data_9I68
# 
_entry.id   9I68 
# 
_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   9I68         pdb_00009i68 10.2210/pdb9i68/pdb 
WWPDB D_1292145047 ?            ?                   
# 
_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                        9I68 
_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        'PDB entries for the same citation' 
_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-3EG-SER-ASP                  1013.007  1   ? ? ? ? 
3 water   nat water                                    18.015    236 ? ? ? ? 
# 
_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(3EG)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   3EG 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 
3EG 'L-peptide linking' . '(2S)-2-amino-4,4,4-trifluorobutanoic acid' ? 'C4 H6 F3 N O2'  157.091 
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   3EG 4   4   4   3EG 3EG 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        3EG 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   3EG 
_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 10  HOH HOH A . 
C 3 HOH 2   502 168 HOH HOH A . 
C 3 HOH 3   503 195 HOH HOH A . 
C 3 HOH 4   504 235 HOH HOH A . 
C 3 HOH 5   505 112 HOH HOH A . 
C 3 HOH 6   506 155 HOH HOH A . 
C 3 HOH 7   507 80  HOH HOH A . 
C 3 HOH 8   508 75  HOH HOH A . 
C 3 HOH 9   509 127 HOH HOH A . 
C 3 HOH 10  510 219 HOH HOH A . 
C 3 HOH 11  511 133 HOH HOH A . 
C 3 HOH 12  512 99  HOH HOH A . 
C 3 HOH 13  513 123 HOH HOH A . 
C 3 HOH 14  514 49  HOH HOH A . 
C 3 HOH 15  515 119 HOH HOH A . 
C 3 HOH 16  516 40  HOH HOH A . 
C 3 HOH 17  517 67  HOH HOH A . 
C 3 HOH 18  518 179 HOH HOH A . 
C 3 HOH 19  519 84  HOH HOH A . 
C 3 HOH 20  520 164 HOH HOH A . 
C 3 HOH 21  521 107 HOH HOH A . 
C 3 HOH 22  522 65  HOH HOH A . 
C 3 HOH 23  523 74  HOH HOH A . 
C 3 HOH 24  524 225 HOH HOH A . 
C 3 HOH 25  525 61  HOH HOH A . 
C 3 HOH 26  526 72  HOH HOH A . 
C 3 HOH 27  527 81  HOH HOH A . 
C 3 HOH 28  528 161 HOH HOH A . 
C 3 HOH 29  529 39  HOH HOH A . 
C 3 HOH 30  530 178 HOH HOH A . 
C 3 HOH 31  531 58  HOH HOH A . 
C 3 HOH 32  532 137 HOH HOH A . 
C 3 HOH 33  533 48  HOH HOH A . 
C 3 HOH 34  534 140 HOH HOH A . 
C 3 HOH 35  535 129 HOH HOH A . 
C 3 HOH 36  536 108 HOH HOH A . 
C 3 HOH 37  537 93  HOH HOH A . 
C 3 HOH 38  538 51  HOH HOH A . 
C 3 HOH 39  539 35  HOH HOH A . 
C 3 HOH 40  540 87  HOH HOH A . 
C 3 HOH 41  541 203 HOH HOH A . 
C 3 HOH 42  542 54  HOH HOH A . 
C 3 HOH 43  543 110 HOH HOH A . 
C 3 HOH 44  544 111 HOH HOH A . 
C 3 HOH 45  545 124 HOH HOH A . 
C 3 HOH 46  546 156 HOH HOH A . 
C 3 HOH 47  547 19  HOH HOH A . 
C 3 HOH 48  548 28  HOH HOH A . 
C 3 HOH 49  549 198 HOH HOH A . 
C 3 HOH 50  550 63  HOH HOH A . 
C 3 HOH 51  551 3   HOH HOH A . 
C 3 HOH 52  552 42  HOH HOH A . 
C 3 HOH 53  553 34  HOH HOH A . 
C 3 HOH 54  554 41  HOH HOH A . 
C 3 HOH 55  555 215 HOH HOH A . 
C 3 HOH 56  556 76  HOH HOH A . 
C 3 HOH 57  557 30  HOH HOH A . 
C 3 HOH 58  558 16  HOH HOH A . 
C 3 HOH 59  559 130 HOH HOH A . 
C 3 HOH 60  560 45  HOH HOH A . 
C 3 HOH 61  561 5   HOH HOH A . 
C 3 HOH 62  562 91  HOH HOH A . 
C 3 HOH 63  563 29  HOH HOH A . 
C 3 HOH 64  564 192 HOH HOH A . 
C 3 HOH 65  565 214 HOH HOH A . 
C 3 HOH 66  566 221 HOH HOH A . 
C 3 HOH 67  567 105 HOH HOH A . 
C 3 HOH 68  568 234 HOH HOH A . 
C 3 HOH 69  569 66  HOH HOH A . 
C 3 HOH 70  570 15  HOH HOH A . 
C 3 HOH 71  571 160 HOH HOH A . 
C 3 HOH 72  572 154 HOH HOH A . 
C 3 HOH 73  573 11  HOH HOH A . 
C 3 HOH 74  574 60  HOH HOH A . 
C 3 HOH 75  575 100 HOH HOH A . 
C 3 HOH 76  576 197 HOH HOH A . 
C 3 HOH 77  577 92  HOH HOH A . 
C 3 HOH 78  578 204 HOH HOH A . 
C 3 HOH 79  579 6   HOH HOH A . 
C 3 HOH 80  580 96  HOH HOH A . 
C 3 HOH 81  581 27  HOH HOH A . 
C 3 HOH 82  582 106 HOH HOH A . 
C 3 HOH 83  583 189 HOH HOH A . 
C 3 HOH 84  584 64  HOH HOH A . 
C 3 HOH 85  585 14  HOH HOH A . 
C 3 HOH 86  586 125 HOH HOH A . 
C 3 HOH 87  587 193 HOH HOH A . 
C 3 HOH 88  588 182 HOH HOH A . 
C 3 HOH 89  589 114 HOH HOH A . 
C 3 HOH 90  590 50  HOH HOH A . 
C 3 HOH 91  591 37  HOH HOH A . 
C 3 HOH 92  592 145 HOH HOH A . 
C 3 HOH 93  593 33  HOH HOH A . 
C 3 HOH 94  594 43  HOH HOH A . 
C 3 HOH 95  595 88  HOH HOH A . 
C 3 HOH 96  596 159 HOH HOH A . 
C 3 HOH 97  597 103 HOH HOH A . 
C 3 HOH 98  598 188 HOH HOH A . 
C 3 HOH 99  599 21  HOH HOH A . 
C 3 HOH 100 600 138 HOH HOH A . 
C 3 HOH 101 601 141 HOH HOH A . 
C 3 HOH 102 602 53  HOH HOH A . 
C 3 HOH 103 603 20  HOH HOH A . 
C 3 HOH 104 604 206 HOH HOH A . 
C 3 HOH 105 605 218 HOH HOH A . 
C 3 HOH 106 606 169 HOH HOH A . 
C 3 HOH 107 607 59  HOH HOH A . 
C 3 HOH 108 608 47  HOH HOH A . 
C 3 HOH 109 609 194 HOH HOH A . 
C 3 HOH 110 610 55  HOH HOH A . 
C 3 HOH 111 611 231 HOH HOH A . 
C 3 HOH 112 612 132 HOH HOH A . 
C 3 HOH 113 613 8   HOH HOH A . 
C 3 HOH 114 614 1   HOH HOH A . 
C 3 HOH 115 615 151 HOH HOH A . 
C 3 HOH 116 616 116 HOH HOH A . 
C 3 HOH 117 617 69  HOH HOH A . 
C 3 HOH 118 618 13  HOH HOH A . 
C 3 HOH 119 619 17  HOH HOH A . 
C 3 HOH 120 620 70  HOH HOH A . 
C 3 HOH 121 621 56  HOH HOH A . 
C 3 HOH 122 622 46  HOH HOH A . 
C 3 HOH 123 623 115 HOH HOH A . 
C 3 HOH 124 624 210 HOH HOH A . 
C 3 HOH 125 625 57  HOH HOH A . 
C 3 HOH 126 626 78  HOH HOH A . 
C 3 HOH 127 627 82  HOH HOH A . 
C 3 HOH 128 628 77  HOH HOH A . 
C 3 HOH 129 629 222 HOH HOH A . 
C 3 HOH 130 630 31  HOH HOH A . 
C 3 HOH 131 631 118 HOH HOH A . 
C 3 HOH 132 632 187 HOH HOH A . 
C 3 HOH 133 633 26  HOH HOH A . 
C 3 HOH 134 634 196 HOH HOH A . 
C 3 HOH 135 635 147 HOH HOH A . 
C 3 HOH 136 636 199 HOH HOH A . 
C 3 HOH 137 637 162 HOH HOH A . 
C 3 HOH 138 638 173 HOH HOH A . 
C 3 HOH 139 639 83  HOH HOH A . 
C 3 HOH 140 640 68  HOH HOH A . 
C 3 HOH 141 641 97  HOH HOH A . 
C 3 HOH 142 642 190 HOH HOH A . 
C 3 HOH 143 643 98  HOH HOH A . 
C 3 HOH 144 644 174 HOH HOH A . 
C 3 HOH 145 645 148 HOH HOH A . 
C 3 HOH 146 646 158 HOH HOH A . 
C 3 HOH 147 647 232 HOH HOH A . 
C 3 HOH 148 648 32  HOH HOH A . 
C 3 HOH 149 649 128 HOH HOH A . 
C 3 HOH 150 650 113 HOH HOH A . 
C 3 HOH 151 651 73  HOH HOH A . 
C 3 HOH 152 652 95  HOH HOH A . 
C 3 HOH 153 653 71  HOH HOH A . 
C 3 HOH 154 654 213 HOH HOH A . 
C 3 HOH 155 655 12  HOH HOH A . 
C 3 HOH 156 656 146 HOH HOH A . 
C 3 HOH 157 657 163 HOH HOH A . 
C 3 HOH 158 658 23  HOH HOH A . 
C 3 HOH 159 659 22  HOH HOH A . 
C 3 HOH 160 660 184 HOH HOH A . 
C 3 HOH 161 661 36  HOH HOH A . 
C 3 HOH 162 662 52  HOH HOH A . 
C 3 HOH 163 663 62  HOH HOH A . 
C 3 HOH 164 664 102 HOH HOH A . 
C 3 HOH 165 665 101 HOH HOH A . 
C 3 HOH 166 666 181 HOH HOH A . 
C 3 HOH 167 667 236 HOH HOH A . 
C 3 HOH 168 668 176 HOH HOH A . 
C 3 HOH 169 669 233 HOH HOH A . 
C 3 HOH 170 670 175 HOH HOH A . 
C 3 HOH 171 671 7   HOH HOH A . 
C 3 HOH 172 672 122 HOH HOH A . 
C 3 HOH 173 673 25  HOH HOH A . 
C 3 HOH 174 674 90  HOH HOH A . 
C 3 HOH 175 675 143 HOH HOH A . 
C 3 HOH 176 676 152 HOH HOH A . 
C 3 HOH 177 677 224 HOH HOH A . 
C 3 HOH 178 678 185 HOH HOH A . 
C 3 HOH 179 679 157 HOH HOH A . 
C 3 HOH 180 680 166 HOH HOH A . 
C 3 HOH 181 681 38  HOH HOH A . 
C 3 HOH 182 682 18  HOH HOH A . 
C 3 HOH 183 683 167 HOH HOH A . 
C 3 HOH 184 684 44  HOH HOH A . 
C 3 HOH 185 685 191 HOH HOH A . 
C 3 HOH 186 686 104 HOH HOH A . 
C 3 HOH 187 687 142 HOH HOH A . 
C 3 HOH 188 688 223 HOH HOH A . 
C 3 HOH 189 689 79  HOH HOH A . 
C 3 HOH 190 690 139 HOH HOH A . 
C 3 HOH 191 691 4   HOH HOH A . 
C 3 HOH 192 692 86  HOH HOH A . 
C 3 HOH 193 693 131 HOH HOH A . 
C 3 HOH 194 694 186 HOH HOH A . 
C 3 HOH 195 695 183 HOH HOH A . 
C 3 HOH 196 696 170 HOH HOH A . 
C 3 HOH 197 697 227 HOH HOH A . 
C 3 HOH 198 698 165 HOH HOH A . 
C 3 HOH 199 699 177 HOH HOH A . 
C 3 HOH 200 700 9   HOH HOH A . 
C 3 HOH 201 701 230 HOH HOH A . 
C 3 HOH 202 702 216 HOH HOH A . 
C 3 HOH 203 703 172 HOH HOH A . 
C 3 HOH 204 704 134 HOH HOH A . 
C 3 HOH 205 705 149 HOH HOH A . 
C 3 HOH 206 706 2   HOH HOH A . 
C 3 HOH 207 707 94  HOH HOH A . 
C 3 HOH 208 708 117 HOH HOH A . 
C 3 HOH 209 709 24  HOH HOH A . 
C 3 HOH 210 710 200 HOH HOH A . 
C 3 HOH 211 711 126 HOH HOH A . 
C 3 HOH 212 712 201 HOH HOH A . 
C 3 HOH 213 713 109 HOH HOH A . 
C 3 HOH 214 714 220 HOH HOH A . 
C 3 HOH 215 715 226 HOH HOH A . 
C 3 HOH 216 716 89  HOH HOH A . 
C 3 HOH 217 717 205 HOH HOH A . 
C 3 HOH 218 718 211 HOH HOH A . 
C 3 HOH 219 719 212 HOH HOH A . 
C 3 HOH 220 720 217 HOH HOH A . 
C 3 HOH 221 721 136 HOH HOH A . 
C 3 HOH 222 722 85  HOH HOH A . 
C 3 HOH 223 723 228 HOH HOH A . 
C 3 HOH 224 724 180 HOH HOH A . 
C 3 HOH 225 725 144 HOH HOH A . 
C 3 HOH 226 726 229 HOH HOH A . 
C 3 HOH 227 727 171 HOH HOH A . 
C 3 HOH 228 728 150 HOH HOH A . 
C 3 HOH 229 729 208 HOH HOH A . 
C 3 HOH 230 730 207 HOH HOH A . 
C 3 HOH 231 731 209 HOH HOH A . 
C 3 HOH 232 732 135 HOH HOH A . 
D 3 HOH 1   101 120 HOH HOH B . 
D 3 HOH 2   102 121 HOH HOH B . 
D 3 HOH 3   103 153 HOH HOH B . 
D 3 HOH 4   104 202 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 
17 1 Y 1 A GLN 422 ? CG  ? A GLN 422 CG  
18 1 Y 1 A GLN 422 ? CD  ? A GLN 422 CD  
19 1 Y 1 A GLN 422 ? OE1 ? A GLN 422 OE1 
20 1 Y 1 A GLN 422 ? NE2 ? A GLN 422 NE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? BUSTER    ? ? ? '2.10.3 (20-MAY-2020)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless   ? ? ? .                      2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? STARANISO ? ? ? .                      3 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS       ? ? ? .                      4 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER    ? ? ? .                      5 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   109.71 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9I68 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     35.491 
_cell.length_a_esd                 ? 
_cell.length_b                     87.550 
_cell.length_b_esd                 ? 
_cell.length_c                     48.573 
_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                         9I68 
_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                   9I68 
_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                                       9I68 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.505 
_reflns.d_resolution_low                               45.73 
_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                                     32820 
_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                           74.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.1 
_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                                0.056 
_reflns.pdbx_Rpim_I_all                                0.024 
_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                              0.050 
_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                                    1.509 
_reflns_shell.d_res_low                                     1.666 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1641 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               3.7 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               0.688 
_reflns_shell.pdbx_Rpim_I_all                               0.333 
_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                                  0.598 
_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]                            -0.36770 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            0.75860 
_refine.aniso_B[2][2]                            1.67780 
_refine.aniso_B[2][3]                            0.00000 
_refine.aniso_B[3][3]                            -1.31010 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               25.82 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.959 
_refine.correlation_coeff_Fo_to_Fc_free          0.951 
_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                                 9I68 
_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                            1.505 
_refine.ls_d_res_low                             45.73 
_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                     32820 
_refine.ls_number_reflns_R_free                  1602 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    74.2 
_refine.ls_percent_reflns_R_free                 4.880 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1761 
_refine.ls_R_factor_R_free                       0.1938 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1752 
_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   0.093 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.094 
_refine.pdbx_overall_SU_R_Blow_DPI               0.105 
_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             0.103 
_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                        9I68 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.20 
_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                       1.505 
_refine_hist.d_res_low                        45.73 
_refine_hist.number_atoms_solvent             236 
_refine_hist.number_atoms_total               2670 
_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        2425 
_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 ? 2574 ? t_bond_d                  2.00  HARMONIC     
'X-RAY DIFFRACTION' ? 1.01  ? 3531 ? t_angle_deg               2.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 840  ? 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' ? ?     ? 444  ? t_gen_planes              5.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 2574 ? t_it                      10.00 HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_nbd                     ?     ?            
'X-RAY DIFFRACTION' ? 4.22  ? ?    ? t_omega_torsion           ?     ?            
'X-RAY DIFFRACTION' ? 15.71 ? ?    ? t_other_torsion           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_improper_torsion        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 325  ? t_chiral_improper_torsion 5.00  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? ?     ? 8    ? 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' ? ?     ? 2273 ? t_ideal_dist_contact      4.00  SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.505 
_refine_ls_shell.d_res_low                        1.60 
_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             629 
_refine_ls_shell.percent_reflns_obs               8.60 
_refine_ls_shell.percent_reflns_R_free            4.26 
_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                  0.2086 
_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                  0.2327 
# 
_struct.entry_id                     9I68 
_struct.title                        'Crystal structure of human Cdc20 bound to synthetic D-box peptide D21' 
_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        9I68 
_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 9I68        9I68   ? 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 9I68 A 1 ? 499 ? Q12834 1 ? 499 ? 1 499 
2 2 9I68 B 1 ? 9   ? 9I68   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)' 830   ? 
1 MORE         -0    ? 
1 'SSA (A^2)'  12310 ? 
# 
_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 3EG 4 N ? ? B PRO 3 B 3EG 4 1_555 ? ? ? ? ? ? ? 1.346 ? ? 
covale2 covale both ? B 3EG 4 C ? ? ? 1_555 B SER 5 N ? ? B 3EG 4 B SER 5 1_555 ? ? ? ? ? ? ? 1.335 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      3EG 
_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                       3EG 
_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                ? 
_pdbx_modification_feature.ref_pcm_id                         1 
_pdbx_modification_feature.ref_comp_id                        3EG 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Non-standard residue' 
# 
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 10.10 
2 TYR 430 A . ? TYR 430 A PRO 431 A ? PRO 431 A 1 7.50  
# 
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 ? SER A 408 ? VAL A 402 SER A 408 
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 ARG A 174 ? N ARG A 174 O LEU A 469 ? O LEU A 469 
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 ASP A 254 ? N ASP A 254 O LYS A 259 ? O LYS A 259 
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 SER A 408 ? N SER A 408 O GLU A 413 ? O GLU A 413 
AA7 2 3 N LEU A 414 ? N LEU A 414 O TRP A 428 ? O TRP A 428 
AA7 3 4 N LEU A 425 ? N LEU A 425 O LEU A 439 ? O LEU A 439 
# 
_pdbx_entry_details.entry_id                   9I68 
_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 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    614 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    706 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.13 
# 
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 ASN A 196 ? ? 70.61   36.11   
2 1 ASP A 203 ? ? 61.32   -107.73 
3 1 SER A 266 ? ? -170.92 -33.14  
4 1 SER A 278 ? ? 58.81   -124.99 
5 1 SER A 278 ? ? 58.81   -124.51 
6 1 GLN A 355 ? ? -105.21 46.72   
# 
_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         -1.5267 
_pdbx_refine_tls.origin_y         -15.8789 
_pdbx_refine_tls.origin_z         14.6791 
_pdbx_refine_tls.T[1][1]          -0.0829 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0377 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          0.0077 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          -0.0364 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.0194 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          -0.0600 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          0.9589 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.0993 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.2671 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.6599 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          0.0225 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          2.3955 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0611 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.0086 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.0085 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.0008 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.0323 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.0186 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.0112 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.1262 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.0289 
_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 
3EG C    C N N 1   
3EG N    N N N 2   
3EG O    O N N 3   
3EG CA   C N S 4   
3EG CB   C N N 5   
3EG FAC  F N N 6   
3EG FAD  F N N 7   
3EG FAE  F N N 8   
3EG CG   C N N 9   
3EG OXT  O N N 10  
3EG H    H N N 11  
3EG H2   H N N 12  
3EG HA   H N N 13  
3EG HB   H N N 14  
3EG HBA  H N N 15  
3EG HXT  H N N 16  
ALA N    N N N 17  
ALA CA   C N S 18  
ALA C    C N N 19  
ALA O    O N N 20  
ALA CB   C N N 21  
ALA OXT  O N N 22  
ALA H    H N N 23  
ALA H2   H N N 24  
ALA HA   H N N 25  
ALA HB1  H N N 26  
ALA HB2  H N N 27  
ALA HB3  H N N 28  
ALA HXT  H N N 29  
ARG N    N N N 30  
ARG CA   C N S 31  
ARG C    C N N 32  
ARG O    O N N 33  
ARG CB   C N N 34  
ARG CG   C N N 35  
ARG CD   C N N 36  
ARG NE   N N N 37  
ARG CZ   C N N 38  
ARG NH1  N N N 39  
ARG NH2  N N N 40  
ARG OXT  O N N 41  
ARG H    H N N 42  
ARG H2   H N N 43  
ARG HA   H N N 44  
ARG HB2  H N N 45  
ARG HB3  H N N 46  
ARG HG2  H N N 47  
ARG HG3  H N N 48  
ARG HD2  H N N 49  
ARG HD3  H N N 50  
ARG HE   H N N 51  
ARG HH11 H N N 52  
ARG HH12 H N N 53  
ARG HH21 H N N 54  
ARG HH22 H N N 55  
ARG HXT  H N N 56  
ASN N    N N N 57  
ASN CA   C N S 58  
ASN C    C N N 59  
ASN O    O N N 60  
ASN CB   C N N 61  
ASN CG   C N N 62  
ASN OD1  O N N 63  
ASN ND2  N N N 64  
ASN OXT  O N N 65  
ASN H    H N N 66  
ASN H2   H N N 67  
ASN HA   H N N 68  
ASN HB2  H N N 69  
ASN HB3  H N N 70  
ASN HD21 H N N 71  
ASN HD22 H N N 72  
ASN HXT  H N N 73  
ASP N    N N N 74  
ASP CA   C N S 75  
ASP C    C N N 76  
ASP O    O N N 77  
ASP CB   C N N 78  
ASP CG   C N N 79  
ASP OD1  O N N 80  
ASP OD2  O N N 81  
ASP OXT  O N N 82  
ASP H    H N N 83  
ASP H2   H N N 84  
ASP HA   H N N 85  
ASP HB2  H N N 86  
ASP HB3  H N N 87  
ASP HD2  H N N 88  
ASP HXT  H N N 89  
CYS N    N N N 90  
CYS CA   C N R 91  
CYS C    C N N 92  
CYS O    O N N 93  
CYS CB   C N N 94  
CYS SG   S N N 95  
CYS OXT  O N N 96  
CYS H    H N N 97  
CYS H2   H N N 98  
CYS HA   H N N 99  
CYS HB2  H N N 100 
CYS HB3  H N N 101 
CYS HG   H N N 102 
CYS HXT  H N N 103 
GLN N    N N N 104 
GLN CA   C N S 105 
GLN C    C N N 106 
GLN O    O N N 107 
GLN CB   C N N 108 
GLN CG   C N N 109 
GLN CD   C N N 110 
GLN OE1  O N N 111 
GLN NE2  N N N 112 
GLN OXT  O N N 113 
GLN H    H N N 114 
GLN H2   H N N 115 
GLN HA   H N N 116 
GLN HB2  H N N 117 
GLN HB3  H N N 118 
GLN HG2  H N N 119 
GLN HG3  H N N 120 
GLN HE21 H N N 121 
GLN HE22 H N N 122 
GLN HXT  H N N 123 
GLU N    N N N 124 
GLU CA   C N S 125 
GLU C    C N N 126 
GLU O    O N N 127 
GLU CB   C N N 128 
GLU CG   C N N 129 
GLU CD   C N N 130 
GLU OE1  O N N 131 
GLU OE2  O N N 132 
GLU OXT  O N N 133 
GLU H    H N N 134 
GLU H2   H N N 135 
GLU HA   H N N 136 
GLU HB2  H N N 137 
GLU HB3  H N N 138 
GLU HG2  H N N 139 
GLU HG3  H N N 140 
GLU HE2  H N N 141 
GLU HXT  H N N 142 
GLY N    N N N 143 
GLY CA   C N N 144 
GLY C    C N N 145 
GLY O    O N N 146 
GLY OXT  O N N 147 
GLY H    H N N 148 
GLY H2   H N N 149 
GLY HA2  H N N 150 
GLY HA3  H N N 151 
GLY HXT  H N N 152 
HIS N    N N N 153 
HIS CA   C N S 154 
HIS C    C N N 155 
HIS O    O N N 156 
HIS CB   C N N 157 
HIS CG   C Y N 158 
HIS ND1  N Y N 159 
HIS CD2  C Y N 160 
HIS CE1  C Y N 161 
HIS NE2  N Y N 162 
HIS OXT  O N N 163 
HIS H    H N N 164 
HIS H2   H N N 165 
HIS HA   H N N 166 
HIS HB2  H N N 167 
HIS HB3  H N N 168 
HIS HD1  H N N 169 
HIS HD2  H N N 170 
HIS HE1  H N N 171 
HIS HE2  H N N 172 
HIS HXT  H N N 173 
HOH O    O N N 174 
HOH H1   H N N 175 
HOH H2   H N N 176 
ILE N    N N N 177 
ILE CA   C N S 178 
ILE C    C N N 179 
ILE O    O N N 180 
ILE CB   C N S 181 
ILE CG1  C N N 182 
ILE CG2  C N N 183 
ILE CD1  C N N 184 
ILE OXT  O N N 185 
ILE H    H N N 186 
ILE H2   H N N 187 
ILE HA   H N N 188 
ILE HB   H N N 189 
ILE HG12 H N N 190 
ILE HG13 H N N 191 
ILE HG21 H N N 192 
ILE HG22 H N N 193 
ILE HG23 H N N 194 
ILE HD11 H N N 195 
ILE HD12 H N N 196 
ILE HD13 H N N 197 
ILE HXT  H N N 198 
LEU N    N N N 199 
LEU CA   C N S 200 
LEU C    C N N 201 
LEU O    O N N 202 
LEU CB   C N N 203 
LEU CG   C N N 204 
LEU CD1  C N N 205 
LEU CD2  C N N 206 
LEU OXT  O N N 207 
LEU H    H N N 208 
LEU H2   H N N 209 
LEU HA   H N N 210 
LEU HB2  H N N 211 
LEU HB3  H N N 212 
LEU HG   H N N 213 
LEU HD11 H N N 214 
LEU HD12 H N N 215 
LEU HD13 H N N 216 
LEU HD21 H N N 217 
LEU HD22 H N N 218 
LEU HD23 H N N 219 
LEU HXT  H N N 220 
LYS N    N N N 221 
LYS CA   C N S 222 
LYS C    C N N 223 
LYS O    O N N 224 
LYS CB   C N N 225 
LYS CG   C N N 226 
LYS CD   C N N 227 
LYS CE   C N N 228 
LYS NZ   N N N 229 
LYS OXT  O N N 230 
LYS H    H N N 231 
LYS H2   H N N 232 
LYS HA   H N N 233 
LYS HB2  H N N 234 
LYS HB3  H N N 235 
LYS HG2  H N N 236 
LYS HG3  H N N 237 
LYS HD2  H N N 238 
LYS HD3  H N N 239 
LYS HE2  H N N 240 
LYS HE3  H N N 241 
LYS HZ1  H N N 242 
LYS HZ2  H N N 243 
LYS HZ3  H N N 244 
LYS HXT  H N N 245 
MET N    N N N 246 
MET CA   C N S 247 
MET C    C N N 248 
MET O    O N N 249 
MET CB   C N N 250 
MET CG   C N N 251 
MET SD   S N N 252 
MET CE   C N N 253 
MET OXT  O N N 254 
MET H    H N N 255 
MET H2   H N N 256 
MET HA   H N N 257 
MET HB2  H N N 258 
MET HB3  H N N 259 
MET HG2  H N N 260 
MET HG3  H N N 261 
MET HE1  H N N 262 
MET HE2  H N N 263 
MET HE3  H N N 264 
MET HXT  H N N 265 
PHE N    N N N 266 
PHE CA   C N S 267 
PHE C    C N N 268 
PHE O    O N N 269 
PHE CB   C N N 270 
PHE CG   C Y N 271 
PHE CD1  C Y N 272 
PHE CD2  C Y N 273 
PHE CE1  C Y N 274 
PHE CE2  C Y N 275 
PHE CZ   C Y N 276 
PHE OXT  O N N 277 
PHE H    H N N 278 
PHE H2   H N N 279 
PHE HA   H N N 280 
PHE HB2  H N N 281 
PHE HB3  H N N 282 
PHE HD1  H N N 283 
PHE HD2  H N N 284 
PHE HE1  H N N 285 
PHE HE2  H N N 286 
PHE HZ   H N N 287 
PHE HXT  H N N 288 
PRO N    N N N 289 
PRO CA   C N S 290 
PRO C    C N N 291 
PRO O    O N N 292 
PRO CB   C N N 293 
PRO CG   C N N 294 
PRO CD   C N N 295 
PRO OXT  O N N 296 
PRO H    H N N 297 
PRO HA   H N N 298 
PRO HB2  H N N 299 
PRO HB3  H N N 300 
PRO HG2  H N N 301 
PRO HG3  H N N 302 
PRO HD2  H N N 303 
PRO HD3  H N N 304 
PRO HXT  H N N 305 
SER N    N N N 306 
SER CA   C N S 307 
SER C    C N N 308 
SER O    O N N 309 
SER CB   C N N 310 
SER OG   O N N 311 
SER OXT  O N N 312 
SER H    H N N 313 
SER H2   H N N 314 
SER HA   H N N 315 
SER HB2  H N N 316 
SER HB3  H N N 317 
SER HG   H N N 318 
SER HXT  H N N 319 
THR N    N N N 320 
THR CA   C N S 321 
THR C    C N N 322 
THR O    O N N 323 
THR CB   C N R 324 
THR OG1  O N N 325 
THR CG2  C N N 326 
THR OXT  O N N 327 
THR H    H N N 328 
THR H2   H N N 329 
THR HA   H N N 330 
THR HB   H N N 331 
THR HG1  H N N 332 
THR HG21 H N N 333 
THR HG22 H N N 334 
THR HG23 H N N 335 
THR HXT  H N N 336 
TRP N    N N N 337 
TRP CA   C N S 338 
TRP C    C N N 339 
TRP O    O N N 340 
TRP CB   C N N 341 
TRP CG   C Y N 342 
TRP CD1  C Y N 343 
TRP CD2  C Y N 344 
TRP NE1  N Y N 345 
TRP CE2  C Y N 346 
TRP CE3  C Y N 347 
TRP CZ2  C Y N 348 
TRP CZ3  C Y N 349 
TRP CH2  C Y N 350 
TRP OXT  O N N 351 
TRP H    H N N 352 
TRP H2   H N N 353 
TRP HA   H N N 354 
TRP HB2  H N N 355 
TRP HB3  H N N 356 
TRP HD1  H N N 357 
TRP HE1  H N N 358 
TRP HE3  H N N 359 
TRP HZ2  H N N 360 
TRP HZ3  H N N 361 
TRP HH2  H N N 362 
TRP HXT  H N N 363 
TYR N    N N N 364 
TYR CA   C N S 365 
TYR C    C N N 366 
TYR O    O N N 367 
TYR CB   C N N 368 
TYR CG   C Y N 369 
TYR CD1  C Y N 370 
TYR CD2  C Y N 371 
TYR CE1  C Y N 372 
TYR CE2  C Y N 373 
TYR CZ   C Y N 374 
TYR OH   O N N 375 
TYR OXT  O N N 376 
TYR H    H N N 377 
TYR H2   H N N 378 
TYR HA   H N N 379 
TYR HB2  H N N 380 
TYR HB3  H N N 381 
TYR HD1  H N N 382 
TYR HD2  H N N 383 
TYR HE1  H N N 384 
TYR HE2  H N N 385 
TYR HH   H N N 386 
TYR HXT  H N N 387 
VAL N    N N N 388 
VAL CA   C N S 389 
VAL C    C N N 390 
VAL O    O N N 391 
VAL CB   C N N 392 
VAL CG1  C N N 393 
VAL CG2  C N N 394 
VAL OXT  O N N 395 
VAL H    H N N 396 
VAL H2   H N N 397 
VAL HA   H N N 398 
VAL HB   H N N 399 
VAL HG11 H N N 400 
VAL HG12 H N N 401 
VAL HG13 H N N 402 
VAL HG21 H N N 403 
VAL HG22 H N N 404 
VAL HG23 H N N 405 
VAL HXT  H N N 406 
# 
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 
3EG C   O    doub N N 1   
3EG C   CA   sing N N 2   
3EG C   OXT  sing N N 3   
3EG N   CA   sing N N 4   
3EG N   H    sing N N 5   
3EG N   H2   sing N N 6   
3EG CA  CB   sing N N 7   
3EG CA  HA   sing N N 8   
3EG CB  CG   sing N N 9   
3EG CB  HB   sing N N 10  
3EG CB  HBA  sing N N 11  
3EG FAC CG   sing N N 12  
3EG FAD CG   sing N N 13  
3EG FAE CG   sing N N 14  
3EG OXT HXT  sing N N 15  
ALA N   CA   sing N N 16  
ALA N   H    sing N N 17  
ALA N   H2   sing N N 18  
ALA CA  C    sing N N 19  
ALA CA  CB   sing N N 20  
ALA CA  HA   sing N N 21  
ALA C   O    doub N N 22  
ALA C   OXT  sing N N 23  
ALA CB  HB1  sing N N 24  
ALA CB  HB2  sing N N 25  
ALA CB  HB3  sing N N 26  
ALA OXT HXT  sing N N 27  
ARG N   CA   sing N N 28  
ARG N   H    sing N N 29  
ARG N   H2   sing N N 30  
ARG CA  C    sing N N 31  
ARG CA  CB   sing N N 32  
ARG CA  HA   sing N N 33  
ARG C   O    doub N N 34  
ARG C   OXT  sing N N 35  
ARG CB  CG   sing N N 36  
ARG CB  HB2  sing N N 37  
ARG CB  HB3  sing N N 38  
ARG CG  CD   sing N N 39  
ARG CG  HG2  sing N N 40  
ARG CG  HG3  sing N N 41  
ARG CD  NE   sing N N 42  
ARG CD  HD2  sing N N 43  
ARG CD  HD3  sing N N 44  
ARG NE  CZ   sing N N 45  
ARG NE  HE   sing N N 46  
ARG CZ  NH1  sing N N 47  
ARG CZ  NH2  doub N N 48  
ARG NH1 HH11 sing N N 49  
ARG NH1 HH12 sing N N 50  
ARG NH2 HH21 sing N N 51  
ARG NH2 HH22 sing N N 52  
ARG OXT HXT  sing N N 53  
ASN N   CA   sing N N 54  
ASN N   H    sing N N 55  
ASN N   H2   sing N N 56  
ASN CA  C    sing N N 57  
ASN CA  CB   sing N N 58  
ASN CA  HA   sing N N 59  
ASN C   O    doub N N 60  
ASN C   OXT  sing N N 61  
ASN CB  CG   sing N N 62  
ASN CB  HB2  sing N N 63  
ASN CB  HB3  sing N N 64  
ASN CG  OD1  doub N N 65  
ASN CG  ND2  sing N N 66  
ASN ND2 HD21 sing N N 67  
ASN ND2 HD22 sing N N 68  
ASN OXT HXT  sing N N 69  
ASP N   CA   sing N N 70  
ASP N   H    sing N N 71  
ASP N   H2   sing N N 72  
ASP CA  C    sing N N 73  
ASP CA  CB   sing N N 74  
ASP CA  HA   sing N N 75  
ASP C   O    doub N N 76  
ASP C   OXT  sing N N 77  
ASP CB  CG   sing N N 78  
ASP CB  HB2  sing N N 79  
ASP CB  HB3  sing N N 80  
ASP CG  OD1  doub N N 81  
ASP CG  OD2  sing N N 82  
ASP OD2 HD2  sing N N 83  
ASP OXT HXT  sing N N 84  
CYS N   CA   sing N N 85  
CYS N   H    sing N N 86  
CYS N   H2   sing N N 87  
CYS CA  C    sing N N 88  
CYS CA  CB   sing N N 89  
CYS CA  HA   sing N N 90  
CYS C   O    doub N N 91  
CYS C   OXT  sing N N 92  
CYS CB  SG   sing N N 93  
CYS CB  HB2  sing N N 94  
CYS CB  HB3  sing N N 95  
CYS SG  HG   sing N N 96  
CYS OXT HXT  sing N N 97  
GLN N   CA   sing N N 98  
GLN N   H    sing N N 99  
GLN N   H2   sing N N 100 
GLN CA  C    sing N N 101 
GLN CA  CB   sing N N 102 
GLN CA  HA   sing N N 103 
GLN C   O    doub N N 104 
GLN C   OXT  sing N N 105 
GLN CB  CG   sing N N 106 
GLN CB  HB2  sing N N 107 
GLN CB  HB3  sing N N 108 
GLN CG  CD   sing N N 109 
GLN CG  HG2  sing N N 110 
GLN CG  HG3  sing N N 111 
GLN CD  OE1  doub N N 112 
GLN CD  NE2  sing N N 113 
GLN NE2 HE21 sing N N 114 
GLN NE2 HE22 sing N N 115 
GLN OXT HXT  sing N N 116 
GLU N   CA   sing N N 117 
GLU N   H    sing N N 118 
GLU N   H2   sing N N 119 
GLU CA  C    sing N N 120 
GLU CA  CB   sing N N 121 
GLU CA  HA   sing N N 122 
GLU C   O    doub N N 123 
GLU C   OXT  sing N N 124 
GLU CB  CG   sing N N 125 
GLU CB  HB2  sing N N 126 
GLU CB  HB3  sing N N 127 
GLU CG  CD   sing N N 128 
GLU CG  HG2  sing N N 129 
GLU CG  HG3  sing N N 130 
GLU CD  OE1  doub N N 131 
GLU CD  OE2  sing N N 132 
GLU OE2 HE2  sing N N 133 
GLU OXT HXT  sing N N 134 
GLY N   CA   sing N N 135 
GLY N   H    sing N N 136 
GLY N   H2   sing N N 137 
GLY CA  C    sing N N 138 
GLY CA  HA2  sing N N 139 
GLY CA  HA3  sing N N 140 
GLY C   O    doub N N 141 
GLY C   OXT  sing N N 142 
GLY OXT HXT  sing N N 143 
HIS N   CA   sing N N 144 
HIS N   H    sing N N 145 
HIS N   H2   sing N N 146 
HIS CA  C    sing N N 147 
HIS CA  CB   sing N N 148 
HIS CA  HA   sing N N 149 
HIS C   O    doub N N 150 
HIS C   OXT  sing N N 151 
HIS CB  CG   sing N N 152 
HIS CB  HB2  sing N N 153 
HIS CB  HB3  sing N N 154 
HIS CG  ND1  sing Y N 155 
HIS CG  CD2  doub Y N 156 
HIS ND1 CE1  doub Y N 157 
HIS ND1 HD1  sing N N 158 
HIS CD2 NE2  sing Y N 159 
HIS CD2 HD2  sing N N 160 
HIS CE1 NE2  sing Y N 161 
HIS CE1 HE1  sing N N 162 
HIS NE2 HE2  sing N N 163 
HIS OXT HXT  sing N N 164 
HOH O   H1   sing N N 165 
HOH O   H2   sing N N 166 
ILE N   CA   sing N N 167 
ILE N   H    sing N N 168 
ILE N   H2   sing N N 169 
ILE CA  C    sing N N 170 
ILE CA  CB   sing N N 171 
ILE CA  HA   sing N N 172 
ILE C   O    doub N N 173 
ILE C   OXT  sing N N 174 
ILE CB  CG1  sing N N 175 
ILE CB  CG2  sing N N 176 
ILE CB  HB   sing N N 177 
ILE CG1 CD1  sing N N 178 
ILE CG1 HG12 sing N N 179 
ILE CG1 HG13 sing N N 180 
ILE CG2 HG21 sing N N 181 
ILE CG2 HG22 sing N N 182 
ILE CG2 HG23 sing N N 183 
ILE CD1 HD11 sing N N 184 
ILE CD1 HD12 sing N N 185 
ILE CD1 HD13 sing N N 186 
ILE OXT HXT  sing N N 187 
LEU N   CA   sing N N 188 
LEU N   H    sing N N 189 
LEU N   H2   sing N N 190 
LEU CA  C    sing N N 191 
LEU CA  CB   sing N N 192 
LEU CA  HA   sing N N 193 
LEU C   O    doub N N 194 
LEU C   OXT  sing N N 195 
LEU CB  CG   sing N N 196 
LEU CB  HB2  sing N N 197 
LEU CB  HB3  sing N N 198 
LEU CG  CD1  sing N N 199 
LEU CG  CD2  sing N N 200 
LEU CG  HG   sing N N 201 
LEU CD1 HD11 sing N N 202 
LEU CD1 HD12 sing N N 203 
LEU CD1 HD13 sing N N 204 
LEU CD2 HD21 sing N N 205 
LEU CD2 HD22 sing N N 206 
LEU CD2 HD23 sing N N 207 
LEU OXT HXT  sing N N 208 
LYS N   CA   sing N N 209 
LYS N   H    sing N N 210 
LYS N   H2   sing N N 211 
LYS CA  C    sing N N 212 
LYS CA  CB   sing N N 213 
LYS CA  HA   sing N N 214 
LYS C   O    doub N N 215 
LYS C   OXT  sing N N 216 
LYS CB  CG   sing N N 217 
LYS CB  HB2  sing N N 218 
LYS CB  HB3  sing N N 219 
LYS CG  CD   sing N N 220 
LYS CG  HG2  sing N N 221 
LYS CG  HG3  sing N N 222 
LYS CD  CE   sing N N 223 
LYS CD  HD2  sing N N 224 
LYS CD  HD3  sing N N 225 
LYS CE  NZ   sing N N 226 
LYS CE  HE2  sing N N 227 
LYS CE  HE3  sing N N 228 
LYS NZ  HZ1  sing N N 229 
LYS NZ  HZ2  sing N N 230 
LYS NZ  HZ3  sing N N 231 
LYS OXT HXT  sing N N 232 
MET N   CA   sing N N 233 
MET N   H    sing N N 234 
MET N   H2   sing N N 235 
MET CA  C    sing N N 236 
MET CA  CB   sing N N 237 
MET CA  HA   sing N N 238 
MET C   O    doub N N 239 
MET C   OXT  sing N N 240 
MET CB  CG   sing N N 241 
MET CB  HB2  sing N N 242 
MET CB  HB3  sing N N 243 
MET CG  SD   sing N N 244 
MET CG  HG2  sing N N 245 
MET CG  HG3  sing N N 246 
MET SD  CE   sing N N 247 
MET CE  HE1  sing N N 248 
MET CE  HE2  sing N N 249 
MET CE  HE3  sing N N 250 
MET OXT HXT  sing N N 251 
PHE N   CA   sing N N 252 
PHE N   H    sing N N 253 
PHE N   H2   sing N N 254 
PHE CA  C    sing N N 255 
PHE CA  CB   sing N N 256 
PHE CA  HA   sing N N 257 
PHE C   O    doub N N 258 
PHE C   OXT  sing N N 259 
PHE CB  CG   sing N N 260 
PHE CB  HB2  sing N N 261 
PHE CB  HB3  sing N N 262 
PHE CG  CD1  doub Y N 263 
PHE CG  CD2  sing Y N 264 
PHE CD1 CE1  sing Y N 265 
PHE CD1 HD1  sing N N 266 
PHE CD2 CE2  doub Y N 267 
PHE CD2 HD2  sing N N 268 
PHE CE1 CZ   doub Y N 269 
PHE CE1 HE1  sing N N 270 
PHE CE2 CZ   sing Y N 271 
PHE CE2 HE2  sing N N 272 
PHE CZ  HZ   sing N N 273 
PHE OXT HXT  sing N N 274 
PRO N   CA   sing N N 275 
PRO N   CD   sing N N 276 
PRO N   H    sing N N 277 
PRO CA  C    sing N N 278 
PRO CA  CB   sing N N 279 
PRO CA  HA   sing N N 280 
PRO C   O    doub N N 281 
PRO C   OXT  sing N N 282 
PRO CB  CG   sing N N 283 
PRO CB  HB2  sing N N 284 
PRO CB  HB3  sing N N 285 
PRO CG  CD   sing N N 286 
PRO CG  HG2  sing N N 287 
PRO CG  HG3  sing N N 288 
PRO CD  HD2  sing N N 289 
PRO CD  HD3  sing N N 290 
PRO OXT HXT  sing N N 291 
SER N   CA   sing N N 292 
SER N   H    sing N N 293 
SER N   H2   sing N N 294 
SER CA  C    sing N N 295 
SER CA  CB   sing N N 296 
SER CA  HA   sing N N 297 
SER C   O    doub N N 298 
SER C   OXT  sing N N 299 
SER CB  OG   sing N N 300 
SER CB  HB2  sing N N 301 
SER CB  HB3  sing N N 302 
SER OG  HG   sing N N 303 
SER OXT HXT  sing N N 304 
THR N   CA   sing N N 305 
THR N   H    sing N N 306 
THR N   H2   sing N N 307 
THR CA  C    sing N N 308 
THR CA  CB   sing N N 309 
THR CA  HA   sing N N 310 
THR C   O    doub N N 311 
THR C   OXT  sing N N 312 
THR CB  OG1  sing N N 313 
THR CB  CG2  sing N N 314 
THR CB  HB   sing N N 315 
THR OG1 HG1  sing N N 316 
THR CG2 HG21 sing N N 317 
THR CG2 HG22 sing N N 318 
THR CG2 HG23 sing N N 319 
THR OXT HXT  sing N N 320 
TRP N   CA   sing N N 321 
TRP N   H    sing N N 322 
TRP N   H2   sing N N 323 
TRP CA  C    sing N N 324 
TRP CA  CB   sing N N 325 
TRP CA  HA   sing N N 326 
TRP C   O    doub N N 327 
TRP C   OXT  sing N N 328 
TRP CB  CG   sing N N 329 
TRP CB  HB2  sing N N 330 
TRP CB  HB3  sing N N 331 
TRP CG  CD1  doub Y N 332 
TRP CG  CD2  sing Y N 333 
TRP CD1 NE1  sing Y N 334 
TRP CD1 HD1  sing N N 335 
TRP CD2 CE2  doub Y N 336 
TRP CD2 CE3  sing Y N 337 
TRP NE1 CE2  sing Y N 338 
TRP NE1 HE1  sing N N 339 
TRP CE2 CZ2  sing Y N 340 
TRP CE3 CZ3  doub Y N 341 
TRP CE3 HE3  sing N N 342 
TRP CZ2 CH2  doub Y N 343 
TRP CZ2 HZ2  sing N N 344 
TRP CZ3 CH2  sing Y N 345 
TRP CZ3 HZ3  sing N N 346 
TRP CH2 HH2  sing N N 347 
TRP OXT HXT  sing N N 348 
TYR N   CA   sing N N 349 
TYR N   H    sing N N 350 
TYR N   H2   sing N N 351 
TYR CA  C    sing N N 352 
TYR CA  CB   sing N N 353 
TYR CA  HA   sing N N 354 
TYR C   O    doub N N 355 
TYR C   OXT  sing N N 356 
TYR CB  CG   sing N N 357 
TYR CB  HB2  sing N N 358 
TYR CB  HB3  sing N N 359 
TYR CG  CD1  doub Y N 360 
TYR CG  CD2  sing Y N 361 
TYR CD1 CE1  sing Y N 362 
TYR CD1 HD1  sing N N 363 
TYR CD2 CE2  doub Y N 364 
TYR CD2 HD2  sing N N 365 
TYR CE1 CZ   doub Y N 366 
TYR CE1 HE1  sing N N 367 
TYR CE2 CZ   sing Y N 368 
TYR CE2 HE2  sing N N 369 
TYR CZ  OH   sing N N 370 
TYR OH  HH   sing N N 371 
TYR OXT HXT  sing N N 372 
VAL N   CA   sing N N 373 
VAL N   H    sing N N 374 
VAL N   H2   sing N N 375 
VAL CA  C    sing N N 376 
VAL CA  CB   sing N N 377 
VAL CA  HA   sing N N 378 
VAL C   O    doub N N 379 
VAL C   OXT  sing N N 380 
VAL CB  CG1  sing N N 381 
VAL CB  CG2  sing N N 382 
VAL CB  HB   sing N N 383 
VAL CG1 HG11 sing N N 384 
VAL CG1 HG12 sing N N 385 
VAL CG1 HG13 sing N N 386 
VAL CG2 HG21 sing N N 387 
VAL CG2 HG22 sing N N 388 
VAL CG2 HG23 sing N N 389 
VAL OXT HXT  sing N N 390 
# 
_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                    9I68 
_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]   0.028176 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.010094 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011422 
_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]   0.021869 
_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 
F 
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 ? -17.771 0.622   -0.657  1.00 43.85 ? 166 ARG A N   1 
ATOM   2    C CA  . ARG A 1 166 ? -18.422 0.457   0.640   1.00 43.82 ? 166 ARG A CA  1 
ATOM   3    C C   . ARG A 1 166 ? -17.780 1.347   1.718   1.00 44.91 ? 166 ARG A C   1 
ATOM   4    O O   . ARG A 1 166 ? -16.619 1.734   1.576   1.00 45.57 ? 166 ARG A O   1 
ATOM   5    C CB  . ARG A 1 166 ? -18.431 -1.024  1.055   1.00 43.92 ? 166 ARG A CB  1 
ATOM   6    C CG  . ARG A 1 166 ? -17.066 -1.606  1.455   1.00 43.72 ? 166 ARG A CG  1 
ATOM   7    C CD  . ARG A 1 166 ? -17.222 -3.043  1.943   1.00 42.63 ? 166 ARG A CD  1 
ATOM   8    N NE  . ARG A 1 166 ? -16.043 -3.548  2.659   1.00 39.87 ? 166 ARG A NE  1 
ATOM   9    C CZ  . ARG A 1 166 ? -15.851 -3.420  3.968   1.00 37.67 ? 166 ARG A CZ  1 
ATOM   10   N NH1 . ARG A 1 166 ? -16.751 -2.800  4.723   1.00 36.31 ? 166 ARG A NH1 1 
ATOM   11   N NH2 . ARG A 1 166 ? -14.755 -3.906  4.533   1.00 36.01 ? 166 ARG A NH2 1 
ATOM   12   N N   . TYR A 1 167 ? -18.520 1.673   2.791   1.00 44.91 ? 167 TYR A N   1 
ATOM   13   C CA  . TYR A 1 167 ? -17.978 2.521   3.860   1.00 45.25 ? 167 TYR A CA  1 
ATOM   14   C C   . TYR A 1 167 ? -17.215 1.741   4.951   1.00 43.35 ? 167 TYR A C   1 
ATOM   15   O O   . TYR A 1 167 ? -17.759 0.844   5.604   1.00 43.96 ? 167 TYR A O   1 
ATOM   16   C CB  . TYR A 1 167 ? -19.062 3.429   4.484   1.00 46.65 ? 167 TYR A CB  1 
ATOM   17   C CG  . TYR A 1 167 ? -18.560 4.269   5.643   1.00 48.73 ? 167 TYR A CG  1 
ATOM   18   C CD1 . TYR A 1 167 ? -18.643 3.806   6.951   1.00 50.26 ? 167 TYR A CD1 1 
ATOM   19   C CD2 . TYR A 1 167 ? -17.977 5.510   5.429   1.00 50.01 ? 167 TYR A CD2 1 
ATOM   20   C CE1 . TYR A 1 167 ? -18.136 4.546   8.012   1.00 51.63 ? 167 TYR A CE1 1 
ATOM   21   C CE2 . TYR A 1 167 ? -17.489 6.271   6.486   1.00 51.25 ? 167 TYR A CE2 1 
ATOM   22   C CZ  . TYR A 1 167 ? -17.571 5.785   7.778   1.00 52.70 ? 167 TYR A CZ  1 
ATOM   23   O OH  . TYR A 1 167 ? -17.099 6.523   8.840   1.00 54.94 ? 167 TYR A OH  1 
ATOM   24   N N   . ILE A 1 168 ? -15.964 2.150   5.192   1.00 40.52 ? 168 ILE A N   1 
ATOM   25   C CA  . ILE A 1 168 ? -15.107 1.572   6.222   1.00 38.14 ? 168 ILE A CA  1 
ATOM   26   C C   . ILE A 1 168 ? -14.707 2.702   7.175   1.00 36.35 ? 168 ILE A C   1 
ATOM   27   O O   . ILE A 1 168 ? -14.210 3.729   6.722   1.00 35.60 ? 168 ILE A O   1 
ATOM   28   C CB  . ILE A 1 168 ? -13.866 0.940   5.553   1.00 37.91 ? 168 ILE A CB  1 
ATOM   29   C CG1 . ILE A 1 168 ? -14.272 -0.232  4.652   1.00 38.78 ? 168 ILE A CG1 1 
ATOM   30   C CG2 . ILE A 1 168 ? -12.835 0.517   6.586   1.00 37.56 ? 168 ILE A CG2 1 
ATOM   31   C CD1 . ILE A 1 168 ? -13.432 -0.394  3.457   1.00 39.63 ? 168 ILE A CD1 1 
ATOM   32   N N   . PRO A 1 169 ? -14.919 2.539   8.489   1.00 35.13 ? 169 PRO A N   1 
ATOM   33   C CA  . PRO A 1 169 ? -14.581 3.623   9.426   1.00 33.86 ? 169 PRO A CA  1 
ATOM   34   C C   . PRO A 1 169 ? -13.084 3.902   9.530   1.00 31.90 ? 169 PRO A C   1 
ATOM   35   O O   . PRO A 1 169 ? -12.289 2.972   9.584   1.00 31.89 ? 169 PRO A O   1 
ATOM   36   C CB  . PRO A 1 169 ? -15.164 3.142   10.764  1.00 35.58 ? 169 PRO A CB  1 
ATOM   37   C CG  . PRO A 1 169 ? -16.081 2.003   10.416  1.00 36.43 ? 169 PRO A CG  1 
ATOM   38   C CD  . PRO A 1 169 ? -15.510 1.383   9.186   1.00 34.94 ? 169 PRO A CD  1 
ATOM   39   N N   . SER A 1 170 ? -12.696 5.185   9.536   1.00 30.46 ? 170 SER A N   1 
ATOM   40   C CA  . SER A 1 170 ? -11.274 5.545   9.650   1.00 29.84 ? 170 SER A CA  1 
ATOM   41   C C   . SER A 1 170 ? -10.747 5.467   11.103  1.00 27.79 ? 170 SER A C   1 
ATOM   42   O O   . SER A 1 170 ? -9.531  5.442   11.327  1.00 28.06 ? 170 SER A O   1 
ATOM   43   C CB  . SER A 1 170 ? -11.026 6.926   9.058   1.00 31.76 ? 170 SER A CB  1 
ATOM   44   O OG  . SER A 1 170 ? -11.816 7.893   9.722   1.00 35.81 ? 170 SER A OG  1 
ATOM   45   N N   . LEU A 1 171 ? -11.654 5.441   12.088  1.00 25.54 ? 171 LEU A N   1 
ATOM   46   C CA  . LEU A 1 171 ? -11.268 5.325   13.485  1.00 24.51 ? 171 LEU A CA  1 
ATOM   47   C C   . LEU A 1 171 ? -11.591 3.941   14.009  1.00 24.23 ? 171 LEU A C   1 
ATOM   48   O O   . LEU A 1 171 ? -12.588 3.354   13.603  1.00 25.26 ? 171 LEU A O   1 
ATOM   49   C CB  . LEU A 1 171 ? -12.070 6.320   14.334  1.00 24.48 ? 171 LEU A CB  1 
ATOM   50   C CG  . LEU A 1 171 ? -11.898 7.773   13.946  1.00 26.91 ? 171 LEU A CG  1 
ATOM   51   C CD1 . LEU A 1 171 ? -12.817 8.636   14.759  1.00 27.61 ? 171 LEU A CD1 1 
ATOM   52   C CD2 . LEU A 1 171 ? -10.434 8.211   14.102  1.00 28.39 ? 171 LEU A CD2 1 
ATOM   53   N N   . PRO A 1 172 ? -10.793 3.427   14.946  1.00 23.08 ? 172 PRO A N   1 
ATOM   54   C CA  . PRO A 1 172 ? -11.146 2.141   15.567  1.00 22.99 ? 172 PRO A CA  1 
ATOM   55   C C   . PRO A 1 172 ? -12.371 2.321   16.477  1.00 24.54 ? 172 PRO A C   1 
ATOM   56   O O   . PRO A 1 172 ? -12.675 3.428   16.925  1.00 24.50 ? 172 PRO A O   1 
ATOM   57   C CB  . PRO A 1 172 ? -9.912  1.815   16.407  1.00 23.08 ? 172 PRO A CB  1 
ATOM   58   C CG  . PRO A 1 172 ? -9.345  3.152   16.748  1.00 23.88 ? 172 PRO A CG  1 
ATOM   59   C CD  . PRO A 1 172 ? -9.600  4.030   15.571  1.00 22.40 ? 172 PRO A CD  1 
ATOM   60   N N   . ASP A 1 173 ? -13.073 1.232   16.734  1.00 24.59 ? 173 ASP A N   1 
ATOM   61   C CA  . ASP A 1 173 ? -14.224 1.157   17.626  1.00 26.29 ? 173 ASP A CA  1 
ATOM   62   C C   . ASP A 1 173 ? -13.735 1.256   19.083  1.00 26.35 ? 173 ASP A C   1 
ATOM   63   O O   . ASP A 1 173 ? -14.452 1.803   19.911  1.00 27.87 ? 173 ASP A O   1 
ATOM   64   C CB  . ASP A 1 173 ? -14.950 -0.198  17.394  1.00 30.35 ? 173 ASP A CB  1 
ATOM   65   C CG  . ASP A 1 173 ? -16.202 -0.457  18.218  1.00 39.71 ? 173 ASP A CG  1 
ATOM   66   O OD1 . ASP A 1 173 ? -16.245 -1.494  18.924  1.00 41.20 ? 173 ASP A OD1 1 
ATOM   67   O OD2 . ASP A 1 173 ? -17.149 0.353   18.134  1.00 43.92 ? 173 ASP A OD2 1 
ATOM   68   N N   . ARG A 1 174 ? -12.554 0.696   19.412  1.00 25.32 ? 174 ARG A N   1 
ATOM   69   C CA  . ARG A 1 174 ? -11.984 0.719   20.768  1.00 25.71 ? 174 ARG A CA  1 
ATOM   70   C C   . ARG A 1 174 ? -10.479 0.840   20.709  1.00 25.05 ? 174 ARG A C   1 
ATOM   71   O O   . ARG A 1 174 ? -9.858  0.401   19.744  1.00 24.07 ? 174 ARG A O   1 
ATOM   72   C CB  . ARG A 1 174 ? -12.274 -0.607  21.517  1.00 27.76 ? 174 ARG A CB  1 
ATOM   73   C CG  . ARG A 1 174 ? -13.720 -0.889  21.840  1.00 31.88 ? 174 ARG A CG  1 
ATOM   74   C CD  . ARG A 1 174 ? -14.275 0.131   22.817  1.00 35.82 ? 174 ARG A CD  1 
ATOM   75   N NE  . ARG A 1 174 ? -14.083 -0.268  24.210  1.00 40.42 ? 174 ARG A NE  1 
ATOM   76   C CZ  . ARG A 1 174 ? -14.907 -1.068  24.881  1.00 43.76 ? 174 ARG A CZ  1 
ATOM   77   N NH1 . ARG A 1 174 ? -14.673 -1.353  26.156  1.00 42.76 ? 174 ARG A NH1 1 
ATOM   78   N NH2 . ARG A 1 174 ? -15.971 -1.593  24.280  1.00 43.95 ? 174 ARG A NH2 1 
ATOM   79   N N   . ILE A 1 175 ? -9.869  1.401   21.766  1.00 24.85 ? 175 ILE A N   1 
ATOM   80   C CA  . ILE A 1 175 ? -8.416  1.440   21.873  1.00 25.13 ? 175 ILE A CA  1 
ATOM   81   C C   . ILE A 1 175 ? -8.117  0.974   23.285  1.00 25.90 ? 175 ILE A C   1 
ATOM   82   O O   . ILE A 1 175 ? -8.492  1.661   24.235  1.00 27.08 ? 175 ILE A O   1 
ATOM   83   C CB  . ILE A 1 175 ? -7.793  2.836   21.604  1.00 25.63 ? 175 ILE A CB  1 
ATOM   84   C CG1 . ILE A 1 175 ? -8.118  3.305   20.159  1.00 26.02 ? 175 ILE A CG1 1 
ATOM   85   C CG2 . ILE A 1 175 ? -6.269  2.759   21.793  1.00 26.13 ? 175 ILE A CG2 1 
ATOM   86   C CD1 . ILE A 1 175 ? -7.638  4.681   19.803  1.00 26.93 ? 175 ILE A CD1 1 
ATOM   87   N N   . LEU A 1 176 ? -7.505  -0.201  23.428  1.00 24.50 ? 176 LEU A N   1 
ATOM   88   C CA  . LEU A 1 176 ? -7.179  -0.770  24.734  1.00 24.32 ? 176 LEU A CA  1 
ATOM   89   C C   . LEU A 1 176 ? -5.712  -0.575  25.031  1.00 24.33 ? 176 LEU A C   1 
ATOM   90   O O   . LEU A 1 176 ? -4.882  -0.703  24.132  1.00 23.79 ? 176 LEU A O   1 
ATOM   91   C CB  . LEU A 1 176 ? -7.501  -2.278  24.748  1.00 24.45 ? 176 LEU A CB  1 
ATOM   92   C CG  . LEU A 1 176 ? -8.918  -2.664  24.354  1.00 26.53 ? 176 LEU A CG  1 
ATOM   93   C CD1 . LEU A 1 176 ? -9.094  -4.190  24.369  1.00 26.96 ? 176 LEU A CD1 1 
ATOM   94   C CD2 . LEU A 1 176 ? -9.953  -1.981  25.245  1.00 27.82 ? 176 LEU A CD2 1 
ATOM   95   N N   . ASP A 1 177 ? -5.377  -0.295  26.300  1.00 24.63 ? 177 ASP A N   1 
ATOM   96   C CA  . ASP A 1 177 ? -3.975  -0.102  26.661  1.00 25.34 ? 177 ASP A CA  1 
ATOM   97   C C   . ASP A 1 177 ? -3.294  -1.474  26.680  1.00 25.65 ? 177 ASP A C   1 
ATOM   98   O O   . ASP A 1 177 ? -3.862  -2.441  27.155  1.00 26.95 ? 177 ASP A O   1 
ATOM   99   C CB  . ASP A 1 177 ? -3.847  0.602   28.031  1.00 28.20 ? 177 ASP A CB  1 
ATOM   100  C CG  . ASP A 1 177 ? -2.520  1.310   28.262  1.00 37.30 ? 177 ASP A CG  1 
ATOM   101  O OD1 . ASP A 1 177 ? -1.670  1.309   27.340  1.00 38.97 ? 177 ASP A OD1 1 
ATOM   102  O OD2 . ASP A 1 177 ? -2.328  1.868   29.366  1.00 41.30 ? 177 ASP A OD2 1 
ATOM   103  N N   . ALA A 1 178 ? -2.109  -1.574  26.120  1.00 25.06 ? 178 ALA A N   1 
ATOM   104  C CA  . ALA A 1 178 ? -1.324  -2.813  26.124  1.00 24.32 ? 178 ALA A CA  1 
ATOM   105  C C   . ALA A 1 178 ? 0.060   -2.485  26.716  1.00 23.58 ? 178 ALA A C   1 
ATOM   106  O O   . ALA A 1 178 ? 1.079   -2.638  26.052  1.00 22.95 ? 178 ALA A O   1 
ATOM   107  C CB  . ALA A 1 178 ? -1.192  -3.365  24.702  1.00 24.21 ? 178 ALA A CB  1 
ATOM   108  N N   . PRO A 1 179 ? 0.114   -2.046  27.988  1.00 23.78 ? 179 PRO A N   1 
ATOM   109  C CA  . PRO A 1 179 ? 1.410   -1.679  28.580  1.00 23.71 ? 179 PRO A CA  1 
ATOM   110  C C   . PRO A 1 179 ? 2.341   -2.867  28.662  1.00 23.78 ? 179 PRO A C   1 
ATOM   111  O O   . PRO A 1 179 ? 1.893   -3.969  28.966  1.00 24.35 ? 179 PRO A O   1 
ATOM   112  C CB  . PRO A 1 179 ? 1.024   -1.137  29.969  1.00 25.29 ? 179 PRO A CB  1 
ATOM   113  C CG  . PRO A 1 179 ? -0.282  -1.809  30.263  1.00 25.46 ? 179 PRO A CG  1 
ATOM   114  C CD  . PRO A 1 179 ? -0.985  -1.855  28.946  1.00 23.35 ? 179 PRO A CD  1 
ATOM   115  N N   . GLU A 1 180 ? 3.632   -2.645  28.381  1.00 24.30 ? 180 GLU A N   1 
ATOM   116  C CA  . GLU A 1 180 ? 4.689   -3.658  28.437  1.00 24.77 ? 180 GLU A CA  1 
ATOM   117  C C   . GLU A 1 180 ? 4.532   -4.787  27.406  1.00 24.39 ? 180 GLU A C   1 
ATOM   118  O O   . GLU A 1 180 ? 5.079   -5.882  27.590  1.00 24.91 ? 180 GLU A O   1 
ATOM   119  C CB  . GLU A 1 180 ? 4.857   -4.229  29.847  1.00 28.07 ? 180 GLU A CB  1 
ATOM   120  C CG  . GLU A 1 180 ? 5.106   -3.142  30.881  1.00 36.29 ? 180 GLU A CG  1 
ATOM   121  C CD  . GLU A 1 180 ? 5.600   -3.658  32.215  1.00 47.25 ? 180 GLU A CD  1 
ATOM   122  O OE1 . GLU A 1 180 ? 6.383   -4.636  32.217  1.00 50.83 ? 180 GLU A OE1 1 
ATOM   123  O OE2 . GLU A 1 180 ? 5.209   -3.083  33.257  1.00 49.95 ? 180 GLU A OE2 1 
ATOM   124  N N   . ILE A 1 181 ? 3.810   -4.533  26.293  1.00 23.86 ? 181 ILE A N   1 
ATOM   125  C CA  . ILE A 1 181 ? 3.718   -5.532  25.227  1.00 23.47 ? 181 ILE A CA  1 
ATOM   126  C C   . ILE A 1 181 ? 5.144   -5.753  24.651  1.00 24.12 ? 181 ILE A C   1 
ATOM   127  O O   . ILE A 1 181 ? 5.922   -4.790  24.546  1.00 24.57 ? 181 ILE A O   1 
ATOM   128  C CB  . ILE A 1 181 ? 2.669   -5.174  24.148  1.00 23.35 ? 181 ILE A CB  1 
ATOM   129  C CG1 . ILE A 1 181 ? 2.336   -6.411  23.284  1.00 23.48 ? 181 ILE A CG1 1 
ATOM   130  C CG2 . ILE A 1 181 ? 3.107   -3.961  23.308  1.00 23.65 ? 181 ILE A CG2 1 
ATOM   131  C CD1 . ILE A 1 181 ? 1.156   -6.218  22.374  1.00 24.04 ? 181 ILE A CD1 1 
ATOM   132  N N   . ARG A 1 182 ? 5.536   -7.016  24.475  1.00 23.51 ? 182 ARG A N   1 
ATOM   133  C CA  . ARG A 1 182 ? 6.888   -7.320  24.014  1.00 24.78 ? 182 ARG A CA  1 
ATOM   134  C C   . ARG A 1 182 ? 7.007   -7.031  22.523  1.00 24.07 ? 182 ARG A C   1 
ATOM   135  O O   . ARG A 1 182 ? 6.280   -7.602  21.726  1.00 23.69 ? 182 ARG A O   1 
ATOM   136  C CB  . ARG A 1 182 ? 7.266   -8.765  24.340  1.00 27.59 ? 182 ARG A CB  1 
ATOM   137  C CG  . ARG A 1 182 ? 8.718   -9.076  24.005  1.00 32.70 ? 182 ARG A CG  1 
ATOM   138  C CD  . ARG A 1 182 ? 9.174   -10.377 24.632  1.00 35.82 ? 182 ARG A CD  1 
ATOM   139  N NE  . ARG A 1 182 ? 9.277   -10.242 26.080  1.00 37.58 ? 182 ARG A NE  1 
ATOM   140  C CZ  . ARG A 1 182 ? 10.420  -10.115 26.746  1.00 36.44 ? 182 ARG A CZ  1 
ATOM   141  N NH1 . ARG A 1 182 ? 10.414  -9.983  28.060  1.00 35.83 ? 182 ARG A NH1 1 
ATOM   142  N NH2 . ARG A 1 182 ? 11.580  -10.165 26.105  1.00 35.23 ? 182 ARG A NH2 1 
ATOM   143  N N   . ASN A 1 183 ? 7.865   -6.088  22.165  1.00 23.56 ? 183 ASN A N   1 
ATOM   144  C CA  . ASN A 1 183 ? 8.048   -5.692  20.774  1.00 23.91 ? 183 ASN A CA  1 
ATOM   145  C C   . ASN A 1 183 ? 9.009   -6.668  20.091  1.00 24.95 ? 183 ASN A C   1 
ATOM   146  O O   . ASN A 1 183 ? 10.156  -6.321  19.781  1.00 26.12 ? 183 ASN A O   1 
ATOM   147  C CB  . ASN A 1 183 ? 8.567   -4.251  20.715  1.00 25.02 ? 183 ASN A CB  1 
ATOM   148  C CG  . ASN A 1 183 ? 8.703   -3.719  19.308  1.00 27.10 ? 183 ASN A CG  1 
ATOM   149  O OD1 . ASN A 1 183 ? 8.148   -4.270  18.364  1.00 27.20 ? 183 ASN A OD1 1 
ATOM   150  N ND2 . ASN A 1 183 ? 9.422   -2.612  19.150  1.00 27.57 ? 183 ASN A ND2 1 
ATOM   151  N N   . ASP A 1 184 ? 8.567   -7.910  19.949  1.00 24.08 ? 184 ASP A N   1 
ATOM   152  C CA  . ASP A 1 184 ? 9.337   -8.976  19.342  1.00 24.10 ? 184 ASP A CA  1 
ATOM   153  C C   . ASP A 1 184 ? 8.480   -9.469  18.198  1.00 24.09 ? 184 ASP A C   1 
ATOM   154  O O   . ASP A 1 184 ? 7.410   -10.018 18.430  1.00 23.57 ? 184 ASP A O   1 
ATOM   155  C CB  . ASP A 1 184 ? 9.568   -10.099 20.358  1.00 25.27 ? 184 ASP A CB  1 
ATOM   156  C CG  . ASP A 1 184 ? 10.501  -11.183 19.858  1.00 28.25 ? 184 ASP A CG  1 
ATOM   157  O OD1 . ASP A 1 184 ? 10.351  -11.603 18.698  1.00 28.35 ? 184 ASP A OD1 1 
ATOM   158  O OD2 . ASP A 1 184 ? 11.384  -11.603 20.625  1.00 30.89 ? 184 ASP A OD2 1 
ATOM   159  N N   . TYR A 1 185 ? 8.964   -9.281  16.955  1.00 23.82 ? 185 TYR A N   1 
ATOM   160  C CA  . TYR A 1 185 ? 8.206   -9.622  15.763  1.00 23.65 ? 185 TYR A CA  1 
ATOM   161  C C   . TYR A 1 185 ? 7.756   -11.078 15.695  1.00 22.20 ? 185 TYR A C   1 
ATOM   162  O O   . TYR A 1 185 ? 6.721   -11.362 15.121  1.00 23.21 ? 185 TYR A O   1 
ATOM   163  C CB  . TYR A 1 185 ? 9.091   -9.298  14.540  1.00 23.94 ? 185 TYR A CB  1 
ATOM   164  C CG  . TYR A 1 185 ? 8.380   -9.387  13.210  1.00 25.08 ? 185 TYR A CG  1 
ATOM   165  C CD1 . TYR A 1 185 ? 7.549   -8.365  12.775  1.00 26.62 ? 185 TYR A CD1 1 
ATOM   166  C CD2 . TYR A 1 185 ? 8.545   -10.489 12.382  1.00 25.95 ? 185 TYR A CD2 1 
ATOM   167  C CE1 . TYR A 1 185 ? 6.913   -8.430  11.541  1.00 26.92 ? 185 TYR A CE1 1 
ATOM   168  C CE2 . TYR A 1 185 ? 7.932   -10.555 11.137  1.00 26.71 ? 185 TYR A CE2 1 
ATOM   169  C CZ  . TYR A 1 185 ? 7.088   -9.539  10.738  1.00 27.41 ? 185 TYR A CZ  1 
ATOM   170  O OH  . TYR A 1 185 ? 6.492   -9.581  9.515   1.00 27.48 ? 185 TYR A OH  1 
ATOM   171  N N   . TYR A 1 186 ? 8.543   -12.007 16.240  1.00 19.86 ? 186 TYR A N   1 
ATOM   172  C CA  . TYR A 1 186 ? 8.267   -13.443 16.077  1.00 19.73 ? 186 TYR A CA  1 
ATOM   173  C C   . TYR A 1 186 ? 7.200   -14.015 17.017  1.00 19.34 ? 186 TYR A C   1 
ATOM   174  O O   . TYR A 1 186 ? 6.798   -15.170 16.844  1.00 20.24 ? 186 TYR A O   1 
ATOM   175  C CB  . TYR A 1 186 ? 9.567   -14.227 16.202  1.00 20.63 ? 186 TYR A CB  1 
ATOM   176  C CG  . TYR A 1 186 ? 10.589  -13.707 15.211  1.00 22.63 ? 186 TYR A CG  1 
ATOM   177  C CD1 . TYR A 1 186 ? 10.544  -14.086 13.881  1.00 24.42 ? 186 TYR A CD1 1 
ATOM   178  C CD2 . TYR A 1 186 ? 11.475  -12.695 15.565  1.00 25.39 ? 186 TYR A CD2 1 
ATOM   179  C CE1 . TYR A 1 186 ? 11.431  -13.559 12.948  1.00 25.97 ? 186 TYR A CE1 1 
ATOM   180  C CE2 . TYR A 1 186 ? 12.358  -12.153 14.642  1.00 26.68 ? 186 TYR A CE2 1 
ATOM   181  C CZ  . TYR A 1 186 ? 12.339  -12.595 13.332  1.00 27.39 ? 186 TYR A CZ  1 
ATOM   182  O OH  . TYR A 1 186 ? 13.244  -12.099 12.411  1.00 30.59 ? 186 TYR A OH  1 
ATOM   183  N N   . LEU A 1 187 ? 6.792   -13.242 18.011  1.00 17.16 ? 187 LEU A N   1 
ATOM   184  C CA  . LEU A 1 187 ? 5.795   -13.720 18.973  1.00 16.83 ? 187 LEU A CA  1 
ATOM   185  C C   . LEU A 1 187 ? 4.347   -13.565 18.508  1.00 17.09 ? 187 LEU A C   1 
ATOM   186  O O   . LEU A 1 187 ? 4.060   -12.728 17.662  1.00 17.87 ? 187 LEU A O   1 
ATOM   187  C CB  . LEU A 1 187 ? 6.000   -13.041 20.325  1.00 16.73 ? 187 LEU A CB  1 
ATOM   188  C CG  . LEU A 1 187 ? 7.407   -13.144 20.891  1.00 19.99 ? 187 LEU A CG  1 
ATOM   189  C CD1 . LEU A 1 187 ? 7.477   -12.465 22.245  1.00 20.35 ? 187 LEU A CD1 1 
ATOM   190  C CD2 . LEU A 1 187 ? 7.889   -14.635 20.943  1.00 21.14 ? 187 LEU A CD2 1 
ATOM   191  N N   . ASN A 1 188 ? 3.415   -14.374 19.064  1.00 15.48 ? 188 ASN A N   1 
ATOM   192  C CA  . ASN A 1 188 ? 2.010   -14.293 18.634  1.00 13.84 ? 188 ASN A CA  1 
ATOM   193  C C   . ASN A 1 188 ? 1.201   -14.073 19.932  1.00 14.44 ? 188 ASN A C   1 
ATOM   194  O O   . ASN A 1 188 ? 0.728   -15.014 20.568  1.00 15.74 ? 188 ASN A O   1 
ATOM   195  C CB  . ASN A 1 188 ? 1.646   -15.597 17.917  1.00 14.84 ? 188 ASN A CB  1 
ATOM   196  C CG  . ASN A 1 188 ? 2.243   -15.656 16.512  1.00 16.34 ? 188 ASN A CG  1 
ATOM   197  O OD1 . ASN A 1 188 ? 1.701   -15.084 15.554  1.00 18.71 ? 188 ASN A OD1 1 
ATOM   198  N ND2 . ASN A 1 188 ? 3.365   -16.311 16.362  1.00 16.24 ? 188 ASN A ND2 1 
ATOM   199  N N   . LEU A 1 189 ? 1.091   -12.828 20.317  1.00 13.64 ? 189 LEU A N   1 
ATOM   200  C CA  . LEU A 1 189 ? 0.616   -12.432 21.647  1.00 15.14 ? 189 LEU A CA  1 
ATOM   201  C C   . LEU A 1 189 ? -0.859  -12.129 21.840  1.00 15.01 ? 189 LEU A C   1 
ATOM   202  O O   . LEU A 1 189 ? -1.241  -11.824 22.975  1.00 15.32 ? 189 LEU A O   1 
ATOM   203  C CB  . LEU A 1 189 ? 1.423   -11.200 22.088  1.00 16.87 ? 189 LEU A CB  1 
ATOM   204  C CG  . LEU A 1 189 ? 2.969   -11.393 22.099  1.00 20.74 ? 189 LEU A CG  1 
ATOM   205  C CD1 . LEU A 1 189 ? 3.692   -10.076 22.282  1.00 22.66 ? 189 LEU A CD1 1 
ATOM   206  C CD2 . LEU A 1 189 ? 3.394   -12.421 23.119  1.00 21.52 ? 189 LEU A CD2 1 
ATOM   207  N N   A VAL A 1 190 ? -1.692  -12.208 20.782  0.63 14.81 ? 190 VAL A N   1 
ATOM   208  N N   B VAL A 1 190 ? -1.687  -12.227 20.788  0.37 14.66 ? 190 VAL A N   1 
ATOM   209  C CA  A VAL A 1 190 ? -3.118  -11.929 20.941  0.63 14.74 ? 190 VAL A CA  1 
ATOM   210  C CA  B VAL A 1 190 ? -3.103  -11.907 20.933  0.37 14.57 ? 190 VAL A CA  1 
ATOM   211  C C   A VAL A 1 190 ? -3.968  -12.973 20.216  0.63 14.13 ? 190 VAL A C   1 
ATOM   212  C C   B VAL A 1 190 ? -4.005  -12.885 20.170  0.37 14.10 ? 190 VAL A C   1 
ATOM   213  O O   A VAL A 1 190 ? -3.577  -13.497 19.161  0.63 13.93 ? 190 VAL A O   1 
ATOM   214  O O   B VAL A 1 190 ? -3.657  -13.325 19.070  0.37 14.00 ? 190 VAL A O   1 
ATOM   215  C CB  A VAL A 1 190 ? -3.529  -10.492 20.481  0.63 15.68 ? 190 VAL A CB  1 
ATOM   216  C CB  B VAL A 1 190 ? -3.362  -10.424 20.545  0.37 15.40 ? 190 VAL A CB  1 
ATOM   217  C CG1 A VAL A 1 190 ? -2.796  -9.402  21.268  0.63 15.45 ? 190 VAL A CG1 1 
ATOM   218  C CG1 B VAL A 1 190 ? -2.962  -10.143 19.094  0.37 16.16 ? 190 VAL A CG1 1 
ATOM   219  C CG2 A VAL A 1 190 ? -3.337  -10.304 18.969  0.63 16.13 ? 190 VAL A CG2 1 
ATOM   220  C CG2 B VAL A 1 190 ? -4.809  -10.022 20.798  0.37 15.21 ? 190 VAL A CG2 1 
ATOM   221  N N   . ASP A 1 191 ? -5.158  -13.242 20.765  1.00 13.46 ? 191 ASP A N   1 
ATOM   222  C CA  . ASP A 1 191 ? -6.094  -14.142 20.103  1.00 13.19 ? 191 ASP A CA  1 
ATOM   223  C C   . ASP A 1 191 ? -7.486  -13.887 20.634  1.00 13.74 ? 191 ASP A C   1 
ATOM   224  O O   . ASP A 1 191 ? -7.644  -13.716 21.842  1.00 13.14 ? 191 ASP A O   1 
ATOM   225  C CB  . ASP A 1 191 ? -5.696  -15.626 20.302  1.00 14.12 ? 191 ASP A CB  1 
ATOM   226  C CG  . ASP A 1 191 ? -6.398  -16.543 19.291  1.00 17.63 ? 191 ASP A CG  1 
ATOM   227  O OD1 . ASP A 1 191 ? -6.757  -16.055 18.184  1.00 19.75 ? 191 ASP A OD1 1 
ATOM   228  O OD2 . ASP A 1 191 ? -6.588  -17.741 19.602  1.00 17.59 ? 191 ASP A OD2 1 
ATOM   229  N N   . TRP A 1 192 ? -8.484  -13.879 19.725  1.00 14.19 ? 192 TRP A N   1 
ATOM   230  C CA  . TRP A 1 192 ? -9.878  -13.591 20.075  1.00 14.58 ? 192 TRP A CA  1 
ATOM   231  C C   . TRP A 1 192 ? -10.643 -14.917 20.048  1.00 15.20 ? 192 TRP A C   1 
ATOM   232  O O   . TRP A 1 192 ? -10.642 -15.615 19.032  1.00 16.09 ? 192 TRP A O   1 
ATOM   233  C CB  . TRP A 1 192 ? -10.465 -12.625 19.027  1.00 14.84 ? 192 TRP A CB  1 
ATOM   234  C CG  . TRP A 1 192 ? -11.591 -11.762 19.534  1.00 15.95 ? 192 TRP A CG  1 
ATOM   235  C CD1 . TRP A 1 192 ? -12.599 -12.126 20.387  1.00 17.24 ? 192 TRP A CD1 1 
ATOM   236  C CD2 . TRP A 1 192 ? -11.787 -10.370 19.244  1.00 16.74 ? 192 TRP A CD2 1 
ATOM   237  N NE1 . TRP A 1 192 ? -13.425 -11.038 20.636  1.00 17.62 ? 192 TRP A NE1 1 
ATOM   238  C CE2 . TRP A 1 192 ? -12.967 -9.961  19.910  1.00 17.70 ? 192 TRP A CE2 1 
ATOM   239  C CE3 . TRP A 1 192 ? -11.123 -9.450  18.417  1.00 17.26 ? 192 TRP A CE3 1 
ATOM   240  C CZ2 . TRP A 1 192 ? -13.439 -8.648  19.844  1.00 18.12 ? 192 TRP A CZ2 1 
ATOM   241  C CZ3 . TRP A 1 192 ? -11.598 -8.150  18.347  1.00 17.91 ? 192 TRP A CZ3 1 
ATOM   242  C CH2 . TRP A 1 192 ? -12.767 -7.775  19.021  1.00 18.07 ? 192 TRP A CH2 1 
ATOM   243  N N   . SER A 1 193 ? -11.254 -15.282 21.168  1.00 15.03 ? 193 SER A N   1 
ATOM   244  C CA  . SER A 1 193 ? -11.920 -16.556 21.289  1.00 16.38 ? 193 SER A CA  1 
ATOM   245  C C   . SER A 1 193 ? -13.261 -16.601 20.627  1.00 18.31 ? 193 SER A C   1 
ATOM   246  O O   . SER A 1 193 ? -13.917 -15.566 20.496  1.00 18.83 ? 193 SER A O   1 
ATOM   247  C CB  . SER A 1 193 ? -12.085 -16.909 22.766  1.00 16.15 ? 193 SER A CB  1 
ATOM   248  O OG  . SER A 1 193 ? -13.270 -16.346 23.316  1.00 17.05 ? 193 SER A OG  1 
ATOM   249  N N   . SER A 1 194 ? -13.760 -17.822 20.378  1.00 18.75 ? 194 SER A N   1 
ATOM   250  C CA  . SER A 1 194 ? -15.110 -18.000 19.866  1.00 20.68 ? 194 SER A CA  1 
ATOM   251  C C   . SER A 1 194 ? -16.181 -17.502 20.863  1.00 21.84 ? 194 SER A C   1 
ATOM   252  O O   . SER A 1 194 ? -17.331 -17.298 20.454  1.00 24.12 ? 194 SER A O   1 
ATOM   253  C CB  . SER A 1 194 ? -15.351 -19.472 19.538  1.00 22.55 ? 194 SER A CB  1 
ATOM   254  O OG  . SER A 1 194 ? -15.255 -20.252 20.718  1.00 23.40 ? 194 SER A OG  1 
ATOM   255  N N   . GLY A 1 195 ? -15.819 -17.364 22.152  1.00 20.36 ? 195 GLY A N   1 
ATOM   256  C CA  . GLY A 1 195 ? -16.674 -16.842 23.216  1.00 20.39 ? 195 GLY A CA  1 
ATOM   257  C C   . GLY A 1 195 ? -16.579 -15.333 23.365  1.00 19.89 ? 195 GLY A C   1 
ATOM   258  O O   . GLY A 1 195 ? -17.030 -14.778 24.365  1.00 20.83 ? 195 GLY A O   1 
ATOM   259  N N   . ASN A 1 196 ? -15.900 -14.658 22.408  1.00 18.65 ? 196 ASN A N   1 
ATOM   260  C CA  . ASN A 1 196 ? -15.789 -13.204 22.364  1.00 18.86 ? 196 ASN A CA  1 
ATOM   261  C C   . ASN A 1 196 ? -14.904 -12.638 23.467  1.00 18.73 ? 196 ASN A C   1 
ATOM   262  O O   . ASN A 1 196 ? -15.166 -11.563 23.997  1.00 18.99 ? 196 ASN A O   1 
ATOM   263  C CB  . ASN A 1 196 ? -17.186 -12.550 22.344  1.00 20.11 ? 196 ASN A CB  1 
