data_9I69
# 
_entry.id   9I69 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9I69         pdb_00009i69 10.2210/pdb9i69/pdb 
WWPDB D_1292145045 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-02-12 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9I69 
_pdbx_database_status.recvd_initial_deposition_date   2025-01-29 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_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_database_related.db_name        PDB 
_pdbx_database_related.details        . 
_pdbx_database_related.db_id          9I6A 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              lsi10@cam.ac.uk 
_pdbx_contact_author.name_first         Itzhaki 
_pdbx_contact_author.name_last          Laura 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-6504-2576 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Eapen, R.'         1  0000-0001-7269-3633 
'Okoye, C.'         2  ?                   
'Stubbs, C.'        3  ?                   
'Schimpl, M.'       4  0000-0003-2284-5250 
'Tischer, T.'       5  ?                   
'Fisher, E.J.'      6  ?                   
'Zacharopoulou, M.' 7  ?                   
'Ferrer, F.'        8  ?                   
'Barford, D.'       9  ?                   
'Spring, D.'        10 ?                   
'Lindon, C.'        11 ?                   
'Phillips, C.'      12 ?                   
'Itzhaki, L.S.'     13 0000-0001-6504-2576 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            '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                     'Development of D-box peptides to inhibit the Anaphase Promoting Complex/Cyclosome' 
_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 'Eapen, R.'         1  0000-0001-7269-3633 
primary 'Okoye, C.'         2  ?                   
primary 'Stubbs, C.'        3  ?                   
primary 'Schimpl, M.'       4  0000-0003-2284-5250 
primary 'Tischer, T.'       5  ?                   
primary 'Fisher, E.J.'      6  ?                   
primary 'Zacharopoulou, M.' 7  ?                   
primary 'Ferrer, F.'        8  ?                   
primary 'Barford, D.'       9  ?                   
primary 'Spring, D.'        10 ?                   
primary 'Lindon, C.'        11 ?                   
primary 'Phillips, C.'      12 ?                   
primary 'Itzhaki, L.S.'     13 0000-0001-6504-2576 
# 
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 'Cell division cycle protein 20 homolog' 54796.508 1   ? ? ? ? 
2 polymer syn ARG-ALA-PRO-0JY-SER-ASP                  1001.116  1   ? ? ? ? 
3 water   nat water                                    18.015    240 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        p55CDC 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no  
;MAQFAFESDLHSLLQLDAPIPNAPPARWQRKAKEAAGPAPSPMRAANRSHSAGRTPGRTPGKSSSKVQTTPSKPGGDRYI
PHRSAAQMEVASFLLSKENQPENSQTPTKKEHQKAWALNLNGFDVEEAKILRLSGKPQNAPEGYQNRLKVLYSQKATPGS
SRKTCRYIPSLPDRILDAPEIRNDYYLNLVDWSSGNVLAVALDNSVYLWSASSGDILQLLQMEQPGEYISSVAWIKEGNY
LAVGTSSAEVQLWDVQQQKRLRNMTSHSARVGSLSWNSYILSSGSRSGHIHHHDVRVAEHHVATLSGHSQEVCGLRWAPD
GRHLASGGNDNLVNVWPSAPGEGGWVPLQTFTQHQGAVKAVAWCPWQSNVLATGGGTSDRHIRIWNVCSGACLSAVDAHS
QVCSILWSPHYKELISGHGFAQNQLVIWKYPTMAKVAELKGHTSRVLSLTMSPDGATVASAAADETLRLWRCFELDPARR
REREKASAAKSSLIHQGIR
;
;MAQFAFESDLHSLLQLDAPIPNAPPARWQRKAKEAAGPAPSPMRAANRSHSAGRTPGRTPGKSSSKVQTTPSKPGGDRYI
PHRSAAQMEVASFLLSKENQPENSQTPTKKEHQKAWALNLNGFDVEEAKILRLSGKPQNAPEGYQNRLKVLYSQKATPGS
SRKTCRYIPSLPDRILDAPEIRNDYYLNLVDWSSGNVLAVALDNSVYLWSASSGDILQLLQMEQPGEYISSVAWIKEGNY
LAVGTSSAEVQLWDVQQQKRLRNMTSHSARVGSLSWNSYILSSGSRSGHIHHHDVRVAEHHVATLSGHSQEVCGLRWAPD
GRHLASGGNDNLVNVWPSAPGEGGWVPLQTFTQHQGAVKAVAWCPWQSNVLATGGGTSDRHIRIWNVCSGACLSAVDAHS
QVCSILWSPHYKELISGHGFAQNQLVIWKYPTMAKVAELKGHTSRVLSLTMSPDGATVASAAADETLRLWRCFELDPARR
REREKASAAKSSLIHQGIR
;
A ? 
2 'polypeptide(L)' no yes 'RAP(0JY)SDITN' RAPXSDITN B ? 
# 
_pdbx_entity_nonpoly.entity_id   3 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ALA n 
1 3   GLN n 
1 4   PHE n 
1 5   ALA n 
1 6   PHE n 
1 7   GLU n 
1 8   SER n 
1 9   ASP n 
1 10  LEU n 
1 11  HIS n 
1 12  SER n 
1 13  LEU n 
1 14  LEU n 
1 15  GLN n 
1 16  LEU n 
1 17  ASP n 
1 18  ALA n 
1 19  PRO n 
1 20  ILE n 
1 21  PRO n 
1 22  ASN n 
1 23  ALA n 
1 24  PRO n 
1 25  PRO n 
1 26  ALA n 
1 27  ARG n 
1 28  TRP n 
1 29  GLN n 
1 30  ARG n 
1 31  LYS n 
1 32  ALA n 
1 33  LYS n 
1 34  GLU n 
1 35  ALA n 
1 36  ALA n 
1 37  GLY n 
1 38  PRO n 
1 39  ALA n 
1 40  PRO n 
1 41  SER n 
1 42  PRO n 
1 43  MET n 
1 44  ARG n 
1 45  ALA n 
1 46  ALA n 
1 47  ASN n 
1 48  ARG n 
1 49  SER n 
1 50  HIS n 
1 51  SER n 
1 52  ALA n 
1 53  GLY n 
1 54  ARG n 
1 55  THR n 
1 56  PRO n 
1 57  GLY n 
1 58  ARG n 
1 59  THR n 
1 60  PRO n 
1 61  GLY n 
1 62  LYS n 
1 63  SER n 
1 64  SER n 
1 65  SER n 
1 66  LYS n 
1 67  VAL n 
1 68  GLN n 
1 69  THR n 
1 70  THR n 
1 71  PRO n 
1 72  SER n 
1 73  LYS n 
1 74  PRO n 
1 75  GLY n 
1 76  GLY n 
1 77  ASP n 
1 78  ARG n 
1 79  TYR n 
1 80  ILE n 
1 81  PRO n 
1 82  HIS n 
1 83  ARG n 
1 84  SER n 
1 85  ALA n 
1 86  ALA n 
1 87  GLN n 
1 88  MET n 
1 89  GLU n 
1 90  VAL n 
1 91  ALA n 
1 92  SER n 
1 93  PHE n 
1 94  LEU n 
1 95  LEU n 
1 96  SER n 
1 97  LYS n 
1 98  GLU n 
1 99  ASN n 
1 100 GLN n 
1 101 PRO n 
1 102 GLU n 
1 103 ASN n 
1 104 SER n 
1 105 GLN n 
1 106 THR n 
1 107 PRO n 
1 108 THR n 
1 109 LYS n 
1 110 LYS n 
1 111 GLU n 
1 112 HIS n 
1 113 GLN n 
1 114 LYS n 
1 115 ALA n 
1 116 TRP n 
1 117 ALA n 
1 118 LEU n 
1 119 ASN n 
1 120 LEU n 
1 121 ASN n 
1 122 GLY n 
1 123 PHE n 
1 124 ASP n 
1 125 VAL n 
1 126 GLU n 
1 127 GLU n 
1 128 ALA n 
1 129 LYS n 
1 130 ILE n 
1 131 LEU n 
1 132 ARG n 
1 133 LEU n 
1 134 SER n 
1 135 GLY n 
1 136 LYS n 
1 137 PRO n 
1 138 GLN n 
1 139 ASN n 
1 140 ALA n 
1 141 PRO n 
1 142 GLU n 
1 143 GLY n 
1 144 TYR n 
1 145 GLN n 
1 146 ASN n 
1 147 ARG n 
1 148 LEU n 
1 149 LYS n 
1 150 VAL n 
1 151 LEU n 
1 152 TYR n 
1 153 SER n 
1 154 GLN n 
1 155 LYS n 
1 156 ALA n 
1 157 THR n 
1 158 PRO n 
1 159 GLY n 
1 160 SER n 
1 161 SER n 
1 162 ARG n 
1 163 LYS n 
1 164 THR n 
1 165 CYS n 
1 166 ARG n 
1 167 TYR n 
1 168 ILE n 
1 169 PRO n 
1 170 SER n 
1 171 LEU n 
1 172 PRO n 
1 173 ASP n 
1 174 ARG n 
1 175 ILE n 
1 176 LEU n 
1 177 ASP n 
1 178 ALA n 
1 179 PRO n 
1 180 GLU n 
1 181 ILE n 
1 182 ARG n 
1 183 ASN n 
1 184 ASP n 
1 185 TYR n 
1 186 TYR n 
1 187 LEU n 
1 188 ASN n 
1 189 LEU n 
1 190 VAL n 
1 191 ASP n 
1 192 TRP n 
1 193 SER n 
1 194 SER n 
1 195 GLY n 
1 196 ASN n 
1 197 VAL n 
1 198 LEU n 
1 199 ALA n 
1 200 VAL n 
1 201 ALA n 
1 202 LEU n 
1 203 ASP n 
1 204 ASN n 
1 205 SER n 
1 206 VAL n 
1 207 TYR n 
1 208 LEU n 
1 209 TRP n 
1 210 SER n 
1 211 ALA n 
1 212 SER n 
1 213 SER n 
1 214 GLY n 
1 215 ASP n 
1 216 ILE n 
1 217 LEU n 
1 218 GLN n 
1 219 LEU n 
1 220 LEU n 
1 221 GLN n 
1 222 MET n 
1 223 GLU n 
1 224 GLN n 
1 225 PRO n 
1 226 GLY n 
1 227 GLU n 
1 228 TYR n 
1 229 ILE n 
1 230 SER n 
1 231 SER n 
1 232 VAL n 
1 233 ALA n 
1 234 TRP n 
1 235 ILE n 
1 236 LYS n 
1 237 GLU n 
1 238 GLY n 
1 239 ASN n 
1 240 TYR n 
1 241 LEU n 
1 242 ALA n 
1 243 VAL n 
1 244 GLY n 
1 245 THR n 
1 246 SER n 
1 247 SER n 
1 248 ALA n 
1 249 GLU n 
1 250 VAL n 
1 251 GLN n 
1 252 LEU n 
1 253 TRP n 
1 254 ASP n 
1 255 VAL n 
1 256 GLN n 
1 257 GLN n 
1 258 GLN n 
1 259 LYS n 
1 260 ARG n 
1 261 LEU n 
1 262 ARG n 
1 263 ASN n 
1 264 MET n 
1 265 THR n 
1 266 SER n 
1 267 HIS n 
1 268 SER n 
1 269 ALA n 
1 270 ARG n 
1 271 VAL n 
1 272 GLY n 
1 273 SER n 
1 274 LEU n 
1 275 SER n 
1 276 TRP n 
1 277 ASN n 
1 278 SER n 
1 279 TYR n 
1 280 ILE n 
1 281 LEU n 
1 282 SER n 
1 283 SER n 
1 284 GLY n 
1 285 SER n 
1 286 ARG n 
1 287 SER n 
1 288 GLY n 
1 289 HIS n 
1 290 ILE n 
1 291 HIS n 
1 292 HIS n 
1 293 HIS n 
1 294 ASP n 
1 295 VAL n 
1 296 ARG n 
1 297 VAL n 
1 298 ALA n 
1 299 GLU n 
1 300 HIS n 
1 301 HIS n 
1 302 VAL n 
1 303 ALA n 
1 304 THR n 
1 305 LEU n 
1 306 SER n 
1 307 GLY n 
1 308 HIS n 
1 309 SER n 
1 310 GLN n 
1 311 GLU n 
1 312 VAL n 
1 313 CYS n 
1 314 GLY n 
1 315 LEU n 
1 316 ARG n 
1 317 TRP n 
1 318 ALA n 
1 319 PRO n 
1 320 ASP n 
1 321 GLY n 
1 322 ARG n 
1 323 HIS n 
1 324 LEU n 
1 325 ALA n 
1 326 SER n 
1 327 GLY n 
1 328 GLY n 
1 329 ASN n 
1 330 ASP n 
1 331 ASN n 
1 332 LEU n 
1 333 VAL n 
1 334 ASN n 
1 335 VAL n 
1 336 TRP n 
1 337 PRO n 
1 338 SER n 
1 339 ALA n 
1 340 PRO n 
1 341 GLY n 
1 342 GLU n 
1 343 GLY n 
1 344 GLY n 
1 345 TRP n 
1 346 VAL n 
1 347 PRO n 
1 348 LEU n 
1 349 GLN n 
1 350 THR n 
1 351 PHE n 
1 352 THR n 
1 353 GLN n 
1 354 HIS n 
1 355 GLN n 
1 356 GLY n 
1 357 ALA n 
1 358 VAL n 
1 359 LYS n 
1 360 ALA n 
1 361 VAL n 
1 362 ALA n 
1 363 TRP n 
1 364 CYS n 
1 365 PRO n 
1 366 TRP n 
1 367 GLN n 
1 368 SER n 
1 369 ASN n 
1 370 VAL n 
1 371 LEU n 
1 372 ALA n 
1 373 THR n 
1 374 GLY n 
1 375 GLY n 
1 376 GLY n 
1 377 THR n 
1 378 SER n 
1 379 ASP n 
1 380 ARG n 
1 381 HIS n 
1 382 ILE n 
1 383 ARG n 
1 384 ILE n 
1 385 TRP n 
1 386 ASN n 
1 387 VAL n 
1 388 CYS n 
1 389 SER n 
1 390 GLY n 
1 391 ALA n 
1 392 CYS n 
1 393 LEU n 
1 394 SER n 
1 395 ALA n 
1 396 VAL n 
1 397 ASP n 
1 398 ALA n 
1 399 HIS n 
1 400 SER n 
1 401 GLN n 
1 402 VAL n 
1 403 CYS n 
1 404 SER n 
1 405 ILE n 
1 406 LEU n 
1 407 TRP n 
1 408 SER n 
1 409 PRO n 
1 410 HIS n 
1 411 TYR n 
1 412 LYS n 
1 413 GLU n 
1 414 LEU n 
1 415 ILE n 
1 416 SER n 
1 417 GLY n 
1 418 HIS n 
1 419 GLY n 
1 420 PHE n 
1 421 ALA n 
1 422 GLN n 
1 423 ASN n 
1 424 GLN n 
1 425 LEU n 
1 426 VAL n 
1 427 ILE n 
1 428 TRP n 
1 429 LYS n 
1 430 TYR n 
1 431 PRO n 
1 432 THR n 
1 433 MET n 
1 434 ALA n 
1 435 LYS n 
1 436 VAL n 
1 437 ALA n 
1 438 GLU n 
1 439 LEU n 
1 440 LYS n 
1 441 GLY n 
1 442 HIS n 
1 443 THR n 
1 444 SER n 
1 445 ARG n 
1 446 VAL n 
1 447 LEU n 
1 448 SER n 
1 449 LEU n 
1 450 THR n 
1 451 MET n 
1 452 SER n 
1 453 PRO n 
1 454 ASP n 
1 455 GLY n 
1 456 ALA n 
1 457 THR n 
1 458 VAL n 
1 459 ALA n 
1 460 SER n 
1 461 ALA n 
1 462 ALA n 
1 463 ALA n 
1 464 ASP n 
1 465 GLU n 
1 466 THR n 
1 467 LEU n 
1 468 ARG n 
1 469 LEU n 
1 470 TRP n 
1 471 ARG n 
1 472 CYS n 
1 473 PHE n 
1 474 GLU n 
1 475 LEU n 
1 476 ASP n 
1 477 PRO n 
1 478 ALA n 
1 479 ARG n 
1 480 ARG n 
1 481 ARG n 
1 482 GLU n 
1 483 ARG n 
1 484 GLU n 
1 485 LYS n 
1 486 ALA n 
1 487 SER n 
1 488 ALA n 
1 489 ALA n 
1 490 LYS n 
1 491 SER n 
1 492 SER n 
1 493 LEU n 
1 494 ILE n 
1 495 HIS n 
1 496 GLN n 
1 497 GLY n 
1 498 ILE n 
1 499 ARG n 
2 1   ARG n 
2 2   ALA n 
2 3   PRO n 
2 4   0JY n 
2 5   SER n 
2 6   ASP n 
2 7   ILE n 
2 8   THR n 
2 9   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                   499 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CDC20 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_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      'Spodoptera frugiperda' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     7108 
_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            Sf21 
_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                   ? 
# 
_pdbx_entity_src_syn.entity_id              2 
_pdbx_entity_src_syn.pdbx_src_id            1 
_pdbx_entity_src_syn.pdbx_alt_source_flag   sample 
_pdbx_entity_src_syn.pdbx_beg_seq_num       1 
_pdbx_entity_src_syn.pdbx_end_seq_num       9 
_pdbx_entity_src_syn.organism_scientific    'Homo sapiens' 
_pdbx_entity_src_syn.organism_common_name   ? 
_pdbx_entity_src_syn.ncbi_taxonomy_id       9606 
_pdbx_entity_src_syn.details                ? 
# 
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 
0JY non-polymer         . 4-methyl-L-leucine ? 'C7 H15 N O2'    145.200 
ALA 'L-peptide linking' y ALANINE            ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE           ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE         ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'    ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE           ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE          ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'    ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE            ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE          ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER              ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE         ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE            ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE             ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE         ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE      ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE            ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE             ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE          ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN         ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE           ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE             ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   ALA 2   2   ?   ?   ?   A . n 
A 1 3   GLN 3   3   ?   ?   ?   A . n 
A 1 4   PHE 4   4   ?   ?   ?   A . n 
A 1 5   ALA 5   5   ?   ?   ?   A . n 
A 1 6   PHE 6   6   ?   ?   ?   A . n 
A 1 7   GLU 7   7   ?   ?   ?   A . n 
A 1 8   SER 8   8   ?   ?   ?   A . n 
A 1 9   ASP 9   9   ?   ?   ?   A . n 
A 1 10  LEU 10  10  ?   ?   ?   A . n 
A 1 11  HIS 11  11  ?   ?   ?   A . n 
A 1 12  SER 12  12  ?   ?   ?   A . n 
A 1 13  LEU 13  13  ?   ?   ?   A . n 
A 1 14  LEU 14  14  ?   ?   ?   A . n 
A 1 15  GLN 15  15  ?   ?   ?   A . n 
A 1 16  LEU 16  16  ?   ?   ?   A . n 
A 1 17  ASP 17  17  ?   ?   ?   A . n 
A 1 18  ALA 18  18  ?   ?   ?   A . n 
A 1 19  PRO 19  19  ?   ?   ?   A . n 
A 1 20  ILE 20  20  ?   ?   ?   A . n 
A 1 21  PRO 21  21  ?   ?   ?   A . n 
A 1 22  ASN 22  22  ?   ?   ?   A . n 
A 1 23  ALA 23  23  ?   ?   ?   A . n 
A 1 24  PRO 24  24  ?   ?   ?   A . n 
A 1 25  PRO 25  25  ?   ?   ?   A . n 
A 1 26  ALA 26  26  ?   ?   ?   A . n 
A 1 27  ARG 27  27  ?   ?   ?   A . n 
A 1 28  TRP 28  28  ?   ?   ?   A . n 
A 1 29  GLN 29  29  ?   ?   ?   A . n 
A 1 30  ARG 30  30  ?   ?   ?   A . n 
A 1 31  LYS 31  31  ?   ?   ?   A . n 
A 1 32  ALA 32  32  ?   ?   ?   A . n 
A 1 33  LYS 33  33  ?   ?   ?   A . n 
A 1 34  GLU 34  34  ?   ?   ?   A . n 
A 1 35  ALA 35  35  ?   ?   ?   A . n 
A 1 36  ALA 36  36  ?   ?   ?   A . n 
A 1 37  GLY 37  37  ?   ?   ?   A . n 
A 1 38  PRO 38  38  ?   ?   ?   A . n 
A 1 39  ALA 39  39  ?   ?   ?   A . n 
A 1 40  PRO 40  40  ?   ?   ?   A . n 
A 1 41  SER 41  41  ?   ?   ?   A . n 
A 1 42  PRO 42  42  ?   ?   ?   A . n 
A 1 43  MET 43  43  ?   ?   ?   A . n 
A 1 44  ARG 44  44  ?   ?   ?   A . n 
A 1 45  ALA 45  45  ?   ?   ?   A . n 
A 1 46  ALA 46  46  ?   ?   ?   A . n 
A 1 47  ASN 47  47  ?   ?   ?   A . n 
A 1 48  ARG 48  48  ?   ?   ?   A . n 
A 1 49  SER 49  49  ?   ?   ?   A . n 
A 1 50  HIS 50  50  ?   ?   ?   A . n 
A 1 51  SER 51  51  ?   ?   ?   A . n 
A 1 52  ALA 52  52  ?   ?   ?   A . n 
A 1 53  GLY 53  53  ?   ?   ?   A . n 
A 1 54  ARG 54  54  ?   ?   ?   A . n 
A 1 55  THR 55  55  ?   ?   ?   A . n 
A 1 56  PRO 56  56  ?   ?   ?   A . n 
A 1 57  GLY 57  57  ?   ?   ?   A . n 
A 1 58  ARG 58  58  ?   ?   ?   A . n 
A 1 59  THR 59  59  ?   ?   ?   A . n 
A 1 60  PRO 60  60  ?   ?   ?   A . n 
A 1 61  GLY 61  61  ?   ?   ?   A . n 
A 1 62  LYS 62  62  ?   ?   ?   A . n 
A 1 63  SER 63  63  ?   ?   ?   A . n 
A 1 64  SER 64  64  ?   ?   ?   A . n 
A 1 65  SER 65  65  ?   ?   ?   A . n 
A 1 66  LYS 66  66  ?   ?   ?   A . n 
A 1 67  VAL 67  67  ?   ?   ?   A . n 
A 1 68  GLN 68  68  ?   ?   ?   A . n 
A 1 69  THR 69  69  ?   ?   ?   A . n 
A 1 70  THR 70  70  ?   ?   ?   A . n 
A 1 71  PRO 71  71  ?   ?   ?   A . n 
A 1 72  SER 72  72  ?   ?   ?   A . n 
A 1 73  LYS 73  73  ?   ?   ?   A . n 
A 1 74  PRO 74  74  ?   ?   ?   A . n 
A 1 75  GLY 75  75  ?   ?   ?   A . n 
A 1 76  GLY 76  76  ?   ?   ?   A . n 
A 1 77  ASP 77  77  ?   ?   ?   A . n 
A 1 78  ARG 78  78  ?   ?   ?   A . n 
A 1 79  TYR 79  79  ?   ?   ?   A . n 
A 1 80  ILE 80  80  ?   ?   ?   A . n 
A 1 81  PRO 81  81  ?   ?   ?   A . n 
A 1 82  HIS 82  82  ?   ?   ?   A . n 
A 1 83  ARG 83  83  ?   ?   ?   A . n 
A 1 84  SER 84  84  ?   ?   ?   A . n 
A 1 85  ALA 85  85  ?   ?   ?   A . n 
A 1 86  ALA 86  86  ?   ?   ?   A . n 
A 1 87  GLN 87  87  ?   ?   ?   A . n 
A 1 88  MET 88  88  ?   ?   ?   A . n 
A 1 89  GLU 89  89  ?   ?   ?   A . n 
A 1 90  VAL 90  90  ?   ?   ?   A . n 
A 1 91  ALA 91  91  ?   ?   ?   A . n 
A 1 92  SER 92  92  ?   ?   ?   A . n 
A 1 93  PHE 93  93  ?   ?   ?   A . n 
A 1 94  LEU 94  94  ?   ?   ?   A . n 
A 1 95  LEU 95  95  ?   ?   ?   A . n 
A 1 96  SER 96  96  ?   ?   ?   A . n 
A 1 97  LYS 97  97  ?   ?   ?   A . n 
A 1 98  GLU 98  98  ?   ?   ?   A . n 
A 1 99  ASN 99  99  ?   ?   ?   A . n 
A 1 100 GLN 100 100 ?   ?   ?   A . n 
A 1 101 PRO 101 101 ?   ?   ?   A . n 
A 1 102 GLU 102 102 ?   ?   ?   A . n 
A 1 103 ASN 103 103 ?   ?   ?   A . n 
A 1 104 SER 104 104 ?   ?   ?   A . n 
A 1 105 GLN 105 105 ?   ?   ?   A . n 
A 1 106 THR 106 106 ?   ?   ?   A . n 
A 1 107 PRO 107 107 ?   ?   ?   A . n 
A 1 108 THR 108 108 ?   ?   ?   A . n 
A 1 109 LYS 109 109 ?   ?   ?   A . n 
A 1 110 LYS 110 110 ?   ?   ?   A . n 
A 1 111 GLU 111 111 ?   ?   ?   A . n 
A 1 112 HIS 112 112 ?   ?   ?   A . n 
A 1 113 GLN 113 113 ?   ?   ?   A . n 
A 1 114 LYS 114 114 ?   ?   ?   A . n 
A 1 115 ALA 115 115 ?   ?   ?   A . n 
A 1 116 TRP 116 116 ?   ?   ?   A . n 
A 1 117 ALA 117 117 ?   ?   ?   A . n 
A 1 118 LEU 118 118 ?   ?   ?   A . n 
A 1 119 ASN 119 119 ?   ?   ?   A . n 
A 1 120 LEU 120 120 ?   ?   ?   A . n 
A 1 121 ASN 121 121 ?   ?   ?   A . n 
A 1 122 GLY 122 122 ?   ?   ?   A . n 
A 1 123 PHE 123 123 ?   ?   ?   A . n 
A 1 124 ASP 124 124 ?   ?   ?   A . n 
A 1 125 VAL 125 125 ?   ?   ?   A . n 
A 1 126 GLU 126 126 ?   ?   ?   A . n 
A 1 127 GLU 127 127 ?   ?   ?   A . n 
A 1 128 ALA 128 128 ?   ?   ?   A . n 
A 1 129 LYS 129 129 ?   ?   ?   A . n 
A 1 130 ILE 130 130 ?   ?   ?   A . n 
A 1 131 LEU 131 131 ?   ?   ?   A . n 
A 1 132 ARG 132 132 ?   ?   ?   A . n 
A 1 133 LEU 133 133 ?   ?   ?   A . n 
A 1 134 SER 134 134 ?   ?   ?   A . n 
A 1 135 GLY 135 135 ?   ?   ?   A . n 
A 1 136 LYS 136 136 ?   ?   ?   A . n 
A 1 137 PRO 137 137 ?   ?   ?   A . n 
A 1 138 GLN 138 138 ?   ?   ?   A . n 
A 1 139 ASN 139 139 ?   ?   ?   A . n 
A 1 140 ALA 140 140 ?   ?   ?   A . n 
A 1 141 PRO 141 141 ?   ?   ?   A . n 
A 1 142 GLU 142 142 ?   ?   ?   A . n 
A 1 143 GLY 143 143 ?   ?   ?   A . n 
A 1 144 TYR 144 144 ?   ?   ?   A . n 
A 1 145 GLN 145 145 ?   ?   ?   A . n 
A 1 146 ASN 146 146 ?   ?   ?   A . n 
A 1 147 ARG 147 147 ?   ?   ?   A . n 
A 1 148 LEU 148 148 ?   ?   ?   A . n 
A 1 149 LYS 149 149 ?   ?   ?   A . n 
A 1 150 VAL 150 150 ?   ?   ?   A . n 
A 1 151 LEU 151 151 ?   ?   ?   A . n 
A 1 152 TYR 152 152 ?   ?   ?   A . n 
A 1 153 SER 153 153 ?   ?   ?   A . n 
A 1 154 GLN 154 154 ?   ?   ?   A . n 
A 1 155 LYS 155 155 ?   ?   ?   A . n 
A 1 156 ALA 156 156 ?   ?   ?   A . n 
A 1 157 THR 157 157 ?   ?   ?   A . n 
A 1 158 PRO 158 158 ?   ?   ?   A . n 
A 1 159 GLY 159 159 ?   ?   ?   A . n 
A 1 160 SER 160 160 ?   ?   ?   A . n 
A 1 161 SER 161 161 ?   ?   ?   A . n 
A 1 162 ARG 162 162 ?   ?   ?   A . n 
A 1 163 LYS 163 163 ?   ?   ?   A . n 
A 1 164 THR 164 164 ?   ?   ?   A . n 
A 1 165 CYS 165 165 ?   ?   ?   A . n 
A 1 166 ARG 166 166 166 ARG ARG A . n 
A 1 167 TYR 167 167 167 TYR TYR A . n 
A 1 168 ILE 168 168 168 ILE ILE A . n 
A 1 169 PRO 169 169 169 PRO PRO A . n 
A 1 170 SER 170 170 170 SER SER A . n 
A 1 171 LEU 171 171 171 LEU LEU A . n 
A 1 172 PRO 172 172 172 PRO PRO A . n 
A 1 173 ASP 173 173 173 ASP ASP A . n 
A 1 174 ARG 174 174 174 ARG ARG A . n 
A 1 175 ILE 175 175 175 ILE ILE A . n 
A 1 176 LEU 176 176 176 LEU LEU A . n 
A 1 177 ASP 177 177 177 ASP ASP A . n 
A 1 178 ALA 178 178 178 ALA ALA A . n 
A 1 179 PRO 179 179 179 PRO PRO A . n 
A 1 180 GLU 180 180 180 GLU GLU A . n 
A 1 181 ILE 181 181 181 ILE ILE A . n 
A 1 182 ARG 182 182 182 ARG ARG A . n 
A 1 183 ASN 183 183 183 ASN ASN A . n 
A 1 184 ASP 184 184 184 ASP ASP A . n 
A 1 185 TYR 185 185 185 TYR TYR A . n 
A 1 186 TYR 186 186 186 TYR TYR A . n 
A 1 187 LEU 187 187 187 LEU LEU A . n 
A 1 188 ASN 188 188 188 ASN ASN A . n 
A 1 189 LEU 189 189 189 LEU LEU A . n 
A 1 190 VAL 190 190 190 VAL VAL A . n 
A 1 191 ASP 191 191 191 ASP ASP A . n 
A 1 192 TRP 192 192 192 TRP TRP A . n 
A 1 193 SER 193 193 193 SER SER A . n 
A 1 194 SER 194 194 194 SER SER A . n 
A 1 195 GLY 195 195 195 GLY GLY A . n 
A 1 196 ASN 196 196 196 ASN ASN A . n 
A 1 197 VAL 197 197 197 VAL VAL A . n 
A 1 198 LEU 198 198 198 LEU LEU A . n 
A 1 199 ALA 199 199 199 ALA ALA A . n 
A 1 200 VAL 200 200 200 VAL VAL A . n 
A 1 201 ALA 201 201 201 ALA ALA A . n 
A 1 202 LEU 202 202 202 LEU LEU A . n 
A 1 203 ASP 203 203 203 ASP ASP A . n 
A 1 204 ASN 204 204 204 ASN ASN A . n 
A 1 205 SER 205 205 205 SER SER A . n 
A 1 206 VAL 206 206 206 VAL VAL A . n 
A 1 207 TYR 207 207 207 TYR TYR A . n 
A 1 208 LEU 208 208 208 LEU LEU A . n 
A 1 209 TRP 209 209 209 TRP TRP A . n 
A 1 210 SER 210 210 210 SER SER A . n 
A 1 211 ALA 211 211 211 ALA ALA A . n 
A 1 212 SER 212 212 212 SER SER A . n 
A 1 213 SER 213 213 213 SER SER A . n 
A 1 214 GLY 214 214 214 GLY GLY A . n 
A 1 215 ASP 215 215 215 ASP ASP A . n 
A 1 216 ILE 216 216 216 ILE ILE A . n 
A 1 217 LEU 217 217 217 LEU LEU A . n 
A 1 218 GLN 218 218 218 GLN GLN A . n 
A 1 219 LEU 219 219 219 LEU LEU A . n 
A 1 220 LEU 220 220 220 LEU LEU A . n 
A 1 221 GLN 221 221 221 GLN GLN A . n 
A 1 222 MET 222 222 222 MET MET A . n 
A 1 223 GLU 223 223 223 GLU GLU A . n 
A 1 224 GLN 224 224 224 GLN GLN A . n 
A 1 225 PRO 225 225 225 PRO PRO A . n 
A 1 226 GLY 226 226 226 GLY GLY A . n 
A 1 227 GLU 227 227 227 GLU GLU A . n 
A 1 228 TYR 228 228 228 TYR TYR A . n 
A 1 229 ILE 229 229 229 ILE ILE A . n 
A 1 230 SER 230 230 230 SER SER A . n 
A 1 231 SER 231 231 231 SER SER A . n 
A 1 232 VAL 232 232 232 VAL VAL A . n 
A 1 233 ALA 233 233 233 ALA ALA A . n 
A 1 234 TRP 234 234 234 TRP TRP A . n 
A 1 235 ILE 235 235 235 ILE ILE A . n 
A 1 236 LYS 236 236 236 LYS LYS A . n 
A 1 237 GLU 237 237 237 GLU GLU A . n 
A 1 238 GLY 238 238 238 GLY GLY A . n 
A 1 239 ASN 239 239 239 ASN ASN A . n 
A 1 240 TYR 240 240 240 TYR TYR A . n 
A 1 241 LEU 241 241 241 LEU LEU A . n 
A 1 242 ALA 242 242 242 ALA ALA A . n 
A 1 243 VAL 243 243 243 VAL VAL A . n 
A 1 244 GLY 244 244 244 GLY GLY A . n 
A 1 245 THR 245 245 245 THR THR A . n 
A 1 246 SER 246 246 246 SER SER A . n 
A 1 247 SER 247 247 247 SER SER A . n 
A 1 248 ALA 248 248 248 ALA ALA A . n 
A 1 249 GLU 249 249 249 GLU GLU A . n 
A 1 250 VAL 250 250 250 VAL VAL A . n 
A 1 251 GLN 251 251 251 GLN GLN A . n 
A 1 252 LEU 252 252 252 LEU LEU A . n 
A 1 253 TRP 253 253 253 TRP TRP A . n 
A 1 254 ASP 254 254 254 ASP ASP A . n 
A 1 255 VAL 255 255 255 VAL VAL A . n 
A 1 256 GLN 256 256 256 GLN GLN A . n 
A 1 257 GLN 257 257 257 GLN GLN A . n 
A 1 258 GLN 258 258 258 GLN GLN A . n 
A 1 259 LYS 259 259 259 LYS LYS A . n 
A 1 260 ARG 260 260 260 ARG ARG A . n 
A 1 261 LEU 261 261 261 LEU LEU A . n 
A 1 262 ARG 262 262 262 ARG ARG A . n 
A 1 263 ASN 263 263 263 ASN ASN A . n 
A 1 264 MET 264 264 264 MET MET A . n 
A 1 265 THR 265 265 265 THR THR A . n 
A 1 266 SER 266 266 266 SER SER A . n 
A 1 267 HIS 267 267 267 HIS HIS A . n 
A 1 268 SER 268 268 268 SER SER A . n 
A 1 269 ALA 269 269 269 ALA ALA A . n 
A 1 270 ARG 270 270 270 ARG ARG A . n 
A 1 271 VAL 271 271 271 VAL VAL A . n 
A 1 272 GLY 272 272 272 GLY GLY A . n 
A 1 273 SER 273 273 273 SER SER A . n 
A 1 274 LEU 274 274 274 LEU LEU A . n 
A 1 275 SER 275 275 275 SER SER A . n 
A 1 276 TRP 276 276 276 TRP TRP A . n 
A 1 277 ASN 277 277 277 ASN ASN A . n 
A 1 278 SER 278 278 278 SER SER A . n 
A 1 279 TYR 279 279 279 TYR TYR A . n 
A 1 280 ILE 280 280 280 ILE ILE A . n 
A 1 281 LEU 281 281 281 LEU LEU A . n 
A 1 282 SER 282 282 282 SER SER A . n 
A 1 283 SER 283 283 283 SER SER A . n 
A 1 284 GLY 284 284 284 GLY GLY A . n 
A 1 285 SER 285 285 285 SER SER A . n 
A 1 286 ARG 286 286 286 ARG ARG A . n 
A 1 287 SER 287 287 287 SER SER A . n 
A 1 288 GLY 288 288 288 GLY GLY A . n 
A 1 289 HIS 289 289 289 HIS HIS A . n 
A 1 290 ILE 290 290 290 ILE ILE A . n 
A 1 291 HIS 291 291 291 HIS HIS A . n 
A 1 292 HIS 292 292 292 HIS HIS A . n 
A 1 293 HIS 293 293 293 HIS HIS A . n 
A 1 294 ASP 294 294 294 ASP ASP A . n 
A 1 295 VAL 295 295 295 VAL VAL A . n 
A 1 296 ARG 296 296 296 ARG ARG A . n 
A 1 297 VAL 297 297 297 VAL VAL A . n 
A 1 298 ALA 298 298 298 ALA ALA A . n 
A 1 299 GLU 299 299 299 GLU GLU A . n 
A 1 300 HIS 300 300 300 HIS HIS A . n 
A 1 301 HIS 301 301 301 HIS HIS A . n 
A 1 302 VAL 302 302 302 VAL VAL A . n 
A 1 303 ALA 303 303 303 ALA ALA A . n 
A 1 304 THR 304 304 304 THR THR A . n 
A 1 305 LEU 305 305 305 LEU LEU A . n 
A 1 306 SER 306 306 306 SER SER A . n 
A 1 307 GLY 307 307 307 GLY GLY A . n 
A 1 308 HIS 308 308 308 HIS HIS A . n 
A 1 309 SER 309 309 309 SER SER A . n 
A 1 310 GLN 310 310 310 GLN GLN A . n 
A 1 311 GLU 311 311 311 GLU GLU A . n 
A 1 312 VAL 312 312 312 VAL VAL A . n 
A 1 313 CYS 313 313 313 CYS CYS A . n 
A 1 314 GLY 314 314 314 GLY GLY A . n 
A 1 315 LEU 315 315 315 LEU LEU A . n 
A 1 316 ARG 316 316 316 ARG ARG A . n 
A 1 317 TRP 317 317 317 TRP TRP A . n 
A 1 318 ALA 318 318 318 ALA ALA A . n 
A 1 319 PRO 319 319 319 PRO PRO A . n 
A 1 320 ASP 320 320 320 ASP ASP A . n 
A 1 321 GLY 321 321 321 GLY GLY A . n 
A 1 322 ARG 322 322 322 ARG ARG A . n 
A 1 323 HIS 323 323 323 HIS HIS A . n 
A 1 324 LEU 324 324 324 LEU LEU A . n 
A 1 325 ALA 325 325 325 ALA ALA A . n 
A 1 326 SER 326 326 326 SER SER A . n 
A 1 327 GLY 327 327 327 GLY GLY A . n 
A 1 328 GLY 328 328 328 GLY GLY A . n 
A 1 329 ASN 329 329 329 ASN ASN A . n 
A 1 330 ASP 330 330 330 ASP ASP A . n 
A 1 331 ASN 331 331 331 ASN ASN A . n 
A 1 332 LEU 332 332 332 LEU LEU A . n 
A 1 333 VAL 333 333 333 VAL VAL A . n 
A 1 334 ASN 334 334 334 ASN ASN A . n 
A 1 335 VAL 335 335 335 VAL VAL A . n 
A 1 336 TRP 336 336 336 TRP TRP A . n 
A 1 337 PRO 337 337 337 PRO PRO A . n 
A 1 338 SER 338 338 338 SER SER A . n 
A 1 339 ALA 339 339 339 ALA ALA A . n 
A 1 340 PRO 340 340 340 PRO PRO A . n 
A 1 341 GLY 341 341 341 GLY GLY A . n 
A 1 342 GLU 342 342 342 GLU GLU A . n 
A 1 343 GLY 343 343 343 GLY GLY A . n 
A 1 344 GLY 344 344 344 GLY GLY A . n 
A 1 345 TRP 345 345 345 TRP TRP A . n 
A 1 346 VAL 346 346 346 VAL VAL A . n 
A 1 347 PRO 347 347 347 PRO PRO A . n 
A 1 348 LEU 348 348 348 LEU LEU A . n 
A 1 349 GLN 349 349 349 GLN GLN A . n 
A 1 350 THR 350 350 350 THR THR A . n 
A 1 351 PHE 351 351 351 PHE PHE A . n 
A 1 352 THR 352 352 352 THR THR A . n 
A 1 353 GLN 353 353 353 GLN GLN A . n 
A 1 354 HIS 354 354 354 HIS HIS A . n 
A 1 355 GLN 355 355 355 GLN GLN A . n 
A 1 356 GLY 356 356 356 GLY GLY A . n 
A 1 357 ALA 357 357 357 ALA ALA A . n 
A 1 358 VAL 358 358 358 VAL VAL A . n 
A 1 359 LYS 359 359 359 LYS LYS A . n 
A 1 360 ALA 360 360 360 ALA ALA A . n 
A 1 361 VAL 361 361 361 VAL VAL A . n 
A 1 362 ALA 362 362 362 ALA ALA A . n 
A 1 363 TRP 363 363 363 TRP TRP A . n 
A 1 364 CYS 364 364 364 CYS CYS A . n 
A 1 365 PRO 365 365 365 PRO PRO A . n 
A 1 366 TRP 366 366 366 TRP TRP A . n 
A 1 367 GLN 367 367 367 GLN GLN A . n 
A 1 368 SER 368 368 368 SER SER A . n 
A 1 369 ASN 369 369 369 ASN ASN A . n 
A 1 370 VAL 370 370 370 VAL VAL A . n 
A 1 371 LEU 371 371 371 LEU LEU A . n 
A 1 372 ALA 372 372 372 ALA ALA A . n 
A 1 373 THR 373 373 373 THR THR A . n 
A 1 374 GLY 374 374 374 GLY GLY A . n 
A 1 375 GLY 375 375 375 GLY GLY A . n 
A 1 376 GLY 376 376 376 GLY GLY A . n 
A 1 377 THR 377 377 377 THR THR A . n 
A 1 378 SER 378 378 378 SER SER A . n 
A 1 379 ASP 379 379 379 ASP ASP A . n 
A 1 380 ARG 380 380 380 ARG ARG A . n 
A 1 381 HIS 381 381 381 HIS HIS A . n 
A 1 382 ILE 382 382 382 ILE ILE A . n 
A 1 383 ARG 383 383 383 ARG ARG A . n 
A 1 384 ILE 384 384 384 ILE ILE A . n 
A 1 385 TRP 385 385 385 TRP TRP A . n 
A 1 386 ASN 386 386 386 ASN ASN A . n 
A 1 387 VAL 387 387 387 VAL VAL A . n 
A 1 388 CYS 388 388 388 CYS CYS A . n 
A 1 389 SER 389 389 389 SER SER A . n 
A 1 390 GLY 390 390 390 GLY GLY A . n 
A 1 391 ALA 391 391 391 ALA ALA A . n 
A 1 392 CYS 392 392 392 CYS CYS A . n 
A 1 393 LEU 393 393 393 LEU LEU A . n 
A 1 394 SER 394 394 394 SER SER A . n 
A 1 395 ALA 395 395 395 ALA ALA A . n 
A 1 396 VAL 396 396 396 VAL VAL A . n 
A 1 397 ASP 397 397 397 ASP ASP A . n 
A 1 398 ALA 398 398 398 ALA ALA A . n 
A 1 399 HIS 399 399 399 HIS HIS A . n 
A 1 400 SER 400 400 400 SER SER A . n 
A 1 401 GLN 401 401 401 GLN GLN A . n 
A 1 402 VAL 402 402 402 VAL VAL A . n 
A 1 403 CYS 403 403 403 CYS CYS A . n 
A 1 404 SER 404 404 404 SER SER A . n 
A 1 405 ILE 405 405 405 ILE ILE A . n 
A 1 406 LEU 406 406 406 LEU LEU A . n 
A 1 407 TRP 407 407 407 TRP TRP A . n 
A 1 408 SER 408 408 408 SER SER A . n 
A 1 409 PRO 409 409 409 PRO PRO A . n 
A 1 410 HIS 410 410 410 HIS HIS A . n 
A 1 411 TYR 411 411 411 TYR TYR A . n 
A 1 412 LYS 412 412 412 LYS LYS A . n 
A 1 413 GLU 413 413 413 GLU GLU A . n 
A 1 414 LEU 414 414 414 LEU LEU A . n 
A 1 415 ILE 415 415 415 ILE ILE A . n 
A 1 416 SER 416 416 416 SER SER A . n 
A 1 417 GLY 417 417 417 GLY GLY A . n 
A 1 418 HIS 418 418 418 HIS HIS A . n 
A 1 419 GLY 419 419 419 GLY GLY A . n 
A 1 420 PHE 420 420 420 PHE PHE A . n 
A 1 421 ALA 421 421 421 ALA ALA A . n 
A 1 422 GLN 422 422 422 GLN GLN A . n 
A 1 423 ASN 423 423 423 ASN ASN A . n 
A 1 424 GLN 424 424 424 GLN GLN A . n 
A 1 425 LEU 425 425 425 LEU LEU A . n 
A 1 426 VAL 426 426 426 VAL VAL A . n 
A 1 427 ILE 427 427 427 ILE ILE A . n 
A 1 428 TRP 428 428 428 TRP TRP A . n 
A 1 429 LYS 429 429 429 LYS LYS A . n 
A 1 430 TYR 430 430 430 TYR TYR A . n 
A 1 431 PRO 431 431 431 PRO PRO A . n 
A 1 432 THR 432 432 432 THR THR A . n 
A 1 433 MET 433 433 433 MET MET A . n 
A 1 434 ALA 434 434 434 ALA ALA A . n 
A 1 435 LYS 435 435 435 LYS LYS A . n 
A 1 436 VAL 436 436 436 VAL VAL A . n 
A 1 437 ALA 437 437 437 ALA ALA A . n 
A 1 438 GLU 438 438 438 GLU GLU A . n 
A 1 439 LEU 439 439 439 LEU LEU A . n 
A 1 440 LYS 440 440 440 LYS LYS A . n 
A 1 441 GLY 441 441 441 GLY GLY A . n 
A 1 442 HIS 442 442 442 HIS HIS A . n 
A 1 443 THR 443 443 443 THR THR A . n 
A 1 444 SER 444 444 444 SER SER A . n 
A 1 445 ARG 445 445 445 ARG ARG A . n 
A 1 446 VAL 446 446 446 VAL VAL A . n 
A 1 447 LEU 447 447 447 LEU LEU A . n 
A 1 448 SER 448 448 448 SER SER A . n 
A 1 449 LEU 449 449 449 LEU LEU A . n 
A 1 450 THR 450 450 450 THR THR A . n 
A 1 451 MET 451 451 451 MET MET A . n 
A 1 452 SER 452 452 452 SER SER A . n 
A 1 453 PRO 453 453 453 PRO PRO A . n 
A 1 454 ASP 454 454 454 ASP ASP A . n 
A 1 455 GLY 455 455 455 GLY GLY A . n 
A 1 456 ALA 456 456 456 ALA ALA A . n 
A 1 457 THR 457 457 457 THR THR A . n 
A 1 458 VAL 458 458 458 VAL VAL A . n 
A 1 459 ALA 459 459 459 ALA ALA A . n 
A 1 460 SER 460 460 460 SER SER A . n 
A 1 461 ALA 461 461 461 ALA ALA A . n 
A 1 462 ALA 462 462 462 ALA ALA A . n 
A 1 463 ALA 463 463 463 ALA ALA A . n 
A 1 464 ASP 464 464 464 ASP ASP A . n 
A 1 465 GLU 465 465 465 GLU GLU A . n 
A 1 466 THR 466 466 466 THR THR A . n 
A 1 467 LEU 467 467 467 LEU LEU A . n 
A 1 468 ARG 468 468 468 ARG ARG A . n 
A 1 469 LEU 469 469 469 LEU LEU A . n 
A 1 470 TRP 470 470 470 TRP TRP A . n 
A 1 471 ARG 471 471 471 ARG ARG A . n 
A 1 472 CYS 472 472 472 CYS CYS A . n 
A 1 473 PHE 473 473 473 PHE PHE A . n 
A 1 474 GLU 474 474 474 GLU GLU A . n 
A 1 475 LEU 475 475 475 LEU LEU A . n 
A 1 476 ASP 476 476 476 ASP ASP A . n 
A 1 477 PRO 477 477 ?   ?   ?   A . n 
A 1 478 ALA 478 478 ?   ?   ?   A . n 
A 1 479 ARG 479 479 ?   ?   ?   A . n 
A 1 480 ARG 480 480 ?   ?   ?   A . n 
A 1 481 ARG 481 481 ?   ?   ?   A . n 
A 1 482 GLU 482 482 ?   ?   ?   A . n 
A 1 483 ARG 483 483 ?   ?   ?   A . n 
A 1 484 GLU 484 484 ?   ?   ?   A . n 
A 1 485 LYS 485 485 ?   ?   ?   A . n 
A 1 486 ALA 486 486 ?   ?   ?   A . n 
A 1 487 SER 487 487 ?   ?   ?   A . n 
A 1 488 ALA 488 488 ?   ?   ?   A . n 
A 1 489 ALA 489 489 ?   ?   ?   A . n 
A 1 490 LYS 490 490 ?   ?   ?   A . n 
A 1 491 SER 491 491 ?   ?   ?   A . n 
A 1 492 SER 492 492 ?   ?   ?   A . n 
A 1 493 LEU 493 493 ?   ?   ?   A . n 
A 1 494 ILE 494 494 ?   ?   ?   A . n 
A 1 495 HIS 495 495 ?   ?   ?   A . n 
A 1 496 GLN 496 496 ?   ?   ?   A . n 
A 1 497 GLY 497 497 ?   ?   ?   A . n 
A 1 498 ILE 498 498 ?   ?   ?   A . n 
A 1 499 ARG 499 499 ?   ?   ?   A . n 
B 2 1   ARG 1   1   1   ARG ARG B . n 
B 2 2   ALA 2   2   2   ALA ALA B . n 
B 2 3   PRO 3   3   3   PRO PRO B . n 
B 2 4   0JY 4   4   4   0JY 0JY B . n 
B 2 5   SER 5   5   5   SER SER B . n 
B 2 6   ASP 6   6   6   ASP ASP B . n 
B 2 7   ILE 7   7   ?   ?   ?   B . n 
B 2 8   THR 8   8   ?   ?   ?   B . n 
B 2 9   ASN 9   9   ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        0JY 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   0JY 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 HOH 1   501 104 HOH HOH A . 
C 3 HOH 2   502 117 HOH HOH A . 
C 3 HOH 3   503 52  HOH HOH A . 
C 3 HOH 4   504 224 HOH HOH A . 
C 3 HOH 5   505 103 HOH HOH A . 
C 3 HOH 6   506 193 HOH HOH A . 
C 3 HOH 7   507 39  HOH HOH A . 
C 3 HOH 8   508 40  HOH HOH A . 
C 3 HOH 9   509 68  HOH HOH A . 
C 3 HOH 10  510 222 HOH HOH A . 
C 3 HOH 11  511 98  HOH HOH A . 
C 3 HOH 12  512 230 HOH HOH A . 
C 3 HOH 13  513 236 HOH HOH A . 
C 3 HOH 14  514 82  HOH HOH A . 
C 3 HOH 15  515 85  HOH HOH A . 
C 3 HOH 16  516 223 HOH HOH A . 
C 3 HOH 17  517 112 HOH HOH A . 
C 3 HOH 18  518 83  HOH HOH A . 
C 3 HOH 19  519 30  HOH HOH A . 
C 3 HOH 20  520 90  HOH HOH A . 
C 3 HOH 21  521 227 HOH HOH A . 
C 3 HOH 22  522 99  HOH HOH A . 
C 3 HOH 23  523 37  HOH HOH A . 
C 3 HOH 24  524 75  HOH HOH A . 
C 3 HOH 25  525 77  HOH HOH A . 
C 3 HOH 26  526 228 HOH HOH A . 
C 3 HOH 27  527 94  HOH HOH A . 
C 3 HOH 28  528 23  HOH HOH A . 
C 3 HOH 29  529 28  HOH HOH A . 
C 3 HOH 30  530 226 HOH HOH A . 
C 3 HOH 31  531 91  HOH HOH A . 
C 3 HOH 32  532 157 HOH HOH A . 
C 3 HOH 33  533 2   HOH HOH A . 
C 3 HOH 34  534 17  HOH HOH A . 
C 3 HOH 35  535 62  HOH HOH A . 
C 3 HOH 36  536 18  HOH HOH A . 
C 3 HOH 37  537 158 HOH HOH A . 
C 3 HOH 38  538 13  HOH HOH A . 
C 3 HOH 39  539 61  HOH HOH A . 
C 3 HOH 40  540 32  HOH HOH A . 
C 3 HOH 41  541 51  HOH HOH A . 
C 3 HOH 42  542 231 HOH HOH A . 
C 3 HOH 43  543 92  HOH HOH A . 
C 3 HOH 44  544 166 HOH HOH A . 
C 3 HOH 45  545 218 HOH HOH A . 
C 3 HOH 46  546 47  HOH HOH A . 
C 3 HOH 47  547 113 HOH HOH A . 
C 3 HOH 48  548 205 HOH HOH A . 
C 3 HOH 49  549 26  HOH HOH A . 
C 3 HOH 50  550 170 HOH HOH A . 
C 3 HOH 51  551 194 HOH HOH A . 
C 3 HOH 52  552 139 HOH HOH A . 
C 3 HOH 53  553 43  HOH HOH A . 
C 3 HOH 54  554 182 HOH HOH A . 
C 3 HOH 55  555 219 HOH HOH A . 
C 3 HOH 56  556 29  HOH HOH A . 
C 3 HOH 57  557 147 HOH HOH A . 
C 3 HOH 58  558 12  HOH HOH A . 
C 3 HOH 59  559 221 HOH HOH A . 
C 3 HOH 60  560 63  HOH HOH A . 
C 3 HOH 61  561 42  HOH HOH A . 
C 3 HOH 62  562 35  HOH HOH A . 
C 3 HOH 63  563 239 HOH HOH A . 
C 3 HOH 64  564 160 HOH HOH A . 
C 3 HOH 65  565 10  HOH HOH A . 
C 3 HOH 66  566 9   HOH HOH A . 
C 3 HOH 67  567 33  HOH HOH A . 
C 3 HOH 68  568 67  HOH HOH A . 
C 3 HOH 69  569 84  HOH HOH A . 
C 3 HOH 70  570 167 HOH HOH A . 
C 3 HOH 71  571 48  HOH HOH A . 
C 3 HOH 72  572 133 HOH HOH A . 
C 3 HOH 73  573 89  HOH HOH A . 
C 3 HOH 74  574 1   HOH HOH A . 
C 3 HOH 75  575 124 HOH HOH A . 
C 3 HOH 76  576 5   HOH HOH A . 
C 3 HOH 77  577 141 HOH HOH A . 
C 3 HOH 78  578 3   HOH HOH A . 
C 3 HOH 79  579 11  HOH HOH A . 
C 3 HOH 80  580 55  HOH HOH A . 
C 3 HOH 81  581 153 HOH HOH A . 
C 3 HOH 82  582 142 HOH HOH A . 
C 3 HOH 83  583 46  HOH HOH A . 
C 3 HOH 84  584 118 HOH HOH A . 
C 3 HOH 85  585 14  HOH HOH A . 
C 3 HOH 86  586 197 HOH HOH A . 
C 3 HOH 87  587 24  HOH HOH A . 
C 3 HOH 88  588 191 HOH HOH A . 
C 3 HOH 89  589 57  HOH HOH A . 
C 3 HOH 90  590 111 HOH HOH A . 
C 3 HOH 91  591 233 HOH HOH A . 
C 3 HOH 92  592 19  HOH HOH A . 
C 3 HOH 93  593 129 HOH HOH A . 
C 3 HOH 94  594 168 HOH HOH A . 
C 3 HOH 95  595 27  HOH HOH A . 
C 3 HOH 96  596 81  HOH HOH A . 
C 3 HOH 97  597 120 HOH HOH A . 
C 3 HOH 98  598 176 HOH HOH A . 
C 3 HOH 99  599 95  HOH HOH A . 
C 3 HOH 100 600 143 HOH HOH A . 
C 3 HOH 101 601 54  HOH HOH A . 
C 3 HOH 102 602 101 HOH HOH A . 
C 3 HOH 103 603 126 HOH HOH A . 
C 3 HOH 104 604 105 HOH HOH A . 
C 3 HOH 105 605 20  HOH HOH A . 
C 3 HOH 106 606 60  HOH HOH A . 
C 3 HOH 107 607 177 HOH HOH A . 
C 3 HOH 108 608 235 HOH HOH A . 
C 3 HOH 109 609 116 HOH HOH A . 
C 3 HOH 110 610 97  HOH HOH A . 
C 3 HOH 111 611 22  HOH HOH A . 
C 3 HOH 112 612 196 HOH HOH A . 
C 3 HOH 113 613 36  HOH HOH A . 
C 3 HOH 114 614 181 HOH HOH A . 
C 3 HOH 115 615 34  HOH HOH A . 
C 3 HOH 116 616 183 HOH HOH A . 
C 3 HOH 117 617 119 HOH HOH A . 
C 3 HOH 118 618 93  HOH HOH A . 
C 3 HOH 119 619 155 HOH HOH A . 
C 3 HOH 120 620 66  HOH HOH A . 
C 3 HOH 121 621 122 HOH HOH A . 
C 3 HOH 122 622 195 HOH HOH A . 
C 3 HOH 123 623 71  HOH HOH A . 
C 3 HOH 124 624 121 HOH HOH A . 
C 3 HOH 125 625 45  HOH HOH A . 
C 3 HOH 126 626 8   HOH HOH A . 
C 3 HOH 127 627 225 HOH HOH A . 
C 3 HOH 128 628 165 HOH HOH A . 
C 3 HOH 129 629 53  HOH HOH A . 
C 3 HOH 130 630 38  HOH HOH A . 
C 3 HOH 131 631 212 HOH HOH A . 
C 3 HOH 132 632 130 HOH HOH A . 
C 3 HOH 133 633 25  HOH HOH A . 
C 3 HOH 134 634 41  HOH HOH A . 
C 3 HOH 135 635 7   HOH HOH A . 
C 3 HOH 136 636 206 HOH HOH A . 
C 3 HOH 137 637 192 HOH HOH A . 
C 3 HOH 138 638 238 HOH HOH A . 
C 3 HOH 139 639 70  HOH HOH A . 
C 3 HOH 140 640 86  HOH HOH A . 
C 3 HOH 141 641 217 HOH HOH A . 
C 3 HOH 142 642 159 HOH HOH A . 
C 3 HOH 143 643 138 HOH HOH A . 
C 3 HOH 144 644 185 HOH HOH A . 
C 3 HOH 145 645 135 HOH HOH A . 
C 3 HOH 146 646 172 HOH HOH A . 
C 3 HOH 147 647 189 HOH HOH A . 
C 3 HOH 148 648 148 HOH HOH A . 
C 3 HOH 149 649 58  HOH HOH A . 
C 3 HOH 150 650 128 HOH HOH A . 
C 3 HOH 151 651 140 HOH HOH A . 
C 3 HOH 152 652 144 HOH HOH A . 
C 3 HOH 153 653 16  HOH HOH A . 
C 3 HOH 154 654 171 HOH HOH A . 
C 3 HOH 155 655 184 HOH HOH A . 
C 3 HOH 156 656 6   HOH HOH A . 
C 3 HOH 157 657 15  HOH HOH A . 
C 3 HOH 158 658 50  HOH HOH A . 
C 3 HOH 159 659 76  HOH HOH A . 
C 3 HOH 160 660 56  HOH HOH A . 
C 3 HOH 161 661 234 HOH HOH A . 
C 3 HOH 162 662 179 HOH HOH A . 
C 3 HOH 163 663 201 HOH HOH A . 
C 3 HOH 164 664 229 HOH HOH A . 
C 3 HOH 165 665 88  HOH HOH A . 
C 3 HOH 166 666 106 HOH HOH A . 
C 3 HOH 167 667 202 HOH HOH A . 
C 3 HOH 168 668 109 HOH HOH A . 
C 3 HOH 169 669 190 HOH HOH A . 
C 3 HOH 170 670 65  HOH HOH A . 
C 3 HOH 171 671 100 HOH HOH A . 
C 3 HOH 172 672 188 HOH HOH A . 
C 3 HOH 173 673 31  HOH HOH A . 
C 3 HOH 174 674 237 HOH HOH A . 
C 3 HOH 175 675 73  HOH HOH A . 
C 3 HOH 176 676 186 HOH HOH A . 
C 3 HOH 177 677 199 HOH HOH A . 
C 3 HOH 178 678 110 HOH HOH A . 
C 3 HOH 179 679 64  HOH HOH A . 
C 3 HOH 180 680 132 HOH HOH A . 
C 3 HOH 181 681 96  HOH HOH A . 
C 3 HOH 182 682 21  HOH HOH A . 
C 3 HOH 183 683 4   HOH HOH A . 
C 3 HOH 184 684 162 HOH HOH A . 
C 3 HOH 185 685 211 HOH HOH A . 
C 3 HOH 186 686 200 HOH HOH A . 
C 3 HOH 187 687 136 HOH HOH A . 
C 3 HOH 188 688 72  HOH HOH A . 
C 3 HOH 189 689 114 HOH HOH A . 
C 3 HOH 190 690 107 HOH HOH A . 
C 3 HOH 191 691 163 HOH HOH A . 
C 3 HOH 192 692 123 HOH HOH A . 
C 3 HOH 193 693 59  HOH HOH A . 
C 3 HOH 194 694 80  HOH HOH A . 
C 3 HOH 195 695 207 HOH HOH A . 
C 3 HOH 196 696 69  HOH HOH A . 
C 3 HOH 197 697 134 HOH HOH A . 
C 3 HOH 198 698 49  HOH HOH A . 
C 3 HOH 199 699 44  HOH HOH A . 
C 3 HOH 200 700 214 HOH HOH A . 
C 3 HOH 201 701 216 HOH HOH A . 
C 3 HOH 202 702 169 HOH HOH A . 
C 3 HOH 203 703 204 HOH HOH A . 
C 3 HOH 204 704 125 HOH HOH A . 
C 3 HOH 205 705 152 HOH HOH A . 
C 3 HOH 206 706 131 HOH HOH A . 
C 3 HOH 207 707 173 HOH HOH A . 
C 3 HOH 208 708 198 HOH HOH A . 
C 3 HOH 209 709 74  HOH HOH A . 
C 3 HOH 210 710 164 HOH HOH A . 
C 3 HOH 211 711 102 HOH HOH A . 
C 3 HOH 212 712 180 HOH HOH A . 
C 3 HOH 213 713 215 HOH HOH A . 
C 3 HOH 214 714 150 HOH HOH A . 
C 3 HOH 215 715 187 HOH HOH A . 
C 3 HOH 216 716 78  HOH HOH A . 
C 3 HOH 217 717 203 HOH HOH A . 
C 3 HOH 218 718 213 HOH HOH A . 
C 3 HOH 219 719 137 HOH HOH A . 
C 3 HOH 220 720 115 HOH HOH A . 
C 3 HOH 221 721 220 HOH HOH A . 
C 3 HOH 222 722 79  HOH HOH A . 
C 3 HOH 223 723 156 HOH HOH A . 
C 3 HOH 224 724 127 HOH HOH A . 
C 3 HOH 225 725 151 HOH HOH A . 
C 3 HOH 226 726 154 HOH HOH A . 
C 3 HOH 227 727 209 HOH HOH A . 
C 3 HOH 228 728 108 HOH HOH A . 
C 3 HOH 229 729 240 HOH HOH A . 
C 3 HOH 230 730 210 HOH HOH A . 
C 3 HOH 231 731 145 HOH HOH A . 
C 3 HOH 232 732 178 HOH HOH A . 
C 3 HOH 233 733 146 HOH HOH A . 
C 3 HOH 234 734 149 HOH HOH A . 
C 3 HOH 235 735 174 HOH HOH A . 
C 3 HOH 236 736 232 HOH HOH A . 
C 3 HOH 237 737 208 HOH HOH A . 
C 3 HOH 238 738 161 HOH HOH A . 
D 3 HOH 1   101 87  HOH HOH B . 
D 3 HOH 2   102 175 HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 236 ? CG  ? A LYS 236 CG  
2  1 Y 1 A LYS 236 ? CD  ? A LYS 236 CD  
3  1 Y 1 A LYS 236 ? CE  ? A LYS 236 CE  
4  1 Y 1 A LYS 236 ? NZ  ? A LYS 236 NZ  
5  1 Y 1 A GLU 237 ? CG  ? A GLU 237 CG  
6  1 Y 1 A GLU 237 ? CD  ? A GLU 237 CD  
7  1 Y 1 A GLU 237 ? OE1 ? A GLU 237 OE1 
8  1 Y 1 A GLU 237 ? OE2 ? A GLU 237 OE2 
9  1 Y 1 A GLN 256 ? CG  ? A GLN 256 CG  
10 1 Y 1 A GLN 256 ? CD  ? A GLN 256 CD  
11 1 Y 1 A GLN 256 ? OE1 ? A GLN 256 OE1 
12 1 Y 1 A GLN 256 ? NE2 ? A GLN 256 NE2 
13 1 Y 1 A GLU 299 ? CG  ? A GLU 299 CG  
14 1 Y 1 A GLU 299 ? CD  ? A GLU 299 CD  
15 1 Y 1 A GLU 299 ? OE1 ? A GLU 299 OE1 
16 1 Y 1 A GLU 299 ? OE2 ? A GLU 299 OE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? BUSTER  ? ? ? '2.10.3 (20-MAY-2020)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                      2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .                      3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .                      4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   110.14 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9I69 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     35.339 
_cell.length_a_esd                 ? 
_cell.length_b                     87.341 
_cell.length_b_esd                 ? 
_cell.length_c                     48.511 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        2 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9I69 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9I69 
_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             ? 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          ? 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              6.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '10 % MPD, 12-14 % PEG 6000, 0.1 M MES pH 6.5' 
_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 EIGER2 S 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2019-10-24 
_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   0.9795 
_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                        'DIAMOND BEAMLINE I04' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9795 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I04 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9I69 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.463 
_reflns.d_resolution_low                               45.55 
_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                                     35450 
_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                           74.5 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.6 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.054 
_reflns.pdbx_Rpim_I_all                                0.023 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.048 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.463 
_reflns_shell.d_res_low                                     1.599 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           10465 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1772 
_reflns_shell.percent_possible_obs                          16.0 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               5.9 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.4 
_reflns_shell.pdbx_Rrim_I_all                               1.099 
_reflns_shell.pdbx_Rpim_I_all                               0.453 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.000 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            -0.02070 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            0.45750 
_refine.aniso_B[2][2]                            0.56660 
_refine.aniso_B[2][3]                            0.00000 
_refine.aniso_B[3][3]                            -0.54600 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               27.77 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.969 
_refine.correlation_coeff_Fo_to_Fc_free          0.962 
_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                                 9I69 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.463 
_refine.ls_d_res_low                             45.55 
_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                     35450 
_refine.ls_number_reflns_R_free                  1721 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    74.4 
_refine.ls_percent_reflns_R_free                 4.850 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1663 
_refine.ls_R_factor_R_free                       0.1842 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1654 
_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                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.082 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.083 
_refine.pdbx_overall_SU_R_Blow_DPI               0.091 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             0.089 
_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_analyze.entry_id                        9I69 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.19 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_sigma_a_free_details    ? 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_sigma_a_obs_details     ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.RG_d_res_high                   ? 
_refine_analyze.RG_d_res_low                    ? 
_refine_analyze.RG_free                         ? 
_refine_analyze.RG_work                         ? 
_refine_analyze.RG_free_work_ratio              ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.463 
_refine_hist.d_res_low                        45.55 
_refine_hist.number_atoms_solvent             240 
_refine_hist.number_atoms_total               2678 
_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        2429 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         9 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.008 ? 2552 ? t_bond_d                  2.00  HARMONIC     
'X-RAY DIFFRACTION' ? 1.02  ? 3497 ? t_angle_deg               2.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 835  ? t_dihedral_angle_d        2.00  SINUSOIDAL   
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_incorr_chiral_ct        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_pseud_angle             ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_trig_c_planes           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 439  ? t_gen_planes              5.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 2552 ? t_it                      10.00 HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_nbd                     ?     ?            
'X-RAY DIFFRACTION' ? 4.39  ? ?    ? t_omega_torsion           ?     ?            
'X-RAY DIFFRACTION' ? 15.17 ? ?    ? t_other_torsion           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_improper_torsion        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 323  ? t_chiral_improper_torsion 5.00  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? ?     ? 6    ? t_sum_occupancies         1.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_utility_distance        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_utility_angle           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_utility_torsion         ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 2208 ? t_ideal_dist_contact      4.00  SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.463 
_refine_ls_shell.d_res_low                        1.55 
_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             673 
_refine_ls_shell.percent_reflns_obs               9.28 
_refine_ls_shell.percent_reflns_R_free            5.08 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.2181 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   ? 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.2177 
# 
_struct.entry_id                     9I69 
_struct.title                        'Crystal structure of human Cdc20 bound to synthetic D-box peptide D20' 
_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        9I69 
_struct_keywords.text            'APC/C, degron, D-box, LIGASE' 
_struct_keywords.pdbx_keywords   LIGASE 
# 
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 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP CDC20_HUMAN Q12834 ? 1 
;MAQFAFESDLHSLLQLDAPIPNAPPARWQRKAKEAAGPAPSPMRAANRSHSAGRTPGRTPGKSSSKVQTTPSKPGGDRYI
PHRSAAQMEVASFLLSKENQPENSQTPTKKEHQKAWALNLNGFDVEEAKILRLSGKPQNAPEGYQNRLKVLYSQKATPGS
SRKTCRYIPSLPDRILDAPEIRNDYYLNLVDWSSGNVLAVALDNSVYLWSASSGDILQLLQMEQPGEYISSVAWIKEGNY
LAVGTSSAEVQLWDVQQQKRLRNMTSHSARVGSLSWNSYILSSGSRSGHIHHHDVRVAEHHVATLSGHSQEVCGLRWAPD
GRHLASGGNDNLVNVWPSAPGEGGWVPLQTFTQHQGAVKAVAWCPWQSNVLATGGGTSDRHIRIWNVCSGACLSAVDAHS
QVCSILWSPHYKELISGHGFAQNQLVIWKYPTMAKVAELKGHTSRVLSLTMSPDGATVASAAADETLRLWRCFELDPARR
REREKASAAKSSLIHQGIR
;
1 
2 PDB 9I69        9I69   ? 2 ? 1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9I69 A 1 ? 499 ? Q12834 1 ? 499 ? 1 499 
2 2 9I69 B 1 ? 9   ? 9I69   1 ? 9   ? 1 9   
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 860   ? 
1 MORE         -1    ? 
1 'SSA (A^2)'  12320 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1 covale both ? B PRO 3 C ? ? ? 1_555 B 0JY 4 N ? ? B PRO 3 B 0JY 4 1_555 ? ? ? ? ? ? ? 1.335 ? ? 
covale2 covale both ? B 0JY 4 C ? ? ? 1_555 B SER 5 N ? ? B 0JY 4 B SER 5 1_555 ? ? ? ? ? ? ? 1.334 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      0JY 
_pdbx_modification_feature.label_asym_id                      B 
_pdbx_modification_feature.label_seq_id                       4 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     . 
_pdbx_modification_feature.modified_residue_label_asym_id     . 
_pdbx_modification_feature.modified_residue_label_seq_id      . 
_pdbx_modification_feature.modified_residue_label_alt_id      . 
_pdbx_modification_feature.auth_comp_id                       0JY 
_pdbx_modification_feature.auth_asym_id                       B 
_pdbx_modification_feature.auth_seq_id                        4 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      . 
_pdbx_modification_feature.modified_residue_auth_asym_id      . 
_pdbx_modification_feature.modified_residue_auth_seq_id       . 
_pdbx_modification_feature.modified_residue_PDB_ins_code      . 
_pdbx_modification_feature.modified_residue_symmetry          . 
_pdbx_modification_feature.comp_id_linking_atom               . 
_pdbx_modification_feature.modified_residue_id_linking_atom   . 
_pdbx_modification_feature.modified_residue_id                LEU 
_pdbx_modification_feature.ref_pcm_id                         1 
_pdbx_modification_feature.ref_comp_id                        0JY 
_pdbx_modification_feature.type                               Methylation 
_pdbx_modification_feature.category                           'Named protein modification' 
# 
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 PHE 420 A . ? PHE 420 A ALA 421 A ? ALA 421 A 1 6.57  
2 TYR 430 A . ? TYR 430 A PRO 431 A ? PRO 431 A 1 10.10 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 4 ? 
AA3 ? 4 ? 
AA4 ? 4 ? 
AA5 ? 4 ? 
AA6 ? 4 ? 
AA7 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ARG A 174 ? ASP A 177 ? ARG A 174 ASP A 177 
AA1 2 THR A 466 ? TRP A 470 ? THR A 466 TRP A 470 
AA1 3 VAL A 458 ? ALA A 462 ? VAL A 458 ALA A 462 
AA1 4 VAL A 446 ? MET A 451 ? VAL A 446 MET A 451 
AA2 1 VAL A 190 ? TRP A 192 ? VAL A 190 TRP A 192 
AA2 2 VAL A 197 ? LEU A 202 ? VAL A 197 LEU A 202 
AA2 3 SER A 205 ? SER A 210 ? SER A 205 SER A 210 
AA2 4 ILE A 216 ? GLN A 221 ? ILE A 216 GLN A 221 
AA3 1 ILE A 229 ? TRP A 234 ? ILE A 229 TRP A 234 
AA3 2 TYR A 240 ? THR A 245 ? TYR A 240 THR A 245 
AA3 3 GLU A 249 ? ASP A 254 ? GLU A 249 ASP A 254 
AA3 4 LYS A 259 ? THR A 265 ? LYS A 259 THR A 265 
AA4 1 VAL A 271 ? ASN A 277 ? VAL A 271 ASN A 277 
AA4 2 ILE A 280 ? SER A 285 ? ILE A 280 SER A 285 
AA4 3 HIS A 289 ? ASP A 294 ? HIS A 289 ASP A 294 
AA4 4 HIS A 301 ? SER A 306 ? HIS A 301 SER A 306 
AA5 1 VAL A 312 ? TRP A 317 ? VAL A 312 TRP A 317 
AA5 2 HIS A 323 ? GLY A 328 ? HIS A 323 GLY A 328 
AA5 3 VAL A 333 ? PRO A 337 ? VAL A 333 PRO A 337 
AA5 4 GLN A 349 ? PHE A 351 ? GLN A 349 PHE A 351 
AA6 1 VAL A 358 ? TRP A 363 ? VAL A 358 TRP A 363 
AA6 2 VAL A 370 ? GLY A 375 ? VAL A 370 GLY A 375 
AA6 3 HIS A 381 ? ASN A 386 ? HIS A 381 ASN A 386 
AA6 4 CYS A 392 ? ASP A 397 ? CYS A 392 ASP A 397 
AA7 1 VAL A 402 ? TRP A 407 ? VAL A 402 TRP A 407 
AA7 2 GLU A 413 ? HIS A 418 ? GLU A 413 HIS A 418 
AA7 3 LEU A 425 ? LYS A 429 ? LEU A 425 LYS A 429 
AA7 4 ALA A 434 ? LEU A 439 ? ALA A 434 LEU A 439 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 176 ? N LEU A 176 O LEU A 467 ? O LEU A 467 
AA1 2 3 O TRP A 470 ? O TRP A 470 N VAL A 458 ? N VAL A 458 
AA1 3 4 O ALA A 461 ? O ALA A 461 N LEU A 447 ? N LEU A 447 
AA2 1 2 N ASP A 191 ? N ASP A 191 O ALA A 199 ? O ALA A 199 
AA2 2 3 N VAL A 200 ? N VAL A 200 O TYR A 207 ? O TYR A 207 
AA2 3 4 N LEU A 208 ? N LEU A 208 O LEU A 217 ? O LEU A 217 
AA3 1 2 N ALA A 233 ? N ALA A 233 O ALA A 242 ? O ALA A 242 
AA3 2 3 N VAL A 243 ? N VAL A 243 O GLN A 251 ? O GLN A 251 
AA3 3 4 N LEU A 252 ? N LEU A 252 O LEU A 261 ? O LEU A 261 
AA4 1 2 N SER A 275 ? N SER A 275 O SER A 282 ? O SER A 282 
AA4 2 3 N LEU A 281 ? N LEU A 281 O HIS A 293 ? O HIS A 293 
AA4 3 4 N ILE A 290 ? N ILE A 290 O LEU A 305 ? O LEU A 305 
AA5 1 2 N ARG A 316 ? N ARG A 316 O ALA A 325 ? O ALA A 325 
AA5 2 3 N LEU A 324 ? N LEU A 324 O TRP A 336 ? O TRP A 336 
AA5 3 4 N VAL A 333 ? N VAL A 333 O PHE A 351 ? O PHE A 351 
AA6 1 2 N ALA A 362 ? N ALA A 362 O ALA A 372 ? O ALA A 372 
AA6 2 3 N LEU A 371 ? N LEU A 371 O TRP A 385 ? O TRP A 385 
AA6 3 4 N ILE A 382 ? N ILE A 382 O VAL A 396 ? O VAL A 396 
AA7 1 2 N LEU A 406 ? N LEU A 406 O ILE A 415 ? O ILE A 415 
AA7 2 3 N LEU A 414 ? N LEU A 414 O TRP A 428 ? O TRP A 428 
AA7 3 4 N ILE A 427 ? N ILE A 427 O VAL A 436 ? O VAL A 436 
# 
_pdbx_entry_details.entry_id                   9I69 
_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   Y 
# 
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 ASP A 203 ? ? 59.29   -106.26 
2 1 SER A 266 ? ? -164.74 -33.85  
3 1 SER A 278 ? ? 60.09   -124.47 
4 1 GLN A 355 ? A -104.09 46.55   
5 1 GLN A 355 ? B -104.39 51.96   
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         -1.7512 
_pdbx_refine_tls.origin_y         -15.7204 
_pdbx_refine_tls.origin_z         14.6000 
_pdbx_refine_tls.T[1][1]          -0.0649 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0282 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          0.0025 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          -0.0453 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.0267 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          -0.0341 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          1.0001 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.1453 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.3562 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.5793 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          0.0544 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          2.1006 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0481 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.0698 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.0109 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.0112 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.0437 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.0096 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          0.0488 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.0343 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.0044 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_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   '{ A|* }' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 A MET 1   ? A MET 1   
2   1 Y 1 A ALA 2   ? A ALA 2   
3   1 Y 1 A GLN 3   ? A GLN 3   
4   1 Y 1 A PHE 4   ? A PHE 4   
5   1 Y 1 A ALA 5   ? A ALA 5   
6   1 Y 1 A PHE 6   ? A PHE 6   
7   1 Y 1 A GLU 7   ? A GLU 7   
8   1 Y 1 A SER 8   ? A SER 8   
9   1 Y 1 A ASP 9   ? A ASP 9   
10  1 Y 1 A LEU 10  ? A LEU 10  
11  1 Y 1 A HIS 11  ? A HIS 11  
12  1 Y 1 A SER 12  ? A SER 12  
13  1 Y 1 A LEU 13  ? A LEU 13  
14  1 Y 1 A LEU 14  ? A LEU 14  
15  1 Y 1 A GLN 15  ? A GLN 15  
16  1 Y 1 A LEU 16  ? A LEU 16  
17  1 Y 1 A ASP 17  ? A ASP 17  
18  1 Y 1 A ALA 18  ? A ALA 18  
19  1 Y 1 A PRO 19  ? A PRO 19  
20  1 Y 1 A ILE 20  ? A ILE 20  
21  1 Y 1 A PRO 21  ? A PRO 21  
22  1 Y 1 A ASN 22  ? A ASN 22  
23  1 Y 1 A ALA 23  ? A ALA 23  
24  1 Y 1 A PRO 24  ? A PRO 24  
25  1 Y 1 A PRO 25  ? A PRO 25  
26  1 Y 1 A ALA 26  ? A ALA 26  
27  1 Y 1 A ARG 27  ? A ARG 27  
28  1 Y 1 A TRP 28  ? A TRP 28  
29  1 Y 1 A GLN 29  ? A GLN 29  
30  1 Y 1 A ARG 30  ? A ARG 30  
31  1 Y 1 A LYS 31  ? A LYS 31  
32  1 Y 1 A ALA 32  ? A ALA 32  
33  1 Y 1 A LYS 33  ? A LYS 33  
34  1 Y 1 A GLU 34  ? A GLU 34  
35  1 Y 1 A ALA 35  ? A ALA 35  
36  1 Y 1 A ALA 36  ? A ALA 36  
37  1 Y 1 A GLY 37  ? A GLY 37  
38  1 Y 1 A PRO 38  ? A PRO 38  
39  1 Y 1 A ALA 39  ? A ALA 39  
40  1 Y 1 A PRO 40  ? A PRO 40  
41  1 Y 1 A SER 41  ? A SER 41  
42  1 Y 1 A PRO 42  ? A PRO 42  
43  1 Y 1 A MET 43  ? A MET 43  
44  1 Y 1 A ARG 44  ? A ARG 44  
45  1 Y 1 A ALA 45  ? A ALA 45  
46  1 Y 1 A ALA 46  ? A ALA 46  
47  1 Y 1 A ASN 47  ? A ASN 47  
48  1 Y 1 A ARG 48  ? A ARG 48  
49  1 Y 1 A SER 49  ? A SER 49  
50  1 Y 1 A HIS 50  ? A HIS 50  
51  1 Y 1 A SER 51  ? A SER 51  
52  1 Y 1 A ALA 52  ? A ALA 52  
53  1 Y 1 A GLY 53  ? A GLY 53  
54  1 Y 1 A ARG 54  ? A ARG 54  
55  1 Y 1 A THR 55  ? A THR 55  
56  1 Y 1 A PRO 56  ? A PRO 56  
57  1 Y 1 A GLY 57  ? A GLY 57  
58  1 Y 1 A ARG 58  ? A ARG 58  
59  1 Y 1 A THR 59  ? A THR 59  
60  1 Y 1 A PRO 60  ? A PRO 60  
61  1 Y 1 A GLY 61  ? A GLY 61  
62  1 Y 1 A LYS 62  ? A LYS 62  
63  1 Y 1 A SER 63  ? A SER 63  
64  1 Y 1 A SER 64  ? A SER 64  
65  1 Y 1 A SER 65  ? A SER 65  
66  1 Y 1 A LYS 66  ? A LYS 66  
67  1 Y 1 A VAL 67  ? A VAL 67  
68  1 Y 1 A GLN 68  ? A GLN 68  
69  1 Y 1 A THR 69  ? A THR 69  
70  1 Y 1 A THR 70  ? A THR 70  
71  1 Y 1 A PRO 71  ? A PRO 71  
72  1 Y 1 A SER 72  ? A SER 72  
73  1 Y 1 A LYS 73  ? A LYS 73  
74  1 Y 1 A PRO 74  ? A PRO 74  
75  1 Y 1 A GLY 75  ? A GLY 75  
76  1 Y 1 A GLY 76  ? A GLY 76  
77  1 Y 1 A ASP 77  ? A ASP 77  
78  1 Y 1 A ARG 78  ? A ARG 78  
79  1 Y 1 A TYR 79  ? A TYR 79  
80  1 Y 1 A ILE 80  ? A ILE 80  
81  1 Y 1 A PRO 81  ? A PRO 81  
82  1 Y 1 A HIS 82  ? A HIS 82  
83  1 Y 1 A ARG 83  ? A ARG 83  
84  1 Y 1 A SER 84  ? A SER 84  
85  1 Y 1 A ALA 85  ? A ALA 85  
86  1 Y 1 A ALA 86  ? A ALA 86  
87  1 Y 1 A GLN 87  ? A GLN 87  
88  1 Y 1 A MET 88  ? A MET 88  
89  1 Y 1 A GLU 89  ? A GLU 89  
90  1 Y 1 A VAL 90  ? A VAL 90  
91  1 Y 1 A ALA 91  ? A ALA 91  
92  1 Y 1 A SER 92  ? A SER 92  
93  1 Y 1 A PHE 93  ? A PHE 93  
94  1 Y 1 A LEU 94  ? A LEU 94  
95  1 Y 1 A LEU 95  ? A LEU 95  
96  1 Y 1 A SER 96  ? A SER 96  
97  1 Y 1 A LYS 97  ? A LYS 97  
98  1 Y 1 A GLU 98  ? A GLU 98  
99  1 Y 1 A ASN 99  ? A ASN 99  
100 1 Y 1 A GLN 100 ? A GLN 100 
101 1 Y 1 A PRO 101 ? A PRO 101 
102 1 Y 1 A GLU 102 ? A GLU 102 
103 1 Y 1 A ASN 103 ? A ASN 103 
104 1 Y 1 A SER 104 ? A SER 104 
105 1 Y 1 A GLN 105 ? A GLN 105 
106 1 Y 1 A THR 106 ? A THR 106 
107 1 Y 1 A PRO 107 ? A PRO 107 
108 1 Y 1 A THR 108 ? A THR 108 
109 1 Y 1 A LYS 109 ? A LYS 109 
110 1 Y 1 A LYS 110 ? A LYS 110 
111 1 Y 1 A GLU 111 ? A GLU 111 
112 1 Y 1 A HIS 112 ? A HIS 112 
113 1 Y 1 A GLN 113 ? A GLN 113 
114 1 Y 1 A LYS 114 ? A LYS 114 
115 1 Y 1 A ALA 115 ? A ALA 115 
116 1 Y 1 A TRP 116 ? A TRP 116 
117 1 Y 1 A ALA 117 ? A ALA 117 
118 1 Y 1 A LEU 118 ? A LEU 118 
119 1 Y 1 A ASN 119 ? A ASN 119 
120 1 Y 1 A LEU 120 ? A LEU 120 
121 1 Y 1 A ASN 121 ? A ASN 121 
122 1 Y 1 A GLY 122 ? A GLY 122 
123 1 Y 1 A PHE 123 ? A PHE 123 
124 1 Y 1 A ASP 124 ? A ASP 124 
125 1 Y 1 A VAL 125 ? A VAL 125 
126 1 Y 1 A GLU 126 ? A GLU 126 
127 1 Y 1 A GLU 127 ? A GLU 127 
128 1 Y 1 A ALA 128 ? A ALA 128 
129 1 Y 1 A LYS 129 ? A LYS 129 
130 1 Y 1 A ILE 130 ? A ILE 130 
131 1 Y 1 A LEU 131 ? A LEU 131 
132 1 Y 1 A ARG 132 ? A ARG 132 
133 1 Y 1 A LEU 133 ? A LEU 133 
134 1 Y 1 A SER 134 ? A SER 134 
135 1 Y 1 A GLY 135 ? A GLY 135 
136 1 Y 1 A LYS 136 ? A LYS 136 
137 1 Y 1 A PRO 137 ? A PRO 137 
138 1 Y 1 A GLN 138 ? A GLN 138 
139 1 Y 1 A ASN 139 ? A ASN 139 
140 1 Y 1 A ALA 140 ? A ALA 140 
141 1 Y 1 A PRO 141 ? A PRO 141 
142 1 Y 1 A GLU 142 ? A GLU 142 
143 1 Y 1 A GLY 143 ? A GLY 143 
144 1 Y 1 A TYR 144 ? A TYR 144 
145 1 Y 1 A GLN 145 ? A GLN 145 
146 1 Y 1 A ASN 146 ? A ASN 146 
147 1 Y 1 A ARG 147 ? A ARG 147 
148 1 Y 1 A LEU 148 ? A LEU 148 
149 1 Y 1 A LYS 149 ? A LYS 149 
150 1 Y 1 A VAL 150 ? A VAL 150 
151 1 Y 1 A LEU 151 ? A LEU 151 
152 1 Y 1 A TYR 152 ? A TYR 152 
153 1 Y 1 A SER 153 ? A SER 153 
154 1 Y 1 A GLN 154 ? A GLN 154 
155 1 Y 1 A LYS 155 ? A LYS 155 
156 1 Y 1 A ALA 156 ? A ALA 156 
157 1 Y 1 A THR 157 ? A THR 157 
158 1 Y 1 A PRO 158 ? A PRO 158 
159 1 Y 1 A GLY 159 ? A GLY 159 
160 1 Y 1 A SER 160 ? A SER 160 
161 1 Y 1 A SER 161 ? A SER 161 
162 1 Y 1 A ARG 162 ? A ARG 162 
163 1 Y 1 A LYS 163 ? A LYS 163 
164 1 Y 1 A THR 164 ? A THR 164 
165 1 Y 1 A CYS 165 ? A CYS 165 
166 1 Y 1 A PRO 477 ? A PRO 477 
167 1 Y 1 A ALA 478 ? A ALA 478 
168 1 Y 1 A ARG 479 ? A ARG 479 
169 1 Y 1 A ARG 480 ? A ARG 480 
170 1 Y 1 A ARG 481 ? A ARG 481 
171 1 Y 1 A GLU 482 ? A GLU 482 
172 1 Y 1 A ARG 483 ? A ARG 483 
173 1 Y 1 A GLU 484 ? A GLU 484 
174 1 Y 1 A LYS 485 ? A LYS 485 
175 1 Y 1 A ALA 486 ? A ALA 486 
176 1 Y 1 A SER 487 ? A SER 487 
177 1 Y 1 A ALA 488 ? A ALA 488 
178 1 Y 1 A ALA 489 ? A ALA 489 
179 1 Y 1 A LYS 490 ? A LYS 490 
180 1 Y 1 A SER 491 ? A SER 491 
181 1 Y 1 A SER 492 ? A SER 492 
182 1 Y 1 A LEU 493 ? A LEU 493 
183 1 Y 1 A ILE 494 ? A ILE 494 
184 1 Y 1 A HIS 495 ? A HIS 495 
185 1 Y 1 A GLN 496 ? A GLN 496 
186 1 Y 1 A GLY 497 ? A GLY 497 
187 1 Y 1 A ILE 498 ? A ILE 498 
188 1 Y 1 A ARG 499 ? A ARG 499 
189 1 Y 1 B ILE 7   ? B ILE 7   
190 1 Y 1 B THR 8   ? B THR 8   
191 1 Y 1 B ASN 9   ? B ASN 9   
# 
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 
0JY O    O N N 1   
0JY C    C N N 2   
0JY CA   C N S 3   
0JY N    N N N 4   
0JY CB   C N N 5   
0JY CAI  C N N 6   
0JY CAB  C N N 7   
0JY CAC  C N N 8   
0JY CAA  C N N 9   
0JY HA   H N N 10  
0JY H2   H N N 11  
0JY H    H N N 12  
0JY H6   H N N 13  
0JY H7   H N N 14  
0JY H8   H N N 15  
0JY H9   H N N 16  
0JY H10  H N N 17  
0JY H11  H N N 18  
0JY H12  H N N 19  
0JY H13  H N N 20  
0JY H14  H N N 21  
0JY H15  H N N 22  
0JY H16  H N N 23  
0JY OXT  O N N 24  
0JY HXT  H N N 25  
ALA N    N N N 26  
ALA CA   C N S 27  
ALA C    C N N 28  
ALA O    O N N 29  
ALA CB   C N N 30  
ALA OXT  O N N 31  
ALA H    H N N 32  
ALA H2   H N N 33  
ALA HA   H N N 34  
ALA HB1  H N N 35  
ALA HB2  H N N 36  
ALA HB3  H N N 37  
ALA HXT  H N N 38  
ARG N    N N N 39  
ARG CA   C N S 40  
ARG C    C N N 41  
ARG O    O N N 42  
ARG CB   C N N 43  
ARG CG   C N N 44  
ARG CD   C N N 45  
ARG NE   N N N 46  
ARG CZ   C N N 47  
ARG NH1  N N N 48  
ARG NH2  N N N 49  
ARG OXT  O N N 50  
ARG H    H N N 51  
ARG H2   H N N 52  
ARG HA   H N N 53  
ARG HB2  H N N 54  
ARG HB3  H N N 55  
ARG HG2  H N N 56  
ARG HG3  H N N 57  
ARG HD2  H N N 58  
ARG HD3  H N N 59  
ARG HE   H N N 60  
ARG HH11 H N N 61  
ARG HH12 H N N 62  
ARG HH21 H N N 63  
ARG HH22 H N N 64  
ARG HXT  H N N 65  
ASN N    N N N 66  
ASN CA   C N S 67  
ASN C    C N N 68  
ASN O    O N N 69  
ASN CB   C N N 70  
ASN CG   C N N 71  
ASN OD1  O N N 72  
ASN ND2  N N N 73  
ASN OXT  O N N 74  
ASN H    H N N 75  
ASN H2   H N N 76  
ASN HA   H N N 77  
ASN HB2  H N N 78  
ASN HB3  H N N 79  
ASN HD21 H N N 80  
ASN HD22 H N N 81  
ASN HXT  H N N 82  
ASP N    N N N 83  
ASP CA   C N S 84  
ASP C    C N N 85  
ASP O    O N N 86  
ASP CB   C N N 87  
ASP CG   C N N 88  
ASP OD1  O N N 89  
ASP OD2  O N N 90  
ASP OXT  O N N 91  
ASP H    H N N 92  
ASP H2   H N N 93  
ASP HA   H N N 94  
ASP HB2  H N N 95  
ASP HB3  H N N 96  
ASP HD2  H N N 97  
ASP HXT  H N N 98  
CYS N    N N N 99  
CYS CA   C N R 100 
CYS C    C N N 101 
CYS O    O N N 102 
CYS CB   C N N 103 
CYS SG   S N N 104 
CYS OXT  O N N 105 
CYS H    H N N 106 
CYS H2   H N N 107 
CYS HA   H N N 108 
CYS HB2  H N N 109 
CYS HB3  H N N 110 
CYS HG   H N N 111 
CYS HXT  H N N 112 
GLN N    N N N 113 
GLN CA   C N S 114 
GLN C    C N N 115 
GLN O    O N N 116 
GLN CB   C N N 117 
GLN CG   C N N 118 
GLN CD   C N N 119 
GLN OE1  O N N 120 
GLN NE2  N N N 121 
GLN OXT  O N N 122 
GLN H    H N N 123 
GLN H2   H N N 124 
GLN HA   H N N 125 
GLN HB2  H N N 126 
GLN HB3  H N N 127 
GLN HG2  H N N 128 
GLN HG3  H N N 129 
GLN HE21 H N N 130 
GLN HE22 H N N 131 
GLN HXT  H N N 132 
GLU N    N N N 133 
GLU CA   C N S 134 
GLU C    C N N 135 
GLU O    O N N 136 
GLU CB   C N N 137 
GLU CG   C N N 138 
GLU CD   C N N 139 
GLU OE1  O N N 140 
GLU OE2  O N N 141 
GLU OXT  O N N 142 
GLU H    H N N 143 
GLU H2   H N N 144 
GLU HA   H N N 145 
GLU HB2  H N N 146 
GLU HB3  H N N 147 
GLU HG2  H N N 148 
GLU HG3  H N N 149 
GLU HE2  H N N 150 
GLU HXT  H N N 151 
GLY N    N N N 152 
GLY CA   C N N 153 
