900  -41.26200 1.000 58.91846  ? 473 HIS A O     1 
ATOM   3522 C  CB    . HIS A 1 507 ? -55.66800 13.17500  -40.28600 1.000 55.27463  ? 473 HIS A CB    1 
ATOM   3523 C  CG    . HIS A 1 507 ? -56.16700 13.87400  -39.06200 1.000 56.76256  ? 473 HIS A CG    1 
ATOM   3524 N  ND1   . HIS A 1 507 ? -57.44700 13.70600  -38.57900 1.000 62.96508  ? 473 HIS A ND1   1 
ATOM   3525 C  CD2   . HIS A 1 507 ? -55.56000 14.74700  -38.22300 1.000 55.91365  ? 473 HIS A CD2   1 
ATOM   3526 C  CE1   . HIS A 1 507 ? -57.60500 14.44000  -37.49200 1.000 60.65127  ? 473 HIS A CE1   1 
ATOM   3527 N  NE2   . HIS A 1 507 ? -56.47600 15.08400  -37.25600 1.000 59.44006  ? 473 HIS A NE2   1 
ATOM   3528 N  N     . SER A 1 508 ? -54.89100 10.92700  -42.33200 1.000 50.21652  ? 474 SER A N     1 
ATOM   3529 C  CA    . SER A 1 508 ? -55.18100 10.14400  -43.52800 1.000 55.33956  ? 474 SER A CA    1 
ATOM   3530 C  C     . SER A 1 508 ? -54.99900 8.64900   -43.29700 1.000 58.90424  ? 474 SER A C     1 
ATOM   3531 O  O     . SER A 1 508 ? -55.58400 7.84500   -44.03100 1.000 63.32603  ? 474 SER A O     1 
ATOM   3532 C  CB    . SER A 1 508 ? -54.29200 10.59000  -44.69000 1.000 49.59531  ? 474 SER A CB    1 
ATOM   3533 O  OG    . SER A 1 508 ? -52.97700 10.08000  -44.55900 1.000 62.80575  ? 474 SER A OG    1 
ATOM   3534 N  N     . VAL A 1 509 ? -54.19400 8.26000   -42.30800 1.000 51.78424  ? 475 VAL A N     1 
ATOM   3535 C  CA    . VAL A 1 509 ? -54.02800 6.84400   -41.99800 1.000 58.81840  ? 475 VAL A CA    1 
ATOM   3536 C  C     . VAL A 1 509 ? -55.25400 6.30900   -41.26600 1.000 57.44164  ? 475 VAL A C     1 
ATOM   3537 O  O     . VAL A 1 509 ? -55.69600 5.18200   -41.51400 1.000 66.37092  ? 475 VAL A O     1 
ATOM   3538 C  CB    . VAL A 1 509 ? -52.73200 6.63400   -41.19100 1.000 62.07693  ? 475 VAL A CB    1 
ATOM   3539 C  CG1   . VAL A 1 509 ? -52.84200 5.41300   -40.29500 1.000 62.70018  ? 475 VAL A CG1   1 
ATOM   3540 C  CG2   . VAL A 1 509 ? -51.54200 6.50300   -42.13300 1.000 60.31408  ? 475 VAL A CG2   1 
ATOM   3541 N  N     . VAL A 1 510 ? -55.82700 7.10700   -40.37300 1.000 57.47613  ? 476 VAL A N     1 
ATOM   3542 C  CA    . VAL A 1 510 ? -57.03900 6.73100   -39.66100 1.000 60.37807  ? 476 VAL A CA    1 
ATOM   3543 C  C     . VAL A 1 510 ? -58.24600 6.81100   -40.59200 1.000 62.43150  ? 476 VAL A C     1 
ATOM   3544 O  O     . VAL A 1 510 ? -58.96800 5.83000   -40.77300 1.000 78.12135  ? 476 VAL A O     1 
ATOM   3545 C  CB    . VAL A 1 510 ? -57.24400 7.62000   -38.42000 1.000 55.06357  ? 476 VAL A CB    1 
ATOM   3546 C  CG1   . VAL A 1 510 ? -58.58600 7.32900   -37.76600 1.000 64.31129  ? 476 VAL A CG1   1 
ATOM   3547 C  CG2   . VAL A 1 510 ? -56.09900 7.42300   -37.43300 1.000 57.54825  ? 476 VAL A CG2   1 
HETATM 3548 CL CL    . CL  B 2 .   ? -35.55700 17.50100  -25.88400 1.000 29.68795  ? 501 CL  A CL    1 
HETATM 3549 S  S     . SO4 C 3 .   ? -58.75400 6.17600   -16.63400 1.000 114.50691 ? 502 SO4 A S     1 
HETATM 3550 O  O1    . SO4 C 3 .   ? -57.30500 6.13300   -16.45200 1.000 91.23452  ? 502 SO4 A O1    1 
HETATM 3551 O  O2    . SO4 C 3 .   ? -59.28800 7.33400   -15.91900 1.000 87.43327  ? 502 SO4 A O2    1 
HETATM 3552 O  O3    . SO4 C 3 .   ? -59.06700 6.28300   -18.05900 1.000 90.05300  ? 502 SO4 A O3    1 
HETATM 3553 O  O4    . SO4 C 3 .   ? -59.35100 4.95200   -16.10200 1.000 100.24354 ? 502 SO4 A O4    1 
HETATM 3554 S  S     . SO4 D 3 .   ? -15.21100 5.58000   -46.15600 1.000 94.59793  ? 503 SO4 A S     1 
HETATM 3555 O  O1    . SO4 D 3 .   ? -14.56200 6.51000   -47.07700 1.000 96.51388  ? 503 SO4 A O1    1 
HETATM 3556 O  O2    . SO4 D 3 .   ? -15.56000 6.28000   -44.92200 1.000 74.05657  ? 503 SO4 A O2    1 
HETATM 3557 O  O3    . SO4 D 3 .   ? -16.42000 5.04700   -46.78000 1.000 77.60363  ? 503 SO4 A O3    1 
HETATM 3558 O  O4    . SO4 D 3 .   ? -14.30100 4.47700   -45.84900 1.000 86.33847  ? 503 SO4 A O4    1 
HETATM 3559 S  S     . SO4 E 3 .   ? -59.27700 13.53600  -16.26600 1.000 122.83909 ? 504 SO4 A S     1 
HETATM 3560 O  O1    . SO4 E 3 .   ? -59.60000 14.59100  -15.30900 1.000 116.98094 ? 504 SO4 A O1    1 
HETATM 3561 O  O2    . SO4 E 3 .   ? -57.96400 12.98000  -15.94900 1.000 104.02288 ? 504 SO4 A O2    1 
HETATM 3562 O  O3    . SO4 E 3 .   ? -60.28600 12.48200  -16.19000 1.000 114.38713 ? 504 SO4 A O3    1 
HETATM 3563 O  O4    . SO4 E 3 .   ? -59.26100 14.09400  -17.61600 1.000 109.75022 ? 504 SO4 A O4    1 
HETATM 3564 CL CL    . CL  F 2 .   ? -15.13400 8.11600   -13.00700 1.000 51.69868  ? 505 CL  A CL    1 
HETATM 3565 CL CL    . CL  G 2 .   ? -38.79800 22.21500  -44.16000 1.000 63.59919  ? 506 CL  A CL    1 
HETATM 3566 S  S     . SO4 H 3 .   ? -42.22800 -0.39900  -37.88600 1.000 76.73590  ? 507 SO4 A S     1 
HETATM 3567 O  O1    . SO4 H 3 .   ? -41.26100 -1.00700  -38.80200 1.000 57.78932  ? 507 SO4 A O1    1 
HETATM 3568 O  O2    . SO4 H 3 .   ? -41.89400 1.00800   -37.66400 1.000 64.32594  ? 507 SO4 A O2    1 
HETATM 3569 O  O3    . SO4 H 3 .   ? -43.57000 -0.50000  -38.45400 1.000 68.84709  ? 507 SO4 A O3    1 
HETATM 3570 O  O4    . SO4 H 3 .   ? -42.18900 -1.10500  -36.60700 1.000 82.48775  ? 507 SO4 A O4    1 
HETATM 3571 N  N1    . UDP I 4 .   ? -29.95000 20.26100  -13.16800 1.000 66.90016  ? 508 UDP A N1    1 
HETATM 3572 C  C2    . UDP I 4 .   ? -30.01500 21.50200  -12.56700 1.000 67.59988  ? 508 UDP A C2    1 
HETATM 3573 N  N3    . UDP I 4 .   ? -29.11700 21.69100  -11.55300 1.000 66.96925  ? 508 UDP A N3    1 
HETATM 3574 C  C4    . UDP I 4 .   ? -28.17500 20.79800  -11.09100 1.000 69.26799  ? 508 UDP A C4    1 
HETATM 3575 C  C5    . UDP I 4 .   ? -28.16700 19.53600  -11.76800 1.000 72.60194  ? 508 UDP A C5    1 
HETATM 3576 C  C6    . UDP I 4 .   ? -29.03900 19.31600  -12.76200 1.000 68.79889  ? 508 UDP A C6    1 
HETATM 3577 O  O2    . UDP I 4 .   ? -30.81400 22.36500  -12.90200 1.000 55.64507  ? 508 UDP A O2    1 
HETATM 3578 O  O4    . UDP I 4 .   ? -27.43600 21.13300  -10.16800 1.000 64.99054  ? 508 UDP A O4    1 
HETATM 3579 C  "C1'" . UDP I 4 .   ? -30.89900 19.99700  -14.26000 1.000 65.91273  ? 508 UDP A "C1'" 1 
HETATM 3580 C  "C2'" . UDP I 4 .   ? -30.30300 20.28400  -15.63600 1.000 70.62922  ? 508 UDP A "C2'" 1 
HETATM 3581 O  "O2'" . UDP I 4 .   ? -30.61300 21.60300  -16.03000 1.000 65.35350  ? 508 UDP A "O2'" 1 
HETATM 3582 C  "C3'" . UDP I 4 .   ? -31.04400 19.25700  -16.49000 1.000 68.81949  ? 508 UDP A "C3'" 1 
HETATM 3583 C  "C4'" . UDP I 4 .   ? -31.12400 18.04800  -15.55000 1.000 72.21415  ? 508 UDP A "C4'" 1 
HETATM 3584 O  "O4'" . UDP I 4 .   ? -31.24600 18.62900  -14.22700 1.000 81.34589  ? 508 UDP A "O4'" 1 
HETATM 3585 O  "O3'" . UDP I 4 .   ? -32.33400 19.72900  -16.85800 1.000 65.72236  ? 508 UDP A "O3'" 1 
HETATM 3586 C  "C5'" . UDP I 4 .   ? -29.94600 17.10700  -15.59100 1.000 78.40197  ? 508 UDP A "C5'" 1 
HETATM 3587 O  "O5'" . UDP I 4 .   ? -29.93700 16.27300  -14.40500 1.000 92.51776  ? 508 UDP A "O5'" 1 
HETATM 3588 P  PA    . UDP I 4 .   ? -28.74000 15.21900  -14.25400 1.000 119.72424 ? 508 UDP A PA    1 
HETATM 3589 O  O1A   . UDP I 4 .   ? -27.48700 15.81100  -14.80700 1.000 103.33738 ? 508 UDP A O1A   1 
HETATM 3590 O  O2A   . UDP I 4 .   ? -28.71600 14.66900  -12.86600 1.000 81.24584  ? 508 UDP A O2A   1 
HETATM 3591 O  O3A   . UDP I 4 .   ? -29.21600 14.06200  -15.25100 1.000 117.79284 ? 508 UDP A O3A   1 
HETATM 3592 P  PB    . UDP I 4 .   ? -28.34800 12.99200  -16.08100 1.000 118.99866 ? 508 UDP A PB    1 
HETATM 3593 O  O1B   . UDP I 4 .   ? -28.01700 13.65900  -17.38600 1.000 103.51344 ? 508 UDP A O1B   1 
HETATM 3594 O  O2B   . UDP I 4 .   ? -27.12600 12.72100  -15.23600 1.000 102.09851 ? 508 UDP A O2B   1 
HETATM 3595 O  O3B   . UDP I 4 .   ? -29.22200 11.77700  -16.25500 1.000 102.47933 ? 508 UDP A O3B   1 
HETATM 3596 O  O     . HOH J 5 .   ? -25.86400 19.93200  -41.04200 1.000 40.24293  ? 601 HOH A O     1 
HETATM 3597 O  O     . HOH J 5 .   ? -8.96200  19.89600  -35.81700 1.000 47.26355  ? 602 HOH A O     1 
HETATM 3598 O  O     . HOH J 5 .   ? -22.97900 -5.29700  -19.71400 1.000 49.30231  ? 603 HOH A O     1 
HETATM 3599 O  O     . HOH J 5 .   ? -50.46500 -1.76100  -36.44000 1.000 54.66310  ? 604 HOH A O     1 
HETATM 3600 O  O     . HOH J 5 .   ? -21.28300 34.44000  -5.43000  1.000 47.38847  ? 605 HOH A O     1 
HETATM 3601 O  O     . HOH J 5 .   ? -10.20300 0.90100   -37.33000 1.000 39.55899  ? 606 HOH A O     1 
HETATM 3602 O  O     . HOH J 5 .   ? -13.50600 10.08600  -26.82500 1.000 42.23764  ? 607 HOH A O     1 
HETATM 3603 O  O     . HOH J 5 .   ? -16.89100 8.86800   -28.22700 1.000 35.71303  ? 608 HOH A O     1 
HETATM 3604 O  O     . HOH J 5 .   ? -16.30500 6.67700   -20.33600 1.000 29.64331  ? 609 HOH A O     1 
HETATM 3605 O  O     . HOH J 5 .   ? -30.53500 7.05800   -32.62000 1.000 29.05548  ? 610 HOH A O     1 
HETATM 3606 O  O     . HOH J 5 .   ? -43.60500 1.83200   -6.77700  1.000 46.95130  ? 611 HOH A O     1 
HETATM 3607 O  O     . HOH J 5 .   ? -29.56200 -3.25800  -5.07800  1.000 54.42543  ? 612 HOH A O     1 
HETATM 3608 O  O     . HOH J 5 .   ? -31.92600 15.53100  -41.33500 1.000 30.15456  ? 613 HOH A O     1 
HETATM 3609 O  O     . HOH J 5 .   ? -36.45400 19.31900  -38.01600 1.000 28.58494  ? 614 HOH A O     1 
HETATM 3610 O  O     . HOH J 5 .   ? -13.82500 12.34900  -24.42000 1.000 35.76436  ? 615 HOH A O     1 
HETATM 3611 O  O     . HOH J 5 .   ? -45.14700 1.69700   -38.06300 1.000 44.52108  ? 616 HOH A O     1 
HETATM 3612 O  O     . HOH J 5 .   ? -46.28500 22.94000  -36.42000 1.000 46.36252  ? 617 HOH A O     1 
HETATM 3613 O  O     . HOH J 5 .   ? -39.46400 19.82500  -42.04200 1.000 38.62581  ? 618 HOH A O     1 
HETATM 3614 O  O     . HOH J 5 .   ? -21.63500 2.10400   -42.66500 1.000 40.66870  ? 619 HOH A O     1 
HETATM 3615 O  O     . HOH J 5 .   ? -27.22200 0.99900   -27.49400 1.000 44.75471  ? 620 HOH A O     1 
HETATM 3616 O  O     . HOH J 5 .   ? -26.819   22.227    -44.172   1.000 45.92315  ? 621 HOH A O     1 
HETATM 3617 O  O     . HOH J 5 .   ? -25.42600 15.86300  -39.50500 1.000 26.08970  ? 622 HOH A O     1 
HETATM 3618 O  O     . HOH J 5 .   ? -15.37200 1.10300   -39.59300 1.000 45.89314  ? 623 HOH A O     1 
HETATM 3619 O  O     . HOH J 5 .   ? -52.21600 21.07600  -42.15500 1.000 60.33413  ? 624 HOH A O     1 
HETATM 3620 O  O     . HOH J 5 .   ? -46.87200 1.89000   -8.89200  1.000 43.55693  ? 625 HOH A O     1 
HETATM 3621 O  O     . HOH J 5 .   ? -29.94200 27.53300  -20.79600 1.000 44.52802  ? 626 HOH A O     1 
HETATM 3622 O  O     . HOH J 5 .   ? -39.21400 6.05600   -9.16500  1.000 47.76554  ? 627 HOH A O     1 
HETATM 3623 O  O     . HOH J 5 .   ? -23.83300 31.61200  -22.30200 1.000 30.40570  ? 628 HOH A O     1 
HETATM 3624 O  O     . HOH J 5 .   ? -33.37800 11.94000  -24.58700 1.000 32.55501  ? 629 HOH A O     1 
HETATM 3625 O  O     . HOH J 5 .   ? -49.36900 -5.71200  -16.79000 1.000 54.36991  ? 630 HOH A O     1 
HETATM 3626 O  O     . HOH J 5 .   ? -28.33100 39.93100  -13.42600 1.000 50.87176  ? 631 HOH A O     1 
HETATM 3627 O  O     . HOH J 5 .   ? -31.25600 -4.17500  -29.92100 1.000 51.70032  ? 632 HOH A O     1 
HETATM 3628 O  O     . HOH J 5 .   ? -34.58900 9.31300   -47.94100 1.000 47.70369  ? 633 HOH A O     1 
HETATM 3629 O  O     . HOH J 5 .   ? -37.44500 12.45700  -43.46300 1.000 43.73957  ? 634 HOH A O     1 
HETATM 3630 O  O     . HOH J 5 .   ? -13.49700 0.02300   -22.30100 1.000 38.38163  ? 635 HOH A O     1 
HETATM 3631 O  O     . HOH J 5 .   ? -48.34700 -4.78100  -12.53600 1.000 62.50236  ? 636 HOH A O     1 
HETATM 3632 O  O     . HOH J 5 .   ? -8.21100  9.48600   -22.07400 1.000 40.57623  ? 637 HOH A O     1 
HETATM 3633 O  O     . HOH J 5 .   ? -7.55900  16.23900  -24.68400 1.000 35.26627  ? 638 HOH A O     1 
HETATM 3634 O  O     . HOH J 5 .   ? -32.78500 14.36600  -48.10700 1.000 46.51529  ? 639 HOH A O     1 
HETATM 3635 O  O     . HOH J 5 .   ? -22.70100 23.47400  -28.35000 1.000 31.41708  ? 640 HOH A O     1 
HETATM 3636 O  O     . HOH J 5 .   ? -10.29500 26.48000  -37.18700 1.000 27.26029  ? 641 HOH A O     1 
HETATM 3637 O  O     . HOH J 5 .   ? -19.30200 17.51000  -11.63800 1.000 46.51221  ? 642 HOH A O     1 
HETATM 3638 O  O     . HOH J 5 .   ? -41.52900 2.57200   -45.35400 1.000 49.69059  ? 643 HOH A O     1 
HETATM 3639 O  O     . HOH J 5 .   ? -10.76400 31.71400  -18.58900 1.000 33.04341  ? 644 HOH A O     1 
HETATM 3640 O  O     . HOH J 5 .   ? -34.32000 4.98600   -4.84500  1.000 52.14523  ? 645 HOH A O     1 
HETATM 3641 O  O     . HOH J 5 .   ? -22.72500 25.19800  -36.42200 1.000 31.17764  ? 646 HOH A O     1 
HETATM 3642 O  O     . HOH J 5 .   ? -38.64200 22.70700  -21.90900 1.000 39.67329  ? 647 HOH A O     1 
HETATM 3643 O  O     . HOH J 5 .   ? -47.13500 -8.34400  -18.75000 1.000 54.65161  ? 648 HOH A O     1 
HETATM 3644 O  O     . HOH J 5 .   ? -14.08000 19.18400  -32.34700 1.000 36.68545  ? 649 HOH A O     1 
HETATM 3645 O  O     . HOH J 5 .   ? -44.77200 4.87100   -18.84100 1.000 37.61912  ? 650 HOH A O     1 
HETATM 3646 O  O     . HOH J 5 .   ? -40.23600 7.52200   -24.04200 1.000 38.52534  ? 651 HOH A O     1 
HETATM 3647 O  O     . HOH J 5 .   ? -39.91900 -1.77700  -35.11900 1.000 59.43365  ? 652 HOH A O     1 
HETATM 3648 O  O     . HOH J 5 .   ? -21.43700 18.84800  -40.31100 1.000 44.24869  ? 653 HOH A O     1 
HETATM 3649 O  O     . HOH J 5 .   ? -8.86000  -2.59000  -35.75500 1.000 55.50876  ? 654 HOH A O     1 
HETATM 3650 O  O     . HOH J 5 .   ? -14.69000 9.79200   -20.56700 1.000 34.82949  ? 655 HOH A O     1 
HETATM 3651 O  O     . HOH J 5 .   ? -32.87500 24.76300  -38.55900 1.000 35.76378  ? 656 HOH A O     1 
HETATM 3652 O  O     . HOH J 5 .   ? -17.98100 7.76800   -14.97200 1.000 48.93038  ? 657 HOH A O     1 
HETATM 3653 O  O     . HOH J 5 .   ? -6.04600  7.34500   -19.34800 1.000 47.60369  ? 658 HOH A O     1 
HETATM 3654 O  O     . HOH J 5 .   ? -17.74400 7.10900   -41.95800 1.000 30.29790  ? 659 HOH A O     1 
HETATM 3655 O  O     . HOH J 5 .   ? -41.86400 0.48500   -29.54600 1.000 54.06866  ? 660 HOH A O     1 
HETATM 3656 O  O     . HOH J 5 .   ? -35.49300 -7.58000  -4.89100  1.000 41.06758  ? 661 HOH A O     1 
HETATM 3657 O  O     . HOH J 5 .   ? -21.28000 23.32000  -37.36800 1.000 32.32837  ? 662 HOH A O     1 
HETATM 3658 O  O     . HOH J 5 .   ? -13.51400 7.30500   -20.27000 1.000 37.33575  ? 663 HOH A O     1 
HETATM 3659 O  O     . HOH J 5 .   ? -17.88900 10.97700  -17.77600 1.000 45.93874  ? 664 HOH A O     1 
HETATM 3660 O  O     . HOH J 5 .   ? -45.10600 25.37800  -39.13400 1.000 57.00708  ? 665 HOH A O     1 
HETATM 3661 O  O     . HOH J 5 .   ? -6.19600  9.77900   -20.04300 1.000 45.04673  ? 666 HOH A O     1 
HETATM 3662 O  O     . HOH J 5 .   ? -27.54200 3.62500   -45.57000 1.000 39.40244  ? 667 HOH A O     1 
HETATM 3663 O  O     . HOH J 5 .   ? -48.58100 14.75000  -44.33100 1.000 47.96943  ? 668 HOH A O     1 
HETATM 3664 O  O     . HOH J 5 .   ? -54.98700 13.07800  -16.42000 1.000 53.79343  ? 669 HOH A O     1 
HETATM 3665 O  O     . HOH J 5 .   ? -20.44100 31.04100  -40.75900 1.000 41.13620  ? 670 HOH A O     1 
HETATM 3666 O  O     . HOH J 5 .   ? -41.82400 4.29700   -43.34600 1.000 40.29543  ? 671 HOH A O     1 
HETATM 3667 O  O     . HOH J 5 .   ? -28.11600 14.77000  -19.97900 1.000 35.30698  ? 672 HOH A O     1 
HETATM 3668 O  O     . HOH J 5 .   ? -6.42400  4.80100   -28.74700 1.000 49.19448  ? 673 HOH A O     1 
HETATM 3669 O  O     . HOH J 5 .   ? -7.40000  3.65600   -21.64400 1.000 54.09598  ? 674 HOH A O     1 
HETATM 3670 O  O     . HOH J 5 .   ? -22.65400 21.73000  -38.61200 1.000 33.50763  ? 675 HOH A O     1 
HETATM 3671 O  O     . HOH J 5 .   ? -24.364   39.865    -9.094    1.000 47.46012  ? 676 HOH A O     1 
HETATM 3672 O  O     . HOH J 5 .   ? -31.88000 -7.11500  -13.13600 1.000 43.44183  ? 677 HOH A O     1 
HETATM 3673 O  O     . HOH J 5 .   ? -24.20500 -2.19200  -10.02000 1.000 43.60951  ? 678 HOH A O     1 
HETATM 3674 O  O     . HOH J 5 .   ? -28.95600 3.36600   -28.51000 1.000 51.31128  ? 679 HOH A O     1 
HETATM 3675 O  O     . HOH J 5 .   ? -31.72100 5.71200   -29.98300 1.000 44.13266  ? 680 HOH A O     1 
HETATM 3676 O  O     . HOH J 5 .   ? -7.70500  27.21200  -13.59500 1.000 43.21608  ? 681 HOH A O     1 
HETATM 3677 O  O     . HOH J 5 .   ? -24.45200 24.60000  -30.20800 1.000 37.90710  ? 682 HOH A O     1 
HETATM 3678 O  O     . HOH J 5 .   ? -22.25000 -0.85000  -43.72400 1.000 53.31998  ? 683 HOH A O     1 
HETATM 3679 O  O     . HOH J 5 .   ? -13.18400 -1.28800  -24.61800 1.000 49.92157  ? 684 HOH A O     1 
HETATM 3680 O  O     . HOH J 5 .   ? -44.91900 24.71600  -30.18600 1.000 44.42665  ? 685 HOH A O     1 
HETATM 3681 O  O     . HOH J 5 .   ? -15.52900 14.41900  -39.26600 1.000 42.75802  ? 686 HOH A O     1 
HETATM 3682 O  O     . HOH J 5 .   ? -38.87600 20.18200  -21.04500 1.000 50.53416  ? 687 HOH A O     1 
HETATM 3683 O  O     . HOH J 5 .   ? -13.98400 17.72000  -36.17600 1.000 43.04084  ? 688 HOH A O     1 
HETATM 3684 O  O     . HOH J 5 .   ? -56.76000 3.63400   -36.41000 1.000 53.69105  ? 689 HOH A O     1 
HETATM 3685 O  O     . HOH J 5 .   ? -13.18600 37.25000  -16.15400 1.000 44.99089  ? 690 HOH A O     1 
HETATM 3686 O  O     . HOH J 5 .   ? -17.72800 23.90500  -42.72400 1.000 31.16733  ? 691 HOH A O     1 
HETATM 3687 O  O     . HOH J 5 .   ? -37.75700 17.05600  -23.78200 1.000 34.78277  ? 692 HOH A O     1 
HETATM 3688 O  O     . HOH J 5 .   ? -22.65100 3.46400   -46.63000 1.000 45.31418  ? 693 HOH A O     1 
HETATM 3689 O  O     . HOH J 5 .   ? -2.51800  18.62600  -15.97200 1.000 54.80047  ? 694 HOH A O     1 
HETATM 3690 O  O     . HOH J 5 .   ? -35.67600 25.05700  -39.71000 1.000 38.36904  ? 695 HOH A O     1 
HETATM 3691 O  O     . HOH J 5 .   ? -13.26600 7.09400   -40.87500 1.000 53.21172  ? 696 HOH A O     1 
HETATM 3692 O  O     . HOH J 5 .   ? -21.17900 15.61800  -9.84300  1.000 50.99445  ? 697 HOH A O     1 
HETATM 3693 O  O     . HOH J 5 .   ? -23.16600 6.37700   -10.45400 1.000 55.03308  ? 698 HOH A O     1 
HETATM 3694 O  O     . HOH J 5 .   ? -20.58800 30.51300  -24.90200 1.000 43.95142  ? 699 HOH A O     1 
HETATM 3695 O  O     . HOH J 5 .   ? -38.38800 29.32000  -38.38100 1.000 45.83829  ? 700 HOH A O     1 
HETATM 3696 O  O     . HOH J 5 .   ? -19.34900 -1.98300  -19.87700 1.000 54.46132  ? 701 HOH A O     1 
HETATM 3697 O  O     . HOH J 5 .   ? -50.62500 -5.34700  -12.73800 1.000 56.00911  ? 702 HOH A O     1 
HETATM 3698 O  O     . HOH J 5 .   ? -27.54600 31.85800  -24.53700 1.000 44.01615  ? 703 HOH A O     1 
HETATM 3699 O  O     . HOH J 5 .   ? -28.15900 34.26000  -17.06700 1.000 42.87803  ? 704 HOH A O     1 
HETATM 3700 O  O     . HOH J 5 .   ? -11.37200 19.94000  -32.73400 1.000 53.47362  ? 705 HOH A O     1 
HETATM 3701 O  O     . HOH J 5 .   ? -31.38100 4.92700   -22.62000 1.000 53.20779  ? 706 HOH A O     1 
HETATM 3702 O  O     . HOH J 5 .   ? -22.94800 2.30400   -25.71100 1.000 49.41396  ? 707 HOH A O     1 
HETATM 3703 O  O     . HOH J 5 .   ? -16.99100 18.28100  -39.30400 1.000 33.26082  ? 708 HOH A O     1 
HETATM 3704 O  O     . HOH J 5 .   ? -17.57400 14.57800  -44.77300 1.000 41.37581  ? 709 HOH A O     1 
HETATM 3705 O  O     . HOH J 5 .   ? -12.34600 17.45600  -30.73400 1.000 40.16089  ? 710 HOH A O     1 
HETATM 3706 O  O     . HOH J 5 .   ? -26.58900 30.61200  -3.21100  1.000 60.21897  ? 711 HOH A O     1 
HETATM 3707 O  O     . HOH J 5 .   ? -25.86100 2.56400   -25.80400 1.000 40.89494  ? 712 HOH A O     1 
HETATM 3708 O  O     . HOH J 5 .   ? -8.51200  8.95200   -25.67400 1.000 59.15110  ? 713 HOH A O     1 
HETATM 3709 O  O     . HOH J 5 .   ? -57.89500 17.78400  -36.05200 1.000 58.59316  ? 714 HOH A O     1 
HETATM 3710 O  O     . HOH J 5 .   ? -22.71100 7.59200   -46.29600 1.000 42.25808  ? 715 HOH A O     1 
HETATM 3711 O  O     . HOH J 5 .   ? -25.95700 18.28000  -17.29800 1.000 39.05814  ? 716 HOH A O     1 
HETATM 3712 O  O     . HOH J 5 .   ? -48.58000 -0.10500  -37.47700 1.000 51.99679  ? 717 HOH A O     1 
HETATM 3713 O  O     . HOH J 5 .   ? -13.27800 11.56900  -21.85400 1.000 33.13852  ? 718 HOH A O     1 
HETATM 3714 O  O     . HOH J 5 .   ? -14.63900 6.88400   -5.71900  1.000 53.11397  ? 719 HOH A O     1 
HETATM 3715 O  O     . HOH J 5 .   ? -28.28700 10.32800  -23.91400 1.000 40.69181  ? 720 HOH A O     1 
HETATM 3716 O  O     . HOH J 5 .   ? -9.29200  13.80600  -28.04100 1.000 54.30495  ? 721 HOH A O     1 
HETATM 3717 O  O     . HOH J 5 .   ? -37.39900 15.04700  -41.04900 1.000 46.33421  ? 722 HOH A O     1 
HETATM 3718 O  O     . HOH J 5 .   ? -9.73800  -0.32300  -27.16500 1.000 44.81567  ? 723 HOH A O     1 
HETATM 3719 O  O     . HOH J 5 .   ? -33.80900 16.61800  -23.49800 1.000 30.90908  ? 724 HOH A O     1 
HETATM 3720 O  O     . HOH J 5 .   ? -20.837   17.853    -44.104   1.000 39.18447  ? 725 HOH A O     1 
HETATM 3721 O  O     . HOH J 5 .   ? -25.68500 -4.74400  -9.48700  1.000 42.69021  ? 726 HOH A O     1 
HETATM 3722 O  O     . HOH J 5 .   ? -34.94800 14.92500  -19.89000 1.000 51.53491  ? 727 HOH A O     1 
HETATM 3723 O  O     . HOH J 5 .   ? -30.54400 12.59700  -21.38600 1.000 39.94035  ? 728 HOH A O     1 
HETATM 3724 O  O     . HOH J 5 .   ? -37.83600 17.80600  -39.98500 1.000 41.70946  ? 729 HOH A O     1 
HETATM 3725 O  O     . HOH J 5 .   ? -27.24200 9.52000   -21.48600 1.000 47.11670  ? 730 HOH A O     1 
HETATM 3726 O  O     . HOH J 5 .   ? -19.27900 9.55900   -15.96300 1.000 49.67670  ? 731 HOH A O     1 
HETATM 3727 O  O     . HOH J 5 .   ? -15.57400 9.40600   -17.75200 1.000 47.01159  ? 732 HOH A O     1 
HETATM 3728 O  O     . HOH J 5 .   ? -35.90300 16.90300  -21.61900 1.000 41.82661  ? 733 HOH A O     1 
HETATM 3729 O  O     . HOH J 5 .   ? -12.54900 6.72500   -17.66900 1.000 38.40435  ? 734 HOH A O     1 
HETATM 3730 O  O     . HOH J 5 .   ? -26.87700 5.75800   -47.35000 1.000 46.36629  ? 735 HOH A O     1 
HETATM 3731 O  O     . HOH J 5 .   ? -25.46200 1.56100   -45.51900 1.000 53.85254  ? 736 HOH A O     1 
HETATM 3732 O  O     . HOH J 5 .   ? -51.291   13.673    -45.299   1.000 53.95422  ? 737 HOH A O     1 
HETATM 3733 O  O     . HOH J 5 .   ? -55.19100 18.53900  -37.68900 1.000 62.66489  ? 738 HOH A O     1 
HETATM 3734 O  O     . HOH J 5 .   ? -18.83300 14.85600  -10.30200 1.000 36.71317  ? 739 HOH A O     1 
HETATM 3735 O  O     . HOH J 5 .   ? -36.22200 19.00200  -20.51400 1.000 43.76084  ? 740 HOH A O     1 
HETATM 3736 O  O     . HOH J 5 .   ? -10.98300 13.49400  -37.20900 1.000 58.59290  ? 741 HOH A O     1 
HETATM 3737 O  O     . HOH J 5 .   ? -33.26300 14.09900  -22.83400 1.000 34.80423  ? 742 HOH A O     1 
HETATM 3738 O  O     . HOH J 5 .   ? -13.11400 14.16800  -37.69300 1.000 52.18574  ? 743 HOH A O     1 
HETATM 3739 O  O     . HOH J 5 .   ? -3.67800  9.75100   -21.48000 1.000 60.11879  ? 744 HOH A O     1 
HETATM 3740 O  O     . HOH J 5 .   ? -20.99800 7.52600   -15.62600 1.000 46.06814  ? 745 HOH A O     1 
HETATM 3741 O  O     . HOH J 5 .   ? -29.97100 4.42200   -30.44700 1.000 51.52512  ? 746 HOH A O     1 
HETATM 3742 O  O     . HOH J 5 .   ? -14.79400 7.16200   -27.44900 1.000 46.68882  ? 747 HOH A O     1 
HETATM 3743 O  O     . HOH J 5 .   ? -25.306   7.959     -46.559   1.000 40.39466  ? 748 HOH A O     1 
HETATM 3744 O  O     . HOH J 5 .   ? -10.57700 -1.95700  -25.05100 1.000 58.33666  ? 749 HOH A O     1 
HETATM 3745 O  O     . HOH J 5 .   ? -28.32400 35.37700  -14.57400 1.000 44.62197  ? 750 HOH A O     1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . PRO A 41  ? 0.48260 0.79845 0.85404 0.02231  -0.12407 0.19294  7   PRO A N   
2    C CA  . PRO A 41  ? 0.58664 0.89176 0.94692 0.02586  -0.11072 0.18865  7   PRO A CA  
3    C C   . PRO A 41  ? 0.51318 0.81674 0.86993 0.00975  -0.10803 0.18514  7   PRO A C   
4    O O   . PRO A 41  ? 0.52292 0.85024 0.90613 0.00200  -0.11002 0.19137  7   PRO A O   
5    C CB  . PRO A 41  ? 0.59167 0.91049 0.96960 0.04243  -0.09388 0.19082  7   PRO A CB  
6    C CG  . PRO A 41  ? 0.54580 0.87607 0.93815 0.05056  -0.09947 0.19523  7   PRO A CG  
7    C CD  . PRO A 41  ? 0.61405 0.95108 1.01125 0.03506  -0.11684 0.19796  7   PRO A CD  
8    N N   . LEU A 42  ? 0.48462 0.76032 0.80964 0.00476  -0.10338 0.17542  8   LEU A N   
9    C CA  . LEU A 42  ? 0.55497 0.82481 0.87303 -0.00990 -0.10136 0.17156  8   LEU A CA  
10   C C   . LEU A 42  ? 0.41157 0.68531 0.73473 -0.00438 -0.08304 0.17051  8   LEU A C   
11   O O   . LEU A 42  ? 0.42960 0.69992 0.74872 0.01022  -0.07138 0.16873  8   LEU A O   
12   C CB  . LEU A 42  ? 0.46426 0.70269 0.74604 -0.01813 -0.10617 0.16190  8   LEU A CB  
13   C CG  . LEU A 42  ? 0.59743 0.82890 0.86908 -0.02715 -0.12443 0.16231  8   LEU A CG  
14   C CD1 . LEU A 42  ? 0.48458 0.68552 0.72050 -0.03539 -0.12602 0.15244  8   LEU A CD1 
15   C CD2 . LEU A 42  ? 0.49689 0.74939 0.79185 -0.03976 -0.13646 0.16906  8   LEU A CD2 
16   N N   . LYS A 43  ? 0.47520 0.75499 0.80619 -0.01646 -0.08089 0.17176  9   LYS A N   
17   C CA  . LYS A 43  ? 0.43074 0.71025 0.76162 -0.01394 -0.06441 0.17068  9   LYS A CA  
18   C C   . LYS A 43  ? 0.37475 0.62430 0.67249 -0.02019 -0.06259 0.16071  9   LYS A C   
19   O O   . LYS A 43  ? 0.45490 0.69599 0.74564 -0.03482 -0.07004 0.15870  9   LYS A O   
20   C CB  . LYS A 43  ? 0.46063 0.76388 0.82023 -0.02357 -0.06257 0.17893  9   LYS A CB  
21   C CG  . LYS A 43  ? 0.47774 0.79030 0.84660 -0.01621 -0.04384 0.18193  9   LYS A CG  
22   C CD  . LYS A 43  ? 0.64743 0.98586 1.04280 -0.00139 -0.03639 0.18938  9   LYS A CD  
23   C CE  . LYS A 43  ? 0.82156 1.16432 1.21859 0.00837  -0.01608 0.19081  9   LYS A CE  
24   N NZ  . LYS A 43  ? 0.64193 0.98436 1.03511 0.02861  -0.00705 0.18910  9   LYS A NZ  
25   N N   . ILE A 44  ? 0.37885 0.61221 0.65644 -0.00902 -0.05311 0.15429  10  ILE A N   
26   C CA  . ILE A 44  ? 0.37849 0.58442 0.62536 -0.01281 -0.05200 0.14461  10  ILE A CA  
27   C C   . ILE A 44  ? 0.37695 0.57845 0.61738 -0.00677 -0.03682 0.14241  10  ILE A C   
28   O O   . ILE A 44  ? 0.37648 0.58144 0.61790 0.00677  -0.02725 0.14246  10  ILE A O   
29   C CB  . ILE A 44  ? 0.38846 0.57702 0.61471 -0.00654 -0.05664 0.13834  10  ILE A CB  
30   C CG1 . ILE A 44  ? 0.38773 0.58038 0.61896 -0.01202 -0.07195 0.14161  10  ILE A CG1 
31   C CG2 . ILE A 44  ? 0.38224 0.54514 0.57961 -0.01088 -0.05506 0.12866  10  ILE A CG2 
32   C CD1 . ILE A 44  ? 0.35871 0.53475 0.57069 -0.00602 -0.07645 0.13713  10  ILE A CD1 
33   N N   . TYR A 45  ? 0.34169 0.53441 0.57439 -0.01651 -0.03488 0.14055  11  TYR A N   
34   C CA  . TYR A 45  ? 0.42861 0.61369 0.65108 -0.01185 -0.02203 0.13829  11  TYR A CA  
35   C C   . TYR A 45  ? 0.43148 0.59105 0.62482 -0.01109 -0.02260 0.12814  11  TYR A C   
36   O O   . TYR A 45  ? 0.40213 0.54868 0.58396 -0.02055 -0.03132 0.12379  11  TYR A O   
37   C CB  . TYR A 45  ? 0.37672 0.56700 0.60886 -0.02230 -0.01871 0.14339  11  TYR A CB  
38   C CG  . TYR A 45  ? 0.39026 0.60761 0.65311 -0.02331 -0.01500 0.15412  11  TYR A CG  
39   C CD1 . TYR A 45  ? 0.43301 0.66984 0.71421 -0.01343 -0.01401 0.15875  11  TYR A CD1 
40   C CD2 . TYR A 45  ? 0.41756 0.64101 0.69198 -0.03419 -0.01217 0.15992  11  TYR A CD2 
41   C CE1 . TYR A 45  ? 0.44465 0.70867 0.75654 -0.01400 -0.00997 0.16891  11  TYR A CE1 
42   C CE2 . TYR A 45  ? 0.47097 0.72089 0.77565 -0.03618 -0.00831 0.17021  11  TYR A CE2 
43   C CZ  . TYR A 45  ? 0.47658 0.74794 0.80077 -0.02586 -0.00702 0.17471  11  TYR A CZ  
44   O OH  . TYR A 45  ? 0.57609 0.87622 0.93294 -0.02740 -0.00243 0.18532  11  TYR A OH  
45   N N   . MET A 46  ? 0.37340 0.52635 0.55506 0.00013  -0.01310 0.12436  12  MET A N   
46   C CA  . MET A 46  ? 0.38745 0.51942 0.54438 0.00270  -0.01307 0.11497  12  MET A CA  
47   C C   . MET A 46  ? 0.44615 0.57143 0.59317 0.00588  -0.00339 0.11350  12  MET A C   
48   O O   . MET A 46  ? 0.35457 0.48813 0.50632 0.01454  0.00602  0.11686  12  MET A O   
49   C CB  . MET A 46  ? 0.38027 0.50914 0.53110 0.01341  -0.01310 0.11111  12  MET A CB  
50   C CG  . MET A 46  ? 0.45626 0.58624 0.61110 0.00983  -0.02395 0.11177  12  MET A CG  
51   S SD  . MET A 46  ? 0.42831 0.54402 0.56690 0.01858  -0.02543 0.10481  12  MET A SD  
52   C CE  . MET A 46  ? 0.37760 0.50186 0.52865 0.01665  -0.03649 0.11054  12  MET A CE  
53   N N   . LEU A 47  ? 0.35490 0.46488 0.48752 -0.00057 -0.00557 0.10874  13  LEU A N   
54   C CA  . LEU A 47  ? 0.41643 0.51902 0.53969 0.00114  0.00196  0.10833  13  LEU A CA  
55   C C   . LEU A 47  ? 0.38812 0.47468 0.49059 0.00655  0.00222  0.09937  13  LEU A C   
56   O O   . LEU A 47  ? 0.37014 0.44417 0.46257 0.00057  -0.00292 0.09423  13  LEU A O   
57   C CB  . LEU A 47  ? 0.38741 0.48578 0.51342 -0.01087 -0.00039 0.11139  13  LEU A CB  
58   C CG  . LEU A 47  ? 0.44182 0.52959 0.55697 -0.01000 0.00630  0.11158  13  LEU A CG  
59   C CD1 . LEU A 47  ? 0.39670 0.49401 0.51555 -0.00087 0.01731  0.11722  13  LEU A CD1 
60   C CD2 . LEU A 47  ? 0.38197 0.46398 0.50072 -0.02272 0.00323  0.11481  13  LEU A CD2 
61   N N   . PRO A 48  ? 0.41935 0.50587 0.51497 0.01765  0.00806  0.09707  14  PRO A N   
62   C CA  . PRO A 48  ? 0.36249 0.43555 0.44014 0.02231  0.00763  0.08874  14  PRO A CA  
63   C C   . PRO A 48  ? 0.46882 0.53409 0.53643 0.02319  0.01182  0.08861  14  PRO A C   
64   O O   . PRO A 48  ? 0.41743 0.48730 0.48915 0.02361  0.01781  0.09520  14  PRO A O   
65   C CB  . PRO A 48  ? 0.31830 0.39470 0.39325 0.03348  0.01148  0.08675  14  PRO A CB  
66   C CG  . PRO A 48  ? 0.42149 0.51190 0.50949 0.03703  0.01850  0.09508  14  PRO A CG  
67   C CD  . PRO A 48  ? 0.39103 0.49028 0.49553 0.02659  0.01487  0.10165  14  PRO A CD  
68   N N   . PHE A 49  ? 0.42428 0.47780 0.47896 0.02365  0.00870  0.08141  15  PHE A N   
69   C CA  . PHE A 49  ? 0.43577 0.48141 0.47970 0.02675  0.01182  0.08071  15  PHE A CA  
70   C C   . PHE A 49  ? 0.41870 0.46524 0.45353 0.03785  0.01631  0.07905  15  PHE A C   
71   O O   . PHE A 49  ? 0.36630 0.41557 0.40010 0.04280  0.01567  0.07537  15  PHE A O   
72   C CB  . PHE A 49  ? 0.36735 0.40166 0.40302 0.02338  0.00679  0.07398  15  PHE A CB  
73   C CG  . PHE A 49  ? 0.43940 0.46582 0.46445 0.02809  0.00900  0.07303  15  PHE A CG  
74   C CD1 . PHE A 49  ? 0.44363 0.46654 0.46841 0.02632  0.01268  0.07945  15  PHE A CD1 
75   C CD2 . PHE A 49  ? 0.45361 0.47623 0.46946 0.03415  0.00698  0.06619  15  PHE A CD2 
76   C CE1 . PHE A 49  ? 0.48565 0.50030 0.49985 0.03148  0.01428  0.07935  15  PHE A CE1 
77   C CE2 . PHE A 49  ? 0.45224 0.46869 0.45908 0.03918  0.00792  0.06581  15  PHE A CE2 
78   C CZ  . PHE A 49  ? 0.43439 0.44632 0.43975 0.03834  0.01155  0.07254  15  PHE A CZ  
79   N N   . PHE A 50  ? 0.39175 0.43429 0.41836 0.04171  0.02065  0.08185  16  PHE A N   
80   C CA  . PHE A 50  ? 0.48236 0.52483 0.49776 0.05207  0.02528  0.08138  16  PHE A CA  
81   C C   . PHE A 50  ? 0.50755 0.54250 0.51017 0.05688  0.02013  0.07248  16  PHE A C   
82   O O   . PHE A 50  ? 0.54205 0.57123 0.53303 0.06163  0.02033  0.07186  16  PHE A O   
83   C CB  . PHE A 50  ? 0.46677 0.50748 0.47725 0.05397  0.03189  0.08902  16  PHE A CB  
84   C CG  . PHE A 50  ? 0.51140 0.55610 0.53519 0.04519  0.03467  0.09729  16  PHE A CG  
85   C CD1 . PHE A 50  ? 0.46386 0.52138 0.50268 0.04282  0.03844  0.10266  16  PHE A CD1 
86   C CD2 . PHE A 50  ? 0.42286 0.45841 0.44471 0.03938  0.03333  0.09979  16  PHE A CD2 
87   C CE1 . PHE A 50  ? 0.45178 0.51433 0.50457 0.03362  0.04011  0.11035  16  PHE A CE1 
88   C CE2 . PHE A 50  ? 0.44964 0.48743 0.48337 0.03009  0.03527  0.10707  16  PHE A CE2 
89   C CZ  . PHE A 50  ? 0.41210 0.46412 0.46183 0.02665  0.03835  0.11238  16  PHE A CZ  
90   N N   . ALA A 51  ? 0.44892 0.48435 0.45432 0.05544  0.01517  0.06596  17  ALA A N   
91   C CA  . ALA A 51  ? 0.45352 0.48375 0.44976 0.05874  0.01011  0.05742  17  ALA A CA  
92   C C   . ALA A 51  ? 0.42550 0.45736 0.42453 0.05907  0.00797  0.05279  17  ALA A C   
93   O O   . ALA A 51  ? 0.40267 0.43811 0.41207 0.05405  0.00750  0.05495  17  ALA A O   
94   C CB  . ALA A 51  ? 0.39260 0.41818 0.38989 0.05342  0.00509  0.05385  17  ALA A CB  
95   N N   . GLN A 52  ? 0.39427 0.42251 0.38332 0.06489  0.00613  0.04657  18  GLN A N   
96   C CA  . GLN A 52  ? 0.52613 0.55335 0.51554 0.06657  0.00513  0.04260  18  GLN A CA  
97   C C   . GLN A 52  ? 0.45853 0.48485 0.45643 0.05866  0.00024  0.03986  18  GLN A C   
98   O O   . GLN A 52  ? 0.49354 0.52080 0.49710 0.05784  0.00046  0.04100  18  GLN A O   
99   C CB  . GLN A 52  ? 0.53351 0.55460 0.50904 0.07291  0.00287  0.03541  18  GLN A CB  
100  C CG  . GLN A 52  ? 0.81978 0.84006 0.78297 0.08158  0.00782  0.03780  18  GLN A CG  
101  C CD  . GLN A 52  ? 0.98694 1.01041 0.95157 0.08697  0.01579  0.04270  18  GLN A CD  
102  O OE1 . GLN A 52  ? 0.84746 0.87851 0.82466 0.08416  0.02021  0.05018  18  GLN A OE1 
103  N NE2 . GLN A 52  ? 1.01521 1.03303 0.96716 0.09486  0.01765  0.03832  18  GLN A NE2 
104  N N   . GLY A 53  ? 0.32808 0.35240 0.32651 0.05334  -0.00389 0.03654  19  GLY A N   
105  C CA  . GLY A 53  ? 0.39783 0.42069 0.40240 0.04565  -0.00746 0.03425  19  GLY A CA  
106  C C   . GLY A 53  ? 0.47264 0.49851 0.48599 0.03983  -0.00655 0.04029  19  GLY A C   
107  O O   . GLY A 53  ? 0.42611 0.45021 0.44290 0.03396  -0.00935 0.03934  19  GLY A O   
108  N N   . HIS A 54  ? 0.42366 0.45366 0.44016 0.04077  -0.00300 0.04665  20  HIS A N   
109  C CA  . HIS A 54  ? 0.42129 0.45524 0.44720 0.03482  -0.00284 0.05276  20  HIS A CA  
110  C C   . HIS A 54  ? 0.43640 0.47773 0.46946 0.03850  0.00008  0.05820  20  HIS A C   
111  O O   . HIS A 54  ? 0.42168 0.46672 0.46334 0.03421  -0.00229 0.06137  20  HIS A O   
112  C CB  . HIS A 54  ? 0.36439 0.39802 0.39125 0.03184  -0.00094 0.05682  20  HIS A CB  
113  C CG  . HIS A 54  ? 0.44357 0.47004 0.46544 0.02820  -0.00350 0.05222  20  HIS A CG  
114  N ND1 . HIS A 54  ? 0.39969 0.42240 0.42397 0.02036  -0.00525 0.05326  20  HIS A ND1 
115  C CD2 . HIS A 54  ? 0.35813 0.38085 0.37316 0.03169  -0.00454 0.04648  20  HIS A CD2 
116  C CE1 . HIS A 54  ? 0.42129 0.43778 0.44013 0.01999  -0.00620 0.04829  20  HIS A CE1 
117  N NE2 . HIS A 54  ? 0.37072 0.38836 0.38529 0.02677  -0.00596 0.04442  20  HIS A NE2 
118  N N   . LEU A 55  ? 0.34444 0.38796 0.37354 0.04695  0.00513  0.05921  21  LEU A N   
119  C CA  . LEU A 55  ? 0.44932 0.50134 0.48611 0.05174  0.01009  0.06515  21  LEU A CA  
120  C C   . LEU A 55  ? 0.37909 0.43072 0.41832 0.05492  0.00821  0.06297  21  LEU A C   
121  O O   . LEU A 55  ? 0.37114 0.43033 0.42257 0.05376  0.00793  0.06815  21  LEU A O   
122  C CB  . LEU A 55  ? 0.35598 0.40859 0.38451 0.06046  0.01709  0.06637  21  LEU A CB  
123  C CG  . LEU A 55  ? 0.46998 0.53096 0.50409 0.06792  0.02442  0.07148  21  LEU A CG  
124  C CD1 . LEU A 55  ? 0.40779 0.48116 0.45955 0.06265  0.02693  0.08077  21  LEU A CD1 
125  C CD2 . LEU A 55  ? 0.49327 0.55159 0.51376 0.07696  0.03140  0.07117  21  LEU A CD2 
126  N N   . ILE A 56  ? 0.38523 0.42787 0.41331 0.05897  0.00651  0.05558  22  ILE A N   
127  C CA  . ILE A 56  ? 0.40570 0.44488 0.43375 0.06324  0.00554  0.05333  22  ILE A CA  
128  C C   . ILE A 56  ? 0.41974 0.45774 0.45478 0.05570  -0.00064 0.05415  22  ILE A C   
129  O O   . ILE A 56  ? 0.41564 0.45633 0.45789 0.05831  -0.00097 0.05756  22  ILE A O   
130  C CB  . ILE A 56  ? 0.38715 0.41510 0.40040 0.06818  0.00469  0.04476  22  ILE A CB  
131  C CG1 . ILE A 56  ? 0.43615 0.46465 0.43996 0.07620  0.01046  0.04436  22  ILE A CG1 
132  C CG2 . ILE A 56  ? 0.37394 0.39519 0.38606 0.07232  0.00371  0.04229  22  ILE A CG2 
133  C CD1 . ILE A 56  ? 0.49013 0.52510 0.49808 0.08476  0.01830  0.04981  22  ILE A CD1 
134  N N   . PRO A 57  ? 0.44108 0.47490 0.47376 0.04701  -0.00538 0.05142  23  PRO A N   
135  C CA  . PRO A 57  ? 0.38837 0.42094 0.42594 0.03981  -0.01066 0.05320  23  PRO A CA  
136  C C   . PRO A 57  ? 0.39217 0.43522 0.44264 0.03745  -0.01131 0.06144  23  PRO A C   
137  O O   . PRO A 57  ? 0.38610 0.42999 0.44175 0.03643  -0.01505 0.06443  23  PRO A O   
138  C CB  . PRO A 57  ? 0.35226 0.37946 0.38408 0.03176  -0.01351 0.04890  23  PRO A CB  
139  C CG  . PRO A 57  ? 0.44098 0.46414 0.46432 0.03611  -0.01144 0.04274  23  PRO A CG  
140  C CD  . PRO A 57  ? 0.39332 0.42201 0.41740 0.04433  -0.00639 0.04579  23  PRO A CD  
141  N N   . LEU A 58  ? 0.35074 0.40182 0.40693 0.03631  -0.00822 0.06563  24  LEU A N   
142  C CA  . LEU A 58  ? 0.33691 0.39931 0.40744 0.03284  -0.00941 0.07360  24  LEU A CA  
143  C C   . LEU A 58  ? 0.34674 0.41902 0.42766 0.04166  -0.00555 0.07854  24  LEU A C   
144  O O   . LEU A 58  ? 0.37018 0.45119 0.46385 0.04024  -0.00890 0.08426  24  LEU A O   
145  C CB  . LEU A 58  ? 0.29564 0.36253 0.36964 0.02796  -0.00702 0.07691  24  LEU A CB  
146  C CG  . LEU A 58  ? 0.36328 0.44112 0.45256 0.02122  -0.01010 0.08457  24  LEU A CG  
147  C CD1 . LEU A 58  ? 0.45040 0.52494 0.53984 0.01462  -0.01893 0.08396  24  LEU A CD1 
148  C CD2 . LEU A 58  ? 0.44452 0.52203 0.53463 0.01399  -0.00908 0.08669  24  LEU A CD2 
149  N N   . VAL A 59  ? 0.39749 0.46875 0.47300 0.05126  0.00142  0.07645  25  VAL A N   
150  C CA  . VAL A 59  ? 0.47943 0.55847 0.56314 0.06121  0.00635  0.08021  25  VAL A CA  
151  C C   . VAL A 59  ? 0.37879 0.45239 0.46301 0.06361  0.00121  0.07887  25  VAL A C   
152  O O   . VAL A 59  ? 0.33538 0.41870 0.43343 0.06717  0.00073  0.08487  25  VAL A O   
153  C CB  . VAL A 59  ? 0.34941 0.42457 0.42220 0.07131  0.01475  0.07671  25  VAL A CB  
154  C CG1 . VAL A 59  ? 0.38797 0.46648 0.46518 0.08295  0.01990  0.07828  25  VAL A CG1 
155  C CG2 . VAL A 59  ? 0.40801 0.49098 0.48290 0.07031  0.02102  0.08105  25  VAL A CG2 
156  N N   . ASN A 60  ? 0.35892 0.41718 0.42890 0.06152  -0.00284 0.07154  26  ASN A N   
157  C CA  . ASN A 60  ? 0.39512 0.44544 0.46362 0.06312  -0.00757 0.07060  26  ASN A CA  
158  C C   . ASN A 60  ? 0.46289 0.51922 0.54165 0.05565  -0.01491 0.07664  26  ASN A C   
159  O O   . ASN A 60  ? 0.45092 0.50902 0.53662 0.05973  -0.01774 0.08075  26  ASN A O   
160  C CB  . ASN A 60  ? 0.41700 0.45017 0.46891 0.06042  -0.01007 0.06191  26  ASN A CB  
161  C CG  . ASN A 60  ? 0.48072 0.50616 0.52206 0.06921  -0.00475 0.05582  26  ASN A CG  
162  O OD1 . ASN A 60  ? 0.50056 0.52959 0.54506 0.07924  0.00064  0.05785  26  ASN A OD1 
163  N ND2 . ASN A 60  ? 0.44782 0.46302 0.47660 0.06569  -0.00619 0.04825  26  ASN A ND2 
164  N N   . LEU A 61  ? 0.34354 0.40234 0.42262 0.04512  -0.01843 0.07730  27  LEU A N   
165  C CA  . LEU A 61  ? 0.41272 0.47782 0.50070 0.03770  -0.02582 0.08311  27  LEU A CA  
166  C C   . LEU A 61  ? 0.39692 0.48013 0.50481 0.04214  -0.02486 0.09171  27  LEU A C   
167  O O   . LEU A 61  ? 0.35296 0.44181 0.47006 0.04141  -0.03130 0.09711  27  LEU A O   
168  C CB  . LEU A 61  ? 0.35921 0.42282 0.44304 0.02626  -0.02864 0.08169  27  LEU A CB  
169  C CG  . LEU A 61  ? 0.41590 0.48471 0.50662 0.01763  -0.03710 0.08701  27  LEU A CG  
170  C CD1 . LEU A 61  ? 0.33172 0.39022 0.41388 0.01628  -0.04366 0.08623  27  LEU A CD1 
171  C CD2 . LEU A 61  ? 0.42582 0.49198 0.51190 0.00698  -0.03891 0.08524  27  LEU A CD2 
172  N N   . ALA A 62  ? 0.43034 0.52352 0.54544 0.04689  -0.01679 0.09354  28  ALA A N   
173  C CA  . ALA A 62  ? 0.41242 0.52508 0.54868 0.05126  -0.01418 0.10208  28  ALA A CA  
174  C C   . ALA A 62  ? 0.40649 0.52119 0.54882 0.06297  -0.01325 0.10420  28  ALA A C   
175  O O   . ALA A 62  ? 0.37935 0.50830 0.53979 0.06455  -0.01688 0.11166  28  ALA A O   
176  C CB  . ALA A 62  ? 0.35171 0.47257 0.49166 0.05458  -0.00387 0.10345  28  ALA A CB  
177  N N   . ARG A 63  ? 0.38718 0.48735 0.51474 0.07137  -0.00888 0.09767  29  ARG A N   
178  C CA  . ARG A 63  ? 0.41468 0.51229 0.54504 0.08303  -0.00784 0.09872  29  ARG A CA  
179  C C   . ARG A 63  ? 0.49387 0.58605 0.62499 0.07925  -0.01861 0.10119  29  ARG A C   
180  O O   . ARG A 63  ? 0.48381 0.58276 0.62719 0.08687  -0.02048 0.10689  29  ARG A O   
181  C CB  . ARG A 63  ? 0.40531 0.48491 0.51659 0.09093  -0.00188 0.09000  29  ARG A CB  
182  C CG  . ARG A 63  ? 0.42534 0.50862 0.53256 0.09596  0.00854  0.08755  29  ARG A CG  
183  C CD  . ARG A 63  ? 0.39160 0.45478 0.47623 0.09970  0.01108  0.07746  29  ARG A CD  
184  N NE  . ARG A 63  ? 0.50438 0.55558 0.58365 0.10976  0.01179  0.07471  29  ARG A NE  
185  C CZ  . ARG A 63  ? 0.49261 0.52379 0.55285 0.11232  0.01182  0.06584  29  ARG A CZ  
186  N NH1 . ARG A 63  ? 0.55758 0.58026 0.60353 0.10574  0.01061  0.05895  29  ARG A NH1 
187  N NH2 . ARG A 63  ? 0.58183 0.60109 0.63783 0.12169  0.01271  0.06390  29  ARG A NH2 
188  N N   . LEU A 64  ? 0.39046 0.47042 0.50824 0.06803  -0.02551 0.09732  30  LEU A N   
189  C CA  . LEU A 64  ? 0.44558 0.51852 0.56061 0.06379  -0.03545 0.09984  30  LEU A CA  
190  C C   . LEU A 64  ? 0.41754 0.50849 0.55087 0.05944  -0.04285 0.10891  30  LEU A C   
191  O O   . LEU A 64  ? 0.48328 0.57665 0.62367 0.06349  -0.04910 0.11455  30  LEU A O   
192  C CB  . LEU A 64  ? 0.42720 0.48353 0.52304 0.05269  -0.03940 0.09349  30  LEU A CB  
193  C CG  . LEU A 64  ? 0.42444 0.46350 0.50324 0.05516  -0.03398 0.08446  30  LEU A CG  
194  C CD1 . LEU A 64  ? 0.33054 0.35978 0.39556 0.04353  -0.03617 0.07877  30  LEU A CD1 
195  C CD2 . LEU A 64  ? 0.39457 0.41959 0.46701 0.06254  -0.03505 0.08386  30  LEU A CD2 
196  N N   . VAL A 65  ? 0.38289 0.48614 0.52411 0.05110  -0.04284 0.11060  31  VAL A N   
197  C CA  . VAL A 65  ? 0.49178 0.61222 0.65060 0.04498  -0.05091 0.11869  31  VAL A CA  
198  C C   . VAL A 65  ? 0.44436 0.58578 0.62794 0.05565  -0.04781 0.12661  31  VAL A C   
199  O O   . VAL A 65  ? 0.46533 0.61897 0.66399 0.05565  -0.05632 0.13402  31  VAL A O   
200  C CB  . VAL A 65  ? 0.40818 0.53340 0.56756 0.03265  -0.05119 0.11769  31  VAL A CB  
201  C CG1 . VAL A 65  ? 0.38839 0.53184 0.56706 0.02528  -0.05988 0.12578  31  VAL A CG1 
202  C CG2 . VAL A 65  ? 0.36593 0.47083 0.50173 0.02325  -0.05444 0.11015  31  VAL A CG2 
203  N N   . ALA A 66  ? 0.43550 0.58167 0.62345 0.06540  -0.03560 0.12531  32  ALA A N   
204  C CA  . ALA A 66  ? 0.48122 0.64658 0.69190 0.07749  -0.03051 0.13236  32  ALA A CA  
205  C C   . ALA A 66  ? 0.52976 0.68818 0.73996 0.08841  -0.03439 0.13398  32  ALA A C   
206  O O   . ALA A 66  ? 0.46378 0.63963 0.69581 0.09521  -0.03707 0.14214  32  ALA A O   
207  C CB  . ALA A 66  ? 0.47365 0.64176 0.68387 0.08631  -0.01548 0.12966  32  ALA A CB  
208  N N   . SER A 67  ? 0.48005 0.61313 0.66634 0.09014  -0.03492 0.12665  33  SER A N   
209  C CA  . SER A 67  ? 0.56197 0.68389 0.74461 0.09954  -0.03893 0.12803  33  SER A CA  
210  C C   . SER A 67  ? 0.60095 0.72641 0.78924 0.09337  -0.05323 0.13489  33  SER A C   
211  O O   . SER A 67  ? 0.59978 0.71962 0.78928 0.10203  -0.05760 0.13862  33  SER A O   
212  C CB  . SER A 67  ? 0.57642 0.66936 0.73164 0.10025  -0.03644 0.11850  33  SER A CB  
213  O OG  . SER A 67  ? 0.63935 0.72742 0.78969 0.11068  -0.02440 0.11302  33  SER A OG  
214  N N   . LYS A 68  ? 0.47492 0.60779 0.66498 0.07893  -0.06090 0.13653  34  LYS A N   
215  C CA  . LYS A 68  ? 0.54833 0.68743 0.74467 0.07251  -0.07522 0.14352  34  LYS A CA  
216  C C   . LYS A 68  ? 0.58313 0.75305 0.81032 0.07207  -0.07870 0.15257  34  LYS A C   
217  O O   . LYS A 68  ? 0.53768 0.71603 0.77012 0.06076  -0.09035 0.15663  34  LYS A O   
218  C CB  . LYS A 68  ? 0.51203 0.63668 0.68755 0.05642  -0.08245 0.13892  34  LYS A CB  