ATOM   264  C CG  . ASN A 1 196 ? -17.175 -11.178 21.725  1.00 24.11 ? 196 ASN A CG  1 
ATOM   265  O OD1 . ASN A 1 196 ? -16.284 -10.845 20.936  1.00 22.96 ? 196 ASN A OD1 1 
ATOM   266  N ND2 . ASN A 1 196 ? -18.172 -10.360 22.084  1.00 26.15 ? 196 ASN A ND2 1 
ATOM   267  N N   . VAL A 1 197 ? -13.837 -13.372 23.802  1.00 17.57 ? 197 VAL A N   1 
ATOM   268  C CA  . VAL A 1 197 ? -12.898 -12.920 24.823  1.00 16.85 ? 197 VAL A CA  1 
ATOM   269  C C   . VAL A 1 197 ? -11.524 -12.772 24.163  1.00 16.45 ? 197 VAL A C   1 
ATOM   270  O O   . VAL A 1 197 ? -11.039 -13.737 23.570  1.00 16.18 ? 197 VAL A O   1 
ATOM   271  C CB  . VAL A 1 197 ? -12.829 -13.937 25.987  1.00 18.44 ? 197 VAL A CB  1 
ATOM   272  C CG1 . VAL A 1 197 ? -11.770 -13.513 27.010  1.00 19.24 ? 197 VAL A CG1 1 
ATOM   273  C CG2 . VAL A 1 197 ? -14.182 -14.103 26.677  1.00 19.12 ? 197 VAL A CG2 1 
ATOM   274  N N   . LEU A 1 198 ? -10.873 -11.605 24.314  1.00 15.82 ? 198 LEU A N   1 
ATOM   275  C CA  . LEU A 1 198 ? -9.530  -11.382 23.772  1.00 15.49 ? 198 LEU A CA  1 
ATOM   276  C C   . LEU A 1 198 ? -8.533  -11.793 24.831  1.00 15.61 ? 198 LEU A C   1 
ATOM   277  O O   . LEU A 1 198 ? -8.679  -11.414 25.988  1.00 16.76 ? 198 LEU A O   1 
ATOM   278  C CB  . LEU A 1 198 ? -9.301  -9.878  23.534  1.00 16.53 ? 198 LEU A CB  1 
ATOM   279  C CG  . LEU A 1 198 ? -9.394  -9.344  22.143  1.00 19.34 ? 198 LEU A CG  1 
ATOM   280  C CD1 . LEU A 1 198 ? -9.104  -7.837  22.138  1.00 21.36 ? 198 LEU A CD1 1 
ATOM   281  C CD2 . LEU A 1 198 ? -8.427  -10.061 21.188  1.00 18.22 ? 198 LEU A CD2 1 
ATOM   282  N N   . ALA A 1 199 ? -7.519  -12.554 24.450  1.00 14.19 ? 199 ALA A N   1 
ATOM   283  C CA  . ALA A 1 199 ? -6.443  -12.962 25.335  1.00 14.74 ? 199 ALA A CA  1 
ATOM   284  C C   . ALA A 1 199 ? -5.250  -12.130 24.883  1.00 14.55 ? 199 ALA A C   1 
ATOM   285  O O   . ALA A 1 199 ? -4.911  -12.124 23.691  1.00 14.55 ? 199 ALA A O   1 
ATOM   286  C CB  . ALA A 1 199 ? -6.155  -14.445 25.141  1.00 15.28 ? 199 ALA A CB  1 
ATOM   287  N N   . VAL A 1 200 ? -4.640  -11.407 25.808  1.00 15.06 ? 200 VAL A N   1 
ATOM   288  C CA  . VAL A 1 200 ? -3.541  -10.513 25.478  1.00 17.12 ? 200 VAL A CA  1 
ATOM   289  C C   . VAL A 1 200 ? -2.347  -10.803 26.369  1.00 16.98 ? 200 VAL A C   1 
ATOM   290  O O   . VAL A 1 200 ? -2.467  -10.667 27.576  1.00 17.52 ? 200 VAL A O   1 
ATOM   291  C CB  . VAL A 1 200 ? -3.976  -9.029  25.652  1.00 19.03 ? 200 VAL A CB  1 
ATOM   292  C CG1 . VAL A 1 200 ? -2.884  -8.093  25.140  1.00 20.18 ? 200 VAL A CG1 1 
ATOM   293  C CG2 . VAL A 1 200 ? -5.320  -8.736  24.960  1.00 20.71 ? 200 VAL A CG2 1 
ATOM   294  N N   . ALA A 1 201 ? -1.198  -11.161 25.785  1.00 16.32 ? 201 ALA A N   1 
ATOM   295  C CA  . ALA A 1 201 ? 0.001   -11.399 26.573  1.00 17.53 ? 201 ALA A CA  1 
ATOM   296  C C   . ALA A 1 201 ? 0.793   -10.101 26.716  1.00 17.94 ? 201 ALA A C   1 
ATOM   297  O O   . ALA A 1 201 ? 1.270   -9.545  25.726  1.00 17.59 ? 201 ALA A O   1 
ATOM   298  C CB  . ALA A 1 201 ? 0.852   -12.460 25.919  1.00 19.10 ? 201 ALA A CB  1 
ATOM   299  N N   . LEU A 1 202 ? 0.925   -9.615  27.952  1.00 17.67 ? 202 LEU A N   1 
ATOM   300  C CA  . LEU A 1 202 ? 1.688   -8.412  28.227  1.00 18.81 ? 202 LEU A CA  1 
ATOM   301  C C   . LEU A 1 202 ? 2.867   -8.766  29.129  1.00 20.06 ? 202 LEU A C   1 
ATOM   302  O O   . LEU A 1 202 ? 2.706   -8.929  30.348  1.00 20.01 ? 202 LEU A O   1 
ATOM   303  C CB  . LEU A 1 202 ? 0.808   -7.335  28.880  1.00 19.44 ? 202 LEU A CB  1 
ATOM   304  C CG  . LEU A 1 202 ? -0.403  -6.912  28.052  1.00 19.85 ? 202 LEU A CG  1 
ATOM   305  C CD1 . LEU A 1 202 ? -1.251  -5.916  28.801  1.00 20.22 ? 202 LEU A CD1 1 
ATOM   306  C CD2 . LEU A 1 202 ? 0.009   -6.349  26.708  1.00 20.26 ? 202 LEU A CD2 1 
ATOM   307  N N   . ASP A 1 203 ? 4.048   -8.906  28.506  1.00 20.88 ? 203 ASP A N   1 
ATOM   308  C CA  . ASP A 1 203 ? 5.290   -9.273  29.194  1.00 21.44 ? 203 ASP A CA  1 
ATOM   309  C C   . ASP A 1 203 ? 5.133   -10.669 29.844  1.00 20.59 ? 203 ASP A C   1 
ATOM   310  O O   . ASP A 1 203 ? 5.066   -11.644 29.095  1.00 20.19 ? 203 ASP A O   1 
ATOM   311  C CB  . ASP A 1 203 ? 5.800   -8.173  30.151  1.00 24.67 ? 203 ASP A CB  1 
ATOM   312  C CG  . ASP A 1 203 ? 7.115   -8.531  30.842  1.00 33.26 ? 203 ASP A CG  1 
ATOM   313  O OD1 . ASP A 1 203 ? 7.951   -9.225  30.214  1.00 33.27 ? 203 ASP A OD1 1 
ATOM   314  O OD2 . ASP A 1 203 ? 7.294   -8.138  32.016  1.00 38.10 ? 203 ASP A OD2 1 
ATOM   315  N N   . ASN A 1 204 ? 5.021   -10.778 31.196  1.00 20.62 ? 204 ASN A N   1 
ATOM   316  C CA  . ASN A 1 204 ? 4.907   -12.076 31.837  1.00 21.12 ? 204 ASN A CA  1 
ATOM   317  C C   . ASN A 1 204 ? 3.489   -12.423 32.274  1.00 21.41 ? 204 ASN A C   1 
ATOM   318  O O   . ASN A 1 204 ? 3.330   -13.343 33.064  1.00 22.63 ? 204 ASN A O   1 
ATOM   319  C CB  . ASN A 1 204 ? 5.850   -12.160 33.055  1.00 24.08 ? 204 ASN A CB  1 
ATOM   320  C CG  . ASN A 1 204 ? 5.498   -11.198 34.166  1.00 27.96 ? 204 ASN A CG  1 
ATOM   321  O OD1 . ASN A 1 204 ? 4.682   -10.289 33.983  1.00 29.09 ? 204 ASN A OD1 1 
ATOM   322  N ND2 . ASN A 1 204 ? 6.111   -11.374 35.352  1.00 29.34 ? 204 ASN A ND2 1 
ATOM   323  N N   . SER A 1 205 ? 2.485   -11.671 31.844  1.00 19.93 ? 205 SER A N   1 
ATOM   324  C CA  . SER A 1 205 ? 1.096   -11.923 32.240  1.00 19.43 ? 205 SER A CA  1 
ATOM   325  C C   . SER A 1 205 ? 0.191   -12.101 31.035  1.00 19.08 ? 205 SER A C   1 
ATOM   326  O O   . SER A 1 205 ? 0.507   -11.631 29.933  1.00 19.16 ? 205 SER A O   1 
ATOM   327  C CB  . SER A 1 205 ? 0.570   -10.762 33.083  1.00 21.27 ? 205 SER A CB  1 
ATOM   328  O OG  . SER A 1 205 ? 1.205   -10.684 34.352  1.00 24.81 ? 205 SER A OG  1 
ATOM   329  N N   . VAL A 1 206 ? -0.934  -12.787 31.238  1.00 17.15 ? 206 VAL A N   1 
ATOM   330  C CA  . VAL A 1 206 ? -1.949  -12.906 30.191  1.00 16.39 ? 206 VAL A CA  1 
ATOM   331  C C   . VAL A 1 206 ? -3.183  -12.246 30.770  1.00 16.93 ? 206 VAL A C   1 
ATOM   332  O O   . VAL A 1 206 ? -3.607  -12.594 31.874  1.00 16.82 ? 206 VAL A O   1 
ATOM   333  C CB  . VAL A 1 206 ? -2.228  -14.365 29.744  1.00 16.29 ? 206 VAL A CB  1 
ATOM   334  C CG1 . VAL A 1 206 ? -3.407  -14.420 28.756  1.00 16.77 ? 206 VAL A CG1 1 
ATOM   335  C CG2 . VAL A 1 206 ? -0.971  -14.963 29.094  1.00 16.18 ? 206 VAL A CG2 1 
ATOM   336  N N   . TYR A 1 207 ? -3.777  -11.313 30.029  1.00 16.88 ? 207 TYR A N   1 
ATOM   337  C CA  . TYR A 1 207 ? -4.998  -10.643 30.443  1.00 16.90 ? 207 TYR A CA  1 
ATOM   338  C C   . TYR A 1 207 ? -6.124  -11.084 29.513  1.00 16.28 ? 207 TYR A C   1 
ATOM   339  O O   . TYR A 1 207 ? -5.895  -11.289 28.313  1.00 15.88 ? 207 TYR A O   1 
ATOM   340  C CB  . TYR A 1 207 ? -4.834  -9.115  30.342  1.00 17.61 ? 207 TYR A CB  1 
ATOM   341  C CG  . TYR A 1 207 ? -4.017  -8.571  31.481  1.00 19.95 ? 207 TYR A CG  1 
ATOM   342  C CD1 . TYR A 1 207 ? -2.632  -8.536  31.412  1.00 21.42 ? 207 TYR A CD1 1 
ATOM   343  C CD2 . TYR A 1 207 ? -4.624  -8.153  32.660  1.00 21.70 ? 207 TYR A CD2 1 
ATOM   344  C CE1 . TYR A 1 207 ? -1.872  -8.066  32.472  1.00 23.57 ? 207 TYR A CE1 1 
ATOM   345  C CE2 . TYR A 1 207 ? -3.873  -7.667  33.720  1.00 23.27 ? 207 TYR A CE2 1 
ATOM   346  C CZ  . TYR A 1 207 ? -2.495  -7.670  33.637  1.00 25.34 ? 207 TYR A CZ  1 
ATOM   347  O OH  . TYR A 1 207 ? -1.755  -7.159  34.681  1.00 30.15 ? 207 TYR A OH  1 
ATOM   348  N N   . LEU A 1 208 ? -7.324  -11.214 30.052  1.00 15.66 ? 208 LEU A N   1 
ATOM   349  C CA  . LEU A 1 208 ? -8.492  -11.541 29.253  1.00 16.54 ? 208 LEU A CA  1 
ATOM   350  C C   . LEU A 1 208 ? -9.413  -10.351 29.289  1.00 18.16 ? 208 LEU A C   1 
ATOM   351  O O   . LEU A 1 208 ? -9.735  -9.863  30.366  1.00 19.44 ? 208 LEU A O   1 
ATOM   352  C CB  . LEU A 1 208 ? -9.233  -12.745 29.827  1.00 16.69 ? 208 LEU A CB  1 
ATOM   353  C CG  . LEU A 1 208 ? -8.404  -14.002 30.026  1.00 17.38 ? 208 LEU A CG  1 
ATOM   354  C CD1 . LEU A 1 208 ? -9.279  -15.112 30.607  1.00 18.24 ? 208 LEU A CD1 1 
ATOM   355  C CD2 . LEU A 1 208 ? -7.761  -14.454 28.699  1.00 17.18 ? 208 LEU A CD2 1 
ATOM   356  N N   . TRP A 1 209 ? -9.896  -9.926  28.127  1.00 18.02 ? 209 TRP A N   1 
ATOM   357  C CA  . TRP A 1 209 ? -10.835 -8.828  28.016  1.00 19.07 ? 209 TRP A CA  1 
ATOM   358  C C   . TRP A 1 209 ? -12.110 -9.380  27.353  1.00 19.78 ? 209 TRP A C   1 
ATOM   359  O O   . TRP A 1 209 ? -12.081 -9.841  26.206  1.00 18.43 ? 209 TRP A O   1 
ATOM   360  C CB  . TRP A 1 209 ? -10.205 -7.678  27.213  1.00 19.59 ? 209 TRP A CB  1 
ATOM   361  C CG  . TRP A 1 209 ? -11.100 -6.506  26.958  1.00 21.33 ? 209 TRP A CG  1 
ATOM   362  C CD1 . TRP A 1 209 ? -11.358 -5.467  27.806  1.00 23.06 ? 209 TRP A CD1 1 
ATOM   363  C CD2 . TRP A 1 209 ? -11.798 -6.213  25.740  1.00 21.41 ? 209 TRP A CD2 1 
ATOM   364  N NE1 . TRP A 1 209 ? -12.207 -4.566  27.205  1.00 23.71 ? 209 TRP A NE1 1 
ATOM   365  C CE2 . TRP A 1 209 ? -12.483 -4.995  25.931  1.00 23.00 ? 209 TRP A CE2 1 
ATOM   366  C CE3 . TRP A 1 209 ? -11.884 -6.847  24.495  1.00 21.83 ? 209 TRP A CE3 1 
ATOM   367  C CZ2 . TRP A 1 209 ? -13.268 -4.418  24.933  1.00 23.36 ? 209 TRP A CZ2 1 
ATOM   368  C CZ3 . TRP A 1 209 ? -12.656 -6.267  23.510  1.00 22.85 ? 209 TRP A CZ3 1 
ATOM   369  C CH2 . TRP A 1 209 ? -13.349 -5.074  23.741  1.00 23.30 ? 209 TRP A CH2 1 
ATOM   370  N N   . SER A 1 210 ? -13.238 -9.304  28.062  1.00 20.95 ? 210 SER A N   1 
ATOM   371  C CA  . SER A 1 210 ? -14.508 -9.788  27.535  1.00 23.12 ? 210 SER A CA  1 
ATOM   372  C C   . SER A 1 210 ? -15.089 -8.669  26.713  1.00 24.77 ? 210 SER A C   1 
ATOM   373  O O   . SER A 1 210 ? -15.413 -7.621  27.269  1.00 25.36 ? 210 SER A O   1 
ATOM   374  C CB  . SER A 1 210 ? -15.450 -10.175 28.671  1.00 26.92 ? 210 SER A CB  1 
ATOM   375  O OG  . SER A 1 210 ? -14.848 -11.188 29.472  1.00 32.00 ? 210 SER A OG  1 
ATOM   376  N N   . ALA A 1 211 ? -15.203 -8.858  25.403  1.00 24.87 ? 211 ALA A N   1 
ATOM   377  C CA  . ALA A 1 211 ? -15.672 -7.788  24.517  1.00 26.37 ? 211 ALA A CA  1 
ATOM   378  C C   . ALA A 1 211 ? -17.055 -7.261  24.824  1.00 29.06 ? 211 ALA A C   1 
ATOM   379  O O   . ALA A 1 211 ? -17.266 -6.052  24.690  1.00 30.75 ? 211 ALA A O   1 
ATOM   380  C CB  . ALA A 1 211 ? -15.583 -8.218  23.063  1.00 26.73 ? 211 ALA A CB  1 
ATOM   381  N N   . SER A 1 212 ? -17.988 -8.126  25.255  1.00 28.94 ? 212 SER A N   1 
ATOM   382  C CA  . SER A 1 212 ? -19.347 -7.664  25.514  1.00 30.75 ? 212 SER A CA  1 
ATOM   383  C C   . SER A 1 212 ? -19.496 -6.883  26.812  1.00 31.30 ? 212 SER A C   1 
ATOM   384  O O   . SER A 1 212 ? -20.339 -5.971  26.877  1.00 32.09 ? 212 SER A O   1 
ATOM   385  C CB  . SER A 1 212 ? -20.343 -8.817  25.442  1.00 33.52 ? 212 SER A CB  1 
ATOM   386  O OG  . SER A 1 212 ? -20.170 -9.753  26.492  1.00 37.61 ? 212 SER A OG  1 
ATOM   387  N N   . SER A 1 213 ? -18.694 -7.209  27.851  1.00 30.22 ? 213 SER A N   1 
ATOM   388  C CA  . SER A 1 213 ? -18.852 -6.499  29.122  1.00 29.77 ? 213 SER A CA  1 
ATOM   389  C C   . SER A 1 213 ? -17.761 -5.502  29.453  1.00 29.28 ? 213 SER A C   1 
ATOM   390  O O   . SER A 1 213 ? -17.977 -4.624  30.290  1.00 29.16 ? 213 SER A O   1 
ATOM   391  C CB  . SER A 1 213 ? -19.001 -7.483  30.273  1.00 30.25 ? 213 SER A CB  1 
ATOM   392  O OG  . SER A 1 213 ? -17.833 -8.280  30.371  1.00 31.33 ? 213 SER A OG  1 
ATOM   393  N N   . GLY A 1 214 ? -16.589 -5.673  28.860  1.00 27.91 ? 214 GLY A N   1 
ATOM   394  C CA  . GLY A 1 214 ? -15.433 -4.862  29.212  1.00 27.27 ? 214 GLY A CA  1 
ATOM   395  C C   . GLY A 1 214 ? -14.682 -5.379  30.442  1.00 27.14 ? 214 GLY A C   1 
ATOM   396  O O   . GLY A 1 214 ? -13.721 -4.742  30.882  1.00 28.64 ? 214 GLY A O   1 
ATOM   397  N N   A ASP A 1 215 ? -15.115 -6.514  31.025  0.57 26.27 ? 215 ASP A N   1 
ATOM   398  N N   B ASP A 1 215 ? -15.077 -6.557  30.969  0.43 26.09 ? 215 ASP A N   1 
ATOM   399  C CA  A ASP A 1 215 ? -14.449 -7.071  32.200  0.57 25.82 ? 215 ASP A CA  1 
ATOM   400  C CA  B ASP A 1 215 ? -14.455 -7.210  32.121  0.43 25.51 ? 215 ASP A CA  1 
ATOM   401  C C   A ASP A 1 215 ? -13.043 -7.552  31.831  0.57 25.22 ? 215 ASP A C   1 
ATOM   402  C C   B ASP A 1 215 ? -13.005 -7.567  31.790  0.43 25.11 ? 215 ASP A C   1 
ATOM   403  O O   A ASP A 1 215 ? -12.839 -8.108  30.753  0.57 24.91 ? 215 ASP A O   1 
ATOM   404  O O   B ASP A 1 215 ? -12.738 -8.082  30.707  0.43 24.89 ? 215 ASP A O   1 
ATOM   405  C CB  A ASP A 1 215 ? -15.267 -8.214  32.804  0.57 27.49 ? 215 ASP A CB  1 
ATOM   406  C CB  B ASP A 1 215 ? -15.224 -8.500  32.444  0.43 26.43 ? 215 ASP A CB  1 
ATOM   407  C CG  A ASP A 1 215 ? -16.582 -7.786  33.431  0.57 31.90 ? 215 ASP A CG  1 
ATOM   408  C CG  B ASP A 1 215 ? -14.678 -9.297  33.611  0.43 29.33 ? 215 ASP A CG  1 
ATOM   409  O OD1 A ASP A 1 215 ? -16.768 -6.567  33.662  0.57 32.07 ? 215 ASP A OD1 1 
ATOM   410  O OD1 B ASP A 1 215 ? -15.079 -9.014  34.758  0.43 29.08 ? 215 ASP A OD1 1 
ATOM   411  O OD2 A ASP A 1 215 ? -17.425 -8.665  33.685  0.57 34.77 ? 215 ASP A OD2 1 
ATOM   412  O OD2 B ASP A 1 215 ? -13.859 -10.221 33.373  0.43 30.77 ? 215 ASP A OD2 1 
ATOM   413  N N   . ILE A 1 216 ? -12.075 -7.279  32.707  1.00 24.79 ? 216 ILE A N   1 
ATOM   414  C CA  . ILE A 1 216 ? -10.662 -7.609  32.508  1.00 24.63 ? 216 ILE A CA  1 
ATOM   415  C C   . ILE A 1 216 ? -10.223 -8.502  33.644  1.00 23.48 ? 216 ILE A C   1 
ATOM   416  O O   . ILE A 1 216 ? -10.512 -8.210  34.801  1.00 23.21 ? 216 ILE A O   1 
ATOM   417  C CB  . ILE A 1 216 ? -9.797  -6.327  32.483  1.00 25.71 ? 216 ILE A CB  1 
ATOM   418  C CG1 . ILE A 1 216 ? -10.233 -5.376  31.355  1.00 26.66 ? 216 ILE A CG1 1 
ATOM   419  C CG2 . ILE A 1 216 ? -8.291  -6.651  32.410  1.00 26.23 ? 216 ILE A CG2 1 
ATOM   420  C CD1 . ILE A 1 216 ? -9.735  -3.961  31.534  1.00 28.14 ? 216 ILE A CD1 1 
ATOM   421  N N   . LEU A 1 217 ? -9.562  -9.597  33.322  1.00 22.24 ? 217 LEU A N   1 
ATOM   422  C CA  . LEU A 1 217 ? -9.049  -10.534 34.309  1.00 21.89 ? 217 LEU A CA  1 
ATOM   423  C C   . LEU A 1 217 ? -7.568  -10.782 34.019  1.00 20.73 ? 217 LEU A C   1 
ATOM   424  O O   . LEU A 1 217 ? -7.223  -11.062 32.881  1.00 20.24 ? 217 LEU A O   1 
ATOM   425  C CB  . LEU A 1 217 ? -9.797  -11.879 34.154  1.00 22.87 ? 217 LEU A CB  1 
ATOM   426  C CG  . LEU A 1 217 ? -9.304  -13.008 35.085  1.00 25.89 ? 217 LEU A CG  1 
ATOM   427  C CD1 . LEU A 1 217 ? -9.949  -12.876 36.446  1.00 26.81 ? 217 LEU A CD1 1 
ATOM   428  C CD2 . LEU A 1 217 ? -9.615  -14.381 34.505  1.00 27.02 ? 217 LEU A CD2 1 
ATOM   429  N N   . GLN A 1 218 ? -6.707  -10.744 35.044  1.00 20.26 ? 218 GLN A N   1 
ATOM   430  C CA  . GLN A 1 218 ? -5.313  -11.145 34.872  1.00 20.05 ? 218 GLN A CA  1 
ATOM   431  C C   . GLN A 1 218 ? -5.345  -12.672 35.080  1.00 19.53 ? 218 GLN A C   1 
ATOM   432  O O   . GLN A 1 218 ? -5.461  -13.141 36.220  1.00 20.43 ? 218 GLN A O   1 
ATOM   433  C CB  . GLN A 1 218 ? -4.393  -10.485 35.911  1.00 21.07 ? 218 GLN A CB  1 
ATOM   434  C CG  . GLN A 1 218 ? -2.907  -10.790 35.620  1.00 24.92 ? 218 GLN A CG  1 
ATOM   435  C CD  . GLN A 1 218 ? -1.958  -10.269 36.665  1.00 30.00 ? 218 GLN A CD  1 
ATOM   436  O OE1 . GLN A 1 218 ? -2.356  -9.794  37.726  1.00 32.06 ? 218 GLN A OE1 1 
ATOM   437  N NE2 . GLN A 1 218 ? -0.662  -10.348 36.393  1.00 31.80 ? 218 GLN A NE2 1 
ATOM   438  N N   . LEU A 1 219 ? -5.371  -13.433 33.992  1.00 18.12 ? 219 LEU A N   1 
ATOM   439  C CA  . LEU A 1 219 ? -5.495  -14.890 34.075  1.00 18.95 ? 219 LEU A CA  1 
ATOM   440  C C   . LEU A 1 219 ? -4.318  -15.534 34.771  1.00 20.21 ? 219 LEU A C   1 
ATOM   441  O O   . LEU A 1 219 ? -4.485  -16.471 35.573  1.00 21.12 ? 219 LEU A O   1 
ATOM   442  C CB  . LEU A 1 219 ? -5.641  -15.484 32.654  1.00 18.68 ? 219 LEU A CB  1 
ATOM   443  C CG  . LEU A 1 219 ? -5.717  -17.010 32.566  1.00 18.91 ? 219 LEU A CG  1 
ATOM   444  C CD1 . LEU A 1 219 ? -6.958  -17.545 33.296  1.00 20.15 ? 219 LEU A CD1 1 
ATOM   445  C CD2 . LEU A 1 219 ? -5.661  -17.463 31.095  1.00 19.65 ? 219 LEU A CD2 1 
ATOM   446  N N   . LEU A 1 220 ? -3.121  -15.077 34.429  1.00 20.18 ? 220 LEU A N   1 
ATOM   447  C CA  . LEU A 1 220 ? -1.922  -15.691 34.959  1.00 20.41 ? 220 LEU A CA  1 
ATOM   448  C C   . LEU A 1 220 ? -0.739  -14.767 34.893  1.00 20.94 ? 220 LEU A C   1 
ATOM   449  O O   . LEU A 1 220 ? -0.736  -13.773 34.158  1.00 20.49 ? 220 LEU A O   1 
ATOM   450  C CB  . LEU A 1 220 ? -1.627  -16.975 34.141  1.00 20.80 ? 220 LEU A CB  1 
ATOM   451  C CG  . LEU A 1 220 ? -1.178  -16.752 32.675  1.00 23.20 ? 220 LEU A CG  1 
ATOM   452  C CD1 . LEU A 1 220 ? 0.332   -16.934 32.544  1.00 24.81 ? 220 LEU A CD1 1 
ATOM   453  C CD2 . LEU A 1 220 ? -1.904  -17.702 31.734  1.00 23.95 ? 220 LEU A CD2 1 
ATOM   454  N N   . GLN A 1 221 ? 0.280   -15.128 35.644  1.00 20.74 ? 221 GLN A N   1 
ATOM   455  C CA  . GLN A 1 221 ? 1.541   -14.440 35.603  1.00 22.35 ? 221 GLN A CA  1 
ATOM   456  C C   . GLN A 1 221 ? 2.625   -15.493 35.722  1.00 22.79 ? 221 GLN A C   1 
ATOM   457  O O   . GLN A 1 221 ? 2.533   -16.393 36.565  1.00 23.26 ? 221 GLN A O   1 
ATOM   458  C CB  . GLN A 1 221 ? 1.650   -13.385 36.707  1.00 25.04 ? 221 GLN A CB  1 
ATOM   459  C CG  . GLN A 1 221 ? 2.926   -12.556 36.573  1.00 31.20 ? 221 GLN A CG  1 
ATOM   460  C CD  . GLN A 1 221 ? 3.096   -11.529 37.664  1.00 39.73 ? 221 GLN A CD  1 
ATOM   461  O OE1 . GLN A 1 221 ? 3.000   -11.822 38.864  1.00 41.67 ? 221 GLN A OE1 1 
ATOM   462  N NE2 . GLN A 1 221 ? 3.375   -10.300 37.261  1.00 41.90 ? 221 GLN A NE2 1 
ATOM   463  N N   . MET A 1 222 ? 3.686   -15.362 34.916  1.00 22.50 ? 222 MET A N   1 
ATOM   464  C CA  . MET A 1 222 ? 4.842   -16.242 34.993  1.00 23.12 ? 222 MET A CA  1 
ATOM   465  C C   . MET A 1 222 ? 5.479   -16.168 36.382  1.00 24.12 ? 222 MET A C   1 
ATOM   466  O O   . MET A 1 222 ? 5.454   -15.103 37.008  1.00 24.86 ? 222 MET A O   1 
ATOM   467  C CB  . MET A 1 222 ? 5.869   -15.846 33.920  1.00 23.73 ? 222 MET A CB  1 
ATOM   468  C CG  . MET A 1 222 ? 5.320   -15.924 32.504  1.00 27.27 ? 222 MET A CG  1 
ATOM   469  S SD  . MET A 1 222 ? 5.305   -17.589 31.795  1.00 33.15 ? 222 MET A SD  1 
ATOM   470  C CE  . MET A 1 222 ? 3.744   -18.175 32.329  1.00 35.26 ? 222 MET A CE  1 
ATOM   471  N N   . GLU A 1 223 ? 5.959   -17.302 36.897  1.00 24.43 ? 223 GLU A N   1 
ATOM   472  C CA  . GLU A 1 223 ? 6.488   -17.331 38.255  1.00 27.05 ? 223 GLU A CA  1 
ATOM   473  C C   . GLU A 1 223 ? 7.993   -17.143 38.353  1.00 28.08 ? 223 GLU A C   1 
ATOM   474  O O   . GLU A 1 223 ? 8.460   -16.808 39.430  1.00 29.28 ? 223 GLU A O   1 
ATOM   475  C CB  . GLU A 1 223 ? 6.053   -18.606 39.014  1.00 31.93 ? 223 GLU A CB  1 
ATOM   476  C CG  . GLU A 1 223 ? 4.554   -18.680 39.279  1.00 40.07 ? 223 GLU A CG  1 
ATOM   477  C CD  . GLU A 1 223 ? 4.150   -19.048 40.698  1.00 51.22 ? 223 GLU A CD  1 
ATOM   478  O OE1 . GLU A 1 223 ? 2.936   -19.009 41.008  1.00 54.12 ? 223 GLU A OE1 1 
ATOM   479  O OE2 . GLU A 1 223 ? 5.049   -19.371 41.504  1.00 54.45 ? 223 GLU A OE2 1 
ATOM   480  N N   . GLN A 1 224 ? 8.750   -17.352 37.265  1.00 27.87 ? 224 GLN A N   1 
ATOM   481  C CA  . GLN A 1 224 ? 10.206  -17.228 37.363  1.00 29.06 ? 224 GLN A CA  1 
ATOM   482  C C   . GLN A 1 224 ? 10.739  -15.916 36.795  1.00 27.62 ? 224 GLN A C   1 
ATOM   483  O O   . GLN A 1 224 ? 10.249  -15.446 35.770  1.00 26.65 ? 224 GLN A O   1 
ATOM   484  C CB  . GLN A 1 224 ? 10.909  -18.406 36.656  1.00 31.72 ? 224 GLN A CB  1 
ATOM   485  C CG  . GLN A 1 224 ? 10.253  -19.776 36.803  1.00 36.39 ? 224 GLN A CG  1 
ATOM   486  C CD  . GLN A 1 224 ? 10.055  -20.189 38.228  1.00 42.91 ? 224 GLN A CD  1 
ATOM   487  O OE1 . GLN A 1 224 ? 8.987   -20.668 38.619  1.00 45.03 ? 224 GLN A OE1 1 
ATOM   488  N NE2 . GLN A 1 224 ? 11.089  -20.030 39.033  1.00 44.45 ? 224 GLN A NE2 1 
ATOM   489  N N   . PRO A 1 225 ? 11.810  -15.371 37.410  1.00 27.45 ? 225 PRO A N   1 
ATOM   490  C CA  . PRO A 1 225 ? 12.449  -14.161 36.861  1.00 27.28 ? 225 PRO A CA  1 
ATOM   491  C C   . PRO A 1 225 ? 12.892  -14.375 35.412  1.00 28.25 ? 225 PRO A C   1 
ATOM   492  O O   . PRO A 1 225 ? 13.283  -15.478 35.034  1.00 29.51 ? 225 PRO A O   1 
ATOM   493  C CB  . PRO A 1 225 ? 13.677  -13.981 37.770  1.00 28.04 ? 225 PRO A CB  1 
ATOM   494  C CG  . PRO A 1 225 ? 13.241  -14.578 39.096  1.00 27.96 ? 225 PRO A CG  1 
ATOM   495  C CD  . PRO A 1 225 ? 12.471  -15.811 38.654  1.00 26.45 ? 225 PRO A CD  1 
ATOM   496  N N   . GLY A 1 226 ? 12.745  -13.347 34.593  1.00 27.16 ? 226 GLY A N   1 
ATOM   497  C CA  . GLY A 1 226 ? 13.124  -13.417 33.187  1.00 27.19 ? 226 GLY A CA  1 
ATOM   498  C C   . GLY A 1 226 ? 12.077  -14.019 32.260  1.00 27.22 ? 226 GLY A C   1 
ATOM   499  O O   . GLY A 1 226 ? 12.112  -13.789 31.053  1.00 29.48 ? 226 GLY A O   1 
ATOM   500  N N   . GLU A 1 227 ? 11.161  -14.830 32.793  1.00 25.74 ? 227 GLU A N   1 
ATOM   501  C CA  . GLU A 1 227 ? 10.154  -15.516 31.986  1.00 24.17 ? 227 GLU A CA  1 
ATOM   502  C C   . GLU A 1 227 ? 9.131   -14.576 31.364  1.00 22.47 ? 227 GLU A C   1 
ATOM   503  O O   . GLU A 1 227 ? 8.689   -13.636 32.012  1.00 22.37 ? 227 GLU A O   1 
ATOM   504  C CB  . GLU A 1 227 ? 9.382   -16.542 32.816  1.00 26.99 ? 227 GLU A CB  1 
ATOM   505  C CG  . GLU A 1 227 ? 10.070  -17.856 33.089  1.00 33.41 ? 227 GLU A CG  1 
ATOM   506  C CD  . GLU A 1 227 ? 9.097   -18.852 33.700  1.00 41.83 ? 227 GLU A CD  1 
ATOM   507  O OE1 . GLU A 1 227 ? 8.290   -18.437 34.568  1.00 40.39 ? 227 GLU A OE1 1 
ATOM   508  O OE2 . GLU A 1 227 ? 9.139   -20.044 33.313  1.00 43.58 ? 227 GLU A OE2 1 
ATOM   509  N N   . TYR A 1 228 ? 8.780   -14.817 30.100  1.00 20.74 ? 228 TYR A N   1 
ATOM   510  C CA  . TYR A 1 228 ? 7.747   -14.044 29.437  1.00 20.18 ? 228 TYR A CA  1 
ATOM   511  C C   . TYR A 1 228 ? 6.846   -14.970 28.606  1.00 19.57 ? 228 TYR A C   1 
ATOM   512  O O   . TYR A 1 228 ? 7.225   -16.115 28.297  1.00 19.80 ? 228 TYR A O   1 
ATOM   513  C CB  . TYR A 1 228 ? 8.308   -12.893 28.565  1.00 20.36 ? 228 TYR A CB  1 
ATOM   514  C CG  . TYR A 1 228 ? 9.270   -13.345 27.484  1.00 21.69 ? 228 TYR A CG  1 
ATOM   515  C CD1 . TYR A 1 228 ? 10.636  -13.415 27.727  1.00 23.05 ? 228 TYR A CD1 1 
ATOM   516  C CD2 . TYR A 1 228 ? 8.819   -13.649 26.207  1.00 22.63 ? 228 TYR A CD2 1 
ATOM   517  C CE1 . TYR A 1 228 ? 11.524  -13.817 26.735  1.00 23.60 ? 228 TYR A CE1 1 
ATOM   518  C CE2 . TYR A 1 228 ? 9.698   -14.056 25.211  1.00 23.57 ? 228 TYR A CE2 1 
ATOM   519  C CZ  . TYR A 1 228 ? 11.049  -14.134 25.481  1.00 24.68 ? 228 TYR A CZ  1 
ATOM   520  O OH  . TYR A 1 228 ? 11.911  -14.546 24.496  1.00 26.30 ? 228 TYR A OH  1 
ATOM   521  N N   . ILE A 1 229 ? 5.671   -14.469 28.248  1.00 18.07 ? 229 ILE A N   1 
ATOM   522  C CA  . ILE A 1 229 ? 4.755   -15.218 27.410  1.00 17.55 ? 229 ILE A CA  1 
ATOM   523  C C   . ILE A 1 229 ? 5.157   -15.001 25.957  1.00 16.84 ? 229 ILE A C   1 
ATOM   524  O O   . ILE A 1 229 ? 5.386   -13.862 25.542  1.00 17.76 ? 229 ILE A O   1 
ATOM   525  C CB  . ILE A 1 229 ? 3.315   -14.737 27.610  1.00 18.39 ? 229 ILE A CB  1 
ATOM   526  C CG1 . ILE A 1 229 ? 2.914   -14.735 29.107  1.00 20.43 ? 229 ILE A CG1 1 
ATOM   527  C CG2 . ILE A 1 229 ? 2.370   -15.567 26.709  1.00 17.28 ? 229 ILE A CG2 1 
ATOM   528  C CD1 . ILE A 1 229 ? 2.873   -16.020 29.687  1.00 22.91 ? 229 ILE A CD1 1 
ATOM   529  N N   . SER A 1 230 ? 5.236   -16.083 25.179  1.00 15.08 ? 230 SER A N   1 
ATOM   530  C CA  . SER A 1 230 ? 5.639   -16.003 23.765  1.00 15.19 ? 230 SER A CA  1 
ATOM   531  C C   . SER A 1 230 ? 4.525   -16.320 22.784  1.00 14.60 ? 230 SER A C   1 
ATOM   532  O O   . SER A 1 230 ? 4.639   -15.969 21.598  1.00 15.04 ? 230 SER A O   1 
ATOM   533  C CB  . SER A 1 230 ? 6.864   -16.879 23.505  1.00 17.34 ? 230 SER A CB  1 
ATOM   534  O OG  . SER A 1 230 ? 6.790   -18.108 24.213  1.00 20.43 ? 230 SER A OG  1 
ATOM   535  N N   . SER A 1 231 ? 3.423   -16.917 23.260  1.00 13.53 ? 231 SER A N   1 
ATOM   536  C CA  . SER A 1 231 ? 2.279   -17.155 22.380  1.00 13.77 ? 231 SER A CA  1 
ATOM   537  C C   . SER A 1 231 ? 1.012   -17.455 23.130  1.00 13.38 ? 231 SER A C   1 
ATOM   538  O O   . SER A 1 231 ? 1.080   -17.953 24.251  1.00 14.05 ? 231 SER A O   1 
ATOM   539  C CB  . SER A 1 231 ? 2.555   -18.314 21.438  1.00 15.69 ? 231 SER A CB  1 
ATOM   540  O OG  . SER A 1 231 ? 3.034   -19.461 22.120  1.00 15.49 ? 231 SER A OG  1 
ATOM   541  N N   . VAL A 1 232 ? -0.150  -17.192 22.511  1.00 13.26 ? 232 VAL A N   1 
ATOM   542  C CA  . VAL A 1 232 ? -1.435  -17.547 23.098  1.00 13.54 ? 232 VAL A CA  1 
ATOM   543  C C   . VAL A 1 232 ? -2.342  -18.015 21.945  1.00 13.13 ? 232 VAL A C   1 
ATOM   544  O O   . VAL A 1 232 ? -2.237  -17.526 20.803  1.00 13.01 ? 232 VAL A O   1 
ATOM   545  C CB  . VAL A 1 232 ? -2.144  -16.411 23.904  1.00 15.05 ? 232 VAL A CB  1 
ATOM   546  C CG1 . VAL A 1 232 ? -1.311  -15.935 25.110  1.00 15.43 ? 232 VAL A CG1 1 
ATOM   547  C CG2 . VAL A 1 232 ? -2.535  -15.231 23.009  1.00 16.15 ? 232 VAL A CG2 1 
ATOM   548  N N   . ALA A 1 233 ? -3.155  -19.030 22.222  1.00 12.39 ? 233 ALA A N   1 
ATOM   549  C CA  . ALA A 1 233 ? -4.139  -19.494 21.249  1.00 12.56 ? 233 ALA A CA  1 
ATOM   550  C C   . ALA A 1 233 ? -5.306  -20.161 21.943  1.00 13.19 ? 233 ALA A C   1 
ATOM   551  O O   . ALA A 1 233 ? -5.109  -21.112 22.688  1.00 13.73 ? 233 ALA A O   1 
ATOM   552  C CB  . ALA A 1 233 ? -3.517  -20.431 20.214  1.00 13.30 ? 233 ALA A CB  1 
ATOM   553  N N   . TRP A 1 234 ? -6.542  -19.755 21.593  1.00 12.96 ? 234 TRP A N   1 
ATOM   554  C CA  . TRP A 1 234 ? -7.722  -20.348 22.169  1.00 14.04 ? 234 TRP A CA  1 
ATOM   555  C C   . TRP A 1 234 ? -8.080  -21.641 21.470  1.00 15.04 ? 234 TRP A C   1 
ATOM   556  O O   . TRP A 1 234 ? -8.038  -21.693 20.234  1.00 15.12 ? 234 TRP A O   1 
ATOM   557  C CB  . TRP A 1 234 ? -8.907  -19.409 21.962  1.00 14.80 ? 234 TRP A CB  1 
ATOM   558  C CG  . TRP A 1 234 ? -8.844  -18.175 22.791  1.00 14.67 ? 234 TRP A CG  1 
ATOM   559  C CD1 . TRP A 1 234 ? -8.521  -16.924 22.372  1.00 15.38 ? 234 TRP A CD1 1 
ATOM   560  C CD2 . TRP A 1 234 ? -9.263  -18.048 24.158  1.00 14.42 ? 234 TRP A CD2 1 
ATOM   561  N NE1 . TRP A 1 234 ? -8.689  -16.022 23.397  1.00 15.51 ? 234 TRP A NE1 1 
ATOM   562  C CE2 . TRP A 1 234 ? -9.134  -16.688 24.509  1.00 15.43 ? 234 TRP A CE2 1 
ATOM   563  C CE3 . TRP A 1 234 ? -9.783  -18.940 25.099  1.00 15.45 ? 234 TRP A CE3 1 
ATOM   564  C CZ2 . TRP A 1 234 ? -9.466  -16.209 25.774  1.00 15.64 ? 234 TRP A CZ2 1 
ATOM   565  C CZ3 . TRP A 1 234 ? -10.123 -18.461 26.350  1.00 16.02 ? 234 TRP A CZ3 1 
ATOM   566  C CH2 . TRP A 1 234 ? -9.951  -17.111 26.679  1.00 16.32 ? 234 TRP A CH2 1 
ATOM   567  N N   . ILE A 1 235 ? -8.604  -22.607 22.225  1.00 16.21 ? 235 ILE A N   1 
ATOM   568  C CA  . ILE A 1 235 ? -9.158  -23.818 21.612  1.00 17.46 ? 235 ILE A CA  1 
ATOM   569  C C   . ILE A 1 235 ? -10.469 -23.398 20.880  1.00 19.08 ? 235 ILE A C   1 
ATOM   570  O O   . ILE A 1 235 ? -11.029 -22.325 21.176  1.00 18.84 ? 235 ILE A O   1 
ATOM   571  C CB  . ILE A 1 235 ? -9.440  -24.907 22.699  1.00 17.64 ? 235 ILE A CB  1 
ATOM   572  C CG1 . ILE A 1 235 ? -9.523  -26.321 22.089  1.00 19.15 ? 235 ILE A CG1 1 
ATOM   573  C CG2 . ILE A 1 235 ? -10.711 -24.584 23.510  1.00 18.25 ? 235 ILE A CG2 1 
ATOM   574  C CD1 . ILE A 1 235 ? -9.584  -27.431 23.106  1.00 19.34 ? 235 ILE A CD1 1 
ATOM   575  N N   . LYS A 1 236 ? -10.923 -24.198 19.910  1.00 20.55 ? 236 LYS A N   1 
ATOM   576  C CA  . LYS A 1 236 ? -12.122 -23.876 19.116  1.00 22.91 ? 236 LYS A CA  1 
ATOM   577  C C   . LYS A 1 236 ? -13.351 -23.490 19.934  1.00 24.17 ? 236 LYS A C   1 
ATOM   578  O O   . LYS A 1 236 ? -13.964 -22.472 19.633  1.00 25.44 ? 236 LYS A O   1 
ATOM   579  C CB  . LYS A 1 236 ? -12.478 -25.012 18.142  1.00 25.46 ? 236 LYS A CB  1 
ATOM   580  N N   . GLU A 1 237 ? -13.674 -24.230 20.987  1.00 24.39 ? 237 GLU A N   1 
ATOM   581  C CA  . GLU A 1 237 ? -14.829 -23.919 21.857  1.00 25.38 ? 237 GLU A CA  1 
ATOM   582  C C   . GLU A 1 237 ? -14.644 -22.677 22.767  1.00 25.30 ? 237 GLU A C   1 
ATOM   583  O O   . GLU A 1 237 ? -15.595 -22.253 23.437  1.00 26.13 ? 237 GLU A O   1 
ATOM   584  C CB  . GLU A 1 237 ? -15.198 -25.135 22.721  1.00 28.84 ? 237 GLU A CB  1 
ATOM   585  N N   . GLY A 1 238 ? -13.427 -22.161 22.839  1.00 24.33 ? 238 GLY A N   1 
ATOM   586  C CA  . GLY A 1 238 ? -13.119 -20.975 23.626  1.00 24.21 ? 238 GLY A CA  1 
ATOM   587  C C   . GLY A 1 238 ? -13.058 -21.147 25.136  1.00 23.64 ? 238 GLY A C   1 
ATOM   588  O O   . GLY A 1 238 ? -12.987 -20.143 25.843  1.00 24.60 ? 238 GLY A O   1 
ATOM   589  N N   . ASN A 1 239 ? -13.050 -22.392 25.653  1.00 21.84 ? 239 ASN A N   1 
ATOM   590  C CA  . ASN A 1 239 ? -12.974 -22.597 27.127  1.00 22.39 ? 239 ASN A CA  1 
ATOM   591  C C   . ASN A 1 239 ? -11.549 -22.884 27.677  1.00 21.02 ? 239 ASN A C   1 
ATOM   592  O O   . ASN A 1 239 ? -11.300 -22.804 28.900  1.00 21.76 ? 239 ASN A O   1 
ATOM   593  C CB  . ASN A 1 239 ? -13.940 -23.680 27.569  1.00 25.29 ? 239 ASN A CB  1 
ATOM   594  C CG  . ASN A 1 239 ? -13.831 -24.995 26.830  1.00 30.91 ? 239 ASN A CG  1 
ATOM   595  O OD1 . ASN A 1 239 ? -13.386 -25.087 25.663  1.00 31.33 ? 239 ASN A OD1 1 
ATOM   596  N ND2 . ASN A 1 239 ? -14.282 -26.060 27.493  1.00 33.08 ? 239 ASN A ND2 1 
ATOM   597  N N   . TYR A 1 240 ? -10.620 -23.181 26.792  1.00 19.03 ? 240 TYR A N   1 
ATOM   598  C CA  . TYR A 1 240 ? -9.232  -23.464 27.176  1.00 18.28 ? 240 TYR A CA  1 
ATOM   599  C C   . TYR A 1 240 ? -8.307  -22.553 26.380  1.00 17.18 ? 240 TYR A C   1 
ATOM   600  O O   . TYR A 1 240 ? -8.521  -22.355 25.170  1.00 17.02 ? 240 TYR A O   1 
ATOM   601  C CB  . TYR A 1 240 ? -8.865  -24.927 26.838  1.00 19.80 ? 240 TYR A CB  1 
ATOM   602  C CG  . TYR A 1 240 ? -9.726  -25.916 27.583  1.00 23.36 ? 240 TYR A CG  1 
ATOM   603  C CD1 . TYR A 1 240 ? -9.628  -26.053 28.954  1.00 25.23 ? 240 TYR A CD1 1 
ATOM   604  C CD2 . TYR A 1 240 ? -10.704 -26.651 26.927  1.00 26.28 ? 240 TYR A CD2 1 
ATOM   605  C CE1 . TYR A 1 240 ? -10.427 -26.950 29.649  1.00 27.21 ? 240 TYR A CE1 1 
ATOM   606  C CE2 . TYR A 1 240 ? -11.493 -27.571 27.608  1.00 28.08 ? 240 TYR A CE2 1 
ATOM   607  C CZ  . TYR A 1 240 ? -11.370 -27.697 28.978  1.00 29.52 ? 240 TYR A CZ  1 
ATOM   608  O OH  . TYR A 1 240 ? -12.171 -28.559 29.692  1.00 33.49 ? 240 TYR A OH  1 
ATOM   609  N N   . LEU A 1 241 ? -7.281  -22.023 27.034  1.00 15.74 ? 241 LEU A N   1 
ATOM   610  C CA  . LEU A 1 241 ? -6.314  -21.165 26.358  1.00 15.40 ? 241 LEU A CA  1 
ATOM   611  C C   . LEU A 1 241 ? -4.959  -21.843 26.416  1.00 15.23 ? 241 LEU A C   1 
ATOM   612  O O   . LEU A 1 241 ? -4.543  -22.266 27.499  1.00 15.19 ? 241 LEU A O   1 
ATOM   613  C CB  . LEU A 1 241 ? -6.214  -19.797 27.068  1.00 15.43 ? 241 LEU A CB  1 
ATOM   614  C CG  . LEU A 1 241 ? -5.218  -18.811 26.421  1.00 15.99 ? 241 LEU A CG  1 
ATOM   615  C CD1 . LEU A 1 241 ? -5.759  -18.310 25.103  1.00 16.33 ? 241 LEU A CD1 1 
ATOM   616  C CD2 . LEU A 1 241 ? -4.958  -17.597 27.350  1.00 17.59 ? 241 LEU A CD2 1 
ATOM   617  N N   . ALA A 1 242 ? -4.277  -21.972 25.277  1.00 14.66 ? 242 ALA A N   1 
ATOM   618  C CA  . ALA A 1 242 ? -2.912  -22.508 25.269  1.00 14.27 ? 242 ALA A CA  1 
ATOM   619  C C   . ALA A 1 242 ? -1.992  -21.291 25.415  1.00 15.08 ? 242 ALA A C   1 
ATOM   620  O O   . ALA A 1 242 ? -2.245  -20.232 24.825  1.00 15.12 ? 242 ALA A O   1 
ATOM   621  C CB  . ALA A 1 242 ? -2.624  -23.230 23.954  1.00 14.37 ? 242 ALA A CB  1 
ATOM   622  N N   . VAL A 1 243 ? -0.919  -21.432 26.219  1.00 15.34 ? 243 VAL A N   1 
ATOM   623  C CA  . VAL A 1 243 ? 0.013   -20.339 26.466  1.00 15.47 ? 243 VAL A CA  1 
ATOM   624  C C   . VAL A 1 243 ? 1.440   -20.872 26.293  1.00 16.73 ? 243 VAL A C   1 
ATOM   625  O O   . VAL A 1 243 ? 1.870   -21.728 27.062  1.00 17.35 ? 243 VAL A O   1 
ATOM   626  C CB  . VAL A 1 243 ? -0.192  -19.806 27.914  1.00 16.47 ? 243 VAL A CB  1 
ATOM   627  C CG1 . VAL A 1 243 ? 0.827   -18.733 28.238  1.00 18.01 ? 243 VAL A CG1 1 
ATOM   628  C CG2 . VAL A 1 243 ? -1.630  -19.269 28.102  1.00 15.99 ? 243 VAL A CG2 1 
ATOM   629  N N   . GLY A 1 244 ? 2.157   -20.380 25.290  1.00 16.62 ? 244 GLY A N   1 
ATOM   630  C CA  . GLY A 1 244 ? 3.542   -20.768 25.088  1.00 17.00 ? 244 GLY A CA  1 
ATOM   631  C C   . GLY A 1 244 ? 4.435   -19.813 25.838  1.00 17.61 ? 244 GLY A C   1 
ATOM   632  O O   . GLY A 1 244 ? 4.149   -18.609 25.907  1.00 16.96 ? 244 GLY A O   1 
ATOM   633  N N   . THR A 1 245 ? 5.535   -20.332 26.401  1.00 17.69 ? 245 THR A N   1 
ATOM   634  C CA  . THR A 1 245 ? 6.404   -19.500 27.214  1.00 18.96 ? 245 THR A CA  1 
ATOM   635  C C   . THR A 1 245 ? 7.851   -19.466 26.726  1.00 20.20 ? 245 THR A C   1 
ATOM   636  O O   . THR A 1 245 ? 8.298   -20.342 25.985  1.00 19.11 ? 245 THR A O   1 
ATOM   637  C CB  . THR A 1 245 ? 6.349   -19.965 28.708  1.00 19.87 ? 245 THR A CB  1 
ATOM   638  O OG1 . THR A 1 245 ? 7.246   -21.059 28.889  1.00 20.54 ? 245 THR A OG1 1 
ATOM   639  C CG2 . THR A 1 245 ? 4.929   -20.331 29.194  1.00 20.46 ? 245 THR A CG2 1 
ATOM   640  N N   . SER A 1 246 ? 8.596   -18.463 27.214  1.00 21.41 ? 246 SER A N   1 
ATOM   641  C CA  . SER A 1 246 ? 10.022  -18.314 26.962  1.00 22.31 ? 246 SER A CA  1 
ATOM   642  C C   . SER A 1 246 ? 10.823  -19.494 27.539  1.00 24.39 ? 246 SER A C   1 
ATOM   643  O O   . SER A 1 246 ? 11.917  -19.779 27.037  1.00 26.13 ? 246 SER A O   1 
ATOM   644  C CB  . SER A 1 246 ? 10.510  -17.022 27.594  1.00 21.86 ? 246 SER A CB  1 
ATOM   645  O OG  . SER A 1 246 ? 10.337  -17.093 29.003  1.00 22.47 ? 246 SER A OG  1 
ATOM   646  N N   A SER A 1 247 ? 10.305  -20.152 28.594  0.59 23.85 ? 247 SER A N   1 
ATOM   647  N N   B SER A 1 247 ? 10.309  -20.161 28.595  0.41 24.01 ? 247 SER A N   1 
ATOM   648  C CA  A SER A 1 247 ? 10.943  -21.315 29.198  0.59 23.81 ? 247 SER A CA  1 
ATOM   649  C CA  B SER A 1 247 ? 10.975  -21.328 29.176  0.41 24.12 ? 247 SER A CA  1 
ATOM   650  C C   A SER A 1 247 ? 10.558  -22.626 28.488  0.59 24.27 ? 247 SER A C   1 
ATOM   651  C C   B SER A 1 247 ? 10.627  -22.632 28.454  0.41 24.21 ? 247 SER A C   1 
ATOM   652  O O   A SER A 1 247 ? 10.649  -23.691 29.099  0.59 24.96 ? 247 SER A O   1 
ATOM   653  O O   B SER A 1 247 ? 10.810  -23.705 29.028  0.41 24.68 ? 247 SER A O   1 
ATOM   654  C CB  A SER A 1 247 ? 10.613  -21.392 30.689  0.59 24.62 ? 247 SER A CB  1 
ATOM   655  C CB  B SER A 1 247 ? 10.638  -21.462 30.657  0.41 25.49 ? 247 SER A CB  1 
ATOM   656  O OG  A SER A 1 247 ? 9.224   -21.212 30.916  0.59 25.64 ? 247 SER A OG  1 
ATOM   657  O OG  B SER A 1 247 ? 11.219  -20.402 31.392  0.41 27.45 ? 247 SER A OG  1 
ATOM   658  N N   . ALA A 1 248 ? 10.127  -22.549 27.201  1.00 23.37 ? 248 ALA A N   1 
ATOM   659  C CA  . ALA A 1 248 ? 9.776   -23.701 26.350  1.00 23.14 ? 248 ALA A CA  1 
ATOM   660  C C   . ALA A 1 248 ? 8.584   -24.526 26.836  1.00 23.40 ? 248 ALA A C   1 
ATOM   661  O O   . ALA A 1 248 ? 8.489   -25.710 26.509  1.00 24.49 ? 248 ALA A O   1 
ATOM   662  C CB  . ALA A 1 248 ? 11.004  -24.609 26.108  1.00 22.14 ? 248 ALA A CB  1 
ATOM   663  N N   . GLU A 1 249 ? 7.670   -23.909 27.588  1.00 21.55 ? 249 GLU A N   1 
ATOM   664  C CA  . GLU A 1 249 ? 6.490   -24.615 28.065  1.00 21.16 ? 249 GLU A CA  1 
ATOM   665  C C   . GLU A 1 249 ? 5.287   -24.303 27.190  1.00 20.54 ? 249 GLU A C   1 
ATOM   666  O O   . GLU A 1 249 ? 5.181   -23.204 26.650  1.00 20.62 ? 249 GLU A O   1 
ATOM   667  C CB  . GLU A 1 249 ? 6.134   -24.181 29.497  1.00 23.25 ? 249 GLU A CB  1 
ATOM   668  C CG  . GLU A 1 249 ? 7.238   -24.441 30.500  1.00 27.83 ? 249 GLU A CG  1 
ATOM   669  C CD  . GLU A 1 249 ? 7.089   -23.617 31.761  1.00 36.01 ? 249 GLU A CD  1 
ATOM   670  O OE1 . GLU A 1 249 ? 7.539   -24.086 32.832  1.00 35.62 ? 249 GLU A OE1 1 
ATOM   671  O OE2 . GLU A 1 249 ? 6.559   -22.485 31.670  1.00 39.32 ? 249 GLU A OE2 1 
ATOM   672  N N   . VAL A 1 250 ? 4.365   -25.247 27.098  1.00 20.03 ? 250 VAL A N   1 
ATOM   673  C CA  . VAL A 1 250 ? 3.078   -25.019 26.445  1.00 19.32 ? 250 VAL A CA  1 
ATOM   674  C C   . VAL A 1 250 ? 2.056   -25.326 27.546  1.00 19.47 ? 250 VAL A C   1 
ATOM   675  O O   . VAL A 1 250 ? 1.875   -26.477 27.914  1.00 19.86 ? 250 VAL A O   1 
ATOM   676  C CB  . VAL A 1 250 ? 2.876   -25.909 25.217  1.00 21.12 ? 250 VAL A CB  1 
ATOM   677  C CG1 . VAL A 1 250 ? 1.499   -25.664 24.603  1.00 22.01 ? 250 VAL A CG1 1 
ATOM   678  C CG2 . VAL A 1 250 ? 3.986   -25.658 24.191  1.00 21.79 ? 250 VAL A CG2 1 
ATOM   679  N N   . GLN A 1 251 ? 1.506   -24.297 28.146  1.00 19.20 ? 251 GLN A N   1 
ATOM   680  C CA  . GLN A 1 251 ? 0.566   -24.429 29.267  1.00 19.39 ? 251 GLN A CA  1 
ATOM   681  C C   . GLN A 1 251 ? -0.864  -24.484 28.754  1.00 20.04 ? 251 GLN A C   1 
ATOM   682  O O   . GLN A 1 251 ? -1.163  -23.895 27.727  1.00 21.33 ? 251 GLN A O   1 
ATOM   683  C CB  . GLN A 1 251 ? 0.730   -23.248 30.234  1.00 21.48 ? 251 GLN A CB  1 
ATOM   684  C CG  . GLN A 1 251 ? 2.169   -23.107 30.736  1.00 24.46 ? 251 GLN A CG  1 
ATOM   685  C CD  . GLN A 1 251 ? 2.332   -22.111 31.853  1.00 28.50 ? 251 GLN A CD  1 
ATOM   686  O OE1 . GLN A 1 251 ? 1.397   -21.396 32.253  1.00 28.38 ? 251 GLN A OE1 1 
ATOM   687  N NE2 . GLN A 1 251 ? 3.551   -22.053 32.401  1.00 30.83 ? 251 GLN A NE2 1 
ATOM   688  N N   . LEU A 1 252 ? -1.726  -25.242 29.419  1.00 18.92 ? 252 LEU A N   1 
ATOM   689  C CA  . LEU A 1 252 ? -3.120  -25.320 29.020  1.00 18.81 ? 252 LEU A CA  1 
ATOM   690  C C   . LEU A 1 252 ? -3.904  -24.792 30.201  1.00 17.99 ? 252 LEU A C   1 
ATOM   691  O O   . LEU A 1 252 ? -3.746  -25.298 31.300  1.00 18.54 ? 252 LEU A O   1 
ATOM   692  C CB  . LEU A 1 252 ? -3.554  -26.735 28.644  1.00 20.25 ? 252 LEU A CB  1 
ATOM   693  C CG  . LEU A 1 252 ? -4.976  -26.811 28.078  1.00 23.69 ? 252 LEU A CG  1 
ATOM   694  C CD1 . LEU A 1 252 ? -5.128  -25.969 26.780  1.00 23.69 ? 252 LEU A CD1 1 
ATOM   695  C CD2 . LEU A 1 252 ? -5.407  -28.259 27.869  1.00 26.45 ? 252 LEU A CD2 1 
ATOM   696  N N   . TRP A 1 253 ? -4.615  -23.680 30.002  1.00 16.79 ? 253 TRP A N   1 
ATOM   697  C CA  . TRP A 1 253 ? -5.369  -23.029 31.062  1.00 17.00 ? 253 TRP A CA  1 
ATOM   698  C C   . TRP A 1 253 ? -6.866  -23.181 30.864  1.00 17.48 ? 253 TRP A C   1 
ATOM   699  O O   . TRP A 1 253 ? -7.365  -22.977 29.761  1.00 19.02 ? 253 TRP A O   1 
ATOM   700  C CB  . TRP A 1 253 ? -4.986  -21.528 31.101  1.00 16.84 ? 253 TRP A CB  1 
ATOM   701  C CG  . TRP A 1 253 ? -3.673  -21.301 31.783  1.00 17.13 ? 253 TRP A CG  1 
ATOM   702  C CD1 . TRP A 1 253 ? -2.420  -21.496 31.265  1.00 18.32 ? 253 TRP A CD1 1 
ATOM   703  C CD2 . TRP A 1 253 ? -3.494  -20.922 33.149  1.00 17.78 ? 253 TRP A CD2 1 
ATOM   704  N NE1 . TRP A 1 253 ? -1.469  -21.267 32.238  1.00 18.73 ? 253 TRP A NE1 1 
ATOM   705  C CE2 . TRP A 1 253 ? -2.103  -20.876 33.393  1.00 18.48 ? 253 TRP A CE2 1 
ATOM   706  C CE3 . TRP A 1 253 ? -4.377  -20.553 34.172  1.00 18.76 ? 253 TRP A CE3 1 
ATOM   707  C CZ2 . TRP A 1 253 ? -1.582  -20.506 34.633  1.00 19.12 ? 253 TRP A CZ2 1 
ATOM   708  C CZ3 . TRP A 1 253 ? -3.862  -20.215 35.413  1.00 19.74 ? 253 TRP A CZ3 1 
ATOM   709  C CH2 . TRP A 1 253 ? -2.476  -20.188 35.631  1.00 19.60 ? 253 TRP A CH2 1 
ATOM   710  N N   . ASP A 1 254 ? -7.588  -23.494 31.933  1.00 16.12 ? 254 ASP A N   1 
ATOM   711  C CA  . ASP A 1 254 ? -9.051  -23.561 31.882  1.00 17.59 ? 254 ASP A CA  1 
ATOM   712  C C   . ASP A 1 254 ? -9.487  -22.170 32.333  1.00 18.70 ? 254 ASP A C   1 
ATOM   713  O O   . ASP A 1 254 ? -9.242  -21.808 33.479  1.00 18.88 ? 254 ASP A O   1 
ATOM   714  C CB  . ASP A 1 254 ? -9.528  -24.636 32.849  1.00 20.15 ? 254 ASP A CB  1 
ATOM   715  C CG  . ASP A 1 254 ? -11.033 -24.793 32.929  1.00 24.20 ? 254 ASP A CG  1 
ATOM   716  O OD1 . ASP A 1 254 ? -11.743 -23.760 32.897  1.00 24.39 ? 254 ASP A OD1 1 
ATOM   717  O OD2 . ASP A 1 254 ? -11.500 -25.944 33.042  1.00 26.58 ? 254 ASP A OD2 1 
ATOM   718  N N   . VAL A 1 255 ? -10.071 -21.372 31.433  1.00 18.71 ? 255 VAL A N   1 
ATOM   719  C CA  . VAL A 1 255 ? -10.425 -20.002 31.783  1.00 19.56 ? 255 VAL A CA  1 
ATOM   720  C C   . VAL A 1 255 ? -11.686 -19.929 32.623  1.00 20.60 ? 255 VAL A C   1 
ATOM   721  O O   . VAL A 1 255 ? -11.818 -18.948 33.338  1.00 21.99 ? 255 VAL A O   1 
ATOM   722  C CB  . VAL A 1 255 ? -10.468 -19.058 30.580  1.00 20.54 ? 255 VAL A CB  1 
ATOM   723  C CG1 . VAL A 1 255 ? -9.137  -19.121 29.837  1.00 20.00 ? 255 VAL A CG1 1 
ATOM   724  C CG2 . VAL A 1 255 ? -11.622 -19.417 29.651  1.00 21.51 ? 255 VAL A CG2 1 
ATOM   725  N N   . GLN A 1 256 ? -12.568 -20.955 32.604  1.00 20.32 ? 256 GLN A N   1 
ATOM   726  C CA  . GLN A 1 256 ? -13.756 -20.926 33.477  1.00 20.95 ? 256 GLN A CA  1 
ATOM   727  C C   . GLN A 1 256 ? -13.313 -21.145 34.930  1.00 21.07 ? 256 GLN A C   1 
ATOM   728  O O   . GLN A 1 256 ? -13.808 -20.485 35.848  1.00 21.88 ? 256 GLN A O   1 
ATOM   729  C CB  . GLN A 1 256 ? -14.752 -22.016 33.052  1.00 23.34 ? 256 GLN A CB  1 
ATOM   730  N N   . GLN A 1 257 ? -12.389 -22.082 35.148  1.00 20.00 ? 257 GLN A N   1 
ATOM   731  C CA  . GLN A 1 257 ? -11.873 -22.352 36.491  1.00 19.74 ? 257 GLN A CA  1 
ATOM   732  C C   . GLN A 1 257 ? -10.689 -21.433 36.873  1.00 19.47 ? 257 GLN A C   1 
ATOM   733  O O   . GLN A 1 257 ? -10.272 -21.460 38.020  1.00 20.58 ? 257 GLN A O   1 
ATOM   734  C CB  . GLN A 1 257 ? -11.374 -23.802 36.564  1.00 20.94 ? 257 GLN A CB  1 
ATOM   735  C CG  . GLN A 1 257 ? -12.460 -24.844 36.311  1.00 23.72 ? 257 GLN A CG  1 
ATOM   736  C CD  . GLN A 1 257 ? -11.976 -26.224 36.680  1.00 30.08 ? 257 GLN A CD  1 
ATOM   737  O OE1 . GLN A 1 257 ? -12.114 -26.676 37.812  1.00 33.56 ? 257 GLN A OE1 1 
ATOM   738  N NE2 . GLN A 1 257 ? -11.361 -26.913 35.741  1.00 31.19 ? 257 GLN A NE2 1 
ATOM   739  N N   A GLN A 1 258 ? -10.110 -20.687 35.907  0.66 18.85 ? 258 GLN A N   1 
ATOM   740  N N   B GLN A 1 258 ? -10.116 -20.665 35.920  0.34 19.37 ? 258 GLN A N   1 
ATOM   741  C CA  A GLN A 1 258 ? -8.935  -19.837 36.125  0.66 19.27 ? 258 GLN A CA  1 
ATOM   742  C CA  B GLN A 1 258 ? -8.922  -19.822 36.126  0.34 20.06 ? 258 GLN A CA  1 
ATOM   743  C C   A GLN A 1 258 ? -7.801  -20.660 36.748  0.66 20.36 ? 258 GLN A C   1 
ATOM   744  C C   B GLN A 1 258 ? -7.785  -20.649 36.725  0.34 20.55 ? 258 GLN A C   1 
ATOM   745  O O   A GLN A 1 258 ? -7.319  -20.369 37.851  0.66 20.78 ? 258 GLN A O   1 
ATOM   746  O O   B GLN A 1 258 ? -7.233  -20.304 37.773  0.34 20.85 ? 258 GLN A O   1 
ATOM   747  C CB  A GLN A 1 258 ? -9.315  -18.582 36.937  0.66 19.75 ? 258 GLN A CB  1 
ATOM   748  C CB  B GLN A 1 258 ? -9.217  -18.570 36.977  0.34 21.64 ? 258 GLN A CB  1 
ATOM   749  C CG  A GLN A 1 258 ? -10.427 -17.786 36.253  0.66 20.32 ? 258 GLN A CG  1 
ATOM   750  C CG  B GLN A 1 258 ? -8.431  -17.350 36.506  0.34 24.64 ? 258 GLN A CG  1 
ATOM   751  C CD  A GLN A 1 258 ? -10.863 -16.580 37.046  0.66 24.07 ? 258 GLN A CD  1 
ATOM   752  C CD  B GLN A 1 258 ? -7.490  -16.780 37.535  0.34 28.10 ? 258 GLN A CD  1 
ATOM   753  O OE1 A GLN A 1 258 ? -10.117 -16.055 37.880  0.66 24.88 ? 258 GLN A OE1 1 
ATOM   754  O OE1 B GLN A 1 258 ? -7.816  -15.819 38.244  0.34 28.91 ? 258 GLN A OE1 1 
ATOM   755  N NE2 A GLN A 1 258 ? -12.071 -16.096 36.764  0.66 24.18 ? 258 GLN A NE2 1 
ATOM   756  N NE2 B GLN A 1 258 ? -6.292  -17.351 37.629  0.34 27.86 ? 258 GLN A NE2 1 
ATOM   757  N N   . LYS A 1 259 ? -7.502  -21.795 36.105  1.00 20.37 ? 259 LYS A N   1 
ATOM   758  C CA  . LYS A 1 259 ? -6.492  -22.711 36.626  1.00 21.15 ? 259 LYS A CA  1 
ATOM   759  C C   . LYS A 1 259 ? -5.734  -23.388 35.533  1.00 20.99 ? 259 LYS A C   1 
ATOM   760  O O   . LYS A 1 259 ? -6.274  -23.629 34.459  1.00 20.39 ? 259 LYS A O   1 
ATOM   761  C CB  . LYS A 1 259 ? -7.089  -23.754 37.588  1.00 24.28 ? 259 LYS A CB  1 
ATOM   762  C CG  . LYS A 1 259 ? -7.734  -24.967 36.928  1.00 30.26 ? 259 LYS A CG  1 
ATOM   763  C CD  . LYS A 1 259 ? -8.299  -25.966 37.943  1.00 35.35 ? 259 LYS A CD  1 
ATOM   764  C CE  . LYS A 1 259 ? -7.280  -26.448 38.941  1.00 39.98 ? 259 LYS A CE  1 
ATOM   765  N NZ  . LYS A 1 259 ? -7.904  -27.347 39.944  1.00 43.84 ? 259 LYS A NZ  1 
ATOM   766  N N   . ARG A 1 260 ? -4.465  -23.680 35.808  1.00 21.06 ? 260 ARG A N   1 
ATOM   767  C CA  . ARG A 1 260 ? -3.624  -24.350 34.846  1.00 20.77 ? 260 ARG A CA  1 
ATOM   768  C C   . ARG A 1 260 ? -3.899  -25.837 34.925  1.00 22.11 ? 260 ARG A C   1 
ATOM   769  O O   . ARG A 1 260 ? -3.847  -26.416 36.008  1.00 23.29 ? 260 ARG A O   1 
ATOM   770  C CB  . ARG A 1 260 ? -2.152  -24.083 35.160  1.00 21.31 ? 260 ARG A CB  1 
ATOM   771  C CG  . ARG A 1 260 ? -1.249  -24.486 34.013  1.00 22.86 ? 260 ARG A CG  1 
ATOM   772  C CD  . ARG A 1 260 ? 0.161   -24.077 34.303  1.00 25.82 ? 260 ARG A CD  1 
ATOM   773  N NE  . ARG A 1 260 ? 0.737   -24.921 35.343  1.00 29.99 ? 260 ARG A NE  1 
ATOM   774  C CZ  . ARG A 1 260 ? 1.961   -24.769 35.836  1.00 36.22 ? 260 ARG A CZ  1 
ATOM   775  N NH1 . ARG A 1 260 ? 2.751   -23.798 35.388  1.00 36.20 ? 260 ARG A NH1 1 
ATOM   776  N NH2 . ARG A 1 260 ? 2.405   -25.585 36.786  1.00 37.46 ? 260 ARG A NH2 1 
ATOM   777  N N   . LEU A 1 261 ? -4.281  -26.437 33.803  1.00 21.99 ? 261 LEU A N   1 
ATOM   778  C CA  . LEU A 1 261 ? -4.540  -27.867 33.746  1.00 23.58 ? 261 LEU A CA  1 
ATOM   779  C C   . LEU A 1 261 ? -3.253  -28.631 33.426  1.00 23.95 ? 261 LEU A C   1 
ATOM   780  O O   . LEU A 1 261 ? -3.080  -29.764 33.890  1.00 24.52 ? 261 LEU A O   1 
ATOM   781  C CB  . LEU A 1 261 ? -5.583  -28.160 32.656  1.00 24.78 ? 261 LEU A CB  1 
ATOM   782  C CG  . LEU A 1 261 ? -7.011  -27.639 32.897  1.00 28.35 ? 261 LEU A CG  1 
ATOM   783  C CD1 . LEU A 1 261 ? -7.946  -28.140 31.813  1.00 29.74 ? 261 LEU A CD1 1 
ATOM   784  C CD2 . LEU A 1 261 ? -7.543  -28.081 34.228  1.00 29.37 ? 261 LEU A CD2 1 
ATOM   785  N N   . ARG A 1 262 ? -2.410  -28.072 32.544  1.00 22.33 ? 262 ARG A N   1 
ATOM   786  C CA  . ARG A 1 262 ? -1.193  -28.762 32.118  1.00 22.61 ? 262 ARG A CA  1 
ATOM   787  C C   . ARG A 1 262 ? -0.036  -27.825 31.922  1.00 22.57 ? 262 ARG A C   1 
ATOM   788  O O   . ARG A 1 262 ? -0.229  -26.669 31.558  1.00 22.26 ? 262 ARG A O   1 
ATOM   789  C CB  . ARG A 1 262 ? -1.433  -29.458 30.765  1.00 24.36 ? 262 ARG A CB  1 
ATOM   790  C CG  . ARG A 1 262 ? -2.625  -30.402 30.780  1.00 27.64 ? 262 ARG A CG  1 
ATOM   791  C CD  . ARG A 1 262 ? -2.557  -31.380 29.669  1.00 28.54 ? 262 ARG A CD  1 
ATOM   792  N NE  . ARG A 1 262 ? -1.435  -32.293 29.850  1.00 27.54 ? 262 ARG A NE  1 
ATOM   793  C CZ  . ARG A 1 262 ? -1.225  -33.369 29.107  1.00 25.79 ? 262 ARG A CZ  1 
ATOM   794  N NH1 . ARG A 1 262 ? -2.061  -33.677 28.122  1.00 23.77 ? 262 ARG A NH1 1 
ATOM   795  N NH2 . ARG A 1 262 ? -0.180  -34.148 29.342  1.00 26.17 ? 262 ARG A NH2 1 
ATOM   796  N N   . ASN A 1 263 ? 1.180   -28.343 32.097  1.00 22.70 ? 263 ASN A N   1 
ATOM   797  C CA  . ASN A 1 263 ? 2.379   -27.596 31.819  1.00 23.99 ? 263 ASN A CA  1 
ATOM   798  C C   . ASN A 1 263 ? 3.231   -28.546 31.018  1.00 25.11 ? 263 ASN A C   1 
ATOM   799  O O   . ASN A 1 263 ? 4.002   -29.312 31.577  1.00 25.66 ? 263 ASN A O   1 
ATOM   800  C CB  . ASN A 1 263 ? 3.087   -27.132 33.085  1.00 26.13 ? 263 ASN A CB  1 
ATOM   801  C CG  . ASN A 1 263 ? 4.204   -26.161 32.776  1.00 29.97 ? 263 ASN A CG  1 
ATOM   802  O OD1 . ASN A 1 263 ? 4.241   -25.525 31.714  1.00 30.24 ? 263 ASN A OD1 1 
ATOM   803  N ND2 . ASN A 1 263 ? 5.170   -26.054 33.675  1.00 32.23 ? 263 ASN A ND2 1 
ATOM   804  N N   . MET A 1 264 ? 3.011   -28.545 29.706  1.00 24.60 ? 264 MET A N   1 
ATOM   805  C CA  . MET A 1 264 ? 3.604   -29.463 28.763  1.00 25.30 ? 264 MET A CA  1 
ATOM   806  C C   . MET A 1 264 ? 4.967   -29.034 28.294  1.00 25.58 ? 264 MET A C   1 
ATOM   807  O O   . MET A 1 264 ? 5.129   -27.985 27.676  1.00 25.08 ? 264 MET A O   1 
ATOM   808  C CB  . MET A 1 264 ? 2.648   -29.672 27.571  1.00 25.76 ? 264 MET A CB  1 
ATOM   809  C CG  . MET A 1 264 ? 1.317   -30.293 27.971  1.00 26.21 ? 264 MET A CG  1 
ATOM   810  S SD  . MET A 1 264 ? 0.116   -30.401 26.600  1.00 25.13 ? 264 MET A SD  1 
ATOM   811  C CE  . MET A 1 264 ? -0.331  -28.663 26.439  1.00 25.58 ? 264 MET A CE  1 
ATOM   812  N N   . THR A 1 265 ? 5.952   -29.879 28.560  1.00 26.02 ? 265 THR A N   1 
ATOM   813  C CA  . THR A 1 265 ? 7.306   -29.633 28.140  1.00 26.95 ? 265 THR A CA  1 
ATOM   814  C C   . THR A 1 265 ? 7.675   -30.669 27.083  1.00 28.29 ? 265 THR A C   1 
ATOM   815  O O   . THR A 1 265 ? 7.285   -31.832 27.162  1.00 30.43 ? 265 THR A O   1 
ATOM   816  C CB  . THR A 1 265 ? 8.261   -29.605 29.348  1.00 29.74 ? 265 THR A CB  1 
ATOM   817  O OG1 . THR A 1 265 ? 8.079   -30.794 30.104  1.00 30.90 ? 265 THR A OG1 1 
ATOM   818  C CG2 . THR A 1 265 ? 8.025   -28.395 30.244  1.00 30.02 ? 265 THR A CG2 1 
ATOM   819  N N   . SER A 1 266 ? 8.389   -30.228 26.088  1.00 26.89 ? 266 SER A N   1 
ATOM   820  C CA  . SER A 1 266 ? 8.871   -31.053 24.985  1.00 26.25 ? 266 SER A CA  1 
ATOM   821  C C   . SER A 1 266 ? 9.855   -30.243 24.136  1.00 26.00 ? 266 SER A C   1 
ATOM   822  O O   . SER A 1 266 ? 10.818  -30.798 23.622  1.00 26.08 ? 266 SER A O   1 
ATOM   823  C CB  . SER A 1 266 ? 7.704   -31.550 24.136  1.00 26.11 ? 266 SER A CB  1 
ATOM   824  O OG  . SER A 1 266 ? 7.046   -30.461 23.519  1.00 26.13 ? 266 SER A OG  1 
ATOM   825  N N   . HIS A 1 267 ? 9.634   -28.919 24.027  1.00 25.31 ? 267 HIS A N   1 
ATOM   826  C CA  . HIS A 1 267 ? 10.480  -28.043 23.247  1.00 25.68 ? 267 HIS A CA  1 
ATOM   827  C C   . HIS A 1 267 ? 11.809  -27.706 23.923  1.00 26.74 ? 267 HIS A C   1 
ATOM   828  O O   . HIS A 1 267 ? 11.917  -27.776 25.145  1.00 27.03 ? 267 HIS A O   1 
ATOM   829  C CB  . HIS A 1 267 ? 9.718   -26.771 22.840  1.00 25.47 ? 267 HIS A CB  1 
ATOM   830  C CG  . HIS A 1 267 ? 8.789   -26.997 21.685  1.00 24.76 ? 267 HIS A CG  1 
ATOM   831  N ND1 . HIS A 1 267 ? 9.273   -27.330 20.444  1.00 25.33 ? 267 HIS A ND1 1 
ATOM   832  C CD2 . HIS A 1 267 ? 7.434   -26.904 21.625  1.00 24.46 ? 267 HIS A CD2 1 
ATOM   833  C CE1 . HIS A 1 267 ? 8.203   -27.430 19.659  1.00 25.99 ? 267 HIS A CE1 1 
ATOM   834  N NE2 . HIS A 1 267 ? 7.075   -27.184 20.330  1.00 24.40 ? 267 HIS A NE2 1 
ATOM   835  N N   . SER A 1 268 ? 12.816  -27.357 23.113  1.00 27.11 ? 268 SER A N   1 
ATOM   836  C CA  . SER A 1 268 ? 14.143  -26.985 23.611  1.00 28.14 ? 268 SER A CA  1 
ATOM   837  C C   . SER A 1 268 ? 14.341  -25.453 23.669  1.00 27.98 ? 268 SER A C   1 
ATOM   838  O O   . SER A 1 268 ? 15.402  -25.001 24.077  1.00 29.90 ? 268 SER A O   1 
ATOM   839  C CB  . SER A 1 268 ? 15.225  -27.613 22.737  1.00 29.66 ? 268 SER A CB  1 
ATOM   840  O OG  . SER A 1 268 ? 15.107  -27.190 21.385  1.00 32.07 ? 268 SER A OG  1 
ATOM   841  N N   . ALA A 1 269 ? 13.345  -24.659 23.267  1.00 25.63 ? 269 ALA A N   1 
ATOM   842  C CA  . ALA A 1 269 ? 13.446  -23.206 23.222  1.00 23.64 ? 269 ALA A CA  1 
ATOM   843  C C   . ALA A 1 269 ? 12.021  -22.573 23.235  1.00 22.06 ? 269 ALA A C   1 
ATOM   844  O O   . ALA A 1 269 ? 11.022  -23.297 23.225  1.00 21.90 ? 269 ALA A O   1 
ATOM   845  C CB  . ALA A 1 269 ? 14.239  -22.779 21.970  1.00 23.61 ? 269 ALA A CB  1 
ATOM   846  N N   . ARG A 1 270 ? 11.917  -21.241 23.299  1.00 21.28 ? 270 ARG A N   1 
ATOM   847  C CA  . ARG A 1 270 ? 10.623  -20.576 23.406  1.00 20.91 ? 270 ARG A CA  1 
ATOM   848  C C   . ARG A 1 270 ? 9.615   -20.990 22.342  1.00 20.14 ? 270 ARG A C   1 
ATOM   849  O O   . ARG A 1 270 ? 9.953   -21.258 21.172  1.00 19.42 ? 270 ARG A O   1 
ATOM   850  C CB  . ARG A 1 270 ? 10.785  -19.062 23.451  1.00 22.94 ? 270 ARG A CB  1 
ATOM   851  C CG  . ARG A 1 270 ? 11.147  -18.463 22.107  1.00 24.62 ? 270 ARG A CG  1 
ATOM   852  C CD  . ARG A 1 270 ? 10.998  -16.958 22.162  1.00 25.13 ? 270 ARG A CD  1 
ATOM   853  N NE  . ARG A 1 270 ? 11.170  -16.358 20.832  1.00 23.21 ? 270 ARG A NE  1 
ATOM   854  C CZ  . ARG A 1 270 ? 11.392  -15.061 20.628  1.00 25.89 ? 270 ARG A CZ  1 
ATOM   855  N NH1 . ARG A 1 270 ? 11.500  -14.587 19.393  1.00 24.53 ? 270 ARG A NH1 1 
ATOM   856  N NH2 . ARG A 1 270 ? 11.471  -14.221 21.659  1.00 25.54 ? 270 ARG A NH2 1 
ATOM   857  N N   . VAL A 1 271 ? 8.358   -21.019 22.757  1.00 18.58 ? 271 VAL A N   1 
ATOM   858  C CA  . VAL A 1 271 ? 7.276   -21.413 21.877  1.00 18.30 ? 271 VAL A CA  1 
ATOM   859  C C   . VAL A 1 271 ? 6.549   -20.141 21.432  1.00 16.84 ? 271 VAL A C   1 
ATOM   860  O O   . VAL A 1 271 ? 5.721   -19.619 22.170  1.00 16.82 ? 271 VAL A O   1 
ATOM   861  C CB  . VAL A 1 271 ? 6.343   -22.380 22.636  1.00 19.99 ? 271 VAL A CB  1 
ATOM   862  C CG1 . VAL A 1 271 ? 5.110   -22.724 21.783  1.00 19.93 ? 271 VAL A CG1 1 
ATOM   863  C CG2 . VAL A 1 271 ? 7.106   -23.647 23.036  1.00 21.58 ? 271 VAL A CG2 1 
ATOM   864  N N   . GLY A 1 272 ? 6.901   -19.639 20.261  1.00 15.16 ? 272 GLY A N   1 
ATOM   865  C CA  . GLY A 1 272 ? 6.355   -18.382 19.775  1.00 16.10 ? 272 GLY A CA  1 
ATOM   866  C C   . GLY A 1 272 ? 5.120   -18.522 18.908  1.00 15.76 ? 272 GLY A C   1 
ATOM   867  O O   . GLY A 1 272 ? 4.509   -17.512 18.567  1.00 15.95 ? 272 GLY A O   1 
ATOM   868  N N   . SER A 1 273 ? 4.728   -19.755 18.550  1.00 15.05 ? 273 SER A N   1 
ATOM   869  C CA  . SER A 1 273 ? 3.541   -19.944 17.713  1.00 14.73 ? 273 SER A CA  1 
ATOM   870  C C   . SER A 1 273 ? 2.731   -21.156 18.125  1.00 15.19 ? 273 SER A C   1 
ATOM   871  O O   . SER A 1 273 ? 3.273   -22.133 18.645  1.00 15.44 ? 273 SER A O   1 
ATOM   872  C CB  . SER A 1 273 ? 3.922   -20.013 16.232  1.00 17.54 ? 273 SER A CB  1 
ATOM   873  O OG  . SER A 1 273 ? 4.747   -21.133 15.970  1.00 20.48 ? 273 SER A OG  1 
ATOM   874  N N   . LEU A 1 274 ? 1.405   -21.060 17.950  1.00 14.62 ? 274 LEU A N   1 
ATOM   875  C CA  . LEU A 1 274 ? 0.484   -22.114 18.371  1.00 14.52 ? 274 LEU A CA  1 
ATOM   876  C C   . LEU A 1 274 ? -0.690  -22.170 17.421  1.00 13.99 ? 274 LEU A C   1 
ATOM   877  O O   . LEU A 1 274 ? -1.176  -21.121 16.980  1.00 14.65 ? 274 LEU A O   1 
ATOM   878  C CB  . LEU A 1 274 ? -0.113  -21.809 19.765  1.00 14.40 ? 274 LEU A CB  1 
ATOM   879  C CG  . LEU A 1 274 ? 0.854   -21.778 20.964  1.00 14.64 ? 274 LEU A CG  1 
ATOM   880  C CD1 . LEU A 1 274 ? 0.165   -21.149 22.201  1.00 15.87 ? 274 LEU A CD1 1 
ATOM   881  C CD2 . LEU A 1 274 ? 1.334   -23.224 21.340  1.00 14.94 ? 274 LEU A CD2 1 
ATOM   882  N N   . SER A 1 275 ? -1.234  -23.364 17.220  1.00 13.33 ? 275 SER A N   1 
ATOM   883  C CA  . SER A 1 275 ? -2.450  -23.504 16.418  1.00 13.32 ? 275 SER A CA  1 
ATOM   884  C C   . SER A 1 275 ? -3.161  -24.781 16.777  1.00 15.74 ? 275 SER A C   1 
ATOM   885  O O   . SER A 1 275 ? -2.541  -25.839 16.814  1.00 16.68 ? 275 SER A O   1 
ATOM   886  C CB  . SER A 1 275 ? -2.139  -23.478 14.922  1.00 14.39 ? 275 SER A CB  1 
ATOM   887  O OG  . SER A 1 275 ? -3.345  -23.570 14.175  1.00 16.12 ? 275 SER A OG  1 
ATOM   888  N N   . TRP A 1 276 ? -4.482  -24.696 16.998  1.00 15.82 ? 276 TRP A N   1 
ATOM   889  C CA  . TRP A 1 276 ? -5.264  -25.866 17.337  1.00 16.28 ? 276 TRP A CA  1 
ATOM   890  C C   . TRP A 1 276 ? -5.932  -26.504 16.127  1.00 17.92 ? 276 TRP A C   1 
ATOM   891  O O   . TRP A 1 276 ? -6.350  -25.816 15.200  1.00 17.91 ? 276 TRP A O   1 
ATOM   892  C CB  . TRP A 1 276 ? -6.398  -25.456 18.273  1.00 15.87 ? 276 TRP A CB  1 
ATOM   893  C CG  . TRP A 1 276 ? -5.981  -25.054 19.645  1.00 15.45 ? 276 TRP A CG  1 
ATOM   894  C CD1 . TRP A 1 276 ? -5.681  -23.798 20.084  1.00 16.78 ? 276 TRP A CD1 1 
ATOM   895  C CD2 . TRP A 1 276 ? -5.998  -25.896 20.807  1.00 15.67 ? 276 TRP A CD2 1 
ATOM   896  N NE1 . TRP A 1 276 ? -5.501  -23.811 21.454  1.00 16.89 ? 276 TRP A NE1 1 
ATOM   897  C CE2 . TRP A 1 276 ? -5.634  -25.102 21.909  1.00 16.57 ? 276 TRP A CE2 1 
ATOM   898  C CE3 . TRP A 1 276 ? -6.198  -27.271 20.998  1.00 15.98 ? 276 TRP A CE3 1 
ATOM   899  C CZ2 . TRP A 1 276 ? -5.612  -25.614 23.222  1.00 17.50 ? 276 TRP A CZ2 1 
ATOM   900  C CZ3 . TRP A 1 276 ? -6.121  -27.790 22.278  1.00 16.43 ? 276 TRP A CZ3 1 
ATOM   901  C CH2 . TRP A 1 276 ? -5.790  -26.977 23.367  1.00 16.59 ? 276 TRP A CH2 1 
ATOM   902  N N   . ASN A 1 277 ? -6.111  -27.827 16.195  1.00 18.66 ? 277 ASN A N   1 
ATOM   903  C CA  . ASN A 1 277 ? -6.894  -28.627 15.262  1.00 20.07 ? 277 ASN A CA  1 
ATOM   904  C C   . ASN A 1 277 ? -7.704  -29.560 16.170  1.00 20.86 ? 277 ASN A C   1 
ATOM   905  O O   . ASN A 1 277 ? -7.187  -30.605 16.559  1.00 21.04 ? 277 ASN A O   1 
ATOM   906  C CB  . ASN A 1 277 ? -5.987  -29.455 14.364  1.00 22.22 ? 277 ASN A CB  1 
ATOM   907  C CG  . ASN A 1 277 ? -6.746  -30.253 13.335  1.00 28.78 ? 277 ASN A CG  1 
ATOM   908  O OD1 . ASN A 1 277 ? -7.901  -29.968 13.023  1.00 31.03 ? 277 ASN A OD1 1 
ATOM   909  N ND2 . ASN A 1 277 ? -6.109  -31.266 12.778  1.00 29.70 ? 277 ASN A ND2 1 
ATOM   910  N N   . SER A 1 278 ? -8.939  -29.169 16.574  1.00 21.00 ? 278 SER A N   1 
ATOM   911  C CA  . SER A 1 278 ? -9.746  -29.941 17.527  1.00 21.57 ? 278 SER A CA  1 
ATOM   912  C C   . SER A 1 278 ? -8.912  -30.071 18.870  1.00 21.24 ? 278 SER A C   1 
ATOM   913  O O   . SER A 1 278 ? -8.461  -29.037 19.359  1.00 21.46 ? 278 SER A O   1 
ATOM   914  C CB  . SER A 1 278 ? -10.230 -31.259 16.893  1.00 23.49 ? 278 SER A CB  1 
ATOM   915  O OG  . SER A 1 278 ? -10.886 -32.076 17.851  1.00 27.94 ? 278 SER A OG  1 
ATOM   916  N N   A TYR A 1 279 ? -8.663  -31.291 19.393  0.55 20.85 ? 279 TYR A N   1 
ATOM   917  N N   B TYR A 1 279 ? -8.653  -31.288 19.390  0.45 20.88 ? 279 TYR A N   1 
ATOM   918  C CA  A TYR A 1 279 ? -7.890  -31.492 20.625  0.55 21.38 ? 279 TYR A CA  1 
ATOM   919  C CA  B TYR A 1 279 ? -7.866  -31.445 20.616  0.45 21.35 ? 279 TYR A CA  1 
ATOM   920  C C   A TYR A 1 279 ? -6.367  -31.556 20.412  0.55 21.04 ? 279 TYR A C   1 
ATOM   921  C C   B TYR A 1 279 ? -6.359  -31.541 20.408  0.45 20.99 ? 279 TYR A C   1 
ATOM   922  O O   A TYR A 1 279 ? -5.632  -31.729 21.384  0.55 21.66 ? 279 TYR A O   1 
ATOM   923  O O   B TYR A 1 279 ? -5.627  -31.701 21.385  0.45 21.51 ? 279 TYR A O   1 
ATOM   924  C CB  A TYR A 1 279 ? -8.376  -32.736 21.384  0.55 22.15 ? 279 TYR A CB  1 
ATOM   925  C CB  B TYR A 1 279 ? -8.353  -32.631 21.434  0.45 22.06 ? 279 TYR A CB  1 
ATOM   926  C CG  A TYR A 1 279 ? -8.486  -33.970 20.515  0.55 23.65 ? 279 TYR A CG  1 
ATOM   927  C CG  B TYR A 1 279 ? -9.670  -32.347 22.106  0.45 23.54 ? 279 TYR A CG  1 
ATOM   928  C CD1 A TYR A 1 279 ? -7.355  -34.673 20.124  0.55 24.96 ? 279 TYR A CD1 1 
ATOM   929  C CD1 B TYR A 1 279 ? -9.738  -31.540 23.233  0.45 24.77 ? 279 TYR A CD1 1 
ATOM   930  C CD2 A TYR A 1 279 ? -9.723  -34.447 20.102  0.55 25.03 ? 279 TYR A CD2 1 
ATOM   931  C CD2 B TYR A 1 279 ? -10.856 -32.850 21.593  0.45 24.84 ? 279 TYR A CD2 1 
ATOM   932  C CE1 A TYR A 1 279 ? -7.445  -35.789 19.301  0.55 26.10 ? 279 TYR A CE1 1 
ATOM   933  C CE1 B TYR A 1 279 ? -10.947 -31.286 23.865  0.45 25.89 ? 279 TYR A CE1 1 
ATOM   934  C CE2 A TYR A 1 279 ? -9.826  -35.560 19.277  0.55 26.09 ? 279 TYR A CE2 1 
ATOM   935  C CE2 B TYR A 1 279 ? -12.074 -32.586 22.204  0.45 25.78 ? 279 TYR A CE2 1 
ATOM   936  C CZ  A TYR A 1 279 ? -8.685  -36.243 18.899  0.55 27.20 ? 279 TYR A CZ  1 
ATOM   937  C CZ  B TYR A 1 279 ? -12.114 -31.812 23.345  0.45 26.94 ? 279 TYR A CZ  1 
ATOM   938  O OH  A TYR A 1 279 ? -8.779  -37.359 18.111  0.55 29.28 ? 279 TYR A OH  1 
ATOM   939  O OH  B TYR A 1 279 ? -13.320 -31.547 23.939  0.45 28.81 ? 279 TYR A OH  1 
ATOM   940  N N   . ILE A 1 280 ? -5.889  -31.452 19.161  1.00 20.09 ? 280 ILE A N   1 
ATOM   941  C CA  . ILE A 1 280 ? -4.462  -31.447 18.897  1.00 19.73 ? 280 ILE A CA  1 
ATOM   942  C C   . ILE A 1 280 ? -4.054  -29.972 18.931  1.00 19.13 ? 280 ILE A C   1 
ATOM   943  O O   . ILE A 1 280 ? -4.663  -29.152 18.244  1.00 19.10 ? 280 ILE A O   1 
ATOM   944  C CB  . ILE A 1 280 ? -4.146  -32.058 17.512  1.00 21.21 ? 280 ILE A CB  1 
ATOM   945  C CG1 . ILE A 1 280 ? -4.391  -33.585 17.521  1.00 23.69 ? 280 ILE A CG1 1 
ATOM   946  C CG2 . ILE A 1 280 ? -2.694  -31.710 17.086  1.00 21.65 ? 280 ILE A CG2 1 
ATOM   947  C CD1 . ILE A 1 280 ? -3.497  -34.339 18.479  1.00 26.37 ? 280 ILE A CD1 1 
ATOM   948  N N   . LEU A 1 281 ? -3.025  -29.641 19.709  1.00 18.02 ? 281 LEU A N   1 
ATOM   949  C CA  . LEU A 1 281 ? -2.498  -28.298 19.742  1.00 17.46 ? 281 LEU A CA  1 
ATOM   950  C C   . LEU A 1 281 ? -1.118  -28.406 19.111  1.00 18.01 ? 281 LEU A C   1 
ATOM   951  O O   . LEU A 1 281 ? -0.319  -29.205 19.576  1.00 18.97 ? 281 LEU A O   1 
ATOM   952  C CB  . LEU A 1 281 ? -2.335  -27.856 21.204  1.00 17.45 ? 281 LEU A CB  1 
ATOM   953  C CG  . LEU A 1 281 ? -1.545  -26.567 21.429  1.00 18.35 ? 281 LEU A CG  1 
ATOM   954  C CD1 . LEU A 1 281 ? -2.268  -25.374 20.764  1.00 18.04 ? 281 LEU A CD1 1 
ATOM   955  C CD2 . LEU A 1 281 ? -1.426  -26.297 22.934  1.00 19.38 ? 281 LEU A CD2 1 