GLY C    C N N 154 
GLY O    O N N 155 
GLY OXT  O N N 156 
GLY H    H N N 157 
GLY H2   H N N 158 
GLY HA2  H N N 159 
GLY HA3  H N N 160 
GLY HXT  H N N 161 
HIS N    N N N 162 
HIS CA   C N S 163 
HIS C    C N N 164 
HIS O    O N N 165 
HIS CB   C N N 166 
HIS CG   C Y N 167 
HIS ND1  N Y N 168 
HIS CD2  C Y N 169 
HIS CE1  C Y N 170 
HIS NE2  N Y N 171 
HIS OXT  O N N 172 
HIS H    H N N 173 
HIS H2   H N N 174 
HIS HA   H N N 175 
HIS HB2  H N N 176 
HIS HB3  H N N 177 
HIS HD1  H N N 178 
HIS HD2  H N N 179 
HIS HE1  H N N 180 
HIS HE2  H N N 181 
HIS HXT  H N N 182 
HOH O    O N N 183 
HOH H1   H N N 184 
HOH H2   H N N 185 
ILE N    N N N 186 
ILE CA   C N S 187 
ILE C    C N N 188 
ILE O    O N N 189 
ILE CB   C N S 190 
ILE CG1  C N N 191 
ILE CG2  C N N 192 
ILE CD1  C N N 193 
ILE OXT  O N N 194 
ILE H    H N N 195 
ILE H2   H N N 196 
ILE HA   H N N 197 
ILE HB   H N N 198 
ILE HG12 H N N 199 
ILE HG13 H N N 200 
ILE HG21 H N N 201 
ILE HG22 H N N 202 
ILE HG23 H N N 203 
ILE HD11 H N N 204 
ILE HD12 H N N 205 
ILE HD13 H N N 206 
ILE HXT  H N N 207 
LEU N    N N N 208 
LEU CA   C N S 209 
LEU C    C N N 210 
LEU O    O N N 211 
LEU CB   C N N 212 
LEU CG   C N N 213 
LEU CD1  C N N 214 
LEU CD2  C N N 215 
LEU OXT  O N N 216 
LEU H    H N N 217 
LEU H2   H N N 218 
LEU HA   H N N 219 
LEU HB2  H N N 220 
LEU HB3  H N N 221 
LEU HG   H N N 222 
LEU HD11 H N N 223 
LEU HD12 H N N 224 
LEU HD13 H N N 225 
LEU HD21 H N N 226 
LEU HD22 H N N 227 
LEU HD23 H N N 228 
LEU HXT  H N N 229 
LYS N    N N N 230 
LYS CA   C N S 231 
LYS C    C N N 232 
LYS O    O N N 233 
LYS CB   C N N 234 
LYS CG   C N N 235 
LYS CD   C N N 236 
LYS CE   C N N 237 
LYS NZ   N N N 238 
LYS OXT  O N N 239 
LYS H    H N N 240 
LYS H2   H N N 241 
LYS HA   H N N 242 
LYS HB2  H N N 243 
LYS HB3  H N N 244 
LYS HG2  H N N 245 
LYS HG3  H N N 246 
LYS HD2  H N N 247 
LYS HD3  H N N 248 
LYS HE2  H N N 249 
LYS HE3  H N N 250 
LYS HZ1  H N N 251 
LYS HZ2  H N N 252 
LYS HZ3  H N N 253 
LYS HXT  H N N 254 
MET N    N N N 255 
MET CA   C N S 256 
MET C    C N N 257 
MET O    O N N 258 
MET CB   C N N 259 
MET CG   C N N 260 
MET SD   S N N 261 
MET CE   C N N 262 
MET OXT  O N N 263 
MET H    H N N 264 
MET H2   H N N 265 
MET HA   H N N 266 
MET HB2  H N N 267 
MET HB3  H N N 268 
MET HG2  H N N 269 
MET HG3  H N N 270 
MET HE1  H N N 271 
MET HE2  H N N 272 
MET HE3  H N N 273 
MET HXT  H N N 274 
PHE N    N N N 275 
PHE CA   C N S 276 
PHE C    C N N 277 
PHE O    O N N 278 
PHE CB   C N N 279 
PHE CG   C Y N 280 
PHE CD1  C Y N 281 
PHE CD2  C Y N 282 
PHE CE1  C Y N 283 
PHE CE2  C Y N 284 
PHE CZ   C Y N 285 
PHE OXT  O N N 286 
PHE H    H N N 287 
PHE H2   H N N 288 
PHE HA   H N N 289 
PHE HB2  H N N 290 
PHE HB3  H N N 291 
PHE HD1  H N N 292 
PHE HD2  H N N 293 
PHE HE1  H N N 294 
PHE HE2  H N N 295 
PHE HZ   H N N 296 
PHE HXT  H N N 297 
PRO N    N N N 298 
PRO CA   C N S 299 
PRO C    C N N 300 
PRO O    O N N 301 
PRO CB   C N N 302 
PRO CG   C N N 303 
PRO CD   C N N 304 
PRO OXT  O N N 305 
PRO H    H N N 306 
PRO HA   H N N 307 
PRO HB2  H N N 308 
PRO HB3  H N N 309 
PRO HG2  H N N 310 
PRO HG3  H N N 311 
PRO HD2  H N N 312 
PRO HD3  H N N 313 
PRO HXT  H N N 314 
SER N    N N N 315 
SER CA   C N S 316 
SER C    C N N 317 
SER O    O N N 318 
SER CB   C N N 319 
SER OG   O N N 320 
SER OXT  O N N 321 
SER H    H N N 322 
SER H2   H N N 323 
SER HA   H N N 324 
SER HB2  H N N 325 
SER HB3  H N N 326 
SER HG   H N N 327 
SER HXT  H N N 328 
THR N    N N N 329 
THR CA   C N S 330 
THR C    C N N 331 
THR O    O N N 332 
THR CB   C N R 333 
THR OG1  O N N 334 
THR CG2  C N N 335 
THR OXT  O N N 336 
THR H    H N N 337 
THR H2   H N N 338 
THR HA   H N N 339 
THR HB   H N N 340 
THR HG1  H N N 341 
THR HG21 H N N 342 
THR HG22 H N N 343 
THR HG23 H N N 344 
THR HXT  H N N 345 
TRP N    N N N 346 
TRP CA   C N S 347 
TRP C    C N N 348 
TRP O    O N N 349 
TRP CB   C N N 350 
TRP CG   C Y N 351 
TRP CD1  C Y N 352 
TRP CD2  C Y N 353 
TRP NE1  N Y N 354 
TRP CE2  C Y N 355 
TRP CE3  C Y N 356 
TRP CZ2  C Y N 357 
TRP CZ3  C Y N 358 
TRP CH2  C Y N 359 
TRP OXT  O N N 360 
TRP H    H N N 361 
TRP H2   H N N 362 
TRP HA   H N N 363 
TRP HB2  H N N 364 
TRP HB3  H N N 365 
TRP HD1  H N N 366 
TRP HE1  H N N 367 
TRP HE3  H N N 368 
TRP HZ2  H N N 369 
TRP HZ3  H N N 370 
TRP HH2  H N N 371 
TRP HXT  H N N 372 
TYR N    N N N 373 
TYR CA   C N S 374 
TYR C    C N N 375 
TYR O    O N N 376 
TYR CB   C N N 377 
TYR CG   C Y N 378 
TYR CD1  C Y N 379 
TYR CD2  C Y N 380 
TYR CE1  C Y N 381 
TYR CE2  C Y N 382 
TYR CZ   C Y N 383 
TYR OH   O N N 384 
TYR OXT  O N N 385 
TYR H    H N N 386 
TYR H2   H N N 387 
TYR HA   H N N 388 
TYR HB2  H N N 389 
TYR HB3  H N N 390 
TYR HD1  H N N 391 
TYR HD2  H N N 392 
TYR HE1  H N N 393 
TYR HE2  H N N 394 
TYR HH   H N N 395 
TYR HXT  H N N 396 
VAL N    N N N 397 
VAL CA   C N S 398 
VAL C    C N N 399 
VAL O    O N N 400 
VAL CB   C N N 401 
VAL CG1  C N N 402 
VAL CG2  C N N 403 
VAL OXT  O N N 404 
VAL H    H N N 405 
VAL H2   H N N 406 
VAL HA   H N N 407 
VAL HB   H N N 408 
VAL HG11 H N N 409 
VAL HG12 H N N 410 
VAL HG13 H N N 411 
VAL HG21 H N N 412 
VAL HG22 H N N 413 
VAL HG23 H N N 414 
VAL HXT  H N N 415 
# 
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 
0JY O   C    doub N N 1   
0JY C   CA   sing N N 2   
0JY CA  N    sing N N 3   
0JY CA  CB   sing N N 4   
0JY CAC CAI  sing N N 5   
0JY CB  CAI  sing N N 6   
0JY CAI CAB  sing N N 7   
0JY CAI CAA  sing N N 8   
0JY CA  HA   sing N N 9   
0JY N   H2   sing N N 10  
0JY N   H    sing N N 11  
0JY CB  H6   sing N N 12  
0JY CB  H7   sing N N 13  
0JY CAB H8   sing N N 14  
0JY CAB H9   sing N N 15  
0JY CAB H10  sing N N 16  
0JY CAC H11  sing N N 17  
0JY CAC H12  sing N N 18  
0JY CAC H13  sing N N 19  
0JY CAA H14  sing N N 20  
0JY CAA H15  sing N N 21  
0JY CAA H16  sing N N 22  
0JY C   OXT  sing N N 23  
0JY OXT HXT  sing N N 24  
ALA N   CA   sing N N 25  
ALA N   H    sing N N 26  
ALA N   H2   sing N N 27  
ALA CA  C    sing N N 28  
ALA CA  CB   sing N N 29  
ALA CA  HA   sing N N 30  
ALA C   O    doub N N 31  
ALA C   OXT  sing N N 32  
ALA CB  HB1  sing N N 33  
ALA CB  HB2  sing N N 34  
ALA CB  HB3  sing N N 35  
ALA OXT HXT  sing N N 36  
ARG N   CA   sing N N 37  
ARG N   H    sing N N 38  
ARG N   H2   sing N N 39  
ARG CA  C    sing N N 40  
ARG CA  CB   sing N N 41  
ARG CA  HA   sing N N 42  
ARG C   O    doub N N 43  
ARG C   OXT  sing N N 44  
ARG CB  CG   sing N N 45  
ARG CB  HB2  sing N N 46  
ARG CB  HB3  sing N N 47  
ARG CG  CD   sing N N 48  
ARG CG  HG2  sing N N 49  
ARG CG  HG3  sing N N 50  
ARG CD  NE   sing N N 51  
ARG CD  HD2  sing N N 52  
ARG CD  HD3  sing N N 53  
ARG NE  CZ   sing N N 54  
ARG NE  HE   sing N N 55  
ARG CZ  NH1  sing N N 56  
ARG CZ  NH2  doub N N 57  
ARG NH1 HH11 sing N N 58  
ARG NH1 HH12 sing N N 59  
ARG NH2 HH21 sing N N 60  
ARG NH2 HH22 sing N N 61  
ARG OXT HXT  sing N N 62  
ASN N   CA   sing N N 63  
ASN N   H    sing N N 64  
ASN N   H2   sing N N 65  
ASN CA  C    sing N N 66  
ASN CA  CB   sing N N 67  
ASN CA  HA   sing N N 68  
ASN C   O    doub N N 69  
ASN C   OXT  sing N N 70  
ASN CB  CG   sing N N 71  
ASN CB  HB2  sing N N 72  
ASN CB  HB3  sing N N 73  
ASN CG  OD1  doub N N 74  
ASN CG  ND2  sing N N 75  
ASN ND2 HD21 sing N N 76  
ASN ND2 HD22 sing N N 77  
ASN OXT HXT  sing N N 78  
ASP N   CA   sing N N 79  
ASP N   H    sing N N 80  
ASP N   H2   sing N N 81  
ASP CA  C    sing N N 82  
ASP CA  CB   sing N N 83  
ASP CA  HA   sing N N 84  
ASP C   O    doub N N 85  
ASP C   OXT  sing N N 86  
ASP CB  CG   sing N N 87  
ASP CB  HB2  sing N N 88  
ASP CB  HB3  sing N N 89  
ASP CG  OD1  doub N N 90  
ASP CG  OD2  sing N N 91  
ASP OD2 HD2  sing N N 92  
ASP OXT HXT  sing N N 93  
CYS N   CA   sing N N 94  
CYS N   H    sing N N 95  
CYS N   H2   sing N N 96  
CYS CA  C    sing N N 97  
CYS CA  CB   sing N N 98  
CYS CA  HA   sing N N 99  
CYS C   O    doub N N 100 
CYS C   OXT  sing N N 101 
CYS CB  SG   sing N N 102 
CYS CB  HB2  sing N N 103 
CYS CB  HB3  sing N N 104 
CYS SG  HG   sing N N 105 
CYS OXT HXT  sing N N 106 
GLN N   CA   sing N N 107 
GLN N   H    sing N N 108 
GLN N   H2   sing N N 109 
GLN CA  C    sing N N 110 
GLN CA  CB   sing N N 111 
GLN CA  HA   sing N N 112 
GLN C   O    doub N N 113 
GLN C   OXT  sing N N 114 
GLN CB  CG   sing N N 115 
GLN CB  HB2  sing N N 116 
GLN CB  HB3  sing N N 117 
GLN CG  CD   sing N N 118 
GLN CG  HG2  sing N N 119 
GLN CG  HG3  sing N N 120 
GLN CD  OE1  doub N N 121 
GLN CD  NE2  sing N N 122 
GLN NE2 HE21 sing N N 123 
GLN NE2 HE22 sing N N 124 
GLN OXT HXT  sing N N 125 
GLU N   CA   sing N N 126 
GLU N   H    sing N N 127 
GLU N   H2   sing N N 128 
GLU CA  C    sing N N 129 
GLU CA  CB   sing N N 130 
GLU CA  HA   sing N N 131 
GLU C   O    doub N N 132 
GLU C   OXT  sing N N 133 
GLU CB  CG   sing N N 134 
GLU CB  HB2  sing N N 135 
GLU CB  HB3  sing N N 136 
GLU CG  CD   sing N N 137 
GLU CG  HG2  sing N N 138 
GLU CG  HG3  sing N N 139 
GLU CD  OE1  doub N N 140 
GLU CD  OE2  sing N N 141 
GLU OE2 HE2  sing N N 142 
GLU OXT HXT  sing N N 143 
GLY N   CA   sing N N 144 
GLY N   H    sing N N 145 
GLY N   H2   sing N N 146 
GLY CA  C    sing N N 147 
GLY CA  HA2  sing N N 148 
GLY CA  HA3  sing N N 149 
GLY C   O    doub N N 150 
GLY C   OXT  sing N N 151 
GLY OXT HXT  sing N N 152 
HIS N   CA   sing N N 153 
HIS N   H    sing N N 154 
HIS N   H2   sing N N 155 
HIS CA  C    sing N N 156 
HIS CA  CB   sing N N 157 
HIS CA  HA   sing N N 158 
HIS C   O    doub N N 159 
HIS C   OXT  sing N N 160 
HIS CB  CG   sing N N 161 
HIS CB  HB2  sing N N 162 
HIS CB  HB3  sing N N 163 
HIS CG  ND1  sing Y N 164 
HIS CG  CD2  doub Y N 165 
HIS ND1 CE1  doub Y N 166 
HIS ND1 HD1  sing N N 167 
HIS CD2 NE2  sing Y N 168 
HIS CD2 HD2  sing N N 169 
HIS CE1 NE2  sing Y N 170 
HIS CE1 HE1  sing N N 171 
HIS NE2 HE2  sing N N 172 
HIS OXT HXT  sing N N 173 
HOH O   H1   sing N N 174 
HOH O   H2   sing N N 175 
ILE N   CA   sing N N 176 
ILE N   H    sing N N 177 
ILE N   H2   sing N N 178 
ILE CA  C    sing N N 179 
ILE CA  CB   sing N N 180 
ILE CA  HA   sing N N 181 
ILE C   O    doub N N 182 
ILE C   OXT  sing N N 183 
ILE CB  CG1  sing N N 184 
ILE CB  CG2  sing N N 185 
ILE CB  HB   sing N N 186 
ILE CG1 CD1  sing N N 187 
ILE CG1 HG12 sing N N 188 
ILE CG1 HG13 sing N N 189 
ILE CG2 HG21 sing N N 190 
ILE CG2 HG22 sing N N 191 
ILE CG2 HG23 sing N N 192 
ILE CD1 HD11 sing N N 193 
ILE CD1 HD12 sing N N 194 
ILE CD1 HD13 sing N N 195 
ILE OXT HXT  sing N N 196 
LEU N   CA   sing N N 197 
LEU N   H    sing N N 198 
LEU N   H2   sing N N 199 
LEU CA  C    sing N N 200 
LEU CA  CB   sing N N 201 
LEU CA  HA   sing N N 202 
LEU C   O    doub N N 203 
LEU C   OXT  sing N N 204 
LEU CB  CG   sing N N 205 
LEU CB  HB2  sing N N 206 
LEU CB  HB3  sing N N 207 
LEU CG  CD1  sing N N 208 
LEU CG  CD2  sing N N 209 
LEU CG  HG   sing N N 210 
LEU CD1 HD11 sing N N 211 
LEU CD1 HD12 sing N N 212 
LEU CD1 HD13 sing N N 213 
LEU CD2 HD21 sing N N 214 
LEU CD2 HD22 sing N N 215 
LEU CD2 HD23 sing N N 216 
LEU OXT HXT  sing N N 217 
LYS N   CA   sing N N 218 
LYS N   H    sing N N 219 
LYS N   H2   sing N N 220 
LYS CA  C    sing N N 221 
LYS CA  CB   sing N N 222 
LYS CA  HA   sing N N 223 
LYS C   O    doub N N 224 
LYS C   OXT  sing N N 225 
LYS CB  CG   sing N N 226 
LYS CB  HB2  sing N N 227 
LYS CB  HB3  sing N N 228 
LYS CG  CD   sing N N 229 
LYS CG  HG2  sing N N 230 
LYS CG  HG3  sing N N 231 
LYS CD  CE   sing N N 232 
LYS CD  HD2  sing N N 233 
LYS CD  HD3  sing N N 234 
LYS CE  NZ   sing N N 235 
LYS CE  HE2  sing N N 236 
LYS CE  HE3  sing N N 237 
LYS NZ  HZ1  sing N N 238 
LYS NZ  HZ2  sing N N 239 
LYS NZ  HZ3  sing N N 240 
LYS OXT HXT  sing N N 241 
MET N   CA   sing N N 242 
MET N   H    sing N N 243 
MET N   H2   sing N N 244 
MET CA  C    sing N N 245 
MET CA  CB   sing N N 246 
MET CA  HA   sing N N 247 
MET C   O    doub N N 248 
MET C   OXT  sing N N 249 
MET CB  CG   sing N N 250 
MET CB  HB2  sing N N 251 
MET CB  HB3  sing N N 252 
MET CG  SD   sing N N 253 
MET CG  HG2  sing N N 254 
MET CG  HG3  sing N N 255 
MET SD  CE   sing N N 256 
MET CE  HE1  sing N N 257 
MET CE  HE2  sing N N 258 
MET CE  HE3  sing N N 259 
MET OXT HXT  sing N N 260 
PHE N   CA   sing N N 261 
PHE N   H    sing N N 262 
PHE N   H2   sing N N 263 
PHE CA  C    sing N N 264 
PHE CA  CB   sing N N 265 
PHE CA  HA   sing N N 266 
PHE C   O    doub N N 267 
PHE C   OXT  sing N N 268 
PHE CB  CG   sing N N 269 
PHE CB  HB2  sing N N 270 
PHE CB  HB3  sing N N 271 
PHE CG  CD1  doub Y N 272 
PHE CG  CD2  sing Y N 273 
PHE CD1 CE1  sing Y N 274 
PHE CD1 HD1  sing N N 275 
PHE CD2 CE2  doub Y N 276 
PHE CD2 HD2  sing N N 277 
PHE CE1 CZ   doub Y N 278 
PHE CE1 HE1  sing N N 279 
PHE CE2 CZ   sing Y N 280 
PHE CE2 HE2  sing N N 281 
PHE CZ  HZ   sing N N 282 
PHE OXT HXT  sing N N 283 
PRO N   CA   sing N N 284 
PRO N   CD   sing N N 285 
PRO N   H    sing N N 286 
PRO CA  C    sing N N 287 
PRO CA  CB   sing N N 288 
PRO CA  HA   sing N N 289 
PRO C   O    doub N N 290 
PRO C   OXT  sing N N 291 
PRO CB  CG   sing N N 292 
PRO CB  HB2  sing N N 293 
PRO CB  HB3  sing N N 294 
PRO CG  CD   sing N N 295 
PRO CG  HG2  sing N N 296 
PRO CG  HG3  sing N N 297 
PRO CD  HD2  sing N N 298 
PRO CD  HD3  sing N N 299 
PRO OXT HXT  sing N N 300 
SER N   CA   sing N N 301 
SER N   H    sing N N 302 
SER N   H2   sing N N 303 
SER CA  C    sing N N 304 
SER CA  CB   sing N N 305 
SER CA  HA   sing N N 306 
SER C   O    doub N N 307 
SER C   OXT  sing N N 308 
SER CB  OG   sing N N 309 
SER CB  HB2  sing N N 310 
SER CB  HB3  sing N N 311 
SER OG  HG   sing N N 312 
SER OXT HXT  sing N N 313 
THR N   CA   sing N N 314 
THR N   H    sing N N 315 
THR N   H2   sing N N 316 
THR CA  C    sing N N 317 
THR CA  CB   sing N N 318 
THR CA  HA   sing N N 319 
THR C   O    doub N N 320 
THR C   OXT  sing N N 321 
THR CB  OG1  sing N N 322 
THR CB  CG2  sing N N 323 
THR CB  HB   sing N N 324 
THR OG1 HG1  sing N N 325 
THR CG2 HG21 sing N N 326 
THR CG2 HG22 sing N N 327 
THR CG2 HG23 sing N N 328 
THR OXT HXT  sing N N 329 
TRP N   CA   sing N N 330 
TRP N   H    sing N N 331 
TRP N   H2   sing N N 332 
TRP CA  C    sing N N 333 
TRP CA  CB   sing N N 334 
TRP CA  HA   sing N N 335 
TRP C   O    doub N N 336 
TRP C   OXT  sing N N 337 
TRP CB  CG   sing N N 338 
TRP CB  HB2  sing N N 339 
TRP CB  HB3  sing N N 340 
TRP CG  CD1  doub Y N 341 
TRP CG  CD2  sing Y N 342 
TRP CD1 NE1  sing Y N 343 
TRP CD1 HD1  sing N N 344 
TRP CD2 CE2  doub Y N 345 
TRP CD2 CE3  sing Y N 346 
TRP NE1 CE2  sing Y N 347 
TRP NE1 HE1  sing N N 348 
TRP CE2 CZ2  sing Y N 349 
TRP CE3 CZ3  doub Y N 350 
TRP CE3 HE3  sing N N 351 
TRP CZ2 CH2  doub Y N 352 
TRP CZ2 HZ2  sing N N 353 
TRP CZ3 CH2  sing Y N 354 
TRP CZ3 HZ3  sing N N 355 
TRP CH2 HH2  sing N N 356 
TRP OXT HXT  sing N N 357 
TYR N   CA   sing N N 358 
TYR N   H    sing N N 359 
TYR N   H2   sing N N 360 
TYR CA  C    sing N N 361 
TYR CA  CB   sing N N 362 
TYR CA  HA   sing N N 363 
TYR C   O    doub N N 364 
TYR C   OXT  sing N N 365 
TYR CB  CG   sing N N 366 
TYR CB  HB2  sing N N 367 
TYR CB  HB3  sing N N 368 
TYR CG  CD1  doub Y N 369 
TYR CG  CD2  sing Y N 370 
TYR CD1 CE1  sing Y N 371 
TYR CD1 HD1  sing N N 372 
TYR CD2 CE2  doub Y N 373 
TYR CD2 HD2  sing N N 374 
TYR CE1 CZ   doub Y N 375 
TYR CE1 HE1  sing N N 376 
TYR CE2 CZ   sing Y N 377 
TYR CE2 HE2  sing N N 378 
TYR CZ  OH   sing N N 379 
TYR OH  HH   sing N N 380 
TYR OXT HXT  sing N N 381 
VAL N   CA   sing N N 382 
VAL N   H    sing N N 383 
VAL N   H2   sing N N 384 
VAL CA  C    sing N N 385 
VAL CA  CB   sing N N 386 
VAL CA  HA   sing N N 387 
VAL C   O    doub N N 388 
VAL C   OXT  sing N N 389 
VAL CB  CG1  sing N N 390 
VAL CB  CG2  sing N N 391 
VAL CB  HB   sing N N 392 
VAL CG1 HG11 sing N N 393 
VAL CG1 HG12 sing N N 394 
VAL CG1 HG13 sing N N 395 
VAL CG2 HG21 sing N N 396 
VAL CG2 HG22 sing N N 397 
VAL CG2 HG23 sing N N 398 
VAL OXT HXT  sing N N 399 
# 
_pdbx_audit_support.funding_organization   'Biotechnology and Biological Sciences Research Council (BBSRC)' 
_pdbx_audit_support.country                'United Kingdom' 
_pdbx_audit_support.grant_number           BB/R004137/1 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   4GGC 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9I69 
_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]   0.028297 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.010378 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011449 
_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]   0.021956 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . ARG A 1 166 ? -17.499 0.793   -0.636  1.00 44.99 ? 166 ARG A N   1 
ATOM   2    C CA  . ARG A 1 166 ? -18.228 0.624   0.621   1.00 44.54 ? 166 ARG A CA  1 
ATOM   3    C C   . ARG A 1 166 ? -17.611 1.483   1.740   1.00 45.38 ? 166 ARG A C   1 
ATOM   4    O O   . ARG A 1 166 ? -16.408 1.761   1.707   1.00 45.83 ? 166 ARG A O   1 
ATOM   5    C CB  . ARG A 1 166 ? -18.272 -0.867  1.008   1.00 43.95 ? 166 ARG A CB  1 
ATOM   6    C CG  . ARG A 1 166 ? -16.916 -1.492  1.389   1.00 42.31 ? 166 ARG A CG  1 
ATOM   7    C CD  . ARG A 1 166 ? -17.073 -2.948  1.833   1.00 39.70 ? 166 ARG A CD  1 
ATOM   8    N NE  . ARG A 1 166 ? -15.893 -3.464  2.534   1.00 34.85 ? 166 ARG A NE  1 
ATOM   9    C CZ  . ARG A 1 166 ? -15.684 -3.342  3.841   1.00 32.32 ? 166 ARG A CZ  1 
ATOM   10   N NH1 . ARG A 1 166 ? -16.575 -2.719  4.610   1.00 29.37 ? 166 ARG A NH1 1 
ATOM   11   N NH2 . ARG A 1 166 ? -14.576 -3.818  4.387   1.00 30.69 ? 166 ARG A NH2 1 
ATOM   12   N N   . TYR A 1 167 ? -18.419 1.907   2.726   1.00 45.53 ? 167 TYR A N   1 
ATOM   13   C CA  . TYR A 1 167 ? -17.913 2.725   3.835   1.00 46.24 ? 167 TYR A CA  1 
ATOM   14   C C   . TYR A 1 167 ? -17.139 1.919   4.898   1.00 44.83 ? 167 TYR A C   1 
ATOM   15   O O   . TYR A 1 167 ? -17.697 1.026   5.539   1.00 45.48 ? 167 TYR A O   1 
ATOM   16   C CB  . TYR A 1 167 ? -19.034 3.568   4.493   1.00 47.65 ? 167 TYR A CB  1 
ATOM   17   C CG  . TYR A 1 167 ? -18.590 4.302   5.747   1.00 49.84 ? 167 TYR A CG  1 
ATOM   18   C CD1 . TYR A 1 167 ? -17.786 5.431   5.668   1.00 51.35 ? 167 TYR A CD1 1 
ATOM   19   C CD2 . TYR A 1 167 ? -18.933 3.835   7.008   1.00 51.38 ? 167 TYR A CD2 1 
ATOM   20   C CE1 . TYR A 1 167 ? -17.346 6.087   6.813   1.00 52.67 ? 167 TYR A CE1 1 
ATOM   21   C CE2 . TYR A 1 167 ? -18.498 4.482   8.161   1.00 52.75 ? 167 TYR A CE2 1 
ATOM   22   C CZ  . TYR A 1 167 ? -17.702 5.607   8.059   1.00 54.00 ? 167 TYR A CZ  1 
ATOM   23   O OH  . TYR A 1 167 ? -17.271 6.246   9.199   1.00 56.16 ? 167 TYR A OH  1 
ATOM   24   N N   . ILE A 1 168 ? -15.869 2.283   5.122   1.00 42.27 ? 168 ILE A N   1 
ATOM   25   C CA  . ILE A 1 168 ? -15.035 1.674   6.157   1.00 40.20 ? 168 ILE A CA  1 
ATOM   26   C C   . ILE A 1 168 ? -14.631 2.790   7.125   1.00 38.59 ? 168 ILE A C   1 
ATOM   27   O O   . ILE A 1 168 ? -14.114 3.810   6.676   1.00 38.31 ? 168 ILE A O   1 
ATOM   28   C CB  . ILE A 1 168 ? -13.795 1.009   5.516   1.00 39.96 ? 168 ILE A CB  1 
ATOM   29   C CG1 . ILE A 1 168 ? -14.214 -0.042  4.481   1.00 40.90 ? 168 ILE A CG1 1 
ATOM   30   C CG2 . ILE A 1 168 ? -12.878 0.410   6.581   1.00 39.72 ? 168 ILE A CG2 1 
ATOM   31   C CD1 . ILE A 1 168 ? -13.106 -0.591  3.650   1.00 41.99 ? 168 ILE A CD1 1 
ATOM   32   N N   . PRO A 1 169 ? -14.873 2.650   8.440   1.00 37.84 ? 169 PRO A N   1 
ATOM   33   C CA  . PRO A 1 169 ? -14.515 3.737   9.370   1.00 36.57 ? 169 PRO A CA  1 
ATOM   34   C C   . PRO A 1 169 ? -13.014 3.982   9.452   1.00 34.61 ? 169 PRO A C   1 
ATOM   35   O O   . PRO A 1 169 ? -12.238 3.029   9.499   1.00 34.58 ? 169 PRO A O   1 
ATOM   36   C CB  . PRO A 1 169 ? -15.087 3.262   10.714  1.00 37.93 ? 169 PRO A CB  1 
ATOM   37   C CG  . PRO A 1 169 ? -16.100 2.215   10.348  1.00 38.92 ? 169 PRO A CG  1 
ATOM   38   C CD  . PRO A 1 169 ? -15.515 1.530   9.150   1.00 37.57 ? 169 PRO A CD  1 
ATOM   39   N N   . SER A 1 170 ? -12.596 5.260   9.460   1.00 32.88 ? 170 SER A N   1 
ATOM   40   C CA  . SER A 1 170 ? -11.169 5.582   9.570   1.00 31.48 ? 170 SER A CA  1 
ATOM   41   C C   . SER A 1 170 ? -10.650 5.507   11.022  1.00 29.32 ? 170 SER A C   1 
ATOM   42   O O   . SER A 1 170 ? -9.440  5.486   11.242  1.00 29.69 ? 170 SER A O   1 
ATOM   43   C CB  . SER A 1 170 ? -10.880 6.951   8.970   1.00 33.04 ? 170 SER A CB  1 
ATOM   44   O OG  . SER A 1 170 ? -11.627 7.930   9.668   1.00 36.54 ? 170 SER A OG  1 
ATOM   45   N N   . LEU A 1 171 ? -11.557 5.505   12.011  1.00 27.19 ? 171 LEU A N   1 
ATOM   46   C CA  . LEU A 1 171 ? -11.170 5.391   13.405  1.00 26.15 ? 171 LEU A CA  1 
ATOM   47   C C   . LEU A 1 171 ? -11.491 3.994   13.911  1.00 25.45 ? 171 LEU A C   1 
ATOM   48   O O   . LEU A 1 171 ? -12.491 3.398   13.504  1.00 25.13 ? 171 LEU A O   1 
ATOM   49   C CB  . LEU A 1 171 ? -11.953 6.397   14.270  1.00 26.38 ? 171 LEU A CB  1 
ATOM   50   C CG  . LEU A 1 171 ? -11.758 7.861   13.907  1.00 28.73 ? 171 LEU A CG  1 
ATOM   51   C CD1 . LEU A 1 171 ? -12.624 8.742   14.778  1.00 29.89 ? 171 LEU A CD1 1 
ATOM   52   C CD2 . LEU A 1 171 ? -10.276 8.261   14.026  1.00 30.49 ? 171 LEU A CD2 1 
ATOM   53   N N   . PRO A 1 172 ? -10.698 3.490   14.861  1.00 24.96 ? 172 PRO A N   1 
ATOM   54   C CA  . PRO A 1 172 ? -11.054 2.210   15.488  1.00 24.90 ? 172 PRO A CA  1 
ATOM   55   C C   . PRO A 1 172 ? -12.247 2.389   16.429  1.00 25.71 ? 172 PRO A C   1 
ATOM   56   O O   . PRO A 1 172 ? -12.526 3.498   16.902  1.00 25.34 ? 172 PRO A O   1 
ATOM   57   C CB  . PRO A 1 172 ? -9.798  1.852   16.279  1.00 25.66 ? 172 PRO A CB  1 
ATOM   58   C CG  . PRO A 1 172 ? -9.206  3.160   16.644  1.00 26.47 ? 172 PRO A CG  1 
ATOM   59   C CD  . PRO A 1 172 ? -9.522  4.107   15.508  1.00 24.90 ? 172 PRO A CD  1 
ATOM   60   N N   . ASP A 1 173 ? -12.970 1.310   16.684  1.00 25.74 ? 173 ASP A N   1 
ATOM   61   C CA  . ASP A 1 173 ? -14.088 1.290   17.617  1.00 28.10 ? 173 ASP A CA  1 
ATOM   62   C C   . ASP A 1 173 ? -13.616 1.395   19.075  1.00 28.49 ? 173 ASP A C   1 
ATOM   63   O O   . ASP A 1 173 ? -14.334 1.942   19.914  1.00 29.72 ? 173 ASP A O   1 
ATOM   64   C CB  . ASP A 1 173 ? -14.844 -0.025  17.442  1.00 32.72 ? 173 ASP A CB  1 
ATOM   65   C CG  . ASP A 1 173 ? -16.114 0.160   16.660  1.00 42.72 ? 173 ASP A CG  1 
ATOM   66   O OD1 . ASP A 1 173 ? -16.123 1.009   15.735  1.00 44.10 ? 173 ASP A OD1 1 
ATOM   67   O OD2 . ASP A 1 173 ? -17.110 -0.517  16.987  1.00 47.16 ? 173 ASP A OD2 1 
ATOM   68   N N   . ARG A 1 174 ? -12.448 0.824   19.387  1.00 27.73 ? 174 ARG A N   1 
ATOM   69   C CA  . ARG A 1 174 ? -11.865 0.835   20.731  1.00 28.06 ? 174 ARG A CA  1 
ATOM   70   C C   . ARG A 1 174 ? -10.348 0.942   20.647  1.00 27.67 ? 174 ARG A C   1 
ATOM   71   O O   . ARG A 1 174 ? -9.737  0.489   19.678  1.00 26.85 ? 174 ARG A O   1 
ATOM   72   C CB  . ARG A 1 174 ? -12.194 -0.469  21.505  1.00 30.40 ? 174 ARG A CB  1 
ATOM   73   C CG  . ARG A 1 174 ? -13.655 -0.696  21.843  1.00 35.24 ? 174 ARG A CG  1 
ATOM   74   C CD  . ARG A 1 174 ? -14.145 0.292   22.885  1.00 40.27 ? 174 ARG A CD  1 
ATOM   75   N NE  . ARG A 1 174 ? -13.878 -0.174  24.246  1.00 45.98 ? 174 ARG A NE  1 
ATOM   76   C CZ  . ARG A 1 174 ? -14.685 -0.971  24.940  1.00 49.04 ? 174 ARG A CZ  1 
ATOM   77   N NH1 . ARG A 1 174 ? -14.372 -1.326  26.179  1.00 49.00 ? 174 ARG A NH1 1 
ATOM   78   N NH2 . ARG A 1 174 ? -15.818 -1.411  24.402  1.00 49.02 ? 174 ARG A NH2 1 
ATOM   79   N N   . ILE A 1 175 ? -9.733  1.512   21.677  1.00 26.95 ? 175 ILE A N   1 
ATOM   80   C CA  . ILE A 1 175 ? -8.288  1.565   21.807  1.00 27.41 ? 175 ILE A CA  1 
ATOM   81   C C   . ILE A 1 175 ? -7.999  1.102   23.213  1.00 28.95 ? 175 ILE A C   1 
ATOM   82   O O   . ILE A 1 175 ? -8.380  1.787   24.162  1.00 29.83 ? 175 ILE A O   1 
ATOM   83   C CB  . ILE A 1 175 ? -7.658  2.943   21.540  1.00 27.56 ? 175 ILE A CB  1 
ATOM   84   C CG1 . ILE A 1 175 ? -7.940  3.418   20.093  1.00 27.39 ? 175 ILE A CG1 1 
ATOM   85   C CG2 . ILE A 1 175 ? -6.146  2.863   21.798  1.00 28.13 ? 175 ILE A CG2 1 
ATOM   86   C CD1 . ILE A 1 175 ? -7.479  4.771   19.787  1.00 28.84 ? 175 ILE A CD1 1 
ATOM   87   N N   . LEU A 1 176 ? -7.402  -0.094  23.358  1.00 28.06 ? 176 LEU A N   1 
ATOM   88   C CA  . LEU A 1 176 ? -7.113  -0.652  24.681  1.00 28.11 ? 176 LEU A CA  1 
ATOM   89   C C   . LEU A 1 176 ? -5.629  -0.502  24.989  1.00 27.51 ? 176 LEU A C   1 
ATOM   90   O O   . LEU A 1 176 ? -4.810  -0.645  24.085  1.00 26.92 ? 176 LEU A O   1 
ATOM   91   C CB  . LEU A 1 176 ? -7.517  -2.141  24.706  1.00 28.75 ? 176 LEU A CB  1 
ATOM   92   C CG  . LEU A 1 176 ? -8.931  -2.455  24.236  1.00 30.84 ? 176 LEU A CG  1 
ATOM   93   C CD1 . LEU A 1 176 ? -9.170  -3.978  24.170  1.00 31.64 ? 176 LEU A CD1 1 
ATOM   94   C CD2 . LEU A 1 176 ? -9.969  -1.732  25.075  1.00 31.89 ? 176 LEU A CD2 1 
ATOM   95   N N   . ASP A 1 177 ? -5.271  -0.156  26.240  1.00 27.26 ? 177 ASP A N   1 
ATOM   96   C CA  . ASP A 1 177 ? -3.866  0.011   26.599  1.00 27.89 ? 177 ASP A CA  1 
ATOM   97   C C   . ASP A 1 177 ? -3.213  -1.359  26.644  1.00 27.27 ? 177 ASP A C   1 
ATOM   98   O O   . ASP A 1 177 ? -3.801  -2.314  27.128  1.00 27.87 ? 177 ASP A O   1 
ATOM   99   C CB  . ASP A 1 177 ? -3.708  0.734   27.959  1.00 31.48 ? 177 ASP A CB  1 
ATOM   100  C CG  . ASP A 1 177 ? -2.371  1.426   28.166  1.00 40.82 ? 177 ASP A CG  1 
ATOM   101  O OD1 . ASP A 1 177 ? -1.546  1.433   27.219  1.00 43.21 ? 177 ASP A OD1 1 
ATOM   102  O OD2 . ASP A 1 177 ? -2.145  1.967   29.274  1.00 44.50 ? 177 ASP A OD2 1 
ATOM   103  N N   . ALA A 1 178 ? -2.006  -1.473  26.114  1.00 26.29 ? 178 ALA A N   1 
ATOM   104  C CA  . ALA A 1 178 ? -1.261  -2.737  26.118  1.00 25.01 ? 178 ALA A CA  1 
ATOM   105  C C   . ALA A 1 178 ? 0.139   -2.449  26.683  1.00 25.49 ? 178 ALA A C   1 
ATOM   106  O O   . ALA A 1 178 ? 1.134   -2.615  25.986  1.00 25.52 ? 178 ALA A O   1 
ATOM   107  C CB  . ALA A 1 178 ? -1.182  -3.312  24.688  1.00 24.22 ? 178 ALA A CB  1 
ATOM   108  N N   . PRO A 1 179 ? 0.237   -1.973  27.951  1.00 26.05 ? 179 PRO A N   1 
ATOM   109  C CA  . PRO A 1 179 ? 1.561   -1.655  28.508  1.00 26.07 ? 179 PRO A CA  1 
ATOM   110  C C   . PRO A 1 179 ? 2.446   -2.878  28.584  1.00 25.77 ? 179 PRO A C   1 
ATOM   111  O O   . PRO A 1 179 ? 1.950   -3.969  28.869  1.00 26.02 ? 179 PRO A O   1 
ATOM   112  C CB  . PRO A 1 179 ? 1.237   -1.126  29.917  1.00 27.57 ? 179 PRO A CB  1 
ATOM   113  C CG  . PRO A 1 179 ? -0.104  -1.748  30.235  1.00 28.06 ? 179 PRO A CG  1 
ATOM   114  C CD  . PRO A 1 179 ? -0.832  -1.736  28.940  1.00 26.69 ? 179 PRO A CD  1 
ATOM   115  N N   . GLU A 1 180 ? 3.753   -2.700  28.333  1.00 25.71 ? 180 GLU A N   1 
ATOM   116  C CA  . GLU A 1 180 ? 4.738   -3.772  28.401  1.00 26.06 ? 180 GLU A CA  1 
ATOM   117  C C   . GLU A 1 180 ? 4.587   -4.833  27.331  1.00 25.69 ? 180 GLU A C   1 
ATOM   118  O O   . GLU A 1 180 ? 5.232   -5.886  27.445  1.00 26.85 ? 180 GLU A O   1 
ATOM   119  C CB  . GLU A 1 180 ? 4.802   -4.430  29.782  1.00 29.28 ? 180 GLU A CB  1 
ATOM   120  C CG  . GLU A 1 180 ? 5.064   -3.448  30.911  1.00 38.66 ? 180 GLU A CG  1 
ATOM   121  C CD  . GLU A 1 180 ? 6.439   -3.571  31.524  1.00 51.83 ? 180 GLU A CD  1 
ATOM   122  O OE1 . GLU A 1 180 ? 7.361   -4.056  30.827  1.00 55.12 ? 180 GLU A OE1 1 
ATOM   123  O OE2 . GLU A 1 180 ? 6.600   -3.173  32.702  1.00 57.25 ? 180 GLU A OE2 1 
ATOM   124  N N   . ILE A 1 181 ? 3.809   -4.578  26.250  1.00 24.18 ? 181 ILE A N   1 
ATOM   125  C CA  . ILE A 1 181 ? 3.737   -5.561  25.144  1.00 23.88 ? 181 ILE A CA  1 
ATOM   126  C C   . ILE A 1 181 ? 5.156   -5.783  24.561  1.00 24.19 ? 181 ILE A C   1 
ATOM   127  O O   . ILE A 1 181 ? 5.937   -4.833  24.482  1.00 24.32 ? 181 ILE A O   1 
ATOM   128  C CB  . ILE A 1 181 ? 2.705   -5.184  24.057  1.00 24.49 ? 181 ILE A CB  1 
ATOM   129  C CG1 . ILE A 1 181 ? 2.348   -6.399  23.169  1.00 25.52 ? 181 ILE A CG1 1 
ATOM   130  C CG2 . ILE A 1 181 ? 3.171   -3.958  23.231  1.00 25.44 ? 181 ILE A CG2 1 
ATOM   131  C CD1 . ILE A 1 181 ? 1.070   -6.214  22.357  1.00 26.23 ? 181 ILE A CD1 1 
ATOM   132  N N   . ARG A 1 182 ? 5.510   -7.039  24.309  1.00 23.51 ? 182 ARG A N   1 
ATOM   133  C CA  . ARG A 1 182 ? 6.857   -7.364  23.848  1.00 24.70 ? 182 ARG A CA  1 
ATOM   134  C C   . ARG A 1 182 ? 7.001   -7.043  22.375  1.00 24.47 ? 182 ARG A C   1 
ATOM   135  O O   . ARG A 1 182 ? 6.290   -7.607  21.567  1.00 24.60 ? 182 ARG A O   1 
ATOM   136  C CB  . ARG A 1 182 ? 7.166   -8.838  24.123  1.00 27.67 ? 182 ARG A CB  1 
ATOM   137  C CG  . ARG A 1 182 ? 8.638   -9.173  23.971  1.00 33.60 ? 182 ARG A CG  1 
ATOM   138  C CD  . ARG A 1 182 ? 8.972   -10.498 24.620  1.00 37.10 ? 182 ARG A CD  1 
ATOM   139  N NE  . ARG A 1 182 ? 9.130   -10.355 26.065  1.00 40.31 ? 182 ARG A NE  1 
ATOM   140  C CZ  . ARG A 1 182 ? 10.304  -10.220 26.680  1.00 41.54 ? 182 ARG A CZ  1 
ATOM   141  N NH1 . ARG A 1 182 ? 10.357  -10.087 27.994  1.00 41.19 ? 182 ARG A NH1 1 
ATOM   142  N NH2 . ARG A 1 182 ? 11.434  -10.249 25.984  1.00 40.95 ? 182 ARG A NH2 1 
ATOM   143  N N   . ASN A 1 183 ? 7.895   -6.103  22.032  1.00 24.56 ? 183 ASN A N   1 
ATOM   144  C CA  . ASN A 1 183 ? 8.088   -5.697  20.644  1.00 24.72 ? 183 ASN A CA  1 
ATOM   145  C C   . ASN A 1 183 ? 9.023   -6.703  19.955  1.00 25.48 ? 183 ASN A C   1 
ATOM   146  O O   . ASN A 1 183 ? 10.191  -6.408  19.678  1.00 26.18 ? 183 ASN A O   1 
ATOM   147  C CB  . ASN A 1 183 ? 8.663   -4.281  20.590  1.00 25.75 ? 183 ASN A CB  1 
ATOM   148  C CG  . ASN A 1 183 ? 8.757   -3.728  19.189  1.00 28.11 ? 183 ASN A CG  1 
ATOM   149  O OD1 . ASN A 1 183 ? 8.176   -4.282  18.241  1.00 28.22 ? 183 ASN A OD1 1 
ATOM   150  N ND2 . ASN A 1 183 ? 9.443   -2.593  19.046  1.00 28.63 ? 183 ASN A ND2 1 
ATOM   151  N N   . ASP A 1 184 ? 8.529   -7.910  19.762  1.00 24.70 ? 184 ASP A N   1 
ATOM   152  C CA  . ASP A 1 184 ? 9.280   -8.995  19.155  1.00 25.18 ? 184 ASP A CA  1 
ATOM   153  C C   . ASP A 1 184 ? 8.406   -9.494  18.016  1.00 25.68 ? 184 ASP A C   1 
ATOM   154  O O   . ASP A 1 184 ? 7.283   -9.974  18.221  1.00 26.09 ? 184 ASP A O   1 
ATOM   155  C CB  . ASP A 1 184 ? 9.547   -10.095 20.198  1.00 26.06 ? 184 ASP A CB  1 
ATOM   156  C CG  . ASP A 1 184 ? 10.407  -11.259 19.740  1.00 27.93 ? 184 ASP A CG  1 
ATOM   157  O OD1 . ASP A 1 184 ? 10.212  -11.729 18.608  1.00 28.26 ? 184 ASP A OD1 1 
ATOM   158  O OD2 . ASP A 1 184 ? 11.247  -11.725 20.539  1.00 30.00 ? 184 ASP A OD2 1 
ATOM   159  N N   . TYR A 1 185 ? 8.917   -9.341  16.788  1.00 25.06 ? 185 TYR A N   1 
ATOM   160  C CA  . TYR A 1 185 ? 8.173   -9.690  15.589  1.00 23.71 ? 185 TYR A CA  1 
ATOM   161  C C   . TYR A 1 185 ? 7.686   -11.123 15.527  1.00 22.77 ? 185 TYR A C   1 
ATOM   162  O O   . TYR A 1 185 ? 6.637   -11.382 14.959  1.00 23.50 ? 185 TYR A O   1 
ATOM   163  C CB  . TYR A 1 185 ? 9.103   -9.469  14.387  1.00 23.99 ? 185 TYR A CB  1 
ATOM   164  C CG  . TYR A 1 185 ? 8.412   -9.562  13.053  1.00 24.95 ? 185 TYR A CG  1 
ATOM   165  C CD1 . TYR A 1 185 ? 7.695   -8.491  12.551  1.00 26.29 ? 185 TYR A CD1 1 
ATOM   166  C CD2 . TYR A 1 185 ? 8.551   -10.687 12.252  1.00 26.23 ? 185 TYR A CD2 1 
ATOM   167  C CE1 . TYR A 1 185 ? 7.080   -8.554  11.315  1.00 26.47 ? 185 TYR A CE1 1 
ATOM   168  C CE2 . TYR A 1 185 ? 7.937   -10.763 11.006  1.00 26.77 ? 185 TYR A CE2 1 
ATOM   169  C CZ  . TYR A 1 185 ? 7.198   -9.691  10.547  1.00 27.60 ? 185 TYR A CZ  1 
ATOM   170  O OH  . TYR A 1 185 ? 6.610   -9.710  9.314   1.00 29.50 ? 185 TYR A OH  1 
ATOM   171  N N   . TYR A 1 186 ? 8.433   -12.049 16.077  1.00 21.64 ? 186 TYR A N   1 
ATOM   172  C CA  . TYR A 1 186 ? 8.157   -13.479 15.926  1.00 21.91 ? 186 TYR A CA  1 
ATOM   173  C C   . TYR A 1 186 ? 7.050   -14.025 16.831  1.00 22.69 ? 186 TYR A C   1 
ATOM   174  O O   . TYR A 1 186 ? 6.605   -15.139 16.608  1.00 24.64 ? 186 TYR A O   1 
ATOM   175  C CB  . TYR A 1 186 ? 9.441   -14.274 16.111  1.00 22.67 ? 186 TYR A CB  1 
ATOM   176  C CG  . TYR A 1 186 ? 10.510  -13.820 15.147  1.00 23.77 ? 186 TYR A CG  1 
ATOM   177  C CD1 . TYR A 1 186 ? 10.486  -14.222 13.822  1.00 24.73 ? 186 TYR A CD1 1 
ATOM   178  C CD2 . TYR A 1 186 ? 11.428  -12.843 15.509  1.00 25.94 ? 186 TYR A CD2 1 
ATOM   179  C CE1 . TYR A 1 186 ? 11.421  -13.756 12.909  1.00 25.55 ? 186 TYR A CE1 1 
ATOM   180  C CE2 . TYR A 1 186 ? 12.367  -12.364 14.605  1.00 26.89 ? 186 TYR A CE2 1 
ATOM   181  C CZ  . TYR A 1 186 ? 12.366  -12.835 13.304  1.00 27.05 ? 186 TYR A CZ  1 
ATOM   182  O OH  . TYR A 1 186 ? 13.300  -12.425 12.381  1.00 28.13 ? 186 TYR A OH  1 
ATOM   183  N N   . LEU A 1 187 ? 6.640   -13.266 17.836  1.00 20.25 ? 187 LEU A N   1 
ATOM   184  C CA  . LEU A 1 187 ? 5.649   -13.738 18.799  1.00 19.14 ? 187 LEU A CA  1 
ATOM   185  C C   . LEU A 1 187 ? 4.217   -13.575 18.348  1.00 19.93 ? 187 LEU A C   1 
ATOM   186  O O   . LEU A 1 187 ? 3.932   -12.697 17.552  1.00 21.14 ? 187 LEU A O   1 
ATOM   187  C CB  . LEU A 1 187 ? 5.861   -13.060 20.166  1.00 18.94 ? 187 LEU A CB  1 
ATOM   188  C CG  . LEU A 1 187 ? 7.304   -13.133 20.690  1.00 20.75 ? 187 LEU A CG  1 
ATOM   189  C CD1 . LEU A 1 187 ? 7.405   -12.463 22.047  1.00 21.87 ? 187 LEU A CD1 1 
ATOM   190  C CD2 . LEU A 1 187 ? 7.773   -14.586 20.781  1.00 21.57 ? 187 LEU A CD2 1 
ATOM   191  N N   . ASN A 1 188 ? 3.316   -14.429 18.846  1.00 18.32 ? 188 ASN A N   1 
ATOM   192  C CA  . ASN A 1 188 ? 1.903   -14.356 18.439  1.00 17.65 ? 188 ASN A CA  1 
ATOM   193  C C   . ASN A 1 188 ? 1.099   -14.088 19.731  1.00 17.94 ? 188 ASN A C   1 
ATOM   194  O O   . ASN A 1 188 ? 0.642   -15.002 20.383  1.00 17.80 ? 188 ASN A O   1 
ATOM   195  C CB  . ASN A 1 188 ? 1.537   -15.662 17.739  1.00 18.86 ? 188 ASN A CB  1 
ATOM   196  C CG  . ASN A 1 188 ? 2.127   -15.690 16.336  1.00 20.24 ? 188 ASN A CG  1 
ATOM   197  O OD1 . ASN A 1 188 ? 1.591   -15.079 15.397  1.00 20.75 ? 188 ASN A OD1 1 
ATOM   198  N ND2 . ASN A 1 188 ? 3.279   -16.328 16.169  1.00 19.44 ? 188 ASN A ND2 1 
ATOM   199  N N   . LEU A 1 189 ? 1.017   -12.827 20.107  1.00 17.87 ? 189 LEU A N   1 
ATOM   200  C CA  . LEU A 1 189 ? 0.562   -12.412 21.433  1.00 17.24 ? 189 LEU A CA  1 
ATOM   201  C C   . LEU A 1 189 ? -0.919  -12.139 21.646  1.00 17.07 ? 189 LEU A C   1 
ATOM   202  O O   . LEU A 1 189 ? -1.297  -11.856 22.791  1.00 17.68 ? 189 LEU A O   1 
ATOM   203  C CB  . LEU A 1 189 ? 1.333   -11.183 21.870  1.00 18.14 ? 189 LEU A CB  1 
ATOM   204  C CG  . LEU A 1 189 ? 2.881   -11.390 21.879  1.00 20.58 ? 189 LEU A CG  1 
ATOM   205  C CD1 . LEU A 1 189 ? 3.598   -10.086 22.090  1.00 23.17 ? 189 LEU A CD1 1 
ATOM   206  C CD2 . LEU A 1 189 ? 3.285   -12.391 22.922  1.00 22.26 ? 189 LEU A CD2 1 
ATOM   207  N N   A VAL A 1 190 ? -1.740  -12.170 20.592  0.62 16.78 ? 190 VAL A N   1 
ATOM   208  N N   B VAL A 1 190 ? -1.743  -12.180 20.593  0.38 16.68 ? 190 VAL A N   1 
ATOM   209  C CA  A VAL A 1 190 ? -3.180  -11.940 20.755  0.62 17.29 ? 190 VAL A CA  1 
ATOM   210  C CA  B VAL A 1 190 ? -3.172  -11.883 20.746  0.38 16.97 ? 190 VAL A CA  1 
ATOM   211  C C   A VAL A 1 190 ? -4.045  -12.975 20.033  0.62 17.45 ? 190 VAL A C   1 
ATOM   212  C C   B VAL A 1 190 ? -4.074  -12.897 20.007  0.38 17.13 ? 190 VAL A C   1 
ATOM   213  O O   A VAL A 1 190 ? -3.669  -13.492 18.969  0.62 18.12 ? 190 VAL A O   1 
ATOM   214  O O   B VAL A 1 190 ? -3.732  -13.339 18.906  0.38 17.59 ? 190 VAL A O   1 
ATOM   215  C CB  A VAL A 1 190 ? -3.616  -10.502 20.367  0.62 18.65 ? 190 VAL A CB  1 
ATOM   216  C CB  B VAL A 1 190 ? -3.480  -10.427 20.293  0.38 17.88 ? 190 VAL A CB  1 
ATOM   217  C CG1 A VAL A 1 190 ? -3.082  -9.455  21.348  0.62 19.72 ? 190 VAL A CG1 1 
ATOM   218  C CG1 B VAL A 1 190 ? -4.908  -10.035 20.626  0.38 18.20 ? 190 VAL A CG1 1 
ATOM   219  C CG2 A VAL A 1 190 ? -3.220  -10.173 18.923  0.62 18.62 ? 190 VAL A CG2 1 
ATOM   220  C CG2 B VAL A 1 190 ? -2.502  -9.417  20.890  0.38 18.32 ? 190 VAL A CG2 1 
ATOM   221  N N   . ASP A 1 191 ? -5.233  -13.259 20.603  1.00 16.47 ? 191 ASP A N   1 
ATOM   222  C CA  . ASP A 1 191 ? -6.173  -14.164 19.947  1.00 17.15 ? 191 ASP A CA  1 
ATOM   223  C C   . ASP A 1 191 ? -7.563  -13.883 20.491  1.00 17.58 ? 191 ASP A C   1 
ATOM   224  O O   . ASP A 1 191 ? -7.715  -13.642 21.688  1.00 17.99 ? 191 ASP A O   1 
ATOM   225  C CB  . ASP A 1 191 ? -5.815  -15.649 20.130  1.00 18.24 ? 191 ASP A CB  1 
ATOM   226  C CG  . ASP A 1 191 ? -6.521  -16.550 19.108  1.00 21.03 ? 191 ASP A CG  1 
ATOM   227  O OD1 . ASP A 1 191 ? -6.825  -16.067 18.001  1.00 21.89 ? 191 ASP A OD1 1 
ATOM   228  O OD2 . ASP A 1 191 ? -6.750  -17.734 19.413  1.00 20.18 ? 191 ASP A OD2 1 
ATOM   229  N N   . TRP A 1 192 ? -8.541  -13.887 19.607  1.00 17.35 ? 192 TRP A N   1 
ATOM   230  C CA  . TRP A 1 192 ? -9.951  -13.577 19.910  1.00 17.87 ? 192 TRP A CA  1 
ATOM   231  C C   . TRP A 1 192 ? -10.755 -14.869 19.832  1.00 19.08 ? 192 TRP A C   1 
ATOM   232  O O   . TRP A 1 192 ? -10.791 -15.540 18.795  1.00 19.36 ? 192 TRP A O   1 
ATOM   233  C CB  . TRP A 1 192 ? -10.465 -12.546 18.908  1.00 17.97 ? 192 TRP A CB  1 
ATOM   234  C CG  . TRP A 1 192 ? -11.582 -11.679 19.420  1.00 18.71 ? 192 TRP A CG  1 
ATOM   235  C CD1 . TRP A 1 192 ? -12.625 -12.064 20.219  1.00 19.45 ? 192 TRP A CD1 1 
ATOM   236  C CD2 . TRP A 1 192 ? -11.811 -10.298 19.093  1.00 19.11 ? 192 TRP A CD2 1 
ATOM   237  N NE1 . TRP A 1 192 ? -13.482 -10.995 20.430  1.00 20.45 ? 192 TRP A NE1 1 
ATOM   238  C CE2 . TRP A 1 192 ? -13.015 -9.909  19.725  1.00 20.24 ? 192 TRP A CE2 1 
ATOM   239  C CE3 . TRP A 1 192 ? -11.148 -9.369  18.273  1.00 19.72 ? 192 TRP A CE3 1 
ATOM   240  C CZ2 . TRP A 1 192 ? -13.510 -8.603  19.646  1.00 20.54 ? 192 TRP A CZ2 1 
ATOM   241  C CZ3 . TRP A 1 192 ? -11.635 -8.071  18.208  1.00 20.38 ? 192 TRP A CZ3 1 
ATOM   242  C CH2 . TRP A 1 192 ? -12.829 -7.714  18.850  1.00 20.31 ? 192 TRP A CH2 1 
ATOM   243  N N   . SER A 1 193 ? -11.375 -15.249 20.952  1.00 18.83 ? 193 SER A N   1 
ATOM   244  C CA  . SER A 1 193 ? -12.057 -16.515 21.057  1.00 19.43 ? 193 SER A CA  1 
ATOM   245  C C   . SER A 1 193 ? -13.414 -16.554 20.389  1.00 21.46 ? 193 SER A C   1 
ATOM   246  O O   . SER A 1 193 ? -14.066 -15.513 20.224  1.00 21.68 ? 193 SER A O   1 
ATOM   247  C CB  . SER A 1 193 ? -12.223 -16.891 22.533  1.00 20.31 ? 193 SER A CB  1 
ATOM   248  O OG  . SER A 1 193 ? -13.373 -16.293 23.107  1.00 20.26 ? 193 SER A OG  1 
ATOM   249  N N   . SER A 1 194 ? -13.909 -17.771 20.149  1.00 22.22 ? 194 SER A N   1 
ATOM   250  C CA  . SER A 1 194 ? -15.264 -17.947 19.634  1.00 24.83 ? 194 SER A CA  1 
ATOM   251  C C   . SER A 1 194 ? -16.330 -17.481 20.660  1.00 26.19 ? 194 SER A C   1 
ATOM   252  O O   . SER A 1 194 ? -17.471 -17.234 20.279  1.00 28.32 ? 194 SER A O   1 
ATOM   253  C CB  . SER A 1 194 ? -15.493 -19.405 19.253  1.00 27.31 ? 194 SER A CB  1 
ATOM   254  O OG  . SER A 1 194 ? -15.371 -20.218 20.409  1.00 29.74 ? 194 SER A OG  1 
ATOM   255  N N   . GLY A 1 195 ? -15.954 -17.366 21.945  1.00 25.65 ? 195 GLY A N   1 
ATOM   256  C CA  . GLY A 1 195 ? -16.796 -16.850 23.014  1.00 25.41 ? 195 GLY A CA  1 
ATOM   257  C C   . GLY A 1 195 ? -16.690 -15.339 23.180  1.00 24.06 ? 195 GLY A C   1 
ATOM   258  O O   . GLY A 1 195 ? -17.167 -14.795 24.182  1.00 24.00 ? 195 GLY A O   1 
ATOM   259  N N   . ASN A 1 196 ? -16.004 -14.653 22.218  1.00 22.76 ? 196 ASN A N   1 
ATOM   260  C CA  . ASN A 1 196 ? -15.867 -13.200 22.167  1.00 22.28 ? 196 ASN A CA  1 
ATOM   261  C C   . ASN A 1 196 ? -15.028 -12.634 23.307  1.00 22.61 ? 196 ASN A C   1 
ATOM   262  O O   . ASN A 1 196 ? -15.336 -11.574 23.871  1.00 23.94 ? 196 ASN A O   1 
ATOM   263  C CB  . ASN A 1 196 ? -17.268 -12.542 22.091  1.00 23.49 ? 196 ASN A CB  1 
ATOM   264  C CG  . ASN A 1 196 ? -17.269 -11.154 21.488  1.00 26.90 ? 196 ASN A CG  1 
ATOM   265  O OD1 . ASN A 1 196 ? -16.390 -10.780 20.701  1.00 26.48 ? 196 ASN A OD1 1 
ATOM   266  N ND2 . ASN A 1 196 ? -18.289 -10.358 21.846  1.00 28.34 ? 196 ASN A ND2 1 
ATOM   267  N N   . VAL A 1 197 ? -13.918 -13.334 23.620  1.00 20.06 ? 197 VAL A N   1 
ATOM   268  C CA  . VAL A 1 197 ? -12.987 -12.908 24.647  1.00 18.90 ? 197 VAL A CA  1 
ATOM   269  C C   . VAL A 1 197 ? -11.620 -12.768 23.980  1.00 18.13 ? 197 VAL A C   1 
ATOM   270  O O   . VAL A 1 197 ? -11.162 -13.712 23.332  1.00 19.02 ? 197 VAL A O   1 
ATOM   271  C CB  . VAL A 1 197 ? -12.900 -13.923 25.818  1.00 19.65 ? 197 VAL A CB  1 
ATOM   272  C CG1 . VAL A 1 197 ? -11.873 -13.472 26.856  1.00 20.78 ? 197 VAL A CG1 1 
ATOM   273  C CG2 . VAL A 1 197 ? -14.269 -14.146 26.480  1.00 20.96 ? 197 VAL A CG2 1 
ATOM   274  N N   . LEU A 1 198 ? -10.980 -11.615 24.127  1.00 17.85 ? 198 LEU A N   1 
ATOM   275  C CA  . LEU A 1 198 ? -9.635  -11.398 23.589  1.00 18.73 ? 198 LEU A CA  1 
ATOM   276  C C   . LEU A 1 198 ? -8.649  -11.794 24.649  1.00 18.60 ? 198 LEU A C   1 
ATOM   277  O O   . LEU A 1 198 ? -8.755  -11.307 25.770  1.00 19.10 ? 198 LEU A O   1 
ATOM   278  C CB  . LEU A 1 198 ? -9.412  -9.891  23.350  1.00 20.92 ? 198 LEU A CB  1 
ATOM   279  C CG  . LEU A 1 198 ? -9.418  -9.306  21.967  1.00 24.01 ? 198 LEU A CG  1 
ATOM   280  C CD1 . LEU A 1 198 ? -8.936  -7.834  22.021  1.00 25.12 ? 198 LEU A CD1 1 
ATOM   281  C CD2 . LEU A 1 198 ? -8.528  -10.080 21.014  1.00 22.60 ? 198 LEU A CD2 1 
ATOM   282  N N   . ALA A 1 199 ? -7.611  -12.568 24.279  1.00 17.31 ? 199 ALA A N   1 
ATOM   283  C CA  . ALA A 1 199 ? -6.514  -12.928 25.170  1.00 17.78 ? 199 ALA A CA  1 
ATOM   284  C C   . ALA A 1 199 ? -5.347  -12.096 24.689  1.00 17.59 ? 199 ALA A C   1 
ATOM   285  O O   . ALA A 1 199 ? -5.076  -12.088 23.479  1.00 17.90 ? 199 ALA A O   1 
ATOM   286  C CB  . ALA A 1 199 ? -6.170  -14.410 25.005  1.00 17.74 ? 199 ALA A CB  1 
ATOM   287  N N   . VAL A 1 200 ? -4.676  -11.384 25.605  1.00 17.22 ? 200 VAL A N   1 
ATOM   288  C CA  . VAL A 1 200 ? -3.540  -10.520 25.227  1.00 18.43 ? 200 VAL A CA  1 
ATOM   289  C C   . VAL A 1 200 ? -2.403  -10.816 26.147  1.00 18.87 ? 200 VAL A C   1 
ATOM   290  O O   . VAL A 1 200 ? -2.553  -10.673 27.362  1.00 19.09 ? 200 VAL A O   1 
ATOM   291  C CB  . VAL A 1 200 ? -3.935  -9.025  25.364  1.00 20.18 ? 200 VAL A CB  1 
ATOM   292  C CG1 . VAL A 1 200 ? -2.823  -8.117  24.846  1.00 21.23 ? 200 VAL A CG1 1 
ATOM   293  C CG2 . VAL A 1 200 ? -5.279  -8.731  24.684  1.00 21.56 ? 200 VAL A CG2 1 
ATOM   294  N N   . ALA A 1 201 ? -1.228  -11.144 25.589  1.00 18.59 ? 201 ALA A N   1 
ATOM   295  C CA  . ALA A 1 201 ? -0.065  -11.414 26.392  1.00 20.25 ? 201 ALA A CA  1 
ATOM   296  C C   . ALA A 1 201 ? 0.726   -10.113 26.533  1.00 20.90 ? 201 ALA A C   1 
ATOM   297  O O   . ALA A 1 201 ? 1.185   -9.540  25.540  1.00 21.18 ? 201 ALA A O   1 
ATOM   298  C CB  . ALA A 1 201 ? 0.787   -12.469 25.718  1.00 21.03 ? 201 ALA A CB  1 
ATOM   299  N N   . LEU A 1 202 ? 0.860   -9.630  27.776  1.00 20.93 ? 202 LEU A N   1 
ATOM   300  C CA  . LEU A 1 202 ? 1.641   -8.436  28.064  1.00 21.23 ? 202 LEU A CA  1 
ATOM   301  C C   . LEU A 1 202 ? 2.817   -8.831  28.945  1.00 23.48 ? 202 LEU A C   1 
ATOM   302  O O   . LEU A 1 202 ? 2.652   -8.988  30.164  1.00 24.37 ? 202 LEU A O   1 
ATOM   303  C CB  . LEU A 1 202 ? 0.781   -7.369  28.761  1.00 21.21 ? 202 LEU A CB  1 
ATOM   304  C CG  . LEU A 1 202 ? -0.430  -6.859  27.983  1.00 21.94 ? 202 LEU A CG  1 
ATOM   305  C CD1 . LEU A 1 202 ? -1.194  -5.795  28.815  1.00 22.50 ? 202 LEU A CD1 1 
ATOM   306  C CD2 . LEU A 1 202 ? -0.026  -6.309  26.619  1.00 22.15 ? 202 LEU A CD2 1 
ATOM   307  N N   . ASP A 1 203 ? 4.001   -8.977  28.323  1.00 23.81 ? 203 ASP A N   1 
ATOM   308  C CA  . ASP A 1 203 ? 5.245   -9.379  28.981  1.00 24.00 ? 203 ASP A CA  1 
ATOM   309  C C   . ASP A 1 203 ? 5.072   -10.768 29.642  1.00 23.05 ? 203 ASP A C   1 
ATOM   310  O O   . ASP A 1 203 ? 4.992   -11.763 28.907  1.00 22.55 ? 203 ASP A O   1 
ATOM   311  C CB  . ASP A 1 203 ? 5.811   -8.280  29.920  1.00 27.18 ? 203 ASP A CB  1 
ATOM   312  C CG  . ASP A 1 203 ? 7.133   -8.680  30.563  1.00 34.13 ? 203 ASP A CG  1 
ATOM   313  O OD1 . ASP A 1 203 ? 7.868   -9.495  29.958  1.00 33.78 ? 203 ASP A OD1 1 
ATOM   314  O OD2 . ASP A 1 203 ? 7.412   -8.209  31.684  1.00 38.89 ? 203 ASP A OD2 1 
ATOM   315  N N   . ASN A 1 204 ? 4.966   -10.851 30.980  1.00 23.63 ? 204 ASN A N   1 
ATOM   316  C CA  . ASN A 1 204 ? 4.844   -12.142 31.655  1.00 24.39 ? 204 ASN A CA  1 
ATOM   317  C C   . ASN A 1 204 ? 3.433   -12.476 32.090  1.00 23.66 ? 204 ASN A C   1 
ATOM   318  O O   . ASN A 1 204 ? 3.266   -13.387 32.887  1.00 24.61 ? 204 ASN A O   1 
ATOM   319  C CB  . ASN A 1 204 ? 5.780   -12.211 32.871  1.00 26.44 ? 204 ASN A CB  1 
ATOM   320  C CG  . ASN A 1 204 ? 5.433   -11.220 33.964  1.00 29.59 ? 204 ASN A CG  1 
ATOM   321  O OD1 . ASN A 1 204 ? 4.613   -10.316 33.782  1.00 29.34 ? 204 ASN A OD1 1 
ATOM   322  N ND2 . ASN A 1 204 ? 6.074   -11.353 35.122  1.00 31.34 ? 204 ASN A ND2 1 
ATOM   323  N N   . SER A 1 205 ? 2.438   -11.726 31.635  1.00 21.63 ? 205 SER A N   1 
ATOM   324  C CA  . SER A 1 205 ? 1.053   -11.957 32.025  1.00 21.79 ? 205 SER A CA  1 
ATOM   325  C C   . SER A 1 205 ? 0.149   -12.151 30.825  1.00 21.40 ? 205 SER A C   1 
ATOM   326  O O   . SER A 1 205 ? 0.439   -11.650 29.739  1.00 22.10 ? 205 SER A O   1 
ATOM   327  C CB  . SER A 1 205 ? 0.538   -10.773 32.837  1.00 24.04 ? 205 SER A CB  1 
ATOM   328  O OG  . SER A 1 205 ? 1.153   -10.669 34.109  1.00 27.04 ? 205 SER A OG  1 
ATOM   329  N N   . VAL A 1 206 ? -1.024  -12.791 31.038  1.00 20.03 ? 206 VAL A N   1 
ATOM   330  C CA  . VAL A 1 206 ? -2.026  -12.894 29.987  1.00 20.01 ? 206 VAL A CA  1 
ATOM   331  C C   . VAL A 1 206 ? -3.264  -12.263 30.581  1.00 19.63 ? 206 VAL A C   1 
ATOM   332  O O   . VAL A 1 206 ? -3.667  -12.613 31.708  1.00 19.37 ? 206 VAL A O   1 
ATOM   333  C CB  . VAL A 1 206 ? -2.325  -14.354 29.559  1.00 20.64 ? 206 VAL A CB  1 
ATOM   334  C CG1 . VAL A 1 206 ? -3.557  -14.431 28.650  1.00 21.62 ? 206 VAL A CG1 1 
ATOM   335  C CG2 . VAL A 1 206 ? -1.103  -14.979 28.902  1.00 20.59 ? 206 VAL A CG2 1 
ATOM   336  N N   . TYR A 1 207 ? -3.846  -11.307 29.864  1.00 18.85 ? 207 TYR A N   1 
ATOM   337  C CA  . TYR A 1 207 ? -5.091  -10.652 30.273  1.00 18.80 ? 207 TYR A CA  1 
ATOM   338  C C   . TYR A 1 207 ? -6.218  -11.109 29.346  1.00 18.99 ? 207 TYR A C   1 
ATOM   339  O O   . TYR A 1 207 ? -5.999  -11.344 28.157  1.00 18.96 ? 207 TYR A O   1 
ATOM   340  C CB  . TYR A 1 207 ? -4.944  -9.112  30.202  1.00 20.34 ? 207 TYR A CB  1 
ATOM   341  C CG  . TYR A 1 207 ? -4.027  -8.575  31.273  1.00 23.21 ? 207 TYR A CG  1 
ATOM   342  C CD1 . TYR A 1 207 ? -2.649  -8.582  31.102  1.00 25.42 ? 207 TYR A CD1 1 
ATOM   343  C CD2 . TYR A 1 207 ? -4.533  -8.093  32.476  1.00 25.45 ? 207 TYR A CD2 1 
ATOM   344  C CE1 . TYR A 1 207 ? -1.799  -8.142  32.106  1.00 27.75 ? 207 TYR A CE1 1 
ATOM   345  C CE2 . TYR A 1 207 ? -3.690  -7.665  33.491  1.00 27.13 ? 207 TYR A CE2 1 
ATOM   346  C CZ  . TYR A 1 207 ? -2.321  -7.702  33.303  1.00 29.57 ? 207 TYR A CZ  1 
ATOM   347  O OH  . TYR A 1 207 ? -1.474  -7.237  34.278  1.00 34.27 ? 207 TYR A OH  1 
ATOM   348  N N   . LEU A 1 208 ? -7.427  -11.187 29.876  1.00 18.47 ? 208 LEU A N   1 
ATOM   349  C CA  . LEU A 1 208 ? -8.598  -11.523 29.093  1.00 20.18 ? 208 LEU A CA  1 
ATOM   350  C C   . LEU A 1 208 ? -9.532  -10.329 29.111  1.00 22.00 ? 208 LEU A C   1 
ATOM   351  O O   . LEU A 1 208 ? -9.738  -9.726  30.159  1.00 23.28 ? 208 LEU A O   1 
ATOM   352  C CB  . LEU A 1 208 ? -9.323  -12.729 29.697  1.00 19.97 ? 208 LEU A CB  1 
ATOM   353  C CG  . LEU A 1 208 ? -8.500  -14.006 29.826  1.00 21.29 ? 208 LEU A CG  1 
ATOM   354  C CD1 . LEU A 1 208 ? -9.370  -15.106 30.451  1.00 22.35 ? 208 LEU A CD1 1 
ATOM   355  C CD2 . LEU A 1 208 ? -7.910  -14.445 28.467  1.00 21.84 ? 208 LEU A CD2 1 
ATOM   356  N N   . TRP A 1 209 ? -10.058 -9.960  27.958  1.00 21.85 ? 209 TRP A N   1 
ATOM   357  C CA  . TRP A 1 209 ? -10.979 -8.839  27.860  1.00 23.69 ? 209 TRP A CA  1 
ATOM   358  C C   . TRP A 1 209 ? -12.248 -9.370  27.216  1.00 24.32 ? 209 TRP A C   1 
ATOM   359  O O   . TRP A 1 209 ? -12.219 -9.836  26.068  1.00 22.89 ? 209 TRP A O   1 
ATOM   360  C CB  . TRP A 1 209 ? -10.351 -7.708  27.024  1.00 24.84 ? 209 TRP A CB  1 
ATOM   361  C CG  . TRP A 1 209 ? -11.224 -6.506  26.809  1.00 26.93 ? 209 TRP A CG  1 
ATOM   362  C CD1 . TRP A 1 209 ? -11.472 -5.501  27.699  1.00 28.65 ? 209 TRP A CD1 1 
ATOM   363  C CD2 . TRP A 1 209 ? -11.887 -6.140  25.597  1.00 27.16 ? 209 TRP A CD2 1 
ATOM   364  N NE1 . TRP A 1 209 ? -12.281 -4.549  27.124  1.00 29.01 ? 209 TRP A NE1 1 
ATOM   365  C CE2 . TRP A 1 209 ? -12.557 -4.921  25.835  1.00 28.57 ? 209 TRP A CE2 1 
ATOM   366  C CE3 . TRP A 1 209 ? -12.037 -6.757  24.349  1.00 27.43 ? 209 TRP A CE3 1 
ATOM   367  C CZ2 . TRP A 1 209 ? -13.321 -4.288  24.857  1.00 28.93 ? 209 TRP A CZ2 1 
ATOM   368  C CZ3 . TRP A 1 209 ? -12.771 -6.115  23.378  1.00 28.27 ? 209 TRP A CZ3 1 
ATOM   369  C CH2 . TRP A 1 209 ? -13.433 -4.913  23.646  1.00 28.58 ? 209 TRP A CH2 1 
ATOM   370  N N   A SER A 1 210 ? -13.370 -9.330  27.939  0.58 25.38 ? 210 SER A N   1 
ATOM   371  N N   B SER A 1 210 ? -13.358 -9.284  27.938  0.42 25.45 ? 210 SER A N   1 
ATOM   372  C CA  A SER A 1 210 ? -14.643 -9.797  27.395  0.58 27.20 ? 210 SER A CA  1 
ATOM   373  C CA  B SER A 1 210 ? -14.640 -9.705  27.411  0.42 27.26 ? 210 SER A CA  1 
ATOM   374  C C   A SER A 1 210 ? -15.233 -8.646  26.600  0.58 28.53 ? 210 SER A C   1 
ATOM   375  C C   B SER A 1 210 ? -15.139 -8.556  26.566  0.42 28.51 ? 210 SER A C   1 
ATOM   376  O O   A SER A 1 210 ? -15.593 -7.636  27.194  0.58 28.66 ? 210 SER A O   1 
ATOM   377  O O   B SER A 1 210 ? -15.353 -7.468  27.094  0.42 28.62 ? 210 SER A O   1 
ATOM   378  C CB  A SER A 1 210 ? -15.583 -10.218 28.520  0.58 29.23 ? 210 SER A CB  1 
ATOM   379  C CB  B SER A 1 210 ? -15.621 -9.965  28.547  0.42 29.38 ? 210 SER A CB  1 
ATOM   380  O OG  A SER A 1 210 ? -15.024 -11.290 29.264  0.58 31.59 ? 210 SER A OG  1 
ATOM   381  O OG  B SER A 1 210 ? -16.922 -10.211 28.043  0.42 32.41 ? 210 SER A OG  1 
ATOM   382  N N   . ALA A 1 211 ? -15.301 -8.771  25.263  1.00 29.21 ? 211 ALA A N   1 
ATOM   383  C CA  . ALA A 1 211 ? -15.769 -7.701  24.366  1.00 30.77 ? 211 ALA A CA  1 
ATOM   384  C C   . ALA A 1 211 ? -17.179 -7.195  24.637  1.00 33.79 ? 211 ALA A C   1 
ATOM   385  O O   . ALA A 1 211 ? -17.432 -6.001  24.481  1.00 35.01 ? 211 ALA A O   1 
ATOM   386  C CB  . ALA A 1 211 ? -15.640 -8.133  22.911  1.00 31.07 ? 211 ALA A CB  1 
ATOM   387  N N   . SER A 1 212 ? -18.072 -8.067  25.106  1.00 34.84 ? 212 SER A N   1 
ATOM   388  C CA  . SER A 1 212 ? -19.445 -7.670  25.372  1.00 37.08 ? 212 SER A CA  1 
ATOM   389  C C   . SER A 1 212 ? -19.625 -6.812  26.639  1.00 37.92 ? 212 SER A C   1 
ATOM   390  O O   . SER A 1 212 ? -20.502 -5.947  26.671  1.00 38.90 ? 212 SER A O   1 
ATOM   391  C CB  . SER A 1 212 ? -20.348 -8.899  25.415  1.00 40.30 ? 212 SER A CB  1 
ATOM   392  O OG  . SER A 1 212 ? -20.289 -9.529  26.684  1.00 45.11 ? 212 SER A OG  1 
ATOM   393  N N   . SER A 1 213 ? -18.830 -7.061  27.690  1.00 36.85 ? 213 SER A N   1 
ATOM   394  C CA  . SER A 1 213 ? -19.002 -6.342  28.958  1.00 35.99 ? 213 SER A CA  1 
ATOM   395  C C   . SER A 1 213 ? -17.888 -5.366  29.301  1.00 35.16 ? 213 SER A C   1 
ATOM   396  O O   . SER A 1 213 ? -18.074 -4.504  30.152  1.00 35.36 ? 213 SER A O   1 
ATOM   397  C CB  . SER A 1 213 ? -19.122 -7.342  30.098  1.00 36.97 ? 213 SER A CB  1 
ATOM   398  O OG  . SER A 1 213 ? -17.907 -8.072  30.187  1.00 39.24 ? 213 SER A OG  1 
ATOM   399  N N   . GLY A 1 214 ? -16.719 -5.559  28.707  1.00 33.50 ? 214 GLY A N   1 
ATOM   400  C CA  . GLY A 1 214 ? -15.546 -4.761  29.031  1.00 32.74 ? 214 GLY A CA  1 
ATOM   401  C C   . GLY A 1 214 ? -14.769 -5.278  30.238  1.00 31.09 ? 214 GLY A C   1 
ATOM   402  O O   . GLY A 1 214 ? -13.798 -4.644  30.649  1.00 32.36 ? 214 GLY A O   1 
ATOM   403  N N   A ASP A 1 215 ? -15.200 -6.405  30.833  0.60 29.96 ? 215 ASP A N   1 
ATOM   404  N N   B ASP A 1 215 ? -15.175 -6.436  30.797  0.40 29.90 ? 215 ASP A N   1 
ATOM   405  C CA  A ASP A 1 215 ? -14.525 -6.973  31.991  0.60 29.79 ? 215 ASP A CA  1 
ATOM   406  C CA  B ASP A 1 215 ? -14.534 -7.074  31.943  0.40 29.51 ? 215 ASP A CA  1 
ATOM   407  C C   A ASP A 1 215 ? -13.112 -7.423  31.613  0.60 29.19 ? 215 ASP A C   1 
ATOM   408  C C   B ASP A 1 215 ? -13.094 -7.451  31.594  0.40 29.10 ? 215 ASP A C   1 
ATOM   409  O O   A ASP A 1 215 ? -12.896 -7.954  30.522  0.60 28.77 ? 215 ASP A O   1 
ATOM   410  O O   B ASP A 1 215 ? -12.846 -7.992  30.516  0.40 28.88 ? 215 ASP A O   1 
ATOM   411  C CB  A ASP A 1 215 ? -15.325 -8.147  32.563  0.60 31.85 ? 215 ASP A CB  1 
ATOM   412  C CB  B ASP A 1 215 ? -15.311 -8.346  32.319  0.40 30.75 ? 215 ASP A CB  1 
ATOM   413  C CG  A ASP A 1 215 ? -16.625 -7.736  33.233  0.60 37.35 ? 215 ASP A CG  1 
ATOM   414  C CG  B ASP A 1 215 ? -14.729 -9.131  33.473  0.40 34.73 ? 215 ASP A CG  1 
ATOM   415  O OD1 A ASP A 1 215 ? -16.746 -6.552  33.628  0.60 37.68 ? 215 ASP A OD1 1 
ATOM   416  O OD1 B ASP A 1 215 ? -14.862 -8.673  34.625  0.40 35.19 ? 215 ASP A OD1 1 
ATOM   417  O OD2 A ASP A 1 215 ? -17.522 -8.595  33.362  0.60 40.44 ? 215 ASP A OD2 1 
ATOM   418  O OD2 B ASP A 1 215 ? -14.153 -10.215 33.225  0.40 37.02 ? 215 ASP A OD2 1 
ATOM   419  N N   . ILE A 1 216 ? -12.153 -7.158  32.493  1.00 28.70 ? 216 ILE A N   1 
ATOM   420  C CA  . ILE A 1 216 ? -10.756 -7.509  32.270  1.00 28.57 ? 216 ILE A CA  1 
ATOM   421  C C   . ILE A 1 216 ? -10.332 -8.432  33.397  1.00 28.21 ? 216 ILE A C   1 
ATOM   422  O O   . ILE A 1 216 ? -10.660 -8.173  34.558  1.00 28.61 ? 216 ILE A O   1 
ATOM   423  C CB  . ILE A 1 216 ? -9.859  -6.252  32.240  1.00 30.00 ? 216 ILE A CB  1 
ATOM   424  C CG1 . ILE A 1 216 ? -10.223 -5.323  31.066  1.00 31.73 ? 216 ILE A CG1 1 
ATOM   425  C CG2 . ILE A 1 216 ? -8.368  -6.619  32.240  1.00 30.23 ? 216 ILE A CG2 1 
ATOM   426  C CD1 . ILE A 1 216 ? -9.828  -3.890  31.302  1.00 33.87 ? 216 ILE A CD1 1 
ATOM   427  N N   . LEU A 1 217 ? -9.604  -9.499  33.076  1.00 26.41 ? 217 LEU A N   1 
ATOM   428  C CA  . LEU A 1 217 ? -9.120  -10.430 34.085  1.00 26.24 ? 217 LEU A CA  1 
ATOM   429  C C   . LEU A 1 217 ? -7.640  -10.697 33.815  1.00 24.64 ? 217 LEU A C   1 
ATOM   430  O O   . LEU A 1 217 ? -7.281  -10.977 32.673  1.00 25.11 ? 217 LEU A O   1 
ATOM   431  C CB  . LEU A 1 217 ? -9.887  -11.771 33.957  1.00 27.49 ? 217 LEU A CB  1 
ATOM   432  C CG  . LEU A 1 217 ? -9.376  -12.919 34.851  1.00 29.65 ? 217 LEU A CG  1 
ATOM   433  C CD1 . LEU A 1 217 ? -9.886  -12.744 36.281  1.00 30.08 ? 217 LEU A CD1 1 
ATOM   434  C CD2 . LEU A 1 217 ? -9.788  -14.273 34.314  1.00 30.97 ? 217 LEU A CD2 1 
ATOM   435  N N   . GLN A 1 218 ? -6.792  -10.655 34.853  1.00 23.27 ? 218 GLN A N   1 
ATOM   436  C CA  . GLN A 1 218 ? -5.401  -11.064 34.688  1.00 22.90 ? 218 GLN A CA  1 
ATOM   437  C C   . GLN A 1 218 ? -5.457  -12.589 34.900  1.00 23.20 ? 218 GLN A C   1 
ATOM   438  O O   . GLN A 1 218 ? -5.611  -13.037 36.036  1.00 24.90 ? 218 GLN A O   1 
ATOM   439  C CB  . GLN A 1 218 ? -4.500  -10.411 35.747  1.00 23.35 ? 218 GLN A CB  1 
ATOM   440  C CG  . GLN A 1 218 ? -3.011  -10.708 35.472  1.00 26.25 ? 218 GLN A CG  1 
ATOM   441  C CD  . GLN A 1 218 ? -2.085  -10.099 36.489  1.00 31.66 ? 218 GLN A CD  1 
ATOM   442  O OE1 . GLN A 1 218 ? -2.511  -9.553  37.501  1.00 33.81 ? 218 GLN A OE1 1 
ATOM   443  N NE2 . GLN A 1 218 ? -0.779  -10.174 36.247  1.00 31.77 ? 218 GLN A NE2 1 
ATOM   444  N N   . LEU A 1 219 ? -5.440  -13.375 33.823  1.00 22.17 ? 219 LEU A N   1 
ATOM   445  C CA  . LEU A 1 219 ? -5.579  -14.837 33.927  1.00 22.40 ? 219 LEU A CA  1 
ATOM   446  C C   . LEU A 1 219 ? -4.398  -15.499 34.615  1.00 22.72 ? 219 LEU A C   1 
ATOM   447  O O   . LEU A 1 219 ? -4.565  -16.439 35.425  1.00 24.74 ? 219 LEU A O   1 
ATOM   448  C CB  . LEU A 1 219 ? -5.750  -15.441 32.521  1.00 21.87 ? 219 LEU A CB  1 
ATOM   449  C CG  . LEU A 1 219 ? -5.871  -16.960 32.461  1.00 22.78 ? 219 LEU A CG  1 
ATOM   450  C CD1 . LEU A 1 219 ? -7.155  -17.434 33.131  1.00 22.94 ? 219 LEU A CD1 1 
ATOM   451  C CD2 . LEU A 1 219 ? -5.782  -17.458 31.019  1.00 23.62 ? 219 LEU A CD2 1 
ATOM   452  N N   . LEU A 1 220 ? -3.206  -15.052 34.260  1.00 22.30 ? 220 LEU A N   1 
ATOM   453  C CA  . LEU A 1 220 ? -2.011  -15.663 34.787  1.00 22.23 ? 220 LEU A CA  1 
ATOM   454  C C   . LEU A 1 220 ? -0.835  -14.759 34.703  1.00 22.72 ? 220 LEU A C   1 
ATOM   455  O O   . LEU A 1 220 ? -0.824  -13.787 33.938  1.00 22.08 ? 220 LEU A O   1 
ATOM   456  C CB  . LEU A 1 220 ? -1.720  -16.962 33.999  1.00 22.37 ? 220 LEU A CB  1 
ATOM   457  C CG  . LEU A 1 220 ? -1.341  -16.771 32.504  1.00 24.81 ? 220 LEU A CG  1 
ATOM   458  C CD1 . LEU A 1 220 ? 0.169   -16.774 32.312  1.00 26.42 ? 220 LEU A CD1 1 
ATOM   459  C CD2 . LEU A 1 220 ? -1.995  -17.832 31.642  1.00 25.73 ? 220 LEU A CD2 1 
ATOM   460  N N   . GLN A 1 221 ? 0.175   -15.118 35.473  1.00 23.17 ? 221 GLN A N   1 
ATOM   461  C CA  . GLN A 1 221 ? 1.465   -14.474 35.394  1.00 24.67 ? 221 GLN A CA  1 
ATOM   462  C C   . GLN A 1 221 ? 2.523   -15.545 35.547  1.00 25.72 ? 221 GLN A C   1 
ATOM   463  O O   . GLN A 1 221 ? 2.402   -16.429 36.409  1.00 26.10 ? 221 GLN A O   1 
ATOM   464  C CB  . GLN A 1 221 ? 1.608   -13.367 36.442  1.00 27.64 ? 221 GLN A CB  1 
ATOM   465  C CG  . GLN A 1 221 ? 2.928   -12.613 36.308  1.00 33.52 ? 221 GLN A CG  1 
ATOM   466  C CD  . GLN A 1 221 ? 3.047   -11.511 37.332  1.00 41.80 ? 221 GLN A CD  1 
ATOM   467  O OE1 . GLN A 1 221 ? 2.750   -11.687 38.521  1.00 44.20 ? 221 GLN A OE1 1 
ATOM   468  N NE2 . GLN A 1 221 ? 3.518   -10.354 36.902  1.00 43.73 ? 221 GLN A NE2 1 
ATOM   469  N N   . MET A 1 222 ? 3.603   -15.455 34.752  1.00 24.94 ? 222 MET A N   1 
ATOM   470  C CA  . MET A 1 222 ? 4.726   -16.388 34.847  1.00 25.95 ? 222 MET A CA  1 
ATOM   471  C C   . MET A 1 222 ? 5.328   -16.355 36.251  1.00 26.96 ? 222 MET A C   1 
ATOM   472  O O   . MET A 1 222 ? 5.301   -15.304 36.885  1.00 27.02 ? 222 MET A O   1 
ATOM   473  C CB  . MET A 1 222 ? 5.784   -16.026 33.801  1.00 27.17 ? 222 MET A CB  1 
ATOM   474  C CG  . MET A 1 222 ? 5.258   -16.087 32.381  1.00 30.15 ? 222 MET A CG  1 
ATOM   475  S SD  . MET A 1 222 ? 5.146   -17.767 31.723  1.00 37.90 ? 222 MET A SD  1 
ATOM   476  C CE  . MET A 1 222 ? 3.477   -18.229 32.164  1.00 39.09 ? 222 MET A CE  1 
ATOM   477  N N   . GLU A 1 223 ? 5.757   -17.505 36.775  1.00 27.98 ? 223 GLU A N   1 
ATOM   478  C CA  . GLU A 1 223 ? 6.210   -17.584 38.155  1.00 30.66 ? 223 GLU A CA  1 
ATOM   479  C C   . GLU A 1 223 ? 7.682   -17.391 38.380  1.00 32.13 ? 223 GLU A C   1 
ATOM   480  O O   . GLU A 1 223 ? 8.056   -17.342 39.538  1.00 33.97 ? 223 GLU A O   1 
ATOM   481  C CB  . GLU A 1 223 ? 5.789   -18.914 38.819  1.00 34.53 ? 223 GLU A CB  1 
ATOM   482  C CG  . GLU A 1 223 ? 4.304   -19.028 39.117  1.00 42.45 ? 223 GLU A CG  1 
ATOM   483  C CD  . GLU A 1 223 ? 3.948   -18.805 40.574  1.00 52.68 ? 223 GLU A CD  1 
ATOM   484  O OE1 . GLU A 1 223 ? 2.909   -19.343 41.023  1.00 54.95 ? 223 GLU A OE1 1 
ATOM   485  O OE2 . GLU A 1 223 ? 4.710   -18.097 41.270  1.00 55.81 ? 223 GLU A OE2 1 
ATOM   486  N N   . GLN A 1 224 ? 8.509   -17.351 37.342  1.00 31.60 ? 224 GLN A N   1 
ATOM   487  C CA  . GLN A 1 224 ? 9.950   -17.220 37.564  1.00 32.14 ? 224 GLN A CA  1 
ATOM   488  C C   . GLN A 1 224 ? 10.538  -16.006 36.840  1.00 30.19 ? 224 GLN A C   1 
ATOM   489  O O   . GLN A 1 224 ? 10.036  -15.619 35.788  1.00 29.70 ? 224 GLN A O   1 
ATOM   490  C CB  . GLN A 1 224 ? 10.647  -18.536 37.177  1.00 35.15 ? 224 GLN A CB  1 
ATOM   491  C CG  . GLN A 1 224 ? 10.466  -19.652 38.241  1.00 40.23 ? 224 GLN A CG  1 
ATOM   492  C CD  . GLN A 1 224 ? 11.130  -20.971 37.861  1.00 46.21 ? 224 GLN A CD  1 
ATOM   493  O OE1 . GLN A 1 224 ? 11.585  -21.752 38.719  1.00 47.73 ? 224 GLN A OE1 1 
ATOM   494  N NE2 . GLN A 1 224 ? 11.185  -21.262 36.573  1.00 46.86 ? 224 GLN A NE2 1 
ATOM   495  N N   . PRO A 1 225 ? 11.575  -15.362 37.416  1.00 28.58 ? 225 PRO A N   1 
ATOM   496  C CA  . PRO A 1 225 ? 12.175  -14.198 36.743  1.00 28.03 ? 225 PRO A CA  1 
ATOM   497  C C   . PRO A 1 225 ? 12.679  -14.536 35.344  1.00 28.74 ? 225 PRO A C   1 
ATOM   498  O O   . PRO A 1 225 ? 13.180  -15.643 35.121  1.00 30.44 ? 225 PRO A O   1 
ATOM   499  C CB  . PRO A 1 225 ? 13.359  -13.835 37.654  1.00 28.61 ? 225 PRO A CB  1 
ATOM   500  C CG  . PRO A 1 225 ? 12.961  -14.368 39.008  1.00 29.13 ? 225 PRO A CG  1 
ATOM   501  C CD  . PRO A 1 225 ? 12.246  -15.658 38.693  1.00 27.74 ? 225 PRO A CD  1 
ATOM   502  N N   . GLY A 1 226 ? 12.575  -13.580 34.430  1.00 27.29 ? 226 GLY A N   1 
ATOM   503  C CA  . GLY A 1 226 ? 13.042  -13.747 33.057  1.00 28.83 ? 226 GLY A CA  1 
ATOM   504  C C   . GLY A 1 226 ? 12.031  -14.380 32.119  1.00 30.22 ? 226 GLY A C   1 
ATOM   505  O O   . GLY A 1 226 ? 12.170  -14.285 30.896  1.00 32.69 ? 226 GLY A O   1 
ATOM   506  N N   . GLU A 1 227 ? 11.022  -15.062 32.667  1.00 29.02 ? 227 GLU A N   1 
ATOM   507  C CA  . GLU A 1 227 ? 10.028  -15.749 31.847  1.00 28.09 ? 227 GLU A CA  1 
ATOM   508  C C   . GLU A 1 227 ? 9.025   -14.785 31.226  1.00 26.58 ? 227 GLU A C   1 
ATOM   509  O O   . GLU A 1 227 ? 8.582   -13.848 31.884  1.00 26.43 ? 227 GLU A O   1 
ATOM   510  C CB  . GLU A 1 227 ? 9.274   -16.813 32.654  1.00 31.38 ? 227 GLU A CB  1 
ATOM   511  C CG  . GLU A 1 227 ? 10.072  -18.060 32.980  1.00 39.39 ? 227 GLU A CG  1 
ATOM   512  C CD  . GLU A 1 227 ? 9.284   -19.078 33.790  1.00 48.06 ? 227 GLU A CD  1 
ATOM   513  O OE1 . GLU A 1 227 ? 8.439   -18.665 34.620  1.00 46.36 ? 227 GLU A OE1 1 
ATOM   514  O OE2 . GLU A 1 227 ? 9.517   -20.293 33.594  1.00 52.33 ? 227 GLU A OE2 1 
ATOM   515  N N   . TYR A 1 228 ? 8.694   -14.995 29.952  1.00 24.18 ? 228 TYR A N   1 
ATOM   516  C CA  . TYR A 1 228 ? 7.680   -14.185 29.284  1.00 23.31 ? 228 TYR A CA  1 
ATOM   517  C C   . TYR A 1 228 ? 6.760   -15.063 28.418  1.00 21.15 ? 228 TYR A C   1 
ATOM   518  O O   . TYR A 1 228 ? 7.111   -16.209 28.092  1.00 20.90 ? 228 TYR A O   1 
ATOM   519  C CB  . TYR A 1 228 ? 8.284   -13.021 28.462  1.00 23.61 ? 228 TYR A CB  1 
ATOM   520  C CG  . TYR A 1 228 ? 9.216   -13.470 27.348  1.00 24.45 ? 228 TYR A CG  1 
ATOM   521  C CD1 . TYR A 1 228 ? 8.727   -13.767 26.082  1.00 24.97 ? 228 TYR A CD1 1 
ATOM   522  C CD2 . TYR A 1 228 ? 10.584  -13.535 27.547  1.00 25.75 ? 228 TYR A CD2 1 
ATOM   523  C CE1 . TYR A 1 228 ? 9.572   -14.187 25.060  1.00 25.29 ? 228 TYR A CE1 1 
ATOM   524  C CE2 . TYR A 1 228 ? 11.442  -13.945 26.532  1.00 26.22 ? 228 TYR A CE2 1 
ATOM   525  C CZ  . TYR A 1 228 ? 10.935  -14.265 25.288  1.00 26.31 ? 228 TYR A CZ  1 
ATOM   526  O OH  . TYR A 1 228 ? 11.784  -14.673 24.277  1.00 27.72 ? 228 TYR A OH  1 
ATOM   527  N N   . ILE A 1 229 ? 5.559   -14.541 28.086  1.00 19.86 ? 229 ILE A N   1 
ATOM   528  C CA  . ILE A 1 229 ? 4.633   -15.266 27.243  1.00 19.16 ? 229 ILE A CA  1 
ATOM   529  C C   . ILE A 1 229 ? 5.022   -15.044 25.784  1.00 19.18 ? 229 ILE A C   1 
ATOM   530  O O   . ILE A 1 229 ? 5.261   -13.901 25.361  1.00 19.17 ? 229 ILE A O   1 
ATOM   531  C CB  . ILE A 1 229 ? 3.182   -14.791 27.469  1.00 19.88 ? 229 ILE A CB  1 
ATOM   532  C CG1 . ILE A 1 229 ? 2.805   -14.762 28.970  1.00 20.99 ? 229 ILE A CG1 1 
ATOM   533  C CG2 . ILE A 1 229 ? 2.204   -15.623 26.614  1.00 19.98 ? 229 ILE A CG2 1 
ATOM   534  C CD1 . ILE A 1 229 ? 2.776   -16.049 29.598  1.00 22.74 ? 229 ILE A CD1 1 
ATOM   535  N N   . SER A 1 230 ? 5.113   -16.138 25.018  1.00 18.31 ? 230 SER A N   1 
ATOM   536  C CA  . SER A 1 230 ? 5.520   -16.050 23.621  1.00 18.18 ? 230 SER A CA  1 
ATOM   537  C C   . SER A 1 230 ? 4.392   -16.347 22.615  1.00 17.29 ? 230 SER A C   1 
ATOM   538  O O   . SER A 1 230 ? 4.513   -15.951 21.446  1.00 17.97 ? 230 SER A O   1 
ATOM   539  C CB  . SER A 1 230 ? 6.755   -16.918 23.351  1.00 18.53 ? 230 SER A CB  1 
ATOM   540  O OG  . SER A 1 230 ? 6.686   -18.176 24.005  1.00 21.63 ? 230 SER A OG  1 
ATOM   541  N N   . SER A 1 231 ? 3.275   -16.965 23.059  1.00 16.74 ? 231 SER A N   1 
ATOM   542  C CA  . SER A 1 231 ? 2.150   -17.183 22.165  1.00 16.25 ? 231 SER A CA  1 
ATOM   543  C C   . SER A 1 231 ? 0.874   -17.464 22.927  1.00 16.13 ? 231 SER A C   1 
ATOM   544  O O   . SER A 1 231 ? 0.920   -18.006 24.039  1.00 16.62 ? 231 SER A O   1 
ATOM   545  C CB  . SER A 1 231 ? 2.417   -18.334 21.192  1.00 18.40 ? 231 SER A CB  1 
ATOM   546  O OG  . SER A 1 231 ? 2.907   -19.475 21.885  1.00 19.77 ? 231 SER A OG  1 
ATOM   547  N N   . VAL A 1 232 ? -0.273  -17.166 22.309  1.00 16.13 ? 232 VAL A N   1 
ATOM   548  C CA  . VAL A 1 232 ? -1.558  -17.546 22.856  1.00 16.37 ? 232 VAL A CA  1 
ATOM   549  C C   . VAL A 1 232 ? -2.474  -18.044 21.726  1.00 16.13 ? 232 VAL A C   1 
ATOM   550  O O   . VAL A 1 232 ? -2.406  -17.539 20.598  1.00 16.55 ? 232 VAL A O   1 
ATOM   551  C CB  . VAL A 1 232 ? -2.283  -16.431 23.675  1.00 17.88 ? 232 VAL A CB  1 
ATOM   552  C CG1 . VAL A 1 232 ? -1.478  -16.031 24.922  1.00 18.55 ? 232 VAL A CG1 1 
ATOM   553  C CG2 . VAL A 1 232 ? -2.575  -15.215 22.811  1.00 18.81 ? 232 VAL A CG2 1 
ATOM   554  N N   . ALA A 1 233 ? -3.322  -19.039 22.019  1.00 15.12 ? 233 ALA A N   1 
ATOM   555  C CA  . ALA A 1 233 ? -4.301  -19.496 21.040  1.00 15.76 ? 233 ALA A CA  1 
ATOM   556  C C   . ALA A 1 233 ? -5.471  -20.169 21.714  1.00 17.12 ? 233 ALA A C   1 
ATOM   557  O O   . ALA A 1 233 ? -5.267  -21.096 22.500  1.00 17.28 ? 233 ALA A O   1 
ATOM   558  C CB  . ALA A 1 233 ? -3.677  -20.459 20.029  1.00 15.37 ? 233 ALA A CB  1 
ATOM   559  N N   . TRP A 1 234 ? -6.690  -19.751 21.369  1.00 17.29 ? 234 TRP A N   1 
ATOM   560  C CA  . TRP A 1 234 ? -7.881  -20.351 21.909  1.00 17.10 ? 234 TRP A CA  1 
ATOM   561  C C   . TRP A 1 234 ? -8.250  -21.632 21.181  1.00 17.93 ? 234 TRP A C   1 
ATOM   562  O O   . TRP A 1 234 ? -8.230  -21.670 19.928  1.00 17.95 ? 234 TRP A O   1 