219  C CG  . LYS A 68  ? 0.56152 0.65870 0.70929 0.05551  -0.07764 0.12984  34  LYS A CG  
220  C CD  . LYS A 68  ? 0.57317 0.65624 0.70091 0.04118  -0.08509 0.12652  34  LYS A CD  
221  C CE  . LYS A 68  ? 0.68782 0.75745 0.80386 0.04147  -0.09463 0.13025  34  LYS A CE  
222  N NZ  . LYS A 68  ? 0.71346 0.76375 0.81684 0.05035  -0.08886 0.12687  34  LYS A NZ  
223  N N   . ASN A 69  ? 0.55126 0.73809 0.79862 0.08379  -0.06836 0.15553  35  ASN A N   
224  C CA  . ASN A 69  ? 0.61026 0.82907 0.89132 0.08593  -0.07011 0.16525  35  ASN A CA  
225  C C   . ASN A 69  ? 0.56709 0.79975 0.85684 0.06967  -0.07334 0.16644  35  ASN A C   
226  O O   . ASN A 69  ? 0.68578 0.93781 0.99526 0.06274  -0.08410 0.17382  35  ASN A O   
227  C CB  . ASN A 69  ? 0.63847 0.86593 0.93281 0.09073  -0.08342 0.17386  35  ASN A CB  
228  C CG  . ASN A 69  ? 0.83149 1.03742 1.11032 0.10405  -0.08283 0.17211  35  ASN A CG  
229  O OD1 . ASN A 69  ? 0.84825 1.04287 1.11899 0.11523  -0.07009 0.16690  35  ASN A OD1 
230  N ND2 . ASN A 69  ? 0.91590 1.11453 1.18902 0.10258  -0.09699 0.17647  35  ASN A ND2 
231  N N   . GLN A 70  ? 0.49163 0.71345 0.76623 0.06342  -0.06456 0.15913  36  GLN A N   
232  C CA  . GLN A 70  ? 0.49850 0.73040 0.77984 0.04905  -0.06546 0.15982  36  GLN A CA  
233  C C   . GLN A 70  ? 0.36501 0.60795 0.65662 0.05403  -0.04955 0.15994  36  GLN A C   
234  O O   . GLN A 70  ? 0.44002 0.67509 0.72340 0.06655  -0.03779 0.15615  36  GLN A O   
235  C CB  . GLN A 70  ? 0.39833 0.60637 0.65119 0.03570  -0.07026 0.15163  36  GLN A CB  
236  C CG  . GLN A 70  ? 0.45397 0.64624 0.69014 0.03179  -0.08349 0.15036  36  GLN A CG  
237  C CD  . GLN A 70  ? 0.51071 0.71983 0.76457 0.02601  -0.09836 0.15882  36  GLN A CD  
238  O OE1 . GLN A 70  ? 0.48333 0.70777 0.75194 0.01541  -0.10276 0.16222  36  GLN A OE1 
239  N NE2 . GLN A 70  ? 0.49647 0.70245 0.74897 0.03288  -0.10669 0.16252  36  GLN A NE2 
240  N N   . HIS A 71  ? 0.37261 0.63294 0.68131 0.04376  -0.04938 0.16446  37  HIS A N   
241  C CA  . HIS A 71  ? 0.44614 0.71881 0.76612 0.04682  -0.03443 0.16640  37  HIS A CA  
242  C C   . HIS A 71  ? 0.33454 0.58742 0.63041 0.03776  -0.02993 0.15881  37  HIS A C   
243  O O   . HIS A 71  ? 0.40624 0.65813 0.70150 0.02284  -0.03646 0.15902  37  HIS A O   
244  C CB  . HIS A 71  ? 0.44894 0.75310 0.80394 0.04086  -0.03621 0.17688  37  HIS A CB  
245  C CG  . HIS A 71  ? 0.54698 0.87450 0.92964 0.05244  -0.03805 0.18507  37  HIS A CG  
246  N ND1 . HIS A 71  ? 0.58205 0.94136 0.99946 0.05455  -0.03211 0.19459  37  HIS A ND1 
247  C CD2 . HIS A 71  ? 0.47320 0.79678 0.85432 0.06298  -0.04484 0.18550  37  HIS A CD2 
248  C CE1 . HIS A 71  ? 0.50424 0.87073 0.93157 0.06487  -0.03424 0.19666  37  HIS A CE1 
249  N NE2 . HIS A 71  ? 0.56901 0.91643 0.97760 0.07081  -0.04243 0.19252  37  HIS A NE2 
250  N N   . VAL A 72  ? 0.38868 0.62514 0.66439 0.04707  -0.01927 0.15197  38  VAL A N   
251  C CA  . VAL A 72  ? 0.40275 0.61858 0.65348 0.04097  -0.01570 0.14409  38  VAL A CA  
252  C C   . VAL A 72  ? 0.38682 0.60920 0.64066 0.04527  -0.00087 0.14568  38  VAL A C   
253  O O   . VAL A 72  ? 0.39993 0.62909 0.65873 0.05879  0.00966  0.14712  38  VAL A O   
254  C CB  . VAL A 72  ? 0.44916 0.63992 0.67255 0.04683  -0.01660 0.13462  38  VAL A CB  
255  C CG1 . VAL A 72  ? 0.33391 0.50659 0.53459 0.04203  -0.01221 0.12696  38  VAL A CG1 
256  C CG2 . VAL A 72  ? 0.35127 0.53372 0.56902 0.04135  -0.03065 0.13360  38  VAL A CG2 
257  N N   . THR A 73  ? 0.38040 0.59923 0.62972 0.03416  0.00023  0.14545  39  THR A N   
258  C CA  . THR A 73  ? 0.39188 0.61136 0.63760 0.03697  0.01369  0.14635  39  THR A CA  
259  C C   . THR A 73  ? 0.42602 0.62083 0.64310 0.03339  0.01380  0.13769  39  THR A C   
260  O O   . THR A 73  ? 0.42631 0.61104 0.63604 0.02156  0.00497  0.13499  39  THR A O   
261  C CB  . THR A 73  ? 0.39150 0.63005 0.65998 0.02717  0.01616  0.15562  39  THR A CB  
262  O OG1 . THR A 73  ? 0.42657 0.69120 0.72503 0.03052  0.01570  0.16412  39  THR A OG1 
263  C CG2 . THR A 73  ? 0.35485 0.59255 0.61744 0.03071  0.03106  0.15737  39  THR A CG2 
264  N N   . ILE A 74  ? 0.37851 0.56375 0.57941 0.04400  0.02358  0.13323  40  ILE A N   
265  C CA  . ILE A 74  ? 0.39108 0.55590 0.56696 0.04236  0.02487  0.12590  40  ILE A CA  
266  C C   . ILE A 74  ? 0.43034 0.59909 0.60748 0.03984  0.03419  0.13089  40  ILE A C   
267  O O   . ILE A 74  ? 0.38235 0.56167 0.56571 0.04811  0.04547  0.13561  40  ILE A O   
268  C CB  . ILE A 74  ? 0.40578 0.55719 0.56218 0.05472  0.02870  0.11799  40  ILE A CB  
269  C CG1 . ILE A 74  ? 0.39010 0.53674 0.54567 0.05743  0.02039  0.11404  40  ILE A CG1 
270  C CG2 . ILE A 74  ? 0.37619 0.50906 0.50916 0.05278  0.02893  0.11088  40  ILE A CG2 
271  C CD1 . ILE A 74  ? 0.32240 0.45628 0.46118 0.06943  0.02431  0.10679  40  ILE A CD1 
272  N N   . ILE A 75  ? 0.40689 0.56593 0.57698 0.02891  0.03017  0.12998  41  ILE A N   
273  C CA  . ILE A 75  ? 0.43164 0.59074 0.60079 0.02529  0.03806  0.13500  41  ILE A CA  
274  C C   . ILE A 75  ? 0.48211 0.62219 0.62486 0.03110  0.04164  0.12831  41  ILE A C   
275  O O   . ILE A 75  ? 0.36173 0.48624 0.49023 0.02729  0.03412  0.12119  41  ILE A O   
276  C CB  . ILE A 75  ? 0.38747 0.54637 0.56569 0.00956  0.03115  0.13863  41  ILE A CB  
277  C CG1 . ILE A 75  ? 0.45705 0.63623 0.66231 0.00326  0.02580  0.14523  41  ILE A CG1 
278  C CG2 . ILE A 75  ? 0.44220 0.59813 0.61790 0.00566  0.03947  0.14410  41  ILE A CG2 
279  C CD1 . ILE A 75  ? 0.36552 0.54238 0.57770 -0.01314 0.01605  0.14701  41  ILE A CD1 
280  N N   . THR A 76  ? 0.36839 0.51006 0.50441 0.04047  0.05303  0.13067  42  THR A N   
281  C CA  . THR A 76  ? 0.41151 0.53613 0.52207 0.04685  0.05548  0.12454  42  THR A CA  
282  C C   . THR A 76  ? 0.48857 0.61640 0.59405 0.05311  0.06854  0.13082  42  THR A C   
283  O O   . THR A 76  ? 0.46081 0.60442 0.58342 0.05217  0.07643  0.13980  42  THR A O   
284  C CB  . THR A 76  ? 0.44766 0.56443 0.54538 0.05598  0.05186  0.11502  42  THR A CB  
285  O OG1 . THR A 76  ? 0.46275 0.56277 0.53765 0.05881  0.05014  0.10810  42  THR A OG1 
286  C CG2 . THR A 76  ? 0.47531 0.60088 0.57528 0.06822  0.06080  0.11646  42  THR A CG2 
287  N N   . THR A 77  ? 0.48197 0.59499 0.56354 0.05938  0.07069  0.12630  43  THR A N   
288  C CA  . THR A 77  ? 0.47398 0.58511 0.54380 0.06532  0.08199  0.13153  43  THR A CA  
289  C C   . THR A 77  ? 0.55013 0.66207 0.60812 0.07953  0.08936  0.12813  43  THR A C   
290  O O   . THR A 77  ? 0.52515 0.63382 0.57911 0.08471  0.08396  0.11984  43  THR A O   
291  C CB  . THR A 77  ? 0.47462 0.56782 0.52394 0.06363  0.07851  0.12902  43  THR A CB  
292  O OG1 . THR A 77  ? 0.51538 0.59679 0.54784 0.06934  0.07086  0.11804  43  THR A OG1 
293  C CG2 . THR A 77  ? 0.49844 0.58809 0.55760 0.05026  0.07192  0.13179  43  THR A CG2 
294  N N   . PRO A 78  ? 0.58347 0.69835 0.63429 0.08603  0.10220  0.13438  44  PRO A N   
295  C CA  . PRO A 78  ? 0.49979 0.61635 0.54040 0.09989  0.11078  0.13152  44  PRO A CA  
296  C C   . PRO A 78  ? 0.51697 0.61661 0.53254 0.10784  0.10410  0.11940  44  PRO A C   
297  O O   . PRO A 78  ? 0.51211 0.61225 0.52648 0.11570  0.10442  0.11357  44  PRO A O   
298  C CB  . PRO A 78  ? 0.57243 0.69112 0.60446 0.10382  0.12529  0.14051  44  PRO A CB  
299  C CG  . PRO A 78  ? 0.60037 0.72745 0.65174 0.09086  0.12612  0.15071  44  PRO A CG  
300  C CD  . PRO A 78  ? 0.57426 0.69193 0.62782 0.08067  0.11058  0.14518  44  PRO A CD  
301  N N   . SER A 79  ? 0.51462 0.59922 0.51062 0.10618  0.09795  0.11556  45  SER A N   
302  C CA  . SER A 79  ? 0.54113 0.61123 0.51474 0.11297  0.09100  0.10420  45  SER A CA  
303  C C   . SER A 79  ? 0.60912 0.67791 0.59215 0.10902  0.07946  0.09587  45  SER A C   
304  O O   . SER A 79  ? 0.53730 0.59790 0.50804 0.11527  0.07571  0.08679  45  SER A O   
305  C CB  . SER A 79  ? 0.55857 0.61527 0.51217 0.11195  0.08612  0.10281  45  SER A CB  
306  O OG  . SER A 79  ? 0.76390 0.81845 0.70276 0.11745  0.09669  0.10979  45  SER A OG  
307  N N   . ASN A 80  ? 0.52124 0.59670 0.52451 0.09837  0.07366  0.09874  46  ASN A N   
308  C CA  . ASN A 80  ? 0.59944 0.67316 0.61035 0.09436  0.06336  0.09170  46  ASN A CA  
309  C C   . ASN A 80  ? 0.53997 0.62338 0.56492 0.09847  0.06640  0.09249  46  ASN A C   
310  O O   . ASN A 80  ? 0.49357 0.57102 0.51522 0.10115  0.06079  0.08502  46  ASN A O   
311  C CB  . ASN A 80  ? 0.45020 0.52511 0.47380 0.08179  0.05560  0.09374  46  ASN A CB  
312  C CG  . ASN A 80  ? 0.55252 0.61560 0.56186 0.07898  0.05086  0.09090  46  ASN A CG  
313  O OD1 . ASN A 80  ? 0.52085 0.57428 0.51642 0.08212  0.04502  0.08254  46  ASN A OD1 
314  N ND2 . ASN A 80  ? 0.54274 0.60655 0.55626 0.07299  0.05312  0.09802  46  ASN A ND2 
315  N N   . ALA A 81  ? 0.49794 0.59626 0.53907 0.09927  0.07538  0.10176  47  ALA A N   
316  C CA  . ALA A 81  ? 0.53853 0.64799 0.59534 0.10442  0.07857  0.10344  47  ALA A CA  
317  C C   . ALA A 81  ? 0.64487 0.74615 0.68514 0.11813  0.08386  0.09692  47  ALA A C   
318  O O   . ALA A 81  ? 0.58806 0.68976 0.63432 0.12282  0.08183  0.09364  47  ALA A O   
319  C CB  . ALA A 81  ? 0.47819 0.60748 0.55706 0.10288  0.08802  0.11520  47  ALA A CB  
320  N N   . GLN A 82  ? 0.61223 0.70444 0.63019 0.12484  0.09024  0.09486  48  GLN A N   
321  C CA  . GLN A 82  ? 0.73491 0.81686 0.73390 0.13766  0.09490  0.08768  48  GLN A CA  
322  C C   . GLN A 82  ? 0.72031 0.78521 0.70476 0.13721  0.08310  0.07577  48  GLN A C   
323  O O   . GLN A 82  ? 0.81651 0.87064 0.78567 0.14671  0.08503  0.06857  48  GLN A O   
324  C CB  . GLN A 82  ? 0.76223 0.83872 0.73915 0.14479  0.10487  0.08910  48  GLN A CB  
325  C CG  . GLN A 82  ? 0.90540 0.96574 0.85783 0.14237  0.09702  0.08290  48  GLN A CG  
326  C CD  . GLN A 82  ? 1.10764 1.16362 1.03874 0.14874  0.10673  0.08653  48  GLN A CD  
327  O OE1 . GLN A 82  ? 1.01943 1.08681 0.95923 0.14915  0.11824  0.09685  48  GLN A OE1 
328  N NE2 . GLN A 82  ? 0.87773 0.91726 0.78063 0.15335  0.10188  0.07837  48  GLN A NE2 
329  N N   . LEU A 83  ? 0.68355 0.74534 0.67237 0.12633  0.07144  0.07345  49  LEU A N   
330  C CA  . LEU A 83  ? 0.69385 0.74215 0.67362 0.12447  0.06069  0.06319  49  LEU A CA  
331  C C   . LEU A 83  ? 0.59441 0.64477 0.58859 0.12447  0.05750  0.06219  49  LEU A C   
332  O O   . LEU A 83  ? 0.65377 0.69173 0.63982 0.12409  0.05025  0.05396  49  LEU A O   
333  C CB  . LEU A 83  ? 0.64954 0.69449 0.62917 0.11344  0.05060  0.06129  49  LEU A CB  
334  C CG  . LEU A 83  ? 0.72358 0.76403 0.68803 0.11323  0.05098  0.06153  49  LEU A CG  
335  C CD1 . LEU A 83  ? 0.58504 0.62453 0.55488 0.10270  0.04191  0.06085  49  LEU A CD1 
336  C CD2 . LEU A 83  ? 0.69460 0.72162 0.63405 0.12131  0.04995  0.05297  49  LEU A CD2 
337  N N   . PHE A 84  ? 0.59757 0.66332 0.61326 0.12463  0.06233  0.07073  50  PHE A N   
338  C CA  . PHE A 84  ? 0.64908 0.71707 0.67871 0.12508  0.05832  0.07078  50  PHE A CA  
339  C C   . PHE A 84  ? 0.64714 0.73132 0.69550 0.13247  0.06742  0.07902  50  PHE A C   
340  O O   . PHE A 84  ? 0.62760 0.71692 0.69140 0.13249  0.06353  0.08126  50  PHE A O   
341  C CB  . PHE A 84  ? 0.51761 0.58825 0.55945 0.11184  0.04732  0.07221  50  PHE A CB  
342  C CG  . PHE A 84  ? 0.54951 0.63553 0.60790 0.10343  0.04826  0.08129  50  PHE A CG  
343  C CD1 . PHE A 84  ? 0.54360 0.62717 0.59448 0.09704  0.04762  0.08154  50  PHE A CD1 
344  C CD2 . PHE A 84  ? 0.48757 0.58991 0.56929 0.10170  0.04905  0.08958  50  PHE A CD2 
345  C CE1 . PHE A 84  ? 0.48626 0.58122 0.55124 0.08874  0.04834  0.08958  50  PHE A CE1 
346  C CE2 . PHE A 84  ? 0.46142 0.57700 0.55842 0.09262  0.04904  0.09754  50  PHE A CE2 
347  C CZ  . PHE A 84  ? 0.44494 0.55571 0.53289 0.08592  0.04894  0.09736  50  PHE A CZ  
348  N N   . ASP A 85  ? 0.65887 0.75168 0.70675 0.13904  0.07950  0.08398  51  ASP A N   
349  C CA  . ASP A 85  ? 0.68668 0.79784 0.75538 0.14612  0.08922  0.09244  51  ASP A CA  
350  C C   . ASP A 85  ? 0.67038 0.77512 0.73653 0.15923  0.09227  0.08804  51  ASP A C   
351  O O   . ASP A 85  ? 0.69108 0.81031 0.77953 0.16359  0.09483  0.09419  51  ASP A O   
352  C CB  . ASP A 85  ? 0.75644 0.87684 0.82271 0.15041  0.10302  0.09851  51  ASP A CB  
353  C CG  . ASP A 85  ? 0.92466 1.02832 0.96084 0.16163  0.11040  0.09103  51  ASP A CG  
354  O OD1 . ASP A 85  ? 0.91935 1.00338 0.93344 0.16015  0.10197  0.08122  51  ASP A OD1 
355  O OD2 . ASP A 85  ? 1.10160 1.21199 1.13605 0.17174  0.12462  0.09492  51  ASP A OD2 
356  N N   . LYS A 86  ? 0.70156 0.78447 0.74113 0.16576  0.09168  0.07752  52  LYS A N   
357  C CA  . LYS A 86  ? 0.74765 0.82024 0.78237 0.17792  0.09397  0.07239  52  LYS A CA  
358  C C   . LYS A 86  ? 0.77026 0.84124 0.81893 0.17311  0.08259  0.07244  52  LYS A C   
359  O O   . LYS A 86  ? 0.67894 0.75251 0.73851 0.18239  0.08528  0.07445  52  LYS A O   
360  C CB  . LYS A 86  ? 0.78575 0.83294 0.78724 0.18391  0.09409  0.06028  52  LYS A CB  
361  C CG  . LYS A 86  ? 1.09130 1.13656 1.07386 0.19207  0.10627  0.05940  52  LYS A CG  
362  C CD  . LYS A 86  ? 1.17659 1.19550 1.12502 0.19685  0.10371  0.04659  52  LYS A CD  
363  C CE  . LYS A 86  ? 1.30873 1.32516 1.23597 0.20541  0.11573  0.04617  52  LYS A CE  
364  N NZ  . LYS A 86  ? 1.35905 1.34961 1.25158 0.20950  0.11183  0.03336  52  LYS A NZ  
365  N N   . THR A 87  ? 0.66615 0.73279 0.71436 0.15926  0.07030  0.07070  53  THR A N   
366  C CA  . THR A 87  ? 0.68454 0.75061 0.74544 0.15348  0.05974  0.07208  53  THR A CA  
367  C C   . THR A 87  ? 0.59144 0.68183 0.68221 0.15203  0.06048  0.08368  53  THR A C   
368  O O   . THR A 87  ? 0.55567 0.64856 0.65911 0.15559  0.05665  0.08663  53  THR A O   
369  C CB  . THR A 87  ? 0.68403 0.74086 0.73677 0.13901  0.04809  0.06776  53  THR A CB  
370  O OG1 . THR A 87  ? 0.70581 0.74170 0.73336 0.14027  0.04646  0.05705  53  THR A OG1 
371  C CG2 . THR A 87  ? 0.59967 0.65509 0.66317 0.13262  0.03776  0.06966  53  THR A CG2 
372  N N   . ILE A 88  ? 0.54927 0.65746 0.65167 0.14671  0.06492  0.09064  54  ILE A N   
373  C CA  . ILE A 88  ? 0.64012 0.77311 0.77245 0.14392  0.06521  0.10181  54  ILE A CA  
374  C C   . ILE A 88  ? 0.70834 0.85276 0.85475 0.15913  0.07496  0.10628  54  ILE A C   
375  O O   . ILE A 88  ? 0.64954 0.80815 0.81905 0.16046  0.07112  0.11295  54  ILE A O   
376  C CB  . ILE A 88  ? 0.65111 0.79852 0.79125 0.13487  0.06915  0.10797  54  ILE A CB  
377  C CG1 . ILE A 88  ? 0.59140 0.72622 0.71720 0.12126  0.05984  0.10321  54  ILE A CG1 
378  C CG2 . ILE A 88  ? 0.58101 0.75461 0.75347 0.13029  0.06838  0.11938  54  ILE A CG2 
379  C CD1 . ILE A 88  ? 0.62226 0.75386 0.75406 0.11116  0.04587  0.10257  54  ILE A CD1 
380  N N   . GLU A 89  ? 0.66606 0.80453 0.79842 0.17136  0.08767  0.10272  55  GLU A N   
381  C CA  . GLU A 89  ? 0.75567 0.90349 0.89951 0.18760  0.09875  0.10612  55  GLU A CA  
382  C C   . GLU A 89  ? 0.72372 0.85943 0.86770 0.19498  0.09192  0.10263  55  GLU A C   
383  O O   . GLU A 89  ? 0.71634 0.86696 0.88303 0.20355  0.09427  0.10933  55  GLU A O   
384  C CB  . GLU A 89  ? 0.77797 0.91619 0.89989 0.19931  0.11335  0.10103  55  GLU A CB  
385  C CG  . GLU A 89  ? 0.94087 1.09722 1.06955 0.19703  0.12498  0.10835  55  GLU A CG  
386  C CD  . GLU A 89  ? 1.01711 1.20518 1.18363 0.19182  0.12616  0.12148  55  GLU A CD  
387  O OE1 . GLU A 89  ? 0.99173 1.19594 1.17902 0.20314  0.13387  0.12702  55  GLU A OE1 
388  O OE2 . GLU A 89  ? 0.88712 1.08398 1.06304 0.17647  0.11922  0.12618  55  GLU A OE2 
389  N N   . GLU A 90  ? 0.70992 0.81889 0.82965 0.19161  0.08325  0.09269  56  GLU A N   
390  C CA  . GLU A 90  ? 0.70602 0.80026 0.82374 0.19717  0.07628  0.08959  56  GLU A CA  
391  C C   . GLU A 90  ? 0.74009 0.84770 0.88109 0.18863  0.06439  0.09766  56  GLU A C   
392  O O   . GLU A 90  ? 0.72896 0.83736 0.88142 0.19684  0.06180  0.10104  56  GLU A O   
393  C CB  . GLU A 90  ? 0.75323 0.81650 0.84033 0.19317  0.06974  0.07747  56  GLU A CB  
394  C CG  . GLU A 90  ? 0.85484 0.89954 0.91725 0.20547  0.07968  0.06832  56  GLU A CG  
395  C CD  . GLU A 90  ? 1.04045 1.05796 1.07407 0.19857  0.07231  0.05654  56  GLU A CD  
396  O OE1 . GLU A 90  ? 1.02600 1.04097 1.06013 0.18433  0.06083  0.05598  56  GLU A OE1 
397  O OE2 . GLU A 90  ? 1.07646 1.07542 1.08702 0.20726  0.07799  0.04773  56  GLU A OE2 
398  N N   . GLU A 91  ? 0.65215 0.76919 0.79921 0.17257  0.05672  0.10080  57  GLU A N   
399  C CA  . GLU A 91  ? 0.76075 0.89033 0.92797 0.16379  0.04503  0.10830  57  GLU A CA  
400  C C   . GLU A 91  ? 0.67956 0.83898 0.87902 0.16968  0.04948  0.11970  57  GLU A C   
401  O O   . GLU A 91  ? 0.74857 0.91622 0.96517 0.17200  0.04214  0.12567  57  GLU A O   
402  C CB  . GLU A 91  ? 0.66454 0.79482 0.82797 0.14548  0.03648  0.10788  57  GLU A CB  
403  C CG  . GLU A 91  ? 0.59162 0.69571 0.72704 0.13870  0.03127  0.09739  57  GLU A CG  
404  C CD  . GLU A 91  ? 0.66660 0.75581 0.79639 0.13513  0.01990  0.09547  57  GLU A CD  
405  O OE1 . GLU A 91  ? 0.84024 0.93856 0.98654 0.13808  0.01513  0.10247  57  GLU A OE1 
406  O OE2 . GLU A 91  ? 0.57350 0.64233 0.68268 0.12929  0.01568  0.08740  57  GLU A OE2 
407  N N   . LYS A 92  ? 0.63788 0.81440 0.84648 0.17195  0.06132  0.12339  58  LYS A N   
408  C CA  . LYS A 92  ? 0.73745 0.94453 0.97889 0.17786  0.06726  0.13444  58  LYS A CA  
409  C C   . LYS A 92  ? 0.75261 0.95972 1.00105 0.19724  0.07354  0.13528  58  LYS A C   
410  O O   . LYS A 92  ? 0.62392 0.84983 0.89818 0.20016  0.07021  0.14300  58  LYS A O   
411  C CB  . LYS A 92  ? 0.72232 0.94496 0.96905 0.17670  0.08073  0.13790  58  LYS A CB  
412  C CG  . LYS A 92  ? 0.68105 0.91046 0.93070 0.15772  0.07435  0.14066  58  LYS A CG  
413  C CD  . LYS A 92  ? 0.76293 1.01820 1.03338 0.15584  0.08579  0.14967  58  LYS A CD  
414  C CE  . LYS A 92  ? 0.66186 0.90600 0.91059 0.14916  0.09224  0.14592  58  LYS A CE  
415  N NZ  . LYS A 92  ? 0.85680 1.12186 1.12030 0.15158  0.10764  0.15410  58  LYS A NZ  
416  N N   . ALA A 93  ? 0.75995 0.94319 0.98257 0.20881  0.08144  0.12596  59  ALA A N   
417  C CA  . ALA A 93  ? 0.78140 0.95762 1.00414 0.22584  0.08708  0.12417  59  ALA A CA  
418  C C   . ALA A 93  ? 0.71266 0.87827 0.93835 0.22631  0.07317  0.12475  59  ALA A C   
419  O O   . ALA A 93  ? 0.83084 0.99529 1.06293 0.23663  0.07470  0.12515  59  ALA A O   
420  C CB  . ALA A 93  ? 0.77035 0.91987 0.96112 0.23684  0.09762  0.11298  59  ALA A CB  
421  N N   . ALA A 94  ? 0.69395 0.84936 0.91187 0.21336  0.05929  0.12379  60  ALA A N   
422  C CA  . ALA A 94  ? 0.73835 0.88405 0.95827 0.21224  0.04558  0.12578  60  ALA A CA  
423  C C   . ALA A 94  ? 0.75851 0.93199 1.00913 0.20508  0.03545  0.13758  60  ALA A C   
424  O O   . ALA A 94  ? 0.76780 0.93471 1.01981 0.20240  0.02256  0.14032  60  ALA A O   
425  C CB  . ALA A 94  ? 0.74386 0.86095 0.93505 0.19922  0.03558  0.11702  60  ALA A CB  
426  N N   . GLY A 95  ? 0.66212 0.86392 0.93412 0.19964  0.04024  0.14348  61  GLY A N   
427  C CA  . GLY A 95  ? 0.64748 0.87456 0.94651 0.19006  0.03011  0.15278  61  GLY A CA  
428  C C   . GLY A 95  ? 0.76131 0.99452 1.06272 0.17229  0.01907  0.15605  61  GLY A C   
429  O O   . GLY A 95  ? 0.71178 0.96477 1.03385 0.16258  0.00947  0.16316  61  GLY A O   
430  N N   . HIS A 96  ? 0.74347 0.95401 1.01620 0.16295  0.01934  0.14674  62  HIS A N   
431  C CA  . HIS A 96  ? 0.73148 0.94053 0.99826 0.14343  0.00913  0.14597  62  HIS A CA  
432  C C   . HIS A 96  ? 0.63013 0.86126 0.91236 0.13551  0.01555  0.15038  62  HIS A C   
433  O O   . HIS A 96  ? 0.59865 0.83217 0.87790 0.14189  0.02971  0.14855  62  HIS A O   
434  C CB  . HIS A 96  ? 0.62163 0.79952 0.85404 0.13739  0.00753  0.13471  62  HIS A CB  
435  C CG  . HIS A 96  ? 0.75259 0.90741 0.96926 0.14182  0.00024  0.13079  62  HIS A CG  
436  N ND1 . HIS A 96  ? 0.85726 0.98430 1.04628 0.14446  0.00339  0.12066  62  HIS A ND1 
437  C CD2 . HIS A 96  ? 0.63763 0.79257 0.86216 0.14370  -0.01031 0.13610  62  HIS A CD2 
438  C CE1 . HIS A 96  ? 0.78459 0.89505 0.96541 0.14725  -0.00420 0.11998  62  HIS A CE1 
439  N NE2 . HIS A 96  ? 0.74182 0.86816 0.94295 0.14731  -0.01248 0.12944  62  HIS A NE2 
440  N N   . HIS A 97  ? 0.53356 0.77943 0.83090 0.12127  0.00498  0.15623  63  HIS A N   
441  C CA  . HIS A 97  ? 0.57508 0.84180 0.88925 0.11176  0.00945  0.16146  63  HIS A CA  
442  C C   . HIS A 97  ? 0.58666 0.83475 0.87592 0.09933  0.00976  0.15402  63  HIS A C   
443  O O   . HIS A 97  ? 0.56253 0.80601 0.84727 0.08448  -0.00136 0.15332  63  HIS A O   
444  C CB  . HIS A 97  ? 0.47013 0.76083 0.81268 0.10213  -0.00281 0.17099  63  HIS A CB  
445  C CG  . HIS A 97  ? 0.74486 1.05581 1.11411 0.11491  -0.00432 0.17900  63  HIS A CG  
446  N ND1 . HIS A 97  ? 0.78325 1.10150 1.15980 0.12938  0.01047  0.17922  63  HIS A ND1 
447  C CD2 . HIS A 97  ? 0.76252 1.07839 1.14134 0.11229  -0.01848 0.18253  63  HIS A CD2 
448  C CE1 . HIS A 97  ? 0.67845 1.00595 1.06954 0.13542  0.00554  0.18258  63  HIS A CE1 
449  N NE2 . HIS A 97  ? 0.76368 1.09016 1.15652 0.12541  -0.01214 0.18478  63  HIS A NE2 
450  N N   . ILE A 98  ? 0.46171 0.69841 0.73382 0.10612  0.02259  0.14829  64  ILE A N   
451  C CA  . ILE A 98  ? 0.56238 0.78242 0.81153 0.09691  0.02427  0.14159  64  ILE A CA  
452  C C   . ILE A 98  ? 0.48211 0.70991 0.73233 0.10198  0.03992  0.14330  64  ILE A C   
453  O O   . ILE A 98  ? 0.57987 0.81039 0.83062 0.11662  0.05119  0.14327  64  ILE A O   
454  C CB  . ILE A 98  ? 0.49848 0.68908 0.71682 0.09936  0.02114  0.13062  64  ILE A CB  
455  C CG1 . ILE A 98  ? 0.55210 0.72823 0.74946 0.09065  0.02271  0.12429  64  ILE A CG1 
456  C CG2 . ILE A 98  ? 0.59084 0.77316 0.80076 0.11655  0.03018  0.12679  64  ILE A CG2 
457  C CD1 . ILE A 98  ? 0.50225 0.65321 0.67447 0.08753  0.01558  0.11466  64  ILE A CD1 
458  N N   . ARG A 99  ? 0.45050 0.68051 0.69970 0.09018  0.04097  0.14492  65  ARG A N   
459  C CA  . ARG A 99  ? 0.42665 0.66326 0.67569 0.09351  0.05559  0.14773  65  ARG A CA  
460  C C   . ARG A 99  ? 0.52665 0.74779 0.75585 0.08263  0.05435  0.14363  65  ARG A C   
461  O O   . ARG A 99  ? 0.44938 0.65966 0.67107 0.07134  0.04257  0.14009  65  ARG A O   
462  C CB  . ARG A 99  ? 0.57176 0.83880 0.85437 0.09146  0.06108  0.15968  65  ARG A CB  
463  C CG  . ARG A 99  ? 0.64173 0.91948 0.94173 0.07386  0.04920  0.16512  65  ARG A CG  
464  C CD  . ARG A 99  ? 0.72609 1.03504 1.06062 0.07093  0.05530  0.17711  65  ARG A CD  
465  N NE  . ARG A 99  ? 1.11877 1.43657 1.46895 0.05285  0.04318  0.18179  65  ARG A NE  
466  C CZ  . ARG A 99  ? 1.24460 1.58958 1.62693 0.04577  0.04431  0.19218  65  ARG A CZ  
467  N NH1 . ARG A 99  ? 1.23278 1.60102 1.63717 0.05546  0.05816  0.19978  65  ARG A NH1 
468  N NH2 . ARG A 99  ? 1.16905 1.51798 1.56175 0.02835  0.03141  0.19488  65  ARG A NH2 
469  N N   . VAL A 100 ? 0.47704 0.69684 0.69707 0.08686  0.06708  0.14436  66  VAL A N   
470  C CA  . VAL A 100 ? 0.46459 0.67032 0.66603 0.07877  0.06758  0.14163  66  VAL A CA  
471  C C   . VAL A 100 ? 0.48174 0.70378 0.69975 0.07198  0.07557  0.15175  66  VAL A C   
472  O O   . VAL A 100 ? 0.58425 0.82124 0.81333 0.08002  0.08854  0.15795  66  VAL A O   
473  C CB  . VAL A 100 ? 0.50331 0.68994 0.67525 0.08922  0.07457  0.13362  66  VAL A CB  
474  C CG1 . VAL A 100 ? 0.56836 0.74064 0.72185 0.08127  0.07335  0.13113  66  VAL A CG1 
475  C CG2 . VAL A 100 ? 0.47899 0.65050 0.63692 0.09587  0.06751  0.12410  66  VAL A CG2 
476  N N   . HIS A 101 ? 0.46582 0.68430 0.68526 0.05719  0.06850  0.15346  67  HIS A N   
477  C CA  . HIS A 101 ? 0.48459 0.71300 0.71530 0.04887  0.07560  0.16237  67  HIS A CA  
478  C C   . HIS A 101 ? 0.56280 0.77084 0.76628 0.04868  0.08045  0.15891  67  HIS A C   
479  O O   . HIS A 101 ? 0.48156 0.67128 0.66874 0.04227  0.07117  0.15248  67  HIS A O   
480  C CB  . HIS A 101 ? 0.45620 0.69271 0.70637 0.03211  0.06451  0.16696  67  HIS A CB  
481  C CG  . HIS A 101 ? 0.54984 0.79218 0.80920 0.02155  0.07068  0.17539  67  HIS A CG  
482  N ND1 . HIS A 101 ? 0.55240 0.81691 0.83345 0.02325  0.08310  0.18580  67  HIS A ND1 
483  C CD2 . HIS A 101 ? 0.57642 0.80427 0.82582 0.00935  0.06685  0.17516  67  HIS A CD2 
484  C CE1 . HIS A 101 ? 0.58022 0.84343 0.86434 0.01153  0.08638  0.19197  67  HIS A CE1 
485  N NE2 . HIS A 101 ? 0.50064 0.74080 0.76520 0.00322  0.07642  0.18554  67  HIS A NE2 
486  N N   . ILE A 102 ? 0.53010 0.74160 0.72858 0.05619  0.09512  0.16345  68  ILE A N   
487  C CA  . ILE A 102 ? 0.51685 0.70959 0.68833 0.05792  0.10025  0.16115  68  ILE A CA  
488  C C   . ILE A 102 ? 0.59650 0.78694 0.77295 0.04354  0.09911  0.16772  68  ILE A C   
489  O O   . ILE A 102 ? 0.58431 0.79226 0.78468 0.03595  0.10366  0.17763  68  ILE A O   
490  C CB  . ILE A 102 ? 0.55232 0.74838 0.71405 0.07149  0.11659  0.16396  68  ILE A CB  
491  C CG1 . ILE A 102 ? 0.50851 0.70263 0.66212 0.08600  0.11728  0.15612  68  ILE A CG1 
492  C CG2 . ILE A 102 ? 0.53511 0.71233 0.66868 0.07277  0.12132  0.16305  68  ILE A CG2 
493  C CD1 . ILE A 102 ? 0.52150 0.69409 0.65258 0.08741  0.10524  0.14393  68  ILE A CD1 
494  N N   . ILE A 103 ? 0.52768 0.69641 0.68234 0.03969  0.09290  0.16226  69  ILE A N   
495  C CA  . ILE A 103 ? 0.51368 0.67419 0.66586 0.02884  0.09373  0.16785  69  ILE A CA  
496  C C   . ILE A 103 ? 0.60281 0.74529 0.72590 0.03682  0.09998  0.16599  69  ILE A C   
497  O O   . ILE A 103 ? 0.58724 0.71978 0.69061 0.04751  0.09826  0.15749  69  ILE A O   
498  C CB  . ILE A 103 ? 0.65284 0.80299 0.80716 0.01575  0.07933  0.16369  69  ILE A CB  
499  C CG1 . ILE A 103 ? 0.61132 0.74160 0.74167 0.02093  0.07082  0.15184  69  ILE A CG1 
500  C CG2 . ILE A 103 ? 0.52483 0.69223 0.70578 0.00788  0.07165  0.16542  69  ILE A CG2 
501  C CD1 . ILE A 103 ? 0.65542 0.77491 0.78568 0.00982  0.05799  0.14684  69  ILE A CD1 
502  N N   . LYS A 104 ? 0.56233 0.70025 0.68269 0.03121  0.10679  0.17432  70  LYS A N   
503  C CA  . LYS A 104 ? 0.59461 0.71598 0.68752 0.03862  0.11317  0.17473  70  LYS A CA  
504  C C   . LYS A 104 ? 0.60757 0.70688 0.68100 0.03735  0.10143  0.16615  70  LYS A C   
505  O O   . LYS A 104 ? 0.63049 0.72268 0.71007 0.02601  0.09384  0.16640  70  LYS A O   
506  C CB  . LYS A 104 ? 0.59932 0.72222 0.69631 0.03231  0.12433  0.18760  70  LYS A CB  
507  C CG  . LYS A 104 ? 0.79979 0.91032 0.86961 0.04220  0.13467  0.19086  70  LYS A CG  
508  C CD  . LYS A 104 ? 0.88075 0.98814 0.95294 0.03358  0.14395  0.20390  70  LYS A CD  
509  C CE  . LYS A 104 ? 0.90845 1.02213 0.97147 0.04255  0.16160  0.21244  70  LYS A CE  
510  N NZ  . LYS A 104 ? 1.05784 1.19685 1.15124 0.03664  0.17279  0.22261  70  LYS A NZ  
511  N N   . PHE A 105 ? 0.52177 0.61040 0.57205 0.04896  0.09997  0.15844  71  PHE A N   
512  C CA  . PHE A 105 ? 0.52747 0.59684 0.55969 0.04908  0.09025  0.15130  71  PHE A CA  
513  C C   . PHE A 105 ? 0.59695 0.65304 0.61824 0.04572  0.09425  0.15901  71  PHE A C   
514  O O   . PHE A 105 ? 0.58412 0.64015 0.59572 0.05092  0.10515  0.16652  71  PHE A O   
515  C CB  . PHE A 105 ? 0.53714 0.59971 0.54826 0.06188  0.08771  0.14203  71  PHE A CB  
516  C CG  . PHE A 105 ? 0.54452 0.59165 0.54228 0.06196  0.07651  0.13374  71  PHE A CG  
517  C CD1 . PHE A 105 ? 0.49912 0.54666 0.50476 0.05815  0.06612  0.12497  71  PHE A CD1 
518  C CD2 . PHE A 105 ? 0.54299 0.57574 0.52071 0.06619  0.07665  0.13522  71  PHE A CD2 
519  C CE1 . PHE A 105 ? 0.53798 0.57322 0.53330 0.05838  0.05703  0.11763  71  PHE A CE1 
520  C CE2 . PHE A 105 ? 0.56085 0.58166 0.52903 0.06701  0.06656  0.12793  71  PHE A CE2 
521  C CZ  . PHE A 105 ? 0.63025 0.65299 0.60806 0.06299  0.05721  0.11902  71  PHE A CZ  
522  N N   . PRO A 106 ? 0.55337 0.59666 0.57429 0.03770  0.08621  0.15751  72  PRO A N   
523  C CA  . PRO A 106 ? 0.59339 0.62268 0.60583 0.03357  0.09014  0.16585  72  PRO A CA  
524  C C   . PRO A 106 ? 0.59852 0.61269 0.58342 0.04491  0.09109  0.16499  72  PRO A C   
525  O O   . PRO A 106 ? 0.48600 0.48351 0.46022 0.04444  0.08490  0.16313  72  PRO A O   
526  C CB  . PRO A 106 ? 0.58983 0.60915 0.61010 0.02251  0.08011  0.16231  72  PRO A CB  
527  C CG  . PRO A 106 ? 0.55218 0.57363 0.57210 0.02624  0.07005  0.14983  72  PRO A CG  
528  C CD  . PRO A 106 ? 0.54175 0.58145 0.56897 0.03227  0.07378  0.14822  72  PRO A CD  
529  N N   . SER A 107 ? 0.53958 0.55914 0.51233 0.05559  0.09855  0.16624  73  SER A N   
530  C CA  . SER A 107 ? 0.55108 0.55690 0.49601 0.06677  0.09822  0.16510  73  SER A CA  
531  C C   . SER A 107 ? 0.52786 0.51849 0.46170 0.06428  0.10287  0.17575  73  SER A C   
532  O O   . SER A 107 ? 0.60210 0.57674 0.51820 0.06932  0.09679  0.17397  73  SER A O   
533  C CB  . SER A 107 ? 0.63304 0.64665 0.56574 0.07793  0.10617  0.16466  73  SER A CB  
534  O OG  . SER A 107 ? 0.55541 0.58085 0.49793 0.08038  0.10193  0.15501  73  SER A OG  
535  N N   . ALA A 108 ? 0.48851 0.48402 0.43371 0.05632  0.11345  0.18725  74  ALA A N   
536  C CA  . ALA A 108 ? 0.51442 0.49456 0.44805 0.05373  0.11964  0.19882  74  ALA A CA  
537  C C   . ALA A 108 ? 0.60712 0.57018 0.54281 0.04620  0.11024  0.19758  74  ALA A C   
538  O O   . ALA A 108 ? 0.62536 0.56914 0.54188 0.05045  0.10883  0.20115  74  ALA A O   
539  C CB  . ALA A 108 ? 0.64956 0.64097 0.59832 0.04541  0.13359  0.21142  74  ALA A CB  
540  N N   . GLN A 109 ? 0.60271 0.57170 0.56047 0.03554  0.10373  0.19257  75  GLN A N   
541  C CA  . GLN A 109 ? 0.64637 0.59849 0.60578 0.02837  0.09504  0.18998  75  GLN A CA  
542  C C   . GLN A 109 ? 0.60178 0.54192 0.54481 0.03858  0.08484  0.18016  75  GLN A C   
543  O O   . GLN A 109 ? 0.72130 0.64307 0.65840 0.03689  0.07984  0.17987  75  GLN A O   
544  C CB  . GLN A 109 ? 0.71240 0.67431 0.69688 0.01536  0.08961  0.18542  75  GLN A CB  
545  C CG  . GLN A 109 ? 0.74452 0.72512 0.75169 0.00495  0.09760  0.19349  75  GLN A CG  
546  C CD  . GLN A 109 ? 0.88515 0.88911 0.89890 0.01241  0.10335  0.19244  75  GLN A CD  
547  O OE1 . GLN A 109 ? 0.78006 0.78387 0.77626 0.02546  0.10706  0.19101  75  GLN A OE1 
548  N NE2 . GLN A 109 ? 0.98310 1.00661 1.02200 0.00424  0.10368  0.19308  75  GLN A NE2 
549  N N   . LEU A 110 ? 0.62119 0.57129 0.55773 0.04895  0.08165  0.17209  76  LEU A N   
550  C CA  . LEU A 110 ? 0.59766 0.54014 0.52207 0.05796  0.07153  0.16243  76  LEU A CA  
551  C C   . LEU A 110 ? 0.62861 0.56357 0.52840 0.07111  0.07269  0.16511  76  LEU A C   
552  O O   . LEU A 110 ? 0.65474 0.58380 0.54440 0.07911  0.06388  0.15819  76  LEU A O   
553  C CB  . LEU A 110 ? 0.55450 0.51192 0.48894 0.05929  0.06500  0.15037  76  LEU A CB  
554  C CG  . LEU A 110 ? 0.68112 0.64489 0.63742 0.04724  0.06146  0.14642  76  LEU A CG  
555  C CD1 . LEU A 110 ? 0.59658 0.57711 0.56237 0.04868  0.05833  0.13790  76  LEU A CD1 
556  C CD2 . LEU A 110 ? 0.61161 0.56084 0.56749 0.04405  0.05343  0.14136  76  LEU A CD2 
557  N N   . GLY A 111 ? 0.55290 0.48840 0.44281 0.07350  0.08321  0.17512  77  GLY A N   
558  C CA  . GLY A 111 ? 0.66613 0.59458 0.52996 0.08619  0.08416  0.17754  77  GLY A CA  
559  C C   . GLY A 111 ? 0.68864 0.62776 0.54506 0.09562  0.07920  0.16709  77  GLY A C   
560  O O   . GLY A 111 ? 0.67012 0.60216 0.50517 0.10626  0.07447  0.16525  77  GLY A O   
561  N N   . LEU A 112 ? 0.53604 0.49130 0.40925 0.09187  0.07951  0.16025  78  LEU A N   
562  C CA  . LEU A 112 ? 0.55066 0.51443 0.41745 0.09987  0.07480  0.14983  78  LEU A CA  
563  C C   . LEU A 112 ? 0.60210 0.57230 0.45784 0.10568  0.08586  0.15388  78  LEU A C   
564  O O   . LEU A 112 ? 0.62748 0.60491 0.49402 0.10037  0.09725  0.16201  78  LEU A O   
565  C CB  . LEU A 112 ? 0.45141 0.42706 0.34041 0.09366  0.06894  0.14003  78  LEU A CB  
566  C CG  . LEU A 112 ? 0.56432 0.53504 0.46257 0.08942  0.05770  0.13313  78  LEU A CG  
567  C CD1 . LEU A 112 ? 0.53108 0.51326 0.45147 0.08129  0.05475  0.12636  78  LEU A CD1 
568  C CD2 . LEU A 112 ? 0.53487 0.50068 0.41816 0.09886  0.04788  0.12526  78  LEU A CD2 
569  N N   . PRO A 113 ? 0.68272 0.65073 0.51736 0.11645  0.08289  0.14815  79  PRO A N   
570  C CA  . PRO A 113 ? 0.58919 0.56225 0.41155 0.12286  0.09379  0.15037  79  PRO A CA  
571  C C   . PRO A 113 ? 0.67538 0.66418 0.51827 0.11972  0.09686  0.14457  79  PRO A C   
572  O O   . PRO A 113 ? 0.60888 0.60277 0.46758 0.11557  0.08745  0.13563  79  PRO A O   
573  C CB  . PRO A 113 ? 0.66727 0.63163 0.46104 0.13444  0.08623  0.14335  79  PRO A CB  
574  C CG  . PRO A 113 ? 0.58557 0.54868 0.38757 0.13264  0.07029  0.13333  79  PRO A CG  
575  C CD  . PRO A 113 ? 0.51943 0.48087 0.34124 0.12304  0.06916  0.13878  79  PRO A CD  
576  N N   . THR A 114 ? 0.60936 0.60581 0.45177 0.12220  0.11066  0.15025  80  THR A N   
577  C CA  . THR A 114 ? 0.63280 0.64505 0.49666 0.11991  0.11502  0.14682  80  THR A CA  
578  C C   . THR A 114 ? 0.52918 0.54140 0.38771 0.12579  0.10556  0.13266  80  THR A C   
579  O O   . THR A 114 ? 0.64945 0.65114 0.48326 0.13392  0.09985  0.12638  80  THR A O   
580  C CB  . THR A 114 ? 0.62790 0.64830 0.48973 0.12403  0.13253  0.15537  80  THR A CB  
581  O OG1 . THR A 114 ? 0.66021 0.69757 0.54709 0.12168  0.13657  0.15328  80  THR A OG1 
582  C CG2 . THR A 114 ? 0.49242 0.50357 0.32099 0.13739  0.13660  0.15200  80  THR A CG2 
583  N N   . GLY A 115 ? 0.53173 0.55528 0.41361 0.12113  0.10317  0.12780  81  GLY A N   
584  C CA  . GLY A 115 ? 0.67413 0.69678 0.55324 0.12512  0.09426  0.11496  81  GLY A CA  
585  C C   . GLY A 115 ? 0.58364 0.60033 0.46539 0.12044  0.07880  0.10688  81  GLY A C   
586  O O   . GLY A 115 ? 0.61118 0.62675 0.49132 0.12256  0.07097  0.09631  81  GLY A O   
587  N N   . VAL A 116 ? 0.53340 0.54566 0.41900 0.11436  0.07468  0.11150  82  VAL A N   
588  C CA  . VAL A 116 ? 0.46159 0.46999 0.35338 0.10958  0.06157  0.10454  82  VAL A CA  
589  C C   . VAL A 116 ? 0.60368 0.61987 0.52198 0.09850  0.06141  0.10711  82  VAL A C   
590  O O   . VAL A 116 ? 0.56095 0.57468 0.48632 0.09206  0.06296  0.11428  82  VAL A O   
591  C CB  . VAL A 116 ? 0.50670 0.50366 0.38382 0.11174  0.05656  0.10707  82  VAL A CB  
592  C CG1 . VAL A 116 ? 0.49884 0.49375 0.38495 0.10743  0.04421  0.09974  82  VAL A CG1 
593  C CG2 . VAL A 116 ? 0.59253 0.58206 0.44185 0.12275  0.05595  0.10497  82  VAL A CG2 
594  N N   . GLU A 117 ? 0.53585 0.56027 0.46786 0.09614  0.05911  0.10119  83  GLU A N   
595  C CA  . GLU A 117 ? 0.58723 0.62017 0.54327 0.08619  0.05896  0.10380  83  GLU A CA  
596  C C   . GLU A 117 ? 0.64297 0.67615 0.60801 0.08164  0.04850  0.09453  83  GLU A C   
597  O O   . GLU A 117 ? 0.53934 0.57944 0.52238 0.07411  0.04731  0.09551  83  GLU A O   
598  C CB  . GLU A 117 ? 0.53731 0.58282 0.50501 0.08716  0.06864  0.10901  83  GLU A CB  
599  C CG  . GLU A 117 ? 0.55516 0.60213 0.51537 0.09126  0.08109  0.11900  83  GLU A CG  
600  C CD  . GLU A 117 ? 0.58736 0.64986 0.56462 0.09106  0.09147  0.12541  83  GLU A CD  
601  O OE1 . GLU A 117 ? 0.55090 0.62294 0.54655 0.08760  0.08798  0.12256  83  GLU A OE1 
602  O OE2 . GLU A 117 ? 0.57224 0.63791 0.54495 0.09453  0.10335  0.13386  83  GLU A OE2 
603  N N   . ASN A 118 ? 0.53394 0.56016 0.48712 0.08562  0.04082  0.08594  84  ASN A N   
604  C CA  . ASN A 118 ? 0.57195 0.59816 0.53320 0.08090  0.03183  0.07765  84  ASN A CA  
605  C C   . ASN A 118 ? 0.59449 0.61308 0.54391 0.08400  0.02413  0.07129  84  ASN A C   
606  O O   . ASN A 118 ? 0.62138 0.63504 0.55489 0.09108  0.02468  0.07216  84  ASN A O   
607  C CB  . ASN A 118 ? 0.57753 0.60871 0.54299 0.08279  0.03151  0.07236  84  ASN A CB  
608  C CG  . ASN A 118 ? 0.64759 0.67522 0.59580 0.09292  0.03361  0.06842  84  ASN A CG  
609  O OD1 . ASN A 118 ? 0.77608 0.79674 0.70900 0.09726  0.02927  0.06425  84  ASN A OD1 
610  N ND2 . ASN A 118 ? 0.59885 0.63110 0.54913 0.09709  0.04010  0.06966  84  ASN A ND2 
611  N N   . LEU A 119 ? 0.53662 0.55500 0.49419 0.07873  0.01687  0.06506  85  LEU A N   
612  C CA  . LEU A 119 ? 0.55470 0.56871 0.50584 0.08090  0.00945  0.05919  85  LEU A CA  
613  C C   . LEU A 119 ? 0.51399 0.52686 0.45175 0.08822  0.00577  0.05287  85  LEU A C   
614  O O   . LEU A 119 ? 0.66767 0.67756 0.59650 0.09245  0.00037  0.05027  85  LEU A O   
615  C CB  . LEU A 119 ? 0.55342 0.56883 0.51695 0.07364  0.00402  0.05367  85  LEU A CB  
616  C CG  . LEU A 119 ? 0.68076 0.69329 0.65258 0.06735  0.00476  0.05752  85  LEU A CG  
617  C CD1 . LEU A 119 ? 0.49329 0.50653 0.47406 0.06137  -0.00007 0.05099  85  LEU A CD1 
618  C CD2 . LEU A 119 ? 0.54544 0.55153 0.50885 0.07203  0.00486  0.06141  85  LEU A CD2 
619  N N   . PHE A 120 ? 0.55909 0.57377 0.49511 0.09000  0.00807  0.05018  86  PHE A N   
620  C CA  . PHE A 120 ? 0.67196 0.68311 0.59309 0.09660  0.00449  0.04351  86  PHE A CA  
621  C C   . PHE A 120 ? 0.65342 0.65994 0.55550 0.10495  0.00733  0.04745  86  PHE A C   
622  O O   . PHE A 120 ? 0.71285 0.71510 0.59998 0.11022  0.00160  0.04184  86  PHE A O   
623  C CB  . PHE A 120 ? 0.68917 0.70076 0.61140 0.09744  0.00748  0.04017  86  PHE A CB  
624  N N   . ALA A 121 ? 0.67360 0.68051 0.57528 0.10580  0.01577  0.05716  87  ALA A N   
625  C CA  . ALA A 121 ? 0.65895 0.66051 0.54143 0.11337  0.01968  0.06248  87  ALA A CA  
626  C C   . ALA A 121 ? 0.72463 0.72190 0.60279 0.11399  0.01465  0.06570  87  ALA A C   
627  O O   . ALA A 121 ? 0.65678 0.64810 0.51672 0.12072  0.01604  0.07001  87  ALA A O   
628  C CB  . ALA A 121 ? 0.55118 0.55541 0.43562 0.11381  0.03245  0.07231  87  ALA A CB  
629  N N   . ALA A 122 ? 0.64669 0.64604 0.54004 0.10781  0.00921  0.06393  88  ALA A N   
630  C CA  . ALA A 122 ? 0.62830 0.62335 0.51929 0.10929  0.00440  0.06648  88  ALA A CA  
631  C C   . ALA A 122 ? 0.63796 0.63348 0.52208 0.11382  -0.00673 0.05830  88  ALA A C   
632  O O   . ALA A 122 ? 0.77616 0.77598 0.66399 0.11210  -0.01167 0.04956  88  ALA A O   
633  C CB  . ALA A 122 ? 0.59362 0.58983 0.50335 0.10120  0.00439  0.06792  88  ALA A CB  
634  N N   . SER A 123 ? 0.59483 0.58585 0.46952 0.11943  -0.01104 0.06157  89  SER A N   
635  C CA  . SER A 123 ? 0.64575 0.63870 0.51442 0.12436  -0.02258 0.05497  89  SER A CA  
636  C C   . SER A 123 ? 0.58987 0.58297 0.46652 0.12585  -0.02813 0.05688  89  SER A C   
637  O O   . SER A 123 ? 0.67335 0.66950 0.54668 0.13081  -0.03817 0.05291  89  SER A O   
638  C CB  . SER A 123 ? 0.64348 0.63058 0.48634 0.13311  -0.02428 0.05630  89  SER A CB  
639  O OG  . SER A 123 ? 0.79048 0.76936 0.62110 0.13729  -0.01722 0.06740  89  SER A OG  
640  N N   . ASP A 124 ? 0.60055 0.59034 0.48786 0.12184  -0.02214 0.06264  90  ASP A N   
641  C CA  . ASP A 124 ? 0.64129 0.62874 0.53532 0.12413  -0.02586 0.06479  90  ASP A CA  
642  C C   . ASP A 124 ? 0.46076 0.44539 0.36981 0.11612  -0.01902 0.06713  90  ASP A C   
643  O O   . ASP A 124 ? 0.50732 0.49131 0.41939 0.10961  -0.01164 0.06931  90  ASP A O   
644  C CB  . ASP A 124 ? 0.58195 0.55949 0.45827 0.13300  -0.02634 0.07358  90  ASP A CB  
645  C CG  . ASP A 124 ? 0.66735 0.63610 0.53063 0.13226  -0.01586 0.08275  90  ASP A CG  
646  O OD1 . ASP A 124 ? 0.62638 0.59075 0.49849 0.12580  -0.00784 0.08784  90  ASP A OD1 
647  O OD2 . ASP A 124 ? 0.82825 0.79459 0.67236 0.13787  -0.01553 0.08480  90  ASP A OD2 
648  N N   . ASN A 125 ? 0.43558 0.41832 0.35374 0.11707  -0.02173 0.06670  91  ASN A N   
649  C CA  . ASN A 125 ? 0.60839 0.58678 0.53904 0.10943  -0.01622 0.06750  91  ASN A CA  
650  C C   . ASN A 125 ? 0.55696 0.52312 0.48074 0.10683  -0.00812 0.07737  91  ASN A C   
651  O O   . ASN A 125 ? 0.52431 0.48841 0.45642 0.09791  -0.00275 0.07826  91  ASN A O   
652  C CB  . ASN A 125 ? 0.61252 0.58991 0.55237 0.11252  -0.02007 0.06470  91  ASN A CB  
653  C CG  . ASN A 125 ? 0.55884 0.55035 0.51004 0.11296  -0.02685 0.05506  91  ASN A CG  
654  O OD1 . ASN A 125 ? 0.54537 0.54529 0.50099 0.10729  -0.02732 0.04953  91  ASN A OD1 
655  N ND2 . ASN A 125 ? 0.65978 0.65407 0.61649 0.11983  -0.03203 0.05336  91  ASN A ND2 
656  N N   . GLN A 126 ? 0.55029 0.50807 0.45896 0.11403  -0.00744 0.08519  92  GLN A N   
657  C CA  . GLN A 126 ? 0.57282 0.51859 0.47541 0.11081  0.00086  0.09540  92  GLN A CA  
658  C C   . GLN A 126 ? 0.49951 0.45103 0.40368 0.10380  0.00787  0.09726  92  GLN A C   
659  O O   . GLN A 126 ? 0.57638 0.52443 0.48828 0.09524  0.01406  0.10136  92  GLN A O   
660  C CB  . GLN A 126 ? 0.64332 0.57867 0.52732 0.12030  0.00048  0.10400  92  GLN A CB  
661  C CG  . GLN A 126 ? 0.76128 0.67935 0.64255 0.11895  0.00539  0.11319  92  GLN A CG  
662  C CD  . GLN A 126 ? 1.02706 0.93394 0.88806 0.12507  0.00906  0.12459  92  GLN A CD  
663  O OE1 . GLN A 126 ? 0.87439 0.78345 0.72102 0.13459  0.00420  0.12503  92  GLN A OE1 
664  N NE2 . GLN A 126 ? 0.89721 0.79158 0.75631 0.11908  0.01754  0.13403  92  GLN A NE2 
665  N N   . THR A 127 ? 0.49694 0.45726 0.39419 0.10746  0.00673  0.09413  93  THR A N   
666  C CA  . THR A 127 ? 0.57691 0.54377 0.47686 0.10237  0.01363  0.09529  93  THR A CA  
667  C C   . THR A 127 ? 0.56249 0.53715 0.48136 0.09313  0.01316  0.08900  93  THR A C   
668  O O   . THR A 127 ? 0.54343 0.52009 0.47086 0.08577  0.01939  0.09290  93  THR A O   
669  C CB  . THR A 127 ? 0.64606 0.61837 0.53266 0.10937  0.01218  0.09196  93  THR A CB  
670  O OG1 . THR A 127 ? 0.58192 0.54621 0.44857 0.11850  0.01081  0.09713  93  THR A OG1 
671  C CG2 . THR A 127 ? 0.57183 0.54939 0.45950 0.10627  0.02124  0.09490  93  THR A CG2 
672  N N   . ALA A 128 ? 0.54701 0.52659 0.47283 0.09319  0.00571  0.07970  94  ALA A N   
673  C CA  . ALA A 128 ? 0.52447 0.51013 0.46593 0.08466  0.00513  0.07396  94  ALA A CA  
674  C C   . ALA A 128 ? 0.55563 0.53453 0.50585 0.07681  0.00850  0.07796  94  ALA A C   
675  O O   . ALA A 128 ? 0.53115 0.51351 0.49109 0.06861  0.01124  0.07823  94  ALA A O   
676  C CB  . ALA A 128 ? 0.52966 0.52073 0.47631 0.08609  -0.00267 0.06421  94  ALA A CB  
677  N N   . GLY A 129 ? 0.54035 0.50870 0.48664 0.07936  0.00787  0.08114  95  GLY A N   
678  C CA  . GLY A 129 ? 0.54409 0.50274 0.49603 0.07186  0.01104  0.08482  95  GLY A CA  
679  C C   . GLY A 129 ? 0.57637 0.53270 0.52822 0.06619  0.01802  0.09394  95  GLY A C   
680  O O   . GLY A 129 ? 0.53724 0.49076 0.49787 0.05651  0.02005  0.09553  95  GLY A O   
681  N N   . LYS A 130 ? 0.56102 0.51887 0.50293 0.07181  0.02182  0.10007  96  LYS A N   
682  C CA  . LYS A 130 ? 0.57170 0.52956 0.51498 0.06660  0.02985  0.10944  96  LYS A CA  
683  C C   . LYS A 130 ? 0.46620 0.43806 0.42251 0.06014  0.03182  0.10734  96  LYS A C   
684  O O   . LYS A 130 ? 0.46293 0.43648 0.42950 0.05126  0.03602  0.11269  96  LYS A O   
685  C CB  . LYS A 130 ? 0.50608 0.46167 0.43339 0.07516  0.03442  0.11654  96  LYS A CB  
686  C CG  . LYS A 130 ? 0.51858 0.45816 0.43305 0.08032  0.03383  0.12226  96  LYS A CG  
687  C CD  . LYS A 130 ? 0.57394 0.50998 0.47091 0.08760  0.03938  0.13094  96  LYS A CD  
688  C CE  . LYS A 130 ? 0.59734 0.51537 0.48152 0.09202  0.03907  0.13833  96  LYS A CE  
689  N NZ  . LYS A 130 ? 0.70449 0.61739 0.57054 0.09754  0.04598  0.14865  96  LYS A NZ  
690  N N   . ILE A 131 ? 0.46424 0.44599 0.42073 0.06441  0.02839  0.09979  97  ILE A N   
691  C CA  . ILE A 131 ? 0.49988 0.49380 0.46842 0.05953  0.02948  0.09743  97  ILE A CA  
692  C C   . ILE A 131 ? 0.53389 0.52746 0.51600 0.04930  0.02579  0.09434  97  ILE A C   
693  O O   . ILE A 131 ? 0.48237 0.48290 0.47639 0.04202  0.02781  0.09714  97  ILE A O   
694  C CB  . ILE A 131 ? 0.53275 0.53371 0.49652 0.06646  0.02600  0.08949  97  ILE A CB  