ATOM   956  N N   . SER A 1 282 ? -0.835  -27.632 18.064  1.00 16.44 ? 282 SER A N   1 
ATOM   957  C CA  . SER A 1 282 ? 0.481   -27.631 17.461  1.00 16.03 ? 282 SER A CA  1 
ATOM   958  C C   . SER A 1 282 ? 1.244   -26.426 17.977  1.00 15.65 ? 282 SER A C   1 
ATOM   959  O O   . SER A 1 282 ? 0.689   -25.330 18.081  1.00 14.98 ? 282 SER A O   1 
ATOM   960  C CB  . SER A 1 282 ? 0.384   -27.608 15.940  1.00 18.13 ? 282 SER A CB  1 
ATOM   961  O OG  . SER A 1 282 ? -0.422  -28.698 15.516  1.00 19.70 ? 282 SER A OG  1 
ATOM   962  N N   . SER A 1 283 ? 2.526   -26.621 18.257  1.00 16.01 ? 283 SER A N   1 
ATOM   963  C CA  . SER A 1 283 ? 3.377   -25.570 18.784  1.00 17.14 ? 283 SER A CA  1 
ATOM   964  C C   . SER A 1 283 ? 4.662   -25.449 17.992  1.00 17.84 ? 283 SER A C   1 
ATOM   965  O O   . SER A 1 283 ? 5.273   -26.456 17.662  1.00 17.93 ? 283 SER A O   1 
ATOM   966  C CB  . SER A 1 283 ? 3.724   -25.860 20.244  1.00 18.77 ? 283 SER A CB  1 
ATOM   967  O OG  . SER A 1 283 ? 4.351   -27.120 20.401  1.00 21.21 ? 283 SER A OG  1 
ATOM   968  N N   . GLY A 1 284 ? 5.067   -24.219 17.707  1.00 18.23 ? 284 GLY A N   1 
ATOM   969  C CA  . GLY A 1 284 ? 6.291   -23.953 16.968  1.00 19.23 ? 284 GLY A CA  1 
ATOM   970  C C   . GLY A 1 284 ? 7.271   -23.256 17.877  1.00 20.78 ? 284 GLY A C   1 
ATOM   971  O O   . GLY A 1 284 ? 6.888   -22.422 18.716  1.00 21.12 ? 284 GLY A O   1 
ATOM   972  N N   . SER A 1 285 ? 8.532   -23.600 17.729  1.00 20.56 ? 285 SER A N   1 
ATOM   973  C CA  . SER A 1 285 ? 9.572   -23.125 18.602  1.00 21.53 ? 285 SER A CA  1 
ATOM   974  C C   . SER A 1 285 ? 10.692  -22.384 17.882  1.00 21.42 ? 285 SER A C   1 
ATOM   975  O O   . SER A 1 285 ? 10.879  -22.533 16.669  1.00 20.02 ? 285 SER A O   1 
ATOM   976  C CB  . SER A 1 285 ? 10.170  -24.314 19.354  1.00 23.54 ? 285 SER A CB  1 
ATOM   977  O OG  . SER A 1 285 ? 11.242  -23.935 20.198  1.00 26.49 ? 285 SER A OG  1 
ATOM   978  N N   . ARG A 1 286 ? 11.449  -21.583 18.656  1.00 22.00 ? 286 ARG A N   1 
ATOM   979  C CA  . ARG A 1 286 ? 12.634  -20.881 18.166  1.00 23.75 ? 286 ARG A CA  1 
ATOM   980  C C   . ARG A 1 286 ? 13.662  -21.894 17.600  1.00 25.21 ? 286 ARG A C   1 
ATOM   981  O O   . ARG A 1 286 ? 14.471  -21.536 16.750  1.00 25.38 ? 286 ARG A O   1 
ATOM   982  C CB  . ARG A 1 286 ? 13.239  -20.067 19.324  1.00 26.32 ? 286 ARG A CB  1 
ATOM   983  C CG  . ARG A 1 286 ? 14.387  -19.131 18.941  1.00 30.87 ? 286 ARG A CG  1 
ATOM   984  C CD  . ARG A 1 286 ? 14.948  -18.460 20.185  1.00 35.82 ? 286 ARG A CD  1 
ATOM   985  N NE  . ARG A 1 286 ? 15.002  -17.002 20.058  1.00 40.57 ? 286 ARG A NE  1 
ATOM   986  C CZ  . ARG A 1 286 ? 15.024  -16.159 21.088  1.00 44.78 ? 286 ARG A CZ  1 
ATOM   987  N NH1 . ARG A 1 286 ? 14.988  -16.620 22.338  1.00 41.56 ? 286 ARG A NH1 1 
ATOM   988  N NH2 . ARG A 1 286 ? 15.082  -14.849 20.878  1.00 47.44 ? 286 ARG A NH2 1 
ATOM   989  N N   . SER A 1 287 ? 13.622  -23.166 18.064  1.00 25.70 ? 287 SER A N   1 
ATOM   990  C CA  . SER A 1 287 ? 14.505  -24.234 17.586  1.00 25.86 ? 287 SER A CA  1 
ATOM   991  C C   . SER A 1 287 ? 14.213  -24.653 16.127  1.00 26.00 ? 287 SER A C   1 
ATOM   992  O O   . SER A 1 287 ? 15.033  -25.357 15.529  1.00 27.01 ? 287 SER A O   1 
ATOM   993  C CB  . SER A 1 287 ? 14.334  -25.468 18.471  1.00 27.23 ? 287 SER A CB  1 
ATOM   994  O OG  . SER A 1 287 ? 13.034  -26.009 18.275  1.00 28.88 ? 287 SER A OG  1 
ATOM   995  N N   . GLY A 1 288 ? 13.040  -24.295 15.608  1.00 24.45 ? 288 GLY A N   1 
ATOM   996  C CA  . GLY A 1 288 ? 12.606  -24.659 14.261  1.00 24.20 ? 288 GLY A CA  1 
ATOM   997  C C   . GLY A 1 288 ? 11.703  -25.877 14.218  1.00 23.47 ? 288 GLY A C   1 
ATOM   998  O O   . GLY A 1 288 ? 11.186  -26.231 13.153  1.00 24.40 ? 288 GLY A O   1 
ATOM   999  N N   . HIS A 1 289 ? 11.517  -26.546 15.368  1.00 21.64 ? 289 HIS A N   1 
ATOM   1000 C CA  . HIS A 1 289 ? 10.668  -27.732 15.401  1.00 21.62 ? 289 HIS A CA  1 
ATOM   1001 C C   . HIS A 1 289 ? 9.223   -27.352 15.688  1.00 20.62 ? 289 HIS A C   1 
ATOM   1002 O O   . HIS A 1 289 ? 8.951   -26.331 16.319  1.00 20.53 ? 289 HIS A O   1 
ATOM   1003 C CB  . HIS A 1 289 ? 11.151  -28.716 16.466  1.00 23.99 ? 289 HIS A CB  1 
ATOM   1004 C CG  . HIS A 1 289 ? 12.540  -29.219 16.223  1.00 27.51 ? 289 HIS A CG  1 
ATOM   1005 N ND1 . HIS A 1 289 ? 12.820  -30.099 15.189  1.00 31.01 ? 289 HIS A ND1 1 
ATOM   1006 C CD2 . HIS A 1 289 ? 13.686  -28.943 16.889  1.00 29.06 ? 289 HIS A CD2 1 
ATOM   1007 C CE1 . HIS A 1 289 ? 14.129  -30.333 15.256  1.00 31.59 ? 289 HIS A CE1 1 
ATOM   1008 N NE2 . HIS A 1 289 ? 14.695  -29.657 16.262  1.00 30.70 ? 289 HIS A NE2 1 
ATOM   1009 N N   . ILE A 1 290 ? 8.304   -28.195 15.215  1.00 19.80 ? 290 ILE A N   1 
ATOM   1010 C CA  . ILE A 1 290 ? 6.888   -28.105 15.493  1.00 18.85 ? 290 ILE A CA  1 
ATOM   1011 C C   . ILE A 1 290 ? 6.513   -29.384 16.207  1.00 19.32 ? 290 ILE A C   1 
ATOM   1012 O O   . ILE A 1 290 ? 6.871   -30.468 15.758  1.00 19.64 ? 290 ILE A O   1 
ATOM   1013 C CB  . ILE A 1 290 ? 6.048   -27.946 14.192  1.00 18.94 ? 290 ILE A CB  1 
ATOM   1014 C CG1 . ILE A 1 290 ? 6.251   -26.539 13.595  1.00 19.11 ? 290 ILE A CG1 1 
ATOM   1015 C CG2 . ILE A 1 290 ? 4.544   -28.178 14.477  1.00 19.13 ? 290 ILE A CG2 1 
ATOM   1016 C CD1 . ILE A 1 290 ? 6.014   -26.529 12.049  1.00 20.91 ? 290 ILE A CD1 1 
ATOM   1017 N N   . HIS A 1 291 ? 5.765   -29.277 17.311  1.00 18.70 ? 291 HIS A N   1 
ATOM   1018 C CA  . HIS A 1 291 ? 5.307   -30.472 18.010  1.00 19.40 ? 291 HIS A CA  1 
ATOM   1019 C C   . HIS A 1 291 ? 3.797   -30.483 17.986  1.00 20.02 ? 291 HIS A C   1 
ATOM   1020 O O   . HIS A 1 291 ? 3.172   -29.423 18.101  1.00 20.04 ? 291 HIS A O   1 
ATOM   1021 C CB  . HIS A 1 291 ? 5.774   -30.438 19.474  1.00 20.45 ? 291 HIS A CB  1 
ATOM   1022 C CG  . HIS A 1 291 ? 7.243   -30.689 19.671  1.00 22.48 ? 291 HIS A CG  1 
ATOM   1023 N ND1 . HIS A 1 291 ? 7.800   -30.701 20.935  1.00 24.30 ? 291 HIS A ND1 1 
ATOM   1024 C CD2 . HIS A 1 291 ? 8.229   -30.891 18.761  1.00 22.79 ? 291 HIS A CD2 1 
ATOM   1025 C CE1 . HIS A 1 291 ? 9.088   -30.946 20.762  1.00 24.81 ? 291 HIS A CE1 1 
ATOM   1026 N NE2 . HIS A 1 291 ? 9.396   -31.073 19.473  1.00 23.54 ? 291 HIS A NE2 1 
ATOM   1027 N N   . HIS A 1 292 ? 3.210   -31.676 17.849  1.00 19.74 ? 292 HIS A N   1 
ATOM   1028 C CA  . HIS A 1 292 ? 1.789   -31.856 17.975  1.00 20.47 ? 292 HIS A CA  1 
ATOM   1029 C C   . HIS A 1 292 ? 1.584   -32.391 19.400  1.00 20.73 ? 292 HIS A C   1 
ATOM   1030 O O   . HIS A 1 292 ? 2.210   -33.403 19.778  1.00 21.41 ? 292 HIS A O   1 
ATOM   1031 C CB  . HIS A 1 292 ? 1.261   -32.907 16.984  1.00 22.01 ? 292 HIS A CB  1 
ATOM   1032 C CG  . HIS A 1 292 ? 1.230   -32.439 15.564  1.00 22.41 ? 292 HIS A CG  1 
ATOM   1033 N ND1 . HIS A 1 292 ? 1.041   -31.096 15.246  1.00 22.82 ? 292 HIS A ND1 1 
ATOM   1034 C CD2 . HIS A 1 292 ? 1.293   -33.158 14.416  1.00 23.46 ? 292 HIS A CD2 1 
ATOM   1035 C CE1 . HIS A 1 292 ? 1.045   -31.042 13.922  1.00 23.75 ? 292 HIS A CE1 1 
ATOM   1036 N NE2 . HIS A 1 292 ? 1.181   -32.258 13.380  1.00 23.93 ? 292 HIS A NE2 1 
ATOM   1037 N N   . HIS A 1 293 ? 0.668   -31.774 20.139  1.00 19.64 ? 293 HIS A N   1 
ATOM   1038 C CA  . HIS A 1 293 ? 0.312   -32.197 21.494  1.00 19.67 ? 293 HIS A CA  1 
ATOM   1039 C C   . HIS A 1 293 ? -1.143  -32.691 21.545  1.00 21.07 ? 293 HIS A C   1 
ATOM   1040 O O   . HIS A 1 293 ? -2.045  -31.936 21.172  1.00 21.46 ? 293 HIS A O   1 
ATOM   1041 C CB  . HIS A 1 293 ? 0.441   -31.026 22.503  1.00 18.74 ? 293 HIS A CB  1 
ATOM   1042 C CG  . HIS A 1 293 ? 1.753   -30.319 22.462  1.00 18.90 ? 293 HIS A CG  1 
ATOM   1043 N ND1 . HIS A 1 293 ? 2.862   -30.802 23.157  1.00 21.36 ? 293 HIS A ND1 1 
ATOM   1044 C CD2 . HIS A 1 293 ? 2.106   -29.207 21.784  1.00 19.05 ? 293 HIS A CD2 1 
ATOM   1045 C CE1 . HIS A 1 293 ? 3.850   -29.966 22.883  1.00 21.60 ? 293 HIS A CE1 1 
ATOM   1046 N NE2 . HIS A 1 293 ? 3.444   -28.984 22.051  1.00 21.12 ? 293 HIS A NE2 1 
ATOM   1047 N N   . ASP A 1 294 ? -1.380  -33.937 21.996  1.00 21.27 ? 294 ASP A N   1 
ATOM   1048 C CA  . ASP A 1 294 ? -2.748  -34.401 22.197  1.00 21.65 ? 294 ASP A CA  1 
ATOM   1049 C C   . ASP A 1 294 ? -2.984  -33.947 23.643  1.00 21.25 ? 294 ASP A C   1 
ATOM   1050 O O   . ASP A 1 294 ? -2.510  -34.595 24.567  1.00 21.35 ? 294 ASP A O   1 
ATOM   1051 C CB  . ASP A 1 294 ? -2.873  -35.931 22.072  1.00 23.48 ? 294 ASP A CB  1 
ATOM   1052 C CG  . ASP A 1 294 ? -4.300  -36.437 22.289  1.00 28.90 ? 294 ASP A CG  1 
ATOM   1053 O OD1 . ASP A 1 294 ? -5.118  -35.692 22.910  1.00 29.46 ? 294 ASP A OD1 1 
ATOM   1054 O OD2 . ASP A 1 294 ? -4.603  -37.575 21.846  1.00 30.48 ? 294 ASP A OD2 1 
ATOM   1055 N N   . VAL A 1 295 ? -3.676  -32.818 23.839  1.00 20.68 ? 295 VAL A N   1 
ATOM   1056 C CA  . VAL A 1 295 ? -3.850  -32.260 25.197  1.00 21.08 ? 295 VAL A CA  1 
ATOM   1057 C C   . VAL A 1 295 ? -4.703  -33.130 26.136  1.00 23.15 ? 295 VAL A C   1 
ATOM   1058 O O   . VAL A 1 295 ? -4.710  -32.887 27.350  1.00 23.67 ? 295 VAL A O   1 
ATOM   1059 C CB  . VAL A 1 295 ? -4.378  -30.812 25.146  1.00 21.17 ? 295 VAL A CB  1 
ATOM   1060 C CG1 . VAL A 1 295 ? -3.519  -29.960 24.195  1.00 21.38 ? 295 VAL A CG1 1 
ATOM   1061 C CG2 . VAL A 1 295 ? -5.842  -30.783 24.723  1.00 21.27 ? 295 VAL A CG2 1 
ATOM   1062 N N   . ARG A 1 296 ? -5.370  -34.175 25.606  1.00 23.66 ? 296 ARG A N   1 
ATOM   1063 C CA  . ARG A 1 296 ? -6.202  -35.040 26.447  1.00 24.83 ? 296 ARG A CA  1 
ATOM   1064 C C   . ARG A 1 296 ? -5.419  -36.151 27.150  1.00 25.39 ? 296 ARG A C   1 
ATOM   1065 O O   . ARG A 1 296 ? -5.983  -36.805 28.045  1.00 26.44 ? 296 ARG A O   1 
ATOM   1066 C CB  . ARG A 1 296 ? -7.275  -35.753 25.601  1.00 27.20 ? 296 ARG A CB  1 
ATOM   1067 C CG  . ARG A 1 296 ? -8.056  -34.874 24.637  1.00 30.32 ? 296 ARG A CG  1 
ATOM   1068 C CD  . ARG A 1 296 ? -8.795  -35.746 23.616  1.00 33.47 ? 296 ARG A CD  1 
ATOM   1069 N NE  . ARG A 1 296 ? -7.875  -36.563 22.812  1.00 34.47 ? 296 ARG A NE  1 
ATOM   1070 C CZ  . ARG A 1 296 ? -8.238  -37.646 22.125  1.00 34.97 ? 296 ARG A CZ  1 
ATOM   1071 N NH1 . ARG A 1 296 ? -7.331  -38.345 21.445  1.00 32.40 ? 296 ARG A NH1 1 
ATOM   1072 N NH2 . ARG A 1 296 ? -9.513  -38.030 22.100  1.00 33.90 ? 296 ARG A NH2 1 
ATOM   1073 N N   . VAL A 1 297 ? -4.177  -36.433 26.717  1.00 25.34 ? 297 VAL A N   1 
ATOM   1074 C CA  . VAL A 1 297 ? -3.454  -37.588 27.258  1.00 27.39 ? 297 VAL A CA  1 
ATOM   1075 C C   . VAL A 1 297 ? -2.139  -37.264 27.981  1.00 27.62 ? 297 VAL A C   1 
ATOM   1076 O O   . VAL A 1 297 ? -1.535  -36.223 27.739  1.00 26.09 ? 297 VAL A O   1 
ATOM   1077 C CB  . VAL A 1 297 ? -3.227  -38.630 26.138  1.00 28.70 ? 297 VAL A CB  1 
ATOM   1078 C CG1 . VAL A 1 297 ? -4.560  -39.021 25.500  1.00 29.93 ? 297 VAL A CG1 1 
ATOM   1079 C CG2 . VAL A 1 297 ? -2.242  -38.121 25.083  1.00 29.24 ? 297 VAL A CG2 1 
ATOM   1080 N N   . ALA A 1 298 ? -1.705  -38.189 28.862  1.00 27.86 ? 298 ALA A N   1 
ATOM   1081 C CA  . ALA A 1 298 ? -0.488  -38.089 29.675  1.00 28.64 ? 298 ALA A CA  1 
ATOM   1082 C C   . ALA A 1 298 ? 0.789   -37.788 28.837  1.00 29.17 ? 298 ALA A C   1 
ATOM   1083 O O   . ALA A 1 298 ? 1.436   -36.775 29.085  1.00 30.23 ? 298 ALA A O   1 
ATOM   1084 C CB  . ALA A 1 298 ? -0.314  -39.355 30.515  1.00 28.78 ? 298 ALA A CB  1 
ATOM   1085 N N   . GLU A 1 299 ? 1.117   -38.603 27.825  1.00 28.85 ? 299 GLU A N   1 
ATOM   1086 C CA  . GLU A 1 299 ? 2.283   -38.327 26.979  1.00 29.56 ? 299 GLU A CA  1 
ATOM   1087 C C   . GLU A 1 299 ? 1.723   -37.514 25.836  1.00 29.16 ? 299 GLU A C   1 
ATOM   1088 O O   . GLU A 1 299 ? 1.345   -38.052 24.795  1.00 30.22 ? 299 GLU A O   1 
ATOM   1089 C CB  . GLU A 1 299 ? 2.979   -39.602 26.486  1.00 33.95 ? 299 GLU A CB  1 
ATOM   1090 N N   . HIS A 1 300 ? 1.586   -36.223 26.078  1.00 27.72 ? 300 HIS A N   1 
ATOM   1091 C CA  . HIS A 1 300 ? 0.995   -35.272 25.138  1.00 27.26 ? 300 HIS A CA  1 
ATOM   1092 C C   . HIS A 1 300 ? 1.737   -35.190 23.808  1.00 26.95 ? 300 HIS A C   1 
ATOM   1093 O O   . HIS A 1 300 ? 1.110   -34.995 22.782  1.00 26.52 ? 300 HIS A O   1 
ATOM   1094 C CB  . HIS A 1 300 ? 0.941   -33.874 25.780  1.00 27.13 ? 300 HIS A CB  1 
ATOM   1095 C CG  . HIS A 1 300 ? 2.298   -33.355 26.155  1.00 28.08 ? 300 HIS A CG  1 
ATOM   1096 N ND1 . HIS A 1 300 ? 3.095   -32.676 25.238  1.00 29.46 ? 300 HIS A ND1 1 
ATOM   1097 C CD2 . HIS A 1 300 ? 2.985   -33.488 27.317  1.00 29.02 ? 300 HIS A CD2 1 
ATOM   1098 C CE1 . HIS A 1 300 ? 4.219   -32.394 25.881  1.00 30.00 ? 300 HIS A CE1 1 
ATOM   1099 N NE2 . HIS A 1 300 ? 4.193   -32.851 27.140  1.00 29.67 ? 300 HIS A NE2 1 
ATOM   1100 N N   . HIS A 1 301 ? 3.060   -35.328 23.824  1.00 26.79 ? 301 HIS A N   1 
ATOM   1101 C CA  . HIS A 1 301 ? 3.868   -35.166 22.620  1.00 27.04 ? 301 HIS A CA  1 
ATOM   1102 C C   . HIS A 1 301 ? 3.758   -36.364 21.666  1.00 28.34 ? 301 HIS A C   1 
ATOM   1103 O O   . HIS A 1 301 ? 4.407   -37.391 21.864  1.00 28.98 ? 301 HIS A O   1 
ATOM   1104 C CB  . HIS A 1 301 ? 5.307   -34.838 23.013  1.00 26.83 ? 301 HIS A CB  1 
ATOM   1105 C CG  . HIS A 1 301 ? 6.190   -34.480 21.862  1.00 27.88 ? 301 HIS A CG  1 
ATOM   1106 N ND1 . HIS A 1 301 ? 7.560   -34.602 21.958  1.00 29.39 ? 301 HIS A ND1 1 
ATOM   1107 C CD2 . HIS A 1 301 ? 5.872   -34.021 20.628  1.00 28.54 ? 301 HIS A CD2 1 
ATOM   1108 C CE1 . HIS A 1 301 ? 8.043   -34.217 20.783  1.00 29.40 ? 301 HIS A CE1 1 
ATOM   1109 N NE2 . HIS A 1 301 ? 7.068   -33.858 19.948  1.00 29.47 ? 301 HIS A NE2 1 
ATOM   1110 N N   . VAL A 1 302 ? 2.923   -36.225 20.619  1.00 28.37 ? 302 VAL A N   1 
ATOM   1111 C CA  . VAL A 1 302 ? 2.643   -37.331 19.702  1.00 29.06 ? 302 VAL A CA  1 
ATOM   1112 C C   . VAL A 1 302 ? 3.280   -37.214 18.329  1.00 29.46 ? 302 VAL A C   1 
ATOM   1113 O O   . VAL A 1 302 ? 3.181   -38.158 17.546  1.00 30.21 ? 302 VAL A O   1 
ATOM   1114 C CB  . VAL A 1 302 ? 1.125   -37.537 19.563  1.00 29.76 ? 302 VAL A CB  1 
ATOM   1115 C CG1 . VAL A 1 302 ? 0.512   -37.929 20.909  1.00 30.25 ? 302 VAL A CG1 1 
ATOM   1116 C CG2 . VAL A 1 302 ? 0.462   -36.272 19.009  1.00 30.34 ? 302 VAL A CG2 1 
ATOM   1117 N N   . ALA A 1 303 ? 3.881   -36.070 18.002  1.00 28.62 ? 303 ALA A N   1 
ATOM   1118 C CA  . ALA A 1 303 ? 4.526   -35.903 16.696  1.00 28.55 ? 303 ALA A CA  1 
ATOM   1119 C C   . ALA A 1 303 ? 5.525   -34.762 16.731  1.00 27.42 ? 303 ALA A C   1 
ATOM   1120 O O   . ALA A 1 303 ? 5.334   -33.792 17.455  1.00 26.61 ? 303 ALA A O   1 
ATOM   1121 C CB  . ALA A 1 303 ? 3.482   -35.617 15.609  1.00 28.83 ? 303 ALA A CB  1 
ATOM   1122 N N   . THR A 1 304 ? 6.558   -34.861 15.895  1.00 26.19 ? 304 THR A N   1 
ATOM   1123 C CA  . THR A 1 304 ? 7.550   -33.801 15.722  1.00 26.25 ? 304 THR A CA  1 
ATOM   1124 C C   . THR A 1 304 ? 7.686   -33.575 14.220  1.00 25.44 ? 304 THR A C   1 
ATOM   1125 O O   . THR A 1 304 ? 7.993   -34.509 13.480  1.00 26.35 ? 304 THR A O   1 
ATOM   1126 C CB  . THR A 1 304 ? 8.917   -34.204 16.318  1.00 28.18 ? 304 THR A CB  1 
ATOM   1127 O OG1 . THR A 1 304 ? 8.777   -34.306 17.734  1.00 28.63 ? 304 THR A OG1 1 
ATOM   1128 C CG2 . THR A 1 304 ? 9.999   -33.174 16.015  1.00 28.89 ? 304 THR A CG2 1 
ATOM   1129 N N   . LEU A 1 305 ? 7.443   -32.347 13.771  1.00 23.74 ? 305 LEU A N   1 
ATOM   1130 C CA  . LEU A 1 305 ? 7.521   -31.942 12.370  1.00 23.01 ? 305 LEU A CA  1 
ATOM   1131 C C   . LEU A 1 305 ? 8.751   -31.055 12.262  1.00 23.47 ? 305 LEU A C   1 
ATOM   1132 O O   . LEU A 1 305 ? 8.799   -29.999 12.894  1.00 23.18 ? 305 LEU A O   1 
ATOM   1133 C CB  . LEU A 1 305 ? 6.264   -31.167 11.963  1.00 22.96 ? 305 LEU A CB  1 
ATOM   1134 C CG  . LEU A 1 305 ? 4.973   -31.949 11.668  1.00 24.16 ? 305 LEU A CG  1 
ATOM   1135 C CD1 . LEU A 1 305 ? 4.582   -32.913 12.816  1.00 24.89 ? 305 LEU A CD1 1 
ATOM   1136 C CD2 . LEU A 1 305 ? 3.812   -31.005 11.388  1.00 24.07 ? 305 LEU A CD2 1 
ATOM   1137 N N   . SER A 1 306 ? 9.776   -31.499 11.523  1.00 23.43 ? 306 SER A N   1 
ATOM   1138 C CA  . SER A 1 306 ? 11.029  -30.752 11.441  1.00 24.17 ? 306 SER A CA  1 
ATOM   1139 C C   . SER A 1 306 ? 11.325  -30.312 10.023  1.00 24.76 ? 306 SER A C   1 
ATOM   1140 O O   . SER A 1 306 ? 11.977  -31.039 9.283   1.00 25.58 ? 306 SER A O   1 
ATOM   1141 C CB  . SER A 1 306 ? 12.195  -31.591 11.961  1.00 26.21 ? 306 SER A CB  1 
ATOM   1142 O OG  . SER A 1 306 ? 11.954  -31.944 13.313  1.00 30.31 ? 306 SER A OG  1 
ATOM   1143 N N   . GLY A 1 307 ? 10.840  -29.134 9.661   1.00 24.12 ? 307 GLY A N   1 
ATOM   1144 C CA  . GLY A 1 307 ? 11.063  -28.582 8.332   1.00 23.72 ? 307 GLY A CA  1 
ATOM   1145 C C   . GLY A 1 307 ? 11.605  -27.159 8.342   1.00 23.69 ? 307 GLY A C   1 
ATOM   1146 O O   . GLY A 1 307 ? 11.634  -26.510 7.293   1.00 24.28 ? 307 GLY A O   1 
ATOM   1147 N N   . HIS A 1 308 ? 12.021  -26.641 9.519   1.00 22.57 ? 308 HIS A N   1 
ATOM   1148 C CA  . HIS A 1 308 ? 12.583  -25.286 9.591   1.00 22.50 ? 308 HIS A CA  1 
ATOM   1149 C C   . HIS A 1 308 ? 13.929  -25.281 10.300  1.00 24.51 ? 308 HIS A C   1 
ATOM   1150 O O   . HIS A 1 308 ? 14.132  -26.040 11.247  1.00 26.11 ? 308 HIS A O   1 
ATOM   1151 C CB  . HIS A 1 308 ? 11.637  -24.295 10.286  1.00 21.33 ? 308 HIS A CB  1 
ATOM   1152 C CG  . HIS A 1 308 ? 10.346  -24.036 9.567   1.00 20.08 ? 308 HIS A CG  1 
ATOM   1153 N ND1 . HIS A 1 308 ? 10.230  -23.014 8.646   1.00 21.21 ? 308 HIS A ND1 1 
ATOM   1154 C CD2 . HIS A 1 308 ? 9.133   -24.614 9.732   1.00 20.15 ? 308 HIS A CD2 1 
ATOM   1155 C CE1 . HIS A 1 308 ? 8.961   -23.033 8.241   1.00 20.66 ? 308 HIS A CE1 1 
ATOM   1156 N NE2 . HIS A 1 308 ? 8.272   -23.998 8.844   1.00 20.25 ? 308 HIS A NE2 1 
ATOM   1157 N N   . SER A 1 309 ? 14.845  -24.412 9.869   1.00 25.21 ? 309 SER A N   1 
ATOM   1158 C CA  . SER A 1 309 ? 16.166  -24.318 10.518  1.00 25.85 ? 309 SER A CA  1 
ATOM   1159 C C   . SER A 1 309 ? 16.286  -23.100 11.440  1.00 26.23 ? 309 SER A C   1 
ATOM   1160 O O   . SER A 1 309 ? 17.338  -22.917 12.066  1.00 27.49 ? 309 SER A O   1 
ATOM   1161 C CB  . SER A 1 309 ? 17.277  -24.275 9.476   1.00 27.39 ? 309 SER A CB  1 
ATOM   1162 O OG  . SER A 1 309 ? 17.058  -23.170 8.617   1.00 29.70 ? 309 SER A OG  1 
ATOM   1163 N N   . GLN A 1 310 ? 15.246  -22.238 11.476  1.00 24.25 ? 310 GLN A N   1 
ATOM   1164 C CA  . GLN A 1 310 ? 15.137  -21.041 12.309  1.00 22.94 ? 310 GLN A CA  1 
ATOM   1165 C C   . GLN A 1 310 ? 13.726  -21.012 12.964  1.00 21.68 ? 310 GLN A C   1 
ATOM   1166 O O   . GLN A 1 310 ? 12.886  -21.852 12.668  1.00 21.24 ? 310 GLN A O   1 
ATOM   1167 C CB  . GLN A 1 310 ? 15.401  -19.764 11.494  1.00 23.14 ? 310 GLN A CB  1 
ATOM   1168 C CG  . GLN A 1 310 ? 16.795  -19.737 10.823  1.00 27.02 ? 310 GLN A CG  1 
ATOM   1169 C CD  . GLN A 1 310 ? 17.963  -19.643 11.784  1.00 32.64 ? 310 GLN A CD  1 
ATOM   1170 O OE1 . GLN A 1 310 ? 17.848  -19.157 12.913  1.00 35.91 ? 310 GLN A OE1 1 
ATOM   1171 N NE2 . GLN A 1 310 ? 19.130  -20.104 11.347  1.00 34.16 ? 310 GLN A NE2 1 
ATOM   1172 N N   . GLU A 1 311 ? 13.462  -20.006 13.781  1.00 21.15 ? 311 GLU A N   1 
ATOM   1173 C CA  . GLU A 1 311 ? 12.220  -19.892 14.543  1.00 20.19 ? 311 GLU A CA  1 
ATOM   1174 C C   . GLU A 1 311 ? 10.927  -20.064 13.736  1.00 19.98 ? 311 GLU A C   1 
ATOM   1175 O O   . GLU A 1 311 ? 10.752  -19.456 12.673  1.00 19.99 ? 311 GLU A O   1 
ATOM   1176 C CB  . GLU A 1 311 ? 12.185  -18.551 15.296  1.00 21.01 ? 311 GLU A CB  1 
ATOM   1177 C CG  . GLU A 1 311 ? 10.950  -18.412 16.186  1.00 22.93 ? 311 GLU A CG  1 
ATOM   1178 C CD  . GLU A 1 311 ? 11.104  -17.508 17.395  1.00 26.93 ? 311 GLU A CD  1 
ATOM   1179 O OE1 . GLU A 1 311 ? 10.390  -17.722 18.408  1.00 24.92 ? 311 GLU A OE1 1 
ATOM   1180 O OE2 . GLU A 1 311 ? 11.952  -16.589 17.330  1.00 28.12 ? 311 GLU A OE2 1 
ATOM   1181 N N   . VAL A 1 312 ? 10.007  -20.881 14.252  1.00 19.50 ? 312 VAL A N   1 
ATOM   1182 C CA  . VAL A 1 312 ? 8.702   -21.044 13.603  1.00 18.91 ? 312 VAL A CA  1 
ATOM   1183 C C   . VAL A 1 312 ? 7.818   -19.910 14.143  1.00 19.06 ? 312 VAL A C   1 
ATOM   1184 O O   . VAL A 1 312 ? 7.362   -19.989 15.290  1.00 20.50 ? 312 VAL A O   1 
ATOM   1185 C CB  . VAL A 1 312 ? 8.079   -22.421 13.886  1.00 19.75 ? 312 VAL A CB  1 
ATOM   1186 C CG1 . VAL A 1 312 ? 6.704   -22.508 13.216  1.00 19.46 ? 312 VAL A CG1 1 
ATOM   1187 C CG2 . VAL A 1 312 ? 9.004   -23.543 13.407  1.00 20.84 ? 312 VAL A CG2 1 
ATOM   1188 N N   . CYS A 1 313 ? 7.591   -18.861 13.349  1.00 17.87 ? 313 CYS A N   1 
ATOM   1189 C CA  . CYS A 1 313 ? 6.822   -17.692 13.788  1.00 18.21 ? 313 CYS A CA  1 
ATOM   1190 C C   . CYS A 1 313 ? 5.374   -17.650 13.296  1.00 18.72 ? 313 CYS A C   1 
ATOM   1191 O O   . CYS A 1 313 ? 4.592   -16.827 13.802  1.00 19.48 ? 313 CYS A O   1 
ATOM   1192 C CB  . CYS A 1 313 ? 7.545   -16.395 13.452  1.00 19.49 ? 313 CYS A CB  1 
ATOM   1193 S SG  . CYS A 1 313 ? 8.207   -16.331 11.764  1.00 23.97 ? 313 CYS A SG  1 
ATOM   1194 N N   . GLY A 1 314 ? 5.028   -18.463 12.296  1.00 17.32 ? 314 GLY A N   1 
ATOM   1195 C CA  . GLY A 1 314 ? 3.649   -18.489 11.817  1.00 17.11 ? 314 GLY A CA  1 
ATOM   1196 C C   . GLY A 1 314 ? 3.200   -19.929 11.789  1.00 16.24 ? 314 GLY A C   1 
ATOM   1197 O O   . GLY A 1 314 ? 3.968   -20.781 11.351  1.00 16.54 ? 314 GLY A O   1 
ATOM   1198 N N   . LEU A 1 315 ? 2.034   -20.237 12.374  1.00 15.24 ? 315 LEU A N   1 
ATOM   1199 C CA  . LEU A 1 315 ? 1.605   -21.644 12.433  1.00 15.23 ? 315 LEU A CA  1 
ATOM   1200 C C   . LEU A 1 315 ? 0.102   -21.644 12.384  1.00 15.21 ? 315 LEU A C   1 
ATOM   1201 O O   . LEU A 1 315 ? -0.532  -20.957 13.191  1.00 16.08 ? 315 LEU A O   1 
ATOM   1202 C CB  . LEU A 1 315 ? 2.126   -22.290 13.742  1.00 15.10 ? 315 LEU A CB  1 
ATOM   1203 C CG  . LEU A 1 315 ? 1.971   -23.813 13.901  1.00 17.56 ? 315 LEU A CG  1 
ATOM   1204 C CD1 . LEU A 1 315 ? 2.748   -24.577 12.804  1.00 19.11 ? 315 LEU A CD1 1 
ATOM   1205 C CD2 . LEU A 1 315 ? 2.481   -24.261 15.271  1.00 18.70 ? 315 LEU A CD2 1 
ATOM   1206 N N   . ARG A 1 316 ? -0.482  -22.344 11.381  1.00 14.36 ? 316 ARG A N   1 
ATOM   1207 C CA  . ARG A 1 316 ? -1.939  -22.281 11.226  1.00 14.82 ? 316 ARG A CA  1 
ATOM   1208 C C   . ARG A 1 316 ? -2.516  -23.508 10.566  1.00 14.73 ? 316 ARG A C   1 
ATOM   1209 O O   . ARG A 1 316 ? -2.230  -23.807 9.395   1.00 14.27 ? 316 ARG A O   1 
ATOM   1210 C CB  . ARG A 1 316 ? -2.299  -21.056 10.376  1.00 16.44 ? 316 ARG A CB  1 
ATOM   1211 C CG  . ARG A 1 316 ? -3.685  -20.475 10.648  1.00 19.77 ? 316 ARG A CG  1 
ATOM   1212 C CD  . ARG A 1 316 ? -3.631  -19.495 11.822  1.00 22.21 ? 316 ARG A CD  1 
ATOM   1213 N NE  . ARG A 1 316 ? -2.812  -18.343 11.459  1.00 23.36 ? 316 ARG A NE  1 
ATOM   1214 C CZ  . ARG A 1 316 ? -1.883  -17.797 12.232  1.00 27.19 ? 316 ARG A CZ  1 
ATOM   1215 N NH1 . ARG A 1 316 ? -1.746  -18.187 13.496  1.00 27.44 ? 316 ARG A NH1 1 
ATOM   1216 N NH2 . ARG A 1 316 ? -1.128  -16.809 11.772  1.00 26.81 ? 316 ARG A NH2 1 
ATOM   1217 N N   . TRP A 1 317 ? -3.400  -24.189 11.295  1.00 14.29 ? 317 TRP A N   1 
ATOM   1218 C CA  . TRP A 1 317 ? -4.127  -25.321 10.750  1.00 15.56 ? 317 TRP A CA  1 
ATOM   1219 C C   . TRP A 1 317 ? -5.209  -24.751 9.819   1.00 16.96 ? 317 TRP A C   1 
ATOM   1220 O O   . TRP A 1 317 ? -5.807  -23.708 10.129  1.00 17.15 ? 317 TRP A O   1 
ATOM   1221 C CB  . TRP A 1 317 ? -4.824  -26.075 11.900  1.00 16.27 ? 317 TRP A CB  1 
ATOM   1222 C CG  . TRP A 1 317 ? -3.948  -27.131 12.495  1.00 17.04 ? 317 TRP A CG  1 
ATOM   1223 C CD1 . TRP A 1 317 ? -3.246  -27.060 13.664  1.00 17.84 ? 317 TRP A CD1 1 
ATOM   1224 C CD2 . TRP A 1 317 ? -3.697  -28.424 11.949  1.00 18.05 ? 317 TRP A CD2 1 
ATOM   1225 N NE1 . TRP A 1 317 ? -2.591  -28.250 13.892  1.00 18.68 ? 317 TRP A NE1 1 
ATOM   1226 C CE2 . TRP A 1 317 ? -2.845  -29.102 12.846  1.00 18.89 ? 317 TRP A CE2 1 
ATOM   1227 C CE3 . TRP A 1 317 ? -4.116  -29.087 10.783  1.00 19.56 ? 317 TRP A CE3 1 
ATOM   1228 C CZ2 . TRP A 1 317 ? -2.423  -30.414 12.624  1.00 20.18 ? 317 TRP A CZ2 1 
ATOM   1229 C CZ3 . TRP A 1 317 ? -3.664  -30.373 10.547  1.00 20.80 ? 317 TRP A CZ3 1 
ATOM   1230 C CH2 . TRP A 1 317 ? -2.874  -31.039 11.485  1.00 21.12 ? 317 TRP A CH2 1 
ATOM   1231 N N   . ALA A 1 318 ? -5.486  -25.447 8.713   1.00 17.78 ? 318 ALA A N   1 
ATOM   1232 C CA  . ALA A 1 318 ? -6.567  -25.038 7.825   1.00 19.48 ? 318 ALA A CA  1 
ATOM   1233 C C   . ALA A 1 318 ? -7.916  -25.260 8.551   1.00 21.16 ? 318 ALA A C   1 
ATOM   1234 O O   . ALA A 1 318 ? -8.032  -26.190 9.362   1.00 20.95 ? 318 ALA A O   1 
ATOM   1235 C CB  . ALA A 1 318 ? -6.531  -25.889 6.572   1.00 20.01 ? 318 ALA A CB  1 
ATOM   1236 N N   . PRO A 1 319 ? -8.959  -24.457 8.250   1.00 23.93 ? 319 PRO A N   1 
ATOM   1237 C CA  . PRO A 1 319 ? -10.264 -24.659 8.914   1.00 25.19 ? 319 PRO A CA  1 
ATOM   1238 C C   . PRO A 1 319 ? -10.853 -26.058 8.727   1.00 25.55 ? 319 PRO A C   1 
ATOM   1239 O O   . PRO A 1 319 ? -11.528 -26.546 9.623   1.00 26.73 ? 319 PRO A O   1 
ATOM   1240 C CB  . PRO A 1 319 ? -11.153 -23.576 8.303   1.00 26.94 ? 319 PRO A CB  1 
ATOM   1241 C CG  . PRO A 1 319 ? -10.198 -22.545 7.769   1.00 27.45 ? 319 PRO A CG  1 
ATOM   1242 C CD  . PRO A 1 319 ? -8.981  -23.288 7.349   1.00 24.95 ? 319 PRO A CD  1 
ATOM   1243 N N   . ASP A 1 320 ? -10.549 -26.734 7.613   1.00 24.85 ? 320 ASP A N   1 
ATOM   1244 C CA  . ASP A 1 320 ? -11.022 -28.107 7.391   1.00 24.82 ? 320 ASP A CA  1 
ATOM   1245 C C   . ASP A 1 320 ? -10.115 -29.207 7.996   1.00 25.00 ? 320 ASP A C   1 
ATOM   1246 O O   . ASP A 1 320 ? -10.398 -30.398 7.824   1.00 25.19 ? 320 ASP A O   1 
ATOM   1247 C CB  . ASP A 1 320 ? -11.265 -28.368 5.895   1.00 24.65 ? 320 ASP A CB  1 
ATOM   1248 C CG  . ASP A 1 320 ? -10.031 -28.340 5.002   1.00 29.95 ? 320 ASP A CG  1 
ATOM   1249 O OD1 . ASP A 1 320 ? -8.887  -28.234 5.542   1.00 27.88 ? 320 ASP A OD1 1 
ATOM   1250 O OD2 . ASP A 1 320 ? -10.196 -28.425 3.768   1.00 32.09 ? 320 ASP A OD2 1 
ATOM   1251 N N   . GLY A 1 321 ? -9.013  -28.805 8.624   1.00 24.54 ? 321 GLY A N   1 
ATOM   1252 C CA  . GLY A 1 321 ? -8.051  -29.711 9.239   1.00 25.81 ? 321 GLY A CA  1 
ATOM   1253 C C   . GLY A 1 321 ? -7.247  -30.587 8.293   1.00 27.13 ? 321 GLY A C   1 
ATOM   1254 O O   . GLY A 1 321 ? -6.540  -31.486 8.748   1.00 28.85 ? 321 GLY A O   1 
ATOM   1255 N N   . ARG A 1 322 ? -7.316  -30.342 6.986   1.00 25.93 ? 322 ARG A N   1 
ATOM   1256 C CA  . ARG A 1 322 ? -6.601  -31.157 5.999   1.00 26.00 ? 322 ARG A CA  1 
ATOM   1257 C C   . ARG A 1 322 ? -5.124  -30.791 5.832   1.00 24.20 ? 322 ARG A C   1 
ATOM   1258 O O   . ARG A 1 322 ? -4.353  -31.590 5.304   1.00 24.40 ? 322 ARG A O   1 
ATOM   1259 C CB  . ARG A 1 322 ? -7.313  -31.087 4.648   1.00 28.55 ? 322 ARG A CB  1 
ATOM   1260 C CG  . ARG A 1 322 ? -8.645  -31.828 4.612   1.00 33.72 ? 322 ARG A CG  1 
ATOM   1261 C CD  . ARG A 1 322 ? -9.400  -31.597 3.304   1.00 39.25 ? 322 ARG A CD  1 
ATOM   1262 N NE  . ARG A 1 322 ? -8.629  -31.978 2.114   1.00 43.55 ? 322 ARG A NE  1 
ATOM   1263 C CZ  . ARG A 1 322 ? -8.128  -31.114 1.232   1.00 46.26 ? 322 ARG A CZ  1 
ATOM   1264 N NH1 . ARG A 1 322 ? -8.300  -29.808 1.399   1.00 44.67 ? 322 ARG A NH1 1 
ATOM   1265 N NH2 . ARG A 1 322 ? -7.436  -31.549 0.188   1.00 47.84 ? 322 ARG A NH2 1 
ATOM   1266 N N   . HIS A 1 323 ? -4.734  -29.578 6.219   1.00 22.65 ? 323 HIS A N   1 
ATOM   1267 C CA  . HIS A 1 323 ? -3.332  -29.147 6.096   1.00 21.19 ? 323 HIS A CA  1 
ATOM   1268 C C   . HIS A 1 323 ? -2.943  -28.262 7.273   1.00 19.30 ? 323 HIS A C   1 
ATOM   1269 O O   . HIS A 1 323 ? -3.802  -27.594 7.838   1.00 19.35 ? 323 HIS A O   1 
ATOM   1270 C CB  . HIS A 1 323 ? -3.123  -28.313 4.816   1.00 22.51 ? 323 HIS A CB  1 
ATOM   1271 C CG  . HIS A 1 323 ? -3.444  -29.007 3.527   1.00 25.68 ? 323 HIS A CG  1 
ATOM   1272 N ND1 . HIS A 1 323 ? -4.691  -28.885 2.935   1.00 27.48 ? 323 HIS A ND1 1 
ATOM   1273 C CD2 . HIS A 1 323 ? -2.646  -29.750 2.722   1.00 27.54 ? 323 HIS A CD2 1 
ATOM   1274 C CE1 . HIS A 1 323 ? -4.631  -29.594 1.814   1.00 28.15 ? 323 HIS A CE1 1 
ATOM   1275 N NE2 . HIS A 1 323 ? -3.424  -30.144 1.646   1.00 28.40 ? 323 HIS A NE2 1 
ATOM   1276 N N   . LEU A 1 324 ? -1.637  -28.179 7.575   1.00 17.33 ? 324 LEU A N   1 
ATOM   1277 C CA  . LEU A 1 324 ? -1.086  -27.264 8.571   1.00 16.87 ? 324 LEU A CA  1 
ATOM   1278 C C   . LEU A 1 324 ? -0.024  -26.436 7.855   1.00 17.15 ? 324 LEU A C   1 
ATOM   1279 O O   . LEU A 1 324 ? 0.858   -27.032 7.261   1.00 18.22 ? 324 LEU A O   1 
ATOM   1280 C CB  . LEU A 1 324 ? -0.438  -28.034 9.727   1.00 16.79 ? 324 LEU A CB  1 
ATOM   1281 C CG  . LEU A 1 324 ? 0.396   -27.234 10.702  1.00 18.48 ? 324 LEU A CG  1 
ATOM   1282 C CD1 . LEU A 1 324 ? -0.452  -26.230 11.455  1.00 18.80 ? 324 LEU A CD1 1 
ATOM   1283 C CD2 . LEU A 1 324 ? 1.076   -28.148 11.705  1.00 20.31 ? 324 LEU A CD2 1 
ATOM   1284 N N   . ALA A 1 325 ? -0.097  -25.100 7.916   1.00 15.93 ? 325 ALA A N   1 
ATOM   1285 C CA  . ALA A 1 325 ? 0.925   -24.258 7.304   1.00 17.34 ? 325 ALA A CA  1 
ATOM   1286 C C   . ALA A 1 325 ? 1.848   -23.713 8.381   1.00 16.74 ? 325 ALA A C   1 
ATOM   1287 O O   . ALA A 1 325 ? 1.395   -23.379 9.484   1.00 16.48 ? 325 ALA A O   1 
ATOM   1288 C CB  . ALA A 1 325 ? 0.271   -23.091 6.552   1.00 17.85 ? 325 ALA A CB  1 
ATOM   1289 N N   . SER A 1 326 ? 3.130   -23.633 8.075   1.00 16.14 ? 326 SER A N   1 
ATOM   1290 C CA  . SER A 1 326 ? 4.099   -23.041 8.987   1.00 16.13 ? 326 SER A CA  1 
ATOM   1291 C C   . SER A 1 326 ? 5.019   -22.103 8.251   1.00 17.08 ? 326 SER A C   1 
ATOM   1292 O O   . SER A 1 326 ? 5.372   -22.357 7.107   1.00 17.02 ? 326 SER A O   1 
ATOM   1293 C CB  . SER A 1 326 ? 4.902   -24.098 9.724   1.00 16.96 ? 326 SER A CB  1 
ATOM   1294 O OG  . SER A 1 326 ? 5.668   -24.885 8.830   1.00 18.90 ? 326 SER A OG  1 
ATOM   1295 N N   . GLY A 1 327 ? 5.315   -20.973 8.873   1.00 16.94 ? 327 GLY A N   1 
ATOM   1296 C CA  . GLY A 1 327 ? 6.220   -19.983 8.321   1.00 17.87 ? 327 GLY A CA  1 
ATOM   1297 C C   . GLY A 1 327 ? 7.356   -19.755 9.298   1.00 17.97 ? 327 GLY A C   1 
ATOM   1298 O O   . GLY A 1 327 ? 7.146   -19.791 10.521  1.00 17.60 ? 327 GLY A O   1 
ATOM   1299 N N   . GLY A 1 328 ? 8.549   -19.531 8.772   1.00 18.66 ? 328 GLY A N   1 
ATOM   1300 C CA  . GLY A 1 328 ? 9.709   -19.369 9.643   1.00 19.60 ? 328 GLY A CA  1 
ATOM   1301 C C   . GLY A 1 328 ? 10.627  -18.206 9.373   1.00 20.15 ? 328 GLY A C   1 
ATOM   1302 O O   . GLY A 1 328 ? 10.536  -17.544 8.337   1.00 20.14 ? 328 GLY A O   1 
ATOM   1303 N N   . ASN A 1 329 ? 11.534  -17.966 10.323  1.00 19.92 ? 329 ASN A N   1 
ATOM   1304 C CA  . ASN A 1 329 ? 12.574  -16.958 10.167  1.00 20.90 ? 329 ASN A CA  1 
ATOM   1305 C C   . ASN A 1 329 ? 13.690  -17.460 9.192   1.00 21.98 ? 329 ASN A C   1 
ATOM   1306 O O   . ASN A 1 329 ? 14.728  -16.816 9.054   1.00 23.63 ? 329 ASN A O   1 
ATOM   1307 C CB  . ASN A 1 329 ? 13.191  -16.615 11.514  1.00 21.48 ? 329 ASN A CB  1 
ATOM   1308 C CG  . ASN A 1 329 ? 14.040  -15.384 11.435  1.00 25.93 ? 329 ASN A CG  1 
ATOM   1309 O OD1 . ASN A 1 329 ? 13.720  -14.443 10.692  1.00 27.22 ? 329 ASN A OD1 1 
ATOM   1310 N ND2 . ASN A 1 329 ? 15.151  -15.372 12.171  1.00 26.58 ? 329 ASN A ND2 1 
ATOM   1311 N N   . ASP A 1 330 ? 13.512  -18.642 8.599   1.00 21.58 ? 330 ASP A N   1 
ATOM   1312 C CA  . ASP A 1 330 ? 14.401  -19.198 7.586   1.00 21.70 ? 330 ASP A CA  1 
ATOM   1313 C C   . ASP A 1 330 ? 13.818  -18.921 6.162   1.00 22.68 ? 330 ASP A C   1 
ATOM   1314 O O   . ASP A 1 330 ? 14.305  -19.495 5.179   1.00 23.07 ? 330 ASP A O   1 
ATOM   1315 C CB  . ASP A 1 330 ? 14.617  -20.705 7.817   1.00 22.53 ? 330 ASP A CB  1 
ATOM   1316 C CG  . ASP A 1 330 ? 13.336  -21.540 7.891   1.00 24.57 ? 330 ASP A CG  1 
ATOM   1317 O OD1 . ASP A 1 330 ? 12.231  -20.949 7.905   1.00 25.45 ? 330 ASP A OD1 1 
ATOM   1318 O OD2 . ASP A 1 330 ? 13.443  -22.780 7.909   1.00 26.30 ? 330 ASP A OD2 1 
ATOM   1319 N N   . ASN A 1 331 ? 12.819  -18.003 6.062   1.00 22.90 ? 331 ASN A N   1 
ATOM   1320 C CA  . ASN A 1 331 ? 12.166  -17.588 4.820   1.00 23.44 ? 331 ASN A CA  1 
ATOM   1321 C C   . ASN A 1 331 ? 11.414  -18.727 4.140   1.00 22.67 ? 331 ASN A C   1 
ATOM   1322 O O   . ASN A 1 331 ? 11.248  -18.672 2.921   1.00 23.99 ? 331 ASN A O   1 
ATOM   1323 C CB  . ASN A 1 331 ? 13.170  -16.964 3.830   1.00 25.71 ? 331 ASN A CB  1 
ATOM   1324 C CG  . ASN A 1 331 ? 14.242  -16.089 4.432   1.00 31.57 ? 331 ASN A CG  1 
ATOM   1325 O OD1 . ASN A 1 331 ? 14.012  -15.378 5.397   1.00 32.18 ? 331 ASN A OD1 1 
ATOM   1326 N ND2 . ASN A 1 331 ? 15.416  -16.094 3.826   1.00 34.52 ? 331 ASN A ND2 1 
ATOM   1327 N N   . LEU A 1 332 ? 11.055  -19.790 4.871   1.00 20.31 ? 332 LEU A N   1 
ATOM   1328 C CA  . LEU A 1 332 ? 10.325  -20.891 4.247   1.00 20.33 ? 332 LEU A CA  1 
ATOM   1329 C C   . LEU A 1 332 ? 8.873   -20.889 4.707   1.00 19.06 ? 332 LEU A C   1 
ATOM   1330 O O   . LEU A 1 332 ? 8.563   -20.503 5.839   1.00 18.37 ? 332 LEU A O   1 
ATOM   1331 C CB  . LEU A 1 332 ? 10.900  -22.247 4.664   1.00 21.61 ? 332 LEU A CB  1 
ATOM   1332 C CG  . LEU A 1 332 ? 12.315  -22.565 4.292   1.00 25.27 ? 332 LEU A CG  1 
ATOM   1333 C CD1 . LEU A 1 332 ? 12.690  -23.935 4.839   1.00 27.55 ? 332 LEU A CD1 1 
ATOM   1334 C CD2 . LEU A 1 332 ? 12.476  -22.571 2.777   1.00 26.47 ? 332 LEU A CD2 1 
ATOM   1335 N N   . VAL A 1 333 ? 8.014   -21.418 3.849   1.00 17.77 ? 333 VAL A N   1 
ATOM   1336 C CA  . VAL A 1 333 ? 6.653   -21.773 4.187   1.00 18.01 ? 333 VAL A CA  1 
ATOM   1337 C C   . VAL A 1 333 ? 6.560   -23.281 3.914   1.00 18.09 ? 333 VAL A C   1 
ATOM   1338 O O   . VAL A 1 333 ? 6.937   -23.728 2.835   1.00 18.40 ? 333 VAL A O   1 
ATOM   1339 C CB  . VAL A 1 333 ? 5.599   -21.031 3.356   1.00 18.47 ? 333 VAL A CB  1 
ATOM   1340 C CG1 . VAL A 1 333 ? 4.190   -21.555 3.660   1.00 19.16 ? 333 VAL A CG1 1 
ATOM   1341 C CG2 . VAL A 1 333 ? 5.688   -19.520 3.565   1.00 19.06 ? 333 VAL A CG2 1 
ATOM   1342 N N   . ASN A 1 334 ? 6.123   -24.064 4.892   1.00 17.26 ? 334 ASN A N   1 
ATOM   1343 C CA  . ASN A 1 334 ? 5.899   -25.490 4.685   1.00 17.57 ? 334 ASN A CA  1 
ATOM   1344 C C   . ASN A 1 334 ? 4.395   -25.738 4.822   1.00 17.79 ? 334 ASN A C   1 
ATOM   1345 O O   . ASN A 1 334 ? 3.737   -25.126 5.664   1.00 18.07 ? 334 ASN A O   1 
ATOM   1346 C CB  . ASN A 1 334 ? 6.628   -26.321 5.740   1.00 19.06 ? 334 ASN A CB  1 
ATOM   1347 C CG  . ASN A 1 334 ? 8.097   -26.433 5.511   1.00 21.78 ? 334 ASN A CG  1 
ATOM   1348 O OD1 . ASN A 1 334 ? 8.553   -26.961 4.489   1.00 23.36 ? 334 ASN A OD1 1 
ATOM   1349 N ND2 . ASN A 1 334 ? 8.878   -25.966 6.467   1.00 22.21 ? 334 ASN A ND2 1 
ATOM   1350 N N   . VAL A 1 335 ? 3.864   -26.661 4.018   1.00 17.96 ? 335 VAL A N   1 
ATOM   1351 C CA  . VAL A 1 335 ? 2.485   -27.083 4.149   1.00 18.96 ? 335 VAL A CA  1 
ATOM   1352 C C   . VAL A 1 335 ? 2.578   -28.556 4.475   1.00 19.38 ? 335 VAL A C   1 
ATOM   1353 O O   . VAL A 1 335 ? 3.101   -29.325 3.679   1.00 19.13 ? 335 VAL A O   1 
ATOM   1354 C CB  . VAL A 1 335 ? 1.677   -26.861 2.852   1.00 20.45 ? 335 VAL A CB  1 
ATOM   1355 C CG1 . VAL A 1 335 ? 0.264   -27.393 3.031   1.00 20.33 ? 335 VAL A CG1 1 
ATOM   1356 C CG2 . VAL A 1 335 ? 1.652   -25.365 2.494   1.00 21.23 ? 335 VAL A CG2 1 
ATOM   1357 N N   . TRP A 1 336 ? 2.092   -28.941 5.642   1.00 19.33 ? 336 TRP A N   1 
ATOM   1358 C CA  . TRP A 1 336 ? 2.198   -30.293 6.144   1.00 19.65 ? 336 TRP A CA  1 
ATOM   1359 C C   . TRP A 1 336 ? 0.895   -31.045 5.949   1.00 21.67 ? 336 TRP A C   1 
ATOM   1360 O O   . TRP A 1 336 ? -0.187  -30.457 6.022   1.00 21.87 ? 336 TRP A O   1 
ATOM   1361 C CB  . TRP A 1 336 ? 2.508   -30.219 7.677   1.00 19.08 ? 336 TRP A CB  1 
ATOM   1362 C CG  . TRP A 1 336 ? 3.735   -29.422 8.015   1.00 19.52 ? 336 TRP A CG  1 
ATOM   1363 C CD1 . TRP A 1 336 ? 3.811   -28.078 8.263   1.00 19.78 ? 336 TRP A CD1 1 
ATOM   1364 C CD2 . TRP A 1 336 ? 5.077   -29.920 8.087   1.00 20.22 ? 336 TRP A CD2 1 
ATOM   1365 N NE1 . TRP A 1 336 ? 5.112   -27.723 8.536   1.00 20.18 ? 336 TRP A NE1 1 
ATOM   1366 C CE2 . TRP A 1 336 ? 5.914   -28.831 8.406   1.00 20.76 ? 336 TRP A CE2 1 
ATOM   1367 C CE3 . TRP A 1 336 ? 5.643   -31.193 7.968   1.00 22.03 ? 336 TRP A CE3 1 
ATOM   1368 C CZ2 . TRP A 1 336 ? 7.286   -28.987 8.629   1.00 22.00 ? 336 TRP A CZ2 1 
ATOM   1369 C CZ3 . TRP A 1 336 ? 7.006   -31.339 8.148   1.00 23.37 ? 336 TRP A CZ3 1 
ATOM   1370 C CH2 . TRP A 1 336 ? 7.815   -30.237 8.435   1.00 23.18 ? 336 TRP A CH2 1 
ATOM   1371 N N   . PRO A 1 337 ? 0.965   -32.377 5.859   1.00 23.86 ? 337 PRO A N   1 
ATOM   1372 C CA  . PRO A 1 337 ? -0.276  -33.169 5.828   1.00 25.67 ? 337 PRO A CA  1 
ATOM   1373 C C   . PRO A 1 337 ? -0.908  -33.242 7.229   1.00 27.89 ? 337 PRO A C   1 
ATOM   1374 O O   . PRO A 1 337 ? -0.284  -32.864 8.228   1.00 27.82 ? 337 PRO A O   1 
ATOM   1375 C CB  . PRO A 1 337 ? 0.218   -34.549 5.394   1.00 26.11 ? 337 PRO A CB  1 
ATOM   1376 C CG  . PRO A 1 337 ? 1.580   -34.650 6.003   1.00 26.29 ? 337 PRO A CG  1 
ATOM   1377 C CD  . PRO A 1 337 ? 2.161   -33.245 5.827   1.00 23.98 ? 337 PRO A CD  1 
ATOM   1378 N N   . SER A 1 338 ? -2.159  -33.696 7.304   1.00 29.54 ? 338 SER A N   1 
ATOM   1379 C CA  . SER A 1 338 ? -2.855  -33.808 8.600   1.00 32.37 ? 338 SER A CA  1 
ATOM   1380 C C   . SER A 1 338 ? -2.477  -35.070 9.397   1.00 35.27 ? 338 SER A C   1 
ATOM   1381 O O   . SER A 1 338 ? -2.842  -35.189 10.566  1.00 35.66 ? 338 SER A O   1 
ATOM   1382 C CB  . SER A 1 338 ? -4.358  -33.799 8.379   1.00 34.30 ? 338 SER A CB  1 
ATOM   1383 O OG  . SER A 1 338 ? -4.726  -34.929 7.609   1.00 37.40 ? 338 SER A OG  1 
ATOM   1384 N N   . ALA A 1 339 ? -1.800  -36.028 8.755   1.00 36.99 ? 339 ALA A N   1 
ATOM   1385 C CA  . ALA A 1 339 ? -1.374  -37.293 9.361   1.00 39.64 ? 339 ALA A CA  1 
ATOM   1386 C C   . ALA A 1 339 ? -0.127  -37.808 8.616   1.00 41.41 ? 339 ALA A C   1 
ATOM   1387 O O   . ALA A 1 339 ? 0.061   -37.468 7.445   1.00 41.33 ? 339 ALA A O   1 
ATOM   1388 C CB  . ALA A 1 339 ? -2.502  -38.321 9.268   1.00 40.15 ? 339 ALA A CB  1 
ATOM   1389 N N   . PRO A 1 340 ? 0.768   -38.577 9.272   1.00 43.05 ? 340 PRO A N   1 
ATOM   1390 C CA  . PRO A 1 340 ? 1.948   -39.077 8.548   1.00 44.73 ? 340 PRO A CA  1 
ATOM   1391 C C   . PRO A 1 340 ? 1.628   -40.221 7.574   1.00 46.75 ? 340 PRO A C   1 
ATOM   1392 O O   . PRO A 1 340 ? 2.389   -40.446 6.630   1.00 47.38 ? 340 PRO A O   1 
ATOM   1393 C CB  . PRO A 1 340 ? 2.918   -39.498 9.662   1.00 45.20 ? 340 PRO A CB  1 
ATOM   1394 C CG  . PRO A 1 340 ? 2.099   -39.597 10.914  1.00 45.13 ? 340 PRO A CG  1 
ATOM   1395 C CD  . PRO A 1 340 ? 0.702   -39.106 10.650  1.00 43.18 ? 340 PRO A CD  1 
ATOM   1396 N N   . GLY A 1 341 ? 0.500   -40.904 7.790   1.00 47.48 ? 341 GLY A N   1 
ATOM   1397 C CA  . GLY A 1 341 ? 0.058   -42.019 6.966   1.00 48.66 ? 341 GLY A CA  1 
ATOM   1398 C C   . GLY A 1 341 ? 1.044   -43.161 7.015   1.00 49.77 ? 341 GLY A C   1 
ATOM   1399 O O   . GLY A 1 341 ? 1.576   -43.476 8.084   1.00 49.93 ? 341 GLY A O   1 
ATOM   1400 N N   . GLU A 1 342 ? 1.336   -43.757 5.854   1.00 50.12 ? 342 GLU A N   1 
ATOM   1401 C CA  . GLU A 1 342 ? 2.311   -44.850 5.792   1.00 51.03 ? 342 GLU A CA  1 
ATOM   1402 C C   . GLU A 1 342 ? 3.771   -44.357 5.668   1.00 50.86 ? 342 GLU A C   1 
ATOM   1403 O O   . GLU A 1 342 ? 4.701   -45.128 5.898   1.00 51.19 ? 342 GLU A O   1 
ATOM   1404 C CB  . GLU A 1 342 ? 1.960   -45.868 4.690   1.00 54.23 ? 342 GLU A CB  1 
ATOM   1405 C CG  . GLU A 1 342 ? 0.476   -46.194 4.577   1.00 60.66 ? 342 GLU A CG  1 
ATOM   1406 C CD  . GLU A 1 342 ? -0.156  -47.029 5.677   1.00 69.24 ? 342 GLU A CD  1 
ATOM   1407 O OE1 . GLU A 1 342 ? -1.372  -47.310 5.572   1.00 71.87 ? 342 GLU A OE1 1 
ATOM   1408 O OE2 . GLU A 1 342 ? 0.555   -47.412 6.634   1.00 71.17 ? 342 GLU A OE2 1 
ATOM   1409 N N   . GLY A 1 343 ? 3.954   -43.086 5.316   1.00 50.09 ? 343 GLY A N   1 
ATOM   1410 C CA  . GLY A 1 343 ? 5.265   -42.462 5.246   1.00 49.85 ? 343 GLY A CA  1 
ATOM   1411 C C   . GLY A 1 343 ? 5.562   -41.716 6.533   1.00 49.28 ? 343 GLY A C   1 
ATOM   1412 O O   . GLY A 1 343 ? 5.008   -42.042 7.595   1.00 50.08 ? 343 GLY A O   1 
ATOM   1413 N N   . GLY A 1 344 ? 6.405   -40.697 6.444   1.00 47.31 ? 344 GLY A N   1 
ATOM   1414 C CA  . GLY A 1 344 ? 6.756   -39.909 7.620   1.00 45.33 ? 344 GLY A CA  1 
ATOM   1415 C C   . GLY A 1 344 ? 6.218   -38.497 7.595   1.00 42.88 ? 344 GLY A C   1 
ATOM   1416 O O   . GLY A 1 344 ? 5.425   -38.140 6.718   1.00 43.00 ? 344 GLY A O   1 
ATOM   1417 N N   . TRP A 1 345 ? 6.650   -37.684 8.565   1.00 40.25 ? 345 TRP A N   1 
ATOM   1418 C CA  . TRP A 1 345 ? 6.242   -36.281 8.641   1.00 38.28 ? 345 TRP A CA  1 
ATOM   1419 C C   . TRP A 1 345 ? 7.068   -35.451 7.667   1.00 37.05 ? 345 TRP A C   1 
ATOM   1420 O O   . TRP A 1 345 ? 8.117   -34.915 8.029   1.00 37.61 ? 345 TRP A O   1 
ATOM   1421 C CB  . TRP A 1 345 ? 6.377   -35.741 10.074  1.00 37.51 ? 345 TRP A CB  1 
ATOM   1422 C CG  . TRP A 1 345 ? 5.241   -36.131 10.968  1.00 36.93 ? 345 TRP A CG  1 
ATOM   1423 C CD1 . TRP A 1 345 ? 5.284   -36.985 12.032  1.00 37.66 ? 345 TRP A CD1 1 
ATOM   1424 C CD2 . TRP A 1 345 ? 3.881   -35.685 10.865  1.00 36.40 ? 345 TRP A CD2 1 
ATOM   1425 N NE1 . TRP A 1 345 ? 4.032   -37.098 12.598  1.00 37.77 ? 345 TRP A NE1 1 
ATOM   1426 C CE2 . TRP A 1 345 ? 3.157   -36.295 11.910  1.00 37.09 ? 345 TRP A CE2 1 
ATOM   1427 C CE3 . TRP A 1 345 ? 3.205   -34.828 9.989   1.00 36.46 ? 345 TRP A CE3 1 
ATOM   1428 C CZ2 . TRP A 1 345 ? 1.795   -36.080 12.094  1.00 37.13 ? 345 TRP A CZ2 1 
ATOM   1429 C CZ3 . TRP A 1 345 ? 1.853   -34.627 10.171  1.00 36.91 ? 345 TRP A CZ3 1 
ATOM   1430 C CH2 . TRP A 1 345 ? 1.164   -35.245 11.214  1.00 36.94 ? 345 TRP A CH2 1 
ATOM   1431 N N   . VAL A 1 346 ? 6.621   -35.388 6.417   1.00 35.11 ? 346 VAL A N   1 
ATOM   1432 C CA  . VAL A 1 346 ? 7.311   -34.619 5.393   1.00 34.24 ? 346 VAL A CA  1 
ATOM   1433 C C   . VAL A 1 346 ? 6.336   -33.602 4.787   1.00 31.52 ? 346 VAL A C   1 
ATOM   1434 O O   . VAL A 1 346 ? 5.148   -33.896 4.603   1.00 31.07 ? 346 VAL A O   1 
ATOM   1435 C CB  . VAL A 1 346 ? 7.964   -35.514 4.303   1.00 36.81 ? 346 VAL A CB  1 
ATOM   1436 C CG1 . VAL A 1 346 ? 9.184   -36.256 4.849   1.00 38.25 ? 346 VAL A CG1 1 
ATOM   1437 C CG2 . VAL A 1 346 ? 6.955   -36.490 3.709   1.00 37.84 ? 346 VAL A CG2 1 
ATOM   1438 N N   . PRO A 1 347 ? 6.813   -32.384 4.499   1.00 29.41 ? 347 PRO A N   1 
ATOM   1439 C CA  . PRO A 1 347 ? 5.913   -31.386 3.912   1.00 28.05 ? 347 PRO A CA  1 
ATOM   1440 C C   . PRO A 1 347 ? 5.387   -31.795 2.548   1.00 27.01 ? 347 PRO A C   1 
ATOM   1441 O O   . PRO A 1 347 ? 6.133   -32.327 1.723   1.00 26.42 ? 347 PRO A O   1 
ATOM   1442 C CB  . PRO A 1 347 ? 6.782   -30.122 3.802   1.00 28.81 ? 347 PRO A CB  1 
ATOM   1443 C CG  . PRO A 1 347 ? 7.967   -30.370 4.710   1.00 29.62 ? 347 PRO A CG  1 
ATOM   1444 C CD  . PRO A 1 347 ? 8.178   -31.855 4.687   1.00 28.34 ? 347 PRO A CD  1 
ATOM   1445 N N   . LEU A 1 348 ? 4.104   -31.505 2.305   1.00 25.92 ? 348 LEU A N   1 
ATOM   1446 C CA  . LEU A 1 348 ? 3.443   -31.659 1.008   1.00 26.09 ? 348 LEU A CA  1 
ATOM   1447 C C   . LEU A 1 348 ? 3.949   -30.555 0.048   1.00 25.48 ? 348 LEU A C   1 
ATOM   1448 O O   . LEU A 1 348 ? 3.985   -30.753 -1.171  1.00 25.44 ? 348 LEU A O   1 
ATOM   1449 C CB  . LEU A 1 348 ? 1.927   -31.494 1.186   1.00 26.62 ? 348 LEU A CB  1 
ATOM   1450 C CG  . LEU A 1 348 ? 1.221   -32.626 1.899   1.00 28.56 ? 348 LEU A CG  1 
ATOM   1451 C CD1 . LEU A 1 348 ? -0.232  -32.262 2.181   1.00 28.69 ? 348 LEU A CD1 1 
ATOM   1452 C CD2 . LEU A 1 348 ? 1.302   -33.913 1.083   1.00 30.45 ? 348 LEU A CD2 1 
ATOM   1453 N N   . GLN A 1 349 ? 4.252   -29.360 0.592   1.00 24.34 ? 349 GLN A N   1 
ATOM   1454 C CA  . GLN A 1 349 ? 4.786   -28.232 -0.165  1.00 23.26 ? 349 GLN A CA  1 
ATOM   1455 C C   . GLN A 1 349 ? 5.823   -27.474 0.667   1.00 21.79 ? 349 GLN A C   1 
ATOM   1456 O O   . GLN A 1 349 ? 5.688   -27.376 1.884   1.00 21.04 ? 349 GLN A O   1 
ATOM   1457 C CB  . GLN A 1 349 ? 3.676   -27.240 -0.581  1.00 24.41 ? 349 GLN A CB  1 
ATOM   1458 C CG  . GLN A 1 349 ? 2.552   -27.807 -1.459  1.00 26.42 ? 349 GLN A CG  1 
ATOM   1459 C CD  . GLN A 1 349 ? 2.942   -28.037 -2.901  1.00 29.03 ? 349 GLN A CD  1 
ATOM   1460 O OE1 . GLN A 1 349 ? 4.094   -27.848 -3.310  1.00 27.90 ? 349 GLN A OE1 1 
ATOM   1461 N NE2 . GLN A 1 349 ? 1.979   -28.460 -3.698  1.00 29.65 ? 349 GLN A NE2 1 
ATOM   1462 N N   . THR A 1 350 ? 6.871   -26.950 0.009   1.00 21.70 ? 350 THR A N   1 
ATOM   1463 C CA  . THR A 1 350 ? 7.855   -26.090 0.659   1.00 21.73 ? 350 THR A CA  1 
ATOM   1464 C C   . THR A 1 350 ? 8.066   -24.916 -0.277  1.00 21.70 ? 350 THR A C   1 
ATOM   1465 O O   . THR A 1 350 ? 8.627   -25.075 -1.373  1.00 22.37 ? 350 THR A O   1 
ATOM   1466 C CB  . THR A 1 350 ? 9.157   -26.792 1.001   1.00 23.90 ? 350 THR A CB  1 
ATOM   1467 O OG1 . THR A 1 350 ? 8.891   -27.775 1.993   1.00 24.48 ? 350 THR A OG1 1 
ATOM   1468 C CG2 . THR A 1 350 ? 10.181  -25.834 1.566   1.00 24.59 ? 350 THR A CG2 1 
ATOM   1469 N N   . PHE A 1 351 ? 7.526   -23.761 0.112   1.00 20.15 ? 351 PHE A N   1 
ATOM   1470 C CA  . PHE A 1 351 ? 7.597   -22.545 -0.674  1.00 19.75 ? 351 PHE A CA  1 
ATOM   1471 C C   . PHE A 1 351 ? 8.785   -21.721 -0.214  1.00 19.83 ? 351 PHE A C   1 
ATOM   1472 O O   . PHE A 1 351 ? 8.814   -21.273 0.939   1.00 19.87 ? 351 PHE A O   1 
ATOM   1473 C CB  . PHE A 1 351 ? 6.303   -21.738 -0.547  1.00 19.37 ? 351 PHE A CB  1 
ATOM   1474 C CG  . PHE A 1 351 ? 5.023   -22.458 -0.942  1.00 19.76 ? 351 PHE A CG  1 
ATOM   1475 C CD1 . PHE A 1 351 ? 4.929   -23.133 -2.147  1.00 20.09 ? 351 PHE A CD1 1 
ATOM   1476 C CD2 . PHE A 1 351 ? 3.901   -22.419 -0.121  1.00 19.75 ? 351 PHE A CD2 1 
ATOM   1477 C CE1 . PHE A 1 351 ? 3.735   -23.750 -2.532  1.00 20.58 ? 351 PHE A CE1 1 
ATOM   1478 C CE2 . PHE A 1 351 ? 2.707   -23.039 -0.502  1.00 20.41 ? 351 PHE A CE2 1 
ATOM   1479 C CZ  . PHE A 1 351 ? 2.630   -23.703 -1.698  1.00 19.83 ? 351 PHE A CZ  1 
ATOM   1480 N N   . THR A 1 352 ? 9.735   -21.484 -1.121  1.00 19.83 ? 352 THR A N   1 
ATOM   1481 C CA  . THR A 1 352 ? 10.940  -20.718 -0.799  1.00 21.09 ? 352 THR A CA  1 
ATOM   1482 C C   . THR A 1 352 ? 10.935  -19.288 -1.373  1.00 20.93 ? 352 THR A C   1 
ATOM   1483 O O   . THR A 1 352 ? 11.961  -18.617 -1.294  1.00 21.81 ? 352 THR A O   1 
ATOM   1484 C CB  . THR A 1 352 ? 12.161  -21.443 -1.362  1.00 24.84 ? 352 THR A CB  1 
ATOM   1485 O OG1 . THR A 1 352 ? 12.009  -21.536 -2.792  1.00 26.47 ? 352 THR A OG1 1 
ATOM   1486 C CG2 . THR A 1 352 ? 12.341  -22.828 -0.768  1.00 26.67 ? 352 THR A CG2 1 
ATOM   1487 N N   . GLN A 1 353 ? 9.824   -18.845 -1.990  1.00 19.63 ? 353 GLN A N   1 
ATOM   1488 C CA  . GLN A 1 353 ? 9.787   -17.584 -2.729  1.00 19.83 ? 353 GLN A CA  1 
ATOM   1489 C C   . GLN A 1 353 ? 9.823   -16.335 -1.870  1.00 19.17 ? 353 GLN A C   1 
ATOM   1490 O O   . GLN A 1 353 ? 10.225  -15.291 -2.390  1.00 20.90 ? 353 GLN A O   1 
ATOM   1491 C CB  . GLN A 1 353 ? 8.591   -17.550 -3.700  1.00 20.96 ? 353 GLN A CB  1 
ATOM   1492 C CG  . GLN A 1 353 ? 8.640   -18.667 -4.768  1.00 21.82 ? 353 GLN A CG  1 
ATOM   1493 C CD  . GLN A 1 353 ? 7.971   -19.969 -4.362  1.00 23.66 ? 353 GLN A CD  1 
ATOM   1494 O OE1 . GLN A 1 353 ? 7.835   -20.312 -3.176  1.00 22.03 ? 353 GLN A OE1 1 
ATOM   1495 N NE2 . GLN A 1 353 ? 7.563   -20.751 -5.334  1.00 24.44 ? 353 GLN A NE2 1 
ATOM   1496 N N   . HIS A 1 354 ? 9.405   -16.408 -0.577  1.00 18.76 ? 354 HIS A N   1 
ATOM   1497 C CA  . HIS A 1 354 ? 9.528   -15.222 0.266   1.00 19.22 ? 354 HIS A CA  1 
ATOM   1498 C C   . HIS A 1 354 ? 11.009  -15.010 0.624   1.00 21.79 ? 354 HIS A C   1 
ATOM   1499 O O   . HIS A 1 354 ? 11.725  -15.956 0.943   1.00 23.78 ? 354 HIS A O   1 
ATOM   1500 C CB  . HIS A 1 354 ? 8.695   -15.321 1.552   1.00 17.54 ? 354 HIS A CB  1 
ATOM   1501 C CG  . HIS A 1 354 ? 7.208   -15.194 1.357   1.00 17.50 ? 354 HIS A CG  1 
ATOM   1502 N ND1 . HIS A 1 354 ? 6.603   -13.951 1.179   1.00 18.55 ? 354 HIS A ND1 1 
ATOM   1503 C CD2 . HIS A 1 354 ? 6.244   -16.134 1.454   1.00 17.24 ? 354 HIS A CD2 1 
ATOM   1504 C CE1 . HIS A 1 354 ? 5.295   -14.191 1.155   1.00 18.58 ? 354 HIS A CE1 1 
ATOM   1505 N NE2 . HIS A 1 354 ? 5.034   -15.486 1.300   1.00 18.21 ? 354 HIS A NE2 1 
ATOM   1506 N N   . GLN A 1 355 ? 11.470  -13.779 0.538   1.00 21.83 ? 355 GLN A N   1 
ATOM   1507 C CA  . GLN A 1 355 ? 12.866  -13.450 0.846   1.00 23.86 ? 355 GLN A CA  1 
ATOM   1508 C C   . GLN A 1 355 ? 12.925  -12.754 2.198   1.00 23.60 ? 355 GLN A C   1 
ATOM   1509 O O   . GLN A 1 355 ? 13.571  -11.726 2.370   1.00 24.35 ? 355 GLN A O   1 
ATOM   1510 C CB  . GLN A 1 355 ? 13.455  -12.572 -0.265  1.00 27.18 ? 355 GLN A CB  1 
ATOM   1511 C CG  . GLN A 1 355 ? 13.194  -13.105 -1.679  1.00 34.20 ? 355 GLN A CG  1 
ATOM   1512 C CD  . GLN A 1 355 ? 14.069  -14.292 -2.016  1.00 41.38 ? 355 GLN A CD  1 
ATOM   1513 O OE1 . GLN A 1 355 ? 15.291  -14.166 -2.212  1.00 44.86 ? 355 GLN A OE1 1 
ATOM   1514 N NE2 . GLN A 1 355 ? 13.464  -15.472 -2.102  1.00 41.60 ? 355 GLN A NE2 1 
ATOM   1515 N N   . GLY A 1 356 ? 12.237  -13.322 3.154   1.00 23.72 ? 356 GLY A N   1 
ATOM   1516 C CA  . GLY A 1 356 ? 12.198  -12.807 4.515   1.00 22.88 ? 356 GLY A CA  1 
ATOM   1517 C C   . GLY A 1 356 ? 11.381  -13.710 5.415   1.00 22.00 ? 356 GLY A C   1 
ATOM   1518 O O   . GLY A 1 356 ? 10.754  -14.670 4.951   1.00 21.02 ? 356 GLY A O   1 
ATOM   1519 N N   . ALA A 1 357 ? 11.372  -13.405 6.713   1.00 20.66 ? 357 ALA A N   1 
ATOM   1520 C CA  . ALA A 1 357 ? 10.616  -14.202 7.683   1.00 20.14 ? 357 ALA A CA  1 
ATOM   1521 C C   . ALA A 1 357 ? 9.126   -14.248 7.341   1.00 19.74 ? 357 ALA A C   1 
ATOM   1522 O O   . ALA A 1 357 ? 8.572   -13.252 6.888   1.00 20.34 ? 357 ALA A O   1 
ATOM   1523 C CB  . ALA A 1 357 ? 10.788  -13.625 9.090   1.00 20.73 ? 357 ALA A CB  1 
ATOM   1524 N N   . VAL A 1 358 ? 8.500   -15.403 7.521   1.00 18.31 ? 358 VAL A N   1 
ATOM   1525 C CA  . VAL A 1 358 ? 7.087   -15.548 7.215   1.00 17.88 ? 358 VAL A CA  1 
ATOM   1526 C C   . VAL A 1 358 ? 6.283   -15.710 8.506   1.00 19.18 ? 358 VAL A C   1 
ATOM   1527 O O   . VAL A 1 358 ? 6.126   -16.828 9.002   1.00 20.60 ? 358 VAL A O   1 
ATOM   1528 C CB  . VAL A 1 358 ? 6.795   -16.660 6.185   1.00 19.08 ? 358 VAL A CB  1 
ATOM   1529 C CG1 . VAL A 1 358 ? 5.321   -16.626 5.786   1.00 19.31 ? 358 VAL A CG1 1 
ATOM   1530 C CG2 . VAL A 1 358 ? 7.683   -16.489 4.947   1.00 20.64 ? 358 VAL A CG2 1 
ATOM   1531 N N   . LYS A 1 359 ? 5.799   -14.594 9.064   1.00 17.63 ? 359 LYS A N   1 
ATOM   1532 C CA  . LYS A 1 359 ? 4.938   -14.658 10.251  1.00 17.66 ? 359 LYS A CA  1 
ATOM   1533 C C   . LYS A 1 359 ? 3.459   -14.732 9.841   1.00 16.95 ? 359 LYS A C   1 
ATOM   1534 O O   . LYS A 1 359 ? 2.636   -15.319 10.548  1.00 17.90 ? 359 LYS A O   1 
ATOM   1535 C CB  . LYS A 1 359 ? 5.111   -13.382 11.099  1.00 18.85 ? 359 LYS A CB  1 
ATOM   1536 C CG  . LYS A 1 359 ? 4.379   -13.470 12.432  1.00 20.53 ? 359 LYS A CG  1 
ATOM   1537 C CD  . LYS A 1 359 ? 4.535   -12.184 13.211  1.00 21.79 ? 359 LYS A CD  1 
ATOM   1538 C CE  . LYS A 1 359 ? 3.680   -12.263 14.443  1.00 22.07 ? 359 LYS A CE  1 
ATOM   1539 N NZ  . LYS A 1 359 ? 4.012   -11.194 15.391  1.00 20.64 ? 359 LYS A NZ  1 
ATOM   1540 N N   . ALA A 1 360 ? 3.102   -14.096 8.719   1.00 16.38 ? 360 ALA A N   1 
ATOM   1541 C CA  . ALA A 1 360 ? 1.709   -14.025 8.291   1.00 17.16 ? 360 ALA A CA  1 
ATOM   1542 C C   . ALA A 1 360 ? 1.324   -15.269 7.538   1.00 16.45 ? 360 ALA A C   1 
ATOM   1543 O O   . ALA A 1 360 ? 1.911   -15.590 6.509   1.00 16.88 ? 360 ALA A O   1 
ATOM   1544 C CB  . ALA A 1 360 ? 1.480   -12.781 7.437   1.00 17.97 ? 360 ALA A CB  1 
ATOM   1545 N N   . VAL A 1 361 ? 0.339   -16.004 8.071   1.00 16.08 ? 361 VAL A N   1 
ATOM   1546 C CA  . VAL A 1 361 ? -0.097  -17.281 7.493   1.00 16.13 ? 361 VAL A CA  1 
ATOM   1547 C C   . VAL A 1 361 ? -1.605  -17.345 7.772   1.00 15.55 ? 361 VAL A C   1 
ATOM   1548 O O   . VAL A 1 361 ? -1.993  -17.301 8.940   1.00 14.74 ? 361 VAL A O   1 
ATOM   1549 C CB  . VAL A 1 361 ? 0.598   -18.478 8.190   1.00 18.21 ? 361 VAL A CB  1 
ATOM   1550 C CG1 . VAL A 1 361 ? 0.082   -19.804 7.629   1.00 19.44 ? 361 VAL A CG1 1 
ATOM   1551 C CG2 . VAL A 1 361 ? 2.129   -18.417 8.103   1.00 18.81 ? 361 VAL A CG2 1 
ATOM   1552 N N   . ALA A 1 362 ? -2.443  -17.433 6.736   1.00 14.74 ? 362 ALA A N   1 
ATOM   1553 C CA  . ALA A 1 362 ? -3.906  -17.487 6.957   1.00 14.55 ? 362 ALA A CA  1 
ATOM   1554 C C   . ALA A 1 362 ? -4.591  -18.196 5.817   1.00 14.93 ? 362 ALA A C   1 
ATOM   1555 O O   . ALA A 1 362 ? -4.302  -17.877 4.665   1.00 15.26 ? 362 ALA A O   1 
ATOM   1556 C CB  . ALA A 1 362 ? -4.464  -16.069 7.063   1.00 15.29 ? 362 ALA A CB  1 
ATOM   1557 N N   . TRP A 1 363 ? -5.490  -19.141 6.127   1.00 14.56 ? 363 TRP A N   1 
ATOM   1558 C CA  . TRP A 1 363 ? -6.206  -19.919 5.108   1.00 15.25 ? 363 TRP A CA  1 
ATOM   1559 C C   . TRP A 1 363 ? -7.471  -19.226 4.676   1.00 16.45 ? 363 TRP A C   1 
ATOM   1560 O O   . TRP A 1 363 ? -8.178  -18.626 5.509   1.00 17.26 ? 363 TRP A O   1 
ATOM   1561 C CB  . TRP A 1 363 ? -6.575  -21.307 5.653   1.00 15.62 ? 363 TRP A CB  1 
ATOM   1562 C CG  . TRP A 1 363 ? -5.388  -22.176 5.964   1.00 15.91 ? 363 TRP A CG  1 
ATOM   1563 C CD1 . TRP A 1 363 ? -4.722  -22.259 7.150   1.00 16.88 ? 363 TRP A CD1 1 
ATOM   1564 C CD2 . TRP A 1 363 ? -4.714  -23.063 5.055   1.00 15.54 ? 363 TRP A CD2 1 
ATOM   1565 N NE1 . TRP A 1 363 ? -3.679  -23.150 7.044   1.00 17.64 ? 363 TRP A NE1 1 
ATOM   1566 C CE2 . TRP A 1 363 ? -3.648  -23.655 5.760   1.00 16.48 ? 363 TRP A CE2 1 
ATOM   1567 C CE3 . TRP A 1 363 ? -4.940  -23.445 3.721   1.00 16.40 ? 363 TRP A CE3 1 
ATOM   1568 C CZ2 . TRP A 1 363 ? -2.817  -24.623 5.183   1.00 16.93 ? 363 TRP A CZ2 1 
ATOM   1569 C CZ3 . TRP A 1 363 ? -4.091  -24.368 3.131   1.00 16.82 ? 363 TRP A CZ3 1 
ATOM   1570 C CH2 . TRP A 1 363 ? -3.047  -24.951 3.859   1.00 17.30 ? 363 TRP A CH2 1 
ATOM   1571 N N   . CYS A 1 364 ? -7.819  -19.390 3.387   1.00 16.59 ? 364 CYS A N   1 
ATOM   1572 C CA  . CYS A 1 364 ? -9.049  -18.808 2.881   1.00 17.06 ? 364 CYS A CA  1 
ATOM   1573 C C   . CYS A 1 364 ? -10.224 -19.625 3.463   1.00 17.58 ? 364 CYS A C   1 
ATOM   1574 O O   . CYS A 1 364 ? -10.302 -20.852 3.299   1.00 17.81 ? 364 CYS A O   1 
ATOM   1575 C CB  . CYS A 1 364 ? -9.063  -18.827 1.360   1.00 17.37 ? 364 CYS A CB  1 
ATOM   1576 S SG  . CYS A 1 364 ? -10.636 -18.292 0.639   1.00 21.65 ? 364 CYS A SG  1 
ATOM   1577 N N   . PRO A 1 365 ? -11.146 -18.960 4.152   1.00 19.13 ? 365 PRO A N   1 
ATOM   1578 C CA  . PRO A 1 365 ? -12.263 -19.696 4.786   1.00 20.54 ? 365 PRO A CA  1 
ATOM   1579 C C   . PRO A 1 365 ? -13.251 -20.355 3.830   1.00 23.37 ? 365 PRO A C   1 
ATOM   1580 O O   . PRO A 1 365 ? -14.006 -21.240 4.246   1.00 24.25 ? 365 PRO A O   1 
ATOM   1581 C CB  . PRO A 1 365 ? -12.988 -18.615 5.594   1.00 20.89 ? 365 PRO A CB  1 
ATOM   1582 C CG  . PRO A 1 365 ? -12.032 -17.472 5.697   1.00 20.66 ? 365 PRO A CG  1 
ATOM   1583 C CD  . PRO A 1 365 ? -11.198 -17.521 4.459   1.00 18.70 ? 365 PRO A CD  1 
ATOM   1584 N N   . TRP A 1 366 ? -13.284 -19.908 2.565   1.00 23.79 ? 366 TRP A N   1 
ATOM   1585 C CA  . TRP A 1 366 ? -14.237 -20.469 1.610   1.00 25.43 ? 366 TRP A CA  1 
ATOM   1586 C C   . TRP A 1 366 ? -13.597 -21.281 0.468   1.00 26.71 ? 366 TRP A C   1 
ATOM   1587 O O   . TRP A 1 366 ? -14.295 -21.651 -0.496  1.00 27.51 ? 366 TRP A O   1 
ATOM   1588 C CB  . TRP A 1 366 ? -15.153 -19.370 1.062   1.00 26.08 ? 366 TRP A CB  1 
ATOM   1589 C CG  . TRP A 1 366 ? -14.447 -18.385 0.189   1.00 27.05 ? 366 TRP A CG  1 
ATOM   1590 C CD1 . TRP A 1 366 ? -14.316 -18.431 -1.171  1.00 28.42 ? 366 TRP A CD1 1 
ATOM   1591 C CD2 . TRP A 1 366 ? -13.824 -17.176 0.612   1.00 26.65 ? 366 TRP A CD2 1 
ATOM   1592 N NE1 . TRP A 1 366 ? -13.591 -17.350 -1.609  1.00 28.59 ? 366 TRP A NE1 1 
ATOM   1593 C CE2 . TRP A 1 366 ? -13.318 -16.538 -0.538  1.00 27.42 ? 366 TRP A CE2 1 
ATOM   1594 C CE3 . TRP A 1 366 ? -13.694 -16.535 1.850   1.00 26.43 ? 366 TRP A CE3 1 
ATOM   1595 C CZ2 . TRP A 1 366 ? -12.641 -15.331 -0.474  1.00 27.58 ? 366 TRP A CZ2 1 
ATOM   1596 C CZ3 . TRP A 1 366 ? -13.047 -15.324 1.905   1.00 27.03 ? 366 TRP A CZ3 1 
ATOM   1597 C CH2 . TRP A 1 366 ? -12.511 -14.744 0.757   1.00 27.45 ? 366 TRP A CH2 1 
ATOM   1598 N N   . GLN A 1 367 ? -12.290 -21.570 0.561   1.00 26.87 ? 367 GLN A N   1 
ATOM   1599 C CA  . GLN A 1 367 ? -11.588 -22.386 -0.448  1.00 27.69 ? 367 GLN A CA  1 
ATOM   1600 C C   . GLN A 1 367 ? -10.559 -23.218 0.283   1.00 27.92 ? 367 GLN A C   1 
ATOM   1601 O O   . GLN A 1 367 ? -9.539  -22.676 0.697   1.00 27.83 ? 367 GLN A O   1 
ATOM   1602 C CB  . GLN A 1 367 ? -10.851 -21.513 -1.440  1.00 29.91 ? 367 GLN A CB  1 
ATOM   1603 C CG  . GLN A 1 367 ? -11.731 -20.554 -2.155  1.00 34.92 ? 367 GLN A CG  1 
ATOM   1604 C CD  . GLN A 1 367 ? -10.983 -19.957 -3.274  1.00 41.75 ? 367 GLN A CD  1 
ATOM   1605 O OE1 . GLN A 1 367 ? -10.219 -19.000 -3.099  1.00 44.52 ? 367 GLN A OE1 1 
ATOM   1606 N NE2 . GLN A 1 367 ? -11.174 -20.518 -4.448  1.00 42.90 ? 367 GLN A NE2 1 
ATOM   1607 N N   . SER A 1 368 ? -10.786 -24.529 0.371   1.00 27.09 ? 368 SER A N   1 
ATOM   1608 C CA  . SER A 1 368 ? -9.991  -25.463 1.162   1.00 27.68 ? 368 SER A CA  1 
ATOM   1609 C C   . SER A 1 368 ? -8.463  -25.337 1.042   1.00 26.32 ? 368 SER A C   1 
ATOM   1610 O O   . SER A 1 368 ? -7.751  -25.343 2.058   1.00 27.09 ? 368 SER A O   1 
ATOM   1611 C CB  . SER A 1 368 ? -10.414 -26.896 0.827   1.00 31.75 ? 368 SER A CB  1 
ATOM   1612 O OG  . SER A 1 368 ? -9.530  -27.860 1.384   1.00 37.03 ? 368 SER A OG  1 
ATOM   1613 N N   . ASN A 1 369 ? -7.978  -25.267 -0.189  1.00 24.05 ? 369 ASN A N   1 
ATOM   1614 C CA  . ASN A 1 369 ? -6.563  -25.307 -0.510  1.00 23.11 ? 369 ASN A CA  1 
ATOM   1615 C C   . ASN A 1 369 ? -5.898  -23.951 -0.706  1.00 21.05 ? 369 ASN A C   1 
ATOM   1616 O O   . ASN A 1 369 ? -4.761  -23.935 -1.156  1.00 21.77 ? 369 ASN A O   1 
ATOM   1617 C CB  . ASN A 1 369 ? -6.379  -26.133 -1.785  1.00 25.63 ? 369 ASN A CB  1 
ATOM   1618 C CG  . ASN A 1 369 ? -6.866  -27.545 -1.620  1.00 31.31 ? 369 ASN A CG  1 
ATOM   1619 O OD1 . ASN A 1 369 ? -6.681  -28.156 -0.570  1.00 32.87 ? 369 ASN A OD1 1 
ATOM   1620 N ND2 . ASN A 1 369 ? -7.521  -28.086 -2.643  1.00 33.92 ? 369 ASN A ND2 1 
ATOM   1621 N N   . VAL A 1 370 ? -6.591  -22.837 -0.460  1.00 18.28 ? 370 VAL A N   1 
ATOM   1622 C CA  . VAL A 1 370 ? -6.013  -21.509 -0.700  1.00 17.02 ? 370 VAL A CA  1 
ATOM   1623 C C   . VAL A 1 370 ? -5.415  -20.931 0.554   1.00 15.73 ? 370 VAL A C   1 
ATOM   1624 O O   . VAL A 1 370 ? -6.090  -20.823 1.584   1.00 15.38 ? 370 VAL A O   1 
ATOM   1625 C CB  . VAL A 1 370 ? -7.028  -20.558 -1.357  1.00 17.33 ? 370 VAL A CB  1 
ATOM   1626 C CG1 . VAL A 1 370 ? -6.462  -19.145 -1.492  1.00 16.99 ? 370 VAL A CG1 1 
ATOM   1627 C CG2 . VAL A 1 370 ? -7.452  -21.099 -2.728  1.00 18.38 ? 370 VAL A CG2 1 
ATOM   1628 N N   . LEU A 1 371 ? -4.143  -20.549 0.473   1.00 15.94 ? 371 LEU A N   1 
ATOM   1629 C CA  . LEU A 1 371 ? -3.409  -20.011 1.612   1.00 15.50 ? 371 LEU A CA  1 
ATOM   1630 C C   . LEU A 1 371 ? -2.829  -18.635 1.304   1.00 15.58 ? 371 LEU A C   1 
ATOM   1631 O O   . LEU A 1 371 ? -2.322  -18.444 0.204   1.00 15.66 ? 371 LEU A O   1 
ATOM   1632 C CB  . LEU A 1 371 ? -2.263  -20.992 1.873   1.00 16.04 ? 371 LEU A CB  1 
ATOM   1633 C CG  . LEU A 1 371 ? -1.249  -20.591 2.960   1.00 17.08 ? 371 LEU A CG  1 
ATOM   1634 C CD1 . LEU A 1 371 ? -1.898  -20.565 4.358   1.00 17.68 ? 371 LEU A CD1 1 
ATOM   1635 C CD2 . LEU A 1 371 ? -0.040  -21.532 2.988   1.00 17.95 ? 371 LEU A CD2 1 
ATOM   1636 N N   . ALA A 1 372 ? -2.842  -17.693 2.258   1.00 14.78 ? 372 ALA A N   1 
ATOM   1637 C CA  . ALA A 1 372 ? -2.161  -16.407 2.095   1.00 15.22 ? 372 ALA A CA  1 
ATOM   1638 C C   . ALA A 1 372 ? -0.982  -16.395 3.062   1.00 15.15 ? 372 ALA A C   1 
ATOM   1639 O O   . ALA A 1 372 ? -1.110  -16.854 4.209   1.00 15.29 ? 372 ALA A O   1 
ATOM   1640 C CB  . ALA A 1 372 ? -3.077  -15.252 2.450   1.00 15.90 ? 372 ALA A CB  1 
ATOM   1641 N N   . THR A 1 373 ? 0.163   -15.903 2.599   1.00 14.33 ? 373 THR A N   1 
ATOM   1642 C CA  . THR A 1 373 ? 1.345   -15.740 3.448   1.00 15.25 ? 373 THR A CA  1 
ATOM   1643 C C   . THR A 1 373 ? 1.935   -14.341 3.234   1.00 16.42 ? 373 THR A C   1 
ATOM   1644 O O   . THR A 1 373 ? 1.716   -13.729 2.190   1.00 16.99 ? 373 THR A O   1 
ATOM   1645 C CB  . THR A 1 373 ? 2.392   -16.838 3.225   1.00 17.52 ? 373 THR A CB  1 
ATOM   1646 O OG1 . THR A 1 373 ? 2.882   -16.743 1.883   1.00 19.07 ? 373 THR A OG1 1 