ATOM   563  C CB  . TRP A 1 234 ? -9.075  -19.393 21.736  1.00 16.37 ? 234 TRP A CB  1 
ATOM   564  C CG  . TRP A 1 234 ? -9.005  -18.151 22.565  1.00 16.35 ? 234 TRP A CG  1 
ATOM   565  C CD1 . TRP A 1 234 ? -8.680  -16.900 22.143  1.00 17.00 ? 234 TRP A CD1 1 
ATOM   566  C CD2 . TRP A 1 234 ? -9.356  -18.035 23.943  1.00 16.54 ? 234 TRP A CD2 1 
ATOM   567  N NE1 . TRP A 1 234 ? -8.829  -16.000 23.177  1.00 17.11 ? 234 TRP A NE1 1 
ATOM   568  C CE2 . TRP A 1 234 ? -9.273  -16.668 24.285  1.00 17.29 ? 234 TRP A CE2 1 
ATOM   569  C CE3 . TRP A 1 234 ? -9.864  -18.931 24.883  1.00 17.19 ? 234 TRP A CE3 1 
ATOM   570  C CZ2 . TRP A 1 234 ? -9.578  -16.196 25.559  1.00 18.68 ? 234 TRP A CZ2 1 
ATOM   571  C CZ3 . TRP A 1 234 ? -10.157 -18.465 26.158  1.00 18.69 ? 234 TRP A CZ3 1 
ATOM   572  C CH2 . TRP A 1 234 ? -10.024 -17.112 26.480  1.00 19.27 ? 234 TRP A CH2 1 
ATOM   573  N N   . ILE A 1 235 ? -8.753  -22.621 21.936  1.00 19.08 ? 235 ILE A N   1 
ATOM   574  C CA  . ILE A 1 235 ? -9.325  -23.819 21.329  1.00 20.49 ? 235 ILE A CA  1 
ATOM   575  C C   . ILE A 1 235 ? -10.641 -23.367 20.617  1.00 22.35 ? 235 ILE A C   1 
ATOM   576  O O   . ILE A 1 235 ? -11.176 -22.294 20.933  1.00 21.59 ? 235 ILE A O   1 
ATOM   577  C CB  . ILE A 1 235 ? -9.614  -24.897 22.418  1.00 20.36 ? 235 ILE A CB  1 
ATOM   578  C CG1 . ILE A 1 235 ? -9.762  -26.298 21.798  1.00 21.63 ? 235 ILE A CG1 1 
ATOM   579  C CG2 . ILE A 1 235 ? -10.861 -24.530 23.257  1.00 20.61 ? 235 ILE A CG2 1 
ATOM   580  C CD1 . ILE A 1 235 ? -9.779  -27.434 22.821  1.00 22.28 ? 235 ILE A CD1 1 
ATOM   581  N N   . LYS A 1 236 ? -11.102 -24.123 19.608  1.00 24.09 ? 236 LYS A N   1 
ATOM   582  C CA  . LYS A 1 236 ? -12.291 -23.744 18.835  1.00 26.23 ? 236 LYS A CA  1 
ATOM   583  C C   . LYS A 1 236 ? -13.519 -23.419 19.676  1.00 27.57 ? 236 LYS A C   1 
ATOM   584  O O   . LYS A 1 236 ? -14.168 -22.419 19.388  1.00 29.18 ? 236 LYS A O   1 
ATOM   585  C CB  . LYS A 1 236 ? -12.653 -24.798 17.770  1.00 29.16 ? 236 LYS A CB  1 
ATOM   586  N N   . GLU A 1 237 ? -13.797 -24.182 20.742  1.00 27.79 ? 237 GLU A N   1 
ATOM   587  C CA  . GLU A 1 237 ? -14.944 -23.911 21.634  1.00 29.15 ? 237 GLU A CA  1 
ATOM   588  C C   . GLU A 1 237 ? -14.776 -22.658 22.530  1.00 28.94 ? 237 GLU A C   1 
ATOM   589  O O   . GLU A 1 237 ? -15.737 -22.200 23.152  1.00 30.00 ? 237 GLU A O   1 
ATOM   590  C CB  . GLU A 1 237 ? -15.237 -25.119 22.543  1.00 33.25 ? 237 GLU A CB  1 
ATOM   591  N N   . GLY A 1 238 ? -13.554 -22.147 22.628  1.00 27.42 ? 238 GLY A N   1 
ATOM   592  C CA  . GLY A 1 238 ? -13.279 -20.965 23.420  1.00 27.49 ? 238 GLY A CA  1 
ATOM   593  C C   . GLY A 1 238 ? -13.181 -21.177 24.922  1.00 27.48 ? 238 GLY A C   1 
ATOM   594  O O   . GLY A 1 238 ? -13.033 -20.191 25.638  1.00 28.62 ? 238 GLY A O   1 
ATOM   595  N N   . ASN A 1 239 ? -13.194 -22.440 25.430  1.00 26.36 ? 239 ASN A N   1 
ATOM   596  C CA  . ASN A 1 239 ? -13.088 -22.648 26.902  1.00 26.50 ? 239 ASN A CA  1 
ATOM   597  C C   . ASN A 1 239 ? -11.659 -22.862 27.443  1.00 24.56 ? 239 ASN A C   1 
ATOM   598  O O   . ASN A 1 239 ? -11.397 -22.720 28.653  1.00 24.88 ? 239 ASN A O   1 
ATOM   599  C CB  . ASN A 1 239 ? -13.980 -23.771 27.361  1.00 30.36 ? 239 ASN A CB  1 
ATOM   600  C CG  . ASN A 1 239 ? -13.848 -25.082 26.633  1.00 36.44 ? 239 ASN A CG  1 
ATOM   601  O OD1 . ASN A 1 239 ? -13.416 -25.174 25.463  1.00 37.48 ? 239 ASN A OD1 1 
ATOM   602  N ND2 . ASN A 1 239 ? -14.288 -26.137 27.307  1.00 37.95 ? 239 ASN A ND2 1 
ATOM   603  N N   . TYR A 1 240 ? -10.762 -23.236 26.568  1.00 22.35 ? 240 TYR A N   1 
ATOM   604  C CA  . TYR A 1 240 ? -9.368  -23.482 26.921  1.00 21.91 ? 240 TYR A CA  1 
ATOM   605  C C   . TYR A 1 240 ? -8.484  -22.543 26.141  1.00 20.50 ? 240 TYR A C   1 
ATOM   606  O O   . TYR A 1 240 ? -8.700  -22.367 24.929  1.00 19.90 ? 240 TYR A O   1 
ATOM   607  C CB  . TYR A 1 240 ? -8.984  -24.922 26.546  1.00 23.19 ? 240 TYR A CB  1 
ATOM   608  C CG  . TYR A 1 240 ? -9.835  -25.948 27.262  1.00 27.60 ? 240 TYR A CG  1 
ATOM   609  C CD1 . TYR A 1 240 ? -9.948  -25.943 28.641  1.00 29.36 ? 240 TYR A CD1 1 
ATOM   610  C CD2 . TYR A 1 240 ? -10.627 -26.840 26.552  1.00 31.25 ? 240 TYR A CD2 1 
ATOM   611  C CE1 . TYR A 1 240 ? -10.747 -26.860 29.303  1.00 32.13 ? 240 TYR A CE1 1 
ATOM   612  C CE2 . TYR A 1 240 ? -11.446 -27.752 27.203  1.00 33.26 ? 240 TYR A CE2 1 
ATOM   613  C CZ  . TYR A 1 240 ? -11.493 -27.767 28.583  1.00 34.54 ? 240 TYR A CZ  1 
ATOM   614  O OH  . TYR A 1 240 ? -12.311 -28.649 29.243  1.00 37.92 ? 240 TYR A OH  1 
ATOM   615  N N   . LEU A 1 241 ? -7.424  -22.028 26.788  1.00 18.54 ? 241 LEU A N   1 
ATOM   616  C CA  . LEU A 1 241 ? -6.452  -21.156 26.136  1.00 18.02 ? 241 LEU A CA  1 
ATOM   617  C C   . LEU A 1 241 ? -5.086  -21.816 26.199  1.00 18.31 ? 241 LEU A C   1 
ATOM   618  O O   . LEU A 1 241 ? -4.686  -22.259 27.273  1.00 18.81 ? 241 LEU A O   1 
ATOM   619  C CB  . LEU A 1 241 ? -6.360  -19.793 26.843  1.00 17.99 ? 241 LEU A CB  1 
ATOM   620  C CG  . LEU A 1 241 ? -5.395  -18.794 26.211  1.00 18.41 ? 241 LEU A CG  1 
ATOM   621  C CD1 . LEU A 1 241 ? -5.892  -18.340 24.847  1.00 18.74 ? 241 LEU A CD1 1 
ATOM   622  C CD2 . LEU A 1 241 ? -5.165  -17.568 27.121  1.00 19.95 ? 241 LEU A CD2 1 
ATOM   623  N N   . ALA A 1 242 ? -4.421  -21.979 25.050  1.00 17.98 ? 242 ALA A N   1 
ATOM   624  C CA  . ALA A 1 242 ? -3.061  -22.516 25.056  1.00 17.52 ? 242 ALA A CA  1 
ATOM   625  C C   . ALA A 1 242 ? -2.141  -21.305 25.222  1.00 18.37 ? 242 ALA A C   1 
ATOM   626  O O   . ALA A 1 242 ? -2.376  -20.256 24.598  1.00 18.03 ? 242 ALA A O   1 
ATOM   627  C CB  . ALA A 1 242 ? -2.765  -23.224 23.732  1.00 18.15 ? 242 ALA A CB  1 
ATOM   628  N N   . VAL A 1 243 ? -1.055  -21.447 26.028  1.00 18.70 ? 243 VAL A N   1 
ATOM   629  C CA  . VAL A 1 243 ? -0.132  -20.342 26.263  1.00 18.12 ? 243 VAL A CA  1 
ATOM   630  C C   . VAL A 1 243 ? 1.283   -20.897 26.100  1.00 18.72 ? 243 VAL A C   1 
ATOM   631  O O   . VAL A 1 243 ? 1.672   -21.761 26.872  1.00 19.81 ? 243 VAL A O   1 
ATOM   632  C CB  . VAL A 1 243 ? -0.339  -19.789 27.709  1.00 19.32 ? 243 VAL A CB  1 
ATOM   633  C CG1 . VAL A 1 243 ? 0.642   -18.674 28.012  1.00 19.63 ? 243 VAL A CG1 1 
ATOM   634  C CG2 . VAL A 1 243 ? -1.785  -19.280 27.901  1.00 19.24 ? 243 VAL A CG2 1 
ATOM   635  N N   . GLY A 1 244 ? 2.008   -20.432 25.089  1.00 17.79 ? 244 GLY A N   1 
ATOM   636  C CA  . GLY A 1 244 ? 3.398   -20.834 24.869  1.00 18.94 ? 244 GLY A CA  1 
ATOM   637  C C   . GLY A 1 244 ? 4.287   -19.892 25.644  1.00 19.99 ? 244 GLY A C   1 
ATOM   638  O O   . GLY A 1 244 ? 3.993   -18.684 25.728  1.00 19.40 ? 244 GLY A O   1 
ATOM   639  N N   . THR A 1 245 ? 5.413   -20.423 26.197  1.00 20.48 ? 245 THR A N   1 
ATOM   640  C CA  . THR A 1 245 ? 6.267   -19.593 27.022  1.00 22.34 ? 245 THR A CA  1 
ATOM   641  C C   . THR A 1 245 ? 7.720   -19.601 26.562  1.00 22.94 ? 245 THR A C   1 
ATOM   642  O O   . THR A 1 245 ? 8.164   -20.499 25.840  1.00 22.60 ? 245 THR A O   1 
ATOM   643  C CB  . THR A 1 245 ? 6.183   -20.030 28.527  1.00 24.35 ? 245 THR A CB  1 
ATOM   644  O OG1 . THR A 1 245 ? 7.035   -21.157 28.737  1.00 24.73 ? 245 THR A OG1 1 
ATOM   645  C CG2 . THR A 1 245 ? 4.751   -20.352 28.994  1.00 24.92 ? 245 THR A CG2 1 
ATOM   646  N N   . SER A 1 246 ? 8.457   -18.567 26.989  1.00 24.13 ? 246 SER A N   1 
ATOM   647  C CA  . SER A 1 246 ? 9.889   -18.423 26.741  1.00 25.01 ? 246 SER A CA  1 
ATOM   648  C C   . SER A 1 246 ? 10.686  -19.580 27.327  1.00 27.02 ? 246 SER A C   1 
ATOM   649  O O   . SER A 1 246 ? 11.805  -19.838 26.865  1.00 28.12 ? 246 SER A O   1 
ATOM   650  C CB  . SER A 1 246 ? 10.365  -17.123 27.364  1.00 25.29 ? 246 SER A CB  1 
ATOM   651  O OG  . SER A 1 246 ? 10.266  -17.179 28.777  1.00 25.34 ? 246 SER A OG  1 
ATOM   652  N N   . SER A 1 247 ? 10.162  -20.237 28.380  1.00 27.10 ? 247 SER A N   1 
ATOM   653  C CA  . SER A 1 247 ? 10.806  -21.386 29.008  1.00 27.35 ? 247 SER A CA  1 
ATOM   654  C C   . SER A 1 247 ? 10.414  -22.702 28.311  1.00 27.28 ? 247 SER A C   1 
ATOM   655  O O   . SER A 1 247 ? 10.572  -23.764 28.903  1.00 28.10 ? 247 SER A O   1 
ATOM   656  C CB  . SER A 1 247 ? 10.445  -21.446 30.494  1.00 29.45 ? 247 SER A CB  1 
ATOM   657  O OG  . SER A 1 247 ? 9.030   -21.449 30.597  1.00 32.67 ? 247 SER A OG  1 
ATOM   658  N N   . ALA A 1 248 ? 9.896   -22.645 27.042  1.00 25.70 ? 248 ALA A N   1 
ATOM   659  C CA  . ALA A 1 248 ? 9.580   -23.817 26.220  1.00 25.11 ? 248 ALA A CA  1 
ATOM   660  C C   . ALA A 1 248 ? 8.427   -24.655 26.712  1.00 25.35 ? 248 ALA A C   1 
ATOM   661  O O   . ALA A 1 248 ? 8.391   -25.868 26.454  1.00 26.11 ? 248 ALA A O   1 
ATOM   662  C CB  . ALA A 1 248 ? 10.831  -24.697 26.037  1.00 24.41 ? 248 ALA A CB  1 
ATOM   663  N N   . GLU A 1 249 ? 7.472   -24.024 27.410  1.00 24.35 ? 249 GLU A N   1 
ATOM   664  C CA  . GLU A 1 249 ? 6.314   -24.761 27.889  1.00 24.28 ? 249 GLU A CA  1 
ATOM   665  C C   . GLU A 1 249 ? 5.114   -24.411 27.039  1.00 22.91 ? 249 GLU A C   1 
ATOM   666  O O   . GLU A 1 249 ? 5.027   -23.318 26.485  1.00 22.55 ? 249 GLU A O   1 
ATOM   667  C CB  . GLU A 1 249 ? 5.972   -24.363 29.338  1.00 27.26 ? 249 GLU A CB  1 
ATOM   668  C CG  . GLU A 1 249 ? 7.135   -24.430 30.300  1.00 32.74 ? 249 GLU A CG  1 
ATOM   669  C CD  . GLU A 1 249 ? 6.836   -23.704 31.595  1.00 41.23 ? 249 GLU A CD  1 
ATOM   670  O OE1 . GLU A 1 249 ? 7.152   -24.256 32.674  1.00 42.57 ? 249 GLU A OE1 1 
ATOM   671  O OE2 . GLU A 1 249 ? 6.288   -22.578 31.529  1.00 43.35 ? 249 GLU A OE2 1 
ATOM   672  N N   . VAL A 1 250 ? 4.189   -25.339 26.944  1.00 23.02 ? 250 VAL A N   1 
ATOM   673  C CA  . VAL A 1 250 ? 2.896   -25.087 26.325  1.00 23.54 ? 250 VAL A CA  1 
ATOM   674  C C   . VAL A 1 250 ? 1.891   -25.367 27.455  1.00 23.75 ? 250 VAL A C   1 
ATOM   675  O O   . VAL A 1 250 ? 1.637   -26.525 27.789  1.00 24.07 ? 250 VAL A O   1 
ATOM   676  C CB  . VAL A 1 250 ? 2.649   -25.974 25.087  1.00 26.10 ? 250 VAL A CB  1 
ATOM   677  C CG1 . VAL A 1 250 ? 1.307   -25.632 24.444  1.00 27.44 ? 250 VAL A CG1 1 
ATOM   678  C CG2 . VAL A 1 250 ? 3.780   -25.812 24.073  1.00 26.85 ? 250 VAL A CG2 1 
ATOM   679  N N   . GLN A 1 251 ? 1.365   -24.308 28.077  1.00 23.17 ? 251 GLN A N   1 
ATOM   680  C CA  . GLN A 1 251 ? 0.406   -24.433 29.169  1.00 23.34 ? 251 GLN A CA  1 
ATOM   681  C C   . GLN A 1 251 ? -1.009  -24.460 28.621  1.00 23.65 ? 251 GLN A C   1 
ATOM   682  O O   . GLN A 1 251 ? -1.289  -23.839 27.594  1.00 24.57 ? 251 GLN A O   1 
ATOM   683  C CB  . GLN A 1 251 ? 0.556   -23.264 30.156  1.00 25.33 ? 251 GLN A CB  1 
ATOM   684  C CG  . GLN A 1 251 ? 1.999   -23.020 30.586  1.00 29.27 ? 251 GLN A CG  1 
ATOM   685  C CD  . GLN A 1 251 ? 2.127   -22.079 31.756  1.00 33.61 ? 251 GLN A CD  1 
ATOM   686  O OE1 . GLN A 1 251 ? 1.170   -21.402 32.179  1.00 33.74 ? 251 GLN A OE1 1 
ATOM   687  N NE2 . GLN A 1 251 ? 3.333   -22.017 32.312  1.00 34.38 ? 251 GLN A NE2 1 
ATOM   688  N N   . LEU A 1 252 ? -1.883  -25.218 29.259  1.00 22.52 ? 252 LEU A N   1 
ATOM   689  C CA  . LEU A 1 252 ? -3.265  -25.294 28.839  1.00 22.40 ? 252 LEU A CA  1 
ATOM   690  C C   . LEU A 1 252 ? -4.090  -24.763 30.003  1.00 21.09 ? 252 LEU A C   1 
ATOM   691  O O   . LEU A 1 252 ? -4.067  -25.327 31.099  1.00 21.06 ? 252 LEU A O   1 
ATOM   692  C CB  . LEU A 1 252 ? -3.675  -26.715 28.467  1.00 23.84 ? 252 LEU A CB  1 
ATOM   693  C CG  . LEU A 1 252 ? -5.074  -26.817 27.898  1.00 26.30 ? 252 LEU A CG  1 
ATOM   694  C CD1 . LEU A 1 252 ? -5.216  -26.008 26.589  1.00 26.41 ? 252 LEU A CD1 1 
ATOM   695  C CD2 . LEU A 1 252 ? -5.499  -28.270 27.750  1.00 28.63 ? 252 LEU A CD2 1 
ATOM   696  N N   . TRP A 1 253 ? -4.772  -23.649 29.785  1.00 20.24 ? 253 TRP A N   1 
ATOM   697  C CA  . TRP A 1 253 ? -5.568  -23.012 30.832  1.00 20.58 ? 253 TRP A CA  1 
ATOM   698  C C   . TRP A 1 253 ? -7.066  -23.180 30.599  1.00 21.15 ? 253 TRP A C   1 
ATOM   699  O O   . TRP A 1 253 ? -7.535  -23.003 29.475  1.00 21.75 ? 253 TRP A O   1 
ATOM   700  C CB  . TRP A 1 253 ? -5.212  -21.498 30.910  1.00 21.09 ? 253 TRP A CB  1 
ATOM   701  C CG  . TRP A 1 253 ? -3.895  -21.247 31.592  1.00 21.83 ? 253 TRP A CG  1 
ATOM   702  C CD1 . TRP A 1 253 ? -2.640  -21.466 31.093  1.00 23.34 ? 253 TRP A CD1 1 
ATOM   703  C CD2 . TRP A 1 253 ? -3.722  -20.868 32.963  1.00 22.56 ? 253 TRP A CD2 1 
ATOM   704  N NE1 . TRP A 1 253 ? -1.699  -21.249 32.075  1.00 23.64 ? 253 TRP A NE1 1 
ATOM   705  C CE2 . TRP A 1 253 ? -2.335  -20.828 33.216  1.00 23.42 ? 253 TRP A CE2 1 
ATOM   706  C CE3 . TRP A 1 253 ? -4.604  -20.493 33.976  1.00 23.44 ? 253 TRP A CE3 1 
ATOM   707  C CZ2 . TRP A 1 253 ? -1.816  -20.464 34.457  1.00 24.36 ? 253 TRP A CZ2 1 
ATOM   708  C CZ3 . TRP A 1 253 ? -4.083  -20.164 35.221  1.00 24.13 ? 253 TRP A CZ3 1 
ATOM   709  C CH2 . TRP A 1 253 ? -2.703  -20.123 35.436  1.00 24.08 ? 253 TRP A CH2 1 
ATOM   710  N N   . ASP A 1 254 ? -7.812  -23.497 31.645  1.00 20.26 ? 254 ASP A N   1 
ATOM   711  C CA  . ASP A 1 254 ? -9.262  -23.583 31.560  1.00 20.45 ? 254 ASP A CA  1 
ATOM   712  C C   . ASP A 1 254 ? -9.717  -22.215 32.044  1.00 21.12 ? 254 ASP A C   1 
ATOM   713  O O   . ASP A 1 254 ? -9.519  -21.897 33.209  1.00 20.72 ? 254 ASP A O   1 
ATOM   714  C CB  . ASP A 1 254 ? -9.776  -24.697 32.471  1.00 22.16 ? 254 ASP A CB  1 
ATOM   715  C CG  . ASP A 1 254 ? -11.286 -24.808 32.519  1.00 26.69 ? 254 ASP A CG  1 
ATOM   716  O OD1 . ASP A 1 254 ? -11.962 -23.758 32.452  1.00 26.35 ? 254 ASP A OD1 1 
ATOM   717  O OD2 . ASP A 1 254 ? -11.790 -25.934 32.717  1.00 30.87 ? 254 ASP A OD2 1 
ATOM   718  N N   . VAL A 1 255 ? -10.264 -21.377 31.149  1.00 21.06 ? 255 VAL A N   1 
ATOM   719  C CA  . VAL A 1 255 ? -10.610 -20.005 31.542  1.00 22.00 ? 255 VAL A CA  1 
ATOM   720  C C   . VAL A 1 255 ? -11.912 -19.896 32.322  1.00 22.73 ? 255 VAL A C   1 
ATOM   721  O O   . VAL A 1 255 ? -12.109 -18.887 32.999  1.00 24.08 ? 255 VAL A O   1 
ATOM   722  C CB  . VAL A 1 255 ? -10.580 -19.017 30.367  1.00 22.17 ? 255 VAL A CB  1 
ATOM   723  C CG1 . VAL A 1 255 ? -9.236  -19.091 29.658  1.00 22.02 ? 255 VAL A CG1 1 
ATOM   724  C CG2 . VAL A 1 255 ? -11.707 -19.298 29.395  1.00 22.84 ? 255 VAL A CG2 1 
ATOM   725  N N   . GLN A 1 256 ? -12.767 -20.929 32.296  1.00 22.05 ? 256 GLN A N   1 
ATOM   726  C CA  . GLN A 1 256 ? -13.989 -20.915 33.110  1.00 23.01 ? 256 GLN A CA  1 
ATOM   727  C C   . GLN A 1 256 ? -13.578 -21.160 34.572  1.00 23.17 ? 256 GLN A C   1 
ATOM   728  O O   . GLN A 1 256 ? -14.083 -20.491 35.483  1.00 24.26 ? 256 GLN A O   1 
ATOM   729  C CB  . GLN A 1 256 ? -14.971 -21.984 32.616  1.00 26.16 ? 256 GLN A CB  1 
ATOM   730  N N   . GLN A 1 257 ? -12.663 -22.125 34.805  1.00 22.62 ? 257 GLN A N   1 
ATOM   731  C CA  . GLN A 1 257 ? -12.152 -22.404 36.145  1.00 22.97 ? 257 GLN A CA  1 
ATOM   732  C C   . GLN A 1 257 ? -10.982 -21.480 36.533  1.00 21.98 ? 257 GLN A C   1 
ATOM   733  O O   . GLN A 1 257 ? -10.615 -21.453 37.703  1.00 22.85 ? 257 GLN A O   1 
ATOM   734  C CB  . GLN A 1 257 ? -11.643 -23.849 36.246  1.00 24.47 ? 257 GLN A CB  1 
ATOM   735  C CG  . GLN A 1 257 ? -12.704 -24.906 35.994  1.00 28.77 ? 257 GLN A CG  1 
ATOM   736  C CD  . GLN A 1 257 ? -12.137 -26.243 36.392  1.00 33.65 ? 257 GLN A CD  1 
ATOM   737  O OE1 . GLN A 1 257 ? -12.311 -26.697 37.510  1.00 36.26 ? 257 GLN A OE1 1 
ATOM   738  N NE2 . GLN A 1 257 ? -11.384 -26.863 35.506  1.00 32.56 ? 257 GLN A NE2 1 
ATOM   739  N N   . GLN A 1 258 ? -10.385 -20.758 35.590  1.00 21.36 ? 258 GLN A N   1 
ATOM   740  C CA  . GLN A 1 258 ? -9.224  -19.900 35.820  1.00 22.33 ? 258 GLN A CA  1 
ATOM   741  C C   . GLN A 1 258 ? -8.094  -20.686 36.458  1.00 23.26 ? 258 GLN A C   1 
ATOM   742  O O   . GLN A 1 258 ? -7.602  -20.348 37.543  1.00 24.28 ? 258 GLN A O   1 
ATOM   743  C CB  . GLN A 1 258 ? -9.620  -18.647 36.621  1.00 24.23 ? 258 GLN A CB  1 
ATOM   744  C CG  . GLN A 1 258 ? -10.744 -17.861 35.928  1.00 26.00 ? 258 GLN A CG  1 
ATOM   745  C CD  . GLN A 1 258 ? -11.111 -16.598 36.663  1.00 30.16 ? 258 GLN A CD  1 
ATOM   746  O OE1 . GLN A 1 258 ? -10.351 -16.087 37.502  1.00 31.24 ? 258 GLN A OE1 1 
ATOM   747  N NE2 . GLN A 1 258 ? -12.277 -16.055 36.344  1.00 28.93 ? 258 GLN A NE2 1 
ATOM   748  N N   . LYS A 1 259 ? -7.768  -21.816 35.838  1.00 23.11 ? 259 LYS A N   1 
ATOM   749  C CA  . LYS A 1 259 ? -6.735  -22.691 36.362  1.00 23.83 ? 259 LYS A CA  1 
ATOM   750  C C   . LYS A 1 259 ? -5.964  -23.372 35.282  1.00 24.01 ? 259 LYS A C   1 
ATOM   751  O O   . LYS A 1 259 ? -6.477  -23.605 34.195  1.00 22.89 ? 259 LYS A O   1 
ATOM   752  C CB  . LYS A 1 259 ? -7.309  -23.722 37.348  1.00 26.69 ? 259 LYS A CB  1 
ATOM   753  C CG  . LYS A 1 259 ? -8.133  -24.810 36.688  1.00 33.54 ? 259 LYS A CG  1 
ATOM   754  C CD  . LYS A 1 259 ? -8.716  -25.797 37.698  1.00 39.67 ? 259 LYS A CD  1 
ATOM   755  C CE  . LYS A 1 259 ? -7.682  -26.443 38.581  1.00 44.75 ? 259 LYS A CE  1 
ATOM   756  N NZ  . LYS A 1 259 ? -8.325  -27.322 39.597  1.00 48.03 ? 259 LYS A NZ  1 
ATOM   757  N N   . ARG A 1 260 ? -4.704  -23.665 35.586  1.00 24.51 ? 260 ARG A N   1 
ATOM   758  C CA  . ARG A 1 260 ? -3.847  -24.338 34.649  1.00 24.70 ? 260 ARG A CA  1 
ATOM   759  C C   . ARG A 1 260 ? -4.135  -25.821 34.724  1.00 26.45 ? 260 ARG A C   1 
ATOM   760  O O   . ARG A 1 260 ? -4.139  -26.405 35.810  1.00 27.68 ? 260 ARG A O   1 
ATOM   761  C CB  . ARG A 1 260 ? -2.380  -24.058 34.968  1.00 25.42 ? 260 ARG A CB  1 
ATOM   762  C CG  . ARG A 1 260 ? -1.497  -24.528 33.849  1.00 26.47 ? 260 ARG A CG  1 
ATOM   763  C CD  . ARG A 1 260 ? -0.043  -24.198 34.091  1.00 30.29 ? 260 ARG A CD  1 
ATOM   764  N NE  . ARG A 1 260 ? 0.497   -25.002 35.180  1.00 35.41 ? 260 ARG A NE  1 
ATOM   765  C CZ  . ARG A 1 260 ? 1.742   -24.909 35.632  1.00 41.66 ? 260 ARG A CZ  1 
ATOM   766  N NH1 . ARG A 1 260 ? 2.591   -24.043 35.089  1.00 41.86 ? 260 ARG A NH1 1 
ATOM   767  N NH2 . ARG A 1 260 ? 2.152   -25.688 36.628  1.00 42.54 ? 260 ARG A NH2 1 
ATOM   768  N N   . LEU A 1 261 ? -4.481  -26.413 33.586  1.00 26.33 ? 261 LEU A N   1 
ATOM   769  C CA  . LEU A 1 261 ? -4.767  -27.837 33.526  1.00 27.43 ? 261 LEU A CA  1 
ATOM   770  C C   . LEU A 1 261 ? -3.495  -28.609 33.227  1.00 27.74 ? 261 LEU A C   1 
ATOM   771  O O   . LEU A 1 261 ? -3.322  -29.718 33.732  1.00 28.76 ? 261 LEU A O   1 
ATOM   772  C CB  . LEU A 1 261 ? -5.798  -28.127 32.430  1.00 28.57 ? 261 LEU A CB  1 
ATOM   773  C CG  . LEU A 1 261 ? -7.176  -27.505 32.604  1.00 31.97 ? 261 LEU A CG  1 
ATOM   774  C CD1 . LEU A 1 261 ? -8.064  -27.827 31.408  1.00 33.31 ? 261 LEU A CD1 1 
ATOM   775  C CD2 . LEU A 1 261 ? -7.835  -27.995 33.844  1.00 32.99 ? 261 LEU A CD2 1 
ATOM   776  N N   . ARG A 1 262 ? -2.656  -28.075 32.328  1.00 26.81 ? 262 ARG A N   1 
ATOM   777  C CA  . ARG A 1 262 ? -1.455  -28.773 31.902  1.00 27.02 ? 262 ARG A CA  1 
ATOM   778  C C   . ARG A 1 262 ? -0.294  -27.842 31.731  1.00 26.90 ? 262 ARG A C   1 
ATOM   779  O O   . ARG A 1 262 ? -0.462  -26.684 31.349  1.00 25.88 ? 262 ARG A O   1 
ATOM   780  C CB  . ARG A 1 262 ? -1.709  -29.418 30.529  1.00 28.48 ? 262 ARG A CB  1 
ATOM   781  C CG  . ARG A 1 262 ? -2.945  -30.297 30.490  1.00 31.80 ? 262 ARG A CG  1 
ATOM   782  C CD  . ARG A 1 262 ? -2.844  -31.321 29.415  1.00 33.19 ? 262 ARG A CD  1 
ATOM   783  N NE  . ARG A 1 262 ? -1.721  -32.236 29.634  1.00 31.39 ? 262 ARG A NE  1 
ATOM   784  C CZ  . ARG A 1 262 ? -1.501  -33.319 28.904  1.00 29.49 ? 262 ARG A CZ  1 
ATOM   785  N NH1 . ARG A 1 262 ? -2.328  -33.642 27.918  1.00 27.31 ? 262 ARG A NH1 1 
ATOM   786  N NH2 . ARG A 1 262 ? -0.468  -34.108 29.171  1.00 30.20 ? 262 ARG A NH2 1 
ATOM   787  N N   . ASN A 1 263 ? 0.903   -28.390 31.893  1.00 27.05 ? 263 ASN A N   1 
ATOM   788  C CA  . ASN A 1 263 ? 2.113   -27.670 31.614  1.00 27.72 ? 263 ASN A CA  1 
ATOM   789  C C   . ASN A 1 263 ? 2.922   -28.640 30.768  1.00 28.35 ? 263 ASN A C   1 
ATOM   790  O O   . ASN A 1 263 ? 3.621   -29.490 31.300  1.00 29.45 ? 263 ASN A O   1 
ATOM   791  C CB  . ASN A 1 263 ? 2.858   -27.274 32.890  1.00 30.08 ? 263 ASN A CB  1 
ATOM   792  C CG  . ASN A 1 263 ? 3.977   -26.299 32.585  1.00 34.12 ? 263 ASN A CG  1 
ATOM   793  O OD1 . ASN A 1 263 ? 3.954   -25.581 31.578  1.00 35.29 ? 263 ASN A OD1 1 
ATOM   794  N ND2 . ASN A 1 263 ? 4.996   -26.265 33.424  1.00 35.29 ? 263 ASN A ND2 1 
ATOM   795  N N   . MET A 1 264 ? 2.738   -28.567 29.454  1.00 27.25 ? 264 MET A N   1 
ATOM   796  C CA  . MET A 1 264 ? 3.339   -29.496 28.523  1.00 28.01 ? 264 MET A CA  1 
ATOM   797  C C   . MET A 1 264 ? 4.723   -29.096 28.096  1.00 28.43 ? 264 MET A C   1 
ATOM   798  O O   . MET A 1 264 ? 4.929   -28.067 27.446  1.00 27.78 ? 264 MET A O   1 
ATOM   799  C CB  . MET A 1 264 ? 2.419   -29.729 27.323  1.00 28.39 ? 264 MET A CB  1 
ATOM   800  C CG  . MET A 1 264 ? 1.048   -30.260 27.741  1.00 29.38 ? 264 MET A CG  1 
ATOM   801  S SD  . MET A 1 264 ? -0.110  -30.431 26.358  1.00 29.81 ? 264 MET A SD  1 
ATOM   802  C CE  . MET A 1 264 ? -0.488  -28.689 26.043  1.00 31.04 ? 264 MET A CE  1 
ATOM   803  N N   . THR A 1 265 ? 5.674   -29.960 28.418  1.00 29.28 ? 265 THR A N   1 
ATOM   804  C CA  . THR A 1 265 ? 7.045   -29.751 28.038  1.00 30.74 ? 265 THR A CA  1 
ATOM   805  C C   . THR A 1 265 ? 7.374   -30.810 26.982  1.00 32.09 ? 265 THR A C   1 
ATOM   806  O O   . THR A 1 265 ? 6.985   -31.976 27.100  1.00 34.89 ? 265 THR A O   1 
ATOM   807  C CB  . THR A 1 265 ? 7.977   -29.838 29.258  1.00 33.82 ? 265 THR A CB  1 
ATOM   808  O OG1 . THR A 1 265 ? 7.815   -31.115 29.880  1.00 35.64 ? 265 THR A OG1 1 
ATOM   809  C CG2 . THR A 1 265 ? 7.726   -28.730 30.267  1.00 34.80 ? 265 THR A CG2 1 
ATOM   810  N N   . SER A 1 266 ? 8.019   -30.389 25.934  1.00 30.56 ? 266 SER A N   1 
ATOM   811  C CA  . SER A 1 266 ? 8.481   -31.238 24.842  1.00 29.39 ? 266 SER A CA  1 
ATOM   812  C C   . SER A 1 266 ? 9.508   -30.458 24.008  1.00 28.49 ? 266 SER A C   1 
ATOM   813  O O   . SER A 1 266 ? 10.454  -31.046 23.503  1.00 28.02 ? 266 SER A O   1 
ATOM   814  C CB  . SER A 1 266 ? 7.314   -31.748 23.990  1.00 28.80 ? 266 SER A CB  1 
ATOM   815  O OG  . SER A 1 266 ? 6.584   -30.706 23.366  1.00 28.45 ? 266 SER A OG  1 
ATOM   816  N N   . HIS A 1 267 ? 9.322   -29.119 23.887  1.00 27.92 ? 267 HIS A N   1 
ATOM   817  C CA  . HIS A 1 267 ? 10.195  -28.229 23.142  1.00 27.98 ? 267 HIS A CA  1 
ATOM   818  C C   . HIS A 1 267 ? 11.495  -27.891 23.842  1.00 29.52 ? 267 HIS A C   1 
ATOM   819  O O   . HIS A 1 267 ? 11.573  -27.946 25.067  1.00 30.16 ? 267 HIS A O   1 
ATOM   820  C CB  . HIS A 1 267 ? 9.444   -26.939 22.802  1.00 27.26 ? 267 HIS A CB  1 
ATOM   821  C CG  . HIS A 1 267 ? 8.529   -27.108 21.641  1.00 26.09 ? 267 HIS A CG  1 
ATOM   822  N ND1 . HIS A 1 267 ? 9.016   -27.425 20.398  1.00 26.65 ? 267 HIS A ND1 1 
ATOM   823  C CD2 . HIS A 1 267 ? 7.180   -26.986 21.573  1.00 25.52 ? 267 HIS A CD2 1 
ATOM   824  C CE1 . HIS A 1 267 ? 7.959   -27.472 19.601  1.00 26.35 ? 267 HIS A CE1 1 
ATOM   825  N NE2 . HIS A 1 267 ? 6.829   -27.231 20.268  1.00 25.14 ? 267 HIS A NE2 1 
ATOM   826  N N   . SER A 1 268 ? 12.507  -27.520 23.056  1.00 29.79 ? 268 SER A N   1 
ATOM   827  C CA  . SER A 1 268 ? 13.825  -27.157 23.582  1.00 30.95 ? 268 SER A CA  1 
ATOM   828  C C   . SER A 1 268 ? 14.073  -25.644 23.594  1.00 30.74 ? 268 SER A C   1 
ATOM   829  O O   . SER A 1 268 ? 15.158  -25.215 23.970  1.00 32.62 ? 268 SER A O   1 
ATOM   830  C CB  . SER A 1 268 ? 14.907  -27.829 22.753  1.00 32.77 ? 268 SER A CB  1 
ATOM   831  O OG  . SER A 1 268 ? 14.856  -27.344 21.419  1.00 35.03 ? 268 SER A OG  1 
ATOM   832  N N   . ALA A 1 269 ? 13.111  -24.842 23.144  1.00 27.83 ? 269 ALA A N   1 
ATOM   833  C CA  . ALA A 1 269 ? 13.264  -23.395 23.054  1.00 26.13 ? 269 ALA A CA  1 
ATOM   834  C C   . ALA A 1 269 ? 11.867  -22.725 23.103  1.00 23.51 ? 269 ALA A C   1 
ATOM   835  O O   . ALA A 1 269 ? 10.848  -23.428 23.110  1.00 23.61 ? 269 ALA A O   1 
ATOM   836  C CB  . ALA A 1 269 ? 14.007  -23.042 21.756  1.00 26.71 ? 269 ALA A CB  1 
ATOM   837  N N   . ARG A 1 270 ? 11.796  -21.381 23.142  1.00 21.65 ? 270 ARG A N   1 
ATOM   838  C CA  . ARG A 1 270 ? 10.505  -20.695 23.246  1.00 21.28 ? 270 ARG A CA  1 
ATOM   839  C C   . ARG A 1 270 ? 9.486   -21.111 22.204  1.00 20.71 ? 270 ARG A C   1 
ATOM   840  O O   . ARG A 1 270 ? 9.813   -21.433 21.044  1.00 20.41 ? 270 ARG A O   1 
ATOM   841  C CB  . ARG A 1 270 ? 10.681  -19.183 23.256  1.00 23.29 ? 270 ARG A CB  1 
ATOM   842  C CG  . ARG A 1 270 ? 11.095  -18.609 21.935  1.00 24.71 ? 270 ARG A CG  1 
ATOM   843  C CD  . ARG A 1 270 ? 10.954  -17.097 21.977  1.00 24.98 ? 270 ARG A CD  1 
ATOM   844  N NE  . ARG A 1 270 ? 11.048  -16.497 20.639  1.00 23.92 ? 270 ARG A NE  1 
ATOM   845  C CZ  . ARG A 1 270 ? 11.237  -15.195 20.430  1.00 24.83 ? 270 ARG A CZ  1 
ATOM   846  N NH1 . ARG A 1 270 ? 11.274  -14.714 19.194  1.00 24.14 ? 270 ARG A NH1 1 
ATOM   847  N NH2 . ARG A 1 270 ? 11.363  -14.357 21.463  1.00 24.74 ? 270 ARG A NH2 1 
ATOM   848  N N   . VAL A 1 271 ? 8.222   -21.134 22.642  1.00 19.55 ? 271 VAL A N   1 
ATOM   849  C CA  . VAL A 1 271 ? 7.121   -21.526 21.773  1.00 19.90 ? 271 VAL A CA  1 
ATOM   850  C C   . VAL A 1 271 ? 6.411   -20.252 21.315  1.00 19.77 ? 271 VAL A C   1 
ATOM   851  O O   . VAL A 1 271 ? 5.614   -19.674 22.056  1.00 20.49 ? 271 VAL A O   1 
ATOM   852  C CB  . VAL A 1 271 ? 6.172   -22.496 22.520  1.00 21.46 ? 271 VAL A CB  1 
ATOM   853  C CG1 . VAL A 1 271 ? 4.967   -22.834 21.653  1.00 21.62 ? 271 VAL A CG1 1 
ATOM   854  C CG2 . VAL A 1 271 ? 6.921   -23.775 22.924  1.00 23.34 ? 271 VAL A CG2 1 
ATOM   855  N N   . GLY A 1 272 ? 6.756   -19.787 20.122  1.00 18.07 ? 272 GLY A N   1 
ATOM   856  C CA  . GLY A 1 272 ? 6.214   -18.540 19.606  1.00 19.31 ? 272 GLY A CA  1 
ATOM   857  C C   . GLY A 1 272 ? 4.974   -18.628 18.732  1.00 18.70 ? 272 GLY A C   1 
ATOM   858  O O   . GLY A 1 272 ? 4.386   -17.591 18.413  1.00 18.63 ? 272 GLY A O   1 
ATOM   859  N N   . SER A 1 273 ? 4.564   -19.841 18.318  1.00 18.21 ? 273 SER A N   1 
ATOM   860  C CA  . SER A 1 273 ? 3.372   -19.997 17.485  1.00 17.46 ? 273 SER A CA  1 
ATOM   861  C C   . SER A 1 273 ? 2.549   -21.199 17.907  1.00 17.01 ? 273 SER A C   1 
ATOM   862  O O   . SER A 1 273 ? 3.095   -22.180 18.405  1.00 17.38 ? 273 SER A O   1 
ATOM   863  C CB  . SER A 1 273 ? 3.747   -20.094 16.003  1.00 18.67 ? 273 SER A CB  1 
ATOM   864  O OG  . SER A 1 273 ? 4.600   -21.209 15.791  1.00 19.78 ? 273 SER A OG  1 
ATOM   865  N N   . LEU A 1 274 ? 1.210   -21.103 17.748  1.00 15.72 ? 274 LEU A N   1 
ATOM   866  C CA  . LEU A 1 274 ? 0.286   -22.165 18.144  1.00 16.59 ? 274 LEU A CA  1 
ATOM   867  C C   . LEU A 1 274 ? -0.883  -22.181 17.198  1.00 17.03 ? 274 LEU A C   1 
ATOM   868  O O   . LEU A 1 274 ? -1.343  -21.124 16.775  1.00 16.87 ? 274 LEU A O   1 
ATOM   869  C CB  . LEU A 1 274 ? -0.320  -21.828 19.534  1.00 16.16 ? 274 LEU A CB  1 
ATOM   870  C CG  . LEU A 1 274 ? 0.656   -21.769 20.714  1.00 17.95 ? 274 LEU A CG  1 
ATOM   871  C CD1 . LEU A 1 274 ? -0.007  -21.094 21.955  1.00 18.74 ? 274 LEU A CD1 1 
ATOM   872  C CD2 . LEU A 1 274 ? 1.128   -23.184 21.100  1.00 17.92 ? 274 LEU A CD2 1 
ATOM   873  N N   . SER A 1 275 ? -1.415  -23.361 16.934  1.00 16.95 ? 275 SER A N   1 
ATOM   874  C CA  . SER A 1 275 ? -2.655  -23.486 16.152  1.00 16.20 ? 275 SER A CA  1 
ATOM   875  C C   . SER A 1 275 ? -3.374  -24.760 16.537  1.00 17.54 ? 275 SER A C   1 
ATOM   876  O O   . SER A 1 275 ? -2.764  -25.825 16.554  1.00 18.35 ? 275 SER A O   1 
ATOM   877  C CB  . SER A 1 275 ? -2.361  -23.506 14.649  1.00 16.99 ? 275 SER A CB  1 
ATOM   878  O OG  . SER A 1 275 ? -3.580  -23.527 13.917  1.00 17.48 ? 275 SER A OG  1 
ATOM   879  N N   . TRP A 1 276 ? -4.700  -24.679 16.728  1.00 17.13 ? 276 TRP A N   1 
ATOM   880  C CA  . TRP A 1 276 ? -5.478  -25.861 17.083  1.00 18.56 ? 276 TRP A CA  1 
ATOM   881  C C   . TRP A 1 276 ? -6.147  -26.487 15.859  1.00 20.18 ? 276 TRP A C   1 
ATOM   882  O O   . TRP A 1 276 ? -6.532  -25.777 14.925  1.00 21.30 ? 276 TRP A O   1 
ATOM   883  C CB  . TRP A 1 276 ? -6.607  -25.457 18.045  1.00 18.05 ? 276 TRP A CB  1 
ATOM   884  C CG  . TRP A 1 276 ? -6.171  -25.041 19.423  1.00 18.66 ? 276 TRP A CG  1 
ATOM   885  C CD1 . TRP A 1 276 ? -5.829  -23.788 19.846  1.00 19.77 ? 276 TRP A CD1 1 
ATOM   886  C CD2 . TRP A 1 276 ? -6.179  -25.876 20.589  1.00 19.49 ? 276 TRP A CD2 1 
ATOM   887  N NE1 . TRP A 1 276 ? -5.621  -23.791 21.212  1.00 20.08 ? 276 TRP A NE1 1 
ATOM   888  C CE2 . TRP A 1 276 ? -5.818  -25.071 21.688  1.00 19.94 ? 276 TRP A CE2 1 
ATOM   889  C CE3 . TRP A 1 276 ? -6.409  -27.245 20.796  1.00 20.72 ? 276 TRP A CE3 1 
ATOM   890  C CZ2 . TRP A 1 276 ? -5.736  -25.584 22.988  1.00 20.99 ? 276 TRP A CZ2 1 
ATOM   891  C CZ3 . TRP A 1 276 ? -6.308  -27.758 22.079  1.00 21.01 ? 276 TRP A CZ3 1 
ATOM   892  C CH2 . TRP A 1 276 ? -5.958  -26.938 23.152  1.00 21.07 ? 276 TRP A CH2 1 
ATOM   893  N N   . ASN A 1 277 ? -6.360  -27.810 15.923  1.00 20.43 ? 277 ASN A N   1 
ATOM   894  C CA  . ASN A 1 277 ? -7.158  -28.608 15.011  1.00 22.18 ? 277 ASN A CA  1 
ATOM   895  C C   . ASN A 1 277 ? -7.973  -29.541 15.906  1.00 23.38 ? 277 ASN A C   1 
ATOM   896  O O   . ASN A 1 277 ? -7.458  -30.566 16.321  1.00 23.53 ? 277 ASN A O   1 
ATOM   897  C CB  . ASN A 1 277 ? -6.274  -29.422 14.099  1.00 24.48 ? 277 ASN A CB  1 
ATOM   898  C CG  . ASN A 1 277 ? -7.036  -30.184 13.059  1.00 30.53 ? 277 ASN A CG  1 
ATOM   899  O OD1 . ASN A 1 277 ? -8.209  -29.925 12.793  1.00 34.56 ? 277 ASN A OD1 1 
ATOM   900  N ND2 . ASN A 1 277 ? -6.394  -31.164 12.462  1.00 31.74 ? 277 ASN A ND2 1 
ATOM   901  N N   . SER A 1 278 ? -9.201  -29.137 16.303  1.00 23.69 ? 278 SER A N   1 
ATOM   902  C CA  . SER A 1 278 ? -10.021 -29.880 17.261  1.00 25.07 ? 278 SER A CA  1 
ATOM   903  C C   . SER A 1 278 ? -9.215  -29.968 18.603  1.00 24.89 ? 278 SER A C   1 
ATOM   904  O O   . SER A 1 278 ? -8.770  -28.914 19.070  1.00 24.60 ? 278 SER A O   1 
ATOM   905  C CB  . SER A 1 278 ? -10.462 -31.224 16.668  1.00 27.61 ? 278 SER A CB  1 
ATOM   906  O OG  . SER A 1 278 ? -11.180 -32.005 17.608  1.00 32.09 ? 278 SER A OG  1 
ATOM   907  N N   . TYR A 1 279 ? -8.962  -31.165 19.160  1.00 25.57 ? 279 TYR A N   1 
ATOM   908  C CA  . TYR A 1 279 ? -8.203  -31.356 20.397  1.00 26.61 ? 279 TYR A CA  1 
ATOM   909  C C   . TYR A 1 279 ? -6.683  -31.449 20.162  1.00 25.50 ? 279 TYR A C   1 
ATOM   910  O O   . TYR A 1 279 ? -5.948  -31.579 21.128  1.00 25.99 ? 279 TYR A O   1 
ATOM   911  C CB  . TYR A 1 279 ? -8.704  -32.596 21.172  1.00 28.50 ? 279 TYR A CB  1 
ATOM   912  C CG  . TYR A 1 279 ? -8.831  -33.836 20.311  1.00 31.96 ? 279 TYR A CG  1 
ATOM   913  C CD1 . TYR A 1 279 ? -7.709  -34.530 19.886  1.00 34.03 ? 279 TYR A CD1 1 
ATOM   914  C CD2 . TYR A 1 279 ? -10.077 -34.310 19.917  1.00 34.48 ? 279 TYR A CD2 1 
ATOM   915  C CE1 . TYR A 1 279 ? -7.818  -35.649 19.069  1.00 35.84 ? 279 TYR A CE1 1 
ATOM   916  C CE2 . TYR A 1 279 ? -10.197 -35.414 19.085  1.00 35.92 ? 279 TYR A CE2 1 
ATOM   917  C CZ  . TYR A 1 279 ? -9.065  -36.096 18.681  1.00 37.13 ? 279 TYR A CZ  1 
ATOM   918  O OH  . TYR A 1 279 ? -9.168  -37.210 17.887  1.00 38.87 ? 279 TYR A OH  1 
ATOM   919  N N   . ILE A 1 280 ? -6.208  -31.413 18.899  1.00 23.93 ? 280 ILE A N   1 
ATOM   920  C CA  . ILE A 1 280 ? -4.775  -31.424 18.645  1.00 23.13 ? 280 ILE A CA  1 
ATOM   921  C C   . ILE A 1 280 ? -4.323  -29.955 18.672  1.00 22.27 ? 280 ILE A C   1 
ATOM   922  O O   . ILE A 1 280 ? -4.946  -29.110 18.040  1.00 22.62 ? 280 ILE A O   1 
ATOM   923  C CB  . ILE A 1 280 ? -4.474  -32.081 17.276  1.00 24.56 ? 280 ILE A CB  1 
ATOM   924  C CG1 . ILE A 1 280 ? -4.789  -33.582 17.284  1.00 26.94 ? 280 ILE A CG1 1 
ATOM   925  C CG2 . ILE A 1 280 ? -3.037  -31.795 16.846  1.00 24.41 ? 280 ILE A CG2 1 
ATOM   926  C CD1 . ILE A 1 280 ? -3.995  -34.383 18.250  1.00 29.06 ? 280 ILE A CD1 1 
ATOM   927  N N   . LEU A 1 281 ? -3.251  -29.651 19.398  1.00 20.93 ? 281 LEU A N   1 
ATOM   928  C CA  . LEU A 1 281 ? -2.705  -28.311 19.454  1.00 19.41 ? 281 LEU A CA  1 
ATOM   929  C C   . LEU A 1 281 ? -1.319  -28.424 18.877  1.00 20.21 ? 281 LEU A C   1 
ATOM   930  O O   . LEU A 1 281 ? -0.543  -29.247 19.342  1.00 20.87 ? 281 LEU A O   1 
ATOM   931  C CB  . LEU A 1 281 ? -2.648  -27.846 20.920  1.00 19.34 ? 281 LEU A CB  1 
ATOM   932  C CG  . LEU A 1 281 ? -1.815  -26.583 21.173  1.00 19.83 ? 281 LEU A CG  1 
ATOM   933  C CD1 . LEU A 1 281 ? -2.459  -25.373 20.484  1.00 19.17 ? 281 LEU A CD1 1 
ATOM   934  C CD2 . LEU A 1 281 ? -1.682  -26.354 22.666  1.00 20.52 ? 281 LEU A CD2 1 
ATOM   935  N N   . SER A 1 282 ? -1.017  -27.642 17.835  1.00 18.29 ? 282 SER A N   1 
ATOM   936  C CA  . SER A 1 282 ? 0.293   -27.666 17.232  1.00 18.33 ? 282 SER A CA  1 
ATOM   937  C C   . SER A 1 282 ? 1.066   -26.490 17.764  1.00 17.91 ? 282 SER A C   1 
ATOM   938  O O   . SER A 1 282 ? 0.526   -25.390 17.874  1.00 18.21 ? 282 SER A O   1 
ATOM   939  C CB  . SER A 1 282 ? 0.157   -27.593 15.708  1.00 19.49 ? 282 SER A CB  1 
ATOM   940  O OG  . SER A 1 282 ? -0.610  -28.709 15.275  1.00 20.50 ? 282 SER A OG  1 
ATOM   941  N N   . SER A 1 283 ? 2.338   -26.698 18.083  1.00 17.19 ? 283 SER A N   1 
ATOM   942  C CA  . SER A 1 283 ? 3.168   -25.647 18.638  1.00 18.49 ? 283 SER A CA  1 
ATOM   943  C C   . SER A 1 283 ? 4.470   -25.546 17.863  1.00 19.07 ? 283 SER A C   1 
ATOM   944  O O   . SER A 1 283 ? 5.066   -26.567 17.534  1.00 19.39 ? 283 SER A O   1 
ATOM   945  C CB  . SER A 1 283 ? 3.482   -25.943 20.105  1.00 19.63 ? 283 SER A CB  1 
ATOM   946  O OG  . SER A 1 283 ? 4.088   -27.220 20.212  1.00 22.24 ? 283 SER A OG  1 
ATOM   947  N N   . GLY A 1 284 ? 4.861   -24.325 17.534  1.00 18.75 ? 284 GLY A N   1 
ATOM   948  C CA  . GLY A 1 284 ? 6.099   -24.071 16.807  1.00 19.35 ? 284 GLY A CA  1 
ATOM   949  C C   . GLY A 1 284 ? 7.098   -23.388 17.712  1.00 19.97 ? 284 GLY A C   1 
ATOM   950  O O   . GLY A 1 284 ? 6.748   -22.537 18.525  1.00 20.80 ? 284 GLY A O   1 
ATOM   951  N N   . SER A 1 285 ? 8.356   -23.757 17.567  1.00 19.96 ? 285 SER A N   1 
ATOM   952  C CA  . SER A 1 285 ? 9.399   -23.274 18.452  1.00 20.69 ? 285 SER A CA  1 
ATOM   953  C C   . SER A 1 285 ? 10.519  -22.522 17.737  1.00 20.65 ? 285 SER A C   1 
ATOM   954  O O   . SER A 1 285 ? 10.731  -22.668 16.531  1.00 20.07 ? 285 SER A O   1 
ATOM   955  C CB  . SER A 1 285 ? 9.997   -24.460 19.213  1.00 23.40 ? 285 SER A CB  1 
ATOM   956  O OG  . SER A 1 285 ? 11.092  -24.094 20.044  1.00 26.70 ? 285 SER A OG  1 
ATOM   957  N N   . ARG A 1 286 ? 11.269  -21.743 18.521  1.00 21.18 ? 286 ARG A N   1 
ATOM   958  C CA  . ARG A 1 286 ? 12.485  -21.064 18.049  1.00 22.92 ? 286 ARG A CA  1 
ATOM   959  C C   . ARG A 1 286 ? 13.507  -22.113 17.515  1.00 24.51 ? 286 ARG A C   1 
ATOM   960  O O   . ARG A 1 286 ? 14.327  -21.787 16.666  1.00 25.25 ? 286 ARG A O   1 
ATOM   961  C CB  . ARG A 1 286 ? 13.076  -20.246 19.208  1.00 25.58 ? 286 ARG A CB  1 
ATOM   962  C CG  . ARG A 1 286 ? 14.302  -19.398 18.870  1.00 30.82 ? 286 ARG A CG  1 
ATOM   963  C CD  . ARG A 1 286 ? 14.796  -18.724 20.146  1.00 35.57 ? 286 ARG A CD  1 
ATOM   964  N NE  . ARG A 1 286 ? 14.830  -17.267 20.019  1.00 39.64 ? 286 ARG A NE  1 
ATOM   965  C CZ  . ARG A 1 286 ? 14.810  -16.419 21.045  1.00 42.11 ? 286 ARG A CZ  1 
ATOM   966  N NH1 . ARG A 1 286 ? 14.740  -16.873 22.293  1.00 38.92 ? 286 ARG A NH1 1 
ATOM   967  N NH2 . ARG A 1 286 ? 14.868  -15.111 20.832  1.00 44.01 ? 286 ARG A NH2 1 
ATOM   968  N N   . SER A 1 287 ? 13.415  -23.383 17.962  1.00 24.46 ? 287 SER A N   1 
ATOM   969  C CA  . SER A 1 287 ? 14.305  -24.441 17.493  1.00 24.73 ? 287 SER A CA  1 
ATOM   970  C C   . SER A 1 287 ? 14.068  -24.817 16.017  1.00 24.49 ? 287 SER A C   1 
ATOM   971  O O   . SER A 1 287 ? 14.936  -25.431 15.403  1.00 25.91 ? 287 SER A O   1 
ATOM   972  C CB  . SER A 1 287 ? 14.115  -25.691 18.348  1.00 25.94 ? 287 SER A CB  1 
ATOM   973  O OG  . SER A 1 287 ? 12.805  -26.206 18.151  1.00 28.08 ? 287 SER A OG  1 
ATOM   974  N N   . GLY A 1 288 ? 12.871  -24.537 15.498  1.00 23.03 ? 288 GLY A N   1 
ATOM   975  C CA  . GLY A 1 288 ? 12.509  -24.896 14.128  1.00 22.79 ? 288 GLY A CA  1 
ATOM   976  C C   . GLY A 1 288 ? 11.538  -26.061 14.064  1.00 22.83 ? 288 GLY A C   1 
ATOM   977  O O   . GLY A 1 288 ? 11.019  -26.373 12.994  1.00 24.39 ? 288 GLY A O   1 
ATOM   978  N N   . HIS A 1 289 ? 11.295  -26.727 15.205  1.00 21.40 ? 289 HIS A N   1 
ATOM   979  C CA  . HIS A 1 289 ? 10.417  -27.882 15.240  1.00 21.49 ? 289 HIS A CA  1 
ATOM   980  C C   . HIS A 1 289 ? 8.979   -27.498 15.526  1.00 20.82 ? 289 HIS A C   1 
ATOM   981  O O   . HIS A 1 289 ? 8.707   -26.481 16.157  1.00 21.35 ? 289 HIS A O   1 
ATOM   982  C CB  . HIS A 1 289 ? 10.890  -28.874 16.302  1.00 23.81 ? 289 HIS A CB  1 
ATOM   983  C CG  . HIS A 1 289 ? 12.292  -29.347 16.079  1.00 28.09 ? 289 HIS A CG  1 
ATOM   984  N ND1 . HIS A 1 289 ? 12.606  -30.229 15.050  1.00 31.26 ? 289 HIS A ND1 1 
ATOM   985  C CD2 . HIS A 1 289 ? 13.424  -29.039 16.757  1.00 29.79 ? 289 HIS A CD2 1 
ATOM   986  C CE1 . HIS A 1 289 ? 13.916  -30.442 15.146  1.00 32.36 ? 289 HIS A CE1 1 
ATOM   987  N NE2 . HIS A 1 289 ? 14.453  -29.756 16.165  1.00 31.66 ? 289 HIS A NE2 1 
ATOM   988  N N   . ILE A 1 290 ? 8.065   -28.337 15.062  1.00 19.75 ? 290 ILE A N   1 
ATOM   989  C CA  . ILE A 1 290 ? 6.636   -28.220 15.327  1.00 19.04 ? 290 ILE A CA  1 
ATOM   990  C C   . ILE A 1 290 ? 6.222   -29.495 16.032  1.00 20.47 ? 290 ILE A C   1 
ATOM   991  O O   . ILE A 1 290 ? 6.556   -30.600 15.569  1.00 21.10 ? 290 ILE A O   1 
ATOM   992  C CB  . ILE A 1 290 ? 5.830   -28.031 14.033  1.00 18.66 ? 290 ILE A CB  1 
ATOM   993  C CG1 . ILE A 1 290 ? 6.163   -26.664 13.399  1.00 17.97 ? 290 ILE A CG1 1 
ATOM   994  C CG2 . ILE A 1 290 ? 4.316   -28.169 14.294  1.00 19.86 ? 290 ILE A CG2 1 
ATOM   995  C CD1 . ILE A 1 290 ? 5.901   -26.661 11.871  1.00 19.44 ? 290 ILE A CD1 1 
ATOM   996  N N   . HIS A 1 291 ? 5.508   -29.357 17.140  1.00 20.50 ? 291 HIS A N   1 
ATOM   997  C CA  . HIS A 1 291 ? 5.020   -30.520 17.868  1.00 21.27 ? 291 HIS A CA  1 
ATOM   998  C C   . HIS A 1 291 ? 3.503   -30.571 17.803  1.00 21.81 ? 291 HIS A C   1 
ATOM   999  O O   . HIS A 1 291 ? 2.875   -29.536 17.920  1.00 21.77 ? 291 HIS A O   1 
ATOM   1000 C CB  . HIS A 1 291 ? 5.471   -30.432 19.344  1.00 22.22 ? 291 HIS A CB  1 
ATOM   1001 C CG  . HIS A 1 291 ? 6.929   -30.710 19.562  1.00 25.19 ? 291 HIS A CG  1 
ATOM   1002 N ND1 . HIS A 1 291 ? 7.471   -30.716 20.829  1.00 27.24 ? 291 HIS A ND1 1 
ATOM   1003 C CD2 . HIS A 1 291 ? 7.906   -31.014 18.667  1.00 26.44 ? 291 HIS A CD2 1 
ATOM   1004 C CE1 . HIS A 1 291 ? 8.755   -31.006 20.670  1.00 27.43 ? 291 HIS A CE1 1 
ATOM   1005 N NE2 . HIS A 1 291 ? 9.060   -31.199 19.383  1.00 27.46 ? 291 HIS A NE2 1 
ATOM   1006 N N   . HIS A 1 292 ? 2.909   -31.768 17.641  1.00 21.25 ? 292 HIS A N   1 
ATOM   1007 C CA  . HIS A 1 292 ? 1.464   -31.912 17.754  1.00 21.72 ? 292 HIS A CA  1 
ATOM   1008 C C   . HIS A 1 292 ? 1.239   -32.460 19.173  1.00 22.28 ? 292 HIS A C   1 
ATOM   1009 O O   . HIS A 1 292 ? 1.895   -33.437 19.563  1.00 22.80 ? 292 HIS A O   1 
ATOM   1010 C CB  . HIS A 1 292 ? 0.887   -32.936 16.766  1.00 22.65 ? 292 HIS A CB  1 
ATOM   1011 C CG  . HIS A 1 292 ? 0.894   -32.491 15.344  1.00 22.31 ? 292 HIS A CG  1 
ATOM   1012 N ND1 . HIS A 1 292 ? 0.806   -31.147 15.000  1.00 22.31 ? 292 HIS A ND1 1 
ATOM   1013 C CD2 . HIS A 1 292 ? 0.973   -33.233 14.212  1.00 23.51 ? 292 HIS A CD2 1 
ATOM   1014 C CE1 . HIS A 1 292 ? 0.850   -31.116 13.674  1.00 23.48 ? 292 HIS A CE1 1 
ATOM   1015 N NE2 . HIS A 1 292 ? 0.944   -32.350 13.156  1.00 23.71 ? 292 HIS A NE2 1 
ATOM   1016 N N   . HIS A 1 293 ? 0.303   -31.856 19.908  1.00 21.75 ? 293 HIS A N   1 
ATOM   1017 C CA  . HIS A 1 293 ? -0.045  -32.274 21.263  1.00 22.31 ? 293 HIS A CA  1 
ATOM   1018 C C   . HIS A 1 293 ? -1.492  -32.727 21.292  1.00 23.90 ? 293 HIS A C   1 
ATOM   1019 O O   . HIS A 1 293 ? -2.363  -31.955 20.884  1.00 25.09 ? 293 HIS A O   1 
ATOM   1020 C CB  . HIS A 1 293 ? 0.102   -31.095 22.265  1.00 22.14 ? 293 HIS A CB  1 
ATOM   1021 C CG  . HIS A 1 293 ? 1.419   -30.388 22.207  1.00 22.18 ? 293 HIS A CG  1 
ATOM   1022 N ND1 . HIS A 1 293 ? 2.537   -30.886 22.858  1.00 24.06 ? 293 HIS A ND1 1 
ATOM   1023 C CD2 . HIS A 1 293 ? 1.753   -29.239 21.575  1.00 22.37 ? 293 HIS A CD2 1 
ATOM   1024 C CE1 . HIS A 1 293 ? 3.504   -30.015 22.625  1.00 25.00 ? 293 HIS A CE1 1 
ATOM   1025 N NE2 . HIS A 1 293 ? 3.088   -29.020 21.830  1.00 23.54 ? 293 HIS A NE2 1 
ATOM   1026 N N   . ASP A 1 294 ? -1.764  -33.939 21.811  1.00 23.53 ? 294 ASP A N   1 
ATOM   1027 C CA  . ASP A 1 294 ? -3.138  -34.355 22.016  1.00 23.38 ? 294 ASP A CA  1 
ATOM   1028 C C   . ASP A 1 294 ? -3.337  -33.919 23.475  1.00 23.12 ? 294 ASP A C   1 
ATOM   1029 O O   . ASP A 1 294 ? -2.836  -34.574 24.380  1.00 23.35 ? 294 ASP A O   1 
ATOM   1030 C CB  . ASP A 1 294 ? -3.300  -35.878 21.852  1.00 25.63 ? 294 ASP A CB  1 
ATOM   1031 C CG  . ASP A 1 294 ? -4.730  -36.366 22.075  1.00 29.79 ? 294 ASP A CG  1 
ATOM   1032 O OD1 . ASP A 1 294 ? -5.537  -35.611 22.696  1.00 28.91 ? 294 ASP A OD1 1 
ATOM   1033 O OD2 . ASP A 1 294 ? -5.036  -37.514 21.670  1.00 31.76 ? 294 ASP A OD2 1 
ATOM   1034 N N   . VAL A 1 295 ? -3.981  -32.769 23.692  1.00 22.25 ? 295 VAL A N   1 
ATOM   1035 C CA  . VAL A 1 295 ? -4.135  -32.189 25.028  1.00 22.56 ? 295 VAL A CA  1 
ATOM   1036 C C   . VAL A 1 295 ? -5.023  -33.000 25.983  1.00 24.42 ? 295 VAL A C   1 
ATOM   1037 O O   . VAL A 1 295 ? -5.048  -32.699 27.179  1.00 25.27 ? 295 VAL A O   1 
ATOM   1038 C CB  . VAL A 1 295 ? -4.626  -30.732 24.952  1.00 22.60 ? 295 VAL A CB  1 
ATOM   1039 C CG1 . VAL A 1 295 ? -3.757  -29.909 23.981  1.00 22.72 ? 295 VAL A CG1 1 
ATOM   1040 C CG2 . VAL A 1 295 ? -6.096  -30.686 24.541  1.00 23.15 ? 295 VAL A CG2 1 
ATOM   1041 N N   . ARG A 1 296 ? -5.744  -34.015 25.473  1.00 25.08 ? 296 ARG A N   1 
ATOM   1042 C CA  . ARG A 1 296 ? -6.606  -34.835 26.320  1.00 26.21 ? 296 ARG A CA  1 
ATOM   1043 C C   . ARG A 1 296 ? -5.851  -35.957 27.027  1.00 26.77 ? 296 ARG A C   1 
ATOM   1044 O O   . ARG A 1 296 ? -6.427  -36.582 27.929  1.00 27.22 ? 296 ARG A O   1 
ATOM   1045 C CB  . ARG A 1 296 ? -7.693  -35.524 25.476  1.00 28.49 ? 296 ARG A CB  1 
ATOM   1046 C CG  . ARG A 1 296 ? -8.541  -34.627 24.587  1.00 30.97 ? 296 ARG A CG  1 
ATOM   1047 C CD  . ARG A 1 296 ? -9.334  -35.491 23.594  1.00 33.21 ? 296 ARG A CD  1 
ATOM   1048 N NE  . ARG A 1 296 ? -8.457  -36.324 22.755  1.00 35.87 ? 296 ARG A NE  1 
ATOM   1049 C CZ  . ARG A 1 296 ? -8.869  -37.380 22.054  1.00 37.97 ? 296 ARG A CZ  1 
ATOM   1050 N NH1 . ARG A 1 296 ? -8.006  -38.077 21.324  1.00 37.49 ? 296 ARG A NH1 1 
ATOM   1051 N NH2 . ARG A 1 296 ? -10.152 -37.728 22.055  1.00 36.65 ? 296 ARG A NH2 1 
ATOM   1052 N N   . VAL A 1 297 ? -4.630  -36.302 26.562  1.00 26.39 ? 297 VAL A N   1 
ATOM   1053 C CA  . VAL A 1 297 ? -3.930  -37.471 27.078  1.00 28.57 ? 297 VAL A CA  1 
ATOM   1054 C C   . VAL A 1 297 ? -2.591  -37.170 27.770  1.00 28.94 ? 297 VAL A C   1 
ATOM   1055 O O   . VAL A 1 297 ? -1.955  -36.146 27.503  1.00 27.61 ? 297 VAL A O   1 
ATOM   1056 C CB  . VAL A 1 297 ? -3.763  -38.519 25.948  1.00 30.56 ? 297 VAL A CB  1 
ATOM   1057 C CG1 . VAL A 1 297 ? -5.120  -38.857 25.321  1.00 31.89 ? 297 VAL A CG1 1 
ATOM   1058 C CG2 . VAL A 1 297 ? -2.775  -38.048 24.879  1.00 30.98 ? 297 VAL A CG2 1 
ATOM   1059 N N   . ALA A 1 298 ? -2.204  -38.054 28.695  1.00 29.45 ? 298 ALA A N   1 
ATOM   1060 C CA  . ALA A 1 298 ? -0.980  -37.964 29.494  1.00 30.76 ? 298 ALA A CA  1 
ATOM   1061 C C   . ALA A 1 298 ? 0.285   -37.810 28.629  1.00 31.88 ? 298 ALA A C   1 
ATOM   1062 O O   . ALA A 1 298 ? 1.051   -36.878 28.853  1.00 32.68 ? 298 ALA A O   1 
ATOM   1063 C CB  . ALA A 1 298 ? -0.865  -39.176 30.410  1.00 31.06 ? 298 ALA A CB  1 
ATOM   1064 N N   . GLU A 1 299 ? 0.463   -38.666 27.604  1.00 31.62 ? 299 GLU A N   1 
ATOM   1065 C CA  . GLU A 1 299 ? 1.589   -38.599 26.678  1.00 32.40 ? 299 GLU A CA  1 
ATOM   1066 C C   . GLU A 1 299 ? 1.134   -37.705 25.538  1.00 31.77 ? 299 GLU A C   1 
ATOM   1067 O O   . GLU A 1 299 ? 0.734   -38.192 24.477  1.00 32.44 ? 299 GLU A O   1 
ATOM   1068 C CB  . GLU A 1 299 ? 1.938   -40.009 26.155  1.00 36.54 ? 299 GLU A CB  1 
ATOM   1069 N N   . HIS A 1 300 ? 1.098   -36.396 25.802  1.00 30.07 ? 300 HIS A N   1 
ATOM   1070 C CA  . HIS A 1 300 ? 0.590   -35.397 24.867  1.00 29.83 ? 300 HIS A CA  1 
ATOM   1071 C C   . HIS A 1 300 ? 1.368   -35.286 23.571  1.00 29.36 ? 300 HIS A C   1 
ATOM   1072 O O   . HIS A 1 300 ? 0.767   -34.986 22.551  1.00 28.82 ? 300 HIS A O   1 
ATOM   1073 C CB  . HIS A 1 300 ? 0.519   -34.018 25.545  1.00 30.15 ? 300 HIS A CB  1 
ATOM   1074 C CG  . HIS A 1 300 ? 1.869   -33.497 25.923  1.00 31.21 ? 300 HIS A CG  1 
ATOM   1075 N ND1 . HIS A 1 300 ? 2.636   -32.758 25.031  1.00 32.67 ? 300 HIS A ND1 1 
ATOM   1076 C CD2 . HIS A 1 300 ? 2.570   -33.666 27.069  1.00 32.23 ? 300 HIS A CD2 1 
ATOM   1077 C CE1 . HIS A 1 300 ? 3.772   -32.504 25.662  1.00 33.51 ? 300 HIS A CE1 1 
ATOM   1078 N NE2 . HIS A 1 300 ? 3.772   -33.012 26.900  1.00 33.24 ? 300 HIS A NE2 1 
ATOM   1079 N N   . HIS A 1 301 ? 2.694   -35.484 23.597  1.00 29.36 ? 301 HIS A N   1 
ATOM   1080 C CA  . HIS A 1 301 ? 3.506   -35.287 22.390  1.00 29.66 ? 301 HIS A CA  1 
ATOM   1081 C C   . HIS A 1 301 ? 3.355   -36.433 21.384  1.00 30.69 ? 301 HIS A C   1 
ATOM   1082 O O   . HIS A 1 301 ? 3.989   -37.469 21.535  1.00 31.68 ? 301 HIS A O   1 
ATOM   1083 C CB  . HIS A 1 301 ? 4.966   -35.024 22.781  1.00 29.70 ? 301 HIS A CB  1 
ATOM   1084 C CG  . HIS A 1 301 ? 5.852   -34.651 21.636  1.00 30.91 ? 301 HIS A CG  1 
ATOM   1085 N ND1 . HIS A 1 301 ? 7.222   -34.734 21.745  1.00 32.55 ? 301 HIS A ND1 1 
ATOM   1086 C CD2 . HIS A 1 301 ? 5.534   -34.176 20.405  1.00 31.54 ? 301 HIS A CD2 1 
ATOM   1087 C CE1 . HIS A 1 301 ? 7.702   -34.339 20.572  1.00 32.81 ? 301 HIS A CE1 1 
ATOM   1088 N NE2 . HIS A 1 301 ? 6.723   -33.985 19.737  1.00 32.51 ? 301 HIS A NE2 1 
ATOM   1089 N N   . VAL A 1 302 ? 2.501   -36.251 20.354  1.00 30.34 ? 302 VAL A N   1 
ATOM   1090 C CA  . VAL A 1 302 ? 2.198   -37.340 19.425  1.00 30.51 ? 302 VAL A CA  1 
ATOM   1091 C C   . VAL A 1 302 ? 2.877   -37.258 18.074  1.00 30.57 ? 302 VAL A C   1 
ATOM   1092 O O   . VAL A 1 302 ? 2.772   -38.206 17.298  1.00 30.60 ? 302 VAL A O   1 
ATOM   1093 C CB  . VAL A 1 302 ? 0.675   -37.495 19.251  1.00 31.80 ? 302 VAL A CB  1 
ATOM   1094 C CG1 . VAL A 1 302 ? 0.022   -37.835 20.592  1.00 32.89 ? 302 VAL A CG1 1 
ATOM   1095 C CG2 . VAL A 1 302 ? 0.055   -36.232 18.651  1.00 32.15 ? 302 VAL A CG2 1 
ATOM   1096 N N   . ALA A 1 303 ? 3.545   -36.143 17.761  1.00 29.86 ? 303 ALA A N   1 
ATOM   1097 C CA  . ALA A 1 303 ? 4.231   -36.009 16.469  1.00 29.80 ? 303 ALA A CA  1 
ATOM   1098 C C   . ALA A 1 303 ? 5.219   -34.856 16.506  1.00 28.50 ? 303 ALA A C   1 
ATOM   1099 O O   . ALA A 1 303 ? 4.989   -33.872 17.211  1.00 27.59 ? 303 ALA A O   1 
ATOM   1100 C CB  . ALA A 1 303 ? 3.221   -35.760 15.344  1.00 29.88 ? 303 ALA A CB  1 
ATOM   1101 N N   . THR A 1 304 ? 6.293   -34.969 15.708  1.00 28.08 ? 304 THR A N   1 
ATOM   1102 C CA  . THR A 1 304 ? 7.300   -33.921 15.528  1.00 27.86 ? 304 THR A CA  1 
ATOM   1103 C C   . THR A 1 304 ? 7.439   -33.695 14.011  1.00 27.00 ? 304 THR A C   1 
ATOM   1104 O O   . THR A 1 304 ? 7.698   -34.638 13.253  1.00 28.06 ? 304 THR A O   1 
ATOM   1105 C CB  . THR A 1 304 ? 8.657   -34.307 16.145  1.00 30.08 ? 304 THR A CB  1 
ATOM   1106 O OG1 . THR A 1 304 ? 8.512   -34.463 17.562  1.00 30.68 ? 304 THR A OG1 1 
ATOM   1107 C CG2 . THR A 1 304 ? 9.737   -33.251 15.867  1.00 30.63 ? 304 THR A CG2 1 
ATOM   1108 N N   . LEU A 1 305 ? 7.249   -32.447 13.581  1.00 24.99 ? 305 LEU A N   1 
ATOM   1109 C CA  . LEU A 1 305 ? 7.326   -32.022 12.184  1.00 24.62 ? 305 LEU A CA  1 
ATOM   1110 C C   . LEU A 1 305 ? 8.561   -31.146 12.107  1.00 25.04 ? 305 LEU A C   1 
ATOM   1111 O O   . LEU A 1 305 ? 8.616   -30.097 12.768  1.00 25.13 ? 305 LEU A O   1 
ATOM   1112 C CB  . LEU A 1 305 ? 6.080   -31.203 11.807  1.00 23.75 ? 305 LEU A CB  1 
ATOM   1113 C CG  . LEU A 1 305 ? 4.806   -31.975 11.429  1.00 25.20 ? 305 LEU A CG  1 
ATOM   1114 C CD1 . LEU A 1 305 ? 4.383   -32.979 12.529  1.00 25.96 ? 305 LEU A CD1 1 
ATOM   1115 C CD2 . LEU A 1 305 ? 3.667   -31.005 11.169  1.00 24.20 ? 305 LEU A CD2 1 
ATOM   1116 N N   . SER A 1 306 ? 9.568   -31.572 11.345  1.00 24.52 ? 306 SER A N   1 
ATOM   1117 C CA  . SER A 1 306 ? 10.829  -30.848 11.283  1.00 24.79 ? 306 SER A CA  1 
ATOM   1118 C C   . SER A 1 306 ? 11.150  -30.405 9.866   1.00 24.47 ? 306 SER A C   1 
ATOM   1119 O O   . SER A 1 306 ? 11.792  -31.150 9.117   1.00 25.64 ? 306 SER A O   1 
ATOM   1120 C CB  . SER A 1 306 ? 11.960  -31.726 11.809  1.00 27.45 ? 306 SER A CB  1 
ATOM   1121 O OG  . SER A 1 306 ? 11.697  -32.032 13.170  1.00 30.81 ? 306 SER A OG  1 
ATOM   1122 N N   . GLY A 1 307 ? 10.684  -29.213 9.506   1.00 22.78 ? 307 GLY A N   1 
ATOM   1123 C CA  . GLY A 1 307 ? 10.924  -28.660 8.174   1.00 22.80 ? 307 GLY A CA  1 
ATOM   1124 C C   . GLY A 1 307 ? 11.480  -27.239 8.180   1.00 22.70 ? 307 GLY A C   1 
ATOM   1125 O O   . GLY A 1 307 ? 11.533  -26.589 7.133   1.00 23.82 ? 307 GLY A O   1 
ATOM   1126 N N   . HIS A 1 308 ? 11.915  -26.750 9.348   1.00 21.77 ? 308 HIS A N   1 
ATOM   1127 C CA  . HIS A 1 308 ? 12.472  -25.410 9.459   1.00 21.70 ? 308 HIS A CA  1 
ATOM   1128 C C   . HIS A 1 308 ? 13.809  -25.448 10.177  1.00 23.71 ? 308 HIS A C   1 
ATOM   1129 O O   . HIS A 1 308 ? 13.987  -26.210 11.142  1.00 25.46 ? 308 HIS A O   1 
ATOM   1130 C CB  . HIS A 1 308 ? 11.536  -24.459 10.206  1.00 21.28 ? 308 HIS A CB  1 
ATOM   1131 C CG  . HIS A 1 308 ? 10.272  -24.158 9.474   1.00 19.52 ? 308 HIS A CG  1 
ATOM   1132 N ND1 . HIS A 1 308 ? 10.206  -23.130 8.551   1.00 20.31 ? 308 HIS A ND1 1 
ATOM   1133 C CD2 . HIS A 1 308 ? 9.051   -24.728 9.588   1.00 19.42 ? 308 HIS A CD2 1 
ATOM   1134 C CE1 . HIS A 1 308 ? 8.946   -23.119 8.125   1.00 19.23 ? 308 HIS A CE1 1 
ATOM   1135 N NE2 . HIS A 1 308 ? 8.219   -24.065 8.715   1.00 19.25 ? 308 HIS A NE2 1 
ATOM   1136 N N   . SER A 1 309 ? 14.716  -24.584 9.766   1.00 24.61 ? 309 SER A N   1 
ATOM   1137 C CA  . SER A 1 309 ? 16.027  -24.504 10.430  1.00 25.22 ? 309 SER A CA  1 
ATOM   1138 C C   . SER A 1 309 ? 16.137  -23.305 11.364  1.00 25.65 ? 309 SER A C   1 
ATOM   1139 O O   . SER A 1 309 ? 17.179  -23.138 11.989  1.00 26.86 ? 309 SER A O   1 
ATOM   1140 C CB  . SER A 1 309 ? 17.165  -24.466 9.417   1.00 26.43 ? 309 SER A CB  1 
ATOM   1141 O OG  . SER A 1 309 ? 17.028  -23.365 8.534   1.00 28.20 ? 309 SER A OG  1 
ATOM   1142 N N   . GLN A 1 310 ? 15.107  -22.436 11.411  1.00 24.34 ? 310 GLN A N   1 
ATOM   1143 C CA  . GLN A 1 310 ? 15.040  -21.255 12.269  1.00 23.37 ? 310 GLN A CA  1 
ATOM   1144 C C   . GLN A 1 310 ? 13.611  -21.189 12.860  1.00 22.43 ? 310 GLN A C   1 
ATOM   1145 O O   . GLN A 1 310 ? 12.770  -22.034 12.555  1.00 21.86 ? 310 GLN A O   1 
ATOM   1146 C CB  . GLN A 1 310 ? 15.390  -19.984 11.460  1.00 24.35 ? 310 GLN A CB  1 
ATOM   1147 C CG  . GLN A 1 310 ? 16.803  -20.014 10.820  1.00 29.14 ? 310 GLN A CG  1 
ATOM   1148 C CD  . GLN A 1 310 ? 17.938  -19.850 11.800  1.00 35.55 ? 310 GLN A CD  1 
ATOM   1149 O OE1 . GLN A 1 310 ? 17.766  -19.352 12.911  1.00 37.66 ? 310 GLN A OE1 1 
ATOM   1150 N NE2 . GLN A 1 310 ? 19.151  -20.249 11.403  1.00 37.99 ? 310 GLN A NE2 1 
ATOM   1151 N N   . GLU A 1 311 ? 13.352  -20.188 13.693  1.00 21.62 ? 311 GLU A N   1 
ATOM   1152 C CA  . GLU A 1 311 ? 12.104  -20.061 14.435  1.00 20.39 ? 311 GLU A CA  1 
ATOM   1153 C C   . GLU A 1 311 ? 10.838  -20.201 13.614  1.00 20.24 ? 311 GLU A C   1 
ATOM   1154 O O   . GLU A 1 311 ? 10.715  -19.591 12.558  1.00 20.77 ? 311 GLU A O   1 
ATOM   1155 C CB  . GLU A 1 311 ? 12.087  -18.729 15.204  1.00 21.49 ? 311 GLU A CB  1 
ATOM   1156 C CG  . GLU A 1 311 ? 10.818  -18.567 16.031  1.00 23.29 ? 311 GLU A CG  1 
ATOM   1157 C CD  . GLU A 1 311 ? 10.945  -17.652 17.233  1.00 27.54 ? 311 GLU A CD  1 
ATOM   1158 O OE1 . GLU A 1 311 ? 10.241  -17.886 18.248  1.00 25.99 ? 311 GLU A OE1 1 
ATOM   1159 O OE2 . GLU A 1 311 ? 11.745  -16.690 17.149  1.00 27.84 ? 311 GLU A OE2 1 
ATOM   1160 N N   . VAL A 1 312 ? 9.899   -21.027 14.088  1.00 19.44 ? 312 VAL A N   1 
ATOM   1161 C CA  . VAL A 1 312 ? 8.606   -21.158 13.448  1.00 19.27 ? 312 VAL A CA  1 
ATOM   1162 C C   . VAL A 1 312 ? 7.717   -20.052 14.010  1.00 19.98 ? 312 VAL A C   1 
ATOM   1163 O O   . VAL A 1 312 ? 7.254   -20.148 15.154  1.00 20.87 ? 312 VAL A O   1 
ATOM   1164 C CB  . VAL A 1 312 ? 7.968   -22.535 13.694  1.00 19.23 ? 312 VAL A CB  1 
ATOM   1165 C CG1 . VAL A 1 312 ? 6.606   -22.615 12.993  1.00 19.35 ? 312 VAL A CG1 1 
ATOM   1166 C CG2 . VAL A 1 312 ? 8.893   -23.654 13.234  1.00 19.40 ? 312 VAL A CG2 1 
ATOM   1167 N N   . CYS A 1 313 ? 7.524   -18.987 13.239  1.00 18.87 ? 313 CYS A N   1 
ATOM   1168 C CA  . CYS A 1 313 ? 6.780   -17.824 13.693  1.00 19.07 ? 313 CYS A CA  1 
ATOM   1169 C C   . CYS A 1 313 ? 5.338   -17.752 13.174  1.00 19.36 ? 313 CYS A C   1 
ATOM   1170 O O   . CYS A 1 313 ? 4.571   -16.937 13.675  1.00 20.23 ? 313 CYS A O   1 
ATOM   1171 C CB  . CYS A 1 313 ? 7.554   -16.555 13.368  1.00 20.17 ? 313 CYS A CB  1 
ATOM   1172 S SG  . CYS A 1 313 ? 8.172   -16.480 11.662  1.00 22.35 ? 313 CYS A SG  1 
ATOM   1173 N N   . GLY A 1 314 ? 4.994   -18.543 12.153  1.00 17.78 ? 314 GLY A N   1 
ATOM   1174 C CA  . GLY A 1 314 ? 3.614   -18.578 11.663  1.00 17.04 ? 314 GLY A CA  1 
ATOM   1175 C C   . GLY A 1 314 ? 3.125   -20.015 11.635  1.00 16.15 ? 314 GLY A C   1 
ATOM   1176 O O   . GLY A 1 314 ? 3.872   -20.884 11.222  1.00 16.37 ? 314 GLY A O   1 
ATOM   1177 N N   . LEU A 1 315 ? 1.902   -20.298 12.120  1.00 16.16 ? 315 LEU A N   1 
ATOM   1178 C CA  . LEU A 1 315 ? 1.452   -21.694 12.199  1.00 16.74 ? 315 LEU A CA  1 
ATOM   1179 C C   . LEU A 1 315 ? -0.057  -21.680 12.166  1.00 16.80 ? 315 LEU A C   1 
ATOM   1180 O O   . LEU A 1 315 ? -0.680  -21.013 13.000  1.00 17.34 ? 315 LEU A O   1 
ATOM   1181 C CB  . LEU A 1 315 ? 1.986   -22.315 13.514  1.00 17.27 ? 315 LEU A CB  1 
ATOM   1182 C CG  . LEU A 1 315 ? 1.815   -23.838 13.685  1.00 19.58 ? 315 LEU A CG  1 
ATOM   1183 C CD1 . LEU A 1 315 ? 2.637   -24.611 12.647  1.00 20.07 ? 315 LEU A CD1 1 
ATOM   1184 C CD2 . LEU A 1 315 ? 2.255   -24.264 15.066  1.00 20.77 ? 315 LEU A CD2 1 
ATOM   1185 N N   . ARG A 1 316 ? -0.648  -22.334 11.162  1.00 15.73 ? 316 ARG A N   1 
ATOM   1186 C CA  . ARG A 1 316 ? -2.098  -22.267 10.997  1.00 16.81 ? 316 ARG A CA  1 
ATOM   1187 C C   . ARG A 1 316 ? -2.668  -23.496 10.342  1.00 17.52 ? 316 ARG A C   1 
ATOM   1188 O O   . ARG A 1 316 ? -2.381  -23.806 9.161   1.00 16.67 ? 316 ARG A O   1 
ATOM   1189 C CB  . ARG A 1 316 ? -2.465  -21.028 10.145  1.00 20.01 ? 316 ARG A CB  1 
ATOM   1190 C CG  . ARG A 1 316 ? -3.853  -20.453 10.407  1.00 24.75 ? 316 ARG A CG  1 
ATOM   1191 C CD  . ARG A 1 316 ? -3.812  -19.458 11.570  1.00 28.70 ? 316 ARG A CD  1 
ATOM   1192 N NE  . ARG A 1 316 ? -2.956  -18.319 11.243  1.00 32.62 ? 316 ARG A NE  1 
ATOM   1193 C CZ  . ARG A 1 316 ? -2.013  -17.823 12.036  1.00 36.71 ? 316 ARG A CZ  1 
ATOM   1194 N NH1 . ARG A 1 316 ? -1.854  -18.295 13.266  1.00 36.27 ? 316 ARG A NH1 1 
ATOM   1195 N NH2 . ARG A 1 316 ? -1.249  -16.820 11.621  1.00 37.49 ? 316 ARG A NH2 1 
ATOM   1196 N N   . TRP A 1 317 ? -3.559  -24.165 11.080  1.00 17.37 ? 317 TRP A N   1 
ATOM   1197 C CA  . TRP A 1 317 ? -4.286  -25.280 10.505  1.00 18.00 ? 317 TRP A CA  1 
ATOM   1198 C C   . TRP A 1 317 ? -5.352  -24.707 9.577   1.00 19.99 ? 317 TRP A C   1 
ATOM   1199 O O   . TRP A 1 317 ? -5.959  -23.657 9.867   1.00 20.43 ? 317 TRP A O   1 
ATOM   1200 C CB  . TRP A 1 317 ? -5.015  -26.043 11.613  1.00 18.09 ? 317 TRP A CB  1 
ATOM   1201 C CG  . TRP A 1 317 ? -4.168  -27.095 12.230  1.00 19.01 ? 317 TRP A CG  1 
ATOM   1202 C CD1 . TRP A 1 317 ? -3.507  -27.024 13.416  1.00 20.09 ? 317 TRP A CD1 1 
ATOM   1203 C CD2 . TRP A 1 317 ? -3.891  -28.382 11.687  1.00 20.27 ? 317 TRP A CD2 1 
ATOM   1204 N NE1 . TRP A 1 317 ? -2.856  -28.205 13.663  1.00 20.88 ? 317 TRP A NE1 1 
ATOM   1205 C CE2 . TRP A 1 317 ? -3.095  -29.069 12.625  1.00 21.17 ? 317 TRP A CE2 1 
ATOM   1206 C CE3 . TRP A 1 317 ? -4.305  -29.055 10.532  1.00 21.39 ? 317 TRP A CE3 1 
ATOM   1207 C CZ2 . TRP A 1 317 ? -2.673  -30.377 12.424  1.00 22.13 ? 317 TRP A CZ2 1 
ATOM   1208 C CZ3 . TRP A 1 317 ? -3.870  -30.348 10.324  1.00 22.96 ? 317 TRP A CZ3 1 
ATOM   1209 C CH2 . TRP A 1 317 ? -3.076  -31.001 11.269  1.00 23.27 ? 317 TRP A CH2 1 
ATOM   1210 N N   . ALA A 1 318 ? -5.616  -25.413 8.475   1.00 20.97 ? 318 ALA A N   1 
ATOM   1211 C CA  . ALA A 1 318 ? -6.677  -25.010 7.572   1.00 22.47 ? 318 ALA A CA  1 
ATOM   1212 C C   . ALA A 1 318 ? -8.035  -25.219 8.272   1.00 24.35 ? 318 ALA A C   1 
ATOM   1213 O O   . ALA A 1 318 ? -8.165  -26.118 9.104   1.00 22.96 ? 318 ALA A O   1 
ATOM   1214 C CB  . ALA A 1 318 ? -6.609  -25.856 6.310   1.00 22.76 ? 318 ALA A CB  1 
ATOM   1215 N N   . PRO A 1 319 ? -9.049  -24.392 7.963   1.00 26.99 ? 319 PRO A N   1 
ATOM   1216 C CA  . PRO A 1 319 ? -10.379 -24.568 8.590   1.00 28.16 ? 319 PRO A CA  1 
ATOM   1217 C C   . PRO A 1 319 ? -10.986 -25.963 8.405   1.00 28.51 ? 319 PRO A C   1 
ATOM   1218 O O   . PRO A 1 319 ? -11.750 -26.419 9.270   1.00 29.30 ? 319 PRO A O   1 
ATOM   1219 C CB  . PRO A 1 319 ? -11.228 -23.499 7.899   1.00 29.84 ? 319 PRO A CB  1 
ATOM   1220 C CG  . PRO A 1 319 ? -10.236 -22.459 7.464   1.00 30.50 ? 319 PRO A CG  1 
ATOM   1221 C CD  . PRO A 1 319 ? -9.035  -23.237 7.050   1.00 28.01 ? 319 PRO A CD  1 
ATOM   1222 N N   . ASP A 1 320 ? -10.663 -26.648 7.304   1.00 27.52 ? 320 ASP A N   1 
ATOM   1223 C CA  . ASP A 1 320 ? -11.173 -28.015 7.109   1.00 28.11 ? 320 ASP A CA  1 
ATOM   1224 C C   . ASP A 1 320 ? -10.279 -29.116 7.736   1.00 28.24 ? 320 ASP A C   1 
ATOM   1225 O O   . ASP A 1 320 ? -10.609 -30.297 7.645   1.00 28.15 ? 320 ASP A O   1 
ATOM   1226 C CB  . ASP A 1 320 ? -11.452 -28.296 5.641   1.00 29.32 ? 320 ASP A CB  1 
ATOM   1227 C CG  . ASP A 1 320 ? -10.245 -28.281 4.729   1.00 32.57 ? 320 ASP A CG  1 
ATOM   1228 O OD1 . ASP A 1 320 ? -9.098  -28.200 5.245   1.00 31.44 ? 320 ASP A OD1 1 
ATOM   1229 O OD2 . ASP A 1 320 ? -10.441 -28.342 3.500   1.00 34.95 ? 320 ASP A OD2 1 
ATOM   1230 N N   . GLY A 1 321 ? -9.160  -28.722 8.340   1.00 27.68 ? 321 GLY A N   1 
ATOM   1231 C CA  . GLY A 1 321 ? -8.214  -29.633 8.973   1.00 28.47 ? 321 GLY A CA  1 
ATOM   1232 C C   . GLY A 1 321 ? -7.435  -30.527 8.017   1.00 28.68 ? 321 GLY A C   1 
ATOM   1233 O O   . GLY A 1 321 ? -6.811  -31.494 8.459   1.00 29.65 ? 321 GLY A O   1 
ATOM   1234 N N   . ARG A 1 322 ? -7.483  -30.259 6.700   1.00 27.59 ? 322 ARG A N   1 
ATOM   1235 C CA  . ARG A 1 322 ? -6.782  -31.113 5.735   1.00 27.04 ? 322 ARG A CA  1 
ATOM   1236 C C   . ARG A 1 322 ? -5.290  -30.770 5.600   1.00 25.80 ? 322 ARG A C   1 
ATOM   1237 O O   . ARG A 1 322 ? -4.523  -31.586 5.098   1.00 26.56 ? 322 ARG A O   1 
ATOM   1238 C CB  . ARG A 1 322 ? -7.443  -31.037 4.361   1.00 29.84 ? 322 ARG A CB  1 
ATOM   1239 C CG  . ARG A 1 322 ? -8.828  -31.685 4.299   1.00 35.28 ? 322 ARG A CG  1 
ATOM   1240 C CD  . ARG A 1 322 ? -9.523  -31.433 2.970   1.00 40.93 ? 322 ARG A CD  1 
ATOM   1241 N NE  . ARG A 1 322 ? -8.739  -31.885 1.815   1.00 46.01 ? 322 ARG A NE  1 
ATOM   1242 C CZ  . ARG A 1 322 ? -8.167  -31.069 0.931   1.00 48.11 ? 322 ARG A CZ  1 
ATOM   1243 N NH1 . ARG A 1 322 ? -8.285  -29.752 1.058   1.00 46.24 ? 322 ARG A NH1 1 
ATOM   1244 N NH2 . ARG A 1 322 ? -7.471  -31.565 -0.084  1.00 48.35 ? 322 ARG A NH2 1 
ATOM   1245 N N   . HIS A 1 323 ? -4.894  -29.554 5.954   1.00 24.12 ? 323 HIS A N   1 
ATOM   1246 C CA  . HIS A 1 323 ? -3.491  -29.133 5.846   1.00 22.40 ? 323 HIS A CA  1 
ATOM   1247 C C   . HIS A 1 323 ? -3.095  -28.243 7.027   1.00 20.67 ? 323 HIS A C   1 
ATOM   1248 O O   . HIS A 1 323 ? -3.945  -27.565 7.586   1.00 20.06 ? 323 HIS A O   1 
ATOM   1249 C CB  . HIS A 1 323 ? -3.294  -28.294 4.566   1.00 23.37 ? 323 HIS A CB  1 
ATOM   1250 C CG  . HIS A 1 323 ? -3.607  -28.995 3.282   1.00 26.45 ? 323 HIS A CG  1 
ATOM   1251 N ND1 . HIS A 1 323 ? -4.856  -28.884 2.682   1.00 28.95 ? 323 HIS A ND1 1 
ATOM   1252 C CD2 . HIS A 1 323 ? -2.813  -29.757 2.497   1.00 28.12 ? 323 HIS A CD2 1 
ATOM   1253 C CE1 . HIS A 1 323 ? -4.787  -29.602 1.568   1.00 28.87 ? 323 HIS A CE1 1 
ATOM   1254 N NE2 . HIS A 1 323 ? -3.586  -30.165 1.427   1.00 29.68 ? 323 HIS A NE2 1 
ATOM   1255 N N   . LEU A 1 324 ? -1.791  -28.177 7.339   1.00 19.41 ? 324 LEU A N   1 
ATOM   1256 C CA  . LEU A 1 324 ? -1.258  -27.263 8.342   1.00 18.88 ? 324 LEU A CA  1 
ATOM   1257 C C   . LEU A 1 324 ? -0.182  -26.443 7.626   1.00 18.10 ? 324 LEU A C   1 
ATOM   1258 O O   . LEU A 1 324 ? 0.697   -27.042 7.019   1.00 18.80 ? 324 LEU A O   1 
ATOM   1259 C CB  . LEU A 1 324 ? -0.606  -28.037 9.500   1.00 19.38 ? 324 LEU A CB  1 
ATOM   1260 C CG  . LEU A 1 324 ? 0.270   -27.236 10.473  1.00 19.75 ? 324 LEU A CG  1 
ATOM   1261 C CD1 . LEU A 1 324 ? -0.538  -26.173 11.205  1.00 19.65 ? 324 LEU A CD1 1 
ATOM   1262 C CD2 . LEU A 1 324 ? 0.940   -28.167 11.483  1.00 20.95 ? 324 LEU A CD2 1 
ATOM   1263 N N   . ALA A 1 325 ? -0.224  -25.115 7.717   1.00 16.57 ? 325 ALA A N   1 
ATOM   1264 C CA  . ALA A 1 325 ? 0.812   -24.298 7.100   1.00 17.78 ? 325 ALA A CA  1 
ATOM   1265 C C   . ALA A 1 325 ? 1.738   -23.747 8.170   1.00 17.43 ? 325 ALA A C   1 
ATOM   1266 O O   . ALA A 1 325 ? 1.280   -23.329 9.236   1.00 17.83 ? 325 ALA A O   1 
ATOM   1267 C CB  . ALA A 1 325 ? 0.185   -23.150 6.316   1.00 18.62 ? 325 ALA A CB  1 
ATOM   1268 N N   . SER A 1 326 ? 3.028   -23.709 7.879   1.00 16.15 ? 326 SER A N   1 
ATOM   1269 C CA  . SER A 1 326 ? 4.000   -23.117 8.802   1.00 16.47 ? 326 SER A CA  1 
ATOM   1270 C C   . SER A 1 326 ? 4.909   -22.166 8.069   1.00 16.79 ? 326 SER A C   1 
ATOM   1271 O O   . SER A 1 326 ? 5.251   -22.430 6.914   1.00 16.27 ? 326 SER A O   1 
ATOM   1272 C CB  . SER A 1 326 ? 4.839   -24.166 9.518   1.00 18.70 ? 326 SER A CB  1 
ATOM   1273 O OG  . SER A 1 326 ? 5.614   -24.984 8.652   1.00 21.49 ? 326 SER A OG  1 
ATOM   1274 N N   . GLY A 1 327 ? 5.214   -21.045 8.697   1.00 16.68 ? 327 GLY A N   1 
ATOM   1275 C CA  . GLY A 1 327 ? 6.166   -20.061 8.178   1.00 17.09 ? 327 GLY A CA  1 
ATOM   1276 C C   . GLY A 1 327 ? 7.298   -19.852 9.168   1.00 17.28 ? 327 GLY A C   1 
ATOM   1277 O O   . GLY A 1 327 ? 7.084   -19.852 10.394  1.00 17.36 ? 327 GLY A O   1 
ATOM   1278 N N   . GLY A 1 328 ? 8.509   -19.652 8.657   1.00 17.56 ? 328 GLY A N   1 
ATOM   1279 C CA  . GLY A 1 328 ? 9.651   -19.532 9.543   1.00 18.73 ? 328 GLY A CA  1 
ATOM   1280 C C   . GLY A 1 328 ? 10.558  -18.366 9.295   1.00 19.20 ? 328 GLY A C   1 
ATOM   1281 O O   . GLY A 1 328 ? 10.475  -17.717 8.250   1.00 19.38 ? 328 GLY A O   1 
ATOM   1282 N N   . ASN A 1 329 ? 11.477  -18.144 10.245  1.00 19.26 ? 329 ASN A N   1 
ATOM   1283 C CA  . ASN A 1 329 ? 12.525  -17.134 10.098  1.00 20.38 ? 329 ASN A CA  1 
ATOM   1284 C C   . ASN A 1 329 ? 13.640  -17.610 9.127   1.00 22.34 ? 329 ASN A C   1 
ATOM   1285 O O   . ASN A 1 329 ? 14.654  -16.935 8.953   1.00 23.66 ? 329 ASN A O   1 
ATOM   1286 C CB  . ASN A 1 329 ? 13.113  -16.785 11.452  1.00 21.97 ? 329 ASN A CB  1 
ATOM   1287 C CG  . ASN A 1 329 ? 14.023  -15.595 11.375  1.00 25.54 ? 329 ASN A CG  1 
ATOM   1288 O OD1 . ASN A 1 329 ? 13.715  -14.598 10.701  1.00 25.33 ? 329 ASN A OD1 1 
ATOM   1289 N ND2 . ASN A 1 329 ? 15.167  -15.688 12.043  1.00 26.84 ? 329 ASN A ND2 1 
ATOM   1290 N N   . ASP A 1 330 ? 13.484  -18.808 8.552   1.00 21.89 ? 330 ASP A N   1 
ATOM   1291 C CA  . ASP A 1 330 ? 14.352  -19.352 7.524   1.00 21.81 ? 330 ASP A CA  1 
ATOM   1292 C C   . ASP A 1 330 ? 13.754  -19.037 6.117   1.00 22.28 ? 330 ASP A C   1 
ATOM   1293 O O   . ASP A 1 330 ? 14.204  -19.634 5.135   1.00 22.93 ? 330 ASP A O   1 
ATOM   1294 C CB  . ASP A 1 330 ? 14.541  -20.863 7.707   1.00 22.46 ? 330 ASP A CB  1 
ATOM   1295 C CG  . ASP A 1 330 ? 13.254  -21.676 7.776   1.00 24.31 ? 330 ASP A CG  1 
ATOM   1296 O OD1 . ASP A 1 330 ? 12.159  -21.068 7.771   1.00 24.32 ? 330 ASP A OD1 1 
ATOM   1297 O OD2 . ASP A 1 330 ? 13.347  -22.928 7.803   1.00 25.72 ? 330 ASP A OD2 1 
ATOM   1298 N N   . ASN A 1 331 ? 12.751  -18.098 6.029   1.00 21.61 ? 331 ASN A N   1 
ATOM   1299 C CA  . ASN A 1 331 ? 12.167  -17.661 4.758   1.00 21.82 ? 331 ASN A CA  1 
ATOM   1300 C C   . ASN A 1 331 ? 11.406  -18.781 4.059   1.00 22.03 ? 331 ASN A C   1 
ATOM   1301 O O   . ASN A 1 331 ? 11.296  -18.736 2.830   1.00 23.66 ? 331 ASN A O   1 
ATOM   1302 C CB  . ASN A 1 331 ? 13.267  -17.097 3.814   1.00 23.78 ? 331 ASN A CB  1 
ATOM   1303 C CG  . ASN A 1 331 ? 14.246  -16.219 4.551   1.00 27.77 ? 331 ASN A CG  1 
ATOM   1304 O OD1 . ASN A 1 331 ? 13.852  -15.320 5.282   1.00 24.93 ? 331 ASN A OD1 1 
ATOM   1305 N ND2 . ASN A 1 331 ? 15.536  -16.516 4.424   1.00 31.90 ? 331 ASN A ND2 1 
ATOM   1306 N N   . LEU A 1 332 ? 10.979  -19.832 4.794   1.00 19.45 ? 332 LEU A N   1 
ATOM   1307 C CA  . LEU A 1 332 ? 10.279  -20.940 4.137   1.00 18.49 ? 332 LEU A CA  1 
ATOM   1308 C C   . LEU A 1 332 ? 8.822   -20.987 4.592   1.00 16.94 ? 332 LEU A C   1 
ATOM   1309 O O   . LEU A 1 332 ? 8.515   -20.686 5.745   1.00 17.52 ? 332 LEU A O   1 
ATOM   1310 C CB  . LEU A 1 332 ? 10.873  -22.287 4.570   1.00 18.77 ? 332 LEU A CB  1 
ATOM   1311 C CG  . LEU A 1 332 ? 12.315  -22.627 4.235   1.00 22.63 ? 332 LEU A CG  1 
ATOM   1312 C CD1 . LEU A 1 332 ? 12.632  -24.039 4.714   1.00 24.53 ? 332 LEU A CD1 1 
ATOM   1313 C CD2 . LEU A 1 332 ? 12.523  -22.608 2.750   1.00 24.24 ? 332 LEU A CD2 1 