695  C CG1 . ILE A 131 ? 0.54635 0.54789 0.49571 0.07560  0.03084  0.09309  97  ILE A CG1 
696  C CG2 . ILE A 131 ? 0.40638 0.41738 0.38300 0.06148  0.02553  0.08600  97  ILE A CG2 
697  C CD1 . ILE A 131 ? 0.65238 0.65316 0.58929 0.08401  0.02490  0.08529  97  ILE A CD1 
698  N N   . HIS A 132 ? 0.50155 0.48713 0.48182 0.04884  0.02036  0.08874  98  HIS A N   
699  C CA  . HIS A 132 ? 0.56184 0.54388 0.55127 0.03921  0.01757  0.08608  98  HIS A CA  
700  C C   . HIS A 132 ? 0.48681 0.46163 0.47986 0.03128  0.02123  0.09411  98  HIS A C   
701  O O   . HIS A 132 ? 0.52677 0.50442 0.53004 0.02161  0.02038  0.09486  98  HIS A O   
702  C CB  . HIS A 132 ? 0.47121 0.44536 0.45681 0.04152  0.01273  0.07878  98  HIS A CB  
703  C CG  . HIS A 132 ? 0.66781 0.65039 0.65540 0.04423  0.00842  0.07005  98  HIS A CG  
704  N ND1 . HIS A 132 ? 0.62498 0.60900 0.61908 0.03774  0.00554  0.06423  98  HIS A ND1 
705  C CD2 . HIS A 132 ? 0.63095 0.62005 0.61415 0.05205  0.00639  0.06630  98  HIS A CD2 
706  C CE1 . HIS A 132 ? 0.61890 0.61015 0.61348 0.04125  0.00259  0.05780  98  HIS A CE1 
707  N NE2 . HIS A 132 ? 0.72368 0.71813 0.71222 0.04963  0.00266  0.05860  98  HIS A NE2 
708  N N   . MET A 133 ? 0.48958 0.45478 0.47407 0.03492  0.02489  0.10054  99  MET A N   
709  C CA  . MET A 133 ? 0.47846 0.43543 0.46590 0.02686  0.02891  0.10898  99  MET A CA  
710  C C   . MET A 133 ? 0.57818 0.54849 0.57643 0.02145  0.03402  0.11591  99  MET A C   
711  O O   . MET A 133 ? 0.55450 0.52290 0.56170 0.01103  0.03565  0.12138  99  MET A O   
712  C CB  . MET A 133 ? 0.58044 0.52357 0.55470 0.03314  0.03224  0.11521  99  MET A CB  
713  C CG  . MET A 133 ? 0.85431 0.78070 0.82842 0.02500  0.03420  0.12125  99  MET A CG  
714  S SD  . MET A 133 ? 1.02894 0.94173 1.00574 0.01776  0.02775  0.11273  99  MET A SD  
715  C CE  . MET A 133 ? 0.90678 0.81208 0.89231 0.00160  0.03022  0.12025  99  MET A CE  
716  N N   . ALA A 134 ? 0.52590 0.50972 0.52386 0.02845  0.03665  0.11573  100 ALA A N   
717  C CA  . ALA A 134 ? 0.47499 0.47321 0.48444 0.02511  0.04248  0.12217  100 ALA A CA  
718  C C   . ALA A 134 ? 0.48063 0.48781 0.50734 0.01490  0.03825  0.12004  100 ALA A C   
719  O O   . ALA A 134 ? 0.53709 0.55434 0.57756 0.00829  0.04198  0.12701  100 ALA A O   
720  C CB  . ALA A 134 ? 0.42239 0.43113 0.42608 0.03594  0.04580  0.12055  100 ALA A CB  
721  N N   . ALA A 135 ? 0.44355 0.44781 0.46999 0.01340  0.03045  0.11092  101 ALA A N   
722  C CA  . ALA A 135 ? 0.58768 0.59865 0.62762 0.00384  0.02542  0.10890  101 ALA A CA  
723  C C   . ALA A 135 ? 0.54850 0.55322 0.59580 -0.00854 0.02472  0.11425  101 ALA A C   
724  O O   . ALA A 135 ? 0.48951 0.50411 0.55132 -0.01726 0.02239  0.11687  101 ALA A O   
725  C CB  . ALA A 135 ? 0.46272 0.46872 0.49761 0.00445  0.01806  0.09848  101 ALA A CB  
726  N N   . HIS A 136 ? 0.60986 0.59773 0.64746 -0.00960 0.02612  0.11602  102 HIS A N   
727  C CA  . HIS A 136 ? 0.62377 0.60308 0.66717 -0.02200 0.02558  0.12112  102 HIS A CA  
728  C C   . HIS A 136 ? 0.68187 0.67042 0.73542 -0.02549 0.03320  0.13274  102 HIS A C   
729  O O   . HIS A 136 ? 0.71565 0.70805 0.78287 -0.03772 0.03209  0.13764  102 HIS A O   
730  C CB  . HIS A 136 ? 0.81237 0.76791 0.84130 -0.02168 0.02465  0.11890  102 HIS A CB  
731  C CG  . HIS A 136 ? 1.08280 1.02534 1.11528 -0.03503 0.02318  0.12260  102 HIS A CG  
732  N ND1 . HIS A 136 ? 1.17134 1.10781 1.20635 -0.04510 0.01572  0.11667  102 HIS A ND1 
733  C CD2 . HIS A 136 ? 1.04189 0.97512 1.07479 -0.04057 0.02803  0.13160  102 HIS A CD2 
734  C CE1 . HIS A 136 ? 1.14271 1.06636 1.17956 -0.05645 0.01540  0.12120  102 HIS A CE1 
735  N NE2 . HIS A 136 ? 1.19249 1.11395 1.22889 -0.05423 0.02297  0.13051  102 HIS A NE2 
736  N N   . PHE A 137 ? 0.59913 0.59178 0.64616 -0.01520 0.04097  0.13732  103 PHE A N   
737  C CA  . PHE A 137 ? 0.56470 0.56399 0.61884 -0.01796 0.05013  0.14906  103 PHE A CA  
738  C C   . PHE A 137 ? 0.64830 0.67204 0.72312 -0.02129 0.05261  0.15301  103 PHE A C   
739  O O   . PHE A 137 ? 0.63779 0.66991 0.72578 -0.02835 0.05879  0.16284  103 PHE A O   
740  C CB  . PHE A 137 ? 0.65114 0.64590 0.68880 -0.00534 0.05787  0.15266  103 PHE A CB  
741  C CG  . PHE A 137 ? 0.74513 0.71637 0.76566 -0.00352 0.05752  0.15371  103 PHE A CG  
742  C CD1 . PHE A 137 ? 0.86161 0.82038 0.88391 -0.01324 0.06060  0.16189  103 PHE A CD1 
743  C CD2 . PHE A 137 ? 0.66568 0.62718 0.66918 0.00786  0.05379  0.14670  103 PHE A CD2 
744  C CE1 . PHE A 137 ? 0.97459 0.90983 0.98054 -0.01065 0.06029  0.16316  103 PHE A CE1 
745  C CE2 . PHE A 137 ? 0.74953 0.69006 0.73845 0.01076  0.05313  0.14804  103 PHE A CE2 
746  C CZ  . PHE A 137 ? 0.83222 0.75870 0.82165 0.00199  0.05652  0.15631  103 PHE A CZ  
747  N N   . VAL A 138 ? 0.52699 0.56256 0.60602 -0.01643 0.04806  0.14598  104 VAL A N   
748  C CA  . VAL A 138 ? 0.55706 0.61591 0.65560 -0.01721 0.05049  0.14975  104 VAL A CA  
749  C C   . VAL A 138 ? 0.54774 0.61308 0.66545 -0.03185 0.04334  0.15141  104 VAL A C   
750  O O   . VAL A 138 ? 0.61002 0.69591 0.74777 -0.03444 0.04381  0.15550  104 VAL A O   
751  C CB  . VAL A 138 ? 0.58309 0.64999 0.67789 -0.00617 0.04813  0.14195  104 VAL A CB  
752  C CG1 . VAL A 138 ? 0.48988 0.55443 0.56853 0.00768  0.05616  0.14193  104 VAL A CG1 
753  C CG2 . VAL A 138 ? 0.46147 0.51650 0.54709 -0.00730 0.03739  0.13114  104 VAL A CG2 
754  N N   . LYS A 139 ? 0.54667 0.59426 0.65805 -0.04118 0.03643  0.14820  105 LYS A N   
755  C CA  . LYS A 139 ? 0.61819 0.66859 0.74373 -0.05559 0.02759  0.14801  105 LYS A CA  
756  C C   . LYS A 139 ? 0.69501 0.76230 0.84386 -0.06535 0.03172  0.15923  105 LYS A C   
757  O O   . LYS A 139 ? 0.64999 0.73389 0.81819 -0.07258 0.02577  0.16062  105 LYS A O   
758  C CB  . LYS A 139 ? 0.64671 0.67160 0.75834 -0.06344 0.02153  0.14311  105 LYS A CB  
759  C CG  . LYS A 139 ? 0.71728 0.74119 0.83880 -0.07858 0.01111  0.14127  105 LYS A CG  
760  C CD  . LYS A 139 ? 0.77772 0.77357 0.88220 -0.08487 0.00600  0.13520  105 LYS A CD  
761  C CE  . LYS A 139 ? 0.80830 0.79810 0.92255 -0.10196 0.00259  0.14045  105 LYS A CE  
762  N NZ  . LYS A 139 ? 1.07617 1.06832 1.19665 -0.11353 -0.00978 0.13550  105 LYS A NZ  
763  N N   . ALA A 140 ? 0.56120 0.62493 0.70908 -0.06594 0.04174  0.16782  106 ALA A N   
764  C CA  . ALA A 140 ? 0.64724 0.72661 0.81826 -0.07666 0.04669  0.17925  106 ALA A CA  
765  C C   . ALA A 140 ? 0.64888 0.75881 0.84074 -0.07064 0.05174  0.18384  106 ALA A C   
766  O O   . ALA A 140 ? 0.65172 0.78094 0.86874 -0.08010 0.04773  0.18818  106 ALA A O   
767  C CB  . ALA A 140 ? 0.71261 0.77994 0.87523 -0.07731 0.05784  0.18790  106 ALA A CB  
768  N N   . ASP A 141 ? 0.57339 0.68787 0.75508 -0.05460 0.06022  0.18282  107 ASP A N   
769  C CA  . ASP A 141 ? 0.56919 0.71045 0.76854 -0.04692 0.06620  0.18657  107 ASP A CA  
770  C C   . ASP A 141 ? 0.58008 0.73332 0.79195 -0.04787 0.05452  0.18048  107 ASP A C   
771  O O   . ASP A 141 ? 0.61604 0.79397 0.85280 -0.04885 0.05546  0.18580  107 ASP A O   
772  C CB  . ASP A 141 ? 0.48709 0.62594 0.66799 -0.02926 0.07625  0.18457  107 ASP A CB  
773  C CG  . ASP A 141 ? 0.72259 0.85698 0.89565 -0.02718 0.09016  0.19368  107 ASP A CG  
774  O OD1 . ASP A 141 ? 0.69410 0.82642 0.87652 -0.03981 0.09237  0.20180  107 ASP A OD1 
775  O OD2 . ASP A 141 ? 0.69041 0.82231 0.84681 -0.01326 0.09874  0.19281  107 ASP A OD2 
776  N N   . ILE A 142 ? 0.51847 0.65486 0.71368 -0.04730 0.04372  0.16984  108 ILE A N   
777  C CA  . ILE A 142 ? 0.59894 0.74400 0.80244 -0.04790 0.03264  0.16424  108 ILE A CA  
778  C C   . ILE A 142 ? 0.62472 0.77650 0.84712 -0.06457 0.02253  0.16745  108 ILE A C   
779  O O   . ILE A 142 ? 0.54639 0.71881 0.78980 -0.06648 0.01747  0.17014  108 ILE A O   
780  C CB  . ILE A 142 ? 0.50504 0.63008 0.68399 -0.04200 0.02565  0.15226  108 ILE A CB  
781  C CG1 . ILE A 142 ? 0.44481 0.56687 0.60815 -0.02567 0.03416  0.14900  108 ILE A CG1 
782  C CG2 . ILE A 142 ? 0.42135 0.55226 0.60673 -0.04461 0.01375  0.14715  108 ILE A CG2 
783  C CD1 . ILE A 142 ? 0.41662 0.51886 0.55625 -0.02039 0.02887  0.13814  108 ILE A CD1 
784  N N   . GLU A 143 ? 0.60219 0.73615 0.81719 -0.07670 0.01889  0.16718  109 GLU A N   
785  C CA  . GLU A 143 ? 0.64583 0.78414 0.87725 -0.09389 0.00872  0.16990  109 GLU A CA  
786  C C   . GLU A 143 ? 0.64675 0.81308 0.90996 -0.09959 0.01393  0.18193  109 GLU A C   
787  O O   . GLU A 143 ? 0.63840 0.82283 0.92351 -0.10756 0.00485  0.18440  109 GLU A O   
788  C CB  . GLU A 143 ? 0.60192 0.71326 0.81789 -0.10509 0.00581  0.16761  109 GLU A CB  
789  C CG  . GLU A 143 ? 0.65049 0.73901 0.84394 -0.10590 -0.00484 0.15567  109 GLU A CG  
790  C CD  . GLU A 143 ? 0.87781 0.94038 1.05884 -0.11830 -0.00887 0.15340  109 GLU A CD  
791  O OE1 . GLU A 143 ? 0.91101 0.96734 1.09366 -0.12234 -0.00103 0.16026  109 GLU A OE1 
792  O OE2 . GLU A 143 ? 0.90377 0.95093 1.07227 -0.12379 -0.01944 0.14484  109 GLU A OE2 
793  N N   . GLU A 144 ? 0.62661 0.79765 0.89297 -0.09541 0.02858  0.18989  110 GLU A N   
794  C CA  . GLU A 144 ? 0.65681 0.85660 0.95438 -0.09942 0.03613  0.20190  110 GLU A CA  
795  C C   . GLU A 144 ? 0.62922 0.85658 0.94574 -0.08940 0.03544  0.20266  110 GLU A C   
796  O O   . GLU A 144 ? 0.66304 0.91588 1.01021 -0.09684 0.03172  0.20940  110 GLU A O   
797  C CB  . GLU A 144 ? 0.67803 0.87607 0.97039 -0.09370 0.05384  0.20968  110 GLU A CB  
798  C CG  . GLU A 144 ? 0.80911 1.03557 1.13359 -0.09953 0.06380  0.22316  110 GLU A CG  
799  C CD  . GLU A 144 ? 1.06753 1.29105 1.40644 -0.12085 0.05953  0.22972  110 GLU A CD  
800  O OE1 . GLU A 144 ? 1.07125 1.27743 1.39803 -0.12531 0.06797  0.23433  110 GLU A OE1 
801  O OE2 . GLU A 144 ? 0.98524 1.22169 1.34510 -0.13251 0.04695  0.22928  110 GLU A OE2 
802  N N   . PHE A 145 ? 0.62319 0.84566 0.92237 -0.07249 0.03858  0.19589  111 PHE A N   
803  C CA  . PHE A 145 ? 0.58475 0.82962 0.89906 -0.06150 0.03828  0.19606  111 PHE A CA  
804  C C   . PHE A 145 ? 0.59602 0.84667 0.92085 -0.06878 0.02089  0.19233  111 PHE A C   
805  O O   . PHE A 145 ? 0.62048 0.89630 0.96981 -0.06579 0.01852  0.19675  111 PHE A O   
806  C CB  . PHE A 145 ? 0.54654 0.78006 0.83651 -0.04306 0.04457  0.18862  111 PHE A CB  
807  C CG  . PHE A 145 ? 0.60738 0.85715 0.90759 -0.03133 0.04260  0.18679  111 PHE A CG  
808  C CD1 . PHE A 145 ? 0.60809 0.88475 0.93263 -0.02401 0.05249  0.19503  111 PHE A CD1 
809  C CD2 . PHE A 145 ? 0.54785 0.78533 0.83309 -0.02711 0.03165  0.17710  111 PHE A CD2 
810  C CE1 . PHE A 145 ? 0.59703 0.88691 0.93052 -0.01204 0.05090  0.19340  111 PHE A CE1 
811  C CE2 . PHE A 145 ? 0.55179 0.80173 0.84525 -0.01615 0.02989  0.17585  111 PHE A CE2 
812  C CZ  . PHE A 145 ? 0.52478 0.80034 0.84220 -0.00825 0.03923  0.18388  111 PHE A CZ  
813  N N   . MET A 146 ? 0.56699 0.79466 0.87327 -0.07777 0.00882  0.18453  112 MET A N   
814  C CA  . MET A 146 ? 0.64868 0.87868 0.96013 -0.08489 -0.00803 0.18058  112 MET A CA  
815  C C   . MET A 146 ? 0.62517 0.86658 0.95956 -0.10356 -0.01740 0.18675  112 MET A C   
816  O O   . MET A 146 ? 0.55645 0.81120 0.90539 -0.10843 -0.03027 0.18723  112 MET A O   
817  C CB  . MET A 146 ? 0.52021 0.72010 0.79947 -0.08510 -0.01624 0.16869  112 MET A CB  
818  C CG  . MET A 146 ? 0.64091 0.83771 0.90668 -0.07014 -0.01683 0.16188  112 MET A CG  
819  S SD  . MET A 146 ? 0.58297 0.74574 0.81027 -0.06532 -0.01659 0.14964  112 MET A SD  
820  C CE  . MET A 146 ? 0.65428 0.80206 0.87269 -0.08065 -0.03354 0.14372  112 MET A CE  
821  N N   . LYS A 147 ? 0.60845 0.84415 0.94592 -0.11459 -0.01201 0.19160  113 LYS A N   
822  C CA  . LYS A 147 ? 0.62250 0.87256 0.98615 -0.13287 -0.01990 0.19868  113 LYS A CA  
823  C C   . LYS A 147 ? 0.59743 0.88633 0.99935 -0.13025 -0.01443 0.20997  113 LYS A C   
824  O O   . LYS A 147 ? 0.63834 0.94274 1.06056 -0.13950 -0.02553 0.21220  113 LYS A O   
825  C CB  . LYS A 147 ? 0.74247 0.97437 1.09919 -0.14580 -0.01497 0.20133  113 LYS A CB  
826  C CG  . LYS A 147 ? 0.88974 1.08330 1.21093 -0.14921 -0.02091 0.19050  113 LYS A CG  
827  C CD  . LYS A 147 ? 0.95480 1.12931 1.26922 -0.16028 -0.01477 0.19401  113 LYS A CD  
828  C CE  . LYS A 147 ? 0.85279 1.01792 1.15170 -0.14659 0.00260  0.19612  113 LYS A CE  
829  N NZ  . LYS A 147 ? 0.79378 0.93013 1.07504 -0.15461 0.00640  0.19643  113 LYS A NZ  
830  N N   . GLU A 148 ? 0.58342 0.88356 0.98858 -0.11483 0.00237  0.21419  114 GLU A N   
831  C CA  . GLU A 148 ? 0.62495 0.95851 1.06132 -0.10858 0.00957  0.22280  114 GLU A CA  
832  C C   . GLU A 148 ? 0.63112 0.98183 1.07800 -0.09713 0.00208  0.22089  114 GLU A C   
833  O O   . GLU A 148 ? 0.62889 1.00098 1.09866 -0.09745 -0.00314 0.22427  114 GLU A O   
834  C CB  . GLU A 148 ? 0.60096 0.93853 1.03483 -0.09639 0.03136  0.22812  114 GLU A CB  
835  C CG  . GLU A 148 ? 0.84574 1.17558 1.27870 -0.10684 0.04018  0.23315  114 GLU A CG  
836  C CD  . GLU A 148 ? 1.00473 1.33772 1.43215 -0.09381 0.06154  0.23832  114 GLU A CD  
837  O OE1 . GLU A 148 ? 1.01775 1.37084 1.45642 -0.07913 0.06976  0.24042  114 GLU A OE1 
838  O OE2 . GLU A 148 ? 1.03002 1.34367 1.43988 -0.09769 0.06994  0.24000  114 GLU A OE2 
839  N N   . ASN A 149 ? 0.56359 0.89791 0.98560 -0.08456 0.00124  0.21255  115 ASN A N   
840  C CA  . ASN A 149 ? 0.58049 0.92492 1.00650 -0.07236 -0.00555 0.20967  115 ASN A CA  
841  C C   . ASN A 149 ? 0.55554 0.87356 0.95364 -0.07581 -0.02107 0.19867  115 ASN A C   
842  O O   . ASN A 149 ? 0.48161 0.77973 0.85233 -0.06423 -0.01823 0.19037  115 ASN A O   
843  C CB  . ASN A 149 ? 0.53242 0.87931 0.95097 -0.05117 0.00999  0.20881  115 ASN A CB  
844  C CG  . ASN A 149 ? 0.62610 0.99305 1.06423 -0.04722 0.02839  0.21862  115 ASN A CG  
845  O OD1 . ASN A 149 ? 0.64487 0.99733 1.06567 -0.04618 0.04068  0.21833  115 ASN A OD1 
846  N ND2 . ASN A 149 ? 0.66582 1.06069 1.13346 -0.04369 0.03003  0.22542  115 ASN A ND2 
847  N N   . PRO A 150 ? 0.54919 0.86641 0.95308 -0.09179 -0.03745 0.19831  116 PRO A N   
848  C CA  . PRO A 150 ? 0.46262 0.75357 0.83809 -0.09585 -0.05125 0.18796  116 PRO A CA  
849  C C   . PRO A 150 ? 0.50585 0.79950 0.87616 -0.08239 -0.05668 0.18452  116 PRO A C   
850  O O   . PRO A 150 ? 0.51355 0.83299 0.90976 -0.07832 -0.06108 0.19104  116 PRO A O   
851  C CB  . PRO A 150 ? 0.54796 0.84313 0.93617 -0.11596 -0.06737 0.19021  116 PRO A CB  
852  C CG  . PRO A 150 ? 0.50543 0.83674 0.93464 -0.11860 -0.06544 0.20205  116 PRO A CG  
853  C CD  . PRO A 150 ? 0.49952 0.84031 0.93648 -0.10739 -0.04420 0.20741  116 PRO A CD  
854  N N   . PRO A 151 ? 0.47567 0.74332 0.81374 -0.07507 -0.05627 0.17476  117 PRO A N   
855  C CA  . PRO A 151 ? 0.48164 0.74846 0.81256 -0.06357 -0.06183 0.17142  117 PRO A CA  
856  C C   . PRO A 151 ? 0.43105 0.68770 0.75149 -0.07365 -0.08022 0.16746  117 PRO A C   
857  O O   . PRO A 151 ? 0.42662 0.67567 0.74388 -0.08939 -0.08866 0.16630  117 PRO A O   
858  C CB  . PRO A 151 ? 0.48633 0.73012 0.78809 -0.05199 -0.05109 0.16312  117 PRO A CB  
859  C CG  . PRO A 151 ? 0.41191 0.63505 0.69590 -0.06280 -0.04943 0.15861  117 PRO A CG  
860  C CD  . PRO A 151 ? 0.52516 0.76423 0.83331 -0.07539 -0.04914 0.16701  117 PRO A CD  
861  N N   . ASP A 152 ? 0.41966 0.67410 0.73264 -0.06472 -0.08643 0.16523  118 ASP A N   
862  C CA  . ASP A 152 ? 0.50837 0.74984 0.80591 -0.07321 -0.10304 0.16108  118 ASP A CA  
863  C C   . ASP A 152 ? 0.44849 0.65689 0.70903 -0.07523 -0.10152 0.15006  118 ASP A C   
864  O O   . ASP A 152 ? 0.49452 0.68778 0.73987 -0.08780 -0.11159 0.14565  118 ASP A O   
865  C CB  . ASP A 152 ? 0.42466 0.67652 0.72893 -0.06315 -0.11061 0.16428  118 ASP A CB  
866  C CG  . ASP A 152 ? 0.47211 0.75840 0.81510 -0.06172 -0.11440 0.17549  118 ASP A CG  
867  O OD1 . ASP A 152 ? 0.46157 0.76032 0.82104 -0.07589 -0.12454 0.17982  118 ASP A OD1 
868  O OD2 . ASP A 152 ? 0.45226 0.75323 0.80979 -0.04645 -0.10698 0.17986  118 ASP A OD2 
869  N N   . VAL A 153 ? 0.49054 0.68765 0.73645 -0.06298 -0.08902 0.14536  119 VAL A N   
870  C CA  . VAL A 153 ? 0.49376 0.66248 0.70754 -0.06316 -0.08654 0.13529  119 VAL A CA  
871  C C   . VAL A 153 ? 0.48387 0.64648 0.69214 -0.05676 -0.07111 0.13282  119 VAL A C   
872  O O   . VAL A 153 ? 0.34855 0.52564 0.57141 -0.04700 -0.06122 0.13742  119 VAL A O   
873  C CB  . VAL A 153 ? 0.43701 0.59541 0.63438 -0.05454 -0.08990 0.13113  119 VAL A CB  
874  C CG1 . VAL A 153 ? 0.44980 0.58090 0.61616 -0.05641 -0.08783 0.12109  119 VAL A CG1 
875  C CG2 . VAL A 153 ? 0.44554 0.61143 0.64897 -0.05931 -0.10537 0.13519  119 VAL A CG2 
876  N N   . PHE A 154 ? 0.39438 0.53501 0.58060 -0.06178 -0.06910 0.12554  120 PHE A N   
877  C CA  . PHE A 154 ? 0.46501 0.59679 0.64221 -0.05593 -0.05621 0.12257  120 PHE A CA  
878  C C   . PHE A 154 ? 0.37636 0.48682 0.52716 -0.05082 -0.05454 0.11303  120 PHE A C   
879  O O   . PHE A 154 ? 0.40967 0.50365 0.54396 -0.05846 -0.06054 0.10732  120 PHE A O   
880  C CB  . PHE A 154 ? 0.44780 0.57424 0.62635 -0.06674 -0.05449 0.12391  120 PHE A CB  
881  C CG  . PHE A 154 ? 0.47455 0.59224 0.64418 -0.06056 -0.04187 0.12223  120 PHE A CG  
882  C CD1 . PHE A 154 ? 0.54647 0.67463 0.72217 -0.04785 -0.03132 0.12504  120 PHE A CD1 
883  C CD2 . PHE A 154 ? 0.58655 0.68491 0.74103 -0.06705 -0.04077 0.11801  120 PHE A CD2 
884  C CE1 . PHE A 154 ? 0.55027 0.67006 0.71599 -0.04206 -0.02067 0.12377  120 PHE A CE1 
885  C CE2 . PHE A 154 ? 0.63105 0.72147 0.77718 -0.06073 -0.03003 0.11722  120 PHE A CE2 
886  C CZ  . PHE A 154 ? 0.61169 0.71312 0.76309 -0.04845 -0.02037 0.12022  120 PHE A CZ  
887  N N   . ILE A 155 ? 0.41973 0.53049 0.56660 -0.03818 -0.04614 0.11117  121 ILE A N   
888  C CA  . ILE A 155 ? 0.37826 0.47147 0.50323 -0.03303 -0.04372 0.10259  121 ILE A CA  
889  C C   . ILE A 155 ? 0.43453 0.52196 0.55301 -0.02780 -0.03326 0.10035  121 ILE A C   
890  O O   . ILE A 155 ? 0.41943 0.51730 0.54695 -0.01990 -0.02549 0.10428  121 ILE A O   
891  C CB  . ILE A 155 ? 0.37847 0.47441 0.50230 -0.02339 -0.04417 0.10160  121 ILE A CB  
892  C CG1 . ILE A 155 ? 0.35150 0.44929 0.47728 -0.02880 -0.05570 0.10353  121 ILE A CG1 
893  C CG2 . ILE A 155 ? 0.30776 0.38806 0.41218 -0.01766 -0.03967 0.09332  121 ILE A CG2 
894  C CD1 . ILE A 155 ? 0.35192 0.45416 0.48051 -0.01921 -0.05672 0.10500  121 ILE A CD1 
895  N N   . SER A 156 ? 0.36834 0.43895 0.47053 -0.03160 -0.03293 0.09421  122 SER A N   
896  C CA  . SER A 156 ? 0.37444 0.43863 0.46996 -0.02722 -0.02451 0.09263  122 SER A CA  
897  C C   . SER A 156 ? 0.41347 0.46251 0.49046 -0.02338 -0.02340 0.08386  122 SER A C   
898  O O   . SER A 156 ? 0.39891 0.43805 0.46617 -0.02840 -0.02871 0.07883  122 SER A O   
899  C CB  . SER A 156 ? 0.47571 0.53542 0.57357 -0.03619 -0.02422 0.09573  122 SER A CB  
900  O OG  . SER A 156 ? 0.53351 0.57854 0.62007 -0.04511 -0.03081 0.09063  122 SER A OG  
901  N N   . ASP A 157 ? 0.35974 0.40764 0.43199 -0.01445 -0.01631 0.08229  123 ASP A N   
902  C CA  . ASP A 157 ? 0.37278 0.40875 0.43030 -0.01056 -0.01495 0.07458  123 ASP A CA  
903  C C   . ASP A 157 ? 0.45887 0.48149 0.50790 -0.01745 -0.01658 0.07148  123 ASP A C   
904  O O   . ASP A 157 ? 0.42643 0.44702 0.47904 -0.02305 -0.01629 0.07558  123 ASP A O   
905  C CB  . ASP A 157 ? 0.36253 0.40025 0.41704 -0.00054 -0.00806 0.07451  123 ASP A CB  
906  C CG  . ASP A 157 ? 0.42433 0.45291 0.46641 0.00402  -0.00764 0.06677  123 ASP A CG  
907  O OD1 . ASP A 157 ? 0.44899 0.46840 0.48450 0.00218  -0.00720 0.06441  123 ASP A OD1 
908  O OD2 . ASP A 157 ? 0.41766 0.44826 0.45730 0.00942  -0.00785 0.06310  123 ASP A OD2 
909  N N   . ILE A 158 ? 0.51144 0.52441 0.54923 -0.01693 -0.01779 0.06412  124 ILE A N   
910  C CA  . ILE A 158 ? 0.55306 0.55206 0.58116 -0.02171 -0.01838 0.05987  124 ILE A CA  
911  C C   . ILE A 158 ? 0.56071 0.55451 0.58828 -0.02023 -0.01421 0.06254  124 ILE A C   
912  O O   . ILE A 158 ? 0.56315 0.54557 0.58614 -0.02635 -0.01523 0.06198  124 ILE A O   
913  C CB  . ILE A 158 ? 0.66768 0.66043 0.68596 -0.01792 -0.01735 0.05198  124 ILE A CB  
914  C CG1 . ILE A 158 ? 0.63231 0.63283 0.65265 -0.00841 -0.01429 0.05082  124 ILE A CG1 
915  C CG2 . ILE A 158 ? 0.71624 0.70592 0.72965 -0.02373 -0.02174 0.04882  124 ILE A CG2 
916  C CD1 . ILE A 158 ? 0.82795 0.82376 0.84136 -0.00461 -0.01266 0.04368  124 ILE A CD1 
917  N N   . ILE A 159 ? 0.53936 0.53961 0.56989 -0.01206 -0.00948 0.06550  125 ILE A N   
918  C CA  . ILE A 159 ? 0.50637 0.49970 0.53318 -0.00897 -0.00522 0.06779  125 ILE A CA  
919  C C   . ILE A 159 ? 0.51521 0.50694 0.54815 -0.01668 -0.00484 0.07494  125 ILE A C   
920  O O   . ILE A 159 ? 0.53795 0.51697 0.56553 -0.01925 -0.00362 0.07559  125 ILE A O   
921  C CB  . ILE A 159 ? 0.53054 0.53073 0.55643 0.00184  -0.00082 0.06909  125 ILE A CB  
922  C CG1 . ILE A 159 ? 0.50288 0.50108 0.52169 0.00809  -0.00190 0.06120  125 ILE A CG1 
923  C CG2 . ILE A 159 ? 0.49265 0.48741 0.51550 0.00472  0.00373  0.07444  125 ILE A CG2 
924  C CD1 . ILE A 159 ? 0.64170 0.64612 0.65816 0.01791  0.00043  0.06095  125 ILE A CD1 
925  N N   . PHE A 160 ? 0.51849 0.52288 0.56353 -0.02065 -0.00593 0.08054  126 PHE A N   
926  C CA  . PHE A 160 ? 0.53015 0.53622 0.58444 -0.02898 -0.00563 0.08807  126 PHE A CA  
927  C C   . PHE A 160 ? 0.69409 0.68812 0.74494 -0.04055 -0.01207 0.08518  126 PHE A C   
928  O O   . PHE A 160 ? 0.60869 0.60866 0.66655 -0.04837 -0.01824 0.08596  126 PHE A O   
929  C CB  . PHE A 160 ? 0.51137 0.53688 0.58193 -0.02948 -0.00521 0.09464  126 PHE A CB  
930  C CG  . PHE A 160 ? 0.50853 0.54429 0.58058 -0.01789 0.00173  0.09704  126 PHE A CG  
931  C CD1 . PHE A 160 ? 0.53710 0.57498 0.61090 -0.01480 0.00932  0.10376  126 PHE A CD1 
932  C CD2 . PHE A 160 ? 0.41993 0.46162 0.49001 -0.01030 0.00085  0.09256  126 PHE A CD2 
933  C CE1 . PHE A 160 ? 0.45723 0.50305 0.52950 -0.00394 0.01586  0.10550  126 PHE A CE1 
934  C CE2 . PHE A 160 ? 0.41621 0.46505 0.48544 0.00023  0.00690  0.09385  126 PHE A CE2 
935  C CZ  . PHE A 160 ? 0.51094 0.56194 0.58061 0.00368  0.01442  0.10009  126 PHE A CZ  
936  N N   . THR A 161 ? 0.70008 0.67596 0.73901 -0.04126 -0.01088 0.08177  127 THR A N   
937  C CA  . THR A 161 ? 0.65945 0.61999 0.69103 -0.05122 -0.01634 0.07745  127 THR A CA  
938  C C   . THR A 161 ? 0.66552 0.62674 0.70678 -0.06378 -0.01992 0.08367  127 THR A C   
939  O O   . THR A 161 ? 0.85409 0.80747 0.89190 -0.07388 -0.02693 0.08055  127 THR A O   
940  C CB  . THR A 161 ? 0.64278 0.58292 0.65975 -0.04760 -0.01319 0.07256  127 THR A CB  
941  O OG1 . THR A 161 ? 0.87505 0.81032 0.89375 -0.04617 -0.00813 0.07912  127 THR A OG1 
942  C CG2 . THR A 161 ? 0.71336 0.65495 0.72323 -0.03594 -0.01038 0.06636  127 THR A CG2 
943  N N   . TRP A 162 ? 0.68414 0.65462 0.73718 -0.06383 -0.01527 0.09249  128 TRP A N   
944  C CA  . TRP A 162 ? 0.67082 0.64445 0.73627 -0.07659 -0.01825 0.09925  128 TRP A CA  
945  C C   . TRP A 162 ? 0.65967 0.65283 0.74055 -0.08241 -0.02501 0.10172  128 TRP A C   
946  O O   . TRP A 162 ? 0.70030 0.69766 0.79295 -0.09447 -0.02976 0.10654  128 TRP A O   
947  C CB  . TRP A 162 ? 0.64541 0.62447 0.71959 -0.07468 -0.00983 0.10880  128 TRP A CB  
948  C CG  . TRP A 162 ? 0.73513 0.73244 0.81554 -0.06238 -0.00298 0.11238  128 TRP A CG  
949  C CD1 . TRP A 162 ? 0.63606 0.62934 0.70556 -0.04969 0.00371  0.11106  128 TRP A CD1 
950  C CD2 . TRP A 162 ? 0.70068 0.72232 0.79892 -0.06128 -0.00240 0.11763  128 TRP A CD2 
951  N NE1 . TRP A 162 ? 0.57023 0.58219 0.64768 -0.04126 0.00837  0.11451  128 TRP A NE1 
952  C CE2 . TRP A 162 ? 0.60442 0.63375 0.69970 -0.04763 0.00539  0.11860  128 TRP A CE2 
953  C CE3 . TRP A 162 ? 0.65287 0.69056 0.76936 -0.07006 -0.00808 0.12156  128 TRP A CE3 
954  C CZ2 . TRP A 162 ? 0.54128 0.59199 0.65007 -0.04208 0.00868  0.12289  128 TRP A CZ2 
955  C CZ3 . TRP A 162 ? 0.62693 0.68781 0.75907 -0.06404 -0.00492 0.12652  128 TRP A CZ3 
956  C CH2 . TRP A 162 ? 0.59186 0.65823 0.71953 -0.04996 0.00391  0.12694  128 TRP A CH2 
957  N N   . SER A 163 ? 0.61416 0.61915 0.69582 -0.07428 -0.02596 0.09885  129 SER A N   
958  C CA  . SER A 163 ? 0.54936 0.57341 0.64629 -0.07782 -0.03213 0.10217  129 SER A CA  
959  C C   . SER A 163 ? 0.65093 0.66753 0.74440 -0.09044 -0.04360 0.09881  129 SER A C   
960  O O   . SER A 163 ? 0.57553 0.60679 0.68469 -0.09776 -0.05041 0.10378  129 SER A O   
961  C CB  . SER A 163 ? 0.60511 0.63882 0.70037 -0.06603 -0.03069 0.09921  129 SER A CB  
962  O OG  . SER A 163 ? 0.67496 0.69399 0.75196 -0.06424 -0.03387 0.09002  129 SER A OG  
963  N N   . GLU A 164 ? 0.50557 0.49981 0.57849 -0.09276 -0.04596 0.09042  130 GLU A N   
964  C CA  . GLU A 164 ? 0.63657 0.62037 0.70168 -0.10466 -0.05663 0.08628  130 GLU A CA  
965  C C   . GLU A 164 ? 0.74560 0.72865 0.82145 -0.11862 -0.06139 0.09159  130 GLU A C   
966  O O   . GLU A 164 ? 0.64378 0.63651 0.72970 -0.12844 -0.07136 0.09427  130 GLU A O   
967  C CB  . GLU A 164 ? 0.69235 0.65101 0.73226 -0.10308 -0.05567 0.07612  130 GLU A CB  
968  C CG  . GLU A 164 ? 0.77808 0.72016 0.80468 -0.11550 -0.06537 0.07077  130 GLU A CG  
969  C CD  . GLU A 164 ? 0.91490 0.83686 0.91684 -0.11137 -0.06369 0.06041  130 GLU A CD  
970  O OE1 . GLU A 164 ? 1.04325 0.96023 1.03928 -0.10056 -0.05447 0.05746  130 GLU A OE1 
971  O OE2 . GLU A 164 ? 1.05484 0.96654 1.04335 -0.11882 -0.07155 0.05537  130 GLU A OE2 
972  N N   . SER A 165 ? 0.75305 0.72476 0.82745 -0.11994 -0.05475 0.09362  131 SER A N   
973  C CA  . SER A 165 ? 0.66842 0.63832 0.75369 -0.13408 -0.05841 0.09921  131 SER A CA  
974  C C   . SER A 165 ? 0.70828 0.70772 0.82249 -0.13662 -0.05828 0.11011  131 SER A C   
975  O O   . SER A 165 ? 0.76795 0.77407 0.89622 -0.15040 -0.06592 0.11456  131 SER A O   
976  C CB  . SER A 165 ? 0.78078 0.73043 0.85706 -0.13371 -0.05020 0.09974  131 SER A CB  
977  O OG  . SER A 165 ? 0.89911 0.85778 0.97980 -0.12058 -0.03867 0.10438  131 SER A OG  
978  N N   . THR A 166 ? 0.71580 0.73337 0.83950 -0.12356 -0.04976 0.11432  132 THR A N   
979  C CA  . THR A 166 ? 0.69938 0.74598 0.85067 -0.12390 -0.04809 0.12445  132 THR A CA  
980  C C   . THR A 166 ? 0.68367 0.74681 0.84682 -0.12859 -0.05993 0.12483  132 THR A C   
981  O O   . THR A 166 ? 0.74562 0.82830 0.93262 -0.13707 -0.06436 0.13255  132 THR A O   
982  C CB  . THR A 166 ? 0.62512 0.68383 0.77938 -0.10754 -0.03598 0.12737  132 THR A CB  
983  O OG1 . THR A 166 ? 0.72891 0.77414 0.87395 -0.10404 -0.02575 0.12889  132 THR A OG1 
984  C CG2 . THR A 166 ? 0.58289 0.67200 0.76487 -0.10588 -0.03334 0.13706  132 THR A CG2 
985  N N   . ALA A 167 ? 0.66881 0.72490 0.81614 -0.12325 -0.06527 0.11709  133 ALA A N   
986  C CA  . ALA A 167 ? 0.66622 0.73572 0.82173 -0.12682 -0.07709 0.11768  133 ALA A CA  
987  C C   . ALA A 167 ? 0.68475 0.74615 0.83897 -0.14416 -0.09054 0.11639  133 ALA A C   
988  O O   . ALA A 167 ? 0.72830 0.80787 0.90018 -0.15093 -0.10077 0.12131  133 ALA A O   
989  C CB  . ALA A 167 ? 0.63026 0.69177 0.76679 -0.11687 -0.07836 0.11014  133 ALA A CB  
990  N N   . LYS A 168 ? 0.64508 0.67908 0.77837 -0.15119 -0.09118 0.10966  134 LYS A N   
991  C CA  . LYS A 168 ? 0.74098 0.76373 0.87010 -0.16828 -0.10403 0.10741  134 LYS A CA  
992  C C   . LYS A 168 ? 0.79783 0.83644 0.95429 -0.18038 -0.10615 0.11695  134 LYS A C   
993  O O   . LYS A 168 ? 0.73932 0.79114 0.91033 -0.19179 -0.11894 0.12030  134 LYS A O   
994  C CB  . LYS A 168 ? 0.82448 0.81217 0.92402 -0.17158 -0.10241 0.09767  134 LYS A CB  
995  C CG  . LYS A 168 ? 0.92395 0.89532 1.01617 -0.18973 -0.11482 0.09445  134 LYS A CG  
996  C CD  . LYS A 168 ? 1.12488 1.06022 1.18871 -0.19142 -0.11081 0.08522  134 LYS A CD  
997  C CE  . LYS A 168 ? 1.15217 1.06836 1.20680 -0.20990 -0.12319 0.08130  134 LYS A CE  
998  N NZ  . LYS A 168 ? 1.22658 1.10569 1.25291 -0.21055 -0.11853 0.07204  134 LYS A NZ  
999  N N   . ASN A 169 ? 0.86339 0.90167 1.02762 -0.17818 -0.09379 0.12193  135 ASN A N   
1000 C CA  . ASN A 169 ? 0.89347 0.94575 1.08355 -0.19017 -0.09367 0.13164  135 ASN A CA  
1001 C C   . ASN A 169 ? 0.83442 0.92487 1.05787 -0.18844 -0.09536 0.14154  135 ASN A C   
1002 O O   . ASN A 169 ? 0.99684 1.10345 1.24532 -0.20124 -0.09972 0.14936  135 ASN A O   
1003 C CB  . ASN A 169 ? 0.91885 0.96170 1.10745 -0.18615 -0.07844 0.13550  135 ASN A CB  
1004 C CG  . ASN A 169 ? 1.15279 1.15791 1.31104 -0.18799 -0.07681 0.12674  135 ASN A CG  
1005 O OD1 . ASN A 169 ? 1.24843 1.23375 1.39013 -0.19722 -0.08754 0.11878  135 ASN A OD1 
1006 N ND2 . ASN A 169 ? 1.17569 1.17023 1.32577 -0.17861 -0.06337 0.12820  135 ASN A ND2 
1007 N N   . LEU A 170 ? 0.75734 0.86241 0.98249 -0.17300 -0.09187 0.14149  136 LEU A N   
1008 C CA  . LEU A 170 ? 0.66741 0.80733 0.92257 -0.16919 -0.09379 0.15005  136 LEU A CA  
1009 C C   . LEU A 170 ? 0.72298 0.86933 0.97703 -0.17096 -0.10962 0.14705  136 LEU A C   
1010 O O   . LEU A 170 ? 0.73016 0.90497 1.00868 -0.16685 -0.11286 0.15394  136 LEU A O   
1011 C CB  . LEU A 170 ? 0.80633 0.95854 1.06541 -0.15009 -0.07871 0.15295  136 LEU A CB  
1012 C CG  . LEU A 170 ? 0.87315 1.04095 1.15286 -0.14807 -0.06442 0.16267  136 LEU A CG  
1013 C CD1 . LEU A 170 ? 0.73052 0.87245 0.98908 -0.14726 -0.05371 0.15974  136 LEU A CD1 
1014 C CD2 . LEU A 170 ? 0.77386 0.96477 1.06688 -0.13097 -0.05475 0.16723  136 LEU A CD2 
1015 N N   . GLN A 171 ? 0.72528 0.84556 0.95098 -0.17629 -0.11908 0.13725  137 GLN A N   
1016 C CA  . GLN A 171 ? 0.71891 0.84045 0.93761 -0.17884 -0.13466 0.13390  137 GLN A CA  
1017 C C   . GLN A 171 ? 0.67821 0.81853 0.90458 -0.16264 -0.13207 0.13677  137 GLN A C   
1018 O O   . GLN A 171 ? 0.68454 0.84890 0.93222 -0.16278 -0.14096 0.14315  137 GLN A O   
1019 C CB  . GLN A 171 ? 0.74149 0.87697 0.98029 -0.19619 -0.15064 0.13889  137 GLN A CB  
1020 C CG  . GLN A 171 ? 0.80618 0.91457 1.02676 -0.21357 -0.15858 0.13244  137 GLN A CG  
1021 C CD  . GLN A 171 ? 0.95919 1.07728 1.19173 -0.22565 -0.17250 0.13435  137 GLN A CD  
1022 O OE1 . GLN A 171 ? 0.86048 1.00901 1.12260 -0.22318 -0.17390 0.14284  137 GLN A OE1 
1023 N NE2 . GLN A 171 ? 1.02094 1.11198 1.22865 -0.23705 -0.18179 0.12570  137 GLN A NE2 
1024 N N   . ILE A 172 ? 0.82772 0.95604 1.03641 -0.14847 -0.11995 0.13193  138 ILE A N   
1025 C CA  . ILE A 172 ? 0.84872 0.98992 1.06120 -0.13239 -0.11544 0.13357  138 ILE A CA  
1026 C C   . ILE A 172 ? 0.78448 0.90085 0.96421 -0.12481 -0.11302 0.12360  138 ILE A C   
1027 O O   . ILE A 172 ? 0.70546 0.80068 0.86611 -0.12463 -0.10540 0.11726  138 ILE A O   
1028 C CB  . ILE A 172 ? 0.73467 0.89350 0.96674 -0.12131 -0.09998 0.14010  138 ILE A CB  
1029 C CG1 . ILE A 172 ? 0.80028 0.97245 1.03760 -0.10516 -0.09635 0.14189  138 ILE A CG1 
1030 C CG2 . ILE A 172 ? 0.66765 0.80661 0.88219 -0.11784 -0.08678 0.13539  138 ILE A CG2 
1031 C CD1 . ILE A 172 ? 0.76155 0.95472 1.02114 -0.09492 -0.08305 0.14923  138 ILE A CD1 
1032 N N   . PRO A 173 ? 0.66111 0.77921 0.83396 -0.11854 -0.11914 0.12232  139 PRO A N   
1033 C CA  . PRO A 173 ? 0.52939 0.62521 0.67270 -0.11181 -0.11579 0.11346  139 PRO A CA  
1034 C C   . PRO A 173 ? 0.56870 0.66173 0.70886 -0.09882 -0.09987 0.11143  139 PRO A C   
1035 O O   . PRO A 173 ? 0.45751 0.56860 0.61653 -0.08982 -0.09261 0.11726  139 PRO A O   
1036 C CB  . PRO A 173 ? 0.59974 0.70287 0.74251 -0.10727 -0.12499 0.11548  139 PRO A CB  
1037 C CG  . PRO A 173 ? 0.60692 0.73982 0.78281 -0.10522 -0.12817 0.12593  139 PRO A CG  
1038 C CD  . PRO A 173 ? 0.72260 0.86298 0.91477 -0.11740 -0.12955 0.12943  139 PRO A CD  
1039 N N   . ARG A 174 ? 0.47706 0.54724 0.59279 -0.09769 -0.09457 0.10292  140 ARG A N   
1040 C CA  . ARG A 174 ? 0.57552 0.64111 0.68558 -0.08616 -0.08116 0.10000  140 ARG A CA  
1041 C C   . ARG A 174 ? 0.55954 0.60949 0.64681 -0.08062 -0.08014 0.09219  140 ARG A C   
1042 O O   . ARG A 174 ? 0.53700 0.56993 0.60533 -0.08743 -0.08525 0.08629  140 ARG A O   
1043 C CB  . ARG A 174 ? 0.48050 0.53510 0.58642 -0.08957 -0.07392 0.09816  140 ARG A CB  
1044 C CG  . ARG A 174 ? 0.54246 0.59087 0.64016 -0.07800 -0.06161 0.09474  140 ARG A CG  
1045 C CD  . ARG A 174 ? 0.65188 0.68271 0.73825 -0.08197 -0.05707 0.09113  140 ARG A CD  
1046 N NE  . ARG A 174 ? 0.72435 0.73441 0.78973 -0.08811 -0.06229 0.08307  140 ARG A NE  
1047 C CZ  . ARG A 174 ? 0.75196 0.74520 0.79937 -0.08332 -0.05679 0.07571  140 ARG A CZ  
1048 N NH1 . ARG A 174 ? 0.65429 0.64849 0.70179 -0.07299 -0.04724 0.07531  140 ARG A NH1 
1049 N NH2 . ARG A 174 ? 0.65275 0.62801 0.68155 -0.08887 -0.06102 0.06862  140 ARG A NH2 
1050 N N   . LEU A 175 ? 0.51301 0.56833 0.60184 -0.06859 -0.07321 0.09210  141 LEU A N   
1051 C CA  . LEU A 175 ? 0.45584 0.49764 0.52562 -0.06293 -0.07008 0.08504  141 LEU A CA  
1052 C C   . LEU A 175 ? 0.46379 0.50225 0.53088 -0.05439 -0.05850 0.08182  141 LEU A C   
1053 O O   . LEU A 175 ? 0.45111 0.50155 0.53197 -0.04834 -0.05265 0.08627  141 LEU A O   
1054 C CB  . LEU A 175 ? 0.51383 0.56247 0.58578 -0.05682 -0.07351 0.08726  141 LEU A CB  
1055 C CG  . LEU A 175 ? 0.46071 0.50671 0.52656 -0.06412 -0.08566 0.08862  141 LEU A CG  
1056 C CD1 . LEU A 175 ? 0.43691 0.50094 0.52396 -0.06858 -0.09394 0.09700  141 LEU A CD1 
1057 C CD2 . LEU A 175 ? 0.42154 0.46401 0.47890 -0.05745 -0.08642 0.08786  141 LEU A CD2 
1058 N N   . VAL A 176 ? 0.42122 0.44392 0.47054 -0.05378 -0.05533 0.07429  142 VAL A N   
1059 C CA  . VAL A 176 ? 0.46777 0.48632 0.51279 -0.04591 -0.04595 0.07046  142 VAL A CA  
1060 C C   . VAL A 176 ? 0.41041 0.43268 0.45430 -0.03682 -0.04307 0.06876  142 VAL A C   
1061 O O   . VAL A 176 ? 0.37807 0.39736 0.41580 -0.03801 -0.04737 0.06739  142 VAL A O   
1062 C CB  . VAL A 176 ? 0.57109 0.57196 0.59946 -0.04955 -0.04420 0.06327  142 VAL A CB  
1063 C CG1 . VAL A 176 ? 0.60884 0.60575 0.63062 -0.04096 -0.03691 0.05802  142 VAL A CG1 
1064 C CG2 . VAL A 176 ? 0.57709 0.57276 0.60740 -0.05536 -0.04376 0.06490  142 VAL A CG2 
1065 N N   . PHE A 177 ? 0.37725 0.40485 0.42589 -0.02798 -0.03608 0.06899  143 PHE A N   
1066 C CA  . PHE A 177 ? 0.33643 0.36553 0.38294 -0.01971 -0.03339 0.06651  143 PHE A CA  
1067 C C   . PHE A 177 ? 0.39018 0.41046 0.42608 -0.01611 -0.02837 0.05956  143 PHE A C   
1068 O O   . PHE A 177 ? 0.37039 0.39062 0.40685 -0.01295 -0.02381 0.05929  143 PHE A O   
1069 C CB  . PHE A 177 ? 0.27412 0.31604 0.33314 -0.01169 -0.02994 0.07156  143 PHE A CB  
1070 C CG  . PHE A 177 ? 0.40474 0.44559 0.45985 -0.00305 -0.02702 0.06818  143 PHE A CG  
1071 C CD1 . PHE A 177 ? 0.34796 0.38603 0.40027 -0.00290 -0.03107 0.06735  143 PHE A CD1 
1072 C CD2 . PHE A 177 ? 0.36545 0.40661 0.41836 0.00458  -0.02072 0.06584  143 PHE A CD2 
1073 C CE1 . PHE A 177 ? 0.45580 0.49081 0.50409 0.00416  -0.02861 0.06405  143 PHE A CE1 
1074 C CE2 . PHE A 177 ? 0.43790 0.47666 0.48623 0.01163  -0.01893 0.06202  143 PHE A CE2 
1075 C CZ  . PHE A 177 ? 0.39040 0.42571 0.43680 0.01115  -0.02274 0.06097  143 PHE A CZ  
1076 N N   . ASN A 178 ? 0.37964 0.39302 0.40646 -0.01661 -0.02931 0.05450  144 ASN A N   
1077 C CA  . ASN A 178 ? 0.31222 0.31973 0.33158 -0.01344 -0.02509 0.04794  144 ASN A CA  
1078 C C   . ASN A 178 ? 0.43933 0.45041 0.46030 -0.00649 -0.02343 0.04644  144 ASN A C   
1079 O O   . ASN A 178 ? 0.42302 0.43230 0.44207 -0.00760 -0.02594 0.04635  144 ASN A O   
1080 C CB  . ASN A 178 ? 0.40668 0.40419 0.41524 -0.01962 -0.02621 0.04321  144 ASN A CB  
1081 C CG  . ASN A 178 ? 0.45694 0.45072 0.46071 -0.01656 -0.02146 0.03671  144 ASN A CG  
1082 O OD1 . ASN A 178 ? 0.47729 0.47537 0.48511 -0.01013 -0.01850 0.03563  144 ASN A OD1 
1083 N ND2 . ASN A 178 ? 0.50576 0.49201 0.50081 -0.02111 -0.02074 0.03256  144 ASN A ND2 
1084 N N   . PRO A 179 ? 0.33364 0.34817 0.35656 0.00056  -0.01964 0.04518  145 PRO A N   
1085 C CA  . PRO A 179 ? 0.29932 0.31618 0.32290 0.00713  -0.01869 0.04373  145 PRO A CA  
1086 C C   . PRO A 179 ? 0.34325 0.35470 0.36091 0.00668  -0.01877 0.03719  145 PRO A C   
1087 O O   . PRO A 179 ? 0.34571 0.35711 0.36276 0.01137  -0.01848 0.03507  145 PRO A O   
1088 C CB  . PRO A 179 ? 0.37218 0.39373 0.39764 0.01421  -0.01490 0.04482  145 PRO A CB  
1089 C CG  . PRO A 179 ? 0.37053 0.38928 0.39365 0.01161  -0.01370 0.04390  145 PRO A CG  
1090 C CD  . PRO A 179 ? 0.34763 0.36283 0.37098 0.00296  -0.01646 0.04556  145 PRO A CD  
1091 N N   . ILE A 180 ? 0.31629 0.32299 0.32964 0.00104  -0.01882 0.03385  146 ILE A N   
1092 C CA  . ILE A 180 ? 0.32155 0.32484 0.33139 -0.00054 -0.01811 0.02822  146 ILE A CA  
1093 C C   . ILE A 180 ? 0.40911 0.40618 0.41352 -0.00836 -0.01895 0.02806  146 ILE A C   
1094 O O   . ILE A 180 ? 0.33938 0.33435 0.34184 -0.01223 -0.02121 0.03194  146 ILE A O   
1095 C CB  . ILE A 180 ? 0.31994 0.32544 0.33044 0.00217  -0.01560 0.02348  146 ILE A CB  
1096 C CG1 . ILE A 180 ? 0.38304 0.38612 0.39177 -0.00062 -0.01395 0.02365  146 ILE A CG1 
1097 C CG2 . ILE A 180 ? 0.32708 0.33746 0.33994 0.01007  -0.01535 0.02383  146 ILE A CG2 
1098 C CD1 . ILE A 180 ? 0.45896 0.46397 0.46902 0.00266  -0.01146 0.01916  146 ILE A CD1 
1099 N N   . SER A 181 ? 0.33751 0.33181 0.33919 -0.01100 -0.01717 0.02361  147 SER A N   
1100 C CA  . SER A 181 ? 0.34744 0.33504 0.34183 -0.01821 -0.01655 0.02321  147 SER A CA  
1101 C C   . SER A 181 ? 0.39535 0.38020 0.38527 -0.02124 -0.01483 0.02238  147 SER A C   
1102 O O   . SER A 181 ? 0.39230 0.38022 0.38567 -0.01781 -0.01270 0.02038  147 SER A O   
1103 C CB  . SER A 181 ? 0.36107 0.34788 0.35531 -0.02038 -0.01346 0.01865  147 SER A CB  
1104 O OG  . SER A 181 ? 0.46336 0.44425 0.44984 -0.02699 -0.01072 0.01781  147 SER A OG  
1105 N N   . ILE A 182 ? 0.35281 0.33025 0.33343 -0.02755 -0.01602 0.02391  148 ILE A N   
1106 C CA  . ILE A 182 ? 0.36102 0.33260 0.33406 -0.03115 -0.01433 0.02211  148 ILE A CA  
1107 C C   . ILE A 182 ? 0.34413 0.31448 0.31493 -0.03129 -0.00749 0.01622  148 ILE A C   
1108 O O   . ILE A 182 ? 0.36252 0.32811 0.32824 -0.03193 -0.00462 0.01356  148 ILE A O   
1109 C CB  . ILE A 182 ? 0.36300 0.32609 0.32439 -0.03803 -0.01851 0.02523  148 ILE A CB  
1110 C CG1 . ILE A 182 ? 0.43596 0.39254 0.39025 -0.04135 -0.01940 0.02428  148 ILE A CG1 
1111 C CG2 . ILE A 182 ? 0.31202 0.26850 0.26303 -0.04255 -0.01558 0.02362  148 ILE A CG2 
1112 C CD1 . ILE A 182 ? 0.39302 0.35475 0.35677 -0.03873 -0.02258 0.02728  148 ILE A CD1 
1113 N N   . PHE A 183 ? 0.34852 0.32322 0.32392 -0.03052 -0.00457 0.01400  149 PHE A N   
1114 C CA  . PHE A 183 ? 0.39516 0.37214 0.37221 -0.03051 0.00243  0.00873  149 PHE A CA  
1115 C C   . PHE A 183 ? 0.35208 0.33415 0.33629 -0.02424 0.00461  0.00580  149 PHE A C   
1116 O O   . PHE A 183 ? 0.38558 0.36554 0.36714 -0.02409 0.01012  0.00225  149 PHE A O   
1117 C CB  . PHE A 183 ? 0.33683 0.32025 0.32184 -0.03077 0.00375  0.00734  149 PHE A CB  
1118 C CG  . PHE A 183 ? 0.36842 0.35992 0.36209 -0.02937 0.00986  0.00230  149 PHE A CG  
1119 C CD1 . PHE A 183 ? 0.31900 0.30824 0.30810 -0.03409 0.01691  0.00018  149 PHE A CD1 
1120 C CD2 . PHE A 183 ? 0.27124 0.27329 0.27772 -0.02316 0.00858  -0.00002 149 PHE A CD2 
1121 C CE1 . PHE A 183 ? 0.32776 0.32689 0.32764 -0.03248 0.02297  -0.00403 149 PHE A CE1 
1122 C CE2 . PHE A 183 ? 0.30236 0.31385 0.31893 -0.02166 0.01324  -0.00422 149 PHE A CE2 
1123 C CZ  . PHE A 183 ? 0.37606 0.38701 0.39073 -0.02626 0.02062  -0.00616 149 PHE A CZ  
1124 N N   . ASP A 184 ? 0.29570 0.28362 0.28791 -0.01868 0.00083  0.00745  150 ASP A N   
1125 C CA  . ASP A 184 ? 0.37473 0.36728 0.37348 -0.01187 0.00237  0.00544  150 ASP A CA  
1126 C C   . ASP A 184 ? 0.32848 0.31203 0.31977 -0.01222 0.00471  0.00491  150 ASP A C   
1127 O O   . ASP A 184 ? 0.39079 0.37486 0.38398 -0.00884 0.00943  0.00118  150 ASP A O   
1128 C CB  . ASP A 184 ? 0.32861 0.32676 0.33352 -0.00635 -0.00210 0.00823  150 ASP A CB  
1129 C CG  . ASP A 184 ? 0.47911 0.48436 0.49008 -0.00497 -0.00442 0.00743  150 ASP A CG  
1130 O OD1 . ASP A 184 ? 0.38978 0.39262 0.39825 -0.00997 -0.00499 0.00782  150 ASP A OD1 
1131 O OD2 . ASP A 184 ? 0.35450 0.36625 0.37132 0.00108  -0.00597 0.00645  150 ASP A OD2 
1132 N N   . VAL A 185 ? 0.33526 0.31094 0.31906 -0.01606 0.00120  0.00847  151 VAL A N   
1133 C CA  . VAL A 185 ? 0.36771 0.33215 0.34274 -0.01780 0.00237  0.00772  151 VAL A CA  
1134 C C   . VAL A 185 ? 0.43704 0.39414 0.40233 -0.02115 0.00799  0.00285  151 VAL A C   
1135 O O   . VAL A 185 ? 0.35927 0.30907 0.32004 -0.01893 0.01209  -0.00048 151 VAL A O   
1136 C CB  . VAL A 185 ? 0.41874 0.37727 0.38872 -0.02300 -0.00353 0.01253  151 VAL A CB  
1137 C CG1 . VAL A 185 ? 0.33583 0.29017 0.29708 -0.03051 -0.00660 0.01382  151 VAL A CG1 
1138 C CG2 . VAL A 185 ? 0.55397 0.50156 0.51795 -0.02393 -0.00326 0.01204  151 VAL A CG2 
1139 N N   . CYS A 186 ? 0.33311 0.29161 0.29505 -0.02571 0.00883  0.00262  152 CYS A N   
1140 C CA  . CYS A 186 ? 0.38493 0.33674 0.33661 -0.02887 0.01549  -0.00158 152 CYS A CA  
1141 C C   . CYS A 186 ? 0.39717 0.35664 0.35842 -0.02271 0.02313  -0.00619 152 CYS A C   
1142 O O   . CYS A 186 ? 0.39619 0.34897 0.35096 -0.02121 0.02957  -0.01031 152 CYS A O   
1143 C CB  . CYS A 186 ? 0.45424 0.40560 0.39999 -0.03521 0.01516  0.00017  152 CYS A CB  
1144 S SG  . CYS A 186 ? 0.42828 0.37096 0.36230 -0.04209 0.00574  0.00595  152 CYS A SG  
1145 N N   . MET A 187 ? 0.32004 0.29364 0.29679 -0.01892 0.02233  -0.00575 153 MET A N   
1146 C CA  . MET A 187 ? 0.39168 0.37561 0.38076 -0.01277 0.02797  -0.00959 153 MET A CA  
1147 C C   . MET A 187 ? 0.40269 0.38294 0.39282 -0.00536 0.02893  -0.01095 153 MET A C   
1148 O O   . MET A 187 ? 0.35112 0.33157 0.34307 -0.00108 0.03586  -0.01487 153 MET A O   
1149 C CB  . MET A 187 ? 0.35763 0.35643 0.36226 -0.01051 0.02426  -0.00867 153 MET A CB  
1150 C CG  . MET A 187 ? 0.37609 0.38847 0.39563 -0.00575 0.02893  -0.01240 153 MET A CG  
1151 S SD  . MET A 187 ? 0.38309 0.41106 0.41831 -0.00620 0.02362  -0.01214 153 MET A SD  
1152 C CE  . MET A 187 ? 0.41271 0.45641 0.46597 0.00288  0.02562  -0.01561 153 MET A CE  
1153 N N   . ILE A 188 ? 0.37129 0.34780 0.36046 -0.00349 0.02254  -0.00739 154 ILE A N   
1154 C CA  . ILE A 188 ? 0.41735 0.38749 0.40579 0.00284  0.02299  -0.00758 154 ILE A CA  
1155 C C   . ILE A 188 ? 0.41296 0.36689 0.38711 0.00061  0.02800  -0.01086 154 ILE A C   
1156 O O   . ILE A 188 ? 0.42127 0.37156 0.39604 0.00695  0.03345  -0.01427 154 ILE A O   
1157 C CB  . ILE A 188 ? 0.38101 0.34872 0.36913 0.00301  0.01590  -0.00221 154 ILE A CB  
1158 C CG1 . ILE A 188 ? 0.38030 0.36241 0.38103 0.00814  0.01213  -0.00002 154 ILE A CG1 
1159 C CG2 . ILE A 188 ? 0.37933 0.33457 0.36180 0.00633  0.01658  -0.00168 154 ILE A CG2 
1160 C CD1 . ILE A 188 ? 0.33256 0.31341 0.33278 0.00887  0.00669  0.00555  154 ILE A CD1 
1161 N N   . GLN A 189 ? 0.43522 0.37852 0.39556 -0.00804 0.02587  -0.01000 155 GLN A N   
1162 C CA  . GLN A 189 ? 0.46603 0.39164 0.40946 -0.01104 0.02962  -0.01366 155 GLN A CA  
1163 C C   . GLN A 189 ? 0.39536 0.32152 0.33648 -0.00851 0.03971  -0.01935 155 GLN A C   
1164 O O   . GLN A 189 ? 0.47331 0.38770 0.40614 -0.00493 0.04556  -0.02373 155 GLN A O   
1165 C CB  . GLN A 189 ? 0.50641 0.42226 0.43545 -0.02127 0.02401  -0.01145 155 GLN A CB  
1166 C CG  . GLN A 189 ? 0.50795 0.40306 0.41720 -0.02527 0.02538  -0.01518 155 GLN A CG  
1167 C CD  . GLN A 189 ? 0.57623 0.46512 0.47179 -0.02761 0.03301  -0.02018 155 GLN A CD  
1168 O OE1 . GLN A 189 ? 0.60569 0.50555 0.50585 -0.02875 0.03584  -0.01944 155 GLN A OE1 
1169 N NE2 . GLN A 189 ? 0.58334 0.45352 0.46109 -0.02839 0.03693  -0.02536 155 GLN A NE2 
1170 N N   . ALA A 190 ? 0.38434 0.32362 0.33284 -0.01025 0.04250  -0.01932 156 ALA A N   