ATOM   1647 C CG2 . THR A 1 373 ? 1.861   -18.243 3.537   1.00 17.36 ? 373 THR A CG2 1 
ATOM   1648 N N   . GLY A 1 374 ? 2.694   -13.849 4.219   1.00 15.90 ? 374 GLY A N   1 
ATOM   1649 C CA  . GLY A 1 374 ? 3.290   -12.528 4.113   1.00 16.53 ? 374 GLY A CA  1 
ATOM   1650 C C   . GLY A 1 374 ? 4.679   -12.511 4.694   1.00 18.22 ? 374 GLY A C   1 
ATOM   1651 O O   . GLY A 1 374 ? 4.911   -13.093 5.750   1.00 19.53 ? 374 GLY A O   1 
ATOM   1652 N N   . GLY A 1 375 ? 5.608   -11.869 3.995   1.00 17.89 ? 375 GLY A N   1 
ATOM   1653 C CA  . GLY A 1 375 ? 6.989   -11.830 4.445   1.00 18.91 ? 375 GLY A CA  1 
ATOM   1654 C C   . GLY A 1 375 ? 7.371   -10.567 5.186   1.00 20.18 ? 375 GLY A C   1 
ATOM   1655 O O   . GLY A 1 375 ? 6.670   -9.549  5.119   1.00 20.32 ? 375 GLY A O   1 
ATOM   1656 N N   . GLY A 1 376 ? 8.529   -10.628 5.831   1.00 20.34 ? 376 GLY A N   1 
ATOM   1657 C CA  . GLY A 1 376 ? 9.046   -9.529  6.619   1.00 21.60 ? 376 GLY A CA  1 
ATOM   1658 C C   . GLY A 1 376 ? 9.607   -8.386  5.807   1.00 21.65 ? 376 GLY A C   1 
ATOM   1659 O O   . GLY A 1 376 ? 9.373   -8.281  4.600   1.00 21.60 ? 376 GLY A O   1 
ATOM   1660 N N   . THR A 1 377 ? 10.383  -7.536  6.462   1.00 21.91 ? 377 THR A N   1 
ATOM   1661 C CA  . THR A 1 377 ? 10.936  -6.311  5.890   1.00 22.84 ? 377 THR A CA  1 
ATOM   1662 C C   . THR A 1 377 ? 11.732  -6.511  4.615   1.00 23.34 ? 377 THR A C   1 
ATOM   1663 O O   . THR A 1 377 ? 11.651  -5.676  3.710   1.00 24.19 ? 377 THR A O   1 
ATOM   1664 C CB  . THR A 1 377 ? 11.757  -5.575  6.936   1.00 24.83 ? 377 THR A CB  1 
ATOM   1665 O OG1 . THR A 1 377 ? 10.952  -5.409  8.098   1.00 25.60 ? 377 THR A OG1 1 
ATOM   1666 C CG2 . THR A 1 377 ? 12.255  -4.207  6.445   1.00 25.33 ? 377 THR A CG2 1 
ATOM   1667 N N   . SER A 1 378 ? 12.514  -7.600  4.536   1.00 22.21 ? 378 SER A N   1 
ATOM   1668 C CA  . SER A 1 378 ? 13.329  -7.837  3.335   1.00 22.94 ? 378 SER A CA  1 
ATOM   1669 C C   . SER A 1 378 ? 12.518  -8.401  2.167   1.00 22.19 ? 378 SER A C   1 
ATOM   1670 O O   . SER A 1 378 ? 13.066  -8.516  1.062   1.00 23.49 ? 378 SER A O   1 
ATOM   1671 C CB  . SER A 1 378 ? 14.467  -8.792  3.658   1.00 23.63 ? 378 SER A CB  1 
ATOM   1672 O OG  . SER A 1 378 ? 13.935  -9.990  4.195   1.00 25.02 ? 378 SER A OG  1 
ATOM   1673 N N   . ASP A 1 379 ? 11.252  -8.788  2.415   1.00 21.33 ? 379 ASP A N   1 
ATOM   1674 C CA  . ASP A 1 379 ? 10.366  -9.396  1.433   1.00 21.18 ? 379 ASP A CA  1 
ATOM   1675 C C   . ASP A 1 379 ? 9.205   -8.471  1.039   1.00 21.22 ? 379 ASP A C   1 
ATOM   1676 O O   . ASP A 1 379 ? 9.067   -8.143  -0.141  1.00 21.33 ? 379 ASP A O   1 
ATOM   1677 C CB  . ASP A 1 379 ? 9.858   -10.748 1.936   1.00 22.21 ? 379 ASP A CB  1 
ATOM   1678 C CG  . ASP A 1 379 ? 8.931   -11.386 0.932   1.00 25.17 ? 379 ASP A CG  1 
ATOM   1679 O OD1 . ASP A 1 379 ? 9.436   -11.878 -0.103  1.00 26.74 ? 379 ASP A OD1 1 
ATOM   1680 O OD2 . ASP A 1 379 ? 7.697   -11.344 1.154   1.00 25.04 ? 379 ASP A OD2 1 
ATOM   1681 N N   . ARG A 1 380 ? 8.364   -8.087  2.017   1.00 20.28 ? 380 ARG A N   1 
ATOM   1682 C CA  . ARG A 1 380 ? 7.273   -7.132  1.872   1.00 21.61 ? 380 ARG A CA  1 
ATOM   1683 C C   . ARG A 1 380 ? 6.118   -7.615  1.030   1.00 22.51 ? 380 ARG A C   1 
ATOM   1684 O O   . ARG A 1 380 ? 5.272   -6.786  0.700   1.00 24.07 ? 380 ARG A O   1 
ATOM   1685 C CB  . ARG A 1 380 ? 7.746   -5.771  1.285   1.00 24.07 ? 380 ARG A CB  1 
ATOM   1686 C CG  . ARG A 1 380 ? 9.057   -5.197  1.794   1.00 29.28 ? 380 ARG A CG  1 
ATOM   1687 C CD  . ARG A 1 380 ? 9.518   -3.977  0.971   1.00 35.14 ? 380 ARG A CD  1 
ATOM   1688 N NE  . ARG A 1 380 ? 9.290   -4.118  -0.476  1.00 40.26 ? 380 ARG A NE  1 
ATOM   1689 C CZ  . ARG A 1 380 ? 10.232  -4.436  -1.363  1.00 45.38 ? 380 ARG A CZ  1 
ATOM   1690 N NH1 . ARG A 1 380 ? 9.931   -4.543  -2.653  1.00 46.00 ? 380 ARG A NH1 1 
ATOM   1691 N NH2 . ARG A 1 380 ? 11.480  -4.647  -0.969  1.00 45.37 ? 380 ARG A NH2 1 
ATOM   1692 N N   . HIS A 1 381 ? 6.086   -8.898  0.633   1.00 20.85 ? 381 HIS A N   1 
ATOM   1693 C CA  . HIS A 1 381 ? 5.017   -9.364  -0.230  1.00 20.53 ? 381 HIS A CA  1 
ATOM   1694 C C   . HIS A 1 381 ? 3.988   -10.262 0.464   1.00 19.46 ? 381 HIS A C   1 
ATOM   1695 O O   . HIS A 1 381 ? 4.308   -11.014 1.375   1.00 19.20 ? 381 HIS A O   1 
ATOM   1696 C CB  . HIS A 1 381 ? 5.576   -10.123 -1.450  1.00 20.88 ? 381 HIS A CB  1 
ATOM   1697 C CG  . HIS A 1 381 ? 6.194   -9.261  -2.516  1.00 23.73 ? 381 HIS A CG  1 
ATOM   1698 N ND1 . HIS A 1 381 ? 7.306   -8.487  -2.267  1.00 24.90 ? 381 HIS A ND1 1 
ATOM   1699 C CD2 . HIS A 1 381 ? 5.843   -9.120  -3.815  1.00 25.35 ? 381 HIS A CD2 1 
ATOM   1700 C CE1 . HIS A 1 381 ? 7.604   -7.890  -3.413  1.00 26.36 ? 381 HIS A CE1 1 
ATOM   1701 N NE2 . HIS A 1 381 ? 6.761   -8.259  -4.386  1.00 26.42 ? 381 HIS A NE2 1 
ATOM   1702 N N   . ILE A 1 382 ? 2.755   -10.167 -0.004  1.00 18.36 ? 382 ILE A N   1 
ATOM   1703 C CA  . ILE A 1 382 ? 1.659   -11.059 0.306   1.00 17.04 ? 382 ILE A CA  1 
ATOM   1704 C C   . ILE A 1 382 ? 1.582   -12.001 -0.900  1.00 17.32 ? 382 ILE A C   1 
ATOM   1705 O O   . ILE A 1 382 ? 1.539   -11.550 -2.052  1.00 18.49 ? 382 ILE A O   1 
ATOM   1706 C CB  . ILE A 1 382 ? 0.320   -10.303 0.457   1.00 18.06 ? 382 ILE A CB  1 
ATOM   1707 C CG1 . ILE A 1 382 ? 0.366   -9.379  1.713   1.00 19.68 ? 382 ILE A CG1 1 
ATOM   1708 C CG2 . ILE A 1 382 ? -0.847  -11.290 0.528   1.00 17.77 ? 382 ILE A CG2 1 
ATOM   1709 C CD1 . ILE A 1 382 ? -0.818  -8.337  1.761   1.00 20.86 ? 382 ILE A CD1 1 
ATOM   1710 N N   . ARG A 1 383 ? 1.611   -13.294 -0.643  1.00 16.68 ? 383 ARG A N   1 
ATOM   1711 C CA  . ARG A 1 383 ? 1.505   -14.285 -1.710  1.00 17.09 ? 383 ARG A CA  1 
ATOM   1712 C C   . ARG A 1 383 ? 0.314   -15.174 -1.433  1.00 17.01 ? 383 ARG A C   1 
ATOM   1713 O O   . ARG A 1 383 ? 0.050   -15.495 -0.280  1.00 17.01 ? 383 ARG A O   1 
ATOM   1714 C CB  . ARG A 1 383 ? 2.787   -15.112 -1.812  1.00 18.14 ? 383 ARG A CB  1 
ATOM   1715 C CG  . ARG A 1 383 ? 3.922   -14.342 -2.483  1.00 17.69 ? 383 ARG A CG  1 
ATOM   1716 C CD  . ARG A 1 383 ? 5.207   -15.116 -2.420  1.00 19.72 ? 383 ARG A CD  1 
ATOM   1717 N NE  . ARG A 1 383 ? 6.288   -14.450 -3.162  1.00 20.82 ? 383 ARG A NE  1 
ATOM   1718 C CZ  . ARG A 1 383 ? 6.576   -14.690 -4.441  1.00 22.98 ? 383 ARG A CZ  1 
ATOM   1719 N NH1 . ARG A 1 383 ? 7.579   -14.059 -5.028  1.00 23.77 ? 383 ARG A NH1 1 
ATOM   1720 N NH2 . ARG A 1 383 ? 5.900   -15.614 -5.122  1.00 23.36 ? 383 ARG A NH2 1 
ATOM   1721 N N   . ILE A 1 384 ? -0.416  -15.539 -2.470  1.00 16.67 ? 384 ILE A N   1 
ATOM   1722 C CA  . ILE A 1 384 ? -1.590  -16.415 -2.326  1.00 16.69 ? 384 ILE A CA  1 
ATOM   1723 C C   . ILE A 1 384 ? -1.241  -17.700 -3.052  1.00 16.54 ? 384 ILE A C   1 
ATOM   1724 O O   . ILE A 1 384 ? -0.694  -17.652 -4.157  1.00 17.06 ? 384 ILE A O   1 
ATOM   1725 C CB  . ILE A 1 384 ? -2.835  -15.765 -2.963  1.00 18.04 ? 384 ILE A CB  1 
ATOM   1726 C CG1 . ILE A 1 384 ? -3.063  -14.337 -2.459  1.00 17.79 ? 384 ILE A CG1 1 
ATOM   1727 C CG2 . ILE A 1 384 ? -4.070  -16.652 -2.798  1.00 19.51 ? 384 ILE A CG2 1 
ATOM   1728 C CD1 . ILE A 1 384 ? -3.312  -14.250 -0.964  1.00 19.39 ? 384 ILE A CD1 1 
ATOM   1729 N N   . TRP A 1 385 ? -1.490  -18.843 -2.434  1.00 16.58 ? 385 TRP A N   1 
ATOM   1730 C CA  . TRP A 1 385 ? -1.117  -20.131 -2.996  1.00 17.03 ? 385 TRP A CA  1 
ATOM   1731 C C   . TRP A 1 385 ? -2.271  -21.083 -3.107  1.00 17.69 ? 385 TRP A C   1 
ATOM   1732 O O   . TRP A 1 385 ? -3.202  -21.028 -2.287  1.00 17.26 ? 385 TRP A O   1 
ATOM   1733 C CB  . TRP A 1 385 ? -0.134  -20.822 -2.046  1.00 17.58 ? 385 TRP A CB  1 
ATOM   1734 C CG  . TRP A 1 385 ? 0.970   -19.960 -1.519  1.00 18.60 ? 385 TRP A CG  1 
ATOM   1735 C CD1 . TRP A 1 385 ? 0.972   -19.238 -0.360  1.00 19.38 ? 385 TRP A CD1 1 
ATOM   1736 C CD2 . TRP A 1 385 ? 2.267   -19.787 -2.107  1.00 18.52 ? 385 TRP A CD2 1 
ATOM   1737 N NE1 . TRP A 1 385 ? 2.201   -18.649 -0.172  1.00 19.98 ? 385 TRP A NE1 1 
ATOM   1738 C CE2 . TRP A 1 385 ? 3.002   -18.934 -1.252  1.00 19.58 ? 385 TRP A CE2 1 
ATOM   1739 C CE3 . TRP A 1 385 ? 2.891   -20.300 -3.257  1.00 19.65 ? 385 TRP A CE3 1 
ATOM   1740 C CZ2 . TRP A 1 385 ? 4.323   -18.586 -1.509  1.00 20.87 ? 385 TRP A CZ2 1 
ATOM   1741 C CZ3 . TRP A 1 385 ? 4.196   -19.928 -3.521  1.00 20.50 ? 385 TRP A CZ3 1 
ATOM   1742 C CH2 . TRP A 1 385 ? 4.893   -19.087 -2.655  1.00 21.13 ? 385 TRP A CH2 1 
ATOM   1743 N N   . ASN A 1 386 ? -2.155  -22.053 -4.032  1.00 17.67 ? 386 ASN A N   1 
ATOM   1744 C CA  . ASN A 1 386 ? -3.051  -23.197 -4.035  1.00 19.01 ? 386 ASN A CA  1 
ATOM   1745 C C   . ASN A 1 386 ? -2.102  -24.306 -3.532  1.00 20.65 ? 386 ASN A C   1 
ATOM   1746 O O   . ASN A 1 386 ? -1.121  -24.624 -4.213  1.00 21.39 ? 386 ASN A O   1 
ATOM   1747 C CB  . ASN A 1 386 ? -3.591  -23.525 -5.425  1.00 21.32 ? 386 ASN A CB  1 
ATOM   1748 C CG  . ASN A 1 386 ? -4.488  -24.728 -5.335  1.00 26.12 ? 386 ASN A CG  1 
ATOM   1749 O OD1 . ASN A 1 386 ? -4.050  -25.807 -4.937  1.00 25.98 ? 386 ASN A OD1 1 
ATOM   1750 N ND2 . ASN A 1 386 ? -5.770  -24.562 -5.639  1.00 28.02 ? 386 ASN A ND2 1 
ATOM   1751 N N   . VAL A 1 387 ? -2.339  -24.847 -2.335  1.00 20.74 ? 387 VAL A N   1 
ATOM   1752 C CA  . VAL A 1 387 ? -1.423  -25.834 -1.743  1.00 21.56 ? 387 VAL A CA  1 
ATOM   1753 C C   . VAL A 1 387 ? -1.488  -27.236 -2.367  1.00 23.21 ? 387 VAL A C   1 
ATOM   1754 O O   . VAL A 1 387 ? -0.620  -28.066 -2.080  1.00 23.69 ? 387 VAL A O   1 
ATOM   1755 C CB  . VAL A 1 387 ? -1.562  -25.921 -0.219  1.00 21.62 ? 387 VAL A CB  1 
ATOM   1756 C CG1 . VAL A 1 387 ? -1.411  -24.547 0.428   1.00 21.56 ? 387 VAL A CG1 1 
ATOM   1757 C CG2 . VAL A 1 387 ? -2.884  -26.567 0.164   1.00 22.87 ? 387 VAL A CG2 1 
ATOM   1758 N N   A CYS A 1 388 ? -2.491  -27.514 -3.220  0.44 23.45 ? 388 CYS A N   1 
ATOM   1759 N N   B CYS A 1 388 ? -2.493  -27.493 -3.181  0.55 23.45 ? 388 CYS A N   1 
ATOM   1760 C CA  A CYS A 1 388 ? -2.607  -28.814 -3.905  0.44 24.23 ? 388 CYS A CA  1 
ATOM   1761 C CA  B CYS A 1 388 ? -2.617  -28.760 -3.865  0.55 24.31 ? 388 CYS A CA  1 
ATOM   1762 C C   A CYS A 1 388 ? -1.848  -28.824 -5.234  0.44 24.02 ? 388 CYS A C   1 
ATOM   1763 C C   B CYS A 1 388 ? -1.720  -28.723 -5.115  0.55 24.22 ? 388 CYS A C   1 
ATOM   1764 O O   A CYS A 1 388 ? -1.241  -29.833 -5.590  0.44 24.32 ? 388 CYS A O   1 
ATOM   1765 O O   B CYS A 1 388 ? -0.824  -29.552 -5.251  0.55 24.85 ? 388 CYS A O   1 
ATOM   1766 C CB  A CYS A 1 388 ? -4.066  -29.218 -4.091  0.44 26.23 ? 388 CYS A CB  1 
ATOM   1767 C CB  B CYS A 1 388 ? -4.078  -29.016 -4.219  0.55 26.29 ? 388 CYS A CB  1 
ATOM   1768 S SG  A CYS A 1 388 ? -4.886  -29.736 -2.563  0.44 32.75 ? 388 CYS A SG  1 
ATOM   1769 S SG  B CYS A 1 388 ? -4.358  -30.545 -5.128  0.55 32.52 ? 388 CYS A SG  1 
ATOM   1770 N N   . SER A 1 389 ? -1.912  -27.726 -5.979  1.00 23.39 ? 389 SER A N   1 
ATOM   1771 C CA  . SER A 1 389 ? -1.151  -27.604 -7.229  1.00 23.28 ? 389 SER A CA  1 
ATOM   1772 C C   . SER A 1 389 ? 0.241   -26.966 -7.019  1.00 23.86 ? 389 SER A C   1 
ATOM   1773 O O   . SER A 1 389 ? 1.104   -27.072 -7.898  1.00 24.44 ? 389 SER A O   1 
ATOM   1774 C CB  . SER A 1 389 ? -1.930  -26.765 -8.230  1.00 24.02 ? 389 SER A CB  1 
ATOM   1775 O OG  . SER A 1 389 ? -2.006  -25.429 -7.763  1.00 25.06 ? 389 SER A OG  1 
ATOM   1776 N N   . GLY A 1 390 ? 0.426   -26.251 -5.908  1.00 22.99 ? 390 GLY A N   1 
ATOM   1777 C CA  . GLY A 1 390 ? 1.655   -25.508 -5.639  1.00 23.48 ? 390 GLY A CA  1 
ATOM   1778 C C   . GLY A 1 390 ? 1.704   -24.153 -6.329  1.00 23.24 ? 390 GLY A C   1 
ATOM   1779 O O   . GLY A 1 390 ? 2.698   -23.440 -6.226  1.00 23.08 ? 390 GLY A O   1 
ATOM   1780 N N   . ALA A 1 391 ? 0.628   -23.774 -7.043  1.00 23.02 ? 391 ALA A N   1 
ATOM   1781 C CA  . ALA A 1 391 ? 0.604   -22.513 -7.772  1.00 22.93 ? 391 ALA A CA  1 
ATOM   1782 C C   . ALA A 1 391 ? 0.651   -21.308 -6.876  1.00 21.24 ? 391 ALA A C   1 
ATOM   1783 O O   . ALA A 1 391 ? -0.001  -21.275 -5.822  1.00 20.37 ? 391 ALA A O   1 
ATOM   1784 C CB  . ALA A 1 391 ? -0.639  -22.445 -8.649  1.00 23.29 ? 391 ALA A CB  1 
ATOM   1785 N N   . CYS A 1 392 ? 1.410   -20.299 -7.295  1.00 19.92 ? 392 CYS A N   1 
ATOM   1786 C CA  . CYS A 1 392 ? 1.390   -19.016 -6.634  1.00 20.09 ? 392 CYS A CA  1 
ATOM   1787 C C   . CYS A 1 392 ? 0.405   -18.230 -7.461  1.00 21.18 ? 392 CYS A C   1 
ATOM   1788 O O   . CYS A 1 392 ? 0.636   -17.966 -8.643  1.00 22.16 ? 392 CYS A O   1 
ATOM   1789 C CB  . CYS A 1 392 ? 2.743   -18.331 -6.605  1.00 21.21 ? 392 CYS A CB  1 
ATOM   1790 S SG  . CYS A 1 392 ? 2.664   -16.676 -5.872  1.00 27.06 ? 392 CYS A SG  1 
ATOM   1791 N N   . LEU A 1 393 ? -0.769  -18.018 -6.900  1.00 20.69 ? 393 LEU A N   1 
ATOM   1792 C CA  . LEU A 1 393 ? -1.864  -17.353 -7.593  1.00 20.85 ? 393 LEU A CA  1 
ATOM   1793 C C   . LEU A 1 393 ? -1.679  -15.834 -7.670  1.00 21.15 ? 393 LEU A C   1 
ATOM   1794 O O   . LEU A 1 393 ? -2.208  -15.208 -8.583  1.00 21.47 ? 393 LEU A O   1 
ATOM   1795 C CB  . LEU A 1 393 ? -3.163  -17.670 -6.835  1.00 21.57 ? 393 LEU A CB  1 
ATOM   1796 C CG  . LEU A 1 393 ? -3.470  -19.148 -6.616  1.00 23.25 ? 393 LEU A CG  1 
ATOM   1797 C CD1 . LEU A 1 393 ? -4.721  -19.317 -5.764  1.00 24.45 ? 393 LEU A CD1 1 
ATOM   1798 C CD2 . LEU A 1 393 ? -3.648  -19.864 -7.936  1.00 23.53 ? 393 LEU A CD2 1 
ATOM   1799 N N   . SER A 1 394 ? -0.954  -15.243 -6.714  1.00 20.56 ? 394 SER A N   1 
ATOM   1800 C CA  . SER A 1 394 ? -0.770  -13.794 -6.681  1.00 21.05 ? 394 SER A CA  1 
ATOM   1801 C C   . SER A 1 394 ? 0.433   -13.439 -5.786  1.00 21.23 ? 394 SER A C   1 
ATOM   1802 O O   . SER A 1 394 ? 0.692   -14.129 -4.815  1.00 21.17 ? 394 SER A O   1 
ATOM   1803 C CB  . SER A 1 394 ? -2.033  -13.139 -6.104  1.00 23.49 ? 394 SER A CB  1 
ATOM   1804 O OG  . SER A 1 394 ? -1.903  -11.732 -6.009  1.00 27.72 ? 394 SER A OG  1 
ATOM   1805 N N   . ALA A 1 395 ? 1.177   -12.387 -6.121  1.00 21.12 ? 395 ALA A N   1 
ATOM   1806 C CA  . ALA A 1 395 ? 2.280   -11.905 -5.285  1.00 21.77 ? 395 ALA A CA  1 
ATOM   1807 C C   . ALA A 1 395 ? 2.143   -10.393 -5.342  1.00 22.75 ? 395 ALA A C   1 
ATOM   1808 O O   . ALA A 1 395 ? 2.160   -9.842  -6.439  1.00 23.82 ? 395 ALA A O   1 
ATOM   1809 C CB  . ALA A 1 395 ? 3.630   -12.339 -5.861  1.00 22.04 ? 395 ALA A CB  1 
ATOM   1810 N N   . VAL A 1 396 ? 1.844   -9.730  -4.211  1.00 22.44 ? 396 VAL A N   1 
ATOM   1811 C CA  . VAL A 1 396 ? 1.635   -8.289  -4.218  1.00 23.39 ? 396 VAL A CA  1 
ATOM   1812 C C   . VAL A 1 396 ? 2.621   -7.634  -3.253  1.00 23.31 ? 396 VAL A C   1 
ATOM   1813 O O   . VAL A 1 396 ? 2.771   -8.109  -2.139  1.00 22.85 ? 396 VAL A O   1 
ATOM   1814 C CB  . VAL A 1 396 ? 0.172   -7.931  -3.851  1.00 25.66 ? 396 VAL A CB  1 
ATOM   1815 C CG1 . VAL A 1 396 ? -0.003  -6.417  -3.758  1.00 27.24 ? 396 VAL A CG1 1 
ATOM   1816 C CG2 . VAL A 1 396 ? -0.816  -8.526  -4.856  1.00 26.54 ? 396 VAL A CG2 1 
ATOM   1817 N N   . ASP A 1 397 ? 3.247   -6.529  -3.661  1.00 23.67 ? 397 ASP A N   1 
ATOM   1818 C CA  . ASP A 1 397 ? 4.177   -5.822  -2.795  1.00 24.38 ? 397 ASP A CA  1 
ATOM   1819 C C   . ASP A 1 397 ? 3.376   -4.907  -1.876  1.00 25.07 ? 397 ASP A C   1 
ATOM   1820 O O   . ASP A 1 397 ? 2.684   -4.003  -2.348  1.00 26.95 ? 397 ASP A O   1 
ATOM   1821 C CB  . ASP A 1 397 ? 5.147   -4.981  -3.660  1.00 25.50 ? 397 ASP A CB  1 
ATOM   1822 C CG  . ASP A 1 397 ? 6.340   -4.417  -2.919  1.00 29.31 ? 397 ASP A CG  1 
ATOM   1823 O OD1 . ASP A 1 397 ? 6.350   -4.483  -1.666  1.00 29.34 ? 397 ASP A OD1 1 
ATOM   1824 O OD2 . ASP A 1 397 ? 7.273   -3.901  -3.597  1.00 32.79 ? 397 ASP A OD2 1 
ATOM   1825 N N   . ALA A 1 398 ? 3.477   -5.128  -0.581  1.00 23.71 ? 398 ALA A N   1 
ATOM   1826 C CA  . ALA A 1 398 ? 2.791   -4.304  0.416   1.00 24.53 ? 398 ALA A CA  1 
ATOM   1827 C C   . ALA A 1 398 ? 3.627   -3.100  0.881   1.00 25.32 ? 398 ALA A C   1 
ATOM   1828 O O   . ALA A 1 398 ? 3.132   -2.316  1.690   1.00 26.20 ? 398 ALA A O   1 
ATOM   1829 C CB  . ALA A 1 398 ? 2.370   -5.155  1.612   1.00 24.24 ? 398 ALA A CB  1 
ATOM   1830 N N   . HIS A 1 399 ? 4.899   -2.975  0.411   1.00 24.99 ? 399 HIS A N   1 
ATOM   1831 C CA  . HIS A 1 399 ? 5.828   -1.894  0.743   1.00 25.86 ? 399 HIS A CA  1 
ATOM   1832 C C   . HIS A 1 399 ? 6.221   -1.822  2.216   1.00 26.22 ? 399 HIS A C   1 
ATOM   1833 O O   . HIS A 1 399 ? 6.694   -0.789  2.674   1.00 27.32 ? 399 HIS A O   1 
ATOM   1834 C CB  . HIS A 1 399 ? 5.299   -0.538  0.260   1.00 27.40 ? 399 HIS A CB  1 
ATOM   1835 C CG  . HIS A 1 399 ? 4.944   -0.544  -1.194  1.00 31.80 ? 399 HIS A CG  1 
ATOM   1836 N ND1 . HIS A 1 399 ? 5.918   -0.529  -2.172  1.00 35.02 ? 399 HIS A ND1 1 
ATOM   1837 C CD2 . HIS A 1 399 ? 3.727   -0.589  -1.785  1.00 33.67 ? 399 HIS A CD2 1 
ATOM   1838 C CE1 . HIS A 1 399 ? 5.271   -0.549  -3.328  1.00 35.36 ? 399 HIS A CE1 1 
ATOM   1839 N NE2 . HIS A 1 399 ? 3.949   -0.589  -3.147  1.00 35.00 ? 399 HIS A NE2 1 
ATOM   1840 N N   . SER A 1 400 ? 6.043   -2.912  2.946   1.00 25.09 ? 400 SER A N   1 
ATOM   1841 C CA  . SER A 1 400 ? 6.421   -2.983  4.344   1.00 23.76 ? 400 SER A CA  1 
ATOM   1842 C C   . SER A 1 400 ? 6.413   -4.443  4.758   1.00 21.95 ? 400 SER A C   1 
ATOM   1843 O O   . SER A 1 400 ? 5.846   -5.291  4.057   1.00 21.83 ? 400 SER A O   1 
ATOM   1844 C CB  . SER A 1 400 ? 5.393   -2.234  5.195   1.00 25.35 ? 400 SER A CB  1 
ATOM   1845 O OG  . SER A 1 400 ? 5.745   -2.306  6.571   1.00 26.81 ? 400 SER A OG  1 
ATOM   1846 N N   . GLN A 1 401 ? 6.965   -4.753  5.945   1.00 20.93 ? 401 GLN A N   1 
ATOM   1847 C CA  . GLN A 1 401 ? 6.821   -6.105  6.506   1.00 21.47 ? 401 GLN A CA  1 
ATOM   1848 C C   . GLN A 1 401 ? 5.318   -6.433  6.669   1.00 21.88 ? 401 GLN A C   1 
ATOM   1849 O O   . GLN A 1 401 ? 4.500   -5.530  6.878   1.00 22.91 ? 401 GLN A O   1 
ATOM   1850 C CB  . GLN A 1 401 ? 7.483   -6.183  7.885   1.00 24.66 ? 401 GLN A CB  1 
ATOM   1851 C CG  . GLN A 1 401 ? 6.946   -5.201  8.893   1.00 27.74 ? 401 GLN A CG  1 
ATOM   1852 C CD  . GLN A 1 401 ? 7.672   -5.263  10.236  1.00 34.04 ? 401 GLN A CD  1 
ATOM   1853 O OE1 . GLN A 1 401 ? 7.172   -4.744  11.234  1.00 36.02 ? 401 GLN A OE1 1 
ATOM   1854 N NE2 . GLN A 1 401 ? 8.870   -5.873  10.315  1.00 33.86 ? 401 GLN A NE2 1 
ATOM   1855 N N   . VAL A 1 402 ? 4.961   -7.697  6.530   1.00 20.23 ? 402 VAL A N   1 
ATOM   1856 C CA  . VAL A 1 402 ? 3.575   -8.137  6.671   1.00 20.52 ? 402 VAL A CA  1 
ATOM   1857 C C   . VAL A 1 402 ? 3.557   -9.001  7.942   1.00 21.25 ? 402 VAL A C   1 
ATOM   1858 O O   . VAL A 1 402 ? 4.044   -10.133 7.904   1.00 22.87 ? 402 VAL A O   1 
ATOM   1859 C CB  . VAL A 1 402 ? 3.126   -8.972  5.447   1.00 20.45 ? 402 VAL A CB  1 
ATOM   1860 C CG1 . VAL A 1 402 ? 1.619   -9.258  5.507   1.00 20.82 ? 402 VAL A CG1 1 
ATOM   1861 C CG2 . VAL A 1 402 ? 3.492   -8.281  4.130   1.00 20.87 ? 402 VAL A CG2 1 
ATOM   1862 N N   . CYS A 1 403 ? 3.057   -8.475  9.061   1.00 20.56 ? 403 CYS A N   1 
ATOM   1863 C CA  . CYS A 1 403 ? 3.078   -9.217  10.328  1.00 20.36 ? 403 CYS A CA  1 
ATOM   1864 C C   . CYS A 1 403 ? 1.968   -10.247 10.405  1.00 19.22 ? 403 CYS A C   1 
ATOM   1865 O O   . CYS A 1 403 ? 2.162   -11.325 10.956  1.00 20.35 ? 403 CYS A O   1 
ATOM   1866 C CB  . CYS A 1 403 ? 3.015   -8.256  11.514  1.00 21.64 ? 403 CYS A CB  1 
ATOM   1867 S SG  . CYS A 1 403 ? 1.421   -7.413  11.704  1.00 26.48 ? 403 CYS A SG  1 
ATOM   1868 N N   A SER A 1 404 ? 0.803   -9.918  9.850   0.60 17.53 ? 404 SER A N   1 
ATOM   1869 N N   B SER A 1 404 ? 0.796   -9.914  9.853   0.40 17.88 ? 404 SER A N   1 
ATOM   1870 C CA  A SER A 1 404 ? -0.361  -10.785 9.878   0.60 16.66 ? 404 SER A CA  1 
ATOM   1871 C CA  B SER A 1 404 ? -0.367  -10.779 9.939   0.40 17.23 ? 404 SER A CA  1 
ATOM   1872 C C   A SER A 1 404 ? -1.220  -10.598 8.659   0.60 15.40 ? 404 SER A C   1 
ATOM   1873 C C   B SER A 1 404 ? -1.347  -10.542 8.815   0.40 16.00 ? 404 SER A C   1 
ATOM   1874 O O   A SER A 1 404 ? -1.179  -9.560  8.002   0.60 14.97 ? 404 SER A O   1 
ATOM   1875 O O   B SER A 1 404 ? -1.532  -9.410  8.404   0.40 15.91 ? 404 SER A O   1 
ATOM   1876 C CB  A SER A 1 404 ? -1.233  -10.464 11.095  0.60 18.39 ? 404 SER A CB  1 
ATOM   1877 C CB  B SER A 1 404 ? -1.084  -10.522 11.260  0.40 19.02 ? 404 SER A CB  1 
ATOM   1878 O OG  A SER A 1 404 ? -0.637  -10.832 12.325  0.60 20.28 ? 404 SER A OG  1 
ATOM   1879 O OG  B SER A 1 404 ? -2.214  -11.359 11.422  0.40 21.16 ? 404 SER A OG  1 
ATOM   1880 N N   . ILE A 1 405 ? -2.050  -11.599 8.391   1.00 15.03 ? 405 ILE A N   1 
ATOM   1881 C CA  . ILE A 1 405 ? -3.072  -11.546 7.372   1.00 15.75 ? 405 ILE A CA  1 
ATOM   1882 C C   . ILE A 1 405 ? -4.300  -12.231 7.964   1.00 15.58 ? 405 ILE A C   1 
ATOM   1883 O O   . ILE A 1 405 ? -4.175  -13.275 8.602   1.00 15.41 ? 405 ILE A O   1 
ATOM   1884 C CB  . ILE A 1 405 ? -2.658  -12.298 6.089   1.00 16.66 ? 405 ILE A CB  1 
ATOM   1885 C CG1 . ILE A 1 405 ? -1.516  -11.590 5.388   1.00 17.66 ? 405 ILE A CG1 1 
ATOM   1886 C CG2 . ILE A 1 405 ? -3.855  -12.443 5.129   1.00 16.61 ? 405 ILE A CG2 1 
ATOM   1887 C CD1 . ILE A 1 405 ? -0.823  -12.464 4.371   1.00 19.39 ? 405 ILE A CD1 1 
ATOM   1888 N N   . LEU A 1 406 ? -5.481  -11.681 7.712   1.00 15.17 ? 406 LEU A N   1 
ATOM   1889 C CA  . LEU A 1 406 ? -6.750  -12.310 8.060   1.00 15.07 ? 406 LEU A CA  1 
ATOM   1890 C C   . LEU A 1 406 ? -7.647  -12.229 6.832   1.00 15.15 ? 406 LEU A C   1 
ATOM   1891 O O   . LEU A 1 406 ? -7.526  -11.296 6.032   1.00 16.22 ? 406 LEU A O   1 
ATOM   1892 C CB  . LEU A 1 406 ? -7.455  -11.570 9.208   1.00 16.13 ? 406 LEU A CB  1 
ATOM   1893 C CG  . LEU A 1 406 ? -6.732  -11.574 10.543  1.00 17.87 ? 406 LEU A CG  1 
ATOM   1894 C CD1 . LEU A 1 406 ? -7.374  -10.568 11.461  1.00 19.20 ? 406 LEU A CD1 1 
ATOM   1895 C CD2 . LEU A 1 406 ? -6.737  -12.949 11.169  1.00 18.59 ? 406 LEU A CD2 1 
ATOM   1896 N N   . TRP A 1 407 ? -8.550  -13.176 6.679   1.00 14.05 ? 407 TRP A N   1 
ATOM   1897 C CA  . TRP A 1 407 ? -9.537  -13.119 5.606   1.00 15.75 ? 407 TRP A CA  1 
ATOM   1898 C C   . TRP A 1 407 ? -10.901 -12.764 6.208   1.00 16.94 ? 407 TRP A C   1 
ATOM   1899 O O   . TRP A 1 407 ? -11.264 -13.340 7.235   1.00 17.00 ? 407 TRP A O   1 
ATOM   1900 C CB  . TRP A 1 407 ? -9.718  -14.520 4.981   1.00 16.16 ? 407 TRP A CB  1 
ATOM   1901 C CG  . TRP A 1 407 ? -8.501  -15.056 4.283   1.00 17.26 ? 407 TRP A CG  1 
ATOM   1902 C CD1 . TRP A 1 407 ? -7.400  -15.609 4.869   1.00 17.62 ? 407 TRP A CD1 1 
ATOM   1903 C CD2 . TRP A 1 407 ? -8.287  -15.135 2.867   1.00 17.17 ? 407 TRP A CD2 1 
ATOM   1904 N NE1 . TRP A 1 407 ? -6.540  -16.080 3.903   1.00 17.25 ? 407 TRP A NE1 1 
ATOM   1905 C CE2 . TRP A 1 407 ? -7.059  -15.793 2.665   1.00 17.56 ? 407 TRP A CE2 1 
ATOM   1906 C CE3 . TRP A 1 407 ? -9.048  -14.777 1.745   1.00 18.50 ? 407 TRP A CE3 1 
ATOM   1907 C CZ2 . TRP A 1 407 ? -6.551  -16.058 1.388   1.00 18.34 ? 407 TRP A CZ2 1 
ATOM   1908 C CZ3 . TRP A 1 407 ? -8.546  -15.046 0.483   1.00 19.80 ? 407 TRP A CZ3 1 
ATOM   1909 C CH2 . TRP A 1 407 ? -7.291  -15.636 0.318   1.00 19.83 ? 407 TRP A CH2 1 
ATOM   1910 N N   . SER A 1 408 ? -11.719 -11.939 5.504   1.00 18.79 ? 408 SER A N   1 
ATOM   1911 C CA  . SER A 1 408 ? -13.093 -11.722 5.951   1.00 21.25 ? 408 SER A CA  1 
ATOM   1912 C C   . SER A 1 408 ? -13.869 -12.769 5.188   1.00 25.60 ? 408 SER A C   1 
ATOM   1913 O O   . SER A 1 408 ? -13.948 -12.671 3.969   1.00 26.64 ? 408 SER A O   1 
ATOM   1914 C CB  . SER A 1 408 ? -13.653 -10.374 5.500   1.00 20.81 ? 408 SER A CB  1 
ATOM   1915 O OG  . SER A 1 408 ? -15.065 -10.352 5.721   1.00 21.14 ? 408 SER A OG  1 
ATOM   1916 N N   . PRO A 1 409 ? -14.569 -13.657 5.877   1.00 28.99 ? 409 PRO A N   1 
ATOM   1917 C CA  . PRO A 1 409 ? -15.420 -14.622 5.158   1.00 30.52 ? 409 PRO A CA  1 
ATOM   1918 C C   . PRO A 1 409 ? -16.708 -13.995 4.588   1.00 30.91 ? 409 PRO A C   1 
ATOM   1919 O O   . PRO A 1 409 ? -17.280 -14.506 3.612   1.00 33.48 ? 409 PRO A O   1 
ATOM   1920 C CB  . PRO A 1 409 ? -15.730 -15.669 6.227   1.00 31.70 ? 409 PRO A CB  1 
ATOM   1921 C CG  . PRO A 1 409 ? -15.621 -14.964 7.514   1.00 31.78 ? 409 PRO A CG  1 
ATOM   1922 C CD  . PRO A 1 409 ? -14.621 -13.842 7.339   1.00 29.23 ? 409 PRO A CD  1 
ATOM   1923 N N   A HIS A 1 410 ? -17.156 -12.882 5.173   0.54 29.20 ? 410 HIS A N   1 
ATOM   1924 N N   B HIS A 1 410 ? -17.156 -12.881 5.171   0.46 29.30 ? 410 HIS A N   1 
ATOM   1925 C CA  A HIS A 1 410 ? -18.373 -12.220 4.728   0.54 28.72 ? 410 HIS A CA  1 
ATOM   1926 C CA  B HIS A 1 410 ? -18.376 -12.224 4.724   0.46 28.80 ? 410 HIS A CA  1 
ATOM   1927 C C   A HIS A 1 410 ? -18.150 -11.310 3.516   0.54 28.36 ? 410 HIS A C   1 
ATOM   1928 C C   B HIS A 1 410 ? -18.159 -11.298 3.521   0.46 28.38 ? 410 HIS A C   1 
ATOM   1929 O O   A HIS A 1 410 ? -18.948 -11.332 2.578   0.54 28.70 ? 410 HIS A O   1 
ATOM   1930 O O   B HIS A 1 410 ? -18.963 -11.310 2.588   0.46 28.68 ? 410 HIS A O   1 
ATOM   1931 C CB  A HIS A 1 410 ? -18.990 -11.431 5.894   0.54 29.33 ? 410 HIS A CB  1 
ATOM   1932 C CB  B HIS A 1 410 ? -19.028 -11.480 5.898   0.46 29.39 ? 410 HIS A CB  1 
ATOM   1933 C CG  A HIS A 1 410 ? -19.216 -12.264 7.117   0.54 31.42 ? 410 HIS A CG  1 
ATOM   1934 C CG  B HIS A 1 410 ? -19.286 -12.368 7.075   0.46 31.33 ? 410 HIS A CG  1 
ATOM   1935 N ND1 A HIS A 1 410 ? -20.130 -13.300 7.126   0.54 33.14 ? 410 HIS A ND1 1 
ATOM   1936 N ND1 B HIS A 1 410 ? -18.481 -12.327 8.199   0.46 33.43 ? 410 HIS A ND1 1 
ATOM   1937 C CD2 A HIS A 1 410 ? -18.630 -12.188 8.335   0.54 32.88 ? 410 HIS A CD2 1 
ATOM   1938 C CD2 B HIS A 1 410 ? -20.227 -13.326 7.246   0.46 32.41 ? 410 HIS A CD2 1 
ATOM   1939 C CE1 A HIS A 1 410 ? -20.080 -13.813 8.342   0.54 33.90 ? 410 HIS A CE1 1 
ATOM   1940 C CE1 B HIS A 1 410 ? -18.972 -13.239 9.025   0.46 34.08 ? 410 HIS A CE1 1 
ATOM   1941 N NE2 A HIS A 1 410 ? -19.198 -13.173 9.110   0.54 34.15 ? 410 HIS A NE2 1 
ATOM   1942 N NE2 B HIS A 1 410 ? -20.026 -13.863 8.495   0.46 33.69 ? 410 HIS A NE2 1 
ATOM   1943 N N   . TYR A 1 411 ? -17.073 -10.512 3.524   1.00 27.52 ? 411 TYR A N   1 
ATOM   1944 C CA  . TYR A 1 411 ? -16.811 -9.570  2.420   1.00 27.19 ? 411 TYR A CA  1 
ATOM   1945 C C   . TYR A 1 411 ? -15.920 -10.029 1.264   1.00 28.98 ? 411 TYR A C   1 
ATOM   1946 O O   . TYR A 1 411 ? -15.771 -9.267  0.301   1.00 29.74 ? 411 TYR A O   1 
ATOM   1947 C CB  . TYR A 1 411 ? -16.215 -8.279  2.977   1.00 26.58 ? 411 TYR A CB  1 
ATOM   1948 C CG  . TYR A 1 411 ? -17.259 -7.393  3.599   1.00 26.69 ? 411 TYR A CG  1 
ATOM   1949 C CD1 . TYR A 1 411 ? -18.047 -6.558  2.818   1.00 28.09 ? 411 TYR A CD1 1 
ATOM   1950 C CD2 . TYR A 1 411 ? -17.486 -7.410  4.968   1.00 27.39 ? 411 TYR A CD2 1 
ATOM   1951 C CE1 . TYR A 1 411 ? -19.019 -5.746  3.388   1.00 29.00 ? 411 TYR A CE1 1 
ATOM   1952 C CE2 . TYR A 1 411 ? -18.470 -6.618  5.544   1.00 29.03 ? 411 TYR A CE2 1 
ATOM   1953 C CZ  . TYR A 1 411 ? -19.214 -5.769  4.751   1.00 30.27 ? 411 TYR A CZ  1 
ATOM   1954 O OH  . TYR A 1 411 ? -20.178 -4.972  5.313   1.00 33.62 ? 411 TYR A OH  1 
ATOM   1955 N N   . LYS A 1 412 ? -15.259 -11.193 1.362   1.00 28.44 ? 412 LYS A N   1 
ATOM   1956 C CA  . LYS A 1 412 ? -14.363 -11.626 0.267   1.00 27.69 ? 412 LYS A CA  1 
ATOM   1957 C C   . LYS A 1 412 ? -13.189 -10.624 0.167   1.00 24.18 ? 412 LYS A C   1 
ATOM   1958 O O   . LYS A 1 412 ? -12.905 -10.058 -0.893  1.00 23.93 ? 412 LYS A O   1 
ATOM   1959 C CB  . LYS A 1 412 ? -15.122 -11.722 -1.070  1.00 31.91 ? 412 LYS A CB  1 
ATOM   1960 C CG  . LYS A 1 412 ? -14.975 -13.052 -1.758  1.00 38.83 ? 412 LYS A CG  1 
ATOM   1961 C CD  . LYS A 1 412 ? -16.306 -13.736 -1.957  1.00 44.02 ? 412 LYS A CD  1 
ATOM   1962 C CE  . LYS A 1 412 ? -16.136 -15.036 -2.694  1.00 47.99 ? 412 LYS A CE  1 
ATOM   1963 N NZ  . LYS A 1 412 ? -17.345 -15.882 -2.581  1.00 50.50 ? 412 LYS A NZ  1 
ATOM   1964 N N   . GLU A 1 413 ? -12.609 -10.327 1.304   1.00 21.27 ? 413 GLU A N   1 
ATOM   1965 C CA  . GLU A 1 413 ? -11.501 -9.378  1.419   1.00 19.83 ? 413 GLU A CA  1 
ATOM   1966 C C   . GLU A 1 413 ? -10.432 -9.964  2.324   1.00 20.32 ? 413 GLU A C   1 
ATOM   1967 O O   . GLU A 1 413 ? -10.691 -10.897 3.075   1.00 20.39 ? 413 GLU A O   1 
ATOM   1968 C CB  . GLU A 1 413 ? -11.994 -8.029  2.023   1.00 20.75 ? 413 GLU A CB  1 
ATOM   1969 C CG  . GLU A 1 413 ? -12.943 -7.248  1.119   1.00 22.08 ? 413 GLU A CG  1 
ATOM   1970 C CD  . GLU A 1 413 ? -13.619 -6.026  1.720   1.00 24.01 ? 413 GLU A CD  1 
ATOM   1971 O OE1 . GLU A 1 413 ? -13.404 -5.743  2.921   1.00 24.64 ? 413 GLU A OE1 1 
ATOM   1972 O OE2 . GLU A 1 413 ? -14.374 -5.350  0.986   1.00 26.66 ? 413 GLU A OE2 1 
ATOM   1973 N N   . LEU A 1 414 ? -9.230  -9.397  2.273   1.00 19.33 ? 414 LEU A N   1 
ATOM   1974 C CA  . LEU A 1 414 ? -8.153  -9.770  3.189   1.00 20.28 ? 414 LEU A CA  1 
ATOM   1975 C C   . LEU A 1 414 ? -7.732  -8.497  3.904   1.00 18.59 ? 414 LEU A C   1 
ATOM   1976 O O   . LEU A 1 414 ? -7.876  -7.414  3.353   1.00 18.87 ? 414 LEU A O   1 
ATOM   1977 C CB  . LEU A 1 414 ? -6.940  -10.259 2.408   1.00 23.45 ? 414 LEU A CB  1 
ATOM   1978 C CG  . LEU A 1 414 ? -7.177  -11.446 1.575   1.00 28.29 ? 414 LEU A CG  1 
ATOM   1979 C CD1 . LEU A 1 414 ? -7.245  -11.050 0.146   1.00 30.46 ? 414 LEU A CD1 1 
ATOM   1980 C CD2 . LEU A 1 414 ? -6.142  -12.493 1.862   1.00 29.91 ? 414 LEU A CD2 1 
ATOM   1981 N N   . ILE A 1 415 ? -7.187  -8.618  5.107   1.00 16.97 ? 415 ILE A N   1 
ATOM   1982 C CA  . ILE A 1 415 ? -6.640  -7.477  5.823   1.00 16.33 ? 415 ILE A CA  1 
ATOM   1983 C C   . ILE A 1 415 ? -5.248  -7.882  6.299   1.00 16.30 ? 415 ILE A C   1 
ATOM   1984 O O   . ILE A 1 415 ? -5.029  -9.022  6.761   1.00 16.47 ? 415 ILE A O   1 
ATOM   1985 C CB  . ILE A 1 415 ? -7.552  -6.981  6.967   1.00 17.20 ? 415 ILE A CB  1 
ATOM   1986 C CG1 . ILE A 1 415 ? -7.012  -5.669  7.553   1.00 18.26 ? 415 ILE A CG1 1 
ATOM   1987 C CG2 . ILE A 1 415 ? -7.725  -8.048  8.035   1.00 17.95 ? 415 ILE A CG2 1 
ATOM   1988 C CD1 . ILE A 1 415 ? -7.995  -5.003  8.536   1.00 19.20 ? 415 ILE A CD1 1 
ATOM   1989 N N   . SER A 1 416 ? -4.290  -6.981  6.139   1.00 16.02 ? 416 SER A N   1 
ATOM   1990 C CA  . SER A 1 416 ? -2.914  -7.245  6.535   1.00 15.16 ? 416 SER A CA  1 
ATOM   1991 C C   . SER A 1 416 ? -2.407  -6.153  7.454   1.00 16.62 ? 416 SER A C   1 
ATOM   1992 O O   . SER A 1 416 ? -2.885  -5.028  7.370   1.00 17.72 ? 416 SER A O   1 
ATOM   1993 C CB  . SER A 1 416 ? -2.018  -7.361  5.301   1.00 16.08 ? 416 SER A CB  1 
ATOM   1994 O OG  . SER A 1 416 ? -2.129  -6.210  4.477   1.00 17.83 ? 416 SER A OG  1 
ATOM   1995 N N   . GLY A 1 417 ? -1.467  -6.484  8.338   1.00 16.11 ? 417 GLY A N   1 
ATOM   1996 C CA  . GLY A 1 417 ? -0.875  -5.500  9.244   1.00 17.17 ? 417 GLY A CA  1 
ATOM   1997 C C   . GLY A 1 417 ? 0.567   -5.245  8.869   1.00 17.92 ? 417 GLY A C   1 
ATOM   1998 O O   . GLY A 1 417 ? 1.249   -6.134  8.348   1.00 18.39 ? 417 GLY A O   1 
ATOM   1999 N N   . HIS A 1 418 ? 1.031   -4.022  9.097   1.00 17.53 ? 418 HIS A N   1 
ATOM   2000 C CA  . HIS A 1 418 ? 2.331   -3.570  8.606   1.00 19.52 ? 418 HIS A CA  1 
ATOM   2001 C C   . HIS A 1 418 ? 3.140   -2.748  9.580   1.00 20.70 ? 418 HIS A C   1 
ATOM   2002 O O   . HIS A 1 418 ? 2.654   -2.394  10.651  1.00 20.84 ? 418 HIS A O   1 
ATOM   2003 C CB  . HIS A 1 418 ? 2.120   -2.786  7.296   1.00 19.66 ? 418 HIS A CB  1 
ATOM   2004 C CG  . HIS A 1 418 ? 1.364   -3.589  6.284   1.00 21.29 ? 418 HIS A CG  1 
ATOM   2005 N ND1 . HIS A 1 418 ? 1.968   -4.641  5.603   1.00 23.03 ? 418 HIS A ND1 1 
ATOM   2006 C CD2 . HIS A 1 418 ? 0.047   -3.557  5.963   1.00 22.93 ? 418 HIS A CD2 1 
ATOM   2007 C CE1 . HIS A 1 418 ? 1.008   -5.195  4.868   1.00 23.68 ? 418 HIS A CE1 1 
ATOM   2008 N NE2 . HIS A 1 418 ? -0.159  -4.560  5.027   1.00 23.58 ? 418 HIS A NE2 1 
ATOM   2009 N N   . GLY A 1 419 ? 4.397   -2.501  9.202   1.00 21.28 ? 419 GLY A N   1 
ATOM   2010 C CA  . GLY A 1 419 ? 5.355   -1.761  9.989   1.00 22.83 ? 419 GLY A CA  1 
ATOM   2011 C C   . GLY A 1 419 ? 5.767   -0.498  9.273   1.00 24.87 ? 419 GLY A C   1 
ATOM   2012 O O   . GLY A 1 419 ? 4.933   0.216   8.717   1.00 24.86 ? 419 GLY A O   1 
ATOM   2013 N N   . PHE A 1 420 ? 7.068   -0.227  9.257   1.00 25.60 ? 420 PHE A N   1 
ATOM   2014 C CA  . PHE A 1 420 ? 7.632   0.968   8.634   1.00 27.85 ? 420 PHE A CA  1 
ATOM   2015 C C   . PHE A 1 420 ? 7.202   1.063   7.155   1.00 27.63 ? 420 PHE A C   1 
ATOM   2016 O O   . PHE A 1 420 ? 7.195   0.052   6.486   1.00 27.13 ? 420 PHE A O   1 
ATOM   2017 C CB  . PHE A 1 420 ? 9.160   0.912   8.781   1.00 29.42 ? 420 PHE A CB  1 
ATOM   2018 C CG  . PHE A 1 420 ? 9.866   2.165   8.337   1.00 32.41 ? 420 PHE A CG  1 
ATOM   2019 C CD1 . PHE A 1 420 ? 10.012  3.237   9.198   1.00 34.06 ? 420 PHE A CD1 1 
ATOM   2020 C CD2 . PHE A 1 420 ? 10.351  2.286   7.047   1.00 34.19 ? 420 PHE A CD2 1 
ATOM   2021 C CE1 . PHE A 1 420 ? 10.661  4.393   8.786   1.00 35.47 ? 420 PHE A CE1 1 
ATOM   2022 C CE2 . PHE A 1 420 ? 11.012  3.443   6.641   1.00 35.44 ? 420 PHE A CE2 1 
ATOM   2023 C CZ  . PHE A 1 420 ? 11.154  4.487   7.510   1.00 35.48 ? 420 PHE A CZ  1 
ATOM   2024 N N   . ALA A 1 421 ? 6.710   2.217   6.685   1.00 28.91 ? 421 ALA A N   1 
ATOM   2025 C CA  . ALA A 1 421 ? 6.735   3.486   7.414   1.00 30.38 ? 421 ALA A CA  1 
ATOM   2026 C C   . ALA A 1 421 ? 5.390   3.958   7.968   1.00 30.43 ? 421 ALA A C   1 
ATOM   2027 O O   . ALA A 1 421 ? 5.369   4.863   8.799   1.00 31.57 ? 421 ALA A O   1 
ATOM   2028 C CB  . ALA A 1 421 ? 7.334   4.561   6.522   1.00 31.27 ? 421 ALA A CB  1 
ATOM   2029 N N   . GLN A 1 422 ? 4.280   3.384   7.500   1.00 29.01 ? 422 GLN A N   1 
ATOM   2030 C CA  . GLN A 1 422 ? 2.955   3.851   7.894   1.00 27.83 ? 422 GLN A CA  1 
ATOM   2031 C C   . GLN A 1 422 ? 2.330   3.151   9.087   1.00 26.12 ? 422 GLN A C   1 
ATOM   2032 O O   . GLN A 1 422 ? 1.356   3.679   9.607   1.00 26.47 ? 422 GLN A O   1 
ATOM   2033 C CB  . GLN A 1 422 ? 1.991   3.776   6.702   1.00 29.74 ? 422 GLN A CB  1 
ATOM   2034 N N   . ASN A 1 423 ? 2.828   1.956   9.499   1.00 23.98 ? 423 ASN A N   1 
ATOM   2035 C CA  . ASN A 1 423 ? 2.273   1.189   10.647  1.00 22.83 ? 423 ASN A CA  1 
ATOM   2036 C C   . ASN A 1 423 ? 0.765   1.007   10.504  1.00 22.85 ? 423 ASN A C   1 
ATOM   2037 O O   . ASN A 1 423 ? -0.001  1.207   11.456  1.00 22.91 ? 423 ASN A O   1 
ATOM   2038 C CB  . ASN A 1 423 ? 2.606   1.886   11.966  1.00 22.87 ? 423 ASN A CB  1 
ATOM   2039 C CG  . ASN A 1 423 ? 4.081   2.107   12.115  1.00 25.01 ? 423 ASN A CG  1 
ATOM   2040 O OD1 . ASN A 1 423 ? 4.883   1.213   11.861  1.00 24.55 ? 423 ASN A OD1 1 
ATOM   2041 N ND2 . ASN A 1 423 ? 4.483   3.293   12.514  1.00 27.58 ? 423 ASN A ND2 1 
ATOM   2042 N N   . GLN A 1 424 ? 0.341   0.671   9.295   1.00 22.08 ? 424 GLN A N   1 
ATOM   2043 C CA  . GLN A 1 424 ? -1.076  0.592   8.987   1.00 21.86 ? 424 GLN A CA  1 
ATOM   2044 C C   . GLN A 1 424 ? -1.617  -0.802  8.746   1.00 21.40 ? 424 GLN A C   1 
ATOM   2045 O O   . GLN A 1 424 ? -0.852  -1.765  8.566   1.00 22.07 ? 424 GLN A O   1 
ATOM   2046 C CB  . GLN A 1 424 ? -1.359  1.488   7.752   1.00 22.50 ? 424 GLN A CB  1 
ATOM   2047 C CG  . GLN A 1 424 ? -1.178  0.810   6.366   1.00 25.35 ? 424 GLN A CG  1 
ATOM   2048 C CD  . GLN A 1 424 ? 0.247   0.692   5.877   1.00 28.74 ? 424 GLN A CD  1 
ATOM   2049 O OE1 . GLN A 1 424 ? 1.199   0.484   6.641   1.00 29.41 ? 424 GLN A OE1 1 
ATOM   2050 N NE2 . GLN A 1 424 ? 0.435   0.837   4.565   1.00 29.51 ? 424 GLN A NE2 1 
ATOM   2051 N N   . LEU A 1 425 ? -2.961  -0.904  8.709   1.00 19.62 ? 425 LEU A N   1 
ATOM   2052 C CA  . LEU A 1 425 ? -3.612  -2.121  8.246   1.00 19.16 ? 425 LEU A CA  1 
ATOM   2053 C C   . LEU A 1 425 ? -4.075  -1.817  6.816   1.00 19.43 ? 425 LEU A C   1 
ATOM   2054 O O   . LEU A 1 425 ? -4.507  -0.687  6.524   1.00 19.57 ? 425 LEU A O   1 
ATOM   2055 C CB  . LEU A 1 425 ? -4.840  -2.501  9.085   1.00 19.74 ? 425 LEU A CB  1 
ATOM   2056 C CG  . LEU A 1 425 ? -4.677  -2.627  10.602  1.00 23.55 ? 425 LEU A CG  1 
ATOM   2057 C CD1 . LEU A 1 425 ? -5.859  -3.435  11.193  1.00 22.90 ? 425 LEU A CD1 1 
ATOM   2058 C CD2 . LEU A 1 425 ? -3.404  -3.362  10.961  1.00 26.61 ? 425 LEU A CD2 1 
ATOM   2059 N N   . VAL A 1 426 ? -3.973  -2.799  5.917   1.00 18.03 ? 426 VAL A N   1 
ATOM   2060 C CA  . VAL A 1 426 ? -4.456  -2.611  4.553   1.00 17.65 ? 426 VAL A CA  1 
ATOM   2061 C C   . VAL A 1 426 ? -5.567  -3.622  4.267   1.00 18.52 ? 426 VAL A C   1 
ATOM   2062 O O   . VAL A 1 426 ? -5.390  -4.791  4.568   1.00 17.85 ? 426 VAL A O   1 
ATOM   2063 C CB  . VAL A 1 426 ? -3.331  -2.734  3.503   1.00 18.92 ? 426 VAL A CB  1 
ATOM   2064 C CG1 . VAL A 1 426 ? -3.913  -2.584  2.104   1.00 19.12 ? 426 VAL A CG1 1 
ATOM   2065 C CG2 . VAL A 1 426 ? -2.241  -1.682  3.745   1.00 18.89 ? 426 VAL A CG2 1 
ATOM   2066 N N   . ILE A 1 427 ? -6.705  -3.172  3.710   1.00 18.83 ? 427 ILE A N   1 
ATOM   2067 C CA  . ILE A 1 427 ? -7.790  -4.063  3.315   1.00 19.35 ? 427 ILE A CA  1 
ATOM   2068 C C   . ILE A 1 427 ? -7.678  -4.241  1.809   1.00 19.17 ? 427 ILE A C   1 
ATOM   2069 O O   . ILE A 1 427 ? -7.572  -3.251  1.080   1.00 19.55 ? 427 ILE A O   1 
ATOM   2070 C CB  . ILE A 1 427 ? -9.173  -3.536  3.759   1.00 20.80 ? 427 ILE A CB  1 
ATOM   2071 C CG1 . ILE A 1 427 ? -9.207  -3.430  5.300   1.00 21.90 ? 427 ILE A CG1 1 
ATOM   2072 C CG2 . ILE A 1 427 ? -10.282 -4.459  3.261   1.00 21.63 ? 427 ILE A CG2 1 
ATOM   2073 C CD1 . ILE A 1 427 ? -10.510 -2.854  5.872   1.00 24.54 ? 427 ILE A CD1 1 
ATOM   2074 N N   . TRP A 1 428 ? -7.716  -5.488  1.348   1.00 18.49 ? 428 TRP A N   1 
ATOM   2075 C CA  . TRP A 1 428 ? -7.582  -5.848  -0.060  1.00 19.28 ? 428 TRP A CA  1 
ATOM   2076 C C   . TRP A 1 428 ? -8.827  -6.580  -0.538  1.00 20.41 ? 428 TRP A C   1 
ATOM   2077 O O   . TRP A 1 428 ? -9.343  -7.432  0.180   1.00 20.34 ? 428 TRP A O   1 
ATOM   2078 C CB  . TRP A 1 428 ? -6.383  -6.796  -0.244  1.00 19.13 ? 428 TRP A CB  1 
ATOM   2079 C CG  . TRP A 1 428 ? -5.115  -6.381  0.419   1.00 19.41 ? 428 TRP A CG  1 
ATOM   2080 C CD1 . TRP A 1 428 ? -4.723  -6.674  1.687   1.00 20.05 ? 428 TRP A CD1 1 
ATOM   2081 C CD2 . TRP A 1 428 ? -3.994  -5.746  -0.213  1.00 19.79 ? 428 TRP A CD2 1 
ATOM   2082 N NE1 . TRP A 1 428 ? -3.462  -6.177  1.917   1.00 20.37 ? 428 TRP A NE1 1 
ATOM   2083 C CE2 . TRP A 1 428 ? -2.976  -5.636  0.753   1.00 20.31 ? 428 TRP A CE2 1 
ATOM   2084 C CE3 . TRP A 1 428 ? -3.758  -5.263  -1.503  1.00 20.60 ? 428 TRP A CE3 1 
ATOM   2085 C CZ2 . TRP A 1 428 ? -1.752  -5.026  0.477   1.00 21.71 ? 428 TRP A CZ2 1 
ATOM   2086 C CZ3 . TRP A 1 428 ? -2.554  -4.633  -1.767  1.00 21.62 ? 428 TRP A CZ3 1 
ATOM   2087 C CH2 . TRP A 1 428 ? -1.558  -4.549  -0.795  1.00 21.76 ? 428 TRP A CH2 1 
ATOM   2088 N N   . LYS A 1 429 ? -9.300  -6.287  -1.741  1.00 21.18 ? 429 LYS A N   1 
ATOM   2089 C CA  . LYS A 1 429 ? -10.450 -6.998  -2.287  1.00 22.55 ? 429 LYS A CA  1 
ATOM   2090 C C   . LYS A 1 429 ? -9.931  -8.299  -2.884  1.00 23.88 ? 429 LYS A C   1 
ATOM   2091 O O   . LYS A 1 429 ? -8.906  -8.282  -3.558  1.00 24.59 ? 429 LYS A O   1 
ATOM   2092 C CB  . LYS A 1 429 ? -11.167 -6.172  -3.357  1.00 26.25 ? 429 LYS A CB  1 
ATOM   2093 C CG  . LYS A 1 429 ? -12.456 -6.825  -3.867  1.00 33.01 ? 429 LYS A CG  1 
ATOM   2094 C CD  . LYS A 1 429 ? -13.505 -6.904  -2.749  1.00 39.21 ? 429 LYS A CD  1 
ATOM   2095 C CE  . LYS A 1 429 ? -14.710 -7.732  -3.120  1.00 43.99 ? 429 LYS A CE  1 
ATOM   2096 N NZ  . LYS A 1 429 ? -14.429 -9.186  -3.026  1.00 46.74 ? 429 LYS A NZ  1 
ATOM   2097 N N   . TYR A 1 430 ? -10.607 -9.421  -2.638  1.00 23.88 ? 430 TYR A N   1 
ATOM   2098 C CA  . TYR A 1 430 ? -10.200 -10.702 -3.210  1.00 24.09 ? 430 TYR A CA  1 
ATOM   2099 C C   . TYR A 1 430 ? -11.225 -11.129 -4.291  1.00 24.09 ? 430 TYR A C   1 
ATOM   2100 O O   . TYR A 1 430 ? -12.414 -10.908 -4.079  1.00 23.74 ? 430 TYR A O   1 
ATOM   2101 C CB  . TYR A 1 430 ? -10.121 -11.746 -2.102  1.00 24.23 ? 430 TYR A CB  1 
ATOM   2102 C CG  . TYR A 1 430 ? -9.398  -12.998 -2.541  1.00 26.15 ? 430 TYR A CG  1 
ATOM   2103 C CD1 . TYR A 1 430 ? -8.013  -13.043 -2.584  1.00 27.52 ? 430 TYR A CD1 1 
ATOM   2104 C CD2 . TYR A 1 430 ? -10.099 -14.122 -2.956  1.00 27.91 ? 430 TYR A CD2 1 
ATOM   2105 C CE1 . TYR A 1 430 ? -7.340  -14.181 -2.993  1.00 29.24 ? 430 TYR A CE1 1 
ATOM   2106 C CE2 . TYR A 1 430 ? -9.435  -15.270 -3.373  1.00 29.21 ? 430 TYR A CE2 1 
ATOM   2107 C CZ  . TYR A 1 430 ? -8.052  -15.296 -3.375  1.00 30.80 ? 430 TYR A CZ  1 
ATOM   2108 O OH  . TYR A 1 430 ? -7.362  -16.403 -3.797  1.00 33.83 ? 430 TYR A OH  1 
ATOM   2109 N N   . PRO A 1 431 ? -10.823 -11.670 -5.467  1.00 24.40 ? 431 PRO A N   1 
ATOM   2110 C CA  . PRO A 1 431 ? -9.465  -12.082 -5.870  1.00 25.05 ? 431 PRO A CA  1 
ATOM   2111 C C   . PRO A 1 431 ? -8.616  -11.083 -6.633  1.00 26.01 ? 431 PRO A C   1 
ATOM   2112 O O   . PRO A 1 431 ? -7.505  -11.437 -7.012  1.00 26.37 ? 431 PRO A O   1 
ATOM   2113 C CB  . PRO A 1 431 ? -9.745  -13.307 -6.749  1.00 25.84 ? 431 PRO A CB  1 
ATOM   2114 C CG  . PRO A 1 431 ? -11.017 -12.920 -7.467  1.00 26.35 ? 431 PRO A CG  1 
ATOM   2115 C CD  . PRO A 1 431 ? -11.828 -12.120 -6.452  1.00 24.46 ? 431 PRO A CD  1 
ATOM   2116 N N   . THR A 1 432 ? -9.103  -9.861  -6.872  1.00 26.46 ? 432 THR A N   1 
ATOM   2117 C CA  . THR A 1 432 ? -8.344  -8.867  -7.636  1.00 27.49 ? 432 THR A CA  1 
ATOM   2118 C C   . THR A 1 432 ? -7.102  -8.323  -6.944  1.00 27.68 ? 432 THR A C   1 
ATOM   2119 O O   . THR A 1 432 ? -6.224  -7.761  -7.607  1.00 27.82 ? 432 THR A O   1 
ATOM   2120 C CB  . THR A 1 432 ? -9.247  -7.692  -8.010  1.00 30.15 ? 432 THR A CB  1 
ATOM   2121 O OG1 . THR A 1 432 ? -9.667  -7.049  -6.802  1.00 31.54 ? 432 THR A OG1 1 
ATOM   2122 C CG2 . THR A 1 432 ? -10.458 -8.116  -8.851  1.00 31.07 ? 432 THR A CG2 1 
ATOM   2123 N N   . MET A 1 433 ? -7.041  -8.458  -5.607  1.00 26.42 ? 433 MET A N   1 
ATOM   2124 C CA  . MET A 1 433 ? -5.979  -7.927  -4.759  1.00 27.23 ? 433 MET A CA  1 
ATOM   2125 C C   . MET A 1 433 ? -5.868  -6.402  -4.882  1.00 28.01 ? 433 MET A C   1 
ATOM   2126 O O   . MET A 1 433 ? -4.791  -5.852  -4.700  1.00 28.83 ? 433 MET A O   1 
ATOM   2127 C CB  . MET A 1 433 ? -4.626  -8.650  -4.955  1.00 28.08 ? 433 MET A CB  1 
ATOM   2128 C CG  . MET A 1 433 ? -4.644  -10.115 -4.457  1.00 30.16 ? 433 MET A CG  1 
ATOM   2129 S SD  . MET A 1 433 ? -5.161  -10.316 -2.710  1.00 34.65 ? 433 MET A SD  1 
ATOM   2130 C CE  . MET A 1 433 ? -3.836  -9.464  -1.881  1.00 30.31 ? 433 MET A CE  1 
ATOM   2131 N N   . ALA A 1 434 ? -6.990  -5.715  -5.184  1.00 27.95 ? 434 ALA A N   1 
ATOM   2132 C CA  . ALA A 1 434 ? -7.010  -4.259  -5.275  1.00 28.40 ? 434 ALA A CA  1 
ATOM   2133 C C   . ALA A 1 434 ? -7.039  -3.694  -3.856  1.00 28.21 ? 434 ALA A C   1 
ATOM   2134 O O   . ALA A 1 434 ? -7.702  -4.255  -2.990  1.00 27.32 ? 434 ALA A O   1 
ATOM   2135 C CB  . ALA A 1 434 ? -8.240  -3.794  -6.031  1.00 28.39 ? 434 ALA A CB  1 
ATOM   2136 N N   . LYS A 1 435 ? -6.370  -2.566  -3.632  1.00 28.89 ? 435 LYS A N   1 
ATOM   2137 C CA  . LYS A 1 435 ? -6.343  -1.944  -2.304  1.00 30.31 ? 435 LYS A CA  1 
ATOM   2138 C C   . LYS A 1 435 ? -7.664  -1.233  -2.071  1.00 31.14 ? 435 LYS A C   1 
ATOM   2139 O O   . LYS A 1 435 ? -8.006  -0.316  -2.821  1.00 31.76 ? 435 LYS A O   1 
ATOM   2140 C CB  . LYS A 1 435 ? -5.178  -0.949  -2.241  1.00 32.60 ? 435 LYS A CB  1 
ATOM   2141 C CG  . LYS A 1 435 ? -4.694  -0.565  -0.859  1.00 35.63 ? 435 LYS A CG  1 
ATOM   2142 C CD  . LYS A 1 435 ? -3.345  0.147   -1.008  1.00 41.02 ? 435 LYS A CD  1 
ATOM   2143 C CE  . LYS A 1 435 ? -2.485  0.113   0.222   1.00 45.73 ? 435 LYS A CE  1 
ATOM   2144 N NZ  . LYS A 1 435 ? -1.062  0.428   -0.079  1.00 48.95 ? 435 LYS A NZ  1 
ATOM   2145 N N   . VAL A 1 436 ? -8.409  -1.648  -1.050  1.00 30.70 ? 436 VAL A N   1 
ATOM   2146 C CA  . VAL A 1 436 ? -9.721  -1.090  -0.721  1.00 31.31 ? 436 VAL A CA  1 
ATOM   2147 C C   . VAL A 1 436 ? -9.614  0.098   0.235   1.00 30.64 ? 436 VAL A C   1 
ATOM   2148 O O   . VAL A 1 436 ? -10.298 1.112   0.063   1.00 31.01 ? 436 VAL A O   1 
ATOM   2149 C CB  . VAL A 1 436 ? -10.616 -2.202  -0.108  1.00 33.14 ? 436 VAL A CB  1 
ATOM   2150 C CG1 . VAL A 1 436 ? -11.932 -1.644  0.415   1.00 34.80 ? 436 VAL A CG1 1 
ATOM   2151 C CG2 . VAL A 1 436 ? -10.871 -3.301  -1.117  1.00 33.40 ? 436 VAL A CG2 1 
ATOM   2152 N N   . ALA A 1 437 ? -8.794  -0.048  1.277   1.00 28.44 ? 437 ALA A N   1 
ATOM   2153 C CA  . ALA A 1 437 ? -8.689  0.960   2.315   1.00 27.47 ? 437 ALA A CA  1 
ATOM   2154 C C   . ALA A 1 437 ? -7.408  0.771   3.133   1.00 25.94 ? 437 ALA A C   1 
ATOM   2155 O O   . ALA A 1 437 ? -6.826  -0.324  3.143   1.00 25.75 ? 437 ALA A O   1 
ATOM   2156 C CB  . ALA A 1 437 ? -9.914  0.851   3.250   1.00 27.64 ? 437 ALA A CB  1 
ATOM   2157 N N   . GLU A 1 438 ? -7.010  1.813   3.871   1.00 24.69 ? 438 GLU A N   1 
ATOM   2158 C CA  . GLU A 1 438 ? -5.883  1.748   4.784   1.00 24.84 ? 438 GLU A CA  1 
ATOM   2159 C C   . GLU A 1 438 ? -6.342  2.262   6.148   1.00 24.63 ? 438 GLU A C   1 
ATOM   2160 O O   . GLU A 1 438 ? -6.943  3.340   6.238   1.00 25.39 ? 438 GLU A O   1 
ATOM   2161 C CB  . GLU A 1 438 ? -4.718  2.592   4.263   1.00 27.47 ? 438 GLU A CB  1 
ATOM   2162 C CG  . GLU A 1 438 ? -3.987  1.927   3.115   1.00 33.02 ? 438 GLU A CG  1 
ATOM   2163 C CD  . GLU A 1 438 ? -2.711  2.668   2.769   1.00 41.81 ? 438 GLU A CD  1 
ATOM   2164 O OE1 . GLU A 1 438 ? -2.804  3.862   2.401   1.00 44.72 ? 438 GLU A OE1 1 
ATOM   2165 O OE2 . GLU A 1 438 ? -1.621  2.062   2.877   1.00 42.78 ? 438 GLU A OE2 1 
ATOM   2166 N N   . LEU A 1 439 ? -6.075  1.497   7.206   1.00 23.02 ? 439 LEU A N   1 
ATOM   2167 C CA  . LEU A 1 439 ? -6.439  1.904   8.553   1.00 22.59 ? 439 LEU A CA  1 
ATOM   2168 C C   . LEU A 1 439 ? -5.188  2.415   9.266   1.00 23.39 ? 439 LEU A C   1 
ATOM   2169 O O   . LEU A 1 439 ? -4.312  1.634   9.622   1.00 23.15 ? 439 LEU A O   1 
ATOM   2170 C CB  . LEU A 1 439 ? -7.086  0.738   9.314   1.00 22.10 ? 439 LEU A CB  1 
ATOM   2171 C CG  . LEU A 1 439 ? -8.319  0.123   8.634   1.00 22.46 ? 439 LEU A CG  1 
ATOM   2172 C CD1 . LEU A 1 439 ? -8.796  -1.094  9.391   1.00 21.79 ? 439 LEU A CD1 1 
ATOM   2173 C CD2 . LEU A 1 439 ? -9.438  1.150   8.467   1.00 23.94 ? 439 LEU A CD2 1 
ATOM   2174 N N   . LYS A 1 440 ? -5.121  3.726   9.476   1.00 23.91 ? 440 LYS A N   1 
ATOM   2175 C CA  . LYS A 1 440 ? -3.969  4.383   10.089  1.00 24.90 ? 440 LYS A CA  1 
ATOM   2176 C C   . LYS A 1 440 ? -4.263  4.878   11.487  1.00 25.87 ? 440 LYS A C   1 
ATOM   2177 O O   . LYS A 1 440 ? -5.415  5.167   11.829  1.00 26.53 ? 440 LYS A O   1 
ATOM   2178 C CB  . LYS A 1 440 ? -3.486  5.547   9.195   1.00 26.75 ? 440 LYS A CB  1 
ATOM   2179 C CG  . LYS A 1 440 ? -2.911  5.068   7.866   1.00 31.18 ? 440 LYS A CG  1 
ATOM   2180 C CD  . LYS A 1 440 ? -2.535  6.233   6.940   1.00 36.54 ? 440 LYS A CD  1 
ATOM   2181 C CE  . LYS A 1 440 ? -2.055  5.753   5.591   1.00 41.25 ? 440 LYS A CE  1 
ATOM   2182 N NZ  . LYS A 1 440 ? -1.834  6.884   4.645   1.00 43.98 ? 440 LYS A NZ  1 
ATOM   2183 N N   . GLY A 1 441 ? -3.221  4.971   12.296  1.00 25.91 ? 441 GLY A N   1 
ATOM   2184 C CA  . GLY A 1 441 ? -3.381  5.393   13.679  1.00 26.28 ? 441 GLY A CA  1 
ATOM   2185 C C   . GLY A 1 441 ? -2.280  4.897   14.579  1.00 25.95 ? 441 GLY A C   1 
ATOM   2186 O O   . GLY A 1 441 ? -1.853  5.624   15.473  1.00 26.53 ? 441 GLY A O   1 
ATOM   2187 N N   . HIS A 1 442 ? -1.807  3.659   14.370  1.00 25.04 ? 442 HIS A N   1 
ATOM   2188 C CA  . HIS A 1 442 ? -0.707  3.122   15.185  1.00 24.77 ? 442 HIS A CA  1 
ATOM   2189 C C   . HIS A 1 442 ? 0.554   3.979   14.972  1.00 25.72 ? 442 HIS A C   1 
ATOM   2190 O O   . HIS A 1 442 ? 0.801   4.424   13.854  1.00 25.85 ? 442 HIS A O   1 
ATOM   2191 C CB  . HIS A 1 442 ? -0.412  1.647   14.858  1.00 23.76 ? 442 HIS A CB  1 
ATOM   2192 C CG  . HIS A 1 442 ? -1.358  0.672   15.500  1.00 22.80 ? 442 HIS A CG  1 
ATOM   2193 N ND1 . HIS A 1 442 ? -1.463  0.568   16.893  1.00 23.74 ? 442 HIS A ND1 1 
ATOM   2194 C CD2 . HIS A 1 442 ? -2.200  -0.222  14.931  1.00 22.57 ? 442 HIS A CD2 1 
ATOM   2195 C CE1 . HIS A 1 442 ? -2.329  -0.417  17.113  1.00 24.07 ? 442 HIS A CE1 1 
ATOM   2196 N NE2 . HIS A 1 442 ? -2.813  -0.910  15.972  1.00 23.61 ? 442 HIS A NE2 1 
ATOM   2197 N N   . THR A 1 443 ? 1.306   4.250   16.047  1.00 26.43 ? 443 THR A N   1 
ATOM   2198 C CA  . THR A 1 443 ? 2.509   5.092   15.951  1.00 27.72 ? 443 THR A CA  1 
ATOM   2199 C C   . THR A 1 443 ? 3.834   4.292   15.929  1.00 27.44 ? 443 THR A C   1 
ATOM   2200 O O   . THR A 1 443 ? 4.905   4.883   15.785  1.00 28.32 ? 443 THR A O   1 
ATOM   2201 C CB  . THR A 1 443 ? 2.495   6.147   17.046  1.00 30.30 ? 443 THR A CB  1 
ATOM   2202 O OG1 . THR A 1 443 ? 2.539   5.480   18.302  1.00 32.00 ? 443 THR A OG1 1 
ATOM   2203 C CG2 . THR A 1 443 ? 1.258   7.031   16.981  1.00 30.73 ? 443 THR A CG2 1 
ATOM   2204 N N   . SER A 1 444 ? 3.745   2.965   16.055  1.00 26.59 ? 444 SER A N   1 
ATOM   2205 C CA  . SER A 1 444 ? 4.827   1.995   15.947  1.00 26.11 ? 444 SER A CA  1 
ATOM   2206 C C   . SER A 1 444 ? 4.300   0.726   15.215  1.00 24.56 ? 444 SER A C   1 
ATOM   2207 O O   . SER A 1 444 ? 3.084   0.568   15.061  1.00 23.77 ? 444 SER A O   1 
ATOM   2208 C CB  . SER A 1 444 ? 5.414   1.666   17.312  1.00 28.38 ? 444 SER A CB  1 
ATOM   2209 O OG  . SER A 1 444 ? 6.085   2.794   17.845  1.00 33.24 ? 444 SER A OG  1 
ATOM   2210 N N   . ARG A 1 445 ? 5.204   -0.141  14.731  1.00 23.15 ? 445 ARG A N   1 
ATOM   2211 C CA  . ARG A 1 445 ? 4.809   -1.298  13.919  1.00 22.71 ? 445 ARG A CA  1 
ATOM   2212 C C   . ARG A 1 445 ? 3.721   -2.181  14.513  1.00 20.80 ? 445 ARG A C   1 
ATOM   2213 O O   . ARG A 1 445 ? 3.690   -2.433  15.714  1.00 21.24 ? 445 ARG A O   1 
ATOM   2214 C CB  . ARG A 1 445 ? 6.025   -2.163  13.553  1.00 24.62 ? 445 ARG A CB  1 
ATOM   2215 C CG  . ARG A 1 445 ? 6.668   -2.834  14.749  1.00 29.39 ? 445 ARG A CG  1 
ATOM   2216 C CD  . ARG A 1 445 ? 7.827   -3.729  14.354  1.00 33.86 ? 445 ARG A CD  1 
ATOM   2217 N NE  . ARG A 1 445 ? 8.377   -4.450  15.507  1.00 35.87 ? 445 ARG A NE  1 
ATOM   2218 C CZ  . ARG A 1 445 ? 9.422   -5.267  15.447  1.00 38.63 ? 445 ARG A CZ  1 
ATOM   2219 N NH1 . ARG A 1 445 ? 9.877   -5.853  16.546  1.00 37.02 ? 445 ARG A NH1 1 
ATOM   2220 N NH2 . ARG A 1 445 ? 10.044  -5.480  14.293  1.00 39.63 ? 445 ARG A NH2 1 
ATOM   2221 N N   . VAL A 1 446 ? 2.822   -2.660  13.656  1.00 20.18 ? 446 VAL A N   1 
ATOM   2222 C CA  . VAL A 1 446 ? 1.817   -3.612  14.085  1.00 20.01 ? 446 VAL A CA  1 
ATOM   2223 C C   . VAL A 1 446 ? 2.535   -4.954  14.288  1.00 19.87 ? 446 VAL A C   1 
ATOM   2224 O O   . VAL A 1 446 ? 3.433   -5.304  13.507  1.00 21.09 ? 446 VAL A O   1 
ATOM   2225 C CB  . VAL A 1 446 ? 0.677   -3.689  13.056  1.00 20.32 ? 446 VAL A CB  1 
ATOM   2226 C CG1 . VAL A 1 446 ? -0.361  -4.724  13.463  1.00 20.01 ? 446 VAL A CG1 1 
ATOM   2227 C CG2 . VAL A 1 446 ? 0.044   -2.308  12.886  1.00 20.17 ? 446 VAL A CG2 1 
ATOM   2228 N N   . LEU A 1 447 ? 2.182   -5.655  15.358  1.00 18.65 ? 447 LEU A N   1 
ATOM   2229 C CA  . LEU A 1 447 ? 2.750   -6.943  15.775  1.00 18.76 ? 447 LEU A CA  1 
ATOM   2230 C C   . LEU A 1 447 ? 1.864   -8.112  15.361  1.00 19.32 ? 447 LEU A C   1 
ATOM   2231 O O   . LEU A 1 447 ? 2.374   -9.096  14.825  1.00 20.29 ? 447 LEU A O   1 
ATOM   2232 C CB  . LEU A 1 447 ? 2.954   -6.947  17.299  1.00 19.23 ? 447 LEU A CB  1 
ATOM   2233 C CG  . LEU A 1 447 ? 4.006   -5.950  17.797  1.00 20.93 ? 447 LEU A CG  1 
ATOM   2234 C CD1 . LEU A 1 447 ? 3.981   -5.823  19.336  1.00 21.95 ? 447 LEU A CD1 1 
ATOM   2235 C CD2 . LEU A 1 447 ? 5.377   -6.355  17.314  1.00 21.30 ? 447 LEU A CD2 1 
ATOM   2236 N N   . SER A 1 448 ? 0.552   -8.026  15.631  1.00 18.22 ? 448 SER A N   1 
ATOM   2237 C CA  . SER A 1 448 ? -0.358  -9.129  15.298  1.00 19.07 ? 448 SER A CA  1 
ATOM   2238 C C   . SER A 1 448 ? -1.765  -8.612  15.061  1.00 17.88 ? 448 SER A C   1 
ATOM   2239 O O   . SER A 1 448 ? -2.149  -7.565  15.593  1.00 18.03 ? 448 SER A O   1 
ATOM   2240 C CB  . SER A 1 448 ? -0.425  -10.090 16.480  1.00 23.14 ? 448 SER A CB  1 
ATOM   2241 O OG  . SER A 1 448 ? 0.772   -10.833 16.651  1.00 29.90 ? 448 SER A OG  1 
ATOM   2242 N N   . LEU A 1 449 ? -2.560  -9.394  14.313  1.00 16.71 ? 449 LEU A N   1 
ATOM   2243 C CA  . LEU A 1 449 ? -3.969  -9.133  14.110  1.00 16.95 ? 449 LEU A CA  1 
ATOM   2244 C C   . LEU A 1 449 ? -4.739  -10.352 14.554  1.00 16.83 ? 449 LEU A C   1 
ATOM   2245 O O   . LEU A 1 449 ? -4.272  -11.489 14.382  1.00 17.34 ? 449 LEU A O   1 
ATOM   2246 C CB  . LEU A 1 449 ? -4.302  -8.950  12.621  1.00 16.90 ? 449 LEU A CB  1 
ATOM   2247 C CG  . LEU A 1 449 ? -3.585  -7.830  11.871  1.00 17.75 ? 449 LEU A CG  1 
ATOM   2248 C CD1 . LEU A 1 449 ? -4.157  -7.685  10.450  1.00 18.54 ? 449 LEU A CD1 1 
ATOM   2249 C CD2 . LEU A 1 449 ? -3.756  -6.522  12.584  1.00 18.09 ? 449 LEU A CD2 1 
ATOM   2250 N N   . THR A 1 450 ? -5.946  -10.131 15.070  1.00 15.34 ? 450 THR A N   1 
ATOM   2251 C CA  . THR A 1 450 ? -6.855  -11.218 15.384  1.00 15.03 ? 450 THR A CA  1 
ATOM   2252 C C   . THR A 1 450 ? -8.279  -10.776 15.071  1.00 15.45 ? 450 THR A C   1 
ATOM   2253 O O   . THR A 1 450 ? -8.576  -9.590  15.144  1.00 16.05 ? 450 THR A O   1 
ATOM   2254 C CB  . THR A 1 450 ? -6.659  -11.764 16.795  1.00 16.47 ? 450 THR A CB  1 
ATOM   2255 O OG1 . THR A 1 450 ? -7.436  -12.970 16.958  1.00 17.89 ? 450 THR A OG1 1 
ATOM   2256 C CG2 . THR A 1 450 ? -7.036  -10.754 17.877  1.00 17.10 ? 450 THR A CG2 1 
ATOM   2257 N N   . MET A 1 451 ? -9.141  -11.716 14.709  1.00 15.79 ? 451 MET A N   1 
ATOM   2258 C CA  . MET A 1 451 ? -10.504 -11.361 14.312  1.00 16.03 ? 451 MET A CA  1 
ATOM   2259 C C   . MET A 1 451 ? -11.550 -11.808 15.323  1.00 16.88 ? 451 MET A C   1 
ATOM   2260 O O   . MET A 1 451 ? -11.463 -12.914 15.850  1.00 17.03 ? 451 MET A O   1 
ATOM   2261 C CB  . MET A 1 451 ? -10.793 -11.998 12.950  1.00 16.72 ? 451 MET A CB  1 
ATOM   2262 C CG  . MET A 1 451 ? -12.194 -11.683 12.451  1.00 20.43 ? 451 MET A CG  1 
ATOM   2263 S SD  . MET A 1 451 ? -12.367 -12.266 10.784  1.00 23.11 ? 451 MET A SD  1 
ATOM   2264 C CE  . MET A 1 451 ? -11.313 -11.047 9.918   1.00 25.61 ? 451 MET A CE  1 
ATOM   2265 N N   . SER A 1 452 ? -12.578 -10.977 15.545  1.00 16.39 ? 452 SER A N   1 
ATOM   2266 C CA  . SER A 1 452 ? -13.708 -11.302 16.451  1.00 17.37 ? 452 SER A CA  1 
ATOM   2267 C C   . SER A 1 452 ? -14.476 -12.519 15.913  1.00 17.77 ? 452 SER A C   1 
ATOM   2268 O O   . SER A 1 452 ? -14.428 -12.799 14.702  1.00 16.83 ? 452 SER A O   1 
ATOM   2269 C CB  . SER A 1 452 ? -14.648 -10.107 16.565  1.00 18.19 ? 452 SER A CB  1 
ATOM   2270 O OG  . SER A 1 452 ? -15.254 -9.842  15.316  1.00 20.20 ? 452 SER A OG  1 
ATOM   2271 N N   . PRO A 1 453 ? -15.191 -13.268 16.775  1.00 19.32 ? 453 PRO A N   1 
ATOM   2272 C CA  . PRO A 1 453 ? -15.844 -14.496 16.279  1.00 20.70 ? 453 PRO A CA  1 
ATOM   2273 C C   . PRO A 1 453 ? -16.941 -14.237 15.252  1.00 22.11 ? 453 PRO A C   1 
ATOM   2274 O O   . PRO A 1 453 ? -17.236 -15.123 14.444  1.00 24.18 ? 453 PRO A O   1 
ATOM   2275 C CB  . PRO A 1 453 ? -16.335 -15.199 17.548  1.00 22.06 ? 453 PRO A CB  1 
ATOM   2276 C CG  . PRO A 1 453 ? -16.356 -14.123 18.621  1.00 22.31 ? 453 PRO A CG  1 
ATOM   2277 C CD  . PRO A 1 453 ? -15.316 -13.117 18.239  1.00 20.26 ? 453 PRO A CD  1 
ATOM   2278 N N   . ASP A 1 454 ? -17.517 -13.027 15.244  1.00 21.59 ? 454 ASP A N   1 
ATOM   2279 C CA  . ASP A 1 454 ? -18.548 -12.717 14.261  1.00 22.34 ? 454 ASP A CA  1 
ATOM   2280 C C   . ASP A 1 454 ? -17.981 -12.221 12.913  1.00 21.99 ? 454 ASP A C   1 
ATOM   2281 O O   . ASP A 1 454 ? -18.728 -12.121 11.954  1.00 23.50 ? 454 ASP A O   1 
ATOM   2282 C CB  . ASP A 1 454 ? -19.598 -11.772 14.823  1.00 23.63 ? 454 ASP A CB  1 
ATOM   2283 C CG  . ASP A 1 454 ? -19.126 -10.377 15.145  1.00 27.83 ? 454 ASP A CG  1 
ATOM   2284 O OD1 . ASP A 1 454 ? -17.906 -10.139 15.113  1.00 28.15 ? 454 ASP A OD1 1 
ATOM   2285 O OD2 . ASP A 1 454 ? -19.970 -9.543  15.500  1.00 30.19 ? 454 ASP A OD2 1 
ATOM   2286 N N   . GLY A 1 455 ? -16.683 -11.953 12.849  1.00 20.04 ? 455 GLY A N   1 
ATOM   2287 C CA  . GLY A 1 455 ? -16.007 -11.495 11.640  1.00 19.89 ? 455 GLY A CA  1 
ATOM   2288 C C   . GLY A 1 455 ? -16.059 -9.988  11.417  1.00 19.77 ? 455 GLY A C   1 
ATOM   2289 O O   . GLY A 1 455 ? -15.512 -9.502  10.424  1.00 19.87 ? 455 GLY A O   1 
ATOM   2290 N N   . ALA A 1 456 ? -16.701 -9.227  12.324  1.00 18.94 ? 456 ALA A N   1 
ATOM   2291 C CA  . ALA A 1 456 ? -16.879 -7.774  12.112  1.00 19.26 ? 456 ALA A CA  1 
ATOM   2292 C C   . ALA A 1 456 ? -15.677 -6.909  12.503  1.00 18.59 ? 456 ALA A C   1 
ATOM   2293 O O   . ALA A 1 456 ? -15.481 -5.836  11.941  1.00 19.45 ? 456 ALA A O   1 
ATOM   2294 C CB  . ALA A 1 456 ? -18.087 -7.302  12.902  1.00 20.54 ? 456 ALA A CB  1 
ATOM   2295 N N   . THR A 1 457 ? -14.949 -7.323  13.532  1.00 17.88 ? 457 THR A N   1 
ATOM   2296 C CA  . THR A 1 457 ? -13.886 -6.527  14.120  1.00 17.19 ? 457 THR A CA  1 
ATOM   2297 C C   . THR A 1 457 ? -12.538 -7.212  14.066  1.00 17.08 ? 457 THR A C   1 
ATOM   2298 O O   . THR A 1 457 ? -12.428 -8.426  14.287  1.00 17.06 ? 457 THR A O   1 
ATOM   2299 C CB  . THR A 1 457 ? -14.272 -6.193  15.600  1.00 19.54 ? 457 THR A CB  1 
ATOM   2300 O OG1 . THR A 1 457 ? -15.595 -5.626  15.660  1.00 22.06 ? 457 THR A OG1 1 
ATOM   2301 C CG2 . THR A 1 457 ? -13.285 -5.246  16.272  1.00 19.23 ? 457 THR A CG2 1 
ATOM   2302 N N   . VAL A 1 458 ? -11.499 -6.424  13.813  1.00 15.58 ? 458 VAL A N   1 
ATOM   2303 C CA  . VAL A 1 458 ? -10.124 -6.881  13.762  1.00 15.07 ? 458 VAL A CA  1 
ATOM   2304 C C   . VAL A 1 458 ? -9.367  -6.149  14.847  1.00 16.03 ? 458 VAL A C   1 
ATOM   2305 O O   . VAL A 1 458 ? -9.405  -4.918  14.865  1.00 17.53 ? 458 VAL A O   1 
ATOM   2306 C CB  . VAL A 1 458 ? -9.527  -6.580  12.368  1.00 16.20 ? 458 VAL A CB  1 
ATOM   2307 C CG1 . VAL A 1 458 ? -8.005  -6.773  12.383  1.00 17.56 ? 458 VAL A CG1 1 
ATOM   2308 C CG2 . VAL A 1 458 ? -10.184 -7.477  11.310  1.00 17.22 ? 458 VAL A CG2 1 
ATOM   2309 N N   . ALA A 1 459 ? -8.707  -6.881  15.759  1.00 14.98 ? 459 ALA A N   1 
ATOM   2310 C CA  . ALA A 1 459 ? -7.893  -6.257  16.775  1.00 15.76 ? 459 ALA A CA  1 
ATOM   2311 C C   . ALA A 1 459 ? -6.453  -6.227  16.282  1.00 16.54 ? 459 ALA A C   1 
ATOM   2312 O O   . ALA A 1 459 ? -5.941  -7.267  15.879  1.00 16.20 ? 459 ALA A O   1 
ATOM   2313 C CB  . ALA A 1 459 ? -7.958  -7.066  18.057  1.00 16.40 ? 459 ALA A CB  1 
ATOM   2314 N N   . SER A 1 460 ? -5.803  -5.073  16.331  1.00 16.91 ? 460 SER A N   1 
ATOM   2315 C CA  . SER A 1 460 ? -4.404  -4.988  15.955  1.00 17.66 ? 460 SER A CA  1 
ATOM   2316 C C   . SER A 1 460 ? -3.604  -4.650  17.210  1.00 18.43 ? 460 SER A C   1 
ATOM   2317 O O   . SER A 1 460 ? -3.946  -3.701  17.913  1.00 19.36 ? 460 SER A O   1 
ATOM   2318 C CB  . SER A 1 460 ? -4.183  -3.945  14.864  1.00 18.98 ? 460 SER A CB  1 
ATOM   2319 O OG  . SER A 1 460 ? -4.667  -2.660  15.232  1.00 19.90 ? 460 SER A OG  1 
ATOM   2320 N N   . ALA A 1 461 ? -2.583  -5.434  17.510  1.00 17.84 ? 461 ALA A N   1 
ATOM   2321 C CA  . ALA A 1 461 ? -1.712  -5.183  18.659  1.00 18.63 ? 461 ALA A CA  1 
ATOM   2322 C C   . ALA A 1 461 ? -0.444  -4.580  18.046  1.00 19.56 ? 461 ALA A C   1 
ATOM   2323 O O   . ALA A 1 461 ? 0.042   -5.092  17.039  1.00 19.27 ? 461 ALA A O   1 
ATOM   2324 C CB  . ALA A 1 461 ? -1.378  -6.498  19.373  1.00 18.48 ? 461 ALA A CB  1 
ATOM   2325 N N   . ALA A 1 462 ? 0.065   -3.503  18.630  1.00 19.92 ? 462 ALA A N   1 
ATOM   2326 C CA  . ALA A 1 462 ? 1.209   -2.829  18.054  1.00 21.25 ? 462 ALA A CA  1 
ATOM   2327 C C   . ALA A 1 462 ? 2.267   -2.456  19.101  1.00 22.03 ? 462 ALA A C   1 
ATOM   2328 O O   . ALA A 1 462 ? 1.979   -2.417  20.300  1.00 22.29 ? 462 ALA A O   1 
ATOM   2329 C CB  . ALA A 1 462 ? 0.736   -1.599  17.281  1.00 21.40 ? 462 ALA A CB  1 
ATOM   2330 N N   . ALA A 1 463 ? 3.492   -2.195  18.638  1.00 22.44 ? 463 ALA A N   1 
ATOM   2331 C CA  . ALA A 1 463 ? 4.620   -1.802  19.483  1.00 23.52 ? 463 ALA A CA  1 
ATOM   2332 C C   . ALA A 1 463 ? 4.416   -0.427  20.182  1.00 24.61 ? 463 ALA A C   1 
ATOM   2333 O O   . ALA A 1 463 ? 5.230   -0.033  21.040  1.00 25.90 ? 463 ALA A O   1 
ATOM   2334 C CB  . ALA A 1 463 ? 5.897   -1.806  18.651  1.00 23.53 ? 463 ALA A CB  1 
ATOM   2335 N N   . ASP A 1 464 ? 3.341   0.311   19.818  1.00 24.11 ? 464 ASP A N   1 
ATOM   2336 C CA  . ASP A 1 464 ? 2.985   1.552   20.507  1.00 24.75 ? 464 ASP A CA  1 
ATOM   2337 C C   . ASP A 1 464 ? 2.203   1.281   21.813  1.00 24.75 ? 464 ASP A C   1 