ATOM   1314 N N   . VAL A 1 333 ? 7.976   -21.486 3.730   1.00 15.41 ? 333 VAL A N   1 
ATOM   1315 C CA  . VAL A 1 333 ? 6.602   -21.832 4.058   1.00 15.40 ? 333 VAL A CA  1 
ATOM   1316 C C   . VAL A 1 333 ? 6.494   -23.333 3.784   1.00 16.32 ? 333 VAL A C   1 
ATOM   1317 O O   . VAL A 1 333 ? 6.842   -23.767 2.687   1.00 17.03 ? 333 VAL A O   1 
ATOM   1318 C CB  . VAL A 1 333 ? 5.579   -21.106 3.195   1.00 16.74 ? 333 VAL A CB  1 
ATOM   1319 C CG1 . VAL A 1 333 ? 4.164   -21.618 3.497   1.00 16.66 ? 333 VAL A CG1 1 
ATOM   1320 C CG2 . VAL A 1 333 ? 5.673   -19.594 3.396   1.00 19.34 ? 333 VAL A CG2 1 
ATOM   1321 N N   . ASN A 1 334 ? 6.057   -24.126 4.764   1.00 16.00 ? 334 ASN A N   1 
ATOM   1322 C CA  . ASN A 1 334 ? 5.803   -25.545 4.525   1.00 16.43 ? 334 ASN A CA  1 
ATOM   1323 C C   . ASN A 1 334 ? 4.295   -25.780 4.627   1.00 16.64 ? 334 ASN A C   1 
ATOM   1324 O O   . ASN A 1 334 ? 3.628   -25.147 5.445   1.00 17.19 ? 334 ASN A O   1 
ATOM   1325 C CB  . ASN A 1 334 ? 6.505   -26.442 5.537   1.00 17.50 ? 334 ASN A CB  1 
ATOM   1326 C CG  . ASN A 1 334 ? 7.980   -26.527 5.322   1.00 20.00 ? 334 ASN A CG  1 
ATOM   1327 O OD1 . ASN A 1 334 ? 8.462   -27.039 4.298   1.00 22.82 ? 334 ASN A OD1 1 
ATOM   1328 N ND2 . ASN A 1 334 ? 8.738   -26.058 6.293   1.00 21.06 ? 334 ASN A ND2 1 
ATOM   1329 N N   . VAL A 1 335 ? 3.769   -26.689 3.801   1.00 17.36 ? 335 VAL A N   1 
ATOM   1330 C CA  . VAL A 1 335 ? 2.368   -27.075 3.904   1.00 18.48 ? 335 VAL A CA  1 
ATOM   1331 C C   . VAL A 1 335 ? 2.447   -28.549 4.263   1.00 19.42 ? 335 VAL A C   1 
ATOM   1332 O O   . VAL A 1 335 ? 2.992   -29.339 3.489   1.00 19.32 ? 335 VAL A O   1 
ATOM   1333 C CB  . VAL A 1 335 ? 1.565   -26.853 2.589   1.00 20.20 ? 335 VAL A CB  1 
ATOM   1334 C CG1 . VAL A 1 335 ? 0.135   -27.350 2.766   1.00 20.16 ? 335 VAL A CG1 1 
ATOM   1335 C CG2 . VAL A 1 335 ? 1.562   -25.374 2.197   1.00 21.28 ? 335 VAL A CG2 1 
ATOM   1336 N N   . TRP A 1 336 ? 1.944   -28.916 5.442   1.00 19.96 ? 336 TRP A N   1 
ATOM   1337 C CA  . TRP A 1 336 ? 2.026   -30.268 5.951   1.00 20.54 ? 336 TRP A CA  1 
ATOM   1338 C C   . TRP A 1 336 ? 0.700   -31.003 5.761   1.00 22.75 ? 336 TRP A C   1 
ATOM   1339 O O   . TRP A 1 336 ? -0.371  -30.397 5.823   1.00 22.29 ? 336 TRP A O   1 
ATOM   1340 C CB  . TRP A 1 336 ? 2.344   -30.208 7.484   1.00 20.17 ? 336 TRP A CB  1 
ATOM   1341 C CG  . TRP A 1 336 ? 3.599   -29.458 7.829   1.00 19.91 ? 336 TRP A CG  1 
ATOM   1342 C CD1 . TRP A 1 336 ? 3.718   -28.118 8.086   1.00 19.61 ? 336 TRP A CD1 1 
ATOM   1343 C CD2 . TRP A 1 336 ? 4.916   -30.006 7.933   1.00 20.26 ? 336 TRP A CD2 1 
ATOM   1344 N NE1 . TRP A 1 336 ? 5.033   -27.804 8.340   1.00 19.37 ? 336 TRP A NE1 1 
ATOM   1345 C CE2 . TRP A 1 336 ? 5.785   -28.950 8.281   1.00 20.18 ? 336 TRP A CE2 1 
ATOM   1346 C CE3 . TRP A 1 336 ? 5.439   -31.301 7.821   1.00 21.45 ? 336 TRP A CE3 1 
ATOM   1347 C CZ2 . TRP A 1 336 ? 7.157   -29.146 8.471   1.00 21.29 ? 336 TRP A CZ2 1 
ATOM   1348 C CZ3 . TRP A 1 336 ? 6.795   -31.494 8.004   1.00 23.34 ? 336 TRP A CZ3 1 
ATOM   1349 C CH2 . TRP A 1 336 ? 7.643   -30.419 8.292   1.00 22.84 ? 336 TRP A CH2 1 
ATOM   1350 N N   . PRO A 1 337 ? 0.746   -32.336 5.668   1.00 25.35 ? 337 PRO A N   1 
ATOM   1351 C CA  . PRO A 1 337 ? -0.509  -33.108 5.624   1.00 27.33 ? 337 PRO A CA  1 
ATOM   1352 C C   . PRO A 1 337 ? -1.149  -33.199 7.007   1.00 29.67 ? 337 PRO A C   1 
ATOM   1353 O O   . PRO A 1 337 ? -0.517  -32.858 8.020   1.00 29.97 ? 337 PRO A O   1 
ATOM   1354 C CB  . PRO A 1 337 ? -0.046  -34.500 5.180   1.00 27.76 ? 337 PRO A CB  1 
ATOM   1355 C CG  . PRO A 1 337 ? 1.347   -34.624 5.755   1.00 27.92 ? 337 PRO A CG  1 
ATOM   1356 C CD  . PRO A 1 337 ? 1.936   -33.213 5.647   1.00 25.26 ? 337 PRO A CD  1 
ATOM   1357 N N   . SER A 1 338 ? -2.409  -33.639 7.063   1.00 31.26 ? 338 SER A N   1 
ATOM   1358 C CA  . SER A 1 338 ? -3.109  -33.769 8.344   1.00 34.07 ? 338 SER A CA  1 
ATOM   1359 C C   . SER A 1 338 ? -2.685  -35.031 9.126   1.00 36.95 ? 338 SER A C   1 
ATOM   1360 O O   . SER A 1 338 ? -2.837  -35.092 10.341  1.00 37.40 ? 338 SER A O   1 
ATOM   1361 C CB  . SER A 1 338 ? -4.614  -33.782 8.119   1.00 35.53 ? 338 SER A CB  1 
ATOM   1362 O OG  . SER A 1 338 ? -4.978  -34.910 7.342   1.00 37.89 ? 338 SER A OG  1 
ATOM   1363 N N   . ALA A 1 339 ? -2.189  -36.040 8.426   1.00 38.32 ? 339 ALA A N   1 
ATOM   1364 C CA  . ALA A 1 339 ? -1.734  -37.283 9.024   1.00 40.72 ? 339 ALA A CA  1 
ATOM   1365 C C   . ALA A 1 339 ? -0.461  -37.750 8.295   1.00 42.97 ? 339 ALA A C   1 
ATOM   1366 O O   . ALA A 1 339 ? -0.267  -37.411 7.120   1.00 43.19 ? 339 ALA A O   1 
ATOM   1367 C CB  . ALA A 1 339 ? -2.832  -38.341 8.908   1.00 41.09 ? 339 ALA A CB  1 
ATOM   1368 N N   . PRO A 1 340 ? 0.432   -38.505 8.964   1.00 44.65 ? 340 PRO A N   1 
ATOM   1369 C CA  . PRO A 1 340 ? 1.625   -39.002 8.258   1.00 46.10 ? 340 PRO A CA  1 
ATOM   1370 C C   . PRO A 1 340 ? 1.327   -40.201 7.341   1.00 48.00 ? 340 PRO A C   1 
ATOM   1371 O O   . PRO A 1 340 ? 2.097   -40.456 6.419   1.00 48.89 ? 340 PRO A O   1 
ATOM   1372 C CB  . PRO A 1 340 ? 2.578   -39.385 9.394   1.00 46.47 ? 340 PRO A CB  1 
ATOM   1373 C CG  . PRO A 1 340 ? 1.689   -39.720 10.544  1.00 46.63 ? 340 PRO A CG  1 
ATOM   1374 C CD  . PRO A 1 340 ? 0.359   -39.029 10.346  1.00 44.81 ? 340 PRO A CD  1 
ATOM   1375 N N   . GLY A 1 341 ? 0.231   -40.923 7.596   1.00 48.48 ? 341 GLY A N   1 
ATOM   1376 C CA  . GLY A 1 341 ? -0.136  -42.103 6.819   1.00 49.46 ? 341 GLY A CA  1 
ATOM   1377 C C   . GLY A 1 341 ? 0.902   -43.191 6.985   1.00 50.49 ? 341 GLY A C   1 
ATOM   1378 O O   . GLY A 1 341 ? 1.411   -43.389 8.092   1.00 50.64 ? 341 GLY A O   1 
ATOM   1379 N N   . GLU A 1 342 ? 1.265   -43.882 5.887   1.00 50.78 ? 342 GLU A N   1 
ATOM   1380 C CA  . GLU A 1 342 ? 2.318   -44.905 5.961   1.00 51.34 ? 342 GLU A CA  1 
ATOM   1381 C C   . GLU A 1 342 ? 3.742   -44.345 5.745   1.00 51.02 ? 342 GLU A C   1 
ATOM   1382 O O   . GLU A 1 342 ? 4.719   -45.067 5.938   1.00 50.88 ? 342 GLU A O   1 
ATOM   1383 C CB  . GLU A 1 342 ? 2.040   -46.080 5.025   1.00 54.58 ? 342 GLU A CB  1 
ATOM   1384 C CG  . GLU A 1 342 ? 0.875   -46.932 5.498   1.00 61.07 ? 342 GLU A CG  1 
ATOM   1385 C CD  . GLU A 1 342 ? -0.478  -46.552 4.931   1.00 68.80 ? 342 GLU A CD  1 
ATOM   1386 O OE1 . GLU A 1 342 ? -1.486  -47.170 5.346   1.00 70.03 ? 342 GLU A OE1 1 
ATOM   1387 O OE2 . GLU A 1 342 ? -0.534  -45.647 4.067   1.00 71.40 ? 342 GLU A OE2 1 
ATOM   1388 N N   . GLY A 1 343 ? 3.843   -43.075 5.356   1.00 50.48 ? 343 GLY A N   1 
ATOM   1389 C CA  . GLY A 1 343 ? 5.121   -42.396 5.196   1.00 50.28 ? 343 GLY A CA  1 
ATOM   1390 C C   . GLY A 1 343 ? 5.469   -41.609 6.445   1.00 49.86 ? 343 GLY A C   1 
ATOM   1391 O O   . GLY A 1 343 ? 4.827   -41.770 7.494   1.00 50.66 ? 343 GLY A O   1 
ATOM   1392 N N   . GLY A 1 344 ? 6.481   -40.761 6.344   1.00 48.02 ? 344 GLY A N   1 
ATOM   1393 C CA  . GLY A 1 344 ? 6.874   -39.922 7.473   1.00 46.42 ? 344 GLY A CA  1 
ATOM   1394 C C   . GLY A 1 344 ? 6.251   -38.544 7.417   1.00 43.96 ? 344 GLY A C   1 
ATOM   1395 O O   . GLY A 1 344 ? 5.527   -38.217 6.469   1.00 44.22 ? 344 GLY A O   1 
ATOM   1396 N N   . TRP A 1 345 ? 6.519   -37.718 8.437   1.00 41.19 ? 345 TRP A N   1 
ATOM   1397 C CA  . TRP A 1 345 ? 6.013   -36.350 8.465   1.00 39.15 ? 345 TRP A CA  1 
ATOM   1398 C C   . TRP A 1 345 ? 6.845   -35.527 7.500   1.00 37.64 ? 345 TRP A C   1 
ATOM   1399 O O   . TRP A 1 345 ? 7.923   -35.052 7.858   1.00 38.21 ? 345 TRP A O   1 
ATOM   1400 C CB  . TRP A 1 345 ? 6.109   -35.767 9.875   1.00 38.24 ? 345 TRP A CB  1 
ATOM   1401 C CG  . TRP A 1 345 ? 4.997   -36.197 10.777  1.00 37.45 ? 345 TRP A CG  1 
ATOM   1402 C CD1 . TRP A 1 345 ? 5.080   -37.060 11.831  1.00 37.90 ? 345 TRP A CD1 1 
ATOM   1403 C CD2 . TRP A 1 345 ? 3.631   -35.765 10.717  1.00 36.86 ? 345 TRP A CD2 1 
ATOM   1404 N NE1 . TRP A 1 345 ? 3.845   -37.204 12.420  1.00 37.95 ? 345 TRP A NE1 1 
ATOM   1405 C CE2 . TRP A 1 345 ? 2.943   -36.401 11.769  1.00 37.44 ? 345 TRP A CE2 1 
ATOM   1406 C CE3 . TRP A 1 345 ? 2.919   -34.916 9.864   1.00 37.00 ? 345 TRP A CE3 1 
ATOM   1407 C CZ2 . TRP A 1 345 ? 1.585   -36.197 12.002  1.00 37.63 ? 345 TRP A CZ2 1 
ATOM   1408 C CZ3 . TRP A 1 345 ? 1.571   -34.718 10.098  1.00 37.49 ? 345 TRP A CZ3 1 
ATOM   1409 C CH2 . TRP A 1 345 ? 0.915   -35.369 11.143  1.00 37.47 ? 345 TRP A CH2 1 
ATOM   1410 N N   . VAL A 1 346 ? 6.404   -35.451 6.249   1.00 35.21 ? 346 VAL A N   1 
ATOM   1411 C CA  . VAL A 1 346 ? 7.125   -34.713 5.222   1.00 33.85 ? 346 VAL A CA  1 
ATOM   1412 C C   . VAL A 1 346 ? 6.175   -33.672 4.594   1.00 30.85 ? 346 VAL A C   1 
ATOM   1413 O O   . VAL A 1 346 ? 4.995   -33.959 4.392   1.00 30.13 ? 346 VAL A O   1 
ATOM   1414 C CB  . VAL A 1 346 ? 7.701   -35.679 4.151   1.00 36.02 ? 346 VAL A CB  1 
ATOM   1415 C CG1 . VAL A 1 346 ? 8.790   -36.582 4.742   1.00 36.93 ? 346 VAL A CG1 1 
ATOM   1416 C CG2 . VAL A 1 346 ? 6.595   -36.521 3.523   1.00 37.28 ? 346 VAL A CG2 1 
ATOM   1417 N N   . PRO A 1 347 ? 6.651   -32.445 4.320   1.00 28.85 ? 347 PRO A N   1 
ATOM   1418 C CA  . PRO A 1 347 ? 5.756   -31.438 3.736   1.00 28.17 ? 347 PRO A CA  1 
ATOM   1419 C C   . PRO A 1 347 ? 5.230   -31.824 2.360   1.00 28.03 ? 347 PRO A C   1 
ATOM   1420 O O   . PRO A 1 347 ? 5.968   -32.385 1.555   1.00 28.45 ? 347 PRO A O   1 
ATOM   1421 C CB  . PRO A 1 347 ? 6.649   -30.184 3.633   1.00 28.98 ? 347 PRO A CB  1 
ATOM   1422 C CG  . PRO A 1 347 ? 7.786   -30.428 4.565   1.00 29.63 ? 347 PRO A CG  1 
ATOM   1423 C CD  . PRO A 1 347 ? 8.010   -31.912 4.526   1.00 28.04 ? 347 PRO A CD  1 
ATOM   1424 N N   . LEU A 1 348 ? 3.945   -31.516 2.095   1.00 26.92 ? 348 LEU A N   1 
ATOM   1425 C CA  . LEU A 1 348 ? 3.304   -31.660 0.784   1.00 26.85 ? 348 LEU A CA  1 
ATOM   1426 C C   . LEU A 1 348 ? 3.840   -30.548 -0.164  1.00 25.65 ? 348 LEU A C   1 
ATOM   1427 O O   . LEU A 1 348 ? 3.877   -30.722 -1.383  1.00 25.30 ? 348 LEU A O   1 
ATOM   1428 C CB  . LEU A 1 348 ? 1.794   -31.452 0.952   1.00 27.99 ? 348 LEU A CB  1 
ATOM   1429 C CG  . LEU A 1 348 ? 1.035   -32.590 1.605   1.00 30.65 ? 348 LEU A CG  1 
ATOM   1430 C CD1 . LEU A 1 348 ? -0.362  -32.147 1.974   1.00 31.64 ? 348 LEU A CD1 1 
ATOM   1431 C CD2 . LEU A 1 348 ? 0.985   -33.823 0.674   1.00 32.13 ? 348 LEU A CD2 1 
ATOM   1432 N N   . GLN A 1 349 ? 4.144   -29.363 0.391   1.00 23.70 ? 349 GLN A N   1 
ATOM   1433 C CA  . GLN A 1 349 ? 4.689   -28.249 -0.381  1.00 23.37 ? 349 GLN A CA  1 
ATOM   1434 C C   . GLN A 1 349 ? 5.713   -27.500 0.464   1.00 22.47 ? 349 GLN A C   1 
ATOM   1435 O O   . GLN A 1 349 ? 5.559   -27.408 1.680   1.00 21.55 ? 349 GLN A O   1 
ATOM   1436 C CB  . GLN A 1 349 ? 3.584   -27.243 -0.771  1.00 24.81 ? 349 GLN A CB  1 
ATOM   1437 C CG  . GLN A 1 349 ? 2.479   -27.786 -1.688  1.00 26.80 ? 349 GLN A CG  1 
ATOM   1438 C CD  . GLN A 1 349 ? 2.883   -27.999 -3.134  1.00 28.58 ? 349 GLN A CD  1 
ATOM   1439 O OE1 . GLN A 1 349 ? 4.023   -27.757 -3.552  1.00 27.53 ? 349 GLN A OE1 1 
ATOM   1440 N NE2 . GLN A 1 349 ? 1.943   -28.481 -3.923  1.00 29.01 ? 349 GLN A NE2 1 
ATOM   1441 N N   . THR A 1 350 ? 6.764   -26.963 -0.176  1.00 22.12 ? 350 THR A N   1 
ATOM   1442 C CA  . THR A 1 350 ? 7.731   -26.098 0.500   1.00 21.51 ? 350 THR A CA  1 
ATOM   1443 C C   . THR A 1 350 ? 7.953   -24.938 -0.448  1.00 21.76 ? 350 THR A C   1 
ATOM   1444 O O   . THR A 1 350 ? 8.486   -25.126 -1.550  1.00 23.28 ? 350 THR A O   1 
ATOM   1445 C CB  . THR A 1 350 ? 9.042   -26.793 0.843   1.00 22.87 ? 350 THR A CB  1 
ATOM   1446 O OG1 . THR A 1 350 ? 8.788   -27.864 1.761   1.00 23.39 ? 350 THR A OG1 1 
ATOM   1447 C CG2 . THR A 1 350 ? 10.045  -25.829 1.448   1.00 23.10 ? 350 THR A CG2 1 
ATOM   1448 N N   . PHE A 1 351 ? 7.518   -23.756 -0.039  1.00 20.09 ? 351 PHE A N   1 
ATOM   1449 C CA  . PHE A 1 351 ? 7.592   -22.543 -0.836  1.00 19.32 ? 351 PHE A CA  1 
ATOM   1450 C C   . PHE A 1 351 ? 8.776   -21.735 -0.357  1.00 19.60 ? 351 PHE A C   1 
ATOM   1451 O O   . PHE A 1 351 ? 8.815   -21.299 0.811   1.00 19.79 ? 351 PHE A O   1 
ATOM   1452 C CB  . PHE A 1 351 ? 6.279   -21.734 -0.716  1.00 19.05 ? 351 PHE A CB  1 
ATOM   1453 C CG  . PHE A 1 351 ? 5.019   -22.462 -1.117  1.00 20.18 ? 351 PHE A CG  1 
ATOM   1454 C CD1 . PHE A 1 351 ? 4.958   -23.175 -2.297  1.00 20.34 ? 351 PHE A CD1 1 
ATOM   1455 C CD2 . PHE A 1 351 ? 3.893   -22.434 -0.308  1.00 20.94 ? 351 PHE A CD2 1 
ATOM   1456 C CE1 . PHE A 1 351 ? 3.784   -23.802 -2.689  1.00 21.28 ? 351 PHE A CE1 1 
ATOM   1457 C CE2 . PHE A 1 351 ? 2.722   -23.077 -0.695  1.00 21.48 ? 351 PHE A CE2 1 
ATOM   1458 C CZ  . PHE A 1 351 ? 2.686   -23.791 -1.862  1.00 21.28 ? 351 PHE A CZ  1 
ATOM   1459 N N   . THR A 1 352 ? 9.747   -21.537 -1.236  1.00 20.18 ? 352 THR A N   1 
ATOM   1460 C CA  . THR A 1 352 ? 10.951  -20.787 -0.907  1.00 20.96 ? 352 THR A CA  1 
ATOM   1461 C C   . THR A 1 352 ? 10.944  -19.349 -1.484  1.00 20.77 ? 352 THR A C   1 
ATOM   1462 O O   . THR A 1 352 ? 11.947  -18.660 -1.379  1.00 21.72 ? 352 THR A O   1 
ATOM   1463 C CB  . THR A 1 352 ? 12.177  -21.554 -1.432  1.00 23.64 ? 352 THR A CB  1 
ATOM   1464 O OG1 . THR A 1 352 ? 12.092  -21.621 -2.873  1.00 25.17 ? 352 THR A OG1 1 
ATOM   1465 C CG2 . THR A 1 352 ? 12.247  -22.978 -0.886  1.00 25.49 ? 352 THR A CG2 1 
ATOM   1466 N N   . GLN A 1 353 ? 9.844   -18.900 -2.094  1.00 19.05 ? 353 GLN A N   1 
ATOM   1467 C CA  . GLN A 1 353 ? 9.839   -17.629 -2.840  1.00 19.00 ? 353 GLN A CA  1 
ATOM   1468 C C   . GLN A 1 353 ? 9.862   -16.380 -1.976  1.00 19.95 ? 353 GLN A C   1 
ATOM   1469 O O   . GLN A 1 353 ? 10.285  -15.336 -2.498  1.00 21.87 ? 353 GLN A O   1 
ATOM   1470 C CB  . GLN A 1 353 ? 8.671   -17.580 -3.850  1.00 18.98 ? 353 GLN A CB  1 
ATOM   1471 C CG  . GLN A 1 353 ? 8.742   -18.702 -4.897  1.00 19.24 ? 353 GLN A CG  1 
ATOM   1472 C CD  . GLN A 1 353 ? 8.013   -19.977 -4.485  1.00 21.44 ? 353 GLN A CD  1 
ATOM   1473 O OE1 . GLN A 1 353 ? 7.873   -20.319 -3.303  1.00 20.49 ? 353 GLN A OE1 1 
ATOM   1474 N NE2 . GLN A 1 353 ? 7.559   -20.742 -5.458  1.00 22.79 ? 353 GLN A NE2 1 
ATOM   1475 N N   . HIS A 1 354 ? 9.485   -16.465 -0.682  1.00 19.73 ? 354 HIS A N   1 
ATOM   1476 C CA  . HIS A 1 354 ? 9.583   -15.279 0.170   1.00 19.97 ? 354 HIS A CA  1 
ATOM   1477 C C   . HIS A 1 354 ? 11.076  -15.055 0.541   1.00 21.84 ? 354 HIS A C   1 
ATOM   1478 O O   . HIS A 1 354 ? 11.776  -15.992 0.881   1.00 24.21 ? 354 HIS A O   1 
ATOM   1479 C CB  . HIS A 1 354 ? 8.743   -15.421 1.446   1.00 18.84 ? 354 HIS A CB  1 
ATOM   1480 C CG  . HIS A 1 354 ? 7.257   -15.227 1.248   1.00 17.60 ? 354 HIS A CG  1 
ATOM   1481 N ND1 . HIS A 1 354 ? 6.719   -13.960 1.047   1.00 19.21 ? 354 HIS A ND1 1 
ATOM   1482 C CD2 . HIS A 1 354 ? 6.246   -16.121 1.321   1.00 18.00 ? 354 HIS A CD2 1 
ATOM   1483 C CE1 . HIS A 1 354 ? 5.396   -14.133 0.998   1.00 18.76 ? 354 HIS A CE1 1 
ATOM   1484 N NE2 . HIS A 1 354 ? 5.068   -15.417 1.140   1.00 18.08 ? 354 HIS A NE2 1 
ATOM   1485 N N   A GLN A 1 355 ? 11.544  -13.823 0.449   0.53 21.52 ? 355 GLN A N   1 
ATOM   1486 N N   B GLN A 1 355 ? 11.561  -13.818 0.428   0.47 21.62 ? 355 GLN A N   1 
ATOM   1487 C CA  A GLN A 1 355 ? 12.938  -13.474 0.732   0.53 22.29 ? 355 GLN A CA  1 
ATOM   1488 C CA  B GLN A 1 355 ? 12.954  -13.489 0.755   0.47 22.35 ? 355 GLN A CA  1 
ATOM   1489 C C   A GLN A 1 355 ? 13.012  -12.790 2.105   0.53 22.80 ? 355 GLN A C   1 
ATOM   1490 C C   B GLN A 1 355 ? 12.976  -12.768 2.103   0.47 22.78 ? 355 GLN A C   1 
ATOM   1491 O O   A GLN A 1 355 ? 13.623  -11.737 2.246   0.53 24.27 ? 355 GLN A O   1 
ATOM   1492 O O   B GLN A 1 355 ? 13.483  -11.660 2.224   0.47 24.01 ? 355 GLN A O   1 
ATOM   1493 C CB  A GLN A 1 355 ? 13.453  -12.530 -0.374  0.53 23.95 ? 355 GLN A CB  1 
ATOM   1494 C CB  B GLN A 1 355 ? 13.606  -12.624 -0.343  0.47 24.09 ? 355 GLN A CB  1 
ATOM   1495 C CG  A GLN A 1 355 ? 13.290  -13.098 -1.777  0.53 28.79 ? 355 GLN A CG  1 
ATOM   1496 C CG  B GLN A 1 355 ? 15.133  -12.732 -0.321  0.47 28.57 ? 355 GLN A CG  1 
ATOM   1497 C CD  A GLN A 1 355 ? 14.182  -14.296 -1.991  0.53 33.46 ? 355 GLN A CD  1 
ATOM   1498 C CD  B GLN A 1 355 ? 15.844  -11.543 -0.924  0.47 33.27 ? 355 GLN A CD  1 
ATOM   1499 O OE1 A GLN A 1 355 ? 15.409  -14.177 -2.071  0.53 35.97 ? 355 GLN A OE1 1 
ATOM   1500 O OE1 B GLN A 1 355 ? 16.284  -11.575 -2.076  0.47 35.50 ? 355 GLN A OE1 1 
ATOM   1501 N NE2 A GLN A 1 355 ? 13.583  -15.479 -2.101  0.53 32.82 ? 355 GLN A NE2 1 
ATOM   1502 N NE2 B GLN A 1 355 ? 15.980  -10.466 -0.151  0.47 32.40 ? 355 GLN A NE2 1 
ATOM   1503 N N   . GLY A 1 356 ? 12.348  -13.377 3.087   1.00 22.40 ? 356 GLY A N   1 
ATOM   1504 C CA  . GLY A 1 356 ? 12.271  -12.831 4.445   1.00 21.44 ? 356 GLY A CA  1 
ATOM   1505 C C   . GLY A 1 356 ? 11.410  -13.710 5.346   1.00 21.72 ? 356 GLY A C   1 
ATOM   1506 O O   . GLY A 1 356 ? 10.765  -14.658 4.871   1.00 21.72 ? 356 GLY A O   1 
ATOM   1507 N N   . ALA A 1 357 ? 11.416  -13.437 6.665   1.00 21.07 ? 357 ALA A N   1 
ATOM   1508 C CA  . ALA A 1 357 ? 10.643  -14.261 7.604   1.00 20.33 ? 357 ALA A CA  1 
ATOM   1509 C C   . ALA A 1 357 ? 9.154   -14.313 7.245   1.00 20.22 ? 357 ALA A C   1 
ATOM   1510 O O   . ALA A 1 357 ? 8.615   -13.298 6.833   1.00 20.42 ? 357 ALA A O   1 
ATOM   1511 C CB  . ALA A 1 357 ? 10.796  -13.722 9.019   1.00 21.08 ? 357 ALA A CB  1 
ATOM   1512 N N   . VAL A 1 358 ? 8.504   -15.470 7.416   1.00 18.67 ? 358 VAL A N   1 
ATOM   1513 C CA  . VAL A 1 358 ? 7.084   -15.586 7.088   1.00 19.25 ? 358 VAL A CA  1 
ATOM   1514 C C   . VAL A 1 358 ? 6.270   -15.765 8.356   1.00 19.96 ? 358 VAL A C   1 
ATOM   1515 O O   . VAL A 1 358 ? 6.133   -16.882 8.858   1.00 21.09 ? 358 VAL A O   1 
ATOM   1516 C CB  . VAL A 1 358 ? 6.801   -16.707 6.047   1.00 20.98 ? 358 VAL A CB  1 
ATOM   1517 C CG1 . VAL A 1 358 ? 5.327   -16.705 5.651   1.00 21.62 ? 358 VAL A CG1 1 
ATOM   1518 C CG2 . VAL A 1 358 ? 7.693   -16.553 4.815   1.00 21.45 ? 358 VAL A CG2 1 
ATOM   1519 N N   . LYS A 1 359 ? 5.770   -14.662 8.906   1.00 18.73 ? 359 LYS A N   1 
ATOM   1520 C CA  . LYS A 1 359 ? 4.937   -14.737 10.115  1.00 18.35 ? 359 LYS A CA  1 
ATOM   1521 C C   . LYS A 1 359 ? 3.447   -14.809 9.743   1.00 17.80 ? 359 LYS A C   1 
ATOM   1522 O O   . LYS A 1 359 ? 2.631   -15.413 10.443  1.00 19.15 ? 359 LYS A O   1 
ATOM   1523 C CB  . LYS A 1 359 ? 5.148   -13.464 10.965  1.00 19.46 ? 359 LYS A CB  1 
ATOM   1524 C CG  . LYS A 1 359 ? 4.457   -13.557 12.304  1.00 23.17 ? 359 LYS A CG  1 
ATOM   1525 C CD  . LYS A 1 359 ? 4.540   -12.253 13.075  1.00 25.42 ? 359 LYS A CD  1 
ATOM   1526 C CE  . LYS A 1 359 ? 3.696   -12.346 14.307  1.00 25.48 ? 359 LYS A CE  1 
ATOM   1527 N NZ  . LYS A 1 359 ? 3.992   -11.234 15.242  1.00 25.45 ? 359 LYS A NZ  1 
ATOM   1528 N N   . ALA A 1 360 ? 3.100   -14.216 8.606   1.00 16.63 ? 360 ALA A N   1 
ATOM   1529 C CA  . ALA A 1 360 ? 1.714   -14.095 8.180   1.00 16.20 ? 360 ALA A CA  1 
ATOM   1530 C C   . ALA A 1 360 ? 1.305   -15.293 7.398   1.00 16.76 ? 360 ALA A C   1 
ATOM   1531 O O   . ALA A 1 360 ? 1.852   -15.565 6.336   1.00 16.53 ? 360 ALA A O   1 
ATOM   1532 C CB  . ALA A 1 360 ? 1.556   -12.829 7.346   1.00 17.39 ? 360 ALA A CB  1 
ATOM   1533 N N   . VAL A 1 361 ? 0.361   -16.060 7.950   1.00 16.91 ? 361 VAL A N   1 
ATOM   1534 C CA  . VAL A 1 361 ? -0.101  -17.322 7.335   1.00 16.60 ? 361 VAL A CA  1 
ATOM   1535 C C   . VAL A 1 361 ? -1.620  -17.374 7.592   1.00 16.60 ? 361 VAL A C   1 
ATOM   1536 O O   . VAL A 1 361 ? -2.036  -17.327 8.756   1.00 17.16 ? 361 VAL A O   1 
ATOM   1537 C CB  . VAL A 1 361 ? 0.596   -18.539 8.016   1.00 18.41 ? 361 VAL A CB  1 
ATOM   1538 C CG1 . VAL A 1 361 ? 0.112   -19.848 7.431   1.00 19.85 ? 361 VAL A CG1 1 
ATOM   1539 C CG2 . VAL A 1 361 ? 2.128   -18.460 7.897   1.00 19.05 ? 361 VAL A CG2 1 
ATOM   1540 N N   . ALA A 1 362 ? -2.419  -17.462 6.544   1.00 15.46 ? 362 ALA A N   1 
ATOM   1541 C CA  . ALA A 1 362 ? -3.898  -17.506 6.725   1.00 15.46 ? 362 ALA A CA  1 
ATOM   1542 C C   . ALA A 1 362 ? -4.585  -18.189 5.601   1.00 16.58 ? 362 ALA A C   1 
ATOM   1543 O O   . ALA A 1 362 ? -4.303  -17.897 4.450   1.00 16.91 ? 362 ALA A O   1 
ATOM   1544 C CB  . ALA A 1 362 ? -4.450  -16.087 6.866   1.00 16.35 ? 362 ALA A CB  1 
ATOM   1545 N N   . TRP A 1 363 ? -5.516  -19.102 5.914   1.00 17.27 ? 363 TRP A N   1 
ATOM   1546 C CA  . TRP A 1 363 ? -6.211  -19.864 4.883   1.00 18.34 ? 363 TRP A CA  1 
ATOM   1547 C C   . TRP A 1 363 ? -7.471  -19.187 4.431   1.00 19.81 ? 363 TRP A C   1 
ATOM   1548 O O   . TRP A 1 363 ? -8.160  -18.576 5.252   1.00 20.48 ? 363 TRP A O   1 
ATOM   1549 C CB  . TRP A 1 363 ? -6.595  -21.244 5.427   1.00 18.64 ? 363 TRP A CB  1 
ATOM   1550 C CG  . TRP A 1 363 ? -5.412  -22.110 5.724   1.00 17.73 ? 363 TRP A CG  1 
ATOM   1551 C CD1 . TRP A 1 363 ? -4.726  -22.197 6.898   1.00 18.84 ? 363 TRP A CD1 1 
ATOM   1552 C CD2 . TRP A 1 363 ? -4.781  -23.022 4.817   1.00 17.77 ? 363 TRP A CD2 1 
ATOM   1553 N NE1 . TRP A 1 363 ? -3.701  -23.113 6.781   1.00 19.05 ? 363 TRP A NE1 1 
ATOM   1554 C CE2 . TRP A 1 363 ? -3.711  -23.629 5.507   1.00 18.17 ? 363 TRP A CE2 1 
ATOM   1555 C CE3 . TRP A 1 363 ? -5.040  -23.405 3.490   1.00 17.78 ? 363 TRP A CE3 1 
ATOM   1556 C CZ2 . TRP A 1 363 ? -2.916  -24.612 4.926   1.00 18.94 ? 363 TRP A CZ2 1 
ATOM   1557 C CZ3 . TRP A 1 363 ? -4.221  -24.355 2.902   1.00 18.88 ? 363 TRP A CZ3 1 
ATOM   1558 C CH2 . TRP A 1 363 ? -3.154  -24.917 3.608   1.00 19.39 ? 363 TRP A CH2 1 
ATOM   1559 N N   . CYS A 1 364 ? -7.834  -19.385 3.144   1.00 19.14 ? 364 CYS A N   1 
ATOM   1560 C CA  . CYS A 1 364 ? -9.059  -18.815 2.642   1.00 19.62 ? 364 CYS A CA  1 
ATOM   1561 C C   . CYS A 1 364 ? -10.235 -19.577 3.255   1.00 20.99 ? 364 CYS A C   1 
ATOM   1562 O O   . CYS A 1 364 ? -10.343 -20.787 3.088   1.00 21.02 ? 364 CYS A O   1 
ATOM   1563 C CB  . CYS A 1 364 ? -9.102  -18.865 1.123   1.00 19.72 ? 364 CYS A CB  1 
ATOM   1564 S SG  . CYS A 1 364 ? -10.664 -18.260 0.447   1.00 24.72 ? 364 CYS A SG  1 
ATOM   1565 N N   . PRO A 1 365 ? -11.114 -18.897 4.004   1.00 22.42 ? 365 PRO A N   1 
ATOM   1566 C CA  . PRO A 1 365 ? -12.239 -19.613 4.661   1.00 24.36 ? 365 PRO A CA  1 
ATOM   1567 C C   . PRO A 1 365 ? -13.228 -20.282 3.723   1.00 26.47 ? 365 PRO A C   1 
ATOM   1568 O O   . PRO A 1 365 ? -13.988 -21.159 4.164   1.00 27.12 ? 365 PRO A O   1 
ATOM   1569 C CB  . PRO A 1 365 ? -12.957 -18.509 5.468   1.00 24.52 ? 365 PRO A CB  1 
ATOM   1570 C CG  . PRO A 1 365 ? -11.994 -17.400 5.579   1.00 24.30 ? 365 PRO A CG  1 
ATOM   1571 C CD  . PRO A 1 365 ? -11.119 -17.460 4.322   1.00 22.18 ? 365 PRO A CD  1 
ATOM   1572 N N   . TRP A 1 366 ? -13.300 -19.833 2.462   1.00 26.84 ? 366 TRP A N   1 
ATOM   1573 C CA  . TRP A 1 366 ? -14.259 -20.426 1.531   1.00 29.02 ? 366 TRP A CA  1 
ATOM   1574 C C   . TRP A 1 366 ? -13.611 -21.270 0.423   1.00 30.43 ? 366 TRP A C   1 
ATOM   1575 O O   . TRP A 1 366 ? -14.302 -21.681 -0.510  1.00 31.74 ? 366 TRP A O   1 
ATOM   1576 C CB  . TRP A 1 366 ? -15.186 -19.361 0.944   1.00 29.97 ? 366 TRP A CB  1 
ATOM   1577 C CG  . TRP A 1 366 ? -14.488 -18.377 0.064   1.00 30.92 ? 366 TRP A CG  1 
ATOM   1578 C CD1 . TRP A 1 366 ? -14.406 -18.406 -1.301  1.00 31.96 ? 366 TRP A CD1 1 
ATOM   1579 C CD2 . TRP A 1 366 ? -13.871 -17.160 0.479   1.00 30.56 ? 366 TRP A CD2 1 
ATOM   1580 N NE1 . TRP A 1 366 ? -13.711 -17.314 -1.751  1.00 32.28 ? 366 TRP A NE1 1 
ATOM   1581 C CE2 . TRP A 1 366 ? -13.398 -16.514 -0.679  1.00 31.43 ? 366 TRP A CE2 1 
ATOM   1582 C CE3 . TRP A 1 366 ? -13.718 -16.522 1.717   1.00 30.55 ? 366 TRP A CE3 1 
ATOM   1583 C CZ2 . TRP A 1 366 ? -12.714 -15.309 -0.626  1.00 31.57 ? 366 TRP A CZ2 1 
ATOM   1584 C CZ3 . TRP A 1 366 ? -13.024 -15.334 1.768   1.00 31.25 ? 366 TRP A CZ3 1 
ATOM   1585 C CH2 . TRP A 1 366 ? -12.538 -14.738 0.607   1.00 31.63 ? 366 TRP A CH2 1 
ATOM   1586 N N   . GLN A 1 367 ? -12.282 -21.490 0.485   1.00 29.67 ? 367 GLN A N   1 
ATOM   1587 C CA  . GLN A 1 367 ? -11.603 -22.302 -0.529  1.00 30.62 ? 367 GLN A CA  1 
ATOM   1588 C C   . GLN A 1 367 ? -10.547 -23.103 0.168   1.00 30.63 ? 367 GLN A C   1 
ATOM   1589 O O   . GLN A 1 367 ? -9.498  -22.568 0.516   1.00 29.60 ? 367 GLN A O   1 
ATOM   1590 C CB  . GLN A 1 367 ? -10.923 -21.436 -1.566  1.00 32.94 ? 367 GLN A CB  1 
ATOM   1591 C CG  . GLN A 1 367 ? -11.859 -20.695 -2.461  1.00 37.82 ? 367 GLN A CG  1 
ATOM   1592 C CD  . GLN A 1 367 ? -11.073 -20.071 -3.554  1.00 43.59 ? 367 GLN A CD  1 
ATOM   1593 O OE1 . GLN A 1 367 ? -10.910 -20.651 -4.623  1.00 46.29 ? 367 GLN A OE1 1 
ATOM   1594 N NE2 . GLN A 1 367 ? -10.531 -18.893 -3.293  1.00 44.60 ? 367 GLN A NE2 1 
ATOM   1595 N N   . SER A 1 368 ? -10.806 -24.397 0.293   1.00 30.20 ? 368 SER A N   1 
ATOM   1596 C CA  . SER A 1 368 ? -10.017 -25.389 0.992   1.00 30.30 ? 368 SER A CA  1 
ATOM   1597 C C   . SER A 1 368 ? -8.506  -25.278 0.803   1.00 27.97 ? 368 SER A C   1 
ATOM   1598 O O   . SER A 1 368 ? -7.763  -25.287 1.780   1.00 29.02 ? 368 SER A O   1 
ATOM   1599 C CB  . SER A 1 368 ? -10.503 -26.788 0.599   1.00 34.15 ? 368 SER A CB  1 
ATOM   1600 O OG  . SER A 1 368 ? -9.660  -27.835 1.064   1.00 39.79 ? 368 SER A OG  1 
ATOM   1601 N N   . ASN A 1 369 ? -8.062  -25.191 -0.442  1.00 25.35 ? 369 ASN A N   1 
ATOM   1602 C CA  . ASN A 1 369 ? -6.645  -25.240 -0.752  1.00 24.19 ? 369 ASN A CA  1 
ATOM   1603 C C   . ASN A 1 369 ? -5.985  -23.901 -0.981  1.00 22.56 ? 369 ASN A C   1 
ATOM   1604 O O   . ASN A 1 369 ? -4.828  -23.897 -1.392  1.00 22.40 ? 369 ASN A O   1 
ATOM   1605 C CB  . ASN A 1 369 ? -6.457  -26.101 -1.991  1.00 27.54 ? 369 ASN A CB  1 
ATOM   1606 C CG  . ASN A 1 369 ? -6.964  -27.497 -1.794  1.00 33.58 ? 369 ASN A CG  1 
ATOM   1607 O OD1 . ASN A 1 369 ? -6.872  -28.061 -0.699  1.00 35.53 ? 369 ASN A OD1 1 
ATOM   1608 N ND2 . ASN A 1 369 ? -7.518  -28.081 -2.842  1.00 36.55 ? 369 ASN A ND2 1 
ATOM   1609 N N   . VAL A 1 370 ? -6.655  -22.776 -0.685  1.00 20.00 ? 370 VAL A N   1 
ATOM   1610 C CA  . VAL A 1 370 ? -6.052  -21.474 -0.950  1.00 18.55 ? 370 VAL A CA  1 
ATOM   1611 C C   . VAL A 1 370 ? -5.434  -20.874 0.310   1.00 17.45 ? 370 VAL A C   1 
ATOM   1612 O O   . VAL A 1 370 ? -6.089  -20.814 1.349   1.00 17.39 ? 370 VAL A O   1 
ATOM   1613 C CB  . VAL A 1 370 ? -7.051  -20.519 -1.641  1.00 19.35 ? 370 VAL A CB  1 
ATOM   1614 C CG1 . VAL A 1 370 ? -6.456  -19.122 -1.785  1.00 18.49 ? 370 VAL A CG1 1 
ATOM   1615 C CG2 . VAL A 1 370 ? -7.491  -21.075 -3.014  1.00 20.56 ? 370 VAL A CG2 1 
ATOM   1616 N N   . LEU A 1 371 ? -4.150  -20.515 0.241   1.00 16.92 ? 371 LEU A N   1 
ATOM   1617 C CA  . LEU A 1 371 ? -3.415  -19.996 1.385   1.00 16.80 ? 371 LEU A CA  1 
ATOM   1618 C C   . LEU A 1 371 ? -2.815  -18.630 1.080   1.00 16.73 ? 371 LEU A C   1 
ATOM   1619 O O   . LEU A 1 371 ? -2.315  -18.443 -0.020  1.00 17.12 ? 371 LEU A O   1 
ATOM   1620 C CB  . LEU A 1 371 ? -2.260  -20.972 1.655   1.00 16.17 ? 371 LEU A CB  1 
ATOM   1621 C CG  . LEU A 1 371 ? -1.278  -20.591 2.748   1.00 17.02 ? 371 LEU A CG  1 
ATOM   1622 C CD1 . LEU A 1 371 ? -1.970  -20.533 4.097   1.00 16.83 ? 371 LEU A CD1 1 
ATOM   1623 C CD2 . LEU A 1 371 ? -0.109  -21.561 2.797   1.00 16.76 ? 371 LEU A CD2 1 
ATOM   1624 N N   . ALA A 1 372 ? -2.807  -17.691 2.051   1.00 15.62 ? 372 ALA A N   1 
ATOM   1625 C CA  . ALA A 1 372 ? -2.114  -16.399 1.911   1.00 15.59 ? 372 ALA A CA  1 
ATOM   1626 C C   . ALA A 1 372 ? -0.947  -16.386 2.898   1.00 16.28 ? 372 ALA A C   1 
ATOM   1627 O O   . ALA A 1 372 ? -1.076  -16.840 4.042   1.00 16.94 ? 372 ALA A O   1 
ATOM   1628 C CB  . ALA A 1 372 ? -3.051  -15.234 2.256   1.00 15.62 ? 372 ALA A CB  1 
ATOM   1629 N N   . THR A 1 373 ? 0.206   -15.917 2.453   1.00 16.02 ? 373 THR A N   1 
ATOM   1630 C CA  . THR A 1 373 ? 1.393   -15.771 3.289   1.00 16.78 ? 373 THR A CA  1 
ATOM   1631 C C   . THR A 1 373 ? 1.977   -14.375 3.075   1.00 17.40 ? 373 THR A C   1 
ATOM   1632 O O   . THR A 1 373 ? 1.754   -13.774 2.027   1.00 18.29 ? 373 THR A O   1 
ATOM   1633 C CB  . THR A 1 373 ? 2.436   -16.872 3.007   1.00 17.77 ? 373 THR A CB  1 
ATOM   1634 O OG1 . THR A 1 373 ? 2.839   -16.767 1.637   1.00 18.57 ? 373 THR A OG1 1 
ATOM   1635 C CG2 . THR A 1 373 ? 1.872   -18.282 3.289   1.00 18.24 ? 373 THR A CG2 1 
ATOM   1636 N N   . GLY A 1 374 ? 2.688   -13.861 4.079   1.00 17.22 ? 374 GLY A N   1 
ATOM   1637 C CA  . GLY A 1 374 ? 3.331   -12.557 3.961   1.00 16.69 ? 374 GLY A CA  1 
ATOM   1638 C C   . GLY A 1 374 ? 4.731   -12.574 4.537   1.00 17.18 ? 374 GLY A C   1 
ATOM   1639 O O   . GLY A 1 374 ? 4.940   -13.130 5.616   1.00 18.05 ? 374 GLY A O   1 
ATOM   1640 N N   . GLY A 1 375 ? 5.656   -11.868 3.894   1.00 17.58 ? 375 GLY A N   1 
ATOM   1641 C CA  . GLY A 1 375 ? 7.037   -11.858 4.342   1.00 18.82 ? 375 GLY A CA  1 
ATOM   1642 C C   . GLY A 1 375 ? 7.453   -10.600 5.077   1.00 19.88 ? 375 GLY A C   1 
ATOM   1643 O O   . GLY A 1 375 ? 6.787   -9.570  4.997   1.00 19.81 ? 375 GLY A O   1 
ATOM   1644 N N   . GLY A 1 376 ? 8.585   -10.681 5.744   1.00 19.79 ? 376 GLY A N   1 
ATOM   1645 C CA  . GLY A 1 376 ? 9.138   -9.581  6.516   1.00 21.54 ? 376 GLY A CA  1 
ATOM   1646 C C   . GLY A 1 376 ? 9.689   -8.437  5.687   1.00 22.15 ? 376 GLY A C   1 
ATOM   1647 O O   . GLY A 1 376 ? 9.438   -8.346  4.481   1.00 21.93 ? 376 GLY A O   1 
ATOM   1648 N N   . THR A 1 377 ? 10.445  -7.557  6.334   1.00 21.89 ? 377 THR A N   1 
ATOM   1649 C CA  . THR A 1 377 ? 10.980  -6.331  5.753   1.00 22.91 ? 377 THR A CA  1 
ATOM   1650 C C   . THR A 1 377 ? 11.766  -6.515  4.473   1.00 22.79 ? 377 THR A C   1 
ATOM   1651 O O   . THR A 1 377 ? 11.654  -5.685  3.558   1.00 23.80 ? 377 THR A O   1 
ATOM   1652 C CB  . THR A 1 377 ? 11.820  -5.573  6.774   1.00 25.58 ? 377 THR A CB  1 
ATOM   1653 O OG1 . THR A 1 377 ? 11.052  -5.437  7.966   1.00 26.44 ? 377 THR A OG1 1 
ATOM   1654 C CG2 . THR A 1 377 ? 12.241  -4.211  6.261   1.00 26.49 ? 377 THR A CG2 1 
ATOM   1655 N N   . SER A 1 378 ? 12.576  -7.582  4.392   1.00 21.82 ? 378 SER A N   1 
ATOM   1656 C CA  . SER A 1 378 ? 13.382  -7.822  3.191   1.00 21.85 ? 378 SER A CA  1 
ATOM   1657 C C   . SER A 1 378 ? 12.557  -8.410  2.021   1.00 20.76 ? 378 SER A C   1 
ATOM   1658 O O   . SER A 1 378 ? 13.087  -8.511  0.899   1.00 21.71 ? 378 SER A O   1 
ATOM   1659 C CB  . SER A 1 378 ? 14.527  -8.778  3.525   1.00 23.48 ? 378 SER A CB  1 
ATOM   1660 O OG  . SER A 1 378 ? 13.991  -10.001 4.004   1.00 25.11 ? 378 SER A OG  1 
ATOM   1661 N N   . ASP A 1 379 ? 11.273  -8.768  2.273   1.00 19.78 ? 379 ASP A N   1 
ATOM   1662 C CA  . ASP A 1 379 ? 10.396  -9.404  1.294   1.00 20.12 ? 379 ASP A CA  1 
ATOM   1663 C C   . ASP A 1 379 ? 9.248   -8.495  0.895   1.00 20.62 ? 379 ASP A C   1 
ATOM   1664 O O   . ASP A 1 379 ? 9.118   -8.172  -0.290  1.00 20.92 ? 379 ASP A O   1 
ATOM   1665 C CB  . ASP A 1 379 ? 9.869   -10.749 1.822   1.00 20.50 ? 379 ASP A CB  1 
ATOM   1666 C CG  . ASP A 1 379 ? 8.939   -11.416 0.833   1.00 22.77 ? 379 ASP A CG  1 
ATOM   1667 O OD1 . ASP A 1 379 ? 9.441   -11.909 -0.208  1.00 23.41 ? 379 ASP A OD1 1 
ATOM   1668 O OD2 . ASP A 1 379 ? 7.701   -11.402 1.068   1.00 23.60 ? 379 ASP A OD2 1 
ATOM   1669 N N   . ARG A 1 380 ? 8.428   -8.092  1.883   1.00 20.06 ? 380 ARG A N   1 
ATOM   1670 C CA  . ARG A 1 380 ? 7.337   -7.143  1.770   1.00 20.52 ? 380 ARG A CA  1 
ATOM   1671 C C   . ARG A 1 380 ? 6.173   -7.630  0.959   1.00 21.38 ? 380 ARG A C   1 
ATOM   1672 O O   . ARG A 1 380 ? 5.311   -6.806  0.674   1.00 23.30 ? 380 ARG A O   1 
ATOM   1673 C CB  . ARG A 1 380 ? 7.809   -5.800  1.166   1.00 22.19 ? 380 ARG A CB  1 
ATOM   1674 C CG  . ARG A 1 380 ? 9.064   -5.216  1.797   1.00 26.80 ? 380 ARG A CG  1 
ATOM   1675 C CD  . ARG A 1 380 ? 9.501   -3.899  1.129   1.00 32.13 ? 380 ARG A CD  1 
ATOM   1676 N NE  . ARG A 1 380 ? 9.361   -3.931  -0.328  1.00 39.67 ? 380 ARG A NE  1 
ATOM   1677 C CZ  . ARG A 1 380 ? 10.281  -4.406  -1.165  1.00 47.05 ? 380 ARG A CZ  1 
ATOM   1678 N NH1 . ARG A 1 380 ? 10.058  -4.408  -2.475  1.00 48.56 ? 380 ARG A NH1 1 
ATOM   1679 N NH2 . ARG A 1 380 ? 11.441  -4.860  -0.702  1.00 47.05 ? 380 ARG A NH2 1 
ATOM   1680 N N   . HIS A 1 381 ? 6.148   -8.911  0.524   1.00 19.98 ? 381 HIS A N   1 
ATOM   1681 C CA  . HIS A 1 381 ? 5.054   -9.352  -0.332  1.00 19.21 ? 381 HIS A CA  1 
ATOM   1682 C C   . HIS A 1 381 ? 4.010   -10.227 0.357   1.00 18.94 ? 381 HIS A C   1 
ATOM   1683 O O   . HIS A 1 381 ? 4.317   -11.004 1.247   1.00 19.60 ? 381 HIS A O   1 
ATOM   1684 C CB  . HIS A 1 381 ? 5.615   -10.160 -1.526  1.00 19.82 ? 381 HIS A CB  1 
ATOM   1685 C CG  . HIS A 1 381 ? 6.228   -9.319  -2.611  1.00 23.02 ? 381 HIS A CG  1 
ATOM   1686 N ND1 . HIS A 1 381 ? 7.307   -8.490  -2.364  1.00 23.97 ? 381 HIS A ND1 1 
ATOM   1687 C CD2 . HIS A 1 381 ? 5.873   -9.200  -3.911  1.00 24.48 ? 381 HIS A CD2 1 
ATOM   1688 C CE1 . HIS A 1 381 ? 7.581   -7.894  -3.515  1.00 25.69 ? 381 HIS A CE1 1 
ATOM   1689 N NE2 . HIS A 1 381 ? 6.746   -8.299  -4.482  1.00 26.00 ? 381 HIS A NE2 1 
ATOM   1690 N N   . ILE A 1 382 ? 2.774   -10.128 -0.127  1.00 17.64 ? 382 ILE A N   1 
ATOM   1691 C CA  . ILE A 1 382 ? 1.702   -11.043 0.182   1.00 16.70 ? 382 ILE A CA  1 
ATOM   1692 C C   . ILE A 1 382 ? 1.635   -11.992 -1.030  1.00 17.70 ? 382 ILE A C   1 
ATOM   1693 O O   . ILE A 1 382 ? 1.593   -11.530 -2.190  1.00 18.51 ? 382 ILE A O   1 
ATOM   1694 C CB  . ILE A 1 382 ? 0.365   -10.300 0.321   1.00 17.07 ? 382 ILE A CB  1 
ATOM   1695 C CG1 . ILE A 1 382 ? 0.421   -9.395  1.570   1.00 18.82 ? 382 ILE A CG1 1 
ATOM   1696 C CG2 . ILE A 1 382 ? -0.766  -11.309 0.388   1.00 16.44 ? 382 ILE A CG2 1 
ATOM   1697 C CD1 . ILE A 1 382 ? -0.721  -8.367  1.640   1.00 20.96 ? 382 ILE A CD1 1 
ATOM   1698 N N   . ARG A 1 383 ? 1.645   -13.297 -0.777  1.00 17.08 ? 383 ARG A N   1 
ATOM   1699 C CA  . ARG A 1 383 ? 1.547   -14.270 -1.870  1.00 17.42 ? 383 ARG A CA  1 
ATOM   1700 C C   . ARG A 1 383 ? 0.339   -15.165 -1.618  1.00 17.48 ? 383 ARG A C   1 
ATOM   1701 O O   . ARG A 1 383 ? 0.059   -15.521 -0.460  1.00 18.29 ? 383 ARG A O   1 
ATOM   1702 C CB  . ARG A 1 383 ? 2.827   -15.111 -1.952  1.00 18.13 ? 383 ARG A CB  1 
ATOM   1703 C CG  . ARG A 1 383 ? 3.970   -14.314 -2.534  1.00 18.00 ? 383 ARG A CG  1 
ATOM   1704 C CD  . ARG A 1 383 ? 5.244   -15.128 -2.562  1.00 20.00 ? 383 ARG A CD  1 
ATOM   1705 N NE  . ARG A 1 383 ? 6.341   -14.461 -3.288  1.00 20.70 ? 383 ARG A NE  1 
ATOM   1706 C CZ  . ARG A 1 383 ? 6.630   -14.665 -4.569  1.00 22.03 ? 383 ARG A CZ  1 
ATOM   1707 N NH1 . ARG A 1 383 ? 7.685   -14.074 -5.120  1.00 22.85 ? 383 ARG A NH1 1 
ATOM   1708 N NH2 . ARG A 1 383 ? 5.945   -15.556 -5.279  1.00 22.26 ? 383 ARG A NH2 1 
ATOM   1709 N N   . ILE A 1 384 ? -0.399  -15.486 -2.675  1.00 17.28 ? 384 ILE A N   1 
ATOM   1710 C CA  . ILE A 1 384 ? -1.560  -16.373 -2.562  1.00 17.50 ? 384 ILE A CA  1 
ATOM   1711 C C   . ILE A 1 384 ? -1.192  -17.642 -3.300  1.00 18.14 ? 384 ILE A C   1 
ATOM   1712 O O   . ILE A 1 384 ? -0.672  -17.564 -4.411  1.00 18.74 ? 384 ILE A O   1 
ATOM   1713 C CB  . ILE A 1 384 ? -2.807  -15.733 -3.186  1.00 19.28 ? 384 ILE A CB  1 
ATOM   1714 C CG1 . ILE A 1 384 ? -3.052  -14.310 -2.645  1.00 20.79 ? 384 ILE A CG1 1 
ATOM   1715 C CG2 . ILE A 1 384 ? -4.020  -16.626 -3.001  1.00 20.45 ? 384 ILE A CG2 1 
ATOM   1716 C CD1 . ILE A 1 384 ? -3.228  -14.235 -1.134  1.00 22.32 ? 384 ILE A CD1 1 
ATOM   1717 N N   . TRP A 1 385 ? -1.460  -18.793 -2.700  1.00 17.98 ? 385 TRP A N   1 
ATOM   1718 C CA  . TRP A 1 385 ? -1.103  -20.094 -3.263  1.00 17.98 ? 385 TRP A CA  1 
ATOM   1719 C C   . TRP A 1 385 ? -2.279  -21.050 -3.365  1.00 18.46 ? 385 TRP A C   1 
ATOM   1720 O O   . TRP A 1 385 ? -3.167  -21.021 -2.515  1.00 18.73 ? 385 TRP A O   1 
ATOM   1721 C CB  . TRP A 1 385 ? -0.163  -20.787 -2.283  1.00 17.38 ? 385 TRP A CB  1 
ATOM   1722 C CG  . TRP A 1 385 ? 0.954   -19.930 -1.758  1.00 17.78 ? 385 TRP A CG  1 
ATOM   1723 C CD1 . TRP A 1 385 ? 0.961   -19.207 -0.603  1.00 18.65 ? 385 TRP A CD1 1 
ATOM   1724 C CD2 . TRP A 1 385 ? 2.252   -19.767 -2.342  1.00 18.42 ? 385 TRP A CD2 1 
ATOM   1725 N NE1 . TRP A 1 385 ? 2.200   -18.623 -0.415  1.00 19.29 ? 385 TRP A NE1 1 
ATOM   1726 C CE2 . TRP A 1 385 ? 2.995   -18.924 -1.488  1.00 19.22 ? 385 TRP A CE2 1 
ATOM   1727 C CE3 . TRP A 1 385 ? 2.858   -20.258 -3.508  1.00 19.66 ? 385 TRP A CE3 1 
ATOM   1728 C CZ2 . TRP A 1 385 ? 4.328   -18.589 -1.745  1.00 20.49 ? 385 TRP A CZ2 1 
ATOM   1729 C CZ3 . TRP A 1 385 ? 4.177   -19.915 -3.767  1.00 20.68 ? 385 TRP A CZ3 1 
ATOM   1730 C CH2 . TRP A 1 385 ? 4.885   -19.072 -2.907  1.00 21.46 ? 385 TRP A CH2 1 
ATOM   1731 N N   . ASN A 1 386 ? -2.209  -21.997 -4.314  1.00 18.20 ? 386 ASN A N   1 
ATOM   1732 C CA  . ASN A 1 386 ? -3.105  -23.138 -4.307  1.00 20.11 ? 386 ASN A CA  1 
ATOM   1733 C C   . ASN A 1 386 ? -2.155  -24.251 -3.802  1.00 21.59 ? 386 ASN A C   1 
ATOM   1734 O O   . ASN A 1 386 ? -1.174  -24.579 -4.489  1.00 22.02 ? 386 ASN A O   1 
ATOM   1735 C CB  . ASN A 1 386 ? -3.671  -23.464 -5.690  1.00 21.72 ? 386 ASN A CB  1 
ATOM   1736 C CG  . ASN A 1 386 ? -4.547  -24.691 -5.631  1.00 26.97 ? 386 ASN A CG  1 
ATOM   1737 O OD1 . ASN A 1 386 ? -4.107  -25.751 -5.210  1.00 26.91 ? 386 ASN A OD1 1 
ATOM   1738 N ND2 . ASN A 1 386 ? -5.819  -24.566 -5.996  1.00 29.51 ? 386 ASN A ND2 1 
ATOM   1739 N N   . VAL A 1 387 ? -2.399  -24.800 -2.597  1.00 21.16 ? 387 VAL A N   1 
ATOM   1740 C CA  . VAL A 1 387 ? -1.494  -25.792 -2.003  1.00 21.49 ? 387 VAL A CA  1 
ATOM   1741 C C   . VAL A 1 387 ? -1.551  -27.178 -2.642  1.00 23.84 ? 387 VAL A C   1 
ATOM   1742 O O   . VAL A 1 387 ? -0.670  -27.996 -2.382  1.00 24.94 ? 387 VAL A O   1 
ATOM   1743 C CB  . VAL A 1 387 ? -1.655  -25.902 -0.474  1.00 20.34 ? 387 VAL A CB  1 
ATOM   1744 C CG1 . VAL A 1 387 ? -1.509  -24.522 0.173   1.00 20.73 ? 387 VAL A CG1 1 
ATOM   1745 C CG2 . VAL A 1 387 ? -3.008  -26.509 -0.118  1.00 20.17 ? 387 VAL A CG2 1 
ATOM   1746 N N   A CYS A 1 388 ? -2.574  -27.444 -3.443  0.51 24.10 ? 388 CYS A N   1 
ATOM   1747 N N   B CYS A 1 388 ? -2.546  -27.448 -3.492  0.49 24.36 ? 388 CYS A N   1 
ATOM   1748 C CA  A CYS A 1 388 ? -2.696  -28.710 -4.128  0.51 25.12 ? 388 CYS A CA  1 
ATOM   1749 C CA  B CYS A 1 388 ? -2.644  -28.738 -4.175  0.49 25.60 ? 388 CYS A CA  1 
ATOM   1750 C C   A CYS A 1 388 ? -1.789  -28.679 -5.366  0.51 25.23 ? 388 CYS A C   1 
ATOM   1751 C C   B CYS A 1 388 ? -1.839  -28.737 -5.457  0.49 25.51 ? 388 CYS A C   1 
ATOM   1752 O O   A CYS A 1 388 ? -0.948  -29.559 -5.519  0.51 25.81 ? 388 CYS A O   1 
ATOM   1753 O O   B CYS A 1 388 ? -1.192  -29.732 -5.782  0.49 26.11 ? 388 CYS A O   1 
ATOM   1754 C CB  A CYS A 1 388 ? -4.152  -28.964 -4.500  0.51 26.40 ? 388 CYS A CB  1 
ATOM   1755 C CB  B CYS A 1 388 ? -4.098  -29.094 -4.438  0.49 27.47 ? 388 CYS A CB  1 
ATOM   1756 S SG  A CYS A 1 388 ? -4.431  -30.524 -5.367  0.51 30.65 ? 388 CYS A SG  1 
ATOM   1757 S SG  B CYS A 1 388 ? -5.013  -29.527 -2.946  0.49 33.49 ? 388 CYS A SG  1 
ATOM   1758 N N   . SER A 1 389 ? -1.931  -27.650 -6.220  1.00 24.77 ? 389 SER A N   1 
ATOM   1759 C CA  . SER A 1 389 ? -1.166  -27.528 -7.459  1.00 24.36 ? 389 SER A CA  1 
ATOM   1760 C C   . SER A 1 389 ? 0.221   -26.900 -7.257  1.00 24.44 ? 389 SER A C   1 
ATOM   1761 O O   . SER A 1 389 ? 1.027   -26.920 -8.190  1.00 25.29 ? 389 SER A O   1 
ATOM   1762 C CB  . SER A 1 389 ? -1.932  -26.671 -8.455  1.00 25.23 ? 389 SER A CB  1 
ATOM   1763 O OG  . SER A 1 389 ? -1.997  -25.334 -7.981  1.00 25.06 ? 389 SER A OG  1 
ATOM   1764 N N   . GLY A 1 390 ? 0.438   -26.239 -6.117  1.00 22.42 ? 390 GLY A N   1 
ATOM   1765 C CA  . GLY A 1 390 ? 1.678   -25.509 -5.861  1.00 22.89 ? 390 GLY A CA  1 
ATOM   1766 C C   . GLY A 1 390 ? 1.738   -24.153 -6.551  1.00 22.72 ? 390 GLY A C   1 
ATOM   1767 O O   . GLY A 1 390 ? 2.768   -23.469 -6.484  1.00 23.97 ? 390 GLY A O   1 
ATOM   1768 N N   . ALA A 1 391 ? 0.656   -23.750 -7.237  1.00 22.13 ? 391 ALA A N   1 
ATOM   1769 C CA  . ALA A 1 391 ? 0.668   -22.497 -7.982  1.00 22.80 ? 391 ALA A CA  1 
ATOM   1770 C C   . ALA A 1 391 ? 0.723   -21.292 -7.082  1.00 21.69 ? 391 ALA A C   1 
ATOM   1771 O O   . ALA A 1 391 ? 0.029   -21.250 -6.078  1.00 21.05 ? 391 ALA A O   1 
ATOM   1772 C CB  . ALA A 1 391 ? -0.561  -22.397 -8.869  1.00 23.42 ? 391 ALA A CB  1 
ATOM   1773 N N   . CYS A 1 392 ? 1.491   -20.277 -7.487  1.00 20.54 ? 392 CYS A N   1 
ATOM   1774 C CA  . CYS A 1 392 ? 1.441   -18.980 -6.818  1.00 20.95 ? 392 CYS A CA  1 
ATOM   1775 C C   . CYS A 1 392 ? 0.469   -18.195 -7.680  1.00 21.81 ? 392 CYS A C   1 
ATOM   1776 O O   . CYS A 1 392 ? 0.727   -17.950 -8.866  1.00 22.88 ? 392 CYS A O   1 
ATOM   1777 C CB  . CYS A 1 392 ? 2.798   -18.292 -6.782  1.00 21.50 ? 392 CYS A CB  1 
ATOM   1778 S SG  . CYS A 1 392 ? 2.712   -16.646 -6.014  1.00 25.98 ? 392 CYS A SG  1 
ATOM   1779 N N   . LEU A 1 393 ? -0.706  -17.929 -7.142  1.00 21.67 ? 393 LEU A N   1 
ATOM   1780 C CA  . LEU A 1 393 ? -1.777  -17.252 -7.840  1.00 22.00 ? 393 LEU A CA  1 
ATOM   1781 C C   . LEU A 1 393 ? -1.587  -15.735 -7.886  1.00 22.13 ? 393 LEU A C   1 
ATOM   1782 O O   . LEU A 1 393 ? -2.111  -15.083 -8.782  1.00 22.36 ? 393 LEU A O   1 
ATOM   1783 C CB  . LEU A 1 393 ? -3.090  -17.576 -7.132  1.00 22.72 ? 393 LEU A CB  1 
ATOM   1784 C CG  . LEU A 1 393 ? -3.384  -19.067 -6.911  1.00 24.49 ? 393 LEU A CG  1 
ATOM   1785 C CD1 . LEU A 1 393 ? -4.642  -19.262 -6.110  1.00 24.76 ? 393 LEU A CD1 1 
ATOM   1786 C CD2 . LEU A 1 393 ? -3.476  -19.804 -8.223  1.00 25.90 ? 393 LEU A CD2 1 
ATOM   1787 N N   . SER A 1 394 ? -0.880  -15.167 -6.901  1.00 21.83 ? 394 SER A N   1 
ATOM   1788 C CA  . SER A 1 394 ? -0.671  -13.731 -6.848  1.00 21.22 ? 394 SER A CA  1 
ATOM   1789 C C   . SER A 1 394 ? 0.523   -13.398 -5.958  1.00 21.83 ? 394 SER A C   1 
ATOM   1790 O O   . SER A 1 394 ? 0.743   -14.079 -4.969  1.00 20.87 ? 394 SER A O   1 
ATOM   1791 C CB  . SER A 1 394 ? -1.911  -13.054 -6.261  1.00 22.07 ? 394 SER A CB  1 
ATOM   1792 O OG  . SER A 1 394 ? -1.740  -11.647 -6.187  1.00 25.00 ? 394 SER A OG  1 
ATOM   1793 N N   . ALA A 1 395 ? 1.268   -12.336 -6.292  1.00 21.85 ? 395 ALA A N   1 
ATOM   1794 C CA  . ALA A 1 395 ? 2.384   -11.867 -5.465  1.00 22.32 ? 395 ALA A CA  1 
ATOM   1795 C C   . ALA A 1 395 ? 2.279   -10.361 -5.513  1.00 23.72 ? 395 ALA A C   1 
ATOM   1796 O O   . ALA A 1 395 ? 2.365   -9.777  -6.602  1.00 25.63 ? 395 ALA A O   1 
ATOM   1797 C CB  . ALA A 1 395 ? 3.719   -12.332 -6.023  1.00 22.80 ? 395 ALA A CB  1 
ATOM   1798 N N   . VAL A 1 396 ? 1.973   -9.738  -4.381  1.00 22.41 ? 396 VAL A N   1 
ATOM   1799 C CA  . VAL A 1 396 ? 1.757   -8.301  -4.321  1.00 23.20 ? 396 VAL A CA  1 
ATOM   1800 C C   . VAL A 1 396 ? 2.723   -7.653  -3.351  1.00 23.15 ? 396 VAL A C   1 
ATOM   1801 O O   . VAL A 1 396 ? 2.856   -8.115  -2.230  1.00 21.93 ? 396 VAL A O   1 
ATOM   1802 C CB  . VAL A 1 396 ? 0.288   -7.973  -3.960  1.00 26.24 ? 396 VAL A CB  1 
ATOM   1803 C CG1 . VAL A 1 396 ? 0.095   -6.466  -3.820  1.00 27.58 ? 396 VAL A CG1 1 
ATOM   1804 C CG2 . VAL A 1 396 ? -0.673  -8.542  -5.005  1.00 27.21 ? 396 VAL A CG2 1 
ATOM   1805 N N   . ASP A 1 397 ? 3.385   -6.567  -3.770  1.00 24.07 ? 397 ASP A N   1 
ATOM   1806 C CA  . ASP A 1 397 ? 4.308   -5.849  -2.908  1.00 25.22 ? 397 ASP A CA  1 
ATOM   1807 C C   . ASP A 1 397 ? 3.507   -4.909  -2.004  1.00 25.36 ? 397 ASP A C   1 
ATOM   1808 O O   . ASP A 1 397 ? 2.873   -3.971  -2.496  1.00 27.34 ? 397 ASP A O   1 
ATOM   1809 C CB  . ASP A 1 397 ? 5.301   -5.029  -3.780  1.00 27.45 ? 397 ASP A CB  1 
ATOM   1810 C CG  . ASP A 1 397 ? 6.481   -4.447  -3.025  1.00 31.70 ? 397 ASP A CG  1 
ATOM   1811 O OD1 . ASP A 1 397 ? 6.428   -4.402  -1.772  1.00 30.96 ? 397 ASP A OD1 1 
ATOM   1812 O OD2 . ASP A 1 397 ? 7.475   -4.052  -3.688  1.00 35.40 ? 397 ASP A OD2 1 
ATOM   1813 N N   . ALA A 1 398 ? 3.546   -5.149  -0.690  1.00 23.06 ? 398 ALA A N   1 
ATOM   1814 C CA  . ALA A 1 398 ? 2.884   -4.310  0.306   1.00 23.76 ? 398 ALA A CA  1 
ATOM   1815 C C   . ALA A 1 398 ? 3.715   -3.101  0.750   1.00 24.68 ? 398 ALA A C   1 
ATOM   1816 O O   . ALA A 1 398 ? 3.206   -2.288  1.525   1.00 25.11 ? 398 ALA A O   1 
ATOM   1817 C CB  . ALA A 1 398 ? 2.497   -5.144  1.528   1.00 23.60 ? 398 ALA A CB  1 
ATOM   1818 N N   . HIS A 1 399 ? 5.011   -3.013  0.324   1.00 24.61 ? 399 HIS A N   1 
ATOM   1819 C CA  . HIS A 1 399 ? 5.962   -1.942  0.648   1.00 25.69 ? 399 HIS A CA  1 
ATOM   1820 C C   . HIS A 1 399 ? 6.364   -1.861  2.119   1.00 24.83 ? 399 HIS A C   1 
ATOM   1821 O O   . HIS A 1 399 ? 6.830   -0.820  2.579   1.00 25.63 ? 399 HIS A O   1 
ATOM   1822 C CB  . HIS A 1 399 ? 5.470   -0.569  0.158   1.00 28.45 ? 399 HIS A CB  1 
ATOM   1823 C CG  . HIS A 1 399 ? 5.091   -0.587  -1.288  1.00 32.98 ? 399 HIS A CG  1 
ATOM   1824 N ND1 . HIS A 1 399 ? 6.050   -0.568  -2.282  1.00 36.45 ? 399 HIS A ND1 1 
ATOM   1825 C CD2 . HIS A 1 399 ? 3.867   -0.661  -1.856  1.00 34.68 ? 399 HIS A CD2 1 
ATOM   1826 C CE1 . HIS A 1 399 ? 5.382   -0.621  -3.422  1.00 37.26 ? 399 HIS A CE1 1 
ATOM   1827 N NE2 . HIS A 1 399 ? 4.063   -0.674  -3.215  1.00 36.56 ? 399 HIS A NE2 1 
ATOM   1828 N N   . SER A 1 400 ? 6.178   -2.945  2.856   1.00 23.24 ? 400 SER A N   1 
ATOM   1829 C CA  . SER A 1 400 ? 6.532   -2.997  4.254   1.00 22.26 ? 400 SER A CA  1 
ATOM   1830 C C   . SER A 1 400 ? 6.522   -4.443  4.682   1.00 21.53 ? 400 SER A C   1 
ATOM   1831 O O   . SER A 1 400 ? 5.928   -5.287  4.005   1.00 22.34 ? 400 SER A O   1 
ATOM   1832 C CB  . SER A 1 400 ? 5.472   -2.259  5.077   1.00 23.81 ? 400 SER A CB  1 
ATOM   1833 O OG  . SER A 1 400 ? 5.875   -2.152  6.438   1.00 25.35 ? 400 SER A OG  1 
ATOM   1834 N N   . GLN A 1 401 ? 7.061   -4.738  5.873   1.00 20.93 ? 401 GLN A N   1 
ATOM   1835 C CA  . GLN A 1 401 ? 6.925   -6.095  6.435   1.00 20.94 ? 401 GLN A CA  1 
ATOM   1836 C C   . GLN A 1 401 ? 5.449   -6.423  6.605   1.00 21.15 ? 401 GLN A C   1 
ATOM   1837 O O   . GLN A 1 401 ? 4.645   -5.503  6.823   1.00 21.97 ? 401 GLN A O   1 
ATOM   1838 C CB  . GLN A 1 401 ? 7.630   -6.223  7.784   1.00 23.82 ? 401 GLN A CB  1 
ATOM   1839 C CG  . GLN A 1 401 ? 7.274   -5.162  8.797   1.00 28.70 ? 401 GLN A CG  1 
ATOM   1840 C CD  . GLN A 1 401 ? 7.937   -5.389  10.145  1.00 36.31 ? 401 GLN A CD  1 
ATOM   1841 O OE1 . GLN A 1 401 ? 7.360   -5.059  11.182  1.00 38.63 ? 401 GLN A OE1 1 
ATOM   1842 N NE2 . GLN A 1 401 ? 9.151   -5.954  10.180  1.00 35.39 ? 401 GLN A NE2 1 
ATOM   1843 N N   . VAL A 1 402 ? 5.085   -7.691  6.445   1.00 19.64 ? 402 VAL A N   1 
ATOM   1844 C CA  . VAL A 1 402 ? 3.679   -8.098  6.574   1.00 19.41 ? 402 VAL A CA  1 
ATOM   1845 C C   . VAL A 1 402 ? 3.608   -9.007  7.828   1.00 20.75 ? 402 VAL A C   1 
ATOM   1846 O O   . VAL A 1 402 ? 3.965   -10.182 7.748   1.00 21.73 ? 402 VAL A O   1 
ATOM   1847 C CB  . VAL A 1 402 ? 3.227   -8.901  5.317   1.00 19.70 ? 402 VAL A CB  1 
ATOM   1848 C CG1 . VAL A 1 402 ? 1.737   -9.254  5.395   1.00 20.15 ? 402 VAL A CG1 1 
ATOM   1849 C CG2 . VAL A 1 402 ? 3.539   -8.164  4.026   1.00 19.99 ? 402 VAL A CG2 1 
ATOM   1850 N N   . CYS A 1 403 ? 3.218   -8.463  8.969   1.00 20.04 ? 403 CYS A N   1 
ATOM   1851 C CA  . CYS A 1 403 ? 3.189   -9.223  10.225  1.00 19.92 ? 403 CYS A CA  1 
ATOM   1852 C C   . CYS A 1 403 ? 2.076   -10.221 10.296  1.00 20.52 ? 403 CYS A C   1 
ATOM   1853 O O   . CYS A 1 403 ? 2.230   -11.281 10.910  1.00 22.15 ? 403 CYS A O   1 
ATOM   1854 C CB  . CYS A 1 403 ? 3.137   -8.275  11.420  1.00 21.18 ? 403 CYS A CB  1 
ATOM   1855 S SG  . CYS A 1 403 ? 1.568   -7.395  11.595  1.00 25.83 ? 403 CYS A SG  1 
ATOM   1856 N N   A SER A 1 404 ? 0.942   -9.900  9.677   0.43 19.41 ? 404 SER A N   1 
ATOM   1857 N N   B SER A 1 404 ? 0.923   -9.889  9.711   0.57 19.18 ? 404 SER A N   1 
ATOM   1858 C CA  A SER A 1 404 ? -0.239  -10.733 9.784   0.43 19.29 ? 404 SER A CA  1 
ATOM   1859 C CA  B SER A 1 404 ? -0.268  -10.734 9.784   0.57 18.87 ? 404 SER A CA  1 
ATOM   1860 C C   A SER A 1 404 ? -1.181  -10.542 8.621   0.43 18.63 ? 404 SER A C   1 
ATOM   1861 C C   B SER A 1 404 ? -1.146  -10.563 8.581   0.57 18.31 ? 404 SER A C   1 
ATOM   1862 O O   A SER A 1 404 ? -1.220  -9.468  8.029   0.43 18.74 ? 404 SER A O   1 
ATOM   1863 O O   B SER A 1 404 ? -1.152  -9.502  7.960   0.57 18.29 ? 404 SER A O   1 
ATOM   1864 C CB  A SER A 1 404 ? -0.970  -10.380 11.077  0.43 20.94 ? 404 SER A CB  1 
ATOM   1865 C CB  B SER A 1 404 ? -1.122  -10.355 10.998  0.57 20.13 ? 404 SER A CB  1 
ATOM   1866 O OG  A SER A 1 404 ? -2.086  -11.215 11.308  0.43 22.66 ? 404 SER A OG  1 
ATOM   1867 O OG  B SER A 1 404 ? -0.631  -10.825 12.238  0.57 21.13 ? 404 SER A OG  1 
ATOM   1868 N N   . ILE A 1 405 ? -1.960  -11.581 8.304   1.00 17.97 ? 405 ILE A N   1 
ATOM   1869 C CA  . ILE A 1 405 ? -2.993  -11.549 7.265   1.00 18.00 ? 405 ILE A CA  1 
ATOM   1870 C C   . ILE A 1 405 ? -4.218  -12.244 7.843   1.00 17.35 ? 405 ILE A C   1 
ATOM   1871 O O   . ILE A 1 405 ? -4.117  -13.305 8.487   1.00 17.60 ? 405 ILE A O   1 
ATOM   1872 C CB  . ILE A 1 405 ? -2.587  -12.290 5.963   1.00 19.17 ? 405 ILE A CB  1 
ATOM   1873 C CG1 . ILE A 1 405 ? -1.415  -11.600 5.266   1.00 19.45 ? 405 ILE A CG1 1 
ATOM   1874 C CG2 . ILE A 1 405 ? -3.765  -12.396 4.994   1.00 19.89 ? 405 ILE A CG2 1 
ATOM   1875 C CD1 . ILE A 1 405 ? -0.747  -12.559 4.237   1.00 21.16 ? 405 ILE A CD1 1 
ATOM   1876 N N   . LEU A 1 406 ? -5.380  -11.656 7.609   1.00 16.72 ? 406 LEU A N   1 
ATOM   1877 C CA  . LEU A 1 406 ? -6.649  -12.290 7.952   1.00 16.38 ? 406 LEU A CA  1 
ATOM   1878 C C   . LEU A 1 406 ? -7.559  -12.205 6.725   1.00 16.56 ? 406 LEU A C   1 
ATOM   1879 O O   . LEU A 1 406 ? -7.459  -11.253 5.951   1.00 17.68 ? 406 LEU A O   1 
ATOM   1880 C CB  . LEU A 1 406 ? -7.349  -11.528 9.094   1.00 17.39 ? 406 LEU A CB  1 
ATOM   1881 C CG  . LEU A 1 406 ? -6.616  -11.532 10.415  1.00 20.45 ? 406 LEU A CG  1 
ATOM   1882 C CD1 . LEU A 1 406 ? -7.275  -10.594 11.386  1.00 20.43 ? 406 LEU A CD1 1 
ATOM   1883 C CD2 . LEU A 1 406 ? -6.529  -12.927 10.991  1.00 22.14 ? 406 LEU A CD2 1 
ATOM   1884 N N   . TRP A 1 407 ? -8.483  -13.149 6.580   1.00 15.49 ? 407 TRP A N   1 
ATOM   1885 C CA  . TRP A 1 407 ? -9.480  -13.076 5.522   1.00 16.55 ? 407 TRP A CA  1 
ATOM   1886 C C   . TRP A 1 407 ? -10.818 -12.732 6.163   1.00 17.58 ? 407 TRP A C   1 
ATOM   1887 O O   . TRP A 1 407 ? -11.142 -13.273 7.229   1.00 17.67 ? 407 TRP A O   1 
ATOM   1888 C CB  . TRP A 1 407 ? -9.684  -14.453 4.840   1.00 16.62 ? 407 TRP A CB  1 
ATOM   1889 C CG  . TRP A 1 407 ? -8.476  -14.986 4.136   1.00 17.82 ? 407 TRP A CG  1 
ATOM   1890 C CD1 . TRP A 1 407 ? -7.359  -15.509 4.721   1.00 18.79 ? 407 TRP A CD1 1 
ATOM   1891 C CD2 . TRP A 1 407 ? -8.288  -15.113 2.723   1.00 18.00 ? 407 TRP A CD2 1 
ATOM   1892 N NE1 . TRP A 1 407 ? -6.507  -15.992 3.761   1.00 19.21 ? 407 TRP A NE1 1 
ATOM   1893 C CE2 . TRP A 1 407 ? -7.035  -15.735 2.522   1.00 18.37 ? 407 TRP A CE2 1 
ATOM   1894 C CE3 . TRP A 1 407 ? -9.063  -14.793 1.603   1.00 19.27 ? 407 TRP A CE3 1 
ATOM   1895 C CZ2 . TRP A 1 407 ? -6.540  -16.028 1.255   1.00 19.57 ? 407 TRP A CZ2 1 
ATOM   1896 C CZ3 . TRP A 1 407 ? -8.564  -15.073 0.343   1.00 20.66 ? 407 TRP A CZ3 1 
ATOM   1897 C CH2 . TRP A 1 407 ? -7.308  -15.675 0.179   1.00 20.50 ? 407 TRP A CH2 1 
ATOM   1898 N N   . SER A 1 408 ? -11.624 -11.912 5.490   1.00 17.97 ? 408 SER A N   1 
ATOM   1899 C CA  . SER A 1 408 ? -12.985 -11.677 5.986   1.00 19.78 ? 408 SER A CA  1 
ATOM   1900 C C   . SER A 1 408 ? -13.773 -12.889 5.562   1.00 24.26 ? 408 SER A C   1 
ATOM   1901 O O   . SER A 1 408 ? -13.792 -13.209 4.374   1.00 25.69 ? 408 SER A O   1 
ATOM   1902 C CB  . SER A 1 408 ? -13.595 -10.429 5.361   1.00 19.39 ? 408 SER A CB  1 
ATOM   1903 O OG  . SER A 1 408 ? -14.993 -10.411 5.608   1.00 20.05 ? 408 SER A OG  1 
ATOM   1904 N N   . PRO A 1 409 ? -14.493 -13.528 6.502   1.00 26.14 ? 409 PRO A N   1 
ATOM   1905 C CA  . PRO A 1 409 ? -15.327 -14.671 6.119   1.00 27.29 ? 409 PRO A CA  1 
ATOM   1906 C C   . PRO A 1 409 ? -16.657 -14.250 5.497   1.00 27.99 ? 409 PRO A C   1 
ATOM   1907 O O   . PRO A 1 409 ? -17.486 -15.139 5.271   1.00 30.13 ? 409 PRO A O   1 
ATOM   1908 C CB  . PRO A 1 409 ? -15.566 -15.370 7.445   1.00 28.81 ? 409 PRO A CB  1 
ATOM   1909 C CG  . PRO A 1 409 ? -15.608 -14.227 8.452   1.00 29.59 ? 409 PRO A CG  1 
ATOM   1910 C CD  . PRO A 1 409 ? -14.599 -13.219 7.943   1.00 27.07 ? 409 PRO A CD  1 
ATOM   1911 N N   . HIS A 1 410 ? -16.888 -12.919 5.232   1.00 24.77 ? 410 HIS A N   1 
ATOM   1912 C CA  . HIS A 1 410 ? -18.149 -12.420 4.675   1.00 23.97 ? 410 HIS A CA  1 
ATOM   1913 C C   . HIS A 1 410 ? -17.946 -11.522 3.443   1.00 24.51 ? 410 HIS A C   1 
ATOM   1914 O O   . HIS A 1 410 ? -18.717 -11.629 2.497   1.00 25.52 ? 410 HIS A O   1 
ATOM   1915 C CB  . HIS A 1 410 ? -18.918 -11.617 5.746   1.00 24.16 ? 410 HIS A CB  1 
ATOM   1916 C CG  . HIS A 1 410 ? -19.213 -12.397 6.985   1.00 26.64 ? 410 HIS A CG  1 
ATOM   1917 N ND1 . HIS A 1 410 ? -20.126 -13.440 6.986   1.00 28.07 ? 410 HIS A ND1 1 
ATOM   1918 C CD2 . HIS A 1 410 ? -18.686 -12.275 8.222   1.00 29.01 ? 410 HIS A CD2 1 
ATOM   1919 C CE1 . HIS A 1 410 ? -20.148 -13.896 8.228   1.00 28.46 ? 410 HIS A CE1 1 
ATOM   1920 N NE2 . HIS A 1 410 ? -19.319 -13.216 9.015   1.00 30.27 ? 410 HIS A NE2 1 
ATOM   1921 N N   . TYR A 1 411 ? -16.936 -10.630 3.445   1.00 23.03 ? 411 TYR A N   1 
ATOM   1922 C CA  . TYR A 1 411 ? -16.707 -9.693  2.315   1.00 24.14 ? 411 TYR A CA  1 
ATOM   1923 C C   . TYR A 1 411 ? -15.809 -10.113 1.139   1.00 28.33 ? 411 TYR A C   1 
ATOM   1924 O O   . TYR A 1 411 ? -15.652 -9.300  0.208   1.00 29.90 ? 411 TYR A O   1 
ATOM   1925 C CB  . TYR A 1 411 ? -16.124 -8.379  2.817   1.00 23.32 ? 411 TYR A CB  1 
ATOM   1926 C CG  . TYR A 1 411 ? -17.152 -7.439  3.388   1.00 24.63 ? 411 TYR A CG  1 
ATOM   1927 C CD1 . TYR A 1 411 ? -17.923 -6.636  2.560   1.00 26.51 ? 411 TYR A CD1 1 
ATOM   1928 C CD2 . TYR A 1 411 ? -17.379 -7.375  4.751   1.00 25.49 ? 411 TYR A CD2 1 
ATOM   1929 C CE1 . TYR A 1 411 ? -18.879 -5.773  3.081   1.00 27.55 ? 411 TYR A CE1 1 
ATOM   1930 C CE2 . TYR A 1 411 ? -18.371 -6.559  5.277   1.00 27.12 ? 411 TYR A CE2 1 
ATOM   1931 C CZ  . TYR A 1 411 ? -19.086 -5.727  4.443   1.00 28.41 ? 411 TYR A CZ  1 
ATOM   1932 O OH  . TYR A 1 411 ? -20.033 -4.893  4.979   1.00 32.47 ? 411 TYR A OH  1 
ATOM   1933 N N   . LYS A 1 412 ? -15.152 -11.265 1.168   1.00 28.84 ? 412 LYS A N   1 
ATOM   1934 C CA  . LYS A 1 412 ? -14.206 -11.615 0.061   1.00 27.65 ? 412 LYS A CA  1 
ATOM   1935 C C   . LYS A 1 412 ? -13.081 -10.554 -0.009  1.00 23.80 ? 412 LYS A C   1 
ATOM   1936 O O   . LYS A 1 412 ? -12.800 -9.937  -1.043  1.00 23.10 ? 412 LYS A O   1 
ATOM   1937 C CB  . LYS A 1 412 ? -14.884 -11.808 -1.317  1.00 31.98 ? 412 LYS A CB  1 
ATOM   1938 C CG  . LYS A 1 412 ? -15.698 -13.089 -1.400  1.00 39.35 ? 412 LYS A CG  1 
ATOM   1939 C CD  . LYS A 1 412 ? -15.865 -13.591 -2.823  1.00 46.07 ? 412 LYS A CD  1 
ATOM   1940 C CE  . LYS A 1 412 ? -16.535 -14.947 -2.817  1.00 51.15 ? 412 LYS A CE  1 
ATOM   1941 N NZ  . LYS A 1 412 ? -16.588 -15.544 -4.178  1.00 54.51 ? 412 LYS A NZ  1 
ATOM   1942 N N   . GLU A 1 413 ? -12.534 -10.282 1.141   1.00 21.26 ? 413 GLU A N   1 
ATOM   1943 C CA  . GLU A 1 413 ? -11.435 -9.333  1.295   1.00 19.43 ? 413 GLU A CA  1 
ATOM   1944 C C   . GLU A 1 413 ? -10.394 -9.925  2.223   1.00 19.45 ? 413 GLU A C   1 
ATOM   1945 O O   . GLU A 1 413 ? -10.676 -10.827 3.012   1.00 19.84 ? 413 GLU A O   1 
ATOM   1946 C CB  . GLU A 1 413 ? -11.936 -7.989  1.889   1.00 20.38 ? 413 GLU A CB  1 
ATOM   1947 C CG  . GLU A 1 413 ? -12.804 -7.178  0.940   1.00 23.98 ? 413 GLU A CG  1 
ATOM   1948 C CD  . GLU A 1 413 ? -13.515 -5.989  1.557   1.00 27.10 ? 413 GLU A CD  1 
ATOM   1949 O OE1 . GLU A 1 413 ? -13.255 -5.671  2.741   1.00 26.47 ? 413 GLU A OE1 1 
ATOM   1950 O OE2 . GLU A 1 413 ? -14.320 -5.357  0.843   1.00 27.80 ? 413 GLU A OE2 1 
ATOM   1951 N N   . LEU A 1 414 ? -9.186  -9.377  2.166   1.00 18.41 ? 414 LEU A N   1 
ATOM   1952 C CA  . LEU A 1 414 ? -8.119  -9.750  3.086   1.00 19.66 ? 414 LEU A CA  1 
ATOM   1953 C C   . LEU A 1 414 ? -7.676  -8.473  3.810   1.00 18.73 ? 414 LEU A C   1 
ATOM   1954 O O   . LEU A 1 414 ? -7.780  -7.388  3.250   1.00 18.84 ? 414 LEU A O   1 
ATOM   1955 C CB  . LEU A 1 414 ? -6.898  -10.266 2.317   1.00 22.07 ? 414 LEU A CB  1 
ATOM   1956 C CG  . LEU A 1 414 ? -7.018  -11.584 1.616   1.00 27.32 ? 414 LEU A CG  1 
ATOM   1957 C CD1 . LEU A 1 414 ? -7.468  -11.363 0.184   1.00 28.31 ? 414 LEU A CD1 1 
ATOM   1958 C CD2 . LEU A 1 414 ? -5.669  -12.277 1.619   1.00 29.21 ? 414 LEU A CD2 1 
ATOM   1959 N N   . ILE A 1 415 ? -7.134  -8.600  5.012   1.00 17.18 ? 415 ILE A N   1 
ATOM   1960 C CA  . ILE A 1 415 ? -6.564  -7.464  5.729   1.00 16.86 ? 415 ILE A CA  1 
ATOM   1961 C C   . ILE A 1 415 ? -5.170  -7.851  6.209   1.00 16.73 ? 415 ILE A C   1 
ATOM   1962 O O   . ILE A 1 415 ? -4.968  -8.975  6.694   1.00 16.73 ? 415 ILE A O   1 
ATOM   1963 C CB  . ILE A 1 415 ? -7.471  -6.952  6.862   1.00 17.83 ? 415 ILE A CB  1 
ATOM   1964 C CG1 . ILE A 1 415 ? -6.923  -5.623  7.420   1.00 18.26 ? 415 ILE A CG1 1 
ATOM   1965 C CG2 . ILE A 1 415 ? -7.664  -8.008  7.963   1.00 18.44 ? 415 ILE A CG2 1 
ATOM   1966 C CD1 . ILE A 1 415 ? -7.932  -4.966  8.427   1.00 19.19 ? 415 ILE A CD1 1 
ATOM   1967 N N   . SER A 1 416 ? -4.208  -6.952  6.053   1.00 15.72 ? 416 SER A N   1 
ATOM   1968 C CA  . SER A 1 416 ? -2.812  -7.208  6.440   1.00 15.86 ? 416 SER A CA  1 
ATOM   1969 C C   . SER A 1 416 ? -2.296  -6.116  7.362   1.00 16.46 ? 416 SER A C   1 
ATOM   1970 O O   . SER A 1 416 ? -2.801  -4.998  7.292   1.00 17.38 ? 416 SER A O   1 
ATOM   1971 C CB  . SER A 1 416 ? -1.930  -7.346  5.204   1.00 16.36 ? 416 SER A CB  1 
ATOM   1972 O OG  . SER A 1 416 ? -2.055  -6.206  4.363   1.00 18.07 ? 416 SER A OG  1 
ATOM   1973 N N   . GLY A 1 417 ? -1.332  -6.444  8.231   1.00 16.61 ? 417 GLY A N   1 
ATOM   1974 C CA  . GLY A 1 417 ? -0.751  -5.508  9.191   1.00 17.13 ? 417 GLY A CA  1 
ATOM   1975 C C   . GLY A 1 417 ? 0.701   -5.248  8.839   1.00 18.28 ? 417 GLY A C   1 
ATOM   1976 O O   . GLY A 1 417 ? 1.377   -6.127  8.296   1.00 18.05 ? 417 GLY A O   1 
ATOM   1977 N N   . HIS A 1 418 ? 1.154   -4.028  9.062   1.00 17.77 ? 418 HIS A N   1 
ATOM   1978 C CA  . HIS A 1 418 ? 2.471   -3.603  8.589   1.00 18.58 ? 418 HIS A CA  1 
ATOM   1979 C C   . HIS A 1 418 ? 3.265   -2.760  9.567   1.00 20.21 ? 418 HIS A C   1 
ATOM   1980 O O   . HIS A 1 418 ? 2.777   -2.402  10.637  1.00 21.08 ? 418 HIS A O   1 
ATOM   1981 C CB  . HIS A 1 418 ? 2.287   -2.828  7.267   1.00 18.36 ? 418 HIS A CB  1 
ATOM   1982 C CG  . HIS A 1 418 ? 1.543   -3.610  6.235   1.00 18.80 ? 418 HIS A CG  1 
ATOM   1983 N ND1 . HIS A 1 418 ? 2.152   -4.644  5.521   1.00 19.17 ? 418 HIS A ND1 1 
ATOM   1984 C CD2 . HIS A 1 418 ? 0.223   -3.586  5.934   1.00 19.67 ? 418 HIS A CD2 1 
ATOM   1985 C CE1 . HIS A 1 418 ? 1.186   -5.192  4.794   1.00 20.07 ? 418 HIS A CE1 1 
ATOM   1986 N NE2 . HIS A 1 418 ? 0.020   -4.565  4.974   1.00 19.96 ? 418 HIS A NE2 1 
ATOM   1987 N N   . GLY A 1 419 ? 4.529   -2.519  9.196   1.00 21.50 ? 419 GLY A N   1 
ATOM   1988 C CA  . GLY A 1 419 ? 5.466   -1.734  9.968   1.00 23.24 ? 419 GLY A CA  1 
ATOM   1989 C C   . GLY A 1 419 ? 5.884   -0.476  9.233   1.00 24.71 ? 419 GLY A C   1 
ATOM   1990 O O   . GLY A 1 419 ? 5.049   0.213   8.650   1.00 24.62 ? 419 GLY A O   1 
ATOM   1991 N N   . PHE A 1 420 ? 7.191   -0.178  9.222   1.00 25.41 ? 420 PHE A N   1 
ATOM   1992 C CA  . PHE A 1 420 ? 7.753   1.021   8.582   1.00 27.30 ? 420 PHE A CA  1 
ATOM   1993 C C   . PHE A 1 420 ? 7.313   1.109   7.116   1.00 27.59 ? 420 PHE A C   1 
ATOM   1994 O O   . PHE A 1 420 ? 7.328   0.094   6.436   1.00 26.71 ? 420 PHE A O   1 
ATOM   1995 C CB  . PHE A 1 420 ? 9.292   0.970   8.688   1.00 28.66 ? 420 PHE A CB  1 
ATOM   1996 C CG  . PHE A 1 420 ? 10.010  2.192   8.161   1.00 31.71 ? 420 PHE A CG  1 
ATOM   1997 C CD1 . PHE A 1 420 ? 10.374  2.279   6.832   1.00 33.54 ? 420 PHE A CD1 1 
ATOM   1998 C CD2 . PHE A 1 420 ? 10.305  3.254   8.996   1.00 33.52 ? 420 PHE A CD2 1 
ATOM   1999 C CE1 . PHE A 1 420 ? 11.043  3.399   6.353   1.00 34.65 ? 420 PHE A CE1 1 
ATOM   2000 C CE2 . PHE A 1 420 ? 10.962  4.373   8.514   1.00 35.01 ? 420 PHE A CE2 1 
ATOM   2001 C CZ  . PHE A 1 420 ? 11.317  4.441   7.191   1.00 34.99 ? 420 PHE A CZ  1 
ATOM   2002 N N   . ALA A 1 421 ? 6.857   2.278   6.640   1.00 28.68 ? 421 ALA A N   1 
ATOM   2003 C CA  . ALA A 1 421 ? 6.864   3.548   7.374   1.00 29.59 ? 421 ALA A CA  1 
ATOM   2004 C C   . ALA A 1 421 ? 5.519   3.982   7.934   1.00 29.48 ? 421 ALA A C   1 
ATOM   2005 O O   . ALA A 1 421 ? 5.485   4.875   8.786   1.00 29.95 ? 421 ALA A O   1 
ATOM   2006 C CB  . ALA A 1 421 ? 7.390   4.642   6.461   1.00 30.10 ? 421 ALA A CB  1 
ATOM   2007 N N   . GLN A 1 422 ? 4.418   3.386   7.461   1.00 28.08 ? 422 GLN A N   1 
ATOM   2008 C CA  . GLN A 1 422 ? 3.088   3.849   7.852   1.00 28.09 ? 422 GLN A CA  1 
ATOM   2009 C C   . GLN A 1 422 ? 2.422   3.132   9.022   1.00 26.50 ? 422 GLN A C   1 
ATOM   2010 O O   . GLN A 1 422 ? 1.435   3.657   9.537   1.00 26.15 ? 422 GLN A O   1 
ATOM   2011 C CB  . GLN A 1 422 ? 2.148   3.818   6.637   1.00 31.00 ? 422 GLN A CB  1 
ATOM   2012 C CG  . GLN A 1 422 ? 2.603   4.737   5.494   1.00 38.06 ? 422 GLN A CG  1 
ATOM   2013 C CD  . GLN A 1 422 ? 2.728   6.182   5.910   1.00 48.31 ? 422 GLN A CD  1 
ATOM   2014 O OE1 . GLN A 1 422 ? 1.836   6.761   6.554   1.00 51.69 ? 422 GLN A OE1 1 
ATOM   2015 N NE2 . GLN A 1 422 ? 3.846   6.809   5.542   1.00 50.94 ? 422 GLN A NE2 1 
ATOM   2016 N N   . ASN A 1 423 ? 2.901   1.932   9.422   1.00 24.33 ? 423 ASN A N   1 
ATOM   2017 C CA  . ASN A 1 423 ? 2.336   1.160   10.559  1.00 22.44 ? 423 ASN A CA  1 
ATOM   2018 C C   . ASN A 1 423 ? 0.822   0.993   10.408  1.00 22.81 ? 423 ASN A C   1 
ATOM   2019 O O   . ASN A 1 423 ? 0.059   1.177   11.360  1.00 24.19 ? 423 ASN A O   1 
ATOM   2020 C CB  . ASN A 1 423 ? 2.656   1.862   11.886  1.00 22.74 ? 423 ASN A CB  1 
ATOM   2021 C CG  . ASN A 1 423 ? 4.130   2.092   12.050  1.00 24.63 ? 423 ASN A CG  1 
ATOM   2022 O OD1 . ASN A 1 423 ? 4.930   1.198   11.801  1.00 24.14 ? 423 ASN A OD1 1 
ATOM   2023 N ND2 . ASN A 1 423 ? 4.516   3.281   12.480  1.00 26.60 ? 423 ASN A ND2 1 
ATOM   2024 N N   . GLN A 1 424 ? 0.399   0.707   9.185   1.00 21.56 ? 424 GLN A N   1 
ATOM   2025 C CA  . GLN A 1 424 ? -1.018  0.649   8.870   1.00 21.54 ? 424 GLN A CA  1 
ATOM   2026 C C   . GLN A 1 424 ? -1.546  -0.752  8.648   1.00 20.92 ? 424 GLN A C   1 
ATOM   2027 O O   . GLN A 1 424 ? -0.783  -1.718  8.517   1.00 20.87 ? 424 GLN A O   1 
ATOM   2028 C CB  . GLN A 1 424 ? -1.256  1.551   7.619   1.00 22.76 ? 424 GLN A CB  1 
ATOM   2029 C CG  . GLN A 1 424 ? -1.080  0.891   6.232   1.00 24.99 ? 424 GLN A CG  1 
ATOM   2030 C CD  . GLN A 1 424 ? 0.345   0.674   5.765   1.00 29.59 ? 424 GLN A CD  1 
ATOM   2031 O OE1 . GLN A 1 424 ? 1.285   0.520   6.556   1.00 30.20 ? 424 GLN A OE1 1 
ATOM   2032 N NE2 . GLN A 1 424 ? 0.541   0.659   4.437   1.00 31.08 ? 424 GLN A NE2 1 
ATOM   2033 N N   . LEU A 1 425 ? -2.883  -0.865  8.602   1.00 18.72 ? 425 LEU A N   1 
ATOM   2034 C CA  . LEU A 1 425 ? -3.520  -2.092  8.160   1.00 18.81 ? 425 LEU A CA  1 
ATOM   2035 C C   . LEU A 1 425 ? -4.010  -1.787  6.723   1.00 19.03 ? 425 LEU A C   1 
ATOM   2036 O O   . LEU A 1 425 ? -4.468  -0.671  6.433   1.00 19.44 ? 425 LEU A O   1 
ATOM   2037 C CB  . LEU A 1 425 ? -4.716  -2.496  9.042   1.00 18.82 ? 425 LEU A CB  1 
ATOM   2038 C CG  . LEU A 1 425 ? -4.380  -2.973  10.483  1.00 21.84 ? 425 LEU A CG  1 
ATOM   2039 C CD1 . LEU A 1 425 ? -3.988  -1.821  11.356  1.00 22.91 ? 425 LEU A CD1 1 
ATOM   2040 C CD2 . LEU A 1 425 ? -5.631  -3.571  11.135  1.00 22.56 ? 425 LEU A CD2 1 
ATOM   2041 N N   . VAL A 1 426 ? -3.906  -2.758  5.830   1.00 17.45 ? 426 VAL A N   1 
ATOM   2042 C CA  . VAL A 1 426 ? -4.389  -2.576  4.465   1.00 17.64 ? 426 VAL A CA  1 
ATOM   2043 C C   . VAL A 1 426 ? -5.486  -3.582  4.185   1.00 17.92 ? 426 VAL A C   1 
ATOM   2044 O O   . VAL A 1 426 ? -5.315  -4.767  4.482   1.00 17.61 ? 426 VAL A O   1 
ATOM   2045 C CB  . VAL A 1 426 ? -3.262  -2.718  3.431   1.00 18.91 ? 426 VAL A CB  1 
ATOM   2046 C CG1 . VAL A 1 426 ? -3.822  -2.551  2.017   1.00 19.11 ? 426 VAL A CG1 1 
ATOM   2047 C CG2 . VAL A 1 426 ? -2.143  -1.710  3.695   1.00 18.76 ? 426 VAL A CG2 1 
ATOM   2048 N N   . ILE A 1 427 ? -6.616  -3.121  3.651   1.00 18.14 ? 427 ILE A N   1 
ATOM   2049 C CA  . ILE A 1 427 ? -7.678  -4.012  3.238   1.00 18.72 ? 427 ILE A CA  1 
ATOM   2050 C C   . ILE A 1 427 ? -7.583  -4.215  1.736   1.00 18.97 ? 427 ILE A C   1 
ATOM   2051 O O   . ILE A 1 427 ? -7.460  -3.254  0.992   1.00 19.29 ? 427 ILE A O   1 
ATOM   2052 C CB  . ILE A 1 427 ? -9.052  -3.481  3.663   1.00 19.93 ? 427 ILE A CB  1 
ATOM   2053 C CG1 . ILE A 1 427 ? -9.082  -3.354  5.214   1.00 21.38 ? 427 ILE A CG1 1 
ATOM   2054 C CG2 . ILE A 1 427 ? -10.145 -4.414  3.160   1.00 20.68 ? 427 ILE A CG2 1 
ATOM   2055 C CD1 . ILE A 1 427 ? -10.342 -2.700  5.745   1.00 23.04 ? 427 ILE A CD1 1 
ATOM   2056 N N   . TRP A 1 428 ? -7.615  -5.466  1.289   1.00 18.25 ? 428 TRP A N   1 
ATOM   2057 C CA  . TRP A 1 428 ? -7.510  -5.810  -0.123  1.00 18.44 ? 428 TRP A CA  1 
ATOM   2058 C C   . TRP A 1 428 ? -8.752  -6.536  -0.605  1.00 20.20 ? 428 TRP A C   1 
ATOM   2059 O O   . TRP A 1 428 ? -9.267  -7.389  0.106   1.00 20.25 ? 428 TRP A O   1 
ATOM   2060 C CB  . TRP A 1 428 ? -6.342  -6.779  -0.326  1.00 18.24 ? 428 TRP A CB  1 
ATOM   2061 C CG  . TRP A 1 428 ? -5.047  -6.364  0.310   1.00 17.95 ? 428 TRP A CG  1 
ATOM   2062 C CD1 . TRP A 1 428 ? -4.660  -6.598  1.595   1.00 18.83 ? 428 TRP A CD1 1 
ATOM   2063 C CD2 . TRP A 1 428 ? -3.931  -5.727  -0.338  1.00 18.93 ? 428 TRP A CD2 1 
ATOM   2064 N NE1 . TRP A 1 428 ? -3.378  -6.133  1.793   1.00 19.27 ? 428 TRP A NE1 1 
ATOM   2065 C CE2 . TRP A 1 428 ? -2.916  -5.579  0.627   1.00 19.49 ? 428 TRP A CE2 1 