1171 C CA  . ALA A 190 ? 0.45575 0.39807 0.40443 -0.00819 0.05328  -0.02409 156 ALA A CA  
1172 C C   . ALA A 190 ? 0.49253 0.44364 0.45641 0.00282  0.05837  -0.02681 156 ALA A C   
1173 O O   . ALA A 190 ? 0.46957 0.41622 0.42982 0.00716  0.06780  -0.03151 156 ALA A O   
1174 C CB  . ALA A 190 ? 0.36581 0.32092 0.32115 -0.01332 0.05494  -0.02261 156 ALA A CB  
1175 N N   . ILE A 191 ? 0.44316 0.40648 0.42344 0.00806  0.05228  -0.02385 157 ILE A N   
1176 C CA  . ILE A 191 ? 0.44721 0.41841 0.44148 0.01927  0.05513  -0.02550 157 ILE A CA  
1177 C C   . ILE A 191 ? 0.43283 0.38491 0.41501 0.02417  0.05700  -0.02723 157 ILE A C   
1178 O O   . ILE A 191 ? 0.47909 0.42883 0.46301 0.03192  0.06484  -0.03121 157 ILE A O   
1179 C CB  . ILE A 191 ? 0.40071 0.38656 0.41105 0.02326  0.04673  -0.02151 157 ILE A CB  
1180 C CG1 . ILE A 191 ? 0.32472 0.32900 0.34820 0.01926  0.04552  -0.02109 157 ILE A CG1 
1181 C CG2 . ILE A 191 ? 0.44048 0.43103 0.46191 0.03537  0.04759  -0.02212 157 ILE A CG2 
1182 C CD1 . ILE A 191 ? 0.33428 0.34899 0.36786 0.02104  0.03602  -0.01749 157 ILE A CD1 
1183 N N   . GLN A 192 ? 0.45341 0.39139 0.42383 0.01969  0.04996  -0.02416 158 GLN A N   
1184 C CA  . GLN A 192 ? 0.49716 0.41490 0.45567 0.02279  0.05060  -0.02536 158 GLN A CA  
1185 C C   . GLN A 192 ? 0.53559 0.43709 0.47750 0.02154  0.05919  -0.03166 158 GLN A C   
1186 O O   . GLN A 192 ? 0.64419 0.53302 0.58129 0.02885  0.06427  -0.03508 158 GLN A O   
1187 C CB  . GLN A 192 ? 0.50811 0.41505 0.45767 0.01542  0.04161  -0.02068 158 GLN A CB  
1188 C CG  . GLN A 192 ? 0.54328 0.46114 0.50603 0.01901  0.03471  -0.01461 158 GLN A CG  
1189 C CD  . GLN A 192 ? 0.76839 0.67126 0.72323 0.01623  0.02948  -0.01064 158 GLN A CD  
1190 O OE1 . GLN A 192 ? 0.69178 0.58837 0.63846 0.00659  0.02477  -0.00848 158 GLN A OE1 
1191 N NE2 . GLN A 192 ? 0.66633 0.56361 0.62419 0.02458  0.03016  -0.00919 158 GLN A NE2 
1192 N N   . SER A 193 ? 0.52540 0.42563 0.45687 0.01280  0.06117  -0.03325 159 SER A N   
1193 C CA  . SER A 193 ? 0.56553 0.44806 0.47665 0.01053  0.06898  -0.03922 159 SER A CA  
1194 C C   . SER A 193 ? 0.61414 0.50565 0.53205 0.01791  0.08182  -0.04402 159 SER A C   
1195 O O   . SER A 193 ? 0.60746 0.48468 0.50784 0.01724  0.09033  -0.04945 159 SER A O   
1196 C CB  . SER A 193 ? 0.55441 0.43011 0.44863 -0.00204 0.06512  -0.03825 159 SER A CB  
1197 O OG  . SER A 193 ? 0.60106 0.49585 0.50656 -0.00547 0.06498  -0.03519 159 SER A OG  
1198 N N   . HIS A 194 ? 0.58354 0.49841 0.52615 0.02484  0.08354  -0.04229 160 HIS A N   
1199 C CA  . HIS A 194 ? 0.53333 0.46079 0.48744 0.03224  0.09569  -0.04621 160 HIS A CA  
1200 C C   . HIS A 194 ? 0.56748 0.50780 0.54364 0.04537  0.09580  -0.04561 160 HIS A C   
1201 O O   . HIS A 194 ? 0.64146 0.60641 0.64088 0.04885  0.09638  -0.04407 160 HIS A O   
1202 C CB  . HIS A 194 ? 0.56819 0.51527 0.53258 0.02561  0.09816  -0.04457 160 HIS A CB  
1203 C CG  . HIS A 194 ? 0.64812 0.58260 0.59019 0.01389  0.09928  -0.04483 160 HIS A CG  
1204 N ND1 . HIS A 194 ? 0.64941 0.57855 0.58268 0.00426  0.08825  -0.04040 160 HIS A ND1 
1205 C CD2 . HIS A 194 ? 0.58630 0.51252 0.51251 0.01075  0.11013  -0.04863 160 HIS A CD2 
1206 C CE1 . HIS A 194 ? 0.61669 0.53474 0.52979 -0.00428 0.09121  -0.04121 160 HIS A CE1 
1207 N NE2 . HIS A 194 ? 0.68255 0.59793 0.58974 -0.00084 0.10453  -0.04620 160 HIS A NE2 
1208 N N   . PRO A 195 ? 0.60319 0.52672 0.57242 0.05288  0.09493  -0.04671 161 PRO A N   
1209 C CA  . PRO A 195 ? 0.69842 0.63298 0.68751 0.06635  0.09434  -0.04534 161 PRO A CA  
1210 C C   . PRO A 195 ? 0.65100 0.60182 0.65662 0.07621  0.10595  -0.04911 161 PRO A C   
1211 O O   . PRO A 195 ? 0.70474 0.67456 0.73347 0.08600  0.10409  -0.04703 161 PRO A O   
1212 C CB  . PRO A 195 ? 0.72725 0.63437 0.70000 0.07093  0.09262  -0.04610 161 PRO A CB  
1213 C CG  . PRO A 195 ? 0.65565 0.53915 0.60195 0.06327  0.09812  -0.05129 161 PRO A CG  
1214 C CD  . PRO A 195 ? 0.72620 0.61893 0.66875 0.04988  0.09520  -0.04970 161 PRO A CD  
1215 N N   . GLU A 196 ? 0.60939 0.55425 0.60412 0.07399  0.11789  -0.05437 162 GLU A N   
1216 C CA  . GLU A 196 ? 0.65942 0.62177 0.67139 0.08307  0.13062  -0.05771 162 GLU A CA  
1217 C C   . GLU A 196 ? 0.68806 0.68364 0.72681 0.07952  0.12915  -0.05449 162 GLU A C   
1218 O O   . GLU A 196 ? 0.73101 0.74796 0.79269 0.08796  0.13682  -0.05568 162 GLU A O   
1219 C CB  . GLU A 196 ? 0.66523 0.61145 0.65578 0.08074  0.14475  -0.06403 162 GLU A CB  
1220 C CG  . GLU A 196 ? 0.75875 0.70401 0.73510 0.06529  0.14536  -0.06348 162 GLU A CG  
1221 C CD  . GLU A 196 ? 0.78140 0.70152 0.73045 0.05431  0.13481  -0.06225 162 GLU A CD  
1222 O OE1 . GLU A 196 ? 0.74388 0.64675 0.68475 0.05772  0.12778  -0.06207 162 GLU A OE1 
1223 O OE2 . GLU A 196 ? 0.81233 0.73013 0.74862 0.04214  0.13350  -0.06108 162 GLU A OE2 
1224 N N   . SER A 197 ? 0.59901 0.59940 0.63619 0.06732  0.11936  -0.05046 163 SER A N   
1225 C CA  . SER A 197 ? 0.68226 0.71104 0.74285 0.06263  0.11691  -0.04767 163 SER A CA  
1226 C C   . SER A 197 ? 0.60281 0.65046 0.68735 0.06972  0.10626  -0.04410 163 SER A C   
1227 O O   . SER A 197 ? 0.57599 0.64873 0.68289 0.06743  0.10416  -0.04261 163 SER A O   
1228 C CB  . SER A 197 ? 0.55160 0.57570 0.59939 0.04737  0.11093  -0.04497 163 SER A CB  
1229 O OG  . SER A 197 ? 0.65845 0.66337 0.68115 0.04062  0.11904  -0.04772 163 SER A OG  
1230 N N   . PHE A 198 ? 0.57868 0.61419 0.65825 0.07780  0.09936  -0.04259 164 PHE A N   
1231 C CA  . PHE A 198 ? 0.60903 0.65871 0.70598 0.08418  0.08797  -0.03853 164 PHE A CA  
1232 C C   . PHE A 198 ? 0.72010 0.76930 0.82595 0.10051  0.08991  -0.03893 164 PHE A C   
1233 O O   . PHE A 198 ? 0.78628 0.83368 0.89443 0.10682  0.08019  -0.03510 164 PHE A O   
1234 C CB  . PHE A 198 ? 0.56266 0.59872 0.64482 0.07769  0.07575  -0.03430 164 PHE A CB  
1235 C CG  . PHE A 198 ? 0.61605 0.65196 0.68994 0.06310  0.07288  -0.03333 164 PHE A CG  
1236 C CD1 . PHE A 198 ? 0.53096 0.54721 0.58239 0.05447  0.07742  -0.03496 164 PHE A CD1 
1237 C CD2 . PHE A 198 ? 0.45607 0.51047 0.54379 0.05827  0.06515  -0.03086 164 PHE A CD2 
1238 C CE1 . PHE A 198 ? 0.50958 0.52547 0.55354 0.04200  0.07434  -0.03341 164 PHE A CE1 
1239 C CE2 . PHE A 198 ? 0.52420 0.57679 0.60403 0.04576  0.06272  -0.02980 164 PHE A CE2 
1240 C CZ  . PHE A 198 ? 0.58886 0.62260 0.64730 0.03797  0.06735  -0.03071 164 PHE A CZ  
1241 N N   . VAL A 199 ? 0.74334 0.79361 0.85365 0.10809  0.10284  -0.04326 165 VAL A N   
1242 C CA  . VAL A 199 ? 0.82838 0.87708 0.94727 0.12497  0.10547  -0.04368 165 VAL A CA  
1243 C C   . VAL A 199 ? 0.86886 0.95102 1.02168 0.13406  0.10247  -0.04174 165 VAL A C   
1244 O O   . VAL A 199 ? 0.88957 0.97356 1.05188 0.14802  0.09857  -0.03963 165 VAL A O   
1245 C CB  . VAL A 199 ? 0.69503 0.72737 0.80201 0.13082  0.12120  -0.04962 165 VAL A CB  
1246 C CG1 . VAL A 199 ? 0.71990 0.71850 0.79215 0.12096  0.12242  -0.05187 165 VAL A CG1 
1247 C CG2 . VAL A 199 ? 0.73007 0.78479 0.85301 0.12893  0.13376  -0.05301 165 VAL A CG2 
1248 N N   . SER A 200 ? 0.88685 0.99518 1.05824 0.12624  0.10347  -0.04206 166 SER A N   
1249 C CA  . SER A 200 ? 0.81462 0.95677 1.02022 0.13344  0.10016  -0.04057 166 SER A CA  
1250 C C   . SER A 200 ? 0.89014 1.03903 1.10188 0.13554  0.08251  -0.03558 166 SER A C   
1251 O O   . SER A 200 ? 0.79357 0.92795 0.98704 0.12686  0.07343  -0.03325 166 SER A O   
1252 C CB  . SER A 200 ? 0.74267 0.90937 0.96551 0.12210  0.10533  -0.04203 166 SER A CB  
1253 O OG  . SER A 200 ? 0.89398 1.09466 1.15116 0.12692  0.09971  -0.04037 166 SER A OG  
1254 N N   . ASP A 201 ? 0.99103 1.16275 1.22882 0.14777  0.07778  -0.03381 167 ASP A N   
1255 C CA  . ASP A 201 ? 1.04880 1.22798 1.29194 0.15072  0.06076  -0.02912 167 ASP A CA  
1256 C C   . ASP A 201 ? 0.86477 1.06314 1.11783 0.13700  0.05171  -0.02872 167 ASP A C   
1257 O O   . ASP A 201 ? 0.67301 0.86657 0.91674 0.13347  0.03861  -0.02572 167 ASP A O   
1258 C CB  . ASP A 201 ? 1.06893 1.26664 1.33633 0.16839  0.05733  -0.02711 167 ASP A CB  
1259 C CG  . ASP A 201 ? 1.24582 1.42027 1.50079 0.18335  0.06400  -0.02672 167 ASP A CG  
1260 O OD1 . ASP A 201 ? 1.28811 1.43099 1.51402 0.18110  0.06271  -0.02544 167 ASP A OD1 
1261 O OD2 . ASP A 201 ? 1.32183 1.50948 1.59673 0.19731  0.07062  -0.02763 167 ASP A OD2 
1262 N N   . SER A 202 ? 0.84852 1.06730 1.11937 0.12912  0.05905  -0.03169 168 SER A N   
1263 C CA  . SER A 202 ? 0.78269 1.01908 1.06428 0.11549  0.05150  -0.03177 168 SER A CA  
1264 C C   . SER A 202 ? 0.73516 0.96049 1.00224 0.10002  0.06098  -0.03409 168 SER A C   
1265 O O   . SER A 202 ? 0.72415 0.93969 0.98343 0.10032  0.07554  -0.03642 168 SER A O   
1266 C CB  . SER A 202 ? 0.69306 0.96686 1.01263 0.11840  0.05005  -0.03235 168 SER A CB  
1267 O OG  . SER A 202 ? 0.77252 1.06134 1.10157 0.10742  0.03748  -0.03192 168 SER A OG  
1268 N N   . GLY A 203 ? 0.62260 0.84836 0.88473 0.08693  0.05247  -0.03342 169 GLY A N   
1269 C CA  . GLY A 203 ? 0.51471 0.73103 0.76411 0.07211  0.05943  -0.03472 169 GLY A CA  
1270 C C   . GLY A 203 ? 0.52538 0.76581 0.79887 0.06531  0.06823  -0.03655 169 GLY A C   
1271 O O   . GLY A 203 ? 0.59580 0.86135 0.89737 0.07279  0.07027  -0.03709 169 GLY A O   
1272 N N   . PRO A 204 ? 0.58013 0.81399 0.84395 0.05088  0.07365  -0.03699 170 PRO A N   
1273 C CA  . PRO A 204 ? 0.46099 0.66780 0.69425 0.04138  0.07126  -0.03598 170 PRO A CA  
1274 C C   . PRO A 204 ? 0.49328 0.67442 0.70056 0.04521  0.08083  -0.03664 170 PRO A C   
1275 O O   . PRO A 204 ? 0.48627 0.66937 0.69773 0.05322  0.09220  -0.03858 170 PRO A O   
1276 C CB  . PRO A 204 ? 0.41278 0.62651 0.65097 0.02603  0.07598  -0.03605 170 PRO A CB  
1277 C CG  . PRO A 204 ? 0.56562 0.81213 0.83935 0.02625  0.07744  -0.03694 170 PRO A CG  
1278 C CD  . PRO A 204 ? 0.52788 0.78404 0.81415 0.04231  0.08220  -0.03792 170 PRO A CD  
1279 N N   . TYR A 205 ? 0.42443 0.58123 0.60483 0.03959  0.07630  -0.03525 171 TYR A N   
1280 C CA  . TYR A 205 ? 0.48160 0.61276 0.63580 0.04103  0.08335  -0.03598 171 TYR A CA  
1281 C C   . TYR A 205 ? 0.51919 0.63607 0.65390 0.02749  0.08648  -0.03527 171 TYR A C   
1282 O O   . TYR A 205 ? 0.47074 0.58770 0.60363 0.01892  0.07802  -0.03303 171 TYR A O   
1283 C CB  . TYR A 205 ? 0.42841 0.54251 0.56804 0.04790  0.07402  -0.03424 171 TYR A CB  
1284 C CG  . TYR A 205 ? 0.51797 0.64331 0.67385 0.06172  0.06959  -0.03390 171 TYR A CG  
1285 C CD1 . TYR A 205 ? 0.46403 0.58540 0.62112 0.07320  0.07810  -0.03587 171 TYR A CD1 
1286 C CD2 . TYR A 205 ? 0.44736 0.58569 0.61565 0.06387  0.05667  -0.03157 171 TYR A CD2 
1287 C CE1 . TYR A 205 ? 0.58642 0.71708 0.75800 0.08677  0.07367  -0.03487 171 TYR A CE1 
1288 C CE2 . TYR A 205 ? 0.49590 0.64381 0.67745 0.07691  0.05171  -0.03060 171 TYR A CE2 
1289 C CZ  . TYR A 205 ? 0.62327 0.76757 0.80705 0.08850  0.06014  -0.03192 171 TYR A CZ  
1290 O OH  . TYR A 205 ? 0.60688 0.75987 0.80368 0.10241  0.05497  -0.03031 171 TYR A OH  
1291 N N   . GLN A 206 ? 0.37420 0.47769 0.49309 0.02617  0.09849  -0.03720 172 GLN A N   
1292 C CA  . GLN A 206 ? 0.43533 0.52384 0.53326 0.01417  0.10214  -0.03625 172 GLN A CA  
1293 C C   . GLN A 206 ? 0.48965 0.55128 0.55945 0.01329  0.09656  -0.03541 172 GLN A C   
1294 O O   . GLN A 206 ? 0.44911 0.49852 0.50947 0.02126  0.09875  -0.03747 172 GLN A O   
1295 C CB  . GLN A 206 ? 0.46049 0.54975 0.55530 0.01249  0.11878  -0.03876 172 GLN A CB  
1296 C CG  . GLN A 206 ? 0.45716 0.57348 0.57959 0.00996  0.12584  -0.03874 172 GLN A CG  
1297 C CD  . GLN A 206 ? 0.63331 0.75852 0.76457 -0.00140 0.11705  -0.03541 172 GLN A CD  
1298 O OE1 . GLN A 206 ? 0.71472 0.85750 0.86800 0.00033  0.10779  -0.03482 172 GLN A OE1 
1299 N NE2 . GLN A 206 ? 0.74798 0.85955 0.86063 -0.01290 0.11943  -0.03324 172 GLN A NE2 
1300 N N   . ILE A 207 ? 0.42676 0.47910 0.48389 0.00356  0.08941  -0.03230 173 ILE A N   
1301 C CA  . ILE A 207 ? 0.44874 0.47769 0.48069 0.00084  0.08402  -0.03094 173 ILE A CA  
1302 C C   . ILE A 207 ? 0.52165 0.53686 0.53265 -0.00802 0.09120  -0.03108 173 ILE A C   
1303 O O   . ILE A 207 ? 0.47448 0.49361 0.48582 -0.01671 0.09136  -0.02861 173 ILE A O   
1304 C CB  . ILE A 207 ? 0.48035 0.50862 0.51283 -0.00230 0.07035  -0.02687 173 ILE A CB  
1305 C CG1 . ILE A 207 ? 0.50528 0.54763 0.55715 0.00647  0.06364  -0.02667 173 ILE A CG1 
1306 C CG2 . ILE A 207 ? 0.42825 0.43509 0.43816 -0.00470 0.06501  -0.02512 173 ILE A CG2 
1307 C CD1 . ILE A 207 ? 0.41801 0.46069 0.47054 0.00439  0.05148  -0.02311 173 ILE A CD1 
1308 N N   . HIS A 208 ? 0.53706 0.53458 0.52826 -0.00591 0.09680  -0.03391 174 HIS A N   
1309 C CA  . HIS A 208 ? 0.57836 0.56141 0.54664 -0.01306 0.10457  -0.03480 174 HIS A CA  
1310 C C   . HIS A 208 ? 0.58066 0.54209 0.52392 -0.01917 0.09540  -0.03269 174 HIS A C   
1311 O O   . HIS A 208 ? 0.52678 0.48240 0.46933 -0.01650 0.08562  -0.03163 174 HIS A O   
1312 C CB  . HIS A 208 ? 0.53515 0.51234 0.49623 -0.00658 0.11843  -0.04041 174 HIS A CB  
1313 C CG  . HIS A 208 ? 0.60685 0.60694 0.59365 -0.00038 0.12888  -0.04228 174 HIS A CG  
1314 N ND1 . HIS A 208 ? 0.68606 0.70090 0.68322 -0.00661 0.13654  -0.04068 174 HIS A ND1 
1315 C CD2 . HIS A 208 ? 0.56761 0.57891 0.57277 0.01143  0.13290  -0.04522 174 HIS A CD2 
1316 C CE1 . HIS A 208 ? 0.56412 0.60021 0.58676 0.00060  0.14463  -0.04267 174 HIS A CE1 
1317 N NE2 . HIS A 208 ? 0.65652 0.69114 0.68450 0.01218  0.14236  -0.04543 174 HIS A NE2 
1318 N N   . GLY A 209 ? 0.56365 0.51368 0.48650 -0.02763 0.09872  -0.03166 175 GLY A N   
1319 C CA  . GLY A 209 ? 0.43693 0.36625 0.33423 -0.03367 0.09084  -0.03004 175 GLY A CA  
1320 C C   . GLY A 209 ? 0.47622 0.40681 0.37403 -0.04068 0.07894  -0.02370 175 GLY A C   
1321 O O   . GLY A 209 ? 0.55271 0.46813 0.43119 -0.04582 0.07143  -0.02165 175 GLY A O   
1322 N N   . LEU A 210 ? 0.44243 0.39037 0.36182 -0.04089 0.07659  -0.02068 176 LEU A N   
1323 C CA  . LEU A 210 ? 0.47482 0.42355 0.39591 -0.04593 0.06560  -0.01502 176 LEU A CA  
1324 C C   . LEU A 210 ? 0.42542 0.37387 0.34112 -0.05379 0.06947  -0.01178 176 LEU A C   
1325 O O   . LEU A 210 ? 0.47290 0.42505 0.38892 -0.05524 0.08115  -0.01372 176 LEU A O   
1326 C CB  . LEU A 210 ? 0.43659 0.40144 0.38241 -0.04077 0.05921  -0.01407 176 LEU A CB  
1327 C CG  . LEU A 210 ? 0.46019 0.42376 0.40999 -0.03357 0.05358  -0.01537 176 LEU A CG  
1328 C CD1 . LEU A 210 ? 0.39220 0.37207 0.36484 -0.02787 0.04887  -0.01473 176 LEU A CD1 
1329 C CD2 . LEU A 210 ? 0.36770 0.31731 0.30212 -0.03714 0.04423  -0.01208 176 LEU A CD2 
1330 N N   . PRO A 211 ? 0.46491 0.40851 0.37541 -0.05887 0.06040  -0.00638 177 PRO A N   
1331 C CA  . PRO A 211 ? 0.47956 0.42159 0.38545 -0.06621 0.06371  -0.00252 177 PRO A CA  
1332 C C   . PRO A 211 ? 0.46561 0.42400 0.39291 -0.06663 0.07120  -0.00373 177 PRO A C   
1333 O O   . PRO A 211 ? 0.53070 0.48787 0.45346 -0.07288 0.07924  -0.00198 177 PRO A O   
1334 C CB  . PRO A 211 ? 0.43458 0.37182 0.33849 -0.06838 0.05091  0.00316  177 PRO A CB  
1335 C CG  . PRO A 211 ? 0.50388 0.43361 0.39895 -0.06526 0.04291  0.00277  177 PRO A CG  
1336 C CD  . PRO A 211 ? 0.46325 0.40017 0.36878 -0.05846 0.04754  -0.00313 177 PRO A CD  
1337 N N   . HIS A 212 ? 0.45016 0.42390 0.40046 -0.06059 0.06868  -0.00643 178 HIS A N   
1338 C CA  . HIS A 212 ? 0.45622 0.44721 0.42894 -0.06138 0.07377  -0.00777 178 HIS A CA  
1339 C C   . HIS A 212 ? 0.40614 0.41111 0.39484 -0.05351 0.07979  -0.01308 178 HIS A C   
1340 O O   . HIS A 212 ? 0.47060 0.47353 0.45841 -0.04609 0.07563  -0.01520 178 HIS A O   
1341 C CB  . HIS A 212 ? 0.36165 0.35924 0.34870 -0.06169 0.06329  -0.00577 178 HIS A CB  
1342 C CG  . HIS A 212 ? 0.43042 0.41446 0.40391 -0.06787 0.05707  -0.00040 178 HIS A CG  
1343 N ND1 . HIS A 212 ? 0.37668 0.34867 0.33633 -0.06601 0.04813  0.00245  178 HIS A ND1 
1344 C CD2 . HIS A 212 ? 0.39186 0.37244 0.36429 -0.07561 0.05841  0.00300  178 HIS A CD2 
1345 C CE1 . HIS A 212 ? 0.46737 0.42965 0.41828 -0.07135 0.04408  0.00740  178 HIS A CE1 
1346 N NE2 . HIS A 212 ? 0.52920 0.49509 0.48657 -0.07722 0.05021  0.00783  178 HIS A NE2 
1347 N N   . PRO A 213 ? 0.36564 0.38500 0.36973 -0.05484 0.08972  -0.01489 179 PRO A N   
1348 C CA  . PRO A 213 ? 0.42515 0.46124 0.44934 -0.04623 0.09409  -0.01940 179 PRO A CA  
1349 C C   . PRO A 213 ? 0.45759 0.50659 0.50200 -0.04177 0.08269  -0.01973 179 PRO A C   
1350 O O   . PRO A 213 ? 0.46702 0.52226 0.52140 -0.04720 0.07730  -0.01790 179 PRO A O   
1351 C CB  . PRO A 213 ? 0.41012 0.46004 0.44730 -0.05060 0.10730  -0.02008 179 PRO A CB  
1352 C CG  . PRO A 213 ? 0.54826 0.58437 0.56647 -0.06155 0.11123  -0.01590 179 PRO A CG  
1353 C CD  . PRO A 213 ? 0.40660 0.42855 0.41212 -0.06432 0.09735  -0.01233 179 PRO A CD  
1354 N N   . LEU A 214 ? 0.39826 0.44930 0.44671 -0.03192 0.07892  -0.02205 180 LEU A N   
1355 C CA  . LEU A 214 ? 0.52674 0.58854 0.59113 -0.02662 0.06825  -0.02223 180 LEU A CA  
1356 C C   . LEU A 214 ? 0.46291 0.54189 0.54739 -0.01737 0.07178  -0.02559 180 LEU A C   
1357 O O   . LEU A 214 ? 0.41646 0.49356 0.49788 -0.01222 0.08093  -0.02787 180 LEU A O   
1358 C CB  . LEU A 214 ? 0.43677 0.48437 0.48696 -0.02296 0.05839  -0.02040 180 LEU A CB  
1359 C CG  . LEU A 214 ? 0.42102 0.45243 0.45249 -0.03042 0.05357  -0.01658 180 LEU A CG  
1360 C CD1 . LEU A 214 ? 0.50392 0.52543 0.52610 -0.02600 0.04464  -0.01472 180 LEU A CD1 
1361 C CD2 . LEU A 214 ? 0.40492 0.44160 0.44406 -0.03710 0.04940  -0.01469 180 LEU A CD2 
1362 N N   . THR A 215 ? 0.43839 0.53359 0.54283 -0.01492 0.06418  -0.02599 181 THR A N   
1363 C CA  . THR A 215 ? 0.45099 0.56497 0.57710 -0.00576 0.06505  -0.02847 181 THR A CA  
1364 C C   . THR A 215 ? 0.45485 0.57109 0.58499 0.00139  0.05215  -0.02787 181 THR A C   
1365 O O   . THR A 215 ? 0.48329 0.59328 0.60664 -0.00256 0.04292  -0.02612 181 THR A O   
1366 C CB  . THR A 215 ? 0.46502 0.60184 0.61594 -0.01062 0.06910  -0.02964 181 THR A CB  
1367 O OG1 . THR A 215 ? 0.59314 0.73418 0.75009 -0.01767 0.05876  -0.02864 181 THR A OG1 
1368 C CG2 . THR A 215 ? 0.43801 0.57212 0.58372 -0.01860 0.08289  -0.02941 181 THR A CG2 
1369 N N   . LEU A 216 ? 0.43247 0.55690 0.57280 0.01257  0.05209  -0.02914 182 LEU A N   
1370 C CA  . LEU A 216 ? 0.42010 0.54733 0.56409 0.02051  0.04072  -0.02816 182 LEU A CA  
1371 C C   . LEU A 216 ? 0.41395 0.56452 0.58353 0.02839  0.03983  -0.02985 182 LEU A C   
1372 O O   . LEU A 216 ? 0.37602 0.53303 0.55427 0.03414  0.04930  -0.03139 182 LEU A O   
1373 C CB  . LEU A 216 ? 0.44454 0.55277 0.57013 0.02768  0.03993  -0.02657 182 LEU A CB  
1374 C CG  . LEU A 216 ? 0.47082 0.55817 0.57340 0.02131  0.03702  -0.02408 182 LEU A CG  
1375 C CD1 . LEU A 216 ? 0.49946 0.57069 0.58791 0.02824  0.03634  -0.02253 182 LEU A CD1 
1376 C CD2 . LEU A 216 ? 0.43122 0.52095 0.53413 0.01700  0.02670  -0.02231 182 LEU A CD2 
1377 N N   . PRO A 217 ? 0.37987 0.54358 0.56190 0.02925  0.02860  -0.02976 183 PRO A N   
1378 C CA  . PRO A 217 ? 0.40010 0.58722 0.60720 0.03736  0.02561  -0.03094 183 PRO A CA  
1379 C C   . PRO A 217 ? 0.41060 0.59346 0.61442 0.05182  0.02216  -0.02938 183 PRO A C   
1380 O O   . PRO A 217 ? 0.42722 0.62584 0.64943 0.06128  0.02358  -0.02994 183 PRO A O   
1381 C CB  . PRO A 217 ? 0.41264 0.61158 0.62950 0.03140  0.01322  -0.03160 183 PRO A CB  
1382 C CG  . PRO A 217 ? 0.45222 0.62939 0.64439 0.02676  0.00752  -0.03002 183 PRO A CG  
1383 C CD  . PRO A 217 ? 0.34102 0.49947 0.51530 0.02209  0.01838  -0.02896 183 PRO A CD  
1384 N N   . ILE A 218 ? 0.41389 0.57570 0.59510 0.05376  0.01772  -0.02696 184 ILE A N   
1385 C CA  . ILE A 218 ? 0.48154 0.63504 0.65595 0.06628  0.01440  -0.02453 184 ILE A CA  
1386 C C   . ILE A 218 ? 0.46464 0.59260 0.61586 0.06582  0.02122  -0.02322 184 ILE A C   
1387 O O   . ILE A 218 ? 0.41741 0.53239 0.55342 0.05620  0.02208  -0.02276 184 ILE A O   
1388 C CB  . ILE A 218 ? 0.48847 0.64219 0.65842 0.06934  0.00062  -0.02211 184 ILE A CB  
1389 C CG1 . ILE A 218 ? 0.49601 0.67206 0.68491 0.06543  -0.00761 -0.02432 184 ILE A CG1 
1390 C CG2 . ILE A 218 ? 0.57447 0.72373 0.74174 0.08333  -0.00279 -0.01901 184 ILE A CG2 
1391 C CD1 . ILE A 218 ? 0.47301 0.67109 0.68540 0.07524  -0.01080 -0.02480 184 ILE A CD1 
1392 N N   . LYS A 219 ? 0.46843 0.58861 0.61691 0.07625  0.02538  -0.02255 185 LYS A N   
1393 C CA  . LYS A 219 ? 0.57676 0.67176 0.70328 0.07527  0.03112  -0.02177 185 LYS A CA  
1394 C C   . LYS A 219 ? 0.46673 0.54693 0.57686 0.07485  0.02259  -0.01742 185 LYS A C   
1395 O O   . LYS A 219 ? 0.46433 0.55131 0.57900 0.08065  0.01375  -0.01479 185 LYS A O   
1396 C CB  . LYS A 219 ? 0.55013 0.63877 0.67774 0.08638  0.03878  -0.02290 185 LYS A CB  
1397 C CG  . LYS A 219 ? 0.59959 0.69032 0.73301 0.09980  0.03223  -0.01979 185 LYS A CG  
1398 C CD  . LYS A 219 ? 0.64863 0.72488 0.77692 0.11021  0.04019  -0.02056 185 LYS A CD  
1399 C CE  . LYS A 219 ? 0.61943 0.70790 0.76253 0.11354  0.05155  -0.02536 185 LYS A CE  
1400 N NZ  . LYS A 219 ? 0.77206 0.84394 0.90839 0.12471  0.05991  -0.02677 185 LYS A NZ  
1401 N N   . PRO A 220 ? 0.45757 0.51833 0.54865 0.06775  0.02500  -0.01641 186 PRO A N   
1402 C CA  . PRO A 220 ? 0.43291 0.48089 0.51010 0.06697  0.01819  -0.01181 186 PRO A CA  
1403 C C   . PRO A 220 ? 0.50578 0.54590 0.58026 0.07826  0.01613  -0.00858 186 PRO A C   
1404 O O   . PRO A 220 ? 0.57457 0.60758 0.64906 0.08475  0.02203  -0.00993 186 PRO A O   
1405 C CB  . PRO A 220 ? 0.42118 0.45121 0.48148 0.05759  0.02256  -0.01182 186 PRO A CB  
1406 C CG  . PRO A 220 ? 0.43805 0.47463 0.50283 0.05099  0.02922  -0.01619 186 PRO A CG  
1407 C CD  . PRO A 220 ? 0.43193 0.48324 0.51380 0.05921  0.03353  -0.01921 186 PRO A CD  
1408 N N   . SER A 221 ? 0.41118 0.45140 0.48214 0.08093  0.00808  -0.00418 187 SER A N   
1409 C CA  . SER A 221 ? 0.45751 0.48959 0.52426 0.09133  0.00531  0.00017  187 SER A CA  
1410 C C   . SER A 221 ? 0.45244 0.46049 0.50183 0.08849  0.00886  0.00325  187 SER A C   
1411 O O   . SER A 221 ? 0.40637 0.40681 0.44693 0.07812  0.01049  0.00305  187 SER A O   
1412 C CB  . SER A 221 ? 0.45162 0.49213 0.51870 0.09468  -0.00423 0.00391  187 SER A CB  
1413 O OG  . SER A 221 ? 0.56956 0.59636 0.62107 0.09045  -0.00586 0.00862  187 SER A OG  
1414 N N   . PRO A 222 ? 0.55559 0.55106 0.60020 0.09735  0.00969  0.00632  188 PRO A N   
1415 C CA  . PRO A 222 ? 0.42808 0.39944 0.45672 0.09366  0.01290  0.00912  188 PRO A CA  
1416 C C   . PRO A 222 ? 0.43895 0.40623 0.45829 0.08477  0.00912  0.01368  188 PRO A C   
1417 O O   . PRO A 222 ? 0.50142 0.47810 0.52225 0.08677  0.00345  0.01728  188 PRO A O   
1418 C CB  . PRO A 222 ? 0.50187 0.46287 0.52829 0.10599  0.01220  0.01320  188 PRO A CB  
1419 C CG  . PRO A 222 ? 0.52428 0.50307 0.56712 0.11657  0.01161  0.01014  188 PRO A CG  
1420 C CD  . PRO A 222 ? 0.52659 0.52875 0.58042 0.11112  0.00722  0.00769  188 PRO A CD  
1421 N N   . GLY A 223 ? 0.46017 0.41376 0.46983 0.07504  0.01228  0.01331  189 GLY A N   
1422 C CA  . GLY A 223 ? 0.44835 0.39999 0.45177 0.06618  0.00941  0.01749  189 GLY A CA  
1423 C C   . GLY A 223 ? 0.45644 0.42204 0.46450 0.05845  0.00775  0.01483  189 GLY A C   
1424 O O   . GLY A 223 ? 0.47678 0.44424 0.48205 0.05334  0.00491  0.01857  189 GLY A O   
1425 N N   . PHE A 224 ? 0.48749 0.46258 0.50268 0.05756  0.01000  0.00882  190 PHE A N   
1426 C CA  . PHE A 224 ? 0.42639 0.41308 0.44542 0.05019  0.00844  0.00670  190 PHE A CA  
1427 C C   . PHE A 224 ? 0.39051 0.36773 0.40048 0.03941  0.00916  0.00763  190 PHE A C   
1428 O O   . PHE A 224 ? 0.51434 0.49880 0.52571 0.03370  0.00679  0.00789  190 PHE A O   
1429 C CB  . PHE A 224 ? 0.43620 0.43421 0.46494 0.05079  0.01170  0.00066  190 PHE A CB  
1430 C CG  . PHE A 224 ? 0.43959 0.42723 0.46289 0.04754  0.01875  -0.00331 190 PHE A CG  
1431 C CD1 . PHE A 224 ? 0.44007 0.41828 0.46161 0.05475  0.02309  -0.00470 190 PHE A CD1 
1432 C CD2 . PHE A 224 ? 0.40528 0.39124 0.42367 0.03782  0.02110  -0.00566 190 PHE A CD2 
1433 C CE1 . PHE A 224 ? 0.46372 0.43058 0.47790 0.05227  0.03011  -0.00908 190 PHE A CE1 
1434 C CE2 . PHE A 224 ? 0.45976 0.43489 0.47015 0.03495  0.02766  -0.00953 190 PHE A CE2 
1435 C CZ  . PHE A 224 ? 0.40237 0.36775 0.41028 0.04215  0.03241  -0.01162 190 PHE A CZ  
1436 N N   . ALA A 225 ? 0.43607 0.39682 0.43669 0.03651  0.01175  0.00813  191 ALA A N   
1437 C CA  . ALA A 225 ? 0.51923 0.47126 0.51139 0.02587  0.01142  0.00855  191 ALA A CA  
1438 C C   . ALA A 225 ? 0.50051 0.44585 0.48860 0.02230  0.00794  0.01505  191 ALA A C   
1439 O O   . ALA A 225 ? 0.49474 0.42942 0.47556 0.01416  0.00728  0.01588  191 ALA A O   
1440 C CB  . ALA A 225 ? 0.43335 0.37107 0.41651 0.02314  0.01619  0.00374  191 ALA A CB  
1441 N N   . ARG A 226 ? 0.56328 0.51513 0.55585 0.02791  0.00570  0.01978  192 ARG A N   
1442 C CA  . ARG A 226 ? 0.53823 0.48624 0.52850 0.02466  0.00367  0.02665  192 ARG A CA  
1443 C C   . ARG A 226 ? 0.44409 0.39903 0.43620 0.01656  0.00109  0.02825  192 ARG A C   
1444 O O   . ARG A 226 ? 0.47305 0.43798 0.46872 0.01583  0.00011  0.02519  192 ARG A O   
1445 C CB  . ARG A 226 ? 0.52508 0.47939 0.51806 0.03304  0.00258  0.03134  192 ARG A CB  
1446 C CG  . ARG A 226 ? 0.61599 0.56456 0.60760 0.04249  0.00391  0.03125  192 ARG A CG  
1447 C CD  . ARG A 226 ? 0.61429 0.57325 0.60833 0.05118  0.00139  0.03422  192 ARG A CD  
1448 N NE  . ARG A 226 ? 0.74176 0.69713 0.73552 0.06131  0.00147  0.03411  192 ARG A NE  
1449 C CZ  . ARG A 226 ? 0.72467 0.68894 0.72025 0.07025  -0.00178 0.03535  192 ARG A CZ  
1450 N NH1 . ARG A 226 ? 0.63581 0.61132 0.63181 0.07028  -0.00491 0.03642  192 ARG A NH1 
1451 N NH2 . ARG A 226 ? 0.68084 0.64209 0.67723 0.07978  -0.00226 0.03534  192 ARG A NH2 
1452 N N   . LEU A 227 ? 0.58440 0.53411 0.57494 0.01058  -0.00010 0.03359  193 LEU A N   
1453 C CA  . LEU A 227 ? 0.73389 0.69118 0.72811 0.00390  -0.00290 0.03666  193 LEU A CA  
1454 C C   . LEU A 227 ? 0.56442 0.52115 0.55604 -0.00274 -0.00457 0.03194  193 LEU A C   
1455 O O   . LEU A 227 ? 0.82569 0.79161 0.82092 -0.00480 -0.00677 0.03247  193 LEU A O   
1456 C CB  . LEU A 227 ? 0.71587 0.68719 0.71609 0.00957  -0.00338 0.03926  193 LEU A CB  
1457 C CG  . LEU A 227 ? 0.78704 0.75910 0.78724 0.01686  -0.00155 0.04415  193 LEU A CG  
1458 C CD1 . LEU A 227 ? 0.73198 0.71640 0.73516 0.02247  -0.00204 0.04539  193 LEU A CD1 
1459 C CD2 . LEU A 227 ? 0.71544 0.68068 0.71539 0.01204  -0.00044 0.05109  193 LEU A CD2 
1460 N N   . THR A 228 ? 0.56058 0.50508 0.54444 -0.00563 -0.00319 0.02734  194 THR A N   
1461 C CA  . THR A 228 ? 0.58441 0.52553 0.56225 -0.01250 -0.00435 0.02323  194 THR A CA  
1462 C C   . THR A 228 ? 0.67841 0.60397 0.64645 -0.02081 -0.00608 0.02251  194 THR A C   
1463 O O   . THR A 228 ? 0.72359 0.64533 0.68436 -0.02737 -0.00810 0.01983  194 THR A O   
1464 C CB  . THR A 228 ? 0.55147 0.49321 0.52697 -0.00822 -0.00008 0.01646  194 THR A CB  
1465 O OG1 . THR A 228 ? 0.59435 0.52325 0.56345 -0.00544 0.00385  0.01284  194 THR A OG1 
1466 C CG2 . THR A 228 ? 0.62224 0.57822 0.60761 -0.00017 0.00094  0.01641  194 THR A CG2 
1467 N N   . GLU A 229 ? 0.62706 0.68090 0.69972 -0.03058 -0.03963 0.03776  195 GLU A N   
1468 C CA  . GLU A 229 ? 0.68740 0.73771 0.76152 -0.03312 -0.04498 0.03652  195 GLU A CA  
1469 C C   . GLU A 229 ? 0.62489 0.67478 0.69781 -0.03299 -0.05020 0.03934  195 GLU A C   
1470 O O   . GLU A 229 ? 0.66026 0.70455 0.72694 -0.03491 -0.05437 0.03676  195 GLU A O   
1471 N N   . SER A 230 ? 0.52289 0.57895 0.60157 -0.03054 -0.05014 0.04442  196 SER A N   
1472 C CA  . SER A 230 ? 0.65628 0.71257 0.73490 -0.03007 -0.05511 0.04731  196 SER A CA  
1473 C C   . SER A 230 ? 0.66819 0.71731 0.73206 -0.02998 -0.05521 0.04542  196 SER A C   
1474 O O   . SER A 230 ? 0.62364 0.67017 0.68401 -0.03037 -0.06036 0.04616  196 SER A O   
1475 C CB  . SER A 230 ? 0.57612 0.64131 0.66519 -0.02721 -0.05439 0.05305  196 SER A CB  
1476 O OG  . SER A 230 ? 0.85414 0.91916 0.93677 -0.02480 -0.05155 0.05395  196 SER A OG  
1477 N N   . LEU A 231 ? 0.54735 0.59326 0.60281 -0.02945 -0.04966 0.04310  197 LEU A N   
1478 C CA  . LEU A 231 ? 0.56703 0.60581 0.60884 -0.02943 -0.04885 0.04181  197 LEU A CA  
1479 C C   . LEU A 231 ? 0.53638 0.56711 0.56690 -0.03216 -0.04938 0.03695  197 LEU A C   
1480 O O   . LEU A 231 ? 0.65964 0.68464 0.67955 -0.03255 -0.05178 0.03676  197 LEU A O   
1481 C CB  . LEU A 231 ? 0.55856 0.59774 0.59769 -0.02765 -0.04241 0.04158  197 LEU A CB  
1482 C CG  . LEU A 231 ? 0.58600 0.62996 0.62987 -0.02452 -0.04193 0.04579  197 LEU A CG  
1483 C CD1 . LEU A 231 ? 0.60926 0.65469 0.65272 -0.02299 -0.03540 0.04418  197 LEU A CD1 
1484 C CD2 . LEU A 231 ? 0.51612 0.55506 0.55254 -0.02399 -0.04532 0.04789  197 LEU A CD2 
1485 N N   . ILE A 232 ? 0.57817 0.60855 0.61061 -0.03382 -0.04711 0.03306  198 ILE A N   
1486 C CA  . ILE A 232 ? 0.47049 0.49363 0.49216 -0.03622 -0.04661 0.02778  198 ILE A CA  
1487 C C   . ILE A 232 ? 0.55353 0.57482 0.57495 -0.03794 -0.05338 0.02622  198 ILE A C   
1488 O O   . ILE A 232 ? 0.63805 0.65307 0.64763 -0.03935 -0.05463 0.02272  198 ILE A O   
1489 C CB  . ILE A 232 ? 0.66650 0.69011 0.69081 -0.03706 -0.04133 0.02384  198 ILE A CB  
1490 C CG1 . ILE A 232 ? 0.66653 0.68768 0.68347 -0.03639 -0.03471 0.02259  198 ILE A CG1 
1491 C CG2 . ILE A 232 ? 0.64031 0.65942 0.66085 -0.03963 -0.04278 0.01839  198 ILE A CG2 
1492 C CD1 . ILE A 232 ? 0.77228 0.79476 0.79267 -0.03687 -0.02952 0.01875  198 ILE A CD1 
1493 N N   . GLU A 233 ? 0.60884 0.63569 0.64321 -0.03781 -0.05781 0.02866  199 GLU A N   
1494 C CA  . GLU A 233 ? 0.74882 0.77438 0.78495 -0.03957 -0.06454 0.02658  199 GLU A CA  
1495 C C   . GLU A 233 ? 0.68702 0.70872 0.71215 -0.03925 -0.06929 0.02717  199 GLU A C   
1496 O O   . GLU A 233 ? 0.60706 0.62917 0.62857 -0.03727 -0.06877 0.03129  199 GLU A O   
1497 C CB  . GLU A 233 ? 0.69870 0.73144 0.75240 -0.03942 -0.06806 0.02997  199 GLU A CB  
1498 C CG  . GLU A 233 ? 0.78994 0.82742 0.84891 -0.03749 -0.07141 0.03578  199 GLU A CG  
1499 C CD  . GLU A 233 ? 0.93091 0.97607 1.00810 -0.03741 -0.07382 0.03948  199 GLU A CD  
1500 O OE1 . GLU A 233 ? 0.99587 1.04166 1.08129 -0.03918 -0.07421 0.03735  199 GLU A OE1 
1501 O OE2 . GLU A 233 ? 0.94873 0.99927 1.03242 -0.03553 -0.07514 0.04463  199 GLU A OE2 
1502 N N   . ALA A 234 ? 0.72220 0.74018 0.74202 -0.04102 -0.07408 0.02283  200 ALA A N   
1503 C CA  . ALA A 234 ? 0.72572 0.73992 0.73361 -0.04064 -0.07902 0.02282  200 ALA A CA  
1504 C C   . ALA A 234 ? 0.81456 0.83379 0.83121 -0.03916 -0.08508 0.02790  200 ALA A C   
1505 O O   . ALA A 234 ? 0.84450 0.87019 0.87694 -0.03881 -0.08574 0.03093  200 ALA A O   
1506 C CB  . ALA A 234 ? 0.68919 0.69931 0.69023 -0.04271 -0.08310 0.01627  200 ALA A CB  
1507 N N   . GLU A 235 ? 0.89371 0.91010 0.89984 -0.03814 -0.08944 0.02902  201 GLU A N   
1508 C CA  . GLU A 235 ? 0.92415 0.94499 0.93740 -0.03646 -0.09541 0.03370  201 GLU A CA  
1509 C C   . GLU A 235 ? 1.01241 1.03674 1.03617 -0.03798 -0.10315 0.03125  201 GLU A C   
1510 O O   . GLU A 235 ? 1.04713 1.06819 1.06572 -0.03990 -0.10609 0.02541  201 GLU A O   
1511 C CB  . GLU A 235 ? 0.78402 0.80049 0.78239 -0.03459 -0.09778 0.03591  201 GLU A CB  
1512 C CG  . GLU A 235 ? 0.87342 0.88472 0.85770 -0.03563 -0.10263 0.03122  201 GLU A CG  
1513 C CD  . GLU A 235 ? 1.03393 1.04871 1.02368 -0.03545 -0.11265 0.03082  201 GLU A CD  
1514 O OE1 . GLU A 235 ? 0.98056 0.99970 0.97834 -0.03353 -0.11605 0.03593  201 GLU A OE1 
1515 O OE2 . GLU A 235 ? 0.97957 0.99298 0.96620 -0.03718 -0.11718 0.02501  201 GLU A OE2 
1516 N N   . ASN A 236 ? 0.95253 0.98376 0.99172 -0.03712 -0.10634 0.03552  202 ASN A N   
1517 C CA  . ASN A 236 ? 0.97148 1.00666 1.02209 -0.03830 -0.11448 0.03418  202 ASN A CA  
1518 C C   . ASN A 236 ? 0.93985 0.97888 0.99354 -0.03586 -0.11927 0.03940  202 ASN A C   
1519 O O   . ASN A 236 ? 0.90621 0.95218 0.97548 -0.03503 -0.11935 0.04391  202 ASN A O   
1520 C CB  . ASN A 236 ? 1.11576 1.15630 1.18550 -0.04002 -0.11313 0.03431  202 ASN A CB  
1521 C CG  . ASN A 236 ? 1.16446 1.20555 1.24233 -0.04256 -0.12013 0.02937  202 ASN A CG  
1522 O OD1 . ASN A 236 ? 1.14605 1.18313 1.21346 -0.04314 -0.12558 0.02459  202 ASN A OD1 
1523 N ND2 . ASN A 236 ? 1.15200 1.19815 1.24871 -0.04401 -0.12000 0.03048  202 ASN A ND2 
1524 N N   . ASP A 237 ? 0.84796 0.88260 0.88661 -0.03454 -0.12304 0.03896  203 ASP A N   
1525 C CA  . ASP A 237 ? 0.72148 0.75856 0.76025 -0.03173 -0.12720 0.04404  203 ASP A CA  
1526 C C   . ASP A 237 ? 0.62087 0.66088 0.66518 -0.02948 -0.12067 0.05006  203 ASP A C   
1527 O O   . ASP A 237 ? 0.61110 0.65807 0.66986 -0.02818 -0.12210 0.05422  203 ASP A O   
1528 C CB  . ASP A 237 ? 0.80939 0.85281 0.86260 -0.03213 -0.13606 0.04398  203 ASP A CB  
1529 C CG  . ASP A 237 ? 0.91493 0.95592 0.96393 -0.03438 -0.14281 0.03708  203 ASP A CG  
1530 O OD1 . ASP A 237 ? 0.74114 0.77601 0.77160 -0.03389 -0.14450 0.03419  203 ASP A OD1 
1531 O OD2 . ASP A 237 ? 1.00468 1.04998 1.06910 -0.03658 -0.14632 0.03452  203 ASP A OD2 
1532 N N   . SER A 238 ? 0.57905 0.61384 0.61183 -0.02903 -0.11328 0.05009  204 SER A N   
1533 C CA  . SER A 238 ? 0.47770 0.51481 0.51490 -0.02705 -0.10646 0.05449  204 SER A CA  
1534 C C   . SER A 238 ? 0.42770 0.46364 0.45935 -0.02381 -0.10796 0.05915  204 SER A C   
1535 O O   . SER A 238 ? 0.50842 0.53807 0.52520 -0.02317 -0.11027 0.05882  204 SER A O   
1536 C CB  . SER A 238 ? 0.54936 0.58162 0.57790 -0.02801 -0.09802 0.05208  204 SER A CB  
1537 O OG  . SER A 238 ? 0.55342 0.58703 0.58368 -0.02577 -0.09198 0.05579  204 SER A OG  
1538 N N   . HIS A 239 ? 0.37433 0.41651 0.41811 -0.02160 -0.10652 0.06363  205 HIS A N   
1539 C CA  . HIS A 239 ? 0.44513 0.48646 0.48568 -0.01821 -0.10662 0.06814  205 HIS A CA  
1540 C C   . HIS A 239 ? 0.42819 0.46440 0.45971 -0.01720 -0.09847 0.06870  205 HIS A C   
1541 O O   . HIS A 239 ? 0.39071 0.42569 0.42027 -0.01435 -0.09755 0.07233  205 HIS A O   
1542 C CB  . HIS A 239 ? 0.40577 0.45643 0.46390 -0.01611 -0.10826 0.07220  205 HIS A CB  
1543 C CG  . HIS A 239 ? 0.48537 0.54177 0.55476 -0.01716 -0.11607 0.07191  205 HIS A CG  
1544 N ND1 . HIS A 239 ? 0.50120 0.55719 0.56833 -0.01599 -0.12428 0.07291  205 HIS A ND1 
1545 C CD2 . HIS A 239 ? 0.52361 0.58635 0.60727 -0.01929 -0.11699 0.07075  205 HIS A CD2 
1546 C CE1 . HIS A 239 ? 0.55592 0.61799 0.63594 -0.01748 -0.13003 0.07191  205 HIS A CE1 
1547 N NE2 . HIS A 239 ? 0.51776 0.58378 0.60820 -0.01959 -0.12559 0.07074  205 HIS A NE2 
1548 N N   . GLY A 240 ? 0.41652 0.44986 0.44354 -0.01941 -0.09266 0.06509  206 GLY A N   
1549 C CA  . GLY A 240 ? 0.40728 0.43564 0.42603 -0.01888 -0.08502 0.06482  206 GLY A CA  
1550 C C   . GLY A 240 ? 0.45618 0.49037 0.48600 -0.01834 -0.07863 0.06487  206 GLY A C   
1551 O O   . GLY A 240 ? 0.42582 0.46818 0.46968 -0.01799 -0.07973 0.06603  206 GLY A O   
1552 N N   . VAL A 241 ? 0.36734 0.39729 0.39042 -0.01820 -0.07176 0.06363  207 VAL A N   
1553 C CA  . VAL A 241 ? 0.33320 0.36792 0.36424 -0.01737 -0.06526 0.06305  207 VAL A CA  
1554 C C   . VAL A 241 ? 0.36293 0.39609 0.39263 -0.01448 -0.06198 0.06542  207 VAL A C   
1555 O O   . VAL A 241 ? 0.38204 0.40710 0.40028 -0.01454 -0.06048 0.06540  207 VAL A O   
1556 C CB  . VAL A 241 ? 0.39690 0.42851 0.42269 -0.01990 -0.05989 0.05841  207 VAL A CB  
1557 C CG1 . VAL A 241 ? 0.32333 0.36074 0.35760 -0.01869 -0.05372 0.05774  207 VAL A CG1 
1558 C CG2 . VAL A 241 ? 0.50571 0.53798 0.53277 -0.02270 -0.06334 0.05573  207 VAL A CG2 
1559 N N   . ILE A 242 ? 0.34198 0.38288 0.38358 -0.01189 -0.06073 0.06747  208 ILE A N   
1560 C CA  . ILE A 242 ? 0.34172 0.38204 0.38411 -0.00892 -0.05733 0.06896  208 ILE A CA  
1561 C C   . ILE A 242 ? 0.35989 0.39977 0.40115 -0.00934 -0.04985 0.06536  208 ILE A C   
1562 O O   . ILE A 242 ? 0.35151 0.39823 0.40016 -0.00957 -0.04735 0.06366  208 ILE A O   
1563 C CB  . ILE A 242 ? 0.47272 0.52211 0.52845 -0.00568 -0.05931 0.07223  208 ILE A CB  
1564 C CG1 . ILE A 242 ? 0.43785 0.48817 0.49579 -0.00536 -0.06710 0.07553  208 ILE A CG1 
1565 C CG2 . ILE A 242 ? 0.34031 0.38895 0.39728 -0.00243 -0.05576 0.07306  208 ILE A CG2 
1566 C CD1 . ILE A 242 ? 0.35278 0.41327 0.42551 -0.00257 -0.06914 0.07862  208 ILE A CD1 
1567 N N   . VAL A 243 ? 0.30180 0.33384 0.33427 -0.00936 -0.04630 0.06437  209 VAL A N   
1568 C CA  . VAL A 243 ? 0.35855 0.38892 0.38885 -0.01026 -0.03944 0.06034  209 VAL A CA  
1569 C C   . VAL A 243 ? 0.42943 0.46029 0.46382 -0.00730 -0.03584 0.06060  209 VAL A C   
1570 O O   . VAL A 243 ? 0.37280 0.39792 0.40347 -0.00602 -0.03695 0.06319  209 VAL A O   
1571 C CB  . VAL A 243 ? 0.39994 0.42050 0.41693 -0.01339 -0.03754 0.05816  209 VAL A CB  
1572 C CG1 . VAL A 243 ? 0.33041 0.34869 0.34590 -0.01404 -0.03031 0.05428  209 VAL A CG1 
1573 C CG2 . VAL A 243 ? 0.29144 0.31247 0.30561 -0.01627 -0.04031 0.05642  209 VAL A CG2 
1574 N N   . ASN A 244 ? 0.33409 0.37191 0.37631 -0.00604 -0.03168 0.05784  210 ASN A N   
1575 C CA  . ASN A 244 ? 0.32725 0.36639 0.37424 -0.00317 -0.02797 0.05676  210 ASN A CA  
1576 C C   . ASN A 244 ? 0.36546 0.39638 0.40537 -0.00485 -0.02275 0.05335  210 ASN A C   
1577 O O   . ASN A 244 ? 0.34714 0.38079 0.38969 -0.00500 -0.01803 0.04897  210 ASN A O   
1578 C CB  . ASN A 244 ? 0.30595 0.35665 0.36373 -0.00085 -0.02591 0.05493  210 ASN A CB  
1579 C CG  . ASN A 244 ? 0.35487 0.40777 0.41809 0.00246  -0.02257 0.05316  210 ASN A CG  
1580 O OD1 . ASN A 244 ? 0.32839 0.37638 0.39103 0.00397  -0.02362 0.05512  210 ASN A OD1 
1581 N ND2 . ASN A 244 ? 0.32539 0.38552 0.39387 0.00372  -0.01860 0.04919  210 ASN A ND2 
1582 N N   . SER A 245 ? 0.32358 0.34451 0.35460 -0.00600 -0.02369 0.05563  211 SER A N   
1583 C CA  . SER A 245 ? 0.36669 0.37873 0.39089 -0.00767 -0.01878 0.05358  211 SER A CA  
1584 C C   . SER A 245 ? 0.32673 0.32956 0.34380 -0.00729 -0.02106 0.05835  211 SER A C   
1585 O O   . SER A 245 ? 0.33530 0.33943 0.35343 -0.00550 -0.02654 0.06261  211 SER A O   
1586 C CB  . SER A 245 ? 0.34713 0.35635 0.36408 -0.01147 -0.01620 0.05025  211 SER A CB  
1587 O OG  . SER A 245 ? 0.36741 0.36960 0.38003 -0.01302 -0.01052 0.04772  211 SER A OG  
1588 N N   . PHE A 246 ? 0.35082 0.34451 0.36101 -0.00888 -0.01682 0.05788  212 PHE A N   
1589 C CA  . PHE A 246 ? 0.36164 0.34587 0.36381 -0.00859 -0.01844 0.06297  212 PHE A CA  
1590 C C   . PHE A 246 ? 0.41546 0.39141 0.40411 -0.01219 -0.01640 0.06306  212 PHE A C   
1591 O O   . PHE A 246 ? 0.36612 0.34229 0.35299 -0.01485 -0.01203 0.05854  212 PHE A O   
1592 C CB  . PHE A 246 ? 0.34301 0.32312 0.35056 -0.00634 -0.01524 0.06388  212 PHE A CB  
1593 C CG  . PHE A 246 ? 0.35139 0.32975 0.36212 -0.00779 -0.00795 0.05874  212 PHE A CG  
1594 C CD1 . PHE A 246 ? 0.34381 0.33113 0.36441 -0.00705 -0.00563 0.05307  212 PHE A CD1 
1595 C CD2 . PHE A 246 ? 0.37431 0.34229 0.37869 -0.00967 -0.00347 0.05978  212 PHE A CD2 
1596 C CE1 . PHE A 246 ? 0.32201 0.30826 0.34622 -0.00821 0.00057  0.04787  212 PHE A CE1 
1597 C CE2 . PHE A 246 ? 0.47307 0.43966 0.48179 -0.01111 0.00315  0.05480  212 PHE A CE2 
1598 C CZ  . PHE A 246 ? 0.36992 0.34582 0.38878 -0.01035 0.00494  0.04851  212 PHE A CZ  
1599 N N   . ALA A 247 ? 0.36628 0.33532 0.34527 -0.01198 -0.01978 0.06835  213 ALA A N   
1600 C CA  . ALA A 247 ? 0.43029 0.39278 0.39497 -0.01495 -0.01933 0.06901  213 ALA A CA  
1601 C C   . ALA A 247 ? 0.40053 0.35686 0.36104 -0.01760 -0.01133 0.06633  213 ALA A C   
1602 O O   . ALA A 247 ? 0.38414 0.33940 0.33762 -0.02060 -0.00900 0.06326  213 ALA A O   
1603 C CB  . ALA A 247 ? 0.41942 0.37550 0.37447 -0.01355 -0.02406 0.07563  213 ALA A CB  
1604 N N   . GLU A 248 ? 0.46211 0.41429 0.42751 -0.01656 -0.00702 0.06731  214 GLU A N   
1605 C CA  . GLU A 248 ? 0.44620 0.39217 0.40897 -0.01915 0.00076  0.06510  214 GLU A CA  
1606 C C   . GLU A 248 ? 0.48279 0.43485 0.45121 -0.02130 0.00479  0.05764  214 GLU A C   
1607 O O   . GLU A 248 ? 0.46271 0.41113 0.42525 -0.02440 0.00975  0.05513  214 GLU A O   
1608 C CB  . GLU A 248 ? 0.57190 0.51327 0.54202 -0.01737 0.00407  0.06702  214 GLU A CB  
1609 C CG  . GLU A 248 ? 0.70329 0.63931 0.67446 -0.02001 0.01239  0.06403  214 GLU A CG  
1610 C CD  . GLU A 248 ? 0.88389 0.81046 0.84075 -0.02274 0.01557  0.06773  214 GLU A CD  
1611 O OE1 . GLU A 248 ? 0.85957 0.77974 0.80827 -0.02143 0.01288  0.07476  214 GLU A OE1 
1612 O OE2 . GLU A 248 ? 0.94784 0.87371 0.90154 -0.02600 0.02077  0.06369  214 GLU A OE2 
1613 N N   . LEU A 249 ? 0.37622 0.33780 0.35614 -0.01952 0.00289  0.05417  215 LEU A N   
1614 C CA  . LEU A 249 ? 0.39960 0.36758 0.38504 -0.02108 0.00619  0.04747  215 LEU A CA  
1615 C C   . LEU A 249 ? 0.35428 0.32417 0.33229 -0.02339 0.00420  0.04600  215 LEU A C   
1616 O O   . LEU A 249 ? 0.34541 0.31529 0.32181 -0.02597 0.00845  0.04154  215 LEU A O   
1617 C CB  . LEU A 249 ? 0.32003 0.29809 0.31888 -0.01813 0.00450  0.04482  215 LEU A CB  
1618 C CG  . LEU A 249 ? 0.36457 0.34914 0.37149 -0.01871 0.00879  0.03792  215 LEU A CG  
1619 C CD1 . LEU A 249 ? 0.35561 0.33519 0.36579 -0.01954 0.01511  0.03507  215 LEU A CD1 
1620 C CD2 . LEU A 249 ? 0.37056 0.36630 0.38840 -0.01546 0.00592  0.03632  215 LEU A CD2 
1621 N N   . ASP A 250 ? 0.34094 0.31247 0.31500 -0.02251 -0.00230 0.04940  216 ASP A N   
1622 C CA  . ASP A 250 ? 0.32639 0.30005 0.29476 -0.02446 -0.00501 0.04774  216 ASP A CA  
1623 C C   . ASP A 250 ? 0.38314 0.34837 0.33657 -0.02672 -0.00466 0.04958  216 ASP A C   
1624 O O   . ASP A 250 ? 0.39645 0.36282 0.34426 -0.02824 -0.00734 0.04802  216 ASP A O   
1625 C CB  . ASP A 250 ? 0.35562 0.33596 0.32854 -0.02249 -0.01242 0.04993  216 ASP A CB  
1626 C CG  . ASP A 250 ? 0.39515 0.38545 0.38205 -0.02055 -0.01256 0.04761  216 ASP A CG  
1627 O OD1 . ASP A 250 ? 0.34819 0.34021 0.34123 -0.02017 -0.00750 0.04443  216 ASP A OD1 
1628 O OD2 . ASP A 250 ? 0.34983 0.34652 0.34162 -0.01939 -0.01776 0.04891  216 ASP A OD2 
1629 N N   . GLU A 251 ? 0.39925 0.35619 0.34628 -0.02687 -0.00135 0.05285  217 GLU A N   
1630 C CA  . GLU A 251 ? 0.37239 0.32148 0.30411 -0.02836 -0.00140 0.05588  217 GLU A CA  
1631 C C   . GLU A 251 ? 0.43371 0.38261 0.35890 -0.03159 0.00174  0.05095  217 GLU A C   
1632 O O   . GLU A 251 ? 0.42707 0.37744 0.35753 -0.03327 0.00755  0.04618  217 GLU A O   
1633 C CB  . GLU A 251 ? 0.36278 0.30309 0.29033 -0.02826 0.00347  0.06000  217 GLU A CB  
1634 C CG  . GLU A 251 ? 0.51002 0.44207 0.42074 -0.02963 0.00435  0.06378  217 GLU A CG  
1635 C CD  . GLU A 251 ? 0.71408 0.63778 0.62093 -0.02830 0.00637  0.07055  217 GLU A CD  
1636 O OE1 . GLU A 251 ? 0.66738 0.58820 0.58143 -0.02879 0.01255  0.07006  217 GLU A OE1 
1637 O OE2 . GLU A 251 ? 0.69474 0.61483 0.59187 -0.02666 0.00157  0.07634  217 GLU A OE2 
1638 N N   . GLY A 252 ? 0.42691 0.37431 0.34098 -0.03230 -0.00232 0.05174  218 GLY A N   
1639 C CA  . GLY A 252 ? 0.39146 0.33926 0.29944 -0.03504 -0.00038 0.04668  218 GLY A CA  
1640 C C   . GLY A 252 ? 0.48508 0.44114 0.40147 -0.03514 -0.00455 0.04220  218 GLY A C   
1641 O O   . GLY A 252 ? 0.46300 0.41967 0.37325 -0.03635 -0.00750 0.03979  218 GLY A O   
1642 N N   . TYR A 253 ? 0.36351 0.32602 0.29409 -0.03378 -0.00479 0.04107  219 TYR A N   
1643 C CA  . TYR A 253 ? 0.38025 0.35076 0.31962 -0.03366 -0.00858 0.03784  219 TYR A CA  
1644 C C   . TYR A 253 ? 0.36019 0.33371 0.30086 -0.03183 -0.01692 0.04138  219 TYR A C   
1645 O O   . TYR A 253 ? 0.36096 0.33857 0.30387 -0.03247 -0.02113 0.03923  219 TYR A O   