ATOM   2338 O O   . ASP A 1 464 ? 1.611   2.211   22.361  1.00 25.21 ? 464 ASP A O   1 
ATOM   2339 C CB  . ASP A 1 464 ? 2.175   2.489   19.599  1.00 26.02 ? 464 ASP A CB  1 
ATOM   2340 C CG  . ASP A 1 464 ? 0.856   1.924   19.107  1.00 27.32 ? 464 ASP A CG  1 
ATOM   2341 O OD1 . ASP A 1 464 ? 0.423   0.880   19.632  1.00 26.03 ? 464 ASP A OD1 1 
ATOM   2342 O OD2 . ASP A 1 464 ? 0.249   2.535   18.202  1.00 28.30 ? 464 ASP A OD2 1 
ATOM   2343 N N   . GLU A 1 465 ? 2.139   -0.009  22.270  1.00 23.51 ? 465 GLU A N   1 
ATOM   2344 C CA  . GLU A 1 465 ? 1.466   -0.403  23.492  1.00 23.37 ? 465 GLU A CA  1 
ATOM   2345 C C   . GLU A 1 465 ? -0.033  -0.160  23.464  1.00 23.57 ? 465 GLU A C   1 
ATOM   2346 O O   . GLU A 1 465 ? -0.620  0.186   24.492  1.00 24.48 ? 465 GLU A O   1 
ATOM   2347 C CB  . GLU A 1 465 ? 2.113   0.227   24.732  1.00 24.76 ? 465 GLU A CB  1 
ATOM   2348 C CG  . GLU A 1 465 ? 3.568   -0.152  24.870  1.00 30.75 ? 465 GLU A CG  1 
ATOM   2349 C CD  . GLU A 1 465 ? 4.183   0.227   26.200  1.00 38.58 ? 465 GLU A CD  1 
ATOM   2350 O OE1 . GLU A 1 465 ? 3.798   1.275   26.765  1.00 40.71 ? 465 GLU A OE1 1 
ATOM   2351 O OE2 . GLU A 1 465 ? 5.026   -0.553  26.695  1.00 40.33 ? 465 GLU A OE2 1 
ATOM   2352 N N   . THR A 1 466 ? -0.653  -0.316  22.299  1.00 22.70 ? 466 THR A N   1 
ATOM   2353 C CA  . THR A 1 466 ? -2.106  -0.227  22.197  1.00 22.54 ? 466 THR A CA  1 
ATOM   2354 C C   . THR A 1 466 ? -2.631  -1.452  21.435  1.00 22.83 ? 466 THR A C   1 
ATOM   2355 O O   . THR A 1 466 ? -1.924  -2.025  20.603  1.00 23.40 ? 466 THR A O   1 
ATOM   2356 C CB  . THR A 1 466 ? -2.568  1.044   21.445  1.00 23.34 ? 466 THR A CB  1 
ATOM   2357 O OG1 . THR A 1 466 ? -2.205  0.952   20.050  1.00 22.96 ? 466 THR A OG1 1 
ATOM   2358 C CG2 . THR A 1 466 ? -2.089  2.338   22.095  1.00 23.77 ? 466 THR A CG2 1 
ATOM   2359 N N   . LEU A 1 467 ? -3.904  -1.768  21.643  1.00 22.52 ? 467 LEU A N   1 
ATOM   2360 C CA  . LEU A 1 467 ? -4.632  -2.758  20.883  1.00 23.55 ? 467 LEU A CA  1 
ATOM   2361 C C   . LEU A 1 467 ? -5.754  -1.946  20.271  1.00 22.96 ? 467 LEU A C   1 
ATOM   2362 O O   . LEU A 1 467 ? -6.582  -1.434  21.014  1.00 24.16 ? 467 LEU A O   1 
ATOM   2363 C CB  . LEU A 1 467 ? -5.257  -3.809  21.800  1.00 25.36 ? 467 LEU A CB  1 
ATOM   2364 C CG  . LEU A 1 467 ? -4.743  -5.202  21.651  1.00 29.67 ? 467 LEU A CG  1 
ATOM   2365 C CD1 . LEU A 1 467 ? -3.307  -5.282  22.133  1.00 30.19 ? 467 LEU A CD1 1 
ATOM   2366 C CD2 . LEU A 1 467 ? -5.650  -6.184  22.403  1.00 30.81 ? 467 LEU A CD2 1 
ATOM   2367 N N   . ARG A 1 468 ? -5.766  -1.771  18.952  1.00 20.96 ? 468 ARG A N   1 
ATOM   2368 C CA  . ARG A 1 468 ? -6.836  -1.022  18.304  1.00 21.03 ? 468 ARG A CA  1 
ATOM   2369 C C   . ARG A 1 468 ? -7.846  -1.987  17.741  1.00 20.77 ? 468 ARG A C   1 
ATOM   2370 O O   . ARG A 1 468 ? -7.467  -2.903  17.025  1.00 20.37 ? 468 ARG A O   1 
ATOM   2371 C CB  . ARG A 1 468 ? -6.288  -0.120  17.210  1.00 22.80 ? 468 ARG A CB  1 
ATOM   2372 C CG  . ARG A 1 468 ? -5.568  1.107   17.793  1.00 26.99 ? 468 ARG A CG  1 
ATOM   2373 C CD  . ARG A 1 468 ? -4.886  1.912   16.702  1.00 32.59 ? 468 ARG A CD  1 
ATOM   2374 N NE  . ARG A 1 468 ? -4.829  3.344   16.999  1.00 40.31 ? 468 ARG A NE  1 
ATOM   2375 C CZ  . ARG A 1 468 ? -3.927  3.923   17.783  1.00 43.91 ? 468 ARG A CZ  1 
ATOM   2376 N NH1 . ARG A 1 468 ? -3.949  5.232   17.972  1.00 44.63 ? 468 ARG A NH1 1 
ATOM   2377 N NH2 . ARG A 1 468 ? -3.001  3.193   18.392  1.00 43.77 ? 468 ARG A NH2 1 
ATOM   2378 N N   . LEU A 1 469 ? -9.135  -1.789  18.049  1.00 19.79 ? 469 LEU A N   1 
ATOM   2379 C CA  . LEU A 1 469 ? -10.176 -2.695  17.556  1.00 19.49 ? 469 LEU A CA  1 
ATOM   2380 C C   . LEU A 1 469 ? -10.973 -2.031  16.462  1.00 19.67 ? 469 LEU A C   1 
ATOM   2381 O O   . LEU A 1 469 ? -11.732 -1.098  16.734  1.00 21.18 ? 469 LEU A O   1 
ATOM   2382 C CB  . LEU A 1 469 ? -11.086 -3.087  18.710  1.00 19.95 ? 469 LEU A CB  1 
ATOM   2383 C CG  . LEU A 1 469 ? -10.683 -4.316  19.534  1.00 22.15 ? 469 LEU A CG  1 
ATOM   2384 C CD1 . LEU A 1 469 ? -9.272  -4.233  20.078  1.00 22.85 ? 469 LEU A CD1 1 
ATOM   2385 C CD2 . LEU A 1 469 ? -11.642 -4.489  20.683  1.00 22.27 ? 469 LEU A CD2 1 
ATOM   2386 N N   . TRP A 1 470 ? -10.802 -2.491  15.224  1.00 17.45 ? 470 TRP A N   1 
ATOM   2387 C CA  . TRP A 1 470 ? -11.405 -1.872  14.057  1.00 17.29 ? 470 TRP A CA  1 
ATOM   2388 C C   . TRP A 1 470 ? -12.650 -2.615  13.614  1.00 18.24 ? 470 TRP A C   1 
ATOM   2389 O O   . TRP A 1 470 ? -12.537 -3.772  13.203  1.00 17.15 ? 470 TRP A O   1 
ATOM   2390 C CB  . TRP A 1 470 ? -10.390 -1.885  12.916  1.00 17.28 ? 470 TRP A CB  1 
ATOM   2391 C CG  . TRP A 1 470 ? -9.005  -1.395  13.262  1.00 17.53 ? 470 TRP A CG  1 
ATOM   2392 C CD1 . TRP A 1 470 ? -7.959  -2.140  13.737  1.00 18.29 ? 470 TRP A CD1 1 
ATOM   2393 C CD2 . TRP A 1 470 ? -8.503  -0.059  13.084  1.00 17.80 ? 470 TRP A CD2 1 
ATOM   2394 N NE1 . TRP A 1 470 ? -6.848  -1.338  13.906  1.00 19.44 ? 470 TRP A NE1 1 
ATOM   2395 C CE2 . TRP A 1 470 ? -7.144  -0.067  13.462  1.00 19.25 ? 470 TRP A CE2 1 
ATOM   2396 C CE3 . TRP A 1 470 ? -9.060  1.132   12.593  1.00 18.43 ? 470 TRP A CE3 1 
ATOM   2397 C CZ2 . TRP A 1 470 ? -6.343  1.079   13.388  1.00 20.08 ? 470 TRP A CZ2 1 
ATOM   2398 C CZ3 . TRP A 1 470 ? -8.272  2.272   12.538  1.00 19.85 ? 470 TRP A CZ3 1 
ATOM   2399 C CH2 . TRP A 1 470 ? -6.940  2.245   12.962  1.00 20.28 ? 470 TRP A CH2 1 
ATOM   2400 N N   . ARG A 1 471 ? -13.822 -1.970  13.633  1.00 19.46 ? 471 ARG A N   1 
ATOM   2401 C CA  . ARG A 1 471 ? -15.045 -2.618  13.145  1.00 21.04 ? 471 ARG A CA  1 
ATOM   2402 C C   . ARG A 1 471 ? -15.094 -2.361  11.613  1.00 22.13 ? 471 ARG A C   1 
ATOM   2403 O O   . ARG A 1 471 ? -15.979 -1.669  11.095  1.00 23.21 ? 471 ARG A O   1 
ATOM   2404 C CB  . ARG A 1 471 ? -16.272 -2.082  13.889  1.00 23.22 ? 471 ARG A CB  1 
ATOM   2405 C CG  . ARG A 1 471 ? -17.542 -2.909  13.717  1.00 28.76 ? 471 ARG A CG  1 
ATOM   2406 C CD  . ARG A 1 471 ? -18.576 -2.589  14.803  1.00 33.48 ? 471 ARG A CD  1 
ATOM   2407 N NE  . ARG A 1 471 ? -19.699 -3.525  14.756  1.00 37.48 ? 471 ARG A NE  1 
ATOM   2408 C CZ  . ARG A 1 471 ? -19.715 -4.713  15.357  1.00 39.92 ? 471 ARG A CZ  1 
ATOM   2409 N NH1 . ARG A 1 471 ? -18.689 -5.104  16.100  1.00 38.74 ? 471 ARG A NH1 1 
ATOM   2410 N NH2 . ARG A 1 471 ? -20.767 -5.509  15.232  1.00 41.42 ? 471 ARG A NH2 1 
ATOM   2411 N N   . CYS A 1 472 ? -14.076 -2.875  10.904  1.00 21.60 ? 472 CYS A N   1 
ATOM   2412 C CA  . CYS A 1 472 ? -13.893 -2.648  9.475   1.00 22.84 ? 472 CYS A CA  1 
ATOM   2413 C C   . CYS A 1 472 ? -14.687 -3.595  8.576   1.00 24.12 ? 472 CYS A C   1 
ATOM   2414 O O   . CYS A 1 472 ? -14.695 -3.390  7.355   1.00 25.06 ? 472 CYS A O   1 
ATOM   2415 C CB  . CYS A 1 472 ? -12.412 -2.667  9.121   1.00 22.86 ? 472 CYS A CB  1 
ATOM   2416 S SG  . CYS A 1 472 ? -11.565 -4.194  9.599   1.00 23.02 ? 472 CYS A SG  1 
ATOM   2417 N N   . PHE A 1 473 ? -15.327 -4.628  9.146   1.00 23.32 ? 473 PHE A N   1 
ATOM   2418 C CA  . PHE A 1 473 ? -16.167 -5.527  8.366   1.00 24.17 ? 473 PHE A CA  1 
ATOM   2419 C C   . PHE A 1 473 ? -17.636 -5.500  8.855   1.00 28.84 ? 473 PHE A C   1 
ATOM   2420 O O   . PHE A 1 473 ? -18.243 -6.557  8.981   1.00 30.27 ? 473 PHE A O   1 
ATOM   2421 C CB  . PHE A 1 473 ? -15.611 -6.956  8.351   1.00 21.97 ? 473 PHE A CB  1 
ATOM   2422 C CG  . PHE A 1 473 ? -14.225 -7.051  7.777   1.00 20.82 ? 473 PHE A CG  1 
ATOM   2423 C CD1 . PHE A 1 473 ? -13.973 -6.678  6.467   1.00 20.44 ? 473 PHE A CD1 1 
ATOM   2424 C CD2 . PHE A 1 473 ? -13.165 -7.487  8.554   1.00 20.88 ? 473 PHE A CD2 1 
ATOM   2425 C CE1 . PHE A 1 473 ? -12.687 -6.754  5.942   1.00 20.77 ? 473 PHE A CE1 1 
ATOM   2426 C CE2 . PHE A 1 473 ? -11.885 -7.554  8.031   1.00 21.04 ? 473 PHE A CE2 1 
ATOM   2427 C CZ  . PHE A 1 473 ? -11.648 -7.184  6.729   1.00 20.46 ? 473 PHE A CZ  1 
ATOM   2428 N N   . GLU A 1 474 ? -18.205 -4.305  9.112   1.00 31.40 ? 474 GLU A N   1 
ATOM   2429 C CA  . GLU A 1 474 ? -19.619 -4.137  9.504   1.00 35.16 ? 474 GLU A CA  1 
ATOM   2430 C C   . GLU A 1 474 ? -20.044 -2.670  9.534   1.00 39.48 ? 474 GLU A C   1 
ATOM   2431 O O   . GLU A 1 474 ? -19.204 -1.780  9.665   1.00 40.17 ? 474 GLU A O   1 
ATOM   2432 C CB  . GLU A 1 474 ? -19.967 -4.801  10.860  1.00 38.36 ? 474 GLU A CB  1 
ATOM   2433 C CG  . GLU A 1 474 ? -20.775 -6.084  10.738  1.00 44.32 ? 474 GLU A CG  1 
ATOM   2434 C CD  . GLU A 1 474 ? -22.281 -5.962  10.600  1.00 51.38 ? 474 GLU A CD  1 
ATOM   2435 O OE1 . GLU A 1 474 ? -22.983 -6.922  10.993  1.00 54.95 ? 474 GLU A OE1 1 
ATOM   2436 O OE2 . GLU A 1 474 ? -22.766 -4.916  10.113  1.00 51.09 ? 474 GLU A OE2 1 
ATOM   2437 N N   . LEU A 1 475 ? -21.364 -2.435  9.428   1.00 41.76 ? 475 LEU A N   1 
ATOM   2438 C CA  . LEU A 1 475 ? -22.026 -1.137  9.504   1.00 44.77 ? 475 LEU A CA  1 
ATOM   2439 C C   . LEU A 1 475 ? -23.137 -1.157  10.597  1.00 47.01 ? 475 LEU A C   1 
ATOM   2440 O O   . LEU A 1 475 ? -23.506 -0.094  11.106  1.00 47.76 ? 475 LEU A O   1 
ATOM   2441 C CB  . LEU A 1 475 ? -22.625 -0.757  8.141   1.00 45.50 ? 475 LEU A CB  1 
ATOM   2442 C CG  . LEU A 1 475 ? -21.612 -0.452  7.036   1.00 47.83 ? 475 LEU A CG  1 
ATOM   2443 C CD1 . LEU A 1 475 ? -22.308 -0.244  5.699   1.00 48.37 ? 475 LEU A CD1 1 
ATOM   2444 C CD2 . LEU A 1 475 ? -20.791 0.780   7.378   1.00 49.05 ? 475 LEU A CD2 1 
ATOM   2445 N N   . ASP A 1 476 ? -23.658 -2.358  10.953  1.00 47.69 ? 476 ASP A N   1 
ATOM   2446 C CA  . ASP A 1 476 ? -24.706 -2.570  11.960  1.00 48.77 ? 476 ASP A CA  1 
ATOM   2447 C C   . ASP A 1 476 ? -26.040 -1.896  11.591  1.00 48.84 ? 476 ASP A C   1 
ATOM   2448 O O   . ASP A 1 476 ? -26.576 -2.110  10.500  1.00 48.35 ? 476 ASP A O   1 
ATOM   2449 C CB  . ASP A 1 476 ? -24.239 -2.140  13.365  1.00 51.35 ? 476 ASP A CB  1 
ATOM   2450 C CG  . ASP A 1 476 ? -22.936 -2.766  13.807  1.00 58.01 ? 476 ASP A CG  1 
ATOM   2451 O OD1 . ASP A 1 476 ? -21.897 -2.065  13.776  1.00 58.87 ? 476 ASP A OD1 1 
ATOM   2452 O OD2 . ASP A 1 476 ? -22.950 -3.953  14.191  1.00 61.64 ? 476 ASP A OD2 1 
ATOM   2453 N N   . ARG B 2 1   ? -1.589  3.419   34.151  1.00 41.76 ? 1   ARG B N   1 
ATOM   2454 C CA  . ARG B 2 1   ? -1.681  2.468   33.042  1.00 41.66 ? 1   ARG B CA  1 
ATOM   2455 C C   . ARG B 2 1   ? -2.275  1.152   33.528  1.00 40.79 ? 1   ARG B C   1 
ATOM   2456 O O   . ARG B 2 1   ? -1.582  0.373   34.184  1.00 41.69 ? 1   ARG B O   1 
ATOM   2457 C CB  . ARG B 2 1   ? -0.292  2.184   32.440  1.00 43.34 ? 1   ARG B CB  1 
ATOM   2458 C CG  . ARG B 2 1   ? 0.517   3.423   32.083  1.00 46.49 ? 1   ARG B CG  1 
ATOM   2459 C CD  . ARG B 2 1   ? 0.152   4.052   30.744  1.00 49.94 ? 1   ARG B CD  1 
ATOM   2460 N NE  . ARG B 2 1   ? 0.149   3.111   29.617  1.00 53.19 ? 1   ARG B NE  1 
ATOM   2461 C CZ  . ARG B 2 1   ? 1.238   2.677   28.985  1.00 55.15 ? 1   ARG B CZ  1 
ATOM   2462 N NH1 . ARG B 2 1   ? 1.129   1.844   27.959  1.00 53.94 ? 1   ARG B NH1 1 
ATOM   2463 N NH2 . ARG B 2 1   ? 2.443   3.059   29.386  1.00 55.31 ? 1   ARG B NH2 1 
ATOM   2464 N N   . ALA B 2 2   ? -3.544  0.895   33.206  1.00 38.46 ? 2   ALA B N   1 
ATOM   2465 C CA  . ALA B 2 2   ? -4.188  -0.356  33.581  1.00 36.51 ? 2   ALA B CA  1 
ATOM   2466 C C   . ALA B 2 2   ? -4.245  -1.238  32.319  1.00 34.33 ? 2   ALA B C   1 
ATOM   2467 O O   . ALA B 2 2   ? -4.667  -0.773  31.254  1.00 34.29 ? 2   ALA B O   1 
ATOM   2468 C CB  . ALA B 2 2   ? -5.594  -0.082  34.092  1.00 36.50 ? 2   ALA B CB  1 
ATOM   2469 N N   . PRO B 2 3   ? -3.795  -2.496  32.409  1.00 31.96 ? 3   PRO B N   1 
ATOM   2470 C CA  . PRO B 2 3   ? -3.812  -3.364  31.223  1.00 30.20 ? 3   PRO B CA  1 
ATOM   2471 C C   . PRO B 2 3   ? -5.217  -3.581  30.666  1.00 28.49 ? 3   PRO B C   1 
ATOM   2472 O O   . PRO B 2 3   ? -6.168  -3.800  31.419  1.00 27.35 ? 3   PRO B O   1 
ATOM   2473 C CB  . PRO B 2 3   ? -3.207  -4.665  31.735  1.00 31.09 ? 3   PRO B CB  1 
ATOM   2474 C CG  . PRO B 2 3   ? -2.407  -4.259  32.941  1.00 32.07 ? 3   PRO B CG  1 
ATOM   2475 C CD  . PRO B 2 3   ? -3.227  -3.193  33.576  1.00 30.72 ? 3   PRO B CD  1 
HETATM 2476 C C   . 3EG B 2 4   ? -7.679  -2.566  28.886  1.00 28.82 ? 4   3EG B C   1 
HETATM 2477 N N   . 3EG B 2 4   ? -5.349  -3.433  29.335  1.00 27.29 ? 4   3EG B N   1 
HETATM 2478 O O   . 3EG B 2 4   ? -8.809  -2.732  28.440  1.00 27.96 ? 4   3EG B O   1 
HETATM 2479 C CA  . 3EG B 2 4   ? -6.599  -3.609  28.606  1.00 27.54 ? 4   3EG B CA  1 
HETATM 2480 C CB  . 3EG B 2 4   ? -7.171  -5.036  28.743  1.00 27.46 ? 4   3EG B CB  1 
HETATM 2481 F FAC . 3EG B 2 4   ? -5.086  -6.090  28.642  1.00 28.06 ? 4   3EG B FAC 1 
HETATM 2482 F FAD . 3EG B 2 4   ? -6.769  -7.266  28.126  1.00 27.92 ? 4   3EG B FAD 1 
HETATM 2483 F FAE . 3EG B 2 4   ? -6.060  -5.749  26.796  1.00 28.49 ? 4   3EG B FAE 1 
HETATM 2484 C CG  . 3EG B 2 4   ? -6.277  -6.031  28.083  1.00 27.97 ? 4   3EG B CG  1 
ATOM   2485 N N   . SER B 2 5   ? -7.337  -1.489  29.596  1.00 30.81 ? 5   SER B N   1 
ATOM   2486 C CA  . SER B 2 5   ? -8.314  -0.439  29.884  1.00 33.13 ? 5   SER B CA  1 
ATOM   2487 C C   . SER B 2 5   ? -8.479  0.512   28.690  1.00 35.18 ? 5   SER B C   1 
ATOM   2488 O O   . SER B 2 5   ? -7.557  0.679   27.892  1.00 34.65 ? 5   SER B O   1 
ATOM   2489 C CB  . SER B 2 5   ? -7.894  0.358   31.116  1.00 35.10 ? 5   SER B CB  1 
ATOM   2490 O OG  . SER B 2 5   ? -6.601  0.915   30.930  1.00 39.07 ? 5   SER B OG  1 
ATOM   2491 N N   . ASP B 2 6   ? -9.654  1.152   28.591  1.00 37.43 ? 6   ASP B N   1 
ATOM   2492 C CA  . ASP B 2 6   ? -9.951  2.154   27.566  1.00 40.08 ? 6   ASP B CA  1 
ATOM   2493 C C   . ASP B 2 6   ? -9.394  3.499   28.029  1.00 41.09 ? 6   ASP B C   1 
ATOM   2494 O O   . ASP B 2 6   ? -8.273  3.570   28.536  1.00 41.68 ? 6   ASP B O   1 
ATOM   2495 C CB  . ASP B 2 6   ? -11.462 2.310   27.386  1.00 43.61 ? 6   ASP B CB  1 
ATOM   2496 C CG  . ASP B 2 6   ? -12.136 1.105   26.780  1.00 50.89 ? 6   ASP B CG  1 
ATOM   2497 O OD1 . ASP B 2 6   ? -11.897 0.834   25.582  1.00 52.65 ? 6   ASP B OD1 1 
ATOM   2498 O OD2 . ASP B 2 6   ? -12.928 0.451   27.489  1.00 53.13 ? 6   ASP B OD2 1 
HETATM 2499 O O   . HOH C 3 .   ? 1.806   -9.223  -8.579  1.00 40.50 ? 501 HOH A O   1 
HETATM 2500 O O   . HOH C 3 .   ? -8.834  -18.300 -4.801  1.00 28.90 ? 502 HOH A O   1 
HETATM 2501 O O   . HOH C 3 .   ? -16.478 2.951   19.500  1.00 39.89 ? 503 HOH A O   1 
HETATM 2502 O O   . HOH C 3 .   ? -18.946 -8.812  8.348   1.00 36.05 ? 504 HOH A O   1 
HETATM 2503 O O   . HOH C 3 .   ? -15.879 -10.623 8.218   1.00 26.63 ? 505 HOH A O   1 
HETATM 2504 O O   . HOH C 3 .   ? 17.309  -26.307 16.049  1.00 41.12 ? 506 HOH A O   1 
HETATM 2505 O O   . HOH C 3 .   ? -7.396  6.063   13.106  1.00 31.80 ? 507 HOH A O   1 
HETATM 2506 O O   . HOH C 3 .   ? -0.097  -13.309 15.698  1.00 28.32 ? 508 HOH A O   1 
HETATM 2507 O O   . HOH C 3 .   ? 10.231  -27.880 27.058  1.00 32.74 ? 509 HOH A O   1 
HETATM 2508 O O   . HOH C 3 .   ? 19.848  -23.417 12.196  1.00 47.54 ? 510 HOH A O   1 
HETATM 2509 O O   . HOH C 3 .   ? -11.522 -28.469 32.573  1.00 35.53 ? 511 HOH A O   1 
HETATM 2510 O O   . HOH C 3 .   ? 12.201  -22.325 39.357  1.00 44.20 ? 512 HOH A O   1 
HETATM 2511 O O   . HOH C 3 .   ? 12.744  -4.850  1.530   1.00 47.72 ? 513 HOH A O   1 
HETATM 2512 O O   . HOH C 3 .   ? -1.265  -13.681 18.025  1.00 23.98 ? 514 HOH A O   1 
HETATM 2513 O O   . HOH C 3 .   ? 6.341   -2.314  25.176  1.00 33.24 ? 515 HOH A O   1 
HETATM 2514 O O   . HOH C 3 .   ? -8.791  -18.027 7.958   1.00 22.22 ? 516 HOH A O   1 
HETATM 2515 O O   . HOH C 3 .   ? 2.112   -10.494 18.849  1.00 22.07 ? 517 HOH A O   1 
HETATM 2516 O O   . HOH C 3 .   ? 7.132   -1.147  22.433  1.00 38.18 ? 518 HOH A O   1 
HETATM 2517 O O   . HOH C 3 .   ? 17.346  -16.795 9.075   1.00 42.98 ? 519 HOH A O   1 
HETATM 2518 O O   . HOH C 3 .   ? -17.904 -10.790 31.203  1.00 50.18 ? 520 HOH A O   1 
HETATM 2519 O O   . HOH C 3 .   ? 4.869   4.726   19.302  1.00 34.94 ? 521 HOH A O   1 
HETATM 2520 O O   . HOH C 3 .   ? 13.252  -18.726 1.013   1.00 29.91 ? 522 HOH A O   1 
HETATM 2521 O O   . HOH C 3 .   ? 14.544  -14.601 24.830  1.00 41.45 ? 523 HOH A O   1 
HETATM 2522 O O   . HOH C 3 .   ? -18.450 -0.071  11.553  1.00 40.13 ? 524 HOH A O   1 
HETATM 2523 O O   . HOH C 3 .   ? -13.978 -17.698 25.534  1.00 26.59 ? 525 HOH A O   1 
HETATM 2524 O O   . HOH C 3 .   ? 3.806   0.583   6.118   1.00 27.94 ? 526 HOH A O   1 
HETATM 2525 O O   . HOH C 3 .   ? -6.393  5.112   15.770  1.00 31.25 ? 527 HOH A O   1 
HETATM 2526 O O   . HOH C 3 .   ? 2.176   -7.401  32.464  1.00 39.32 ? 528 HOH A O   1 
HETATM 2527 O O   . HOH C 3 .   ? 1.343   -15.580 12.960  1.00 18.72 ? 529 HOH A O   1 
HETATM 2528 O O   . HOH C 3 .   ? -16.583 -2.748  21.253  1.00 60.60 ? 530 HOH A O   1 
HETATM 2529 O O   . HOH C 3 .   ? 0.374   -13.293 12.140  1.00 22.55 ? 531 HOH A O   1 
HETATM 2530 O O   . HOH C 3 .   ? -19.592 -10.149 0.270   1.00 39.69 ? 532 HOH A O   1 
HETATM 2531 O O   . HOH C 3 .   ? -1.644  -16.934 18.270  1.00 22.88 ? 533 HOH A O   1 
HETATM 2532 O O   . HOH C 3 .   ? 12.412  -10.764 22.944  1.00 40.13 ? 534 HOH A O   1 
HETATM 2533 O O   . HOH C 3 .   ? 8.770   -35.097 24.289  1.00 33.63 ? 535 HOH A O   1 
HETATM 2534 O O   . HOH C 3 .   ? 4.462   -5.214  11.041  1.00 35.78 ? 536 HOH A O   1 
HETATM 2535 O O   . HOH C 3 .   ? 6.685   -27.363 -2.857  1.00 30.53 ? 537 HOH A O   1 
HETATM 2536 O O   . HOH C 3 .   ? 6.088   -11.851 8.092   1.00 23.59 ? 538 HOH A O   1 
HETATM 2537 O O   . HOH C 3 .   ? 12.087  -27.541 20.256  1.00 24.62 ? 539 HOH A O   1 
HETATM 2538 O O   . HOH C 3 .   ? 15.591  -23.850 6.479   1.00 31.50 ? 540 HOH A O   1 
HETATM 2539 O O   . HOH C 3 .   ? -15.107 -33.545 23.974  1.00 62.50 ? 541 HOH A O   1 
HETATM 2540 O O   . HOH C 3 .   ? 9.410   -27.543 11.632  1.00 21.26 ? 542 HOH A O   1 
HETATM 2541 O O   . HOH C 3 .   ? -2.239  -13.036 13.562  1.00 39.34 ? 543 HOH A O   1 
HETATM 2542 O O   . HOH C 3 .   ? 4.821   -9.660  19.038  1.00 35.01 ? 544 HOH A O   1 
HETATM 2543 O O   . HOH C 3 .   ? 12.573  -17.949 30.219  1.00 30.30 ? 545 HOH A O   1 
HETATM 2544 O O   . HOH C 3 .   ? -6.959  -33.143 10.820  1.00 31.00 ? 546 HOH A O   1 
HETATM 2545 O O   . HOH C 3 .   ? -21.857 -10.112 28.556  1.00 57.39 ? 547 HOH A O   1 
HETATM 2546 O O   . HOH C 3 .   ? 9.053   -18.619 1.310   1.00 21.04 ? 548 HOH A O   1 
HETATM 2547 O O   . HOH C 3 .   ? 16.121  -28.807 19.487  1.00 42.21 ? 549 HOH A O   1 
HETATM 2548 O O   . HOH C 3 .   ? -3.036  -19.940 15.433  1.00 28.53 ? 550 HOH A O   1 
HETATM 2549 O O   . HOH C 3 .   ? -24.508 -8.291  9.246   1.00 33.70 ? 551 HOH A O   1 
HETATM 2550 O O   . HOH C 3 .   ? 5.265   -11.281 26.303  1.00 21.11 ? 552 HOH A O   1 
HETATM 2551 O O   . HOH C 3 .   ? -11.924 -20.003 20.141  1.00 20.02 ? 553 HOH A O   1 
HETATM 2552 O O   . HOH C 3 .   ? 8.006   -12.509 -2.306  1.00 23.65 ? 554 HOH A O   1 
HETATM 2553 O O   . HOH C 3 .   ? 12.908  -34.317 14.192  1.00 52.31 ? 555 HOH A O   1 
HETATM 2554 O O   . HOH C 3 .   ? 18.974  -21.284 8.323   1.00 29.89 ? 556 HOH A O   1 
HETATM 2555 O O   . HOH C 3 .   ? -3.842  -15.000 10.659  1.00 21.94 ? 557 HOH A O   1 
HETATM 2556 O O   . HOH C 3 .   ? -22.975 -9.456  11.944  1.00 49.52 ? 558 HOH A O   1 
HETATM 2557 O O   . HOH C 3 .   ? 7.181   -34.449 26.477  1.00 40.04 ? 559 HOH A O   1 
HETATM 2558 O O   . HOH C 3 .   ? -0.525  4.595   11.330  1.00 24.60 ? 560 HOH A O   1 
HETATM 2559 O O   . HOH C 3 .   ? -9.193  4.800   6.634   1.00 36.41 ? 561 HOH A O   1 
HETATM 2560 O O   . HOH C 3 .   ? 9.653   -34.047 10.088  1.00 33.99 ? 562 HOH A O   1 
HETATM 2561 O O   . HOH C 3 .   ? -9.713  -26.704 18.772  1.00 20.49 ? 563 HOH A O   1 
HETATM 2562 O O   . HOH C 3 .   ? -3.435  -38.300 19.507  1.00 43.62 ? 564 HOH A O   1 
HETATM 2563 O O   . HOH C 3 .   ? 3.307   -38.330 5.032   1.00 67.73 ? 565 HOH A O   1 
HETATM 2564 O O   . HOH C 3 .   ? 13.946  -15.468 15.868  1.00 50.40 ? 566 HOH A O   1 
HETATM 2565 O O   . HOH C 3 .   ? 6.327   1.754   3.571   1.00 39.23 ? 567 HOH A O   1 
HETATM 2566 O O   . HOH C 3 .   ? -14.504 7.338   8.740   1.00 47.97 ? 568 HOH A O   1 
HETATM 2567 O O   . HOH C 3 .   ? -11.023 -23.139 40.028  1.00 24.20 ? 569 HOH A O   1 
HETATM 2568 O O   . HOH C 3 .   ? -17.293 -1.555  7.735   1.00 45.07 ? 570 HOH A O   1 
HETATM 2569 O O   . HOH C 3 .   ? 3.183   -0.100  3.277   1.00 35.99 ? 571 HOH A O   1 
HETATM 2570 O O   . HOH C 3 .   ? 7.790   -6.167  27.638  1.00 36.78 ? 572 HOH A O   1 
HETATM 2571 O O   . HOH C 3 .   ? -16.455 -6.038  -0.650  1.00 52.06 ? 573 HOH A O   1 
HETATM 2572 O O   . HOH C 3 .   ? -7.086  -20.099 18.224  1.00 26.54 ? 574 HOH A O   1 
HETATM 2573 O O   . HOH C 3 .   ? -3.900  -24.180 -9.299  1.00 42.20 ? 575 HOH A O   1 
HETATM 2574 O O   . HOH C 3 .   ? 13.392  -30.852 22.673  1.00 43.13 ? 576 HOH A O   1 
HETATM 2575 O O   . HOH C 3 .   ? 8.731   -32.145 0.855   1.00 51.44 ? 577 HOH A O   1 
HETATM 2576 O O   . HOH C 3 .   ? -12.297 -34.007 16.499  1.00 44.48 ? 578 HOH A O   1 
HETATM 2577 O O   . HOH C 3 .   ? 15.853  -21.479 4.076   1.00 40.64 ? 579 HOH A O   1 
HETATM 2578 O O   . HOH C 3 .   ? 12.512  -19.445 -4.505  1.00 30.34 ? 580 HOH A O   1 
HETATM 2579 O O   . HOH C 3 .   ? 3.988   -9.133  25.600  1.00 18.45 ? 581 HOH A O   1 
HETATM 2580 O O   . HOH C 3 .   ? 7.592   1.599   12.176  1.00 30.58 ? 582 HOH A O   1 
HETATM 2581 O O   . HOH C 3 .   ? 16.346  -11.635 -1.903  1.00 52.96 ? 583 HOH A O   1 
HETATM 2582 O O   . HOH C 3 .   ? -4.866  -21.278 14.394  1.00 27.27 ? 584 HOH A O   1 
HETATM 2583 O O   . HOH C 3 .   ? 11.274  -14.764 -4.893  1.00 51.79 ? 585 HOH A O   1 
HETATM 2584 O O   . HOH C 3 .   ? 13.667  -21.850 26.496  1.00 34.57 ? 586 HOH A O   1 
HETATM 2585 O O   . HOH C 3 .   ? -13.118 -27.472 24.290  1.00 34.43 ? 587 HOH A O   1 
HETATM 2586 O O   . HOH C 3 .   ? -12.537 -11.183 31.142  1.00 29.44 ? 588 HOH A O   1 
HETATM 2587 O O   . HOH C 3 .   ? -17.274 -7.686  16.432  1.00 36.77 ? 589 HOH A O   1 
HETATM 2588 O O   . HOH C 3 .   ? 5.282   -32.696 29.680  1.00 29.44 ? 590 HOH A O   1 
HETATM 2589 O O   . HOH C 3 .   ? 8.501   -13.351 34.761  1.00 22.24 ? 591 HOH A O   1 
HETATM 2590 O O   . HOH C 3 .   ? 9.736   -11.091 31.669  1.00 47.41 ? 592 HOH A O   1 
HETATM 2591 O O   . HOH C 3 .   ? -6.917  -27.402 3.721   1.00 22.41 ? 593 HOH A O   1 
HETATM 2592 O O   . HOH C 3 .   ? -2.651  1.702   12.117  1.00 22.02 ? 594 HOH A O   1 
HETATM 2593 O O   . HOH C 3 .   ? -7.247  -21.344 9.899   1.00 25.54 ? 595 HOH A O   1 
HETATM 2594 O O   . HOH C 3 .   ? 0.396   -1.525  -1.412  1.00 54.55 ? 596 HOH A O   1 
HETATM 2595 O O   . HOH C 3 .   ? -2.956  -49.431 6.429   1.00 29.90 ? 597 HOH A O   1 
HETATM 2596 O O   . HOH C 3 .   ? -14.260 -21.880 6.942   1.00 32.46 ? 598 HOH A O   1 
HETATM 2597 O O   . HOH C 3 .   ? 9.869   -35.955 12.018  1.00 48.77 ? 599 HOH A O   1 
HETATM 2598 O O   . HOH C 3 .   ? 11.142  -27.966 4.680   1.00 31.64 ? 600 HOH A O   1 
HETATM 2599 O O   . HOH C 3 .   ? -17.707 -3.466  25.636  1.00 54.01 ? 601 HOH A O   1 
HETATM 2600 O O   . HOH C 3 .   ? -7.602  5.329   9.316   1.00 27.56 ? 602 HOH A O   1 
HETATM 2601 O O   . HOH C 3 .   ? 6.621   -8.099  -7.168  1.00 50.76 ? 603 HOH A O   1 
HETATM 2602 O O   . HOH C 3 .   ? -9.081  -16.398 16.674  1.00 57.18 ? 604 HOH A O   1 
HETATM 2603 O O   . HOH C 3 .   ? 17.359  -29.130 16.918  1.00 49.25 ? 605 HOH A O   1 
HETATM 2604 O O   . HOH C 3 .   ? -13.014 -28.824 39.360  1.00 45.15 ? 606 HOH A O   1 
HETATM 2605 O O   . HOH C 3 .   ? -8.775  -23.160 3.724   1.00 27.72 ? 607 HOH A O   1 
HETATM 2606 O O   . HOH C 3 .   ? -12.592 -15.217 16.975  1.00 27.22 ? 608 HOH A O   1 
HETATM 2607 O O   . HOH C 3 .   ? -14.298 -25.863 33.174  1.00 34.95 ? 609 HOH A O   1 
HETATM 2608 O O   . HOH C 3 .   ? 7.118   -27.587 24.941  1.00 28.06 ? 610 HOH A O   1 
HETATM 2609 O O   . HOH C 3 .   ? 3.626   -35.699 3.079   1.00 44.88 ? 611 HOH A O   1 
HETATM 2610 O O   . HOH C 3 .   ? -13.696 -17.573 35.004  1.00 35.40 ? 612 HOH A O   1 
HETATM 2611 O O   . HOH C 3 .   ? 12.411  -6.969  13.967  1.00 51.03 ? 613 HOH A O   1 
HETATM 2612 O O   . HOH C 3 .   ? -8.415  -15.410 8.396   1.00 21.30 ? 614 HOH A O   1 
HETATM 2613 O O   . HOH C 3 .   ? -16.518 -4.130  17.867  1.00 55.19 ? 615 HOH A O   1 
HETATM 2614 O O   . HOH C 3 .   ? -3.305  -17.619 37.867  1.00 25.25 ? 616 HOH A O   1 
HETATM 2615 O O   . HOH C 3 .   ? 0.292   -31.651 10.715  1.00 26.99 ? 617 HOH A O   1 
HETATM 2616 O O   . HOH C 3 .   ? -6.802  3.336   25.768  1.00 45.16 ? 618 HOH A O   1 
HETATM 2617 O O   . HOH C 3 .   ? 4.411   -14.649 39.601  1.00 46.36 ? 619 HOH A O   1 
HETATM 2618 O O   . HOH C 3 .   ? 9.840   -1.151  16.757  1.00 37.15 ? 620 HOH A O   1 
HETATM 2619 O O   . HOH C 3 .   ? -10.067 -26.617 15.992  1.00 26.44 ? 621 HOH A O   1 
HETATM 2620 O O   . HOH C 3 .   ? -8.709  -36.455 28.807  1.00 30.38 ? 622 HOH A O   1 
HETATM 2621 O O   . HOH C 3 .   ? -7.548  -9.846  37.624  1.00 33.63 ? 623 HOH A O   1 
HETATM 2622 O O   . HOH C 3 .   ? -5.390  7.659   18.447  1.00 45.46 ? 624 HOH A O   1 
HETATM 2623 O O   . HOH C 3 .   ? -14.093 0.919   13.628  1.00 26.43 ? 625 HOH A O   1 
HETATM 2624 O O   . HOH C 3 .   ? -12.612 0.464   10.926  1.00 32.04 ? 626 HOH A O   1 
HETATM 2625 O O   . HOH C 3 .   ? -9.105  -22.304 17.642  1.00 34.33 ? 627 HOH A O   1 
HETATM 2626 O O   . HOH C 3 .   ? 9.571   -4.772  24.063  1.00 31.63 ? 628 HOH A O   1 
HETATM 2627 O O   . HOH C 3 .   ? -22.989 -6.437  27.880  1.00 59.54 ? 629 HOH A O   1 
HETATM 2628 O O   . HOH C 3 .   ? -6.216  -19.219 8.914   1.00 17.40 ? 630 HOH A O   1 
HETATM 2629 O O   . HOH C 3 .   ? 1.488   -4.809  31.694  1.00 30.45 ? 631 HOH A O   1 
HETATM 2630 O O   . HOH C 3 .   ? -13.095 -11.197 35.976  1.00 56.69 ? 632 HOH A O   1 
HETATM 2631 O O   . HOH C 3 .   ? 8.662   -19.995 18.006  1.00 18.80 ? 633 HOH A O   1 
HETATM 2632 O O   . HOH C 3 .   ? 12.171  -31.699 18.995  1.00 40.12 ? 634 HOH A O   1 
HETATM 2633 O O   . HOH C 3 .   ? 7.970   0.582   15.136  1.00 34.24 ? 635 HOH A O   1 
HETATM 2634 O O   . HOH C 3 .   ? -5.613  -21.510 39.889  1.00 37.05 ? 636 HOH A O   1 
HETATM 2635 O O   . HOH C 3 .   ? 9.584   -12.866 -6.738  1.00 46.86 ? 637 HOH A O   1 
HETATM 2636 O O   . HOH C 3 .   ? 14.649  -19.087 23.812  1.00 29.84 ? 638 HOH A O   1 
HETATM 2637 O O   . HOH C 3 .   ? 15.586  -18.158 14.465  1.00 39.21 ? 639 HOH A O   1 
HETATM 2638 O O   . HOH C 3 .   ? 3.168   5.880   12.495  1.00 32.98 ? 640 HOH A O   1 
HETATM 2639 O O   . HOH C 3 .   ? -13.421 -25.519 -0.352  1.00 45.57 ? 641 HOH A O   1 
HETATM 2640 O O   . HOH C 3 .   ? -4.427  -33.465 13.669  1.00 51.28 ? 642 HOH A O   1 
HETATM 2641 O O   . HOH C 3 .   ? -9.436  -24.860 -2.673  1.00 37.81 ? 643 HOH A O   1 
HETATM 2642 O O   . HOH C 3 .   ? 6.005   -19.915 35.617  1.00 44.11 ? 644 HOH A O   1 
HETATM 2643 O O   . HOH C 3 .   ? 12.219  -10.637 7.061   1.00 32.43 ? 645 HOH A O   1 
HETATM 2644 O O   . HOH C 3 .   ? 2.805   -33.016 -2.584  1.00 49.06 ? 646 HOH A O   1 
HETATM 2645 O O   . HOH C 3 .   ? 8.806   -2.771  7.043   1.00 36.23 ? 647 HOH A O   1 
HETATM 2646 O O   . HOH C 3 .   ? -3.442  -22.725 38.373  1.00 25.92 ? 648 HOH A O   1 
HETATM 2647 O O   . HOH C 3 .   ? 11.088  -33.708 23.726  1.00 45.11 ? 649 HOH A O   1 
HETATM 2648 O O   . HOH C 3 .   ? -8.302  4.290   3.006   1.00 38.74 ? 650 HOH A O   1 
HETATM 2649 O O   . HOH C 3 .   ? -8.539  -26.601 12.222  1.00 41.44 ? 651 HOH A O   1 
HETATM 2650 O O   . HOH C 3 .   ? 9.734   -23.012 -3.918  1.00 31.21 ? 652 HOH A O   1 
HETATM 2651 O O   . HOH C 3 .   ? 11.775  -8.485  16.640  1.00 25.96 ? 653 HOH A O   1 
HETATM 2652 O O   . HOH C 3 .   ? 2.595   -39.152 14.839  1.00 48.60 ? 654 HOH A O   1 
HETATM 2653 O O   . HOH C 3 .   ? 7.154   -22.409 37.110  1.00 44.81 ? 655 HOH A O   1 
HETATM 2654 O O   . HOH C 3 .   ? 1.065   -18.247 14.393  1.00 24.41 ? 656 HOH A O   1 
HETATM 2655 O O   . HOH C 3 .   ? -4.504  -19.843 38.800  1.00 34.87 ? 657 HOH A O   1 
HETATM 2656 O O   . HOH C 3 .   ? -10.330 -29.641 36.215  1.00 41.71 ? 658 HOH A O   1 
HETATM 2657 O O   . HOH C 3 .   ? -11.552 -9.426  37.285  1.00 57.02 ? 659 HOH A O   1 
HETATM 2658 O O   . HOH C 3 .   ? -17.527 -15.481 0.824   1.00 55.20 ? 660 HOH A O   1 
HETATM 2659 O O   . HOH C 3 .   ? 0.225   -18.493 17.035  1.00 18.70 ? 661 HOH A O   1 
HETATM 2660 O O   . HOH C 3 .   ? -8.150  -14.511 14.466  1.00 37.19 ? 662 HOH A O   1 
HETATM 2661 O O   . HOH C 3 .   ? -17.510 -11.162 25.787  1.00 28.80 ? 663 HOH A O   1 
HETATM 2662 O O   . HOH C 3 .   ? 0.726   -11.541 -8.942  1.00 35.01 ? 664 HOH A O   1 
HETATM 2663 O O   . HOH C 3 .   ? 10.867  -8.227  -2.514  1.00 49.68 ? 665 HOH A O   1 
HETATM 2664 O O   . HOH C 3 .   ? -5.688  -15.110 15.567  1.00 37.94 ? 666 HOH A O   1 
HETATM 2665 O O   . HOH C 3 .   ? -20.026 -9.863  10.498  1.00 50.34 ? 667 HOH A O   1 
HETATM 2666 O O   . HOH C 3 .   ? 1.117   -19.010 36.829  1.00 56.28 ? 668 HOH A O   1 
HETATM 2667 O O   . HOH C 3 .   ? 17.118  -19.162 4.225   1.00 61.40 ? 669 HOH A O   1 
HETATM 2668 O O   . HOH C 3 .   ? 2.119   -20.748 35.086  1.00 46.92 ? 670 HOH A O   1 
HETATM 2669 O O   . HOH C 3 .   ? -11.683 -15.773 8.933   1.00 40.90 ? 671 HOH A O   1 
HETATM 2670 O O   . HOH C 3 .   ? -12.930 -5.585  35.037  1.00 41.38 ? 672 HOH A O   1 
HETATM 2671 O O   . HOH C 3 .   ? -5.629  -21.913 16.910  1.00 22.39 ? 673 HOH A O   1 
HETATM 2672 O O   . HOH C 3 .   ? 7.177   -37.693 15.022  1.00 34.14 ? 674 HOH A O   1 
HETATM 2673 O O   . HOH C 3 .   ? -6.490  -22.172 12.650  1.00 50.54 ? 675 HOH A O   1 
HETATM 2674 O O   . HOH C 3 .   ? -16.005 3.071   22.228  1.00 38.52 ? 676 HOH A O   1 
HETATM 2675 O O   . HOH C 3 .   ? -14.713 3.953   3.041   1.00 47.58 ? 677 HOH A O   1 
HETATM 2676 O O   . HOH C 3 .   ? 13.966  -8.912  7.073   1.00 39.09 ? 678 HOH A O   1 
HETATM 2677 O O   . HOH C 3 .   ? -3.493  -34.533 4.663   1.00 53.61 ? 679 HOH A O   1 
HETATM 2678 O O   . HOH C 3 .   ? -13.993 -13.692 36.489  1.00 51.80 ? 680 HOH A O   1 
HETATM 2679 O O   . HOH C 3 .   ? -1.386  -14.195 9.972   1.00 18.54 ? 681 HOH A O   1 
HETATM 2680 O O   . HOH C 3 .   ? 6.281   -15.734 41.374  1.00 46.31 ? 682 HOH A O   1 
HETATM 2681 O O   . HOH C 3 .   ? -17.274 -15.624 11.370  1.00 45.75 ? 683 HOH A O   1 
HETATM 2682 O O   . HOH C 3 .   ? -0.633  -17.230 37.758  1.00 27.79 ? 684 HOH A O   1 
HETATM 2683 O O   . HOH C 3 .   ? -10.556 -24.891 5.085   1.00 33.44 ? 685 HOH A O   1 
HETATM 2684 O O   . HOH C 3 .   ? 8.812   -0.712  -0.973  1.00 52.66 ? 686 HOH A O   1 
HETATM 2685 O O   . HOH C 3 .   ? -18.194 -20.797 21.695  1.00 35.22 ? 687 HOH A O   1 
HETATM 2686 O O   . HOH C 3 .   ? -11.125 3.659   6.032   1.00 51.22 ? 688 HOH A O   1 
HETATM 2687 O O   . HOH C 3 .   ? -14.624 6.485   11.759  1.00 39.44 ? 689 HOH A O   1 
HETATM 2688 O O   . HOH C 3 .   ? 15.087  -16.300 0.679   1.00 39.29 ? 690 HOH A O   1 
HETATM 2689 O O   . HOH C 3 .   ? -17.153 -21.544 4.498   1.00 44.99 ? 691 HOH A O   1 
HETATM 2690 O O   . HOH C 3 .   ? -6.888  -31.898 29.461  1.00 42.32 ? 692 HOH A O   1 
HETATM 2691 O O   . HOH C 3 .   ? 5.135   -36.195 26.097  1.00 33.13 ? 693 HOH A O   1 
HETATM 2692 O O   . HOH C 3 .   ? 5.487   -25.304 37.608  1.00 71.10 ? 694 HOH A O   1 
HETATM 2693 O O   . HOH C 3 .   ? -3.131  -7.135  -8.167  1.00 60.03 ? 695 HOH A O   1 
HETATM 2694 O O   . HOH C 3 .   ? 16.245  -27.518 13.181  1.00 62.26 ? 696 HOH A O   1 
HETATM 2695 O O   . HOH C 3 .   ? -7.293  -27.378 -6.055  1.00 53.34 ? 697 HOH A O   1 
HETATM 2696 O O   . HOH C 3 .   ? 1.127   -15.456 -10.642 1.00 66.88 ? 698 HOH A O   1 
HETATM 2697 O O   . HOH C 3 .   ? 0.845   -31.909 32.149  1.00 43.37 ? 699 HOH A O   1 
HETATM 2698 O O   . HOH C 3 .   ? 13.782  -17.088 25.335  1.00 49.44 ? 700 HOH A O   1 
HETATM 2699 O O   . HOH C 3 .   ? 7.477   -44.055 8.334   1.00 50.62 ? 701 HOH A O   1 
HETATM 2700 O O   . HOH C 3 .   ? -17.355 -2.152  27.922  1.00 63.06 ? 702 HOH A O   1 
HETATM 2701 O O   . HOH C 3 .   ? -20.686 -12.006 23.508  1.00 38.09 ? 703 HOH A O   1 
HETATM 2702 O O   . HOH C 3 .   ? 0.649   -25.133 -10.578 1.00 34.37 ? 704 HOH A O   1 
HETATM 2703 O O   . HOH C 3 .   ? 10.263  -11.212 35.324  1.00 40.43 ? 705 HOH A O   1 
HETATM 2704 O O   . HOH C 3 .   ? -9.832  -14.872 9.892   1.00 23.02 ? 706 HOH A O   1 
HETATM 2705 O O   . HOH C 3 .   ? 7.563   -24.264 -4.505  1.00 35.57 ? 707 HOH A O   1 
HETATM 2706 O O   . HOH C 3 .   ? -2.829  -13.607 38.455  1.00 49.54 ? 708 HOH A O   1 
HETATM 2707 O O   . HOH C 3 .   ? 9.505   -11.128 -4.804  1.00 63.79 ? 709 HOH A O   1 
HETATM 2708 O O   . HOH C 3 .   ? 6.913   -37.770 19.399  1.00 41.78 ? 710 HOH A O   1 
HETATM 2709 O O   . HOH C 3 .   ? 14.341  -23.454 28.754  1.00 52.84 ? 711 HOH A O   1 
HETATM 2710 O O   . HOH C 3 .   ? 0.050   -28.356 35.970  1.00 42.23 ? 712 HOH A O   1 
HETATM 2711 O O   . HOH C 3 .   ? -3.862  -17.960 17.283  1.00 35.29 ? 713 HOH A O   1 
HETATM 2712 O O   . HOH C 3 .   ? 18.017  -21.920 17.102  1.00 45.91 ? 714 HOH A O   1 
HETATM 2713 O O   . HOH C 3 .   ? 15.128  -5.711  0.119   1.00 60.87 ? 715 HOH A O   1 
HETATM 2714 O O   . HOH C 3 .   ? -5.987  -16.791 10.505  1.00 30.46 ? 716 HOH A O   1 
HETATM 2715 O O   . HOH C 3 .   ? -10.465 -19.152 17.961  1.00 49.78 ? 717 HOH A O   1 
HETATM 2716 O O   . HOH C 3 .   ? -12.920 -25.168 3.330   1.00 57.04 ? 718 HOH A O   1 
HETATM 2717 O O   . HOH C 3 .   ? -2.112  -34.929 14.207  1.00 60.60 ? 719 HOH A O   1 
HETATM 2718 O O   . HOH C 3 .   ? 12.675  -30.946 27.084  1.00 51.28 ? 720 HOH A O   1 
HETATM 2719 O O   . HOH C 3 .   ? 21.234  -18.030 8.813   1.00 41.54 ? 721 HOH A O   1 
HETATM 2720 O O   . HOH C 3 .   ? 18.826  -18.629 7.698   1.00 37.46 ? 722 HOH A O   1 
HETATM 2721 O O   . HOH C 3 .   ? -5.977  -31.656 31.963  1.00 36.39 ? 723 HOH A O   1 
HETATM 2722 O O   . HOH C 3 .   ? 11.836  -6.968  23.350  1.00 63.69 ? 724 HOH A O   1 
HETATM 2723 O O   . HOH C 3 .   ? -17.061 1.339   13.674  1.00 45.09 ? 725 HOH A O   1 
HETATM 2724 O O   . HOH C 3 .   ? -9.194  -30.673 27.555  1.00 59.55 ? 726 HOH A O   1 
HETATM 2725 O O   . HOH C 3 .   ? -15.913 -5.705  19.964  1.00 47.14 ? 727 HOH A O   1 
HETATM 2726 O O   . HOH C 3 .   ? -6.848  8.416   14.292  1.00 42.29 ? 728 HOH A O   1 
HETATM 2727 O O   . HOH C 3 .   ? -9.377  -21.452 11.383  1.00 42.29 ? 729 HOH A O   1 
HETATM 2728 O O   . HOH C 3 .   ? 22.647  -20.244 8.718   1.00 38.44 ? 730 HOH A O   1 
HETATM 2729 O O   . HOH C 3 .   ? -7.043  -17.694 12.897  1.00 51.26 ? 731 HOH A O   1 
HETATM 2730 O O   . HOH C 3 .   ? -10.477 -19.366 9.495   1.00 41.57 ? 732 HOH A O   1 
HETATM 2731 O O   . HOH D 3 .   ? -11.412 -2.067  28.611  1.00 33.80 ? 101 HOH B O   1 
HETATM 2732 O O   . HOH D 3 .   ? -6.791  -3.650  34.069  1.00 36.68 ? 102 HOH B O   1 
HETATM 2733 O O   . HOH D 3 .   ? -11.574 2.891   23.625  1.00 33.81 ? 103 HOH B O   1 
HETATM 2734 O O   . HOH D 3 .   ? -5.243  4.161   30.872  1.00 52.03 ? 104 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 ? 0.5937 0.6104 0.4620 0.1291  -0.0351 0.0632  166 ARG A N   
2    C CA  . ARG A 166 ? 0.5847 0.6136 0.4669 0.1344  -0.0340 0.0574  166 ARG A CA  
3    C C   . ARG A 166 ? 0.6163 0.6037 0.4866 0.1354  -0.0283 0.0569  166 ARG A C   
4    O O   . ARG A 166 ? 0.6398 0.5940 0.4975 0.1244  -0.0248 0.0584  166 ARG A O   
5    C CB  . ARG A 166 ? 0.5665 0.6281 0.4741 0.1176  -0.0349 0.0480  166 ARG A CB  
6    C CG  . ARG A 166 ? 0.5687 0.6120 0.4803 0.0962  -0.0307 0.0427  166 ARG A CG  
7    C CD  . ARG A 166 ? 0.5372 0.6107 0.4718 0.0829  -0.0313 0.0342  166 ARG A CD  
8    N NE  . ARG A 166 ? 0.5063 0.5631 0.4455 0.0666  -0.0270 0.0290  166 ARG A NE  
9    C CZ  . ARG A 166 ? 0.4809 0.5266 0.4238 0.0658  -0.0235 0.0255  166 ARG A CZ  
10   N NH1 . ARG A 166 ? 0.4632 0.5110 0.4054 0.0802  -0.0233 0.0262  166 ARG A NH1 
11   N NH2 . ARG A 166 ? 0.4626 0.4960 0.4094 0.0514  -0.0203 0.0212  166 ARG A NH2 
12   N N   . TYR A 167 ? 0.6139 0.6044 0.4880 0.1478  -0.0270 0.0544  167 TYR A N   
13   C CA  . TYR A 167 ? 0.6355 0.5868 0.4970 0.1492  -0.0217 0.0528  167 TYR A CA  
14   C C   . TYR A 167 ? 0.6063 0.5583 0.4826 0.1303  -0.0187 0.0437  167 TYR A C   
15   O O   . TYR A 167 ? 0.5967 0.5803 0.4933 0.1278  -0.0195 0.0379  167 TYR A O   
16   C CB  . TYR A 167 ? 0.6575 0.6046 0.5106 0.1740  -0.0210 0.0548  167 TYR A CB  
17   C CG  . TYR A 167 ? 0.7018 0.6085 0.5411 0.1753  -0.0155 0.0517  167 TYR A CG  
18   C CD1 . TYR A 167 ? 0.7130 0.6302 0.5663 0.1706  -0.0132 0.0434  167 TYR A CD1 
19   C CD2 . TYR A 167 ? 0.7442 0.6009 0.5550 0.1798  -0.0124 0.0570  167 TYR A CD2 
20   C CE1 . TYR A 167 ? 0.7471 0.6277 0.5868 0.1704  -0.0085 0.0397  167 TYR A CE1 
21   C CE2 . TYR A 167 ? 0.7775 0.5956 0.5741 0.1790  -0.0075 0.0531  167 TYR A CE2 
22   C CZ  . TYR A 167 ? 0.7865 0.6177 0.5980 0.1744  -0.0058 0.0441  167 TYR A CZ  
23   O OH  . TYR A 167 ? 0.8320 0.6265 0.6289 0.1733  -0.0012 0.0395  167 TYR A OH  
24   N N   . ILE A 168 ? 0.5861 0.5025 0.4510 0.1174  -0.0150 0.0429  168 ILE A N   
25   C CA  . ILE A 168 ? 0.5535 0.4666 0.4289 0.1006  -0.0122 0.0352  168 ILE A CA  
26   C C   . ILE A 168 ? 0.5501 0.4234 0.4076 0.1041  -0.0081 0.0340  168 ILE A C   
27   O O   . ILE A 168 ? 0.5598 0.3975 0.3954 0.1054  -0.0063 0.0389  168 ILE A O   
28   C CB  . ILE A 168 ? 0.5499 0.4615 0.4289 0.0800  -0.0119 0.0348  168 ILE A CB  
29   C CG1 . ILE A 168 ? 0.5431 0.4923 0.4383 0.0762  -0.0158 0.0346  168 ILE A CG1 
30   C CG2 . ILE A 168 ? 0.5455 0.4498 0.4319 0.0639  -0.0090 0.0278  168 ILE A CG2 
31   C CD1 . ILE A 168 ? 0.5573 0.5016 0.4469 0.0656  -0.0161 0.0381  168 ILE A CD1 
32   N N   . PRO A 169 ? 0.5307 0.4081 0.3958 0.1052  -0.0063 0.0274  169 PRO A N   
33   C CA  . PRO A 169 ? 0.5336 0.3727 0.3802 0.1087  -0.0025 0.0251  169 PRO A CA  
34   C C   . PRO A 169 ? 0.5219 0.3311 0.3589 0.0889  -0.0001 0.0232  169 PRO A C   
35   O O   . PRO A 169 ? 0.5113 0.3369 0.3634 0.0716  -0.0007 0.0198  169 PRO A O   
36   C CB  . PRO A 169 ? 0.5443 0.4030 0.4046 0.1128  -0.0015 0.0180  169 PRO A CB  
37   C CG  . PRO A 169 ? 0.5315 0.4378 0.4150 0.1159  -0.0047 0.0183  169 PRO A CG  
38   C CD  . PRO A 169 ? 0.5076 0.4235 0.3966 0.1033  -0.0074 0.0217  169 PRO A CD  
39   N N   . SER A 170 ? 0.5270 0.2923 0.3382 0.0914  0.0027  0.0256  170 SER A N   
40   C CA  . SER A 170 ? 0.5319 0.2689 0.3329 0.0710  0.0052  0.0236  170 SER A CA  
41   C C   . SER A 170 ? 0.5067 0.2383 0.3111 0.0617  0.0069  0.0142  170 SER A C   
42   O O   . SER A 170 ? 0.5138 0.2352 0.3173 0.0423  0.0080  0.0109  170 SER A O   
43   C CB  . SER A 170 ? 0.5820 0.2724 0.3525 0.0746  0.0078  0.0298  170 SER A CB  
44   O OG  . SER A 170 ? 0.6479 0.3123 0.4005 0.0930  0.0098  0.0290  170 SER A OG  
45   N N   . LEU A 171 ? 0.4740 0.2141 0.2822 0.0755  0.0071  0.0099  171 LEU A N   
46   C CA  . LEU A 171 ? 0.4607 0.1985 0.2719 0.0684  0.0085  0.0011  171 LEU A CA  
47   C C   . LEU A 171 ? 0.4331 0.2156 0.2719 0.0662  0.0066  -0.0026 171 LEU A C   
48   O O   . LEU A 171 ? 0.4323 0.2434 0.2841 0.0774  0.0049  0.0004  171 LEU A O   
49   C CB  . LEU A 171 ? 0.4745 0.1879 0.2678 0.0863  0.0111  -0.0017 171 LEU A CB  
50   C CG  . LEU A 171 ? 0.5327 0.1955 0.2943 0.0915  0.0138  0.0017  171 LEU A CG  
51   C CD1 . LEU A 171 ? 0.5543 0.1959 0.2989 0.1124  0.0165  -0.0013 171 LEU A CD1 
52   C CD2 . LEU A 171 ? 0.5655 0.1983 0.3148 0.0678  0.0153  -0.0017 171 LEU A CD2 
53   N N   . PRO A 172 ? 0.4138 0.2024 0.2608 0.0521  0.0069  -0.0091 172 PRO A N   
54   C CA  . PRO A 172 ? 0.3921 0.2189 0.2624 0.0511  0.0057  -0.0123 172 PRO A CA  
55   C C   . PRO A 172 ? 0.4096 0.2434 0.2794 0.0686  0.0072  -0.0149 172 PRO A C   
56   O O   . PRO A 172 ? 0.4247 0.2309 0.2754 0.0791  0.0094  -0.0165 172 PRO A O   
57   C CB  . PRO A 172 ? 0.3931 0.2174 0.2663 0.0335  0.0059  -0.0182 172 PRO A CB  
58   C CG  . PRO A 172 ? 0.4249 0.2087 0.2740 0.0307  0.0078  -0.0208 172 PRO A CG  
59   C CD  . PRO A 172 ? 0.4187 0.1796 0.2527 0.0373  0.0083  -0.0141 172 PRO A CD  
60   N N   . ASP A 173 ? 0.3914 0.2616 0.2813 0.0715  0.0065  -0.0153 173 ASP A N   
61   C CA  . ASP A 173 ? 0.4062 0.2922 0.3003 0.0858  0.0083  -0.0178 173 ASP A CA  
62   C C   . ASP A 173 ? 0.4121 0.2879 0.3011 0.0808  0.0105  -0.0250 173 ASP A C   
63   O O   . ASP A 173 ? 0.4357 0.3065 0.3167 0.0940  0.0131  -0.0280 173 ASP A O   
64   C CB  . ASP A 173 ? 0.4352 0.3646 0.3535 0.0850  0.0070  -0.0160 173 ASP A CB  
65   C CG  . ASP A 173 ? 0.5429 0.4968 0.4693 0.0978  0.0092  -0.0177 173 ASP A CG  
66   O OD1 . ASP A 173 ? 0.5493 0.5260 0.4900 0.0902  0.0101  -0.0202 173 ASP A OD1 
67   O OD2 . ASP A 173 ? 0.5999 0.5509 0.5180 0.1158  0.0102  -0.0161 173 ASP A OD2 
68   N N   . ARG A 174 ? 0.3975 0.2731 0.2914 0.0630  0.0095  -0.0278 174 ARG A N   
69   C CA  . ARG A 174 ? 0.4062 0.2750 0.2956 0.0568  0.0108  -0.0345 174 ARG A CA  
70   C C   . ARG A 174 ? 0.4050 0.2576 0.2892 0.0388  0.0092  -0.0366 174 ARG A C   
71   O O   . ARG A 174 ? 0.3880 0.2467 0.2799 0.0291  0.0072  -0.0328 174 ARG A O   
72   C CB  . ARG A 174 ? 0.4145 0.3173 0.3229 0.0541  0.0111  -0.0357 174 ARG A CB  
73   C CG  . ARG A 174 ? 0.4566 0.3820 0.3727 0.0689  0.0134  -0.0347 174 ARG A CG  
74   C CD  . ARG A 174 ? 0.5174 0.4262 0.4174 0.0824  0.0165  -0.0392 174 ARG A CD  
75   N NE  . ARG A 174 ? 0.5731 0.4889 0.4738 0.0787  0.0183  -0.0445 174 ARG A NE  
76   C CZ  . ARG A 174 ? 0.6017 0.5462 0.5146 0.0834  0.0207  -0.0444 174 ARG A CZ  
77   N NH1 . ARG A 174 ? 0.5887 0.5366 0.4994 0.0803  0.0225  -0.0488 174 ARG A NH1 
78   N NH2 . ARG A 174 ? 0.5906 0.5616 0.5175 0.0905  0.0213  -0.0397 174 ARG A NH2 
79   N N   . ILE A 175 ? 0.4127 0.2472 0.2843 0.0337  0.0099  -0.0431 175 ILE A N   
80   C CA  . ILE A 175 ? 0.4203 0.2457 0.2890 0.0154  0.0081  -0.0460 175 ILE A CA  
81   C C   . ILE A 175 ? 0.4252 0.2623 0.2967 0.0116  0.0079  -0.0521 175 ILE A C   
82   O O   . ILE A 175 ? 0.4497 0.2719 0.3074 0.0184  0.0097  -0.0575 175 ILE A O   
83   C CB  . ILE A 175 ? 0.4475 0.2332 0.2930 0.0097  0.0087  -0.0480 175 ILE A CB  
84   C CG1 . ILE A 175 ? 0.4583 0.2312 0.2990 0.0146  0.0091  -0.0407 175 ILE A CG1 
85   C CG2 . ILE A 175 ? 0.4544 0.2385 0.3000 -0.0113 0.0066  -0.0515 175 ILE A CG2 
86   C CD1 . ILE A 175 ? 0.4923 0.2228 0.3080 0.0103  0.0105  -0.0412 175 ILE A CD1 
87   N N   . LEU A 176 ? 0.3929 0.2564 0.2814 0.0024  0.0061  -0.0512 176 LEU A N   
88   C CA  . LEU A 176 ? 0.3851 0.2623 0.2768 -0.0009 0.0056  -0.0557 176 LEU A CA  
89   C C   . LEU A 176 ? 0.3885 0.2601 0.2756 -0.0169 0.0029  -0.0597 176 LEU A C   
90   O O   . LEU A 176 ? 0.3793 0.2528 0.2718 -0.0271 0.0013  -0.0569 176 LEU A O   
91   C CB  . LEU A 176 ? 0.3689 0.2789 0.2811 0.0007  0.0056  -0.0514 176 LEU A CB  
92   C CG  . LEU A 176 ? 0.3884 0.3109 0.3087 0.0136  0.0080  -0.0471 176 LEU A CG  
93   C CD1 . LEU A 176 ? 0.3781 0.3296 0.3168 0.0115  0.0082  -0.0433 176 LEU A CD1 
94   C CD2 . LEU A 176 ? 0.4106 0.3260 0.3204 0.0268  0.0110  -0.0505 176 LEU A CD2 
95   N N   . ASP A 177 ? 0.3967 0.2644 0.2745 -0.0195 0.0024  -0.0665 177 ASP A N   
96   C CA  . ASP A 177 ? 0.4076 0.2740 0.2814 -0.0355 -0.0007 -0.0710 177 ASP A CA  
97   C C   . ASP A 177 ? 0.3941 0.2933 0.2873 -0.0408 -0.0030 -0.0674 177 ASP A C   
98   O O   . ASP A 177 ? 0.4010 0.3192 0.3039 -0.0328 -0.0021 -0.0650 177 ASP A O   
99   C CB  . ASP A 177 ? 0.4538 0.3072 0.3106 -0.0366 -0.0011 -0.0800 177 ASP A CB  
100  C CG  . ASP A 177 ? 0.5763 0.4184 0.4224 -0.0543 -0.0041 -0.0863 177 ASP A CG  
101  O OD1 . ASP A 177 ? 0.5947 0.4391 0.4467 -0.0660 -0.0056 -0.0834 177 ASP A OD1 
102  O OD2 . ASP A 177 ? 0.6353 0.4673 0.4667 -0.0571 -0.0049 -0.0944 177 ASP A OD2 
103  N N   . ALA A 178 ? 0.3828 0.2882 0.2811 -0.0538 -0.0055 -0.0667 178 ALA A N   
104  C CA  . ALA A 178 ? 0.3580 0.2932 0.2730 -0.0580 -0.0076 -0.0636 178 ALA A CA  
105  C C   . ALA A 178 ? 0.3481 0.2891 0.2589 -0.0720 -0.0112 -0.0691 178 ALA A C   
106  O O   . ALA A 178 ? 0.3341 0.2857 0.2521 -0.0822 -0.0128 -0.0675 178 ALA A O   
107  C CB  . ALA A 178 ? 0.3498 0.2928 0.2773 -0.0592 -0.0069 -0.0568 178 ALA A CB  
108  N N   . PRO A 179 ? 0.3559 0.2924 0.2551 -0.0728 -0.0126 -0.0759 179 PRO A N   
109  C CA  . PRO A 179 ? 0.3542 0.2980 0.2488 -0.0873 -0.0166 -0.0819 179 PRO A CA  
110  C C   . PRO A 179 ? 0.3378 0.3165 0.2491 -0.0896 -0.0196 -0.0784 179 PRO A C   
111  O O   . PRO A 179 ? 0.3366 0.3313 0.2572 -0.0784 -0.0188 -0.0738 179 PRO A O   
112  C CB  . PRO A 179 ? 0.3831 0.3161 0.2617 -0.0842 -0.0172 -0.0896 179 PRO A CB  
113  C CG  . PRO A 179 ? 0.3830 0.3187 0.2656 -0.0667 -0.0138 -0.0853 179 PRO A CG  
114  C CD  . PRO A 179 ? 0.3571 0.2836 0.2466 -0.0611 -0.0105 -0.0787 179 PRO A CD  
115  N N   . GLU A 180 ? 0.3395 0.3300 0.2539 -0.1039 -0.0226 -0.0805 180 GLU A N   
116  C CA  . GLU A 180 ? 0.3288 0.3543 0.2582 -0.1062 -0.0256 -0.0777 180 GLU A CA  
117  C C   . GLU A 180 ? 0.3141 0.3526 0.2600 -0.0977 -0.0232 -0.0688 180 GLU A C   
118  O O   . GLU A 180 ? 0.3081 0.3730 0.2653 -0.0930 -0.0247 -0.0653 180 GLU A O   
119  C CB  . GLU A 180 ? 0.3648 0.4088 0.2929 -0.1009 -0.0288 -0.0801 180 GLU A CB  
120  C CG  . GLU A 180 ? 0.4782 0.5113 0.3893 -0.1104 -0.0317 -0.0900 180 GLU A CG  
121  C CD  . GLU A 180 ? 0.6093 0.6666 0.5192 -0.1083 -0.0361 -0.0928 180 GLU A CD  
122  O OE1 . GLU A 180 ? 0.6398 0.7283 0.5632 -0.1061 -0.0387 -0.0884 180 GLU A OE1 
123  O OE2 . GLU A 180 ? 0.6529 0.6977 0.5474 -0.1079 -0.0369 -0.0995 180 GLU A OE2 
124  N N   . ILE A 181 ? 0.3137 0.3334 0.2597 -0.0952 -0.0195 -0.0651 181 ILE A N   
125  C CA  . ILE A 181 ? 0.3002 0.3312 0.2602 -0.0891 -0.0174 -0.0578 181 ILE A CA  
126  C C   . ILE A 181 ? 0.2978 0.3513 0.2673 -0.0991 -0.0191 -0.0571 181 ILE A C   
127  O O   . ILE A 181 ? 0.3063 0.3570 0.2704 -0.1132 -0.0205 -0.0613 181 ILE A O   
128  C CB  . ILE A 181 ? 0.3071 0.3157 0.2646 -0.0847 -0.0136 -0.0544 181 ILE A CB  
129  C CG1 . ILE A 181 ? 0.3002 0.3211 0.2711 -0.0762 -0.0116 -0.0476 181 ILE A CG1 
130  C CG2 . ILE A 181 ? 0.3192 0.3106 0.2687 -0.0969 -0.0131 -0.0560 181 ILE A CG2 
131  C CD1 . ILE A 181 ? 0.3136 0.3171 0.2826 -0.0700 -0.0086 -0.0443 181 ILE A CD1 
132  N N   . ARG A 182 ? 0.2779 0.3550 0.2604 -0.0920 -0.0192 -0.0525 182 ARG A N   
133  C CA  . ARG A 182 ? 0.2822 0.3849 0.2745 -0.0989 -0.0206 -0.0518 182 ARG A CA  
134  C C   . ARG A 182 ? 0.2742 0.3704 0.2699 -0.1045 -0.0175 -0.0490 182 ARG A C   
135  O O   . ARG A 182 ? 0.2710 0.3593 0.2701 -0.0960 -0.0145 -0.0444 182 ARG A O   
136  C CB  . ARG A 182 ? 0.3059 0.4337 0.3087 -0.0872 -0.0213 -0.0478 182 ARG A CB  
137  C CG  . ARG A 182 ? 0.3570 0.5156 0.3700 -0.0922 -0.0230 -0.0474 182 ARG A CG  
138  C CD  . ARG A 182 ? 0.3861 0.5688 0.4061 -0.0794 -0.0245 -0.0441 182 ARG A CD  
139  N NE  . ARG A 182 ? 0.4082 0.5979 0.4219 -0.0786 -0.0287 -0.0474 182 ARG A NE  
140  C CZ  . ARG A 182 ? 0.3835 0.6012 0.3999 -0.0836 -0.0333 -0.0504 182 ARG A CZ  
141  N NH1 . ARG A 182 ? 0.3766 0.5991 0.3857 -0.0825 -0.0372 -0.0536 182 ARG A NH1 
142  N NH2 . ARG A 182 ? 0.3560 0.5998 0.3826 -0.0892 -0.0341 -0.0502 182 ARG A NH2 
143  N N   . ASN A 183 ? 0.2680 0.3661 0.2612 -0.1198 -0.0181 -0.0519 183 ASN A N   
144  C CA  . ASN A 183 ? 0.2743 0.3655 0.2685 -0.1268 -0.0149 -0.0490 183 ASN A CA  
145  C C   . ASN A 183 ? 0.2721 0.3945 0.2812 -0.1248 -0.0140 -0.0455 183 ASN A C   
146  O O   . ASN A 183 ? 0.2793 0.4205 0.2927 -0.1370 -0.0144 -0.0468 183 ASN A O   
147  C CB  . ASN A 183 ? 0.2964 0.3743 0.2798 -0.1453 -0.0152 -0.0534 183 ASN A CB  
148  C CG  . ASN A 183 ? 0.3271 0.3940 0.3085 -0.1533 -0.0114 -0.0498 183 ASN A CG  
149  O OD1 . ASN A 183 ? 0.3283 0.3914 0.3139 -0.1439 -0.0086 -0.0445 183 ASN A OD1 
150  N ND2 . ASN A 183 ? 0.3379 0.3983 0.3113 -0.1717 -0.0110 -0.0528 183 ASN A ND2 
151  N N   . ASP A 184 ? 0.2565 0.3855 0.2729 -0.1096 -0.0129 -0.0415 184 ASP A N   
152  C CA  . ASP A 184 ? 0.2441 0.3990 0.2727 -0.1038 -0.0115 -0.0382 184 ASP A CA  
153  C C   . ASP A 184 ? 0.2491 0.3883 0.2778 -0.0961 -0.0076 -0.0340 184 ASP A C   
154  O O   . ASP A 184 ? 0.2482 0.3730 0.2745 -0.0856 -0.0071 -0.0325 184 ASP A O   
155  C CB  . ASP A 184 ? 0.2509 0.4246 0.2848 -0.0914 -0.0139 -0.0376 184 ASP A CB  
156  C CG  . ASP A 184 ? 0.2756 0.4771 0.3208 -0.0839 -0.0126 -0.0346 184 ASP A CG  
157  O OD1 . ASP A 184 ? 0.2773 0.4746 0.3253 -0.0806 -0.0087 -0.0317 184 ASP A OD1 
158  O OD2 . ASP A 184 ? 0.2986 0.5262 0.3488 -0.0807 -0.0154 -0.0353 184 ASP A OD2 
159  N N   . TYR A 185 ? 0.2433 0.3871 0.2748 -0.1020 -0.0048 -0.0321 185 TYR A N   
160  C CA  . TYR A 185 ? 0.2462 0.3759 0.2766 -0.0965 -0.0013 -0.0286 185 TYR A CA  
161  C C   . TYR A 185 ? 0.2248 0.3584 0.2602 -0.0813 -0.0001 -0.0264 185 TYR A C   
162  O O   . TYR A 185 ? 0.2444 0.3610 0.2766 -0.0759 0.0015  -0.0247 185 TYR A O   
163  C CB  . TYR A 185 ? 0.2452 0.3862 0.2784 -0.1054 0.0016  -0.0271 185 TYR A CB  
164  C CG  . TYR A 185 ? 0.2659 0.3916 0.2954 -0.1025 0.0050  -0.0238 185 TYR A CG  
165  C CD1 . TYR A 185 ? 0.2978 0.3971 0.3166 -0.1078 0.0054  -0.0227 185 TYR A CD1 
166  C CD2 . TYR A 185 ? 0.2710 0.4084 0.3065 -0.0939 0.0076  -0.0219 185 TYR A CD2 
167  C CE1 . TYR A 185 ? 0.3068 0.3944 0.3217 -0.1048 0.0079  -0.0194 185 TYR A CE1 
168  C CE2 . TYR A 185 ? 0.2862 0.4113 0.3175 -0.0921 0.0103  -0.0194 185 TYR A CE2 
169  C CZ  . TYR A 185 ? 0.3062 0.4075 0.3277 -0.0974 0.0102  -0.0180 185 TYR A CZ  
170  O OH  . TYR A 185 ? 0.3121 0.4033 0.3289 -0.0953 0.0123  -0.0153 185 TYR A OH  
171  N N   . TYR A 186 ? 0.1855 0.3412 0.2280 -0.0744 -0.0009 -0.0264 186 TYR A N   
172  C CA  . TYR A 186 ? 0.1824 0.3395 0.2277 -0.0603 0.0011  -0.0241 186 TYR A CA  
173  C C   . TYR A 186 ? 0.1841 0.3258 0.2250 -0.0517 0.0001  -0.0236 186 TYR A C   
174  O O   . TYR A 186 ? 0.1971 0.3341 0.2380 -0.0416 0.0022  -0.0216 186 TYR A O   
175  C CB  . TYR A 186 ? 0.1816 0.3675 0.2347 -0.0545 0.0014  -0.0236 186 TYR A CB  
176  C CG  . TYR A 186 ? 0.1992 0.4031 0.2575 -0.0633 0.0032  -0.0240 186 TYR A CG  
177  C CD1 . TYR A 186 ? 0.2227 0.4239 0.2813 -0.0611 0.0074  -0.0225 186 TYR A CD1 
178  C CD2 . TYR A 186 ? 0.2276 0.4483 0.2887 -0.0762 0.0010  -0.0262 186 TYR A CD2 
179  C CE1 . TYR A 186 ? 0.2357 0.4531 0.2980 -0.0699 0.0097  -0.0225 186 TYR A CE1 
180  C CE2 . TYR A 186 ? 0.2373 0.4739 0.3024 -0.0865 0.0033  -0.0262 186 TYR A CE2 
181  C CZ  . TYR A 186 ? 0.2464 0.4818 0.3124 -0.0828 0.0079  -0.0240 186 TYR A CZ  
182  O OH  . TYR A 186 ? 0.2798 0.5329 0.3496 -0.0927 0.0109  -0.0237 186 TYR A OH  
183  N N   . LEU A 187 ? 0.1604 0.2945 0.1969 -0.0559 -0.0027 -0.0254 187 LEU A N   
184  C CA  . LEU A 187 ? 0.1619 0.2836 0.1941 -0.0484 -0.0033 -0.0248 187 LEU A CA  
185  C C   . LEU A 187 ? 0.1743 0.2732 0.2019 -0.0478 -0.0015 -0.0241 187 LEU A C   
186  O O   . LEU A 187 ? 0.1878 0.2777 0.2134 -0.0541 -0.0010 -0.0246 187 LEU A O   
187  C CB  . LEU A 187 ? 0.1605 0.2861 0.1892 -0.0519 -0.0069 -0.0275 187 LEU A CB  
188  C CG  . LEU A 187 ? 0.1914 0.3434 0.2248 -0.0530 -0.0096 -0.0286 187 LEU A CG  
189  C CD1 . LEU A 187 ? 0.1970 0.3511 0.2250 -0.0570 -0.0135 -0.0319 187 LEU A CD1 
190  C CD2 . LEU A 187 ? 0.1998 0.3658 0.2378 -0.0397 -0.0083 -0.0248 187 LEU A CD2 
191  N N   . ASN A 188 ? 0.1574 0.2478 0.1830 -0.0401 -0.0004 -0.0226 188 ASN A N   
192  C CA  . ASN A 188 ? 0.1432 0.2168 0.1659 -0.0395 0.0011  -0.0220 188 ASN A CA  
193  C C   . ASN A 188 ? 0.1543 0.2216 0.1726 -0.0371 0.0003  -0.0227 188 ASN A C   
194  O O   . ASN A 188 ? 0.1714 0.2377 0.1889 -0.0312 0.0017  -0.0208 188 ASN A O   
195  C CB  . ASN A 188 ? 0.1560 0.2272 0.1807 -0.0340 0.0041  -0.0198 188 ASN A CB  
196  C CG  . ASN A 188 ? 0.1727 0.2480 0.2001 -0.0365 0.0053  -0.0198 188 ASN A CG  
197  O OD1 . ASN A 188 ? 0.2055 0.2738 0.2317 -0.0406 0.0056  -0.0201 188 ASN A OD1 
198  N ND2 . ASN A 188 ? 0.1663 0.2539 0.1967 -0.0333 0.0062  -0.0194 188 ASN A ND2 
199  N N   . LEU A 189 ? 0.1473 0.2094 0.1613 -0.0419 -0.0016 -0.0253 189 LEU A N   
200  C CA  . LEU A 189 ? 0.1695 0.2278 0.1779 -0.0401 -0.0027 -0.0271 189 LEU A CA  
201  C C   . LEU A 189 ? 0.1733 0.2191 0.1780 -0.0369 -0.0011 -0.0271 189 LEU A C   
202  O O   . LEU A 189 ? 0.1797 0.2233 0.1792 -0.0347 -0.0015 -0.0288 189 LEU A O   
203  C CB  . LEU A 189 ? 0.1927 0.2518 0.1965 -0.0476 -0.0056 -0.0311 189 LEU A CB  
204  C CG  . LEU A 189 ? 0.2340 0.3115 0.2424 -0.0519 -0.0077 -0.0317 189 LEU A CG  
205  C CD1 . LEU A 189 ? 0.2601 0.3371 0.2638 -0.0628 -0.0103 -0.0362 189 LEU A CD1 
206  C CD2 . LEU A 189 ? 0.2386 0.3302 0.2488 -0.0449 -0.0087 -0.0303 189 LEU A CD2 
207  N N   A VAL A 190 ? 0.1720 0.2117 0.1790 -0.0361 0.0006  -0.0255 190 VAL A N   
208  N N   B VAL A 190 ? 0.1701 0.2099 0.1771 -0.0360 0.0006  -0.0254 190 VAL A N   
209  C CA  A VAL A 190 ? 0.1743 0.2067 0.1790 -0.0322 0.0020  -0.0254 190 VAL A CA  
210  C CA  B VAL A 190 ? 0.1722 0.2045 0.1769 -0.0323 0.0020  -0.0254 190 VAL A CA  
211  C C   A VAL A 190 ? 0.1638 0.1989 0.1741 -0.0299 0.0043  -0.0226 190 VAL A C   
212  C C   B VAL A 190 ? 0.1637 0.1983 0.1738 -0.0300 0.0042  -0.0227 190 VAL A C   
213  O O   A VAL A 190 ? 0.1593 0.1965 0.1733 -0.0320 0.0045  -0.0214 190 VAL A O   
214  O O   B VAL A 190 ? 0.1607 0.1969 0.1743 -0.0322 0.0044  -0.0216 190 VAL A O   
215  C CB  A VAL A 190 ? 0.1921 0.2126 0.1909 -0.0335 0.0011  -0.0271 190 VAL A CB  
216  C CB  B VAL A 190 ? 0.1887 0.2092 0.1871 -0.0342 0.0008  -0.0274 190 VAL A CB  
217  C CG1 A VAL A 190 ? 0.1941 0.2080 0.1849 -0.0372 -0.0008 -0.0308 190 VAL A CG1 
218  C CG1 B VAL A 190 ? 0.1988 0.2165 0.1986 -0.0384 0.0004  -0.0260 190 VAL A CG1 
219  C CG2 A VAL A 190 ? 0.1980 0.2160 0.1989 -0.0367 0.0009  -0.0254 190 VAL A CG2 
220  C CG2 B VAL A 190 ? 0.1892 0.2041 0.1847 -0.0279 0.0022  -0.0275 190 VAL A CG2 
221  N N   . ASP A 191 ? 0.1552 0.1909 0.1655 -0.0263 0.0061  -0.0220 191 ASP A N   
222  C CA  . ASP A 191 ? 0.1490 0.1880 0.1642 -0.0261 0.0082  -0.0201 191 ASP A CA  
223  C C   . ASP A 191 ? 0.1550 0.1968 0.1702 -0.0227 0.0098  -0.0201 191 ASP A C   
224  O O   . ASP A 191 ? 0.1483 0.1906 0.1601 -0.0200 0.0107  -0.0206 191 ASP A O   
225  C CB  . ASP A 191 ? 0.1594 0.2007 0.1764 -0.0269 0.0102  -0.0181 191 ASP A CB  
226  C CG  . ASP A 191 ? 0.2025 0.2443 0.2230 -0.0294 0.0120  -0.0172 191 ASP A CG  
227  O OD1 . ASP A 191 ? 0.2284 0.2709 0.2509 -0.0310 0.0107  -0.0180 191 ASP A OD1 
228  O OD2 . ASP A 191 ? 0.2026 0.2430 0.2225 -0.0302 0.0148  -0.0156 191 ASP A OD2 
229  N N   . TRP A 192 ? 0.1582 0.2038 0.1772 -0.0227 0.0100  -0.0196 192 TRP A N   
230  C CA  . TRP A 192 ? 0.1602 0.2130 0.1808 -0.0188 0.0115  -0.0196 192 TRP A CA  
231  C C   . TRP A 192 ? 0.1630 0.2252 0.1893 -0.0228 0.0143  -0.0181 192 TRP A C   
232  O O   . TRP A 192 ? 0.1729 0.2362 0.2023 -0.0275 0.0140  -0.0177 192 TRP A O   
233  C CB  . TRP A 192 ? 0.1633 0.2165 0.1841 -0.0157 0.0094  -0.0198 192 TRP A CB  
234  C CG  . TRP A 192 ? 0.1762 0.2342 0.1956 -0.0079 0.0101  -0.0204 192 TRP A CG  
235  C CD1 . TRP A 192 ? 0.1875 0.2575 0.2102 -0.0054 0.0131  -0.0202 192 TRP A CD1 
236  C CD2 . TRP A 192 ? 0.1911 0.2408 0.2041 -0.0009 0.0085  -0.0210 192 TRP A CD2 
237  N NE1 . TRP A 192 ? 0.1926 0.2648 0.2123 0.0039  0.0132  -0.0211 192 TRP A NE1 
238  C CE2 . TRP A 192 ? 0.2003 0.2587 0.2134 0.0073  0.0104  -0.0214 192 TRP A CE2 
239  C CE3 . TRP A 192 ? 0.2046 0.2402 0.2110 -0.0007 0.0060  -0.0207 192 TRP A CE3 
240  C CZ2 . TRP A 192 ? 0.2106 0.2616 0.2163 0.0173  0.0098  -0.0220 192 TRP A CZ2 
241  C CZ3 . TRP A 192 ? 0.2187 0.2449 0.2169 0.0078  0.0054  -0.0209 192 TRP A CZ3 
242  C CH2 . TRP A 192 ? 0.2184 0.2519 0.2161 0.0175  0.0072  -0.0215 192 TRP A CH2 
243  N N   . SER A 193 ? 0.1591 0.2268 0.1852 -0.0218 0.0174  -0.0173 193 SER A N   
244  C CA  . SER A 193 ? 0.1730 0.2470 0.2025 -0.0274 0.0208  -0.0156 193 SER A CA  
245  C C   . SER A 193 ? 0.1902 0.2789 0.2266 -0.0294 0.0214  -0.0160 193 SER A C   
246  O O   . SER A 193 ? 0.1934 0.2902 0.2317 -0.0233 0.0199  -0.0169 193 SER A O   
247  C CB  . SER A 193 ? 0.1709 0.2461 0.1968 -0.0261 0.0245  -0.0140 193 SER A CB  
248  O OG  . SER A 193 ? 0.1772 0.2653 0.2055 -0.0225 0.0264  -0.0145 193 SER A OG  
249  N N   . SER A 194 ? 0.1935 0.2863 0.2328 -0.0377 0.0239  -0.0151 194 SER A N   
250  C CA  . SER A 194 ? 0.2093 0.3204 0.2560 -0.0418 0.0246  -0.0157 194 SER A CA  
251  C C   . SER A 194 ? 0.2174 0.3451 0.2674 -0.0372 0.0274  -0.0151 194 SER A C   
252  O O   . SER A 194 ? 0.2370 0.3850 0.2944 -0.0374 0.0272  -0.0158 194 SER A O   
253  C CB  . SER A 194 ? 0.2335 0.3429 0.2805 -0.0538 0.0274  -0.0155 194 SER A CB  
254  O OG  . SER A 194 ? 0.2481 0.3505 0.2903 -0.0567 0.0323  -0.0130 194 SER A OG  
255  N N   . GLY A 195 ? 0.2026 0.3238 0.2470 -0.0331 0.0300  -0.0139 195 GLY A N   
256  C CA  . GLY A 195 ? 0.1983 0.3330 0.2436 -0.0274 0.0331  -0.0135 195 GLY A CA  
257  C C   . GLY A 195 ? 0.1934 0.3266 0.2357 -0.0149 0.0304  -0.0156 195 GLY A C   
258  O O   . GLY A 195 ? 0.2041 0.3433 0.2440 -0.0080 0.0329  -0.0160 195 GLY A O   
259  N N   . ASN A 196 ? 0.1820 0.3041 0.2225 -0.0119 0.0256  -0.0169 196 ASN A N   
260  C CA  . ASN A 196 ? 0.1885 0.3043 0.2240 -0.0011 0.0230  -0.0188 196 ASN A CA  
261  C C   . ASN A 196 ? 0.1954 0.2954 0.2208 0.0029  0.0233  -0.0202 196 ASN A C   
262  O O   . ASN A 196 ? 0.2016 0.2989 0.2212 0.0121  0.0236  -0.0222 196 ASN A O   
263  C CB  . ASN A 196 ? 0.1962 0.3316 0.2363 0.0074  0.0241  -0.0191 196 ASN A CB  
264  C CG  . ASN A 196 ? 0.2513 0.3786 0.2862 0.0182  0.0207  -0.0201 196 ASN A CG  
265  O OD1 . ASN A 196 ? 0.2437 0.3544 0.2741 0.0165  0.0172  -0.0202 196 ASN A OD1 
266  N ND2 . ASN A 196 ? 0.2735 0.4121 0.3080 0.0300  0.0223  -0.0207 196 ASN A ND2 
267  N N   . VAL A 197 ? 0.1853 0.2748 0.2077 -0.0036 0.0232  -0.0195 197 VAL A N   
268  C CA  . VAL A 197 ? 0.1834 0.2604 0.1965 -0.0011 0.0227  -0.0211 197 VAL A CA  
269  C C   . VAL A 197 ? 0.1840 0.2469 0.1943 -0.0048 0.0187  -0.0217 197 VAL A C   
270  O O   . VAL A 197 ? 0.1793 0.2419 0.1937 -0.0110 0.0183  -0.0198 197 VAL A O   
271  C CB  . VAL A 197 ? 0.2029 0.2836 0.2142 -0.0041 0.0264  -0.0190 197 VAL A CB  
272  C CG1 . VAL A 197 ? 0.2199 0.2899 0.2212 -0.0018 0.0250  -0.0207 197 VAL A CG1 
273  C CG2 . VAL A 197 ? 0.2053 0.3019 0.2192 -0.0016 0.0312  -0.0180 197 VAL A CG2 
274  N N   . LEU A 198 ? 0.1824 0.2335 0.1851 -0.0016 0.0161  -0.0247 198 LEU A N   
275  C CA  . LEU A 198 ? 0.1828 0.2230 0.1829 -0.0063 0.0126  -0.0255 198 LEU A CA  
276  C C   . LEU A 198 ? 0.1861 0.2250 0.1821 -0.0087 0.0123  -0.0260 198 LEU A C   
277  O O   . LEU A 198 ? 0.2030 0.2413 0.1924 -0.0052 0.0133  -0.0280 198 LEU A O   
278  C CB  . LEU A 198 ? 0.2031 0.2300 0.1951 -0.0034 0.0104  -0.0285 198 LEU A CB  
279  C CG  . LEU A 198 ? 0.2400 0.2615 0.2332 -0.0036 0.0086  -0.0275 198 LEU A CG  
280  C CD1 . LEU A 198 ? 0.2756 0.2790 0.2570 -0.0009 0.0072  -0.0303 198 LEU A CD1 
281  C CD2 . LEU A 198 ? 0.2237 0.2465 0.2223 -0.0114 0.0069  -0.0256 198 LEU A CD2 
282  N N   . ALA A 199 ? 0.1671 0.2063 0.1660 -0.0136 0.0110  -0.0244 199 ALA A N   
283  C CA  . ALA A 199 ? 0.1749 0.2152 0.1702 -0.0148 0.0099  -0.0244 199 ALA A CA  
284  C C   . ALA A 199 ? 0.1749 0.2100 0.1679 -0.0187 0.0061  -0.0272 199 ALA A C   
285  O O   . ALA A 199 ? 0.1739 0.2075 0.1713 -0.0219 0.0051  -0.0264 199 ALA A O   
286  C CB  . ALA A 199 ? 0.1786 0.2235 0.1785 -0.0163 0.0116  -0.0203 199 ALA A CB  
287  N N   . VAL A 200 ? 0.1846 0.2174 0.1702 -0.0192 0.0041  -0.0306 200 VAL A N   
288  C CA  . VAL A 200 ? 0.2133 0.2416 0.1958 -0.0250 0.0007  -0.0339 200 VAL A CA  
289  C C   . VAL A 200 ? 0.2091 0.2465 0.1896 -0.0274 -0.0018 -0.0351 200 VAL A C   
290  O O   . VAL A 200 ? 0.2178 0.2565 0.1916 -0.0249 -0.0020 -0.0371 200 VAL A O   
291  C CB  . VAL A 200 ? 0.2454 0.2592 0.2182 -0.0249 0.0003  -0.0384 200 VAL A CB  
292  C CG1 . VAL A 200 ? 0.2640 0.2702 0.2327 -0.0333 -0.0026 -0.0414 200 VAL A CG1 
293  C CG2 . VAL A 200 ? 0.2685 0.2759 0.2425 -0.0192 0.0028  -0.0369 200 VAL A CG2 
294  N N   . ALA A 201 ? 0.1963 0.2418 0.1821 -0.0317 -0.0038 -0.0340 201 ALA A N   
295  C CA  . ALA A 201 ? 0.2076 0.2659 0.1925 -0.0334 -0.0068 -0.0350 201 ALA A CA  
296  C C   . ALA A 201 ? 0.2154 0.2714 0.1947 -0.0421 -0.0102 -0.0409 201 ALA A C   
297  O O   . ALA A 201 ? 0.2113 0.2641 0.1929 -0.0489 -0.0108 -0.0417 201 ALA A O   
298  C CB  . ALA A 201 ? 0.2205 0.2911 0.2139 -0.0325 -0.0069 -0.0311 201 ALA A CB  
299  N N   . LEU A 202 ? 0.2147 0.2714 0.1852 -0.0428 -0.0122 -0.0450 202 LEU A N   
300  C CA  . LEU A 202 ? 0.2327 0.2861 0.1958 -0.0526 -0.0156 -0.0516 202 LEU A CA  
301  C C   . LEU A 202 ? 0.2412 0.3161 0.2048 -0.0551 -0.0197 -0.0532 202 LEU A C   
302  O O   . LEU A 202 ? 0.2415 0.3206 0.1983 -0.0508 -0.0208 -0.0547 202 LEU A O   
303  C CB  . LEU A 202 ? 0.2518 0.2852 0.2014 -0.0519 -0.0146 -0.0568 202 LEU A CB  
304  C CG  . LEU A 202 ? 0.2639 0.2781 0.2123 -0.0475 -0.0107 -0.0551 202 LEU A CG  
305  C CD1 . LEU A 202 ? 0.2793 0.2753 0.2137 -0.0441 -0.0095 -0.0602 202 LEU A CD1 