ATOM   2066 C CE3 . TRP A 1 428 ? -3.692  -5.286  -1.645  1.00 20.37 ? 428 TRP A CE3 1 
ATOM   2067 C CZ2 . TRP A 1 428 ? -1.664  -5.033  0.315   1.00 21.64 ? 428 TRP A CZ2 1 
ATOM   2068 C CZ3 . TRP A 1 428 ? -2.481  -4.682  -1.938  1.00 21.75 ? 428 TRP A CZ3 1 
ATOM   2069 C CH2 . TRP A 1 428 ? -1.488  -4.544  -0.961  1.00 22.03 ? 428 TRP A CH2 1 
ATOM   2070 N N   . LYS A 1 429 ? -9.162  -6.293  -1.850  1.00 21.55 ? 429 LYS A N   1 
ATOM   2071 C CA  . LYS A 1 429 ? -10.310 -6.980  -2.417  1.00 22.69 ? 429 LYS A CA  1 
ATOM   2072 C C   . LYS A 1 429 ? -9.808  -8.271  -3.039  1.00 23.78 ? 429 LYS A C   1 
ATOM   2073 O O   . LYS A 1 429 ? -8.810  -8.248  -3.747  1.00 24.63 ? 429 LYS A O   1 
ATOM   2074 C CB  . LYS A 1 429 ? -10.956 -6.123  -3.505  1.00 25.58 ? 429 LYS A CB  1 
ATOM   2075 C CG  . LYS A 1 429 ? -12.245 -6.710  -4.056  1.00 31.88 ? 429 LYS A CG  1 
ATOM   2076 C CD  . LYS A 1 429 ? -13.335 -6.836  -2.994  1.00 38.67 ? 429 LYS A CD  1 
ATOM   2077 C CE  . LYS A 1 429 ? -14.323 -7.894  -3.421  1.00 43.31 ? 429 LYS A CE  1 
ATOM   2078 N NZ  . LYS A 1 429 ? -15.275 -8.256  -2.347  1.00 45.26 ? 429 LYS A NZ  1 
ATOM   2079 N N   . TYR A 1 430 ? -10.476 -9.383  -2.783  1.00 23.39 ? 430 TYR A N   1 
ATOM   2080 C CA  . TYR A 1 430 ? -10.099 -10.665 -3.369  1.00 23.26 ? 430 TYR A CA  1 
ATOM   2081 C C   . TYR A 1 430 ? -11.154 -11.059 -4.437  1.00 23.19 ? 430 TYR A C   1 
ATOM   2082 O O   . TYR A 1 430 ? -12.348 -10.835 -4.200  1.00 23.25 ? 430 TYR A O   1 
ATOM   2083 C CB  . TYR A 1 430 ? -10.029 -11.694 -2.257  1.00 23.52 ? 430 TYR A CB  1 
ATOM   2084 C CG  . TYR A 1 430 ? -9.529  -13.042 -2.718  1.00 25.65 ? 430 TYR A CG  1 
ATOM   2085 C CD1 . TYR A 1 430 ? -8.171  -13.306 -2.811  1.00 27.40 ? 430 TYR A CD1 1 
ATOM   2086 C CD2 . TYR A 1 430 ? -10.412 -14.024 -3.126  1.00 27.65 ? 430 TYR A CD2 1 
ATOM   2087 C CE1 . TYR A 1 430 ? -7.707  -14.539 -3.252  1.00 29.59 ? 430 TYR A CE1 1 
ATOM   2088 C CE2 . TYR A 1 430 ? -9.962  -15.257 -3.573  1.00 29.69 ? 430 TYR A CE2 1 
ATOM   2089 C CZ  . TYR A 1 430 ? -8.609  -15.518 -3.612  1.00 31.00 ? 430 TYR A CZ  1 
ATOM   2090 O OH  . TYR A 1 430 ? -8.176  -16.733 -4.078  1.00 35.05 ? 430 TYR A OH  1 
ATOM   2091 N N   . PRO A 1 431 ? -10.775 -11.552 -5.648  1.00 23.57 ? 431 PRO A N   1 
ATOM   2092 C CA  . PRO A 1 431 ? -9.435  -11.982 -6.082  1.00 23.43 ? 431 PRO A CA  1 
ATOM   2093 C C   . PRO A 1 431 ? -8.561  -10.983 -6.830  1.00 24.01 ? 431 PRO A C   1 
ATOM   2094 O O   . PRO A 1 431 ? -7.416  -11.326 -7.166  1.00 24.24 ? 431 PRO A O   1 
ATOM   2095 C CB  . PRO A 1 431 ? -9.750  -13.183 -6.984  1.00 23.92 ? 431 PRO A CB  1 
ATOM   2096 C CG  . PRO A 1 431 ? -11.043 -12.788 -7.665  1.00 25.12 ? 431 PRO A CG  1 
ATOM   2097 C CD  . PRO A 1 431 ? -11.812 -11.968 -6.618  1.00 23.46 ? 431 PRO A CD  1 
ATOM   2098 N N   . THR A 1 432 ? -9.038  -9.749  -7.062  1.00 23.71 ? 432 THR A N   1 
ATOM   2099 C CA  . THR A 1 432 ? -8.242  -8.765  -7.802  1.00 24.70 ? 432 THR A CA  1 
ATOM   2100 C C   . THR A 1 432 ? -6.991  -8.300  -7.095  1.00 24.23 ? 432 THR A C   1 
ATOM   2101 O O   . THR A 1 432 ? -6.049  -7.838  -7.757  1.00 24.47 ? 432 THR A O   1 
ATOM   2102 C CB  . THR A 1 432 ? -9.094  -7.557  -8.173  1.00 28.72 ? 432 THR A CB  1 
ATOM   2103 O OG1 . THR A 1 432 ? -9.510  -6.894  -6.973  1.00 30.03 ? 432 THR A OG1 1 
ATOM   2104 C CG2 . THR A 1 432 ? -10.286 -7.925  -9.064  1.00 30.73 ? 432 THR A CG2 1 
ATOM   2105 N N   . MET A 1 433 ? -6.964  -8.418  -5.749  1.00 22.90 ? 433 MET A N   1 
ATOM   2106 C CA  . MET A 1 433 ? -5.874  -7.913  -4.922  1.00 24.24 ? 433 MET A CA  1 
ATOM   2107 C C   . MET A 1 433 ? -5.727  -6.382  -5.072  1.00 25.96 ? 433 MET A C   1 
ATOM   2108 O O   . MET A 1 433 ? -4.636  -5.847  -4.910  1.00 27.28 ? 433 MET A O   1 
ATOM   2109 C CB  . MET A 1 433 ? -4.549  -8.672  -5.123  1.00 25.22 ? 433 MET A CB  1 
ATOM   2110 C CG  . MET A 1 433 ? -4.597  -10.142 -4.695  1.00 28.91 ? 433 MET A CG  1 
ATOM   2111 S SD  . MET A 1 433 ? -5.136  -10.413 -2.970  1.00 35.17 ? 433 MET A SD  1 
ATOM   2112 C CE  . MET A 1 433 ? -3.855  -9.613  -2.093  1.00 32.22 ? 433 MET A CE  1 
ATOM   2113 N N   . ALA A 1 434 ? -6.832  -5.684  -5.355  1.00 26.65 ? 434 ALA A N   1 
ATOM   2114 C CA  . ALA A 1 434 ? -6.863  -4.225  -5.414  1.00 27.74 ? 434 ALA A CA  1 
ATOM   2115 C C   . ALA A 1 434 ? -6.915  -3.716  -3.964  1.00 28.12 ? 434 ALA A C   1 
ATOM   2116 O O   . ALA A 1 434 ? -7.581  -4.306  -3.118  1.00 27.49 ? 434 ALA A O   1 
ATOM   2117 C CB  . ALA A 1 434 ? -8.109  -3.762  -6.147  1.00 28.36 ? 434 ALA A CB  1 
ATOM   2118 N N   . LYS A 1 435 ? -6.261  -2.601  -3.691  1.00 28.64 ? 435 LYS A N   1 
ATOM   2119 C CA  . LYS A 1 435 ? -6.236  -2.014  -2.351  1.00 30.10 ? 435 LYS A CA  1 
ATOM   2120 C C   . LYS A 1 435 ? -7.561  -1.278  -2.149  1.00 31.08 ? 435 LYS A C   1 
ATOM   2121 O O   . LYS A 1 435 ? -7.894  -0.408  -2.949  1.00 32.09 ? 435 LYS A O   1 
ATOM   2122 C CB  . LYS A 1 435 ? -5.049  -1.043  -2.300  1.00 32.71 ? 435 LYS A CB  1 
ATOM   2123 C CG  . LYS A 1 435 ? -4.520  -0.639  -0.943  1.00 37.22 ? 435 LYS A CG  1 
ATOM   2124 C CD  . LYS A 1 435 ? -3.102  -0.090  -1.140  1.00 43.41 ? 435 LYS A CD  1 
ATOM   2125 C CE  . LYS A 1 435 ? -2.318  0.149   0.122   1.00 48.90 ? 435 LYS A CE  1 
ATOM   2126 N NZ  . LYS A 1 435 ? -0.890  0.486   -0.166  1.00 51.71 ? 435 LYS A NZ  1 
ATOM   2127 N N   . VAL A 1 436 ? -8.327  -1.637  -1.105  1.00 30.70 ? 436 VAL A N   1 
ATOM   2128 C CA  . VAL A 1 436 ? -9.643  -1.059  -0.799  1.00 31.16 ? 436 VAL A CA  1 
ATOM   2129 C C   . VAL A 1 436 ? -9.522  0.134   0.149   1.00 30.16 ? 436 VAL A C   1 
ATOM   2130 O O   . VAL A 1 436 ? -10.235 1.146   -0.006  1.00 30.75 ? 436 VAL A O   1 
ATOM   2131 C CB  . VAL A 1 436 ? -10.557 -2.154  -0.174  1.00 33.01 ? 436 VAL A CB  1 
ATOM   2132 C CG1 . VAL A 1 436 ? -11.862 -1.565  0.358   1.00 34.75 ? 436 VAL A CG1 1 
ATOM   2133 C CG2 . VAL A 1 436 ? -10.852 -3.248  -1.184  1.00 33.73 ? 436 VAL A CG2 1 
ATOM   2134 N N   . ALA A 1 437 ? -8.664  -0.006  1.167   1.00 28.22 ? 437 ALA A N   1 
ATOM   2135 C CA  . ALA A 1 437 ? -8.523  1.003   2.220   1.00 27.10 ? 437 ALA A CA  1 
ATOM   2136 C C   . ALA A 1 437 ? -7.239  0.809   3.043   1.00 25.29 ? 437 ALA A C   1 
ATOM   2137 O O   . ALA A 1 437 ? -6.659  -0.279  3.043   1.00 24.44 ? 437 ALA A O   1 
ATOM   2138 C CB  . ALA A 1 437 ? -9.748  0.930   3.155   1.00 27.34 ? 437 ALA A CB  1 
ATOM   2139 N N   . GLU A 1 438 ? -6.835  1.853   3.808   1.00 23.98 ? 438 GLU A N   1 
ATOM   2140 C CA  . GLU A 1 438 ? -5.714  1.778   4.724   1.00 23.96 ? 438 GLU A CA  1 
ATOM   2141 C C   . GLU A 1 438 ? -6.195  2.327   6.052   1.00 24.41 ? 438 GLU A C   1 
ATOM   2142 O O   . GLU A 1 438 ? -6.784  3.411   6.103   1.00 25.31 ? 438 GLU A O   1 
ATOM   2143 C CB  . GLU A 1 438 ? -4.515  2.594   4.228   1.00 26.78 ? 438 GLU A CB  1 
ATOM   2144 C CG  . GLU A 1 438 ? -3.836  1.947   3.042   1.00 32.72 ? 438 GLU A CG  1 
ATOM   2145 C CD  . GLU A 1 438 ? -2.592  2.682   2.602   1.00 41.35 ? 438 GLU A CD  1 
ATOM   2146 O OE1 . GLU A 1 438 ? -2.736  3.708   1.895   1.00 45.06 ? 438 GLU A OE1 1 
ATOM   2147 O OE2 . GLU A 1 438 ? -1.478  2.236   2.959   1.00 40.96 ? 438 GLU A OE2 1 
ATOM   2148 N N   . LEU A 1 439 ? -5.978  1.568   7.125   1.00 22.88 ? 439 LEU A N   1 
ATOM   2149 C CA  . LEU A 1 439 ? -6.339  1.985   8.466   1.00 23.32 ? 439 LEU A CA  1 
ATOM   2150 C C   . LEU A 1 439 ? -5.083  2.481   9.167   1.00 23.73 ? 439 LEU A C   1 
ATOM   2151 O O   . LEU A 1 439 ? -4.198  1.696   9.499   1.00 23.66 ? 439 LEU A O   1 
ATOM   2152 C CB  . LEU A 1 439 ? -6.982  0.833   9.237   1.00 23.56 ? 439 LEU A CB  1 
ATOM   2153 C CG  . LEU A 1 439 ? -8.204  0.209   8.559   1.00 24.84 ? 439 LEU A CG  1 
ATOM   2154 C CD1 . LEU A 1 439 ? -8.698  -0.995  9.335   1.00 24.40 ? 439 LEU A CD1 1 
ATOM   2155 C CD2 . LEU A 1 439 ? -9.328  1.233   8.398   1.00 26.50 ? 439 LEU A CD2 1 
ATOM   2156 N N   . LYS A 1 440 ? -5.020  3.792   9.401   1.00 24.04 ? 440 LYS A N   1 
ATOM   2157 C CA  . LYS A 1 440 ? -3.867  4.433   10.019  1.00 24.86 ? 440 LYS A CA  1 
ATOM   2158 C C   . LYS A 1 440 ? -4.161  4.907   11.436  1.00 25.42 ? 440 LYS A C   1 
ATOM   2159 O O   . LYS A 1 440 ? -5.311  5.204   11.774  1.00 25.71 ? 440 LYS A O   1 
ATOM   2160 C CB  . LYS A 1 440 ? -3.405  5.621   9.145   1.00 27.37 ? 440 LYS A CB  1 
ATOM   2161 C CG  . LYS A 1 440 ? -2.836  5.137   7.815   1.00 32.39 ? 440 LYS A CG  1 
ATOM   2162 C CD  . LYS A 1 440 ? -2.286  6.270   6.939   1.00 38.13 ? 440 LYS A CD  1 
ATOM   2163 C CE  . LYS A 1 440 ? -1.870  5.739   5.583   1.00 43.56 ? 440 LYS A CE  1 
ATOM   2164 N NZ  . LYS A 1 440 ? -1.499  6.838   4.642   1.00 46.54 ? 440 LYS A NZ  1 
ATOM   2165 N N   . GLY A 1 441 ? -3.122  5.000   12.249  1.00 25.42 ? 441 GLY A N   1 
ATOM   2166 C CA  . GLY A 1 441 ? -3.281  5.469   13.619  1.00 26.50 ? 441 GLY A CA  1 
ATOM   2167 C C   . GLY A 1 441 ? -2.204  4.972   14.548  1.00 26.35 ? 441 GLY A C   1 
ATOM   2168 O O   . GLY A 1 441 ? -1.801  5.691   15.455  1.00 26.49 ? 441 GLY A O   1 
ATOM   2169 N N   . HIS A 1 442 ? -1.735  3.731   14.342  1.00 25.13 ? 442 HIS A N   1 
ATOM   2170 C CA  . HIS A 1 442 ? -0.649  3.179   15.161  1.00 25.15 ? 442 HIS A CA  1 
ATOM   2171 C C   . HIS A 1 442 ? 0.620   4.007   14.933  1.00 25.74 ? 442 HIS A C   1 
ATOM   2172 O O   . HIS A 1 442 ? 0.901   4.400   13.802  1.00 25.79 ? 442 HIS A O   1 
ATOM   2173 C CB  . HIS A 1 442 ? -0.377  1.702   14.815  1.00 24.19 ? 442 HIS A CB  1 
ATOM   2174 C CG  . HIS A 1 442 ? -1.325  0.729   15.458  1.00 22.52 ? 442 HIS A CG  1 
ATOM   2175 N ND1 . HIS A 1 442 ? -1.424  0.614   16.850  1.00 22.83 ? 442 HIS A ND1 1 
ATOM   2176 C CD2 . HIS A 1 442 ? -2.133  -0.193  14.886  1.00 22.47 ? 442 HIS A CD2 1 
ATOM   2177 C CE1 . HIS A 1 442 ? -2.282  -0.380  17.066  1.00 23.37 ? 442 HIS A CE1 1 
ATOM   2178 N NE2 . HIS A 1 442 ? -2.758  -0.873  15.918  1.00 22.62 ? 442 HIS A NE2 1 
ATOM   2179 N N   . THR A 1 443 ? 1.362   4.283   16.000  1.00 26.57 ? 443 THR A N   1 
ATOM   2180 C CA  . THR A 1 443 ? 2.585   5.092   15.895  1.00 27.63 ? 443 THR A CA  1 
ATOM   2181 C C   . THR A 1 443 ? 3.888   4.274   15.910  1.00 27.79 ? 443 THR A C   1 
ATOM   2182 O O   . THR A 1 443 ? 4.979   4.846   15.817  1.00 28.85 ? 443 THR A O   1 
ATOM   2183 C CB  . THR A 1 443 ? 2.583   6.149   16.968  1.00 30.10 ? 443 THR A CB  1 
ATOM   2184 O OG1 . THR A 1 443 ? 2.586   5.477   18.218  1.00 31.91 ? 443 THR A OG1 1 
ATOM   2185 C CG2 . THR A 1 443 ? 1.385   7.067   16.866  1.00 30.69 ? 443 THR A CG2 1 
ATOM   2186 N N   . SER A 1 444 ? 3.772   2.949   15.999  1.00 27.13 ? 444 SER A N   1 
ATOM   2187 C CA  . SER A 1 444 ? 4.857   1.984   15.904  1.00 27.03 ? 444 SER A CA  1 
ATOM   2188 C C   . SER A 1 444 ? 4.317   0.733   15.176  1.00 25.21 ? 444 SER A C   1 
ATOM   2189 O O   . SER A 1 444 ? 3.102   0.597   14.981  1.00 24.57 ? 444 SER A O   1 
ATOM   2190 C CB  . SER A 1 444 ? 5.463   1.675   17.274  1.00 29.98 ? 444 SER A CB  1 
ATOM   2191 O OG  . SER A 1 444 ? 6.133   2.816   17.794  1.00 34.75 ? 444 SER A OG  1 
ATOM   2192 N N   . ARG A 1 445 ? 5.208   -0.153  14.752  1.00 23.56 ? 445 ARG A N   1 
ATOM   2193 C CA  . ARG A 1 445 ? 4.830   -1.289  13.927  1.00 23.76 ? 445 ARG A CA  1 
ATOM   2194 C C   . ARG A 1 445 ? 3.755   -2.185  14.524  1.00 22.47 ? 445 ARG A C   1 
ATOM   2195 O O   . ARG A 1 445 ? 3.709   -2.417  15.735  1.00 22.42 ? 445 ARG A O   1 
ATOM   2196 C CB  . ARG A 1 445 ? 6.066   -2.105  13.568  1.00 25.54 ? 445 ARG A CB  1 
ATOM   2197 C CG  . ARG A 1 445 ? 6.648   -2.831  14.754  1.00 30.63 ? 445 ARG A CG  1 
ATOM   2198 C CD  . ARG A 1 445 ? 7.586   -3.912  14.300  1.00 34.57 ? 445 ARG A CD  1 
ATOM   2199 N NE  . ARG A 1 445 ? 8.332   -4.494  15.415  1.00 36.16 ? 445 ARG A NE  1 
ATOM   2200 C CZ  . ARG A 1 445 ? 9.318   -5.369  15.271  1.00 38.02 ? 445 ARG A CZ  1 
ATOM   2201 N NH1 . ARG A 1 445 ? 9.946   -5.848  16.335  1.00 36.04 ? 445 ARG A NH1 1 
ATOM   2202 N NH2 . ARG A 1 445 ? 9.677   -5.785  14.060  1.00 39.56 ? 445 ARG A NH2 1 
ATOM   2203 N N   . VAL A 1 446 ? 2.852   -2.646  13.660  1.00 21.43 ? 446 VAL A N   1 
ATOM   2204 C CA  . VAL A 1 446 ? 1.844   -3.608  14.040  1.00 21.17 ? 446 VAL A CA  1 
ATOM   2205 C C   . VAL A 1 446 ? 2.571   -4.944  14.235  1.00 21.17 ? 446 VAL A C   1 
ATOM   2206 O O   . VAL A 1 446 ? 3.497   -5.269  13.484  1.00 21.98 ? 446 VAL A O   1 
ATOM   2207 C CB  . VAL A 1 446 ? 0.757   -3.698  12.949  1.00 20.63 ? 446 VAL A CB  1 
ATOM   2208 C CG1 . VAL A 1 446 ? -0.297  -4.739  13.312  1.00 20.66 ? 446 VAL A CG1 1 
ATOM   2209 C CG2 . VAL A 1 446 ? 0.116   -2.320  12.727  1.00 20.28 ? 446 VAL A CG2 1 
ATOM   2210 N N   . LEU A 1 447 ? 2.201   -5.658  15.284  1.00 20.11 ? 447 LEU A N   1 
ATOM   2211 C CA  . LEU A 1 447 ? 2.766   -6.941  15.697  1.00 20.30 ? 447 LEU A CA  1 
ATOM   2212 C C   . LEU A 1 447 ? 1.896   -8.114  15.296  1.00 20.27 ? 447 LEU A C   1 
ATOM   2213 O O   . LEU A 1 447 ? 2.400   -9.091  14.753  1.00 21.34 ? 447 LEU A O   1 
ATOM   2214 C CB  . LEU A 1 447 ? 2.992   -6.949  17.231  1.00 20.82 ? 447 LEU A CB  1 
ATOM   2215 C CG  . LEU A 1 447 ? 4.093   -6.008  17.693  1.00 22.63 ? 447 LEU A CG  1 
ATOM   2216 C CD1 . LEU A 1 447 ? 4.114   -5.863  19.248  1.00 24.08 ? 447 LEU A CD1 1 
ATOM   2217 C CD2 . LEU A 1 447 ? 5.438   -6.463  17.157  1.00 23.46 ? 447 LEU A CD2 1 
ATOM   2218 N N   . SER A 1 448 ? 0.577   -8.025  15.528  1.00 19.03 ? 448 SER A N   1 
ATOM   2219 C CA  . SER A 1 448 ? -0.324  -9.141  15.235  1.00 19.95 ? 448 SER A CA  1 
ATOM   2220 C C   . SER A 1 448 ? -1.722  -8.619  14.989  1.00 18.64 ? 448 SER A C   1 
ATOM   2221 O O   . SER A 1 448 ? -2.090  -7.580  15.522  1.00 18.92 ? 448 SER A O   1 
ATOM   2222 C CB  . SER A 1 448 ? -0.446  -10.040 16.467  1.00 24.29 ? 448 SER A CB  1 
ATOM   2223 O OG  . SER A 1 448 ? 0.734   -10.790 16.706  1.00 31.90 ? 448 SER A OG  1 
ATOM   2224 N N   . LEU A 1 449 ? -2.499  -9.370  14.228  1.00 17.82 ? 449 LEU A N   1 
ATOM   2225 C CA  . LEU A 1 449 ? -3.923  -9.124  14.046  1.00 17.20 ? 449 LEU A CA  1 
ATOM   2226 C C   . LEU A 1 449 ? -4.684  -10.354 14.512  1.00 18.46 ? 449 LEU A C   1 
ATOM   2227 O O   . LEU A 1 449 ? -4.233  -11.497 14.345  1.00 19.38 ? 449 LEU A O   1 
ATOM   2228 C CB  . LEU A 1 449 ? -4.274  -8.918  12.564  1.00 17.08 ? 449 LEU A CB  1 
ATOM   2229 C CG  . LEU A 1 449 ? -3.545  -7.801  11.814  1.00 19.02 ? 449 LEU A CG  1 
ATOM   2230 C CD1 . LEU A 1 449 ? -4.089  -7.668  10.392  1.00 19.83 ? 449 LEU A CD1 1 
ATOM   2231 C CD2 . LEU A 1 449 ? -3.681  -6.480  12.537  1.00 19.67 ? 449 LEU A CD2 1 
ATOM   2232 N N   . THR A 1 450 ? -5.903  -10.126 14.993  1.00 17.11 ? 450 THR A N   1 
ATOM   2233 C CA  . THR A 1 450 ? -6.841  -11.209 15.292  1.00 16.57 ? 450 THR A CA  1 
ATOM   2234 C C   . THR A 1 450 ? -8.240  -10.725 14.955  1.00 17.53 ? 450 THR A C   1 
ATOM   2235 O O   . THR A 1 450 ? -8.501  -9.523  14.984  1.00 18.12 ? 450 THR A O   1 
ATOM   2236 C CB  . THR A 1 450 ? -6.685  -11.787 16.698  1.00 18.20 ? 450 THR A CB  1 
ATOM   2237 O OG1 . THR A 1 450 ? -7.536  -12.941 16.825  1.00 18.83 ? 450 THR A OG1 1 
ATOM   2238 C CG2 . THR A 1 450 ? -7.044  -10.786 17.779  1.00 17.91 ? 450 THR A CG2 1 
ATOM   2239 N N   . MET A 1 451 ? -9.128  -11.638 14.610  1.00 18.04 ? 451 MET A N   1 
ATOM   2240 C CA  . MET A 1 451 ? -10.489 -11.260 14.206  1.00 18.23 ? 451 MET A CA  1 
ATOM   2241 C C   . MET A 1 451 ? -11.552 -11.729 15.175  1.00 18.98 ? 451 MET A C   1 
ATOM   2242 O O   . MET A 1 451 ? -11.466 -12.837 15.698  1.00 18.82 ? 451 MET A O   1 
ATOM   2243 C CB  . MET A 1 451 ? -10.741 -11.834 12.804  1.00 18.84 ? 451 MET A CB  1 
ATOM   2244 C CG  . MET A 1 451 ? -12.115 -11.487 12.268  1.00 21.11 ? 451 MET A CG  1 
ATOM   2245 S SD  . MET A 1 451 ? -12.294 -12.097 10.588  1.00 25.13 ? 451 MET A SD  1 
ATOM   2246 C CE  . MET A 1 451 ? -11.426 -10.775 9.701   1.00 25.25 ? 451 MET A CE  1 
ATOM   2247 N N   . SER A 1 452 ? -12.606 -10.912 15.360  1.00 19.16 ? 452 SER A N   1 
ATOM   2248 C CA  . SER A 1 452 ? -13.714 -11.251 16.250  1.00 20.54 ? 452 SER A CA  1 
ATOM   2249 C C   . SER A 1 452 ? -14.493 -12.447 15.661  1.00 22.13 ? 452 SER A C   1 
ATOM   2250 O O   . SER A 1 452 ? -14.445 -12.699 14.453  1.00 21.03 ? 452 SER A O   1 
ATOM   2251 C CB  . SER A 1 452 ? -14.638 -10.045 16.409  1.00 21.70 ? 452 SER A CB  1 
ATOM   2252 O OG  . SER A 1 452 ? -15.205 -9.695  15.163  1.00 22.35 ? 452 SER A OG  1 
ATOM   2253 N N   . PRO A 1 453 ? -15.222 -13.197 16.507  1.00 23.76 ? 453 PRO A N   1 
ATOM   2254 C CA  . PRO A 1 453 ? -15.894 -14.409 16.007  1.00 25.01 ? 453 PRO A CA  1 
ATOM   2255 C C   . PRO A 1 453 ? -16.992 -14.127 14.980  1.00 26.25 ? 453 PRO A C   1 
ATOM   2256 O O   . PRO A 1 453 ? -17.265 -14.978 14.122  1.00 28.10 ? 453 PRO A O   1 
ATOM   2257 C CB  . PRO A 1 453 ? -16.398 -15.101 17.291  1.00 25.75 ? 453 PRO A CB  1 
ATOM   2258 C CG  . PRO A 1 453 ? -16.441 -14.011 18.331  1.00 25.90 ? 453 PRO A CG  1 
ATOM   2259 C CD  . PRO A 1 453 ? -15.305 -13.086 17.980  1.00 23.80 ? 453 PRO A CD  1 
ATOM   2260 N N   . ASP A 1 454 ? -17.596 -12.936 15.027  1.00 24.96 ? 454 ASP A N   1 
ATOM   2261 C CA  . ASP A 1 454 ? -18.587 -12.566 14.021  1.00 25.34 ? 454 ASP A CA  1 
ATOM   2262 C C   . ASP A 1 454 ? -17.968 -12.078 12.690  1.00 24.37 ? 454 ASP A C   1 
ATOM   2263 O O   . ASP A 1 454 ? -18.679 -11.943 11.704  1.00 26.16 ? 454 ASP A O   1 
ATOM   2264 C CB  . ASP A 1 454 ? -19.599 -11.562 14.561  1.00 27.75 ? 454 ASP A CB  1 
ATOM   2265 C CG  . ASP A 1 454 ? -19.048 -10.233 15.017  1.00 32.38 ? 454 ASP A CG  1 
ATOM   2266 O OD1 . ASP A 1 454 ? -17.824 -10.040 14.947  1.00 31.60 ? 454 ASP A OD1 1 
ATOM   2267 O OD2 . ASP A 1 454 ? -19.843 -9.396  15.473  1.00 36.64 ? 454 ASP A OD2 1 
ATOM   2268 N N   . GLY A 1 455 ? -16.666 -11.847 12.666  1.00 21.95 ? 455 GLY A N   1 
ATOM   2269 C CA  . GLY A 1 455 ? -15.957 -11.382 11.482  1.00 22.20 ? 455 GLY A CA  1 
ATOM   2270 C C   . GLY A 1 455 ? -15.993 -9.876  11.279  1.00 21.70 ? 455 GLY A C   1 
ATOM   2271 O O   . GLY A 1 455 ? -15.413 -9.377  10.314  1.00 21.92 ? 455 GLY A O   1 
ATOM   2272 N N   . ALA A 1 456 ? -16.643 -9.123  12.192  1.00 21.15 ? 456 ALA A N   1 
ATOM   2273 C CA  . ALA A 1 456 ? -16.818 -7.686  12.007  1.00 21.51 ? 456 ALA A CA  1 
ATOM   2274 C C   . ALA A 1 456 ? -15.630 -6.811  12.394  1.00 20.99 ? 456 ALA A C   1 
ATOM   2275 O O   . ALA A 1 456 ? -15.450 -5.726  11.842  1.00 21.42 ? 456 ALA A O   1 
ATOM   2276 C CB  . ALA A 1 456 ? -18.032 -7.246  12.812  1.00 22.99 ? 456 ALA A CB  1 
ATOM   2277 N N   . THR A 1 457 ? -14.846 -7.257  13.377  1.00 19.87 ? 457 THR A N   1 
ATOM   2278 C CA  . THR A 1 457 ? -13.802 -6.447  13.961  1.00 19.53 ? 457 THR A CA  1 
ATOM   2279 C C   . THR A 1 457 ? -12.454 -7.144  13.950  1.00 19.01 ? 457 THR A C   1 
ATOM   2280 O O   . THR A 1 457 ? -12.348 -8.364  14.193  1.00 19.36 ? 457 THR A O   1 
ATOM   2281 C CB  . THR A 1 457 ? -14.223 -6.103  15.415  1.00 21.87 ? 457 THR A CB  1 
ATOM   2282 O OG1 . THR A 1 457 ? -15.538 -5.523  15.415  1.00 24.01 ? 457 THR A OG1 1 
ATOM   2283 C CG2 . THR A 1 457 ? -13.272 -5.171  16.102  1.00 22.32 ? 457 THR A CG2 1 
ATOM   2284 N N   . VAL A 1 458 ? -11.429 -6.362  13.673  1.00 17.44 ? 458 VAL A N   1 
ATOM   2285 C CA  . VAL A 1 458 ? -10.048 -6.813  13.670  1.00 17.02 ? 458 VAL A CA  1 
ATOM   2286 C C   . VAL A 1 458 ? -9.320  -6.086  14.786  1.00 18.57 ? 458 VAL A C   1 
ATOM   2287 O O   . VAL A 1 458 ? -9.326  -4.849  14.806  1.00 19.44 ? 458 VAL A O   1 
ATOM   2288 C CB  . VAL A 1 458 ? -9.392  -6.517  12.293  1.00 17.29 ? 458 VAL A CB  1 
ATOM   2289 C CG1 . VAL A 1 458 ? -7.865  -6.739  12.332  1.00 17.49 ? 458 VAL A CG1 1 
ATOM   2290 C CG2 . VAL A 1 458 ? -10.046 -7.369  11.194  1.00 19.03 ? 458 VAL A CG2 1 
ATOM   2291 N N   . ALA A 1 459 ? -8.659  -6.828  15.681  1.00 17.37 ? 459 ALA A N   1 
ATOM   2292 C CA  . ALA A 1 459 ? -7.839  -6.214  16.710  1.00 17.27 ? 459 ALA A CA  1 
ATOM   2293 C C   . ALA A 1 459 ? -6.396  -6.222  16.226  1.00 17.49 ? 459 ALA A C   1 
ATOM   2294 O O   . ALA A 1 459 ? -5.907  -7.265  15.814  1.00 17.33 ? 459 ALA A O   1 
ATOM   2295 C CB  . ALA A 1 459 ? -7.931  -7.028  17.978  1.00 17.15 ? 459 ALA A CB  1 
ATOM   2296 N N   . SER A 1 460 ? -5.742  -5.083  16.269  1.00 16.86 ? 460 SER A N   1 
ATOM   2297 C CA  . SER A 1 460 ? -4.343  -4.975  15.880  1.00 17.43 ? 460 SER A CA  1 
ATOM   2298 C C   . SER A 1 460 ? -3.566  -4.647  17.139  1.00 18.73 ? 460 SER A C   1 
ATOM   2299 O O   . SER A 1 460 ? -3.884  -3.671  17.817  1.00 20.18 ? 460 SER A O   1 
ATOM   2300 C CB  . SER A 1 460 ? -4.170  -3.890  14.813  1.00 18.81 ? 460 SER A CB  1 
ATOM   2301 O OG  . SER A 1 460 ? -4.615  -2.588  15.185  1.00 20.10 ? 460 SER A OG  1 
ATOM   2302 N N   . ALA A 1 461 ? -2.526  -5.414  17.439  1.00 19.20 ? 461 ALA A N   1 
ATOM   2303 C CA  . ALA A 1 461 ? -1.682  -5.170  18.598  1.00 20.40 ? 461 ALA A CA  1 
ATOM   2304 C C   . ALA A 1 461 ? -0.403  -4.579  18.003  1.00 20.65 ? 461 ALA A C   1 
ATOM   2305 O O   . ALA A 1 461 ? 0.101   -5.121  17.014  1.00 19.64 ? 461 ALA A O   1 
ATOM   2306 C CB  . ALA A 1 461 ? -1.356  -6.495  19.287  1.00 21.16 ? 461 ALA A CB  1 
ATOM   2307 N N   . ALA A 1 462 ? 0.089   -3.487  18.569  1.00 20.51 ? 462 ALA A N   1 
ATOM   2308 C CA  . ALA A 1 462 ? 1.258   -2.819  18.009  1.00 22.01 ? 462 ALA A CA  1 
ATOM   2309 C C   . ALA A 1 462 ? 2.294   -2.473  19.066  1.00 22.58 ? 462 ALA A C   1 
ATOM   2310 O O   . ALA A 1 462 ? 1.988   -2.402  20.254  1.00 23.30 ? 462 ALA A O   1 
ATOM   2311 C CB  . ALA A 1 462 ? 0.806   -1.556  17.264  1.00 22.82 ? 462 ALA A CB  1 
ATOM   2312 N N   . ALA A 1 463 ? 3.527   -2.208  18.624  1.00 23.23 ? 463 ALA A N   1 
ATOM   2313 C CA  . ALA A 1 463 ? 4.639   -1.813  19.480  1.00 24.11 ? 463 ALA A CA  1 
ATOM   2314 C C   . ALA A 1 463 ? 4.448   -0.438  20.168  1.00 25.26 ? 463 ALA A C   1 
ATOM   2315 O O   . ALA A 1 463 ? 5.268   -0.047  21.014  1.00 26.09 ? 463 ALA A O   1 
ATOM   2316 C CB  . ALA A 1 463 ? 5.916   -1.833  18.665  1.00 24.22 ? 463 ALA A CB  1 
ATOM   2317 N N   . ASP A 1 464 ? 3.374   0.296   19.823  1.00 24.87 ? 464 ASP A N   1 
ATOM   2318 C CA  . ASP A 1 464 ? 3.072   1.555   20.494  1.00 25.50 ? 464 ASP A CA  1 
ATOM   2319 C C   . ASP A 1 464 ? 2.290   1.323   21.807  1.00 25.62 ? 464 ASP A C   1 
ATOM   2320 O O   . ASP A 1 464 ? 1.699   2.271   22.304  1.00 26.51 ? 464 ASP A O   1 
ATOM   2321 C CB  . ASP A 1 464 ? 2.276   2.493   19.572  1.00 26.64 ? 464 ASP A CB  1 
ATOM   2322 C CG  . ASP A 1 464 ? 0.959   1.937   19.065  1.00 27.63 ? 464 ASP A CG  1 
ATOM   2323 O OD1 . ASP A 1 464 ? 0.523   0.889   19.573  1.00 27.90 ? 464 ASP A OD1 1 
ATOM   2324 O OD2 . ASP A 1 464 ? 0.366   2.555   18.161  1.00 27.52 ? 464 ASP A OD2 1 
ATOM   2325 N N   . GLU A 1 465 ? 2.168   0.044   22.264  1.00 24.83 ? 465 GLU A N   1 
ATOM   2326 C CA  . GLU A 1 465 ? 1.496   -0.351  23.482  1.00 24.85 ? 465 GLU A CA  1 
ATOM   2327 C C   . GLU A 1 465 ? 0.002   -0.095  23.431  1.00 25.33 ? 465 GLU A C   1 
ATOM   2328 O O   . GLU A 1 465 ? -0.595  0.291   24.435  1.00 26.05 ? 465 GLU A O   1 
ATOM   2329 C CB  . GLU A 1 465 ? 2.160   0.290   24.720  1.00 26.43 ? 465 GLU A CB  1 
ATOM   2330 C CG  . GLU A 1 465 ? 3.617   -0.104  24.857  1.00 31.22 ? 465 GLU A CG  1 
ATOM   2331 C CD  . GLU A 1 465 ? 4.277   0.351   26.145  1.00 41.03 ? 465 GLU A CD  1 
ATOM   2332 O OE1 . GLU A 1 465 ? 4.095   1.529   26.524  1.00 44.95 ? 465 GLU A OE1 1 
ATOM   2333 O OE2 . GLU A 1 465 ? 4.983   -0.469  26.772  1.00 42.95 ? 465 GLU A OE2 1 
ATOM   2334 N N   . THR A 1 466 ? -0.615  -0.331  22.268  1.00 24.17 ? 466 THR A N   1 
ATOM   2335 C CA  . THR A 1 466 ? -2.070  -0.227  22.139  1.00 23.42 ? 466 THR A CA  1 
ATOM   2336 C C   . THR A 1 466 ? -2.609  -1.435  21.373  1.00 23.44 ? 466 THR A C   1 
ATOM   2337 O O   . THR A 1 466 ? -1.916  -2.020  20.538  1.00 22.91 ? 466 THR A O   1 
ATOM   2338 C CB  . THR A 1 466 ? -2.529  1.050   21.367  1.00 25.22 ? 466 THR A CB  1 
ATOM   2339 O OG1 . THR A 1 466 ? -2.132  0.976   19.986  1.00 25.09 ? 466 THR A OG1 1 
ATOM   2340 C CG2 . THR A 1 466 ? -2.081  2.352   22.021  1.00 25.98 ? 466 THR A CG2 1 
ATOM   2341 N N   . LEU A 1 467 ? -3.882  -1.750  21.608  1.00 23.65 ? 467 LEU A N   1 
ATOM   2342 C CA  . LEU A 1 467 ? -4.612  -2.723  20.829  1.00 24.78 ? 467 LEU A CA  1 
ATOM   2343 C C   . LEU A 1 467 ? -5.726  -1.892  20.216  1.00 24.11 ? 467 LEU A C   1 
ATOM   2344 O O   . LEU A 1 467 ? -6.532  -1.345  20.963  1.00 25.07 ? 467 LEU A O   1 
ATOM   2345 C CB  . LEU A 1 467 ? -5.238  -3.777  21.727  1.00 26.20 ? 467 LEU A CB  1 
ATOM   2346 C CG  . LEU A 1 467 ? -4.718  -5.167  21.539  1.00 31.20 ? 467 LEU A CG  1 
ATOM   2347 C CD1 . LEU A 1 467 ? -3.293  -5.270  22.092  1.00 32.18 ? 467 LEU A CD1 1 
ATOM   2348 C CD2 . LEU A 1 467 ? -5.636  -6.161  22.228  1.00 32.69 ? 467 LEU A CD2 1 
ATOM   2349 N N   . ARG A 1 468 ? -5.773  -1.758  18.887  1.00 21.73 ? 468 ARG A N   1 
ATOM   2350 C CA  . ARG A 1 468 ? -6.837  -0.995  18.238  1.00 21.15 ? 468 ARG A CA  1 
ATOM   2351 C C   . ARG A 1 468 ? -7.855  -1.954  17.684  1.00 20.61 ? 468 ARG A C   1 
ATOM   2352 O O   . ARG A 1 468 ? -7.467  -2.906  17.006  1.00 21.28 ? 468 ARG A O   1 
ATOM   2353 C CB  . ARG A 1 468 ? -6.262  -0.108  17.128  1.00 21.66 ? 468 ARG A CB  1 
ATOM   2354 C CG  . ARG A 1 468 ? -5.520  1.114   17.714  1.00 24.90 ? 468 ARG A CG  1 
ATOM   2355 C CD  . ARG A 1 468 ? -4.888  1.943   16.617  1.00 30.52 ? 468 ARG A CD  1 
ATOM   2356 N NE  . ARG A 1 468 ? -4.943  3.382   16.869  1.00 38.45 ? 468 ARG A NE  1 
ATOM   2357 C CZ  . ARG A 1 468 ? -4.080  4.055   17.620  1.00 40.57 ? 468 ARG A CZ  1 
ATOM   2358 N NH1 . ARG A 1 468 ? -4.197  5.366   17.755  1.00 40.90 ? 468 ARG A NH1 1 
ATOM   2359 N NH2 . ARG A 1 468 ? -3.099  3.421   18.249  1.00 40.44 ? 468 ARG A NH2 1 
ATOM   2360 N N   . LEU A 1 469 ? -9.155  -1.744  17.965  1.00 20.85 ? 469 LEU A N   1 
ATOM   2361 C CA  . LEU A 1 469 ? -10.171 -2.674  17.462  1.00 21.23 ? 469 LEU A CA  1 
ATOM   2362 C C   . LEU A 1 469 ? -10.924 -1.994  16.364  1.00 21.33 ? 469 LEU A C   1 
ATOM   2363 O O   . LEU A 1 469 ? -11.629 -1.024  16.625  1.00 22.66 ? 469 LEU A O   1 
ATOM   2364 C CB  . LEU A 1 469 ? -11.127 -3.079  18.576  1.00 21.53 ? 469 LEU A CB  1 
ATOM   2365 C CG  . LEU A 1 469 ? -10.748 -4.284  19.437  1.00 24.14 ? 469 LEU A CG  1 
ATOM   2366 C CD1 . LEU A 1 469 ? -9.304  -4.233  19.963  1.00 25.50 ? 469 LEU A CD1 1 
ATOM   2367 C CD2 . LEU A 1 469 ? -11.735 -4.426  20.566  1.00 25.75 ? 469 LEU A CD2 1 
ATOM   2368 N N   . TRP A 1 470 ? -10.763 -2.465  15.128  1.00 19.15 ? 470 TRP A N   1 
ATOM   2369 C CA  . TRP A 1 470 ? -11.351 -1.808  13.972  1.00 19.29 ? 470 TRP A CA  1 
ATOM   2370 C C   . TRP A 1 470 ? -12.586 -2.535  13.509  1.00 20.09 ? 470 TRP A C   1 
ATOM   2371 O O   . TRP A 1 470 ? -12.471 -3.679  13.065  1.00 20.14 ? 470 TRP A O   1 
ATOM   2372 C CB  . TRP A 1 470 ? -10.347 -1.790  12.817  1.00 18.92 ? 470 TRP A CB  1 
ATOM   2373 C CG  . TRP A 1 470 ? -8.964  -1.320  13.162  1.00 18.79 ? 470 TRP A CG  1 
ATOM   2374 C CD1 . TRP A 1 470 ? -7.941  -2.078  13.642  1.00 19.46 ? 470 TRP A CD1 1 
ATOM   2375 C CD2 . TRP A 1 470 ? -8.440  0.007   12.992  1.00 19.19 ? 470 TRP A CD2 1 
ATOM   2376 N NE1 . TRP A 1 470 ? -6.806  -1.304  13.789  1.00 20.29 ? 470 TRP A NE1 1 
ATOM   2377 C CE2 . TRP A 1 470 ? -7.092  -0.017  13.410  1.00 20.28 ? 470 TRP A CE2 1 
ATOM   2378 C CE3 . TRP A 1 470 ? -8.981  1.216   12.520  1.00 20.76 ? 470 TRP A CE3 1 
ATOM   2379 C CZ2 . TRP A 1 470 ? -6.271  1.115   13.362  1.00 21.34 ? 470 TRP A CZ2 1 
ATOM   2380 C CZ3 . TRP A 1 470 ? -8.171  2.342   12.488  1.00 21.45 ? 470 TRP A CZ3 1 
ATOM   2381 C CH2 . TRP A 1 470 ? -6.825  2.276   12.879  1.00 21.35 ? 470 TRP A CH2 1 
ATOM   2382 N N   . ARG A 1 471 ? -13.727 -1.859  13.468  1.00 20.45 ? 471 ARG A N   1 
ATOM   2383 C CA  . ARG A 1 471 ? -14.939 -2.504  12.980  1.00 21.76 ? 471 ARG A CA  1 
ATOM   2384 C C   . ARG A 1 471 ? -14.992 -2.252  11.479  1.00 22.86 ? 471 ARG A C   1 
ATOM   2385 O O   . ARG A 1 471 ? -15.893 -1.571  10.985  1.00 24.38 ? 471 ARG A O   1 
ATOM   2386 C CB  . ARG A 1 471 ? -16.166 -1.963  13.697  1.00 23.91 ? 471 ARG A CB  1 
ATOM   2387 C CG  . ARG A 1 471 ? -17.351 -2.903  13.662  1.00 28.70 ? 471 ARG A CG  1 
ATOM   2388 C CD  . ARG A 1 471 ? -18.436 -2.489  14.668  1.00 34.43 ? 471 ARG A CD  1 
ATOM   2389 N NE  . ARG A 1 471 ? -19.589 -3.379  14.581  1.00 39.14 ? 471 ARG A NE  1 
ATOM   2390 C CZ  . ARG A 1 471 ? -19.695 -4.545  15.209  1.00 41.94 ? 471 ARG A CZ  1 
ATOM   2391 N NH1 . ARG A 1 471 ? -18.733 -4.961  16.019  1.00 41.61 ? 471 ARG A NH1 1 
ATOM   2392 N NH2 . ARG A 1 471 ? -20.772 -5.302  15.034  1.00 43.22 ? 471 ARG A NH2 1 
ATOM   2393 N N   . CYS A 1 472 ? -13.996 -2.777  10.763  1.00 22.28 ? 472 CYS A N   1 
ATOM   2394 C CA  . CYS A 1 472 ? -13.806 -2.534  9.337   1.00 23.41 ? 472 CYS A CA  1 
ATOM   2395 C C   . CYS A 1 472 ? -14.611 -3.463  8.426   1.00 25.06 ? 472 CYS A C   1 
ATOM   2396 O O   . CYS A 1 472 ? -14.630 -3.235  7.208   1.00 25.98 ? 472 CYS A O   1 
ATOM   2397 C CB  . CYS A 1 472 ? -12.321 -2.573  8.996   1.00 24.26 ? 472 CYS A CB  1 
ATOM   2398 S SG  . CYS A 1 472 ? -11.505 -4.115  9.479   1.00 24.49 ? 472 CYS A SG  1 
ATOM   2399 N N   . PHE A 1 473 ? -15.245 -4.513  8.985   1.00 24.48 ? 473 PHE A N   1 
ATOM   2400 C CA  . PHE A 1 473 ? -16.077 -5.400  8.180   1.00 24.54 ? 473 PHE A CA  1 
ATOM   2401 C C   . PHE A 1 473 ? -17.546 -5.359  8.631   1.00 28.56 ? 473 PHE A C   1 
ATOM   2402 O O   . PHE A 1 473 ? -18.210 -6.380  8.589   1.00 29.74 ? 473 PHE A O   1 
ATOM   2403 C CB  . PHE A 1 473 ? -15.550 -6.845  8.184   1.00 22.21 ? 473 PHE A CB  1 
ATOM   2404 C CG  . PHE A 1 473 ? -14.160 -6.977  7.626   1.00 21.32 ? 473 PHE A CG  1 
ATOM   2405 C CD1 . PHE A 1 473 ? -13.882 -6.602  6.320   1.00 21.23 ? 473 PHE A CD1 1 
ATOM   2406 C CD2 . PHE A 1 473 ? -13.128 -7.463  8.405   1.00 21.92 ? 473 PHE A CD2 1 
ATOM   2407 C CE1 . PHE A 1 473 ? -12.596 -6.696  5.814   1.00 21.42 ? 473 PHE A CE1 1 
ATOM   2408 C CE2 . PHE A 1 473 ? -11.848 -7.592  7.886   1.00 22.09 ? 473 PHE A CE2 1 
ATOM   2409 C CZ  . PHE A 1 473 ? -11.585 -7.199  6.590   1.00 21.44 ? 473 PHE A CZ  1 
ATOM   2410 N N   . GLU A 1 474 ? -18.068 -4.183  9.028   1.00 30.84 ? 474 GLU A N   1 
ATOM   2411 C CA  . GLU A 1 474 ? -19.470 -4.041  9.426   1.00 34.29 ? 474 GLU A CA  1 
ATOM   2412 C C   . GLU A 1 474 ? -19.913 -2.583  9.428   1.00 37.97 ? 474 GLU A C   1 
ATOM   2413 O O   . GLU A 1 474 ? -19.081 -1.680  9.546   1.00 38.23 ? 474 GLU A O   1 
ATOM   2414 C CB  . GLU A 1 474 ? -19.726 -4.607  10.836  1.00 38.19 ? 474 GLU A CB  1 
ATOM   2415 C CG  . GLU A 1 474 ? -20.516 -5.901  10.895  1.00 43.35 ? 474 GLU A CG  1 
ATOM   2416 C CD  . GLU A 1 474 ? -21.860 -5.978  10.205  1.00 49.72 ? 474 GLU A CD  1 
ATOM   2417 O OE1 . GLU A 1 474 ? -22.189 -7.087  9.730   1.00 52.68 ? 474 GLU A OE1 1 
ATOM   2418 O OE2 . GLU A 1 474 ? -22.585 -4.957  10.137  1.00 48.72 ? 474 GLU A OE2 1 
ATOM   2419 N N   . LEU A 1 475 ? -21.250 -2.371  9.333   1.00 39.90 ? 475 LEU A N   1 
ATOM   2420 C CA  . LEU A 1 475 ? -21.961 -1.095  9.402   1.00 42.98 ? 475 LEU A CA  1 
ATOM   2421 C C   . LEU A 1 475 ? -23.073 -1.140  10.490  1.00 45.14 ? 475 LEU A C   1 
ATOM   2422 O O   . LEU A 1 475 ? -23.518 -0.083  10.944  1.00 46.08 ? 475 LEU A O   1 
ATOM   2423 C CB  . LEU A 1 475 ? -22.594 -0.759  8.039   1.00 43.86 ? 475 LEU A CB  1 
ATOM   2424 C CG  . LEU A 1 475 ? -21.615 -0.685  6.872   1.00 46.01 ? 475 LEU A CG  1 
ATOM   2425 C CD1 . LEU A 1 475 ? -22.353 -0.502  5.547   1.00 46.82 ? 475 LEU A CD1 1 
ATOM   2426 C CD2 . LEU A 1 475 ? -20.622 0.434   7.076   1.00 47.06 ? 475 LEU A CD2 1 
ATOM   2427 N N   . ASP A 1 476 ? -23.552 -2.356  10.852  1.00 45.53 ? 476 ASP A N   1 
ATOM   2428 C CA  . ASP A 1 476 ? -24.586 -2.621  11.856  1.00 46.25 ? 476 ASP A CA  1 
ATOM   2429 C C   . ASP A 1 476 ? -25.940 -2.020  11.504  1.00 45.82 ? 476 ASP A C   1 
ATOM   2430 O O   . ASP A 1 476 ? -26.380 -2.130  10.362  1.00 45.08 ? 476 ASP A O   1 
ATOM   2431 C CB  . ASP A 1 476 ? -24.128 -2.186  13.252  1.00 49.00 ? 476 ASP A CB  1 
ATOM   2432 C CG  . ASP A 1 476 ? -22.751 -2.702  13.588  1.00 55.69 ? 476 ASP A CG  1 
ATOM   2433 O OD1 . ASP A 1 476 ? -22.500 -3.900  13.364  1.00 57.65 ? 476 ASP A OD1 1 
ATOM   2434 O OD2 . ASP A 1 476 ? -21.915 -1.900  14.050  1.00 58.55 ? 476 ASP A OD2 1 
ATOM   2435 N N   . ARG B 2 1   ? -1.292  3.079   34.752  1.00 49.43 ? 1   ARG B N   1 
ATOM   2436 C CA  . ARG B 2 1   ? -1.601  2.426   33.480  1.00 49.31 ? 1   ARG B CA  1 
ATOM   2437 C C   . ARG B 2 1   ? -2.192  1.048   33.706  1.00 48.39 ? 1   ARG B C   1 
ATOM   2438 O O   . ARG B 2 1   ? -1.453  0.089   33.917  1.00 48.75 ? 1   ARG B O   1 
ATOM   2439 C CB  . ARG B 2 1   ? -0.349  2.309   32.601  1.00 51.14 ? 1   ARG B CB  1 
ATOM   2440 C CG  . ARG B 2 1   ? 0.117   3.639   32.034  1.00 55.12 ? 1   ARG B CG  1 
ATOM   2441 C CD  . ARG B 2 1   ? 1.291   3.445   31.100  1.00 59.15 ? 1   ARG B CD  1 
ATOM   2442 N NE  . ARG B 2 1   ? 0.876   2.861   29.823  1.00 62.00 ? 1   ARG B NE  1 
ATOM   2443 C CZ  . ARG B 2 1   ? 1.713   2.398   28.902  1.00 63.96 ? 1   ARG B CZ  1 
ATOM   2444 N NH1 . ARG B 2 1   ? 3.025   2.425   29.112  1.00 63.68 ? 1   ARG B NH1 1 
ATOM   2445 N NH2 . ARG B 2 1   ? 1.247   1.890   27.770  1.00 63.62 ? 1   ARG B NH2 1 
ATOM   2446 N N   . ALA B 2 2   ? -3.523  0.941   33.648  1.00 46.77 ? 2   ALA B N   1 
ATOM   2447 C CA  . ALA B 2 2   ? -4.190  -0.334  33.827  1.00 45.51 ? 2   ALA B CA  1 
ATOM   2448 C C   . ALA B 2 2   ? -4.184  -1.098  32.502  1.00 43.93 ? 2   ALA B C   1 
ATOM   2449 O O   . ALA B 2 2   ? -4.560  -0.552  31.461  1.00 44.11 ? 2   ALA B O   1 
ATOM   2450 C CB  . ALA B 2 2   ? -5.616  -0.112  34.294  1.00 45.56 ? 2   ALA B CB  1 
ATOM   2451 N N   . PRO B 2 3   ? -3.748  -2.363  32.526  1.00 41.65 ? 3   PRO B N   1 
ATOM   2452 C CA  . PRO B 2 3   ? -3.735  -3.151  31.294  1.00 40.05 ? 3   PRO B CA  1 
ATOM   2453 C C   . PRO B 2 3   ? -5.130  -3.325  30.702  1.00 38.78 ? 3   PRO B C   1 
ATOM   2454 O O   . PRO B 2 3   ? -6.107  -3.544  31.419  1.00 37.64 ? 3   PRO B O   1 
ATOM   2455 C CB  . PRO B 2 3   ? -3.153  -4.490  31.741  1.00 40.90 ? 3   PRO B CB  1 
ATOM   2456 C CG  . PRO B 2 3   ? -2.416  -4.188  32.996  1.00 41.97 ? 3   PRO B CG  1 
ATOM   2457 C CD  . PRO B 2 3   ? -3.238  -3.140  33.667  1.00 40.82 ? 3   PRO B CD  1 
HETATM 2458 O O   . 0JY B 2 4   ? -8.667  -2.452  28.435  1.00 39.97 ? 4   0JY B O   1 
HETATM 2459 C C   . 0JY B 2 4   ? -7.539  -2.281  28.887  1.00 40.28 ? 4   0JY B C   1 
HETATM 2460 C CA  . 0JY B 2 4   ? -6.428  -3.285  28.577  1.00 38.35 ? 4   0JY B CA  1 
HETATM 2461 N N   . 0JY B 2 4   ? -5.217  -3.142  29.382  1.00 38.03 ? 4   0JY B N   1 
HETATM 2462 C CB  . 0JY B 2 4   ? -6.964  -4.733  28.563  1.00 37.41 ? 4   0JY B CB  1 
HETATM 2463 C CAI . 0JY B 2 4   ? -6.180  -5.778  27.746  1.00 36.97 ? 4   0JY B CAI 1 
HETATM 2464 C CAB . 0JY B 2 4   ? -4.782  -5.977  28.325  1.00 36.74 ? 4   0JY B CAB 1 
HETATM 2465 C CAC . 0JY B 2 4   ? -6.053  -5.326  26.290  1.00 36.81 ? 4   0JY B CAC 1 
HETATM 2466 C CAA . 0JY B 2 4   ? -6.906  -7.120  27.788  1.00 36.73 ? 4   0JY B CAA 1 
ATOM   2467 N N   . SER B 2 5   ? -7.209  -1.206  29.605  1.00 41.87 ? 5   SER B N   1 
ATOM   2468 C CA  . SER B 2 5   ? -8.186  -0.173  29.930  1.00 43.81 ? 5   SER B CA  1 
ATOM   2469 C C   . SER B 2 5   ? -8.388  0.777   28.735  1.00 45.75 ? 5   SER B C   1 
ATOM   2470 O O   . SER B 2 5   ? -7.527  0.877   27.857  1.00 45.51 ? 5   SER B O   1 
ATOM   2471 C CB  . SER B 2 5   ? -7.728  0.615   31.154  1.00 44.67 ? 5   SER B CB  1 
ATOM   2472 O OG  . SER B 2 5   ? -6.494  1.266   30.895  1.00 46.25 ? 5   SER B OG  1 
ATOM   2473 N N   . ASP B 2 6   ? -9.529  1.476   28.710  1.00 47.17 ? 6   ASP B N   1 
ATOM   2474 C CA  . ASP B 2 6   ? -9.831  2.429   27.645  1.00 49.01 ? 6   ASP B CA  1 
ATOM   2475 C C   . ASP B 2 6   ? -9.362  3.821   28.030  1.00 49.61 ? 6   ASP B C   1 
ATOM   2476 O O   . ASP B 2 6   ? -8.207  3.993   28.422  1.00 49.91 ? 6   ASP B O   1 
ATOM   2477 C CB  . ASP B 2 6   ? -11.329 2.454   27.349  1.00 51.70 ? 6   ASP B CB  1 
ATOM   2478 C CG  . ASP B 2 6   ? -11.800 1.233   26.598  1.00 57.95 ? 6   ASP B CG  1 
ATOM   2479 O OD1 . ASP B 2 6   ? -11.740 1.247   25.350  1.00 59.26 ? 6   ASP B OD1 1 
ATOM   2480 O OD2 . ASP B 2 6   ? -12.237 0.269   27.254  1.00 60.44 ? 6   ASP B OD2 1 
HETATM 2481 O O   . HOH C 3 .   ? -17.445 -8.657  -1.046  1.00 38.50 ? 501 HOH A O   1 
HETATM 2482 O O   . HOH C 3 .   ? 6.949   -34.306 26.616  1.00 45.01 ? 502 HOH A O   1 
HETATM 2483 O O   . HOH C 3 .   ? 2.026   -10.463 18.699  1.00 31.85 ? 503 HOH A O   1 
HETATM 2484 O O   . HOH C 3 .   ? 7.668   -17.268 16.901  1.00 57.77 ? 504 HOH A O   1 
HETATM 2485 O O   . HOH C 3 .   ? 10.002  -28.040 26.948  1.00 36.91 ? 505 HOH A O   1 
HETATM 2486 O O   . HOH C 3 .   ? 12.770  -31.097 22.647  1.00 50.83 ? 506 HOH A O   1 
HETATM 2487 O O   . HOH C 3 .   ? -15.975 -10.295 8.074   1.00 27.60 ? 507 HOH A O   1 
HETATM 2488 O O   . HOH C 3 .   ? -7.266  6.112   13.022  1.00 29.57 ? 508 HOH A O   1 
HETATM 2489 O O   . HOH C 3 .   ? -24.237 -8.408  9.174   1.00 29.88 ? 509 HOH A O   1 
HETATM 2490 O O   . HOH C 3 .   ? 17.840  -10.332 -3.594  1.00 73.92 ? 510 HOH A O   1 
HETATM 2491 O O   . HOH C 3 .   ? -1.488  -13.659 17.743  1.00 29.77 ? 511 HOH A O   1 
HETATM 2492 O O   . HOH C 3 .   ? 12.791  -4.341  1.772   1.00 59.69 ? 512 HOH A O   1 
HETATM 2493 O O   . HOH C 3 .   ? -17.035 1.669   13.473  1.00 55.27 ? 513 HOH A O   1 
HETATM 2494 O O   . HOH C 3 .   ? -7.950  -15.718 38.228  1.00 53.56 ? 514 HOH A O   1 
HETATM 2495 O O   . HOH C 3 .   ? 4.963   -9.510  19.153  1.00 43.62 ? 515 HOH A O   1 
HETATM 2496 O O   . HOH C 3 .   ? 5.356   -15.636 41.287  1.00 64.32 ? 516 HOH A O   1 
HETATM 2497 O O   . HOH C 3 .   ? 2.966   -8.513  34.565  1.00 58.50 ? 517 HOH A O   1 
HETATM 2498 O O   . HOH C 3 .   ? -0.230  -13.271 15.458  1.00 35.07 ? 518 HOH A O   1 
HETATM 2499 O O   . HOH C 3 .   ? -18.811 -8.831  8.100   1.00 30.67 ? 519 HOH A O   1 
HETATM 2500 O O   . HOH C 3 .   ? -11.925 -28.435 32.132  1.00 37.21 ? 520 HOH A O   1 
HETATM 2501 O O   . HOH C 3 .   ? -1.992  8.105   16.368  1.00 53.46 ? 521 HOH A O   1 
HETATM 2502 O O   . HOH C 3 .   ? -2.406  -13.077 13.413  1.00 51.53 ? 522 HOH A O   1 
HETATM 2503 O O   . HOH C 3 .   ? -6.287  5.263   15.697  1.00 32.13 ? 523 HOH A O   1 
HETATM 2504 O O   . HOH C 3 .   ? 12.516  -17.705 29.974  1.00 32.72 ? 524 HOH A O   1 
HETATM 2505 O O   . HOH C 3 .   ? 14.322  -15.214 24.559  1.00 41.33 ? 525 HOH A O   1 
HETATM 2506 O O   . HOH C 3 .   ? 0.958   4.774   22.269  1.00 46.49 ? 526 HOH A O   1 
HETATM 2507 O O   . HOH C 3 .   ? -18.031 -10.516 31.100  1.00 49.54 ? 527 HOH A O   1 
HETATM 2508 O O   . HOH C 3 .   ? 6.061   -11.906 7.982   1.00 23.21 ? 528 HOH A O   1 
HETATM 2509 O O   . HOH C 3 .   ? -8.894  -17.962 7.704   1.00 32.67 ? 529 HOH A O   1 
HETATM 2510 O O   . HOH C 3 .   ? -16.930 -16.638 -6.552  1.00 68.48 ? 530 HOH A O   1 
HETATM 2511 O O   . HOH C 3 .   ? -3.233  -19.945 15.365  1.00 35.34 ? 531 HOH A O   1 
HETATM 2512 O O   . HOH C 3 .   ? 11.014  -33.623 23.595  1.00 48.16 ? 532 HOH A O   1 
HETATM 2513 O O   . HOH C 3 .   ? 8.080   -12.507 -2.393  1.00 22.22 ? 533 HOH A O   1 
HETATM 2514 O O   . HOH C 3 .   ? 9.246   -27.684 11.531  1.00 22.44 ? 534 HOH A O   1 
HETATM 2515 O O   . HOH C 3 .   ? 12.173  -10.498 22.694  1.00 47.11 ? 535 HOH A O   1 
HETATM 2516 O O   . HOH C 3 .   ? 5.114   -11.372 26.130  1.00 25.67 ? 536 HOH A O   1 
HETATM 2517 O O   . HOH C 3 .   ? -7.445  -33.027 10.526  1.00 36.94 ? 537 HOH A O   1 
HETATM 2518 O O   . HOH C 3 .   ? 5.303   -23.123 -5.788  1.00 23.33 ? 538 HOH A O   1 
HETATM 2519 O O   . HOH C 3 .   ? 9.255   -34.187 9.985   1.00 34.10 ? 539 HOH A O   1 
HETATM 2520 O O   . HOH C 3 .   ? 13.300  -18.796 0.901   1.00 30.34 ? 540 HOH A O   1 
HETATM 2521 O O   . HOH C 3 .   ? -17.523 -11.259 25.677  1.00 34.42 ? 541 HOH A O   1 
HETATM 2522 O O   . HOH C 3 .   ? -0.615  -45.245 1.442   1.00 72.83 ? 542 HOH A O   1 
HETATM 2523 O O   . HOH C 3 .   ? -4.973  -21.281 14.219  1.00 37.52 ? 543 HOH A O   1 
HETATM 2524 O O   . HOH C 3 .   ? 0.880   -1.012  1.208   1.00 60.86 ? 544 HOH A O   1 
HETATM 2525 O O   . HOH C 3 .   ? 3.469   -35.349 2.683   1.00 50.57 ? 545 HOH A O   1 
HETATM 2526 O O   . HOH C 3 .   ? 4.691   -5.243  11.013  1.00 34.46 ? 546 HOH A O   1 
HETATM 2527 O O   . HOH C 3 .   ? 7.131   -1.408  22.384  1.00 37.17 ? 547 HOH A O   1 
HETATM 2528 O O   . HOH C 3 .   ? -21.723 -10.754 28.595  1.00 58.70 ? 548 HOH A O   1 
HETATM 2529 O O   . HOH C 3 .   ? -14.027 -17.715 25.330  1.00 29.30 ? 549 HOH A O   1 
HETATM 2530 O O   . HOH C 3 .   ? -6.296  -17.353 37.266  1.00 42.02 ? 550 HOH A O   1 
HETATM 2531 O O   . HOH C 3 .   ? -18.418 -0.015  11.550  1.00 45.08 ? 551 HOH A O   1 
HETATM 2532 O O   . HOH C 3 .   ? -3.764  -23.919 -9.433  1.00 39.79 ? 552 HOH A O   1 
HETATM 2533 O O   . HOH C 3 .   ? 6.937   -27.588 24.976  1.00 30.16 ? 553 HOH A O   1 
HETATM 2534 O O   . HOH C 3 .   ? -22.122 -8.549  14.311  1.00 38.31 ? 554 HOH A O   1 
HETATM 2535 O O   . HOH C 3 .   ? -0.066  -38.443 4.636   1.00 55.80 ? 555 HOH A O   1 
HETATM 2536 O O   . HOH C 3 .   ? 1.277   -15.653 12.778  1.00 23.19 ? 556 HOH A O   1 
HETATM 2537 O O   . HOH C 3 .   ? -16.199 -6.135  -0.953  1.00 45.84 ? 557 HOH A O   1 
HETATM 2538 O O   . HOH C 3 .   ? 8.386   -13.462 34.555  1.00 24.58 ? 558 HOH A O   1 
HETATM 2539 O O   . HOH C 3 .   ? 7.598   1.536   12.108  1.00 34.83 ? 559 HOH A O   1 
HETATM 2540 O O   . HOH C 3 .   ? 4.949   4.775   19.338  1.00 40.17 ? 560 HOH A O   1 
HETATM 2541 O O   . HOH C 3 .   ? -7.312  -20.081 17.937  1.00 30.13 ? 561 HOH A O   1 
HETATM 2542 O O   . HOH C 3 .   ? -1.887  -17.050 17.982  1.00 28.17 ? 562 HOH A O   1 
HETATM 2543 O O   . HOH C 3 .   ? -17.072 6.406   11.900  1.00 63.37 ? 563 HOH A O   1 
HETATM 2544 O O   . HOH C 3 .   ? 12.651  -34.408 14.076  1.00 49.09 ? 564 HOH A O   1 
HETATM 2545 O O   . HOH C 3 .   ? -0.457  4.578   11.255  1.00 25.01 ? 565 HOH A O   1 
HETATM 2546 O O   . HOH C 3 .   ? -7.024  -27.385 3.343   1.00 25.14 ? 566 HOH A O   1 
HETATM 2547 O O   . HOH C 3 .   ? 0.008   -31.658 10.402  1.00 30.04 ? 567 HOH A O   1 
HETATM 2548 O O   . HOH C 3 .   ? 6.660   -27.353 -3.027  1.00 33.96 ? 568 HOH A O   1 
HETATM 2549 O O   . HOH C 3 .   ? 0.373   -13.349 12.088  1.00 34.59 ? 569 HOH A O   1 
HETATM 2550 O O   . HOH C 3 .   ? -14.826 -7.550  37.103  1.00 47.51 ? 570 HOH A O   1 
HETATM 2551 O O   . HOH C 3 .   ? 15.575  -24.040 6.334   1.00 34.39 ? 571 HOH A O   1 
HETATM 2552 O O   . HOH C 3 .   ? 12.470  -19.543 -4.591  1.00 35.42 ? 572 HOH A O   1 
HETATM 2553 O O   . HOH C 3 .   ? 6.447   -2.152  25.210  1.00 41.60 ? 573 HOH A O   1 
HETATM 2554 O O   . HOH C 3 .   ? 11.784  -27.772 20.132  1.00 25.58 ? 574 HOH A O   1 
HETATM 2555 O O   . HOH C 3 .   ? 9.761   -35.907 12.006  1.00 54.26 ? 575 HOH A O   1 
HETATM 2556 O O   . HOH C 3 .   ? 3.873   -9.117  25.408  1.00 21.24 ? 576 HOH A O   1 
HETATM 2557 O O   . HOH C 3 .   ? -2.520  -10.477 -8.521  1.00 50.27 ? 577 HOH A O   1 
HETATM 2558 O O   . HOH C 3 .   ? 9.054   -18.619 1.242   1.00 21.33 ? 578 HOH A O   1 
HETATM 2559 O O   . HOH C 3 .   ? -9.959  -26.555 18.394  1.00 24.81 ? 579 HOH A O   1 
HETATM 2560 O O   . HOH C 3 .   ? -17.470 -3.487  25.539  1.00 55.49 ? 580 HOH A O   1 
HETATM 2561 O O   . HOH C 3 .   ? 17.578  -25.636 16.072  1.00 55.15 ? 581 HOH A O   1 
HETATM 2562 O O   . HOH C 3 .   ? -2.893  -49.226 6.484   1.00 37.14 ? 582 HOH A O   1 
HETATM 2563 O O   . HOH C 3 .   ? -9.023  -36.228 28.735  1.00 30.00 ? 583 HOH A O   1 
HETATM 2564 O O   . HOH C 3 .   ? 8.496   -35.372 24.092  1.00 37.52 ? 584 HOH A O   1 
HETATM 2565 O O   . HOH C 3 .   ? -13.880 1.030   13.556  1.00 27.95 ? 585 HOH A O   1 
HETATM 2566 O O   . HOH C 3 .   ? 14.168  -13.293 29.293  1.00 54.67 ? 586 HOH A O   1 
HETATM 2567 O O   . HOH C 3 .   ? 3.995   0.651   6.124   1.00 29.93 ? 587 HOH A O   1 
HETATM 2568 O O   . HOH C 3 .   ? -9.239  -22.424 17.480  1.00 38.03 ? 588 HOH A O   1 
HETATM 2569 O O   . HOH C 3 .   ? -7.474  -21.382 9.518   1.00 28.78 ? 589 HOH A O   1 
HETATM 2570 O O   . HOH C 3 .   ? -6.778  3.486   25.627  1.00 52.55 ? 590 HOH A O   1 
HETATM 2571 O O   . HOH C 3 .   ? -13.189 -27.551 24.072  1.00 36.08 ? 591 HOH A O   1 
HETATM 2572 O O   . HOH C 3 .   ? -12.027 -19.899 19.841  1.00 23.70 ? 592 HOH A O   1 
HETATM 2573 O O   . HOH C 3 .   ? 17.393  -16.884 9.344   1.00 39.10 ? 593 HOH A O   1 
HETATM 2574 O O   . HOH C 3 .   ? 6.081   -6.950  -6.809  1.00 61.32 ? 594 HOH A O   1 
HETATM 2575 O O   . HOH C 3 .   ? -3.863  -15.154 10.535  1.00 28.88 ? 595 HOH A O   1 
HETATM 2576 O O   . HOH C 3 .   ? 9.819   -10.811 31.425  1.00 46.75 ? 596 HOH A O   1 
HETATM 2577 O O   . HOH C 3 .   ? 13.458  -22.019 26.381  1.00 39.24 ? 597 HOH A O   1 
HETATM 2578 O O   . HOH C 3 .   ? -12.706 -11.105 31.013  1.00 40.96 ? 598 HOH A O   1 
HETATM 2579 O O   . HOH C 3 .   ? 2.067   -7.379  32.367  1.00 51.45 ? 599 HOH A O   1 
HETATM 2580 O O   . HOH C 3 .   ? 3.083   -0.120  3.288   1.00 35.35 ? 600 HOH A O   1 
HETATM 2581 O O   . HOH C 3 .   ? -13.963 -17.537 34.674  1.00 31.62 ? 601 HOH A O   1 
HETATM 2582 O O   . HOH C 3 .   ? 11.079  -28.002 4.562   1.00 36.16 ? 602 HOH A O   1 
HETATM 2583 O O   . HOH C 3 .   ? -14.355 -21.887 6.845   1.00 34.22 ? 603 HOH A O   1 
HETATM 2584 O O   . HOH C 3 .   ? -14.359 3.662   1.944   1.00 59.77 ? 604 HOH A O   1 
HETATM 2585 O O   . HOH C 3 .   ? -2.580  1.777   12.104  1.00 21.66 ? 605 HOH A O   1 
HETATM 2586 O O   . HOH C 3 .   ? 18.914  -21.296 8.325   1.00 34.16 ? 606 HOH A O   1 
HETATM 2587 O O   . HOH C 3 .   ? -3.932  -38.122 19.159  1.00 44.02 ? 607 HOH A O   1 
HETATM 2588 O O   . HOH C 3 .   ? -17.291 -1.406  7.395   1.00 70.51 ? 608 HOH A O   1 
HETATM 2589 O O   . HOH C 3 .   ? -3.483  -17.636 37.729  1.00 31.89 ? 609 HOH A O   1 
HETATM 2590 O O   . HOH C 3 .   ? 8.047   -6.042  27.565  1.00 50.38 ? 610 HOH A O   1 
HETATM 2591 O O   . HOH C 3 .   ? -7.557  5.313   9.145   1.00 29.50 ? 611 HOH A O   1 
HETATM 2592 O O   . HOH C 3 .   ? -18.799 -7.674  21.099  1.00 46.89 ? 612 HOH A O   1 
HETATM 2593 O O   . HOH C 3 .   ? 0.883   -18.252 14.011  1.00 27.99 ? 613 HOH A O   1 
HETATM 2594 O O   . HOH C 3 .   ? -6.452  -22.295 12.308  1.00 49.81 ? 614 HOH A O   1 
HETATM 2595 O O   . HOH C 3 .   ? -12.678 -15.201 16.698  1.00 26.08 ? 615 HOH A O   1 
HETATM 2596 O O   . HOH C 3 .   ? 9.849   -1.338  16.532  1.00 38.19 ? 616 HOH A O   1 
HETATM 2597 O O   . HOH C 3 .   ? 11.709  -31.976 18.716  1.00 43.18 ? 617 HOH A O   1 
HETATM 2598 O O   . HOH C 3 .   ? -17.375 -7.459  16.406  1.00 40.51 ? 618 HOH A O   1 
HETATM 2599 O O   . HOH C 3 .   ? 8.739   -33.591 28.668  1.00 63.81 ? 619 HOH A O   1 
HETATM 2600 O O   . HOH C 3 .   ? 5.074   -32.657 29.416  1.00 41.90 ? 620 HOH A O   1 
HETATM 2601 O O   . HOH C 3 .   ? 15.105  -14.674 18.018  1.00 61.12 ? 621 HOH A O   1 
HETATM 2602 O O   . HOH C 3 .   ? 17.095  -29.087 17.037  1.00 48.17 ? 622 HOH A O   1 
HETATM 2603 O O   . HOH C 3 .   ? 14.347  -19.376 23.626  1.00 39.20 ? 623 HOH A O   1 
HETATM 2604 O O   . HOH C 3 .   ? 14.124  -15.822 15.802  1.00 52.19 ? 624 HOH A O   1 
HETATM 2605 O O   . HOH C 3 .   ? -10.309 -26.548 15.740  1.00 34.46 ? 625 HOH A O   1 
HETATM 2606 O O   . HOH C 3 .   ? 8.462   -20.104 17.832  1.00 20.48 ? 626 HOH A O   1 
HETATM 2607 O O   . HOH C 3 .   ? -14.141 -9.492  -6.001  1.00 63.93 ? 627 HOH A O   1 
HETATM 2608 O O   . HOH C 3 .   ? 4.083   -14.316 39.295  1.00 44.19 ? 628 HOH A O   1 
HETATM 2609 O O   . HOH C 3 .   ? -7.506  -9.814  37.511  1.00 34.62 ? 629 HOH A O   1 
HETATM 2610 O O   . HOH C 3 .   ? -12.459 0.482   10.842  1.00 31.15 ? 630 HOH A O   1 
HETATM 2611 O O   . HOH C 3 .   ? 12.251  -10.930 35.533  1.00 49.56 ? 631 HOH A O   1 
HETATM 2612 O O   . HOH C 3 .   ? -17.435 -15.175 11.244  1.00 49.81 ? 632 HOH A O   1 
HETATM 2613 O O   . HOH C 3 .   ? 11.636  -8.427  16.416  1.00 26.51 ? 633 HOH A O   1 
HETATM 2614 O O   . HOH C 3 .   ? 9.649   -4.921  24.006  1.00 39.27 ? 634 HOH A O   1 
HETATM 2615 O O   . HOH C 3 .   ? -6.372  -19.273 8.673   1.00 21.41 ? 635 HOH A O   1 
HETATM 2616 O O   . HOH C 3 .   ? -19.127 -1.385  4.289   1.00 61.44 ? 636 HOH A O   1 
HETATM 2617 O O   . HOH C 3 .   ? -2.455  -12.712 -10.413 1.00 48.16 ? 637 HOH A O   1 
HETATM 2618 O O   . HOH C 3 .   ? -17.297 -8.979  18.619  1.00 58.72 ? 638 HOH A O   1 
HETATM 2619 O O   . HOH C 3 .   ? -8.214  -15.452 8.327   1.00 23.47 ? 639 HOH A O   1 
HETATM 2620 O O   . HOH C 3 .   ? -9.261  4.856   6.558   1.00 40.25 ? 640 HOH A O   1 
HETATM 2621 O O   . HOH C 3 .   ? -5.781  -21.337 39.577  1.00 47.00 ? 641 HOH A O   1 
HETATM 2622 O O   . HOH C 3 .   ? 8.162   -38.789 10.582  1.00 51.80 ? 642 HOH A O   1 
HETATM 2623 O O   . HOH C 3 .   ? -9.526  -24.716 -2.912  1.00 51.81 ? 643 HOH A O   1 
HETATM 2624 O O   . HOH C 3 .   ? 8.977   -2.768  6.837   1.00 42.06 ? 644 HOH A O   1 
HETATM 2625 O O   . HOH C 3 .   ? 12.323  -10.747 7.324   1.00 35.67 ? 645 HOH A O   1 
HETATM 2626 O O   . HOH C 3 .   ? 10.287  -26.895 -3.007  1.00 52.29 ? 646 HOH A O   1 
HETATM 2627 O O   . HOH C 3 .   ? -14.699 -25.725 32.647  1.00 42.46 ? 647 HOH A O   1 
HETATM 2628 O O   . HOH C 3 .   ? -14.544 7.371   8.923   1.00 54.08 ? 648 HOH A O   1 
HETATM 2629 O O   . HOH C 3 .   ? -8.796  -23.226 3.577   1.00 33.95 ? 649 HOH A O   1 
HETATM 2630 O O   . HOH C 3 .   ? 16.290  -21.388 4.074   1.00 57.32 ? 650 HOH A O   1 
HETATM 2631 O O   . HOH C 3 .   ? -13.512 -28.908 39.005  1.00 52.61 ? 651 HOH A O   1 
HETATM 2632 O O   . HOH C 3 .   ? 6.384   1.912   3.540   1.00 43.22 ? 652 HOH A O   1 
HETATM 2633 O O   . HOH C 3 .   ? 0.190   -18.513 16.816  1.00 21.20 ? 653 HOH A O   1 
HETATM 2634 O O   . HOH C 3 .   ? -10.469 -29.594 36.087  1.00 45.47 ? 654 HOH A O   1 
HETATM 2635 O O   . HOH C 3 .   ? -9.105  -16.195 16.139  1.00 53.42 ? 655 HOH A O   1 
HETATM 2636 O O   . HOH C 3 .   ? -3.742  -22.743 38.221  1.00 29.84 ? 656 HOH A O   1 
HETATM 2637 O O   . HOH C 3 .   ? -5.799  -21.937 16.668  1.00 26.24 ? 657 HOH A O   1 
HETATM 2638 O O   . HOH C 3 .   ? 6.800   -37.749 14.839  1.00 32.54 ? 658 HOH A O   1 
HETATM 2639 O O   . HOH C 3 .   ? 0.869   -11.336 -9.049  1.00 39.57 ? 659 HOH A O   1 
HETATM 2640 O O   . HOH C 3 .   ? -8.891  -26.391 11.970  1.00 37.07 ? 660 HOH A O   1 
HETATM 2641 O O   . HOH C 3 .   ? -19.874 -9.538  10.437  1.00 38.58 ? 661 HOH A O   1 
HETATM 2642 O O   . HOH C 3 .   ? 14.311  -18.018 -3.458  1.00 54.04 ? 662 HOH A O   1 
HETATM 2643 O O   . HOH C 3 .   ? -12.902 -5.517  34.856  1.00 58.38 ? 663 HOH A O   1 
HETATM 2644 O O   . HOH C 3 .   ? 8.125   0.411   15.011  1.00 40.57 ? 664 HOH A O   1 
HETATM 2645 O O   . HOH C 3 .   ? 2.697   -39.174 14.476  1.00 49.41 ? 665 HOH A O   1 
HETATM 2646 O O   . HOH C 3 .   ? -8.281  4.401   3.229   1.00 44.72 ? 666 HOH A O   1 
HETATM 2647 O O   . HOH C 3 .   ? 9.337   -11.602 -5.412  1.00 58.95 ? 667 HOH A O   1 
HETATM 2648 O O   . HOH C 3 .   ? -16.018 -3.668  17.713  1.00 56.98 ? 668 HOH A O   1 
HETATM 2649 O O   . HOH C 3 .   ? 17.206  -18.883 3.675   1.00 56.98 ? 669 HOH A O   1 
HETATM 2650 O O   . HOH C 3 .   ? 1.974   -20.567 34.938  1.00 51.18 ? 670 HOH A O   1 
HETATM 2651 O O   . HOH C 3 .   ? 15.779  -27.425 13.208  1.00 47.75 ? 671 HOH A O   1 
HETATM 2652 O O   . HOH C 3 .   ? 4.859   -25.130 37.787  1.00 57.35 ? 672 HOH A O   1 
HETATM 2653 O O   . HOH C 3 .   ? 15.271  -17.950 14.255  1.00 31.33 ? 673 HOH A O   1 
HETATM 2654 O O   . HOH C 3 .   ? -22.884 -1.668  16.891  1.00 79.56 ? 674 HOH A O   1 
HETATM 2655 O O   . HOH C 3 .   ? -5.997  -14.958 15.204  1.00 43.23 ? 675 HOH A O   1 
HETATM 2656 O O   . HOH C 3 .   ? -12.258 -8.074  37.129  1.00 60.55 ? 676 HOH A O   1 
HETATM 2657 O O   . HOH C 3 .   ? 5.570   -23.502 35.169  1.00 66.61 ? 677 HOH A O   1 
HETATM 2658 O O   . HOH C 3 .   ? -0.608  -40.625 23.263  1.00 40.31 ? 678 HOH A O   1 
HETATM 2659 O O   . HOH C 3 .   ? 3.122   5.975   12.427  1.00 39.52 ? 679 HOH A O   1 
HETATM 2660 O O   . HOH C 3 .   ? 9.664   -23.068 -3.987  1.00 36.31 ? 680 HOH A O   1 
HETATM 2661 O O   . HOH C 3 .   ? 1.458   -4.763  31.764  1.00 38.62 ? 681 HOH A O   1 
HETATM 2662 O O   . HOH C 3 .   ? 4.546   -36.544 25.774  1.00 35.56 ? 682 HOH A O   1 
HETATM 2663 O O   . HOH C 3 .   ? -1.363  -14.172 9.809   1.00 19.80 ? 683 HOH A O   1 
HETATM 2664 O O   . HOH C 3 .   ? 0.708   -25.297 -10.769 1.00 38.12 ? 684 HOH A O   1 
HETATM 2665 O O   . HOH C 3 .   ? -3.099  -7.312  -8.425  1.00 57.55 ? 685 HOH A O   1 
HETATM 2666 O O   . HOH C 3 .   ? -3.057  -6.174  36.692  1.00 63.50 ? 686 HOH A O   1 
HETATM 2667 O O   . HOH C 3 .   ? 13.944  -8.887  6.878   1.00 37.64 ? 687 HOH A O   1 
HETATM 2668 O O   . HOH C 3 .   ? -8.247  -14.565 14.203  1.00 34.27 ? 688 HOH A O   1 
HETATM 2669 O O   . HOH C 3 .   ? -22.871 -9.397  11.659  1.00 52.38 ? 689 HOH A O   1 
HETATM 2670 O O   . HOH C 3 .   ? -11.139 3.722   5.824   1.00 53.16 ? 690 HOH A O   1 
HETATM 2671 O O   . HOH C 3 .   ? 0.996   -19.148 36.938  1.00 59.06 ? 691 HOH A O   1 
HETATM 2672 O O   . HOH C 3 .   ? -7.099  -31.725 29.300  1.00 48.63 ? 692 HOH A O   1 
HETATM 2673 O O   . HOH C 3 .   ? -10.575 -24.937 4.710   1.00 35.59 ? 693 HOH A O   1 
HETATM 2674 O O   . HOH C 3 .   ? -4.051  -34.534 4.231   1.00 59.60 ? 694 HOH A O   1 
HETATM 2675 O O   . HOH C 3 .   ? -11.779 -15.922 8.773   1.00 57.18 ? 695 HOH A O   1 
HETATM 2676 O O   . HOH C 3 .   ? -14.476 6.644   11.685  1.00 41.73 ? 696 HOH A O   1 
HETATM 2677 O O   . HOH C 3 .   ? 11.153  -15.117 -5.531  1.00 55.38 ? 697 HOH A O   1 
HETATM 2678 O O   . HOH C 3 .   ? -0.715  -17.278 37.614  1.00 30.93 ? 698 HOH A O   1 
HETATM 2679 O O   . HOH C 3 .   ? -18.245 -20.818 21.608  1.00 37.01 ? 699 HOH A O   1 
HETATM 2680 O O   . HOH C 3 .   ? 8.924   -0.547  -0.915  1.00 64.04 ? 700 HOH A O   1 
HETATM 2681 O O   . HOH C 3 .   ? 13.601  -6.735  -2.099  1.00 68.17 ? 701 HOH A O   1 
HETATM 2682 O O   . HOH C 3 .   ? -14.381 -13.682 36.040  1.00 53.97 ? 702 HOH A O   1 
HETATM 2683 O O   . HOH C 3 .   ? 11.327  -8.223  -2.599  1.00 55.91 ? 703 HOH A O   1 
HETATM 2684 O O   . HOH C 3 .   ? 10.717  -33.069 6.785   1.00 63.27 ? 704 HOH A O   1 
HETATM 2685 O O   . HOH C 3 .   ? 17.504  -21.696 17.143  1.00 52.40 ? 705 HOH A O   1 
HETATM 2686 O O   . HOH C 3 .   ? 7.530   -24.358 -4.567  1.00 41.92 ? 706 HOH A O   1 
HETATM 2687 O O   . HOH C 3 .   ? 15.188  -16.619 0.521   1.00 46.35 ? 707 HOH A O   1 
HETATM 2688 O O   . HOH C 3 .   ? 14.719  -26.916 6.273   1.00 62.09 ? 708 HOH A O   1 
HETATM 2689 O O   . HOH C 3 .   ? -9.923  -14.796 9.932   1.00 41.37 ? 709 HOH A O   1 
HETATM 2690 O O   . HOH C 3 .   ? 4.634   -20.107 34.996  1.00 55.64 ? 710 HOH A O   1 
HETATM 2691 O O   . HOH C 3 .   ? 0.651   -31.833 31.968  1.00 41.94 ? 711 HOH A O   1 
HETATM 2692 O O   . HOH C 3 .   ? -3.945  -17.541 16.939  1.00 41.83 ? 712 HOH A O   1 
HETATM 2693 O O   . HOH C 3 .   ? 14.853  -4.255  -0.002  1.00 56.17 ? 713 HOH A O   1 
HETATM 2694 O O   . HOH C 3 .   ? 11.583  -7.006  22.886  1.00 65.63 ? 714 HOH A O   1 
HETATM 2695 O O   . HOH C 3 .   ? 9.906   -11.226 34.721  1.00 51.96 ? 715 HOH A O   1 
HETATM 2696 O O   . HOH C 3 .   ? -0.157  -28.433 35.943  1.00 48.21 ? 716 HOH A O   1 
HETATM 2697 O O   . HOH C 3 .   ? -10.001 -4.374  -9.527  1.00 72.19 ? 717 HOH A O   1 
HETATM 2698 O O   . HOH C 3 .   ? 8.850   1.190   19.559  1.00 53.07 ? 718 HOH A O   1 
HETATM 2699 O O   . HOH C 3 .   ? -6.029  -16.679 10.079  1.00 36.04 ? 719 HOH A O   1 
HETATM 2700 O O   . HOH C 3 .   ? -2.652  -13.754 38.209  1.00 49.68 ? 720 HOH A O   1 
HETATM 2701 O O   . HOH C 3 .   ? -3.917  8.645   11.173  1.00 52.31 ? 721 HOH A O   1 
HETATM 2702 O O   . HOH C 3 .   ? 6.697   -37.912 18.936  1.00 52.78 ? 722 HOH A O   1 
HETATM 2703 O O   . HOH C 3 .   ? 12.146  -31.140 27.015  1.00 53.12 ? 723 HOH A O   1 
HETATM 2704 O O   . HOH C 3 .   ? -12.873 -25.236 3.369   1.00 52.24 ? 724 HOH A O   1 
HETATM 2705 O O   . HOH C 3 .   ? -17.974 -18.790 16.778  1.00 51.19 ? 725 HOH A O   1 
HETATM 2706 O O   . HOH C 3 .   ? 13.045  -30.488 20.031  1.00 42.39 ? 726 HOH A O   1 
HETATM 2707 O O   . HOH C 3 .   ? -11.230 -19.327 17.424  1.00 60.49 ? 727 HOH A O   1 
HETATM 2708 O O   . HOH C 3 .   ? -6.771  8.677   10.005  1.00 63.66 ? 728 HOH A O   1 
HETATM 2709 O O   . HOH C 3 .   ? 3.975   2.381   2.765   1.00 53.41 ? 729 HOH A O   1 
HETATM 2710 O O   . HOH C 3 .   ? -10.630 -30.496 33.554  1.00 52.99 ? 730 HOH A O   1 
HETATM 2711 O O   . HOH C 3 .   ? 17.936  -15.643 0.947   1.00 43.90 ? 731 HOH A O   1 
HETATM 2712 O O   . HOH C 3 .   ? -1.954  -35.597 14.421  1.00 60.56 ? 732 HOH A O   1 
HETATM 2713 O O   . HOH C 3 .   ? -14.151 -16.213 11.463  1.00 57.29 ? 733 HOH A O   1 
HETATM 2714 O O   . HOH C 3 .   ? -6.716  8.368   14.422  1.00 46.73 ? 734 HOH A O   1 
HETATM 2715 O O   . HOH C 3 .   ? -15.855 -5.307  19.813  1.00 60.65 ? 735 HOH A O   1 
HETATM 2716 O O   . HOH C 3 .   ? 0.826   -37.078 2.539   1.00 63.38 ? 736 HOH A O   1 
HETATM 2717 O O   . HOH C 3 .   ? -10.462 -19.446 9.298   1.00 56.17 ? 737 HOH A O   1 
HETATM 2718 O O   . HOH C 3 .   ? 11.901  -30.491 4.290   1.00 52.68 ? 738 HOH A O   1 
HETATM 2719 O O   . HOH D 3 .   ? -11.601 3.100   23.451  1.00 31.56 ? 101 HOH B O   1 
HETATM 2720 O O   . HOH D 3 .   ? -11.701 -1.969  28.627  1.00 52.37 ? 102 HOH B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . ARG A 166 ? 0.5693 0.6248 0.5153 0.1320  -0.0129 0.0571  166 ARG A N   
2    C CA  . ARG A 166 ? 0.5551 0.6246 0.5124 0.1352  -0.0129 0.0516  166 ARG A CA  
3    C C   . ARG A 166 ? 0.5800 0.6134 0.5309 0.1367  -0.0066 0.0495  166 ARG A C   
4    O O   . ARG A 166 ? 0.5986 0.6009 0.5420 0.1271  -0.0029 0.0491  166 ARG A O   
5    C CB  . ARG A 166 ? 0.5328 0.6294 0.5076 0.1179  -0.0164 0.0429  166 ARG A CB  
6    C CG  . ARG A 166 ? 0.5181 0.5941 0.4953 0.0987  -0.0140 0.0369  166 ARG A CG  
7    C CD  . ARG A 166 ? 0.4717 0.5725 0.4643 0.0840  -0.0169 0.0291  166 ARG A CD  
8    N NE  . ARG A 166 ? 0.4157 0.4973 0.4111 0.0693  -0.0141 0.0234  166 ARG A NE  
9    C CZ  . ARG A 166 ? 0.3860 0.4572 0.3850 0.0677  -0.0111 0.0193  166 ARG A CZ  
10   N NH1 . ARG A 166 ? 0.3463 0.4231 0.3463 0.0797  -0.0101 0.0199  166 ARG A NH1 
11   N NH2 . ARG A 166 ? 0.3697 0.4258 0.3706 0.0550  -0.0091 0.0147  166 ARG A NH2 
12   N N   . TYR A 167 ? 0.5792 0.6178 0.5329 0.1483  -0.0052 0.0479  167 TYR A N   
13   C CA  . TYR A 167 ? 0.6017 0.6069 0.5484 0.1501  0.0007  0.0448  167 TYR A CA  
14   C C   . TYR A 167 ? 0.5811 0.5838 0.5385 0.1315  0.0015  0.0353  167 TYR A C   
15   O O   . TYR A 167 ? 0.5752 0.6059 0.5469 0.1270  -0.0010 0.0302  167 TYR A O   
16   C CB  . TYR A 167 ? 0.6195 0.6283 0.5627 0.1712  0.0026  0.0465  167 TYR A CB  
17   C CG  . TYR A 167 ? 0.6600 0.6370 0.5965 0.1722  0.0084  0.0415  167 TYR A CG  
18   C CD1 . TYR A 167 ? 0.7004 0.6320 0.6185 0.1746  0.0138  0.0441  167 TYR A CD1 
19   C CD2 . TYR A 167 ? 0.6708 0.6627 0.6187 0.1691  0.0087  0.0338  167 TYR A CD2 
20   C CE1 . TYR A 167 ? 0.7293 0.6314 0.6405 0.1737  0.0190  0.0382  167 TYR A CE1 
21   C CE2 . TYR A 167 ? 0.6999 0.6635 0.6409 0.1694  0.0138  0.0284  167 TYR A CE2 
22   C CZ  . TYR A 167 ? 0.7368 0.6556 0.6594 0.1714  0.0187  0.0302  167 TYR A CZ  
23   O OH  . TYR A 167 ? 0.7760 0.6668 0.6910 0.1705  0.0235  0.0237  167 TYR A OH  
24   N N   . ILE A 168 ? 0.5624 0.5315 0.5123 0.1212  0.0053  0.0333  168 ILE A N   
25   C CA  . ILE A 168 ? 0.5352 0.4993 0.4930 0.1054  0.0063  0.0248  168 ILE A CA  
26   C C   . ILE A 168 ? 0.5295 0.4604 0.4764 0.1094  0.0117  0.0221  168 ILE A C   
27   O O   . ILE A 168 ? 0.5412 0.4411 0.4733 0.1126  0.0153  0.0260  168 ILE A O   
28   C CB  . ILE A 168 ? 0.5335 0.4917 0.4931 0.0879  0.0055  0.0239  168 ILE A CB  
29   C CG1 . ILE A 168 ? 0.5328 0.5209 0.5005 0.0845  0.0005  0.0261  168 ILE A CG1 
30   C CG2 . ILE A 168 ? 0.5295 0.4830 0.4965 0.0730  0.0065  0.0158  168 ILE A CG2 
31   C CD1 . ILE A 168 ? 0.5486 0.5310 0.5157 0.0708  0.0001  0.0263  168 ILE A CD1 
32   N N   . PRO A 169 ? 0.5165 0.4520 0.4691 0.1093  0.0127  0.0154  169 PRO A N   
33   C CA  . PRO A 169 ? 0.5151 0.4186 0.4559 0.1132  0.0178  0.0117  169 PRO A CA  
34   C C   . PRO A 169 ? 0.5019 0.3766 0.4366 0.0973  0.0203  0.0084  169 PRO A C   
35   O O   . PRO A 169 ? 0.4944 0.3802 0.4392 0.0817  0.0179  0.0050  169 PRO A O   
36   C CB  . PRO A 169 ? 0.5228 0.4449 0.4733 0.1144  0.0174  0.0048  169 PRO A CB  
37   C CG  . PRO A 169 ? 0.5167 0.4800 0.4818 0.1168  0.0129  0.0072  169 PRO A CG  
38   C CD  . PRO A 169 ? 0.4966 0.4658 0.4652 0.1057  0.0096  0.0108  169 PRO A CD  
39   N N   . SER A 170 ? 0.4981 0.3355 0.4158 0.1012  0.0252  0.0093  170 SER A N   
40   C CA  . SER A 170 ? 0.4912 0.3020 0.4030 0.0849  0.0280  0.0057  170 SER A CA  
41   C C   . SER A 170 ? 0.4642 0.2705 0.3792 0.0760  0.0289  -0.0048 170 SER A C   
42   O O   . SER A 170 ? 0.4730 0.2675 0.3877 0.0602  0.0299  -0.0093 170 SER A O   
43   C CB  . SER A 170 ? 0.5308 0.3022 0.4223 0.0900  0.0334  0.0108  170 SER A CB  
44   O OG  . SER A 170 ? 0.5854 0.3378 0.4651 0.1053  0.0370  0.0094  170 SER A OG  
45   N N   . LEU A 171 ? 0.4330 0.2496 0.3503 0.0865  0.0288  -0.0087 171 LEU A N   
46   C CA  . LEU A 171 ? 0.4195 0.2348 0.3392 0.0794  0.0294  -0.0184 171 LEU A CA  
47   C C   . LEU A 171 ? 0.3920 0.2452 0.3298 0.0751  0.0249  -0.0207 171 LEU A C   
48   O O   . LEU A 171 ? 0.3764 0.2555 0.3227 0.0834  0.0224  -0.0161 171 LEU A O   
49   C CB  . LEU A 171 ? 0.4320 0.2305 0.3398 0.0946  0.0334  -0.0217 171 LEU A CB  
50   C CG  . LEU A 171 ? 0.4831 0.2388 0.3697 0.1010  0.0389  -0.0197 171 LEU A CG  
51   C CD1 . LEU A 171 ? 0.5065 0.2477 0.3815 0.1179  0.0429  -0.0233 171 LEU A CD1 
52   C CD2 . LEU A 171 ? 0.5168 0.2451 0.3964 0.0817  0.0411  -0.0249 171 LEU A CD2 
53   N N   . PRO A 172 ? 0.3827 0.2397 0.3259 0.0625  0.0240  -0.0281 172 PRO A N   
54   C CA  . PRO A 172 ? 0.3662 0.2556 0.3241 0.0595  0.0207  -0.0301 172 PRO A CA  
55   C C   . PRO A 172 ? 0.3732 0.2729 0.3307 0.0728  0.0220  -0.0323 172 PRO A C   
56   O O   . PRO A 172 ? 0.3795 0.2584 0.3247 0.0823  0.0257  -0.0349 172 PRO A O   
57   C CB  . PRO A 172 ? 0.3765 0.2621 0.3365 0.0443  0.0200  -0.0370 172 PRO A CB  
58   C CG  . PRO A 172 ? 0.4025 0.2555 0.3478 0.0432  0.0237  -0.0416 172 PRO A CG  
59   C CD  . PRO A 172 ? 0.3929 0.2252 0.3278 0.0513  0.0263  -0.0351 172 PRO A CD  
60   N N   . ASP A 173 ? 0.3588 0.2900 0.3291 0.0736  0.0196  -0.0312 173 ASP A N   
61   C CA  . ASP A 173 ? 0.3828 0.3299 0.3551 0.0844  0.0211  -0.0332 173 ASP A CA  
62   C C   . ASP A 173 ? 0.3914 0.3314 0.3599 0.0802  0.0228  -0.0415 173 ASP A C   
63   O O   . ASP A 173 ? 0.4088 0.3483 0.3720 0.0912  0.0257  -0.0447 173 ASP A O   
64   C CB  . ASP A 173 ? 0.4242 0.4072 0.4118 0.0822  0.0182  -0.0298 173 ASP A CB  
65   C CG  . ASP A 173 ? 0.5444 0.5440 0.5347 0.0955  0.0178  -0.0238 173 ASP A CG  
66   O OD1 . ASP A 173 ? 0.5699 0.5535 0.5521 0.1029  0.0182  -0.0198 173 ASP A OD1 
67   O OD2 . ASP A 173 ? 0.5876 0.6167 0.5877 0.0986  0.0173  -0.0231 173 ASP A OD2 
68   N N   . ARG A 174 ? 0.3817 0.3191 0.3530 0.0653  0.0210  -0.0449 174 ARG A N   
69   C CA  . ARG A 174 ? 0.3884 0.3216 0.3561 0.0599  0.0217  -0.0527 174 ARG A CA  
70   C C   . ARG A 174 ? 0.3901 0.3066 0.3546 0.0457  0.0204  -0.0563 174 ARG A C   
71   O O   . ARG A 174 ? 0.3774 0.2955 0.3473 0.0378  0.0183  -0.0522 174 ARG A O   
72   C CB  . ARG A 174 ? 0.4048 0.3670 0.3835 0.0562  0.0201  -0.0528 174 ARG A CB  
73   C CG  . ARG A 174 ? 0.4574 0.4411 0.4406 0.0678  0.0218  -0.0504 174 ARG A CG  
74   C CD  . ARG A 174 ? 0.5277 0.5019 0.5004 0.0788  0.0257  -0.0561 174 ARG A CD  
75   N NE  . ARG A 174 ? 0.5976 0.5799 0.5698 0.0741  0.0261  -0.0616 174 ARG A NE  
76   C CZ  . ARG A 174 ? 0.6254 0.6335 0.6046 0.0765  0.0271  -0.0603 174 ARG A CZ  
77   N NH1 . ARG A 174 ? 0.6240 0.6371 0.6005 0.0726  0.0278  -0.0650 174 ARG A NH1 
78   N NH2 . ARG A 174 ? 0.6147 0.6447 0.6030 0.0825  0.0275  -0.0543 174 ARG A NH2 
79   N N   . ILE A 175 ? 0.3883 0.2912 0.3444 0.0421  0.0216  -0.0643 175 ILE A N   
80   C CA  . ILE A 175 ? 0.3982 0.2909 0.3524 0.0277  0.0201  -0.0689 175 ILE A CA  
81   C C   . ILE A 175 ? 0.4133 0.3183 0.3682 0.0241  0.0190  -0.0755 175 ILE A C   
82   O O   . ILE A 175 ? 0.4304 0.3271 0.3760 0.0301  0.0213  -0.0816 175 ILE A O   
83   C CB  . ILE A 175 ? 0.4157 0.2753 0.3562 0.0246  0.0229  -0.0729 175 ILE A CB  
84   C CG1 . ILE A 175 ? 0.4187 0.2649 0.3569 0.0290  0.0244  -0.0651 175 ILE A CG1 
85   C CG2 . ILE A 175 ? 0.4238 0.2802 0.3648 0.0080  0.0210  -0.0784 175 ILE A CG2 
86   C CD1 . ILE A 175 ? 0.4538 0.2650 0.3769 0.0272  0.0282  -0.0675 175 ILE A CD1 
87   N N   . LEU A 176 ? 0.3919 0.3172 0.3570 0.0159  0.0156  -0.0739 176 LEU A N   
88   C CA  . LEU A 176 ? 0.3879 0.3269 0.3533 0.0132  0.0142  -0.0788 176 LEU A CA  
89   C C   . LEU A 176 ? 0.3827 0.3167 0.3459 0.0007  0.0119  -0.0847 176 LEU A C   
90   O O   . LEU A 176 ? 0.3744 0.3061 0.3422 -0.0072 0.0104  -0.0821 176 LEU A O   
91   C CB  . LEU A 176 ? 0.3835 0.3483 0.3604 0.0137  0.0124  -0.0724 176 LEU A CB  
92   C CG  . LEU A 176 ? 0.4050 0.3799 0.3868 0.0232  0.0142  -0.0661 176 LEU A CG  
93   C CD1 . LEU A 176 ? 0.4041 0.4016 0.3966 0.0202  0.0127  -0.0602 176 LEU A CD1 
94   C CD2 . LEU A 176 ? 0.4212 0.3946 0.3960 0.0343  0.0176  -0.0695 176 LEU A CD2 
95   N N   . ASP A 177 ? 0.3822 0.3154 0.3380 -0.0012 0.0116  -0.0930 177 ASP A N   
96   C CA  . ASP A 177 ? 0.3912 0.3234 0.3452 -0.0135 0.0090  -0.0995 177 ASP A CA  
97   C C   . ASP A 177 ? 0.3713 0.3282 0.3364 -0.0180 0.0051  -0.0951 177 ASP A C   
98   O O   . ASP A 177 ? 0.3721 0.3456 0.3413 -0.0120 0.0047  -0.0911 177 ASP A O   
99   C CB  . ASP A 177 ? 0.4426 0.3690 0.3847 -0.0141 0.0093  -0.1103 177 ASP A CB  
100  C CG  . ASP A 177 ? 0.5655 0.4830 0.5024 -0.0277 0.0076  -0.1190 177 ASP A CG  