1646 C CB  . TYR A 253 ? 0.37014 0.34689 0.32338 -0.03278 -0.00512 0.03525  219 TYR A CB  
1647 C CG  . TYR A 253 ? 0.37912 0.35319 0.33105 -0.03490 0.00259  0.03094  219 TYR A CG  
1648 C CD1 . TYR A 253 ? 0.28981 0.26610 0.24209 -0.03689 0.00448  0.02572  219 TYR A CD1 
1649 C CD2 . TYR A 253 ? 0.32571 0.29443 0.27586 -0.03504 0.00794  0.03219  219 TYR A CD2 
1650 C CE1 . TYR A 253 ? 0.29067 0.26469 0.24196 -0.03886 0.01145  0.02166  219 TYR A CE1 
1651 C CE2 . TYR A 253 ? 0.40028 0.36652 0.34969 -0.03724 0.01504  0.02822  219 TYR A CE2 
1652 C CZ  . TYR A 253 ? 0.31675 0.28590 0.26668 -0.03911 0.01675  0.02290  219 TYR A CZ  
1653 O OH  . TYR A 253 ? 0.39473 0.36187 0.34472 -0.04122 0.02380  0.01881  219 TYR A OH  
1654 N N   . THR A 254 ? 0.33245 0.30383 0.27226 -0.02960 -0.01943 0.04673  220 THR A N   
1655 C CA  . THR A 254 ? 0.38241 0.35570 0.32174 -0.02793 -0.02754 0.05034  220 THR A CA  
1656 C C   . THR A 254 ? 0.41834 0.38868 0.34592 -0.02961 -0.03129 0.04908  220 THR A C   
1657 O O   . THR A 254 ? 0.40267 0.37759 0.33373 -0.02973 -0.03718 0.04778  220 THR A O   
1658 C CB  . THR A 254 ? 0.40706 0.37652 0.34437 -0.02540 -0.02893 0.05633  220 THR A CB  
1659 O OG1 . THR A 254 ? 0.49507 0.46691 0.44316 -0.02388 -0.02492 0.05660  220 THR A OG1 
1660 C CG2 . THR A 254 ? 0.40839 0.38109 0.34756 -0.02332 -0.03758 0.05994  220 THR A CG2 
1661 N N   . GLU A 255 ? 0.45773 0.42053 0.37153 -0.03091 -0.02775 0.04927  221 GLU A N   
1662 C CA  . GLU A 255 ? 0.42858 0.38837 0.32935 -0.03214 -0.03112 0.04797  221 GLU A CA  
1663 C C   . GLU A 255 ? 0.45055 0.41348 0.35337 -0.03460 -0.03013 0.04117  221 GLU A C   
1664 O O   . GLU A 255 ? 0.38945 0.35407 0.28941 -0.03512 -0.03580 0.03895  221 GLU A O   
1665 C CB  . GLU A 255 ? 0.43255 0.38373 0.31778 -0.03264 -0.02672 0.05049  221 GLU A CB  
1666 C CG  . GLU A 255 ? 0.38332 0.33049 0.26496 -0.03002 -0.02870 0.05784  221 GLU A CG  
1667 C CD  . GLU A 255 ? 0.45373 0.39921 0.34362 -0.02932 -0.02254 0.06010  221 GLU A CD  
1668 O OE1 . GLU A 255 ? 0.53204 0.48089 0.43185 -0.03056 -0.01775 0.05584  221 GLU A OE1 
1669 O OE2 . GLU A 255 ? 0.51183 0.45273 0.39871 -0.02738 -0.02273 0.06600  221 GLU A OE2 
1670 N N   . TYR A 256 ? 0.35659 0.32036 0.26487 -0.03604 -0.02315 0.03757  222 TYR A N   
1671 C CA  . TYR A 256 ? 0.43816 0.40552 0.35087 -0.03800 -0.02220 0.03130  222 TYR A CA  
1672 C C   . TYR A 256 ? 0.47357 0.44804 0.39778 -0.03722 -0.02899 0.03074  222 TYR A C   
1673 O O   . TYR A 256 ? 0.43030 0.40621 0.35390 -0.03847 -0.03246 0.02704  222 TYR A O   
1674 C CB  . TYR A 256 ? 0.46902 0.43764 0.38898 -0.03895 -0.01439 0.02828  222 TYR A CB  
1675 C CG  . TYR A 256 ? 0.45247 0.42431 0.37683 -0.04081 -0.01277 0.02194  222 TYR A CG  
1676 C CD1 . TYR A 256 ? 0.40368 0.38273 0.34150 -0.04024 -0.01567 0.02042  222 TYR A CD1 
1677 C CD2 . TYR A 256 ? 0.43270 0.40043 0.34802 -0.04300 -0.00813 0.01771  222 TYR A CD2 
1678 C CE1 . TYR A 256 ? 0.44301 0.42465 0.38535 -0.04173 -0.01427 0.01503  222 TYR A CE1 
1679 C CE2 . TYR A 256 ? 0.43052 0.40107 0.35046 -0.04449 -0.00668 0.01177  222 TYR A CE2 
1680 C CZ  . TYR A 256 ? 0.51771 0.49499 0.45123 -0.04382 -0.00990 0.01053  222 TYR A CZ  
1681 O OH  . TYR A 256 ? 0.53504 0.51475 0.47357 -0.04512 -0.00852 0.00500  222 TYR A OH  
1682 N N   . TYR A 257 ? 0.41816 0.39722 0.35345 -0.03513 -0.03079 0.03437  223 TYR A N   
1683 C CA  . TYR A 257 ? 0.41872 0.40514 0.36642 -0.03437 -0.03635 0.03448  223 TYR A CA  
1684 C C   . TYR A 257 ? 0.35860 0.34478 0.30226 -0.03397 -0.04458 0.03617  223 TYR A C   
1685 O O   . TYR A 257 ? 0.41533 0.40510 0.36427 -0.03490 -0.04904 0.03362  223 TYR A O   
1686 C CB  . TYR A 257 ? 0.37166 0.36334 0.33147 -0.03198 -0.03564 0.03802  223 TYR A CB  
1687 C CG  . TYR A 257 ? 0.37408 0.37362 0.34667 -0.03100 -0.04110 0.03920  223 TYR A CG  
1688 C CD1 . TYR A 257 ? 0.37786 0.38321 0.36093 -0.03169 -0.03971 0.03638  223 TYR A CD1 
1689 C CD2 . TYR A 257 ? 0.34665 0.34793 0.32130 -0.02931 -0.04757 0.04339  223 TYR A CD2 
1690 C CE1 . TYR A 257 ? 0.43361 0.44614 0.42885 -0.03088 -0.04422 0.03809  223 TYR A CE1 
1691 C CE2 . TYR A 257 ? 0.41634 0.42507 0.40358 -0.02860 -0.05220 0.04462  223 TYR A CE2 
1692 C CZ  . TYR A 257 ? 0.45644 0.47069 0.45393 -0.02947 -0.05029 0.04213  223 TYR A CZ  
1693 O OH  . TYR A 257 ? 0.44125 0.46286 0.45166 -0.02884 -0.05440 0.04397  223 TYR A OH  
1694 N N   . GLU A 258 ? 0.36374 0.34597 0.29907 -0.03246 -0.04695 0.04055  224 GLU A N   
1695 C CA  . GLU A 258 ? 0.51199 0.49418 0.44284 -0.03180 -0.05521 0.04208  224 GLU A CA  
1696 C C   . GLU A 258 ? 0.50253 0.48170 0.42287 -0.03396 -0.05693 0.03709  224 GLU A C   
1697 O O   . GLU A 258 ? 0.43303 0.41512 0.35609 -0.03435 -0.06369 0.03511  224 GLU A O   
1698 C CB  . GLU A 258 ? 0.46095 0.43886 0.38357 -0.02953 -0.05686 0.04789  224 GLU A CB  
1699 C CG  . GLU A 258 ? 0.43375 0.41561 0.36843 -0.02701 -0.05693 0.05248  224 GLU A CG  
1700 C CD  . GLU A 258 ? 0.48416 0.46163 0.41203 -0.02451 -0.05875 0.05839  224 GLU A CD  
1701 O OE1 . GLU A 258 ? 0.60978 0.58067 0.52260 -0.02476 -0.05905 0.05945  224 GLU A OE1 
1702 O OE2 . GLU A 258 ? 0.47695 0.45766 0.41453 -0.02211 -0.05981 0.06210  224 GLU A OE2 
1703 N N   . ASN A 259 ? 0.44182 0.41541 0.35081 -0.03539 -0.05075 0.03465  225 ASN A N   
1704 C CA  . ASN A 259 ? 0.43854 0.40967 0.33761 -0.03733 -0.05165 0.02919  225 ASN A CA  
1705 C C   . ASN A 259 ? 0.50298 0.47895 0.41362 -0.03906 -0.05243 0.02351  225 ASN A C   
1706 O O   . ASN A 259 ? 0.55711 0.53369 0.46567 -0.04005 -0.05737 0.01938  225 ASN A O   
1707 C CB  . ASN A 259 ? 0.54509 0.50980 0.43079 -0.03847 -0.04381 0.02796  225 ASN A CB  
1708 C CG  . ASN A 259 ? 0.77134 0.73425 0.64817 -0.04051 -0.04325 0.02135  225 ASN A CG  
1709 O OD1 . ASN A 259 ? 0.78559 0.74993 0.66811 -0.04227 -0.03898 0.01626  225 ASN A OD1 
1710 N ND2 . ASN A 259 ? 0.88020 0.84021 0.74296 -0.04005 -0.04772 0.02121  225 ASN A ND2 
1711 N N   . LEU A 260 ? 0.47906 0.45862 0.40224 -0.03928 -0.04780 0.02322  226 LEU A N   
1712 C CA  . LEU A 260 ? 0.48117 0.46500 0.41541 -0.04076 -0.04784 0.01843  226 LEU A CA  
1713 C C   . LEU A 260 ? 0.50725 0.49683 0.45371 -0.04021 -0.05551 0.01958  226 LEU A C   
1714 O O   . LEU A 260 ? 0.52190 0.51289 0.47218 -0.04163 -0.05909 0.01528  226 LEU A O   
1715 C CB  . LEU A 260 ? 0.46324 0.44962 0.40674 -0.04077 -0.04077 0.01820  226 LEU A CB  
1716 C CG  . LEU A 260 ? 0.58495 0.57688 0.54251 -0.04156 -0.04137 0.01506  226 LEU A CG  
1717 C CD1 . LEU A 260 ? 0.54687 0.53604 0.49964 -0.04377 -0.04030 0.00835  226 LEU A CD1 
1718 C CD2 . LEU A 260 ? 0.49284 0.48887 0.46057 -0.04066 -0.03582 0.01628  226 LEU A CD2 
1719 N N   . THR A 261 ? 0.49716 0.49027 0.45088 -0.03819 -0.05793 0.02523  227 THR A N   
1720 C CA  . THR A 261 ? 0.50431 0.50379 0.47187 -0.03768 -0.06421 0.02686  227 THR A CA  
1721 C C   . THR A 261 ? 0.50380 0.50300 0.46747 -0.03679 -0.07238 0.02894  227 THR A C   
1722 O O   . THR A 261 ? 0.46729 0.47128 0.44174 -0.03697 -0.07838 0.02897  227 THR A O   
1723 C CB  . THR A 261 ? 0.39284 0.39805 0.37326 -0.03582 -0.06176 0.03149  227 THR A CB  
1724 O OG1 . THR A 261 ? 0.43651 0.44010 0.41190 -0.03362 -0.06192 0.03640  227 THR A OG1 
1725 C CG2 . THR A 261 ? 0.46706 0.47302 0.45089 -0.03629 -0.05392 0.02947  227 THR A CG2 
1726 N N   . GLY A 262 ? 0.47998 0.47394 0.42920 -0.03575 -0.07280 0.03092  228 GLY A N   
1727 C CA  . GLY A 262 ? 0.45796 0.45216 0.40367 -0.03432 -0.08072 0.03361  228 GLY A CA  
1728 C C   . GLY A 262 ? 0.54861 0.54735 0.50466 -0.03187 -0.08310 0.03979  228 GLY A C   
1729 O O   . GLY A 262 ? 0.59330 0.59325 0.54880 -0.03049 -0.09022 0.04219  228 GLY A O   
1730 N N   . ARG A 263 ? 0.38290 0.38450 0.34829 -0.03109 -0.07745 0.04217  229 ARG A N   
1731 C CA  . ARG A 263 ? 0.35845 0.36554 0.33560 -0.02869 -0.07918 0.04739  229 ARG A CA  
1732 C C   . ARG A 263 ? 0.41509 0.41836 0.38546 -0.02640 -0.07562 0.05173  229 ARG A C   
1733 O O   . ARG A 263 ? 0.48245 0.48158 0.44681 -0.02686 -0.06855 0.05080  229 ARG A O   
1734 C CB  . ARG A 263 ? 0.47295 0.48692 0.46607 -0.02898 -0.07569 0.04707  229 ARG A CB  
1735 C CG  . ARG A 263 ? 0.63832 0.65499 0.63833 -0.03149 -0.07788 0.04274  229 ARG A CG  
1736 C CD  . ARG A 263 ? 0.70631 0.72861 0.71955 -0.03180 -0.07310 0.04247  229 ARG A CD  
1737 N NE  . ARG A 263 ? 0.54467 0.57424 0.57082 -0.02953 -0.07356 0.04744  229 ARG A NE  
1738 C CZ  . ARG A 263 ? 0.74144 0.77763 0.78062 -0.02927 -0.07074 0.04841  229 ARG A CZ  
1739 N NH1 . ARG A 263 ? 0.73196 0.76833 0.77375 -0.03105 -0.06756 0.04502  229 ARG A NH1 
1740 N NH2 . ARG A 263 ? 0.75952 0.80255 0.80935 -0.02695 -0.07108 0.05301  229 ARG A NH2 
1741 N N   . LYS A 264 ? 0.47641 0.48118 0.44891 -0.02392 -0.08059 0.05637  230 LYS A N   
1742 C CA  . LYS A 264 ? 0.47738 0.47862 0.44530 -0.02140 -0.07803 0.06095  230 LYS A CA  
1743 C C   . LYS A 264 ? 0.49267 0.49734 0.47093 -0.02038 -0.07143 0.06185  230 LYS A C   
1744 O O   . LYS A 264 ? 0.35740 0.36976 0.34967 -0.02009 -0.07167 0.06163  230 LYS A O   
1745 C CB  . LYS A 264 ? 0.46644 0.46976 0.43692 -0.01874 -0.08556 0.06552  230 LYS A CB  
1746 C CG  . LYS A 264 ? 0.46922 0.47080 0.44038 -0.01557 -0.08350 0.07073  230 LYS A CG  
1747 C CD  . LYS A 264 ? 0.45257 0.44447 0.40666 -0.01523 -0.08129 0.07252  230 LYS A CD  
1748 C CE  . LYS A 264 ? 0.47855 0.46806 0.43356 -0.01186 -0.08069 0.07819  230 LYS A CE  
1749 N NZ  . LYS A 264 ? 0.49885 0.47859 0.43883 -0.01189 -0.07627 0.08012  230 LYS A NZ  
1750 N N   . VAL A 265 ? 0.39461 0.39372 0.36603 -0.01971 -0.06553 0.06294  231 VAL A N   
1751 C CA  . VAL A 265 ? 0.44636 0.44813 0.42646 -0.01833 -0.05953 0.06352  231 VAL A CA  
1752 C C   . VAL A 265 ? 0.41333 0.41455 0.39587 -0.01495 -0.06121 0.06864  231 VAL A C   
1753 O O   . VAL A 265 ? 0.42990 0.42398 0.40184 -0.01419 -0.06217 0.07144  231 VAL A O   
1754 C CB  . VAL A 265 ? 0.48850 0.48469 0.46135 -0.02004 -0.05153 0.06052  231 VAL A CB  
1755 C CG1 . VAL A 265 ? 0.46296 0.46150 0.44429 -0.01826 -0.04593 0.06094  231 VAL A CG1 
1756 C CG2 . VAL A 265 ? 0.38220 0.37985 0.35474 -0.02304 -0.04967 0.05524  231 VAL A CG2 
1757 N N   . TRP A 266 ? 0.36645 0.37530 0.36298 -0.01275 -0.06145 0.07000  232 TRP A N   
1758 C CA  . TRP A 266 ? 0.39244 0.40167 0.39367 -0.00924 -0.06208 0.07415  232 TRP A CA  
1759 C C   . TRP A 266 ? 0.44248 0.45246 0.44886 -0.00831 -0.05457 0.07251  232 TRP A C   
1760 O O   . TRP A 266 ? 0.36194 0.37993 0.37932 -0.00776 -0.05248 0.07065  232 TRP A O   
1761 C CB  . TRP A 266 ? 0.34618 0.36412 0.36002 -0.00706 -0.06788 0.07666  232 TRP A CB  
1762 C CG  . TRP A 266 ? 0.41313 0.43232 0.42527 -0.00805 -0.07580 0.07745  232 TRP A CG  
1763 C CD1 . TRP A 266 ? 0.38082 0.40535 0.39837 -0.01024 -0.07844 0.07497  232 TRP A CD1 
1764 C CD2 . TRP A 266 ? 0.35504 0.37035 0.36043 -0.00670 -0.08237 0.08084  232 TRP A CD2 
1765 N NE1 . TRP A 266 ? 0.39901 0.42323 0.41390 -0.01053 -0.08631 0.07602  232 TRP A NE1 
1766 C CE2 . TRP A 266 ? 0.37882 0.39775 0.38592 -0.00825 -0.08900 0.07960  232 TRP A CE2 
1767 C CE3 . TRP A 266 ? 0.39171 0.40084 0.39007 -0.00421 -0.08342 0.08488  232 TRP A CE3 
1768 C CZ2 . TRP A 266 ? 0.47135 0.48841 0.47289 -0.00733 -0.09688 0.08179  232 TRP A CZ2 
1769 C CZ3 . TRP A 266 ? 0.41615 0.42324 0.40852 -0.00313 -0.09114 0.08773  232 TRP A CZ3 
1770 C CH2 . TRP A 266 ? 0.45295 0.46428 0.44678 -0.00464 -0.09791 0.08595  232 TRP A CH2 
1771 N N   . HIS A 267 ? 0.38365 0.38551 0.38235 -0.00804 -0.05059 0.07326  233 HIS A N   
1772 C CA  . HIS A 267 ? 0.42154 0.42336 0.42526 -0.00710 -0.04377 0.07135  233 HIS A CA  
1773 C C   . HIS A 267 ? 0.49203 0.49658 0.50483 -0.00311 -0.04515 0.07452  233 HIS A C   
1774 O O   . HIS A 267 ? 0.49370 0.49231 0.50213 -0.00150 -0.04751 0.07862  233 HIS A O   
1775 C CB  . HIS A 267 ? 0.30019 0.29192 0.29287 -0.00892 -0.03852 0.07056  233 HIS A CB  
1776 C CG  . HIS A 267 ? 0.42017 0.41088 0.40757 -0.01248 -0.03456 0.06585  233 HIS A CG  
1777 N ND1 . HIS A 267 ? 0.40179 0.38604 0.37618 -0.01511 -0.03508 0.06568  233 HIS A ND1 
1778 C CD2 . HIS A 267 ? 0.36825 0.36395 0.36176 -0.01360 -0.03012 0.06104  233 HIS A CD2 
1779 C CE1 . HIS A 267 ? 0.44376 0.42890 0.41704 -0.01779 -0.03097 0.06081  233 HIS A CE1 
1780 N NE2 . HIS A 267 ? 0.41613 0.40813 0.40099 -0.01692 -0.02806 0.05808  233 HIS A NE2 
1781 N N   . VAL A 268 ? 0.40797 0.42161 0.43331 -0.00131 -0.04358 0.07268  234 VAL A N   
1782 C CA  . VAL A 268 ? 0.45191 0.46970 0.48717 0.00271  -0.04494 0.07507  234 VAL A CA  
1783 C C   . VAL A 268 ? 0.39938 0.42050 0.44223 0.00426  -0.03871 0.07139  234 VAL A C   
1784 O O   . VAL A 268 ? 0.41214 0.43918 0.46516 0.00773  -0.03891 0.07188  234 VAL A O   
1785 C CB  . VAL A 268 ? 0.40553 0.43319 0.45015 0.00416  -0.05038 0.07697  234 VAL A CB  
1786 C CG1 . VAL A 268 ? 0.43412 0.45878 0.47201 0.00273  -0.05719 0.08001  234 VAL A CG1 
1787 C CG2 . VAL A 268 ? 0.36773 0.40444 0.41924 0.00307  -0.04785 0.07352  234 VAL A CG2 
1788 N N   . GLY A 269 ? 0.37449 0.39215 0.41272 0.00186  -0.03323 0.06735  235 GLY A N   
1789 C CA  . GLY A 269 ? 0.34824 0.37033 0.39380 0.00307  -0.02769 0.06284  235 GLY A CA  
1790 C C   . GLY A 269 ? 0.33811 0.35161 0.38050 0.00273  -0.02270 0.06105  235 GLY A C   
1791 O O   . GLY A 269 ? 0.31959 0.32320 0.35426 0.00192  -0.02328 0.06426  235 GLY A O   
1792 N N   . PRO A 270 ? 0.34528 0.36269 0.39408 0.00349  -0.01767 0.05591  236 PRO A N   
1793 C CA  . PRO A 270 ? 0.30238 0.33192 0.36030 0.00519  -0.01661 0.05227  236 PRO A CA  
1794 C C   . PRO A 270 ? 0.30778 0.34453 0.37515 0.00945  -0.01962 0.05456  236 PRO A C   
1795 O O   . PRO A 270 ? 0.38956 0.42323 0.46067 0.01192  -0.01898 0.05493  236 PRO A O   
1796 C CB  . PRO A 270 ? 0.32834 0.35739 0.38896 0.00507  -0.01050 0.04622  236 PRO A CB  
1797 C CG  . PRO A 270 ? 0.35477 0.37116 0.40679 0.00210  -0.00800 0.04667  236 PRO A CG  
1798 C CD  . PRO A 270 ? 0.33917 0.34885 0.38645 0.00268  -0.01240 0.05324  236 PRO A CD  
1799 N N   . THR A 271 ? 0.33920 0.38543 0.41124 0.01041  -0.02276 0.05623  237 THR A N   
1800 C CA  . THR A 271 ? 0.38455 0.43752 0.46556 0.01434  -0.02572 0.05894  237 THR A CA  
1801 C C   . THR A 271 ? 0.42183 0.48089 0.51178 0.01810  -0.02200 0.05495  237 THR A C   
1802 O O   . THR A 271 ? 0.43941 0.50142 0.53637 0.02168  -0.02365 0.05661  237 THR A O   
1803 C CB  . THR A 271 ? 0.34453 0.40698 0.42970 0.01432  -0.02918 0.06145  237 THR A CB  
1804 O OG1 . THR A 271 ? 0.38074 0.45124 0.46868 0.01392  -0.02576 0.05785  237 THR A OG1 
1805 C CG2 . THR A 271 ? 0.32399 0.38052 0.40119 0.01087  -0.03358 0.06490  237 THR A CG2 
1806 N N   . SER A 272 ? 0.38820 0.44949 0.47837 0.01756  -0.01718 0.04935  238 SER A N   
1807 C CA  . SER A 272 ? 0.37423 0.44107 0.47248 0.02122  -0.01380 0.04464  238 SER A CA  
1808 C C   . SER A 272 ? 0.38370 0.44103 0.48264 0.02228  -0.01279 0.04408  238 SER A C   
1809 O O   . SER A 272 ? 0.44496 0.50611 0.55213 0.02615  -0.01184 0.04185  238 SER A O   
1810 C CB  . SER A 272 ? 0.36637 0.43773 0.46440 0.02036  -0.00935 0.03847  238 SER A CB  
1811 O OG  . SER A 272 ? 0.37507 0.43611 0.46593 0.01669  -0.00689 0.03631  238 SER A OG  
1812 N N   . LEU A 273 ? 0.46326 0.50823 0.55387 0.01901  -0.01281 0.04612  239 LEU A N   
1813 C CA  . LEU A 273 ? 0.47335 0.50830 0.56444 0.01989  -0.01213 0.04713  239 LEU A CA  
1814 C C   . LEU A 273 ? 0.48564 0.51775 0.57718 0.02181  -0.01726 0.05377  239 LEU A C   
1815 O O   . LEU A 273 ? 0.46981 0.49843 0.56680 0.02468  -0.01734 0.05444  239 LEU A O   
1816 C CB  . LEU A 273 ? 0.27065 0.29361 0.35256 0.01569  -0.00934 0.04690  239 LEU A CB  
1817 C CG  . LEU A 273 ? 0.44349 0.46848 0.52456 0.01331  -0.00441 0.04038  239 LEU A CG  
1818 C CD1 . LEU A 273 ? 0.41696 0.42971 0.49006 0.00934  -0.00127 0.04052  239 LEU A CD1 
1819 C CD2 . LEU A 273 ? 0.38345 0.41560 0.47509 0.01649  -0.00126 0.03371  239 LEU A CD2 
1820 N N   . MET A 274 ? 0.37139 0.40518 0.45811 0.02041  -0.02174 0.05843  240 MET A N   
1821 C CA  . MET A 274 ? 0.36396 0.39563 0.45115 0.02221  -0.02725 0.06463  240 MET A CA  
1822 C C   . MET A 274 ? 0.50694 0.54761 0.60658 0.02714  -0.02853 0.06444  240 MET A C   
1823 O O   . MET A 274 ? 0.48309 0.52006 0.58595 0.02978  -0.03127 0.06791  240 MET A O   
1824 C CB  . MET A 274 ? 0.41176 0.44516 0.49282 0.01975  -0.03193 0.06848  240 MET A CB  
1825 C CG  . MET A 274 ? 0.44359 0.46767 0.51160 0.01522  -0.03150 0.06924  240 MET A CG  
1826 S SD  . MET A 274 ? 0.49421 0.50624 0.55255 0.01481  -0.03626 0.07608  240 MET A SD  
1827 C CE  . MET A 274 ? 0.46261 0.48287 0.52693 0.01727  -0.04408 0.08056  240 MET A CE  
1828 N N   . VAL A 275 ? 0.40120 0.45388 0.50791 0.02865  -0.02650 0.06054  241 VAL A N   
1829 C CA  . VAL A 275 ? 0.40606 0.46880 0.52441 0.03340  -0.02739 0.06025  241 VAL A CA  
1830 C C   . VAL A 275 ? 0.50602 0.56681 0.63082 0.03660  -0.02383 0.05582  241 VAL A C   
1831 O O   . VAL A 275 ? 0.63250 0.70187 0.76735 0.04090  -0.02339 0.05388  241 VAL A O   
1832 C CB  . VAL A 275 ? 0.45365 0.53052 0.57685 0.03409  -0.02624 0.05821  241 VAL A CB  
1833 C CG1 . VAL A 275 ? 0.43099 0.51019 0.55046 0.03131  -0.03030 0.06297  241 VAL A CG1 
1834 C CG2 . VAL A 275 ? 0.37505 0.45428 0.49629 0.03292  -0.02091 0.05188  241 VAL A CG2 
1835 N N   . GLU A 276 ? 0.56784 0.61753 0.68748 0.03454  -0.02111 0.05399  242 GLU A N   
1836 C CA  . GLU A 276 ? 0.68328 0.72920 0.80960 0.03722  -0.01805 0.05003  242 GLU A CA  
1837 C C   . GLU A 276 ? 0.54737 0.57984 0.67109 0.03712  -0.01999 0.05500  242 GLU A C   
1838 O O   . GLU A 276 ? 0.72935 0.75733 0.85969 0.03963  -0.01829 0.05309  242 GLU A O   
1839 C CB  . GLU A 276 ? 0.61632 0.66109 0.74130 0.03524  -0.01257 0.04301  242 GLU A CB  
1840 C CG  . GLU A 276 ? 0.82034 0.87910 0.94988 0.03677  -0.01033 0.03728  242 GLU A CG  
1841 C CD  . GLU A 276 ? 0.89153 0.94953 1.02097 0.03540  -0.00535 0.02976  242 GLU A CD  
1842 O OE1 . GLU A 276 ? 0.84671 0.89666 0.96822 0.03104  -0.00386 0.02998  242 GLU A OE1 
1843 O OE2 . GLU A 276 ? 1.05177 1.11754 1.18927 0.03879  -0.00297 0.02336  242 GLU A OE2 
1844 N N   . LYS A 294 ? 0.89005 1.07515 1.11999 0.08876  0.02307  -0.12815 260 LYS A N   
1845 C CA  . LYS A 294 ? 0.80870 0.98091 1.03591 0.08174  0.02356  -0.12509 260 LYS A CA  
1846 C C   . LYS A 294 ? 0.80736 0.98902 1.02802 0.08089  0.02354  -0.12934 260 LYS A C   
1847 O O   . LYS A 294 ? 0.84842 1.03963 1.07343 0.08408  0.02350  -0.14130 260 LYS A O   
1848 C CB  . LYS A 294 ? 0.86854 1.02703 1.10756 0.07932  0.02461  -0.13173 260 LYS A CB  
1849 C CG  . LYS A 294 ? 0.82357 0.96670 1.06037 0.07180  0.02570  -0.12677 260 LYS A CG  
1850 C CD  . LYS A 294 ? 0.80732 0.93533 1.05628 0.06952  0.02706  -0.13041 260 LYS A CD  
1851 C CE  . LYS A 294 ? 0.76779 0.87965 1.01354 0.06209  0.02858  -0.12300 260 LYS A CE  
1852 N NZ  . LYS A 294 ? 0.90291 0.99897 1.16002 0.05994  0.03015  -0.12391 260 LYS A NZ  
1853 N N   . HIS A 295 ? 0.64382 0.82275 0.85425 0.07669  0.02334  -0.11963 261 HIS A N   
1854 C CA  . HIS A 295 ? 0.67111 0.85825 0.87491 0.07569  0.02317  -0.12205 261 HIS A CA  
1855 C C   . HIS A 295 ? 0.66932 0.85083 0.87972 0.07270  0.02401  -0.13198 261 HIS A C   
1856 O O   . HIS A 295 ? 0.64393 0.81081 0.86129 0.06886  0.02517  -0.13260 261 HIS A O   
1857 C CB  . HIS A 295 ? 0.65252 0.83507 0.84549 0.07118  0.02287  -0.10934 261 HIS A CB  
1858 C CG  . HIS A 295 ? 0.77330 0.96673 0.95859 0.07140  0.02242  -0.10983 261 HIS A CG  
1859 N ND1 . HIS A 295 ? 0.70335 0.89396 0.88860 0.06788  0.02287  -0.11471 261 HIS A ND1 
1860 C CD2 . HIS A 295 ? 0.80444 1.01169 0.98236 0.07485  0.02161  -0.10583 261 HIS A CD2 
1861 C CE1 . HIS A 295 ? 0.81226 1.01438 0.99033 0.06933  0.02208  -0.11378 261 HIS A CE1 
1862 N NE2 . HIS A 295 ? 0.90944 1.12163 1.08283 0.07352  0.02138  -0.10819 261 HIS A NE2 
1863 N N   . GLN A 296 ? 0.82033 0.80400 0.61077 0.02168  0.09432  -0.04804 262 GLN A N   
1864 C CA  . GLN A 296 ? 0.77170 0.74742 0.55721 0.02498  0.07681  -0.05640 262 GLN A CA  
1865 C C   . GLN A 296 ? 0.75040 0.73408 0.56291 0.01898  0.06530  -0.05570 262 GLN A C   
1866 O O   . GLN A 296 ? 0.67076 0.65387 0.49099 0.01998  0.05308  -0.06396 262 GLN A O   
1867 C CB  . GLN A 296 ? 0.92698 0.88382 0.67645 0.03013  0.07014  -0.05640 262 GLN A CB  
1868 C CG  . GLN A 296 ? 1.00636 0.95766 0.74588 0.02632  0.07201  -0.04544 262 GLN A CG  
1869 C CD  . GLN A 296 ? 1.19226 1.12469 0.90200 0.03141  0.05849  -0.04701 262 GLN A CD  
1870 O OE1 . GLN A 296 ? 1.20535 1.13256 0.91053 0.03631  0.04446  -0.05673 262 GLN A OE1 
1871 N NE2 . GLN A 296 ? 1.19362 1.11488 0.88260 0.03034  0.06219  -0.03774 262 GLN A NE2 
1872 N N   . SER A 297 ? 0.60384 0.59449 0.43060 0.01262  0.06918  -0.04629 263 SER A N   
1873 C CA  . SER A 297 ? 0.68947 0.68750 0.54125 0.00727  0.05924  -0.04552 263 SER A CA  
1874 C C   . SER A 297 ? 0.51537 0.52433 0.39394 0.00542  0.05908  -0.05129 263 SER A C   
1875 O O   . SER A 297 ? 0.56786 0.57759 0.45804 0.00426  0.04792  -0.05719 263 SER A O   
1876 C CB  . SER A 297 ? 0.53292 0.53523 0.39333 0.00127  0.06425  -0.03421 263 SER A CB  
1877 O OG  . SER A 297 ? 0.66029 0.67158 0.53077 -0.00134 0.07948  -0.02921 263 SER A OG  
1878 N N   . LEU A 298 ? 0.50585 0.52267 0.39383 0.00534  0.07146  -0.05014 264 LEU A N   
1879 C CA  . LEU A 298 ? 0.54373 0.56852 0.45453 0.00449  0.07121  -0.05555 264 LEU A CA  
1880 C C   . LEU A 298 ? 0.58435 0.60190 0.48640 0.00937  0.06403  -0.06667 264 LEU A C   
1881 O O   . LEU A 298 ? 0.54551 0.56467 0.46339 0.00743  0.05734  -0.07202 264 LEU A O   
1882 C CB  . LEU A 298 ? 0.55130 0.58578 0.47265 0.00475  0.08542  -0.05275 264 LEU A CB  
1883 C CG  . LEU A 298 ? 0.51585 0.55901 0.45121 -0.00110 0.09230  -0.04242 264 LEU A CG  
1884 C CD1 . LEU A 298 ? 0.56831 0.62186 0.51312 -0.00023 0.10685  -0.04091 264 LEU A CD1 
1885 C CD2 . LEU A 298 ? 0.53883 0.58685 0.49811 -0.00647 0.08396  -0.04062 264 LEU A CD2 
1886 N N   . THR A 299 ? 0.56648 0.57465 0.44222 0.01553  0.06534  -0.07028 265 THR A N   
1887 C CA  . THR A 299 ? 0.56231 0.56205 0.42767 0.02047  0.05753  -0.08121 265 THR A CA  
1888 C C   . THR A 299 ? 0.50771 0.50317 0.37680 0.01793  0.04177  -0.08564 265 THR A C   
1889 O O   . THR A 299 ? 0.57206 0.56587 0.44958 0.01755  0.03441  -0.09398 265 THR A O   
1890 C CB  . THR A 299 ? 0.60875 0.59786 0.44240 0.02805  0.06187  -0.08358 265 THR A CB  
1891 O OG1 . THR A 299 ? 0.65372 0.64872 0.48681 0.03033  0.07767  -0.08079 265 THR A OG1 
1892 C CG2 . THR A 299 ? 0.63539 0.61409 0.45649 0.03351  0.05204  -0.09535 265 THR A CG2 
1893 N N   . TRP A 300 ? 0.54805 0.54156 0.41134 0.01609  0.03652  -0.08044 266 TRP A N   
1894 C CA  . TRP A 300 ? 0.49678 0.48898 0.36731 0.01361  0.02183  -0.08474 266 TRP A CA  
1895 C C   . TRP A 300 ? 0.46347 0.46608 0.36495 0.00639  0.02026  -0.08419 266 TRP A C   
1896 O O   . TRP A 300 ? 0.48558 0.48817 0.39791 0.00415  0.01102  -0.09169 266 TRP A O   
1897 C CB  . TRP A 300 ? 0.54220 0.52974 0.39912 0.01423  0.01686  -0.07898 266 TRP A CB  
1898 C CG  . TRP A 300 ? 0.59591 0.58266 0.45903 0.01312  0.00123  -0.08430 266 TRP A CG  
1899 C CD1 . TRP A 300 ? 0.66008 0.63918 0.51199 0.01745  -0.01105 -0.09431 266 TRP A CD1 
1900 C CD2 . TRP A 300 ? 0.57504 0.56972 0.45827 0.00758  -0.00400 -0.08062 266 TRP A CD2 
1901 N NE1 . TRP A 300 ? 0.61339 0.59663 0.47904 0.01474  -0.02339 -0.09739 266 TRP A NE1 
1902 C CE2 . TRP A 300 ? 0.66515 0.65784 0.54956 0.00885  -0.01894 -0.08904 266 TRP A CE2 
1903 C CE3 . TRP A 300 ? 0.60413 0.60741 0.50470 0.00196  0.00223  -0.07151 266 TRP A CE3 
1904 C CZ2 . TRP A 300 ? 0.55010 0.55003 0.45282 0.00485  -0.02687 -0.08870 266 TRP A CZ2 
1905 C CZ3 . TRP A 300 ? 0.51811 0.52682 0.43465 -0.00180 -0.00601 -0.07082 266 TRP A CZ3 
1906 C CH2 . TRP A 300 ? 0.57547 0.58293 0.49319 -0.00027 -0.01995 -0.07939 266 TRP A CH2 
1907 N N   . LEU A 301 ? 0.45764 0.46853 0.37330 0.00253  0.02944  -0.07567 267 LEU A N   
1908 C CA  . LEU A 301 ? 0.45425 0.47300 0.39666 -0.00373 0.02824  -0.07471 267 LEU A CA  
1909 C C   . LEU A 301 ? 0.41534 0.43327 0.36686 -0.00371 0.02908  -0.08213 267 LEU A C   
1910 O O   . LEU A 301 ? 0.42606 0.44570 0.39462 -0.00849 0.02448  -0.08486 267 LEU A O   
1911 C CB  . LEU A 301 ? 0.44780 0.47430 0.40172 -0.00704 0.03724  -0.06429 267 LEU A CB  
1912 C CG  . LEU A 301 ? 0.43205 0.45881 0.38066 -0.00873 0.03600  -0.05586 267 LEU A CG  
1913 C CD1 . LEU A 301 ? 0.44176 0.47576 0.40220 -0.01212 0.04566  -0.04641 267 LEU A CD1 
1914 C CD2 . LEU A 301 ? 0.36567 0.39284 0.32314 -0.01181 0.02410  -0.05758 267 LEU A CD2 
1915 N N   . ASP A 302 ? 0.45267 0.46684 0.39194 0.00174  0.03504  -0.08561 268 ASP A N   
1916 C CA  . ASP A 302 ? 0.45674 0.46786 0.40200 0.00270  0.03508  -0.09312 268 ASP A CA  
1917 C C   . ASP A 302 ? 0.44577 0.44965 0.39000 0.00132  0.02359  -0.10265 268 ASP A C   
1918 O O   . ASP A 302 ? 0.47235 0.47224 0.42363 0.00024  0.02234  -0.10861 268 ASP A O   
1919 C CB  . ASP A 302 ? 0.45660 0.46502 0.38707 0.00997  0.04348  -0.09554 268 ASP A CB  
1920 C CG  . ASP A 302 ? 0.48931 0.50684 0.43030 0.01032  0.05549  -0.08898 268 ASP A CG  
1921 O OD1 . ASP A 302 ? 0.47866 0.50208 0.44015 0.00550  0.05588  -0.08519 268 ASP A OD1 
1922 O OD2 . ASP A 302 ? 0.48008 0.49887 0.40902 0.01551  0.06457  -0.08801 268 ASP A OD2 
1923 N N   . THR A 303 ? 0.46528 0.46683 0.40107 0.00136  0.01488  -0.10460 269 THR A N   
1924 C CA  . THR A 303 ? 0.48913 0.48565 0.42656 -0.00043 0.00328  -0.11429 269 THR A CA  
1925 C C   . THR A 303 ? 0.47607 0.47891 0.43480 -0.00828 -0.00260 -0.11366 269 THR A C   
1926 O O   . THR A 303 ? 0.49089 0.49165 0.45533 -0.01117 -0.01161 -0.12190 269 THR A O   
1927 C CB  . THR A 303 ? 0.54539 0.53520 0.46090 0.00534  -0.00449 -0.11878 269 THR A CB  
1928 O OG1 . THR A 303 ? 0.49786 0.49169 0.41184 0.00469  -0.00756 -0.11255 269 THR A OG1 
1929 C CG2 . THR A 303 ? 0.45022 0.43286 0.34171 0.01352  0.00237  -0.11899 269 THR A CG2 
1930 N N   . LYS A 304 ? 0.45251 0.46310 0.42354 -0.01187 0.00240  -0.10457 270 LYS A N   
1931 C CA  . LYS A 304 ? 0.45818 0.47502 0.44707 -0.01831 -0.00265 -0.10325 270 LYS A CA  
1932 C C   . LYS A 304 ? 0.41671 0.43524 0.42450 -0.02442 0.00199  -0.10183 270 LYS A C   
1933 O O   . LYS A 304 ? 0.44720 0.46393 0.45521 -0.02315 0.00983  -0.09874 270 LYS A O   
1934 C CB  . LYS A 304 ? 0.43140 0.45373 0.41844 -0.01761 -0.00188 -0.09415 270 LYS A CB  
1935 C CG  . LYS A 304 ? 0.45329 0.47127 0.41943 -0.01163 -0.00767 -0.09534 270 LYS A CG  
1936 C CD  . LYS A 304 ? 0.48277 0.49863 0.44945 -0.01151 -0.02022 -0.10614 270 LYS A CD  
1937 C CE  . LYS A 304 ? 0.54466 0.55389 0.48840 -0.00442 -0.02768 -0.10829 270 LYS A CE  
1938 N NZ  . LYS A 304 ? 0.61469 0.62348 0.56242 -0.00429 -0.04151 -0.11954 270 LYS A NZ  
1939 N N   . GLU A 305 ? 0.47649 0.49808 0.49977 -0.03075 -0.00298 -0.10448 271 GLU A N   
1940 C CA  . GLU A 305 ? 0.40641 0.42723 0.44539 -0.03696 0.00103  -0.10336 271 GLU A CA  
1941 C C   . GLU A 305 ? 0.48684 0.51251 0.53225 -0.03742 0.00749  -0.09270 271 GLU A C   
1942 O O   . GLU A 305 ? 0.44005 0.47140 0.48221 -0.03518 0.00718  -0.08670 271 GLU A O   
1943 C CB  . GLU A 305 ? 0.55387 0.57734 0.60721 -0.04389 -0.00502 -0.10909 271 GLU A CB  
1944 C CG  . GLU A 305 ? 0.58568 0.60227 0.63967 -0.04694 -0.00922 -0.12006 271 GLU A CG  
1945 C CD  . GLU A 305 ? 0.71126 0.71662 0.75856 -0.04599 -0.00383 -0.12137 271 GLU A CD  
1946 O OE1 . GLU A 305 ? 0.67329 0.67362 0.72923 -0.05124 0.00054  -0.12007 271 GLU A OE1 
1947 O OE2 . GLU A 305 ? 0.69644 0.69685 0.72862 -0.03956 -0.00420 -0.12402 271 GLU A OE2 
1948 N N   . PRO A 306 ? 0.53349 0.55563 0.58706 -0.04013 0.01279  -0.09035 272 PRO A N   
1949 C CA  . PRO A 306 ? 0.51079 0.53702 0.57139 -0.04049 0.01780  -0.08090 272 PRO A CA  
1950 C C   . PRO A 306 ? 0.43399 0.46715 0.50326 -0.04393 0.01429  -0.07703 272 PRO A C   
1951 O O   . PRO A 306 ? 0.34152 0.37557 0.41808 -0.04831 0.00966  -0.08192 272 PRO A O   
1952 C CB  . PRO A 306 ? 0.44805 0.46650 0.51566 -0.04335 0.02129  -0.08156 272 PRO A CB  
1953 C CG  . PRO A 306 ? 0.56123 0.57097 0.62078 -0.04197 0.02031  -0.09002 272 PRO A CG  
1954 C CD  . PRO A 306 ? 0.46994 0.48227 0.52486 -0.04245 0.01390  -0.09632 272 PRO A CD  
1955 N N   . SER A 307 ? 0.33972 0.37801 0.40851 -0.04188 0.01663  -0.06855 273 SER A N   
1956 C CA  . SER A 307 ? 0.42726 0.47110 0.50344 -0.04422 0.01366  -0.06363 273 SER A CA  
1957 C C   . SER A 307 ? 0.37113 0.41855 0.44520 -0.04414 0.00569  -0.06856 273 SER A C   
1958 O O   . SER A 307 ? 0.46202 0.51379 0.54514 -0.04671 0.00195  -0.06782 273 SER A O   
1959 C CB  . SER A 307 ? 0.32911 0.37133 0.41901 -0.04929 0.01508  -0.06223 273 SER A CB  
1960 O OG  . SER A 307 ? 0.45141 0.48968 0.54300 -0.04845 0.02087  -0.05765 273 SER A OG  
1961 N N   . SER A 308 ? 0.37560 0.42111 0.43753 -0.04052 0.00247  -0.07401 274 SER A N   
1962 C CA  . SER A 308 ? 0.37411 0.42221 0.43456 -0.03986 -0.00667 -0.08054 274 SER A CA  
1963 C C   . SER A 308 ? 0.42541 0.47407 0.47185 -0.03445 -0.01076 -0.07670 274 SER A C   
1964 O O   . SER A 308 ? 0.34827 0.39876 0.39304 -0.03281 -0.01980 -0.08193 274 SER A O   
1965 C CB  . SER A 308 ? 0.42479 0.46850 0.48055 -0.03943 -0.00990 -0.09083 274 SER A CB  
1966 O OG  . SER A 308 ? 0.44573 0.48381 0.48363 -0.03373 -0.00711 -0.09027 274 SER A OG  
1967 N N   . VAL A 309 ? 0.33004 0.37663 0.36636 -0.03172 -0.00457 -0.06809 275 VAL A N   
1968 C CA  . VAL A 309 ? 0.37495 0.41859 0.39346 -0.02675 -0.00699 -0.06408 275 VAL A CA  
1969 C C   . VAL A 309 ? 0.34748 0.39334 0.36942 -0.02806 -0.00481 -0.05394 275 VAL A C   
1970 O O   . VAL A 309 ? 0.34796 0.39571 0.37798 -0.03071 0.00299  -0.04765 275 VAL A O   
1971 C CB  . VAL A 309 ? 0.44691 0.48471 0.44711 -0.02247 -0.00062 -0.06312 275 VAL A CB  
1972 C CG1 . VAL A 309 ? 0.36611 0.39859 0.34552 -0.01800 -0.00164 -0.05776 275 VAL A CG1 
1973 C CG2 . VAL A 309 ? 0.39355 0.42758 0.38838 -0.02045 -0.00405 -0.07365 275 VAL A CG2 
1974 N N   . LEU A 310 ? 0.39875 0.44356 0.41420 -0.02580 -0.01253 -0.05279 276 LEU A N   
1975 C CA  . LEU A 310 ? 0.32145 0.36562 0.33547 -0.02619 -0.01162 -0.04315 276 LEU A CA  
1976 C C   . LEU A 310 ? 0.43856 0.47520 0.43094 -0.02309 -0.00630 -0.03646 276 LEU A C   
1977 O O   . LEU A 310 ? 0.44367 0.47331 0.41648 -0.01833 -0.01059 -0.03941 276 LEU A O   
1978 C CB  . LEU A 310 ? 0.32305 0.36821 0.33879 -0.02449 -0.02289 -0.04543 276 LEU A CB  
1979 C CG  . LEU A 310 ? 0.46189 0.50405 0.47340 -0.02415 -0.02370 -0.03588 276 LEU A CG  
1980 C CD1 . LEU A 310 ? 0.37940 0.42761 0.41111 -0.02929 -0.01911 -0.03137 276 LEU A CD1 
1981 C CD2 . LEU A 310 ? 0.35205 0.39189 0.35716 -0.01972 -0.03623 -0.03909 276 LEU A CD2 
1982 N N   . TYR A 311 ? 0.39095 0.42857 0.38662 -0.02583 0.00314  -0.02783 277 TYR A N   
1983 C CA  . TYR A 311 ? 0.41507 0.44648 0.39265 -0.02441 0.01002  -0.02049 277 TYR A CA  
1984 C C   . TYR A 311 ? 0.44625 0.47223 0.41627 -0.02454 0.00558  -0.01307 277 TYR A C   
1985 O O   . TYR A 311 ? 0.43107 0.46104 0.41621 -0.02772 0.00361  -0.00938 277 TYR A O   
1986 C CB  . TYR A 311 ? 0.34878 0.38535 0.33634 -0.02762 0.02240  -0.01572 277 TYR A CB  
1987 C CG  . TYR A 311 ? 0.36829 0.40067 0.34121 -0.02762 0.03175  -0.00795 277 TYR A CG  
1988 C CD1 . TYR A 311 ? 0.47522 0.49988 0.42425 -0.02349 0.03441  -0.00951 277 TYR A CD1 
1989 C CD2 . TYR A 311 ? 0.35599 0.39178 0.33898 -0.03202 0.03840  0.00066  277 TYR A CD2 
1990 C CE1 . TYR A 311 ? 0.44185 0.46222 0.37682 -0.02416 0.04465  -0.00232 277 TYR A CE1 
1991 C CE2 . TYR A 311 ? 0.39639 0.42911 0.36779 -0.03320 0.04815  0.00758  277 TYR A CE2 
1992 C CZ  . TYR A 311 ? 0.49064 0.51564 0.43776 -0.02947 0.05190  0.00622  277 TYR A CZ  
1993 O OH  . TYR A 311 ? 0.46352 0.48493 0.39829 -0.03127 0.06314  0.01322  277 TYR A OH  
1994 N N   . ILE A 312 ? 0.42048 0.43567 0.36545 -0.02070 0.00357  -0.01107 278 ILE A N   
1995 C CA  . ILE A 312 ? 0.43683 0.44316 0.36954 -0.01997 -0.00160 -0.00428 278 ILE A CA  
1996 C C   . ILE A 312 ? 0.50590 0.50290 0.41848 -0.02093 0.00865  0.00457  278 ILE A C   
1997 O O   . ILE A 312 ? 0.51516 0.50519 0.40739 -0.01761 0.01246  0.00269  278 ILE A O   
1998 C CB  . ILE A 312 ? 0.47294 0.47192 0.39153 -0.01379 -0.01582 -0.01063 278 ILE A CB  
1999 C CG1 . ILE A 312 ? 0.40439 0.41438 0.34398 -0.01335 -0.02407 -0.02128 278 ILE A CG1 
2000 C CG2 . ILE A 312 ? 0.40894 0.39839 0.31682 -0.01258 -0.02262 -0.00401 278 ILE A CG2 
2001 C CD1 . ILE A 312 ? 0.64077 0.64604 0.56938 -0.00692 -0.03813 -0.03002 278 ILE A CD1 
2002 N N   . SER A 313 ? 0.50977 0.50603 0.42746 -0.02563 0.01330  0.01403  279 SER A N   
2003 C CA  . SER A 313 ? 0.58121 0.56891 0.48180 -0.02814 0.02412  0.02305  279 SER A CA  
2004 C C   . SER A 313 ? 0.51496 0.49868 0.41958 -0.03268 0.02338  0.03247  279 SER A C   
2005 O O   . SER A 313 ? 0.53513 0.52923 0.46467 -0.03689 0.02434  0.03413  279 SER A O   
2006 C CB  . SER A 313 ? 0.51162 0.50924 0.42287 -0.03133 0.03872  0.02330  279 SER A CB  
2007 O OG  . SER A 313 ? 0.61817 0.60936 0.51565 -0.03466 0.05051  0.03176  279 SER A OG  
2008 N N   . PHE A 314 ? 0.61038 0.57745 0.48908 -0.03164 0.02136  0.03858  280 PHE A N   
2009 C CA  . PHE A 314 ? 0.67311 0.63302 0.55139 -0.03607 0.02079  0.04809  280 PHE A CA  
2010 C C   . PHE A 314 ? 0.72653 0.67864 0.59147 -0.04181 0.03506  0.05767  280 PHE A C   
2011 O O   . PHE A 314 ? 0.64678 0.59176 0.51062 -0.04668 0.03598  0.06622  280 PHE A O   
2012 C CB  . PHE A 314 ? 0.60965 0.55445 0.46891 -0.03064 0.00581  0.04798  280 PHE A CB  
2013 C CG  . PHE A 314 ? 0.56887 0.52309 0.44587 -0.02628 -0.00780 0.03931  280 PHE A CG  
2014 C CD1 . PHE A 314 ? 0.50066 0.46072 0.37864 -0.02086 -0.01337 0.02862  280 PHE A CD1 
2015 C CD2 . PHE A 314 ? 0.56990 0.52724 0.46309 -0.02789 -0.01451 0.04154  280 PHE A CD2 
2016 C CE1 . PHE A 314 ? 0.50923 0.47900 0.40528 -0.01787 -0.02457 0.02034  280 PHE A CE1 
2017 C CE2 . PHE A 314 ? 0.53892 0.50561 0.44879 -0.02418 -0.02547 0.03332  280 PHE A CE2 
2018 C CZ  . PHE A 314 ? 0.58858 0.56203 0.50062 -0.01956 -0.03007 0.02270  280 PHE A CZ  
2019 N N   . GLY A 315 ? 0.72124 0.67432 0.57613 -0.04158 0.04651  0.05628  281 GLY A N   
2020 C CA  . GLY A 315 ? 0.67946 0.62726 0.52389 -0.04762 0.06210  0.06469  281 GLY A CA  
2021 C C   . GLY A 315 ? 0.73011 0.65300 0.53705 -0.04675 0.06091  0.07158  281 GLY A C   
2022 O O   . GLY A 315 ? 0.80927 0.71828 0.59455 -0.03962 0.04785  0.06849  281 GLY A O   
2023 N N   . SER A 316 ? 0.84019 0.75688 0.63959 -0.05427 0.07477  0.08092  282 SER A N   
2024 C CA  . SER A 316 ? 0.94338 0.83400 0.70441 -0.05491 0.07707  0.08879  282 SER A CA  
2025 C C   . SER A 316 ? 0.94338 0.82113 0.70148 -0.05864 0.06878  0.09673  282 SER A C   
2026 O O   . SER A 316 ? 0.82745 0.68266 0.55548 -0.05379 0.05814  0.09879  282 SER A O   
2027 C CB  . SER A 316 ? 0.86017 0.74963 0.61217 -0.06170 0.09851  0.09454  282 SER A CB  
2028 O OG  . SER A 316 ? 1.12454 1.03757 0.91409 -0.06916 0.10938  0.09495  282 SER A OG  
2029 N N   . LEU A 317 ? 0.94193 0.83273 0.73021 -0.06666 0.07277  0.10086  283 LEU A N   
2030 C CA  . LEU A 317 ? 0.86874 0.74731 0.65551 -0.07054 0.06508  0.10836  283 LEU A CA  
2031 C C   . LEU A 317 ? 0.91057 0.78373 0.69445 -0.06172 0.04411  0.10316  283 LEU A C   
2032 O O   . LEU A 317 ? 0.85369 0.70431 0.61071 -0.05866 0.03453  0.10707  283 LEU A O   
2033 C CB  . LEU A 317 ? 0.92537 0.82148 0.74877 -0.07967 0.07153  0.11172  283 LEU A CB  
2034 C CG  . LEU A 317 ? 1.02324 0.90551 0.84360 -0.08739 0.07063  0.12196  283 LEU A CG  
2035 C CD1 . LEU A 317 ? 0.82563 0.67912 0.60403 -0.08921 0.07507  0.13012  283 LEU A CD1 
2036 C CD2 . LEU A 317 ? 0.84754 0.74682 0.70029 -0.09801 0.08291  0.12559  283 LEU A CD2 
2037 N N   . CYS A 318 ? 0.79866 0.69192 0.60978 -0.05745 0.03691  0.09404  284 CYS A N   
2038 C CA  . CYS A 318 ? 0.85714 0.74945 0.67106 -0.04963 0.01832  0.08794  284 CYS A CA  
2039 C C   . CYS A 318 ? 0.87624 0.76403 0.67148 -0.03982 0.01004  0.07919  284 CYS A C   
2040 O O   . CYS A 318 ? 0.81592 0.71591 0.62726 -0.03426 -0.00024 0.06991  284 CYS A O   
2041 C CB  . CYS A 318 ? 0.83051 0.74547 0.68345 -0.05104 0.01533  0.08307  284 CYS A CB  
2042 S SG  . CYS A 318 ? 0.81581 0.73798 0.69355 -0.06219 0.02489  0.09195  284 CYS A SG  
2043 N N   . ARG A 319 ? 0.88387 0.75361 0.64484 -0.03764 0.01425  0.08167  285 ARG A N   
2044 C CA  . ARG A 319 ? 1.00397 0.86683 0.74450 -0.02767 0.00484  0.07319  285 ARG A CA  
2045 C C   . ARG A 319 ? 0.88591 0.73572 0.61412 -0.01980 -0.01503 0.07047  285 ARG A C   
2046 O O   . ARG A 319 ? 0.80906 0.64351 0.52586 -0.02140 -0.01939 0.07796  285 ARG A O   
2047 C CB  . ARG A 319 ? 0.96991 0.81478 0.67432 -0.02707 0.01506  0.07685  285 ARG A CB  
2048 C CG  . ARG A 319 ? 1.02929 0.84574 0.69935 -0.02947 0.01670  0.08785  285 ARG A CG  
2049 C CD  . ARG A 319 ? 1.07619 0.87543 0.71056 -0.02941 0.02931  0.09130  285 ARG A CD  
2050 N NE  . ARG A 319 ? 1.29865 1.06743 0.89626 -0.03191 0.03133  0.10205  285 ARG A NE  
2051 C CZ  . ARG A 319 ? 1.55545 1.29692 1.11568 -0.02338 0.01755  0.10193  285 ARG A CZ  
2052 N NH1 . ARG A 319 ? 1.44502 1.18711 1.00109 -0.01165 0.00021  0.09111  285 ARG A NH1 
2053 N NH2 . ARG A 319 ? 1.58515 1.29731 1.11123 -0.02672 0.02093  0.11264  285 ARG A NH2 
2054 N N   . LEU A 320 ? 0.78027 0.63653 0.51172 -0.01117 -0.02736 0.05912  286 LEU A N   
2055 C CA  . LEU A 320 ? 0.80434 0.65488 0.53284 -0.00297 -0.04700 0.05365  286 LEU A CA  
2056 C C   . LEU A 320 ? 0.82556 0.64858 0.51124 0.00555  -0.05677 0.05361  286 LEU A C   
2057 O O   . LEU A 320 ? 0.80534 0.61597 0.46445 0.00650  -0.04939 0.05509  286 LEU A O   
2058 C CB  . LEU A 320 ? 0.71683 0.58985 0.47382 0.00142  -0.05545 0.04058  286 LEU A CB  
2059 C CG  . LEU A 320 ? 0.74429 0.64284 0.54100 -0.00602 -0.04625 0.03945  286 LEU A CG  
2060 C CD1 . LEU A 320 ? 0.68153 0.59884 0.50135 -0.00198 -0.05366 0.02644  286 LEU A CD1 
2061 C CD2 . LEU A 320 ? 0.73435 0.63462 0.54670 -0.01058 -0.04757 0.04611  286 LEU A CD2 
2062 N N   . SER A 321 ? 0.83170 0.64459 0.51021 0.01251  -0.07404 0.05138  287 SER A N   
2063 C CA  . SER A 321 ? 0.86243 0.64783 0.50049 0.02217  -0.08667 0.05041  287 SER A CA  
2064 C C   . SER A 321 ? 0.81356 0.60451 0.44900 0.03179  -0.09728 0.03690  287 SER A C   
2065 O O   . SER A 321 ? 0.76358 0.58033 0.43163 0.03132  -0.09765 0.02759  287 SER A O   
2066 C CB  . SER A 321 ? 0.84306 0.61668 0.47637 0.02738  -0.10290 0.05145  287 SER A CB  
2067 O OG  . SER A 321 ? 0.77133 0.56581 0.43459 0.03338  -0.11669 0.03940  287 SER A OG  
2068 N N   . ASN A 322 ? 0.91647 0.68106 0.51119 0.04064  -0.10655 0.03583  288 ASN A N   
2069 C CA  . ASN A 322 ? 0.88315 0.64934 0.47123 0.05072  -0.11863 0.02273  288 ASN A CA  
2070 C C   . ASN A 322 ? 0.83542 0.62207 0.45583 0.05674  -0.13599 0.01004  288 ASN A C   
2071 O O   . ASN A 322 ? 0.82521 0.63214 0.46829 0.05839  -0.13870 -0.00130 288 ASN A O   
2072 C CB  . ASN A 322 ? 0.86679 0.59744 0.40286 0.06036  -0.12827 0.02412  288 ASN A CB  
2073 C CG  . ASN A 322 ? 1.10461 0.81651 0.60736 0.05544  -0.11022 0.03372  288 ASN A CG  
2074 O OD1 . ASN A 322 ? 1.09514 0.82366 0.61404 0.04784  -0.09317 0.03472  288 ASN A OD1 
2075 N ND2 . ASN A 322 ? 1.18211 0.85839 0.63716 0.06001  -0.11369 0.04066  288 ASN A ND2 
2076 N N   . GLU A 323 ? 0.86046 0.64170 0.48325 0.05999  -0.14768 0.01152  289 GLU A N   
2077 C CA  . GLU A 323 ? 0.85883 0.66072 0.51405 0.06540  -0.16289 -0.00045 289 GLU A CA  
2078 C C   . GLU A 323 ? 0.81889 0.65397 0.52103 0.05598  -0.15164 -0.00293 289 GLU A C   
2079 O O   . GLU A 323 ? 0.75200 0.60887 0.48257 0.05856  -0.15870 -0.01533 289 GLU A O   
2080 C CB  . GLU A 323 ? 0.85175 0.64038 0.49930 0.07045  -0.17578 0.00278  289 GLU A CB  
2081 C CG  . GLU A 323 ? 1.07078 0.87585 0.74388 0.07931  -0.19464 -0.01108 289 GLU A CG  
2082 C CD  . GLU A 323 ? 1.24593 1.03974 0.91445 0.08387  -0.20584 -0.00756 289 GLU A CD  
2083 O OE1 . GLU A 323 ? 1.28244 1.05326 0.92547 0.08002  -0.19970 0.00594  289 GLU A OE1 
2084 O OE2 . GLU A 323 ? 1.16401 0.97217 0.85512 0.09105  -0.22037 -0.01850 289 GLU A OE2 
2085 N N   . GLN A 324 ? 0.79108 0.62967 0.50152 0.04489  -0.13413 0.00853  290 GLN A N   
2086 C CA  . GLN A 324 ? 0.70252 0.56962 0.45434 0.03631  -0.12349 0.00680  290 GLN A CA  
2087 C C   . GLN A 324 ? 0.63650 0.51738 0.39808 0.03423  -0.11570 -0.00003 290 GLN A C   
2088 O O   . GLN A 324 ? 0.61876 0.52295 0.41314 0.03221  -0.11570 -0.00846 290 GLN A O   
2089 C CB  . GLN A 324 ? 0.67178 0.53751 0.42857 0.02581  -0.10818 0.02037  290 GLN A CB  
2090 C CG  . GLN A 324 ? 0.68920 0.58150 0.48625 0.01748  -0.09786 0.01928  290 GLN A CG  
2091 C CD  . GLN A 324 ? 0.64985 0.55767 0.47512 0.02035  -0.10877 0.01181  290 GLN A CD  
2092 O OE1 . GLN A 324 ? 0.71668 0.62084 0.54620 0.01957  -0.11199 0.01700  290 GLN A OE1 
2093 N NE2 . GLN A 324 ? 0.62600 0.55100 0.47067 0.02352  -0.11422 -0.00068 290 GLN A NE2 
2094 N N   . LEU A 325 ? 0.69170 0.55729 0.42395 0.03474  -0.10885 0.00340  291 LEU A N   
2095 C CA  . LEU A 325 ? 0.64608 0.52257 0.38463 0.03358  -0.10185 -0.00320 291 LEU A CA  
2096 C C   . LEU A 325 ? 0.70539 0.58993 0.45216 0.04191  -0.11795 -0.01848 291 LEU A C   
2097 O O   . LEU A 325 ? 0.71239 0.61581 0.48312 0.03938  -0.11489 -0.02659 291 LEU A O   
2098 C CB  . LEU A 325 ? 0.71808 0.57436 0.42011 0.03353  -0.09164 0.00348  291 LEU A CB  
2099 C CG  . LEU A 325 ? 0.78580 0.63912 0.48558 0.02343  -0.07227 0.01731  291 LEU A CG  
2100 C CD1 . LEU A 325 ? 0.82186 0.65458 0.48396 0.02372  -0.06173 0.02331  291 LEU A CD1 
2101 C CD2 . LEU A 325 ? 0.69766 0.57753 0.43609 0.01483  -0.05978 0.01646  291 LEU A CD2 
2102 N N   . LYS A 326 ? 0.72259 0.59276 0.45032 0.05186  -0.13568 -0.02296 292 LYS A N   
2103 C CA  . LYS A 326 ? 0.77126 0.65025 0.50945 0.06008  -0.15254 -0.03848 292 LYS A CA  
2104 C C   . LYS A 326 ? 0.69257 0.59964 0.47613 0.05656  -0.15543 -0.04597 292 LYS A C   
2105 O O   . LYS A 326 ? 0.65641 0.58152 0.46338 0.05581  -0.15734 -0.05708 292 LYS A O   
2106 C CB  . LYS A 326 ? 0.77396 0.63066 0.48183 0.07226  -0.17180 -0.04156 292 LYS A CB  
2107 C CG  . LYS A 326 ? 0.85788 0.68761 0.52059 0.07857  -0.17343 -0.04003 292 LYS A CG  
2108 C CD  . LYS A 326 ? 0.93318 0.73992 0.56591 0.09185  -0.19485 -0.04445 292 LYS A CD  
2109 C CE  . LYS A 326 ? 1.01051 0.78118 0.58996 0.09498  -0.19100 -0.03373 292 LYS A CE  
2110 N NZ  . LYS A 326 ? 1.09828 0.84893 0.64467 0.10766  -0.20687 -0.04286 292 LYS A NZ  
2111 N N   . GLU A 327 ? 0.64247 0.55246 0.43799 0.05426  -0.15561 -0.04011 293 GLU A N   
2112 C CA  . GLU A 327 ? 0.62013 0.55562 0.45709 0.05041  -0.15617 -0.04613 293 GLU A CA  
2113 C C   . GLU A 327 ? 0.63153 0.58528 0.49340 0.04012  -0.13985 -0.04566 293 GLU A C   
2114 O O   . GLU A 327 ? 0.66591 0.64039 0.55867 0.03781  -0.14098 -0.05522 293 GLU A O   
2115 C CB  . GLU A 327 ? 0.64139 0.57393 0.48279 0.04915  -0.15668 -0.03793 293 GLU A CB  
2116 C CG  . GLU A 327 ? 0.77920 0.69591 0.60114 0.06014  -0.17493 -0.04022 293 GLU A CG  
2117 C CD  . GLU A 327 ? 0.81293 0.74721 0.66063 0.06701  -0.19039 -0.05525 293 GLU A CD  
2118 O OE1 . GLU A 327 ? 0.71204 0.67112 0.59424 0.06185  -0.18554 -0.06287 293 GLU A OE1 
2119 O OE2 . GLU A 327 ? 1.12751 1.05042 0.96087 0.07762  -0.20737 -0.05969 293 GLU A OE2 
2120 N N   . MET A 328 ? 0.62349 0.56925 0.47195 0.03390  -0.12451 -0.03492 294 MET A N   
2121 C CA  . MET A 328 ? 0.59542 0.55647 0.46511 0.02506  -0.10945 -0.03425 294 MET A CA  