306  C CD2 . LEU A 202 ? 0.2710 0.2770 0.2221 -0.0549 -0.0109 -0.0543 202 LEU A CD2 
307  N N   . ASP A 203 ? 0.2438 0.3343 0.2153 -0.0615 -0.0220 -0.0526 203 ASP A N   
308  C CA  . ASP A 203 ? 0.2412 0.3577 0.2155 -0.0635 -0.0264 -0.0536 203 ASP A CA  
309  C C   . ASP A 203 ? 0.2254 0.3543 0.2026 -0.0499 -0.0257 -0.0475 203 ASP A C   
310  O O   . ASP A 203 ? 0.2167 0.3482 0.2022 -0.0433 -0.0230 -0.0415 203 ASP A O   
311  C CB  . ASP A 203 ? 0.2854 0.4030 0.2490 -0.0738 -0.0307 -0.0619 203 ASP A CB  
312  C CG  . ASP A 203 ? 0.3824 0.5316 0.3497 -0.0764 -0.0360 -0.0632 203 ASP A CG  
313  O OD1 . ASP A 203 ? 0.3714 0.5418 0.3509 -0.0750 -0.0366 -0.0590 203 ASP A OD1 
314  O OD2 . ASP A 203 ? 0.4452 0.5994 0.4030 -0.0788 -0.0396 -0.0684 203 ASP A OD2 
315  N N   . ASN A 204 ? 0.2271 0.3607 0.1958 -0.0455 -0.0277 -0.0490 204 ASN A N   
316  C CA  . ASN A 204 ? 0.2300 0.3732 0.1991 -0.0329 -0.0267 -0.0424 204 ASN A CA  
317  C C   . ASN A 204 ? 0.2420 0.3669 0.2047 -0.0253 -0.0220 -0.0396 204 ASN A C   
318  O O   . ASN A 204 ? 0.2568 0.3871 0.2159 -0.0162 -0.0210 -0.0348 204 ASN A O   
319  C CB  . ASN A 204 ? 0.2617 0.4275 0.2259 -0.0318 -0.0322 -0.0443 204 ASN A CB  
320  C CG  . ASN A 204 ? 0.3175 0.4765 0.2685 -0.0366 -0.0343 -0.0514 204 ASN A CG  
321  O OD1 . ASN A 204 ? 0.3409 0.4780 0.2862 -0.0418 -0.0320 -0.0559 204 ASN A OD1 
322  N ND2 . ASN A 204 ? 0.3309 0.5085 0.2754 -0.0341 -0.0388 -0.0526 204 ASN A ND2 
323  N N   . SER A 205 ? 0.2306 0.3356 0.1910 -0.0286 -0.0190 -0.0423 205 SER A N   
324  C CA  . SER A 205 ? 0.2305 0.3218 0.1860 -0.0219 -0.0142 -0.0401 205 SER A CA  
325  C C   . SER A 205 ? 0.2278 0.3063 0.1906 -0.0212 -0.0098 -0.0371 205 SER A C   
326  O O   . SER A 205 ? 0.2282 0.3030 0.1966 -0.0269 -0.0106 -0.0385 205 SER A O   
327  C CB  . SER A 205 ? 0.2611 0.3423 0.2046 -0.0244 -0.0147 -0.0471 205 SER A CB  
328  O OG  . SER A 205 ? 0.3050 0.3979 0.2397 -0.0242 -0.0185 -0.0501 205 SER A OG  
329  N N   . VAL A 206 ? 0.2055 0.2784 0.1678 -0.0148 -0.0052 -0.0328 206 VAL A N   
330  C CA  . VAL A 206 ? 0.1972 0.2600 0.1657 -0.0145 -0.0013 -0.0307 206 VAL A CA  
331  C C   . VAL A 206 ? 0.2089 0.2634 0.1709 -0.0119 0.0015  -0.0332 206 VAL A C   
332  O O   . VAL A 206 ? 0.2085 0.2663 0.1644 -0.0074 0.0033  -0.0321 206 VAL A O   
333  C CB  . VAL A 206 ? 0.1932 0.2580 0.1679 -0.0107 0.0021  -0.0236 206 VAL A CB  
334  C CG1 . VAL A 206 ? 0.2001 0.2566 0.1804 -0.0115 0.0058  -0.0224 206 VAL A CG1 
335  C CG2 . VAL A 206 ? 0.1873 0.2598 0.1677 -0.0115 -0.0003 -0.0215 206 VAL A CG2 
336  N N   . TYR A 207 ? 0.2114 0.2557 0.1742 -0.0136 0.0021  -0.0363 207 TYR A N   
337  C CA  . TYR A 207 ? 0.2160 0.2531 0.1731 -0.0092 0.0050  -0.0387 207 TYR A CA  
338  C C   . TYR A 207 ? 0.2053 0.2423 0.1711 -0.0067 0.0087  -0.0347 207 TYR A C   
339  O O   . TYR A 207 ? 0.1981 0.2339 0.1715 -0.0100 0.0078  -0.0327 207 TYR A O   
340  C CB  . TYR A 207 ? 0.2323 0.2558 0.1809 -0.0117 0.0028  -0.0455 207 TYR A CB  
341  C CG  . TYR A 207 ? 0.2657 0.2891 0.2032 -0.0144 -0.0003 -0.0510 207 TYR A CG  
342  C CD1 . TYR A 207 ? 0.2822 0.3112 0.2204 -0.0221 -0.0049 -0.0526 207 TYR A CD1 
343  C CD2 . TYR A 207 ? 0.2925 0.3130 0.2189 -0.0093 0.0015  -0.0547 207 TYR A CD2 
344  C CE1 . TYR A 207 ? 0.3118 0.3439 0.2400 -0.0257 -0.0083 -0.0581 207 TYR A CE1 
345  C CE2 . TYR A 207 ? 0.3161 0.3369 0.2310 -0.0123 -0.0017 -0.0604 207 TYR A CE2 
346  C CZ  . TYR A 207 ? 0.3397 0.3673 0.2559 -0.0208 -0.0069 -0.0620 207 TYR A CZ  
347  O OH  . TYR A 207 ? 0.4035 0.4337 0.3083 -0.0249 -0.0106 -0.0683 207 TYR A OH  
348  N N   . LEU A 208 ? 0.1969 0.2368 0.1615 -0.0014 0.0128  -0.0337 208 LEU A N   
349  C CA  . LEU A 208 ? 0.2040 0.2475 0.1768 0.0005  0.0161  -0.0307 208 LEU A CA  
350  C C   . LEU A 208 ? 0.2277 0.2662 0.1960 0.0064  0.0173  -0.0345 208 LEU A C   
351  O O   . LEU A 208 ? 0.2471 0.2848 0.2066 0.0111  0.0189  -0.0376 208 LEU A O   
352  C CB  . LEU A 208 ? 0.2013 0.2554 0.1773 0.0015  0.0207  -0.0259 208 LEU A CB  
353  C CG  . LEU A 208 ? 0.2090 0.2653 0.1860 -0.0020 0.0204  -0.0215 208 LEU A CG  
354  C CD1 . LEU A 208 ? 0.2175 0.2805 0.1950 -0.0018 0.0259  -0.0164 208 LEU A CD1 
355  C CD2 . LEU A 208 ? 0.2050 0.2582 0.1897 -0.0066 0.0181  -0.0199 208 LEU A CD2 
356  N N   . TRP A 209 ? 0.2252 0.2607 0.1986 0.0073  0.0169  -0.0342 209 TRP A N   
357  C CA  . TRP A 209 ? 0.2417 0.2724 0.2106 0.0151  0.0182  -0.0369 209 TRP A CA  
358  C C   . TRP A 209 ? 0.2420 0.2876 0.2219 0.0181  0.0210  -0.0330 209 TRP A C   
359  O O   . TRP A 209 ? 0.2210 0.2697 0.2094 0.0138  0.0195  -0.0302 209 TRP A O   
360  C CB  . TRP A 209 ? 0.2565 0.2689 0.2190 0.0139  0.0146  -0.0397 209 TRP A CB  
361  C CG  . TRP A 209 ? 0.2839 0.2869 0.2396 0.0234  0.0158  -0.0418 209 TRP A CG  
362  C CD1 . TRP A 209 ? 0.3145 0.3052 0.2565 0.0306  0.0172  -0.0468 209 TRP A CD1 
363  C CD2 . TRP A 209 ? 0.2832 0.2867 0.2437 0.0277  0.0156  -0.0390 209 TRP A CD2 
364  N NE1 . TRP A 209 ? 0.3268 0.3095 0.2646 0.0403  0.0182  -0.0469 209 TRP A NE1 
365  C CE2 . TRP A 209 ? 0.3111 0.3025 0.2604 0.0388  0.0170  -0.0418 209 TRP A CE2 
366  C CE3 . TRP A 209 ? 0.2819 0.2941 0.2536 0.0237  0.0142  -0.0346 209 TRP A CE3 
367  C CZ2 . TRP A 209 ? 0.3161 0.3056 0.2658 0.0470  0.0170  -0.0395 209 TRP A CZ2 
368  C CZ3 . TRP A 209 ? 0.2948 0.3062 0.2671 0.0305  0.0139  -0.0328 209 TRP A CZ3 
369  C CH2 . TRP A 209 ? 0.3076 0.3085 0.2693 0.0426  0.0152  -0.0349 209 TRP A CH2 
370  N N   . SER A 210 ? 0.2532 0.3098 0.2328 0.0253  0.0251  -0.0333 210 SER A N   
371  C CA  . SER A 210 ? 0.2708 0.3462 0.2615 0.0275  0.0278  -0.0302 210 SER A CA  
372  C C   . SER A 210 ? 0.2935 0.3649 0.2827 0.0362  0.0264  -0.0316 210 SER A C   
373  O O   . SER A 210 ? 0.3068 0.3707 0.2862 0.0461  0.0276  -0.0350 210 SER A O   
374  C CB  . SER A 210 ? 0.3133 0.4051 0.3045 0.0313  0.0333  -0.0296 210 SER A CB  
375  O OG  . SER A 210 ? 0.3779 0.4702 0.3677 0.0239  0.0346  -0.0275 210 SER A OG  
376  N N   . ALA A 211 ? 0.2912 0.3658 0.2882 0.0334  0.0240  -0.0290 211 ALA A N   
377  C CA  . ALA A 211 ? 0.3128 0.3821 0.3070 0.0423  0.0221  -0.0294 211 ALA A CA  
378  C C   . ALA A 211 ? 0.3416 0.4259 0.3366 0.0554  0.0253  -0.0298 211 ALA A C   
379  O O   . ALA A 211 ? 0.3707 0.4420 0.3558 0.0668  0.0248  -0.0315 211 ALA A O   
380  C CB  . ALA A 211 ? 0.3133 0.3866 0.3158 0.0365  0.0190  -0.0262 211 ALA A CB  
381  N N   . SER A 212 ? 0.3278 0.4385 0.3334 0.0543  0.0289  -0.0281 212 SER A N   
382  C CA  . SER A 212 ? 0.3430 0.4738 0.3515 0.0671  0.0322  -0.0284 212 SER A CA  
383  C C   . SER A 212 ? 0.3567 0.4798 0.3530 0.0778  0.0359  -0.0322 212 SER A C   
384  O O   . SER A 212 ? 0.3665 0.4940 0.3586 0.0931  0.0376  -0.0336 212 SER A O   
385  C CB  . SER A 212 ? 0.3615 0.5259 0.3861 0.0608  0.0350  -0.0254 212 SER A CB  
386  O OG  . SER A 212 ? 0.4113 0.5807 0.4371 0.0518  0.0389  -0.0250 212 SER A OG  
387  N N   . SER A 213 ? 0.3490 0.4608 0.3384 0.0710  0.0372  -0.0341 213 SER A N   
388  C CA  . SER A 213 ? 0.3497 0.4551 0.3264 0.0807  0.0408  -0.0384 213 SER A CA  
389  C C   . SER A 213 ? 0.3607 0.4324 0.3194 0.0821  0.0380  -0.0434 213 SER A C   
390  O O   . SER A 213 ? 0.3670 0.4287 0.3122 0.0926  0.0406  -0.0481 213 SER A O   
391  C CB  . SER A 213 ? 0.3494 0.4709 0.3293 0.0745  0.0453  -0.0374 213 SER A CB  
392  O OG  . SER A 213 ? 0.3669 0.4772 0.3464 0.0607  0.0426  -0.0360 213 SER A OG  
393  N N   . GLY A 214 ? 0.3491 0.4042 0.3071 0.0709  0.0333  -0.0428 214 GLY A N   
394  C CA  . GLY A 214 ? 0.3560 0.3819 0.2981 0.0682  0.0305  -0.0476 214 GLY A CA  
395  C C   . GLY A 214 ? 0.3561 0.3818 0.2933 0.0608  0.0310  -0.0498 214 GLY A C   
396  O O   . GLY A 214 ? 0.3864 0.3914 0.3103 0.0576  0.0286  -0.0546 214 GLY A O   
397  N N   A ASP A 215 ? 0.3343 0.3828 0.2809 0.0579  0.0342  -0.0464 215 ASP A N   
398  N N   B ASP A 215 ? 0.3319 0.3804 0.2791 0.0573  0.0340  -0.0462 215 ASP A N   
399  C CA  A ASP A 215 ? 0.3302 0.3796 0.2713 0.0522  0.0348  -0.0474 215 ASP A CA  
400  C CA  B ASP A 215 ? 0.3251 0.3762 0.2680 0.0513  0.0347  -0.0467 215 ASP A CA  
401  C C   A ASP A 215 ? 0.3252 0.3652 0.2678 0.0400  0.0296  -0.0462 215 ASP A C   
402  C C   B ASP A 215 ? 0.3238 0.3635 0.2666 0.0397  0.0294  -0.0461 215 ASP A C   
403  O O   A ASP A 215 ? 0.3167 0.3596 0.2702 0.0341  0.0275  -0.0422 215 ASP A O   
404  O O   B ASP A 215 ? 0.3170 0.3586 0.2702 0.0336  0.0271  -0.0423 215 ASP A O   
405  C CB  A ASP A 215 ? 0.3402 0.4143 0.2901 0.0514  0.0399  -0.0428 215 ASP A CB  
406  C CB  B ASP A 215 ? 0.3245 0.4008 0.2791 0.0486  0.0392  -0.0410 215 ASP A CB  
407  C CG  A ASP A 215 ? 0.3921 0.4800 0.3400 0.0632  0.0458  -0.0443 215 ASP A CG  
408  C CG  B ASP A 215 ? 0.3617 0.4413 0.3113 0.0434  0.0406  -0.0398 215 ASP A CG  
409  O OD1 A ASP A 215 ? 0.4024 0.4776 0.3386 0.0738  0.0460  -0.0500 215 ASP A OD1 
410  O OD1 B ASP A 215 ? 0.3603 0.4439 0.3006 0.0495  0.0443  -0.0423 215 ASP A OD1 
411  O OD2 A ASP A 215 ? 0.4176 0.5285 0.3751 0.0619  0.0505  -0.0400 215 ASP A OD2 
412  O OD2 B ASP A 215 ? 0.3789 0.4574 0.3329 0.0340  0.0382  -0.0360 215 ASP A OD2 
413  N N   . ILE A 216 ? 0.3271 0.3567 0.2580 0.0369  0.0274  -0.0503 216 ILE A N   
414  C CA  . ILE A 216 ? 0.3271 0.3504 0.2583 0.0265  0.0224  -0.0500 216 ILE A CA  
415  C C   . ILE A 216 ? 0.3098 0.3436 0.2386 0.0238  0.0230  -0.0483 216 ILE A C   
416  O O   . ILE A 216 ? 0.3095 0.3445 0.2278 0.0287  0.0253  -0.0515 216 ILE A O   
417  C CB  . ILE A 216 ? 0.3523 0.3541 0.2704 0.0243  0.0184  -0.0569 216 ILE A CB  
418  C CG1 . ILE A 216 ? 0.3693 0.3568 0.2868 0.0279  0.0182  -0.0578 216 ILE A CG1 
419  C CG2 . ILE A 216 ? 0.3591 0.3597 0.2780 0.0131  0.0132  -0.0571 216 ILE A CG2 
420  C CD1 . ILE A 216 ? 0.4025 0.3644 0.3025 0.0278  0.0163  -0.0651 216 ILE A CD1 
421  N N   . LEU A 217 ? 0.2890 0.3299 0.2262 0.0172  0.0214  -0.0431 217 LEU A N   
422  C CA  . LEU A 217 ? 0.2826 0.3322 0.2168 0.0154  0.0216  -0.0401 217 LEU A CA  
423  C C   . LEU A 217 ? 0.2684 0.3157 0.2036 0.0087  0.0159  -0.0399 217 LEU A C   
424  O O   . LEU A 217 ? 0.2596 0.3053 0.2042 0.0046  0.0142  -0.0375 217 LEU A O   
425  C CB  . LEU A 217 ? 0.2879 0.3494 0.2317 0.0150  0.0263  -0.0322 217 LEU A CB  
426  C CG  . LEU A 217 ? 0.3254 0.3931 0.2650 0.0138  0.0274  -0.0272 217 LEU A CG  
427  C CD1 . LEU A 217 ? 0.3387 0.4122 0.2678 0.0190  0.0315  -0.0281 217 LEU A CD1 
428  C CD2 . LEU A 217 ? 0.3352 0.4071 0.2841 0.0101  0.0305  -0.0195 217 LEU A CD2 
429  N N   . GLN A 218 ? 0.2648 0.3144 0.1906 0.0079  0.0131  -0.0422 218 GLN A N   
430  C CA  . GLN A 218 ? 0.2601 0.3136 0.1880 0.0026  0.0080  -0.0411 218 GLN A CA  
431  C C   . GLN A 218 ? 0.2488 0.3120 0.1814 0.0049  0.0106  -0.0325 218 GLN A C   
432  O O   . GLN A 218 ? 0.2609 0.3299 0.1855 0.0086  0.0123  -0.0302 218 GLN A O   
433  C CB  . GLN A 218 ? 0.2767 0.3317 0.1923 0.0007  0.0034  -0.0473 218 GLN A CB  
434  C CG  . GLN A 218 ? 0.3212 0.3846 0.2411 -0.0050 -0.0024 -0.0466 218 GLN A CG  
435  C CD  . GLN A 218 ? 0.3871 0.4569 0.2959 -0.0079 -0.0075 -0.0525 218 GLN A CD  
436  O OE1 . GLN A 218 ? 0.4182 0.4856 0.3145 -0.0052 -0.0067 -0.0568 218 GLN A OE1 
437  N NE2 . GLN A 218 ? 0.4051 0.4850 0.3181 -0.0135 -0.0129 -0.0531 218 GLN A NE2 
438  N N   . LEU A 219 ? 0.2273 0.2901 0.1710 0.0029  0.0116  -0.0275 219 LEU A N   
439  C CA  . LEU A 219 ? 0.2357 0.3023 0.1819 0.0046  0.0149  -0.0195 219 LEU A CA  
440  C C   . LEU A 219 ? 0.2514 0.3243 0.1921 0.0068  0.0118  -0.0166 219 LEU A C   
441  O O   . LEU A 219 ? 0.2643 0.3393 0.1988 0.0107  0.0148  -0.0107 219 LEU A O   
442  C CB  . LEU A 219 ? 0.2297 0.2925 0.1875 0.0014  0.0160  -0.0163 219 LEU A CB  
443  C CG  . LEU A 219 ? 0.2326 0.2944 0.1917 0.0021  0.0196  -0.0086 219 LEU A CG  
444  C CD1 . LEU A 219 ? 0.2493 0.3118 0.2045 0.0030  0.0259  -0.0049 219 LEU A CD1 
445  C CD2 . LEU A 219 ? 0.2401 0.2973 0.2092 -0.0017 0.0196  -0.0075 219 LEU A CD2 
446  N N   . LEU A 220 ? 0.2492 0.3257 0.1919 0.0042  0.0060  -0.0201 220 LEU A N   
447  C CA  . LEU A 220 ? 0.2499 0.3363 0.1892 0.0071  0.0024  -0.0172 220 LEU A CA  
448  C C   . LEU A 220 ? 0.2537 0.3483 0.1936 0.0026  -0.0044 -0.0237 220 LEU A C   
449  O O   . LEU A 220 ? 0.2485 0.3377 0.1925 -0.0037 -0.0059 -0.0294 220 LEU A O   
450  C CB  . LEU A 220 ? 0.2531 0.3379 0.1992 0.0095  0.0043  -0.0100 220 LEU A CB  
451  C CG  . LEU A 220 ? 0.2803 0.3634 0.2379 0.0048  0.0025  -0.0122 220 LEU A CG  
452  C CD1 . LEU A 220 ? 0.2956 0.3914 0.2556 0.0062  -0.0025 -0.0120 220 LEU A CD1 
453  C CD2 . LEU A 220 ? 0.2913 0.3641 0.2544 0.0049  0.0076  -0.0073 220 LEU A CD2 
454  N N   . GLN A 221 ? 0.2482 0.3563 0.1835 0.0057  -0.0083 -0.0224 221 GLN A N   
455  C CA  . GLN A 221 ? 0.2637 0.3849 0.2007 0.0006  -0.0150 -0.0278 221 GLN A CA  
456  C C   . GLN A 221 ? 0.2631 0.4005 0.2024 0.0071  -0.0175 -0.0218 221 GLN A C   
457  O O   . GLN A 221 ? 0.2706 0.4108 0.2025 0.0158  -0.0161 -0.0156 221 GLN A O   
458  C CB  . GLN A 221 ? 0.3004 0.4250 0.2260 -0.0030 -0.0186 -0.0355 221 GLN A CB  
459  C CG  . GLN A 221 ? 0.3734 0.5111 0.3010 -0.0118 -0.0255 -0.0424 221 GLN A CG  
460  C CD  . GLN A 221 ? 0.4850 0.6249 0.3997 -0.0168 -0.0293 -0.0511 221 GLN A CD  
461  O OE1 . GLN A 221 ? 0.5108 0.6575 0.4149 -0.0111 -0.0301 -0.0503 221 GLN A OE1 
462  N NE2 . GLN A 221 ? 0.5152 0.6481 0.4289 -0.0282 -0.0318 -0.0597 221 GLN A NE2 
463  N N   . MET A 222 ? 0.2525 0.4014 0.2012 0.0034  -0.0212 -0.0234 222 MET A N   
464  C CA  . MET A 222 ? 0.2529 0.4211 0.2045 0.0106  -0.0242 -0.0185 222 MET A CA  
465  C C   . MET A 222 ? 0.2626 0.4492 0.2045 0.0142  -0.0293 -0.0195 222 MET A C   
466  O O   . MET A 222 ? 0.2732 0.4622 0.2093 0.0064  -0.0326 -0.0271 222 MET A O   
467  C CB  . MET A 222 ? 0.2523 0.4333 0.2160 0.0041  -0.0273 -0.0218 222 MET A CB  
468  C CG  . MET A 222 ? 0.2998 0.4642 0.2722 0.0008  -0.0226 -0.0209 222 MET A CG  
469  S SD  . MET A 222 ? 0.3747 0.5338 0.3509 0.0131  -0.0177 -0.0113 222 MET A SD  
470  C CE  . MET A 222 ? 0.4127 0.5475 0.3795 0.0172  -0.0116 -0.0069 222 MET A CE  
471  N N   . GLU A 223 ? 0.2643 0.4613 0.2025 0.0266  -0.0297 -0.0116 223 GLU A N   
472  C CA  . GLU A 223 ? 0.2950 0.5100 0.2226 0.0317  -0.0346 -0.0113 223 GLU A CA  
473  C C   . GLU A 223 ? 0.2954 0.5430 0.2284 0.0315  -0.0425 -0.0140 223 GLU A C   
474  O O   . GLU A 223 ? 0.3074 0.5727 0.2324 0.0316  -0.0480 -0.0168 223 GLU A O   
475  C CB  . GLU A 223 ? 0.3633 0.5704 0.2794 0.0461  -0.0306 -0.0007 223 GLU A CB  
476  C CG  . GLU A 223 ? 0.4778 0.6586 0.3862 0.0447  -0.0234 0.0011  223 GLU A CG  
477  C CD  . GLU A 223 ? 0.6246 0.8051 0.5164 0.0519  -0.0223 0.0055  223 GLU A CD  
478  O OE1 . GLU A 223 ? 0.6692 0.8322 0.5548 0.0499  -0.0164 0.0062  223 GLU A OE1 
479  O OE2 . GLU A 223 ? 0.6614 0.8610 0.5463 0.0598  -0.0274 0.0084  223 GLU A OE2 
480  N N   . GLN A 224 ? 0.2849 0.5426 0.2312 0.0311  -0.0430 -0.0132 224 GLN A N   
481  C CA  . GLN A 224 ? 0.2859 0.5795 0.2387 0.0313  -0.0502 -0.0153 224 GLN A CA  
482  C C   . GLN A 224 ? 0.2608 0.5657 0.2230 0.0131  -0.0541 -0.0258 224 GLN A C   
483  O O   . GLN A 224 ? 0.2527 0.5387 0.2212 0.0041  -0.0501 -0.0285 224 GLN A O   
484  C CB  . GLN A 224 ? 0.3136 0.6176 0.2742 0.0451  -0.0486 -0.0070 224 GLN A CB  
485  C CG  . GLN A 224 ? 0.3831 0.6650 0.3346 0.0617  -0.0424 0.0039  224 GLN A CG  
486  C CD  . GLN A 224 ? 0.4704 0.7538 0.4061 0.0712  -0.0439 0.0086  224 GLN A CD  
487  O OE1 . GLN A 224 ? 0.5099 0.7665 0.4346 0.0749  -0.0383 0.0135  224 GLN A OE1 
488  N NE2 . GLN A 224 ? 0.4795 0.7959 0.4134 0.0751  -0.0515 0.0075  224 GLN A NE2 
489  N N   . PRO A 225 ? 0.2476 0.5849 0.2105 0.0074  -0.0619 -0.0312 225 PRO A N   
490  C CA  . PRO A 225 ? 0.2387 0.5881 0.2099 -0.0117 -0.0654 -0.0410 225 PRO A CA  
491  C C   . PRO A 225 ? 0.2445 0.5976 0.2312 -0.0134 -0.0623 -0.0387 225 PRO A C   
492  O O   . PRO A 225 ? 0.2548 0.6186 0.2477 0.0013  -0.0605 -0.0308 225 PRO A O   
493  C CB  . PRO A 225 ? 0.2344 0.6256 0.2053 -0.0133 -0.0744 -0.0445 225 PRO A CB  
494  C CG  . PRO A 225 ? 0.2393 0.6281 0.1950 0.0002  -0.0756 -0.0401 225 PRO A CG  
495  C CD  . PRO A 225 ? 0.2284 0.5929 0.1836 0.0173  -0.0679 -0.0287 225 PRO A CD  
496  N N   . GLY A 226 ? 0.2334 0.5741 0.2246 -0.0302 -0.0608 -0.0453 226 GLY A N   
497  C CA  . GLY A 226 ? 0.2284 0.5716 0.2331 -0.0337 -0.0575 -0.0438 226 GLY A CA  
498  C C   . GLY A 226 ? 0.2394 0.5499 0.2450 -0.0260 -0.0497 -0.0379 226 GLY A C   
499  O O   . GLY A 226 ? 0.2676 0.5715 0.2812 -0.0322 -0.0464 -0.0384 226 GLY A O   
500  N N   . GLU A 227 ? 0.2300 0.5210 0.2269 -0.0128 -0.0466 -0.0323 227 GLU A N   
501  C CA  . GLU A 227 ? 0.2197 0.4818 0.2169 -0.0058 -0.0394 -0.0268 227 GLU A CA  
502  C C   . GLU A 227 ? 0.2081 0.4417 0.2038 -0.0177 -0.0360 -0.0313 227 GLU A C   
503  O O   . GLU A 227 ? 0.2125 0.4369 0.2003 -0.0260 -0.0378 -0.0370 227 GLU A O   
504  C CB  . GLU A 227 ? 0.2634 0.5116 0.2504 0.0087  -0.0367 -0.0199 227 GLU A CB  
505  C CG  . GLU A 227 ? 0.3397 0.6034 0.3263 0.0258  -0.0370 -0.0119 227 GLU A CG  
506  C CD  . GLU A 227 ? 0.4580 0.6985 0.4327 0.0377  -0.0323 -0.0045 227 GLU A CD  
507  O OE1 . GLU A 227 ? 0.4469 0.6757 0.4122 0.0342  -0.0322 -0.0063 227 GLU A OE1 
508  O OE2 . GLU A 227 ? 0.4828 0.7162 0.4567 0.0503  -0.0284 0.0029  227 GLU A OE2 
509  N N   . TYR A 228 ? 0.1885 0.4086 0.1909 -0.0180 -0.0314 -0.0291 228 TYR A N   
510  C CA  . TYR A 228 ? 0.1909 0.3843 0.1916 -0.0266 -0.0280 -0.0320 228 TYR A CA  
511  C C   . TYR A 228 ? 0.1889 0.3630 0.1916 -0.0186 -0.0220 -0.0263 228 TYR A C   
512  O O   . TYR A 228 ? 0.1884 0.3693 0.1947 -0.0085 -0.0203 -0.0209 228 TYR A O   
513  C CB  . TYR A 228 ? 0.1902 0.3870 0.1962 -0.0416 -0.0294 -0.0376 228 TYR A CB  
514  C CG  . TYR A 228 ? 0.1973 0.4121 0.2149 -0.0412 -0.0286 -0.0352 228 TYR A CG  
515  C CD1 . TYR A 228 ? 0.2014 0.4493 0.2252 -0.0425 -0.0327 -0.0362 228 TYR A CD1 
516  C CD2 . TYR A 228 ? 0.2124 0.4131 0.2346 -0.0400 -0.0239 -0.0323 228 TYR A CD2 
517  C CE1 . TYR A 228 ? 0.1984 0.4651 0.2331 -0.0413 -0.0315 -0.0340 228 TYR A CE1 
518  C CE2 . TYR A 228 ? 0.2156 0.4327 0.2473 -0.0391 -0.0226 -0.0305 228 TYR A CE2 
519  C CZ  . TYR A 228 ? 0.2164 0.4667 0.2545 -0.0395 -0.0262 -0.0313 228 TYR A CZ  
520  O OH  . TYR A 228 ? 0.2276 0.4963 0.2754 -0.0376 -0.0244 -0.0294 228 TYR A OH  
521  N N   . ILE A 229 ? 0.1788 0.3294 0.1784 -0.0229 -0.0190 -0.0277 229 ILE A N   
522  C CA  . ILE A 229 ? 0.1771 0.3108 0.1788 -0.0179 -0.0138 -0.0234 229 ILE A CA  
523  C C   . ILE A 229 ? 0.1651 0.2997 0.1750 -0.0233 -0.0127 -0.0242 229 ILE A C   
524  O O   . ILE A 229 ? 0.1765 0.3107 0.1874 -0.0337 -0.0144 -0.0286 229 ILE A O   
525  C CB  . ILE A 229 ? 0.1967 0.3093 0.1927 -0.0199 -0.0112 -0.0247 229 ILE A CB  
526  C CG1 . ILE A 229 ? 0.2257 0.3383 0.2124 -0.0159 -0.0120 -0.0250 229 ILE A CG1 
527  C CG2 . ILE A 229 ? 0.1863 0.2850 0.1852 -0.0161 -0.0062 -0.0206 229 ILE A CG2 
528  C CD1 . ILE A 229 ? 0.2571 0.3724 0.2411 -0.0059 -0.0102 -0.0188 229 ILE A CD1 
529  N N   . SER A 230 ? 0.1417 0.2758 0.1557 -0.0165 -0.0097 -0.0199 230 SER A N   
530  C CA  . SER A 230 ? 0.1400 0.2761 0.1611 -0.0204 -0.0082 -0.0203 230 SER A CA  
531  C C   . SER A 230 ? 0.1393 0.2553 0.1601 -0.0202 -0.0040 -0.0189 230 SER A C   
532  O O   . SER A 230 ? 0.1441 0.2587 0.1689 -0.0253 -0.0030 -0.0200 230 SER A O   
533  C CB  . SER A 230 ? 0.1590 0.3148 0.1852 -0.0131 -0.0083 -0.0179 230 SER A CB  
534  O OG  . SER A 230 ? 0.2001 0.3544 0.2217 -0.0004 -0.0070 -0.0133 230 SER A OG  
535  N N   . SER A 231 ? 0.1323 0.2339 0.1481 -0.0154 -0.0017 -0.0167 231 SER A N   
536  C CA  . SER A 231 ? 0.1407 0.2259 0.1566 -0.0168 0.0017  -0.0160 231 SER A CA  
537  C C   . SER A 231 ? 0.1415 0.2147 0.1523 -0.0147 0.0037  -0.0145 231 SER A C   
538  O O   . SER A 231 ? 0.1508 0.2261 0.1570 -0.0096 0.0037  -0.0124 231 SER A O   
539  C CB  . SER A 231 ? 0.1650 0.2485 0.1827 -0.0120 0.0047  -0.0136 231 SER A CB  
540  O OG  . SER A 231 ? 0.1628 0.2487 0.1769 -0.0026 0.0058  -0.0101 231 SER A OG  
541  N N   . VAL A 232 ? 0.1433 0.2058 0.1548 -0.0183 0.0055  -0.0153 232 VAL A N   
542  C CA  . VAL A 232 ? 0.1507 0.2048 0.1589 -0.0170 0.0081  -0.0138 232 VAL A CA  
543  C C   . VAL A 232 ? 0.1470 0.1935 0.1581 -0.0195 0.0108  -0.0134 232 VAL A C   
544  O O   . VAL A 232 ? 0.1443 0.1909 0.1590 -0.0229 0.0098  -0.0152 232 VAL A O   
545  C CB  . VAL A 232 ? 0.1710 0.2243 0.1764 -0.0187 0.0069  -0.0163 232 VAL A CB  
546  C CG1 . VAL A 232 ? 0.1749 0.2355 0.1758 -0.0173 0.0040  -0.0177 232 VAL A CG1 
547  C CG2 . VAL A 232 ? 0.1855 0.2350 0.1932 -0.0233 0.0056  -0.0194 232 VAL A CG2 
548  N N   . ALA A 233 ? 0.1408 0.1809 0.1493 -0.0184 0.0143  -0.0108 233 ALA A N   
549  C CA  . ALA A 233 ? 0.1440 0.1784 0.1547 -0.0223 0.0166  -0.0111 233 ALA A CA  
550  C C   . ALA A 233 ? 0.1543 0.1848 0.1623 -0.0236 0.0202  -0.0089 233 ALA A C   
551  O O   . ALA A 233 ? 0.1649 0.1898 0.1671 -0.0210 0.0228  -0.0057 233 ALA A O   
552  C CB  . ALA A 233 ? 0.1552 0.1846 0.1656 -0.0220 0.0178  -0.0108 233 ALA A CB  
553  N N   . TRP A 234 ? 0.1491 0.1826 0.1609 -0.0278 0.0208  -0.0103 234 TRP A N   
554  C CA  . TRP A 234 ? 0.1630 0.1966 0.1737 -0.0306 0.0246  -0.0086 234 TRP A CA  
555  C C   . TRP A 234 ? 0.1790 0.2043 0.1880 -0.0360 0.0278  -0.0077 234 TRP A C   
556  O O   . TRP A 234 ? 0.1794 0.2038 0.1913 -0.0389 0.0264  -0.0101 234 TRP A O   
557  C CB  . TRP A 234 ? 0.1673 0.2111 0.1837 -0.0323 0.0238  -0.0107 234 TRP A CB  
558  C CG  . TRP A 234 ? 0.1644 0.2130 0.1798 -0.0272 0.0218  -0.0119 234 TRP A CG  
559  C CD1 . TRP A 234 ? 0.1726 0.2223 0.1893 -0.0248 0.0182  -0.0146 234 TRP A CD1 
560  C CD2 . TRP A 234 ? 0.1613 0.2134 0.1731 -0.0244 0.0240  -0.0107 234 TRP A CD2 
561  N NE1 . TRP A 234 ? 0.1749 0.2264 0.1881 -0.0206 0.0178  -0.0158 234 TRP A NE1 
562  C CE2 . TRP A 234 ? 0.1739 0.2282 0.1843 -0.0199 0.0213  -0.0137 234 TRP A CE2 
563  C CE3 . TRP A 234 ? 0.1754 0.2280 0.1837 -0.0256 0.0285  -0.0075 234 TRP A CE3 
564  C CZ2 . TRP A 234 ? 0.1771 0.2345 0.1828 -0.0159 0.0226  -0.0141 234 TRP A CZ2 
565  C CZ3 . TRP A 234 ? 0.1823 0.2398 0.1865 -0.0217 0.0299  -0.0072 234 TRP A CZ3 
566  C CH2 . TRP A 234 ? 0.1856 0.2459 0.1886 -0.0165 0.0269  -0.0109 234 TRP A CH2 
567  N N   . ILE A 235 ? 0.1976 0.2170 0.2013 -0.0385 0.0322  -0.0046 235 ILE A N   
568  C CA  . ILE A 235 ? 0.2178 0.2273 0.2184 -0.0461 0.0359  -0.0044 235 ILE A CA  
569  C C   . ILE A 235 ? 0.2310 0.2537 0.2402 -0.0538 0.0353  -0.0075 235 ILE A C   
570  O O   . ILE A 235 ? 0.2208 0.2586 0.2364 -0.0516 0.0334  -0.0084 235 ILE A O   
571  C CB  . ILE A 235 ? 0.2270 0.2252 0.2181 -0.0480 0.0415  0.0005  235 ILE A CB  
572  C CG1 . ILE A 235 ? 0.2554 0.2342 0.2381 -0.0545 0.0455  0.0009  235 ILE A CG1 
573  C CG2 . ILE A 235 ? 0.2293 0.2403 0.2239 -0.0527 0.0440  0.0016  235 ILE A CG2 
574  C CD1 . ILE A 235 ? 0.2676 0.2295 0.2377 -0.0553 0.0513  0.0066  235 ILE A CD1 
575  N N   . LYS A 236 ? 0.2515 0.2692 0.2600 -0.0621 0.0366  -0.0096 236 LYS A N   
576  C CA  . LYS A 236 ? 0.2736 0.3067 0.2902 -0.0695 0.0353  -0.0128 236 LYS A CA  
577  C C   . LYS A 236 ? 0.2819 0.3323 0.3043 -0.0721 0.0372  -0.0115 236 LYS A C   
578  O O   . LYS A 236 ? 0.2891 0.3577 0.3200 -0.0696 0.0341  -0.0133 236 LYS A O   
579  C CB  . LYS A 236 ? 0.3102 0.3341 0.3230 -0.0802 0.0372  -0.0154 236 LYS A CB  
580  N N   . GLU A 237 ? 0.2881 0.3333 0.3052 -0.0757 0.0423  -0.0080 237 GLU A N   
581  C CA  . GLU A 237 ? 0.2929 0.3563 0.3151 -0.0782 0.0451  -0.0065 237 GLU A CA  
582  C C   . GLU A 237 ? 0.2877 0.3611 0.3124 -0.0664 0.0433  -0.0056 237 GLU A C   
583  O O   . GLU A 237 ? 0.2911 0.3815 0.3202 -0.0661 0.0455  -0.0049 237 GLU A O   
584  C CB  . GLU A 237 ? 0.3430 0.3959 0.3568 -0.0867 0.0520  -0.0025 237 GLU A CB  
585  N N   . GLY A 238 ? 0.2802 0.3431 0.3010 -0.0573 0.0399  -0.0057 238 GLY A N   
586  C CA  . GLY A 238 ? 0.2766 0.3455 0.2978 -0.0474 0.0377  -0.0059 238 GLY A CA  
587  C C   . GLY A 238 ? 0.2723 0.3393 0.2865 -0.0442 0.0414  -0.0025 238 GLY A C   
588  O O   . GLY A 238 ? 0.2826 0.3558 0.2963 -0.0368 0.0399  -0.0035 238 GLY A O   
589  N N   . ASN A 239 ? 0.2554 0.3121 0.2625 -0.0494 0.0461  0.0016  239 ASN A N   
590  C CA  . ASN A 239 ? 0.2658 0.3204 0.2645 -0.0460 0.0498  0.0057  239 ASN A CA  
591  C C   . ASN A 239 ? 0.2569 0.2960 0.2455 -0.0388 0.0481  0.0083  239 ASN A C   
592  O O   . ASN A 239 ? 0.2687 0.3079 0.2500 -0.0336 0.0494  0.0112  239 ASN A O   
593  C CB  . ASN A 239 ? 0.3039 0.3580 0.2992 -0.0557 0.0568  0.0097  239 ASN A CB  
594  C CG  . ASN A 239 ? 0.3825 0.4191 0.3729 -0.0648 0.0592  0.0112  239 ASN A CG  
595  O OD1 . ASN A 239 ? 0.3890 0.4190 0.3823 -0.0659 0.0557  0.0080  239 ASN A OD1 
596  N ND2 . ASN A 239 ? 0.4159 0.4434 0.3976 -0.0722 0.0659  0.0162  239 ASN A ND2 
597  N N   . TYR A 240 ? 0.2355 0.2638 0.2238 -0.0377 0.0450  0.0073  240 TYR A N   
598  C CA  . TYR A 240 ? 0.2322 0.2498 0.2126 -0.0300 0.0430  0.0095  240 TYR A CA  
599  C C   . TYR A 240 ? 0.2147 0.2367 0.2013 -0.0257 0.0368  0.0050  240 TYR A C   
600  O O   . TYR A 240 ? 0.2099 0.2332 0.2036 -0.0297 0.0351  0.0016  240 TYR A O   
601  C CB  . TYR A 240 ? 0.2609 0.2589 0.2327 -0.0322 0.0465  0.0133  240 TYR A CB  
602  C CG  . TYR A 240 ? 0.3116 0.3011 0.2748 -0.0382 0.0534  0.0184  240 TYR A CG  
603  C CD1 . TYR A 240 ? 0.3385 0.3273 0.2927 -0.0334 0.0558  0.0235  240 TYR A CD1 
604  C CD2 . TYR A 240 ? 0.3501 0.3341 0.3143 -0.0499 0.0575  0.0179  240 TYR A CD2 
605  C CE1 . TYR A 240 ? 0.3694 0.3499 0.3146 -0.0398 0.0628  0.0289  240 TYR A CE1 
606  C CE2 . TYR A 240 ? 0.3785 0.3542 0.3342 -0.0575 0.0644  0.0228  240 TYR A CE2 
607  C CZ  . TYR A 240 ? 0.4005 0.3743 0.3467 -0.0524 0.0674  0.0286  240 TYR A CZ  
608  O OH  . TYR A 240 ? 0.4566 0.4225 0.3935 -0.0606 0.0748  0.0341  240 TYR A OH  
609  N N   . LEU A 241 ? 0.1965 0.2214 0.1801 -0.0185 0.0334  0.0049  241 LEU A N   
610  C CA  . LEU A 241 ? 0.1890 0.2185 0.1778 -0.0158 0.0279  0.0009  241 LEU A CA  
611  C C   . LEU A 241 ? 0.1901 0.2146 0.1739 -0.0102 0.0266  0.0034  241 LEU A C   
612  O O   . LEU A 241 ? 0.1926 0.2162 0.1686 -0.0049 0.0274  0.0071  241 LEU A O   
613  C CB  . LEU A 241 ? 0.1858 0.2253 0.1753 -0.0132 0.0244  -0.0024 241 LEU A CB  
614  C CG  . LEU A 241 ? 0.1902 0.2334 0.1838 -0.0127 0.0191  -0.0066 241 LEU A CG  
615  C CD1 . LEU A 241 ? 0.1922 0.2350 0.1932 -0.0170 0.0184  -0.0094 241 LEU A CD1 
616  C CD2 . LEU A 241 ? 0.2096 0.2587 0.1999 -0.0106 0.0160  -0.0099 241 LEU A CD2 
617  N N   . ALA A 242 ? 0.1821 0.2048 0.1700 -0.0103 0.0249  0.0016  242 ALA A N   
618  C CA  . ALA A 242 ? 0.1786 0.2006 0.1630 -0.0033 0.0234  0.0035  242 ALA A CA  
619  C C   . ALA A 242 ? 0.1822 0.2193 0.1716 -0.0019 0.0179  0.0000  242 ALA A C   
620  O O   . ALA A 242 ? 0.1790 0.2209 0.1748 -0.0071 0.0157  -0.0043 242 ALA A O   
621  C CB  . ALA A 242 ? 0.1822 0.1959 0.1680 -0.0040 0.0249  0.0027  242 ALA A CB  
622  N N   . VAL A 243 ? 0.1842 0.2288 0.1697 0.0049  0.0157  0.0019  243 VAL A N   
623  C CA  . VAL A 243 ? 0.1794 0.2397 0.1687 0.0046  0.0104  -0.0017 243 VAL A CA  
624  C C   . VAL A 243 ? 0.1919 0.2619 0.1819 0.0114  0.0085  0.0000  243 VAL A C   
625  O O   . VAL A 243 ? 0.2019 0.2723 0.1851 0.0200  0.0092  0.0046  243 VAL A O   
626  C CB  . VAL A 243 ? 0.1922 0.2578 0.1756 0.0057  0.0088  -0.0018 243 VAL A CB  
627  C CG1 . VAL A 243 ? 0.2058 0.2869 0.1915 0.0040  0.0032  -0.0062 243 VAL A CG1 
628  C CG2 . VAL A 243 ? 0.1888 0.2470 0.1718 0.0005  0.0113  -0.0036 243 VAL A CG2 
629  N N   . GLY A 244 ? 0.1851 0.2635 0.1828 0.0084  0.0064  -0.0033 244 GLY A N   
630  C CA  . GLY A 244 ? 0.1845 0.2771 0.1845 0.0149  0.0047  -0.0023 244 GLY A CA  
631  C C   . GLY A 244 ? 0.1843 0.2978 0.1868 0.0128  -0.0007 -0.0050 244 GLY A C   
632  O O   . GLY A 244 ? 0.1749 0.2900 0.1796 0.0035  -0.0031 -0.0096 244 GLY A O   
633  N N   . THR A 245 ? 0.1804 0.3101 0.1817 0.0217  -0.0028 -0.0024 245 THR A N   
634  C CA  . THR A 245 ? 0.1883 0.3407 0.1915 0.0192  -0.0085 -0.0053 245 THR A CA  
635  C C   . THR A 245 ? 0.1926 0.3709 0.2040 0.0212  -0.0113 -0.0063 245 THR A C   
636  O O   . THR A 245 ? 0.1776 0.3571 0.1913 0.0293  -0.0085 -0.0033 245 THR A O   
637  C CB  . THR A 245 ? 0.2023 0.3571 0.1956 0.0274  -0.0099 -0.0016 245 THR A CB  
638  O OG1 . THR A 245 ? 0.2081 0.3733 0.1992 0.0412  -0.0098 0.0039  245 THR A OG1 
639  C CG2 . THR A 245 ? 0.2209 0.3510 0.2054 0.0277  -0.0055 0.0012  245 THR A CG2 
640  N N   . SER A 246 ? 0.1995 0.3994 0.2145 0.0138  -0.0166 -0.0107 246 SER A N   
641  C CA  . SER A 246 ? 0.1977 0.4288 0.2212 0.0139  -0.0199 -0.0120 246 SER A CA  
642  C C   . SER A 246 ? 0.2192 0.4670 0.2406 0.0312  -0.0207 -0.0063 246 SER A C   
643  O O   . SER A 246 ? 0.2307 0.5023 0.2598 0.0363  -0.0214 -0.0057 246 SER A O   
644  C CB  . SER A 246 ? 0.1856 0.4341 0.2108 0.0008  -0.0256 -0.0183 246 SER A CB  
645  O OG  . SER A 246 ? 0.1956 0.4464 0.2119 0.0052  -0.0288 -0.0176 246 SER A OG  
646  N N   A SER A 247 ? 0.2198 0.4563 0.2303 0.0408  -0.0204 -0.0018 247 SER A N   
647  N N   B SER A 247 ? 0.2217 0.4582 0.2322 0.0409  -0.0204 -0.0018 247 SER A N   
648  C CA  A SER A 247 ? 0.2176 0.4645 0.2227 0.0590  -0.0207 0.0049  247 SER A CA  
649  C CA  B SER A 247 ? 0.2212 0.4687 0.2265 0.0592  -0.0207 0.0049  247 SER A CA  
650  C C   A SER A 247 ? 0.2332 0.4559 0.2331 0.0712  -0.0139 0.0108  247 SER A C   
651  C C   B SER A 247 ? 0.2318 0.4560 0.2322 0.0715  -0.0140 0.0107  247 SER A C   
652  O O   A SER A 247 ? 0.2473 0.4639 0.2370 0.0866  -0.0124 0.0175  247 SER A O   
653  O O   B SER A 247 ? 0.2422 0.4623 0.2331 0.0875  -0.0127 0.0175  247 SER A O   
654  C CB  A SER A 247 ? 0.2320 0.4776 0.2257 0.0632  -0.0234 0.0075  247 SER A CB  
655  C CB  B SER A 247 ? 0.2431 0.4886 0.2368 0.0641  -0.0232 0.0078  247 SER A CB  
656  O OG  A SER A 247 ? 0.2576 0.4728 0.2439 0.0564  -0.0199 0.0071  247 SER A OG  
657  O OG  B SER A 247 ? 0.2581 0.5297 0.2550 0.0551  -0.0300 0.0022  247 SER A OG  
658  N N   . ALA A 248 ? 0.2252 0.4325 0.2304 0.0643  -0.0097 0.0082  248 ALA A N   
659  C CA  . ALA A 248 ? 0.2318 0.4154 0.2320 0.0732  -0.0033 0.0119  248 ALA A CA  
660  C C   . ALA A 248 ? 0.2510 0.4007 0.2374 0.0768  0.0012  0.0165  248 ALA A C   
661  O O   . ALA A 248 ? 0.2739 0.4047 0.2520 0.0876  0.0061  0.0210  248 ALA A O   
662  C CB  . ALA A 248 ? 0.2133 0.4142 0.2139 0.0905  -0.0028 0.0155  248 ALA A CB  
663  N N   . GLU A 249 ? 0.2313 0.3727 0.2148 0.0673  0.0000  0.0153  249 GLU A N   
664  C CA  . GLU A 249 ? 0.2401 0.3523 0.2116 0.0685  0.0047  0.0196  249 GLU A CA  
665  C C   . GLU A 249 ? 0.2379 0.3299 0.2126 0.0556  0.0082  0.0159  249 GLU A C   
666  O O   . GLU A 249 ? 0.2328 0.3335 0.2173 0.0445  0.0058  0.0100  249 GLU A O   
667  C CB  . GLU A 249 ? 0.2672 0.3840 0.2324 0.0670  0.0019  0.0209  249 GLU A CB  
668  C CG  . GLU A 249 ? 0.3193 0.4581 0.2800 0.0795  -0.0024 0.0247  249 GLU A CG  
669  C CD  . GLU A 249 ? 0.4197 0.5710 0.3773 0.0747  -0.0070 0.0229  249 GLU A CD  
670  O OE1 . GLU A 249 ? 0.4150 0.5751 0.3632 0.0856  -0.0090 0.0280  249 GLU A OE1 
671  O OE2 . GLU A 249 ? 0.4595 0.6117 0.4229 0.0607  -0.0086 0.0162  249 GLU A OE2 
672  N N   . VAL A 250 ? 0.2435 0.3085 0.2089 0.0569  0.0139  0.0196  250 VAL A N   
673  C CA  . VAL A 250 ? 0.2394 0.2874 0.2071 0.0447  0.0171  0.0165  250 VAL A CA  
674  C C   . VAL A 250 ? 0.2491 0.2837 0.2070 0.0432  0.0198  0.0205  250 VAL A C   
675  O O   . VAL A 250 ? 0.2639 0.2810 0.2098 0.0498  0.0241  0.0264  250 VAL A O   
676  C CB  . VAL A 250 ? 0.2690 0.2986 0.2348 0.0452  0.0218  0.0164  250 VAL A CB  
677  C CG1 . VAL A 250 ? 0.2841 0.2998 0.2524 0.0321  0.0243  0.0132  250 VAL A CG1 
678  C CG2 . VAL A 250 ? 0.2695 0.3146 0.2440 0.0482  0.0196  0.0129  250 VAL A CG2 
679  N N   . GLN A 251 ? 0.2416 0.2850 0.2031 0.0357  0.0173  0.0176  251 GLN A N   
680  C CA  . GLN A 251 ? 0.2495 0.2849 0.2025 0.0343  0.0199  0.0209  251 GLN A CA  
681  C C   . GLN A 251 ? 0.2620 0.2828 0.2167 0.0241  0.0244  0.0195  251 GLN A C   
682  O O   . GLN A 251 ? 0.2744 0.2973 0.2388 0.0169  0.0235  0.0144  251 GLN A O   
683  C CB  . GLN A 251 ? 0.2691 0.3229 0.2242 0.0324  0.0149  0.0176  251 GLN A CB  
684  C CG  . GLN A 251 ? 0.3004 0.3737 0.2551 0.0408  0.0095  0.0181  251 GLN A CG  
685  C CD  . GLN A 251 ? 0.3469 0.4361 0.2998 0.0389  0.0048  0.0150  251 GLN A CD  
686  O OE1 . GLN A 251 ? 0.3470 0.4324 0.2991 0.0318  0.0056  0.0119  251 GLN A OE1 
687  N NE2 . GLN A 251 ? 0.3702 0.4790 0.3222 0.0456  -0.0003 0.0155  251 GLN A NE2 
688  N N   . LEU A 252 ? 0.2558 0.2625 0.2008 0.0233  0.0296  0.0245  252 LEU A N   
689  C CA  . LEU A 252 ? 0.2569 0.2539 0.2041 0.0128  0.0340  0.0233  252 LEU A CA  
690  C C   . LEU A 252 ? 0.2451 0.2490 0.1895 0.0105  0.0349  0.0242  252 LEU A C   
691  O O   . LEU A 252 ? 0.2569 0.2576 0.1901 0.0161  0.0367  0.0297  252 LEU A O   
692  C CB  . LEU A 252 ? 0.2859 0.2596 0.2239 0.0113  0.0403  0.0278  252 LEU A CB  
693  C CG  . LEU A 252 ? 0.3302 0.2977 0.2722 -0.0016 0.0443  0.0255  252 LEU A CG  
694  C CD1 . LEU A 252 ? 0.3220 0.2996 0.2783 -0.0075 0.0407  0.0181  252 LEU A CD1 
695  C CD2 . LEU A 252 ? 0.3774 0.3197 0.3076 -0.0051 0.0510  0.0299  252 LEU A CD2 
696  N N   . TRP A 253 ? 0.2231 0.2378 0.1769 0.0039  0.0333  0.0186  253 TRP A N   
697  C CA  . TRP A 253 ? 0.2238 0.2466 0.1753 0.0026  0.0342  0.0181  253 TRP A CA  
698  C C   . TRP A 253 ? 0.2298 0.2501 0.1843 -0.0058 0.0396  0.0182  253 TRP A C   
699  O O   . TRP A 253 ? 0.2461 0.2668 0.2098 -0.0117 0.0394  0.0146  253 TRP A O   
700  C CB  . TRP A 253 ? 0.2148 0.2522 0.1730 0.0032  0.0283  0.0113  253 TRP A CB  
701  C CG  . TRP A 253 ? 0.2174 0.2625 0.1709 0.0101  0.0234  0.0113  253 TRP A CG  
702  C CD1 . TRP A 253 ? 0.2307 0.2789 0.1865 0.0140  0.0196  0.0112  253 TRP A CD1 
703  C CD2 . TRP A 253 ? 0.2258 0.2788 0.1708 0.0143  0.0219  0.0117  253 TRP A CD2 
704  N NE1 . TRP A 253 ? 0.2341 0.2934 0.1842 0.0200  0.0155  0.0117  253 TRP A NE1 
705  C CE2 . TRP A 253 ? 0.2324 0.2943 0.1755 0.0199  0.0166  0.0116  253 TRP A CE2 
706  C CE3 . TRP A 253 ? 0.2395 0.2949 0.1785 0.0137  0.0246  0.0115  253 TRP A CE3 
707  C CZ2 . TRP A 253 ? 0.2397 0.3124 0.1745 0.0243  0.0133  0.0113  253 TRP A CZ2 
708  C CZ3 . TRP A 253 ? 0.2522 0.3160 0.1818 0.0187  0.0219  0.0114  253 TRP A CZ3 
709  C CH2 . TRP A 253 ? 0.2483 0.3206 0.1758 0.0236  0.0160  0.0111  253 TRP A CH2 
710  N N   . ASP A 254 ? 0.2151 0.2354 0.1620 -0.0064 0.0442  0.0222  254 ASP A N   
711  C CA  . ASP A 254 ? 0.2315 0.2549 0.1821 -0.0147 0.0495  0.0222  254 ASP A CA  
712  C C   . ASP A 254 ? 0.2382 0.2782 0.1940 -0.0126 0.0472  0.0168  254 ASP A C   
713  O O   . ASP A 254 ? 0.2414 0.2862 0.1896 -0.0072 0.0468  0.0176  254 ASP A O   
714  C CB  . ASP A 254 ? 0.2709 0.2856 0.2092 -0.0165 0.0565  0.0298  254 ASP A CB  
715  C CG  . ASP A 254 ? 0.3190 0.3399 0.2607 -0.0262 0.0628  0.0305  254 ASP A CG  
716  O OD1 . ASP A 254 ? 0.3124 0.3508 0.2636 -0.0270 0.0617  0.0254  254 ASP A OD1 
717  O OD2 . ASP A 254 ? 0.3557 0.3642 0.2899 -0.0330 0.0691  0.0361  254 ASP A OD2 
718  N N   . VAL A 255 ? 0.2319 0.2798 0.1992 -0.0159 0.0454  0.0113  255 VAL A N   
719  C CA  . VAL A 255 ? 0.2376 0.2975 0.2080 -0.0123 0.0431  0.0060  255 VAL A CA  
720  C C   . VAL A 255 ? 0.2478 0.3181 0.2168 -0.0132 0.0489  0.0072  255 VAL A C   
721  O O   . VAL A 255 ? 0.2639 0.3415 0.2301 -0.0077 0.0480  0.0037  255 VAL A O   
722  C CB  . VAL A 255 ? 0.2456 0.3085 0.2263 -0.0130 0.0388  0.0002  255 VAL A CB  
723  C CG1 . VAL A 255 ? 0.2413 0.2958 0.2228 -0.0123 0.0337  -0.0007 255 VAL A CG1 
724  C CG2 . VAL A 255 ? 0.2533 0.3211 0.2430 -0.0196 0.0418  0.0004  255 VAL A CG2 
725  N N   . GLN A 256 ? 0.2440 0.3147 0.2135 -0.0203 0.0551  0.0119  256 GLN A N   
726  C CA  . GLN A 256 ? 0.2480 0.3318 0.2162 -0.0218 0.0613  0.0135  256 GLN A CA  
727  C C   . GLN A 256 ? 0.2555 0.3358 0.2094 -0.0167 0.0635  0.0175  256 GLN A C   
728  O O   . GLN A 256 ? 0.2630 0.3547 0.2136 -0.0123 0.0656  0.0159  256 GLN A O   
729  C CB  . GLN A 256 ? 0.2763 0.3618 0.2485 -0.0332 0.0675  0.0175  256 GLN A CB  
730  N N   . GLN A 257 ? 0.2501 0.3150 0.1947 -0.0163 0.0631  0.0228  257 GLN A N   
731  C CA  . GLN A 257 ? 0.2529 0.3145 0.1826 -0.0105 0.0645  0.0273  257 GLN A CA  
732  C C   . GLN A 257 ? 0.2502 0.3134 0.1761 -0.0012 0.0568  0.0227  257 GLN A C   
733  O O   . GLN A 257 ? 0.2679 0.3321 0.1817 0.0044  0.0569  0.0252  257 GLN A O   
734  C CB  . GLN A 257 ? 0.2776 0.3209 0.1970 -0.0125 0.0674  0.0358  257 GLN A CB  
735  C CG  . GLN A 257 ? 0.3146 0.3524 0.2340 -0.0238 0.0756  0.0408  257 GLN A CG  
736  C CD  . GLN A 257 ? 0.4078 0.4234 0.3116 -0.0244 0.0795  0.0500  257 GLN A CD  
737  O OE1 . GLN A 257 ? 0.4574 0.4700 0.3477 -0.0228 0.0844  0.0566  257 GLN A OE1 
738  N NE2 . GLN A 257 ? 0.4276 0.4261 0.3315 -0.0255 0.0777  0.0506  257 GLN A NE2 
739  N N   A GLN A 258 ? 0.2393 0.3025 0.1745 -0.0003 0.0504  0.0165  258 GLN A N   
740  N N   B GLN A 258 ? 0.2457 0.3092 0.1810 -0.0002 0.0504  0.0164  258 GLN A N   
741  C CA  A GLN A 258 ? 0.2450 0.3098 0.1776 0.0057  0.0431  0.0117  258 GLN A CA  
742  C CA  B GLN A 258 ? 0.2549 0.3197 0.1874 0.0058  0.0430  0.0116  258 GLN A CA  
743  C C   A GLN A 258 ? 0.2642 0.3233 0.1860 0.0105  0.0413  0.0173  258 GLN A C   
744  C C   B GLN A 258 ? 0.2665 0.3257 0.1886 0.0104  0.0411  0.0172  258 GLN A C   
745  O O   A GLN A 258 ? 0.2712 0.3356 0.1829 0.0159  0.0393  0.0172  258 GLN A O   
746  O O   B GLN A 258 ? 0.2717 0.3363 0.1842 0.0159  0.0386  0.0166  258 GLN A O   
747  C CB  A GLN A 258 ? 0.2490 0.3233 0.1779 0.0093  0.0423  0.0055  258 GLN A CB  
748  C CB  B GLN A 258 ? 0.2733 0.3474 0.2016 0.0097  0.0418  0.0054  258 GLN A CB  
749  C CG  A GLN A 258 ? 0.2511 0.3308 0.1902 0.0071  0.0441  0.0005  258 GLN A CG  
750  C CG  B GLN A 258 ? 0.3100 0.3842 0.2419 0.0110  0.0345  -0.0027 258 GLN A CG  
751  C CD  A GLN A 258 ? 0.2981 0.3845 0.2317 0.0123  0.0442  -0.0056 258 GLN A CD  
752  C CD  B GLN A 258 ? 0.3565 0.4338 0.2773 0.0153  0.0299  -0.0060 258 GLN A CD  
753  O OE1 A GLN A 258 ? 0.3121 0.3975 0.2355 0.0163  0.0408  -0.0088 258 GLN A OE1 
754  O OE1 B GLN A 258 ? 0.3678 0.4483 0.2823 0.0177  0.0298  -0.0117 258 GLN A OE1 
755  N NE2 A GLN A 258 ? 0.2951 0.3888 0.2350 0.0127  0.0480  -0.0079 258 GLN A NE2 
756  N NE2 B GLN A 258 ? 0.3545 0.4315 0.2724 0.0167  0.0259  -0.0030 258 GLN A NE2 
757  N N   . LYS A 259 ? 0.2677 0.3158 0.1902 0.0089  0.0428  0.0228  259 LYS A N   
758  C CA  . LYS A 259 ? 0.2836 0.3249 0.1951 0.0153  0.0419  0.0294  259 LYS A CA  
759  C C   . LYS A 259 ? 0.2833 0.3148 0.1993 0.0158  0.0400  0.0308  259 LYS A C   
760  O O   . LYS A 259 ? 0.2752 0.3001 0.1996 0.0093  0.0422  0.0295  259 LYS A O   
761  C CB  . LYS A 259 ? 0.3305 0.3637 0.2283 0.0157  0.0492  0.0383  259 LYS A CB  
762  C CG  . LYS A 259 ? 0.4121 0.4285 0.3093 0.0091  0.0558  0.0440  259 LYS A CG  
763  C CD  . LYS A 259 ? 0.4849 0.4915 0.3665 0.0082  0.0636  0.0534  259 LYS A CD  
764  C CE  . LYS A 259 ? 0.5506 0.5525 0.4159 0.0195  0.0618  0.0601  259 LYS A CE  
765  N NZ  . LYS A 259 ? 0.6085 0.6000 0.4572 0.0183  0.0700  0.0697  259 LYS A NZ  
766  N N   . ARG A 260 ? 0.2858 0.3183 0.1960 0.0242  0.0357  0.0332  260 ARG A N   
767  C CA  . ARG A 260 ? 0.2837 0.3084 0.1970 0.0271  0.0342  0.0347  260 ARG A CA  
768  C C   . ARG A 260 ? 0.3115 0.3154 0.2132 0.0289  0.0408  0.0436  260 ARG A C   
769  O O   . ARG A 260 ? 0.3327 0.3321 0.2202 0.0345  0.0433  0.0506  260 ARG A O   
770  C CB  . ARG A 260 ? 0.2868 0.3243 0.1987 0.0363  0.0272  0.0340  260 ARG A CB  
771  C CG  . ARG A 260 ? 0.3051 0.3400 0.2236 0.0393  0.0249  0.0334  260 ARG A CG  
772  C CD  . ARG A 260 ? 0.3359 0.3896 0.2556 0.0470  0.0178  0.0318  260 ARG A CD  
773  N NE  . ARG A 260 ? 0.3934 0.4471 0.2991 0.0588  0.0179  0.0397  260 ARG A NE  
774  C CZ  . ARG A 260 ? 0.4666 0.5391 0.3707 0.0676  0.0118  0.0400  260 ARG A CZ  
775  N NH1 . ARG A 260 ? 0.4554 0.5483 0.3717 0.0643  0.0054  0.0325  260 ARG A NH1 
776  N NH2 . ARG A 260 ? 0.4872 0.5590 0.3771 0.0796  0.0122  0.0482  260 ARG A NH2 
777  N N   . LEU A 261 ? 0.3132 0.3030 0.2192 0.0231  0.0441  0.0434  261 LEU A N   
778  C CA  . LEU A 261 ? 0.3456 0.3111 0.2392 0.0232  0.0508  0.0509  261 LEU A CA  
779  C C   . LEU A 261 ? 0.3557 0.3117 0.2426 0.0350  0.0488  0.0544  261 LEU A C   
780  O O   . LEU A 261 ? 0.3749 0.3114 0.2454 0.0414  0.0532  0.0627  261 LEU A O   
781  C CB  . LEU A 261 ? 0.3621 0.3169 0.2626 0.0103  0.0552  0.0479  261 LEU A CB  
782  C CG  . LEU A 261 ? 0.4021 0.3661 0.3088 -0.0014 0.0586  0.0456  261 LEU A CG  
783  C CD1 . LEU A 261 ? 0.4213 0.3753 0.3333 -0.0138 0.0628  0.0434  261 LEU A CD1 
784  C CD2 . LEU A 261 ? 0.4208 0.3811 0.3141 -0.0012 0.0641  0.0527  261 LEU A CD2 
785  N N   . ARG A 262 ? 0.3273 0.2951 0.2261 0.0378  0.0430  0.0484  262 ARG A N   
786  C CA  . ARG A 262 ? 0.3342 0.2964 0.2286 0.0496  0.0414  0.0509  262 ARG A CA  
787  C C   . ARG A 262 ? 0.3210 0.3094 0.2270 0.0553  0.0334  0.0457  262 ARG A C   
788  O O   . ARG A 262 ? 0.3073 0.3116 0.2268 0.0471  0.0297  0.0383  262 ARG A O   
789  C CB  . ARG A 262 ? 0.3622 0.3050 0.2583 0.0449  0.0451  0.0489  262 ARG A CB  
790  C CG  . ARG A 262 ? 0.4162 0.3324 0.3015 0.0358  0.0532  0.0528  262 ARG A CG  
791  C CD  . ARG A 262 ? 0.4374 0.3297 0.3175 0.0350  0.0570  0.0523  262 ARG A CD  
792  N NE  . ARG A 262 ? 0.4339 0.3125 0.3000 0.0514  0.0577  0.0581  262 ARG A NE  
793  C CZ  . ARG A 262 ? 0.4243 0.2759 0.2795 0.0549  0.0621  0.0594  262 ARG A CZ  
794  N NH1 . ARG A 262 ? 0.4035 0.2393 0.2603 0.0414  0.0658  0.0546  262 ARG A NH1 
795  N NH2 . ARG A 262 ? 0.4374 0.2778 0.2792 0.0725  0.0628  0.0651  262 ARG A NH2 
796  N N   . ASN A 263 ? 0.3233 0.3156 0.2236 0.0693  0.0311  0.0496  263 ASN A N   
797  C CA  . ASN A 263 ? 0.3271 0.3459 0.2386 0.0743  0.0240  0.0449  263 ASN A CA  
798  C C   . ASN A 263 ? 0.3451 0.3554 0.2535 0.0853  0.0255  0.0475  263 ASN A C   
799  O O   . ASN A 263 ? 0.3561 0.3654 0.2535 0.1002  0.0255  0.0541  263 ASN A O   
800  C CB  . ASN A 263 ? 0.3479 0.3890 0.2558 0.0817  0.0185  0.0468  263 ASN A CB  
801  C CG  . ASN A 263 ? 0.3818 0.4534 0.3034 0.0820  0.0109  0.0403  263 ASN A CG  
802  O OD1 . ASN A 263 ? 0.3791 0.4559 0.3139 0.0735  0.0097  0.0336  263 ASN A OD1 
803  N ND2 . ASN A 263 ? 0.4045 0.4977 0.3226 0.0915  0.0057  0.0424  263 ASN A ND2 
804  N N   . MET A 264 ? 0.3385 0.3410 0.2551 0.0785  0.0274  0.0426  264 MET A N   
805  C CA  . MET A 264 ? 0.3528 0.3427 0.2658 0.0870  0.0302  0.0436  264 MET A CA  
806  C C   . MET A 264 ? 0.3437 0.3609 0.2673 0.0952  0.0250  0.0405  264 MET A C   
807  O O   . MET A 264 ? 0.3258 0.3625 0.2648 0.0861  0.0212  0.0336  264 MET A O   
808  C CB  . MET A 264 ? 0.3647 0.3338 0.2803 0.0747  0.0348  0.0392  264 MET A CB  
809  C CG  . MET A 264 ? 0.3831 0.3252 0.2875 0.0662  0.0408  0.0427  264 MET A CG  
810  S SD  . MET A 264 ? 0.3737 0.2981 0.2832 0.0492  0.0449  0.0364  264 MET A SD  
811  C CE  . MET A 264 ? 0.3624 0.3170 0.2926 0.0370  0.0389  0.0289  264 MET A CE  
812  N N   . THR A 265 ? 0.3518 0.3701 0.2666 0.1130  0.0253  0.0461  265 THR A N   
813  C CA  . THR A 265 ? 0.3510 0.3976 0.2753 0.1227  0.0211  0.0440  265 THR A CA  
814  C C   . THR A 265 ? 0.3760 0.4044 0.2943 0.1329  0.0263  0.0448  265 THR A C   
815  O O   . THR A 265 ? 0.4199 0.4152 0.3209 0.1402  0.0323  0.0501  265 THR A O   
816  C CB  . THR A 265 ? 0.3791 0.4507 0.3001 0.1364  0.0160  0.0490  265 THR A CB  
817  O OG1 . THR A 265 ? 0.4091 0.4555 0.3096 0.1498  0.0203  0.0583  265 THR A OG1 
818  C CG2 . THR A 265 ? 0.3729 0.4664 0.3013 0.1248  0.0101  0.0458  265 THR A CG2 
819  N N   . SER A 266 ? 0.3472 0.3956 0.2787 0.1323  0.0244  0.0392  266 SER A N   
820  C CA  . SER A 266 ? 0.3443 0.3812 0.2721 0.1422  0.0289  0.0383  266 SER A CA  
821  C C   . SER A 266 ? 0.3231 0.3956 0.2690 0.1409  0.0252  0.0323  266 SER A C   
822  O O   . SER A 266 ? 0.3214 0.4028 0.2666 0.1557  0.0268  0.0330  266 SER A O   
823  C CB  . SER A 266 ? 0.3575 0.3566 0.2778 0.1313  0.0351  0.0357  266 SER A CB  
824  O OG  . SER A 266 ? 0.3499 0.3583 0.2848 0.1117  0.0328  0.0286  266 SER A OG  
825  N N   . HIS A 267 ? 0.3023 0.3957 0.2638 0.1235  0.0206  0.0267  267 HIS A N   
826  C CA  . HIS A 267 ? 0.2907 0.4164 0.2688 0.1186  0.0174  0.0212  267 HIS A CA  
827  C C   . HIS A 267 ? 0.2880 0.4544 0.2738 0.1281  0.0119  0.0228  267 HIS A C   
828  O O   . HIS A 267 ? 0.2911 0.4641 0.2717 0.1340  0.0087  0.0271  267 HIS A O   
829  C CB  . HIS A 267 ? 0.2836 0.4116 0.2726 0.0966  0.0151  0.0151  267 HIS A CB  
830  C CG  . HIS A 267 ? 0.2844 0.3853 0.2709 0.0881  0.0199  0.0119  267 HIS A CG  
831  N ND1 . HIS A 267 ? 0.2906 0.3924 0.2793 0.0918  0.0230  0.0092  267 HIS A ND1 
832  C CD2 . HIS A 267 ? 0.2904 0.3660 0.2728 0.0763  0.0217  0.0107  267 HIS A CD2 
833  C CE1 . HIS A 267 ? 0.3087 0.3850 0.2938 0.0817  0.0262  0.0064  267 HIS A CE1 
834  N NE2 . HIS A 267 ? 0.2948 0.3558 0.2767 0.0721  0.0254  0.0072  267 HIS A NE2 
835  N N   . SER A 268 ? 0.2789 0.4742 0.2769 0.1295  0.0110  0.0194  268 SER A N   
836  C CA  . SER A 268 ? 0.2737 0.5138 0.2816 0.1366  0.0058  0.0199  268 SER A CA  
837  C C   . SER A 268 ? 0.2569 0.5257 0.2804 0.1162  0.0000  0.0139  268 SER A C   
838  O O   . SER A 268 ? 0.2650 0.5733 0.2979 0.1177  -0.0049 0.0132  268 SER A O   
839  C CB  . SER A 268 ? 0.2858 0.5437 0.2973 0.1519  0.0089  0.0202  268 SER A CB  
840  O OG  . SER A 268 ? 0.3145 0.5702 0.3340 0.1404  0.0121  0.0145  268 SER A OG  
841  N N   . ALA A 269 ? 0.2330 0.4823 0.2584 0.0972  0.0005  0.0096  269 ALA A N   
842  C CA  . ALA A 269 ? 0.1976 0.4662 0.2345 0.0776  -0.0040 0.0039  269 ALA A CA  
843  C C   . ALA A 269 ? 0.1896 0.4266 0.2220 0.0621  -0.0033 0.0014  269 ALA A C   
844  O O   . ALA A 269 ? 0.2016 0.4065 0.2239 0.0661  0.0006  0.0040  269 ALA A O   
845  C CB  . ALA A 269 ? 0.1861 0.4762 0.2349 0.0721  -0.0025 0.0002  269 ALA A CB  
846  N N   . ARG A 270 ? 0.1746 0.4206 0.2135 0.0449  -0.0069 -0.0035 270 ARG A N   
847  C CA  . ARG A 270 ? 0.1802 0.3996 0.2147 0.0325  -0.0066 -0.0057 270 ARG A CA  
848  C C   . ARG A 270 ? 0.1814 0.3712 0.2126 0.0309  -0.0011 -0.0055 270 ARG A C   
849  O O   . ARG A 270 ? 0.1705 0.3619 0.2055 0.0321  0.0019  -0.0062 270 ARG A O   
850  C CB  . ARG A 270 ? 0.1997 0.4314 0.2404 0.0151  -0.0106 -0.0113 270 ARG A CB  
851  C CG  . ARG A 270 ? 0.2163 0.4541 0.2651 0.0054  -0.0088 -0.0143 270 ARG A CG  
852  C CD  . ARG A 270 ? 0.2222 0.4601 0.2726 -0.0128 -0.0118 -0.0193 270 ARG A CD  
853  N NE  . ARG A 270 ? 0.1962 0.4340 0.2518 -0.0228 -0.0093 -0.0212 270 ARG A NE  
854  C CZ  . ARG A 270 ? 0.2281 0.4699 0.2856 -0.0389 -0.0111 -0.0251 270 ARG A CZ  
855  N NH1 . ARG A 270 ? 0.2108 0.4501 0.2712 -0.0471 -0.0083 -0.0258 270 ARG A NH1 
856  N NH2 . ARG A 270 ? 0.2235 0.4691 0.2779 -0.0471 -0.0155 -0.0284 270 ARG A NH2 
857  N N   . VAL A 271 ? 0.1725 0.3371 0.1964 0.0278  0.0000  -0.0048 271 VAL A N   
858  C CA  . VAL A 271 ? 0.1789 0.3170 0.1994 0.0252  0.0046  -0.0048 271 VAL A CA  
859  C C   . VAL A 271 ? 0.1610 0.2935 0.1854 0.0103  0.0033  -0.0091 271 VAL A C   
860  O O   . VAL A 271 ? 0.1648 0.2883 0.1859 0.0054  0.0020  -0.0097 271 VAL A O   
861  C CB  . VAL A 271 ? 0.2115 0.3269 0.2212 0.0319  0.0073  -0.0007 271 VAL A CB  
862  C CG1 . VAL A 271 ? 0.2203 0.3102 0.2268 0.0266  0.0116  -0.0015 271 VAL A CG1 
863  C CG2 . VAL A 271 ? 0.2331 0.3504 0.2363 0.0481  0.0090  0.0042  271 VAL A CG2 
864  N N   . GLY A 272 ? 0.1357 0.2740 0.1661 0.0041  0.0038  -0.0117 272 GLY A N   
865  C CA  . GLY A 272 ? 0.1486 0.2816 0.1814 -0.0090 0.0026  -0.0150 272 GLY A CA  
866  C C   . GLY A 272 ? 0.1526 0.2637 0.1825 -0.0119 0.0056  -0.0152 272 GLY A C   
867  O O   . GLY A 272 ? 0.1571 0.2616 0.1874 -0.0207 0.0046  -0.0172 272 GLY A O   
868  N N   . SER A 273 ? 0.1488 0.2480 0.1749 -0.0046 0.0091  -0.0132 273 SER A N   
869  C CA  . SER A 273 ? 0.1517 0.2328 0.1753 -0.0084 0.0115  -0.0140 273 SER A CA  
870  C C   . SER A 273 ? 0.1654 0.2297 0.1820 -0.0030 0.0146  -0.0117 273 SER A C   
871  O O   . SER A 273 ? 0.1703 0.2339 0.1827 0.0061  0.0161  -0.0092 273 SER A O   
872  C CB  . SER A 273 ? 0.1858 0.2691 0.2116 -0.0101 0.0134  -0.0156 273 SER A CB  
873  O OG  . SER A 273 ? 0.2226 0.3091 0.2465 -0.0006 0.0161  -0.0146 273 SER A OG  
874  N N   . LEU A 274 ? 0.1630 0.2143 0.1780 -0.0087 0.0154  -0.0124 274 LEU A N   
875  C CA  . LEU A 274 ? 0.1693 0.2048 0.1777 -0.0069 0.0186  -0.0105 274 LEU A CA  
876  C C   . LEU A 274 ? 0.1657 0.1915 0.1742 -0.0141 0.0200  -0.0127 274 LEU A C   
877  O O   . LEU A 274 ? 0.1707 0.2020 0.1841 -0.0200 0.0176  -0.0146 274 LEU A O   
878  C CB  . LEU A 274 ? 0.1684 0.2037 0.1750 -0.0073 0.0176  -0.0086 274 LEU A CB  
879  C CG  . LEU A 274 ? 0.1687 0.2139 0.1736 -0.0004 0.0158  -0.0062 274 LEU A CG  
880  C CD1 . LEU A 274 ? 0.1843 0.2309 0.1877 -0.0027 0.0144  -0.0057 274 LEU A CD1 
881  C CD2 . LEU A 274 ? 0.1780 0.2148 0.1748 0.0095  0.0190  -0.0021 274 LEU A CD2 
882  N N   . SER A 275 ? 0.1645 0.1755 0.1665 -0.0138 0.0236  -0.0122 275 SER A N   
883  C CA  . SER A 275 ? 0.1667 0.1707 0.1686 -0.0219 0.0247  -0.0146 275 SER A CA  
884  C C   . SER A 275 ? 0.2058 0.1929 0.1993 -0.0234 0.0289  -0.0133 275 SER A C   
885  O O   . SER A 275 ? 0.2246 0.1993 0.2099 -0.0177 0.0319  -0.0121 275 SER A O   
886  C CB  . SER A 275 ? 0.1796 0.1846 0.1824 -0.0237 0.0244  -0.0180 275 SER A CB  
887  O OG  . SER A 275 ? 0.2030 0.2038 0.2057 -0.0318 0.0246  -0.0205 275 SER A OG  
888  N N   . TRP A 276 ? 0.2067 0.1930 0.2016 -0.0312 0.0294  -0.0135 276 TRP A N   
889  C CA  . TRP A 276 ? 0.2203 0.1911 0.2072 -0.0356 0.0338  -0.0123 276 TRP A CA  
890  C C   . TRP A 276 ? 0.2449 0.2073 0.2289 -0.0440 0.0353  -0.0166 276 TRP A C   
891  O O   . TRP A 276 ? 0.2386 0.2124 0.2294 -0.0486 0.0323  -0.0200 276 TRP A O   
892  C CB  . TRP A 276 ? 0.2115 0.1895 0.2021 -0.0408 0.0340  -0.0105 276 TRP A CB  
893  C CG  . TRP A 276 ? 0.2046 0.1875 0.1948 -0.0341 0.0336  -0.0065 276 TRP A CG  
894  C CD1 . TRP A 276 ? 0.2142 0.2122 0.2113 -0.0305 0.0296  -0.0068 276 TRP A CD1 
895  C CD2 . TRP A 276 ? 0.2142 0.1860 0.1953 -0.0316 0.0374  -0.0017 276 TRP A CD2 
896  N NE1 . TRP A 276 ? 0.2166 0.2153 0.2098 -0.0259 0.0304  -0.0031 276 TRP A NE1 
897  C CE2 . TRP A 276 ? 0.2210 0.2043 0.2044 -0.0257 0.0351  0.0005  276 TRP A CE2 
898  C CE3 . TRP A 276 ? 0.2289 0.1801 0.1983 -0.0334 0.0427  0.0010  276 TRP A CE3 
899  C CZ2 . TRP A 276 ? 0.2374 0.2149 0.2126 -0.0219 0.0378  0.0056  276 TRP A CZ2 
900  C CZ3 . TRP A 276 ? 0.2402 0.1834 0.2007 -0.0293 0.0457  0.0067  276 TRP A CZ3 
901  C CH2 . TRP A 276 ? 0.2364 0.1938 0.2001 -0.0230 0.0431  0.0091  276 TRP A CH2 
902  N N   . ASN A 277 ? 0.2651 0.2065 0.2375 -0.0466 0.0400  -0.0162 277 ASN A N   
903  C CA  . ASN A 277 ? 0.2886 0.2185 0.2554 -0.0570 0.0422  -0.0206 277 ASN A CA  
904  C C   . ASN A 277 ? 0.3065 0.2212 0.2649 -0.0640 0.0471  -0.0176 277 ASN A C   
905  O O   . ASN A 277 ? 0.3211 0.2123 0.2659 -0.0597 0.0515  -0.0152 277 ASN A O   
906  C CB  . ASN A 277 ? 0.3252 0.2376 0.2816 -0.0520 0.0442  -0.0235 277 ASN A CB  
907  C CG  . ASN A 277 ? 0.4151 0.3146 0.3640 -0.0635 0.0462  -0.0293 277 ASN A CG  
908  O OD1 . ASN A 277 ? 0.4378 0.3484 0.3928 -0.0755 0.0444  -0.0319 277 ASN A OD1 
909  N ND2 . ASN A 277 ? 0.4389 0.3154 0.3740 -0.0597 0.0497  -0.0318 277 ASN A ND2 
910  N N   . SER A 278 ? 0.3012 0.2297 0.2670 -0.0738 0.0467  -0.0173 278 SER A N   
911  C CA  . SER A 278 ? 0.3143 0.2322 0.2733 -0.0815 0.0518  -0.0138 278 SER A CA  
912  C C   . SER A 278 ? 0.3151 0.2243 0.2676 -0.0696 0.0539  -0.0068 278 SER A C   
913  O O   . SER A 278 ? 0.3089 0.2360 0.2704 -0.0609 0.0501  -0.0051 278 SER A O   
914  C CB  . SER A 278 ? 0.3507 0.2450 0.2968 -0.0935 0.0564  -0.0171 278 SER A CB  
915  O OG  . SER A 278 ? 0.4147 0.2950 0.3518 -0.1014 0.0622  -0.0130 278 SER A OG  
916  N N   A TYR A 279 ? 0.3248 0.2066 0.2610 -0.0686 0.0596  -0.0030 279 TYR A N   
917  N N   B TYR A 279 ? 0.3251 0.2069 0.2613 -0.0685 0.0595  -0.0030 279 TYR A N   
918  C CA  A TYR A 279 ? 0.3367 0.2104 0.2651 -0.0566 0.0613  0.0041  279 TYR A CA  
919  C CA  B TYR A 279 ? 0.3358 0.2105 0.2648 -0.0562 0.0611  0.0040  279 TYR A CA  
920  C C   A TYR A 279 ? 0.3357 0.2036 0.2600 -0.0402 0.0594  0.0049  279 TYR A C   
921  C C   B TYR A 279 ? 0.3349 0.2031 0.2594 -0.0401 0.0593  0.0048  279 TYR A C   
922  O O   A TYR A 279 ? 0.3472 0.2108 0.2650 -0.0288 0.0601  0.0107  279 TYR A O   
923  O O   B TYR A 279 ? 0.3449 0.2091 0.2631 -0.0287 0.0600  0.0107  279 TYR A O   
924  C CB  A TYR A 279 ? 0.3612 0.2079 0.2725 -0.0624 0.0687  0.0092  279 TYR A CB  
925  C CB  B TYR A 279 ? 0.3588 0.2080 0.2714 -0.0617 0.0683  0.0094  279 TYR A CB  
926  C CG  A TYR A 279 ? 0.3954 0.2115 0.2919 -0.0696 0.0732  0.0061  279 TYR A CG  
927  C CG  B TYR A 279 ? 0.3708 0.2339 0.2895 -0.0744 0.0701  0.0109  279 TYR A CG  
928  C CD1 A TYR A 279 ? 0.4241 0.2169 0.3075 -0.0573 0.0745  0.0063  279 TYR A CD1 
929  C CD1 B TYR A 279 ? 0.3778 0.2602 0.3033 -0.0689 0.0687  0.0151  279 TYR A CD1 
930  C CD2 A TYR A 279 ? 0.4152 0.2259 0.3100 -0.0887 0.0763  0.0026  279 TYR A CD2 
931  C CD2 B TYR A 279 ? 0.3888 0.2483 0.3069 -0.0922 0.0733  0.0075  279 TYR A CD2 
932  C CE1 A TYR A 279 ? 0.4540 0.2160 0.3217 -0.0632 0.0789  0.0025  279 TYR A CE1 
933  C CE1 B TYR A 279 ? 0.3853 0.2820 0.3162 -0.0794 0.0711  0.0164  279 TYR A CE1 
934  C CE2 A TYR A 279 ? 0.4435 0.2245 0.3231 -0.0967 0.0803  -0.0014 279 TYR A CE2 
935  C CE2 B TYR A 279 ? 0.3926 0.2692 0.3177 -0.1038 0.0754  0.0089  279 TYR A CE2 
936  C CZ  A TYR A 279 ? 0.4713 0.2258 0.3364 -0.0837 0.0819  -0.0015 279 TYR A CZ  
937  C CZ  B TYR A 279 ? 0.3990 0.2941 0.3304 -0.0967 0.0745  0.0135  279 TYR A CZ  
938  O OH  A TYR A 279 ? 0.5145 0.2361 0.3620 -0.0909 0.0863  -0.0060 279 TYR A OH  
939  O OH  B TYR A 279 ? 0.4143 0.3279 0.3525 -0.1070 0.0771  0.0147  279 TYR A OH  
940  N N   . ILE A 280 ? 0.3222 0.1915 0.2497 -0.0387 0.0570  -0.0008 280 ILE A N   
941  C CA  . ILE A 280 ? 0.3184 0.1873 0.2439 -0.0236 0.0554  -0.0005 280 ILE A CA  
942  C C   . ILE A 280 ? 0.2944 0.1953 0.2373 -0.0199 0.0489  -0.0016 280 ILE A C   
943  O O   . ILE A 280 ? 0.2851 0.2013 0.2392 -0.0283 0.0458  -0.0060 280 ILE A O   
944  C CB  . ILE A 280 ? 0.3438 0.1988 0.2632 -0.0240 0.0567  -0.0063 280 ILE A CB  
945  C CG1 . ILE A 280 ? 0.3947 0.2122 0.2931 -0.0263 0.0637  -0.0054 280 ILE A CG1 
946  C CG2 . ILE A 280 ? 0.3446 0.2105 0.2676 -0.0090 0.0541  -0.0069 280 ILE A CG2 
947  C CD1 . ILE A 280 ? 0.4394 0.2388 0.3236 -0.0110 0.0671  0.0018  280 ILE A CD1 
948  N N   . LEU A 281 ? 0.2768 0.1870 0.2208 -0.0077 0.0469  0.0023  281 LEU A N   
949  C CA  . LEU A 281 ? 0.2560 0.1933 0.2141 -0.0049 0.0411  0.0008  281 LEU A CA  
950  C C   . LEU A 281 ? 0.2617 0.2030 0.2197 0.0058  0.0400  -0.0003 281 LEU A C   
951  O O   . LEU A 281 ? 0.2800 0.2121 0.2286 0.0172  0.0422  0.0035  281 LEU A O   
952  C CB  . LEU A 281 ? 0.2524 0.1995 0.2111 0.0000  0.0396  0.0056  281 LEU A CB  
953  C CG  . LEU A 281 ? 0.2517 0.2239 0.2216 0.0039  0.0338  0.0043  281 LEU A CG  
954  C CD1 . LEU A 281 ? 0.2396 0.2247 0.2213 -0.0061 0.0307  -0.0006 281 LEU A CD1 
955  C CD2 . LEU A 281 ? 0.2632 0.2425 0.2307 0.0084  0.0327  0.0086  281 LEU A CD2 
956  N N   . SER A 282 ? 0.2338 0.1893 0.2014 0.0030  0.0370  -0.0049 282 SER A N   
957  C CA  . SER A 282 ? 0.2253 0.1894 0.1945 0.0124  0.0362  -0.0060 282 SER A CA  
958  C C   . SER A 282 ? 0.2081 0.1982 0.1884 0.0148  0.0313  -0.0053 282 SER A C   
959  O O   . SER A 282 ? 0.1931 0.1942 0.1817 0.0065  0.0280  -0.0068 282 SER A O   
960  C CB  . SER A 282 ? 0.2518 0.2143 0.2227 0.0074  0.0367  -0.0115 282 SER A CB  
961  O OG  . SER A 282 ? 0.2838 0.2215 0.2434 0.0029  0.0410  -0.0131 282 SER A OG  
962  N N   . SER A 283 ? 0.2093 0.2096 0.1892 0.0263  0.0307  -0.0033 283 SER A N   
963  C CA  . SER A 283 ? 0.2118 0.2381 0.2014 0.0279  0.0260  -0.0029 283 SER A CA  
964  C C   . SER A 283 ? 0.2132 0.2566 0.2080 0.0338  0.0255  -0.0046 283 SER A C   
965  O O   . SER A 283 ? 0.2186 0.2557 0.2069 0.0445  0.0288  -0.0036 283 SER A O   
966  C CB  . SER A 283 ? 0.2331 0.2624 0.2179 0.0362  0.0251  0.0021  283 SER A CB  
967  O OG  . SER A 283 ? 0.2708 0.2897 0.2453 0.0498  0.0285  0.0057  283 SER A OG  
968  N N   . GLY A 284 ? 0.2076 0.2719 0.2132 0.0269  0.0218  -0.0071 284 GLY A N   
969  C CA  . GLY A 284 ? 0.2112 0.2961 0.2233 0.0301  0.0214  -0.0087 284 GLY A CA  
970  C C   . GLY A 284 ? 0.2199 0.3308 0.2389 0.0318  0.0172  -0.0075 284 GLY A C   
971  O O   . GLY A 284 ? 0.2222 0.3365 0.2435 0.0246  0.0137  -0.0076 284 GLY A O   
972  N N   . SER A 285 ? 0.2096 0.3401 0.2316 0.0413  0.0176  -0.0068 285 SER A N   
973  C CA  . SER A 285 ? 0.2102 0.3691 0.2386 0.0442  0.0135  -0.0057 285 SER A CA  
974  C C   . SER A 285 ? 0.1952 0.3840 0.2348 0.0397  0.0124  -0.0083 285 SER A C   
975  O O   . SER A 285 ? 0.1770 0.3654 0.2181 0.0393  0.0158  -0.0100 285 SER A O   
976  C CB  . SER A 285 ? 0.2373 0.3981 0.2589 0.0624  0.0146  -0.0012 285 SER A CB  
977  O OG  . SER A 285 ? 0.2620 0.4546 0.2900 0.0666  0.0102  0.0000  285 SER A OG  
978  N N   . ARG A 286 ? 0.1912 0.4067 0.2380 0.0354  0.0077  -0.0088 286 ARG A N   
979  C CA  . ARG A 286 ? 0.1986 0.4473 0.2565 0.0300  0.0064  -0.0110 286 ARG A CA  
980  C C   . ARG A 286 ? 0.2106 0.4768 0.2705 0.0460  0.0099  -0.0093 286 ARG A C   
981  O O   . ARG A 286 ? 0.2025 0.4913 0.2706 0.0423  0.0114  -0.0111 286 ARG A O   
982  C CB  . ARG A 286 ? 0.2211 0.4947 0.2842 0.0240  0.0004  -0.0118 286 ARG A CB  
983  C CG  . ARG A 286 ? 0.2632 0.5717 0.3379 0.0132  -0.0015 -0.0147 286 ARG A CG  
984  C CD  . ARG A 286 ? 0.3170 0.6491 0.3950 0.0074  -0.0078 -0.0161 286 ARG A CD  
985  N NE  . ARG A 286 ? 0.3744 0.7111 0.4561 -0.0142 -0.0102 -0.0207 286 ARG A NE  
986  C CZ  . ARG A 286 ? 0.4264 0.7684 0.5065 -0.0244 -0.0154 -0.0235 286 ARG A CZ  
987  N NH1 . ARG A 286 ? 0.3857 0.7318 0.4617 -0.0148 -0.0191 -0.0221 286 ARG A NH1 
988  N NH2 . ARG A 286 ? 0.4598 0.8016 0.5410 -0.0443 -0.0168 -0.0278 286 ARG A NH2 
989  N N   . SER A 287 ? 0.2235 0.4781 0.2747 0.0641  0.0119  -0.0056 287 SER A N   
990  C CA  . SER A 287 ? 0.2223 0.4881 0.2723 0.0825  0.0158  -0.0038 287 SER A CA  
991  C C   . SER A 287 ? 0.2313 0.4792 0.2776 0.0829  0.0219  -0.0062 287 SER A C   
992  O O   . SER A 287 ? 0.2400 0.5001 0.2862 0.0966  0.0257  -0.0060 287 SER A O   
993  C CB  . SER A 287 ? 0.2496 0.4978 0.2871 0.1012  0.0168  0.0011  287 SER A CB  
994  O OG  . SER A 287 ? 0.2892 0.4938 0.3142 0.0989  0.0202  0.0014  287 SER A OG  
995  N N   . GLY A 288 ? 0.2224 0.4419 0.2645 0.0696  0.0229  -0.0084 288 GLY A N   
996  C CA  . GLY A 288 ? 0.2273 0.4279 0.2643 0.0683  0.0280  -0.0111 288 GLY A CA  
997  C C   . GLY A 288 ? 0.2358 0.3982 0.2577 0.0770  0.0317  -0.0103 288 GLY A C   
998  O O   . GLY A 288 ? 0.2561 0.3992 0.2718 0.0748  0.0355  -0.0132 288 GLY A O   
999  N N   . HIS A 289 ? 0.2189 0.3697 0.2334 0.0865  0.0308  -0.0064 289 HIS A N   
1000 C CA  . HIS A 289 ? 0.2369 0.3493 0.2353 0.0934  0.0349  -0.0052 289 HIS A CA  
1001 C C   . HIS A 289 ? 0.2331 0.3217 0.2287 0.0781  0.0333  -0.0058 289 HIS A C   
1002 O O   . HIS A 289 ? 0.2254 0.3257 0.2291 0.0674  0.0287  -0.0055 289 HIS A O   
1003 C CB  . HIS A 289 ? 0.2713 0.3798 0.2606 0.1118  0.0356  0.0002  289 HIS A CB  
1004 C CG  . HIS A 289 ? 0.3074 0.4395 0.2984 0.1302  0.0374  0.0013  289 HIS A CG  
1005 N ND1 . HIS A 289 ? 0.3589 0.4780 0.3413 0.1411  0.0435  -0.0009 289 HIS A ND1 
1006 C CD2 . HIS A 289 ? 0.3116 0.4807 0.3118 0.1394  0.0340  0.0040  289 HIS A CD2 
1007 C CE1 . HIS A 289 ? 0.3548 0.5038 0.3418 0.1578  0.0439  0.0008  289 HIS A CE1 
1008 N NE2 . HIS A 289 ? 0.3289 0.5103 0.3273 0.1571  0.0380  0.0039  289 HIS A NE2 
1009 N N   . ILE A 290 ? 0.2379 0.2932 0.2212 0.0772  0.0374  -0.0071 290 ILE A N   
1010 C CA  . ILE A 290 ? 0.2349 0.2671 0.2140 0.0648  0.0369  -0.0073 290 ILE A CA  
1011 C C   . ILE A 290 ? 0.2557 0.2593 0.2190 0.0740  0.0406  -0.0036 290 ILE A C   
1012 O O   . ILE A 290 ? 0.2693 0.2562 0.2208 0.0853  0.0453  -0.0037 290 ILE A O   
1013 C CB  . ILE A 290 ? 0.2406 0.2601 0.2190 0.0527  0.0385  -0.0126 290 ILE A CB  
1014 C CG1 . ILE A 290 ? 0.2295 0.2742 0.2222 0.0420  0.0347  -0.0152 290 ILE A CG1 
1015 C CG2 . ILE A 290 ? 0.2535 0.2478 0.2255 0.0421  0.0390  -0.0128 290 ILE A CG2 
1016 C CD1 . ILE A 290 ? 0.2546 0.2943 0.2457 0.0363  0.0370  -0.0200 290 ILE A CD1 
1017 N N   . HIS A 291 ? 0.2512 0.2468 0.2124 0.0691  0.0390  -0.0001 291 HIS A N   
1018 C CA  . HIS A 291 ? 0.2756 0.2415 0.2202 0.0757  0.0430  0.0042  291 HIS A CA  
1019 C C   . HIS A 291 ? 0.2916 0.2364 0.2327 0.0599  0.0443  0.0027  291 HIS A C   
1020 O O   . HIS A 291 ? 0.2834 0.2421 0.2359 0.0474  0.0405  0.0010  291 HIS A O   
1021 C CB  . HIS A 291 ? 0.2856 0.2623 0.2291 0.0849  0.0405  0.0107  291 HIS A CB  