101  O OD1 . ASP A 177 ? 0.5949 0.5097 0.5374 -0.0367 0.0066  -0.1165 177 ASP A OD1 
102  O OD2 . ASP A 177 ? 0.6165 0.5307 0.5435 -0.0299 0.0073  -0.1288 177 ASP A OD2 
103  N N   . ALA A 178 ? 0.3567 0.3158 0.3263 -0.0282 0.0028  -0.0955 178 ALA A N   
104  C CA  . ALA A 178 ? 0.3299 0.3113 0.3091 -0.0314 -0.0006 -0.0915 178 ALA A CA  
105  C C   . ALA A 178 ? 0.3343 0.3222 0.3121 -0.0418 -0.0036 -0.0991 178 ALA A C   
106  O O   . ALA A 178 ? 0.3309 0.3238 0.3149 -0.0495 -0.0051 -0.0979 178 ALA A O   
107  C CB  . ALA A 178 ? 0.3166 0.2988 0.3048 -0.0325 -0.0004 -0.0832 178 ALA A CB  
108  N N   . PRO A 179 ? 0.3438 0.3329 0.3132 -0.0424 -0.0045 -0.1074 179 PRO A N   
109  C CA  . PRO A 179 ? 0.3416 0.3393 0.3095 -0.0532 -0.0079 -0.1156 179 PRO A CA  
110  C C   . PRO A 179 ? 0.3256 0.3503 0.3032 -0.0543 -0.0119 -0.1113 179 PRO A C   
111  O O   . PRO A 179 ? 0.3238 0.3606 0.3044 -0.0454 -0.0124 -0.1046 179 PRO A O   
112  C CB  . PRO A 179 ? 0.3650 0.3613 0.3213 -0.0509 -0.0081 -0.1244 179 PRO A CB  
113  C CG  . PRO A 179 ? 0.3707 0.3691 0.3263 -0.0373 -0.0059 -0.1180 179 PRO A CG  
114  C CD  . PRO A 179 ? 0.3560 0.3412 0.3168 -0.0335 -0.0026 -0.1101 179 PRO A CD  
115  N N   . GLU A 180 ? 0.3204 0.3543 0.3023 -0.0650 -0.0144 -0.1150 180 GLU A N   
116  C CA  . GLU A 180 ? 0.3127 0.3737 0.3036 -0.0653 -0.0183 -0.1116 180 GLU A CA  
117  C C   . GLU A 180 ? 0.3038 0.3684 0.3040 -0.0596 -0.0172 -0.1006 180 GLU A C   
118  O O   . GLU A 180 ? 0.3097 0.3949 0.3157 -0.0564 -0.0198 -0.0966 180 GLU A O   
119  C CB  . GLU A 180 ? 0.3483 0.4288 0.3353 -0.0592 -0.0217 -0.1131 180 GLU A CB  
120  C CG  . GLU A 180 ? 0.4705 0.5508 0.4477 -0.0653 -0.0235 -0.1251 180 GLU A CG  
121  C CD  . GLU A 180 ? 0.6275 0.7344 0.6073 -0.0724 -0.0289 -0.1310 180 GLU A CD  
122  O OE1 . GLU A 180 ? 0.6607 0.7825 0.6509 -0.0759 -0.0306 -0.1273 180 GLU A OE1 
123  O OE2 . GLU A 180 ? 0.6966 0.8109 0.6678 -0.0743 -0.0315 -0.1395 180 GLU A OE2 
124  N N   . ILE A 181 ? 0.2908 0.3360 0.2919 -0.0581 -0.0134 -0.0959 181 ILE A N   
125  C CA  . ILE A 181 ? 0.2831 0.3318 0.2924 -0.0542 -0.0124 -0.0865 181 ILE A CA  
126  C C   . ILE A 181 ? 0.2795 0.3430 0.2966 -0.0614 -0.0143 -0.0868 181 ILE A C   
127  O O   . ILE A 181 ? 0.2817 0.3439 0.2984 -0.0720 -0.0145 -0.0933 181 ILE A O   
128  C CB  . ILE A 181 ? 0.2980 0.3259 0.3066 -0.0518 -0.0086 -0.0820 181 ILE A CB  
129  C CG1 . ILE A 181 ? 0.3072 0.3400 0.3224 -0.0459 -0.0079 -0.0728 181 ILE A CG1 
130  C CG2 . ILE A 181 ? 0.3158 0.3282 0.3227 -0.0613 -0.0067 -0.0855 181 ILE A CG2 
131  C CD1 . ILE A 181 ? 0.3218 0.3391 0.3357 -0.0412 -0.0049 -0.0681 181 ILE A CD1 
132  N N   . ARG A 182 ? 0.2637 0.3424 0.2871 -0.0558 -0.0154 -0.0806 182 ARG A N   
133  C CA  . ARG A 182 ? 0.2702 0.3669 0.3013 -0.0604 -0.0171 -0.0806 182 ARG A CA  
134  C C   . ARG A 182 ? 0.2693 0.3558 0.3048 -0.0656 -0.0140 -0.0778 182 ARG A C   
135  O O   . ARG A 182 ? 0.2739 0.3508 0.3101 -0.0599 -0.0118 -0.0712 182 ARG A O   
136  C CB  . ARG A 182 ? 0.3009 0.4152 0.3351 -0.0504 -0.0188 -0.0747 182 ARG A CB  
137  C CG  . ARG A 182 ? 0.3655 0.5040 0.4071 -0.0530 -0.0212 -0.0757 182 ARG A CG  
138  C CD  . ARG A 182 ? 0.4041 0.5600 0.4456 -0.0414 -0.0234 -0.0710 182 ARG A CD  
139  N NE  . ARG A 182 ? 0.4421 0.6107 0.4786 -0.0399 -0.0271 -0.0754 182 ARG A NE  
140  C CZ  . ARG A 182 ? 0.4482 0.6425 0.4877 -0.0427 -0.0312 -0.0802 182 ARG A CZ  
141  N NH1 . ARG A 182 ? 0.4421 0.6474 0.4756 -0.0410 -0.0346 -0.0844 182 ARG A NH1 
142  N NH2 . ARG A 182 ? 0.4320 0.6434 0.4805 -0.0467 -0.0318 -0.0809 182 ARG A NH2 
143  N N   . ASN A 183 ? 0.2692 0.3573 0.3066 -0.0773 -0.0137 -0.0830 183 ASN A N   
144  C CA  . ASN A 183 ? 0.2736 0.3517 0.3140 -0.0832 -0.0102 -0.0802 183 ASN A CA  
145  C C   . ASN A 183 ? 0.2732 0.3721 0.3227 -0.0810 -0.0106 -0.0758 183 ASN A C   
146  O O   . ASN A 183 ? 0.2752 0.3892 0.3305 -0.0896 -0.0107 -0.0787 183 ASN A O   
147  C CB  . ASN A 183 ? 0.2903 0.3603 0.3279 -0.0976 -0.0089 -0.0872 183 ASN A CB  
148  C CG  . ASN A 183 ? 0.3247 0.3804 0.3628 -0.1040 -0.0045 -0.0837 183 ASN A CG  
149  O OD1 . ASN A 183 ? 0.3281 0.3768 0.3673 -0.0968 -0.0026 -0.0763 183 ASN A OD1 
150  N ND2 . ASN A 183 ? 0.3340 0.3837 0.3700 -0.1181 -0.0027 -0.0892 183 ASN A ND2 
151  N N   . ASP A 184 ? 0.2624 0.3631 0.3129 -0.0696 -0.0107 -0.0693 184 ASP A N   
152  C CA  . ASP A 184 ? 0.2609 0.3780 0.3179 -0.0646 -0.0106 -0.0649 184 ASP A CA  
153  C C   . ASP A 184 ? 0.2733 0.3737 0.3287 -0.0595 -0.0075 -0.0584 184 ASP A C   
154  O O   . ASP A 184 ? 0.2840 0.3723 0.3348 -0.0525 -0.0074 -0.0553 184 ASP A O   
155  C CB  . ASP A 184 ? 0.2662 0.4006 0.3234 -0.0546 -0.0138 -0.0637 184 ASP A CB  
156  C CG  . ASP A 184 ? 0.2822 0.4341 0.3448 -0.0473 -0.0138 -0.0595 184 ASP A CG  
157  O OD1 . ASP A 184 ? 0.2890 0.4323 0.3524 -0.0448 -0.0108 -0.0550 184 ASP A OD1 
158  O OD2 . ASP A 184 ? 0.3003 0.4744 0.3651 -0.0430 -0.0168 -0.0607 184 ASP A OD2 
159  N N   . TYR A 185 ? 0.2641 0.3648 0.3231 -0.0639 -0.0050 -0.0567 185 TYR A N   
160  C CA  . TYR A 185 ? 0.2527 0.3387 0.3096 -0.0605 -0.0022 -0.0514 185 TYR A CA  
161  C C   . TYR A 185 ? 0.2411 0.3274 0.2968 -0.0495 -0.0024 -0.0468 185 TYR A C   
162  O O   . TYR A 185 ? 0.2564 0.3280 0.3083 -0.0465 -0.0011 -0.0435 185 TYR A O   
163  C CB  . TYR A 185 ? 0.2525 0.3452 0.3137 -0.0664 0.0005  -0.0505 185 TYR A CB  
164  C CG  . TYR A 185 ? 0.2708 0.3483 0.3288 -0.0649 0.0035  -0.0457 185 TYR A CG  
165  C CD1 . TYR A 185 ? 0.2958 0.3544 0.3488 -0.0700 0.0053  -0.0451 185 TYR A CD1 
166  C CD2 . TYR A 185 ? 0.2849 0.3675 0.3441 -0.0583 0.0047  -0.0421 185 TYR A CD2 
167  C CE1 . TYR A 185 ? 0.3030 0.3501 0.3525 -0.0682 0.0076  -0.0405 185 TYR A CE1 
168  C CE2 . TYR A 185 ? 0.2972 0.3674 0.3527 -0.0575 0.0071  -0.0385 185 TYR A CE2 
169  C CZ  . TYR A 185 ? 0.3146 0.3684 0.3656 -0.0624 0.0083  -0.0375 185 TYR A CZ  
170  O OH  . TYR A 185 ? 0.3435 0.3871 0.3904 -0.0614 0.0102  -0.0337 185 TYR A OH  
171  N N   . TYR A 186 ? 0.2205 0.3231 0.2787 -0.0435 -0.0039 -0.0465 186 TYR A N   
172  C CA  . TYR A 186 ? 0.2253 0.3262 0.2810 -0.0332 -0.0032 -0.0420 186 TYR A CA  
173  C C   . TYR A 186 ? 0.2407 0.3311 0.2904 -0.0276 -0.0042 -0.0401 186 TYR A C   
174  O O   . TYR A 186 ? 0.2689 0.3523 0.3149 -0.0210 -0.0029 -0.0363 186 TYR A O   
175  C CB  . TYR A 186 ? 0.2268 0.3483 0.2864 -0.0273 -0.0038 -0.0416 186 TYR A CB  
176  C CG  . TYR A 186 ? 0.2343 0.3685 0.3004 -0.0329 -0.0022 -0.0431 186 TYR A CG  
177  C CD1 . TYR A 186 ? 0.2488 0.3764 0.3143 -0.0317 0.0012  -0.0404 186 TYR A CD1 
178  C CD2 . TYR A 186 ? 0.2542 0.4051 0.3263 -0.0416 -0.0035 -0.0477 186 TYR A CD2 
179  C CE1 . TYR A 186 ? 0.2535 0.3928 0.3245 -0.0373 0.0034  -0.0415 186 TYR A CE1 
180  C CE2 . TYR A 186 ? 0.2603 0.4230 0.3385 -0.0485 -0.0013 -0.0489 186 TYR A CE2 
181  C CZ  . TYR A 186 ? 0.2643 0.4215 0.3420 -0.0459 0.0023  -0.0454 186 TYR A CZ  
182  O OH  . TYR A 186 ? 0.2718 0.4417 0.3551 -0.0522 0.0052  -0.0460 186 TYR A OH  
183  N N   . LEU A 187 ? 0.2106 0.2999 0.2588 -0.0305 -0.0061 -0.0430 187 LEU A N   
184  C CA  . LEU A 187 ? 0.2007 0.2830 0.2434 -0.0254 -0.0066 -0.0414 187 LEU A CA  
185  C C   . LEU A 187 ? 0.2176 0.2825 0.2572 -0.0265 -0.0048 -0.0395 187 LEU A C   
186  O O   . LEU A 187 ? 0.2350 0.2925 0.2758 -0.0318 -0.0039 -0.0407 187 LEU A O   
187  C CB  . LEU A 187 ? 0.1957 0.2866 0.2372 -0.0269 -0.0094 -0.0457 187 LEU A CB  
188  C CG  . LEU A 187 ? 0.2102 0.3230 0.2554 -0.0264 -0.0120 -0.0483 187 LEU A CG  
189  C CD1 . LEU A 187 ? 0.2225 0.3435 0.2652 -0.0286 -0.0150 -0.0534 187 LEU A CD1 
190  C CD2 . LEU A 187 ? 0.2183 0.3390 0.2623 -0.0159 -0.0118 -0.0432 187 LEU A CD2 
191  N N   . ASN A 188 ? 0.2006 0.2598 0.2358 -0.0215 -0.0041 -0.0363 188 ASN A N   
192  C CA  . ASN A 188 ? 0.1969 0.2436 0.2301 -0.0226 -0.0025 -0.0345 188 ASN A CA  
193  C C   . ASN A 188 ? 0.2018 0.2485 0.2316 -0.0210 -0.0030 -0.0354 188 ASN A C   
194  O O   . ASN A 188 ? 0.2012 0.2476 0.2274 -0.0172 -0.0021 -0.0324 188 ASN A O   
195  C CB  . ASN A 188 ? 0.2150 0.2555 0.2460 -0.0200 -0.0005 -0.0303 188 ASN A CB  
196  C CG  . ASN A 188 ? 0.2320 0.2714 0.2657 -0.0220 0.0002  -0.0303 188 ASN A CG  
197  O OD1 . ASN A 188 ? 0.2398 0.2738 0.2747 -0.0258 0.0007  -0.0306 188 ASN A OD1 
198  N ND2 . ASN A 188 ? 0.2195 0.2653 0.2537 -0.0188 0.0005  -0.0298 188 ASN A ND2 
199  N N   . LEU A 189 ? 0.2009 0.2473 0.2310 -0.0240 -0.0040 -0.0397 189 LEU A N   
200  C CA  . LEU A 189 ? 0.1933 0.2420 0.2197 -0.0223 -0.0046 -0.0421 189 LEU A CA  
201  C C   . LEU A 189 ? 0.1942 0.2361 0.2183 -0.0207 -0.0028 -0.0412 189 LEU A C   
202  O O   . LEU A 189 ? 0.2023 0.2468 0.2225 -0.0185 -0.0029 -0.0432 189 LEU A O   
203  C CB  . LEU A 189 ? 0.2037 0.2554 0.2300 -0.0265 -0.0064 -0.0484 189 LEU A CB  
204  C CG  . LEU A 189 ? 0.2293 0.2937 0.2589 -0.0286 -0.0086 -0.0501 189 LEU A CG  
205  C CD1 . LEU A 189 ? 0.2613 0.3276 0.2914 -0.0358 -0.0099 -0.0570 189 LEU A CD1 
206  C CD2 . LEU A 189 ? 0.2474 0.3238 0.2746 -0.0226 -0.0101 -0.0483 189 LEU A CD2 
207  N N   A VAL A 190 ? 0.1921 0.2274 0.2182 -0.0215 -0.0013 -0.0386 190 VAL A N   
208  N N   B VAL A 190 ? 0.1909 0.2261 0.2169 -0.0215 -0.0013 -0.0386 190 VAL A N   
209  C CA  A VAL A 190 ? 0.1997 0.2326 0.2247 -0.0194 0.0003  -0.0376 190 VAL A CA  
210  C CA  B VAL A 190 ? 0.1956 0.2283 0.2207 -0.0194 0.0003  -0.0378 190 VAL A CA  
211  C C   A VAL A 190 ? 0.2012 0.2340 0.2280 -0.0196 0.0018  -0.0329 190 VAL A C   
212  C C   B VAL A 190 ? 0.1971 0.2297 0.2240 -0.0196 0.0018  -0.0330 190 VAL A C   
213  O O   A VAL A 190 ? 0.2099 0.2401 0.2386 -0.0218 0.0016  -0.0311 190 VAL A O   
214  O O   B VAL A 190 ? 0.2032 0.2331 0.2321 -0.0218 0.0016  -0.0313 190 VAL A O   
215  C CB  A VAL A 190 ? 0.2194 0.2452 0.2440 -0.0194 0.0005  -0.0405 190 VAL A CB  
216  C CB  B VAL A 190 ? 0.2098 0.2351 0.2345 -0.0199 0.0003  -0.0408 190 VAL A CB  
217  C CG1 A VAL A 190 ? 0.2349 0.2587 0.2555 -0.0197 -0.0003 -0.0463 190 VAL A CG1 
218  C CG1 B VAL A 190 ? 0.2143 0.2395 0.2376 -0.0156 0.0020  -0.0404 190 VAL A CG1 
219  C CG2 A VAL A 190 ? 0.2202 0.2399 0.2472 -0.0225 0.0003  -0.0394 190 VAL A CG2 
220  C CG2 B VAL A 190 ? 0.2172 0.2399 0.2392 -0.0221 -0.0009 -0.0464 190 VAL A CG2 
221  N N   . ASP A 191 ? 0.1878 0.2243 0.2138 -0.0179 0.0035  -0.0313 191 ASP A N   
222  C CA  . ASP A 191 ? 0.1954 0.2331 0.2232 -0.0200 0.0050  -0.0276 191 ASP A CA  
223  C C   . ASP A 191 ? 0.1982 0.2429 0.2267 -0.0182 0.0067  -0.0272 191 ASP A C   
224  O O   . ASP A 191 ? 0.2031 0.2514 0.2289 -0.0153 0.0077  -0.0283 191 ASP A O   
225  C CB  . ASP A 191 ? 0.2107 0.2465 0.2357 -0.0217 0.0063  -0.0244 191 ASP A CB  
226  C CG  . ASP A 191 ? 0.2464 0.2801 0.2726 -0.0261 0.0075  -0.0219 191 ASP A CG  
227  O OD1 . ASP A 191 ? 0.2560 0.2900 0.2857 -0.0277 0.0064  -0.0229 191 ASP A OD1 
228  O OD2 . ASP A 191 ? 0.2378 0.2687 0.2604 -0.0283 0.0098  -0.0192 191 ASP A OD2 
229  N N   . TRP A 192 ? 0.1928 0.2412 0.2250 -0.0196 0.0071  -0.0259 192 TRP A N   
230  C CA  . TRP A 192 ? 0.1951 0.2541 0.2298 -0.0174 0.0086  -0.0254 192 TRP A CA  
231  C C   . TRP A 192 ? 0.2076 0.2735 0.2439 -0.0232 0.0107  -0.0223 192 TRP A C   
232  O O   . TRP A 192 ? 0.2113 0.2753 0.2490 -0.0282 0.0100  -0.0212 192 TRP A O   
233  C CB  . TRP A 192 ? 0.1949 0.2552 0.2326 -0.0142 0.0072  -0.0261 192 TRP A CB  
234  C CG  . TRP A 192 ? 0.2010 0.2704 0.2397 -0.0077 0.0085  -0.0269 192 TRP A CG  
235  C CD1 . TRP A 192 ? 0.2051 0.2881 0.2457 -0.0071 0.0110  -0.0259 192 TRP A CD1 
236  C CD2 . TRP A 192 ? 0.2077 0.2733 0.2451 -0.0004 0.0079  -0.0284 192 TRP A CD2 
237  N NE1 . TRP A 192 ? 0.2153 0.3051 0.2566 0.0012  0.0119  -0.0271 192 TRP A NE1 
238  C CE2 . TRP A 192 ? 0.2174 0.2954 0.2562 0.0058  0.0100  -0.0285 192 TRP A CE2 
239  C CE3 . TRP A 192 ? 0.2208 0.2732 0.2554 0.0016  0.0064  -0.0292 192 TRP A CE3 
240  C CZ2 . TRP A 192 ? 0.2227 0.2984 0.2592 0.0154  0.0104  -0.0297 192 TRP A CZ2 
241  C CZ3 . TRP A 192 ? 0.2315 0.2797 0.2631 0.0099  0.0070  -0.0301 192 TRP A CZ3 
242  C CH2 . TRP A 192 ? 0.2265 0.2860 0.2590 0.0175  0.0089  -0.0303 192 TRP A CH2 
243  N N   . SER A 193 ? 0.2025 0.2756 0.2375 -0.0232 0.0135  -0.0211 193 SER A N   
244  C CA  . SER A 193 ? 0.2086 0.2861 0.2436 -0.0301 0.0163  -0.0180 193 SER A CA  
245  C C   . SER A 193 ? 0.2272 0.3194 0.2687 -0.0337 0.0169  -0.0176 193 SER A C   
246  O O   . SER A 193 ? 0.2250 0.3279 0.2710 -0.0281 0.0159  -0.0190 193 SER A O   
247  C CB  . SER A 193 ? 0.2203 0.3007 0.2507 -0.0292 0.0197  -0.0162 193 SER A CB  
248  O OG  . SER A 193 ? 0.2133 0.3093 0.2471 -0.0263 0.0217  -0.0167 193 SER A OG  
249  N N   . SER A 194 ? 0.2363 0.3301 0.2777 -0.0429 0.0191  -0.0156 194 SER A N   
250  C CA  . SER A 194 ? 0.2611 0.3729 0.3092 -0.0484 0.0199  -0.0155 194 SER A CA  
251  C C   . SER A 194 ? 0.2708 0.4016 0.3227 -0.0450 0.0228  -0.0148 194 SER A C   
252  O O   . SER A 194 ? 0.2886 0.4397 0.3478 -0.0459 0.0228  -0.0152 194 SER A O   
253  C CB  . SER A 194 ? 0.2951 0.4020 0.3407 -0.0609 0.0221  -0.0142 194 SER A CB  
254  O OG  . SER A 194 ? 0.3304 0.4301 0.3696 -0.0640 0.0266  -0.0112 194 SER A OG  
255  N N   . GLY A 195 ? 0.2673 0.3935 0.3140 -0.0405 0.0252  -0.0139 195 GLY A N   
256  C CA  . GLY A 195 ? 0.2583 0.4006 0.3067 -0.0357 0.0282  -0.0136 195 GLY A CA  
257  C C   . GLY A 195 ? 0.2402 0.3846 0.2894 -0.0230 0.0260  -0.0169 195 GLY A C   
258  O O   . GLY A 195 ? 0.2365 0.3904 0.2848 -0.0168 0.0286  -0.0176 195 GLY A O   
259  N N   . ASN A 196 ? 0.2273 0.3607 0.2768 -0.0192 0.0217  -0.0190 196 ASN A N   
260  C CA  . ASN A 196 ? 0.2223 0.3530 0.2711 -0.0082 0.0198  -0.0220 196 ASN A CA  
261  C C   . ASN A 196 ? 0.2329 0.3520 0.2742 -0.0027 0.0204  -0.0245 196 ASN A C   
262  O O   . ASN A 196 ? 0.2496 0.3711 0.2889 0.0062  0.0213  -0.0272 196 ASN A O   
263  C CB  . ASN A 196 ? 0.2285 0.3807 0.2835 -0.0018 0.0211  -0.0220 196 ASN A CB  
264  C CG  . ASN A 196 ? 0.2733 0.4209 0.3277 0.0091  0.0188  -0.0240 196 ASN A CG  
265  O OD1 . ASN A 196 ? 0.2745 0.4054 0.3260 0.0093  0.0157  -0.0247 196 ASN A OD1 
266  N ND2 . ASN A 196 ? 0.2860 0.4485 0.3425 0.0190  0.0207  -0.0246 196 ASN A ND2 
267  N N   . VAL A 197 ? 0.2066 0.3127 0.2429 -0.0075 0.0197  -0.0239 197 VAL A N   
268  C CA  . VAL A 197 ? 0.1975 0.2941 0.2264 -0.0036 0.0194  -0.0266 197 VAL A CA  
269  C C   . VAL A 197 ? 0.1936 0.2746 0.2208 -0.0054 0.0157  -0.0280 197 VAL A C   
270  O O   . VAL A 197 ? 0.2060 0.2823 0.2342 -0.0112 0.0149  -0.0254 197 VAL A O   
271  C CB  . VAL A 197 ? 0.2078 0.3072 0.2318 -0.0067 0.0224  -0.0238 197 VAL A CB  
272  C CG1 . VAL A 197 ? 0.2271 0.3192 0.2433 -0.0024 0.0212  -0.0269 197 VAL A CG1 
273  C CG2 . VAL A 197 ? 0.2178 0.3346 0.2439 -0.0064 0.0269  -0.0218 197 VAL A CG2 
274  N N   . LEU A 198 ? 0.1939 0.2666 0.2178 -0.0007 0.0139  -0.0325 198 LEU A N   
275  C CA  . LEU A 198 ? 0.2097 0.2698 0.2321 -0.0031 0.0108  -0.0342 198 LEU A CA  
276  C C   . LEU A 198 ? 0.2103 0.2688 0.2275 -0.0040 0.0103  -0.0354 198 LEU A C   
277  O O   . LEU A 198 ? 0.2174 0.2786 0.2297 -0.0003 0.0112  -0.0384 198 LEU A O   
278  C CB  . LEU A 198 ? 0.2411 0.2923 0.2614 0.0011  0.0097  -0.0389 198 LEU A CB  
279  C CG  . LEU A 198 ? 0.2818 0.3258 0.3048 0.0010  0.0084  -0.0381 198 LEU A CG  
280  C CD1 . LEU A 198 ? 0.3023 0.3326 0.3197 0.0043  0.0081  -0.0429 198 LEU A CD1 
281  C CD2 . LEU A 198 ? 0.2641 0.3045 0.2900 -0.0055 0.0065  -0.0358 198 LEU A CD2 
282  N N   . ALA A 199 ? 0.1954 0.2496 0.2127 -0.0079 0.0086  -0.0337 199 ALA A N   
283  C CA  . ALA A 199 ? 0.2030 0.2572 0.2154 -0.0076 0.0073  -0.0345 199 ALA A CA  
284  C C   . ALA A 199 ? 0.2022 0.2507 0.2155 -0.0090 0.0042  -0.0389 199 ALA A C   
285  O O   . ALA A 199 ? 0.2065 0.2499 0.2239 -0.0118 0.0034  -0.0379 199 ALA A O   
286  C CB  . ALA A 199 ? 0.2028 0.2565 0.2146 -0.0098 0.0080  -0.0290 199 ALA A CB  
287  N N   . VAL A 200 ? 0.1986 0.2482 0.2075 -0.0079 0.0027  -0.0439 200 VAL A N   
288  C CA  . VAL A 200 ? 0.2152 0.2603 0.2248 -0.0112 0.0000  -0.0488 200 VAL A CA  
289  C C   . VAL A 200 ? 0.2191 0.2722 0.2256 -0.0115 -0.0024 -0.0510 200 VAL A C   
290  O O   . VAL A 200 ? 0.2221 0.2805 0.2229 -0.0088 -0.0024 -0.0534 200 VAL A O   
291  C CB  . VAL A 200 ? 0.2411 0.2781 0.2474 -0.0106 0.0006  -0.0548 200 VAL A CB  
292  C CG1 . VAL A 200 ? 0.2568 0.2865 0.2633 -0.0160 -0.0013 -0.0595 200 VAL A CG1 
293  C CG2 . VAL A 200 ? 0.2595 0.2919 0.2679 -0.0072 0.0032  -0.0521 200 VAL A CG2 
294  N N   . ALA A 201 ? 0.2136 0.2693 0.2235 -0.0145 -0.0045 -0.0505 201 ALA A N   
295  C CA  . ALA A 201 ? 0.2316 0.2985 0.2394 -0.0141 -0.0074 -0.0525 201 ALA A CA  
296  C C   . ALA A 201 ? 0.2398 0.3071 0.2474 -0.0197 -0.0096 -0.0608 201 ALA A C   
297  O O   . ALA A 201 ? 0.2437 0.3054 0.2556 -0.0250 -0.0098 -0.0624 201 ALA A O   
298  C CB  . ALA A 201 ? 0.2385 0.3100 0.2504 -0.0135 -0.0081 -0.0477 201 ALA A CB  
299  N N   . LEU A 202 ? 0.2402 0.3134 0.2417 -0.0192 -0.0111 -0.0662 202 LEU A N   
300  C CA  . LEU A 202 ? 0.2445 0.3180 0.2441 -0.0258 -0.0133 -0.0752 202 LEU A CA  
301  C C   . LEU A 202 ? 0.2668 0.3599 0.2655 -0.0261 -0.0174 -0.0777 202 LEU A C   
302  O O   . LEU A 202 ? 0.2776 0.3787 0.2695 -0.0221 -0.0184 -0.0793 202 LEU A O   
303  C CB  . LEU A 202 ? 0.2504 0.3132 0.2422 -0.0253 -0.0116 -0.0813 202 LEU A CB  
304  C CG  . LEU A 202 ? 0.2655 0.3108 0.2574 -0.0231 -0.0077 -0.0791 202 LEU A CG  
305  C CD1 . LEU A 202 ? 0.2788 0.3145 0.2615 -0.0207 -0.0059 -0.0858 202 LEU A CD1 
306  C CD2 . LEU A 202 ? 0.2702 0.3045 0.2671 -0.0291 -0.0072 -0.0788 202 LEU A CD2 
307  N N   . ASP A 203 ? 0.2656 0.3681 0.2709 -0.0306 -0.0195 -0.0779 203 ASP A N   
308  C CA  . ASP A 203 ? 0.2601 0.3854 0.2666 -0.0305 -0.0238 -0.0798 203 ASP A CA  
309  C C   . ASP A 203 ? 0.2460 0.3809 0.2491 -0.0193 -0.0241 -0.0719 203 ASP A C   
310  O O   . ASP A 203 ? 0.2395 0.3713 0.2461 -0.0145 -0.0222 -0.0640 203 ASP A O   
311  C CB  . ASP A 203 ? 0.2993 0.4322 0.3011 -0.0378 -0.0269 -0.0907 203 ASP A CB  
312  C CG  . ASP A 203 ? 0.3774 0.5383 0.3813 -0.0379 -0.0319 -0.0930 203 ASP A CG  
313  O OD1 . ASP A 203 ? 0.3663 0.5394 0.3776 -0.0350 -0.0327 -0.0875 203 ASP A OD1 
314  O OD2 . ASP A 203 ? 0.4361 0.6078 0.4338 -0.0400 -0.0351 -0.1002 203 ASP A OD2 
315  N N   . ASN A 204 ? 0.2529 0.3970 0.2479 -0.0151 -0.0258 -0.0738 204 ASN A N   
316  C CA  . ASN A 204 ? 0.2616 0.4135 0.2516 -0.0044 -0.0257 -0.0656 204 ASN A CA  
317  C C   . ASN A 204 ? 0.2591 0.3975 0.2423 0.0004  -0.0215 -0.0611 204 ASN A C   
318  O O   . ASN A 204 ? 0.2716 0.4155 0.2480 0.0081  -0.0210 -0.0552 204 ASN A O   
319  C CB  . ASN A 204 ? 0.2814 0.4566 0.2664 -0.0015 -0.0306 -0.0690 204 ASN A CB  
320  C CG  . ASN A 204 ? 0.3235 0.5003 0.3005 -0.0050 -0.0319 -0.0778 204 ASN A CG  
321  O OD1 . ASN A 204 ? 0.3263 0.4864 0.3020 -0.0103 -0.0293 -0.0826 204 ASN A OD1 
322  N ND2 . ASN A 204 ? 0.3410 0.5382 0.3117 -0.0016 -0.0361 -0.0804 204 ASN A ND2 
323  N N   . SER A 205 ? 0.2385 0.3608 0.2227 -0.0038 -0.0184 -0.0636 205 SER A N   
324  C CA  . SER A 205 ? 0.2453 0.3581 0.2243 0.0002  -0.0142 -0.0599 205 SER A CA  
325  C C   . SER A 205 ? 0.2435 0.3412 0.2285 -0.0012 -0.0104 -0.0552 205 SER A C   
326  O O   . SER A 205 ? 0.2522 0.3435 0.2440 -0.0062 -0.0108 -0.0573 205 SER A O   
327  C CB  . SER A 205 ? 0.2767 0.3872 0.2495 -0.0016 -0.0140 -0.0684 205 SER A CB  
328  O OG  . SER A 205 ? 0.3124 0.4375 0.2775 0.0002  -0.0173 -0.0728 205 SER A OG  
329  N N   . VAL A 206 ? 0.2288 0.3216 0.2109 0.0025  -0.0063 -0.0493 206 VAL A N   
330  C CA  . VAL A 206 ? 0.2304 0.3118 0.2180 0.0007  -0.0029 -0.0458 206 VAL A CA  
331  C C   . VAL A 206 ? 0.2274 0.3070 0.2114 0.0023  0.0000  -0.0481 206 VAL A C   
332  O O   . VAL A 206 ? 0.2243 0.3103 0.2014 0.0061  0.0016  -0.0465 206 VAL A O   
333  C CB  . VAL A 206 ? 0.2392 0.3176 0.2274 0.0025  -0.0003 -0.0365 206 VAL A CB  
334  C CG1 . VAL A 206 ? 0.2529 0.3228 0.2459 -0.0002 0.0031  -0.0339 206 VAL A CG1 
335  C CG2 . VAL A 206 ? 0.2372 0.3166 0.2284 0.0025  -0.0027 -0.0344 206 VAL A CG2 
336  N N   . TYR A 207 ? 0.2190 0.2904 0.2069 0.0002  0.0009  -0.0517 207 TYR A N   
337  C CA  . TYR A 207 ? 0.2198 0.2896 0.2051 0.0032  0.0041  -0.0537 207 TYR A CA  
338  C C   . TYR A 207 ? 0.2208 0.2882 0.2125 0.0032  0.0073  -0.0479 207 TYR A C   
339  O O   . TYR A 207 ? 0.2201 0.2822 0.2180 -0.0001 0.0064  -0.0455 207 TYR A O   
340  C CB  . TYR A 207 ? 0.2428 0.3042 0.2260 0.0024  0.0031  -0.0626 207 TYR A CB  
341  C CG  . TYR A 207 ? 0.2803 0.3455 0.2560 0.0014  0.0003  -0.0699 207 TYR A CG  
342  C CD1 . TYR A 207 ? 0.3068 0.3748 0.2842 -0.0037 -0.0038 -0.0724 207 TYR A CD1 
343  C CD2 . TYR A 207 ? 0.3106 0.3789 0.2775 0.0056  0.0018  -0.0746 207 TYR A CD2 
344  C CE1 . TYR A 207 ? 0.3362 0.4113 0.3070 -0.0054 -0.0068 -0.0795 207 TYR A CE1 
345  C CE2 . TYR A 207 ? 0.3328 0.4062 0.2920 0.0042  -0.0011 -0.0818 207 TYR A CE2 
346  C CZ  . TYR A 207 ? 0.3615 0.4390 0.3230 -0.0016 -0.0057 -0.0843 207 TYR A CZ  
347  O OH  . TYR A 207 ? 0.4209 0.5059 0.3751 -0.0039 -0.0091 -0.0923 207 TYR A OH  
348  N N   . LEU A 208 ? 0.2130 0.2857 0.2030 0.0065  0.0109  -0.0462 208 LEU A N   
349  C CA  . LEU A 208 ? 0.2320 0.3064 0.2284 0.0061  0.0138  -0.0416 208 LEU A CA  
350  C C   . LEU A 208 ? 0.2550 0.3295 0.2515 0.0110  0.0156  -0.0459 208 LEU A C   
351  O O   . LEU A 208 ? 0.2725 0.3496 0.2624 0.0155  0.0169  -0.0502 208 LEU A O   
352  C CB  . LEU A 208 ? 0.2267 0.3102 0.2218 0.0055  0.0175  -0.0352 208 LEU A CB  
353  C CG  . LEU A 208 ? 0.2452 0.3264 0.2374 0.0025  0.0168  -0.0299 208 LEU A CG  
354  C CD1 . LEU A 208 ? 0.2576 0.3448 0.2467 0.0014  0.0216  -0.0233 208 LEU A CD1 
355  C CD2 . LEU A 208 ? 0.2530 0.3257 0.2511 -0.0018 0.0146  -0.0280 208 LEU A CD2 
356  N N   . TRP A 209 ? 0.2522 0.3233 0.2549 0.0110  0.0156  -0.0450 209 TRP A N   
357  C CA  . TRP A 209 ? 0.2756 0.3463 0.2781 0.0175  0.0174  -0.0481 209 TRP A CA  
358  C C   . TRP A 209 ? 0.2770 0.3598 0.2873 0.0181  0.0197  -0.0427 209 TRP A C   
359  O O   . TRP A 209 ? 0.2573 0.3389 0.2737 0.0136  0.0182  -0.0392 209 TRP A O   
360  C CB  . TRP A 209 ? 0.2960 0.3506 0.2973 0.0179  0.0151  -0.0522 209 TRP A CB  
361  C CG  . TRP A 209 ? 0.3247 0.3746 0.3239 0.0261  0.0171  -0.0549 209 TRP A CG  
362  C CD1 . TRP A 209 ? 0.3510 0.3957 0.3419 0.0329  0.0191  -0.0608 209 TRP A CD1 
363  C CD2 . TRP A 209 ? 0.3266 0.3748 0.3307 0.0292  0.0172  -0.0518 209 TRP A CD2 
364  N NE1 . TRP A 209 ? 0.3577 0.3967 0.3477 0.0410  0.0209  -0.0613 209 TRP A NE1 
365  C CE2 . TRP A 209 ? 0.3484 0.3904 0.3466 0.0392  0.0196  -0.0554 209 TRP A CE2 
366  C CE3 . TRP A 209 ? 0.3260 0.3782 0.3380 0.0253  0.0157  -0.0463 209 TRP A CE3 
367  C CZ2 . TRP A 209 ? 0.3531 0.3930 0.3533 0.0461  0.0203  -0.0529 209 TRP A CZ2 
368  C CZ3 . TRP A 209 ? 0.3362 0.3874 0.3503 0.0311  0.0160  -0.0444 209 TRP A CZ3 
369  C CH2 . TRP A 209 ? 0.3438 0.3898 0.3523 0.0419  0.0183  -0.0472 209 TRP A CH2 
370  N N   A SER A 210 ? 0.2860 0.3822 0.2961 0.0230  0.0235  -0.0423 210 SER A N   
371  N N   B SER A 210 ? 0.2871 0.3828 0.2970 0.0232  0.0234  -0.0425 210 SER A N   
372  C CA  A SER A 210 ? 0.3010 0.4131 0.3193 0.0229  0.0258  -0.0377 210 SER A CA  
373  C CA  B SER A 210 ? 0.3021 0.4137 0.3201 0.0235  0.0257  -0.0381 210 SER A CA  
374  C C   A SER A 210 ? 0.3175 0.4281 0.3382 0.0308  0.0253  -0.0397 210 SER A C   
375  C C   B SER A 210 ? 0.3182 0.4268 0.3383 0.0310  0.0250  -0.0401 210 SER A C   
376  O O   A SER A 210 ? 0.3214 0.4307 0.3369 0.0400  0.0272  -0.0437 210 SER A O   
377  O O   B SER A 210 ? 0.3230 0.4273 0.3373 0.0400  0.0265  -0.0445 210 SER A O   
378  C CB  A SER A 210 ? 0.3212 0.4508 0.3387 0.0248  0.0305  -0.0362 210 SER A CB  
379  C CB  B SER A 210 ? 0.3235 0.4524 0.3403 0.0266  0.0305  -0.0372 210 SER A CB  
380  O OG  A SER A 210 ? 0.3526 0.4816 0.3661 0.0182  0.0312  -0.0334 210 SER A OG  
381  O OG  B SER A 210 ? 0.3527 0.5003 0.3783 0.0272  0.0328  -0.0338 210 SER A OG  
382  N N   . ALA A 211 ? 0.3245 0.4339 0.3514 0.0280  0.0229  -0.0368 211 ALA A N   
383  C CA  . ALA A 211 ? 0.3449 0.4512 0.3729 0.0361  0.0221  -0.0375 211 ALA A CA  
384  C C   . ALA A 211 ? 0.3763 0.5005 0.4069 0.0464  0.0253  -0.0372 211 ALA A C   
385  O O   . ALA A 211 ? 0.3958 0.5124 0.4220 0.0573  0.0258  -0.0395 211 ALA A O   
386  C CB  . ALA A 211 ? 0.3470 0.4524 0.3811 0.0305  0.0190  -0.0338 211 ALA A CB  
387  N N   . SER A 212 ? 0.3799 0.5271 0.4166 0.0434  0.0279  -0.0345 212 SER A N   
388  C CA  . SER A 212 ? 0.3995 0.5690 0.4403 0.0529  0.0313  -0.0341 212 SER A CA  
389  C C   . SER A 212 ? 0.4138 0.5809 0.4462 0.0636  0.0350  -0.0387 212 SER A C   
390  O O   . SER A 212 ? 0.4233 0.5993 0.4556 0.0765  0.0373  -0.0398 212 SER A O   
391  C CB  . SER A 212 ? 0.4281 0.6245 0.4787 0.0442  0.0333  -0.0298 212 SER A CB  
392  O OG  . SER A 212 ? 0.4888 0.6895 0.5359 0.0397  0.0369  -0.0299 212 SER A OG  
393  N N   . SER A 213 ? 0.4063 0.5629 0.4311 0.0592  0.0358  -0.0414 213 SER A N   
394  C CA  . SER A 213 ? 0.3987 0.5544 0.4145 0.0684  0.0395  -0.0464 213 SER A CA  
395  C C   . SER A 213 ? 0.4018 0.5291 0.4052 0.0714  0.0377  -0.0530 213 SER A C   
396  O O   . SER A 213 ? 0.4088 0.5315 0.4032 0.0808  0.0405  -0.0585 213 SER A O   
397  C CB  . SER A 213 ? 0.4066 0.5763 0.4218 0.0620  0.0426  -0.0447 213 SER A CB  
398  O OG  . SER A 213 ? 0.4413 0.5966 0.4532 0.0511  0.0395  -0.0439 213 SER A OG  
399  N N   . GLY A 214 ? 0.3869 0.4965 0.3895 0.0626  0.0334  -0.0530 214 GLY A N   
400  C CA  . GLY A 214 ? 0.3890 0.4740 0.3809 0.0621  0.0314  -0.0594 214 GLY A CA  
401  C C   . GLY A 214 ? 0.3701 0.4552 0.3558 0.0562  0.0312  -0.0622 214 GLY A C   
402  O O   . GLY A 214 ? 0.3949 0.4631 0.3716 0.0549  0.0294  -0.0684 214 GLY A O   
403  N N   A ASP A 215 ? 0.3481 0.4524 0.3378 0.0526  0.0331  -0.0577 215 ASP A N   
404  N N   B ASP A 215 ? 0.3473 0.4514 0.3373 0.0522  0.0329  -0.0575 215 ASP A N   
405  C CA  A ASP A 215 ? 0.3477 0.4536 0.3306 0.0482  0.0330  -0.0589 215 ASP A CA  
406  C CA  B ASP A 215 ? 0.3436 0.4503 0.3273 0.0476  0.0330  -0.0583 215 ASP A CA  
407  C C   A ASP A 215 ? 0.3443 0.4377 0.3270 0.0390  0.0281  -0.0586 215 ASP A C   
408  C C   B ASP A 215 ? 0.3432 0.4366 0.3261 0.0388  0.0280  -0.0584 215 ASP A C   
409  O O   A ASP A 215 ? 0.3372 0.4283 0.3277 0.0334  0.0259  -0.0540 215 ASP A O   
410  O O   B ASP A 215 ? 0.3386 0.4295 0.3291 0.0330  0.0257  -0.0539 215 ASP A O   
411  C CB  A ASP A 215 ? 0.3654 0.4926 0.3522 0.0457  0.0367  -0.0525 215 ASP A CB  
412  C CB  B ASP A 215 ? 0.3506 0.4781 0.3396 0.0439  0.0363  -0.0511 215 ASP A CB  
413  C CG  A ASP A 215 ? 0.4298 0.5734 0.4158 0.0548  0.0423  -0.0535 215 ASP A CG  
414  C CG  B ASP A 215 ? 0.4024 0.5329 0.3841 0.0399  0.0369  -0.0499 215 ASP A CG  
415  O OD1 A ASP A 215 ? 0.4387 0.5754 0.4175 0.0643  0.0433  -0.0605 215 ASP A OD1 
416  O OD1 B ASP A 215 ? 0.4101 0.5443 0.3828 0.0457  0.0392  -0.0543 215 ASP A OD1 
417  O OD2 A ASP A 215 ? 0.4602 0.6236 0.4526 0.0522  0.0459  -0.0476 215 ASP A OD2 
418  O OD2 B ASP A 215 ? 0.4312 0.5602 0.4152 0.0318  0.0352  -0.0445 215 ASP A OD2 
419  N N   . ILE A 216 ? 0.3436 0.4300 0.3170 0.0379  0.0263  -0.0639 216 ILE A N   
420  C CA  . ILE A 216 ? 0.3448 0.4229 0.3178 0.0303  0.0215  -0.0643 216 ILE A CA  
421  C C   . ILE A 216 ? 0.3386 0.4268 0.3063 0.0283  0.0215  -0.0622 216 ILE A C   
422  O O   . ILE A 216 ? 0.3443 0.4388 0.3038 0.0330  0.0238  -0.0656 216 ILE A O   
423  C CB  . ILE A 216 ? 0.3708 0.4320 0.3371 0.0299  0.0188  -0.0733 216 ILE A CB  
424  C CG1 . ILE A 216 ? 0.3961 0.4439 0.3658 0.0322  0.0192  -0.0742 216 ILE A CG1 
425  C CG2 . ILE A 216 ? 0.3749 0.4331 0.3406 0.0219  0.0140  -0.0745 216 ILE A CG2 
426  C CD1 . ILE A 216 ? 0.4326 0.4621 0.3923 0.0344  0.0191  -0.0836 216 ILE A CD1 
427  N N   . LEU A 217 ? 0.3143 0.4037 0.2854 0.0225  0.0192  -0.0567 217 LEU A N   
428  C CA  . LEU A 217 ? 0.3116 0.4091 0.2766 0.0217  0.0190  -0.0535 217 LEU A CA  
429  C C   . LEU A 217 ? 0.2929 0.3854 0.2579 0.0175  0.0138  -0.0541 217 LEU A C   
430  O O   . LEU A 217 ? 0.2984 0.3847 0.2710 0.0135  0.0121  -0.0514 217 LEU A O   
431  C CB  . LEU A 217 ? 0.3235 0.4285 0.2923 0.0197  0.0228  -0.0435 217 LEU A CB  
432  C CG  . LEU A 217 ? 0.3517 0.4615 0.3132 0.0192  0.0233  -0.0378 217 LEU A CG  
433  C CD1 . LEU A 217 ? 0.3570 0.4771 0.3086 0.0242  0.0266  -0.0391 217 LEU A CD1 
434  C CD2 . LEU A 217 ? 0.3673 0.4765 0.3328 0.0146  0.0262  -0.0281 217 LEU A CD2 
435  N N   . GLN A 218 ? 0.2768 0.3741 0.2332 0.0186  0.0113  -0.0576 218 GLN A N   
436  C CA  . GLN A 218 ? 0.2717 0.3696 0.2287 0.0154  0.0065  -0.0573 218 GLN A CA  
437  C C   . GLN A 218 ? 0.2741 0.3773 0.2298 0.0168  0.0083  -0.0468 218 GLN A C   
438  O O   . GLN A 218 ? 0.2959 0.4072 0.2428 0.0206  0.0099  -0.0443 218 GLN A O   
439  C CB  . GLN A 218 ? 0.2784 0.3823 0.2265 0.0161  0.0027  -0.0654 218 GLN A CB  
440  C CG  . GLN A 218 ? 0.3129 0.4209 0.2636 0.0127  -0.0027 -0.0659 218 GLN A CG  
441  C CD  . GLN A 218 ? 0.3810 0.4984 0.3237 0.0121  -0.0070 -0.0744 218 GLN A CD  
442  O OE1 . GLN A 218 ? 0.4103 0.5305 0.3439 0.0147  -0.0059 -0.0798 218 GLN A OE1 
443  N NE2 . GLN A 218 ? 0.3790 0.5031 0.3249 0.0086  -0.0120 -0.0763 218 GLN A NE2 
444  N N   . LEU A 219 ? 0.2606 0.3579 0.2237 0.0138  0.0088  -0.0405 219 LEU A N   
445  C CA  . LEU A 219 ? 0.2644 0.3618 0.2250 0.0146  0.0115  -0.0306 219 LEU A CA  
446  C C   . LEU A 219 ? 0.2693 0.3716 0.2226 0.0182  0.0086  -0.0280 219 LEU A C   
447  O O   . LEU A 219 ? 0.2969 0.4017 0.2416 0.0217  0.0113  -0.0210 219 LEU A O   
448  C CB  . LEU A 219 ? 0.2579 0.3459 0.2272 0.0101  0.0124  -0.0262 219 LEU A CB  
449  C CG  . LEU A 219 ? 0.2722 0.3554 0.2380 0.0097  0.0157  -0.0165 219 LEU A CG  
450  C CD1 . LEU A 219 ? 0.2746 0.3609 0.2362 0.0089  0.0216  -0.0118 219 LEU A CD1 
451  C CD2 . LEU A 219 ? 0.2837 0.3568 0.2571 0.0051  0.0155  -0.0143 219 LEU A CD2 
452  N N   . LEU A 220 ? 0.2623 0.3664 0.2187 0.0175  0.0034  -0.0329 220 LEU A N   
453  C CA  . LEU A 220 ? 0.2605 0.3724 0.2117 0.0217  0.0000  -0.0305 220 LEU A CA  
454  C C   . LEU A 220 ? 0.2630 0.3829 0.2175 0.0197  -0.0059 -0.0391 220 LEU A C   
455  O O   . LEU A 220 ? 0.2540 0.3689 0.2160 0.0140  -0.0071 -0.0457 220 LEU A O   
456  C CB  . LEU A 220 ? 0.2644 0.3683 0.2174 0.0229  0.0015  -0.0215 220 LEU A CB  
457  C CG  . LEU A 220 ? 0.2940 0.3904 0.2582 0.0181  0.0000  -0.0236 220 LEU A CG  
458  C CD1 . LEU A 220 ? 0.3108 0.4158 0.2773 0.0202  -0.0050 -0.0257 220 LEU A CD1 
459  C CD2 . LEU A 220 ? 0.3096 0.3926 0.2755 0.0165  0.0045  -0.0161 220 LEU A CD2 
460  N N   . GLN A 221 ? 0.2662 0.3991 0.2150 0.0243  -0.0095 -0.0385 221 GLN A N   
461  C CA  . GLN A 221 ? 0.2801 0.4247 0.2327 0.0219  -0.0155 -0.0458 221 GLN A CA  
462  C C   . GLN A 221 ? 0.2904 0.4458 0.2409 0.0289  -0.0179 -0.0393 221 GLN A C   
463  O O   . GLN A 221 ? 0.2975 0.4564 0.2379 0.0368  -0.0166 -0.0321 221 GLN A O   
464  C CB  . GLN A 221 ? 0.3163 0.4711 0.2630 0.0199  -0.0184 -0.0559 221 GLN A CB  
465  C CG  . GLN A 221 ? 0.3849 0.5524 0.3364 0.0146  -0.0245 -0.0648 221 GLN A CG  
466  C CD  . GLN A 221 ? 0.4894 0.6650 0.4337 0.0111  -0.0273 -0.0759 221 GLN A CD  
467  O OE1 . GLN A 221 ? 0.5209 0.7043 0.4543 0.0165  -0.0273 -0.0757 221 GLN A OE1 
468  N NE2 . GLN A 221 ? 0.5130 0.6863 0.4621 0.0017  -0.0296 -0.0862 221 GLN A NE2 
469  N N   . MET A 222 ? 0.2756 0.4373 0.2347 0.0267  -0.0214 -0.0415 222 MET A N   
470  C CA  . MET A 222 ? 0.2844 0.4593 0.2423 0.0347  -0.0241 -0.0361 222 MET A CA  
471  C C   . MET A 222 ? 0.2932 0.4893 0.2418 0.0405  -0.0284 -0.0378 222 MET A C   
472  O O   . MET A 222 ? 0.2918 0.4960 0.2388 0.0349  -0.0311 -0.0472 222 MET A O   
473  C CB  . MET A 222 ? 0.2935 0.4757 0.2633 0.0300  -0.0272 -0.0404 222 MET A CB  
474  C CG  . MET A 222 ? 0.3350 0.4975 0.3129 0.0249  -0.0232 -0.0385 222 MET A CG  
475  S SD  . MET A 222 ? 0.4386 0.5878 0.4136 0.0341  -0.0189 -0.0260 222 MET A SD  
476  C CE  . MET A 222 ? 0.4634 0.5924 0.4296 0.0342  -0.0130 -0.0202 222 MET A CE  
477  N N   . GLU A 223 ? 0.3066 0.5094 0.2472 0.0521  -0.0285 -0.0286 223 GLU A N   
478  C CA  . GLU A 223 ? 0.3374 0.5603 0.2672 0.0593  -0.0323 -0.0287 223 GLU A CA  
479  C C   . GLU A 223 ? 0.3452 0.5969 0.2787 0.0620  -0.0396 -0.0332 223 GLU A C   
480  O O   . GLU A 223 ? 0.3650 0.6360 0.2896 0.0672  -0.0435 -0.0345 223 GLU A O   
481  C CB  . GLU A 223 ? 0.3938 0.6087 0.3095 0.0717  -0.0282 -0.0154 223 GLU A CB  
482  C CG  . GLU A 223 ? 0.5032 0.6977 0.4119 0.0689  -0.0215 -0.0117 223 GLU A CG  
483  C CD  . GLU A 223 ? 0.6337 0.8387 0.5292 0.0723  -0.0220 -0.0125 223 GLU A CD  
484  O OE1 . GLU A 223 ? 0.6701 0.8617 0.5562 0.0744  -0.0159 -0.0053 223 GLU A OE1 
485  O OE2 . GLU A 223 ? 0.6663 0.8938 0.5605 0.0725  -0.0283 -0.0206 223 GLU A OE2 
486  N N   . GLN A 224 ? 0.3326 0.5897 0.2784 0.0594  -0.0413 -0.0350 224 GLN A N   
487  C CA  . GLN A 224 ? 0.3273 0.6163 0.2776 0.0622  -0.0482 -0.0390 224 GLN A CA  
488  C C   . GLN A 224 ? 0.2946 0.5931 0.2592 0.0474  -0.0514 -0.0513 224 GLN A C   
489  O O   . GLN A 224 ? 0.2927 0.5708 0.2650 0.0387  -0.0476 -0.0530 224 GLN A O   
490  C CB  . GLN A 224 ? 0.3642 0.6574 0.3139 0.0766  -0.0474 -0.0278 224 GLN A CB  
491  C CG  . GLN A 224 ? 0.4343 0.7271 0.3670 0.0927  -0.0462 -0.0165 224 GLN A CG  
492  C CD  . GLN A 224 ? 0.5111 0.8037 0.4408 0.1086  -0.0447 -0.0050 224 GLN A CD  
493  O OE1 . GLN A 224 ? 0.5303 0.8351 0.4483 0.1237  -0.0463 0.0028  224 GLN A OE1 
494  N NE2 . GLN A 224 ? 0.5213 0.7989 0.4600 0.1065  -0.0413 -0.0035 224 GLN A NE2 
495  N N   . PRO A 225 ? 0.2631 0.5925 0.2304 0.0436  -0.0582 -0.0600 225 PRO A N   
496  C CA  . PRO A 225 ? 0.2490 0.5868 0.2290 0.0278  -0.0606 -0.0717 225 PRO A CA  
497  C C   . PRO A 225 ? 0.2548 0.5895 0.2476 0.0270  -0.0583 -0.0680 225 PRO A C   
498  O O   . PRO A 225 ? 0.2736 0.6164 0.2668 0.0401  -0.0580 -0.0588 225 PRO A O   
499  C CB  . PRO A 225 ? 0.2432 0.6203 0.2234 0.0268  -0.0686 -0.0792 225 PRO A CB  
500  C CG  . PRO A 225 ? 0.2534 0.6356 0.2178 0.0386  -0.0700 -0.0747 225 PRO A CG  
501  C CD  . PRO A 225 ? 0.2455 0.6044 0.2041 0.0528  -0.0639 -0.0596 225 PRO A CD  
502  N N   . GLY A 226 ? 0.2374 0.5603 0.2392 0.0123  -0.0566 -0.0751 226 GLY A N   
503  C CA  . GLY A 226 ? 0.2538 0.5739 0.2675 0.0097  -0.0542 -0.0727 226 GLY A CA  
504  C C   . GLY A 226 ? 0.2828 0.5700 0.2954 0.0140  -0.0475 -0.0641 226 GLY A C   
505  O O   . GLY A 226 ? 0.3139 0.5928 0.3353 0.0091  -0.0448 -0.0636 226 GLY A O   
506  N N   . GLU A 227 ? 0.2772 0.5467 0.2789 0.0228  -0.0447 -0.0571 227 GLU A N   
507  C CA  . GLU A 227 ? 0.2758 0.5158 0.2758 0.0263  -0.0385 -0.0491 227 GLU A CA  
508  C C   . GLU A 227 ? 0.2635 0.4802 0.2663 0.0141  -0.0353 -0.0540 227 GLU A C   
509  O O   . GLU A 227 ? 0.2633 0.4781 0.2626 0.0074  -0.0364 -0.0609 227 GLU A O   
510  C CB  . GLU A 227 ? 0.3253 0.5546 0.3124 0.0383  -0.0360 -0.0398 227 GLU A CB  
511  C CG  . GLU A 227 ? 0.4240 0.6664 0.4061 0.0536  -0.0370 -0.0312 227 GLU A CG  
512  C CD  . GLU A 227 ? 0.5436 0.7717 0.5110 0.0644  -0.0337 -0.0215 227 GLU A CD  
513  O OE1 . GLU A 227 ? 0.5262 0.7486 0.4866 0.0610  -0.0331 -0.0234 227 GLU A OE1 
514  O OE2 . GLU A 227 ? 0.6014 0.8233 0.5634 0.0764  -0.0312 -0.0120 227 GLU A OE2 
515  N N   . TYR A 228 ? 0.2369 0.4365 0.2453 0.0119  -0.0314 -0.0507 228 TYR A N   
516  C CA  . TYR A 228 ? 0.2326 0.4100 0.2429 0.0025  -0.0281 -0.0538 228 TYR A CA  
517  C C   . TYR A 228 ? 0.2128 0.3684 0.2223 0.0066  -0.0231 -0.0457 228 TYR A C   
518  O O   . TYR A 228 ? 0.2097 0.3659 0.2183 0.0148  -0.0219 -0.0388 228 TYR A O   
519  C CB  . TYR A 228 ? 0.2324 0.4129 0.2519 -0.0097 -0.0292 -0.0616 228 TYR A CB  
520  C CG  . TYR A 228 ? 0.2374 0.4260 0.2657 -0.0092 -0.0288 -0.0589 228 TYR A CG  
521  C CD1 . TYR A 228 ? 0.2489 0.4195 0.2803 -0.0098 -0.0247 -0.0546 228 TYR A CD1 
522  C CD2 . TYR A 228 ? 0.2429 0.4589 0.2764 -0.0085 -0.0325 -0.0614 228 TYR A CD2 
523  C CE1 . TYR A 228 ? 0.2482 0.4262 0.2866 -0.0088 -0.0239 -0.0524 228 TYR A CE1 
524  C CE2 . TYR A 228 ? 0.2431 0.4684 0.2847 -0.0073 -0.0317 -0.0590 228 TYR A CE2 
525  C CZ  . TYR A 228 ? 0.2502 0.4556 0.2939 -0.0074 -0.0272 -0.0546 228 TYR A CZ  
526  O OH  . TYR A 228 ? 0.2625 0.4773 0.3134 -0.0057 -0.0259 -0.0525 228 TYR A OH  
527  N N   . ILE A 229 ? 0.2031 0.3396 0.2118 0.0013  -0.0201 -0.0467 229 ILE A N   
528  C CA  . ILE A 229 ? 0.2005 0.3186 0.2089 0.0031  -0.0157 -0.0403 229 ILE A CA  
529  C C   . ILE A 229 ? 0.1995 0.3131 0.2162 -0.0019 -0.0149 -0.0412 229 ILE A C   
530  O O   . ILE A 229 ? 0.1974 0.3118 0.2192 -0.0100 -0.0159 -0.0472 229 ILE A O   
531  C CB  . ILE A 229 ? 0.2154 0.3193 0.2205 0.0002  -0.0130 -0.0410 229 ILE A CB  
532  C CG1 . ILE A 229 ? 0.2303 0.3403 0.2269 0.0040  -0.0137 -0.0416 229 ILE A CG1 
533  C CG2 . ILE A 229 ? 0.2220 0.3100 0.2271 0.0011  -0.0088 -0.0345 229 ILE A CG2 
534  C CD1 . ILE A 229 ? 0.2543 0.3660 0.2437 0.0124  -0.0124 -0.0339 229 ILE A CD1 
535  N N   . SER A 230 ? 0.1903 0.2981 0.2072 0.0029  -0.0126 -0.0352 230 SER A N   
536  C CA  . SER A 230 ? 0.1875 0.2921 0.2112 -0.0008 -0.0116 -0.0356 230 SER A CA  
537  C C   . SER A 230 ? 0.1829 0.2679 0.2060 -0.0031 -0.0079 -0.0325 230 SER A C   
538  O O   . SER A 230 ? 0.1911 0.2722 0.2193 -0.0079 -0.0072 -0.0339 230 SER A O   
539  C CB  . SER A 230 ? 0.1874 0.3041 0.2127 0.0060  -0.0122 -0.0329 230 SER A CB  
540  O OG  . SER A 230 ? 0.2300 0.3443 0.2473 0.0165  -0.0111 -0.0267 230 SER A OG  
541  N N   . SER A 231 ? 0.1816 0.2557 0.1987 -0.0006 -0.0057 -0.0286 231 SER A N   
542  C CA  . SER A 231 ? 0.1804 0.2395 0.1976 -0.0040 -0.0028 -0.0266 231 SER A CA  
543  C C   . SER A 231 ? 0.1829 0.2353 0.1948 -0.0037 -0.0008 -0.0241 231 SER A C   
544  O O   . SER A 231 ? 0.1899 0.2456 0.1958 0.0012  -0.0005 -0.0215 231 SER A O   
545  C CB  . SER A 231 ? 0.2107 0.2621 0.2265 -0.0013 -0.0005 -0.0227 231 SER A CB  
546  O OG  . SER A 231 ? 0.2301 0.2819 0.2391 0.0067  0.0003  -0.0183 231 SER A OG  
547  N N   . VAL A 232 ? 0.1848 0.2294 0.1988 -0.0083 0.0009  -0.0243 232 VAL A N   
548  C CA  . VAL A 232 ? 0.1905 0.2307 0.2008 -0.0088 0.0035  -0.0216 232 VAL A CA  
549  C C   . VAL A 232 ? 0.1900 0.2211 0.2019 -0.0131 0.0058  -0.0196 232 VAL A C   
550  O O   . VAL A 232 ? 0.1941 0.2237 0.2110 -0.0161 0.0049  -0.0218 232 VAL A O   
551  C CB  . VAL A 232 ? 0.2077 0.2532 0.2185 -0.0097 0.0029  -0.0250 232 VAL A CB  
552  C CG1 . VAL A 232 ? 0.2142 0.2690 0.2216 -0.0061 0.0007  -0.0276 232 VAL A CG1 
553  C CG2 . VAL A 232 ? 0.2180 0.2619 0.2347 -0.0134 0.0019  -0.0292 232 VAL A CG2 
554  N N   . ALA A 233 ? 0.1806 0.2062 0.1878 -0.0141 0.0090  -0.0155 233 ALA A N   
555  C CA  . ALA A 233 ? 0.1903 0.2096 0.1990 -0.0198 0.0111  -0.0146 233 ALA A CA  
556  C C   . ALA A 233 ? 0.2091 0.2272 0.2140 -0.0227 0.0146  -0.0113 233 ALA A C   
557  O O   . ALA A 233 ? 0.2157 0.2281 0.2128 -0.0205 0.0170  -0.0073 233 ALA A O   
558  C CB  . ALA A 233 ? 0.1896 0.1986 0.1957 -0.0202 0.0119  -0.0134 233 ALA A CB  
559  N N   . TRP A 234 ? 0.2078 0.2315 0.2176 -0.0275 0.0152  -0.0124 234 TRP A N   
560  C CA  . TRP A 234 ? 0.2054 0.2312 0.2131 -0.0318 0.0189  -0.0096 234 TRP A CA  
561  C C   . TRP A 234 ? 0.2208 0.2357 0.2248 -0.0388 0.0218  -0.0074 234 TRP A C   
562  O O   . TRP A 234 ? 0.2210 0.2329 0.2281 -0.0422 0.0203  -0.0097 234 TRP A O   
563  C CB  . TRP A 234 ? 0.1890 0.2283 0.2045 -0.0338 0.0184  -0.0120 234 TRP A CB  
564  C CG  . TRP A 234 ? 0.1853 0.2333 0.2026 -0.0275 0.0168  -0.0146 234 TRP A CG  
565  C CD1 . TRP A 234 ? 0.1913 0.2416 0.2129 -0.0239 0.0136  -0.0186 234 TRP A CD1 
566  C CD2 . TRP A 234 ? 0.1867 0.2411 0.2004 -0.0246 0.0189  -0.0135 234 TRP A CD2 
567  N NE1 . TRP A 234 ? 0.1911 0.2476 0.2116 -0.0191 0.0136  -0.0207 234 TRP A NE1 
568  C CE2 . TRP A 234 ? 0.1935 0.2539 0.2095 -0.0192 0.0167  -0.0179 234 TRP A CE2 
569  C CE3 . TRP A 234 ? 0.1965 0.2519 0.2046 -0.0265 0.0230  -0.0093 234 TRP A CE3 
570  C CZ2 . TRP A 234 ? 0.2099 0.2775 0.2226 -0.0150 0.0181  -0.0188 234 TRP A CZ2 
571  C CZ3 . TRP A 234 ? 0.2136 0.2776 0.2188 -0.0222 0.0245  -0.0095 234 TRP A CZ3 
572  C CH2 . TRP A 234 ? 0.2180 0.2885 0.2255 -0.0164 0.0219  -0.0145 234 TRP A CH2 
573  N N   . ILE A 235 ? 0.2394 0.2490 0.2365 -0.0422 0.0262  -0.0032 235 ILE A N   
574  C CA  . ILE A 235 ? 0.2625 0.2608 0.2551 -0.0512 0.0298  -0.0016 235 ILE A CA  
575  C C   . ILE A 235 ? 0.2781 0.2911 0.2801 -0.0594 0.0292  -0.0047 235 ILE A C   
576  O O   . ILE A 235 ? 0.2602 0.2903 0.2699 -0.0565 0.0274  -0.0063 235 ILE A O   
577  C CB  . ILE A 235 ? 0.2677 0.2561 0.2496 -0.0536 0.0355  0.0042  235 ILE A CB  
578  C CG1 . ILE A 235 ? 0.2936 0.2615 0.2666 -0.0618 0.0396  0.0058  235 ILE A CG1 
579  C CG2 . ILE A 235 ? 0.2641 0.2690 0.2501 -0.0579 0.0379  0.0053  235 ILE A CG2 
580  C CD1 . ILE A 235 ? 0.3120 0.2635 0.2711 -0.0627 0.0458  0.0125  235 ILE A CD1 
581  N N   . LYS A 236 ? 0.3024 0.3093 0.3036 -0.0685 0.0303  -0.0060 236 LYS A N   
582  C CA  . LYS A 236 ? 0.3210 0.3445 0.3312 -0.0760 0.0290  -0.0091 236 LYS A CA  
583  C C   . LYS A 236 ? 0.3297 0.3723 0.3454 -0.0791 0.0312  -0.0077 236 LYS A C   
584  O O   . LYS A 236 ? 0.3404 0.4025 0.3657 -0.0768 0.0284  -0.0101 236 LYS A O   
585  C CB  . LYS A 236 ? 0.3626 0.3764 0.3690 -0.0873 0.0304  -0.0111 236 LYS A CB  
586  N N   . GLU A 237 ? 0.3365 0.3740 0.3455 -0.0827 0.0364  -0.0036 237 GLU A N   
587  C CA  . GLU A 237 ? 0.3456 0.4027 0.3594 -0.0855 0.0394  -0.0019 237 GLU A CA  
588  C C   . GLU A 237 ? 0.3373 0.4073 0.3551 -0.0732 0.0374  -0.0021 237 GLU A C   
589  O O   . GLU A 237 ? 0.3425 0.4318 0.3656 -0.0733 0.0393  -0.0017 237 GLU A O   
590  C CB  . GLU A 237 ? 0.4046 0.4505 0.4083 -0.0933 0.0463  0.0033  237 GLU A CB  
591  N N   . GLY A 238 ? 0.3224 0.3821 0.3371 -0.0632 0.0341  -0.0029 238 GLY A N   
592  C CA  . GLY A 238 ? 0.3195 0.3883 0.3365 -0.0527 0.0321  -0.0042 238 GLY A CA  
593  C C   . GLY A 238 ? 0.3220 0.3906 0.3316 -0.0492 0.0356  -0.0007 238 GLY A C   
594  O O   . GLY A 238 ? 0.3333 0.4101 0.3439 -0.0411 0.0341  -0.0026 238 GLY A O   
595  N N   . ASN A 239 ? 0.3146 0.3719 0.3151 -0.0548 0.0403  0.0045  239 ASN A N   
596  C CA  . ASN A 239 ? 0.3193 0.3766 0.3111 -0.0506 0.0439  0.0087  239 ASN A CA  
597  C C   . ASN A 239 ? 0.3029 0.3455 0.2849 -0.0419 0.0420  0.0107  239 ASN A C   
598  O O   . ASN A 239 ? 0.3081 0.3538 0.2835 -0.0358 0.0431  0.0129  239 ASN A O   
599  C CB  . ASN A 239 ? 0.3706 0.4259 0.3569 -0.0606 0.0509  0.0142  239 ASN A CB  
600  C CG  . ASN A 239 ? 0.4566 0.4913 0.4364 -0.0699 0.0535  0.0168  239 ASN A CG  
601  O OD1 . ASN A 239 ? 0.4719 0.4978 0.4545 -0.0714 0.0500  0.0135  239 ASN A OD1 
602  N ND2 . ASN A 239 ? 0.4821 0.5079 0.4521 -0.0770 0.0603  0.0228  239 ASN A ND2 
603  N N   . TYR A 240 ? 0.2800 0.3084 0.2607 -0.0413 0.0394  0.0099  240 TYR A N   
604  C CA  . TYR A 240 ? 0.2809 0.2980 0.2536 -0.0326 0.0373  0.0116  240 TYR A CA  
605  C C   . TYR A 240 ? 0.2594 0.2798 0.2396 -0.0276 0.0311  0.0058  240 TYR A C   
606  O O   . TYR A 240 ? 0.2498 0.2694 0.2371 -0.0322 0.0295  0.0025  240 TYR A O   
607  C CB  . TYR A 240 ? 0.3078 0.3028 0.2703 -0.0355 0.0407  0.0165  240 TYR A CB  
608  C CG  . TYR A 240 ? 0.3694 0.3568 0.3225 -0.0422 0.0478  0.0229  240 TYR A CG  
609  C CD1 . TYR A 240 ? 0.3922 0.3851 0.3383 -0.0378 0.0505  0.0274  240 TYR A CD1 
610  C CD2 . TYR A 240 ? 0.4197 0.3964 0.3713 -0.0541 0.0521  0.0239  240 TYR A CD2 
611  C CE1 . TYR A 240 ? 0.4326 0.4186 0.3695 -0.0446 0.0577  0.0338  240 TYR A CE1 
612  C CE2 . TYR A 240 ? 0.4503 0.4200 0.3933 -0.0623 0.0592  0.0296  240 TYR A CE2 
613  C CZ  . TYR A 240 ? 0.4677 0.4416 0.4031 -0.0573 0.0623  0.0351  240 TYR A CZ  
614  O OH  . TYR A 240 ? 0.5158 0.4829 0.4421 -0.0659 0.0700  0.0414  240 TYR A OH  
615  N N   . LEU A 241 ? 0.2343 0.2580 0.2121 -0.0189 0.0279  0.0047  241 LEU A N   
616  C CA  . LEU A 241 ? 0.2245 0.2513 0.2087 -0.0150 0.0224  -0.0006 241 LEU A CA  
617  C C   . LEU A 241 ? 0.2331 0.2520 0.2108 -0.0089 0.0211  0.0017  241 LEU A C   
618  O O   . LEU A 241 ? 0.2422 0.2611 0.2113 -0.0033 0.0221  0.0056  241 LEU A O   
619  C CB  . LEU A 241 ? 0.2184 0.2590 0.2062 -0.0110 0.0194  -0.0056 241 LEU A CB  
620  C CG  . LEU A 241 ? 0.2208 0.2640 0.2147 -0.0089 0.0143  -0.0113 241 LEU A CG  
621  C CD1 . LEU A 241 ? 0.2228 0.2640 0.2251 -0.0138 0.0136  -0.0140 241 LEU A CD1 
622  C CD2 . LEU A 241 ? 0.2369 0.2902 0.2309 -0.0053 0.0118  -0.0164 241 LEU A CD2 
623  N N   . ALA A 242 ? 0.2299 0.2423 0.2109 -0.0092 0.0193  0.0000  242 ALA A N   
624  C CA  . ALA A 242 ? 0.2271 0.2353 0.2033 -0.0019 0.0179  0.0018  242 ALA A CA  
625  C C   . ALA A 242 ? 0.2307 0.2539 0.2135 0.0018  0.0127  -0.0036 242 ALA A C   
626  O O   . ALA A 242 ? 0.2216 0.2503 0.2132 -0.0026 0.0105  -0.0088 242 ALA A O   
627  C CB  . ALA A 242 ? 0.2394 0.2348 0.2157 -0.0039 0.0189  0.0019  242 ALA A CB  
628  N N   . VAL A 243 ? 0.2341 0.2639 0.2124 0.0097  0.0107  -0.0023 243 VAL A N   
629  C CA  . VAL A 243 ? 0.2197 0.2650 0.2037 0.0116  0.0057  -0.0080 243 VAL A CA  
630  C C   . VAL A 243 ? 0.2265 0.2758 0.2091 0.0188  0.0038  -0.0065 243 VAL A C   
631  O O   . VAL A 243 ? 0.2435 0.2922 0.2171 0.0266  0.0048  -0.0012 243 VAL A O   
632  C CB  . VAL A 243 ? 0.2327 0.2889 0.2126 0.0138  0.0046  -0.0091 243 VAL A CB  
633  C CG1 . VAL A 243 ? 0.2298 0.3015 0.2145 0.0144  -0.0006 -0.0159 243 VAL A CG1 
634  C CG2 . VAL A 243 ? 0.2320 0.2857 0.2132 0.0081  0.0071  -0.0104 243 VAL A CG2 
635  N N   . GLY A 244 ? 0.2106 0.2641 0.2013 0.0168  0.0017  -0.0105 244 GLY A N   
636  C CA  . GLY A 244 ? 0.2223 0.2839 0.2135 0.0238  -0.0001 -0.0098 244 GLY A CA  
637  C C   . GLY A 244 ? 0.2271 0.3102 0.2223 0.0247  -0.0050 -0.0146 244 GLY A C   
638  O O   . GLY A 244 ? 0.2160 0.3044 0.2167 0.0173  -0.0069 -0.0206 244 GLY A O   
639  N N   . THR A 245 ? 0.2300 0.3261 0.2220 0.0341  -0.0069 -0.0123 245 THR A N   
640  C CA  . THR A 245 ? 0.2446 0.3641 0.2400 0.0344  -0.0119 -0.0173 245 THR A CA  
641  C C   . THR A 245 ? 0.2439 0.3819 0.2459 0.0381  -0.0147 -0.0191 245 THR A C   
642  O O   . THR A 245 ? 0.2414 0.3747 0.2427 0.0447  -0.0125 -0.0148 245 THR A O   
643  C CB  . THR A 245 ? 0.2716 0.3972 0.2564 0.0422  -0.0128 -0.0134 245 THR A CB  
644  O OG1 . THR A 245 ? 0.2768 0.4072 0.2555 0.0550  -0.0127 -0.0069 245 THR A OG1 
645  C CG2 . THR A 245 ? 0.2877 0.3947 0.2644 0.0404  -0.0087 -0.0095 245 THR A CG2 
646  N N   . SER A 246 ? 0.2495 0.4093 0.2579 0.0333  -0.0193 -0.0260 246 SER A N   
647  C CA  . SER A 246 ? 0.2499 0.4343 0.2659 0.0353  -0.0225 -0.0288 246 SER A CA  
648  C C   . SER A 246 ? 0.2732 0.4702 0.2831 0.0509  -0.0235 -0.0223 246 SER A C   
649  O O   . SER A 246 ? 0.2795 0.4939 0.2951 0.0560  -0.0246 -0.0222 246 SER A O   
650  C CB  . SER A 246 ? 0.2450 0.4494 0.2664 0.0260  -0.0273 -0.0377 246 SER A CB  
651  O OG  . SER A 246 ? 0.2452 0.4589 0.2586 0.0308  -0.0301 -0.0376 246 SER A OG  
652  N N   . SER A 247 ? 0.2805 0.4706 0.2785 0.0590  -0.0229 -0.0168 247 SER A N   
653  C CA  . SER A 247 ? 0.2841 0.4821 0.2732 0.0755  -0.0232 -0.0091 247 SER A CA  
654  C C   . SER A 247 ? 0.2948 0.4658 0.2758 0.0841  -0.0171 -0.0006 247 SER A C   
655  O O   . SER A 247 ? 0.3107 0.4771 0.2798 0.0979  -0.0156 0.0074  247 SER A O   
656  C CB  . SER A 247 ? 0.3126 0.5153 0.2909 0.0800  -0.0251 -0.0068 247 SER A CB  
657  O OG  . SER A 247 ? 0.3644 0.5405 0.3365 0.0737  -0.0209 -0.0051 247 SER A OG  
658  N N   . ALA A 248 ? 0.2795 0.4314 0.2656 0.0760  -0.0134 -0.0022 248 ALA A N   
659  C CA  . ALA A 248 ? 0.2829 0.4091 0.2618 0.0820  -0.0077 0.0039  248 ALA A CA  
660  C C   . ALA A 248 ? 0.2999 0.3985 0.2648 0.0837  -0.0031 0.0106  248 ALA A C   
661  O O   . ALA A 248 ? 0.3197 0.3985 0.2739 0.0926  0.0014  0.0173  248 ALA A O   
662  C CB  . ALA A 248 ? 0.2714 0.4085 0.2477 0.0978  -0.0076 0.0080  248 ALA A CB  
663  N N   . GLU A 249 ? 0.2882 0.3844 0.2525 0.0749  -0.0038 0.0088  249 GLU A N   
664  C CA  . GLU A 249 ? 0.2994 0.3717 0.2514 0.0746  0.0010  0.0150  249 GLU A CA  
665  C C   . GLU A 249 ? 0.2861 0.3413 0.2432 0.0609  0.0040  0.0117  249 GLU A C   
666  O O   . GLU A 249 ? 0.2745 0.3387 0.2435 0.0515  0.0013  0.0045  249 GLU A O   
667  C CB  . GLU A 249 ? 0.3354 0.4184 0.2821 0.0752  -0.0010 0.0158  249 GLU A CB  
668  C CG  . GLU A 249 ? 0.3979 0.5049 0.3412 0.0873  -0.0055 0.0174  249 GLU A CG  
669  C CD  . GLU A 249 ? 0.5014 0.6231 0.4420 0.0849  -0.0087 0.0150  249 GLU A CD  
670  O OE1 . GLU A 249 ? 0.5200 0.6485 0.4491 0.0959  -0.0094 0.0210  249 GLU A OE1 
671  O OE2 . GLU A 249 ? 0.5241 0.6500 0.4731 0.0727  -0.0103 0.0072  249 GLU A OE2 
672  N N   . VAL A 250 ? 0.2989 0.3294 0.2462 0.0598  0.0095  0.0172  250 VAL A N   
673  C CA  . VAL A 250 ? 0.3089 0.3257 0.2599 0.0469  0.0122  0.0147  250 VAL A CA  
674  C C   . VAL A 250 ? 0.3168 0.3269 0.2586 0.0453  0.0152  0.0194  250 VAL A C   
675  O O   . VAL A 250 ? 0.3312 0.3234 0.2598 0.0496  0.0200  0.0269  250 VAL A O   
676  C CB  . VAL A 250 ? 0.3496 0.3442 0.2977 0.0446  0.0166  0.0161  250 VAL A CB  
677  C CG1 . VAL A 250 ? 0.3680 0.3534 0.3211 0.0309  0.0185  0.0130  250 VAL A CG1 
678  C CG2 . VAL A 250 ? 0.3541 0.3567 0.3094 0.0486  0.0142  0.0124  250 VAL A CG2 
679  N N   . GLN A 251 ? 0.3029 0.3269 0.2504 0.0396  0.0128  0.0152  251 GLN A N   
680  C CA  . GLN A 251 ? 0.3085 0.3300 0.2483 0.0379  0.0156  0.0189  251 GLN A CA  
681  C C   . GLN A 251 ? 0.3156 0.3249 0.2583 0.0264  0.0198  0.0184  251 GLN A C   
682  O O   . GLN A 251 ? 0.3233 0.3337 0.2766 0.0193  0.0184  0.0127  251 GLN A O   
683  C CB  . GLN A 251 ? 0.3252 0.3685 0.2688 0.0384  0.0111  0.0139  251 GLN A CB  
684  C CG  . GLN A 251 ? 0.3690 0.4303 0.3129 0.0474  0.0057  0.0123  251 GLN A CG  
685  C CD  . GLN A 251 ? 0.4176 0.4984 0.3612 0.0481  0.0018  0.0079  251 GLN A CD  
686  O OE1 . GLN A 251 ? 0.4186 0.5003 0.3632 0.0418  0.0028  0.0047  251 GLN A OE1 
687  N NE2 . GLN A 251 ? 0.4220 0.5205 0.3639 0.0562  -0.0029 0.0072  251 GLN A NE2 
688  N N   . LEU A 252 ? 0.3083 0.3064 0.2409 0.0246  0.0251  0.0246  252 LEU A N   
689  C CA  . LEU A 252 ? 0.3085 0.2988 0.2440 0.0132  0.0292  0.0242  252 LEU A CA  
690  C C   . LEU A 252 ? 0.2884 0.2905 0.2226 0.0113  0.0304  0.0247  252 LEU A C   
691  O O   . LEU A 252 ? 0.2926 0.2926 0.2149 0.0164  0.0331  0.0310  252 LEU A O   
692  C CB  . LEU A 252 ? 0.3383 0.3042 0.2632 0.0100  0.0355  0.0307  252 LEU A CB  
693  C CG  . LEU A 252 ? 0.3699 0.3303 0.2991 -0.0036 0.0394  0.0293  252 LEU A CG  
694  C CD1 . LEU A 252 ? 0.3639 0.3317 0.3078 -0.0096 0.0354  0.0213  252 LEU A CD1 
695  C CD2 . LEU A 252 ? 0.4122 0.3472 0.3284 -0.0082 0.0464  0.0358  252 LEU A CD2 
696  N N   . TRP A 253 ? 0.2696 0.2844 0.2150 0.0055  0.0284  0.0181  253 TRP A N   
697  C CA  . TRP A 253 ? 0.2698 0.2974 0.2147 0.0046  0.0296  0.0173  253 TRP A CA  
698  C C   . TRP A 253 ? 0.2765 0.3027 0.2245 -0.0052 0.0347  0.0184  253 TRP A C   
699  O O   . TRP A 253 ? 0.2816 0.3060 0.2388 -0.0118 0.0342  0.0150  253 TRP A O   
700  C CB  . TRP A 253 ? 0.2678 0.3118 0.2217 0.0067  0.0238  0.0085  253 TRP A CB  
701  C CG  . TRP A 253 ? 0.2760 0.3278 0.2255 0.0153  0.0192  0.0072  253 TRP A CG  
702  C CD1 . TRP A 253 ? 0.2953 0.3458 0.2458 0.0197  0.0156  0.0068  253 TRP A CD1 
703  C CD2 . TRP A 253 ? 0.2836 0.3475 0.2260 0.0207  0.0181  0.0067  253 TRP A CD2 
704  N NE1 . TRP A 253 ? 0.2968 0.3594 0.2420 0.0273  0.0121  0.0061  253 TRP A NE1 
705  C CE2 . TRP A 253 ? 0.2930 0.3638 0.2330 0.0277  0.0132  0.0055  253 TRP A CE2 
706  C CE3 . TRP A 253 ? 0.2937 0.3652 0.2318 0.0203  0.0207  0.0064  253 TRP A CE3 
707  C CZ2 . TRP A 253 ? 0.3026 0.3875 0.2356 0.0338  0.0104  0.0041  253 TRP A CZ2 
708  C CZ3 . TRP A 253 ? 0.3012 0.3845 0.2311 0.0268  0.0184  0.0053  253 TRP A CZ3 
709  C CH2 . TRP A 253 ? 0.2991 0.3892 0.2267 0.0331  0.0130  0.0037  253 TRP A CH2 
710  N N   . ASP A 254 ? 0.2666 0.2959 0.2073 -0.0061 0.0394  0.0230  254 ASP A N   
711  C CA  . ASP A 254 ? 0.2663 0.2997 0.2110 -0.0154 0.0444  0.0238  254 ASP A CA  
712  C C   . ASP A 254 ? 0.2656 0.3191 0.2177 -0.0128 0.0420  0.0174  254 ASP A C   
713  O O   . ASP A 254 ? 0.2602 0.3215 0.2055 -0.0066 0.0421  0.0179  254 ASP A O   
714  C CB  . ASP A 254 ? 0.2950 0.3205 0.2265 -0.0180 0.0516  0.0327  254 ASP A CB  
715  C CG  . ASP A 254 ? 0.3483 0.3818 0.2841 -0.0286 0.0574  0.0338  254 ASP A CG  
716  O OD1 . ASP A 254 ? 0.3341 0.3863 0.2809 -0.0294 0.0557  0.0279  254 ASP A OD1 
717  O OD2 . ASP A 254 ? 0.4081 0.4296 0.3351 -0.0357 0.0641  0.0409  254 ASP A OD2 
718  N N   . VAL A 255 ? 0.2581 0.3191 0.2228 -0.0164 0.0398  0.0113  255 VAL A N   
719  C CA  . VAL A 255 ? 0.2630 0.3397 0.2334 -0.0123 0.0376  0.0048  255 VAL A CA  
720  C C   . VAL A 255 ? 0.2677 0.3580 0.2378 -0.0142 0.0430  0.0062  255 VAL A C   
721  O O   . VAL A 255 ? 0.2808 0.3827 0.2513 -0.0085 0.0422  0.0017  255 VAL A O   
722  C CB  . VAL A 255 ? 0.2606 0.3392 0.2426 -0.0128 0.0331  -0.0020 255 VAL A CB  
723  C CG1 . VAL A 255 ? 0.2625 0.3297 0.2445 -0.0109 0.0283  -0.0035 255 VAL A CG1 
724  C CG2 . VAL A 255 ? 0.2653 0.3468 0.2556 -0.0207 0.0356  -0.0011 255 VAL A CG2 
725  N N   . GLN A 256 ? 0.2601 0.3490 0.2286 -0.0222 0.0488  0.0124  256 GLN A N   
726  C CA  . GLN A 256 ? 0.2674 0.3716 0.2355 -0.0247 0.0548  0.0145  256 GLN A CA  
727  C C   . GLN A 256 ? 0.2741 0.3780 0.2283 -0.0187 0.0572  0.0185  256 GLN A C   
728  O O   . GLN A 256 ? 0.2834 0.4023 0.2361 -0.0142 0.0591  0.0165  256 GLN A O   
729  C CB  . GLN A 256 ? 0.3069 0.4099 0.2773 -0.0372 0.0605  0.0197  256 GLN A CB  
730  N N   . GLN A 257 ? 0.2764 0.3636 0.2195 -0.0176 0.0573  0.0244  257 GLN A N   
731  C CA  . GLN A 257 ? 0.2858 0.3724 0.2144 -0.0106 0.0590  0.0290  257 GLN A CA  
732  C C   . GLN A 257 ? 0.2726 0.3631 0.1993 0.0001  0.0517  0.0228  257 GLN A C   
733  O O   . GLN A 257 ? 0.2857 0.3811 0.2014 0.0068  0.0520  0.0246  257 GLN A O   
734  C CB  . GLN A 257 ? 0.3159 0.3822 0.2318 -0.0123 0.0623  0.0386  257 GLN A CB  
735  C CG  . GLN A 257 ? 0.3734 0.4322 0.2876 -0.0245 0.0703  0.0453  257 GLN A CG  
736  C CD  . GLN A 257 ? 0.4484 0.4846 0.3456 -0.0236 0.0744  0.0554  257 GLN A CD  
737  O OE1 . GLN A 257 ? 0.4859 0.5218 0.3700 -0.0216 0.0796  0.0625  257 GLN A OE1 
738  N NE2 . GLN A 257 ? 0.4417 0.4581 0.3373 -0.0237 0.0722  0.0562  257 GLN A NE2 
739  N N   . GLN A 258 ? 0.2620 0.3508 0.1986 0.0012  0.0454  0.0157  258 GLN A N   
740  C CA  . GLN A 258 ? 0.2736 0.3655 0.2093 0.0088  0.0386  0.0093  258 GLN A CA  
741  C C   . GLN A 258 ? 0.2914 0.3773 0.2150 0.0148  0.0371  0.0147  258 GLN A C   
742  O O   . GLN A 258 ? 0.3042 0.3989 0.2193 0.0216  0.0352  0.0134  258 GLN A O   
743  C CB  . GLN A 258 ? 0.2926 0.3995 0.2285 0.0129  0.0378  0.0019  258 GLN A CB  
744  C CG  . GLN A 258 ? 0.3091 0.4220 0.2569 0.0092  0.0393  -0.0030 258 GLN A CG  
745  C CD  . GLN A 258 ? 0.3582 0.4828 0.3049 0.0146  0.0390  -0.0107 258 GLN A CD  
746  O OE1 . GLN A 258 ? 0.3738 0.5008 0.3125 0.0202  0.0359  -0.0150 258 GLN A OE1 
747  N NE2 . GLN A 258 ? 0.3375 0.4700 0.2918 0.0135  0.0420  -0.0130 258 GLN A NE2 
748  N N   . LYS A 259 ? 0.2955 0.3662 0.2166 0.0127  0.0386  0.0214  259 LYS A N   
749  C CA  . LYS A 259 ? 0.3111 0.3744 0.2198 0.0200  0.0379  0.0279  259 LYS A CA  
750  C C   . LYS A 259 ? 0.3176 0.3661 0.2287 0.0199  0.0361  0.0299  259 LYS A C   
751  O O   . LYS A 259 ? 0.3040 0.3431 0.2227 0.0122  0.0379  0.0292  259 LYS A O   
752  C CB  . LYS A 259 ? 0.3542 0.4117 0.2482 0.0204  0.0451  0.0383  259 LYS A CB  
753  C CG  . LYS A 259 ? 0.4470 0.4872 0.3400 0.0111  0.0520  0.0450  259 LYS A CG  
754  C CD  . LYS A 259 ? 0.5322 0.5654 0.4096 0.0102  0.0601  0.0556  259 LYS A CD  
755  C CE  . LYS A 259 ? 0.6044 0.6310 0.4648 0.0219  0.0595  0.0631  259 LYS A CE  
756  N NZ  . LYS A 259 ? 0.6538 0.6733 0.4979 0.0208  0.0679  0.0739  259 LYS A NZ  
757  N N   . ARG A 260 ? 0.3262 0.3744 0.2305 0.0292  0.0324  0.0319  260 ARG A N   
758  C CA  . ARG A 260 ? 0.3326 0.3680 0.2378 0.0316  0.0309  0.0339  260 ARG A CA  
759  C C   . ARG A 260 ? 0.3664 0.3803 0.2583 0.0318  0.0378  0.0448  260 ARG A C   
760  O O   . ARG A 260 ? 0.3875 0.3992 0.2651 0.0374  0.0410  0.0524  260 ARG A O   
761  C CB  . ARG A 260 ? 0.3384 0.3853 0.2421 0.0421  0.0243  0.0318  260 ARG A CB  
762  C CG  . ARG A 260 ? 0.3534 0.3911 0.2613 0.0444  0.0223  0.0319  260 ARG A CG  
763  C CD  . ARG A 260 ? 0.3963 0.4497 0.3051 0.0541  0.0157  0.0292  260 ARG A CD  
764  N NE  . ARG A 260 ? 0.4658 0.5205 0.3591 0.0658  0.0164  0.0375  260 ARG A NE  
765  C CZ  . ARG A 260 ? 0.5402 0.6114 0.4314 0.0762  0.0109  0.0370  260 ARG A CZ  
766  N NH1 . ARG A 260 ? 0.5328 0.6206 0.4370 0.0750  0.0046  0.0282  260 ARG A NH1 
767  N NH2 . ARG A 260 ? 0.5561 0.6283 0.4320 0.0880  0.0119  0.0457  260 ARG A NH2 
768  N N   . LEU A 261 ? 0.3694 0.3663 0.2649 0.0247  0.0407  0.0455  261 LEU A N   
769  C CA  . LEU A 261 ? 0.3961 0.3681 0.2782 0.0232  0.0478  0.0548  261 LEU A CA  
770  C C   . LEU A 261 ? 0.4071 0.3659 0.2809 0.0343  0.0463  0.0588  261 LEU A C   
771  O O   . LEU A 261 ? 0.4316 0.3724 0.2886 0.0402  0.0512  0.0683  261 LEU A O   
772  C CB  . LEU A 261 ? 0.4122 0.3721 0.3012 0.0091  0.0517  0.0527  261 LEU A CB  
773  C CG  . LEU A 261 ? 0.4480 0.4212 0.3455 -0.0021 0.0541  0.0495  261 LEU A CG  
774  C CD1 . LEU A 261 ? 0.4656 0.4296 0.3706 -0.0155 0.0569  0.0470  261 LEU A CD1 
775  C CD2 . LEU A 261 ? 0.4653 0.4376 0.3505 -0.0029 0.0604  0.0572  261 LEU A CD2 
776  N N   . ARG A 262 ? 0.3891 0.3553 0.2742 0.0371  0.0403  0.0518  262 ARG A N   
777  C CA  . ARG A 262 ? 0.3971 0.3533 0.2763 0.0479  0.0390  0.0547  262 ARG A CA  
778  C C   . ARG A 262 ? 0.3842 0.3635 0.2745 0.0550  0.0309  0.0479  262 ARG A C   
779  O O   . ARG A 262 ? 0.3609 0.3564 0.2660 0.0480  0.0266  0.0391  262 ARG A O   
780  C CB  . ARG A 262 ? 0.4222 0.3565 0.3034 0.0408  0.0422  0.0535  262 ARG A CB  
781  C CG  . ARG A 262 ? 0.4748 0.3863 0.3471 0.0298  0.0504  0.0584  262 ARG A CG  
782  C CD  . ARG A 262 ? 0.5037 0.3878 0.3697 0.0275  0.0543  0.0595  262 ARG A CD  
783  N NE  . ARG A 262 ? 0.4910 0.3596 0.3420 0.0430  0.0556  0.0662  262 ARG A NE  
784  C CZ  . ARG A 262 ? 0.4803 0.3200 0.3203 0.0447  0.0602  0.0689  262 ARG A CZ  
785  N NH1 . ARG A 262 ? 0.4573 0.2809 0.2995 0.0304  0.0637  0.0650  262 ARG A NH1 
786  N NH2 . ARG A 262 ? 0.4982 0.3250 0.3240 0.0611  0.0615  0.0754  262 ARG A NH2 
787  N N   . ASN A 263 ? 0.3884 0.3678 0.2714 0.0686  0.0291  0.0519  263 ASN A N   
788  C CA  . ASN A 263 ? 0.3860 0.3876 0.2795 0.0750  0.0220  0.0458  263 ASN A CA  
789  C C   . ASN A 263 ? 0.4006 0.3871 0.2893 0.0835  0.0237  0.0493  263 ASN A C   
790  O O   . ASN A 263 ? 0.4207 0.4022 0.2963 0.0975  0.0249  0.0569  263 ASN A O   
791  C CB  . ASN A 263 ? 0.4095 0.4347 0.2989 0.0851  0.0172  0.0468  263 ASN A CB  
792  C CG  . ASN A 263 ? 0.4470 0.4992 0.3503 0.0872  0.0094  0.0383  263 ASN A CG  
793  O OD1 . ASN A 263 ? 0.4561 0.5115 0.3734 0.0783  0.0075  0.0305  263 ASN A OD1 
794  N ND2 . ASN A 263 ? 0.4563 0.5290 0.3555 0.0988  0.0049  0.0398  263 ASN A ND2 
795  N N   . MET A 264 ? 0.3868 0.3641 0.2845 0.0756  0.0245  0.0442  264 MET A N   
796  C CA  . MET A 264 ? 0.4040 0.3638 0.2966 0.0821  0.0272  0.0464  264 MET A CA  
797  C C   . MET A 264 ? 0.3992 0.3801 0.3008 0.0914  0.0218  0.0424  264 MET A C   
798  O O   . MET A 264 ? 0.3799 0.3783 0.2974 0.0841  0.0174  0.0341  264 MET A O   
799  C CB  . MET A 264 ? 0.4147 0.3535 0.3105 0.0689  0.0312  0.0431  264 MET A CB  
800  C CG  . MET A 264 ? 0.4370 0.3557 0.3235 0.0589  0.0373  0.0475  264 MET A CG  
801  S SD  . MET A 264 ? 0.4469 0.3470 0.3387 0.0415  0.0410  0.0423  264 MET A SD  
802  C CE  . MET A 264 ? 0.4448 0.3757 0.3590 0.0316  0.0342  0.0324  264 MET A CE  
803  N N   . THR A 265 ? 0.4146 0.3929 0.3051 0.1079  0.0226  0.0489  265 THR A N   
804  C CA  . THR A 265 ? 0.4233 0.4232 0.3213 0.1186  0.0182  0.0462  265 THR A CA  
805  C C   . THR A 265 ? 0.4509 0.4267 0.3415 0.1255  0.0232  0.0486  265 THR A C   
806  O O   . THR A 265 ? 0.5026 0.4474 0.3757 0.1306  0.0296  0.0560  265 THR A O   
807  C CB  . THR A 265 ? 0.4571 0.4790 0.3490 0.1342  0.0144  0.0511  265 THR A CB  
808  O OG1 . THR A 265 ? 0.4955 0.4925 0.3662 0.1461  0.0201  0.0623  265 THR A OG1 
809  C CG2 . THR A 265 ? 0.4588 0.5058 0.3577 0.1271  0.0091  0.0471  265 THR A CG2 
810  N N   . SER A 266 ? 0.4234 0.4114 0.3264 0.1243  0.0209  0.0421  266 SER A N   
811  C CA  . SER A 266 ? 0.4161 0.3864 0.3140 0.1314  0.0250  0.0425  266 SER A CA  
812  C C   . SER A 266 ? 0.3895 0.3886 0.3044 0.1322  0.0205  0.0352  266 SER A C   
813  O O   . SER A 266 ? 0.3840 0.3847 0.2961 0.1454  0.0219  0.0365  266 SER A O   
814  C CB  . SER A 266 ? 0.4223 0.3578 0.3142 0.1188  0.0309  0.0413  266 SER A CB  
815  O OG  . SER A 266 ? 0.4100 0.3541 0.3170 0.1007  0.0283  0.0334  266 SER A OG  
816  N N   . HIS A 267 ? 0.3690 0.3909 0.3010 0.1181  0.0154  0.0277  267 HIS A N   
817  C CA  . HIS A 267 ? 0.3551 0.4044 0.3037 0.1153  0.0114  0.0206  267 HIS A CA  
818  C C   . HIS A 267 ? 0.3607 0.4457 0.3153 0.1263  0.0063  0.0207  267 HIS A C   
819  O O   . HIS A 267 ? 0.3676 0.4618 0.3166 0.1325  0.0039  0.0246  267 HIS A O   
820  C CB  . HIS A 267 ? 0.3393 0.3952 0.3012 0.0960  0.0087  0.0133  267 HIS A CB  
821  C CG  . HIS A 267 ? 0.3329 0.3640 0.2942 0.0856  0.0127  0.0110  267 HIS A CG  
822  N ND1 . HIS A 267 ? 0.3410 0.3676 0.3040 0.0878  0.0149  0.0088  267 HIS A ND1 
823  C CD2 . HIS A 267 ? 0.3327 0.3451 0.2918 0.0734  0.0145  0.0104  267 HIS A CD2 
824  C CE1 . HIS A 267 ? 0.3447 0.3500 0.3063 0.0764  0.0177  0.0066  267 HIS A CE1 
825  N NE2 . HIS A 267 ? 0.3330 0.3298 0.2925 0.0676  0.0175  0.0076  267 HIS A NE2 
826  N N   . SER A 268 ? 0.3529 0.4599 0.3191 0.1282  0.0046  0.0163  268 SER A N   
827  C CA  . SER A 268 ? 0.3518 0.4979 0.3262 0.1373  -0.0005 0.0153  268 SER A CA  
828  C C   . SER A 268 ? 0.3334 0.5090 0.3254 0.1217  -0.0061 0.0066  268 SER A C   
829  O O   . SER A 268 ? 0.3427 0.5535 0.3434 0.1258  -0.0106 0.0043  268 SER A O   
830  C CB  . SER A 268 ? 0.3720 0.5261 0.3470 0.1513  0.0019  0.0165  268 SER A CB  
831  O OG  . SER A 268 ? 0.3981 0.5497 0.3831 0.1399  0.0038  0.0103  268 SER A OG  
832  N N   . ALA A 269 ? 0.2995 0.4613 0.2966 0.1041  -0.0056 0.0018  269 ALA A N   
833  C CA  . ALA A 269 ? 0.2660 0.4490 0.2777 0.0888  -0.0099 -0.0063 269 ALA A CA  
834  C C   . ALA A 269 ? 0.2405 0.4016 0.2511 0.0738  -0.0092 -0.0088 269 ALA A C   
835  O O   . ALA A 269 ? 0.2546 0.3876 0.2549 0.0750  -0.0055 -0.0044 269 ALA A O   
836  C CB  . ALA A 269 ? 0.2658 0.4604 0.2887 0.0847  -0.0087 -0.0105 269 ALA A CB  
837  N N   . ARG A 270 ? 0.2095 0.3830 0.2301 0.0599  -0.0125 -0.0158 270 ARG A N   
838  C CA  . ARG A 270 ? 0.2113 0.3663 0.2308 0.0478  -0.0119 -0.0181 270 ARG A CA  
839  C C   . ARG A 270 ? 0.2149 0.3412 0.2309 0.0439  -0.0071 -0.0161 270 ARG A C   
840  O O   . ARG A 270 ? 0.2116 0.3335 0.2302 0.0447  -0.0047 -0.0160 270 ARG A O   
841  C CB  . ARG A 270 ? 0.2285 0.3981 0.2582 0.0342  -0.0153 -0.0261 270 ARG A CB  
842  C CG  . ARG A 270 ? 0.2426 0.4146 0.2817 0.0262  -0.0140 -0.0298 270 ARG A CG  
843  C CD  . ARG A 270 ? 0.2422 0.4189 0.2879 0.0115  -0.0161 -0.0369 270 ARG A CD  
844  N NE  . ARG A 270 ? 0.2282 0.3999 0.2806 0.0026  -0.0138 -0.0393 270 ARG A NE  
845  C CZ  . ARG A 270 ? 0.2361 0.4128 0.2945 -0.0101 -0.0148 -0.0451 270 ARG A CZ  
846  N NH1 . ARG A 270 ? 0.2281 0.3982 0.2908 -0.0173 -0.0122 -0.0460 270 ARG A NH1 
847  N NH2 . ARG A 270 ? 0.2316 0.4180 0.2903 -0.0157 -0.0182 -0.0502 270 ARG A NH2 
848  N N   . VAL A 271 ? 0.2084 0.3164 0.2183 0.0399  -0.0058 -0.0145 271 VAL A N   
849  C CA  . VAL A 271 ? 0.2222 0.3051 0.2287 0.0351  -0.0017 -0.0129 271 VAL A CA  
850  C C   . VAL A 271 ? 0.2185 0.3001 0.2326 0.0221  -0.0028 -0.0183 271 VAL A C   
851  O O   . VAL A 271 ? 0.2286 0.3084 0.2417 0.0176  -0.0037 -0.0195 271 VAL A O   
852  C CB  . VAL A 271 ? 0.2522 0.3167 0.2466 0.0393  0.0012  -0.0070 271 VAL A CB  
853  C CG1 . VAL A 271 ? 0.2627 0.3042 0.2545 0.0321  0.0051  -0.0063 271 VAL A CG1 
854  C CG2 . VAL A 271 ? 0.2799 0.3422 0.2646 0.0536  0.0029  -0.0008 271 VAL A CG2 
855  N N   . GLY A 272 ? 0.1941 0.2774 0.2152 0.0170  -0.0024 -0.0213 272 GLY A N   
856  C CA  . GLY A 272 ? 0.2083 0.2899 0.2357 0.0059  -0.0032 -0.0257 272 GLY A CA  
857  C C   . GLY A 272 ? 0.2074 0.2700 0.2329 0.0009  -0.0006 -0.0247 272 GLY A C   
858  O O   . GLY A 272 ? 0.2061 0.2663 0.2353 -0.0066 -0.0012 -0.0276 272 GLY A O   
859  N N   . SER A 273 ? 0.2080 0.2568 0.2270 0.0049  0.0024  -0.0209 273 SER A N   
860  C CA  . SER A 273 ? 0.2043 0.2377 0.2215 -0.0007 0.0045  -0.0205 273 SER A CA  
861  C C   . SER A 273 ? 0.2065 0.2252 0.2146 0.0018  0.0073  -0.0164 273 SER A C   
862  O O   . SER A 273 ? 0.2143 0.2299 0.2159 0.0095  0.0087  -0.0132 273 SER A O   
863  C CB  . SER A 273 ? 0.2198 0.2503 0.2391 -0.0024 0.0058  -0.0217 273 SER A CB  
864  O OG  . SER A 273 ? 0.2361 0.2646 0.2507 0.0056  0.0077  -0.0198 273 SER A OG  
865  N N   . LEU A 274 ? 0.1932 0.2035 0.2007 -0.0048 0.0083  -0.0164 274 LEU A N   
866  C CA  . LEU A 274 ? 0.2113 0.2082 0.2107 -0.0054 0.0114  -0.0129 274 LEU A CA  
867  C C   . LEU A 274 ? 0.2190 0.2086 0.2196 -0.0137 0.0126  -0.0143 274 LEU A C   
868  O O   . LEU A 274 ? 0.2120 0.2092 0.2197 -0.0182 0.0105  -0.0170 274 LEU A O   
869  C CB  . LEU A 274 ? 0.2045 0.2066 0.2030 -0.0054 0.0110  -0.0114 274 LEU A CB  
870  C CG  . LEU A 274 ? 0.2246 0.2364 0.2210 0.0025  0.0093  -0.0100 274 LEU A CG  
871  C CD1 . LEU A 274 ? 0.2320 0.2516 0.2286 0.0012  0.0083  -0.0103 274 LEU A CD1 
872  C CD2 . LEU A 274 ? 0.2314 0.2326 0.2169 0.0103  0.0122  -0.0046 274 LEU A CD2 
873  N N   . SER A 275 ? 0.2255 0.2003 0.2183 -0.0158 0.0160  -0.0124 275 SER A N   
874  C CA  . SER A 275 ? 0.2174 0.1874 0.2109 -0.0249 0.0170  -0.0139 275 SER A CA  
875  C C   . SER A 275 ? 0.2425 0.1974 0.2264 -0.0285 0.0212  -0.0111 275 SER A C   
876  O O   . SER A 275 ? 0.2610 0.2010 0.2353 -0.0242 0.0241  -0.0091 275 SER A O   
877  C CB  . SER A 275 ? 0.2280 0.1952 0.2225 -0.0270 0.0164  -0.0172 275 SER A CB  
878  O OG  . SER A 275 ? 0.2340 0.2004 0.2297 -0.0359 0.0165  -0.0190 275 SER A OG  