2122 C C   . MET A 328 ? 0.58764 0.55590 0.46154 0.02693  -0.11179 -0.04574 294 MET A C   
2123 O O   . MET A 328 ? 0.56494 0.55143 0.46743 0.02230  -0.10848 -0.05237 294 MET A O   
2124 C CB  . MET A 328 ? 0.51988 0.47055 0.37335 0.01919  -0.09354 -0.02111 294 MET A CB  
2125 C CG  . MET A 328 ? 0.76818 0.73210 0.63903 0.01172  -0.07870 -0.02093 294 MET A CG  
2126 S SD  . MET A 328 ? 0.79348 0.75601 0.66700 0.00269  -0.06133 -0.00605 294 MET A SD  
2127 C CE  . MET A 328 ? 0.69748 0.66867 0.59552 0.00064  -0.06746 -0.00426 294 MET A CE  
2128 N N   . ALA A 329 ? 0.59141 0.54386 0.43554 0.03373  -0.11772 -0.04825 295 ALA A N   
2129 C CA  . ALA A 329 ? 0.65567 0.61258 0.50085 0.03604  -0.12079 -0.05927 295 ALA A CA  
2130 C C   . ALA A 329 ? 0.67531 0.64878 0.54784 0.03849  -0.13422 -0.07344 295 ALA A C   
2131 O O   . ALA A 329 ? 0.62397 0.61129 0.51686 0.03479  -0.13173 -0.08172 295 ALA A O   
2132 C CB  . ALA A 329 ? 0.70318 0.63729 0.50802 0.04428  -0.12665 -0.05947 295 ALA A CB  
2133 N N   . ASN A 330 ? 0.58014 0.55241 0.45405 0.04457  -0.14833 -0.07669 296 ASN A N   
2134 C CA  . ASN A 330 ? 0.60173 0.59210 0.50497 0.04661  -0.16042 -0.09054 296 ASN A CA  
2135 C C   . ASN A 330 ? 0.59576 0.60820 0.53678 0.03670  -0.14973 -0.09081 296 ASN A C   
2136 O O   . ASN A 330 ? 0.56479 0.59324 0.53054 0.03338  -0.15035 -0.10135 296 ASN A O   
2137 C CB  . ASN A 330 ? 0.57750 0.56220 0.47475 0.05567  -0.17698 -0.09333 296 ASN A CB  
2138 C CG  . ASN A 330 ? 0.73236 0.69541 0.59379 0.06695  -0.19122 -0.09659 296 ASN A CG  
2139 O OD1 . ASN A 330 ? 0.70795 0.66816 0.56080 0.06973  -0.19513 -0.10426 296 ASN A OD1 
2140 N ND2 . ASN A 330 ? 0.85768 0.80345 0.69617 0.07384  -0.19956 -0.09080 296 ASN A ND2 
2141 N N   . GLY A 331 ? 0.58551 0.59777 0.53053 0.03178  -0.14008 -0.07940 297 GLY A N   
2142 C CA  . GLY A 331 ? 0.48056 0.51074 0.45772 0.02290  -0.12979 -0.07890 297 GLY A CA  
2143 C C   . GLY A 331 ? 0.51508 0.55093 0.50014 0.01547  -0.11702 -0.07932 297 GLY A C   
2144 O O   . GLY A 331 ? 0.51509 0.56636 0.52684 0.01012  -0.11392 -0.08636 297 GLY A O   
2145 N N   . ILE A 332 ? 0.55144 0.57413 0.51262 0.01520  -0.10930 -0.07208 298 ILE A N   
2146 C CA  . ILE A 332 ? 0.56028 0.58686 0.52649 0.00943  -0.09770 -0.07268 298 ILE A CA  
2147 C C   . ILE A 332 ? 0.60548 0.63807 0.57893 0.01128  -0.10541 -0.08664 298 ILE A C   
2148 O O   . ILE A 332 ? 0.52861 0.57232 0.52287 0.00517  -0.09969 -0.09181 298 ILE A O   
2149 C CB  . ILE A 332 ? 0.55857 0.57002 0.49679 0.00985  -0.08815 -0.06270 298 ILE A CB  
2150 C CG1 . ILE A 332 ? 0.61935 0.62908 0.55910 0.00492  -0.07747 -0.04947 298 ILE A CG1 
2151 C CG2 . ILE A 332 ? 0.59905 0.61284 0.53830 0.00680  -0.07953 -0.06611 298 ILE A CG2 
2152 C CD1 . ILE A 332 ? 0.52883 0.55336 0.49840 -0.00290 -0.06881 -0.04881 298 ILE A CD1 
2153 N N   . GLU A 333 ? 0.62496 0.64899 0.58063 0.01977  -0.11907 -0.09316 299 GLU A N   
2154 C CA  . GLU A 333 ? 0.67480 0.70426 0.63779 0.02196  -0.12830 -0.10736 299 GLU A CA  
2155 C C   . GLU A 333 ? 0.61025 0.65956 0.60916 0.01825  -0.13357 -0.11751 299 GLU A C   
2156 O O   . GLU A 333 ? 0.58265 0.64212 0.60043 0.01301  -0.13130 -0.12586 299 GLU A O   
2157 C CB  . GLU A 333 ? 0.62926 0.64417 0.56474 0.03288  -0.14353 -0.11240 299 GLU A CB  
2158 C CG  . GLU A 333 ? 0.76244 0.78278 0.70610 0.03589  -0.15548 -0.12817 299 GLU A CG  
2159 C CD  . GLU A 333 ? 0.89453 0.89705 0.80613 0.04743  -0.17027 -0.13281 299 GLU A CD  
2160 O OE1 . GLU A 333 ? 0.90011 0.88573 0.78312 0.05317  -0.17174 -0.12378 299 GLU A OE1 
2161 O OE2 . GLU A 333 ? 0.85892 0.86302 0.77291 0.05068  -0.18061 -0.14556 299 GLU A OE2 
2162 N N   . ALA A 334 ? 0.55372 0.60834 0.56234 0.02065  -0.14003 -0.11698 300 ALA A N   
2163 C CA  . ALA A 334 ? 0.59008 0.66457 0.63361 0.01698  -0.14342 -0.12643 300 ALA A CA  
2164 C C   . ALA A 334 ? 0.56824 0.65343 0.63451 0.00577  -0.12758 -0.12271 300 ALA A C   
2165 O O   . ALA A 334 ? 0.59267 0.69355 0.68738 0.00072  -0.12750 -0.13166 300 ALA A O   
2166 C CB  . ALA A 334 ? 0.60396 0.68094 0.65134 0.02263  -0.15264 -0.12579 300 ALA A CB  
2167 N N   . SER A 335 ? 0.50132 0.57800 0.55573 0.00178  -0.11421 -0.11007 301 SER A N   
2168 C CA  . SER A 335 ? 0.55342 0.63782 0.62682 -0.00788 -0.10020 -0.10667 301 SER A CA  
2169 C C   . SER A 335 ? 0.53896 0.62648 0.62014 -0.01290 -0.09617 -0.11433 301 SER A C   
2170 O O   . SER A 335 ? 0.54070 0.63570 0.64121 -0.02092 -0.08723 -0.11520 301 SER A O   
2171 C CB  . SER A 335 ? 0.46770 0.54240 0.52717 -0.01004 -0.08832 -0.09193 301 SER A CB  
2172 O OG  . SER A 335 ? 0.47577 0.54050 0.51639 -0.00974 -0.08264 -0.08894 301 SER A OG  
2173 N N   . LYS A 336 ? 0.53173 0.61188 0.59653 -0.00816 -0.10282 -0.11986 302 LYS A N   
2174 C CA  . LYS A 336 ? 0.53202 0.61275 0.60084 -0.01179 -0.10086 -0.12782 302 LYS A CA  
2175 C C   . LYS A 336 ? 0.59605 0.67144 0.66084 -0.01758 -0.08568 -0.11992 302 LYS A C   
2176 O O   . LYS A 336 ? 0.63365 0.71013 0.70596 -0.02228 -0.08206 -0.12578 302 LYS A O   
2177 C CB  . LYS A 336 ? 0.61275 0.70868 0.71190 -0.01728 -0.10498 -0.14050 302 LYS A CB  
2178 C CG  . LYS A 336 ? 0.77679 0.88345 0.88977 -0.01304 -0.11774 -0.14806 302 LYS A CG  
2179 C CD  . LYS A 336 ? 0.95346 1.07587 1.09709 -0.01911 -0.12098 -0.16206 302 LYS A CD  
2180 C CE  . LYS A 336 ? 0.99339 1.12940 1.16338 -0.02583 -0.11357 -0.16088 302 LYS A CE  
2181 N NZ  . LYS A 336 ? 0.99422 1.13720 1.18571 -0.03500 -0.10461 -0.16567 302 LYS A NZ  
2182 N N   . HIS A 337 ? 0.50833 0.57763 0.56175 -0.01723 -0.07719 -0.10716 303 HIS A N   
2183 C CA  . HIS A 337 ? 0.48884 0.55375 0.53917 -0.02167 -0.06362 -0.10003 303 HIS A CA  
2184 C C   . HIS A 337 ? 0.44311 0.49566 0.46582 -0.01637 -0.06098 -0.09535 303 HIS A C   
2185 O O   . HIS A 337 ? 0.48542 0.53072 0.48872 -0.00989 -0.06696 -0.09278 303 HIS A O   
2186 C CB  . HIS A 337 ? 0.44021 0.50790 0.49977 -0.02568 -0.05495 -0.08962 303 HIS A CB  
2187 C CG  . HIS A 337 ? 0.47857 0.55608 0.56386 -0.03261 -0.05223 -0.09340 303 HIS A CG  
2188 N ND1 . HIS A 337 ? 0.41089 0.48863 0.50594 -0.03883 -0.04439 -0.09582 303 HIS A ND1 
2189 C CD2 . HIS A 337 ? 0.51385 0.60030 0.61594 -0.03412 -0.05611 -0.09562 303 HIS A CD2 
2190 C CE1 . HIS A 337 ? 0.42801 0.51348 0.54369 -0.04444 -0.04289 -0.09883 303 HIS A CE1 
2191 N NE2 . HIS A 337 ? 0.41445 0.50624 0.53553 -0.04168 -0.04957 -0.09893 303 HIS A NE2 
2192 N N   . GLN A 338 ? 0.48814 0.53743 0.50832 -0.01895 -0.05174 -0.09448 304 GLN A N   
2193 C CA  . GLN A 338 ? 0.50156 0.54035 0.49712 -0.01430 -0.04696 -0.09028 304 GLN A CA  
2194 C C   . GLN A 338 ? 0.46585 0.50153 0.45242 -0.01382 -0.03914 -0.07729 304 GLN A C   
2195 O O   . GLN A 338 ? 0.42673 0.46819 0.42845 -0.01838 -0.03418 -0.07120 304 GLN A O   
2196 C CB  . GLN A 338 ? 0.49963 0.53673 0.49708 -0.01687 -0.03913 -0.09338 304 GLN A CB  
2197 C CG  . GLN A 338 ? 0.54878 0.58681 0.55306 -0.01776 -0.04684 -0.10636 304 GLN A CG  
2198 C CD  . GLN A 338 ? 0.63627 0.67211 0.64548 -0.02141 -0.03931 -0.10931 304 GLN A CD  
2199 O OE1 . GLN A 338 ? 0.74792 0.77869 0.75029 -0.01959 -0.04333 -0.11786 304 GLN A OE1 
2200 N NE2 . GLN A 338 ? 0.54367 0.58210 0.56398 -0.02613 -0.02923 -0.10260 304 GLN A NE2 
2201 N N   . PHE A 339 ? 0.45954 0.48513 0.42056 -0.00840 -0.03805 -0.07316 305 PHE A N   
2202 C CA  . PHE A 339 ? 0.51016 0.53198 0.46184 -0.00851 -0.03105 -0.06107 305 PHE A CA  
2203 C C   . PHE A 339 ? 0.51995 0.53230 0.44766 -0.00522 -0.02256 -0.05693 305 PHE A C   
2204 O O   . PHE A 339 ? 0.50297 0.50821 0.41372 -0.00035 -0.02589 -0.06324 305 PHE A O   
2205 C CB  . PHE A 339 ? 0.42241 0.44036 0.36658 -0.00539 -0.04074 -0.05832 305 PHE A CB  
2206 C CG  . PHE A 339 ? 0.57575 0.58388 0.49802 0.00213  -0.05241 -0.06477 305 PHE A CG  
2207 C CD1 . PHE A 339 ? 0.58463 0.59766 0.51690 0.00413  -0.06492 -0.07671 305 PHE A CD1 
2208 C CD2 . PHE A 339 ? 0.55903 0.55240 0.45048 0.00717  -0.05100 -0.05908 305 PHE A CD2 
2209 C CE1 . PHE A 339 ? 0.55045 0.55407 0.46291 0.01180  -0.07723 -0.08339 305 PHE A CE1 
2210 C CE2 . PHE A 339 ? 0.63767 0.61953 0.50622 0.01493  -0.06265 -0.06509 305 PHE A CE2 
2211 C CZ  . PHE A 339 ? 0.58885 0.57595 0.46818 0.01765  -0.07651 -0.07750 305 PHE A CZ  
2212 N N   . LEU A 340 ? 0.52663 0.53926 0.45383 -0.00802 -0.01133 -0.04662 306 LEU A N   
2213 C CA  . LEU A 340 ? 0.47018 0.47448 0.37494 -0.00566 -0.00164 -0.04073 306 LEU A CA  
2214 C C   . LEU A 340 ? 0.52947 0.52785 0.42420 -0.00651 -0.00065 -0.03033 306 LEU A C   
2215 O O   . LEU A 340 ? 0.49809 0.50282 0.40871 -0.01169 0.00466  -0.02320 306 LEU A O   
2216 C CB  . LEU A 340 ? 0.47311 0.48429 0.38891 -0.00882 0.01195  -0.03870 306 LEU A CB  
2217 C CG  . LEU A 340 ? 0.47075 0.47645 0.36768 -0.00716 0.02445  -0.03287 306 LEU A CG  
2218 C CD1 . LEU A 340 ? 0.50175 0.49559 0.37029 -0.00030 0.02170  -0.03848 306 LEU A CD1 
2219 C CD2 . LEU A 340 ? 0.44616 0.46149 0.35953 -0.00992 0.03654  -0.03217 306 LEU A CD2 
2220 N N   . TRP A 341 ? 0.53261 0.51737 0.40016 -0.00125 -0.00660 -0.02973 307 TRP A N   
2221 C CA  . TRP A 341 ? 0.51134 0.48670 0.36529 -0.00127 -0.00834 -0.02075 307 TRP A CA  
2222 C C   . TRP A 341 ? 0.61853 0.58225 0.44646 -0.00091 0.00381  -0.01283 307 TRP A C   
2223 O O   . TRP A 341 ? 0.64766 0.60030 0.45012 0.00453  0.00382  -0.01626 307 TRP A O   
2224 C CB  . TRP A 341 ? 0.62812 0.59448 0.46891 0.00491  -0.02520 -0.02601 307 TRP A CB  
2225 C CG  . TRP A 341 ? 0.55838 0.51555 0.38919 0.00515  -0.02988 -0.01799 307 TRP A CG  
2226 C CD1 . TRP A 341 ? 0.55732 0.51213 0.38785 -0.00006 -0.02031 -0.00636 307 TRP A CD1 
2227 C CD2 . TRP A 341 ? 0.63590 0.58420 0.45538 0.01122  -0.04607 -0.02148 307 TRP A CD2 
2228 N NE1 . TRP A 341 ? 0.57205 0.51565 0.39028 0.00217  -0.02941 -0.00195 307 TRP A NE1 
2229 C CE2 . TRP A 341 ? 0.58880 0.52829 0.39991 0.00955  -0.04544 -0.01117 307 TRP A CE2 
2230 C CE3 . TRP A 341 ? 0.65032 0.59735 0.46669 0.01812  -0.06168 -0.03289 307 TRP A CE3 
2231 C CZ2 . TRP A 341 ? 0.71161 0.64012 0.50989 0.01521  -0.06001 -0.01179 307 TRP A CZ2 
2232 C CZ3 . TRP A 341 ? 0.64866 0.58646 0.45414 0.02387  -0.07627 -0.03398 307 TRP A CZ3 
2233 C CH2 . TRP A 341 ? 0.69444 0.62263 0.49028 0.02271  -0.07541 -0.02342 307 TRP A CH2 
2234 N N   . VAL A 342 ? 0.58653 0.55242 0.42074 -0.00682 0.01425  -0.00254 308 VAL A N   
2235 C CA  . VAL A 342 ? 0.57606 0.53224 0.38875 -0.00828 0.02763  0.00591  308 VAL A CA  
2236 C C   . VAL A 342 ? 0.69759 0.63904 0.49229 -0.00894 0.02354  0.01463  308 VAL A C   
2237 O O   . VAL A 342 ? 0.71053 0.65683 0.52245 -0.01312 0.02012  0.01919  308 VAL A O   
2238 C CB  . VAL A 342 ? 0.59558 0.56567 0.43002 -0.01501 0.04346  0.01054  308 VAL A CB  
2239 C CG1 . VAL A 342 ? 0.63492 0.59657 0.44809 -0.01671 0.05873  0.01795  308 VAL A CG1 
2240 C CG2 . VAL A 342 ? 0.63001 0.61378 0.48382 -0.01386 0.04525  0.00144  308 VAL A CG2 
2241 N N   . VAL A 343 ? 0.71280 0.63449 0.47110 -0.00444 0.02343  0.01681  309 VAL A N   
2242 C CA  . VAL A 343 ? 0.82474 0.72764 0.55923 -0.00434 0.01963  0.02525  309 VAL A CA  
2243 C C   . VAL A 343 ? 0.82795 0.71829 0.53737 -0.00762 0.03648  0.03427  309 VAL A C   
2244 O O   . VAL A 343 ? 0.79509 0.68227 0.48887 -0.00477 0.04476  0.03118  309 VAL A O   
2245 C CB  . VAL A 343 ? 0.86933 0.75584 0.57889 0.00509  0.00145  0.01921  309 VAL A CB  
2246 C CG1 . VAL A 343 ? 0.98251 0.84775 0.66662 0.00567  -0.00341 0.02803  309 VAL A CG1 
2247 C CG2 . VAL A 343 ? 0.76325 0.66458 0.50009 0.00793  -0.01388 0.00895  309 VAL A CG2 
2248 N N   . HIS A 344 ? 0.82769 0.71080 0.53357 -0.01388 0.04201  0.04521  310 HIS A N   
2249 C CA  . HIS A 344 ? 0.82945 0.69977 0.51205 -0.01858 0.05880  0.05471  310 HIS A CA  
2250 C C   . HIS A 344 ? 1.00440 0.84475 0.64590 -0.01527 0.05198  0.06076  310 HIS A C   
2251 O O   . HIS A 344 ? 0.93899 0.77220 0.57993 -0.01294 0.03666  0.06132  310 HIS A O   
2252 C CB  . HIS A 344 ? 0.83904 0.72297 0.54882 -0.02960 0.07213  0.06300  310 HIS A CB  
2253 C CG  . HIS A 344 ? 0.95011 0.86087 0.69656 -0.03262 0.08050  0.05780  310 HIS A CG  
2254 N ND1 . HIS A 344 ? 1.00513 0.92324 0.75200 -0.03467 0.09778  0.05746  310 HIS A ND1 
2255 C CD2 . HIS A 344 ? 0.90498 0.83574 0.68770 -0.03354 0.07391  0.05264  310 HIS A CD2 
2256 C CE1 . HIS A 344 ? 0.97989 0.92119 0.76189 -0.03623 0.10043  0.05205  310 HIS A CE1 
2257 N NE2 . HIS A 344 ? 0.92430 0.87270 0.72749 -0.03577 0.08623  0.04933  310 HIS A NE2 
2258 N N   . GLY A 345 ? 0.97111 0.79299 0.57702 -0.01457 0.06335  0.06497  311 GLY A N   
2259 C CA  . GLY A 345 ? 1.13110 0.92095 0.69365 -0.01198 0.05894  0.07190  311 GLY A CA  
2260 C C   . GLY A 345 ? 1.16909 0.94099 0.70367 0.00056  0.03879  0.06416  311 GLY A C   
2261 O O   . GLY A 345 ? 1.12426 0.87381 0.63449 0.00396  0.02687  0.06800  311 GLY A O   
2262 N N   . LYS A 346 ? 1.21292 0.99350 0.75043 0.00786  0.03379  0.05283  312 LYS A N   
2263 C CA  . LYS A 346 ? 1.21392 0.97832 0.72576 0.02011  0.01438  0.04411  312 LYS A CA  
2264 C C   . LYS A 346 ? 1.23496 0.98791 0.71659 0.02658  0.02005  0.03912  312 LYS A C   
2265 O O   . LYS A 346 ? 1.13825 0.88095 0.60228 0.03721  0.00382  0.02972  312 LYS A O   
2266 C CB  . LYS A 346 ? 1.09538 0.88142 0.64310 0.02400  -0.00327 0.03266  312 LYS A CB  
2267 C CG  . LYS A 346 ? 1.09640 0.88828 0.66603 0.02097  -0.01365 0.03588  312 LYS A CG  
2268 C CD  . LYS A 346 ? 1.18866 0.95083 0.72165 0.02672  -0.02619 0.04041  312 LYS A CD  
2269 C CE  . LYS A 346 ? 1.07864 0.84647 0.63330 0.02417  -0.03631 0.04340  312 LYS A CE  
2270 N NZ  . LYS A 346 ? 1.27861 1.01638 0.79700 0.03093  -0.05026 0.04700  312 LYS A NZ  
2271 N N   . GLU A 347 ? 1.30875 1.06357 0.78464 0.02074  0.04233  0.04456  313 GLU A N   
2272 C CA  . GLU A 347 ? 1.42260 1.16566 0.86790 0.02699  0.04948  0.04022  313 GLU A CA  
2273 C C   . GLU A 347 ? 1.42865 1.13303 0.81695 0.03402  0.04426  0.04437  313 GLU A C   
2274 O O   . GLU A 347 ? 1.29557 0.98165 0.66274 0.02874  0.05182  0.05607  313 GLU A O   
2275 C CB  . GLU A 347 ? 1.43925 1.19499 0.89419 0.01872  0.07586  0.04528  313 GLU A CB  
2276 C CG  . GLU A 347 ? 1.54192 1.33286 1.04655 0.01485  0.08037  0.03860  313 GLU A CG  
2277 C CD  . GLU A 347 ? 1.52367 1.33248 1.05522 0.00289  0.10132  0.04699  313 GLU A CD  
2278 O OE1 . GLU A 347 ? 1.27841 1.09787 0.83717 -0.00421 0.09848  0.05210  313 GLU A OE1 
2279 O OE2 . GLU A 347 ? 1.52881 1.34123 1.05477 0.00092  0.12030  0.04795  313 GLU A OE2 
2280 N N   . GLY A 348 ? 1.42806 1.11857 0.79054 0.04595  0.03079  0.03464  314 GLY A N   
2281 C CA  . GLY A 348 ? 1.56621 1.21781 0.87199 0.05442  0.02338  0.03726  314 GLY A CA  
2282 C C   . GLY A 348 ? 1.59668 1.23281 0.89347 0.05844  0.00231  0.03878  314 GLY A C   
2283 O O   . GLY A 348 ? 1.65520 1.25904 0.90965 0.05991  0.00239  0.04744  314 GLY A O   
2284 N N   . GLU A 349 ? 1.41202 1.06978 0.74718 0.06029  -0.01545 0.03049  315 GLU A N   
2285 C CA  . GLU A 349 ? 1.43020 1.07639 0.76066 0.06574  -0.03744 0.02950  315 GLU A CA  
2286 C C   . GLU A 349 ? 1.33477 0.99080 0.67937 0.07646  -0.06101 0.01348  315 GLU A C   
2287 O O   . GLU A 349 ? 1.39079 1.07442 0.77068 0.07483  -0.05975 0.00466  315 GLU A O   
2288 C CB  . GLU A 349 ? 1.37686 1.04140 0.74499 0.05553  -0.03475 0.03667  315 GLU A CB  
2289 C CG  . GLU A 349 ? 1.38311 1.03614 0.74722 0.06143  -0.05704 0.03567  315 GLU A CG  
2290 C CD  . GLU A 349 ? 1.45950 1.12439 0.85213 0.05132  -0.05235 0.04470  315 GLU A CD  
2291 O OE1 . GLU A 349 ? 1.37841 1.05660 0.78894 0.03947  -0.03135 0.05296  315 GLU A OE1 
2292 O OE2 . GLU A 349 ? 1.45005 1.11075 0.84710 0.05564  -0.07007 0.04311  315 GLU A OE2 
2293 N N   . ASP A 350 ? 1.34178 0.97439 0.65838 0.08743  -0.08268 0.00948  316 ASP A N   
2294 C CA  . ASP A 350 ? 1.37232 1.01386 0.70302 0.09783  -0.10674 -0.00638 316 ASP A CA  
2295 C C   . ASP A 350 ? 1.18910 0.86748 0.57907 0.09183  -0.11177 -0.01159 316 ASP A C   
2296 O O   . ASP A 350 ? 1.06727 0.74929 0.47189 0.08799  -0.11490 -0.00583 316 ASP A O   
2297 C CB  . ASP A 350 ? 1.35671 0.97383 0.66457 0.10848  -0.12658 -0.00893 316 ASP A CB  
2298 C CG  . ASP A 350 ? 1.55923 1.18161 0.87691 0.11977  -0.14723 -0.02541 316 ASP A CG  
2299 O OD1 . ASP A 350 ? 1.69135 1.30958 0.99551 0.12337  -0.14359 -0.03071 316 ASP A OD1 
2300 O OD2 . ASP A 350 ? 1.60695 1.23828 0.94760 0.12484  -0.16653 -0.03320 316 ASP A OD2 
2301 N N   . GLU A 351 ? 1.04124 0.74547 0.46371 0.09103  -0.11225 -0.02246 317 GLU A N   
2302 C CA  . GLU A 351 ? 1.12650 0.86516 0.60416 0.08480  -0.11515 -0.02771 317 GLU A CA  
2303 C C   . GLU A 351 ? 1.13800 0.87880 0.62797 0.09136  -0.13844 -0.03490 317 GLU A C   
2304 O O   . GLU A 351 ? 1.07178 0.83595 0.60190 0.08549  -0.13939 -0.03537 317 GLU A O   
2305 C CB  . GLU A 351 ? 1.07457 0.83520 0.57811 0.08386  -0.11295 -0.03888 317 GLU A CB  
2306 C CG  . GLU A 351 ? 0.97180 0.73554 0.47102 0.07704  -0.08931 -0.03264 317 GLU A CG  
2307 C CD  . GLU A 351 ? 1.10782 0.88883 0.62713 0.07757  -0.08876 -0.04416 317 GLU A CD  
2308 O OE1 . GLU A 351 ? 1.18168 0.96767 0.71110 0.08397  -0.10730 -0.05720 317 GLU A OE1 
2309 O OE2 . GLU A 351 ? 1.07758 0.86725 0.60334 0.07156  -0.07002 -0.04055 317 GLU A OE2 
2310 N N   . ASP A 352 ? 1.10888 0.82544 0.56480 0.10391  -0.15739 -0.04082 318 ASP A N   
2311 C CA  . ASP A 352 ? 1.10901 0.82681 0.57543 0.11132  -0.18026 -0.04812 318 ASP A CA  
2312 C C   . ASP A 352 ? 1.05017 0.76096 0.51521 0.10738  -0.17795 -0.03622 318 ASP A C   
2313 O O   . ASP A 352 ? 1.05231 0.77279 0.53896 0.11061  -0.19293 -0.04133 318 ASP A O   
2314 C CB  . ASP A 352 ? 1.26847 0.96496 0.70983 0.12409  -0.19642 -0.05559 318 ASP A CB  
2315 C CG  . ASP A 352 ? 1.44884 1.15498 0.89903 0.12848  -0.20209 -0.06918 318 ASP A CG  
2316 O OD1 . ASP A 352 ? 1.39365 1.10849 0.84420 0.12297  -0.18968 -0.06952 318 ASP A OD1 
2317 O OD2 . ASP A 352 ? 1.69203 1.39665 1.14916 0.13751  -0.21875 -0.07963 318 ASP A OD2 
2318 N N   . ASN A 353 ? 1.00502 0.69969 0.44618 0.10028  -0.15931 -0.02087 319 ASN A N   
2319 C CA  . ASN A 353 ? 1.12647 0.81303 0.56553 0.09548  -0.15621 -0.00896 319 ASN A CA  
2320 C C   . ASN A 353 ? 1.07957 0.79955 0.57115 0.08452  -0.14771 -0.00702 319 ASN A C   
2321 O O   . ASN A 353 ? 1.02129 0.74052 0.52145 0.08302  -0.15247 -0.00205 319 ASN A O   
2322 C CB  . ASN A 353 ? 1.11895 0.77831 0.51749 0.09002  -0.13775 0.00661  319 ASN A CB  
2323 C CG  . ASN A 353 ? 1.37770 1.00163 0.73066 0.09962  -0.14589 0.00761  319 ASN A CG  
2324 O OD1 . ASN A 353 ? 1.29465 0.89878 0.61548 0.09749  -0.13140 0.01497  319 ASN A OD1 
2325 N ND2 . ASN A 353 ? 1.39071 1.01091 0.75073 0.10914  -0.16643 -0.00046 319 ASN A ND2 
2326 N N   . TRP A 354 ? 1.05351 0.80101 0.57856 0.07728  -0.13565 -0.01086 320 TRP A N   
2327 C CA  . TRP A 354 ? 1.02817 0.80505 0.60005 0.06692  -0.12667 -0.00859 320 TRP A CA  
2328 C C   . TRP A 354 ? 1.01534 0.82272 0.62820 0.06595  -0.12989 -0.02154 320 TRP A C   
2329 O O   . TRP A 354 ? 0.91161 0.74301 0.56246 0.05731  -0.12139 -0.02020 320 TRP A O   
2330 C CB  . TRP A 354 ? 1.07459 0.85271 0.64666 0.05498  -0.10209 0.00491  320 TRP A CB  
2331 C CG  . TRP A 354 ? 1.08051 0.85707 0.63905 0.05335  -0.08794 0.00461  320 TRP A CG  
2332 C CD1 . TRP A 354 ? 1.07055 0.82036 0.58376 0.05862  -0.08534 0.00704  320 TRP A CD1 
2333 C CD2 . TRP A 354 ? 0.99757 0.79915 0.58667 0.04645  -0.07429 0.00163  320 TRP A CD2 
2334 N NE1 . TRP A 354 ? 1.08154 0.83941 0.59622 0.05558  -0.07067 0.00543  320 TRP A NE1 
2335 C CE2 . TRP A 354 ? 1.02444 0.81395 0.58561 0.04827  -0.06408 0.00202  320 TRP A CE2 
2336 C CE3 . TRP A 354 ? 0.92868 0.76006 0.56422 0.03939  -0.06990 -0.00141 320 TRP A CE3 
2337 C CZ2 . TRP A 354 ? 1.04030 0.84749 0.61983 0.04364  -0.05030 -0.00093 320 TRP A CZ2 
2338 C CZ3 . TRP A 354 ? 0.93843 0.78580 0.59078 0.03466  -0.05655 -0.00401 320 TRP A CZ3 
2339 C CH2 . TRP A 354 ? 0.91884 0.75457 0.54393 0.03697  -0.04716 -0.00393 320 TRP A CH2 
2340 N N   . LEU A 355 ? 0.99947 0.80546 0.60517 0.07430  -0.14199 -0.03398 321 LEU A N   
2341 C CA  . LEU A 355 ? 1.01498 0.84779 0.65808 0.07331  -0.14639 -0.04703 321 LEU A CA  
2342 C C   . LEU A 355 ? 1.00873 0.83910 0.64987 0.08480  -0.17052 -0.06131 321 LEU A C   
2343 O O   . LEU A 355 ? 1.05492 0.85948 0.65783 0.09480  -0.18231 -0.06207 321 LEU A O   
2344 C CB  . LEU A 355 ? 0.86736 0.70469 0.50854 0.07003  -0.13343 -0.04916 321 LEU A CB  
2345 C CG  . LEU A 355 ? 1.00325 0.84708 0.65138 0.05904  -0.10941 -0.03745 321 LEU A CG  
2346 C CD1 . LEU A 355 ? 0.88023 0.72316 0.51781 0.05883  -0.09893 -0.04042 321 LEU A CD1 
2347 C CD2 . LEU A 355 ? 0.83726 0.70860 0.53191 0.04989  -0.10368 -0.03690 321 LEU A CD2 
2348 N N   . PRO A 356 ? 1.02532 0.88161 0.70683 0.08362  -0.17828 -0.07300 322 PRO A N   
2349 C CA  . PRO A 356 ? 0.98954 0.84704 0.67407 0.09408  -0.20110 -0.08845 322 PRO A CA  
2350 C C   . PRO A 356 ? 1.10990 0.95374 0.76820 0.10077  -0.20634 -0.09598 322 PRO A C   
2351 O O   . PRO A 356 ? 1.06962 0.90806 0.71410 0.09651  -0.19133 -0.09085 322 PRO A O   
2352 C CB  . PRO A 356 ? 0.92869 0.81966 0.66561 0.08788  -0.20204 -0.09804 322 PRO A CB  
2353 C CG  . PRO A 356 ? 0.92155 0.82430 0.67851 0.07635  -0.18357 -0.08587 322 PRO A CG  
2354 C CD  . PRO A 356 ? 0.74035 0.62545 0.46681 0.07262  -0.16683 -0.07265 322 PRO A CD  
2355 N N   . LYS A 357 ? 1.17242 1.01076 0.82424 0.11203  -0.22869 -0.10907 323 LYS A N   
2356 C CA  . LYS A 357 ? 1.05555 0.88019 0.68628 0.11885  -0.23330 -0.11541 323 LYS A CA  
2357 C C   . LYS A 357 ? 1.03097 0.87223 0.67919 0.11321  -0.22767 -0.12390 323 LYS A C   
2358 O O   . LYS A 357 ? 1.09776 0.96567 0.78886 0.10870  -0.23144 -0.13396 323 LYS A O   
2359 C CB  . LYS A 357 ? 1.13603 0.96063 0.77905 0.12834  -0.25058 -0.12512 323 LYS A CB  
2360 N N   . GLY A 358 ? 1.01810 0.84458 0.63772 0.11218  -0.21487 -0.11818 324 GLY A N   
2361 C CA  . GLY A 358 ? 1.12997 0.96976 0.76603 0.10697  -0.20660 -0.12447 324 GLY A CA  
2362 C C   . GLY A 358 ? 1.07419 0.94202 0.75378 0.09343  -0.19019 -0.12088 324 GLY A C   
2363 O O   . GLY A 358 ? 0.97464 0.85960 0.68109 0.08917  -0.18966 -0.13023 324 GLY A O   
2364 N N   . PHE A 359 ? 0.96061 0.83200 0.64663 0.08657  -0.17709 -0.10755 325 PHE A N   
2365 C CA  . PHE A 359 ? 0.97704 0.87329 0.70276 0.07438  -0.16231 -0.10391 325 PHE A CA  
2366 C C   . PHE A 359 ? 1.01204 0.91184 0.73855 0.06886  -0.14649 -0.10285 325 PHE A C   
2367 O O   . PHE A 359 ? 0.92402 0.84387 0.68379 0.06191  -0.14196 -0.10827 325 PHE A O   
2368 C CB  . PHE A 359 ? 0.85219 0.74784 0.57928 0.06903  -0.15166 -0.08937 325 PHE A CB  
2369 C CG  . PHE A 359 ? 0.88100 0.79958 0.64570 0.05729  -0.13694 -0.08499 325 PHE A CG  
2370 C CD1 . PHE A 359 ? 0.81564 0.75577 0.61895 0.05365  -0.14306 -0.09191 325 PHE A CD1 
2371 C CD2 . PHE A 359 ? 0.78997 0.70819 0.55108 0.05020  -0.11700 -0.07432 325 PHE A CD2 
2372 C CE1 . PHE A 359 ? 0.80113 0.75961 0.63582 0.04336  -0.12980 -0.08777 325 PHE A CE1 
2373 C CE2 . PHE A 359 ? 0.80347 0.74111 0.59769 0.04036  -0.10484 -0.07072 325 PHE A CE2 
2374 C CZ  . PHE A 359 ? 0.75518 0.71176 0.58476 0.03704  -0.11139 -0.07721 325 PHE A CZ  
2375 N N   . VAL A 360 ? 1.03394 0.91360 0.72318 0.07208  -0.13778 -0.09614 326 VAL A N   
2376 C CA  . VAL A 360 ? 1.16295 1.04562 0.85166 0.06769  -0.12199 -0.09488 326 VAL A CA  
2377 C C   . VAL A 360 ? 1.16222 1.04726 0.85462 0.07170  -0.13191 -0.10964 326 VAL A C   
2378 O O   . VAL A 360 ? 1.21279 1.10869 0.92144 0.06643  -0.12227 -0.11236 326 VAL A O   
2379 C CB  . VAL A 360 ? 1.11913 0.98011 0.76704 0.06999  -0.10872 -0.08367 326 VAL A CB  
2380 C CG1 . VAL A 360 ? 1.15495 1.02455 0.81089 0.06332  -0.08845 -0.07953 326 VAL A CG1 
2381 C CG2 . VAL A 360 ? 1.03815 0.89110 0.67598 0.06803  -0.10473 -0.07081 326 VAL A CG2 
2382 N N   . GLU A 361 ? 1.15928 1.03358 0.83682 0.08123  -0.15187 -0.11974 327 GLU A N   
2383 C CA  . GLU A 361 ? 1.36141 1.23737 1.04293 0.08509  -0.16296 -0.13462 327 GLU A CA  
2384 C C   . GLU A 361 ? 1.13952 1.04257 0.86960 0.07620  -0.16341 -0.14266 327 GLU A C   
2385 O O   . GLU A 361 ? 1.14351 1.05349 0.88502 0.07152  -0.15542 -0.14630 327 GLU A O   
2386 C CB  . GLU A 361 ? 1.38092 1.24166 1.04094 0.09714  -0.18636 -0.14458 327 GLU A CB  
2387 C CG  . GLU A 361 ? 1.53919 1.36826 1.14480 0.10712  -0.18703 -0.13858 327 GLU A CG  
2388 C CD  . GLU A 361 ? 1.78728 1.60083 1.37363 0.11946  -0.21023 -0.14902 327 GLU A CD  
2389 O OE1 . GLU A 361 ? 1.71287 1.54397 1.33535 0.11903  -0.22324 -0.15940 327 GLU A OE1 
2390 O OE2 . GLU A 361 ? 1.83953 1.62700 1.38545 0.12726  -0.20990 -0.14310 327 GLU A OE2 
2391 N N   . ARG A 362 ? 1.08882 1.00653 0.84707 0.07382  -0.17234 -0.14551 328 ARG A N   
2392 C CA  . ARG A 362 ? 1.08061 1.02338 0.88440 0.06459  -0.17124 -0.15240 328 ARG A CA  
2393 C C   . ARG A 362 ? 1.03071 0.98429 0.85161 0.05379  -0.14992 -0.14200 328 ARG A C   
2394 O O   . ARG A 362 ? 1.02981 0.99877 0.88029 0.04609  -0.14562 -0.14728 328 ARG A O   
2395 C CB  . ARG A 362 ? 0.94203 0.89805 0.77096 0.06478  -0.18387 -0.15705 328 ARG A CB  
2396 C CG  . ARG A 362 ? 0.99823 0.94008 0.80233 0.07222  -0.18978 -0.14924 328 ARG A CG  
2397 C CD  . ARG A 362 ? 1.02405 0.98022 0.85477 0.07249  -0.20099 -0.15345 328 ARG A CD  
2398 N NE  . ARG A 362 ? 1.12873 1.06800 0.93191 0.08065  -0.20801 -0.14630 328 ARG A NE  
2399 C CZ  . ARG A 362 ? 1.15577 1.10252 0.97360 0.08111  -0.21328 -0.14434 328 ARG A CZ  
2400 N NH1 . ARG A 362 ? 1.09044 1.06227 0.95070 0.07412  -0.21220 -0.14927 328 ARG A NH1 
2401 N NH2 . ARG A 362 ? 1.21681 1.14419 1.00468 0.08893  -0.21969 -0.13736 328 ARG A NH2 
2402 N N   . MET A 363 ? 0.98925 0.93421 0.79174 0.05304  -0.13676 -0.12765 329 MET A N   
2403 C CA  . MET A 363 ? 1.01663 0.97179 0.83561 0.04354  -0.11751 -0.11813 329 MET A CA  
2404 C C   . MET A 363 ? 1.03695 0.99244 0.85586 0.04120  -0.10867 -0.12195 329 MET A C   
2405 O O   . MET A 363 ? 0.95545 0.92478 0.80133 0.03310  -0.09998 -0.12220 329 MET A O   
2406 C CB  . MET A 363 ? 1.05710 1.00166 0.85435 0.04373  -0.10599 -0.10293 329 MET A CB  
2407 C CG  . MET A 363 ? 0.88005 0.83545 0.69521 0.03450  -0.08736 -0.09302 329 MET A CG  
2408 S SD  . MET A 363 ? 1.05967 1.00065 0.84449 0.03474  -0.07072 -0.07750 329 MET A SD  
2409 C CE  . MET A 363 ? 0.82681 0.75342 0.58080 0.04115  -0.06720 -0.08267 329 MET A CE  
2410 N N   . LYS A 364 ? 1.05462 0.99351 0.84190 0.04873  -0.11114 -0.12520 330 LYS A N   
2411 C CA  . LYS A 364 ? 1.15955 1.09679 0.94357 0.04801  -0.10386 -0.12963 330 LYS A CA  
2412 C C   . LYS A 364 ? 1.14560 1.08757 0.94451 0.04845  -0.11730 -0.14514 330 LYS A C   
2413 O O   . LYS A 364 ? 1.23840 1.18466 1.04811 0.04450  -0.11125 -0.14940 330 LYS A O   
2414 C CB  . LYS A 364 ? 1.16138 1.07792 0.90314 0.05597  -0.09864 -0.12587 330 LYS A CB  
2415 C CG  . LYS A 364 ? 1.23173 1.14280 0.95773 0.05462  -0.08334 -0.11071 330 LYS A CG  
2416 C CD  . LYS A 364 ? 1.39081 1.28149 1.07497 0.06189  -0.07645 -0.10755 330 LYS A CD  
2417 C CE  . LYS A 364 ? 1.58056 1.47303 1.26095 0.05705  -0.05476 -0.09435 330 LYS A CE  
2418 N NZ  . LYS A 364 ? 1.63420 1.51438 1.28588 0.06185  -0.04355 -0.09405 330 LYS A NZ  
2419 N N   . GLU A 365 ? 1.11358 1.05456 0.91366 0.05322  -0.13577 -0.15410 331 GLU A N   
2420 C CA  . GLU A 365 ? 1.16224 1.10860 0.97862 0.05305  -0.14910 -0.16966 331 GLU A CA  
2421 C C   . GLU A 365 ? 1.04690 1.01466 0.90669 0.04149  -0.14477 -0.17275 331 GLU A C   
2422 O O   . GLU A 365 ? 1.14097 1.11239 1.01390 0.03723  -0.14438 -0.18086 331 GLU A O   
2423 C CB  . GLU A 365 ? 1.25632 1.19758 1.06523 0.06142  -0.17059 -0.17906 331 GLU A CB  
2424 C CG  . GLU A 365 ? 1.46869 1.41274 1.28963 0.06272  -0.18598 -0.19621 331 GLU A CG  
2425 C CD  . GLU A 365 ? 1.53265 1.46854 1.34064 0.07324  -0.20823 -0.20590 331 GLU A CD  
2426 O OE1 . GLU A 365 ? 1.40213 1.33033 1.19267 0.07931  -0.21194 -0.19920 331 GLU A OE1 
2427 O OE2 . GLU A 365 ? 1.59031 1.52833 1.41071 0.07410  -0.21680 -0.21462 331 GLU A OE2 
2428 N N   . GLU A 366 ? 1.08953 1.07000 0.97037 0.03627  -0.14123 -0.16628 332 GLU A N   
2429 C CA  . GLU A 366 ? 1.01426 1.01323 0.93341 0.02518  -0.13514 -0.16778 332 GLU A CA  
2430 C C   . GLU A 366 ? 0.77095 0.77150 0.69384 0.01841  -0.11578 -0.15745 332 GLU A C   
2431 O O   . GLU A 366 ? 0.95586 0.96909 0.90718 0.00934  -0.10943 -0.15727 332 GLU A O   
2432 C CB  . GLU A 366 ? 1.02245 1.03440 0.96304 0.02299  -0.14008 -0.16631 332 GLU A CB  
2433 C CG  . GLU A 366 ? 1.11717 1.12272 1.04250 0.03293  -0.15681 -0.17044 332 GLU A CG  
2434 C CD  . GLU A 366 ? 1.14736 1.16523 1.09275 0.03153  -0.16080 -0.16829 332 GLU A CD  
2435 O OE1 . GLU A 366 ? 1.23615 1.27024 1.21286 0.02742  -0.16784 -0.17828 332 GLU A OE1 
2436 O OE2 . GLU A 366 ? 1.17086 1.18206 1.10080 0.03436  -0.15644 -0.15669 332 GLU A OE2 
2437 N N   . LYS A 367 ? 0.84861 0.83644 0.74367 0.02278  -0.10639 -0.14942 333 LYS A N   
2438 C CA  . LYS A 367 ? 0.91230 0.90155 0.81025 0.01769  -0.08885 -0.14088 333 LYS A CA  
2439 C C   . LYS A 367 ? 0.90570 0.90690 0.82545 0.01058  -0.08017 -0.13126 333 LYS A C   
2440 O O   . LYS A 367 ? 0.90300 0.91080 0.83988 0.00374  -0.06969 -0.12834 333 LYS A O   
2441 C CB  . LYS A 367 ? 0.97015 0.96089 0.87992 0.01346  -0.08675 -0.14924 333 LYS A CB  
2442 C CG  . LYS A 367 ? 0.95532 0.93284 0.84218 0.02062  -0.09422 -0.15854 333 LYS A CG  
2443 C CD  . LYS A 367 ? 1.09198 1.05636 0.94654 0.02752  -0.08443 -0.15113 333 LYS A CD  
2444 C CE  . LYS A 367 ? 1.18918 1.13947 1.02017 0.03484  -0.09089 -0.16068 333 LYS A CE  
2445 N NZ  . LYS A 367 ? 1.16377 1.10152 0.96294 0.04162  -0.07989 -0.15388 333 LYS A NZ  
2446 N N   . LYS A 368 ? 0.83653 0.83903 0.75425 0.01275  -0.08528 -0.12654 334 LYS A N   
2447 C CA  . LYS A 368 ? 0.84842 0.86179 0.78694 0.00661  -0.07934 -0.11859 334 LYS A CA  
2448 C C   . LYS A 368 ? 0.73088 0.73944 0.65609 0.00662  -0.06633 -0.10453 334 LYS A C   
2449 O O   . LYS A 368 ? 0.69386 0.70946 0.63480 0.00039  -0.05530 -0.09822 334 LYS A O   
2450 C CB  . LYS A 368 ? 0.91491 0.93342 0.86172 0.00873  -0.09239 -0.12183 334 LYS A CB  
2451 C CG  . LYS A 368 ? 0.97658 1.00808 0.95228 0.00435  -0.10101 -0.13397 334 LYS A CG  
2452 C CD  . LYS A 368 ? 0.72603 0.77065 0.73073 -0.00511 -0.09176 -0.13028 334 LYS A CD  
2453 C CE  . LYS A 368 ? 0.81468 0.86784 0.84319 -0.01201 -0.09269 -0.14110 334 LYS A CE  
2454 N NZ  . LYS A 368 ? 0.80764 0.87527 0.86589 -0.01882 -0.09217 -0.14277 334 LYS A NZ  
2455 N N   . GLY A 369 ? 0.62466 0.62052 0.52063 0.01338  -0.06739 -0.09965 335 GLY A N   
2456 C CA  . GLY A 369 ? 0.67671 0.66842 0.56141 0.01263  -0.05594 -0.08636 335 GLY A CA  
2457 C C   . GLY A 369 ? 0.76717 0.74459 0.61968 0.01800  -0.04923 -0.08282 335 GLY A C   
2458 O O   . GLY A 369 ? 0.68325 0.65110 0.51687 0.02410  -0.05577 -0.09041 335 GLY A O   
2459 N N   . MET A 370 ? 0.66276 0.63886 0.50954 0.01551  -0.03569 -0.07131 336 MET A N   
2460 C CA  . MET A 370 ? 0.62986 0.59324 0.44676 0.01948  -0.02631 -0.06589 336 MET A CA  
2461 C C   . MET A 370 ? 0.77797 0.73569 0.58405 0.01806  -0.02121 -0.05361 336 MET A C   
2462 O O   . MET A 370 ? 0.60610 0.57385 0.43352 0.01181  -0.01650 -0.04706 336 MET A O   
2463 C CB  . MET A 370 ? 0.63796 0.60722 0.46178 0.01684  -0.01163 -0.06516 336 MET A CB  
2464 C CG  . MET A 370 ? 0.77265 0.73505 0.57611 0.01763  0.00331  -0.05584 336 MET A CG  
2465 S SD  . MET A 370 ? 0.85751 0.82283 0.65956 0.01906  0.01681  -0.05965 336 MET A SD  
2466 C CE  . MET A 370 ? 0.71155 0.66635 0.49650 0.02680  0.00300  -0.07360 336 MET A CE  
2467 N N   . LEU A 371 ? 0.66649 0.60659 0.43830 0.02387  -0.02270 -0.05063 337 LEU A N   
2468 C CA  . LEU A 371 ? 0.72222 0.65285 0.47851 0.02263  -0.01811 -0.03893 337 LEU A CA  
2469 C C   . LEU A 371 ? 0.73728 0.65894 0.47041 0.02257  -0.00136 -0.03190 337 LEU A C   
2470 O O   . LEU A 371 ? 0.68948 0.59860 0.39552 0.02885  -0.00108 -0.03608 337 LEU A O   
2471 C CB  . LEU A 371 ? 0.79747 0.71231 0.53070 0.02940  -0.03413 -0.04068 337 LEU A CB  
2472 C CG  . LEU A 371 ? 0.78981 0.69032 0.50205 0.02886  -0.03146 -0.02886 337 LEU A CG  
2473 C CD1 . LEU A 371 ? 0.72807 0.63796 0.46464 0.02470  -0.03806 -0.02550 337 LEU A CD1 
2474 C CD2 . LEU A 371 ? 0.87031 0.74624 0.54152 0.03822  -0.04209 -0.03067 337 LEU A CD2 
2475 N N   . ILE A 372 ? 0.71237 0.64076 0.45678 0.01552  0.01265  -0.02176 338 ILE A N   
2476 C CA  . ILE A 372 ? 0.78966 0.71312 0.51784 0.01390  0.03065  -0.01472 338 ILE A CA  
2477 C C   . ILE A 372 ? 0.80531 0.71584 0.51515 0.01108  0.03491  -0.00288 338 ILE A C   
2478 O O   . ILE A 372 ? 0.83523 0.75134 0.56275 0.00599  0.03181  0.00262  338 ILE A O   
2479 C CB  . ILE A 372 ? 0.71142 0.65459 0.47010 0.00769  0.04455  -0.01360 338 ILE A CB  
2480 C CG1 . ILE A 372 ? 0.69984 0.65396 0.47696 0.01005  0.03909  -0.02516 338 ILE A CG1 
2481 C CG2 . ILE A 372 ? 0.84370 0.78350 0.58689 0.00660  0.06345  -0.00785 338 ILE A CG2 
2482 C CD1 . ILE A 372 ? 0.93009 0.87579 0.68439 0.01689  0.04174  -0.03224 338 ILE A CD1 
2483 N N   . LYS A 373 ? 0.88660 0.77853 0.55976 0.01431  0.04222  0.00106  339 LYS A N   
2484 C CA  . LYS A 373 ? 0.91812 0.79348 0.56774 0.01149  0.04770  0.01263  339 LYS A CA  
2485 C C   . LYS A 373 ? 0.93137 0.81087 0.58028 0.00525  0.07079  0.02014  339 LYS A C   
2486 O O   . LYS A 373 ? 1.16978 1.03865 0.79179 0.00865  0.08086  0.01971  339 LYS A O   
2487 C CB  . LYS A 373 ? 0.96512 0.81258 0.56957 0.02015  0.03775  0.01155  339 LYS A CB  
2488 C CG  . LYS A 373 ? 0.97968 0.82393 0.58551 0.02728  0.01407  0.00257  339 LYS A CG  
2489 C CD  . LYS A 373 ? 1.10667 0.92120 0.66608 0.03634  0.00339  0.00215  339 LYS A CD  
2490 C CE  . LYS A 373 ? 1.07246 0.88596 0.63113 0.04580  -0.01766 -0.01156 339 LYS A CE  
2491 N NZ  . LYS A 373 ? 1.09793 0.88137 0.60962 0.05607  -0.02911 -0.01329 339 LYS A NZ  
2492 N N   . GLY A 374 ? 0.83730 0.73238 0.51604 -0.00368 0.07908  0.02655  340 GLY A N   
2493 C CA  . GLY A 374 ? 0.87851 0.78120 0.56325 -0.01034 0.10048  0.03291  340 GLY A CA  
2494 C C   . GLY A 374 ? 0.90980 0.83895 0.64039 -0.01671 0.10477  0.03214  340 GLY A C   
2495 O O   . GLY A 374 ? 0.80251 0.74019 0.55661 -0.01800 0.09251  0.03046  340 GLY A O   
2496 N N   . TRP A 375 ? 0.84744 0.78883 0.58936 -0.02011 0.12235  0.03294  341 TRP A N   
2497 C CA  . TRP A 375 ? 0.86166 0.82688 0.64511 -0.02596 0.12809  0.03270  341 TRP A CA  
2498 C C   . TRP A 375 ? 0.82718 0.80635 0.63049 -0.02077 0.12228  0.02138  341 TRP A C   
2499 O O   . TRP A 375 ? 0.84223 0.81687 0.62892 -0.01404 0.12325  0.01435  341 TRP A O   
2500 C CB  . TRP A 375 ? 0.87261 0.84545 0.66096 -0.03197 0.14958  0.03829  341 TRP A CB  
2501 C CG  . TRP A 375 ? 0.86418 0.86122 0.69498 -0.03739 0.15528  0.03766  341 TRP A CG  
2502 C CD1 . TRP A 375 ? 0.84011 0.84480 0.69423 -0.04556 0.15596  0.04458  341 TRP A CD1 
2503 C CD2 . TRP A 375 ? 0.83554 0.85079 0.68931 -0.03434 0.16010  0.02926  341 TRP A CD2 
2504 N NE1 . TRP A 375 ? 0.89903 0.92568 0.78924 -0.04756 0.16057  0.04082  341 TRP A NE1 
2505 C CE2 . TRP A 375 ? 0.87606 0.90934 0.76655 -0.04064 0.16314  0.03148  341 TRP A CE2 
2506 C CE3 . TRP A 375 ? 0.74073 0.75760 0.58676 -0.02646 0.16136  0.01980  341 TRP A CE3 
2507 C CZ2 . TRP A 375 ? 0.83191 0.88422 0.75082 -0.03884 0.16701  0.02450  341 TRP A CZ2 
2508 C CZ3 . TRP A 375 ? 0.75464 0.79034 0.62891 -0.02501 0.16569  0.01312  341 TRP A CZ3 
2509 C CH2 . TRP A 375 ? 0.74764 0.80063 0.65767 -0.03097 0.16831  0.01547  341 TRP A CH2 
2510 N N   . VAL A 376 ? 0.83199 0.82642 0.66938 -0.02392 0.11612  0.01973  342 VAL A N   
2511 C CA  . VAL A 376 ? 0.68358 0.69045 0.54167 -0.02027 0.11115  0.00983  342 VAL A CA  
2512 C C   . VAL A 376 ? 0.73253 0.75834 0.62546 -0.02543 0.11899  0.01117  342 VAL A C   
2513 O O   . VAL A 376 ? 0.68832 0.71784 0.59376 -0.03205 0.12212  0.01908  342 VAL A O   
2514 C CB  . VAL A 376 ? 0.76741 0.77114 0.63006 -0.01775 0.09242  0.00468  342 VAL A CB  
2515 C CG1 . VAL A 376 ? 0.77693 0.76293 0.60670 -0.01148 0.08326  0.00149  342 VAL A CG1 
2516 C CG2 . VAL A 376 ? 0.65328 0.66005 0.53340 -0.02357 0.08593  0.01114  342 VAL A CG2 
2517 N N   . PRO A 377 ? 0.71052 0.74760 0.61929 -0.02231 0.12163  0.00343  343 PRO A N   
2518 C CA  . PRO A 377 ? 0.62882 0.68279 0.57133 -0.02609 0.12600  0.00367  343 PRO A CA  
2519 C C   . PRO A 377 ? 0.63990 0.69634 0.60208 -0.02843 0.11237  0.00345  343 PRO A C   
2520 O O   . PRO A 377 ? 0.58421 0.64319 0.55612 -0.02527 0.10469  -0.00401 343 PRO A O   
2521 C CB  . PRO A 377 ? 0.52883 0.59016 0.47644 -0.02027 0.13112  -0.00558 343 PRO A CB  
2522 C CG  . PRO A 377 ? 0.57013 0.61856 0.49347 -0.01394 0.12235  -0.01218 343 PRO A CG  
2523 C CD  . PRO A 377 ? 0.66379 0.69730 0.55899 -0.01474 0.12049  -0.00609 343 PRO A CD  
2524 N N   . GLN A 378 ? 0.54999 0.60462 0.51706 -0.03412 0.10974  0.01165  344 GLN A N   
2525 C CA  . GLN A 378 ? 0.64145 0.69600 0.62251 -0.03591 0.09656  0.01186  344 GLN A CA  
2526 C C   . GLN A 378 ? 0.61356 0.68031 0.62362 -0.03642 0.09548  0.00780  344 GLN A C   
2527 O O   . GLN A 378 ? 0.44782 0.51377 0.46591 -0.03521 0.08515  0.00336  344 GLN A O   
2528 C CB  . GLN A 378 ? 0.59354 0.64339 0.57375 -0.04156 0.09501  0.02161  344 GLN A CB  
2529 C CG  . GLN A 378 ? 0.52689 0.57709 0.52208 -0.04324 0.08235  0.02212  344 GLN A CG  
2530 C CD  . GLN A 378 ? 0.61459 0.65450 0.59854 -0.04616 0.07684  0.02986  344 GLN A CD  
2531 O OE1 . GLN A 378 ? 0.66635 0.69423 0.62645 -0.04324 0.07170  0.02997  344 GLN A OE1 
2532 N NE2 . GLN A 378 ? 0.61352 0.65709 0.61406 -0.05142 0.07694  0.03601  344 GLN A NE2 
2533 N N   . ALA A 379 ? 0.50218 0.57982 0.52802 -0.03814 0.10605  0.00899  345 ALA A N   
2534 C CA  . ALA A 379 ? 0.49268 0.58036 0.54492 -0.03785 0.10424  0.00515  345 ALA A CA  
2535 C C   . ALA A 379 ? 0.54298 0.62974 0.59388 -0.03187 0.10032  -0.00469 345 ALA A C   
2536 O O   . ALA A 379 ? 0.46484 0.55174 0.52871 -0.03133 0.09240  -0.00828 345 ALA A O   
2537 C CB  . ALA A 379 ? 0.46472 0.56502 0.53414 -0.04005 0.11616  0.00727  345 ALA A CB  
2538 N N   . LEU A 380 ? 0.45589 0.54015 0.48965 -0.02741 0.10586  -0.00914 346 LEU A N   
2539 C CA  . LEU A 380 ? 0.49370 0.57523 0.52398 -0.02175 0.10172  -0.01872 346 LEU A CA  
2540 C C   . LEU A 380 ? 0.44203 0.51332 0.46243 -0.02150 0.08896  -0.02150 346 LEU A C   
2541 O O   . LEU A 380 ? 0.51378 0.58321 0.54050 -0.01975 0.08240  -0.02808 346 LEU A O   
2542 C CB  . LEU A 380 ? 0.51429 0.59501 0.52736 -0.01666 0.11090  -0.02282 346 LEU A CB  
2543 C CG  . LEU A 380 ? 0.62390 0.71678 0.64926 -0.01494 0.12387  -0.02403 346 LEU A CG  
2544 C CD1 . LEU A 380 ? 0.54317 0.63337 0.54661 -0.01030 0.13381  -0.02683 346 LEU A CD1 
2545 C CD2 . LEU A 380 ? 0.57851 0.67695 0.62343 -0.01145 0.12036  -0.03125 346 LEU A CD2 
2546 N N   . ILE A 381 ? 0.44163 0.50580 0.44644 -0.02322 0.08529  -0.01694 347 ILE A N   
2547 C CA  . ILE A 381 ? 0.44968 0.50601 0.44749 -0.02283 0.07278  -0.02019 347 ILE A CA  
2548 C C   . ILE A 381 ? 0.42808 0.48761 0.44683 -0.02657 0.06550  -0.01953 347 ILE A C   
2549 O O   . ILE A 381 ? 0.38986 0.44723 0.41330 -0.02592 0.05828  -0.02593 347 ILE A O   
2550 C CB  . ILE A 381 ? 0.43256 0.48030 0.40943 -0.02305 0.06978  -0.01536 347 ILE A CB  
2551 C CG1 . ILE A 381 ? 0.42904 0.46998 0.38063 -0.01815 0.07520  -0.01795 347 ILE A CG1 
2552 C CG2 . ILE A 381 ? 0.38159 0.42415 0.35734 -0.02317 0.05598  -0.01825 347 ILE A CG2 
2553 C CD1 . ILE A 381 ? 0.56153 0.59138 0.48858 -0.01772 0.07360  -0.01258 347 ILE A CD1 
2554 N N   . LEU A 382 ? 0.37673 0.44074 0.40800 -0.03073 0.06771  -0.01195 348 LEU A N   
2555 C CA  . LEU A 382 ? 0.36829 0.43393 0.41742 -0.03383 0.06105  -0.01097 348 LEU A CA  
2556 C C   . LEU A 382 ? 0.31041 0.37922 0.37452 -0.03261 0.06163  -0.01655 348 LEU A C   
2557 O O   . LEU A 382 ? 0.39282 0.45935 0.46625 -0.03415 0.05505  -0.01846 348 LEU A O   
2558 C CB  . LEU A 382 ? 0.38311 0.45182 0.44136 -0.03809 0.06311  -0.00186 348 LEU A CB  
2559 C CG  . LEU A 382 ? 0.46796 0.53050 0.51171 -0.03978 0.06000  0.00426  348 LEU A CG  
2560 C CD1 . LEU A 382 ? 0.41789 0.48277 0.47071 -0.04440 0.06317  0.01323  348 LEU A CD1 
2561 C CD2 . LEU A 382 ? 0.37744 0.43467 0.41807 -0.03918 0.04832  0.00129  348 LEU A CD2 
2562 N N   . ASP A 383 ? 0.36918 0.44219 0.43465 -0.02956 0.06939  -0.01947 349 ASP A N   
2563 C CA  . ASP A 383 ? 0.37810 0.45199 0.45493 -0.02714 0.06923  -0.02555 349 ASP A CA  
2564 C C   . ASP A 383 ? 0.45646 0.52331 0.52280 -0.02397 0.06531  -0.03427 349 ASP A C   
2565 O O   . ASP A 383 ? 0.43366 0.49794 0.50691 -0.02222 0.06382  -0.03960 349 ASP A O   
2566 C CB  . ASP A 383 ? 0.40605 0.48848 0.49088 -0.02449 0.07880  -0.02571 349 ASP A CB  
2567 C CG  . ASP A 383 ? 0.47186 0.56081 0.57724 -0.02696 0.07958  -0.02112 349 ASP A CG  
2568 O OD1 . ASP A 383 ? 0.55016 0.63514 0.66273 -0.02992 0.07231  -0.01865 349 ASP A OD1 
2569 O OD2 . ASP A 383 ? 0.60539 0.70368 0.72017 -0.02578 0.08749  -0.02039 349 ASP A OD2 
2570 N N   . HIS A 384 ? 0.37412 0.43656 0.42334 -0.02304 0.06304  -0.03607 350 HIS A N   
2571 C CA  . HIS A 384 ? 0.33628 0.39198 0.37571 -0.02023 0.05880  -0.04484 350 HIS A CA  
2572 C C   . HIS A 384 ? 0.29552 0.34647 0.34268 -0.02378 0.04994  -0.04790 350 HIS A C   
2573 O O   . HIS A 384 ? 0.28458 0.33613 0.33529 -0.02747 0.04522  -0.04392 350 HIS A O   
2574 C CB  . HIS A 384 ? 0.37876 0.43049 0.39715 -0.01780 0.05784  -0.04613 350 HIS A CB  
2575 C CG  . HIS A 384 ? 0.43273 0.47791 0.43944 -0.01375 0.05497  -0.05556 350 HIS A CG  
2576 N ND1 . HIS A 384 ? 0.39241 0.43204 0.39999 -0.01535 0.04569  -0.06186 350 HIS A ND1 
2577 C CD2 . HIS A 384 ? 0.34226 0.38530 0.33608 -0.00826 0.06015  -0.06006 350 HIS A CD2 
2578 C CE1 . HIS A 384 ? 0.46112 0.49489 0.45698 -0.01126 0.04456  -0.06980 350 HIS A CE1 
2579 N NE2 . HIS A 384 ? 0.40621 0.44149 0.39273 -0.00647 0.05305  -0.06887 350 HIS A NE2 
2580 N N   . PRO A 385 ? 0.33353 0.37908 0.38277 -0.02284 0.04783  -0.05512 351 PRO A N   
2581 C CA  . PRO A 385 ? 0.36140 0.40184 0.41834 -0.02724 0.04111  -0.05792 351 PRO A CA  
2582 C C   . PRO A 385 ? 0.43022 0.46943 0.48165 -0.02969 0.03403  -0.06043 351 PRO A C   
2583 O O   . PRO A 385 ? 0.38551 0.42353 0.44581 -0.03423 0.02948  -0.06107 351 PRO A O   
2584 C CB  . PRO A 385 ? 0.35699 0.38978 0.41300 -0.02529 0.04125  -0.06556 351 PRO A CB  
2585 C CG  . PRO A 385 ? 0.42905 0.46283 0.47325 -0.01914 0.04584  -0.06863 351 PRO A CG  
2586 C CD  . PRO A 385 ? 0.35820 0.40140 0.40303 -0.01781 0.05208  -0.06094 351 PRO A CD  
2587 N N   . SER A 386 ? 0.40910 0.44838 0.44614 -0.02654 0.03282  -0.06220 352 SER A N   
2588 C CA  . SER A 386 ? 0.35969 0.39778 0.39191 -0.02784 0.02456  -0.06582 352 SER A CA  
2589 C C   . SER A 386 ? 0.32218 0.36480 0.35751 -0.02988 0.02167  -0.05901 352 SER A C   
2590 O O   . SER A 386 ? 0.33027 0.37327 0.36658 -0.03133 0.01394  -0.06217 352 SER A O   
2591 C CB  . SER A 386 ? 0.45904 0.49316 0.47224 -0.02269 0.02287  -0.07084 352 SER A CB  
2592 O OG  . SER A 386 ? 0.46423 0.49289 0.47418 -0.02078 0.02357  -0.07860 352 SER A OG  
2593 N N   . ILE A 387 ? 0.33447 0.38058 0.37212 -0.02997 0.02722  -0.05029 353 ILE A N   
2594 C CA  . ILE A 387 ? 0.38553 0.43425 0.42526 -0.03184 0.02422  -0.04356 353 ILE A CA  
2595 C C   . ILE A 387 ? 0.37049 0.42116 0.42755 -0.03640 0.02120  -0.04291 353 ILE A C   
2596 O O   . ILE A 387 ? 0.36559 0.41630 0.43322 -0.03813 0.02534  -0.04154 353 ILE A O   