1022 C CG  . HIS A 291 ? 0.3043 0.3010 0.2486 0.1031  0.0396  0.0134  291 HIS A CG  
1023 N ND1 . HIS A 291 ? 0.3235 0.3335 0.2663 0.1133  0.0369  0.0192  291 HIS A ND1 
1024 C CD2 . HIS A 291 ? 0.3034 0.3120 0.2503 0.1127  0.0410  0.0109  291 HIS A CD2 
1025 C CE1 . HIS A 291 ? 0.3226 0.3525 0.2675 0.1290  0.0364  0.0202  291 HIS A CE1 
1026 N NE2 . HIS A 291 ? 0.3055 0.3356 0.2532 0.1295  0.0392  0.0153  291 HIS A NE2 
1027 N N   . HIS A 292 ? 0.3046 0.2160 0.2295 0.0604  0.0497  0.0033  292 HIS A N   
1028 C CA  . HIS A 292 ? 0.3218 0.2138 0.2421 0.0455  0.0515  0.0026  292 HIS A CA  
1029 C C   . HIS A 292 ? 0.3327 0.2121 0.2428 0.0503  0.0533  0.0101  292 HIS A C   
1030 O O   . HIS A 292 ? 0.3523 0.2138 0.2475 0.0644  0.0570  0.0145  292 HIS A O   
1031 C CB  . HIS A 292 ? 0.3561 0.2173 0.2627 0.0410  0.0568  -0.0016 292 HIS A CB  
1032 C CG  . HIS A 292 ? 0.3553 0.2264 0.2698 0.0342  0.0554  -0.0091 292 HIS A CG  
1033 N ND1 . HIS A 292 ? 0.3448 0.2448 0.2773 0.0254  0.0500  -0.0115 292 HIS A ND1 
1034 C CD2 . HIS A 292 ? 0.3777 0.2312 0.2824 0.0345  0.0589  -0.0144 292 HIS A CD2 
1035 C CE1 . HIS A 292 ? 0.3562 0.2567 0.2896 0.0214  0.0502  -0.0175 292 HIS A CE1 
1036 N NE2 . HIS A 292 ? 0.3726 0.2466 0.2899 0.0263  0.0554  -0.0198 292 HIS A NE2 
1037 N N   . HIS A 293 ? 0.3145 0.2010 0.2307 0.0392  0.0514  0.0115  293 HIS A N   
1038 C CA  . HIS A 293 ? 0.3217 0.1975 0.2283 0.0414  0.0534  0.0185  293 HIS A CA  
1039 C C   . HIS A 293 ? 0.3492 0.2028 0.2486 0.0259  0.0578  0.0183  293 HIS A C   
1040 O O   . HIS A 293 ? 0.3459 0.2121 0.2572 0.0119  0.0557  0.0139  293 HIS A O   
1041 C CB  . HIS A 293 ? 0.2959 0.2010 0.2150 0.0413  0.0479  0.0205  293 HIS A CB  
1042 C CG  . HIS A 293 ? 0.2855 0.2181 0.2146 0.0518  0.0427  0.0196  293 HIS A CG  
1043 N ND1 . HIS A 293 ? 0.3177 0.2541 0.2398 0.0686  0.0424  0.0249  293 HIS A ND1 
1044 C CD2 . HIS A 293 ? 0.2739 0.2311 0.2187 0.0472  0.0381  0.0142  293 HIS A CD2 
1045 C CE1 . HIS A 293 ? 0.3066 0.2725 0.2417 0.0726  0.0374  0.0220  293 HIS A CE1 
1046 N NE2 . HIS A 293 ? 0.2921 0.2699 0.2406 0.0595  0.0349  0.0156  293 HIS A NE2 
1047 N N   . ASP A 294 ? 0.3690 0.1905 0.2488 0.0282  0.0640  0.0232  294 ASP A N   
1048 C CA  . ASP A 294 ? 0.3823 0.1852 0.2552 0.0120  0.0685  0.0237  294 ASP A CA  
1049 C C   . ASP A 294 ? 0.3722 0.1880 0.2471 0.0132  0.0675  0.0303  294 ASP A C   
1050 O O   . ASP A 294 ? 0.3828 0.1849 0.2435 0.0243  0.0701  0.0378  294 ASP A O   
1051 C CB  . ASP A 294 ? 0.4279 0.1876 0.2766 0.0127  0.0762  0.0262  294 ASP A CB  
1052 C CG  . ASP A 294 ? 0.5052 0.2465 0.3465 -0.0068 0.0813  0.0266  294 ASP A CG  
1053 O OD1 . ASP A 294 ? 0.5011 0.2639 0.3544 -0.0168 0.0795  0.0277  294 ASP A OD1 
1054 O OD2 . ASP A 294 ? 0.5431 0.2489 0.3662 -0.0124 0.0874  0.0257  294 ASP A OD2 
1055 N N   . VAL A 295 ? 0.3506 0.1930 0.2420 0.0034  0.0636  0.0276  295 VAL A N   
1056 C CA  . VAL A 295 ? 0.3499 0.2073 0.2436 0.0053  0.0623  0.0327  295 VAL A CA  
1057 C C   . VAL A 295 ? 0.3885 0.2244 0.2669 -0.0007 0.0690  0.0394  295 VAL A C   
1058 O O   . VAL A 295 ? 0.3933 0.2373 0.2690 0.0036  0.0689  0.0449  295 VAL A O   
1059 C CB  . VAL A 295 ? 0.3340 0.2229 0.2475 -0.0025 0.0570  0.0276  295 VAL A CB  
1060 C CG1 . VAL A 295 ? 0.3261 0.2334 0.2528 0.0022  0.0510  0.0217  295 VAL A CG1 
1061 C CG2 . VAL A 295 ? 0.3342 0.2218 0.2523 -0.0197 0.0597  0.0243  295 VAL A CG2 
1062 N N   . ARG A 296 ? 0.4083 0.2158 0.2750 -0.0106 0.0752  0.0391  296 ARG A N   
1063 C CA  . ARG A 296 ? 0.4358 0.2209 0.2867 -0.0187 0.0824  0.0456  296 ARG A CA  
1064 C C   . ARG A 296 ? 0.4610 0.2156 0.2882 -0.0047 0.0870  0.0545  296 ARG A C   
1065 O O   . ARG A 296 ? 0.4853 0.2216 0.2975 -0.0093 0.0930  0.0618  296 ARG A O   
1066 C CB  . ARG A 296 ? 0.4739 0.2394 0.3201 -0.0376 0.0876  0.0413  296 ARG A CB  
1067 C CG  . ARG A 296 ? 0.4977 0.2893 0.3648 -0.0510 0.0834  0.0322  296 ARG A CG  
1068 C CD  . ARG A 296 ? 0.5475 0.3170 0.4072 -0.0670 0.0877  0.0271  296 ARG A CD  
1069 N NE  . ARG A 296 ? 0.5742 0.3155 0.4201 -0.0582 0.0889  0.0250  296 ARG A NE  
1070 C CZ  . ARG A 296 ? 0.5963 0.3056 0.4268 -0.0684 0.0941  0.0220  296 ARG A CZ  
1071 N NH1 . ARG A 296 ? 0.5769 0.2604 0.3938 -0.0578 0.0954  0.0201  296 ARG A NH1 
1072 N NH2 . ARG A 296 ? 0.5854 0.2890 0.4136 -0.0897 0.0982  0.0205  296 ARG A NH2 
1073 N N   . VAL A 297 ? 0.4643 0.2119 0.2866 0.0122  0.0848  0.0544  297 VAL A N   
1074 C CA  . VAL A 297 ? 0.5092 0.2246 0.3069 0.0272  0.0895  0.0629  297 VAL A CA  
1075 C C   . VAL A 297 ? 0.5061 0.2393 0.3042 0.0500  0.0846  0.0681  297 VAL A C   
1076 O O   . VAL A 297 ? 0.4687 0.2365 0.2862 0.0550  0.0772  0.0632  297 VAL A O   
1077 C CB  . VAL A 297 ? 0.5421 0.2227 0.3257 0.0282  0.0940  0.0594  297 VAL A CB  
1078 C CG1 . VAL A 297 ? 0.5643 0.2272 0.3456 0.0039  0.0988  0.0542  297 VAL A CG1 
1079 C CG2 . VAL A 297 ? 0.5380 0.2377 0.3351 0.0388  0.0882  0.0521  297 VAL A CG2 
1080 N N   . ALA A 298 ? 0.5248 0.2335 0.3002 0.0634  0.0888  0.0783  298 ALA A N   
1081 C CA  . ALA A 298 ? 0.5311 0.2542 0.3027 0.0862  0.0847  0.0848  298 ALA A CA  
1082 C C   . ALA A 298 ? 0.5279 0.2700 0.3103 0.1017  0.0790  0.0796  298 ALA A C   
1083 O O   . ALA A 298 ? 0.5225 0.3036 0.3224 0.1074  0.0715  0.0773  298 ALA A O   
1084 C CB  . ALA A 298 ? 0.5557 0.2407 0.2970 0.0982  0.0915  0.0967  298 ALA A CB  
1085 N N   . GLU A 299 ? 0.5358 0.2519 0.3086 0.1068  0.0828  0.0769  299 GLU A N   
1086 C CA  . GLU A 299 ? 0.5346 0.2705 0.3181 0.1207  0.0783  0.0717  299 GLU A CA  
1087 C C   . GLU A 299 ? 0.5171 0.2695 0.3214 0.1024  0.0757  0.0604  299 GLU A C   
1088 O O   . GLU A 299 ? 0.5402 0.2690 0.3390 0.0950  0.0797  0.0550  299 GLU A O   
1089 C CB  . GLU A 299 ? 0.6094 0.3098 0.3706 0.1382  0.0839  0.0744  299 GLU A CB  
1090 N N   . HIS A 300 ? 0.4788 0.2695 0.3051 0.0943  0.0691  0.0569  300 HIS A N   
1091 C CA  . HIS A 300 ? 0.4598 0.2695 0.3064 0.0772  0.0659  0.0473  300 HIS A CA  
1092 C C   . HIS A 300 ? 0.4512 0.2677 0.3052 0.0821  0.0643  0.0403  300 HIS A C   
1093 O O   . HIS A 300 ? 0.4445 0.2580 0.3052 0.0685  0.0649  0.0332  300 HIS A O   
1094 C CB  . HIS A 300 ? 0.4388 0.2873 0.3047 0.0721  0.0589  0.0459  300 HIS A CB  
1095 C CG  . HIS A 300 ? 0.4387 0.3162 0.3118 0.0881  0.0530  0.0473  300 HIS A CG  
1096 N ND1 . HIS A 300 ? 0.4431 0.3448 0.3316 0.0903  0.0486  0.0409  300 HIS A ND1 
1097 C CD2 . HIS A 300 ? 0.4501 0.3362 0.3162 0.1020  0.0512  0.0545  300 HIS A CD2 
1098 C CE1 . HIS A 300 ? 0.4409 0.3667 0.3324 0.1043  0.0441  0.0440  300 HIS A CE1 
1099 N NE2 . HIS A 300 ? 0.4436 0.3618 0.3221 0.1120  0.0451  0.0520  300 HIS A NE2 
1100 N N   . HIS A 301 ? 0.4456 0.2737 0.2987 0.1015  0.0624  0.0424  301 HIS A N   
1101 C CA  . HIS A 301 ? 0.4419 0.2823 0.3033 0.1072  0.0609  0.0361  301 HIS A CA  
1102 C C   . HIS A 301 ? 0.4769 0.2793 0.3208 0.1101  0.0679  0.0337  301 HIS A C   
1103 O O   . HIS A 301 ? 0.4983 0.2788 0.3240 0.1277  0.0720  0.0386  301 HIS A O   
1104 C CB  . HIS A 301 ? 0.4265 0.2980 0.2948 0.1261  0.0564  0.0389  301 HIS A CB  
1105 C CG  . HIS A 301 ? 0.4288 0.3214 0.3090 0.1310  0.0546  0.0326  301 HIS A CG  
1106 N ND1 . HIS A 301 ? 0.4403 0.3543 0.3222 0.1509  0.0528  0.0351  301 HIS A ND1 
1107 C CD2 . HIS A 301 ? 0.4326 0.3291 0.3228 0.1186  0.0545  0.0245  301 HIS A CD2 
1108 C CE1 . HIS A 301 ? 0.4312 0.3614 0.3243 0.1494  0.0522  0.0283  301 HIS A CE1 
1109 N NE2 . HIS A 301 ? 0.4341 0.3535 0.3320 0.1304  0.0531  0.0220  301 HIS A NE2 
1110 N N   . VAL A 302 ? 0.4786 0.2725 0.3269 0.0930  0.0691  0.0260  302 VAL A N   
1111 C CA  . VAL A 302 ? 0.5060 0.2617 0.3364 0.0918  0.0756  0.0223  302 VAL A CA  
1112 C C   . VAL A 302 ? 0.5061 0.2708 0.3422 0.0960  0.0752  0.0145  302 VAL A C   
1113 O O   . VAL A 302 ? 0.5318 0.2646 0.3514 0.0971  0.0806  0.0107  302 VAL A O   
1114 C CB  . VAL A 302 ? 0.5237 0.2574 0.3495 0.0687  0.0785  0.0196  302 VAL A CB  
1115 C CG1 . VAL A 302 ? 0.5390 0.2567 0.3538 0.0658  0.0812  0.0281  302 VAL A CG1 
1116 C CG2 . VAL A 302 ? 0.5125 0.2783 0.3620 0.0512  0.0728  0.0130  302 VAL A CG2 
1117 N N   . ALA A 303 ? 0.4744 0.2805 0.3324 0.0967  0.0691  0.0116  303 ALA A N   
1118 C CA  . ALA A 303 ? 0.4678 0.2853 0.3316 0.1004  0.0690  0.0046  303 ALA A CA  
1119 C C   . ALA A 303 ? 0.4311 0.2949 0.3160 0.1063  0.0630  0.0047  303 ALA A C   
1120 O O   . ALA A 303 ? 0.4081 0.2959 0.3071 0.0990  0.0578  0.0069  303 ALA A O   
1121 C CB  . ALA A 303 ? 0.4721 0.2833 0.3400 0.0799  0.0690  -0.0035 303 ALA A CB  
1122 N N   . THR A 304 ? 0.4107 0.2868 0.2975 0.1184  0.0640  0.0017  304 THR A N   
1123 C CA  . THR A 304 ? 0.3899 0.3108 0.2967 0.1220  0.0591  0.0008  304 THR A CA  
1124 C C   . THR A 304 ? 0.3761 0.3029 0.2875 0.1169  0.0605  -0.0069 304 THR A C   
1125 O O   . THR A 304 ? 0.3990 0.3058 0.2965 0.1270  0.0659  -0.0097 304 THR A O   
1126 C CB  . THR A 304 ? 0.4096 0.3469 0.3143 0.1455  0.0593  0.0061  304 THR A CB  
1127 O OG1 . THR A 304 ? 0.4174 0.3522 0.3182 0.1494  0.0572  0.0134  304 THR A OG1 
1128 C CG2 . THR A 304 ? 0.3956 0.3810 0.3209 0.1478  0.0549  0.0043  304 THR A CG2 
1129 N N   . LEU A 305 ? 0.3405 0.2924 0.2692 0.1018  0.0560  -0.0102 305 LEU A N   
1130 C CA  . LEU A 305 ? 0.3264 0.2874 0.2604 0.0951  0.0567  -0.0168 305 LEU A CA  
1131 C C   . LEU A 305 ? 0.3127 0.3158 0.2632 0.1006  0.0538  -0.0161 305 LEU A C   
1132 O O   . LEU A 305 ? 0.2964 0.3233 0.2608 0.0927  0.0485  -0.0138 305 LEU A O   
1133 C CB  . LEU A 305 ? 0.3248 0.2824 0.2652 0.0736  0.0537  -0.0202 305 LEU A CB  
1134 C CG  . LEU A 305 ? 0.3568 0.2781 0.2831 0.0639  0.0566  -0.0231 305 LEU A CG  
1135 C CD1 . LEU A 305 ? 0.3797 0.2737 0.2924 0.0689  0.0592  -0.0182 305 LEU A CD1 
1136 C CD2 . LEU A 305 ? 0.3502 0.2780 0.2864 0.0442  0.0526  -0.0255 305 LEU A CD2 
1137 N N   . SER A 306 ? 0.3100 0.3224 0.2579 0.1142  0.0575  -0.0180 306 SER A N   
1138 C CA  . SER A 306 ? 0.2998 0.3551 0.2633 0.1196  0.0554  -0.0171 306 SER A CA  
1139 C C   . SER A 306 ? 0.3009 0.3701 0.2696 0.1141  0.0574  -0.0225 306 SER A C   
1140 O O   . SER A 306 ? 0.3143 0.3820 0.2755 0.1273  0.0626  -0.0250 306 SER A O   
1141 C CB  . SER A 306 ? 0.3242 0.3889 0.2827 0.1436  0.0579  -0.0133 306 SER A CB  
1142 O OG  . SER A 306 ? 0.3817 0.4352 0.3349 0.1489  0.0558  -0.0074 306 SER A OG  
1143 N N   . GLY A 307 ? 0.2851 0.3664 0.2651 0.0954  0.0536  -0.0241 307 GLY A N   
1144 C CA  . GLY A 307 ? 0.2739 0.3688 0.2585 0.0882  0.0552  -0.0284 307 GLY A CA  
1145 C C   . GLY A 307 ? 0.2556 0.3867 0.2579 0.0771  0.0512  -0.0269 307 GLY A C   
1146 O O   . GLY A 307 ? 0.2586 0.3994 0.2646 0.0677  0.0520  -0.0294 307 GLY A O   
1147 N N   . HIS A 308 ? 0.2318 0.3820 0.2439 0.0771  0.0469  -0.0228 308 HIS A N   
1148 C CA  . HIS A 308 ? 0.2148 0.3977 0.2422 0.0652  0.0432  -0.0219 308 HIS A CA  
1149 C C   . HIS A 308 ? 0.2255 0.4436 0.2623 0.0756  0.0423  -0.0193 308 HIS A C   
1150 O O   . HIS A 308 ? 0.2482 0.4630 0.2809 0.0892  0.0416  -0.0166 308 HIS A O   
1151 C CB  . HIS A 308 ? 0.2017 0.3759 0.2328 0.0491  0.0377  -0.0208 308 HIS A CB  
1152 C CG  . HIS A 308 ? 0.1967 0.3447 0.2217 0.0372  0.0377  -0.0230 308 HIS A CG  
1153 N ND1 . HIS A 308 ? 0.2070 0.3626 0.2364 0.0242  0.0373  -0.0244 308 HIS A ND1 
1154 C CD2 . HIS A 308 ? 0.2111 0.3281 0.2266 0.0361  0.0378  -0.0237 308 HIS A CD2 
1155 C CE1 . HIS A 308 ? 0.2109 0.3410 0.2332 0.0173  0.0367  -0.0259 308 HIS A CE1 
1156 N NE2 . HIS A 308 ? 0.2157 0.3234 0.2302 0.0235  0.0371  -0.0259 308 HIS A NE2 
1157 N N   . SER A 309 ? 0.2187 0.4716 0.2677 0.0688  0.0420  -0.0199 309 SER A N   
1158 C CA  . SER A 309 ? 0.2097 0.5028 0.2698 0.0767  0.0406  -0.0178 309 SER A CA  
1159 C C   . SER A 309 ? 0.2045 0.5167 0.2754 0.0613  0.0341  -0.0166 309 SER A C   
1160 O O   . SER A 309 ? 0.2053 0.5533 0.2861 0.0651  0.0318  -0.0153 309 SER A O   
1161 C CB  . SER A 309 ? 0.2163 0.5411 0.2832 0.0804  0.0453  -0.0194 309 SER A CB  
1162 O OG  . SER A 309 ? 0.2429 0.5713 0.3143 0.0604  0.0456  -0.0211 309 SER A OG  
1163 N N   . GLN A 310 ? 0.1875 0.4777 0.2564 0.0439  0.0313  -0.0175 310 GLN A N   
1164 C CA  . GLN A 310 ? 0.1659 0.4645 0.2412 0.0282  0.0255  -0.0172 310 GLN A CA  
1165 C C   . GLN A 310 ? 0.1652 0.4270 0.2316 0.0241  0.0227  -0.0168 310 GLN A C   
1166 O O   . GLN A 310 ? 0.1724 0.4055 0.2292 0.0311  0.0253  -0.0167 310 GLN A O   
1167 C CB  . GLN A 310 ? 0.1618 0.4739 0.2436 0.0092  0.0259  -0.0189 310 GLN A CB  
1168 C CG  . GLN A 310 ? 0.1945 0.5463 0.2860 0.0112  0.0293  -0.0192 310 GLN A CG  
1169 C CD  . GLN A 310 ? 0.2487 0.6403 0.3512 0.0145  0.0260  -0.0185 310 GLN A CD  
1170 O OE1 . GLN A 310 ? 0.2889 0.6824 0.3931 0.0085  0.0203  -0.0183 310 GLN A OE1 
1171 N NE2 . GLN A 310 ? 0.2538 0.6803 0.3638 0.0245  0.0294  -0.0183 310 GLN A NE2 
1172 N N   . GLU A 311 ? 0.1570 0.4203 0.2263 0.0117  0.0179  -0.0170 311 GLU A N   
1173 C CA  . GLU A 311 ? 0.1569 0.3913 0.2191 0.0084  0.0152  -0.0165 311 GLU A CA  
1174 C C   . GLU A 311 ? 0.1679 0.3692 0.2221 0.0052  0.0177  -0.0172 311 GLU A C   
1175 O O   . GLU A 311 ? 0.1687 0.3673 0.2235 -0.0041 0.0193  -0.0187 311 GLU A O   
1176 C CB  . GLU A 311 ? 0.1636 0.4050 0.2295 -0.0066 0.0102  -0.0178 311 GLU A CB  
1177 C CG  . GLU A 311 ? 0.1992 0.4141 0.2580 -0.0086 0.0077  -0.0175 311 GLU A CG  
1178 C CD  . GLU A 311 ? 0.2463 0.4704 0.3066 -0.0164 0.0025  -0.0186 311 GLU A CD  
1179 O OE1 . GLU A 311 ? 0.2274 0.4376 0.2820 -0.0126 0.0007  -0.0178 311 GLU A OE1 
1180 O OE2 . GLU A 311 ? 0.2522 0.4977 0.3186 -0.0269 0.0006  -0.0207 311 GLU A OE2 
1181 N N   . VAL A 312 ? 0.1726 0.3497 0.2187 0.0122  0.0181  -0.0161 312 VAL A N   
1182 C CA  . VAL A 312 ? 0.1769 0.3255 0.2161 0.0079  0.0199  -0.0171 312 VAL A CA  
1183 C C   . VAL A 312 ? 0.1814 0.3215 0.2213 -0.0043 0.0161  -0.0174 312 VAL A C   
1184 O O   . VAL A 312 ? 0.2025 0.3361 0.2402 -0.0025 0.0140  -0.0162 312 VAL A O   
1185 C CB  . VAL A 312 ? 0.1982 0.3243 0.2278 0.0189  0.0226  -0.0159 312 VAL A CB  
1186 C CG1 . VAL A 312 ? 0.2050 0.3057 0.2287 0.0119  0.0238  -0.0176 312 VAL A CG1 
1187 C CG2 . VAL A 312 ? 0.2112 0.3429 0.2378 0.0330  0.0267  -0.0157 312 VAL A CG2 
1188 N N   . CYS A 313 ? 0.1657 0.3056 0.2075 -0.0156 0.0156  -0.0188 313 CYS A N   
1189 C CA  . CYS A 313 ? 0.1732 0.3043 0.2143 -0.0259 0.0124  -0.0192 313 CYS A CA  
1190 C C   . CYS A 313 ? 0.1891 0.2974 0.2249 -0.0287 0.0129  -0.0195 313 CYS A C   
1191 O O   . CYS A 313 ? 0.2022 0.3017 0.2364 -0.0341 0.0105  -0.0196 313 CYS A O   
1192 C CB  . CYS A 313 ? 0.1837 0.3282 0.2287 -0.0370 0.0110  -0.0200 313 CYS A CB  
1193 S SG  . CYS A 313 ? 0.2367 0.3906 0.2833 -0.0402 0.0149  -0.0201 313 CYS A SG  
1194 N N   . GLY A 314 ? 0.1751 0.2753 0.2077 -0.0253 0.0159  -0.0200 314 GLY A N   
1195 C CA  . GLY A 314 ? 0.1798 0.2623 0.2079 -0.0283 0.0159  -0.0205 314 GLY A CA  
1196 C C   . GLY A 314 ? 0.1741 0.2453 0.1976 -0.0213 0.0186  -0.0211 314 GLY A C   
1197 O O   . GLY A 314 ? 0.1774 0.2518 0.1992 -0.0149 0.0214  -0.0217 314 GLY A O   
1198 N N   . LEU A 315 ? 0.1669 0.2248 0.1875 -0.0220 0.0181  -0.0208 315 LEU A N   
1199 C CA  . LEU A 315 ? 0.1732 0.2176 0.1877 -0.0171 0.0211  -0.0212 315 LEU A CA  
1200 C C   . LEU A 315 ? 0.1774 0.2105 0.1900 -0.0232 0.0205  -0.0220 315 LEU A C   
1201 O O   . LEU A 315 ? 0.1871 0.2215 0.2024 -0.0260 0.0183  -0.0206 315 LEU A O   
1202 C CB  . LEU A 315 ? 0.1722 0.2164 0.1851 -0.0093 0.0217  -0.0186 315 LEU A CB  
1203 C CG  . LEU A 315 ? 0.2120 0.2395 0.2158 -0.0025 0.0257  -0.0181 315 LEU A CG  
1204 C CD1 . LEU A 315 ? 0.2336 0.2592 0.2332 0.0034  0.0290  -0.0202 315 LEU A CD1 
1205 C CD2 . LEU A 315 ? 0.2269 0.2553 0.2285 0.0058  0.0258  -0.0143 315 LEU A CD2 
1206 N N   . ARG A 316 ? 0.1713 0.1951 0.1791 -0.0256 0.0224  -0.0245 316 ARG A N   
1207 C CA  . ARG A 316 ? 0.1793 0.1974 0.1866 -0.0325 0.0213  -0.0256 316 ARG A CA  
1208 C C   . ARG A 316 ? 0.1850 0.1899 0.1849 -0.0350 0.0241  -0.0287 316 ARG A C   
1209 O O   . ARG A 316 ? 0.1810 0.1843 0.1770 -0.0354 0.0251  -0.0317 316 ARG A O   
1210 C CB  . ARG A 316 ? 0.1953 0.2226 0.2066 -0.0373 0.0181  -0.0261 316 ARG A CB  
1211 C CG  . ARG A 316 ? 0.2361 0.2650 0.2502 -0.0420 0.0158  -0.0257 316 ARG A CG  
1212 C CD  . ARG A 316 ? 0.2640 0.2975 0.2823 -0.0401 0.0140  -0.0230 316 ARG A CD  
1213 N NE  . ARG A 316 ? 0.2761 0.3155 0.2958 -0.0399 0.0121  -0.0221 316 ARG A NE  
1214 C CZ  . ARG A 316 ? 0.3229 0.3661 0.3443 -0.0381 0.0115  -0.0209 316 ARG A CZ  
1215 N NH1 . ARG A 316 ? 0.3260 0.3685 0.3479 -0.0351 0.0121  -0.0200 316 ARG A NH1 
1216 N NH2 . ARG A 316 ? 0.3163 0.3643 0.3382 -0.0402 0.0104  -0.0204 316 ARG A NH2 
1217 N N   . TRP A 317 ? 0.1835 0.1787 0.1805 -0.0379 0.0255  -0.0282 317 TRP A N   
1218 C CA  . TRP A 317 ? 0.2071 0.1882 0.1961 -0.0432 0.0281  -0.0316 317 TRP A CA  
1219 C C   . TRP A 317 ? 0.2203 0.2109 0.2132 -0.0519 0.0250  -0.0344 317 TRP A C   
1220 O O   . TRP A 317 ? 0.2157 0.2194 0.2166 -0.0537 0.0218  -0.0325 317 TRP A O   
1221 C CB  . TRP A 317 ? 0.2210 0.1908 0.2064 -0.0457 0.0307  -0.0294 317 TRP A CB  
1222 C CG  . TRP A 317 ? 0.2394 0.1926 0.2154 -0.0378 0.0348  -0.0275 317 TRP A CG  
1223 C CD1 . TRP A 317 ? 0.2489 0.2034 0.2254 -0.0294 0.0353  -0.0227 317 TRP A CD1 
1224 C CD2 . TRP A 317 ? 0.2637 0.1955 0.2266 -0.0365 0.0391  -0.0302 317 TRP A CD2 
1225 N NE1 . TRP A 317 ? 0.2697 0.2056 0.2345 -0.0220 0.0395  -0.0215 317 TRP A NE1 
1226 C CE2 . TRP A 317 ? 0.2807 0.2007 0.2364 -0.0259 0.0423  -0.0262 317 TRP A CE2 
1227 C CE3 . TRP A 317 ? 0.2891 0.2097 0.2443 -0.0431 0.0406  -0.0360 317 TRP A CE3 
1228 C CZ2 . TRP A 317 ? 0.3103 0.2055 0.2508 -0.0207 0.0473  -0.0273 317 TRP A CZ2 
1229 C CZ3 . TRP A 317 ? 0.3183 0.2138 0.2581 -0.0390 0.0456  -0.0380 317 TRP A CZ3 
1230 C CH2 . TRP A 317 ? 0.3296 0.2112 0.2618 -0.0278 0.0491  -0.0334 317 TRP A CH2 
1231 N N   . ALA A 318 ? 0.2353 0.2190 0.2214 -0.0567 0.0260  -0.0392 318 ALA A N   
1232 C CA  . ALA A 318 ? 0.2525 0.2466 0.2412 -0.0649 0.0227  -0.0420 318 ALA A CA  
1233 C C   . ALA A 318 ? 0.2718 0.2684 0.2637 -0.0728 0.0225  -0.0416 318 ALA A C   
1234 O O   . ALA A 318 ? 0.2754 0.2582 0.2625 -0.0748 0.0262  -0.0410 318 ALA A O   
1235 C CB  . ALA A 318 ? 0.2655 0.2506 0.2444 -0.0688 0.0241  -0.0480 318 ALA A CB  
1236 N N   . PRO A 319 ? 0.2985 0.3128 0.2978 -0.0773 0.0186  -0.0417 319 PRO A N   
1237 C CA  . PRO A 319 ? 0.3107 0.3320 0.3144 -0.0848 0.0187  -0.0415 319 PRO A CA  
1238 C C   . PRO A 319 ? 0.3221 0.3309 0.3177 -0.0959 0.0219  -0.0459 319 PRO A C   
1239 O O   . PRO A 319 ? 0.3376 0.3441 0.3338 -0.1017 0.0245  -0.0446 319 PRO A O   
1240 C CB  . PRO A 319 ? 0.3225 0.3667 0.3343 -0.0857 0.0135  -0.0415 319 PRO A CB  
1241 C CG  . PRO A 319 ? 0.3281 0.3743 0.3404 -0.0767 0.0112  -0.0394 319 PRO A CG  
1242 C CD  . PRO A 319 ? 0.3048 0.3344 0.3086 -0.0746 0.0141  -0.0413 319 PRO A CD  
1243 N N   . ASP A 320 ? 0.3197 0.3183 0.3062 -0.0993 0.0223  -0.0511 320 ASP A N   
1244 C CA  . ASP A 320 ? 0.3287 0.3102 0.3043 -0.1107 0.0258  -0.0563 320 ASP A CA  
1245 C C   . ASP A 320 ? 0.3453 0.2962 0.3083 -0.1066 0.0320  -0.0554 320 ASP A C   
1246 O O   . ASP A 320 ? 0.3587 0.2891 0.3093 -0.1155 0.0357  -0.0596 320 ASP A O   
1247 C CB  . ASP A 320 ? 0.3276 0.3116 0.2972 -0.1174 0.0234  -0.0634 320 ASP A CB  
1248 C CG  . ASP A 320 ? 0.4005 0.3749 0.3626 -0.1082 0.0237  -0.0653 320 ASP A CG  
1249 O OD1 . ASP A 320 ? 0.3778 0.3425 0.3390 -0.0965 0.0263  -0.0612 320 ASP A OD1 
1250 O OD2 . ASP A 320 ? 0.4279 0.4063 0.3849 -0.1124 0.0215  -0.0708 320 ASP A OD2 
1251 N N   . GLY A 321 ? 0.3400 0.2877 0.3048 -0.0932 0.0329  -0.0504 321 GLY A N   
1252 C CA  . GLY A 321 ? 0.3681 0.2908 0.3218 -0.0857 0.0381  -0.0484 321 GLY A CA  
1253 C C   . GLY A 321 ? 0.3963 0.2986 0.3359 -0.0822 0.0410  -0.0534 321 GLY A C   
1254 O O   . GLY A 321 ? 0.4298 0.3087 0.3578 -0.0754 0.0458  -0.0521 321 GLY A O   
1255 N N   . ARG A 322 ? 0.3785 0.2890 0.3177 -0.0853 0.0383  -0.0589 322 ARG A N   
1256 C CA  . ARG A 322 ? 0.3904 0.2825 0.3151 -0.0820 0.0413  -0.0646 322 ARG A CA  
1257 C C   . ARG A 322 ? 0.3661 0.2615 0.2918 -0.0659 0.0422  -0.0622 322 ARG A C   
1258 O O   . ARG A 322 ? 0.3789 0.2566 0.2916 -0.0594 0.0461  -0.0657 322 ARG A O   
1259 C CB  . ARG A 322 ? 0.4205 0.3211 0.3431 -0.0927 0.0381  -0.0719 322 ARG A CB  
1260 C CG  . ARG A 322 ? 0.4904 0.3835 0.4075 -0.1100 0.0384  -0.0767 322 ARG A CG  
1261 C CD  . ARG A 322 ? 0.5552 0.4638 0.4724 -0.1205 0.0338  -0.0837 322 ARG A CD  
1262 N NE  . ARG A 322 ? 0.6176 0.5151 0.5220 -0.1159 0.0350  -0.0898 322 ARG A NE  
1263 C CZ  . ARG A 322 ? 0.6442 0.5601 0.5534 -0.1088 0.0317  -0.0897 322 ARG A CZ  
1264 N NH1 . ARG A 322 ? 0.6093 0.5530 0.5349 -0.1053 0.0268  -0.0836 322 ARG A NH1 
1265 N NH2 . ARG A 322 ? 0.6721 0.5773 0.5684 -0.1048 0.0337  -0.0955 322 ARG A NH2 
1266 N N   . HIS A 323 ? 0.3339 0.2525 0.2742 -0.0599 0.0387  -0.0567 323 HIS A N   
1267 C CA  . HIS A 323 ? 0.3120 0.2382 0.2549 -0.0466 0.0393  -0.0543 323 HIS A CA  
1268 C C   . HIS A 323 ? 0.2791 0.2197 0.2344 -0.0408 0.0373  -0.0471 323 HIS A C   
1269 O O   . HIS A 323 ? 0.2735 0.2243 0.2375 -0.0471 0.0342  -0.0446 323 HIS A O   
1270 C CB  . HIS A 323 ? 0.3215 0.2653 0.2684 -0.0475 0.0363  -0.0568 323 HIS A CB  
1271 C CG  . HIS A 323 ? 0.3690 0.3030 0.3039 -0.0530 0.0375  -0.0644 323 HIS A CG  
1272 N ND1 . HIS A 323 ? 0.3900 0.3291 0.3250 -0.0656 0.0340  -0.0681 323 HIS A ND1 
1273 C CD2 . HIS A 323 ? 0.4007 0.3225 0.3233 -0.0469 0.0415  -0.0691 323 HIS A CD2 
1274 C CE1 . HIS A 323 ? 0.4064 0.3349 0.3284 -0.0680 0.0357  -0.0753 323 HIS A CE1 
1275 N NE2 . HIS A 323 ? 0.4164 0.3328 0.3300 -0.0568 0.0406  -0.0763 323 HIS A NE2 
1276 N N   . LEU A 324 ? 0.2526 0.1970 0.2090 -0.0288 0.0389  -0.0442 324 LEU A N   
1277 C CA  . LEU A 324 ? 0.2375 0.1983 0.2052 -0.0236 0.0365  -0.0384 324 LEU A CA  
1278 C C   . LEU A 324 ? 0.2329 0.2121 0.2065 -0.0189 0.0354  -0.0383 324 LEU A C   
1279 O O   . LEU A 324 ? 0.2496 0.2256 0.2171 -0.0115 0.0386  -0.0404 324 LEU A O   
1280 C CB  . LEU A 324 ? 0.2418 0.1917 0.2046 -0.0138 0.0396  -0.0347 324 LEU A CB  
1281 C CG  . LEU A 324 ? 0.2540 0.2217 0.2265 -0.0069 0.0373  -0.0296 324 LEU A CG  
1282 C CD1 . LEU A 324 ? 0.2515 0.2294 0.2334 -0.0147 0.0334  -0.0271 324 LEU A CD1 
1283 C CD2 . LEU A 324 ? 0.2831 0.2402 0.2485 0.0045  0.0404  -0.0260 324 LEU A CD2 
1284 N N   . ALA A 325 ? 0.2078 0.2053 0.1922 -0.0229 0.0313  -0.0359 325 ALA A N   
1285 C CA  . ALA A 325 ? 0.2182 0.2328 0.2078 -0.0203 0.0306  -0.0352 325 ALA A CA  
1286 C C   . ALA A 325 ? 0.2039 0.2310 0.2011 -0.0151 0.0296  -0.0310 325 ALA A C   
1287 O O   . ALA A 325 ? 0.1995 0.2261 0.2005 -0.0167 0.0275  -0.0284 325 ALA A O   
1288 C CB  . ALA A 325 ? 0.2201 0.2440 0.2140 -0.0289 0.0270  -0.0353 325 ALA A CB  
1289 N N   . SER A 326 ? 0.1914 0.2313 0.1906 -0.0090 0.0313  -0.0307 326 SER A N   
1290 C CA  . SER A 326 ? 0.1831 0.2396 0.1903 -0.0055 0.0299  -0.0274 326 SER A CA  
1291 C C   . SER A 326 ? 0.1865 0.2630 0.1996 -0.0084 0.0296  -0.0272 326 SER A C   
1292 O O   . SER A 326 ? 0.1860 0.2649 0.1957 -0.0072 0.0324  -0.0294 326 SER A O   
1293 C CB  . SER A 326 ? 0.1951 0.2503 0.1992 0.0068  0.0325  -0.0262 326 SER A CB  
1294 O OG  . SER A 326 ? 0.2212 0.2769 0.2200 0.0149  0.0367  -0.0285 326 SER A OG  
1295 N N   . GLY A 327 ? 0.1779 0.2672 0.1985 -0.0136 0.0265  -0.0248 327 GLY A N   
1296 C CA  . GLY A 327 ? 0.1816 0.2896 0.2076 -0.0186 0.0264  -0.0241 327 GLY A CA  
1297 C C   . GLY A 327 ? 0.1741 0.3015 0.2073 -0.0157 0.0254  -0.0225 327 GLY A C   
1298 O O   . GLY A 327 ? 0.1698 0.2945 0.2043 -0.0139 0.0229  -0.0213 327 GLY A O   
1299 N N   . GLY A 328 ? 0.1741 0.3229 0.2119 -0.0156 0.0274  -0.0225 328 GLY A N   
1300 C CA  . GLY A 328 ? 0.1756 0.3481 0.2212 -0.0129 0.0263  -0.0214 328 GLY A CA  
1301 C C   . GLY A 328 ? 0.1724 0.3680 0.2251 -0.0236 0.0258  -0.0209 328 GLY A C   
1302 O O   . GLY A 328 ? 0.1734 0.3675 0.2244 -0.0323 0.0274  -0.0209 328 GLY A O   
1303 N N   . ASN A 329 ? 0.1598 0.3773 0.2198 -0.0234 0.0236  -0.0204 329 ASN A N   
1304 C CA  . ASN A 329 ? 0.1610 0.4046 0.2285 -0.0346 0.0233  -0.0203 329 ASN A CA  
1305 C C   . ASN A 329 ? 0.1647 0.4337 0.2368 -0.0290 0.0283  -0.0205 329 ASN A C   
1306 O O   . ASN A 329 ? 0.1736 0.4708 0.2534 -0.0370 0.0290  -0.0204 329 ASN A O   
1307 C CB  . ASN A 329 ? 0.1602 0.4219 0.2340 -0.0365 0.0190  -0.0205 329 ASN A CB  
1308 C CG  . ASN A 329 ? 0.2074 0.4908 0.2871 -0.0527 0.0180  -0.0211 329 ASN A CG  
1309 O OD1 . ASN A 329 ? 0.2290 0.5006 0.3048 -0.0658 0.0193  -0.0209 329 ASN A OD1 
1310 N ND2 . ASN A 329 ? 0.2019 0.5175 0.2904 -0.0523 0.0160  -0.0218 329 ASN A ND2 
1311 N N   . ASP A 330 ? 0.1641 0.4244 0.2313 -0.0150 0.0320  -0.0211 330 ASP A N   
1312 C CA  . ASP A 330 ? 0.1587 0.4383 0.2276 -0.0077 0.0376  -0.0218 330 ASP A CA  
1313 C C   . ASP A 330 ? 0.1788 0.4425 0.2403 -0.0147 0.0410  -0.0225 330 ASP A C   
1314 O O   . ASP A 330 ? 0.1814 0.4541 0.2409 -0.0077 0.0461  -0.0237 330 ASP A O   
1315 C CB  . ASP A 330 ? 0.1711 0.4486 0.2365 0.0134  0.0399  -0.0224 330 ASP A CB  
1316 C CG  . ASP A 330 ? 0.2140 0.4524 0.2672 0.0197  0.0398  -0.0232 330 ASP A CG  
1317 O OD1 . ASP A 330 ? 0.2339 0.4500 0.2832 0.0085  0.0370  -0.0233 330 ASP A OD1 
1318 O OD2 . ASP A 330 ? 0.2406 0.4710 0.2876 0.0357  0.0427  -0.0239 330 ASP A OD2 
1319 N N   . ASN A 331 ? 0.1905 0.4324 0.2473 -0.0278 0.0381  -0.0217 331 ASN A N   
1320 C CA  . ASN A 331 ? 0.2050 0.4316 0.2540 -0.0350 0.0401  -0.0216 331 ASN A CA  
1321 C C   . ASN A 331 ? 0.2051 0.4115 0.2447 -0.0243 0.0424  -0.0241 331 ASN A C   
1322 O O   . ASN A 331 ? 0.2252 0.4278 0.2585 -0.0267 0.0453  -0.0247 331 ASN A O   
1323 C CB  . ASN A 331 ? 0.2249 0.4753 0.2768 -0.0428 0.0444  -0.0205 331 ASN A CB  
1324 C CG  . ASN A 331 ? 0.2864 0.5644 0.3487 -0.0528 0.0436  -0.0190 331 ASN A CG  
1325 O OD1 . ASN A 331 ? 0.2952 0.5677 0.3596 -0.0607 0.0390  -0.0183 331 ASN A OD1 
1326 N ND2 . ASN A 331 ? 0.3117 0.6202 0.3799 -0.0535 0.0483  -0.0187 331 ASN A ND2 
1327 N N   . LEU A 332 ? 0.1800 0.3743 0.2174 -0.0127 0.0414  -0.0255 332 LEU A N   
1328 C CA  . LEU A 332 ? 0.1910 0.3635 0.2179 -0.0045 0.0437  -0.0285 332 LEU A CA  
1329 C C   . LEU A 332 ? 0.1858 0.3308 0.2075 -0.0087 0.0397  -0.0287 332 LEU A C   
1330 O O   . LEU A 332 ? 0.1766 0.3188 0.2026 -0.0115 0.0358  -0.0267 332 LEU A O   
1331 C CB  . LEU A 332 ? 0.2074 0.3813 0.2323 0.0123  0.0467  -0.0301 332 LEU A CB  
1332 C CG  . LEU A 332 ? 0.2430 0.4448 0.2724 0.0215  0.0512  -0.0304 332 LEU A CG  
1333 C CD1 . LEU A 332 ? 0.2750 0.4719 0.2999 0.0403  0.0536  -0.0314 332 LEU A CD1 
1334 C CD2 . LEU A 332 ? 0.2591 0.4639 0.2828 0.0199  0.0560  -0.0329 332 LEU A CD2 
1335 N N   . VAL A 333 ? 0.1788 0.3053 0.1910 -0.0085 0.0409  -0.0314 333 VAL A N   
1336 C CA  . VAL A 333 ? 0.1918 0.2942 0.1984 -0.0106 0.0382  -0.0325 333 VAL A CA  
1337 C C   . VAL A 333 ? 0.2011 0.2884 0.1980 -0.0005 0.0419  -0.0366 333 VAL A C   
1338 O O   . VAL A 333 ? 0.2066 0.2953 0.1972 0.0030  0.0457  -0.0397 333 VAL A O   
1339 C CB  . VAL A 333 ? 0.2017 0.2956 0.2045 -0.0209 0.0358  -0.0327 333 VAL A CB  
1340 C CG1 . VAL A 333 ? 0.2191 0.2920 0.2169 -0.0225 0.0333  -0.0344 333 VAL A CG1 
1341 C CG2 . VAL A 333 ? 0.2037 0.3075 0.2129 -0.0302 0.0328  -0.0285 333 VAL A CG2 
1342 N N   . ASN A 334 ? 0.1964 0.2686 0.1907 0.0044  0.0413  -0.0365 334 ASN A N   
1343 C CA  . ASN A 334 ? 0.2113 0.2627 0.1935 0.0125  0.0450  -0.0402 334 ASN A CA  
1344 C C   . ASN A 334 ? 0.2234 0.2525 0.2000 0.0040  0.0426  -0.0418 334 ASN A C   
1345 O O   . ASN A 334 ? 0.2247 0.2542 0.2077 -0.0022 0.0388  -0.0388 334 ASN A O   
1346 C CB  . ASN A 334 ? 0.2310 0.2807 0.2123 0.0256  0.0470  -0.0382 334 ASN A CB  
1347 C CG  . ASN A 334 ? 0.2571 0.3285 0.2419 0.0369  0.0503  -0.0377 334 ASN A CG  
1348 O OD1 . ASN A 334 ? 0.2795 0.3507 0.2574 0.0428  0.0548  -0.0413 334 ASN A OD1 
1349 N ND2 . ASN A 334 ? 0.2521 0.3443 0.2474 0.0404  0.0483  -0.0335 334 ASN A ND2 
1350 N N   . VAL A 335 ? 0.2358 0.2463 0.2001 0.0037  0.0452  -0.0470 335 VAL A N   
1351 C CA  . VAL A 335 ? 0.2571 0.2478 0.2155 -0.0047 0.0435  -0.0491 335 VAL A CA  
1352 C C   . VAL A 335 ? 0.2750 0.2412 0.2203 0.0031  0.0481  -0.0516 335 VAL A C   
1353 O O   . VAL A 335 ? 0.2783 0.2359 0.2129 0.0097  0.0524  -0.0560 335 VAL A O   
1354 C CB  . VAL A 335 ? 0.2779 0.2674 0.2316 -0.0144 0.0420  -0.0537 335 VAL A CB  
1355 C CG1 . VAL A 335 ? 0.2840 0.2562 0.2323 -0.0236 0.0404  -0.0564 335 VAL A CG1 
1356 C CG2 . VAL A 335 ? 0.2769 0.2883 0.2413 -0.0205 0.0380  -0.0501 335 VAL A CG2 
1357 N N   . TRP A 336 ? 0.2785 0.2324 0.2234 0.0027  0.0477  -0.0487 336 TRP A N   
1358 C CA  . TRP A 336 ? 0.2958 0.2237 0.2270 0.0105  0.0523  -0.0494 336 TRP A CA  
1359 C C   . TRP A 336 ? 0.3337 0.2362 0.2537 -0.0009 0.0531  -0.0536 336 TRP A C   
1360 O O   . TRP A 336 ? 0.3318 0.2404 0.2587 -0.0138 0.0491  -0.0535 336 TRP A O   
1361 C CB  . TRP A 336 ? 0.2857 0.2168 0.2226 0.0170  0.0515  -0.0424 336 TRP A CB  
1362 C CG  . TRP A 336 ? 0.2778 0.2369 0.2270 0.0260  0.0499  -0.0383 336 TRP A CG  
1363 C CD1 . TRP A 336 ? 0.2675 0.2520 0.2319 0.0198  0.0451  -0.0355 336 TRP A CD1 
1364 C CD2 . TRP A 336 ? 0.2855 0.2509 0.2319 0.0423  0.0532  -0.0371 336 TRP A CD2 
1365 N NE1 . TRP A 336 ? 0.2630 0.2693 0.2346 0.0294  0.0451  -0.0328 336 TRP A NE1 
1366 C CE2 . TRP A 336 ? 0.2764 0.2742 0.2383 0.0437  0.0499  -0.0337 336 TRP A CE2 
1367 C CE3 . TRP A 336 ? 0.3197 0.2660 0.2514 0.0564  0.0588  -0.0385 336 TRP A CE3 
1368 C CZ2 . TRP A 336 ? 0.2850 0.3009 0.2500 0.0581  0.0517  -0.0315 336 TRP A CZ2 
1369 C CZ3 . TRP A 336 ? 0.3301 0.2934 0.2643 0.0730  0.0607  -0.0361 336 TRP A CZ3 
1370 C CH2 . TRP A 336 ? 0.3097 0.3098 0.2613 0.0732  0.0571  -0.0328 336 TRP A CH2 
1371 N N   . PRO A 337 ? 0.3771 0.2501 0.2793 0.0041  0.0584  -0.0569 337 PRO A N   
1372 C CA  . PRO A 337 ? 0.4127 0.2595 0.3031 -0.0087 0.0595  -0.0608 337 PRO A CA  
1373 C C   . PRO A 337 ? 0.4420 0.2824 0.3356 -0.0128 0.0589  -0.0547 337 PRO A C   
1374 O O   . PRO A 337 ? 0.4347 0.2862 0.3362 -0.0034 0.0581  -0.0479 337 PRO A O   
1375 C CB  . PRO A 337 ? 0.4364 0.2508 0.3047 0.0000  0.0662  -0.0656 337 PRO A CB  
1376 C CG  . PRO A 337 ? 0.4365 0.2564 0.3060 0.0202  0.0688  -0.0601 337 PRO A CG  
1377 C CD  . PRO A 337 ? 0.3865 0.2474 0.2772 0.0217  0.0638  -0.0571 337 PRO A CD  
1378 N N   . SER A 338 ? 0.4700 0.2949 0.3577 -0.0276 0.0591  -0.0572 338 SER A N   
1379 C CA  . SER A 338 ? 0.5071 0.3261 0.3969 -0.0330 0.0593  -0.0515 338 SER A CA  
1380 C C   . SER A 338 ? 0.5611 0.3462 0.4327 -0.0246 0.0656  -0.0485 338 SER A C   
1381 O O   . SER A 338 ? 0.5678 0.3476 0.4396 -0.0261 0.0664  -0.0425 338 SER A O   
1382 C CB  . SER A 338 ? 0.5310 0.3499 0.4223 -0.0529 0.0574  -0.0552 338 SER A CB  
1383 O OG  . SER A 338 ? 0.5859 0.3766 0.4587 -0.0605 0.0613  -0.0624 338 SER A OG  
1384 N N   . ALA A 339 ? 0.5970 0.3575 0.4510 -0.0156 0.0704  -0.0526 339 ALA A N   
1385 C CA  . ALA A 339 ? 0.6499 0.3734 0.4828 -0.0053 0.0771  -0.0499 339 ALA A CA  
1386 C C   . ALA A 339 ? 0.6793 0.3933 0.5009 0.0130  0.0807  -0.0532 339 ALA A C   
1387 O O   . ALA A 339 ? 0.6729 0.3997 0.4980 0.0115  0.0792  -0.0598 339 ALA A O   
1388 C CB  . ALA A 339 ? 0.6742 0.3622 0.4890 -0.0219 0.0812  -0.0542 339 ALA A CB  
1389 N N   . PRO A 340 ? 0.7110 0.4053 0.5195 0.0318  0.0855  -0.0482 340 PRO A N   
1390 C CA  . PRO A 340 ? 0.7382 0.4254 0.5359 0.0509  0.0893  -0.0514 340 PRO A CA  
1391 C C   . PRO A 340 ? 0.7860 0.4322 0.5582 0.0470  0.0952  -0.0606 340 PRO A C   
1392 O O   . PRO A 340 ? 0.7965 0.4419 0.5619 0.0583  0.0977  -0.0662 340 PRO A O   
1393 C CB  . PRO A 340 ? 0.7478 0.4295 0.5401 0.0728  0.0920  -0.0424 340 PRO A CB  
1394 C CG  . PRO A 340 ? 0.7511 0.4213 0.5425 0.0635  0.0914  -0.0354 340 PRO A CG  
1395 C CD  . PRO A 340 ? 0.7216 0.3972 0.5219 0.0370  0.0880  -0.0395 340 PRO A CD  
1396 N N   . GLY A 341 ? 0.8107 0.4245 0.5689 0.0301  0.0974  -0.0626 341 GLY A N   
1397 C CA  . GLY A 341 ? 0.8487 0.4197 0.5806 0.0225  0.1029  -0.0719 341 GLY A CA  
1398 C C   . GLY A 341 ? 0.8840 0.4171 0.5900 0.0451  0.1108  -0.0714 341 GLY A C   
1399 O O   . GLY A 341 ? 0.8907 0.4143 0.5920 0.0605  0.1132  -0.0620 341 GLY A O   
1400 N N   . GLU A 342 ? 0.9009 0.4139 0.5896 0.0491  0.1147  -0.0813 342 GLU A N   
1401 C CA  . GLU A 342 ? 0.9336 0.4094 0.5958 0.0732  0.1227  -0.0818 342 GLU A CA  
1402 C C   . GLU A 342 ? 0.9157 0.4261 0.5907 0.1006  0.1221  -0.0782 342 GLU A C   
1403 O O   . GLU A 342 ? 0.9328 0.4215 0.5906 0.1251  0.1280  -0.0755 342 GLU A O   
1404 C CB  . GLU A 342 ? 0.9989 0.4300 0.6316 0.0660  0.1284  -0.0946 342 GLU A CB  
1405 C CG  . GLU A 342 ? 1.0912 0.4982 0.7152 0.0345  0.1278  -0.1004 342 GLU A CG  
1406 C CD  . GLU A 342 ? 1.2199 0.5847 0.8261 0.0266  0.1322  -0.0942 342 GLU A CD  
1407 O OE1 . GLU A 342 ? 1.2614 0.6086 0.8608 -0.0006 0.1321  -0.0992 342 GLU A OE1 
1408 O OE2 . GLU A 342 ? 1.2519 0.6020 0.8504 0.0473  0.1360  -0.0842 342 GLU A OE2 
1409 N N   . GLY A 343 ? 0.8783 0.4420 0.5828 0.0962  0.1152  -0.0779 343 GLY A N   
1410 C CA  . GLY A 343 ? 0.8568 0.4601 0.5773 0.1177  0.1140  -0.0741 343 GLY A CA  
1411 C C   . GLY A 343 ? 0.8319 0.4666 0.5738 0.1226  0.1092  -0.0623 343 GLY A C   
1412 O O   . GLY A 343 ? 0.8505 0.4653 0.5870 0.1179  0.1093  -0.0560 343 GLY A O   
1413 N N   . GLY A 344 ? 0.7826 0.4664 0.5484 0.1305  0.1050  -0.0595 344 GLY A N   
1414 C CA  . GLY A 344 ? 0.7398 0.4564 0.5262 0.1346  0.0999  -0.0494 344 GLY A CA  
1415 C C   . GLY A 344 ? 0.6867 0.4425 0.5001 0.1149  0.0921  -0.0488 344 GLY A C   
1416 O O   . GLY A 344 ? 0.6871 0.4436 0.5032 0.0970  0.0902  -0.0555 344 GLY A O   
1417 N N   . TRP A 345 ? 0.6362 0.4245 0.4685 0.1188  0.0873  -0.0409 345 TRP A N   
1418 C CA  . TRP A 345 ? 0.5909 0.4157 0.4478 0.1022  0.0801  -0.0398 345 TRP A CA  
1419 C C   . TRP A 345 ? 0.5585 0.4196 0.4297 0.1049  0.0786  -0.0431 345 TRP A C   
1420 O O   . TRP A 345 ? 0.5504 0.4438 0.4347 0.1160  0.0769  -0.0388 345 TRP A O   
1421 C CB  . TRP A 345 ? 0.5711 0.4139 0.4403 0.1045  0.0759  -0.0308 345 TRP A CB  
1422 C CG  . TRP A 345 ? 0.5755 0.3910 0.4365 0.0936  0.0759  -0.0276 345 TRP A CG  
1423 C CD1 . TRP A 345 ? 0.5975 0.3888 0.4445 0.1035  0.0788  -0.0214 345 TRP A CD1 
1424 C CD2 . TRP A 345 ? 0.5686 0.3798 0.4346 0.0709  0.0731  -0.0302 345 TRP A CD2 
1425 N NE1 . TRP A 345 ? 0.6068 0.3786 0.4497 0.0870  0.0785  -0.0200 345 TRP A NE1 
1426 C CE2 . TRP A 345 ? 0.5894 0.3750 0.4449 0.0671  0.0748  -0.0255 345 TRP A CE2 
1427 C CE3 . TRP A 345 ? 0.5600 0.3874 0.4379 0.0541  0.0693  -0.0357 345 TRP A CE3 
1428 C CZ2 . TRP A 345 ? 0.5915 0.3700 0.4494 0.0468  0.0732  -0.0265 345 TRP A CZ2 
1429 C CZ3 . TRP A 345 ? 0.5676 0.3874 0.4474 0.0354  0.0673  -0.0366 345 TRP A CZ3 
1430 C CH2 . TRP A 345 ? 0.5785 0.3756 0.4493 0.0316  0.0692  -0.0323 345 TRP A CH2 
1431 N N   . VAL A 346 ? 0.5369 0.3929 0.4044 0.0946  0.0795  -0.0507 346 VAL A N   
1432 C CA  . VAL A 346 ? 0.5114 0.3992 0.3902 0.0954  0.0787  -0.0539 346 VAL A CA  
1433 C C   . VAL A 346 ? 0.4692 0.3692 0.3590 0.0735  0.0736  -0.0566 346 VAL A C   
1434 O O   . VAL A 346 ? 0.4741 0.3508 0.3558 0.0598  0.0728  -0.0601 346 VAL A O   
1435 C CB  . VAL A 346 ? 0.5541 0.4282 0.4162 0.1087  0.0855  -0.0605 346 VAL A CB  
1436 C CG1 . VAL A 346 ? 0.5746 0.4487 0.4302 0.1342  0.0902  -0.0568 346 VAL A CG1 
1437 C CG2 . VAL A 346 ? 0.5892 0.4196 0.4290 0.1003  0.0888  -0.0679 346 VAL A CG2 
1438 N N   . PRO A 347 ? 0.4242 0.3610 0.3321 0.0697  0.0701  -0.0547 347 PRO A N   
1439 C CA  . PRO A 347 ? 0.4007 0.3479 0.3173 0.0510  0.0653  -0.0564 347 PRO A CA  
1440 C C   . PRO A 347 ? 0.3967 0.3290 0.3005 0.0447  0.0675  -0.0644 347 PRO A C   
1441 O O   . PRO A 347 ? 0.3928 0.3235 0.2874 0.0549  0.0723  -0.0687 347 PRO A O   
1442 C CB  . PRO A 347 ? 0.3912 0.3774 0.3259 0.0510  0.0627  -0.0527 347 PRO A CB  
1443 C CG  . PRO A 347 ? 0.3955 0.3950 0.3348 0.0671  0.0644  -0.0480 347 PRO A CG  
1444 C CD  . PRO A 347 ? 0.3951 0.3659 0.3156 0.0818  0.0703  -0.0508 347 PRO A CD  
1445 N N   . LEU A 348 ? 0.3856 0.3099 0.2894 0.0280  0.0636  -0.0666 348 LEU A N   
1446 C CA  . LEU A 348 ? 0.3937 0.3099 0.2878 0.0186  0.0637  -0.0741 348 LEU A CA  
1447 C C   . LEU A 348 ? 0.3726 0.3191 0.2764 0.0168  0.0620  -0.0736 348 LEU A C   
1448 O O   . LEU A 348 ? 0.3758 0.3208 0.2701 0.0158  0.0640  -0.0796 348 LEU A O   
1449 C CB  . LEU A 348 ? 0.4032 0.3100 0.2982 0.0014  0.0591  -0.0751 348 LEU A CB  
1450 C CG  . LEU A 348 ? 0.4426 0.3173 0.3253 -0.0014 0.0612  -0.0767 348 LEU A CG  
1451 C CD1 . LEU A 348 ? 0.4422 0.3173 0.3306 -0.0189 0.0563  -0.0764 348 LEU A CD1 
1452 C CD2 . LEU A 348 ? 0.4840 0.3288 0.3440 0.0019  0.0669  -0.0852 348 LEU A CD2 
1453 N N   . GLN A 349 ? 0.3435 0.3161 0.2650 0.0147  0.0583  -0.0667 349 GLN A N   
1454 C CA  . GLN A 349 ? 0.3177 0.3178 0.2483 0.0120  0.0570  -0.0647 349 GLN A CA  
1455 C C   . GLN A 349 ? 0.2860 0.3102 0.2317 0.0177  0.0565  -0.0579 349 GLN A C   
1456 O O   . GLN A 349 ? 0.2747 0.2975 0.2273 0.0182  0.0542  -0.0538 349 GLN A O   
1457 C CB  . GLN A 349 ? 0.3287 0.3347 0.2642 -0.0031 0.0513  -0.0639 349 GLN A CB  
1458 C CG  . GLN A 349 ? 0.3642 0.3529 0.2868 -0.0113 0.0503  -0.0706 349 GLN A CG  
1459 C CD  . GLN A 349 ? 0.4000 0.3912 0.3116 -0.0094 0.0535  -0.0762 349 GLN A CD  
1460 O OE1 . GLN A 349 ? 0.3806 0.3861 0.2934 -0.0011 0.0573  -0.0751 349 GLN A OE1 
1461 N NE2 . GLN A 349 ? 0.4159 0.3947 0.3160 -0.0175 0.0520  -0.0825 349 GLN A NE2 
1462 N N   . THR A 350 ? 0.2755 0.3231 0.2258 0.0214  0.0590  -0.0570 350 THR A N   
1463 C CA  . THR A 350 ? 0.2619 0.3365 0.2271 0.0234  0.0581  -0.0511 350 THR A CA  
1464 C C   . THR A 350 ? 0.2532 0.3479 0.2234 0.0140  0.0575  -0.0495 350 THR A C   
1465 O O   . THR A 350 ? 0.2608 0.3638 0.2254 0.0172  0.0618  -0.0523 350 THR A O   
1466 C CB  . THR A 350 ? 0.2855 0.3712 0.2514 0.0395  0.0629  -0.0509 350 THR A CB  
1467 O OG1 . THR A 350 ? 0.3017 0.3663 0.2620 0.0479  0.0631  -0.0508 350 THR A OG1 
1468 C CG2 . THR A 350 ? 0.2779 0.3965 0.2600 0.0391  0.0616  -0.0455 350 THR A CG2 
1469 N N   . PHE A 351 ? 0.2293 0.3287 0.2078 0.0023  0.0523  -0.0452 351 PHE A N   
1470 C CA  . PHE A 351 ? 0.2185 0.3320 0.2000 -0.0076 0.0513  -0.0425 351 PHE A CA  
1471 C C   . PHE A 351 ? 0.2069 0.3461 0.2003 -0.0086 0.0522  -0.0379 351 PHE A C   
1472 O O   . PHE A 351 ? 0.2034 0.3458 0.2056 -0.0109 0.0488  -0.0348 351 PHE A O   
1473 C CB  . PHE A 351 ? 0.2175 0.3193 0.1991 -0.0188 0.0455  -0.0404 351 PHE A CB  
1474 C CG  . PHE A 351 ? 0.2329 0.3133 0.2045 -0.0202 0.0437  -0.0448 351 PHE A CG  
1475 C CD1 . PHE A 351 ? 0.2428 0.3178 0.2027 -0.0184 0.0466  -0.0500 351 PHE A CD1 
1476 C CD2 . PHE A 351 ? 0.2364 0.3039 0.2101 -0.0244 0.0392  -0.0441 351 PHE A CD2 
1477 C CE1 . PHE A 351 ? 0.2581 0.3153 0.2086 -0.0219 0.0445  -0.0547 351 PHE A CE1 
1478 C CE2 . PHE A 351 ? 0.2529 0.3044 0.2184 -0.0277 0.0375  -0.0483 351 PHE A CE2 
1479 C CZ  . PHE A 351 ? 0.2509 0.2974 0.2049 -0.0271 0.0399  -0.0537 351 PHE A CZ  
1480 N N   . THR A 352 ? 0.2004 0.3590 0.1939 -0.0082 0.0567  -0.0378 352 THR A N   
1481 C CA  . THR A 352 ? 0.2031 0.3900 0.2081 -0.0109 0.0582  -0.0339 352 THR A CA  
1482 C C   . THR A 352 ? 0.1980 0.3929 0.2044 -0.0259 0.0573  -0.0295 352 THR A C   
1483 O O   . THR A 352 ? 0.1985 0.4173 0.2129 -0.0307 0.0594  -0.0266 352 THR A O   
1484 C CB  . THR A 352 ? 0.2437 0.4513 0.2488 0.0003  0.0649  -0.0362 352 THR A CB  
1485 O OG1 . THR A 352 ? 0.2690 0.4736 0.2633 -0.0009 0.0687  -0.0387 352 THR A OG1 
1486 C CG2 . THR A 352 ? 0.2705 0.4701 0.2728 0.0170  0.0666  -0.0398 352 THR A CG2 
1487 N N   . GLN A 353 ? 0.1908 0.3667 0.1884 -0.0329 0.0547  -0.0289 353 GLN A N   
1488 C CA  . GLN A 353 ? 0.1931 0.3726 0.1878 -0.0451 0.0547  -0.0244 353 GLN A CA  
1489 C C   . GLN A 353 ? 0.1821 0.3627 0.1837 -0.0558 0.0512  -0.0194 353 GLN A C   
1490 O O   . GLN A 353 ? 0.2021 0.3898 0.2021 -0.0659 0.0529  -0.0152 353 GLN A O   
1491 C CB  . GLN A 353 ? 0.2180 0.3784 0.2000 -0.0472 0.0528  -0.0251 353 GLN A CB  
1492 C CG  . GLN A 353 ? 0.2322 0.3921 0.2046 -0.0389 0.0568  -0.0307 353 GLN A CG  
1493 C CD  . GLN A 353 ? 0.2623 0.4054 0.2314 -0.0299 0.0553  -0.0369 353 GLN A CD  
1494 O OE1 . GLN A 353 ? 0.2412 0.3784 0.2173 -0.0266 0.0529  -0.0372 353 GLN A OE1 
1495 N NE2 . GLN A 353 ? 0.2791 0.4134 0.2363 -0.0261 0.0570  -0.0421 353 GLN A NE2 
1496 N N   . HIS A 354 ? 0.1777 0.3496 0.1854 -0.0541 0.0466  -0.0199 354 HIS A N   
1497 C CA  . HIS A 354 ? 0.1815 0.3543 0.1945 -0.0642 0.0436  -0.0161 354 HIS A CA  
1498 C C   . HIS A 354 ? 0.2014 0.4023 0.2244 -0.0672 0.0467  -0.0154 354 HIS A C   
1499 O O   . HIS A 354 ? 0.2191 0.4359 0.2484 -0.0574 0.0487  -0.0181 354 HIS A O   
1500 C CB  . HIS A 354 ? 0.1643 0.3218 0.1803 -0.0616 0.0382  -0.0170 354 HIS A CB  
1501 C CG  . HIS A 354 ? 0.1744 0.3080 0.1826 -0.0617 0.0346  -0.0168 354 HIS A CG  
1502 N ND1 . HIS A 354 ? 0.1934 0.3152 0.1962 -0.0701 0.0322  -0.0129 354 HIS A ND1 
1503 C CD2 . HIS A 354 ? 0.1763 0.2969 0.1817 -0.0545 0.0329  -0.0199 354 HIS A CD2 
1504 C CE1 . HIS A 354 ? 0.2008 0.3062 0.1991 -0.0665 0.0289  -0.0138 354 HIS A CE1 
1505 N NE2 . HIS A 354 ? 0.1956 0.3005 0.1956 -0.0583 0.0292  -0.0181 354 HIS A NE2 
1506 N N   . GLN A 355 ? 0.1997 0.4067 0.2231 -0.0807 0.0472  -0.0117 355 GLN A N   
1507 C CA  . GLN A 355 ? 0.2122 0.4489 0.2455 -0.0868 0.0500  -0.0111 355 GLN A CA  
1508 C C   . GLN A 355 ? 0.2075 0.4426 0.2466 -0.0941 0.0452  -0.0108 355 GLN A C   
1509 O O   . GLN A 355 ? 0.2131 0.4578 0.2543 -0.1082 0.0457  -0.0088 355 GLN A O   
1510 C CB  . GLN A 355 ? 0.2526 0.4988 0.2812 -0.0992 0.0549  -0.0073 355 GLN A CB  
1511 C CG  . GLN A 355 ? 0.3458 0.5887 0.3651 -0.0930 0.0592  -0.0073 355 GLN A CG  
1512 C CD  . GLN A 355 ? 0.4262 0.6945 0.4515 -0.0807 0.0640  -0.0111 355 GLN A CD  
1513 O OE1 . GLN A 355 ? 0.4576 0.7566 0.4904 -0.0843 0.0687  -0.0104 355 GLN A OE1 
1514 N NE2 . GLN A 355 ? 0.4343 0.6905 0.4559 -0.0660 0.0632  -0.0152 355 GLN A NE2 
1515 N N   . GLY A 356 ? 0.2127 0.4351 0.2534 -0.0852 0.0408  -0.0130 356 GLY A N   
1516 C CA  . GLY A 356 ? 0.2015 0.4213 0.2466 -0.0898 0.0361  -0.0135 356 GLY A CA  
1517 C C   . GLY A 356 ? 0.1947 0.4009 0.2403 -0.0771 0.0324  -0.0158 356 GLY A C   
1518 O O   . GLY A 356 ? 0.1871 0.3826 0.2288 -0.0665 0.0334  -0.0169 356 GLY A O   
1519 N N   . ALA A 357 ? 0.1765 0.3824 0.2260 -0.0792 0.0282  -0.0166 357 ALA A N   
1520 C CA  . ALA A 357 ? 0.1741 0.3675 0.2235 -0.0682 0.0250  -0.0180 357 ALA A CA  
1521 C C   . ALA A 357 ? 0.1819 0.3456 0.2225 -0.0660 0.0238  -0.0177 357 ALA A C   
1522 O O   . ALA A 357 ? 0.1963 0.3459 0.2308 -0.0746 0.0232  -0.0160 357 ALA A O   
1523 C CB  . ALA A 357 ? 0.1793 0.3761 0.2323 -0.0730 0.0207  -0.0188 357 ALA A CB  
1524 N N   . VAL A 358 ? 0.1672 0.3218 0.2065 -0.0546 0.0238  -0.0190 358 VAL A N   
1525 C CA  . VAL A 358 ? 0.1720 0.3029 0.2043 -0.0529 0.0225  -0.0191 358 VAL A CA  
1526 C C   . VAL A 358 ? 0.1922 0.3115 0.2249 -0.0498 0.0191  -0.0195 358 VAL A C   
1527 O O   . VAL A 358 ? 0.2108 0.3278 0.2440 -0.0409 0.0196  -0.0206 358 VAL A O   
1528 C CB  . VAL A 358 ? 0.1902 0.3166 0.2181 -0.0456 0.0256  -0.0207 358 VAL A CB  
1529 C CG1 . VAL A 358 ? 0.2023 0.3080 0.2235 -0.0468 0.0238  -0.0210 358 VAL A CG1 
1530 C CG2 . VAL A 358 ? 0.2056 0.3460 0.2328 -0.0482 0.0296  -0.0204 358 VAL A CG2 
1531 N N   . LYS A 359 ? 0.1760 0.2868 0.2072 -0.0568 0.0161  -0.0186 359 LYS A N   
1532 C CA  . LYS A 359 ? 0.1802 0.2799 0.2108 -0.0538 0.0133  -0.0191 359 LYS A CA  
1533 C C   . LYS A 359 ? 0.1789 0.2609 0.2044 -0.0523 0.0126  -0.0188 359 LYS A C   
1534 O O   . LYS A 359 ? 0.1933 0.2680 0.2187 -0.0476 0.0117  -0.0194 359 LYS A O   
1535 C CB  . LYS A 359 ? 0.1959 0.2945 0.2260 -0.0615 0.0105  -0.0190 359 LYS A CB  
1536 C CG  . LYS A 359 ? 0.2201 0.3105 0.2495 -0.0578 0.0080  -0.0198 359 LYS A CG  
1537 C CD  . LYS A 359 ? 0.2381 0.3250 0.2647 -0.0654 0.0055  -0.0207 359 LYS A CD  
1538 C CE  . LYS A 359 ? 0.2453 0.3233 0.2700 -0.0608 0.0035  -0.0217 359 LYS A CE  
1539 N NZ  . LYS A 359 ? 0.2289 0.3052 0.2502 -0.0671 0.0011  -0.0237 359 LYS A NZ  
1540 N N   . ALA A 360 ? 0.1749 0.2514 0.1959 -0.0566 0.0130  -0.0177 360 ALA A N   
1541 C CA  . ALA A 360 ? 0.1906 0.2542 0.2071 -0.0552 0.0117  -0.0173 360 ALA A CA  
1542 C C   . ALA A 360 ? 0.1818 0.2457 0.1976 -0.0508 0.0133  -0.0190 360 ALA A C   
1543 O O   . ALA A 360 ? 0.1859 0.2553 0.2000 -0.0511 0.0156  -0.0194 360 ALA A O   
1544 C CB  . ALA A 360 ? 0.2051 0.2622 0.2154 -0.0605 0.0111  -0.0147 360 ALA A CB  
1545 N N   . VAL A 361 ? 0.1790 0.2366 0.1954 -0.0473 0.0125  -0.0203 361 VAL A N   
1546 C CA  . VAL A 361 ? 0.1813 0.2359 0.1955 -0.0445 0.0142  -0.0228 361 VAL A CA  
1547 C C   . VAL A 361 ? 0.1764 0.2243 0.1901 -0.0452 0.0120  -0.0232 361 VAL A C   
1548 O O   . VAL A 361 ? 0.1660 0.2117 0.1824 -0.0440 0.0112  -0.0225 361 VAL A O   
1549 C CB  . VAL A 361 ? 0.2069 0.2623 0.2226 -0.0392 0.0167  -0.0242 361 VAL A CB  
1550 C CG1 . VAL A 361 ? 0.2270 0.2740 0.2377 -0.0371 0.0188  -0.0272 361 VAL A CG1 
1551 C CG2 . VAL A 361 ? 0.2098 0.2769 0.2279 -0.0370 0.0186  -0.0237 361 VAL A CG2 
1552 N N   . ALA A 362 ? 0.1677 0.2146 0.1780 -0.0472 0.0111  -0.0242 362 ALA A N   
1553 C CA  . ALA A 362 ? 0.1654 0.2108 0.1765 -0.0482 0.0090  -0.0247 362 ALA A CA  
1554 C C   . ALA A 362 ? 0.1712 0.2176 0.1785 -0.0508 0.0087  -0.0276 362 ALA A C   
1555 O O   . ALA A 362 ? 0.1759 0.2249 0.1789 -0.0516 0.0083  -0.0276 362 ALA A O   
1556 C CB  . ALA A 362 ? 0.1743 0.2211 0.1857 -0.0478 0.0060  -0.0215 362 ALA A CB  
1557 N N   . TRP A 363 ? 0.1670 0.2113 0.1748 -0.0530 0.0090  -0.0302 363 TRP A N   
1558 C CA  . TRP A 363 ? 0.1769 0.2220 0.1803 -0.0574 0.0085  -0.0342 363 TRP A CA  
1559 C C   . TRP A 363 ? 0.1879 0.2437 0.1933 -0.0593 0.0044  -0.0334 363 TRP A C   
1560 O O   . TRP A 363 ? 0.1948 0.2553 0.2056 -0.0578 0.0028  -0.0309 363 TRP A O   
1561 C CB  . TRP A 363 ? 0.1851 0.2217 0.1869 -0.0607 0.0112  -0.0377 363 TRP A CB  
1562 C CG  . TRP A 363 ? 0.1940 0.2187 0.1916 -0.0570 0.0155  -0.0386 363 TRP A CG  
1563 C CD1 . TRP A 363 ? 0.2069 0.2273 0.2071 -0.0522 0.0174  -0.0358 363 TRP A CD1 
1564 C CD2 . TRP A 363 ? 0.1949 0.2117 0.1841 -0.0563 0.0183  -0.0426 363 TRP A CD2 
1565 N NE1 . TRP A 363 ? 0.2215 0.2329 0.2160 -0.0478 0.0211  -0.0373 363 TRP A NE1 
1566 C CE2 . TRP A 363 ? 0.2101 0.2183 0.1976 -0.0499 0.0220  -0.0416 363 TRP A CE2 
1567 C CE3 . TRP A 363 ? 0.2083 0.2246 0.1903 -0.0600 0.0180  -0.0472 363 TRP A CE3 
1568 C CZ2 . TRP A 363 ? 0.2219 0.2204 0.2008 -0.0459 0.0259  -0.0449 363 TRP A CZ2 
1569 C CZ3 . TRP A 363 ? 0.2200 0.2260 0.1931 -0.0570 0.0220  -0.0510 363 TRP A CZ3 
1570 C CH2 . TRP A 363 ? 0.2296 0.2264 0.2012 -0.0495 0.0260  -0.0498 363 TRP A CH2 
1571 N N   . CYS A 364 ? 0.1897 0.2505 0.1901 -0.0622 0.0027  -0.0359 364 CYS A N   
1572 C CA  . CYS A 364 ? 0.1908 0.2647 0.1926 -0.0631 -0.0018 -0.0352 364 CYS A CA  
1573 C C   . CYS A 364 ? 0.1940 0.2735 0.2004 -0.0688 -0.0021 -0.0384 364 CYS A C   
1574 O O   . CYS A 364 ? 0.2001 0.2738 0.2030 -0.0755 -0.0001 -0.0434 364 CYS A O   
1575 C CB  . CYS A 364 ? 0.1956 0.2746 0.1899 -0.0648 -0.0037 -0.0372 364 CYS A CB  
1576 S SG  . CYS A 364 ? 0.2428 0.3418 0.2381 -0.0655 -0.0099 -0.0367 364 CYS A SG  
1577 N N   . PRO A 365 ? 0.2078 0.2979 0.2213 -0.0664 -0.0042 -0.0355 365 PRO A N   
1578 C CA  . PRO A 365 ? 0.2211 0.3193 0.2400 -0.0726 -0.0039 -0.0380 365 PRO A CA  
1579 C C   . PRO A 365 ? 0.2529 0.3644 0.2706 -0.0811 -0.0066 -0.0429 365 PRO A C   
1580 O O   . PRO A 365 ? 0.2619 0.3773 0.2823 -0.0897 -0.0053 -0.0462 365 PRO A O   
1581 C CB  . PRO A 365 ? 0.2192 0.3290 0.2455 -0.0660 -0.0057 -0.0335 365 PRO A CB  
1582 C CG  . PRO A 365 ? 0.2205 0.3206 0.2440 -0.0571 -0.0058 -0.0290 365 PRO A CG  
1583 C CD  . PRO A 365 ? 0.2002 0.2941 0.2160 -0.0580 -0.0063 -0.0299 365 PRO A CD  
1584 N N   . TRP A 366 ? 0.2572 0.3765 0.2703 -0.0794 -0.0103 -0.0432 366 TRP A N   
1585 C CA  . TRP A 366 ? 0.2733 0.4080 0.2848 -0.0876 -0.0137 -0.0483 366 TRP A CA  
1586 C C   . TRP A 366 ? 0.2970 0.4210 0.2971 -0.0932 -0.0130 -0.0539 366 TRP A C   
1587 O O   . TRP A 366 ? 0.3040 0.4408 0.3006 -0.0999 -0.0165 -0.0586 366 TRP A O   
1588 C CB  . TRP A 366 ? 0.2725 0.4310 0.2875 -0.0813 -0.0196 -0.0447 366 TRP A CB  
1589 C CG  . TRP A 366 ? 0.2887 0.4427 0.2964 -0.0722 -0.0214 -0.0404 366 TRP A CG  
1590 C CD1 . TRP A 366 ? 0.3077 0.4656 0.3065 -0.0736 -0.0241 -0.0423 366 TRP A CD1 
1591 C CD2 . TRP A 366 ? 0.2868 0.4314 0.2941 -0.0613 -0.0206 -0.0334 366 TRP A CD2 
1592 N NE1 . TRP A 366 ? 0.3143 0.4649 0.3072 -0.0642 -0.0244 -0.0362 366 TRP A NE1 
1593 C CE2 . TRP A 366 ? 0.3006 0.4429 0.2985 -0.0570 -0.0224 -0.0308 366 TRP A CE2 
1594 C CE3 . TRP A 366 ? 0.2844 0.4224 0.2973 -0.0553 -0.0184 -0.0293 366 TRP A CE3 
1595 C CZ2 . TRP A 366 ? 0.3076 0.4390 0.3014 -0.0482 -0.0217 -0.0241 366 TRP A CZ2 
1596 C CZ3 . TRP A 366 ? 0.2970 0.4244 0.3057 -0.0463 -0.0182 -0.0234 366 TRP A CZ3 
1597 C CH2 . TRP A 366 ? 0.3068 0.4302 0.3060 -0.0435 -0.0196 -0.0208 366 TRP A CH2 
1598 N N   . GLN A 367 ? 0.3081 0.4105 0.3022 -0.0903 -0.0085 -0.0538 367 GLN A N   
1599 C CA  . GLN A 367 ? 0.3263 0.4169 0.3087 -0.0939 -0.0067 -0.0594 367 GLN A CA  
1600 C C   . GLN A 367 ? 0.3381 0.4056 0.3173 -0.0931 -0.0004 -0.0606 367 GLN A C   
1601 O O   . GLN A 367 ? 0.3386 0.3992 0.3194 -0.0848 0.0018  -0.0560 367 GLN A O   
1602 C CB  . GLN A 367 ? 0.3556 0.4485 0.3325 -0.0866 -0.0081 -0.0563 367 GLN A CB  
1603 C CG  . GLN A 367 ? 0.4116 0.5253 0.3899 -0.0844 -0.0141 -0.0534 367 GLN A CG  
1604 C CD  . GLN A 367 ? 0.5015 0.6142 0.4708 -0.0793 -0.0146 -0.0511 367 GLN A CD  
1605 O OE1 . GLN A 367 ? 0.5382 0.6455 0.5079 -0.0718 -0.0132 -0.0446 367 GLN A OE1 
1606 N NE2 . GLN A 367 ? 0.5175 0.6349 0.4775 -0.0844 -0.0163 -0.0567 367 GLN A NE2 
1607 N N   . SER A 368 ? 0.3337 0.3888 0.3068 -0.1016 0.0024  -0.0669 368 SER A N   
1608 C CA  . SER A 368 ? 0.3505 0.3821 0.3191 -0.1004 0.0084  -0.0678 368 SER A CA  
1609 C C   . SER A 368 ? 0.3387 0.3586 0.3028 -0.0899 0.0119  -0.0658 368 SER A C   
1610 O O   . SER A 368 ? 0.3502 0.3614 0.3177 -0.0836 0.0151  -0.0618 368 SER A O   
1611 C CB  . SER A 368 ? 0.4108 0.4274 0.3681 -0.1115 0.0109  -0.0761 368 SER A CB  
1612 O OG  . SER A 368 ? 0.4894 0.4794 0.4382 -0.1083 0.0171  -0.0771 368 SER A OG  
1613 N N   . ASN A 369 ? 0.3119 0.3334 0.2684 -0.0882 0.0115  -0.0687 369 ASN A N   
1614 C CA  . ASN A 369 ? 0.3046 0.3176 0.2558 -0.0795 0.0154  -0.0681 369 ASN A CA  
1615 C C   . ASN A 369 ? 0.2718 0.2987 0.2294 -0.0724 0.0137  -0.0615 369 ASN A C   
1616 O O   . ASN A 369 ? 0.2832 0.3075 0.2366 -0.0666 0.0169  -0.0613 369 ASN A O   
1617 C CB  . ASN A 369 ? 0.3439 0.3491 0.2807 -0.0823 0.0170  -0.0759 369 ASN A CB  
1618 C CG  . ASN A 369 ? 0.4257 0.4113 0.3527 -0.0899 0.0197  -0.0832 369 ASN A CG  
1619 O OD1 . ASN A 369 ? 0.4503 0.4207 0.3778 -0.0884 0.0233  -0.0819 369 ASN A OD1 
1620 N ND2 . ASN A 369 ? 0.4624 0.4472 0.3793 -0.0987 0.0180  -0.0909 369 ASN A ND2 
1621 N N   . VAL A 370 ? 0.2291 0.2701 0.1954 -0.0729 0.0092  -0.0564 370 VAL A N   
1622 C CA  . VAL A 370 ? 0.2090 0.2593 0.1786 -0.0674 0.0079  -0.0501 370 VAL A CA  
1623 C C   . VAL A 370 ? 0.1905 0.2386 0.1687 -0.0626 0.0093  -0.0447 370 VAL A C   
1624 O O   . VAL A 370 ? 0.1837 0.2321 0.1687 -0.0634 0.0080  -0.0430 370 VAL A O   
1625 C CB  . VAL A 370 ? 0.2078 0.2725 0.1782 -0.0690 0.0023  -0.0476 370 VAL A CB  
1626 C CG1 . VAL A 370 ? 0.2015 0.2707 0.1733 -0.0635 0.0015  -0.0403 370 VAL A CG1 
1627 C CG2 . VAL A 370 ? 0.2229 0.2920 0.1834 -0.0735 0.0006  -0.0532 370 VAL A CG2 
1628 N N   . LEU A 371 ? 0.1935 0.2409 0.1713 -0.0580 0.0121  -0.0422 371 LEU A N   
1629 C CA  . LEU A 371 ? 0.1858 0.2325 0.1708 -0.0543 0.0134  -0.0378 371 LEU A CA  
1630 C C   . LEU A 371 ? 0.1841 0.2377 0.1702 -0.0533 0.0125  -0.0325 371 LEU A C   
1631 O O   . LEU A 371 ? 0.1858 0.2430 0.1661 -0.0536 0.0136  -0.0324 371 LEU A O   
1632 C CB  . LEU A 371 ? 0.1953 0.2358 0.1785 -0.0503 0.0182  -0.0402 371 LEU A CB  
1633 C CG  . LEU A 371 ? 0.2053 0.2483 0.1953 -0.0459 0.0197  -0.0363 371 LEU A CG  
1634 C CD1 . LEU A 371 ? 0.2123 0.2512 0.2082 -0.0461 0.0180  -0.0346 371 LEU A CD1 
1635 C CD2 . LEU A 371 ? 0.2179 0.2588 0.2054 -0.0399 0.0244  -0.0385 371 LEU A CD2 
1636 N N   . ALA A 372 ? 0.1719 0.2258 0.1639 -0.0525 0.0110  -0.0281 372 ALA A N   
1637 C CA  . ALA A 372 ? 0.1768 0.2332 0.1682 -0.0529 0.0109  -0.0233 372 ALA A CA  
1638 C C   . ALA A 372 ? 0.1738 0.2312 0.1707 -0.0519 0.0134  -0.0226 372 ALA A C   
1639 O O   . ALA A 372 ? 0.1747 0.2295 0.1766 -0.0500 0.0133  -0.0236 372 ALA A O   
1640 C CB  . ALA A 372 ? 0.1860 0.2402 0.1779 -0.0528 0.0072  -0.0195 372 ALA A CB  
1641 N N   . THR A 373 ? 0.1620 0.2248 0.1576 -0.0534 0.0158  -0.0207 373 THR A N   
1642 C CA  . THR A 373 ? 0.1699 0.2382 0.1712 -0.0535 0.0177  -0.0199 373 THR A CA  
1643 C C   . THR A 373 ? 0.1846 0.2550 0.1842 -0.0592 0.0177  -0.0157 373 THR A C   
1644 O O   . THR A 373 ? 0.1949 0.2631 0.1876 -0.0619 0.0178  -0.0133 373 THR A O   
1645 C CB  . THR A 373 ? 0.1956 0.2720 0.1983 -0.0496 0.0216  -0.0228 373 THR A CB  
1646 O OG1 . THR A 373 ? 0.2150 0.2973 0.2123 -0.0511 0.0242  -0.0227 373 THR A OG1 
1647 C CG2 . THR A 373 ? 0.1962 0.2654 0.1981 -0.0442 0.0222  -0.0268 373 THR A CG2 
1648 N N   . GLY A 374 ? 0.1752 0.2492 0.1798 -0.0616 0.0178  -0.0148 374 GLY A N   
1649 C CA  . GLY A 374 ? 0.1842 0.2579 0.1860 -0.0691 0.0182  -0.0113 374 GLY A CA  
1650 C C   . GLY A 374 ? 0.1985 0.2867 0.2070 -0.0726 0.0201  -0.0120 374 GLY A C   
1651 O O   . GLY A 374 ? 0.2112 0.3047 0.2263 -0.0687 0.0192  -0.0142 374 GLY A O   
1652 N N   . GLY A 375 ? 0.1924 0.2887 0.1989 -0.0798 0.0229  -0.0098 375 GLY A N   
1653 C CA  . GLY A 375 ? 0.1964 0.3118 0.2103 -0.0842 0.0249  -0.0106 375 GLY A CA  
1654 C C   . GLY A 375 ? 0.2140 0.3260 0.2269 -0.0949 0.0235  -0.0092 375 GLY A C   
1655 O O   . GLY A 375 ? 0.2253 0.3174 0.2294 -0.0996 0.0220  -0.0069 375 GLY A O   
1656 N N   . GLY A 376 ? 0.2065 0.3385 0.2277 -0.0987 0.0241  -0.0108 376 GLY A N   
1657 C CA  . GLY A 376 ? 0.2227 0.3546 0.2435 -0.1104 0.0227  -0.0108 376 GLY A CA  
1658 C C   . GLY A 376 ? 0.2263 0.3562 0.2402 -0.1246 0.0257  -0.0077 376 GLY A C   
1659 O O   . GLY A 376 ? 0.2299 0.3536 0.2371 -0.1249 0.0286  -0.0045 376 GLY A O   
1660 N N   . THR A 377 ? 0.2274 0.3629 0.2421 -0.1374 0.0252  -0.0086 377 THR A N   
1661 C CA  . THR A 377 ? 0.2438 0.3737 0.2502 -0.1541 0.0282  -0.0057 377 THR A CA  
1662 C C   . THR A 377 ? 0.2433 0.3922 0.2515 -0.1582 0.0338  -0.0028 377 THR A C   
1663 O O   . THR A 377 ? 0.2628 0.3970 0.2594 -0.1670 0.0369  0.0016  377 THR A O   
1664 C CB  . THR A 377 ? 0.2656 0.4034 0.2745 -0.1679 0.0265  -0.0088 377 THR A CB  
1665 O OG1 . THR A 377 ? 0.2827 0.4016 0.2883 -0.1629 0.0217  -0.0117 377 THR A OG1 
1666 C CG2 . THR A 377 ? 0.2796 0.4056 0.2771 -0.1878 0.0298  -0.0060 377 THR A CG2 
1667 N N   . SER A 378 ? 0.2138 0.3950 0.2352 -0.1511 0.0354  -0.0049 378 SER A N   
1668 C CA  . SER A 378 ? 0.2152 0.4178 0.2387 -0.1538 0.0413  -0.0026 378 SER A CA  
1669 C C   . SER A 378 ? 0.2125 0.4020 0.2285 -0.1428 0.0433  -0.0004 378 SER A C   
1670 O O   . SER A 378 ? 0.2249 0.4280 0.2395 -0.1450 0.0485  0.0017  378 SER A O   
1671 C CB  . SER A 378 ? 0.2053 0.4478 0.2449 -0.1483 0.0426  -0.0058 378 SER A CB  
1672 O OG  . SER A 378 ? 0.2215 0.4629 0.2662 -0.1300 0.0396  -0.0088 378 SER A OG  
1673 N N   . ASP A 379 ? 0.2109 0.3771 0.2225 -0.1314 0.0393  -0.0014 379 ASP A N   
1674 C CA  . ASP A 379 ? 0.2151 0.3696 0.2200 -0.1210 0.0399  -0.0004 379 ASP A CA  
1675 C C   . ASP A 379 ? 0.2310 0.3539 0.2214 -0.1235 0.0379  0.0036  379 ASP A C   
1676 O O   . ASP A 379 ? 0.2376 0.3548 0.2181 -0.1259 0.0407  0.0074  379 ASP A O   
1677 C CB  . ASP A 379 ? 0.2251 0.3819 0.2368 -0.1054 0.0373  -0.0049 379 ASP A CB  
1678 C CG  . ASP A 379 ? 0.2690 0.4142 0.2732 -0.0966 0.0377  -0.0049 379 ASP A CG  
1679 O OD1 . ASP A 379 ? 0.2851 0.4430 0.2879 -0.0945 0.0421  -0.0050 379 ASP A OD1 
1680 O OD2 . ASP A 379 ? 0.2759 0.4002 0.2751 -0.0924 0.0338  -0.0049 379 ASP A OD2 
1681 N N   . ARG A 380 ? 0.2261 0.3297 0.2147 -0.1217 0.0331  0.0027  380 ARG A N   
1682 C CA  . ARG A 380 ? 0.2572 0.3313 0.2325 -0.1224 0.0308  0.0062  380 ARG A CA  
1683 C C   . ARG A 380 ? 0.2739 0.3384 0.2432 -0.1117 0.0295  0.0075  380 ARG A C   
1684 O O   . ARG A 380 ? 0.3048 0.3479 0.2621 -0.1114 0.0280  0.0115  380 ARG A O   
1685 C CB  . ARG A 380 ? 0.2965 0.3588 0.2592 -0.1364 0.0341  0.0117  380 ARG A CB  
1686 C CG  . ARG A 380 ? 0.3568 0.4318 0.3238 -0.1515 0.0366  0.0109  380 ARG A CG  
1687 C CD  . ARG A 380 ? 0.4399 0.5027 0.3927 -0.1665 0.0411  0.0169  380 ARG A CD  
1688 N NE  . ARG A 380 ? 0.5078 0.5696 0.4522 -0.1630 0.0445  0.0219  380 ARG A NE  
1689 C CZ  . ARG A 380 ? 0.5638 0.6489 0.5114 -0.1681 0.0499  0.0233  380 ARG A CZ  
1690 N NH1 . ARG A 380 ? 0.5758 0.6581 0.5138 -0.1643 0.0526  0.0276  380 ARG A NH1 
1691 N NH2 . ARG A 380 ? 0.5502 0.6635 0.5103 -0.1768 0.0525  0.0203  380 ARG A NH2 
1692 N N   . HIS A 381 ? 0.2456 0.3250 0.2216 -0.1031 0.0300  0.0042  381 HIS A N   
1693 C CA  . HIS A 381 ? 0.2461 0.3182 0.2159 -0.0948 0.0286  0.0046  381 HIS A CA  
1694 C C   . HIS A 381 ? 0.2319 0.3003 0.2074 -0.0849 0.0244  0.0003  381 HIS A C   
1695 O O   . HIS A 381 ? 0.2224 0.2993 0.2079 -0.0819 0.0240  -0.0037 381 HIS A O   
1696 C CB  . HIS A 381 ? 0.2457 0.3333 0.2143 -0.0933 0.0327  0.0039  381 HIS A CB  
1697 C CG  . HIS A 381 ? 0.2847 0.3733 0.2435 -0.1018 0.0369  0.0093  381 HIS A CG  
1698 N ND1 . HIS A 381 ? 0.2968 0.3919 0.2572 -0.1132 0.0403  0.0118  381 HIS A ND1 
1699 C CD2 . HIS A 381 ? 0.3104 0.3953 0.2574 -0.1010 0.0383  0.0127  381 HIS A CD2 
1700 C CE1 . HIS A 381 ? 0.3194 0.4133 0.2687 -0.1193 0.0442  0.0169  381 HIS A CE1 
1701 N NE2 . HIS A 381 ? 0.3250 0.4131 0.2658 -0.1116 0.0432  0.0178  381 HIS A NE2 
1702 N N   . ILE A 382 ? 0.2240 0.2809 0.1925 -0.0800 0.0215  0.0016  382 ILE A N   
1703 C CA  . ILE A 382 ? 0.2064 0.2621 0.1788 -0.0720 0.0181  -0.0021 382 ILE A CA  
1704 C C   . ILE A 382 ? 0.2083 0.2723 0.1775 -0.0692 0.0195  -0.0044 382 ILE A C   
1705 O O   . ILE A 382 ? 0.2266 0.2897 0.1862 -0.0708 0.0204  -0.0011 382 ILE A O   
1706 C CB  . ILE A 382 ? 0.2261 0.2675 0.1927 -0.0687 0.0139  0.0007  382 ILE A CB  
1707 C CG1 . ILE A 382 ? 0.2497 0.2804 0.2178 -0.0708 0.0127  0.0020  382 ILE A CG1 
1708 C CG2 . ILE A 382 ? 0.2200 0.2646 0.1905 -0.0620 0.0108  -0.0032 382 ILE A CG2 
1709 C CD1 . ILE A 382 ? 0.2729 0.2874 0.2322 -0.0665 0.0095  0.0058  382 ILE A CD1 
1710 N N   . ARG A 383 ? 0.1960 0.2665 0.1714 -0.0649 0.0201  -0.0099 383 ARG A N   
1711 C CA  . ARG A 383 ? 0.2009 0.2766 0.1719 -0.0622 0.0215  -0.0135 383 ARG A CA  
1712 C C   . ARG A 383 ? 0.2011 0.2718 0.1734 -0.0583 0.0182  -0.0179 383 ARG A C   
1713 O O   . ARG A 383 ? 0.1998 0.2672 0.1793 -0.0566 0.0169  -0.0194 383 ARG A O   
1714 C CB  . ARG A 383 ? 0.2092 0.2962 0.1837 -0.0608 0.0266  -0.0167 383 ARG A CB  
1715 C CG  . ARG A 383 ? 0.2013 0.2978 0.1731 -0.0658 0.0307  -0.0128 383 ARG A CG  
1716 C CD  . ARG A 383 ? 0.2201 0.3317 0.1976 -0.0632 0.0356  -0.0159 383 ARG A CD  
1717 N NE  . ARG A 383 ? 0.2305 0.3550 0.2057 -0.0689 0.0402  -0.0124 383 ARG A NE  
1718 C CZ  . ARG A 383 ? 0.2582 0.3894 0.2255 -0.0683 0.0440  -0.0128 383 ARG A CZ  
1719 N NH1 . ARG A 383 ? 0.2644 0.4087 0.2302 -0.0743 0.0487  -0.0091 383 ARG A NH1 
1720 N NH2 . ARG A 383 ? 0.2672 0.3928 0.2276 -0.0622 0.0434  -0.0173 383 ARG A NH2 
1721 N N   . ILE A 384 ? 0.1991 0.2702 0.1640 -0.0577 0.0168  -0.0198 384 ILE A N   
1722 C CA  . ILE A 384 ? 0.2001 0.2684 0.1657 -0.0563 0.0136  -0.0245 384 ILE A CA  
1723 C C   . ILE A 384 ? 0.1994 0.2689 0.1600 -0.0555 0.0167  -0.0310 384 ILE A C   
1724 O O   . ILE A 384 ? 0.2071 0.2813 0.1601 -0.0557 0.0190  -0.0311 384 ILE A O   
1725 C CB  . ILE A 384 ? 0.2187 0.2879 0.1789 -0.0566 0.0087  -0.0220 384 ILE A CB  
1726 C CG1 . ILE A 384 ? 0.2165 0.2817 0.1777 -0.0558 0.0066  -0.0150 384 ILE A CG1 
1727 C CG2 . ILE A 384 ? 0.2363 0.3067 0.1985 -0.0570 0.0054  -0.0272 384 ILE A CG2 
1728 C CD1 . ILE A 384 ? 0.2351 0.2957 0.2059 -0.0547 0.0056  -0.0150 384 ILE A CD1 
1729 N N   . TRP A 385 ? 0.2008 0.2648 0.1642 -0.0543 0.0173  -0.0363 385 TRP A N   
1730 C CA  . TRP A 385 ? 0.2099 0.2704 0.1668 -0.0527 0.0208  -0.0430 385 TRP A CA  
1731 C C   . TRP A 385 ? 0.2220 0.2754 0.1747 -0.0558 0.0185  -0.0489 385 TRP A C   
1732 O O   . TRP A 385 ? 0.2152 0.2665 0.1739 -0.0582 0.0152  -0.0481 385 TRP A O   
1733 C CB  . TRP A 385 ? 0.2166 0.2730 0.1784 -0.0478 0.0250  -0.0441 385 TRP A CB  
1734 C CG  . TRP A 385 ? 0.2241 0.2894 0.1934 -0.0459 0.0268  -0.0386 385 TRP A CG  
1735 C CD1 . TRP A 385 ? 0.2306 0.2968 0.2089 -0.0467 0.0248  -0.0342 385 TRP A CD1 
1736 C CD2 . TRP A 385 ? 0.2200 0.2957 0.1881 -0.0437 0.0312  -0.0376 385 TRP A CD2 