879  N N   . TRP A 276 ? 0.2356 0.1937 0.2216 -0.0367 0.0220  -0.0111 276 TRP A N   
880  C CA  . TRP A 276 ? 0.2614 0.2055 0.2384 -0.0427 0.0266  -0.0085 276 TRP A CA  
881  C C   . TRP A 276 ? 0.2856 0.2210 0.2600 -0.0523 0.0279  -0.0118 276 TRP A C   
882  O O   . TRP A 276 ? 0.2933 0.2402 0.2757 -0.0562 0.0248  -0.0157 276 TRP A O   
883  C CB  . TRP A 276 ? 0.2498 0.2054 0.2308 -0.0474 0.0273  -0.0067 276 TRP A CB  
884  C CG  . TRP A 276 ? 0.2555 0.2177 0.2360 -0.0395 0.0269  -0.0033 276 TRP A CG  
885  C CD1 . TRP A 276 ? 0.2615 0.2398 0.2499 -0.0341 0.0231  -0.0050 276 TRP A CD1 
886  C CD2 . TRP A 276 ? 0.2725 0.2252 0.2429 -0.0373 0.0310  0.0021  276 TRP A CD2 
887  N NE1 . TRP A 276 ? 0.2659 0.2470 0.2502 -0.0288 0.0240  -0.0017 276 TRP A NE1 
888  C CE2 . TRP A 276 ? 0.2728 0.2388 0.2460 -0.0301 0.0288  0.0032  276 TRP A CE2 
889  C CE3 . TRP A 276 ? 0.2990 0.2313 0.2568 -0.0407 0.0365  0.0062  276 TRP A CE3 
890  C CZ2 . TRP A 276 ? 0.2904 0.2526 0.2546 -0.0259 0.0317  0.0087  276 TRP A CZ2 
891  C CZ3 . TRP A 276 ? 0.3079 0.2342 0.2563 -0.0363 0.0398  0.0123  276 TRP A CZ3 
892  C CH2 . TRP A 276 ? 0.3022 0.2444 0.2540 -0.0285 0.0372  0.0137  276 TRP A CH2 
893  N N   . ASN A 277 ? 0.2997 0.2144 0.2622 -0.0567 0.0328  -0.0103 277 ASN A N   
894  C CA  . ASN A 277 ? 0.3271 0.2310 0.2846 -0.0685 0.0351  -0.0137 277 ASN A CA  
895  C C   . ASN A 277 ? 0.3491 0.2409 0.2981 -0.0763 0.0405  -0.0099 277 ASN A C   
896  O O   . ASN A 277 ? 0.3635 0.2318 0.2988 -0.0729 0.0451  -0.0065 277 ASN A O   
897  C CB  . ASN A 277 ? 0.3664 0.2500 0.3137 -0.0650 0.0367  -0.0160 277 ASN A CB  
898  C CG  . ASN A 277 ? 0.4488 0.3211 0.3902 -0.0776 0.0386  -0.0210 277 ASN A CG  
899  O OD1 . ASN A 277 ? 0.4932 0.3787 0.4411 -0.0893 0.0373  -0.0236 277 ASN A OD1 
900  N ND2 . ASN A 277 ? 0.4764 0.3248 0.4048 -0.0754 0.0418  -0.0229 277 ASN A ND2 
901  N N   . SER A 278 ? 0.3449 0.2535 0.3017 -0.0854 0.0404  -0.0098 278 SER A N   
902  C CA  . SER A 278 ? 0.3670 0.2684 0.3173 -0.0934 0.0459  -0.0056 278 SER A CA  
903  C C   . SER A 278 ? 0.3694 0.2635 0.3130 -0.0813 0.0479  0.0013  278 SER A C   
904  O O   . SER A 278 ? 0.3568 0.2687 0.3091 -0.0716 0.0438  0.0019  278 SER A O   
905  C CB  . SER A 278 ? 0.4113 0.2887 0.3491 -0.1061 0.0510  -0.0075 278 SER A CB  
906  O OG  . SER A 278 ? 0.4741 0.3414 0.4038 -0.1147 0.0572  -0.0029 278 SER A OG  
907  N N   . TYR A 279 ? 0.3920 0.2599 0.3195 -0.0811 0.0539  0.0062  279 TYR A N   
908  C CA  . TYR A 279 ? 0.4105 0.2710 0.3297 -0.0689 0.0559  0.0133  279 TYR A CA  
909  C C   . TYR A 279 ? 0.4014 0.2521 0.3155 -0.0533 0.0538  0.0139  279 TYR A C   
910  O O   . TYR A 279 ? 0.4108 0.2582 0.3184 -0.0418 0.0546  0.0195  279 TYR A O   
911  C CB  . TYR A 279 ? 0.4477 0.2844 0.3507 -0.0754 0.0640  0.0197  279 TYR A CB  
912  C CG  . TYR A 279 ? 0.5063 0.3124 0.3958 -0.0843 0.0690  0.0177  279 TYR A CG  
913  C CD1 . TYR A 279 ? 0.5449 0.3260 0.4219 -0.0738 0.0702  0.0183  279 TYR A CD1 
914  C CD2 . TYR A 279 ? 0.5394 0.3423 0.4285 -0.1035 0.0725  0.0148  279 TYR A CD2 
915  C CE1 . TYR A 279 ? 0.5826 0.3333 0.4457 -0.0816 0.0750  0.0155  279 TYR A CE1 
916  C CE2 . TYR A 279 ? 0.5715 0.3456 0.4476 -0.1130 0.0769  0.0116  279 TYR A CE2 
917  C CZ  . TYR A 279 ? 0.6009 0.3469 0.4630 -0.1018 0.0784  0.0120  279 TYR A CZ  
918  O OH  . TYR A 279 ? 0.6384 0.3528 0.4855 -0.1107 0.0832  0.0084  279 TYR A OH  
919  N N   . ILE A 280 ? 0.3817 0.2292 0.2983 -0.0527 0.0513  0.0082  280 ILE A N   
920  C CA  . ILE A 280 ? 0.3740 0.2170 0.2877 -0.0379 0.0493  0.0084  280 ILE A CA  
921  C C   . ILE A 280 ? 0.3475 0.2207 0.2779 -0.0319 0.0424  0.0057  280 ILE A C   
922  O O   . ILE A 280 ? 0.3425 0.2320 0.2849 -0.0394 0.0389  0.0009  280 ILE A O   
923  C CB  . ILE A 280 ? 0.4001 0.2255 0.3077 -0.0400 0.0506  0.0033  280 ILE A CB  
924  C CG1 . ILE A 280 ? 0.4483 0.2388 0.3365 -0.0452 0.0581  0.0056  280 ILE A CG1 
925  C CG2 . ILE A 280 ? 0.3961 0.2260 0.3055 -0.0252 0.0476  0.0022  280 ILE A CG2 
926  C CD1 . ILE A 280 ? 0.4869 0.2576 0.3599 -0.0321 0.0624  0.0134  280 ILE A CD1 
927  N N   . LEU A 281 ? 0.3282 0.2086 0.2585 -0.0187 0.0404  0.0088  281 LEU A N   
928  C CA  . LEU A 281 ? 0.2957 0.2018 0.2400 -0.0138 0.0343  0.0059  281 LEU A CA  
929  C C   . LEU A 281 ? 0.3065 0.2116 0.2498 -0.0031 0.0328  0.0048  281 LEU A C   
930  O O   . LEU A 281 ? 0.3222 0.2158 0.2548 0.0070  0.0353  0.0091  281 LEU A O   
931  C CB  . LEU A 281 ? 0.2904 0.2091 0.2355 -0.0086 0.0332  0.0099  281 LEU A CB  
932  C CG  . LEU A 281 ? 0.2851 0.2272 0.2412 -0.0020 0.0274  0.0071  281 LEU A CG  
933  C CD1 . LEU A 281 ? 0.2673 0.2241 0.2370 -0.0104 0.0240  0.0012  281 LEU A CD1 
934  C CD2 . LEU A 281 ? 0.2916 0.2430 0.2449 0.0038  0.0268  0.0109  281 LEU A CD2 
935  N N   . SER A 282 ? 0.2749 0.1918 0.2285 -0.0050 0.0293  -0.0007 282 SER A N   
936  C CA  . SER A 282 ? 0.2743 0.1938 0.2284 0.0043  0.0281  -0.0021 282 SER A CA  
937  C C   . SER A 282 ? 0.2571 0.2013 0.2222 0.0094  0.0233  -0.0029 282 SER A C   
938  O O   . SER A 282 ? 0.2530 0.2111 0.2279 0.0029  0.0202  -0.0055 282 SER A O   
939  C CB  . SER A 282 ? 0.2890 0.2054 0.2461 -0.0017 0.0279  -0.0074 282 SER A CB  
940  O OG  . SER A 282 ? 0.3134 0.2065 0.2593 -0.0079 0.0324  -0.0075 282 SER A OG  
941  N N   . SER A 283 ? 0.2466 0.1966 0.2098 0.0211  0.0227  -0.0011 283 SER A N   
942  C CA  . SER A 283 ? 0.2517 0.2261 0.2246 0.0250  0.0181  -0.0025 283 SER A CA  
943  C C   . SER A 283 ? 0.2542 0.2389 0.2315 0.0316  0.0170  -0.0047 283 SER A C   
944  O O   . SER A 283 ? 0.2645 0.2387 0.2335 0.0403  0.0200  -0.0026 283 SER A O   
945  C CB  . SER A 283 ? 0.2667 0.2454 0.2337 0.0333  0.0178  0.0024  283 SER A CB  
946  O OG  . SER A 283 ? 0.3086 0.2733 0.2633 0.0445  0.0213  0.0072  283 SER A OG  
947  N N   . GLY A 284 ? 0.2396 0.2436 0.2291 0.0271  0.0134  -0.0090 284 GLY A N   
948  C CA  . GLY A 284 ? 0.2406 0.2585 0.2361 0.0315  0.0125  -0.0114 284 GLY A CA  
949  C C   . GLY A 284 ? 0.2381 0.2805 0.2403 0.0358  0.0087  -0.0119 284 GLY A C   
950  O O   . GLY A 284 ? 0.2443 0.2953 0.2507 0.0306  0.0058  -0.0132 284 GLY A O   
951  N N   . SER A 285 ? 0.2334 0.2884 0.2366 0.0454  0.0088  -0.0113 285 SER A N   
952  C CA  . SER A 285 ? 0.2319 0.3132 0.2410 0.0504  0.0051  -0.0118 285 SER A CA  
953  C C   . SER A 285 ? 0.2196 0.3244 0.2404 0.0481  0.0036  -0.0160 285 SER A C   
954  O O   . SER A 285 ? 0.2132 0.3140 0.2355 0.0472  0.0063  -0.0173 285 SER A O   
955  C CB  . SER A 285 ? 0.2696 0.3505 0.2690 0.0663  0.0063  -0.0062 285 SER A CB  
956  O OG  . SER A 285 ? 0.2999 0.4099 0.3048 0.0727  0.0023  -0.0066 285 SER A OG  
957  N N   . ARG A 286 ? 0.2153 0.3459 0.2438 0.0470  -0.0005 -0.0184 286 ARG A N   
958  C CA  . ARG A 286 ? 0.2244 0.3820 0.2643 0.0446  -0.0020 -0.0222 286 ARG A CA  
959  C C   . ARG A 286 ? 0.2423 0.4083 0.2805 0.0588  0.0007  -0.0195 286 ARG A C   
960  O O   . ARG A 286 ? 0.2436 0.4257 0.2899 0.0569  0.0017  -0.0221 286 ARG A O   
961  C CB  . ARG A 286 ? 0.2473 0.4309 0.2935 0.0418  -0.0070 -0.0252 286 ARG A CB  
962  C CG  . ARG A 286 ? 0.2993 0.5136 0.3582 0.0359  -0.0089 -0.0301 286 ARG A CG  
963  C CD  . ARG A 286 ? 0.3500 0.5885 0.4129 0.0331  -0.0142 -0.0335 286 ARG A CD  
964  N NE  . ARG A 286 ? 0.3966 0.6420 0.4677 0.0156  -0.0159 -0.0404 286 ARG A NE  
965  C CZ  . ARG A 286 ? 0.4243 0.6793 0.4964 0.0081  -0.0199 -0.0450 286 ARG A CZ  
966  N NH1 . ARG A 286 ? 0.3839 0.6451 0.4500 0.0167  -0.0231 -0.0434 286 ARG A NH1 
967  N NH2 . ARG A 286 ? 0.4456 0.7030 0.5236 -0.0079 -0.0206 -0.0514 286 ARG A NH2 
968  N N   . SER A 287 ? 0.2500 0.4029 0.2765 0.0732  0.0026  -0.0140 287 SER A N   
969  C CA  . SER A 287 ? 0.2536 0.4102 0.2758 0.0888  0.0057  -0.0111 287 SER A CA  
970  C C   . SER A 287 ? 0.2577 0.3956 0.2773 0.0869  0.0107  -0.0123 287 SER A C   
971  O O   . SER A 287 ? 0.2735 0.4188 0.2923 0.0979  0.0135  -0.0117 287 SER A O   
972  C CB  . SER A 287 ? 0.2794 0.4197 0.2867 0.1042  0.0072  -0.0044 287 SER A CB  
973  O OG  . SER A 287 ? 0.3225 0.4258 0.3186 0.0993  0.0106  -0.0024 287 SER A OG  
974  N N   . GLY A 288 ? 0.2481 0.3618 0.2650 0.0746  0.0119  -0.0139 288 GLY A N   
975  C CA  . GLY A 288 ? 0.2527 0.3478 0.2656 0.0718  0.0162  -0.0154 288 GLY A CA  
976  C C   . GLY A 288 ? 0.2700 0.3302 0.2673 0.0757  0.0198  -0.0125 288 GLY A C   
977  O O   . GLY A 288 ? 0.2975 0.3392 0.2899 0.0714  0.0230  -0.0144 288 GLY A O   
978  N N   . HIS A 289 ? 0.2579 0.3086 0.2464 0.0832  0.0196  -0.0079 289 HIS A N   
979  C CA  . HIS A 289 ? 0.2759 0.2923 0.2484 0.0861  0.0237  -0.0047 289 HIS A CA  
980  C C   . HIS A 289 ? 0.2728 0.2740 0.2445 0.0717  0.0227  -0.0052 289 HIS A C   
981  O O   . HIS A 289 ? 0.2713 0.2875 0.2522 0.0638  0.0186  -0.0062 289 HIS A O   
982  C CB  . HIS A 289 ? 0.3106 0.3223 0.2719 0.1025  0.0250  0.0016  289 HIS A CB  
983  C CG  . HIS A 289 ? 0.3594 0.3872 0.3206 0.1194  0.0262  0.0027  289 HIS A CG  
984  N ND1 . HIS A 289 ? 0.4079 0.4194 0.3603 0.1275  0.0314  0.0020  289 HIS A ND1 
985  C CD2 . HIS A 289 ? 0.3676 0.4277 0.3365 0.1293  0.0228  0.0042  289 HIS A CD2 
986  C CE1 . HIS A 289 ? 0.4133 0.4478 0.3685 0.1434  0.0314  0.0034  289 HIS A CE1 
987  N NE2 . HIS A 289 ? 0.3907 0.4560 0.3561 0.1449  0.0260  0.0049  289 HIS A NE2 
988  N N   . ILE A 290 ? 0.2730 0.2445 0.2331 0.0684  0.0267  -0.0047 290 ILE A N   
989  C CA  . ILE A 290 ? 0.2699 0.2259 0.2276 0.0558  0.0267  -0.0046 290 ILE A CA  
990  C C   . ILE A 290 ? 0.3021 0.2322 0.2433 0.0618  0.0309  0.0007  290 ILE A C   
991  O O   . ILE A 290 ? 0.3210 0.2311 0.2496 0.0702  0.0355  0.0019  290 ILE A O   
992  C CB  . ILE A 290 ? 0.2680 0.2137 0.2272 0.0436  0.0277  -0.0095 290 ILE A CB  
993  C CG1 . ILE A 290 ? 0.2460 0.2161 0.2206 0.0370  0.0238  -0.0138 290 ILE A CG1 
994  C CG2 . ILE A 290 ? 0.2901 0.2193 0.2451 0.0318  0.0285  -0.0091 290 ILE A CG2 
995  C CD1 . ILE A 290 ? 0.2671 0.2300 0.2413 0.0308  0.0255  -0.0181 290 ILE A CD1 
996  N N   . HIS A 291 ? 0.3034 0.2321 0.2432 0.0579  0.0300  0.0041  291 HIS A N   
997  C CA  . HIS A 291 ? 0.3273 0.2303 0.2506 0.0619  0.0345  0.0100  291 HIS A CA  
998  C C   . HIS A 291 ? 0.3401 0.2273 0.2612 0.0461  0.0363  0.0090  291 HIS A C   
999  O O   . HIS A 291 ? 0.3303 0.2336 0.2633 0.0359  0.0327  0.0062  291 HIS A O   
1000 C CB  . HIS A 291 ? 0.3356 0.2515 0.2574 0.0715  0.0325  0.0158  291 HIS A CB  
1001 C CG  . HIS A 291 ? 0.3693 0.2984 0.2895 0.0892  0.0316  0.0183  291 HIS A CG  
1002 N ND1 . HIS A 291 ? 0.3915 0.3343 0.3093 0.0999  0.0295  0.0236  291 HIS A ND1 
1003 C CD2 . HIS A 291 ? 0.3840 0.3161 0.3046 0.0983  0.0327  0.0163  291 HIS A CD2 
1004 C CE1 . HIS A 291 ? 0.3898 0.3450 0.3073 0.1151  0.0290  0.0246  291 HIS A CE1 
1005 N NE2 . HIS A 291 ? 0.3915 0.3407 0.3109 0.1149  0.0311  0.0203  291 HIS A NE2 
1006 N N   . HIS A 292 ? 0.3487 0.2046 0.2541 0.0440  0.0421  0.0111  292 HIS A N   
1007 C CA  . HIS A 292 ? 0.3598 0.2029 0.2627 0.0287  0.0442  0.0108  292 HIS A CA  
1008 C C   . HIS A 292 ? 0.3736 0.2072 0.2658 0.0332  0.0470  0.0188  292 HIS A C   
1009 O O   . HIS A 292 ? 0.3911 0.2069 0.2684 0.0457  0.0509  0.0242  292 HIS A O   
1010 C CB  . HIS A 292 ? 0.3855 0.1988 0.2763 0.0212  0.0494  0.0080  292 HIS A CB  
1011 C CG  . HIS A 292 ? 0.3760 0.1964 0.2751 0.0151  0.0472  0.0002  292 HIS A CG  
1012 N ND1 . HIS A 292 ? 0.3605 0.2097 0.2775 0.0098  0.0413  -0.0037 292 HIS A ND1 
1013 C CD2 . HIS A 292 ? 0.4008 0.2016 0.2907 0.0137  0.0504  -0.0041 292 HIS A CD2 
1014 C CE1 . HIS A 292 ? 0.3753 0.2227 0.2939 0.0058  0.0411  -0.0095 292 HIS A CE1 
1015 N NE2 . HIS A 292 ? 0.3929 0.2124 0.2956 0.0078  0.0463  -0.0104 292 HIS A NE2 
1016 N N   . HIS A 293 ? 0.3610 0.2057 0.2595 0.0236  0.0456  0.0197  293 HIS A N   
1017 C CA  . HIS A 293 ? 0.3735 0.2116 0.2625 0.0260  0.0484  0.0272  293 HIS A CA  
1018 C C   . HIS A 293 ? 0.4008 0.2228 0.2846 0.0101  0.0529  0.0277  293 HIS A C   
1019 O O   . HIS A 293 ? 0.4067 0.2433 0.3033 -0.0026 0.0504  0.0225  293 HIS A O   
1020 C CB  . HIS A 293 ? 0.3570 0.2260 0.2580 0.0287  0.0428  0.0276  293 HIS A CB  
1021 C CG  . HIS A 293 ? 0.3469 0.2387 0.2570 0.0403  0.0373  0.0254  293 HIS A CG  
1022 N ND1 . HIS A 293 ? 0.3732 0.2659 0.2749 0.0565  0.0373  0.0306  293 HIS A ND1 
1023 C CD2 . HIS A 293 ? 0.3364 0.2509 0.2626 0.0371  0.0319  0.0187  293 HIS A CD2 
1024 C CE1 . HIS A 293 ? 0.3723 0.2909 0.2866 0.0617  0.0318  0.0264  293 HIS A CE1 
1025 N NE2 . HIS A 293 ? 0.3451 0.2756 0.2738 0.0499  0.0287  0.0192  293 HIS A NE2 
1026 N N   . ASP A 294 ? 0.4118 0.2051 0.2771 0.0106  0.0598  0.0342  294 ASP A N   
1027 C CA  . ASP A 294 ? 0.4156 0.1964 0.2763 -0.0056 0.0646  0.0353  294 ASP A CA  
1028 C C   . ASP A 294 ? 0.4068 0.2031 0.2685 -0.0021 0.0640  0.0416  294 ASP A C   
1029 O O   . ASP A 294 ? 0.4188 0.2022 0.2661 0.0088  0.0673  0.0496  294 ASP A O   
1030 C CB  . ASP A 294 ? 0.4654 0.2047 0.3037 -0.0078 0.0731  0.0392  294 ASP A CB  
1031 C CG  . ASP A 294 ? 0.5242 0.2505 0.3572 -0.0269 0.0788  0.0403  294 ASP A CG  
1032 O OD1 . ASP A 294 ? 0.5011 0.2514 0.3458 -0.0349 0.0768  0.0406  294 ASP A OD1 
1033 O OD2 . ASP A 294 ? 0.5659 0.2583 0.3826 -0.0339 0.0855  0.0408  294 ASP A OD2 
1034 N N   . VAL A 295 ? 0.3808 0.2057 0.2590 -0.0095 0.0596  0.0378  295 VAL A N   
1035 C CA  . VAL A 295 ? 0.3780 0.2210 0.2583 -0.0058 0.0584  0.0421  295 VAL A CA  
1036 C C   . VAL A 295 ? 0.4112 0.2386 0.2780 -0.0121 0.0657  0.0497  295 VAL A C   
1037 O O   . VAL A 295 ? 0.4187 0.2580 0.2834 -0.0070 0.0656  0.0545  295 VAL A O   
1038 C CB  . VAL A 295 ? 0.3611 0.2362 0.2614 -0.0116 0.0524  0.0355  295 VAL A CB  
1039 C CG1 . VAL A 295 ? 0.3539 0.2428 0.2667 -0.0066 0.0458  0.0284  295 VAL A CG1 
1040 C CG2 . VAL A 295 ? 0.3657 0.2421 0.2716 -0.0289 0.0550  0.0325  295 VAL A CG2 
1041 N N   . ARG A 296 ? 0.4316 0.2328 0.2884 -0.0239 0.0722  0.0506  296 ARG A N   
1042 C CA  . ARG A 296 ? 0.4562 0.2406 0.2992 -0.0321 0.0801  0.0580  296 ARG A CA  
1043 C C   . ARG A 296 ? 0.4808 0.2357 0.3008 -0.0195 0.0857  0.0680  296 ARG A C   
1044 O O   . ARG A 296 ? 0.4954 0.2368 0.3021 -0.0238 0.0924  0.0759  296 ARG A O   
1045 C CB  . ARG A 296 ? 0.4918 0.2585 0.3323 -0.0518 0.0854  0.0546  296 ARG A CB  
1046 C CG  . ARG A 296 ? 0.5078 0.3001 0.3689 -0.0651 0.0807  0.0450  296 ARG A CG  
1047 C CD  . ARG A 296 ? 0.5447 0.3164 0.4006 -0.0826 0.0854  0.0409  296 ARG A CD  
1048 N NE  . ARG A 296 ? 0.5928 0.3343 0.4359 -0.0767 0.0867  0.0394  296 ARG A NE  
1049 C CZ  . ARG A 296 ? 0.6333 0.3453 0.4639 -0.0889 0.0924  0.0372  296 ARG A CZ  
1050 N NH1 . ARG A 296 ? 0.6405 0.3253 0.4588 -0.0813 0.0937  0.0354  296 ARG A NH1 
1051 N NH2 . ARG A 296 ? 0.6171 0.3278 0.4476 -0.1093 0.0970  0.0360  296 ARG A NH2 
1052 N N   . VAL A 297 ? 0.4822 0.2248 0.2958 -0.0046 0.0838  0.0681  297 VAL A N   
1053 C CA  . VAL A 297 ? 0.5283 0.2392 0.3182 0.0085  0.0897  0.0776  297 VAL A CA  
1054 C C   . VAL A 297 ? 0.5286 0.2542 0.3169 0.0316  0.0848  0.0821  297 VAL A C   
1055 O O   . VAL A 297 ? 0.4957 0.2518 0.3013 0.0378  0.0765  0.0758  297 VAL A O   
1056 C CB  . VAL A 297 ? 0.5696 0.2443 0.3471 0.0059  0.0945  0.0751  297 VAL A CB  
1057 C CG1 . VAL A 297 ? 0.5907 0.2522 0.3689 -0.0186 0.0993  0.0703  297 VAL A CG1 
1058 C CG2 . VAL A 297 ? 0.5671 0.2539 0.3559 0.0155  0.0879  0.0672  297 VAL A CG2 
1059 N N   . ALA A 298 ? 0.5491 0.2537 0.3161 0.0437  0.0900  0.0932  298 ALA A N   
1060 C CA  . ALA A 298 ? 0.5634 0.2803 0.3250 0.0665  0.0862  0.0993  298 ALA A CA  
1061 C C   . ALA A 298 ? 0.5728 0.2976 0.3410 0.0808  0.0808  0.0941  298 ALA A C   
1062 O O   . ALA A 298 ? 0.5666 0.3261 0.3490 0.0900  0.0728  0.0909  298 ALA A O   
1063 C CB  . ALA A 298 ? 0.5874 0.2718 0.3210 0.0767  0.0944  0.1129  298 ALA A CB  
1064 N N   . GLU A 299 ? 0.5828 0.2769 0.3417 0.0811  0.0853  0.0923  299 GLU A N   
1065 C CA  . GLU A 299 ? 0.5889 0.2888 0.3534 0.0937  0.0814  0.0871  299 GLU A CA  
1066 C C   . GLU A 299 ? 0.5674 0.2857 0.3539 0.0774  0.0767  0.0747  299 GLU A C   
1067 O O   . GLU A 299 ? 0.5844 0.2803 0.3677 0.0677  0.0803  0.0696  299 GLU A O   
1068 C CB  . GLU A 299 ? 0.6643 0.3189 0.4051 0.1024  0.0895  0.0913  299 GLU A CB  
1069 N N   . HIS A 300 ? 0.5258 0.2836 0.3333 0.0734  0.0690  0.0698  300 HIS A N   
1070 C CA  . HIS A 300 ? 0.5091 0.2868 0.3375 0.0585  0.0643  0.0591  300 HIS A CA  
1071 C C   . HIS A 300 ? 0.4998 0.2801 0.3354 0.0626  0.0617  0.0520  300 HIS A C   
1072 O O   . HIS A 300 ? 0.4901 0.2702 0.3347 0.0490  0.0610  0.0445  300 HIS A O   
1073 C CB  . HIS A 300 ? 0.4941 0.3109 0.3405 0.0562  0.0571  0.0563  300 HIS A CB  
1074 C CG  . HIS A 300 ? 0.4974 0.3391 0.3494 0.0730  0.0511  0.0566  300 HIS A CG  
1075 N ND1 . HIS A 300 ? 0.5041 0.3659 0.3712 0.0751  0.0455  0.0490  300 HIS A ND1 
1076 C CD2 . HIS A 300 ? 0.5104 0.3603 0.3541 0.0878  0.0500  0.0637  300 HIS A CD2 
1077 C CE1 . HIS A 300 ? 0.5074 0.3898 0.3759 0.0901  0.0414  0.0513  300 HIS A CE1 
1078 N NE2 . HIS A 300 ? 0.5103 0.3876 0.3651 0.0985  0.0435  0.0599  300 HIS A NE2 
1079 N N   . HIS A 301 ? 0.4993 0.2849 0.3315 0.0816  0.0600  0.0543  301 HIS A N   
1080 C CA  . HIS A 301 ? 0.4978 0.2907 0.3383 0.0862  0.0574  0.0474  301 HIS A CA  
1081 C C   . HIS A 301 ? 0.5284 0.2837 0.3538 0.0849  0.0642  0.0461  301 HIS A C   
1082 O O   . HIS A 301 ? 0.5547 0.2866 0.3622 0.0998  0.0690  0.0518  301 HIS A O   
1083 C CB  . HIS A 301 ? 0.4891 0.3063 0.3333 0.1061  0.0531  0.0497  301 HIS A CB  
1084 C CG  . HIS A 301 ? 0.4956 0.3277 0.3510 0.1105  0.0501  0.0427  301 HIS A CG  
1085 N ND1 . HIS A 301 ? 0.5107 0.3595 0.3666 0.1295  0.0481  0.0447  301 HIS A ND1 
1086 C CD2 . HIS A 301 ? 0.4990 0.3338 0.3654 0.0982  0.0490  0.0342  301 HIS A CD2 
1087 C CE1 . HIS A 301 ? 0.5066 0.3666 0.3735 0.1277  0.0464  0.0374  301 HIS A CE1 
1088 N NE2 . HIS A 301 ? 0.5036 0.3550 0.3766 0.1093  0.0468  0.0310  301 HIS A NE2 
1089 N N   . VAL A 302 ? 0.5240 0.2731 0.3557 0.0675  0.0647  0.0384  302 VAL A N   
1090 C CA  . VAL A 302 ? 0.5437 0.2557 0.3599 0.0631  0.0713  0.0360  302 VAL A CA  
1091 C C   . VAL A 302 ? 0.5418 0.2569 0.3628 0.0669  0.0699  0.0283  302 VAL A C   
1092 O O   . VAL A 302 ? 0.5576 0.2411 0.3639 0.0656  0.0755  0.0257  302 VAL A O   
1093 C CB  . VAL A 302 ? 0.5655 0.2627 0.3802 0.0403  0.0742  0.0333  302 VAL A CB  
1094 C CG1 . VAL A 302 ? 0.5855 0.2734 0.3909 0.0374  0.0778  0.0420  302 VAL A CG1 
1095 C CG2 . VAL A 302 ? 0.5516 0.2806 0.3894 0.0257  0.0677  0.0253  302 VAL A CG2 
1096 N N   . ALA A 303 ? 0.5142 0.2657 0.3547 0.0705  0.0630  0.0242  303 ALA A N   
1097 C CA  . ALA A 303 ? 0.5099 0.2671 0.3554 0.0741  0.0620  0.0172  303 ALA A CA  
1098 C C   . ALA A 303 ? 0.4732 0.2715 0.3380 0.0819  0.0551  0.0157  303 ALA A C   
1099 O O   . ALA A 303 ? 0.4488 0.2724 0.3271 0.0766  0.0501  0.0165  303 ALA A O   
1100 C CB  . ALA A 303 ? 0.5107 0.2629 0.3615 0.0547  0.0617  0.0090  303 ALA A CB  
1101 N N   . THR A 304 ? 0.4656 0.2700 0.3312 0.0935  0.0554  0.0129  304 THR A N   
1102 C CA  . THR A 304 ? 0.4439 0.2871 0.3276 0.0993  0.0497  0.0104  304 THR A CA  
1103 C C   . THR A 304 ? 0.4305 0.2759 0.3195 0.0939  0.0501  0.0026  304 THR A C   
1104 O O   . THR A 304 ? 0.4561 0.2785 0.3317 0.1005  0.0552  0.0009  304 THR A O   
1105 C CB  . THR A 304 ? 0.4694 0.3242 0.3493 0.1215  0.0499  0.0158  304 THR A CB  
1106 O OG1 . THR A 304 ? 0.4789 0.3335 0.3534 0.1265  0.0492  0.0233  304 THR A OG1 
1107 C CG2 . THR A 304 ? 0.4560 0.3526 0.3551 0.1257  0.0445  0.0124  304 THR A CG2 
1108 N N   . LEU A 305 ? 0.3903 0.2617 0.2973 0.0822  0.0450  -0.0021 305 LEU A N   
1109 C CA  . LEU A 305 ? 0.3814 0.2592 0.2949 0.0757  0.0446  -0.0089 305 LEU A CA  
1110 C C   . LEU A 305 ? 0.3701 0.2831 0.2984 0.0833  0.0411  -0.0096 305 LEU A C   
1111 O O   . LEU A 305 ? 0.3584 0.2960 0.3003 0.0786  0.0361  -0.0087 305 LEU A O   
1112 C CB  . LEU A 305 ? 0.3666 0.2471 0.2887 0.0561  0.0416  -0.0127 305 LEU A CB  
1113 C CG  . LEU A 305 ? 0.3990 0.2493 0.3090 0.0447  0.0449  -0.0147 305 LEU A CG  
1114 C CD1 . LEU A 305 ? 0.4217 0.2475 0.3173 0.0479  0.0487  -0.0089 305 LEU A CD1 
1115 C CD2 . LEU A 305 ? 0.3789 0.2405 0.3002 0.0276  0.0410  -0.0178 305 LEU A CD2 
1116 N N   . SER A 306 ? 0.3636 0.2794 0.2888 0.0948  0.0439  -0.0112 306 SER A N   
1117 C CA  . SER A 306 ? 0.3507 0.3017 0.2896 0.1024  0.0413  -0.0117 306 SER A CA  
1118 C C   . SER A 306 ? 0.3413 0.3021 0.2864 0.0976  0.0422  -0.0174 306 SER A C   
1119 O O   . SER A 306 ? 0.3611 0.3150 0.2980 0.1084  0.0466  -0.0190 306 SER A O   
1120 C CB  . SER A 306 ? 0.3861 0.3397 0.3172 0.1239  0.0439  -0.0073 306 SER A CB  
1121 O OG  . SER A 306 ? 0.4326 0.3799 0.3582 0.1283  0.0427  -0.0012 306 SER A OG  
1122 N N   . GLY A 307 ? 0.3107 0.2861 0.2687 0.0823  0.0384  -0.0203 307 GLY A N   
1123 C CA  . GLY A 307 ? 0.3057 0.2913 0.2695 0.0764  0.0391  -0.0250 307 GLY A CA  
1124 C C   . GLY A 307 ? 0.2871 0.3063 0.2690 0.0696  0.0351  -0.0256 307 GLY A C   
1125 O O   . GLY A 307 ? 0.2968 0.3242 0.2840 0.0621  0.0355  -0.0287 307 GLY A O   
1126 N N   . HIS A 308 ? 0.2662 0.3042 0.2566 0.0718  0.0316  -0.0228 308 HIS A N   
1127 C CA  . HIS A 308 ? 0.2500 0.3182 0.2564 0.0642  0.0281  -0.0240 308 HIS A CA  
1128 C C   . HIS A 308 ? 0.2639 0.3599 0.2770 0.0757  0.0271  -0.0223 308 HIS A C   
1129 O O   . HIS A 308 ? 0.2892 0.3818 0.2962 0.0873  0.0268  -0.0189 308 HIS A O   
1130 C CB  . HIS A 308 ? 0.2432 0.3101 0.2552 0.0513  0.0236  -0.0237 308 HIS A CB  
1131 C CG  . HIS A 308 ? 0.2285 0.2761 0.2373 0.0392  0.0238  -0.0255 308 HIS A CG  
1132 N ND1 . HIS A 308 ? 0.2333 0.2891 0.2491 0.0290  0.0232  -0.0279 308 HIS A ND1 
1133 C CD2 . HIS A 308 ? 0.2386 0.2613 0.2381 0.0359  0.0242  -0.0249 308 HIS A CD2 
1134 C CE1 . HIS A 308 ? 0.2278 0.2646 0.2384 0.0211  0.0230  -0.0286 308 HIS A CE1 
1135 N NE2 . HIS A 308 ? 0.2374 0.2551 0.2389 0.0243  0.0235  -0.0272 308 HIS A NE2 
1136 N N   . SER A 309 ? 0.2615 0.3863 0.2872 0.0718  0.0265  -0.0244 309 SER A N   
1137 C CA  . SER A 309 ? 0.2554 0.4131 0.2898 0.0810  0.0250  -0.0235 309 SER A CA  
1138 C C   . SER A 309 ? 0.2497 0.4288 0.2962 0.0700  0.0196  -0.0246 309 SER A C   
1139 O O   . SER A 309 ? 0.2523 0.4615 0.3069 0.0754  0.0176  -0.0245 309 SER A O   
1140 C CB  . SER A 309 ? 0.2610 0.4415 0.3017 0.0853  0.0286  -0.0255 309 SER A CB  
1141 O OG  . SER A 309 ? 0.2788 0.4653 0.3273 0.0692  0.0289  -0.0284 309 SER A OG  
1142 N N   . GLN A 310 ? 0.2373 0.4025 0.2850 0.0547  0.0175  -0.0260 310 GLN A N   
1143 C CA  . GLN A 310 ? 0.2175 0.3965 0.2741 0.0433  0.0128  -0.0278 310 GLN A CA  
1144 C C   . GLN A 310 ? 0.2170 0.3690 0.2663 0.0378  0.0110  -0.0267 310 GLN A C   
1145 O O   . GLN A 310 ? 0.2219 0.3480 0.2607 0.0416  0.0133  -0.0247 310 GLN A O   
1146 C CB  . GLN A 310 ? 0.2218 0.4147 0.2887 0.0288  0.0133  -0.0313 310 GLN A CB  
1147 C CG  . GLN A 310 ? 0.2698 0.4923 0.3450 0.0328  0.0158  -0.0323 310 GLN A CG  
1148 C CD  . GLN A 310 ? 0.3365 0.5935 0.4209 0.0368  0.0126  -0.0333 310 GLN A CD  
1149 O OE1 . GLN A 310 ? 0.3607 0.6228 0.4474 0.0321  0.0081  -0.0343 310 GLN A OE1 
1150 N NE2 . GLN A 310 ? 0.3564 0.6405 0.4466 0.0455  0.0149  -0.0333 310 GLN A NE2 
1151 N N   . GLU A 311 ? 0.2028 0.3615 0.2573 0.0284  0.0071  -0.0285 311 GLU A N   
1152 C CA  . GLU A 311 ? 0.1958 0.3346 0.2445 0.0243  0.0052  -0.0276 311 GLU A CA  
1153 C C   . GLU A 311 ? 0.2052 0.3164 0.2475 0.0191  0.0076  -0.0270 311 GLU A C   
1154 O O   . GLU A 311 ? 0.2117 0.3206 0.2571 0.0112  0.0089  -0.0287 311 GLU A O   
1155 C CB  . GLU A 311 ? 0.2032 0.3541 0.2592 0.0133  0.0014  -0.0311 311 GLU A CB  
1156 C CG  . GLU A 311 ? 0.2340 0.3668 0.2841 0.0102  -0.0003 -0.0304 311 GLU A CG  
1157 C CD  . GLU A 311 ? 0.2823 0.4280 0.3360 0.0051  -0.0043 -0.0335 311 GLU A CD  
1158 O OE1 . GLU A 311 ? 0.2673 0.4051 0.3151 0.0079  -0.0057 -0.0320 311 GLU A OE1 
1159 O OE2 . GLU A 311 ? 0.2774 0.4410 0.3392 -0.0026 -0.0057 -0.0376 311 GLU A OE2 
1160 N N   . VAL A 312 ? 0.2048 0.2960 0.2378 0.0232  0.0081  -0.0242 312 VAL A N   
1161 C CA  . VAL A 312 ? 0.2123 0.2802 0.2397 0.0172  0.0098  -0.0240 312 VAL A CA  
1162 C C   . VAL A 312 ? 0.2205 0.2872 0.2517 0.0074  0.0070  -0.0253 312 VAL A C   
1163 O O   . VAL A 312 ? 0.2334 0.2978 0.2619 0.0089  0.0054  -0.0240 312 VAL A O   
1164 C CB  . VAL A 312 ? 0.2227 0.2696 0.2382 0.0243  0.0122  -0.0207 312 VAL A CB  
1165 C CG1 . VAL A 312 ? 0.2324 0.2591 0.2435 0.0160  0.0135  -0.0214 312 VAL A CG1 
1166 C CG2 . VAL A 312 ? 0.2272 0.2730 0.2371 0.0361  0.0154  -0.0194 312 VAL A CG2 
1167 N N   . CYS A 313 ? 0.2041 0.2724 0.2405 -0.0018 0.0066  -0.0277 313 CYS A N   
1168 C CA  . CYS A 313 ? 0.2062 0.2728 0.2456 -0.0100 0.0044  -0.0293 313 CYS A CA  
1169 C C   . CYS A 313 ? 0.2169 0.2664 0.2524 -0.0144 0.0051  -0.0285 313 CYS A C   
1170 O O   . CYS A 313 ? 0.2285 0.2753 0.2650 -0.0188 0.0036  -0.0293 313 CYS A O   
1171 C CB  . CYS A 313 ? 0.2133 0.2929 0.2602 -0.0170 0.0036  -0.0322 313 CYS A CB  
1172 S SG  . CYS A 313 ? 0.2396 0.3213 0.2884 -0.0195 0.0067  -0.0322 313 CYS A SG  
1173 N N   . GLY A 314 ? 0.2018 0.2411 0.2328 -0.0133 0.0073  -0.0274 314 GLY A N   
1174 C CA  . GLY A 314 ? 0.1978 0.2242 0.2254 -0.0176 0.0076  -0.0270 314 GLY A CA  
1175 C C   . GLY A 314 ? 0.1933 0.2072 0.2130 -0.0141 0.0096  -0.0256 314 GLY A C   
1176 O O   . GLY A 314 ? 0.1981 0.2099 0.2140 -0.0089 0.0117  -0.0254 314 GLY A O   
1177 N N   . LEU A 315 ? 0.1973 0.2028 0.2140 -0.0167 0.0095  -0.0246 315 LEU A N   
1178 C CA  . LEU A 315 ? 0.2121 0.2038 0.2201 -0.0149 0.0120  -0.0232 315 LEU A CA  
1179 C C   . LEU A 315 ? 0.2150 0.2011 0.2221 -0.0220 0.0118  -0.0233 315 LEU A C   
1180 O O   . LEU A 315 ? 0.2188 0.2105 0.2297 -0.0239 0.0103  -0.0226 315 LEU A O   
1181 C CB  . LEU A 315 ? 0.2201 0.2114 0.2246 -0.0078 0.0127  -0.0205 315 LEU A CB  
1182 C CG  . LEU A 315 ? 0.2590 0.2329 0.2522 -0.0041 0.0163  -0.0182 315 LEU A CG  
1183 C CD1 . LEU A 315 ? 0.2693 0.2361 0.2573 0.0008  0.0188  -0.0195 315 LEU A CD1 
1184 C CD2 . LEU A 315 ? 0.2750 0.2497 0.2644 0.0034  0.0167  -0.0145 315 LEU A CD2 
1185 N N   . ARG A 316 ? 0.2062 0.1831 0.2085 -0.0262 0.0132  -0.0247 316 ARG A N   
1186 C CA  . ARG A 316 ? 0.2199 0.1960 0.2227 -0.0338 0.0126  -0.0253 316 ARG A CA  
1187 C C   . ARG A 316 ? 0.2361 0.1989 0.2305 -0.0384 0.0150  -0.0268 316 ARG A C   
1188 O O   . ARG A 316 ? 0.2280 0.1865 0.2188 -0.0393 0.0156  -0.0295 316 ARG A O   
1189 C CB  . ARG A 316 ? 0.2546 0.2416 0.2642 -0.0368 0.0098  -0.0266 316 ARG A CB  
1190 C CG  . ARG A 316 ? 0.3109 0.3048 0.3246 -0.0415 0.0081  -0.0262 316 ARG A CG  
1191 C CD  . ARG A 316 ? 0.3567 0.3580 0.3758 -0.0382 0.0069  -0.0247 316 ARG A CD  
1192 N NE  . ARG A 316 ? 0.4035 0.4096 0.4264 -0.0354 0.0054  -0.0252 316 ARG A NE  
1193 C CZ  . ARG A 316 ? 0.4537 0.4626 0.4787 -0.0319 0.0050  -0.0252 316 ARG A CZ  
1194 N NH1 . ARG A 316 ? 0.4487 0.4572 0.4722 -0.0294 0.0057  -0.0243 316 ARG A NH1 
1195 N NH2 . ARG A 316 ? 0.4613 0.4739 0.4893 -0.0315 0.0042  -0.0260 316 ARG A NH2 
1196 N N   . TRP A 317 ? 0.2376 0.1939 0.2284 -0.0427 0.0167  -0.0255 317 TRP A N   
1197 C CA  . TRP A 317 ? 0.2527 0.1960 0.2353 -0.0501 0.0192  -0.0276 317 TRP A CA  
1198 C C   . TRP A 317 ? 0.2722 0.2272 0.2602 -0.0581 0.0164  -0.0306 317 TRP A C   
1199 O O   . TRP A 317 ? 0.2694 0.2403 0.2664 -0.0588 0.0136  -0.0294 317 TRP A O   
1200 C CB  . TRP A 317 ? 0.2581 0.1931 0.2361 -0.0539 0.0221  -0.0249 317 TRP A CB  
1201 C CG  . TRP A 317 ? 0.2796 0.1959 0.2468 -0.0474 0.0261  -0.0222 317 TRP A CG  
1202 C CD1 . TRP A 317 ? 0.2932 0.2103 0.2600 -0.0389 0.0266  -0.0178 317 TRP A CD1 
1203 C CD2 . TRP A 317 ? 0.3075 0.2011 0.2616 -0.0480 0.0301  -0.0237 317 TRP A CD2 
1204 N NE1 . TRP A 317 ? 0.3140 0.2110 0.2683 -0.0332 0.0307  -0.0156 317 TRP A NE1 
1205 C CE2 . TRP A 317 ? 0.3261 0.2065 0.2718 -0.0387 0.0333  -0.0192 317 TRP A CE2 
1206 C CE3 . TRP A 317 ? 0.3278 0.2099 0.2750 -0.0557 0.0315  -0.0287 317 TRP A CE3 
1207 C CZ2 . TRP A 317 ? 0.3520 0.2063 0.2824 -0.0356 0.0382  -0.0190 317 TRP A CZ2 
1208 C CZ3 . TRP A 317 ? 0.3615 0.2173 0.2935 -0.0538 0.0364  -0.0295 317 TRP A CZ3 
1209 C CH2 . TRP A 317 ? 0.3733 0.2143 0.2967 -0.0434 0.0399  -0.0244 317 TRP A CH2 
1210 N N   . ALA A 318 ? 0.2892 0.2366 0.2708 -0.0639 0.0172  -0.0345 318 ALA A N   
1211 C CA  . ALA A 318 ? 0.3028 0.2627 0.2882 -0.0717 0.0143  -0.0374 318 ALA A CA  
1212 C C   . ALA A 318 ? 0.3236 0.2899 0.3119 -0.0803 0.0146  -0.0368 318 ALA A C   
1213 O O   . ALA A 318 ? 0.3121 0.2657 0.2947 -0.0832 0.0183  -0.0354 318 ALA A O   
1214 C CB  . ALA A 318 ? 0.3132 0.2625 0.2893 -0.0765 0.0153  -0.0425 318 ALA A CB  
1215 N N   . PRO A 319 ? 0.3474 0.3340 0.3443 -0.0839 0.0111  -0.0373 319 PRO A N   
1216 C CA  . PRO A 319 ? 0.3573 0.3545 0.3582 -0.0921 0.0115  -0.0368 319 PRO A CA  
1217 C C   . PRO A 319 ? 0.3685 0.3539 0.3609 -0.1046 0.0148  -0.0402 319 PRO A C   
1218 O O   . PRO A 319 ? 0.3779 0.3644 0.3708 -0.1114 0.0174  -0.0387 319 PRO A O   
1219 C CB  . PRO A 319 ? 0.3675 0.3889 0.3775 -0.0921 0.0069  -0.0376 319 PRO A CB  
1220 C CG  . PRO A 319 ? 0.3751 0.3968 0.3870 -0.0814 0.0046  -0.0360 319 PRO A CG  
1221 C CD  . PRO A 319 ? 0.3533 0.3549 0.3560 -0.0798 0.0069  -0.0376 319 PRO A CD  
1222 N N   . ASP A 320 ? 0.3628 0.3362 0.3466 -0.1085 0.0150  -0.0449 320 ASP A N   
1223 C CA  . ASP A 320 ? 0.3790 0.3368 0.3524 -0.1213 0.0186  -0.0490 320 ASP A CA  
1224 C C   . ASP A 320 ? 0.3955 0.3217 0.3558 -0.1185 0.0245  -0.0474 320 ASP A C   
1225 O O   . ASP A 320 ? 0.4044 0.3116 0.3535 -0.1286 0.0286  -0.0504 320 ASP A O   
1226 C CB  . ASP A 320 ? 0.3949 0.3552 0.3638 -0.1286 0.0163  -0.0559 320 ASP A CB  
1227 C CG  . ASP A 320 ? 0.4425 0.3904 0.4044 -0.1198 0.0159  -0.0579 320 ASP A CG  
1228 O OD1 . ASP A 320 ? 0.4331 0.3684 0.3929 -0.1083 0.0181  -0.0541 320 ASP A OD1 
1229 O OD2 . ASP A 320 ? 0.4723 0.4251 0.4307 -0.1242 0.0135  -0.0633 320 ASP A OD2 
1230 N N   . GLY A 321 ? 0.3901 0.3107 0.3511 -0.1047 0.0251  -0.0428 321 GLY A N   
1231 C CA  . GLY A 321 ? 0.4128 0.3069 0.3621 -0.0984 0.0301  -0.0401 321 GLY A CA  
1232 C C   . GLY A 321 ? 0.4274 0.2989 0.3633 -0.0966 0.0325  -0.0445 321 GLY A C   
1233 O O   . GLY A 321 ? 0.4523 0.2984 0.3757 -0.0923 0.0375  -0.0428 321 GLY A O   
1234 N N   . ARG A 322 ? 0.4107 0.2900 0.3475 -0.0993 0.0295  -0.0501 322 ARG A N   
1235 C CA  . ARG A 322 ? 0.4154 0.2735 0.3385 -0.0976 0.0321  -0.0551 322 ARG A CA  
1236 C C   . ARG A 322 ? 0.4004 0.2566 0.3234 -0.0813 0.0323  -0.0528 322 ARG A C   
1237 O O   . ARG A 322 ? 0.4209 0.2570 0.3314 -0.0764 0.0359  -0.0556 322 ARG A O   
1238 C CB  . ARG A 322 ? 0.4479 0.3156 0.3704 -0.1075 0.0290  -0.0625 322 ARG A CB  
1239 C CG  . ARG A 322 ? 0.5181 0.3848 0.4374 -0.1254 0.0296  -0.0668 322 ARG A CG  
1240 C CD  . ARG A 322 ? 0.5836 0.4671 0.5045 -0.1345 0.0251  -0.0739 322 ARG A CD  
1241 N NE  . ARG A 322 ? 0.6568 0.5257 0.5657 -0.1310 0.0261  -0.0797 322 ARG A NE  
1242 C CZ  . ARG A 322 ? 0.6772 0.5606 0.5902 -0.1224 0.0225  -0.0801 322 ARG A CZ  
1243 N NH1 . ARG A 322 ? 0.6393 0.5499 0.5676 -0.1168 0.0178  -0.0750 322 ARG A NH1 
1244 N NH2 . ARG A 322 ? 0.6889 0.5585 0.5898 -0.1194 0.0242  -0.0856 322 ARG A NH2 
1245 N N   . HIS A 323 ? 0.3673 0.2452 0.3038 -0.0735 0.0286  -0.0485 323 HIS A N   
1246 C CA  . HIS A 323 ? 0.3440 0.2247 0.2824 -0.0597 0.0286  -0.0465 323 HIS A CA  
1247 C C   . HIS A 323 ? 0.3137 0.2085 0.2633 -0.0523 0.0268  -0.0402 323 HIS A C   
1248 O O   . HIS A 323 ? 0.2985 0.2067 0.2568 -0.0574 0.0242  -0.0383 323 HIS A O   
1249 C CB  . HIS A 323 ? 0.3493 0.2460 0.2929 -0.0595 0.0252  -0.0496 323 HIS A CB  
1250 C CG  . HIS A 323 ? 0.3949 0.2820 0.3280 -0.0660 0.0261  -0.0565 323 HIS A CG  
1251 N ND1 . HIS A 323 ? 0.4232 0.3191 0.3576 -0.0783 0.0232  -0.0603 323 HIS A ND1 
1252 C CD2 . HIS A 323 ? 0.4252 0.2967 0.3464 -0.0614 0.0294  -0.0605 323 HIS A CD2 
1253 C CE1 . HIS A 323 ? 0.4298 0.3145 0.3525 -0.0818 0.0246  -0.0668 323 HIS A CE1 
1254 N NE2 . HIS A 323 ? 0.4485 0.3168 0.3624 -0.0718 0.0287  -0.0673 323 HIS A NE2 
1255 N N   . LEU A 324 ? 0.2980 0.1920 0.2474 -0.0402 0.0279  -0.0377 324 LEU A N   
1256 C CA  . LEU A 324 ? 0.2827 0.1922 0.2425 -0.0334 0.0257  -0.0330 324 LEU A CA  
1257 C C   . LEU A 324 ? 0.2661 0.1895 0.2322 -0.0270 0.0240  -0.0339 324 LEU A C   
1258 O O   . LEU A 324 ? 0.2797 0.1955 0.2390 -0.0208 0.0266  -0.0355 324 LEU A O   
1259 C CB  . LEU A 324 ? 0.2952 0.1928 0.2484 -0.0248 0.0289  -0.0288 324 LEU A CB  
1260 C CG  . LEU A 324 ? 0.2916 0.2053 0.2535 -0.0159 0.0267  -0.0249 324 LEU A CG  
1261 C CD1 . LEU A 324 ? 0.2816 0.2108 0.2541 -0.0217 0.0232  -0.0234 324 LEU A CD1 
1262 C CD2 . LEU A 324 ? 0.3138 0.2154 0.2668 -0.0060 0.0299  -0.0207 324 LEU A CD2 
1263 N N   . ALA A 325 ? 0.2365 0.1789 0.2143 -0.0282 0.0203  -0.0327 325 ALA A N   
1264 C CA  . ALA A 325 ? 0.2457 0.2007 0.2292 -0.0237 0.0193  -0.0330 325 ALA A CA  
1265 C C   . ALA A 325 ? 0.2354 0.2011 0.2256 -0.0170 0.0185  -0.0299 325 ALA A C   
1266 O O   . ALA A 325 ? 0.2377 0.2074 0.2323 -0.0183 0.0167  -0.0278 325 ALA A O   
1267 C CB  . ALA A 325 ? 0.2502 0.2170 0.2402 -0.0301 0.0162  -0.0339 325 ALA A CB  
1268 N N   . SER A 326 ? 0.2166 0.1890 0.2081 -0.0101 0.0196  -0.0301 326 SER A N   
1269 C CA  . SER A 326 ? 0.2134 0.2002 0.2123 -0.0047 0.0183  -0.0280 326 SER A CA  
1270 C C   . SER A 326 ? 0.2098 0.2123 0.2160 -0.0051 0.0178  -0.0291 326 SER A C   
1271 O O   . SER A 326 ? 0.2048 0.2058 0.2077 -0.0044 0.0199  -0.0309 326 SER A O   
1272 C CB  . SER A 326 ? 0.2450 0.2274 0.2381 0.0059  0.0206  -0.0262 326 SER A CB  
1273 O OG  . SER A 326 ? 0.2842 0.2614 0.2709 0.0126  0.0240  -0.0276 326 SER A OG  
1274 N N   . GLY A 327 ? 0.2008 0.2171 0.2158 -0.0074 0.0153  -0.0284 327 GLY A N   
1275 C CA  . GLY A 327 ? 0.1984 0.2303 0.2208 -0.0092 0.0152  -0.0291 327 GLY A CA  
1276 C C   . GLY A 327 ? 0.1936 0.2413 0.2219 -0.0048 0.0144  -0.0288 327 GLY A C   
1277 O O   . GLY A 327 ? 0.1940 0.2424 0.2231 -0.0033 0.0123  -0.0279 327 GLY A O   
1278 N N   . GLY A 328 ? 0.1905 0.2532 0.2233 -0.0028 0.0158  -0.0296 328 GLY A N   
1279 C CA  . GLY A 328 ? 0.1969 0.2787 0.2360 0.0016  0.0148  -0.0296 328 GLY A CA  
1280 C C   . GLY A 328 ? 0.1932 0.2946 0.2418 -0.0052 0.0145  -0.0312 328 GLY A C   
1281 O O   . GLY A 328 ? 0.1957 0.2954 0.2451 -0.0120 0.0162  -0.0317 328 GLY A O   
1282 N N   . ASN A 329 ? 0.1853 0.3062 0.2403 -0.0032 0.0127  -0.0320 329 ASN A N   
1283 C CA  . ASN A 329 ? 0.1889 0.3320 0.2535 -0.0104 0.0127  -0.0342 329 ASN A CA  
1284 C C   . ASN A 329 ? 0.2075 0.3664 0.2748 -0.0053 0.0165  -0.0341 329 ASN A C   
1285 O O   . ASN A 329 ? 0.2140 0.3951 0.2898 -0.0107 0.0172  -0.0357 329 ASN A O   
1286 C CB  . ASN A 329 ? 0.2011 0.3622 0.2715 -0.0105 0.0091  -0.0359 329 ASN A CB  
1287 C CG  . ASN A 329 ? 0.2363 0.4179 0.3162 -0.0216 0.0089  -0.0390 329 ASN A CG  
1288 O OD1 . ASN A 329 ? 0.2364 0.4095 0.3168 -0.0329 0.0104  -0.0397 329 ASN A OD1 
1289 N ND2 . ASN A 329 ? 0.2412 0.4505 0.3282 -0.0187 0.0073  -0.0407 329 ASN A ND2 
1290 N N   . ASP A 330 ? 0.2080 0.3560 0.2676 0.0051  0.0191  -0.0326 330 ASP A N   
1291 C CA  . ASP A 330 ? 0.2036 0.3619 0.2633 0.0113  0.0233  -0.0327 330 ASP A CA  
1292 C C   . ASP A 330 ? 0.2160 0.3596 0.2709 0.0043  0.0263  -0.0328 330 ASP A C   
1293 O O   . ASP A 330 ? 0.2247 0.3705 0.2762 0.0100  0.0302  -0.0331 330 ASP A O   
1294 C CB  . ASP A 330 ? 0.2165 0.3686 0.2682 0.0277  0.0249  -0.0314 330 ASP A CB  
1295 C CG  . ASP A 330 ? 0.2549 0.3749 0.2941 0.0303  0.0248  -0.0303 330 ASP A CG  
1296 O OD1 . ASP A 330 ? 0.2602 0.3655 0.2982 0.0200  0.0229  -0.0305 330 ASP A OD1 
1297 O OD2 . ASP A 330 ? 0.2791 0.3886 0.3093 0.0427  0.0271  -0.0293 330 ASP A OD2 
1298 N N   . ASN A 331 ? 0.2126 0.3421 0.2666 -0.0071 0.0244  -0.0325 331 ASN A N   
1299 C CA  . ASN A 331 ? 0.2207 0.3384 0.2701 -0.0137 0.0265  -0.0320 331 ASN A CA  
1300 C C   . ASN A 331 ? 0.2333 0.3320 0.2716 -0.0072 0.0279  -0.0321 331 ASN A C   
1301 O O   . ASN A 331 ? 0.2568 0.3516 0.2906 -0.0092 0.0306  -0.0323 331 ASN A O   
1302 C CB  . ASN A 331 ? 0.2375 0.3741 0.2920 -0.0178 0.0304  -0.0321 331 ASN A CB  
1303 C CG  . ASN A 331 ? 0.2766 0.4359 0.3425 -0.0240 0.0296  -0.0329 331 ASN A CG  
1304 O OD1 . ASN A 331 ? 0.2412 0.3963 0.3098 -0.0322 0.0266  -0.0332 331 ASN A OD1 
1305 N ND2 . ASN A 331 ? 0.3185 0.5029 0.3908 -0.0197 0.0321  -0.0338 331 ASN A ND2 
1306 N N   . LEU A 332 ? 0.2062 0.2935 0.2393 0.0007  0.0266  -0.0323 332 LEU A N   
1307 C CA  . LEU A 332 ? 0.2046 0.2720 0.2260 0.0054  0.0284  -0.0332 332 LEU A CA  
1308 C C   . LEU A 332 ? 0.1928 0.2411 0.2097 0.0005  0.0254  -0.0328 332 LEU A C   
1309 O O   . LEU A 332 ? 0.1987 0.2475 0.2195 -0.0009 0.0225  -0.0316 332 LEU A O   
1310 C CB  . LEU A 332 ? 0.2107 0.2757 0.2267 0.0187  0.0305  -0.0335 332 LEU A CB  
1311 C CG  . LEU A 332 ? 0.2522 0.3363 0.2712 0.0280  0.0340  -0.0340 332 LEU A CG  
1312 C CD1 . LEU A 332 ? 0.2822 0.3572 0.2926 0.0428  0.0360  -0.0337 332 LEU A CD1 
1313 C CD2 . LEU A 332 ? 0.2736 0.3584 0.2888 0.0266  0.0378  -0.0359 332 LEU A CD2 
1314 N N   . VAL A 333 ? 0.1815 0.2143 0.1897 -0.0013 0.0263  -0.0341 333 VAL A N   
1315 C CA  . VAL A 333 ? 0.1888 0.2045 0.1917 -0.0052 0.0241  -0.0343 333 VAL A CA  
1316 C C   . VAL A 333 ? 0.2099 0.2091 0.2010 0.0010  0.0270  -0.0364 333 VAL A C   
1317 O O   . VAL A 333 ? 0.2217 0.2186 0.2067 0.0033  0.0299  -0.0389 333 VAL A O   
1318 C CB  . VAL A 333 ? 0.2073 0.2196 0.2091 -0.0140 0.0225  -0.0346 333 VAL A CB  
1319 C CG1 . VAL A 333 ? 0.2129 0.2107 0.2096 -0.0178 0.0205  -0.0353 333 VAL A CG1 
1320 C CG2 . VAL A 333 ? 0.2332 0.2574 0.2443 -0.0196 0.0204  -0.0322 333 VAL A CG2 
1321 N N   . ASN A 334 ? 0.2115 0.1983 0.1982 0.0038  0.0268  -0.0356 334 ASN A N   
1322 C CA  . ASN A 334 ? 0.2283 0.1942 0.2017 0.0079  0.0300  -0.0376 334 ASN A CA  
1323 C C   . ASN A 334 ? 0.2376 0.1886 0.2063 -0.0016 0.0284  -0.0386 334 ASN A C   
1324 O O   . ASN A 334 ? 0.2407 0.1965 0.2161 -0.0067 0.0253  -0.0362 334 ASN A O   
1325 C CB  . ASN A 334 ? 0.2451 0.2054 0.2143 0.0192  0.0321  -0.0354 334 ASN A CB  
1326 C CG  . ASN A 334 ? 0.2713 0.2458 0.2429 0.0304  0.0345  -0.0351 334 ASN A CG  
1327 O OD1 . ASN A 334 ? 0.3104 0.2813 0.2755 0.0350  0.0380  -0.0380 334 ASN A OD1 
1328 N ND2 . ASN A 334 ? 0.2756 0.2680 0.2564 0.0353  0.0327  -0.0321 334 ASN A ND2 
1329 N N   . VAL A 335 ? 0.2562 0.1901 0.2133 -0.0042 0.0306  -0.0424 335 VAL A N   
1330 C CA  . VAL A 335 ? 0.2763 0.1972 0.2285 -0.0140 0.0295  -0.0439 335 VAL A CA  
1331 C C   . VAL A 335 ? 0.3011 0.1974 0.2393 -0.0094 0.0339  -0.0449 335 VAL A C   
1332 O O   . VAL A 335 ? 0.3073 0.1919 0.2350 -0.0043 0.0376  -0.0483 335 VAL A O   
1333 C CB  . VAL A 335 ? 0.2986 0.2207 0.2481 -0.0231 0.0280  -0.0482 335 VAL A CB  
1334 C CG1 . VAL A 335 ? 0.3033 0.2146 0.2483 -0.0337 0.0269  -0.0502 335 VAL A CG1 
1335 C CG2 . VAL A 335 ? 0.3010 0.2450 0.2624 -0.0259 0.0243  -0.0462 335 VAL A CG2 
1336 N N   . TRP A 336 ? 0.3112 0.1988 0.2483 -0.0106 0.0341  -0.0416 336 TRP A N   
1337 C CA  . TRP A 336 ? 0.3318 0.1939 0.2546 -0.0059 0.0388  -0.0411 336 TRP A CA  
1338 C C   . TRP A 336 ? 0.3694 0.2121 0.2828 -0.0187 0.0401  -0.0443 336 TRP A C   
1339 O O   . TRP A 336 ? 0.3575 0.2108 0.2787 -0.0301 0.0366  -0.0446 336 TRP A O   
1340 C CB  . TRP A 336 ? 0.3249 0.1902 0.2515 0.0011  0.0385  -0.0344 336 TRP A CB  
1341 C CG  . TRP A 336 ? 0.3107 0.1982 0.2476 0.0121  0.0367  -0.0315 336 TRP A CG  
1342 C CD1 . TRP A 336 ? 0.2932 0.2062 0.2455 0.0093  0.0321  -0.0302 336 TRP A CD1 
1343 C CD2 . TRP A 336 ? 0.3170 0.2037 0.2492 0.0272  0.0396  -0.0300 336 TRP A CD2 
1344 N NE1 . TRP A 336 ? 0.2831 0.2118 0.2410 0.0200  0.0319  -0.0284 336 TRP A NE1 
1345 C CE2 . TRP A 336 ? 0.3016 0.2168 0.2482 0.0317  0.0363  -0.0280 336 TRP A CE2 
1346 C CE3 . TRP A 336 ? 0.3446 0.2090 0.2613 0.0378  0.0449  -0.0301 336 TRP A CE3 
1347 C CZ2 . TRP A 336 ? 0.3119 0.2379 0.2592 0.0459  0.0377  -0.0262 336 TRP A CZ2 
1348 C CZ3 . TRP A 336 ? 0.3654 0.2392 0.2821 0.0539  0.0465  -0.0278 336 TRP A CZ3 
1349 C CH2 . TRP A 336 ? 0.3428 0.2493 0.2756 0.0576  0.0427  -0.0261 336 TRP A CH2 
1350 N N   . PRO A 337 ? 0.4177 0.2315 0.3140 -0.0168 0.0454  -0.0463 337 PRO A N   
1351 C CA  . PRO A 337 ? 0.4527 0.2465 0.3392 -0.0309 0.0472  -0.0494 337 PRO A CA  
1352 C C   . PRO A 337 ? 0.4828 0.2734 0.3713 -0.0346 0.0476  -0.0434 337 PRO A C   
1353 O O   . PRO A 337 ? 0.4818 0.2808 0.3759 -0.0244 0.0470  -0.0371 337 PRO A O   
1354 C CB  . PRO A 337 ? 0.4763 0.2367 0.3419 -0.0257 0.0537  -0.0529 337 PRO A CB  
1355 C CG  . PRO A 337 ? 0.4787 0.2389 0.3431 -0.0061 0.0559  -0.0476 337 PRO A CG  
1356 C CD  . PRO A 337 ? 0.4261 0.2233 0.3104 -0.0017 0.0503  -0.0457 337 PRO A CD  
1357 N N   . SER A 338 ? 0.5077 0.2883 0.3918 -0.0497 0.0485  -0.0456 338 SER A N   
1358 C CA  . SER A 338 ? 0.5437 0.3216 0.4291 -0.0547 0.0496  -0.0400 338 SER A CA  
1359 C C   . SER A 338 ? 0.5973 0.3421 0.4647 -0.0478 0.0565  -0.0359 338 SER A C   
1360 O O   . SER A 338 ? 0.6034 0.3467 0.4710 -0.0459 0.0578  -0.0292 338 SER A O   
1361 C CB  . SER A 338 ? 0.5600 0.3421 0.4480 -0.0738 0.0485  -0.0437 338 SER A CB  
1362 O OG  . SER A 338 ? 0.6041 0.3598 0.4759 -0.0831 0.0526  -0.0501 338 SER A OG  
1363 N N   . ALA A 339 ? 0.6293 0.3468 0.4799 -0.0439 0.0611  -0.0397 339 ALA A N   
1364 C CA  . ALA A 339 ? 0.6781 0.3601 0.5088 -0.0357 0.0683  -0.0359 339 ALA A CA  
1365 C C   . ALA A 339 ? 0.7143 0.3836 0.5348 -0.0193 0.0710  -0.0384 339 ALA A C   
1366 O O   . ALA A 339 ? 0.7123 0.3920 0.5367 -0.0207 0.0686  -0.0453 339 ALA A O   
1367 C CB  . ALA A 339 ? 0.6983 0.3496 0.5133 -0.0528 0.0735  -0.0395 339 ALA A CB  
1368 N N   . PRO A 340 ? 0.7469 0.3954 0.5543 -0.0027 0.0759  -0.0326 340 PRO A N   
1369 C CA  . PRO A 340 ? 0.7725 0.4094 0.5696 0.0141  0.0790  -0.0351 340 PRO A CA  
1370 C C   . PRO A 340 ? 0.8174 0.4146 0.5918 0.0083  0.0854  -0.0427 340 PRO A C   
1371 O O   . PRO A 340 ? 0.8326 0.4245 0.6004 0.0182  0.0872  -0.0478 340 PRO A O   
1372 C CB  . PRO A 340 ? 0.7815 0.4117 0.5724 0.0343  0.0818  -0.0256 340 PRO A CB  
1373 C CG  . PRO A 340 ? 0.7901 0.4060 0.5757 0.0253  0.0838  -0.0193 340 PRO A CG  
1374 C CD  . PRO A 340 ? 0.7570 0.3897 0.5561 0.0021  0.0795  -0.0235 340 PRO A CD  
1375 N N   . GLY A 341 ? 0.8366 0.4066 0.5989 -0.0079 0.0891  -0.0438 341 GLY A N   
1376 C CA  . GLY A 341 ? 0.8705 0.3994 0.6094 -0.0161 0.0956  -0.0516 341 GLY A CA  
1377 C C   . GLY A 341 ? 0.9034 0.3955 0.6194 0.0045  0.1034  -0.0486 341 GLY A C   
1378 O O   . GLY A 341 ? 0.9084 0.3948 0.6210 0.0186  0.1056  -0.0385 341 GLY A O   
1379 N N   . GLU A 342 ? 0.9207 0.3887 0.6202 0.0079  0.1076  -0.0573 342 GLU A N   
1380 C CA  . GLU A 342 ? 0.9469 0.3799 0.6237 0.0302  0.1154  -0.0549 342 GLU A CA  
1381 C C   . GLU A 342 ? 0.9295 0.3917 0.6172 0.0552  0.1128  -0.0524 342 GLU A C   
1382 O O   . GLU A 342 ? 0.9398 0.3811 0.6121 0.0773  0.1185  -0.0488 342 GLU A O   
1383 C CB  . GLU A 342 ? 1.0129 0.3987 0.6623 0.0234  0.1228  -0.0652 342 GLU A CB  
1384 C CG  . GLU A 342 ? 1.1137 0.4606 0.7461 0.0030  0.1281  -0.0654 342 GLU A CG  
1385 C CD  . GLU A 342 ? 1.2037 0.5645 0.8460 -0.0275 0.1236  -0.0742 342 GLU A CD  
1386 O OE1 . GLU A 342 ? 1.2316 0.5663 0.8629 -0.0465 0.1275  -0.0744 342 GLU A OE1 
1387 O OE2 . GLU A 342 ? 1.2180 0.6163 0.8786 -0.0323 0.1163  -0.0806 342 GLU A OE2 
1388 N N   . GLY A 343 ? 0.8980 0.4082 0.6118 0.0515  0.1046  -0.0541 343 GLY A N   
1389 C CA  . GLY A 343 ? 0.8797 0.4234 0.6072 0.0715  0.1016  -0.0516 343 GLY A CA  
1390 C C   . GLY A 343 ? 0.8579 0.4327 0.6037 0.0790  0.0968  -0.0408 343 GLY A C   
1391 O O   . GLY A 343 ? 0.8721 0.4367 0.6159 0.0726  0.0971  -0.0345 343 GLY A O   
1392 N N   . GLY A 344 ? 0.8162 0.4292 0.5792 0.0919  0.0927  -0.0390 344 GLY A N   
1393 C CA  . GLY A 344 ? 0.7789 0.4247 0.5600 0.0983  0.0875  -0.0302 344 GLY A CA  
1394 C C   . GLY A 344 ? 0.7272 0.4101 0.5328 0.0812  0.0794  -0.0316 344 GLY A C   
1395 O O   . GLY A 344 ? 0.7286 0.4138 0.5378 0.0653  0.0776  -0.0389 344 GLY A O   
1396 N N   . TRP A 345 ? 0.6771 0.3890 0.4988 0.0847  0.0745  -0.0248 345 TRP A N   
1397 C CA  . TRP A 345 ? 0.6323 0.3785 0.4765 0.0706  0.0672  -0.0258 345 TRP A CA  
1398 C C   . TRP A 345 ? 0.5990 0.3748 0.4564 0.0745  0.0644  -0.0300 345 TRP A C   
1399 O O   . TRP A 345 ? 0.5943 0.3956 0.4618 0.0873  0.0626  -0.0266 345 TRP A O   
1400 C CB  . TRP A 345 ? 0.6108 0.3764 0.4658 0.0738  0.0635  -0.0179 345 TRP A CB  
1401 C CG  . TRP A 345 ? 0.6104 0.3551 0.4576 0.0638  0.0649  -0.0141 345 TRP A CG  
1402 C CD1 . TRP A 345 ? 0.6279 0.3510 0.4609 0.0728  0.0689  -0.0070 345 TRP A CD1 
1403 C CD2 . TRP A 345 ? 0.6007 0.3461 0.4539 0.0431  0.0625  -0.0168 345 TRP A CD2 
1404 N NE1 . TRP A 345 ? 0.6342 0.3438 0.4639 0.0578  0.0696  -0.0051 345 TRP A NE1 
1405 C CE2 . TRP A 345 ? 0.6183 0.3431 0.4612 0.0395  0.0655  -0.0112 345 TRP A CE2 
1406 C CE3 . TRP A 345 ? 0.5926 0.3547 0.4583 0.0278  0.0583  -0.0229 345 TRP A CE3 
1407 C CZ2 . TRP A 345 ? 0.6202 0.3433 0.4665 0.0208  0.0646  -0.0121 345 TRP A CZ2 
1408 C CZ3 . TRP A 345 ? 0.5984 0.3588 0.4672 0.0105  0.0570  -0.0237 345 TRP A CZ3 
1409 C CH2 . TRP A 345 ? 0.6075 0.3491 0.4670 0.0068  0.0602  -0.0186 345 TRP A CH2 
1410 N N   . VAL A 346 ? 0.5701 0.3419 0.4260 0.0642  0.0647  -0.0375 346 VAL A N   
1411 C CA  . VAL A 346 ? 0.5407 0.3382 0.4071 0.0667  0.0629  -0.0414 346 VAL A CA  
1412 C C   . VAL A 346 ? 0.4933 0.3069 0.3720 0.0479  0.0577  -0.0452 346 VAL A C   
1413 O O   . VAL A 346 ? 0.4919 0.2885 0.3644 0.0341  0.0576  -0.0482 346 VAL A O   
1414 C CB  . VAL A 346 ? 0.5806 0.3579 0.4303 0.0763  0.0690  -0.0470 346 VAL A CB  
1415 C CG1 . VAL A 346 ? 0.5995 0.3654 0.4382 0.0984  0.0740  -0.0427 346 VAL A CG1 
1416 C CG2 . VAL A 346 ? 0.6137 0.3563 0.4462 0.0636  0.0720  -0.0534 346 VAL A CG2 
1417 N N   . PRO A 347 ? 0.4511 0.2980 0.3472 0.0470  0.0536  -0.0446 347 PRO A N   
1418 C CA  . PRO A 347 ? 0.4344 0.2952 0.3408 0.0310  0.0489  -0.0471 347 PRO A CA  
1419 C C   . PRO A 347 ? 0.4403 0.2883 0.3365 0.0235  0.0506  -0.0544 347 PRO A C   
1420 O O   . PRO A 347 ? 0.4508 0.2922 0.3378 0.0320  0.0546  -0.0580 347 PRO A O   
1421 C CB  . PRO A 347 ? 0.4277 0.3224 0.3511 0.0344  0.0459  -0.0450 347 PRO A CB  
1422 C CG  . PRO A 347 ? 0.4326 0.3349 0.3582 0.0493  0.0473  -0.0404 347 PRO A CG  
1423 C CD  . PRO A 347 ? 0.4284 0.3019 0.3352 0.0599  0.0531  -0.0415 347 PRO A CD  
1424 N N   . LEU A 348 ? 0.4263 0.2725 0.3241 0.0079  0.0474  -0.0568 348 LEU A N   
1425 C CA  . LEU A 348 ? 0.4296 0.2703 0.3201 -0.0015 0.0472  -0.0638 348 LEU A CA  
1426 C C   . LEU A 348 ? 0.4021 0.2696 0.3029 -0.0007 0.0448  -0.0642 348 LEU A C   
1427 O O   . LEU A 348 ? 0.4008 0.2663 0.2940 -0.0022 0.0461  -0.0696 348 LEU A O   
1428 C CB  . LEU A 348 ? 0.4437 0.2830 0.3368 -0.0178 0.0435  -0.0648 348 LEU A CB  
1429 C CG  . LEU A 348 ? 0.4907 0.3023 0.3717 -0.0234 0.0464  -0.0658 348 LEU A CG  
1430 C CD1 . LEU A 348 ? 0.4980 0.3176 0.3866 -0.0386 0.0422  -0.0652 348 LEU A CD1 
1431 C CD2 . LEU A 348 ? 0.5255 0.3091 0.3862 -0.0251 0.0512  -0.0737 348 LEU A CD2 
1432 N N   . GLN A 349 ? 0.3638 0.2555 0.2812 0.0002  0.0413  -0.0586 349 GLN A N   
1433 C CA  . GLN A 349 ? 0.3486 0.2641 0.2755 0.0004  0.0396  -0.0578 349 GLN A CA  
1434 C C   . GLN A 349 ? 0.3263 0.2610 0.2664 0.0078  0.0391  -0.0522 349 GLN A C   
1435 O O   . GLN A 349 ? 0.3128 0.2475 0.2584 0.0084  0.0373  -0.0484 349 GLN A O   
1436 C CB  . GLN A 349 ? 0.3608 0.2874 0.2947 -0.0122 0.0346  -0.0575 349 GLN A CB  
1437 C CG  . GLN A 349 ? 0.3935 0.3083 0.3166 -0.0215 0.0339  -0.0634 349 GLN A CG  
1438 C CD  . GLN A 349 ? 0.4191 0.3340 0.3327 -0.0200 0.0361  -0.0684 349 GLN A CD  
1439 O OE1 . GLN A 349 ? 0.4022 0.3265 0.3173 -0.0116 0.0388  -0.0674 349 GLN A OE1 
1440 N NE2 . GLN A 349 ? 0.4309 0.3368 0.3345 -0.0285 0.0351  -0.0742 349 GLN A NE2 
1441 N N   . THR A 350 ? 0.3145 0.2667 0.2594 0.0129  0.0406  -0.0519 350 THR A N   
1442 C CA  . THR A 350 ? 0.2947 0.2691 0.2534 0.0172  0.0397  -0.0473 350 THR A CA  
1443 C C   . THR A 350 ? 0.2895 0.2821 0.2552 0.0113  0.0389  -0.0469 350 THR A C   
1444 O O   . THR A 350 ? 0.3095 0.3054 0.2698 0.0142  0.0423  -0.0494 350 THR A O   
1445 C CB  . THR A 350 ? 0.3109 0.2897 0.2682 0.0314  0.0436  -0.0468 350 THR A CB  
1446 O OG1 . THR A 350 ? 0.3269 0.2859 0.2759 0.0375  0.0446  -0.0461 350 THR A OG1 
1447 C CG2 . THR A 350 ? 0.2996 0.3058 0.2721 0.0338  0.0423  -0.0429 350 THR A CG2 
1448 N N   . PHE A 351 ? 0.2616 0.2643 0.2375 0.0032  0.0350  -0.0436 351 PHE A N   
1449 C CA  . PHE A 351 ? 0.2454 0.2619 0.2268 -0.0034 0.0343  -0.0421 351 PHE A CA  
1450 C C   . PHE A 351 ? 0.2383 0.2750 0.2314 -0.0016 0.0352  -0.0391 351 PHE A C   
1451 O O   . PHE A 351 ? 0.2365 0.2779 0.2377 -0.0026 0.0326  -0.0369 351 PHE A O   
1452 C CB  . PHE A 351 ? 0.2426 0.2549 0.2263 -0.0131 0.0298  -0.0404 351 PHE A CB  
1453 C CG  . PHE A 351 ? 0.2654 0.2619 0.2393 -0.0167 0.0283  -0.0435 351 PHE A CG  
1454 C CD1 . PHE A 351 ? 0.2734 0.2632 0.2362 -0.0160 0.0305  -0.0476 351 PHE A CD1 
1455 C CD2 . PHE A 351 ? 0.2768 0.2663 0.2526 -0.0214 0.0247  -0.0427 351 PHE A CD2 
1456 C CE1 . PHE A 351 ? 0.2925 0.2696 0.2465 -0.0212 0.0288  -0.0513 351 PHE A CE1 
1457 C CE2 . PHE A 351 ? 0.2900 0.2683 0.2579 -0.0264 0.0234  -0.0459 351 PHE A CE2 
1458 C CZ  . PHE A 351 ? 0.2932 0.2650 0.2502 -0.0267 0.0253  -0.0504 351 PHE A CZ  
1459 N N   . THR A 352 ? 0.2412 0.2909 0.2348 0.0006  0.0389  -0.0394 352 THR A N   
1460 C CA  . THR A 352 ? 0.2398 0.3118 0.2447 0.0008  0.0403  -0.0372 352 THR A CA  
1461 C C   . THR A 352 ? 0.2326 0.3139 0.2427 -0.0098 0.0402  -0.0343 352 THR A C   
1462 O O   . THR A 352 ? 0.2356 0.3353 0.2543 -0.0120 0.0420  -0.0328 352 THR A O   
1463 C CB  . THR A 352 ? 0.2705 0.3541 0.2735 0.0110  0.0454  -0.0391 352 THR A CB  
1464 O OG1 . THR A 352 ? 0.2937 0.3746 0.2882 0.0097  0.0487  -0.0407 352 THR A OG1 
1465 C CG2 . THR A 352 ? 0.3004 0.3719 0.2962 0.0231  0.0463  -0.0414 352 THR A CG2 
1466 N N   . GLN A 353 ? 0.2168 0.2858 0.2211 -0.0162 0.0383  -0.0334 353 GLN A N   
1467 C CA  . GLN A 353 ? 0.2140 0.2884 0.2195 -0.0245 0.0392  -0.0300 353 GLN A CA  
1468 C C   . GLN A 353 ? 0.2216 0.3000 0.2363 -0.0318 0.0370  -0.0269 353 GLN A C   
1469 O O   . GLN A 353 ? 0.2432 0.3281 0.2596 -0.0383 0.0394  -0.0239 353 GLN A O   
1470 C CB  . GLN A 353 ? 0.2216 0.2831 0.2166 -0.0272 0.0377  -0.0297 353 GLN A CB  
1471 C CG  . GLN A 353 ? 0.2295 0.2878 0.2138 -0.0216 0.0404  -0.0336 353 GLN A CG  
1472 C CD  . GLN A 353 ? 0.2643 0.3077 0.2425 -0.0171 0.0383  -0.0381 353 GLN A CD  
1473 O OE1 . GLN A 353 ? 0.2522 0.2911 0.2352 -0.0152 0.0362  -0.0385 353 GLN A OE1 
1474 N NE2 . GLN A 353 ? 0.2882 0.3232 0.2546 -0.0157 0.0391  -0.0419 353 GLN A NE2 
1475 N N   . HIS A 354 ? 0.2187 0.2928 0.2383 -0.0311 0.0333  -0.0276 354 HIS A N   
1476 C CA  . HIS A 354 ? 0.2180 0.2955 0.2453 -0.0379 0.0316  -0.0257 354 HIS A CA  
1477 C C   . HIS A 354 ? 0.2317 0.3300 0.2682 -0.0389 0.0342  -0.0264 354 HIS A C   
1478 O O   . HIS A 354 ? 0.2574 0.3658 0.2965 -0.0313 0.0350  -0.0286 354 HIS A O   
1479 C CB  . HIS A 354 ? 0.2061 0.2744 0.2352 -0.0367 0.0270  -0.0266 354 HIS A CB  
1480 C CG  . HIS A 354 ? 0.1978 0.2500 0.2208 -0.0384 0.0242  -0.0254 354 HIS A CG  
1481 N ND1 . HIS A 354 ? 0.2202 0.2670 0.2426 -0.0445 0.0234  -0.0225 354 HIS A ND1 
1482 C CD2 . HIS A 354 ? 0.2080 0.2499 0.2259 -0.0349 0.0220  -0.0268 354 HIS A CD2 
1483 C CE1 . HIS A 354 ? 0.2196 0.2557 0.2373 -0.0432 0.0205  -0.0221 354 HIS A CE1 
1484 N NE2 . HIS A 354 ? 0.2126 0.2463 0.2279 -0.0385 0.0196  -0.0248 354 HIS A NE2 
1485 N N   A GLN A 355 ? 0.2241 0.3288 0.2649 -0.0482 0.0358  -0.0246 355 GLN A N   
1486 N N   B GLN A 355 ? 0.2253 0.3301 0.2661 -0.0482 0.0359  -0.0245 355 GLN A N   
1487 C CA  A GLN A 355 ? 0.2233 0.3502 0.2735 -0.0518 0.0383  -0.0255 355 GLN A CA  
1488 C CA  B GLN A 355 ? 0.2238 0.3511 0.2742 -0.0517 0.0383  -0.0256 355 GLN A CA  
1489 C C   A GLN A 355 ? 0.2265 0.3560 0.2839 -0.0573 0.0349  -0.0270 355 GLN A C   
1490 C C   B GLN A 355 ? 0.2265 0.3553 0.2837 -0.0574 0.0348  -0.0269 355 GLN A C   
1491 O O   A GLN A 355 ? 0.2408 0.3782 0.3032 -0.0675 0.0364  -0.0269 355 GLN A O   
1492 O O   B GLN A 355 ? 0.2388 0.3733 0.3002 -0.0680 0.0362  -0.0266 355 GLN A O   
1493 C CB  A GLN A 355 ? 0.2430 0.3748 0.2920 -0.0608 0.0433  -0.0226 355 GLN A CB  
1494 C CB  B GLN A 355 ? 0.2436 0.3784 0.2935 -0.0602 0.0436  -0.0229 355 GLN A CB  
1495 C CG  A GLN A 355 ? 0.3085 0.4370 0.3486 -0.0560 0.0467  -0.0211 355 GLN A CG  
1496 C CG  B GLN A 355 ? 0.2874 0.4510 0.3470 -0.0613 0.0472  -0.0245 355 GLN A CG  
1497 C CD  A GLN A 355 ? 0.3612 0.5067 0.4036 -0.0462 0.0492  -0.0240 355 GLN A CD  
1498 C CD  B GLN A 355 ? 0.3432 0.5156 0.4053 -0.0744 0.0520  -0.0221 355 GLN A CD  
1499 O OE1 A GLN A 355 ? 0.3829 0.5512 0.4328 -0.0478 0.0529  -0.0244 355 GLN A OE1 
1500 O OE1 B GLN A 355 ? 0.3702 0.5496 0.4291 -0.0750 0.0572  -0.0200 355 GLN A OE1 
1501 N NE2 A GLN A 355 ? 0.3589 0.4937 0.3944 -0.0359 0.0475  -0.0260 355 GLN A NE2 
1502 N NE2 B GLN A 355 ? 0.3307 0.5024 0.3977 -0.0858 0.0508  -0.0226 355 GLN A NE2 
1503 N N   . GLY A 356 ? 0.2243 0.3458 0.2811 -0.0511 0.0305  -0.0285 356 GLY A N   
1504 C CA  . GLY A 356 ? 0.2102 0.3326 0.2720 -0.0548 0.0268  -0.0303 356 GLY A CA  
1505 C C   . GLY A 356 ? 0.2180 0.3301 0.2769 -0.0462 0.0229  -0.0311 356 GLY A C   
1506 O O   . GLY A 356 ? 0.2238 0.3252 0.2763 -0.0390 0.0230  -0.0302 356 GLY A O   
1507 N N   . ALA A 357 ? 0.2074 0.3229 0.2703 -0.0473 0.0195  -0.0330 357 ALA A N   
1508 C CA  . ALA A 357 ? 0.2019 0.3087 0.2618 -0.0395 0.0162  -0.0332 357 ALA A CA  
1509 C C   . ALA A 357 ? 0.2107 0.2948 0.2628 -0.0392 0.0154  -0.0314 357 ALA A C   
1510 O O   . ALA A 357 ? 0.2168 0.2918 0.2672 -0.0460 0.0157  -0.0305 357 ALA A O   
1511 C CB  . ALA A 357 ? 0.2078 0.3211 0.2720 -0.0423 0.0129  -0.0355 357 ALA A CB  
1512 N N   . VAL A 358 ? 0.1955 0.2710 0.2428 -0.0315 0.0146  -0.0308 358 VAL A N   
1513 C CA  . VAL A 358 ? 0.2109 0.2687 0.2518 -0.0320 0.0137  -0.0296 358 VAL A CA  
1514 C C   . VAL A 358 ? 0.2221 0.2738 0.2625 -0.0303 0.0109  -0.0298 358 VAL A C   
1515 O O   . VAL A 358 ? 0.2384 0.2873 0.2758 -0.0241 0.0107  -0.0296 358 VAL A O   
1516 C CB  . VAL A 358 ? 0.2374 0.2881 0.2716 -0.0275 0.0157  -0.0293 358 VAL A CB  
1517 C CG1 . VAL A 358 ? 0.2521 0.2885 0.2809 -0.0299 0.0143  -0.0286 358 VAL A CG1 
1518 C CG2 . VAL A 358 ? 0.2407 0.2993 0.2750 -0.0285 0.0190  -0.0293 358 VAL A CG2 
1519 N N   . LYS A 359 ? 0.2068 0.2558 0.2490 -0.0353 0.0091  -0.0301 359 LYS A N   
1520 C CA  . LYS A 359 ? 0.2040 0.2481 0.2453 -0.0336 0.0068  -0.0304 359 LYS A CA  
1521 C C   . LYS A 359 ? 0.2026 0.2342 0.2396 -0.0340 0.0063  -0.0289 359 LYS A C   
1522 O O   . LYS A 359 ? 0.2218 0.2492 0.2568 -0.0316 0.0054  -0.0285 359 LYS A O   
1523 C CB  . LYS A 359 ? 0.2157 0.2632 0.2604 -0.0384 0.0053  -0.0323 359 LYS A CB  
1524 C CG  . LYS A 359 ? 0.2639 0.3090 0.3075 -0.0360 0.0032  -0.0331 359 LYS A CG  
1525 C CD  . LYS A 359 ? 0.2916 0.3373 0.3367 -0.0408 0.0020  -0.0359 359 LYS A CD  
1526 C CE  . LYS A 359 ? 0.2942 0.3369 0.3370 -0.0377 0.0003  -0.0366 359 LYS A CE  
1527 N NZ  . LYS A 359 ? 0.2930 0.3377 0.3363 -0.0417 -0.0010 -0.0406 359 LYS A NZ  
1528 N N   . ALA A 360 ? 0.1897 0.2171 0.2251 -0.0372 0.0071  -0.0278 360 ALA A N   
1529 C CA  . ALA A 360 ? 0.1880 0.2076 0.2201 -0.0375 0.0062  -0.0264 360 ALA A CA  
1530 C C   . ALA A 360 ? 0.1973 0.2143 0.2253 -0.0360 0.0068  -0.0263 360 ALA A C   
1531 O O   . ALA A 360 ? 0.1948 0.2127 0.2206 -0.0362 0.0084  -0.0263 360 ALA A O   
1532 C CB  . ALA A 360 ? 0.2046 0.2208 0.2354 -0.0407 0.0067  -0.0248 360 ALA A CB  
1533 N N   . VAL A 361 ? 0.2009 0.2144 0.2273 -0.0349 0.0059  -0.0265 361 VAL A N   
1534 C CA  . VAL A 361 ? 0.2002 0.2089 0.2216 -0.0349 0.0067  -0.0272 361 VAL A CA  
1535 C C   . VAL A 361 ? 0.2007 0.2082 0.2217 -0.0373 0.0051  -0.0269 361 VAL A C   
1536 O O   . VAL A 361 ? 0.2069 0.2150 0.2301 -0.0366 0.0046  -0.0264 361 VAL A O   
1537 C CB  . VAL A 361 ? 0.2250 0.2305 0.2441 -0.0312 0.0084  -0.0279 361 VAL A CB  
1538 C CG1 . VAL A 361 ? 0.2488 0.2450 0.2606 -0.0319 0.0099  -0.0292 361 VAL A CG1 
1539 C CG2 . VAL A 361 ? 0.2305 0.2419 0.2514 -0.0276 0.0098  -0.0283 361 VAL A CG2 
1540 N N   . ALA A 362 ? 0.1871 0.1948 0.2054 -0.0399 0.0044  -0.0272 362 ALA A N   
1541 C CA  . ALA A 362 ? 0.1858 0.1968 0.2049 -0.0425 0.0027  -0.0270 362 ALA A CA  
1542 C C   . ALA A 362 ? 0.2012 0.2128 0.2160 -0.0464 0.0021  -0.0288 362 ALA A C   
1543 O O   . ALA A 362 ? 0.2059 0.2188 0.2180 -0.0463 0.0018  -0.0289 362 ALA A O   
1544 C CB  . ALA A 362 ? 0.1937 0.2106 0.2168 -0.0406 0.0009  -0.0249 362 ALA A CB  
1545 N N   . TRP A 363 ? 0.2105 0.2217 0.2239 -0.0508 0.0022  -0.0303 363 TRP A N   
1546 C CA  . TRP A 363 ? 0.2255 0.2375 0.2340 -0.0564 0.0015  -0.0332 363 TRP A CA  
1547 C C   . TRP A 363 ? 0.2380 0.2644 0.2501 -0.0583 -0.0017 -0.0326 363 TRP A C   
1548 O O   . TRP A 363 ? 0.2420 0.2762 0.2600 -0.0567 -0.0026 -0.0305 363 TRP A O   
1549 C CB  . TRP A 363 ? 0.2335 0.2368 0.2379 -0.0619 0.0037  -0.0356 363 TRP A CB  
1550 C CG  . TRP A 363 ? 0.2292 0.2169 0.2277 -0.0588 0.0071  -0.0362 363 TRP A CG  
1551 C CD1 . TRP A 363 ? 0.2446 0.2269 0.2443 -0.0539 0.0089  -0.0337 363 TRP A CD1 
1552 C CD2 . TRP A 363 ? 0.2364 0.2129 0.2261 -0.0593 0.0092  -0.0395 363 TRP A CD2 
1553 N NE1 . TRP A 363 ? 0.2540 0.2233 0.2466 -0.0505 0.0119  -0.0347 363 TRP A NE1 
1554 C CE2 . TRP A 363 ? 0.2465 0.2111 0.2327 -0.0535 0.0124  -0.0384 363 TRP A CE2 
1555 C CE3 . TRP A 363 ? 0.2389 0.2145 0.2223 -0.0636 0.0086  -0.0435 363 TRP A CE3 
1556 C CZ2 . TRP A 363 ? 0.2640 0.2150 0.2407 -0.0510 0.0155  -0.0410 363 TRP A CZ2 
1557 C CZ3 . TRP A 363 ? 0.2607 0.2221 0.2345 -0.0620 0.0117  -0.0467 363 TRP A CZ3 
1558 C CH2 . TRP A 363 ? 0.2723 0.2215 0.2430 -0.0551 0.0152  -0.0453 363 TRP A CH2 
1559 N N   . CYS A 364 ? 0.2294 0.2606 0.2373 -0.0614 -0.0034 -0.0347 364 CYS A N   
1560 C CA  . CYS A 364 ? 0.2289 0.2767 0.2398 -0.0624 -0.0069 -0.0341 364 CYS A CA  
1561 C C   . CYS A 364 ? 0.2429 0.2980 0.2566 -0.0697 -0.0072 -0.0363 364 CYS A C   
1562 O O   . CYS A 364 ? 0.2471 0.2956 0.2559 -0.0776 -0.0058 -0.0405 364 CYS A O   
1563 C CB  . CYS A 364 ? 0.2307 0.2831 0.2354 -0.0639 -0.0088 -0.0359 364 CYS A CB  
1564 S SG  . CYS A 364 ? 0.2849 0.3616 0.2927 -0.0644 -0.0138 -0.0351 364 CYS A SG  
1565 N N   . PRO A 365 ? 0.2542 0.3222 0.2754 -0.0673 -0.0084 -0.0337 365 PRO A N   
1566 C CA  . PRO A 365 ? 0.2744 0.3518 0.2993 -0.0750 -0.0080 -0.0355 365 PRO A CA  
1567 C C   . PRO A 365 ? 0.2972 0.3880 0.3206 -0.0843 -0.0104 -0.0397 365 PRO A C   
1568 O O   . PRO A 365 ? 0.3037 0.3986 0.3282 -0.0939 -0.0091 -0.0423 365 PRO A O   
1569 C CB  . PRO A 365 ? 0.2688 0.3608 0.3021 -0.0681 -0.0090 -0.0316 365 PRO A CB  
1570 C CG  . PRO A 365 ? 0.2694 0.3518 0.3021 -0.0579 -0.0088 -0.0282 365 PRO A CG  
1571 C CD  . PRO A 365 ? 0.2477 0.3214 0.2737 -0.0577 -0.0095 -0.0291 365 PRO A CD  
1572 N N   . TRP A 366 ? 0.2998 0.3994 0.3207 -0.0820 -0.0138 -0.0402 366 TRP A N   
1573 C CA  . TRP A 366 ? 0.3227 0.4380 0.3420 -0.0910 -0.0167 -0.0448 366 TRP A CA  
1574 C C   . TRP A 366 ? 0.3486 0.4508 0.3569 -0.0967 -0.0164 -0.0499 366 TRP A C   
1575 O O   . TRP A 366 ? 0.3618 0.4769 0.3671 -0.1039 -0.0194 -0.0545 366 TRP A O   
1576 C CB  . TRP A 366 ? 0.3241 0.4660 0.3487 -0.0847 -0.0216 -0.0420 366 TRP A CB  
1577 C CG  . TRP A 366 ? 0.3390 0.4770 0.3589 -0.0742 -0.0232 -0.0382 366 TRP A CG  
1578 C CD1 . TRP A 366 ? 0.3529 0.4957 0.3658 -0.0747 -0.0260 -0.0399 366 TRP A CD1 
1579 C CD2 . TRP A 366 ? 0.3365 0.4664 0.3581 -0.0620 -0.0220 -0.0320 366 TRP A CD2 
1580 N NE1 . TRP A 366 ? 0.3601 0.4968 0.3697 -0.0636 -0.0260 -0.0344 366 TRP A NE1 
1581 C CE2 . TRP A 366 ? 0.3502 0.4787 0.3652 -0.0561 -0.0236 -0.0296 366 TRP A CE2 
1582 C CE3 . TRP A 366 ? 0.3365 0.4605 0.3637 -0.0559 -0.0197 -0.0284 366 TRP A CE3 
1583 C CZ2 . TRP A 366 ? 0.3558 0.4744 0.3694 -0.0456 -0.0224 -0.0237 366 TRP A CZ2 
1584 C CZ3 . TRP A 366 ? 0.3492 0.4633 0.3748 -0.0456 -0.0189 -0.0235 366 TRP A CZ3 
1585 C CH2 . TRP A 366 ? 0.3572 0.4682 0.3762 -0.0410 -0.0200 -0.0211 366 TRP A CH2 
1586 N N   . GLN A 367 ? 0.3489 0.4275 0.3511 -0.0928 -0.0130 -0.0495 367 GLN A N   
1587 C CA  . GLN A 367 ? 0.3691 0.4342 0.3601 -0.0966 -0.0119 -0.0546 367 GLN A CA  
1588 C C   . GLN A 367 ? 0.3794 0.4189 0.3655 -0.0962 -0.0067 -0.0553 367 GLN A C   
1589 O O   . GLN A 367 ? 0.3689 0.3995 0.3561 -0.0871 -0.0049 -0.0513 367 GLN A O   
1590 C CB  . GLN A 367 ? 0.3987 0.4663 0.3864 -0.0880 -0.0136 -0.0521 367 GLN A CB  
1591 C CG  . GLN A 367 ? 0.4522 0.5435 0.4415 -0.0868 -0.0188 -0.0511 367 GLN A CG  
1592 C CD  . GLN A 367 ? 0.5281 0.6172 0.5109 -0.0798 -0.0193 -0.0489 367 GLN A CD  
1593 O OE1 . GLN A 367 ? 0.5659 0.6537 0.5394 -0.0838 -0.0198 -0.0537 367 GLN A OE1 
1594 N NE2 . GLN A 367 ? 0.5404 0.6275 0.5268 -0.0697 -0.0186 -0.0419 367 GLN A NE2 
1595 N N   . SER A 368 ? 0.3802 0.4078 0.3597 -0.1062 -0.0043 -0.0606 368 SER A N   
1596 C CA  . SER A 368 ? 0.3922 0.3941 0.3649 -0.1066 0.0010  -0.0615 368 SER A CA  
1597 C C   . SER A 368 ? 0.3694 0.3562 0.3373 -0.0960 0.0036  -0.0598 368 SER A C   
1598 O O   . SER A 368 ? 0.3854 0.3618 0.3552 -0.0897 0.0064  -0.0561 368 SER A O   
1599 C CB  . SER A 368 ? 0.4489 0.4381 0.4107 -0.1196 0.0031  -0.0689 368 SER A CB  
1600 O OG  . SER A 368 ? 0.5333 0.4935 0.4850 -0.1186 0.0088  -0.0700 368 SER A OG  
1601 N N   . ASN A 369 ? 0.3379 0.3255 0.2998 -0.0941 0.0026  -0.0627 369 ASN A N   
1602 C CA  . ASN A 369 ? 0.3293 0.3041 0.2858 -0.0853 0.0056  -0.0621 369 ASN A CA  
1603 C C   . ASN A 369 ? 0.3021 0.2892 0.2658 -0.0760 0.0040  -0.0566 369 ASN A C   
1604 O O   . ASN A 369 ? 0.3036 0.2840 0.2633 -0.0697 0.0065  -0.0564 369 ASN A O   
1605 C CB  . ASN A 369 ? 0.3792 0.3447 0.3225 -0.0891 0.0068  -0.0692 369 ASN A CB  
1606 C CG  . ASN A 369 ? 0.4647 0.4126 0.3984 -0.0988 0.0095  -0.0753 369 ASN A CG  
1607 O OD1 . ASN A 369 ? 0.4942 0.4280 0.4277 -0.0990 0.0128  -0.0735 369 ASN A OD1 
1608 N ND2 . ASN A 369 ? 0.5057 0.4532 0.4300 -0.1075 0.0083  -0.0828 369 ASN A ND2 
1609 N N   . VAL A 370 ? 0.2609 0.2647 0.2343 -0.0749 0.0005  -0.0521 370 VAL A N   
1610 C CA  . VAL A 370 ? 0.2382 0.2503 0.2164 -0.0671 -0.0005 -0.0470 370 VAL A CA  
1611 C C   . VAL A 370 ? 0.2227 0.2317 0.2087 -0.0614 0.0010  -0.0422 370 VAL A C   
1612 O O   . VAL A 370 ? 0.2192 0.2306 0.2110 -0.0628 0.0003  -0.0408 370 VAL A O   
1613 C CB  . VAL A 370 ? 0.2414 0.2716 0.2223 -0.0675 -0.0051 -0.0449 370 VAL A CB  
1614 C CG1 . VAL A 370 ? 0.2278 0.2623 0.2123 -0.0596 -0.0053 -0.0387 370 VAL A CG1 
1615 C CG2 . VAL A 370 ? 0.2580 0.2933 0.2300 -0.0726 -0.0069 -0.0499 370 VAL A CG2 
1616 N N   . LEU A 371 ? 0.2176 0.2220 0.2034 -0.0555 0.0033  -0.0403 371 LEU A N   
1617 C CA  . LEU A 371 ? 0.2145 0.2169 0.2071 -0.0508 0.0047  -0.0368 371 LEU A CA  
1618 C C   . LEU A 371 ? 0.2101 0.2190 0.2065 -0.0470 0.0043  -0.0328 371 LEU A C   
1619 O O   . LEU A 371 ? 0.2161 0.2265 0.2081 -0.0462 0.0052  -0.0328 371 LEU A O   
1620 C CB  . LEU A 371 ? 0.2115 0.2028 0.2000 -0.0478 0.0085  -0.0387 371 LEU A CB  
1621 C CG  . LEU A 371 ? 0.2203 0.2116 0.2148 -0.0425 0.0098  -0.0359 371 LEU A CG  
1622 C CD1 . LEU A 371 ? 0.2163 0.2076 0.2157 -0.0436 0.0086  -0.0343 371 LEU A CD1 
1623 C CD2 . LEU A 371 ? 0.2212 0.2046 0.2109 -0.0377 0.0134  -0.0376 371 LEU A CD2 
1624 N N   . ALA A 372 ? 0.1928 0.2043 0.1962 -0.0449 0.0036  -0.0295 372 ALA A N   
1625 C CA  . ALA A 372 ? 0.1908 0.2046 0.1968 -0.0423 0.0042  -0.0260 372 ALA A CA  
1626 C C   . ALA A 372 ? 0.1989 0.2103 0.2092 -0.0405 0.0063  -0.0261 372 ALA A C   
1627 O O   . ALA A 372 ? 0.2069 0.2165 0.2201 -0.0399 0.0060  -0.0270 372 ALA A O   
1628 C CB  . ALA A 372 ? 0.1889 0.2064 0.1982 -0.0413 0.0018  -0.0228 372 ALA A CB  
1629 N N   . THR A 373 ? 0.1951 0.2082 0.2056 -0.0398 0.0084  -0.0251 373 THR A N   
1630 C CA  . THR A 373 ? 0.2024 0.2176 0.2177 -0.0385 0.0101  -0.0254 373 THR A CA  
1631 C C   . THR A 373 ? 0.2086 0.2263 0.2263 -0.0407 0.0110  -0.0228 373 THR A C   
1632 O O   . THR A 373 ? 0.2214 0.2382 0.2352 -0.0420 0.0115  -0.0206 373 THR A O   
1633 C CB  . THR A 373 ? 0.2151 0.2316 0.2284 -0.0357 0.0127  -0.0276 373 THR A CB  
1634 O OG1 . THR A 373 ? 0.2259 0.2447 0.2349 -0.0364 0.0147  -0.0274 373 THR A OG1 
1635 C CG2 . THR A 373 ? 0.2250 0.2342 0.2339 -0.0339 0.0126  -0.0301 373 THR A CG2 
1636 N N   . GLY A 374 ? 0.2035 0.2240 0.2267 -0.0414 0.0113  -0.0232 374 GLY A N   
1637 C CA  . GLY A 374 ? 0.1960 0.2172 0.2209 -0.0453 0.0128  -0.0215 374 GLY A CA  
1638 C C   . GLY A 374 ? 0.1972 0.2277 0.2277 -0.0469 0.0144  -0.0234 374 GLY A C   
1639 O O   . GLY A 374 ? 0.2057 0.2403 0.2399 -0.0444 0.0130  -0.0256 374 GLY A O   
1640 N N   . GLY A 375 ? 0.2007 0.2356 0.2318 -0.0514 0.0172  -0.0223 375 GLY A N   
1641 C CA  . GLY A 375 ? 0.2097 0.2580 0.2473 -0.0537 0.0188  -0.0243 375 GLY A CA  
1642 C C   . GLY A 375 ? 0.2220 0.2703 0.2630 -0.0610 0.0189  -0.0252 375 GLY A C   
1643 O O   . GLY A 375 ? 0.2268 0.2621 0.2637 -0.0645 0.0189  -0.0235 375 GLY A O   
1644 N N   . GLY A 376 ? 0.2136 0.2770 0.2615 -0.0631 0.0191  -0.0280 376 GLY A N   
1645 C CA  . GLY A 376 ? 0.2337 0.2997 0.2852 -0.0715 0.0191  -0.0303 376 GLY A CA  
1646 C C   . GLY A 376 ? 0.2428 0.3060 0.2926 -0.0815 0.0231  -0.0286 376 GLY A C   
1647 O O   . GLY A 376 ? 0.2441 0.3004 0.2887 -0.0813 0.0258  -0.0247 376 GLY A O   
1648 N N   . THR A 377 ? 0.2366 0.3051 0.2902 -0.0910 0.0237  -0.0316 377 THR A N   
1649 C CA  . THR A 377 ? 0.2521 0.3150 0.3033 -0.1030 0.0280  -0.0305 377 THR A CA  
1650 C C   . THR A 377 ? 0.2466 0.3205 0.2988 -0.1057 0.0327  -0.0273 377 THR A C   
1651 O O   . THR A 377 ? 0.2662 0.3268 0.3114 -0.1116 0.0368  -0.0232 377 THR A O   
1652 C CB  . THR A 377 ? 0.2814 0.3528 0.3378 -0.1138 0.0276  -0.0359 377 THR A CB  
1653 O OG1 . THR A 377 ? 0.2964 0.3575 0.3507 -0.1104 0.0234  -0.0392 377 THR A OG1 
1654 C CG2 . THR A 377 ? 0.2983 0.3582 0.3501 -0.1280 0.0325  -0.0350 377 THR A CG2 
1655 N N   . SER A 378 ? 0.2238 0.3215 0.2836 -0.1006 0.0326  -0.0287 378 SER A N   
1656 C CA  . SER A 378 ? 0.2196 0.3303 0.2805 -0.1021 0.0375  -0.0262 378 SER A CA  