2597 C CB  . ILE A 387 ? 0.40336 0.45422 0.43941 -0.03111 0.03150  -0.03454 353 ILE A CB  
2598 C CG1 . ILE A 387 ? 0.36848 0.41619 0.38456 -0.02677 0.03530  -0.03502 353 ILE A CG1 
2599 C CG2 . ILE A 387 ? 0.34950 0.40141 0.38862 -0.03352 0.02801  -0.02729 353 ILE A CG2 
2600 C CD1 . ILE A 387 ? 0.38427 0.42651 0.38392 -0.02442 0.02747  -0.03705 353 ILE A CD1 
2601 N N   . GLY A 388 ? 0.33555 0.38729 0.39490 -0.03782 0.01379  -0.04440 354 GLY A N   
2602 C CA  . GLY A 388 ? 0.39929 0.45287 0.47380 -0.04194 0.01149  -0.04401 354 GLY A CA  
2603 C C   . GLY A 388 ? 0.42911 0.48506 0.50573 -0.04231 0.00828  -0.03734 354 GLY A C   
2604 O O   . GLY A 388 ? 0.36916 0.42660 0.45725 -0.04512 0.00624  -0.03673 354 GLY A O   
2605 N N   . GLY A 389 ? 0.34016 0.39517 0.40447 -0.03943 0.00803  -0.03230 355 GLY A N   
2606 C CA  . GLY A 389 ? 0.29688 0.35201 0.36074 -0.03944 0.00430  -0.02589 355 GLY A CA  
2607 C C   . GLY A 389 ? 0.39318 0.44461 0.44143 -0.03713 0.00692  -0.01913 355 GLY A C   
2608 O O   . GLY A 389 ? 0.36864 0.41750 0.40362 -0.03458 0.00988  -0.02094 355 GLY A O   
2609 N N   . PHE A 390 ? 0.31253 0.36260 0.36143 -0.03819 0.00601  -0.01130 356 PHE A N   
2610 C CA  . PHE A 390 ? 0.31964 0.36486 0.35443 -0.03750 0.00958  -0.00345 356 PHE A CA  
2611 C C   . PHE A 390 ? 0.39031 0.43072 0.41886 -0.03650 0.00157  0.00052  356 PHE A C   
2612 O O   . PHE A 390 ? 0.34736 0.38855 0.38626 -0.03878 0.00011  0.00515  356 PHE A O   
2613 C CB  . PHE A 390 ? 0.28241 0.33034 0.32628 -0.04081 0.01885  0.00315  356 PHE A CB  
2614 C CG  . PHE A 390 ? 0.36799 0.41187 0.39889 -0.04142 0.02495  0.01087  356 PHE A CG  
2615 C CD1 . PHE A 390 ? 0.41907 0.45542 0.42760 -0.03852 0.02366  0.01121  356 PHE A CD1 
2616 C CD2 . PHE A 390 ? 0.36872 0.41564 0.40962 -0.04510 0.03210  0.01757  356 PHE A CD2 
2617 C CE1 . PHE A 390 ? 0.46344 0.49434 0.45832 -0.03984 0.03065  0.01874  356 PHE A CE1 
2618 C CE2 . PHE A 390 ? 0.46194 0.50561 0.49238 -0.04689 0.03902  0.02458  356 PHE A CE2 
2619 C CZ  . PHE A 390 ? 0.43681 0.47196 0.44347 -0.04454 0.03895  0.02548  356 PHE A CZ  
2620 N N   . LEU A 391 ? 0.39780 0.43203 0.40830 -0.03244 -0.00434 -0.00164 357 LEU A N   
2621 C CA  . LEU A 391 ? 0.36613 0.39330 0.36646 -0.03020 -0.01266 0.00196  357 LEU A CA  
2622 C C   . LEU A 391 ? 0.40960 0.42744 0.39339 -0.03143 -0.00672 0.01199  357 LEU A C   
2623 O O   . LEU A 391 ? 0.39160 0.40371 0.35755 -0.02988 -0.00199 0.01259  357 LEU A O   
2624 C CB  . LEU A 391 ? 0.36654 0.39055 0.35517 -0.02454 -0.02315 -0.00608 357 LEU A CB  
2625 C CG  . LEU A 391 ? 0.41617 0.43025 0.38869 -0.02007 -0.03339 -0.00381 357 LEU A CG  
2626 C CD1 . LEU A 391 ? 0.41613 0.43207 0.40150 -0.02168 -0.03738 0.00027  357 LEU A CD1 
2627 C CD2 . LEU A 391 ? 0.46410 0.47832 0.43130 -0.01415 -0.04488 -0.01435 357 LEU A CD2 
2628 N N   . THR A 392 ? 0.43140 0.44707 0.42063 -0.03449 -0.00643 0.01979  358 THR A N   
2629 C CA  . THR A 392 ? 0.42681 0.43385 0.40291 -0.03730 0.00026  0.02969  358 THR A CA  
2630 C C   . THR A 392 ? 0.44680 0.44825 0.42551 -0.03906 -0.00504 0.03652  358 THR A C   
2631 O O   . THR A 392 ? 0.40317 0.40754 0.39266 -0.03726 -0.01384 0.03330  358 THR A O   
2632 C CB  . THR A 392 ? 0.53171 0.54600 0.51820 -0.04201 0.01368  0.03255  358 THR A CB  
2633 O OG1 . THR A 392 ? 0.48285 0.48902 0.45378 -0.04473 0.02173  0.04074  358 THR A OG1 
2634 C CG2 . THR A 392 ? 0.25500 0.27778 0.26671 -0.04597 0.01479  0.03437  358 THR A CG2 
2635 N N   . HIS A 393 ? 0.42700 0.42023 0.39590 -0.04291 0.00106  0.04590  359 HIS A N   
2636 C CA  . HIS A 393 ? 0.45651 0.43972 0.42078 -0.04463 -0.00382 0.05352  359 HIS A CA  
2637 C C   . HIS A 393 ? 0.40581 0.39604 0.39347 -0.04968 -0.00160 0.05732  359 HIS A C   
2638 O O   . HIS A 393 ? 0.38864 0.37046 0.37393 -0.05135 -0.00595 0.06353  359 HIS A O   
2639 C CB  . HIS A 393 ? 0.44825 0.41701 0.38862 -0.04724 0.00232  0.06201  359 HIS A CB  
2640 C CG  . HIS A 393 ? 0.57329 0.54804 0.51676 -0.05228 0.01754  0.06456  359 HIS A CG  
2641 N ND1 . HIS A 393 ? 0.50982 0.49666 0.47770 -0.05801 0.02548  0.06666  359 HIS A ND1 
2642 C CD2 . HIS A 393 ? 0.64269 0.61316 0.56804 -0.05188 0.02615  0.06477  359 HIS A CD2 
2643 C CE1 . HIS A 393 ? 0.55694 0.54815 0.52344 -0.06093 0.03838  0.06774  359 HIS A CE1 
2644 N NE2 . HIS A 393 ? 0.64873 0.63006 0.58913 -0.05744 0.03963  0.06680  359 HIS A NE2 
2645 N N   . CYS A 394 ? 0.33234 0.33602 0.34088 -0.05180 0.00450  0.05378  360 CYS A N   
2646 C CA  . CYS A 394 ? 0.39164 0.40143 0.42211 -0.05559 0.00561  0.05623  360 CYS A CA  
2647 C C   . CYS A 394 ? 0.42920 0.43604 0.46163 -0.06189 0.01305  0.06509  360 CYS A C   
2648 O O   . CYS A 394 ? 0.37766 0.38475 0.42358 -0.06477 0.01080  0.06868  360 CYS A O   
2649 C CB  . CYS A 394 ? 0.41839 0.42485 0.45398 -0.05323 -0.00559 0.05565  360 CYS A CB  
2650 S SG  . CYS A 394 ? 0.58376 0.59476 0.62010 -0.04680 -0.01428 0.04519  360 CYS A SG  
2651 N N   . GLY A 395 ? 0.33316 0.33661 0.35215 -0.06429 0.02191  0.06864  361 GLY A N   
2652 C CA  . GLY A 395 ? 0.34930 0.35424 0.37571 -0.07133 0.03164  0.07555  361 GLY A CA  
2653 C C   . GLY A 395 ? 0.36946 0.38948 0.42334 -0.07316 0.03609  0.07224  361 GLY A C   
2654 O O   . GLY A 395 ? 0.28118 0.30967 0.34347 -0.06921 0.03518  0.06471  361 GLY A O   
2655 N N   . TRP A 396 ? 0.34803 0.37672 0.30332 0.00390  -0.00024 0.03247  362 TRP A N   
2656 C CA  . TRP A 396 ? 0.44883 0.47423 0.40835 0.00441  0.00135  0.03262  362 TRP A CA  
2657 C C   . TRP A 396 ? 0.41572 0.44804 0.38184 0.00663  0.00321  0.02709  362 TRP A C   
2658 O O   . TRP A 396 ? 0.33743 0.36454 0.30889 0.00847  0.00391  0.02488  362 TRP A O   
2659 C CB  . TRP A 396 ? 0.41591 0.44081 0.37160 0.00185  0.00041  0.03837  362 TRP A CB  
2660 C CG  . TRP A 396 ? 0.42364 0.44414 0.38325 0.00246  0.00033  0.03916  362 TRP A CG  
2661 C CD1 . TRP A 396 ? 0.38126 0.40837 0.34597 0.00291  0.00008  0.03920  362 TRP A CD1 
2662 C CD2 . TRP A 396 ? 0.33436 0.34271 0.29305 0.00260  0.00010  0.04000  362 TRP A CD2 
2663 N NE1 . TRP A 396 ? 0.33282 0.35177 0.29961 0.00377  -0.00164 0.04064  362 TRP A NE1 
2664 C CE2 . TRP A 396 ? 0.36335 0.37005 0.32494 0.00308  -0.00139 0.04138  362 TRP A CE2 
2665 C CE3 . TRP A 396 ? 0.41462 0.41367 0.37044 0.00210  0.00120  0.03952  362 TRP A CE3 
2666 C CZ2 . TRP A 396 ? 0.43492 0.42922 0.39377 0.00253  -0.00235 0.04312  362 TRP A CZ2 
2667 C CZ3 . TRP A 396 ? 0.53026 0.51814 0.48392 0.00112  0.00177  0.04050  362 TRP A CZ3 
2668 C CH2 . TRP A 396 ? 0.42927 0.41398 0.38303 0.00107  -0.00025 0.04269  362 TRP A CH2 
2669 N N   . ASN A 397 ? 0.34855 0.39167 0.31366 0.00630  0.00417  0.02466  363 ASN A N   
2670 C CA  . ASN A 397 ? 0.37342 0.42340 0.34538 0.00874  0.00661  0.01830  363 ASN A CA  
2671 C C   . ASN A 397 ? 0.34479 0.39102 0.32050 0.01091  0.00694  0.01215  363 ASN A C   
2672 O O   . ASN A 397 ? 0.41358 0.45716 0.39649 0.01356  0.00804  0.00816  363 ASN A O   
2673 C CB  . ASN A 397 ? 0.41888 0.48155 0.38747 0.00702  0.00878  0.01620  363 ASN A CB  
2674 C CG  . ASN A 397 ? 0.67313 0.74340 0.64953 0.00991  0.01219  0.00820  363 ASN A CG  
2675 O OD1 . ASN A 397 ? 0.64721 0.71975 0.63251 0.01221  0.01326  0.00732  363 ASN A OD1 
2676 N ND2 . ASN A 397 ? 0.67730 0.75111 0.65091 0.01007  0.01339  0.00193  363 ASN A ND2 
2677 N N   . ALA A 398 ? 0.31514 0.36065 0.28668 0.00976  0.00543  0.01139  364 ALA A N   
2678 C CA  . ALA A 398 ? 0.41039 0.45265 0.38646 0.01089  0.00542  0.00562  364 ALA A CA  
2679 C C   . ALA A 398 ? 0.37170 0.40270 0.35268 0.01138  0.00602  0.00686  364 ALA A C   
2680 O O   . ALA A 398 ? 0.39937 0.42631 0.38580 0.01241  0.00724  0.00208  364 ALA A O   
2681 C CB  . ALA A 398 ? 0.34995 0.39424 0.32218 0.00955  0.00251  0.00535  364 ALA A CB  
2682 N N   . THR A 399 ? 0.38967 0.41444 0.36752 0.01010  0.00534  0.01322  365 THR A N   
2683 C CA  . THR A 399 ? 0.34300 0.35620 0.32248 0.00946  0.00637  0.01487  365 THR A CA  
2684 C C   . THR A 399 ? 0.34397 0.35295 0.32635 0.01106  0.00662  0.01478  365 THR A C   
2685 O O   . THR A 399 ? 0.36423 0.36451 0.34933 0.01107  0.00747  0.01285  365 THR A O   
2686 C CB  . THR A 399 ? 0.46827 0.47584 0.44207 0.00750  0.00579  0.02114  365 THR A CB  
2687 O OG1 . THR A 399 ? 0.37735 0.38779 0.35040 0.00701  0.00497  0.02079  365 THR A OG1 
2688 C CG2 . THR A 399 ? 0.30681 0.30185 0.27948 0.00584  0.00746  0.02284  365 THR A CG2 
2689 N N   . VAL A 400 ? 0.34347 0.35837 0.32591 0.01229  0.00560  0.01694  366 VAL A N   
2690 C CA  . VAL A 400 ? 0.33139 0.34368 0.31895 0.01482  0.00469  0.01679  366 VAL A CA  
2691 C C   . VAL A 400 ? 0.39771 0.41175 0.39247 0.01787  0.00601  0.00922  366 VAL A C   
2692 O O   . VAL A 400 ? 0.38201 0.38680 0.38071 0.01972  0.00510  0.00825  366 VAL A O   
2693 C CB  . VAL A 400 ? 0.40707 0.42851 0.39571 0.01526  0.00352  0.01985  366 VAL A CB  
2694 C CG1 . VAL A 400 ? 0.35668 0.37964 0.35471 0.01930  0.00232  0.01764  366 VAL A CG1 
2695 C CG2 . VAL A 400 ? 0.34297 0.35865 0.32455 0.01204  0.00141  0.02742  366 VAL A CG2 
2696 N N   . GLU A 401 ? 0.28516 0.30974 0.28059 0.01816  0.00783  0.00378  367 GLU A N   
2697 C CA  . GLU A 401 ? 0.39937 0.42532 0.40068 0.02066  0.00935  -0.00453 367 GLU A CA  
2698 C C   . GLU A 401 ? 0.40217 0.41649 0.40426 0.01941  0.00931  -0.00677 367 GLU A C   
2699 O O   . GLU A 401 ? 0.37303 0.38023 0.38044 0.02149  0.00945  -0.01080 367 GLU A O   
2700 C CB  . GLU A 401 ? 0.38821 0.42710 0.38689 0.01997  0.01117  -0.00976 367 GLU A CB  
2701 C CG  . GLU A 401 ? 0.40597 0.45698 0.40620 0.02128  0.01306  -0.01063 367 GLU A CG  
2702 C CD  . GLU A 401 ? 0.59236 0.65503 0.58665 0.01934  0.01537  -0.01551 367 GLU A CD  
2703 O OE1 . GLU A 401 ? 0.55952 0.62076 0.54891 0.01755  0.01437  -0.01835 367 GLU A OE1 
2704 O OE2 . GLU A 401 ? 0.71509 0.78865 0.70938 0.01913  0.01811  -0.01652 367 GLU A OE2 
2705 N N   . ALA A 402 ? 0.31545 0.32754 0.31311 0.01589  0.00923  -0.00445 368 ALA A N   
2706 C CA  . ALA A 402 ? 0.35285 0.35519 0.35228 0.01358  0.01005  -0.00659 368 ALA A CA  
2707 C C   . ALA A 402 ? 0.43312 0.42080 0.43212 0.01320  0.00987  -0.00246 368 ALA A C   
2708 O O   . ALA A 402 ? 0.37736 0.35548 0.37925 0.01272  0.01045  -0.00560 368 ALA A O   
2709 C CB  . ALA A 402 ? 0.32622 0.33082 0.32316 0.01031  0.01020  -0.00488 368 ALA A CB  
2710 N N   . ILE A 403 ? 0.38812 0.37274 0.38237 0.01292  0.00861  0.00477  369 ILE A N   
2711 C CA  . ILE A 403 ? 0.39982 0.36977 0.39116 0.01220  0.00732  0.00951  369 ILE A CA  
2712 C C   . ILE A 403 ? 0.45353 0.41997 0.45097 0.01668  0.00499  0.00713  369 ILE A C   
2713 O O   . ILE A 403 ? 0.40040 0.35296 0.39789 0.01620  0.00428  0.00697  369 ILE A O   
2714 C CB  . ILE A 403 ? 0.43579 0.40429 0.42019 0.01094  0.00562  0.01718  369 ILE A CB  
2715 C CG1 . ILE A 403 ? 0.38954 0.35728 0.36821 0.00663  0.00832  0.01897  369 ILE A CG1 
2716 C CG2 . ILE A 403 ? 0.44307 0.39710 0.42348 0.01072  0.00259  0.02232  369 ILE A CG2 
2717 C CD1 . ILE A 403 ? 0.34386 0.31017 0.31504 0.00513  0.00692  0.02550  369 ILE A CD1 
2718 N N   . SER A 404 ? 0.36544 0.34416 0.36851 0.02101  0.00398  0.00492  370 SER A N   
2719 C CA  . SER A 404 ? 0.43799 0.41502 0.44948 0.02637  0.00188  0.00181  370 SER A CA  
2720 C C   . SER A 404 ? 0.40264 0.37386 0.41881 0.02748  0.00344  -0.00590 370 SER A C   
2721 O O   . SER A 404 ? 0.41708 0.37932 0.43898 0.03137  0.00109  -0.00758 370 SER A O   
2722 C CB  . SER A 404 ? 0.33717 0.33146 0.35518 0.03013  0.00231  -0.00082 370 SER A CB  
2723 O OG  . SER A 404 ? 0.51149 0.51704 0.53093 0.03009  0.00616  -0.00841 370 SER A OG  
2724 N N   . SER A 405 ? 0.40646 0.38200 0.42068 0.02420  0.00666  -0.01067 371 SER A N   
2725 C CA  . SER A 405 ? 0.41300 0.38318 0.43103 0.02399  0.00807  -0.01848 371 SER A CA  
2726 C C   . SER A 405 ? 0.39564 0.35146 0.40961 0.01841  0.00881  -0.01654 371 SER A C   
2727 O O   . SER A 405 ? 0.39371 0.34335 0.41071 0.01704  0.00985  -0.02265 371 SER A O   
2728 C CB  . SER A 405 ? 0.37946 0.36447 0.39831 0.02345  0.01050  -0.02603 371 SER A CB  
2729 O OG  . SER A 405 ? 0.62086 0.61807 0.64337 0.02796  0.01116  -0.02964 371 SER A OG  
2730 N N   . GLY A 406 ? 0.40918 0.35972 0.41627 0.01457  0.00885  -0.00881 372 GLY A N   
2731 C CA  . GLY A 406 ? 0.34987 0.28754 0.35285 0.00839  0.01090  -0.00716 372 GLY A CA  
2732 C C   . GLY A 406 ? 0.42973 0.37514 0.43556 0.00420  0.01416  -0.01282 372 GLY A C   
2733 O O   . GLY A 406 ? 0.40659 0.34279 0.41307 -0.00071 0.01633  -0.01493 372 GLY A O   
2734 N N   . VAL A 407 ? 0.36041 0.32231 0.36801 0.00565  0.01412  -0.01514 373 VAL A N   
2735 C CA  . VAL A 407 ? 0.33976 0.31077 0.35130 0.00269  0.01538  -0.02092 373 VAL A CA  
2736 C C   . VAL A 407 ? 0.36946 0.34458 0.37897 -0.00042 0.01678  -0.01655 373 VAL A C   
2737 O O   . VAL A 407 ? 0.32455 0.30522 0.32994 0.00178  0.01559  -0.01164 373 VAL A O   
2738 C CB  . VAL A 407 ? 0.39448 0.37994 0.40800 0.00620  0.01354  -0.02657 373 VAL A CB  
2739 C CG1 . VAL A 407 ? 0.29046 0.28541 0.30716 0.00308  0.01312  -0.03151 373 VAL A CG1 
2740 C CG2 . VAL A 407 ? 0.33055 0.31196 0.34715 0.00939  0.01321  -0.03265 373 VAL A CG2 
2741 N N   . PRO A 408 ? 0.35593 0.32868 0.36905 -0.00556 0.01953  -0.01864 374 PRO A N   
2742 C CA  . PRO A 408 ? 0.30135 0.27942 0.31493 -0.00774 0.02130  -0.01597 374 PRO A CA  
2743 C C   . PRO A 408 ? 0.41242 0.40639 0.42947 -0.00481 0.01797  -0.01813 374 PRO A C   
2744 O O   . PRO A 408 ? 0.38311 0.38486 0.40392 -0.00369 0.01528  -0.02379 374 PRO A O   
2745 C CB  . PRO A 408 ? 0.35342 0.32695 0.37287 -0.01414 0.02557  -0.01964 374 PRO A CB  
2746 C CG  . PRO A 408 ? 0.40346 0.37399 0.42701 -0.01501 0.02448  -0.02581 374 PRO A CG  
2747 C CD  . PRO A 408 ? 0.31398 0.27840 0.33153 -0.00997 0.02160  -0.02366 374 PRO A CD  
2748 N N   . MET A 409 ? 0.33344 0.33106 0.34809 -0.00383 0.01778  -0.01352 375 MET A N   
2749 C CA  . MET A 409 ? 0.36769 0.37800 0.38386 -0.00093 0.01364  -0.01404 375 MET A CA  
2750 C C   . MET A 409 ? 0.31105 0.32811 0.33670 -0.00259 0.01376  -0.01710 375 MET A C   
2751 O O   . MET A 409 ? 0.34945 0.36195 0.37939 -0.00590 0.01844  -0.01742 375 MET A O   
2752 C CB  . MET A 409 ? 0.38492 0.39528 0.39283 0.00185  0.01208  -0.00709 375 MET A CB  
2753 C CG  . MET A 409 ? 0.37682 0.38558 0.37810 0.00416  0.01092  -0.00486 375 MET A CG  
2754 S SD  . MET A 409 ? 0.46713 0.47071 0.45972 0.00498  0.01093  0.00385  375 MET A SD  
2755 C CE  . MET A 409 ? 0.51650 0.53209 0.50554 0.00725  0.00672  0.00548  375 MET A CE  
2756 N N   . VAL A 410 ? 0.32731 0.35564 0.35640 -0.00046 0.00844  -0.01970 376 VAL A N   
2757 C CA  . VAL A 410 ? 0.28666 0.32330 0.32510 0.00004  0.00613  -0.02128 376 VAL A CA  
2758 C C   . VAL A 410 ? 0.36888 0.40831 0.40021 0.00415  0.00144  -0.01554 376 VAL A C   
2759 O O   . VAL A 410 ? 0.39819 0.44177 0.42234 0.00595  -0.00341 -0.01464 376 VAL A O   
2760 C CB  . VAL A 410 ? 0.34476 0.39125 0.39288 -0.00110 0.00201  -0.02857 376 VAL A CB  
2761 C CG1 . VAL A 410 ? 0.31841 0.37379 0.37981 -0.00042 -0.00033 -0.03062 376 VAL A CG1 
2762 C CG2 . VAL A 410 ? 0.36730 0.40889 0.41976 -0.00578 0.00646  -0.03400 376 VAL A CG2 
2763 N N   . THR A 411 ? 0.33690 0.37302 0.36901 0.00509  0.00335  -0.01175 377 THR A N   
2764 C CA  . THR A 411 ? 0.34579 0.38000 0.36867 0.00807  0.00020  -0.00517 377 THR A CA  
2765 C C   . THR A 411 ? 0.32278 0.36441 0.35096 0.01133  -0.00663 -0.00508 377 THR A C   
2766 O O   . THR A 411 ? 0.33920 0.38467 0.38034 0.01209  -0.00647 -0.00852 377 THR A O   
2767 C CB  . THR A 411 ? 0.36864 0.39297 0.38736 0.00717  0.00561  -0.00103 377 THR A CB  
2768 O OG1 . THR A 411 ? 0.37743 0.40224 0.40713 0.00638  0.00933  -0.00449 377 THR A OG1 
2769 C CG2 . THR A 411 ? 0.42697 0.44287 0.43878 0.00427  0.01040  0.00011  377 THR A CG2 
2770 N N   . MET A 412 ? 0.34032 0.38386 0.35868 0.01312  -0.01269 -0.00112 378 MET A N   
2771 C CA  . MET A 412 ? 0.37376 0.42163 0.39360 0.01631  -0.02080 0.00082  378 MET A CA  
2772 C C   . MET A 412 ? 0.41608 0.45828 0.42086 0.01697  -0.02325 0.00867  378 MET A C   
2773 O O   . MET A 412 ? 0.38979 0.43453 0.38374 0.01615  -0.02731 0.01079  378 MET A O   
2774 C CB  . MET A 412 ? 0.36252 0.41985 0.38507 0.01624  -0.02751 -0.00355 378 MET A CB  
2775 C CG  . MET A 412 ? 0.47149 0.53368 0.49974 0.01977  -0.03701 -0.00261 378 MET A CG  
2776 S SD  . MET A 412 ? 0.55214 0.62567 0.58440 0.01883  -0.04545 -0.00875 378 MET A SD  
2777 C CE  . MET A 412 ? 0.46393 0.54242 0.51579 0.01625  -0.03815 -0.01799 378 MET A CE  
2778 N N   . PRO A 413 ? 0.38466 0.41886 0.38772 0.01769  -0.02037 0.01283  379 PRO A N   
2779 C CA  . PRO A 413 ? 0.37224 0.40024 0.36106 0.01709  -0.02182 0.02024  379 PRO A CA  
2780 C C   . PRO A 413 ? 0.41253 0.44124 0.39583 0.01903  -0.03081 0.02444  379 PRO A C   
2781 O O   . PRO A 413 ? 0.37764 0.40847 0.37009 0.02245  -0.03629 0.02290  379 PRO A O   
2782 C CB  . PRO A 413 ? 0.32416 0.34297 0.31438 0.01727  -0.01699 0.02223  379 PRO A CB  
2783 C CG  . PRO A 413 ? 0.38202 0.40327 0.38786 0.01951  -0.01558 0.01652  379 PRO A CG  
2784 C CD  . PRO A 413 ? 0.37917 0.40949 0.39270 0.01832  -0.01505 0.01040  379 PRO A CD  
2785 N N   . GLY A 414 ? 0.40454 0.43128 0.37285 0.01660  -0.03242 0.02994  380 GLY A N   
2786 C CA  . GLY A 414 ? 0.48129 0.50761 0.44013 0.01690  -0.04093 0.03472  380 GLY A CA  
2787 C C   . GLY A 414 ? 0.49110 0.50688 0.44121 0.01675  -0.04333 0.04260  380 GLY A C   
2788 O O   . GLY A 414 ? 0.49854 0.51002 0.44737 0.01930  -0.05136 0.04616  380 GLY A O   
2789 N N   . PHE A 415 ? 0.38456 0.39546 0.32890 0.01376  -0.03719 0.04541  381 PHE A N   
2790 C CA  . PHE A 415 ? 0.45647 0.45671 0.39172 0.01249  -0.03916 0.05270  381 PHE A CA  
2791 C C   . PHE A 415 ? 0.43094 0.42702 0.36499 0.00970  -0.03174 0.05344  381 PHE A C   
2792 O O   . PHE A 415 ? 0.46290 0.46479 0.39996 0.00821  -0.02591 0.04975  381 PHE A O   
2793 C CB  . PHE A 415 ? 0.47355 0.47322 0.39240 0.00856  -0.04396 0.05908  381 PHE A CB  
2794 C CG  . PHE A 415 ? 0.50326 0.50849 0.41343 0.00291  -0.03784 0.05979  381 PHE A CG  
2795 C CD1 . PHE A 415 ? 0.53502 0.55153 0.44597 0.00189  -0.03492 0.05449  381 PHE A CD1 
2796 C CD2 . PHE A 415 ? 0.58809 0.58766 0.49056 -0.00134 -0.03505 0.06514  381 PHE A CD2 
2797 C CE1 . PHE A 415 ? 0.51012 0.53270 0.41567 -0.00245 -0.02897 0.05415  381 PHE A CE1 
2798 C CE2 . PHE A 415 ? 0.64695 0.65366 0.54454 -0.00619 -0.02943 0.06511  381 PHE A CE2 
2799 C CZ  . PHE A 415 ? 0.49760 0.51611 0.39734 -0.00635 -0.02625 0.05946  381 PHE A CZ  
2800 N N   . GLY A 416 ? 0.45779 0.44284 0.38712 0.00904  -0.03282 0.05830  382 GLY A N   
2801 C CA  . GLY A 416 ? 0.45585 0.43642 0.37953 0.00480  -0.02793 0.06092  382 GLY A CA  
2802 C C   . GLY A 416 ? 0.39595 0.37721 0.32774 0.00537  -0.02134 0.05587  382 GLY A C   
2803 O O   . GLY A 416 ? 0.38537 0.36340 0.32589 0.00873  -0.01984 0.05177  382 GLY A O   
2804 N N   . ASP A 417 ? 0.42074 0.40619 0.34958 0.00183  -0.01738 0.05618  383 ASP A N   
2805 C CA  . ASP A 417 ? 0.40781 0.39222 0.34166 0.00167  -0.01217 0.05270  383 ASP A CA  
2806 C C   . ASP A 417 ? 0.46223 0.45246 0.40597 0.00465  -0.00981 0.04624  383 ASP A C   
2807 O O   . ASP A 417 ? 0.36927 0.35654 0.31652 0.00435  -0.00559 0.04346  383 ASP A O   
2808 C CB  . ASP A 417 ? 0.43990 0.42830 0.36979 -0.00210 -0.01009 0.05473  383 ASP A CB  
2809 C CG  . ASP A 417 ? 0.73544 0.71743 0.65693 -0.00625 -0.01151 0.06055  383 ASP A CG  
2810 O OD1 . ASP A 417 ? 0.63081 0.60173 0.54945 -0.00624 -0.01254 0.06206  383 ASP A OD1 
2811 O OD2 . ASP A 417 ? 0.72166 0.70996 0.64008 -0.00973 -0.01133 0.06306  383 ASP A OD2 
2812 N N   . GLN A 418 ? 0.39717 0.39477 0.34449 0.00684  -0.01269 0.04392  384 GLN A N   
2813 C CA  . GLN A 418 ? 0.44035 0.44406 0.39713 0.00865  -0.01051 0.03746  384 GLN A CA  
2814 C C   . GLN A 418 ? 0.40466 0.40405 0.37065 0.01067  -0.00821 0.03362  384 GLN A C   
2815 O O   . GLN A 418 ? 0.35219 0.35362 0.32513 0.01045  -0.00423 0.02873  384 GLN A O   
2816 C CB  . GLN A 418 ? 0.32899 0.34161 0.28636 0.00985  -0.01485 0.03563  384 GLN A CB  
2817 C CG  . GLN A 418 ? 0.38646 0.40491 0.33494 0.00715  -0.01501 0.03766  384 GLN A CG  
2818 C CD  . GLN A 418 ? 0.36502 0.39022 0.30939 0.00729  -0.01984 0.03690  384 GLN A CD  
2819 O OE1 . GLN A 418 ? 0.39529 0.42055 0.34350 0.00975  -0.02467 0.03575  384 GLN A OE1 
2820 N NE2 . GLN A 418 ? 0.41553 0.44681 0.35214 0.00452  -0.01867 0.03723  384 GLN A NE2 
2821 N N   . TYR A 419 ? 0.34160 0.33477 0.30805 0.01240  -0.01021 0.03539  385 TYR A N   
2822 C CA  . TYR A 419 ? 0.33850 0.32850 0.31476 0.01424  -0.00672 0.03075  385 TYR A CA  
2823 C C   . TYR A 419 ? 0.40731 0.38982 0.37995 0.01097  0.00031  0.03007  385 TYR A C   
2824 O O   . TYR A 419 ? 0.33292 0.31471 0.31278 0.01067  0.00555  0.02507  385 TYR A O   
2825 C CB  . TYR A 419 ? 0.37078 0.35537 0.34924 0.01767  -0.01069 0.03220  385 TYR A CB  
2826 C CG  . TYR A 419 ? 0.41672 0.40664 0.39696 0.02086  -0.01924 0.03401  385 TYR A CG  
2827 C CD1 . TYR A 419 ? 0.33365 0.33307 0.32662 0.02393  -0.02186 0.02891  385 TYR A CD1 
2828 C CD2 . TYR A 419 ? 0.45837 0.44339 0.42678 0.02012  -0.02507 0.04103  385 TYR A CD2 
2829 C CE1 . TYR A 419 ? 0.41551 0.41913 0.40859 0.02660  -0.03094 0.03090  385 TYR A CE1 
2830 C CE2 . TYR A 419 ? 0.38914 0.37733 0.35636 0.02233  -0.03348 0.04348  385 TYR A CE2 
2831 C CZ  . TYR A 419 ? 0.42044 0.41777 0.39961 0.02578  -0.03681 0.03848  385 TYR A CZ  
2832 O OH  . TYR A 419 ? 0.47933 0.47914 0.45582 0.02775  -0.04639 0.04126  385 TYR A OH  
2833 N N   . TYR A 420 ? 0.37632 0.35325 0.33755 0.00795  0.00037  0.03505  386 TYR A N   
2834 C CA  . TYR A 420 ? 0.35704 0.32637 0.31310 0.00451  0.00557  0.03499  386 TYR A CA  
2835 C C   . TYR A 420 ? 0.37678 0.35030 0.33419 0.00295  0.00777  0.03336  386 TYR A C   
2836 O O   . TYR A 420 ? 0.37618 0.34492 0.33404 0.00092  0.01258  0.03082  386 TYR A O   
2837 C CB  . TYR A 420 ? 0.39981 0.36164 0.34424 0.00178  0.00372  0.04074  386 TYR A CB  
2838 C CG  . TYR A 420 ? 0.45403 0.41095 0.39618 0.00325  0.00020  0.04316  386 TYR A CG  
2839 C CD1 . TYR A 420 ? 0.42445 0.37476 0.37055 0.00531  0.00232  0.03980  386 TYR A CD1 
2840 C CD2 . TYR A 420 ? 0.50238 0.46085 0.43865 0.00242  -0.00498 0.04855  386 TYR A CD2 
2841 C CE1 . TYR A 420 ? 0.44206 0.38616 0.38676 0.00738  -0.00151 0.04185  386 TYR A CE1 
2842 C CE2 . TYR A 420 ? 0.41981 0.37139 0.35288 0.00342  -0.00878 0.05142  386 TYR A CE2 
2843 C CZ  . TYR A 420 ? 0.42910 0.37295 0.36670 0.00635  -0.00748 0.04809  386 TYR A CZ  
2844 O OH  . TYR A 420 ? 0.50764 0.44300 0.44278 0.00806  -0.01181 0.05074  386 TYR A OH  
2845 N N   . ASN A 421 ? 0.37331 0.35493 0.33088 0.00366  0.00452  0.03457  387 ASN A N   
2846 C CA  . ASN A 421 ? 0.40519 0.39048 0.36559 0.00313  0.00618  0.03215  387 ASN A CA  
2847 C C   . ASN A 421 ? 0.35985 0.34670 0.32927 0.00360  0.00937  0.02621  387 ASN A C   
2848 O O   . ASN A 421 ? 0.36207 0.34542 0.33226 0.00177  0.01260  0.02434  387 ASN A O   
2849 C CB  . ASN A 421 ? 0.32070 0.31580 0.28129 0.00434  0.00284  0.03261  387 ASN A CB  
2850 C CG  . ASN A 421 ? 0.40540 0.40076 0.35843 0.00286  0.00062  0.03805  387 ASN A CG  
2851 O OD1 . ASN A 421 ? 0.41748 0.40541 0.36535 0.00080  0.00111  0.04147  387 ASN A OD1 
2852 N ND2 . ASN A 421 ? 0.39349 0.39765 0.34535 0.00319  -0.00167 0.03862  387 ASN A ND2 
2853 N N   . GLU A 422 ? 0.32410 0.31601 0.30087 0.00581  0.00804  0.02330  388 GLU A N   
2854 C CA  . GLU A 422 ? 0.35333 0.34853 0.34092 0.00575  0.01107  0.01712  388 GLU A CA  
2855 C C   . GLU A 422 ? 0.33383 0.32013 0.32073 0.00250  0.01792  0.01565  388 GLU A C   
2856 O O   . GLU A 422 ? 0.39781 0.38281 0.38781 -0.00021 0.02196  0.01241  388 GLU A O   
2857 C CB  . GLU A 422 ? 0.30086 0.30317 0.29775 0.00912  0.00748  0.01459  388 GLU A CB  
2858 C CG  . GLU A 422 ? 0.39398 0.40100 0.40474 0.00873  0.01096  0.00766  388 GLU A CG  
2859 C CD  . GLU A 422 ? 0.44367 0.45918 0.46602 0.01279  0.00591  0.00495  388 GLU A CD  
2860 O OE1 . GLU A 422 ? 0.37915 0.39166 0.40081 0.01576  0.00331  0.00750  388 GLU A OE1 
2861 O OE2 . GLU A 422 ? 0.41019 0.43485 0.44246 0.01305  0.00385  0.00023  388 GLU A OE2 
2862 N N   . LYS A 423 ? 0.31481 0.29384 0.29632 0.00209  0.01950  0.01792  389 LYS A N   
2863 C CA  . LYS A 423 ? 0.36860 0.33891 0.34764 -0.00161 0.02671  0.01592  389 LYS A CA  
2864 C C   . LYS A 423 ? 0.36028 0.32165 0.32829 -0.00595 0.02878  0.01893  389 LYS A C   
2865 O O   . LYS A 423 ? 0.39116 0.34695 0.35810 -0.01004 0.03465  0.01654  389 LYS A O   
2866 C CB  . LYS A 423 ? 0.43768 0.40147 0.41215 -0.00095 0.02760  0.01713  389 LYS A CB  
2867 C CG  . LYS A 423 ? 0.42326 0.39395 0.41051 0.00374  0.02597  0.01339  389 LYS A CG  
2868 C CD  . LYS A 423 ? 0.43182 0.40953 0.43376 0.00330  0.03131  0.00594  389 LYS A CD  
2869 C CE  . LYS A 423 ? 0.55706 0.54607 0.57502 0.00903  0.02620  0.00263  389 LYS A CE  
2870 N NZ  . LYS A 423 ? 0.58020 0.57724 0.61501 0.00839  0.03181  -0.00541 389 LYS A NZ  
2871 N N   . LEU A 424 ? 0.32227 0.28199 0.28213 -0.00535 0.02387  0.02430  390 LEU A N   
2872 C CA  . LEU A 424 ? 0.39573 0.34807 0.34747 -0.00823 0.02390  0.02727  390 LEU A CA  
2873 C C   . LEU A 424 ? 0.39030 0.34469 0.34861 -0.00892 0.02571  0.02372  390 LEU A C   
2874 O O   . LEU A 424 ? 0.36634 0.31108 0.31915 -0.01278 0.02871  0.02426  390 LEU A O   
2875 C CB  . LEU A 424 ? 0.39790 0.35268 0.34511 -0.00640 0.01779  0.03230  390 LEU A CB  
2876 C CG  . LEU A 424 ? 0.43666 0.38480 0.37724 -0.00807 0.01582  0.03590  390 LEU A CG  
2877 C CD1 . LEU A 424 ? 0.40170 0.33579 0.33004 -0.01273 0.01801  0.03859  390 LEU A CD1 
2878 C CD2 . LEU A 424 ? 0.32088 0.27554 0.26128 -0.00583 0.01027  0.03955  390 LEU A CD2 
2879 N N   . VAL A 425 ? 0.31463 0.28039 0.28363 -0.00574 0.02364  0.02012  391 VAL A N   
2880 C CA  . VAL A 425 ? 0.31130 0.27942 0.28698 -0.00634 0.02459  0.01613  391 VAL A CA  
2881 C C   . VAL A 425 ? 0.34375 0.31026 0.32559 -0.01004 0.03078  0.01120  391 VAL A C   
2882 O O   . VAL A 425 ? 0.36478 0.32434 0.34543 -0.01385 0.03397  0.01004  391 VAL A O   
2883 C CB  . VAL A 425 ? 0.39289 0.37377 0.37623 -0.00227 0.01998  0.01353  391 VAL A CB  
2884 C CG1 . VAL A 425 ? 0.39027 0.37454 0.38231 -0.00327 0.02132  0.00759  391 VAL A CG1 
2885 C CG2 . VAL A 425 ? 0.31257 0.29504 0.29042 0.00011  0.01569  0.01733  391 VAL A CG2 
2886 N N   . THR A 426 ? 0.32305 0.29584 0.31226 -0.00913 0.03259  0.00811  392 THR A N   
2887 C CA  . THR A 426 ? 0.33744 0.31384 0.33761 -0.01200 0.03817  0.00184  392 THR A CA  
2888 C C   . THR A 426 ? 0.39926 0.36706 0.39486 -0.01685 0.04626  0.00115  392 THR A C   
2889 O O   . THR A 426 ? 0.39571 0.36253 0.39622 -0.02185 0.05274  -0.00309 392 THR A O   
2890 C CB  . THR A 426 ? 0.33714 0.32755 0.35175 -0.00768 0.03505  -0.00246 392 THR A CB  
2891 O OG1 . THR A 426 ? 0.28905 0.27876 0.30157 -0.00467 0.03411  -0.00032 392 THR A OG1 
2892 C CG2 . THR A 426 ? 0.30952 0.30833 0.32670 -0.00391 0.02740  -0.00232 392 THR A CG2 
2893 N N   . GLU A 427 ? 0.39048 0.35210 0.37662 -0.01614 0.04653  0.00465  393 GLU A N   
2894 C CA  . GLU A 427 ? 0.47097 0.42413 0.45113 -0.02096 0.05476  0.00317  393 GLU A CA  
2895 C C   . GLU A 427 ? 0.47588 0.41299 0.43598 -0.02571 0.05572  0.00906  393 GLU A C   
2896 O O   . GLU A 427 ? 0.53811 0.46597 0.49040 -0.03223 0.06327  0.00791  393 GLU A O   
2897 C CB  . GLU A 427 ? 0.44882 0.40555 0.43333 -0.01711 0.05514  0.00127  393 GLU A CB  
2898 C CG  . GLU A 427 ? 0.45038 0.42096 0.45589 -0.01400 0.05696  -0.00617 393 GLU A CG  
2899 C CD  . GLU A 427 ? 0.59362 0.56583 0.60449 -0.00975 0.05765  -0.00862 393 GLU A CD  
2900 O OE1 . GLU A 427 ? 0.62983 0.59471 0.62951 -0.00757 0.05366  -0.00376 393 GLU A OE1 
2901 O OE2 . GLU A 427 ? 0.66318 0.64419 0.69072 -0.00846 0.06200  -0.01577 393 GLU A OE2 
2902 N N   . VAL A 428 ? 0.45021 0.38407 0.40178 -0.02305 0.04818  0.01526  394 VAL A N   
2903 C CA  . VAL A 428 ? 0.49701 0.41622 0.43081 -0.02720 0.04736  0.02108  394 VAL A CA  
2904 C C   . VAL A 428 ? 0.51883 0.43217 0.45043 -0.03009 0.04694  0.02245  394 VAL A C   
2905 O O   . VAL A 428 ? 0.47355 0.37400 0.39384 -0.03658 0.05136  0.02380  394 VAL A O   
2906 C CB  . VAL A 428 ? 0.45409 0.37299 0.38137 -0.02351 0.03941  0.02683  394 VAL A CB  
2907 C CG1 . VAL A 428 ? 0.44726 0.35184 0.35756 -0.02758 0.03703  0.03287  394 VAL A CG1 
2908 C CG2 . VAL A 428 ? 0.42333 0.34482 0.35106 -0.02152 0.03991  0.02576  394 VAL A CG2 
2909 N N   . HIS A 429 ? 0.35617 0.27766 0.29749 -0.02567 0.04171  0.02200  395 HIS A N   
2910 C CA  . HIS A 429 ? 0.43258 0.34710 0.37183 -0.02719 0.03984  0.02355  395 HIS A CA  
2911 C C   . HIS A 429 ? 0.40517 0.32444 0.35616 -0.02890 0.04363  0.01761  395 HIS A C   
2912 O O   . HIS A 429 ? 0.42441 0.33457 0.37245 -0.03166 0.04344  0.01851  395 HIS A O   
2913 C CB  . HIS A 429 ? 0.35352 0.27196 0.29430 -0.02130 0.03136  0.02689  395 HIS A CB  
2914 C CG  . HIS A 429 ? 0.44917 0.36114 0.37824 -0.02089 0.02689  0.03330  395 HIS A CG  
2915 N ND1 . HIS A 429 ? 0.43532 0.33143 0.35021 -0.02519 0.02602  0.03828  395 HIS A ND1 
2916 C CD2 . HIS A 429 ? 0.35607 0.27492 0.28503 -0.01739 0.02266  0.03564  395 HIS A CD2 
2917 C CE1 . HIS A 429 ? 0.38319 0.27771 0.29079 -0.02401 0.02096  0.04306  395 HIS A CE1 
2918 N NE2 . HIS A 429 ? 0.41917 0.32747 0.33550 -0.01952 0.01927  0.04143  395 HIS A NE2 
2919 N N   . ARG A 430 ? 0.35185 0.28445 0.31627 -0.02745 0.04637  0.01166  396 ARG A N   
2920 C CA  . ARG A 430 ? 0.38024 0.31898 0.35735 -0.02968 0.04965  0.00534  396 ARG A CA  
2921 C C   . ARG A 430 ? 0.33397 0.27296 0.31439 -0.02724 0.04425  0.00503  396 ARG A C   
2922 O O   . ARG A 430 ? 0.34183 0.27520 0.32427 -0.03145 0.04661  0.00268  396 ARG A O   
2923 C CB  . ARG A 430 ? 0.31185 0.24075 0.28462 -0.03847 0.05862  0.00377  396 ARG A CB  
2924 C CG  . ARG A 430 ? 0.39902 0.33080 0.37240 -0.04085 0.06573  0.00123  396 ARG A CG  
2925 C CD  . ARG A 430 ? 0.45724 0.38025 0.42588 -0.05066 0.07618  -0.00106 396 ARG A CD  
2926 N NE  . ARG A 430 ? 0.51946 0.44854 0.50174 -0.05441 0.07943  -0.00672 396 ARG A NE  
2927 C CZ  . ARG A 430 ? 0.47103 0.41674 0.47326 -0.05355 0.08252  -0.01445 396 ARG A CZ  
2928 N NH1 . ARG A 430 ? 0.43022 0.38776 0.44173 -0.04821 0.08241  -0.01737 396 ARG A NH1 
2929 N NH2 . ARG A 430 ? 0.43766 0.38783 0.45135 -0.05816 0.08519  -0.01940 396 ARG A NH2 
2930 N N   . ILE A 431 ? 0.35085 0.29562 0.33131 -0.02079 0.03737  0.00719  397 ILE A N   
2931 C CA  . ILE A 431 ? 0.34803 0.29576 0.33319 -0.01746 0.03270  0.00533  397 ILE A CA  
2932 C C   . ILE A 431 ? 0.34610 0.31049 0.34309 -0.01368 0.03013  -0.00011 397 ILE A C   
2933 O O   . ILE A 431 ? 0.35457 0.32426 0.35397 -0.00986 0.02578  -0.00173 397 ILE A O   
2934 C CB  . ILE A 431 ? 0.36433 0.30711 0.34165 -0.01347 0.02733  0.01079  397 ILE A CB  
2935 C CG1 . ILE A 431 ? 0.35408 0.30500 0.32898 -0.00980 0.02456  0.01400  397 ILE A CG1 
2936 C CG2 . ILE A 431 ? 0.33370 0.25826 0.29911 -0.01746 0.02821  0.01621  397 ILE A CG2 
2937 C CD1 . ILE A 431 ? 0.33338 0.28228 0.30288 -0.00632 0.01947  0.01887  397 ILE A CD1 
2938 N N   . GLY A 432 ? 0.38245 0.35508 0.38664 -0.01463 0.03256  -0.00311 398 GLY A N   
2939 C CA  . GLY A 432 ? 0.34855 0.33615 0.36360 -0.01140 0.02901  -0.00784 398 GLY A CA  
2940 C C   . GLY A 432 ? 0.41000 0.40428 0.43530 -0.01334 0.03257  -0.01163 398 GLY A C   
2941 O O   . GLY A 432 ? 0.34098 0.32882 0.36411 -0.01701 0.03868  -0.01076 398 GLY A O   
2942 N N   . VAL A 433 ? 0.40050 0.40812 0.43713 -0.01082 0.02852  -0.01623 399 VAL A N   
2943 C CA  . VAL A 433 ? 0.42393 0.44121 0.47484 -0.01145 0.03027  -0.02107 399 VAL A CA  
2944 C C   . VAL A 433 ? 0.41015 0.43631 0.46353 -0.00519 0.02362  -0.01941 399 VAL A C   
2945 O O   . VAL A 433 ? 0.41140 0.44131 0.46010 -0.00173 0.01670  -0.01770 399 VAL A O   
2946 C CB  . VAL A 433 ? 0.44937 0.47454 0.51354 -0.01467 0.03004  -0.02849 399 VAL A CB  
2947 C CG1 . VAL A 433 ? 0.55562 0.59458 0.63765 -0.01386 0.02950  -0.03383 399 VAL A CG1 
2948 C CG2 . VAL A 433 ? 0.50223 0.51662 0.56403 -0.02194 0.03749  -0.02980 399 VAL A CG2 
2949 N N   . GLU A 434 ? 0.34105 0.36977 0.40123 -0.00395 0.02592  -0.02006 400 GLU A N   
2950 C CA  . GLU A 434 ? 0.37218 0.40622 0.43411 0.00212  0.01951  -0.01774 400 GLU A CA  
2951 C C   . GLU A 434 ? 0.46320 0.51163 0.54244 0.00470  0.01376  -0.02330 400 GLU A C   
2952 O O   . GLU A 434 ? 0.42099 0.47607 0.51607 0.00253  0.01794  -0.02956 400 GLU A O   
2953 C CB  . GLU A 434 ? 0.44329 0.47105 0.50359 0.00274  0.02462  -0.01598 400 GLU A CB  
2954 C CG  . GLU A 434 ? 0.51180 0.54485 0.57920 0.00891  0.01901  -0.01553 400 GLU A CG  
2955 C CD  . GLU A 434 ? 0.61464 0.63791 0.67519 0.00969  0.02340  -0.01276 400 GLU A CD  
2956 O OE1 . GLU A 434 ? 0.64032 0.65320 0.68937 0.00501  0.03045  -0.01094 400 GLU A OE1 
2957 O OE2 . GLU A 434 ? 0.55370 0.57863 0.61955 0.01493  0.01920  -0.01231 400 GLU A OE2 
2958 N N   . VAL A 435 ? 0.35337 0.40689 0.42941 0.00878  0.00405  -0.02108 401 VAL A N   
2959 C CA  . VAL A 435 ? 0.34294 0.40941 0.43379 0.01176  -0.00368 -0.02533 401 VAL A CA  
2960 C C   . VAL A 435 ? 0.32632 0.39574 0.42870 0.01650  -0.00498 -0.02554 401 VAL A C   
2961 O O   . VAL A 435 ? 0.38231 0.46213 0.50480 0.01730  -0.00506 -0.03186 401 VAL A O   
2962 C CB  . VAL A 435 ? 0.35756 0.42686 0.43832 0.01414  -0.01393 -0.02230 401 VAL A CB  
2963 C CG1 . VAL A 435 ? 0.36150 0.44233 0.45544 0.01792  -0.02382 -0.02504 401 VAL A CG1 
2964 C CG2 . VAL A 435 ? 0.33364 0.40272 0.40790 0.00992  -0.01273 -0.02496 401 VAL A CG2 
2965 N N   . GLY A 436 ? 0.37526 0.43579 0.46625 0.01972  -0.00607 -0.01911 402 GLY A N   
2966 C CA  . GLY A 436 ? 0.42232 0.48317 0.52265 0.02500  -0.00801 -0.01902 402 GLY A CA  
2967 C C   . GLY A 436 ? 0.40517 0.46397 0.49752 0.03033  -0.01957 -0.01267 402 GLY A C   
2968 O O   . GLY A 436 ? 0.44693 0.51418 0.54506 0.03286  -0.02937 -0.01345 402 GLY A O   
2969 N N   . ALA A 437 ? 0.42221 0.46912 0.50008 0.03138  -0.01895 -0.00613 403 ALA A N   
2970 C CA  . ALA A 437 ? 0.47754 0.52023 0.54528 0.03518  -0.02934 0.00085  403 ALA A CA  
2971 C C   . ALA A 437 ? 0.52379 0.57014 0.60744 0.04209  -0.03706 -0.00077 403 ALA A C   
2972 O O   . ALA A 437 ? 0.39951 0.44785 0.49960 0.04458  -0.03204 -0.00627 403 ALA A O   
2973 C CB  . ALA A 437 ? 0.41783 0.44665 0.46745 0.03374  -0.02621 0.00785  403 ALA A CB  
2974 N N   . ALA A 438 ? 0.43105 0.47815 0.50963 0.04517  -0.04952 0.00393  404 ALA A N   
2975 C CA  . ALA A 438 ? 0.49437 0.54317 0.58654 0.05255  -0.05954 0.00387  404 ALA A CA  
2976 C C   . ALA A 438 ? 0.49549 0.52969 0.57383 0.05570  -0.06579 0.01257  404 ALA A C   
2977 O O   . ALA A 438 ? 0.51418 0.54610 0.60432 0.06260  -0.07272 0.01258  404 ALA A O   
2978 C CB  . ALA A 438 ? 0.49818 0.55849 0.59686 0.05409  -0.07146 0.00253  404 ALA A CB  
2979 N N   . GLU A 439 ? 0.51227 0.53652 0.56717 0.05082  -0.06352 0.01965  405 GLU A N   
2980 C CA  . GLU A 439 ? 0.48616 0.49595 0.52608 0.05217  -0.06929 0.02842  405 GLU A CA  
2981 C C   . GLU A 439 ? 0.53943 0.54053 0.56045 0.04569  -0.06049 0.03263  405 GLU A C   
2982 O O   . GLU A 439 ? 0.51196 0.51874 0.52592 0.04032  -0.05490 0.03152  405 GLU A O   
2983 C CB  . GLU A 439 ? 0.54759 0.55691 0.57641 0.05282  -0.08300 0.03498  405 GLU A CB  
2984 C CG  . GLU A 439 ? 0.68119 0.67451 0.69036 0.05205  -0.08876 0.04527  405 GLU A CG  
2985 C CD  . GLU A 439 ? 0.78675 0.77894 0.78363 0.05202  -0.10252 0.05187  405 GLU A CD  
2986 O OE1 . GLU A 439 ? 0.71051 0.71384 0.71822 0.05475  -0.10952 0.04787  405 GLU A OE1 
2987 O OE2 . GLU A 439 ? 0.69987 0.67993 0.67567 0.04859  -0.10639 0.06102  405 GLU A OE2 
2988 N N   . TRP A 440 ? 0.42623 0.41359 0.44019 0.04638  -0.05966 0.03703  406 TRP A N   
2989 C CA  . TRP A 440 ? 0.50922 0.48805 0.50561 0.04020  -0.05300 0.04161  406 TRP A CA  
2990 C C   . TRP A 440 ? 0.54327 0.51419 0.52070 0.03769  -0.06103 0.05127  406 TRP A C   
2991 O O   . TRP A 440 ? 0.60738 0.56697 0.58205 0.04080  -0.06808 0.05601  406 TRP A O   
2992 C CB  . TRP A 440 ? 0.42175 0.39010 0.42104 0.04104  -0.04615 0.03971  406 TRP A CB  
2993 C CG  . TRP A 440 ? 0.47092 0.43339 0.45525 0.03423  -0.03856 0.04261  406 TRP A CG  
2994 C CD1 . TRP A 440 ? 0.51489 0.47032 0.48130 0.02949  -0.04091 0.05050  406 TRP A CD1 
2995 C CD2 . TRP A 440 ? 0.40296 0.36635 0.38916 0.03102  -0.02792 0.03777  406 TRP A CD2 
2996 N NE1 . TRP A 440 ? 0.43886 0.39198 0.39793 0.02415  -0.03293 0.05048  406 TRP A NE1 
2997 C CE2 . TRP A 440 ? 0.43127 0.38827 0.40118 0.02510  -0.02540 0.04312  406 TRP A CE2 
2998 C CE3 . TRP A 440 ? 0.46442 0.43321 0.46407 0.03204  -0.02038 0.02961  406 TRP A CE3 
2999 C CZ2 . TRP A 440 ? 0.35247 0.30771 0.31885 0.02089  -0.01700 0.04094  406 TRP A CZ2 
3000 C CZ3 . TRP A 440 ? 0.38283 0.34862 0.37683 0.02711  -0.01124 0.02781  406 TRP A CZ3 
3001 C CH2 . TRP A 440 ? 0.46747 0.42622 0.44480 0.02194  -0.01028 0.03364  406 TRP A CH2 
3002 N N   . SER A 441 ? 0.41637 0.39275 0.38079 0.03188  -0.05965 0.05392  407 SER A N   
3003 C CA  . SER A 441 ? 0.54307 0.51399 0.48832 0.02785  -0.06566 0.06253  407 SER A CA  
3004 C C   . SER A 441 ? 0.45831 0.42507 0.39037 0.02101  -0.05819 0.06610  407 SER A C   
3005 O O   . SER A 441 ? 0.57858 0.55283 0.51313 0.01832  -0.04993 0.06191  407 SER A O   
3006 C CB  . SER A 441 ? 0.44237 0.42419 0.38280 0.02625  -0.07033 0.06209  407 SER A CB  
3007 O OG  . SER A 441 ? 0.71918 0.69668 0.63879 0.02043  -0.07317 0.06978  407 SER A OG  
3008 N N   . MET A 442 ? 0.52282 0.47730 0.44148 0.01814  -0.06166 0.07393  408 MET A N   
3009 C CA  . MET A 442 ? 0.53078 0.48219 0.43712 0.01090  -0.05580 0.07787  408 MET A CA  
3010 C C   . MET A 442 ? 0.59427 0.55392 0.48741 0.00464  -0.05538 0.08104  408 MET A C   
3011 O O   . MET A 442 ? 0.73633 0.69844 0.62308 -0.00125 -0.04924 0.08243  408 MET A O   
3012 C CB  . MET A 442 ? 0.58680 0.52098 0.48458 0.00943  -0.05923 0.08457  408 MET A CB  
3013 C CG  . MET A 442 ? 0.62700 0.55251 0.53361 0.01218  -0.05490 0.08091  408 MET A CG  
3014 S SD  . MET A 442 ? 0.64556 0.58287 0.56370 0.01219  -0.04397 0.07201  408 MET A SD  
3015 C CE  . MET A 442 ? 0.53337 0.46987 0.43809 0.00305  -0.03879 0.07653  408 MET A CE  
3016 N N   . SER A 443 ? 0.57084 0.53542 0.46014 0.00562  -0.06163 0.08166  409 SER A N   
3017 C CA  . SER A 443 ? 0.70420 0.67475 0.57798 -0.00099 -0.06133 0.08490  409 SER A CA  
3018 C C   . SER A 443 ? 0.52404 0.50777 0.40131 0.00071  -0.06232 0.07893  409 SER A C   
3019 O O   . SER A 443 ? 0.48676 0.47141 0.37296 0.00650  -0.06884 0.07615  409 SER A O   
3020 C CB  . SER A 443 ? 0.69456 0.65275 0.55067 -0.00448 -0.06964 0.09464  409 SER A CB  
3021 O OG  . SER A 443 ? 0.83799 0.79633 0.69142 -0.00115 -0.07939 0.09546  409 SER A OG  
3022 N N   . PRO A 444 ? 0.56754 0.56189 0.43863 -0.00429 -0.05610 0.07639  410 PRO A N   
3023 C CA  . PRO A 444 ? 0.63091 0.63674 0.50342 -0.00339 -0.05693 0.07019  410 PRO A CA  
3024 C C   . PRO A 444 ? 0.61336 0.61679 0.47070 -0.00524 -0.06638 0.07449  410 PRO A C   
3025 O O   . PRO A 444 ? 0.59648 0.60761 0.45575 -0.00361 -0.06967 0.06932  410 PRO A O   
3026 C CB  . PRO A 444 ? 0.62849 0.64453 0.49815 -0.00827 -0.04693 0.06641  410 PRO A CB  
3027 C CG  . PRO A 444 ? 0.62756 0.63765 0.48593 -0.01420 -0.04417 0.07375  410 PRO A CG  
3028 C CD  . PRO A 444 ? 0.63884 0.63541 0.50163 -0.01115 -0.04835 0.07873  410 PRO A CD  
3029 N N   . TYR A 445 ? 0.62774 0.61979 0.46912 -0.00908 -0.07133 0.08395  411 TYR A N   
3030 C CA  . TYR A 445 ? 0.66789 0.65599 0.49031 -0.01243 -0.08034 0.08936  411 TYR A CA  
3031 C C   . TYR A 445 ? 0.83005 0.80861 0.65642 -0.00587 -0.09400 0.09290  411 TYR A C   
3032 O O   . TYR A 445 ? 0.79713 0.77531 0.61242 -0.00657 -0.10327 0.09488  411 TYR A O   
3033 C CB  . TYR A 445 ? 0.62807 0.60806 0.42850 -0.02151 -0.07853 0.09842  411 TYR A CB  
3034 C CG  . TYR A 445 ? 0.54462 0.53433 0.34494 -0.02744 -0.06513 0.09515  411 TYR A CG  
3035 C CD1 . TYR A 445 ? 0.63060 0.63459 0.42700 -0.03104 -0.05834 0.08854  411 TYR A CD1 
3036 C CD2 . TYR A 445 ? 0.64394 0.62882 0.44918 -0.02916 -0.05959 0.09803  411 TYR A CD2 
3037 C CE1 . TYR A 445 ? 0.62936 0.64322 0.42850 -0.03546 -0.04648 0.08494  411 TYR A CE1 
3038 C CE2 . TYR A 445 ? 0.68341 0.67841 0.49083 -0.03411 -0.04842 0.09488  411 TYR A CE2 
3039 C CZ  . TYR A 445 ? 0.67811 0.68790 0.48336 -0.03686 -0.04197 0.08837  411 TYR A CZ  
3040 O OH  . TYR A 445 ? 0.80299 0.82363 0.61292 -0.04086 -0.03131 0.08476  411 TYR A OH  
3041 N N   . ASP A 446 ? 0.79603 0.76704 0.63792 0.00052  -0.09567 0.09336  412 ASP A N   
3042 C CA  . ASP A 446 ? 0.87426 0.83712 0.72375 0.00797  -0.10844 0.09574  412 ASP A CA  
3043 C C   . ASP A 446 ? 0.74225 0.71820 0.60793 0.01369  -0.11210 0.08706  412 ASP A C   
3044 O O   . ASP A 446 ? 0.64248 0.63010 0.52377 0.01526  -0.10322 0.07811  412 ASP A O   
3045 C CB  . ASP A 446 ? 0.94108 0.89373 0.80480 0.01343  -0.10729 0.09647  412 ASP A CB  
3046 C CG  . ASP A 446 ? 0.94106 0.87699 0.78816 0.00836  -0.10796 0.10635  412 ASP A CG  
3047 O OD1 . ASP A 446 ? 1.02999 0.95946 0.85493 0.00206  -0.11325 0.11433  412 ASP A OD1 
3048 O OD2 . ASP A 446 ? 0.98615 0.91489 0.84132 0.00994  -0.10301 0.10602  412 ASP A OD2 
3049 N N   . ALA A 447 ? 0.85025 0.82378 0.71169 0.01630  -0.12576 0.08996  413 ALA A N   
3050 C CA  . ALA A 447 ? 0.86359 0.84937 0.74252 0.02191  -0.13106 0.08186  413 ALA A CA  
3051 C C   . ALA A 447 ? 0.83446 0.82110 0.74187 0.03105  -0.13090 0.07684  413 ALA A C   
3052 O O   . ALA A 447 ? 0.83078 0.80487 0.74162 0.03517  -0.13472 0.08186  413 ALA A O   
3053 C CB  . ALA A 447 ? 0.83625 0.81878 0.70288 0.02225  -0.14732 0.08682  413 ALA A CB  
3054 N N   . LYS A 448 ? 0.73815 0.73927 0.66578 0.03375  -0.12583 0.06646  414 LYS A N   
3055 C CA  . LYS A 448 ? 0.66608 0.67026 0.62109 0.04113  -0.12310 0.06022  414 LYS A CA  
3056 C C   . LYS A 448 ? 0.76928 0.77562 0.73968 0.04887  -0.13757 0.05938  414 LYS A C   
3057 O O   . LYS A 448 ? 0.76577 0.78074 0.73550 0.04844  -0.14612 0.05739  414 LYS A O   
3058 C CB  . LYS A 448 ? 0.73273 0.75058 0.70209 0.03959  -0.11077 0.04985  414 LYS A CB  
3059 C CG  . LYS A 448 ? 0.70716 0.72183 0.66742 0.03418  -0.09673 0.05026  414 LYS A CG  
3060 C CD  . LYS A 448 ? 0.68415 0.70882 0.66041 0.03384  -0.08549 0.04083  414 LYS A CD  
3061 C CE  . LYS A 448 ? 0.54218 0.56128 0.51266 0.03029  -0.07344 0.04200  414 LYS A CE  
3062 N NZ  . LYS A 448 ? 0.60225 0.61918 0.55121 0.02394  -0.07113 0.04704  414 LYS A NZ  
3063 N N   . LYS A 449 ? 0.72632 0.72483 0.71105 0.05607  -0.14064 0.06049  415 LYS A N   
3064 C CA  . LYS A 449 ? 0.78927 0.79009 0.79268 0.06485  -0.15456 0.05924  415 LYS A CA  
3065 C C   . LYS A 449 ? 0.76086 0.78039 0.79423 0.06877  -0.15099 0.04707  415 LYS A C   
3066 O O   . LYS A 449 ? 0.80694 0.83353 0.85773 0.07513  -0.16307 0.04450  415 LYS A O   
3067 C CB  . LYS A 449 ? 0.89581 0.88125 0.90567 0.07181  -0.15858 0.06373  415 LYS A CB  
3068 C CG  . LYS A 449 ? 0.94185 0.90670 0.92285 0.06777  -0.16338 0.07641  415 LYS A CG  
3069 C CD  . LYS A 449 ? 1.05229 1.01515 1.00958 0.06286  -0.17557 0.08409  415 LYS A CD  
3070 C CE  . LYS A 449 ? 1.11495 1.05588 1.05260 0.06329  -0.18816 0.09696  415 LYS A CE  
3071 N NZ  . LYS A 449 ? 1.10164 1.03854 1.05453 0.07369  -0.20614 0.09868  415 LYS A NZ  
3072 N N   . THR A 450 ? 0.82109 0.84854 0.86121 0.06489  -0.13518 0.03974  416 THR A N   