1737 N NE1 . TRP A 385 ? 0.2334 0.3096 0.2161 -0.0461 0.0273  -0.0310 385 TRP A NE1 
1738 C CE2 . TRP A 385 ? 0.2277 0.3112 0.2049 -0.0445 0.0313  -0.0326 385 TRP A CE2 
1739 C CE3 . TRP A 385 ? 0.2354 0.3157 0.1953 -0.0411 0.0354  -0.0409 385 TRP A CE3 
1740 C CZ2 . TRP A 385 ? 0.2385 0.3361 0.2182 -0.0440 0.0354  -0.0306 385 TRP A CZ2 
1741 C CZ3 . TRP A 385 ? 0.2406 0.3352 0.2030 -0.0394 0.0398  -0.0385 385 TRP A CZ3 
1742 C CH2 . TRP A 385 ? 0.2421 0.3461 0.2148 -0.0414 0.0397  -0.0333 385 TRP A CH2 
1743 N N   . ASN A 386 ? 0.2267 0.2757 0.1689 -0.0561 0.0208  -0.0556 386 ASN A N   
1744 C CA  . ASN A 386 ? 0.2490 0.2876 0.1857 -0.0603 0.0199  -0.0628 386 ASN A CA  
1745 C C   . ASN A 386 ? 0.2755 0.3003 0.2090 -0.0547 0.0260  -0.0663 386 ASN A C   
1746 O O   . ASN A 386 ? 0.2872 0.3117 0.2138 -0.0494 0.0304  -0.0686 386 ASN A O   
1747 C CB  . ASN A 386 ? 0.2815 0.3226 0.2060 -0.0648 0.0182  -0.0686 386 ASN A CB  
1748 C CG  . ASN A 386 ? 0.3482 0.3775 0.2668 -0.0713 0.0175  -0.0766 386 ASN A CG  
1749 O OD1 . ASN A 386 ? 0.3537 0.3662 0.2673 -0.0695 0.0221  -0.0811 386 ASN A OD1 
1750 N ND2 . ASN A 386 ? 0.3692 0.4071 0.2882 -0.0790 0.0118  -0.0781 386 ASN A ND2 
1751 N N   . VAL A 387 ? 0.2785 0.2928 0.2168 -0.0544 0.0266  -0.0661 387 VAL A N   
1752 C CA  . VAL A 387 ? 0.2946 0.2952 0.2295 -0.0470 0.0322  -0.0679 387 VAL A CA  
1753 C C   . VAL A 387 ? 0.3272 0.3086 0.2462 -0.0472 0.0359  -0.0767 387 VAL A C   
1754 O O   . VAL A 387 ? 0.3393 0.3082 0.2525 -0.0386 0.0412  -0.0784 387 VAL A O   
1755 C CB  . VAL A 387 ? 0.2944 0.2894 0.2379 -0.0456 0.0319  -0.0638 387 VAL A CB  
1756 C CG1 . VAL A 387 ? 0.2835 0.2951 0.2407 -0.0451 0.0287  -0.0561 387 VAL A CG1 
1757 C CG2 . VAL A 387 ? 0.3149 0.2982 0.2557 -0.0543 0.0300  -0.0670 387 VAL A CG2 
1758 N N   A CYS A 388 ? 0.3338 0.3125 0.2447 -0.0564 0.0332  -0.0825 388 CYS A N   
1759 N N   B CYS A 388 ? 0.3336 0.3125 0.2449 -0.0564 0.0331  -0.0823 388 CYS A N   
1760 C CA  A CYS A 388 ? 0.3563 0.3148 0.2496 -0.0585 0.0365  -0.0921 388 CYS A CA  
1761 C CA  B CYS A 388 ? 0.3566 0.3161 0.2509 -0.0585 0.0363  -0.0917 388 CYS A CA  
1762 C C   A CYS A 388 ? 0.3555 0.3188 0.2384 -0.0536 0.0391  -0.0962 388 CYS A C   
1763 C C   B CYS A 388 ? 0.3569 0.3217 0.2418 -0.0523 0.0393  -0.0949 388 CYS A C   
1764 O O   A CYS A 388 ? 0.3697 0.3157 0.2388 -0.0478 0.0447  -0.1024 388 CYS A O   
1765 O O   B CYS A 388 ? 0.3727 0.3239 0.2477 -0.0435 0.0454  -0.0987 388 CYS A O   
1766 C CB  A CYS A 388 ? 0.3846 0.3382 0.2737 -0.0726 0.0324  -0.0974 388 CYS A CB  
1767 C CB  B CYS A 388 ? 0.3835 0.3414 0.2738 -0.0726 0.0316  -0.0968 388 CYS A CB  
1768 S SG  A CYS A 388 ? 0.4696 0.4100 0.3649 -0.0787 0.0322  -0.0951 388 CYS A SG  
1769 S SG  B CYS A 388 ? 0.4788 0.4110 0.3456 -0.0789 0.0350  -0.1099 388 CYS A SG  
1770 N N   . SER A 389 ? 0.3385 0.3236 0.2264 -0.0555 0.0355  -0.0927 389 SER A N   
1771 C CA  . SER A 389 ? 0.3379 0.3304 0.2164 -0.0509 0.0383  -0.0953 389 SER A CA  
1772 C C   . SER A 389 ? 0.3382 0.3434 0.2248 -0.0403 0.0425  -0.0886 389 SER A C   
1773 O O   . SER A 389 ? 0.3466 0.3568 0.2253 -0.0345 0.0469  -0.0909 389 SER A O   
1774 C CB  . SER A 389 ? 0.3421 0.3512 0.2192 -0.0586 0.0326  -0.0946 389 SER A CB  
1775 O OG  . SER A 389 ? 0.3446 0.3709 0.2365 -0.0586 0.0289  -0.0845 389 SER A OG  
1776 N N   . GLY A 390 ? 0.3195 0.3324 0.2216 -0.0389 0.0409  -0.0805 390 GLY A N   
1777 C CA  . GLY A 390 ? 0.3175 0.3458 0.2290 -0.0318 0.0438  -0.0739 390 GLY A CA  
1778 C C   . GLY A 390 ? 0.3067 0.3542 0.2222 -0.0361 0.0413  -0.0681 390 GLY A C   
1779 O O   . GLY A 390 ? 0.2977 0.3590 0.2201 -0.0329 0.0438  -0.0626 390 GLY A O   
1780 N N   . ALA A 391 ? 0.3052 0.3540 0.2156 -0.0438 0.0364  -0.0689 391 ALA A N   
1781 C CA  . ALA A 391 ? 0.2988 0.3625 0.2098 -0.0470 0.0340  -0.0628 391 ALA A CA  
1782 C C   . ALA A 391 ? 0.2708 0.3414 0.1950 -0.0485 0.0315  -0.0537 391 ALA A C   
1783 O O   . ALA A 391 ? 0.2588 0.3238 0.1913 -0.0501 0.0281  -0.0524 391 ALA A O   
1784 C CB  . ALA A 391 ? 0.3061 0.3702 0.2084 -0.0534 0.0286  -0.0655 391 ALA A CB  
1785 N N   . CYS A 392 ? 0.2499 0.3320 0.1751 -0.0487 0.0333  -0.0476 392 CYS A N   
1786 C CA  . CYS A 392 ? 0.2477 0.3337 0.1817 -0.0516 0.0308  -0.0392 392 CYS A CA  
1787 C C   . CYS A 392 ? 0.2637 0.3507 0.1903 -0.0554 0.0261  -0.0360 392 CYS A C   
1788 O O   . CYS A 392 ? 0.2776 0.3704 0.1941 -0.0561 0.0276  -0.0350 392 CYS A O   
1789 C CB  . CYS A 392 ? 0.2571 0.3537 0.1951 -0.0514 0.0356  -0.0342 392 CYS A CB  
1790 S SG  . CYS A 392 ? 0.3287 0.4255 0.2739 -0.0570 0.0325  -0.0246 392 CYS A SG  
1791 N N   . LEU A 393 ? 0.2577 0.3400 0.1883 -0.0569 0.0204  -0.0352 393 LEU A N   
1792 C CA  . LEU A 393 ? 0.2611 0.3460 0.1853 -0.0587 0.0150  -0.0323 393 LEU A CA  
1793 C C   . LEU A 393 ? 0.2649 0.3507 0.1879 -0.0590 0.0143  -0.0225 393 LEU A C   
1794 O O   . LEU A 393 ? 0.2712 0.3598 0.1848 -0.0589 0.0116  -0.0188 393 LEU A O   
1795 C CB  . LEU A 393 ? 0.2689 0.3511 0.1994 -0.0596 0.0096  -0.0348 393 LEU A CB  
1796 C CG  . LEU A 393 ? 0.2917 0.3691 0.2224 -0.0612 0.0103  -0.0440 393 LEU A CG  
1797 C CD1 . LEU A 393 ? 0.3047 0.3814 0.2429 -0.0635 0.0056  -0.0452 393 LEU A CD1 
1798 C CD2 . LEU A 393 ? 0.2988 0.3787 0.2166 -0.0631 0.0104  -0.0505 393 LEU A CD2 
1799 N N   . SER A 394 ? 0.2558 0.3383 0.1870 -0.0595 0.0166  -0.0184 394 SER A N   
1800 C CA  . SER A 394 ? 0.2641 0.3429 0.1927 -0.0611 0.0164  -0.0095 394 SER A CA  
1801 C C   . SER A 394 ? 0.2639 0.3420 0.2006 -0.0639 0.0206  -0.0075 394 SER A C   
1802 O O   . SER A 394 ? 0.2597 0.3385 0.2064 -0.0627 0.0213  -0.0117 394 SER A O   
1803 C CB  . SER A 394 ? 0.2965 0.3691 0.2269 -0.0588 0.0104  -0.0064 394 SER A CB  
1804 O OG  . SER A 394 ? 0.3545 0.4187 0.2800 -0.0594 0.0104  0.0019  394 SER A OG  
1805 N N   . ALA A 395 ? 0.2646 0.3418 0.1962 -0.0681 0.0235  -0.0010 395 ALA A N   
1806 C CA  . ALA A 395 ? 0.2700 0.3482 0.2090 -0.0728 0.0270  0.0010  395 ALA A CA  
1807 C C   . ALA A 395 ? 0.2892 0.3552 0.2199 -0.0773 0.0263  0.0092  395 ALA A C   
1808 O O   . ALA A 395 ? 0.3075 0.3717 0.2259 -0.0791 0.0277  0.0141  395 ALA A O   
1809 C CB  . ALA A 395 ? 0.2683 0.3611 0.2079 -0.0754 0.0334  -0.0005 395 ALA A CB  
1810 N N   . VAL A 396 ? 0.2875 0.3426 0.2226 -0.0780 0.0237  0.0108  396 VAL A N   
1811 C CA  . VAL A 396 ? 0.3085 0.3469 0.2333 -0.0813 0.0231  0.0182  396 VAL A CA  
1812 C C   . VAL A 396 ? 0.3071 0.3419 0.2366 -0.0896 0.0258  0.0190  396 VAL A C   
1813 O O   . VAL A 396 ? 0.2958 0.3352 0.2373 -0.0888 0.0246  0.0142  396 VAL A O   
1814 C CB  . VAL A 396 ? 0.3424 0.3684 0.2642 -0.0735 0.0173  0.0194  396 VAL A CB  
1815 C CG1 . VAL A 396 ? 0.3736 0.3785 0.2830 -0.0752 0.0172  0.0270  396 VAL A CG1 
1816 C CG2 . VAL A 396 ? 0.3528 0.3857 0.2697 -0.0666 0.0141  0.0185  396 VAL A CG2 
1817 N N   . ASP A 397 ? 0.3182 0.3440 0.2373 -0.0982 0.0292  0.0252  397 ASP A N   
1818 C CA  . ASP A 397 ? 0.3273 0.3494 0.2495 -0.1085 0.0315  0.0257  397 ASP A CA  
1819 C C   . ASP A 397 ? 0.3458 0.3441 0.2627 -0.1066 0.0278  0.0272  397 ASP A C   
1820 O O   . ASP A 397 ? 0.3815 0.3593 0.2833 -0.1042 0.0269  0.0331  397 ASP A O   
1821 C CB  . ASP A 397 ? 0.3457 0.3662 0.2570 -0.1204 0.0373  0.0317  397 ASP A CB  
1822 C CG  . ASP A 397 ? 0.3911 0.4152 0.3071 -0.1342 0.0406  0.0312  397 ASP A CG  
1823 O OD1 . ASP A 397 ? 0.3886 0.4122 0.3141 -0.1342 0.0377  0.0266  397 ASP A OD1 
1824 O OD2 . ASP A 397 ? 0.4357 0.4644 0.3456 -0.1457 0.0461  0.0353  397 ASP A OD2 
1825 N N   . ALA A 398 ? 0.3241 0.3248 0.2520 -0.1066 0.0258  0.0221  398 ALA A N   
1826 C CA  . ALA A 398 ? 0.3432 0.3224 0.2663 -0.1046 0.0228  0.0224  398 ALA A CA  
1827 C C   . ALA A 398 ? 0.3610 0.3251 0.2761 -0.1178 0.0254  0.0245  398 ALA A C   
1828 O O   . ALA A 398 ? 0.3813 0.3243 0.2897 -0.1168 0.0235  0.0244  398 ALA A O   
1829 C CB  . ALA A 398 ? 0.3317 0.3202 0.2692 -0.0977 0.0192  0.0158  398 ALA A CB  
1830 N N   . HIS A 399 ? 0.3527 0.3283 0.2683 -0.1307 0.0301  0.0257  399 HIS A N   
1831 C CA  . HIS A 399 ? 0.3698 0.3346 0.2781 -0.1467 0.0333  0.0273  399 HIS A CA  
1832 C C   . HIS A 399 ? 0.3705 0.3379 0.2877 -0.1517 0.0311  0.0210  399 HIS A C   
1833 O O   . HIS A 399 ? 0.3929 0.3442 0.3011 -0.1642 0.0325  0.0215  399 HIS A O   
1834 C CB  . HIS A 399 ? 0.4090 0.3378 0.2941 -0.1492 0.0346  0.0345  399 HIS A CB  
1835 C CG  . HIS A 399 ? 0.4691 0.3956 0.3436 -0.1443 0.0365  0.0414  399 HIS A CG  
1836 N ND1 . HIS A 399 ? 0.5065 0.4457 0.3785 -0.1551 0.0420  0.0451  399 HIS A ND1 
1837 C CD2 . HIS A 399 ? 0.4989 0.4148 0.3654 -0.1298 0.0336  0.0450  399 HIS A CD2 
1838 C CE1 . HIS A 399 ? 0.5163 0.4499 0.3774 -0.1468 0.0422  0.0508  399 HIS A CE1 
1839 N NE2 . HIS A 399 ? 0.5173 0.4377 0.3749 -0.1315 0.0369  0.0509  399 HIS A NE2 
1840 N N   . SER A 400 ? 0.3444 0.3311 0.2778 -0.1426 0.0279  0.0153  400 SER A N   
1841 C CA  . SER A 400 ? 0.3225 0.3154 0.2648 -0.1458 0.0255  0.0093  400 SER A CA  
1842 C C   . SER A 400 ? 0.2849 0.3043 0.2449 -0.1352 0.0234  0.0047  400 SER A C   
1843 O O   . SER A 400 ? 0.2802 0.3060 0.2433 -0.1247 0.0233  0.0055  400 SER A O   
1844 C CB  . SER A 400 ? 0.3556 0.3195 0.2879 -0.1407 0.0222  0.0085  400 SER A CB  
1845 O OG  . SER A 400 ? 0.3696 0.3397 0.3094 -0.1437 0.0198  0.0025  400 SER A OG  
1846 N N   . GLN A 401 ? 0.2639 0.2970 0.2343 -0.1374 0.0215  -0.0004 401 GLN A N   
1847 C CA  . GLN A 401 ? 0.2597 0.3120 0.2442 -0.1257 0.0194  -0.0043 401 GLN A CA  
1848 C C   . GLN A 401 ? 0.2714 0.3071 0.2528 -0.1124 0.0164  -0.0042 401 GLN A C   
1849 O O   . GLN A 401 ? 0.2959 0.3079 0.2667 -0.1118 0.0150  -0.0027 401 GLN A O   
1850 C CB  . GLN A 401 ? 0.2932 0.3578 0.2858 -0.1293 0.0171  -0.0089 401 GLN A CB  
1851 C CG  . GLN A 401 ? 0.3429 0.3844 0.3266 -0.1327 0.0143  -0.0107 401 GLN A CG  
1852 C CD  . GLN A 401 ? 0.4156 0.4713 0.4063 -0.1373 0.0119  -0.0157 401 GLN A CD  
1853 O OE1 . GLN A 401 ? 0.4479 0.4878 0.4328 -0.1370 0.0092  -0.0183 401 GLN A OE1 
1854 N NE2 . GLN A 401 ? 0.3990 0.4858 0.4017 -0.1410 0.0126  -0.0172 401 GLN A NE2 
1855 N N   . VAL A 402 ? 0.2436 0.2917 0.2335 -0.1020 0.0159  -0.0057 402 VAL A N   
1856 C CA  . VAL A 402 ? 0.2512 0.2886 0.2400 -0.0910 0.0133  -0.0061 402 VAL A CA  
1857 C C   . VAL A 402 ? 0.2541 0.3007 0.2526 -0.0855 0.0114  -0.0101 402 VAL A C   
1858 O O   . VAL A 402 ? 0.2664 0.3294 0.2731 -0.0816 0.0125  -0.0119 402 VAL A O   
1859 C CB  . VAL A 402 ? 0.2485 0.2912 0.2374 -0.0849 0.0145  -0.0049 402 VAL A CB  
1860 C CG1 . VAL A 402 ? 0.2572 0.2899 0.2442 -0.0758 0.0116  -0.0051 402 VAL A CG1 
1861 C CG2 . VAL A 402 ? 0.2578 0.2973 0.2377 -0.0909 0.0172  -0.0006 402 VAL A CG2 
1862 N N   . CYS A 403 ? 0.2497 0.2854 0.2460 -0.0847 0.0090  -0.0116 403 CYS A N   
1863 C CA  . CYS A 403 ? 0.2418 0.2860 0.2457 -0.0800 0.0073  -0.0148 403 CYS A CA  
1864 C C   . CYS A 403 ? 0.2266 0.2698 0.2338 -0.0697 0.0067  -0.0153 403 CYS A C   
1865 O O   . CYS A 403 ? 0.2353 0.2888 0.2492 -0.0651 0.0068  -0.0169 403 CYS A O   
1866 C CB  . CYS A 403 ? 0.2631 0.2967 0.2623 -0.0837 0.0053  -0.0167 403 CYS A CB  
1867 S SG  . CYS A 403 ? 0.3362 0.3447 0.3251 -0.0778 0.0039  -0.0157 403 CYS A SG  
1868 N N   A SER A 404 ? 0.2111 0.2421 0.2128 -0.0664 0.0060  -0.0135 404 SER A N   
1869 N N   B SER A 404 ? 0.2155 0.2465 0.2172 -0.0663 0.0060  -0.0135 404 SER A N   
1870 C CA  A SER A 404 ? 0.1991 0.2303 0.2037 -0.0587 0.0053  -0.0141 404 SER A CA  
1871 C CA  B SER A 404 ? 0.2063 0.2374 0.2110 -0.0586 0.0052  -0.0142 404 SER A CA  
1872 C C   A SER A 404 ? 0.1863 0.2127 0.1861 -0.0567 0.0050  -0.0119 404 SER A C   
1873 C C   B SER A 404 ? 0.1942 0.2196 0.1940 -0.0562 0.0047  -0.0120 404 SER A C   
1874 O O   A SER A 404 ? 0.1863 0.2041 0.1784 -0.0594 0.0050  -0.0091 404 SER A O   
1875 O O   B SER A 404 ? 0.1993 0.2141 0.1912 -0.0577 0.0042  -0.0094 404 SER A O   
1876 C CB  A SER A 404 ? 0.2236 0.2477 0.2275 -0.0548 0.0036  -0.0152 404 SER A CB  
1877 C CB  B SER A 404 ? 0.2309 0.2561 0.2356 -0.0551 0.0036  -0.0155 404 SER A CB  
1878 O OG  A SER A 404 ? 0.2442 0.2740 0.2522 -0.0550 0.0034  -0.0174 404 SER A OG  
1879 O OG  B SER A 404 ? 0.2562 0.2836 0.2643 -0.0491 0.0033  -0.0160 404 SER A OG  
1880 N N   . ILE A 405 ? 0.1788 0.2102 0.1822 -0.0523 0.0047  -0.0130 405 ILE A N   
1881 C CA  . ILE A 405 ? 0.1894 0.2197 0.1892 -0.0497 0.0035  -0.0116 405 ILE A CA  
1882 C C   . ILE A 405 ? 0.1845 0.2183 0.1890 -0.0453 0.0022  -0.0134 405 ILE A C   
1883 O O   . ILE A 405 ? 0.1791 0.2173 0.1891 -0.0453 0.0034  -0.0159 405 ILE A O   
1884 C CB  . ILE A 405 ? 0.1988 0.2361 0.1979 -0.0516 0.0049  -0.0121 405 ILE A CB  
1885 C CG1 . ILE A 405 ? 0.2135 0.2498 0.2078 -0.0565 0.0067  -0.0097 405 ILE A CG1 
1886 C CG2 . ILE A 405 ? 0.1987 0.2379 0.1947 -0.0490 0.0029  -0.0116 405 ILE A CG2 
1887 C CD1 . ILE A 405 ? 0.2323 0.2776 0.2269 -0.0579 0.0092  -0.0111 405 ILE A CD1 
1888 N N   . LEU A 406 ? 0.1806 0.2133 0.1825 -0.0414 0.0001  -0.0118 406 LEU A N   
1889 C CA  . LEU A 406 ? 0.1752 0.2155 0.1821 -0.0383 -0.0010 -0.0134 406 LEU A CA  
1890 C C   . LEU A 406 ? 0.1749 0.2216 0.1791 -0.0365 -0.0032 -0.0122 406 LEU A C   
1891 O O   . LEU A 406 ? 0.1925 0.2341 0.1894 -0.0348 -0.0043 -0.0090 406 LEU A O   
1892 C CB  . LEU A 406 ? 0.1896 0.2266 0.1969 -0.0333 -0.0016 -0.0127 406 LEU A CB  
1893 C CG  . LEU A 406 ? 0.2127 0.2446 0.2217 -0.0345 0.0000  -0.0141 406 LEU A CG  
1894 C CD1 . LEU A 406 ? 0.2326 0.2585 0.2384 -0.0290 -0.0007 -0.0136 406 LEU A CD1 
1895 C CD2 . LEU A 406 ? 0.2172 0.2562 0.2330 -0.0364 0.0016  -0.0165 406 LEU A CD2 
1896 N N   . TRP A 407 ? 0.1557 0.2134 0.1648 -0.0374 -0.0040 -0.0147 407 TRP A N   
1897 C CA  . TRP A 407 ? 0.1744 0.2423 0.1818 -0.0359 -0.0069 -0.0142 407 TRP A CA  
1898 C C   . TRP A 407 ? 0.1847 0.2626 0.1965 -0.0304 -0.0088 -0.0135 407 TRP A C   
1899 O O   . TRP A 407 ? 0.1819 0.2636 0.2003 -0.0318 -0.0073 -0.0156 407 TRP A O   
1900 C CB  . TRP A 407 ? 0.1760 0.2522 0.1859 -0.0424 -0.0066 -0.0186 407 TRP A CB  
1901 C CG  . TRP A 407 ? 0.1937 0.2629 0.1991 -0.0465 -0.0044 -0.0202 407 TRP A CG  
1902 C CD1 . TRP A 407 ? 0.2005 0.2617 0.2072 -0.0485 -0.0009 -0.0216 407 TRP A CD1 
1903 C CD2 . TRP A 407 ? 0.1940 0.2658 0.1928 -0.0482 -0.0053 -0.0206 407 TRP A CD2 
1904 N NE1 . TRP A 407 ? 0.1981 0.2574 0.1999 -0.0509 0.0007  -0.0232 407 TRP A NE1 
1905 C CE2 . TRP A 407 ? 0.2018 0.2669 0.1985 -0.0512 -0.0017 -0.0227 407 TRP A CE2 
1906 C CE3 . TRP A 407 ? 0.2094 0.2901 0.2035 -0.0468 -0.0088 -0.0195 407 TRP A CE3 
1907 C CZ2 . TRP A 407 ? 0.2137 0.2799 0.2034 -0.0531 -0.0011 -0.0240 407 TRP A CZ2 
1908 C CZ3 . TRP A 407 ? 0.2281 0.3094 0.2149 -0.0493 -0.0085 -0.0206 407 TRP A CZ3 
1909 C CH2 . TRP A 407 ? 0.2318 0.3054 0.2163 -0.0524 -0.0044 -0.0228 407 TRP A CH2 
1910 N N   . SER A 408 ? 0.2071 0.2916 0.2152 -0.0239 -0.0120 -0.0104 408 SER A N   
1911 C CA  . SER A 408 ? 0.2315 0.3310 0.2449 -0.0178 -0.0139 -0.0101 408 SER A CA  
1912 C C   . SER A 408 ? 0.2783 0.3976 0.2968 -0.0237 -0.0160 -0.0134 408 SER A C   
1913 O O   . SER A 408 ? 0.2914 0.4158 0.3050 -0.0236 -0.0188 -0.0125 408 SER A O   
1914 C CB  . SER A 408 ? 0.2286 0.3273 0.2347 -0.0063 -0.0166 -0.0050 408 SER A CB  
1915 O OG  . SER A 408 ? 0.2234 0.3436 0.2361 0.0000  -0.0188 -0.0051 408 SER A OG  
1916 N N   . PRO A 409 ? 0.3140 0.4458 0.3416 -0.0286 -0.0150 -0.0168 409 PRO A N   
1917 C CA  . PRO A 409 ? 0.3254 0.4770 0.3574 -0.0359 -0.0172 -0.0206 409 PRO A CA  
1918 C C   . PRO A 409 ? 0.3215 0.4972 0.3558 -0.0288 -0.0218 -0.0186 409 PRO A C   
1919 O O   . PRO A 409 ? 0.3481 0.5408 0.3831 -0.0338 -0.0252 -0.0211 409 PRO A O   
1920 C CB  . PRO A 409 ? 0.3367 0.4914 0.3764 -0.0439 -0.0137 -0.0241 409 PRO A CB  
1921 C CG  . PRO A 409 ? 0.3394 0.4869 0.3811 -0.0365 -0.0113 -0.0212 409 PRO A CG  
1922 C CD  . PRO A 409 ? 0.3163 0.4448 0.3495 -0.0286 -0.0116 -0.0175 409 PRO A CD  
1923 N N   A HIS A 410 ? 0.2991 0.4767 0.3338 -0.0165 -0.0222 -0.0143 410 HIS A N   
1924 N N   B HIS A 410 ? 0.3003 0.4779 0.3350 -0.0165 -0.0223 -0.0143 410 HIS A N   
1925 C CA  A HIS A 410 ? 0.2844 0.4857 0.3211 -0.0066 -0.0265 -0.0118 410 HIS A CA  
1926 C CA  B HIS A 410 ? 0.2853 0.4867 0.3221 -0.0067 -0.0265 -0.0118 410 HIS A CA  
1927 C C   A HIS A 410 ? 0.2856 0.4813 0.3109 0.0019  -0.0302 -0.0072 410 HIS A C   
1928 C C   B HIS A 410 ? 0.2857 0.4815 0.3110 0.0020  -0.0302 -0.0071 410 HIS A C   
1929 O O   A HIS A 410 ? 0.2823 0.5003 0.3080 0.0041  -0.0348 -0.0068 410 HIS A O   
1930 O O   B HIS A 410 ? 0.2820 0.5001 0.3077 0.0044  -0.0348 -0.0067 410 HIS A O   
1931 C CB  A HIS A 410 ? 0.2895 0.4946 0.3301 0.0048  -0.0247 -0.0093 410 HIS A CB  
1932 C CB  B HIS A 410 ? 0.2898 0.4960 0.3309 0.0044  -0.0248 -0.0095 410 HIS A CB  
1933 C CG  A HIS A 410 ? 0.3109 0.5214 0.3614 -0.0030 -0.0207 -0.0130 410 HIS A CG  
1934 C CG  B HIS A 410 ? 0.3086 0.5216 0.3600 -0.0041 -0.0208 -0.0134 410 HIS A CG  
1935 N ND1 A HIS A 410 ? 0.3203 0.5573 0.3816 -0.0128 -0.0210 -0.0168 410 HIS A ND1 
1936 N ND1 B HIS A 410 ? 0.3433 0.5341 0.3928 -0.0049 -0.0163 -0.0135 410 HIS A ND1 
1937 C CD2 A HIS A 410 ? 0.3356 0.5281 0.3856 -0.0030 -0.0162 -0.0132 410 HIS A CD2 
1938 C CD2 B HIS A 410 ? 0.3101 0.5490 0.3724 -0.0130 -0.0208 -0.0170 410 HIS A CD2 
1939 C CE1 A HIS A 410 ? 0.3296 0.5625 0.3959 -0.0179 -0.0163 -0.0185 410 HIS A CE1 
1940 C CE1 B HIS A 410 ? 0.3444 0.5475 0.4031 -0.0129 -0.0135 -0.0165 410 HIS A CE1 
1941 N NE2 A HIS A 410 ? 0.3435 0.5506 0.4034 -0.0116 -0.0135 -0.0164 410 HIS A NE2 
1942 N NE2 B HIS A 410 ? 0.3275 0.5588 0.3940 -0.0186 -0.0157 -0.0187 410 HIS A NE2 
1943 N N   . TYR A 411 ? 0.2880 0.4550 0.3025 0.0060  -0.0281 -0.0035 411 TYR A N   
1944 C CA  . TYR A 411 ? 0.2913 0.4492 0.2927 0.0139  -0.0307 0.0019  411 TYR A CA  
1945 C C   . TYR A 411 ? 0.3190 0.4691 0.3132 0.0049  -0.0311 0.0011  411 TYR A C   
1946 O O   . TYR A 411 ? 0.3344 0.4787 0.3170 0.0112  -0.0332 0.0062  411 TYR A O   
1947 C CB  . TYR A 411 ? 0.2963 0.4264 0.2873 0.0233  -0.0281 0.0070  411 TYR A CB  
1948 C CG  . TYR A 411 ? 0.2952 0.4324 0.2865 0.0386  -0.0290 0.0100  411 TYR A CG  
1949 C CD1 . TYR A 411 ? 0.3126 0.4584 0.2964 0.0526  -0.0328 0.0155  411 TYR A CD1 
1950 C CD2 . TYR A 411 ? 0.3020 0.4384 0.3005 0.0401  -0.0259 0.0074  411 TYR A CD2 
1951 C CE1 . TYR A 411 ? 0.3218 0.4748 0.3053 0.0688  -0.0334 0.0182  411 TYR A CE1 
1952 C CE2 . TYR A 411 ? 0.3201 0.4644 0.3186 0.0553  -0.0263 0.0097  411 TYR A CE2 
1953 C CZ  . TYR A 411 ? 0.3358 0.4876 0.3266 0.0701  -0.0298 0.0151  411 TYR A CZ  
1954 O OH  . TYR A 411 ? 0.3759 0.5356 0.3660 0.0872  -0.0298 0.0174  411 TYR A OH  
1955 N N   . LYS A 412 ? 0.3115 0.4587 0.3105 -0.0084 -0.0286 -0.0046 412 LYS A N   
1956 C CA  . LYS A 412 ? 0.3071 0.4467 0.2984 -0.0157 -0.0283 -0.0058 412 LYS A CA  
1957 C C   . LYS A 412 ? 0.2749 0.3888 0.2552 -0.0122 -0.0255 -0.0004 412 LYS A C   
1958 O O   . LYS A 412 ? 0.2769 0.3863 0.2461 -0.0095 -0.0268 0.0037  412 LYS A O   
1959 C CB  . LYS A 412 ? 0.3553 0.5148 0.3423 -0.0144 -0.0335 -0.0056 412 LYS A CB  
1960 C CG  . LYS A 412 ? 0.4397 0.6075 0.4280 -0.0269 -0.0338 -0.0127 412 LYS A CG  
1961 C CD  . LYS A 412 ? 0.4932 0.6901 0.4894 -0.0306 -0.0382 -0.0172 412 LYS A CD  
1962 C CE  . LYS A 412 ? 0.5427 0.7436 0.5370 -0.0440 -0.0383 -0.0251 412 LYS A CE  
1963 N NZ  . LYS A 412 ? 0.5629 0.7892 0.5665 -0.0519 -0.0413 -0.0310 412 LYS A NZ  
1964 N N   . GLU A 413 ? 0.2423 0.3407 0.2251 -0.0122 -0.0219 -0.0002 413 GLU A N   
1965 C CA  . GLU A 413 ? 0.2352 0.3098 0.2086 -0.0112 -0.0190 0.0041  413 GLU A CA  
1966 C C   . GLU A 413 ? 0.2427 0.3075 0.2218 -0.0194 -0.0148 0.0002  413 GLU A C   
1967 O O   . GLU A 413 ? 0.2375 0.3105 0.2267 -0.0230 -0.0141 -0.0045 413 GLU A O   
1968 C CB  . GLU A 413 ? 0.2524 0.3161 0.2200 0.0002  -0.0195 0.0091  413 GLU A CB  
1969 C CG  . GLU A 413 ? 0.2699 0.3402 0.2289 0.0114  -0.0234 0.0146  413 GLU A CG  
1970 C CD  . GLU A 413 ? 0.2996 0.3604 0.2524 0.0253  -0.0239 0.0192  413 GLU A CD  
1971 O OE1 . GLU A 413 ? 0.3108 0.3595 0.2660 0.0258  -0.0211 0.0175  413 GLU A OE1 
1972 O OE2 . GLU A 413 ? 0.3344 0.3997 0.2789 0.0366  -0.0271 0.0244  413 GLU A OE2 
1973 N N   . LEU A 414 ? 0.2381 0.2859 0.2104 -0.0224 -0.0120 0.0025  414 LEU A N   
1974 C CA  . LEU A 414 ? 0.2511 0.2912 0.2283 -0.0289 -0.0085 -0.0004 414 LEU A CA  
1975 C C   . LEU A 414 ? 0.2378 0.2598 0.2085 -0.0265 -0.0072 0.0030  414 LEU A C   
1976 O O   . LEU A 414 ? 0.2486 0.2600 0.2083 -0.0222 -0.0079 0.0080  414 LEU A O   
1977 C CB  . LEU A 414 ? 0.2923 0.3314 0.2672 -0.0362 -0.0059 -0.0013 414 LEU A CB  
1978 C CG  . LEU A 414 ? 0.3484 0.4006 0.3259 -0.0390 -0.0066 -0.0051 414 LEU A CG  
1979 C CD1 . LEU A 414 ? 0.3785 0.4327 0.3461 -0.0381 -0.0079 -0.0019 414 LEU A CD1 
1980 C CD2 . LEU A 414 ? 0.3670 0.4196 0.3497 -0.0449 -0.0031 -0.0095 414 LEU A CD2 
1981 N N   . ILE A 415 ? 0.2172 0.2344 0.1932 -0.0294 -0.0053 0.0002  415 ILE A N   
1982 C CA  . ILE A 415 ? 0.2173 0.2167 0.1864 -0.0296 -0.0039 0.0020  415 ILE A CA  
1983 C C   . ILE A 415 ? 0.2159 0.2146 0.1891 -0.0388 -0.0013 -0.0006 415 ILE A C   
1984 O O   . ILE A 415 ? 0.2107 0.2211 0.1939 -0.0410 -0.0007 -0.0045 415 ILE A O   
1985 C CB  . ILE A 415 ? 0.2296 0.2247 0.1991 -0.0219 -0.0048 0.0013  415 ILE A CB  
1986 C CG1 . ILE A 415 ? 0.2544 0.2267 0.2128 -0.0222 -0.0035 0.0028  415 ILE A CG1 
1987 C CG2 . ILE A 415 ? 0.2308 0.2385 0.2129 -0.0233 -0.0044 -0.0035 415 ILE A CG2 
1988 C CD1 . ILE A 415 ? 0.2697 0.2350 0.2250 -0.0122 -0.0041 0.0022  415 ILE A CD1 
1989 N N   . SER A 416 ? 0.2193 0.2051 0.1842 -0.0442 0.0004  0.0016  416 SER A N   
1990 C CA  . SER A 416 ? 0.2061 0.1948 0.1751 -0.0532 0.0027  -0.0006 416 SER A CA  
1991 C C   . SER A 416 ? 0.2319 0.2051 0.1945 -0.0572 0.0033  -0.0008 416 SER A C   
1992 O O   . SER A 416 ? 0.2558 0.2109 0.2067 -0.0544 0.0030  0.0021  416 SER A O   
1993 C CB  . SER A 416 ? 0.2171 0.2105 0.1834 -0.0594 0.0048  0.0015  416 SER A CB  
1994 O OG  . SER A 416 ? 0.2487 0.2273 0.2015 -0.0601 0.0052  0.0068  416 SER A OG  
1995 N N   . GLY A 417 ? 0.2211 0.2008 0.1902 -0.0631 0.0041  -0.0043 417 GLY A N   
1996 C CA  . GLY A 417 ? 0.2409 0.2078 0.2039 -0.0690 0.0044  -0.0057 417 GLY A CA  
1997 C C   . GLY A 417 ? 0.2493 0.2202 0.2115 -0.0813 0.0066  -0.0054 417 GLY A C   
1998 O O   . GLY A 417 ? 0.2461 0.2356 0.2171 -0.0837 0.0078  -0.0056 417 GLY A O   
1999 N N   . HIS A 418 ? 0.2538 0.2072 0.2048 -0.0893 0.0074  -0.0049 418 HIS A N   
2000 C CA  . HIS A 418 ? 0.2792 0.2351 0.2274 -0.1031 0.0099  -0.0038 418 HIS A CA  
2001 C C   . HIS A 418 ? 0.2983 0.2465 0.2418 -0.1145 0.0100  -0.0072 418 HIS A C   
2002 O O   . HIS A 418 ? 0.3051 0.2417 0.2449 -0.1112 0.0080  -0.0106 418 HIS A O   
2003 C CB  . HIS A 418 ? 0.2910 0.2303 0.2257 -0.1048 0.0121  0.0024  418 HIS A CB  
2004 C CG  . HIS A 418 ? 0.3070 0.2561 0.2457 -0.0946 0.0117  0.0053  418 HIS A CG  
2005 N ND1 . HIS A 418 ? 0.3176 0.2904 0.2670 -0.0960 0.0130  0.0049  418 HIS A ND1 
2006 C CD2 . HIS A 418 ? 0.3322 0.2727 0.2664 -0.0826 0.0097  0.0076  418 HIS A CD2 
2007 C CE1 . HIS A 418 ? 0.3248 0.3003 0.2745 -0.0863 0.0118  0.0066  418 HIS A CE1 
2008 N NE2 . HIS A 418 ? 0.3322 0.2904 0.2735 -0.0783 0.0096  0.0085  418 HIS A NE2 
2009 N N   . GLY A 419 ? 0.3023 0.2597 0.2465 -0.1284 0.0123  -0.0068 419 GLY A N   
2010 C CA  . GLY A 419 ? 0.3239 0.2789 0.2646 -0.1429 0.0124  -0.0105 419 GLY A CA  
2011 C C   . GLY A 419 ? 0.3628 0.2953 0.2870 -0.1563 0.0157  -0.0069 419 GLY A C   
2012 O O   . GLY A 419 ? 0.3771 0.2812 0.2862 -0.1514 0.0167  -0.0026 419 GLY A O   
2013 N N   . PHE A 420 ? 0.3667 0.3126 0.2933 -0.1734 0.0176  -0.0083 420 PHE A N   
2014 C CA  . PHE A 420 ? 0.4072 0.3329 0.3179 -0.1901 0.0215  -0.0050 420 PHE A CA  
2015 C C   . PHE A 420 ? 0.4107 0.3258 0.3133 -0.1853 0.0249  0.0031  420 PHE A C   
2016 O O   . PHE A 420 ? 0.3920 0.3315 0.3073 -0.1771 0.0252  0.0050  420 PHE A O   
2017 C CB  . PHE A 420 ? 0.4142 0.3688 0.3348 -0.2087 0.0230  -0.0079 420 PHE A CB  
2018 C CG  . PHE A 420 ? 0.4639 0.3992 0.3683 -0.2300 0.0272  -0.0057 420 PHE A CG  
2019 C CD1 . PHE A 420 ? 0.4980 0.4079 0.3882 -0.2430 0.0265  -0.0101 420 PHE A CD1 
2020 C CD2 . PHE A 420 ? 0.4856 0.4261 0.3874 -0.2375 0.0323  0.0008  420 PHE A CD2 
2021 C CE1 . PHE A 420 ? 0.5284 0.4174 0.4018 -0.2644 0.0308  -0.0080 420 PHE A CE1 
2022 C CE2 . PHE A 420 ? 0.5131 0.4347 0.3989 -0.2587 0.0368  0.0034  420 PHE A CE2 
2023 C CZ  . PHE A 420 ? 0.5271 0.4222 0.3986 -0.2724 0.0361  -0.0009 420 PHE A CZ  
2024 N N   . ALA A 421 ? 0.4469 0.3241 0.3274 -0.1877 0.0271  0.0079  421 ALA A N   
2025 C CA  . ALA A 421 ? 0.4833 0.3259 0.3452 -0.1979 0.0275  0.0056  421 ALA A CA  
2026 C C   . ALA A 421 ? 0.4991 0.3090 0.3479 -0.1819 0.0250  0.0051  421 ALA A C   
2027 O O   . ALA A 421 ? 0.5273 0.3102 0.3620 -0.1880 0.0248  0.0011  421 ALA A O   
2028 C CB  . ALA A 421 ? 0.5084 0.3282 0.3515 -0.2148 0.0330  0.0115  421 ALA A CB  
2029 N N   . GLN A 422 ? 0.4791 0.2916 0.3317 -0.1621 0.0232  0.0087  422 GLN A N   
2030 C CA  . GLN A 422 ? 0.4774 0.2621 0.3178 -0.1456 0.0213  0.0091  422 GLN A CA  
2031 C C   . GLN A 422 ? 0.4466 0.2456 0.3003 -0.1336 0.0171  0.0024  422 GLN A C   
2032 O O   . GLN A 422 ? 0.4625 0.2382 0.3051 -0.1220 0.0161  0.0016  422 GLN A O   
2033 C CB  . GLN A 422 ? 0.5056 0.2840 0.3402 -0.1307 0.0217  0.0172  422 GLN A CB  
2034 N N   . ASN A 423 ? 0.3994 0.2359 0.2757 -0.1348 0.0151  -0.0018 423 ASN A N   
2035 C CA  . ASN A 423 ? 0.3757 0.2272 0.2646 -0.1240 0.0115  -0.0076 423 ASN A CA  
2036 C C   . ASN A 423 ? 0.3792 0.2229 0.2662 -0.1042 0.0101  -0.0049 423 ASN A C   
2037 O O   . ASN A 423 ? 0.3843 0.2180 0.2680 -0.0952 0.0085  -0.0084 423 ASN A O   
2038 C CB  . ASN A 423 ? 0.3835 0.2209 0.2646 -0.1316 0.0105  -0.0143 423 ASN A CB  
2039 C CG  . ASN A 423 ? 0.4063 0.2543 0.2895 -0.1523 0.0115  -0.0173 423 ASN A CG  
2040 O OD1 . ASN A 423 ? 0.3837 0.2650 0.2839 -0.1571 0.0113  -0.0173 423 ASN A OD1 
2041 N ND2 . ASN A 423 ? 0.4539 0.2746 0.3194 -0.1653 0.0128  -0.0200 423 ASN A ND2 
2042 N N   . GLN A 424 ? 0.3670 0.2163 0.2556 -0.0978 0.0107  0.0010  424 GLN A N   
2043 C CA  . GLN A 424 ? 0.3668 0.2108 0.2529 -0.0802 0.0092  0.0042  424 GLN A CA  
2044 C C   . GLN A 424 ? 0.3445 0.2193 0.2493 -0.0712 0.0071  0.0037  424 GLN A C   
2045 O O   . GLN A 424 ? 0.3404 0.2392 0.2590 -0.0777 0.0073  0.0021  424 GLN A O   
2046 C CB  . GLN A 424 ? 0.3885 0.2095 0.2567 -0.0782 0.0111  0.0119  424 GLN A CB  
2047 C CG  . GLN A 424 ? 0.4161 0.2562 0.2907 -0.0790 0.0117  0.0170  424 GLN A CG  
2048 C CD  . GLN A 424 ? 0.4548 0.3047 0.3324 -0.0963 0.0146  0.0174  424 GLN A CD  
2049 O OE1 . GLN A 424 ? 0.4570 0.3175 0.3429 -0.1074 0.0151  0.0122  424 GLN A OE1 
2050 N NE2 . GLN A 424 ? 0.4673 0.3159 0.3379 -0.0986 0.0168  0.0238  424 GLN A NE2 
2051 N N   . LEU A 425 ? 0.3224 0.1964 0.2268 -0.0561 0.0053  0.0052  425 LEU A N   
2052 C CA  . LEU A 425 ? 0.3030 0.2030 0.2220 -0.0486 0.0034  0.0055  425 LEU A CA  
2053 C C   . LEU A 425 ? 0.3108 0.2063 0.2213 -0.0439 0.0034  0.0121  425 LEU A C   
2054 O O   . LEU A 425 ? 0.3260 0.1977 0.2198 -0.0386 0.0039  0.0164  425 LEU A O   
2055 C CB  . LEU A 425 ? 0.3056 0.2131 0.2312 -0.0362 0.0014  0.0028  425 LEU A CB  
2056 C CG  . LEU A 425 ? 0.3520 0.2603 0.2824 -0.0375 0.0013  -0.0030 425 LEU A CG  
2057 C CD1 . LEU A 425 ? 0.3345 0.2598 0.2758 -0.0266 -0.0001 -0.0050 425 LEU A CD1 
2058 C CD2 . LEU A 425 ? 0.3828 0.3051 0.3233 -0.0496 0.0019  -0.0064 425 LEU A CD2 
2059 N N   . VAL A 426 ? 0.2827 0.1994 0.2027 -0.0452 0.0029  0.0129  426 VAL A N   
2060 C CA  . VAL A 426 ? 0.2809 0.1967 0.1929 -0.0403 0.0024  0.0188  426 VAL A CA  
2061 C C   . VAL A 426 ? 0.2807 0.2191 0.2038 -0.0308 -0.0008 0.0174  426 VAL A C   
2062 O O   . VAL A 426 ? 0.2609 0.2187 0.1985 -0.0341 -0.0011 0.0127  426 VAL A O   
2063 C CB  . VAL A 426 ? 0.2966 0.2160 0.2061 -0.0514 0.0050  0.0213  426 VAL A CB  
2064 C CG1 . VAL A 426 ? 0.3022 0.2218 0.2026 -0.0453 0.0042  0.0274  426 VAL A CG1 
2065 C CG2 . VAL A 426 ? 0.3071 0.2053 0.2052 -0.0630 0.0085  0.0228  426 VAL A CG2 
2066 N N   . ILE A 427 ? 0.2879 0.2237 0.2037 -0.0192 -0.0031 0.0216  427 ILE A N   
2067 C CA  . ILE A 427 ? 0.2834 0.2429 0.2090 -0.0117 -0.0064 0.0204  427 ILE A CA  
2068 C C   . ILE A 427 ? 0.2808 0.2469 0.2007 -0.0132 -0.0071 0.0243  427 ILE A C   
2069 O O   . ILE A 427 ? 0.2964 0.2458 0.2005 -0.0107 -0.0065 0.0307  427 ILE A O   
2070 C CB  . ILE A 427 ? 0.3026 0.2618 0.2259 0.0028  -0.0090 0.0217  427 ILE A CB  
2071 C CG1 . ILE A 427 ? 0.3167 0.2700 0.2452 0.0035  -0.0077 0.0171  427 ILE A CG1 
2072 C CG2 . ILE A 427 ? 0.3002 0.2877 0.2341 0.0084  -0.0126 0.0204  427 ILE A CG2 
2073 C CD1 . ILE A 427 ? 0.3511 0.3040 0.2772 0.0186  -0.0092 0.0180  427 ILE A CD1 
2074 N N   . TRP A 428 ? 0.2610 0.2495 0.1921 -0.0170 -0.0082 0.0204  428 TRP A N   
2075 C CA  . TRP A 428 ? 0.2696 0.2671 0.1960 -0.0191 -0.0088 0.0225  428 TRP A CA  
2076 C C   . TRP A 428 ? 0.2744 0.2940 0.2069 -0.0128 -0.0133 0.0205  428 TRP A C   
2077 O O   . TRP A 428 ? 0.2647 0.2980 0.2102 -0.0132 -0.0144 0.0150  428 TRP A O   
2078 C CB  . TRP A 428 ? 0.2630 0.2677 0.1962 -0.0307 -0.0057 0.0182  428 TRP A CB  
2079 C CG  . TRP A 428 ? 0.2710 0.2627 0.2037 -0.0388 -0.0016 0.0180  428 TRP A CG  
2080 C CD1 . TRP A 428 ? 0.2760 0.2674 0.2184 -0.0420 -0.0005 0.0135  428 TRP A CD1 
2081 C CD2 . TRP A 428 ? 0.2826 0.2639 0.2055 -0.0464 0.0021  0.0220  428 TRP A CD2 
2082 N NE1 . TRP A 428 ? 0.2842 0.2662 0.2235 -0.0507 0.0030  0.0143  428 TRP A NE1 
2083 C CE2 . TRP A 428 ? 0.2891 0.2654 0.2171 -0.0543 0.0049  0.0194  428 TRP A CE2 
2084 C CE3 . TRP A 428 ? 0.2986 0.2755 0.2084 -0.0476 0.0033  0.0278  428 TRP A CE3 
2085 C CZ2 . TRP A 428 ? 0.3118 0.2801 0.2331 -0.0643 0.0089  0.0220  428 TRP A CZ2 
2086 C CZ3 . TRP A 428 ? 0.3176 0.2840 0.2198 -0.0573 0.0078  0.0310  428 TRP A CZ3 
2087 C CH2 . TRP A 428 ? 0.3182 0.2817 0.2270 -0.0661 0.0106  0.0279  428 TRP A CH2 
2088 N N   . LYS A 429 ? 0.2859 0.3101 0.2086 -0.0079 -0.0158 0.0250  429 LYS A N   
2089 C CA  . LYS A 429 ? 0.2933 0.3418 0.2216 -0.0034 -0.0206 0.0226  429 LYS A CA  
2090 C C   . LYS A 429 ? 0.3038 0.3655 0.2379 -0.0138 -0.0197 0.0165  429 LYS A C   
2091 O O   . LYS A 429 ? 0.3178 0.3718 0.2447 -0.0196 -0.0167 0.0178  429 LYS A O   
2092 C CB  . LYS A 429 ? 0.3443 0.3942 0.2587 0.0069  -0.0241 0.0299  429 LYS A CB  
2093 C CG  . LYS A 429 ? 0.4181 0.4973 0.3389 0.0119  -0.0300 0.0273  429 LYS A CG  
2094 C CD  . LYS A 429 ? 0.4885 0.5794 0.4218 0.0182  -0.0319 0.0245  429 LYS A CD  
2095 C CE  . LYS A 429 ? 0.5349 0.6588 0.4778 0.0193  -0.0372 0.0204  429 LYS A CE  
2096 N NZ  . LYS A 429 ? 0.5621 0.6972 0.5165 0.0049  -0.0361 0.0113  429 LYS A NZ  
2097 N N   . TYR A 430 ? 0.2936 0.3740 0.2396 -0.0164 -0.0219 0.0097  430 TYR A N   
2098 C CA  . TYR A 430 ? 0.2920 0.3819 0.2413 -0.0256 -0.0210 0.0032  430 TYR A CA  
2099 C C   . TYR A 430 ? 0.2861 0.3966 0.2327 -0.0241 -0.0262 0.0015  430 TYR A C   
2100 O O   . TYR A 430 ? 0.2758 0.3998 0.2264 -0.0180 -0.0304 0.0024  430 TYR A O   
2101 C CB  . TYR A 430 ? 0.2887 0.3808 0.2513 -0.0314 -0.0189 -0.0037 430 TYR A CB  
2102 C CG  . TYR A 430 ? 0.3122 0.4058 0.2757 -0.0401 -0.0163 -0.0101 430 TYR A CG  
2103 C CD1 . TYR A 430 ? 0.3345 0.4161 0.2949 -0.0437 -0.0115 -0.0098 430 TYR A CD1 
2104 C CD2 . TYR A 430 ? 0.3290 0.4362 0.2952 -0.0447 -0.0185 -0.0165 430 TYR A CD2 
2105 C CE1 . TYR A 430 ? 0.3561 0.4388 0.3163 -0.0493 -0.0087 -0.0157 430 TYR A CE1 
2106 C CE2 . TYR A 430 ? 0.3469 0.4516 0.3112 -0.0517 -0.0156 -0.0228 430 TYR A CE2 
2107 C CZ  . TYR A 430 ? 0.3723 0.4645 0.3336 -0.0529 -0.0106 -0.0222 430 TYR A CZ  
2108 O OH  . TYR A 430 ? 0.4125 0.5019 0.3709 -0.0575 -0.0073 -0.0283 430 TYR A OH  
2109 N N   . PRO A 431 ? 0.2911 0.4060 0.2301 -0.0290 -0.0261 -0.0007 431 PRO A N   
2110 C CA  . PRO A 431 ? 0.3045 0.4084 0.2388 -0.0358 -0.0209 -0.0026 431 PRO A CA  
2111 C C   . PRO A 431 ? 0.3251 0.4172 0.2459 -0.0337 -0.0184 0.0049  431 PRO A C   
2112 O O   . PRO A 431 ? 0.3325 0.4194 0.2501 -0.0394 -0.0138 0.0032  431 PRO A O   
2113 C CB  . PRO A 431 ? 0.3105 0.4282 0.2433 -0.0417 -0.0226 -0.0104 431 PRO A CB  
2114 C CG  . PRO A 431 ? 0.3126 0.4475 0.2410 -0.0364 -0.0293 -0.0081 431 PRO A CG  
2115 C CD  . PRO A 431 ? 0.2857 0.4217 0.2218 -0.0287 -0.0316 -0.0034 431 PRO A CD  
2116 N N   . THR A 432 ? 0.3353 0.4228 0.2475 -0.0256 -0.0209 0.0132  432 THR A N   
2117 C CA  . THR A 432 ? 0.3579 0.4316 0.2549 -0.0245 -0.0181 0.0214  432 THR A CA  
2118 C C   . THR A 432 ? 0.3668 0.4209 0.2639 -0.0295 -0.0120 0.0239  432 THR A C   
2119 O O   . THR A 432 ? 0.3756 0.4201 0.2615 -0.0327 -0.0082 0.0290  432 THR A O   
2120 C CB  . THR A 432 ? 0.3964 0.4670 0.2821 -0.0132 -0.0222 0.0302  432 THR A CB  
2121 O OG1 . THR A 432 ? 0.4153 0.4760 0.3069 -0.0075 -0.0226 0.0321  432 THR A OG1 
2122 C CG2 . THR A 432 ? 0.4007 0.4948 0.2848 -0.0078 -0.0290 0.0286  432 THR A CG2 
2123 N N   . MET A 433 ? 0.3483 0.3977 0.2578 -0.0307 -0.0110 0.0206  433 MET A N   
2124 C CA  . MET A 433 ? 0.3635 0.3967 0.2746 -0.0356 -0.0062 0.0221  433 MET A CA  
2125 C C   . MET A 433 ? 0.3850 0.3977 0.2816 -0.0324 -0.0052 0.0314  433 MET A C   
2126 O O   . MET A 433 ? 0.4012 0.4004 0.2937 -0.0393 -0.0005 0.0339  433 MET A O   
2127 C CB  . MET A 433 ? 0.3718 0.4085 0.2866 -0.0451 -0.0010 0.0182  433 MET A CB  
2128 C CG  . MET A 433 ? 0.3891 0.4389 0.3178 -0.0474 -0.0011 0.0089  433 MET A CG  
2129 S SD  . MET A 433 ? 0.4421 0.4893 0.3850 -0.0454 -0.0027 0.0053  433 MET A SD  
2130 C CE  . MET A 433 ? 0.3918 0.4248 0.3349 -0.0504 0.0018  0.0084  433 MET A CE  
2131 N N   . ALA A 434 ? 0.3878 0.3981 0.2761 -0.0218 -0.0094 0.0365  434 ALA A N   
2132 C CA  . ALA A 434 ? 0.4068 0.3935 0.2786 -0.0166 -0.0084 0.0457  434 ALA A CA  
2133 C C   . ALA A 434 ? 0.4082 0.3792 0.2845 -0.0152 -0.0074 0.0445  434 ALA A C   
2134 O O   . ALA A 434 ? 0.3885 0.3711 0.2785 -0.0117 -0.0099 0.0389  434 ALA A O   
2135 C CB  . ALA A 434 ? 0.4087 0.3999 0.2701 -0.0033 -0.0135 0.0513  434 ALA A CB  
2136 N N   . LYS A 435 ? 0.4299 0.3743 0.2935 -0.0183 -0.0036 0.0498  435 LYS A N   
2137 C CA  . LYS A 435 ? 0.4532 0.3800 0.3183 -0.0176 -0.0025 0.0483  435 LYS A CA  
2138 C C   . LYS A 435 ? 0.4688 0.3879 0.3266 -0.0013 -0.0061 0.0519  435 LYS A C   
2139 O O   . LYS A 435 ? 0.4879 0.3916 0.3274 0.0065  -0.0065 0.0601  435 LYS A O   
2140 C CB  . LYS A 435 ? 0.4958 0.3955 0.3474 -0.0281 0.0028  0.0524  435 LYS A CB  
2141 C CG  . LYS A 435 ? 0.5377 0.4230 0.3931 -0.0338 0.0048  0.0481  435 LYS A CG  
2142 C CD  . LYS A 435 ? 0.6158 0.4824 0.4606 -0.0489 0.0103  0.0509  435 LYS A CD  
2143 C CE  . LYS A 435 ? 0.6731 0.5374 0.5269 -0.0599 0.0122  0.0445  435 LYS A CE  
2144 N NZ  . LYS A 435 ? 0.7168 0.5766 0.5663 -0.0772 0.0173  0.0459  435 LYS A NZ  
2145 N N   . VAL A 436 ? 0.4550 0.3852 0.3262 0.0046  -0.0086 0.0463  436 VAL A N   
2146 C CA  . VAL A 436 ? 0.4644 0.3933 0.3319 0.0212  -0.0119 0.0487  436 VAL A CA  
2147 C C   . VAL A 436 ? 0.4705 0.3675 0.3261 0.0253  -0.0092 0.0505  436 VAL A C   
2148 O O   . VAL A 436 ? 0.4863 0.3660 0.3260 0.0390  -0.0099 0.0567  436 VAL A O   
2149 C CB  . VAL A 436 ? 0.4702 0.4301 0.3587 0.0245  -0.0153 0.0415  436 VAL A CB  
2150 C CG1 . VAL A 436 ? 0.4910 0.4533 0.3781 0.0415  -0.0181 0.0431  436 VAL A CG1 
2151 C CG2 . VAL A 436 ? 0.4612 0.4497 0.3582 0.0211  -0.0183 0.0395  436 VAL A CG2 
2152 N N   . ALA A 437 ? 0.4427 0.3324 0.3054 0.0143  -0.0062 0.0447  437 ALA A N   
2153 C CA  . ALA A 437 ? 0.4435 0.3045 0.2958 0.0166  -0.0039 0.0443  437 ALA A CA  
2154 C C   . ALA A 437 ? 0.4242 0.2787 0.2825 -0.0005 -0.0005 0.0386  437 ALA A C   
2155 O O   . ALA A 437 ? 0.4087 0.2862 0.2834 -0.0106 -0.0006 0.0340  437 ALA A O   
2156 C CB  . ALA A 437 ? 0.4393 0.3112 0.2999 0.0310  -0.0064 0.0408  437 ALA A CB  
2157 N N   . GLU A 438 ? 0.4232 0.2470 0.2678 -0.0030 0.0022  0.0384  438 GLU A N   
2158 C CA  . GLU A 438 ? 0.4253 0.2437 0.2747 -0.0183 0.0047  0.0325  438 GLU A CA  
2159 C C   . GLU A 438 ? 0.4286 0.2325 0.2748 -0.0118 0.0047  0.0279  438 GLU A C   
2160 O O   . GLU A 438 ? 0.4534 0.2299 0.2812 -0.0011 0.0054  0.0311  438 GLU A O   
2161 C CB  . GLU A 438 ? 0.4723 0.2658 0.3055 -0.0326 0.0086  0.0364  438 GLU A CB  
2162 C CG  . GLU A 438 ? 0.5342 0.3468 0.3737 -0.0424 0.0096  0.0392  438 GLU A CG  
2163 C CD  . GLU A 438 ? 0.6563 0.4493 0.4829 -0.0594 0.0142  0.0420  438 GLU A CD  
2164 O OE1 . GLU A 438 ? 0.7120 0.4716 0.5155 -0.0582 0.0164  0.0483  438 GLU A OE1 
2165 O OE2 . GLU A 438 ? 0.6585 0.4694 0.4974 -0.0738 0.0157  0.0382  438 GLU A OE2 
2166 N N   . LEU A 439 ? 0.3970 0.2183 0.2595 -0.0171 0.0041  0.0204  439 LEU A N   
2167 C CA  . LEU A 439 ? 0.3962 0.2061 0.2560 -0.0120 0.0042  0.0152  439 LEU A CA  
2168 C C   . LEU A 439 ? 0.4146 0.2065 0.2676 -0.0282 0.0066  0.0110  439 LEU A C   
2169 O O   . LEU A 439 ? 0.4003 0.2117 0.2676 -0.0403 0.0064  0.0068  439 LEU A O   
2170 C CB  . LEU A 439 ? 0.3726 0.2139 0.2534 -0.0062 0.0020  0.0101  439 LEU A CB  
2171 C CG  . LEU A 439 ? 0.3666 0.2307 0.2562 0.0071  -0.0006 0.0133  439 LEU A CG  
2172 C CD1 . LEU A 439 ? 0.3414 0.2354 0.2513 0.0084  -0.0020 0.0081  439 LEU A CD1 
2173 C CD2 . LEU A 439 ? 0.3959 0.2433 0.2704 0.0246  -0.0009 0.0176  439 LEU A CD2 
2174 N N   . LYS A 440 ? 0.4411 0.1958 0.2717 -0.0280 0.0088  0.0120  440 LYS A N   
2175 C CA  . LYS A 440 ? 0.4639 0.1978 0.2845 -0.0450 0.0111  0.0079  440 LYS A CA  
2176 C C   . LYS A 440 ? 0.4839 0.2018 0.2974 -0.0409 0.0111  0.0009  440 LYS A C   
2177 O O   . LYS A 440 ? 0.4968 0.2067 0.3045 -0.0230 0.0107  0.0010  440 LYS A O   
2178 C CB  . LYS A 440 ? 0.5069 0.2057 0.3037 -0.0523 0.0143  0.0141  440 LYS A CB  
2179 C CG  . LYS A 440 ? 0.5554 0.2708 0.3585 -0.0605 0.0150  0.0203  440 LYS A CG  
2180 C CD  . LYS A 440 ? 0.6437 0.3233 0.4214 -0.0668 0.0188  0.0278  440 LYS A CD  
2181 C CE  . LYS A 440 ? 0.6955 0.3931 0.4787 -0.0732 0.0197  0.0343  440 LYS A CE  
2182 N NZ  . LYS A 440 ? 0.7508 0.4128 0.5076 -0.0774 0.0236  0.0430  440 LYS A NZ  
2183 N N   . GLY A 441 ? 0.4850 0.2006 0.2989 -0.0572 0.0116  -0.0055 441 GLY A N   
2184 C CA  . GLY A 441 ? 0.4965 0.1987 0.3034 -0.0553 0.0115  -0.0132 441 GLY A CA  
2185 C C   . GLY A 441 ? 0.4824 0.2029 0.3008 -0.0719 0.0102  -0.0206 441 GLY A C   
2186 O O   . GLY A 441 ? 0.5010 0.2009 0.3063 -0.0800 0.0108  -0.0269 441 GLY A O   
2187 N N   . HIS A 442 ? 0.4501 0.2092 0.2920 -0.0767 0.0083  -0.0201 442 HIS A N   
2188 C CA  . HIS A 442 ? 0.4359 0.2160 0.2894 -0.0910 0.0068  -0.0263 442 HIS A CA  
2189 C C   . HIS A 442 ? 0.4573 0.2209 0.2988 -0.1120 0.0085  -0.0275 442 HIS A C   
2190 O O   . HIS A 442 ? 0.4658 0.2170 0.2994 -0.1173 0.0108  -0.0216 442 HIS A O   
2191 C CB  . HIS A 442 ? 0.4009 0.2223 0.2795 -0.0907 0.0051  -0.0245 442 HIS A CB  
2192 C CG  . HIS A 442 ? 0.3776 0.2190 0.2696 -0.0760 0.0033  -0.0259 442 HIS A CG  
2193 N ND1 . HIS A 442 ? 0.3882 0.2327 0.2810 -0.0739 0.0021  -0.0322 442 HIS A ND1 
2194 C CD2 . HIS A 442 ? 0.3648 0.2238 0.2687 -0.0643 0.0029  -0.0219 442 HIS A CD2 
2195 C CE1 . HIS A 442 ? 0.3815 0.2458 0.2873 -0.0615 0.0013  -0.0312 442 HIS A CE1 
2196 N NE2 . HIS A 442 ? 0.3703 0.2435 0.2831 -0.0558 0.0017  -0.0254 442 HIS A NE2 
2197 N N   . THR A 443 ? 0.4676 0.2305 0.3063 -0.1241 0.0074  -0.0352 443 THR A N   
2198 C CA  . THR A 443 ? 0.4924 0.2412 0.3195 -0.1465 0.0088  -0.0375 443 THR A CA  
2199 C C   . THR A 443 ? 0.4692 0.2575 0.3160 -0.1620 0.0073  -0.0391 443 THR A C   
2200 O O   . THR A 443 ? 0.4837 0.2679 0.3243 -0.1821 0.0085  -0.0407 443 THR A O   
2201 C CB  . THR A 443 ? 0.5427 0.2595 0.3489 -0.1518 0.0089  -0.0454 443 THR A CB  
2202 O OG1 . THR A 443 ? 0.5523 0.2932 0.3704 -0.1488 0.0054  -0.0525 443 THR A OG1 
2203 C CG2 . THR A 443 ? 0.5694 0.2447 0.3537 -0.1356 0.0112  -0.0435 443 THR A CG2 
2204 N N   . SER A 444 ? 0.4384 0.2640 0.3079 -0.1525 0.0049  -0.0384 444 SER A N   
2205 C CA  . SER A 444 ? 0.4121 0.2781 0.3020 -0.1608 0.0036  -0.0386 444 SER A CA  
2206 C C   . SER A 444 ? 0.3786 0.2687 0.2860 -0.1458 0.0036  -0.0329 444 SER A C   
2207 O O   . SER A 444 ? 0.3731 0.2520 0.2782 -0.1301 0.0037  -0.0302 444 SER A O   
2208 C CB  . SER A 444 ? 0.4320 0.3177 0.3288 -0.1657 0.0000  -0.0463 444 SER A CB  
2209 O OG  . SER A 444 ? 0.5048 0.3719 0.3862 -0.1832 0.0000  -0.0521 444 SER A OG  
2210 N N   . ARG A 445 ? 0.3446 0.2670 0.2682 -0.1510 0.0037  -0.0313 445 ARG A N   
2211 C CA  . ARG A 445 ? 0.3279 0.2697 0.2653 -0.1388 0.0042  -0.0264 445 ARG A CA  
2212 C C   . ARG A 445 ? 0.2994 0.2467 0.2441 -0.1215 0.0022  -0.0271 445 ARG A C   
2213 O O   . ARG A 445 ? 0.3020 0.2556 0.2496 -0.1189 -0.0001 -0.0317 445 ARG A O   
2214 C CB  . ARG A 445 ? 0.3350 0.3120 0.2884 -0.1456 0.0046  -0.0261 445 ARG A CB  
2215 C CG  . ARG A 445 ? 0.3832 0.3857 0.3480 -0.1460 0.0015  -0.0312 445 ARG A CG  
2216 C CD  . ARG A 445 ? 0.4225 0.4610 0.4030 -0.1495 0.0021  -0.0304 445 ARG A CD  
2217 N NE  . ARG A 445 ? 0.4361 0.4998 0.4270 -0.1468 -0.0012 -0.0344 445 ARG A NE  
2218 C CZ  . ARG A 445 ? 0.4552 0.5529 0.4598 -0.1474 -0.0013 -0.0344 445 ARG A CZ  
2219 N NH1 . ARG A 445 ? 0.4253 0.5442 0.4373 -0.1437 -0.0047 -0.0376 445 ARG A NH1 
2220 N NH2 . ARG A 445 ? 0.4615 0.5728 0.4715 -0.1510 0.0020  -0.0311 445 ARG A NH2 
2221 N N   . VAL A 446 ? 0.2913 0.2370 0.2384 -0.1102 0.0032  -0.0225 446 VAL A N   
2222 C CA  . VAL A 446 ? 0.2836 0.2378 0.2390 -0.0957 0.0018  -0.0227 446 VAL A CA  
2223 C C   . VAL A 446 ? 0.2662 0.2509 0.2380 -0.0953 0.0011  -0.0237 446 VAL A C   
2224 O O   . VAL A 446 ? 0.2748 0.2740 0.2524 -0.1012 0.0024  -0.0221 446 VAL A O   
2225 C CB  . VAL A 446 ? 0.2913 0.2368 0.2441 -0.0856 0.0027  -0.0179 446 VAL A CB  
2226 C CG1 . VAL A 446 ? 0.2804 0.2372 0.2425 -0.0728 0.0015  -0.0183 446 VAL A CG1 
2227 C CG2 . VAL A 446 ? 0.3057 0.2202 0.2406 -0.0843 0.0034  -0.0163 446 VAL A CG2 
2228 N N   . LEU A 447 ? 0.2459 0.2392 0.2235 -0.0881 -0.0006 -0.0263 447 LEU A N   
2229 C CA  . LEU A 447 ? 0.2347 0.2529 0.2251 -0.0851 -0.0012 -0.0270 447 LEU A CA  
2230 C C   . LEU A 447 ? 0.2378 0.2613 0.2350 -0.0740 -0.0003 -0.0245 447 LEU A C   
2231 O O   . LEU A 447 ? 0.2422 0.2810 0.2476 -0.0726 0.0008  -0.0232 447 LEU A O   
2232 C CB  . LEU A 447 ? 0.2393 0.2621 0.2294 -0.0848 -0.0035 -0.0312 447 LEU A CB  
2233 C CG  . LEU A 447 ? 0.2628 0.2852 0.2472 -0.0978 -0.0050 -0.0350 447 LEU A CG  
2234 C CD1 . LEU A 447 ? 0.2766 0.2998 0.2575 -0.0967 -0.0076 -0.0397 447 LEU A CD1 
2235 C CD2 . LEU A 447 ? 0.2564 0.3029 0.2500 -0.1054 -0.0048 -0.0344 447 LEU A CD2 
2236 N N   . SER A 448 ? 0.2290 0.2405 0.2226 -0.0664 -0.0004 -0.0241 448 SER A N   
2237 C CA  . SER A 448 ? 0.2359 0.2530 0.2357 -0.0579 0.0004  -0.0222 448 SER A CA  
2238 C C   . SER A 448 ? 0.2268 0.2311 0.2214 -0.0520 0.0004  -0.0210 448 SER A C   
2239 O O   . SER A 448 ? 0.2360 0.2267 0.2222 -0.0512 -0.0001 -0.0222 448 SER A O   
2240 C CB  . SER A 448 ? 0.2824 0.3092 0.2875 -0.0532 0.0001  -0.0237 448 SER A CB  
2241 O OG  . SER A 448 ? 0.3611 0.4028 0.3720 -0.0552 0.0001  -0.0240 448 SER A OG  
2242 N N   . LEU A 449 ? 0.2087 0.2182 0.2079 -0.0473 0.0011  -0.0191 449 LEU A N   
2243 C CA  . LEU A 449 ? 0.2143 0.2187 0.2112 -0.0407 0.0008  -0.0179 449 LEU A CA  
2244 C C   . LEU A 449 ? 0.2065 0.2219 0.2111 -0.0365 0.0014  -0.0185 449 LEU A C   
2245 O O   . LEU A 449 ? 0.2080 0.2322 0.2185 -0.0384 0.0023  -0.0186 449 LEU A O   
2246 C CB  . LEU A 449 ? 0.2148 0.2176 0.2096 -0.0404 0.0006  -0.0150 449 LEU A CB  
2247 C CG  . LEU A 449 ? 0.2326 0.2234 0.2184 -0.0454 0.0007  -0.0131 449 LEU A CG  
2248 C CD1 . LEU A 449 ? 0.2442 0.2338 0.2265 -0.0430 0.0004  -0.0096 449 LEU A CD1 
2249 C CD2 . LEU A 449 ? 0.2462 0.2193 0.2216 -0.0443 0.0004  -0.0137 449 LEU A CD2 
2250 N N   . THR A 450 ? 0.1880 0.2029 0.1920 -0.0305 0.0014  -0.0186 450 THR A N   
2251 C CA  . THR A 450 ? 0.1781 0.2039 0.1890 -0.0280 0.0025  -0.0187 450 THR A CA  
2252 C C   . THR A 450 ? 0.1825 0.2113 0.1932 -0.0220 0.0020  -0.0177 450 THR A C   
2253 O O   . THR A 450 ? 0.1952 0.2153 0.1992 -0.0173 0.0013  -0.0173 450 THR A O   
2254 C CB  . THR A 450 ? 0.1949 0.2234 0.2074 -0.0276 0.0038  -0.0200 450 THR A CB  
2255 O OG1 . THR A 450 ? 0.2079 0.2456 0.2263 -0.0272 0.0056  -0.0195 450 THR A OG1 
2256 C CG2 . THR A 450 ? 0.2069 0.2293 0.2137 -0.0233 0.0037  -0.0215 450 THR A CG2 
2257 N N   . MET A 451 ? 0.1806 0.2216 0.1978 -0.0222 0.0025  -0.0174 451 MET A N   
2258 C CA  . MET A 451 ? 0.1803 0.2298 0.1990 -0.0168 0.0017  -0.0164 451 MET A CA  
2259 C C   . MET A 451 ? 0.1854 0.2466 0.2094 -0.0142 0.0036  -0.0172 451 MET A C   
2260 O O   . MET A 451 ? 0.1843 0.2501 0.2127 -0.0192 0.0056  -0.0180 451 MET A O   
2261 C CB  . MET A 451 ? 0.1850 0.2432 0.2071 -0.0203 0.0003  -0.0158 451 MET A CB  
2262 C CG  . MET A 451 ? 0.2267 0.2984 0.2512 -0.0148 -0.0014 -0.0148 451 MET A CG  
2263 S SD  . MET A 451 ? 0.2572 0.3378 0.2830 -0.0194 -0.0038 -0.0146 451 MET A SD  
2264 C CE  . MET A 451 ? 0.2987 0.3611 0.3133 -0.0168 -0.0053 -0.0117 451 MET A CE  
2265 N N   . SER A 452 ? 0.1778 0.2441 0.2008 -0.0058 0.0033  -0.0167 452 SER A N   
2266 C CA  . SER A 452 ? 0.1834 0.2648 0.2119 -0.0026 0.0056  -0.0173 452 SER A CA  
2267 C C   . SER A 452 ? 0.1789 0.2792 0.2170 -0.0092 0.0059  -0.0173 452 SER A C   
2268 O O   . SER A 452 ? 0.1658 0.2687 0.2051 -0.0130 0.0036  -0.0170 452 SER A O   
2269 C CB  . SER A 452 ? 0.1938 0.2785 0.2190 0.0095  0.0051  -0.0166 452 SER A CB  
2270 O OG  . SER A 452 ? 0.2157 0.3092 0.2424 0.0128  0.0023  -0.0148 452 SER A OG  
2271 N N   . PRO A 453 ? 0.1924 0.3054 0.2361 -0.0119 0.0090  -0.0178 453 PRO A N   
2272 C CA  . PRO A 453 ? 0.2024 0.3304 0.2536 -0.0212 0.0098  -0.0182 453 PRO A CA  
2273 C C   . PRO A 453 ? 0.2117 0.3599 0.2685 -0.0191 0.0070  -0.0182 453 PRO A C   
2274 O O   . PRO A 453 ? 0.2336 0.3908 0.2944 -0.0280 0.0061  -0.0194 453 PRO A O   
2275 C CB  . PRO A 453 ? 0.2161 0.3515 0.2705 -0.0245 0.0144  -0.0181 453 PRO A CB  
2276 C CG  . PRO A 453 ? 0.2219 0.3538 0.2721 -0.0138 0.0155  -0.0178 453 PRO A CG  
2277 C CD  . PRO A 453 ? 0.2052 0.3174 0.2473 -0.0083 0.0124  -0.0180 453 PRO A CD  
2278 N N   . ASP A 454 ? 0.2034 0.3578 0.2590 -0.0069 0.0054  -0.0170 454 ASP A N   
2279 C CA  . ASP A 454 ? 0.2043 0.3798 0.2646 -0.0026 0.0022  -0.0163 454 ASP A CA  
2280 C C   . ASP A 454 ? 0.2056 0.3705 0.2596 -0.0007 -0.0022 -0.0152 454 ASP A C   
2281 O O   . ASP A 454 ? 0.2179 0.4002 0.2748 0.0015  -0.0054 -0.0145 454 ASP A O   
2282 C CB  . ASP A 454 ? 0.2149 0.4059 0.2770 0.0111  0.0029  -0.0152 454 ASP A CB  
2283 C CG  . ASP A 454 ? 0.2790 0.4486 0.3298 0.0247  0.0026  -0.0138 454 ASP A CG  
2284 O OD1 . ASP A 454 ? 0.2949 0.4377 0.3370 0.0219  0.0022  -0.0139 454 ASP A OD1 
2285 O OD2 . ASP A 454 ? 0.3058 0.4854 0.3560 0.0380  0.0031  -0.0130 454 ASP A OD2 
2286 N N   . GLY A 455 ? 0.1924 0.3312 0.2378 -0.0021 -0.0021 -0.0148 455 GLY A N   
2287 C CA  . GLY A 455 ? 0.1967 0.3238 0.2352 -0.0015 -0.0053 -0.0133 455 GLY A CA  
2288 C C   . GLY A 455 ? 0.2018 0.3184 0.2310 0.0115  -0.0070 -0.0102 455 GLY A C   
2289 O O   . GLY A 455 ? 0.2093 0.3146 0.2310 0.0123  -0.0092 -0.0081 455 GLY A O   
2290 N N   . ALA A 456 ? 0.1912 0.3094 0.2192 0.0221  -0.0055 -0.0097 456 ALA A N   
2291 C CA  . ALA A 456 ? 0.2030 0.3089 0.2200 0.0362  -0.0068 -0.0067 456 ALA A CA  
2292 C C   . ALA A 456 ? 0.2100 0.2827 0.2138 0.0363  -0.0054 -0.0065 456 ALA A C   
2293 O O   . ALA A 456 ? 0.2307 0.2861 0.2223 0.0434  -0.0066 -0.0035 456 ALA A O   
2294 C CB  . ALA A 456 ? 0.2132 0.3343 0.2330 0.0489  -0.0054 -0.0067 456 ALA A CB  
2295 N N   . THR A 457 ? 0.2033 0.2676 0.2085 0.0289  -0.0028 -0.0095 457 THR A N   
2296 C CA  . THR A 457 ? 0.2075 0.2445 0.2012 0.0280  -0.0015 -0.0104 457 THR A CA  
2297 C C   . THR A 457 ? 0.2081 0.2373 0.2035 0.0145  -0.0013 -0.0118 457 THR A C   
2298 O O   . THR A 457 ? 0.2002 0.2426 0.2055 0.0069  -0.0005 -0.0134 457 THR A O   
2299 C CB  . THR A 457 ? 0.2384 0.2736 0.2304 0.0342  0.0013  -0.0132 457 THR A CB  
2300 O OG1 . THR A 457 ? 0.2666 0.3131 0.2583 0.0484  0.0015  -0.0121 457 THR A OG1 
2301 C CG2 . THR A 457 ? 0.2485 0.2554 0.2269 0.0335  0.0023  -0.0152 457 THR A CG2 
2302 N N   . VAL A 458 ? 0.1999 0.2073 0.1848 0.0115  -0.0016 -0.0112 458 VAL A N   
2303 C CA  . VAL A 458 ? 0.1954 0.1964 0.1810 -0.0002 -0.0013 -0.0124 458 VAL A CA  
2304 C C   . VAL A 458 ? 0.2159 0.1997 0.1934 -0.0018 -0.0001 -0.0150 458 VAL A C   
2305 O O   . VAL A 458 ? 0.2454 0.2104 0.2103 0.0028  0.0000  -0.0145 458 VAL A O   
2306 C CB  . VAL A 458 ? 0.2137 0.2075 0.1942 -0.0041 -0.0026 -0.0093 458 VAL A CB  
2307 C CG1 . VAL A 458 ? 0.2336 0.2201 0.2133 -0.0152 -0.0017 -0.0105 458 VAL A CG1 
2308 C CG2 . VAL A 458 ? 0.2176 0.2304 0.2063 -0.0041 -0.0040 -0.0078 458 VAL A CG2 
2309 N N   . ALA A 459 ? 0.1990 0.1882 0.1819 -0.0080 0.0008  -0.0178 459 ALA A N   
2310 C CA  . ALA A 459 ? 0.2158 0.1916 0.1912 -0.0111 0.0012  -0.0209 459 ALA A CA  
2311 C C   . ALA A 459 ? 0.2280 0.1984 0.2019 -0.0219 0.0005  -0.0209 459 ALA A C   
2312 O O   . ALA A 459 ? 0.2162 0.1998 0.1993 -0.0270 0.0004  -0.0201 459 ALA A O   
2313 C CB  . ALA A 459 ? 0.2182 0.2052 0.1997 -0.0112 0.0023  -0.0235 459 ALA A CB  
2314 N N   . SER A 460 ? 0.2429 0.1943 0.2051 -0.0257 0.0003  -0.0218 460 SER A N   
2315 C CA  . SER A 460 ? 0.2536 0.2028 0.2148 -0.0373 0.0000  -0.0221 460 SER A CA  
2316 C C   . SER A 460 ? 0.2660 0.2109 0.2231 -0.0430 -0.0004 -0.0268 460 SER A C   
2317 O O   . SER A 460 ? 0.2872 0.2155 0.2330 -0.0402 -0.0002 -0.0295 460 SER A O   
2318 C CB  . SER A 460 ? 0.2798 0.2112 0.2300 -0.0402 0.0004  -0.0191 460 SER A CB  
2319 O OG  . SER A 460 ? 0.3048 0.2120 0.2396 -0.0356 0.0009  -0.0198 460 SER A OG  
2320 N N   . ALA A 461 ? 0.2507 0.2111 0.2162 -0.0500 -0.0011 -0.0281 461 ALA A N   
2321 C CA  . ALA A 461 ? 0.2614 0.2224 0.2239 -0.0563 -0.0022 -0.0326 461 ALA A CA  
2322 C C   . ALA A 461 ? 0.2755 0.2331 0.2346 -0.0690 -0.0025 -0.0328 461 ALA A C   
2323 O O   . ALA A 461 ? 0.2659 0.2341 0.2322 -0.0722 -0.0019 -0.0297 461 ALA A O   
2324 C CB  . ALA A 461 ? 0.2482 0.2315 0.2224 -0.0547 -0.0028 -0.0331 461 ALA A CB  
2325 N N   . ALA A 462 ? 0.2888 0.2317 0.2363 -0.0767 -0.0032 -0.0368 462 ALA A N   
2326 C CA  . ALA A 462 ? 0.3085 0.2472 0.2516 -0.0907 -0.0030 -0.0371 462 ALA A CA  
2327 C C   . ALA A 462 ? 0.3178 0.2613 0.2578 -0.1021 -0.0050 -0.0430 462 ALA A C   
2328 O O   . ALA A 462 ? 0.3228 0.2649 0.2593 -0.0984 -0.0065 -0.0474 462 ALA A O   
2329 C CB  . ALA A 462 ? 0.3257 0.2343 0.2531 -0.0917 -0.0011 -0.0349 462 ALA A CB  
2330 N N   . ALA A 463 ? 0.3199 0.2714 0.2614 -0.1163 -0.0050 -0.0433 463 ALA A N   
2331 C CA  . ALA A 463 ? 0.3314 0.2915 0.2709 -0.1298 -0.0073 -0.0491 463 ALA A CA  
2332 C C   . ALA A 463 ? 0.3623 0.2912 0.2815 -0.1367 -0.0075 -0.0547 463 ALA A C   
2333 O O   . ALA A 463 ? 0.3782 0.3122 0.2935 -0.1484 -0.0098 -0.0610 463 ALA A O   
2334 C CB  . ALA A 463 ? 0.3235 0.3009 0.2698 -0.1438 -0.0066 -0.0474 463 ALA A CB  
2335 N N   . ASP A 464 ? 0.3713 0.2680 0.2768 -0.1292 -0.0051 -0.0529 464 ASP A N   
2336 C CA  . ASP A 464 ? 0.3977 0.2607 0.2818 -0.1319 -0.0047 -0.0584 464 ASP A CA  
2337 C C   . ASP A 464 ? 0.3980 0.2620 0.2806 -0.1195 -0.0062 -0.0629 464 ASP A C   
2338 O O   . ASP A 464 ? 0.4195 0.2545 0.2841 -0.1164 -0.0053 -0.0671 464 ASP A O   
2339 C CB  . ASP A 464 ? 0.4311 0.2583 0.2993 -0.1270 -0.0013 -0.0542 464 ASP A CB  
2340 C CG  . ASP A 464 ? 0.4450 0.2737 0.3192 -0.1069 -0.0001 -0.0483 464 ASP A CG  
2341 O OD1 . ASP A 464 ? 0.4159 0.2686 0.3045 -0.0967 -0.0016 -0.0485 464 ASP A OD1 
2342 O OD2 . ASP A 464 ? 0.4684 0.2744 0.3323 -0.1016 0.0022  -0.0435 464 ASP A OD2 
2343 N N   . GLU A 465 ? 0.3657 0.2616 0.2659 -0.1113 -0.0081 -0.0617 465 GLU A N   
2344 C CA  . GLU A 465 ? 0.3623 0.2633 0.2623 -0.1004 -0.0091 -0.0650 465 GLU A CA  
2345 C C   . GLU A 465 ? 0.3737 0.2554 0.2666 -0.0842 -0.0064 -0.0632 465 GLU A C   
2346 O O   . GLU A 465 ? 0.3919 0.2634 0.2750 -0.0778 -0.0062 -0.0679 465 GLU A O   
2347 C CB  . GLU A 465 ? 0.3851 0.2819 0.2737 -0.1102 -0.0116 -0.0738 465 GLU A CB  
2348 C CG  . GLU A 465 ? 0.4487 0.3728 0.3470 -0.1248 -0.0150 -0.0756 465 GLU A CG  
2349 C CD  . GLU A 465 ? 0.5493 0.4776 0.4390 -0.1333 -0.0185 -0.0843 465 GLU A CD  
2350 O OE1 . GLU A 465 ? 0.5925 0.4916 0.4627 -0.1355 -0.0179 -0.0906 465 GLU A OE1 
2351 O OE2 . GLU A 465 ? 0.5565 0.5175 0.4582 -0.1365 -0.0219 -0.0849 465 GLU A OE2 
2352 N N   . THR A 466 ? 0.3623 0.2405 0.2598 -0.0775 -0.0043 -0.0566 466 THR A N   
2353 C CA  . THR A 466 ? 0.3650 0.2324 0.2591 -0.0611 -0.0021 -0.0541 466 THR A CA  
2354 C C   . THR A 466 ? 0.3546 0.2457 0.2670 -0.0532 -0.0017 -0.0474 466 THR A C   
2355 O O   . THR A 466 ? 0.3539 0.2588 0.2766 -0.0601 -0.0024 -0.0440 466 THR A O   
2356 C CB  . THR A 466 ? 0.3922 0.2258 0.2688 -0.0589 0.0001  -0.0526 466 THR A CB  
2357 O OG1 . THR A 466 ? 0.3851 0.2205 0.2668 -0.0640 0.0005  -0.0464 466 THR A OG1 
2358 C CG2 . THR A 466 ? 0.4150 0.2182 0.2698 -0.0675 0.0004  -0.0595 466 THR A CG2 
2359 N N   . LEU A 467 ? 0.3487 0.2431 0.2638 -0.0391 -0.0003 -0.0458 467 LEU A N   
2360 C CA  . LEU A 467 ? 0.3511 0.2634 0.2803 -0.0318 0.0003  -0.0402 467 LEU A CA  
2361 C C   . LEU A 467 ? 0.3522 0.2476 0.2725 -0.0210 0.0019  -0.0377 467 LEU A C   
2362 O O   . LEU A 467 ? 0.3731 0.2595 0.2852 -0.0114 0.0032  -0.0403 467 LEU A O   
2363 C CB  . LEU A 467 ? 0.3639 0.2965 0.3031 -0.0248 0.0008  -0.0406 467 LEU A CB  
2364 C CG  . LEU A 467 ? 0.4055 0.3617 0.3601 -0.0289 0.0000  -0.0381 467 LEU A CG  
2365 C CD1 . LEU A 467 ? 0.4106 0.3714 0.3651 -0.0396 -0.0020 -0.0409 467 LEU A CD1 
2366 C CD2 . LEU A 467 ? 0.4122 0.3840 0.3745 -0.0210 0.0016  -0.0372 467 LEU A CD2 
2367 N N   . ARG A 468 ? 0.3284 0.2193 0.2488 -0.0218 0.0018  -0.0329 468 ARG A N   
2368 C CA  . ARG A 468 ? 0.3369 0.2135 0.2484 -0.0101 0.0029  -0.0297 468 ARG A CA  
2369 C C   . ARG A 468 ? 0.3208 0.2215 0.2469 -0.0013 0.0027  -0.0256 468 ARG A C   
2370 O O   . ARG A 468 ? 0.3062 0.2236 0.2443 -0.0075 0.0017  -0.0230 468 ARG A O   
2371 C CB  . ARG A 468 ? 0.3707 0.2253 0.2702 -0.0158 0.0031  -0.0264 468 ARG A CB  
2372 C CG  . ARG A 468 ? 0.4404 0.2643 0.3206 -0.0233 0.0040  -0.0308 468 ARG A CG  
2373 C CD  . ARG A 468 ? 0.5225 0.3249 0.3908 -0.0322 0.0048  -0.0271 468 ARG A CD  
2374 N NE  . ARG A 468 ? 0.6415 0.4048 0.4852 -0.0328 0.0066  -0.0294 468 ARG A NE  
2375 C CZ  . ARG A 468 ? 0.6958 0.4434 0.5290 -0.0459 0.0069  -0.0356 468 ARG A CZ  
2376 N NH1 . ARG A 468 ? 0.7263 0.4345 0.5348 -0.0464 0.0089  -0.0378 468 ARG A NH1 
2377 N NH2 . ARG A 468 ? 0.6819 0.4529 0.5284 -0.0583 0.0049  -0.0398 468 ARG A NH2 
2378 N N   . LEU A 469 ? 0.3079 0.2112 0.2327 0.0128  0.0037  -0.0253 469 LEU A N   
2379 C CA  . LEU A 469 ? 0.2908 0.2199 0.2299 0.0198  0.0034  -0.0220 469 LEU A CA  
2380 C C   . LEU A 469 ? 0.2971 0.2201 0.2300 0.0300  0.0029  -0.0173 469 LEU A C   
2381 O O   . LEU A 469 ? 0.3242 0.2346 0.2461 0.0427  0.0040  -0.0173 469 LEU A O   
2382 C CB  . LEU A 469 ? 0.2899 0.2336 0.2345 0.0278  0.0051  -0.0247 469 LEU A CB  
2383 C CG  . LEU A 469 ? 0.3076 0.2698 0.2644 0.0196  0.0055  -0.0268 469 LEU A CG  
2384 C CD1 . LEU A 469 ? 0.3218 0.2727 0.2738 0.0082  0.0047  -0.0300 469 LEU A CD1 
2385 C CD2 . LEU A 469 ? 0.3046 0.2781 0.2635 0.0281  0.0079  -0.0290 469 LEU A CD2 
2386 N N   . TRP A 470 ? 0.2640 0.1959 0.2031 0.0255  0.0012  -0.0132 470 TRP A N   
2387 C CA  . TRP A 470 ? 0.2661 0.1925 0.1982 0.0341  0.0001  -0.0080 470 TRP A CA  
2388 C C   . TRP A 470 ? 0.2641 0.2199 0.2092 0.0424  -0.0013 -0.0059 470 TRP A C   
2389 O O   . TRP A 470 ? 0.2386 0.2156 0.1975 0.0343  -0.0024 -0.0060 470 TRP A O   
2390 C CB  . TRP A 470 ? 0.2697 0.1881 0.1989 0.0230  -0.0009 -0.0049 470 TRP A CB  
2391 C CG  . TRP A 470 ? 0.2829 0.1798 0.2032 0.0104  0.0004  -0.0072 470 TRP A CG  
2392 C CD1 . TRP A 470 ? 0.2865 0.1924 0.2158 -0.0026 0.0005  -0.0107 470 TRP A CD1 
2393 C CD2 . TRP A 470 ? 0.3041 0.1678 0.2043 0.0089  0.0016  -0.0059 470 TRP A CD2 
2394 N NE1 . TRP A 470 ? 0.3122 0.1964 0.2299 -0.0126 0.0014  -0.0121 470 TRP A NE1 
2395 C CE2 . TRP A 470 ? 0.3250 0.1818 0.2244 -0.0070 0.0023  -0.0092 470 TRP A CE2 
2396 C CE3 . TRP A 470 ? 0.3265 0.1654 0.2085 0.0195  0.0024  -0.0018 470 TRP A CE3 
2397 C CZ2 . TRP A 470 ? 0.3517 0.1780 0.2331 -0.0148 0.0038  -0.0091 470 TRP A CZ2 
2398 C CZ3 . TRP A 470 ? 0.3626 0.1668 0.2248 0.0129  0.0042  -0.0014 470 TRP A CZ3 
2399 C CH2 . TRP A 470 ? 0.3701 0.1682 0.2322 -0.0051 0.0050  -0.0054 470 TRP A CH2 
2400 N N   . ARG A 471 ? 0.2804 0.2382 0.2208 0.0584  -0.0012 -0.0041 471 ARG A N   
2401 C CA  . ARG A 471 ? 0.2855 0.2752 0.2387 0.0659  -0.0029 -0.0021 471 ARG A CA  
2402 C C   . ARG A 471 ? 0.3013 0.2899 0.2496 0.0679  -0.0058 0.0035  471 ARG A C   
2403 O O   . ARG A 471 ? 0.3166 0.3069 0.2583 0.0827  -0.0071 0.0074  471 ARG A O   
2404 C CB  . ARG A 471 ? 0.3110 0.3085 0.2627 0.0829  -0.0014 -0.0028 471 ARG A CB  
2405 C CG  . ARG A 471 ? 0.3622 0.3996 0.3308 0.0880  -0.0026 -0.0022 471 ARG A CG  
2406 C CD  . ARG A 471 ? 0.4176 0.4668 0.3877 0.1017  0.0002  -0.0043 471 ARG A CD  
2407 N NE  . ARG A 471 ? 0.4482 0.5393 0.4368 0.1025  -0.0003 -0.0044 471 ARG A NE  
2408 C CZ  . ARG A 471 ? 0.4677 0.5785 0.4707 0.0899  0.0012  -0.0074 471 ARG A CZ  
2409 N NH1 . ARG A 471 ? 0.4589 0.5527 0.4602 0.0778  0.0032  -0.0105 471 ARG A NH1 
2410 N NH2 . ARG A 471 ? 0.4692 0.6171 0.4877 0.0892  0.0009  -0.0074 471 ARG A NH2 
2411 N N   . CYS A 472 ? 0.2952 0.2803 0.2454 0.0538  -0.0067 0.0040  472 CYS A N   
2412 C CA  . CYS A 472 ? 0.3142 0.2956 0.2580 0.0533  -0.0089 0.0090  472 CYS A CA  
2413 C C   . CYS A 472 ? 0.3153 0.3291 0.2719 0.0536  -0.0121 0.0101  472 CYS A C   
2414 O O   . CYS A 472 ? 0.3293 0.3430 0.2798 0.0552  -0.0144 0.0145  472 CYS A O   
2415 C CB  . CYS A 472 ? 0.3225 0.2852 0.2609 0.0385  -0.0078 0.0090  472 CYS A CB  
2416 S SG  . CYS A 472 ? 0.3129 0.2930 0.2688 0.0218  -0.0070 0.0034  472 CYS A SG  
2417 N N   . PHE A 473 ? 0.2908 0.3316 0.2636 0.0510  -0.0122 0.0061  473 PHE A N   
2418 C CA  . PHE A 473 ? 0.2872 0.3595 0.2718 0.0498  -0.0152 0.0062  473 PHE A CA  
2419 C C   . PHE A 473 ? 0.3350 0.4332 0.3277 0.0617  -0.0159 0.0058  473 PHE A C   
2420 O O   . PHE A 473 ? 0.3390 0.4650 0.3463 0.0554  -0.0164 0.0028  473 PHE A O   
2421 C CB  . PHE A 473 ? 0.2517 0.3350 0.2480 0.0332  -0.0146 0.0019  473 PHE A CB  
2422 C CG  . PHE A 473 ? 0.2458 0.3097 0.2357 0.0229  -0.0139 0.0022  473 PHE A CG  
2423 C CD1 . PHE A 473 ? 0.2455 0.3044 0.2268 0.0235  -0.0160 0.0060  473 PHE A CD1 
2424 C CD2 . PHE A 473 ? 0.2497 0.3018 0.2417 0.0131  -0.0110 -0.0010 473 PHE A CD2 
2425 C CE1 . PHE A 473 ? 0.2567 0.3000 0.2323 0.0139  -0.0147 0.0064  473 PHE A CE1 
2426 C CE2 . PHE A 473 ? 0.2581 0.2961 0.2451 0.0043  -0.0102 -0.0006 473 PHE A CE2 
2427 C CZ  . PHE A 473 ? 0.2548 0.2887 0.2339 0.0044  -0.0117 0.0030  473 PHE A CZ  
2428 N N   . GLU A 474 ? 0.3736 0.4629 0.3564 0.0786  -0.0155 0.0089  474 GLU A N   
2429 C CA  . GLU A 474 ? 0.4101 0.5261 0.3997 0.0929  -0.0160 0.0091  474 GLU A CA  
2430 C C   . GLU A 474 ? 0.4761 0.5744 0.4495 0.1139  -0.0157 0.0135  474 GLU A C   
2431 O O   . GLU A 474 ? 0.5031 0.5636 0.4597 0.1155  -0.0138 0.0149  474 GLU A O   
2432 C CB  . GLU A 474 ? 0.4415 0.5722 0.4437 0.0887  -0.0125 0.0040  474 GLU A CB  
2433 C CG  . GLU A 474 ? 0.4975 0.6679 0.5187 0.0798  -0.0137 0.0015  474 GLU A CG  
2434 C CD  . GLU A 474 ? 0.5716 0.7790 0.6015 0.0924  -0.0154 0.0028  474 GLU A CD  
2435 O OE1 . GLU A 474 ? 0.6013 0.8399 0.6468 0.0847  -0.0145 -0.0003 474 GLU A OE1 
2436 O OE2 . GLU A 474 ? 0.5715 0.7775 0.5923 0.1101  -0.0175 0.0071  474 GLU A OE2 
2437 N N   . LEU A 475 ? 0.4941 0.6203 0.4724 0.1299  -0.0173 0.0155  475 LEU A N   
2438 C CA  . LEU A 475 ? 0.5404 0.6561 0.5046 0.1536  -0.0169 0.0196  475 LEU A CA  
2439 C C   . LEU A 475 ? 0.5565 0.6986 0.5309 0.1656  -0.0142 0.0167  475 LEU A C   
2440 O O   . LEU A 475 ? 0.5756 0.7021 0.5372 0.1847  -0.0118 0.0180  475 LEU A O   
2441 C CB  . LEU A 475 ? 0.5470 0.6758 0.5061 0.1655  -0.0219 0.0263  475 LEU A CB  
2442 C CG  . LEU A 475 ? 0.5913 0.6905 0.5355 0.1583  -0.0238 0.0306  475 LEU A CG  
2443 C CD1 . LEU A 475 ? 0.5926 0.7116 0.5335 0.1695  -0.0292 0.0370  475 LEU A CD1 
2444 C CD2 . LEU A 475 ? 0.6320 0.6794 0.5524 0.1642  -0.0200 0.0331  475 LEU A CD2 
2445 N N   . ASP A 476 ? 0.5450 0.7258 0.5412 0.1542  -0.0142 0.0126  476 ASP A N   
2446 C CA  . ASP A 476 ? 0.5442 0.7560 0.5528 0.1618  -0.0112 0.0097  476 ASP A CA  
2447 C C   . ASP A 476 ? 0.5353 0.7759 0.5447 0.1857  -0.0132 0.0136  476 ASP A C   
2448 O O   . ASP A 476 ? 0.5182 0.7853 0.5335 0.1877  -0.0184 0.0168  476 ASP A O   
2449 C CB  . ASP A 476 ? 0.5888 0.7731 0.5892 0.1637  -0.0053 0.0059  476 ASP A CB  
2450 C CG  . ASP A 476 ? 0.6819 0.8407 0.6814 0.1421  -0.0036 0.0023  476 ASP A CG  
2451 O OD1 . ASP A 476 ? 0.7122 0.8298 0.6949 0.1409  -0.0031 0.0028  476 ASP A OD1 
2452 O OD2 . ASP A 476 ? 0.7155 0.8956 0.7307 0.1263  -0.0027 -0.0009 476 ASP A OD2 
# 