1657 C C   . SER A 378 ? 0.2127 0.3112 0.2650 -0.0935 0.0385  -0.0218 378 SER A C   
1658 O O   . SER A 378 ? 0.2227 0.3287 0.2734 -0.0946 0.0430  -0.0192 378 SER A O   
1659 C CB  . SER A 378 ? 0.2265 0.3675 0.2980 -0.0978 0.0372  -0.0294 378 SER A CB  
1660 O OG  . SER A 378 ? 0.2476 0.3880 0.3187 -0.0840 0.0331  -0.0304 378 SER A OG  
1661 N N   . ASP A 379 ? 0.2079 0.2892 0.2545 -0.0856 0.0346  -0.0211 379 ASP A N   
1662 C CA  . ASP A 379 ? 0.2181 0.2896 0.2568 -0.0778 0.0344  -0.0182 379 ASP A CA  
1663 C C   . ASP A 379 ? 0.2350 0.2842 0.2644 -0.0794 0.0340  -0.0142 379 ASP A C   
1664 O O   . ASP A 379 ? 0.2429 0.2867 0.2651 -0.0805 0.0371  -0.0099 379 ASP A O   
1665 C CB  . ASP A 379 ? 0.2219 0.2950 0.2618 -0.0671 0.0305  -0.0208 379 ASP A CB  
1666 C CG  . ASP A 379 ? 0.2569 0.3202 0.2883 -0.0608 0.0302  -0.0189 379 ASP A CG  
1667 O OD1 . ASP A 379 ? 0.2634 0.3338 0.2921 -0.0589 0.0334  -0.0183 379 ASP A OD1 
1668 O OD2 . ASP A 379 ? 0.2733 0.3229 0.3004 -0.0582 0.0268  -0.0183 379 ASP A OD2 
1669 N N   . ARG A 380 ? 0.2319 0.2692 0.2609 -0.0786 0.0304  -0.0154 380 ARG A N   
1670 C CA  . ARG A 380 ? 0.2473 0.2641 0.2682 -0.0787 0.0298  -0.0120 380 ARG A CA  
1671 C C   . ARG A 380 ? 0.2627 0.2728 0.2767 -0.0707 0.0280  -0.0090 380 ARG A C   
1672 O O   . ARG A 380 ? 0.2944 0.2897 0.3011 -0.0697 0.0278  -0.0052 380 ARG A O   
1673 C CB  . ARG A 380 ? 0.2737 0.2805 0.2889 -0.0879 0.0346  -0.0083 380 ARG A CB  
1674 C CG  . ARG A 380 ? 0.3271 0.3422 0.3488 -0.0989 0.0372  -0.0116 380 ARG A CG  
1675 C CD  . ARG A 380 ? 0.4013 0.4037 0.4158 -0.1096 0.0429  -0.0075 380 ARG A CD  
1676 N NE  . ARG A 380 ? 0.5004 0.4998 0.5071 -0.1073 0.0464  -0.0011 380 ARG A NE  
1677 C CZ  . ARG A 380 ? 0.5872 0.6038 0.5968 -0.1099 0.0500  -0.0001 380 ARG A CZ  
1678 N NH1 . ARG A 380 ? 0.6106 0.6232 0.6113 -0.1072 0.0530  0.0057  380 ARG A NH1 
1679 N NH2 . ARG A 380 ? 0.5759 0.6151 0.5968 -0.1146 0.0507  -0.0049 380 ARG A NH2 
1680 N N   . HIS A 381 ? 0.2412 0.2615 0.2565 -0.0652 0.0269  -0.0104 381 HIS A N   
1681 C CA  . HIS A 381 ? 0.2355 0.2506 0.2436 -0.0594 0.0251  -0.0083 381 HIS A CA  
1682 C C   . HIS A 381 ? 0.2318 0.2461 0.2418 -0.0535 0.0205  -0.0111 381 HIS A C   
1683 O O   . HIS A 381 ? 0.2362 0.2564 0.2522 -0.0522 0.0192  -0.0150 381 HIS A O   
1684 C CB  . HIS A 381 ? 0.2412 0.2657 0.2464 -0.0580 0.0277  -0.0082 381 HIS A CB  
1685 C CG  . HIS A 381 ? 0.2837 0.3077 0.2834 -0.0627 0.0324  -0.0036 381 HIS A CG  
1686 N ND1 . HIS A 381 ? 0.2935 0.3201 0.2970 -0.0704 0.0363  -0.0028 381 HIS A ND1 
1687 C CD2 . HIS A 381 ? 0.3062 0.3275 0.2964 -0.0611 0.0338  0.0003  381 HIS A CD2 
1688 C CE1 . HIS A 381 ? 0.3186 0.3430 0.3147 -0.0736 0.0405  0.0022  381 HIS A CE1 
1689 N NE2 . HIS A 381 ? 0.3264 0.3476 0.3139 -0.0675 0.0392  0.0044  381 HIS A NE2 
1690 N N   . ILE A 382 ? 0.2194 0.2276 0.2235 -0.0500 0.0182  -0.0088 382 ILE A N   
1691 C CA  . ILE A 382 ? 0.2068 0.2164 0.2115 -0.0458 0.0144  -0.0112 382 ILE A CA  
1692 C C   . ILE A 382 ? 0.2196 0.2340 0.2189 -0.0444 0.0147  -0.0120 382 ILE A C   
1693 O O   . ILE A 382 ? 0.2323 0.2463 0.2248 -0.0445 0.0160  -0.0087 382 ILE A O   
1694 C CB  . ILE A 382 ? 0.2144 0.2177 0.2163 -0.0429 0.0117  -0.0084 382 ILE A CB  
1695 C CG1 . ILE A 382 ? 0.2375 0.2342 0.2433 -0.0438 0.0117  -0.0086 382 ILE A CG1 
1696 C CG2 . ILE A 382 ? 0.2047 0.2129 0.2069 -0.0400 0.0081  -0.0108 382 ILE A CG2 
1697 C CD1 . ILE A 382 ? 0.2688 0.2573 0.2703 -0.0398 0.0103  -0.0051 382 ILE A CD1 
1698 N N   . ARG A 383 ? 0.2101 0.2279 0.2110 -0.0430 0.0139  -0.0164 383 ARG A N   
1699 C CA  . ARG A 383 ? 0.2158 0.2360 0.2102 -0.0420 0.0143  -0.0186 383 ARG A CA  
1700 C C   . ARG A 383 ? 0.2175 0.2361 0.2106 -0.0414 0.0107  -0.0216 383 ARG A C   
1701 O O   . ARG A 383 ? 0.2267 0.2432 0.2249 -0.0412 0.0095  -0.0233 383 ARG A O   
1702 C CB  . ARG A 383 ? 0.2232 0.2470 0.2184 -0.0410 0.0177  -0.0216 383 ARG A CB  
1703 C CG  . ARG A 383 ? 0.2197 0.2488 0.2153 -0.0428 0.0217  -0.0188 383 ARG A CG  
1704 C CD  . ARG A 383 ? 0.2420 0.2784 0.2397 -0.0406 0.0252  -0.0218 383 ARG A CD  
1705 N NE  . ARG A 383 ? 0.2480 0.2927 0.2459 -0.0430 0.0297  -0.0193 383 ARG A NE  
1706 C CZ  . ARG A 383 ? 0.2661 0.3142 0.2567 -0.0423 0.0326  -0.0189 383 ARG A CZ  
1707 N NH1 . ARG A 383 ? 0.2732 0.3303 0.2648 -0.0450 0.0373  -0.0164 383 ARG A NH1 
1708 N NH2 . ARG A 383 ? 0.2733 0.3171 0.2556 -0.0391 0.0314  -0.0217 383 ARG A NH2 
1709 N N   . ILE A 384 ? 0.2167 0.2372 0.2027 -0.0418 0.0092  -0.0224 384 ILE A N   
1710 C CA  . ILE A 384 ? 0.2199 0.2407 0.2044 -0.0433 0.0061  -0.0260 384 ILE A CA  
1711 C C   . ILE A 384 ? 0.2312 0.2496 0.2086 -0.0443 0.0078  -0.0312 384 ILE A C   
1712 O O   . ILE A 384 ? 0.2401 0.2606 0.2112 -0.0435 0.0096  -0.0311 384 ILE A O   
1713 C CB  . ILE A 384 ? 0.2411 0.2685 0.2229 -0.0433 0.0024  -0.0235 384 ILE A CB  
1714 C CG1 . ILE A 384 ? 0.2589 0.2861 0.2451 -0.0404 0.0017  -0.0176 384 ILE A CG1 
1715 C CG2 . ILE A 384 ? 0.2547 0.2858 0.2364 -0.0465 -0.0009 -0.0276 384 ILE A CG2 
1716 C CD1 . ILE A 384 ? 0.2765 0.3007 0.2711 -0.0403 0.0012  -0.0182 384 ILE A CD1 
1717 N N   . TRP A 385 ? 0.2312 0.2436 0.2082 -0.0459 0.0077  -0.0357 385 TRP A N   
1718 C CA  . TRP A 385 ? 0.2364 0.2418 0.2050 -0.0464 0.0100  -0.0414 385 TRP A CA  
1719 C C   . TRP A 385 ? 0.2454 0.2472 0.2090 -0.0520 0.0077  -0.0463 385 TRP A C   
1720 O O   . TRP A 385 ? 0.2466 0.2497 0.2155 -0.0549 0.0054  -0.0455 385 TRP A O   
1721 C CB  . TRP A 385 ? 0.2307 0.2279 0.2018 -0.0428 0.0133  -0.0424 385 TRP A CB  
1722 C CG  . TRP A 385 ? 0.2313 0.2339 0.2101 -0.0387 0.0151  -0.0382 385 TRP A CG  
1723 C CD1 . TRP A 385 ? 0.2385 0.2437 0.2263 -0.0383 0.0138  -0.0348 385 TRP A CD1 
1724 C CD2 . TRP A 385 ? 0.2383 0.2454 0.2162 -0.0350 0.0187  -0.0376 385 TRP A CD2 
1725 N NE1 . TRP A 385 ? 0.2432 0.2540 0.2358 -0.0356 0.0162  -0.0326 385 TRP A NE1 
1726 C CE2 . TRP A 385 ? 0.2433 0.2564 0.2306 -0.0337 0.0193  -0.0340 385 TRP A CE2 
1727 C CE3 . TRP A 385 ? 0.2566 0.2640 0.2264 -0.0330 0.0218  -0.0403 385 TRP A CE3 
1728 C CZ2 . TRP A 385 ? 0.2558 0.2770 0.2457 -0.0312 0.0228  -0.0328 385 TRP A CZ2 
1729 C CZ3 . TRP A 385 ? 0.2660 0.2814 0.2384 -0.0294 0.0256  -0.0387 385 TRP A CZ3 
1730 C CH2 . TRP A 385 ? 0.2698 0.2929 0.2526 -0.0291 0.0260  -0.0349 385 TRP A CH2 
1731 N N   . ASN A 386 ? 0.2475 0.2438 0.2004 -0.0539 0.0091  -0.0520 386 ASN A N   
1732 C CA  . ASN A 386 ? 0.2762 0.2649 0.2228 -0.0606 0.0081  -0.0581 386 ASN A CA  
1733 C C   . ASN A 386 ? 0.3027 0.2735 0.2442 -0.0571 0.0132  -0.0610 386 ASN A C   
1734 O O   . ASN A 386 ? 0.3120 0.2781 0.2466 -0.0521 0.0166  -0.0631 386 ASN A O   
1735 C CB  . ASN A 386 ? 0.2985 0.2916 0.2349 -0.0654 0.0063  -0.0633 386 ASN A CB  
1736 C CG  . ASN A 386 ? 0.3705 0.3544 0.3000 -0.0743 0.0058  -0.0706 386 ASN A CG  
1737 O OD1 . ASN A 386 ? 0.3779 0.3433 0.3014 -0.0745 0.0097  -0.0743 386 ASN A OD1 
1738 N ND2 . ASN A 386 ? 0.3981 0.3948 0.3282 -0.0820 0.0011  -0.0726 386 ASN A ND2 
1739 N N   . VAL A 387 ? 0.2995 0.2607 0.2438 -0.0583 0.0140  -0.0606 387 VAL A N   
1740 C CA  . VAL A 387 ? 0.3111 0.2551 0.2502 -0.0529 0.0188  -0.0619 387 VAL A CA  
1741 C C   . VAL A 387 ? 0.3524 0.2774 0.2760 -0.0557 0.0219  -0.0693 387 VAL A C   
1742 O O   . VAL A 387 ? 0.3738 0.2834 0.2906 -0.0488 0.0265  -0.0705 387 VAL A O   
1743 C CB  . VAL A 387 ? 0.2960 0.2352 0.2417 -0.0522 0.0190  -0.0580 387 VAL A CB  
1744 C CG1 . VAL A 387 ? 0.2907 0.2467 0.2502 -0.0491 0.0163  -0.0517 387 VAL A CG1 
1745 C CG2 . VAL A 387 ? 0.2967 0.2299 0.2398 -0.0624 0.0177  -0.0605 387 VAL A CG2 
1746 N N   A CYS A 388 ? 0.3573 0.2835 0.2749 -0.0653 0.0195  -0.0745 388 CYS A N   
1747 N N   B CYS A 388 ? 0.3607 0.2869 0.2780 -0.0651 0.0196  -0.0747 388 CYS A N   
1748 C CA  A CYS A 388 ? 0.3817 0.2893 0.2834 -0.0697 0.0223  -0.0829 388 CYS A CA  
1749 C CA  B CYS A 388 ? 0.3883 0.2953 0.2893 -0.0693 0.0225  -0.0831 388 CYS A CA  
1750 C C   A CYS A 388 ? 0.3854 0.2944 0.2789 -0.0632 0.0244  -0.0860 388 CYS A C   
1751 C C   B CYS A 388 ? 0.3893 0.2979 0.2818 -0.0639 0.0243  -0.0867 388 CYS A C   
1752 O O   A CYS A 388 ? 0.4022 0.2935 0.2850 -0.0569 0.0295  -0.0894 388 CYS A O   
1753 O O   B CYS A 388 ? 0.4076 0.2972 0.2871 -0.0598 0.0292  -0.0918 388 CYS A O   
1754 C CB  A CYS A 388 ? 0.3974 0.3092 0.2964 -0.0838 0.0186  -0.0879 388 CYS A CB  
1755 C CB  B CYS A 388 ? 0.4123 0.3211 0.3102 -0.0836 0.0192  -0.0882 388 CYS A CB  
1756 S SG  A CYS A 388 ? 0.4666 0.3539 0.3442 -0.0925 0.0218  -0.0998 388 CYS A SG  
1757 S SG  B CYS A 388 ? 0.4893 0.3904 0.3928 -0.0914 0.0193  -0.0857 388 CYS A SG  
1758 N N   . SER A 389 ? 0.3709 0.3010 0.2692 -0.0637 0.0208  -0.0841 389 SER A N   
1759 C CA  . SER A 389 ? 0.3669 0.3012 0.2574 -0.0585 0.0227  -0.0865 389 SER A CA  
1760 C C   . SER A 389 ? 0.3635 0.3043 0.2609 -0.0468 0.0260  -0.0804 389 SER A C   
1761 O O   . SER A 389 ? 0.3756 0.3189 0.2663 -0.0415 0.0290  -0.0823 389 SER A O   
1762 C CB  . SER A 389 ? 0.3710 0.3253 0.2625 -0.0638 0.0176  -0.0861 389 SER A CB  
1763 O OG  . SER A 389 ? 0.3582 0.3297 0.2642 -0.0612 0.0146  -0.0771 389 SER A OG  
1764 N N   . GLY A 390 ? 0.3314 0.2781 0.2424 -0.0439 0.0252  -0.0734 390 GLY A N   
1765 C CA  . GLY A 390 ? 0.3313 0.2878 0.2506 -0.0351 0.0276  -0.0677 390 GLY A CA  
1766 C C   . GLY A 390 ? 0.3207 0.2965 0.2461 -0.0360 0.0255  -0.0628 390 GLY A C   
1767 O O   . GLY A 390 ? 0.3313 0.3164 0.2630 -0.0307 0.0278  -0.0584 390 GLY A O   
1768 N N   . ALA A 391 ? 0.3119 0.2941 0.2347 -0.0428 0.0212  -0.0635 391 ALA A N   
1769 C CA  . ALA A 391 ? 0.3143 0.3120 0.2399 -0.0427 0.0196  -0.0583 391 ALA A CA  
1770 C C   . ALA A 391 ? 0.2932 0.2986 0.2322 -0.0419 0.0180  -0.0505 391 ALA A C   
1771 O O   . ALA A 391 ? 0.2836 0.2868 0.2294 -0.0443 0.0153  -0.0494 391 ALA A O   
1772 C CB  . ALA A 391 ? 0.3223 0.3261 0.2414 -0.0488 0.0150  -0.0605 391 ALA A CB  
1773 N N   . CYS A 392 ? 0.2747 0.2890 0.2166 -0.0392 0.0199  -0.0452 392 CYS A N   
1774 C CA  . CYS A 392 ? 0.2745 0.2947 0.2267 -0.0396 0.0184  -0.0381 392 CYS A CA  
1775 C C   . CYS A 392 ? 0.2849 0.3114 0.2326 -0.0418 0.0149  -0.0350 392 CYS A C   
1776 O O   . CYS A 392 ? 0.2994 0.3307 0.2391 -0.0411 0.0164  -0.0341 392 CYS A O   
1777 C CB  . CYS A 392 ? 0.2783 0.3036 0.2352 -0.0369 0.0228  -0.0341 392 CYS A CB  
1778 S SG  . CYS A 392 ? 0.3305 0.3591 0.2975 -0.0390 0.0214  -0.0263 392 CYS A SG  
1779 N N   . LEU A 393 ? 0.2814 0.3089 0.2330 -0.0440 0.0104  -0.0339 393 LEU A N   
1780 C CA  . LEU A 393 ? 0.2842 0.3196 0.2321 -0.0447 0.0063  -0.0310 393 LEU A CA  
1781 C C   . LEU A 393 ? 0.2842 0.3221 0.2346 -0.0418 0.0069  -0.0224 393 LEU A C   
1782 O O   . LEU A 393 ? 0.2873 0.3310 0.2314 -0.0402 0.0051  -0.0185 393 LEU A O   
1783 C CB  . LEU A 393 ? 0.2910 0.3286 0.2434 -0.0476 0.0016  -0.0332 393 LEU A CB  
1784 C CG  . LEU A 393 ? 0.3164 0.3483 0.2660 -0.0523 0.0014  -0.0415 393 LEU A CG  
1785 C CD1 . LEU A 393 ? 0.3165 0.3521 0.2720 -0.0563 -0.0025 -0.0427 393 LEU A CD1 
1786 C CD2 . LEU A 393 ? 0.3376 0.3712 0.2750 -0.0547 0.0013  -0.0471 393 LEU A CD2 
1787 N N   . SER A 394 ? 0.2793 0.3120 0.2381 -0.0411 0.0093  -0.0195 394 SER A N   
1788 C CA  . SER A 394 ? 0.2716 0.3028 0.2318 -0.0396 0.0105  -0.0120 394 SER A CA  
1789 C C   . SER A 394 ? 0.2783 0.3049 0.2462 -0.0409 0.0144  -0.0112 394 SER A C   
1790 O O   . SER A 394 ? 0.2644 0.2895 0.2390 -0.0414 0.0142  -0.0152 394 SER A O   
1791 C CB  . SER A 394 ? 0.2812 0.3127 0.2446 -0.0377 0.0062  -0.0090 394 SER A CB  
1792 O OG  . SER A 394 ? 0.3203 0.3463 0.2831 -0.0356 0.0079  -0.0019 394 SER A OG  
1793 N N   . ALA A 395 ? 0.2797 0.3044 0.2461 -0.0417 0.0180  -0.0058 395 ALA A N   
1794 C CA  . ALA A 395 ? 0.2839 0.3065 0.2578 -0.0445 0.0215  -0.0052 395 ALA A CA  
1795 C C   . ALA A 395 ? 0.3049 0.3201 0.2763 -0.0458 0.0227  0.0017  395 ALA A C   
1796 O O   . ALA A 395 ? 0.3323 0.3464 0.2950 -0.0457 0.0250  0.0066  395 ALA A O   
1797 C CB  . ALA A 395 ? 0.2878 0.3171 0.2613 -0.0459 0.0264  -0.0068 395 ALA A CB  
1798 N N   . VAL A 396 ? 0.2886 0.2971 0.2656 -0.0462 0.0212  0.0022  396 VAL A N   
1799 C CA  . VAL A 396 ? 0.3037 0.3010 0.2768 -0.0466 0.0225  0.0082  396 VAL A CA  
1800 C C   . VAL A 396 ? 0.3026 0.2949 0.2820 -0.0524 0.0255  0.0073  396 VAL A C   
1801 O O   . VAL A 396 ? 0.2832 0.2787 0.2713 -0.0531 0.0237  0.0024  396 VAL A O   
1802 C CB  . VAL A 396 ? 0.3443 0.3371 0.3157 -0.0407 0.0180  0.0097  396 VAL A CB  
1803 C CG1 . VAL A 396 ? 0.3681 0.3460 0.3340 -0.0397 0.0199  0.0158  396 VAL A CG1 
1804 C CG2 . VAL A 396 ? 0.3560 0.3569 0.3210 -0.0360 0.0147  0.0105  396 VAL A CG2 
1805 N N   . ASP A 397 ? 0.3186 0.3029 0.2930 -0.0572 0.0302  0.0120  397 ASP A N   
1806 C CA  . ASP A 397 ? 0.3330 0.3126 0.3125 -0.0647 0.0332  0.0107  397 ASP A CA  
1807 C C   . ASP A 397 ? 0.3406 0.3044 0.3184 -0.0629 0.0314  0.0116  397 ASP A C   
1808 O O   . ASP A 397 ? 0.3740 0.3233 0.3416 -0.0600 0.0324  0.0176  397 ASP A O   
1809 C CB  . ASP A 397 ? 0.3644 0.3405 0.3381 -0.0721 0.0397  0.0156  397 ASP A CB  
1810 C CG  . ASP A 397 ? 0.4160 0.3924 0.3961 -0.0826 0.0433  0.0131  397 ASP A CG  
1811 O OD1 . ASP A 397 ? 0.4047 0.3799 0.3918 -0.0837 0.0406  0.0083  397 ASP A OD1 
1812 O OD2 . ASP A 397 ? 0.4624 0.4421 0.4406 -0.0903 0.0489  0.0157  397 ASP A OD2 
1813 N N   . ALA A 398 ? 0.3078 0.2740 0.2943 -0.0638 0.0289  0.0060  398 ALA A N   
1814 C CA  . ALA A 398 ? 0.3218 0.2741 0.3069 -0.0622 0.0275  0.0055  398 ALA A CA  
1815 C C   . ALA A 398 ? 0.3387 0.2777 0.3215 -0.0712 0.0317  0.0055  398 ALA A C   
1816 O O   . ALA A 398 ? 0.3503 0.2743 0.3296 -0.0700 0.0313  0.0048  398 ALA A O   
1817 C CB  . ALA A 398 ? 0.3137 0.2750 0.3081 -0.0590 0.0230  -0.0006 398 ALA A CB  
1818 N N   . HIS A 399 ? 0.3350 0.2803 0.3197 -0.0808 0.0360  0.0054  399 HIS A N   
1819 C CA  . HIS A 399 ? 0.3525 0.2881 0.3356 -0.0925 0.0406  0.0047  399 HIS A CA  
1820 C C   . HIS A 399 ? 0.3378 0.2767 0.3291 -0.0976 0.0386  -0.0028 399 HIS A C   
1821 O O   . HIS A 399 ? 0.3533 0.2792 0.3412 -0.1067 0.0416  -0.0044 399 HIS A O   
1822 C CB  . HIS A 399 ? 0.4015 0.3094 0.3699 -0.0930 0.0445  0.0112  399 HIS A CB  
1823 C CG  . HIS A 399 ? 0.4629 0.3682 0.4219 -0.0877 0.0464  0.0193  399 HIS A CG  
1824 N ND1 . HIS A 399 ? 0.5054 0.4171 0.4624 -0.0951 0.0514  0.0227  399 HIS A ND1 
1825 C CD2 . HIS A 399 ? 0.4887 0.3886 0.4402 -0.0756 0.0437  0.0242  399 HIS A CD2 
1826 C CE1 . HIS A 399 ? 0.5199 0.4284 0.4674 -0.0872 0.0516  0.0295  399 HIS A CE1 
1827 N NE2 . HIS A 399 ? 0.5144 0.4163 0.4584 -0.0753 0.0468  0.0306  399 HIS A NE2 
1828 N N   . SER A 400 ? 0.3090 0.2642 0.3097 -0.0919 0.0337  -0.0076 400 SER A N   
1829 C CA  . SER A 400 ? 0.2921 0.2533 0.3002 -0.0952 0.0313  -0.0145 400 SER A CA  
1830 C C   . SER A 400 ? 0.2728 0.2548 0.2904 -0.0884 0.0270  -0.0177 400 SER A C   
1831 O O   . SER A 400 ? 0.2820 0.2681 0.2988 -0.0805 0.0256  -0.0150 400 SER A O   
1832 C CB  . SER A 400 ? 0.3204 0.2621 0.3223 -0.0908 0.0295  -0.0155 400 SER A CB  
1833 O OG  . SER A 400 ? 0.3367 0.2827 0.3438 -0.0952 0.0276  -0.0226 400 SER A OG  
1834 N N   . GLN A 401 ? 0.2588 0.2522 0.2841 -0.0907 0.0247  -0.0236 401 GLN A N   
1835 C CA  . GLN A 401 ? 0.2513 0.2605 0.2836 -0.0828 0.0208  -0.0260 401 GLN A CA  
1836 C C   . GLN A 401 ? 0.2589 0.2578 0.2870 -0.0733 0.0179  -0.0243 401 GLN A C   
1837 O O   . GLN A 401 ? 0.2767 0.2592 0.2987 -0.0727 0.0179  -0.0234 401 GLN A O   
1838 C CB  . GLN A 401 ? 0.2813 0.3030 0.3206 -0.0858 0.0186  -0.0319 401 GLN A CB  
1839 C CG  . GLN A 401 ? 0.3489 0.3572 0.3845 -0.0898 0.0177  -0.0353 401 GLN A CG  
1840 C CD  . GLN A 401 ? 0.4381 0.4613 0.4801 -0.0922 0.0148  -0.0415 401 GLN A CD  
1841 O OE1 . GLN A 401 ? 0.4710 0.4866 0.5103 -0.0905 0.0126  -0.0447 401 GLN A OE1 
1842 N NE2 . GLN A 401 ? 0.4162 0.4621 0.4663 -0.0952 0.0147  -0.0434 401 GLN A NE2 
1843 N N   . VAL A 402 ? 0.2359 0.2437 0.2666 -0.0662 0.0158  -0.0239 402 VAL A N   
1844 C CA  . VAL A 402 ? 0.2363 0.2375 0.2639 -0.0587 0.0132  -0.0226 402 VAL A CA  
1845 C C   . VAL A 402 ? 0.2486 0.2583 0.2814 -0.0552 0.0104  -0.0261 402 VAL A C   
1846 O O   . VAL A 402 ? 0.2568 0.2763 0.2925 -0.0523 0.0099  -0.0267 402 VAL A O   
1847 C CB  . VAL A 402 ? 0.2401 0.2434 0.2649 -0.0547 0.0134  -0.0194 402 VAL A CB  
1848 C CG1 . VAL A 402 ? 0.2481 0.2471 0.2704 -0.0486 0.0107  -0.0183 402 VAL A CG1 
1849 C CG2 . VAL A 402 ? 0.2473 0.2455 0.2668 -0.0580 0.0166  -0.0155 402 VAL A CG2 
1850 N N   . CYS A 403 ? 0.2411 0.2463 0.2739 -0.0550 0.0089  -0.0285 403 CYS A N   
1851 C CA  . CYS A 403 ? 0.2358 0.2490 0.2723 -0.0519 0.0065  -0.0314 403 CYS A CA  
1852 C C   . CYS A 403 ? 0.2438 0.2566 0.2793 -0.0455 0.0050  -0.0297 403 CYS A C   
1853 O O   . CYS A 403 ? 0.2613 0.2813 0.2990 -0.0426 0.0040  -0.0306 403 CYS A O   
1854 C CB  . CYS A 403 ? 0.2535 0.2622 0.2891 -0.0541 0.0057  -0.0349 403 CYS A CB  
1855 S SG  . CYS A 403 ? 0.3199 0.3124 0.3491 -0.0499 0.0056  -0.0336 403 CYS A SG  
1856 N N   A SER A 404 ? 0.2336 0.2385 0.2654 -0.0433 0.0050  -0.0272 404 SER A N   
1857 N N   B SER A 404 ? 0.2306 0.2355 0.2625 -0.0433 0.0050  -0.0272 404 SER A N   
1858 C CA  A SER A 404 ? 0.2317 0.2380 0.2632 -0.0389 0.0036  -0.0261 404 SER A CA  
1859 C CA  B SER A 404 ? 0.2265 0.2327 0.2579 -0.0389 0.0036  -0.0260 404 SER A CA  
1860 C C   A SER A 404 ? 0.2256 0.2284 0.2538 -0.0374 0.0036  -0.0230 404 SER A C   
1861 C C   B SER A 404 ? 0.2215 0.2244 0.2497 -0.0375 0.0036  -0.0229 404 SER A C   
1862 O O   A SER A 404 ? 0.2304 0.2265 0.2553 -0.0378 0.0045  -0.0211 404 SER A O   
1863 O O   B SER A 404 ? 0.2246 0.2209 0.2495 -0.0381 0.0046  -0.0210 404 SER A O   
1864 C CB  A SER A 404 ? 0.2529 0.2579 0.2846 -0.0365 0.0025  -0.0276 404 SER A CB  
1865 C CB  B SER A 404 ? 0.2430 0.2475 0.2744 -0.0362 0.0025  -0.0273 404 SER A CB  
1866 O OG  A SER A 404 ? 0.2735 0.2820 0.3056 -0.0334 0.0016  -0.0267 404 SER A OG  
1867 O OG  B SER A 404 ? 0.2531 0.2629 0.2868 -0.0360 0.0019  -0.0299 404 SER A OG  
1868 N N   . ILE A 405 ? 0.2159 0.2230 0.2441 -0.0358 0.0026  -0.0224 405 ILE A N   
1869 C CA  . ILE A 405 ? 0.2168 0.2248 0.2423 -0.0343 0.0017  -0.0200 405 ILE A CA  
1870 C C   . ILE A 405 ? 0.2061 0.2198 0.2334 -0.0329 0.0002  -0.0207 405 ILE A C   
1871 O O   . ILE A 405 ? 0.2081 0.2238 0.2370 -0.0343 0.0004  -0.0224 405 ILE A O   
1872 C CB  . ILE A 405 ? 0.2318 0.2418 0.2547 -0.0363 0.0023  -0.0196 405 ILE A CB  
1873 C CG1 . ILE A 405 ? 0.2372 0.2436 0.2582 -0.0382 0.0044  -0.0184 405 ILE A CG1 
1874 C CG2 . ILE A 405 ? 0.2407 0.2544 0.2606 -0.0351 0.0006  -0.0180 405 ILE A CG2 
1875 C CD1 . ILE A 405 ? 0.2585 0.2682 0.2774 -0.0397 0.0056  -0.0191 405 ILE A CD1 
1876 N N   . LEU A 406 ? 0.1973 0.2139 0.2240 -0.0298 -0.0010 -0.0189 406 LEU A N   
1877 C CA  . LEU A 406 ? 0.1891 0.2150 0.2183 -0.0294 -0.0023 -0.0193 406 LEU A CA  
1878 C C   . LEU A 406 ? 0.1895 0.2227 0.2169 -0.0283 -0.0041 -0.0174 406 LEU A C   
1879 O O   . LEU A 406 ? 0.2060 0.2358 0.2299 -0.0250 -0.0043 -0.0147 406 LEU A O   
1880 C CB  . LEU A 406 ? 0.2006 0.2281 0.2320 -0.0249 -0.0022 -0.0192 406 LEU A CB  
1881 C CG  . LEU A 406 ? 0.2408 0.2632 0.2732 -0.0255 -0.0009 -0.0214 406 LEU A CG  
1882 C CD1 . LEU A 406 ? 0.2404 0.2630 0.2730 -0.0205 -0.0006 -0.0217 406 LEU A CD1 
1883 C CD2 . LEU A 406 ? 0.2604 0.2864 0.2945 -0.0292 -0.0005 -0.0227 406 LEU A CD2 
1884 N N   . TRP A 407 ? 0.1718 0.2155 0.2011 -0.0313 -0.0054 -0.0186 407 TRP A N   
1885 C CA  . TRP A 407 ? 0.1818 0.2369 0.2102 -0.0304 -0.0078 -0.0174 407 TRP A CA  
1886 C C   . TRP A 407 ? 0.1888 0.2573 0.2219 -0.0267 -0.0089 -0.0166 407 TRP A C   
1887 O O   . TRP A 407 ? 0.1877 0.2592 0.2247 -0.0293 -0.0078 -0.0183 407 TRP A O   
1888 C CB  . TRP A 407 ? 0.1814 0.2416 0.2085 -0.0381 -0.0086 -0.0205 407 TRP A CB  
1889 C CG  . TRP A 407 ? 0.2019 0.2510 0.2239 -0.0411 -0.0072 -0.0219 407 TRP A CG  
1890 C CD1 . TRP A 407 ? 0.2183 0.2560 0.2397 -0.0427 -0.0046 -0.0234 407 TRP A CD1 
1891 C CD2 . TRP A 407 ? 0.2057 0.2561 0.2222 -0.0423 -0.0082 -0.0222 407 TRP A CD2 
1892 N NE1 . TRP A 407 ? 0.2271 0.2593 0.2435 -0.0446 -0.0037 -0.0247 407 TRP A NE1 
1893 C CE2 . TRP A 407 ? 0.2154 0.2544 0.2283 -0.0446 -0.0057 -0.0241 407 TRP A CE2 
1894 C CE3 . TRP A 407 ? 0.2190 0.2805 0.2328 -0.0411 -0.0110 -0.0210 407 TRP A CE3 
1895 C CZ2 . TRP A 407 ? 0.2331 0.2706 0.2397 -0.0459 -0.0055 -0.0251 407 TRP A CZ2 
1896 C CZ3 . TRP A 407 ? 0.2395 0.2992 0.2464 -0.0428 -0.0111 -0.0218 407 TRP A CZ3 
1897 C CH2 . TRP A 407 ? 0.2427 0.2901 0.2461 -0.0453 -0.0081 -0.0240 407 TRP A CH2 
1898 N N   . SER A 408 ? 0.1909 0.2687 0.2231 -0.0205 -0.0109 -0.0137 408 SER A N   
1899 C CA  . SER A 408 ? 0.2063 0.3015 0.2437 -0.0163 -0.0121 -0.0131 408 SER A CA  
1900 C C   . SER A 408 ? 0.2562 0.3684 0.2970 -0.0246 -0.0140 -0.0158 408 SER A C   
1901 O O   . SER A 408 ? 0.2740 0.3906 0.3115 -0.0275 -0.0161 -0.0162 408 SER A O   
1902 C CB  . SER A 408 ? 0.2005 0.3010 0.2351 -0.0053 -0.0136 -0.0087 408 SER A CB  
1903 O OG  . SER A 408 ? 0.1994 0.3227 0.2398 -0.0013 -0.0153 -0.0083 408 SER A OG  
1904 N N   . PRO A 409 ? 0.2746 0.3972 0.3213 -0.0289 -0.0130 -0.0179 409 PRO A N   
1905 C CA  . PRO A 409 ? 0.2828 0.4218 0.3325 -0.0388 -0.0144 -0.0209 409 PRO A CA  
1906 C C   . PRO A 409 ? 0.2812 0.4473 0.3351 -0.0350 -0.0179 -0.0197 409 PRO A C   
1907 O O   . PRO A 409 ? 0.3011 0.4849 0.3588 -0.0442 -0.0192 -0.0227 409 PRO A O   
1908 C CB  . PRO A 409 ? 0.3006 0.4397 0.3545 -0.0444 -0.0113 -0.0225 409 PRO A CB  
1909 C CG  . PRO A 409 ? 0.3102 0.4477 0.3662 -0.0334 -0.0099 -0.0197 409 PRO A CG  
1910 C CD  . PRO A 409 ? 0.2860 0.4063 0.3362 -0.0256 -0.0104 -0.0176 409 PRO A CD  
1911 N N   . HIS A 410 ? 0.2394 0.4094 0.2924 -0.0216 -0.0192 -0.0154 410 HIS A N   
1912 C CA  . HIS A 410 ? 0.2189 0.4162 0.2755 -0.0148 -0.0226 -0.0133 410 HIS A CA  
1913 C C   . HIS A 410 ? 0.2291 0.4239 0.2784 -0.0053 -0.0253 -0.0092 410 HIS A C   
1914 O O   . HIS A 410 ? 0.2344 0.4511 0.2843 -0.0048 -0.0293 -0.0089 410 HIS A O   
1915 C CB  . HIS A 410 ? 0.2161 0.4237 0.2783 -0.0045 -0.0210 -0.0111 410 HIS A CB  
1916 C CG  . HIS A 410 ? 0.2437 0.4561 0.3125 -0.0126 -0.0180 -0.0142 410 HIS A CG  
1917 N ND1 . HIS A 410 ? 0.2516 0.4875 0.3273 -0.0238 -0.0188 -0.0173 410 HIS A ND1 
1918 C CD2 . HIS A 410 ? 0.2792 0.4753 0.3476 -0.0116 -0.0140 -0.0145 410 HIS A CD2 
1919 C CE1 . HIS A 410 ? 0.2567 0.4891 0.3357 -0.0287 -0.0149 -0.0186 410 HIS A CE1 
1920 N NE2 . HIS A 410 ? 0.2885 0.4983 0.3633 -0.0209 -0.0122 -0.0170 410 HIS A NE2 
1921 N N   . TYR A 411 ? 0.2213 0.3904 0.2633 0.0019  -0.0232 -0.0059 411 TYR A N   
1922 C CA  . TYR A 411 ? 0.2401 0.4036 0.2735 0.0112  -0.0247 -0.0009 411 TYR A CA  
1923 C C   . TYR A 411 ? 0.2992 0.4522 0.3251 0.0047  -0.0256 -0.0014 411 TYR A C   
1924 O O   . TYR A 411 ? 0.3231 0.4718 0.3411 0.0127  -0.0265 0.0036  411 TYR A O   
1925 C CB  . TYR A 411 ? 0.2394 0.3796 0.2670 0.0221  -0.0214 0.0034  411 TYR A CB  
1926 C CG  . TYR A 411 ? 0.2517 0.4026 0.2814 0.0359  -0.0212 0.0065  411 TYR A CG  
1927 C CD1 . TYR A 411 ? 0.2730 0.4360 0.2984 0.0488  -0.0236 0.0120  411 TYR A CD1 
1928 C CD2 . TYR A 411 ? 0.2611 0.4110 0.2963 0.0369  -0.0186 0.0041  411 TYR A CD2 
1929 C CE1 . TYR A 411 ? 0.2824 0.4554 0.3090 0.0634  -0.0231 0.0150  411 TYR A CE1 
1930 C CE2 . TYR A 411 ? 0.2774 0.4387 0.3144 0.0503  -0.0180 0.0065  411 TYR A CE2 
1931 C CZ  . TYR A 411 ? 0.2918 0.4634 0.3243 0.0641  -0.0202 0.0120  411 TYR A CZ  
1932 O OH  . TYR A 411 ? 0.3395 0.5215 0.3729 0.0793  -0.0192 0.0144  411 TYR A OH  
1933 N N   . LYS A 412 ? 0.3076 0.4538 0.3345 -0.0081 -0.0247 -0.0066 412 LYS A N   
1934 C CA  . LYS A 412 ? 0.2990 0.4339 0.3178 -0.0130 -0.0247 -0.0072 412 LYS A CA  
1935 C C   . LYS A 412 ? 0.2604 0.3713 0.2723 -0.0065 -0.0215 -0.0025 412 LYS A C   
1936 O O   . LYS A 412 ? 0.2557 0.3626 0.2595 -0.0017 -0.0219 0.0017  412 LYS A O   
1937 C CB  . LYS A 412 ? 0.3486 0.5030 0.3634 -0.0129 -0.0292 -0.0069 412 LYS A CB  
1938 C CG  . LYS A 412 ? 0.4334 0.6080 0.4535 -0.0242 -0.0319 -0.0135 412 LYS A CG  
1939 C CD  . LYS A 412 ? 0.5169 0.7033 0.5304 -0.0286 -0.0355 -0.0159 412 LYS A CD  
1940 C CE  . LYS A 412 ? 0.5747 0.7762 0.5924 -0.0427 -0.0374 -0.0238 412 LYS A CE  
1941 N NZ  . LYS A 412 ? 0.6171 0.8273 0.6269 -0.0488 -0.0407 -0.0278 412 LYS A NZ  
1942 N N   . GLU A 413 ? 0.2322 0.3284 0.2470 -0.0063 -0.0182 -0.0030 413 GLU A N   
1943 C CA  . GLU A 413 ? 0.2184 0.2919 0.2279 -0.0028 -0.0148 0.0001  413 GLU A CA  
1944 C C   . GLU A 413 ? 0.2218 0.2825 0.2348 -0.0105 -0.0119 -0.0041 413 GLU A C   
1945 O O   . GLU A 413 ? 0.2226 0.2896 0.2418 -0.0155 -0.0121 -0.0082 413 GLU A O   
1946 C CB  . GLU A 413 ? 0.2327 0.3010 0.2407 0.0085  -0.0138 0.0044  413 GLU A CB  
1947 C CG  . GLU A 413 ? 0.2772 0.3546 0.2794 0.0192  -0.0160 0.0102  413 GLU A CG  
1948 C CD  . GLU A 413 ? 0.3183 0.3926 0.3188 0.0322  -0.0150 0.0141  413 GLU A CD  
1949 O OE1 . GLU A 413 ? 0.3134 0.3759 0.3164 0.0324  -0.0122 0.0119  413 GLU A OE1 
1950 O OE2 . GLU A 413 ? 0.3256 0.4092 0.3215 0.0429  -0.0169 0.0193  413 GLU A OE2 
1951 N N   . LEU A 414 ? 0.2159 0.2590 0.2246 -0.0111 -0.0090 -0.0028 414 LEU A N   
1952 C CA  . LEU A 414 ? 0.2342 0.2666 0.2460 -0.0168 -0.0064 -0.0062 414 LEU A CA  
1953 C C   . LEU A 414 ? 0.2279 0.2458 0.2377 -0.0127 -0.0040 -0.0043 414 LEU A C   
1954 O O   . LEU A 414 ? 0.2339 0.2445 0.2374 -0.0073 -0.0032 0.0001  414 LEU A O   
1955 C CB  . LEU A 414 ? 0.2678 0.2942 0.2764 -0.0226 -0.0048 -0.0072 414 LEU A CB  
1956 C CG  . LEU A 414 ? 0.3314 0.3667 0.3399 -0.0276 -0.0063 -0.0104 414 LEU A CG  
1957 C CD1 . LEU A 414 ? 0.3439 0.3858 0.3460 -0.0255 -0.0081 -0.0076 414 LEU A CD1 
1958 C CD2 . LEU A 414 ? 0.3580 0.3857 0.3661 -0.0326 -0.0036 -0.0131 414 LEU A CD2 
1959 N N   . ILE A 415 ? 0.2088 0.2214 0.2227 -0.0156 -0.0026 -0.0076 415 ILE A N   
1960 C CA  . ILE A 415 ? 0.2104 0.2084 0.2217 -0.0139 -0.0002 -0.0074 415 ILE A CA  
1961 C C   . ILE A 415 ? 0.2097 0.2025 0.2234 -0.0213 0.0015  -0.0107 415 ILE A C   
1962 O O   . ILE A 415 ? 0.2055 0.2059 0.2243 -0.0248 0.0007  -0.0139 415 ILE A O   
1963 C CB  . ILE A 415 ? 0.2219 0.2206 0.2349 -0.0079 -0.0004 -0.0083 415 ILE A CB  
1964 C CG1 . ILE A 415 ? 0.2355 0.2156 0.2429 -0.0060 0.0023  -0.0084 415 ILE A CG1 
1965 C CG2 . ILE A 415 ? 0.2239 0.2328 0.2441 -0.0112 -0.0012 -0.0125 415 ILE A CG2 
1966 C CD1 . ILE A 415 ? 0.2476 0.2270 0.2544 0.0023  0.0026  -0.0092 415 ILE A CD1 
1967 N N   . SER A 416 ? 0.2024 0.1827 0.2121 -0.0237 0.0040  -0.0099 416 SER A N   
1968 C CA  . SER A 416 ? 0.2038 0.1825 0.2163 -0.0309 0.0056  -0.0130 416 SER A CA  
1969 C C   . SER A 416 ? 0.2159 0.1830 0.2266 -0.0327 0.0073  -0.0150 416 SER A C   
1970 O O   . SER A 416 ? 0.2338 0.1886 0.2381 -0.0290 0.0085  -0.0129 416 SER A O   
1971 C CB  . SER A 416 ? 0.2109 0.1896 0.2210 -0.0350 0.0072  -0.0109 416 SER A CB  
1972 O OG  . SER A 416 ? 0.2389 0.2065 0.2411 -0.0334 0.0091  -0.0062 416 SER A OG  
1973 N N   . GLY A 417 ? 0.2150 0.1857 0.2303 -0.0379 0.0075  -0.0193 417 GLY A N   
1974 C CA  . GLY A 417 ? 0.2251 0.1869 0.2388 -0.0415 0.0088  -0.0228 417 GLY A CA  
1975 C C   . GLY A 417 ? 0.2395 0.2010 0.2539 -0.0503 0.0109  -0.0239 417 GLY A C   
1976 O O   . GLY A 417 ? 0.2312 0.2043 0.2501 -0.0526 0.0108  -0.0234 417 GLY A O   
1977 N N   . HIS A 418 ? 0.2392 0.1872 0.2487 -0.0552 0.0133  -0.0252 418 HIS A N   
1978 C CA  . HIS A 418 ? 0.2498 0.1970 0.2593 -0.0651 0.0161  -0.0257 418 HIS A CA  
1979 C C   . HIS A 418 ? 0.2725 0.2142 0.2813 -0.0736 0.0172  -0.0314 418 HIS A C   
1980 O O   . HIS A 418 ? 0.2862 0.2219 0.2929 -0.0711 0.0159  -0.0352 418 HIS A O   
1981 C CB  . HIS A 418 ? 0.2546 0.1875 0.2557 -0.0654 0.0195  -0.0195 418 HIS A CB  
1982 C CG  . HIS A 418 ? 0.2577 0.1976 0.2588 -0.0579 0.0181  -0.0145 418 HIS A CG  
1983 N ND1 . HIS A 418 ? 0.2555 0.2110 0.2618 -0.0597 0.0179  -0.0138 418 HIS A ND1 
1984 C CD2 . HIS A 418 ? 0.2716 0.2073 0.2685 -0.0485 0.0165  -0.0110 418 HIS A CD2 
1985 C CE1 . HIS A 418 ? 0.2666 0.2249 0.2709 -0.0525 0.0161  -0.0104 418 HIS A CE1 
1986 N NE2 . HIS A 418 ? 0.2704 0.2185 0.2695 -0.0460 0.0152  -0.0084 418 HIS A NE2 
1987 N N   . GLY A 419 ? 0.2866 0.2329 0.2975 -0.0840 0.0195  -0.0324 419 GLY A N   
1988 C CA  . GLY A 419 ? 0.3093 0.2535 0.3202 -0.0950 0.0208  -0.0384 419 GLY A CA  
1989 C C   . GLY A 419 ? 0.3374 0.2619 0.3396 -0.1044 0.0260  -0.0363 419 GLY A C   
1990 O O   . GLY A 419 ? 0.3470 0.2495 0.3389 -0.0996 0.0283  -0.0314 419 GLY A O   
1991 N N   . PHE A 420 ? 0.3421 0.2751 0.3480 -0.1179 0.0282  -0.0395 420 PHE A N   
1992 C CA  . PHE A 420 ? 0.3750 0.2896 0.3726 -0.1300 0.0340  -0.0380 420 PHE A CA  
1993 C C   . PHE A 420 ? 0.3846 0.2881 0.3755 -0.1251 0.0374  -0.0285 420 PHE A C   
1994 O O   . PHE A 420 ? 0.3653 0.2870 0.3627 -0.1192 0.0360  -0.0249 420 PHE A O   
1995 C CB  . PHE A 420 ? 0.3821 0.3182 0.3888 -0.1450 0.0353  -0.0425 420 PHE A CB  
1996 C CG  . PHE A 420 ? 0.4288 0.3482 0.4278 -0.1609 0.0417  -0.0420 420 PHE A CG  
1997 C CD1 . PHE A 420 ? 0.4531 0.3715 0.4499 -0.1645 0.0466  -0.0348 420 PHE A CD1 
1998 C CD2 . PHE A 420 ? 0.4591 0.3625 0.4519 -0.1728 0.0432  -0.0488 420 PHE A CD2 
1999 C CE1 . PHE A 420 ? 0.4752 0.3773 0.4641 -0.1801 0.0532  -0.0337 420 PHE A CE1 
2000 C CE2 . PHE A 420 ? 0.4866 0.3723 0.4712 -0.1890 0.0498  -0.0484 420 PHE A CE2 
2001 C CZ  . PHE A 420 ? 0.4873 0.3720 0.4700 -0.1925 0.0549  -0.0404 420 PHE A CZ  
2002 N N   . ALA A 421 ? 0.4133 0.2863 0.3900 -0.1263 0.0419  -0.0243 421 ALA A N   
2003 C CA  . ALA A 421 ? 0.4371 0.2837 0.4033 -0.1338 0.0446  -0.0287 421 ALA A CA  
2004 C C   . ALA A 421 ? 0.4463 0.2708 0.4029 -0.1207 0.0431  -0.0286 421 ALA A C   
2005 O O   . ALA A 421 ? 0.4614 0.2663 0.4102 -0.1252 0.0445  -0.0343 421 ALA A O   
2006 C CB  . ALA A 421 ? 0.4552 0.2788 0.4097 -0.1451 0.0520  -0.0240 421 ALA A CB  
2007 N N   . GLN A 422 ? 0.4273 0.2555 0.3840 -0.1049 0.0404  -0.0227 422 GLN A N   
2008 C CA  . GLN A 422 ? 0.4368 0.2461 0.3844 -0.0914 0.0395  -0.0215 422 GLN A CA  
2009 C C   . GLN A 422 ? 0.4089 0.2335 0.3646 -0.0828 0.0340  -0.0272 422 GLN A C   
2010 O O   . GLN A 422 ? 0.4123 0.2212 0.3602 -0.0732 0.0340  -0.0277 422 GLN A O   
2011 C CB  . GLN A 422 ? 0.4779 0.2809 0.4190 -0.0789 0.0403  -0.0114 422 GLN A CB  
2012 C CG  . GLN A 422 ? 0.5787 0.3600 0.5073 -0.0851 0.0466  -0.0043 422 GLN A CG  
2013 C CD  . GLN A 422 ? 0.7257 0.4710 0.6388 -0.0908 0.0520  -0.0060 422 GLN A CD  
2014 O OE1 . GLN A 422 ? 0.7775 0.5042 0.6821 -0.0811 0.0519  -0.0076 422 GLN A OE1 
2015 N NE2 . GLN A 422 ? 0.7642 0.4984 0.6727 -0.1072 0.0575  -0.0060 422 GLN A NE2 
2016 N N   . ASN A 423 ? 0.3667 0.2211 0.3368 -0.0849 0.0298  -0.0307 423 ASN A N   
2017 C CA  . ASN A 423 ? 0.3352 0.2048 0.3125 -0.0776 0.0249  -0.0355 423 ASN A CA  
2018 C C   . ASN A 423 ? 0.3422 0.2080 0.3163 -0.0620 0.0235  -0.0309 423 ASN A C   
2019 O O   . ASN A 423 ? 0.3618 0.2235 0.3337 -0.0552 0.0222  -0.0343 423 ASN A O   
2020 C CB  . ASN A 423 ? 0.3432 0.2039 0.3170 -0.0836 0.0251  -0.0442 423 ASN A CB  
2021 C CG  . ASN A 423 ? 0.3638 0.2308 0.3411 -0.1000 0.0263  -0.0493 423 ASN A CG  
2022 O OD1 . ASN A 423 ? 0.3458 0.2374 0.3342 -0.1043 0.0245  -0.0491 423 ASN A OD1 
2023 N ND2 . ASN A 423 ? 0.3991 0.2448 0.3668 -0.1095 0.0295  -0.0544 423 ASN A ND2 
2024 N N   . GLN A 424 ? 0.3260 0.1938 0.2993 -0.0567 0.0238  -0.0234 424 GLN A N   
2025 C CA  . GLN A 424 ? 0.3276 0.1934 0.2975 -0.0427 0.0225  -0.0185 424 GLN A CA  
2026 C C   . GLN A 424 ? 0.3078 0.1990 0.2882 -0.0373 0.0183  -0.0170 424 GLN A C   
2027 O O   . GLN A 424 ? 0.2986 0.2066 0.2876 -0.0434 0.0168  -0.0185 424 GLN A O   
2028 C CB  . GLN A 424 ? 0.3535 0.1997 0.3115 -0.0396 0.0262  -0.0107 424 GLN A CB  
2029 C CG  . GLN A 424 ? 0.3768 0.2354 0.3374 -0.0400 0.0259  -0.0044 424 GLN A CG  
2030 C CD  . GLN A 424 ? 0.4320 0.2961 0.3963 -0.0535 0.0280  -0.0052 424 GLN A CD  
2031 O OE1 . GLN A 424 ? 0.4354 0.3057 0.4061 -0.0631 0.0279  -0.0116 424 GLN A OE1 
2032 N NE2 . GLN A 424 ? 0.4522 0.3161 0.4125 -0.0541 0.0300  0.0013  424 GLN A NE2 
2033 N N   . LEU A 425 ? 0.2793 0.1734 0.2585 -0.0255 0.0166  -0.0142 425 LEU A N   
2034 C CA  . LEU A 425 ? 0.2706 0.1862 0.2577 -0.0212 0.0131  -0.0120 425 LEU A CA  
2035 C C   . LEU A 425 ? 0.2768 0.1886 0.2575 -0.0160 0.0138  -0.0046 425 LEU A C   
2036 O O   . LEU A 425 ? 0.2912 0.1857 0.2616 -0.0098 0.0161  -0.0008 425 LEU A O   
2037 C CB  . LEU A 425 ? 0.2660 0.1921 0.2572 -0.0128 0.0106  -0.0139 425 LEU A CB  
2038 C CG  . LEU A 425 ? 0.2998 0.2328 0.2970 -0.0166 0.0095  -0.0206 425 LEU A CG  
2039 C CD1 . LEU A 425 ? 0.3217 0.2368 0.3121 -0.0183 0.0119  -0.0247 425 LEU A CD1 
2040 C CD2 . LEU A 425 ? 0.3028 0.2497 0.3045 -0.0088 0.0075  -0.0210 425 LEU A CD2 
2041 N N   . VAL A 426 ? 0.2503 0.1772 0.2356 -0.0179 0.0120  -0.0025 426 VAL A N   
2042 C CA  . VAL A 426 ? 0.2548 0.1814 0.2338 -0.0129 0.0121  0.0041  426 VAL A CA  
2043 C C   . VAL A 426 ? 0.2497 0.1970 0.2343 -0.0072 0.0079  0.0046  426 VAL A C   
2044 O O   . VAL A 426 ? 0.2380 0.2000 0.2312 -0.0119 0.0058  0.0006  426 VAL A O   
2045 C CB  . VAL A 426 ? 0.2721 0.1974 0.2491 -0.0210 0.0143  0.0063  426 VAL A CB  
2046 C CG1 . VAL A 426 ? 0.2769 0.2030 0.2462 -0.0151 0.0141  0.0133  426 VAL A CG1 
2047 C CG2 . VAL A 426 ? 0.2781 0.1845 0.2500 -0.0290 0.0188  0.0056  426 VAL A CG2 
2048 N N   . ILE A 427 ? 0.2536 0.2025 0.2332 0.0030  0.0067  0.0094  427 ILE A N   
2049 C CA  . ILE A 427 ? 0.2520 0.2228 0.2366 0.0072  0.0026  0.0098  427 ILE A CA  
2050 C C   . ILE A 427 ? 0.2553 0.2309 0.2347 0.0069  0.0018  0.0143  427 ILE A C   
2051 O O   . ILE A 427 ? 0.2670 0.2297 0.2363 0.0111  0.0040  0.0201  427 ILE A O   
2052 C CB  . ILE A 427 ? 0.2658 0.2417 0.2497 0.0191  0.0012  0.0116  427 ILE A CB  
2053 C CG1 . ILE A 427 ? 0.2841 0.2558 0.2727 0.0188  0.0023  0.0064  427 ILE A CG1 
2054 C CG2 . ILE A 427 ? 0.2646 0.2667 0.2545 0.0217  -0.0032 0.0118  427 ILE A CG2 
2055 C CD1 . ILE A 427 ? 0.3045 0.2794 0.2917 0.0313  0.0020  0.0077  427 ILE A CD1 
2056 N N   . TRP A 428 ? 0.2384 0.2312 0.2236 0.0018  -0.0008 0.0115  428 TRP A N   
2057 C CA  . TRP A 428 ? 0.2404 0.2397 0.2205 0.0007  -0.0018 0.0144  428 TRP A CA  
2058 C C   . TRP A 428 ? 0.2544 0.2758 0.2373 0.0043  -0.0065 0.0139  428 TRP A C   
2059 O O   . TRP A 428 ? 0.2482 0.2817 0.2396 0.0015  -0.0086 0.0089  428 TRP A O   
2060 C CB  . TRP A 428 ? 0.2365 0.2368 0.2199 -0.0096 -0.0005 0.0102  428 TRP A CB  
2061 C CG  . TRP A 428 ? 0.2375 0.2229 0.2217 -0.0154 0.0036  0.0087  428 TRP A CG  
2062 C CD1 . TRP A 428 ? 0.2470 0.2302 0.2384 -0.0190 0.0041  0.0039  428 TRP A CD1 
2063 C CD2 . TRP A 428 ? 0.2560 0.2294 0.2339 -0.0194 0.0076  0.0118  428 TRP A CD2 
2064 N NE1 . TRP A 428 ? 0.2565 0.2287 0.2471 -0.0249 0.0077  0.0034  428 TRP A NE1 
2065 C CE2 . TRP A 428 ? 0.2641 0.2300 0.2467 -0.0258 0.0102  0.0082  428 TRP A CE2 
2066 C CE3 . TRP A 428 ? 0.2786 0.2483 0.2471 -0.0186 0.0095  0.0174  428 TRP A CE3 
2067 C CZ2 . TRP A 428 ? 0.2954 0.2519 0.2749 -0.0324 0.0145  0.0094  428 TRP A CZ2 
2068 C CZ3 . TRP A 428 ? 0.3014 0.2592 0.2657 -0.0247 0.0144  0.0195  428 TRP A CZ3 
2069 C CH2 . TRP A 428 ? 0.3050 0.2567 0.2752 -0.0319 0.0169  0.0154  428 TRP A CH2 
2070 N N   . LYS A 429 ? 0.2720 0.2995 0.2473 0.0090  -0.0081 0.0186  429 LYS A N   
2071 C CA  . LYS A 429 ? 0.2778 0.3291 0.2553 0.0113  -0.0130 0.0176  429 LYS A CA  
2072 C C   . LYS A 429 ? 0.2886 0.3477 0.2674 0.0010  -0.0140 0.0123  429 LYS A C   
2073 O O   . LYS A 429 ? 0.3046 0.3539 0.2773 -0.0024 -0.0115 0.0135  429 LYS A O   
2074 C CB  . LYS A 429 ? 0.3162 0.3719 0.2837 0.0219  -0.0146 0.0252  429 LYS A CB  
2075 C CG  . LYS A 429 ? 0.3855 0.4699 0.3558 0.0250  -0.0204 0.0241  429 LYS A CG  
2076 C CD  . LYS A 429 ? 0.4633 0.5623 0.4439 0.0283  -0.0226 0.0214  429 LYS A CD  
2077 C CE  . LYS A 429 ? 0.5099 0.6390 0.4965 0.0239  -0.0279 0.0169  429 LYS A CE  
2078 N NZ  . LYS A 429 ? 0.5254 0.6707 0.5237 0.0235  -0.0293 0.0131  429 LYS A NZ  
2079 N N   . TYR A 430 ? 0.2757 0.3512 0.2617 -0.0041 -0.0171 0.0065  430 TYR A N   
2080 C CA  . TYR A 430 ? 0.2725 0.3533 0.2581 -0.0135 -0.0179 0.0008  430 TYR A CA  
2081 C C   . TYR A 430 ? 0.2654 0.3678 0.2478 -0.0128 -0.0228 0.0001  430 TYR A C   
2082 O O   . TYR A 430 ? 0.2592 0.3782 0.2458 -0.0082 -0.0261 0.0012  430 TYR A O   
2083 C CB  . TYR A 430 ? 0.2731 0.3532 0.2675 -0.0211 -0.0171 -0.0057 430 TYR A CB  
2084 C CG  . TYR A 430 ? 0.3007 0.3805 0.2933 -0.0303 -0.0168 -0.0119 430 TYR A CG  
2085 C CD1 . TYR A 430 ? 0.3289 0.3937 0.3185 -0.0333 -0.0130 -0.0130 430 TYR A CD1 
2086 C CD2 . TYR A 430 ? 0.3210 0.4157 0.3140 -0.0359 -0.0201 -0.0167 430 TYR A CD2 
2087 C CE1 . TYR A 430 ? 0.3583 0.4214 0.3448 -0.0399 -0.0122 -0.0187 430 TYR A CE1 
2088 C CE2 . TYR A 430 ? 0.3493 0.4402 0.3384 -0.0442 -0.0193 -0.0229 430 TYR A CE2 
2089 C CZ  . TYR A 430 ? 0.3727 0.4468 0.3583 -0.0453 -0.0152 -0.0238 430 TYR A CZ  
2090 O OH  . TYR A 430 ? 0.4273 0.4965 0.4078 -0.0518 -0.0140 -0.0299 430 TYR A OH  
2091 N N   . PRO A 431 ? 0.2720 0.3770 0.2465 -0.0164 -0.0234 -0.0013 431 PRO A N   
2092 C CA  . PRO A 431 ? 0.2770 0.3671 0.2462 -0.0218 -0.0195 -0.0033 431 PRO A CA  
2093 C C   . PRO A 431 ? 0.2913 0.3696 0.2515 -0.0168 -0.0163 0.0035  431 PRO A C   
2094 O O   . PRO A 431 ? 0.2986 0.3669 0.2554 -0.0212 -0.0126 0.0019  431 PRO A O   
2095 C CB  . PRO A 431 ? 0.2804 0.3829 0.2456 -0.0287 -0.0223 -0.0100 431 PRO A CB  
2096 C CG  . PRO A 431 ? 0.2892 0.4133 0.2521 -0.0236 -0.0278 -0.0073 431 PRO A CG  
2097 C CD  . PRO A 431 ? 0.2641 0.3919 0.2354 -0.0167 -0.0287 -0.0031 431 PRO A CD  
2098 N N   . THR A 432 ? 0.2889 0.3670 0.2447 -0.0074 -0.0169 0.0115  432 THR A N   
2099 C CA  . THR A 432 ? 0.3095 0.3741 0.2549 -0.0034 -0.0131 0.0188  432 THR A CA  
2100 C C   . THR A 432 ? 0.3097 0.3534 0.2573 -0.0068 -0.0072 0.0198  432 THR A C   
2101 O O   . THR A 432 ? 0.3188 0.3522 0.2588 -0.0079 -0.0031 0.0238  432 THR A O   
2102 C CB  . THR A 432 ? 0.3620 0.4287 0.3005 0.0084  -0.0148 0.0276  432 THR A CB  
2103 O OG1 . THR A 432 ? 0.3788 0.4384 0.3238 0.0132  -0.0142 0.0291  432 THR A OG1 
2104 C CG2 . THR A 432 ? 0.3803 0.4719 0.3154 0.0127  -0.0210 0.0275  432 THR A CG2 
2105 N N   . MET A 433 ? 0.2912 0.3299 0.2490 -0.0090 -0.0067 0.0162  433 MET A N   
2106 C CA  . MET A 433 ? 0.3130 0.3343 0.2738 -0.0123 -0.0019 0.0165  433 MET A CA  
2107 C C   . MET A 433 ? 0.3429 0.3483 0.2954 -0.0066 0.0012  0.0247  433 MET A C   
2108 O O   . MET A 433 ? 0.3649 0.3557 0.3157 -0.0109 0.0060  0.0262  433 MET A O   
2109 C CB  . MET A 433 ? 0.3259 0.3443 0.2879 -0.0206 0.0014  0.0124  433 MET A CB  
2110 C CG  . MET A 433 ? 0.3671 0.3948 0.3365 -0.0256 -0.0006 0.0041  433 MET A CG  
2111 S SD  . MET A 433 ? 0.4426 0.4700 0.4236 -0.0261 -0.0023 0.0001  433 MET A SD  
2112 C CE  . MET A 433 ? 0.4093 0.4216 0.3932 -0.0282 0.0023  0.0014  433 MET A CE  
2113 N N   . ALA A 434 ? 0.3523 0.3607 0.2996 0.0032  -0.0013 0.0300  434 ALA A N   
2114 C CA  . ALA A 434 ? 0.3753 0.3656 0.3130 0.0105  0.0018  0.0382  434 ALA A CA  
2115 C C   . ALA A 434 ? 0.3820 0.3604 0.3260 0.0112  0.0032  0.0357  434 ALA A C   
2116 O O   . ALA A 434 ? 0.3668 0.3570 0.3207 0.0118  -0.0001 0.0305  434 ALA A O   
2117 C CB  . ALA A 434 ? 0.3826 0.3825 0.3126 0.0228  -0.0018 0.0444  434 ALA A CB  
2118 N N   . LYS A 435 ? 0.3986 0.3535 0.3361 0.0109  0.0082  0.0395  435 LYS A N   
2119 C CA  . LYS A 435 ? 0.4204 0.3617 0.3617 0.0111  0.0099  0.0367  435 LYS A CA  
2120 C C   . LYS A 435 ? 0.4347 0.3749 0.3713 0.0253  0.0080  0.0409  435 LYS A C   
2121 O O   . LYS A 435 ? 0.4549 0.3855 0.3789 0.0341  0.0094  0.0489  435 LYS A O   
2122 C CB  . LYS A 435 ? 0.4644 0.3802 0.3982 0.0046  0.0163  0.0391  435 LYS A CB  
2123 C CG  . LYS A 435 ? 0.5246 0.4267 0.4630 -0.0009 0.0186  0.0337  435 LYS A CG  
2124 C CD  . LYS A 435 ? 0.6101 0.4956 0.5439 -0.0124 0.0244  0.0345  435 LYS A CD  
2125 C CE  . LYS A 435 ? 0.6806 0.5571 0.6202 -0.0213 0.0264  0.0278  435 LYS A CE  
2126 N NZ  . LYS A 435 ? 0.7197 0.5875 0.6573 -0.0343 0.0316  0.0278  435 LYS A NZ  
2127 N N   . VAL A 436 ? 0.4230 0.3742 0.3693 0.0285  0.0051  0.0358  436 VAL A N   
2128 C CA  . VAL A 436 ? 0.4282 0.3835 0.3723 0.0427  0.0032  0.0388  436 VAL A CA  
2129 C C   . VAL A 436 ? 0.4263 0.3555 0.3643 0.0473  0.0075  0.0393  436 VAL A C   
2130 O O   . VAL A 436 ? 0.4408 0.3593 0.3685 0.0609  0.0087  0.0453  436 VAL A O   
2131 C CB  . VAL A 436 ? 0.4375 0.4210 0.3957 0.0425  -0.0018 0.0327  436 VAL A CB  
2132 C CG1 . VAL A 436 ? 0.4572 0.4475 0.4154 0.0567  -0.0032 0.0346  436 VAL A CG1 
2133 C CG2 . VAL A 436 ? 0.4373 0.4451 0.3991 0.0387  -0.0061 0.0320  436 VAL A CG2 
2134 N N   . ALA A 437 ? 0.4030 0.3226 0.3467 0.0369  0.0097  0.0327  437 ALA A N   
2135 C CA  . ALA A 437 ? 0.3983 0.2944 0.3370 0.0393  0.0135  0.0309  437 ALA A CA  
2136 C C   . ALA A 437 ? 0.3768 0.2634 0.3206 0.0245  0.0158  0.0239  437 ALA A C   
2137 O O   . ALA A 437 ? 0.3572 0.2600 0.3112 0.0146  0.0138  0.0198  437 ALA A O   
2138 C CB  . ALA A 437 ? 0.3952 0.3041 0.3396 0.0499  0.0109  0.0281  437 ALA A CB  
2139 N N   . GLU A 438 ? 0.3713 0.2323 0.3076 0.0235  0.0200  0.0221  438 GLU A N   
2140 C CA  . GLU A 438 ? 0.3719 0.2258 0.3128 0.0102  0.0218  0.0148  438 GLU A CA  
2141 C C   . GLU A 438 ? 0.3812 0.2256 0.3207 0.0154  0.0224  0.0097  438 GLU A C   
2142 O O   . GLU A 438 ? 0.4033 0.2274 0.3308 0.0256  0.0252  0.0128  438 GLU A O   
2143 C CB  . GLU A 438 ? 0.4186 0.2490 0.3499 0.0001  0.0269  0.0169  438 GLU A CB  
2144 C CG  . GLU A 438 ? 0.4890 0.3313 0.4230 -0.0070 0.0267  0.0205  438 GLU A CG  
2145 C CD  . GLU A 438 ? 0.6075 0.4301 0.5336 -0.0187 0.0323  0.0223  438 GLU A CD  
2146 O OE1 . GLU A 438 ? 0.6669 0.4669 0.5782 -0.0146 0.0364  0.0295  438 GLU A OE1 
2147 O OE2 . GLU A 438 ? 0.5973 0.4275 0.5317 -0.0319 0.0329  0.0168  438 GLU A OE2 
2148 N N   . LEU A 439 ? 0.3533 0.2120 0.3040 0.0097  0.0201  0.0022  439 LEU A N   
2149 C CA  . LEU A 439 ? 0.3615 0.2135 0.3113 0.0134  0.0208  -0.0036 439 LEU A CA  
2150 C C   . LEU A 439 ? 0.3733 0.2084 0.3201 0.0005  0.0236  -0.0098 439 LEU A C   
2151 O O   . LEU A 439 ? 0.3646 0.2134 0.3210 -0.0106 0.0219  -0.0142 439 LEU A O   
2152 C CB  . LEU A 439 ? 0.3508 0.2305 0.3138 0.0156  0.0166  -0.0074 439 LEU A CB  
2153 C CG  . LEU A 439 ? 0.3583 0.2593 0.3261 0.0256  0.0134  -0.0024 439 LEU A CG  
2154 C CD1 . LEU A 439 ? 0.3400 0.2667 0.3206 0.0243  0.0101  -0.0065 439 LEU A CD1 
2155 C CD2 . LEU A 439 ? 0.3858 0.2771 0.3440 0.0413  0.0149  0.0020  439 LEU A CD2 
2156 N N   . LYS A 440 ? 0.3917 0.1970 0.3246 0.0023  0.0279  -0.0103 440 LYS A N   
2157 C CA  . LYS A 440 ? 0.4100 0.1968 0.3380 -0.0110 0.0310  -0.0166 440 LYS A CA  
2158 C C   . LYS A 440 ? 0.4213 0.1990 0.3456 -0.0082 0.0315  -0.0247 440 LYS A C   
2159 O O   . LYS A 440 ? 0.4275 0.2020 0.3474 0.0063  0.0317  -0.0237 440 LYS A O   
2160 C CB  . LYS A 440 ? 0.4575 0.2126 0.3699 -0.0144 0.0366  -0.0116 440 LYS A CB  
2161 C CG  . LYS A 440 ? 0.5164 0.2817 0.4326 -0.0205 0.0366  -0.0048 440 LYS A CG  
2162 C CD  . LYS A 440 ? 0.6047 0.3391 0.5051 -0.0256 0.0428  0.0008  440 LYS A CD  
2163 C CE  . LYS A 440 ? 0.6681 0.4153 0.5718 -0.0294 0.0427  0.0082  440 LYS A CE  
2164 N NZ  . LYS A 440 ? 0.7214 0.4386 0.6083 -0.0324 0.0492  0.0155  440 LYS A NZ  
2165 N N   . GLY A 441 ? 0.4218 0.1966 0.3475 -0.0218 0.0319  -0.0327 441 GLY A N   
2166 C CA  . GLY A 441 ? 0.4400 0.2059 0.3610 -0.0207 0.0324  -0.0415 441 GLY A CA  
2167 C C   . GLY A 441 ? 0.4305 0.2109 0.3600 -0.0349 0.0300  -0.0502 441 GLY A C   
2168 O O   . GLY A 441 ? 0.4399 0.2051 0.3617 -0.0410 0.0317  -0.0583 441 GLY A O   
2169 N N   . HIS A 442 ? 0.4001 0.2101 0.3446 -0.0399 0.0260  -0.0488 442 HIS A N   
2170 C CA  . HIS A 442 ? 0.3919 0.2190 0.3449 -0.0521 0.0234  -0.0561 442 HIS A CA  
2171 C C   . HIS A 442 ? 0.4063 0.2180 0.3538 -0.0681 0.0265  -0.0596 442 HIS A C   
2172 O O   . HIS A 442 ? 0.4121 0.2121 0.3557 -0.0717 0.0296  -0.0538 442 HIS A O   
2173 C CB  . HIS A 442 ? 0.3640 0.2227 0.3324 -0.0528 0.0194  -0.0526 442 HIS A CB  
2174 C CG  . HIS A 442 ? 0.3343 0.2118 0.3095 -0.0423 0.0160  -0.0522 442 HIS A CG  
2175 N ND1 . HIS A 442 ? 0.3361 0.2199 0.3116 -0.0413 0.0144  -0.0590 442 HIS A ND1 
2176 C CD2 . HIS A 442 ? 0.3266 0.2188 0.3084 -0.0341 0.0142  -0.0461 442 HIS A CD2 
2177 C CE1 . HIS A 442 ? 0.3346 0.2362 0.3169 -0.0325 0.0121  -0.0560 442 HIS A CE1 
2178 N NE2 . HIS A 442 ? 0.3222 0.2288 0.3084 -0.0283 0.0119  -0.0486 442 HIS A NE2 
2179 N N   . THR A 443 ? 0.4167 0.2294 0.3634 -0.0780 0.0258  -0.0691 443 THR A N   
2180 C CA  . THR A 443 ? 0.4359 0.2361 0.3778 -0.0954 0.0287  -0.0738 443 THR A CA  
2181 C C   . THR A 443 ? 0.4231 0.2535 0.3792 -0.1081 0.0257  -0.0762 443 THR A C   
2182 O O   . THR A 443 ? 0.4385 0.2648 0.3930 -0.1239 0.0278  -0.0803 443 THR A O   
2183 C CB  . THR A 443 ? 0.4790 0.2566 0.4081 -0.0997 0.0306  -0.0835 443 THR A CB  
2184 O OG1 . THR A 443 ? 0.4919 0.2924 0.4281 -0.0977 0.0258  -0.0905 443 THR A OG1 
2185 C CG2 . THR A 443 ? 0.5026 0.2475 0.4160 -0.0865 0.0347  -0.0809 443 THR A CG2 
2186 N N   . SER A 444 ? 0.4004 0.2606 0.3696 -0.1010 0.0211  -0.0734 444 SER A N   
2187 C CA  . SER A 444 ? 0.3846 0.2752 0.3675 -0.1082 0.0182  -0.0738 444 SER A CA  
2188 C C   . SER A 444 ? 0.3529 0.2605 0.3447 -0.0968 0.0162  -0.0655 444 SER A C   
2189 O O   . SER A 444 ? 0.3485 0.2479 0.3370 -0.0845 0.0162  -0.0609 444 SER A O   
2190 C CB  . SER A 444 ? 0.4140 0.3237 0.4016 -0.1129 0.0142  -0.0828 444 SER A CB  
2191 O OG  . SER A 444 ? 0.4816 0.3774 0.4613 -0.1265 0.0161  -0.0913 444 SER A OG  
2192 N N   . ARG A 445 ? 0.3206 0.2516 0.3231 -0.1009 0.0147  -0.0637 445 ARG A N   
2193 C CA  . ARG A 445 ? 0.3165 0.2605 0.3257 -0.0921 0.0135  -0.0565 445 ARG A CA  
2194 C C   . ARG A 445 ? 0.2970 0.2482 0.3084 -0.0793 0.0103  -0.0552 445 ARG A C   
2195 O O   . ARG A 445 ? 0.2933 0.2524 0.3059 -0.0777 0.0077  -0.0601 445 ARG A O   
2196 C CB  . ARG A 445 ? 0.3274 0.2959 0.3470 -0.0980 0.0126  -0.0563 445 ARG A CB  
2197 C CG  . ARG A 445 ? 0.3820 0.3731 0.4088 -0.0980 0.0086  -0.0617 445 ARG A CG  
2198 C CD  . ARG A 445 ? 0.4201 0.4363 0.4570 -0.0980 0.0075  -0.0596 445 ARG A CD  
2199 N NE  . ARG A 445 ? 0.4306 0.4697 0.4738 -0.0983 0.0038  -0.0645 445 ARG A NE  
2200 C CZ  . ARG A 445 ? 0.4431 0.5067 0.4949 -0.0978 0.0027  -0.0639 445 ARG A CZ  
2201 N NH1 . ARG A 445 ? 0.4095 0.4941 0.4659 -0.0967 -0.0009 -0.0679 445 ARG A NH1 
2202 N NH2 . ARG A 445 ? 0.4598 0.5279 0.5152 -0.0974 0.0052  -0.0591 445 ARG A NH2 
2203 N N   . VAL A 446 ? 0.2849 0.2333 0.2961 -0.0708 0.0107  -0.0485 446 VAL A N   
2204 C CA  . VAL A 446 ? 0.2776 0.2348 0.2918 -0.0604 0.0081  -0.0466 446 VAL A CA  
2205 C C   . VAL A 446 ? 0.2671 0.2468 0.2904 -0.0610 0.0057  -0.0468 446 VAL A C   
2206 O O   . VAL A 446 ? 0.2734 0.2611 0.3007 -0.0657 0.0064  -0.0454 446 VAL A O   
2207 C CB  . VAL A 446 ? 0.2741 0.2242 0.2857 -0.0530 0.0091  -0.0399 446 VAL A CB  
2208 C CG1 . VAL A 446 ? 0.2695 0.2305 0.2848 -0.0442 0.0067  -0.0382 446 VAL A CG1 
2209 C CG2 . VAL A 446 ? 0.2806 0.2078 0.2820 -0.0508 0.0118  -0.0389 446 VAL A CG2 
2210 N N   . LEU A 447 ? 0.2499 0.2389 0.2753 -0.0559 0.0033  -0.0485 447 LEU A N   
2211 C CA  . LEU A 447 ? 0.2440 0.2515 0.2756 -0.0541 0.0011  -0.0485 447 LEU A CA  
2212 C C   . LEU A 447 ? 0.2420 0.2527 0.2752 -0.0468 0.0008  -0.0435 447 LEU A C   
2213 O O   . LEU A 447 ? 0.2516 0.2709 0.2884 -0.0461 0.0007  -0.0412 447 LEU A O   
2214 C CB  . LEU A 447 ? 0.2483 0.2635 0.2794 -0.0538 -0.0011 -0.0536 447 LEU A CB  
2215 C CG  . LEU A 447 ? 0.2707 0.2879 0.3013 -0.0629 -0.0014 -0.0598 447 LEU A CG  
2216 C CD1 . LEU A 447 ? 0.2880 0.3111 0.3159 -0.0622 -0.0038 -0.0656 447 LEU A CD1 
2217 C CD2 . LEU A 447 ? 0.2736 0.3067 0.3111 -0.0681 -0.0017 -0.0595 447 LEU A CD2 
2218 N N   . SER A 448 ? 0.2297 0.2335 0.2598 -0.0415 0.0009  -0.0421 448 SER A N   
2219 C CA  . SER A 448 ? 0.2396 0.2475 0.2711 -0.0363 0.0006  -0.0381 448 SER A CA  
2220 C C   . SER A 448 ? 0.2263 0.2268 0.2550 -0.0322 0.0013  -0.0363 448 SER A C   
2221 O O   . SER A 448 ? 0.2336 0.2266 0.2586 -0.0309 0.0018  -0.0385 448 SER A O   
2222 C CB  . SER A 448 ? 0.2914 0.3079 0.3237 -0.0332 -0.0005 -0.0390 448 SER A CB  
2223 O OG  . SER A 448 ? 0.3838 0.4096 0.4186 -0.0344 -0.0014 -0.0396 448 SER A OG  
2224 N N   . LEU A 449 ? 0.2145 0.2179 0.2446 -0.0299 0.0013  -0.0326 449 LEU A N   
2225 C CA  . LEU A 449 ? 0.2074 0.2099 0.2363 -0.0253 0.0014  -0.0306 449 LEU A CA  
2226 C C   . LEU A 449 ? 0.2192 0.2315 0.2508 -0.0239 0.0010  -0.0295 449 LEU A C   
2227 O O   . LEU A 449 ? 0.2290 0.2451 0.2621 -0.0264 0.0009  -0.0287 449 LEU A O   
2228 C CB  . LEU A 449 ? 0.2071 0.2069 0.2350 -0.0249 0.0016  -0.0271 449 LEU A CB  
2229 C CG  . LEU A 449 ? 0.2367 0.2253 0.2607 -0.0270 0.0027  -0.0265 449 LEU A CG  
2230 C CD1 . LEU A 449 ? 0.2481 0.2354 0.2700 -0.0251 0.0028  -0.0222 449 LEU A CD1 
2231 C CD2 . LEU A 449 ? 0.2502 0.2276 0.2696 -0.0250 0.0039  -0.0287 449 LEU A CD2 
2232 N N   . THR A 450 ? 0.2009 0.2167 0.2324 -0.0199 0.0013  -0.0291 450 THR A N   
2233 C CA  . THR A 450 ? 0.1900 0.2157 0.2240 -0.0198 0.0016  -0.0275 450 THR A CA  
2234 C C   . THR A 450 ? 0.1997 0.2314 0.2349 -0.0156 0.0016  -0.0260 450 THR A C   
2235 O O   . THR A 450 ? 0.2095 0.2365 0.2424 -0.0106 0.0019  -0.0265 450 THR A O   
2236 C CB  . THR A 450 ? 0.2097 0.2387 0.2431 -0.0199 0.0023  -0.0288 450 THR A CB  
2237 O OG1 . THR A 450 ? 0.2147 0.2512 0.2497 -0.0216 0.0033  -0.0266 450 THR A OG1 
2238 C CG2 . THR A 450 ? 0.2069 0.2356 0.2382 -0.0154 0.0030  -0.0313 450 THR A CG2 
2239 N N   . MET A 451 ? 0.2018 0.2437 0.2400 -0.0177 0.0015  -0.0242 451 MET A N   
2240 C CA  . MET A 451 ? 0.1997 0.2526 0.2404 -0.0138 0.0012  -0.0227 451 MET A CA  
2241 C C   . MET A 451 ? 0.2037 0.2698 0.2475 -0.0133 0.0026  -0.0227 451 MET A C   
2242 O O   . MET A 451 ? 0.2008 0.2690 0.2453 -0.0190 0.0038  -0.0227 451 MET A O   
2243 C CB  . MET A 451 ? 0.2054 0.2630 0.2473 -0.0175 -0.0005 -0.0210 451 MET A CB  
2244 C CG  . MET A 451 ? 0.2282 0.3008 0.2731 -0.0135 -0.0016 -0.0193 451 MET A CG  
2245 S SD  . MET A 451 ? 0.2772 0.3557 0.3221 -0.0183 -0.0041 -0.0182 451 MET A SD  
2246 C CE  . MET A 451 ? 0.2858 0.3491 0.3247 -0.0122 -0.0047 -0.0162 451 MET A CE  
2247 N N   . SER A 452 ? 0.2024 0.2778 0.2478 -0.0062 0.0030  -0.0222 452 SER A N   
2248 C CA  . SER A 452 ? 0.2133 0.3048 0.2624 -0.0052 0.0049  -0.0221 452 SER A CA  
2249 C C   . SER A 452 ? 0.2267 0.3332 0.2810 -0.0132 0.0045  -0.0207 452 SER A C   
2250 O O   . SER A 452 ? 0.2124 0.3194 0.2673 -0.0165 0.0023  -0.0200 452 SER A O   
2251 C CB  . SER A 452 ? 0.2254 0.3244 0.2748 0.0058  0.0055  -0.0220 452 SER A CB  
2252 O OG  . SER A 452 ? 0.2306 0.3367 0.2820 0.0090  0.0033  -0.0198 452 SER A OG  
2253 N N   . PRO A 453 ? 0.2422 0.3611 0.2995 -0.0172 0.0070  -0.0205 453 PRO A N   
2254 C CA  . PRO A 453 ? 0.2528 0.3836 0.3139 -0.0274 0.0071  -0.0198 453 PRO A CA  
2255 C C   . PRO A 453 ? 0.2600 0.4107 0.3269 -0.0262 0.0048  -0.0193 453 PRO A C   
2256 O O   . PRO A 453 ? 0.2808 0.4375 0.3494 -0.0351 0.0035  -0.0198 453 PRO A O   
2257 C CB  . PRO A 453 ? 0.2594 0.3976 0.3213 -0.0315 0.0111  -0.0192 453 PRO A CB  
2258 C CG  . PRO A 453 ? 0.2614 0.4004 0.3221 -0.0207 0.0125  -0.0197 453 PRO A CG  
2259 C CD  . PRO A 453 ? 0.2429 0.3627 0.2986 -0.0143 0.0100  -0.0211 453 PRO A CD  
2260 N N   . ASP A 454 ? 0.2396 0.4002 0.3086 -0.0147 0.0042  -0.0187 454 ASP A N   
2261 C CA  . ASP A 454 ? 0.2360 0.4168 0.3099 -0.0110 0.0016  -0.0176 454 ASP A CA  
2262 C C   . ASP A 454 ? 0.2290 0.3983 0.2986 -0.0080 -0.0020 -0.0168 454 ASP A C   
2263 O O   . ASP A 454 ? 0.2453 0.4309 0.3178 -0.0062 -0.0048 -0.0157 454 ASP A O   
2264 C CB  . ASP A 454 ? 0.2596 0.4578 0.3370 0.0016  0.0027  -0.0167 454 ASP A CB  
2265 C CG  . ASP A 454 ? 0.3265 0.5064 0.3972 0.0148  0.0037  -0.0166 454 ASP A CG  
2266 O OD1 . ASP A 454 ? 0.3275 0.4819 0.3914 0.0134  0.0033  -0.0173 454 ASP A OD1 
2267 O OD2 . ASP A 454 ? 0.3763 0.5676 0.4482 0.0264  0.0051  -0.0161 454 ASP A OD2 
2268 N N   . GLY A 455 ? 0.2092 0.3529 0.2720 -0.0079 -0.0019 -0.0172 455 GLY A N   
2269 C CA  . GLY A 455 ? 0.2180 0.3492 0.2761 -0.0058 -0.0044 -0.0161 455 GLY A CA  
2270 C C   . GLY A 455 ? 0.2152 0.3400 0.2692 0.0075  -0.0047 -0.0139 455 GLY A C   
2271 O O   . GLY A 455 ? 0.2236 0.3368 0.2724 0.0097  -0.0061 -0.0122 455 GLY A O   
2272 N N   . ALA A 456 ? 0.2061 0.3364 0.2610 0.0167  -0.0027 -0.0138 456 ALA A N   
2273 C CA  . ALA A 456 ? 0.2151 0.3378 0.2645 0.0307  -0.0024 -0.0116 456 ALA A CA  
2274 C C   . ALA A 456 ? 0.2214 0.3142 0.2620 0.0331  -0.0005 -0.0127 456 ALA A C   
2275 O O   . ALA A 456 ? 0.2338 0.3129 0.2672 0.0413  -0.0004 -0.0104 456 ALA A O   
2276 C CB  . ALA A 456 ? 0.2265 0.3674 0.2797 0.0405  -0.0007 -0.0115 456 ALA A CB  
2277 N N   . THR A 457 ? 0.2105 0.2936 0.2509 0.0260  0.0011  -0.0161 457 THR A N   
2278 C CA  . THR A 457 ? 0.2166 0.2758 0.2497 0.0272  0.0029  -0.0184 457 THR A CA  
2279 C C   . THR A 457 ? 0.2140 0.2618 0.2466 0.0160  0.0023  -0.0202 457 THR A C   
2280 O O   . THR A 457 ? 0.2138 0.2706 0.2513 0.0080  0.0019  -0.0209 457 THR A O   
2281 C CB  . THR A 457 ? 0.2458 0.3071 0.2781 0.0325  0.0055  -0.0215 457 THR A CB  
2282 O OG1 . THR A 457 ? 0.2678 0.3430 0.3013 0.0442  0.0063  -0.0197 457 THR A OG1 
2283 C CG2 . THR A 457 ? 0.2621 0.2998 0.2860 0.0339  0.0073  -0.0249 457 THR A CG2 
2284 N N   . VAL A 458 ? 0.2029 0.2307 0.2291 0.0155  0.0028  -0.0207 458 VAL A N   
2285 C CA  . VAL A 458 ? 0.2011 0.2189 0.2267 0.0063  0.0025  -0.0226 458 VAL A CA  
2286 C C   . VAL A 458 ? 0.2267 0.2311 0.2476 0.0063  0.0042  -0.0267 458 VAL A C   
2287 O O   . VAL A 458 ? 0.2447 0.2351 0.2589 0.0116  0.0056  -0.0274 458 VAL A O   
2288 C CB  . VAL A 458 ? 0.2087 0.2172 0.2311 0.0039  0.0018  -0.0198 458 VAL A CB  
2289 C CG1 . VAL A 458 ? 0.2149 0.2132 0.2364 -0.0046 0.0022  -0.0220 458 VAL A CG1 
2290 C CG2 . VAL A 458 ? 0.2245 0.2476 0.2510 0.0027  -0.0002 -0.0167 458 VAL A CG2 
2291 N N   . ALA A 459 ? 0.2097 0.2172 0.2329 0.0005  0.0040  -0.0297 459 ALA A N   
2292 C CA  . ALA A 459 ? 0.2134 0.2106 0.2322 -0.0009 0.0049  -0.0343 459 ALA A CA  
2293 C C   . ALA A 459 ? 0.2191 0.2080 0.2373 -0.0087 0.0042  -0.0353 459 ALA A C   
2294 O O   . ALA A 459 ? 0.2132 0.2095 0.2359 -0.0135 0.0030  -0.0337 459 ALA A O   
2295 C CB  . ALA A 459 ? 0.2075 0.2155 0.2287 -0.0019 0.0049  -0.0365 459 ALA A CB  
2296 N N   . SER A 460 ? 0.2183 0.1920 0.2305 -0.0101 0.0052  -0.0380 460 SER A N   
2297 C CA  . SER A 460 ? 0.2274 0.1952 0.2394 -0.0185 0.0050  -0.0393 460 SER A CA  
2298 C C   . SER A 460 ? 0.2453 0.2113 0.2551 -0.0223 0.0049  -0.0456 460 SER A C   
2299 O O   . SER A 460 ? 0.2693 0.2247 0.2726 -0.0195 0.0062  -0.0493 460 SER A O   
2300 C CB  . SER A 460 ? 0.2523 0.2039 0.2586 -0.0190 0.0068  -0.0372 460 SER A CB  
2301 O OG  . SER A 460 ? 0.2772 0.2118 0.2747 -0.0143 0.0090  -0.0391 460 SER A OG  
2302 N N   . ALA A 461 ? 0.2464 0.2225 0.2607 -0.0282 0.0032  -0.0472 461 ALA A N   
2303 C CA  . ALA A 461 ? 0.2615 0.2397 0.2741 -0.0324 0.0024  -0.0533 461 ALA A CA  
2304 C C   . ALA A 461 ? 0.2665 0.2392 0.2789 -0.0414 0.0027  -0.0552 461 ALA A C   
2305 O O   . ALA A 461 ? 0.2505 0.2282 0.2676 -0.0441 0.0026  -0.0515 461 ALA A O   
2306 C CB  . ALA A 461 ? 0.2635 0.2592 0.2812 -0.0319 0.0003  -0.0527 461 ALA A CB  
2307 N N   . ALA A 462 ? 0.2700 0.2325 0.2767 -0.0465 0.0035  -0.0612 462 ALA A N   
2308 C CA  . ALA A 462 ? 0.2912 0.2479 0.2973 -0.0568 0.0045  -0.0633 462 ALA A CA  
2309 C C   . ALA A 462 ? 0.2966 0.2594 0.3019 -0.0651 0.0030  -0.0713 462 ALA A C   
2310 O O   . ALA A 462 ? 0.3061 0.2711 0.3080 -0.0622 0.0017  -0.0760 462 ALA A O   
2311 C CB  . ALA A 462 ? 0.3127 0.2445 0.3100 -0.0571 0.0081  -0.0620 462 ALA A CB  
2312 N N   . ALA A 463 ? 0.3026 0.2693 0.3107 -0.0758 0.0033  -0.0732 463 ALA A N   
2313 C CA  . ALA A 463 ? 0.3108 0.2862 0.3192 -0.0859 0.0017  -0.0813 463 ALA A CA  
2314 C C   . ALA A 463 ? 0.3364 0.2903 0.3332 -0.0911 0.0034  -0.0889 463 ALA A C   
2315 O O   . ALA A 463 ? 0.3451 0.3057 0.3406 -0.1001 0.0018  -0.0972 463 ALA A O   
2316 C CB  . ALA A 463 ? 0.3065 0.2923 0.3214 -0.0965 0.0023  -0.0807 463 ALA A CB  
2317 N N   . ASP A 464 ? 0.3428 0.2714 0.3306 -0.0850 0.0068  -0.0867 464 ASP A N   
2318 C CA  . ASP A 464 ? 0.3630 0.2679 0.3379 -0.0874 0.0090  -0.0938 464 ASP A CA  
2319 C C   . ASP A 464 ? 0.3641 0.2740 0.3355 -0.0780 0.0070  -0.0980 464 ASP A C   
2320 O O   . ASP A 464 ? 0.3863 0.2749 0.3460 -0.0754 0.0094  -0.1027 464 ASP A O   
2321 C CB  . ASP A 464 ? 0.3909 0.2652 0.3559 -0.0831 0.0139  -0.0892 464 ASP A CB  
2322 C CG  . ASP A 464 ? 0.4026 0.2777 0.3695 -0.0674 0.0141  -0.0807 464 ASP A CG  
2323 O OD1 . ASP A 464 ? 0.3965 0.2925 0.3709 -0.0601 0.0110  -0.0792 464 ASP A OD1 
2324 O OD2 . ASP A 464 ? 0.4100 0.2652 0.3705 -0.0628 0.0175  -0.0755 464 ASP A OD2 
2325 N N   . GLU A 465 ? 0.3424 0.2781 0.3229 -0.0716 0.0034  -0.0951 465 GLU A N   
2326 C CA  . GLU A 465 ? 0.3405 0.2849 0.3187 -0.0632 0.0017  -0.0977 465 GLU A CA  
2327 C C   . GLU A 465 ? 0.3533 0.2834 0.3258 -0.0507 0.0045  -0.0943 465 GLU A C   
2328 O O   . GLU A 465 ? 0.3665 0.2918 0.3313 -0.0455 0.0051  -0.0993 465 GLU A O   
2329 C CB  . GLU A 465 ? 0.3627 0.3079 0.3339 -0.0707 0.0001  -0.1089 465 GLU A CB  
2330 C CG  . GLU A 465 ? 0.4136 0.3804 0.3923 -0.0820 -0.0035 -0.1121 465 GLU A CG  
2331 C CD  . GLU A 465 ? 0.5373 0.5115 0.5102 -0.0893 -0.0062 -0.1233 465 GLU A CD  
2332 O OE1 . GLU A 465 ? 0.5982 0.5503 0.5593 -0.0939 -0.0039 -0.1312 465 GLU A OE1 
2333 O OE2 . GLU A 465 ? 0.5503 0.5520 0.5296 -0.0901 -0.0105 -0.1242 465 GLU A OE2 
2334 N N   . THR A 466 ? 0.3389 0.2644 0.3151 -0.0454 0.0062  -0.0859 466 THR A N   
2335 C CA  . THR A 466 ? 0.3329 0.2511 0.3059 -0.0327 0.0084  -0.0817 466 THR A CA  
2336 C C   . THR A 466 ? 0.3242 0.2588 0.3077 -0.0274 0.0072  -0.0727 466 THR A C   
2337 O O   . THR A 466 ? 0.3127 0.2546 0.3031 -0.0329 0.0059  -0.0688 466 THR A O   
2338 C CB  . THR A 466 ? 0.3682 0.2583 0.3315 -0.0301 0.0124  -0.0808 466 THR A CB  
2339 O OG1 . THR A 466 ? 0.3665 0.2532 0.3338 -0.0343 0.0129  -0.0744 466 THR A OG1 
2340 C CG2 . THR A 466 ? 0.3898 0.2571 0.3401 -0.0358 0.0146  -0.0900 466 THR A CG2 
2341 N N   . LEU A 467 ? 0.3250 0.2646 0.3089 -0.0168 0.0080  -0.0695 467 LEU A N   
2342 C CA  . LEU A 467 ? 0.3325 0.2845 0.3244 -0.0120 0.0074  -0.0617 467 LEU A CA  
2343 C C   . LEU A 467 ? 0.3299 0.2694 0.3169 -0.0031 0.0100  -0.0588 467 LEU A C   
2344 O O   . LEU A 467 ? 0.3452 0.2807 0.3265 0.0046  0.0118  -0.0615 467 LEU A O   
2345 C CB  . LEU A 467 ? 0.3428 0.3136 0.3390 -0.0077 0.0065  -0.0607 467 LEU A CB  
2346 C CG  . LEU A 467 ? 0.3980 0.3848 0.4025 -0.0121 0.0042  -0.0569 467 LEU A CG  
2347 C CD1 . LEU A 467 ? 0.4095 0.3993 0.4137 -0.0197 0.0022  -0.0614 467 LEU A CD1 
2348 C CD2 . LEU A 467 ? 0.4110 0.4126 0.4184 -0.0071 0.0045  -0.0542 467 LEU A CD2 
2349 N N   . ARG A 468 ? 0.3013 0.2350 0.2895 -0.0032 0.0104  -0.0534 468 ARG A N   
2350 C CA  . ARG A 468 ? 0.2990 0.2224 0.2821 0.0069  0.0126  -0.0496 468 ARG A CA  
2351 C C   . ARG A 468 ? 0.2827 0.2260 0.2743 0.0126  0.0112  -0.0434 468 ARG A C   
2352 O O   . ARG A 468 ? 0.2852 0.2394 0.2841 0.0067  0.0092  -0.0402 468 ARG A O   
2353 C CB  . ARG A 468 ? 0.3145 0.2173 0.2913 0.0035  0.0142  -0.0473 468 ARG A CB  
2354 C CG  . ARG A 468 ? 0.3674 0.2458 0.3328 -0.0014 0.0168  -0.0540 468 ARG A CG  
2355 C CD  . ARG A 468 ? 0.4480 0.3051 0.4065 -0.0066 0.0191  -0.0511 468 ARG A CD  
2356 N NE  . ARG A 468 ? 0.5636 0.3902 0.5070 -0.0043 0.0232  -0.0546 468 ARG A NE  
2357 C CZ  . ARG A 468 ? 0.5979 0.4095 0.5341 -0.0139 0.0246  -0.0627 468 ARG A CZ  
2358 N NH1 . ARG A 468 ? 0.6177 0.3980 0.5383 -0.0118 0.0290  -0.0657 468 ARG A NH1 
2359 N NH2 . ARG A 468 ? 0.5882 0.4160 0.5323 -0.0255 0.0218  -0.0680 468 ARG A NH2 
2360 N N   . LEU A 469 ? 0.2840 0.2332 0.2748 0.0237  0.0124  -0.0421 469 LEU A N   
2361 C CA  . LEU A 469 ? 0.2786 0.2498 0.2782 0.0276  0.0110  -0.0369 469 LEU A CA  
2362 C C   . LEU A 469 ? 0.2825 0.2491 0.2790 0.0364  0.0116  -0.0318 469 LEU A C   
2363 O O   . LEU A 469 ? 0.3043 0.2627 0.2939 0.0473  0.0139  -0.0322 469 LEU A O   
2364 C CB  . LEU A 469 ? 0.2758 0.2635 0.2786 0.0331  0.0118  -0.0386 469 LEU A CB  
2365 C CG  . LEU A 469 ? 0.3022 0.3040 0.3110 0.0252  0.0107  -0.0404 469 LEU A CG  
2366 C CD1 . LEU A 469 ? 0.3245 0.3146 0.3297 0.0165  0.0099  -0.0450 469 LEU A CD1 
2367 C CD2 . LEU A 469 ? 0.3179 0.3331 0.3274 0.0315  0.0126  -0.0420 469 LEU A CD2 
2368 N N   . TRP A 470 ? 0.2520 0.2233 0.2523 0.0326  0.0097  -0.0270 470 TRP A N   
2369 C CA  . TRP A 470 ? 0.2566 0.2234 0.2527 0.0408  0.0099  -0.0215 470 TRP A CA  
2370 C C   . TRP A 470 ? 0.2553 0.2483 0.2595 0.0461  0.0078  -0.0176 470 TRP A C   
2371 O O   . TRP A 470 ? 0.2483 0.2565 0.2605 0.0380  0.0054  -0.0167 470 TRP A O   
2372 C CB  . TRP A 470 ? 0.2565 0.2120 0.2502 0.0330  0.0092  -0.0187 470 TRP A CB  
2373 C CG  . TRP A 470 ? 0.2634 0.1985 0.2519 0.0237  0.0109  -0.0227 470 TRP A CG  
2374 C CD1 . TRP A 470 ? 0.2685 0.2084 0.2624 0.0124  0.0097  -0.0266 470 TRP A CD1 
2375 C CD2 . TRP A 470 ? 0.2818 0.1892 0.2582 0.0245  0.0140  -0.0230 470 TRP A CD2 
2376 N NE1 . TRP A 470 ? 0.2877 0.2082 0.2751 0.0056  0.0116  -0.0297 470 TRP A NE1 
2377 C CE2 . TRP A 470 ? 0.2985 0.1975 0.2748 0.0118  0.0145  -0.0278 470 TRP A CE2 
2378 C CE3 . TRP A 470 ? 0.3119 0.2001 0.2767 0.0348  0.0168  -0.0194 470 TRP A CE3 
2379 C CZ2 . TRP A 470 ? 0.3240 0.1969 0.2898 0.0070  0.0176  -0.0298 470 TRP A CZ2 
2380 C CZ3 . TRP A 470 ? 0.3346 0.1929 0.2874 0.0309  0.0204  -0.0209 470 TRP A CZ3 
2381 C CH2 . TRP A 470 ? 0.3354 0.1867 0.2891 0.0160  0.0208  -0.0262 470 TRP A CH2 
2382 N N   . ARG A 471 ? 0.2590 0.2571 0.2607 0.0597  0.0088  -0.0153 471 ARG A N   
2383 C CA  . ARG A 471 ? 0.2633 0.2901 0.2734 0.0644  0.0065  -0.0118 471 ARG A CA  
2384 C C   . ARG A 471 ? 0.2787 0.3041 0.2857 0.0673  0.0046  -0.0059 471 ARG A C   
2385 O O   . ARG A 471 ? 0.2975 0.3279 0.3010 0.0805  0.0046  -0.0018 471 ARG A O   
2386 C CB  . ARG A 471 ? 0.2867 0.3251 0.2968 0.0783  0.0084  -0.0121 471 ARG A CB  
2387 C CG  . ARG A 471 ? 0.3312 0.4056 0.3535 0.0789  0.0065  -0.0107 471 ARG A CG  
2388 C CD  . ARG A 471 ? 0.3987 0.4870 0.4224 0.0909  0.0092  -0.0122 471 ARG A CD  
2389 N NE  . ARG A 471 ? 0.4418 0.5673 0.4780 0.0901  0.0075  -0.0108 471 ARG A NE  
2390 C CZ  . ARG A 471 ? 0.4685 0.6110 0.5138 0.0782  0.0075  -0.0132 471 ARG A CZ  
2391 N NH1 . ARG A 471 ? 0.4705 0.5970 0.5136 0.0681  0.0089  -0.0169 471 ARG A NH1 
2392 N NH2 . ARG A 471 ? 0.4700 0.6460 0.5261 0.0762  0.0064  -0.0119 471 ARG A NH2 
2393 N N   . CYS A 472 ? 0.2736 0.2921 0.2809 0.0557  0.0032  -0.0055 472 CYS A N   
2394 C CA  . CYS A 472 ? 0.2911 0.3048 0.2936 0.0567  0.0018  -0.0003 472 CYS A CA  
2395 C C   . CYS A 472 ? 0.3001 0.3419 0.3102 0.0557  -0.0021 0.0023  472 CYS A C   
2396 O O   . CYS A 472 ? 0.3134 0.3548 0.3190 0.0584  -0.0036 0.0070  472 CYS A O   
2397 C CB  . CYS A 472 ? 0.3101 0.3034 0.3085 0.0452  0.0027  -0.0013 472 CYS A CB  
2398 S SG  . CYS A 472 ? 0.3058 0.3100 0.3146 0.0292  0.0012  -0.0065 472 CYS A SG  
2399 N N   . PHE A 473 ? 0.2811 0.3468 0.3020 0.0508  -0.0036 -0.0008 473 PHE A N   
2400 C CA  . PHE A 473 ? 0.2703 0.3636 0.2984 0.0483  -0.0072 0.0006  473 PHE A CA  
2401 C C   . PHE A 473 ? 0.3100 0.4302 0.3447 0.0571  -0.0078 0.0010  473 PHE A C   
2402 O O   . PHE A 473 ? 0.3135 0.4589 0.3574 0.0503  -0.0099 -0.0007 473 PHE A O   
2403 C CB  . PHE A 473 ? 0.2367 0.3359 0.2711 0.0323  -0.0084 -0.0032 473 PHE A CB  
2404 C CG  . PHE A 473 ? 0.2344 0.3125 0.2634 0.0244  -0.0080 -0.0035 473 PHE A CG  
2405 C CD1 . PHE A 473 ? 0.2371 0.3099 0.2598 0.0264  -0.0093 0.0003  473 PHE A CD1 
2406 C CD2 . PHE A 473 ? 0.2459 0.3111 0.2758 0.0158  -0.0061 -0.0072 473 PHE A CD2 
2407 C CE1 . PHE A 473 ? 0.2469 0.3021 0.2649 0.0193  -0.0082 0.0001  473 PHE A CE1 
2408 C CE2 . PHE A 473 ? 0.2547 0.3040 0.2805 0.0091  -0.0056 -0.0075 473 PHE A CE2 
2409 C CZ  . PHE A 473 ? 0.2499 0.2945 0.2701 0.0107  -0.0064 -0.0040 473 PHE A CZ  
2410 N N   . GLU A 474 ? 0.3423 0.4574 0.3720 0.0724  -0.0058 0.0031  474 GLU A N   
2411 C CA  . GLU A 474 ? 0.3748 0.5175 0.4107 0.0831  -0.0060 0.0039  474 GLU A CA  
2412 C C   . GLU A 474 ? 0.4281 0.5601 0.4546 0.1030  -0.0039 0.0078  474 GLU A C   
2413 O O   . GLU A 474 ? 0.4464 0.5449 0.4612 0.1065  -0.0011 0.0083  474 GLU A O   
2414 C CB  . GLU A 474 ? 0.4184 0.5706 0.4619 0.0779  -0.0035 -0.0011 474 GLU A CB  
2415 C CG  . GLU A 474 ? 0.4684 0.6540 0.5247 0.0676  -0.0054 -0.0029 474 GLU A CG  
2416 C CD  . GLU A 474 ? 0.5347 0.7562 0.5982 0.0741  -0.0084 -0.0002 474 GLU A CD  
2417 O OE1 . GLU A 474 ? 0.5625 0.8053 0.6339 0.0616  -0.0111 -0.0016 474 GLU A OE1 
2418 O OE2 . GLU A 474 ? 0.5205 0.7492 0.5814 0.0916  -0.0079 0.0031  474 GLU A OE2 
2419 N N   . LEU A 475 ? 0.4412 0.6023 0.4725 0.1159  -0.0050 0.0103  475 LEU A N   
2420 C CA  . LEU A 475 ? 0.4838 0.6418 0.5073 0.1378  -0.0029 0.0142  475 LEU A CA  
2421 C C   . LEU A 475 ? 0.4994 0.6841 0.5316 0.1460  -0.0009 0.0116  475 LEU A C   
2422 O O   . LEU A 475 ? 0.5164 0.6931 0.5413 0.1640  0.0024  0.0129  475 LEU A O   
2423 C CB  . LEU A 475 ? 0.4907 0.6642 0.5115 0.1489  -0.0067 0.0212  475 LEU A CB  
2424 C CG  . LEU A 475 ? 0.5286 0.6793 0.5402 0.1424  -0.0084 0.0246  475 LEU A CG  
2425 C CD1 . LEU A 475 ? 0.5323 0.7046 0.5420 0.1529  -0.0128 0.0314  475 LEU A CD1 
2426 C CD2 . LEU A 475 ? 0.5628 0.6669 0.5582 0.1471  -0.0037 0.0260  475 LEU A CD2 
2427 N N   . ASP A 476 ? 0.4889 0.7053 0.5358 0.1331  -0.0025 0.0081  476 ASP A N   
2428 C CA  . ASP A 476 ? 0.4847 0.7310 0.5418 0.1368  -0.0004 0.0056  476 ASP A CA  
2429 C C   . ASP A 476 ? 0.4675 0.7456 0.5279 0.1564  -0.0012 0.0097  476 ASP A C   
2430 O O   . ASP A 476 ? 0.4507 0.7484 0.5137 0.1588  -0.0058 0.0137  476 ASP A O   
2431 C CB  . ASP A 476 ? 0.5292 0.7518 0.5806 0.1388  0.0051  0.0013  476 ASP A CB  
2432 C CG  . ASP A 476 ? 0.6253 0.8180 0.6728 0.1213  0.0056  -0.0025 476 ASP A CG  
2433 O OD1 . ASP A 476 ? 0.6436 0.8474 0.6993 0.1041  0.0032  -0.0038 476 ASP A OD1 
2434 O OD2 . ASP A 476 ? 0.6769 0.8351 0.7128 0.1248  0.0084  -0.0042 476 ASP A OD2 
# 