3073 C CA  . THR A 450 ? 0.72213 0.76676 0.78810 0.06640  -0.12996 0.02834  416 THR A CA  
3074 C C   . THR A 450 ? 0.73346 0.78722 0.78960 0.05829  -0.12293 0.02448  416 THR A C   
3075 O O   . THR A 450 ? 0.82851 0.87593 0.85985 0.05209  -0.12000 0.02971  416 THR A O   
3076 C CB  . THR A 450 ? 0.70083 0.74549 0.78533 0.06905  -0.11687 0.02220  416 THR A CB  
3077 O OG1 . THR A 450 ? 1.00564 1.04422 1.07408 0.06218  -0.10293 0.02344  416 THR A OG1 
3078 C CG2 . THR A 450 ? 0.76366 0.79667 0.85536 0.07690  -0.12241 0.02578  416 THR A CG2 
3079 N N   . VAL A 451 ? 0.60363 0.67258 0.68054 0.05828  -0.11999 0.01473  417 VAL A N   
3080 C CA  . VAL A 451 ? 0.58785 0.66520 0.65873 0.05117  -0.11375 0.00970  417 VAL A CA  
3081 C C   . VAL A 451 ? 0.55702 0.64270 0.64851 0.04990  -0.10040 0.00032  417 VAL A C   
3082 O O   . VAL A 451 ? 0.56711 0.65828 0.68257 0.05470  -0.09936 -0.00456 417 VAL A O   
3083 C CB  . VAL A 451 ? 0.60317 0.69018 0.67386 0.05043  -0.12703 0.00772  417 VAL A CB  
3084 C CG1 . VAL A 451 ? 0.55385 0.65549 0.65628 0.05501  -0.13200 -0.00072 417 VAL A CG1 
3085 C CG2 . VAL A 451 ? 0.64634 0.73714 0.70230 0.04255  -0.12130 0.00443  417 VAL A CG2 
3086 N N   . VAL A 452 ? 0.52197 0.60789 0.60369 0.04327  -0.08980 -0.00217 418 VAL A N   
3087 C CA  . VAL A 452 ? 0.45099 0.54380 0.54885 0.04041  -0.07788 -0.01066 418 VAL A CA  
3088 C C   . VAL A 452 ? 0.53297 0.64040 0.64620 0.03903  -0.08347 -0.01851 418 VAL A C   
3089 O O   . VAL A 452 ? 0.44120 0.55100 0.54225 0.03525  -0.08818 -0.01896 418 VAL A O   
3090 C CB  . VAL A 452 ? 0.48730 0.57318 0.56883 0.03429  -0.06592 -0.00978 418 VAL A CB  
3091 C CG1 . VAL A 452 ? 0.44500 0.53600 0.54154 0.03079  -0.05467 -0.01778 418 VAL A CG1 
3092 C CG2 . VAL A 452 ? 0.42191 0.49426 0.48895 0.03517  -0.06128 -0.00213 418 VAL A CG2 
3093 N N   . ARG A 453 ? 0.45613 0.57379 0.59645 0.04169  -0.08263 -0.02531 419 ARG A N   
3094 C CA  . ARG A 453 ? 0.57771 0.71073 0.73598 0.04090  -0.09005 -0.03271 419 ARG A CA  
3095 C C   . ARG A 453 ? 0.52674 0.66389 0.68434 0.03278  -0.08114 -0.03935 419 ARG A C   
3096 O O   . ARG A 453 ? 0.46699 0.59666 0.61726 0.02867  -0.06790 -0.03949 419 ARG A O   
3097 C CB  . ARG A 453 ? 0.53019 0.67450 0.72038 0.04624  -0.09129 -0.03856 419 ARG A CB  
3098 C CG  . ARG A 453 ? 0.68146 0.82259 0.87541 0.05539  -0.10364 -0.03290 419 ARG A CG  
3099 C CD  . ARG A 453 ? 0.91770 1.07488 1.13814 0.06039  -0.11723 -0.03811 419 ARG A CD  
3100 N NE  . ARG A 453 ? 1.09460 1.24909 1.32685 0.07035  -0.12587 -0.03473 419 ARG A NE  
3101 C CZ  . ARG A 453 ? 1.14810 1.30775 1.40604 0.07545  -0.11920 -0.04026 419 ARG A CZ  
3102 N NH1 . ARG A 453 ? 1.09179 1.25961 1.36521 0.07080  -0.10324 -0.04899 419 ARG A NH1 
3103 N NH2 . ARG A 453 ? 1.10013 1.25583 1.36786 0.08526  -0.12854 -0.03708 419 ARG A NH2 
3104 N N   . ALA A 454 ? 0.48088 0.62934 0.64623 0.03043  -0.08945 -0.04489 420 ALA A N   
3105 C CA  . ALA A 454 ? 0.43347 0.58387 0.59459 0.02258  -0.08352 -0.05082 420 ALA A CA  
3106 C C   . ALA A 454 ? 0.44763 0.60136 0.62662 0.01828  -0.06950 -0.05765 420 ALA A C   
3107 O O   . ALA A 454 ? 0.43118 0.57822 0.60041 0.01223  -0.05976 -0.05934 420 ALA A O   
3108 C CB  . ALA A 454 ? 0.49448 0.65632 0.66065 0.02081  -0.09661 -0.05580 420 ALA A CB  
3109 N N   . GLU A 455 ? 0.37701 0.54077 0.58221 0.02109  -0.06820 -0.06183 421 GLU A N   
3110 C CA  . GLU A 455 ? 0.48748 0.65465 0.70886 0.01579  -0.05400 -0.06848 421 GLU A CA  
3111 C C   . GLU A 455 ? 0.41413 0.56521 0.61839 0.01373  -0.04020 -0.06365 421 GLU A C   
3112 O O   . GLU A 455 ? 0.41098 0.55786 0.61356 0.00666  -0.02899 -0.06676 421 GLU A O   
3113 C CB  . GLU A 455 ? 0.45051 0.63195 0.70324 0.01968  -0.05402 -0.07404 421 GLU A CB  
3114 C CG  . GLU A 455 ? 0.70332 0.90112 0.97527 0.02399  -0.07016 -0.07766 421 GLU A CG  
3115 C CD  . GLU A 455 ? 0.87367 1.06733 1.13867 0.03380  -0.08362 -0.06993 421 GLU A CD  
3116 O OE1 . GLU A 455 ? 1.03148 1.22398 1.30704 0.04027  -0.08114 -0.06852 421 GLU A OE1 
3117 O OE2 . GLU A 455 ? 0.72434 0.91486 0.97221 0.03463  -0.09645 -0.06535 421 GLU A OE2 
3118 N N   . ARG A 456 ? 0.35128 0.49240 0.54222 0.01948  -0.04151 -0.05579 422 ARG A N   
3119 C CA  . ARG A 456 ? 0.38477 0.51084 0.55910 0.01757  -0.02982 -0.05096 422 ARG A CA  
3120 C C   . ARG A 456 ? 0.48854 0.60496 0.64088 0.01249  -0.02726 -0.04836 422 ARG A C   
3121 O O   . ARG A 456 ? 0.39694 0.50468 0.54258 0.00767  -0.01629 -0.04836 422 ARG A O   
3122 C CB  . ARG A 456 ? 0.41382 0.53152 0.57870 0.02445  -0.03315 -0.04334 422 ARG A CB  
3123 C CG  . ARG A 456 ? 0.43402 0.55920 0.62124 0.03043  -0.03461 -0.04636 422 ARG A CG  
3124 C CD  . ARG A 456 ? 0.58706 0.69968 0.76565 0.03362  -0.02838 -0.04143 422 ARG A CD  
3125 N NE  . ARG A 456 ? 0.71005 0.81450 0.88123 0.02731  -0.01340 -0.04249 422 ARG A NE  
3126 C CZ  . ARG A 456 ? 0.70753 0.81291 0.89101 0.02618  -0.00258 -0.04741 422 ARG A CZ  
3127 N NH1 . ARG A 456 ? 0.65943 0.77491 0.86615 0.03146  -0.00402 -0.05278 422 ARG A NH1 
3128 N NH2 . ARG A 456 ? 0.55952 0.65530 0.73155 0.01957  0.00992  -0.04712 422 ARG A NH2 
3129 N N   . ILE A 457 ? 0.41816 0.53572 0.55901 0.01350  -0.03742 -0.04640 423 ILE A N   
3130 C CA  . ILE A 457 ? 0.35251 0.46271 0.47506 0.00915  -0.03505 -0.04569 423 ILE A CA  
3131 C C   . ILE A 457 ? 0.39457 0.50849 0.52726 0.00247  -0.02975 -0.05380 423 ILE A C   
3132 O O   . ILE A 457 ? 0.37989 0.48428 0.50325 -0.00180 -0.02158 -0.05391 423 ILE A O   
3133 C CB  . ILE A 457 ? 0.46797 0.57954 0.57593 0.01123  -0.04662 -0.04281 423 ILE A CB  
3134 C CG1 . ILE A 457 ? 0.46189 0.56800 0.55889 0.01686  -0.05153 -0.03404 423 ILE A CG1 
3135 C CG2 . ILE A 457 ? 0.40039 0.50536 0.49078 0.00717  -0.04332 -0.04344 423 ILE A CG2 
3136 C CD1 . ILE A 457 ? 0.50695 0.61411 0.58897 0.01831  -0.06328 -0.03048 423 ILE A CD1 
3137 N N   . GLU A 458 ? 0.37701 0.50447 0.52956 0.00134  -0.03481 -0.06066 424 GLU A N   
3138 C CA  . GLU A 458 ? 0.40285 0.53414 0.56612 -0.00599 -0.03015 -0.06873 424 GLU A CA  
3139 C C   . GLU A 458 ? 0.37310 0.49862 0.54312 -0.01052 -0.01608 -0.06992 424 GLU A C   
3140 O O   . GLU A 458 ? 0.38525 0.50295 0.55030 -0.01696 -0.00895 -0.07224 424 GLU A O   
3141 C CB  . GLU A 458 ? 0.39759 0.54635 0.58286 -0.00634 -0.03920 -0.07585 424 GLU A CB  
3142 C CG  . GLU A 458 ? 0.38247 0.53702 0.58376 -0.01469 -0.03347 -0.08476 424 GLU A CG  
3143 C CD  . GLU A 458 ? 0.48312 0.65735 0.71230 -0.01472 -0.04057 -0.09185 424 GLU A CD  
3144 O OE1 . GLU A 458 ? 0.45082 0.63342 0.68680 -0.00734 -0.05067 -0.08950 424 GLU A OE1 
3145 O OE2 . GLU A 458 ? 0.50927 0.69039 0.75415 -0.02224 -0.03637 -0.09970 424 GLU A OE2 
3146 N N   . LYS A 459 ? 0.40895 0.53697 0.58911 -0.00745 -0.01190 -0.06838 425 LYS A N   
3147 C CA  . LYS A 459 ? 0.37198 0.49438 0.55669 -0.01255 0.00198  -0.06970 425 LYS A CA  
3148 C C   . LYS A 459 ? 0.34977 0.45318 0.51052 -0.01433 0.00907  -0.06308 425 LYS A C   
3149 O O   . LYS A 459 ? 0.34104 0.43608 0.49868 -0.02130 0.01827  -0.06444 425 LYS A O   
3150 C CB  . LYS A 459 ? 0.37278 0.50193 0.57254 -0.00833 0.00501  -0.07023 425 LYS A CB  
3151 C CG  . LYS A 459 ? 0.66855 0.79713 0.87866 -0.01504 0.01946  -0.07459 425 LYS A CG  
3152 C CD  . LYS A 459 ? 0.72422 0.85105 0.93719 -0.01056 0.02519  -0.07270 425 LYS A CD  
3153 C CE  . LYS A 459 ? 0.78642 0.90969 1.00349 -0.01850 0.04111  -0.07639 425 LYS A CE  
3154 N NZ  . LYS A 459 ? 0.79155 0.89747 0.98734 -0.01820 0.04849  -0.06974 425 LYS A NZ  
3155 N N   . ALA A 460 ? 0.32597 0.42215 0.46975 -0.00842 0.00445  -0.05568 426 ALA A N   
3156 C CA  . ALA A 460 ? 0.37627 0.45604 0.49923 -0.00954 0.01010  -0.04943 426 ALA A CA  
3157 C C   . ALA A 460 ? 0.36421 0.43754 0.47792 -0.01372 0.01021  -0.05098 426 ALA A C   
3158 O O   . ALA A 460 ? 0.35273 0.41358 0.45785 -0.01786 0.01759  -0.04930 426 ALA A O   
3159 C CB  . ALA A 460 ? 0.31028 0.38576 0.41912 -0.00285 0.00463  -0.04180 426 ALA A CB  
3160 N N   . VAL A 461 ? 0.32361 0.40430 0.43821 -0.01266 0.00172  -0.05429 427 VAL A N   
3161 C CA  . VAL A 461 ? 0.34651 0.42117 0.45354 -0.01638 0.00191  -0.05731 427 VAL A CA  
3162 C C   . VAL A 461 ? 0.36312 0.43537 0.48087 -0.02421 0.00900  -0.06308 427 VAL A C   
3163 O O   . VAL A 461 ? 0.40473 0.46373 0.51383 -0.02799 0.01444  -0.06247 427 VAL A O   
3164 C CB  . VAL A 461 ? 0.37036 0.45401 0.47592 -0.01441 -0.00844 -0.06086 427 VAL A CB  
3165 C CG1 . VAL A 461 ? 0.27517 0.35289 0.37506 -0.01859 -0.00761 -0.06599 427 VAL A CG1 
3166 C CG2 . VAL A 461 ? 0.34958 0.43279 0.44056 -0.00810 -0.01425 -0.05428 427 VAL A CG2 
3167 N N   . LYS A 462 ? 0.34974 0.43464 0.48710 -0.02693 0.00887  -0.06872 428 LYS A N   
3168 C CA  . LYS A 462 ? 0.48389 0.56753 0.63251 -0.03569 0.01656  -0.07431 428 LYS A CA  
3169 C C   . LYS A 462 ? 0.45612 0.52573 0.59714 -0.03929 0.02796  -0.06970 428 LYS A C   
3170 O O   . LYS A 462 ? 0.44230 0.50063 0.57961 -0.04650 0.03430  -0.07083 428 LYS A O   
3171 C CB  . LYS A 462 ? 0.34414 0.44640 0.51764 -0.03757 0.01497  -0.08115 428 LYS A CB  
3172 C CG  . LYS A 462 ? 0.47077 0.58600 0.65397 -0.03768 0.00424  -0.08769 428 LYS A CG  
3173 C CD  . LYS A 462 ? 0.42167 0.55572 0.63257 -0.04039 0.00349  -0.09487 428 LYS A CD  
3174 C CE  . LYS A 462 ? 0.66206 0.80908 0.88311 -0.04163 -0.00798 -0.10182 428 LYS A CE  
3175 N NZ  . LYS A 462 ? 0.64604 0.81308 0.89700 -0.04436 -0.00920 -0.10927 428 LYS A NZ  
3176 N N   . LYS A 463 ? 0.42133 0.49021 0.55881 -0.03473 0.03031  -0.06437 429 LYS A N   
3177 C CA  . LYS A 463 ? 0.37868 0.43388 0.50667 -0.03837 0.04059  -0.05987 429 LYS A CA  
3178 C C   . LYS A 463 ? 0.40440 0.44083 0.51177 -0.03927 0.04137  -0.05437 429 LYS A C   
3179 O O   . LYS A 463 ? 0.47105 0.49391 0.57140 -0.04574 0.04897  -0.05267 429 LYS A O   
3180 C CB  . LYS A 463 ? 0.41911 0.47669 0.54565 -0.03248 0.04141  -0.05558 429 LYS A CB  
3181 C CG  . LYS A 463 ? 0.57160 0.61467 0.68538 -0.03579 0.05110  -0.05064 429 LYS A CG  
3182 C CD  . LYS A 463 ? 0.62883 0.67879 0.75053 -0.03276 0.05472  -0.05119 429 LYS A CD  
3183 C CE  . LYS A 463 ? 0.80419 0.83854 0.90787 -0.03410 0.06155  -0.04498 429 LYS A CE  
3184 N NZ  . LYS A 463 ? 0.86382 0.90030 0.96543 -0.02651 0.05850  -0.04187 429 LYS A NZ  
3185 N N   . LEU A 464 ? 0.39915 0.43447 0.49676 -0.03299 0.03350  -0.05161 430 LEU A N   
3186 C CA  . LEU A 464 ? 0.43733 0.45660 0.51844 -0.03282 0.03380  -0.04725 430 LEU A CA  
3187 C C   . LEU A 464 ? 0.52230 0.53668 0.60543 -0.03748 0.03322  -0.05265 430 LEU A C   
3188 O O   . LEU A 464 ? 0.53624 0.53483 0.61193 -0.04196 0.03772  -0.05087 430 LEU A O   
3189 C CB  . LEU A 464 ? 0.36945 0.39012 0.44005 -0.02472 0.02699  -0.04272 430 LEU A CB  
3190 C CG  . LEU A 464 ? 0.40472 0.41182 0.46180 -0.02346 0.02649  -0.03956 430 LEU A CG  
3191 C CD1 . LEU A 464 ? 0.36529 0.35651 0.41281 -0.02623 0.03247  -0.03342 430 LEU A CD1 
3192 C CD2 . LEU A 464 ? 0.38495 0.39662 0.43408 -0.01636 0.02050  -0.03657 430 LEU A CD2 
3193 N N   . MET A 465 ? 0.48987 0.51650 0.58232 -0.03673 0.02717  -0.05926 431 MET A N   
3194 C CA  . MET A 465 ? 0.47048 0.49188 0.56216 -0.03967 0.02503  -0.06473 431 MET A CA  
3195 C C   . MET A 465 ? 0.58973 0.60766 0.69159 -0.04935 0.03037  -0.07010 431 MET A C   
3196 O O   . MET A 465 ? 0.62696 0.63249 0.72464 -0.05318 0.03123  -0.07259 431 MET A O   
3197 C CB  . MET A 465 ? 0.43815 0.47325 0.53323 -0.03580 0.01612  -0.06994 431 MET A CB  
3198 C CG  . MET A 465 ? 0.50669 0.54481 0.59019 -0.02750 0.01091  -0.06509 431 MET A CG  
3199 S SD  . MET A 465 ? 0.74350 0.76670 0.81054 -0.02401 0.01173  -0.06245 431 MET A SD  
3200 C CE  . MET A 465 ? 0.49690 0.51985 0.56678 -0.02736 0.00855  -0.07309 431 MET A CE  
3201 N N   . ASP A 466 ? 0.56136 0.58998 0.67730 -0.05359 0.03415  -0.07240 432 ASP A N   
3202 C CA  . ASP A 466 ? 0.69033 0.71658 0.81655 -0.06409 0.04050  -0.07748 432 ASP A CA  
3203 C C   . ASP A 466 ? 0.78911 0.79322 0.90192 -0.06960 0.04868  -0.07196 432 ASP A C   
3204 O O   . ASP A 466 ? 0.70229 0.69762 0.80267 -0.06625 0.05140  -0.06428 432 ASP A O   
3205 C CB  . ASP A 466 ? 0.66071 0.70446 0.80612 -0.06714 0.04406  -0.08118 432 ASP A CB  
3206 C CG  . ASP A 466 ? 0.64059 0.70586 0.80186 -0.06305 0.03469  -0.08740 432 ASP A CG  
3207 O OD1 . ASP A 466 ? 0.51360 0.57975 0.66804 -0.05802 0.02572  -0.08821 432 ASP A OD1 
3208 O OD2 . ASP A 466 ? 0.59319 0.67462 0.77377 -0.06491 0.03621  -0.09164 432 ASP A OD2 
3209 N N   . SER A 467 ? 0.91148 0.90571 1.02628 -0.07865 0.05206  -0.07578 433 SER A N   
3210 C CA  . SER A 467 ? 1.16448 1.13433 1.26431 -0.08405 0.05790  -0.07014 433 SER A CA  
3211 C C   . SER A 467 ? 1.23460 1.20123 1.33408 -0.09192 0.06843  -0.06686 433 SER A C   
3212 O O   . SER A 467 ? 1.18088 1.13341 1.26450 -0.09105 0.07180  -0.05874 433 SER A O   
3213 C CB  . SER A 467 ? 1.14481 1.10280 1.24560 -0.09106 0.05716  -0.07525 433 SER A CB  
3214 O OG  . SER A 467 ? 1.08607 1.05546 1.20412 -0.10076 0.06096  -0.08284 433 SER A OG  
3215 N N   . ASN A 468 ? 1.22564 1.20560 1.34249 -0.10005 0.07384  -0.07351 434 ASN A N   
3216 C CA  . ASN A 468 ? 1.31890 1.29664 1.43647 -0.10929 0.08569  -0.07209 434 ASN A CA  
3217 C C   . ASN A 468 ? 1.24668 1.24002 1.36960 -0.10256 0.08736  -0.07089 434 ASN A C   
3218 O O   . ASN A 468 ? 1.37097 1.38653 1.51492 -0.10198 0.08792  -0.07760 434 ASN A O   
3219 C CB  . ASN A 468 ? 1.22274 1.20931 1.35858 -0.12143 0.09163  -0.08054 434 ASN A CB  
3220 C CG  . ASN A 468 ? 1.26107 1.24020 1.39355 -0.13364 0.10557  -0.07886 434 ASN A CG  
3221 O OD1 . ASN A 468 ? 1.21295 1.17163 1.32365 -0.13541 0.11000  -0.07044 434 ASN A OD1 
3222 N ND2 . ASN A 468 ? 1.27449 1.27061 1.42848 -0.14257 0.11254  -0.08708 434 ASN A ND2 
3223 N N   . GLY A 469 ? 0.91029 0.89147 1.01457 -0.09726 0.08761  -0.06241 435 GLY A N   
3224 C CA  . GLY A 469 ? 0.85685 0.84936 0.96381 -0.09126 0.08948  -0.06097 435 GLY A CA  
3225 C C   . GLY A 469 ? 0.91864 0.89628 1.00343 -0.08521 0.08771  -0.05146 435 GLY A C   
3226 O O   . GLY A 469 ? 0.75114 0.70728 0.81699 -0.08960 0.09013  -0.04517 435 GLY A O   
3227 N N   . GLU A 470 ? 0.78187 0.77056 0.86909 -0.07525 0.08276  -0.05019 436 GLU A N   
3228 C CA  . GLU A 470 ? 0.71044 0.68776 0.77881 -0.06953 0.08080  -0.04180 436 GLU A CA  
3229 C C   . GLU A 470 ? 0.57060 0.53921 0.62765 -0.06278 0.07102  -0.03703 436 GLU A C   
3230 O O   . GLU A 470 ? 0.48872 0.44373 0.52854 -0.06027 0.06964  -0.02955 436 GLU A O   
3231 C CB  . GLU A 470 ? 0.69520 0.68708 0.77120 -0.06223 0.07974  -0.04265 436 GLU A CB  
3232 C CG  . GLU A 470 ? 0.76323 0.74437 0.82333 -0.06212 0.08460  -0.03672 436 GLU A CG  
3233 C CD  . GLU A 470 ? 0.88389 0.87925 0.95554 -0.05766 0.08688  -0.04014 436 GLU A CD  
3234 O OE1 . GLU A 470 ? 0.91491 0.92844 1.00860 -0.05607 0.08613  -0.04744 436 GLU A OE1 
3235 O OE2 . GLU A 470 ? 0.89332 0.88137 0.95248 -0.05559 0.08885  -0.03575 436 GLU A OE2 
3236 N N   . GLY A 471 ? 0.51857 0.49515 0.58525 -0.06003 0.06436  -0.04171 437 GLY A N   
3237 C CA  . GLY A 471 ? 0.40514 0.37690 0.46325 -0.05277 0.05574  -0.03874 437 GLY A CA  
3238 C C   . GLY A 471 ? 0.39871 0.34863 0.44185 -0.05544 0.05607  -0.03392 437 GLY A C   
3239 O O   . GLY A 471 ? 0.41168 0.35522 0.44509 -0.04893 0.05052  -0.02943 437 GLY A O   
3240 N N   . GLY A 472 ? 0.43542 0.37348 0.47698 -0.06508 0.06230  -0.03473 438 GLY A N   
3241 C CA  . GLY A 472 ? 0.44814 0.36278 0.47441 -0.06771 0.06187  -0.02915 438 GLY A CA  
3242 C C   . GLY A 472 ? 0.42588 0.32872 0.43508 -0.06503 0.06167  -0.01986 438 GLY A C   
3243 O O   . GLY A 472 ? 0.44013 0.33088 0.43924 -0.06015 0.05587  -0.01482 438 GLY A O   
3244 N N   . GLU A 473 ? 0.42871 0.33523 0.43515 -0.06814 0.06786  -0.01802 439 GLU A N   
3245 C CA  . GLU A 473 ? 0.46116 0.35717 0.45074 -0.06609 0.06737  -0.00973 439 GLU A CA  
3246 C C   . GLU A 473 ? 0.42660 0.33103 0.41638 -0.05472 0.05884  -0.00741 439 GLU A C   
3247 O O   . GLU A 473 ? 0.43011 0.32308 0.40782 -0.05101 0.05376  -0.00091 439 GLU A O   
3248 C CB  . GLU A 473 ? 0.35132 0.25156 0.33924 -0.07144 0.07627  -0.01012 439 GLU A CB  
3249 C CG  . GLU A 473 ? 0.37800 0.27266 0.35109 -0.06776 0.07477  -0.00327 439 GLU A CG  
3250 C CD  . GLU A 473 ? 0.44466 0.35005 0.42157 -0.06915 0.08195  -0.00623 439 GLU A CD  
3251 O OE1 . GLU A 473 ? 0.46441 0.38396 0.45799 -0.07179 0.08764  -0.01383 439 GLU A OE1 
3252 O OE2 . GLU A 473 ? 0.46128 0.36095 0.42524 -0.06750 0.08168  -0.00137 439 GLU A OE2 
3253 N N   . ILE A 474 ? 0.46921 0.39375 0.47282 -0.04943 0.05693  -0.01255 440 ILE A N   
3254 C CA  . ILE A 474 ? 0.43870 0.37177 0.44182 -0.03990 0.04973  -0.01032 440 ILE A CA  
3255 C C   . ILE A 474 ? 0.41932 0.34777 0.42084 -0.03510 0.04298  -0.00986 440 ILE A C   
3256 O O   . ILE A 474 ? 0.41106 0.33625 0.40514 -0.02957 0.03821  -0.00491 440 ILE A O   
3257 C CB  . ILE A 474 ? 0.38649 0.34031 0.40389 -0.03612 0.04865  -0.01573 440 ILE A CB  
3258 C CG1 . ILE A 474 ? 0.52228 0.47947 0.54127 -0.03941 0.05532  -0.01594 440 ILE A CG1 
3259 C CG2 . ILE A 474 ? 0.33141 0.29321 0.34723 -0.02741 0.04120  -0.01342 440 ILE A CG2 
3260 C CD1 . ILE A 474 ? 0.58636 0.56246 0.62144 -0.03620 0.05448  -0.02154 440 ILE A CD1 
3261 N N   . ARG A 475 ? 0.37468 0.30249 0.38366 -0.03743 0.04278  -0.01549 441 ARG A N   
3262 C CA  . ARG A 475 ? 0.49208 0.41398 0.49989 -0.03295 0.03723  -0.01622 441 ARG A CA  
3263 C C   . ARG A 475 ? 0.38673 0.28819 0.38154 -0.03324 0.03588  -0.00893 441 ARG A C   
3264 O O   . ARG A 475 ? 0.44204 0.34133 0.43411 -0.02643 0.03037  -0.00648 441 ARG A O   
3265 C CB  . ARG A 475 ? 0.44355 0.36618 0.46086 -0.03654 0.03773  -0.02415 441 ARG A CB  
3266 C CG  . ARG A 475 ? 0.55569 0.47229 0.57296 -0.03169 0.03261  -0.02673 441 ARG A CG  
3267 C CD  . ARG A 475 ? 0.70061 0.62328 0.72838 -0.03422 0.03222  -0.03629 441 ARG A CD  
3268 N NE  . ARG A 475 ? 0.65510 0.59928 0.69095 -0.03089 0.02985  -0.04129 441 ARG A NE  
3269 C CZ  . ARG A 475 ? 0.74580 0.70260 0.79047 -0.03497 0.03184  -0.04465 441 ARG A CZ  
3270 N NH1 . ARG A 475 ? 0.61562 0.56774 0.66333 -0.04293 0.03766  -0.04434 441 ARG A NH1 
3271 N NH2 . ARG A 475 ? 0.64607 0.62072 0.69684 -0.03112 0.02783  -0.04847 441 ARG A NH2 
3272 N N   . LYS A 476 ? 0.50232 0.38888 0.48889 -0.04128 0.04072  -0.00528 442 LYS A N   
3273 C CA  . LYS A 476 ? 0.43572 0.30103 0.40801 -0.04206 0.03822  0.00258  442 LYS A CA  
3274 C C   . LYS A 476 ? 0.44713 0.31382 0.41065 -0.03725 0.03498  0.00946  442 LYS A C   
3275 O O   . LYS A 476 ? 0.43677 0.29495 0.39492 -0.03216 0.02859  0.01422  442 LYS A O   
3276 C CB  . LYS A 476 ? 0.61613 0.46455 0.57910 -0.05325 0.04460  0.00515  442 LYS A CB  
3277 C CG  . LYS A 476 ? 0.61452 0.43803 0.56056 -0.05511 0.04106  0.01398  442 LYS A CG  
3278 C CD  . LYS A 476 ? 0.71863 0.52448 0.65366 -0.06765 0.04797  0.01646  442 LYS A CD  
3279 C CE  . LYS A 476 ? 0.86105 0.64055 0.77613 -0.06979 0.04328  0.02663  442 LYS A CE  
3280 N NZ  . LYS A 476 ? 0.99955 0.76063 0.89983 -0.08343 0.05073  0.03014  442 LYS A NZ  
3281 N N   . ARG A 477 ? 0.44131 0.31880 0.40438 -0.03867 0.03900  0.00965  443 ARG A N   
3282 C CA  . ARG A 477 ? 0.42302 0.30238 0.37814 -0.03463 0.03594  0.01546  443 ARG A CA  
3283 C C   . ARG A 477 ? 0.46730 0.35830 0.42948 -0.02505 0.02891  0.01476  443 ARG A C   
3284 O O   . ARG A 477 ? 0.41258 0.29981 0.36834 -0.02120 0.02386  0.02033  443 ARG A O   
3285 C CB  . ARG A 477 ? 0.36752 0.25705 0.32321 -0.03734 0.04175  0.01410  443 ARG A CB  
3286 C CG  . ARG A 477 ? 0.48744 0.36508 0.43299 -0.04708 0.04971  0.01563  443 ARG A CG  
3287 C CD  . ARG A 477 ? 0.34963 0.23835 0.29743 -0.04804 0.05522  0.01335  443 ARG A CD  
3288 N NE  . ARG A 477 ? 0.50404 0.38331 0.44281 -0.05762 0.06442  0.01341  443 ARG A NE  
3289 C CZ  . ARG A 477 ? 0.51023 0.37450 0.42986 -0.06195 0.06579  0.01950  443 ARG A CZ  
3290 N NH1 . ARG A 477 ? 0.42403 0.28040 0.33249 -0.05763 0.05766  0.02640  443 ARG A NH1 
3291 N NH2 . ARG A 477 ? 0.48037 0.33777 0.39182 -0.07127 0.07560  0.01831  443 ARG A NH2 
3292 N N   . ALA A 478 ? 0.36715 0.27275 0.34232 -0.02168 0.02856  0.00776  444 ALA A N   
3293 C CA  . ALA A 478 ? 0.35379 0.27104 0.33466 -0.01365 0.02319  0.00637  444 ALA A CA  
3294 C C   . ALA A 478 ? 0.41421 0.32137 0.39429 -0.00970 0.01835  0.00773  444 ALA A C   
3295 O O   . ALA A 478 ? 0.44379 0.35491 0.42380 -0.00396 0.01389  0.01042  444 ALA A O   
3296 C CB  . ALA A 478 ? 0.39571 0.32887 0.38815 -0.01207 0.02383  -0.00162 444 ALA A CB  
3297 N N   . LYS A 479 ? 0.45696 0.35105 0.43750 -0.01272 0.01910  0.00566  445 LYS A N   
3298 C CA  . LYS A 479 ? 0.50918 0.39096 0.48959 -0.00855 0.01401  0.00695  445 LYS A CA  
3299 C C   . LYS A 479 ? 0.46940 0.33804 0.43884 -0.00816 0.00994  0.01634  445 LYS A C   
3300 O O   . LYS A 479 ? 0.49432 0.36094 0.46615 -0.00160 0.00386  0.01835  445 LYS A O   
3301 C CB  . LYS A 479 ? 0.49452 0.36215 0.47629 -0.01296 0.01566  0.00328  445 LYS A CB  
3302 C CG  . LYS A 479 ? 0.76212 0.60891 0.73953 -0.01078 0.01038  0.00738  445 LYS A CG  
3303 C CD  . LYS A 479 ? 0.82790 0.65623 0.80254 -0.01782 0.01270  0.00590  445 LYS A CD  
3304 C CE  . LYS A 479 ? 1.03309 0.83668 0.99978 -0.01659 0.00663  0.01256  445 LYS A CE  
3305 N NZ  . LYS A 479 ? 1.12120 0.92684 1.09779 -0.00542 -0.00029 0.00986  445 LYS A NZ  
3306 N N   . GLU A 480 ? 0.48846 0.34866 0.44609 -0.01521 0.01312  0.02175  446 GLU A N   
3307 C CA  . GLU A 480 ? 0.51938 0.36612 0.46409 -0.01583 0.00868  0.03079  446 GLU A CA  
3308 C C   . GLU A 480 ? 0.48421 0.34447 0.43008 -0.01053 0.00513  0.03335  446 GLU A C   
3309 O O   . GLU A 480 ? 0.48148 0.33561 0.42346 -0.00711 -0.00172 0.03899  446 GLU A O   
3310 C CB  . GLU A 480 ? 0.55684 0.39031 0.48666 -0.02591 0.01412  0.03502  446 GLU A CB  
3311 C CG  . GLU A 480 ? 0.56155 0.37561 0.48601 -0.03234 0.01608  0.03542  446 GLU A CG  
3312 C CD  . GLU A 480 ? 0.67318 0.48100 0.58732 -0.04341 0.02499  0.03611  446 GLU A CD  
3313 O OE1 . GLU A 480 ? 0.66706 0.48731 0.58074 -0.04486 0.02970  0.03497  446 GLU A OE1 
3314 O OE2 . GLU A 480 ? 0.76866 0.55903 0.67546 -0.05080 0.02756  0.03750  446 GLU A OE2 
3315 N N   . MET A 481 ? 0.46687 0.34511 0.41824 -0.01003 0.00912  0.02951  447 MET A N   
3316 C CA  . MET A 481 ? 0.38289 0.27371 0.33555 -0.00562 0.00594  0.03175  447 MET A CA  
3317 C C   . MET A 481 ? 0.46414 0.36388 0.42805 0.00244  0.00074  0.02936  447 MET A C   
3318 O O   . MET A 481 ? 0.44024 0.34454 0.40445 0.00597  -0.00397 0.03306  447 MET A O   
3319 C CB  . MET A 481 ? 0.37870 0.28511 0.33475 -0.00673 0.01084  0.02822  447 MET A CB  
3320 C CG  . MET A 481 ? 0.40572 0.32137 0.35944 -0.00451 0.00838  0.03175  447 MET A CG  
3321 S SD  . MET A 481 ? 0.48784 0.38861 0.42530 -0.00857 0.00559  0.04051  447 MET A SD  
3322 C CE  . MET A 481 ? 0.44569 0.34037 0.37451 -0.01645 0.01419  0.03923  447 MET A CE  
3323 N N   . LYS A 482 ? 0.42639 0.32936 0.40011 0.00509  0.00188  0.02254  448 LYS A N   
3324 C CA  . LYS A 482 ? 0.47687 0.38674 0.46142 0.01269  -0.00208 0.01909  448 LYS A CA  
3325 C C   . LYS A 482 ? 0.44689 0.34360 0.42978 0.01587  -0.00903 0.02478  448 LYS A C   
3326 O O   . LYS A 482 ? 0.44811 0.35342 0.43759 0.02152  -0.01339 0.02573  448 LYS A O   
3327 C CB  . LYS A 482 ? 0.43473 0.34546 0.42767 0.01399  0.00039  0.01050  448 LYS A CB  
3328 C CG  . LYS A 482 ? 0.43803 0.35255 0.44203 0.02187  -0.00303 0.00589  448 LYS A CG  
3329 C CD  . LYS A 482 ? 0.47785 0.38982 0.48842 0.02260  -0.00074 -0.00298 448 LYS A CD  
3330 C CE  . LYS A 482 ? 0.57715 0.49232 0.59923 0.03098  -0.00354 -0.00851 448 LYS A CE  
3331 N NZ  . LYS A 482 ? 0.62649 0.53866 0.65439 0.03170  -0.00118 -0.01827 448 LYS A NZ  
3332 N N   . GLU A 483 ? 0.46375 0.33948 0.43797 0.01198  -0.01044 0.02876  449 GLU A N   
3333 C CA  . GLU A 483 ? 0.53551 0.39601 0.50640 0.01476  -0.01856 0.03523  449 GLU A CA  
3334 C C   . GLU A 483 ? 0.52266 0.38540 0.48581 0.01389  -0.02271 0.04280  449 GLU A C   
3335 O O   . GLU A 483 ? 0.43614 0.29943 0.40428 0.01944  -0.03045 0.04595  449 GLU A O   
3336 C CB  . GLU A 483 ? 0.57721 0.41269 0.53648 0.00887  -0.01888 0.03903  449 GLU A CB  
3337 C CG  . GLU A 483 ? 0.66210 0.49241 0.62870 0.00905  -0.01569 0.03182  449 GLU A CG  
3338 C CD  . GLU A 483 ? 0.96338 0.76911 0.91677 0.00090  -0.01454 0.03596  449 GLU A CD  
3339 O OE1 . GLU A 483 ? 1.13596 0.92296 1.07761 -0.00059 -0.02067 0.04462  449 GLU A OE1 
3340 O OE2 . GLU A 483 ? 0.99306 0.79818 0.94734 -0.00463 -0.00770 0.03070  449 GLU A OE2 
3341 N N   . LYS A 484 ? 0.42503 0.28924 0.37684 0.00700  -0.01788 0.04531  450 LYS A N   
3342 C CA  . LYS A 484 ? 0.48239 0.34769 0.42554 0.00537  -0.02155 0.05187  450 LYS A CA  
3343 C C   . LYS A 484 ? 0.52438 0.41096 0.48000 0.01122  -0.02357 0.04960  450 LYS A C   
3344 O O   . LYS A 484 ? 0.49193 0.37972 0.44681 0.01295  -0.03020 0.05449  450 LYS A O   
3345 C CB  . LYS A 484 ? 0.53846 0.40028 0.46748 -0.00311 -0.01482 0.05354  450 LYS A CB  
3346 C CG  . LYS A 484 ? 0.62395 0.46260 0.53656 -0.01045 -0.01383 0.05812  450 LYS A CG  
3347 C CD  . LYS A 484 ? 0.81305 0.64933 0.71327 -0.01899 -0.00540 0.05811  450 LYS A CD  
3348 C CE  . LYS A 484 ? 0.74314 0.58906 0.65285 -0.02056 0.00360  0.05025  450 LYS A CE  
3349 N NZ  . LYS A 484 ? 0.80182 0.64365 0.70118 -0.02900 0.01222  0.04965  450 LYS A NZ  
3350 N N   . ALA A 485 ? 0.49232 0.39564 0.45908 0.01378  -0.01821 0.04228  451 ALA A N   
3351 C CA  . ALA A 485 ? 0.42200 0.34532 0.39906 0.01805  -0.01900 0.04011  451 ALA A CA  
3352 C C   . ALA A 485 ? 0.46100 0.38863 0.45170 0.02560  -0.02494 0.03866  451 ALA A C   
3353 O O   . ALA A 485 ? 0.38794 0.32560 0.38410 0.02799  -0.02903 0.04088  451 ALA A O   
3354 C CB  . ALA A 485 ? 0.43845 0.37667 0.42117 0.01804  -0.01202 0.03306  451 ALA A CB  
3355 N N   . TRP A 486 ? 0.43438 0.35496 0.43199 0.02946  -0.02544 0.03439  452 TRP A N   
3356 C CA  . TRP A 486 ? 0.50064 0.42535 0.51344 0.03770  -0.03088 0.03187  452 TRP A CA  
3357 C C   . TRP A 486 ? 0.45991 0.37118 0.46947 0.03910  -0.04083 0.04007  452 TRP A C   
3358 O O   . TRP A 486 ? 0.49229 0.41286 0.51457 0.04505  -0.04663 0.04018  452 TRP A O   
3359 C CB  . TRP A 486 ? 0.45575 0.37508 0.47673 0.04167  -0.02873 0.02431  452 TRP A CB  
3360 C CG  . TRP A 486 ? 0.41150 0.34894 0.44025 0.04273  -0.02105 0.01486  452 TRP A CG  
3361 C CD1 . TRP A 486 ? 0.38875 0.32582 0.41239 0.03846  -0.01466 0.01025  452 TRP A CD1 
3362 C CD2 . TRP A 486 ? 0.43150 0.39030 0.47357 0.04772  -0.01917 0.00899  452 TRP A CD2 
3363 N NE1 . TRP A 486 ? 0.42588 0.38160 0.45724 0.04060  -0.00980 0.00229  452 TRP A NE1 
3364 C CE2 . TRP A 486 ? 0.40871 0.37771 0.45066 0.04594  -0.01180 0.00135  452 TRP A CE2 
3365 C CE3 . TRP A 486 ? 0.43567 0.40651 0.48999 0.05304  -0.02292 0.00928  452 TRP A CE3 
3366 C CZ2 . TRP A 486 ? 0.40272 0.39201 0.45375 0.04878  -0.00763 -0.00567 452 TRP A CZ2 
3367 C CZ3 . TRP A 486 ? 0.48574 0.47816 0.55122 0.05584  -0.01789 0.00177  452 TRP A CZ3 
3368 C CH2 . TRP A 486 ? 0.42796 0.42870 0.49046 0.05346  -0.01009 -0.00546 452 TRP A CH2 
3369 N N   . LYS A 487 ? 0.46081 0.35072 0.45344 0.03333  -0.04302 0.04687  453 LYS A N   
3370 C CA  . LYS A 487 ? 0.46573 0.34146 0.45106 0.03328  -0.05324 0.05576  453 LYS A CA  
3371 C C   . LYS A 487 ? 0.47146 0.36025 0.45630 0.03209  -0.05653 0.05970  453 LYS A C   
3372 O O   . LYS A 487 ? 0.50283 0.39292 0.49468 0.03644  -0.06606 0.06329  453 LYS A O   
3373 C CB  . LYS A 487 ? 0.53008 0.38099 0.49337 0.02508  -0.05300 0.06220  453 LYS A CB  
3374 C CG  . LYS A 487 ? 0.72457 0.55634 0.67704 0.02452  -0.06453 0.07185  453 LYS A CG  
3375 C CD  . LYS A 487 ? 0.82329 0.63258 0.74999 0.01406  -0.06235 0.07838  453 LYS A CD  
3376 C CE  . LYS A 487 ? 0.96454 0.76306 0.87537 0.01040  -0.07155 0.08801  453 LYS A CE  
3377 N NZ  . LYS A 487 ? 1.08167 0.85172 0.96775 0.00200  -0.07288 0.09530  453 LYS A NZ  
3378 N N   . ALA A 488 ? 0.44037 0.33892 0.41799 0.02633  -0.04924 0.05887  454 ALA A N   
3379 C CA  . ALA A 488 ? 0.46146 0.37016 0.43668 0.02394  -0.05199 0.06267  454 ALA A CA  
3380 C C   . ALA A 488 ? 0.50456 0.43486 0.50067 0.03062  -0.05479 0.05898  454 ALA A C   
3381 O O   . ALA A 488 ? 0.49817 0.43445 0.49635 0.03029  -0.06116 0.06304  454 ALA A O   
3382 C CB  . ALA A 488 ? 0.45389 0.36791 0.41864 0.01718  -0.04320 0.06161  454 ALA A CB  
3383 N N   . VAL A 489 ? 0.40335 0.34600 0.41511 0.03617  -0.04987 0.05087  455 VAL A N   
3384 C CA  . VAL A 489 ? 0.44217 0.40698 0.47414 0.04187  -0.05046 0.04611  455 VAL A CA  
3385 C C   . VAL A 489 ? 0.48466 0.44833 0.53397 0.05095  -0.05736 0.04367  455 VAL A C   
3386 O O   . VAL A 489 ? 0.43830 0.42106 0.50705 0.05634  -0.05804 0.03907  455 VAL A O   
3387 C CB  . VAL A 489 ? 0.43219 0.41433 0.47013 0.04176  -0.03990 0.03791  455 VAL A CB  
3388 C CG1 . VAL A 489 ? 0.39598 0.37812 0.41783 0.03369  -0.03409 0.04043  455 VAL A CG1 
3389 C CG2 . VAL A 489 ? 0.40212 0.37896 0.44493 0.04585  -0.03589 0.03085  455 VAL A CG2 
3390 N N   . GLN A 490 ? 0.48466 0.42656 0.52812 0.05272  -0.06229 0.04638  456 GLN A N   
3391 C CA  . GLN A 490 ? 0.51764 0.45505 0.57710 0.06193  -0.07027 0.04475  456 GLN A CA  
3392 C C   . GLN A 490 ? 0.55889 0.49066 0.61855 0.06316  -0.08340 0.05331  456 GLN A C   
3393 O O   . GLN A 490 ? 0.53654 0.46620 0.58181 0.05610  -0.08582 0.06030  456 GLN A O   
3394 C CB  . GLN A 490 ? 0.46642 0.38117 0.51901 0.06295  -0.07002 0.04394  456 GLN A CB  
3395 C CG  . GLN A 490 ? 0.63246 0.55589 0.69803 0.06762  -0.06155 0.03250  456 GLN A CG  
3396 C CD  . GLN A 490 ? 0.74248 0.64552 0.79551 0.06402  -0.05763 0.03152  456 GLN A CD  
3397 O OE1 . GLN A 490 ? 0.78007 0.66130 0.81570 0.05853  -0.06135 0.03953  456 GLN A OE1 
3398 N NE2 . GLN A 490 ? 0.73900 0.64913 0.80033 0.06639  -0.04986 0.02140  456 GLN A NE2 
3399 N N   . GLU A 491 ? 0.57558 0.50451 0.65204 0.07243  -0.09254 0.05244  457 GLU A N   
3400 C CA  . GLU A 491 ? 0.65378 0.57758 0.73286 0.07478  -0.10703 0.06036  457 GLU A CA  
3401 C C   . GLU A 491 ? 0.56288 0.46001 0.61249 0.06625  -0.11287 0.07166  457 GLU A C   
3402 O O   . GLU A 491 ? 0.62166 0.49553 0.65671 0.06420  -0.11218 0.07405  457 GLU A O   
3403 C CB  . GLU A 491 ? 0.74564 0.66578 0.84655 0.08690  -0.11633 0.05755  457 GLU A CB  
3404 C CG  . GLU A 491 ? 0.90292 0.83340 1.02115 0.09266  -0.12983 0.06100  457 GLU A CG  
3405 C CD  . GLU A 491 ? 1.06338 0.97658 1.19224 0.10267  -0.14390 0.06365  457 GLU A CD  
3406 O OE1 . GLU A 491 ? 1.03527 0.91828 1.14219 0.09942  -0.15060 0.07221  457 GLU A OE1 
3407 O OE2 . GLU A 491 ? 1.19109 1.12059 1.35041 0.11373  -0.14812 0.05705  457 GLU A OE2 
3408 N N   . GLY A 492 ? 0.67091 0.57143 0.71085 0.06036  -0.11781 0.07816  458 GLY A N   
3409 C CA  . GLY A 492 ? 0.60547 0.48215 0.61618 0.05148  -0.12287 0.08829  458 GLY A CA  
3410 C C   . GLY A 492 ? 0.57518 0.44721 0.56342 0.04087  -0.11036 0.08829  458 GLY A C   
3411 O O   . GLY A 492 ? 0.55278 0.40526 0.51568 0.03271  -0.11269 0.09571  458 GLY A O   
3412 N N   . GLY A 493 ? 0.50387 0.39309 0.50038 0.04067  -0.09737 0.08005  459 GLY A N   
3413 C CA  . GLY A 493 ? 0.44362 0.32998 0.42186 0.03168  -0.08621 0.07956  459 GLY A CA  
3414 C C   . GLY A 493 ? 0.52282 0.41812 0.49250 0.02519  -0.08583 0.08256  459 GLY A C   
3415 O O   . GLY A 493 ? 0.49120 0.40011 0.47225 0.02747  -0.09244 0.08354  459 GLY A O   
3416 N N   . SER A 494 ? 0.47349 0.36104 0.42379 0.01689  -0.07772 0.08347  460 SER A N   
3417 C CA  . SER A 494 ? 0.44730 0.33858 0.38597 0.00995  -0.07701 0.08633  460 SER A CA  
3418 C C   . SER A 494 ? 0.49950 0.41632 0.45576 0.01236  -0.07523 0.08222  460 SER A C   
3419 O O   . SER A 494 ? 0.53769 0.45990 0.49271 0.00955  -0.08093 0.08554  460 SER A O   
3420 C CB  . SER A 494 ? 0.43573 0.31775 0.35590 0.00236  -0.06638 0.08541  460 SER A CB  
3421 O OG  . SER A 494 ? 0.45964 0.35385 0.39062 0.00478  -0.05612 0.07813  460 SER A OG  
3422 N N   . SER A 495 ? 0.37203 0.30440 0.34378 0.01674  -0.06738 0.07501  461 SER A N   
3423 C CA  . SER A 495 ? 0.45381 0.40936 0.43912 0.01735  -0.06425 0.07137  461 SER A CA  
3424 C C   . SER A 495 ? 0.46441 0.43439 0.47082 0.02346  -0.07218 0.07062  461 SER A C   
3425 O O   . SER A 495 ? 0.42599 0.41176 0.44002 0.02153  -0.07331 0.07065  461 SER A O   
3426 C CB  . SER A 495 ? 0.42548 0.39228 0.41746 0.01895  -0.05317 0.06409  461 SER A CB  
3427 O OG  . SER A 495 ? 0.46635 0.42418 0.44170 0.01306  -0.04620 0.06454  461 SER A OG  
3428 N N   . GLN A 496 ? 0.43538 0.40036 0.45246 0.03076  -0.07766 0.06964  462 GLN A N   
3429 C CA  . GLN A 496 ? 0.50371 0.48151 0.54259 0.03745  -0.08651 0.06892  462 GLN A CA  
3430 C C   . GLN A 496 ? 0.46102 0.43230 0.49277 0.03396  -0.09875 0.07699  462 GLN A C   
3431 O O   . GLN A 496 ? 0.50787 0.49663 0.55450 0.03467  -0.10357 0.07671  462 GLN A O   
3432 C CB  . GLN A 496 ? 0.51879 0.48964 0.57015 0.04668  -0.09029 0.06603  462 GLN A CB  
3433 C CG  . GLN A 496 ? 0.55298 0.53438 0.61651 0.05129  -0.07944 0.05638  462 GLN A CG  
3434 C CD  . GLN A 496 ? 0.59223 0.60205 0.68038 0.05570  -0.07589 0.04902  462 GLN A CD  
3435 O OE1 . GLN A 496 ? 0.50429 0.52708 0.60311 0.05566  -0.08184 0.05104  462 GLN A OE1 
3436 N NE2 . GLN A 496 ? 0.49637 0.51636 0.59347 0.05891  -0.06596 0.04008  462 GLN A NE2 
3437 N N   . ASN A 497 ? 0.46163 0.40804 0.47029 0.02953  -0.10383 0.08403  463 ASN A N   
3438 C CA  . ASN A 497 ? 0.42037 0.35861 0.41788 0.02489  -0.11551 0.09179  463 ASN A CA  
3439 C C   . ASN A 497 ? 0.48959 0.43970 0.48187 0.01714  -0.11177 0.09190  463 ASN A C   
3440 O O   . ASN A 497 ? 0.49232 0.45180 0.49171 0.01586  -0.12053 0.09437  463 ASN A O   
3441 C CB  . ASN A 497 ? 0.41405 0.32219 0.38337 0.01981  -0.11927 0.09884  463 ASN A CB  
3442 C CG  . ASN A 497 ? 0.57543 0.46850 0.54819 0.02666  -0.12484 0.10015  463 ASN A CG  
3443 O OD1 . ASN A 497 ? 0.62322 0.52764 0.62068 0.03621  -0.12892 0.09641  463 ASN A OD1 
3444 N ND2 . ASN A 497 ? 0.56979 0.43669 0.51779 0.02155  -0.12484 0.10526  463 ASN A ND2 
3445 N N   . CYS A 498 ? 0.45720 0.40695 0.43792 0.01194  -0.09932 0.08914  464 CYS A N   
3446 C CA  . CYS A 498 ? 0.45649 0.41427 0.43056 0.00446  -0.09577 0.08948  464 CYS A CA  
3447 C C   . CYS A 498 ? 0.46432 0.44926 0.46245 0.00680  -0.09465 0.08521  464 CYS A C   
3448 O O   . CYS A 498 ? 0.47127 0.46416 0.46981 0.00158  -0.09830 0.08718  464 CYS A O   
3449 C CB  . CYS A 498 ? 0.51169 0.46246 0.46996 -0.00034 -0.08328 0.08723  464 CYS A CB  
3450 S SG  . CYS A 498 ? 0.51671 0.47289 0.46493 -0.00920 -0.07904 0.08776  464 CYS A SG  
3451 N N   . LEU A 499 ? 0.40466 0.40396 0.42258 0.01395  -0.08924 0.07897  465 LEU A N   
3452 C CA  . LEU A 499 ? 0.43819 0.46409 0.47941 0.01586  -0.08718 0.07428  465 LEU A CA  
3453 C C   . LEU A 499 ? 0.48581 0.52070 0.54295 0.01815  -0.09990 0.07670  465 LEU A C   
3454 O O   . LEU A 499 ? 0.41344 0.46604 0.48135 0.01443  -0.10083 0.07608  465 LEU A O   
3455 C CB  . LEU A 499 ? 0.43302 0.47085 0.49107 0.02330  -0.07905 0.06644  465 LEU A CB  
3456 C CG  . LEU A 499 ? 0.55569 0.62189 0.63813 0.02528  -0.07497 0.06032  465 LEU A CG  
3457 C CD1 . LEU A 499 ? 0.41461 0.49045 0.48949 0.01612  -0.06822 0.06100  465 LEU A CD1 
3458 C CD2 . LEU A 499 ? 0.49178 0.56690 0.58790 0.03260  -0.06675 0.05188  465 LEU A CD2 
3459 N N   . THR A 500 ? 0.43122 0.45384 0.49034 0.02404  -0.11035 0.07964  466 THR A N   
3460 C CA  . THR A 500 ? 0.42367 0.45310 0.49762 0.02677  -0.12468 0.08263  466 THR A CA  
3461 C C   . THR A 500 ? 0.41643 0.43938 0.47357 0.01707  -0.13197 0.08926  466 THR A C   
3462 O O   . THR A 500 ? 0.43787 0.47815 0.51000 0.01514  -0.13797 0.08922  466 THR A O   
3463 C CB  . THR A 500 ? 0.52702 0.54013 0.60285 0.03494  -0.13530 0.08551  466 THR A CB  
3464 O OG1 . THR A 500 ? 0.48826 0.50823 0.58154 0.04403  -0.12834 0.07821  466 THR A OG1 
3465 C CG2 . THR A 500 ? 0.40084 0.42049 0.49288 0.03857  -0.15219 0.08906  466 THR A CG2 
3466 N N   . LYS A 501 ? 0.47198 0.47069 0.49846 0.01045  -0.13099 0.09430  467 LYS A N   
3467 C CA  . LYS A 501 ? 0.48028 0.47083 0.48814 0.00073  -0.13696 0.09969  467 LYS A CA  
3468 C C   . LYS A 501 ? 0.50151 0.50944 0.51393 -0.00596 -0.12925 0.09658  467 LYS A C   
3469 O O   . LYS A 501 ? 0.49894 0.51178 0.51094 -0.01205 -0.13663 0.09916  467 LYS A O   
3470 C CB  . LYS A 501 ? 0.40405 0.36584 0.37818 -0.00510 -0.13456 0.10406  467 LYS A CB  
3471 C CG  . LYS A 501 ? 0.74895 0.68937 0.71245 -0.00166 -0.14479 0.10945  467 LYS A CG  
3472 C CD  . LYS A 501 ? 0.74784 0.66072 0.67616 -0.00978 -0.14250 0.11395  467 LYS A CD  
3473 C CE  . LYS A 501 ? 0.84258 0.73275 0.75798 -0.00768 -0.15316 0.12030  467 LYS A CE  
3474 N NZ  . LYS A 501 ? 0.70821 0.60023 0.63126 -0.00568 -0.17173 0.12555  467 LYS A NZ  
3475 N N   . LEU A 502 ? 0.43465 0.45082 0.45025 -0.00551 -0.11503 0.09134  468 LEU A N   
3476 C CA  . LEU A 502 ? 0.42747 0.45865 0.44643 -0.01200 -0.10756 0.08892  468 LEU A CA  
3477 C C   . LEU A 502 ? 0.42131 0.47845 0.46760 -0.01115 -0.11248 0.08674  468 LEU A C   
3478 O O   . LEU A 502 ? 0.41640 0.48020 0.46227 -0.01889 -0.11570 0.08848  468 LEU A O   
3479 C CB  . LEU A 502 ? 0.46504 0.50046 0.48361 -0.01053 -0.09281 0.08395  468 LEU A CB  
3480 C CG  . LEU A 502 ? 0.44302 0.49541 0.46752 -0.01605 -0.08438 0.08118  468 LEU A CG  
3481 C CD1 . LEU A 502 ? 0.40969 0.45153 0.41505 -0.02617 -0.08579 0.08534  468 LEU A CD1 
3482 C CD2 . LEU A 502 ? 0.36070 0.41595 0.38425 -0.01350 -0.07163 0.07662  468 LEU A CD2 
3483 N N   . VAL A 503 ? 0.38970 0.46203 0.46087 -0.00194 -0.11281 0.08233  469 VAL A N   
3484 C CA  . VAL A 503 ? 0.42143 0.52120 0.52216 -0.00049 -0.11617 0.07889  469 VAL A CA  
3485 C C   . VAL A 503 ? 0.42434 0.52306 0.52858 -0.00263 -0.13259 0.08400  469 VAL A C   
3486 O O   . VAL A 503 ? 0.48840 0.60479 0.60558 -0.00821 -0.13565 0.08353  469 VAL A O   
3487 C CB  . VAL A 503 ? 0.42914 0.54376 0.55582 0.01086  -0.11285 0.07209  469 VAL A CB  
3488 C CG1 . VAL A 503 ? 0.44120 0.58533 0.60124 0.01308  -0.11665 0.06777  469 VAL A CG1 
3489 C CG2 . VAL A 503 ? 0.35711 0.47495 0.47967 0.01130  -0.09663 0.06658  469 VAL A CG2 
3490 N N   . ASP A 504 ? 0.40701 0.48440 0.49859 0.00092  -0.14367 0.08920  470 ASP A N   
3491 C CA  . ASP A 504 ? 0.51180 0.58473 0.60176 -0.00194 -0.16060 0.09495  470 ASP A CA  
3492 C C   . ASP A 504 ? 0.57439 0.64102 0.64358 -0.01492 -0.16079 0.09837  470 ASP A C   
3493 O O   . ASP A 504 ? 0.50331 0.58190 0.58253 -0.01981 -0.17004 0.09960  470 ASP A O   
3494 C CB  . ASP A 504 ? 0.49814 0.54476 0.57157 0.00277  -0.17146 0.10082  470 ASP A CB  
3495 C CG  . ASP A 504 ? 0.61232 0.66466 0.70935 0.01592  -0.17562 0.09813  470 ASP A CG  
3496 O OD1 . ASP A 504 ? 0.69883 0.77818 0.82827 0.02163  -0.17277 0.09154  470 ASP A OD1 
3497 O OD2 . ASP A 504 ? 0.80448 0.83386 0.88754 0.02027  -0.18133 0.10230  470 ASP A OD2 
3498 N N   . TYR A 505 ? 0.46669 0.51475 0.50795 -0.02057 -0.15078 0.09944  471 TYR A N   
3499 C CA  . TYR A 505 ? 0.53188 0.57199 0.55286 -0.03242 -0.14999 0.10184  471 TYR A CA  
3500 C C   . TYR A 505 ? 0.58915 0.65371 0.62810 -0.03789 -0.14443 0.09814  471 TYR A C   
3501 O O   . TYR A 505 ? 0.64079 0.70773 0.67660 -0.04668 -0.15066 0.10009  471 TYR A O   
3502 C CB  . TYR A 505 ? 0.47018 0.48774 0.46195 -0.03578 -0.13896 0.10235  471 TYR A CB  
3503 C CG  . TYR A 505 ? 0.47559 0.48791 0.45064 -0.04665 -0.13380 0.10258  471 TYR A CG  
3504 C CD1 . TYR A 505 ? 0.55690 0.55454 0.51240 -0.05492 -0.14274 0.10644  471 TYR A CD1 
3505 C CD2 . TYR A 505 ? 0.50007 0.52071 0.47788 -0.04872 -0.12039 0.09892  471 TYR A CD2 
3506 C CE1 . TYR A 505 ? 0.52618 0.51748 0.46657 -0.06459 -0.13803 0.10602  471 TYR A CE1 
3507 C CE2 . TYR A 505 ? 0.53841 0.55225 0.50114 -0.05816 -0.11633 0.09935  471 TYR A CE2 
3508 C CZ  . TYR A 505 ? 0.52093 0.52007 0.46563 -0.06587 -0.12496 0.10260  471 TYR A CZ  
3509 O OH  . TYR A 505 ? 0.48735 0.47843 0.41737 -0.07499 -0.12092 0.10240  471 TYR A OH  
3510 N N   . LEU A 506 ? 0.41896 0.50127 0.47578 -0.03359 -0.13262 0.09274  472 LEU A N   
3511 C CA  . LEU A 506 ? 0.51989 0.62585 0.59358 -0.03941 -0.12646 0.08933  472 LEU A CA  
3512 C C   . LEU A 506 ? 0.54615 0.67406 0.64674 -0.03963 -0.13778 0.08870  472 LEU A C   
3513 O O   . LEU A 506 ? 0.55577 0.69613 0.66238 -0.04885 -0.13841 0.08858  472 LEU A O   
3514 C CB  . LEU A 506 ? 0.43655 0.55686 0.52305 -0.03449 -0.11195 0.08349  472 LEU A CB  
3515 C CG  . LEU A 506 ? 0.55066 0.65415 0.61374 -0.03578 -0.09986 0.08346  472 LEU A CG  
3516 C CD1 . LEU A 506 ? 0.41129 0.53137 0.48775 -0.03210 -0.08688 0.07763  472 LEU A CD1 
3517 C CD2 . LEU A 506 ? 0.51709 0.60871 0.55876 -0.04711 -0.09801 0.08687  472 LEU A CD2 
3518 N N   . HIS A 507 ? 0.47458 0.60743 0.59256 -0.02957 -0.14720 0.08821  473 HIS A N   
3519 C CA  . HIS A 507 ? 0.58386 0.73789 0.72972 -0.02859 -0.15972 0.08752  473 HIS A CA  
3520 C C   . HIS A 507 ? 0.64434 0.78817 0.77539 -0.03841 -0.17295 0.09329  473 HIS A C   
3521 O O   . HIS A 507 ? 0.64270 0.80581 0.79013 -0.04529 -0.17713 0.09216  473 HIS A O   
3522 C CB  . HIS A 507 ? 0.59333 0.74931 0.75755 -0.01504 -0.16923 0.08677  473 HIS A CB  
3523 C CG  . HIS A 507 ? 0.59238 0.77460 0.78974 -0.00620 -0.16048 0.07852  473 HIS A CG  
3524 N ND1 . HIS A 507 ? 0.64858 0.86322 0.88059 -0.00641 -0.16155 0.07330  473 HIS A ND1 
3525 C CD2 . HIS A 507 ? 0.58070 0.76185 0.78191 0.00273  -0.15008 0.07387  473 HIS A CD2 
3526 C CE1 . HIS A 507 ? 0.60563 0.83796 0.86088 0.00216  -0.15147 0.06548  473 HIS A CE1 
3527 N NE2 . HIS A 507 ? 0.60329 0.81524 0.83992 0.00786  -0.14476 0.06570  473 HIS A NE2 
3528 N N   . SER A 508 ? 0.56505 0.67855 0.66441 -0.04001 -0.17920 0.09912  474 SER A N   
3529 C CA  . SER A 508 ? 0.63998 0.74123 0.72145 -0.04984 -0.19157 0.10416  474 SER A CA  
3530 C C   . SER A 508 ? 0.68988 0.79038 0.75783 -0.06278 -0.18284 0.10334  474 SER A C   
3531 O O   . SER A 508 ? 0.74803 0.84755 0.81052 -0.07217 -0.19231 0.10552  474 SER A O   
3532 C CB  . SER A 508 ? 0.58937 0.65731 0.63771 -0.04902 -0.19861 0.11002  474 SER A CB  
3533 O OG  . SER A 508 ? 0.77302 0.82068 0.79263 -0.05317 -0.18507 0.10998  474 SER A OG  
3534 N N   . VAL A 509 ? 0.60205 0.70173 0.66379 -0.06358 -0.16581 0.10039  475 VAL A N   
3535 C CA  . VAL A 509 ? 0.69553 0.79375 0.74555 -0.07527 -0.15762 0.09985  475 VAL A CA  
3536 C C   . VAL A 509 ? 0.65823 0.78698 0.73731 -0.08046 -0.15651 0.09658  475 VAL A C   
3537 O O   . VAL A 509 ? 0.77245 0.90239 0.84695 -0.09204 -0.15879 0.09751  475 VAL A O   
3538 C CB  . VAL A 509 ? 0.74632 0.83246 0.77985 -0.07387 -0.14119 0.09834  475 VAL A CB  
3539 C CG1 . VAL A 509 ? 0.75048 0.84611 0.78573 -0.08289 -0.13074 0.09648  475 VAL A CG1 
3540 C CG2 . VAL A 509 ? 0.74625 0.80006 0.74534 -0.07523 -0.14185 0.10162  475 VAL A CG2 
3541 N N   . VAL A 510 ? 0.64028 0.79391 0.74964 -0.07250 -0.15271 0.09227  476 VAL A N   
3542 C CA  . VAL A 510 ? 0.65617 0.84167 0.79625 -0.07701 -0.15077 0.08827  476 VAL A CA  
3543 C C   . VAL A 510 ? 0.67225 0.86974 0.83012 -0.07893 -0.16845 0.08951  476 VAL A C   
3544 O O   . VAL A 510 ? 0.86627 1.07322 1.02877 -0.09037 -0.17194 0.08978  476 VAL A O   
3545 C CB  . VAL A 510 ? 0.57230 0.78072 0.73915 -0.06739 -0.14026 0.08209  476 VAL A CB  
3546 C CG1 . VAL A 510 ? 0.66620 0.90985 0.86748 -0.07192 -0.13842 0.07717  476 VAL A CG1 
3547 C CG2 . VAL A 510 ? 0.61325 0.81118 0.76215 -0.06711 -0.12333 0.08086  476 VAL A CG2 
# 
